data_7HGV
# 
_entry.id   7HGV 
# 
_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   7HGV         pdb_00007hgv 10.2210/pdb7hgv/pdb 
WWPDB D_1001407457 ?            ?                   
# 
_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             ? 
# 
loop_
_database_PDB_caveat.id 
_database_PDB_caveat.text 
1 'A1A33 B 103 HAS WRONG CHIRALITY AT ATOM C6' 
2 'A1A33 C 102 HAS WRONG CHIRALITY AT ATOM C6' 
# 
_pdbx_database_status.entry_id                        7HGV 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-29 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.email 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
5 'von Delft' Frank  ?  frank.von-delft@diamond.ac.uk 'principal investigator/group leader' 0000-0003-0378-0017 
6 Strelkov    Sergei V. sergei.strelkov@kuleuven.be   'principal investigator/group leader' 0000-0003-3101-2867 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Vantieghem, T.'  1 
'Osipov, E.'      2 
'Fearon, D.'      3 
'Douangamath, A.' 4 
'von Delft, F.'   5 
'Strelkov, S.'    6 
# 
_citation.id                        primary 
_citation.title                     'Rational fragment-based design of compounds targeting the PWWP domain of the HRP family.' 
_citation.journal_abbrev            Eur.J.Med.Chem. 
_citation.journal_volume            280 
_citation.page_first                116960 
_citation.page_last                 116960 
_citation.year                      2024 
_citation.pdbx_database_id_PubMed   39461037 
_citation.pdbx_database_id_DOI      10.1016/j.ejmech.2024.116960 
_citation.journal_id_ASTM           EJMCA5 
_citation.country                   FR 
_citation.journal_id_ISSN           0223-5234 
_citation.journal_id_CSD            0493 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Vantieghem, T.'   ? 1  
primary 'Aslam, N.A.'      ? 2  
primary 'Osipov, E.M.'     ? 3  
primary 'Akele, M.'        ? 4  
primary 'Van Belle, S.'    ? 5  
primary 'Beelen, S.'       ? 6  
primary 'Drexler, M.'      ? 7  
primary 'Paulovcakova, T.' ? 8  
primary 'Lux, V.'          ? 9  
primary 'Fearon, D.'       ? 10 
primary 'Douangamath, A.'  ? 11 
primary 'von Delft, F.'    ? 12 
primary 'Christ, F.'       ? 13 
primary 'Veverka, V.'      ? 14 
primary 'Verwilst, P.'     ? 15 
primary 'Van Aerschot, A.' ? 16 
primary 'Debyser, Z.'      ? 17 
primary 'Strelkov, S.V.'   ? 18 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Hepatoma-derived growth factor-related protein 2' 10698.171 3   ? C64S ? ? 
2 non-polymer syn 'SULFATE ION'                                      96.063    6   ? ?    ? ? 
3 non-polymer syn 1,2-ETHANEDIOL                                     62.068    1   ? ?    ? ? 
4 non-polymer syn '[(3S)-1-(propan-2-yl)piperidin-3-yl]methanol'     157.253   3   ? ?    ? ? 
5 water       nat water                                              18.015    277 ? ?    ? ? 
# 
_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 '[(3S)-1-(propan-2-yl)piperidin-3-yl]methanol' A1A33 
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 
A1A33 non-polymer         . '[(3S)-1-(propan-2-yl)piperidin-3-yl]methanol' ?                 'C9 H19 N O'     157.253 
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        A1A33 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1A33 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
D 2 SO4   1   101 95  SO4   SO4 A . 
E 2 SO4   1   102 96  SO4   SO4 A . 
F 3 EDO   1   103 97  EDO   EDO A . 
G 4 A1A33 1   104 101 A1A33 LIG A . 
H 2 SO4   1   105 4   SO4   SO4 A . 
I 2 SO4   1   101 1   SO4   SO4 B . 
J 2 SO4   1   102 3   SO4   SO4 B . 
K 4 A1A33 1   103 101 A1A33 LIG B . 
L 2 SO4   1   101 5   SO4   SO4 C . 
M 4 A1A33 1   102 101 A1A33 LIG C . 
N 5 HOH   1   201 290 HOH   HOH A . 
N 5 HOH   2   202 304 HOH   HOH A . 
N 5 HOH   3   203 202 HOH   HOH A . 
N 5 HOH   4   204 307 HOH   HOH A . 
N 5 HOH   5   205 84  HOH   HOH A . 
N 5 HOH   6   206 339 HOH   HOH A . 
N 5 HOH   7   207 357 HOH   HOH A . 
N 5 HOH   8   208 66  HOH   HOH A . 
N 5 HOH   9   209 95  HOH   HOH A . 
N 5 HOH   10  210 139 HOH   HOH A . 
N 5 HOH   11  211 55  HOH   HOH A . 
N 5 HOH   12  212 293 HOH   HOH A . 
N 5 HOH   13  213 86  HOH   HOH A . 
N 5 HOH   14  214 71  HOH   HOH A . 
N 5 HOH   15  215 91  HOH   HOH A . 
N 5 HOH   16  216 87  HOH   HOH A . 
N 5 HOH   17  217 34  HOH   HOH A . 
N 5 HOH   18  218 199 HOH   HOH A . 
N 5 HOH   19  219 26  HOH   HOH A . 
N 5 HOH   20  220 28  HOH   HOH A . 
N 5 HOH   21  221 289 HOH   HOH A . 
N 5 HOH   22  222 208 HOH   HOH A . 
N 5 HOH   23  223 37  HOH   HOH A . 
N 5 HOH   24  224 7   HOH   HOH A . 
N 5 HOH   25  225 341 HOH   HOH A . 
N 5 HOH   26  226 85  HOH   HOH A . 
N 5 HOH   27  227 260 HOH   HOH A . 
N 5 HOH   28  228 167 HOH   HOH A . 
N 5 HOH   29  229 8   HOH   HOH A . 
N 5 HOH   30  230 363 HOH   HOH A . 
N 5 HOH   31  231 27  HOH   HOH A . 
N 5 HOH   32  232 287 HOH   HOH A . 
N 5 HOH   33  233 179 HOH   HOH A . 
N 5 HOH   34  234 97  HOH   HOH A . 
N 5 HOH   35  235 370 HOH   HOH A . 
N 5 HOH   36  236 23  HOH   HOH A . 
N 5 HOH   37  237 203 HOH   HOH A . 
N 5 HOH   38  238 12  HOH   HOH A . 
N 5 HOH   39  239 47  HOH   HOH A . 
N 5 HOH   40  240 267 HOH   HOH A . 
N 5 HOH   41  241 21  HOH   HOH A . 
N 5 HOH   42  242 32  HOH   HOH A . 
N 5 HOH   43  243 78  HOH   HOH A . 
N 5 HOH   44  244 99  HOH   HOH A . 
N 5 HOH   45  245 297 HOH   HOH A . 
N 5 HOH   46  246 1   HOH   HOH A . 
N 5 HOH   47  247 288 HOH   HOH A . 
N 5 HOH   48  248 188 HOH   HOH A . 
N 5 HOH   49  249 60  HOH   HOH A . 
N 5 HOH   50  250 2   HOH   HOH A . 
N 5 HOH   51  251 94  HOH   HOH A . 
N 5 HOH   52  252 218 HOH   HOH A . 
N 5 HOH   53  253 58  HOH   HOH A . 
N 5 HOH   54  254 274 HOH   HOH A . 
N 5 HOH   55  255 145 HOH   HOH A . 
N 5 HOH   56  256 111 HOH   HOH A . 
N 5 HOH   57  257 190 HOH   HOH A . 
N 5 HOH   58  258 259 HOH   HOH A . 
N 5 HOH   59  259 164 HOH   HOH A . 
N 5 HOH   60  260 131 HOH   HOH A . 
N 5 HOH   61  261 109 HOH   HOH A . 
N 5 HOH   62  262 292 HOH   HOH A . 
N 5 HOH   63  263 300 HOH   HOH A . 
N 5 HOH   64  264 18  HOH   HOH A . 
N 5 HOH   65  265 42  HOH   HOH A . 
N 5 HOH   66  266 20  HOH   HOH A . 
N 5 HOH   67  267 77  HOH   HOH A . 
N 5 HOH   68  268 116 HOH   HOH A . 
N 5 HOH   69  269 93  HOH   HOH A . 
N 5 HOH   70  270 143 HOH   HOH A . 
N 5 HOH   71  271 64  HOH   HOH A . 
N 5 HOH   72  272 14  HOH   HOH A . 
N 5 HOH   73  273 31  HOH   HOH A . 
N 5 HOH   74  274 38  HOH   HOH A . 
N 5 HOH   75  275 222 HOH   HOH A . 
N 5 HOH   76  276 377 HOH   HOH A . 
N 5 HOH   77  277 115 HOH   HOH A . 
N 5 HOH   78  278 301 HOH   HOH A . 
N 5 HOH   79  279 9   HOH   HOH A . 
N 5 HOH   80  280 19  HOH   HOH A . 
N 5 HOH   81  281 73  HOH   HOH A . 
N 5 HOH   82  282 16  HOH   HOH A . 
N 5 HOH   83  283 165 HOH   HOH A . 
N 5 HOH   84  284 368 HOH   HOH A . 
N 5 HOH   85  285 327 HOH   HOH A . 
N 5 HOH   86  286 281 HOH   HOH A . 
N 5 HOH   87  287 152 HOH   HOH A . 
N 5 HOH   88  288 113 HOH   HOH A . 
N 5 HOH   89  289 22  HOH   HOH A . 
N 5 HOH   90  290 318 HOH   HOH A . 
N 5 HOH   91  291 356 HOH   HOH A . 
N 5 HOH   92  292 63  HOH   HOH A . 
N 5 HOH   93  293 338 HOH   HOH A . 
N 5 HOH   94  294 146 HOH   HOH A . 
N 5 HOH   95  295 365 HOH   HOH A . 
N 5 HOH   96  296 270 HOH   HOH A . 
N 5 HOH   97  297 210 HOH   HOH A . 
N 5 HOH   98  298 83  HOH   HOH A . 
N 5 HOH   99  299 185 HOH   HOH A . 
N 5 HOH   100 300 211 HOH   HOH A . 
N 5 HOH   101 301 219 HOH   HOH A . 
N 5 HOH   102 302 347 HOH   HOH A . 
N 5 HOH   103 303 205 HOH   HOH A . 
N 5 HOH   104 304 35  HOH   HOH A . 
N 5 HOH   105 305 57  HOH   HOH A . 
N 5 HOH   106 306 156 HOH   HOH A . 
N 5 HOH   107 307 283 HOH   HOH A . 
N 5 HOH   108 308 75  HOH   HOH A . 
N 5 HOH   109 309 125 HOH   HOH A . 
N 5 HOH   110 310 332 HOH   HOH A . 
O 5 HOH   1   201 350 HOH   HOH B . 
O 5 HOH   2   202 331 HOH   HOH B . 
O 5 HOH   3   203 247 HOH   HOH B . 
O 5 HOH   4   204 89  HOH   HOH B . 
O 5 HOH   5   205 272 HOH   HOH B . 
O 5 HOH   6   206 258 HOH   HOH B . 
O 5 HOH   7   207 123 HOH   HOH B . 
O 5 HOH   8   208 98  HOH   HOH B . 
O 5 HOH   9   209 17  HOH   HOH B . 
O 5 HOH   10  210 69  HOH   HOH B . 
O 5 HOH   11  211 177 HOH   HOH B . 
O 5 HOH   12  212 249 HOH   HOH B . 
O 5 HOH   13  213 224 HOH   HOH B . 
O 5 HOH   14  214 153 HOH   HOH B . 
O 5 HOH   15  215 333 HOH   HOH B . 
O 5 HOH   16  216 242 HOH   HOH B . 
O 5 HOH   17  217 329 HOH   HOH B . 
O 5 HOH   18  218 375 HOH   HOH B . 
O 5 HOH   19  219 337 HOH   HOH B . 
O 5 HOH   20  220 280 HOH   HOH B . 
O 5 HOH   21  221 334 HOH   HOH B . 
O 5 HOH   22  222 371 HOH   HOH B . 
O 5 HOH   23  223 172 HOH   HOH B . 
O 5 HOH   24  224 261 HOH   HOH B . 
O 5 HOH   25  225 10  HOH   HOH B . 
O 5 HOH   26  226 137 HOH   HOH B . 
O 5 HOH   27  227 320 HOH   HOH B . 
O 5 HOH   28  228 54  HOH   HOH B . 
O 5 HOH   29  229 223 HOH   HOH B . 
O 5 HOH   30  230 68  HOH   HOH B . 
O 5 HOH   31  231 5   HOH   HOH B . 
O 5 HOH   32  232 6   HOH   HOH B . 
O 5 HOH   33  233 150 HOH   HOH B . 
O 5 HOH   34  234 315 HOH   HOH B . 
O 5 HOH   35  235 59  HOH   HOH B . 
O 5 HOH   36  236 24  HOH   HOH B . 
O 5 HOH   37  237 215 HOH   HOH B . 
O 5 HOH   38  238 168 HOH   HOH B . 
O 5 HOH   39  239 119 HOH   HOH B . 
O 5 HOH   40  240 355 HOH   HOH B . 
O 5 HOH   41  241 25  HOH   HOH B . 
O 5 HOH   42  242 61  HOH   HOH B . 
O 5 HOH   43  243 117 HOH   HOH B . 
O 5 HOH   44  244 79  HOH   HOH B . 
O 5 HOH   45  245 169 HOH   HOH B . 
O 5 HOH   46  246 101 HOH   HOH B . 
O 5 HOH   47  247 13  HOH   HOH B . 
O 5 HOH   48  248 170 HOH   HOH B . 
O 5 HOH   49  249 74  HOH   HOH B . 
O 5 HOH   50  250 120 HOH   HOH B . 
O 5 HOH   51  251 214 HOH   HOH B . 
O 5 HOH   52  252 345 HOH   HOH B . 
O 5 HOH   53  253 96  HOH   HOH B . 
O 5 HOH   54  254 336 HOH   HOH B . 
O 5 HOH   55  255 197 HOH   HOH B . 
O 5 HOH   56  256 217 HOH   HOH B . 
O 5 HOH   57  257 76  HOH   HOH B . 
O 5 HOH   58  258 335 HOH   HOH B . 
O 5 HOH   59  259 46  HOH   HOH B . 
O 5 HOH   60  260 348 HOH   HOH B . 
O 5 HOH   61  261 72  HOH   HOH B . 
O 5 HOH   62  262 175 HOH   HOH B . 
O 5 HOH   63  263 157 HOH   HOH B . 
O 5 HOH   64  264 44  HOH   HOH B . 
O 5 HOH   65  265 36  HOH   HOH B . 
O 5 HOH   66  266 378 HOH   HOH B . 
O 5 HOH   67  267 182 HOH   HOH B . 
O 5 HOH   68  268 104 HOH   HOH B . 
O 5 HOH   69  269 358 HOH   HOH B . 
O 5 HOH   70  270 279 HOH   HOH B . 
O 5 HOH   71  271 352 HOH   HOH B . 
O 5 HOH   72  272 322 HOH   HOH B . 
O 5 HOH   73  273 303 HOH   HOH B . 
O 5 HOH   74  274 160 HOH   HOH B . 
O 5 HOH   75  275 379 HOH   HOH B . 
O 5 HOH   76  276 291 HOH   HOH B . 
O 5 HOH   77  277 354 HOH   HOH B . 
O 5 HOH   78  278 340 HOH   HOH B . 
O 5 HOH   79  279 163 HOH   HOH B . 
O 5 HOH   80  280 316 HOH   HOH B . 
O 5 HOH   81  281 103 HOH   HOH B . 
O 5 HOH   82  282 201 HOH   HOH B . 
O 5 HOH   83  283 346 HOH   HOH B . 
O 5 HOH   84  284 314 HOH   HOH B . 
O 5 HOH   85  285 362 HOH   HOH B . 
O 5 HOH   86  286 107 HOH   HOH B . 
O 5 HOH   87  287 312 HOH   HOH B . 
P 5 HOH   1   201 254 HOH   HOH C . 
P 5 HOH   2   202 323 HOH   HOH C . 
P 5 HOH   3   203 321 HOH   HOH C . 
P 5 HOH   4   204 161 HOH   HOH C . 
P 5 HOH   5   205 226 HOH   HOH C . 
P 5 HOH   6   206 360 HOH   HOH C . 
P 5 HOH   7   207 118 HOH   HOH C . 
P 5 HOH   8   208 271 HOH   HOH C . 
P 5 HOH   9   209 344 HOH   HOH C . 
P 5 HOH   10  210 317 HOH   HOH C . 
P 5 HOH   11  211 90  HOH   HOH C . 
P 5 HOH   12  212 173 HOH   HOH C . 
P 5 HOH   13  213 142 HOH   HOH C . 
P 5 HOH   14  214 302 HOH   HOH C . 
P 5 HOH   15  215 330 HOH   HOH C . 
P 5 HOH   16  216 132 HOH   HOH C . 
P 5 HOH   17  217 134 HOH   HOH C . 
P 5 HOH   18  218 269 HOH   HOH C . 
P 5 HOH   19  219 126 HOH   HOH C . 
P 5 HOH   20  220 48  HOH   HOH C . 
P 5 HOH   21  221 189 HOH   HOH C . 
P 5 HOH   22  222 82  HOH   HOH C . 
P 5 HOH   23  223 148 HOH   HOH C . 
P 5 HOH   24  224 15  HOH   HOH C . 
P 5 HOH   25  225 374 HOH   HOH C . 
P 5 HOH   26  226 294 HOH   HOH C . 
P 5 HOH   27  227 380 HOH   HOH C . 
P 5 HOH   28  228 284 HOH   HOH C . 
P 5 HOH   29  229 343 HOH   HOH C . 
P 5 HOH   30  230 198 HOH   HOH C . 
P 5 HOH   31  231 275 HOH   HOH C . 
P 5 HOH   32  232 309 HOH   HOH C . 
P 5 HOH   33  233 295 HOH   HOH C . 
P 5 HOH   34  234 102 HOH   HOH C . 
P 5 HOH   35  235 366 HOH   HOH C . 
P 5 HOH   36  236 4   HOH   HOH C . 
P 5 HOH   37  237 41  HOH   HOH C . 
P 5 HOH   38  238 45  HOH   HOH C . 
P 5 HOH   39  239 53  HOH   HOH C . 
P 5 HOH   40  240 351 HOH   HOH C . 
P 5 HOH   41  241 40  HOH   HOH C . 
P 5 HOH   42  242 184 HOH   HOH C . 
P 5 HOH   43  243 43  HOH   HOH C . 
P 5 HOH   44  244 122 HOH   HOH C . 
P 5 HOH   45  245 67  HOH   HOH C . 
P 5 HOH   46  246 49  HOH   HOH C . 
P 5 HOH   47  247 342 HOH   HOH C . 
P 5 HOH   48  248 56  HOH   HOH C . 
P 5 HOH   49  249 209 HOH   HOH C . 
P 5 HOH   50  250 299 HOH   HOH C . 
P 5 HOH   51  251 62  HOH   HOH C . 
P 5 HOH   52  252 151 HOH   HOH C . 
P 5 HOH   53  253 171 HOH   HOH C . 
P 5 HOH   54  254 298 HOH   HOH C . 
P 5 HOH   55  255 328 HOH   HOH C . 
P 5 HOH   56  256 135 HOH   HOH C . 
P 5 HOH   57  257 65  HOH   HOH C . 
P 5 HOH   58  258 149 HOH   HOH C . 
P 5 HOH   59  259 376 HOH   HOH C . 
P 5 HOH   60  260 373 HOH   HOH C . 
P 5 HOH   61  261 130 HOH   HOH C . 
P 5 HOH   62  262 305 HOH   HOH C . 
P 5 HOH   63  263 364 HOH   HOH C . 
P 5 HOH   64  264 319 HOH   HOH C . 
P 5 HOH   65  265 108 HOH   HOH C . 
P 5 HOH   66  266 241 HOH   HOH C . 
P 5 HOH   67  267 369 HOH   HOH C . 
P 5 HOH   68  268 70  HOH   HOH C . 
P 5 HOH   69  269 324 HOH   HOH C . 
P 5 HOH   70  270 372 HOH   HOH C . 
P 5 HOH   71  271 381 HOH   HOH C . 
P 5 HOH   72  272 353 HOH   HOH C . 
P 5 HOH   73  273 361 HOH   HOH C . 
P 5 HOH   74  274 92  HOH   HOH C . 
P 5 HOH   75  275 367 HOH   HOH C . 
P 5 HOH   76  276 246 HOH   HOH C . 
P 5 HOH   77  277 349 HOH   HOH C . 
P 5 HOH   78  278 313 HOH   HOH C . 
P 5 HOH   79  279 206 HOH   HOH C . 
P 5 HOH   80  280 310 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 ASP 62 ? CG  ? A ASP 63 CG  
2  1 Y 1 A ASP 62 ? OD1 ? A ASP 63 OD1 
3  1 Y 1 A ASP 62 ? OD2 ? A ASP 63 OD2 
4  1 Y 1 A LYS 70 ? CE  ? A LYS 71 CE  
5  1 Y 1 A LYS 70 ? NZ  ? A LYS 71 NZ  
6  1 Y 1 A LYS 73 ? CD  ? A LYS 74 CD  
7  1 Y 1 A LYS 73 ? CE  ? A LYS 74 CE  
8  1 Y 1 A LYS 73 ? NZ  ? A LYS 74 NZ  
9  1 Y 1 A LYS 75 ? NZ  ? A LYS 76 NZ  
10 1 Y 1 B LYS 16 ? CE  ? B LYS 17 CE  
11 1 Y 1 B LYS 16 ? NZ  ? B LYS 17 NZ  
12 1 Y 1 B ILE 28 ? CG1 ? B ILE 29 CG1 
13 1 Y 1 B ILE 28 ? CG2 ? B ILE 29 CG2 
14 1 Y 1 B ILE 28 ? CD1 ? B ILE 29 CD1 
15 1 Y 1 B LYS 34 ? CG  ? B LYS 35 CG  
16 1 Y 1 B LYS 34 ? CD  ? B LYS 35 CD  
17 1 Y 1 B LYS 34 ? CE  ? B LYS 35 CE  
18 1 Y 1 B LYS 34 ? NZ  ? B LYS 35 NZ  
19 1 Y 1 B LYS 73 ? CE  ? B LYS 74 CE  
20 1 Y 1 B LYS 73 ? NZ  ? B LYS 74 NZ  
21 1 Y 1 B GLU 79 ? CD  ? B GLU 80 CD  
22 1 Y 1 B GLU 79 ? OE1 ? B GLU 80 OE1 
23 1 Y 1 B GLU 79 ? OE2 ? B GLU 80 OE2 
24 1 Y 1 C HIS 3  ? CG  ? C HIS 4  CG  
25 1 Y 1 C HIS 3  ? ND1 ? C HIS 4  ND1 
26 1 Y 1 C HIS 3  ? CD2 ? C HIS 4  CD2 
27 1 Y 1 C HIS 3  ? CE1 ? C HIS 4  CE1 
28 1 Y 1 C HIS 3  ? NE2 ? C HIS 4  NE2 
29 1 Y 1 C LYS 6  ? CG  ? C LYS 7  CG  
30 1 Y 1 C LYS 6  ? CD  ? C LYS 7  CD  
31 1 Y 1 C LYS 6  ? CE  ? C LYS 7  CE  
32 1 Y 1 C LYS 6  ? NZ  ? C LYS 7  NZ  
33 1 Y 1 C ASP 27 ? CG  ? C ASP 28 CG  
34 1 Y 1 C ASP 27 ? OD1 ? C ASP 28 OD1 
35 1 Y 1 C ASP 27 ? OD2 ? C ASP 28 OD2 
36 1 Y 1 C ILE 28 ? CG1 ? C ILE 29 CG1 
37 1 Y 1 C ILE 28 ? CG2 ? C ILE 29 CG2 
38 1 Y 1 C ILE 28 ? CD1 ? C ILE 29 CD1 
39 1 Y 1 C LYS 34 ? CG  ? C LYS 35 CG  
40 1 Y 1 C LYS 34 ? CD  ? C LYS 35 CD  
41 1 Y 1 C LYS 34 ? CE  ? C LYS 35 CE  
42 1 Y 1 C LYS 34 ? NZ  ? C LYS 35 NZ  
43 1 Y 1 C LYS 56 ? CG  ? C LYS 57 CG  
44 1 Y 1 C LYS 56 ? CD  ? C LYS 57 CD  
45 1 Y 1 C LYS 56 ? CE  ? C LYS 57 CE  
46 1 Y 1 C LYS 56 ? NZ  ? C LYS 57 NZ  
47 1 Y 1 C LYS 63 ? CG  ? C LYS 64 CG  
48 1 Y 1 C LYS 63 ? CD  ? C LYS 64 CD  
49 1 Y 1 C LYS 63 ? CE  ? C LYS 64 CE  
50 1 Y 1 C LYS 63 ? NZ  ? C LYS 64 NZ  
51 1 Y 1 C LYS 70 ? NZ  ? C LYS 71 NZ  
52 1 Y 1 C LYS 73 ? CG  ? C LYS 74 CG  
53 1 Y 1 C LYS 73 ? CD  ? C LYS 74 CD  
54 1 Y 1 C LYS 73 ? CE  ? C LYS 74 CE  
55 1 Y 1 C LYS 73 ? NZ  ? C LYS 74 NZ  
56 1 Y 1 C LYS 75 ? CE  ? C LYS 76 CE  
57 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           7HGV 
_cell.length_a           41.740 
_cell.length_b           42.190 
_cell.length_c           159.610 
_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                         7HGV 
_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          7HGV 
_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                     7HGV 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             42.19 
_reflns.d_resolution_high            1.48 
_reflns.number_obs                   48131 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.053 
_reflns.pdbx_netI_over_sigmaI        13.4 
_reflns.pdbx_redundancy              6.0 
_reflns.pdbx_Rrim_I_all              0.057 
_reflns.pdbx_Rpim_I_all              0.023 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     288329 
_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                  1.48 
_reflns_shell.d_res_low                   1.52 
_reflns_shell.number_measured_all         15621 
_reflns_shell.number_unique_obs           3506 
_reflns_shell.Rmerge_I_obs                1.669 
_reflns_shell.pdbx_chi_squared            0.78 
_reflns_shell.pdbx_redundancy             4.5 
_reflns_shell.percent_possible_obs        100.0 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.8 
_reflns_shell.pdbx_Rrim_I_all             1.894 
_reflns_shell.pdbx_Rpim_I_all             0.884 
_reflns_shell.pdbx_CC_half                0.361 
_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                                 7HGV 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     45503 
_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                             40.82 
_refine.ls_d_res_high                            1.48 
_refine.ls_percent_reflns_obs                    99.92 
_refine.ls_R_factor_obs                          0.20398 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.20215 
_refine.ls_R_factor_R_free                       0.23656 
_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                  2548 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.968 
_refine.correlation_coeff_Fo_to_Fc_free          0.960 
_refine.B_iso_mean                               36.203 
_refine.aniso_B[1][1]                            0.67 
_refine.aniso_B[2][2]                            -0.34 
_refine.aniso_B[3][3]                            -0.33 
_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                       0.081 
_refine.pdbx_overall_ESU_R_Free                  0.083 
_refine.overall_SU_ML                            0.074 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             2.082 
_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        2138 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         67 
_refine_hist.number_atoms_solvent             277 
_refine_hist.number_atoms_total               2482 
_refine_hist.d_res_high                       1.48 
_refine_hist.d_res_low                        40.82 
# 
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  ? 2299 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          2.000  1.839  ? 3125 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       7.909  5.000  ? 264  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       5.578  5.000  ? 6    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       12.838 10.000 ? 305  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.146  0.200  ? 294  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.011  0.020  ? 1854 '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                  3.191  3.323  ? 1068 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 4.467  5.947  ? 1331 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  4.454  3.663  ? 1231 'X-RAY DIFFRACTION' ? 
r_scbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       8.961  49.65  ? 3609 '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                       1.480 
_refine_ls_shell.d_res_low                        1.518 
_refine_ls_shell.number_reflns_R_work             3318 
_refine_ls_shell.R_factor_R_work                  0.351 
_refine_ls_shell.percent_reflns_obs               99.86 
_refine_ls_shell.R_factor_R_free                  0.352 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             178 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HGV 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of HRP-2 PWWP domain in complex with Z103740620' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HGV 
_struct_keywords.pdbx_keywords   'GENE REGULATION' 
_struct_keywords.text            
'Inhibitor, Fragment screening, Epigenetic reader, methyllysine, PWWP, Diamond Light Source, I04-1, PanDDA, XChem, GENE REGULATION' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 2 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 2 ? 
I N N 2 ? 
J N N 2 ? 
K N N 4 ? 
L N N 2 ? 
M N N 4 ? 
N N N 5 ? 
O N N 5 ? 
P N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    HDGR2_HUMAN 
_struct_ref.pdbx_db_accession          Q7Z4V5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKCKDKYGKPNKRKGFNEG
LWEIQNNPHASYS
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HGV A 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 7HGV B 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
3 1 7HGV 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 7HGV GLY A 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  1 
1 7HGV SER A 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 2 
2 7HGV GLY B 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  3 
2 7HGV SER B 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 4 
3 7HGV GLY C 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  5 
3 7HGV SER C 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 6 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
3 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,D,E,F,G,H,N 
2 1 B,I,J,K,O     
3 1 C,L,M,P       
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 55 ? LYS A 57 ? GLY A 54 LYS A 56 5 ? 3  
HELX_P HELX_P2 AA2 TYR A 62 ? GLY A 70 ? TYR A 61 GLY A 69 1 ? 9  
HELX_P HELX_P3 AA3 GLY A 77 ? ASN A 88 ? GLY A 76 ASN A 87 1 ? 12 
HELX_P HELX_P4 AA4 GLY B 55 ? LYS B 57 ? GLY B 54 LYS B 56 5 ? 3  
HELX_P HELX_P5 AA5 TYR B 62 ? GLY B 70 ? TYR B 61 GLY B 69 1 ? 9  
HELX_P HELX_P6 AA6 GLY B 77 ? ASN B 88 ? GLY B 76 ASN B 87 1 ? 12 
HELX_P HELX_P7 AA7 GLY C 55 ? LYS C 57 ? GLY C 54 LYS C 56 5 ? 3  
HELX_P HELX_P8 AA8 TYR C 62 ? GLY C 70 ? TYR C 61 GLY C 69 1 ? 9  
HELX_P HELX_P9 AA9 GLY C 77 ? ASN C 88 ? GLY C 76 ASN C 87 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 5 ? 
AA3 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 51 ? LEU A 54 ? THR A 50 LEU A 53 
AA1 2 TYR A 41 ? PHE A 45 ? TYR A 40 PHE A 44 
AA1 3 TRP A 22 ? ILE A 26 ? TRP A 21 ILE A 25 
AA1 4 LEU A 11 ? ALA A 14 ? LEU A 10 ALA A 13 
AA1 5 LEU A 59 ? PRO A 61 ? LEU A 58 PRO A 60 
AA2 1 THR B 51 ? LEU B 54 ? THR B 50 LEU B 53 
AA2 2 TYR B 41 ? PHE B 45 ? TYR B 40 PHE B 44 
AA2 3 TRP B 22 ? ILE B 26 ? TRP B 21 ILE B 25 
AA2 4 LEU B 11 ? ALA B 14 ? LEU B 10 ALA B 13 
AA2 5 LEU B 59 ? PRO B 61 ? LEU B 58 PRO B 60 
AA3 1 THR C 51 ? LEU C 54 ? THR C 50 LEU C 53 
AA3 2 TYR C 41 ? PHE C 45 ? TYR C 40 PHE C 44 
AA3 3 TRP C 22 ? ILE C 26 ? TRP C 21 ILE C 25 
AA3 4 LEU C 11 ? ALA C 14 ? LEU C 10 ALA C 13 
AA3 5 LEU C 59 ? PRO C 61 ? LEU C 58 PRO C 60 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ALA A 52 ? O ALA A 51 N ILE A 43 ? N ILE A 42 
AA1 2 3 O PHE A 44 ? O PHE A 43 N ARG A 25 ? N ARG A 24 
AA1 3 4 O ALA A 24 ? O ALA A 23 N VAL A 12 ? N VAL A 11 
AA1 4 5 N PHE A 13 ? N PHE A 12 O PHE A 60 ? O PHE A 59 
AA2 1 2 O ALA B 52 ? O ALA B 51 N ILE B 43 ? N ILE B 42 
AA2 2 3 O PHE B 44 ? O PHE B 43 N ARG B 25 ? N ARG B 24 
AA2 3 4 O TRP B 22 ? O TRP B 21 N ALA B 14 ? N ALA B 13 
AA2 4 5 N PHE B 13 ? N PHE B 12 O PHE B 60 ? O PHE B 59 
AA3 1 2 O LEU C 54 ? O LEU C 53 N TYR C 41 ? N TYR C 40 
AA3 2 3 O PHE C 44 ? O PHE C 43 N ARG C 25 ? N ARG C 24 
AA3 3 4 O 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                   7HGV 
_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   220 ? ? O B HOH 272 ? ? 1.41 
2 1 OE2 B GLU   83  ? ? O B HOH 201 ? ? 1.44 
3 1 NE2 B HIS   48  ? ? O B HOH 201 ? ? 1.57 
4 1 O   C HOH   226 ? ? O C HOH 264 ? ? 1.70 
5 1 O   A A1A33 104 ? ? O A HOH 201 ? ? 1.79 
6 1 OH  A TYR   18  ? ? O A HOH 202 ? ? 2.01 
7 1 O   A HOH   207 ? ? O A HOH 289 ? ? 2.08 
8 1 CD  B GLU   83  ? ? O B HOH 201 ? ? 2.11 
9 1 O4  A SO4   105 ? ? O A HOH 203 ? ? 2.19 
# 
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 294 ? ? 1_555 O C HOH 269 ? ? 4_445 1.86 
2 1 O A HOH 262 ? ? 1_555 O A HOH 275 ? ? 4_545 2.10 
# 
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 ? ? -155.02 66.65  
2 1 ASN B 38 ? ? 76.20   -0.22  
3 1 ASN B 87 ? ? -157.65 60.97  
4 1 ALA C 4  ? ? -168.86 108.54 
5 1 ASN C 87 ? ? -149.97 48.98  
6 1 SER C 91 ? ? -76.05  -71.81 
# 
_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            149.88 
# 
loop_
_pdbx_validate_chiral.id 
_pdbx_validate_chiral.PDB_model_num 
_pdbx_validate_chiral.auth_atom_id 
_pdbx_validate_chiral.label_alt_id 
_pdbx_validate_chiral.auth_asym_id 
_pdbx_validate_chiral.auth_comp_id 
_pdbx_validate_chiral.auth_seq_id 
_pdbx_validate_chiral.PDB_ins_code 
_pdbx_validate_chiral.details 
_pdbx_validate_chiral.omega 
1 1 C6 ? B A1A33 103 ? 'WRONG HAND' . 
2 1 C6 ? C A1A33 102 ? 'WRONG HAND' . 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       310 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.97 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 0  ? A GLY 1  
2  1 Y 1 B GLY 0  ? B GLY 1  
3  1 Y 1 B 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 
A1A33 C4   C N N 1   
A1A33 C5   C N N 2   
A1A33 C6   C N R 3   
A1A33 C7   C N N 4   
A1A33 C8   C N N 5   
A1A33 O    O N N 6   
A1A33 C3   C N N 7   
A1A33 N    N N N 8   
A1A33 C1   C N N 9   
A1A33 C2   C N N 10  
A1A33 C    C N N 11  
A1A33 H9   H N N 12  
A1A33 H10  H N N 13  
A1A33 H11  H N N 14  
A1A33 H12  H N N 15  
A1A33 H13  H N N 16  
A1A33 H15  H N N 17  
A1A33 H14  H N N 18  
A1A33 H18  H N N 19  
A1A33 H17  H N N 20  
A1A33 H16  H N N 21  
A1A33 H7   H N N 22  
A1A33 H8   H N N 23  
A1A33 H3   H N N 24  
A1A33 H6   H N N 25  
A1A33 H5   H N N 26  
A1A33 H4   H N N 27  
A1A33 H2   H N N 28  
A1A33 H    H N N 29  
A1A33 H1   H N N 30  
ALA   N    N N N 31  
ALA   CA   C N S 32  
ALA   C    C N N 33  
ALA   O    O N N 34  
ALA   CB   C N N 35  
ALA   OXT  O N N 36  
ALA   H    H N N 37  
ALA   H2   H N N 38  
ALA   HA   H N N 39  
ALA   HB1  H N N 40  
ALA   HB2  H N N 41  
ALA   HB3  H N N 42  
ALA   HXT  H N N 43  
ARG   N    N N N 44  
ARG   CA   C N S 45  
ARG   C    C N N 46  
ARG   O    O N N 47  
ARG   CB   C N N 48  
ARG   CG   C N N 49  
ARG   CD   C N N 50  
ARG   NE   N N N 51  
ARG   CZ   C N N 52  
ARG   NH1  N N N 53  
ARG   NH2  N N N 54  
ARG   OXT  O N N 55  
ARG   H    H N N 56  
ARG   H2   H N N 57  
ARG   HA   H N N 58  
ARG   HB2  H N N 59  
ARG   HB3  H N N 60  
ARG   HG2  H N N 61  
ARG   HG3  H N N 62  
ARG   HD2  H N N 63  
ARG   HD3  H N N 64  
ARG   HE   H N N 65  
ARG   HH11 H N N 66  
ARG   HH12 H N N 67  
ARG   HH21 H N N 68  
ARG   HH22 H N N 69  
ARG   HXT  H N N 70  
ASN   N    N N N 71  
ASN   CA   C N S 72  
ASN   C    C N N 73  
ASN   O    O N N 74  
ASN   CB   C N N 75  
ASN   CG   C N N 76  
ASN   OD1  O N N 77  
ASN   ND2  N N N 78  
ASN   OXT  O N N 79  
ASN   H    H N N 80  
ASN   H2   H N N 81  
ASN   HA   H N N 82  
ASN   HB2  H N N 83  
ASN   HB3  H N N 84  
ASN   HD21 H N N 85  
ASN   HD22 H N N 86  
ASN   HXT  H N N 87  
ASP   N    N N N 88  
ASP   CA   C N S 89  
ASP   C    C N N 90  
ASP   O    O N N 91  
ASP   CB   C N N 92  
ASP   CG   C N N 93  
ASP   OD1  O N N 94  
ASP   OD2  O N N 95  
ASP   OXT  O N N 96  
ASP   H    H N N 97  
ASP   H2   H N N 98  
ASP   HA   H N N 99  
ASP   HB2  H N N 100 
ASP   HB3  H N N 101 
ASP   HD2  H N N 102 
ASP   HXT  H N N 103 
CYS   N    N N N 104 
CYS   CA   C N R 105 
CYS   C    C N N 106 
CYS   O    O N N 107 
CYS   CB   C N N 108 
CYS   SG   S N N 109 
CYS   OXT  O N N 110 
CYS   H    H N N 111 
CYS   H2   H N N 112 
CYS   HA   H N N 113 
CYS   HB2  H N N 114 
CYS   HB3  H N N 115 
CYS   HG   H N N 116 
CYS   HXT  H N N 117 
EDO   C1   C N N 118 
EDO   O1   O N N 119 
EDO   C2   C N N 120 
EDO   O2   O N N 121 
EDO   H11  H N N 122 
EDO   H12  H N N 123 
EDO   HO1  H N N 124 
EDO   H21  H N N 125 
EDO   H22  H N N 126 
EDO   HO2  H N N 127 
GLN   N    N N N 128 
GLN   CA   C N S 129 
GLN   C    C N N 130 
GLN   O    O N N 131 
GLN   CB   C N N 132 
GLN   CG   C N N 133 
GLN   CD   C N N 134 
GLN   OE1  O N N 135 
GLN   NE2  N N N 136 
GLN   OXT  O N N 137 
GLN   H    H N N 138 
GLN   H2   H N N 139 
GLN   HA   H N N 140 
GLN   HB2  H N N 141 
GLN   HB3  H N N 142 
GLN   HG2  H N N 143 
GLN   HG3  H N N 144 
GLN   HE21 H N N 145 
GLN   HE22 H N N 146 
GLN   HXT  H N N 147 
GLU   N    N N N 148 
GLU   CA   C N S 149 
GLU   C    C N N 150 
GLU   O    O N N 151 
GLU   CB   C N N 152 
GLU   CG   C N N 153 
GLU   CD   C N N 154 
GLU   OE1  O N N 155 
GLU   OE2  O N N 156 
GLU   OXT  O N N 157 
GLU   H    H N N 158 
GLU   H2   H N N 159 
GLU   HA   H N N 160 
GLU   HB2  H N N 161 
GLU   HB3  H N N 162 
GLU   HG2  H N N 163 
GLU   HG3  H N N 164 
GLU   HE2  H N N 165 
GLU   HXT  H N N 166 
GLY   N    N N N 167 
GLY   CA   C N N 168 
GLY   C    C N N 169 
GLY   O    O N N 170 
GLY   OXT  O N N 171 
GLY   H    H N N 172 
GLY   H2   H N N 173 
GLY   HA2  H N N 174 
GLY   HA3  H N N 175 
GLY   HXT  H N N 176 
HIS   N    N N N 177 
HIS   CA   C N S 178 
HIS   C    C N N 179 
HIS   O    O N N 180 
HIS   CB   C N N 181 
HIS   CG   C Y N 182 
HIS   ND1  N Y N 183 
HIS   CD2  C Y N 184 
HIS   CE1  C Y N 185 
HIS   NE2  N Y N 186 
HIS   OXT  O N N 187 
HIS   H    H N N 188 
HIS   H2   H N N 189 
HIS   HA   H N N 190 
HIS   HB2  H N N 191 
HIS   HB3  H N N 192 
HIS   HD1  H N N 193 
HIS   HD2  H N N 194 
HIS   HE1  H N N 195 
HIS   HE2  H N N 196 
HIS   HXT  H N N 197 
HOH   O    O N N 198 
HOH   H1   H N N 199 
HOH   H2   H N N 200 
ILE   N    N N N 201 
ILE   CA   C N S 202 
ILE   C    C N N 203 
ILE   O    O N N 204 
ILE   CB   C N S 205 
ILE   CG1  C N N 206 
ILE   CG2  C N N 207 
ILE   CD1  C N N 208 
ILE   OXT  O N N 209 
ILE   H    H N N 210 
ILE   H2   H N N 211 
ILE   HA   H N N 212 
ILE   HB   H N N 213 
ILE   HG12 H N N 214 
ILE   HG13 H N N 215 
ILE   HG21 H N N 216 
ILE   HG22 H N N 217 
ILE   HG23 H N N 218 
ILE   HD11 H N N 219 
ILE   HD12 H N N 220 
ILE   HD13 H N N 221 
ILE   HXT  H N N 222 
LEU   N    N N N 223 
LEU   CA   C N S 224 
LEU   C    C N N 225 
LEU   O    O N N 226 
LEU   CB   C N N 227 
LEU   CG   C N N 228 
LEU   CD1  C N N 229 
LEU   CD2  C N N 230 
LEU   OXT  O N N 231 
LEU   H    H N N 232 
LEU   H2   H N N 233 
LEU   HA   H N N 234 
LEU   HB2  H N N 235 
LEU   HB3  H N N 236 
LEU   HG   H N N 237 
LEU   HD11 H N N 238 
LEU   HD12 H N N 239 
LEU   HD13 H N N 240 
LEU   HD21 H N N 241 
LEU   HD22 H N N 242 
LEU   HD23 H N N 243 
LEU   HXT  H N N 244 
LYS   N    N N N 245 
LYS   CA   C N S 246 
LYS   C    C N N 247 
LYS   O    O N N 248 
LYS   CB   C N N 249 
LYS   CG   C N N 250 
LYS   CD   C N N 251 
LYS   CE   C N N 252 
LYS   NZ   N N N 253 
LYS   OXT  O N N 254 
LYS   H    H N N 255 
LYS   H2   H N N 256 
LYS   HA   H N N 257 
LYS   HB2  H N N 258 
LYS   HB3  H N N 259 
LYS   HG2  H N N 260 
LYS   HG3  H N N 261 
LYS   HD2  H N N 262 
LYS   HD3  H N N 263 
LYS   HE2  H N N 264 
LYS   HE3  H N N 265 
LYS   HZ1  H N N 266 
LYS   HZ2  H N N 267 
LYS   HZ3  H N N 268 
LYS   HXT  H N N 269 
MET   N    N N N 270 
MET   CA   C N S 271 
MET   C    C N N 272 
MET   O    O N N 273 
MET   CB   C N N 274 
MET   CG   C N N 275 
MET   SD   S N N 276 
MET   CE   C N N 277 
MET   OXT  O N N 278 
MET   H    H N N 279 
MET   H2   H N N 280 
MET   HA   H N N 281 
MET   HB2  H N N 282 
MET   HB3  H N N 283 
MET   HG2  H N N 284 
MET   HG3  H N N 285 
MET   HE1  H N N 286 
MET   HE2  H N N 287 
MET   HE3  H N N 288 
MET   HXT  H N N 289 
PHE   N    N N N 290 
PHE   CA   C N S 291 
PHE   C    C N N 292 
PHE   O    O N N 293 
PHE   CB   C N N 294 
PHE   CG   C Y N 295 
PHE   CD1  C Y N 296 
PHE   CD2  C Y N 297 
PHE   CE1  C Y N 298 
PHE   CE2  C Y N 299 
PHE   CZ   C Y N 300 
PHE   OXT  O N N 301 
PHE   H    H N N 302 
PHE   H2   H N N 303 
PHE   HA   H N N 304 
PHE   HB2  H N N 305 
PHE   HB3  H N N 306 
PHE   HD1  H N N 307 
PHE   HD2  H N N 308 
PHE   HE1  H N N 309 
PHE   HE2  H N N 310 
PHE   HZ   H N N 311 
PHE   HXT  H N N 312 
PRO   N    N N N 313 
PRO   CA   C N S 314 
PRO   C    C N N 315 
PRO   O    O N N 316 
PRO   CB   C N N 317 
PRO   CG   C N N 318 
PRO   CD   C N N 319 
PRO   OXT  O N N 320 
PRO   H    H N N 321 
PRO   HA   H N N 322 
PRO   HB2  H N N 323 
PRO   HB3  H N N 324 
PRO   HG2  H N N 325 
PRO   HG3  H N N 326 
PRO   HD2  H N N 327 
PRO   HD3  H N N 328 
PRO   HXT  H N N 329 
SER   N    N N N 330 
SER   CA   C N S 331 
SER   C    C N N 332 
SER   O    O N N 333 
SER   CB   C N N 334 
SER   OG   O N N 335 
SER   OXT  O N N 336 
SER   H    H N N 337 
SER   H2   H N N 338 
SER   HA   H N N 339 
SER   HB2  H N N 340 
SER   HB3  H N N 341 
SER   HG   H N N 342 
SER   HXT  H N N 343 
SO4   S    S N N 344 
SO4   O1   O N N 345 
SO4   O2   O N N 346 
SO4   O3   O N N 347 
SO4   O4   O N N 348 
THR   N    N N N 349 
THR   CA   C N S 350 
THR   C    C N N 351 
THR   O    O N N 352 
THR   CB   C N R 353 
THR   OG1  O N N 354 
THR   CG2  C N N 355 
THR   OXT  O N N 356 
THR   H    H N N 357 
THR   H2   H N N 358 
THR   HA   H N N 359 
THR   HB   H N N 360 
THR   HG1  H N N 361 
THR   HG21 H N N 362 
THR   HG22 H N N 363 
THR   HG23 H N N 364 
THR   HXT  H N N 365 
TRP   N    N N N 366 
TRP   CA   C N S 367 
TRP   C    C N N 368 
TRP   O    O N N 369 
TRP   CB   C N N 370 
TRP   CG   C Y N 371 
TRP   CD1  C Y N 372 
TRP   CD2  C Y N 373 
TRP   NE1  N Y N 374 
TRP   CE2  C Y N 375 
TRP   CE3  C Y N 376 
TRP   CZ2  C Y N 377 
TRP   CZ3  C Y N 378 
TRP   CH2  C Y N 379 
TRP   OXT  O N N 380 
TRP   H    H N N 381 
TRP   H2   H N N 382 
TRP   HA   H N N 383 
TRP   HB2  H N N 384 
TRP   HB3  H N N 385 
TRP   HD1  H N N 386 
TRP   HE1  H N N 387 
TRP   HE3  H N N 388 
TRP   HZ2  H N N 389 
TRP   HZ3  H N N 390 
TRP   HH2  H N N 391 
TRP   HXT  H N N 392 
