data_7HGB
# 
_entry.id   7HGB 
# 
_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   7HGB         pdb_00007hgb 10.2210/pdb7hgb/pdb 
WWPDB D_1001407437 ?            ?                   
# 
_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                        7HGB 
_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    2   ? ?    ? ? 
4 non-polymer syn '2-methoxy-N-[(4-methylphenyl)methyl]acetamide'    193.242   1   ? ?    ? ? 
5 water       nat water                                              18.015    252 ? ?    ? ? 
# 
_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-methoxy-N-[(4-methylphenyl)methyl]acetamide' A1A34 
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 
A1A34 non-polymer         . '2-methoxy-N-[(4-methylphenyl)methyl]acetamide' ?                 'C11 H15 N O2'   193.242 
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 ?  ?   ?   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        A1A34 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1A34 
_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 A1A34 1   103 101 A1A34 LIG B . 
K 3 EDO   1   101 101 EDO   EDO C . 
L 2 SO4   1   102 5   SO4   SO4 C . 
M 5 HOH   1   201 202 HOH   HOH A . 
M 5 HOH   2   202 307 HOH   HOH A . 
M 5 HOH   3   203 84  HOH   HOH A . 
M 5 HOH   4   204 335 HOH   HOH A . 
M 5 HOH   5   205 259 HOH   HOH A . 
M 5 HOH   6   206 139 HOH   HOH A . 
M 5 HOH   7   207 304 HOH   HOH A . 
M 5 HOH   8   208 95  HOH   HOH A . 
M 5 HOH   9   209 55  HOH   HOH A . 
M 5 HOH   10  210 66  HOH   HOH A . 
M 5 HOH   11  211 343 HOH   HOH A . 
M 5 HOH   12  212 289 HOH   HOH A . 
M 5 HOH   13  213 86  HOH   HOH A . 
M 5 HOH   14  214 87  HOH   HOH A . 
M 5 HOH   15  215 345 HOH   HOH A . 
M 5 HOH   16  216 28  HOH   HOH A . 
M 5 HOH   17  217 71  HOH   HOH A . 
M 5 HOH   18  218 37  HOH   HOH A . 
M 5 HOH   19  219 91  HOH   HOH A . 
M 5 HOH   20  220 26  HOH   HOH A . 
M 5 HOH   21  221 293 HOH   HOH A . 
M 5 HOH   22  222 34  HOH   HOH A . 
M 5 HOH   23  223 341 HOH   HOH A . 
M 5 HOH   24  224 290 HOH   HOH A . 
M 5 HOH   25  225 85  HOH   HOH A . 
M 5 HOH   26  226 8   HOH   HOH A . 
M 5 HOH   27  227 113 HOH   HOH A . 
M 5 HOH   28  228 111 HOH   HOH A . 
M 5 HOH   29  229 97  HOH   HOH A . 
M 5 HOH   30  230 208 HOH   HOH A . 
M 5 HOH   31  231 260 HOH   HOH A . 
M 5 HOH   32  232 179 HOH   HOH A . 
M 5 HOH   33  233 7   HOH   HOH A . 
M 5 HOH   34  234 1   HOH   HOH A . 
M 5 HOH   35  235 21  HOH   HOH A . 
M 5 HOH   36  236 41  HOH   HOH A . 
M 5 HOH   37  237 99  HOH   HOH A . 
M 5 HOH   38  238 267 HOH   HOH A . 
M 5 HOH   39  239 143 HOH   HOH A . 
M 5 HOH   40  240 32  HOH   HOH A . 
M 5 HOH   41  241 342 HOH   HOH A . 
M 5 HOH   42  242 274 HOH   HOH A . 
M 5 HOH   43  243 12  HOH   HOH A . 
M 5 HOH   44  244 350 HOH   HOH A . 
M 5 HOH   45  245 23  HOH   HOH A . 
M 5 HOH   46  246 78  HOH   HOH A . 
M 5 HOH   47  247 2   HOH   HOH A . 
M 5 HOH   48  248 292 HOH   HOH A . 
M 5 HOH   49  249 116 HOH   HOH A . 
M 5 HOH   50  250 167 HOH   HOH A . 
M 5 HOH   51  251 190 HOH   HOH A . 
M 5 HOH   52  252 77  HOH   HOH A . 
M 5 HOH   53  253 188 HOH   HOH A . 
M 5 HOH   54  254 218 HOH   HOH A . 
M 5 HOH   55  255 288 HOH   HOH A . 
M 5 HOH   56  256 334 HOH   HOH A . 
M 5 HOH   57  257 60  HOH   HOH A . 
M 5 HOH   58  258 27  HOH   HOH A . 
M 5 HOH   59  259 203 HOH   HOH A . 
M 5 HOH   60  260 109 HOH   HOH A . 
M 5 HOH   61  261 115 HOH   HOH A . 
M 5 HOH   62  262 300 HOH   HOH A . 
M 5 HOH   63  263 18  HOH   HOH A . 
M 5 HOH   64  264 47  HOH   HOH A . 
M 5 HOH   65  265 20  HOH   HOH A . 
M 5 HOH   66  266 42  HOH   HOH A . 
M 5 HOH   67  267 199 HOH   HOH A . 
M 5 HOH   68  268 14  HOH   HOH A . 
M 5 HOH   69  269 145 HOH   HOH A . 
M 5 HOH   70  270 38  HOH   HOH A . 
M 5 HOH   71  271 93  HOH   HOH A . 
M 5 HOH   72  272 64  HOH   HOH A . 
M 5 HOH   73  273 164 HOH   HOH A . 
M 5 HOH   74  274 58  HOH   HOH A . 
M 5 HOH   75  275 278 HOH   HOH A . 
M 5 HOH   76  276 211 HOH   HOH A . 
M 5 HOH   77  277 131 HOH   HOH A . 
M 5 HOH   78  278 73  HOH   HOH A . 
M 5 HOH   79  279 9   HOH   HOH A . 
M 5 HOH   80  280 222 HOH   HOH A . 
M 5 HOH   81  281 281 HOH   HOH A . 
M 5 HOH   82  282 94  HOH   HOH A . 
M 5 HOH   83  283 16  HOH   HOH A . 
M 5 HOH   84  284 19  HOH   HOH A . 
M 5 HOH   85  285 165 HOH   HOH A . 
M 5 HOH   86  286 301 HOH   HOH A . 
M 5 HOH   87  287 152 HOH   HOH A . 
M 5 HOH   88  288 31  HOH   HOH A . 
M 5 HOH   89  289 327 HOH   HOH A . 
M 5 HOH   90  290 63  HOH   HOH A . 
M 5 HOH   91  291 318 HOH   HOH A . 
M 5 HOH   92  292 22  HOH   HOH A . 
M 5 HOH   93  293 210 HOH   HOH A . 
M 5 HOH   94  294 270 HOH   HOH A . 
M 5 HOH   95  295 296 HOH   HOH A . 
M 5 HOH   96  296 83  HOH   HOH A . 
M 5 HOH   97  297 336 HOH   HOH A . 
M 5 HOH   98  298 205 HOH   HOH A . 
M 5 HOH   99  299 185 HOH   HOH A . 
M 5 HOH   100 300 108 HOH   HOH A . 
M 5 HOH   101 301 219 HOH   HOH A . 
M 5 HOH   102 302 283 HOH   HOH A . 
M 5 HOH   103 303 332 HOH   HOH A . 
M 5 HOH   104 304 35  HOH   HOH A . 
M 5 HOH   105 305 57  HOH   HOH A . 
M 5 HOH   106 306 338 HOH   HOH A . 
M 5 HOH   107 307 75  HOH   HOH A . 
M 5 HOH   108 308 156 HOH   HOH A . 
M 5 HOH   109 309 313 HOH   HOH A . 
M 5 HOH   110 310 125 HOH   HOH A . 
N 5 HOH   1   201 247 HOH   HOH B . 
N 5 HOH   2   202 331 HOH   HOH B . 
N 5 HOH   3   203 272 HOH   HOH B . 
N 5 HOH   4   204 89  HOH   HOH B . 
N 5 HOH   5   205 72  HOH   HOH B . 
N 5 HOH   6   206 69  HOH   HOH B . 
N 5 HOH   7   207 17  HOH   HOH B . 
N 5 HOH   8   208 333 HOH   HOH B . 
N 5 HOH   9   209 258 HOH   HOH B . 
N 5 HOH   10  210 137 HOH   HOH B . 
N 5 HOH   11  211 98  HOH   HOH B . 
N 5 HOH   12  212 172 HOH   HOH B . 
N 5 HOH   13  213 223 HOH   HOH B . 
N 5 HOH   14  214 150 HOH   HOH B . 
N 5 HOH   15  215 68  HOH   HOH B . 
N 5 HOH   16  216 249 HOH   HOH B . 
N 5 HOH   17  217 123 HOH   HOH B . 
N 5 HOH   18  218 346 HOH   HOH B . 
N 5 HOH   19  219 242 HOH   HOH B . 
N 5 HOH   20  220 215 HOH   HOH B . 
N 5 HOH   21  221 280 HOH   HOH B . 
N 5 HOH   22  222 10  HOH   HOH B . 
N 5 HOH   23  223 59  HOH   HOH B . 
N 5 HOH   24  224 168 HOH   HOH B . 
N 5 HOH   25  225 117 HOH   HOH B . 
N 5 HOH   26  226 177 HOH   HOH B . 
N 5 HOH   27  227 6   HOH   HOH B . 
N 5 HOH   28  228 5   HOH   HOH B . 
N 5 HOH   29  229 320 HOH   HOH B . 
N 5 HOH   30  230 329 HOH   HOH B . 
N 5 HOH   31  231 169 HOH   HOH B . 
N 5 HOH   32  232 25  HOH   HOH B . 
N 5 HOH   33  233 261 HOH   HOH B . 
N 5 HOH   34  234 24  HOH   HOH B . 
N 5 HOH   35  235 54  HOH   HOH B . 
N 5 HOH   36  236 214 HOH   HOH B . 
N 5 HOH   37  237 61  HOH   HOH B . 
N 5 HOH   38  238 175 HOH   HOH B . 
N 5 HOH   39  239 119 HOH   HOH B . 
N 5 HOH   40  240 315 HOH   HOH B . 
N 5 HOH   41  241 96  HOH   HOH B . 
N 5 HOH   42  242 13  HOH   HOH B . 
N 5 HOH   43  243 153 HOH   HOH B . 
N 5 HOH   44  244 319 HOH   HOH B . 
N 5 HOH   45  245 79  HOH   HOH B . 
N 5 HOH   46  246 76  HOH   HOH B . 
N 5 HOH   47  247 74  HOH   HOH B . 
N 5 HOH   48  248 224 HOH   HOH B . 
N 5 HOH   49  249 101 HOH   HOH B . 
N 5 HOH   50  250 170 HOH   HOH B . 
N 5 HOH   51  251 316 HOH   HOH B . 
N 5 HOH   52  252 197 HOH   HOH B . 
N 5 HOH   53  253 217 HOH   HOH B . 
N 5 HOH   54  254 46  HOH   HOH B . 
N 5 HOH   55  255 44  HOH   HOH B . 
N 5 HOH   56  256 347 HOH   HOH B . 
N 5 HOH   57  257 104 HOH   HOH B . 
N 5 HOH   58  258 36  HOH   HOH B . 
N 5 HOH   59  259 120 HOH   HOH B . 
N 5 HOH   60  260 279 HOH   HOH B . 
N 5 HOH   61  261 182 HOH   HOH B . 
N 5 HOH   62  262 303 HOH   HOH B . 
N 5 HOH   63  263 351 HOH   HOH B . 
N 5 HOH   64  264 157 HOH   HOH B . 
N 5 HOH   65  265 352 HOH   HOH B . 
N 5 HOH   66  266 322 HOH   HOH B . 
N 5 HOH   67  267 201 HOH   HOH B . 
N 5 HOH   68  268 291 HOH   HOH B . 
N 5 HOH   69  269 163 HOH   HOH B . 
N 5 HOH   70  270 160 HOH   HOH B . 
N 5 HOH   71  271 103 HOH   HOH B . 
N 5 HOH   72  272 314 HOH   HOH B . 
N 5 HOH   73  273 107 HOH   HOH B . 
N 5 HOH   74  274 312 HOH   HOH B . 
O 5 HOH   1   201 321 HOH   HOH C . 
O 5 HOH   2   202 337 HOH   HOH C . 
O 5 HOH   3   203 323 HOH   HOH C . 
O 5 HOH   4   204 254 HOH   HOH C . 
O 5 HOH   5   205 349 HOH   HOH C . 
O 5 HOH   6   206 317 HOH   HOH C . 
O 5 HOH   7   207 325 HOH   HOH C . 
O 5 HOH   8   208 118 HOH   HOH C . 
O 5 HOH   9   209 326 HOH   HOH C . 
O 5 HOH   10  210 294 HOH   HOH C . 
O 5 HOH   11  211 142 HOH   HOH C . 
O 5 HOH   12  212 134 HOH   HOH C . 
O 5 HOH   13  213 271 HOH   HOH C . 
O 5 HOH   14  214 302 HOH   HOH C . 
O 5 HOH   15  215 90  HOH   HOH C . 
O 5 HOH   16  216 269 HOH   HOH C . 
O 5 HOH   17  217 295 HOH   HOH C . 
O 5 HOH   18  218 161 HOH   HOH C . 
O 5 HOH   19  219 53  HOH   HOH C . 
O 5 HOH   20  220 184 HOH   HOH C . 
O 5 HOH   21  221 15  HOH   HOH C . 
O 5 HOH   22  222 49  HOH   HOH C . 
O 5 HOH   23  223 189 HOH   HOH C . 
O 5 HOH   24  224 339 HOH   HOH C . 
O 5 HOH   25  225 126 HOH   HOH C . 
O 5 HOH   26  226 309 HOH   HOH C . 
O 5 HOH   27  227 173 HOH   HOH C . 
O 5 HOH   28  228 122 HOH   HOH C . 
O 5 HOH   29  229 4   HOH   HOH C . 
O 5 HOH   30  230 284 HOH   HOH C . 
O 5 HOH   31  231 151 HOH   HOH C . 
O 5 HOH   32  232 45  HOH   HOH C . 
O 5 HOH   33  233 275 HOH   HOH C . 
O 5 HOH   34  234 102 HOH   HOH C . 
O 5 HOH   35  235 43  HOH   HOH C . 
O 5 HOH   36  236 82  HOH   HOH C . 
O 5 HOH   37  237 67  HOH   HOH C . 
O 5 HOH   38  238 299 HOH   HOH C . 
O 5 HOH   39  239 40  HOH   HOH C . 
O 5 HOH   40  240 48  HOH   HOH C . 
O 5 HOH   41  241 226 HOH   HOH C . 
O 5 HOH   42  242 135 HOH   HOH C . 
O 5 HOH   43  243 148 HOH   HOH C . 
O 5 HOH   44  244 348 HOH   HOH C . 
O 5 HOH   45  245 246 HOH   HOH C . 
O 5 HOH   46  246 62  HOH   HOH C . 
O 5 HOH   47  247 132 HOH   HOH C . 
O 5 HOH   48  248 209 HOH   HOH C . 
O 5 HOH   49  249 130 HOH   HOH C . 
O 5 HOH   50  250 287 HOH   HOH C . 
O 5 HOH   51  251 56  HOH   HOH C . 
O 5 HOH   52  252 198 HOH   HOH C . 
O 5 HOH   53  253 328 HOH   HOH C . 
O 5 HOH   54  254 305 HOH   HOH C . 
O 5 HOH   55  255 65  HOH   HOH C . 
O 5 HOH   56  256 298 HOH   HOH C . 
O 5 HOH   57  257 344 HOH   HOH C . 
O 5 HOH   58  258 149 HOH   HOH C . 
O 5 HOH   59  259 146 HOH   HOH C . 
O 5 HOH   60  260 241 HOH   HOH C . 
O 5 HOH   61  261 70  HOH   HOH C . 
O 5 HOH   62  262 171 HOH   HOH C . 
O 5 HOH   63  263 324 HOH   HOH C . 
O 5 HOH   64  264 330 HOH   HOH C . 
O 5 HOH   65  265 340 HOH   HOH C . 
O 5 HOH   66  266 92  HOH   HOH C . 
O 5 HOH   67  267 206 HOH   HOH C . 
O 5 HOH   68  268 310 HOH   HOH C . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 16 ? CE  ? A LYS 17 CE  
2  1 Y 1 A LYS 16 ? NZ  ? A LYS 17 NZ  
3  1 Y 1 A LYS 70 ? CE  ? A LYS 71 CE  
4  1 Y 1 A LYS 70 ? NZ  ? A LYS 71 NZ  
5  1 Y 1 A LYS 73 ? CD  ? A LYS 74 CD  
6  1 Y 1 A LYS 73 ? CE  ? A LYS 74 CE  
7  1 Y 1 A LYS 73 ? NZ  ? A LYS 74 NZ  
8  1 Y 1 A LYS 75 ? NZ  ? A LYS 76 NZ  
9  1 Y 1 B LYS 16 ? CE  ? B LYS 17 CE  
10 1 Y 1 B LYS 16 ? NZ  ? B LYS 17 NZ  
11 1 Y 1 B ILE 28 ? CG1 ? B ILE 29 CG1 
12 1 Y 1 B ILE 28 ? CG2 ? B ILE 29 CG2 
13 1 Y 1 B ILE 28 ? CD1 ? B ILE 29 CD1 
14 1 Y 1 B LYS 34 ? CG  ? B LYS 35 CG  
15 1 Y 1 B LYS 34 ? CD  ? B LYS 35 CD  
16 1 Y 1 B LYS 34 ? CE  ? B LYS 35 CE  
17 1 Y 1 B LYS 34 ? NZ  ? B LYS 35 NZ  
18 1 Y 1 B LYS 65 ? CD  ? B LYS 66 CD  
19 1 Y 1 B LYS 65 ? CE  ? B LYS 66 CE  
20 1 Y 1 B LYS 65 ? NZ  ? B LYS 66 NZ  
21 1 Y 1 B LYS 73 ? CE  ? B LYS 74 CE  
22 1 Y 1 B LYS 73 ? NZ  ? B LYS 74 NZ  
23 1 Y 1 B GLU 79 ? CD  ? B GLU 80 CD  
24 1 Y 1 B GLU 79 ? OE1 ? B GLU 80 OE1 
25 1 Y 1 B GLU 79 ? OE2 ? B GLU 80 OE2 
26 1 Y 1 B ILE 84 ? CG1 ? B ILE 85 CG1 
27 1 Y 1 B ILE 84 ? CG2 ? B ILE 85 CG2 
28 1 Y 1 B ILE 84 ? CD1 ? B ILE 85 CD1 
29 1 Y 1 C HIS 3  ? CG  ? C HIS 4  CG  
30 1 Y 1 C HIS 3  ? ND1 ? C HIS 4  ND1 
31 1 Y 1 C HIS 3  ? CD2 ? C HIS 4  CD2 
32 1 Y 1 C HIS 3  ? CE1 ? C HIS 4  CE1 
33 1 Y 1 C HIS 3  ? NE2 ? C HIS 4  NE2 
34 1 Y 1 C LYS 6  ? CG  ? C LYS 7  CG  
35 1 Y 1 C LYS 6  ? CD  ? C LYS 7  CD  
36 1 Y 1 C LYS 6  ? CE  ? C LYS 7  CE  
37 1 Y 1 C LYS 6  ? NZ  ? C LYS 7  NZ  
38 1 Y 1 C ASP 27 ? CG  ? C ASP 28 CG  
39 1 Y 1 C ASP 27 ? OD1 ? C ASP 28 OD1 
40 1 Y 1 C ASP 27 ? OD2 ? C ASP 28 OD2 
41 1 Y 1 C ILE 28 ? CG1 ? C ILE 29 CG1 
42 1 Y 1 C ILE 28 ? CG2 ? C ILE 29 CG2 
43 1 Y 1 C ILE 28 ? CD1 ? C ILE 29 CD1 
44 1 Y 1 C LYS 34 ? CG  ? C LYS 35 CG  
45 1 Y 1 C LYS 34 ? CD  ? C LYS 35 CD  
46 1 Y 1 C LYS 34 ? CE  ? C LYS 35 CE  
47 1 Y 1 C LYS 34 ? NZ  ? C LYS 35 NZ  
48 1 Y 1 C LYS 56 ? CG  ? C LYS 57 CG  
49 1 Y 1 C LYS 56 ? CD  ? C LYS 57 CD  
50 1 Y 1 C LYS 56 ? CE  ? C LYS 57 CE  
51 1 Y 1 C LYS 56 ? NZ  ? C LYS 57 NZ  
52 1 Y 1 C LYS 63 ? CG  ? C LYS 64 CG  
53 1 Y 1 C LYS 63 ? CD  ? C LYS 64 CD  
54 1 Y 1 C LYS 63 ? CE  ? C LYS 64 CE  
55 1 Y 1 C LYS 63 ? NZ  ? C LYS 64 NZ  
56 1 Y 1 C LYS 70 ? NZ  ? C LYS 71 NZ  
57 1 Y 1 C LYS 73 ? CE  ? C LYS 74 CE  
58 1 Y 1 C LYS 73 ? NZ  ? C LYS 74 NZ  
59 1 Y 1 C LYS 75 ? CE  ? C LYS 76 CE  
60 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           7HGB 
_cell.length_a           41.660 
_cell.length_b           42.270 
_cell.length_c           159.780 
_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                         7HGB 
_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          7HGB 
_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                     7HGB 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             42.27 
_reflns.d_resolution_high            1.52 
_reflns.number_obs                   44458 
_reflns.percent_possible_obs         99.9 
_reflns.pdbx_Rmerge_I_obs            0.062 
_reflns.pdbx_netI_over_sigmaI        12.3 
_reflns.pdbx_redundancy              6.1 
_reflns.pdbx_Rrim_I_all              0.068 
_reflns.pdbx_Rpim_I_all              0.027 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_number_measured_all     269046 
_reflns.pdbx_chi_squared             0.95 
_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                  1.52 
_reflns_shell.d_res_low                   1.56 
_reflns_shell.number_measured_all         16231 
_reflns_shell.number_unique_obs           3224 
_reflns_shell.Rmerge_I_obs                1.378 
_reflns_shell.pdbx_chi_squared            0.72 
_reflns_shell.pdbx_redundancy             5.0 
_reflns_shell.percent_possible_obs        99.7 
_reflns_shell.pdbx_netI_over_sigmaI_obs   1.0 
_reflns_shell.pdbx_Rrim_I_all             1.541 
_reflns_shell.pdbx_Rpim_I_all             0.676 
_reflns_shell.pdbx_CC_half                0.390 
_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                                 7HGB 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     42028 
_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                             40.90 
_refine.ls_d_res_high                            1.52 
_refine.ls_percent_reflns_obs                    99.75 
_refine.ls_R_factor_obs                          0.21061 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.20865 
_refine.ls_R_factor_R_free                       0.24533 
_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                  2356 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.964 
_refine.correlation_coeff_Fo_to_Fc_free          0.955 
_refine.B_iso_mean                               34.882 
_refine.aniso_B[1][1]                            0.29 
_refine.aniso_B[2][2]                            -0.29 
_refine.aniso_B[3][3]                            0.01 
_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                       0.089 
_refine.pdbx_overall_ESU_R_Free                  0.092 
_refine.overall_SU_ML                            0.076 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             2.148 
_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        2135 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         52 
_refine_hist.number_atoms_solvent             252 
_refine_hist.number_atoms_total               2439 
_refine_hist.d_res_high                       1.52 
_refine_hist.d_res_low                        40.90 
# 
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  ? 2289 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.926  1.832  ? 3113 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       8.065  5.000  ? 266  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       4.234  5.000  ? 6    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       12.252 10.000 ? 297  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.139  0.200  ? 285  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.011  0.020  ? 1906 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  3.162  3.254  ? 1074 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 4.447  5.822  ? 1336 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  4.151  3.532  ? 1215 '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       8.062  45.82  ? 3413 '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                       1.520 
_refine_ls_shell.d_res_low                        1.559 
_refine_ls_shell.number_reflns_R_work             3038 
_refine_ls_shell.R_factor_R_work                  0.336 
_refine_ls_shell.percent_reflns_obs               99.60 
_refine_ls_shell.R_factor_R_free                  0.375 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             177 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HGB 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of HRP-2 PWWP domain in complex with Z33297786' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HGB 
_struct_keywords.pdbx_keywords   'GENE REGULATION' 
_struct_keywords.text            
'Inhibitor, Fragment screening, Epigenetic reader, methyllysine, PWWP, Diamond Light Source, I04-1, PanDDA, XChem, GENE REGULATION' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 2 ? 
E N N 2 ? 
F N N 3 ? 
G N N 2 ? 
H N N 2 ? 
I N N 2 ? 
J N N 4 ? 
K N N 3 ? 
L N N 2 ? 
M N N 5 ? 
N N N 5 ? 
O N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    HDGR2_HUMAN 
_struct_ref.pdbx_db_accession          Q7Z4V5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKCKDKYGKPNKRKGFNEG
LWEIQNNPHASYS
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HGB A 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 7HGB B 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
3 1 7HGB 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 7HGB GLY A 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  1 
1 7HGB SER A 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 2 
2 7HGB GLY B 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  3 
2 7HGB SER B 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 4 
3 7HGB GLY C 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  5 
3 7HGB 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                   7HGB 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   B HOH 221 ? ? O B HOH 266 ? ? 1.53 
2  1 O2  C SO4 102 ? ? O C HOH 201 ? ? 1.96 
3  1 O4  A SO4 104 ? ? O A HOH 201 ? ? 2.01 
4  1 O   A HOH 223 ? ? O A HOH 292 ? ? 2.05 
5  1 O   A HOH 253 ? ? O A HOH 298 ? ? 2.08 
6  1 OH  C TYR 40  ? ? O C HOH 202 ? ? 2.09 
7  1 OD1 C ASP 9   ? ? O C HOH 203 ? ? 2.09 
8  1 O2  A SO4 104 ? ? O A HOH 202 ? ? 2.12 
9  1 O   A HOH 204 ? ? O A HOH 294 ? ? 2.14 
10 1 O   C HOH 259 ? ? O C HOH 263 ? ? 2.14 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 258 ? ? 1_555 O C HOH 265 ? ? 4_445 2.12 
2 1 O A HOH 248 ? ? 1_555 O A HOH 280 ? ? 4_545 2.15 
# 
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 CB A LEU 81 ? ? CG A LEU 81 ? ? CD1 A LEU 81 ? ? 100.00 111.00 -11.00 1.70 N 
2 1 NE C ARG 74 ? ? CZ C ARG 74 ? ? NH1 C ARG 74 ? ? 117.25 120.30 -3.05  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 ? ? -153.00 66.87  
2 1 ASN B 38 ? ? 78.75   -3.93  
3 1 ASN B 87 ? ? -158.64 58.72  
4 1 ALA C 4  ? ? -170.36 149.20 
5 1 ASN C 87 ? ? -141.63 51.34  
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   VAL 
_pdbx_validate_peptide_omega.auth_asym_id_1   A 
_pdbx_validate_peptide_omega.auth_seq_id_1    11 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   PHE 
_pdbx_validate_peptide_omega.auth_asym_id_2   A 
_pdbx_validate_peptide_omega.auth_seq_id_2    12 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            146.20 
# 
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 ALA 29 ? C ALA 30 
11 1 Y 1 C ASP 30 ? C ASP 31 
12 1 Y 1 C GLY 31 ? C GLY 32 
13 1 Y 1 C ALA 32 ? C ALA 33 
14 1 Y 1 C VAL 33 ? C VAL 34 
15 1 Y 1 C 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 
A1A34 C4   C Y N 1   
A1A34 C5   C Y N 2   
A1A34 C6   C Y N 3   
A1A34 C7   C Y N 4   
A1A34 C8   C N N 5   
A1A34 C10  C Y N 6   
A1A34 O1   O N N 7   
A1A34 C2   C N N 8   
A1A34 C1   C N N 9   
A1A34 O    O N N 10  
A1A34 C    C N N 11  
A1A34 N    N N N 12  
A1A34 C3   C N N 13  
A1A34 C9   C Y N 14  
A1A34 H8   H N N 15  
A1A34 H9   H N N 16  
A1A34 H11  H N N 17  
A1A34 H10  H N N 18  
A1A34 H12  H N N 19  
A1A34 H14  H N N 20  
A1A34 H3   H N N 21  
A1A34 H4   H N N 22  
A1A34 H2   H N N 23  
A1A34 H    H N N 24  
A1A34 H1   H N N 25  
A1A34 H5   H N N 26  
A1A34 H7   H N N 27  
A1A34 H6   H N N 28  
A1A34 H13  H N N 29  
ALA   N    N N N 30  
ALA   CA   C N S 31  
ALA   C    C N N 32  
ALA   O    O N N 33  
ALA   CB   C N N 34  
ALA   OXT  O N N 35  
ALA   H    H N N 36  
ALA   H2   H N N 37  
ALA   HA   H N N 38  
ALA   HB1  H N N 39  
ALA   HB2  H N N 40  
ALA   HB3  H N N 41  
ALA   HXT  H N N 42  
ARG   N    N N N 43  
ARG   CA   C N S 44  
ARG   C    C N N 45  
ARG   O    O N N 46  
ARG   CB   C N N 47  
ARG   CG   C N N 48  
ARG   CD   C N N 49  
ARG   NE   N N N 50  
ARG   CZ   C N N 51  
ARG   NH1  N N N 52  
ARG   NH2  N N N 53  
ARG   OXT  O N N 54  
ARG   H    H N N 55  
ARG   H2   H N N 56  
ARG   HA   H N N 57  
ARG   HB2  H N N 58  
ARG   HB3  H N N 59  
ARG   HG2  H N N 60  
ARG   HG3  H N N 61  
ARG   HD2  H N N 62  
ARG   HD3  H N N 63  
ARG   HE   H N N 64  
ARG   HH11 H N N 65  
ARG   HH12 H N N 66  
ARG   HH21 H N N 67  
ARG   HH22 H N N 68  
ARG   HXT  H N N 69  
ASN   N    N N N 70  
ASN   CA   C N S 71  
ASN   C    C N N 72  
ASN   O    O N N 73  
ASN   CB   C N N 74  
ASN   CG   C N N 75  
ASN   OD1  O N N 76  
ASN   ND2  N N N 77  
ASN   OXT  O N N 78  
ASN   H    H N N 79  
ASN   H2   H N N 80  
ASN   HA   H N N 81  
ASN   HB2  H N N 82  
ASN   HB3  H N N 83  
ASN   HD21 H N N 84  
ASN   HD22 H N N 85  
ASN   HXT  H N N 86  
ASP   N    N N N 87  
ASP   CA   C N S 88  
ASP   C    C N N 89  
ASP   O    O N N 90  
ASP   CB   C N N 91  
ASP   CG   C N N 92  
ASP   OD1  O N N 93  
ASP   OD2  O N N 94  
ASP   OXT  O N N 95  
ASP   H    H N N 96  
ASP   H2   H N N 97  
ASP   HA   H N N 98  
ASP   HB2  H N N 99  
ASP   HB3  H N N 100 
ASP   HD2  H N N 101 
ASP   HXT  H N N 102 
CYS   N    N N N 103 
CYS   CA   C N R 104 
CYS   C    C N N 105 
CYS   O    O N N 106 
CYS   CB   C N N 107 
CYS   SG   S N N 108 
CYS   OXT  O N N 109 
CYS   H    H N N 110 
CYS   H2   H N N 111 
CYS   HA   H N N 112 
CYS   HB2  H N N 113 
CYS   HB3  H N N 114 
CYS   HG   H N N 115 
CYS   HXT  H N N 116 
EDO   C1   C N N 117 
EDO   O1   O N N 118 
EDO   C2   C N N 119 
EDO   O2   O N N 120 
EDO   H11  H N N 121 
EDO   H12  H N N 122 
EDO   HO1  H N N 123 
EDO   H21  H N N 124 
EDO   H22  H N N 125 
EDO   HO2  H N N 126 
GLN   N    N N N 127 
GLN   CA   C N S 128 
GLN   C    C N N 129 
GLN   O    O N N 130 
GLN   CB   C N N 131 
GLN   CG   C N N 132 
GLN   CD   C N N 133 
GLN   OE1  O N N 134 
GLN   NE2  N N N 135 
GLN   OXT  O N N 136 
GLN   H    H N N 137 
GLN   H2   H N N 138 
GLN   HA   H N N 139 
GLN   HB2  H N N 140 
GLN   HB3  H N N 141 
GLN   HG2  H N N 142 
GLN   HG3  H N N 143 
GLN   HE21 H N N 144 
GLN   HE22 H N N 145 
GLN   HXT  H N N 146 
GLU   N    N N N 147 
GLU   CA   C N S 148 
GLU   C    C N N 149 
GLU   O    O N N 150 
GLU   CB   C N N 151 
GLU   CG   C N N 152 
GLU   CD   C N N 153 
GLU   OE1  O N N 154 
GLU   OE2  O N N 155 
GLU   OXT  O N N 156 
GLU   H    H N N 157 
GLU   H2   H N N 158 
GLU   HA   H N N 159 
GLU   HB2  H N N 160 
GLU   HB3  H N N 161 
GLU   HG2  H N N 162 
GLU   HG3  H N N 163 
GLU   HE2  H N N 164 
GLU   HXT  H N N 165 
GLY   N    N N N 166 
GLY   CA   C N N 167 
GLY   C    C N N 168 
GLY   O    O N N 169 
GLY   OXT  O N N 170 
GLY   H    H N N 171 
GLY   H2   H N N 172 
GLY   HA2  H N N 173 
GLY   HA3  H N N 174 
GLY   HXT  H N N 175 
HIS   N    N N N 176 
HIS   CA   C N S 177 
HIS   C    C N N 178 
HIS   O    O N N 179 
HIS   CB   C N N 180 
HIS   CG   C Y N 181 
HIS   ND1  N Y N 182 
HIS   CD2  C Y N 183 
HIS   CE1  C Y N 184 
HIS   NE2  N Y N 185 
HIS   OXT  O N N 186 
HIS   H    H N N 187 
HIS   H2   H N N 188 
HIS   HA   H N N 189 
HIS   HB2  H N N 190 
HIS   HB3  H N N 191 
HIS   HD1  H N N 192 
HIS   HD2  H N N 193 
HIS   HE1  H N N 194 
HIS   HE2  H N N 195 
HIS   HXT  H N N 196 
HOH   O    O N N 197 
HOH   H1   H N N 198 
HOH   H2   H N N 199 
ILE   N    N N N 200 
ILE   CA   C N S 201 
ILE   C    C N N 202 
ILE   O    O N N 203 
ILE   CB   C N S 204 
ILE   CG1  C N N 205 
ILE   CG2  C N N 206 
ILE   CD1  C N N 207 
ILE   OXT  O N N 208 
ILE   H    H N N 209 
ILE   H2   H N N 210 
ILE   HA   H N N 211 
ILE   HB   H N N 212 
ILE   HG12 H N N 213 
ILE   HG13 H N N 214 
ILE   HG21 H N N 215 
ILE   HG22 H N N 216 
ILE   HG23 H N N 217 
ILE   HD11 H N N 218 
ILE   HD12 H N N 219 
ILE   HD13 H N N 220 
ILE   HXT  H N N 221 
LEU   N    N N N 222 
LEU   CA   C N S 223 
LEU   C    C N N 224 
LEU   O    O N N 225 
LEU   CB   C N N 226 
LEU   CG   C N N 227 
LEU   CD1  C N N 228 
LEU   CD2  C N N 229 
LEU   OXT  O N N 230 
LEU   H    H N N 231 
LEU   H2   H N N 232 
LEU   HA   H N N 233 
LEU   HB2  H N N 234 
LEU   HB3  H N N 235 
LEU   HG   H N N 236 
LEU   HD11 H N N 237 
LEU   HD12 H N N 238 
LEU   HD13 H N N 239 
LEU   HD21 H N N 240 
LEU   HD22 H N N 241 
LEU   HD23 H N N 242 
LEU   HXT  H N N 243 
LYS   N    N N N 244 
LYS   CA   C N S 245 
LYS   C    C N N 246 
LYS   O    O N N 247 
LYS   CB   C N N 248 
LYS   CG   C N N 249 
LYS   CD   C N N 250 
LYS   CE   C N N 251 
LYS   NZ   N N N 252 
LYS   OXT  O N N 253 
LYS   H    H N N 254 
LYS   H2   H N N 255 
LYS   HA   H N N 256 
LYS   HB2  H N N 257 
LYS   HB3  H N N 258 
LYS   HG2  H N N 259 
LYS   HG3  H N N 260 
LYS   HD2  H N N 261 
LYS   HD3  H N N 262 
LYS   HE2  H N N 263 
LYS   HE3  H N N 264 
LYS   HZ1  H N N 265 
LYS   HZ2  H N N 266 
LYS   HZ3  H N N 267 
LYS   HXT  H N N 268 
MET   N    N N N 269 
MET   CA   C N S 270 
MET   C    C N N 271 
MET   O    O N N 272 
MET   CB   C N N 273 
MET   CG   C N N 274 
MET   SD   S N N 275 
MET   CE   C N N 276 
MET   OXT  O N N 277 
MET   H    H N N 278 
MET   H2   H N N 279 
MET   HA   H N N 280 
MET   HB2  H N N 281 
MET   HB3  H N N 282 
MET   HG2  H N N 283 
MET   HG3  H N N 284 
MET   HE1  H N N 285 
MET   HE2  H N N 286 
MET   HE3  H N N 287 
MET   HXT  H N N 288 
PHE   N    N N N 289 
PHE   CA   C N S 290 
PHE   C    C N N 291 
PHE   O    O N N 292 
PHE   CB   C N N 293 
PHE   CG   C Y N 294 
PHE   CD1  C Y N 295 
PHE   CD2  C Y N 296 
PHE   CE1  C Y N 297 
PHE   CE2  C Y N 298 
PHE   CZ   C Y N 299 
PHE   OXT  O N N 300 
PHE   H    H N N 301 
PHE   H2   H N N 302 
PHE   HA   H N N 303 
PHE   HB2  H N N 304 
PHE   HB3  H N N 305 
PHE   HD1  H N N 306 
PHE   HD2  H N N 307 
PHE   HE1  H N N 308 
PHE   HE2  H N N 309 
PHE   HZ   H N N 310 
PHE   HXT  H N N 311 
PRO   N    N N N 312 
PRO   CA   C N S 313 
PRO   C    C N N 314 
PRO   O    O N N 315 
PRO   CB   C N N 316 
PRO   CG   C N N 317 
PRO   CD   C N N 318 
PRO   OXT  O N N 319 
PRO   H    H N N 320 
PRO   HA   H N N 321 
PRO   HB2  H N N 322 
PRO   HB3  H N N 323 
PRO   HG2  H N N 324 
PRO   HG3  H N N 325 
PRO   HD2  H N N 326 
PRO   HD3  H N N 327 
PRO   HXT  H N N 328 
SER   N    N N N 329 
SER   CA   C N S 330 
SER   C    C N N 331 
SER   O    O N N 332 
SER   CB   C N N 333 
SER   OG   O N N 334 
SER   OXT  O N N 335 
SER   H    H N N 336 
SER   H2   H N N 337 
SER   HA   H N N 338 
SER   HB2  H N N 339 
SER   HB3  H N N 340 
SER   HG   H N N 341 
SER   HXT  H N N 342 
SO4   S    S N N 343 
SO4   O1   O N N 344 
SO4   O2   O N N 345 
SO4   O3   O N N 346 
SO4   O4   O N N 347 
THR   N    N N N 348 
THR   CA   C N S 349 
THR   C    C N N 350 
THR   O    O N N 351 
THR   CB   C N R 352 
THR   OG1  O N N 353 
THR   CG2  C N N 354 
THR   OXT  O N N 355 
THR   H    H N N 356 
THR   H2   H N N 357 
THR   HA   H N N 358 
THR   HB   H N N 359 
THR   HG1  H N N 360 
THR   HG21 H N N 361 
THR   HG22 H N N 362 
THR   HG23 H N N 363 
THR   HXT  H N N 364 
TRP   N    N N N 365 
TRP   CA   C N S 366 
TRP   C    C N N 367 
TRP   O    O N N 368 
TRP   CB   C N N 369 
TRP   CG   C Y N 370 
TRP   CD1  C Y N 371 
TRP   CD2  C Y N 372 
TRP   NE1  N Y N 373 
TRP   CE2  C Y N 374 
TRP   CE3  C Y N 375 
TRP   CZ2  C Y N 376 
TRP   CZ3  C Y N 377 
TRP   CH2  C Y N 378 
TRP   OXT  O N N 379 
TRP   H    H N N 380 
TRP   H2   H N N 381 
TRP   HA   H N N 382 
TRP   HB2  H N N 383 
TRP   HB3  H N N 384 
TRP   HD1  H N N 385 
TRP   HE1  H N N 386 
TRP   HE3  H N N 387 
TRP   HZ2  H N N 388 
TRP   HZ3  H N N 389 
TRP   HH2  H N N 390 
TRP   HXT  H N N 391 
TYR   N    N N N 392 
TYR   CA   C N S 393 
TYR   C    C N N 394 
TYR   O    O N N 395 
TYR   CB   C N N 396 
TYR   CG   C Y N 397 
TYR   CD1  C Y N 398 
TYR   CD2  C Y N 399 
TYR   CE1  C Y N 400 
TYR   CE2  C Y N 401 
TYR   CZ   C Y N 402 
TYR   OH   O N N 403 
TYR   OXT  O N N 404 
TYR   H    H N N 405 
TYR   H2   H N N 406 
TYR   HA   H N N 407 
TYR   HB2  H N N 408 
TYR   HB3  H N N 409 
TYR   HD1  H N N 410 
TYR   HD2  H N N 411 
TYR   HE1  H N N 412 
TYR   HE2  H N N 413 
TYR   HH   H N N 414 
TYR   HXT  H N N 415 
VAL   N    N N N 416 
VAL   CA   C N S 417 
VAL   C    C N N 418 
VAL   O    O N N 419 
VAL   CB   C N N 420 
VAL   CG1  C N N 421 
VAL   CG2  C N N 422 
VAL   OXT  O N N 423 
VAL   H    H N N 424 
VAL   H2   H N N 425 
VAL   HA   H N N 426 
VAL   HB   H N N 427 
VAL   HG11 H N N 428 
VAL   HG12 H N N 429 
VAL   HG13 H N N 430 
VAL   HG21 H N N 431 
VAL   HG22 H N N 432 
VAL   HG23 H N N 433 
VAL   HXT  H N N 434 
# 
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 
A1A34 C   O    sing N N 1   
A1A34 O   C1   sing N N 2   
A1A34 C1  C2   sing N N 3   
A1A34 C2  O1   doub N N 4   
A1A34 N   C2   sing N N 5   
A1A34 C3  N    sing N N 6   
A1A34 C4  C3   sing N N 7   
A1A34 C4  C5   sing Y N 8   
A1A34 C5  C6   doub Y N 9   
A1A34 C6  C7   sing Y N 10  
A1A34 C8  C7   sing N N 11  
A1A34 C7  C9   doub Y N 12  
A1A34 C9  C10  sing Y N 13  
A1A34 C10 C4   doub Y N 14  
A1A34 C5  H8   sing N N 15  
A1A34 C6  H9   sing N N 16  
A1A34 C8  H11  sing N N 17  
A1A34 C8  H10  sing N N 18  
A1A34 C8  H12  sing N N 19  
A1A34 C10 H14  sing N N 20  
A1A34 C1  H3   sing N N 21  
A1A34 C1  H4   sing N N 22  
A1A34 C   H2   sing N N 23  
A1A34 C   H    sing N N 24  
A1A34 C   H1   sing N N 25  
A1A34 N   H5   sing N N 26  
A1A34 C3  H7   sing N N 27  
A1A34 C3  H6   sing N N 28  
A1A34 C9  H13  sing N N 29  
ALA   N   CA   sing N N 30  
ALA   N   H    sing N N 31  
ALA   N   H2   sing N N 32  
ALA   CA  C    sing N N 33  
ALA   CA  CB   sing N N 34  
ALA   CA  HA   sing N N 35  
ALA   C   O    doub N N 36  
ALA   C   OXT  sing N N 37  
ALA   CB  HB1  sing N N 38  
ALA   CB  HB2  sing N N 39  
ALA   CB  HB3  sing N N 40  
ALA   OXT HXT  sing N N 41  
ARG   N   CA   sing N N 42  
ARG   N   H    sing N N 43  
ARG   N   H2   sing N N 44  
ARG   CA  C    sing N N 45  
ARG   CA  CB   sing N N 46  
ARG   CA  HA   sing N N 47  
ARG   C   O    doub N N 48  
ARG   C   OXT  sing N N 49  
ARG   CB  CG   sing N N 50  
ARG   CB  HB2  sing N N 51  
ARG   CB  HB3  sing N N 52  
ARG   CG  CD   sing N N 53  
ARG   CG  HG2  sing N N 54  
ARG   CG  HG3  sing N N 55  
ARG   CD  NE   sing N N 56  
ARG   CD  HD2  sing N N 57  
ARG   CD  HD3  sing N N 58  
ARG   NE  CZ   sing N N 59  
ARG   NE  HE   sing N N 60  
ARG   CZ  NH1  sing N N 61  
ARG   CZ  NH2  doub N N 62  
ARG   NH1 HH11 sing N N 63  
ARG   NH1 HH12 sing N N 64  
ARG   NH2 HH21 sing N N 65  
ARG   NH2 HH22 sing N N 66  
ARG   OXT HXT  sing N N 67  
ASN   N   CA   sing N N 68  
ASN   N   H    sing N N 69  
ASN   N   H2   sing N N 70  
ASN   CA  C    sing N N 71  
ASN   CA  CB   sing N N 72  
ASN   CA  HA   sing N N 73  
ASN   C   O    doub N N 74  
ASN   C   OXT  sing N N 75  
ASN   CB  CG   sing N N 76  
ASN   CB  HB2  sing N N 77  
ASN   CB  HB3  sing N N 78  
ASN   CG  OD1  doub N N 79  
ASN   CG  ND2  sing N N 80  
ASN   ND2 HD21 sing N N 81  
ASN   ND2 HD22 sing N N 82  
ASN   OXT HXT  sing N N 83  
ASP   N   CA   sing N N 84  
ASP   N   H    sing N N 85  
ASP   N   H2   sing N N 86  
ASP   CA  C    sing N N 87  
ASP   CA  CB   sing N N 88  
ASP   CA  HA   sing N N 89  
ASP   C   O    doub N N 90  
ASP   C   OXT  sing N N 91  
ASP   CB  CG   sing N N 92  
ASP   CB  HB2  sing N N 93  
ASP   CB  HB3  sing N N 94  
ASP   CG  OD1  doub N N 95  
ASP   CG  OD2  sing N N 96  
ASP   OD2 HD2  sing N N 97  
ASP   OXT HXT  sing N N 98  
CYS   N   CA   sing N N 99  
CYS   N   H    sing N N 100 
CYS   N   H2   sing N N 101 
CYS   CA  C    sing N N 102 
CYS   CA  CB   sing N N 103 
CYS   CA  HA   sing N N 104 
CYS   C   O    doub N N 105 
CYS   C   OXT  sing N N 106 
CYS   CB  SG   sing N N 107 
CYS   CB  HB2  sing N N 108 
CYS   CB  HB3  sing N N 109 
CYS   SG  HG   sing N N 110 
CYS   OXT HXT  sing N N 111 
EDO   C1  O1   sing N N 112 
EDO   C1  C2   sing N N 113 
EDO   C1  H11  sing N N 114 
EDO   C1  H12  sing N N 115 
EDO   O1  HO1  sing N N 116 
EDO   C2  O2   sing N N 117 
EDO   C2  H21  sing N N 118 
EDO   C2  H22  sing N N 119 
