data_8Z6C
# 
_entry.id   8Z6C 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   8Z6C         pdb_00008z6c 10.2210/pdb8z6c/pdb 
WWPDB D_1300047125 ?            ?                   
# 
_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       2025-04-23 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8Z6C 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-19 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              kruan@ustc.edu.cn 
_pdbx_contact_author.name_first         Ke 
_pdbx_contact_author.name_last          Ruan 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-9358-0451 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Wei, X.'  1 0009-0007-5803-0404 
'Ruan, K.' 2 0000-0001-9358-0451 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Fragment based discovery of small molecule inhibitors of the HDGFRP2 PWWP domain' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Wei, X.'  1 0009-0007-5803-0404 
primary 'Ruan, K.' 2 0000-0001-9358-0451 
# 
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' 10657.184 3   ? ? 'PWWP domain' ? 
2 non-polymer syn '4-(4-bromanyl-1~{H}-pyrazol-3-yl)pyridine'        224.057   3   ? ? ?             ? 
3 non-polymer syn 'SULFATE ION'                                      96.063    5   ? ? ?             ? 
4 water       nat water                                              18.015    153 ? ? ?             ? 
# 
_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       
;MPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKCKDKYGKPNKRKGFNEG
LWEIQNNPHASYS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKCKDKYGKPNKRKGFNEG
LWEIQNNPHASYS
;
_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 '4-(4-bromanyl-1~{H}-pyrazol-3-yl)pyridine' A1D73 
3 'SULFATE ION'                               SO4   
4 water                                       HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1  MET n 
1 2  PRO n 
1 3  HIS n 
1 4  ALA n 
1 5  PHE n 
1 6  LYS n 
1 7  PRO n 
1 8  GLY n 
1 9  ASP n 
1 10 LEU n 
1 11 VAL n 
1 12 PHE n 
1 13 ALA n 
1 14 LYS n 
1 15 MET n 
1 16 LYS n 
1 17 GLY n 
1 18 TYR n 
1 19 PRO n 
1 20 HIS n 
1 21 TRP n 
1 22 PRO n 
1 23 ALA n 
1 24 ARG n 
1 25 ILE n 
1 26 ASP n 
1 27 ASP n 
1 28 ILE n 
1 29 ALA n 
1 30 ASP n 
1 31 GLY n 
1 32 ALA n 
1 33 VAL n 
1 34 LYS n 
1 35 PRO n 
1 36 PRO n 
1 37 PRO n 
1 38 ASN n 
1 39 LYS n 
1 40 TYR n 
1 41 PRO n 
1 42 ILE n 
1 43 PHE n 
1 44 PHE n 
1 45 PHE n 
1 46 GLY n 
1 47 THR n 
1 48 HIS n 
1 49 GLU n 
1 50 THR n 
1 51 ALA n 
1 52 PHE n 
1 53 LEU n 
1 54 GLY n 
1 55 PRO n 
1 56 LYS n 
1 57 ASP n 
1 58 LEU n 
1 59 PHE n 
1 60 PRO n 
1 61 TYR n 
1 62 ASP n 
1 63 LYS n 
1 64 CYS n 
1 65 LYS n 
1 66 ASP n 
1 67 LYS n 
1 68 TYR n 
1 69 GLY n 
1 70 LYS n 
1 71 PRO n 
1 72 ASN n 
1 73 LYS n 
1 74 ARG n 
1 75 LYS n 
1 76 GLY n 
1 77 PHE n 
1 78 ASN n 
1 79 GLU n 
1 80 GLY n 
1 81 LEU n 
1 82 TRP n 
1 83 GLU n 
1 84 ILE n 
1 85 GLN n 
1 86 ASN n 
1 87 ASN n 
1 88 PRO n 
1 89 HIS n 
1 90 ALA n 
1 91 SER n 
1 92 TYR n 
1 93 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                   93 
_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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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          ? 
_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 
A1D73 non-polymer         . '4-(4-bromanyl-1~{H}-pyrazol-3-yl)pyridine' ? 'C8 H6 Br N3'    224.057 
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 
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  MET 1  1  1  MET MET A . n 
A 1 2  PRO 2  2  2  PRO PRO A . n 
A 1 3  HIS 3  3  3  HIS HIS A . n 
A 1 4  ALA 4  4  4  ALA ALA A . n 
A 1 5  PHE 5  5  5  PHE PHE A . n 
A 1 6  LYS 6  6  6  LYS LYS A . n 
A 1 7  PRO 7  7  7  PRO PRO A . n 
A 1 8  GLY 8  8  8  GLY GLY A . n 
A 1 9  ASP 9  9  9  ASP ASP A . n 
A 1 10 LEU 10 10 10 LEU LEU A . n 
A 1 11 VAL 11 11 11 VAL VAL A . n 
A 1 12 PHE 12 12 12 PHE PHE A . n 
A 1 13 ALA 13 13 13 ALA ALA A . n 
A 1 14 LYS 14 14 14 LYS LYS A . n 
A 1 15 MET 15 15 15 MET MET A . n 
A 1 16 LYS 16 16 16 LYS LYS A . n 
A 1 17 GLY 17 17 17 GLY GLY A . n 
A 1 18 TYR 18 18 18 TYR TYR A . n 
A 1 19 PRO 19 19 19 PRO PRO A . n 
A 1 20 HIS 20 20 20 HIS HIS A . n 
A 1 21 TRP 21 21 21 TRP TRP A . n 
A 1 22 PRO 22 22 22 PRO PRO A . n 
A 1 23 ALA 23 23 23 ALA ALA A . n 
A 1 24 ARG 24 24 24 ARG ARG A . n 
A 1 25 ILE 25 25 25 ILE ILE A . n 
A 1 26 ASP 26 26 26 ASP ASP A . n 
A 1 27 ASP 27 27 27 ASP ASP A . n 
A 1 28 ILE 28 28 28 ILE ILE A . n 
A 1 29 ALA 29 29 29 ALA ALA A . n 
A 1 30 ASP 30 30 30 ASP ASP A . n 
A 1 31 GLY 31 31 31 GLY GLY A . n 
A 1 32 ALA 32 32 32 ALA ALA A . n 
A 1 33 VAL 33 33 33 VAL VAL A . n 
A 1 34 LYS 34 34 34 LYS LYS A . n 
A 1 35 PRO 35 35 35 PRO PRO A . n 
A 1 36 PRO 36 36 36 PRO PRO A . n 
A 1 37 PRO 37 37 37 PRO PRO A . n 
A 1 38 ASN 38 38 38 ASN ASN A . n 
A 1 39 LYS 39 39 39 LYS LYS A . n 
A 1 40 TYR 40 40 40 TYR TYR A . n 
A 1 41 PRO 41 41 41 PRO PRO A . n 
A 1 42 ILE 42 42 42 ILE ILE A . n 
A 1 43 PHE 43 43 43 PHE PHE A . n 
A 1 44 PHE 44 44 44 PHE PHE A . n 
A 1 45 PHE 45 45 45 PHE PHE A . n 
A 1 46 GLY 46 46 46 GLY GLY A . n 
A 1 47 THR 47 47 47 THR THR A . n 
A 1 48 HIS 48 48 48 HIS HIS A . n 
A 1 49 GLU 49 49 49 GLU GLU A . n 
A 1 50 THR 50 50 50 THR THR A . n 
A 1 51 ALA 51 51 51 ALA ALA A . n 
A 1 52 PHE 52 52 52 PHE PHE A . n 
A 1 53 LEU 53 53 53 LEU LEU A . n 
A 1 54 GLY 54 54 54 GLY GLY A . n 
A 1 55 PRO 55 55 55 PRO PRO A . n 
A 1 56 LYS 56 56 56 LYS LYS A . n 
A 1 57 ASP 57 57 57 ASP ASP A . n 
A 1 58 LEU 58 58 58 LEU LEU A . n 
A 1 59 PHE 59 59 59 PHE PHE A . n 
A 1 60 PRO 60 60 60 PRO PRO A . n 
A 1 61 TYR 61 61 61 TYR TYR A . n 
A 1 62 ASP 62 62 62 ASP ASP A . n 
A 1 63 LYS 63 63 63 LYS LYS A . n 
A 1 64 CYS 64 64 64 CYS CYS A . n 
A 1 65 LYS 65 65 65 LYS LYS A . n 
A 1 66 ASP 66 66 66 ASP ASP A . n 
A 1 67 LYS 67 67 67 LYS LYS A . n 
A 1 68 TYR 68 68 68 TYR TYR A . n 
A 1 69 GLY 69 69 69 GLY GLY A . n 
A 1 70 LYS 70 70 70 LYS LYS A . n 
A 1 71 PRO 71 71 71 PRO PRO A . n 
A 1 72 ASN 72 72 72 ASN ASN A . n 
A 1 73 LYS 73 73 73 LYS LYS A . n 
A 1 74 ARG 74 74 74 ARG ARG A . n 
A 1 75 LYS 75 75 75 LYS LYS A . n 
A 1 76 GLY 76 76 76 GLY GLY A . n 
A 1 77 PHE 77 77 77 PHE PHE A . n 
A 1 78 ASN 78 78 78 ASN ASN A . n 
A 1 79 GLU 79 79 79 GLU GLU A . n 
A 1 80 GLY 80 80 80 GLY GLY A . n 
A 1 81 LEU 81 81 81 LEU LEU A . n 
A 1 82 TRP 82 82 82 TRP TRP A . n 
A 1 83 GLU 83 83 83 GLU GLU A . n 
A 1 84 ILE 84 84 84 ILE ILE A . n 
A 1 85 GLN 85 85 85 GLN GLN A . n 
A 1 86 ASN 86 86 86 ASN ASN A . n 
A 1 87 ASN 87 87 87 ASN ASN A . n 
A 1 88 PRO 88 88 88 PRO PRO A . n 
A 1 89 HIS 89 89 89 HIS HIS A . n 
A 1 90 ALA 90 90 90 ALA ALA A . n 
A 1 91 SER 91 91 91 SER SER A . n 
A 1 92 TYR 92 92 92 TYR TYR A . n 
A 1 93 SER 93 93 93 SER SER A . n 
B 1 1  MET 1  1  1  MET MET B . n 
B 1 2  PRO 2  2  2  PRO PRO B . n 
B 1 3  HIS 3  3  3  HIS HIS B . n 
B 1 4  ALA 4  4  4  ALA ALA B . n 
B 1 5  PHE 5  5  5  PHE PHE B . n 
B 1 6  LYS 6  6  6  LYS LYS B . n 
B 1 7  PRO 7  7  7  PRO PRO B . n 
B 1 8  GLY 8  8  8  GLY GLY B . n 
B 1 9  ASP 9  9  9  ASP ASP B . n 
B 1 10 LEU 10 10 10 LEU LEU B . n 
B 1 11 VAL 11 11 11 VAL VAL B . n 
B 1 12 PHE 12 12 12 PHE PHE B . n 
B 1 13 ALA 13 13 13 ALA ALA B . n 
B 1 14 LYS 14 14 14 LYS LYS B . n 
B 1 15 MET 15 15 15 MET MET B . n 
B 1 16 LYS 16 16 16 LYS LYS B . n 
B 1 17 GLY 17 17 17 GLY GLY B . n 
B 1 18 TYR 18 18 18 TYR TYR B . n 
B 1 19 PRO 19 19 19 PRO PRO B . n 
B 1 20 HIS 20 20 20 HIS HIS B . n 
B 1 21 TRP 21 21 21 TRP TRP B . n 
B 1 22 PRO 22 22 22 PRO PRO B . n 
B 1 23 ALA 23 23 23 ALA ALA B . n 
B 1 24 ARG 24 24 24 ARG ARG B . n 
B 1 25 ILE 25 25 25 ILE ILE B . n 
B 1 26 ASP 26 26 26 ASP ASP B . n 
B 1 27 ASP 27 27 27 ASP ASP B . n 
B 1 28 ILE 28 28 28 ILE ILE B . n 
B 1 29 ALA 29 29 29 ALA ALA B . n 
B 1 30 ASP 30 30 30 ASP ASP B . n 
B 1 31 GLY 31 31 31 GLY GLY B . n 
B 1 32 ALA 32 32 32 ALA ALA B . n 
B 1 33 VAL 33 33 33 VAL VAL B . n 
B 1 34 LYS 34 34 34 LYS LYS B . n 
B 1 35 PRO 35 35 35 PRO PRO B . n 
B 1 36 PRO 36 36 36 PRO PRO B . n 
B 1 37 PRO 37 37 37 PRO PRO B . n 
B 1 38 ASN 38 38 38 ASN ASN B . n 
B 1 39 LYS 39 39 39 LYS LYS B . n 
B 1 40 TYR 40 40 40 TYR TYR B . n 
B 1 41 PRO 41 41 41 PRO PRO B . n 
B 1 42 ILE 42 42 42 ILE ILE B . n 
B 1 43 PHE 43 43 43 PHE PHE B . n 
B 1 44 PHE 44 44 44 PHE PHE B . n 
B 1 45 PHE 45 45 45 PHE PHE B . n 
B 1 46 GLY 46 46 46 GLY GLY B . n 
B 1 47 THR 47 47 47 THR THR B . n 
B 1 48 HIS 48 48 48 HIS HIS B . n 
B 1 49 GLU 49 49 49 GLU GLU B . n 
B 1 50 THR 50 50 50 THR THR B . n 
B 1 51 ALA 51 51 51 ALA ALA B . n 
B 1 52 PHE 52 52 52 PHE PHE B . n 
B 1 53 LEU 53 53 53 LEU LEU B . n 
B 1 54 GLY 54 54 54 GLY GLY B . n 
B 1 55 PRO 55 55 55 PRO PRO B . n 
B 1 56 LYS 56 56 56 LYS LYS B . n 
B 1 57 ASP 57 57 57 ASP ASP B . n 
B 1 58 LEU 58 58 58 LEU LEU B . n 
B 1 59 PHE 59 59 59 PHE PHE B . n 
B 1 60 PRO 60 60 60 PRO PRO B . n 
B 1 61 TYR 61 61 61 TYR TYR B . n 
B 1 62 ASP 62 62 62 ASP ASP B . n 
B 1 63 LYS 63 63 63 LYS LYS B . n 
B 1 64 CYS 64 64 64 CYS CYS B . n 
B 1 65 LYS 65 65 65 LYS LYS B . n 
B 1 66 ASP 66 66 66 ASP ASP B . n 
B 1 67 LYS 67 67 67 LYS LYS B . n 
B 1 68 TYR 68 68 68 TYR TYR B . n 
B 1 69 GLY 69 69 69 GLY GLY B . n 
B 1 70 LYS 70 70 70 LYS LYS B . n 
B 1 71 PRO 71 71 71 PRO PRO B . n 
B 1 72 ASN 72 72 72 ASN ASN B . n 
B 1 73 LYS 73 73 73 LYS LYS B . n 
B 1 74 ARG 74 74 74 ARG ARG B . n 
B 1 75 LYS 75 75 75 LYS LYS B . n 
B 1 76 GLY 76 76 76 GLY GLY B . n 
B 1 77 PHE 77 77 77 PHE PHE B . n 
B 1 78 ASN 78 78 78 ASN ASN B . n 
B 1 79 GLU 79 79 79 GLU GLU B . n 
B 1 80 GLY 80 80 80 GLY GLY B . n 
B 1 81 LEU 81 81 81 LEU LEU B . n 
B 1 82 TRP 82 82 82 TRP TRP B . n 
B 1 83 GLU 83 83 83 GLU GLU B . n 
B 1 84 ILE 84 84 84 ILE ILE B . n 
B 1 85 GLN 85 85 85 GLN GLN B . n 
B 1 86 ASN 86 86 86 ASN ASN B . n 
B 1 87 ASN 87 87 87 ASN ASN B . n 
B 1 88 PRO 88 88 88 PRO PRO B . n 
B 1 89 HIS 89 89 89 HIS HIS B . n 
B 1 90 ALA 90 90 90 ALA ALA B . n 
B 1 91 SER 91 91 91 SER SER B . n 
B 1 92 TYR 92 92 92 TYR TYR B . n 
B 1 93 SER 93 93 93 SER SER B . n 
C 1 1  MET 1  1  ?  ?   ?   C . n 
C 1 2  PRO 2  2  ?  ?   ?   C . n 
C 1 3  HIS 3  3  3  HIS HIS C . n 
C 1 4  ALA 4  4  4  ALA ALA C . n 
C 1 5  PHE 5  5  5  PHE PHE C . n 
C 1 6  LYS 6  6  6  LYS LYS C . n 
C 1 7  PRO 7  7  7  PRO PRO C . n 
C 1 8  GLY 8  8  8  GLY GLY C . n 
C 1 9  ASP 9  9  9  ASP ASP C . n 
C 1 10 LEU 10 10 10 LEU LEU C . n 
C 1 11 VAL 11 11 11 VAL VAL C . n 
C 1 12 PHE 12 12 12 PHE PHE C . n 
C 1 13 ALA 13 13 13 ALA ALA C . n 
C 1 14 LYS 14 14 14 LYS LYS C . n 
C 1 15 MET 15 15 15 MET MET C . n 
C 1 16 LYS 16 16 16 LYS LYS C . n 
C 1 17 GLY 17 17 17 GLY GLY C . n 
C 1 18 TYR 18 18 18 TYR TYR C . n 
C 1 19 PRO 19 19 19 PRO PRO C . n 
C 1 20 HIS 20 20 20 HIS HIS C . n 
C 1 21 TRP 21 21 21 TRP TRP C . n 
C 1 22 PRO 22 22 22 PRO PRO C . n 
C 1 23 ALA 23 23 23 ALA ALA C . n 
C 1 24 ARG 24 24 24 ARG ARG C . n 
C 1 25 ILE 25 25 25 ILE ILE C . n 
C 1 26 ASP 26 26 26 ASP ASP C . n 
C 1 27 ASP 27 27 27 ASP ASP C . n 
C 1 28 ILE 28 28 28 ILE ILE C . n 
C 1 29 ALA 29 29 29 ALA ALA C . n 
C 1 30 ASP 30 30 30 ASP ASP C . n 
C 1 31 GLY 31 31 31 GLY GLY C . n 
C 1 32 ALA 32 32 32 ALA ALA C . n 
C 1 33 VAL 33 33 33 VAL VAL C . n 
C 1 34 LYS 34 34 34 LYS LYS C . n 
C 1 35 PRO 35 35 35 PRO PRO C . n 
C 1 36 PRO 36 36 36 PRO PRO C . n 
C 1 37 PRO 37 37 37 PRO PRO C . n 
C 1 38 ASN 38 38 38 ASN ASN C . n 
C 1 39 LYS 39 39 39 LYS LYS C . n 
C 1 40 TYR 40 40 40 TYR TYR C . n 
C 1 41 PRO 41 41 41 PRO PRO C . n 
C 1 42 ILE 42 42 42 ILE ILE C . n 
C 1 43 PHE 43 43 43 PHE PHE C . n 
C 1 44 PHE 44 44 44 PHE PHE C . n 
C 1 45 PHE 45 45 45 PHE PHE C . n 
C 1 46 GLY 46 46 46 GLY GLY C . n 
C 1 47 THR 47 47 47 THR THR C . n 
C 1 48 HIS 48 48 48 HIS HIS C . n 
C 1 49 GLU 49 49 49 GLU GLU C . n 
C 1 50 THR 50 50 50 THR THR C . n 
C 1 51 ALA 51 51 51 ALA ALA C . n 
C 1 52 PHE 52 52 52 PHE PHE C . n 
C 1 53 LEU 53 53 53 LEU LEU C . n 
C 1 54 GLY 54 54 54 GLY GLY C . n 
C 1 55 PRO 55 55 55 PRO PRO C . n 
C 1 56 LYS 56 56 56 LYS LYS C . n 
C 1 57 ASP 57 57 57 ASP ASP C . n 
C 1 58 LEU 58 58 58 LEU LEU C . n 
C 1 59 PHE 59 59 59 PHE PHE C . n 
C 1 60 PRO 60 60 60 PRO PRO C . n 
C 1 61 TYR 61 61 61 TYR TYR C . n 
C 1 62 ASP 62 62 62 ASP ASP C . n 
C 1 63 LYS 63 63 63 LYS LYS C . n 
C 1 64 CYS 64 64 64 CYS CYS C . n 
C 1 65 LYS 65 65 65 LYS LYS C . n 
C 1 66 ASP 66 66 66 ASP ASP C . n 
C 1 67 LYS 67 67 67 LYS LYS C . n 
C 1 68 TYR 68 68 68 TYR TYR C . n 
C 1 69 GLY 69 69 69 GLY GLY C . n 
C 1 70 LYS 70 70 70 LYS LYS C . n 
C 1 71 PRO 71 71 71 PRO PRO C . n 
C 1 72 ASN 72 72 72 ASN ASN C . n 
C 1 73 LYS 73 73 73 LYS LYS C . n 
C 1 74 ARG 74 74 74 ARG ARG C . n 
C 1 75 LYS 75 75 75 LYS LYS C . n 
C 1 76 GLY 76 76 76 GLY GLY C . n 
C 1 77 PHE 77 77 77 PHE PHE C . n 
C 1 78 ASN 78 78 78 ASN ASN C . n 
C 1 79 GLU 79 79 79 GLU GLU C . n 
C 1 80 GLY 80 80 80 GLY GLY C . n 
C 1 81 LEU 81 81 81 LEU LEU C . n 
C 1 82 TRP 82 82 82 TRP TRP C . n 
C 1 83 GLU 83 83 83 GLU GLU C . n 
C 1 84 ILE 84 84 84 ILE ILE C . n 
C 1 85 GLN 85 85 85 GLN GLN C . n 
C 1 86 ASN 86 86 86 ASN ASN C . n 
C 1 87 ASN 87 87 87 ASN ASN C . n 
C 1 88 PRO 88 88 88 PRO PRO C . n 
C 1 89 HIS 89 89 89 HIS HIS C . n 
C 1 90 ALA 90 90 90 ALA ALA C . n 
C 1 91 SER 91 91 91 SER SER C . n 
C 1 92 TYR 92 92 92 TYR TYR C . n 
C 1 93 SER 93 93 ?  ?   ?   C . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 A1D73 ? ? A1D73 ? ? 'SUBJECT OF INVESTIGATION' ? 
2 SO4   ? ? SO4   ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 A1D73 1  101 101 A1D73 LIG A . 
E 3 SO4   1  102 2   SO4   SO4 A . 
F 3 SO4   1  103 4   SO4   SO4 A . 
G 2 A1D73 1  101 101 A1D73 LIG B . 
H 3 SO4   1  102 3   SO4   SO4 B . 
I 3 SO4   1  103 5   SO4   SO4 B . 
J 2 A1D73 1  101 101 A1D73 LIG C . 
K 3 SO4   1  102 1   SO4   SO4 C . 
L 4 HOH   1  201 60  HOH   HOH A . 
L 4 HOH   2  202 48  HOH   HOH A . 
L 4 HOH   3  203 10  HOH   HOH A . 
L 4 HOH   4  204 148 HOH   HOH A . 
L 4 HOH   5  205 82  HOH   HOH A . 
L 4 HOH   6  206 24  HOH   HOH A . 
L 4 HOH   7  207 84  HOH   HOH A . 
L 4 HOH   8  208 41  HOH   HOH A . 
L 4 HOH   9  209 70  HOH   HOH A . 
L 4 HOH   10 210 9   HOH   HOH A . 
L 4 HOH   11 211 27  HOH   HOH A . 
L 4 HOH   12 212 156 HOH   HOH A . 
L 4 HOH   13 213 51  HOH   HOH A . 
L 4 HOH   14 214 91  HOH   HOH A . 
L 4 HOH   15 215 38  HOH   HOH A . 
L 4 HOH   16 216 50  HOH   HOH A . 
L 4 HOH   17 217 14  HOH   HOH A . 
L 4 HOH   18 218 67  HOH   HOH A . 
L 4 HOH   19 219 18  HOH   HOH A . 
L 4 HOH   20 220 120 HOH   HOH A . 
L 4 HOH   21 221 54  HOH   HOH A . 
L 4 HOH   22 222 15  HOH   HOH A . 
L 4 HOH   23 223 8   HOH   HOH A . 
L 4 HOH   24 224 30  HOH   HOH A . 
L 4 HOH   25 225 5   HOH   HOH A . 
L 4 HOH   26 226 22  HOH   HOH A . 
L 4 HOH   27 227 85  HOH   HOH A . 
L 4 HOH   28 228 143 HOH   HOH A . 
L 4 HOH   29 229 34  HOH   HOH A . 
L 4 HOH   30 230 56  HOH   HOH A . 
L 4 HOH   31 231 23  HOH   HOH A . 
L 4 HOH   32 232 94  HOH   HOH A . 
L 4 HOH   33 233 3   HOH   HOH A . 
L 4 HOH   34 234 105 HOH   HOH A . 
L 4 HOH   35 235 28  HOH   HOH A . 
L 4 HOH   36 236 76  HOH   HOH A . 
L 4 HOH   37 237 128 HOH   HOH A . 
L 4 HOH   38 238 2   HOH   HOH A . 
L 4 HOH   39 239 19  HOH   HOH A . 
L 4 HOH   40 240 46  HOH   HOH A . 
L 4 HOH   41 241 131 HOH   HOH A . 
L 4 HOH   42 242 42  HOH   HOH A . 
L 4 HOH   43 243 53  HOH   HOH A . 