TYR   N    N N N 393 
TYR   CA   C N S 394 
TYR   C    C N N 395 
TYR   O    O N N 396 
TYR   CB   C N N 397 
TYR   CG   C Y N 398 
TYR   CD1  C Y N 399 
TYR   CD2  C Y N 400 
TYR   CE1  C Y N 401 
TYR   CE2  C Y N 402 
TYR   CZ   C Y N 403 
TYR   OH   O N N 404 
TYR   OXT  O N N 405 
TYR   H    H N N 406 
TYR   H2   H N N 407 
TYR   HA   H N N 408 
TYR   HB2  H N N 409 
TYR   HB3  H N N 410 
TYR   HD1  H N N 411 
TYR   HD2  H N N 412 
TYR   HE1  H N N 413 
TYR   HE2  H N N 414 
TYR   HH   H N N 415 
TYR   HXT  H N N 416 
VAL   N    N N N 417 
VAL   CA   C N S 418 
VAL   C    C N N 419 
VAL   O    O N N 420 
VAL   CB   C N N 421 
VAL   CG1  C N N 422 
VAL   CG2  C N N 423 
VAL   OXT  O N N 424 
VAL   H    H N N 425 
VAL   H2   H N N 426 
VAL   HA   H N N 427 
VAL   HB   H N N 428 
VAL   HG11 H N N 429 
VAL   HG12 H N N 430 
VAL   HG13 H N N 431 
VAL   HG21 H N N 432 
VAL   HG22 H N N 433 
VAL   HG23 H N N 434 
VAL   HXT  H N N 435 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1A33 C   C1   sing N N 1   
A1A33 C2  C1   sing N N 2   
A1A33 C1  N    sing N N 3   
A1A33 N   C3   sing N N 4   
A1A33 C3  C4   sing N N 5   
A1A33 C4  C5   sing N N 6   
A1A33 C5  C6   sing N N 7   
A1A33 C6  C7   sing N N 8   
A1A33 C7  O    sing N N 9   
A1A33 C8  C6   sing N N 10  
A1A33 N   C8   sing N N 11  
A1A33 C4  H9   sing N N 12  
A1A33 C4  H10  sing N N 13  
A1A33 C5  H11  sing N N 14  
A1A33 C5  H12  sing N N 15  
A1A33 C6  H13  sing N N 16  
A1A33 C7  H15  sing N N 17  
A1A33 C7  H14  sing N N 18  
A1A33 C8  H18  sing N N 19  
A1A33 C8  H17  sing N N 20  
A1A33 O   H16  sing N N 21  
A1A33 C3  H7   sing N N 22  
A1A33 C3  H8   sing N N 23  
A1A33 C1  H3   sing N N 24  
A1A33 C2  H6   sing N N 25  
A1A33 C2  H5   sing N N 26  
A1A33 C2  H4   sing N N 27  
A1A33 C   H2   sing N N 28  
A1A33 C   H    sing N N 29  
A1A33 C   H1   sing N N 30  
ALA   N   CA   sing N N 31  
ALA   N   H    sing N N 32  
ALA   N   H2   sing N N 33  
ALA   CA  C    sing N N 34  
ALA   CA  CB   sing N N 35  
ALA   CA  HA   sing N N 36  
ALA   C   O    doub N N 37  
ALA   C   OXT  sing N N 38  
ALA   CB  HB1  sing N N 39  
ALA   CB  HB2  sing N N 40  
ALA   CB  HB3  sing N N 41  
ALA   OXT HXT  sing N N 42  
ARG   N   CA   sing N N 43  
ARG   N   H    sing N N 44  
ARG   N   H2   sing N N 45  
ARG   CA  C    sing N N 46  
ARG   CA  CB   sing N N 47  
ARG   CA  HA   sing N N 48  
ARG   C   O    doub N N 49  
ARG   C   OXT  sing N N 50  
ARG   CB  CG   sing N N 51  
ARG   CB  HB2  sing N N 52  
ARG   CB  HB3  sing N N 53  
ARG   CG  CD   sing N N 54  
ARG   CG  HG2  sing N N 55  
ARG   CG  HG3  sing N N 56  
ARG   CD  NE   sing N N 57  
ARG   CD  HD2  sing N N 58  
ARG   CD  HD3  sing N N 59  
ARG   NE  CZ   sing N N 60  
ARG   NE  HE   sing N N 61  
ARG   CZ  NH1  sing N N 62  
ARG   CZ  NH2  doub N N 63  
ARG   NH1 HH11 sing N N 64  
ARG   NH1 HH12 sing N N 65  
ARG   NH2 HH21 sing N N 66  
ARG   NH2 HH22 sing N N 67  
ARG   OXT HXT  sing N N 68  
ASN   N   CA   sing N N 69  
ASN   N   H    sing N N 70  
ASN   N   H2   sing N N 71  
ASN   CA  C    sing N N 72  
ASN   CA  CB   sing N N 73  
ASN   CA  HA   sing N N 74  
ASN   C   O    doub N N 75  
ASN   C   OXT  sing N N 76  
ASN   CB  CG   sing N N 77  
ASN   CB  HB2  sing N N 78  
ASN   CB  HB3  sing N N 79  
ASN   CG  OD1  doub N N 80  
ASN   CG  ND2  sing N N 81  
ASN   ND2 HD21 sing N N 82  
ASN   ND2 HD22 sing N N 83  
ASN   OXT HXT  sing N N 84  
ASP   N   CA   sing N N 85  
ASP   N   H    sing N N 86  
ASP   N   H2   sing N N 87  
ASP   CA  C    sing N N 88  
ASP   CA  CB   sing N N 89  
ASP   CA  HA   sing N N 90  
ASP   C   O    doub N N 91  
ASP   C   OXT  sing N N 92  
ASP   CB  CG   sing N N 93  
ASP   CB  HB2  sing N N 94  
ASP   CB  HB3  sing N N 95  
ASP   CG  OD1  doub N N 96  
ASP   CG  OD2  sing N N 97  
ASP   OD2 HD2  sing N N 98  
ASP   OXT HXT  sing N N 99  
CYS   N   CA   sing N N 100 
CYS   N   H    sing N N 101 
CYS   N   H2   sing N N 102 
CYS   CA  C    sing N N 103 
CYS   CA  CB   sing N N 104 
CYS   CA  HA   sing N N 105 
CYS   C   O    doub N N 106 
CYS   C   OXT  sing N N 107 
CYS   CB  SG   sing N N 108 
CYS   CB  HB2  sing N N 109 
CYS   CB  HB3  sing N N 110 
CYS   SG  HG   sing N N 111 
CYS   OXT HXT  sing N N 112 
EDO   C1  O1   sing N N 113 
EDO   C1  C2   sing N N 114 
EDO   C1  H11  sing N N 115 
EDO   C1  H12  sing N N 116 
EDO   O1  HO1  sing N N 117 
EDO   C2  O2   sing N N 118 
EDO   C2  H21  sing N N 119 
EDO   C2  H22  sing N N 120 
EDO   O2  HO2  sing N N 121 
GLN   N   CA   sing N N 122 
GLN   N   H    sing N N 123 
GLN   N   H2   sing N N 124 
GLN   CA  C    sing N N 125 
GLN   CA  CB   sing N N 126 
GLN   CA  HA   sing N N 127 
GLN   C   O    doub N N 128 
GLN   C   OXT  sing N N 129 
GLN   CB  CG   sing N N 130 
GLN   CB  HB2  sing N N 131 
GLN   CB  HB3  sing N N 132 
GLN   CG  CD   sing N N 133 
GLN   CG  HG2  sing N N 134 
GLN   CG  HG3  sing N N 135 
GLN   CD  OE1  doub N N 136 
GLN   CD  NE2  sing N N 137 
GLN   NE2 HE21 sing N N 138 
GLN   NE2 HE22 sing N N 139 
GLN   OXT HXT  sing N N 140 
GLU   N   CA   sing N N 141 
GLU   N   H    sing N N 142 
GLU   N   H2   sing N N 143 
GLU   CA  C    sing N N 144 
GLU   CA  CB   sing N N 145 
GLU   CA  HA   sing N N 146 
GLU   C   O    doub N N 147 
GLU   C   OXT  sing N N 148 
GLU   CB  CG   sing N N 149 
GLU   CB  HB2  sing N N 150 
GLU   CB  HB3  sing N N 151 
GLU   CG  CD   sing N N 152 
GLU   CG  HG2  sing N N 153 
GLU   CG  HG3  sing N N 154 
GLU   CD  OE1  doub N N 155 
GLU   CD  OE2  sing N N 156 
GLU   OE2 HE2  sing N N 157 
GLU   OXT HXT  sing N N 158 
GLY   N   CA   sing N N 159 
GLY   N   H    sing N N 160 
GLY   N   H2   sing N N 161 
GLY   CA  C    sing N N 162 
GLY   CA  HA2  sing N N 163 
GLY   CA  HA3  sing N N 164 
GLY   C   O    doub N N 165 
GLY   C   OXT  sing N N 166 
GLY   OXT HXT  sing N N 167 
HIS   N   CA   sing N N 168 
HIS   N   H    sing N N 169 
HIS   N   H2   sing N N 170 
HIS   CA  C    sing N N 171 
HIS   CA  CB   sing N N 172 
HIS   CA  HA   sing N N 173 
HIS   C   O    doub N N 174 
HIS   C   OXT  sing N N 175 
HIS   CB  CG   sing N N 176 
HIS   CB  HB2  sing N N 177 
HIS   CB  HB3  sing N N 178 
HIS   CG  ND1  sing Y N 179 
HIS   CG  CD2  doub Y N 180 
HIS   ND1 CE1  doub Y N 181 
HIS   ND1 HD1  sing N N 182 
HIS   CD2 NE2  sing Y N 183 
HIS   CD2 HD2  sing N N 184 
HIS   CE1 NE2  sing Y N 185 
HIS   CE1 HE1  sing N N 186 
HIS   NE2 HE2  sing N N 187 
HIS   OXT HXT  sing N N 188 
HOH   O   H1   sing N N 189 
HOH   O   H2   sing N N 190 
ILE   N   CA   sing N N 191 
ILE   N   H    sing N N 192 
ILE   N   H2   sing N N 193 
ILE   CA  C    sing N N 194 
ILE   CA  CB   sing N N 195 
ILE   CA  HA   sing N N 196 
ILE   C   O    doub N N 197 
ILE   C   OXT  sing N N 198 
ILE   CB  CG1  sing N N 199 
ILE   CB  CG2  sing N N 200 
ILE   CB  HB   sing N N 201 
ILE   CG1 CD1  sing N N 202 
ILE   CG1 HG12 sing N N 203 
ILE   CG1 HG13 sing N N 204 
ILE   CG2 HG21 sing N N 205 
ILE   CG2 HG22 sing N N 206 
ILE   CG2 HG23 sing N N 207 
ILE   CD1 HD11 sing N N 208 
ILE   CD1 HD12 sing N N 209 
ILE   CD1 HD13 sing N N 210 
ILE   OXT HXT  sing N N 211 
LEU   N   CA   sing N N 212 
LEU   N   H    sing N N 213 
LEU   N   H2   sing N N 214 
LEU   CA  C    sing N N 215 
LEU   CA  CB   sing N N 216 
LEU   CA  HA   sing N N 217 
LEU   C   O    doub N N 218 
LEU   C   OXT  sing N N 219 
LEU   CB  CG   sing N N 220 
LEU   CB  HB2  sing N N 221 
LEU   CB  HB3  sing N N 222 
LEU   CG  CD1  sing N N 223 
LEU   CG  CD2  sing N N 224 
LEU   CG  HG   sing N N 225 
LEU   CD1 HD11 sing N N 226 
LEU   CD1 HD12 sing N N 227 
LEU   CD1 HD13 sing N N 228 
LEU   CD2 HD21 sing N N 229 
LEU   CD2 HD22 sing N N 230 
LEU   CD2 HD23 sing N N 231 
LEU   OXT HXT  sing N N 232 
LYS   N   CA   sing N N 233 
LYS   N   H    sing N N 234 
LYS   N   H2   sing N N 235 
LYS   CA  C    sing N N 236 
LYS   CA  CB   sing N N 237 
LYS   CA  HA   sing N N 238 
LYS   C   O    doub N N 239 
LYS   C   OXT  sing N N 240 
LYS   CB  CG   sing N N 241 
LYS   CB  HB2  sing N N 242 
LYS   CB  HB3  sing N N 243 
LYS   CG  CD   sing N N 244 
LYS   CG  HG2  sing N N 245 
LYS   CG  HG3  sing N N 246 
LYS   CD  CE   sing N N 247 
LYS   CD  HD2  sing N N 248 
LYS   CD  HD3  sing N N 249 
LYS   CE  NZ   sing N N 250 
LYS   CE  HE2  sing N N 251 
LYS   CE  HE3  sing N N 252 
LYS   NZ  HZ1  sing N N 253 
LYS   NZ  HZ2  sing N N 254 
LYS   NZ  HZ3  sing N N 255 
LYS   OXT HXT  sing N N 256 
MET   N   CA   sing N N 257 
MET   N   H    sing N N 258 
MET   N   H2   sing N N 259 
MET   CA  C    sing N N 260 
MET   CA  CB   sing N N 261 
MET   CA  HA   sing N N 262 
MET   C   O    doub N N 263 
MET   C   OXT  sing N N 264 
MET   CB  CG   sing N N 265 
MET   CB  HB2  sing N N 266 
MET   CB  HB3  sing N N 267 
MET   CG  SD   sing N N 268 
MET   CG  HG2  sing N N 269 
MET   CG  HG3  sing N N 270 
MET   SD  CE   sing N N 271 
MET   CE  HE1  sing N N 272 
MET   CE  HE2  sing N N 273 
MET   CE  HE3  sing N N 274 
MET   OXT HXT  sing N N 275 
PHE   N   CA   sing N N 276 
PHE   N   H    sing N N 277 
PHE   N   H2   sing N N 278 
PHE   CA  C    sing N N 279 
PHE   CA  CB   sing N N 280 
PHE   CA  HA   sing N N 281 
PHE   C   O    doub N N 282 
PHE   C   OXT  sing N N 283 
PHE   CB  CG   sing N N 284 
PHE   CB  HB2  sing N N 285 
PHE   CB  HB3  sing N N 286 
PHE   CG  CD1  doub Y N 287 
PHE   CG  CD2  sing Y N 288 
PHE   CD1 CE1  sing Y N 289 
PHE   CD1 HD1  sing N N 290 
PHE   CD2 CE2  doub Y N 291 
PHE   CD2 HD2  sing N N 292 
PHE   CE1 CZ   doub Y N 293 
PHE   CE1 HE1  sing N N 294 
PHE   CE2 CZ   sing Y N 295 
PHE   CE2 HE2  sing N N 296 
PHE   CZ  HZ   sing N N 297 
PHE   OXT HXT  sing N N 298 
PRO   N   CA   sing N N 299 
PRO   N   CD   sing N N 300 
PRO   N   H    sing N N 301 
PRO   CA  C    sing N N 302 
PRO   CA  CB   sing N N 303 
PRO   CA  HA   sing N N 304 
PRO   C   O    doub N N 305 
PRO   C   OXT  sing N N 306 
PRO   CB  CG   sing N N 307 
PRO   CB  HB2  sing N N 308 
PRO   CB  HB3  sing N N 309 
PRO   CG  CD   sing N N 310 
PRO   CG  HG2  sing N N 311 
PRO   CG  HG3  sing N N 312 
PRO   CD  HD2  sing N N 313 
PRO   CD  HD3  sing N N 314 
PRO   OXT HXT  sing N N 315 
SER   N   CA   sing N N 316 
SER   N   H    sing N N 317 
SER   N   H2   sing N N 318 
SER   CA  C    sing N N 319 
SER   CA  CB   sing N N 320 
SER   CA  HA   sing N N 321 
SER   C   O    doub N N 322 
SER   C   OXT  sing N N 323 
SER   CB  OG   sing N N 324 
SER   CB  HB2  sing N N 325 
SER   CB  HB3  sing N N 326 
SER   OG  HG   sing N N 327 
SER   OXT HXT  sing N N 328 
SO4   S   O1   doub N N 329 
SO4   S   O2   doub N N 330 
SO4   S   O3   sing N N 331 
SO4   S   O4   sing N N 332 
THR   N   CA   sing N N 333 
THR   N   H    sing N N 334 
THR   N   H2   sing N N 335 
THR   CA  C    sing N N 336 
THR   CA  CB   sing N N 337 
THR   CA  HA   sing N N 338 
THR   C   O    doub N N 339 
THR   C   OXT  sing N N 340 
THR   CB  OG1  sing N N 341 
THR   CB  CG2  sing N N 342 
THR   CB  HB   sing N N 343 
THR   OG1 HG1  sing N N 344 
THR   CG2 HG21 sing N N 345 
THR   CG2 HG22 sing N N 346 
THR   CG2 HG23 sing N N 347 
THR   OXT HXT  sing N N 348 
TRP   N   CA   sing N N 349 
TRP   N   H    sing N N 350 
TRP   N   H2   sing N N 351 
TRP   CA  C    sing N N 352 
TRP   CA  CB   sing N N 353 
TRP   CA  HA   sing N N 354 
TRP   C   O    doub N N 355 
TRP   C   OXT  sing N N 356 
TRP   CB  CG   sing N N 357 
TRP   CB  HB2  sing N N 358 
TRP   CB  HB3  sing N N 359 
TRP   CG  CD1  doub Y N 360 
TRP   CG  CD2  sing Y N 361 
TRP   CD1 NE1  sing Y N 362 
TRP   CD1 HD1  sing N N 363 
TRP   CD2 CE2  doub Y N 364 
TRP   CD2 CE3  sing Y N 365 
TRP   NE1 CE2  sing Y N 366 
TRP   NE1 HE1  sing N N 367 
TRP   CE2 CZ2  sing Y N 368 
TRP   CE3 CZ3  doub Y N 369 
TRP   CE3 HE3  sing N N 370 
TRP   CZ2 CH2  doub Y N 371 
TRP   CZ2 HZ2  sing N N 372 
TRP   CZ3 CH2  sing Y N 373 
TRP   CZ3 HZ3  sing N N 374 
TRP   CH2 HH2  sing N N 375 
TRP   OXT HXT  sing N N 376 
TYR   N   CA   sing N N 377 
TYR   N   H    sing N N 378 
TYR   N   H2   sing N N 379 
TYR   CA  C    sing N N 380 
TYR   CA  CB   sing N N 381 
TYR   CA  HA   sing N N 382 
TYR   C   O    doub N N 383 
TYR   C   OXT  sing N N 384 
TYR   CB  CG   sing N N 385 
TYR   CB  HB2  sing N N 386 
TYR   CB  HB3  sing N N 387 
TYR   CG  CD1  doub Y N 388 
TYR   CG  CD2  sing Y N 389 
TYR   CD1 CE1  sing Y N 390 
TYR   CD1 HD1  sing N N 391 
TYR   CD2 CE2  doub Y N 392 
TYR   CD2 HD2  sing N N 393 
TYR   CE1 CZ   doub Y N 394 
TYR   CE1 HE1  sing N N 395 
TYR   CE2 CZ   sing Y N 396 
TYR   CE2 HE2  sing N N 397 
TYR   CZ  OH   sing N N 398 
TYR   OH  HH   sing N N 399 
TYR   OXT HXT  sing N N 400 
VAL   N   CA   sing N N 401 
VAL   N   H    sing N N 402 
VAL   N   H2   sing N N 403 
VAL   CA  C    sing N N 404 
VAL   CA  CB   sing N N 405 
VAL   CA  HA   sing N N 406 
VAL   C   O    doub N N 407 
VAL   C   OXT  sing N N 408 
VAL   CB  CG1  sing N N 409 
VAL   CB  CG2  sing N N 410 
VAL   CB  HB   sing N N 411 
VAL   CG1 HG11 sing N N 412 
VAL   CG1 HG12 sing N N 413 
VAL   CG1 HG13 sing N N 414 
VAL   CG2 HG21 sing N N 415 
VAL   CG2 HG22 sing N N 416 
VAL   CG2 HG23 sing N N 417 
VAL   OXT HXT  sing N N 418 
# 
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                    7HGV 
_atom_sites.fract_transf_matrix[1][1]   0.023958 
_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]   0.023702 
_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]   0.006265 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . MET   A 1 2  ? 0.846   4.336   2.325   1.00 48.96  ? 1   MET   A N   1 
ATOM   2    C CA  . MET   A 1 2  ? -0.212  3.510   1.687   1.00 51.41  ? 1   MET   A CA  1 
ATOM   3    C C   . MET   A 1 2  ? 0.426   2.456   0.790   1.00 50.23  ? 1   MET   A C   1 
ATOM   4    O O   . MET   A 1 2  ? 1.515   2.654   0.263   1.00 48.24  ? 1   MET   A O   1 
ATOM   5    C CB  . MET   A 1 2  ? -1.190  4.345   0.853   1.00 54.92  ? 1   MET   A CB  1 
ATOM   6    C CG  . MET   A 1 2  ? -2.200  5.143   1.667   1.00 59.92  ? 1   MET   A CG  1 
ATOM   7    S SD  . MET   A 1 2  ? -3.466  4.285   2.636   1.00 65.79  ? 1   MET   A SD  1 
ATOM   8    C CE  . MET   A 1 2  ? -3.754  5.608   3.823   1.00 61.56  ? 1   MET   A CE  1 
ATOM   9    N N   . PRO   A 1 3  ? -0.233  1.288   0.638   1.00 42.81  ? 2   PRO   A N   1 
ATOM   10   C CA  . PRO   A 1 3  ? 0.236   0.217   -0.249  1.00 42.98  ? 2   PRO   A CA  1 
ATOM   11   C C   . PRO   A 1 3  ? 0.448   0.584   -1.714  1.00 38.77  ? 2   PRO   A C   1 
ATOM   12   O O   . PRO   A 1 3  ? -0.263  1.406   -2.291  1.00 40.18  ? 2   PRO   A O   1 
ATOM   13   C CB  . PRO   A 1 3  ? -0.964  -0.776  -0.113  1.00 43.92  ? 2   PRO   A CB  1 
ATOM   14   C CG  . PRO   A 1 3  ? -1.418  -0.573  1.331   1.00 46.09  ? 2   PRO   A CG  1 
ATOM   15   C CD  . PRO   A 1 3  ? -1.471  0.935   1.365   1.00 44.29  ? 2   PRO   A CD  1 
ATOM   16   N N   . HIS   A 1 4  ? 1.388   -0.117  -2.343  1.00 35.64  ? 3   HIS   A N   1 
ATOM   17   C CA  . HIS   A 1 4  ? 1.542   0.032   -3.770  1.00 34.81  ? 3   HIS   A CA  1 
ATOM   18   C C   . HIS   A 1 4  ? 1.066   -1.286  -4.368  1.00 32.37  ? 3   HIS   A C   1 
ATOM   19   O O   . HIS   A 1 4  ? 0.653   -2.186  -3.636  1.00 32.76  ? 3   HIS   A O   1 
ATOM   20   C CB  . HIS   A 1 4  ? 3.017   0.300   -4.106  1.00 44.44  ? 3   HIS   A CB  1 
ATOM   21   C CG  . HIS   A 1 4  ? 3.544   1.625   -3.633  1.00 55.90  ? 3   HIS   A CG  1 
ATOM   22   N ND1 . HIS   A 1 4  ? 3.488   2.067   -2.327  1.00 63.70  ? 3   HIS   A ND1 1 
ATOM   23   C CD2 . HIS   A 1 4  ? 4.198   2.581   -4.308  1.00 64.38  ? 3   HIS   A CD2 1 
ATOM   24   C CE1 . HIS   A 1 4  ? 4.033   3.269   -2.237  1.00 62.61  ? 3   HIS   A CE1 1 
ATOM   25   N NE2 . HIS   A 1 4  ? 4.478   3.599   -3.429  1.00 60.55  ? 3   HIS   A NE2 1 
ATOM   26   N N   . ALA   A 1 5  ? 1.097   -1.415  -5.692  1.00 29.36  ? 4   ALA   A N   1 
ATOM   27   C CA  . ALA   A 1 5  ? 0.909   -2.712  -6.314  1.00 29.42  ? 4   ALA   A CA  1 
ATOM   28   C C   . ALA   A 1 5  ? 2.071   -3.644  -5.958  1.00 27.78  ? 4   ALA   A C   1 
ATOM   29   O O   . ALA   A 1 5  ? 3.145   -3.202  -5.534  1.00 28.26  ? 4   ALA   A O   1 
ATOM   30   C CB  . ALA   A 1 5  ? 0.761   -2.585  -7.822  1.00 33.25  ? 4   ALA   A CB  1 
ATOM   31   N N   . PHE   A 1 6  ? 1.784   -4.936  -6.053  1.00 26.28  ? 5   PHE   A N   1 
ATOM   32   C CA  . PHE   A 1 6  ? 2.788   -5.991  -5.908  1.00 27.03  ? 5   PHE   A CA  1 
ATOM   33   C C   . PHE   A 1 6  ? 3.924   -5.747  -6.899  1.00 27.36  ? 5   PHE   A C   1 
ATOM   34   O O   . PHE   A 1 6  ? 3.691   -5.289  -8.033  1.00 28.75  ? 5   PHE   A O   1 
ATOM   35   C CB  . PHE   A 1 6  ? 2.220   -7.421  -5.976  1.00 27.05  ? 5   PHE   A CB  1 
ATOM   36   C CG  . PHE   A 1 6  ? 1.437   -7.788  -4.715  1.00 26.81  ? 5   PHE   A CG  1 
ATOM   37   C CD1 . PHE   A 1 6  ? 2.086   -8.006  -3.495  1.00 25.87  ? 5   PHE   A CD1 1 
ATOM   38   C CD2 . PHE   A 1 6  ? 0.032   -7.897  -4.749  1.00 27.36  ? 5   PHE   A CD2 1 
ATOM   39   C CE1 . PHE   A 1 6  ? 1.389   -8.347  -2.335  1.00 26.37  ? 5   PHE   A CE1 1 
ATOM   40   C CE2 . PHE   A 1 6  ? -0.647  -8.283  -3.589  1.00 24.78  ? 5   PHE   A CE2 1 
ATOM   41   C CZ  . PHE   A 1 6  ? 0.006   -8.451  -2.399  1.00 26.13  ? 5   PHE   A CZ  1 
ATOM   42   N N   . LYS   A 1 7  ? 5.144   -6.042  -6.432  1.00 23.11  ? 6   LYS   A N   1 
ATOM   43   C CA  . LYS   A 1 7  ? 6.287   -5.977  -7.329  1.00 24.13  ? 6   LYS   A CA  1 
ATOM   44   C C   . LYS   A 1 7  ? 7.208   -7.159  -7.025  1.00 23.75  ? 6   LYS   A C   1 
ATOM   45   O O   . LYS   A 1 7  ? 7.159   -7.767  -5.948  1.00 23.10  ? 6   LYS   A O   1 
ATOM   46   C CB  . LYS   A 1 7  ? 7.022   -4.653  -7.075  1.00 28.27  ? 6   LYS   A CB  1 
ATOM   47   C CG  . LYS   A 1 7  ? 7.650   -4.545  -5.720  1.00 31.30  ? 6   LYS   A CG  1 
ATOM   48   C CD  . LYS   A 1 7  ? 8.432   -3.248  -5.445  1.00 36.56  ? 6   LYS   A CD  1 
ATOM   49   C CE  . LYS   A 1 7  ? 9.012   -3.244  -4.037  1.00 34.25  ? 6   LYS   A CE  1 
ATOM   50   N NZ  . LYS   A 1 7  ? 8.008   -3.144  -2.969  1.00 37.41  ? 6   LYS   A NZ  1 
ATOM   51   N N   . PRO   A 1 8  ? 8.115   -7.533  -7.942  1.00 25.34  ? 7   PRO   A N   1 
ATOM   52   C CA  . PRO   A 1 8  ? 9.072   -8.607  -7.681  1.00 23.70  ? 7   PRO   A CA  1 
ATOM   53   C C   . PRO   A 1 8  ? 9.854   -8.355  -6.412  1.00 22.08  ? 7   PRO   A C   1 
ATOM   54   O O   . PRO   A 1 8  ? 10.304  -7.233  -6.170  1.00 24.26  ? 7   PRO   A O   1 
ATOM   55   C CB  . PRO   A 1 8  ? 9.985   -8.601  -8.965  1.00 25.69  ? 7   PRO   A CB  1 
ATOM   56   C CG  . PRO   A 1 8  ? 9.006   -8.047  -9.995  1.00 27.43  ? 7   PRO   A CG  1 
ATOM   57   C CD  . PRO   A 1 8  ? 8.260   -6.921  -9.294  1.00 27.02  ? 7   PRO   A CD  1 
ATOM   58   N N   . GLY   A 1 9  ? 10.014  -9.422  -5.616  1.00 22.66  ? 8   GLY   A N   1 
ATOM   59   C CA  . GLY   A 1 9  ? 10.739  -9.359  -4.366  1.00 23.35  ? 8   GLY   A CA  1 
ATOM   60   C C   . GLY   A 1 9  ? 9.812   -9.213  -3.167  1.00 22.55  ? 8   GLY   A C   1 
ATOM   61   O O   . GLY   A 1 9  ? 10.217  -9.475  -2.026  1.00 23.67  ? 8   GLY   A O   1 
ATOM   62   N N   . ASP   A 1 10 ? 8.557   -8.811  -3.413  1.00 19.84  ? 9   ASP   A N   1 
ATOM   63   C CA  . ASP   A 1 10 ? 7.653   -8.753  -2.260  1.00 18.38  ? 9   ASP   A CA  1 
ATOM   64   C C   . ASP   A 1 10 ? 7.425   -10.141 -1.640  1.00 19.25  ? 9   ASP   A C   1 
ATOM   65   O O   . ASP   A 1 10 ? 7.264   -11.129 -2.352  1.00 20.13  ? 9   ASP   A O   1 
ATOM   66   C CB  . ASP   A 1 10 ? 6.319   -8.134  -2.675  1.00 19.72  ? 9   ASP   A CB  1 
ATOM   67   C CG  . ASP   A 1 10 ? 6.315   -6.639  -2.923  1.00 23.42  ? 9   ASP   A CG  1 
ATOM   68   O OD1 . ASP   A 1 10 ? 7.276   -5.947  -2.463  1.00 25.08  ? 9   ASP   A OD1 1 
ATOM   69   O OD2 . ASP   A 1 10 ? 5.323   -6.148  -3.508  1.00 23.88  ? 9   ASP   A OD2 1 
ATOM   70   N N   . LEU   A 1 11 ? 7.272   -10.190 -0.312  1.00 19.59  ? 10  LEU   A N   1 
ATOM   71   C CA  . LEU   A 1 11 ? 7.129   -11.429 0.454   1.00 17.58  ? 10  LEU   A CA  1 
ATOM   72   C C   . LEU   A 1 11 ? 5.656   -11.526 0.854   1.00 19.37  ? 10  LEU   A C   1 
ATOM   73   O O   . LEU   A 1 11 ? 5.086   -10.517 1.321   1.00 21.87  ? 10  LEU   A O   1 
ATOM   74   C CB  . LEU   A 1 11 ? 8.058   -11.479 1.685   1.00 18.80  ? 10  LEU   A CB  1 
ATOM   75   C CG  . LEU   A 1 11 ? 9.541   -11.287 1.322   1.00 21.08  ? 10  LEU   A CG  1 
ATOM   76   C CD1 . LEU   A 1 11 ? 10.374  -11.327 2.616   1.00 22.86  ? 10  LEU   A CD1 1 
ATOM   77   C CD2 . LEU   A 1 11 ? 10.004  -12.299 0.285   1.00 21.38  ? 10  LEU   A CD2 1 
ATOM   78   N N   . VAL   A 1 12 ? 5.111   -12.732 0.712   1.00 19.74  ? 11  VAL   A N   1 
ATOM   79   C CA  . VAL   A 1 12 ? 3.668   -12.928 0.920   1.00 19.13  ? 11  VAL   A CA  1 
ATOM   80   C C   . VAL   A 1 12 ? 3.420   -14.293 1.564   1.00 20.55  ? 11  VAL   A C   1 
ATOM   81   O O   . VAL   A 1 12 ? 4.278   -15.171 1.633   1.00 20.87  ? 11  VAL   A O   1 
ATOM   82   C CB  . VAL   A 1 12 ? 2.821   -12.837 -0.353  1.00 19.29  ? 11  VAL   A CB  1 
ATOM   83   C CG1 . VAL   A 1 12 ? 2.957   -11.454 -0.992  1.00 21.94  ? 11  VAL   A CG1 1 
ATOM   84   C CG2 . VAL   A 1 12 ? 3.263   -13.879 -1.383  1.00 21.66  ? 11  VAL   A CG2 1 
ATOM   85   N N   . PHE   A 1 13 ? 2.186   -14.495 2.074   1.00 19.81  ? 12  PHE   A N   1 
ATOM   86   C CA  . PHE   A 1 13 ? 1.641   -15.837 2.091   1.00 21.29  ? 12  PHE   A CA  1 
ATOM   87   C C   . PHE   A 1 13 ? 0.657   -15.899 0.927   1.00 22.04  ? 12  PHE   A C   1 
ATOM   88   O O   . PHE   A 1 13 ? -0.135  -14.959 0.724   1.00 22.83  ? 12  PHE   A O   1 
ATOM   89   C CB  . PHE   A 1 13 ? 0.858   -16.241 3.379   1.00 21.89  ? 12  PHE   A CB  1 
ATOM   90   C CG  . PHE   A 1 13 ? 1.789   -16.303 4.577   1.00 22.38  ? 12  PHE   A CG  1 
ATOM   91   C CD1 . PHE   A 1 13 ? 2.090   -15.107 5.235   1.00 23.02  ? 12  PHE   A CD1 1 
ATOM   92   C CD2 . PHE   A 1 13 ? 2.336   -17.514 5.008   1.00 26.19  ? 12  PHE   A CD2 1 
ATOM   93   C CE1 . PHE   A 1 13 ? 3.003   -15.136 6.308   1.00 30.06  ? 12  PHE   A CE1 1 
ATOM   94   C CE2 . PHE   A 1 13 ? 3.260   -17.544 6.081   1.00 26.25  ? 12  PHE   A CE2 1 
ATOM   95   C CZ  . PHE   A 1 13 ? 3.548   -16.351 6.723   1.00 26.73  ? 12  PHE   A CZ  1 
ATOM   96   N N   . ALA   A 1 14 ? 0.758   -16.983 0.141   1.00 21.44  ? 13  ALA   A N   1 
ATOM   97   C CA  . ALA   A 1 14 ? -0.053  -17.140 -1.061  1.00 22.13  ? 13  ALA   A CA  1 
ATOM   98   C C   . ALA   A 1 14 ? -1.032  -18.302 -0.837  1.00 22.99  ? 13  ALA   A C   1 
ATOM   99   O O   . ALA   A 1 14 ? -0.637  -19.377 -0.340  1.00 24.19  ? 13  ALA   A O   1 
ATOM   100  C CB  . ALA   A 1 14 ? 0.833   -17.366 -2.290  1.00 23.09  ? 13  ALA   A CB  1 
ATOM   101  N N   . LYS   A 1 15 ? -2.297  -18.084 -1.237  1.00 23.38  ? 14  LYS   A N   1 
ATOM   102  C CA  . LYS   A 1 15 ? -3.331  -19.097 -1.028  1.00 25.40  ? 14  LYS   A CA  1 
ATOM   103  C C   . LYS   A 1 15 ? -3.688  -19.804 -2.338  1.00 26.93  ? 14  LYS   A C   1 
ATOM   104  O O   . LYS   A 1 15 ? -4.045  -19.160 -3.305  1.00 29.69  ? 14  LYS   A O   1 
ATOM   105  C CB  . LYS   A 1 15 ? -4.532  -18.410 -0.351  1.00 26.52  ? 14  LYS   A CB  1 
ATOM   106  C CG  . LYS   A 1 15 ? -5.684  -19.388 0.025   1.00 30.05  ? 14  LYS   A CG  1 
ATOM   107  C CD  . LYS   A 1 15 ? -5.217  -20.364 1.097   1.00 31.13  ? 14  LYS   A CD  1 
ATOM   108  C CE  . LYS   A 1 15 ? -6.259  -21.200 1.804   1.00 33.69  ? 14  LYS   A CE  1 
ATOM   109  N NZ  . LYS   A 1 15 ? -6.584  -22.363 0.964   1.00 36.54  ? 14  LYS   A NZ  1 
ATOM   110  N N   . MET   A 1 16 ? -3.617  -21.145 -2.303  1.00 29.00  ? 15  MET   A N   1 
ATOM   111  C CA  . MET   A 1 16 ? -4.120  -22.016 -3.351  1.00 29.97  ? 15  MET   A CA  1 
ATOM   112  C C   . MET   A 1 16 ? -5.213  -22.896 -2.719  1.00 31.70  ? 15  MET   A C   1 
ATOM   113  O O   . MET   A 1 16 ? -5.085  -23.295 -1.569  1.00 29.45  ? 15  MET   A O   1 
ATOM   114  C CB  . MET   A 1 16 ? -3.004  -22.994 -3.755  1.00 32.41  ? 15  MET   A CB  1 
ATOM   115  C CG  . MET   A 1 16 ? -1.663  -22.383 -4.123  1.00 38.77  ? 15  MET   A CG  1 
ATOM   116  S SD  . MET   A 1 16 ? -1.626  -21.870 -5.852  1.00 39.40  ? 15  MET   A SD  1 
ATOM   117  C CE  . MET   A 1 16 ? -1.641  -23.357 -6.835  1.00 39.12  ? 15  MET   A CE  1 
ATOM   118  N N   . LYS   A 1 17 ? -6.214  -23.257 -3.525  1.00 37.71  ? 16  LYS   A N   1 
ATOM   119  C CA  . LYS   A 1 17 ? -7.264  -24.206 -3.164  1.00 40.14  ? 16  LYS   A CA  1 
ATOM   120  C C   . LYS   A 1 17 ? -6.654  -25.470 -2.574  1.00 34.75  ? 16  LYS   A C   1 
ATOM   121  O O   . LYS   A 1 17 ? -5.754  -26.078 -3.160  1.00 36.01  ? 16  LYS   A O   1 
ATOM   122  C CB  . LYS   A 1 17 ? -7.848  -24.703 -4.493  1.00 45.62  ? 16  LYS   A CB  1 
ATOM   123  C CG  . LYS   A 1 17 ? -9.133  -25.535 -4.367  1.00 54.70  ? 16  LYS   A CG  1 
ATOM   124  C CD  . LYS   A 1 17 ? -10.452 -24.830 -4.695  1.00 64.53  ? 16  LYS   A CD  1 
ATOM   125  C CE  . LYS   A 1 17 ? -10.693 -23.456 -4.135  1.00 66.90  ? 16  LYS   A CE  1 
ATOM   126  N NZ  . LYS   A 1 17 ? -10.737 -23.395 -2.674  1.00 70.59  ? 16  LYS   A NZ  1 
ATOM   127  N N   . GLY   A 1 18 ? -7.125  -25.883 -1.387  1.00 37.47  ? 17  GLY   A N   1 
ATOM   128  C CA  . GLY   A 1 18 ? -6.678  -27.153 -0.853  1.00 35.77  ? 17  GLY   A CA  1 
ATOM   129  C C   . GLY   A 1 18 ? -5.383  -27.074 -0.051  1.00 42.56  ? 17  GLY   A C   1 
ATOM   130  O O   . GLY   A 1 18 ? -4.924  -28.077 0.481   1.00 44.90  ? 17  GLY   A O   1 
ATOM   131  N N   . TYR   A 1 19 ? -4.761  -25.887 0.014   1.00 36.29  ? 18  TYR   A N   1 
ATOM   132  C CA  . TYR   A 1 19 ? -3.529  -25.789 0.759   1.00 32.31  ? 18  TYR   A CA  1 
ATOM   133  C C   . TYR   A 1 19 ? -3.589  -24.630 1.733   1.00 29.18  ? 18  TYR   A C   1 
ATOM   134  O O   . TYR   A 1 19 ? -4.281  -23.659 1.493   1.00 30.66  ? 18  TYR   A O   1 
ATOM   135  C CB  . TYR   A 1 19 ? -2.430  -25.423 -0.236  1.00 35.03  ? 18  TYR   A CB  1 
ATOM   136  C CG  . TYR   A 1 19 ? -2.094  -26.477 -1.280  1.00 41.48  ? 18  TYR   A CG  1 
ATOM   137  C CD1 . TYR   A 1 19 ? -1.101  -27.412 -1.022  1.00 52.66  ? 18  TYR   A CD1 1 
ATOM   138  C CD2 . TYR   A 1 19 ? -2.712  -26.490 -2.531  1.00 42.73  ? 18  TYR   A CD2 1 
ATOM   139  C CE1 . TYR   A 1 19 ? -0.731  -28.341 -1.980  1.00 55.88  ? 18  TYR   A CE1 1 
ATOM   140  C CE2 . TYR   A 1 19 ? -2.359  -27.427 -3.499  1.00 45.71  ? 18  TYR   A CE2 1 
ATOM   141  C CZ  . TYR   A 1 19 ? -1.357  -28.346 -3.215  1.00 60.01  ? 18  TYR   A CZ  1 
ATOM   142  O OH  . TYR   A 1 19 ? -0.946  -29.288 -4.122  1.00 70.75  ? 18  TYR   A OH  1 
ATOM   143  N N   . PRO   A 1 20 ? -2.818  -24.690 2.831   1.00 31.18  ? 19  PRO   A N   1 
ATOM   144  C CA  . PRO   A 1 20 ? -2.757  -23.600 3.814   1.00 29.51  ? 19  PRO   A CA  1 
ATOM   145  C C   . PRO   A 1 20 ? -2.089  -22.393 3.138   1.00 27.69  ? 19  PRO   A C   1 
ATOM   146  O O   . PRO   A 1 20 ? -1.349  -22.598 2.192   1.00 26.90  ? 19  PRO   A O   1 
ATOM   147  C CB  . PRO   A 1 20 ? -1.922  -24.202 4.964   1.00 34.29  ? 19  PRO   A CB  1 
ATOM   148  C CG  . PRO   A 1 20 ? -1.079  -25.284 4.283   1.00 32.65  ? 19  PRO   A CG  1 
ATOM   149  C CD  . PRO   A 1 20 ? -1.950  -25.839 3.169   1.00 33.26  ? 19  PRO   A CD  1 
ATOM   150  N N   . HIS   A 1 21 ? -2.380  -21.192 3.622   1.00 25.81  ? 20  HIS   A N   1 
ATOM   151  C CA  . HIS   A 1 21 ? -1.663  -19.976 3.183   1.00 24.55  ? 20  HIS   A CA  1 
ATOM   152  C C   . HIS   A 1 21 ? -0.151  -20.216 3.323   1.00 27.02  ? 20  HIS   A C   1 
ATOM   153  O O   . HIS   A 1 21 ? 0.311   -20.668 4.377   1.00 25.31  ? 20  HIS   A O   1 
ATOM   154  C CB  . HIS   A 1 21 ? -2.095  -18.797 4.066   1.00 25.37  ? 20  HIS   A CB  1 
ATOM   155  C CG  . HIS   A 1 21 ? -3.532  -18.374 3.886   1.00 25.89  ? 20  HIS   A CG  1 
ATOM   156  N ND1 . HIS   A 1 21 ? -4.557  -19.028 4.549   1.00 30.38  ? 20  HIS   A ND1 1 
ATOM   157  C CD2 . HIS   A 1 21 ? -4.107  -17.400 3.141   1.00 28.81  ? 20  HIS   A CD2 1 
ATOM   158  C CE1 . HIS   A 1 21 ? -5.715  -18.455 4.214   1.00 31.44  ? 20  HIS   A CE1 1 
ATOM   159  N NE2 . HIS   A 1 21 ? -5.478  -17.463 3.366   1.00 32.09  ? 20  HIS   A NE2 1 
ATOM   160  N N   . TRP   A 1 22 ? 0.619   -20.008 2.214   1.00 24.56  ? 21  TRP   A N   1 
ATOM   161  C CA  . TRP   A 1 22 ? 1.925   -20.647 2.079   1.00 23.78  ? 21  TRP   A CA  1 
ATOM   162  C C   . TRP   A 1 22 ? 2.982   -19.540 1.945   1.00 22.58  ? 21  TRP   A C   1 
ATOM   163  O O   . TRP   A 1 22 ? 2.842   -18.635 1.103   1.00 21.95  ? 21  TRP   A O   1 
ATOM   164  C CB  . TRP   A 1 22 ? 1.945   -21.534 0.827   1.00 23.69  ? 21  TRP   A CB  1 
ATOM   165  C CG  . TRP   A 1 22 ? 3.053   -22.560 0.880   1.00 24.67  ? 21  TRP   A CG  1 
ATOM   166  C CD1 . TRP   A 1 22 ? 4.402   -22.369 0.709   1.00 24.07  ? 21  TRP   A CD1 1 
ATOM   167  C CD2 . TRP   A 1 22 ? 2.865   -23.956 1.218   1.00 27.22  ? 21  TRP   A CD2 1 
ATOM   168  N NE1 . TRP   A 1 22 ? 5.048   -23.589 0.841   1.00 24.84  ? 21  TRP   A NE1 1 
ATOM   169  C CE2 . TRP   A 1 22 ? 4.144   -24.561 1.184   1.00 29.25  ? 21  TRP   A CE2 1 
ATOM   170  C CE3 . TRP   A 1 22 ? 1.743   -24.741 1.541   1.00 32.03  ? 21  TRP   A CE3 1 
ATOM   171  C CZ2 . TRP   A 1 22 ? 4.347   -25.921 1.462   1.00 32.35  ? 21  TRP   A CZ2 1 
ATOM   172  C CZ3 . TRP   A 1 22 ? 1.945   -26.091 1.809   1.00 32.45  ? 21  TRP   A CZ3 1 
ATOM   173  C CH2 . TRP   A 1 22 ? 3.226   -26.666 1.759   1.00 35.41  ? 21  TRP   A CH2 1 
ATOM   174  N N   . PRO   A 1 23 ? 4.132   -19.608 2.658   1.00 22.96  ? 22  PRO   A N   1 
ATOM   175  C CA  . PRO   A 1 23 ? 5.203   -18.618 2.460   1.00 22.01  ? 22  PRO   A CA  1 
ATOM   176  C C   . PRO   A 1 23 ? 5.721   -18.561 1.013   1.00 20.82  ? 22  PRO   A C   1 
ATOM   177  O O   . PRO   A 1 23 ? 6.057   -19.594 0.429   1.00 21.56  ? 22  PRO   A O   1 
ATOM   178  C CB  . PRO   A 1 23 ? 6.278   -19.088 3.473   1.00 22.19  ? 22  PRO   A CB  1 
ATOM   179  C CG  . PRO   A 1 23 ? 6.073   -20.587 3.604   1.00 20.84  ? 22  PRO   A CG  1 
ATOM   180  C CD  . PRO   A 1 23 ? 4.521   -20.694 3.593   1.00 22.66  ? 22  PRO   A CD  1 
ATOM   181  N N   . ALA   A 1 24 ? 5.752   -17.365 0.424   1.00 18.87  ? 23  ALA   A N   1 
ATOM   182  C CA  . ALA   A 1 24 ? 6.114   -17.246 -0.991  1.00 21.08  ? 23  ALA   A CA  1 
ATOM   183  C C   . ALA   A 1 24 ? 6.625   -15.840 -1.289  1.00 19.61  ? 23  ALA   A C   1 
ATOM   184  O O   . ALA   A 1 24 ? 6.607   -14.941 -0.474  1.00 19.81  ? 23  ALA   A O   1 
ATOM   185  C CB  . ALA   A 1 24 ? 4.856   -17.600 -1.835  1.00 20.69  ? 23  ALA   A CB  1 
ATOM   186  N N   . ARG   A 1 25 ? 7.126   -15.657 -2.515  1.00 19.33  ? 24  ARG   A N   1 
ATOM   187  C CA  . ARG   A 1 25 ? 7.558   -14.345 -2.961  1.00 19.20  ? 24  ARG   A CA  1 
ATOM   188  C C   . ARG   A 1 25 ? 7.045   -14.086 -4.377  1.00 18.93  ? 24  ARG   A C   1 
ATOM   189  O O   . ARG   A 1 25 ? 6.767   -15.052 -5.112  1.00 21.60  ? 24  ARG   A O   1 
ATOM   190  C CB  . ARG   A 1 25 ? 9.078   -14.215 -2.903  1.00 20.85  ? 24  ARG   A CB  1 
ATOM   191  C CG  . ARG   A 1 25 ? 9.746   -15.124 -3.922  1.00 20.55  ? 24  ARG   A CG  1 
ATOM   192  C CD  . ARG   A 1 25 ? 11.294  -14.932 -3.766  1.00 20.02  ? 24  ARG   A CD  1 
ATOM   193  N NE  . ARG   A 1 25 ? 11.973  -15.731 -4.817  1.00 22.09  ? 24  ARG   A NE  1 
ATOM   194  C CZ  . ARG   A 1 25 ? 13.251  -16.141 -4.716  1.00 23.88  ? 24  ARG   A CZ  1 
ATOM   195  N NH1 . ARG   A 1 25 ? 13.943  -16.010 -3.589  1.00 23.60  ? 24  ARG   A NH1 1 
ATOM   196  N NH2 . ARG   A 1 25 ? 13.810  -16.779 -5.756  1.00 27.43  ? 24  ARG   A NH2 1 
ATOM   197  N N   . ILE   A 1 26 ? 6.887   -12.812 -4.711  1.00 21.05  ? 25  ILE   A N   1 
ATOM   198  C CA  . ILE   A 1 26 ? 6.674   -12.456 -6.121  1.00 20.33  ? 25  ILE   A CA  1 
ATOM   199  C C   . ILE   A 1 26 ? 8.000   -12.578 -6.824  1.00 22.51  ? 25  ILE   A C   1 
ATOM   200  O O   . ILE   A 1 26 ? 8.963   -11.918 -6.465  1.00 22.36  ? 25  ILE   A O   1 
ATOM   201  C CB  . ILE   A 1 26 ? 6.188   -10.999 -6.194  1.00 21.45  ? 25  ILE   A CB  1 
ATOM   202  C CG1 . ILE   A 1 26 ? 5.034   -10.698 -5.218  1.00 26.35  ? 25  ILE   A CG1 1 
ATOM   203  C CG2 . ILE   A 1 26 ? 5.852   -10.624 -7.650  1.00 22.56  ? 25  ILE   A CG2 1 
ATOM   204  C CD1 . ILE   A 1 26 ? 3.690   -11.255 -5.614  1.00 31.24  ? 25  ILE   A CD1 1 
ATOM   205  N N   . ASP   A 1 27 ? 8.026   -13.409 -7.871  1.00 22.13  ? 26  ASP   A N   1 
ATOM   206  C CA  . ASP   A 1 27 ? 9.270   -13.581 -8.621  1.00 23.86  ? 26  ASP   A CA  1 
ATOM   207  C C   . ASP   A 1 27 ? 9.383   -12.570 -9.768  1.00 24.81  ? 26  ASP   A C   1 
ATOM   208  O O   . ASP   A 1 27 ? 8.460   -11.891 -10.185 1.00 25.68  ? 26  ASP   A O   1 
ATOM   209  C CB  . ASP   A 1 27 ? 9.346   -14.980 -9.199  1.00 23.26  ? 26  ASP   A CB  1 
ATOM   210  C CG  . ASP   A 1 27 ? 10.326  -15.906 -8.502  1.00 25.36  ? 26  ASP   A CG  1 
ATOM   211  O OD1 . ASP   A 1 27 ? 10.909  -15.471 -7.461  1.00 30.77  ? 26  ASP   A OD1 1 
ATOM   212  O OD2 . ASP   A 1 27 ? 10.480  -17.045 -8.952  1.00 27.57  ? 26  ASP   A OD2 1 
ATOM   213  N N   . ASP   A 1 28 ? 10.622  -12.419 -10.272 1.00 28.24  ? 27  ASP   A N   1 
ATOM   214  C CA  . ASP   A 1 28 ? 10.810  -11.738 -11.536 1.00 32.59  ? 27  ASP   A CA  1 
ATOM   215  C C   . ASP   A 1 28 ? 10.533  -12.754 -12.648 1.00 28.72  ? 27  ASP   A C   1 
ATOM   216  O O   . ASP   A 1 28 ? 10.481  -13.953 -12.400 1.00 31.06  ? 27  ASP   A O   1 
ATOM   217  C CB  . ASP   A 1 28 ? 12.278  -11.337 -11.693 1.00 37.24  ? 27  ASP   A CB  1 
ATOM   218  C CG  . ASP   A 1 28 ? 12.749  -10.075 -10.974 1.00 46.01  ? 27  ASP   A CG  1 
ATOM   219  O OD1 . ASP   A 1 28 ? 12.379  -8.963  -11.410 1.00 47.70  ? 27  ASP   A OD1 1 
ATOM   220  O OD2 . ASP   A 1 28 ? 13.495  -10.220 -9.980  1.00 51.40  ? 27  ASP   A OD2 1 
ATOM   221  N N   . ILE   A 1 29 ? 10.387  -12.270 -13.880 1.00 34.27  ? 28  ILE   A N   1 
ATOM   222  C CA  . ILE   A 1 29 ? 10.346  -13.176 -15.026 1.00 32.04  ? 28  ILE   A CA  1 
ATOM   223  C C   . ILE   A 1 29 ? 11.687  -12.972 -15.725 1.00 30.31  ? 28  ILE   A C   1 
ATOM   224  O O   . ILE   A 1 29 ? 12.042  -11.824 -15.982 1.00 32.28  ? 28  ILE   A O   1 
ATOM   225  C CB  . ILE   A 1 29 ? 9.197   -12.717 -15.933 1.00 33.20  ? 28  ILE   A CB  1 
ATOM   226  C CG1 . ILE   A 1 29 ? 7.850   -12.725 -15.175 1.00 35.34  ? 28  ILE   A CG1 1 
ATOM   227  C CG2 . ILE   A 1 29 ? 9.155   -13.523 -17.229 1.00 31.99  ? 28  ILE   A CG2 1 
ATOM   228  C CD1 . ILE   A 1 29 ? 6.877   -11.689 -15.691 1.00 39.63  ? 28  ILE   A CD1 1 
ATOM   229  N N   . ALA   A 1 30 ? 12.430  -14.069 -15.910 1.00 30.94  ? 29  ALA   A N   1 
ATOM   230  C CA  . ALA   A 1 30 ? 13.727  -14.015 -16.587 1.00 27.93  ? 29  ALA   A CA  1 
ATOM   231  C C   . ALA   A 1 30 ? 13.519  -13.629 -18.060 1.00 29.39  ? 29  ALA   A C   1 