EDO   O2  HO2  sing N N 120 
GLN   N   CA   sing N N 121 
GLN   N   H    sing N N 122 
GLN   N   H2   sing N N 123 
GLN   CA  C    sing N N 124 
GLN   CA  CB   sing N N 125 
GLN   CA  HA   sing N N 126 
GLN   C   O    doub N N 127 
GLN   C   OXT  sing N N 128 
GLN   CB  CG   sing N N 129 
GLN   CB  HB2  sing N N 130 
GLN   CB  HB3  sing N N 131 
GLN   CG  CD   sing N N 132 
GLN   CG  HG2  sing N N 133 
GLN   CG  HG3  sing N N 134 
GLN   CD  OE1  doub N N 135 
GLN   CD  NE2  sing N N 136 
GLN   NE2 HE21 sing N N 137 
GLN   NE2 HE22 sing N N 138 
GLN   OXT HXT  sing N N 139 
GLU   N   CA   sing N N 140 
GLU   N   H    sing N N 141 
GLU   N   H2   sing N N 142 
GLU   CA  C    sing N N 143 
GLU   CA  CB   sing N N 144 
GLU   CA  HA   sing N N 145 
GLU   C   O    doub N N 146 
GLU   C   OXT  sing N N 147 
GLU   CB  CG   sing N N 148 
GLU   CB  HB2  sing N N 149 
GLU   CB  HB3  sing N N 150 
GLU   CG  CD   sing N N 151 
GLU   CG  HG2  sing N N 152 
GLU   CG  HG3  sing N N 153 
GLU   CD  OE1  doub N N 154 
GLU   CD  OE2  sing N N 155 
GLU   OE2 HE2  sing N N 156 
GLU   OXT HXT  sing N N 157 
GLY   N   CA   sing N N 158 
GLY   N   H    sing N N 159 
GLY   N   H2   sing N N 160 
GLY   CA  C    sing N N 161 
GLY   CA  HA2  sing N N 162 
GLY   CA  HA3  sing N N 163 
GLY   C   O    doub N N 164 
GLY   C   OXT  sing N N 165 
GLY   OXT HXT  sing N N 166 
HIS   N   CA   sing N N 167 
HIS   N   H    sing N N 168 
HIS   N   H2   sing N N 169 
HIS   CA  C    sing N N 170 
HIS   CA  CB   sing N N 171 
HIS   CA  HA   sing N N 172 
HIS   C   O    doub N N 173 
HIS   C   OXT  sing N N 174 
HIS   CB  CG   sing N N 175 
HIS   CB  HB2  sing N N 176 
HIS   CB  HB3  sing N N 177 
HIS   CG  ND1  sing Y N 178 
HIS   CG  CD2  doub Y N 179 
HIS   ND1 CE1  doub Y N 180 
HIS   ND1 HD1  sing N N 181 
HIS   CD2 NE2  sing Y N 182 
HIS   CD2 HD2  sing N N 183 
HIS   CE1 NE2  sing Y N 184 
HIS   CE1 HE1  sing N N 185 
HIS   NE2 HE2  sing N N 186 
HIS   OXT HXT  sing N N 187 
HOH   O   H1   sing N N 188 
HOH   O   H2   sing N N 189 
ILE   N   CA   sing N N 190 
ILE   N   H    sing N N 191 
ILE   N   H2   sing N N 192 
ILE   CA  C    sing N N 193 
ILE   CA  CB   sing N N 194 
ILE   CA  HA   sing N N 195 
ILE   C   O    doub N N 196 
ILE   C   OXT  sing N N 197 
ILE   CB  CG1  sing N N 198 
ILE   CB  CG2  sing N N 199 
ILE   CB  HB   sing N N 200 
ILE   CG1 CD1  sing N N 201 
ILE   CG1 HG12 sing N N 202 
ILE   CG1 HG13 sing N N 203 
ILE   CG2 HG21 sing N N 204 
ILE   CG2 HG22 sing N N 205 
ILE   CG2 HG23 sing N N 206 
ILE   CD1 HD11 sing N N 207 
ILE   CD1 HD12 sing N N 208 
ILE   CD1 HD13 sing N N 209 
ILE   OXT HXT  sing N N 210 
LEU   N   CA   sing N N 211 
LEU   N   H    sing N N 212 
LEU   N   H2   sing N N 213 
LEU   CA  C    sing N N 214 
LEU   CA  CB   sing N N 215 
LEU   CA  HA   sing N N 216 
LEU   C   O    doub N N 217 
LEU   C   OXT  sing N N 218 
LEU   CB  CG   sing N N 219 
LEU   CB  HB2  sing N N 220 
LEU   CB  HB3  sing N N 221 
LEU   CG  CD1  sing N N 222 
LEU   CG  CD2  sing N N 223 
LEU   CG  HG   sing N N 224 
LEU   CD1 HD11 sing N N 225 
LEU   CD1 HD12 sing N N 226 
LEU   CD1 HD13 sing N N 227 
LEU   CD2 HD21 sing N N 228 
LEU   CD2 HD22 sing N N 229 
LEU   CD2 HD23 sing N N 230 
LEU   OXT HXT  sing N N 231 
LYS   N   CA   sing N N 232 
LYS   N   H    sing N N 233 
LYS   N   H2   sing N N 234 
LYS   CA  C    sing N N 235 
LYS   CA  CB   sing N N 236 
LYS   CA  HA   sing N N 237 
LYS   C   O    doub N N 238 
LYS   C   OXT  sing N N 239 
LYS   CB  CG   sing N N 240 
LYS   CB  HB2  sing N N 241 
LYS   CB  HB3  sing N N 242 
LYS   CG  CD   sing N N 243 
LYS   CG  HG2  sing N N 244 
LYS   CG  HG3  sing N N 245 
LYS   CD  CE   sing N N 246 
LYS   CD  HD2  sing N N 247 
LYS   CD  HD3  sing N N 248 
LYS   CE  NZ   sing N N 249 
LYS   CE  HE2  sing N N 250 
LYS   CE  HE3  sing N N 251 
LYS   NZ  HZ1  sing N N 252 
LYS   NZ  HZ2  sing N N 253 
LYS   NZ  HZ3  sing N N 254 
LYS   OXT HXT  sing N N 255 
MET   N   CA   sing N N 256 
MET   N   H    sing N N 257 
MET   N   H2   sing N N 258 
MET   CA  C    sing N N 259 
MET   CA  CB   sing N N 260 
MET   CA  HA   sing N N 261 
MET   C   O    doub N N 262 
MET   C   OXT  sing N N 263 
MET   CB  CG   sing N N 264 
MET   CB  HB2  sing N N 265 
MET   CB  HB3  sing N N 266 
MET   CG  SD   sing N N 267 
MET   CG  HG2  sing N N 268 
MET   CG  HG3  sing N N 269 
MET   SD  CE   sing N N 270 
MET   CE  HE1  sing N N 271 
MET   CE  HE2  sing N N 272 
MET   CE  HE3  sing N N 273 
MET   OXT HXT  sing N N 274 
PHE   N   CA   sing N N 275 
PHE   N   H    sing N N 276 
PHE   N   H2   sing N N 277 
PHE   CA  C    sing N N 278 
PHE   CA  CB   sing N N 279 
PHE   CA  HA   sing N N 280 
PHE   C   O    doub N N 281 
PHE   C   OXT  sing N N 282 
PHE   CB  CG   sing N N 283 
PHE   CB  HB2  sing N N 284 
PHE   CB  HB3  sing N N 285 
PHE   CG  CD1  doub Y N 286 
PHE   CG  CD2  sing Y N 287 
PHE   CD1 CE1  sing Y N 288 
PHE   CD1 HD1  sing N N 289 
PHE   CD2 CE2  doub Y N 290 
PHE   CD2 HD2  sing N N 291 
PHE   CE1 CZ   doub Y N 292 
PHE   CE1 HE1  sing N N 293 
PHE   CE2 CZ   sing Y N 294 
PHE   CE2 HE2  sing N N 295 
PHE   CZ  HZ   sing N N 296 
PHE   OXT HXT  sing N N 297 
PRO   N   CA   sing N N 298 
PRO   N   CD   sing N N 299 
PRO   N   H    sing N N 300 
PRO   CA  C    sing N N 301 
PRO   CA  CB   sing N N 302 
PRO   CA  HA   sing N N 303 
PRO   C   O    doub N N 304 
PRO   C   OXT  sing N N 305 
PRO   CB  CG   sing N N 306 
PRO   CB  HB2  sing N N 307 
PRO   CB  HB3  sing N N 308 
PRO   CG  CD   sing N N 309 
PRO   CG  HG2  sing N N 310 
PRO   CG  HG3  sing N N 311 
PRO   CD  HD2  sing N N 312 
PRO   CD  HD3  sing N N 313 
PRO   OXT HXT  sing N N 314 
SER   N   CA   sing N N 315 
SER   N   H    sing N N 316 
SER   N   H2   sing N N 317 
SER   CA  C    sing N N 318 
SER   CA  CB   sing N N 319 
SER   CA  HA   sing N N 320 
SER   C   O    doub N N 321 
SER   C   OXT  sing N N 322 
SER   CB  OG   sing N N 323 
SER   CB  HB2  sing N N 324 
SER   CB  HB3  sing N N 325 
SER   OG  HG   sing N N 326 
SER   OXT HXT  sing N N 327 
SO4   S   O1   doub N N 328 
SO4   S   O2   doub N N 329 
SO4   S   O3   sing N N 330 
SO4   S   O4   sing N N 331 
THR   N   CA   sing N N 332 
THR   N   H    sing N N 333 
THR   N   H2   sing N N 334 
THR   CA  C    sing N N 335 
THR   CA  CB   sing N N 336 
THR   CA  HA   sing N N 337 
THR   C   O    doub N N 338 
THR   C   OXT  sing N N 339 
THR   CB  OG1  sing N N 340 
THR   CB  CG2  sing N N 341 
THR   CB  HB   sing N N 342 
THR   OG1 HG1  sing N N 343 
THR   CG2 HG21 sing N N 344 
THR   CG2 HG22 sing N N 345 
THR   CG2 HG23 sing N N 346 
THR   OXT HXT  sing N N 347 
TRP   N   CA   sing N N 348 
TRP   N   H    sing N N 349 
TRP   N   H2   sing N N 350 
TRP   CA  C    sing N N 351 
TRP   CA  CB   sing N N 352 
TRP   CA  HA   sing N N 353 
TRP   C   O    doub N N 354 
TRP   C   OXT  sing N N 355 
TRP   CB  CG   sing N N 356 
TRP   CB  HB2  sing N N 357 
TRP   CB  HB3  sing N N 358 
TRP   CG  CD1  doub Y N 359 
TRP   CG  CD2  sing Y N 360 
TRP   CD1 NE1  sing Y N 361 
TRP   CD1 HD1  sing N N 362 
TRP   CD2 CE2  doub Y N 363 
TRP   CD2 CE3  sing Y N 364 
TRP   NE1 CE2  sing Y N 365 
TRP   NE1 HE1  sing N N 366 
TRP   CE2 CZ2  sing Y N 367 
TRP   CE3 CZ3  doub Y N 368 
TRP   CE3 HE3  sing N N 369 
TRP   CZ2 CH2  doub Y N 370 
TRP   CZ2 HZ2  sing N N 371 
TRP   CZ3 CH2  sing Y N 372 
TRP   CZ3 HZ3  sing N N 373 
TRP   CH2 HH2  sing N N 374 
TRP   OXT HXT  sing N N 375 
TYR   N   CA   sing N N 376 
TYR   N   H    sing N N 377 
TYR   N   H2   sing N N 378 
TYR   CA  C    sing N N 379 
TYR   CA  CB   sing N N 380 
TYR   CA  HA   sing N N 381 
TYR   C   O    doub N N 382 
TYR   C   OXT  sing N N 383 
TYR   CB  CG   sing N N 384 
TYR   CB  HB2  sing N N 385 
TYR   CB  HB3  sing N N 386 
TYR   CG  CD1  doub Y N 387 
TYR   CG  CD2  sing Y N 388 
TYR   CD1 CE1  sing Y N 389 
TYR   CD1 HD1  sing N N 390 
TYR   CD2 CE2  doub Y N 391 
TYR   CD2 HD2  sing N N 392 
TYR   CE1 CZ   doub Y N 393 
TYR   CE1 HE1  sing N N 394 
TYR   CE2 CZ   sing Y N 395 
TYR   CE2 HE2  sing N N 396 
TYR   CZ  OH   sing N N 397 
TYR   OH  HH   sing N N 398 
TYR   OXT HXT  sing N N 399 
VAL   N   CA   sing N N 400 
VAL   N   H    sing N N 401 
VAL   N   H2   sing N N 402 
VAL   CA  C    sing N N 403 
VAL   CA  CB   sing N N 404 
VAL   CA  HA   sing N N 405 
VAL   C   O    doub N N 406 
VAL   C   OXT  sing N N 407 
VAL   CB  CG1  sing N N 408 
VAL   CB  CG2  sing N N 409 
VAL   CB  HB   sing N N 410 
VAL   CG1 HG11 sing N N 411 
VAL   CG1 HG12 sing N N 412 
VAL   CG1 HG13 sing N N 413 
VAL   CG2 HG21 sing N N 414 
VAL   CG2 HG22 sing N N 415 
VAL   CG2 HG23 sing N N 416 
VAL   OXT HXT  sing N N 417 
# 
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                    7HGB 
_atom_sites.fract_transf_matrix[1][1]   0.024004 
_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]   0.023657 
_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]   0.006259 
_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  ? 1.090   4.204   2.502   1.00 46.10  ? 1   MET   A N   1 
ATOM   2    C CA  . MET   A 1 2  ? 0.023   3.450   1.791   1.00 44.87  ? 1   MET   A CA  1 
ATOM   3    C C   . MET   A 1 2  ? 0.649   2.432   0.838   1.00 43.34  ? 1   MET   A C   1 
ATOM   4    O O   . MET   A 1 2  ? 1.740   2.628   0.304   1.00 44.66  ? 1   MET   A O   1 
ATOM   5    C CB  . MET   A 1 2  ? -0.928  4.389   1.035   1.00 47.63  ? 1   MET   A CB  1 
ATOM   6    C CG  . MET   A 1 2  ? -1.940  5.123   1.913   1.00 54.60  ? 1   MET   A CG  1 
ATOM   7    S SD  . MET   A 1 2  ? -3.302  4.238   2.722   1.00 55.45  ? 1   MET   A SD  1 
ATOM   8    C CE  . MET   A 1 2  ? -3.646  5.547   3.910   1.00 49.18  ? 1   MET   A CE  1 
ATOM   9    N N   . PRO   A 1 3  ? -0.032  1.296   0.584   1.00 35.78  ? 2   PRO   A N   1 
ATOM   10   C CA  . PRO   A 1 3  ? 0.528   0.232   -0.246  1.00 35.45  ? 2   PRO   A CA  1 
ATOM   11   C C   . PRO   A 1 3  ? 0.658   0.552   -1.731  1.00 37.60  ? 2   PRO   A C   1 
ATOM   12   O O   . PRO   A 1 3  ? -0.037  1.390   -2.293  1.00 36.09  ? 2   PRO   A O   1 
ATOM   13   C CB  . PRO   A 1 3  ? -0.504  -0.906  -0.005  1.00 35.43  ? 2   PRO   A CB  1 
ATOM   14   C CG  . PRO   A 1 3  ? -1.242  -0.501  1.267   1.00 41.65  ? 2   PRO   A CG  1 
ATOM   15   C CD  . PRO   A 1 3  ? -1.394  0.993   1.075   1.00 37.72  ? 2   PRO   A CD  1 
ATOM   16   N N   . HIS   A 1 4  ? 1.576   -0.156  -2.370  1.00 33.38  ? 3   HIS   A N   1 
ATOM   17   C CA  . HIS   A 1 4  ? 1.747   -0.019  -3.798  1.00 35.00  ? 3   HIS   A CA  1 
ATOM   18   C C   . HIS   A 1 4  ? 1.193   -1.311  -4.382  1.00 29.49  ? 3   HIS   A C   1 
ATOM   19   O O   . HIS   A 1 4  ? 0.745   -2.181  -3.628  1.00 30.64  ? 3   HIS   A O   1 
ATOM   20   C CB  . HIS   A 1 4  ? 3.240   0.126   -4.115  1.00 43.35  ? 3   HIS   A CB  1 
ATOM   21   C CG  . HIS   A 1 4  ? 3.845   1.418   -3.645  1.00 55.92  ? 3   HIS   A CG  1 
ATOM   22   N ND1 . HIS   A 1 4  ? 4.312   1.635   -2.365  1.00 57.08  ? 3   HIS   A ND1 1 
ATOM   23   C CD2 . HIS   A 1 4  ? 4.062   2.565   -4.309  1.00 60.89  ? 3   HIS   A CD2 1 
ATOM   24   C CE1 . HIS   A 1 4  ? 4.784   2.872   -2.270  1.00 60.96  ? 3   HIS   A CE1 1 
ATOM   25   N NE2 . HIS   A 1 4  ? 4.646   3.454   -3.441  1.00 57.14  ? 3   HIS   A NE2 1 
ATOM   26   N N   . ALA   A 1 5  ? 1.184   -1.437  -5.700  1.00 27.23  ? 4   ALA   A N   1 
ATOM   27   C CA  . ALA   A 1 5  ? 0.949   -2.736  -6.309  1.00 26.45  ? 4   ALA   A CA  1 
ATOM   28   C C   . ALA   A 1 5  ? 2.100   -3.685  -5.974  1.00 24.81  ? 4   ALA   A C   1 
ATOM   29   O O   . ALA   A 1 5  ? 3.186   -3.238  -5.568  1.00 26.07  ? 4   ALA   A O   1 
ATOM   30   C CB  . ALA   A 1 5  ? 0.800   -2.558  -7.816  1.00 32.51  ? 4   ALA   A CB  1 
ATOM   31   N N   . PHE   A 1 6  ? 1.819   -4.980  -6.108  1.00 24.51  ? 5   PHE   A N   1 
ATOM   32   C CA  . PHE   A 1 6  ? 2.846   -6.013  -5.944  1.00 23.68  ? 5   PHE   A CA  1 
ATOM   33   C C   . PHE   A 1 6  ? 4.000   -5.772  -6.932  1.00 27.22  ? 5   PHE   A C   1 
ATOM   34   O O   . PHE   A 1 6  ? 3.766   -5.395  -8.091  1.00 27.50  ? 5   PHE   A O   1 
ATOM   35   C CB  . PHE   A 1 6  ? 2.288   -7.447  -6.022  1.00 25.77  ? 5   PHE   A CB  1 
ATOM   36   C CG  . PHE   A 1 6  ? 1.496   -7.811  -4.766  1.00 24.86  ? 5   PHE   A CG  1 
ATOM   37   C CD1 . PHE   A 1 6  ? 2.156   -8.016  -3.545  1.00 21.57  ? 5   PHE   A CD1 1 
ATOM   38   C CD2 . PHE   A 1 6  ? 0.103   -7.973  -4.814  1.00 24.35  ? 5   PHE   A CD2 1 
ATOM   39   C CE1 . PHE   A 1 6  ? 1.449   -8.320  -2.371  1.00 22.06  ? 5   PHE   A CE1 1 
ATOM   40   C CE2 . PHE   A 1 6  ? -0.590  -8.323  -3.649  1.00 20.91  ? 5   PHE   A CE2 1 
ATOM   41   C CZ  . PHE   A 1 6  ? 0.072   -8.471  -2.458  1.00 23.79  ? 5   PHE   A CZ  1 
ATOM   42   N N   . LYS   A 1 7  ? 5.230   -6.058  -6.473  1.00 21.35  ? 6   LYS   A N   1 
ATOM   43   C CA  . LYS   A 1 7  ? 6.393   -5.974  -7.364  1.00 22.83  ? 6   LYS   A CA  1 
ATOM   44   C C   . LYS   A 1 7  ? 7.309   -7.176  -7.068  1.00 23.61  ? 6   LYS   A C   1 
ATOM   45   O O   . LYS   A 1 7  ? 7.241   -7.783  -5.998  1.00 22.07  ? 6   LYS   A O   1 
ATOM   46   C CB  . LYS   A 1 7  ? 7.125   -4.656  -7.052  1.00 27.09  ? 6   LYS   A CB  1 
ATOM   47   C CG  . LYS   A 1 7  ? 7.816   -4.562  -5.740  1.00 27.84  ? 6   LYS   A CG  1 
ATOM   48   C CD  . LYS   A 1 7  ? 8.403   -3.177  -5.420  1.00 37.22  ? 6   LYS   A CD  1 
ATOM   49   C CE  . LYS   A 1 7  ? 9.025   -3.182  -4.041  1.00 35.09  ? 6   LYS   A CE  1 
ATOM   50   N NZ  . LYS   A 1 7  ? 8.018   -3.204  -2.964  1.00 34.88  ? 6   LYS   A NZ  1 
ATOM   51   N N   . PRO   A 1 8  ? 8.183   -7.580  -8.003  1.00 21.88  ? 7   PRO   A N   1 
ATOM   52   C CA  . PRO   A 1 8  ? 9.127   -8.667  -7.747  1.00 21.65  ? 7   PRO   A CA  1 
ATOM   53   C C   . PRO   A 1 8  ? 9.892   -8.387  -6.460  1.00 20.45  ? 7   PRO   A C   1 
ATOM   54   O O   . PRO   A 1 8  ? 10.358  -7.272  -6.198  1.00 23.70  ? 7   PRO   A O   1 
ATOM   55   C CB  . PRO   A 1 8  ? 10.022  -8.618  -9.022  1.00 23.71  ? 7   PRO   A CB  1 
ATOM   56   C CG  . PRO   A 1 8  ? 9.058   -8.059  -10.068 1.00 24.68  ? 7   PRO   A CG  1 
ATOM   57   C CD  . PRO   A 1 8  ? 8.357   -6.949  -9.332  1.00 24.38  ? 7   PRO   A CD  1 
ATOM   58   N N   . GLY   A 1 9  ? 10.026  -9.447  -5.632  1.00 20.54  ? 8   GLY   A N   1 
ATOM   59   C CA  . GLY   A 1 9  ? 10.774  -9.364  -4.403  1.00 21.54  ? 8   GLY   A CA  1 
ATOM   60   C C   . GLY   A 1 9  ? 9.841   -9.249  -3.203  1.00 20.87  ? 8   GLY   A C   1 
ATOM   61   O O   . GLY   A 1 9  ? 10.243  -9.511  -2.060  1.00 21.04  ? 8   GLY   A O   1 
ATOM   62   N N   . ASP   A 1 10 ? 8.586   -8.828  -3.451  1.00 18.83  ? 9   ASP   A N   1 
ATOM   63   C CA  . ASP   A 1 10 ? 7.694   -8.784  -2.306  1.00 17.74  ? 9   ASP   A CA  1 
ATOM   64   C C   . ASP   A 1 10 ? 7.435   -10.171 -1.694  1.00 18.20  ? 9   ASP   A C   1 
ATOM   65   O O   . ASP   A 1 10 ? 7.292   -11.164 -2.394  1.00 19.93  ? 9   ASP   A O   1 
ATOM   66   C CB  . ASP   A 1 10 ? 6.370   -8.155  -2.733  1.00 18.55  ? 9   ASP   A CB  1 
ATOM   67   C CG  . ASP   A 1 10 ? 6.388   -6.653  -2.953  1.00 21.44  ? 9   ASP   A CG  1 
ATOM   68   O OD1 . ASP   A 1 10 ? 7.315   -5.974  -2.446  1.00 23.31  ? 9   ASP   A OD1 1 
ATOM   69   O OD2 . ASP   A 1 10 ? 5.408   -6.140  -3.563  1.00 21.72  ? 9   ASP   A OD2 1 
ATOM   70   N N   . LEU   A 1 11 ? 7.299   -10.192 -0.358  1.00 18.82  ? 10  LEU   A N   1 
ATOM   71   C CA  . LEU   A 1 11 ? 7.139   -11.416 0.427   1.00 16.61  ? 10  LEU   A CA  1 
ATOM   72   C C   . LEU   A 1 11 ? 5.663   -11.547 0.815   1.00 18.02  ? 10  LEU   A C   1 
ATOM   73   O O   . LEU   A 1 11 ? 5.061   -10.540 1.232   1.00 20.48  ? 10  LEU   A O   1 
ATOM   74   C CB  . LEU   A 1 11 ? 8.072   -11.493 1.648   1.00 18.38  ? 10  LEU   A CB  1 
ATOM   75   C CG  . LEU   A 1 11 ? 9.566   -11.314 1.298   1.00 18.50  ? 10  LEU   A CG  1 
ATOM   76   C CD1 . LEU   A 1 11 ? 10.463  -11.406 2.546   1.00 21.14  ? 10  LEU   A CD1 1 
ATOM   77   C CD2 . LEU   A 1 11 ? 10.041  -12.280 0.219   1.00 20.36  ? 10  LEU   A CD2 1 
ATOM   78   N N   . VAL   A 1 12 ? 5.105   -12.777 0.670   1.00 17.01  ? 11  VAL   A N   1 
ATOM   79   C CA  . VAL   A 1 12 ? 3.667   -12.978 0.900   1.00 17.84  ? 11  VAL   A CA  1 
ATOM   80   C C   . VAL   A 1 12 ? 3.450   -14.335 1.561   1.00 19.57  ? 11  VAL   A C   1 
ATOM   81   O O   . VAL   A 1 12 ? 4.313   -15.199 1.581   1.00 20.03  ? 11  VAL   A O   1 
ATOM   82   C CB  . VAL   A 1 12 ? 2.836   -12.919 -0.397  1.00 18.38  ? 11  VAL   A CB  1 
ATOM   83   C CG1 . VAL   A 1 12 ? 2.964   -11.556 -1.065  1.00 19.88  ? 11  VAL   A CG1 1 
ATOM   84   C CG2 . VAL   A 1 12 ? 3.267   -13.938 -1.453  1.00 19.91  ? 11  VAL   A CG2 1 
ATOM   85   N N   . PHE   A 1 13 ? 2.222   -14.543 2.070   1.00 19.23  ? 12  PHE   A N   1 
ATOM   86   C CA  . PHE   A 1 13 ? 1.656   -15.885 2.036   1.00 19.55  ? 12  PHE   A CA  1 
ATOM   87   C C   . PHE   A 1 13 ? 0.675   -15.944 0.861   1.00 21.14  ? 12  PHE   A C   1 
ATOM   88   O O   . PHE   A 1 13 ? -0.108  -15.013 0.662   1.00 21.00  ? 12  PHE   A O   1 
ATOM   89   C CB  . PHE   A 1 13 ? 0.910   -16.267 3.338   1.00 20.25  ? 12  PHE   A CB  1 
ATOM   90   C CG  . PHE   A 1 13 ? 1.852   -16.336 4.521   1.00 20.25  ? 12  PHE   A CG  1 
ATOM   91   C CD1 . PHE   A 1 13 ? 2.147   -15.154 5.212   1.00 21.69  ? 12  PHE   A CD1 1 
ATOM   92   C CD2 . PHE   A 1 13 ? 2.341   -17.580 4.975   1.00 22.07  ? 12  PHE   A CD2 1 
ATOM   93   C CE1 . PHE   A 1 13 ? 3.048   -15.245 6.285   1.00 25.37  ? 12  PHE   A CE1 1 
ATOM   94   C CE2 . PHE   A 1 13 ? 3.272   -17.636 6.018   1.00 22.54  ? 12  PHE   A CE2 1 
ATOM   95   C CZ  . PHE   A 1 13 ? 3.587   -16.477 6.664   1.00 23.25  ? 12  PHE   A CZ  1 
ATOM   96   N N   . ALA   A 1 14 ? 0.771   -17.037 0.072   1.00 19.81  ? 13  ALA   A N   1 
ATOM   97   C CA  . ALA   A 1 14 ? -0.017  -17.176 -1.147  1.00 20.62  ? 13  ALA   A CA  1 
ATOM   98   C C   . ALA   A 1 14 ? -0.993  -18.337 -0.914  1.00 21.73  ? 13  ALA   A C   1 
ATOM   99   O O   . ALA   A 1 14 ? -0.618  -19.402 -0.390  1.00 22.68  ? 13  ALA   A O   1 
ATOM   100  C CB  . ALA   A 1 14 ? 0.888   -17.421 -2.360  1.00 19.98  ? 13  ALA   A CB  1 
ATOM   101  N N   . LYS   A 1 15 ? -2.262  -18.117 -1.302  1.00 20.87  ? 14  LYS   A N   1 
ATOM   102  C CA  . LYS   A 1 15 ? -3.288  -19.144 -1.089  1.00 21.75  ? 14  LYS   A CA  1 
ATOM   103  C C   . LYS   A 1 15 ? -3.665  -19.835 -2.404  1.00 25.19  ? 14  LYS   A C   1 
ATOM   104  O O   . LYS   A 1 15 ? -4.037  -19.176 -3.369  1.00 28.55  ? 14  LYS   A O   1 
ATOM   105  C CB  . LYS   A 1 15 ? -4.515  -18.451 -0.462  1.00 23.17  ? 14  LYS   A CB  1 
ATOM   106  C CG  . LYS   A 1 15 ? -5.658  -19.451 -0.011  1.00 27.87  ? 14  LYS   A CG  1 
ATOM   107  C CD  . LYS   A 1 15 ? -5.170  -20.425 1.061   1.00 29.39  ? 14  LYS   A CD  1 
ATOM   108  C CE  . LYS   A 1 15 ? -6.266  -21.203 1.783   1.00 31.16  ? 14  LYS   A CE  1 
ATOM   109  N NZ  . LYS   A 1 15 ? -6.611  -22.356 0.958   1.00 34.34  ? 14  LYS   A NZ  1 
ATOM   110  N N   . MET   A 1 16 ? -3.631  -21.177 -2.354  1.00 24.18  ? 15  MET   A N   1 
ATOM   111  C CA  . MET   A 1 16 ? -4.050  -22.087 -3.412  1.00 27.08  ? 15  MET   A CA  1 
ATOM   112  C C   . MET   A 1 16 ? -5.167  -22.951 -2.794  1.00 33.28  ? 15  MET   A C   1 
ATOM   113  O O   . MET   A 1 16 ? -5.071  -23.361 -1.644  1.00 28.33  ? 15  MET   A O   1 
ATOM   114  C CB  . MET   A 1 16 ? -2.890  -23.047 -3.746  1.00 29.64  ? 15  MET   A CB  1 
ATOM   115  C CG  . MET   A 1 16 ? -1.553  -22.419 -4.170  1.00 30.63  ? 15  MET   A CG  1 
ATOM   116  S SD  . MET   A 1 16 ? -1.635  -21.832 -5.879  1.00 35.65  ? 15  MET   A SD  1 
ATOM   117  C CE  . MET   A 1 16 ? -1.512  -23.334 -6.796  1.00 30.66  ? 15  MET   A CE  1 
ATOM   118  N N   . LYS   A 1 17 ? -6.212  -23.231 -3.572  1.00 36.84  ? 16  LYS   A N   1 
ATOM   119  C CA  . LYS   A 1 17 ? -7.299  -24.098 -3.128  1.00 38.11  ? 16  LYS   A CA  1 
ATOM   120  C C   . LYS   A 1 17 ? -6.716  -25.414 -2.625  1.00 33.71  ? 16  LYS   A C   1 
ATOM   121  O O   . LYS   A 1 17 ? -5.802  -25.996 -3.216  1.00 36.68  ? 16  LYS   A O   1 
ATOM   122  C CB  . LYS   A 1 17 ? -8.195  -24.345 -4.355  1.00 46.85  ? 16  LYS   A CB  1 
ATOM   123  C CG  . LYS   A 1 17 ? -9.448  -25.190 -4.122  1.00 52.32  ? 16  LYS   A CG  1 
ATOM   124  C CD  . LYS   A 1 17 ? -10.492 -24.416 -3.322  1.00 54.72  ? 16  LYS   A CD  1 
ATOM   125  N N   . GLY   A 1 18 ? -7.179  -25.844 -1.442  1.00 37.55  ? 17  GLY   A N   1 
ATOM   126  C CA  . GLY   A 1 18 ? -6.742  -27.132 -0.948  1.00 33.81  ? 17  GLY   A CA  1 
ATOM   127  C C   . GLY   A 1 18 ? -5.414  -27.060 -0.197  1.00 38.71  ? 17  GLY   A C   1 
ATOM   128  O O   . GLY   A 1 18 ? -4.943  -28.055 0.331   1.00 41.54  ? 17  GLY   A O   1 
ATOM   129  N N   . TYR   A 1 19 ? -4.780  -25.876 -0.145  1.00 32.47  ? 18  TYR   A N   1 
ATOM   130  C CA  . TYR   A 1 19 ? -3.500  -25.807 0.542   1.00 29.56  ? 18  TYR   A CA  1 
ATOM   131  C C   . TYR   A 1 19 ? -3.543  -24.699 1.584   1.00 27.44  ? 18  TYR   A C   1 
ATOM   132  O O   . TYR   A 1 19 ? -4.282  -23.733 1.409   1.00 28.08  ? 18  TYR   A O   1 
ATOM   133  C CB  . TYR   A 1 19 ? -2.448  -25.356 -0.476  1.00 34.31  ? 18  TYR   A CB  1 
ATOM   134  C CG  . TYR   A 1 19 ? -1.915  -26.419 -1.425  1.00 37.27  ? 18  TYR   A CG  1 
ATOM   135  C CD1 . TYR   A 1 19 ? -0.820  -27.187 -1.048  1.00 50.77  ? 18  TYR   A CD1 1 
ATOM   136  C CD2 . TYR   A 1 19 ? -2.459  -26.608 -2.690  1.00 43.67  ? 18  TYR   A CD2 1 
ATOM   137  C CE1 . TYR   A 1 19 ? -0.300  -28.156 -1.893  1.00 53.02  ? 18  TYR   A CE1 1 
ATOM   138  C CE2 . TYR   A 1 19 ? -1.919  -27.551 -3.563  1.00 46.54  ? 18  TYR   A CE2 1 
ATOM   139  C CZ  . TYR   A 1 19 ? -0.840  -28.326 -3.155  1.00 54.10  ? 18  TYR   A CZ  1 
ATOM   140  O OH  . TYR   A 1 19 ? -0.275  -29.291 -3.948  1.00 59.90  ? 18  TYR   A OH  1 
ATOM   141  N N   . PRO   A 1 20 ? -2.746  -24.793 2.673   1.00 28.14  ? 19  PRO   A N   1 
ATOM   142  C CA  . PRO   A 1 20 ? -2.663  -23.724 3.688   1.00 26.09  ? 19  PRO   A CA  1 
ATOM   143  C C   . PRO   A 1 20 ? -2.015  -22.479 3.056   1.00 25.77  ? 19  PRO   A C   1 
ATOM   144  O O   . PRO   A 1 20 ? -1.299  -22.649 2.099   1.00 26.89  ? 19  PRO   A O   1 
ATOM   145  C CB  . PRO   A 1 20 ? -1.785  -24.324 4.796   1.00 30.54  ? 19  PRO   A CB  1 
ATOM   146  C CG  . PRO   A 1 20 ? -1.007  -25.454 4.109   1.00 29.01  ? 19  PRO   A CG  1 
ATOM   147  C CD  . PRO   A 1 20 ? -1.861  -25.945 2.966   1.00 31.16  ? 19  PRO   A CD  1 
ATOM   148  N N   . HIS   A 1 21 ? -2.313  -21.274 3.561   1.00 23.87  ? 20  HIS   A N   1 
ATOM   149  C CA  . HIS   A 1 21 ? -1.609  -20.055 3.147   1.00 21.45  ? 20  HIS   A CA  1 
ATOM   150  C C   . HIS   A 1 21 ? -0.105  -20.312 3.248   1.00 24.63  ? 20  HIS   A C   1 
ATOM   151  O O   . HIS   A 1 21 ? 0.369   -20.723 4.303   1.00 22.56  ? 20  HIS   A O   1 
ATOM   152  C CB  . HIS   A 1 21 ? -2.050  -18.878 4.039   1.00 22.98  ? 20  HIS   A CB  1 
ATOM   153  C CG  . HIS   A 1 21 ? -3.504  -18.464 3.837   1.00 25.35  ? 20  HIS   A CG  1 
ATOM   154  N ND1 . HIS   A 1 21 ? -4.550  -19.134 4.462   1.00 27.56  ? 20  HIS   A ND1 1 
ATOM   155  C CD2 . HIS   A 1 21 ? -4.079  -17.484 3.092   1.00 26.39  ? 20  HIS   A CD2 1 
ATOM   156  C CE1 . HIS   A 1 21 ? -5.710  -18.552 4.127   1.00 28.67  ? 20  HIS   A CE1 1 
ATOM   157  N NE2 . HIS   A 1 21 ? -5.461  -17.543 3.308   1.00 28.21  ? 20  HIS   A NE2 1 
ATOM   158  N N   . TRP   A 1 22 ? 0.632   -20.072 2.143   1.00 23.16  ? 21  TRP   A N   1 
ATOM   159  C CA  . TRP   A 1 22 ? 1.948   -20.686 1.973   1.00 20.90  ? 21  TRP   A CA  1 
ATOM   160  C C   . TRP   A 1 22 ? 3.018   -19.597 1.862   1.00 20.80  ? 21  TRP   A C   1 
ATOM   161  O O   . TRP   A 1 22 ? 2.862   -18.685 1.064   1.00 20.54  ? 21  TRP   A O   1 
ATOM   162  C CB  . TRP   A 1 22 ? 1.967   -21.565 0.721   1.00 21.42  ? 21  TRP   A CB  1 
ATOM   163  C CG  . TRP   A 1 22 ? 3.071   -22.592 0.776   1.00 24.15  ? 21  TRP   A CG  1 
ATOM   164  C CD1 . TRP   A 1 22 ? 4.415   -22.403 0.577   1.00 23.41  ? 21  TRP   A CD1 1 
ATOM   165  C CD2 . TRP   A 1 22 ? 2.897   -23.989 1.091   1.00 25.21  ? 21  TRP   A CD2 1 
ATOM   166  N NE1 . TRP   A 1 22 ? 5.091   -23.601 0.719   1.00 23.46  ? 21  TRP   A NE1 1 
ATOM   167  C CE2 . TRP   A 1 22 ? 4.183   -24.583 1.026   1.00 24.53  ? 21  TRP   A CE2 1 
ATOM   168  C CE3 . TRP   A 1 22 ? 1.790   -24.792 1.385   1.00 29.56  ? 21  TRP   A CE3 1 
ATOM   169  C CZ2 . TRP   A 1 22 ? 4.394   -25.945 1.283   1.00 32.29  ? 21  TRP   A CZ2 1 
ATOM   170  C CZ3 . TRP   A 1 22 ? 2.001   -26.150 1.601   1.00 31.78  ? 21  TRP   A CZ3 1 
ATOM   171  C CH2 . TRP   A 1 22 ? 3.294   -26.707 1.580   1.00 31.75  ? 21  TRP   A CH2 1 
ATOM   172  N N   . PRO   A 1 23 ? 4.170   -19.688 2.573   1.00 20.84  ? 22  PRO   A N   1 
ATOM   173  C CA  . PRO   A 1 23 ? 5.251   -18.691 2.400   1.00 20.85  ? 22  PRO   A CA  1 
ATOM   174  C C   . PRO   A 1 23 ? 5.743   -18.635 0.951   1.00 19.20  ? 22  PRO   A C   1 
ATOM   175  O O   . PRO   A 1 23 ? 6.084   -19.670 0.339   1.00 19.97  ? 22  PRO   A O   1 
ATOM   176  C CB  . PRO   A 1 23 ? 6.339   -19.140 3.388   1.00 20.39  ? 22  PRO   A CB  1 
ATOM   177  C CG  . PRO   A 1 23 ? 6.064   -20.620 3.585   1.00 20.34  ? 22  PRO   A CG  1 
ATOM   178  C CD  . PRO   A 1 23 ? 4.530   -20.772 3.516   1.00 19.37  ? 22  PRO   A CD  1 
ATOM   179  N N   . ALA   A 1 24 ? 5.786   -17.415 0.379   1.00 17.48  ? 23  ALA   A N   1 
ATOM   180  C CA  . ALA   A 1 24 ? 6.133   -17.276 -1.028  1.00 18.12  ? 23  ALA   A CA  1 
ATOM   181  C C   . ALA   A 1 24 ? 6.667   -15.881 -1.330  1.00 17.91  ? 23  ALA   A C   1 
ATOM   182  O O   . ALA   A 1 24 ? 6.649   -15.000 -0.491  1.00 18.49  ? 23  ALA   A O   1 
ATOM   183  C CB  . ALA   A 1 24 ? 4.885   -17.612 -1.901  1.00 19.00  ? 23  ALA   A CB  1 
ATOM   184  N N   . ARG   A 1 25 ? 7.207   -15.691 -2.546  1.00 17.20  ? 24  ARG   A N   1 
ATOM   185  C CA  . ARG   A 1 25 ? 7.605   -14.384 -3.048  1.00 18.09  ? 24  ARG   A CA  1 
ATOM   186  C C   . ARG   A 1 25 ? 7.034   -14.134 -4.447  1.00 16.80  ? 24  ARG   A C   1 
ATOM   187  O O   . ARG   A 1 25 ? 6.806   -15.070 -5.227  1.00 18.62  ? 24  ARG   A O   1 
ATOM   188  C CB  . ARG   A 1 25 ? 9.131   -14.241 -2.959  1.00 18.01  ? 24  ARG   A CB  1 
ATOM   189  C CG  . ARG   A 1 25 ? 9.807   -15.098 -4.012  1.00 18.41  ? 24  ARG   A CG  1 
ATOM   190  C CD  . ARG   A 1 25 ? 11.396  -14.930 -3.800  1.00 18.48  ? 24  ARG   A CD  1 
ATOM   191  N NE  . ARG   A 1 25 ? 12.068  -15.728 -4.854  1.00 21.04  ? 24  ARG   A NE  1 
ATOM   192  C CZ  . ARG   A 1 25 ? 13.347  -16.118 -4.766  1.00 21.53  ? 24  ARG   A CZ  1 
ATOM   193  N NH1 . ARG   A 1 25 ? 14.069  -15.998 -3.647  1.00 22.13  ? 24  ARG   A NH1 1 
ATOM   194  N NH2 . ARG   A 1 25 ? 13.876  -16.774 -5.794  1.00 24.84  ? 24  ARG   A NH2 1 
ATOM   195  N N   . ILE   A 1 26 ? 6.891   -12.850 -4.748  1.00 18.54  ? 25  ILE   A N   1 
ATOM   196  C CA  . ILE   A 1 26 ? 6.699   -12.477 -6.147  1.00 19.33  ? 25  ILE   A CA  1 
ATOM   197  C C   . ILE   A 1 26 ? 8.033   -12.585 -6.854  1.00 22.99  ? 25  ILE   A C   1 
ATOM   198  O O   . ILE   A 1 26 ? 8.997   -11.953 -6.456  1.00 21.93  ? 25  ILE   A O   1 
ATOM   199  C CB  . ILE   A 1 26 ? 6.202   -11.033 -6.246  1.00 20.75  ? 25  ILE   A CB  1 
ATOM   200  C CG1 . ILE   A 1 26 ? 5.049   -10.759 -5.251  1.00 24.38  ? 25  ILE   A CG1 1 
ATOM   201  C CG2 . ILE   A 1 26 ? 5.838   -10.670 -7.702  1.00 21.93  ? 25  ILE   A CG2 1 
ATOM   202  C CD1 . ILE   A 1 26 ? 3.691   -11.309 -5.630  1.00 29.01  ? 25  ILE   A CD1 1 
ATOM   203  N N   . ASP   A 1 27 ? 8.071   -13.406 -7.891  1.00 22.54  ? 26  ASP   A N   1 
ATOM   204  C CA  . ASP   A 1 27 ? 9.307   -13.560 -8.654  1.00 23.77  ? 26  ASP   A CA  1 
ATOM   205  C C   . ASP   A 1 27 ? 9.415   -12.563 -9.799  1.00 25.80  ? 26  ASP   A C   1 
ATOM   206  O O   . ASP   A 1 27 ? 8.449   -11.950 -10.244 1.00 26.12  ? 26  ASP   A O   1 
ATOM   207  C CB  . ASP   A 1 27 ? 9.419   -14.945 -9.247  1.00 22.96  ? 26  ASP   A CB  1 
ATOM   208  C CG  . ASP   A 1 27 ? 10.389  -15.902 -8.569  1.00 25.76  ? 26  ASP   A CG  1 
ATOM   209  O OD1 . ASP   A 1 27 ? 10.986  -15.514 -7.521  1.00 29.26  ? 26  ASP   A OD1 1 
ATOM   210  O OD2 . ASP   A 1 27 ? 10.597  -16.984 -9.106  1.00 25.66  ? 26  ASP   A OD2 1 
ATOM   211  N N   . ASP   A 1 28 ? 10.663  -12.436 -10.320 1.00 27.78  ? 27  ASP   A N   1 
ATOM   212  C CA  . ASP   A 1 28 ? 10.866  -11.727 -11.559 1.00 31.42  ? 27  ASP   A CA  1 
ATOM   213  C C   . ASP   A 1 28 ? 10.600  -12.727 -12.688 1.00 31.09  ? 27  ASP   A C   1 
ATOM   214  O O   . ASP   A 1 28 ? 10.497  -13.922 -12.469 1.00 30.28  ? 27  ASP   A O   1 
ATOM   215  C CB  . ASP   A 1 28 ? 12.323  -11.285 -11.684 1.00 38.29  ? 27  ASP   A CB  1 
ATOM   216  C CG  . ASP   A 1 28 ? 12.758  -10.011 -10.962 1.00 46.86  ? 27  ASP   A CG  1 
ATOM   217  O OD1 . ASP   A 1 28 ? 12.383  -8.904  -11.418 1.00 49.57  ? 27  ASP   A OD1 1 
ATOM   218  O OD2 . ASP   A 1 28 ? 13.489  -10.135 -9.953  1.00 51.43  ? 27  ASP   A OD2 1 
ATOM   219  N N   . ILE   A 1 29 ? 10.555  -12.239 -13.918 1.00 32.22  ? 28  ILE   A N   1 
ATOM   220  C CA  . ILE   A 1 29 ? 10.494  -13.152 -15.061 1.00 30.11  ? 28  ILE   A CA  1 
ATOM   221  C C   . ILE   A 1 29 ? 11.803  -12.893 -15.797 1.00 27.10  ? 28  ILE   A C   1 
ATOM   222  O O   . ILE   A 1 29 ? 12.072  -11.735 -16.078 1.00 31.28  ? 28  ILE   A O   1 
ATOM   223  C CB  . ILE   A 1 29 ? 9.303   -12.715 -15.929 1.00 31.60  ? 28  ILE   A CB  1 
ATOM   224  C CG1 . ILE   A 1 29 ? 8.002   -12.849 -15.125 1.00 33.27  ? 28  ILE   A CG1 1 
ATOM   225  C CG2 . ILE   A 1 29 ? 9.243   -13.509 -17.237 1.00 29.40  ? 28  ILE   A CG2 1 
ATOM   226  C CD1 . ILE   A 1 29 ? 6.944   -11.886 -15.569 1.00 31.97  ? 28  ILE   A CD1 1 
ATOM   227  N N   . ALA   A 1 30 ? 12.611  -13.953 -15.971 1.00 29.63  ? 29  ALA   A N   1 
ATOM   228  C CA  . ALA   A 1 30 ? 13.892  -13.876 -16.676 1.00 29.01  ? 29  ALA   A CA  1 
ATOM   229  C C   . ALA   A 1 30 ? 13.646  -13.541 -18.155 1.00 28.13  ? 29  ALA   A C   1 
ATOM   230  O O   . ALA   A 1 30 ? 12.613  -13.882 -18.736 1.00 31.36  ? 29  ALA   A O   1 
ATOM   231  C CB  . ALA   A 1 30 ? 14.572  -15.228 -16.558 1.00 30.79  ? 29  ALA   A CB  1 
ATOM   232  N N   . ASP   A 1 31 ? 14.602  -12.821 -18.764 1.00 28.41  ? 30  ASP   A N   1 
ATOM   233  C CA  . ASP   A 1 31 ? 14.593  -12.667 -20.216 1.00 27.31  ? 30  ASP   A CA  1 
ATOM   234  C C   . ASP   A 1 31 ? 14.410  -14.035 -20.851 1.00 25.66  ? 30  ASP   A C   1 
ATOM   235  O O   . ASP   A 1 31 ? 15.054  -14.982 -20.469 1.00 29.72  ? 30  ASP   A O   1 
ATOM   236  C CB  . ASP   A 1 31 ? 15.935  -12.063 -20.617 1.00 29.44  ? 30  ASP   A CB  1 
ATOM   237  C CG  . ASP   A 1 31 ? 16.063  -10.567 -20.400 1.00 34.68  ? 30  ASP   A CG  1 
ATOM   238  O OD1 . ASP   A 1 31 ? 15.016  -9.938  -20.220 1.00 35.84  ? 30  ASP   A OD1 1 
ATOM   239  O OD2 . ASP   A 1 31 ? 17.234  -10.050 -20.406 1.00 35.16  ? 30  ASP   A OD2 1 
ATOM   240  N N   . GLY   A 1 32 ? 13.494  -14.107 -21.830 1.00 26.38  ? 31  GLY   A N   1 
ATOM   241  C CA  . GLY   A 1 32 ? 13.298  -15.304 -22.625 1.00 28.60  ? 31  GLY   A CA  1 
ATOM   242  C C   . GLY   A 1 32 ? 12.367  -16.328 -21.976 1.00 30.07  ? 31  GLY   A C   1 
ATOM   243  O O   . GLY   A 1 32 ? 12.118  -17.366 -22.561 1.00 33.61  ? 31  GLY   A O   1 
ATOM   244  N N   . ALA   A 1 33 ? 11.967  -16.093 -20.718 1.00 31.20  ? 32  ALA   A N   1 
ATOM   245  C CA  . ALA   A 1 33 ? 11.202  -17.102 -19.999 1.00 29.41  ? 32  ALA   A CA  1 
ATOM   246  C C   . ALA   A 1 33 ? 9.698   -16.864 -20.178 1.00 29.26  ? 32  ALA   A C   1 
ATOM   247  O O   . ALA   A 1 33 ? 9.238   -15.802 -20.584 1.00 28.17  ? 32  ALA   A O   1 
ATOM   248  C CB  . ALA   A 1 33 ? 11.567  -17.047 -18.519 1.00 32.10  ? 32  ALA   A CB  1 
ATOM   249  N N   . VAL   A 1 34 ? 8.908   -17.923 -19.877 1.00 31.00  ? 33  VAL   A N   1 
ATOM   250  C CA  . VAL   A 1 34 ? 7.457   -17.850 -20.005 1.00 32.48  ? 33  VAL   A CA  1 
ATOM   251  C C   . VAL   A 1 34 ? 6.871   -16.825 -19.032 1.00 33.05  ? 33  VAL   A C   1 
ATOM   252  O O   . VAL   A 1 34 ? 7.200   -16.850 -17.846 1.00 32.23  ? 33  VAL   A O   1 
ATOM   253  C CB  . VAL   A 1 34 ? 6.890   -19.250 -19.689 1.00 35.73  ? 33  VAL   A CB  1 
ATOM   254  C CG1 . VAL   A 1 34 ? 5.371   -19.219 -19.590 1.00 38.34  ? 33  VAL   A CG1 1 
ATOM   255  C CG2 . VAL   A 1 34 ? 7.339   -20.250 -20.758 1.00 35.24  ? 33  VAL   A CG2 1 
ATOM   256  N N   . LYS   A 1 35 ? 6.009   -15.956 -19.573 1.00 33.17  ? 34  LYS   A N   1 
ATOM   257  C CA  . LYS   A 1 35 ? 5.342   -14.891 -18.832 1.00 32.86  ? 34  LYS   A CA  1 
ATOM   258  C C   . LYS   A 1 35 ? 4.028   -15.414 -18.250 1.00 35.91  ? 34  LYS   A C   1 
ATOM   259  O O   . LYS   A 1 35 ? 3.450   -16.364 -18.762 1.00 38.61  ? 34  LYS   A O   1 
ATOM   260  C CB  . LYS   A 1 35 ? 4.960   -13.694 -19.697 1.00 34.62  ? 34  LYS   A CB  1 
ATOM   261  C CG  . LYS   A 1 35 ? 6.149   -12.921 -20.257 1.00 33.74  ? 34  LYS   A CG  1 
ATOM   262  C CD  . LYS   A 1 35 ? 5.796   -11.705 -21.112 1.00 44.45  ? 34  LYS   A CD  1 
ATOM   263  C CE  . LYS   A 1 35 ? 5.272   -12.134 -22.458 1.00 42.21  ? 34  LYS   A CE  1 
ATOM   264  N NZ  . LYS   A 1 35 ? 5.149   -10.993 -23.359 1.00 43.54  ? 34  LYS   A NZ  1 
ATOM   265  N N   . PRO   A 1 36 ? 3.477   -14.761 -17.205 1.00 37.80  ? 35  PRO   A N   1 
ATOM   266  C CA  . PRO   A 1 36 ? 2.214   -15.226 -16.626 1.00 33.30  ? 35  PRO   A CA  1 
ATOM   267  C C   . PRO   A 1 36 ? 1.073   -14.710 -17.496 1.00 34.77  ? 35  PRO   A C   1 