L 4 HOH   44 244 37  HOH   HOH A . 
L 4 HOH   45 245 74  HOH   HOH A . 
L 4 HOH   46 246 167 HOH   HOH A . 
L 4 HOH   47 247 125 HOH   HOH A . 
L 4 HOH   48 248 20  HOH   HOH A . 
L 4 HOH   49 249 13  HOH   HOH A . 
L 4 HOH   50 250 16  HOH   HOH A . 
L 4 HOH   51 251 122 HOH   HOH A . 
L 4 HOH   52 252 182 HOH   HOH A . 
L 4 HOH   53 253 183 HOH   HOH A . 
L 4 HOH   54 254 172 HOH   HOH A . 
L 4 HOH   55 255 49  HOH   HOH A . 
L 4 HOH   56 256 181 HOH   HOH A . 
L 4 HOH   57 257 86  HOH   HOH A . 
L 4 HOH   58 258 176 HOH   HOH A . 
L 4 HOH   59 259 110 HOH   HOH A . 
L 4 HOH   60 260 135 HOH   HOH A . 
L 4 HOH   61 261 112 HOH   HOH A . 
L 4 HOH   62 262 133 HOH   HOH A . 
L 4 HOH   63 263 132 HOH   HOH A . 
L 4 HOH   64 264 69  HOH   HOH A . 
L 4 HOH   65 265 90  HOH   HOH A . 
M 4 HOH   1  201 77  HOH   HOH B . 
M 4 HOH   2  202 65  HOH   HOH B . 
M 4 HOH   3  203 12  HOH   HOH B . 
M 4 HOH   4  204 180 HOH   HOH B . 
M 4 HOH   5  205 144 HOH   HOH B . 
M 4 HOH   6  206 75  HOH   HOH B . 
M 4 HOH   7  207 31  HOH   HOH B . 
M 4 HOH   8  208 83  HOH   HOH B . 
M 4 HOH   9  209 21  HOH   HOH B . 
M 4 HOH   10 210 179 HOH   HOH B . 
M 4 HOH   11 211 6   HOH   HOH B . 
M 4 HOH   12 212 126 HOH   HOH B . 
M 4 HOH   13 213 121 HOH   HOH B . 
M 4 HOH   14 214 1   HOH   HOH B . 
M 4 HOH   15 215 93  HOH   HOH B . 
M 4 HOH   16 216 45  HOH   HOH B . 
M 4 HOH   17 217 97  HOH   HOH B . 
M 4 HOH   18 218 104 HOH   HOH B . 
M 4 HOH   19 219 118 HOH   HOH B . 
M 4 HOH   20 220 73  HOH   HOH B . 
M 4 HOH   21 221 57  HOH   HOH B . 
M 4 HOH   22 222 174 HOH   HOH B . 
M 4 HOH   23 223 119 HOH   HOH B . 
M 4 HOH   24 224 80  HOH   HOH B . 
M 4 HOH   25 225 151 HOH   HOH B . 
M 4 HOH   26 226 11  HOH   HOH B . 
M 4 HOH   27 227 173 HOH   HOH B . 
M 4 HOH   28 228 72  HOH   HOH B . 
M 4 HOH   29 229 162 HOH   HOH B . 
M 4 HOH   30 230 150 HOH   HOH B . 
M 4 HOH   31 231 78  HOH   HOH B . 
M 4 HOH   32 232 43  HOH   HOH B . 
M 4 HOH   33 233 171 HOH   HOH B . 
M 4 HOH   34 234 44  HOH   HOH B . 
M 4 HOH   35 235 32  HOH   HOH B . 
M 4 HOH   36 236 175 HOH   HOH B . 
M 4 HOH   37 237 154 HOH   HOH B . 
M 4 HOH   38 238 155 HOH   HOH B . 
M 4 HOH   39 239 40  HOH   HOH B . 
M 4 HOH   40 240 59  HOH   HOH B . 
M 4 HOH   41 241 71  HOH   HOH B . 
M 4 HOH   42 242 157 HOH   HOH B . 
M 4 HOH   43 243 163 HOH   HOH B . 
M 4 HOH   44 244 102 HOH   HOH B . 
M 4 HOH   45 245 113 HOH   HOH B . 
M 4 HOH   46 246 109 HOH   HOH B . 
M 4 HOH   47 247 178 HOH   HOH B . 
M 4 HOH   48 248 81  HOH   HOH B . 
M 4 HOH   49 249 64  HOH   HOH B . 
M 4 HOH   50 250 168 HOH   HOH B . 
M 4 HOH   51 251 127 HOH   HOH B . 
M 4 HOH   52 252 115 HOH   HOH B . 
N 4 HOH   1  201 26  HOH   HOH C . 
N 4 HOH   2  202 58  HOH   HOH C . 
N 4 HOH   3  203 35  HOH   HOH C . 
N 4 HOH   4  204 160 HOH   HOH C . 
N 4 HOH   5  205 146 HOH   HOH C . 
N 4 HOH   6  206 165 HOH   HOH C . 
N 4 HOH   7  207 79  HOH   HOH C . 
N 4 HOH   8  208 177 HOH   HOH C . 
N 4 HOH   9  209 66  HOH   HOH C . 
N 4 HOH   10 210 29  HOH   HOH C . 
N 4 HOH   11 211 100 HOH   HOH C . 
N 4 HOH   12 212 33  HOH   HOH C . 
N 4 HOH   13 213 4   HOH   HOH C . 
N 4 HOH   14 214 52  HOH   HOH C . 
N 4 HOH   15 215 7   HOH   HOH C . 
N 4 HOH   16 216 89  HOH   HOH C . 
N 4 HOH   17 217 62  HOH   HOH C . 
N 4 HOH   18 218 116 HOH   HOH C . 
N 4 HOH   19 219 36  HOH   HOH C . 
N 4 HOH   20 220 139 HOH   HOH C . 
N 4 HOH   21 221 111 HOH   HOH C . 
N 4 HOH   22 222 61  HOH   HOH C . 
N 4 HOH   23 223 25  HOH   HOH C . 
N 4 HOH   24 224 123 HOH   HOH C . 
N 4 HOH   25 225 63  HOH   HOH C . 
N 4 HOH   26 226 87  HOH   HOH C . 
N 4 HOH   27 227 107 HOH   HOH C . 
N 4 HOH   28 228 47  HOH   HOH C . 
N 4 HOH   29 229 55  HOH   HOH C . 
N 4 HOH   30 230 124 HOH   HOH C . 
N 4 HOH   31 231 117 HOH   HOH C . 
N 4 HOH   32 232 152 HOH   HOH C . 
N 4 HOH   33 233 39  HOH   HOH C . 
N 4 HOH   34 234 103 HOH   HOH C . 
N 4 HOH   35 235 114 HOH   HOH C . 
N 4 HOH   36 236 130 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 MET 1  ? CG  ? A MET 1  CG  
2  1 Y 1 A MET 1  ? SD  ? A MET 1  SD  
3  1 Y 1 A MET 1  ? CE  ? A MET 1  CE  
4  1 Y 1 A LYS 73 ? CG  ? A LYS 73 CG  
5  1 Y 1 A LYS 73 ? CD  ? A LYS 73 CD  
6  1 Y 1 A LYS 73 ? CE  ? A LYS 73 CE  
7  1 Y 1 A LYS 73 ? NZ  ? A LYS 73 NZ  
8  1 Y 1 A LYS 75 ? CD  ? A LYS 75 CD  
9  1 Y 1 A LYS 75 ? CE  ? A LYS 75 CE  
10 1 Y 1 A LYS 75 ? NZ  ? A LYS 75 NZ  
11 1 Y 1 B MET 1  ? CG  ? B MET 1  CG  
12 1 Y 1 B MET 1  ? SD  ? B MET 1  SD  
13 1 Y 1 B MET 1  ? CE  ? B MET 1  CE  
14 1 Y 1 B ASP 30 ? CG  ? B ASP 30 CG  
15 1 Y 1 B ASP 30 ? OD1 ? B ASP 30 OD1 
16 1 Y 1 B ASP 30 ? OD2 ? B ASP 30 OD2 
17 1 Y 1 B LYS 34 ? CG  ? B LYS 34 CG  
18 1 Y 1 B LYS 34 ? CD  ? B LYS 34 CD  
19 1 Y 1 B LYS 34 ? CE  ? B LYS 34 CE  
20 1 Y 1 B LYS 34 ? NZ  ? B LYS 34 NZ  
21 1 Y 1 B LYS 73 ? CG  ? B LYS 73 CG  
22 1 Y 1 B LYS 73 ? CD  ? B LYS 73 CD  
23 1 Y 1 B LYS 73 ? CE  ? B LYS 73 CE  
24 1 Y 1 B LYS 73 ? NZ  ? B LYS 73 NZ  
25 1 Y 1 B GLU 79 ? CG  ? B GLU 79 CG  
26 1 Y 1 B GLU 79 ? CD  ? B GLU 79 CD  
27 1 Y 1 B GLU 79 ? OE1 ? B GLU 79 OE1 
28 1 Y 1 B GLU 79 ? OE2 ? B GLU 79 OE2 
29 1 Y 1 B GLN 85 ? CG  ? B GLN 85 CG  
30 1 Y 1 B GLN 85 ? CD  ? B GLN 85 CD  
31 1 Y 1 B GLN 85 ? OE1 ? B GLN 85 OE1 
32 1 Y 1 B GLN 85 ? NE2 ? B GLN 85 NE2 
33 1 Y 1 C HIS 3  ? CG  ? C HIS 3  CG  
34 1 Y 1 C HIS 3  ? ND1 ? C HIS 3  ND1 
35 1 Y 1 C HIS 3  ? CD2 ? C HIS 3  CD2 
36 1 Y 1 C HIS 3  ? CE1 ? C HIS 3  CE1 
37 1 Y 1 C HIS 3  ? NE2 ? C HIS 3  NE2 
38 1 Y 1 C ASP 27 ? CG  ? C ASP 27 CG  
39 1 Y 1 C ASP 27 ? OD1 ? C ASP 27 OD1 
40 1 Y 1 C ASP 27 ? OD2 ? C ASP 27 OD2 
41 1 Y 1 C ASP 30 ? CG  ? C ASP 30 CG  
42 1 Y 1 C ASP 30 ? OD1 ? C ASP 30 OD1 
43 1 Y 1 C ASP 30 ? OD2 ? C ASP 30 OD2 
44 1 Y 1 C LYS 34 ? CG  ? C LYS 34 CG  
45 1 Y 1 C LYS 34 ? CD  ? C LYS 34 CD  
46 1 Y 1 C LYS 34 ? CE  ? C LYS 34 CE  
47 1 Y 1 C LYS 34 ? NZ  ? C LYS 34 NZ  
48 1 Y 1 C LYS 56 ? CG  ? C LYS 56 CG  
49 1 Y 1 C LYS 56 ? CD  ? C LYS 56 CD  
50 1 Y 1 C LYS 56 ? CE  ? C LYS 56 CE  
51 1 Y 1 C LYS 56 ? NZ  ? C LYS 56 NZ  
52 1 Y 1 C LYS 67 ? CG  ? C LYS 67 CG  
53 1 Y 1 C LYS 67 ? CD  ? C LYS 67 CD  
54 1 Y 1 C LYS 67 ? CE  ? C LYS 67 CE  
55 1 Y 1 C LYS 67 ? NZ  ? C LYS 67 NZ  
56 1 Y 1 C LYS 73 ? CD  ? C LYS 73 CD  
57 1 Y 1 C LYS 73 ? CE  ? C LYS 73 CE  
58 1 Y 1 C LYS 73 ? NZ  ? C LYS 73 NZ  
59 1 Y 1 C LYS 75 ? CD  ? C LYS 75 CD  
60 1 Y 1 C LYS 75 ? CE  ? C LYS 75 CE  
61 1 Y 1 C LYS 75 ? NZ  ? C LYS 75 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? 1.19           1 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? 'Jun 30, 2023' 2 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless     ? ? ? .              3 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .              4 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? .              5 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8Z6C 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.140 
_cell.length_a_esd                 ? 
_cell.length_b                     42.371 
_cell.length_b_esd                 ? 
_cell.length_c                     159.201 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        12 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8Z6C 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8Z6C 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.22 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          44.66 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
'0.01 M magnesium sulfate heptahydrate, 0.05 M sodium cacodylate trihydrate (pH 6.5), 2 M ammonium sulfate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            278 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-07-20 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97853 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL18U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97853 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL18U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8Z6C 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.93 
_reflns.d_resolution_low                               42.37 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     21227 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           95.1 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.2 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.115 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.93 
_reflns_shell.d_res_low                                     1.98 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.9 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1428 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.898 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.906 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8Z6C 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.93 
_refine.ls_d_res_low                             37.40 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     21126 
_refine.ls_number_reflns_R_free                  1003 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    94.99 
_refine.ls_percent_reflns_R_free                 4.75 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1912 
_refine.ls_R_factor_R_free                       0.2358 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1890 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 23.11 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.22 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2183 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         61 
_refine_hist.number_atoms_solvent             153 
_refine_hist.number_atoms_total               2397 
_refine_hist.d_res_high                       1.93 
_refine_hist.d_res_low                        37.40 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.008 ? 2336 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.939 ? 3180 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 7.172 ? 297  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.058 ? 288  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.009 ? 419  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.93 2.03  . . 150 2893 99.00  . . . . 0.2256 . . . . . . . . . . . 0.2744 
'X-RAY DIFFRACTION' 2.03 2.16  . . 145 2959 100.00 . . . . 0.1924 . . . . . . . . . . . 0.2519 
'X-RAY DIFFRACTION' 2.16 2.33  . . 79  1985 66.00  . . . . 0.2187 . . . . . . . . . . . 0.2802 
'X-RAY DIFFRACTION' 2.33 2.56  . . 190 2950 100.00 . . . . 0.2124 . . . . . . . . . . . 0.2793 
'X-RAY DIFFRACTION' 2.56 2.93  . . 134 3043 100.00 . . . . 0.2148 . . . . . . . . . . . 0.2603 
'X-RAY DIFFRACTION' 2.93 3.69  . . 150 3072 100.00 . . . . 0.1829 . . . . . . . . . . . 0.2399 
'X-RAY DIFFRACTION' 3.69 37.40 . . 155 3221 100.00 . . . . 0.1661 . . . . . . . . . . . 0.1909 
# 
_struct.entry_id                     8Z6C 
_struct.title                        
'Crystal structure of HDGFRP2 PWWP domain in complex with 4-(4-bromo-1H-pyrazol-3-yl) pyridine' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        8Z6C 
_struct_keywords.text            'Hepatoma-derived growth factor-related protein 2, PWWP domain, hit, SIGNALING PROTEIN' 
_struct_keywords.pdbx_keywords   'SIGNALING PROTEIN' 
# 
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 3 ? 
F N N 3 ? 
G N N 2 ? 
H N N 3 ? 
I N N 3 ? 
J N N 2 ? 
K N N 3 ? 
L N N 4 ? 
M N N 4 ? 
N N N 4 ? 
# 
_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 8Z6C A 1 ? 93 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 8Z6C B 1 ? 93 ? Q7Z4V5 1 ? 93 ? 1 93 
3 1 8Z6C C 1 ? 93 ? Q7Z4V5 1 ? 93 ? 1 93 
# 
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,L 
2 1 B,G,H,I,M 
3 1 C,J,K,N   
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_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 54 ? LYS A 56 ? GLY A 54 LYS A 56 5 ? 3  
HELX_P HELX_P2 AA2 TYR A 61 ? GLY A 69 ? TYR A 61 GLY A 69 1 ? 9  
HELX_P HELX_P3 AA3 GLY A 76 ? ASN A 87 ? GLY A 76 ASN A 87 1 ? 12 
HELX_P HELX_P4 AA4 GLY B 54 ? LYS B 56 ? GLY B 54 LYS B 56 5 ? 3  
HELX_P HELX_P5 AA5 TYR B 61 ? GLY B 69 ? TYR B 61 GLY B 69 1 ? 9  
HELX_P HELX_P6 AA6 GLY B 76 ? ASN B 87 ? GLY B 76 ASN B 87 1 ? 12 
HELX_P HELX_P7 AA7 GLY C 54 ? LYS C 56 ? GLY C 54 LYS C 56 5 ? 3  
HELX_P HELX_P8 AA8 TYR C 61 ? GLY C 69 ? TYR C 61 GLY C 69 1 ? 9  
HELX_P HELX_P9 AA9 GLY C 76 ? ASN C 87 ? 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 50 ? LEU A 53 ? THR A 50 LEU A 53 
AA1 2 TYR A 40 ? PHE A 44 ? TYR A 40 PHE A 44 
AA1 3 TRP A 21 ? ILE A 25 ? TRP A 21 ILE A 25 
AA1 4 LEU A 10 ? ALA A 13 ? LEU A 10 ALA A 13 
AA1 5 LEU A 58 ? PRO A 60 ? LEU A 58 PRO A 60 
AA2 1 THR B 50 ? LEU B 53 ? THR B 50 LEU B 53 
AA2 2 TYR B 40 ? PHE B 44 ? TYR B 40 PHE B 44 
AA2 3 TRP B 21 ? ILE B 25 ? TRP B 21 ILE B 25 
AA2 4 LEU B 10 ? ALA B 13 ? LEU B 10 ALA B 13 
AA2 5 LEU B 58 ? PRO B 60 ? LEU B 58 PRO B 60 
AA3 1 THR C 50 ? LEU C 53 ? THR C 50 LEU C 53 
AA3 2 TYR C 40 ? PHE C 44 ? TYR C 40 PHE C 44 
AA3 3 TRP C 21 ? ILE C 25 ? TRP C 21 ILE C 25 
AA3 4 LEU C 10 ? ALA C 13 ? LEU C 10 ALA C 13 
AA3 5 LEU C 58 ? PRO C 60 ? 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 51 ? O ALA A 51 N ILE A 42 ? N ILE A 42 
AA1 2 3 O PHE A 43 ? O PHE A 43 N ARG A 24 ? N ARG A 24 
AA1 3 4 O ALA A 23 ? O ALA A 23 N VAL A 11 ? N VAL A 11 
AA1 4 5 N PHE A 12 ? N PHE A 12 O PHE A 59 ? O PHE A 59 
AA2 1 2 O ALA B 51 ? O ALA B 51 N ILE B 42 ? N ILE B 42 
AA2 2 3 O PHE B 43 ? O PHE B 43 N ARG B 24 ? N ARG B 24 
AA2 3 4 O ALA B 23 ? O ALA B 23 N VAL B 11 ? N VAL B 11 
AA2 4 5 N PHE B 12 ? N PHE B 12 O PHE B 59 ? O PHE B 59 
AA3 1 2 O ALA C 51 ? O ALA C 51 N ILE C 42 ? N ILE C 42 
AA3 2 3 O PHE C 43 ? O PHE C 43 N ARG C 24 ? N ARG C 24 
AA3 3 4 O ALA C 23 ? O ALA C 23 N VAL C 11 ? N VAL C 11 
AA3 4 5 N PHE C 12 ? N PHE C 12 O PHE C 59 ? O PHE C 59 
# 
_pdbx_entry_details.entry_id                   8Z6C 
_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_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 ? ? -158.39 64.80 
2 1 ASN B 87 ? ? -158.99 64.96 
3 1 ASN C 87 ? ? -163.09 55.05 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1  'X-RAY DIFFRACTION' ? refined 18.6235  6.7711   1.4579  0.0835 ? 0.0165  ? -0.0109 ? 0.1756 ? -0.0031 ? 0.1444 ? 5.7844 ? 
0.3828  ? -1.2324 ? 1.6999 ? 1.4239  ? 3.5361 ? 0.0103  ? -0.0947 ? 0.1576  ? 0.0078  ? 0.1141  ? -0.1832 ? 0.0090  ? 0.1443  ? 
-0.0940 ? 
2  'X-RAY DIFFRACTION' ? refined 15.0581  7.8356   16.1344 0.3263 ? 0.0098  ? 0.0291  ? 0.3717 ? 0.0029  ? 0.2119 ? 8.6940 ? 
0.7485  ? -5.3634 ? 3.5744 ? -0.3586 ? 7.9438 ? 0.1843  ? -0.4774 ? 0.1773  ? 0.4479  ? 0.0435  ? 0.0166  ? -0.2173 ? 0.0511  ? 
-0.1896 ? 
3  'X-RAY DIFFRACTION' ? refined 18.3464  3.2991   -0.6861 0.1007 ? 0.0466  ? -0.0171 ? 0.1467 ? -0.0087 ? 0.1691 ? 5.3969 ? 
1.6487  ? 0.9553  ? 4.1378 ? 1.2798  ? 3.8958 ? 0.1652  ? 0.2816  ? -0.1859 ? -0.0411 ? 0.0676  ? -0.2670 ? 0.1988  ? 0.1877  ? 
-0.2382 ? 
4  'X-RAY DIFFRACTION' ? refined 7.3491   1.5956   -3.0191 0.1192 ? -0.0223 ? -0.0476 ? 0.1263 ? 0.0080  ? 0.2027 ? 7.7239 ? 
-2.8881 ? -0.6277 ? 8.2901 ? 3.8215  ? 3.9593 ? 0.1724  ? -0.1055 ? -0.4524 ? -0.0163 ? 0.0043  ? 0.5101  ? 0.1818  ? -0.1243 ? 
-0.0983 ? 
5  'X-RAY DIFFRACTION' ? refined -0.7578  5.8135   34.9313 0.2918 ? 0.0235  ? 0.0877  ? 0.2031 ? 0.0054  ? 0.2296 ? 5.0491 ? 
-0.7811 ? -0.3630 ? 4.6832 ? -0.7537 ? 4.0687 ? -0.0737 ? 0.1498  ? -0.2660 ? 0.1030  ? 0.0842  ? 0.4977  ? -0.0836 ? -0.4867 ? 
0.0105  ? 
6  'X-RAY DIFFRACTION' ? refined -13.6805 9.7719   31.4335 0.3697 ? 0.0644  ? -0.0006 ? 0.9153 ? 0.3405  ? 0.7915 ? 3.3755 ? 
-0.6334 ? 5.2710  ? 0.1371 ? -0.8829 ? 8.5232 ? -0.1745 ? -0.0873 ? 0.5748  ? -0.0055 ? 1.1422  ? 2.0352  ? -0.1205 ? -1.5753 ? 
-0.6697 ? 
7  'X-RAY DIFFRACTION' ? refined 0.7929   5.4689   34.4127 0.3124 ? 0.0291  ? 0.0547  ? 0.1984 ? -0.0345 ? 0.1758 ? 4.9834 ? 
0.2700  ? -1.0152 ? 5.4749 ? -1.0862 ? 1.6120 ? -0.0322 ? -0.0465 ? 0.0387  ? 0.1263  ? 0.1578  ? -0.1772 ? -0.0313 ? -0.0738 ? 
-0.0764 ? 
8  'X-RAY DIFFRACTION' ? refined 8.4592   13.5057  31.3685 0.3268 ? -0.0273 ? 0.1036  ? 0.2287 ? 0.0231  ? 0.2385 ? 3.6920 ? 
0.1049  ? -1.5725 ? 2.6759 ? 2.1429  ? 5.4156 ? 0.1387  ? 0.2268  ? 0.3964  ? -0.6272 ? 0.0106  ? -0.4336 ? -0.6757 ? 0.2874  ? 
-0.1280 ? 
9  'X-RAY DIFFRACTION' ? refined 19.6053  -13.0801 21.3082 0.3577 ? 0.0938  ? 0.0886  ? 0.3256 ? -0.0004 ? 0.2658 ? 6.0211 ? 
0.6972  ? -1.4269 ? 3.2640 ? 0.9189  ? 5.0340 ? -0.7148 ? -0.5020 ? -0.3563 ? 0.6941  ? 0.3579  ? 0.3045  ? 0.1293  ? -0.3729 ? 
0.3029  ? 
10 'X-RAY DIFFRACTION' ? refined 21.4137  -7.1299  35.5652 0.7308 ? 0.0222  ? 0.0297  ? 0.9420 ? 0.0494  ? 0.5101 ? 2.5662 ? 
-1.4729 ? -1.9907 ? 2.3692 ? 2.2532  ? 2.5281 ? 0.0527  ? -0.1744 ? -0.2623 ? 1.0420  ? -0.4248 ? -0.0894 ? 0.4373  ? 1.1858  ? 
0.1163  ? 
11 'X-RAY DIFFRACTION' ? refined 19.7758  -13.3483 21.3761 0.3213 ? 0.0614  ? 0.0614  ? 0.2992 ? 0.0422  ? 0.2925 ? 8.1342 ? 
-1.1677 ? -3.3903 ? 3.9588 ? 2.3211  ? 6.7115 ? -0.4894 ? -0.5252 ? -0.3448 ? 0.3246  ? 0.3870  ? 0.3548  ? 0.5549  ? 0.0184  ? 
0.0777  ? 
12 'X-RAY DIFFRACTION' ? refined 27.6861  -15.7326 12.1456 0.2415 ? 0.0104  ? 0.0893  ? 0.2430 ? -0.0136 ? 0.2287 ? 5.7162 ? 
-0.4910 ? -2.4276 ? 5.8409 ? 2.3614  ? 8.1432 ? -0.2982 ? -0.1811 ? -0.1079 ? 0.0715  ? 0.4008  ? -0.4043 ? -0.1712 ? 0.2678  ? 
-0.0991 ? 