ATOM   232  O O   . ALA   A 1 30 ? 12.492  -13.948 -18.664 1.00 31.90  ? 29  ALA   A O   1 
ATOM   233  C CB  . ALA   A 1 30 ? 14.379  -15.388 -16.487 1.00 31.87  ? 29  ALA   A CB  1 
ATOM   234  N N   . ASP   A 1 31 ? 14.472  -12.887 -18.642 1.00 28.93  ? 30  ASP   A N   1 
ATOM   235  C CA  . ASP   A 1 31 ? 14.446  -12.724 -20.106 1.00 28.82  ? 30  ASP   A CA  1 
ATOM   236  C C   . ASP   A 1 31 ? 14.313  -14.093 -20.765 1.00 26.36  ? 30  ASP   A C   1 
ATOM   237  O O   . ASP   A 1 31 ? 14.983  -15.032 -20.378 1.00 29.06  ? 30  ASP   A O   1 
ATOM   238  C CB  . ASP   A 1 31 ? 15.723  -12.017 -20.555 1.00 29.37  ? 30  ASP   A CB  1 
ATOM   239  C CG  . ASP   A 1 31 ? 15.832  -10.536 -20.254 1.00 34.39  ? 30  ASP   A CG  1 
ATOM   240  O OD1 . ASP   A 1 31 ? 14.783  -9.905  -20.098 1.00 40.48  ? 30  ASP   A OD1 1 
ATOM   241  O OD2 . ASP   A 1 31 ? 17.001  -10.053 -20.177 1.00 38.78  ? 30  ASP   A OD2 1 
ATOM   242  N N   . GLY   A 1 32 ? 13.417  -14.157 -21.760 1.00 25.93  ? 31  GLY   A N   1 
ATOM   243  C CA  . GLY   A 1 32 ? 13.186  -15.353 -22.553 1.00 26.43  ? 31  GLY   A CA  1 
ATOM   244  C C   . GLY   A 1 32 ? 12.307  -16.407 -21.889 1.00 29.03  ? 31  GLY   A C   1 
ATOM   245  O O   . GLY   A 1 32 ? 12.037  -17.430 -22.504 1.00 32.52  ? 31  GLY   A O   1 
ATOM   246  N N   . ALA   A 1 33 ? 11.859  -16.133 -20.656 1.00 28.39  ? 32  ALA   A N   1 
ATOM   247  C CA  . ALA   A 1 33 ? 11.026  -17.098 -19.929 1.00 28.51  ? 32  ALA   A CA  1 
ATOM   248  C C   . ALA   A 1 33 ? 9.538   -16.840 -20.174 1.00 29.44  ? 32  ALA   A C   1 
ATOM   249  O O   . ALA   A 1 33 ? 9.088   -15.757 -20.552 1.00 29.17  ? 32  ALA   A O   1 
ATOM   250  C CB  . ALA   A 1 33 ? 11.350  -16.988 -18.446 1.00 31.13  ? 32  ALA   A CB  1 
ATOM   251  N N   . VAL   A 1 34 ? 8.736   -17.894 -19.903 1.00 31.68  ? 33  VAL   A N   1 
ATOM   252  C CA  . VAL   A 1 34 ? 7.289   -17.771 -20.048 1.00 34.61  ? 33  VAL   A CA  1 
ATOM   253  C C   . VAL   A 1 34 ? 6.718   -16.704 -19.110 1.00 34.29  ? 33  VAL   A C   1 
ATOM   254  O O   . VAL   A 1 34 ? 6.964   -16.752 -17.907 1.00 35.02  ? 33  VAL   A O   1 
ATOM   255  C CB  . VAL   A 1 34 ? 6.690   -19.143 -19.683 1.00 36.28  ? 33  VAL   A CB  1 
ATOM   256  C CG1 . VAL   A 1 34 ? 5.171   -19.039 -19.576 1.00 38.28  ? 33  VAL   A CG1 1 
ATOM   257  C CG2 . VAL   A 1 34 ? 7.086   -20.180 -20.732 1.00 37.84  ? 33  VAL   A CG2 1 
ATOM   258  N N   . LYS   A 1 35 ? 5.895   -15.820 -19.676 1.00 35.17  ? 34  LYS   A N   1 
ATOM   259  C CA  . LYS   A 1 35 ? 5.238   -14.733 -18.954 1.00 35.92  ? 34  LYS   A CA  1 
ATOM   260  C C   . LYS   A 1 35 ? 3.927   -15.225 -18.350 1.00 38.87  ? 34  LYS   A C   1 
ATOM   261  O O   . LYS   A 1 35 ? 3.280   -16.122 -18.876 1.00 38.31  ? 34  LYS   A O   1 
ATOM   262  C CB  . LYS   A 1 35 ? 4.867   -13.540 -19.835 1.00 35.94  ? 34  LYS   A CB  1 
ATOM   263  C CG  . LYS   A 1 35 ? 6.082   -12.798 -20.374 1.00 37.83  ? 34  LYS   A CG  1 
ATOM   264  C CD  . LYS   A 1 35 ? 5.793   -11.605 -21.283 1.00 46.21  ? 34  LYS   A CD  1 
ATOM   265  C CE  . LYS   A 1 35 ? 5.437   -11.992 -22.680 1.00 44.22  ? 34  LYS   A CE  1 
ATOM   266  N NZ  . LYS   A 1 35 ? 5.178   -10.787 -23.469 1.00 46.27  ? 34  LYS   A NZ  1 
ATOM   267  N N   . PRO   A 1 36 ? 3.458   -14.636 -17.227 1.00 37.36  ? 35  PRO   A N   1 
ATOM   268  C CA  . PRO   A 1 36 ? 2.190   -15.080 -16.654 1.00 35.83  ? 35  PRO   A CA  1 
ATOM   269  C C   . PRO   A 1 36 ? 1.039   -14.557 -17.508 1.00 34.07  ? 35  PRO   A C   1 
ATOM   270  O O   . PRO   A 1 36 ? 1.183   -13.580 -18.246 1.00 36.02  ? 35  PRO   A O   1 
ATOM   271  C CB  . PRO   A 1 36 ? 2.167   -14.455 -15.241 1.00 36.46  ? 35  PRO   A CB  1 
ATOM   272  C CG  . PRO   A 1 36 ? 3.034   -13.211 -15.373 1.00 42.10  ? 35  PRO   A CG  1 
ATOM   273  C CD  . PRO   A 1 36 ? 4.018   -13.459 -16.549 1.00 38.69  ? 35  PRO   A CD  1 
ATOM   274  N N   . PRO   A 1 37 ? -0.177  -15.077 -17.267 1.00 35.58  ? 36  PRO   A N   1 
ATOM   275  C CA  . PRO   A 1 37 ? -1.392  -14.490 -17.839 1.00 40.77  ? 36  PRO   A CA  1 
ATOM   276  C C   . PRO   A 1 37 ? -1.580  -13.052 -17.374 1.00 42.00  ? 36  PRO   A C   1 
ATOM   277  O O   . PRO   A 1 37 ? -1.087  -12.680 -16.308 1.00 32.79  ? 36  PRO   A O   1 
ATOM   278  C CB  . PRO   A 1 37 ? -2.528  -15.363 -17.292 1.00 38.93  ? 36  PRO   A CB  1 
ATOM   279  C CG  . PRO   A 1 37 ? -1.860  -16.633 -16.810 1.00 38.78  ? 36  PRO   A CG  1 
ATOM   280  C CD  . PRO   A 1 37 ? -0.437  -16.250 -16.421 1.00 36.99  ? 36  PRO   A CD  1 
ATOM   281  N N   . PRO   A 1 38 ? -2.347  -12.218 -18.113 1.00 38.79  ? 37  PRO   A N   1 
ATOM   282  C CA  . PRO   A 1 38 ? -2.762  -10.897 -17.638 1.00 41.77  ? 37  PRO   A CA  1 
ATOM   283  C C   . PRO   A 1 38 ? -3.312  -10.908 -16.218 1.00 32.05  ? 37  PRO   A C   1 
ATOM   284  O O   . PRO   A 1 38 ? -4.037  -11.819 -15.846 1.00 35.13  ? 37  PRO   A O   1 
ATOM   285  C CB  . PRO   A 1 38 ? -3.837  -10.402 -18.639 1.00 43.79  ? 37  PRO   A CB  1 
ATOM   286  C CG  . PRO   A 1 38 ? -3.970  -11.537 -19.611 1.00 41.17  ? 37  PRO   A CG  1 
ATOM   287  C CD  . PRO   A 1 38 ? -2.832  -12.515 -19.483 1.00 43.92  ? 37  PRO   A CD  1 
ATOM   288  N N   . ASN   A 1 39 ? -2.895  -9.903  -15.442 1.00 37.50  ? 38  ASN   A N   1 
ATOM   289  C CA  . ASN   A 1 39 ? -3.353  -9.641  -14.092 1.00 35.97  ? 38  ASN   A CA  1 
ATOM   290  C C   . ASN   A 1 39 ? -2.874  -10.711 -13.112 1.00 32.99  ? 38  ASN   A C   1 
ATOM   291  O O   . ASN   A 1 39 ? -3.364  -10.710 -11.976 1.00 33.11  ? 38  ASN   A O   1 
ATOM   292  C CB  . ASN   A 1 39 ? -4.877  -9.565  -14.017 1.00 44.78  ? 38  ASN   A CB  1 
ATOM   293  C CG  . ASN   A 1 39 ? -5.367  -8.376  -14.807 1.00 52.24  ? 38  ASN   A CG  1 
ATOM   294  O OD1 . ASN   A 1 39 ? -5.240  -7.230  -14.345 1.00 49.56  ? 38  ASN   A OD1 1 
ATOM   295  N ND2 . ASN   A 1 39 ? -5.863  -8.628  -16.006 1.00 49.89  ? 38  ASN   A ND2 1 
ATOM   296  N N   . LYS   A 1 40 ? -1.971  -11.625 -13.548 1.00 29.46  ? 39  LYS   A N   1 
ATOM   297  C CA  . LYS   A 1 40 ? -1.431  -12.625 -12.630 1.00 23.73  ? 39  LYS   A CA  1 
ATOM   298  C C   . LYS   A 1 40 ? 0.066   -12.328 -12.418 1.00 23.60  ? 39  LYS   A C   1 
ATOM   299  O O   . LYS   A 1 40 ? 0.717   -11.629 -13.202 1.00 26.26  ? 39  LYS   A O   1 
ATOM   300  C CB  . LYS   A 1 40 ? -1.597  -14.069 -13.104 1.00 28.57  ? 39  LYS   A CB  1 
ATOM   301  C CG  . LYS   A 1 40 ? -3.001  -14.543 -13.593 1.00 31.95  ? 39  LYS   A CG  1 
ATOM   302  C CD  . LYS   A 1 40 ? -3.858  -14.419 -12.342 1.00 34.52  ? 39  LYS   A CD  1 
ATOM   303  C CE  . LYS   A 1 40 ? -5.342  -14.665 -12.600 1.00 45.98  ? 39  LYS   A CE  1 
ATOM   304  N NZ  . LYS   A 1 40 ? -5.558  -16.094 -12.830 1.00 49.64  ? 39  LYS   A NZ  1 
ATOM   305  N N   . TYR   A 1 41 ? 0.572   -12.803 -11.270 1.00 22.57  ? 40  TYR   A N   1 
ATOM   306  C CA  . TYR   A 1 41 ? 1.956   -12.638 -10.872 1.00 23.87  ? 40  TYR   A CA  1 
ATOM   307  C C   . TYR   A 1 41 ? 2.602   -14.012 -10.779 1.00 22.27  ? 40  TYR   A C   1 
ATOM   308  O O   . TYR   A 1 41 ? 1.981   -15.001 -10.393 1.00 22.62  ? 40  TYR   A O   1 
ATOM   309  C CB  . TYR   A 1 41 ? 2.036   -12.045 -9.437  1.00 22.62  ? 40  TYR   A CB  1 
ATOM   310  C CG  . TYR   A 1 41 ? 1.563   -10.599 -9.439  1.00 24.71  ? 40  TYR   A CG  1 
ATOM   311  C CD1 . TYR   A 1 41 ? 0.204   -10.321 -9.306  1.00 27.62  ? 40  TYR   A CD1 1 
ATOM   312  C CD2 . TYR   A 1 41 ? 2.428   -9.531  -9.627  1.00 27.92  ? 40  TYR   A CD2 1 
ATOM   313  C CE1 . TYR   A 1 41 ? -0.269  -9.029  -9.429  1.00 32.23  ? 40  TYR   A CE1 1 
ATOM   314  C CE2 . TYR   A 1 41 ? 1.958   -8.213  -9.705  1.00 28.84  ? 40  TYR   A CE2 1 
ATOM   315  C CZ  . TYR   A 1 41 ? 0.606   -7.972  -9.564  1.00 32.94  ? 40  TYR   A CZ  1 
ATOM   316  O OH  . TYR   A 1 41 ? 0.059   -6.718  -9.715  1.00 33.93  ? 40  TYR   A OH  1 
ATOM   317  N N   . PRO   A 1 42 ? 3.917   -14.155 -11.083 1.00 23.22  ? 41  PRO   A N   1 
ATOM   318  C CA  . PRO   A 1 42 ? 4.587   -15.441 -10.848 1.00 23.38  ? 41  PRO   A CA  1 
ATOM   319  C C   . PRO   A 1 42 ? 4.945   -15.558 -9.371  1.00 22.57  ? 41  PRO   A C   1 
ATOM   320  O O   . PRO   A 1 42 ? 5.652   -14.675 -8.863  1.00 23.96  ? 41  PRO   A O   1 
ATOM   321  C CB  . PRO   A 1 42 ? 5.885   -15.317 -11.678 1.00 24.36  ? 41  PRO   A CB  1 
ATOM   322  C CG  . PRO   A 1 42 ? 6.086   -13.862 -11.858 1.00 24.42  ? 41  PRO   A CG  1 
ATOM   323  C CD  . PRO   A 1 42 ? 4.783   -13.084 -11.612 1.00 25.31  ? 41  PRO   A CD  1 
ATOM   324  N N   . ILE   A 1 43 ? 4.379   -16.572 -8.711  1.00 21.86  ? 42  ILE   A N   1 
ATOM   325  C CA  . ILE   A 1 43 ? 4.590   -16.734 -7.273  1.00 20.83  ? 42  ILE   A CA  1 
ATOM   326  C C   . ILE   A 1 43 ? 5.540   -17.913 -7.075  1.00 22.38  ? 42  ILE   A C   1 
ATOM   327  O O   . ILE   A 1 43 ? 5.255   -19.063 -7.524  1.00 24.59  ? 42  ILE   A O   1 
ATOM   328  C CB  . ILE   A 1 43 ? 3.233   -16.998 -6.618  1.00 21.43  ? 42  ILE   A CB  1 
ATOM   329  C CG1 . ILE   A 1 43 ? 2.257   -15.842 -6.866  1.00 22.37  ? 42  ILE   A CG1 1 
ATOM   330  C CG2 . ILE   A 1 43 ? 3.482   -17.248 -5.114  1.00 22.39  ? 42  ILE   A CG2 1 
ATOM   331  C CD1 . ILE   A 1 43 ? 2.798   -14.465 -6.546  1.00 23.24  ? 42  ILE   A CD1 1 
ATOM   332  N N   . PHE   A 1 44 ? 6.664   -17.671 -6.370  1.00 21.00  ? 43  PHE   A N   1 
ATOM   333  C CA  . PHE   A 1 44 ? 7.547   -18.751 -6.032  1.00 21.65  ? 43  PHE   A CA  1 
ATOM   334  C C   . PHE   A 1 44 ? 7.280   -19.152 -4.579  1.00 22.06  ? 43  PHE   A C   1 
ATOM   335  O O   . PHE   A 1 44 ? 7.311   -18.307 -3.674  1.00 22.10  ? 43  PHE   A O   1 
ATOM   336  C CB  . PHE   A 1 44 ? 8.998   -18.268 -6.219  1.00 23.33  ? 43  PHE   A CB  1 
ATOM   337  C CG  . PHE   A 1 44 ? 10.014  -19.290 -5.743  1.00 24.98  ? 43  PHE   A CG  1 
ATOM   338  C CD1 . PHE   A 1 44 ? 10.422  -20.301 -6.631  1.00 26.02  ? 43  PHE   A CD1 1 
ATOM   339  C CD2 . PHE   A 1 44 ? 10.595  -19.226 -4.463  1.00 26.23  ? 43  PHE   A CD2 1 
ATOM   340  C CE1 . PHE   A 1 44 ? 11.375  -21.252 -6.226  1.00 27.30  ? 43  PHE   A CE1 1 
ATOM   341  C CE2 . PHE   A 1 44 ? 11.545  -20.193 -4.072  1.00 26.81  ? 43  PHE   A CE2 1 
ATOM   342  C CZ  . PHE   A 1 44 ? 11.923  -21.189 -4.959  1.00 26.52  ? 43  PHE   A CZ  1 
ATOM   343  N N   . PHE   A 1 45 ? 6.975   -20.437 -4.378  1.00 21.64  ? 44  PHE   A N   1 
ATOM   344  C CA  . PHE   A 1 45 ? 6.595   -20.960 -3.080  1.00 21.70  ? 44  PHE   A CA  1 
ATOM   345  C C   . PHE   A 1 45 ? 7.822   -21.493 -2.355  1.00 24.35  ? 44  PHE   A C   1 
ATOM   346  O O   . PHE   A 1 45 ? 8.537   -22.378 -2.877  1.00 23.67  ? 44  PHE   A O   1 
ATOM   347  C CB  . PHE   A 1 45 ? 5.583   -22.107 -3.265  1.00 24.60  ? 44  PHE   A CB  1 
ATOM   348  C CG  . PHE   A 1 45 ? 4.203   -21.611 -3.659  1.00 23.70  ? 44  PHE   A CG  1 
ATOM   349  C CD1 . PHE   A 1 45 ? 3.886   -21.419 -4.997  1.00 27.88  ? 44  PHE   A CD1 1 
ATOM   350  C CD2 . PHE   A 1 45 ? 3.224   -21.343 -2.709  1.00 26.30  ? 44  PHE   A CD2 1 
ATOM   351  C CE1 . PHE   A 1 45 ? 2.628   -20.933 -5.377  1.00 29.01  ? 44  PHE   A CE1 1 
ATOM   352  C CE2 . PHE   A 1 45 ? 1.973   -20.889 -3.095  1.00 27.63  ? 44  PHE   A CE2 1 
ATOM   353  C CZ  . PHE   A 1 45 ? 1.681   -20.670 -4.418  1.00 27.77  ? 44  PHE   A CZ  1 
ATOM   354  N N   . PHE   A 1 46 ? 8.129   -20.893 -1.198  1.00 21.36  ? 45  PHE   A N   1 
ATOM   355  C CA  . PHE   A 1 46 ? 9.298   -21.355 -0.436  1.00 21.91  ? 45  PHE   A CA  1 
ATOM   356  C C   . PHE   A 1 46 ? 9.088   -22.805 0.020   1.00 23.93  ? 45  PHE   A C   1 
ATOM   357  O O   . PHE   A 1 46 ? 7.955   -23.263 0.165   1.00 25.51  ? 45  PHE   A O   1 
ATOM   358  C CB  . PHE   A 1 46 ? 9.509   -20.409 0.753   1.00 24.53  ? 45  PHE   A CB  1 
ATOM   359  C CG  . PHE   A 1 46 ? 9.980   -19.038 0.331   1.00 22.26  ? 45  PHE   A CG  1 
ATOM   360  C CD1 . PHE   A 1 46 ? 11.263  -18.891 -0.203  1.00 21.11  ? 45  PHE   A CD1 1 
ATOM   361  C CD2 . PHE   A 1 46 ? 9.248   -17.889 0.621   1.00 22.61  ? 45  PHE   A CD2 1 
ATOM   362  C CE1 . PHE   A 1 46 ? 11.702  -17.640 -0.610  1.00 20.38  ? 45  PHE   A CE1 1 
ATOM   363  C CE2 . PHE   A 1 46 ? 9.730   -16.628 0.256   1.00 20.04  ? 45  PHE   A CE2 1 
ATOM   364  C CZ  . PHE   A 1 46 ? 10.983  -16.502 -0.311  1.00 21.31  ? 45  PHE   A CZ  1 
ATOM   365  N N   . GLY   A 1 47 ? 10.188  -23.540 0.211   1.00 24.51  ? 46  GLY   A N   1 
ATOM   366  C CA  . GLY   A 1 47 ? 10.120  -24.909 0.720   1.00 23.69  ? 46  GLY   A CA  1 
ATOM   367  C C   . GLY   A 1 47 ? 9.879   -25.898 -0.436  1.00 30.58  ? 46  GLY   A C   1 
ATOM   368  O O   . GLY   A 1 47 ? 10.735  -26.720 -0.737  1.00 33.88  ? 46  GLY   A O   1 
ATOM   369  N N   . THR   A 1 48 ? 8.742   -25.794 -1.140  1.00 28.23  ? 47  THR   A N   1 
ATOM   370  C CA  . THR   A 1 48 ? 8.487   -26.663 -2.286  1.00 28.44  ? 47  THR   A CA  1 
ATOM   371  C C   . THR   A 1 48 ? 9.275   -26.184 -3.503  1.00 29.13  ? 47  THR   A C   1 
ATOM   372  O O   . THR   A 1 48 ? 9.554   -26.943 -4.453  1.00 29.20  ? 47  THR   A O   1 
ATOM   373  C CB  . THR   A 1 48 ? 6.988   -26.739 -2.602  1.00 32.57  ? 47  THR   A CB  1 
ATOM   374  O OG1 . THR   A 1 48 ? 6.540   -25.471 -3.080  1.00 30.66  ? 47  THR   A OG1 1 
ATOM   375  C CG2 . THR   A 1 48 ? 6.108   -27.225 -1.471  1.00 33.02  ? 47  THR   A CG2 1 
ATOM   376  N N   . HIS   A 1 49 ? 9.538   -24.866 -3.568  1.00 25.15  ? 48  HIS   A N   1 
ATOM   377  C CA  . HIS   A 1 49 ? 10.232  -24.282 -4.703  1.00 26.56  ? 48  HIS   A CA  1 
ATOM   378  C C   . HIS   A 1 49 ? 9.432   -24.393 -5.998  1.00 28.06  ? 48  HIS   A C   1 
ATOM   379  O O   . HIS   A 1 49 ? 10.018  -24.346 -7.072  1.00 30.04  ? 48  HIS   A O   1 
ATOM   380  C CB  . HIS   A 1 49 ? 11.694  -24.768 -4.834  1.00 26.17  ? 48  HIS   A CB  1 
ATOM   381  C CG  . HIS   A 1 49 ? 12.420  -24.787 -3.529  1.00 28.92  ? 48  HIS   A CG  1 
ATOM   382  N ND1 . HIS   A 1 49 ? 13.227  -25.836 -3.136  1.00 30.10  ? 48  HIS   A ND1 1 
ATOM   383  C CD2 . HIS   A 1 49 ? 12.467  -23.892 -2.522  1.00 25.90  ? 48  HIS   A CD2 1 
ATOM   384  C CE1 . HIS   A 1 49 ? 13.681  -25.608 -1.915  1.00 38.13  ? 48  HIS   A CE1 1 
ATOM   385  N NE2 . HIS   A 1 49 ? 13.283  -24.403 -1.537  1.00 30.03  ? 48  HIS   A NE2 1 
ATOM   386  N N   . GLU   A 1 50 ? 8.104   -24.497 -5.870  1.00 27.57  ? 49  GLU   A N   1 
ATOM   387  C CA  . GLU   A 1 50 ? 7.215   -24.510 -7.028  1.00 28.36  ? 49  GLU   A CA  1 
ATOM   388  C C   . GLU   A 1 50 ? 6.797   -23.095 -7.435  1.00 28.46  ? 49  GLU   A C   1 
ATOM   389  O O   . GLU   A 1 50 ? 6.931   -22.140 -6.659  1.00 27.01  ? 49  GLU   A O   1 
ATOM   390  C CB  . GLU   A 1 50 ? 5.932   -25.285 -6.762  1.00 29.42  ? 49  GLU   A CB  1 
ATOM   391  C CG  . GLU   A 1 50 ? 6.179   -26.723 -6.301  1.00 38.26  ? 49  GLU   A CG  1 
ATOM   392  C CD  . GLU   A 1 50 ? 4.979   -27.339 -5.609  1.00 48.15  ? 49  GLU   A CD  1 
ATOM   393  O OE1 . GLU   A 1 50 ? 4.313   -26.744 -4.738  1.00 47.14  ? 49  GLU   A OE1 1 
ATOM   394  O OE2 . GLU   A 1 50 ? 4.785   -28.512 -5.881  1.00 49.27  ? 49  GLU   A OE2 1 
ATOM   395  N N   . THR   A 1 51 ? 6.340   -22.930 -8.683  1.00 26.60  ? 50  THR   A N   1 
ATOM   396  C CA  . THR   A 1 51 ? 5.835   -21.655 -9.175  1.00 26.17  ? 50  THR   A CA  1 
ATOM   397  C C   . THR   A 1 51 ? 4.390   -21.867 -9.614  1.00 27.95  ? 50  THR   A C   1 
ATOM   398  O O   . THR   A 1 51 ? 4.087   -22.844 -10.321 1.00 30.63  ? 50  THR   A O   1 
ATOM   399  C CB  . THR   A 1 51 ? 6.640   -21.117 -10.361 1.00 31.19  ? 50  THR   A CB  1 
ATOM   400  O OG1 . THR   A 1 51 ? 7.959   -20.778 -9.933  1.00 29.59  ? 50  THR   A OG1 1 
ATOM   401  C CG2 . THR   A 1 51 ? 6.056   -19.847 -10.971 1.00 33.79  ? 50  THR   A CG2 1 
ATOM   402  N N   . ALA   A 1 52 ? 3.487   -20.954 -9.232  1.00 25.48  ? 51  ALA   A N   1 
ATOM   403  C CA  . ALA   A 1 52 ? 2.139   -20.838 -9.779  1.00 24.80  ? 51  ALA   A CA  1 
ATOM   404  C C   . ALA   A 1 52 ? 1.833   -19.380 -10.098 1.00 26.06  ? 51  ALA   A C   1 
ATOM   405  O O   . ALA   A 1 52 ? 2.508   -18.462 -9.622  1.00 27.04  ? 51  ALA   A O   1 
ATOM   406  C CB  . ALA   A 1 52 ? 1.134   -21.395 -8.778  1.00 27.39  ? 51  ALA   A CB  1 
ATOM   407  N N   . PHE   A 1 53 ? 0.798   -19.104 -10.911 1.00 24.30  ? 52  PHE   A N   1 
ATOM   408  C CA  . PHE   A 1 53 ? 0.448   -17.751 -11.269 1.00 24.08  ? 52  PHE   A CA  1 
ATOM   409  C C   . PHE   A 1 53 ? -0.840  -17.399 -10.543 1.00 28.08  ? 52  PHE   A C   1 
ATOM   410  O O   . PHE   A 1 53 ? -1.842  -18.131 -10.601 1.00 31.30  ? 52  PHE   A O   1 
ATOM   411  C CB  . PHE   A 1 53 ? 0.082   -17.761 -12.759 1.00 27.62  ? 52  PHE   A CB  1 
ATOM   412  C CG  . PHE   A 1 53 ? 1.262   -18.127 -13.626 1.00 30.18  ? 52  PHE   A CG  1 
ATOM   413  C CD1 . PHE   A 1 53 ? 2.436   -17.384 -13.564 1.00 33.29  ? 52  PHE   A CD1 1 
ATOM   414  C CD2 . PHE   A 1 53 ? 1.161   -19.164 -14.540 1.00 35.96  ? 52  PHE   A CD2 1 
ATOM   415  C CE1 . PHE   A 1 53 ? 3.531   -17.704 -14.364 1.00 42.76  ? 52  PHE   A CE1 1 
ATOM   416  C CE2 . PHE   A 1 53 ? 2.248   -19.463 -15.343 1.00 37.33  ? 52  PHE   A CE2 1 
ATOM   417  C CZ  . PHE   A 1 53 ? 3.421   -18.749 -15.260 1.00 33.91  ? 52  PHE   A CZ  1 
ATOM   418  N N   . LEU   A 1 54 ? -0.769  -16.322 -9.754  1.00 22.86  ? 53  LEU   A N   1 
ATOM   419  C CA  . LEU   A 1 54 ? -1.861  -15.968 -8.856  1.00 22.99  ? 53  LEU   A CA  1 
ATOM   420  C C   . LEU   A 1 54 ? -2.159  -14.483 -8.968  1.00 24.19  ? 53  LEU   A C   1 
ATOM   421  O O   . LEU   A 1 54 ? -1.305  -13.654 -9.308  1.00 23.95  ? 53  LEU   A O   1 
ATOM   422  C CB  . LEU   A 1 54 ? -1.516  -16.286 -7.392  1.00 25.61  ? 53  LEU   A CB  1 
ATOM   423  C CG  . LEU   A 1 54 ? -1.469  -17.772 -7.063  1.00 26.44  ? 53  LEU   A CG  1 
ATOM   424  C CD1 . LEU   A 1 54 ? -1.106  -17.899 -5.590  1.00 26.23  ? 53  LEU   A CD1 1 
ATOM   425  C CD2 . LEU   A 1 54 ? -2.889  -18.349 -7.290  1.00 32.58  ? 53  LEU   A CD2 1 
ATOM   426  N N   . GLY   A 1 55 ? -3.428  -14.137 -8.687  1.00 23.70  ? 54  GLY   A N   1 
ATOM   427  C CA  . GLY   A 1 55 ? -3.752  -12.733 -8.617  1.00 23.90  ? 54  GLY   A CA  1 
ATOM   428  C C   . GLY   A 1 55 ? -3.788  -12.258 -7.159  1.00 20.59  ? 54  GLY   A C   1 
ATOM   429  O O   . GLY   A 1 55 ? -3.719  -13.065 -6.224  1.00 21.82  ? 54  GLY   A O   1 
ATOM   430  N N   . PRO   A 1 56 ? -3.907  -10.934 -6.997  1.00 21.81  ? 55  PRO   A N   1 
ATOM   431  C CA  . PRO   A 1 56 ? -3.832  -10.297 -5.670  1.00 22.12  ? 55  PRO   A CA  1 
ATOM   432  C C   . PRO   A 1 56 ? -4.797  -10.822 -4.622  1.00 23.98  ? 55  PRO   A C   1 
ATOM   433  O O   . PRO   A 1 56 ? -4.510  -10.770 -3.426  1.00 22.22  ? 55  PRO   A O   1 
ATOM   434  C CB  . PRO   A 1 56 ? -4.070  -8.824  -5.963  1.00 23.05  ? 55  PRO   A CB  1 
ATOM   435  C CG  . PRO   A 1 56 ? -3.498  -8.670  -7.371  1.00 26.16  ? 55  PRO   A CG  1 
ATOM   436  C CD  . PRO   A 1 56 ? -3.889  -9.951  -8.098  1.00 25.17  ? 55  PRO   A CD  1 
ATOM   437  N N   . LYS   A 1 57 ? -5.941  -11.370 -5.094  1.00 24.59  ? 56  LYS   A N   1 
ATOM   438  C CA  . LYS   A 1 57 ? -6.898  -11.869 -4.107  1.00 22.09  ? 56  LYS   A CA  1 
ATOM   439  C C   . LYS   A 1 57 ? -6.362  -13.036 -3.268  1.00 22.79  ? 56  LYS   A C   1 
ATOM   440  O O   . LYS   A 1 57 ? -6.801  -13.278 -2.136  1.00 23.45  ? 56  LYS   A O   1 
ATOM   441  C CB  . LYS   A 1 57 ? -8.148  -12.373 -4.849  1.00 27.64  ? 56  LYS   A CB  1 
ATOM   442  C CG  . LYS   A 1 57 ? -8.026  -13.686 -5.565  1.00 30.17  ? 56  LYS   A CG  1 
ATOM   443  C CD  . LYS   A 1 57 ? -9.370  -14.093 -6.179  1.00 34.96  ? 56  LYS   A CD  1 
ATOM   444  C CE  . LYS   A 1 57 ? -9.320  -15.357 -6.957  1.00 40.08  ? 56  LYS   A CE  1 
ATOM   445  N NZ  . LYS   A 1 57 ? -8.942  -16.498 -6.124  1.00 46.70  ? 56  LYS   A NZ  1 
ATOM   446  N N   . ASP   A 1 58 ? -5.277  -13.712 -3.756  1.00 22.22  ? 57  ASP   A N   1 
ATOM   447  C CA  . ASP   A 1 58 ? -4.716  -14.851 -3.066  1.00 22.66  ? 57  ASP   A CA  1 
ATOM   448  C C   . ASP   A 1 58 ? -3.359  -14.498 -2.424  1.00 21.86  ? 57  ASP   A C   1 
ATOM   449  O O   . ASP   A 1 58 ? -2.692  -15.416 -1.948  1.00 23.51  ? 57  ASP   A O   1 
ATOM   450  C CB  . ASP   A 1 58 ? -4.628  -16.021 -4.044  1.00 24.50  ? 57  ASP   A CB  1 
ATOM   451  C CG  . ASP   A 1 58 ? -5.999  -16.584 -4.403  1.00 28.89  ? 57  ASP   A CG  1 
ATOM   452  O OD1 . ASP   A 1 58 ? -6.803  -16.686 -3.457  1.00 29.16  ? 57  ASP   A OD1 1 
ATOM   453  O OD2 . ASP   A 1 58 ? -6.217  -16.949 -5.564  1.00 31.14  ? 57  ASP   A OD2 1 
ATOM   454  N N   . LEU   A 1 59 ? -3.012  -13.194 -2.421  1.00 20.43  ? 58  LEU   A N   1 
ATOM   455  C CA  . LEU   A 1 59 ? -1.681  -12.745 -1.934  1.00 19.83  ? 58  LEU   A CA  1 
ATOM   456  C C   . LEU   A 1 59 ? -1.839  -11.881 -0.676  1.00 19.72  ? 58  LEU   A C   1 
ATOM   457  O O   . LEU   A 1 59 ? -2.442  -10.798 -0.705  1.00 21.49  ? 58  LEU   A O   1 
ATOM   458  C CB  . LEU   A 1 59 ? -0.929  -12.007 -3.043  1.00 21.33  ? 58  LEU   A CB  1 
ATOM   459  C CG  . LEU   A 1 59 ? -0.806  -12.826 -4.321  1.00 22.20  ? 58  LEU   A CG  1 
ATOM   460  C CD1 . LEU   A 1 59 ? -0.172  -11.951 -5.400  1.00 23.86  ? 58  LEU   A CD1 1 
ATOM   461  C CD2 . LEU   A 1 59 ? -0.019  -14.106 -4.190  1.00 23.46  ? 58  LEU   A CD2 1 
ATOM   462  N N   . PHE   A 1 60 ? -1.269  -12.402 0.424   1.00 20.52  ? 59  PHE   A N   1 
ATOM   463  C CA  . PHE   A 1 60 ? -1.343  -11.673 1.709   1.00 21.99  ? 59  PHE   A CA  1 
ATOM   464  C C   . PHE   A 1 60 ? 0.043   -11.170 2.110   1.00 23.73  ? 59  PHE   A C   1 
ATOM   465  O O   . PHE   A 1 60 ? 0.938   -11.978 2.298   1.00 23.46  ? 59  PHE   A O   1 
ATOM   466  C CB  . PHE   A 1 60 ? -1.820  -12.693 2.746   1.00 22.28  ? 59  PHE   A CB  1 
ATOM   467  C CG  . PHE   A 1 60 ? -3.259  -13.159 2.514   1.00 22.84  ? 59  PHE   A CG  1 
ATOM   468  C CD1 . PHE   A 1 60 ? -3.550  -14.056 1.502   1.00 24.07  ? 59  PHE   A CD1 1 
ATOM   469  C CD2 . PHE   A 1 60 ? -4.294  -12.595 3.268   1.00 25.66  ? 59  PHE   A CD2 1 
ATOM   470  C CE1 . PHE   A 1 60 ? -4.882  -14.429 1.237   1.00 26.00  ? 59  PHE   A CE1 1 
ATOM   471  C CE2 . PHE   A 1 60 ? -5.600  -12.977 2.969   1.00 23.76  ? 59  PHE   A CE2 1 
ATOM   472  C CZ  . PHE   A 1 60 ? -5.859  -13.887 2.006   1.00 23.77  ? 59  PHE   A CZ  1 
ATOM   473  N N   . PRO   A 1 61 ? 0.271   -9.858  2.271   1.00 25.28  ? 60  PRO   A N   1 
ATOM   474  C CA  . PRO   A 1 61 ? 1.627   -9.388  2.584   1.00 24.55  ? 60  PRO   A CA  1 
ATOM   475  C C   . PRO   A 1 61 ? 2.165   -10.026 3.860   1.00 22.76  ? 60  PRO   A C   1 
ATOM   476  O O   . PRO   A 1 61 ? 1.452   -10.208 4.863   1.00 24.51  ? 60  PRO   A O   1 
ATOM   477  C CB  . PRO   A 1 61 ? 1.427   -7.880  2.735   1.00 25.27  ? 60  PRO   A CB  1 
ATOM   478  C CG  . PRO   A 1 61 ? 0.280   -7.559  1.760   1.00 29.33  ? 60  PRO   A CG  1 
ATOM   479  C CD  . PRO   A 1 61 ? -0.652  -8.752  1.930   1.00 27.12  ? 60  PRO   A CD  1 
ATOM   480  N N   . TYR   A 1 62 ? 3.457   -10.438 3.819   1.00 23.68  ? 61  TYR   A N   1 
ATOM   481  C CA  . TYR   A 1 62 ? 4.002   -11.308 4.844   1.00 21.80  ? 61  TYR   A CA  1 
ATOM   482  C C   . TYR   A 1 62 ? 4.064   -10.646 6.235   1.00 22.70  ? 61  TYR   A C   1 
ATOM   483  O O   . TYR   A 1 62 ? 3.682   -11.330 7.200   1.00 26.28  ? 61  TYR   A O   1 
ATOM   484  C CB  . TYR   A 1 62 ? 5.401   -11.708 4.343   1.00 24.82  ? 61  TYR   A CB  1 
ATOM   485  C CG  . TYR   A 1 62 ? 6.203   -12.488 5.373   1.00 24.43  ? 61  TYR   A CG  1 
ATOM   486  C CD1 . TYR   A 1 62 ? 5.918   -13.824 5.671   1.00 24.57  ? 61  TYR   A CD1 1 
ATOM   487  C CD2 . TYR   A 1 62 ? 7.273   -11.878 6.025   1.00 26.55  ? 61  TYR   A CD2 1 
ATOM   488  C CE1 . TYR   A 1 62 ? 6.600   -14.569 6.644   1.00 26.48  ? 61  TYR   A CE1 1 
ATOM   489  C CE2 . TYR   A 1 62 ? 7.962   -12.628 6.970   1.00 25.14  ? 61  TYR   A CE2 1 
ATOM   490  C CZ  . TYR   A 1 62 ? 7.646   -13.932 7.283   1.00 25.99  ? 61  TYR   A CZ  1 
ATOM   491  O OH  . TYR   A 1 62 ? 8.405   -14.645 8.228   1.00 29.12  ? 61  TYR   A OH  1 
ATOM   492  N N   . ASP   A 1 63 ? 4.440   -9.365  6.263   1.00 26.71  ? 62  ASP   A N   1 
ATOM   493  C CA  . ASP   A 1 63 ? 4.615   -8.685  7.559   1.00 29.70  ? 62  ASP   A CA  1 
ATOM   494  C C   . ASP   A 1 63 ? 3.297   -8.672  8.323   1.00 28.86  ? 62  ASP   A C   1 
ATOM   495  O O   . ASP   A 1 63 ? 3.275   -9.174  9.448   1.00 36.67  ? 62  ASP   A O   1 
ATOM   496  C CB  . ASP   A 1 63 ? 5.321   -7.350  7.442   1.00 30.58  ? 62  ASP   A CB  1 
ATOM   497  N N   . LYS   A 1 64 ? 2.241   -8.227  7.630   1.00 30.19  ? 63  LYS   A N   1 
ATOM   498  C CA  . LYS   A 1 64 ? 0.891   -8.132  8.200   1.00 31.02  ? 63  LYS   A CA  1 
ATOM   499  C C   . LYS   A 1 64 ? 0.379   -9.493  8.648   1.00 31.76  ? 63  LYS   A C   1 
ATOM   500  O O   . LYS   A 1 64 ? -0.278  -9.592  9.680   1.00 30.87  ? 63  LYS   A O   1 
ATOM   501  C CB  . LYS   A 1 64 ? -0.037  -7.557  7.126   1.00 30.19  ? 63  LYS   A CB  1 
ATOM   502  C CG  . LYS   A 1 64 ? -1.507  -7.427  7.602   1.00 36.09  ? 63  LYS   A CG  1 
ATOM   503  C CD  . LYS   A 1 64 ? -2.285  -6.625  6.563   1.00 36.19  ? 63  LYS   A CD  1 
ATOM   504  C CE  . LYS   A 1 64 ? -3.383  -5.821  7.176   1.00 41.19  ? 63  LYS   A CE  1 
ATOM   505  N NZ  . LYS   A 1 64 ? -4.541  -6.619  7.559   1.00 49.56  ? 63  LYS   A NZ  1 
ATOM   506  N N   . SER   A 1 65 ? 0.688   -10.566 7.899   1.00 28.48  ? 64  SER   A N   1 
ATOM   507  C CA  . SER   A 1 65 ? 0.029   -11.863 8.000   1.00 27.31  ? 64  SER   A CA  1 
ATOM   508  C C   . SER   A 1 65 ? 0.790   -12.952 8.784   1.00 28.24  ? 64  SER   A C   1 
ATOM   509  O O   . SER   A 1 65 ? 0.224   -14.037 9.012   1.00 29.98  ? 64  SER   A O   1 
ATOM   510  C CB  . SER   A 1 65 ? -0.322  -12.404 6.634   1.00 32.25  ? 64  SER   A CB  1 
ATOM   511  O OG  . SER   A 1 65 ? -1.156  -11.466 5.959   1.00 37.21  ? 64  SER   A OG  1 
ATOM   512  N N   . LYS   A 1 66 ? 2.072   -12.707 9.143   1.00 28.06  ? 65  LYS   A N   1 
ATOM   513  C CA  . LYS   A 1 66 ? 2.894   -13.801 9.646   1.00 30.86  ? 65  LYS   A CA  1 
ATOM   514  C C   . LYS   A 1 66 ? 2.431   -14.314 11.002  1.00 29.36  ? 65  LYS   A C   1 
ATOM   515  O O   . LYS   A 1 66 ? 2.594   -15.498 11.304  1.00 32.83  ? 65  LYS   A O   1 
ATOM   516  C CB  . LYS   A 1 66 ? 4.379   -13.448 9.649   1.00 29.97  ? 65  LYS   A CB  1 
ATOM   517  C CG  . LYS   A 1 66 ? 4.675   -12.192 10.415  1.00 31.98  ? 65  LYS   A CG  1 
ATOM   518  C CD  . LYS   A 1 66 ? 6.162   -12.000 10.119  1.00 40.23  ? 65  LYS   A CD  1 
ATOM   519  C CE  . LYS   A 1 66 ? 6.761   -11.085 11.136  1.00 50.85  ? 65  LYS   A CE  1 
ATOM   520  N NZ  . LYS   A 1 66 ? 6.115   -9.772  11.033  1.00 56.37  ? 65  LYS   A NZ  1 
ATOM   521  N N   A ASP   A 1 67 ? 1.837   -13.425 11.806  0.50 33.15  ? 66  ASP   A N   1 
ATOM   522  N N   B ASP   A 1 67 ? 1.879   -13.416 11.824  0.50 31.91  ? 66  ASP   A N   1 
ATOM   523  C CA  A ASP   A 1 67 ? 1.345   -13.818 13.121  0.50 35.96  ? 66  ASP   A CA  1 
ATOM   524  C CA  B ASP   A 1 67 ? 1.335   -13.835 13.110  0.50 33.80  ? 66  ASP   A CA  1 
ATOM   525  C C   A ASP   A 1 67 ? 0.213   -14.840 13.001  0.50 34.04  ? 66  ASP   A C   1 
ATOM   526  C C   B ASP   A 1 67 ? 0.322   -14.955 12.895  0.50 32.02  ? 66  ASP   A C   1 
ATOM   527  O O   A ASP   A 1 67 ? 0.065   -15.709 13.850  0.50 35.94  ? 66  ASP   A O   1 
ATOM   528  O O   B ASP   A 1 67 ? 0.386   -16.000 13.544  0.50 32.57  ? 66  ASP   A O   1 
ATOM   529  C CB  A ASP   A 1 67 ? 1.026   -12.605 13.981  0.50 38.63  ? 66  ASP   A CB  1 
ATOM   530  C CB  B ASP   A 1 67 ? 0.705   -12.665 13.845  0.50 35.47  ? 66  ASP   A CB  1 
ATOM   531  C CG  A ASP   A 1 67 ? 2.227   -11.906 14.604  0.50 44.12  ? 66  ASP   A CG  1 
ATOM   532  C CG  B ASP   A 1 67 ? 0.241   -12.950 15.268  0.50 38.38  ? 66  ASP   A CG  1 
ATOM   533  O OD1 A ASP   A 1 67 ? 3.345   -12.456 14.508  0.50 44.71  ? 66  ASP   A OD1 1 
ATOM   534  O OD1 B ASP   A 1 67 ? 1.112   -13.098 16.152  0.50 42.56  ? 66  ASP   A OD1 1 
ATOM   535  O OD2 A ASP   A 1 67 ? 2.037   -10.814 15.184  0.50 44.90  ? 66  ASP   A OD2 1 
ATOM   536  O OD2 B ASP   A 1 67 ? -0.988  -13.007 15.481  0.50 42.82  ? 66  ASP   A OD2 1 
ATOM   537  N N   . LYS   A 1 68 ? -0.592  -14.747 11.937  1.00 31.19  ? 67  LYS   A N   1 
ATOM   538  C CA  . LYS   A 1 68 ? -1.662  -15.686 11.699  1.00 29.74  ? 67  LYS   A CA  1 
ATOM   539  C C   . LYS   A 1 68 ? -1.184  -16.921 10.957  1.00 31.34  ? 67  LYS   A C   1 
ATOM   540  O O   . LYS   A 1 68 ? -1.609  -18.031 11.277  1.00 37.05  ? 67  LYS   A O   1 
ATOM   541  C CB  . LYS   A 1 68 ? -2.733  -14.932 10.915  1.00 31.29  ? 67  LYS   A CB  1 
ATOM   542  C CG  . LYS   A 1 68 ? -3.993  -15.709 10.688  1.00 32.37  ? 67  LYS   A CG  1 
ATOM   543  C CD  . LYS   A 1 68 ? -4.994  -14.787 9.973   1.00 40.00  ? 67  LYS   A CD  1 
ATOM   544  C CE  . LYS   A 1 68 ? -6.390  -15.348 9.948   1.00 45.47  ? 67  LYS   A CE  1 
ATOM   545  N NZ  . LYS   A 1 68 ? -7.276  -14.457 9.182   1.00 47.60  ? 67  LYS   A NZ  1 
ATOM   546  N N   . TYR   A 1 69 ? -0.339  -16.746 9.925   1.00 29.37  ? 68  TYR   A N   1 
ATOM   547  C CA  . TYR   A 1 69 ? -0.151  -17.844 8.992   1.00 26.52  ? 68  TYR   A CA  1 
ATOM   548  C C   . TYR   A 1 69 ? 1.244   -18.477 9.118   1.00 26.22  ? 68  TYR   A C   1 
ATOM   549  O O   . TYR   A 1 69 ? 1.480   -19.532 8.549   1.00 29.30  ? 68  TYR   A O   1 
ATOM   550  C CB  . TYR   A 1 69 ? -0.309  -17.309 7.556   1.00 24.60  ? 68  TYR   A CB  1 
ATOM   551  C CG  . TYR   A 1 69 ? -1.702  -16.861 7.155   1.00 27.95  ? 68  TYR   A CG  1 
ATOM   552  C CD1 . TYR   A 1 69 ? -2.837  -17.606 7.499   1.00 28.09  ? 68  TYR   A CD1 1 
ATOM   553  C CD2 . TYR   A 1 69 ? -1.865  -15.687 6.424   1.00 27.37  ? 68  TYR   A CD2 1 
ATOM   554  C CE1 . TYR   A 1 69 ? -4.107  -17.167 7.152   1.00 31.04  ? 68  TYR   A CE1 1 
ATOM   555  C CE2 . TYR   A 1 69 ? -3.134  -15.240 6.068   1.00 29.19  ? 68  TYR   A CE2 1 
ATOM   556  C CZ  . TYR   A 1 69 ? -4.247  -15.991 6.424   1.00 31.18  ? 68  TYR   A CZ  1 
ATOM   557  O OH  . TYR   A 1 69 ? -5.495  -15.603 6.021   1.00 31.92  ? 68  TYR   A OH  1 
ATOM   558  N N   . GLY   A 1 70 ? 2.135   -17.872 9.912   1.00 28.00  ? 69  GLY   A N   1 
ATOM   559  C CA  . GLY   A 1 70 ? 3.521   -18.327 9.983   1.00 27.82  ? 69  GLY   A CA  1 
ATOM   560  C C   . GLY   A 1 70 ? 3.756   -19.305 11.142  1.00 30.30  ? 69  GLY   A C   1 
ATOM   561  O O   . GLY   A 1 70 ? 4.628   -19.065 11.943  1.00 40.50  ? 69  GLY   A O   1 
ATOM   562  N N   . LYS   A 1 71 ? 2.939   -20.344 11.234  1.00 35.80  ? 70  LYS   A N   1 
ATOM   563  C CA  . LYS   A 1 71 ? 3.153   -21.368 12.246  1.00 37.16  ? 70  LYS   A CA  1 
ATOM   564  C C   . LYS   A 1 71 ? 3.454   -22.679 11.533  1.00 32.64  ? 70  LYS   A C   1 
ATOM   565  O O   . LYS   A 1 71 ? 3.059   -22.916 10.407  1.00 34.41  ? 70  LYS   A O   1 
ATOM   566  C CB  . LYS   A 1 71 ? 1.934   -21.448 13.169  1.00 42.02  ? 70  LYS   A CB  1 
ATOM   567  C CG  . LYS   A 1 71 ? 1.629   -20.126 13.848  1.00 42.87  ? 70  LYS   A CG  1 
ATOM   568  C CD  . LYS   A 1 71 ? 0.794   -20.205 15.119  1.00 47.43  ? 70  LYS   A CD  1 
ATOM   569  N N   . PRO   A 1 72 ? 4.217   -23.616 12.141  1.00 36.44  ? 71  PRO   A N   1 
ATOM   570  C CA  . PRO   A 1 72 ? 4.463   -24.897 11.470  1.00 34.00  ? 71  PRO   A CA  1 
ATOM   571  C C   . PRO   A 1 72 ? 3.230   -25.663 11.018  1.00 33.49  ? 71  PRO   A C   1 
ATOM   572  O O   . PRO   A 1 72 ? 2.190   -25.591 11.660  1.00 41.14  ? 71  PRO   A O   1 
ATOM   573  C CB  . PRO   A 1 72 ? 5.285   -25.668 12.542  1.00 38.03  ? 71  PRO   A CB  1 
ATOM   574  C CG  . PRO   A 1 72 ? 5.952   -24.588 13.351  1.00 42.76  ? 71  PRO   A CG  1 
ATOM   575  C CD  . PRO   A 1 72 ? 4.880   -23.478 13.444  1.00 42.51  ? 71  PRO   A CD  1 
ATOM   576  N N   . ASN   A 1 73 ? 3.360   -26.401 9.927   1.00 34.61  ? 72  ASN   A N   1 
ATOM   577  C CA  . ASN   A 1 73 ? 2.275   -27.127 9.297   1.00 41.77  ? 72  ASN   A CA  1 
ATOM   578  C C   . ASN   A 1 73 ? 2.866   -28.467 8.892   1.00 48.11  ? 72  ASN   A C   1 
ATOM   579  O O   . ASN   A 1 73 ? 4.059   -28.571 8.627   1.00 50.06  ? 72  ASN   A O   1 
ATOM   580  C CB  . ASN   A 1 73 ? 1.807   -26.357 8.059   1.00 41.65  ? 72  ASN   A CB  1 
ATOM   581  C CG  . ASN   A 1 73 ? 0.449   -26.749 7.526   1.00 53.17  ? 72  ASN   A CG  1 
ATOM   582  O OD1 . ASN   A 1 73 ? 0.326   -27.692 6.739   1.00 48.99  ? 72  ASN   A OD1 1 
ATOM   583  N ND2 . ASN   A 1 73 ? -0.575  -25.970 7.847   1.00 53.25  ? 72  ASN   A ND2 1 
ATOM   584  N N   . LYS   A 1 74 ? 2.022   -29.491 8.854   1.00 47.02  ? 73  LYS   A N   1 
ATOM   585  C CA  . LYS   A 1 74 ? 2.495   -30.833 8.607   1.00 45.20  ? 73  LYS   A CA  1 
ATOM   586  C C   . LYS   A 1 74 ? 2.799   -31.014 7.120   1.00 42.88  ? 73  LYS   A C   1 
ATOM   587  O O   . LYS   A 1 74 ? 3.412   -32.007 6.720   1.00 40.62  ? 73  LYS   A O   1 
ATOM   588  C CB  . LYS   A 1 74 ? 1.410   -31.758 9.193   1.00 49.70  ? 73  LYS   A CB  1 
ATOM   589  C CG  . LYS   A 1 74 ? 0.162   -31.962 8.330   1.00 54.89  ? 73  LYS   A CG  1 
ATOM   590  N N   . ARG   A 1 75 ? 2.376   -30.062 6.279   1.00 39.12  ? 74  ARG   A N   1 
ATOM   591  C CA  . ARG   A 1 75 ? 2.452   -30.295 4.849   1.00 38.17  ? 74  ARG   A CA  1 
ATOM   592  C C   . ARG   A 1 75 ? 3.895   -30.258 4.347   1.00 35.82  ? 74  ARG   A C   1 
ATOM   593  O O   . ARG   A 1 75 ? 4.712   -29.497 4.861   1.00 33.54  ? 74  ARG   A O   1 
ATOM   594  C CB  . ARG   A 1 75 ? 1.559   -29.309 4.086   1.00 39.58  ? 74  ARG   A CB  1 
ATOM   595  C CG  . ARG   A 1 75 ? 0.099   -29.560 4.423   1.00 49.21  ? 74  ARG   A CG  1 
ATOM   596  C CD  . ARG   A 1 75 ? -0.502  -30.683 3.596   1.00 47.15  ? 74  ARG   A CD  1 
ATOM   597  N NE  . ARG   A 1 75 ? -1.284  -30.160 2.473   1.00 57.49  ? 74  ARG   A NE  1 
ATOM   598  C CZ  . ARG   A 1 75 ? -2.427  -29.475 2.600   1.00 55.08  ? 74  ARG   A CZ  1 
ATOM   599  N NH1 . ARG   A 1 75 ? -3.110  -29.142 1.515   1.00 59.65  ? 74  ARG   A NH1 1 
ATOM   600  N NH2 . ARG   A 1 75 ? -2.906  -29.167 3.801   1.00 61.88  ? 74  ARG   A NH2 1 
ATOM   601  N N   . LYS   A 1 76 ? 4.163   -31.084 3.327   1.00 35.10  ? 75  LYS   A N   1 
ATOM   602  C CA  . LYS   A 1 76 ? 5.482   -31.256 2.744   1.00 35.57  ? 75  LYS   A CA  1 
ATOM   603  C C   . LYS   A 1 76 ? 6.039   -29.904 2.300   1.00 34.24  ? 75  LYS   A C   1 
ATOM   604  O O   . LYS   A 1 76 ? 5.438   -29.223 1.465   1.00 32.36  ? 75  LYS   A O   1 
ATOM   605  C CB  . LYS   A 1 76 ? 5.458   -32.251 1.583   1.00 39.95  ? 75  LYS   A CB  1 
ATOM   606  C CG  . LYS   A 1 76 ? 6.797   -32.504 0.955   1.00 44.72  ? 75  LYS   A CG  1 
ATOM   607  C CD  . LYS   A 1 76 ? 6.739   -33.472 -0.217  1.00 46.99  ? 75  LYS   A CD  1 