ATOM   268  O O   . PRO   A 1 36 ? 1.235   -13.799 -18.299 1.00 34.14  ? 35  PRO   A O   1 
ATOM   269  C CB  . PRO   A 1 36 ? 2.189   -14.566 -15.233 1.00 35.18  ? 35  PRO   A CB  1 
ATOM   270  C CG  . PRO   A 1 36 ? 3.021   -13.296 -15.386 1.00 40.26  ? 35  PRO   A CG  1 
ATOM   271  C CD  . PRO   A 1 36 ? 3.976   -13.518 -16.592 1.00 36.49  ? 35  PRO   A CD  1 
ATOM   272  N N   . PRO   A 1 37 ? -0.157  -15.211 -17.287 1.00 35.52  ? 36  PRO   A N   1 
ATOM   273  C CA  . PRO   A 1 37 ? -1.325  -14.571 -17.898 1.00 41.08  ? 36  PRO   A CA  1 
ATOM   274  C C   . PRO   A 1 37 ? -1.526  -13.130 -17.437 1.00 41.12  ? 36  PRO   A C   1 
ATOM   275  O O   . PRO   A 1 37 ? -1.044  -12.729 -16.378 1.00 34.23  ? 36  PRO   A O   1 
ATOM   276  C CB  . PRO   A 1 37 ? -2.485  -15.474 -17.450 1.00 37.26  ? 36  PRO   A CB  1 
ATOM   277  C CG  . PRO   A 1 37 ? -1.840  -16.797 -17.132 1.00 34.54  ? 36  PRO   A CG  1 
ATOM   278  C CD  . PRO   A 1 37 ? -0.473  -16.440 -16.540 1.00 37.51  ? 36  PRO   A CD  1 
ATOM   279  N N   . PRO   A 1 38 ? -2.296  -12.301 -18.181 1.00 37.35  ? 37  PRO   A N   1 
ATOM   280  C CA  . PRO   A 1 38 ? -2.690  -10.977 -17.699 1.00 37.46  ? 37  PRO   A CA  1 
ATOM   281  C C   . PRO   A 1 38 ? -3.328  -11.009 -16.308 1.00 36.20  ? 37  PRO   A C   1 
ATOM   282  O O   . PRO   A 1 38 ? -4.047  -11.946 -15.964 1.00 41.27  ? 37  PRO   A O   1 
ATOM   283  C CB  . PRO   A 1 38 ? -3.634  -10.423 -18.790 1.00 43.02  ? 37  PRO   A CB  1 
ATOM   284  C CG  . PRO   A 1 38 ? -4.009  -11.645 -19.578 1.00 38.93  ? 37  PRO   A CG  1 
ATOM   285  C CD  . PRO   A 1 38 ? -2.847  -12.612 -19.524 1.00 46.13  ? 37  PRO   A CD  1 
ATOM   286  N N   . ASN   A 1 39 ? -2.972  -9.997  -15.506 1.00 38.24  ? 38  ASN   A N   1 
ATOM   287  C CA  . ASN   A 1 39 ? -3.437  -9.760  -14.155 1.00 38.35  ? 38  ASN   A CA  1 
ATOM   288  C C   . ASN   A 1 39 ? -2.899  -10.791 -13.165 1.00 34.62  ? 38  ASN   A C   1 
ATOM   289  O O   . ASN   A 1 39 ? -3.355  -10.772 -12.015 1.00 34.16  ? 38  ASN   A O   1 
ATOM   290  C CB  . ASN   A 1 39 ? -4.958  -9.650  -14.098 1.00 45.92  ? 38  ASN   A CB  1 
ATOM   291  C CG  . ASN   A 1 39 ? -5.420  -8.424  -14.854 1.00 52.73  ? 38  ASN   A CG  1 
ATOM   292  O OD1 . ASN   A 1 39 ? -5.295  -7.297  -14.356 1.00 49.51  ? 38  ASN   A OD1 1 
ATOM   293  N ND2 . ASN   A 1 39 ? -5.910  -8.629  -16.064 1.00 52.22  ? 38  ASN   A ND2 1 
ATOM   294  N N   . LYS   A 1 40 ? -1.987  -11.689 -13.605 1.00 28.35  ? 39  LYS   A N   1 
ATOM   295  C CA  . LYS   A 1 40 ? -1.431  -12.702 -12.701 1.00 22.09  ? 39  LYS   A CA  1 
ATOM   296  C C   . LYS   A 1 40 ? 0.074   -12.404 -12.500 1.00 22.52  ? 39  LYS   A C   1 
ATOM   297  O O   . LYS   A 1 40 ? 0.712   -11.692 -13.292 1.00 26.58  ? 39  LYS   A O   1 
ATOM   298  C CB  . LYS   A 1 40 ? -1.524  -14.128 -13.235 1.00 26.01  ? 39  LYS   A CB  1 
ATOM   299  C CG  . LYS   A 1 40 ? -2.929  -14.680 -13.576 1.00 29.29  ? 39  LYS   A CG  1 
ATOM   300  C CD  . LYS   A 1 40 ? -3.852  -14.660 -12.364 1.00 31.01  ? 39  LYS   A CD  1 
ATOM   301  C CE  . LYS   A 1 40 ? -5.266  -15.045 -12.817 1.00 33.88  ? 39  LYS   A CE  1 
ATOM   302  N NZ  . LYS   A 1 40 ? -5.409  -16.499 -12.855 1.00 49.22  ? 39  LYS   A NZ  1 
ATOM   303  N N   . TYR   A 1 41 ? 0.582   -12.837 -11.344 1.00 21.05  ? 40  TYR   A N   1 
ATOM   304  C CA  . TYR   A 1 41 ? 1.972   -12.683 -10.959 1.00 22.26  ? 40  TYR   A CA  1 
ATOM   305  C C   . TYR   A 1 41 ? 2.611   -14.061 -10.862 1.00 21.01  ? 40  TYR   A C   1 
ATOM   306  O O   . TYR   A 1 41 ? 1.989   -15.041 -10.446 1.00 21.20  ? 40  TYR   A O   1 
ATOM   307  C CB  . TYR   A 1 41 ? 2.098   -12.088 -9.532  1.00 20.97  ? 40  TYR   A CB  1 
ATOM   308  C CG  . TYR   A 1 41 ? 1.600   -10.653 -9.513  1.00 23.35  ? 40  TYR   A CG  1 
ATOM   309  C CD1 . TYR   A 1 41 ? 0.232   -10.400 -9.410  1.00 26.71  ? 40  TYR   A CD1 1 
ATOM   310  C CD2 . TYR   A 1 41 ? 2.453   -9.566  -9.637  1.00 24.17  ? 40  TYR   A CD2 1 
ATOM   311  C CE1 . TYR   A 1 41 ? -0.267  -9.102  -9.484  1.00 30.39  ? 40  TYR   A CE1 1 
ATOM   312  C CE2 . TYR   A 1 41 ? 1.955   -8.256  -9.716  1.00 25.07  ? 40  TYR   A CE2 1 
ATOM   313  C CZ  . TYR   A 1 41 ? 0.591   -8.028  -9.605  1.00 30.26  ? 40  TYR   A CZ  1 
ATOM   314  O OH  . TYR   A 1 41 ? 0.068   -6.744  -9.754  1.00 30.79  ? 40  TYR   A OH  1 
ATOM   315  N N   . PRO   A 1 42 ? 3.938   -14.186 -11.136 1.00 21.76  ? 41  PRO   A N   1 
ATOM   316  C CA  . PRO   A 1 42 ? 4.625   -15.459 -10.887 1.00 22.37  ? 41  PRO   A CA  1 
ATOM   317  C C   . PRO   A 1 42 ? 4.974   -15.590 -9.417  1.00 21.42  ? 41  PRO   A C   1 
ATOM   318  O O   . PRO   A 1 42 ? 5.654   -14.698 -8.898  1.00 22.45  ? 41  PRO   A O   1 
ATOM   319  C CB  . PRO   A 1 42 ? 5.901   -15.339 -11.732 1.00 23.36  ? 41  PRO   A CB  1 
ATOM   320  C CG  . PRO   A 1 42 ? 6.075   -13.899 -11.985 1.00 24.10  ? 41  PRO   A CG  1 
ATOM   321  C CD  . PRO   A 1 42 ? 4.804   -13.098 -11.642 1.00 23.16  ? 41  PRO   A CD  1 
ATOM   322  N N   . ILE   A 1 43 ? 4.382   -16.592 -8.768  1.00 20.52  ? 42  ILE   A N   1 
ATOM   323  C CA  . ILE   A 1 43 ? 4.587   -16.788 -7.335  1.00 20.16  ? 42  ILE   A CA  1 
ATOM   324  C C   . ILE   A 1 43 ? 5.558   -17.964 -7.137  1.00 22.13  ? 42  ILE   A C   1 
ATOM   325  O O   . ILE   A 1 43 ? 5.298   -19.104 -7.608  1.00 23.25  ? 42  ILE   A O   1 
ATOM   326  C CB  . ILE   A 1 43 ? 3.234   -17.018 -6.636  1.00 21.11  ? 42  ILE   A CB  1 
ATOM   327  C CG1 . ILE   A 1 43 ? 2.260   -15.868 -6.922  1.00 20.40  ? 42  ILE   A CG1 1 
ATOM   328  C CG2 . ILE   A 1 43 ? 3.532   -17.154 -5.126  1.00 20.03  ? 42  ILE   A CG2 1 
ATOM   329  C CD1 . ILE   A 1 43 ? 2.820   -14.484 -6.550  1.00 20.57  ? 42  ILE   A CD1 1 
ATOM   330  N N   . PHE   A 1 44 ? 6.674   -17.709 -6.409  1.00 19.97  ? 43  PHE   A N   1 
ATOM   331  C CA  . PHE   A 1 44 ? 7.610   -18.747 -6.068  1.00 21.71  ? 43  PHE   A CA  1 
ATOM   332  C C   . PHE   A 1 44 ? 7.317   -19.158 -4.630  1.00 22.18  ? 43  PHE   A C   1 
ATOM   333  O O   . PHE   A 1 44 ? 7.369   -18.335 -3.701  1.00 20.10  ? 43  PHE   A O   1 
ATOM   334  C CB  . PHE   A 1 44 ? 9.065   -18.249 -6.285  1.00 21.89  ? 43  PHE   A CB  1 
ATOM   335  C CG  . PHE   A 1 44 ? 10.068  -19.287 -5.833  1.00 22.10  ? 43  PHE   A CG  1 
ATOM   336  C CD1 . PHE   A 1 44 ? 10.422  -20.329 -6.706  1.00 23.32  ? 43  PHE   A CD1 1 
ATOM   337  C CD2 . PHE   A 1 44 ? 10.671  -19.252 -4.565  1.00 22.48  ? 43  PHE   A CD2 1 
ATOM   338  C CE1 . PHE   A 1 44 ? 11.350  -21.279 -6.303  1.00 26.11  ? 43  PHE   A CE1 1 
ATOM   339  C CE2 . PHE   A 1 44 ? 11.602  -20.230 -4.180  1.00 25.31  ? 43  PHE   A CE2 1 
ATOM   340  C CZ  . PHE   A 1 44 ? 11.947  -21.228 -5.073  1.00 26.49  ? 43  PHE   A CZ  1 
ATOM   341  N N   . PHE   A 1 45 ? 6.957   -20.436 -4.479  1.00 19.99  ? 44  PHE   A N   1 
ATOM   342  C CA  . PHE   A 1 45 ? 6.656   -20.974 -3.165  1.00 21.36  ? 44  PHE   A CA  1 
ATOM   343  C C   . PHE   A 1 45 ? 7.895   -21.486 -2.448  1.00 22.09  ? 44  PHE   A C   1 
ATOM   344  O O   . PHE   A 1 45 ? 8.610   -22.358 -2.994  1.00 22.58  ? 44  PHE   A O   1 
ATOM   345  C CB  . PHE   A 1 45 ? 5.653   -22.125 -3.356  1.00 22.06  ? 44  PHE   A CB  1 
ATOM   346  C CG  . PHE   A 1 45 ? 4.263   -21.639 -3.752  1.00 21.79  ? 44  PHE   A CG  1 
ATOM   347  C CD1 . PHE   A 1 45 ? 3.920   -21.464 -5.076  1.00 24.53  ? 44  PHE   A CD1 1 
ATOM   348  C CD2 . PHE   A 1 45 ? 3.276   -21.414 -2.789  1.00 24.45  ? 44  PHE   A CD2 1 
ATOM   349  C CE1 . PHE   A 1 45 ? 2.664   -20.981 -5.437  1.00 26.22  ? 44  PHE   A CE1 1 
ATOM   350  C CE2 . PHE   A 1 45 ? 2.012   -20.963 -3.151  1.00 25.27  ? 44  PHE   A CE2 1 
ATOM   351  C CZ  . PHE   A 1 45 ? 1.717   -20.730 -4.475  1.00 24.10  ? 44  PHE   A CZ  1 
ATOM   352  N N   . PHE   A 1 46 ? 8.174   -20.916 -1.270  1.00 20.32  ? 45  PHE   A N   1 
ATOM   353  C CA  . PHE   A 1 46 ? 9.337   -21.397 -0.513  1.00 20.74  ? 45  PHE   A CA  1 
ATOM   354  C C   . PHE   A 1 46 ? 9.110   -22.855 -0.080  1.00 22.04  ? 45  PHE   A C   1 
ATOM   355  O O   . PHE   A 1 46 ? 7.978   -23.328 0.079   1.00 22.65  ? 45  PHE   A O   1 
ATOM   356  C CB  . PHE   A 1 46 ? 9.552   -20.465 0.693   1.00 21.15  ? 45  PHE   A CB  1 
ATOM   357  C CG  . PHE   A 1 46 ? 10.039  -19.082 0.307   1.00 21.22  ? 45  PHE   A CG  1 
ATOM   358  C CD1 . PHE   A 1 46 ? 11.324  -18.894 -0.221  1.00 20.01  ? 45  PHE   A CD1 1 
ATOM   359  C CD2 . PHE   A 1 46 ? 9.275   -17.956 0.561   1.00 22.13  ? 45  PHE   A CD2 1 
ATOM   360  C CE1 . PHE   A 1 46 ? 11.734  -17.632 -0.642  1.00 18.40  ? 45  PHE   A CE1 1 
ATOM   361  C CE2 . PHE   A 1 46 ? 9.720   -16.683 0.195   1.00 19.28  ? 45  PHE   A CE2 1 
ATOM   362  C CZ  . PHE   A 1 46 ? 10.953  -16.528 -0.382  1.00 19.39  ? 45  PHE   A CZ  1 
ATOM   363  N N   . GLY   A 1 47 ? 10.226  -23.554 0.107   1.00 21.67  ? 46  GLY   A N   1 
ATOM   364  C CA  . GLY   A 1 47 ? 10.167  -24.948 0.576   1.00 21.92  ? 46  GLY   A CA  1 
ATOM   365  C C   . GLY   A 1 47 ? 9.930   -25.927 -0.581  1.00 26.43  ? 46  GLY   A C   1 
ATOM   366  O O   . GLY   A 1 47 ? 10.788  -26.759 -0.881  1.00 29.12  ? 46  GLY   A O   1 
ATOM   367  N N   . THR   A 1 48 ? 8.772   -25.853 -1.252  1.00 26.14  ? 47  THR   A N   1 
ATOM   368  C CA  . THR   A 1 48 ? 8.546   -26.685 -2.433  1.00 26.84  ? 47  THR   A CA  1 
ATOM   369  C C   . THR   A 1 48 ? 9.347   -26.199 -3.641  1.00 27.33  ? 47  THR   A C   1 
ATOM   370  O O   . THR   A 1 48 ? 9.649   -26.977 -4.558  1.00 26.79  ? 47  THR   A O   1 
ATOM   371  C CB  . THR   A 1 48 ? 7.057   -26.732 -2.791  1.00 30.71  ? 47  THR   A CB  1 
ATOM   372  O OG1 . THR   A 1 48 ? 6.673   -25.418 -3.187  1.00 29.81  ? 47  THR   A OG1 1 
ATOM   373  C CG2 . THR   A 1 48 ? 6.131   -27.272 -1.716  1.00 29.01  ? 47  THR   A CG2 1 
ATOM   374  N N   . HIS   A 1 49 ? 9.617   -24.882 -3.698  1.00 24.42  ? 48  HIS   A N   1 
ATOM   375  C CA  . HIS   A 1 49 ? 10.333  -24.293 -4.817  1.00 25.31  ? 48  HIS   A CA  1 
ATOM   376  C C   . HIS   A 1 49 ? 9.528   -24.422 -6.111  1.00 24.82  ? 48  HIS   A C   1 
ATOM   377  O O   . HIS   A 1 49 ? 10.088  -24.399 -7.197  1.00 28.73  ? 48  HIS   A O   1 
ATOM   378  C CB  . HIS   A 1 49 ? 11.790  -24.792 -4.953  1.00 25.00  ? 48  HIS   A CB  1 
ATOM   379  C CG  . HIS   A 1 49 ? 12.502  -24.839 -3.642  1.00 28.04  ? 48  HIS   A CG  1 
ATOM   380  N ND1 . HIS   A 1 49 ? 13.294  -25.901 -3.258  1.00 29.21  ? 48  HIS   A ND1 1 
ATOM   381  C CD2 . HIS   A 1 49 ? 12.560  -23.937 -2.632  1.00 25.77  ? 48  HIS   A CD2 1 
ATOM   382  C CE1 . HIS   A 1 49 ? 13.791  -25.653 -2.052  1.00 32.54  ? 48  HIS   A CE1 1 
ATOM   383  N NE2 . HIS   A 1 49 ? 13.408  -24.435 -1.670  1.00 28.40  ? 48  HIS   A NE2 1 
ATOM   384  N N   . GLU   A 1 50 ? 8.211   -24.454 -5.961  1.00 24.10  ? 49  GLU   A N   1 
ATOM   385  C CA  . GLU   A 1 50 ? 7.345   -24.511 -7.135  1.00 27.30  ? 49  GLU   A CA  1 
ATOM   386  C C   . GLU   A 1 50 ? 6.863   -23.111 -7.519  1.00 28.25  ? 49  GLU   A C   1 
ATOM   387  O O   . GLU   A 1 50 ? 6.980   -22.172 -6.714  1.00 26.48  ? 49  GLU   A O   1 
ATOM   388  C CB  . GLU   A 1 50 ? 6.171   -25.456 -6.912  1.00 30.06  ? 49  GLU   A CB  1 
ATOM   389  C CG  . GLU   A 1 50 ? 6.587   -26.918 -6.743  1.00 36.13  ? 49  GLU   A CG  1 
ATOM   390  C CD  . GLU   A 1 50 ? 5.479   -27.793 -6.180  1.00 46.00  ? 49  GLU   A CD  1 
ATOM   391  O OE1 . GLU   A 1 50 ? 4.326   -27.337 -6.044  1.00 45.73  ? 49  GLU   A OE1 1 
ATOM   392  O OE2 . GLU   A 1 50 ? 5.800   -28.956 -5.844  1.00 49.36  ? 49  GLU   A OE2 1 
ATOM   393  N N   . THR   A 1 51 ? 6.394   -22.938 -8.768  1.00 25.05  ? 50  THR   A N   1 
ATOM   394  C CA  . THR   A 1 51 ? 5.884   -21.668 -9.241  1.00 24.77  ? 50  THR   A CA  1 
ATOM   395  C C   . THR   A 1 51 ? 4.438   -21.873 -9.676  1.00 26.09  ? 50  THR   A C   1 
ATOM   396  O O   . THR   A 1 51 ? 4.107   -22.882 -10.313 1.00 26.79  ? 50  THR   A O   1 
ATOM   397  C CB  . THR   A 1 51 ? 6.704   -21.140 -10.417 1.00 27.88  ? 50  THR   A CB  1 
ATOM   398  O OG1 . THR   A 1 51 ? 8.016   -20.776 -10.001 1.00 28.42  ? 50  THR   A OG1 1 
ATOM   399  C CG2 . THR   A 1 51 ? 6.122   -19.878 -11.049 1.00 28.64  ? 50  THR   A CG2 1 
ATOM   400  N N   . ALA   A 1 52 ? 3.557   -20.951 -9.299  1.00 23.09  ? 51  ALA   A N   1 
ATOM   401  C CA  . ALA   A 1 52 ? 2.205   -20.882 -9.841  1.00 24.30  ? 51  ALA   A CA  1 
ATOM   402  C C   . ALA   A 1 52 ? 1.871   -19.428 -10.152 1.00 23.89  ? 51  ALA   A C   1 
ATOM   403  O O   . ALA   A 1 52 ? 2.577   -18.492 -9.719  1.00 24.35  ? 51  ALA   A O   1 
ATOM   404  C CB  . ALA   A 1 52 ? 1.240   -21.469 -8.858  1.00 25.31  ? 51  ALA   A CB  1 
ATOM   405  N N   . PHE   A 1 53 ? 0.793   -19.187 -10.909 1.00 22.59  ? 52  PHE   A N   1 
ATOM   406  C CA  . PHE   A 1 53 ? 0.442   -17.836 -11.293 1.00 23.21  ? 52  PHE   A CA  1 
ATOM   407  C C   . PHE   A 1 53 ? -0.825  -17.443 -10.552 1.00 26.20  ? 52  PHE   A C   1 
ATOM   408  O O   . PHE   A 1 53 ? -1.827  -18.164 -10.591 1.00 30.24  ? 52  PHE   A O   1 
ATOM   409  C CB  . PHE   A 1 53 ? 0.112   -17.840 -12.784 1.00 26.64  ? 52  PHE   A CB  1 
ATOM   410  C CG  . PHE   A 1 53 ? 1.284   -18.218 -13.654 1.00 28.91  ? 52  PHE   A CG  1 
ATOM   411  C CD1 . PHE   A 1 53 ? 2.466   -17.485 -13.626 1.00 34.54  ? 52  PHE   A CD1 1 
ATOM   412  C CD2 . PHE   A 1 53 ? 1.172   -19.284 -14.541 1.00 33.16  ? 52  PHE   A CD2 1 
ATOM   413  C CE1 . PHE   A 1 53 ? 3.548   -17.817 -14.446 1.00 40.58  ? 52  PHE   A CE1 1 
ATOM   414  C CE2 . PHE   A 1 53 ? 2.255   -19.610 -15.346 1.00 34.33  ? 52  PHE   A CE2 1 
ATOM   415  C CZ  . PHE   A 1 53 ? 3.424   -18.875 -15.325 1.00 35.61  ? 52  PHE   A CZ  1 
ATOM   416  N N   . LEU   A 1 54 ? -0.761  -16.343 -9.778  1.00 20.73  ? 53  LEU   A N   1 
ATOM   417  C CA  . LEU   A 1 54 ? -1.877  -16.007 -8.909  1.00 20.81  ? 53  LEU   A CA  1 
ATOM   418  C C   . LEU   A 1 54 ? -2.142  -14.510 -9.011  1.00 22.07  ? 53  LEU   A C   1 
ATOM   419  O O   . LEU   A 1 54 ? -1.263  -13.716 -9.349  1.00 23.20  ? 53  LEU   A O   1 
ATOM   420  C CB  . LEU   A 1 54 ? -1.526  -16.310 -7.449  1.00 23.29  ? 53  LEU   A CB  1 
ATOM   421  C CG  . LEU   A 1 54 ? -1.476  -17.784 -7.071  1.00 24.44  ? 53  LEU   A CG  1 
ATOM   422  C CD1 . LEU   A 1 54 ? -1.085  -17.883 -5.603  1.00 24.21  ? 53  LEU   A CD1 1 
ATOM   423  C CD2 . LEU   A 1 54 ? -2.892  -18.377 -7.241  1.00 28.74  ? 53  LEU   A CD2 1 
ATOM   424  N N   . GLY   A 1 55 ? -3.396  -14.119 -8.694  1.00 20.42  ? 54  GLY   A N   1 
ATOM   425  C CA  . GLY   A 1 55 ? -3.727  -12.705 -8.632  1.00 20.40  ? 54  GLY   A CA  1 
ATOM   426  C C   . GLY   A 1 55 ? -3.747  -12.245 -7.170  1.00 17.37  ? 54  GLY   A C   1 
ATOM   427  O O   . GLY   A 1 55 ? -3.700  -13.076 -6.251  1.00 18.84  ? 54  GLY   A O   1 
ATOM   428  N N   . PRO   A 1 56 ? -3.867  -10.926 -6.988  1.00 19.85  ? 55  PRO   A N   1 
ATOM   429  C CA  . PRO   A 1 56 ? -3.782  -10.303 -5.662  1.00 19.73  ? 55  PRO   A CA  1 
ATOM   430  C C   . PRO   A 1 56 ? -4.764  -10.827 -4.628  1.00 19.60  ? 55  PRO   A C   1 
ATOM   431  O O   . PRO   A 1 56 ? -4.471  -10.804 -3.442  1.00 20.68  ? 55  PRO   A O   1 
ATOM   432  C CB  . PRO   A 1 56 ? -4.054  -8.843  -5.974  1.00 22.07  ? 55  PRO   A CB  1 
ATOM   433  C CG  . PRO   A 1 56 ? -3.465  -8.674  -7.366  1.00 22.74  ? 55  PRO   A CG  1 
ATOM   434  C CD  . PRO   A 1 56 ? -3.849  -9.958  -8.097  1.00 20.87  ? 55  PRO   A CD  1 
ATOM   435  N N   . LYS   A 1 57 ? -5.934  -11.330 -5.088  1.00 21.57  ? 56  LYS   A N   1 
ATOM   436  C CA  . LYS   A 1 57 ? -6.884  -11.877 -4.113  1.00 20.97  ? 56  LYS   A CA  1 
ATOM   437  C C   . LYS   A 1 57 ? -6.325  -13.030 -3.283  1.00 20.28  ? 56  LYS   A C   1 
ATOM   438  O O   . LYS   A 1 57 ? -6.792  -13.295 -2.184  1.00 21.95  ? 56  LYS   A O   1 
ATOM   439  C CB  . LYS   A 1 57 ? -8.161  -12.363 -4.828  1.00 24.14  ? 56  LYS   A CB  1 
ATOM   440  C CG  . LYS   A 1 57 ? -8.026  -13.649 -5.603  1.00 27.59  ? 56  LYS   A CG  1 
ATOM   441  C CD  . LYS   A 1 57 ? -9.406  -14.140 -6.063  1.00 31.99  ? 56  LYS   A CD  1 
ATOM   442  C CE  . LYS   A 1 57 ? -9.312  -15.362 -6.919  1.00 34.64  ? 56  LYS   A CE  1 
ATOM   443  N NZ  . LYS   A 1 57 ? -9.098  -16.565 -6.117  1.00 42.18  ? 56  LYS   A NZ  1 
ATOM   444  N N   . ASP   A 1 58 ? -5.254  -13.727 -3.781  1.00 19.11  ? 57  ASP   A N   1 
ATOM   445  C CA  . ASP   A 1 58 ? -4.695  -14.879 -3.110  1.00 19.99  ? 57  ASP   A CA  1 
ATOM   446  C C   . ASP   A 1 58 ? -3.335  -14.526 -2.478  1.00 19.00  ? 57  ASP   A C   1 
ATOM   447  O O   . ASP   A 1 58 ? -2.612  -15.442 -2.057  1.00 21.73  ? 57  ASP   A O   1 
ATOM   448  C CB  . ASP   A 1 58 ? -4.618  -16.054 -4.091  1.00 21.17  ? 57  ASP   A CB  1 
ATOM   449  C CG  . ASP   A 1 58 ? -6.015  -16.575 -4.418  1.00 24.17  ? 57  ASP   A CG  1 
ATOM   450  O OD1 . ASP   A 1 58 ? -6.818  -16.679 -3.437  1.00 27.04  ? 57  ASP   A OD1 1 
ATOM   451  O OD2 . ASP   A 1 58 ? -6.236  -16.956 -5.560  1.00 27.34  ? 57  ASP   A OD2 1 
ATOM   452  N N   . LEU   A 1 59 ? -3.006  -13.210 -2.449  1.00 19.14  ? 58  LEU   A N   1 
ATOM   453  C CA  . LEU   A 1 59 ? -1.658  -12.789 -1.980  1.00 17.51  ? 58  LEU   A CA  1 
ATOM   454  C C   . LEU   A 1 59 ? -1.771  -11.909 -0.729  1.00 16.15  ? 58  LEU   A C   1 
ATOM   455  O O   . LEU   A 1 59 ? -2.399  -10.833 -0.716  1.00 19.14  ? 58  LEU   A O   1 
ATOM   456  C CB  . LEU   A 1 59 ? -0.899  -12.060 -3.090  1.00 18.61  ? 58  LEU   A CB  1 
ATOM   457  C CG  . LEU   A 1 59 ? -0.802  -12.877 -4.379  1.00 18.64  ? 58  LEU   A CG  1 
ATOM   458  C CD1 . LEU   A 1 59 ? -0.128  -11.981 -5.426  1.00 21.66  ? 58  LEU   A CD1 1 
ATOM   459  C CD2 . LEU   A 1 59 ? 0.003   -14.153 -4.252  1.00 21.92  ? 58  LEU   A CD2 1 
ATOM   460  N N   . PHE   A 1 60 ? -1.221  -12.431 0.376   1.00 18.26  ? 59  PHE   A N   1 
ATOM   461  C CA  . PHE   A 1 60 ? -1.318  -11.744 1.679   1.00 18.96  ? 59  PHE   A CA  1 
ATOM   462  C C   . PHE   A 1 60 ? 0.059   -11.238 2.103   1.00 20.58  ? 59  PHE   A C   1 
ATOM   463  O O   . PHE   A 1 60 ? 1.004   -12.029 2.291   1.00 22.73  ? 59  PHE   A O   1 
ATOM   464  C CB  . PHE   A 1 60 ? -1.800  -12.793 2.704   1.00 18.88  ? 59  PHE   A CB  1 
ATOM   465  C CG  . PHE   A 1 60 ? -3.250  -13.210 2.465   1.00 19.90  ? 59  PHE   A CG  1 
ATOM   466  C CD1 . PHE   A 1 60 ? -3.539  -14.119 1.461   1.00 21.93  ? 59  PHE   A CD1 1 
ATOM   467  C CD2 . PHE   A 1 60 ? -4.278  -12.685 3.275   1.00 21.09  ? 59  PHE   A CD2 1 
ATOM   468  C CE1 . PHE   A 1 60 ? -4.874  -14.480 1.191   1.00 24.93  ? 59  PHE   A CE1 1 
ATOM   469  C CE2 . PHE   A 1 60 ? -5.587  -13.041 2.954   1.00 20.98  ? 59  PHE   A CE2 1 
ATOM   470  C CZ  . PHE   A 1 60 ? -5.857  -13.955 1.967   1.00 23.87  ? 59  PHE   A CZ  1 
ATOM   471  N N   . PRO   A 1 61 ? 0.304   -9.923  2.202   1.00 23.02  ? 60  PRO   A N   1 
ATOM   472  C CA  . PRO   A 1 61 ? 1.671   -9.459  2.520   1.00 21.29  ? 60  PRO   A CA  1 
ATOM   473  C C   . PRO   A 1 61 ? 2.212   -10.041 3.815   1.00 20.74  ? 60  PRO   A C   1 
ATOM   474  O O   . PRO   A 1 61 ? 1.485   -10.254 4.802   1.00 22.77  ? 60  PRO   A O   1 
ATOM   475  C CB  . PRO   A 1 61 ? 1.431   -7.955  2.662   1.00 24.30  ? 60  PRO   A CB  1 
ATOM   476  C CG  . PRO   A 1 61 ? 0.405   -7.651  1.545   1.00 25.19  ? 60  PRO   A CG  1 
ATOM   477  C CD  . PRO   A 1 61 ? -0.598  -8.813  1.811   1.00 22.93  ? 60  PRO   A CD  1 
ATOM   478  N N   . TYR   A 1 62 ? 3.514   -10.455 3.796   1.00 22.71  ? 61  TYR   A N   1 
ATOM   479  C CA  . TYR   A 1 62 ? 4.050   -11.331 4.822   1.00 20.16  ? 61  TYR   A CA  1 
ATOM   480  C C   . TYR   A 1 62 ? 4.090   -10.659 6.207   1.00 19.55  ? 61  TYR   A C   1 
ATOM   481  O O   . TYR   A 1 62 ? 3.732   -11.362 7.164   1.00 23.19  ? 61  TYR   A O   1 
ATOM   482  C CB  . TYR   A 1 62 ? 5.464   -11.723 4.327   1.00 22.20  ? 61  TYR   A CB  1 
ATOM   483  C CG  . TYR   A 1 62 ? 6.264   -12.503 5.356   1.00 23.84  ? 61  TYR   A CG  1 
ATOM   484  C CD1 . TYR   A 1 62 ? 5.984   -13.843 5.614   1.00 22.53  ? 61  TYR   A CD1 1 
ATOM   485  C CD2 . TYR   A 1 62 ? 7.293   -11.884 6.055   1.00 26.26  ? 61  TYR   A CD2 1 
ATOM   486  C CE1 . TYR   A 1 62 ? 6.635   -14.575 6.607   1.00 24.48  ? 61  TYR   A CE1 1 
ATOM   487  C CE2 . TYR   A 1 62 ? 7.969   -12.618 7.022   1.00 26.08  ? 61  TYR   A CE2 1 
ATOM   488  C CZ  . TYR   A 1 62 ? 7.668   -13.940 7.270   1.00 25.64  ? 61  TYR   A CZ  1 
ATOM   489  O OH  . TYR   A 1 62 ? 8.417   -14.663 8.207   1.00 27.39  ? 61  TYR   A OH  1 
ATOM   490  N N   . ASP   A 1 63 ? 4.440   -9.367  6.224   1.00 24.79  ? 62  ASP   A N   1 
ATOM   491  C CA  . ASP   A 1 63 ? 4.595   -8.670  7.501   1.00 28.72  ? 62  ASP   A CA  1 
ATOM   492  C C   . ASP   A 1 63 ? 3.270   -8.651  8.254   1.00 25.23  ? 62  ASP   A C   1 
ATOM   493  O O   . ASP   A 1 63 ? 3.234   -9.147  9.385   1.00 31.77  ? 62  ASP   A O   1 
ATOM   494  C CB  . ASP   A 1 63 ? 5.318   -7.344  7.402   1.00 32.92  ? 62  ASP   A CB  1 
ATOM   495  C CG  . ASP   A 1 63 ? 5.667   -6.804  8.780   1.00 51.15  ? 62  ASP   A CG  1 
ATOM   496  O OD1 . ASP   A 1 63 ? 5.241   -5.664  9.090   1.00 61.44  ? 62  ASP   A OD1 1 
ATOM   497  O OD2 . ASP   A 1 63 ? 6.323   -7.554  9.554   1.00 52.07  ? 62  ASP   A OD2 1 
ATOM   498  N N   . LYS   A 1 64 ? 2.211   -8.205  7.540   1.00 26.23  ? 63  LYS   A N   1 
ATOM   499  C CA  . LYS   A 1 64 ? 0.876   -8.188  8.138   1.00 27.36  ? 63  LYS   A CA  1 
ATOM   500  C C   . LYS   A 1 64 ? 0.390   -9.573  8.580   1.00 30.12  ? 63  LYS   A C   1 
ATOM   501  O O   . LYS   A 1 64 ? -0.323  -9.671  9.588   1.00 28.47  ? 63  LYS   A O   1 
ATOM   502  C CB  . LYS   A 1 64 ? -0.053  -7.561  7.095   1.00 27.19  ? 63  LYS   A CB  1 
ATOM   503  C CG  . LYS   A 1 64 ? -1.487  -7.432  7.616   1.00 32.55  ? 63  LYS   A CG  1 
ATOM   504  C CD  . LYS   A 1 64 ? -2.213  -6.658  6.532   1.00 33.27  ? 63  LYS   A CD  1 
ATOM   505  C CE  . LYS   A 1 64 ? -3.373  -5.928  7.118   1.00 36.72  ? 63  LYS   A CE  1 
ATOM   506  N NZ  . LYS   A 1 64 ? -4.441  -6.869  7.422   1.00 43.22  ? 63  LYS   A NZ  1 
ATOM   507  N N   . SER   A 1 65 ? 0.733   -10.664 7.857   1.00 25.98  ? 64  SER   A N   1 
ATOM   508  C CA  . SER   A 1 65 ? 0.039   -11.942 7.961   1.00 25.03  ? 64  SER   A CA  1 
ATOM   509  C C   . SER   A 1 65 ? 0.799   -13.030 8.738   1.00 25.21  ? 64  SER   A C   1 
ATOM   510  O O   . SER   A 1 65 ? 0.267   -14.128 8.955   1.00 27.56  ? 64  SER   A O   1 
ATOM   511  C CB  . SER   A 1 65 ? -0.275  -12.504 6.560   1.00 28.31  ? 64  SER   A CB  1 
ATOM   512  O OG  . SER   A 1 65 ? -1.129  -11.572 5.904   1.00 35.06  ? 64  SER   A OG  1 
ATOM   513  N N   . LYS   A 1 66 ? 2.073   -12.774 9.072   1.00 26.32  ? 65  LYS   A N   1 
ATOM   514  C CA  . LYS   A 1 66 ? 2.904   -13.850 9.575   1.00 27.87  ? 65  LYS   A CA  1 
ATOM   515  C C   . LYS   A 1 66 ? 2.425   -14.363 10.929  1.00 26.96  ? 65  LYS   A C   1 
ATOM   516  O O   . LYS   A 1 66 ? 2.555   -15.549 11.225  1.00 29.20  ? 65  LYS   A O   1 
ATOM   517  C CB  . LYS   A 1 66 ? 4.386   -13.474 9.594   1.00 27.57  ? 65  LYS   A CB  1 
ATOM   518  C CG  . LYS   A 1 66 ? 4.725   -12.294 10.471  1.00 28.22  ? 65  LYS   A CG  1 
ATOM   519  C CD  . LYS   A 1 66 ? 6.218   -12.049 10.248  1.00 35.59  ? 65  LYS   A CD  1 
ATOM   520  C CE  . LYS   A 1 66 ? 6.653   -11.127 11.343  1.00 42.03  ? 65  LYS   A CE  1 
ATOM   521  N NZ  . LYS   A 1 66 ? 5.894   -9.881  11.217  1.00 52.17  ? 65  LYS   A NZ  1 
ATOM   522  N N   A ASP   A 1 67 ? 1.857   -13.474 11.751  0.50 30.47  ? 66  ASP   A N   1 
ATOM   523  N N   B ASP   A 1 67 ? 1.903   -13.456 11.767  0.50 29.72  ? 66  ASP   A N   1 
ATOM   524  C CA  A ASP   A 1 67 ? 1.415   -13.922 13.063  0.50 31.21  ? 66  ASP   A CA  1 
ATOM   525  C CA  B ASP   A 1 67 ? 1.365   -13.879 13.052  0.50 30.72  ? 66  ASP   A CA  1 
ATOM   526  C C   A ASP   A 1 67 ? 0.272   -14.932 12.956  0.50 31.68  ? 66  ASP   A C   1 
ATOM   527  C C   B ASP   A 1 67 ? 0.375   -15.022 12.848  0.50 30.95  ? 66  ASP   A C   1 
ATOM   528  O O   A ASP   A 1 67 ? 0.126   -15.796 13.811  0.50 32.96  ? 66  ASP   A O   1 
ATOM   529  O O   B ASP   A 1 67 ? 0.454   -16.063 13.499  0.50 32.91  ? 66  ASP   A O   1 
ATOM   530  C CB  A ASP   A 1 67 ? 1.063   -12.741 13.955  0.50 32.62  ? 66  ASP   A CB  1 
ATOM   531  C CB  B ASP   A 1 67 ? 0.637   -12.728 13.731  0.50 30.37  ? 66  ASP   A CB  1 
ATOM   532  C CG  A ASP   A 1 67 ? 2.231   -11.946 14.523  0.50 38.11  ? 66  ASP   A CG  1 
ATOM   533  C CG  B ASP   A 1 67 ? 0.207   -12.948 15.177  0.50 36.60  ? 66  ASP   A CG  1 
ATOM   534  O OD1 A ASP   A 1 67 ? 3.398   -12.373 14.336  0.50 39.78  ? 66  ASP   A OD1 1 
ATOM   535  O OD1 B ASP   A 1 67 ? 1.047   -12.739 16.084  0.50 39.69  ? 66  ASP   A OD1 1 
ATOM   536  O OD2 A ASP   A 1 67 ? 1.965   -10.892 15.146  0.50 39.86  ? 66  ASP   A OD2 1 
ATOM   537  O OD2 B ASP   A 1 67 ? -0.962  -13.336 15.383  0.50 41.22  ? 66  ASP   A OD2 1 
ATOM   538  N N   . LYS   A 1 68 ? -0.560  -14.814 11.915  1.00 29.80  ? 67  LYS   A N   1 
ATOM   539  C CA  . LYS   A 1 68 ? -1.609  -15.773 11.674  1.00 27.43  ? 67  LYS   A CA  1 
ATOM   540  C C   . LYS   A 1 68 ? -1.103  -16.996 10.919  1.00 29.96  ? 67  LYS   A C   1 
ATOM   541  O O   . LYS   A 1 68 ? -1.507  -18.122 11.228  1.00 34.65  ? 67  LYS   A O   1 
ATOM   542  C CB  . LYS   A 1 68 ? -2.688  -15.045 10.875  1.00 28.89  ? 67  LYS   A CB  1 
ATOM   543  C CG  . LYS   A 1 68 ? -3.930  -15.850 10.641  1.00 32.68  ? 67  LYS   A CG  1 
ATOM   544  C CD  . LYS   A 1 68 ? -4.974  -14.876 10.089  1.00 37.82  ? 67  LYS   A CD  1 
ATOM   545  C CE  . LYS   A 1 68 ? -6.352  -15.445 9.992   1.00 41.53  ? 67  LYS   A CE  1 
ATOM   546  N NZ  . LYS   A 1 68 ? -7.190  -14.426 9.337   1.00 45.39  ? 67  LYS   A NZ  1 
ATOM   547  N N   . TYR   A 1 69 ? -0.269  -16.784 9.879   1.00 26.36  ? 68  TYR   A N   1 
ATOM   548  C CA  . TYR   A 1 69 ? -0.043  -17.876 8.944   1.00 25.68  ? 68  TYR   A CA  1 
ATOM   549  C C   . TYR   A 1 69 ? 1.334   -18.524 9.089   1.00 24.77  ? 68  TYR   A C   1 
ATOM   550  O O   . TYR   A 1 69 ? 1.563   -19.605 8.551   1.00 28.22  ? 68  TYR   A O   1 
ATOM   551  C CB  . TYR   A 1 69 ? -0.208  -17.359 7.507   1.00 23.91  ? 68  TYR   A CB  1 
ATOM   552  C CG  . TYR   A 1 69 ? -1.614  -16.962 7.109   1.00 26.25  ? 68  TYR   A CG  1 
ATOM   553  C CD1 . TYR   A 1 69 ? -2.736  -17.693 7.513   1.00 27.41  ? 68  TYR   A CD1 1 
ATOM   554  C CD2 . TYR   A 1 69 ? -1.793  -15.755 6.449   1.00 26.35  ? 68  TYR   A CD2 1 
ATOM   555  C CE1 . TYR   A 1 69 ? -4.004  -17.283 7.142   1.00 29.49  ? 68  TYR   A CE1 1 
ATOM   556  C CE2 . TYR   A 1 69 ? -3.058  -15.348 6.046   1.00 29.11  ? 68  TYR   A CE2 1 
ATOM   557  C CZ  . TYR   A 1 69 ? -4.162  -16.111 6.408   1.00 29.63  ? 68  TYR   A CZ  1 
ATOM   558  O OH  . TYR   A 1 69 ? -5.395  -15.694 6.011   1.00 28.68  ? 68  TYR   A OH  1 
ATOM   559  N N   . GLY   A 1 70 ? 2.227   -17.908 9.868   1.00 24.83  ? 69  GLY   A N   1 
ATOM   560  C CA  . GLY   A 1 70 ? 3.624   -18.314 9.936   1.00 26.49  ? 69  GLY   A CA  1 
ATOM   561  C C   . GLY   A 1 70 ? 3.856   -19.285 11.093  1.00 29.18  ? 69  GLY   A C   1 
ATOM   562  O O   . GLY   A 1 70 ? 4.609   -18.975 11.990  1.00 35.77  ? 69  GLY   A O   1 
ATOM   563  N N   . LYS   A 1 71 ? 3.142   -20.399 11.055  1.00 32.00  ? 70  LYS   A N   1 
ATOM   564  C CA  . LYS   A 1 71 ? 3.244   -21.432 12.084  1.00 35.70  ? 70  LYS   A CA  1 
ATOM   565  C C   . LYS   A 1 71 ? 3.499   -22.764 11.385  1.00 30.83  ? 70  LYS   A C   1 
ATOM   566  O O   . LYS   A 1 71 ? 3.074   -22.982 10.257  1.00 32.86  ? 70  LYS   A O   1 
ATOM   567  C CB  . LYS   A 1 71 ? 1.960   -21.411 12.930  1.00 37.73  ? 70  LYS   A CB  1 
ATOM   568  C CG  . LYS   A 1 71 ? 1.875   -20.238 13.906  1.00 40.38  ? 70  LYS   A CG  1 
ATOM   569  C CD  . LYS   A 1 71 ? 0.503   -19.896 14.483  1.00 43.50  ? 70  LYS   A CD  1 
ATOM   570  N N   . PRO   A 1 72 ? 4.225   -23.732 12.008  1.00 32.49  ? 71  PRO   A N   1 
ATOM   571  C CA  . PRO   A 1 72 ? 4.487   -25.003 11.333  1.00 31.06  ? 71  PRO   A CA  1 
ATOM   572  C C   . PRO   A 1 72 ? 3.269   -25.748 10.821  1.00 29.48  ? 71  PRO   A C   1 
ATOM   573  O O   . PRO   A 1 72 ? 2.191   -25.691 11.425  1.00 38.23  ? 71  PRO   A O   1 
ATOM   574  C CB  . PRO   A 1 72 ? 5.281   -25.843 12.348  1.00 33.96  ? 71  PRO   A CB  1 
ATOM   575  C CG  . PRO   A 1 72 ? 5.801   -24.829 13.343  1.00 40.36  ? 71  PRO   A CG  1 
ATOM   576  C CD  . PRO   A 1 72 ? 4.830   -23.624 13.343  1.00 37.07  ? 71  PRO   A CD  1 
ATOM   577  N N   . ASN   A 1 73 ? 3.459   -26.511 9.755   1.00 34.56  ? 72  ASN   A N   1 
ATOM   578  C CA  . ASN   A 1 73 ? 2.364   -27.219 9.128   1.00 38.10  ? 72  ASN   A CA  1 
ATOM   579  C C   . ASN   A 1 73 ? 2.919   -28.555 8.664   1.00 42.05  ? 72  ASN   A C   1 
ATOM   580  O O   . ASN   A 1 73 ? 4.091   -28.680 8.315   1.00 43.07  ? 72  ASN   A O   1 
ATOM   581  C CB  . ASN   A 1 73 ? 1.798   -26.422 7.945   1.00 39.82  ? 72  ASN   A CB  1 
ATOM   582  C CG  . ASN   A 1 73 ? 0.473   -26.919 7.397   1.00 46.65  ? 72  ASN   A CG  1 
ATOM   583  O OD1 . ASN   A 1 73 ? 0.432   -27.811 6.541   1.00 44.38  ? 72  ASN   A OD1 1 
ATOM   584  N ND2 . ASN   A 1 73 ? -0.631  -26.288 7.781   1.00 43.48  ? 72  ASN   A ND2 1 
ATOM   585  N N   . LYS   A 1 74 ? 2.042   -29.553 8.648   1.00 43.91  ? 73  LYS   A N   1 
ATOM   586  C CA  . LYS   A 1 74 ? 2.445   -30.906 8.342   1.00 42.67  ? 73  LYS   A CA  1 
ATOM   587  C C   . LYS   A 1 74 ? 2.747   -31.088 6.853   1.00 43.01  ? 73  LYS   A C   1 
ATOM   588  O O   . LYS   A 1 74 ? 3.346   -32.088 6.466   1.00 41.70  ? 73  LYS   A O   1 
ATOM   589  C CB  . LYS   A 1 74 ? 1.339   -31.821 8.902   1.00 48.25  ? 73  LYS   A CB  1 
ATOM   590  C CG  . LYS   A 1 74 ? 0.078   -32.007 8.043   1.00 53.03  ? 73  LYS   A CG  1 
ATOM   591  N N   . ARG   A 1 75 ? 2.349   -30.142 5.990   1.00 36.39  ? 74  ARG   A N   1 
ATOM   592  C CA  . ARG   A 1 75 ? 2.448   -30.411 4.565   1.00 41.47  ? 74  ARG   A CA  1 
ATOM   593  C C   . ARG   A 1 75 ? 3.900   -30.337 4.088   1.00 34.44  ? 74  ARG   A C   1 
ATOM   594  O O   . ARG   A 1 75 ? 4.669   -29.525 4.593   1.00 32.34  ? 74  ARG   A O   1 
ATOM   595  C CB  . ARG   A 1 75 ? 1.585   -29.449 3.739   1.00 39.86  ? 74  ARG   A CB  1 
ATOM   596  C CG  . ARG   A 1 75 ? 0.126   -29.624 4.130   1.00 51.04  ? 74  ARG   A CG  1 
ATOM   597  C CD  . ARG   A 1 75 ? -0.566  -30.780 3.431   1.00 46.79  ? 74  ARG   A CD  1 
ATOM   598  N NE  . ARG   A 1 75 ? -1.351  -30.306 2.287   1.00 61.22  ? 74  ARG   A NE  1 
ATOM   599  C CZ  . ARG   A 1 75 ? -2.485  -29.604 2.372   1.00 56.65  ? 74  ARG   A CZ  1 
ATOM   600  N NH1 . ARG   A 1 75 ? -3.101  -29.257 1.262   1.00 59.13  ? 74  ARG   A NH1 1 
ATOM   601  N NH2 . ARG   A 1 75 ? -3.007  -29.278 3.548   1.00 59.47  ? 74  ARG   A NH2 1 
ATOM   602  N N   . LYS   A 1 76 ? 4.198   -31.174 3.097   1.00 31.60  ? 75  LYS   A N   1 
ATOM   603  C CA  . LYS   A 1 76 ? 5.538   -31.338 2.546   1.00 32.14  ? 75  LYS   A CA  1 
ATOM   604  C C   . LYS   A 1 76 ? 6.098   -29.973 2.137   1.00 32.20  ? 75  LYS   A C   1 
ATOM   605  O O   . LYS   A 1 76 ? 5.503   -29.286 1.313   1.00 31.22  ? 75  LYS   A O   1 
ATOM   606  C CB  . LYS   A 1 76 ? 5.554   -32.324 1.375   1.00 37.96  ? 75  LYS   A CB  1 
ATOM   607  C CG  . LYS   A 1 76 ? 6.901   -32.551 0.718   1.00 43.88  ? 75  LYS   A CG  1 
ATOM   608  C CD  . LYS   A 1 76 ? 6.929   -33.696 -0.293  1.00 50.39  ? 75  LYS   A CD  1 
ATOM   609  C CE  . LYS   A 1 76 ? 8.341   -33.950 -0.749  1.00 54.67  ? 75  LYS   A CE  1 
ATOM   610  N N   . GLY   A 1 77 ? 7.281   -29.643 2.662   1.00 30.14  ? 76  GLY   A N   1 
ATOM   611  C CA  . GLY   A 1 77 ? 7.992   -28.445 2.239   1.00 30.39  ? 76  GLY   A CA  1 
ATOM   612  C C   . GLY   A 1 77 ? 7.676   -27.206 3.070   1.00 27.36  ? 76  GLY   A C   1 
ATOM   613  O O   . GLY   A 1 77 ? 8.439   -26.232 3.024   1.00 27.04  ? 76  GLY   A O   1 
ATOM   614  N N   . PHE   A 1 78 ? 6.590   -27.227 3.826   1.00 27.39  ? 77  PHE   A N   1 
ATOM   615  C CA  . PHE   A 1 78 ? 6.108   -26.008 4.446   1.00 26.07  ? 77  PHE   A CA  1 
ATOM   616  C C   . PHE   A 1 78 ? 7.115   -25.440 5.455   1.00 29.35  ? 77  PHE   A C   1 
ATOM   617  O O   . PHE   A 1 78 ? 7.386   -24.232 5.498   1.00 27.65  ? 77  PHE   A O   1 
ATOM   618  C CB  . PHE   A 1 78 ? 4.735   -26.336 5.037   1.00 28.70  ? 77  PHE   A CB  1 
ATOM   619  C CG  . PHE   A 1 78 ? 4.023   -25.058 5.451   1.00 29.71  ? 77  PHE   A CG  1 
ATOM   620  C CD1 . PHE   A 1 78 ? 4.316   -24.433 6.653   1.00 29.34  ? 77  PHE   A CD1 1 
ATOM   621  C CD2 . PHE   A 1 78 ? 3.046   -24.479 4.620   1.00 30.67  ? 77  PHE   A CD2 1 
ATOM   622  C CE1 . PHE   A 1 78 ? 3.668   -23.259 7.025   1.00 27.61  ? 77  PHE   A CE1 1 
ATOM   623  C CE2 . PHE   A 1 78 ? 2.382   -23.304 5.010   1.00 24.29  ? 77  PHE   A CE2 1 
ATOM   624  C CZ  . PHE   A 1 78 ? 2.695   -22.689 6.203   1.00 24.73  ? 77  PHE   A CZ  1 
ATOM   625  N N   . ASN   A 1 79 ? 7.652   -26.300 6.332   1.00 29.39  ? 78  ASN   A N   1 
ATOM   626  C CA  . ASN   A 1 79 ? 8.525   -25.821 7.398   1.00 27.12  ? 78  ASN   A CA  1 
ATOM   627  C C   . ASN   A 1 79 ? 9.888   -25.351 6.846   1.00 22.52  ? 78  ASN   A C   1 
ATOM   628  O O   . ASN   A 1 79 ? 10.464  -24.368 7.343   1.00 25.47  ? 78  ASN   A O   1 
ATOM   629  C CB  . ASN   A 1 79 ? 8.663   -26.890 8.497   1.00 28.14  ? 78  ASN   A CB  1 
ATOM   630  C CG  . ASN   A 1 79 ? 7.328   -27.153 9.163   1.00 33.12  ? 78  ASN   A CG  1 
ATOM   631  O OD1 . ASN   A 1 79 ? 6.427   -26.307 9.113   1.00 29.51  ? 78  ASN   A OD1 1 
ATOM   632  N ND2 . ASN   A 1 79 ? 7.191   -28.308 9.809   1.00 29.38  ? 78  ASN   A ND2 1 