13 'X-RAY DIFFRACTION' ? refined 31.9260  -19.6507 24.2701 0.7320 ? 0.3909  ? -0.0804 ? 0.6742 ? -0.0036 ? 0.4974 ? 7.3250 ? 
1.5940  ? -2.0069 ? 3.4369 ? -0.8786 ? 8.8224 ? -1.4066 ? -1.8538 ? 0.1890  ? 1.3015  ? 0.6119  ? -0.6745 ? 0.5183  ? 0.8908  ? 
0.5913  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 1 through 25 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 26 through 39 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 40 through 76 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 77 through 93 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 1 through 25 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 26 through 38 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 39 through 68 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 69 through 93 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 3 through 25 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 26 through 38 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 39 through 68 )
;
12 'X-RAY DIFFRACTION' 12 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 69 through 86 )
;
13 'X-RAY DIFFRACTION' 13 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 87 through 92 )
;
# 
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 C MET 1  ? C MET 1  
2 1 Y 1 C PRO 2  ? C PRO 2  
3 1 Y 1 C SER 93 ? C SER 93 
# 
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 
A1D73 C01  C  Y N 1   
A1D73 C02  C  Y N 2   
A1D73 C04  C  Y N 3   
A1D73 C05  C  Y N 4   
A1D73 C06  C  Y N 5   
A1D73 C07  C  Y N 6   
A1D73 C08  C  Y N 7   
A1D73 C09  C  Y N 8   
A1D73 N03  N  Y N 9   
A1D73 N10  N  Y N 10  
A1D73 N11  N  Y N 11  
A1D73 BR12 BR N N 12  
A1D73 H1   H  N N 13  
A1D73 H2   H  N N 14  
A1D73 H3   H  N N 15  
A1D73 H4   H  N N 16  
A1D73 H5   H  N N 17  
A1D73 H6   H  N N 18  
ALA   N    N  N N 19  
ALA   CA   C  N S 20  
ALA   C    C  N N 21  
ALA   O    O  N N 22  
ALA   CB   C  N N 23  
ALA   OXT  O  N N 24  
ALA   H    H  N N 25  
ALA   H2   H  N N 26  
ALA   HA   H  N N 27  
ALA   HB1  H  N N 28  
ALA   HB2  H  N N 29  
ALA   HB3  H  N N 30  
ALA   HXT  H  N N 31  
ARG   N    N  N N 32  
ARG   CA   C  N S 33  
ARG   C    C  N N 34  
ARG   O    O  N N 35  
ARG   CB   C  N N 36  
ARG   CG   C  N N 37  
ARG   CD   C  N N 38  
ARG   NE   N  N N 39  
ARG   CZ   C  N N 40  
ARG   NH1  N  N N 41  
ARG   NH2  N  N N 42  
ARG   OXT  O  N N 43  
ARG   H    H  N N 44  
ARG   H2   H  N N 45  
ARG   HA   H  N N 46  
ARG   HB2  H  N N 47  
ARG   HB3  H  N N 48  
ARG   HG2  H  N N 49  
ARG   HG3  H  N N 50  
ARG   HD2  H  N N 51  
ARG   HD3  H  N N 52  
ARG   HE   H  N N 53  
ARG   HH11 H  N N 54  
ARG   HH12 H  N N 55  
ARG   HH21 H  N N 56  
ARG   HH22 H  N N 57  
ARG   HXT  H  N N 58  
ASN   N    N  N N 59  
ASN   CA   C  N S 60  
ASN   C    C  N N 61  
ASN   O    O  N N 62  
ASN   CB   C  N N 63  
ASN   CG   C  N N 64  
ASN   OD1  O  N N 65  
ASN   ND2  N  N N 66  
ASN   OXT  O  N N 67  
ASN   H    H  N N 68  
ASN   H2   H  N N 69  
ASN   HA   H  N N 70  
ASN   HB2  H  N N 71  
ASN   HB3  H  N N 72  
ASN   HD21 H  N N 73  
ASN   HD22 H  N N 74  
ASN   HXT  H  N N 75  
ASP   N    N  N N 76  
ASP   CA   C  N S 77  
ASP   C    C  N N 78  
ASP   O    O  N N 79  
ASP   CB   C  N N 80  
ASP   CG   C  N N 81  
ASP   OD1  O  N N 82  
ASP   OD2  O  N N 83  
ASP   OXT  O  N N 84  
ASP   H    H  N N 85  
ASP   H2   H  N N 86  
ASP   HA   H  N N 87  
ASP   HB2  H  N N 88  
ASP   HB3  H  N N 89  
ASP   HD2  H  N N 90  
ASP   HXT  H  N N 91  
CYS   N    N  N N 92  
CYS   CA   C  N R 93  
CYS   C    C  N N 94  
CYS   O    O  N N 95  
CYS   CB   C  N N 96  
CYS   SG   S  N N 97  
CYS   OXT  O  N N 98  
CYS   H    H  N N 99  
CYS   H2   H  N N 100 
CYS   HA   H  N N 101 
CYS   HB2  H  N N 102 
CYS   HB3  H  N N 103 
CYS   HG   H  N N 104 
CYS   HXT  H  N N 105 
GLN   N    N  N N 106 
GLN   CA   C  N S 107 
GLN   C    C  N N 108 
GLN   O    O  N N 109 
GLN   CB   C  N N 110 
GLN   CG   C  N N 111 
GLN   CD   C  N N 112 
GLN   OE1  O  N N 113 
GLN   NE2  N  N N 114 
GLN   OXT  O  N N 115 
GLN   H    H  N N 116 
GLN   H2   H  N N 117 
GLN   HA   H  N N 118 
GLN   HB2  H  N N 119 
GLN   HB3  H  N N 120 
GLN   HG2  H  N N 121 
GLN   HG3  H  N N 122 
GLN   HE21 H  N N 123 
GLN   HE22 H  N N 124 
GLN   HXT  H  N N 125 
GLU   N    N  N N 126 
GLU   CA   C  N S 127 
GLU   C    C  N N 128 
GLU   O    O  N N 129 
GLU   CB   C  N N 130 
GLU   CG   C  N N 131 
GLU   CD   C  N N 132 
GLU   OE1  O  N N 133 
GLU   OE2  O  N N 134 
GLU   OXT  O  N N 135 
GLU   H    H  N N 136 
GLU   H2   H  N N 137 
GLU   HA   H  N N 138 
GLU   HB2  H  N N 139 
GLU   HB3  H  N N 140 
GLU   HG2  H  N N 141 
GLU   HG3  H  N N 142 
GLU   HE2  H  N N 143 
GLU   HXT  H  N N 144 
GLY   N    N  N N 145 
GLY   CA   C  N N 146 
GLY   C    C  N N 147 
GLY   O    O  N N 148 
GLY   OXT  O  N N 149 
GLY   H    H  N N 150 
GLY   H2   H  N N 151 
GLY   HA2  H  N N 152 
GLY   HA3  H  N N 153 
GLY   HXT  H  N N 154 
HIS   N    N  N N 155 
HIS   CA   C  N S 156 
HIS   C    C  N N 157 
HIS   O    O  N N 158 
HIS   CB   C  N N 159 
HIS   CG   C  Y N 160 
HIS   ND1  N  Y N 161 
HIS   CD2  C  Y N 162 
HIS   CE1  C  Y N 163 
HIS   NE2  N  Y N 164 
HIS   OXT  O  N N 165 
HIS   H    H  N N 166 
HIS   H2   H  N N 167 
HIS   HA   H  N N 168 
HIS   HB2  H  N N 169 
HIS   HB3  H  N N 170 
HIS   HD1  H  N N 171 
HIS   HD2  H  N N 172 
HIS   HE1  H  N N 173 
HIS   HE2  H  N N 174 
HIS   HXT  H  N N 175 
HOH   O    O  N N 176 
HOH   H1   H  N N 177 
HOH   H2   H  N N 178 
ILE   N    N  N N 179 
ILE   CA   C  N S 180 
ILE   C    C  N N 181 
ILE   O    O  N N 182 
ILE   CB   C  N S 183 
ILE   CG1  C  N N 184 
ILE   CG2  C  N N 185 
ILE   CD1  C  N N 186 
ILE   OXT  O  N N 187 
ILE   H    H  N N 188 
ILE   H2   H  N N 189 
ILE   HA   H  N N 190 
ILE   HB   H  N N 191 
ILE   HG12 H  N N 192 
ILE   HG13 H  N N 193 
ILE   HG21 H  N N 194 
ILE   HG22 H  N N 195 
ILE   HG23 H  N N 196 
ILE   HD11 H  N N 197 
ILE   HD12 H  N N 198 
ILE   HD13 H  N N 199 
ILE   HXT  H  N N 200 
LEU   N    N  N N 201 
LEU   CA   C  N S 202 
LEU   C    C  N N 203 
LEU   O    O  N N 204 
LEU   CB   C  N N 205 
LEU   CG   C  N N 206 
LEU   CD1  C  N N 207 
LEU   CD2  C  N N 208 
LEU   OXT  O  N N 209 
LEU   H    H  N N 210 
LEU   H2   H  N N 211 
LEU   HA   H  N N 212 
LEU   HB2  H  N N 213 
LEU   HB3  H  N N 214 
LEU   HG   H  N N 215 
LEU   HD11 H  N N 216 
LEU   HD12 H  N N 217 
LEU   HD13 H  N N 218 
LEU   HD21 H  N N 219 
LEU   HD22 H  N N 220 
LEU   HD23 H  N N 221 
LEU   HXT  H  N N 222 
LYS   N    N  N N 223 
LYS   CA   C  N S 224 
LYS   C    C  N N 225 
LYS   O    O  N N 226 
LYS   CB   C  N N 227 
LYS   CG   C  N N 228 
LYS   CD   C  N N 229 
LYS   CE   C  N N 230 
LYS   NZ   N  N N 231 
LYS   OXT  O  N N 232 
LYS   H    H  N N 233 
LYS   H2   H  N N 234 
LYS   HA   H  N N 235 
LYS   HB2  H  N N 236 
LYS   HB3  H  N N 237 
LYS   HG2  H  N N 238 
LYS   HG3  H  N N 239 
LYS   HD2  H  N N 240 
LYS   HD3  H  N N 241 
LYS   HE2  H  N N 242 
LYS   HE3  H  N N 243 
LYS   HZ1  H  N N 244 
LYS   HZ2  H  N N 245 
LYS   HZ3  H  N N 246 
LYS   HXT  H  N N 247 
MET   N    N  N N 248 
MET   CA   C  N S 249 
MET   C    C  N N 250 
MET   O    O  N N 251 
MET   CB   C  N N 252 
MET   CG   C  N N 253 
MET   SD   S  N N 254 
MET   CE   C  N N 255 
MET   OXT  O  N N 256 
MET   H    H  N N 257 
MET   H2   H  N N 258 
MET   HA   H  N N 259 
MET   HB2  H  N N 260 
MET   HB3  H  N N 261 
MET   HG2  H  N N 262 
MET   HG3  H  N N 263 
MET   HE1  H  N N 264 
MET   HE2  H  N N 265 
MET   HE3  H  N N 266 
MET   HXT  H  N N 267 
PHE   N    N  N N 268 
PHE   CA   C  N S 269 
PHE   C    C  N N 270 
PHE   O    O  N N 271 
PHE   CB   C  N N 272 
PHE   CG   C  Y N 273 
PHE   CD1  C  Y N 274 
PHE   CD2  C  Y N 275 
PHE   CE1  C  Y N 276 
PHE   CE2  C  Y N 277 
PHE   CZ   C  Y N 278 
PHE   OXT  O  N N 279 
PHE   H    H  N N 280 
PHE   H2   H  N N 281 
PHE   HA   H  N N 282 
PHE   HB2  H  N N 283 
PHE   HB3  H  N N 284 
PHE   HD1  H  N N 285 
PHE   HD2  H  N N 286 
PHE   HE1  H  N N 287 
PHE   HE2  H  N N 288 
PHE   HZ   H  N N 289 
PHE   HXT  H  N N 290 
PRO   N    N  N N 291 
PRO   CA   C  N S 292 
PRO   C    C  N N 293 
PRO   O    O  N N 294 
PRO   CB   C  N N 295 
PRO   CG   C  N N 296 
PRO   CD   C  N N 297 
PRO   OXT  O  N N 298 
PRO   H    H  N N 299 
PRO   HA   H  N N 300 
PRO   HB2  H  N N 301 
PRO   HB3  H  N N 302 
PRO   HG2  H  N N 303 
PRO   HG3  H  N N 304 
PRO   HD2  H  N N 305 
PRO   HD3  H  N N 306 
PRO   HXT  H  N N 307 
SER   N    N  N N 308 
SER   CA   C  N S 309 
SER   C    C  N N 310 
SER   O    O  N N 311 
SER   CB   C  N N 312 
SER   OG   O  N N 313 
SER   OXT  O  N N 314 
SER   H    H  N N 315 
SER   H2   H  N N 316 
SER   HA   H  N N 317 
SER   HB2  H  N N 318 
SER   HB3  H  N N 319 
SER   HG   H  N N 320 
SER   HXT  H  N N 321 
SO4   S    S  N N 322 
SO4   O1   O  N N 323 
SO4   O2   O  N N 324 
SO4   O3   O  N N 325 
SO4   O4   O  N N 326 
THR   N    N  N N 327 
THR   CA   C  N S 328 
THR   C    C  N N 329 
THR   O    O  N N 330 
THR   CB   C  N R 331 
THR   OG1  O  N N 332 
THR   CG2  C  N N 333 
THR   OXT  O  N N 334 
THR   H    H  N N 335 
THR   H2   H  N N 336 
THR   HA   H  N N 337 
THR   HB   H  N N 338 
THR   HG1  H  N N 339 
THR   HG21 H  N N 340 
THR   HG22 H  N N 341 
THR   HG23 H  N N 342 
THR   HXT  H  N N 343 
TRP   N    N  N N 344 
TRP   CA   C  N S 345 
TRP   C    C  N N 346 
TRP   O    O  N N 347 
TRP   CB   C  N N 348 
TRP   CG   C  Y N 349 
TRP   CD1  C  Y N 350 
TRP   CD2  C  Y N 351 
TRP   NE1  N  Y N 352 
TRP   CE2  C  Y N 353 
TRP   CE3  C  Y N 354 
TRP   CZ2  C  Y N 355 
TRP   CZ3  C  Y N 356 
TRP   CH2  C  Y N 357 
TRP   OXT  O  N N 358 
TRP   H    H  N N 359 
TRP   H2   H  N N 360 
TRP   HA   H  N N 361 
TRP   HB2  H  N N 362 
TRP   HB3  H  N N 363 
TRP   HD1  H  N N 364 
TRP   HE1  H  N N 365 
TRP   HE3  H  N N 366 
TRP   HZ2  H  N N 367 
TRP   HZ3  H  N N 368 
TRP   HH2  H  N N 369 
TRP   HXT  H  N N 370 
TYR   N    N  N N 371 
TYR   CA   C  N S 372 
TYR   C    C  N N 373 
TYR   O    O  N N 374 
TYR   CB   C  N N 375 
TYR   CG   C  Y N 376 
TYR   CD1  C  Y N 377 
TYR   CD2  C  Y N 378 
TYR   CE1  C  Y N 379 
TYR   CE2  C  Y N 380 
TYR   CZ   C  Y N 381 
TYR   OH   O  N N 382 
TYR   OXT  O  N N 383 
TYR   H    H  N N 384 
TYR   H2   H  N N 385 
TYR   HA   H  N N 386 
TYR   HB2  H  N N 387 
TYR   HB3  H  N N 388 
TYR   HD1  H  N N 389 
TYR   HD2  H  N N 390 
TYR   HE1  H  N N 391 
TYR   HE2  H  N N 392 
TYR   HH   H  N N 393 
TYR   HXT  H  N N 394 
VAL   N    N  N N 395 
VAL   CA   C  N S 396 
VAL   C    C  N N 397 
VAL   O    O  N N 398 
VAL   CB   C  N N 399 
VAL   CG1  C  N N 400 
VAL   CG2  C  N N 401 
VAL   OXT  O  N N 402 
VAL   H    H  N N 403 
VAL   H2   H  N N 404 
VAL   HA   H  N N 405 
VAL   HB   H  N N 406 
VAL   HG11 H  N N 407 
VAL   HG12 H  N N 408 
VAL   HG13 H  N N 409 
VAL   HG21 H  N N 410 
VAL   HG22 H  N N 411 
VAL   HG23 H  N N 412 
VAL   HXT  H  N N 413 
# 
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 
A1D73 C09  N10  sing Y N 1   
A1D73 C09  C08  doub Y N 2   
A1D73 BR12 C08  sing N N 3   
A1D73 N10  N11  sing Y N 4   
A1D73 C08  C07  sing Y N 5   
A1D73 N11  C07  doub Y N 6   
A1D73 C07  C06  sing N N 7   
A1D73 C05  C06  doub Y N 8   
A1D73 C05  C04  sing Y N 9   
A1D73 C06  C01  sing Y N 10  
A1D73 C04  N03  doub Y N 11  
A1D73 C01  C02  doub Y N 12  
A1D73 N03  C02  sing Y N 13  
A1D73 C01  H1   sing N N 14  
A1D73 C02  H2   sing N N 15  
A1D73 C04  H3   sing N N 16  
A1D73 C05  H4   sing N N 17  
A1D73 C09  H5   sing N N 18  
A1D73 N10  H6   sing N N 19  
ALA   N    CA   sing N N 20  
ALA   N    H    sing N N 21  
ALA   N    H2   sing N N 22  
ALA   CA   C    sing N N 23  
ALA   CA   CB   sing N N 24  
ALA   CA   HA   sing N N 25  
ALA   C    O    doub N N 26  
ALA   C    OXT  sing N N 27  
ALA   CB   HB1  sing N N 28  
ALA   CB   HB2  sing N N 29  
ALA   CB   HB3  sing N N 30  
ALA   OXT  HXT  sing N N 31  
ARG   N    CA   sing N N 32  
ARG   N    H    sing N N 33  
ARG   N    H2   sing N N 34  
ARG   CA   C    sing N N 35  
ARG   CA   CB   sing N N 36  
ARG   CA   HA   sing N N 37  
ARG   C    O    doub N N 38  
ARG   C    OXT  sing N N 39  
ARG   CB   CG   sing N N 40  
ARG   CB   HB2  sing N N 41  
ARG   CB   HB3  sing N N 42  
ARG   CG   CD   sing N N 43  
ARG   CG   HG2  sing N N 44  
ARG   CG   HG3  sing N N 45  
ARG   CD   NE   sing N N 46  
ARG   CD   HD2  sing N N 47  
ARG   CD   HD3  sing N N 48  
ARG   NE   CZ   sing N N 49  
ARG   NE   HE   sing N N 50  
ARG   CZ   NH1  sing N N 51  
ARG   CZ   NH2  doub N N 52  
ARG   NH1  HH11 sing N N 53  
ARG   NH1  HH12 sing N N 54  
ARG   NH2  HH21 sing N N 55  
ARG   NH2  HH22 sing N N 56  
ARG   OXT  HXT  sing N N 57  
ASN   N    CA   sing N N 58  
ASN   N    H    sing N N 59  
ASN   N    H2   sing N N 60  
ASN   CA   C    sing N N 61  
ASN   CA   CB   sing N N 62  
ASN   CA   HA   sing N N 63  
ASN   C    O    doub N N 64  
ASN   C    OXT  sing N N 65  
ASN   CB   CG   sing N N 66  
ASN   CB   HB2  sing N N 67  
ASN   CB   HB3  sing N N 68  
ASN   CG   OD1  doub N N 69  
ASN   CG   ND2  sing N N 70  
ASN   ND2  HD21 sing N N 71  
ASN   ND2  HD22 sing N N 72  
ASN   OXT  HXT  sing N N 73  
ASP   N    CA   sing N N 74  
ASP   N    H    sing N N 75  
ASP   N    H2   sing N N 76  
ASP   CA   C    sing N N 77  
ASP   CA   CB   sing N N 78  
ASP   CA   HA   sing N N 79  
ASP   C    O    doub N N 80  
ASP   C    OXT  sing N N 81  
ASP   CB   CG   sing N N 82  
ASP   CB   HB2  sing N N 83  
ASP   CB   HB3  sing N N 84  
ASP   CG   OD1  doub N N 85  
ASP   CG   OD2  sing N N 86  
ASP   OD2  HD2  sing N N 87  
ASP   OXT  HXT  sing N N 88  
CYS   N    CA   sing N N 89  
CYS   N    H    sing N N 90  
CYS   N    H2   sing N N 91  
CYS   CA   C    sing N N 92  
CYS   CA   CB   sing N N 93  
CYS   CA   HA   sing N N 94  
CYS   C    O    doub N N 95  
CYS   C    OXT  sing N N 96  
CYS   CB   SG   sing N N 97  
CYS   CB   HB2  sing N N 98  
CYS   CB   HB3  sing N N 99  
CYS   SG   HG   sing N N 100 
CYS   OXT  HXT  sing N N 101 
GLN   N    CA   sing N N 102 
GLN   N    H    sing N N 103 
GLN   N    H2   sing N N 104 
GLN   CA   C    sing N N 105 
GLN   CA   CB   sing N N 106 
GLN   CA   HA   sing N N 107 
GLN   C    O    doub N N 108 
GLN   C    OXT  sing N N 109 
GLN   CB   CG   sing N N 110 
GLN   CB   HB2  sing N N 111 
GLN   CB   HB3  sing N N 112 
GLN   CG   CD   sing N N 113 
GLN   CG   HG2  sing N N 114 
GLN   CG   HG3  sing N N 115 
GLN   CD   OE1  doub N N 116 
GLN   CD   NE2  sing N N 117 
GLN   NE2  HE21 sing N N 118 
GLN   NE2  HE22 sing N N 119 
GLN   OXT  HXT  sing N N 120 
GLU   N    CA   sing N N 121 
GLU   N    H    sing N N 122 
GLU   N    H2   sing N N 123 
GLU   CA   C    sing N N 124 
GLU   CA   CB   sing N N 125 
GLU   CA   HA   sing N N 126 
GLU   C    O    doub N N 127 
GLU   C    OXT  sing N N 128 
GLU   CB   CG   sing N N 129 
GLU   CB   HB2  sing N N 130 
GLU   CB   HB3  sing N N 131 
GLU   CG   CD   sing N N 132 
GLU   CG   HG2  sing N N 133 
GLU   CG   HG3  sing N N 134 
GLU   CD   OE1  doub N N 135 
GLU   CD   OE2  sing N N 136 
GLU   OE2  HE2  sing N N 137 
GLU   OXT  HXT  sing N N 138 
GLY   N    CA   sing N N 139 
GLY   N    H    sing N N 140 
GLY   N    H2   sing N N 141 
GLY   CA   C    sing N N 142 
GLY   CA   HA2  sing N N 143 
GLY   CA   HA3  sing N N 144 
GLY   C    O    doub N N 145 
GLY   C    OXT  sing N N 146 
GLY   OXT  HXT  sing N N 147 
HIS   N    CA   sing N N 148 
HIS   N    H    sing N N 149 
HIS   N    H2   sing N N 150 
HIS   CA   C    sing N N 151 
HIS   CA   CB   sing N N 152 
HIS   CA   HA   sing N N 153 
HIS   C    O    doub N N 154 
HIS   C    OXT  sing N N 155 
HIS   CB   CG   sing N N 156 
HIS   CB   HB2  sing N N 157 
HIS   CB   HB3  sing N N 158 
HIS   CG   ND1  sing Y N 159 
HIS   CG   CD2  doub Y N 160 
HIS   ND1  CE1  doub Y N 161 
HIS   ND1  HD1  sing N N 162 
HIS   CD2  NE2  sing Y N 163 
HIS   CD2  HD2  sing N N 164 
HIS   CE1  NE2  sing Y N 165 
HIS   CE1  HE1  sing N N 166 
HIS   NE2  HE2  sing N N 167 
HIS   OXT  HXT  sing N N 168 
HOH   O    H1   sing N N 169 
HOH   O    H2   sing N N 170 
ILE   N    CA   sing N N 171 