ATOM   608  C CE  . LYS   A 1 76 ? 8.117   -33.593 -0.783  1.00 49.72  ? 75  LYS   A CE  1 
ATOM   609  N N   . GLY   A 1 77 ? 7.219   -29.576 2.829   1.00 34.46  ? 76  GLY   A N   1 
ATOM   610  C CA  . GLY   A 1 77 ? 7.927   -28.377 2.407   1.00 30.49  ? 76  GLY   A CA  1 
ATOM   611  C C   . GLY   A 1 77 ? 7.591   -27.142 3.237   1.00 29.65  ? 76  GLY   A C   1 
ATOM   612  O O   . GLY   A 1 77 ? 8.295   -26.138 3.097   1.00 29.92  ? 76  GLY   A O   1 
ATOM   613  N N   . PHE   A 1 78 ? 6.511   -27.178 4.018   1.00 29.73  ? 77  PHE   A N   1 
ATOM   614  C CA  . PHE   A 1 78 ? 6.034   -25.957 4.634   1.00 26.13  ? 77  PHE   A CA  1 
ATOM   615  C C   . PHE   A 1 78 ? 7.051   -25.370 5.626   1.00 28.90  ? 77  PHE   A C   1 
ATOM   616  O O   . PHE   A 1 78 ? 7.320   -24.163 5.652   1.00 28.53  ? 77  PHE   A O   1 
ATOM   617  C CB  . PHE   A 1 78 ? 4.657   -26.217 5.254   1.00 28.77  ? 77  PHE   A CB  1 
ATOM   618  C CG  . PHE   A 1 78 ? 3.957   -24.929 5.657   1.00 30.25  ? 77  PHE   A CG  1 
ATOM   619  C CD1 . PHE   A 1 78 ? 4.232   -24.287 6.865   1.00 31.96  ? 77  PHE   A CD1 1 
ATOM   620  C CD2 . PHE   A 1 78 ? 3.013   -24.355 4.792   1.00 31.08  ? 77  PHE   A CD2 1 
ATOM   621  C CE1 . PHE   A 1 78 ? 3.601   -23.099 7.205   1.00 30.70  ? 77  PHE   A CE1 1 
ATOM   622  C CE2 . PHE   A 1 78 ? 2.358   -23.174 5.148   1.00 28.06  ? 77  PHE   A CE2 1 
ATOM   623  C CZ  . PHE   A 1 78 ? 2.643   -22.542 6.334   1.00 27.96  ? 77  PHE   A CZ  1 
ATOM   624  N N   . ASN   A 1 79 ? 7.582   -26.209 6.533   1.00 28.28  ? 78  ASN   A N   1 
ATOM   625  C CA  . ASN   A 1 79 ? 8.461   -25.686 7.570   1.00 25.62  ? 78  ASN   A CA  1 
ATOM   626  C C   . ASN   A 1 79 ? 9.820   -25.258 6.964   1.00 24.62  ? 78  ASN   A C   1 
ATOM   627  O O   . ASN   A 1 79 ? 10.396  -24.259 7.441   1.00 27.80  ? 78  ASN   A O   1 
ATOM   628  C CB  . ASN   A 1 79 ? 8.609   -26.735 8.684   1.00 29.49  ? 78  ASN   A CB  1 
ATOM   629  C CG  . ASN   A 1 79 ? 7.265   -26.999 9.322   1.00 33.55  ? 78  ASN   A CG  1 
ATOM   630  O OD1 . ASN   A 1 79 ? 6.404   -26.110 9.326   1.00 31.68  ? 78  ASN   A OD1 1 
ATOM   631  N ND2 . ASN   A 1 79 ? 7.090   -28.179 9.931   1.00 30.85  ? 78  ASN   A ND2 1 
ATOM   632  N N   . GLU   A 1 80 ? 10.281  -25.920 5.890   1.00 25.58  ? 79  GLU   A N   1 
ATOM   633  C CA  . GLU   A 1 80 ? 11.460  -25.456 5.170   1.00 24.80  ? 79  GLU   A CA  1 
ATOM   634  C C   . GLU   A 1 80 ? 11.136  -24.068 4.608   1.00 26.21  ? 79  GLU   A C   1 
ATOM   635  O O   . GLU   A 1 80 ? 11.956  -23.142 4.632   1.00 24.65  ? 79  GLU   A O   1 
ATOM   636  C CB  . GLU   A 1 80 ? 11.907  -26.356 4.005   1.00 27.59  ? 79  GLU   A CB  1 
ATOM   637  C CG  . GLU   A 1 80 ? 13.210  -25.918 3.326   1.00 28.39  ? 79  GLU   A CG  1 
ATOM   638  C CD  . GLU   A 1 80 ? 13.691  -27.002 2.369   1.00 38.70  ? 79  GLU   A CD  1 
ATOM   639  O OE1 . GLU   A 1 80 ? 13.067  -28.090 2.263   1.00 46.34  ? 79  GLU   A OE1 1 
ATOM   640  O OE2 . GLU   A 1 80 ? 14.728  -26.777 1.742   1.00 37.58  ? 79  GLU   A OE2 1 
ATOM   641  N N   . GLY   A 1 81 ? 9.928   -23.929 4.052   1.00 25.68  ? 80  GLY   A N   1 
ATOM   642  C CA  . GLY   A 1 81 ? 9.552   -22.621 3.509   1.00 26.22  ? 80  GLY   A CA  1 
ATOM   643  C C   . GLY   A 1 81 ? 9.495   -21.525 4.580   1.00 22.11  ? 80  GLY   A C   1 
ATOM   644  O O   . GLY   A 1 81 ? 9.837   -20.372 4.290   1.00 22.97  ? 80  GLY   A O   1 
ATOM   645  N N   . LEU   A 1 82 ? 9.025   -21.814 5.810   1.00 23.50  ? 81  LEU   A N   1 
ATOM   646  C CA  . LEU   A 1 82 ? 9.063   -20.815 6.866   1.00 23.21  ? 81  LEU   A CA  1 
ATOM   647  C C   . LEU   A 1 82 ? 10.493  -20.342 7.159   1.00 24.15  ? 81  LEU   A C   1 
ATOM   648  O O   . LEU   A 1 82 ? 10.713  -19.140 7.397   1.00 23.41  ? 81  LEU   A O   1 
ATOM   649  C CB  . LEU   A 1 82 ? 8.389   -21.275 8.159   1.00 26.64  ? 81  LEU   A CB  1 
ATOM   650  C CG  . LEU   A 1 82 ? 6.895   -21.594 8.060   1.00 28.43  ? 81  LEU   A CG  1 
ATOM   651  C CD1 . LEU   A 1 82 ? 6.544   -22.144 9.437   1.00 29.76  ? 81  LEU   A CD1 1 
ATOM   652  C CD2 . LEU   A 1 82 ? 6.103   -20.323 7.837   1.00 28.44  ? 81  LEU   A CD2 1 
ATOM   653  N N   . TRP   A 1 83 ? 11.475  -21.275 7.103   1.00 24.51  ? 82  TRP   A N   1 
ATOM   654  C CA  . TRP   A 1 83 ? 12.856  -20.892 7.356   1.00 24.81  ? 82  TRP   A CA  1 
ATOM   655  C C   . TRP   A 1 83 ? 13.310  -19.963 6.232   1.00 23.10  ? 82  TRP   A C   1 
ATOM   656  O O   . TRP   A 1 83 ? 14.007  -18.990 6.496   1.00 23.20  ? 82  TRP   A O   1 
ATOM   657  C CB  . TRP   A 1 83 ? 13.764  -22.151 7.476   1.00 26.51  ? 82  TRP   A CB  1 
ATOM   658  C CG  . TRP   A 1 83 ? 15.210  -21.801 7.765   1.00 25.75  ? 82  TRP   A CG  1 
ATOM   659  C CD1 . TRP   A 1 83 ? 15.846  -21.691 8.976   1.00 28.28  ? 82  TRP   A CD1 1 
ATOM   660  C CD2 . TRP   A 1 83 ? 16.183  -21.470 6.760   1.00 24.55  ? 82  TRP   A CD2 1 
ATOM   661  N NE1 . TRP   A 1 83 ? 17.154  -21.330 8.779   1.00 29.04  ? 82  TRP   A NE1 1 
ATOM   662  C CE2 . TRP   A 1 83 ? 17.385  -21.193 7.435   1.00 28.23  ? 82  TRP   A CE2 1 
ATOM   663  C CE3 . TRP   A 1 83 ? 16.154  -21.410 5.354   1.00 27.54  ? 82  TRP   A CE3 1 
ATOM   664  C CZ2 . TRP   A 1 83 ? 18.541  -20.842 6.741   1.00 27.56  ? 82  TRP   A CZ2 1 
ATOM   665  C CZ3 . TRP   A 1 83 ? 17.300  -21.060 4.664   1.00 27.02  ? 82  TRP   A CZ3 1 
ATOM   666  C CH2 . TRP   A 1 83 ? 18.488  -20.809 5.361   1.00 28.60  ? 82  TRP   A CH2 1 
ATOM   667  N N   . GLU   A 1 84 ? 13.012  -20.350 4.984   1.00 22.35  ? 83  GLU   A N   1 
ATOM   668  C CA  . GLU   A 1 84 ? 13.489  -19.596 3.830   1.00 21.69  ? 83  GLU   A CA  1 
ATOM   669  C C   . GLU   A 1 84 ? 12.983  -18.151 3.854   1.00 22.33  ? 83  GLU   A C   1 
ATOM   670  O O   . GLU   A 1 84 ? 13.749  -17.222 3.647   1.00 21.80  ? 83  GLU   A O   1 
ATOM   671  C CB  . GLU   A 1 84 ? 13.075  -20.267 2.531   1.00 21.64  ? 83  GLU   A CB  1 
ATOM   672  C CG  . GLU   A 1 84 ? 13.821  -21.590 2.402   1.00 24.22  ? 83  GLU   A CG  1 
ATOM   673  C CD  . GLU   A 1 84 ? 13.432  -22.350 1.145   1.00 27.57  ? 83  GLU   A CD  1 
ATOM   674  O OE1 . GLU   A 1 84 ? 12.514  -21.900 0.446   1.00 25.89  ? 83  GLU   A OE1 1 
ATOM   675  O OE2 . GLU   A 1 84 ? 13.995  -23.454 0.858   1.00 26.72  ? 83  GLU   A OE2 1 
ATOM   676  N N   . ILE   A 1 85 ? 11.664  -17.967 4.101   1.00 22.02  ? 84  ILE   A N   1 
ATOM   677  C CA  . ILE   A 1 85 ? 11.094  -16.625 3.980   1.00 20.77  ? 84  ILE   A CA  1 
ATOM   678  C C   . ILE   A 1 85 ? 11.640  -15.738 5.114   1.00 21.76  ? 84  ILE   A C   1 
ATOM   679  O O   . ILE   A 1 85 ? 11.802  -14.543 4.942   1.00 23.32  ? 84  ILE   A O   1 
ATOM   680  C CB  . ILE   A 1 85 ? 9.539   -16.682 3.971   1.00 20.64  ? 84  ILE   A CB  1 
ATOM   681  C CG1 . ILE   A 1 85 ? 8.954   -15.322 3.568   1.00 20.64  ? 84  ILE   A CG1 1 
ATOM   682  C CG2 . ILE   A 1 85 ? 9.012   -17.058 5.371   1.00 22.94  ? 84  ILE   A CG2 1 
ATOM   683  C CD1 . ILE   A 1 85 ? 7.510   -15.419 3.068   1.00 19.48  ? 84  ILE   A CD1 1 
ATOM   684  N N   . GLN   A 1 86 ? 11.960  -16.348 6.267   1.00 21.41  ? 85  GLN   A N   1 
ATOM   685  C CA  . GLN   A 1 86 ? 12.498  -15.566 7.404   1.00 24.03  ? 85  GLN   A CA  1 
ATOM   686  C C   . GLN   A 1 86 ? 13.998  -15.277 7.264   1.00 25.41  ? 85  GLN   A C   1 
ATOM   687  O O   . GLN   A 1 86 ? 14.457  -14.167 7.679   1.00 27.20  ? 85  GLN   A O   1 
ATOM   688  C CB  . GLN   A 1 86 ? 12.259  -16.335 8.710   1.00 24.90  ? 85  GLN   A CB  1 
ATOM   689  C CG  . GLN   A 1 86 ? 12.696  -15.587 9.963   1.00 31.98  ? 85  GLN   A CG  1 
ATOM   690  C CD  . GLN   A 1 86 ? 12.067  -16.178 11.223  1.00 35.21  ? 85  GLN   A CD  1 
ATOM   691  O OE1 . GLN   A 1 86 ? 11.740  -17.377 11.295  1.00 36.26  ? 85  GLN   A OE1 1 
ATOM   692  N NE2 . GLN   A 1 86 ? 11.837  -15.317 12.210  1.00 44.09  ? 85  GLN   A NE2 1 
ATOM   693  N N   . ASN   A 1 87 ? 14.744  -16.251 6.733   1.00 22.75  ? 86  ASN   A N   1 
ATOM   694  C CA  . ASN   A 1 87 ? 16.197  -16.237 6.821   1.00 22.73  ? 86  ASN   A CA  1 
ATOM   695  C C   . ASN   A 1 87 ? 16.924  -15.911 5.525   1.00 25.14  ? 86  ASN   A C   1 
ATOM   696  O O   . ASN   A 1 87 ? 18.029  -15.360 5.579   1.00 26.26  ? 86  ASN   A O   1 
ATOM   697  C CB  . ASN   A 1 87 ? 16.717  -17.534 7.433   1.00 25.10  ? 86  ASN   A CB  1 
ATOM   698  C CG  . ASN   A 1 87 ? 16.285  -17.616 8.880   1.00 30.59  ? 86  ASN   A CG  1 
ATOM   699  O OD1 . ASN   A 1 87 ? 16.629  -16.727 9.681   1.00 32.17  ? 86  ASN   A OD1 1 
ATOM   700  N ND2 . ASN   A 1 87 ? 15.353  -18.505 9.179   1.00 28.22  ? 86  ASN   A ND2 1 
ATOM   701  N N   . ASN   A 1 88 ? 16.363  -16.267 4.362   1.00 21.96  ? 87  ASN   A N   1 
ATOM   702  C CA  . ASN   A 1 88 ? 17.025  -15.880 3.132   1.00 22.21  ? 87  ASN   A CA  1 
ATOM   703  C C   . ASN   A 1 88 ? 15.987  -15.810 2.009   1.00 23.81  ? 87  ASN   A C   1 
ATOM   704  O O   . ASN   A 1 88 ? 16.023  -16.575 1.032   1.00 22.35  ? 87  ASN   A O   1 
ATOM   705  C CB  . ASN   A 1 88 ? 18.193  -16.818 2.801   1.00 23.11  ? 87  ASN   A CB  1 
ATOM   706  C CG  . ASN   A 1 88 ? 19.233  -16.193 1.904   1.00 26.06  ? 87  ASN   A CG  1 
ATOM   707  O OD1 . ASN   A 1 88 ? 18.987  -15.224 1.180   1.00 23.53  ? 87  ASN   A OD1 1 
ATOM   708  N ND2 . ASN   A 1 88 ? 20.453  -16.731 1.889   1.00 29.55  ? 87  ASN   A ND2 1 
ATOM   709  N N   . PRO   A 1 89 ? 15.042  -14.842 2.102   1.00 22.98  ? 88  PRO   A N   1 
ATOM   710  C CA  . PRO   A 1 89 ? 13.902  -14.827 1.188   1.00 20.78  ? 88  PRO   A CA  1 
ATOM   711  C C   . PRO   A 1 89 ? 14.265  -14.396 -0.222  1.00 24.30  ? 88  PRO   A C   1 
ATOM   712  O O   . PRO   A 1 89 ? 13.464  -14.631 -1.127  1.00 22.36  ? 88  PRO   A O   1 
ATOM   713  C CB  . PRO   A 1 89 ? 12.985  -13.808 1.837   1.00 22.81  ? 88  PRO   A CB  1 
ATOM   714  C CG  . PRO   A 1 89 ? 13.930  -12.860 2.546   1.00 22.99  ? 88  PRO   A CG  1 
ATOM   715  C CD  . PRO   A 1 89 ? 14.935  -13.815 3.152   1.00 22.12  ? 88  PRO   A CD  1 
ATOM   716  N N   . HIS   A 1 90 ? 15.490  -13.868 -0.433  1.00 20.16  ? 89  HIS   A N   1 
ATOM   717  C CA  . HIS   A 1 90 ? 15.831  -13.342 -1.748  1.00 21.25  ? 89  HIS   A CA  1 
ATOM   718  C C   . HIS   A 1 90 ? 16.949  -14.138 -2.443  1.00 22.20  ? 89  HIS   A C   1 
ATOM   719  O O   . HIS   A 1 90 ? 17.410  -13.710 -3.511  1.00 23.09  ? 89  HIS   A O   1 
ATOM   720  C CB  . HIS   A 1 90 ? 16.227  -11.859 -1.649  1.00 21.51  ? 89  HIS   A CB  1 
ATOM   721  C CG  . HIS   A 1 90 ? 15.165  -10.981 -1.078  1.00 20.93  ? 89  HIS   A CG  1 
ATOM   722  N ND1 . HIS   A 1 90 ? 13.915  -10.917 -1.685  1.00 21.09  ? 89  HIS   A ND1 1 
ATOM   723  C CD2 . HIS   A 1 90 ? 15.097  -10.247 0.024   1.00 20.91  ? 89  HIS   A CD2 1 
ATOM   724  C CE1 . HIS   A 1 90 ? 13.148  -10.063 -1.004  1.00 20.49  ? 89  HIS   A CE1 1 
ATOM   725  N NE2 . HIS   A 1 90 ? 13.842  -9.678  0.073   1.00 22.46  ? 89  HIS   A NE2 1 
ATOM   726  N N   . ALA   A 1 91 ? 17.206  -15.327 -1.925  1.00 23.08  ? 90  ALA   A N   1 
ATOM   727  C CA  . ALA   A 1 91 ? 18.274  -16.159 -2.501  1.00 24.10  ? 90  ALA   A CA  1 
ATOM   728  C C   . ALA   A 1 91 ? 17.799  -16.888 -3.746  1.00 28.92  ? 90  ALA   A C   1 
ATOM   729  O O   . ALA   A 1 91 ? 16.615  -17.008 -4.035  1.00 26.05  ? 90  ALA   A O   1 
ATOM   730  C CB  . ALA   A 1 91 ? 18.726  -17.146 -1.461  1.00 24.15  ? 90  ALA   A CB  1 
ATOM   731  N N   . SER   A 1 92 ? 18.772  -17.408 -4.491  1.00 26.45  ? 91  SER   A N   1 
ATOM   732  C CA  . SER   A 1 92 ? 18.475  -18.346 -5.561  1.00 28.96  ? 91  SER   A CA  1 
ATOM   733  C C   . SER   A 1 92 ? 18.224  -19.725 -4.977  1.00 30.42  ? 91  SER   A C   1 
ATOM   734  O O   . SER   A 1 92 ? 19.061  -20.242 -4.223  1.00 32.86  ? 91  SER   A O   1 
ATOM   735  C CB  . SER   A 1 92 ? 19.635  -18.345 -6.503  1.00 32.51  ? 91  SER   A CB  1 
ATOM   736  O OG  . SER   A 1 92 ? 19.476  -19.441 -7.381  1.00 38.77  ? 91  SER   A OG  1 
ATOM   737  N N   . TYR   A 1 93 ? 17.072  -20.312 -5.338  1.00 28.54  ? 92  TYR   A N   1 
ATOM   738  C CA  . TYR   A 1 93 ? 16.709  -21.642 -4.896  1.00 30.12  ? 92  TYR   A CA  1 
ATOM   739  C C   . TYR   A 1 93 ? 16.546  -22.546 -6.107  1.00 34.68  ? 92  TYR   A C   1 
ATOM   740  O O   . TYR   A 1 93 ? 15.951  -23.602 -5.975  1.00 43.67  ? 92  TYR   A O   1 
ATOM   741  C CB  . TYR   A 1 93 ? 15.357  -21.563 -4.160  1.00 28.84  ? 92  TYR   A CB  1 
ATOM   742  C CG  . TYR   A 1 93 ? 15.512  -20.959 -2.774  1.00 27.66  ? 92  TYR   A CG  1 
ATOM   743  C CD1 . TYR   A 1 93 ? 15.923  -21.734 -1.680  1.00 29.02  ? 92  TYR   A CD1 1 
ATOM   744  C CD2 . TYR   A 1 93 ? 15.202  -19.608 -2.551  1.00 27.20  ? 92  TYR   A CD2 1 
ATOM   745  C CE1 . TYR   A 1 93 ? 16.069  -21.171 -0.416  1.00 30.46  ? 92  TYR   A CE1 1 
ATOM   746  C CE2 . TYR   A 1 93 ? 15.337  -19.051 -1.290  1.00 29.25  ? 92  TYR   A CE2 1 
ATOM   747  C CZ  . TYR   A 1 93 ? 15.766  -19.828 -0.226  1.00 26.30  ? 92  TYR   A CZ  1 
ATOM   748  O OH  . TYR   A 1 93 ? 15.988  -19.322 1.028   1.00 28.14  ? 92  TYR   A OH  1 
ATOM   749  N N   . SER   A 1 94 ? 17.048  -22.091 -7.256  1.00 43.80  ? 93  SER   A N   1 
ATOM   750  C CA  . SER   A 1 94 ? 17.296  -22.953 -8.400  1.00 58.19  ? 93  SER   A CA  1 
ATOM   751  C C   . SER   A 1 94 ? 18.444  -23.910 -8.044  1.00 70.88  ? 93  SER   A C   1 
ATOM   752  O O   . SER   A 1 94 ? 19.606  -23.433 -8.039  1.00 75.87  ? 93  SER   A O   1 
ATOM   753  C CB  . SER   A 1 94 ? 17.638  -22.123 -9.600  1.00 52.68  ? 93  SER   A CB  1 
ATOM   754  O OG  . SER   A 1 94 ? 16.487  -21.419 -10.035 1.00 62.71  ? 93  SER   A OG  1 
ATOM   755  O OXT . SER   A 1 94 ? 18.137  -25.090 -7.747  1.00 83.63  ? 93  SER   A OXT 1 
ATOM   756  N N   . MET   B 1 2  ? 38.850  -11.225 -42.313 1.00 61.35  ? 1   MET   B N   1 
ATOM   757  C CA  . MET   B 1 2  ? 38.519  -12.108 -43.462 1.00 60.84  ? 1   MET   B CA  1 
ATOM   758  C C   . MET   B 1 2  ? 37.003  -12.300 -43.484 1.00 52.00  ? 1   MET   B C   1 
ATOM   759  O O   . MET   B 1 2  ? 36.423  -12.612 -42.440 1.00 57.50  ? 1   MET   B O   1 
ATOM   760  C CB  . MET   B 1 2  ? 39.262  -13.449 -43.334 1.00 62.25  ? 1   MET   B CB  1 
ATOM   761  C CG  . MET   B 1 2  ? 39.191  -14.378 -44.547 1.00 73.94  ? 1   MET   B CG  1 
ATOM   762  S SD  . MET   B 1 2  ? 40.057  -13.837 -46.041 1.00 75.50  ? 1   MET   B SD  1 
ATOM   763  C CE  . MET   B 1 2  ? 41.342  -12.809 -45.313 1.00 54.28  ? 1   MET   B CE  1 
ATOM   764  N N   . PRO   B 1 3  ? 36.310  -12.079 -44.637 1.00 45.62  ? 2   PRO   B N   1 
ATOM   765  C CA  . PRO   B 1 3  ? 34.865  -12.315 -44.726 1.00 41.74  ? 2   PRO   B CA  1 
ATOM   766  C C   . PRO   B 1 3  ? 34.569  -13.764 -44.345 1.00 46.24  ? 2   PRO   B C   1 
ATOM   767  O O   . PRO   B 1 3  ? 35.356  -14.646 -44.667 1.00 45.15  ? 2   PRO   B O   1 
ATOM   768  C CB  . PRO   B 1 3  ? 34.514  -12.024 -46.176 1.00 42.21  ? 2   PRO   B CB  1 
ATOM   769  C CG  . PRO   B 1 3  ? 35.626  -11.085 -46.624 1.00 38.50  ? 2   PRO   B CG  1 
ATOM   770  C CD  . PRO   B 1 3  ? 36.868  -11.573 -45.901 1.00 39.49  ? 2   PRO   B CD  1 
ATOM   771  N N   . HIS   B 1 4  ? 33.454  -13.975 -43.628 1.00 41.40  ? 3   HIS   B N   1 
ATOM   772  C CA  . HIS   B 1 4  ? 32.983  -15.309 -43.274 1.00 40.62  ? 3   HIS   B CA  1 
ATOM   773  C C   . HIS   B 1 4  ? 31.588  -15.538 -43.851 1.00 37.70  ? 3   HIS   B C   1 
ATOM   774  O O   . HIS   B 1 4  ? 30.996  -14.657 -44.475 1.00 36.84  ? 3   HIS   B O   1 
ATOM   775  C CB  . HIS   B 1 4  ? 33.032  -15.514 -41.757 1.00 45.66  ? 3   HIS   B CB  1 
ATOM   776  C CG  . HIS   B 1 4  ? 34.416  -15.400 -41.219 1.00 52.30  ? 3   HIS   B CG  1 
ATOM   777  N ND1 . HIS   B 1 4  ? 35.417  -16.288 -41.572 1.00 53.79  ? 3   HIS   B ND1 1 
ATOM   778  C CD2 . HIS   B 1 4  ? 34.984  -14.496 -40.406 1.00 53.17  ? 3   HIS   B CD2 1 
ATOM   779  C CE1 . HIS   B 1 4  ? 36.546  -15.934 -40.965 1.00 46.84  ? 3   HIS   B CE1 1 
ATOM   780  N NE2 . HIS   B 1 4  ? 36.304  -14.849 -40.249 1.00 58.10  ? 3   HIS   B NE2 1 
ATOM   781  N N   . ALA   B 1 5  ? 31.034  -16.735 -43.623 1.00 33.74  ? 4   ALA   B N   1 
ATOM   782  C CA  . ALA   B 1 5  ? 29.735  -17.039 -44.203 1.00 36.27  ? 4   ALA   B CA  1 
ATOM   783  C C   . ALA   B 1 5  ? 28.721  -15.999 -43.733 1.00 35.28  ? 4   ALA   B C   1 
ATOM   784  O O   . ALA   B 1 5  ? 27.832  -15.593 -44.470 1.00 38.55  ? 4   ALA   B O   1 
ATOM   785  C CB  . ALA   B 1 5  ? 29.330  -18.432 -43.765 1.00 36.78  ? 4   ALA   B CB  1 
ATOM   786  N N   . PHE   B 1 6  ? 28.833  -15.649 -42.455 1.00 37.00  ? 5   PHE   B N   1 
ATOM   787  C CA  . PHE   B 1 6  ? 28.030  -14.606 -41.840 1.00 39.33  ? 5   PHE   B CA  1 
ATOM   788  C C   . PHE   B 1 6  ? 28.882  -13.365 -41.607 1.00 34.62  ? 5   PHE   B C   1 
ATOM   789  O O   . PHE   B 1 6  ? 30.025  -13.461 -41.171 1.00 38.74  ? 5   PHE   B O   1 
ATOM   790  C CB  . PHE   B 1 6  ? 27.537  -15.050 -40.460 1.00 36.33  ? 5   PHE   B CB  1 
ATOM   791  C CG  . PHE   B 1 6  ? 26.485  -16.148 -40.512 1.00 34.01  ? 5   PHE   B CG  1 
ATOM   792  C CD1 . PHE   B 1 6  ? 25.134  -15.835 -40.645 1.00 32.41  ? 5   PHE   B CD1 1 
ATOM   793  C CD2 . PHE   B 1 6  ? 26.837  -17.496 -40.462 1.00 33.53  ? 5   PHE   B CD2 1 
ATOM   794  C CE1 . PHE   B 1 6  ? 24.159  -16.820 -40.700 1.00 36.64  ? 5   PHE   B CE1 1 
ATOM   795  C CE2 . PHE   B 1 6  ? 25.842  -18.474 -40.510 1.00 32.30  ? 5   PHE   B CE2 1 
ATOM   796  C CZ  . PHE   B 1 6  ? 24.514  -18.149 -40.601 1.00 29.51  ? 5   PHE   B CZ  1 
ATOM   797  N N   . LYS   B 1 7  ? 28.306  -12.214 -41.958 1.00 38.52  ? 6   LYS   B N   1 
ATOM   798  C CA  . LYS   B 1 7  ? 29.008  -10.960 -41.749 1.00 36.04  ? 6   LYS   B CA  1 
ATOM   799  C C   . LYS   B 1 7  ? 28.250  -10.144 -40.703 1.00 33.78  ? 6   LYS   B C   1 
ATOM   800  O O   . LYS   B 1 7  ? 27.017  -10.275 -40.541 1.00 32.11  ? 6   LYS   B O   1 
ATOM   801  C CB  . LYS   B 1 7  ? 29.102  -10.233 -43.088 1.00 41.78  ? 6   LYS   B CB  1 
ATOM   802  C CG  . LYS   B 1 7  ? 27.811  -9.852  -43.769 1.00 43.77  ? 6   LYS   B CG  1 
ATOM   803  C CD  . LYS   B 1 7  ? 28.042  -9.353  -45.202 1.00 41.92  ? 6   LYS   B CD  1 
ATOM   804  C CE  . LYS   B 1 7  ? 26.771  -9.023  -45.932 1.00 47.26  ? 6   LYS   B CE  1 
ATOM   805  N NZ  . LYS   B 1 7  ? 25.868  -10.168 -46.075 1.00 50.53  ? 6   LYS   B NZ  1 
ATOM   806  N N   . PRO   B 1 8  ? 28.941  -9.206  -40.024 1.00 37.64  ? 7   PRO   B N   1 
ATOM   807  C CA  . PRO   B 1 8  ? 28.289  -8.262  -39.116 1.00 31.78  ? 7   PRO   B CA  1 
ATOM   808  C C   . PRO   B 1 8  ? 27.109  -7.593  -39.794 1.00 32.97  ? 7   PRO   B C   1 
ATOM   809  O O   . PRO   B 1 8  ? 27.196  -7.107  -40.942 1.00 36.28  ? 7   PRO   B O   1 
ATOM   810  C CB  . PRO   B 1 8  ? 29.448  -7.290  -38.881 1.00 33.08  ? 7   PRO   B CB  1 
ATOM   811  C CG  . PRO   B 1 8  ? 30.636  -8.214  -38.839 1.00 37.63  ? 7   PRO   B CG  1 
ATOM   812  C CD  . PRO   B 1 8  ? 30.392  -8.956  -40.129 1.00 38.67  ? 7   PRO   B CD  1 
ATOM   813  N N   . GLY   B 1 9  ? 25.996  -7.559  -39.064 1.00 29.75  ? 8   GLY   B N   1 
ATOM   814  C CA  . GLY   B 1 9  ? 24.774  -6.931  -39.510 1.00 29.03  ? 8   GLY   B CA  1 
ATOM   815  C C   . GLY   B 1 9  ? 23.793  -7.898  -40.171 1.00 27.78  ? 8   GLY   B C   1 
ATOM   816  O O   . GLY   B 1 9  ? 22.635  -7.551  -40.405 1.00 29.91  ? 8   GLY   B O   1 
ATOM   817  N N   . ASP   B 1 10 ? 24.241  -9.138  -40.455 1.00 28.47  ? 9   ASP   B N   1 
ATOM   818  C CA  . ASP   B 1 10 ? 23.293  -10.086 -41.016 1.00 28.62  ? 9   ASP   B CA  1 
ATOM   819  C C   . ASP   B 1 10 ? 22.266  -10.483 -39.937 1.00 24.05  ? 9   ASP   B C   1 
ATOM   820  O O   . ASP   B 1 10 ? 22.603  -10.540 -38.750 1.00 27.79  ? 9   ASP   B O   1 
ATOM   821  C CB  . ASP   B 1 10 ? 23.933  -11.413 -41.417 1.00 26.54  ? 9   ASP   B CB  1 
ATOM   822  C CG  . ASP   B 1 10 ? 24.746  -11.452 -42.711 1.00 35.94  ? 9   ASP   B CG  1 
ATOM   823  O OD1 . ASP   B 1 10 ? 24.524  -10.564 -43.550 1.00 36.65  ? 9   ASP   B OD1 1 
ATOM   824  O OD2 . ASP   B 1 10 ? 25.570  -12.401 -42.845 1.00 36.62  ? 9   ASP   B OD2 1 
ATOM   825  N N   . LEU   B 1 11 ? 21.049  -10.657 -40.382 1.00 25.32  ? 10  LEU   B N   1 
ATOM   826  C CA  . LEU   B 1 11 ? 19.928  -10.871 -39.464 1.00 26.05  ? 10  LEU   B CA  1 
ATOM   827  C C   . LEU   B 1 11 ? 19.637  -12.365 -39.459 1.00 25.86  ? 10  LEU   B C   1 
ATOM   828  O O   . LEU   B 1 11 ? 19.658  -12.967 -40.538 1.00 28.98  ? 10  LEU   B O   1 
ATOM   829  C CB  . LEU   B 1 11 ? 18.703  -10.057 -39.875 1.00 27.93  ? 10  LEU   B CB  1 
ATOM   830  C CG  . LEU   B 1 11 ? 18.981  -8.552  -40.040 1.00 26.32  ? 10  LEU   B CG  1 
ATOM   831  C CD1 . LEU   B 1 11 ? 17.667  -7.819  -40.371 1.00 28.91  ? 10  LEU   B CD1 1 
ATOM   832  C CD2 . LEU   B 1 11 ? 19.640  -8.036  -38.756 1.00 28.61  ? 10  LEU   B CD2 1 
ATOM   833  N N   . VAL   B 1 12 ? 19.260  -12.922 -38.289 1.00 25.55  ? 11  VAL   B N   1 
ATOM   834  C CA  . VAL   B 1 12 ? 19.085  -14.369 -38.177 1.00 24.85  ? 11  VAL   B CA  1 
ATOM   835  C C   . VAL   B 1 12 ? 18.017  -14.642 -37.128 1.00 24.02  ? 11  VAL   B C   1 
ATOM   836  O O   . VAL   B 1 12 ? 17.627  -13.733 -36.385 1.00 25.80  ? 11  VAL   B O   1 
ATOM   837  C CB  . VAL   B 1 12 ? 20.398  -15.043 -37.716 1.00 24.19  ? 11  VAL   B CB  1 
ATOM   838  C CG1 . VAL   B 1 12 ? 21.539  -14.865 -38.741 1.00 27.05  ? 11  VAL   B CG1 1 
ATOM   839  C CG2 . VAL   B 1 12 ? 20.886  -14.643 -36.317 1.00 26.30  ? 11  VAL   B CG2 1 
ATOM   840  N N   . PHE   B 1 13 ? 17.563  -15.906 -37.077 1.00 25.18  ? 12  PHE   B N   1 
ATOM   841  C CA  . PHE   B 1 13 ? 17.039  -16.410 -35.812 1.00 24.99  ? 12  PHE   B CA  1 
ATOM   842  C C   . PHE   B 1 13 ? 18.135  -17.263 -35.206 1.00 24.27  ? 12  PHE   B C   1 
ATOM   843  O O   . PHE   B 1 13 ? 18.763  -18.053 -35.931 1.00 26.27  ? 12  PHE   B O   1 
ATOM   844  C CB  . PHE   B 1 13 ? 15.788  -17.244 -36.015 1.00 24.27  ? 12  PHE   B CB  1 
ATOM   845  C CG  . PHE   B 1 13 ? 14.595  -16.418 -36.467 1.00 24.32  ? 12  PHE   B CG  1 
ATOM   846  C CD1 . PHE   B 1 13 ? 14.384  -16.146 -37.819 1.00 27.20  ? 12  PHE   B CD1 1 
ATOM   847  C CD2 . PHE   B 1 13 ? 13.709  -15.908 -35.522 1.00 27.17  ? 12  PHE   B CD2 1 
ATOM   848  C CE1 . PHE   B 1 13 ? 13.284  -15.409 -38.204 1.00 30.61  ? 12  PHE   B CE1 1 
ATOM   849  C CE2 . PHE   B 1 13 ? 12.593  -15.170 -35.914 1.00 30.82  ? 12  PHE   B CE2 1 
ATOM   850  C CZ  . PHE   B 1 13 ? 12.389  -14.921 -37.272 1.00 31.53  ? 12  PHE   B CZ  1 
ATOM   851  N N   . ALA   B 1 14 ? 18.368  -17.118 -33.890 1.00 22.52  ? 13  ALA   B N   1 
ATOM   852  C CA  . ALA   B 1 14 ? 19.395  -17.855 -33.206 1.00 21.98  ? 13  ALA   B CA  1 
ATOM   853  C C   . ALA   B 1 14 ? 18.771  -18.834 -32.201 1.00 23.77  ? 13  ALA   B C   1 
ATOM   854  O O   . ALA   B 1 14 ? 17.859  -18.466 -31.442 1.00 26.09  ? 13  ALA   B O   1 
ATOM   855  C CB  . ALA   B 1 14 ? 20.344  -16.902 -32.472 1.00 26.15  ? 13  ALA   B CB  1 
ATOM   856  N N   . LYS   B 1 15 ? 19.239  -20.085 -32.222 1.00 23.97  ? 14  LYS   B N   1 
ATOM   857  C CA  . LYS   B 1 15 ? 18.591  -21.137 -31.431 1.00 26.10  ? 14  LYS   B CA  1 
ATOM   858  C C   . LYS   B 1 15 ? 19.480  -21.543 -30.262 1.00 27.18  ? 14  LYS   B C   1 
ATOM   859  O O   . LYS   B 1 15 ? 20.677  -21.855 -30.415 1.00 29.17  ? 14  LYS   B O   1 
ATOM   860  C CB  . LYS   B 1 15 ? 18.225  -22.321 -32.336 1.00 27.08  ? 14  LYS   B CB  1 
ATOM   861  C CG  . LYS   B 1 15 ? 17.591  -23.468 -31.459 1.00 25.10  ? 14  LYS   B CG  1 
ATOM   862  C CD  . LYS   B 1 15 ? 16.138  -23.095 -31.216 1.00 27.06  ? 14  LYS   B CD  1 
ATOM   863  C CE  . LYS   B 1 15 ? 15.242  -24.169 -30.531 1.00 29.52  ? 14  LYS   B CE  1 
ATOM   864  N NZ  . LYS   B 1 15 ? 15.798  -24.425 -29.213 1.00 28.45  ? 14  LYS   B NZ  1 
ATOM   865  N N   . MET   B 1 16 ? 18.877  -21.507 -29.060 1.00 27.21  ? 15  MET   B N   1 
ATOM   866  C CA  . MET   B 1 16 ? 19.531  -21.984 -27.849 1.00 28.16  ? 15  MET   B CA  1 
ATOM   867  C C   . MET   B 1 16 ? 18.594  -22.928 -27.092 1.00 27.69  ? 15  MET   B C   1 
ATOM   868  O O   . MET   B 1 16 ? 17.362  -22.809 -27.151 1.00 27.95  ? 15  MET   B O   1 
ATOM   869  C CB  . MET   B 1 16 ? 19.922  -20.794 -26.964 1.00 31.63  ? 15  MET   B CB  1 
ATOM   870  C CG  . MET   B 1 16 ? 21.012  -19.926 -27.649 1.00 30.46  ? 15  MET   B CG  1 
ATOM   871  S SD  . MET   B 1 16 ? 21.754  -18.681 -26.580 1.00 32.92  ? 15  MET   B SD  1 
ATOM   872  C CE  . MET   B 1 16 ? 22.736  -19.680 -25.454 1.00 31.54  ? 15  MET   B CE  1 
ATOM   873  N N   . LYS   B 1 17 ? 19.223  -23.875 -26.369 1.00 30.27  ? 16  LYS   B N   1 
ATOM   874  C CA  . LYS   B 1 17 ? 18.451  -24.901 -25.680 1.00 31.27  ? 16  LYS   B CA  1 
ATOM   875  C C   . LYS   B 1 17 ? 17.504  -24.234 -24.660 1.00 28.65  ? 16  LYS   B C   1 
ATOM   876  O O   . LYS   B 1 17 ? 17.903  -23.335 -23.900 1.00 31.10  ? 16  LYS   B O   1 
ATOM   877  C CB  . LYS   B 1 17 ? 19.447  -25.885 -25.042 1.00 37.79  ? 16  LYS   B CB  1 
ATOM   878  C CG  . LYS   B 1 17 ? 18.826  -26.930 -24.106 1.00 43.37  ? 16  LYS   B CG  1 
ATOM   879  C CD  . LYS   B 1 17 ? 19.569  -28.248 -23.911 1.00 48.11  ? 16  LYS   B CD  1 
ATOM   880  N N   . GLY   B 1 18 ? 16.235  -24.639 -24.717 1.00 31.60  ? 17  GLY   B N   1 
ATOM   881  C CA  . GLY   B 1 18 ? 15.216  -24.115 -23.819 1.00 31.99  ? 17  GLY   B CA  1 
ATOM   882  C C   . GLY   B 1 18 ? 14.465  -22.910 -24.371 1.00 32.51  ? 17  GLY   B C   1 
ATOM   883  O O   . GLY   B 1 18 ? 13.543  -22.406 -23.711 1.00 30.46  ? 17  GLY   B O   1 
ATOM   884  N N   . TYR   B 1 19 ? 14.877  -22.419 -25.560 1.00 28.61  ? 18  TYR   B N   1 
ATOM   885  C CA  . TYR   B 1 19 ? 14.228  -21.208 -26.051 1.00 28.90  ? 18  TYR   B CA  1 
ATOM   886  C C   . TYR   B 1 19 ? 13.822  -21.375 -27.505 1.00 26.82  ? 18  TYR   B C   1 
ATOM   887  O O   . TYR   B 1 19 ? 14.496  -22.109 -28.234 1.00 29.48  ? 18  TYR   B O   1 
ATOM   888  C CB  . TYR   B 1 19 ? 15.191  -20.009 -26.036 1.00 26.95  ? 18  TYR   B CB  1 
ATOM   889  C CG  . TYR   B 1 19 ? 15.641  -19.710 -24.613 1.00 27.88  ? 18  TYR   B CG  1 
ATOM   890  C CD1 . TYR   B 1 19 ? 14.840  -18.947 -23.764 1.00 29.75  ? 18  TYR   B CD1 1 
ATOM   891  C CD2 . TYR   B 1 19 ? 16.781  -20.318 -24.087 1.00 27.55  ? 18  TYR   B CD2 1 
ATOM   892  C CE1 . TYR   B 1 19 ? 15.200  -18.753 -22.426 1.00 30.24  ? 18  TYR   B CE1 1 
ATOM   893  C CE2 . TYR   B 1 19 ? 17.160  -20.102 -22.763 1.00 31.37  ? 18  TYR   B CE2 1 
ATOM   894  C CZ  . TYR   B 1 19 ? 16.362  -19.319 -21.942 1.00 29.81  ? 18  TYR   B CZ  1 
ATOM   895  O OH  . TYR   B 1 19 ? 16.784  -19.140 -20.640 1.00 32.60  ? 18  TYR   B OH  1 
ATOM   896  N N   . PRO   B 1 20 ? 12.776  -20.667 -27.986 1.00 27.30  ? 19  PRO   B N   1 
ATOM   897  C CA  . PRO   B 1 20 ? 12.418  -20.705 -29.408 1.00 25.93  ? 19  PRO   B CA  1 
ATOM   898  C C   . PRO   B 1 20 ? 13.484  -20.000 -30.242 1.00 24.93  ? 19  PRO   B C   1 
ATOM   899  O O   . PRO   B 1 20 ? 14.195  -19.181 -29.714 1.00 25.65  ? 19  PRO   B O   1 
ATOM   900  C CB  . PRO   B 1 20 ? 11.122  -19.998 -29.514 1.00 27.66  ? 19  PRO   B CB  1 
ATOM   901  C CG  . PRO   B 1 20 ? 11.116  -19.056 -28.326 1.00 27.53  ? 19  PRO   B CG  1 
ATOM   902  C CD  . PRO   B 1 20 ? 11.884  -19.788 -27.218 1.00 27.06  ? 19  PRO   B CD  1 
ATOM   903  N N   . HIS   B 1 21 ? 13.590  -20.400 -31.529 1.00 24.69  ? 20  HIS   B N   1 
ATOM   904  C CA  . HIS   B 1 21 ? 14.454  -19.648 -32.460 1.00 24.63  ? 20  HIS   B CA  1 
ATOM   905  C C   . HIS   B 1 21 ? 14.245  -18.132 -32.286 1.00 23.92  ? 20  HIS   B C   1 
ATOM   906  O O   . HIS   B 1 21 ? 13.117  -17.670 -32.373 1.00 24.96  ? 20  HIS   B O   1 
ATOM   907  C CB  . HIS   B 1 21 ? 14.158  -20.120 -33.888 1.00 26.19  ? 20  HIS   B CB  1 
ATOM   908  C CG  . HIS   B 1 21 ? 14.325  -21.599 -34.083 1.00 26.98  ? 20  HIS   B CG  1 
ATOM   909  N ND1 . HIS   B 1 21 ? 13.416  -22.554 -33.606 1.00 27.51  ? 20  HIS   B ND1 1 
ATOM   910  C CD2 . HIS   B 1 21 ? 15.328  -22.271 -34.640 1.00 29.41  ? 20  HIS   B CD2 1 
ATOM   911  C CE1 . HIS   B 1 21 ? 13.847  -23.758 -33.977 1.00 28.94  ? 20  HIS   B CE1 1 
ATOM   912  N NE2 . HIS   B 1 21 ? 15.009  -23.620 -34.605 1.00 28.16  ? 20  HIS   B NE2 1 
ATOM   913  N N   . TRP   B 1 22 ? 15.335  -17.377 -32.079 1.00 22.92  ? 21  TRP   B N   1 
ATOM   914  C CA  . TRP   B 1 22 ? 15.109  -16.060 -31.479 1.00 23.36  ? 21  TRP   B CA  1 
ATOM   915  C C   . TRP   B 1 22 ? 15.592  -14.988 -32.453 1.00 24.29  ? 21  TRP   B C   1 
ATOM   916  O O   . TRP   B 1 22 ? 16.730  -15.085 -32.880 1.00 23.88  ? 21  TRP   B O   1 
ATOM   917  C CB  . TRP   B 1 22 ? 15.888  -15.970 -30.158 1.00 25.58  ? 21  TRP   B CB  1 
ATOM   918  C CG  . TRP   B 1 22 ? 15.375  -14.848 -29.289 1.00 24.08  ? 21  TRP   B CG  1 
ATOM   919  C CD1 . TRP   B 1 22 ? 15.650  -13.510 -29.399 1.00 24.82  ? 21  TRP   B CD1 1 
ATOM   920  C CD2 . TRP   B 1 22 ? 14.432  -14.958 -28.188 1.00 25.89  ? 21  TRP   B CD2 1 
ATOM   921  N NE1 . TRP   B 1 22 ? 14.919  -12.778 -28.476 1.00 24.91  ? 21  TRP   B NE1 1 
ATOM   922  C CE2 . TRP   B 1 22 ? 14.207  -13.652 -27.683 1.00 24.32  ? 21  TRP   B CE2 1 
ATOM   923  C CE3 . TRP   B 1 22 ? 13.802  -16.060 -27.577 1.00 28.15  ? 21  TRP   B CE3 1 
ATOM   924  C CZ2 . TRP   B 1 22 ? 13.315  -13.392 -26.623 1.00 26.16  ? 21  TRP   B CZ2 1 
ATOM   925  C CZ3 . TRP   B 1 22 ? 12.954  -15.810 -26.509 1.00 27.41  ? 21  TRP   B CZ3 1 
ATOM   926  C CH2 . TRP   B 1 22 ? 12.709  -14.501 -26.063 1.00 26.56  ? 21  TRP   B CH2 1 
ATOM   927  N N   . PRO   B 1 23 ? 14.858  -13.877 -32.674 1.00 25.00  ? 22  PRO   B N   1 
ATOM   928  C CA  . PRO   B 1 23 ? 15.320  -12.857 -33.631 1.00 22.65  ? 22  PRO   B CA  1 
ATOM   929  C C   . PRO   B 1 23 ? 16.626  -12.252 -33.116 1.00 24.32  ? 22  PRO   B C   1 
ATOM   930  O O   . PRO   B 1 23 ? 16.726  -11.835 -31.949 1.00 24.33  ? 22  PRO   B O   1 
ATOM   931  C CB  . PRO   B 1 23 ? 14.147  -11.826 -33.683 1.00 23.62  ? 22  PRO   B CB  1 
ATOM   932  C CG  . PRO   B 1 23 ? 13.512  -11.980 -32.294 1.00 23.81  ? 22  PRO   B CG  1 
ATOM   933  C CD  . PRO   B 1 23 ? 13.543  -13.533 -32.136 1.00 24.00  ? 22  PRO   B CD  1 
ATOM   934  N N   . ALA   B 1 24 ? 17.630  -12.103 -33.995 1.00 23.47  ? 23  ALA   B N   1 
ATOM   935  C CA  . ALA   B 1 24 ? 18.978  -11.760 -33.563 1.00 22.27  ? 23  ALA   B CA  1 
ATOM   936  C C   . ALA   B 1 24 ? 19.769  -11.212 -34.762 1.00 23.33  ? 23  ALA   B C   1 
ATOM   937  O O   . ALA   B 1 24 ? 19.278  -11.273 -35.895 1.00 25.05  ? 23  ALA   B O   1 
ATOM   938  C CB  . ALA   B 1 24 ? 19.653  -12.939 -32.856 1.00 24.67  ? 23  ALA   B CB  1 
ATOM   939  N N   . ARG   B 1 25 ? 20.940  -10.679 -34.436 1.00 25.84  ? 24  ARG   B N   1 
ATOM   940  C CA  . ARG   B 1 25 ? 21.851  -10.213 -35.483 1.00 25.82  ? 24  ARG   B CA  1 
ATOM   941  C C   . ARG   B 1 25 ? 23.268  -10.665 -35.164 1.00 25.86  ? 24  ARG   B C   1 
ATOM   942  O O   . ARG   B 1 25 ? 23.658  -10.952 -34.028 1.00 25.79  ? 24  ARG   B O   1 
ATOM   943  C CB  . ARG   B 1 25 ? 21.788  -8.691  -35.632 1.00 27.82  ? 24  ARG   B CB  1 
ATOM   944  C CG  . ARG   B 1 25 ? 22.423  -7.943  -34.469 1.00 27.20  ? 24  ARG   B CG  1 
ATOM   945  C CD  . ARG   B 1 25 ? 22.223  -6.420  -34.580 1.00 26.35  ? 24  ARG   B CD  1 
ATOM   946  N NE  . ARG   B 1 25 ? 22.820  -5.745  -33.427 1.00 29.68  ? 24  ARG   B NE  1 
ATOM   947  C CZ  . ARG   B 1 25 ? 22.547  -4.484  -33.060 1.00 28.77  ? 24  ARG   B CZ  1 
ATOM   948  N NH1 . ARG   B 1 25 ? 21.580  -3.832  -33.699 1.00 29.74  ? 24  ARG   B NH1 1 
ATOM   949  N NH2 . ARG   B 1 25 ? 23.203  -3.971  -32.031 1.00 28.72  ? 24  ARG   B NH2 1 
ATOM   950  N N   . ILE   B 1 26 ? 24.088  -10.734 -36.236 1.00 26.20  ? 25  ILE   B N   1 
ATOM   951  C CA  . ILE   B 1 26 ? 25.501  -10.927 -36.039 1.00 26.03  ? 25  ILE   B CA  1 
ATOM   952  C C   . ILE   B 1 26 ? 26.100  -9.562  -35.716 1.00 31.78  ? 25  ILE   B C   1 
ATOM   953  O O   . ILE   B 1 26 ? 25.859  -8.610  -36.457 1.00 33.04  ? 25  ILE   B O   1 
ATOM   954  C CB  . ILE   B 1 26 ? 26.128  -11.426 -37.354 1.00 31.03  ? 25  ILE   B CB  1 
ATOM   955  C CG1 . ILE   B 1 26 ? 25.378  -12.645 -37.914 1.00 29.94  ? 25  ILE   B CG1 1 
ATOM   956  C CG2 . ILE   B 1 26 ? 27.628  -11.680 -37.181 1.00 34.54  ? 25  ILE   B CG2 1 
ATOM   957  C CD1 . ILE   B 1 26 ? 25.392  -13.852 -36.990 1.00 31.71  ? 25  ILE   B CD1 1 
ATOM   958  N N   . ASP   B 1 27 ? 26.872  -9.520  -34.638 1.00 30.41  ? 26  ASP   B N   1 
ATOM   959  C CA  . ASP   B 1 27 ? 27.544  -8.279  -34.230 1.00 37.58  ? 26  ASP   B CA  1 
ATOM   960  C C   . ASP   B 1 27 ? 29.006  -8.260  -34.694 1.00 39.87  ? 26  ASP   B C   1 
ATOM   961  O O   . ASP   B 1 27 ? 29.553  -9.285  -35.074 1.00 42.49  ? 26  ASP   B O   1 
ATOM   962  C CB  . ASP   B 1 27 ? 27.512  -8.122  -32.722 1.00 33.85  ? 26  ASP   B CB  1 
ATOM   963  C CG  . ASP   B 1 27 ? 26.338  -7.372  -32.115 1.00 37.85  ? 26  ASP   B CG  1 
ATOM   964  O OD1 . ASP   B 1 27 ? 25.509  -6.830  -32.893 1.00 39.59  ? 26  ASP   B OD1 1 
ATOM   965  O OD2 . ASP   B 1 27 ? 26.284  -7.340  -30.844 1.00 36.05  ? 26  ASP   B OD2 1 
ATOM   966  N N   . ASP   B 1 28 ? 29.642  -7.075  -34.612 1.00 50.19  ? 27  ASP   B N   1 
ATOM   967  C CA  . ASP   B 1 28 ? 31.075  -6.913  -34.816 1.00 61.20  ? 27  ASP   B CA  1 
ATOM   968  C C   . ASP   B 1 28 ? 31.835  -7.148  -33.506 1.00 59.87  ? 27  ASP   B C   1 
ATOM   969  O O   . ASP   B 1 28 ? 31.234  -7.171  -32.438 1.00 64.27  ? 27  ASP   B O   1 
ATOM   970  C CB  . ASP   B 1 28 ? 31.376  -5.527  -35.362 1.00 58.77  ? 27  ASP   B CB  1 
ATOM   971  C CG  . ASP   B 1 28 ? 32.258  -5.511  -36.603 1.00 64.97  ? 27  ASP   B CG  1 
ATOM   972  O OD1 . ASP   B 1 28 ? 33.324  -6.163  -36.587 1.00 75.37  ? 27  ASP   B OD1 1 
ATOM   973  O OD2 . ASP   B 1 28 ? 31.873  -4.850  -37.581 1.00 60.22  ? 27  ASP   B OD2 1 
ATOM   974  N N   . ILE   B 1 29 ? 33.164  -7.315  -33.595 1.00 64.39  ? 28  ILE   B N   1 
ATOM   975  C CA  . ILE   B 1 29 ? 34.040  -7.442  -32.435 1.00 65.66  ? 28  ILE   B CA  1 
ATOM   976  C C   . ILE   B 1 29 ? 34.813  -6.124  -32.245 1.00 72.09  ? 28  ILE   B C   1 
ATOM   977  O O   . ILE   B 1 29 ? 34.174  -5.152  -31.774 1.00 66.32  ? 28  ILE   B O   1 
ATOM   978  C CB  . ILE   B 1 29 ? 34.999  -8.644  -32.565 1.00 61.55  ? 28  ILE   B CB  1 
ATOM   979  N N   . VAL   B 1 34 ? 37.150  -9.624  -25.621 1.00 58.20  ? 33  VAL   B N   1 
ATOM   980  C CA  . VAL   B 1 34 ? 36.884  -11.081 -25.828 1.00 62.48  ? 33  VAL   B CA  1 
ATOM   981  C C   . VAL   B 1 34 ? 36.649  -11.282 -27.324 1.00 72.51  ? 33  VAL   B C   1 
ATOM   982  O O   . VAL   B 1 34 ? 35.959  -10.482 -27.963 1.00 79.14  ? 33  VAL   B O   1 
ATOM   983  C CB  . VAL   B 1 34 ? 35.715  -11.574 -24.941 1.00 60.39  ? 33  VAL   B CB  1 
ATOM   984  C CG1 . VAL   B 1 34 ? 34.368  -10.956 -25.310 1.00 65.61  ? 33  VAL   B CG1 1 