ATOM   633  N N   . GLU   A 1 80 ? 10.395  -25.995 5.783   1.00 22.75  ? 79  GLU   A N   1 
ATOM   634  C CA  . GLU   A 1 80 ? 11.573  -25.497 5.100   1.00 23.97  ? 79  GLU   A CA  1 
ATOM   635  C C   . GLU   A 1 80 ? 11.229  -24.110 4.526   1.00 23.27  ? 79  GLU   A C   1 
ATOM   636  O O   . GLU   A 1 80 ? 12.051  -23.193 4.537   1.00 23.67  ? 79  GLU   A O   1 
ATOM   637  C CB  . GLU   A 1 80 ? 12.020  -26.409 3.950   1.00 26.81  ? 79  GLU   A CB  1 
ATOM   638  C CG  . GLU   A 1 80 ? 13.270  -25.930 3.216   1.00 26.75  ? 79  GLU   A CG  1 
ATOM   639  C CD  . GLU   A 1 80 ? 13.762  -26.960 2.197   1.00 36.09  ? 79  GLU   A CD  1 
ATOM   640  O OE1 . GLU   A 1 80 ? 13.080  -27.967 1.914   1.00 41.75  ? 79  GLU   A OE1 1 
ATOM   641  O OE2 . GLU   A 1 80 ? 14.884  -26.750 1.709   1.00 34.13  ? 79  GLU   A OE2 1 
ATOM   642  N N   . GLY   A 1 81 ? 10.015  -23.986 3.984   1.00 23.83  ? 80  GLY   A N   1 
ATOM   643  C CA  . GLY   A 1 81 ? 9.589   -22.704 3.420   1.00 23.28  ? 80  GLY   A CA  1 
ATOM   644  C C   . GLY   A 1 81 ? 9.524   -21.601 4.482   1.00 21.24  ? 80  GLY   A C   1 
ATOM   645  O O   . GLY   A 1 81 ? 9.872   -20.472 4.143   1.00 22.23  ? 80  GLY   A O   1 
ATOM   646  N N   . LEU   A 1 82 ? 9.065   -21.892 5.711   1.00 20.87  ? 81  LEU   A N   1 
ATOM   647  C CA  . LEU   A 1 82 ? 9.079   -20.908 6.782   1.00 21.73  ? 81  LEU   A CA  1 
ATOM   648  C C   . LEU   A 1 82 ? 10.524  -20.464 7.067   1.00 22.73  ? 81  LEU   A C   1 
ATOM   649  O O   . LEU   A 1 82 ? 10.750  -19.273 7.342   1.00 22.64  ? 81  LEU   A O   1 
ATOM   650  C CB  . LEU   A 1 82 ? 8.405   -21.390 8.064   1.00 24.61  ? 81  LEU   A CB  1 
ATOM   651  C CG  . LEU   A 1 82 ? 6.911   -21.687 7.951   1.00 24.69  ? 81  LEU   A CG  1 
ATOM   652  C CD1 . LEU   A 1 82 ? 6.648   -22.259 9.344   1.00 28.76  ? 81  LEU   A CD1 1 
ATOM   653  C CD2 . LEU   A 1 82 ? 6.113   -20.404 7.802   1.00 25.77  ? 81  LEU   A CD2 1 
ATOM   654  N N   . TRP   A 1 83 ? 11.509  -21.393 6.937   1.00 21.87  ? 82  TRP   A N   1 
ATOM   655  C CA  . TRP   A 1 83 ? 12.877  -21.000 7.244   1.00 23.49  ? 82  TRP   A CA  1 
ATOM   656  C C   . TRP   A 1 83 ? 13.376  -20.066 6.149   1.00 20.99  ? 82  TRP   A C   1 
ATOM   657  O O   . TRP   A 1 83 ? 14.032  -19.088 6.446   1.00 21.68  ? 82  TRP   A O   1 
ATOM   658  C CB  . TRP   A 1 83 ? 13.775  -22.256 7.387   1.00 24.14  ? 82  TRP   A CB  1 
ATOM   659  C CG  . TRP   A 1 83 ? 15.227  -21.903 7.657   1.00 24.76  ? 82  TRP   A CG  1 
ATOM   660  C CD1 . TRP   A 1 83 ? 15.846  -21.803 8.876   1.00 27.85  ? 82  TRP   A CD1 1 
ATOM   661  C CD2 . TRP   A 1 83 ? 16.214  -21.543 6.671   1.00 25.30  ? 82  TRP   A CD2 1 
ATOM   662  N NE1 . TRP   A 1 83 ? 17.166  -21.465 8.703   1.00 26.49  ? 82  TRP   A NE1 1 
ATOM   663  C CE2 . TRP   A 1 83 ? 17.413  -21.277 7.368   1.00 25.33  ? 82  TRP   A CE2 1 
ATOM   664  C CE3 . TRP   A 1 83 ? 16.207  -21.447 5.273   1.00 25.94  ? 82  TRP   A CE3 1 
ATOM   665  C CZ2 . TRP   A 1 83 ? 18.580  -20.914 6.706   1.00 25.05  ? 82  TRP   A CZ2 1 
ATOM   666  C CZ3 . TRP   A 1 83 ? 17.357  -21.063 4.615   1.00 25.60  ? 82  TRP   A CZ3 1 
ATOM   667  C CH2 . TRP   A 1 83 ? 18.535  -20.803 5.331   1.00 28.27  ? 82  TRP   A CH2 1 
ATOM   668  N N   . GLU   A 1 84 ? 13.024  -20.374 4.906   1.00 19.83  ? 83  GLU   A N   1 
ATOM   669  C CA  . GLU   A 1 84 ? 13.550  -19.636 3.777   1.00 19.07  ? 83  GLU   A CA  1 
ATOM   670  C C   . GLU   A 1 84 ? 13.024  -18.213 3.833   1.00 20.85  ? 83  GLU   A C   1 
ATOM   671  O O   . GLU   A 1 84 ? 13.773  -17.268 3.621   1.00 21.40  ? 83  GLU   A O   1 
ATOM   672  C CB  . GLU   A 1 84 ? 13.132  -20.313 2.471   1.00 20.19  ? 83  GLU   A CB  1 
ATOM   673  C CG  . GLU   A 1 84 ? 13.918  -21.615 2.316   1.00 21.13  ? 83  GLU   A CG  1 
ATOM   674  C CD  . GLU   A 1 84 ? 13.491  -22.362 1.066   1.00 25.64  ? 83  GLU   A CD  1 
ATOM   675  O OE1 . GLU   A 1 84 ? 12.544  -21.938 0.350   1.00 24.19  ? 83  GLU   A OE1 1 
ATOM   676  O OE2 . GLU   A 1 84 ? 14.068  -23.460 0.794   1.00 25.62  ? 83  GLU   A OE2 1 
ATOM   677  N N   . ILE   A 1 85 ? 11.708  -18.048 4.058   1.00 20.82  ? 84  ILE   A N   1 
ATOM   678  C CA  . ILE   A 1 85 ? 11.123  -16.709 3.974   1.00 19.20  ? 84  ILE   A CA  1 
ATOM   679  C C   . ILE   A 1 85 ? 11.656  -15.804 5.107   1.00 20.44  ? 84  ILE   A C   1 
ATOM   680  O O   . ILE   A 1 85 ? 11.842  -14.597 4.935   1.00 21.51  ? 84  ILE   A O   1 
ATOM   681  C CB  . ILE   A 1 85 ? 9.571   -16.762 3.975   1.00 19.15  ? 84  ILE   A CB  1 
ATOM   682  C CG1 . ILE   A 1 85 ? 8.974   -15.386 3.533   1.00 18.09  ? 84  ILE   A CG1 1 
ATOM   683  C CG2 . ILE   A 1 85 ? 9.039   -17.130 5.371   1.00 21.02  ? 84  ILE   A CG2 1 
ATOM   684  C CD1 . ILE   A 1 85 ? 7.537   -15.483 3.011   1.00 17.43  ? 84  ILE   A CD1 1 
ATOM   685  N N   . GLN   A 1 86 ? 11.989  -16.417 6.257   1.00 19.40  ? 85  GLN   A N   1 
ATOM   686  C CA  . GLN   A 1 86 ? 12.545  -15.677 7.410   1.00 21.99  ? 85  GLN   A CA  1 
ATOM   687  C C   . GLN   A 1 86 ? 14.037  -15.360 7.270   1.00 21.37  ? 85  GLN   A C   1 
ATOM   688  O O   . GLN   A 1 86 ? 14.469  -14.245 7.698   1.00 24.67  ? 85  GLN   A O   1 
ATOM   689  C CB  . GLN   A 1 86 ? 12.209  -16.459 8.689   1.00 23.48  ? 85  GLN   A CB  1 
ATOM   690  C CG  . GLN   A 1 86 ? 12.617  -15.740 9.975   1.00 25.91  ? 85  GLN   A CG  1 
ATOM   691  C CD  . GLN   A 1 86 ? 11.963  -16.344 11.216  1.00 32.06  ? 85  GLN   A CD  1 
ATOM   692  O OE1 . GLN   A 1 86 ? 11.682  -17.555 11.293  1.00 31.11  ? 85  GLN   A OE1 1 
ATOM   693  N NE2 . GLN   A 1 86 ? 11.748  -15.484 12.209  1.00 36.73  ? 85  GLN   A NE2 1 
ATOM   694  N N   . ASN   A 1 87 ? 14.794  -16.301 6.707   1.00 19.80  ? 86  ASN   A N   1 
ATOM   695  C CA  . ASN   A 1 87 ? 16.252  -16.284 6.808   1.00 20.01  ? 86  ASN   A CA  1 
ATOM   696  C C   . ASN   A 1 87 ? 16.993  -15.932 5.518   1.00 21.59  ? 86  ASN   A C   1 
ATOM   697  O O   . ASN   A 1 87 ? 18.071  -15.330 5.587   1.00 24.37  ? 86  ASN   A O   1 
ATOM   698  C CB  . ASN   A 1 87 ? 16.742  -17.580 7.442   1.00 21.01  ? 86  ASN   A CB  1 
ATOM   699  C CG  . ASN   A 1 87 ? 16.275  -17.641 8.878   1.00 25.26  ? 86  ASN   A CG  1 
ATOM   700  O OD1 . ASN   A 1 87 ? 16.603  -16.734 9.678   1.00 27.81  ? 86  ASN   A OD1 1 
ATOM   701  N ND2 . ASN   A 1 87 ? 15.379  -18.566 9.202   1.00 25.09  ? 86  ASN   A ND2 1 
ATOM   702  N N   . ASN   A 1 88 ? 16.453  -16.302 4.334   1.00 20.22  ? 87  ASN   A N   1 
ATOM   703  C CA  . ASN   A 1 88 ? 17.075  -15.921 3.091   1.00 19.94  ? 87  ASN   A CA  1 
ATOM   704  C C   . ASN   A 1 88 ? 16.033  -15.838 1.966   1.00 20.86  ? 87  ASN   A C   1 
ATOM   705  O O   . ASN   A 1 88 ? 16.045  -16.611 1.009   1.00 20.27  ? 87  ASN   A O   1 
ATOM   706  C CB  . ASN   A 1 88 ? 18.239  -16.866 2.751   1.00 22.70  ? 87  ASN   A CB  1 
ATOM   707  C CG  . ASN   A 1 88 ? 19.258  -16.215 1.861   1.00 23.81  ? 87  ASN   A CG  1 
ATOM   708  O OD1 . ASN   A 1 88 ? 19.013  -15.204 1.184   1.00 21.68  ? 87  ASN   A OD1 1 
ATOM   709  N ND2 . ASN   A 1 88 ? 20.453  -16.803 1.858   1.00 26.83  ? 87  ASN   A ND2 1 
ATOM   710  N N   . PRO   A 1 89 ? 15.101  -14.866 2.054   1.00 19.20  ? 88  PRO   A N   1 
ATOM   711  C CA  . PRO   A 1 89 ? 13.958  -14.841 1.143   1.00 19.29  ? 88  PRO   A CA  1 
ATOM   712  C C   . PRO   A 1 89 ? 14.297  -14.414 -0.271  1.00 22.05  ? 88  PRO   A C   1 
ATOM   713  O O   . PRO   A 1 89 ? 13.498  -14.676 -1.167  1.00 20.05  ? 88  PRO   A O   1 
ATOM   714  C CB  . PRO   A 1 89 ? 13.040  -13.826 1.822   1.00 20.73  ? 88  PRO   A CB  1 
ATOM   715  C CG  . PRO   A 1 89 ? 13.953  -12.926 2.561   1.00 20.25  ? 88  PRO   A CG  1 
ATOM   716  C CD  . PRO   A 1 89 ? 14.920  -13.932 3.179   1.00 19.19  ? 88  PRO   A CD  1 
ATOM   717  N N   . HIS   A 1 90 ? 15.500  -13.849 -0.475  1.00 18.13  ? 89  HIS   A N   1 
ATOM   718  C CA  . HIS   A 1 90 ? 15.864  -13.305 -1.787  1.00 18.75  ? 89  HIS   A CA  1 
ATOM   719  C C   . HIS   A 1 90 ? 16.963  -14.139 -2.473  1.00 18.97  ? 89  HIS   A C   1 
ATOM   720  O O   . HIS   A 1 90 ? 17.420  -13.737 -3.543  1.00 20.51  ? 89  HIS   A O   1 
ATOM   721  C CB  . HIS   A 1 90 ? 16.242  -11.807 -1.677  1.00 19.34  ? 89  HIS   A CB  1 
ATOM   722  C CG  . HIS   A 1 90 ? 15.165  -10.991 -1.088  1.00 19.53  ? 89  HIS   A CG  1 
ATOM   723  N ND1 . HIS   A 1 90 ? 13.900  -10.953 -1.677  1.00 19.17  ? 89  HIS   A ND1 1 
ATOM   724  C CD2 . HIS   A 1 90 ? 15.120  -10.261 0.034   1.00 19.86  ? 89  HIS   A CD2 1 
ATOM   725  C CE1 . HIS   A 1 90 ? 13.136  -10.122 -0.970  1.00 18.06  ? 89  HIS   A CE1 1 
ATOM   726  N NE2 . HIS   A 1 90 ? 13.854  -9.708  0.106   1.00 20.47  ? 89  HIS   A NE2 1 
ATOM   727  N N   . ALA   A 1 91 ? 17.261  -15.311 -1.947  1.00 19.80  ? 90  ALA   A N   1 
ATOM   728  C CA  . ALA   A 1 91 ? 18.326  -16.155 -2.524  1.00 20.09  ? 90  ALA   A CA  1 
ATOM   729  C C   . ALA   A 1 91 ? 17.845  -16.889 -3.764  1.00 24.28  ? 90  ALA   A C   1 
ATOM   730  O O   . ALA   A 1 91 ? 16.662  -17.050 -4.048  1.00 23.84  ? 90  ALA   A O   1 
ATOM   731  C CB  . ALA   A 1 91 ? 18.864  -17.148 -1.511  1.00 20.81  ? 90  ALA   A CB  1 
ATOM   732  N N   . SER   A 1 92 ? 18.824  -17.373 -4.541  1.00 24.71  ? 91  SER   A N   1 
ATOM   733  C CA  . SER   A 1 92 ? 18.543  -18.314 -5.609  1.00 26.96  ? 91  SER   A CA  1 
ATOM   734  C C   . SER   A 1 92 ? 18.293  -19.701 -5.032  1.00 27.92  ? 91  SER   A C   1 
ATOM   735  O O   . SER   A 1 92 ? 19.139  -20.216 -4.277  1.00 28.42  ? 91  SER   A O   1 
ATOM   736  C CB  . SER   A 1 92 ? 19.740  -18.333 -6.526  1.00 30.94  ? 91  SER   A CB  1 
ATOM   737  O OG  . SER   A 1 92 ? 19.597  -19.438 -7.398  1.00 33.68  ? 91  SER   A OG  1 
ATOM   738  N N   . TYR   A 1 93 ? 17.149  -20.299 -5.418  1.00 25.39  ? 92  TYR   A N   1 
ATOM   739  C CA  . TYR   A 1 93 ? 16.759  -21.612 -4.955  1.00 26.16  ? 92  TYR   A CA  1 
ATOM   740  C C   . TYR   A 1 93 ? 16.659  -22.553 -6.148  1.00 34.82  ? 92  TYR   A C   1 
ATOM   741  O O   . TYR   A 1 93 ? 16.123  -23.639 -5.994  1.00 39.83  ? 92  TYR   A O   1 
ATOM   742  C CB  . TYR   A 1 93 ? 15.413  -21.598 -4.202  1.00 25.76  ? 92  TYR   A CB  1 
ATOM   743  C CG  . TYR   A 1 93 ? 15.576  -21.007 -2.809  1.00 24.00  ? 92  TYR   A CG  1 
ATOM   744  C CD1 . TYR   A 1 93 ? 15.978  -21.786 -1.717  1.00 25.44  ? 92  TYR   A CD1 1 
ATOM   745  C CD2 . TYR   A 1 93 ? 15.262  -19.661 -2.563  1.00 22.81  ? 92  TYR   A CD2 1 
ATOM   746  C CE1 . TYR   A 1 93 ? 16.152  -21.225 -0.449  1.00 28.42  ? 92  TYR   A CE1 1 
ATOM   747  C CE2 . TYR   A 1 93 ? 15.438  -19.100 -1.312  1.00 24.00  ? 92  TYR   A CE2 1 
ATOM   748  C CZ  . TYR   A 1 93 ? 15.843  -19.886 -0.239  1.00 23.59  ? 92  TYR   A CZ  1 
ATOM   749  O OH  . TYR   A 1 93 ? 16.070  -19.380 1.006   1.00 25.11  ? 92  TYR   A OH  1 
ATOM   750  N N   . SER   A 1 94 ? 17.234  -22.138 -7.280  1.00 44.60  ? 93  SER   A N   1 
ATOM   751  C CA  . SER   A 1 94 ? 17.298  -22.924 -8.505  1.00 58.51  ? 93  SER   A CA  1 
ATOM   752  C C   . SER   A 1 94 ? 18.367  -24.027 -8.426  1.00 68.97  ? 93  SER   A C   1 
ATOM   753  O O   . SER   A 1 94 ? 19.354  -23.842 -7.670  1.00 66.12  ? 93  SER   A O   1 
ATOM   754  C CB  . SER   A 1 94 ? 17.546  -22.036 -9.692  1.00 58.99  ? 93  SER   A CB  1 
ATOM   755  O OG  . SER   A 1 94 ? 16.308  -21.588 -10.215 1.00 59.10  ? 93  SER   A OG  1 
ATOM   756  O OXT . SER   A 1 94 ? 18.192  -25.029 -9.160  1.00 78.89  ? 93  SER   A OXT 1 
ATOM   757  N N   . MET   B 1 2  ? 39.127  -11.142 -42.706 1.00 73.77  ? 1   MET   B N   1 
ATOM   758  C CA  . MET   B 1 2  ? 38.660  -12.147 -43.697 1.00 67.56  ? 1   MET   B CA  1 
ATOM   759  C C   . MET   B 1 2  ? 37.137  -12.262 -43.598 1.00 57.87  ? 1   MET   B C   1 
ATOM   760  O O   . MET   B 1 2  ? 36.612  -12.497 -42.510 1.00 61.38  ? 1   MET   B O   1 
ATOM   761  C CB  . MET   B 1 2  ? 39.348  -13.497 -43.437 1.00 74.75  ? 1   MET   B CB  1 
ATOM   762  C CG  . MET   B 1 2  ? 39.353  -14.482 -44.606 1.00 83.64  ? 1   MET   B CG  1 
ATOM   763  S SD  . MET   B 1 2  ? 40.313  -13.996 -46.059 1.00 80.74  ? 1   MET   B SD  1 
ATOM   764  C CE  . MET   B 1 2  ? 41.805  -13.278 -45.355 1.00 78.03  ? 1   MET   B CE  1 
ATOM   765  N N   . PRO   B 1 3  ? 36.371  -12.078 -44.707 1.00 50.45  ? 2   PRO   B N   1 
ATOM   766  C CA  . PRO   B 1 3  ? 34.920  -12.277 -44.678 1.00 45.54  ? 2   PRO   B CA  1 
ATOM   767  C C   . PRO   B 1 3  ? 34.596  -13.716 -44.285 1.00 47.36  ? 2   PRO   B C   1 
ATOM   768  O O   . PRO   B 1 3  ? 35.399  -14.602 -44.534 1.00 49.02  ? 2   PRO   B O   1 
ATOM   769  C CB  . PRO   B 1 3  ? 34.478  -11.942 -46.097 1.00 43.67  ? 2   PRO   B CB  1 
ATOM   770  C CG  . PRO   B 1 3  ? 35.560  -10.990 -46.572 1.00 42.21  ? 2   PRO   B CG  1 
ATOM   771  C CD  . PRO   B 1 3  ? 36.844  -11.599 -46.018 1.00 44.13  ? 2   PRO   B CD  1 
ATOM   772  N N   . HIS   B 1 4  ? 33.439  -13.909 -43.629 1.00 47.87  ? 3   HIS   B N   1 
ATOM   773  C CA  . HIS   B 1 4  ? 32.960  -15.233 -43.251 1.00 44.38  ? 3   HIS   B CA  1 
ATOM   774  C C   . HIS   B 1 4  ? 31.565  -15.455 -43.832 1.00 41.43  ? 3   HIS   B C   1 
ATOM   775  O O   . HIS   B 1 4  ? 31.014  -14.563 -44.491 1.00 38.29  ? 3   HIS   B O   1 
ATOM   776  C CB  . HIS   B 1 4  ? 33.084  -15.463 -41.740 1.00 51.92  ? 3   HIS   B CB  1 
ATOM   777  C CG  . HIS   B 1 4  ? 34.492  -15.463 -41.227 1.00 64.24  ? 3   HIS   B CG  1 
ATOM   778  N ND1 . HIS   B 1 4  ? 35.443  -16.381 -41.632 1.00 59.75  ? 3   HIS   B ND1 1 
ATOM   779  C CD2 . HIS   B 1 4  ? 35.109  -14.649 -40.346 1.00 59.69  ? 3   HIS   B CD2 1 
ATOM   780  C CE1 . HIS   B 1 4  ? 36.586  -16.131 -41.006 1.00 60.74  ? 3   HIS   B CE1 1 
ATOM   781  N NE2 . HIS   B 1 4  ? 36.405  -15.086 -40.218 1.00 68.42  ? 3   HIS   B NE2 1 
ATOM   782  N N   . ALA   B 1 5  ? 31.008  -16.664 -43.625 1.00 37.13  ? 4   ALA   B N   1 
ATOM   783  C CA  . ALA   B 1 5  ? 29.710  -17.004 -44.184 1.00 38.35  ? 4   ALA   B CA  1 
ATOM   784  C C   . ALA   B 1 5  ? 28.687  -15.974 -43.711 1.00 35.80  ? 4   ALA   B C   1 
ATOM   785  O O   . ALA   B 1 5  ? 27.834  -15.530 -44.479 1.00 38.15  ? 4   ALA   B O   1 
ATOM   786  C CB  . ALA   B 1 5  ? 29.321  -18.384 -43.704 1.00 40.42  ? 4   ALA   B CB  1 
ATOM   787  N N   . PHE   B 1 6  ? 28.798  -15.643 -42.422 1.00 40.07  ? 5   PHE   B N   1 
ATOM   788  C CA  . PHE   B 1 6  ? 28.018  -14.596 -41.779 1.00 42.87  ? 5   PHE   B CA  1 
ATOM   789  C C   . PHE   B 1 6  ? 28.895  -13.368 -41.521 1.00 36.01  ? 5   PHE   B C   1 
ATOM   790  O O   . PHE   B 1 6  ? 30.023  -13.489 -41.049 1.00 43.11  ? 5   PHE   B O   1 
ATOM   791  C CB  . PHE   B 1 6  ? 27.459  -15.068 -40.430 1.00 38.00  ? 5   PHE   B CB  1 
ATOM   792  C CG  . PHE   B 1 6  ? 26.388  -16.145 -40.531 1.00 33.85  ? 5   PHE   B CG  1 
ATOM   793  C CD1 . PHE   B 1 6  ? 25.065  -15.788 -40.765 1.00 30.91  ? 5   PHE   B CD1 1 
ATOM   794  C CD2 . PHE   B 1 6  ? 26.698  -17.509 -40.440 1.00 34.07  ? 5   PHE   B CD2 1 
ATOM   795  C CE1 . PHE   B 1 6  ? 24.054  -16.734 -40.854 1.00 33.00  ? 5   PHE   B CE1 1 
ATOM   796  C CE2 . PHE   B 1 6  ? 25.681  -18.456 -40.537 1.00 30.31  ? 5   PHE   B CE2 1 
ATOM   797  C CZ  . PHE   B 1 6  ? 24.368  -18.082 -40.709 1.00 31.50  ? 5   PHE   B CZ  1 
ATOM   798  N N   . LYS   B 1 7  ? 28.337  -12.196 -41.838 1.00 42.08  ? 6   LYS   B N   1 
ATOM   799  C CA  . LYS   B 1 7  ? 29.041  -10.939 -41.614 1.00 37.86  ? 6   LYS   B CA  1 
ATOM   800  C C   . LYS   B 1 7  ? 28.260  -10.100 -40.600 1.00 38.69  ? 6   LYS   B C   1 
ATOM   801  O O   . LYS   B 1 7  ? 27.025  -10.181 -40.537 1.00 36.65  ? 6   LYS   B O   1 
ATOM   802  C CB  . LYS   B 1 7  ? 29.099  -10.213 -42.962 1.00 44.71  ? 6   LYS   B CB  1 
ATOM   803  C CG  . LYS   B 1 7  ? 27.780  -9.889  -43.652 1.00 45.88  ? 6   LYS   B CG  1 
ATOM   804  C CD  . LYS   B 1 7  ? 28.006  -9.385  -45.080 1.00 50.09  ? 6   LYS   B CD  1 
ATOM   805  C CE  . LYS   B 1 7  ? 26.765  -8.889  -45.763 1.00 52.05  ? 6   LYS   B CE  1 
ATOM   806  N NZ  . LYS   B 1 7  ? 25.778  -9.941  -46.038 1.00 58.28  ? 6   LYS   B NZ  1 
ATOM   807  N N   . PRO   B 1 8  ? 28.940  -9.206  -39.840 1.00 41.92  ? 7   PRO   B N   1 
ATOM   808  C CA  . PRO   B 1 8  ? 28.267  -8.186  -39.023 1.00 34.94  ? 7   PRO   B CA  1 
ATOM   809  C C   . PRO   B 1 8  ? 27.103  -7.498  -39.717 1.00 34.35  ? 7   PRO   B C   1 
ATOM   810  O O   . PRO   B 1 8  ? 27.226  -7.060  -40.875 1.00 38.43  ? 7   PRO   B O   1 
ATOM   811  C CB  . PRO   B 1 8  ? 29.457  -7.241  -38.763 1.00 40.50  ? 7   PRO   B CB  1 
ATOM   812  C CG  . PRO   B 1 8  ? 30.610  -8.218  -38.537 1.00 43.34  ? 7   PRO   B CG  1 
ATOM   813  C CD  . PRO   B 1 8  ? 30.409  -9.112  -39.738 1.00 44.71  ? 7   PRO   B CD  1 
ATOM   814  N N   . GLY   B 1 9  ? 25.953  -7.475  -39.020 1.00 31.09  ? 8   GLY   B N   1 
ATOM   815  C CA  . GLY   B 1 9  ? 24.706  -6.865  -39.465 1.00 30.12  ? 8   GLY   B CA  1 
ATOM   816  C C   . GLY   B 1 9  ? 23.733  -7.853  -40.104 1.00 25.00  ? 8   GLY   B C   1 
ATOM   817  O O   . GLY   B 1 9  ? 22.593  -7.513  -40.408 1.00 28.51  ? 8   GLY   B O   1 
ATOM   818  N N   . ASP   B 1 10 ? 24.223  -9.087  -40.396 1.00 27.55  ? 9   ASP   B N   1 
ATOM   819  C CA  . ASP   B 1 10 ? 23.312  -10.091 -40.929 1.00 28.44  ? 9   ASP   B CA  1 
ATOM   820  C C   . ASP   B 1 10 ? 22.232  -10.424 -39.885 1.00 23.94  ? 9   ASP   B C   1 
ATOM   821  O O   . ASP   B 1 10 ? 22.522  -10.479 -38.689 1.00 27.60  ? 9   ASP   B O   1 
ATOM   822  C CB  . ASP   B 1 10 ? 24.031  -11.393 -41.269 1.00 28.86  ? 9   ASP   B CB  1 
ATOM   823  C CG  . ASP   B 1 10 ? 24.778  -11.446 -42.602 1.00 39.62  ? 9   ASP   B CG  1 
ATOM   824  O OD1 . ASP   B 1 10 ? 24.468  -10.600 -43.479 1.00 36.68  ? 9   ASP   B OD1 1 
ATOM   825  O OD2 . ASP   B 1 10 ? 25.640  -12.365 -42.742 1.00 36.79  ? 9   ASP   B OD2 1 
ATOM   826  N N   . LEU   B 1 11 ? 21.021  -10.551 -40.360 1.00 24.81  ? 10  LEU   B N   1 
ATOM   827  C CA  . LEU   B 1 11 ? 19.868  -10.798 -39.487 1.00 24.81  ? 10  LEU   B CA  1 
ATOM   828  C C   . LEU   B 1 11 ? 19.595  -12.288 -39.519 1.00 26.61  ? 10  LEU   B C   1 
ATOM   829  O O   . LEU   B 1 11 ? 19.631  -12.853 -40.613 1.00 27.06  ? 10  LEU   B O   1 
ATOM   830  C CB  . LEU   B 1 11 ? 18.669  -9.974  -39.929 1.00 27.03  ? 10  LEU   B CB  1 
ATOM   831  C CG  . LEU   B 1 11 ? 18.995  -8.475  -40.077 1.00 27.52  ? 10  LEU   B CG  1 
ATOM   832  C CD1 . LEU   B 1 11 ? 17.707  -7.808  -40.457 1.00 29.23  ? 10  LEU   B CD1 1 
ATOM   833  C CD2 . LEU   B 1 11 ? 19.569  -7.974  -38.755 1.00 28.19  ? 10  LEU   B CD2 1 
ATOM   834  N N   . VAL   B 1 12 ? 19.233  -12.885 -38.355 1.00 23.19  ? 11  VAL   B N   1 
ATOM   835  C CA  . VAL   B 1 12 ? 19.009  -14.341 -38.253 1.00 22.93  ? 11  VAL   B CA  1 
ATOM   836  C C   . VAL   B 1 12 ? 17.923  -14.583 -37.202 1.00 25.25  ? 11  VAL   B C   1 
ATOM   837  O O   . VAL   B 1 12 ? 17.569  -13.690 -36.437 1.00 25.52  ? 11  VAL   B O   1 
ATOM   838  C CB  . VAL   B 1 12 ? 20.311  -15.000 -37.759 1.00 24.21  ? 11  VAL   B CB  1 
ATOM   839  C CG1 . VAL   B 1 12 ? 21.452  -14.870 -38.778 1.00 27.84  ? 11  VAL   B CG1 1 
ATOM   840  C CG2 . VAL   B 1 12 ? 20.794  -14.566 -36.350 1.00 25.68  ? 11  VAL   B CG2 1 
ATOM   841  N N   . PHE   B 1 13 ? 17.442  -15.835 -37.135 1.00 24.03  ? 12  PHE   B N   1 
ATOM   842  C CA  . PHE   B 1 13 ? 16.936  -16.360 -35.871 1.00 22.77  ? 12  PHE   B CA  1 
ATOM   843  C C   . PHE   B 1 13 ? 18.033  -17.241 -35.303 1.00 23.50  ? 12  PHE   B C   1 
ATOM   844  O O   . PHE   B 1 13 ? 18.648  -18.017 -36.053 1.00 25.23  ? 12  PHE   B O   1 
ATOM   845  C CB  . PHE   B 1 13 ? 15.718  -17.240 -36.108 1.00 25.41  ? 12  PHE   B CB  1 
ATOM   846  C CG  . PHE   B 1 13 ? 14.513  -16.400 -36.493 1.00 25.07  ? 12  PHE   B CG  1 
ATOM   847  C CD1 . PHE   B 1 13 ? 14.279  -16.045 -37.824 1.00 28.35  ? 12  PHE   B CD1 1 
ATOM   848  C CD2 . PHE   B 1 13 ? 13.627  -15.965 -35.505 1.00 28.32  ? 12  PHE   B CD2 1 
ATOM   849  C CE1 . PHE   B 1 13 ? 13.179  -15.279 -38.144 1.00 29.83  ? 12  PHE   B CE1 1 
ATOM   850  C CE2 . PHE   B 1 13 ? 12.505  -15.214 -35.848 1.00 29.78  ? 12  PHE   B CE2 1 
ATOM   851  C CZ  . PHE   B 1 13 ? 12.287  -14.878 -37.165 1.00 33.92  ? 12  PHE   B CZ  1 
ATOM   852  N N   . ALA   B 1 14 ? 18.317  -17.087 -33.995 1.00 21.67  ? 13  ALA   B N   1 
ATOM   853  C CA  . ALA   B 1 14 ? 19.359  -17.808 -33.304 1.00 22.41  ? 13  ALA   B CA  1 
ATOM   854  C C   . ALA   B 1 14 ? 18.726  -18.760 -32.280 1.00 24.91  ? 13  ALA   B C   1 
ATOM   855  O O   . ALA   B 1 14 ? 17.762  -18.382 -31.601 1.00 26.30  ? 13  ALA   B O   1 
ATOM   856  C CB  . ALA   B 1 14 ? 20.338  -16.849 -32.641 1.00 24.66  ? 13  ALA   B CB  1 
ATOM   857  N N   . LYS   B 1 15 ? 19.263  -19.981 -32.203 1.00 22.95  ? 14  LYS   B N   1 
ATOM   858  C CA  . LYS   B 1 15 ? 18.649  -21.019 -31.359 1.00 23.90  ? 14  LYS   B CA  1 
ATOM   859  C C   . LYS   B 1 15 ? 19.582  -21.342 -30.204 1.00 26.68  ? 14  LYS   B C   1 
ATOM   860  O O   . LYS   B 1 15 ? 20.783  -21.627 -30.364 1.00 28.86  ? 14  LYS   B O   1 
ATOM   861  C CB  . LYS   B 1 15 ? 18.355  -22.256 -32.223 1.00 26.09  ? 14  LYS   B CB  1 
ATOM   862  C CG  . LYS   B 1 15 ? 17.675  -23.428 -31.399 1.00 25.90  ? 14  LYS   B CG  1 
ATOM   863  C CD  . LYS   B 1 15 ? 16.257  -23.022 -31.014 1.00 27.03  ? 14  LYS   B CD  1 
ATOM   864  C CE  . LYS   B 1 15 ? 15.362  -24.113 -30.328 1.00 30.49  ? 14  LYS   B CE  1 
ATOM   865  N NZ  . LYS   B 1 15 ? 15.880  -24.363 -28.993 1.00 28.59  ? 14  LYS   B NZ  1 
ATOM   866  N N   . MET   B 1 16 ? 18.999  -21.203 -29.002 1.00 24.89  ? 15  MET   B N   1 
ATOM   867  C CA  . MET   B 1 16 ? 19.631  -21.586 -27.749 1.00 30.15  ? 15  MET   B CA  1 
ATOM   868  C C   . MET   B 1 16 ? 18.781  -22.657 -27.067 1.00 30.16  ? 15  MET   B C   1 
ATOM   869  O O   . MET   B 1 16 ? 17.547  -22.587 -27.102 1.00 31.17  ? 15  MET   B O   1 
ATOM   870  C CB  . MET   B 1 16 ? 19.613  -20.410 -26.772 1.00 34.53  ? 15  MET   B CB  1 
ATOM   871  C CG  . MET   B 1 16 ? 20.245  -19.159 -27.320 1.00 41.27  ? 15  MET   B CG  1 
ATOM   872  S SD  . MET   B 1 16 ? 21.991  -18.988 -26.893 1.00 51.66  ? 15  MET   B SD  1 
ATOM   873  C CE  . MET   B 1 16 ? 21.714  -18.725 -25.141 1.00 38.90  ? 15  MET   B CE  1 
ATOM   874  N N   . LYS   B 1 17 ? 19.461  -23.582 -26.363 1.00 30.78  ? 16  LYS   B N   1 
ATOM   875  C CA  . LYS   B 1 17 ? 18.716  -24.626 -25.668 1.00 33.63  ? 16  LYS   B CA  1 
ATOM   876  C C   . LYS   B 1 17 ? 17.780  -23.961 -24.649 1.00 31.17  ? 16  LYS   B C   1 
ATOM   877  O O   . LYS   B 1 17 ? 18.192  -23.069 -23.913 1.00 33.89  ? 16  LYS   B O   1 
ATOM   878  C CB  . LYS   B 1 17 ? 19.688  -25.594 -24.987 1.00 38.81  ? 16  LYS   B CB  1 
ATOM   879  C CG  . LYS   B 1 17 ? 18.973  -26.743 -24.232 1.00 40.20  ? 16  LYS   B CG  1 
ATOM   880  C CD  . LYS   B 1 17 ? 19.770  -28.005 -23.929 1.00 48.69  ? 16  LYS   B CD  1 
ATOM   881  N N   . GLY   B 1 18 ? 16.529  -24.407 -24.626 1.00 34.05  ? 17  GLY   B N   1 
ATOM   882  C CA  . GLY   B 1 18 ? 15.533  -23.896 -23.692 1.00 34.99  ? 17  GLY   B CA  1 
ATOM   883  C C   . GLY   B 1 18 ? 14.699  -22.742 -24.257 1.00 36.39  ? 17  GLY   B C   1 
ATOM   884  O O   . GLY   B 1 18 ? 13.775  -22.267 -23.586 1.00 33.23  ? 17  GLY   B O   1 
ATOM   885  N N   . TYR   B 1 19 ? 15.022  -22.270 -25.482 1.00 29.57  ? 18  TYR   B N   1 
ATOM   886  C CA  . TYR   B 1 19 ? 14.341  -21.071 -25.966 1.00 26.27  ? 18  TYR   B CA  1 
ATOM   887  C C   . TYR   B 1 19 ? 13.909  -21.288 -27.413 1.00 27.12  ? 18  TYR   B C   1 
ATOM   888  O O   . TYR   B 1 19 ? 14.593  -22.023 -28.124 1.00 28.50  ? 18  TYR   B O   1 
ATOM   889  C CB  . TYR   B 1 19 ? 15.219  -19.804 -25.978 1.00 27.75  ? 18  TYR   B CB  1 
ATOM   890  C CG  . TYR   B 1 19 ? 15.761  -19.462 -24.589 1.00 29.37  ? 18  TYR   B CG  1 
ATOM   891  C CD1 . TYR   B 1 19 ? 15.069  -18.617 -23.724 1.00 28.93  ? 18  TYR   B CD1 1 
ATOM   892  C CD2 . TYR   B 1 19 ? 16.874  -20.124 -24.096 1.00 31.58  ? 18  TYR   B CD2 1 
ATOM   893  C CE1 . TYR   B 1 19 ? 15.530  -18.398 -22.422 1.00 28.79  ? 18  TYR   B CE1 1 
ATOM   894  C CE2 . TYR   B 1 19 ? 17.356  -19.895 -22.813 1.00 35.17  ? 18  TYR   B CE2 1 
ATOM   895  C CZ  . TYR   B 1 19 ? 16.661  -19.056 -21.966 1.00 30.14  ? 18  TYR   B CZ  1 
ATOM   896  O OH  . TYR   B 1 19 ? 17.204  -18.822 -20.719 1.00 33.70  ? 18  TYR   B OH  1 
ATOM   897  N N   . PRO   B 1 20 ? 12.863  -20.603 -27.914 1.00 25.91  ? 19  PRO   B N   1 
ATOM   898  C CA  . PRO   B 1 20 ? 12.474  -20.740 -29.322 1.00 25.13  ? 19  PRO   B CA  1 
ATOM   899  C C   . PRO   B 1 20 ? 13.493  -19.988 -30.172 1.00 23.75  ? 19  PRO   B C   1 
ATOM   900  O O   . PRO   B 1 20 ? 14.204  -19.162 -29.638 1.00 26.66  ? 19  PRO   B O   1 
ATOM   901  C CB  . PRO   B 1 20 ? 11.115  -20.077 -29.432 1.00 25.71  ? 19  PRO   B CB  1 
ATOM   902  C CG  . PRO   B 1 20 ? 11.068  -19.079 -28.284 1.00 26.96  ? 19  PRO   B CG  1 
ATOM   903  C CD  . PRO   B 1 20 ? 12.016  -19.634 -27.206 1.00 26.76  ? 19  PRO   B CD  1 
ATOM   904  N N   . HIS   B 1 21 ? 13.586  -20.358 -31.451 1.00 26.81  ? 20  HIS   B N   1 
ATOM   905  C CA  . HIS   B 1 21 ? 14.403  -19.594 -32.404 1.00 24.34  ? 20  HIS   B CA  1 
ATOM   906  C C   . HIS   B 1 21 ? 14.107  -18.100 -32.250 1.00 23.79  ? 20  HIS   B C   1 
ATOM   907  O O   . HIS   B 1 21 ? 12.957  -17.679 -32.323 1.00 24.72  ? 20  HIS   B O   1 
ATOM   908  C CB  . HIS   B 1 21 ? 14.077  -20.090 -33.825 1.00 25.60  ? 20  HIS   B CB  1 
ATOM   909  C CG  . HIS   B 1 21 ? 14.329  -21.558 -34.035 1.00 27.38  ? 20  HIS   B CG  1 
ATOM   910  N ND1 . HIS   B 1 21 ? 13.494  -22.551 -33.536 1.00 27.85  ? 20  HIS   B ND1 1 
ATOM   911  C CD2 . HIS   B 1 21 ? 15.356  -22.201 -34.628 1.00 28.07  ? 20  HIS   B CD2 1 
ATOM   912  C CE1 . HIS   B 1 21 ? 13.996  -23.752 -33.849 1.00 27.89  ? 20  HIS   B CE1 1 
ATOM   913  N NE2 . HIS   B 1 21 ? 15.124  -23.581 -34.521 1.00 27.68  ? 20  HIS   B NE2 1 
ATOM   914  N N   . TRP   B 1 22 ? 15.167  -17.304 -32.083 1.00 23.49  ? 21  TRP   B N   1 
ATOM   915  C CA  . TRP   B 1 22 ? 14.939  -15.974 -31.540 1.00 22.53  ? 21  TRP   B CA  1 
ATOM   916  C C   . TRP   B 1 22 ? 15.490  -14.926 -32.513 1.00 24.46  ? 21  TRP   B C   1 
ATOM   917  O O   . TRP   B 1 22 ? 16.654  -15.054 -32.932 1.00 23.34  ? 21  TRP   B O   1 
ATOM   918  C CB  . TRP   B 1 22 ? 15.709  -15.897 -30.217 1.00 24.80  ? 21  TRP   B CB  1 
ATOM   919  C CG  . TRP   B 1 22 ? 15.198  -14.744 -29.384 1.00 23.15  ? 21  TRP   B CG  1 
ATOM   920  C CD1 . TRP   B 1 22 ? 15.455  -13.405 -29.543 1.00 22.69  ? 21  TRP   B CD1 1 
ATOM   921  C CD2 . TRP   B 1 22 ? 14.258  -14.818 -28.268 1.00 24.20  ? 21  TRP   B CD2 1 
ATOM   922  N NE1 . TRP   B 1 22 ? 14.774  -12.654 -28.601 1.00 25.14  ? 21  TRP   B NE1 1 
ATOM   923  C CE2 . TRP   B 1 22 ? 14.049  -13.503 -27.797 1.00 23.50  ? 21  TRP   B CE2 1 
ATOM   924  C CE3 . TRP   B 1 22 ? 13.607  -15.886 -27.625 1.00 26.65  ? 21  TRP   B CE3 1 
ATOM   925  C CZ2 . TRP   B 1 22 ? 13.191  -13.211 -26.722 1.00 25.14  ? 21  TRP   B CZ2 1 
ATOM   926  C CZ3 . TRP   B 1 22 ? 12.777  -15.605 -26.560 1.00 28.41  ? 21  TRP   B CZ3 1 
ATOM   927  C CH2 . TRP   B 1 22 ? 12.565  -14.290 -26.125 1.00 27.03  ? 21  TRP   B CH2 1 
ATOM   928  N N   . PRO   B 1 23 ? 14.749  -13.824 -32.779 1.00 21.90  ? 22  PRO   B N   1 
ATOM   929  C CA  . PRO   B 1 23 ? 15.231  -12.792 -33.722 1.00 21.92  ? 22  PRO   B CA  1 
ATOM   930  C C   . PRO   B 1 23 ? 16.530  -12.186 -33.201 1.00 23.76  ? 22  PRO   B C   1 
ATOM   931  O O   . PRO   B 1 23 ? 16.629  -11.776 -32.034 1.00 23.82  ? 22  PRO   B O   1 
ATOM   932  C CB  . PRO   B 1 23 ? 14.060  -11.765 -33.793 1.00 21.08  ? 22  PRO   B CB  1 
ATOM   933  C CG  . PRO   B 1 23 ? 13.405  -11.943 -32.410 1.00 23.00  ? 22  PRO   B CG  1 
ATOM   934  C CD  . PRO   B 1 23 ? 13.436  -13.486 -32.211 1.00 22.48  ? 22  PRO   B CD  1 
ATOM   935  N N   . ALA   B 1 24 ? 17.553  -12.066 -34.063 1.00 23.33  ? 23  ALA   B N   1 
ATOM   936  C CA  . ALA   B 1 24 ? 18.875  -11.729 -33.572 1.00 21.82  ? 23  ALA   B CA  1 
ATOM   937  C C   . ALA   B 1 24 ? 19.703  -11.166 -34.738 1.00 23.49  ? 23  ALA   B C   1 
ATOM   938  O O   . ALA   B 1 24 ? 19.257  -11.238 -35.871 1.00 25.52  ? 23  ALA   B O   1 
ATOM   939  C CB  . ALA   B 1 24 ? 19.547  -12.913 -32.890 1.00 23.47  ? 23  ALA   B CB  1 
ATOM   940  N N   . ARG   B 1 25 ? 20.883  -10.636 -34.393 1.00 25.26  ? 24  ARG   B N   1 
ATOM   941  C CA  . ARG   B 1 25 ? 21.793  -10.126 -35.412 1.00 25.84  ? 24  ARG   B CA  1 
ATOM   942  C C   . ARG   B 1 25 ? 23.196  -10.615 -35.116 1.00 25.62  ? 24  ARG   B C   1 
ATOM   943  O O   . ARG   B 1 25 ? 23.559  -10.884 -33.983 1.00 24.87  ? 24  ARG   B O   1 
ATOM   944  C CB  . ARG   B 1 25 ? 21.783  -8.602  -35.568 1.00 27.39  ? 24  ARG   B CB  1 
ATOM   945  C CG  . ARG   B 1 25 ? 22.375  -7.856  -34.381 1.00 25.50  ? 24  ARG   B CG  1 
ATOM   946  C CD  . ARG   B 1 25 ? 22.117  -6.330  -34.507 1.00 24.92  ? 24  ARG   B CD  1 
ATOM   947  N NE  . ARG   B 1 25 ? 22.755  -5.694  -33.360 1.00 26.46  ? 24  ARG   B NE  1 
ATOM   948  C CZ  . ARG   B 1 25 ? 22.492  -4.429  -33.004 1.00 30.36  ? 24  ARG   B CZ  1 
ATOM   949  N NH1 . ARG   B 1 25 ? 21.504  -3.773  -33.606 1.00 29.51  ? 24  ARG   B NH1 1 
ATOM   950  N NH2 . ARG   B 1 25 ? 23.163  -3.890  -31.997 1.00 28.47  ? 24  ARG   B NH2 1 
ATOM   951  N N   . ILE   B 1 26 ? 24.041  -10.691 -36.162 1.00 26.40  ? 25  ILE   B N   1 
ATOM   952  C CA  . ILE   B 1 26 ? 25.461  -10.878 -35.938 1.00 28.33  ? 25  ILE   B CA  1 
ATOM   953  C C   . ILE   B 1 26 ? 26.041  -9.509  -35.600 1.00 30.93  ? 25  ILE   B C   1 
ATOM   954  O O   . ILE   B 1 26 ? 25.756  -8.572  -36.338 1.00 34.67  ? 25  ILE   B O   1 
ATOM   955  C CB  . ILE   B 1 26 ? 26.142  -11.397 -37.221 1.00 31.48  ? 25  ILE   B CB  1 
ATOM   956  C CG1 . ILE   B 1 26 ? 25.428  -12.605 -37.829 1.00 32.74  ? 25  ILE   B CG1 1 
ATOM   957  C CG2 . ILE   B 1 26 ? 27.638  -11.638 -37.012 1.00 37.56  ? 25  ILE   B CG2 1 
ATOM   958  C CD1 . ILE   B 1 26 ? 25.336  -13.821 -36.922 1.00 32.29  ? 25  ILE   B CD1 1 
ATOM   959  N N   . ASP   B 1 27 ? 26.829  -9.465  -34.524 1.00 29.84  ? 26  ASP   B N   1 
ATOM   960  C CA  . ASP   B 1 27 ? 27.519  -8.246  -34.083 1.00 34.80  ? 26  ASP   B CA  1 
ATOM   961  C C   . ASP   B 1 27 ? 28.981  -8.236  -34.549 1.00 41.16  ? 26  ASP   B C   1 
ATOM   962  O O   . ASP   B 1 27 ? 29.494  -9.264  -34.978 1.00 41.92  ? 26  ASP   B O   1 
ATOM   963  C CB  . ASP   B 1 27 ? 27.443  -8.106  -32.569 1.00 34.32  ? 26  ASP   B CB  1 
ATOM   964  C CG  . ASP   B 1 27 ? 26.227  -7.387  -31.986 1.00 36.49  ? 26  ASP   B CG  1 
ATOM   965  O OD1 . ASP   B 1 27 ? 25.412  -6.844  -32.778 1.00 38.79  ? 26  ASP   B OD1 1 
ATOM   966  O OD2 . ASP   B 1 27 ? 26.138  -7.319  -30.722 1.00 35.31  ? 26  ASP   B OD2 1 
ATOM   967  N N   A ASP   B 1 28 ? 29.622  -7.056  -34.463 0.50 47.82  ? 27  ASP   B N   1 
ATOM   968  N N   B ASP   B 1 28 ? 29.635  -7.066  -34.471 0.50 47.62  ? 27  ASP   B N   1 
ATOM   969  C CA  A ASP   B 1 28 ? 31.058  -6.883  -34.651 0.50 55.04  ? 27  ASP   B CA  1 
ATOM   970  C CA  B ASP   B 1 28 ? 31.069  -6.947  -34.703 0.50 54.85  ? 27  ASP   B CA  1 
ATOM   971  C C   A ASP   B 1 28 ? 31.798  -7.362  -33.401 0.50 57.70  ? 27  ASP   B C   1 
ATOM   972  C C   B ASP   B 1 28 ? 31.800  -7.142  -33.372 0.50 58.21  ? 27  ASP   B C   1 
ATOM   973  O O   A ASP   B 1 28 ? 31.176  -7.803  -32.437 0.50 59.79  ? 27  ASP   B O   1 
ATOM   974  O O   B ASP   B 1 28 ? 31.164  -7.174  -32.321 0.50 61.26  ? 27  ASP   B O   1 
ATOM   975  C CB  A ASP   B 1 28 ? 31.425  -5.432  -34.944 0.50 51.62  ? 27  ASP   B CB  1 
ATOM   976  C CB  B ASP   B 1 28 ? 31.416  -5.640  -35.405 0.50 51.21  ? 27  ASP   B CB  1 
ATOM   977  C CG  A ASP   B 1 28 ? 30.526  -4.688  -35.922 0.50 50.76  ? 27  ASP   B CG  1 
ATOM   978  C CG  B ASP   B 1 28 ? 32.425  -5.762  -36.538 0.50 50.35  ? 27  ASP   B CG  1 
ATOM   979  O OD1 A ASP   B 1 28 ? 30.852  -4.675  -37.129 0.50 50.46  ? 27  ASP   B OD1 1 
ATOM   980  O OD1 B ASP   B 1 28 ? 33.410  -6.512  -36.369 0.50 48.46  ? 27  ASP   B OD1 1 
ATOM   981  O OD2 A ASP   B 1 28 ? 29.530  -4.092  -35.467 0.50 47.01  ? 27  ASP   B OD2 1 
ATOM   982  O OD2 B ASP   B 1 28 ? 32.221  -5.103  -37.582 0.50 50.09  ? 27  ASP   B OD2 1 
ATOM   983  N N   . ILE   B 1 29 ? 33.134  -7.271  -33.425 1.00 64.03  ? 28  ILE   B N   1 
ATOM   984  C CA  . ILE   B 1 29 ? 33.942  -7.569  -32.247 1.00 69.74  ? 28  ILE   B CA  1 
ATOM   985  C C   . ILE   B 1 29 ? 34.730  -6.309  -31.844 1.00 75.02  ? 28  ILE   B C   1 
ATOM   986  O O   . ILE   B 1 29 ? 34.090  -5.232  -31.786 1.00 71.95  ? 28  ILE   B O   1 
ATOM   987  C CB  . ILE   B 1 29 ? 34.867  -8.784  -32.468 1.00 66.14  ? 28  ILE   B CB  1 
ATOM   988  N N   . VAL   B 1 34 ? 37.017  -9.919  -25.342 1.00 65.29  ? 33  VAL   B N   1 
ATOM   989  C CA  . VAL   B 1 34 ? 36.840  -11.374 -25.639 1.00 72.06  ? 33  VAL   B CA  1 
ATOM   990  C C   . VAL   B 1 34 ? 36.527  -11.514 -27.125 1.00 75.06  ? 33  VAL   B C   1 
ATOM   991  O O   . VAL   B 1 34 ? 35.664  -10.811 -27.649 1.00 87.12  ? 33  VAL   B O   1 
ATOM   992  C CB  . VAL   B 1 34 ? 35.738  -12.002 -24.758 1.00 75.88  ? 33  VAL   B CB  1 
ATOM   993  C CG1 . VAL   B 1 34 ? 34.400  -11.279 -24.889 1.00 72.54  ? 33  VAL   B CG1 1 
ATOM   994  C CG2 . VAL   B 1 34 ? 35.572  -13.497 -25.012 1.00 70.57  ? 33  VAL   B CG2 1 
ATOM   995  N N   . LYS   B 1 35 ? 37.265  -12.397 -27.806 1.00 72.45  ? 34  LYS   B N   1 
ATOM   996  C CA  . LYS   B 1 35 ? 36.900  -12.793 -29.157 1.00 64.18  ? 34  LYS   B CA  1 
ATOM   997  C C   . LYS   B 1 35 ? 36.036  -14.055 -29.067 1.00 63.88  ? 34  LYS   B C   1 