ILE   N    H    sing N N 172 
ILE   N    H2   sing N N 173 
ILE   CA   C    sing N N 174 
ILE   CA   CB   sing N N 175 
ILE   CA   HA   sing N N 176 
ILE   C    O    doub N N 177 
ILE   C    OXT  sing N N 178 
ILE   CB   CG1  sing N N 179 
ILE   CB   CG2  sing N N 180 
ILE   CB   HB   sing N N 181 
ILE   CG1  CD1  sing N N 182 
ILE   CG1  HG12 sing N N 183 
ILE   CG1  HG13 sing N N 184 
ILE   CG2  HG21 sing N N 185 
ILE   CG2  HG22 sing N N 186 
ILE   CG2  HG23 sing N N 187 
ILE   CD1  HD11 sing N N 188 
ILE   CD1  HD12 sing N N 189 
ILE   CD1  HD13 sing N N 190 
ILE   OXT  HXT  sing N N 191 
LEU   N    CA   sing N N 192 
LEU   N    H    sing N N 193 
LEU   N    H2   sing N N 194 
LEU   CA   C    sing N N 195 
LEU   CA   CB   sing N N 196 
LEU   CA   HA   sing N N 197 
LEU   C    O    doub N N 198 
LEU   C    OXT  sing N N 199 
LEU   CB   CG   sing N N 200 
LEU   CB   HB2  sing N N 201 
LEU   CB   HB3  sing N N 202 
LEU   CG   CD1  sing N N 203 
LEU   CG   CD2  sing N N 204 
LEU   CG   HG   sing N N 205 
LEU   CD1  HD11 sing N N 206 
LEU   CD1  HD12 sing N N 207 
LEU   CD1  HD13 sing N N 208 
LEU   CD2  HD21 sing N N 209 
LEU   CD2  HD22 sing N N 210 
LEU   CD2  HD23 sing N N 211 
LEU   OXT  HXT  sing N N 212 
LYS   N    CA   sing N N 213 
LYS   N    H    sing N N 214 
LYS   N    H2   sing N N 215 
LYS   CA   C    sing N N 216 
LYS   CA   CB   sing N N 217 
LYS   CA   HA   sing N N 218 
LYS   C    O    doub N N 219 
LYS   C    OXT  sing N N 220 
LYS   CB   CG   sing N N 221 
LYS   CB   HB2  sing N N 222 
LYS   CB   HB3  sing N N 223 
LYS   CG   CD   sing N N 224 
LYS   CG   HG2  sing N N 225 
LYS   CG   HG3  sing N N 226 
LYS   CD   CE   sing N N 227 
LYS   CD   HD2  sing N N 228 
LYS   CD   HD3  sing N N 229 
LYS   CE   NZ   sing N N 230 
LYS   CE   HE2  sing N N 231 
LYS   CE   HE3  sing N N 232 
LYS   NZ   HZ1  sing N N 233 
LYS   NZ   HZ2  sing N N 234 
LYS   NZ   HZ3  sing N N 235 
LYS   OXT  HXT  sing N N 236 
MET   N    CA   sing N N 237 
MET   N    H    sing N N 238 
MET   N    H2   sing N N 239 
MET   CA   C    sing N N 240 
MET   CA   CB   sing N N 241 
MET   CA   HA   sing N N 242 
MET   C    O    doub N N 243 
MET   C    OXT  sing N N 244 
MET   CB   CG   sing N N 245 
MET   CB   HB2  sing N N 246 
MET   CB   HB3  sing N N 247 
MET   CG   SD   sing N N 248 
MET   CG   HG2  sing N N 249 
MET   CG   HG3  sing N N 250 
MET   SD   CE   sing N N 251 
MET   CE   HE1  sing N N 252 
MET   CE   HE2  sing N N 253 
MET   CE   HE3  sing N N 254 
MET   OXT  HXT  sing N N 255 
PHE   N    CA   sing N N 256 
PHE   N    H    sing N N 257 
PHE   N    H2   sing N N 258 
PHE   CA   C    sing N N 259 
PHE   CA   CB   sing N N 260 
PHE   CA   HA   sing N N 261 
PHE   C    O    doub N N 262 
PHE   C    OXT  sing N N 263 
PHE   CB   CG   sing N N 264 
PHE   CB   HB2  sing N N 265 
PHE   CB   HB3  sing N N 266 
PHE   CG   CD1  doub Y N 267 
PHE   CG   CD2  sing Y N 268 
PHE   CD1  CE1  sing Y N 269 
PHE   CD1  HD1  sing N N 270 
PHE   CD2  CE2  doub Y N 271 
PHE   CD2  HD2  sing N N 272 
PHE   CE1  CZ   doub Y N 273 
PHE   CE1  HE1  sing N N 274 
PHE   CE2  CZ   sing Y N 275 
PHE   CE2  HE2  sing N N 276 
PHE   CZ   HZ   sing N N 277 
PHE   OXT  HXT  sing N N 278 
PRO   N    CA   sing N N 279 
PRO   N    CD   sing N N 280 
PRO   N    H    sing N N 281 
PRO   CA   C    sing N N 282 
PRO   CA   CB   sing N N 283 
PRO   CA   HA   sing N N 284 
PRO   C    O    doub N N 285 
PRO   C    OXT  sing N N 286 
PRO   CB   CG   sing N N 287 
PRO   CB   HB2  sing N N 288 
PRO   CB   HB3  sing N N 289 
PRO   CG   CD   sing N N 290 
PRO   CG   HG2  sing N N 291 
PRO   CG   HG3  sing N N 292 
PRO   CD   HD2  sing N N 293 
PRO   CD   HD3  sing N N 294 
PRO   OXT  HXT  sing N N 295 
SER   N    CA   sing N N 296 
SER   N    H    sing N N 297 
SER   N    H2   sing N N 298 
SER   CA   C    sing N N 299 
SER   CA   CB   sing N N 300 
SER   CA   HA   sing N N 301 
SER   C    O    doub N N 302 
SER   C    OXT  sing N N 303 
SER   CB   OG   sing N N 304 
SER   CB   HB2  sing N N 305 
SER   CB   HB3  sing N N 306 
SER   OG   HG   sing N N 307 
SER   OXT  HXT  sing N N 308 
SO4   S    O1   doub N N 309 
SO4   S    O2   doub N N 310 
SO4   S    O3   sing N N 311 
SO4   S    O4   sing N N 312 
THR   N    CA   sing N N 313 
THR   N    H    sing N N 314 
THR   N    H2   sing N N 315 
THR   CA   C    sing N N 316 
THR   CA   CB   sing N N 317 
THR   CA   HA   sing N N 318 
THR   C    O    doub N N 319 
THR   C    OXT  sing N N 320 
THR   CB   OG1  sing N N 321 
THR   CB   CG2  sing N N 322 
THR   CB   HB   sing N N 323 
THR   OG1  HG1  sing N N 324 
THR   CG2  HG21 sing N N 325 
THR   CG2  HG22 sing N N 326 
THR   CG2  HG23 sing N N 327 
THR   OXT  HXT  sing N N 328 
TRP   N    CA   sing N N 329 
TRP   N    H    sing N N 330 
TRP   N    H2   sing N N 331 
TRP   CA   C    sing N N 332 
TRP   CA   CB   sing N N 333 
TRP   CA   HA   sing N N 334 
TRP   C    O    doub N N 335 
TRP   C    OXT  sing N N 336 
TRP   CB   CG   sing N N 337 
TRP   CB   HB2  sing N N 338 
TRP   CB   HB3  sing N N 339 
TRP   CG   CD1  doub Y N 340 
TRP   CG   CD2  sing Y N 341 
TRP   CD1  NE1  sing Y N 342 
TRP   CD1  HD1  sing N N 343 
TRP   CD2  CE2  doub Y N 344 
TRP   CD2  CE3  sing Y N 345 
TRP   NE1  CE2  sing Y N 346 
TRP   NE1  HE1  sing N N 347 
TRP   CE2  CZ2  sing Y N 348 
TRP   CE3  CZ3  doub Y N 349 
TRP   CE3  HE3  sing N N 350 
TRP   CZ2  CH2  doub Y N 351 
TRP   CZ2  HZ2  sing N N 352 
TRP   CZ3  CH2  sing Y N 353 
TRP   CZ3  HZ3  sing N N 354 
TRP   CH2  HH2  sing N N 355 
TRP   OXT  HXT  sing N N 356 
TYR   N    CA   sing N N 357 
TYR   N    H    sing N N 358 
TYR   N    H2   sing N N 359 
TYR   CA   C    sing N N 360 
TYR   CA   CB   sing N N 361 
TYR   CA   HA   sing N N 362 
TYR   C    O    doub N N 363 
TYR   C    OXT  sing N N 364 
TYR   CB   CG   sing N N 365 
TYR   CB   HB2  sing N N 366 
TYR   CB   HB3  sing N N 367 
TYR   CG   CD1  doub Y N 368 
TYR   CG   CD2  sing Y N 369 
TYR   CD1  CE1  sing Y N 370 
TYR   CD1  HD1  sing N N 371 
TYR   CD2  CE2  doub Y N 372 
TYR   CD2  HD2  sing N N 373 
TYR   CE1  CZ   doub Y N 374 
TYR   CE1  HE1  sing N N 375 
TYR   CE2  CZ   sing Y N 376 
TYR   CE2  HE2  sing N N 377 
TYR   CZ   OH   sing N N 378 
TYR   OH   HH   sing N N 379 
TYR   OXT  HXT  sing N N 380 
VAL   N    CA   sing N N 381 
VAL   N    H    sing N N 382 
VAL   N    H2   sing N N 383 
VAL   CA   C    sing N N 384 
VAL   CA   CB   sing N N 385 
VAL   CA   HA   sing N N 386 
VAL   C    O    doub N N 387 
VAL   C    OXT  sing N N 388 
VAL   CB   CG1  sing N N 389 
VAL   CB   CG2  sing N N 390 
VAL   CB   HB   sing N N 391 
VAL   CG1  HG11 sing N N 392 
VAL   CG1  HG12 sing N N 393 
VAL   CG1  HG13 sing N N 394 
VAL   CG2  HG21 sing N N 395 
VAL   CG2  HG22 sing N N 396 
VAL   CG2  HG23 sing N N 397 
VAL   OXT  HXT  sing N N 398 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           22377119 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          apo 
# 
_atom_sites.entry_id                    8Z6C 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.023730 
_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]   0.023601 
_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]   0.006281 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
BR 
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 1  ? 21.714  25.292  -1.257  1.00 70.33 ? 1   MET   A N    1 
ATOM   2    C  CA   . MET   A 1 1  ? 20.331  24.831  -1.352  1.00 64.06 ? 1   MET   A CA   1 
ATOM   3    C  C    . MET   A 1 1  ? 20.003  23.553  -0.555  1.00 61.06 ? 1   MET   A C    1 
ATOM   4    O  O    . MET   A 1 1  ? 18.886  23.443  -0.043  1.00 74.26 ? 1   MET   A O    1 
ATOM   5    C  CB   . MET   A 1 1  ? 19.946  24.627  -2.821  1.00 66.89 ? 1   MET   A CB   1 
ATOM   6    N  N    . PRO   A 1 2  ? 20.922  22.577  -0.461  1.00 55.14 ? 2   PRO   A N    1 
ATOM   7    C  CA   . PRO   A 1 2  ? 20.602  21.368  0.318   1.00 50.75 ? 2   PRO   A CA   1 
ATOM   8    C  C    . PRO   A 1 2  ? 20.529  21.645  1.810   1.00 36.64 ? 2   PRO   A C    1 
ATOM   9    O  O    . PRO   A 1 2  ? 21.341  22.384  2.371   1.00 42.97 ? 2   PRO   A O    1 
ATOM   10   C  CB   . PRO   A 1 2  ? 21.750  20.397  -0.010  1.00 43.36 ? 2   PRO   A CB   1 
ATOM   11   C  CG   . PRO   A 1 2  ? 22.300  20.867  -1.285  1.00 46.79 ? 2   PRO   A CG   1 
ATOM   12   C  CD   . PRO   A 1 2  ? 22.144  22.373  -1.262  1.00 54.56 ? 2   PRO   A CD   1 
ATOM   13   N  N    . HIS   A 1 3  ? 19.537  21.039  2.445   1.00 41.48 ? 3   HIS   A N    1 
ATOM   14   C  CA   . HIS   A 1 3  ? 19.373  21.080  3.882   1.00 37.17 ? 3   HIS   A CA   1 
ATOM   15   C  C    . HIS   A 1 3  ? 19.808  19.747  4.480   1.00 31.45 ? 3   HIS   A C    1 
ATOM   16   O  O    . HIS   A 1 3  ? 20.216  18.820  3.776   1.00 33.18 ? 3   HIS   A O    1 
ATOM   17   C  CB   . HIS   A 1 3  ? 17.919  21.406  4.236   1.00 50.47 ? 3   HIS   A CB   1 
ATOM   18   C  CG   . HIS   A 1 3  ? 17.458  22.751  3.757   1.00 48.01 ? 3   HIS   A CG   1 
ATOM   19   N  ND1  . HIS   A 1 3  ? 16.135  23.132  3.772   1.00 46.23 ? 3   HIS   A ND1  1 
ATOM   20   C  CD2  . HIS   A 1 3  ? 18.147  23.812  3.269   1.00 55.31 ? 3   HIS   A CD2  1 
ATOM   21   C  CE1  . HIS   A 1 3  ? 16.025  24.366  3.315   1.00 50.98 ? 3   HIS   A CE1  1 
ATOM   22   N  NE2  . HIS   A 1 3  ? 17.232  24.802  3.001   1.00 53.31 ? 3   HIS   A NE2  1 
ATOM   23   N  N    . ALA   A 1 4  ? 19.712  19.638  5.799   1.00 31.76 ? 4   ALA   A N    1 
ATOM   24   C  CA   . ALA   A 1 4  ? 19.914  18.346  6.432   1.00 31.53 ? 4   ALA   A CA   1 
ATOM   25   C  C    . ALA   A 1 4  ? 18.799  17.385  6.030   1.00 27.92 ? 4   ALA   A C    1 
ATOM   26   O  O    . ALA   A 1 4  ? 17.729  17.793  5.562   1.00 31.46 ? 4   ALA   A O    1 
ATOM   27   C  CB   . ALA   A 1 4  ? 19.951  18.495  7.953   1.00 37.00 ? 4   ALA   A CB   1 
ATOM   28   N  N    . PHE   A 1 5  ? 19.059  16.092  6.207   1.00 24.54 ? 5   PHE   A N    1 
ATOM   29   C  CA   . PHE   A 1 5  ? 18.032  15.095  5.921   1.00 23.08 ? 5   PHE   A CA   1 
ATOM   30   C  C    . PHE   A 1 5  ? 16.870  15.254  6.901   1.00 23.91 ? 5   PHE   A C    1 
ATOM   31   O  O    . PHE   A 1 5  ? 17.057  15.632  8.059   1.00 25.04 ? 5   PHE   A O    1 
ATOM   32   C  CB   . PHE   A 1 5  ? 18.621  13.685  5.993   1.00 23.30 ? 5   PHE   A CB   1 
ATOM   33   C  CG   . PHE   A 1 5  ? 19.443  13.319  4.776   1.00 21.66 ? 5   PHE   A CG   1 
ATOM   34   C  CD1  . PHE   A 1 5  ? 18.820  13.030  3.577   1.00 20.60 ? 5   PHE   A CD1  1 
ATOM   35   C  CD2  . PHE   A 1 5  ? 20.833  13.297  4.830   1.00 23.30 ? 5   PHE   A CD2  1 
ATOM   36   C  CE1  . PHE   A 1 5  ? 19.545  12.703  2.448   1.00 21.14 ? 5   PHE   A CE1  1 
ATOM   37   C  CE2  . PHE   A 1 5  ? 21.572  12.982  3.696   1.00 18.86 ? 5   PHE   A CE2  1 
ATOM   38   C  CZ   . PHE   A 1 5  ? 20.912  12.681  2.503   1.00 19.34 ? 5   PHE   A CZ   1 
ATOM   39   N  N    . LYS   A 1 6  ? 15.658  14.994  6.418   1.00 18.26 ? 6   LYS   A N    1 
ATOM   40   C  CA   . LYS   A 1 6  ? 14.467  15.161  7.234   1.00 25.39 ? 6   LYS   A CA   1 
ATOM   41   C  C    . LYS   A 1 6  ? 13.485  14.049  6.907   1.00 22.74 ? 6   LYS   A C    1 
ATOM   42   O  O    . LYS   A 1 6  ? 13.549  13.454  5.820   1.00 19.72 ? 6   LYS   A O    1 
ATOM   43   C  CB   . LYS   A 1 6  ? 13.825  16.540  7.012   1.00 27.56 ? 6   LYS   A CB   1 
ATOM   44   C  CG   . LYS   A 1 6  ? 13.187  16.694  5.643   1.00 30.40 ? 6   LYS   A CG   1 
ATOM   45   C  CD   . LYS   A 1 6  ? 12.503  18.055  5.501   1.00 34.91 ? 6   LYS   A CD   1 
ATOM   46   C  CE   . LYS   A 1 6  ? 11.849  18.194  4.126   1.00 36.19 ? 6   LYS   A CE   1 
ATOM   47   N  NZ   . LYS   A 1 6  ? 12.849  17.929  3.040   1.00 36.16 ? 6   LYS   A NZ   1 
ATOM   48   N  N    . PRO   A 1 7  ? 12.634  13.675  7.860   1.00 22.70 ? 7   PRO   A N    1 
ATOM   49   C  CA   . PRO   A 1 7  ? 11.606  12.657  7.592   1.00 21.89 ? 7   PRO   A CA   1 
ATOM   50   C  C    . PRO   A 1 7  ? 10.877  12.908  6.281   1.00 25.91 ? 7   PRO   A C    1 
ATOM   51   O  O    . PRO   A 1 7  ? 10.462  14.036  5.989   1.00 21.17 ? 7   PRO   A O    1 
ATOM   52   C  CB   . PRO   A 1 7  ? 10.651  12.813  8.783   1.00 20.22 ? 7   PRO   A CB   1 
ATOM   53   C  CG   . PRO   A 1 7  ? 11.527  13.248  9.886   1.00 24.15 ? 7   PRO   A CG   1 
ATOM   54   C  CD   . PRO   A 1 7  ? 12.573  14.149  9.260   1.00 23.88 ? 7   PRO   A CD   1 
ATOM   55   N  N    . GLY   A 1 8  ? 10.690  11.836  5.509   1.00 20.65 ? 8   GLY   A N    1 
ATOM   56   C  CA   . GLY   A 1 8  ? 10.033  11.892  4.221   1.00 20.44 ? 8   GLY   A CA   1 
ATOM   57   C  C    . GLY   A 1 8  ? 10.970  12.032  3.036   1.00 22.27 ? 8   GLY   A C    1 
ATOM   58   O  O    . GLY   A 1 8  ? 10.538  11.829  1.897   1.00 17.21 ? 8   GLY   A O    1 
ATOM   59   N  N    . ASP   A 1 9  ? 12.238  12.376  3.268   1.00 20.18 ? 9   ASP   A N    1 
ATOM   60   C  CA   . ASP   A 1 9  ? 13.185  12.496  2.165   1.00 21.27 ? 9   ASP   A CA   1 
ATOM   61   C  C    . ASP   A 1 9  ? 13.391  11.140  1.518   1.00 16.80 ? 9   ASP   A C    1 
ATOM   62   O  O    . ASP   A 1 9  ? 13.520  10.134  2.213   1.00 15.74 ? 9   ASP   A O    1 
ATOM   63   C  CB   . ASP   A 1 9  ? 14.547  13.008  2.656   1.00 17.44 ? 9   ASP   A CB   1 
ATOM   64   C  CG   . ASP   A 1 9  ? 14.566  14.498  2.907   1.00 21.01 ? 9   ASP   A CG   1 
ATOM   65   O  OD1  . ASP   A 1 9  ? 13.593  15.186  2.566   1.00 23.11 ? 9   ASP   A OD1  1 
ATOM   66   O  OD2  . ASP   A 1 9  ? 15.569  14.997  3.460   1.00 22.33 ? 9   ASP   A OD2  1 
ATOM   67   N  N    . LEU   A 1 10 ? 13.471  11.121  0.185   1.00 15.18 ? 10  LEU   A N    1 
ATOM   68   C  CA   . LEU   A 1 10 ? 13.645  9.882   -0.567  1.00 16.63 ? 10  LEU   A CA   1 
ATOM   69   C  C    . LEU   A 1 10 ? 15.093  9.731   -0.976  1.00 21.08 ? 10  LEU   A C    1 
ATOM   70   O  O    . LEU   A 1 10 ? 15.719  10.697  -1.435  1.00 15.73 ? 10  LEU   A O    1 
ATOM   71   C  CB   . LEU   A 1 10 ? 12.766  9.866   -1.814  1.00 17.92 ? 10  LEU   A CB   1 
ATOM   72   C  CG   . LEU   A 1 10 ? 11.290  10.045  -1.455  1.00 17.35 ? 10  LEU   A CG   1 
ATOM   73   C  CD1  . LEU   A 1 10 ? 10.427  9.954   -2.707  1.00 17.30 ? 10  LEU   A CD1  1 
ATOM   74   C  CD2  . LEU   A 1 10 ? 10.831  8.992   -0.401  1.00 17.55 ? 10  LEU   A CD2  1 
ATOM   75   N  N    . VAL   A 1 11 ? 15.639  8.528   -0.801  1.00 12.80 ? 11  VAL   A N    1 
ATOM   76   C  CA   . VAL   A 1 11 ? 17.073  8.320   -1.014  1.00 16.00 ? 11  VAL   A CA   1 
ATOM   77   C  C    . VAL   A 1 11 ? 17.324  6.937   -1.605  1.00 20.15 ? 11  VAL   A C    1 
ATOM   78   O  O    . VAL   A 1 11 ? 16.444  6.074   -1.637  1.00 19.07 ? 11  VAL   A O    1 
ATOM   79   C  CB   . VAL   A 1 11 ? 17.894  8.487   0.285   1.00 16.62 ? 11  VAL   A CB   1 
ATOM   80   C  CG1  . VAL   A 1 11 ? 17.689  9.892   0.903   1.00 16.00 ? 11  VAL   A CG1  1 
ATOM   81   C  CG2  . VAL   A 1 11 ? 17.542  7.353   1.299   1.00 17.56 ? 11  VAL   A CG2  1 
ATOM   82   N  N    . PHE   A 1 12 ? 18.547  6.744   -2.088  1.00 17.20 ? 12  PHE   A N    1 
ATOM   83   C  CA   . PHE   A 1 12 ? 19.165  5.422   -2.132  1.00 18.33 ? 12  PHE   A CA   1 
ATOM   84   C  C    . PHE   A 1 12 ? 20.111  5.307   -0.943  1.00 16.12 ? 12  PHE   A C    1 
ATOM   85   O  O    . PHE   A 1 12 ? 20.903  6.219   -0.688  1.00 16.40 ? 12  PHE   A O    1 
ATOM   86   C  CB   . PHE   A 1 12 ? 19.929  5.197   -3.433  1.00 16.99 ? 12  PHE   A CB   1 
ATOM   87   C  CG   . PHE   A 1 12 ? 19.029  5.091   -4.646  1.00 22.11 ? 12  PHE   A CG   1 
ATOM   88   C  CD1  . PHE   A 1 12 ? 18.496  3.871   -5.026  1.00 21.24 ? 12  PHE   A CD1  1 
ATOM   89   C  CD2  . PHE   A 1 12 ? 18.686  6.227   -5.363  1.00 22.09 ? 12  PHE   A CD2  1 
ATOM   90   C  CE1  . PHE   A 1 12 ? 17.664  3.775   -6.138  1.00 20.52 ? 12  PHE   A CE1  1 
ATOM   91   C  CE2  . PHE   A 1 12 ? 17.837  6.145   -6.483  1.00 22.61 ? 12  PHE   A CE2  1 
ATOM   92   C  CZ   . PHE   A 1 12 ? 17.336  4.910   -6.864  1.00 25.48 ? 12  PHE   A CZ   1 
ATOM   93   N  N    . ALA   A 1 13 ? 20.039  4.197   -0.224  1.00 18.82 ? 13  ALA   A N    1 
ATOM   94   C  CA   . ALA   A 1 13 ? 20.823  4.033   0.990   1.00 17.92 ? 13  ALA   A CA   1 