ATOM   985  C CG2 . VAL   B 1 34 ? 35.607  -13.099 -24.863 1.00 55.10  ? 33  VAL   B CG2 1 
ATOM   986  N N   . LYS   B 1 35 ? 37.309  -12.302 -27.889 1.00 68.19  ? 34  LYS   B N   1 
ATOM   987  C CA  . LYS   B 1 35 ? 37.028  -12.747 -29.247 1.00 62.34  ? 34  LYS   B CA  1 
ATOM   988  C C   . LYS   B 1 35 ? 36.169  -14.013 -29.161 1.00 59.77  ? 34  LYS   B C   1 
ATOM   989  O O   . LYS   B 1 35 ? 36.232  -14.730 -28.155 1.00 56.71  ? 34  LYS   B O   1 
ATOM   990  C CB  . LYS   B 1 35 ? 38.353  -12.867 -30.012 1.00 60.78  ? 34  LYS   B CB  1 
ATOM   991  N N   . PRO   B 1 36 ? 35.314  -14.330 -30.174 1.00 59.68  ? 35  PRO   B N   1 
ATOM   992  C CA  . PRO   B 1 36 ? 34.463  -15.527 -30.099 1.00 53.94  ? 35  PRO   B CA  1 
ATOM   993  C C   . PRO   B 1 36 ? 35.350  -16.758 -29.957 1.00 47.76  ? 35  PRO   B C   1 
ATOM   994  O O   . PRO   B 1 36 ? 36.490  -16.718 -30.394 1.00 53.51  ? 35  PRO   B O   1 
ATOM   995  C CB  . PRO   B 1 36 ? 33.658  -15.555 -31.411 1.00 52.54  ? 35  PRO   B CB  1 
ATOM   996  C CG  . PRO   B 1 36 ? 33.925  -14.213 -32.086 1.00 56.27  ? 35  PRO   B CG  1 
ATOM   997  C CD  . PRO   B 1 36 ? 35.117  -13.552 -31.409 1.00 56.33  ? 35  PRO   B CD  1 
ATOM   998  N N   . PRO   B 1 37 ? 34.899  -17.880 -29.340 1.00 47.14  ? 36  PRO   B N   1 
ATOM   999  C CA  . PRO   B 1 37 ? 35.632  -19.139 -29.457 1.00 44.87  ? 36  PRO   B CA  1 
ATOM   1000 C C   . PRO   B 1 37 ? 35.711  -19.474 -30.941 1.00 52.15  ? 36  PRO   B C   1 
ATOM   1001 O O   . PRO   B 1 37 ? 34.938  -18.942 -31.752 1.00 50.93  ? 36  PRO   B O   1 
ATOM   1002 C CB  . PRO   B 1 37 ? 34.765  -20.156 -28.692 1.00 50.36  ? 36  PRO   B CB  1 
ATOM   1003 C CG  . PRO   B 1 37 ? 33.949  -19.313 -27.731 1.00 46.81  ? 36  PRO   B CG  1 
ATOM   1004 C CD  . PRO   B 1 37 ? 33.714  -17.998 -28.469 1.00 48.40  ? 36  PRO   B CD  1 
ATOM   1005 N N   . PRO   B 1 38 ? 36.635  -20.372 -31.352 1.00 54.20  ? 37  PRO   B N   1 
ATOM   1006 C CA  . PRO   B 1 38 ? 36.739  -20.757 -32.767 1.00 53.45  ? 37  PRO   B CA  1 
ATOM   1007 C C   . PRO   B 1 38 ? 35.380  -21.175 -33.345 1.00 44.82  ? 37  PRO   B C   1 
ATOM   1008 O O   . PRO   B 1 38 ? 34.574  -21.807 -32.656 1.00 48.25  ? 37  PRO   B O   1 
ATOM   1009 C CB  . PRO   B 1 38 ? 37.768  -21.916 -32.729 1.00 51.38  ? 37  PRO   B CB  1 
ATOM   1010 C CG  . PRO   B 1 38 ? 38.615  -21.619 -31.494 1.00 54.87  ? 37  PRO   B CG  1 
ATOM   1011 C CD  . PRO   B 1 38 ? 37.618  -21.054 -30.482 1.00 57.58  ? 37  PRO   B CD  1 
ATOM   1012 N N   . ASN   B 1 39 ? 35.125  -20.790 -34.601 1.00 42.64  ? 38  ASN   B N   1 
ATOM   1013 C CA  . ASN   B 1 39 ? 33.943  -21.239 -35.343 1.00 49.09  ? 38  ASN   B CA  1 
ATOM   1014 C C   . ASN   B 1 39 ? 32.648  -20.533 -34.914 1.00 40.09  ? 38  ASN   B C   1 
ATOM   1015 O O   . ASN   B 1 39 ? 31.594  -20.791 -35.476 1.00 37.44  ? 38  ASN   B O   1 
ATOM   1016 C CB  . ASN   B 1 39 ? 33.684  -22.738 -35.192 1.00 48.57  ? 38  ASN   B CB  1 
ATOM   1017 C CG  . ASN   B 1 39 ? 34.866  -23.598 -35.582 1.00 60.24  ? 38  ASN   B CG  1 
ATOM   1018 O OD1 . ASN   B 1 39 ? 35.201  -24.548 -34.862 1.00 62.76  ? 38  ASN   B OD1 1 
ATOM   1019 N ND2 . ASN   B 1 39 ? 35.493  -23.301 -36.713 1.00 53.99  ? 38  ASN   B ND2 1 
ATOM   1020 N N   . LYS   B 1 40 ? 32.702  -19.612 -33.940 1.00 43.01  ? 39  LYS   B N   1 
ATOM   1021 C CA  . LYS   B 1 40 ? 31.481  -18.998 -33.441 1.00 36.94  ? 39  LYS   B CA  1 
ATOM   1022 C C   . LYS   B 1 40 ? 31.444  -17.511 -33.756 1.00 32.46  ? 39  LYS   B C   1 
ATOM   1023 O O   . LYS   B 1 40 ? 32.441  -16.924 -34.167 1.00 37.82  ? 39  LYS   B O   1 
ATOM   1024 C CB  . LYS   B 1 40 ? 31.380  -19.250 -31.937 1.00 38.45  ? 39  LYS   B CB  1 
ATOM   1025 C CG  . LYS   B 1 40 ? 31.330  -20.733 -31.655 1.00 38.29  ? 39  LYS   B CG  1 
ATOM   1026 C CD  . LYS   B 1 40 ? 31.270  -20.959 -30.148 1.00 52.13  ? 39  LYS   B CD  1 
ATOM   1027 C CE  . LYS   B 1 40 ? 30.407  -22.081 -29.677 1.00 61.30  ? 39  LYS   B CE  1 
ATOM   1028 N NZ  . LYS   B 1 40 ? 30.555  -23.249 -30.542 1.00 59.78  ? 39  LYS   B NZ  1 
ATOM   1029 N N   . TYR   B 1 41 ? 30.260  -16.916 -33.589 1.00 32.37  ? 40  TYR   B N   1 
ATOM   1030 C CA  . TYR   B 1 41 ? 29.993  -15.533 -33.953 1.00 29.73  ? 40  TYR   B CA  1 
ATOM   1031 C C   . TYR   B 1 41 ? 29.395  -14.839 -32.740 1.00 32.74  ? 40  TYR   B C   1 
ATOM   1032 O O   . TYR   B 1 41 ? 28.679  -15.446 -31.931 1.00 30.58  ? 40  TYR   B O   1 
ATOM   1033 C CB  . TYR   B 1 41 ? 28.969  -15.424 -35.085 1.00 30.96  ? 40  TYR   B CB  1 
ATOM   1034 C CG  . TYR   B 1 41 ? 29.431  -15.906 -36.457 1.00 29.08  ? 40  TYR   B CG  1 
ATOM   1035 C CD1 . TYR   B 1 41 ? 30.006  -15.029 -37.367 1.00 31.71  ? 40  TYR   B CD1 1 
ATOM   1036 C CD2 . TYR   B 1 41 ? 29.244  -17.225 -36.825 1.00 28.28  ? 40  TYR   B CD2 1 
ATOM   1037 C CE1 . TYR   B 1 41 ? 30.413  -15.483 -38.618 1.00 36.11  ? 40  TYR   B CE1 1 
ATOM   1038 C CE2 . TYR   B 1 41 ? 29.653  -17.697 -38.059 1.00 34.08  ? 40  TYR   B CE2 1 
ATOM   1039 C CZ  . TYR   B 1 41 ? 30.231  -16.812 -38.961 1.00 37.28  ? 40  TYR   B CZ  1 
ATOM   1040 O OH  . TYR   B 1 41 ? 30.606  -17.222 -40.216 1.00 35.06  ? 40  TYR   B OH  1 
ATOM   1041 N N   . PRO   B 1 42 ? 29.613  -13.518 -32.611 1.00 32.61  ? 41  PRO   B N   1 
ATOM   1042 C CA  . PRO   B 1 42 ? 28.931  -12.749 -31.569 1.00 29.71  ? 41  PRO   B CA  1 
ATOM   1043 C C   . PRO   B 1 42 ? 27.519  -12.443 -32.030 1.00 29.26  ? 41  PRO   B C   1 
ATOM   1044 O O   . PRO   B 1 42 ? 27.314  -11.824 -33.083 1.00 28.78  ? 41  PRO   B O   1 
ATOM   1045 C CB  . PRO   B 1 42 ? 29.797  -11.467 -31.403 1.00 34.69  ? 41  PRO   B CB  1 
ATOM   1046 C CG  . PRO   B 1 42 ? 30.623  -11.393 -32.672 1.00 37.61  ? 41  PRO   B CG  1 
ATOM   1047 C CD  . PRO   B 1 42 ? 30.514  -12.706 -33.453 1.00 34.57  ? 41  PRO   B CD  1 
ATOM   1048 N N   . ILE   B 1 43 ? 26.554  -12.903 -31.210 1.00 28.36  ? 42  ILE   B N   1 
ATOM   1049 C CA  . ILE   B 1 43 ? 25.128  -12.727 -31.451 1.00 27.44  ? 42  ILE   B CA  1 
ATOM   1050 C C   . ILE   B 1 43 ? 24.548  -11.673 -30.517 1.00 27.26  ? 42  ILE   B C   1 
ATOM   1051 O O   . ILE   B 1 43 ? 24.819  -11.718 -29.333 1.00 29.80  ? 42  ILE   B O   1 
ATOM   1052 C CB  . ILE   B 1 43 ? 24.404  -14.073 -31.290 1.00 25.50  ? 42  ILE   B CB  1 
ATOM   1053 C CG1 . ILE   B 1 43 ? 25.161  -15.146 -32.160 1.00 28.17  ? 42  ILE   B CG1 1 
ATOM   1054 C CG2 . ILE   B 1 43 ? 22.936  -13.908 -31.690 1.00 26.71  ? 42  ILE   B CG2 1 
ATOM   1055 C CD1 . ILE   B 1 43 ? 25.261  -14.829 -33.644 1.00 28.88  ? 42  ILE   B CD1 1 
ATOM   1056 N N   . PHE   B 1 44 ? 23.731  -10.786 -31.064 1.00 26.44  ? 43  PHE   B N   1 
ATOM   1057 C CA  . PHE   B 1 44 ? 22.896  -9.910  -30.239 1.00 26.51  ? 43  PHE   B CA  1 
ATOM   1058 C C   . PHE   B 1 44 ? 21.457  -10.363 -30.417 1.00 25.09  ? 43  PHE   B C   1 
ATOM   1059 O O   . PHE   B 1 44 ? 20.964  -10.441 -31.536 1.00 26.01  ? 43  PHE   B O   1 
ATOM   1060 C CB  . PHE   B 1 44 ? 23.145  -8.467  -30.700 1.00 27.17  ? 43  PHE   B CB  1 
ATOM   1061 C CG  . PHE   B 1 44 ? 22.199  -7.473  -30.036 1.00 27.37  ? 43  PHE   B CG  1 
ATOM   1062 C CD1 . PHE   B 1 44 ? 20.989  -7.109  -30.638 1.00 25.52  ? 43  PHE   B CD1 1 
ATOM   1063 C CD2 . PHE   B 1 44 ? 22.499  -6.907  -28.808 1.00 33.78  ? 43  PHE   B CD2 1 
ATOM   1064 C CE1 . PHE   B 1 44 ? 20.119  -6.193  -30.051 1.00 29.59  ? 43  PHE   B CE1 1 
ATOM   1065 C CE2 . PHE   B 1 44 ? 21.608  -6.001  -28.215 1.00 29.51  ? 43  PHE   B CE2 1 
ATOM   1066 C CZ  . PHE   B 1 44 ? 20.437  -5.656  -28.831 1.00 31.33  ? 43  PHE   B CZ  1 
ATOM   1067 N N   . PHE   B 1 45 ? 20.755  -10.611 -29.283 1.00 24.90  ? 44  PHE   B N   1 
ATOM   1068 C CA  . PHE   B 1 45 ? 19.362  -11.021 -29.300 1.00 25.16  ? 44  PHE   B CA  1 
ATOM   1069 C C   . PHE   B 1 45 ? 18.468  -9.811  -29.149 1.00 24.86  ? 44  PHE   B C   1 
ATOM   1070 O O   . PHE   B 1 45 ? 18.555  -9.066  -28.153 1.00 27.06  ? 44  PHE   B O   1 
ATOM   1071 C CB  . PHE   B 1 45 ? 19.177  -11.991 -28.111 1.00 24.54  ? 44  PHE   B CB  1 
ATOM   1072 C CG  . PHE   B 1 45 ? 19.903  -13.322 -28.262 1.00 23.90  ? 44  PHE   B CG  1 
ATOM   1073 C CD1 . PHE   B 1 45 ? 21.250  -13.446 -27.924 1.00 26.20  ? 44  PHE   B CD1 1 
ATOM   1074 C CD2 . PHE   B 1 45 ? 19.245  -14.420 -28.826 1.00 24.23  ? 44  PHE   B CD2 1 
ATOM   1075 C CE1 . PHE   B 1 45 ? 21.915  -14.641 -28.117 1.00 29.45  ? 44  PHE   B CE1 1 
ATOM   1076 C CE2 . PHE   B 1 45 ? 19.897  -15.620 -28.976 1.00 24.96  ? 44  PHE   B CE2 1 
ATOM   1077 C CZ  . PHE   B 1 45 ? 21.251  -15.721 -28.652 1.00 25.67  ? 44  PHE   B CZ  1 
ATOM   1078 N N   . PHE   B 1 46 ? 17.625  -9.614  -30.167 1.00 25.25  ? 45  PHE   B N   1 
ATOM   1079 C CA  . PHE   B 1 46 ? 16.643  -8.543  -30.151 1.00 25.43  ? 45  PHE   B CA  1 
ATOM   1080 C C   . PHE   B 1 46 ? 15.662  -8.745  -28.986 1.00 27.54  ? 45  PHE   B C   1 
ATOM   1081 O O   . PHE   B 1 46 ? 15.405  -9.869  -28.562 1.00 26.81  ? 45  PHE   B O   1 
ATOM   1082 C CB  . PHE   B 1 46 ? 15.863  -8.365  -31.450 1.00 23.96  ? 45  PHE   B CB  1 
ATOM   1083 C CG  . PHE   B 1 46 ? 16.792  -7.906  -32.567 1.00 26.46  ? 45  PHE   B CG  1 
ATOM   1084 C CD1 . PHE   B 1 46 ? 17.316  -6.595  -32.555 1.00 28.62  ? 45  PHE   B CD1 1 
ATOM   1085 C CD2 . PHE   B 1 46 ? 17.071  -8.751  -33.643 1.00 25.19  ? 45  PHE   B CD2 1 
ATOM   1086 C CE1 . PHE   B 1 46 ? 18.161  -6.175  -33.596 1.00 26.00  ? 45  PHE   B CE1 1 
ATOM   1087 C CE2 . PHE   B 1 46 ? 17.921  -8.327  -34.675 1.00 26.57  ? 45  PHE   B CE2 1 
ATOM   1088 C CZ  . PHE   B 1 46 ? 18.405  -7.018  -34.649 1.00 25.66  ? 45  PHE   B CZ  1 
ATOM   1089 N N   . GLY   B 1 47 ? 15.111  -7.636  -28.480 1.00 27.44  ? 46  GLY   B N   1 
ATOM   1090 C CA  . GLY   B 1 47 ? 14.103  -7.714  -27.422 1.00 26.76  ? 46  GLY   B CA  1 
ATOM   1091 C C   . GLY   B 1 47 ? 14.770  -7.822  -26.052 1.00 27.09  ? 46  GLY   B C   1 
ATOM   1092 O O   . GLY   B 1 47 ? 14.611  -6.938  -25.192 1.00 32.11  ? 46  GLY   B O   1 
ATOM   1093 N N   . THR   B 1 48 ? 15.513  -8.907  -25.798 1.00 28.27  ? 47  THR   B N   1 
ATOM   1094 C CA  . THR   B 1 48 ? 16.209  -9.088  -24.536 1.00 28.91  ? 47  THR   B CA  1 
ATOM   1095 C C   . THR   B 1 48 ? 17.479  -8.252  -24.484 1.00 30.17  ? 47  THR   B C   1 
ATOM   1096 O O   . THR   B 1 48 ? 17.962  -7.892  -23.408 1.00 31.73  ? 47  THR   B O   1 
ATOM   1097 C CB  . THR   B 1 48 ? 16.525  -10.551 -24.176 1.00 32.61  ? 47  THR   B CB  1 
ATOM   1098 O OG1 . THR   B 1 48 ? 17.544  -11.104 -25.036 1.00 28.80  ? 47  THR   B OG1 1 
ATOM   1099 C CG2 . THR   B 1 48 ? 15.275  -11.421 -24.159 1.00 28.30  ? 47  THR   B CG2 1 
ATOM   1100 N N   . HIS   B 1 49 ? 18.050  -8.006  -25.660 1.00 28.88  ? 48  HIS   B N   1 
ATOM   1101 C CA  . HIS   B 1 49 ? 19.317  -7.315  -25.794 1.00 30.41  ? 48  HIS   B CA  1 
ATOM   1102 C C   . HIS   B 1 49 ? 20.446  -8.082  -25.137 1.00 32.16  ? 48  HIS   B C   1 
ATOM   1103 O O   . HIS   B 1 49 ? 21.471  -7.470  -24.817 1.00 35.06  ? 48  HIS   B O   1 
ATOM   1104 C CB  . HIS   B 1 49 ? 19.268  -5.850  -25.320 1.00 29.11  ? 48  HIS   B CB  1 
ATOM   1105 C CG  . HIS   B 1 49 ? 18.079  -5.162  -25.835 1.00 31.13  ? 48  HIS   B CG  1 
ATOM   1106 N ND1 . HIS   B 1 49 ? 17.282  -4.357  -25.055 1.00 33.04  ? 48  HIS   B ND1 1 
ATOM   1107 C CD2 . HIS   B 1 49 ? 17.494  -5.206  -27.032 1.00 28.82  ? 48  HIS   B CD2 1 
ATOM   1108 C CE1 . HIS   B 1 49 ? 16.241  -3.947  -25.763 1.00 39.17  ? 48  HIS   B CE1 1 
ATOM   1109 N NE2 . HIS   B 1 49 ? 16.364  -4.448  -26.989 1.00 32.60  ? 48  HIS   B NE2 1 
ATOM   1110 N N   . GLU   B 1 50 ? 20.316  -9.407  -24.993 1.00 29.19  ? 49  GLU   B N   1 
ATOM   1111 C CA  . GLU   B 1 50 ? 21.412  -10.201 -24.478 1.00 27.68  ? 49  GLU   B CA  1 
ATOM   1112 C C   . GLU   B 1 50 ? 22.417  -10.489 -25.615 1.00 27.03  ? 49  GLU   B C   1 
ATOM   1113 O O   . GLU   B 1 50 ? 22.098  -10.283 -26.804 1.00 28.99  ? 49  GLU   B O   1 
ATOM   1114 C CB  . GLU   B 1 50 ? 20.861  -11.548 -23.989 1.00 31.49  ? 49  GLU   B CB  1 
ATOM   1115 C CG  . GLU   B 1 50 ? 19.958  -11.393 -22.763 1.00 29.14  ? 49  GLU   B CG  1 
ATOM   1116 C CD  . GLU   B 1 50 ? 19.115  -12.641 -22.525 1.00 31.22  ? 49  GLU   B CD  1 
ATOM   1117 O OE1 . GLU   B 1 50 ? 18.365  -13.051 -23.456 1.00 29.99  ? 49  GLU   B OE1 1 
ATOM   1118 O OE2 . GLU   B 1 50 ? 19.214  -13.244 -21.409 1.00 32.03  ? 49  GLU   B OE2 1 
ATOM   1119 N N   . THR   B 1 51 ? 23.553  -11.066 -25.222 1.00 29.15  ? 50  THR   B N   1 
ATOM   1120 C CA  . THR   B 1 51 ? 24.613  -11.433 -26.161 1.00 30.91  ? 50  THR   B CA  1 
ATOM   1121 C C   . THR   B 1 51 ? 25.108  -12.831 -25.825 1.00 32.47  ? 50  THR   B C   1 
ATOM   1122 O O   . THR   B 1 51 ? 25.076  -13.261 -24.667 1.00 36.95  ? 50  THR   B O   1 
ATOM   1123 C CB  . THR   B 1 51 ? 25.754  -10.400 -26.234 1.00 35.89  ? 50  THR   B CB  1 
ATOM   1124 O OG1 . THR   B 1 51 ? 26.360  -10.322 -24.951 1.00 39.09  ? 50  THR   B OG1 1 
ATOM   1125 C CG2 . THR   B 1 51 ? 25.302  -9.008  -26.622 1.00 33.43  ? 50  THR   B CG2 1 
ATOM   1126 N N   . ALA   B 1 52 ? 25.550  -13.590 -26.847 1.00 30.76  ? 51  ALA   B N   1 
ATOM   1127 C CA  . ALA   B 1 52 ? 26.193  -14.877 -26.665 1.00 32.97  ? 51  ALA   B CA  1 
ATOM   1128 C C   . ALA   B 1 52 ? 27.023  -15.175 -27.909 1.00 31.21  ? 51  ALA   B C   1 
ATOM   1129 O O   . ALA   B 1 52 ? 26.864  -14.502 -28.932 1.00 31.16  ? 51  ALA   B O   1 
ATOM   1130 C CB  . ALA   B 1 52 ? 25.196  -16.016 -26.437 1.00 32.43  ? 51  ALA   B CB  1 
ATOM   1131 N N   . PHE   B 1 53 ? 27.889  -16.184 -27.771 1.00 31.44  ? 52  PHE   B N   1 
ATOM   1132 C CA  . PHE   B 1 53 ? 28.590  -16.730 -28.918 1.00 32.25  ? 52  PHE   B CA  1 
ATOM   1133 C C   . PHE   B 1 53 ? 27.901  -18.016 -29.369 1.00 30.44  ? 52  PHE   B C   1 
ATOM   1134 O O   . PHE   B 1 53 ? 27.761  -18.986 -28.605 1.00 34.37  ? 52  PHE   B O   1 
ATOM   1135 C CB  . PHE   B 1 53 ? 30.054  -16.980 -28.561 1.00 30.87  ? 52  PHE   B CB  1 
ATOM   1136 C CG  . PHE   B 1 53 ? 30.863  -15.764 -28.137 1.00 35.30  ? 52  PHE   B CG  1 
ATOM   1137 C CD1 . PHE   B 1 53 ? 31.108  -14.734 -29.036 1.00 38.74  ? 52  PHE   B CD1 1 
ATOM   1138 C CD2 . PHE   B 1 53 ? 31.407  -15.686 -26.863 1.00 40.21  ? 52  PHE   B CD2 1 
ATOM   1139 C CE1 . PHE   B 1 53 ? 31.849  -13.625 -28.675 1.00 39.55  ? 52  PHE   B CE1 1 
ATOM   1140 C CE2 . PHE   B 1 53 ? 32.139  -14.567 -26.492 1.00 40.12  ? 52  PHE   B CE2 1 
ATOM   1141 C CZ  . PHE   B 1 53 ? 32.361  -13.550 -27.390 1.00 41.37  ? 52  PHE   B CZ  1 
ATOM   1142 N N   . LEU   B 1 54 ? 27.549  -18.061 -30.662 1.00 30.33  ? 53  LEU   B N   1 
ATOM   1143 C CA  . LEU   B 1 54 ? 26.980  -19.263 -31.248 1.00 28.49  ? 53  LEU   B CA  1 
ATOM   1144 C C   . LEU   B 1 54 ? 27.706  -19.622 -32.548 1.00 30.12  ? 53  LEU   B C   1 
ATOM   1145 O O   . LEU   B 1 54 ? 28.176  -18.737 -33.280 1.00 30.08  ? 53  LEU   B O   1 
ATOM   1146 C CB  . LEU   B 1 54 ? 25.485  -19.112 -31.537 1.00 28.67  ? 53  LEU   B CB  1 
ATOM   1147 C CG  . LEU   B 1 54 ? 24.590  -18.971 -30.305 1.00 29.55  ? 53  LEU   B CG  1 
ATOM   1148 C CD1 . LEU   B 1 54 ? 23.194  -18.713 -30.761 1.00 29.54  ? 53  LEU   B CD1 1 
ATOM   1149 C CD2 . LEU   B 1 54 ? 24.754  -20.234 -29.486 1.00 32.08  ? 53  LEU   B CD2 1 
ATOM   1150 N N   . GLY   B 1 55 ? 27.658  -20.911 -32.881 1.00 31.47  ? 54  GLY   B N   1 
ATOM   1151 C CA  . GLY   B 1 55 ? 28.167  -21.431 -34.146 1.00 31.00  ? 54  GLY   B CA  1 
ATOM   1152 C C   . GLY   B 1 55 ? 27.067  -21.506 -35.203 1.00 28.14  ? 54  GLY   B C   1 
ATOM   1153 O O   . GLY   B 1 55 ? 25.871  -21.405 -34.891 1.00 28.26  ? 54  GLY   B O   1 
ATOM   1154 N N   . PRO   B 1 56 ? 27.418  -21.678 -36.507 1.00 28.13  ? 55  PRO   B N   1 
ATOM   1155 C CA  . PRO   B 1 56 ? 26.424  -21.778 -37.573 1.00 29.56  ? 55  PRO   B CA  1 
ATOM   1156 C C   . PRO   B 1 56 ? 25.274  -22.777 -37.473 1.00 25.56  ? 55  PRO   B C   1 
ATOM   1157 O O   . PRO   B 1 56 ? 24.208  -22.535 -38.017 1.00 26.38  ? 55  PRO   B O   1 
ATOM   1158 C CB  . PRO   B 1 56 ? 27.273  -22.054 -38.845 1.00 30.80  ? 55  PRO   B CB  1 
ATOM   1159 C CG  . PRO   B 1 56 ? 28.711  -22.045 -38.437 1.00 34.62  ? 55  PRO   B CG  1 
ATOM   1160 C CD  . PRO   B 1 56 ? 28.803  -21.712 -37.000 1.00 31.26  ? 55  PRO   B CD  1 
ATOM   1161 N N   . LYS   B 1 57 ? 25.479  -23.889 -36.753 1.00 27.32  ? 56  LYS   B N   1 
ATOM   1162 C CA  . LYS   B 1 57 ? 24.425  -24.895 -36.645 1.00 28.76  ? 56  LYS   B CA  1 
ATOM   1163 C C   . LYS   B 1 57 ? 23.180  -24.300 -35.997 1.00 27.84  ? 56  LYS   B C   1 
ATOM   1164 O O   . LYS   B 1 57 ? 22.067  -24.771 -36.228 1.00 28.08  ? 56  LYS   B O   1 
ATOM   1165 C CB  . LYS   B 1 57 ? 24.866  -26.155 -35.877 1.00 32.93  ? 56  LYS   B CB  1 
ATOM   1166 C CG  . LYS   B 1 57 ? 25.015  -26.048 -34.370 1.00 39.46  ? 56  LYS   B CG  1 
ATOM   1167 C CD  . LYS   B 1 57 ? 25.056  -27.448 -33.747 1.00 43.53  ? 56  LYS   B CD  1 
ATOM   1168 C CE  . LYS   B 1 57 ? 25.250  -27.510 -32.255 1.00 44.69  ? 56  LYS   B CE  1 
ATOM   1169 N NZ  . LYS   B 1 57 ? 24.247  -26.806 -31.454 1.00 44.35  ? 56  LYS   B NZ  1 
ATOM   1170 N N   . ASP   B 1 58 ? 23.379  -23.201 -35.232 1.00 26.32  ? 57  ASP   B N   1 
ATOM   1171 C CA  . ASP   B 1 58 ? 22.279  -22.605 -34.473 1.00 28.87  ? 57  ASP   B CA  1 
ATOM   1172 C C   . ASP   B 1 58 ? 21.839  -21.265 -35.057 1.00 26.46  ? 57  ASP   B C   1 
ATOM   1173 O O   . ASP   B 1 58 ? 21.081  -20.544 -34.400 1.00 26.92  ? 57  ASP   B O   1 
ATOM   1174 C CB  . ASP   B 1 58 ? 22.718  -22.416 -33.037 1.00 27.05  ? 57  ASP   B CB  1 
ATOM   1175 C CG  . ASP   B 1 58 ? 22.945  -23.701 -32.246 1.00 31.92  ? 57  ASP   B CG  1 
ATOM   1176 O OD1 . ASP   B 1 58 ? 22.088  -24.613 -32.388 1.00 33.93  ? 57  ASP   B OD1 1 
ATOM   1177 O OD2 . ASP   B 1 58 ? 23.923  -23.710 -31.443 1.00 37.07  ? 57  ASP   B OD2 1 
ATOM   1178 N N   . LEU   B 1 59 ? 22.321  -20.916 -36.270 1.00 25.23  ? 58  LEU   B N   1 
ATOM   1179 C CA  . LEU   B 1 59 ? 22.029  -19.611 -36.866 1.00 25.37  ? 58  LEU   B CA  1 
ATOM   1180 C C   . LEU   B 1 59 ? 21.281  -19.801 -38.173 1.00 25.64  ? 58  LEU   B C   1 
ATOM   1181 O O   . LEU   B 1 59 ? 21.755  -20.489 -39.091 1.00 26.96  ? 58  LEU   B O   1 
ATOM   1182 C CB  . LEU   B 1 59 ? 23.341  -18.867 -37.065 1.00 24.95  ? 58  LEU   B CB  1 
ATOM   1183 C CG  . LEU   B 1 59 ? 24.142  -18.585 -35.806 1.00 24.65  ? 58  LEU   B CG  1 
ATOM   1184 C CD1 . LEU   B 1 59 ? 25.452  -17.908 -36.185 1.00 28.91  ? 58  LEU   B CD1 1 
ATOM   1185 C CD2 . LEU   B 1 59 ? 23.341  -17.723 -34.820 1.00 26.72  ? 58  LEU   B CD2 1 
ATOM   1186 N N   . PHE   B 1 60 ? 20.098  -19.217 -38.247 1.00 24.73  ? 59  PHE   B N   1 
ATOM   1187 C CA  . PHE   B 1 60 ? 19.146  -19.391 -39.334 1.00 25.93  ? 59  PHE   B CA  1 
ATOM   1188 C C   . PHE   B 1 60 ? 18.924  -18.057 -40.042 1.00 25.14  ? 59  PHE   B C   1 
ATOM   1189 O O   . PHE   B 1 60 ? 18.327  -17.135 -39.483 1.00 25.39  ? 59  PHE   B O   1 
ATOM   1190 C CB  . PHE   B 1 60 ? 17.825  -19.948 -38.786 1.00 23.80  ? 59  PHE   B CB  1 
ATOM   1191 C CG  . PHE   B 1 60 ? 17.952  -21.342 -38.186 1.00 24.18  ? 59  PHE   B CG  1 
ATOM   1192 C CD1 . PHE   B 1 60 ? 18.473  -21.523 -36.904 1.00 27.01  ? 59  PHE   B CD1 1 
ATOM   1193 C CD2 . PHE   B 1 60 ? 17.511  -22.433 -38.912 1.00 26.10  ? 59  PHE   B CD2 1 
ATOM   1194 C CE1 . PHE   B 1 60 ? 18.610  -22.803 -36.369 1.00 29.44  ? 59  PHE   B CE1 1 
ATOM   1195 C CE2 . PHE   B 1 60 ? 17.639  -23.721 -38.366 1.00 27.13  ? 59  PHE   B CE2 1 
ATOM   1196 C CZ  . PHE   B 1 60 ? 18.190  -23.895 -37.114 1.00 29.56  ? 59  PHE   B CZ  1 
ATOM   1197 N N   . PRO   B 1 61 ? 19.428  -17.857 -41.276 1.00 27.72  ? 60  PRO   B N   1 
ATOM   1198 C CA  . PRO   B 1 61 ? 19.179  -16.571 -41.967 1.00 27.58  ? 60  PRO   B CA  1 
ATOM   1199 C C   . PRO   B 1 61 ? 17.720  -16.095 -41.918 1.00 26.31  ? 60  PRO   B C   1 
ATOM   1200 O O   . PRO   B 1 61 ? 16.785  -16.844 -42.164 1.00 30.96  ? 60  PRO   B O   1 
ATOM   1201 C CB  . PRO   B 1 61 ? 19.638  -16.937 -43.419 1.00 27.67  ? 60  PRO   B CB  1 
ATOM   1202 C CG  . PRO   B 1 61 ? 20.761  -17.918 -43.214 1.00 37.11  ? 60  PRO   B CG  1 
ATOM   1203 C CD  . PRO   B 1 61 ? 20.283  -18.804 -42.027 1.00 30.88  ? 60  PRO   B CD  1 
ATOM   1204 N N   . TYR   B 1 62 ? 17.510  -14.784 -41.582 1.00 27.42  ? 61  TYR   B N   1 
ATOM   1205 C CA  . TYR   B 1 62 ? 16.207  -14.272 -41.248 1.00 29.50  ? 61  TYR   B CA  1 
ATOM   1206 C C   . TYR   B 1 62 ? 15.251  -14.305 -42.420 1.00 30.02  ? 61  TYR   B C   1 
ATOM   1207 O O   . TYR   B 1 62 ? 14.119  -14.718 -42.227 1.00 33.46  ? 61  TYR   B O   1 
ATOM   1208 C CB  . TYR   B 1 62 ? 16.397  -12.839 -40.728 1.00 31.14  ? 61  TYR   B CB  1 
ATOM   1209 C CG  . TYR   B 1 62 ? 15.079  -12.123 -40.498 1.00 32.56  ? 61  TYR   B CG  1 
ATOM   1210 C CD1 . TYR   B 1 62 ? 14.308  -12.366 -39.379 1.00 34.86  ? 61  TYR   B CD1 1 
ATOM   1211 C CD2 . TYR   B 1 62 ? 14.644  -11.142 -41.387 1.00 39.51  ? 61  TYR   B CD2 1 
ATOM   1212 C CE1 . TYR   B 1 62 ? 13.122  -11.693 -39.159 1.00 36.55  ? 61  TYR   B CE1 1 
ATOM   1213 C CE2 . TYR   B 1 62 ? 13.469  -10.439 -41.176 1.00 41.36  ? 61  TYR   B CE2 1 
ATOM   1214 C CZ  . TYR   B 1 62 ? 12.697  -10.738 -40.069 1.00 41.65  ? 61  TYR   B CZ  1 
ATOM   1215 O OH  . TYR   B 1 62 ? 11.551  -10.063 -39.864 1.00 40.20  ? 61  TYR   B OH  1 
ATOM   1216 N N   . ASP   B 1 63 ? 15.728  -13.876 -43.612 1.00 34.66  ? 62  ASP   B N   1 
ATOM   1217 C CA  . ASP   B 1 63 ? 14.922  -13.922 -44.832 1.00 41.45  ? 62  ASP   B CA  1 
ATOM   1218 C C   . ASP   B 1 63 ? 14.353  -15.308 -45.117 1.00 35.52  ? 62  ASP   B C   1 
ATOM   1219 O O   . ASP   B 1 63 ? 13.137  -15.458 -45.272 1.00 43.21  ? 62  ASP   B O   1 
ATOM   1220 C CB  . ASP   B 1 63 ? 15.633  -13.325 -46.031 1.00 46.59  ? 62  ASP   B CB  1 
ATOM   1221 C CG  . ASP   B 1 63 ? 15.240  -11.884 -46.298 1.00 61.03  ? 62  ASP   B CG  1 
ATOM   1222 O OD1 . ASP   B 1 63 ? 14.591  -11.285 -45.401 1.00 59.59  ? 62  ASP   B OD1 1 
ATOM   1223 O OD2 . ASP   B 1 63 ? 15.553  -11.394 -47.411 1.00 65.80  ? 62  ASP   B OD2 1 
ATOM   1224 N N   . LYS   B 1 64 ? 15.237  -16.297 -45.201 1.00 40.84  ? 63  LYS   B N   1 
ATOM   1225 C CA  . LYS   B 1 64 ? 14.809  -17.658 -45.452 1.00 39.28  ? 63  LYS   B CA  1 
ATOM   1226 C C   . LYS   B 1 64 ? 13.801  -18.120 -44.401 1.00 36.11  ? 63  LYS   B C   1 
ATOM   1227 O O   . LYS   B 1 64 ? 12.866  -18.840 -44.737 1.00 38.39  ? 63  LYS   B O   1 
ATOM   1228 C CB  . LYS   B 1 64 ? 16.023  -18.588 -45.493 1.00 41.17  ? 63  LYS   B CB  1 
ATOM   1229 C CG  . LYS   B 1 64 ? 15.704  -20.027 -45.837 1.00 40.45  ? 63  LYS   B CG  1 
ATOM   1230 C CD  . LYS   B 1 64 ? 16.917  -20.919 -45.638 1.00 47.81  ? 63  LYS   B CD  1 
ATOM   1231 C CE  . LYS   B 1 64 ? 16.785  -22.318 -46.194 1.00 43.75  ? 63  LYS   B CE  1 
ATOM   1232 N NZ  . LYS   B 1 64 ? 15.419  -22.810 -46.379 1.00 47.75  ? 63  LYS   B NZ  1 
ATOM   1233 N N   . SER   B 1 65 ? 13.960  -17.687 -43.140 1.00 35.27  ? 64  SER   B N   1 
ATOM   1234 C CA  . SER   B 1 65 ? 13.322  -18.445 -42.061 1.00 37.00  ? 64  SER   B CA  1 
ATOM   1235 C C   . SER   B 1 65 ? 12.216  -17.685 -41.307 1.00 37.19  ? 64  SER   B C   1 
ATOM   1236 O O   . SER   B 1 65 ? 11.555  -18.251 -40.441 1.00 35.90  ? 64  SER   B O   1 
ATOM   1237 C CB  . SER   B 1 65 ? 14.383  -19.071 -41.175 1.00 38.07  ? 64  SER   B CB  1 
ATOM   1238 O OG  . SER   B 1 65 ? 15.083  -18.089 -40.430 1.00 48.33  ? 64  SER   B OG  1 
ATOM   1239 N N   . LYS   B 1 66 ? 11.901  -16.440 -41.704 1.00 35.46  ? 65  LYS   B N   1 
ATOM   1240 C CA  . LYS   B 1 66 ? 11.008  -15.617 -40.892 1.00 35.03  ? 65  LYS   B CA  1 
ATOM   1241 C C   . LYS   B 1 66 ? 9.562   -16.115 -40.895 1.00 35.84  ? 65  LYS   B C   1 
ATOM   1242 O O   . LYS   B 1 66 ? 8.840   -15.925 -39.914 1.00 37.35  ? 65  LYS   B O   1 
ATOM   1243 C CB  . LYS   B 1 66 ? 11.044  -14.128 -41.260 1.00 35.37  ? 65  LYS   B CB  1 
ATOM   1244 C CG  . LYS   B 1 66 ? 10.483  -13.774 -42.633 1.00 38.39  ? 65  LYS   B CG  1 
ATOM   1245 C CD  . LYS   B 1 66 ? 10.594  -12.270 -42.899 1.00 51.47  ? 65  LYS   B CD  1 
ATOM   1246 C CE  . LYS   B 1 66 ? 10.353  -11.896 -44.348 1.00 59.84  ? 65  LYS   B CE  1 
ATOM   1247 N NZ  . LYS   B 1 66 ? 9.142   -12.471 -44.961 1.00 68.59  ? 65  LYS   B NZ  1 
ATOM   1248 N N   . ASP   B 1 67 ? 9.104   -16.739 -41.982 1.00 38.58  ? 66  ASP   B N   1 
ATOM   1249 C CA  . ASP   B 1 67 ? 7.705   -17.124 -41.982 1.00 42.75  ? 66  ASP   B CA  1 
ATOM   1250 C C   . ASP   B 1 67 ? 7.481   -18.285 -41.009 1.00 45.73  ? 66  ASP   B C   1 
ATOM   1251 O O   . ASP   B 1 67 ? 6.413   -18.392 -40.402 1.00 47.63  ? 66  ASP   B O   1 
ATOM   1252 C CB  . ASP   B 1 67 ? 7.100   -17.129 -43.381 1.00 54.09  ? 66  ASP   B CB  1 
ATOM   1253 C CG  . ASP   B 1 67 ? 7.563   -18.216 -44.335 1.00 73.90  ? 66  ASP   B CG  1 
ATOM   1254 O OD1 . ASP   B 1 67 ? 7.550   -17.950 -45.563 1.00 85.22  ? 66  ASP   B OD1 1 
ATOM   1255 O OD2 . ASP   B 1 67 ? 7.887   -19.325 -43.853 1.00 85.39  ? 66  ASP   B OD2 1 
ATOM   1256 N N   . LYS   B 1 68 ? 8.522   -19.101 -40.828 1.00 39.26  ? 67  LYS   B N   1 
ATOM   1257 C CA  . LYS   B 1 68 ? 8.486   -20.264 -39.957 1.00 37.28  ? 67  LYS   B CA  1 
ATOM   1258 C C   . LYS   B 1 68 ? 8.717   -19.884 -38.494 1.00 35.68  ? 67  LYS   B C   1 
ATOM   1259 O O   . LYS   B 1 68 ? 7.995   -20.397 -37.635 1.00 38.53  ? 67  LYS   B O   1 
ATOM   1260 C CB  . LYS   B 1 68 ? 9.552   -21.258 -40.411 1.00 39.10  ? 67  LYS   B CB  1 
ATOM   1261 C CG  . LYS   B 1 68 ? 9.631   -22.574 -39.657 1.00 47.19  ? 67  LYS   B CG  1 
ATOM   1262 C CD  . LYS   B 1 68 ? 10.896  -23.311 -40.090 1.00 54.24  ? 67  LYS   B CD  1 
ATOM   1263 C CE  . LYS   B 1 68 ? 10.812  -24.802 -40.133 1.00 57.85  ? 67  LYS   B CE  1 
ATOM   1264 N NZ  . LYS   B 1 68 ? 9.782   -25.333 -39.237 1.00 57.94  ? 67  LYS   B NZ  1 
ATOM   1265 N N   . TYR   B 1 69 ? 9.690   -18.993 -38.219 1.00 30.76  ? 68  TYR   B N   1 
ATOM   1266 C CA  . TYR   B 1 69 ? 10.153  -18.709 -36.860 1.00 27.46  ? 68  TYR   B CA  1 
ATOM   1267 C C   . TYR   B 1 69 ? 9.649   -17.354 -36.360 1.00 31.89  ? 68  TYR   B C   1 
ATOM   1268 O O   . TYR   B 1 69 ? 9.763   -17.069 -35.167 1.00 33.91  ? 68  TYR   B O   1 
ATOM   1269 C CB  . TYR   B 1 69 ? 11.682  -18.770 -36.704 1.00 28.19  ? 68  TYR   B CB  1 
ATOM   1270 C CG  . TYR   B 1 69 ? 12.313  -20.132 -36.982 1.00 29.37  ? 68  TYR   B CG  1 
ATOM   1271 C CD1 . TYR   B 1 69 ? 11.762  -21.287 -36.435 1.00 28.57  ? 68  TYR   B CD1 1 
ATOM   1272 C CD2 . TYR   B 1 69 ? 13.426  -20.265 -37.807 1.00 31.51  ? 68  TYR   B CD2 1 
ATOM   1273 C CE1 . TYR   B 1 69 ? 12.308  -22.538 -36.714 1.00 30.20  ? 68  TYR   B CE1 1 
ATOM   1274 C CE2 . TYR   B 1 69 ? 13.958  -21.507 -38.125 1.00 33.73  ? 68  TYR   B CE2 1 
ATOM   1275 C CZ  . TYR   B 1 69 ? 13.411  -22.640 -37.540 1.00 32.10  ? 68  TYR   B CZ  1 
ATOM   1276 O OH  . TYR   B 1 69 ? 13.941  -23.865 -37.823 1.00 32.71  ? 68  TYR   B OH  1 
ATOM   1277 N N   . GLY   B 1 70 ? 9.177   -16.482 -37.263 1.00 33.31  ? 69  GLY   B N   1 
ATOM   1278 C CA  . GLY   B 1 70 ? 8.878   -15.109 -36.878 1.00 35.21  ? 69  GLY   B CA  1 
ATOM   1279 C C   . GLY   B 1 70 ? 7.452   -14.910 -36.353 1.00 37.89  ? 69  GLY   B C   1 
ATOM   1280 O O   . GLY   B 1 70 ? 6.850   -13.876 -36.599 1.00 39.23  ? 69  GLY   B O   1 
ATOM   1281 N N   . LYS   B 1 71 ? 6.898   -15.887 -35.624 1.00 39.50  ? 70  LYS   B N   1 
ATOM   1282 C CA  . LYS   B 1 71 ? 5.544   -15.723 -35.122 1.00 40.15  ? 70  LYS   B CA  1 
ATOM   1283 C C   . LYS   B 1 71 ? 5.603   -15.326 -33.658 1.00 43.84  ? 70  LYS   B C   1 
ATOM   1284 O O   . LYS   B 1 71 ? 6.481   -15.779 -32.928 1.00 36.60  ? 70  LYS   B O   1 
ATOM   1285 C CB  . LYS   B 1 71 ? 4.672   -16.979 -35.177 1.00 42.73  ? 70  LYS   B CB  1 
ATOM   1286 C CG  . LYS   B 1 71 ? 4.018   -17.202 -36.535 1.00 54.74  ? 70  LYS   B CG  1 
ATOM   1287 C CD  . LYS   B 1 71 ? 4.805   -18.120 -37.458 1.00 61.58  ? 70  LYS   B CD  1 
ATOM   1288 C CE  . LYS   B 1 71 ? 4.051   -18.454 -38.714 1.00 65.55  ? 70  LYS   B CE  1 
ATOM   1289 N NZ  . LYS   B 1 71 ? 4.140   -17.370 -39.701 1.00 69.00  ? 70  LYS   B NZ  1 
ATOM   1290 N N   . PRO   B 1 72 ? 4.660   -14.491 -33.173 1.00 41.52  ? 71  PRO   B N   1 
ATOM   1291 C CA  . PRO   B 1 72 ? 4.674   -14.117 -31.761 1.00 38.45  ? 71  PRO   B CA  1 
ATOM   1292 C C   . PRO   B 1 72 ? 4.481   -15.279 -30.794 1.00 34.08  ? 71  PRO   B C   1 
ATOM   1293 O O   . PRO   B 1 72 ? 3.908   -16.323 -31.136 1.00 37.44  ? 71  PRO   B O   1 
ATOM   1294 C CB  . PRO   B 1 72 ? 3.607   -13.035 -31.654 1.00 38.54  ? 71  PRO   B CB  1 
ATOM   1295 C CG  . PRO   B 1 72 ? 3.519   -12.527 -33.075 1.00 42.85  ? 71  PRO   B CG  1 
ATOM   1296 C CD  . PRO   B 1 72 ? 3.640   -13.775 -33.951 1.00 38.68  ? 71  PRO   B CD  1 
ATOM   1297 N N   . ASN   B 1 73 ? 5.039   -15.097 -29.600 1.00 36.14  ? 72  ASN   B N   1 
ATOM   1298 C CA  . ASN   B 1 73 ? 4.843   -16.065 -28.532 1.00 33.98  ? 72  ASN   B CA  1 
ATOM   1299 C C   . ASN   B 1 73 ? 4.806   -15.325 -27.191 1.00 36.01  ? 72  ASN   B C   1 
ATOM   1300 O O   . ASN   B 1 73 ? 4.857   -14.086 -27.140 1.00 42.82  ? 72  ASN   B O   1 
ATOM   1301 C CB  . ASN   B 1 73 ? 5.865   -17.199 -28.605 1.00 36.21  ? 72  ASN   B CB  1 
ATOM   1302 C CG  . ASN   B 1 73 ? 7.285   -16.758 -28.333 1.00 31.09  ? 72  ASN   B CG  1 
ATOM   1303 O OD1 . ASN   B 1 73 ? 7.553   -16.045 -27.347 1.00 31.34  ? 72  ASN   B OD1 1 
ATOM   1304 N ND2 . ASN   B 1 73 ? 8.213   -17.169 -29.205 1.00 30.72  ? 72  ASN   B ND2 1 
ATOM   1305 N N   . LYS   B 1 74 ? 4.772   -16.097 -26.101 1.00 37.77  ? 73  LYS   B N   1 
ATOM   1306 C CA  . LYS   B 1 74 ? 4.657   -15.517 -24.766 1.00 40.34  ? 73  LYS   B CA  1 
ATOM   1307 C C   . LYS   B 1 74 ? 5.982   -15.502 -23.997 1.00 39.66  ? 73  LYS   B C   1 
ATOM   1308 O O   . LYS   B 1 74 ? 5.974   -15.308 -22.777 1.00 40.33  ? 73  LYS   B O   1 
ATOM   1309 C CB  . LYS   B 1 74 ? 3.717   -16.355 -23.886 1.00 43.50  ? 73  LYS   B CB  1 
ATOM   1310 C CG  . LYS   B 1 74 ? 2.261   -16.368 -24.282 1.00 44.27  ? 73  LYS   B CG  1 
ATOM   1311 C CD  . LYS   B 1 74 ? 1.702   -17.788 -24.184 1.00 54.97  ? 73  LYS   B CD  1 
ATOM   1312 N N   . ARG   B 1 75 ? 7.129   -15.734 -24.668 1.00 29.88  ? 74  ARG   B N   1 
ATOM   1313 C CA  . ARG   B 1 75 ? 8.410   -15.571 -23.996 1.00 29.22  ? 74  ARG   B CA  1 
ATOM   1314 C C   . ARG   B 1 75 ? 8.731   -14.078 -23.830 1.00 31.18  ? 74  ARG   B C   1 
ATOM   1315 O O   . ARG   B 1 75 ? 8.585   -13.276 -24.749 1.00 30.85  ? 74  ARG   B O   1 
ATOM   1316 C CB  . ARG   B 1 75 ? 9.526   -16.340 -24.721 1.00 29.06  ? 74  ARG   B CB  1 
ATOM   1317 C CG  . ARG   B 1 75 ? 9.405   -17.845 -24.916 1.00 28.18  ? 74  ARG   B CG  1 
ATOM   1318 C CD  . ARG   B 1 75 ? 9.174   -18.571 -23.616 1.00 28.60  ? 74  ARG   B CD  1 
ATOM   1319 N NE  . ARG   B 1 75 ? 9.402   -20.014 -23.844 1.00 28.61  ? 74  ARG   B NE  1 
ATOM   1320 C CZ  . ARG   B 1 75 ? 10.543  -20.671 -23.667 1.00 30.23  ? 74  ARG   B CZ  1 
ATOM   1321 N NH1 . ARG   B 1 75 ? 11.642  -20.075 -23.232 1.00 34.62  ? 74  ARG   B NH1 1 
ATOM   1322 N NH2 . ARG   B 1 75 ? 10.594  -21.960 -24.019 1.00 36.49  ? 74  ARG   B NH2 1 
ATOM   1323 N N   . LYS   B 1 76 ? 9.129   -13.691 -22.616 1.00 31.18  ? 75  LYS   B N   1 
ATOM   1324 C CA  . LYS   B 1 76 ? 9.544   -12.333 -22.309 1.00 28.66  ? 75  LYS   B CA  1 
ATOM   1325 C C   . LYS   B 1 76 ? 10.647  -11.850 -23.275 1.00 25.28  ? 75  LYS   B C   1 
ATOM   1326 O O   . LYS   B 1 76 ? 11.749  -12.453 -23.320 1.00 27.41  ? 75  LYS   B O   1 
ATOM   1327 C CB  . LYS   B 1 76 ? 10.087  -12.241 -20.874 1.00 30.95  ? 75  LYS   B CB  1 
ATOM   1328 C CG  . LYS   B 1 76 ? 10.420  -10.804 -20.467 1.00 31.52  ? 75  LYS   B CG  1 
ATOM   1329 C CD  . LYS   B 1 76 ? 10.783  -10.725 -18.982 1.00 33.55  ? 75  LYS   B CD  1 
ATOM   1330 C CE  . LYS   B 1 76 ? 11.063  -9.321  -18.539 1.00 39.73  ? 75  LYS   B CE  1 
ATOM   1331 N NZ  . LYS   B 1 76 ? 11.492  -9.320  -17.131 1.00 43.94  ? 75  LYS   B NZ  1 
ATOM   1332 N N   . GLY   B 1 77 ? 10.281  -10.765 -23.981 1.00 26.02  ? 76  GLY   B N   1 
ATOM   1333 C CA  . GLY   B 1 77 ? 11.208  -10.049 -24.871 1.00 27.16  ? 76  GLY   B CA  1 
ATOM   1334 C C   . GLY   B 1 77 ? 11.061  -10.494 -26.318 1.00 30.97  ? 76  GLY   B C   1 
ATOM   1335 O O   . GLY   B 1 77 ? 11.596  -9.845  -27.208 1.00 30.11  ? 76  GLY   B O   1 
ATOM   1336 N N   . PHE   B 1 78 ? 10.364  -11.596 -26.563 1.00 27.14  ? 77  PHE   B N   1 
ATOM   1337 C CA  . PHE   B 1 78 ? 10.283  -12.120 -27.928 1.00 26.90  ? 77  PHE   B CA  1 
ATOM   1338 C C   . PHE   B 1 78 ? 9.524   -11.163 -28.851 1.00 29.50  ? 77  PHE   B C   1 
ATOM   1339 O O   . PHE   B 1 78 ? 9.975   -10.846 -29.961 1.00 28.82  ? 77  PHE   B O   1 
ATOM   1340 C CB  . PHE   B 1 78 ? 9.532   -13.450 -27.951 1.00 25.99  ? 77  PHE   B CB  1 
ATOM   1341 C CG  . PHE   B 1 78 ? 9.784   -14.161 -29.265 1.00 25.99  ? 77  PHE   B CG  1 
ATOM   1342 C CD1 . PHE   B 1 78 ? 10.879  -15.000 -29.360 1.00 24.81  ? 77  PHE   B CD1 1 
ATOM   1343 C CD2 . PHE   B 1 78 ? 8.905   -14.039 -30.339 1.00 28.05  ? 77  PHE   B CD2 1 
ATOM   1344 C CE1 . PHE   B 1 78 ? 11.130  -15.691 -30.561 1.00 26.00  ? 77  PHE   B CE1 1 
ATOM   1345 C CE2 . PHE   B 1 78 ? 9.152   -14.743 -31.527 1.00 27.85  ? 77  PHE   B CE2 1 
ATOM   1346 C CZ  . PHE   B 1 78 ? 10.270  -15.574 -31.613 1.00 27.82  ? 77  PHE   B CZ  1 
ATOM   1347 N N   . ASN   B 1 79 ? 8.327   -10.718 -28.462 1.00 29.47  ? 78  ASN   B N   1 
ATOM   1348 C CA  . ASN   B 1 79 ? 7.539   -9.890  -29.371 1.00 31.34  ? 78  ASN   B CA  1 
ATOM   1349 C C   . ASN   B 1 79 ? 8.236   -8.532  -29.574 1.00 30.89  ? 78  ASN   B C   1 
ATOM   1350 O O   . ASN   B 1 79 ? 8.145   -7.945  -30.679 1.00 30.36  ? 78  ASN   B O   1 
ATOM   1351 C CB  . ASN   B 1 79 ? 6.059   -9.845  -28.969 1.00 35.14  ? 78  ASN   B CB  1 
ATOM   1352 C CG  . ASN   B 1 79 ? 5.342   -11.179 -29.039 1.00 39.85  ? 78  ASN   B CG  1 
ATOM   1353 O OD1 . ASN   B 1 79 ? 5.842   -12.153 -29.620 1.00 36.46  ? 78  ASN   B OD1 1 
ATOM   1354 N ND2 . ASN   B 1 79 ? 4.152   -11.254 -28.443 1.00 38.17  ? 78  ASN   B ND2 1 
ATOM   1355 N N   . GLU   B 1 80 ? 8.969   -8.057  -28.556 1.00 30.52  ? 79  GLU   B N   1 
ATOM   1356 C CA  . GLU   B 1 80 ? 9.704   -6.810  -28.696 1.00 34.41  ? 79  GLU   B CA  1 
ATOM   1357 C C   . GLU   B 1 80 ? 10.848  -7.043  -29.689 1.00 30.13  ? 79  GLU   B C   1 
ATOM   1358 O O   . GLU   B 1 80 ? 11.109  -6.164  -30.525 1.00 30.04  ? 79  GLU   B O   1 
ATOM   1359 C CB  . GLU   B 1 80 ? 10.327  -6.327  -27.395 1.00 34.15  ? 79  GLU   B CB  1 
ATOM   1360 C CG  . GLU   B 1 80 ? 9.327   -5.674  -26.450 1.00 44.12  ? 79  GLU   B CG  1 