ATOM   998  O O   . LYS   B 1 35 ? 36.163  -14.832 -28.115 1.00 57.07  ? 34  LYS   B O   1 
ATOM   999  C CB  . LYS   B 1 35 ? 38.166  -12.902 -30.015 1.00 68.83  ? 34  LYS   B CB  1 
ATOM   1000 N N   . PRO   B 1 36 ? 35.075  -14.282 -29.998 1.00 58.84  ? 35  PRO   B N   1 
ATOM   1001 C CA  . PRO   B 1 36 ? 34.312  -15.535 -29.999 1.00 55.97  ? 35  PRO   B CA  1 
ATOM   1002 C C   . PRO   B 1 36 ? 35.226  -16.752 -29.890 1.00 48.53  ? 35  PRO   B C   1 
ATOM   1003 O O   . PRO   B 1 36 ? 36.359  -16.689 -30.350 1.00 54.93  ? 35  PRO   B O   1 
ATOM   1004 C CB  . PRO   B 1 36 ? 33.537  -15.516 -31.328 1.00 58.95  ? 35  PRO   B CB  1 
ATOM   1005 C CG  . PRO   B 1 36 ? 34.005  -14.260 -32.054 1.00 62.96  ? 35  PRO   B CG  1 
ATOM   1006 C CD  . PRO   B 1 36 ? 34.628  -13.327 -31.028 1.00 57.43  ? 35  PRO   B CD  1 
ATOM   1007 N N   . PRO   B 1 37 ? 34.802  -17.873 -29.253 1.00 47.64  ? 36  PRO   B N   1 
ATOM   1008 C CA  . PRO   B 1 37 ? 35.527  -19.132 -29.391 1.00 51.19  ? 36  PRO   B CA  1 
ATOM   1009 C C   . PRO   B 1 37 ? 35.602  -19.415 -30.888 1.00 56.37  ? 36  PRO   B C   1 
ATOM   1010 O O   . PRO   B 1 37 ? 34.783  -18.902 -31.655 1.00 50.03  ? 36  PRO   B O   1 
ATOM   1011 C CB  . PRO   B 1 37 ? 34.666  -20.177 -28.653 1.00 55.09  ? 36  PRO   B CB  1 
ATOM   1012 C CG  . PRO   B 1 37 ? 33.735  -19.371 -27.759 1.00 53.02  ? 36  PRO   B CG  1 
ATOM   1013 C CD  . PRO   B 1 37 ? 33.641  -17.975 -28.351 1.00 48.95  ? 36  PRO   B CD  1 
ATOM   1014 N N   . PRO   B 1 38 ? 36.575  -20.231 -31.358 1.00 60.54  ? 37  PRO   B N   1 
ATOM   1015 C CA  . PRO   B 1 38 ? 36.629  -20.617 -32.775 1.00 64.79  ? 37  PRO   B CA  1 
ATOM   1016 C C   . PRO   B 1 38 ? 35.276  -21.091 -33.323 1.00 54.43  ? 37  PRO   B C   1 
ATOM   1017 O O   . PRO   B 1 38 ? 34.506  -21.741 -32.615 1.00 50.67  ? 37  PRO   B O   1 
ATOM   1018 C CB  . PRO   B 1 38 ? 37.697  -21.746 -32.787 1.00 65.94  ? 37  PRO   B CB  1 
ATOM   1019 C CG  . PRO   B 1 38 ? 38.580  -21.464 -31.578 1.00 57.66  ? 37  PRO   B CG  1 
ATOM   1020 C CD  . PRO   B 1 38 ? 37.661  -20.822 -30.552 1.00 65.15  ? 37  PRO   B CD  1 
ATOM   1021 N N   . ASN   B 1 39 ? 34.985  -20.738 -34.578 1.00 52.06  ? 38  ASN   B N   1 
ATOM   1022 C CA  . ASN   B 1 39 ? 33.825  -21.261 -35.297 1.00 56.49  ? 38  ASN   B CA  1 
ATOM   1023 C C   . ASN   B 1 39 ? 32.503  -20.581 -34.906 1.00 49.07  ? 38  ASN   B C   1 
ATOM   1024 O O   . ASN   B 1 39 ? 31.468  -20.904 -35.477 1.00 39.09  ? 38  ASN   B O   1 
ATOM   1025 C CB  . ASN   B 1 39 ? 33.655  -22.768 -35.103 1.00 57.17  ? 38  ASN   B CB  1 
ATOM   1026 C CG  . ASN   B 1 39 ? 34.861  -23.581 -35.523 1.00 70.00  ? 38  ASN   B CG  1 
ATOM   1027 O OD1 . ASN   B 1 39 ? 35.205  -24.558 -34.847 1.00 75.88  ? 38  ASN   B OD1 1 
ATOM   1028 N ND2 . ASN   B 1 39 ? 35.492  -23.229 -36.637 1.00 66.86  ? 38  ASN   B ND2 1 
ATOM   1029 N N   . LYS   B 1 40 ? 32.516  -19.666 -33.923 1.00 47.19  ? 39  LYS   B N   1 
ATOM   1030 C CA  . LYS   B 1 40 ? 31.286  -19.077 -33.415 1.00 40.64  ? 39  LYS   B CA  1 
ATOM   1031 C C   . LYS   B 1 40 ? 31.282  -17.579 -33.689 1.00 38.02  ? 39  LYS   B C   1 
ATOM   1032 O O   . LYS   B 1 40 ? 32.320  -17.013 -34.020 1.00 44.56  ? 39  LYS   B O   1 
ATOM   1033 C CB  . LYS   B 1 40 ? 31.184  -19.333 -31.911 1.00 45.21  ? 39  LYS   B CB  1 
ATOM   1034 C CG  . LYS   B 1 40 ? 31.030  -20.801 -31.526 1.00 46.35  ? 39  LYS   B CG  1 
ATOM   1035 C CD  . LYS   B 1 40 ? 30.699  -20.918 -30.040 1.00 51.63  ? 39  LYS   B CD  1 
ATOM   1036 C CE  . LYS   B 1 40 ? 29.703  -21.961 -29.644 1.00 62.27  ? 39  LYS   B CE  1 
ATOM   1037 N NZ  . LYS   B 1 40 ? 30.217  -23.335 -29.613 1.00 55.80  ? 39  LYS   B NZ  1 
ATOM   1038 N N   . TYR   B 1 41 ? 30.110  -16.958 -33.515 1.00 33.49  ? 40  TYR   B N   1 
ATOM   1039 C CA  . TYR   B 1 41 ? 29.855  -15.574 -33.903 1.00 31.19  ? 40  TYR   B CA  1 
ATOM   1040 C C   . TYR   B 1 41 ? 29.281  -14.855 -32.685 1.00 34.95  ? 40  TYR   B C   1 
ATOM   1041 O O   . TYR   B 1 41 ? 28.578  -15.464 -31.881 1.00 31.86  ? 40  TYR   B O   1 
ATOM   1042 C CB  . TYR   B 1 41 ? 28.836  -15.415 -35.039 1.00 33.46  ? 40  TYR   B CB  1 
ATOM   1043 C CG  . TYR   B 1 41 ? 29.330  -15.883 -36.401 1.00 32.62  ? 40  TYR   B CG  1 
ATOM   1044 C CD1 . TYR   B 1 41 ? 29.969  -15.021 -37.279 1.00 33.24  ? 40  TYR   B CD1 1 
ATOM   1045 C CD2 . TYR   B 1 41 ? 29.151  -17.203 -36.798 1.00 31.53  ? 40  TYR   B CD2 1 
ATOM   1046 C CE1 . TYR   B 1 41 ? 30.434  -15.467 -38.510 1.00 40.17  ? 40  TYR   B CE1 1 
ATOM   1047 C CE2 . TYR   B 1 41 ? 29.611  -17.660 -38.019 1.00 32.72  ? 40  TYR   B CE2 1 
ATOM   1048 C CZ  . TYR   B 1 41 ? 30.244  -16.785 -38.888 1.00 37.64  ? 40  TYR   B CZ  1 
ATOM   1049 O OH  . TYR   B 1 41 ? 30.651  -17.239 -40.129 1.00 34.74  ? 40  TYR   B OH  1 
ATOM   1050 N N   . PRO   B 1 42 ? 29.494  -13.532 -32.523 1.00 34.22  ? 41  PRO   B N   1 
ATOM   1051 C CA  . PRO   B 1 42 ? 28.826  -12.814 -31.436 1.00 30.77  ? 41  PRO   B CA  1 
ATOM   1052 C C   . PRO   B 1 42 ? 27.408  -12.494 -31.898 1.00 29.94  ? 41  PRO   B C   1 
ATOM   1053 O O   . PRO   B 1 42 ? 27.204  -11.834 -32.938 1.00 30.81  ? 41  PRO   B O   1 
ATOM   1054 C CB  . PRO   B 1 42 ? 29.697  -11.536 -31.238 1.00 33.23  ? 41  PRO   B CB  1 
ATOM   1055 C CG  . PRO   B 1 42 ? 30.489  -11.394 -32.521 1.00 36.17  ? 41  PRO   B CG  1 
ATOM   1056 C CD  . PRO   B 1 42 ? 30.365  -12.670 -33.354 1.00 33.52  ? 41  PRO   B CD  1 
ATOM   1057 N N   . ILE   B 1 43 ? 26.433  -12.971 -31.090 1.00 28.73  ? 42  ILE   B N   1 
ATOM   1058 C CA  . ILE   B 1 43 ? 25.010  -12.753 -31.362 1.00 26.45  ? 42  ILE   B CA  1 
ATOM   1059 C C   . ILE   B 1 43 ? 24.425  -11.738 -30.391 1.00 25.97  ? 42  ILE   B C   1 
ATOM   1060 O O   . ILE   B 1 43 ? 24.715  -11.816 -29.228 1.00 30.02  ? 42  ILE   B O   1 
ATOM   1061 C CB  . ILE   B 1 43 ? 24.258  -14.089 -31.214 1.00 25.84  ? 42  ILE   B CB  1 
ATOM   1062 C CG1 . ILE   B 1 43 ? 24.990  -15.188 -32.025 1.00 29.93  ? 42  ILE   B CG1 1 
ATOM   1063 C CG2 . ILE   B 1 43 ? 22.775  -13.942 -31.622 1.00 23.45  ? 42  ILE   B CG2 1 
ATOM   1064 C CD1 . ILE   B 1 43 ? 25.178  -14.883 -33.500 1.00 29.50  ? 42  ILE   B CD1 1 
ATOM   1065 N N   . PHE   B 1 44 ? 23.625  -10.832 -30.937 1.00 26.56  ? 43  PHE   B N   1 
ATOM   1066 C CA  . PHE   B 1 44 ? 22.746  -9.945  -30.173 1.00 28.33  ? 43  PHE   B CA  1 
ATOM   1067 C C   . PHE   B 1 44 ? 21.297  -10.369 -30.376 1.00 26.34  ? 43  PHE   B C   1 
ATOM   1068 O O   . PHE   B 1 44 ? 20.774  -10.377 -31.496 1.00 26.12  ? 43  PHE   B O   1 
ATOM   1069 C CB  . PHE   B 1 44 ? 22.949  -8.509  -30.653 1.00 27.46  ? 43  PHE   B CB  1 
ATOM   1070 C CG  . PHE   B 1 44 ? 22.016  -7.499  -29.988 1.00 26.33  ? 43  PHE   B CG  1 
ATOM   1071 C CD1 . PHE   B 1 44 ? 20.835  -7.098  -30.608 1.00 27.49  ? 43  PHE   B CD1 1 
ATOM   1072 C CD2 . PHE   B 1 44 ? 22.378  -6.891  -28.795 1.00 33.85  ? 43  PHE   B CD2 1 
ATOM   1073 C CE1 . PHE   B 1 44 ? 19.986  -6.162  -30.022 1.00 30.80  ? 43  PHE   B CE1 1 
ATOM   1074 C CE2 . PHE   B 1 44 ? 21.536  -5.940  -28.210 1.00 27.57  ? 43  PHE   B CE2 1 
ATOM   1075 C CZ  . PHE   B 1 44 ? 20.346  -5.591  -28.829 1.00 29.60  ? 43  PHE   B CZ  1 
ATOM   1076 N N   . PHE   B 1 45 ? 20.612  -10.696 -29.259 1.00 25.36  ? 44  PHE   B N   1 
ATOM   1077 C CA  . PHE   B 1 45 ? 19.207  -11.038 -29.302 1.00 25.37  ? 44  PHE   B CA  1 
ATOM   1078 C C   . PHE   B 1 45 ? 18.316  -9.825  -29.147 1.00 26.00  ? 44  PHE   B C   1 
ATOM   1079 O O   . PHE   B 1 45 ? 18.423  -9.068  -28.167 1.00 27.67  ? 44  PHE   B O   1 
ATOM   1080 C CB  . PHE   B 1 45 ? 18.916  -12.017 -28.150 1.00 23.61  ? 44  PHE   B CB  1 
ATOM   1081 C CG  . PHE   B 1 45 ? 19.641  -13.358 -28.242 1.00 26.11  ? 44  PHE   B CG  1 
ATOM   1082 C CD1 . PHE   B 1 45 ? 20.783  -13.588 -27.499 1.00 30.45  ? 44  PHE   B CD1 1 
ATOM   1083 C CD2 . PHE   B 1 45 ? 19.159  -14.392 -29.047 1.00 24.24  ? 44  PHE   B CD2 1 
ATOM   1084 C CE1 . PHE   B 1 45 ? 21.472  -14.790 -27.586 1.00 36.49  ? 44  PHE   B CE1 1 
ATOM   1085 C CE2 . PHE   B 1 45 ? 19.814  -15.600 -29.091 1.00 26.92  ? 44  PHE   B CE2 1 
ATOM   1086 C CZ  . PHE   B 1 45 ? 20.991  -15.786 -28.415 1.00 29.69  ? 44  PHE   B CZ  1 
ATOM   1087 N N   . PHE   B 1 46 ? 17.462  -9.626  -30.160 1.00 24.85  ? 45  PHE   B N   1 
ATOM   1088 C CA  . PHE   B 1 46 ? 16.556  -8.487  -30.138 1.00 25.15  ? 45  PHE   B CA  1 
ATOM   1089 C C   . PHE   B 1 46 ? 15.538  -8.669  -29.002 1.00 27.14  ? 45  PHE   B C   1 
ATOM   1090 O O   . PHE   B 1 46 ? 15.261  -9.792  -28.594 1.00 25.53  ? 45  PHE   B O   1 
ATOM   1091 C CB  . PHE   B 1 46 ? 15.814  -8.233  -31.437 1.00 23.51  ? 45  PHE   B CB  1 
ATOM   1092 C CG  . PHE   B 1 46 ? 16.739  -7.775  -32.560 1.00 26.05  ? 45  PHE   B CG  1 
ATOM   1093 C CD1 . PHE   B 1 46 ? 17.265  -6.473  -32.547 1.00 27.33  ? 45  PHE   B CD1 1 
ATOM   1094 C CD2 . PHE   B 1 46 ? 17.020  -8.630  -33.624 1.00 25.06  ? 45  PHE   B CD2 1 
ATOM   1095 C CE1 . PHE   B 1 46 ? 18.120  -6.077  -33.578 1.00 26.05  ? 45  PHE   B CE1 1 
ATOM   1096 C CE2 . PHE   B 1 46 ? 17.840  -8.209  -34.678 1.00 26.37  ? 45  PHE   B CE2 1 
ATOM   1097 C CZ  . PHE   B 1 46 ? 18.338  -6.915  -34.658 1.00 25.88  ? 45  PHE   B CZ  1 
ATOM   1098 N N   . GLY   B 1 47 ? 15.012  -7.547  -28.494 1.00 28.41  ? 46  GLY   B N   1 
ATOM   1099 C CA  . GLY   B 1 47 ? 13.985  -7.579  -27.440 1.00 25.76  ? 46  GLY   B CA  1 
ATOM   1100 C C   . GLY   B 1 47 ? 14.610  -7.681  -26.043 1.00 27.47  ? 46  GLY   B C   1 
ATOM   1101 O O   . GLY   B 1 47 ? 14.459  -6.783  -25.207 1.00 31.39  ? 46  GLY   B O   1 
ATOM   1102 N N   . THR   B 1 48 ? 15.361  -8.748  -25.783 1.00 26.42  ? 47  THR   B N   1 
ATOM   1103 C CA  . THR   B 1 48 ? 16.018  -8.985  -24.508 1.00 27.05  ? 47  THR   B CA  1 
ATOM   1104 C C   . THR   B 1 48 ? 17.322  -8.205  -24.451 1.00 28.92  ? 47  THR   B C   1 
ATOM   1105 O O   . THR   B 1 48 ? 17.789  -7.809  -23.381 1.00 31.43  ? 47  THR   B O   1 
ATOM   1106 C CB  . THR   B 1 48 ? 16.251  -10.480 -24.224 1.00 31.88  ? 47  THR   B CB  1 
ATOM   1107 O OG1 . THR   B 1 48 ? 17.283  -10.956 -25.105 1.00 30.80  ? 47  THR   B OG1 1 
ATOM   1108 C CG2 . THR   B 1 48 ? 14.964  -11.310 -24.166 1.00 28.30  ? 47  THR   B CG2 1 
ATOM   1109 N N   . HIS   B 1 49 ? 17.906  -7.962  -25.630 1.00 28.71  ? 48  HIS   B N   1 
ATOM   1110 C CA  . HIS   B 1 49 ? 19.205  -7.316  -25.741 1.00 29.74  ? 48  HIS   B CA  1 
ATOM   1111 C C   . HIS   B 1 49 ? 20.302  -8.101  -25.036 1.00 31.44  ? 48  HIS   B C   1 
ATOM   1112 O O   . HIS   B 1 49 ? 21.307  -7.505  -24.648 1.00 35.43  ? 48  HIS   B O   1 
ATOM   1113 C CB  . HIS   B 1 49 ? 19.159  -5.836  -25.313 1.00 28.31  ? 48  HIS   B CB  1 
ATOM   1114 C CG  . HIS   B 1 49 ? 17.985  -5.126  -25.876 1.00 30.43  ? 48  HIS   B CG  1 
ATOM   1115 N ND1 . HIS   B 1 49 ? 17.216  -4.274  -25.104 1.00 33.49  ? 48  HIS   B ND1 1 
ATOM   1116 C CD2 . HIS   B 1 49 ? 17.381  -5.163  -27.085 1.00 28.06  ? 48  HIS   B CD2 1 
ATOM   1117 C CE1 . HIS   B 1 49 ? 16.223  -3.790  -25.841 1.00 37.26  ? 48  HIS   B CE1 1 
ATOM   1118 N NE2 . HIS   B 1 49 ? 16.312  -4.317  -27.067 1.00 32.93  ? 48  HIS   B NE2 1 
ATOM   1119 N N   . GLU   B 1 50 ? 20.139  -9.432  -24.890 1.00 29.17  ? 49  GLU   B N   1 
ATOM   1120 C CA  . GLU   B 1 50 ? 21.165  -10.299 -24.335 1.00 29.91  ? 49  GLU   B CA  1 
ATOM   1121 C C   . GLU   B 1 50 ? 22.138  -10.690 -25.458 1.00 30.81  ? 49  GLU   B C   1 
ATOM   1122 O O   . GLU   B 1 50 ? 21.845  -10.465 -26.643 1.00 30.19  ? 49  GLU   B O   1 
ATOM   1123 C CB  . GLU   B 1 50 ? 20.541  -11.607 -23.837 1.00 32.70  ? 49  GLU   B CB  1 
ATOM   1124 C CG  . GLU   B 1 50 ? 19.564  -11.434 -22.675 1.00 36.88  ? 49  GLU   B CG  1 
ATOM   1125 C CD  . GLU   B 1 50 ? 20.207  -11.612 -21.311 1.00 52.63  ? 49  GLU   B CD  1 
ATOM   1126 O OE1 . GLU   B 1 50 ? 19.456  -11.554 -20.315 1.00 50.14  ? 49  GLU   B OE1 1 
ATOM   1127 O OE2 . GLU   B 1 50 ? 21.436  -11.803 -21.220 1.00 56.58  ? 49  GLU   B OE2 1 
ATOM   1128 N N   . THR   B 1 51 ? 23.298  -11.239 -25.065 1.00 30.18  ? 50  THR   B N   1 
ATOM   1129 C CA  . THR   B 1 51 ? 24.322  -11.653 -26.031 1.00 33.14  ? 50  THR   B CA  1 
ATOM   1130 C C   . THR   B 1 51 ? 24.784  -13.080 -25.737 1.00 35.90  ? 50  THR   B C   1 
ATOM   1131 O O   . THR   B 1 51 ? 24.640  -13.596 -24.625 1.00 37.31  ? 50  THR   B O   1 
ATOM   1132 C CB  . THR   B 1 51 ? 25.478  -10.648 -26.159 1.00 35.97  ? 50  THR   B CB  1 
ATOM   1133 O OG1 . THR   B 1 51 ? 26.109  -10.538 -24.893 1.00 37.41  ? 50  THR   B OG1 1 
ATOM   1134 C CG2 . THR   B 1 51 ? 25.064  -9.239  -26.551 1.00 32.38  ? 50  THR   B CG2 1 
ATOM   1135 N N   . ALA   B 1 52 ? 25.300  -13.757 -26.777 1.00 33.46  ? 51  ALA   B N   1 
ATOM   1136 C CA  . ALA   B 1 52 ? 25.928  -15.057 -26.664 1.00 34.13  ? 51  ALA   B CA  1 
ATOM   1137 C C   . ALA   B 1 52 ? 26.830  -15.297 -27.877 1.00 32.22  ? 51  ALA   B C   1 
ATOM   1138 O O   . ALA   B 1 52 ? 26.778  -14.566 -28.869 1.00 32.52  ? 51  ALA   B O   1 
ATOM   1139 C CB  . ALA   B 1 52 ? 24.884  -16.155 -26.539 1.00 35.88  ? 51  ALA   B CB  1 
ATOM   1140 N N   . PHE   B 1 53 ? 27.639  -16.349 -27.771 1.00 32.61  ? 52  PHE   B N   1 
ATOM   1141 C CA  . PHE   B 1 53 ? 28.376  -16.856 -28.913 1.00 34.29  ? 52  PHE   B CA  1 
ATOM   1142 C C   . PHE   B 1 53 ? 27.719  -18.155 -29.389 1.00 32.09  ? 52  PHE   B C   1 
ATOM   1143 O O   . PHE   B 1 53 ? 27.541  -19.105 -28.630 1.00 35.55  ? 52  PHE   B O   1 
ATOM   1144 C CB  . PHE   B 1 53 ? 29.845  -17.107 -28.549 1.00 35.99  ? 52  PHE   B CB  1 
ATOM   1145 C CG  . PHE   B 1 53 ? 30.625  -15.927 -27.993 1.00 38.70  ? 52  PHE   B CG  1 
ATOM   1146 C CD1 . PHE   B 1 53 ? 30.965  -14.860 -28.809 1.00 40.73  ? 52  PHE   B CD1 1 
ATOM   1147 C CD2 . PHE   B 1 53 ? 31.041  -15.920 -26.666 1.00 42.46  ? 52  PHE   B CD2 1 
ATOM   1148 C CE1 . PHE   B 1 53 ? 31.686  -13.784 -28.315 1.00 43.40  ? 52  PHE   B CE1 1 
ATOM   1149 C CE2 . PHE   B 1 53 ? 31.759  -14.839 -26.170 1.00 47.34  ? 52  PHE   B CE2 1 
ATOM   1150 C CZ  . PHE   B 1 53 ? 32.073  -13.778 -26.989 1.00 41.81  ? 52  PHE   B CZ  1 
ATOM   1151 N N   . LEU   B 1 54 ? 27.347  -18.180 -30.673 1.00 31.43  ? 53  LEU   B N   1 
ATOM   1152 C CA  . LEU   B 1 54 ? 26.757  -19.354 -31.285 1.00 30.08  ? 53  LEU   B CA  1 
ATOM   1153 C C   . LEU   B 1 54 ? 27.505  -19.695 -32.567 1.00 30.85  ? 53  LEU   B C   1 
ATOM   1154 O O   . LEU   B 1 54 ? 28.000  -18.787 -33.255 1.00 32.30  ? 53  LEU   B O   1 
ATOM   1155 C CB  . LEU   B 1 54 ? 25.277  -19.133 -31.610 1.00 30.21  ? 53  LEU   B CB  1 
ATOM   1156 C CG  . LEU   B 1 54 ? 24.362  -18.967 -30.399 1.00 30.06  ? 53  LEU   B CG  1 
ATOM   1157 C CD1 . LEU   B 1 54 ? 22.951  -18.681 -30.808 1.00 29.30  ? 53  LEU   B CD1 1 
ATOM   1158 C CD2 . LEU   B 1 54 ? 24.476  -20.290 -29.636 1.00 35.52  ? 53  LEU   B CD2 1 
ATOM   1159 N N   . GLY   B 1 55 ? 27.454  -20.997 -32.905 1.00 32.57  ? 54  GLY   B N   1 
ATOM   1160 C CA  . GLY   B 1 55 ? 27.957  -21.550 -34.154 1.00 31.54  ? 54  GLY   B CA  1 
ATOM   1161 C C   . GLY   B 1 55 ? 26.886  -21.535 -35.242 1.00 28.43  ? 54  GLY   B C   1 
ATOM   1162 O O   . GLY   B 1 55 ? 25.698  -21.410 -34.959 1.00 29.13  ? 54  GLY   B O   1 
ATOM   1163 N N   . PRO   B 1 56 ? 27.272  -21.679 -36.535 1.00 28.88  ? 55  PRO   B N   1 
ATOM   1164 C CA  . PRO   B 1 56 ? 26.302  -21.755 -37.633 1.00 28.54  ? 55  PRO   B CA  1 
ATOM   1165 C C   . PRO   B 1 56 ? 25.150  -22.745 -37.559 1.00 25.83  ? 55  PRO   B C   1 
ATOM   1166 O O   . PRO   B 1 56 ? 24.089  -22.463 -38.104 1.00 26.58  ? 55  PRO   B O   1 
ATOM   1167 C CB  . PRO   B 1 56 ? 27.156  -22.001 -38.899 1.00 32.83  ? 55  PRO   B CB  1 
ATOM   1168 C CG  . PRO   B 1 56 ? 28.588  -21.895 -38.482 1.00 35.13  ? 55  PRO   B CG  1 
ATOM   1169 C CD  . PRO   B 1 56 ? 28.674  -21.771 -36.981 1.00 31.09  ? 55  PRO   B CD  1 
ATOM   1170 N N   . LYS   B 1 57 ? 25.327  -23.874 -36.845 1.00 27.65  ? 56  LYS   B N   1 
ATOM   1171 C CA  . LYS   B 1 57 ? 24.229  -24.837 -36.757 1.00 29.03  ? 56  LYS   B CA  1 
ATOM   1172 C C   . LYS   B 1 57 ? 23.001  -24.241 -36.072 1.00 27.30  ? 56  LYS   B C   1 
ATOM   1173 O O   . LYS   B 1 57 ? 21.882  -24.722 -36.260 1.00 28.28  ? 56  LYS   B O   1 
ATOM   1174 C CB  . LYS   B 1 57 ? 24.637  -26.112 -36.001 1.00 34.81  ? 56  LYS   B CB  1 
ATOM   1175 C CG  . LYS   B 1 57 ? 24.904  -25.975 -34.507 1.00 37.67  ? 56  LYS   B CG  1 
ATOM   1176 C CD  . LYS   B 1 57 ? 24.993  -27.340 -33.821 1.00 42.53  ? 56  LYS   B CD  1 
ATOM   1177 C CE  . LYS   B 1 57 ? 25.278  -27.292 -32.341 1.00 44.32  ? 56  LYS   B CE  1 
ATOM   1178 N NZ  . LYS   B 1 57 ? 24.158  -26.853 -31.509 1.00 47.23  ? 56  LYS   B NZ  1 
ATOM   1179 N N   . ASP   B 1 58 ? 23.223  -23.148 -35.314 1.00 25.37  ? 57  ASP   B N   1 
ATOM   1180 C CA  . ASP   B 1 58 ? 22.160  -22.532 -34.537 1.00 27.45  ? 57  ASP   B CA  1 
ATOM   1181 C C   . ASP   B 1 58 ? 21.730  -21.193 -35.140 1.00 28.01  ? 57  ASP   B C   1 
ATOM   1182 O O   . ASP   B 1 58 ? 20.966  -20.467 -34.504 1.00 27.37  ? 57  ASP   B O   1 
ATOM   1183 C CB  . ASP   B 1 58 ? 22.644  -22.391 -33.105 1.00 26.59  ? 57  ASP   B CB  1 
ATOM   1184 C CG  . ASP   B 1 58 ? 22.800  -23.712 -32.356 1.00 33.04  ? 57  ASP   B CG  1 
ATOM   1185 O OD1 . ASP   B 1 58 ? 21.873  -24.552 -32.460 1.00 32.73  ? 57  ASP   B OD1 1 
ATOM   1186 O OD2 . ASP   B 1 58 ? 23.800  -23.837 -31.620 1.00 34.73  ? 57  ASP   B OD2 1 
ATOM   1187 N N   . LEU   B 1 59 ? 22.261  -20.850 -36.335 1.00 25.38  ? 58  LEU   B N   1 
ATOM   1188 C CA  . LEU   B 1 59 ? 21.951  -19.574 -36.983 1.00 26.26  ? 58  LEU   B CA  1 
ATOM   1189 C C   . LEU   B 1 59 ? 21.185  -19.788 -38.281 1.00 24.52  ? 58  LEU   B C   1 
ATOM   1190 O O   . LEU   B 1 59 ? 21.638  -20.484 -39.202 1.00 27.92  ? 58  LEU   B O   1 
ATOM   1191 C CB  . LEU   B 1 59 ? 23.260  -18.822 -37.193 1.00 25.99  ? 58  LEU   B CB  1 
ATOM   1192 C CG  . LEU   B 1 59 ? 24.105  -18.609 -35.943 1.00 25.07  ? 58  LEU   B CG  1 
ATOM   1193 C CD1 . LEU   B 1 59 ? 25.388  -17.882 -36.307 1.00 27.44  ? 58  LEU   B CD1 1 
ATOM   1194 C CD2 . LEU   B 1 59 ? 23.297  -17.710 -34.963 1.00 27.22  ? 58  LEU   B CD2 1 
ATOM   1195 N N   . PHE   B 1 60 ? 20.032  -19.171 -38.370 1.00 22.86  ? 59  PHE   B N   1 
ATOM   1196 C CA  . PHE   B 1 60 ? 19.055  -19.355 -39.426 1.00 24.86  ? 59  PHE   B CA  1 
ATOM   1197 C C   . PHE   B 1 60 ? 18.882  -18.007 -40.131 1.00 26.59  ? 59  PHE   B C   1 
ATOM   1198 O O   . PHE   B 1 60 ? 18.264  -17.103 -39.591 1.00 24.95  ? 59  PHE   B O   1 
ATOM   1199 C CB  . PHE   B 1 60 ? 17.722  -19.900 -38.887 1.00 23.56  ? 59  PHE   B CB  1 
ATOM   1200 C CG  . PHE   B 1 60 ? 17.845  -21.301 -38.298 1.00 23.66  ? 59  PHE   B CG  1 
ATOM   1201 C CD1 . PHE   B 1 60 ? 18.391  -21.461 -37.026 1.00 25.72  ? 59  PHE   B CD1 1 
ATOM   1202 C CD2 . PHE   B 1 60 ? 17.395  -22.404 -39.025 1.00 25.51  ? 59  PHE   B CD2 1 
ATOM   1203 C CE1 . PHE   B 1 60 ? 18.512  -22.743 -36.498 1.00 29.52  ? 59  PHE   B CE1 1 
ATOM   1204 C CE2 . PHE   B 1 60 ? 17.507  -23.681 -38.468 1.00 25.97  ? 59  PHE   B CE2 1 
ATOM   1205 C CZ  . PHE   B 1 60 ? 18.093  -23.834 -37.232 1.00 28.85  ? 59  PHE   B CZ  1 
ATOM   1206 N N   . PRO   B 1 61 ? 19.414  -17.784 -41.359 1.00 28.75  ? 60  PRO   B N   1 
ATOM   1207 C CA  . PRO   B 1 61 ? 19.209  -16.492 -42.032 1.00 28.10  ? 60  PRO   B CA  1 
ATOM   1208 C C   . PRO   B 1 61 ? 17.746  -16.008 -41.996 1.00 26.50  ? 60  PRO   B C   1 
ATOM   1209 O O   . PRO   B 1 61 ? 16.800  -16.740 -42.264 1.00 28.84  ? 60  PRO   B O   1 
ATOM   1210 C CB  . PRO   B 1 61 ? 19.699  -16.777 -43.476 1.00 29.90  ? 60  PRO   B CB  1 
ATOM   1211 C CG  . PRO   B 1 61 ? 20.747  -17.837 -43.307 1.00 37.99  ? 60  PRO   B CG  1 
ATOM   1212 C CD  . PRO   B 1 61 ? 20.199  -18.735 -42.165 1.00 32.30  ? 60  PRO   B CD  1 
ATOM   1213 N N   . TYR   B 1 62 ? 17.547  -14.718 -41.623 1.00 28.07  ? 61  TYR   B N   1 
ATOM   1214 C CA  . TYR   B 1 62 ? 16.232  -14.225 -41.312 1.00 28.27  ? 61  TYR   B CA  1 
ATOM   1215 C C   . TYR   B 1 62 ? 15.244  -14.257 -42.468 1.00 29.98  ? 61  TYR   B C   1 
ATOM   1216 O O   . TYR   B 1 62 ? 14.094  -14.635 -42.245 1.00 28.97  ? 61  TYR   B O   1 
ATOM   1217 C CB  . TYR   B 1 62 ? 16.367  -12.777 -40.815 1.00 31.32  ? 61  TYR   B CB  1 
ATOM   1218 C CG  . TYR   B 1 62 ? 15.056  -12.049 -40.566 1.00 31.90  ? 61  TYR   B CG  1 
ATOM   1219 C CD1 . TYR   B 1 62 ? 14.298  -12.298 -39.433 1.00 33.84  ? 61  TYR   B CD1 1 
ATOM   1220 C CD2 . TYR   B 1 62 ? 14.642  -11.031 -41.424 1.00 39.50  ? 61  TYR   B CD2 1 
ATOM   1221 C CE1 . TYR   B 1 62 ? 13.127  -11.603 -39.191 1.00 33.68  ? 61  TYR   B CE1 1 
ATOM   1222 C CE2 . TYR   B 1 62 ? 13.487  -10.302 -41.182 1.00 38.81  ? 61  TYR   B CE2 1 
ATOM   1223 C CZ  . TYR   B 1 62 ? 12.727  -10.605 -40.066 1.00 38.12  ? 61  TYR   B CZ  1 
ATOM   1224 O OH  . TYR   B 1 62 ? 11.589  -9.910  -39.864 1.00 40.56  ? 61  TYR   B OH  1 
ATOM   1225 N N   . ASP   B 1 63 ? 15.659  -13.791 -43.671 1.00 32.37  ? 62  ASP   B N   1 
ATOM   1226 C CA  . ASP   B 1 63 ? 14.756  -13.762 -44.821 1.00 40.54  ? 62  ASP   B CA  1 
ATOM   1227 C C   . ASP   B 1 63 ? 14.243  -15.163 -45.151 1.00 34.16  ? 62  ASP   B C   1 
ATOM   1228 O O   . ASP   B 1 63 ? 13.040  -15.378 -45.268 1.00 40.96  ? 62  ASP   B O   1 
ATOM   1229 C CB  . ASP   B 1 63 ? 15.340  -13.021 -46.012 1.00 45.39  ? 62  ASP   B CB  1 
ATOM   1230 C CG  . ASP   B 1 63 ? 15.098  -11.519 -46.048 1.00 61.21  ? 62  ASP   B CG  1 
ATOM   1231 O OD1 . ASP   B 1 63 ? 14.363  -10.996 -45.166 1.00 58.28  ? 62  ASP   B OD1 1 
ATOM   1232 O OD2 . ASP   B 1 63 ? 15.654  -10.875 -46.968 1.00 68.47  ? 62  ASP   B OD2 1 
ATOM   1233 N N   . LYS   B 1 64 ? 15.150  -16.133 -45.223 1.00 38.94  ? 63  LYS   B N   1 
ATOM   1234 C CA  . LYS   B 1 64 ? 14.760  -17.519 -45.436 1.00 37.73  ? 63  LYS   B CA  1 
ATOM   1235 C C   . LYS   B 1 64 ? 13.790  -18.022 -44.362 1.00 35.63  ? 63  LYS   B C   1 
ATOM   1236 O O   . LYS   B 1 64 ? 12.897  -18.809 -44.677 1.00 37.11  ? 63  LYS   B O   1 
ATOM   1237 C CB  . LYS   B 1 64 ? 15.987  -18.435 -45.504 1.00 41.57  ? 63  LYS   B CB  1 
ATOM   1238 C CG  . LYS   B 1 64 ? 15.653  -19.857 -45.948 1.00 42.53  ? 63  LYS   B CG  1 
ATOM   1239 C CD  . LYS   B 1 64 ? 16.819  -20.826 -45.832 1.00 48.70  ? 63  LYS   B CD  1 
ATOM   1240 C CE  . LYS   B 1 64 ? 16.627  -22.144 -46.561 1.00 48.34  ? 63  LYS   B CE  1 
ATOM   1241 N NZ  . LYS   B 1 64 ? 15.355  -22.840 -46.362 1.00 48.90  ? 63  LYS   B NZ  1 
ATOM   1242 N N   . SER   B 1 65 ? 13.934  -17.567 -43.108 1.00 32.69  ? 64  SER   B N   1 
ATOM   1243 C CA  . SER   B 1 65 ? 13.325  -18.327 -42.005 1.00 37.08  ? 64  SER   B CA  1 
ATOM   1244 C C   . SER   B 1 65 ? 12.175  -17.594 -41.301 1.00 35.64  ? 64  SER   B C   1 
ATOM   1245 O O   . SER   B 1 65 ? 11.502  -18.153 -40.439 1.00 35.35  ? 64  SER   B O   1 
ATOM   1246 C CB  . SER   B 1 65 ? 14.371  -18.838 -41.064 1.00 38.50  ? 64  SER   B CB  1 
ATOM   1247 O OG  . SER   B 1 65 ? 15.140  -17.776 -40.515 1.00 51.50  ? 64  SER   B OG  1 
ATOM   1248 N N   . LYS   B 1 66 ? 11.845  -16.372 -41.738 1.00 35.82  ? 65  LYS   B N   1 
ATOM   1249 C CA  . LYS   B 1 66 ? 10.956  -15.540 -40.935 1.00 36.26  ? 65  LYS   B CA  1 
ATOM   1250 C C   . LYS   B 1 66 ? 9.508   -16.047 -40.923 1.00 37.49  ? 65  LYS   B C   1 
ATOM   1251 O O   . LYS   B 1 66 ? 8.775   -15.878 -39.943 1.00 40.02  ? 65  LYS   B O   1 
ATOM   1252 C CB  . LYS   B 1 66 ? 11.090  -14.066 -41.343 1.00 33.34  ? 65  LYS   B CB  1 
ATOM   1253 C CG  . LYS   B 1 66 ? 10.559  -13.784 -42.759 1.00 37.60  ? 65  LYS   B CG  1 
ATOM   1254 N N   . ASP   B 1 67 ? 9.036   -16.661 -42.006 1.00 38.93  ? 66  ASP   B N   1 
ATOM   1255 C CA  . ASP   B 1 67 ? 7.639   -17.056 -41.937 1.00 44.82  ? 66  ASP   B CA  1 
ATOM   1256 C C   . ASP   B 1 67 ? 7.494   -18.284 -41.033 1.00 44.60  ? 66  ASP   B C   1 
ATOM   1257 O O   . ASP   B 1 67 ? 6.451   -18.476 -40.399 1.00 49.66  ? 66  ASP   B O   1 
ATOM   1258 C CB  . ASP   B 1 67 ? 6.927   -17.018 -43.282 1.00 61.26  ? 66  ASP   B CB  1 
ATOM   1259 C CG  . ASP   B 1 67 ? 7.499   -17.917 -44.365 1.00 72.36  ? 66  ASP   B CG  1 
ATOM   1260 O OD1 . ASP   B 1 67 ? 7.804   -17.393 -45.463 1.00 80.17  ? 66  ASP   B OD1 1 
ATOM   1261 O OD2 . ASP   B 1 67 ? 7.632   -19.128 -44.100 1.00 84.54  ? 66  ASP   B OD2 1 
ATOM   1262 N N   . LYS   B 1 68 ? 8.567   -19.073 -40.932 1.00 40.28  ? 67  LYS   B N   1 
ATOM   1263 C CA  . LYS   B 1 68 ? 8.553   -20.236 -40.059 1.00 37.42  ? 67  LYS   B CA  1 
ATOM   1264 C C   . LYS   B 1 68 ? 8.727   -19.867 -38.582 1.00 35.41  ? 67  LYS   B C   1 
ATOM   1265 O O   . LYS   B 1 68 ? 7.992   -20.393 -37.741 1.00 36.50  ? 67  LYS   B O   1 
ATOM   1266 C CB  . LYS   B 1 68 ? 9.620   -21.245 -40.495 1.00 38.31  ? 67  LYS   B CB  1 
ATOM   1267 C CG  . LYS   B 1 68 ? 9.685   -22.507 -39.650 1.00 42.19  ? 67  LYS   B CG  1 
ATOM   1268 C CD  . LYS   B 1 68 ? 10.807  -23.389 -40.181 1.00 50.55  ? 67  LYS   B CD  1 
ATOM   1269 C CE  . LYS   B 1 68 ? 10.960  -24.679 -39.442 1.00 52.79  ? 67  LYS   B CE  1 
ATOM   1270 N NZ  . LYS   B 1 68 ? 9.861   -25.592 -39.756 1.00 55.13  ? 67  LYS   B NZ  1 
ATOM   1271 N N   . TYR   B 1 69 ? 9.700   -18.999 -38.258 1.00 33.38  ? 68  TYR   B N   1 
ATOM   1272 C CA  . TYR   B 1 69 ? 10.076  -18.749 -36.864 1.00 28.17  ? 68  TYR   B CA  1 
ATOM   1273 C C   . TYR   B 1 69 ? 9.556   -17.406 -36.362 1.00 30.71  ? 68  TYR   B C   1 
ATOM   1274 O O   . TYR   B 1 69 ? 9.624   -17.170 -35.158 1.00 35.77  ? 68  TYR   B O   1 
ATOM   1275 C CB  . TYR   B 1 69 ? 11.591  -18.776 -36.659 1.00 28.64  ? 68  TYR   B CB  1 
ATOM   1276 C CG  . TYR   B 1 69 ? 12.216  -20.136 -36.933 1.00 30.34  ? 68  TYR   B CG  1 
ATOM   1277 C CD1 . TYR   B 1 69 ? 11.689  -21.286 -36.351 1.00 30.67  ? 68  TYR   B CD1 1 
ATOM   1278 C CD2 . TYR   B 1 69 ? 13.298  -20.261 -37.799 1.00 31.69  ? 68  TYR   B CD2 1 
ATOM   1279 C CE1 . TYR   B 1 69 ? 12.246  -22.535 -36.609 1.00 32.75  ? 68  TYR   B CE1 1 
ATOM   1280 C CE2 . TYR   B 1 69 ? 13.840  -21.508 -38.084 1.00 32.24  ? 68  TYR   B CE2 1 
ATOM   1281 C CZ  . TYR   B 1 69 ? 13.347  -22.635 -37.435 1.00 30.88  ? 68  TYR   B CZ  1 
ATOM   1282 O OH  . TYR   B 1 69 ? 13.875  -23.844 -37.753 1.00 34.60  ? 68  TYR   B OH  1 
ATOM   1283 N N   . GLY   B 1 70 ? 9.110   -16.522 -37.275 1.00 35.84  ? 69  GLY   B N   1 
ATOM   1284 C CA  . GLY   B 1 70 ? 8.831   -15.152 -36.869 1.00 38.74  ? 69  GLY   B CA  1 
ATOM   1285 C C   . GLY   B 1 70 ? 7.425   -14.936 -36.297 1.00 43.59  ? 69  GLY   B C   1 
ATOM   1286 O O   . GLY   B 1 70 ? 6.829   -13.876 -36.531 1.00 44.21  ? 69  GLY   B O   1 
ATOM   1287 N N   . LYS   B 1 71 ? 6.910   -15.914 -35.532 1.00 42.27  ? 70  LYS   B N   1 
ATOM   1288 C CA  . LYS   B 1 71 ? 5.556   -15.833 -35.014 1.00 48.16  ? 70  LYS   B CA  1 
ATOM   1289 C C   . LYS   B 1 71 ? 5.603   -15.386 -33.565 1.00 52.29  ? 70  LYS   B C   1 
ATOM   1290 O O   . LYS   B 1 71 ? 6.450   -15.868 -32.812 1.00 45.54  ? 70  LYS   B O   1 
ATOM   1291 C CB  . LYS   B 1 71 ? 4.898   -17.205 -34.836 1.00 49.61  ? 70  LYS   B CB  1 
ATOM   1292 C CG  . LYS   B 1 71 ? 3.885   -17.611 -35.896 1.00 62.50  ? 70  LYS   B CG  1 
ATOM   1293 C CD  . LYS   B 1 71 ? 4.483   -17.807 -37.282 1.00 59.56  ? 70  LYS   B CD  1 
ATOM   1294 C CE  . LYS   B 1 71 ? 3.478   -18.419 -38.206 1.00 66.40  ? 70  LYS   B CE  1 
ATOM   1295 N NZ  . LYS   B 1 71 ? 3.962   -18.423 -39.587 1.00 74.79  ? 70  LYS   B NZ  1 
ATOM   1296 N N   . PRO   B 1 72 ? 4.696   -14.483 -33.123 1.00 48.14  ? 71  PRO   B N   1 
ATOM   1297 C CA  . PRO   B 1 72 ? 4.609   -14.158 -31.697 1.00 45.45  ? 71  PRO   B CA  1 
ATOM   1298 C C   . PRO   B 1 72 ? 4.407   -15.376 -30.795 1.00 40.99  ? 71  PRO   B C   1 
ATOM   1299 O O   . PRO   B 1 72 ? 3.834   -16.381 -31.208 1.00 44.17  ? 71  PRO   B O   1 
ATOM   1300 C CB  . PRO   B 1 72 ? 3.464   -13.134 -31.648 1.00 42.39  ? 71  PRO   B CB  1 
ATOM   1301 C CG  . PRO   B 1 72 ? 3.576   -12.468 -33.003 1.00 44.33  ? 71  PRO   B CG  1 
ATOM   1302 C CD  . PRO   B 1 72 ? 3.820   -13.640 -33.956 1.00 39.01  ? 71  PRO   B CD  1 
ATOM   1303 N N   . ASN   B 1 73 ? 4.955   -15.280 -29.579 1.00 43.95  ? 72  ASN   B N   1 
ATOM   1304 C CA  . ASN   B 1 73 ? 4.799   -16.281 -28.533 1.00 35.93  ? 72  ASN   B CA  1 
ATOM   1305 C C   . ASN   B 1 73 ? 4.733   -15.529 -27.192 1.00 43.95  ? 72  ASN   B C   1 
ATOM   1306 O O   . ASN   B 1 73 ? 4.719   -14.290 -27.169 1.00 48.57  ? 72  ASN   B O   1 
ATOM   1307 C CB  . ASN   B 1 73 ? 5.887   -17.358 -28.545 1.00 39.48  ? 72  ASN   B CB  1 
ATOM   1308 C CG  . ASN   B 1 73 ? 7.282   -16.842 -28.245 1.00 36.31  ? 72  ASN   B CG  1 
ATOM   1309 O OD1 . ASN   B 1 73 ? 7.485   -16.061 -27.303 1.00 32.23  ? 72  ASN   B OD1 1 
ATOM   1310 N ND2 . ASN   B 1 73 ? 8.267   -17.255 -29.044 1.00 30.47  ? 72  ASN   B ND2 1 
ATOM   1311 N N   . LYS   B 1 74 ? 4.760   -16.271 -26.082 1.00 41.19  ? 73  LYS   B N   1 
ATOM   1312 C CA  . LYS   B 1 74 ? 4.676   -15.666 -24.752 1.00 46.24  ? 73  LYS   B CA  1 
ATOM   1313 C C   . LYS   B 1 74 ? 5.996   -15.700 -23.954 1.00 44.73  ? 73  LYS   B C   1 
ATOM   1314 O O   . LYS   B 1 74 ? 5.992   -15.653 -22.713 1.00 39.80  ? 73  LYS   B O   1 
ATOM   1315 C CB  . LYS   B 1 74 ? 3.524   -16.339 -23.993 1.00 45.53  ? 73  LYS   B CB  1 
ATOM   1316 C CG  . LYS   B 1 74 ? 3.797   -17.803 -23.677 1.00 54.91  ? 73  LYS   B CG  1 
ATOM   1317 C CD  . LYS   B 1 74 ? 2.587   -18.682 -23.965 1.00 51.90  ? 73  LYS   B CD  1 
ATOM   1318 N N   . ARG   B 1 75 ? 7.146   -15.778 -24.641 1.00 33.38  ? 74  ARG   B N   1 
ATOM   1319 C CA  . ARG   B 1 75 ? 8.425   -15.582 -23.969 1.00 31.41  ? 74  ARG   B CA  1 
ATOM   1320 C C   . ARG   B 1 75 ? 8.678   -14.072 -23.818 1.00 29.62  ? 74  ARG   B C   1 
ATOM   1321 O O   . ARG   B 1 75 ? 8.402   -13.260 -24.705 1.00 30.54  ? 74  ARG   B O   1 
ATOM   1322 C CB  . ARG   B 1 75 ? 9.562   -16.318 -24.702 1.00 30.10  ? 74  ARG   B CB  1 
ATOM   1323 C CG  . ARG   B 1 75 ? 9.458   -17.836 -24.859 1.00 28.18  ? 74  ARG   B CG  1 
ATOM   1324 C CD  . ARG   B 1 75 ? 9.359   -18.607 -23.519 1.00 30.76  ? 74  ARG   B CD  1 
ATOM   1325 N NE  . ARG   B 1 75 ? 9.515   -20.046 -23.762 1.00 28.84  ? 74  ARG   B NE  1 
ATOM   1326 C CZ  . ARG   B 1 75 ? 10.650  -20.684 -23.597 1.00 28.40  ? 74  ARG   B CZ  1 
ATOM   1327 N NH1 . ARG   B 1 75 ? 11.710  -20.012 -23.151 1.00 32.80  ? 74  ARG   B NH1 1 
ATOM   1328 N NH2 . ARG   B 1 75 ? 10.737  -21.972 -23.931 1.00 31.77  ? 74  ARG   B NH2 1 
ATOM   1329 N N   . LYS   B 1 76 ? 9.145   -13.682 -22.623 1.00 29.46  ? 75  LYS   B N   1 
ATOM   1330 C CA  . LYS   B 1 76 ? 9.559   -12.330 -22.309 1.00 26.08  ? 75  LYS   B CA  1 
ATOM   1331 C C   . LYS   B 1 76 ? 10.584  -11.794 -23.316 1.00 26.16  ? 75  LYS   B C   1 
ATOM   1332 O O   . LYS   B 1 76 ? 11.678  -12.373 -23.436 1.00 28.02  ? 75  LYS   B O   1 
ATOM   1333 C CB  . LYS   B 1 76 ? 10.080  -12.235 -20.865 1.00 29.21  ? 75  LYS   B CB  1 
ATOM   1334 C CG  . LYS   B 1 76 ? 10.403  -10.790 -20.465 1.00 31.89  ? 75  LYS   B CG  1 
ATOM   1335 C CD  . LYS   B 1 76 ? 10.960  -10.711 -19.047 1.00 32.93  ? 75  LYS   B CD  1 
ATOM   1336 C CE  . LYS   B 1 76 ? 11.122  -9.268  -18.638 1.00 38.44  ? 75  LYS   B CE  1 
ATOM   1337 N NZ  . LYS   B 1 76 ? 11.607  -9.145  -17.252 1.00 48.01  ? 75  LYS   B NZ  1 
ATOM   1338 N N   . GLY   B 1 77 ? 10.158  -10.711 -23.989 1.00 26.34  ? 76  GLY   B N   1 
ATOM   1339 C CA  . GLY   B 1 77 ? 11.015  -9.943  -24.913 1.00 26.04  ? 76  GLY   B CA  1 
ATOM   1340 C C   . GLY   B 1 77 ? 10.878  -10.370 -26.370 1.00 29.72  ? 76  GLY   B C   1 
ATOM   1341 O O   . GLY   B 1 77 ? 11.440  -9.735  -27.254 1.00 29.73  ? 76  GLY   B O   1 
ATOM   1342 N N   . PHE   B 1 78 ? 10.197  -11.482 -26.628 1.00 27.45  ? 77  PHE   B N   1 
ATOM   1343 C CA  . PHE   B 1 78 ? 10.113  -11.989 -28.006 1.00 26.96  ? 77  PHE   B CA  1 
ATOM   1344 C C   . PHE   B 1 78 ? 9.353   -11.030 -28.931 1.00 30.08  ? 77  PHE   B C   1 
ATOM   1345 O O   . PHE   B 1 78 ? 9.786   -10.776 -30.065 1.00 28.45  ? 77  PHE   B O   1 
ATOM   1346 C CB  . PHE   B 1 78 ? 9.404   -13.348 -27.989 1.00 24.26  ? 77  PHE   B CB  1 
ATOM   1347 C CG  . PHE   B 1 78 ? 9.606   -14.079 -29.296 1.00 25.62  ? 77  PHE   B CG  1 
ATOM   1348 C CD1 . PHE   B 1 78 ? 10.731  -14.883 -29.448 1.00 24.62  ? 77  PHE   B CD1 1 
ATOM   1349 C CD2 . PHE   B 1 78 ? 8.675   -13.961 -30.329 1.00 28.66  ? 77  PHE   B CD2 1 
ATOM   1350 C CE1 . PHE   B 1 78 ? 10.944  -15.559 -30.665 1.00 23.99  ? 77  PHE   B CE1 1 
ATOM   1351 C CE2 . PHE   B 1 78 ? 8.884   -14.653 -31.530 1.00 31.21  ? 77  PHE   B CE2 1 
ATOM   1352 C CZ  . PHE   B 1 78 ? 10.013  -15.433 -31.670 1.00 27.85  ? 77  PHE   B CZ  1 
ATOM   1353 N N   . ASN   B 1 79 ? 8.190   -10.524 -28.519 1.00 32.77  ? 78  ASN   B N   1 
ATOM   1354 C CA  . ASN   B 1 79 ? 7.398   -9.694  -29.418 1.00 31.42  ? 78  ASN   B CA  1 
ATOM   1355 C C   . ASN   B 1 79 ? 8.116   -8.351  -29.632 1.00 31.15  ? 78  ASN   B C   1 
ATOM   1356 O O   . ASN   B 1 79 ? 8.107   -7.823  -30.750 1.00 32.06  ? 78  ASN   B O   1 
ATOM   1357 C CB  . ASN   B 1 79 ? 5.923   -9.639  -29.003 1.00 36.21  ? 78  ASN   B CB  1 
ATOM   1358 C CG  . ASN   B 1 79 ? 5.190   -10.965 -29.106 1.00 38.19  ? 78  ASN   B CG  1 
ATOM   1359 O OD1 . ASN   B 1 79 ? 5.655   -11.912 -29.747 1.00 38.60  ? 78  ASN   B OD1 1 
ATOM   1360 N ND2 . ASN   B 1 79 ? 4.056   -11.099 -28.432 1.00 43.36  ? 78  ASN   B ND2 1 
ATOM   1361 N N   . GLU   B 1 80 ? 8.827   -7.854  -28.612 1.00 28.85  ? 79  GLU   B N   1 