ATOM   95   C  C    . ALA   A 1 13 ? 21.757  2.837   0.854   1.00 19.56 ? 13  ALA   A C    1 
ATOM   96   O  O    . ALA   A 1 13 ? 21.360  1.779   0.339   1.00 19.81 ? 13  ALA   A O    1 
ATOM   97   C  CB   . ALA   A 1 13 ? 19.898  3.863   2.209   1.00 15.25 ? 13  ALA   A CB   1 
ATOM   98   N  N    . LYS   A 1 14 ? 23.000  3.001   1.308   1.00 19.44 ? 14  LYS   A N    1 
ATOM   99   C  CA   . LYS   A 1 14 ? 24.057  2.017   1.066   1.00 16.19 ? 14  LYS   A CA   1 
ATOM   100  C  C    . LYS   A 1 14 ? 24.344  1.219   2.336   1.00 24.37 ? 14  LYS   A C    1 
ATOM   101  O  O    . LYS   A 1 14 ? 24.738  1.789   3.358   1.00 22.82 ? 14  LYS   A O    1 
ATOM   102  C  CB   . LYS   A 1 14 ? 25.332  2.699   0.553   1.00 20.44 ? 14  LYS   A CB   1 
ATOM   103  C  CG   . LYS   A 1 14 ? 26.409  1.725   0.044   1.00 24.91 ? 14  LYS   A CG   1 
ATOM   104  C  CD   . LYS   A 1 14 ? 25.844  0.765   -1.020  1.00 22.69 ? 14  LYS   A CD   1 
ATOM   105  C  CE   . LYS   A 1 14 ? 26.941  -0.084  -1.649  1.00 24.96 ? 14  LYS   A CE   1 
ATOM   106  N  NZ   . LYS   A 1 14 ? 27.267  -1.288  -0.811  1.00 22.36 ? 14  LYS   A NZ   1 
ATOM   107  N  N    . MET   A 1 15 ? 24.157  -0.100  2.249   1.00 23.21 ? 15  MET   A N    1 
ATOM   108  C  CA   . MET   A 1 15 ? 24.504  -1.087  3.267   1.00 22.80 ? 15  MET   A CA   1 
ATOM   109  C  C    . MET   A 1 15 ? 25.637  -1.966  2.743   1.00 26.11 ? 15  MET   A C    1 
ATOM   110  O  O    . MET   A 1 15 ? 25.681  -2.282  1.549   1.00 24.90 ? 15  MET   A O    1 
ATOM   111  C  CB   . MET   A 1 15 ? 23.298  -1.982  3.558   1.00 30.86 ? 15  MET   A CB   1 
ATOM   112  C  CG   . MET   A 1 15 ? 22.123  -1.504  4.414   1.00 37.10 ? 15  MET   A CG   1 
ATOM   113  S  SD   . MET   A 1 15 ? 22.397  -0.599  5.923   1.00 31.86 ? 15  MET   A SD   1 
ATOM   114  C  CE   . MET   A 1 15 ? 22.382  -1.953  7.086   1.00 33.02 ? 15  MET   A CE   1 
ATOM   115  N  N    . LYS   A 1 16 ? 26.532  -2.386  3.633   1.00 23.27 ? 16  LYS   A N    1 
ATOM   116  C  CA   . LYS   A 1 16 ? 27.623  -3.255  3.214   1.00 28.00 ? 16  LYS   A CA   1 
ATOM   117  C  C    . LYS   A 1 16 ? 27.057  -4.511  2.563   1.00 30.42 ? 16  LYS   A C    1 
ATOM   118  O  O    . LYS   A 1 16 ? 26.122  -5.116  3.086   1.00 26.21 ? 16  LYS   A O    1 
ATOM   119  C  CB   . LYS   A 1 16 ? 28.494  -3.611  4.420   1.00 27.33 ? 16  LYS   A CB   1 
ATOM   120  C  CG   . LYS   A 1 16 ? 29.578  -4.620  4.124   1.00 30.10 ? 16  LYS   A CG   1 
ATOM   121  C  CD   . LYS   A 1 16 ? 30.101  -5.215  5.439   1.00 33.16 ? 16  LYS   A CD   1 
ATOM   122  C  CE   . LYS   A 1 16 ? 31.012  -6.422  5.208   1.00 46.91 ? 16  LYS   A CE   1 
ATOM   123  N  NZ   . LYS   A 1 16 ? 30.242  -7.587  4.662   1.00 41.05 ? 16  LYS   A NZ   1 
ATOM   124  N  N    . GLY   A 1 17 ? 27.597  -4.881  1.402   1.00 29.02 ? 17  GLY   A N    1 
ATOM   125  C  CA   . GLY   A 1 17 ? 27.154  -6.081  0.724   1.00 29.42 ? 17  GLY   A CA   1 
ATOM   126  C  C    . GLY   A 1 17 ? 25.878  -5.955  -0.090  1.00 32.75 ? 17  GLY   A C    1 
ATOM   127  O  O    . GLY   A 1 17 ? 25.435  -6.956  -0.664  1.00 33.70 ? 17  GLY   A O    1 
ATOM   128  N  N    . TYR   A 1 18 ? 25.289  -4.769  -0.188  1.00 28.77 ? 18  TYR   A N    1 
ATOM   129  C  CA   . TYR   A 1 18 ? 24.044  -4.536  -0.904  1.00 27.07 ? 18  TYR   A CA   1 
ATOM   130  C  C    . TYR   A 1 18 ? 24.199  -3.402  -1.902  1.00 30.60 ? 18  TYR   A C    1 
ATOM   131  O  O    . TYR   A 1 18 ? 24.912  -2.433  -1.628  1.00 24.63 ? 18  TYR   A O    1 
ATOM   132  C  CB   . TYR   A 1 18 ? 22.908  -4.165  0.058   1.00 25.67 ? 18  TYR   A CB   1 
ATOM   133  C  CG   . TYR   A 1 18 ? 22.435  -5.287  0.937   1.00 29.72 ? 18  TYR   A CG   1 
ATOM   134  C  CD1  . TYR   A 1 18 ? 21.528  -6.229  0.466   1.00 38.15 ? 18  TYR   A CD1  1 
ATOM   135  C  CD2  . TYR   A 1 18 ? 22.909  -5.419  2.234   1.00 31.94 ? 18  TYR   A CD2  1 
ATOM   136  C  CE1  . TYR   A 1 18 ? 21.089  -7.260  1.279   1.00 36.68 ? 18  TYR   A CE1  1 
ATOM   137  C  CE2  . TYR   A 1 18 ? 22.484  -6.437  3.050   1.00 36.06 ? 18  TYR   A CE2  1 
ATOM   138  C  CZ   . TYR   A 1 18 ? 21.572  -7.359  2.574   1.00 43.28 ? 18  TYR   A CZ   1 
ATOM   139  O  OH   . TYR   A 1 18 ? 21.152  -8.378  3.405   1.00 42.42 ? 18  TYR   A OH   1 
ATOM   140  N  N    . PRO   A 1 19 ? 23.531  -3.484  -3.057  1.00 27.90 ? 19  PRO   A N    1 
ATOM   141  C  CA   . PRO   A 1 19 ? 23.500  -2.341  -3.974  1.00 23.37 ? 19  PRO   A CA   1 
ATOM   142  C  C    . PRO   A 1 19 ? 22.799  -1.173  -3.304  1.00 23.01 ? 19  PRO   A C    1 
ATOM   143  O  O    . PRO   A 1 19 ? 22.008  -1.362  -2.384  1.00 17.76 ? 19  PRO   A O    1 
ATOM   144  C  CB   . PRO   A 1 19 ? 22.685  -2.857  -5.160  1.00 26.18 ? 19  PRO   A CB   1 
ATOM   145  C  CG   . PRO   A 1 19 ? 21.768  -3.869  -4.553  1.00 29.83 ? 19  PRO   A CG   1 
ATOM   146  C  CD   . PRO   A 1 19 ? 22.578  -4.537  -3.459  1.00 35.16 ? 19  PRO   A CD   1 
ATOM   147  N  N    . HIS   A 1 20 ? 23.111  0.045   -3.761  1.00 22.66 ? 20  HIS   A N    1 
ATOM   148  C  CA   . HIS   A 1 20 ? 22.385  1.224   -3.291  1.00 19.80 ? 20  HIS   A CA   1 
ATOM   149  C  C    . HIS   A 1 20 ? 20.887  0.988   -3.441  1.00 24.30 ? 20  HIS   A C    1 
ATOM   150  O  O    . HIS   A 1 20 ? 20.412  0.605   -4.516  1.00 19.39 ? 20  HIS   A O    1 
ATOM   151  C  CB   . HIS   A 1 20 ? 22.813  2.466   -4.073  1.00 26.46 ? 20  HIS   A CB   1 
ATOM   152  C  CG   . HIS   A 1 20 ? 24.263  2.807   -3.906  1.00 19.39 ? 20  HIS   A CG   1 
ATOM   153  N  ND1  . HIS   A 1 20 ? 25.263  2.113   -4.550  1.00 22.70 ? 20  HIS   A ND1  1 
ATOM   154  C  CD2  . HIS   A 1 20 ? 24.880  3.733   -3.137  1.00 21.63 ? 20  HIS   A CD2  1 
ATOM   155  C  CE1  . HIS   A 1 20 ? 26.436  2.620   -4.215  1.00 27.27 ? 20  HIS   A CE1  1 
ATOM   156  N  NE2  . HIS   A 1 20 ? 26.231  3.600   -3.352  1.00 26.23 ? 20  HIS   A NE2  1 
ATOM   157  N  N    . TRP   A 1 21 ? 20.153  1.191   -2.350  1.00 21.03 ? 21  TRP   A N    1 
ATOM   158  C  CA   . TRP   A 1 21 ? 18.821  0.635   -2.206  1.00 18.65 ? 21  TRP   A CA   1 
ATOM   159  C  C    . TRP   A 1 21 ? 17.755  1.720   -2.049  1.00 19.41 ? 21  TRP   A C    1 
ATOM   160  O  O    . TRP   A 1 21 ? 17.934  2.646   -1.243  1.00 22.01 ? 21  TRP   A O    1 
ATOM   161  C  CB   . TRP   A 1 21 ? 18.797  -0.300  -0.990  1.00 20.34 ? 21  TRP   A CB   1 
ATOM   162  C  CG   . TRP   A 1 21 ? 17.741  -1.347  -1.085  1.00 19.02 ? 21  TRP   A CG   1 
ATOM   163  C  CD1  . TRP   A 1 21 ? 16.410  -1.189  -0.842  1.00 17.07 ? 21  TRP   A CD1  1 
ATOM   164  C  CD2  . TRP   A 1 21 ? 17.927  -2.726  -1.459  1.00 20.21 ? 21  TRP   A CD2  1 
ATOM   165  N  NE1  . TRP   A 1 21 ? 15.751  -2.396  -1.034  1.00 18.17 ? 21  TRP   A NE1  1 
ATOM   166  C  CE2  . TRP   A 1 21 ? 16.661  -3.346  -1.418  1.00 22.00 ? 21  TRP   A CE2  1 
ATOM   167  C  CE3  . TRP   A 1 21 ? 19.038  -3.487  -1.840  1.00 24.31 ? 21  TRP   A CE3  1 
ATOM   168  C  CZ2  . TRP   A 1 21 ? 16.475  -4.694  -1.735  1.00 24.68 ? 21  TRP   A CZ2  1 
ATOM   169  C  CZ3  . TRP   A 1 21 ? 18.853  -4.832  -2.154  1.00 28.02 ? 21  TRP   A CZ3  1 
ATOM   170  C  CH2  . TRP   A 1 21 ? 17.585  -5.420  -2.094  1.00 27.38 ? 21  TRP   A CH2  1 
ATOM   171  N  N    . PRO   A 1 22 ? 16.640  1.653   -2.779  1.00 16.06 ? 22  PRO   A N    1 
ATOM   172  C  CA   . PRO   A 1 22 ? 15.609  2.701   -2.634  1.00 16.43 ? 22  PRO   A CA   1 
ATOM   173  C  C    . PRO   A 1 22 ? 15.069  2.740   -1.211  1.00 16.80 ? 22  PRO   A C    1 
ATOM   174  O  O    . PRO   A 1 22 ? 14.719  1.710   -0.638  1.00 13.50 ? 22  PRO   A O    1 
ATOM   175  C  CB   . PRO   A 1 22 ? 14.528  2.279   -3.635  1.00 17.69 ? 22  PRO   A CB   1 
ATOM   176  C  CG   . PRO   A 1 22 ? 14.736  0.756   -3.803  1.00 17.33 ? 22  PRO   A CG   1 
ATOM   177  C  CD   . PRO   A 1 22 ? 16.255  0.636   -3.780  1.00 16.97 ? 22  PRO   A CD   1 
ATOM   178  N  N    . ALA   A 1 23 ? 15.012  3.933   -0.626  1.00 13.96 ? 23  ALA   A N    1 
ATOM   179  C  CA   . ALA   A 1 23 ? 14.650  4.018   0.792   1.00 15.64 ? 23  ALA   A CA   1 
ATOM   180  C  C    . ALA   A 1 23 ? 14.108  5.410   1.112   1.00 14.02 ? 23  ALA   A C    1 
ATOM   181  O  O    . ALA   A 1 23 ? 14.095  6.300   0.263   1.00 14.63 ? 23  ALA   A O    1 
ATOM   182  C  CB   . ALA   A 1 23 ? 15.855  3.701   1.680   1.00 17.68 ? 23  ALA   A CB   1 
ATOM   183  N  N    . ARG   A 1 24 ? 13.643  5.582   2.354   1.00 14.09 ? 24  ARG   A N    1 
ATOM   184  C  CA   . ARG   A 1 24 ? 13.193  6.887   2.819   1.00 18.23 ? 24  ARG   A CA   1 
ATOM   185  C  C    . ARG   A 1 24 ? 13.711  7.133   4.224   1.00 20.45 ? 24  ARG   A C    1 
ATOM   186  O  O    . ARG   A 1 24 ? 13.951  6.181   4.980   1.00 18.23 ? 24  ARG   A O    1 
ATOM   187  C  CB   . ARG   A 1 24 ? 11.662  6.976   2.806   1.00 15.92 ? 24  ARG   A CB   1 
ATOM   188  C  CG   . ARG   A 1 24 ? 10.979  6.194   3.936   1.00 19.15 ? 24  ARG   A CG   1 
ATOM   189  C  CD   . ARG   A 1 24 ? 9.432   6.209   3.753   1.00 17.74 ? 24  ARG   A CD   1 
ATOM   190  N  NE   . ARG   A 1 24 ? 8.744   5.484   4.824   1.00 22.47 ? 24  ARG   A NE   1 
ATOM   191  C  CZ   . ARG   A 1 24 ? 7.491   5.048   4.745   1.00 21.82 ? 24  ARG   A CZ   1 
ATOM   192  N  NH1  . ARG   A 1 24 ? 6.774   5.200   3.644   1.00 19.56 ? 24  ARG   A NH1  1 
ATOM   193  N  NH2  . ARG   A 1 24 ? 6.947   4.443   5.797   1.00 25.08 ? 24  ARG   A NH2  1 
ATOM   194  N  N    . ILE   A 1 25 ? 13.885  8.420   4.567   1.00 17.10 ? 25  ILE   A N    1 
ATOM   195  C  CA   . ILE   A 1 25 ? 14.079  8.802   5.966   1.00 16.78 ? 25  ILE   A CA   1 
ATOM   196  C  C    . ILE   A 1 25 ? 12.746  8.658   6.684   1.00 17.36 ? 25  ILE   A C    1 
ATOM   197  O  O    . ILE   A 1 25 ? 11.740  9.274   6.293   1.00 19.25 ? 25  ILE   A O    1 
ATOM   198  C  CB   . ILE   A 1 25 ? 14.591  10.245  6.111   1.00 20.79 ? 25  ILE   A CB   1 
ATOM   199  C  CG1  . ILE   A 1 25 ? 15.738  10.593  5.157   1.00 20.21 ? 25  ILE   A CG1  1 
ATOM   200  C  CG2  . ILE   A 1 25 ? 15.059  10.509  7.572   1.00 20.57 ? 25  ILE   A CG2  1 
ATOM   201  C  CD1  . ILE   A 1 25 ? 16.952  9.698   5.260   1.00 24.58 ? 25  ILE   A CD1  1 
ATOM   202  N  N    . ASP   A 1 26 ? 12.737  7.880   7.749   1.00 26.14 ? 26  ASP   A N    1 
ATOM   203  C  CA   . ASP   A 1 26 ? 11.513  7.647   8.491   1.00 26.81 ? 26  ASP   A CA   1 
ATOM   204  C  C    . ASP   A 1 26 ? 11.357  8.689   9.596   1.00 28.42 ? 26  ASP   A C    1 
ATOM   205  O  O    . ASP   A 1 26 ? 12.326  9.306   10.029  1.00 25.57 ? 26  ASP   A O    1 
ATOM   206  C  CB   . ASP   A 1 26 ? 11.539  6.246   9.093   1.00 26.06 ? 26  ASP   A CB   1 
ATOM   207  C  CG   . ASP   A 1 26 ? 10.496  5.329   8.498   1.00 29.85 ? 26  ASP   A CG   1 
ATOM   208  O  OD1  . ASP   A 1 26 ? 9.834   5.710   7.516   1.00 30.25 ? 26  ASP   A OD1  1 
ATOM   209  O  OD2  . ASP   A 1 26 ? 10.299  4.239   9.064   1.00 28.35 ? 26  ASP   A OD2  1 
ATOM   210  N  N    . ASP   A 1 27 ? 10.115  8.894   10.037  1.00 27.97 ? 27  ASP   A N    1 
ATOM   211  C  CA   . ASP   A 1 27 ? 9.909   9.545   11.322  1.00 33.37 ? 27  ASP   A CA   1 
ATOM   212  C  C    . ASP   A 1 27 ? 10.229  8.576   12.456  1.00 31.86 ? 27  ASP   A C    1 
ATOM   213  O  O    . ASP   A 1 27 ? 10.468  7.384   12.249  1.00 32.03 ? 27  ASP   A O    1 
ATOM   214  C  CB   . ASP   A 1 27 ? 8.470   10.049  11.468  1.00 41.03 ? 27  ASP   A CB   1 
ATOM   215  C  CG   . ASP   A 1 27 ? 8.335   11.537  11.187  1.00 52.44 ? 27  ASP   A CG   1 
ATOM   216  O  OD1  . ASP   A 1 27 ? 8.897   12.327  11.981  1.00 53.28 ? 27  ASP   A OD1  1 
ATOM   217  O  OD2  . ASP   A 1 27 ? 7.660   11.924  10.203  1.00 54.26 ? 27  ASP   A OD2  1 
ATOM   218  N  N    . ILE   A 1 28 ? 10.247  9.105   13.673  1.00 30.92 ? 28  ILE   A N    1 
ATOM   219  C  CA   . ILE   A 1 28 ? 10.317  8.290   14.877  1.00 31.98 ? 28  ILE   A CA   1 
ATOM   220  C  C    . ILE   A 1 28 ? 8.995   8.484   15.588  1.00 33.05 ? 28  ILE   A C    1 
ATOM   221  O  O    . ILE   A 1 28 ? 8.609   9.621   15.881  1.00 30.73 ? 28  ILE   A O    1 
ATOM   222  C  CB   . ILE   A 1 28 ? 11.497  8.679   15.777  1.00 31.58 ? 28  ILE   A CB   1 
ATOM   223  C  CG1  . ILE   A 1 28 ? 12.811  8.484   15.034  1.00 35.59 ? 28  ILE   A CG1  1 
ATOM   224  C  CG2  . ILE   A 1 28 ? 11.513  7.834   17.028  1.00 29.59 ? 28  ILE   A CG2  1 
ATOM   225  C  CD1  . ILE   A 1 28 ? 13.449  9.749   14.632  1.00 37.69 ? 28  ILE   A CD1  1 
ATOM   226  N  N    . ALA   A 1 29 ? 8.260   7.399   15.796  1.00 33.24 ? 29  ALA   A N    1 
ATOM   227  C  CA   . ALA   A 1 29 ? 6.979   7.540   16.471  1.00 29.95 ? 29  ALA   A CA   1 
ATOM   228  C  C    . ALA   A 1 29 ? 7.218   7.803   17.949  1.00 30.30 ? 29  ALA   A C    1 
ATOM   229  O  O    . ALA   A 1 29 ? 8.257   7.431   18.502  1.00 29.32 ? 29  ALA   A O    1 
ATOM   230  C  CB   . ALA   A 1 29 ? 6.126   6.284   16.282  1.00 38.97 ? 29  ALA   A CB   1 
ATOM   231  N  N    . ASP   A 1 30 ? 6.259   8.470   18.592  1.00 32.30 ? 30  ASP   A N    1 
ATOM   232  C  CA   . ASP   A 1 30 ? 6.328   8.611   20.040  1.00 33.35 ? 30  ASP   A CA   1 
ATOM   233  C  C    . ASP   A 1 30 ? 6.525   7.248   20.686  1.00 33.02 ? 30  ASP   A C    1 
ATOM   234  O  O    . ASP   A 1 30 ? 5.903   6.262   20.288  1.00 34.24 ? 30  ASP   A O    1 
ATOM   235  C  CB   . ASP   A 1 30 ? 5.061   9.271   20.577  1.00 36.06 ? 30  ASP   A CB   1 
ATOM   236  C  CG   . ASP   A 1 30 ? 4.973   10.738  20.212  1.00 38.32 ? 30  ASP   A CG   1 
ATOM   237  O  OD1  . ASP   A 1 30 ? 6.037   11.367  20.040  1.00 40.20 ? 30  ASP   A OD1  1 
ATOM   238  O  OD2  . ASP   A 1 30 ? 3.843   11.265  20.099  1.00 46.64 ? 30  ASP   A OD2  1 
ATOM   239  N  N    . GLY   A 1 31 ? 7.409   7.191   21.679  1.00 33.24 ? 31  GLY   A N    1 
ATOM   240  C  CA   . GLY   A 1 31 ? 7.681   5.953   22.376  1.00 34.92 ? 31  GLY   A CA   1 
ATOM   241  C  C    . GLY   A 1 31 ? 8.551   4.953   21.635  1.00 32.27 ? 31  GLY   A C    1 
ATOM   242  O  O    . GLY   A 1 31 ? 8.869   3.904   22.205  1.00 33.95 ? 31  GLY   A O    1 
ATOM   243  N  N    . ALA   A 1 32 ? 8.952   5.236   20.402  1.00 31.60 ? 32  ALA   A N    1 
ATOM   244  C  CA   . ALA   A 1 32 ? 9.777   4.310   19.642  1.00 33.84 ? 32  ALA   A CA   1 
ATOM   245  C  C    . ALA   A 1 32 ? 11.259  4.515   19.944  1.00 35.96 ? 32  ALA   A C    1 
ATOM   246  O  O    . ALA   A 1 32 ? 11.686  5.579   20.395  1.00 31.38 ? 32  ALA   A O    1 
ATOM   247  C  CB   . ALA   A 1 32 ? 9.531   4.475   18.139  1.00 31.53 ? 32  ALA   A CB   1 
ATOM   248  N  N    . VAL   A 1 33 ? 12.044  3.470   19.657  1.00 35.82 ? 33  VAL   A N    1 
ATOM   249  C  CA   . VAL   A 1 33 ? 13.498  3.526   19.809  1.00 34.56 ? 33  VAL   A CA   1 
ATOM   250  C  C    . VAL   A 1 33 ? 14.100  4.604   18.920  1.00 30.17 ? 33  VAL   A C    1 
ATOM   251  O  O    . VAL   A 1 33 ? 13.870  4.634   17.704  1.00 28.08 ? 33  VAL   A O    1 
ATOM   252  C  CB   . VAL   A 1 33 ? 14.114  2.159   19.479  1.00 38.28 ? 33  VAL   A CB   1 
ATOM   253  C  CG1  . VAL   A 1 33 ? 15.629  2.214   19.638  1.00 39.07 ? 33  VAL   A CG1  1 
ATOM   254  C  CG2  . VAL   A 1 33 ? 13.506  1.078   20.384  1.00 35.81 ? 33  VAL   A CG2  1 
ATOM   255  N  N    . LYS   A 1 34 ? 14.907  5.457   19.511  1.00 29.71 ? 34  LYS   A N    1 
ATOM   256  C  CA   . LYS   A 1 34 ? 15.534  6.553   18.788  1.00 31.01 ? 34  LYS   A CA   1 
ATOM   257  C  C    . LYS   A 1 34 ? 16.828  6.092   18.133  1.00 30.06 ? 34  LYS   A C    1 
ATOM   258  O  O    . LYS   A 1 34 ? 17.460  5.123   18.577  1.00 30.09 ? 34  LYS   A O    1 
ATOM   259  C  CB   . LYS   A 1 34 ? 15.826  7.713   19.743  1.00 32.42 ? 34  LYS   A CB   1 
ATOM   260  C  CG   . LYS   A 1 34 ? 14.600  8.476   20.213  1.00 36.24 ? 34  LYS   A CG   1 
ATOM   261  C  CD   . LYS   A 1 34 ? 14.986  9.754   20.958  1.00 40.49 ? 34  LYS   A CD   1 
ATOM   262  C  CE   . LYS   A 1 34 ? 15.780  9.446   22.211  1.00 39.60 ? 34  LYS   A CE   1 
ATOM   263  N  NZ   . LYS   A 1 34 ? 15.365  10.284  23.356  1.00 42.78 ? 34  LYS   A NZ   1 
ATOM   264  N  N    . PRO   A 1 35 ? 17.277  6.783   17.092  1.00 26.37 ? 35  PRO   A N    1 
ATOM   265  C  CA   . PRO   A 1 35 ? 18.532  6.395   16.437  1.00 27.56 ? 35  PRO   A CA   1 