ATOM   1361 N N   . GLY   B 1 81 ? 11.423  -8.262  -29.643 1.00 28.04  ? 80  GLY   B N   1 
ATOM   1362 C CA  . GLY   B 1 81 ? 12.516  -8.646  -30.546 1.00 29.91  ? 80  GLY   B CA  1 
ATOM   1363 C C   . GLY   B 1 81 ? 12.047  -8.703  -31.994 1.00 28.04  ? 80  GLY   B C   1 
ATOM   1364 O O   . GLY   B 1 81 ? 12.803  -8.276  -32.910 1.00 26.75  ? 80  GLY   B O   1 
ATOM   1365 N N   . LEU   B 1 82 ? 10.821  -9.178  -32.205 1.00 27.46  ? 81  LEU   B N   1 
ATOM   1366 C CA  . LEU   B 1 82 ? 10.186  -9.219  -33.521 1.00 28.96  ? 81  LEU   B CA  1 
ATOM   1367 C C   . LEU   B 1 82 ? 10.098  -7.790  -34.052 1.00 28.77  ? 81  LEU   B C   1 
ATOM   1368 O O   . LEU   B 1 82 ? 10.355  -7.547  -35.239 1.00 29.07  ? 81  LEU   B O   1 
ATOM   1369 C CB  . LEU   B 1 82 ? 8.831   -9.952  -33.546 1.00 31.32  ? 81  LEU   B CB  1 
ATOM   1370 C CG  . LEU   B 1 82 ? 8.904   -11.478 -33.365 1.00 29.13  ? 81  LEU   B CG  1 
ATOM   1371 C CD1 . LEU   B 1 82 ? 7.525   -12.138 -33.395 1.00 31.78  ? 81  LEU   B CD1 1 
ATOM   1372 C CD2 . LEU   B 1 82 ? 9.878   -12.135 -34.375 1.00 29.69  ? 81  LEU   B CD2 1 
ATOM   1373 N N   . TRP   B 1 83 ? 9.727   -6.865  -33.153 1.00 28.83  ? 82  TRP   B N   1 
ATOM   1374 C CA  . TRP   B 1 83 ? 9.516   -5.476  -33.535 1.00 30.88  ? 82  TRP   B CA  1 
ATOM   1375 C C   . TRP   B 1 83 ? 10.838  -4.881  -34.007 1.00 29.09  ? 82  TRP   B C   1 
ATOM   1376 O O   . TRP   B 1 83 ? 10.904  -4.273  -35.086 1.00 29.28  ? 82  TRP   B O   1 
ATOM   1377 C CB  . TRP   B 1 83 ? 8.905   -4.635  -32.402 1.00 32.31  ? 82  TRP   B CB  1 
ATOM   1378 C CG  . TRP   B 1 83 ? 8.593   -3.240  -32.896 1.00 31.07  ? 82  TRP   B CG  1 
ATOM   1379 C CD1 . TRP   B 1 83 ? 7.428   -2.838  -33.476 1.00 39.00  ? 82  TRP   B CD1 1 
ATOM   1380 C CD2 . TRP   B 1 83 ? 9.493   -2.118  -32.953 1.00 37.47  ? 82  TRP   B CD2 1 
ATOM   1381 N NE1 . TRP   B 1 83 ? 7.534   -1.525  -33.868 1.00 41.20  ? 82  TRP   B NE1 1 
ATOM   1382 C CE2 . TRP   B 1 83 ? 8.784   -1.062  -33.560 1.00 34.86  ? 82  TRP   B CE2 1 
ATOM   1383 C CE3 . TRP   B 1 83 ? 10.822  -1.903  -32.550 1.00 33.72  ? 82  TRP   B CE3 1 
ATOM   1384 C CZ2 . TRP   B 1 83 ? 9.362   0.193   -33.763 1.00 35.13  ? 82  TRP   B CZ2 1 
ATOM   1385 C CZ3 . TRP   B 1 83 ? 11.383  -0.658  -32.728 1.00 39.52  ? 82  TRP   B CZ3 1 
ATOM   1386 C CH2 . TRP   B 1 83 ? 10.656  0.373   -33.330 1.00 31.97  ? 82  TRP   B CH2 1 
ATOM   1387 N N   . GLU   B 1 84 ? 11.898  -5.173  -33.253 1.00 26.01  ? 83  GLU   B N   1 
ATOM   1388 C CA  . GLU   B 1 84 ? 13.204  -4.600  -33.472 1.00 29.00  ? 83  GLU   B CA  1 
ATOM   1389 C C   . GLU   B 1 84 ? 13.815  -5.123  -34.765 1.00 28.11  ? 83  GLU   B C   1 
ATOM   1390 O O   . GLU   B 1 84 ? 14.405  -4.335  -35.513 1.00 27.70  ? 83  GLU   B O   1 
ATOM   1391 C CB  . GLU   B 1 84 ? 14.141  -4.860  -32.314 1.00 27.61  ? 83  GLU   B CB  1 
ATOM   1392 C CG  . GLU   B 1 84 ? 13.691  -4.108  -31.069 1.00 29.77  ? 83  GLU   B CG  1 
ATOM   1393 C CD  . GLU   B 1 84 ? 14.526  -4.508  -29.902 1.00 30.26  ? 83  GLU   B CD  1 
ATOM   1394 O OE1 . GLU   B 1 84 ? 15.499  -5.316  -29.949 1.00 29.17  ? 83  GLU   B OE1 1 
ATOM   1395 O OE2 . GLU   B 1 84 ? 14.164  -3.898  -28.832 1.00 32.91  ? 83  GLU   B OE2 1 
ATOM   1396 N N   . ILE   B 1 85 ? 13.717  -6.428  -35.008 1.00 27.78  ? 84  ILE   B N   1 
ATOM   1397 C CA  . ILE   B 1 85 ? 14.383  -6.991  -36.189 1.00 25.16  ? 84  ILE   B CA  1 
ATOM   1398 C C   . ILE   B 1 85 ? 13.723  -6.432  -37.465 1.00 25.90  ? 84  ILE   B C   1 
ATOM   1399 O O   . ILE   B 1 85 ? 14.418  -6.227  -38.472 1.00 27.63  ? 84  ILE   B O   1 
ATOM   1400 C CB  . ILE   B 1 85 ? 14.465  -8.529  -36.137 1.00 24.55  ? 84  ILE   B CB  1 
ATOM   1401 C CG1 . ILE   B 1 85 ? 15.545  -9.037  -37.147 1.00 26.02  ? 84  ILE   B CG1 1 
ATOM   1402 C CG2 . ILE   B 1 85 ? 13.101  -9.159  -36.411 1.00 26.93  ? 84  ILE   B CG2 1 
ATOM   1403 C CD1 . ILE   B 1 85 ? 16.022  -10.458 -36.826 1.00 26.96  ? 84  ILE   B CD1 1 
ATOM   1404 N N   . GLN   B 1 86 ? 12.408  -6.175  -37.390 1.00 26.96  ? 85  GLN   B N   1 
ATOM   1405 C CA  . GLN   B 1 86 ? 11.584  -5.623  -38.458 1.00 29.21  ? 85  GLN   B CA  1 
ATOM   1406 C C   . GLN   B 1 86 ? 11.915  -4.145  -38.674 1.00 32.62  ? 85  GLN   B C   1 
ATOM   1407 O O   . GLN   B 1 86 ? 12.062  -3.701  -39.820 1.00 34.75  ? 85  GLN   B O   1 
ATOM   1408 C CB  . GLN   B 1 86 ? 10.105  -5.910  -38.161 1.00 33.73  ? 85  GLN   B CB  1 
ATOM   1409 C CG  . GLN   B 1 86 ? 9.605   -7.288  -38.618 1.00 50.22  ? 85  GLN   B CG  1 
ATOM   1410 C CD  . GLN   B 1 86 ? 8.563   -7.977  -37.740 1.00 55.51  ? 85  GLN   B CD  1 
ATOM   1411 O OE1 . GLN   B 1 86 ? 7.416   -7.520  -37.564 1.00 59.60  ? 85  GLN   B OE1 1 
ATOM   1412 N NE2 . GLN   B 1 86 ? 8.950   -9.139  -37.213 1.00 45.32  ? 85  GLN   B NE2 1 
ATOM   1413 N N   . ASN   B 1 87 ? 11.993  -3.367  -37.587 1.00 28.10  ? 86  ASN   B N   1 
ATOM   1414 C CA  . ASN   B 1 87 ? 11.896  -1.911  -37.756 1.00 26.94  ? 86  ASN   B CA  1 
ATOM   1415 C C   . ASN   B 1 87 ? 13.194  -1.154  -37.527 1.00 28.49  ? 86  ASN   B C   1 
ATOM   1416 O O   . ASN   B 1 87 ? 13.299  -0.009  -37.993 1.00 29.77  ? 86  ASN   B O   1 
ATOM   1417 C CB  . ASN   B 1 87 ? 10.938  -1.311  -36.721 1.00 33.86  ? 86  ASN   B CB  1 
ATOM   1418 C CG  . ASN   B 1 87 ? 9.542   -1.786  -37.011 1.00 39.19  ? 86  ASN   B CG  1 
ATOM   1419 O OD1 . ASN   B 1 87 ? 8.911   -1.293  -37.952 1.00 45.13  ? 86  ASN   B OD1 1 
ATOM   1420 N ND2 . ASN   B 1 87 ? 9.084   -2.800  -36.289 1.00 43.62  ? 86  ASN   B ND2 1 
ATOM   1421 N N   . ASN   B 1 88 ? 14.146  -1.700  -36.764 1.00 27.94  ? 87  ASN   B N   1 
ATOM   1422 C CA  . ASN   B 1 88 ? 15.416  -1.019  -36.547 1.00 29.54  ? 87  ASN   B CA  1 
ATOM   1423 C C   . ASN   B 1 88 ? 16.475  -2.028  -36.146 1.00 28.41  ? 87  ASN   B C   1 
ATOM   1424 O O   . ASN   B 1 88 ? 17.107  -1.965  -35.075 1.00 26.37  ? 87  ASN   B O   1 
ATOM   1425 C CB  . ASN   B 1 88 ? 15.327  0.148   -35.559 1.00 33.46  ? 87  ASN   B CB  1 
ATOM   1426 C CG  . ASN   B 1 88 ? 16.423  1.167   -35.779 1.00 30.95  ? 87  ASN   B CG  1 
ATOM   1427 O OD1 . ASN   B 1 88 ? 17.439  0.920   -36.443 1.00 33.03  ? 87  ASN   B OD1 1 
ATOM   1428 N ND2 . ASN   B 1 88 ? 16.206  2.366   -35.243 1.00 37.16  ? 87  ASN   B ND2 1 
ATOM   1429 N N   . PRO   B 1 89 ? 16.739  -3.001  -37.058 1.00 27.75  ? 88  PRO   B N   1 
ATOM   1430 C CA  . PRO   B 1 89 ? 17.689  -4.063  -36.732 1.00 26.83  ? 88  PRO   B CA  1 
ATOM   1431 C C   . PRO   B 1 89 ? 19.124  -3.625  -36.479 1.00 24.42  ? 88  PRO   B C   1 
ATOM   1432 O O   . PRO   B 1 89 ? 19.901  -4.357  -35.910 1.00 26.62  ? 88  PRO   B O   1 
ATOM   1433 C CB  . PRO   B 1 89 ? 17.601  -4.997  -37.960 1.00 27.04  ? 88  PRO   B CB  1 
ATOM   1434 C CG  . PRO   B 1 89 ? 17.134  -4.079  -39.116 1.00 25.82  ? 88  PRO   B CG  1 
ATOM   1435 C CD  . PRO   B 1 89 ? 16.184  -3.110  -38.430 1.00 27.60  ? 88  PRO   B CD  1 
ATOM   1436 N N   . HIS   B 1 90 ? 19.525  -2.428  -37.010 1.00 25.14  ? 89  HIS   B N   1 
ATOM   1437 C CA  . HIS   B 1 90 ? 20.930  -2.044  -36.940 1.00 24.93  ? 89  HIS   B CA  1 
ATOM   1438 C C   . HIS   B 1 90 ? 21.192  -0.947  -35.891 1.00 26.62  ? 89  HIS   B C   1 
ATOM   1439 O O   . HIS   B 1 90 ? 22.332  -0.476  -35.793 1.00 28.50  ? 89  HIS   B O   1 
ATOM   1440 C CB  . HIS   B 1 90 ? 21.443  -1.617  -38.342 1.00 26.02  ? 89  HIS   B CB  1 
ATOM   1441 C CG  . HIS   B 1 90 ? 21.245  -2.696  -39.361 1.00 27.38  ? 89  HIS   B CG  1 
ATOM   1442 N ND1 . HIS   B 1 90 ? 21.816  -3.929  -39.214 1.00 26.12  ? 89  HIS   B ND1 1 
ATOM   1443 C CD2 . HIS   B 1 90 ? 20.575  -2.713  -40.523 1.00 27.49  ? 89  HIS   B CD2 1 
ATOM   1444 C CE1 . HIS   B 1 90 ? 21.487  -4.663  -40.278 1.00 27.34  ? 89  HIS   B CE1 1 
ATOM   1445 N NE2 . HIS   B 1 90 ? 20.724  -3.950  -41.069 1.00 28.08  ? 89  HIS   B NE2 1 
ATOM   1446 N N   . ALA   B 1 91 ? 20.189  -0.667  -35.050 1.00 27.36  ? 90  ALA   B N   1 
ATOM   1447 C CA  . ALA   B 1 91 ? 20.338  0.368   -34.017 1.00 28.56  ? 90  ALA   B CA  1 
ATOM   1448 C C   . ALA   B 1 91 ? 21.304  -0.042  -32.912 1.00 32.58  ? 90  ALA   B C   1 
ATOM   1449 O O   . ALA   B 1 91 ? 21.532  -1.217  -32.651 1.00 30.47  ? 90  ALA   B O   1 
ATOM   1450 C CB  . ALA   B 1 91 ? 18.984  0.718   -33.463 1.00 28.67  ? 90  ALA   B CB  1 
ATOM   1451 N N   . SER   B 1 92 ? 21.795  0.969   -32.156 1.00 32.38  ? 91  SER   B N   1 
ATOM   1452 C CA  . SER   B 1 92 ? 22.461  0.735   -30.896 1.00 35.59  ? 91  SER   B CA  1 
ATOM   1453 C C   . SER   B 1 92 ? 21.391  0.544   -29.823 1.00 37.92  ? 91  SER   B C   1 
ATOM   1454 O O   . SER   B 1 92 ? 20.508  1.405   -29.681 1.00 39.99  ? 91  SER   B O   1 
ATOM   1455 C CB  . SER   B 1 92 ? 23.297  1.974   -30.558 1.00 40.66  ? 91  SER   B CB  1 
ATOM   1456 O OG  . SER   B 1 92 ? 23.689  1.908   -29.200 1.00 45.44  ? 91  SER   B OG  1 
ATOM   1457 N N   . TYR   B 1 93 ? 21.495  -0.570  -29.083 1.00 37.11  ? 92  TYR   B N   1 
ATOM   1458 C CA  . TYR   B 1 93 ? 20.584  -0.932  -28.016 1.00 40.34  ? 92  TYR   B CA  1 
ATOM   1459 C C   . TYR   B 1 93 ? 21.296  -0.782  -26.672 1.00 50.10  ? 92  TYR   B C   1 
ATOM   1460 O O   . TYR   B 1 93 ? 20.761  -1.215  -25.657 1.00 54.84  ? 92  TYR   B O   1 
ATOM   1461 C CB  . TYR   B 1 93 ? 19.970  -2.320  -28.266 1.00 35.84  ? 92  TYR   B CB  1 
ATOM   1462 C CG  . TYR   B 1 93 ? 18.984  -2.243  -29.413 1.00 29.70  ? 92  TYR   B CG  1 
ATOM   1463 C CD1 . TYR   B 1 93 ? 17.668  -1.861  -29.188 1.00 33.30  ? 92  TYR   B CD1 1 
ATOM   1464 C CD2 . TYR   B 1 93 ? 19.343  -2.571  -30.722 1.00 34.82  ? 92  TYR   B CD2 1 
ATOM   1465 C CE1 . TYR   B 1 93 ? 16.731  -1.738  -30.196 1.00 32.42  ? 92  TYR   B CE1 1 
ATOM   1466 C CE2 . TYR   B 1 93 ? 18.417  -2.418  -31.745 1.00 29.37  ? 92  TYR   B CE2 1 
ATOM   1467 C CZ  . TYR   B 1 93 ? 17.107  -2.062  -31.486 1.00 32.31  ? 92  TYR   B CZ  1 
ATOM   1468 O OH  . TYR   B 1 93 ? 16.158  -1.943  -32.449 1.00 33.19  ? 92  TYR   B OH  1 
ATOM   1469 N N   . SER   B 1 94 ? 22.473  -0.129  -26.694 1.00 62.70  ? 93  SER   B N   1 
ATOM   1470 C CA  . SER   B 1 94 ? 23.202  0.292   -25.501 1.00 66.41  ? 93  SER   B CA  1 
ATOM   1471 C C   . SER   B 1 94 ? 22.224  0.932   -24.503 1.00 76.25  ? 93  SER   B C   1 
ATOM   1472 O O   . SER   B 1 94 ? 21.596  1.946   -24.887 1.00 77.02  ? 93  SER   B O   1 
ATOM   1473 C CB  . SER   B 1 94 ? 24.303  1.286   -25.835 1.00 62.05  ? 93  SER   B CB  1 
ATOM   1474 O OG  . SER   B 1 94 ? 25.251  0.767   -26.758 1.00 63.08  ? 93  SER   B OG  1 
ATOM   1475 O OXT . SER   B 1 94 ? 22.118  0.395   -23.378 1.00 88.42  ? 93  SER   B OXT 1 
ATOM   1476 N N   . HIS   C 1 4  ? 32.918  -24.178 26.902  1.00 76.69  ? 3   HIS   C N   1 
ATOM   1477 C CA  . HIS   C 1 4  ? 31.968  -23.066 27.182  1.00 81.77  ? 3   HIS   C CA  1 
ATOM   1478 C C   . HIS   C 1 4  ? 31.361  -23.271 28.573  1.00 87.99  ? 3   HIS   C C   1 
ATOM   1479 O O   . HIS   C 1 4  ? 32.066  -23.648 29.510  1.00 85.87  ? 3   HIS   C O   1 
ATOM   1480 C CB  . HIS   C 1 4  ? 30.980  -22.891 26.018  1.00 77.71  ? 3   HIS   C CB  1 
ATOM   1481 N N   . ALA   C 1 5  ? 30.045  -23.043 28.686  1.00 84.56  ? 4   ALA   C N   1 
ATOM   1482 C CA  . ALA   C 1 5  ? 29.351  -22.951 29.962  1.00 78.61  ? 4   ALA   C CA  1 
ATOM   1483 C C   . ALA   C 1 5  ? 27.846  -22.964 29.718  1.00 80.70  ? 4   ALA   C C   1 
ATOM   1484 O O   . ALA   C 1 5  ? 27.279  -21.981 29.231  1.00 73.43  ? 4   ALA   C O   1 
ATOM   1485 C CB  . ALA   C 1 5  ? 29.732  -21.647 30.615  1.00 80.77  ? 4   ALA   C CB  1 
ATOM   1486 N N   . PHE   C 1 6  ? 27.195  -24.071 30.076  1.00 64.45  ? 5   PHE   C N   1 
ATOM   1487 C CA  . PHE   C 1 6  ? 25.791  -24.184 29.744  1.00 52.48  ? 5   PHE   C CA  1 
ATOM   1488 C C   . PHE   C 1 6  ? 24.987  -24.202 31.036  1.00 57.04  ? 5   PHE   C C   1 
ATOM   1489 O O   . PHE   C 1 6  ? 25.363  -24.900 31.971  1.00 65.84  ? 5   PHE   C O   1 
ATOM   1490 C CB  . PHE   C 1 6  ? 25.583  -25.393 28.814  1.00 52.32  ? 5   PHE   C CB  1 
ATOM   1491 C CG  . PHE   C 1 6  ? 26.365  -25.352 27.504  1.00 48.28  ? 5   PHE   C CG  1 
ATOM   1492 C CD1 . PHE   C 1 6  ? 27.512  -26.121 27.326  1.00 50.14  ? 5   PHE   C CD1 1 
ATOM   1493 C CD2 . PHE   C 1 6  ? 25.992  -24.502 26.463  1.00 51.21  ? 5   PHE   C CD2 1 
ATOM   1494 C CE1 . PHE   C 1 6  ? 28.253  -26.078 26.144  1.00 50.79  ? 5   PHE   C CE1 1 
ATOM   1495 C CE2 . PHE   C 1 6  ? 26.721  -24.472 25.276  1.00 47.38  ? 5   PHE   C CE2 1 
ATOM   1496 C CZ  . PHE   C 1 6  ? 27.841  -25.266 25.105  1.00 40.32  ? 5   PHE   C CZ  1 
ATOM   1497 N N   . LYS   C 1 7  ? 23.903  -23.418 31.075  1.00 51.98  ? 6   LYS   C N   1 
ATOM   1498 C CA  . LYS   C 1 7  ? 22.972  -23.381 32.195  1.00 58.49  ? 6   LYS   C CA  1 
ATOM   1499 C C   . LYS   C 1 7  ? 21.607  -23.741 31.625  1.00 46.28  ? 6   LYS   C C   1 
ATOM   1500 O O   . LYS   C 1 7  ? 21.447  -23.686 30.402  1.00 45.87  ? 6   LYS   C O   1 
ATOM   1501 C CB  . LYS   C 1 7  ? 22.953  -22.018 32.905  1.00 58.02  ? 6   LYS   C CB  1 
ATOM   1502 N N   . PRO   C 1 8  ? 20.609  -24.177 32.432  1.00 54.08  ? 7   PRO   C N   1 
ATOM   1503 C CA  . PRO   C 1 8  ? 19.284  -24.486 31.879  1.00 49.13  ? 7   PRO   C CA  1 
ATOM   1504 C C   . PRO   C 1 8  ? 18.685  -23.321 31.087  1.00 54.73  ? 7   PRO   C C   1 
ATOM   1505 O O   . PRO   C 1 8  ? 18.632  -22.190 31.570  1.00 59.98  ? 7   PRO   C O   1 
ATOM   1506 C CB  . PRO   C 1 8  ? 18.438  -24.906 33.097  1.00 52.62  ? 7   PRO   C CB  1 
ATOM   1507 C CG  . PRO   C 1 8  ? 19.458  -25.315 34.138  1.00 53.03  ? 7   PRO   C CG  1 
ATOM   1508 C CD  . PRO   C 1 8  ? 20.709  -24.470 33.881  1.00 47.38  ? 7   PRO   C CD  1 
ATOM   1509 N N   . GLY   C 1 9  ? 18.292  -23.594 29.838  1.00 45.42  ? 8   GLY   C N   1 
ATOM   1510 C CA  . GLY   C 1 9  ? 17.614  -22.619 28.991  1.00 43.36  ? 8   GLY   C CA  1 
ATOM   1511 C C   . GLY   C 1 9  ? 18.496  -22.101 27.853  1.00 48.73  ? 8   GLY   C C   1 
ATOM   1512 O O   . GLY   C 1 9  ? 17.981  -21.486 26.923  1.00 52.82  ? 8   GLY   C O   1 
ATOM   1513 N N   . ASP   C 1 10 ? 19.808  -22.367 27.913  1.00 41.79  ? 9   ASP   C N   1 
ATOM   1514 C CA  . ASP   C 1 10 ? 20.737  -22.026 26.855  1.00 37.84  ? 9   ASP   C CA  1 
ATOM   1515 C C   . ASP   C 1 10 ? 20.341  -22.737 25.559  1.00 38.23  ? 9   ASP   C C   1 
ATOM   1516 O O   . ASP   C 1 10 ? 20.056  -23.936 25.561  1.00 37.82  ? 9   ASP   C O   1 
ATOM   1517 C CB  . ASP   C 1 10 ? 22.179  -22.280 27.253  1.00 41.97  ? 9   ASP   C CB  1 
ATOM   1518 C CG  . ASP   C 1 10 ? 22.659  -21.456 28.447  1.00 52.55  ? 9   ASP   C CG  1 
ATOM   1519 O OD1 . ASP   C 1 10 ? 22.014  -20.434 28.729  1.00 53.07  ? 9   ASP   C OD1 1 
ATOM   1520 O OD2 . ASP   C 1 10 ? 23.636  -21.867 29.121  1.00 52.29  ? 9   ASP   C OD2 1 
ATOM   1521 N N   . LEU   C 1 11 ? 20.319  -21.970 24.472  1.00 39.83  ? 10  LEU   C N   1 
ATOM   1522 C CA  . LEU   C 1 11 ? 19.979  -22.512 23.168  1.00 36.53  ? 10  LEU   C CA  1 
ATOM   1523 C C   . LEU   C 1 11 ? 21.234  -23.012 22.471  1.00 35.53  ? 10  LEU   C C   1 
ATOM   1524 O O   . LEU   C 1 11 ? 22.270  -22.335 22.443  1.00 38.13  ? 10  LEU   C O   1 
ATOM   1525 C CB  . LEU   C 1 11 ? 19.264  -21.418 22.365  1.00 35.38  ? 10  LEU   C CB  1 
ATOM   1526 C CG  . LEU   C 1 11 ? 17.958  -20.919 22.984  1.00 33.97  ? 10  LEU   C CG  1 
ATOM   1527 C CD1 . LEU   C 1 11 ? 17.357  -19.943 21.962  1.00 34.27  ? 10  LEU   C CD1 1 
ATOM   1528 C CD2 . LEU   C 1 11 ? 16.976  -22.036 23.357  1.00 36.77  ? 10  LEU   C CD2 1 
ATOM   1529 N N   . VAL   C 1 12 ? 21.131  -24.201 21.821  1.00 32.46  ? 11  VAL   C N   1 
ATOM   1530 C CA  . VAL   C 1 12 ? 22.320  -24.881 21.337  1.00 32.46  ? 11  VAL   C CA  1 
ATOM   1531 C C   . VAL   C 1 12 ? 21.957  -25.615 20.029  1.00 29.37  ? 11  VAL   C C   1 
ATOM   1532 O O   . VAL   C 1 12 ? 20.768  -25.793 19.768  1.00 31.29  ? 11  VAL   C O   1 
ATOM   1533 C CB  . VAL   C 1 12 ? 22.931  -25.886 22.346  1.00 32.93  ? 11  VAL   C CB  1 
ATOM   1534 C CG1 . VAL   C 1 12 ? 23.406  -25.228 23.661  1.00 36.50  ? 11  VAL   C CG1 1 
ATOM   1535 C CG2 . VAL   C 1 12 ? 22.024  -27.087 22.598  1.00 36.81  ? 11  VAL   C CG2 1 
ATOM   1536 N N   . PHE   C 1 13 ? 22.990  -25.997 19.275  1.00 30.56  ? 12  PHE   C N   1 
ATOM   1537 C CA  . PHE   C 1 13 ? 22.943  -27.173 18.401  1.00 28.79  ? 12  PHE   C CA  1 
ATOM   1538 C C   . PHE   C 1 13 ? 23.642  -28.348 19.092  1.00 29.18  ? 12  PHE   C C   1 
ATOM   1539 O O   . PHE   C 1 13 ? 24.744  -28.235 19.666  1.00 31.33  ? 12  PHE   C O   1 
ATOM   1540 C CB  . PHE   C 1 13 ? 23.547  -26.963 17.006  1.00 33.85  ? 12  PHE   C CB  1 
ATOM   1541 C CG  . PHE   C 1 13 ? 22.817  -25.919 16.178  1.00 34.29  ? 12  PHE   C CG  1 
ATOM   1542 C CD1 . PHE   C 1 13 ? 21.754  -26.276 15.326  1.00 31.71  ? 12  PHE   C CD1 1 
ATOM   1543 C CD2 . PHE   C 1 13 ? 23.208  -24.583 16.238  1.00 34.54  ? 12  PHE   C CD2 1 
ATOM   1544 C CE1 . PHE   C 1 13 ? 21.093  -25.307 14.581  1.00 34.81  ? 12  PHE   C CE1 1 
ATOM   1545 C CE2 . PHE   C 1 13 ? 22.521  -23.620 15.515  1.00 37.41  ? 12  PHE   C CE2 1 
ATOM   1546 C CZ  . PHE   C 1 13 ? 21.476  -23.988 14.682  1.00 39.60  ? 12  PHE   C CZ  1 
ATOM   1547 N N   . ALA   C 1 14 ? 22.983  -29.521 19.042  1.00 28.76  ? 13  ALA   C N   1 
ATOM   1548 C CA  . ALA   C 1 14 ? 23.406  -30.685 19.807  1.00 25.32  ? 13  ALA   C CA  1 
ATOM   1549 C C   . ALA   C 1 14 ? 23.682  -31.799 18.808  1.00 28.23  ? 13  ALA   C C   1 
ATOM   1550 O O   . ALA   C 1 14 ? 22.815  -32.060 17.972  1.00 26.65  ? 13  ALA   C O   1 
ATOM   1551 C CB  . ALA   C 1 14 ? 22.303  -31.106 20.748  1.00 26.31  ? 13  ALA   C CB  1 
ATOM   1552 N N   . LYS   C 1 15 ? 24.888  -32.383 18.873  1.00 27.98  ? 14  LYS   C N   1 
ATOM   1553 C CA  . LYS   C 1 15 ? 25.272  -33.395 17.898  1.00 27.40  ? 14  LYS   C CA  1 
ATOM   1554 C C   . LYS   C 1 15 ? 25.288  -34.769 18.537  1.00 27.34  ? 14  LYS   C C   1 
ATOM   1555 O O   . LYS   C 1 15 ? 26.011  -35.026 19.514  1.00 32.60  ? 14  LYS   C O   1 
ATOM   1556 C CB  . LYS   C 1 15 ? 26.691  -33.080 17.410  1.00 28.57  ? 14  LYS   C CB  1 
ATOM   1557 C CG  . LYS   C 1 15 ? 27.132  -34.090 16.328  1.00 29.29  ? 14  LYS   C CG  1 
ATOM   1558 C CD  . LYS   C 1 15 ? 26.357  -33.868 15.022  1.00 30.48  ? 14  LYS   C CD  1 
ATOM   1559 C CE  . LYS   C 1 15 ? 26.741  -34.694 13.794  1.00 34.37  ? 14  LYS   C CE  1 
ATOM   1560 N NZ  . LYS   C 1 15 ? 26.757  -36.127 14.057  1.00 31.62  ? 14  LYS   C NZ  1 
ATOM   1561 N N   . MET   C 1 16 ? 24.525  -35.684 17.949  1.00 25.87  ? 15  MET   C N   1 
ATOM   1562 C CA  . MET   C 1 16 ? 24.593  -37.096 18.313  1.00 25.87  ? 15  MET   C CA  1 
ATOM   1563 C C   . MET   C 1 16 ? 25.028  -37.882 17.075  1.00 30.95  ? 15  MET   C C   1 
ATOM   1564 O O   . MET   C 1 16 ? 24.734  -37.495 15.931  1.00 27.36  ? 15  MET   C O   1 
ATOM   1565 C CB  . MET   C 1 16 ? 23.211  -37.606 18.727  1.00 27.78  ? 15  MET   C CB  1 
ATOM   1566 C CG  . MET   C 1 16 ? 22.678  -36.892 19.981  1.00 31.65  ? 15  MET   C CG  1 
ATOM   1567 S SD  . MET   C 1 16 ? 21.170  -37.576 20.698  1.00 37.18  ? 15  MET   C SD  1 
ATOM   1568 C CE  . MET   C 1 16 ? 21.804  -39.120 21.379  1.00 43.03  ? 15  MET   C CE  1 
ATOM   1569 N N   . LYS   C 1 17 ? 25.687  -39.024 17.314  1.00 27.83  ? 16  LYS   C N   1 
ATOM   1570 C CA  . LYS   C 1 17 ? 26.083  -39.877 16.192  1.00 33.69  ? 16  LYS   C CA  1 
ATOM   1571 C C   . LYS   C 1 17 ? 24.829  -40.295 15.417  1.00 27.12  ? 16  LYS   C C   1 
ATOM   1572 O O   . LYS   C 1 17 ? 23.855  -40.781 15.984  1.00 31.21  ? 16  LYS   C O   1 
ATOM   1573 C CB  . LYS   C 1 17 ? 26.746  -41.129 16.786  1.00 31.47  ? 16  LYS   C CB  1 
ATOM   1574 C CG  . LYS   C 1 17 ? 27.346  -42.116 15.754  1.00 34.09  ? 16  LYS   C CG  1 
ATOM   1575 C CD  . LYS   C 1 17 ? 28.511  -41.364 15.136  1.00 35.99  ? 16  LYS   C CD  1 
ATOM   1576 C CE  . LYS   C 1 17 ? 29.311  -42.216 14.179  1.00 48.15  ? 16  LYS   C CE  1 
ATOM   1577 N NZ  . LYS   C 1 17 ? 30.546  -41.570 13.736  1.00 43.21  ? 16  LYS   C NZ  1 
ATOM   1578 N N   . GLY   C 1 18 ? 24.903  -40.131 14.088  1.00 30.39  ? 17  GLY   C N   1 
ATOM   1579 C CA  . GLY   C 1 18 ? 23.829  -40.636 13.250  1.00 31.06  ? 17  GLY   C CA  1 
ATOM   1580 C C   . GLY   C 1 18 ? 22.861  -39.521 12.864  1.00 28.71  ? 17  GLY   C C   1 
ATOM   1581 O O   . GLY   C 1 18 ? 21.901  -39.813 12.174  1.00 28.75  ? 17  GLY   C O   1 
ATOM   1582 N N   . TYR   C 1 19 ? 23.069  -38.309 13.405  1.00 27.38  ? 18  TYR   C N   1 
ATOM   1583 C CA  . TYR   C 1 19 ? 22.135  -37.198 13.182  1.00 28.11  ? 18  TYR   C CA  1 
ATOM   1584 C C   . TYR   C 1 19 ? 22.895  -35.906 12.920  1.00 26.12  ? 18  TYR   C C   1 
ATOM   1585 O O   . TYR   C 1 19 ? 24.010  -35.715 13.401  1.00 27.30  ? 18  TYR   C O   1 
ATOM   1586 C CB  . TYR   C 1 19 ? 21.277  -36.911 14.429  1.00 26.21  ? 18  TYR   C CB  1 
ATOM   1587 C CG  . TYR   C 1 19 ? 20.493  -38.161 14.768  1.00 28.76  ? 18  TYR   C CG  1 
ATOM   1588 C CD1 . TYR   C 1 19 ? 21.030  -39.125 15.608  1.00 29.88  ? 18  TYR   C CD1 1 
ATOM   1589 C CD2 . TYR   C 1 19 ? 19.207  -38.337 14.260  1.00 31.03  ? 18  TYR   C CD2 1 
ATOM   1590 C CE1 . TYR   C 1 19 ? 20.300  -40.258 15.927  1.00 33.81  ? 18  TYR   C CE1 1 
ATOM   1591 C CE2 . TYR   C 1 19 ? 18.475  -39.467 14.580  1.00 38.24  ? 18  TYR   C CE2 1 
ATOM   1592 C CZ  . TYR   C 1 19 ? 19.025  -40.416 15.415  1.00 37.42  ? 18  TYR   C CZ  1 
ATOM   1593 O OH  . TYR   C 1 19 ? 18.300  -41.540 15.705  1.00 47.73  ? 18  TYR   C OH  1 
ATOM   1594 N N   . PRO   C 1 20 ? 22.320  -34.967 12.142  1.00 27.45  ? 19  PRO   C N   1 
ATOM   1595 C CA  . PRO   C 1 20 ? 22.942  -33.666 11.919  1.00 26.93  ? 19  PRO   C CA  1 
ATOM   1596 C C   . PRO   C 1 20 ? 22.939  -32.858 13.218  1.00 27.74  ? 19  PRO   C C   1 
ATOM   1597 O O   . PRO   C 1 20 ? 22.154  -33.135 14.133  1.00 26.54  ? 19  PRO   C O   1 
ATOM   1598 C CB  . PRO   C 1 20 ? 22.047  -33.003 10.850  1.00 29.94  ? 19  PRO   C CB  1 
ATOM   1599 C CG  . PRO   C 1 20 ? 20.725  -33.670 11.021  1.00 30.09  ? 19  PRO   C CG  1 
ATOM   1600 C CD  . PRO   C 1 20 ? 20.972  -35.074 11.538  1.00 26.45  ? 19  PRO   C CD  1 
ATOM   1601 N N   . HIS   C 1 21 ? 23.796  -31.836 13.267  1.00 27.36  ? 20  HIS   C N   1 
ATOM   1602 C CA  . HIS   C 1 21 ? 23.741  -30.931 14.420  1.00 26.95  ? 20  HIS   C CA  1 
ATOM   1603 C C   . HIS   C 1 21 ? 22.321  -30.384 14.556  1.00 28.39  ? 20  HIS   C C   1 
ATOM   1604 O O   . HIS   C 1 21 ? 21.803  -29.799 13.616  1.00 28.95  ? 20  HIS   C O   1 
ATOM   1605 C CB  . HIS   C 1 21 ? 24.704  -29.772 14.174  1.00 32.12  ? 20  HIS   C CB  1 
ATOM   1606 C CG  . HIS   C 1 21 ? 26.135  -30.202 14.210  1.00 30.57  ? 20  HIS   C CG  1 
ATOM   1607 N ND1 . HIS   C 1 21 ? 26.814  -30.840 13.186  1.00 34.82  ? 20  HIS   C ND1 1 
ATOM   1608 C CD2 . HIS   C 1 21 ? 27.021  -30.035 15.210  1.00 34.42  ? 20  HIS   C CD2 1 
ATOM   1609 C CE1 . HIS   C 1 21 ? 28.067  -31.054 13.566  1.00 40.04  ? 20  HIS   C CE1 1 
ATOM   1610 N NE2 . HIS   C 1 21 ? 28.218  -30.576 14.800  1.00 37.44  ? 20  HIS   C NE2 1 
ATOM   1611 N N   . TRP   C 1 22 ? 21.709  -30.479 15.764  1.00 26.21  ? 21  TRP   C N   1 
ATOM   1612 C CA  . TRP   C 1 22 ? 20.264  -30.360 15.866  1.00 25.69  ? 21  TRP   C CA  1 
ATOM   1613 C C   . TRP   C 1 22 ? 19.851  -29.193 16.767  1.00 27.76  ? 21  TRP   C C   1 
ATOM   1614 O O   . TRP   C 1 22 ? 20.411  -29.030 17.865  1.00 26.27  ? 21  TRP   C O   1 
ATOM   1615 C CB  . TRP   C 1 22 ? 19.692  -31.671 16.451  1.00 24.72  ? 21  TRP   C CB  1 
ATOM   1616 C CG  . TRP   C 1 22 ? 18.232  -31.861 16.121  1.00 26.84  ? 21  TRP   C CG  1 
ATOM   1617 C CD1 . TRP   C 1 22 ? 17.147  -31.258 16.687  1.00 28.38  ? 21  TRP   C CD1 1 
ATOM   1618 C CD2 . TRP   C 1 22 ? 17.726  -32.758 15.101  1.00 26.08  ? 21  TRP   C CD2 1 
ATOM   1619 N NE1 . TRP   C 1 22 ? 15.998  -31.688 16.062  1.00 27.43  ? 21  TRP   C NE1 1 
ATOM   1620 C CE2 . TRP   C 1 22 ? 16.317  -32.618 15.106  1.00 26.16  ? 21  TRP   C CE2 1 
ATOM   1621 C CE3 . TRP   C 1 22 ? 18.324  -33.670 14.217  1.00 25.44  ? 21  TRP   C CE3 1 
ATOM   1622 C CZ2 . TRP   C 1 22 ? 15.509  -33.352 14.230  1.00 27.01  ? 21  TRP   C CZ2 1 
ATOM   1623 C CZ3 . TRP   C 1 22 ? 17.531  -34.387 13.336  1.00 28.23  ? 21  TRP   C CZ3 1 
ATOM   1624 C CH2 . TRP   C 1 22 ? 16.134  -34.252 13.390  1.00 25.41  ? 21  TRP   C CH2 1 
ATOM   1625 N N   . PRO   C 1 23 ? 18.847  -28.359 16.410  1.00 29.92  ? 22  PRO   C N   1 
ATOM   1626 C CA  . PRO   C 1 23 ? 18.416  -27.295 17.328  1.00 26.18  ? 22  PRO   C CA  1 
ATOM   1627 C C   . PRO   C 1 23 ? 17.886  -27.850 18.643  1.00 24.52  ? 22  PRO   C C   1 
ATOM   1628 O O   . PRO   C 1 23 ? 17.053  -28.739 18.631  1.00 26.80  ? 22  PRO   C O   1 
ATOM   1629 C CB  . PRO   C 1 23 ? 17.323  -26.547 16.491  1.00 29.18  ? 22  PRO   C CB  1 
ATOM   1630 C CG  . PRO   C 1 23 ? 16.840  -27.585 15.521  1.00 26.43  ? 22  PRO   C CG  1 
ATOM   1631 C CD  . PRO   C 1 23 ? 18.111  -28.309 15.107  1.00 27.44  ? 22  PRO   C CD  1 
ATOM   1632 N N   . ALA   C 1 24 ? 18.415  -27.314 19.765  1.00 26.64  ? 23  ALA   C N   1 
ATOM   1633 C CA  . ALA   C 1 24 ? 18.078  -27.875 21.072  1.00 30.07  ? 23  ALA   C CA  1 
ATOM   1634 C C   . ALA   C 1 24 ? 18.243  -26.818 22.169  1.00 31.61  ? 23  ALA   C C   1 
ATOM   1635 O O   . ALA   C 1 24 ? 18.740  -25.719 21.908  1.00 31.55  ? 23  ALA   C O   1 
ATOM   1636 C CB  . ALA   C 1 24 ? 18.989  -29.097 21.347  1.00 30.16  ? 23  ALA   C CB  1 
ATOM   1637 N N   . ARG   C 1 25 ? 17.842  -27.175 23.397  1.00 33.46  ? 24  ARG   C N   1 
ATOM   1638 C CA  . ARG   C 1 25 ? 18.195  -26.353 24.544  1.00 32.74  ? 24  ARG   C CA  1 
ATOM   1639 C C   . ARG   C 1 25 ? 18.654  -27.238 25.707  1.00 32.54  ? 24  ARG   C C   1 
ATOM   1640 O O   . ARG   C 1 25 ? 18.373  -28.428 25.712  1.00 33.29  ? 24  ARG   C O   1 
ATOM   1641 C CB  . ARG   C 1 25 ? 16.992  -25.534 25.001  1.00 33.91  ? 24  ARG   C CB  1 
ATOM   1642 C CG  . ARG   C 1 25 ? 15.742  -26.258 25.479  1.00 41.97  ? 24  ARG   C CG  1 
ATOM   1643 C CD  . ARG   C 1 25 ? 14.708  -25.323 26.133  1.00 40.52  ? 24  ARG   C CD  1 
ATOM   1644 N NE  . ARG   C 1 25 ? 13.531  -26.109 26.529  1.00 49.06  ? 24  ARG   C NE  1 
ATOM   1645 C CZ  . ARG   C 1 25 ? 12.275  -25.957 26.134  1.00 46.59  ? 24  ARG   C CZ  1 
ATOM   1646 N NH1 . ARG   C 1 25 ? 11.927  -24.916 25.399  1.00 47.71  ? 24  ARG   C NH1 1 
ATOM   1647 N NH2 . ARG   C 1 25 ? 11.357  -26.846 26.493  1.00 55.34  ? 24  ARG   C NH2 1 
ATOM   1648 N N   . ILE   C 1 26 ? 19.318  -26.604 26.673  1.00 35.95  ? 25  ILE   C N   1 
ATOM   1649 C CA  . ILE   C 1 26 ? 19.683  -27.237 27.931  1.00 34.33  ? 25  ILE   C CA  1 
ATOM   1650 C C   . ILE   C 1 26 ? 18.463  -27.192 28.840  1.00 39.19  ? 25  ILE   C C   1 
ATOM   1651 O O   . ILE   C 1 26 ? 17.849  -26.142 28.997  1.00 42.96  ? 25  ILE   C O   1 
ATOM   1652 C CB  . ILE   C 1 26 ? 20.851  -26.478 28.592  1.00 35.02  ? 25  ILE   C CB  1 
ATOM   1653 C CG1 . ILE   C 1 26 ? 22.046  -26.223 27.685  1.00 38.22  ? 25  ILE   C CG1 1 
ATOM   1654 C CG2 . ILE   C 1 26 ? 21.280  -27.201 29.878  1.00 38.28  ? 25  ILE   C CG2 1 
ATOM   1655 C CD1 . ILE   C 1 26 ? 22.712  -27.453 27.107  1.00 43.02  ? 25  ILE   C CD1 1 
ATOM   1656 N N   . ASP   C 1 27 ? 18.089  -28.334 29.409  1.00 40.03  ? 26  ASP   C N   1 
ATOM   1657 C CA  . ASP   C 1 27 ? 17.043  -28.373 30.416  1.00 48.90  ? 26  ASP   C CA  1 
ATOM   1658 C C   . ASP   C 1 27 ? 17.663  -28.432 31.812  1.00 57.46  ? 26  ASP   C C   1 
ATOM   1659 O O   . ASP   C 1 27 ? 18.858  -28.708 31.950  1.00 57.31  ? 26  ASP   C O   1 
ATOM   1660 C CB  . ASP   C 1 27 ? 16.171  -29.599 30.222  1.00 51.41  ? 26  ASP   C CB  1 
ATOM   1661 C CG  . ASP   C 1 27 ? 15.011  -29.448 29.248  1.00 58.19  ? 26  ASP   C CG  1 
ATOM   1662 O OD1 . ASP   C 1 27 ? 14.858  -28.338 28.668  1.00 54.34  ? 26  ASP   C OD1 1 
ATOM   1663 O OD2 . ASP   C 1 27 ? 14.260  -30.442 29.115  1.00 63.72  ? 26  ASP   C OD2 1 
ATOM   1664 N N   . ASP   C 1 28 ? 16.839  -28.183 32.844  1.00 67.48  ? 27  ASP   C N   1 
ATOM   1665 C CA  . ASP   C 1 28 ? 17.209  -28.486 34.221  1.00 65.63  ? 27  ASP   C CA  1 
ATOM   1666 C C   . ASP   C 1 28 ? 16.789  -29.924 34.510  1.00 65.34  ? 27  ASP   C C   1 
ATOM   1667 O O   . ASP   C 1 28 ? 16.044  -30.508 33.726  1.00 61.08  ? 27  ASP   C O   1 
ATOM   1668 C CB  . ASP   C 1 28 ? 16.655  -27.470 35.213  1.00 68.73  ? 27  ASP   C CB  1 
ATOM   1669 N N   . ILE   C 1 29 ? 17.312  -30.494 35.607  1.00 63.89  ? 28  ILE   C N   1 
ATOM   1670 C CA  . ILE   C 1 29 ? 16.989  -31.849 36.034  1.00 57.88  ? 28  ILE   C CA  1 
ATOM   1671 C C   . ILE   C 1 29 ? 16.031  -31.730 37.224  1.00 58.30  ? 28  ILE   C C   1 
ATOM   1672 O O   . ILE   C 1 29 ? 16.464  -31.044 38.173  1.00 54.89  ? 28  ILE   C O   1 
ATOM   1673 C CB  . ILE   C 1 29 ? 18.260  -32.612 36.453  1.00 55.34  ? 28  ILE   C CB  1 
ATOM   1674 N N   . LYS   C 1 35 ? 20.047  -38.775 37.910  1.00 54.21  ? 34  LYS   C N   1 
ATOM   1675 C CA  . LYS   C 1 35 ? 20.985  -37.687 37.517  1.00 54.30  ? 34  LYS   C CA  1 
ATOM   1676 C C   . LYS   C 1 35 ? 21.628  -38.029 36.177  1.00 49.23  ? 34  LYS   C C   1 
ATOM   1677 O O   . LYS   C 1 35 ? 21.657  -39.189 35.767  1.00 48.52  ? 34  LYS   C O   1 
ATOM   1678 C CB  . LYS   C 1 35 ? 22.094  -37.501 38.556  1.00 52.88  ? 34  LYS   C CB  1 
ATOM   1679 N N   . PRO   C 1 36 ? 22.169  -37.033 35.439  1.00 48.01  ? 35  PRO   C N   1 
ATOM   1680 C CA  . PRO   C 1 36 ? 22.880  -37.343 34.206  1.00 49.82  ? 35  PRO   C CA  1 
ATOM   1681 C C   . PRO   C 1 36 ? 24.008  -38.322 34.522  1.00 54.42  ? 35  PRO   C C   1 
ATOM   1682 O O   . PRO   C 1 36 ? 24.402  -38.519 35.685  1.00 50.65  ? 35  PRO   C O   1 
ATOM   1683 C CB  . PRO   C 1 36 ? 23.396  -35.965 33.726  1.00 56.85  ? 35  PRO   C CB  1 
ATOM   1684 C CG  . PRO   C 1 36 ? 22.489  -34.953 34.417  1.00 52.60  ? 35  PRO   C CG  1 
ATOM   1685 C CD  . PRO   C 1 36 ? 22.121  -35.591 35.745  1.00 47.96  ? 35  PRO   C CD  1 
ATOM   1686 N N   . PRO   C 1 37 ? 24.547  -38.999 33.491  1.00 50.02  ? 36  PRO   C N   1 
ATOM   1687 C CA  . PRO   C 1 37 ? 25.861  -39.607 33.616  1.00 44.87  ? 36  PRO   C CA  1 
ATOM   1688 C C   . PRO   C 1 37 ? 26.800  -38.454 33.958  1.00 44.06  ? 36  PRO   C C   1 
ATOM   1689 O O   . PRO   C 1 37 ? 26.495  -37.266 33.751  1.00 36.65  ? 36  PRO   C O   1 
ATOM   1690 C CB  . PRO   C 1 37 ? 26.072  -40.202 32.210  1.00 44.89  ? 36  PRO   C CB  1 
ATOM   1691 C CG  . PRO   C 1 37 ? 24.663  -40.478 31.753  1.00 46.76  ? 36  PRO   C CG  1 
ATOM   1692 C CD  . PRO   C 1 37 ? 23.934  -39.229 32.171  1.00 43.75  ? 36  PRO   C CD  1 
ATOM   1693 N N   . PRO   C 1 38 ? 27.961  -38.777 34.567  1.00 40.51  ? 37  PRO   C N   1 
ATOM   1694 C CA  . PRO   C 1 38 ? 28.981  -37.772 34.837  1.00 37.19  ? 37  PRO   C CA  1 
ATOM   1695 C C   . PRO   C 1 38 ? 29.270  -36.879 33.641  1.00 33.96  ? 37  PRO   C C   1 
ATOM   1696 O O   . PRO   C 1 38 ? 29.542  -37.370 32.540  1.00 36.46  ? 37  PRO   C O   1 
ATOM   1697 C CB  . PRO   C 1 38 ? 30.196  -38.667 35.195  1.00 43.61  ? 37  PRO   C CB  1 
ATOM   1698 C CG  . PRO   C 1 38 ? 29.530  -39.844 35.876  1.00 39.39  ? 37  PRO   C CG  1 
ATOM   1699 C CD  . PRO   C 1 38 ? 28.357  -40.138 34.970  1.00 43.58  ? 37  PRO   C CD  1 
ATOM   1700 N N   . ASN   C 1 39 ? 29.178  -35.570 33.912  1.00 35.76  ? 38  ASN   C N   1 
ATOM   1701 C CA  . ASN   C 1 39 ? 29.569  -34.481 33.040  1.00 34.51  ? 38  ASN   C CA  1 
ATOM   1702 C C   . ASN   C 1 39 ? 28.658  -34.442 31.826  1.00 39.08  ? 38  ASN   C C   1 
ATOM   1703 O O   . ASN   C 1 39 ? 29.096  -34.006 30.765  1.00 46.04  ? 38  ASN   C O   1 
ATOM   1704 C CB  . ASN   C 1 39 ? 31.023  -34.556 32.591  1.00 40.06  ? 38  ASN   C CB  1 
ATOM   1705 C CG  . ASN   C 1 39 ? 31.553  -33.281 31.966  1.00 48.41  ? 38  ASN   C CG  1 
ATOM   1706 O OD1 . ASN   C 1 39 ? 30.971  -32.198 32.131  1.00 59.92  ? 38  ASN   C OD1 1 
ATOM   1707 N ND2 . ASN   C 1 39 ? 32.640  -33.384 31.207  1.00 50.76  ? 38  ASN   C ND2 1 
ATOM   1708 N N   . LYS   C 1 40 ? 27.411  -34.886 32.001  1.00 33.03  ? 39  LYS   C N   1 
ATOM   1709 C CA  . LYS   C 1 40 ? 26.476  -34.737 30.891  1.00 31.10  ? 39  LYS   C CA  1 
ATOM   1710 C C   . LYS   C 1 40 ? 25.357  -33.760 31.241  1.00 34.99  ? 39  LYS   C C   1 
ATOM   1711 O O   . LYS   C 1 40 ? 24.968  -33.584 32.384  1.00 36.49  ? 39  LYS   C O   1 
ATOM   1712 C CB  . LYS   C 1 40 ? 25.796  -36.047 30.493  1.00 33.27  ? 39  LYS   C CB  1 
ATOM   1713 C CG  . LYS   C 1 40 ? 26.704  -37.180 30.134  1.00 34.46  ? 39  LYS   C CG  1 
ATOM   1714 C CD  . LYS   C 1 40 ? 27.698  -36.964 29.023  1.00 37.65  ? 39  LYS   C CD  1 
ATOM   1715 C CE  . LYS   C 1 40 ? 28.381  -38.277 28.700  1.00 40.81  ? 39  LYS   C CE  1 
ATOM   1716 N NZ  . LYS   C 1 40 ? 29.288  -38.111 27.562  1.00 49.35  ? 39  LYS   C NZ  1 
ATOM   1717 N N   . TYR   C 1 41 ? 24.828  -33.118 30.196  1.00 32.69  ? 40  TYR   C N   1 
ATOM   1718 C CA  . TYR   C 1 41 ? 23.731  -32.161 30.306  1.00 34.80  ? 40  TYR   C CA  1 
ATOM   1719 C C   . TYR   C 1 41 ? 22.432  -32.794 29.821  1.00 31.88  ? 40  TYR   C C   1 
ATOM   1720 O O   . TYR   C 1 41 ? 22.467  -33.555 28.856  1.00 30.47  ? 40  TYR   C O   1 
ATOM   1721 C CB  . TYR   C 1 41 ? 23.977  -30.999 29.342  1.00 30.35  ? 40  TYR   C CB  1 
ATOM   1722 C CG  . TYR   C 1 41 ? 25.105  -30.080 29.761  1.00 29.50  ? 40  TYR   C CG  1 
ATOM   1723 C CD1 . TYR   C 1 41 ? 26.403  -30.293 29.321  1.00 30.52  ? 40  TYR   C CD1 1 
ATOM   1724 C CD2 . TYR   C 1 41 ? 24.867  -29.032 30.657  1.00 35.71  ? 40  TYR   C CD2 1 
ATOM   1725 C CE1 . TYR   C 1 41 ? 27.445  -29.481 29.728  1.00 42.78  ? 40  TYR   C CE1 1 
ATOM   1726 C CE2 . TYR   C 1 41 ? 25.902  -28.193 31.037  1.00 35.30  ? 40  TYR   C CE2 1 
ATOM   1727 C CZ  . TYR   C 1 41 ? 27.188  -28.431 30.595  1.00 37.92  ? 40  TYR   C CZ  1 
ATOM   1728 O OH  . TYR   C 1 41 ? 28.242  -27.654 30.978  1.00 51.82  ? 40  TYR   C OH  1 
ATOM   1729 N N   . PRO   C 1 42 ? 21.259  -32.451 30.408  1.00 34.77  ? 41  PRO   C N   1 
ATOM   1730 C CA  . PRO   C 1 42 ? 19.955  -32.869 29.871  1.00 32.18  ? 41  PRO   C CA  1 
ATOM   1731 C C   . PRO   C 1 42 ? 19.661  -31.937 28.701  1.00 33.30  ? 41  PRO   C C   1 
ATOM   1732 O O   . PRO   C 1 42 ? 19.712  -30.713 28.856  1.00 34.73  ? 41  PRO   C O   1 
ATOM   1733 C CB  . PRO   C 1 42 ? 18.928  -32.698 31.010  1.00 34.10  ? 41  PRO   C CB  1 
ATOM   1734 C CG  . PRO   C 1 42 ? 19.718  -31.941 32.064  1.00 36.77  ? 41  PRO   C CG  1 
ATOM   1735 C CD  . PRO   C 1 42 ? 21.122  -31.563 31.587  1.00 38.38  ? 41  PRO   C CD  1 
ATOM   1736 N N   . ILE   C 1 43 ? 19.379  -32.564 27.555  1.00 31.38  ? 42  ILE   C N   1 
ATOM   1737 C CA  . ILE   C 1 43 ? 19.103  -31.809 26.332  1.00 29.47  ? 42  ILE   C CA  1 