ATOM   1362 C CA  . GLU   B 1 80 ? 9.612   -6.637  -28.774 1.00 30.95  ? 79  GLU   B CA  1 
ATOM   1363 C C   . GLU   B 1 80 ? 10.757  -6.905  -29.752 1.00 30.10  ? 79  GLU   B C   1 
ATOM   1364 O O   . GLU   B 1 80 ? 11.071  -6.020  -30.566 1.00 27.31  ? 79  GLU   B O   1 
ATOM   1365 C CB  . GLU   B 1 80 ? 10.196  -6.137  -27.454 1.00 29.86  ? 79  GLU   B CB  1 
ATOM   1366 C CG  . GLU   B 1 80 ? 9.131   -5.583  -26.510 1.00 41.62  ? 79  GLU   B CG  1 
ATOM   1367 N N   . GLY   B 1 81 ? 11.336  -8.129  -29.664 1.00 28.67  ? 80  GLY   B N   1 
ATOM   1368 C CA  . GLY   B 1 81 ? 12.426  -8.562  -30.540 1.00 30.52  ? 80  GLY   B CA  1 
ATOM   1369 C C   . GLY   B 1 81 ? 11.981  -8.634  -32.002 1.00 29.59  ? 80  GLY   B C   1 
ATOM   1370 O O   . GLY   B 1 81 ? 12.722  -8.220  -32.908 1.00 25.98  ? 80  GLY   B O   1 
ATOM   1371 N N   . LEU   B 1 82 ? 10.756  -9.076  -32.238 1.00 27.14  ? 81  LEU   B N   1 
ATOM   1372 C CA  . LEU   B 1 82 ? 10.171  -9.109  -33.579 1.00 26.80  ? 81  LEU   B CA  1 
ATOM   1373 C C   . LEU   B 1 82 ? 10.046  -7.680  -34.091 1.00 27.59  ? 81  LEU   B C   1 
ATOM   1374 O O   . LEU   B 1 82 ? 10.335  -7.412  -35.257 1.00 29.61  ? 81  LEU   B O   1 
ATOM   1375 C CB  . LEU   B 1 82 ? 8.825   -9.839  -33.622 1.00 27.58  ? 81  LEU   B CB  1 
ATOM   1376 C CG  . LEU   B 1 82 ? 8.862   -11.354 -33.396 1.00 28.17  ? 81  LEU   B CG  1 
ATOM   1377 C CD1 . LEU   B 1 82 ? 7.454   -11.946 -33.444 1.00 29.49  ? 81  LEU   B CD1 1 
ATOM   1378 C CD2 . LEU   B 1 82 ? 9.805   -12.053 -34.371 1.00 28.40  ? 81  LEU   B CD2 1 
ATOM   1379 N N   . TRP   B 1 83 ? 9.643   -6.759  -33.202 1.00 27.67  ? 82  TRP   B N   1 
ATOM   1380 C CA  . TRP   B 1 83 ? 9.510   -5.366  -33.605 1.00 31.22  ? 82  TRP   B CA  1 
ATOM   1381 C C   . TRP   B 1 83 ? 10.867  -4.807  -34.049 1.00 30.89  ? 82  TRP   B C   1 
ATOM   1382 O O   . TRP   B 1 83 ? 10.953  -4.189  -35.121 1.00 27.95  ? 82  TRP   B O   1 
ATOM   1383 C CB  . TRP   B 1 83 ? 8.895   -4.530  -32.468 1.00 33.61  ? 82  TRP   B CB  1 
ATOM   1384 C CG  . TRP   B 1 83 ? 8.557   -3.144  -32.959 1.00 29.86  ? 82  TRP   B CG  1 
ATOM   1385 C CD1 . TRP   B 1 83 ? 7.406   -2.749  -33.577 1.00 39.63  ? 82  TRP   B CD1 1 
ATOM   1386 C CD2 . TRP   B 1 83 ? 9.455   -2.020  -33.019 1.00 34.18  ? 82  TRP   B CD2 1 
ATOM   1387 N NE1 . TRP   B 1 83 ? 7.509   -1.436  -33.968 1.00 41.84  ? 82  TRP   B NE1 1 
ATOM   1388 C CE2 . TRP   B 1 83 ? 8.751   -0.968  -33.639 1.00 35.46  ? 82  TRP   B CE2 1 
ATOM   1389 C CE3 . TRP   B 1 83 ? 10.761  -1.795  -32.572 1.00 32.24  ? 82  TRP   B CE3 1 
ATOM   1390 C CZ2 . TRP   B 1 83 ? 9.324   0.291   -33.829 1.00 35.71  ? 82  TRP   B CZ2 1 
ATOM   1391 C CZ3 . TRP   B 1 83 ? 11.331  -0.553  -32.764 1.00 36.38  ? 82  TRP   B CZ3 1 
ATOM   1392 C CH2 . TRP   B 1 83 ? 10.617  0.465   -33.400 1.00 31.71  ? 82  TRP   B CH2 1 
ATOM   1393 N N   . GLU   B 1 84 ? 11.917  -5.065  -33.250 1.00 25.60  ? 83  GLU   B N   1 
ATOM   1394 C CA  . GLU   B 1 84 ? 13.236  -4.502  -33.484 1.00 28.01  ? 83  GLU   B CA  1 
ATOM   1395 C C   . GLU   B 1 84 ? 13.834  -5.005  -34.806 1.00 26.79  ? 83  GLU   B C   1 
ATOM   1396 O O   . GLU   B 1 84 ? 14.411  -4.223  -35.554 1.00 27.39  ? 83  GLU   B O   1 
ATOM   1397 C CB  . GLU   B 1 84 ? 14.150  -4.799  -32.310 1.00 26.33  ? 83  GLU   B CB  1 
ATOM   1398 C CG  . GLU   B 1 84 ? 13.683  -4.071  -31.043 1.00 29.84  ? 83  GLU   B CG  1 
ATOM   1399 C CD  . GLU   B 1 84 ? 14.551  -4.392  -29.859 1.00 30.49  ? 83  GLU   B CD  1 
ATOM   1400 O OE1 . GLU   B 1 84 ? 15.496  -5.237  -29.957 1.00 27.84  ? 83  GLU   B OE1 1 
ATOM   1401 O OE2 . GLU   B 1 84 ? 14.296  -3.758  -28.777 1.00 31.06  ? 83  GLU   B OE2 1 
ATOM   1402 N N   . ILE   B 1 85 ? 13.711  -6.304  -35.059 1.00 27.12  ? 84  ILE   B N   1 
ATOM   1403 C CA  . ILE   B 1 85 ? 14.340  -6.906  -36.242 1.00 24.12  ? 84  ILE   B CA  1 
ATOM   1404 C C   . ILE   B 1 85 ? 13.723  -6.346  -37.525 1.00 26.58  ? 84  ILE   B C   1 
ATOM   1405 O O   . ILE   B 1 85 ? 14.461  -6.146  -38.520 1.00 26.07  ? 84  ILE   B O   1 
ATOM   1406 C CB  . ILE   B 1 85 ? 14.332  -8.447  -36.180 1.00 25.86  ? 84  ILE   B CB  1 
ATOM   1407 N N   . GLN   B 1 86 ? 12.415  -6.106  -37.474 1.00 28.34  ? 85  GLN   B N   1 
ATOM   1408 C CA  . GLN   B 1 86 ? 11.580  -5.556  -38.533 1.00 29.50  ? 85  GLN   B CA  1 
ATOM   1409 C C   . GLN   B 1 86 ? 11.859  -4.054  -38.715 1.00 33.63  ? 85  GLN   B C   1 
ATOM   1410 O O   . GLN   B 1 86 ? 11.925  -3.566  -39.850 1.00 34.94  ? 85  GLN   B O   1 
ATOM   1411 C CB  . GLN   B 1 86 ? 10.115  -5.894  -38.228 1.00 34.66  ? 85  GLN   B CB  1 
ATOM   1412 C CG  . GLN   B 1 86 ? 9.679   -7.328  -38.564 1.00 47.40  ? 85  GLN   B CG  1 
ATOM   1413 C CD  . GLN   B 1 86 ? 8.482   -7.896  -37.805 1.00 50.86  ? 85  GLN   B CD  1 
ATOM   1414 O OE1 . GLN   B 1 86 ? 7.376   -7.329  -37.738 1.00 56.84  ? 85  GLN   B OE1 1 
ATOM   1415 N NE2 . GLN   B 1 86 ? 8.686   -9.079  -37.238 1.00 46.04  ? 85  GLN   B NE2 1 
ATOM   1416 N N   . ASN   B 1 87 ? 11.982  -3.292  -37.620 1.00 28.38  ? 86  ASN   B N   1 
ATOM   1417 C CA  . ASN   B 1 87 ? 11.856  -1.837  -37.782 1.00 25.95  ? 86  ASN   B CA  1 
ATOM   1418 C C   . ASN   B 1 87 ? 13.168  -1.083  -37.565 1.00 27.75  ? 86  ASN   B C   1 
ATOM   1419 O O   . ASN   B 1 87 ? 13.319  0.054   -38.058 1.00 28.28  ? 86  ASN   B O   1 
ATOM   1420 C CB  . ASN   B 1 87 ? 10.821  -1.266  -36.805 1.00 30.84  ? 86  ASN   B CB  1 
ATOM   1421 C CG  . ASN   B 1 87 ? 9.441   -1.743  -37.197 1.00 36.12  ? 86  ASN   B CG  1 
ATOM   1422 O OD1 . ASN   B 1 87 ? 8.843   -1.244  -38.158 1.00 44.21  ? 86  ASN   B OD1 1 
ATOM   1423 N ND2 . ASN   B 1 87 ? 8.947   -2.774  -36.537 1.00 40.65  ? 86  ASN   B ND2 1 
ATOM   1424 N N   . ASN   B 1 88 ? 14.118  -1.636  -36.825 1.00 29.50  ? 87  ASN   B N   1 
ATOM   1425 C CA  . ASN   B 1 88 ? 15.371  -0.929  -36.599 1.00 27.43  ? 87  ASN   B CA  1 
ATOM   1426 C C   . ASN   B 1 88 ? 16.463  -1.919  -36.203 1.00 27.57  ? 87  ASN   B C   1 
ATOM   1427 O O   . ASN   B 1 88 ? 17.086  -1.864  -35.145 1.00 26.98  ? 87  ASN   B O   1 
ATOM   1428 C CB  . ASN   B 1 88 ? 15.200  0.292   -35.685 1.00 32.58  ? 87  ASN   B CB  1 
ATOM   1429 C CG  . ASN   B 1 88 ? 16.324  1.289   -35.829 1.00 30.51  ? 87  ASN   B CG  1 
ATOM   1430 O OD1 . ASN   B 1 88 ? 17.331  1.042   -36.500 1.00 32.66  ? 87  ASN   B OD1 1 
ATOM   1431 N ND2 . ASN   B 1 88 ? 16.185  2.435   -35.180 1.00 34.21  ? 87  ASN   B ND2 1 
ATOM   1432 N N   . PRO   B 1 89 ? 16.732  -2.909  -37.091 1.00 27.21  ? 88  PRO   B N   1 
ATOM   1433 C CA  . PRO   B 1 89 ? 17.659  -3.982  -36.732 1.00 24.45  ? 88  PRO   B CA  1 
ATOM   1434 C C   . PRO   B 1 89 ? 19.089  -3.538  -36.458 1.00 23.66  ? 88  PRO   B C   1 
ATOM   1435 O O   . PRO   B 1 89 ? 19.890  -4.272  -35.888 1.00 25.29  ? 88  PRO   B O   1 
ATOM   1436 C CB  . PRO   B 1 89 ? 17.597  -4.914  -37.984 1.00 25.79  ? 88  PRO   B CB  1 
ATOM   1437 C CG  . PRO   B 1 89 ? 17.090  -4.026  -39.148 1.00 23.61  ? 88  PRO   B CG  1 
ATOM   1438 C CD  . PRO   B 1 89 ? 16.217  -2.985  -38.473 1.00 28.13  ? 88  PRO   B CD  1 
ATOM   1439 N N   . HIS   B 1 90 ? 19.455  -2.333  -36.975 1.00 23.72  ? 89  HIS   B N   1 
ATOM   1440 C CA  . HIS   B 1 90 ? 20.855  -1.940  -36.902 1.00 25.14  ? 89  HIS   B CA  1 
ATOM   1441 C C   . HIS   B 1 90 ? 21.142  -0.847  -35.861 1.00 27.98  ? 89  HIS   B C   1 
ATOM   1442 O O   . HIS   B 1 90 ? 22.300  -0.421  -35.738 1.00 28.10  ? 89  HIS   B O   1 
ATOM   1443 C CB  . HIS   B 1 90 ? 21.431  -1.512  -38.270 1.00 25.44  ? 89  HIS   B CB  1 
ATOM   1444 C CG  . HIS   B 1 90 ? 21.291  -2.604  -39.281 1.00 28.56  ? 89  HIS   B CG  1 
ATOM   1445 N ND1 . HIS   B 1 90 ? 21.912  -3.827  -39.165 1.00 26.14  ? 89  HIS   B ND1 1 
ATOM   1446 C CD2 . HIS   B 1 90 ? 20.571  -2.645  -40.409 1.00 26.75  ? 89  HIS   B CD2 1 
ATOM   1447 C CE1 . HIS   B 1 90 ? 21.586  -4.566  -40.213 1.00 25.73  ? 89  HIS   B CE1 1 
ATOM   1448 N NE2 . HIS   B 1 90 ? 20.751  -3.885  -40.966 1.00 26.68  ? 89  HIS   B NE2 1 
ATOM   1449 N N   . ALA   B 1 91 ? 20.121  -0.530  -35.057 1.00 27.38  ? 90  ALA   B N   1 
ATOM   1450 C CA  . ALA   B 1 91 ? 20.272  0.467   -34.000 1.00 27.78  ? 90  ALA   B CA  1 
ATOM   1451 C C   . ALA   B 1 91 ? 21.239  0.049   -32.899 1.00 34.40  ? 90  ALA   B C   1 
ATOM   1452 O O   . ALA   B 1 91 ? 21.510  -1.125  -32.627 1.00 29.97  ? 90  ALA   B O   1 
ATOM   1453 C CB  . ALA   B 1 91 ? 18.931  0.864   -33.433 1.00 29.28  ? 90  ALA   B CB  1 
ATOM   1454 N N   . SER   B 1 92 ? 21.729  1.085   -32.190 1.00 33.19  ? 91  SER   B N   1 
ATOM   1455 C CA  . SER   B 1 92 ? 22.379  0.909   -30.918 1.00 36.07  ? 91  SER   B CA  1 
ATOM   1456 C C   . SER   B 1 92 ? 21.305  0.686   -29.851 1.00 36.84  ? 91  SER   B C   1 
ATOM   1457 O O   . SER   B 1 92 ? 20.404  1.524   -29.693 1.00 39.02  ? 91  SER   B O   1 
ATOM   1458 C CB  . SER   B 1 92 ? 23.158  2.176   -30.593 1.00 40.34  ? 91  SER   B CB  1 
ATOM   1459 O OG  . SER   B 1 92 ? 23.509  2.110   -29.229 1.00 41.07  ? 91  SER   B OG  1 
ATOM   1460 N N   . TYR   B 1 93 ? 21.453  -0.428  -29.117 1.00 33.55  ? 92  TYR   B N   1 
ATOM   1461 C CA  . TYR   B 1 93 ? 20.574  -0.858  -28.038 1.00 38.48  ? 92  TYR   B CA  1 
ATOM   1462 C C   . TYR   B 1 93 ? 21.327  -0.735  -26.716 1.00 46.02  ? 92  TYR   B C   1 
ATOM   1463 O O   . TYR   B 1 93 ? 20.966  -1.373  -25.728 1.00 48.54  ? 92  TYR   B O   1 
ATOM   1464 C CB  . TYR   B 1 93 ? 19.999  -2.260  -28.290 1.00 31.57  ? 92  TYR   B CB  1 
ATOM   1465 C CG  . TYR   B 1 93 ? 18.984  -2.210  -29.420 1.00 29.14  ? 92  TYR   B CG  1 
ATOM   1466 C CD1 . TYR   B 1 93 ? 17.677  -1.801  -29.174 1.00 30.70  ? 92  TYR   B CD1 1 
ATOM   1467 C CD2 . TYR   B 1 93 ? 19.311  -2.568  -30.734 1.00 32.00  ? 92  TYR   B CD2 1 
ATOM   1468 C CE1 . TYR   B 1 93 ? 16.745  -1.669  -30.188 1.00 32.26  ? 92  TYR   B CE1 1 
ATOM   1469 C CE2 . TYR   B 1 93 ? 18.377  -2.425  -31.755 1.00 28.06  ? 92  TYR   B CE2 1 
ATOM   1470 C CZ  . TYR   B 1 93 ? 17.088  -2.018  -31.481 1.00 31.77  ? 92  TYR   B CZ  1 
ATOM   1471 O OH  . TYR   B 1 93 ? 16.126  -1.878  -32.442 1.00 31.44  ? 92  TYR   B OH  1 
ATOM   1472 N N   . SER   B 1 94 ? 22.367  0.112   -26.735 1.00 54.04  ? 93  SER   B N   1 
ATOM   1473 C CA  . SER   B 1 94 ? 23.176  0.445   -25.572 1.00 64.69  ? 93  SER   B CA  1 
ATOM   1474 C C   . SER   B 1 94 ? 22.268  1.035   -24.484 1.00 73.79  ? 93  SER   B C   1 
ATOM   1475 O O   . SER   B 1 94 ? 21.606  2.053   -24.785 1.00 73.96  ? 93  SER   B O   1 
ATOM   1476 C CB  . SER   B 1 94 ? 24.279  1.421   -25.934 1.00 65.15  ? 93  SER   B CB  1 
ATOM   1477 O OG  . SER   B 1 94 ? 25.297  0.789   -26.698 1.00 66.59  ? 93  SER   B OG  1 
ATOM   1478 O OXT . SER   B 1 94 ? 22.236  0.442   -23.383 1.00 88.08  ? 93  SER   B OXT 1 
ATOM   1479 N N   . HIS   C 1 4  ? 32.477  -23.619 26.901  1.00 63.52  ? 3   HIS   C N   1 
ATOM   1480 C CA  . HIS   C 1 4  ? 31.734  -22.519 27.576  1.00 74.40  ? 3   HIS   C CA  1 
ATOM   1481 C C   . HIS   C 1 4  ? 31.138  -23.058 28.877  1.00 79.09  ? 3   HIS   C C   1 
ATOM   1482 O O   . HIS   C 1 4  ? 31.862  -23.611 29.707  1.00 76.51  ? 3   HIS   C O   1 
ATOM   1483 C CB  . HIS   C 1 4  ? 30.737  -21.867 26.605  1.00 74.42  ? 3   HIS   C CB  1 
ATOM   1484 N N   . ALA   C 1 5  ? 29.815  -22.894 29.028  1.00 79.90  ? 4   ALA   C N   1 
ATOM   1485 C CA  . ALA   C 1 5  ? 29.039  -23.376 30.161  1.00 70.63  ? 4   ALA   C CA  1 
ATOM   1486 C C   . ALA   C 1 5  ? 27.553  -23.211 29.861  1.00 73.19  ? 4   ALA   C C   1 
ATOM   1487 O O   . ALA   C 1 5  ? 27.149  -22.268 29.179  1.00 71.12  ? 4   ALA   C O   1 
ATOM   1488 C CB  . ALA   C 1 5  ? 29.389  -22.587 31.386  1.00 67.85  ? 4   ALA   C CB  1 
ATOM   1489 N N   . PHE   C 1 6  ? 26.744  -24.112 30.421  1.00 61.18  ? 5   PHE   C N   1 
ATOM   1490 C CA  . PHE   C 1 6  ? 25.361  -24.215 30.010  1.00 52.28  ? 5   PHE   C CA  1 
ATOM   1491 C C   . PHE   C 1 6  ? 24.474  -24.331 31.245  1.00 59.01  ? 5   PHE   C C   1 
ATOM   1492 O O   . PHE   C 1 6  ? 24.732  -25.159 32.116  1.00 72.56  ? 5   PHE   C O   1 
ATOM   1493 C CB  . PHE   C 1 6  ? 25.238  -25.422 29.061  1.00 47.91  ? 5   PHE   C CB  1 
ATOM   1494 C CG  . PHE   C 1 6  ? 25.980  -25.307 27.732  1.00 44.91  ? 5   PHE   C CG  1 
ATOM   1495 C CD1 . PHE   C 1 6  ? 27.092  -26.090 27.464  1.00 43.42  ? 5   PHE   C CD1 1 
ATOM   1496 C CD2 . PHE   C 1 6  ? 25.584  -24.400 26.747  1.00 50.03  ? 5   PHE   C CD2 1 
ATOM   1497 C CE1 . PHE   C 1 6  ? 27.773  -25.996 26.255  1.00 49.24  ? 5   PHE   C CE1 1 
ATOM   1498 C CE2 . PHE   C 1 6  ? 26.267  -24.315 25.537  1.00 46.11  ? 5   PHE   C CE2 1 
ATOM   1499 C CZ  . PHE   C 1 6  ? 27.354  -25.115 25.286  1.00 41.37  ? 5   PHE   C CZ  1 
ATOM   1500 N N   . LYS   C 1 7  ? 23.432  -23.496 31.308  1.00 53.16  ? 6   LYS   C N   1 
ATOM   1501 C CA  . LYS   C 1 7  ? 22.420  -23.593 32.351  1.00 53.93  ? 6   LYS   C CA  1 
ATOM   1502 C C   . LYS   C 1 7  ? 21.105  -23.949 31.670  1.00 49.79  ? 6   LYS   C C   1 
ATOM   1503 O O   . LYS   C 1 7  ? 21.001  -23.792 30.454  1.00 54.17  ? 6   LYS   C O   1 
ATOM   1504 C CB  . LYS   C 1 7  ? 22.335  -22.286 33.153  1.00 58.24  ? 6   LYS   C CB  1 
ATOM   1505 N N   . PRO   C 1 8  ? 20.072  -24.444 32.396  1.00 51.02  ? 7   PRO   C N   1 
ATOM   1506 C CA  . PRO   C 1 8  ? 18.775  -24.736 31.784  1.00 51.99  ? 7   PRO   C CA  1 
ATOM   1507 C C   . PRO   C 1 8  ? 18.279  -23.559 30.944  1.00 57.75  ? 7   PRO   C C   1 
ATOM   1508 O O   . PRO   C 1 8  ? 18.551  -22.400 31.265  1.00 60.96  ? 7   PRO   C O   1 
ATOM   1509 C CB  . PRO   C 1 8  ? 17.882  -25.030 32.999  1.00 57.24  ? 7   PRO   C CB  1 
ATOM   1510 C CG  . PRO   C 1 8  ? 18.843  -25.638 33.999  1.00 49.45  ? 7   PRO   C CG  1 
ATOM   1511 C CD  . PRO   C 1 8  ? 20.110  -24.784 33.833  1.00 49.72  ? 7   PRO   C CD  1 
ATOM   1512 N N   . GLY   C 1 9  ? 17.593  -23.879 29.838  1.00 57.45  ? 8   GLY   C N   1 
ATOM   1513 C CA  . GLY   C 1 9  ? 16.935  -22.870 29.025  1.00 51.28  ? 8   GLY   C CA  1 
ATOM   1514 C C   . GLY   C 1 9  ? 17.808  -22.365 27.876  1.00 49.20  ? 8   GLY   C C   1 
ATOM   1515 O O   . GLY   C 1 9  ? 17.262  -21.871 26.893  1.00 50.79  ? 8   GLY   C O   1 
ATOM   1516 N N   . ASP   C 1 10 ? 19.139  -22.511 27.999  1.00 43.38  ? 9   ASP   C N   1 
ATOM   1517 C CA  . ASP   C 1 10 ? 20.115  -22.137 26.989  1.00 37.03  ? 9   ASP   C CA  1 
ATOM   1518 C C   . ASP   C 1 10 ? 19.886  -22.870 25.657  1.00 37.28  ? 9   ASP   C C   1 
ATOM   1519 O O   . ASP   C 1 10 ? 19.729  -24.092 25.619  1.00 35.85  ? 9   ASP   C O   1 
ATOM   1520 C CB  . ASP   C 1 10 ? 21.547  -22.387 27.445  1.00 38.57  ? 9   ASP   C CB  1 
ATOM   1521 C CG  . ASP   C 1 10 ? 22.155  -21.444 28.485  1.00 49.55  ? 9   ASP   C CG  1 
ATOM   1522 O OD1 . ASP   C 1 10 ? 21.537  -20.409 28.765  1.00 50.57  ? 9   ASP   C OD1 1 
ATOM   1523 O OD2 . ASP   C 1 10 ? 23.252  -21.754 29.015  1.00 53.12  ? 9   ASP   C OD2 1 
ATOM   1524 N N   . LEU   C 1 11 ? 19.978  -22.120 24.553  1.00 37.91  ? 10  LEU   C N   1 
ATOM   1525 C CA  . LEU   C 1 11 ? 19.718  -22.650 23.223  1.00 35.36  ? 10  LEU   C CA  1 
ATOM   1526 C C   . LEU   C 1 11 ? 21.010  -23.105 22.559  1.00 30.67  ? 10  LEU   C C   1 
ATOM   1527 O O   . LEU   C 1 11 ? 21.998  -22.381 22.531  1.00 36.49  ? 10  LEU   C O   1 
ATOM   1528 C CB  . LEU   C 1 11 ? 19.016  -21.546 22.424  1.00 32.25  ? 10  LEU   C CB  1 
ATOM   1529 C CG  . LEU   C 1 11 ? 17.702  -21.054 23.032  1.00 32.99  ? 10  LEU   C CG  1 
ATOM   1530 C CD1 . LEU   C 1 11 ? 17.078  -20.092 22.021  1.00 35.72  ? 10  LEU   C CD1 1 
ATOM   1531 C CD2 . LEU   C 1 11 ? 16.782  -22.242 23.339  1.00 33.19  ? 10  LEU   C CD2 1 
ATOM   1532 N N   . VAL   C 1 12 ? 20.985  -24.295 21.893  1.00 29.61  ? 11  VAL   C N   1 
ATOM   1533 C CA  . VAL   C 1 12 ? 22.200  -24.901 21.379  1.00 29.95  ? 11  VAL   C CA  1 
ATOM   1534 C C   . VAL   C 1 12 ? 21.875  -25.645 20.065  1.00 30.90  ? 11  VAL   C C   1 
ATOM   1535 O O   . VAL   C 1 12 ? 20.692  -25.822 19.780  1.00 30.02  ? 11  VAL   C O   1 
ATOM   1536 C CB  . VAL   C 1 12 ? 22.837  -25.913 22.365  1.00 32.12  ? 11  VAL   C CB  1 
ATOM   1537 C CG1 . VAL   C 1 12 ? 23.235  -25.270 23.705  1.00 35.23  ? 11  VAL   C CG1 1 
ATOM   1538 C CG2 . VAL   C 1 12 ? 21.914  -27.111 22.595  1.00 33.88  ? 11  VAL   C CG2 1 
ATOM   1539 N N   . PHE   C 1 13 ? 22.933  -26.028 19.324  1.00 27.99  ? 12  PHE   C N   1 
ATOM   1540 C CA  . PHE   C 1 13 ? 22.920  -27.179 18.399  1.00 29.13  ? 12  PHE   C CA  1 
ATOM   1541 C C   . PHE   C 1 13 ? 23.616  -28.364 19.082  1.00 29.87  ? 12  PHE   C C   1 
ATOM   1542 O O   . PHE   C 1 13 ? 24.708  -28.230 19.676  1.00 29.53  ? 12  PHE   C O   1 
ATOM   1543 C CB  . PHE   C 1 13 ? 23.585  -26.904 17.045  1.00 30.57  ? 12  PHE   C CB  1 
ATOM   1544 C CG  . PHE   C 1 13 ? 22.805  -25.930 16.198  1.00 32.75  ? 12  PHE   C CG  1 
ATOM   1545 C CD1 . PHE   C 1 13 ? 21.766  -26.384 15.377  1.00 34.23  ? 12  PHE   C CD1 1 
ATOM   1546 C CD2 . PHE   C 1 13 ? 23.124  -24.569 16.196  1.00 33.80  ? 12  PHE   C CD2 1 
ATOM   1547 C CE1 . PHE   C 1 13 ? 21.033  -25.494 14.610  1.00 33.82  ? 12  PHE   C CE1 1 
ATOM   1548 C CE2 . PHE   C 1 13 ? 22.363  -23.685 15.449  1.00 36.97  ? 12  PHE   C CE2 1 
ATOM   1549 C CZ  . PHE   C 1 13 ? 21.342  -24.157 14.640  1.00 30.67  ? 12  PHE   C CZ  1 
ATOM   1550 N N   . ALA   C 1 14 ? 22.970  -29.548 19.057  1.00 26.89  ? 13  ALA   C N   1 
ATOM   1551 C CA  . ALA   C 1 14 ? 23.412  -30.715 19.811  1.00 24.47  ? 13  ALA   C CA  1 
ATOM   1552 C C   . ALA   C 1 14 ? 23.701  -31.835 18.819  1.00 30.67  ? 13  ALA   C C   1 
ATOM   1553 O O   . ALA   C 1 14 ? 22.844  -32.094 17.970  1.00 25.72  ? 13  ALA   C O   1 
ATOM   1554 C CB  . ALA   C 1 14 ? 22.324  -31.164 20.758  1.00 25.09  ? 13  ALA   C CB  1 
ATOM   1555 N N   . LYS   C 1 15 ? 24.894  -32.446 18.932  1.00 27.72  ? 14  LYS   C N   1 
ATOM   1556 C CA  . LYS   C 1 15 ? 25.305  -33.462 17.973  1.00 26.49  ? 14  LYS   C CA  1 
ATOM   1557 C C   . LYS   C 1 15 ? 25.308  -34.834 18.622  1.00 28.43  ? 14  LYS   C C   1 
ATOM   1558 O O   . LYS   C 1 15 ? 26.067  -35.112 19.552  1.00 30.54  ? 14  LYS   C O   1 
ATOM   1559 C CB  . LYS   C 1 15 ? 26.708  -33.139 17.435  1.00 28.95  ? 14  LYS   C CB  1 
ATOM   1560 C CG  . LYS   C 1 15 ? 27.190  -34.108 16.334  1.00 28.60  ? 14  LYS   C CG  1 
ATOM   1561 C CD  . LYS   C 1 15 ? 26.381  -33.966 15.047  1.00 27.76  ? 14  LYS   C CD  1 
ATOM   1562 C CE  . LYS   C 1 15 ? 26.849  -34.784 13.835  1.00 29.72  ? 14  LYS   C CE  1 
ATOM   1563 N NZ  . LYS   C 1 15 ? 26.770  -36.218 14.115  1.00 28.64  ? 14  LYS   C NZ  1 
ATOM   1564 N N   . MET   C 1 16 ? 24.538  -35.750 18.023  1.00 22.74  ? 15  MET   C N   1 
ATOM   1565 C CA  . MET   C 1 16 ? 24.599  -37.165 18.391  1.00 25.90  ? 15  MET   C CA  1 
ATOM   1566 C C   . MET   C 1 16 ? 25.087  -37.963 17.185  1.00 28.54  ? 15  MET   C C   1 
ATOM   1567 O O   . MET   C 1 16 ? 24.867  -37.577 16.039  1.00 27.57  ? 15  MET   C O   1 
ATOM   1568 C CB  . MET   C 1 16 ? 23.198  -37.701 18.705  1.00 27.60  ? 15  MET   C CB  1 
ATOM   1569 C CG  . MET   C 1 16 ? 22.413  -36.918 19.761  1.00 28.36  ? 15  MET   C CG  1 
ATOM   1570 S SD  . MET   C 1 16 ? 20.849  -37.704 20.215  1.00 34.81  ? 15  MET   C SD  1 
ATOM   1571 C CE  . MET   C 1 16 ? 19.857  -37.100 18.833  1.00 31.39  ? 15  MET   C CE  1 
ATOM   1572 N N   . LYS   C 1 17 ? 25.692  -39.132 17.431  1.00 26.54  ? 16  LYS   C N   1 
ATOM   1573 C CA  . LYS   C 1 17 ? 26.092  -39.953 16.295  1.00 29.92  ? 16  LYS   C CA  1 
ATOM   1574 C C   . LYS   C 1 17 ? 24.848  -40.343 15.502  1.00 26.64  ? 16  LYS   C C   1 
ATOM   1575 O O   . LYS   C 1 17 ? 23.868  -40.827 16.071  1.00 28.49  ? 16  LYS   C O   1 
ATOM   1576 C CB  . LYS   C 1 17 ? 26.759  -41.194 16.890  1.00 28.36  ? 16  LYS   C CB  1 
ATOM   1577 C CG  . LYS   C 1 17 ? 27.289  -42.252 15.896  1.00 34.77  ? 16  LYS   C CG  1 
ATOM   1578 C CD  . LYS   C 1 17 ? 28.629  -41.706 15.422  1.00 37.09  ? 16  LYS   C CD  1 
ATOM   1579 C CE  . LYS   C 1 17 ? 29.331  -42.583 14.416  1.00 48.53  ? 16  LYS   C CE  1 
ATOM   1580 N NZ  . LYS   C 1 17 ? 30.472  -41.823 13.899  1.00 45.43  ? 16  LYS   C NZ  1 
ATOM   1581 N N   . GLY   C 1 18 ? 24.982  -40.179 14.179  1.00 30.11  ? 17  GLY   C N   1 
ATOM   1582 C CA  . GLY   C 1 18 ? 23.964  -40.645 13.246  1.00 30.11  ? 17  GLY   C CA  1 
ATOM   1583 C C   . GLY   C 1 18 ? 22.916  -39.580 12.951  1.00 27.77  ? 17  GLY   C C   1 
ATOM   1584 O O   . GLY   C 1 18 ? 21.944  -39.907 12.297  1.00 26.11  ? 17  GLY   C O   1 
ATOM   1585 N N   . TYR   C 1 19 ? 23.104  -38.362 13.489  1.00 27.06  ? 18  TYR   C N   1 
ATOM   1586 C CA  . TYR   C 1 19 ? 22.194  -37.241 13.212  1.00 25.81  ? 18  TYR   C CA  1 
ATOM   1587 C C   . TYR   C 1 19 ? 22.962  -35.953 12.954  1.00 28.73  ? 18  TYR   C C   1 
ATOM   1588 O O   . TYR   C 1 19 ? 24.037  -35.754 13.501  1.00 26.34  ? 18  TYR   C O   1 
ATOM   1589 C CB  . TYR   C 1 19 ? 21.349  -36.935 14.459  1.00 23.08  ? 18  TYR   C CB  1 
ATOM   1590 C CG  . TYR   C 1 19 ? 20.508  -38.124 14.864  1.00 23.80  ? 18  TYR   C CG  1 
ATOM   1591 C CD1 . TYR   C 1 19 ? 21.041  -39.122 15.661  1.00 26.10  ? 18  TYR   C CD1 1 
ATOM   1592 C CD2 . TYR   C 1 19 ? 19.214  -38.271 14.385  1.00 25.82  ? 18  TYR   C CD2 1 
ATOM   1593 C CE1 . TYR   C 1 19 ? 20.296  -40.234 16.023  1.00 28.88  ? 18  TYR   C CE1 1 
ATOM   1594 C CE2 . TYR   C 1 19 ? 18.450  -39.371 14.755  1.00 30.31  ? 18  TYR   C CE2 1 
ATOM   1595 C CZ  . TYR   C 1 19 ? 18.988  -40.338 15.582  1.00 30.99  ? 18  TYR   C CZ  1 
ATOM   1596 O OH  . TYR   C 1 19 ? 18.203  -41.422 15.872  1.00 39.17  ? 18  TYR   C OH  1 
ATOM   1597 N N   . PRO   C 1 20 ? 22.412  -35.019 12.150  1.00 27.08  ? 19  PRO   C N   1 
ATOM   1598 C CA  . PRO   C 1 20 ? 23.029  -33.720 11.930  1.00 25.20  ? 19  PRO   C CA  1 
ATOM   1599 C C   . PRO   C 1 20 ? 22.964  -32.907 13.229  1.00 25.60  ? 19  PRO   C C   1 
ATOM   1600 O O   . PRO   C 1 20 ? 22.217  -33.213 14.160  1.00 24.46  ? 19  PRO   C O   1 
ATOM   1601 C CB  . PRO   C 1 20 ? 22.149  -33.073 10.826  1.00 28.64  ? 19  PRO   C CB  1 
ATOM   1602 C CG  . PRO   C 1 20 ? 20.822  -33.739 10.998  1.00 25.41  ? 19  PRO   C CG  1 
ATOM   1603 C CD  . PRO   C 1 20 ? 21.097  -35.153 11.492  1.00 26.42  ? 19  PRO   C CD  1 
ATOM   1604 N N   . HIS   C 1 21 ? 23.773  -31.855 13.269  1.00 27.59  ? 20  HIS   C N   1 
ATOM   1605 C CA  . HIS   C 1 21 ? 23.731  -30.964 14.425  1.00 24.96  ? 20  HIS   C CA  1 
ATOM   1606 C C   . HIS   C 1 21 ? 22.320  -30.415 14.556  1.00 28.84  ? 20  HIS   C C   1 
ATOM   1607 O O   . HIS   C 1 21 ? 21.787  -29.891 13.584  1.00 27.17  ? 20  HIS   C O   1 
ATOM   1608 C CB  . HIS   C 1 21 ? 24.686  -29.794 14.198  1.00 29.91  ? 20  HIS   C CB  1 
ATOM   1609 C CG  . HIS   C 1 21 ? 26.134  -30.195 14.260  1.00 29.57  ? 20  HIS   C CG  1 
ATOM   1610 N ND1 . HIS   C 1 21 ? 26.864  -30.775 13.243  1.00 32.64  ? 20  HIS   C ND1 1 
ATOM   1611 C CD2 . HIS   C 1 21 ? 26.980  -30.062 15.300  1.00 32.50  ? 20  HIS   C CD2 1 
ATOM   1612 C CE1 . HIS   C 1 21 ? 28.105  -30.997 13.672  1.00 38.13  ? 20  HIS   C CE1 1 
ATOM   1613 N NE2 . HIS   C 1 21 ? 28.209  -30.534 14.907  1.00 34.61  ? 20  HIS   C NE2 1 
ATOM   1614 N N   . TRP   C 1 22 ? 21.715  -30.517 15.754  1.00 24.51  ? 21  TRP   C N   1 
ATOM   1615 C CA  . TRP   C 1 22 ? 20.268  -30.448 15.813  1.00 24.36  ? 21  TRP   C CA  1 
ATOM   1616 C C   . TRP   C 1 22 ? 19.848  -29.287 16.715  1.00 24.80  ? 21  TRP   C C   1 
ATOM   1617 O O   . TRP   C 1 22 ? 20.371  -29.147 17.822  1.00 26.07  ? 21  TRP   C O   1 
ATOM   1618 C CB  . TRP   C 1 22 ? 19.743  -31.785 16.389  1.00 23.85  ? 21  TRP   C CB  1 
ATOM   1619 C CG  . TRP   C 1 22 ? 18.287  -32.005 16.027  1.00 23.08  ? 21  TRP   C CG  1 
ATOM   1620 C CD1 . TRP   C 1 22 ? 17.198  -31.427 16.598  1.00 25.30  ? 21  TRP   C CD1 1 
ATOM   1621 C CD2 . TRP   C 1 22 ? 17.802  -32.890 14.990  1.00 25.61  ? 21  TRP   C CD2 1 
ATOM   1622 N NE1 . TRP   C 1 22 ? 16.056  -31.874 15.967  1.00 25.83  ? 21  TRP   C NE1 1 
ATOM   1623 C CE2 . TRP   C 1 22 ? 16.392  -32.759 14.984  1.00 27.07  ? 21  TRP   C CE2 1 
ATOM   1624 C CE3 . TRP   C 1 22 ? 18.408  -33.769 14.087  1.00 24.80  ? 21  TRP   C CE3 1 
ATOM   1625 C CZ2 . TRP   C 1 22 ? 15.586  -33.499 14.110  1.00 24.94  ? 21  TRP   C CZ2 1 
ATOM   1626 C CZ3 . TRP   C 1 22 ? 17.623  -34.450 13.170  1.00 26.26  ? 21  TRP   C CZ3 1 
ATOM   1627 C CH2 . TRP   C 1 22 ? 16.224  -34.322 13.218  1.00 24.77  ? 21  TRP   C CH2 1 
ATOM   1628 N N   . PRO   C 1 23 ? 18.856  -28.447 16.349  1.00 28.92  ? 22  PRO   C N   1 
ATOM   1629 C CA  . PRO   C 1 23 ? 18.425  -27.374 17.268  1.00 26.33  ? 22  PRO   C CA  1 
ATOM   1630 C C   . PRO   C 1 23 ? 17.873  -27.938 18.578  1.00 25.24  ? 22  PRO   C C   1 
ATOM   1631 O O   . PRO   C 1 23 ? 17.062  -28.836 18.556  1.00 24.91  ? 22  PRO   C O   1 
ATOM   1632 C CB  . PRO   C 1 23 ? 17.328  -26.662 16.411  1.00 26.59  ? 22  PRO   C CB  1 
ATOM   1633 C CG  . PRO   C 1 23 ? 16.806  -27.738 15.469  1.00 26.14  ? 22  PRO   C CG  1 
ATOM   1634 C CD  . PRO   C 1 23 ? 18.097  -28.466 15.075  1.00 25.76  ? 22  PRO   C CD  1 
ATOM   1635 N N   . ALA   C 1 24 ? 18.303  -27.380 19.722  1.00 27.01  ? 23  ALA   C N   1 
ATOM   1636 C CA  . ALA   C 1 24 ? 18.028  -28.019 21.007  1.00 27.74  ? 23  ALA   C CA  1 
ATOM   1637 C C   . ALA   C 1 24 ? 18.113  -26.975 22.115  1.00 29.53  ? 23  ALA   C C   1 
ATOM   1638 O O   . ALA   C 1 24 ? 18.535  -25.834 21.874  1.00 31.22  ? 23  ALA   C O   1 
ATOM   1639 C CB  . ALA   C 1 24 ? 19.040  -29.142 21.247  1.00 28.20  ? 23  ALA   C CB  1 
ATOM   1640 N N   . ARG   C 1 25 ? 17.687  -27.376 23.317  1.00 30.88  ? 24  ARG   C N   1 
ATOM   1641 C CA  . ARG   C 1 25 ? 17.889  -26.544 24.496  1.00 31.61  ? 24  ARG   C CA  1 
ATOM   1642 C C   . ARG   C 1 25 ? 18.346  -27.441 25.652  1.00 34.94  ? 24  ARG   C C   1 
ATOM   1643 O O   . ARG   C 1 25 ? 17.999  -28.618 25.676  1.00 33.55  ? 24  ARG   C O   1 
ATOM   1644 C CB  . ARG   C 1 25 ? 16.618  -25.805 24.907  1.00 30.63  ? 24  ARG   C CB  1 
ATOM   1645 C CG  . ARG   C 1 25 ? 15.403  -26.622 25.306  1.00 37.23  ? 24  ARG   C CG  1 
ATOM   1646 C CD  . ARG   C 1 25 ? 14.354  -25.675 25.894  1.00 41.30  ? 24  ARG   C CD  1 
ATOM   1647 N NE  . ARG   C 1 25 ? 13.157  -26.499 26.126  1.00 41.58  ? 24  ARG   C NE  1 
ATOM   1648 C CZ  . ARG   C 1 25 ? 11.895  -26.180 25.911  1.00 48.09  ? 24  ARG   C CZ  1 
ATOM   1649 N NH1 . ARG   C 1 25 ? 11.565  -24.997 25.413  1.00 42.71  ? 24  ARG   C NH1 1 
ATOM   1650 N NH2 . ARG   C 1 25 ? 10.958  -27.061 26.214  1.00 47.00  ? 24  ARG   C NH2 1 
ATOM   1651 N N   . ILE   C 1 26 ? 19.110  -26.856 26.578  1.00 34.56  ? 25  ILE   C N   1 
ATOM   1652 C CA  . ILE   C 1 26 ? 19.444  -27.444 27.876  1.00 37.13  ? 25  ILE   C CA  1 
ATOM   1653 C C   . ILE   C 1 26 ? 18.207  -27.459 28.767  1.00 42.71  ? 25  ILE   C C   1 
ATOM   1654 O O   . ILE   C 1 26 ? 17.576  -26.424 28.971  1.00 45.28  ? 25  ILE   C O   1 
ATOM   1655 C CB  . ILE   C 1 26 ? 20.580  -26.658 28.565  1.00 37.13  ? 25  ILE   C CB  1 
ATOM   1656 C CG1 . ILE   C 1 26 ? 21.734  -26.307 27.631  1.00 39.64  ? 25  ILE   C CG1 1 
ATOM   1657 C CG2 . ILE   C 1 26 ? 21.056  -27.384 29.834  1.00 37.45  ? 25  ILE   C CG2 1 
ATOM   1658 C CD1 . ILE   C 1 26 ? 22.639  -27.451 27.203  1.00 40.12  ? 25  ILE   C CD1 1 
ATOM   1659 N N   . ASP   C 1 27 ? 17.877  -28.638 29.302  1.00 43.86  ? 26  ASP   C N   1 
ATOM   1660 C CA  . ASP   C 1 27 ? 16.789  -28.785 30.263  1.00 52.47  ? 26  ASP   C CA  1 
ATOM   1661 C C   . ASP   C 1 27 ? 17.306  -28.622 31.691  1.00 59.56  ? 26  ASP   C C   1 
ATOM   1662 O O   . ASP   C 1 27 ? 18.516  -28.662 31.922  1.00 56.04  ? 26  ASP   C O   1 
ATOM   1663 C CB  . ASP   C 1 27 ? 16.178  -30.174 30.211  1.00 51.35  ? 26  ASP   C CB  1 
ATOM   1664 C CG  . ASP   C 1 27 ? 14.915  -30.311 29.381  1.00 58.05  ? 26  ASP   C CG  1 
ATOM   1665 O OD1 . ASP   C 1 27 ? 14.586  -29.329 28.677  1.00 58.88  ? 26  ASP   C OD1 1 
ATOM   1666 O OD2 . ASP   C 1 27 ? 14.260  -31.382 29.492  1.00 58.65  ? 26  ASP   C OD2 1 
ATOM   1667 N N   . ASP   C 1 28 ? 16.366  -28.445 32.635  1.00 68.38  ? 27  ASP   C N   1 
ATOM   1668 C CA  . ASP   C 1 28 ? 16.624  -28.610 34.060  1.00 65.87  ? 27  ASP   C CA  1 
ATOM   1669 C C   . ASP   C 1 28 ? 16.485  -30.093 34.380  1.00 67.46  ? 27  ASP   C C   1 
ATOM   1670 O O   . ASP   C 1 28 ? 15.841  -30.819 33.628  1.00 67.93  ? 27  ASP   C O   1 
ATOM   1671 C CB  . ASP   C 1 28 ? 15.687  -27.776 34.919  1.00 66.00  ? 27  ASP   C CB  1 
ATOM   1672 N N   . ILE   C 1 29 ? 17.104  -30.534 35.483  1.00 68.49  ? 28  ILE   C N   1 
ATOM   1673 C CA  . ILE   C 1 29 ? 17.095  -31.943 35.841  1.00 60.19  ? 28  ILE   C CA  1 
ATOM   1674 C C   . ILE   C 1 29 ? 16.301  -32.110 37.145  1.00 57.29  ? 28  ILE   C C   1 
ATOM   1675 O O   . ILE   C 1 29 ? 16.502  -31.246 38.024  1.00 57.81  ? 28  ILE   C O   1 
ATOM   1676 C CB  . ILE   C 1 29 ? 18.530  -32.496 35.954  1.00 59.69  ? 28  ILE   C CB  1 
ATOM   1677 N N   . LYS   C 1 35 ? 19.925  -39.033 37.923  1.00 50.51  ? 34  LYS   C N   1 
ATOM   1678 C CA  . LYS   C 1 35 ? 20.761  -37.864 37.550  1.00 53.38  ? 34  LYS   C CA  1 
ATOM   1679 C C   . LYS   C 1 35 ? 21.460  -38.190 36.229  1.00 48.56  ? 34  LYS   C C   1 
ATOM   1680 O O   . LYS   C 1 35 ? 21.451  -39.342 35.780  1.00 48.86  ? 34  LYS   C O   1 
ATOM   1681 C CB  . LYS   C 1 35 ? 21.722  -37.555 38.707  1.00 51.72  ? 34  LYS   C CB  1 
ATOM   1682 N N   . PRO   C 1 36 ? 22.053  -37.190 35.539  1.00 51.44  ? 35  PRO   C N   1 
ATOM   1683 C CA  . PRO   C 1 36 ? 22.815  -37.463 34.323  1.00 50.24  ? 35  PRO   C CA  1 
ATOM   1684 C C   . PRO   C 1 36 ? 23.939  -38.455 34.616  1.00 50.17  ? 35  PRO   C C   1 
ATOM   1685 O O   . PRO   C 1 36 ? 24.325  -38.668 35.779  1.00 44.95  ? 35  PRO   C O   1 
ATOM   1686 C CB  . PRO   C 1 36 ? 23.344  -36.063 33.907  1.00 55.08  ? 35  PRO   C CB  1 
ATOM   1687 C CG  . PRO   C 1 36 ? 22.390  -35.082 34.566  1.00 53.64  ? 35  PRO   C CG  1 
ATOM   1688 C CD  . PRO   C 1 36 ? 21.991  -35.753 35.874  1.00 52.46  ? 35  PRO   C CD  1 
ATOM   1689 N N   . PRO   C 1 37 ? 24.471  -39.136 33.580  1.00 47.03  ? 36  PRO   C N   1 
ATOM   1690 C CA  . PRO   C 1 37 ? 25.775  -39.776 33.710  1.00 47.31  ? 36  PRO   C CA  1 
ATOM   1691 C C   . PRO   C 1 37 ? 26.717  -38.613 34.010  1.00 44.94  ? 36  PRO   C C   1 
ATOM   1692 O O   . PRO   C 1 37 ? 26.398  -37.439 33.757  1.00 37.47  ? 36  PRO   C O   1 
ATOM   1693 C CB  . PRO   C 1 37 ? 25.964  -40.386 32.314  1.00 47.23  ? 36  PRO   C CB  1 
ATOM   1694 C CG  . PRO   C 1 37 ? 24.539  -40.650 31.888  1.00 47.02  ? 36  PRO   C CG  1 
ATOM   1695 C CD  . PRO   C 1 37 ? 23.869  -39.348 32.250  1.00 44.07  ? 36  PRO   C CD  1 
ATOM   1696 N N   . PRO   C 1 38 ? 27.884  -38.905 34.624  1.00 41.20  ? 37  PRO   C N   1 
ATOM   1697 C CA  . PRO   C 1 38 ? 28.872  -37.871 34.915  1.00 39.68  ? 37  PRO   C CA  1 
ATOM   1698 C C   . PRO   C 1 38 ? 29.169  -36.966 33.724  1.00 33.38  ? 37  PRO   C C   1 
ATOM   1699 O O   . PRO   C 1 38 ? 29.426  -37.448 32.624  1.00 37.83  ? 37  PRO   C O   1 
ATOM   1700 C CB  . PRO   C 1 38 ? 30.095  -38.719 35.338  1.00 42.48  ? 37  PRO   C CB  1 
ATOM   1701 C CG  . PRO   C 1 38 ? 29.464  -39.937 35.981  1.00 44.03  ? 37  PRO   C CG  1 
ATOM   1702 C CD  . PRO   C 1 38 ? 28.258  -40.242 35.119  1.00 42.42  ? 37  PRO   C CD  1 
ATOM   1703 N N   . ASN   C 1 39 ? 29.064  -35.651 33.973  1.00 37.51  ? 38  ASN   C N   1 
ATOM   1704 C CA  . ASN   C 1 39 ? 29.490  -34.597 33.072  1.00 35.51  ? 38  ASN   C CA  1 
ATOM   1705 C C   . ASN   C 1 39 ? 28.603  -34.566 31.830  1.00 38.26  ? 38  ASN   C C   1 
ATOM   1706 O O   . ASN   C 1 39 ? 29.058  -34.150 30.764  1.00 44.19  ? 38  ASN   C O   1 
ATOM   1707 C CB  . ASN   C 1 39 ? 30.916  -34.776 32.577  1.00 38.19  ? 38  ASN   C CB  1 
ATOM   1708 C CG  . ASN   C 1 39 ? 31.530  -33.516 32.001  1.00 50.17  ? 38  ASN   C CG  1 
ATOM   1709 O OD1 . ASN   C 1 39 ? 31.062  -32.401 32.271  1.00 57.21  ? 38  ASN   C OD1 1 
ATOM   1710 N ND2 . ASN   C 1 39 ? 32.577  -33.667 31.199  1.00 48.77  ? 38  ASN   C ND2 1 
ATOM   1711 N N   . LYS   C 1 40 ? 27.358  -35.030 31.964  1.00 33.76  ? 39  LYS   C N   1 
ATOM   1712 C CA  . LYS   C 1 40 ? 26.448  -34.910 30.832  1.00 31.37  ? 39  LYS   C CA  1 
ATOM   1713 C C   . LYS   C 1 40 ? 25.340  -33.918 31.172  1.00 32.70  ? 39  LYS   C C   1 
ATOM   1714 O O   . LYS   C 1 40 ? 24.948  -33.747 32.312  1.00 34.02  ? 39  LYS   C O   1 
ATOM   1715 C CB  . LYS   C 1 40 ? 25.766  -36.249 30.515  1.00 31.01  ? 39  LYS   C CB  1 
ATOM   1716 C CG  . LYS   C 1 40 ? 26.640  -37.418 30.192  1.00 36.71  ? 39  LYS   C CG  1 
ATOM   1717 C CD  . LYS   C 1 40 ? 27.446  -37.260 28.917  1.00 40.68  ? 39  LYS   C CD  1 
ATOM   1718 C CE  . LYS   C 1 40 ? 28.105  -38.555 28.525  1.00 41.85  ? 39  LYS   C CE  1 
ATOM   1719 N NZ  . LYS   C 1 40 ? 29.033  -38.274 27.423  1.00 50.10  ? 39  LYS   C NZ  1 
ATOM   1720 N N   . TYR   C 1 41 ? 24.799  -33.244 30.145  1.00 29.27  ? 40  TYR   C N   1 
ATOM   1721 C CA  . TYR   C 1 41 ? 23.685  -32.314 30.298  1.00 31.78  ? 40  TYR   C CA  1 
ATOM   1722 C C   . TYR   C 1 41 ? 22.408  -32.953 29.755  1.00 31.59  ? 40  TYR   C C   1 
ATOM   1723 O O   . TYR   C 1 41 ? 22.483  -33.692 28.769  1.00 30.13  ? 40  TYR   C O   1 
ATOM   1724 C CB  . TYR   C 1 41 ? 23.911  -31.123 29.358  1.00 29.78  ? 40  TYR   C CB  1 
ATOM   1725 C CG  . TYR   C 1 41 ? 25.022  -30.184 29.791  1.00 30.12  ? 40  TYR   C CG  1 
ATOM   1726 C CD1 . TYR   C 1 41 ? 26.328  -30.354 29.335  1.00 31.17  ? 40  TYR   C CD1 1 