ATOM   266  C  C    . PRO   A 1 35 ? 19.722  6.820   17.279  1.00 30.53 ? 35  PRO   A C    1 
ATOM   267  O  O    . PRO   A 1 35 ? 19.582  7.684   18.157  1.00 29.87 ? 35  PRO   A O    1 
ATOM   268  C  CB   . PRO   A 1 35 ? 18.485  7.152   15.098  1.00 30.72 ? 35  PRO   A CB   1 
ATOM   269  C  CG   . PRO   A 1 35 ? 17.636  8.338   15.360  1.00 34.62 ? 35  PRO   A CG   1 
ATOM   270  C  CD   . PRO   A 1 35 ? 16.610  7.907   16.403  1.00 30.71 ? 35  PRO   A CD   1 
ATOM   271  N  N    . PRO   A 1 36 ? 20.902  6.246   17.041  1.00 28.75 ? 36  PRO   A N    1 
ATOM   272  C  CA   . PRO   A 1 36 ? 22.121  6.767   17.663  1.00 31.38 ? 36  PRO   A CA   1 
ATOM   273  C  C    . PRO   A 1 36 ? 22.358  8.192   17.207  1.00 34.37 ? 36  PRO   A C    1 
ATOM   274  O  O    . PRO   A 1 36 ? 21.783  8.613   16.190  1.00 29.01 ? 36  PRO   A O    1 
ATOM   275  C  CB   . PRO   A 1 36 ? 23.217  5.830   17.121  1.00 33.70 ? 36  PRO   A CB   1 
ATOM   276  C  CG   . PRO   A 1 36 ? 22.498  4.640   16.619  1.00 32.97 ? 36  PRO   A CG   1 
ATOM   277  C  CD   . PRO   A 1 36 ? 21.205  5.159   16.104  1.00 28.07 ? 36  PRO   A CD   1 
ATOM   278  N  N    . PRO   A 1 37 ? 23.200  8.958   17.912  1.00 34.62 ? 37  PRO   A N    1 
ATOM   279  C  CA   . PRO   A 1 37 ? 23.548  10.306  17.435  1.00 35.02 ? 37  PRO   A CA   1 
ATOM   280  C  C    . PRO   A 1 37 ? 24.103  10.300  16.018  1.00 33.33 ? 37  PRO   A C    1 
ATOM   281  O  O    . PRO   A 1 37 ? 24.840  9.397   15.614  1.00 33.30 ? 37  PRO   A O    1 
ATOM   282  C  CB   . PRO   A 1 37 ? 24.596  10.800  18.443  1.00 39.27 ? 37  PRO   A CB   1 
ATOM   283  C  CG   . PRO   A 1 37 ? 24.689  9.784   19.503  1.00 40.91 ? 37  PRO   A CG   1 
ATOM   284  C  CD   . PRO   A 1 37 ? 23.912  8.573   19.142  1.00 37.77 ? 37  PRO   A CD   1 
ATOM   285  N  N    . ASN   A 1 38 ? 23.724  11.331  15.261  1.00 35.04 ? 38  ASN   A N    1 
ATOM   286  C  CA   . ASN   A 1 38 ? 24.167  11.543  13.887  1.00 32.83 ? 38  ASN   A CA   1 
ATOM   287  C  C    . ASN   A 1 38 ? 23.754  10.422  12.947  1.00 33.20 ? 38  ASN   A C    1 
ATOM   288  O  O    . ASN   A 1 38 ? 24.314  10.292  11.848  1.00 28.56 ? 38  ASN   A O    1 
ATOM   289  C  CB   . ASN   A 1 38 ? 25.679  11.747  13.828  1.00 39.41 ? 38  ASN   A CB   1 
ATOM   290  C  CG   . ASN   A 1 38 ? 26.130  12.843  14.745  1.00 46.00 ? 38  ASN   A CG   1 
ATOM   291  O  OD1  . ASN   A 1 38 ? 26.351  12.625  15.940  1.00 49.57 ? 38  ASN   A OD1  1 
ATOM   292  N  ND2  . ASN   A 1 38 ? 26.237  14.046  14.206  1.00 39.50 ? 38  ASN   A ND2  1 
ATOM   293  N  N    . LYS   A 1 39 ? 22.786  9.594   13.334  1.00 27.39 ? 39  LYS   A N    1 
ATOM   294  C  CA   . LYS   A 1 39 ? 22.235  8.627   12.399  1.00 25.40 ? 39  LYS   A CA   1 
ATOM   295  C  C    . LYS   A 1 39 ? 20.748  8.895   12.204  1.00 24.11 ? 39  LYS   A C    1 
ATOM   296  O  O    . LYS   A 1 39 ? 20.098  9.552   13.022  1.00 24.59 ? 39  LYS   A O    1 
ATOM   297  C  CB   . LYS   A 1 39 ? 22.471  7.180   12.874  1.00 26.12 ? 39  LYS   A CB   1 
ATOM   298  C  CG   . LYS   A 1 39 ? 23.947  6.850   13.161  1.00 29.96 ? 39  LYS   A CG   1 
ATOM   299  C  CD   . LYS   A 1 39 ? 24.412  5.577   12.454  1.00 33.64 ? 39  LYS   A CD   1 
ATOM   300  C  CE   . LYS   A 1 39 ? 25.934  5.377   12.579  1.00 34.22 ? 39  LYS   A CE   1 
ATOM   301  N  NZ   . LYS   A 1 39 ? 26.698  6.650   12.314  1.00 34.22 ? 39  LYS   A NZ   1 
ATOM   302  N  N    . TYR   A 1 40 ? 20.224  8.387   11.095  1.00 17.70 ? 40  TYR   A N    1 
ATOM   303  C  CA   . TYR   A 1 40 ? 18.842  8.537   10.694  1.00 22.23 ? 40  TYR   A CA   1 
ATOM   304  C  C    . TYR   A 1 40 ? 18.148  7.183   10.626  1.00 18.65 ? 40  TYR   A C    1 
ATOM   305  O  O    . TYR   A 1 40 ? 18.767  6.193   10.243  1.00 20.90 ? 40  TYR   A O    1 
ATOM   306  C  CB   . TYR   A 1 40 ? 18.761  9.219   9.320   1.00 17.19 ? 40  TYR   A CB   1 
ATOM   307  C  CG   . TYR   A 1 40 ? 19.277  10.637  9.398   1.00 17.34 ? 40  TYR   A CG   1 
ATOM   308  C  CD1  . TYR   A 1 40 ? 20.628  10.909  9.280   1.00 22.50 ? 40  TYR   A CD1  1 
ATOM   309  C  CD2  . TYR   A 1 40 ? 18.414  11.692  9.652   1.00 25.72 ? 40  TYR   A CD2  1 
ATOM   310  C  CE1  . TYR   A 1 40 ? 21.100  12.194  9.381   1.00 24.55 ? 40  TYR   A CE1  1 
ATOM   311  C  CE2  . TYR   A 1 40 ? 18.872  12.979  9.756   1.00 25.17 ? 40  TYR   A CE2  1 
ATOM   312  C  CZ   . TYR   A 1 40 ? 20.218  13.226  9.614   1.00 28.29 ? 40  TYR   A CZ   1 
ATOM   313  O  OH   . TYR   A 1 40 ? 20.705  14.510  9.739   1.00 31.16 ? 40  TYR   A OH   1 
ATOM   314  N  N    . PRO   A 1 41 ? 16.861  7.115   10.976  1.00 22.25 ? 41  PRO   A N    1 
ATOM   315  C  CA   . PRO   A 1 41 ? 16.087  5.881   10.761  1.00 19.56 ? 41  PRO   A CA   1 
ATOM   316  C  C    . PRO   A 1 41 ? 15.757  5.739   9.282   1.00 25.41 ? 41  PRO   A C    1 
ATOM   317  O  O    . PRO   A 1 41 ? 15.076  6.597   8.706   1.00 23.86 ? 41  PRO   A O    1 
ATOM   318  C  CB   . PRO   A 1 41 ? 14.823  6.102   11.592  1.00 18.28 ? 41  PRO   A CB   1 
ATOM   319  C  CG   . PRO   A 1 41 ? 14.660  7.604   11.648  1.00 20.99 ? 41  PRO   A CG   1 
ATOM   320  C  CD   . PRO   A 1 41 ? 16.024  8.230   11.458  1.00 20.84 ? 41  PRO   A CD   1 
ATOM   321  N  N    . ILE   A 1 42 ? 16.276  4.680   8.659   1.00 20.18 ? 42  ILE   A N    1 
ATOM   322  C  CA   . ILE   A 1 42 ? 16.110  4.440   7.227   1.00 21.76 ? 42  ILE   A CA   1 
ATOM   323  C  C    . ILE   A 1 42 ? 15.112  3.308   7.031   1.00 22.48 ? 42  ILE   A C    1 
ATOM   324  O  O    . ILE   A 1 42 ? 15.299  2.209   7.561   1.00 25.93 ? 42  ILE   A O    1 
ATOM   325  C  CB   . ILE   A 1 42 ? 17.441  4.071   6.549   1.00 19.01 ? 42  ILE   A CB   1 
ATOM   326  C  CG1  . ILE   A 1 42 ? 18.491  5.129   6.832   1.00 14.52 ? 42  ILE   A CG1  1 
ATOM   327  C  CG2  . ILE   A 1 42 ? 17.218  3.904   5.055   1.00 16.85 ? 42  ILE   A CG2  1 
ATOM   328  C  CD1  . ILE   A 1 42 ? 17.982  6.560   6.583   1.00 14.28 ? 42  ILE   A CD1  1 
ATOM   329  N  N    . PHE   A 1 43 ? 14.072  3.560   6.257   1.00 17.20 ? 43  PHE   A N    1 
ATOM   330  C  CA   . PHE   A 1 43 ? 13.127  2.516   5.873   1.00 20.97 ? 43  PHE   A CA   1 
ATOM   331  C  C    . PHE   A 1 43 ? 13.420  2.090   4.438   1.00 19.57 ? 43  PHE   A C    1 
ATOM   332  O  O    . PHE   A 1 43 ? 13.342  2.912   3.529   1.00 18.99 ? 43  PHE   A O    1 
ATOM   333  C  CB   . PHE   A 1 43 ? 11.693  3.033   5.991   1.00 18.82 ? 43  PHE   A CB   1 
ATOM   334  C  CG   . PHE   A 1 43 ? 10.649  2.037   5.570   1.00 22.69 ? 43  PHE   A CG   1 
ATOM   335  C  CD1  . PHE   A 1 43 ? 10.172  1.076   6.466   1.00 22.64 ? 43  PHE   A CD1  1 
ATOM   336  C  CD2  . PHE   A 1 43 ? 10.129  2.060   4.281   1.00 22.79 ? 43  PHE   A CD2  1 
ATOM   337  C  CE1  . PHE   A 1 43 ? 9.222   0.152   6.067   1.00 24.79 ? 43  PHE   A CE1  1 
ATOM   338  C  CE2  . PHE   A 1 43 ? 9.166   1.142   3.889   1.00 27.07 ? 43  PHE   A CE2  1 
ATOM   339  C  CZ   . PHE   A 1 43 ? 8.708   0.189   4.780   1.00 23.64 ? 43  PHE   A CZ   1 
ATOM   340  N  N    . PHE   A 1 44 ? 13.725  0.812   4.236   1.00 17.17 ? 44  PHE   A N    1 
ATOM   341  C  CA   . PHE   A 1 44 ? 14.083  0.310   2.917   1.00 19.44 ? 44  PHE   A CA   1 
ATOM   342  C  C    . PHE   A 1 44 ? 12.835  -0.176  2.211   1.00 19.33 ? 44  PHE   A C    1 
ATOM   343  O  O    . PHE   A 1 44 ? 12.130  -1.054  2.723   1.00 20.04 ? 44  PHE   A O    1 
ATOM   344  C  CB   . PHE   A 1 44 ? 15.088  -0.825  3.015   1.00 20.93 ? 44  PHE   A CB   1 
ATOM   345  C  CG   . PHE   A 1 44 ? 16.417  -0.394  3.538   1.00 24.01 ? 44  PHE   A CG   1 
ATOM   346  C  CD1  . PHE   A 1 44 ? 16.651  -0.359  4.897   1.00 26.77 ? 44  PHE   A CD1  1 
ATOM   347  C  CD2  . PHE   A 1 44 ? 17.418  -0.006  2.677   1.00 21.96 ? 44  PHE   A CD2  1 
ATOM   348  C  CE1  . PHE   A 1 44 ? 17.872  0.073   5.385   1.00 31.87 ? 44  PHE   A CE1  1 
ATOM   349  C  CE2  . PHE   A 1 44 ? 18.640  0.399   3.158   1.00 21.83 ? 44  PHE   A CE2  1 
ATOM   350  C  CZ   . PHE   A 1 44 ? 18.870  0.445   4.500   1.00 25.29 ? 44  PHE   A CZ   1 
ATOM   351  N  N    . PHE   A 1 45 ? 12.576  0.373   1.035   1.00 20.36 ? 45  PHE   A N    1 
ATOM   352  C  CA   . PHE   A 1 45 ? 11.427  -0.092  0.280   1.00 19.30 ? 45  PHE   A CA   1 
ATOM   353  C  C    . PHE   A 1 45 ? 11.667  -1.526  -0.178  1.00 18.99 ? 45  PHE   A C    1 
ATOM   354  O  O    . PHE   A 1 45 ? 12.811  -1.978  -0.307  1.00 20.69 ? 45  PHE   A O    1 
ATOM   355  C  CB   . PHE   A 1 45 ? 11.174  0.820   -0.919  1.00 18.26 ? 45  PHE   A CB   1 
ATOM   356  C  CG   . PHE   A 1 45 ? 10.727  2.221   -0.547  1.00 18.28 ? 45  PHE   A CG   1 
ATOM   357  C  CD1  . PHE   A 1 45 ? 9.463   2.444   -0.015  1.00 15.44 ? 45  PHE   A CD1  1 
ATOM   358  C  CD2  . PHE   A 1 45 ? 11.559  3.298   -0.735  1.00 18.25 ? 45  PHE   A CD2  1 
ATOM   359  C  CE1  . PHE   A 1 45 ? 9.038   3.704   0.329   1.00 20.66 ? 45  PHE   A CE1  1 
ATOM   360  C  CE2  . PHE   A 1 45 ? 11.134  4.589   -0.388  1.00 17.44 ? 45  PHE   A CE2  1 
ATOM   361  C  CZ   . PHE   A 1 45 ? 9.847   4.782   0.129   1.00 16.28 ? 45  PHE   A CZ   1 
ATOM   362  N  N    . GLY   A 1 46 ? 10.570  -2.238  -0.431  1.00 21.32 ? 46  GLY   A N    1 
ATOM   363  C  CA   . GLY   A 1 46 ? 10.631  -3.611  -0.916  1.00 21.65 ? 46  GLY   A CA   1 
ATOM   364  C  C    . GLY   A 1 46 ? 10.805  -4.597  0.221   1.00 26.91 ? 46  GLY   A C    1 
ATOM   365  O  O    . GLY   A 1 46 ? 9.931   -5.421  0.479   1.00 25.26 ? 46  GLY   A O    1 
ATOM   366  N  N    . THR   A 1 47 ? 11.920  -4.516  0.934   1.00 24.23 ? 47  THR   A N    1 
ATOM   367  C  CA   . THR   A 1 47 ? 12.098  -5.393  2.078   1.00 25.65 ? 47  THR   A CA   1 
ATOM   368  C  C    . THR   A 1 47 ? 11.376  -4.892  3.317   1.00 27.26 ? 47  THR   A C    1 
ATOM   369  O  O    . THR   A 1 47 ? 11.076  -5.690  4.214   1.00 25.55 ? 47  THR   A O    1 
ATOM   370  C  CB   . THR   A 1 47 ? 13.567  -5.505  2.413   1.00 30.58 ? 47  THR   A CB   1 
ATOM   371  O  OG1  . THR   A 1 47 ? 13.966  -4.244  2.927   1.00 24.63 ? 47  THR   A OG1  1 
ATOM   372  C  CG2  . THR   A 1 47 ? 14.378  -5.822  1.164   1.00 30.55 ? 47  THR   A CG2  1 
ATOM   373  N  N    . HIS   A 1 48 ? 11.130  -3.592  3.397   1.00 21.68 ? 48  HIS   A N    1 
ATOM   374  C  CA   . HIS   A 1 48 ? 10.458  -2.946  4.527   1.00 20.86 ? 48  HIS   A CA   1 
ATOM   375  C  C    . HIS   A 1 48 ? 11.244  -3.078  5.816   1.00 28.00 ? 48  HIS   A C    1 
ATOM   376  O  O    . HIS   A 1 48 ? 10.673  -3.002  6.906   1.00 28.38 ? 48  HIS   A O    1 
ATOM   377  C  CB   . HIS   A 1 48 ? 9.039   -3.489  4.689   1.00 22.18 ? 48  HIS   A CB   1 
ATOM   378  C  CG   . HIS   A 1 48 ? 8.275   -3.515  3.403   1.00 22.97 ? 48  HIS   A CG   1 
ATOM   379  N  ND1  . HIS   A 1 48 ? 7.376   -4.507  3.087   1.00 29.88 ? 48  HIS   A ND1  1 
ATOM   380  C  CD2  . HIS   A 1 48 ? 8.291   -2.671  2.347   1.00 25.78 ? 48  HIS   A CD2  1 
ATOM   381  C  CE1  . HIS   A 1 48 ? 6.862   -4.267  1.895   1.00 37.63 ? 48  HIS   A CE1  1 
ATOM   382  N  NE2  . HIS   A 1 48 ? 7.402   -3.159  1.422   1.00 27.86 ? 48  HIS   A NE2  1 
ATOM   383  N  N    . GLU   A 1 49 ? 12.555  -3.254  5.718   1.00 24.26 ? 49  GLU   A N    1 
ATOM   384  C  CA   . GLU   A 1 49 ? 13.371  -3.311  6.914   1.00 26.44 ? 49  GLU   A CA   1 
ATOM   385  C  C    . GLU   A 1 49 ? 13.873  -1.909  7.261   1.00 28.24 ? 49  GLU   A C    1 
ATOM   386  O  O    . GLU   A 1 49 ? 13.813  -0.974  6.454   1.00 23.94 ? 49  GLU   A O    1 
ATOM   387  C  CB   . GLU   A 1 49 ? 14.520  -4.318  6.727   1.00 23.29 ? 49  GLU   A CB   1 
ATOM   388  C  CG   . GLU   A 1 49 ? 14.000  -5.764  6.793   1.00 38.68 ? 49  GLU   A CG   1 
ATOM   389  C  CD   . GLU   A 1 49 ? 14.939  -6.767  6.152   1.00 45.86 ? 49  GLU   A CD   1 
ATOM   390  O  OE1  . GLU   A 1 49 ? 16.156  -6.472  6.095   1.00 48.68 ? 49  GLU   A OE1  1 
ATOM   391  O  OE2  . GLU   A 1 49 ? 14.461  -7.847  5.714   1.00 46.76 ? 49  GLU   A OE2  1 
ATOM   392  N  N    . THR   A 1 50 ? 14.304  -1.752  8.503   1.00 22.71 ? 50  THR   A N    1 
ATOM   393  C  CA   . THR   A 1 50 ? 14.791  -0.474  8.972   1.00 24.29 ? 50  THR   A CA   1 
ATOM   394  C  C    . THR   A 1 50 ? 16.216  -0.635  9.469   1.00 31.00 ? 50  THR   A C    1 
ATOM   395  O  O    . THR   A 1 50 ? 16.571  -1.664  10.060  1.00 29.43 ? 50  THR   A O    1 
ATOM   396  C  CB   . THR   A 1 50 ? 13.898  0.069   10.071  1.00 30.10 ? 50  THR   A CB   1 
ATOM   397  O  OG1  . THR   A 1 50 ? 13.696  -0.957  11.043  1.00 47.64 ? 50  THR   A OG1  1 
ATOM   398  C  CG2  . THR   A 1 50 ? 12.566  0.431   9.512   1.00 26.94 ? 50  THR   A CG2  1 
ATOM   399  N  N    . ALA   A 1 51 ? 17.033  0.380   9.226   1.00 27.77 ? 51  ALA   A N    1 
ATOM   400  C  CA   . ALA   A 1 51 ? 18.365  0.411   9.807   1.00 23.13 ? 51  ALA   A CA   1 
ATOM   401  C  C    . ALA   A 1 51 ? 18.726  1.864   10.056  1.00 25.60 ? 51  ALA   A C    1 
ATOM   402  O  O    . ALA   A 1 51 ? 18.079  2.778   9.542   1.00 28.50 ? 51  ALA   A O    1 
ATOM   403  C  CB   . ALA   A 1 51 ? 19.391  -0.299  8.909   1.00 29.90 ? 51  ALA   A CB   1 
ATOM   404  N  N    . PHE   A 1 52 ? 19.769  2.073   10.855  1.00 23.56 ? 52  PHE   A N    1 
ATOM   405  C  CA   . PHE   A 1 52 ? 20.207  3.412   11.227  1.00 21.84 ? 52  PHE   A CA   1 
ATOM   406  C  C    . PHE   A 1 52 ? 21.450  3.750   10.425  1.00 25.51 ? 52  PHE   A C    1 
ATOM   407  O  O    . PHE   A 1 52 ? 22.459  3.041   10.517  1.00 28.53 ? 52  PHE   A O    1 
ATOM   408  C  CB   . PHE   A 1 52 ? 20.516  3.483   12.723  1.00 28.27 ? 52  PHE   A CB   1 
ATOM   409  C  CG   . PHE   A 1 52 ? 19.322  3.280   13.595  1.00 26.57 ? 52  PHE   A CG   1 
ATOM   410  C  CD1  . PHE   A 1 52 ? 18.191  4.047   13.419  1.00 23.67 ? 52  PHE   A CD1  1 
ATOM   411  C  CD2  . PHE   A 1 52 ? 19.327  2.316   14.590  1.00 35.10 ? 52  PHE   A CD2  1 
ATOM   412  C  CE1  . PHE   A 1 52 ? 17.084  3.872   14.221  1.00 35.26 ? 52  PHE   A CE1  1 
ATOM   413  C  CE2  . PHE   A 1 52 ? 18.219  2.140   15.397  1.00 38.52 ? 52  PHE   A CE2  1 
ATOM   414  C  CZ   . PHE   A 1 52 ? 17.099  2.917   15.209  1.00 32.13 ? 52  PHE   A CZ   1 
ATOM   415  N  N    . LEU   A 1 53 ? 21.401  4.836   9.663   1.00 18.02 ? 53  LEU   A N    1 
ATOM   416  C  CA   . LEU   A 1 53 ? 22.527  5.148   8.799   1.00 21.83 ? 53  LEU   A CA   1 
ATOM   417  C  C    . LEU   A 1 53 ? 22.908  6.616   8.923   1.00 21.28 ? 53  LEU   A C    1 
ATOM   418  O  O    . LEU   A 1 53 ? 22.063  7.464   9.215   1.00 21.04 ? 53  LEU   A O    1 
ATOM   419  C  CB   . LEU   A 1 53 ? 22.192  4.826   7.352   1.00 18.36 ? 53  LEU   A CB   1 
ATOM   420  C  CG   . LEU   A 1 53 ? 22.149  3.359   6.924   1.00 25.13 ? 53  LEU   A CG   1 
ATOM   421  C  CD1  . LEU   A 1 53 ? 21.810  3.309   5.436   1.00 22.38 ? 53  LEU   A CD1  1 
ATOM   422  C  CD2  . LEU   A 1 53 ? 23.455  2.673   7.203   1.00 25.39 ? 53  LEU   A CD2  1 
ATOM   423  N  N    . GLY   A 1 54 ? 24.187  6.911   8.669   1.00 17.71 ? 54  GLY   A N    1 
ATOM   424  C  CA   . GLY   A 1 54 ? 24.656  8.286   8.615   1.00 24.11 ? 54  GLY   A CA   1 
ATOM   425  C  C    . GLY   A 1 54 ? 24.623  8.819   7.185   1.00 20.58 ? 54  GLY   A C    1 
ATOM   426  O  O    . GLY   A 1 54 ? 24.507  8.043   6.235   1.00 16.96 ? 54  GLY   A O    1 
ATOM   427  N  N    . PRO   A 1 55 ? 24.738  10.150  7.016   1.00 19.65 ? 55  PRO   A N    1 
ATOM   428  C  CA   . PRO   A 1 55 ? 24.661  10.752  5.671   1.00 19.45 ? 55  PRO   A CA   1 
ATOM   429  C  C    . PRO   A 1 55 ? 25.658  10.213  4.662   1.00 20.35 ? 55  PRO   A C    1 
ATOM   430  O  O    . PRO   A 1 55 ? 25.367  10.260  3.464   1.00 18.86 ? 55  PRO   A O    1 
ATOM   431  C  CB   . PRO   A 1 55 ? 24.912  12.244  5.952   1.00 18.69 ? 55  PRO   A CB   1 
ATOM   432  C  CG   . PRO   A 1 55 ? 24.309  12.437  7.308   1.00 19.94 ? 55  PRO   A CG   1 
ATOM   433  C  CD   . PRO   A 1 55 ? 24.695  11.184  8.069   1.00 26.88 ? 55  PRO   A CD   1 
ATOM   434  N  N    . LYS   A 1 56 ? 26.827  9.723   5.082   1.00 18.12 ? 56  LYS   A N    1 
ATOM   435  C  CA   . LYS   A 1 56 ? 27.774  9.185   4.103   1.00 19.56 ? 56  LYS   A CA   1 
ATOM   436  C  C    . LYS   A 1 56 ? 27.171  8.048   3.281   1.00 19.77 ? 56  LYS   A C    1 