ATOM   1738 C C   . ILE   C 1 43 ? 17.664  -32.030 25.930  1.00 28.69  ? 42  ILE   C C   1 
ATOM   1739 O O   . ILE   C 1 43 ? 17.152  -33.135 25.996  1.00 31.66  ? 42  ILE   C O   1 
ATOM   1740 C CB  . ILE   C 1 43 ? 20.050  -32.260 25.211  1.00 28.89  ? 42  ILE   C CB  1 
ATOM   1741 C CG1 . ILE   C 1 43 ? 21.519  -32.117 25.635  1.00 29.79  ? 42  ILE   C CG1 1 
ATOM   1742 C CG2 . ILE   C 1 43 ? 19.733  -31.490 23.906  1.00 29.73  ? 42  ILE   C CG2 1 
ATOM   1743 C CD1 . ILE   C 1 43 ? 21.974  -30.699 25.941  1.00 32.32  ? 42  ILE   C CD1 1 
ATOM   1744 N N   . PHE   C 1 44 ? 17.017  -30.951 25.445  1.00 30.96  ? 43  PHE   C N   1 
ATOM   1745 C CA  . PHE   C 1 44 ? 15.715  -31.109 24.813  1.00 31.15  ? 43  PHE   C CA  1 
ATOM   1746 C C   . PHE   C 1 44 ? 15.882  -30.703 23.357  1.00 27.84  ? 43  PHE   C C   1 
ATOM   1747 O O   . PHE   C 1 44 ? 16.499  -29.662 23.106  1.00 29.83  ? 43  PHE   C O   1 
ATOM   1748 C CB  . PHE   C 1 44 ? 14.744  -30.091 25.436  1.00 35.32  ? 43  PHE   C CB  1 
ATOM   1749 C CG  . PHE   C 1 44 ? 13.349  -30.074 24.813  1.00 34.60  ? 43  PHE   C CG  1 
ATOM   1750 C CD1 . PHE   C 1 44 ? 12.415  -31.059 25.130  1.00 38.67  ? 43  PHE   C CD1 1 
ATOM   1751 C CD2 . PHE   C 1 44 ? 12.996  -29.072 23.903  1.00 36.89  ? 43  PHE   C CD2 1 
ATOM   1752 C CE1 . PHE   C 1 44 ? 11.143  -31.062 24.541  1.00 42.01  ? 43  PHE   C CE1 1 
ATOM   1753 C CE2 . PHE   C 1 44 ? 11.721  -29.066 23.326  1.00 36.61  ? 43  PHE   C CE2 1 
ATOM   1754 C CZ  . PHE   C 1 44 ? 10.800  -30.044 23.660  1.00 41.06  ? 43  PHE   C CZ  1 
ATOM   1755 N N   . PHE   C 1 45 ? 15.417  -31.581 22.466  1.00 26.97  ? 44  PHE   C N   1 
ATOM   1756 C CA  . PHE   C 1 45 ? 15.567  -31.359 21.034  1.00 29.15  ? 44  PHE   C CA  1 
ATOM   1757 C C   . PHE   C 1 45 ? 14.300  -30.720 20.482  1.00 27.72  ? 44  PHE   C C   1 
ATOM   1758 O O   . PHE   C 1 45 ? 13.203  -31.268 20.601  1.00 31.33  ? 44  PHE   C O   1 
ATOM   1759 C CB  . PHE   C 1 45 ? 15.840  -32.688 20.336  1.00 26.16  ? 44  PHE   C CB  1 
ATOM   1760 C CG  . PHE   C 1 45 ? 17.208  -33.277 20.645  1.00 27.19  ? 44  PHE   C CG  1 
ATOM   1761 C CD1 . PHE   C 1 45 ? 18.330  -32.957 19.869  1.00 27.65  ? 44  PHE   C CD1 1 
ATOM   1762 C CD2 . PHE   C 1 45 ? 17.345  -34.149 21.729  1.00 28.12  ? 44  PHE   C CD2 1 
ATOM   1763 C CE1 . PHE   C 1 45 ? 19.576  -33.517 20.141  1.00 29.15  ? 44  PHE   C CE1 1 
ATOM   1764 C CE2 . PHE   C 1 45 ? 18.593  -34.704 21.998  1.00 31.93  ? 44  PHE   C CE2 1 
ATOM   1765 C CZ  . PHE   C 1 45 ? 19.691  -34.379 21.215  1.00 27.31  ? 44  PHE   C CZ  1 
ATOM   1766 N N   . PHE   C 1 46 ? 14.473  -29.548 19.841  1.00 29.03  ? 45  PHE   C N   1 
ATOM   1767 C CA  . PHE   C 1 46 ? 13.304  -28.964 19.183  1.00 29.02  ? 45  PHE   C CA  1 
ATOM   1768 C C   . PHE   C 1 46 ? 12.848  -29.790 17.983  1.00 30.61  ? 45  PHE   C C   1 
ATOM   1769 O O   . PHE   C 1 46 ? 13.617  -30.543 17.366  1.00 29.32  ? 45  PHE   C O   1 
ATOM   1770 C CB  . PHE   C 1 46 ? 13.602  -27.540 18.709  1.00 27.72  ? 45  PHE   C CB  1 
ATOM   1771 C CG  . PHE   C 1 46 ? 13.871  -26.543 19.818  1.00 29.08  ? 45  PHE   C CG  1 
ATOM   1772 C CD1 . PHE   C 1 46 ? 12.827  -26.078 20.612  1.00 31.21  ? 45  PHE   C CD1 1 
ATOM   1773 C CD2 . PHE   C 1 46 ? 15.168  -26.064 20.031  1.00 28.31  ? 45  PHE   C CD2 1 
ATOM   1774 C CE1 . PHE   C 1 46 ? 13.102  -25.166 21.630  1.00 33.10  ? 45  PHE   C CE1 1 
ATOM   1775 C CE2 . PHE   C 1 46 ? 15.428  -25.167 21.054  1.00 34.18  ? 45  PHE   C CE2 1 
ATOM   1776 C CZ  . PHE   C 1 46 ? 14.390  -24.725 21.843  1.00 32.61  ? 45  PHE   C CZ  1 
ATOM   1777 N N   . GLY   C 1 47 ? 11.556  -29.667 17.647  1.00 28.54  ? 46  GLY   C N   1 
ATOM   1778 C CA  . GLY   C 1 47 ? 11.032  -30.354 16.492  1.00 32.14  ? 46  GLY   C CA  1 
ATOM   1779 C C   . GLY   C 1 47 ? 10.536  -31.742 16.886  1.00 35.06  ? 46  GLY   C C   1 
ATOM   1780 O O   . GLY   C 1 47 ? 9.350   -32.020 16.788  1.00 40.08  ? 46  GLY   C O   1 
ATOM   1781 N N   . THR   C 1 48 ? 11.461  -32.610 17.333  1.00 30.61  ? 47  THR   C N   1 
ATOM   1782 C CA  . THR   C 1 48 ? 11.094  -33.946 17.786  1.00 33.93  ? 47  THR   C CA  1 
ATOM   1783 C C   . THR   C 1 48 ? 10.602  -33.898 19.229  1.00 35.06  ? 47  THR   C C   1 
ATOM   1784 O O   . THR   C 1 48 ? 9.847   -34.782 19.633  1.00 39.12  ? 47  THR   C O   1 
ATOM   1785 C CB  . THR   C 1 48 ? 12.286  -34.900 17.660  1.00 32.82  ? 47  THR   C CB  1 
ATOM   1786 O OG1 . THR   C 1 48 ? 13.224  -34.427 18.633  1.00 32.65  ? 47  THR   C OG1 1 
ATOM   1787 C CG2 . THR   C 1 48 ? 12.795  -35.038 16.235  1.00 31.73  ? 47  THR   C CG2 1 
ATOM   1788 N N   . HIS   C 1 49 ? 11.054  -32.918 20.013  1.00 33.45  ? 48  HIS   C N   1 
ATOM   1789 C CA  . HIS   C 1 49 ? 10.694  -32.806 21.424  1.00 37.20  ? 48  HIS   C CA  1 
ATOM   1790 C C   . HIS   C 1 49 ? 11.154  -34.015 22.241  1.00 38.40  ? 48  HIS   C C   1 
ATOM   1791 O O   . HIS   C 1 49 ? 10.564  -34.282 23.299  1.00 38.21  ? 48  HIS   C O   1 
ATOM   1792 C CB  . HIS   C 1 49 ? 9.178   -32.647 21.591  1.00 34.61  ? 48  HIS   C CB  1 
ATOM   1793 C CG  . HIS   C 1 49 ? 8.618   -31.556 20.725  1.00 41.12  ? 48  HIS   C CG  1 
ATOM   1794 N ND1 . HIS   C 1 49 ? 7.435   -31.691 20.027  1.00 47.91  ? 48  HIS   C ND1 1 
ATOM   1795 C CD2 . HIS   C 1 49 ? 9.079   -30.332 20.449  1.00 40.50  ? 48  HIS   C CD2 1 
ATOM   1796 C CE1 . HIS   C 1 49 ? 7.202   -30.578 19.340  1.00 45.42  ? 48  HIS   C CE1 1 
ATOM   1797 N NE2 . HIS   C 1 49 ? 8.192   -29.741 19.576  1.00 42.75  ? 48  HIS   C NE2 1 
ATOM   1798 N N   . GLU   C 1 50 ? 12.226  -34.675 21.788  1.00 33.30  ? 49  GLU   C N   1 
ATOM   1799 C CA  . GLU   C 1 50 ? 12.850  -35.756 22.535  1.00 35.31  ? 49  GLU   C CA  1 
ATOM   1800 C C   . GLU   C 1 50 ? 13.904  -35.216 23.511  1.00 33.13  ? 49  GLU   C C   1 
ATOM   1801 O O   . GLU   C 1 50 ? 14.263  -34.047 23.519  1.00 31.73  ? 49  GLU   C O   1 
ATOM   1802 C CB  . GLU   C 1 50 ? 13.509  -36.761 21.598  1.00 35.83  ? 49  GLU   C CB  1 
ATOM   1803 C CG  . GLU   C 1 50 ? 12.599  -37.407 20.562  1.00 36.64  ? 49  GLU   C CG  1 
ATOM   1804 C CD  . GLU   C 1 50 ? 13.460  -37.909 19.420  1.00 45.74  ? 49  GLU   C CD  1 
ATOM   1805 O OE1 . GLU   C 1 50 ? 14.332  -37.145 18.935  1.00 51.65  ? 49  GLU   C OE1 1 
ATOM   1806 O OE2 . GLU   C 1 50 ? 13.248  -39.054 18.997  1.00 53.61  ? 49  GLU   C OE2 1 
ATOM   1807 N N   . THR   C 1 51 ? 14.392  -36.101 24.403  1.00 36.71  ? 50  THR   C N   1 
ATOM   1808 C CA  . THR   C 1 51 ? 15.429  -35.740 25.370  1.00 35.91  ? 50  THR   C CA  1 
ATOM   1809 C C   . THR   C 1 51 ? 16.550  -36.780 25.319  1.00 30.85  ? 50  THR   C C   1 
ATOM   1810 O O   . THR   C 1 51 ? 16.341  -37.934 24.929  1.00 34.92  ? 50  THR   C O   1 
ATOM   1811 C CB  . THR   C 1 51 ? 14.840  -35.669 26.788  1.00 35.28  ? 50  THR   C CB  1 
ATOM   1812 O OG1 . THR   C 1 51 ? 14.310  -36.974 27.043  1.00 38.69  ? 50  THR   C OG1 1 
ATOM   1813 C CG2 . THR   C 1 51 ? 13.902  -34.492 27.012  1.00 37.35  ? 50  THR   C CG2 1 
ATOM   1814 N N   . ALA   C 1 52 ? 17.754  -36.325 25.675  1.00 33.02  ? 51  ALA   C N   1 
ATOM   1815 C CA  . ALA   C 1 52 ? 18.936  -37.156 25.847  1.00 31.82  ? 51  ALA   C CA  1 
ATOM   1816 C C   . ALA   C 1 52 ? 19.922  -36.451 26.773  1.00 34.58  ? 51  ALA   C C   1 
ATOM   1817 O O   . ALA   C 1 52 ? 19.764  -35.277 27.104  1.00 34.31  ? 51  ALA   C O   1 
ATOM   1818 C CB  . ALA   C 1 52 ? 19.575  -37.415 24.505  1.00 34.41  ? 51  ALA   C CB  1 
ATOM   1819 N N   . PHE   C 1 53 ? 20.960  -37.185 27.206  1.00 34.23  ? 52  PHE   C N   1 
ATOM   1820 C CA  . PHE   C 1 53 ? 22.066  -36.596 27.948  1.00 33.48  ? 52  PHE   C CA  1 
ATOM   1821 C C   . PHE   C 1 53 ? 23.260  -36.492 27.013  1.00 33.25  ? 52  PHE   C C   1 
ATOM   1822 O O   . PHE   C 1 53 ? 23.627  -37.472 26.360  1.00 35.02  ? 52  PHE   C O   1 
ATOM   1823 C CB  . PHE   C 1 53 ? 22.417  -37.541 29.106  1.00 33.48  ? 52  PHE   C CB  1 
ATOM   1824 C CG  . PHE   C 1 53 ? 21.429  -37.461 30.248  1.00 37.07  ? 52  PHE   C CG  1 
ATOM   1825 C CD1 . PHE   C 1 53 ? 21.112  -36.244 30.835  1.00 40.11  ? 52  PHE   C CD1 1 
ATOM   1826 C CD2 . PHE   C 1 53 ? 20.792  -38.613 30.716  1.00 49.25  ? 52  PHE   C CD2 1 
ATOM   1827 C CE1 . PHE   C 1 53 ? 20.213  -36.179 31.898  1.00 42.62  ? 52  PHE   C CE1 1 
ATOM   1828 C CE2 . PHE   C 1 53 ? 19.883  -38.540 31.771  1.00 41.26  ? 52  PHE   C CE2 1 
ATOM   1829 C CZ  . PHE   C 1 53 ? 19.593  -37.319 32.356  1.00 39.07  ? 52  PHE   C CZ  1 
ATOM   1830 N N   . LEU   C 1 54 ? 23.887  -35.315 26.966  1.00 30.30  ? 53  LEU   C N   1 
ATOM   1831 C CA  . LEU   C 1 54 ? 25.041  -35.139 26.089  1.00 29.46  ? 53  LEU   C CA  1 
ATOM   1832 C C   . LEU   C 1 54 ? 26.142  -34.383 26.818  1.00 31.07  ? 53  LEU   C C   1 
ATOM   1833 O O   . LEU   C 1 54 ? 25.860  -33.549 27.683  1.00 32.62  ? 53  LEU   C O   1 
ATOM   1834 C CB  . LEU   C 1 54 ? 24.683  -34.404 24.792  1.00 31.31  ? 53  LEU   C CB  1 
ATOM   1835 C CG  . LEU   C 1 54 ? 23.784  -35.154 23.811  1.00 33.59  ? 53  LEU   C CG  1 
ATOM   1836 C CD1 . LEU   C 1 54 ? 23.528  -34.172 22.667  1.00 34.25  ? 53  LEU   C CD1 1 
ATOM   1837 C CD2 . LEU   C 1 54 ? 24.490  -36.423 23.280  1.00 39.29  ? 53  LEU   C CD2 1 
ATOM   1838 N N   . GLY   C 1 55 ? 27.383  -34.651 26.419  1.00 32.48  ? 54  GLY   C N   1 
ATOM   1839 C CA  . GLY   C 1 55 ? 28.529  -33.952 26.982  1.00 31.76  ? 54  GLY   C CA  1 
ATOM   1840 C C   . GLY   C 1 55 ? 28.859  -32.674 26.217  1.00 42.14  ? 54  GLY   C C   1 
ATOM   1841 O O   . GLY   C 1 55 ? 28.359  -32.430 25.112  1.00 36.90  ? 54  GLY   C O   1 
ATOM   1842 N N   . PRO   C 1 56 ? 29.700  -31.790 26.797  1.00 38.55  ? 55  PRO   C N   1 
ATOM   1843 C CA  . PRO   C 1 56 ? 29.944  -30.474 26.222  1.00 39.78  ? 55  PRO   C CA  1 
ATOM   1844 C C   . PRO   C 1 56 ? 30.586  -30.532 24.844  1.00 38.88  ? 55  PRO   C C   1 
ATOM   1845 O O   . PRO   C 1 56 ? 30.391  -29.608 24.061  1.00 50.89  ? 55  PRO   C O   1 
ATOM   1846 C CB  . PRO   C 1 56 ? 30.827  -29.753 27.276  1.00 42.80  ? 55  PRO   C CB  1 
ATOM   1847 C CG  . PRO   C 1 56 ? 31.480  -30.891 28.015  1.00 41.21  ? 55  PRO   C CG  1 
ATOM   1848 C CD  . PRO   C 1 56 ? 30.430  -31.989 28.063  1.00 42.43  ? 55  PRO   C CD  1 
ATOM   1849 N N   . LYS   C 1 57 ? 31.290  -31.631 24.541  1.00 43.10  ? 56  LYS   C N   1 
ATOM   1850 C CA  . LYS   C 1 57 ? 31.939  -31.747 23.241  1.00 45.18  ? 56  LYS   C CA  1 
ATOM   1851 C C   . LYS   C 1 57 ? 30.862  -31.771 22.155  1.00 42.73  ? 56  LYS   C C   1 
ATOM   1852 O O   . LYS   C 1 57 ? 31.125  -31.410 21.002  1.00 44.94  ? 56  LYS   C O   1 
ATOM   1853 C CB  . LYS   C 1 57 ? 32.796  -33.012 23.109  1.00 43.19  ? 56  LYS   C CB  1 
ATOM   1854 N N   . ASP   C 1 58 ? 29.643  -32.157 22.550  1.00 38.58  ? 57  ASP   C N   1 
ATOM   1855 C CA  . ASP   C 1 58 ? 28.564  -32.336 21.576  1.00 38.60  ? 57  ASP   C CA  1 
ATOM   1856 C C   . ASP   C 1 58 ? 27.704  -31.086 21.402  1.00 36.18  ? 57  ASP   C C   1 
ATOM   1857 O O   . ASP   C 1 58 ? 26.693  -31.135 20.702  1.00 34.11  ? 57  ASP   C O   1 
ATOM   1858 C CB  . ASP   C 1 58 ? 27.666  -33.493 21.977  1.00 37.71  ? 57  ASP   C CB  1 
ATOM   1859 C CG  . ASP   C 1 58 ? 28.378  -34.824 22.091  1.00 42.30  ? 57  ASP   C CG  1 
ATOM   1860 O OD1 . ASP   C 1 58 ? 29.391  -34.959 21.407  1.00 43.50  ? 57  ASP   C OD1 1 
ATOM   1861 O OD2 . ASP   C 1 58 ? 27.901  -35.691 22.856  1.00 49.47  ? 57  ASP   C OD2 1 
ATOM   1862 N N   . LEU   C 1 59 ? 28.042  -29.978 22.069  1.00 33.78  ? 58  LEU   C N   1 
ATOM   1863 C CA  . LEU   C 1 59 ? 27.124  -28.858 22.187  1.00 35.55  ? 58  LEU   C CA  1 
ATOM   1864 C C   . LEU   C 1 59 ? 27.732  -27.581 21.615  1.00 39.31  ? 58  LEU   C C   1 
ATOM   1865 O O   . LEU   C 1 59 ? 28.916  -27.319 21.850  1.00 46.24  ? 58  LEU   C O   1 
ATOM   1866 C CB  . LEU   C 1 59 ? 26.765  -28.653 23.658  1.00 32.42  ? 58  LEU   C CB  1 
ATOM   1867 C CG  . LEU   C 1 59 ? 26.135  -29.879 24.332  1.00 31.30  ? 58  LEU   C CG  1 
ATOM   1868 C CD1 . LEU   C 1 59 ? 25.858  -29.696 25.810  1.00 34.54  ? 58  LEU   C CD1 1 
ATOM   1869 C CD2 . LEU   C 1 59 ? 24.838  -30.306 23.615  1.00 28.56  ? 58  LEU   C CD2 1 
ATOM   1870 N N   . PHE   C 1 60 ? 26.899  -26.795 20.911  1.00 39.27  ? 59  PHE   C N   1 
ATOM   1871 C CA  . PHE   C 1 60 ? 27.364  -25.594 20.207  1.00 38.51  ? 59  PHE   C CA  1 
ATOM   1872 C C   . PHE   C 1 60 ? 26.404  -24.433 20.487  1.00 40.78  ? 59  PHE   C C   1 
ATOM   1873 O O   . PHE   C 1 60 ? 25.209  -24.528 20.218  1.00 37.43  ? 59  PHE   C O   1 
ATOM   1874 C CB  . PHE   C 1 60 ? 27.570  -25.873 18.707  1.00 35.54  ? 59  PHE   C CB  1 
ATOM   1875 C CG  . PHE   C 1 60 ? 28.544  -27.004 18.398  1.00 35.31  ? 59  PHE   C CG  1 
ATOM   1876 C CD1 . PHE   C 1 60 ? 28.120  -28.331 18.414  1.00 35.55  ? 59  PHE   C CD1 1 
ATOM   1877 C CD2 . PHE   C 1 60 ? 29.907  -26.768 18.209  1.00 41.51  ? 59  PHE   C CD2 1 
ATOM   1878 C CE1 . PHE   C 1 60 ? 29.013  -29.383 18.214  1.00 36.87  ? 59  PHE   C CE1 1 
ATOM   1879 C CE2 . PHE   C 1 60 ? 30.791  -27.814 17.966  1.00 40.75  ? 59  PHE   C CE2 1 
ATOM   1880 C CZ  . PHE   C 1 60 ? 30.350  -29.124 17.949  1.00 43.08  ? 59  PHE   C CZ  1 
ATOM   1881 N N   . PRO   C 1 61 ? 26.856  -23.288 21.069  1.00 42.12  ? 60  PRO   C N   1 
ATOM   1882 C CA  . PRO   C 1 61 ? 25.939  -22.178 21.351  1.00 41.10  ? 60  PRO   C CA  1 
ATOM   1883 C C   . PRO   C 1 61 ? 25.226  -21.699 20.084  1.00 34.53  ? 60  PRO   C C   1 
ATOM   1884 O O   . PRO   C 1 61 ? 25.825  -21.614 19.011  1.00 39.00  ? 60  PRO   C O   1 
ATOM   1885 C CB  . PRO   C 1 61 ? 26.796  -21.069 22.011  1.00 41.65  ? 60  PRO   C CB  1 
ATOM   1886 C CG  . PRO   C 1 61 ? 28.142  -21.722 22.266  1.00 45.31  ? 60  PRO   C CG  1 
ATOM   1887 C CD  . PRO   C 1 61 ? 28.252  -23.012 21.453  1.00 47.00  ? 60  PRO   C CD  1 
ATOM   1888 N N   . TYR   C 1 62 ? 23.905  -21.511 20.216  1.00 41.02  ? 61  TYR   C N   1 
ATOM   1889 C CA  . TYR   C 1 62 ? 22.997  -21.280 19.107  1.00 40.76  ? 61  TYR   C CA  1 
ATOM   1890 C C   . TYR   C 1 62 ? 23.436  -20.050 18.320  1.00 49.63  ? 61  TYR   C C   1 
ATOM   1891 O O   . TYR   C 1 62 ? 23.737  -20.155 17.124  1.00 52.25  ? 61  TYR   C O   1 
ATOM   1892 C CB  . TYR   C 1 62 ? 21.557  -21.061 19.580  1.00 41.90  ? 61  TYR   C CB  1 
ATOM   1893 C CG  . TYR   C 1 62 ? 20.599  -20.719 18.447  1.00 43.18  ? 61  TYR   C CG  1 
ATOM   1894 C CD1 . TYR   C 1 62 ? 20.441  -21.578 17.356  1.00 44.35  ? 61  TYR   C CD1 1 
ATOM   1895 C CD2 . TYR   C 1 62 ? 19.904  -19.513 18.440  1.00 45.30  ? 61  TYR   C CD2 1 
ATOM   1896 C CE1 . TYR   C 1 62 ? 19.576  -21.263 16.313  1.00 47.80  ? 61  TYR   C CE1 1 
ATOM   1897 C CE2 . TYR   C 1 62 ? 19.042  -19.190 17.402  1.00 48.24  ? 61  TYR   C CE2 1 
ATOM   1898 C CZ  . TYR   C 1 62 ? 18.872  -20.065 16.339  1.00 46.14  ? 61  TYR   C CZ  1 
ATOM   1899 O OH  . TYR   C 1 62 ? 18.018  -19.704 15.325  1.00 44.68  ? 61  TYR   C OH  1 
ATOM   1900 N N   . ASP   C 1 63 ? 23.509  -18.906 19.019  1.00 49.93  ? 62  ASP   C N   1 
ATOM   1901 C CA  . ASP   C 1 63 ? 23.779  -17.636 18.358  1.00 52.54  ? 62  ASP   C CA  1 
ATOM   1902 C C   . ASP   C 1 63 ? 25.117  -17.676 17.630  1.00 46.33  ? 62  ASP   C C   1 
ATOM   1903 O O   . ASP   C 1 63 ? 25.242  -17.116 16.537  1.00 52.37  ? 62  ASP   C O   1 
ATOM   1904 C CB  . ASP   C 1 63 ? 23.528  -16.443 19.267  1.00 54.58  ? 62  ASP   C CB  1 
ATOM   1905 C CG  . ASP   C 1 63 ? 22.068  -16.012 19.300  1.00 70.83  ? 62  ASP   C CG  1 
ATOM   1906 O OD1 . ASP   C 1 63 ? 21.485  -15.962 20.405  1.00 66.39  ? 62  ASP   C OD1 1 
ATOM   1907 O OD2 . ASP   C 1 63 ? 21.510  -15.755 18.206  1.00 79.73  ? 62  ASP   C OD2 1 
ATOM   1908 N N   . LYS   C 1 64 ? 26.087  -18.374 18.220  1.00 41.67  ? 63  LYS   C N   1 
ATOM   1909 C CA  . LYS   C 1 64 ? 27.438  -18.445 17.700  1.00 41.81  ? 63  LYS   C CA  1 
ATOM   1910 C C   . LYS   C 1 64 ? 27.477  -19.363 16.483  1.00 44.93  ? 63  LYS   C C   1 
ATOM   1911 O O   . LYS   C 1 64 ? 28.222  -19.094 15.551  1.00 41.01  ? 63  LYS   C O   1 
ATOM   1912 C CB  . LYS   C 1 64 ? 28.443  -18.881 18.778  1.00 48.90  ? 63  LYS   C CB  1 
ATOM   1913 N N   . SER   C 1 65 ? 26.637  -20.422 16.458  1.00 39.51  ? 64  SER   C N   1 
ATOM   1914 C CA  . SER   C 1 65 ? 26.839  -21.419 15.415  1.00 37.78  ? 64  SER   C CA  1 
ATOM   1915 C C   . SER   C 1 65 ? 25.677  -21.497 14.416  1.00 34.28  ? 64  SER   C C   1 
ATOM   1916 O O   . SER   C 1 65 ? 25.782  -22.270 13.464  1.00 34.72  ? 64  SER   C O   1 
ATOM   1917 C CB  . SER   C 1 65 ? 27.194  -22.787 15.963  1.00 38.28  ? 64  SER   C CB  1 
ATOM   1918 O OG  . SER   C 1 65 ? 26.079  -23.252 16.695  1.00 40.36  ? 64  SER   C OG  1 
ATOM   1919 N N   . LYS   C 1 66 ? 24.643  -20.662 14.564  1.00 33.13  ? 65  LYS   C N   1 
ATOM   1920 C CA  . LYS   C 1 66 ? 23.486  -20.797 13.672  1.00 36.37  ? 65  LYS   C CA  1 
ATOM   1921 C C   . LYS   C 1 66 ? 23.822  -20.520 12.204  1.00 39.79  ? 65  LYS   C C   1 
ATOM   1922 O O   . LYS   C 1 66 ? 23.235  -21.126 11.310  1.00 38.31  ? 65  LYS   C O   1 
ATOM   1923 C CB  . LYS   C 1 66 ? 22.266  -19.997 14.122  1.00 41.36  ? 65  LYS   C CB  1 
ATOM   1924 C CG  . LYS   C 1 66 ? 22.503  -18.505 14.172  1.00 36.71  ? 65  LYS   C CG  1 
ATOM   1925 C CD  . LYS   C 1 66 ? 21.176  -17.859 14.540  1.00 44.62  ? 65  LYS   C CD  1 
ATOM   1926 C CE  . LYS   C 1 66 ? 21.344  -16.411 14.847  1.00 45.03  ? 65  LYS   C CE  1 
ATOM   1927 N NZ  . LYS   C 1 66 ? 20.006  -15.928 15.155  1.00 47.68  ? 65  LYS   C NZ  1 
ATOM   1928 N N   . ASP   C 1 67 ? 24.786  -19.635 11.931  1.00 39.21  ? 66  ASP   C N   1 
ATOM   1929 C CA  . ASP   C 1 67 ? 25.148  -19.385 10.539  1.00 38.86  ? 66  ASP   C CA  1 
ATOM   1930 C C   . ASP   C 1 67 ? 25.568  -20.690 9.845   1.00 40.17  ? 66  ASP   C C   1 
ATOM   1931 O O   . ASP   C 1 67 ? 25.264  -20.881 8.678   1.00 39.37  ? 66  ASP   C O   1 
ATOM   1932 C CB  . ASP   C 1 67 ? 25.979  -18.105 10.374  1.00 42.54  ? 66  ASP   C CB  1 
ATOM   1933 C CG  . ASP   C 1 67 ? 27.498  -18.143 10.539  1.00 56.57  ? 66  ASP   C CG  1 
ATOM   1934 O OD1 . ASP   C 1 67 ? 28.129  -19.207 10.277  1.00 55.75  ? 66  ASP   C OD1 1 
ATOM   1935 O OD2 . ASP   C 1 67 ? 28.064  -17.083 10.925  1.00 53.79  ? 66  ASP   C OD2 1 
ATOM   1936 N N   . LYS   C 1 68 ? 26.229  -21.618 10.571  1.00 36.34  ? 67  LYS   C N   1 
ATOM   1937 C CA  . LYS   C 1 68 ? 26.689  -22.880 10.002  1.00 37.23  ? 67  LYS   C CA  1 
ATOM   1938 C C   . LYS   C 1 68 ? 25.625  -23.998 10.104  1.00 33.91  ? 67  LYS   C C   1 
ATOM   1939 O O   . LYS   C 1 68 ? 25.389  -24.763 9.159   1.00 38.00  ? 67  LYS   C O   1 
ATOM   1940 C CB  . LYS   C 1 68 ? 27.942  -23.157 10.838  1.00 36.98  ? 67  LYS   C CB  1 
ATOM   1941 C CG  . LYS   C 1 68 ? 28.818  -24.319 10.464  1.00 39.76  ? 67  LYS   C CG  1 
ATOM   1942 C CD  . LYS   C 1 68 ? 30.048  -24.259 11.376  1.00 47.78  ? 67  LYS   C CD  1 
ATOM   1943 C CE  . LYS   C 1 68 ? 30.910  -25.476 11.473  1.00 58.30  ? 67  LYS   C CE  1 
ATOM   1944 N NZ  . LYS   C 1 68 ? 31.257  -26.097 10.189  1.00 67.02  ? 67  LYS   C NZ  1 
ATOM   1945 N N   . TYR   C 1 69 ? 24.994  -24.125 11.274  1.00 33.43  ? 68  TYR   C N   1 
ATOM   1946 C CA  . TYR   C 1 69 ? 24.108  -25.269 11.466  1.00 31.70  ? 68  TYR   C CA  1 
ATOM   1947 C C   . TYR   C 1 69 ? 22.634  -24.951 11.256  1.00 31.33  ? 68  TYR   C C   1 
ATOM   1948 O O   . TYR   C 1 69 ? 21.854  -25.887 11.078  1.00 31.88  ? 68  TYR   C O   1 
ATOM   1949 C CB  . TYR   C 1 69 ? 24.266  -25.883 12.867  1.00 30.74  ? 68  TYR   C CB  1 
ATOM   1950 C CG  . TYR   C 1 69 ? 25.696  -26.335 13.137  1.00 29.57  ? 68  TYR   C CG  1 
ATOM   1951 C CD1 . TYR   C 1 69 ? 26.406  -27.135 12.238  1.00 34.10  ? 68  TYR   C CD1 1 
ATOM   1952 C CD2 . TYR   C 1 69 ? 26.311  -25.982 14.337  1.00 34.49  ? 68  TYR   C CD2 1 
ATOM   1953 C CE1 . TYR   C 1 69 ? 27.699  -27.579 12.513  1.00 35.42  ? 68  TYR   C CE1 1 
ATOM   1954 C CE2 . TYR   C 1 69 ? 27.595  -26.428 14.622  1.00 33.74  ? 68  TYR   C CE2 1 
ATOM   1955 C CZ  . TYR   C 1 69 ? 28.287  -27.202 13.711  1.00 35.70  ? 68  TYR   C CZ  1 
ATOM   1956 O OH  . TYR   C 1 69 ? 29.569  -27.555 14.043  1.00 41.05  ? 68  TYR   C OH  1 
ATOM   1957 N N   . GLY   C 1 70 ? 22.233  -23.666 11.272  1.00 30.68  ? 69  GLY   C N   1 
ATOM   1958 C CA  . GLY   C 1 70 ? 20.811  -23.361 11.211  1.00 29.70  ? 69  GLY   C CA  1 
ATOM   1959 C C   . GLY   C 1 70 ? 20.407  -23.229 9.750   1.00 35.41  ? 69  GLY   C C   1 
ATOM   1960 O O   . GLY   C 1 70 ? 20.350  -22.123 9.221   1.00 35.89  ? 69  GLY   C O   1 
ATOM   1961 N N   . LYS   C 1 71 ? 20.340  -24.382 9.087   1.00 33.31  ? 70  LYS   C N   1 
ATOM   1962 C CA  . LYS   C 1 71 ? 19.994  -24.482 7.675   1.00 34.77  ? 70  LYS   C CA  1 
ATOM   1963 C C   . LYS   C 1 71 ? 19.086  -25.694 7.560   1.00 35.30  ? 70  LYS   C C   1 
ATOM   1964 O O   . LYS   C 1 71 ? 19.206  -26.658 8.325   1.00 34.34  ? 70  LYS   C O   1 
ATOM   1965 C CB  . LYS   C 1 71 ? 21.190  -24.664 6.731   1.00 36.04  ? 70  LYS   C CB  1 
ATOM   1966 C CG  . LYS   C 1 71 ? 22.213  -25.612 7.289   1.00 39.61  ? 70  LYS   C CG  1 
ATOM   1967 C CD  . LYS   C 1 71 ? 23.308  -26.135 6.370   1.00 45.01  ? 70  LYS   C CD  1 
ATOM   1968 C CE  . LYS   C 1 71 ? 24.114  -27.152 7.135   1.00 48.01  ? 70  LYS   C CE  1 
ATOM   1969 N N   . PRO   C 1 72 ? 18.107  -25.679 6.642   1.00 27.80  ? 71  PRO   C N   1 
ATOM   1970 C CA  . PRO   C 1 72 ? 17.162  -26.785 6.569   1.00 27.30  ? 71  PRO   C CA  1 
ATOM   1971 C C   . PRO   C 1 72 ? 17.803  -28.117 6.222   1.00 28.66  ? 71  PRO   C C   1 
ATOM   1972 O O   . PRO   C 1 72 ? 18.830  -28.182 5.540   1.00 33.24  ? 71  PRO   C O   1 
ATOM   1973 C CB  . PRO   C 1 72 ? 16.204  -26.360 5.441   1.00 27.62  ? 71  PRO   C CB  1 
ATOM   1974 C CG  . PRO   C 1 72 ? 16.282  -24.846 5.459   1.00 28.85  ? 71  PRO   C CG  1 
ATOM   1975 C CD  . PRO   C 1 72 ? 17.732  -24.516 5.800   1.00 28.26  ? 71  PRO   C CD  1 
ATOM   1976 N N   . ASN   C 1 73 ? 17.108  -29.142 6.675   1.00 29.79  ? 72  ASN   C N   1 
ATOM   1977 C CA  . ASN   C 1 73 ? 17.381  -30.475 6.166   1.00 35.48  ? 72  ASN   C CA  1 
ATOM   1978 C C   . ASN   C 1 73 ? 16.118  -31.322 6.276   1.00 33.74  ? 72  ASN   C C   1 
ATOM   1979 O O   . ASN   C 1 73 ? 15.164  -30.959 6.958   1.00 33.66  ? 72  ASN   C O   1 
ATOM   1980 C CB  . ASN   C 1 73 ? 18.745  -31.022 6.578   1.00 42.20  ? 72  ASN   C CB  1 
ATOM   1981 C CG  . ASN   C 1 73 ? 18.693  -31.661 7.939   1.00 42.45  ? 72  ASN   C CG  1 
ATOM   1982 O OD1 . ASN   C 1 73 ? 17.845  -32.526 8.185   1.00 46.74  ? 72  ASN   C OD1 1 
ATOM   1983 N ND2 . ASN   C 1 73 ? 19.618  -31.286 8.800   1.00 45.74  ? 72  ASN   C ND2 1 
ATOM   1984 N N   . LYS   C 1 74 ? 16.152  -32.497 5.639   1.00 33.54  ? 73  LYS   C N   1 
ATOM   1985 C CA  . LYS   C 1 74 ? 14.918  -33.244 5.435   1.00 29.45  ? 73  LYS   C CA  1 
ATOM   1986 C C   . LYS   C 1 74 ? 14.679  -34.228 6.573   1.00 31.17  ? 73  LYS   C C   1 
ATOM   1987 O O   . LYS   C 1 74 ? 13.627  -34.871 6.632   1.00 35.17  ? 73  LYS   C O   1 
ATOM   1988 C CB  . LYS   C 1 74 ? 14.883  -33.976 4.084   1.00 32.61  ? 73  LYS   C CB  1 
ATOM   1989 N N   . ARG   C 1 75 ? 15.592  -34.273 7.564   1.00 28.63  ? 74  ARG   C N   1 
ATOM   1990 C CA  . ARG   C 1 75 ? 15.365  -35.220 8.648   1.00 28.27  ? 74  ARG   C CA  1 
ATOM   1991 C C   . ARG   C 1 75 ? 14.082  -34.930 9.433   1.00 30.80  ? 74  ARG   C C   1 
ATOM   1992 O O   . ARG   C 1 75 ? 13.690  -33.780 9.684   1.00 30.89  ? 74  ARG   C O   1 
ATOM   1993 C CB  . ARG   C 1 75 ? 16.590  -35.295 9.579   1.00 31.28  ? 74  ARG   C CB  1 
ATOM   1994 C CG  . ARG   C 1 75 ? 17.943  -35.535 8.909   1.00 38.05  ? 74  ARG   C CG  1 
ATOM   1995 C CD  . ARG   C 1 75 ? 18.235  -36.917 8.288   1.00 40.69  ? 74  ARG   C CD  1 
ATOM   1996 N NE  . ARG   C 1 75 ? 18.126  -37.879 9.383   1.00 36.57  ? 74  ARG   C NE  1 
ATOM   1997 C CZ  . ARG   C 1 75 ? 19.211  -38.370 10.022  1.00 35.10  ? 74  ARG   C CZ  1 
ATOM   1998 N NH1 . ARG   C 1 75 ? 19.074  -39.030 11.146  1.00 41.54  ? 74  ARG   C NH1 1 
ATOM   1999 N NH2 . ARG   C 1 75 ? 20.400  -38.111 9.541   1.00 34.07  ? 74  ARG   C NH2 1 
ATOM   2000 N N   . LYS   C 1 76 ? 13.450  -36.012 9.899   1.00 33.95  ? 75  LYS   C N   1 
ATOM   2001 C CA  . LYS   C 1 76 ? 12.161  -35.896 10.560  1.00 36.62  ? 75  LYS   C CA  1 
ATOM   2002 C C   . LYS   C 1 76 ? 12.250  -34.908 11.719  1.00 32.68  ? 75  LYS   C C   1 
ATOM   2003 O O   . LYS   C 1 76 ? 13.026  -35.062 12.674  1.00 33.26  ? 75  LYS   C O   1 
ATOM   2004 C CB  . LYS   C 1 76 ? 11.556  -37.239 10.994  1.00 38.60  ? 75  LYS   C CB  1 
ATOM   2005 C CG  . LYS   C 1 76 ? 10.046  -37.137 11.162  1.00 45.09  ? 75  LYS   C CG  1 
ATOM   2006 C CD  . LYS   C 1 76 ? 9.383   -38.211 12.028  1.00 49.70  ? 75  LYS   C CD  1 
ATOM   2007 N N   . GLY   C 1 77 ? 11.471  -33.827 11.573  1.00 32.80  ? 76  GLY   C N   1 
ATOM   2008 C CA  . GLY   C 1 77 ? 11.217  -32.933 12.686  1.00 29.03  ? 76  GLY   C CA  1 
ATOM   2009 C C   . GLY   C 1 77 ? 12.193  -31.753 12.691  1.00 28.84  ? 76  GLY   C C   1 
ATOM   2010 O O   . GLY   C 1 77 ? 12.035  -30.826 13.487  1.00 33.16  ? 76  GLY   C O   1 
ATOM   2011 N N   . PHE   C 1 78 ? 13.200  -31.795 11.819  1.00 28.78  ? 77  PHE   C N   1 
ATOM   2012 C CA  . PHE   C 1 78 ? 14.298  -30.848 11.881  1.00 26.86  ? 77  PHE   C CA  1 
ATOM   2013 C C   . PHE   C 1 78 ? 13.828  -29.420 11.583  1.00 28.88  ? 77  PHE   C C   1 
ATOM   2014 O O   . PHE   C 1 78 ? 14.208  -28.459 12.252  1.00 27.59  ? 77  PHE   C O   1 
ATOM   2015 C CB  . PHE   C 1 78 ? 15.390  -31.257 10.894  1.00 30.16  ? 77  PHE   C CB  1 
ATOM   2016 C CG  . PHE   C 1 78 ? 16.671  -30.478 11.137  1.00 26.14  ? 77  PHE   C CG  1 
ATOM   2017 C CD1 . PHE   C 1 78 ? 16.863  -29.210 10.583  1.00 27.72  ? 77  PHE   C CD1 1 
ATOM   2018 C CD2 . PHE   C 1 78 ? 17.685  -31.008 11.935  1.00 27.61  ? 77  PHE   C CD2 1 
ATOM   2019 C CE1 . PHE   C 1 78 ? 18.037  -28.512 10.804  1.00 29.10  ? 77  PHE   C CE1 1 
ATOM   2020 C CE2 . PHE   C 1 78 ? 18.868  -30.296 12.151  1.00 26.41  ? 77  PHE   C CE2 1 
ATOM   2021 C CZ  . PHE   C 1 78 ? 19.053  -29.049 11.579  1.00 27.38  ? 77  PHE   C CZ  1 
ATOM   2022 N N   . ASN   C 1 79 ? 13.053  -29.269 10.503  1.00 28.07  ? 78  ASN   C N   1 
ATOM   2023 C CA  . ASN   C 1 79 ? 12.722  -27.904 10.121  1.00 31.39  ? 78  ASN   C CA  1 
ATOM   2024 C C   . ASN   C 1 79 ? 11.699  -27.280 11.061  1.00 29.13  ? 78  ASN   C C   1 
ATOM   2025 O O   . ASN   C 1 79 ? 11.749  -26.071 11.341  1.00 29.96  ? 78  ASN   C O   1 
ATOM   2026 C CB  . ASN   C 1 79 ? 12.255  -27.894 8.681   1.00 28.28  ? 78  ASN   C CB  1 
ATOM   2027 C CG  . ASN   C 1 79 ? 13.375  -28.245 7.738   1.00 28.72  ? 78  ASN   C CG  1 
ATOM   2028 O OD1 . ASN   C 1 79 ? 14.543  -27.949 8.007   1.00 27.54  ? 78  ASN   C OD1 1 
ATOM   2029 N ND2 . ASN   C 1 79 ? 13.021  -28.798 6.580   1.00 28.83  ? 78  ASN   C ND2 1 
ATOM   2030 N N   . GLU   C 1 80 ? 10.807  -28.095 11.603  1.00 30.58  ? 79  GLU   C N   1 
ATOM   2031 C CA  . GLU   C 1 80 ? 9.966   -27.583 12.671  1.00 29.87  ? 79  GLU   C CA  1 
ATOM   2032 C C   . GLU   C 1 80 ? 10.838  -27.184 13.861  1.00 35.61  ? 79  GLU   C C   1 
ATOM   2033 O O   . GLU   C 1 80 ? 10.576  -26.161 14.494  1.00 33.61  ? 79  GLU   C O   1 
ATOM   2034 C CB  . GLU   C 1 80 ? 8.876   -28.601 13.006  1.00 37.48  ? 79  GLU   C CB  1 
ATOM   2035 C CG  . GLU   C 1 80 ? 8.023   -28.172 14.191  1.00 39.67  ? 79  GLU   C CG  1 
ATOM   2036 C CD  . GLU   C 1 80 ? 6.767   -28.988 14.367  1.00 49.03  ? 79  GLU   C CD  1 
ATOM   2037 O OE1 . GLU   C 1 80 ? 6.654   -30.130 13.854  1.00 52.48  ? 79  GLU   C OE1 1 
ATOM   2038 O OE2 . GLU   C 1 80 ? 5.863   -28.417 15.002  1.00 47.88  ? 79  GLU   C OE2 1 
ATOM   2039 N N   . GLY   C 1 81 ? 11.907  -27.977 14.153  1.00 29.28  ? 80  GLY   C N   1 
ATOM   2040 C CA  . GLY   C 1 81 ? 12.837  -27.560 15.197  1.00 29.88  ? 80  GLY   C CA  1 
ATOM   2041 C C   . GLY   C 1 81 ? 13.489  -26.199 14.955  1.00 31.51  ? 80  GLY   C C   1 
ATOM   2042 O O   . GLY   C 1 81 ? 13.689  -25.446 15.898  1.00 30.50  ? 80  GLY   C O   1 
ATOM   2043 N N   . LEU   C 1 82 ? 13.900  -25.916 13.699  1.00 31.44  ? 81  LEU   C N   1 
ATOM   2044 C CA  . LEU   C 1 82 ? 14.514  -24.640 13.353  1.00 30.99  ? 81  LEU   C CA  1 
ATOM   2045 C C   . LEU   C 1 82 ? 13.501  -23.529 13.616  1.00 27.95  ? 81  LEU   C C   1 
ATOM   2046 O O   . LEU   C 1 82 ? 13.903  -22.446 14.063  1.00 29.62  ? 81  LEU   C O   1 
ATOM   2047 C CB  . LEU   C 1 82 ? 14.939  -24.613 11.891  1.00 30.20  ? 81  LEU   C CB  1 
ATOM   2048 C CG  . LEU   C 1 82 ? 16.188  -25.412 11.505  1.00 28.60  ? 81  LEU   C CG  1 
ATOM   2049 C CD1 . LEU   C 1 82 ? 16.524  -25.246 10.035  1.00 27.18  ? 81  LEU   C CD1 1 
ATOM   2050 C CD2 . LEU   C 1 82 ? 17.410  -25.042 12.286  1.00 26.65  ? 81  LEU   C CD2 1 
ATOM   2051 N N   . TRP   C 1 83 ? 12.223  -23.792 13.315  1.00 29.40  ? 82  TRP   C N   1 
ATOM   2052 C CA  . TRP   C 1 83 ? 11.226  -22.748 13.536  1.00 33.77  ? 82  TRP   C CA  1 
ATOM   2053 C C   . TRP   C 1 83 ? 11.114  -22.480 15.041  1.00 35.41  ? 82  TRP   C C   1 
ATOM   2054 O O   . TRP   C 1 83 ? 11.131  -21.323 15.475  1.00 34.73  ? 82  TRP   C O   1 
ATOM   2055 C CB  . TRP   C 1 83 ? 9.861   -23.122 12.930  1.00 36.27  ? 82  TRP   C CB  1 
ATOM   2056 C CG  . TRP   C 1 83 ? 8.878   -21.986 13.053  1.00 38.56  ? 82  TRP   C CG  1 
ATOM   2057 C CD1 . TRP   C 1 83 ? 8.736   -20.954 12.166  1.00 39.63  ? 82  TRP   C CD1 1 
ATOM   2058 C CD2 . TRP   C 1 83 ? 7.996   -21.702 14.162  1.00 41.31  ? 82  TRP   C CD2 1 
ATOM   2059 N NE1 . TRP   C 1 83 ? 7.772   -20.086 12.614  1.00 37.09  ? 82  TRP   C NE1 1 
ATOM   2060 C CE2 . TRP   C 1 83 ? 7.310   -20.503 13.834  1.00 39.33  ? 82  TRP   C CE2 1 
ATOM   2061 C CE3 . TRP   C 1 83 ? 7.708   -22.346 15.378  1.00 37.89  ? 82  TRP   C CE3 1 
ATOM   2062 C CZ2 . TRP   C 1 83 ? 6.368   -19.935 14.686  1.00 42.25  ? 82  TRP   C CZ2 1 
ATOM   2063 C CZ3 . TRP   C 1 83 ? 6.767   -21.784 16.218  1.00 47.50  ? 82  TRP   C CZ3 1 
ATOM   2064 C CH2 . TRP   C 1 83 ? 6.125   -20.587 15.880  1.00 45.36  ? 82  TRP   C CH2 1 
ATOM   2065 N N   . GLU   C 1 84 ? 11.069  -23.569 15.832  1.00 32.02  ? 83  GLU   C N   1 
ATOM   2066 C CA  . GLU   C 1 84 ? 10.957  -23.416 17.284  1.00 35.25  ? 83  GLU   C CA  1 
ATOM   2067 C C   . GLU   C 1 84 ? 12.126  -22.656 17.928  1.00 34.69  ? 83  GLU   C C   1 
ATOM   2068 O O   . GLU   C 1 84 ? 11.898  -21.795 18.804  1.00 38.21  ? 83  GLU   C O   1 
ATOM   2069 C CB  . GLU   C 1 84 ? 10.766  -24.786 17.923  1.00 33.73  ? 83  GLU   C CB  1 
ATOM   2070 C CG  . GLU   C 1 84 ? 9.413   -25.400 17.604  1.00 35.35  ? 83  GLU   C CG  1 
ATOM   2071 C CD  . GLU   C 1 84 ? 9.304   -26.800 18.129  1.00 38.51  ? 83  GLU   C CD  1 
ATOM   2072 O OE1 . GLU   C 1 84 ? 10.294  -27.267 18.756  1.00 38.78  ? 83  GLU   C OE1 1 
ATOM   2073 O OE2 . GLU   C 1 84 ? 8.246   -27.418 17.904  1.00 39.09  ? 83  GLU   C OE2 1 
ATOM   2074 N N   . ILE   C 1 85 ? 13.385  -22.965 17.568  1.00 33.65  ? 84  ILE   C N   1 
ATOM   2075 C CA  . ILE   C 1 85 ? 14.541  -22.351 18.201  1.00 35.33  ? 84  ILE   C CA  1 
ATOM   2076 C C   . ILE   C 1 85 ? 14.621  -20.844 17.917  1.00 34.53  ? 84  ILE   C C   1 
ATOM   2077 O O   . ILE   C 1 85 ? 15.161  -20.096 18.726  1.00 36.69  ? 84  ILE   C O   1 
ATOM   2078 C CB  . ILE   C 1 85 ? 15.856  -23.084 17.891  1.00 35.39  ? 84  ILE   C CB  1 
ATOM   2079 C CG1 . ILE   C 1 85 ? 16.901  -22.783 18.955  1.00 34.20  ? 84  ILE   C CG1 1 
ATOM   2080 C CG2 . ILE   C 1 85 ? 16.356  -22.769 16.468  1.00 32.45  ? 84  ILE   C CG2 1 
ATOM   2081 C CD1 . ILE   C 1 85 ? 18.066  -23.752 18.975  1.00 31.36  ? 84  ILE   C CD1 1 
ATOM   2082 N N   . GLN   C 1 86 ? 14.083  -20.424 16.758  1.00 31.94  ? 85  GLN   C N   1 
ATOM   2083 C CA  . GLN   C 1 86 ? 14.167  -19.021 16.376  1.00 37.63  ? 85  GLN   C CA  1 
ATOM   2084 C C   . GLN   C 1 86 ? 12.943  -18.257 16.871  1.00 36.04  ? 85  GLN   C C   1 
ATOM   2085 O O   . GLN   C 1 86 ? 13.058  -17.067 17.175  1.00 40.94  ? 85  GLN   C O   1 
ATOM   2086 C CB  . GLN   C 1 86 ? 14.334  -18.885 14.856  1.00 34.03  ? 85  GLN   C CB  1 
ATOM   2087 C CG  . GLN   C 1 86 ? 14.469  -17.452 14.338  1.00 34.16  ? 85  GLN   C CG  1 
ATOM   2088 C CD  . GLN   C 1 86 ? 14.799  -17.426 12.857  1.00 36.88  ? 85  GLN   C CD  1 
ATOM   2089 O OE1 . GLN   C 1 86 ? 14.658  -18.433 12.142  1.00 37.02  ? 85  GLN   C OE1 1 
ATOM   2090 N NE2 . GLN   C 1 86 ? 15.312  -16.299 12.380  1.00 41.70  ? 85  GLN   C NE2 1 
ATOM   2091 N N   . ASN   C 1 87 ? 11.791  -18.914 16.931  1.00 37.85  ? 86  ASN   C N   1 
ATOM   2092 C CA  . ASN   C 1 87 ? 10.551  -18.174 17.115  1.00 41.67  ? 86  ASN   C CA  1 
ATOM   2093 C C   . ASN   C 1 87 ? 9.955   -18.396 18.497  1.00 45.44  ? 86  ASN   C C   1 
ATOM   2094 O O   . ASN   C 1 87 ? 9.259   -17.517 18.989  1.00 42.74  ? 86  ASN   C O   1 
ATOM   2095 C CB  . ASN   C 1 87 ? 9.527   -18.414 16.015  1.00 39.34  ? 86  ASN   C CB  1 
ATOM   2096 C CG  . ASN   C 1 87 ? 10.100  -17.897 14.727  1.00 40.34  ? 86  ASN   C CG  1 
ATOM   2097 O OD1 . ASN   C 1 87 ? 10.205  -16.678 14.559  1.00 42.85  ? 86  ASN   C OD1 1 
ATOM   2098 N ND2 . ASN   C 1 87 ? 10.565  -18.789 13.864  1.00 35.62  ? 86  ASN   C ND2 1 
ATOM   2099 N N   . ASN   C 1 88 ? 10.225  -19.551 19.112  1.00 42.74  ? 87  ASN   C N   1 
ATOM   2100 C CA  . ASN   C 1 88 ? 9.497   -19.910 20.323  1.00 43.23  ? 87  ASN   C CA  1 
ATOM   2101 C C   . ASN   C 1 88 ? 10.360  -20.776 21.247  1.00 39.26  ? 87  ASN   C C   1 
ATOM   2102 O O   . ASN   C 1 88 ? 9.904   -21.843 21.677  1.00 45.40  ? 87  ASN   C O   1 
ATOM   2103 C CB  . ASN   C 1 88 ? 8.174   -20.582 19.977  1.00 48.02  ? 87  ASN   C CB  1 
ATOM   2104 C CG  . ASN   C 1 88 ? 7.236   -20.637 21.162  1.00 54.14  ? 87  ASN   C CG  1 
ATOM   2105 O OD1 . ASN   C 1 88 ? 7.459   -19.935 22.157  1.00 55.45  ? 87  ASN   C OD1 1 
ATOM   2106 N ND2 . ASN   C 1 88 ? 6.187   -21.442 21.066  1.00 51.57  ? 87  ASN   C ND2 1 
ATOM   2107 N N   . PRO   C 1 89 ? 11.620  -20.383 21.539  1.00 37.96  ? 88  PRO   C N   1 
ATOM   2108 C CA  . PRO   C 1 89 ? 12.580  -21.288 22.181  1.00 38.75  ? 88  PRO   C CA  1 
ATOM   2109 C C   . PRO   C 1 89 ? 12.270  -21.747 23.604  1.00 46.58  ? 88  PRO   C C   1 
ATOM   2110 O O   . PRO   C 1 89 ? 12.841  -22.739 24.062  1.00 43.54  ? 88  PRO   C O   1 
ATOM   2111 C CB  . PRO   C 1 89 ? 13.922  -20.562 22.100  1.00 37.54  ? 88  PRO   C CB  1 
ATOM   2112 C CG  . PRO   C 1 89 ? 13.503  -19.094 22.025  1.00 45.46  ? 88  PRO   C CG  1 
ATOM   2113 C CD  . PRO   C 1 89 ? 12.248  -19.106 21.158  1.00 37.26  ? 88  PRO   C CD  1 