ATOM   1727 C CD2 . TYR   C 1 41 ? 24.753  -29.146 30.679  1.00 33.97  ? 40  TYR   C CD2 1 
ATOM   1728 C CE1 . TYR   C 1 41 ? 27.356  -29.534 29.765  1.00 42.95  ? 40  TYR   C CE1 1 
ATOM   1729 C CE2 . TYR   C 1 41 ? 25.773  -28.300 31.079  1.00 33.67  ? 40  TYR   C CE2 1 
ATOM   1730 C CZ  . TYR   C 1 41 ? 27.062  -28.496 30.633  1.00 39.47  ? 40  TYR   C CZ  1 
ATOM   1731 O OH  . TYR   C 1 41 ? 28.007  -27.649 31.110  1.00 47.47  ? 40  TYR   C OH  1 
ATOM   1732 N N   . PRO   C 1 42 ? 21.222  -32.655 30.348  1.00 34.15  ? 41  PRO   C N   1 
ATOM   1733 C CA  . PRO   C 1 42 ? 19.928  -33.099 29.811  1.00 32.98  ? 41  PRO   C CA  1 
ATOM   1734 C C   . PRO   C 1 42 ? 19.605  -32.200 28.618  1.00 35.63  ? 41  PRO   C C   1 
ATOM   1735 O O   . PRO   C 1 42 ? 19.647  -30.978 28.749  1.00 36.38  ? 41  PRO   C O   1 
ATOM   1736 C CB  . PRO   C 1 42 ? 18.916  -32.888 30.957  1.00 35.80  ? 41  PRO   C CB  1 
ATOM   1737 C CG  . PRO   C 1 42 ? 19.654  -32.022 31.952  1.00 36.87  ? 41  PRO   C CG  1 
ATOM   1738 C CD  . PRO   C 1 42 ? 21.074  -31.735 31.494  1.00 37.97  ? 41  PRO   C CD  1 
ATOM   1739 N N   . ILE   C 1 43 ? 19.309  -32.829 27.469  1.00 30.22  ? 42  ILE   C N   1 
ATOM   1740 C CA  . ILE   C 1 43 ? 19.030  -32.049 26.257  1.00 30.24  ? 42  ILE   C CA  1 
ATOM   1741 C C   . ILE   C 1 43 ? 17.586  -32.288 25.829  1.00 29.56  ? 42  ILE   C C   1 
ATOM   1742 O O   . ILE   C 1 43 ? 17.063  -33.401 25.911  1.00 31.80  ? 42  ILE   C O   1 
ATOM   1743 C CB  . ILE   C 1 43 ? 20.035  -32.416 25.140  1.00 27.22  ? 42  ILE   C CB  1 
ATOM   1744 C CG1 . ILE   C 1 43 ? 21.509  -32.257 25.582  1.00 30.98  ? 42  ILE   C CG1 1 
ATOM   1745 C CG2 . ILE   C 1 43 ? 19.716  -31.656 23.837  1.00 29.44  ? 42  ILE   C CG2 1 
ATOM   1746 C CD1 . ILE   C 1 43 ? 21.943  -30.835 25.918  1.00 29.38  ? 42  ILE   C CD1 1 
ATOM   1747 N N   . PHE   C 1 44 ? 16.919  -31.229 25.320  1.00 29.81  ? 43  PHE   C N   1 
ATOM   1748 C CA  . PHE   C 1 44 ? 15.638  -31.404 24.658  1.00 29.04  ? 43  PHE   C CA  1 
ATOM   1749 C C   . PHE   C 1 44 ? 15.802  -30.912 23.221  1.00 26.69  ? 43  PHE   C C   1 
ATOM   1750 O O   . PHE   C 1 44 ? 16.338  -29.812 23.005  1.00 30.69  ? 43  PHE   C O   1 
ATOM   1751 C CB  . PHE   C 1 44 ? 14.641  -30.448 25.337  1.00 33.38  ? 43  PHE   C CB  1 
ATOM   1752 C CG  . PHE   C 1 44 ? 13.252  -30.360 24.705  1.00 33.31  ? 43  PHE   C CG  1 
ATOM   1753 C CD1 . PHE   C 1 44 ? 12.277  -31.321 24.967  1.00 36.77  ? 43  PHE   C CD1 1 
ATOM   1754 C CD2 . PHE   C 1 44 ? 12.935  -29.304 23.848  1.00 38.33  ? 43  PHE   C CD2 1 
ATOM   1755 C CE1 . PHE   C 1 44 ? 11.012  -31.233 24.370  1.00 36.62  ? 43  PHE   C CE1 1 
ATOM   1756 C CE2 . PHE   C 1 44 ? 11.680  -29.215 23.255  1.00 36.04  ? 43  PHE   C CE2 1 
ATOM   1757 C CZ  . PHE   C 1 44 ? 10.720  -30.176 23.523  1.00 39.31  ? 43  PHE   C CZ  1 
ATOM   1758 N N   . PHE   C 1 45 ? 15.393  -31.774 22.294  1.00 27.76  ? 44  PHE   C N   1 
ATOM   1759 C CA  . PHE   C 1 45 ? 15.576  -31.521 20.867  1.00 29.29  ? 44  PHE   C CA  1 
ATOM   1760 C C   . PHE   C 1 45 ? 14.315  -30.857 20.347  1.00 26.95  ? 44  PHE   C C   1 
ATOM   1761 O O   . PHE   C 1 45 ? 13.213  -31.390 20.512  1.00 30.25  ? 44  PHE   C O   1 
ATOM   1762 C CB  . PHE   C 1 45 ? 15.897  -32.813 20.122  1.00 26.59  ? 44  PHE   C CB  1 
ATOM   1763 C CG  . PHE   C 1 45 ? 17.262  -33.372 20.480  1.00 25.48  ? 44  PHE   C CG  1 
ATOM   1764 C CD1 . PHE   C 1 45 ? 18.409  -32.986 19.780  1.00 25.62  ? 44  PHE   C CD1 1 
ATOM   1765 C CD2 . PHE   C 1 45 ? 17.386  -34.336 21.497  1.00 29.48  ? 44  PHE   C CD2 1 
ATOM   1766 C CE1 . PHE   C 1 45 ? 19.665  -33.524 20.087  1.00 29.20  ? 44  PHE   C CE1 1 
ATOM   1767 C CE2 . PHE   C 1 45 ? 18.641  -34.868 21.798  1.00 30.57  ? 44  PHE   C CE2 1 
ATOM   1768 C CZ  . PHE   C 1 45 ? 19.775  -34.457 21.112  1.00 27.75  ? 44  PHE   C CZ  1 
ATOM   1769 N N   . PHE   C 1 46 ? 14.482  -29.672 19.717  1.00 27.85  ? 45  PHE   C N   1 
ATOM   1770 C CA  . PHE   C 1 46 ? 13.301  -29.107 19.070  1.00 26.23  ? 45  PHE   C CA  1 
ATOM   1771 C C   . PHE   C 1 46 ? 12.847  -29.949 17.877  1.00 28.52  ? 45  PHE   C C   1 
ATOM   1772 O O   . PHE   C 1 46 ? 13.624  -30.709 17.268  1.00 26.95  ? 45  PHE   C O   1 
ATOM   1773 C CB  . PHE   C 1 46 ? 13.619  -27.676 18.614  1.00 25.98  ? 45  PHE   C CB  1 
ATOM   1774 C CG  . PHE   C 1 46 ? 13.790  -26.690 19.748  1.00 26.14  ? 45  PHE   C CG  1 
ATOM   1775 C CD1 . PHE   C 1 46 ? 12.701  -26.262 20.506  1.00 29.84  ? 45  PHE   C CD1 1 
ATOM   1776 C CD2 . PHE   C 1 46 ? 15.068  -26.216 20.035  1.00 26.14  ? 45  PHE   C CD2 1 
ATOM   1777 C CE1 . PHE   C 1 46 ? 12.921  -25.362 21.546  1.00 31.82  ? 45  PHE   C CE1 1 
ATOM   1778 C CE2 . PHE   C 1 46 ? 15.279  -25.331 21.093  1.00 31.05  ? 45  PHE   C CE2 1 
ATOM   1779 C CZ  . PHE   C 1 46 ? 14.193  -24.883 21.811  1.00 31.17  ? 45  PHE   C CZ  1 
ATOM   1780 N N   . GLY   C 1 47 ? 11.568  -29.786 17.513  1.00 26.68  ? 46  GLY   C N   1 
ATOM   1781 C CA  . GLY   C 1 47 ? 11.036  -30.497 16.360  1.00 28.33  ? 46  GLY   C CA  1 
ATOM   1782 C C   . GLY   C 1 47 ? 10.598  -31.912 16.746  1.00 31.93  ? 46  GLY   C C   1 
ATOM   1783 O O   . GLY   C 1 47 ? 9.419   -32.235 16.676  1.00 36.94  ? 46  GLY   C O   1 
ATOM   1784 N N   . THR   C 1 48 ? 11.554  -32.767 17.154  1.00 28.73  ? 47  THR   C N   1 
ATOM   1785 C CA  . THR   C 1 48 ? 11.195  -34.121 17.587  1.00 31.39  ? 47  THR   C CA  1 
ATOM   1786 C C   . THR   C 1 48 ? 10.631  -34.122 19.011  1.00 33.01  ? 47  THR   C C   1 
ATOM   1787 O O   . THR   C 1 48 ? 9.851   -35.012 19.352  1.00 36.43  ? 47  THR   C O   1 
ATOM   1788 C CB  . THR   C 1 48 ? 12.415  -35.037 17.538  1.00 28.82  ? 47  THR   C CB  1 
ATOM   1789 O OG1 . THR   C 1 48 ? 13.265  -34.476 18.545  1.00 32.42  ? 47  THR   C OG1 1 
ATOM   1790 C CG2 . THR   C 1 48 ? 13.030  -35.147 16.164  1.00 29.43  ? 47  THR   C CG2 1 
ATOM   1791 N N   . HIS   C 1 49 ? 11.020  -33.138 19.825  1.00 31.95  ? 48  HIS   C N   1 
ATOM   1792 C CA  . HIS   C 1 49 ? 10.665  -33.028 21.238  1.00 36.40  ? 48  HIS   C CA  1 
ATOM   1793 C C   . HIS   C 1 49 ? 11.174  -34.219 22.059  1.00 34.34  ? 48  HIS   C C   1 
ATOM   1794 O O   . HIS   C 1 49 ? 10.591  -34.545 23.095  1.00 39.43  ? 48  HIS   C O   1 
ATOM   1795 C CB  . HIS   C 1 49 ? 9.162   -32.755 21.416  1.00 34.35  ? 48  HIS   C CB  1 
ATOM   1796 C CG  . HIS   C 1 49 ? 8.640   -31.653 20.541  1.00 37.56  ? 48  HIS   C CG  1 
ATOM   1797 N ND1 . HIS   C 1 49 ? 7.478   -31.818 19.815  1.00 46.18  ? 48  HIS   C ND1 1 
ATOM   1798 C CD2 . HIS   C 1 49 ? 9.090   -30.431 20.249  1.00 41.62  ? 48  HIS   C CD2 1 
ATOM   1799 C CE1 . HIS   C 1 49 ? 7.238   -30.724 19.102  1.00 47.81  ? 48  HIS   C CE1 1 
ATOM   1800 N NE2 . HIS   C 1 49 ? 8.206   -29.861 19.342  1.00 39.38  ? 48  HIS   C NE2 1 
ATOM   1801 N N   . GLU   C 1 50 ? 12.252  -34.865 21.608  1.00 30.85  ? 49  GLU   C N   1 
ATOM   1802 C CA  . GLU   C 1 50 ? 12.822  -35.968 22.366  1.00 32.58  ? 49  GLU   C CA  1 
ATOM   1803 C C   . GLU   C 1 50 ? 13.924  -35.444 23.292  1.00 33.03  ? 49  GLU   C C   1 
ATOM   1804 O O   . GLU   C 1 50 ? 14.270  -34.259 23.280  1.00 33.10  ? 49  GLU   C O   1 
ATOM   1805 C CB  . GLU   C 1 50 ? 13.314  -37.040 21.404  1.00 34.78  ? 49  GLU   C CB  1 
ATOM   1806 C CG  . GLU   C 1 50 ? 12.189  -37.648 20.567  1.00 42.72  ? 49  GLU   C CG  1 
ATOM   1807 C CD  . GLU   C 1 50 ? 12.758  -38.530 19.477  1.00 51.64  ? 49  GLU   C CD  1 
ATOM   1808 O OE1 . GLU   C 1 50 ? 13.985  -38.796 19.489  1.00 58.27  ? 49  GLU   C OE1 1 
ATOM   1809 O OE2 . GLU   C 1 50 ? 11.967  -38.935 18.600  1.00 53.38  ? 49  GLU   C OE2 1 
ATOM   1810 N N   . THR   C 1 51 ? 14.427  -36.323 24.177  1.00 37.97  ? 50  THR   C N   1 
ATOM   1811 C CA  . THR   C 1 51 ? 15.438  -35.952 25.166  1.00 35.79  ? 50  THR   C CA  1 
ATOM   1812 C C   . THR   C 1 51 ? 16.570  -36.975 25.104  1.00 31.69  ? 50  THR   C C   1 
ATOM   1813 O O   . THR   C 1 51 ? 16.374  -38.110 24.662  1.00 37.08  ? 50  THR   C O   1 
ATOM   1814 C CB  . THR   C 1 51 ? 14.892  -35.871 26.597  1.00 35.83  ? 50  THR   C CB  1 
ATOM   1815 O OG1 . THR   C 1 51 ? 14.391  -37.172 26.902  1.00 37.88  ? 50  THR   C OG1 1 
ATOM   1816 C CG2 . THR   C 1 51 ? 13.924  -34.718 26.817  1.00 36.61  ? 50  THR   C CG2 1 
ATOM   1817 N N   . ALA   C 1 52 ? 17.767  -36.506 25.481  1.00 31.71  ? 51  ALA   C N   1 
ATOM   1818 C CA  . ALA   C 1 52 ? 18.967  -37.319 25.622  1.00 31.52  ? 51  ALA   C CA  1 
ATOM   1819 C C   . ALA   C 1 52 ? 19.942  -36.634 26.583  1.00 35.64  ? 51  ALA   C C   1 
ATOM   1820 O O   . ALA   C 1 52 ? 19.743  -35.496 26.995  1.00 36.92  ? 51  ALA   C O   1 
ATOM   1821 C CB  . ALA   C 1 52 ? 19.612  -37.559 24.282  1.00 37.17  ? 51  ALA   C CB  1 
ATOM   1822 N N   . PHE   C 1 53 ? 21.010  -37.350 26.962  1.00 33.60  ? 52  PHE   C N   1 
ATOM   1823 C CA  . PHE   C 1 53 ? 22.095  -36.775 27.757  1.00 34.89  ? 52  PHE   C CA  1 
ATOM   1824 C C   . PHE   C 1 53 ? 23.318  -36.622 26.869  1.00 33.53  ? 52  PHE   C C   1 
ATOM   1825 O O   . PHE   C 1 53 ? 23.727  -37.581 26.221  1.00 35.56  ? 52  PHE   C O   1 
ATOM   1826 C CB  . PHE   C 1 53 ? 22.426  -37.799 28.856  1.00 35.45  ? 52  PHE   C CB  1 
ATOM   1827 C CG  . PHE   C 1 53 ? 21.434  -37.727 30.005  1.00 36.70  ? 52  PHE   C CG  1 
ATOM   1828 C CD1 . PHE   C 1 53 ? 21.239  -36.549 30.718  1.00 36.79  ? 52  PHE   C CD1 1 
ATOM   1829 C CD2 . PHE   C 1 53 ? 20.647  -38.830 30.329  1.00 47.24  ? 52  PHE   C CD2 1 
ATOM   1830 C CE1 . PHE   C 1 53 ? 20.327  -36.484 31.764  1.00 40.10  ? 52  PHE   C CE1 1 
ATOM   1831 C CE2 . PHE   C 1 53 ? 19.730  -38.753 31.375  1.00 46.01  ? 52  PHE   C CE2 1 
ATOM   1832 C CZ  . PHE   C 1 53 ? 19.571  -37.582 32.086  1.00 42.39  ? 52  PHE   C CZ  1 
ATOM   1833 N N   . LEU   C 1 54 ? 23.935  -35.431 26.849  1.00 31.29  ? 53  LEU   C N   1 
ATOM   1834 C CA  . LEU   C 1 54 ? 25.097  -35.231 25.989  1.00 28.37  ? 53  LEU   C CA  1 
ATOM   1835 C C   . LEU   C 1 54 ? 26.189  -34.478 26.742  1.00 30.27  ? 53  LEU   C C   1 
ATOM   1836 O O   . LEU   C 1 54 ? 25.867  -33.742 27.664  1.00 31.73  ? 53  LEU   C O   1 
ATOM   1837 C CB  . LEU   C 1 54 ? 24.745  -34.495 24.691  1.00 29.93  ? 53  LEU   C CB  1 
ATOM   1838 C CG  . LEU   C 1 54 ? 23.878  -35.283 23.706  1.00 34.76  ? 53  LEU   C CG  1 
ATOM   1839 C CD1 . LEU   C 1 54 ? 23.594  -34.324 22.590  1.00 33.90  ? 53  LEU   C CD1 1 
ATOM   1840 C CD2 . LEU   C 1 54 ? 24.650  -36.501 23.144  1.00 39.44  ? 53  LEU   C CD2 1 
ATOM   1841 N N   . GLY   C 1 55 ? 27.449  -34.679 26.340  1.00 32.46  ? 54  GLY   C N   1 
ATOM   1842 C CA  . GLY   C 1 55 ? 28.564  -33.958 26.941  1.00 37.21  ? 54  GLY   C CA  1 
ATOM   1843 C C   . GLY   C 1 55 ? 28.842  -32.625 26.243  1.00 40.80  ? 54  GLY   C C   1 
ATOM   1844 O O   . GLY   C 1 55 ? 28.377  -32.360 25.126  1.00 34.08  ? 54  GLY   C O   1 
ATOM   1845 N N   . PRO   C 1 56 ? 29.594  -31.706 26.890  1.00 38.13  ? 55  PRO   C N   1 
ATOM   1846 C CA  . PRO   C 1 56 ? 29.766  -30.349 26.368  1.00 39.20  ? 55  PRO   C CA  1 
ATOM   1847 C C   . PRO   C 1 56 ? 30.404  -30.230 24.987  1.00 38.09  ? 55  PRO   C C   1 
ATOM   1848 O O   . PRO   C 1 56 ? 30.179  -29.234 24.298  1.00 47.88  ? 55  PRO   C O   1 
ATOM   1849 C CB  . PRO   C 1 56 ? 30.622  -29.637 27.479  1.00 41.04  ? 55  PRO   C CB  1 
ATOM   1850 C CG  . PRO   C 1 56 ? 31.294  -30.781 28.201  1.00 38.51  ? 55  PRO   C CG  1 
ATOM   1851 C CD  . PRO   C 1 56 ? 30.227  -31.878 28.212  1.00 40.78  ? 55  PRO   C CD  1 
ATOM   1852 N N   . LYS   C 1 57 ? 31.187  -31.244 24.598  1.00 38.16  ? 56  LYS   C N   1 
ATOM   1853 C CA  . LYS   C 1 57 ? 31.868  -31.249 23.315  1.00 39.59  ? 56  LYS   C CA  1 
ATOM   1854 C C   . LYS   C 1 57 ? 30.851  -31.434 22.191  1.00 41.28  ? 56  LYS   C C   1 
ATOM   1855 O O   . LYS   C 1 57 ? 31.165  -31.170 21.025  1.00 38.69  ? 56  LYS   C O   1 
ATOM   1856 C CB  . LYS   C 1 57 ? 32.775  -32.476 23.187  1.00 42.69  ? 56  LYS   C CB  1 
ATOM   1857 N N   . ASP   C 1 58 ? 29.650  -31.899 22.567  1.00 39.88  ? 57  ASP   C N   1 
ATOM   1858 C CA  . ASP   C 1 58 ? 28.608  -32.197 21.590  1.00 39.22  ? 57  ASP   C CA  1 
ATOM   1859 C C   . ASP   C 1 58 ? 27.641  -31.032 21.444  1.00 36.87  ? 57  ASP   C C   1 
ATOM   1860 O O   . ASP   C 1 58 ? 26.663  -31.152 20.710  1.00 34.72  ? 57  ASP   C O   1 
ATOM   1861 C CB  . ASP   C 1 58 ? 27.838  -33.453 21.949  1.00 36.17  ? 57  ASP   C CB  1 
ATOM   1862 C CG  . ASP   C 1 58 ? 28.675  -34.720 21.971  1.00 41.68  ? 57  ASP   C CG  1 
ATOM   1863 O OD1 . ASP   C 1 58 ? 29.657  -34.763 21.230  1.00 43.31  ? 57  ASP   C OD1 1 
ATOM   1864 O OD2 . ASP   C 1 58 ? 28.358  -35.620 22.761  1.00 43.83  ? 57  ASP   C OD2 1 
ATOM   1865 N N   . LEU   C 1 59 ? 27.907  -29.921 22.137  1.00 32.47  ? 58  LEU   C N   1 
ATOM   1866 C CA  . LEU   C 1 59 ? 26.987  -28.800 22.227  1.00 34.32  ? 58  LEU   C CA  1 
ATOM   1867 C C   . LEU   C 1 59 ? 27.630  -27.530 21.692  1.00 36.97  ? 58  LEU   C C   1 
ATOM   1868 O O   . LEU   C 1 59 ? 28.813  -27.298 21.966  1.00 39.94  ? 58  LEU   C O   1 
ATOM   1869 C CB  . LEU   C 1 59 ? 26.588  -28.613 23.688  1.00 31.64  ? 58  LEU   C CB  1 
ATOM   1870 C CG  . LEU   C 1 59 ? 26.075  -29.887 24.357  1.00 29.64  ? 58  LEU   C CG  1 
ATOM   1871 C CD1 . LEU   C 1 59 ? 25.759  -29.682 25.813  1.00 31.66  ? 58  LEU   C CD1 1 
ATOM   1872 C CD2 . LEU   C 1 59 ? 24.809  -30.340 23.620  1.00 27.23  ? 58  LEU   C CD2 1 
ATOM   1873 N N   . PHE   C 1 60 ? 26.825  -26.728 20.981  1.00 38.06  ? 59  PHE   C N   1 
ATOM   1874 C CA  . PHE   C 1 60 ? 27.293  -25.526 20.293  1.00 36.30  ? 59  PHE   C CA  1 
ATOM   1875 C C   . PHE   C 1 60 ? 26.295  -24.405 20.583  1.00 39.37  ? 59  PHE   C C   1 
ATOM   1876 O O   . PHE   C 1 60 ? 25.110  -24.516 20.291  1.00 36.35  ? 59  PHE   C O   1 
ATOM   1877 C CB  . PHE   C 1 60 ? 27.490  -25.792 18.788  1.00 37.45  ? 59  PHE   C CB  1 
ATOM   1878 C CG  . PHE   C 1 60 ? 28.463  -26.930 18.504  1.00 34.14  ? 59  PHE   C CG  1 
ATOM   1879 C CD1 . PHE   C 1 60 ? 28.056  -28.261 18.540  1.00 32.97  ? 59  PHE   C CD1 1 
ATOM   1880 C CD2 . PHE   C 1 60 ? 29.813  -26.677 18.245  1.00 40.49  ? 59  PHE   C CD2 1 
ATOM   1881 C CE1 . PHE   C 1 60 ? 28.956  -29.299 18.337  1.00 32.97  ? 59  PHE   C CE1 1 
ATOM   1882 C CE2 . PHE   C 1 60 ? 30.714  -27.721 18.028  1.00 38.39  ? 59  PHE   C CE2 1 
ATOM   1883 C CZ  . PHE   C 1 60 ? 30.293  -29.033 18.063  1.00 39.14  ? 59  PHE   C CZ  1 
ATOM   1884 N N   . PRO   C 1 61 ? 26.703  -23.271 21.201  1.00 37.90  ? 60  PRO   C N   1 
ATOM   1885 C CA  . PRO   C 1 61 ? 25.741  -22.207 21.490  1.00 35.55  ? 60  PRO   C CA  1 
ATOM   1886 C C   . PRO   C 1 61 ? 25.064  -21.735 20.208  1.00 31.75  ? 60  PRO   C C   1 
ATOM   1887 O O   . PRO   C 1 61 ? 25.684  -21.672 19.148  1.00 36.77  ? 60  PRO   C O   1 
ATOM   1888 C CB  . PRO   C 1 61 ? 26.530  -21.077 22.227  1.00 39.55  ? 60  PRO   C CB  1 
ATOM   1889 C CG  . PRO   C 1 61 ? 27.944  -21.621 22.327  1.00 41.63  ? 60  PRO   C CG  1 
ATOM   1890 C CD  . PRO   C 1 61 ? 28.082  -22.970 21.630  1.00 41.66  ? 60  PRO   C CD  1 
ATOM   1891 N N   . TYR   C 1 62 ? 23.744  -21.498 20.327  1.00 36.36  ? 61  TYR   C N   1 
ATOM   1892 C CA  . TYR   C 1 62 ? 22.855  -21.278 19.194  1.00 35.15  ? 61  TYR   C CA  1 
ATOM   1893 C C   . TYR   C 1 62 ? 23.258  -20.018 18.430  1.00 43.21  ? 61  TYR   C C   1 
ATOM   1894 O O   . TYR   C 1 62 ? 23.472  -20.073 17.217  1.00 44.15  ? 61  TYR   C O   1 
ATOM   1895 C CB  . TYR   C 1 62 ? 21.398  -21.127 19.630  1.00 35.93  ? 61  TYR   C CB  1 
ATOM   1896 C CG  . TYR   C 1 62 ? 20.479  -20.741 18.476  1.00 39.36  ? 61  TYR   C CG  1 
ATOM   1897 C CD1 . TYR   C 1 62 ? 20.257  -21.623 17.419  1.00 38.74  ? 61  TYR   C CD1 1 
ATOM   1898 C CD2 . TYR   C 1 62 ? 19.802  -19.528 18.471  1.00 40.24  ? 61  TYR   C CD2 1 
ATOM   1899 C CE1 . TYR   C 1 62 ? 19.410  -21.301 16.367  1.00 41.58  ? 61  TYR   C CE1 1 
ATOM   1900 C CE2 . TYR   C 1 62 ? 18.945  -19.197 17.429  1.00 46.14  ? 61  TYR   C CE2 1 
ATOM   1901 C CZ  . TYR   C 1 62 ? 18.746  -20.084 16.378  1.00 42.40  ? 61  TYR   C CZ  1 
ATOM   1902 O OH  . TYR   C 1 62 ? 17.915  -19.718 15.350  1.00 43.82  ? 61  TYR   C OH  1 
ATOM   1903 N N   . ASP   C 1 63 ? 23.366  -18.889 19.146  1.00 43.90  ? 62  ASP   C N   1 
ATOM   1904 C CA  . ASP   C 1 63 ? 23.630  -17.643 18.437  1.00 46.97  ? 62  ASP   C CA  1 
ATOM   1905 C C   . ASP   C 1 63 ? 24.952  -17.717 17.684  1.00 46.45  ? 62  ASP   C C   1 
ATOM   1906 O O   . ASP   C 1 63 ? 25.035  -17.240 16.548  1.00 47.50  ? 62  ASP   C O   1 
ATOM   1907 C CB  . ASP   C 1 63 ? 23.304  -16.411 19.267  1.00 46.85  ? 62  ASP   C CB  1 
ATOM   1908 C CG  . ASP   C 1 63 ? 21.805  -16.133 19.327  1.00 61.07  ? 62  ASP   C CG  1 
ATOM   1909 O OD1 . ASP   C 1 63 ? 21.307  -15.781 20.424  1.00 57.97  ? 62  ASP   C OD1 1 
ATOM   1910 O OD2 . ASP   C 1 63 ? 21.133  -16.309 18.274  1.00 60.21  ? 62  ASP   C OD2 1 
ATOM   1911 N N   . LYS   C 1 64 ? 25.948  -18.365 18.291  1.00 42.47  ? 63  LYS   C N   1 
ATOM   1912 C CA  . LYS   C 1 64 ? 27.297  -18.373 17.756  1.00 45.13  ? 63  LYS   C CA  1 
ATOM   1913 C C   . LYS   C 1 64 ? 27.411  -19.317 16.562  1.00 44.16  ? 63  LYS   C C   1 
ATOM   1914 O O   . LYS   C 1 64 ? 28.302  -19.152 15.733  1.00 37.87  ? 63  LYS   C O   1 
ATOM   1915 C CB  . LYS   C 1 64 ? 28.333  -18.714 18.838  1.00 49.53  ? 63  LYS   C CB  1 
ATOM   1916 N N   . SER   C 1 65 ? 26.508  -20.314 16.453  1.00 36.84  ? 64  SER   C N   1 
ATOM   1917 C CA  . SER   C 1 65 ? 26.752  -21.344 15.455  1.00 35.41  ? 64  SER   C CA  1 
ATOM   1918 C C   . SER   C 1 65 ? 25.623  -21.496 14.436  1.00 31.56  ? 64  SER   C C   1 
ATOM   1919 O O   . SER   C 1 65 ? 25.788  -22.293 13.526  1.00 32.00  ? 64  SER   C O   1 
ATOM   1920 C CB  . SER   C 1 65 ? 27.111  -22.683 16.059  1.00 40.27  ? 64  SER   C CB  1 
ATOM   1921 O OG  . SER   C 1 65 ? 25.981  -23.218 16.720  1.00 40.64  ? 64  SER   C OG  1 
ATOM   1922 N N   . LYS   C 1 66 ? 24.540  -20.729 14.557  1.00 33.80  ? 65  LYS   C N   1 
ATOM   1923 C CA  . LYS   C 1 66 ? 23.412  -20.884 13.645  1.00 34.64  ? 65  LYS   C CA  1 
ATOM   1924 C C   . LYS   C 1 66 ? 23.783  -20.590 12.190  1.00 39.90  ? 65  LYS   C C   1 
ATOM   1925 O O   . LYS   C 1 66 ? 23.239  -21.214 11.279  1.00 36.42  ? 65  LYS   C O   1 
ATOM   1926 C CB  . LYS   C 1 66 ? 22.198  -20.075 14.093  1.00 38.78  ? 65  LYS   C CB  1 
ATOM   1927 C CG  . LYS   C 1 66 ? 22.422  -18.579 14.145  1.00 32.54  ? 65  LYS   C CG  1 
ATOM   1928 C CD  . LYS   C 1 66 ? 21.124  -17.904 14.571  1.00 39.41  ? 65  LYS   C CD  1 
ATOM   1929 C CE  . LYS   C 1 66 ? 21.302  -16.451 14.868  1.00 43.55  ? 65  LYS   C CE  1 
ATOM   1930 N NZ  . LYS   C 1 66 ? 19.979  -15.882 15.087  1.00 44.43  ? 65  LYS   C NZ  1 
ATOM   1931 N N   . ASP   C 1 67 ? 24.716  -19.658 11.951  1.00 37.84  ? 66  ASP   C N   1 
ATOM   1932 C CA  . ASP   C 1 67 ? 25.110  -19.381 10.572  1.00 40.11  ? 66  ASP   C CA  1 
ATOM   1933 C C   . ASP   C 1 67 ? 25.571  -20.665 9.869   1.00 38.31  ? 66  ASP   C C   1 
ATOM   1934 O O   . ASP   C 1 67 ? 25.305  -20.854 8.693   1.00 36.01  ? 66  ASP   C O   1 
ATOM   1935 C CB  . ASP   C 1 67 ? 26.003  -18.146 10.445  1.00 41.94  ? 66  ASP   C CB  1 
ATOM   1936 C CG  . ASP   C 1 67 ? 27.408  -18.221 11.031  1.00 58.33  ? 66  ASP   C CG  1 
ATOM   1937 O OD1 . ASP   C 1 67 ? 27.754  -19.270 11.631  1.00 63.79  ? 66  ASP   C OD1 1 
ATOM   1938 O OD2 . ASP   C 1 67 ? 28.151  -17.212 10.893  1.00 56.82  ? 66  ASP   C OD2 1 
ATOM   1939 N N   . LYS   C 1 68 ? 26.200  -21.594 10.610  1.00 35.98  ? 67  LYS   C N   1 
ATOM   1940 C CA  . LYS   C 1 68 ? 26.680  -22.855 10.063  1.00 36.06  ? 67  LYS   C CA  1 
ATOM   1941 C C   . LYS   C 1 68 ? 25.647  -23.996 10.154  1.00 33.88  ? 67  LYS   C C   1 
ATOM   1942 O O   . LYS   C 1 68 ? 25.482  -24.769 9.210   1.00 34.84  ? 67  LYS   C O   1 
ATOM   1943 C CB  . LYS   C 1 68 ? 27.910  -23.187 10.913  1.00 36.21  ? 67  LYS   C CB  1 
ATOM   1944 C CG  . LYS   C 1 68 ? 28.764  -24.359 10.500  1.00 39.43  ? 67  LYS   C CG  1 
ATOM   1945 C CD  . LYS   C 1 68 ? 29.977  -24.291 11.441  1.00 47.56  ? 67  LYS   C CD  1 
ATOM   1946 C CE  . LYS   C 1 68 ? 30.821  -25.520 11.569  1.00 57.03  ? 67  LYS   C CE  1 
ATOM   1947 N NZ  . LYS   C 1 68 ? 31.390  -25.959 10.292  1.00 60.20  ? 67  LYS   C NZ  1 
ATOM   1948 N N   . TYR   C 1 69 ? 24.947  -24.135 11.295  1.00 32.96  ? 68  TYR   C N   1 
ATOM   1949 C CA  . TYR   C 1 69 ? 24.125  -25.326 11.446  1.00 29.98  ? 68  TYR   C CA  1 
ATOM   1950 C C   . TYR   C 1 69 ? 22.644  -25.015 11.230  1.00 30.88  ? 68  TYR   C C   1 
ATOM   1951 O O   . TYR   C 1 69 ? 21.844  -25.942 11.098  1.00 30.94  ? 68  TYR   C O   1 
ATOM   1952 C CB  . TYR   C 1 69 ? 24.313  -25.909 12.861  1.00 28.50  ? 68  TYR   C CB  1 
ATOM   1953 C CG  . TYR   C 1 69 ? 25.740  -26.355 13.158  1.00 26.94  ? 68  TYR   C CG  1 
ATOM   1954 C CD1 . TYR   C 1 69 ? 26.444  -27.185 12.294  1.00 31.70  ? 68  TYR   C CD1 1 
ATOM   1955 C CD2 . TYR   C 1 69 ? 26.339  -25.963 14.354  1.00 34.02  ? 68  TYR   C CD2 1 
ATOM   1956 C CE1 . TYR   C 1 69 ? 27.733  -27.608 12.593  1.00 33.62  ? 68  TYR   C CE1 1 
ATOM   1957 C CE2 . TYR   C 1 69 ? 27.612  -26.403 14.676  1.00 35.42  ? 68  TYR   C CE2 1 
ATOM   1958 C CZ  . TYR   C 1 69 ? 28.306  -27.200 13.783  1.00 35.20  ? 68  TYR   C CZ  1 
ATOM   1959 O OH  . TYR   C 1 69 ? 29.568  -27.602 14.121  1.00 39.27  ? 68  TYR   C OH  1 
ATOM   1960 N N   . GLY   C 1 70 ? 22.274  -23.718 11.232  1.00 30.69  ? 69  GLY   C N   1 
ATOM   1961 C CA  . GLY   C 1 70 ? 20.855  -23.370 11.182  1.00 27.99  ? 69  GLY   C CA  1 
ATOM   1962 C C   . GLY   C 1 70 ? 20.428  -23.246 9.727   1.00 30.63  ? 69  GLY   C C   1 
ATOM   1963 O O   . GLY   C 1 70 ? 20.416  -22.148 9.165   1.00 30.69  ? 69  GLY   C O   1 
ATOM   1964 N N   . LYS   C 1 71 ? 20.331  -24.403 9.083   1.00 29.54  ? 70  LYS   C N   1 
ATOM   1965 C CA  . LYS   C 1 71 ? 19.980  -24.499 7.669   1.00 30.26  ? 70  LYS   C CA  1 
ATOM   1966 C C   . LYS   C 1 71 ? 19.105  -25.725 7.529   1.00 32.75  ? 70  LYS   C C   1 
ATOM   1967 O O   . LYS   C 1 71 ? 19.236  -26.698 8.271   1.00 30.41  ? 70  LYS   C O   1 
ATOM   1968 C CB  . LYS   C 1 71 ? 21.198  -24.603 6.737   1.00 33.57  ? 70  LYS   C CB  1 
ATOM   1969 C CG  . LYS   C 1 71 ? 22.159  -25.619 7.283   1.00 37.79  ? 70  LYS   C CG  1 
ATOM   1970 C CD  . LYS   C 1 71 ? 23.400  -26.008 6.495   1.00 44.42  ? 70  LYS   C CD  1 
ATOM   1971 C CE  . LYS   C 1 71 ? 24.064  -27.153 7.213   1.00 45.73  ? 70  LYS   C CE  1 
ATOM   1972 N N   . PRO   C 1 72 ? 18.134  -25.710 6.607   1.00 28.21  ? 71  PRO   C N   1 
ATOM   1973 C CA  . PRO   C 1 72 ? 17.220  -26.843 6.509   1.00 25.48  ? 71  PRO   C CA  1 
ATOM   1974 C C   . PRO   C 1 72 ? 17.871  -28.174 6.162   1.00 30.43  ? 71  PRO   C C   1 
ATOM   1975 O O   . PRO   C 1 72 ? 18.884  -28.260 5.443   1.00 30.87  ? 71  PRO   C O   1 
ATOM   1976 C CB  . PRO   C 1 72 ? 16.193  -26.414 5.436   1.00 26.91  ? 71  PRO   C CB  1 
ATOM   1977 C CG  . PRO   C 1 72 ? 16.324  -24.912 5.395   1.00 27.79  ? 71  PRO   C CG  1 
ATOM   1978 C CD  . PRO   C 1 72 ? 17.743  -24.548 5.784   1.00 26.89  ? 71  PRO   C CD  1 
ATOM   1979 N N   . ASN   C 1 73 ? 17.195  -29.204 6.642   1.00 27.94  ? 72  ASN   C N   1 
ATOM   1980 C CA  . ASN   C 1 73 ? 17.461  -30.495 6.044   1.00 33.85  ? 72  ASN   C CA  1 
ATOM   1981 C C   . ASN   C 1 73 ? 16.226  -31.367 6.205   1.00 29.71  ? 72  ASN   C C   1 
ATOM   1982 O O   . ASN   C 1 73 ? 15.293  -31.061 6.936   1.00 31.16  ? 72  ASN   C O   1 
ATOM   1983 C CB  . ASN   C 1 73 ? 18.835  -31.076 6.369   1.00 37.99  ? 72  ASN   C CB  1 
ATOM   1984 C CG  . ASN   C 1 73 ? 18.849  -31.684 7.746   1.00 40.09  ? 72  ASN   C CG  1 
ATOM   1985 O OD1 . ASN   C 1 73 ? 18.145  -32.671 8.006   1.00 37.46  ? 72  ASN   C OD1 1 
ATOM   1986 N ND2 . ASN   C 1 73 ? 19.698  -31.143 8.599   1.00 43.43  ? 72  ASN   C ND2 1 
ATOM   1987 N N   . LYS   C 1 74 ? 16.281  -32.496 5.525   1.00 30.79  ? 73  LYS   C N   1 
ATOM   1988 C CA  . LYS   C 1 74 ? 15.078  -33.283 5.325   1.00 27.35  ? 73  LYS   C CA  1 
ATOM   1989 C C   . LYS   C 1 74 ? 14.864  -34.293 6.435   1.00 29.68  ? 73  LYS   C C   1 
ATOM   1990 O O   . LYS   C 1 74 ? 13.824  -34.952 6.486   1.00 32.76  ? 73  LYS   C O   1 
ATOM   1991 C CB  . LYS   C 1 74 ? 15.220  -33.972 3.965   1.00 34.65  ? 73  LYS   C CB  1 
ATOM   1992 C CG  . LYS   C 1 74 ? 15.221  -32.972 2.803   1.00 41.10  ? 73  LYS   C CG  1 
ATOM   1993 C CD  . LYS   C 1 74 ? 13.768  -32.774 2.391   1.00 45.37  ? 73  LYS   C CD  1 
ATOM   1994 N N   . ARG   C 1 75 ? 15.771  -34.311 7.418   1.00 26.35  ? 74  ARG   C N   1 
ATOM   1995 C CA  . ARG   C 1 75 ? 15.592  -35.305 8.466   1.00 25.92  ? 74  ARG   C CA  1 
ATOM   1996 C C   . ARG   C 1 75 ? 14.305  -35.010 9.240   1.00 29.83  ? 74  ARG   C C   1 
ATOM   1997 O O   . ARG   C 1 75 ? 13.904  -33.848 9.434   1.00 30.94  ? 74  ARG   C O   1 
ATOM   1998 C CB  . ARG   C 1 75 ? 16.806  -35.327 9.423   1.00 28.75  ? 74  ARG   C CB  1 
ATOM   1999 C CG  . ARG   C 1 75 ? 18.166  -35.597 8.768   1.00 32.32  ? 74  ARG   C CG  1 
ATOM   2000 C CD  . ARG   C 1 75 ? 18.444  -37.000 8.202   1.00 36.62  ? 74  ARG   C CD  1 
ATOM   2001 N NE  . ARG   C 1 75 ? 18.470  -37.925 9.330   1.00 34.42  ? 74  ARG   C NE  1 
ATOM   2002 C CZ  . ARG   C 1 75 ? 19.635  -38.369 9.868   1.00 29.15  ? 74  ARG   C CZ  1 
ATOM   2003 N NH1 . ARG   C 1 75 ? 19.565  -38.996 11.006  1.00 31.48  ? 74  ARG   C NH1 1 
ATOM   2004 N NH2 . ARG   C 1 75 ? 20.788  -38.084 9.278   1.00 30.55  ? 74  ARG   C NH2 1 
ATOM   2005 N N   . LYS   C 1 76 ? 13.681  -36.083 9.737   1.00 31.23  ? 75  LYS   C N   1 
ATOM   2006 C CA  . LYS   C 1 76 ? 12.382  -35.997 10.374  1.00 33.01  ? 75  LYS   C CA  1 
ATOM   2007 C C   . LYS   C 1 76 ? 12.399  -35.023 11.551  1.00 29.92  ? 75  LYS   C C   1 
ATOM   2008 O O   . LYS   C 1 76 ? 13.148  -35.181 12.518  1.00 30.18  ? 75  LYS   C O   1 
ATOM   2009 C CB  . LYS   C 1 76 ? 11.810  -37.378 10.730  1.00 33.27  ? 75  LYS   C CB  1 
ATOM   2010 C CG  . LYS   C 1 76 ? 10.400  -37.302 11.256  1.00 33.98  ? 75  LYS   C CG  1 
ATOM   2011 C CD  . LYS   C 1 76 ? 9.811   -38.659 11.643  1.00 43.80  ? 75  LYS   C CD  1 
ATOM   2012 N N   . GLY   C 1 77 ? 11.589  -33.961 11.415  1.00 30.00  ? 76  GLY   C N   1 
ATOM   2013 C CA  . GLY   C 1 77 ? 11.329  -33.049 12.522  1.00 26.30  ? 76  GLY   C CA  1 
ATOM   2014 C C   . GLY   C 1 77 ? 12.280  -31.843 12.530  1.00 27.25  ? 76  GLY   C C   1 
ATOM   2015 O O   . GLY   C 1 77 ? 12.112  -30.947 13.342  1.00 30.53  ? 76  GLY   C O   1 
ATOM   2016 N N   . PHE   C 1 78 ? 13.294  -31.844 11.665  1.00 27.21  ? 77  PHE   C N   1 
ATOM   2017 C CA  . PHE   C 1 78 ? 14.381  -30.896 11.793  1.00 27.49  ? 77  PHE   C CA  1 
ATOM   2018 C C   . PHE   C 1 78 ? 13.866  -29.481 11.508  1.00 26.60  ? 77  PHE   C C   1 
ATOM   2019 O O   . PHE   C 1 78 ? 14.192  -28.531 12.220  1.00 25.84  ? 77  PHE   C O   1 
ATOM   2020 C CB  . PHE   C 1 78 ? 15.506  -31.315 10.843  1.00 29.62  ? 77  PHE   C CB  1 
ATOM   2021 C CG  . PHE   C 1 78 ? 16.777  -30.531 11.090  1.00 28.06  ? 77  PHE   C CG  1 
ATOM   2022 C CD1 . PHE   C 1 78 ? 16.954  -29.274 10.513  1.00 28.27  ? 77  PHE   C CD1 1 
ATOM   2023 C CD2 . PHE   C 1 78 ? 17.818  -31.067 11.837  1.00 26.81  ? 77  PHE   C CD2 1 
ATOM   2024 C CE1 . PHE   C 1 78 ? 18.115  -28.549 10.754  1.00 29.30  ? 77  PHE   C CE1 1 
ATOM   2025 C CE2 . PHE   C 1 78 ? 18.986  -30.353 12.058  1.00 26.78  ? 77  PHE   C CE2 1 
ATOM   2026 C CZ  . PHE   C 1 78 ? 19.151  -29.096 11.500  1.00 27.23  ? 77  PHE   C CZ  1 
ATOM   2027 N N   . ASN   C 1 79 ? 13.125  -29.354 10.403  1.00 28.53  ? 78  ASN   C N   1 
ATOM   2028 C CA  . ASN   C 1 79 ? 12.734  -28.013 9.988   1.00 29.21  ? 78  ASN   C CA  1 
ATOM   2029 C C   . ASN   C 1 79 ? 11.724  -27.388 10.946  1.00 27.52  ? 78  ASN   C C   1 
ATOM   2030 O O   . ASN   C 1 79 ? 11.785  -26.167 11.241  1.00 27.91  ? 78  ASN   C O   1 
ATOM   2031 C CB  . ASN   C 1 79 ? 12.283  -27.979 8.535   1.00 28.02  ? 78  ASN   C CB  1 
ATOM   2032 C CG  . ASN   C 1 79 ? 13.405  -28.315 7.581   1.00 27.73  ? 78  ASN   C CG  1 
ATOM   2033 O OD1 . ASN   C 1 79 ? 14.577  -28.042 7.863   1.00 25.93  ? 78  ASN   C OD1 1 
ATOM   2034 N ND2 . ASN   C 1 79 ? 13.069  -28.969 6.472   1.00 28.13  ? 78  ASN   C ND2 1 
ATOM   2035 N N   . GLU   C 1 80 ? 10.807  -28.207 11.457  1.00 27.57  ? 79  GLU   C N   1 
ATOM   2036 C CA  . GLU   C 1 80 ? 9.974   -27.726 12.549  1.00 28.93  ? 79  GLU   C CA  1 
ATOM   2037 C C   . GLU   C 1 80 ? 10.844  -27.285 13.738  1.00 36.69  ? 79  GLU   C C   1 
ATOM   2038 O O   . GLU   C 1 80 ? 10.601  -26.241 14.356  1.00 31.87  ? 79  GLU   C O   1 
ATOM   2039 C CB  . GLU   C 1 80 ? 8.873   -28.743 12.874  1.00 34.57  ? 79  GLU   C CB  1 
ATOM   2040 C CG  . GLU   C 1 80 ? 7.988   -28.291 14.032  1.00 31.83  ? 79  GLU   C CG  1 
ATOM   2041 C CD  . GLU   C 1 80 ? 6.729   -29.123 14.163  1.00 41.21  ? 79  GLU   C CD  1 
ATOM   2042 O OE1 . GLU   C 1 80 ? 6.629   -30.258 13.647  1.00 47.87  ? 79  GLU   C OE1 1 
ATOM   2043 O OE2 . GLU   C 1 80 ? 5.784   -28.582 14.754  1.00 42.07  ? 79  GLU   C OE2 1 
ATOM   2044 N N   . GLY   C 1 81 ? 11.888  -28.075 14.048  1.00 29.97  ? 80  GLY   C N   1 
ATOM   2045 C CA  . GLY   C 1 81 ? 12.835  -27.691 15.088  1.00 29.12  ? 80  GLY   C CA  1 
ATOM   2046 C C   . GLY   C 1 81 ? 13.487  -26.330 14.828  1.00 29.65  ? 80  GLY   C C   1 
ATOM   2047 O O   . GLY   C 1 81 ? 13.678  -25.570 15.778  1.00 30.23  ? 80  GLY   C O   1 
ATOM   2048 N N   . LEU   C 1 82 ? 13.931  -26.074 13.569  1.00 26.09  ? 81  LEU   C N   1 
ATOM   2049 C CA  . LEU   C 1 82 ? 14.479  -24.754 13.249  1.00 30.24  ? 81  LEU   C CA  1 
ATOM   2050 C C   . LEU   C 1 82 ? 13.444  -23.669 13.547  1.00 27.00  ? 81  LEU   C C   1 
ATOM   2051 O O   . LEU   C 1 82 ? 13.815  -22.590 14.033  1.00 28.97  ? 81  LEU   C O   1 
ATOM   2052 C CB  . LEU   C 1 82 ? 14.962  -24.661 11.805  1.00 29.53  ? 81  LEU   C CB  1 
ATOM   2053 C CG  . LEU   C 1 82 ? 16.169  -25.529 11.432  1.00 25.88  ? 81  LEU   C CG  1 
ATOM   2054 C CD1 . LEU   C 1 82 ? 16.446  -25.385 9.954   1.00 25.48  ? 81  LEU   C CD1 1 
ATOM   2055 C CD2 . LEU   C 1 82 ? 17.410  -25.145 12.200  1.00 21.73  ? 81  LEU   C CD2 1 
ATOM   2056 N N   . TRP   C 1 83 ? 12.167  -23.938 13.255  1.00 28.89  ? 82  TRP   C N   1 
ATOM   2057 C CA  . TRP   C 1 83 ? 11.168  -22.896 13.447  1.00 31.96  ? 82  TRP   C CA  1 
ATOM   2058 C C   . TRP   C 1 83 ? 11.039  -22.620 14.953  1.00 34.22  ? 82  TRP   C C   1 
ATOM   2059 O O   . TRP   C 1 83 ? 10.989  -21.472 15.402  1.00 33.73  ? 82  TRP   C O   1 
ATOM   2060 C CB  . TRP   C 1 83 ? 9.809   -23.279 12.829  1.00 30.31  ? 82  TRP   C CB  1 
ATOM   2061 C CG  . TRP   C 1 83 ? 8.820   -22.146 12.961  1.00 33.65  ? 82  TRP   C CG  1 
ATOM   2062 C CD1 . TRP   C 1 83 ? 8.690   -21.090 12.095  1.00 34.64  ? 82  TRP   C CD1 1 
ATOM   2063 C CD2 . TRP   C 1 83 ? 7.906   -21.895 14.053  1.00 37.14  ? 82  TRP   C CD2 1 
ATOM   2064 N NE1 . TRP   C 1 83 ? 7.709   -20.232 12.532  1.00 33.33  ? 82  TRP   C NE1 1 
ATOM   2065 C CE2 . TRP   C 1 83 ? 7.217   -20.695 13.733  1.00 36.13  ? 82  TRP   C CE2 1 
ATOM   2066 C CE3 . TRP   C 1 83 ? 7.590   -22.574 15.246  1.00 32.79  ? 82  TRP   C CE3 1 
ATOM   2067 C CZ2 . TRP   C 1 83 ? 6.239   -20.165 14.577  1.00 41.55  ? 82  TRP   C CZ2 1 
ATOM   2068 C CZ3 . TRP   C 1 83 ? 6.628   -22.038 16.079  1.00 43.96  ? 82  TRP   C CZ3 1 
ATOM   2069 C CH2 . TRP   C 1 83 ? 5.983   -20.842 15.754  1.00 40.94  ? 82  TRP   C CH2 1 
ATOM   2070 N N   . GLU   C 1 84 ? 11.039  -23.698 15.747  1.00 29.75  ? 83  GLU   C N   1 
ATOM   2071 C CA  . GLU   C 1 84 ? 10.902  -23.551 17.193  1.00 34.10  ? 83  GLU   C CA  1 
ATOM   2072 C C   . GLU   C 1 84 ? 12.070  -22.787 17.827  1.00 33.89  ? 83  GLU   C C   1 
ATOM   2073 O O   . GLU   C 1 84 ? 11.863  -21.886 18.650  1.00 34.02  ? 83  GLU   C O   1 
ATOM   2074 C CB  . GLU   C 1 84 ? 10.730  -24.911 17.872  1.00 32.08  ? 83  GLU   C CB  1 
ATOM   2075 C CG  . GLU   C 1 84 ? 9.413   -25.595 17.527  1.00 32.52  ? 83  GLU   C CG  1 
ATOM   2076 C CD  . GLU   C 1 84 ? 9.292   -27.032 17.971  1.00 36.06  ? 83  GLU   C CD  1 
ATOM   2077 O OE1 . GLU   C 1 84 ? 10.297  -27.581 18.527  1.00 35.14  ? 83  GLU   C OE1 1 
ATOM   2078 O OE2 . GLU   C 1 84 ? 8.187   -27.597 17.756  1.00 39.13  ? 83  GLU   C OE2 1 
ATOM   2079 N N   . ILE   C 1 85 ? 13.315  -23.133 17.479  1.00 32.12  ? 84  ILE   C N   1 
ATOM   2080 C CA  . ILE   C 1 85 ? 14.460  -22.508 18.120  1.00 33.22  ? 84  ILE   C CA  1 
ATOM   2081 C C   . ILE   C 1 85 ? 14.470  -20.988 17.883  1.00 33.84  ? 84  ILE   C C   1 
ATOM   2082 O O   . ILE   C 1 85 ? 14.890  -20.221 18.740  1.00 31.82  ? 84  ILE   C O   1 
ATOM   2083 C CB  . ILE   C 1 85 ? 15.788  -23.218 17.788  1.00 31.83  ? 84  ILE   C CB  1 
ATOM   2084 C CG1 . ILE   C 1 85 ? 16.864  -22.832 18.807  1.00 32.92  ? 84  ILE   C CG1 1 
ATOM   2085 C CG2 . ILE   C 1 85 ? 16.269  -22.967 16.339  1.00 29.94  ? 84  ILE   C CG2 1 
ATOM   2086 C CD1 . ILE   C 1 85 ? 17.983  -23.850 18.965  1.00 30.60  ? 84  ILE   C CD1 1 
ATOM   2087 N N   . GLN   C 1 86 ? 14.009  -20.567 16.701  1.00 30.25  ? 85  GLN   C N   1 
ATOM   2088 C CA  . GLN   C 1 86 ? 14.077  -19.156 16.325  1.00 33.97  ? 85  GLN   C CA  1 
ATOM   2089 C C   . GLN   C 1 86 ? 12.860  -18.381 16.834  1.00 34.12  ? 85  GLN   C C   1 
ATOM   2090 O O   . GLN   C 1 86 ? 12.985  -17.203 17.164  1.00 37.22  ? 85  GLN   C O   1 