ATOM   437  O  O    . LYS   A 1 56 ? 27.682  7.727   2.198   1.00 20.44 ? 56  LYS   A O    1 
ATOM   438  C  CB   . LYS   A 1 56 ? 29.056  8.685   4.778   1.00 21.58 ? 56  LYS   A CB   1 
ATOM   439  C  CG   . LYS   A 1 56 ? 28.939  7.284   5.438   1.00 25.94 ? 56  LYS   A CG   1 
ATOM   440  C  CD   . LYS   A 1 56 ? 30.197  6.927   6.255   1.00 33.17 ? 56  LYS   A CD   1 
ATOM   441  C  CE   . LYS   A 1 56 ? 30.059  5.581   6.981   1.00 34.14 ? 56  LYS   A CE   1 
ATOM   442  N  NZ   . LYS   A 1 56 ? 29.721  4.450   6.065   1.00 31.42 ? 56  LYS   A NZ   1 
ATOM   443  N  N    . ASP   A 1 57 ? 26.097  7.440   3.760   1.00 18.97 ? 57  ASP   A N    1 
ATOM   444  C  CA   . ASP   A 1 57 ? 25.482  6.311   3.086   1.00 20.61 ? 57  ASP   A CA   1 
ATOM   445  C  C    . ASP   A 1 57 ? 24.144  6.675   2.453   1.00 17.59 ? 57  ASP   A C    1 
ATOM   446  O  O    . ASP   A 1 57 ? 23.425  5.789   1.989   1.00 18.90 ? 57  ASP   A O    1 
ATOM   447  C  CB   . ASP   A 1 57 ? 25.325  5.151   4.074   1.00 18.84 ? 57  ASP   A CB   1 
ATOM   448  C  CG   . ASP   A 1 57 ? 26.650  4.441   4.350   1.00 29.58 ? 57  ASP   A CG   1 
ATOM   449  O  OD1  . ASP   A 1 57 ? 27.480  4.318   3.413   1.00 26.25 ? 57  ASP   A OD1  1 
ATOM   450  O  OD2  . ASP   A 1 57 ? 26.874  4.030   5.505   1.00 23.76 ? 57  ASP   A OD2  1 
ATOM   451  N  N    . LEU   A 1 58 ? 23.807  7.953   2.392   1.00 14.47 ? 58  LEU   A N    1 
ATOM   452  C  CA   . LEU   A 1 58 ? 22.496  8.400   1.941   1.00 13.64 ? 58  LEU   A CA   1 
ATOM   453  C  C    . LEU   A 1 58 ? 22.662  9.257   0.683   1.00 19.21 ? 58  LEU   A C    1 
ATOM   454  O  O    . LEU   A 1 58 ? 23.398  10.253  0.692   1.00 15.33 ? 58  LEU   A O    1 
ATOM   455  C  CB   . LEU   A 1 58 ? 21.791  9.167   3.059   1.00 17.16 ? 58  LEU   A CB   1 
ATOM   456  C  CG   . LEU   A 1 58 ? 21.641  8.358   4.352   1.00 19.26 ? 58  LEU   A CG   1 
ATOM   457  C  CD1  . LEU   A 1 58 ? 21.038  9.243   5.410   1.00 20.13 ? 58  LEU   A CD1  1 
ATOM   458  C  CD2  . LEU   A 1 58 ? 20.756  7.117   4.158   1.00 16.51 ? 58  LEU   A CD2  1 
ATOM   459  N  N    . PHE   A 1 59 ? 21.987  8.867   -0.400  1.00 16.38 ? 59  PHE   A N    1 
ATOM   460  C  CA   . PHE   A 1 59 ? 22.123  9.509   -1.696  1.00 16.61 ? 59  PHE   A CA   1 
ATOM   461  C  C    . PHE   A 1 59 ? 20.762  10.038  -2.139  1.00 19.58 ? 59  PHE   A C    1 
ATOM   462  O  O    . PHE   A 1 59 ? 19.807  9.255   -2.175  1.00 20.48 ? 59  PHE   A O    1 
ATOM   463  C  CB   . PHE   A 1 59 ? 22.654  8.487   -2.737  1.00 19.87 ? 59  PHE   A CB   1 
ATOM   464  C  CG   . PHE   A 1 59 ? 24.068  8.027   -2.473  1.00 18.72 ? 59  PHE   A CG   1 
ATOM   465  C  CD1  . PHE   A 1 59 ? 24.335  7.080   -1.506  1.00 17.26 ? 59  PHE   A CD1  1 
ATOM   466  C  CD2  . PHE   A 1 59 ? 25.124  8.553   -3.192  1.00 18.55 ? 59  PHE   A CD2  1 
ATOM   467  C  CE1  . PHE   A 1 59 ? 25.632  6.680   -1.258  1.00 18.20 ? 59  PHE   A CE1  1 
ATOM   468  C  CE2  . PHE   A 1 59 ? 26.418  8.150   -2.943  1.00 21.82 ? 59  PHE   A CE2  1 
ATOM   469  C  CZ   . PHE   A 1 59 ? 26.665  7.212   -1.969  1.00 21.38 ? 59  PHE   A CZ   1 
ATOM   470  N  N    . PRO   A 1 60 ? 20.612  11.322  -2.475  1.00 23.39 ? 60  PRO   A N    1 
ATOM   471  C  CA   . PRO   A 1 60 ? 19.279  11.818  -2.862  1.00 19.83 ? 60  PRO   A CA   1 
ATOM   472  C  C    . PRO   A 1 60 ? 18.698  11.061  -4.051  1.00 20.77 ? 60  PRO   A C    1 
ATOM   473  O  O    . PRO   A 1 60 ? 19.392  10.757  -5.021  1.00 26.22 ? 60  PRO   A O    1 
ATOM   474  C  CB   . PRO   A 1 60 ? 19.524  13.296  -3.194  1.00 27.31 ? 60  PRO   A CB   1 
ATOM   475  C  CG   . PRO   A 1 60 ? 21.002  13.405  -3.439  1.00 39.08 ? 60  PRO   A CG   1 
ATOM   476  C  CD   . PRO   A 1 60 ? 21.606  12.412  -2.473  1.00 27.89 ? 60  PRO   A CD   1 
ATOM   477  N  N    . TYR   A 1 61 ? 17.399  10.749  -3.959  1.00 17.75 ? 61  TYR   A N    1 
ATOM   478  C  CA   . TYR   A 1 61 ? 16.779  9.854   -4.934  1.00 24.45 ? 61  TYR   A CA   1 
ATOM   479  C  C    . TYR   A 1 61 ? 16.767  10.477  -6.325  1.00 23.36 ? 61  TYR   A C    1 
ATOM   480  O  O    . TYR   A 1 61 ? 17.182  9.848   -7.310  1.00 24.98 ? 61  TYR   A O    1 
ATOM   481  C  CB   . TYR   A 1 61 ? 15.350  9.496   -4.495  1.00 19.87 ? 61  TYR   A CB   1 
ATOM   482  C  CG   . TYR   A 1 61 ? 14.538  8.722   -5.537  1.00 18.86 ? 61  TYR   A CG   1 
ATOM   483  C  CD1  . TYR   A 1 61 ? 14.843  7.401   -5.842  1.00 24.88 ? 61  TYR   A CD1  1 
ATOM   484  C  CD2  . TYR   A 1 61 ? 13.449  9.295   -6.163  1.00 26.14 ? 61  TYR   A CD2  1 
ATOM   485  C  CE1  . TYR   A 1 61 ? 14.111  6.693   -6.778  1.00 22.21 ? 61  TYR   A CE1  1 
ATOM   486  C  CE2  . TYR   A 1 61 ? 12.701  8.593   -7.079  1.00 27.42 ? 61  TYR   A CE2  1 
ATOM   487  C  CZ   . TYR   A 1 61 ? 13.031  7.295   -7.387  1.00 24.06 ? 61  TYR   A CZ   1 
ATOM   488  O  OH   . TYR   A 1 61 ? 12.280  6.596   -8.318  1.00 26.45 ? 61  TYR   A OH   1 
ATOM   489  N  N    . ASP   A 1 62 ? 16.302  11.717  -6.429  1.00 23.89 ? 62  ASP   A N    1 
ATOM   490  C  CA   . ASP   A 1 62 ? 16.110  12.285  -7.759  1.00 27.24 ? 62  ASP   A CA   1 
ATOM   491  C  C    . ASP   A 1 62 ? 17.437  12.580  -8.444  1.00 31.06 ? 62  ASP   A C    1 
ATOM   492  O  O    . ASP   A 1 62 ? 17.519  12.510  -9.671  1.00 35.49 ? 62  ASP   A O    1 
ATOM   493  C  CB   . ASP   A 1 62 ? 15.237  13.534  -7.685  1.00 34.63 ? 62  ASP   A CB   1 
ATOM   494  C  CG   . ASP   A 1 62 ? 15.786  14.572  -6.732  1.00 46.77 ? 62  ASP   A CG   1 
ATOM   495  O  OD1  . ASP   A 1 62 ? 16.850  14.326  -6.111  1.00 42.58 ? 62  ASP   A OD1  1 
ATOM   496  O  OD2  . ASP   A 1 62 ? 15.160  15.651  -6.624  1.00 55.58 ? 62  ASP   A OD2  1 
ATOM   497  N  N    . LYS   A 1 63 ? 18.488  12.893  -7.682  1.00 25.82 ? 63  LYS   A N    1 
ATOM   498  C  CA   . LYS   A 1 63 ? 19.793  13.099  -8.305  1.00 32.60 ? 63  LYS   A CA   1 
ATOM   499  C  C    . LYS   A 1 63 ? 20.396  11.788  -8.794  1.00 24.87 ? 63  LYS   A C    1 
ATOM   500  O  O    . LYS   A 1 63 ? 21.083  11.774  -9.822  1.00 25.71 ? 63  LYS   A O    1 
ATOM   501  C  CB   . LYS   A 1 63 ? 20.743  13.778  -7.318  1.00 37.24 ? 63  LYS   A CB   1 
ATOM   502  C  CG   . LYS   A 1 63 ? 22.209  13.864  -7.769  1.00 38.74 ? 63  LYS   A CG   1 
ATOM   503  C  CD   . LYS   A 1 63 ? 23.105  14.231  -6.584  1.00 36.47 ? 63  LYS   A CD   1 
ATOM   504  C  CE   . LYS   A 1 63 ? 24.442  14.801  -7.004  1.00 33.87 ? 63  LYS   A CE   1 
ATOM   505  N  NZ   . LYS   A 1 63 ? 25.393  13.724  -7.362  1.00 38.79 ? 63  LYS   A NZ   1 
ATOM   506  N  N    . CYS   A 1 64 ? 20.149  10.682  -8.089  1.00 24.63 ? 64  CYS   A N    1 
ATOM   507  C  CA   . CYS   A 1 64 ? 20.873  9.440   -8.329  1.00 26.12 ? 64  CYS   A CA   1 
ATOM   508  C  C    . CYS   A 1 64 ? 20.024  8.305   -8.892  1.00 30.07 ? 64  CYS   A C    1 
ATOM   509  O  O    . CYS   A 1 64 ? 20.544  7.196   -9.050  1.00 24.92 ? 64  CYS   A O    1 
ATOM   510  C  CB   . CYS   A 1 64 ? 21.535  8.962   -7.046  1.00 26.07 ? 64  CYS   A CB   1 
ATOM   511  S  SG   . CYS   A 1 64 ? 22.532  10.209  -6.245  1.00 29.71 ? 64  CYS   A SG   1 
ATOM   512  N  N    . LYS   A 1 65 ? 18.748  8.537   -9.219  1.00 28.69 ? 65  LYS   A N    1 
ATOM   513  C  CA   . LYS   A 1 65 ? 17.942  7.420   -9.704  1.00 27.29 ? 65  LYS   A CA   1 
ATOM   514  C  C    . LYS   A 1 65 ? 18.376  6.956   -11.087 1.00 32.50 ? 65  LYS   A C    1 
ATOM   515  O  O    . LYS   A 1 65 ? 18.183  5.783   -11.427 1.00 30.76 ? 65  LYS   A O    1 
ATOM   516  C  CB   . LYS   A 1 65 ? 16.444  7.760   -9.699  1.00 29.49 ? 65  LYS   A CB   1 
ATOM   517  C  CG   . LYS   A 1 65 ? 16.010  9.089   -10.302 1.00 31.95 ? 65  LYS   A CG   1 
ATOM   518  C  CD   . LYS   A 1 65 ? 14.506  9.008   -10.646 1.00 38.89 ? 65  LYS   A CD   1 
ATOM   519  C  CE   . LYS   A 1 65 ? 14.010  10.188  -11.488 1.00 49.88 ? 65  LYS   A CE   1 
ATOM   520  N  NZ   . LYS   A 1 65 ? 14.031  11.499  -10.763 1.00 52.92 ? 65  LYS   A NZ   1 
ATOM   521  N  N    . ASP   A 1 66 ? 18.966  7.835   -11.901 1.00 31.76 ? 66  ASP   A N    1 
ATOM   522  C  CA   . ASP   A 1 66 ? 19.399  7.371   -13.213 1.00 34.73 ? 66  ASP   A CA   1 
ATOM   523  C  C    . ASP   A 1 66 ? 20.524  6.353   -13.084 1.00 37.27 ? 66  ASP   A C    1 
ATOM   524  O  O    . ASP   A 1 66 ? 20.664  5.469   -13.932 1.00 37.69 ? 66  ASP   A O    1 
ATOM   525  C  CB   . ASP   A 1 66 ? 19.846  8.546   -14.078 1.00 37.52 ? 66  ASP   A CB   1 
ATOM   526  C  CG   . ASP   A 1 66 ? 20.582  8.099   -15.329 1.00 54.49 ? 66  ASP   A CG   1 
ATOM   527  O  OD1  . ASP   A 1 66 ? 19.919  7.538   -16.233 1.00 60.58 ? 66  ASP   A OD1  1 
ATOM   528  O  OD2  . ASP   A 1 66 ? 21.815  8.298   -15.412 1.00 64.37 ? 66  ASP   A OD2  1 
ATOM   529  N  N    . LYS   A 1 67 ? 21.320  6.447   -12.022 1.00 33.58 ? 67  LYS   A N    1 
ATOM   530  C  CA   . LYS   A 1 67 ? 22.428  5.532   -11.817 1.00 34.54 ? 67  LYS   A CA   1 
ATOM   531  C  C    . LYS   A 1 67 ? 21.994  4.296   -11.038 1.00 31.97 ? 67  LYS   A C    1 
ATOM   532  O  O    . LYS   A 1 67 ? 22.326  3.171   -11.417 1.00 32.11 ? 67  LYS   A O    1 
ATOM   533  C  CB   . LYS   A 1 67 ? 23.567  6.254   -11.088 1.00 32.90 ? 67  LYS   A CB   1 
ATOM   534  C  CG   . LYS   A 1 67 ? 24.756  5.376   -10.747 1.00 34.35 ? 67  LYS   A CG   1 
ATOM   535  C  CD   . LYS   A 1 67 ? 25.712  6.104   -9.812  1.00 41.63 ? 67  LYS   A CD   1 
ATOM   536  C  CE   . LYS   A 1 67 ? 26.944  5.252   -9.473  1.00 45.36 ? 67  LYS   A CE   1 
ATOM   537  N  NZ   . LYS   A 1 67 ? 28.229  5.917   -9.819  1.00 48.93 ? 67  LYS   A NZ   1 
ATOM   538  N  N    . TYR   A 1 68 ? 21.247  4.488   -9.950  1.00 25.36 ? 68  TYR   A N    1 
ATOM   539  C  CA   . TYR   A 1 68 ? 20.915  3.400   -9.048  1.00 27.06 ? 68  TYR   A CA   1 
ATOM   540  C  C    . TYR   A 1 68 ? 19.535  2.806   -9.283  1.00 27.55 ? 68  TYR   A C    1 
ATOM   541  O  O    . TYR   A 1 68 ? 19.243  1.753   -8.718  1.00 24.90 ? 68  TYR   A O    1 
ATOM   542  C  CB   . TYR   A 1 68 ? 21.016  3.877   -7.587  1.00 24.38 ? 68  TYR   A CB   1 
ATOM   543  C  CG   . TYR   A 1 68 ? 22.406  4.347   -7.186  1.00 26.71 ? 68  TYR   A CG   1 
ATOM   544  C  CD1  . TYR   A 1 68 ? 23.524  3.615   -7.539  1.00 27.80 ? 68  TYR   A CD1  1 
ATOM   545  C  CD2  . TYR   A 1 68 ? 22.595  5.516   -6.445  1.00 25.62 ? 68  TYR   A CD2  1 
ATOM   546  C  CE1  . TYR   A 1 68 ? 24.806  4.017   -7.166  1.00 31.17 ? 68  TYR   A CE1  1 
ATOM   547  C  CE2  . TYR   A 1 68 ? 23.886  5.930   -6.067  1.00 24.22 ? 68  TYR   A CE2  1 
ATOM   548  C  CZ   . TYR   A 1 68 ? 24.974  5.176   -6.428  1.00 26.05 ? 68  TYR   A CZ   1 
ATOM   549  O  OH   . TYR   A 1 68 ? 26.253  5.575   -6.095  1.00 25.96 ? 68  TYR   A OH   1 
ATOM   550  N  N    . GLY   A 1 69 ? 18.683  3.440   -10.084 1.00 29.03 ? 69  GLY   A N    1 
ATOM   551  C  CA   . GLY   A 1 69 ? 17.292  3.023   -10.146 1.00 28.33 ? 69  GLY   A CA   1 
ATOM   552  C  C    . GLY   A 1 69 ? 16.915  1.962   -11.169 1.00 27.75 ? 69  GLY   A C    1 
ATOM   553  O  O    . GLY   A 1 69 ? 15.737  1.797   -11.474 1.00 35.35 ? 69  GLY   A O    1 
ATOM   554  N  N    . LYS   A 1 70 ? 17.861  1.242   -11.685 1.00 29.62 ? 70  LYS   A N    1 
ATOM   555  C  CA   . LYS   A 1 70 ? 17.551  0.160   -12.604 1.00 30.61 ? 70  LYS   A CA   1 
ATOM   556  C  C    . LYS   A 1 70 ? 17.257  -1.125  -11.843 1.00 31.96 ? 70  LYS   A C    1 
ATOM   557  O  O    . LYS   A 1 70 ? 17.674  -1.290  -10.691 1.00 31.95 ? 70  LYS   A O    1 
ATOM   558  C  CB   . LYS   A 1 70 ? 18.709  -0.031  -13.573 1.00 36.60 ? 70  LYS   A CB   1 
ATOM   559  C  CG   . LYS   A 1 70 ? 19.295  1.303   -14.019 1.00 42.15 ? 70  LYS   A CG   1 
ATOM   560  C  CD   . LYS   A 1 70 ? 20.387  1.178   -15.062 1.00 42.05 ? 70  LYS   A CD   1 
ATOM   561  C  CE   . LYS   A 1 70 ? 21.658  1.933   -14.668 1.00 54.29 ? 70  LYS   A CE   1 
ATOM   562  N  NZ   . LYS   A 1 70 ? 22.868  1.472   -15.434 1.00 57.31 ? 70  LYS   A NZ   1 
ATOM   563  N  N    . PRO   A 1 71 ? 16.493  -2.043  -12.442 1.00 33.14 ? 71  PRO   A N    1 
ATOM   564  C  CA   . PRO   A 1 71 ? 16.154  -3.289  -11.744 1.00 29.41 ? 71  PRO   A CA   1 
ATOM   565  C  C    . PRO   A 1 71 ? 17.395  -4.079  -11.361 1.00 32.58 ? 71  PRO   A C    1 
ATOM   566  O  O    . PRO   A 1 71 ? 18.417  -4.048  -12.049 1.00 33.38 ? 71  PRO   A O    1 
ATOM   567  C  CB   . PRO   A 1 71 ? 15.306  -4.050  -12.768 1.00 38.64 ? 71  PRO   A CB   1 
ATOM   568  C  CG   . PRO   A 1 71 ? 14.751  -2.996  -13.650 1.00 39.49 ? 71  PRO   A CG   1 
ATOM   569  C  CD   . PRO   A 1 71 ? 15.821  -1.950  -13.748 1.00 32.72 ? 71  PRO   A CD   1 
ATOM   570  N  N    . ASN   A 1 72 ? 17.277  -4.811  -10.257 1.00 31.37 ? 72  ASN   A N    1 
ATOM   571  C  CA   . ASN   A 1 72 ? 18.369  -5.580  -9.683  1.00 35.05 ? 72  ASN   A CA   1 
ATOM   572  C  C    . ASN   A 1 72 ? 17.791  -6.899  -9.193  1.00 31.90 ? 72  ASN   A C    1 
ATOM   573  O  O    . ASN   A 1 72 ? 16.611  -6.977  -8.844  1.00 35.52 ? 72  ASN   A O    1 
ATOM   574  C  CB   . ASN   A 1 72 ? 19.030  -4.782  -8.531  1.00 30.82 ? 72  ASN   A CB   1 
ATOM   575  C  CG   . ASN   A 1 72 ? 20.210  -5.491  -7.894  1.00 34.98 ? 72  ASN   A CG   1 
ATOM   576  O  OD1  . ASN   A 1 72 ? 20.122  -6.637  -7.475  1.00 40.03 ? 72  ASN   A OD1  1 
ATOM   577  N  ND2  . ASN   A 1 72 ? 21.323  -4.776  -7.781  1.00 46.59 ? 72  ASN   A ND2  1 
ATOM   578  N  N    . LYS   A 1 73 ? 18.631  -7.933  -9.153  1.00 34.93 ? 73  LYS   A N    1 
ATOM   579  C  CA   . LYS   A 1 73 ? 18.165  -9.273  -8.820  1.00 37.79 ? 73  LYS   A CA   1 
ATOM   580  C  C    . LYS   A 1 73 ? 17.861  -9.457  -7.338  1.00 37.10 ? 73  LYS   A C    1 
ATOM   581  O  O    . LYS   A 1 73 ? 17.091  -10.357 -6.991  1.00 37.55 ? 73  LYS   A O    1 
ATOM   582  C  CB   . LYS   A 1 73 ? 19.208  -10.318 -9.250  1.00 36.47 ? 73  LYS   A CB   1 
ATOM   583  N  N    . ARG   A 1 74 ? 18.447  -8.651  -6.460  1.00 31.96 ? 74  ARG   A N    1 
ATOM   584  C  CA   . ARG   A 1 74 ? 18.375  -8.933  -5.032  1.00 32.71 ? 74  ARG   A CA   1 
ATOM   585  C  C    . ARG   A 1 74 ? 16.935  -8.905  -4.535  1.00 34.13 ? 74  ARG   A C    1 
ATOM   586  O  O    . ARG   A 1 74 ? 16.117  -8.105  -4.997  1.00 29.33 ? 74  ARG   A O    1 
ATOM   587  C  CB   . ARG   A 1 74 ? 19.202  -7.924  -4.253  1.00 32.05 ? 74  ARG   A CB   1 
ATOM   588  C  CG   . ARG   A 1 74 ? 20.662  -7.937  -4.621  1.00 41.48 ? 74  ARG   A CG   1 
ATOM   589  C  CD   . ARG   A 1 74 ? 21.306  -9.252  -4.255  1.00 43.38 ? 74  ARG   A CD   1 
ATOM   590  N  NE   . ARG   A 1 74 ? 21.657  -9.260  -2.844  1.00 47.99 ? 74  ARG   A NE   1 
ATOM   591  C  CZ   . ARG   A 1 74 ? 22.732  -8.666  -2.349  1.00 47.47 ? 74  ARG   A CZ   1 
ATOM   592  N  NH1  . ARG   A 1 74 ? 23.585  -8.019  -3.130  1.00 41.47 ? 74  ARG   A NH1  1 
ATOM   593  N  NH2  . ARG   A 1 74 ? 22.955  -8.719  -1.039  1.00 47.13 ? 74  ARG   A NH2  1 
ATOM   594  N  N    . LYS   A 1 75 ? 16.639  -9.787  -3.581  1.00 35.21 ? 75  LYS   A N    1 
ATOM   595  C  CA   . LYS   A 1 75 ? 15.275  -9.980  -3.108  1.00 33.22 ? 75  LYS   A CA   1 
ATOM   596  C  C    . LYS   A 1 75 ? 14.681  -8.664  -2.626  1.00 28.31 ? 75  LYS   A C    1 
ATOM   597  O  O    . LYS   A 1 75 ? 15.303  -7.927  -1.855  1.00 32.02 ? 75  LYS   A O    1 
ATOM   598  C  CB   . LYS   A 1 75 ? 15.256  -11.025 -1.990  1.00 33.09 ? 75  LYS   A CB   1 
ATOM   599  C  CG   . LYS   A 1 75 ? 13.881  -11.290 -1.396  1.00 33.92 ? 75  LYS   A CG   1 
ATOM   600  N  N    . GLY   A 1 76 ? 13.481  -8.346  -3.110  1.00 24.91 ? 76  GLY   A N    1 
ATOM   601  C  CA   . GLY   A 1 76 ? 12.823  -7.123  -2.707  1.00 26.05 ? 76  GLY   A CA   1 
ATOM   602  C  C    . GLY   A 1 76 ? 13.223  -5.874  -3.467  1.00 26.35 ? 76  GLY   A C    1 
ATOM   603  O  O    . GLY   A 1 76 ? 12.557  -4.842  -3.317  1.00 25.95 ? 76  GLY   A O    1 
ATOM   604  N  N    . PHE   A 1 77 ? 14.281  -5.909  -4.278  1.00 24.46 ? 77  PHE   A N    1 
ATOM   605  C  CA   . PHE   A 1 77 ? 14.751  -4.659  -4.878  1.00 26.27 ? 77  PHE   A CA   1 
ATOM   606  C  C    . PHE   A 1 77 ? 13.721  -4.081  -5.839  1.00 24.99 ? 77  PHE   A C    1 
ATOM   607  O  O    . PHE   A 1 77 ? 13.373  -2.900  -5.756  1.00 22.25 ? 77  PHE   A O    1 
ATOM   608  C  CB   . PHE   A 1 77 ? 16.084  -4.870  -5.600  1.00 27.81 ? 77  PHE   A CB   1 