ATOM   2114 N N   . HIS   C 1 90 ? 11.363  -21.040 24.293  1.00 48.95  ? 89  HIS   C N   1 
ATOM   2115 C CA  . HIS   C 1 90 ? 11.128  -21.377 25.693  1.00 48.77  ? 89  HIS   C CA  1 
ATOM   2116 C C   . HIS   C 1 90 ? 9.696   -21.821 25.996  1.00 52.91  ? 89  HIS   C C   1 
ATOM   2117 O O   . HIS   C 1 90 ? 9.354   -21.940 27.166  1.00 58.48  ? 89  HIS   C O   1 
ATOM   2118 C CB  . HIS   C 1 90 ? 11.591  -20.258 26.622  1.00 40.78  ? 89  HIS   C CB  1 
ATOM   2119 C CG  . HIS   C 1 90 ? 12.977  -19.787 26.333  1.00 38.99  ? 89  HIS   C CG  1 
ATOM   2120 N ND1 . HIS   C 1 90 ? 14.123  -20.513 26.607  1.00 45.57  ? 89  HIS   C ND1 1 
ATOM   2121 C CD2 . HIS   C 1 90 ? 13.377  -18.647 25.781  1.00 39.77  ? 89  HIS   C CD2 1 
ATOM   2122 C CE1 . HIS   C 1 90 ? 15.193  -19.807 26.239  1.00 41.59  ? 89  HIS   C CE1 1 
ATOM   2123 N NE2 . HIS   C 1 90 ? 14.748  -18.666 25.710  1.00 39.55  ? 89  HIS   C NE2 1 
ATOM   2124 N N   . ALA   C 1 91 ? 8.871   -22.088 24.977  1.00 55.37  ? 90  ALA   C N   1 
ATOM   2125 C CA  . ALA   C 1 91 ? 7.575   -22.722 25.193  1.00 55.59  ? 90  ALA   C CA  1 
ATOM   2126 C C   . ALA   C 1 91 ? 7.755   -24.143 25.738  1.00 67.88  ? 90  ALA   C C   1 
ATOM   2127 O O   . ALA   C 1 91 ? 8.865   -24.680 25.741  1.00 64.68  ? 90  ALA   C O   1 
ATOM   2128 C CB  . ALA   C 1 91 ? 6.742   -22.720 23.924  1.00 55.99  ? 90  ALA   C CB  1 
ATOM   2129 N N   . SER   C 1 92 ? 6.630   -24.752 26.152  1.00 76.64  ? 91  SER   C N   1 
ATOM   2130 C CA  . SER   C 1 92 ? 6.586   -26.011 26.886  1.00 77.60  ? 91  SER   C CA  1 
ATOM   2131 C C   . SER   C 1 92 ? 6.847   -27.207 25.972  1.00 73.52  ? 91  SER   C C   1 
ATOM   2132 O O   . SER   C 1 92 ? 7.891   -27.838 26.086  1.00 81.98  ? 91  SER   C O   1 
ATOM   2133 C CB  . SER   C 1 92 ? 5.272   -26.160 27.620  1.00 81.74  ? 91  SER   C CB  1 
ATOM   2134 O OG  . SER   C 1 92 ? 5.116   -25.124 28.577  1.00 83.13  ? 91  SER   C OG  1 
ATOM   2135 N N   . TYR   C 1 93 ? 5.866   -27.526 25.111  1.00 76.37  ? 92  TYR   C N   1 
ATOM   2136 C CA  . TYR   C 1 93 ? 5.916   -28.586 24.106  1.00 77.29  ? 92  TYR   C CA  1 
ATOM   2137 C C   . TYR   C 1 93 ? 5.472   -29.937 24.694  1.00 75.71  ? 92  TYR   C C   1 
ATOM   2138 O O   . TYR   C 1 93 ? 5.625   -30.160 25.913  1.00 87.79  ? 92  TYR   C O   1 
ATOM   2139 C CB  . TYR   C 1 93 ? 7.254   -28.687 23.364  1.00 68.88  ? 92  TYR   C CB  1 
ATOM   2140 C CG  . TYR   C 1 93 ? 7.633   -27.418 22.609  1.00 58.22  ? 92  TYR   C CG  1 
ATOM   2141 C CD1 . TYR   C 1 93 ? 7.001   -27.076 21.416  1.00 51.02  ? 92  TYR   C CD1 1 
ATOM   2142 C CD2 . TYR   C 1 93 ? 8.629   -26.572 23.087  1.00 54.91  ? 92  TYR   C CD2 1 
ATOM   2143 C CE1 . TYR   C 1 93 ? 7.346   -25.930 20.718  1.00 53.92  ? 92  TYR   C CE1 1 
ATOM   2144 C CE2 . TYR   C 1 93 ? 8.973   -25.418 22.399  1.00 57.25  ? 92  TYR   C CE2 1 
ATOM   2145 C CZ  . TYR   C 1 93 ? 8.342   -25.103 21.209  1.00 54.19  ? 92  TYR   C CZ  1 
ATOM   2146 O OH  . TYR   C 1 93 ? 8.681   -23.960 20.533  1.00 60.43  ? 92  TYR   C OH  1 
HETATM 2147 S S   . SO4   D 2 .  ? 1.328   -33.417 1.939   1.00 115.70 ? 101 SO4   A S   1 
HETATM 2148 O O1  . SO4   D 2 .  ? 2.038   -34.301 1.052   1.00 105.11 ? 101 SO4   A O1  1 
HETATM 2149 O O2  . SO4   D 2 .  ? 1.186   -32.123 1.320   1.00 115.09 ? 101 SO4   A O2  1 
HETATM 2150 O O3  . SO4   D 2 .  ? 0.024   -33.963 2.214   1.00 123.75 ? 101 SO4   A O3  1 
HETATM 2151 O O4  . SO4   D 2 .  ? 2.060   -33.286 3.170   1.00 114.34 ? 101 SO4   A O4  1 
HETATM 2152 S S   . SO4   E 2 .  ? -9.089  -24.880 1.272   1.00 95.56  ? 102 SO4   A S   1 
HETATM 2153 O O1  . SO4   E 2 .  ? -8.827  -24.401 -0.061  1.00 84.90  ? 102 SO4   A O1  1 
HETATM 2154 O O2  . SO4   E 2 .  ? -9.013  -23.785 2.210   1.00 86.59  ? 102 SO4   A O2  1 
HETATM 2155 O O3  . SO4   E 2 .  ? -10.400 -25.474 1.308   1.00 97.85  ? 102 SO4   A O3  1 
HETATM 2156 O O4  . SO4   E 2 .  ? -8.115  -25.874 1.637   1.00 93.48  ? 102 SO4   A O4  1 
HETATM 2157 C C1  . EDO   F 3 .  ? 14.229  -19.596 -7.360  1.00 35.86  ? 103 EDO   A C1  1 
HETATM 2158 O O1  . EDO   F 3 .  ? 15.396  -18.835 -7.243  1.00 33.49  ? 103 EDO   A O1  1 
HETATM 2159 C C2  . EDO   F 3 .  ? 13.349  -19.052 -8.442  1.00 34.31  ? 103 EDO   A C2  1 
HETATM 2160 O O2  . EDO   F 3 .  ? 12.855  -17.752 -8.204  1.00 33.36  ? 103 EDO   A O2  1 
HETATM 2161 C C4  . A1A33 G 4 .  ? 0.345   -26.701 -5.762  0.60 50.83  ? 104 A1A33 A C4  1 
HETATM 2162 C C5  . A1A33 G 4 .  ? 1.355   -26.394 -6.860  0.60 53.63  ? 104 A1A33 A C5  1 
HETATM 2163 C C6  . A1A33 G 4 .  ? 2.201   -25.179 -6.509  0.60 50.07  ? 104 A1A33 A C6  1 
HETATM 2164 C C7  . A1A33 G 4 .  ? 2.430   -24.067 -7.506  0.60 59.09  ? 104 A1A33 A C7  1 
HETATM 2165 C C8  . A1A33 G 4 .  ? 1.628   -24.544 -5.256  0.60 51.46  ? 104 A1A33 A C8  1 
HETATM 2166 O O   . A1A33 G 4 .  ? 1.830   -24.377 -8.752  0.60 62.64  ? 104 A1A33 A O   1 
HETATM 2167 C C3  . A1A33 G 4 .  ? 0.989   -26.673 -4.371  0.60 52.00  ? 104 A1A33 A C3  1 
HETATM 2168 N N   . A1A33 G 4 .  ? 1.832   -25.485 -4.148  0.60 48.30  ? 104 A1A33 A N   1 
HETATM 2169 C C1  . A1A33 G 4 .  ? 2.003   -24.800 -2.854  0.60 42.76  ? 104 A1A33 A C1  1 
HETATM 2170 C C2  . A1A33 G 4 .  ? 0.794   -24.848 -1.941  0.60 45.74  ? 104 A1A33 A C2  1 
HETATM 2171 C C   . A1A33 G 4 .  ? 3.296   -25.226 -2.198  0.60 27.99  ? 104 A1A33 A C   1 
HETATM 2172 S S   . SO4   H 2 .  ? 9.321   -29.456 5.924   1.00 56.52  ? 105 SO4   A S   1 
HETATM 2173 O O1  . SO4   H 2 .  ? 10.106  -28.725 4.993   1.00 48.15  ? 105 SO4   A O1  1 
HETATM 2174 O O2  . SO4   H 2 .  ? 8.639   -30.532 5.210   1.00 64.92  ? 105 SO4   A O2  1 
HETATM 2175 O O3  . SO4   H 2 .  ? 10.173  -30.030 6.955   1.00 60.43  ? 105 SO4   A O3  1 
HETATM 2176 O O4  . SO4   H 2 .  ? 8.337   -28.581 6.512   1.00 74.55  ? 105 SO4   A O4  1 
HETATM 2177 S S   . SO4   I 2 .  ? 7.639   -8.394  -24.951 1.00 74.54  ? 101 SO4   B S   1 
HETATM 2178 O O1  . SO4   I 2 .  ? 8.783   -8.463  -25.822 1.00 40.62  ? 101 SO4   B O1  1 
HETATM 2179 O O2  . SO4   I 2 .  ? 6.472   -8.876  -25.649 1.00 65.89  ? 101 SO4   B O2  1 
HETATM 2180 O O3  . SO4   I 2 .  ? 7.820   -9.219  -23.746 1.00 46.41  ? 101 SO4   B O3  1 
HETATM 2181 O O4  . SO4   I 2 .  ? 7.490   -6.987  -24.608 1.00 55.15  ? 101 SO4   B O4  1 
HETATM 2182 S S   . SO4   J 2 .  ? 14.407  -27.076 -26.752 1.00 49.50  ? 102 SO4   B S   1 
HETATM 2183 O O1  . SO4   J 2 .  ? 15.700  -26.664 -26.326 1.00 48.61  ? 102 SO4   B O1  1 
HETATM 2184 O O2  . SO4   J 2 .  ? 14.522  -28.425 -27.258 1.00 63.67  ? 102 SO4   B O2  1 
HETATM 2185 O O3  . SO4   J 2 .  ? 13.502  -27.055 -25.636 1.00 63.83  ? 102 SO4   B O3  1 
HETATM 2186 O O4  . SO4   J 2 .  ? 13.889  -26.217 -27.798 1.00 50.98  ? 102 SO4   B O4  1 
HETATM 2187 C C4  . A1A33 K 4 .  ? 19.731  -17.060 -22.546 0.90 36.19  ? 103 A1A33 B C4  1 
HETATM 2188 C C5  . A1A33 K 4 .  ? 20.694  -15.912 -22.705 0.90 45.47  ? 103 A1A33 B C5  1 
HETATM 2189 C C6  . A1A33 K 4 .  ? 21.174  -15.806 -24.140 0.90 40.97  ? 103 A1A33 B C6  1 
HETATM 2190 C C7  . A1A33 K 4 .  ? 22.440  -15.023 -24.367 0.90 50.28  ? 103 A1A33 B C7  1 
HETATM 2191 C C8  . A1A33 K 4 .  ? 20.000  -15.471 -25.053 0.90 29.89  ? 103 A1A33 B C8  1 
HETATM 2192 O O   . A1A33 K 4 .  ? 23.511  -15.640 -23.648 0.90 54.62  ? 103 A1A33 B O   1 
HETATM 2193 C C3  . A1A33 K 4 .  ? 18.760  -17.076 -23.703 0.90 31.17  ? 103 A1A33 B C3  1 
HETATM 2194 N N   . A1A33 K 4 .  ? 18.696  -15.778 -24.429 0.90 28.02  ? 103 A1A33 B N   1 
HETATM 2195 C C1  . A1A33 K 4 .  ? 17.576  -15.678 -25.391 0.90 27.02  ? 103 A1A33 B C1  1 
HETATM 2196 C C2  . A1A33 K 4 .  ? 17.507  -16.857 -26.378 0.90 25.86  ? 103 A1A33 B C2  1 
HETATM 2197 C C   . A1A33 K 4 .  ? 16.233  -15.487 -24.677 0.90 29.67  ? 103 A1A33 B C   1 
HETATM 2198 S S   . SO4   L 2 .  ? 29.592  -38.282 12.371  1.00 109.23 ? 101 SO4   C S   1 
HETATM 2199 O O1  . SO4   L 2 .  ? 30.590  -37.627 11.565  1.00 106.93 ? 101 SO4   C O1  1 
HETATM 2200 O O2  . SO4   L 2 .  ? 28.371  -37.527 12.311  1.00 107.00 ? 101 SO4   C O2  1 
HETATM 2201 O O3  . SO4   L 2 .  ? 29.354  -39.610 11.869  1.00 98.23  ? 101 SO4   C O3  1 
HETATM 2202 O O4  . SO4   L 2 .  ? 30.051  -38.357 13.737  1.00 101.42 ? 101 SO4   C O4  1 
HETATM 2203 C C4  . A1A33 M 4 .  ? 17.135  -39.916 18.204  0.64 42.94  ? 102 A1A33 C C4  1 
HETATM 2204 C C5  . A1A33 M 4 .  ? 17.052  -40.032 19.715  0.64 40.83  ? 102 A1A33 C C5  1 
HETATM 2205 C C6  . A1A33 M 4 .  ? 17.890  -38.965 20.383  0.64 41.84  ? 102 A1A33 C C6  1 
HETATM 2206 C C7  . A1A33 M 4 .  ? 17.865  -39.059 21.886  0.64 45.46  ? 102 A1A33 C C7  1 
HETATM 2207 C C8  . A1A33 M 4 .  ? 17.381  -37.592 19.957  0.64 40.23  ? 102 A1A33 C C8  1 
HETATM 2208 O O   . A1A33 M 4 .  ? 17.087  -40.151 22.315  0.64 51.30  ? 102 A1A33 C O   1 
HETATM 2209 C C3  . A1A33 M 4 .  ? 17.871  -38.643 17.851  0.64 41.33  ? 102 A1A33 C C3  1 
HETATM 2210 N N   . A1A33 M 4 .  ? 17.247  -37.480 18.492  0.64 32.19  ? 102 A1A33 C N   1 
HETATM 2211 C C1  . A1A33 M 4 .  ? 17.645  -36.142 18.009  0.64 37.05  ? 102 A1A33 C C1  1 
HETATM 2212 C C2  . A1A33 M 4 .  ? 19.006  -36.094 17.331  0.64 33.09  ? 102 A1A33 C C2  1 
HETATM 2213 C C   . A1A33 M 4 .  ? 16.530  -35.382 17.292  0.64 30.50  ? 102 A1A33 C C   1 
HETATM 2214 O O   . HOH   N 5 .  ? 2.604   -25.326 -10.062 1.00 36.61  ? 201 HOH   A O   1 
HETATM 2215 O O   . HOH   N 5 .  ? -2.355  -30.714 -3.954  1.00 46.92  ? 202 HOH   A O   1 
HETATM 2216 O O   . HOH   N 5 .  ? 6.233   -28.993 6.979   1.00 50.21  ? 203 HOH   A O   1 
HETATM 2217 O O   . HOH   N 5 .  ? 9.385   -32.252 3.996   1.00 57.60  ? 204 HOH   A O   1 
HETATM 2218 O O   . HOH   N 5 .  ? -5.620  -13.454 -16.479 1.00 47.66  ? 205 HOH   A O   1 
HETATM 2219 O O   . HOH   N 5 .  ? 18.772  -11.359 -19.177 1.00 50.09  ? 206 HOH   A O   1 
HETATM 2220 O O   . HOH   N 5 .  ? 11.093  -9.383  -13.419 1.00 53.88  ? 207 HOH   A O   1 
HETATM 2221 O O   . HOH   N 5 .  ? 11.385  -29.834 3.214   1.00 43.94  ? 208 HOH   A O   1 
HETATM 2222 O O   . HOH   N 5 .  ? 13.358  -11.966 8.150   1.00 53.06  ? 209 HOH   A O   1 
HETATM 2223 O O   . HOH   N 5 .  ? 0.715   -10.549 -15.480 1.00 44.28  ? 210 HOH   A O   1 
HETATM 2224 O O   . HOH   N 5 .  ? 9.355   -18.288 -10.846 1.00 33.16  ? 211 HOH   A O   1 
HETATM 2225 O O   . HOH   N 5 .  ? -3.501  -10.674 6.730   1.00 42.03  ? 212 HOH   A O   1 
HETATM 2226 O O   . HOH   N 5 .  ? 16.136  -24.568 1.817   1.00 40.60  ? 213 HOH   A O   1 
HETATM 2227 O O   . HOH   N 5 .  ? 0.233   -33.757 4.969   1.00 63.95  ? 214 HOH   A O   1 
HETATM 2228 O O   . HOH   N 5 .  ? -2.085  3.275   -2.162  1.00 44.28  ? 215 HOH   A O   1 
HETATM 2229 O O   . HOH   N 5 .  ? 7.205   -10.535 -12.060 1.00 37.19  ? 216 HOH   A O   1 
HETATM 2230 O O   . HOH   N 5 .  ? 9.793   -6.048  -1.642  1.00 33.38  ? 217 HOH   A O   1 
HETATM 2231 O O   . HOH   N 5 .  ? 8.514   -17.909 -16.090 1.00 47.55  ? 218 HOH   A O   1 
HETATM 2232 O O   . HOH   N 5 .  ? 11.472  -23.775 9.827   1.00 36.53  ? 219 HOH   A O   1 
HETATM 2233 O O   . HOH   N 5 .  ? 4.642   -3.581  -3.297  1.00 33.15  ? 220 HOH   A O   1 
HETATM 2234 O O   . HOH   N 5 .  ? 14.210  -15.691 -9.225  1.00 35.57  ? 221 HOH   A O   1 
HETATM 2235 O O   . HOH   N 5 .  ? 1.795   -24.782 14.178  1.00 53.56  ? 222 HOH   A O   1 
HETATM 2236 O O   . HOH   N 5 .  ? 4.867   -7.842  1.181   1.00 33.34  ? 223 HOH   A O   1 
HETATM 2237 O O   . HOH   N 5 .  ? -0.388  -20.959 6.963   1.00 34.28  ? 224 HOH   A O   1 
HETATM 2238 O O   . HOH   N 5 .  ? 11.811  -16.495 -14.900 1.00 42.03  ? 225 HOH   A O   1 
HETATM 2239 O O   . HOH   N 5 .  ? 9.665   -22.834 -9.483  1.00 38.10  ? 226 HOH   A O   1 
HETATM 2240 O O   . HOH   N 5 .  ? -7.652  -17.117 6.667   1.00 43.35  ? 227 HOH   A O   1 
HETATM 2241 O O   . HOH   N 5 .  ? -0.303  -29.418 10.277  1.00 50.77  ? 228 HOH   A O   1 
HETATM 2242 O O   . HOH   N 5 .  ? -0.708  -5.617  -7.333  1.00 30.39  ? 229 HOH   A O   1 
HETATM 2243 O O   . HOH   N 5 .  ? -2.402  -11.416 13.762  1.00 55.34  ? 230 HOH   A O   1 
HETATM 2244 O O   . HOH   N 5 .  ? 2.177   -4.670  -10.229 1.00 39.12  ? 231 HOH   A O   1 
HETATM 2245 O O   . HOH   N 5 .  ? 14.574  -29.470 4.090   1.00 40.83  ? 232 HOH   A O   1 
HETATM 2246 O O   . HOH   N 5 .  ? 13.741  -28.011 -4.724  1.00 61.06  ? 233 HOH   A O   1 
HETATM 2247 O O   . HOH   N 5 .  ? 11.159  -5.198  -7.815  1.00 34.08  ? 234 HOH   A O   1 
HETATM 2248 O O   . HOH   N 5 .  ? -11.096 -28.039 2.099   1.00 76.21  ? 235 HOH   A O   1 
HETATM 2249 O O   . HOH   N 5 .  ? 11.813  -11.968 5.975   1.00 33.68  ? 236 HOH   A O   1 
HETATM 2250 O O   . HOH   N 5 .  ? 0.532   -23.209 9.292   1.00 47.28  ? 237 HOH   A O   1 
HETATM 2251 O O   . HOH   N 5 .  ? -5.479  -15.890 -8.025  1.00 29.53  ? 238 HOH   A O   1 
HETATM 2252 O O   . HOH   N 5 .  ? 9.393   -20.207 -18.510 1.00 47.73  ? 239 HOH   A O   1 
HETATM 2253 O O   . HOH   N 5 .  ? 13.532  -12.023 -4.213  1.00 23.54  ? 240 HOH   A O   1 
HETATM 2254 O O   . HOH   N 5 .  ? 9.202   -16.334 -13.090 1.00 36.72  ? 241 HOH   A O   1 
HETATM 2255 O O   . HOH   N 5 .  ? -7.711  -15.741 -0.994  1.00 38.56  ? 242 HOH   A O   1 
HETATM 2256 O O   . HOH   N 5 .  ? -7.605  -16.639 1.749   1.00 43.00  ? 243 HOH   A O   1 
HETATM 2257 O O   . HOH   N 5 .  ? 0.911   -17.609 -18.995 1.00 54.48  ? 244 HOH   A O   1 
HETATM 2258 O O   . HOH   N 5 .  ? 2.750   -6.440  5.535   1.00 37.50  ? 245 HOH   A O   1 
HETATM 2259 O O   . HOH   N 5 .  ? 17.443  -12.893 1.367   1.00 22.11  ? 246 HOH   A O   1 
HETATM 2260 O O   . HOH   N 5 .  ? 15.913  -12.111 -5.269  1.00 33.04  ? 247 HOH   A O   1 
HETATM 2261 O O   . HOH   N 5 .  ? -3.892  -21.275 6.099   1.00 40.66  ? 248 HOH   A O   1 
HETATM 2262 O O   . HOH   N 5 .  ? -5.469  -19.758 -5.677  1.00 37.01  ? 249 HOH   A O   1 
HETATM 2263 O O   . HOH   N 5 .  ? -1.525  -22.071 -0.623  1.00 26.88  ? 250 HOH   A O   1 
HETATM 2264 O O   . HOH   N 5 .  ? -6.905  -21.809 -5.867  1.00 49.77  ? 251 HOH   A O   1 
HETATM 2265 O O   . HOH   N 5 .  ? -0.410  -20.607 11.280  1.00 54.53  ? 252 HOH   A O   1 
HETATM 2266 O O   . HOH   N 5 .  ? 8.362   -17.467 8.626   1.00 41.16  ? 253 HOH   A O   1 
HETATM 2267 O O   . HOH   N 5 .  ? 11.750  -12.428 -6.120  1.00 28.05  ? 254 HOH   A O   1 
HETATM 2268 O O   . HOH   N 5 .  ? -1.299  -7.581  11.430  1.00 44.18  ? 255 HOH   A O   1 
HETATM 2269 O O   . HOH   N 5 .  ? 3.445   -29.645 -0.551  1.00 41.82  ? 256 HOH   A O   1 
HETATM 2270 O O   . HOH   N 5 .  ? 10.391  -13.059 9.574   1.00 41.61  ? 257 HOH   A O   1 
HETATM 2271 O O   . HOH   N 5 .  ? 4.196   -34.854 4.319   1.00 69.46  ? 258 HOH   A O   1 
HETATM 2272 O O   . HOH   N 5 .  ? 12.853  -13.336 -8.680  1.00 44.57  ? 259 HOH   A O   1 
HETATM 2273 O O   . HOH   N 5 .  ? 15.152  -13.351 10.374  1.00 51.38  ? 260 HOH   A O   1 
HETATM 2274 O O   . HOH   N 5 .  ? 11.679  -6.006  -3.911  1.00 52.28  ? 261 HOH   A O   1 
HETATM 2275 O O   . HOH   N 5 .  ? 13.145  -9.448  -7.189  1.00 41.35  ? 262 HOH   A O   1 
HETATM 2276 O O   . HOH   N 5 .  ? -1.237  -11.831 11.297  1.00 36.29  ? 263 HOH   A O   1 
HETATM 2277 O O   . HOH   N 5 .  ? 1.932   -10.492 11.766  1.00 36.98  ? 264 HOH   A O   1 
HETATM 2278 O O   . HOH   N 5 .  ? -6.023  -11.734 -11.277 1.00 38.13  ? 265 HOH   A O   1 
HETATM 2279 O O   . HOH   N 5 .  ? 8.154   -7.837  1.223   1.00 31.75  ? 266 HOH   A O   1 
HETATM 2280 O O   . HOH   N 5 .  ? 16.887  -12.236 -17.087 1.00 42.83  ? 267 HOH   A O   1 
HETATM 2281 O O   . HOH   N 5 .  ? 3.091   -9.877  -13.271 1.00 50.45  ? 268 HOH   A O   1 
HETATM 2282 O O   . HOH   N 5 .  ? -4.234  -25.884 -5.689  1.00 44.01  ? 269 HOH   A O   1 
HETATM 2283 O O   . HOH   N 5 .  ? 6.862   -5.954  0.469   1.00 47.28  ? 270 HOH   A O   1 
HETATM 2284 O O   . HOH   N 5 .  ? 10.532  -27.622 -7.180  1.00 49.91  ? 271 HOH   A O   1 
HETATM 2285 O O   . HOH   N 5 .  ? 5.290   -7.616  3.995   1.00 34.65  ? 272 HOH   A O   1 
HETATM 2286 O O   . HOH   N 5 .  ? -5.762  -26.642 3.311   1.00 51.22  ? 273 HOH   A O   1 
HETATM 2287 O O   . HOH   N 5 .  ? -8.269  -21.190 -1.215  1.00 39.67  ? 274 HOH   A O   1 
HETATM 2288 O O   . HOH   N 5 .  ? -5.983  -12.733 6.757   1.00 37.64  ? 275 HOH   A O   1 
HETATM 2289 O O   . HOH   N 5 .  ? -8.573  -16.182 -12.764 1.00 48.88  ? 276 HOH   A O   1 
HETATM 2290 O O   . HOH   N 5 .  ? 6.366   -16.284 -14.979 1.00 49.88  ? 277 HOH   A O   1 
HETATM 2291 O O   . HOH   N 5 .  ? 17.282  -18.363 -9.572  1.00 50.56  ? 278 HOH   A O   1 
HETATM 2292 O O   . HOH   N 5 .  ? 11.311  -7.886  0.334   1.00 27.65  ? 279 HOH   A O   1 
HETATM 2293 O O   . HOH   N 5 .  ? 21.591  -16.704 -3.499  1.00 33.53  ? 280 HOH   A O   1 
HETATM 2294 O O   . HOH   N 5 .  ? -10.940 -16.233 -3.795  1.00 62.46  ? 281 HOH   A O   1 
HETATM 2295 O O   . HOH   N 5 .  ? -7.044  -11.580 -7.972  1.00 30.27  ? 282 HOH   A O   1 
HETATM 2296 O O   . HOH   N 5 .  ? 13.384  -15.131 -12.391 1.00 50.30  ? 283 HOH   A O   1 
HETATM 2297 O O   . HOH   N 5 .  ? -5.572  -16.620 -15.962 1.00 50.72  ? 284 HOH   A O   1 
HETATM 2298 O O   . HOH   N 5 .  ? -3.758  -26.363 7.715   1.00 61.37  ? 285 HOH   A O   1 
HETATM 2299 O O   . HOH   N 5 .  ? 22.646  -16.658 -0.507  1.00 42.83  ? 286 HOH   A O   1 
HETATM 2300 O O   . HOH   N 5 .  ? 9.467   -2.722  -0.091  1.00 63.89  ? 287 HOH   A O   1 
HETATM 2301 O O   . HOH   N 5 .  ? -7.685  -19.842 -3.469  1.00 56.17  ? 288 HOH   A O   1 
HETATM 2302 O O   . HOH   N 5 .  ? 9.065   -9.265  -13.856 1.00 38.61  ? 289 HOH   A O   1 
HETATM 2303 O O   . HOH   N 5 .  ? -3.659  -7.833  10.526  1.00 44.64  ? 290 HOH   A O   1 
HETATM 2304 O O   . HOH   N 5 .  ? -3.155  -7.485  -10.836 1.00 53.13  ? 291 HOH   A O   1 
HETATM 2305 O O   . HOH   N 5 .  ? -5.460  -23.609 -6.875  1.00 39.06  ? 292 HOH   A O   1 
HETATM 2306 O O   . HOH   N 5 .  ? 3.663   -27.345 -9.326  1.00 48.17  ? 293 HOH   A O   1 
HETATM 2307 O O   . HOH   N 5 .  ? 0.274   -8.098  -13.164 1.00 44.77  ? 294 HOH   A O   1 
HETATM 2308 O O   . HOH   N 5 .  ? -0.437  -3.439  -11.117 1.00 61.74  ? 295 HOH   A O   1 
HETATM 2309 O O   . HOH   N 5 .  ? 12.188  -21.265 10.656  1.00 42.66  ? 296 HOH   A O   1 
HETATM 2310 O O   . HOH   N 5 .  ? 17.122  -10.042 -9.359  1.00 50.38  ? 297 HOH   A O   1 
HETATM 2311 O O   . HOH   N 5 .  ? -7.075  -14.053 -9.205  1.00 40.93  ? 298 HOH   A O   1 
HETATM 2312 O O   . HOH   N 5 .  ? -10.276 -28.090 -1.338  1.00 58.05  ? 299 HOH   A O   1 
HETATM 2313 O O   . HOH   N 5 .  ? 15.503  -28.526 -1.577  1.00 57.52  ? 300 HOH   A O   1 
HETATM 2314 O O   . HOH   N 5 .  ? 11.567  -2.105  -1.399  1.00 50.53  ? 301 HOH   A O   1 
HETATM 2315 O O   . HOH   N 5 .  ? -9.671  -21.532 -6.133  1.00 53.22  ? 302 HOH   A O   1 
HETATM 2316 O O   . HOH   N 5 .  ? -5.747  -23.383 5.731   1.00 51.17  ? 303 HOH   A O   1 
HETATM 2317 O O   . HOH   N 5 .  ? 8.313   -8.204  4.563   1.00 37.65  ? 304 HOH   A O   1 
HETATM 2318 O O   . HOH   N 5 .  ? 4.847   -9.675  -11.339 1.00 45.74  ? 305 HOH   A O   1 
HETATM 2319 O O   . HOH   N 5 .  ? -6.926  -19.263 8.249   1.00 48.36  ? 306 HOH   A O   1 
HETATM 2320 O O   . HOH   N 5 .  ? -11.115 -13.574 -2.985  1.00 44.13  ? 307 HOH   A O   1 
HETATM 2321 O O   . HOH   N 5 .  ? 7.206   -30.899 -2.555  1.00 66.48  ? 308 HOH   A O   1 
HETATM 2322 O O   . HOH   N 5 .  ? -4.895  -20.880 -8.289  1.00 52.52  ? 309 HOH   A O   1 
HETATM 2323 O O   . HOH   N 5 .  ? 4.457   -3.493  2.198   1.00 60.36  ? 310 HOH   A O   1 
HETATM 2324 O O   . HOH   O 5 .  ? 15.394  -3.880  -28.079 1.00 47.06  ? 201 HOH   B O   1 
HETATM 2325 O O   . HOH   O 5 .  ? 20.128  -22.309 -23.599 1.00 45.60  ? 202 HOH   B O   1 
HETATM 2326 O O   . HOH   O 5 .  ? 30.763  -7.996  -30.138 1.00 50.36  ? 203 HOH   B O   1 
HETATM 2327 O O   . HOH   O 5 .  ? 6.812   -12.282 -26.252 1.00 35.23  ? 204 HOH   B O   1 
HETATM 2328 O O   . HOH   O 5 .  ? 10.031  -11.336 -38.278 1.00 44.48  ? 205 HOH   B O   1 
HETATM 2329 O O   . HOH   O 5 .  ? 28.057  -8.141  -29.148 1.00 43.39  ? 206 HOH   B O   1 
HETATM 2330 O O   . HOH   O 5 .  ? 26.086  -4.553  -33.983 1.00 56.31  ? 207 HOH   B O   1 
HETATM 2331 O O   . HOH   O 5 .  ? 25.277  -5.068  -30.114 1.00 43.75  ? 208 HOH   B O   1 
HETATM 2332 O O   . HOH   O 5 .  ? 26.384  -22.904 -31.294 1.00 37.85  ? 209 HOH   B O   1 
HETATM 2333 O O   . HOH   O 5 .  ? 30.529  -19.797 -40.554 1.00 35.08  ? 210 HOH   B O   1 
HETATM 2334 O O   . HOH   O 5 .  ? 18.281  -0.429  -25.599 1.00 54.65  ? 211 HOH   B O   1 
HETATM 2335 O O   . HOH   O 5 .  ? 24.441  -1.648  -36.790 1.00 50.44  ? 212 HOH   B O   1 
HETATM 2336 O O   . HOH   O 5 .  ? 20.279  -2.494  -23.427 1.00 77.01  ? 213 HOH   B O   1 
HETATM 2337 O O   . HOH   O 5 .  ? 21.144  -25.860 -30.275 1.00 67.50  ? 214 HOH   B O   1 
HETATM 2338 O O   . HOH   O 5 .  ? 17.654  -15.260 -20.756 1.00 45.90  ? 215 HOH   B O   1 
HETATM 2339 O O   . HOH   O 5 .  ? 6.208   -7.484  -32.400 1.00 60.94  ? 216 HOH   B O   1 
HETATM 2340 O O   . HOH   O 5 .  ? 10.443  -19.683 -43.262 1.00 51.11  ? 217 HOH   B O   1 
HETATM 2341 O O   . HOH   O 5 .  ? 26.757  -12.967 -45.145 1.00 57.95  ? 218 HOH   B O   1 
HETATM 2342 O O   . HOH   O 5 .  ? 11.391  -8.071  -41.605 1.00 44.96  ? 219 HOH   B O   1 
HETATM 2343 O O   . HOH   O 5 .  ? 21.845  3.537   -32.839 1.00 42.83  ? 220 HOH   B O   1 
HETATM 2344 O O   . HOH   O 5 .  ? 15.104  -17.609 -19.206 1.00 36.72  ? 221 HOH   B O   1 
HETATM 2345 O O   . HOH   O 5 .  ? 12.433  -26.091 -38.062 1.00 59.28  ? 222 HOH   B O   1 
HETATM 2346 O O   . HOH   O 5 .  ? 13.030  -4.577  -42.201 1.00 47.08  ? 223 HOH   B O   1 
HETATM 2347 O O   . HOH   O 5 .  ? 22.918  -23.127 -28.988 1.00 39.99  ? 224 HOH   B O   1 
HETATM 2348 O O   . HOH   O 5 .  ? 16.818  -19.379 -29.022 1.00 24.82  ? 225 HOH   B O   1 
HETATM 2349 O O   . HOH   O 5 .  ? 20.689  -13.345 -43.068 1.00 41.16  ? 226 HOH   B O   1 
HETATM 2350 O O   . HOH   O 5 .  ? 17.685  -19.763 -42.248 1.00 49.18  ? 227 HOH   B O   1 
HETATM 2351 O O   . HOH   O 5 .  ? 25.570  -5.883  -36.091 1.00 44.18  ? 228 HOH   B O   1 
HETATM 2352 O O   . HOH   O 5 .  ? 3.119   -8.832  -27.540 1.00 50.25  ? 229 HOH   B O   1 
HETATM 2353 O O   . HOH   O 5 .  ? 10.359  -16.880 -44.473 1.00 43.61  ? 230 HOH   B O   1 
HETATM 2354 O O   . HOH   O 5 .  ? 18.099  -0.556  -38.722 1.00 31.57  ? 231 HOH   B O   1 
HETATM 2355 O O   . HOH   O 5 .  ? 10.678  -18.853 -33.219 1.00 30.75  ? 232 HOH   B O   1 
HETATM 2356 O O   . HOH   O 5 .  ? 23.662  -2.306  -29.423 1.00 39.70  ? 233 HOH   B O   1 
HETATM 2357 O O   . HOH   O 5 .  ? 7.167   -19.135 -35.253 1.00 49.91  ? 234 HOH   B O   1 
HETATM 2358 O O   . HOH   O 5 .  ? 8.759   -8.756  -16.631 1.00 47.66  ? 235 HOH   B O   1 
HETATM 2359 O O   . HOH   O 5 .  ? 14.280  -6.375  -41.305 1.00 39.52  ? 236 HOH   B O   1 
HETATM 2360 O O   . HOH   O 5 .  ? 34.922  -23.170 -30.185 1.00 55.97  ? 237 HOH   B O   1 
HETATM 2361 O O   . HOH   O 5 .  ? 8.573   -27.746 -38.301 1.00 55.83  ? 238 HOH   B O   1 
HETATM 2362 O O   . HOH   O 5 .  ? 32.713  -18.859 -42.704 1.00 46.31  ? 239 HOH   B O   1 
HETATM 2363 O O   . HOH   O 5 .  ? 15.719  -26.412 -34.792 1.00 52.14  ? 240 HOH   B O   1 
HETATM 2364 O O   . HOH   O 5 .  ? 23.843  -4.158  -37.171 1.00 30.41  ? 241 HOH   B O   1 
HETATM 2365 O O   . HOH   O 5 .  ? 20.510  -10.194 -43.182 1.00 39.69  ? 242 HOH   B O   1 
HETATM 2366 O O   . HOH   O 5 .  ? 28.485  -17.278 -25.162 1.00 44.07  ? 243 HOH   B O   1 
HETATM 2367 O O   . HOH   O 5 .  ? 17.811  -3.678  -22.293 1.00 48.80  ? 244 HOH   B O   1 
HETATM 2368 O O   . HOH   O 5 .  ? 13.600  -22.275 -20.814 1.00 45.35  ? 245 HOH   B O   1 
HETATM 2369 O O   . HOH   O 5 .  ? 7.667   -18.219 -31.892 1.00 45.36  ? 246 HOH   B O   1 
HETATM 2370 O O   . HOH   O 5 .  ? 10.683  -21.763 -32.965 1.00 41.66  ? 247 HOH   B O   1 
HETATM 2371 O O   . HOH   O 5 .  ? 31.743  -12.214 -39.166 1.00 53.53  ? 248 HOH   B O   1 
HETATM 2372 O O   . HOH   O 5 .  ? 14.720  -24.320 -40.604 1.00 40.12  ? 249 HOH   B O   1 
HETATM 2373 O O   . HOH   O 5 .  ? 18.356  -25.892 -29.120 1.00 37.50  ? 250 HOH   B O   1 
HETATM 2374 O O   . HOH   O 5 .  ? 18.064  -15.983 -46.007 1.00 42.36  ? 251 HOH   B O   1 
HETATM 2375 O O   . HOH   O 5 .  ? 7.447   -14.828 -44.386 1.00 61.29  ? 252 HOH   B O   1 
HETATM 2376 O O   . HOH   O 5 .  ? 19.914  -25.464 -34.223 1.00 42.41  ? 253 HOH   B O   1 
HETATM 2377 O O   . HOH   O 5 .  ? 4.807   -19.061 -25.851 1.00 56.41  ? 254 HOH   B O   1 
HETATM 2378 O O   . HOH   O 5 .  ? 1.895   -13.200 -28.401 1.00 44.79  ? 255 HOH   B O   1 
HETATM 2379 O O   . HOH   O 5 .  ? 31.995  -21.158 -38.410 1.00 38.76  ? 256 HOH   B O   1 
HETATM 2380 O O   . HOH   O 5 .  ? 7.593   -8.127  -20.968 1.00 46.05  ? 257 HOH   B O   1 
HETATM 2381 O O   . HOH   O 5 .  ? 22.185  -24.173 -26.694 1.00 41.34  ? 258 HOH   B O   1 
HETATM 2382 O O   . HOH   O 5 .  ? 16.814  -9.590  -44.304 1.00 45.79  ? 259 HOH   B O   1 
HETATM 2383 O O   . HOH   O 5 .  ? 20.198  -7.869  -21.357 1.00 46.53  ? 260 HOH   B O   1 
HETATM 2384 O O   . HOH   O 5 .  ? 23.799  -11.032 -22.196 1.00 37.85  ? 261 HOH   B O   1 
HETATM 2385 O O   . HOH   O 5 .  ? 27.663  -10.663 -29.051 1.00 48.86  ? 262 HOH   B O   1 
HETATM 2386 O O   . HOH   O 5 .  ? 7.621   -12.552 -39.244 1.00 49.94  ? 263 HOH   B O   1 
HETATM 2387 O O   . HOH   O 5 .  ? 24.964  -6.556  -43.015 1.00 47.91  ? 264 HOH   B O   1 
HETATM 2388 O O   . HOH   O 5 .  ? 20.934  -6.468  -42.862 1.00 38.97  ? 265 HOH   B O   1 
HETATM 2389 O O   . HOH   O 5 .  ? 25.260  -8.251  -22.922 1.00 49.83  ? 266 HOH   B O   1 
HETATM 2390 O O   . HOH   O 5 .  ? 6.692   -20.776 -25.165 1.00 42.38  ? 267 HOH   B O   1 
HETATM 2391 O O   . HOH   O 5 .  ? 28.091  -24.729 -35.237 1.00 37.22  ? 268 HOH   B O   1 
HETATM 2392 O O   . HOH   O 5 .  ? 12.335  -4.699  -25.042 1.00 47.75  ? 269 HOH   B O   1 
HETATM 2393 O O   . HOH   O 5 .  ? 26.447  -0.385  -29.562 1.00 51.33  ? 270 HOH   B O   1 
HETATM 2394 O O   . HOH   O 5 .  ? 18.678  -13.204 -44.824 1.00 43.81  ? 271 HOH   B O   1 
HETATM 2395 O O   . HOH   O 5 .  ? 20.490  3.783   -33.163 1.00 38.42  ? 272 HOH   B O   1 
HETATM 2396 O O   . HOH   O 5 .  ? 18.548  4.574   -34.445 1.00 37.89  ? 273 HOH   B O   1 
HETATM 2397 O O   . HOH   O 5 .  ? 16.991  -25.301 -21.142 1.00 72.13  ? 274 HOH   B O   1 
HETATM 2398 O O   . HOH   O 5 .  ? 28.989  -12.131 -27.094 1.00 58.15  ? 275 HOH   B O   1 
HETATM 2399 O O   . HOH   O 5 .  ? 9.657   -6.216  -41.142 1.00 47.36  ? 276 HOH   B O   1 
HETATM 2400 O O   . HOH   O 5 .  ? 16.798  1.942   -30.241 1.00 61.76  ? 277 HOH   B O   1 
HETATM 2401 O O   . HOH   O 5 .  ? 22.289  -23.543 -24.162 1.00 46.54  ? 278 HOH   B O   1 
HETATM 2402 O O   . HOH   O 5 .  ? 13.070  -20.236 -19.693 1.00 51.19  ? 279 HOH   B O   1 
HETATM 2403 O O   . HOH   O 5 .  ? 39.842  -13.770 -38.931 1.00 65.06  ? 280 HOH   B O   1 
HETATM 2404 O O   . HOH   O 5 .  ? 11.521  -24.028 -30.067 1.00 44.73  ? 281 HOH   B O   1 
HETATM 2405 O O   . HOH   O 5 .  ? 15.245  -7.988  -43.306 1.00 44.67  ? 282 HOH   B O   1 
HETATM 2406 O O   . HOH   O 5 .  ? 15.321  -18.581 -16.854 1.00 43.13  ? 283 HOH   B O   1 
HETATM 2407 O O   . HOH   O 5 .  ? 15.165  -21.845 -42.153 1.00 48.38  ? 284 HOH   B O   1 
HETATM 2408 O O   . HOH   O 5 .  ? 24.552  -4.166  -28.112 1.00 55.49  ? 285 HOH   B O   1 
HETATM 2409 O O   . HOH   O 5 .  ? 7.486   -9.948  -18.698 1.00 44.80  ? 286 HOH   B O   1 
HETATM 2410 O O   . HOH   O 5 .  ? 22.860  -29.239 -35.763 1.00 38.77  ? 287 HOH   B O   1 
HETATM 2411 O O   . HOH   P 5 .  ? 26.809  -39.141 12.601  1.00 37.93  ? 201 HOH   C O   1 
HETATM 2412 O O   . HOH   P 5 .  ? 20.708  -20.791 30.601  1.00 82.13  ? 202 HOH   C O   1 
HETATM 2413 O O   . HOH   P 5 .  ? 27.236  -37.793 10.237  1.00 38.89  ? 203 HOH   C O   1 
HETATM 2414 O O   . HOH   P 5 .  ? 8.466   -36.509 18.669  1.00 58.34  ? 204 HOH   C O   1 
HETATM 2415 O O   . HOH   P 5 .  ? 7.914   -31.619 12.342  1.00 48.60  ? 205 HOH   C O   1 
HETATM 2416 O O   . HOH   P 5 .  ? 17.134  -18.049 25.427  1.00 68.16  ? 206 HOH   C O   1 
HETATM 2417 O O   . HOH   P 5 .  ? 17.604  -17.258 15.035  1.00 47.29  ? 207 HOH   C O   1 
HETATM 2418 O O   . HOH   P 5 .  ? 19.454  -20.263 10.631  1.00 37.73  ? 208 HOH   C O   1 
HETATM 2419 O O   . HOH   P 5 .  ? 27.637  -19.507 12.730  1.00 63.26  ? 209 HOH   C O   1 
HETATM 2420 O O   . HOH   P 5 .  ? 12.134  -28.688 28.152  1.00 64.18  ? 210 HOH   C O   1 
HETATM 2421 O O   . HOH   P 5 .  ? 13.024  -31.517 8.356   1.00 31.75  ? 211 HOH   C O   1 
HETATM 2422 O O   . HOH   P 5 .  ? 5.988   -26.436 16.707  1.00 53.24  ? 212 HOH   C O   1 
HETATM 2423 O O   . HOH   P 5 .  ? 25.821  -19.592 6.453   1.00 38.04  ? 213 HOH   C O   1 
HETATM 2424 O O   . HOH   P 5 .  ? 31.922  -33.751 25.972  1.00 51.32  ? 214 HOH   C O   1 
HETATM 2425 O O   . HOH   P 5 .  ? 13.738  -22.745 27.973  1.00 61.70  ? 215 HOH   C O   1 
HETATM 2426 O O   . HOH   P 5 .  ? 20.049  -26.722 3.697   1.00 56.52  ? 216 HOH   C O   1 
HETATM 2427 O O   . HOH   P 5 .  ? 23.340  -41.527 18.488  1.00 39.01  ? 217 HOH   C O   1 
HETATM 2428 O O   . HOH   P 5 .  ? 15.471  -21.080 12.390  1.00 38.16  ? 218 HOH   C O   1 
HETATM 2429 O O   . HOH   P 5 .  ? 16.070  -17.661 19.335  1.00 45.69  ? 219 HOH   C O   1 
HETATM 2430 O O   . HOH   P 5 .  ? 29.994  -39.829 31.588  1.00 38.14  ? 220 HOH   C O   1 
HETATM 2431 O O   . HOH   P 5 .  ? 13.661  -37.501 13.623  1.00 48.71  ? 221 HOH   C O   1 
HETATM 2432 O O   . HOH   P 5 .  ? 25.667  -33.834 34.987  1.00 46.19  ? 222 HOH   C O   1 
HETATM 2433 O O   . HOH   P 5 .  ? 9.344   -18.885 23.802  1.00 50.75  ? 223 HOH   C O   1 
HETATM 2434 O O   . HOH   P 5 .  ? 20.272  -41.987 12.140  1.00 28.99  ? 224 HOH   C O   1 
HETATM 2435 O O   . HOH   P 5 .  ? 25.831  -20.093 30.579  1.00 66.62  ? 225 HOH   C O   1 
HETATM 2436 O O   . HOH   P 5 .  ? 27.922  -37.453 25.279  1.00 50.66  ? 226 HOH   C O   1 
HETATM 2437 O O   . HOH   P 5 .  ? 16.534  -38.233 11.829  1.00 54.53  ? 227 HOH   C O   1 
HETATM 2438 O O   . HOH   P 5 .  ? 30.606  -31.499 15.800  1.00 49.12  ? 228 HOH   C O   1 
HETATM 2439 O O   . HOH   P 5 .  ? 24.029  -20.908 24.014  1.00 44.62  ? 229 HOH   C O   1 
HETATM 2440 O O   . HOH   P 5 .  ? 21.378  -19.420 24.625  1.00 60.93  ? 230 HOH   C O   1 
HETATM 2441 O O   . HOH   P 5 .  ? 26.042  -17.592 13.929  1.00 43.29  ? 231 HOH   C O   1 
HETATM 2442 O O   . HOH   P 5 .  ? 33.484  -24.433 31.760  1.00 46.24  ? 232 HOH   C O   1 
HETATM 2443 O O   . HOH   P 5 .  ? 18.271  -40.719 38.838  1.00 59.41  ? 233 HOH   C O   1 
HETATM 2444 O O   . HOH   P 5 .  ? 25.444  -31.429 10.818  1.00 37.82  ? 234 HOH   C O   1 
HETATM 2445 O O   . HOH   P 5 .  ? 30.808  -28.686 30.540  1.00 48.60  ? 235 HOH   C O   1 
HETATM 2446 O O   . HOH   P 5 .  ? 22.314  -34.469 16.590  1.00 25.16  ? 236 HOH   C O   1 
HETATM 2447 O O   . HOH   P 5 .  ? 22.852  -21.666 7.475   1.00 38.15  ? 237 HOH   C O   1 
HETATM 2448 O O   . HOH   P 5 .  ? 22.458  -28.646 11.134  1.00 33.62  ? 238 HOH   C O   1 
HETATM 2449 O O   . HOH   P 5 .  ? 23.526  -18.620 21.820  1.00 51.53  ? 239 HOH   C O   1 
HETATM 2450 O O   . HOH   P 5 .  ? 30.814  -29.263 12.157  1.00 48.50  ? 240 HOH   C O   1 
HETATM 2451 O O   . HOH   P 5 .  ? 7.039   -18.019 10.810  1.00 42.54  ? 241 HOH   C O   1 
HETATM 2452 O O   . HOH   P 5 .  ? 31.622  -29.516 32.840  1.00 69.54  ? 242 HOH   C O   1 
HETATM 2453 O O   . HOH   P 5 .  ? 20.980  -40.008 26.710  1.00 40.17  ? 243 HOH   C O   1 
HETATM 2454 O O   . HOH   P 5 .  ? 21.135  -28.783 8.516   1.00 36.93  ? 244 HOH   C O   1 
HETATM 2455 O O   . HOH   P 5 .  ? 25.932  -17.776 21.041  1.00 72.29  ? 245 HOH   C O   1 
HETATM 2456 O O   . HOH   P 5 .  ? 28.394  -37.422 16.059  1.00 39.75  ? 246 HOH   C O   1 
HETATM 2457 O O   . HOH   P 5 .  ? 18.021  -21.261 12.886  1.00 51.38  ? 247 HOH   C O   1 
HETATM 2458 O O   . HOH   P 5 .  ? 31.625  -39.810 27.352  1.00 42.39  ? 248 HOH   C O   1 
HETATM 2459 O O   . HOH   P 5 .  ? 28.561  -14.967 12.842  1.00 52.95  ? 249 HOH   C O   1 
HETATM 2460 O O   . HOH   P 5 .  ? 9.884   -30.364 10.034  1.00 33.96  ? 250 HOH   C O   1 
HETATM 2461 O O   . HOH   P 5 .  ? 25.853  -39.821 20.166  1.00 37.71  ? 251 HOH   C O   1 
HETATM 2462 O O   . HOH   P 5 .  ? 30.697  -17.503 9.587   1.00 46.24  ? 252 HOH   C O   1 
HETATM 2463 O O   . HOH   P 5 .  ? 2.914   -28.456 14.509  1.00 53.88  ? 253 HOH   C O   1 
HETATM 2464 O O   . HOH   P 5 .  ? 30.615  -35.711 28.778  1.00 53.15  ? 254 HOH   C O   1 
HETATM 2465 O O   . HOH   P 5 .  ? 14.766  -38.713 9.861   1.00 51.92  ? 255 HOH   C O   1 
HETATM 2466 O O   . HOH   P 5 .  ? 31.547  -43.335 16.011  1.00 60.07  ? 256 HOH   C O   1 
HETATM 2467 O O   . HOH   P 5 .  ? 30.390  -32.677 18.320  1.00 42.93  ? 257 HOH   C O   1 
HETATM 2468 O O   . HOH   P 5 .  ? 32.062  -43.385 11.800  1.00 48.55  ? 258 HOH   C O   1 
HETATM 2469 O O   . HOH   P 5 .  ? 25.368  -21.293 26.646  1.00 60.72  ? 259 HOH   C O   1 
HETATM 2470 O O   . HOH   P 5 .  ? 12.934  -38.814 24.105  1.00 52.21  ? 260 HOH   C O   1 
HETATM 2471 O O   . HOH   P 5 .  ? 21.421  -29.867 4.795   1.00 59.11  ? 261 HOH   C O   1 
HETATM 2472 O O   . HOH   P 5 .  ? 29.950  -25.260 32.540  1.00 54.75  ? 262 HOH   C O   1 
HETATM 2473 O O   . HOH   P 5 .  ? 22.666  -39.931 39.693  1.00 68.84  ? 263 HOH   C O   1 
HETATM 2474 O O   . HOH   P 5 .  ? 27.902  -38.964 24.490  1.00 49.59  ? 264 HOH   C O   1 
HETATM 2475 O O   . HOH   P 5 .  ? 26.083  -14.106 11.104  1.00 49.85  ? 265 HOH   C O   1 
HETATM 2476 O O   . HOH   P 5 .  ? 17.306  -36.565 29.422  1.00 58.70  ? 266 HOH   C O   1 
HETATM 2477 O O   . HOH   P 5 .  ? 21.076  -36.601 40.618  1.00 71.43  ? 267 HOH   C O   1 
HETATM 2478 O O   . HOH   P 5 .  ? 29.327  -41.734 27.400  1.00 41.69  ? 268 HOH   C O   1 
HETATM 2479 O O   . HOH   P 5 .  ? 22.672  -14.009 13.475  1.00 53.36  ? 269 HOH   C O   1 
HETATM 2480 O O   . HOH   P 5 .  ? 7.757   -18.656 25.921  1.00 62.86  ? 270 HOH   C O   1 
HETATM 2481 O O   . HOH   P 5 .  ? 14.505  -39.439 11.950  1.00 48.00  ? 271 HOH   C O   1 
HETATM 2482 O O   . HOH   P 5 .  ? 27.811  -44.768 13.987  1.00 81.45  ? 272 HOH   C O   1 
HETATM 2483 O O   . HOH   P 5 .  ? 14.857  -34.186 35.410  1.00 60.81  ? 273 HOH   C O   1 
HETATM 2484 O O   . HOH   P 5 .  ? 28.572  -41.638 30.027  1.00 44.89  ? 274 HOH   C O   1 
HETATM 2485 O O   . HOH   P 5 .  ? 33.316  -27.971 29.204  1.00 62.48  ? 275 HOH   C O   1 
HETATM 2486 O O   . HOH   P 5 .  ? 4.733   -24.521 18.187  1.00 67.52  ? 276 HOH   C O   1 
HETATM 2487 O O   . HOH   P 5 .  ? 24.653  -29.224 9.554   1.00 49.70  ? 277 HOH   C O   1 
HETATM 2488 O O   . HOH   P 5 .  ? 29.421  -40.537 19.480  1.00 56.73  ? 278 HOH   C O   1 
HETATM 2489 O O   . HOH   P 5 .  ? 33.716  -44.604 15.318  1.00 34.79  ? 279 HOH   C O   1 
HETATM 2490 O O   . HOH   P 5 .  ? 37.701  -24.379 26.680  1.00 67.34  ? 280 HOH   C O   1 
# 