ATOM   2091 C CB  . GLN   C 1 86 ? 14.206  -19.053 14.799  1.00 33.33  ? 85  GLN   C CB  1 
ATOM   2092 C CG  . GLN   C 1 86 ? 14.361  -17.623 14.263  1.00 34.46  ? 85  GLN   C CG  1 
ATOM   2093 C CD  . GLN   C 1 86 ? 14.761  -17.570 12.799  1.00 34.40  ? 85  GLN   C CD  1 
ATOM   2094 O OE1 . GLN   C 1 86 ? 14.760  -18.581 12.078  1.00 31.61  ? 85  GLN   C OE1 1 
ATOM   2095 N NE2 . GLN   C 1 86 ? 15.240  -16.412 12.367  1.00 36.93  ? 85  GLN   C NE2 1 
ATOM   2096 N N   . ASN   C 1 87 ? 11.705  -19.036 16.911  1.00 32.24  ? 86  ASN   C N   1 
ATOM   2097 C CA  . ASN   C 1 87 ? 10.426  -18.369 17.062  1.00 36.40  ? 86  ASN   C CA  1 
ATOM   2098 C C   . ASN   C 1 87 ? 9.768   -18.648 18.416  1.00 39.45  ? 86  ASN   C C   1 
ATOM   2099 O O   . ASN   C 1 87 ? 9.099   -17.766 18.941  1.00 41.38  ? 86  ASN   C O   1 
ATOM   2100 C CB  . ASN   C 1 87 ? 9.461   -18.681 15.930  1.00 37.12  ? 86  ASN   C CB  1 
ATOM   2101 C CG  . ASN   C 1 87 ? 9.955   -18.061 14.655  1.00 36.52  ? 86  ASN   C CG  1 
ATOM   2102 O OD1 . ASN   C 1 87 ? 10.032  -16.828 14.558  1.00 40.69  ? 86  ASN   C OD1 1 
ATOM   2103 N ND2 . ASN   C 1 87 ? 10.338  -18.898 13.701  1.00 32.36  ? 86  ASN   C ND2 1 
ATOM   2104 N N   . ASN   C 1 88 ? 9.905   -19.868 18.951  1.00 40.13  ? 87  ASN   C N   1 
ATOM   2105 C CA  . ASN   C 1 88 ? 9.147   -20.232 20.149  1.00 36.65  ? 87  ASN   C CA  1 
ATOM   2106 C C   . ASN   C 1 88 ? 9.992   -21.088 21.094  1.00 36.84  ? 87  ASN   C C   1 
ATOM   2107 O O   . ASN   C 1 88 ? 9.544   -22.174 21.483  1.00 40.45  ? 87  ASN   C O   1 
ATOM   2108 C CB  . ASN   C 1 88 ? 7.869   -20.983 19.784  1.00 42.49  ? 87  ASN   C CB  1 
ATOM   2109 C CG  . ASN   C 1 88 ? 6.856   -20.970 20.910  1.00 48.86  ? 87  ASN   C CG  1 
ATOM   2110 O OD1 . ASN   C 1 88 ? 6.997   -20.213 21.882  1.00 51.79  ? 87  ASN   C OD1 1 
ATOM   2111 N ND2 . ASN   C 1 88 ? 5.828   -21.793 20.793  1.00 47.78  ? 87  ASN   C ND2 1 
ATOM   2112 N N   . PRO   C 1 89 ? 11.223  -20.652 21.449  1.00 35.23  ? 88  PRO   C N   1 
ATOM   2113 C CA  . PRO   C 1 89 ? 12.210  -21.537 22.083  1.00 39.85  ? 88  PRO   C CA  1 
ATOM   2114 C C   . PRO   C 1 89 ? 12.000  -21.963 23.534  1.00 42.48  ? 88  PRO   C C   1 
ATOM   2115 O O   . PRO   C 1 89 ? 12.622  -22.926 24.001  1.00 39.26  ? 88  PRO   C O   1 
ATOM   2116 C CB  . PRO   C 1 89 ? 13.526  -20.787 21.916  1.00 36.92  ? 88  PRO   C CB  1 
ATOM   2117 C CG  . PRO   C 1 89 ? 13.101  -19.322 21.875  1.00 40.22  ? 88  PRO   C CG  1 
ATOM   2118 C CD  . PRO   C 1 89 ? 11.774  -19.321 21.152  1.00 39.14  ? 88  PRO   C CD  1 
ATOM   2119 N N   . HIS   C 1 90 ? 11.117  -21.241 24.227  1.00 46.63  ? 89  HIS   C N   1 
ATOM   2120 C CA  . HIS   C 1 90 ? 10.934  -21.466 25.653  1.00 47.29  ? 89  HIS   C CA  1 
ATOM   2121 C C   . HIS   C 1 90 ? 9.489   -21.874 25.960  1.00 51.39  ? 89  HIS   C C   1 
ATOM   2122 O O   . HIS   C 1 90 ? 9.070   -21.845 27.113  1.00 57.87  ? 89  HIS   C O   1 
ATOM   2123 C CB  . HIS   C 1 90 ? 11.505  -20.290 26.455  1.00 38.06  ? 89  HIS   C CB  1 
ATOM   2124 C CG  . HIS   C 1 90 ? 12.968  -19.992 26.285  1.00 33.10  ? 89  HIS   C CG  1 
ATOM   2125 N ND1 . HIS   C 1 90 ? 13.444  -18.825 25.726  1.00 39.00  ? 89  HIS   C ND1 1 
ATOM   2126 C CD2 . HIS   C 1 90 ? 14.058  -20.689 26.645  1.00 37.56  ? 89  HIS   C CD2 1 
ATOM   2127 C CE1 . HIS   C 1 90 ? 14.775  -18.822 25.734  1.00 40.78  ? 89  HIS   C CE1 1 
ATOM   2128 N NE2 . HIS   C 1 90 ? 15.178  -19.949 26.303  1.00 45.69  ? 89  HIS   C NE2 1 
ATOM   2129 N N   . ALA   C 1 91 ? 8.722   -22.272 24.937  1.00 51.09  ? 90  ALA   C N   1 
ATOM   2130 C CA  . ALA   C 1 91 ? 7.423   -22.900 25.149  1.00 52.06  ? 90  ALA   C CA  1 
ATOM   2131 C C   . ALA   C 1 91 ? 7.589   -24.324 25.687  1.00 53.63  ? 90  ALA   C C   1 
ATOM   2132 O O   . ALA   C 1 91 ? 8.699   -24.849 25.742  1.00 57.86  ? 90  ALA   C O   1 
ATOM   2133 C CB  . ALA   C 1 91 ? 6.594   -22.872 23.879  1.00 53.82  ? 90  ALA   C CB  1 
ATOM   2134 N N   . SER   C 1 92 ? 6.458   -24.963 26.021  1.00 60.30  ? 91  SER   C N   1 
ATOM   2135 C CA  . SER   C 1 92 ? 6.411   -26.177 26.831  1.00 66.25  ? 91  SER   C CA  1 
ATOM   2136 C C   . SER   C 1 92 ? 6.730   -27.447 26.044  1.00 65.49  ? 91  SER   C C   1 
ATOM   2137 O O   . SER   C 1 92 ? 7.576   -28.230 26.470  1.00 67.48  ? 91  SER   C O   1 
ATOM   2138 C CB  . SER   C 1 92 ? 5.076   -26.312 27.532  1.00 64.23  ? 91  SER   C CB  1 
ATOM   2139 O OG  . SER   C 1 92 ? 5.003   -25.400 28.615  1.00 66.04  ? 91  SER   C OG  1 
ATOM   2140 N N   . TYR   C 1 93 ? 5.974   -27.681 24.959  1.00 67.31  ? 92  TYR   C N   1 
ATOM   2141 C CA  . TYR   C 1 93 ? 6.043   -28.889 24.142  1.00 66.90  ? 92  TYR   C CA  1 
ATOM   2142 C C   . TYR   C 1 93 ? 5.975   -30.139 25.036  1.00 70.85  ? 92  TYR   C C   1 
ATOM   2143 O O   . TYR   C 1 93 ? 4.861   -30.538 25.444  1.00 75.71  ? 92  TYR   C O   1 
ATOM   2144 C CB  . TYR   C 1 93 ? 7.314   -28.916 23.284  1.00 64.89  ? 92  TYR   C CB  1 
ATOM   2145 C CG  . TYR   C 1 93 ? 7.640   -27.631 22.530  1.00 57.06  ? 92  TYR   C CG  1 
ATOM   2146 C CD1 . TYR   C 1 93 ? 6.953   -27.286 21.369  1.00 54.45  ? 92  TYR   C CD1 1 
ATOM   2147 C CD2 . TYR   C 1 93 ? 8.644   -26.775 22.974  1.00 50.34  ? 92  TYR   C CD2 1 
ATOM   2148 C CE1 . TYR   C 1 93 ? 7.246   -26.127 20.674  1.00 55.15  ? 92  TYR   C CE1 1 
ATOM   2149 C CE2 . TYR   C 1 93 ? 8.946   -25.610 22.283  1.00 51.87  ? 92  TYR   C CE2 1 
ATOM   2150 C CZ  . TYR   C 1 93 ? 8.250   -25.290 21.131  1.00 52.52  ? 92  TYR   C CZ  1 
ATOM   2151 O OH  . TYR   C 1 93 ? 8.544   -24.138 20.455  1.00 57.32  ? 92  TYR   C OH  1 
HETATM 2152 S S   . SO4   D 2 .  ? 1.648   -33.862 1.719   1.00 89.10  ? 101 SO4   A S   1 
HETATM 2153 O O1  . SO4   D 2 .  ? 2.473   -34.584 0.790   1.00 63.30  ? 101 SO4   A O1  1 
HETATM 2154 O O2  . SO4   D 2 .  ? 1.508   -32.491 1.289   1.00 80.94  ? 101 SO4   A O2  1 
HETATM 2155 O O3  . SO4   D 2 .  ? 0.348   -34.487 1.775   1.00 92.49  ? 101 SO4   A O3  1 
HETATM 2156 O O4  . SO4   D 2 .  ? 2.259   -33.894 3.025   1.00 86.99  ? 101 SO4   A O4  1 
HETATM 2157 S S   . SO4   E 2 .  ? -9.125  -24.698 1.309   1.00 96.17  ? 102 SO4   A S   1 
HETATM 2158 O O1  . SO4   E 2 .  ? -9.414  -24.507 -0.088  1.00 87.38  ? 102 SO4   A O1  1 
HETATM 2159 O O2  . SO4   E 2 .  ? -9.636  -23.581 2.060   1.00 94.59  ? 102 SO4   A O2  1 
HETATM 2160 O O3  . SO4   E 2 .  ? -9.735  -25.922 1.769   1.00 96.10  ? 102 SO4   A O3  1 
HETATM 2161 O O4  . SO4   E 2 .  ? -7.705  -24.783 1.500   1.00 104.86 ? 102 SO4   A O4  1 
HETATM 2162 C C1  . EDO   F 3 .  ? 14.244  -19.591 -7.485  1.00 34.49  ? 103 EDO   A C1  1 
HETATM 2163 O O1  . EDO   F 3 .  ? 15.467  -18.884 -7.210  1.00 30.33  ? 103 EDO   A O1  1 
HETATM 2164 C C2  . EDO   F 3 .  ? 13.349  -19.011 -8.564  1.00 32.01  ? 103 EDO   A C2  1 
HETATM 2165 O O2  . EDO   F 3 .  ? 12.911  -17.679 -8.321  1.00 31.77  ? 103 EDO   A O2  1 
HETATM 2166 S S   . SO4   G 2 .  ? 9.262   -29.682 5.818   1.00 49.36  ? 104 SO4   A S   1 
HETATM 2167 O O1  . SO4   G 2 .  ? 10.079  -28.910 4.987   1.00 37.63  ? 104 SO4   A O1  1 
HETATM 2168 O O2  . SO4   G 2 .  ? 8.743   -30.819 5.038   1.00 48.29  ? 104 SO4   A O2  1 
HETATM 2169 O O3  . SO4   G 2 .  ? 10.052  -30.172 6.941   1.00 52.15  ? 104 SO4   A O3  1 
HETATM 2170 O O4  . SO4   G 2 .  ? 8.133   -28.905 6.278   1.00 56.70  ? 104 SO4   A O4  1 
HETATM 2171 S S   . SO4   H 2 .  ? 7.206   -8.905  -25.118 1.00 55.58  ? 101 SO4   B S   1 
HETATM 2172 O O1  . SO4   H 2 .  ? 8.416   -8.492  -25.844 1.00 40.52  ? 101 SO4   B O1  1 
HETATM 2173 O O2  . SO4   H 2 .  ? 6.545   -9.993  -25.803 1.00 54.22  ? 101 SO4   B O2  1 
HETATM 2174 O O3  . SO4   H 2 .  ? 7.553   -9.341  -23.774 1.00 46.47  ? 101 SO4   B O3  1 
HETATM 2175 O O4  . SO4   H 2 .  ? 6.307   -7.783  -25.068 1.00 62.15  ? 101 SO4   B O4  1 
HETATM 2176 S S   . SO4   I 2 .  ? 14.706  -27.052 -26.596 1.00 51.68  ? 102 SO4   B S   1 
HETATM 2177 O O1  . SO4   I 2 .  ? 15.905  -26.399 -26.149 1.00 62.31  ? 102 SO4   B O1  1 
HETATM 2178 O O2  . SO4   I 2 .  ? 15.058  -28.253 -27.330 1.00 60.90  ? 102 SO4   B O2  1 
HETATM 2179 O O3  . SO4   I 2 .  ? 13.919  -27.409 -25.451 1.00 67.06  ? 102 SO4   B O3  1 
HETATM 2180 O O4  . SO4   I 2 .  ? 13.945  -26.169 -27.451 1.00 50.82  ? 102 SO4   B O4  1 
HETATM 2181 C C4  . A1A34 J 4 .  ? 19.388  -15.751 -22.232 0.72 33.39  ? 103 A1A34 B C4  1 
HETATM 2182 C C5  . A1A34 J 4 .  ? 20.006  -16.711 -21.446 0.72 37.17  ? 103 A1A34 B C5  1 
HETATM 2183 C C6  . A1A34 J 4 .  ? 21.354  -16.987 -21.588 0.72 41.28  ? 103 A1A34 B C6  1 
HETATM 2184 C C7  . A1A34 J 4 .  ? 22.140  -16.296 -22.510 0.72 37.97  ? 103 A1A34 B C7  1 
HETATM 2185 C C8  . A1A34 J 4 .  ? 23.618  -16.586 -22.642 0.72 41.61  ? 103 A1A34 B C8  1 
HETATM 2186 C C10 . A1A34 J 4 .  ? 20.171  -15.049 -23.153 0.72 32.88  ? 103 A1A34 B C10 1 
HETATM 2187 O O1  . A1A34 J 4 .  ? 17.276  -13.484 -23.980 0.72 29.09  ? 103 A1A34 B O1  1 
HETATM 2188 C C2  . A1A34 J 4 .  ? 16.979  -14.647 -24.259 0.72 27.99  ? 103 A1A34 B C2  1 
HETATM 2189 C C1  . A1A34 J 4 .  ? 16.291  -14.911 -25.582 0.72 29.14  ? 103 A1A34 B C1  1 
HETATM 2190 O O   . A1A34 J 4 .  ? 16.274  -16.286 -25.887 0.72 28.00  ? 103 A1A34 B O   1 
HETATM 2191 C C   . A1A34 J 4 .  ? 17.330  -16.668 -26.766 0.72 26.83  ? 103 A1A34 B C   1 
HETATM 2192 N N   . A1A34 J 4 .  ? 17.286  -15.699 -23.501 0.72 31.27  ? 103 A1A34 B N   1 
HETATM 2193 C C3  . A1A34 J 4 .  ? 17.891  -15.568 -22.176 0.72 29.98  ? 103 A1A34 B C3  1 
HETATM 2194 C C9  . A1A34 J 4 .  ? 21.521  -15.322 -23.293 0.72 33.95  ? 103 A1A34 B C9  1 
HETATM 2195 C C1  . EDO   K 3 .  ? 17.000  -36.385 16.293  1.00 31.51  ? 101 EDO   C C1  1 
HETATM 2196 O O1  . EDO   K 3 .  ? 15.890  -37.142 15.774  1.00 34.86  ? 101 EDO   C O1  1 
HETATM 2197 C C2  . EDO   K 3 .  ? 16.514  -35.467 17.398  1.00 28.06  ? 101 EDO   C C2  1 
HETATM 2198 O O2  . EDO   K 3 .  ? 15.661  -36.049 18.368  1.00 29.46  ? 101 EDO   C O2  1 
HETATM 2199 S S   . SO4   L 2 .  ? 29.441  -38.721 12.376  1.00 98.06  ? 102 SO4   C S   1 
HETATM 2200 O O1  . SO4   L 2 .  ? 30.621  -37.894 12.321  1.00 101.98 ? 102 SO4   C O1  1 
HETATM 2201 O O2  . SO4   L 2 .  ? 28.602  -38.436 11.245  1.00 86.69  ? 102 SO4   C O2  1 
HETATM 2202 O O3  . SO4   L 2 .  ? 29.818  -40.108 12.346  1.00 80.70  ? 102 SO4   C O3  1 
HETATM 2203 O O4  . SO4   L 2 .  ? 28.725  -38.445 13.591  1.00 102.66 ? 102 SO4   C O4  1 
HETATM 2204 O O   . HOH   M 5 .  ? 6.178   -28.981 6.751   1.00 51.24  ? 201 HOH   A O   1 
HETATM 2205 O O   . HOH   M 5 .  ? 9.311   -32.522 3.903   1.00 54.34  ? 202 HOH   A O   1 
HETATM 2206 O O   . HOH   M 5 .  ? -5.655  -13.419 -16.562 1.00 49.06  ? 203 HOH   A O   1 
HETATM 2207 O O   . HOH   M 5 .  ? 11.126  -19.501 10.213  1.00 49.24  ? 204 HOH   A O   1 
HETATM 2208 O O   . HOH   M 5 .  ? 4.127   -34.747 4.304   1.00 61.99  ? 205 HOH   A O   1 
HETATM 2209 O O   . HOH   M 5 .  ? 0.782   -10.722 -15.574 1.00 46.78  ? 206 HOH   A O   1 
HETATM 2210 O O   . HOH   M 5 .  ? -2.199  -30.881 -3.886  1.00 48.34  ? 207 HOH   A O   1 
HETATM 2211 O O   . HOH   M 5 .  ? 12.955  -12.307 8.141   1.00 47.33  ? 208 HOH   A O   1 
HETATM 2212 O O   . HOH   M 5 .  ? 9.427   -18.169 -10.979 1.00 33.20  ? 209 HOH   A O   1 
HETATM 2213 O O   . HOH   M 5 .  ? 11.473  -29.822 3.063   1.00 47.13  ? 210 HOH   A O   1 
HETATM 2214 O O   . HOH   M 5 .  ? -6.259  -25.547 -5.680  1.00 56.83  ? 211 HOH   A O   1 
HETATM 2215 O O   . HOH   M 5 .  ? 14.276  -15.760 -9.302  1.00 36.28  ? 212 HOH   A O   1 
HETATM 2216 O O   . HOH   M 5 .  ? 16.267  -24.553 1.941   1.00 38.64  ? 213 HOH   A O   1 
HETATM 2217 O O   . HOH   M 5 .  ? 7.337   -10.599 -12.183 1.00 33.70  ? 214 HOH   A O   1 
HETATM 2218 O O   . HOH   M 5 .  ? -2.418  -11.805 13.844  1.00 53.42  ? 215 HOH   A O   1 
HETATM 2219 O O   . HOH   M 5 .  ? 4.696   -3.622  -3.250  1.00 32.31  ? 216 HOH   A O   1 
HETATM 2220 O O   . HOH   M 5 .  ? -0.010  -33.875 4.378   1.00 54.73  ? 217 HOH   A O   1 
HETATM 2221 O O   . HOH   M 5 .  ? 4.852   -7.903  1.082   1.00 32.58  ? 218 HOH   A O   1 
HETATM 2222 O O   . HOH   M 5 .  ? -1.964  3.217   -2.117  1.00 36.46  ? 219 HOH   A O   1 
HETATM 2223 O O   . HOH   M 5 .  ? 11.554  -23.839 9.727   1.00 33.30  ? 220 HOH   A O   1 
HETATM 2224 O O   . HOH   M 5 .  ? -3.559  -10.926 6.829   1.00 37.79  ? 221 HOH   A O   1 
HETATM 2225 O O   . HOH   M 5 .  ? 9.874   -6.012  -1.616  1.00 30.71  ? 222 HOH   A O   1 
HETATM 2226 O O   . HOH   M 5 .  ? 10.889  -9.458  -13.603 1.00 56.49  ? 223 HOH   A O   1 
HETATM 2227 O O   . HOH   M 5 .  ? 2.813   -25.253 -10.086 1.00 34.63  ? 224 HOH   A O   1 
HETATM 2228 O O   . HOH   M 5 .  ? 9.708   -22.849 -9.544  1.00 38.04  ? 225 HOH   A O   1 
HETATM 2229 O O   . HOH   M 5 .  ? 20.137  -15.502 7.346   1.00 28.59  ? 226 HOH   A O   1 
HETATM 2230 O O   . HOH   M 5 .  ? -8.536  -18.801 -3.326  1.00 45.59  ? 227 HOH   A O   1 
HETATM 2231 O O   . HOH   M 5 .  ? 3.513   -29.642 -0.526  1.00 35.96  ? 228 HOH   A O   1 
HETATM 2232 O O   . HOH   M 5 .  ? 11.137  -5.171  -7.775  1.00 34.19  ? 229 HOH   A O   1 
HETATM 2233 O O   . HOH   M 5 .  ? 1.247   -24.886 13.869  1.00 44.70  ? 230 HOH   A O   1 
HETATM 2234 O O   . HOH   M 5 .  ? -7.643  -17.183 6.533   1.00 38.56  ? 231 HOH   A O   1 
HETATM 2235 O O   . HOH   M 5 .  ? 13.783  -28.080 -4.876  1.00 49.31  ? 232 HOH   A O   1 
HETATM 2236 O O   . HOH   M 5 .  ? -0.319  -21.046 6.956   1.00 31.66  ? 233 HOH   A O   1 
HETATM 2237 O O   . HOH   M 5 .  ? 17.512  -12.886 1.355   1.00 21.22  ? 234 HOH   A O   1 
HETATM 2238 O O   . HOH   M 5 .  ? 9.160   -16.222 -13.237 1.00 36.48  ? 235 HOH   A O   1 
HETATM 2239 O O   . HOH   M 5 .  ? 2.058   0.557   -7.418  1.00 35.38  ? 236 HOH   A O   1 
HETATM 2240 O O   . HOH   M 5 .  ? 1.851   -18.638 -18.704 1.00 38.27  ? 237 HOH   A O   1 
HETATM 2241 O O   . HOH   M 5 .  ? 13.565  -12.010 -4.228  1.00 21.14  ? 238 HOH   A O   1 
HETATM 2242 O O   . HOH   M 5 .  ? 6.837   -5.960  0.295   1.00 49.31  ? 239 HOH   A O   1 
HETATM 2243 O O   . HOH   M 5 .  ? -7.859  -15.741 -1.032  1.00 35.35  ? 240 HOH   A O   1 
HETATM 2244 O O   . HOH   M 5 .  ? -7.477  -20.755 -3.717  1.00 68.21  ? 241 HOH   A O   1 
HETATM 2245 O O   . HOH   M 5 .  ? 11.737  -12.411 -6.210  1.00 27.29  ? 242 HOH   A O   1 
HETATM 2246 O O   . HOH   M 5 .  ? -5.533  -15.950 -8.069  1.00 27.26  ? 243 HOH   A O   1 
HETATM 2247 O O   . HOH   M 5 .  ? 21.897  -20.455 -3.901  1.00 49.57  ? 244 HOH   A O   1 
HETATM 2248 O O   . HOH   M 5 .  ? 11.754  -11.962 5.860   1.00 34.20  ? 245 HOH   A O   1 
HETATM 2249 O O   . HOH   M 5 .  ? -7.602  -16.790 1.661   1.00 39.17  ? 246 HOH   A O   1 
HETATM 2250 O O   . HOH   M 5 .  ? -1.483  -22.074 -0.680  1.00 26.20  ? 247 HOH   A O   1 
HETATM 2251 O O   . HOH   M 5 .  ? 13.217  -9.619  -7.190  1.00 40.19  ? 248 HOH   A O   1 
HETATM 2252 O O   . HOH   M 5 .  ? 3.063   -10.119 -13.332 1.00 44.63  ? 249 HOH   A O   1 
HETATM 2253 O O   . HOH   M 5 .  ? -0.536  -29.534 9.822   1.00 54.19  ? 250 HOH   A O   1 
HETATM 2254 O O   . HOH   M 5 .  ? 10.240  -13.126 9.737   1.00 36.23  ? 251 HOH   A O   1 
HETATM 2255 O O   . HOH   M 5 .  ? 16.850  -12.024 -17.233 1.00 38.20  ? 252 HOH   A O   1 
HETATM 2256 O O   . HOH   M 5 .  ? -3.847  -21.336 6.132   1.00 39.09  ? 253 HOH   A O   1 
HETATM 2257 O O   . HOH   M 5 .  ? -0.299  -20.698 10.918  1.00 71.54  ? 254 HOH   A O   1 
HETATM 2258 O O   . HOH   M 5 .  ? 15.958  -12.019 -5.313  1.00 32.04  ? 255 HOH   A O   1 
HETATM 2259 O O   . HOH   M 5 .  ? 11.962  -16.539 -14.898 1.00 40.00  ? 256 HOH   A O   1 
HETATM 2260 O O   . HOH   M 5 .  ? -5.633  -19.831 -5.673  1.00 34.64  ? 257 HOH   A O   1 
HETATM 2261 O O   . HOH   M 5 .  ? 2.045   -4.676  -10.289 1.00 34.77  ? 258 HOH   A O   1 
HETATM 2262 O O   . HOH   M 5 .  ? 0.481   -23.418 9.055   1.00 45.58  ? 259 HOH   A O   1 
HETATM 2263 O O   . HOH   M 5 .  ? 11.685  -6.063  -3.919  1.00 44.39  ? 260 HOH   A O   1 
HETATM 2264 O O   . HOH   M 5 .  ? 6.483   -16.460 -15.045 1.00 45.79  ? 261 HOH   A O   1 
HETATM 2265 O O   . HOH   M 5 .  ? -1.337  -11.875 11.218  1.00 37.79  ? 262 HOH   A O   1 
HETATM 2266 O O   . HOH   M 5 .  ? 1.847   -10.539 11.558  1.00 34.52  ? 263 HOH   A O   1 
HETATM 2267 O O   . HOH   M 5 .  ? 10.089  -20.331 -18.661 1.00 42.44  ? 264 HOH   A O   1 
HETATM 2268 O O   . HOH   M 5 .  ? 8.257   -7.884  1.204   1.00 30.06  ? 265 HOH   A O   1 
HETATM 2269 O O   . HOH   M 5 .  ? -6.095  -11.722 -11.438 1.00 40.17  ? 266 HOH   A O   1 
HETATM 2270 O O   . HOH   M 5 .  ? 9.023   -17.980 -15.763 1.00 54.55  ? 267 HOH   A O   1 
HETATM 2271 O O   . HOH   M 5 .  ? 5.326   -7.596  3.982   1.00 32.93  ? 268 HOH   A O   1 
HETATM 2272 O O   . HOH   M 5 .  ? -1.268  -7.508  11.428  1.00 37.44  ? 269 HOH   A O   1 
HETATM 2273 O O   . HOH   M 5 .  ? -8.342  -21.274 -1.234  1.00 42.52  ? 270 HOH   A O   1 
HETATM 2274 O O   . HOH   M 5 .  ? -4.073  -25.927 -5.686  1.00 46.49  ? 271 HOH   A O   1 
HETATM 2275 O O   . HOH   M 5 .  ? 10.483  -27.666 -7.376  1.00 51.49  ? 272 HOH   A O   1 
HETATM 2276 O O   . HOH   M 5 .  ? 13.055  -13.504 -8.480  1.00 43.26  ? 273 HOH   A O   1 
HETATM 2277 O O   . HOH   M 5 .  ? 8.385   -17.667 8.753   1.00 44.36  ? 274 HOH   A O   1 
HETATM 2278 O O   . HOH   M 5 .  ? 2.417   -24.985 -6.432  1.00 51.15  ? 275 HOH   A O   1 
HETATM 2279 O O   . HOH   M 5 .  ? 15.717  -28.287 -0.808  1.00 54.63  ? 276 HOH   A O   1 
HETATM 2280 O O   . HOH   M 5 .  ? -4.884  -8.277  -11.085 1.00 63.57  ? 277 HOH   A O   1 
HETATM 2281 O O   . HOH   M 5 .  ? -11.307 -15.950 -4.062  1.00 51.77  ? 278 HOH   A O   1 
HETATM 2282 O O   . HOH   M 5 .  ? 11.375  -7.892  0.379   1.00 25.07  ? 279 HOH   A O   1 
HETATM 2283 O O   . HOH   M 5 .  ? -5.902  -12.738 6.742   1.00 35.61  ? 280 HOH   A O   1 
HETATM 2284 O O   . HOH   M 5 .  ? 22.566  -16.727 -0.417  1.00 40.29  ? 281 HOH   A O   1 
HETATM 2285 O O   . HOH   M 5 .  ? -7.211  -21.634 -6.072  1.00 52.53  ? 282 HOH   A O   1 
HETATM 2286 O O   . HOH   M 5 .  ? -7.020  -11.530 -8.023  1.00 28.08  ? 283 HOH   A O   1 
HETATM 2287 O O   . HOH   M 5 .  ? 21.738  -16.744 -3.506  1.00 28.78  ? 284 HOH   A O   1 
HETATM 2288 O O   . HOH   M 5 .  ? 12.384  -16.455 -12.166 1.00 64.14  ? 285 HOH   A O   1 
HETATM 2289 O O   . HOH   M 5 .  ? 17.468  -18.132 -9.633  1.00 45.15  ? 286 HOH   A O   1 
HETATM 2290 O O   . HOH   M 5 .  ? 9.434   -2.308  -0.195  1.00 66.29  ? 287 HOH   A O   1 
HETATM 2291 O O   . HOH   M 5 .  ? -5.766  -26.698 3.256   1.00 46.89  ? 288 HOH   A O   1 
HETATM 2292 O O   . HOH   M 5 .  ? -3.899  -26.486 7.648   1.00 57.69  ? 289 HOH   A O   1 
HETATM 2293 O O   . HOH   M 5 .  ? -5.278  -23.627 -6.810  1.00 40.39  ? 290 HOH   A O   1 
HETATM 2294 O O   . HOH   M 5 .  ? -3.612  -7.902  10.651  1.00 42.67  ? 291 HOH   A O   1 
HETATM 2295 O O   . HOH   M 5 .  ? 8.887   -9.153  -13.899 1.00 35.23  ? 292 HOH   A O   1 
HETATM 2296 O O   . HOH   M 5 .  ? -3.678  -11.141 9.549   1.00 47.33  ? 293 HOH   A O   1 
HETATM 2297 O O   . HOH   M 5 .  ? 12.190  -21.314 10.600  1.00 40.63  ? 294 HOH   A O   1 
HETATM 2298 O O   . HOH   M 5 .  ? 1.416   -29.557 -7.287  1.00 57.02  ? 295 HOH   A O   1 
HETATM 2299 O O   . HOH   M 5 .  ? -7.113  -14.129 -9.276  1.00 36.83  ? 296 HOH   A O   1 
HETATM 2300 O O   . HOH   M 5 .  ? -0.295  -3.191  -11.013 1.00 55.35  ? 297 HOH   A O   1 
HETATM 2301 O O   . HOH   M 5 .  ? -5.609  -22.439 5.995   1.00 55.03  ? 298 HOH   A O   1 
HETATM 2302 O O   . HOH   M 5 .  ? -9.974  -28.453 -1.825  1.00 48.85  ? 299 HOH   A O   1 
HETATM 2303 O O   . HOH   M 5 .  ? 5.204   -7.201  -11.247 1.00 46.75  ? 300 HOH   A O   1 
HETATM 2304 O O   . HOH   M 5 .  ? 11.650  -1.966  -1.922  1.00 44.14  ? 301 HOH   A O   1 
HETATM 2305 O O   . HOH   M 5 .  ? -11.039 -13.645 -2.794  1.00 38.50  ? 302 HOH   A O   1 
HETATM 2306 O O   . HOH   M 5 .  ? 5.834   -3.486  0.762   1.00 57.92  ? 303 HOH   A O   1 
HETATM 2307 O O   . HOH   M 5 .  ? 8.292   -8.357  4.539   1.00 36.71  ? 304 HOH   A O   1 
HETATM 2308 O O   . HOH   M 5 .  ? 4.894   -9.560  -11.398 1.00 43.32  ? 305 HOH   A O   1 
HETATM 2309 O O   . HOH   M 5 .  ? -2.714  -21.441 8.057   1.00 41.45  ? 306 HOH   A O   1 
HETATM 2310 O O   . HOH   M 5 .  ? 7.992   -30.723 -2.186  1.00 56.66  ? 307 HOH   A O   1 
HETATM 2311 O O   . HOH   M 5 .  ? -6.873  -19.121 8.676   1.00 47.57  ? 308 HOH   A O   1 
HETATM 2312 O O   . HOH   M 5 .  ? 8.837   -22.560 -19.319 1.00 54.89  ? 309 HOH   A O   1 
HETATM 2313 O O   . HOH   M 5 .  ? -4.808  -21.162 -8.076  1.00 45.86  ? 310 HOH   A O   1 
HETATM 2314 O O   . HOH   N 5 .  ? 30.604  -8.023  -30.256 1.00 53.06  ? 201 HOH   B O   1 
HETATM 2315 O O   . HOH   N 5 .  ? 20.281  -22.050 -23.379 1.00 60.62  ? 202 HOH   B O   1 
HETATM 2316 O O   . HOH   N 5 .  ? 10.160  -11.096 -38.254 1.00 54.09  ? 203 HOH   B O   1 
HETATM 2317 O O   . HOH   N 5 .  ? 6.576   -12.534 -26.195 1.00 43.40  ? 204 HOH   B O   1 
HETATM 2318 O O   . HOH   N 5 .  ? 23.725  -11.135 -22.092 1.00 38.84  ? 205 HOH   B O   1 
HETATM 2319 O O   . HOH   N 5 .  ? 30.303  -19.736 -40.544 1.00 37.03  ? 206 HOH   B O   1 
HETATM 2320 O O   . HOH   N 5 .  ? 26.256  -23.037 -31.414 1.00 37.82  ? 207 HOH   B O   1 
HETATM 2321 O O   . HOH   N 5 .  ? 16.182  -17.134 -19.021 1.00 39.02  ? 208 HOH   B O   1 
HETATM 2322 O O   . HOH   N 5 .  ? 27.825  -8.176  -28.912 1.00 41.25  ? 209 HOH   B O   1 
HETATM 2323 O O   . HOH   N 5 .  ? 20.742  -13.295 -42.960 1.00 40.36  ? 210 HOH   B O   1 
HETATM 2324 O O   . HOH   N 5 .  ? 25.087  -5.018  -29.972 1.00 37.76  ? 211 HOH   B O   1 
HETATM 2325 O O   . HOH   N 5 .  ? 12.933  -4.530  -42.100 1.00 57.60  ? 212 HOH   B O   1 
HETATM 2326 O O   . HOH   N 5 .  ? 3.056   -8.829  -27.440 1.00 52.90  ? 213 HOH   B O   1 
HETATM 2327 O O   . HOH   N 5 .  ? 23.498  -2.130  -29.393 1.00 43.21  ? 214 HOH   B O   1 
HETATM 2328 O O   . HOH   N 5 .  ? 10.238  -16.801 -44.509 1.00 40.09  ? 215 HOH   B O   1 
HETATM 2329 O O   . HOH   N 5 .  ? 24.536  -1.693  -36.495 1.00 47.89  ? 216 HOH   B O   1 
HETATM 2330 O O   . HOH   N 5 .  ? 25.914  -4.446  -33.874 1.00 50.49  ? 217 HOH   B O   1 
HETATM 2331 O O   . HOH   N 5 .  ? 11.242  -7.928  -41.665 1.00 47.78  ? 218 HOH   B O   1 
HETATM 2332 O O   . HOH   N 5 .  ? 5.988   -7.266  -32.329 1.00 47.05  ? 219 HOH   B O   1 
HETATM 2333 O O   . HOH   N 5 .  ? 35.090  -22.996 -30.295 1.00 70.01  ? 220 HOH   B O   1 
HETATM 2334 O O   . HOH   N 5 .  ? 21.792  3.719   -32.803 1.00 42.68  ? 221 HOH   B O   1 
HETATM 2335 O O   . HOH   N 5 .  ? 16.868  -19.238 -29.091 1.00 24.83  ? 222 HOH   B O   1 
HETATM 2336 O O   . HOH   N 5 .  ? 8.974   -8.755  -16.680 1.00 40.65  ? 223 HOH   B O   1 
HETATM 2337 O O   . HOH   N 5 .  ? 8.517   -27.638 -38.499 1.00 55.37  ? 224 HOH   B O   1 
HETATM 2338 O O   . HOH   N 5 .  ? 27.839  -17.515 -25.285 1.00 46.63  ? 225 HOH   B O   1 
HETATM 2339 O O   . HOH   N 5 .  ? 18.371  -0.429  -25.553 1.00 58.91  ? 226 HOH   B O   1 
HETATM 2340 O O   . HOH   N 5 .  ? 10.550  -18.825 -33.140 1.00 30.48  ? 227 HOH   B O   1 
HETATM 2341 O O   . HOH   N 5 .  ? 18.175  -0.477  -38.704 1.00 28.31  ? 228 HOH   B O   1 
HETATM 2342 O O   . HOH   N 5 .  ? 17.662  -19.731 -42.387 1.00 45.05  ? 229 HOH   B O   1 
HETATM 2343 O O   . HOH   N 5 .  ? 10.444  -19.295 -43.362 1.00 60.26  ? 230 HOH   B O   1 
HETATM 2344 O O   . HOH   N 5 .  ? 13.772  -22.503 -20.770 1.00 49.38  ? 231 HOH   B O   1 
HETATM 2345 O O   . HOH   N 5 .  ? 23.803  -4.090  -37.065 1.00 32.49  ? 232 HOH   B O   1 
HETATM 2346 O O   . HOH   N 5 .  ? 22.783  -23.114 -28.999 1.00 41.36  ? 233 HOH   B O   1 
HETATM 2347 O O   . HOH   N 5 .  ? 14.350  -6.281  -41.363 1.00 40.00  ? 234 HOH   B O   1 
HETATM 2348 O O   . HOH   N 5 .  ? 25.306  -5.754  -36.099 1.00 41.86  ? 235 HOH   B O   1 
HETATM 2349 O O   . HOH   N 5 .  ? 17.934  -15.900 -45.994 1.00 44.91  ? 236 HOH   B O   1 
HETATM 2350 O O   . HOH   N 5 .  ? 20.523  -10.086 -43.217 1.00 39.76  ? 237 HOH   B O   1 
HETATM 2351 O O   . HOH   N 5 .  ? 27.270  -10.366 -29.128 1.00 49.70  ? 238 HOH   B O   1 
HETATM 2352 O O   . HOH   N 5 .  ? 32.596  -18.908 -42.572 1.00 50.22  ? 239 HOH   B O   1 
HETATM 2353 O O   . HOH   N 5 .  ? 7.164   -19.305 -35.130 1.00 48.57  ? 240 HOH   B O   1 
HETATM 2354 O O   . HOH   N 5 .  ? 19.826  -25.656 -34.363 1.00 39.07  ? 241 HOH   B O   1 
HETATM 2355 O O   . HOH   N 5 .  ? 10.687  -21.872 -32.905 1.00 36.05  ? 242 HOH   B O   1 
HETATM 2356 O O   . HOH   N 5 .  ? 21.052  -26.276 -30.200 1.00 69.15  ? 243 HOH   B O   1 
HETATM 2357 O O   . HOH   N 5 .  ? 8.105   -23.317 -24.299 1.00 60.23  ? 244 HOH   B O   1 
HETATM 2358 O O   . HOH   N 5 .  ? 17.633  -3.524  -22.243 1.00 60.33  ? 245 HOH   B O   1 
HETATM 2359 O O   . HOH   N 5 .  ? 7.644   -8.125  -21.020 1.00 49.84  ? 246 HOH   B O   1 
HETATM 2360 O O   . HOH   N 5 .  ? 14.672  -24.426 -40.601 1.00 40.45  ? 247 HOH   B O   1 
HETATM 2361 O O   . HOH   N 5 .  ? 20.404  -2.593  -23.028 1.00 64.11  ? 248 HOH   B O   1 
HETATM 2362 O O   . HOH   N 5 .  ? 7.619   -18.455 -31.739 1.00 45.36  ? 249 HOH   B O   1 
HETATM 2363 O O   . HOH   N 5 .  ? 31.627  -12.400 -38.731 1.00 67.57  ? 250 HOH   B O   1 
HETATM 2364 O O   . HOH   N 5 .  ? 38.696  -13.115 -40.301 1.00 70.17  ? 251 HOH   B O   1 
HETATM 2365 O O   . HOH   N 5 .  ? 1.993   -13.315 -28.482 1.00 45.92  ? 252 HOH   B O   1 
HETATM 2366 O O   . HOH   N 5 .  ? 31.970  -21.232 -38.458 1.00 43.22  ? 253 HOH   B O   1 
HETATM 2367 O O   . HOH   N 5 .  ? 16.854  -9.545  -44.161 1.00 50.12  ? 254 HOH   B O   1 
HETATM 2368 O O   . HOH   N 5 .  ? 24.985  -6.400  -42.890 1.00 47.88  ? 255 HOH   B O   1 
HETATM 2369 O O   . HOH   N 5 .  ? 12.227  -4.653  -24.918 1.00 45.18  ? 256 HOH   B O   1 
HETATM 2370 O O   . HOH   N 5 .  ? 27.896  -24.766 -35.357 1.00 39.59  ? 257 HOH   B O   1 
HETATM 2371 O O   . HOH   N 5 .  ? 20.979  -6.459  -42.874 1.00 37.13  ? 258 HOH   B O   1 
HETATM 2372 O O   . HOH   N 5 .  ? 18.609  -25.920 -29.093 1.00 41.86  ? 259 HOH   B O   1 
HETATM 2373 O O   . HOH   N 5 .  ? 26.150  -0.225  -29.609 1.00 51.75  ? 260 HOH   B O   1 
HETATM 2374 O O   . HOH   N 5 .  ? 6.606   -20.560 -25.003 1.00 37.28  ? 261 HOH   B O   1 
HETATM 2375 O O   . HOH   N 5 .  ? 18.449  4.604   -34.518 1.00 36.90  ? 262 HOH   B O   1 
HETATM 2376 O O   . HOH   N 5 .  ? 20.104  -7.690  -21.148 1.00 50.33  ? 263 HOH   B O   1 
HETATM 2377 O O   . HOH   N 5 .  ? 7.655   -12.482 -39.327 1.00 55.09  ? 264 HOH   B O   1 
HETATM 2378 O O   . HOH   N 5 .  ? 25.047  -8.297  -22.706 1.00 56.75  ? 265 HOH   B O   1 
HETATM 2379 O O   . HOH   N 5 .  ? 20.379  4.038   -33.288 1.00 39.81  ? 266 HOH   B O   1 
HETATM 2380 O O   . HOH   N 5 .  ? 15.373  -8.123  -43.323 1.00 40.65  ? 267 HOH   B O   1 
HETATM 2381 O O   . HOH   N 5 .  ? 9.730   -5.990  -41.268 1.00 53.85  ? 268 HOH   B O   1 
HETATM 2382 O O   . HOH   N 5 .  ? 13.283  -20.076 -19.545 1.00 49.87  ? 269 HOH   B O   1 
HETATM 2383 O O   . HOH   N 5 .  ? 16.415  -25.542 -20.691 1.00 63.87  ? 270 HOH   B O   1 
HETATM 2384 O O   . HOH   N 5 .  ? 11.494  -24.013 -30.105 1.00 43.77  ? 271 HOH   B O   1 
HETATM 2385 O O   . HOH   N 5 .  ? 15.162  -21.799 -42.206 1.00 50.37  ? 272 HOH   B O   1 
HETATM 2386 O O   . HOH   N 5 .  ? 7.339   -10.012 -18.698 1.00 42.70  ? 273 HOH   B O   1 
HETATM 2387 O O   . HOH   N 5 .  ? 22.600  -29.285 -35.882 1.00 43.28  ? 274 HOH   B O   1 
HETATM 2388 O O   . HOH   O 5 .  ? 27.035  -37.850 10.226  1.00 44.09  ? 201 HOH   C O   1 
HETATM 2389 O O   . HOH   O 5 .  ? 30.055  -27.783 30.718  1.00 54.97  ? 202 HOH   C O   1 
HETATM 2390 O O   . HOH   O 5 .  ? 20.016  -19.606 29.953  1.00 55.16  ? 203 HOH   C O   1 
HETATM 2391 O O   . HOH   O 5 .  ? 26.799  -39.471 12.753  1.00 40.33  ? 204 HOH   C O   1 
HETATM 2392 O O   . HOH   O 5 .  ? 30.269  -16.727 11.910  1.00 52.58  ? 205 HOH   C O   1 
HETATM 2393 O O   . HOH   O 5 .  ? 12.318  -28.533 28.064  1.00 53.06  ? 206 HOH   C O   1 
HETATM 2394 O O   . HOH   O 5 .  ? 14.753  -39.111 16.811  1.00 50.77  ? 207 HOH   C O   1 
HETATM 2395 O O   . HOH   O 5 .  ? 17.519  -17.227 15.217  1.00 42.84  ? 208 HOH   C O   1 
HETATM 2396 O O   . HOH   O 5 .  ? 16.426  -38.099 19.764  1.00 46.33  ? 209 HOH   C O   1 
HETATM 2397 O O   . HOH   O 5 .  ? 28.039  -37.589 25.142  1.00 47.93  ? 210 HOH   C O   1 
HETATM 2398 O O   . HOH   O 5 .  ? 25.870  -19.649 6.468   1.00 38.19  ? 211 HOH   C O   1 
HETATM 2399 O O   . HOH   O 5 .  ? 23.448  -41.742 18.474  1.00 37.96  ? 212 HOH   C O   1 
HETATM 2400 O O   . HOH   O 5 .  ? 19.309  -20.285 10.625  1.00 37.44  ? 213 HOH   C O   1 
HETATM 2401 O O   . HOH   O 5 .  ? 31.824  -33.397 25.970  1.00 43.48  ? 214 HOH   C O   1 
HETATM 2402 O O   . HOH   O 5 .  ? 13.041  -31.676 8.209   1.00 30.67  ? 215 HOH   C O   1 
HETATM 2403 O O   . HOH   O 5 .  ? 15.362  -21.146 12.276  1.00 34.24  ? 216 HOH   C O   1 
HETATM 2404 O O   . HOH   O 5 .  ? 20.005  -41.186 39.458  1.00 66.92  ? 217 HOH   C O   1 
HETATM 2405 O O   . HOH   O 5 .  ? 9.171   -37.218 18.049  1.00 57.95  ? 218 HOH   C O   1 
HETATM 2406 O O   . HOH   O 5 .  ? 23.537  -18.582 21.790  1.00 51.44  ? 219 HOH   C O   1 
HETATM 2407 O O   . HOH   O 5 .  ? 31.276  -29.749 32.059  1.00 55.97  ? 220 HOH   C O   1 
HETATM 2408 O O   . HOH   O 5 .  ? 20.239  -41.970 12.192  1.00 26.32  ? 221 HOH   C O   1 
HETATM 2409 O O   . HOH   O 5 .  ? 28.292  -37.396 16.023  1.00 40.26  ? 222 HOH   C O   1 
HETATM 2410 O O   . HOH   O 5 .  ? 14.894  -37.352 13.280  1.00 40.50  ? 223 HOH   C O   1 
HETATM 2411 O O   . HOH   O 5 .  ? 23.831  -21.023 23.976  1.00 47.41  ? 224 HOH   C O   1 
HETATM 2412 O O   . HOH   O 5 .  ? 15.922  -17.783 19.343  1.00 41.58  ? 225 HOH   C O   1 
HETATM 2413 O O   . HOH   O 5 .  ? 33.522  -24.555 31.667  1.00 49.83  ? 226 HOH   C O   1 
HETATM 2414 O O   . HOH   O 5 .  ? 5.777   -26.725 16.773  1.00 57.07  ? 227 HOH   C O   1 
HETATM 2415 O O   . HOH   O 5 .  ? 21.153  -28.805 8.407   1.00 34.86  ? 228 HOH   C O   1 
HETATM 2416 O O   . HOH   O 5 .  ? 22.374  -34.492 16.618  1.00 24.23  ? 229 HOH   C O   1 
HETATM 2417 O O   . HOH   O 5 .  ? 30.667  -31.488 15.819  1.00 43.47  ? 230 HOH   C O   1 
HETATM 2418 O O   . HOH   O 5 .  ? 30.632  -17.517 9.649   1.00 47.20  ? 231 HOH   C O   1 
HETATM 2419 O O   . HOH   O 5 .  ? 22.463  -28.690 11.129  1.00 33.31  ? 232 HOH   C O   1 
HETATM 2420 O O   . HOH   O 5 .  ? 25.972  -17.528 13.907  1.00 39.01  ? 233 HOH   C O   1 
HETATM 2421 O O   . HOH   O 5 .  ? 25.420  -31.364 10.890  1.00 35.26  ? 234 HOH   C O   1 
HETATM 2422 O O   . HOH   O 5 .  ? 20.879  -40.148 26.488  1.00 40.26  ? 235 HOH   C O   1 
HETATM 2423 O O   . HOH   O 5 .  ? 25.926  -34.031 34.977  1.00 53.51  ? 236 HOH   C O   1 
HETATM 2424 O O   . HOH   O 5 .  ? 25.774  -17.844 21.103  1.00 73.09  ? 237 HOH   C O   1 
HETATM 2425 O O   . HOH   O 5 .  ? 10.010  -30.485 9.902   1.00 31.70  ? 238 HOH   C O   1 
HETATM 2426 O O   . HOH   O 5 .  ? 7.259   -17.894 10.922  1.00 35.71  ? 239 HOH   C O   1 
HETATM 2427 O O   . HOH   O 5 .  ? 29.919  -40.065 31.526  1.00 37.53  ? 240 HOH   C O   1 
HETATM 2428 O O   . HOH   O 5 .  ? 8.227   -32.019 12.021  1.00 49.18  ? 241 HOH   C O   1 
HETATM 2429 O O   . HOH   O 5 .  ? 31.750  -43.388 15.961  1.00 43.50  ? 242 HOH   C O   1 
HETATM 2430 O O   . HOH   O 5 .  ? 9.006   -19.017 23.580  1.00 43.00  ? 243 HOH   C O   1 
HETATM 2431 O O   . HOH   O 5 .  ? 30.990  -29.225 12.173  1.00 47.14  ? 244 HOH   C O   1 
HETATM 2432 O O   . HOH   O 5 .  ? 4.167   -22.833 18.620  1.00 63.88  ? 245 HOH   C O   1 
HETATM 2433 O O   . HOH   O 5 .  ? 25.889  -39.753 20.297  1.00 33.11  ? 246 HOH   C O   1 
HETATM 2434 O O   . HOH   O 5 .  ? 19.302  -26.846 2.888   1.00 51.34  ? 247 HOH   C O   1 
HETATM 2435 O O   . HOH   O 5 .  ? 28.469  -15.115 12.971  1.00 59.46  ? 248 HOH   C O   1 
HETATM 2436 O O   . HOH   O 5 .  ? 21.509  -29.596 4.976   1.00 56.82  ? 249 HOH   C O   1 
HETATM 2437 O O   . HOH   O 5 .  ? 14.620  -29.614 3.960   1.00 37.28  ? 250 HOH   C O   1 
HETATM 2438 O O   . HOH   O 5 .  ? 31.510  -40.005 27.203  1.00 40.92  ? 251 HOH   C O   1 
HETATM 2439 O O   . HOH   O 5 .  ? 19.824  -19.154 25.242  1.00 58.17  ? 252 HOH   C O   1 
HETATM 2440 O O   . HOH   O 5 .  ? 14.757  -38.926 9.462   1.00 55.26  ? 253 HOH   C O   1 
HETATM 2441 O O   . HOH   O 5 .  ? 28.847  -25.336 32.971  1.00 53.01  ? 254 HOH   C O   1 
HETATM 2442 O O   . HOH   O 5 .  ? 30.561  -32.665 18.370  1.00 47.45  ? 255 HOH   C O   1 
HETATM 2443 O O   . HOH   O 5 .  ? 30.629  -35.964 28.773  1.00 48.60  ? 256 HOH   C O   1 
HETATM 2444 O O   . HOH   O 5 .  ? 17.645  -21.299 12.641  1.00 49.33  ? 257 HOH   C O   1 
HETATM 2445 O O   . HOH   O 5 .  ? 32.175  -43.839 11.952  1.00 55.28  ? 258 HOH   C O   1 
HETATM 2446 O O   . HOH   O 5 .  ? 20.783  -13.054 13.402  1.00 48.91  ? 259 HOH   C O   1 
HETATM 2447 O O   . HOH   O 5 .  ? 17.470  -36.847 29.246  1.00 53.33  ? 260 HOH   C O   1 
HETATM 2448 O O   . HOH   O 5 .  ? 29.343  -41.762 27.369  1.00 40.65  ? 261 HOH   C O   1 
HETATM 2449 O O   . HOH   O 5 .  ? 2.954   -29.395 12.733  1.00 65.98  ? 262 HOH   C O   1 
HETATM 2450 O O   . HOH   O 5 .  ? 22.761  -13.865 13.567  1.00 50.72  ? 263 HOH   C O   1 
HETATM 2451 O O   . HOH   O 5 .  ? 13.532  -23.125 28.060  1.00 55.82  ? 264 HOH   C O   1 
HETATM 2452 O O   . HOH   O 5 .  ? 24.019  -15.909 11.989  1.00 44.45  ? 265 HOH   C O   1 
HETATM 2453 O O   . HOH   O 5 .  ? 28.482  -41.794 29.957  1.00 39.06  ? 266 HOH   C O   1 
HETATM 2454 O O   . HOH   O 5 .  ? 33.831  -44.725 15.476  1.00 37.65  ? 267 HOH   C O   1 
HETATM 2455 O O   . HOH   O 5 .  ? 37.278  -24.445 27.042  1.00 83.79  ? 268 HOH   C O   1 
# 