ATOM   609  C  CG   . PHE   A 1 77 ? 16.767  -3.583  -5.973  1.00 31.89 ? 77  PHE   A CG   1 
ATOM   610  C  CD1  . PHE   A 1 77 ? 16.497  -2.964  -7.182  1.00 28.93 ? 77  PHE   A CD1  1 
ATOM   611  C  CD2  . PHE   A 1 77 ? 17.670  -2.978  -5.101  1.00 24.87 ? 77  PHE   A CD2  1 
ATOM   612  C  CE1  . PHE   A 1 77 ? 17.122  -1.779  -7.522  1.00 25.46 ? 77  PHE   A CE1  1 
ATOM   613  C  CE2  . PHE   A 1 77 ? 18.292  -1.779  -5.442  1.00 21.31 ? 77  PHE   A CE2  1 
ATOM   614  C  CZ   . PHE   A 1 77 ? 18.016  -1.193  -6.660  1.00 21.83 ? 77  PHE   A CZ   1 
ATOM   615  N  N    . ASN   A 1 78 ? 13.234  -4.895  -6.777  1.00 24.00 ? 78  ASN   A N    1 
ATOM   616  C  CA   . ASN   A 1 78 ? 12.338  -4.351  -7.787  1.00 19.16 ? 78  ASN   A CA   1 
ATOM   617  C  C    . ASN   A 1 78 ? 11.000  -3.967  -7.182  1.00 24.36 ? 78  ASN   A C    1 
ATOM   618  O  O    . ASN   A 1 78 ? 10.396  -2.969  -7.597  1.00 18.18 ? 78  ASN   A O    1 
ATOM   619  C  CB   . ASN   A 1 78 ? 12.199  -5.353  -8.921  1.00 22.61 ? 78  ASN   A CB   1 
ATOM   620  C  CG   . ASN   A 1 78 ? 13.514  -5.596  -9.604  1.00 28.43 ? 78  ASN   A CG   1 
ATOM   621  O  OD1  . ASN   A 1 78 ? 14.364  -4.719  -9.615  1.00 24.47 ? 78  ASN   A OD1  1 
ATOM   622  N  ND2  . ASN   A 1 78 ? 13.705  -6.790  -10.154 1.00 27.80 ? 78  ASN   A ND2  1 
ATOM   623  N  N    . GLU   A 1 79 ? 10.556  -4.686  -6.147  1.00 20.04 ? 79  GLU   A N    1 
ATOM   624  C  CA   . GLU   A 1 79 ? 9.399   -4.201  -5.403  1.00 21.13 ? 79  GLU   A CA   1 
ATOM   625  C  C    . GLU   A 1 79 ? 9.673   -2.820  -4.823  1.00 18.50 ? 79  GLU   A C    1 
ATOM   626  O  O    . GLU   A 1 79 ? 8.818   -1.928  -4.893  1.00 20.92 ? 79  GLU   A O    1 
ATOM   627  C  CB   . GLU   A 1 79 ? 9.024   -5.174  -4.285  1.00 26.44 ? 79  GLU   A CB   1 
ATOM   628  C  CG   . GLU   A 1 79 ? 7.796   -4.734  -3.500  1.00 21.99 ? 79  GLU   A CG   1 
ATOM   629  C  CD   . GLU   A 1 79 ? 7.223   -5.863  -2.679  1.00 30.56 ? 79  GLU   A CD   1 
ATOM   630  O  OE1  . GLU   A 1 79 ? 7.950   -6.843  -2.438  1.00 38.73 ? 79  GLU   A OE1  1 
ATOM   631  O  OE2  . GLU   A 1 79 ? 6.041   -5.779  -2.290  1.00 37.74 ? 79  GLU   A OE2  1 
ATOM   632  N  N    . GLY   A 1 80 ? 10.867  -2.628  -4.246  1.00 18.54 ? 80  GLY   A N    1 
ATOM   633  C  CA   . GLY   A 1 80 ? 11.214  -1.326  -3.682  1.00 18.06 ? 80  GLY   A CA   1 
ATOM   634  C  C    . GLY   A 1 80 ? 11.238  -0.211  -4.711  1.00 15.99 ? 80  GLY   A C    1 
ATOM   635  O  O    . GLY   A 1 80 ? 10.871  0.931   -4.411  1.00 19.54 ? 80  GLY   A O    1 
ATOM   636  N  N    . LEU   A 1 81 ? 11.700  -0.517  -5.929  1.00 21.63 ? 81  LEU   A N    1 
ATOM   637  C  CA   . LEU   A 1 81 ? 11.666  0.466   -7.012  1.00 17.92 ? 81  LEU   A CA   1 
ATOM   638  C  C    . LEU   A 1 81 ? 10.246  0.921   -7.271  1.00 19.12 ? 81  LEU   A C    1 
ATOM   639  O  O    . LEU   A 1 81 ? 10.000  2.110   -7.498  1.00 18.13 ? 81  LEU   A O    1 
ATOM   640  C  CB   . LEU   A 1 81 ? 12.258  -0.133  -8.296  1.00 17.36 ? 81  LEU   A CB   1 
ATOM   641  C  CG   . LEU   A 1 81 ? 13.788  -0.277  -8.299  1.00 20.82 ? 81  LEU   A CG   1 
ATOM   642  C  CD1  . LEU   A 1 81 ? 14.289  -0.876  -9.605  1.00 24.68 ? 81  LEU   A CD1  1 
ATOM   643  C  CD2  . LEU   A 1 81 ? 14.475  1.072   -8.039  1.00 24.18 ? 81  LEU   A CD2  1 
ATOM   644  N  N    . TRP   A 1 82 ? 9.295   -0.017  -7.263  1.00 16.43 ? 82  TRP   A N    1 
ATOM   645  C  CA   . TRP   A 1 82 ? 7.899   0.355   -7.491  1.00 20.52 ? 82  TRP   A CA   1 
ATOM   646  C  C    . TRP   A 1 82 ? 7.392   1.252   -6.363  1.00 18.71 ? 82  TRP   A C    1 
ATOM   647  O  O    . TRP   A 1 82 ? 6.766   2.286   -6.610  1.00 18.30 ? 82  TRP   A O    1 
ATOM   648  C  CB   . TRP   A 1 82 ? 7.013   -0.894  -7.618  1.00 22.40 ? 82  TRP   A CB   1 
ATOM   649  C  CG   . TRP   A 1 82 ? 5.574   -0.550  -7.911  1.00 20.84 ? 82  TRP   A CG   1 
ATOM   650  C  CD1  . TRP   A 1 82 ? 4.987   -0.450  -9.142  1.00 23.89 ? 82  TRP   A CD1  1 
ATOM   651  C  CD2  . TRP   A 1 82 ? 4.554   -0.221  -6.950  1.00 19.60 ? 82  TRP   A CD2  1 
ATOM   652  N  NE1  . TRP   A 1 82 ? 3.667   -0.084  -9.003  1.00 23.20 ? 82  TRP   A NE1  1 
ATOM   653  C  CE2  . TRP   A 1 82 ? 3.375   0.052   -7.670  1.00 26.06 ? 82  TRP   A CE2  1 
ATOM   654  C  CE3  . TRP   A 1 82 ? 4.525   -0.150  -5.549  1.00 22.41 ? 82  TRP   A CE3  1 
ATOM   655  C  CZ2  . TRP   A 1 82 ? 2.179   0.409   -7.041  1.00 25.55 ? 82  TRP   A CZ2  1 
ATOM   656  C  CZ3  . TRP   A 1 82 ? 3.330   0.195   -4.923  1.00 21.01 ? 82  TRP   A CZ3  1 
ATOM   657  C  CH2  . TRP   A 1 82 ? 2.172   0.466   -5.680  1.00 21.86 ? 82  TRP   A CH2  1 
ATOM   658  N  N    . GLU   A 1 83 ? 7.673   0.875   -5.120  1.00 18.47 ? 83  GLU   A N    1 
ATOM   659  C  CA   . GLU   A 1 83 ? 7.214   1.654   -3.970  1.00 20.24 ? 83  GLU   A CA   1 
ATOM   660  C  C    . GLU   A 1 83 ? 7.739   3.085   -4.010  1.00 14.90 ? 83  GLU   A C    1 
ATOM   661  O  O    . GLU   A 1 83 ? 6.989   4.047   -3.788  1.00 15.21 ? 83  GLU   A O    1 
ATOM   662  C  CB   . GLU   A 1 83 ? 7.637   0.948   -2.672  1.00 16.27 ? 83  GLU   A CB   1 
ATOM   663  C  CG   . GLU   A 1 83 ? 6.972   -0.391  -2.522  1.00 17.69 ? 83  GLU   A CG   1 
ATOM   664  C  CD   . GLU   A 1 83 ? 7.379   -1.175  -1.301  1.00 22.00 ? 83  GLU   A CD   1 
ATOM   665  O  OE1  . GLU   A 1 83 ? 8.336   -0.778  -0.631  1.00 21.29 ? 83  GLU   A OE1  1 
ATOM   666  O  OE2  . GLU   A 1 83 ? 6.755   -2.233  -1.018  1.00 22.49 ? 83  GLU   A OE2  1 
ATOM   667  N  N    . ILE   A 1 84 ? 9.039   3.256   -4.241  1.00 16.32 ? 84  ILE   A N    1 
ATOM   668  C  CA   . ILE   A 1 84 ? 9.594   4.600   -4.115  1.00 15.06 ? 84  ILE   A CA   1 
ATOM   669  C  C    . ILE   A 1 84 ? 9.052   5.495   -5.217  1.00 17.84 ? 84  ILE   A C    1 
ATOM   670  O  O    . ILE   A 1 84 ? 8.918   6.711   -5.035  1.00 15.65 ? 84  ILE   A O    1 
ATOM   671  C  CB   . ILE   A 1 84 ? 11.133  4.549   -4.121  1.00 14.28 ? 84  ILE   A CB   1 
ATOM   672  C  CG1  . ILE   A 1 84 ? 11.709  5.882   -3.626  1.00 17.81 ? 84  ILE   A CG1  1 
ATOM   673  C  CG2  . ILE   A 1 84 ? 11.630  4.201   -5.552  1.00 17.20 ? 84  ILE   A CG2  1 
ATOM   674  C  CD1  . ILE   A 1 84 ? 13.141  5.772   -3.133  1.00 13.70 ? 84  ILE   A CD1  1 
ATOM   675  N  N    . GLN   A 1 85 ? 8.696   4.917   -6.368  1.00 17.72 ? 85  GLN   A N    1 
ATOM   676  C  CA   . GLN   A 1 85 ? 8.203   5.730   -7.465  1.00 20.41 ? 85  GLN   A CA   1 
ATOM   677  C  C    . GLN   A 1 85 ? 6.700   5.952   -7.372  1.00 23.09 ? 85  GLN   A C    1 
ATOM   678  O  O    . GLN   A 1 85 ? 6.207   7.010   -7.789  1.00 18.99 ? 85  GLN   A O    1 
ATOM   679  C  CB   . GLN   A 1 85 ? 8.554   5.066   -8.801  1.00 20.27 ? 85  GLN   A CB   1 
ATOM   680  C  CG   . GLN   A 1 85 ? 7.962   5.783   -9.991  1.00 31.96 ? 85  GLN   A CG   1 
ATOM   681  C  CD   . GLN   A 1 85 ? 8.605   5.363   -11.287 1.00 38.45 ? 85  GLN   A CD   1 
ATOM   682  O  OE1  . GLN   A 1 85 ? 8.787   6.184   -12.191 1.00 42.96 ? 85  GLN   A OE1  1 
ATOM   683  N  NE2  . GLN   A 1 85 ? 8.961   4.074   -11.391 1.00 33.26 ? 85  GLN   A NE2  1 
ATOM   684  N  N    . ASN   A 1 86 ? 5.962   4.992   -6.815  1.00 17.97 ? 86  ASN   A N    1 
ATOM   685  C  CA   . ASN   A 1 86 ? 4.506   5.017   -6.907  1.00 17.61 ? 86  ASN   A CA   1 
ATOM   686  C  C    . ASN   A 1 86 ? 3.780   5.302   -5.603  1.00 19.50 ? 86  ASN   A C    1 
ATOM   687  O  O    . ASN   A 1 86 ? 2.654   5.807   -5.656  1.00 20.48 ? 86  ASN   A O    1 
ATOM   688  C  CB   . ASN   A 1 86 ? 3.990   3.700   -7.493  1.00 18.64 ? 86  ASN   A CB   1 
ATOM   689  C  CG   . ASN   A 1 86 ? 4.419   3.528   -8.925  1.00 22.45 ? 86  ASN   A CG   1 
ATOM   690  O  OD1  . ASN   A 1 86 ? 5.286   2.709   -9.239  1.00 27.41 ? 86  ASN   A OD1  1 
ATOM   691  N  ND2  . ASN   A 1 86 ? 3.890   4.365   -9.786  1.00 21.37 ? 86  ASN   A ND2  1 
ATOM   692  N  N    . ASN   A 1 87 ? 4.378   5.015   -4.441  1.00 16.34 ? 87  ASN   A N    1 
ATOM   693  C  CA   . ASN   A 1 87 ? 3.727   5.386   -3.185  1.00 19.67 ? 87  ASN   A CA   1 
ATOM   694  C  C    . ASN   A 1 87 ? 4.776   5.460   -2.082  1.00 19.96 ? 87  ASN   A C    1 
ATOM   695  O  O    . ASN   A 1 87 ? 4.754   4.647   -1.146  1.00 22.81 ? 87  ASN   A O    1 
ATOM   696  C  CB   . ASN   A 1 87 ? 2.628   4.392   -2.831  1.00 17.67 ? 87  ASN   A CB   1 
ATOM   697  C  CG   . ASN   A 1 87 ? 1.517   5.020   -2.002  1.00 23.91 ? 87  ASN   A CG   1 
ATOM   698  O  OD1  . ASN   A 1 87 ? 1.743   5.994   -1.294  1.00 21.12 ? 87  ASN   A OD1  1 
ATOM   699  N  ND2  . ASN   A 1 87 ? 0.321   4.432   -2.059  1.00 24.84 ? 87  ASN   A ND2  1 
ATOM   700  N  N    . PRO   A 1 88 ? 5.731   6.396   -2.173  1.00 16.73 ? 88  PRO   A N    1 
ATOM   701  C  CA   . PRO   A 1 88 ? 6.867   6.369   -1.237  1.00 14.49 ? 88  PRO   A CA   1 
ATOM   702  C  C    . PRO   A 1 88 ? 6.495   6.739   0.194   1.00 19.53 ? 88  PRO   A C    1 
ATOM   703  O  O    . PRO   A 1 88 ? 7.282   6.471   1.111   1.00 16.70 ? 88  PRO   A O    1 
ATOM   704  C  CB   . PRO   A 1 88 ? 7.834   7.397   -1.836  1.00 15.37 ? 88  PRO   A CB   1 
ATOM   705  C  CG   . PRO   A 1 88 ? 6.948   8.370   -2.585  1.00 15.03 ? 88  PRO   A CG   1 
ATOM   706  C  CD   . PRO   A 1 88 ? 5.832   7.506   -3.140  1.00 16.33 ? 88  PRO   A CD   1 
ATOM   707  N  N    . HIS   A 1 89 ? 5.346   7.374   0.409   1.00 15.26 ? 89  HIS   A N    1 
ATOM   708  C  CA   . HIS   A 1 89 ? 4.954   7.880   1.722   1.00 16.37 ? 89  HIS   A CA   1 
ATOM   709  C  C    . HIS   A 1 89 ? 3.873   7.046   2.387   1.00 18.44 ? 89  HIS   A C    1 
ATOM   710  O  O    . HIS   A 1 89 ? 3.354   7.443   3.438   1.00 18.62 ? 89  HIS   A O    1 
ATOM   711  C  CB   . HIS   A 1 89 ? 4.498   9.335   1.580   1.00 15.47 ? 89  HIS   A CB   1 
ATOM   712  C  CG   . HIS   A 1 89 ? 5.560   10.232  1.034   1.00 18.63 ? 89  HIS   A CG   1 
ATOM   713  N  ND1  . HIS   A 1 89 ? 6.794   10.361  1.631   1.00 19.59 ? 89  HIS   A ND1  1 
ATOM   714  C  CD2  . HIS   A 1 89 ? 5.588   11.022  -0.065  1.00 17.11 ? 89  HIS   A CD2  1 
ATOM   715  C  CE1  . HIS   A 1 89 ? 7.536   11.204  0.933   1.00 21.12 ? 89  HIS   A CE1  1 
ATOM   716  N  NE2  . HIS   A 1 89 ? 6.823   11.623  -0.099  1.00 18.10 ? 89  HIS   A NE2  1 
ATOM   717  N  N    . ALA   A 1 90 ? 3.524   5.894   1.810   1.00 21.02 ? 90  ALA   A N    1 
ATOM   718  C  CA   . ALA   A 1 90 ? 2.486   5.042   2.365   1.00 20.66 ? 90  ALA   A CA   1 
ATOM   719  C  C    . ALA   A 1 90 ? 2.948   4.400   3.664   1.00 22.42 ? 90  ALA   A C    1 
ATOM   720  O  O    . ALA   A 1 90 ? 4.136   4.379   4.004   1.00 24.68 ? 90  ALA   A O    1 
ATOM   721  C  CB   . ALA   A 1 90 ? 2.103   3.938   1.374   1.00 22.42 ? 90  ALA   A CB   1 
ATOM   722  N  N    . SER   A 1 91 ? 1.983   3.863   4.386   1.00 22.86 ? 91  SER   A N    1 
ATOM   723  C  CA   . SER   A 1 91 ? 2.262   3.029   5.540   1.00 34.82 ? 91  SER   A CA   1 
ATOM   724  C  C    . SER   A 1 91 ? 2.445   1.605   5.039   1.00 35.81 ? 91  SER   A C    1 
ATOM   725  O  O    . SER   A 1 91 ? 1.534   1.037   4.428   1.00 40.46 ? 91  SER   A O    1 
ATOM   726  C  CB   . SER   A 1 91 ? 1.123   3.112   6.553   1.00 37.00 ? 91  SER   A CB   1 
ATOM   727  O  OG   . SER   A 1 91 ? 1.180   2.026   7.449   1.00 43.74 ? 91  SER   A OG   1 
ATOM   728  N  N    . TYR   A 1 92 ? 3.628   1.037   5.254   1.00 35.37 ? 92  TYR   A N    1 
ATOM   729  C  CA   . TYR   A 1 92 ? 3.865   -0.349  4.890   1.00 30.11 ? 92  TYR   A CA   1 
ATOM   730  C  C    . TYR   A 1 92 ? 3.790   -1.268  6.101   1.00 45.80 ? 92  TYR   A C    1 
ATOM   731  O  O    . TYR   A 1 92 ? 4.290   -2.396  6.053   1.00 52.89 ? 92  TYR   A O    1 
ATOM   732  C  CB   . TYR   A 1 92 ? 5.201   -0.463  4.151   1.00 32.76 ? 92  TYR   A CB   1 
ATOM   733  C  CG   . TYR   A 1 92 ? 5.151   0.203   2.789   1.00 32.42 ? 92  TYR   A CG   1 
ATOM   734  C  CD1  . TYR   A 1 92 ? 4.645   -0.474  1.679   1.00 37.88 ? 92  TYR   A CD1  1 
ATOM   735  C  CD2  . TYR   A 1 92 ? 5.581   1.511   2.615   1.00 28.80 ? 92  TYR   A CD2  1 
ATOM   736  C  CE1  . TYR   A 1 92 ? 4.587   0.133   0.424   1.00 36.65 ? 92  TYR   A CE1  1 
ATOM   737  C  CE2  . TYR   A 1 92 ? 5.538   2.127   1.367   1.00 21.57 ? 92  TYR   A CE2  1 
ATOM   738  C  CZ   . TYR   A 1 92 ? 5.034   1.438   0.275   1.00 35.19 ? 92  TYR   A CZ   1 
ATOM   739  O  OH   . TYR   A 1 92 ? 4.971   2.037   -0.966  1.00 30.83 ? 92  TYR   A OH   1 
ATOM   740  N  N    . SER   A 1 93 ? 3.135   -0.806  7.168   1.00 53.56 ? 93  SER   A N    1 
ATOM   741  C  CA   . SER   A 1 93 ? 2.865   -1.555  8.402   1.00 59.53 ? 93  SER   A CA   1 
ATOM   742  C  C    . SER   A 1 93 ? 4.078   -2.325  8.904   1.00 72.80 ? 93  SER   A C    1 
ATOM   743  O  O    . SER   A 1 93 ? 4.070   -3.556  8.923   1.00 79.94 ? 93  SER   A O    1 
ATOM   744  C  CB   . SER   A 1 93 ? 1.695   -2.528  8.206   1.00 62.36 ? 93  SER   A CB   1 
ATOM   745  O  OG   . SER   A 1 93 ? 1.868   -3.330  7.049   1.00 65.08 ? 93  SER   A OG   1 
ATOM   746  N  N    . MET   B 1 1  ? -17.571 10.578  42.082  1.00 57.65 ? 1   MET   B N    1 
ATOM   747  C  CA   . MET   B 1 1  ? -17.352 9.633   43.176  1.00 59.28 ? 1   MET   B CA   1 
ATOM   748  C  C    . MET   B 1 1  ? -15.877 9.251   43.271  1.00 53.39 ? 1   MET   B C    1 
ATOM   749  O  O    . MET   B 1 1  ? -15.240 8.988   42.258  1.00 58.84 ? 1   MET   B O    1 
ATOM   750  C  CB   . MET   B 1 1  ? -18.217 8.381   42.999  1.00 60.19 ? 1   MET   B CB   1 
ATOM   751  N  N    . PRO   B 1 2  ? -15.334 9.240   44.489  1.00 53.41 ? 2   PRO   B N    1 
ATOM   752  C  CA   . PRO   B 1 2  ? -13.898 8.959   44.656  1.00 49.63 ? 2   PRO   B CA   1 
ATOM   753  C  C    . PRO   B 1 2  ? -13.585 7.497   44.360  1.00 48.18 ? 2   PRO   B C    1 
ATOM   754  O  O    . PRO   B 1 2  ? -14.300 6.593   44.792  1.00 50.74 ? 2   PRO   B O    1 
ATOM   755  C  CB   . PRO   B 1 2  ? -13.620 9.308   46.122  1.00 51.27 ? 2   PRO   B CB   1 
ATOM   756  C  CG   . PRO   B 1 2  ? -14.847 9.901   46.669  1.00 55.71 ? 2   PRO   B CG   1 
ATOM   757  C  CD   . PRO   B 1 2  ? -15.950 9.853   45.678  1.00 57.17 ? 2   PRO   B CD   1 
ATOM   758  N  N    . HIS   B 1 3  ? -12.517 7.274   43.605  1.00 50.51 ? 3   HIS   B N    1 
ATOM   759  C  CA   . HIS   B 1 3  ? -12.071 5.936   43.240  1.00 45.73 ? 3   HIS   B CA   1 
ATOM   760  C  C    . HIS   B 1 3  ? -10.674 5.692   43.816  1.00 42.45 ? 3   HIS   B C    1 
ATOM   761  O  O    . HIS   B 1 3  ? -10.087 6.554   44.472  1.00 41.59 ? 3   HIS   B O    1 
ATOM   762  C  CB   . HIS   B 1 3  ? -12.095 5.761   41.717  1.00 46.32 ? 3   HIS   B CB   1 
ATOM   763  C  CG   . HIS   B 1 3  ? -13.469 5.828   41.118  1.00 53.87 ? 3   HIS   B CG   1 
ATOM   764  N  ND1  . HIS   B 1 3  ? -14.609 5.523   41.830  1.00 61.48 ? 3   HIS   B ND1  1 
ATOM   765  C  CD2  . HIS   B 1 3  ? -13.884 6.182   39.878  1.00 58.31 ? 3   HIS   B CD2  1 
ATOM   766  C  CE1  . HIS   B 1 3  ? -15.667 5.680   41.054  1.00 60.02 ? 3   HIS   B CE1  1 
ATOM   767  N  NE2  . HIS   B 1 3  ? -15.255 6.081   39.865  1.00 64.13 ? 3   HIS   B NE2  1 
ATOM   768  N  N    . ALA   B 1 4  ? -10.145 4.489   43.581  1.00 39.40 ? 4   ALA   B N    1 
ATOM   769  C  CA   . ALA   B 1 4  ? -8.819  4.169   44.090  1.00 37.39 ? 4   ALA   B CA   1 
ATOM   770  C  C    . ALA   B 1 4  ? -7.784  5.136   43.541  1.00 39.05 ? 4   ALA   B C    1 
ATOM   771  O  O    . ALA   B 1 4  ? -6.835  5.513   44.239  1.00 42.23 ? 4   ALA   B O    1 
ATOM   772  C  CB   . ALA   B 1 4  ? -8.445  2.740   43.722  1.00 36.89 ? 4   ALA   B CB   1 
ATOM   773  N  N    . PHE   B 1 5  ? -7.933  5.517   42.279  1.00 33.11 ? 5   PHE   B N    1 
ATOM   774  C  CA   . PHE   B 1 5  ? -7.094  6.516   41.642  1.00 30.81 ? 5   PHE   B CA   1 
ATOM   775  C  C    . PHE   B 1 5  ? -7.902  7.799   41.509  1.00 38.46 ? 5   PHE   B C    1 
ATOM   776  O  O    . PHE   B 1 5  ? -9.113  7.759   41.249  1.00 34.33 ? 5   PHE   B O    1 
ATOM   777  C  CB   . PHE   B 1 5  ? -6.632  6.034   40.272  1.00 28.88 ? 5   PHE   B CB   1 
ATOM   778  C  CG   . PHE   B 1 5  ? -5.569  4.981   40.338  1.00 30.70 ? 5   PHE   B CG   1 
ATOM   779  C  CD1  . PHE   B 1 5  ? -4.235  5.322   40.378  1.00 30.63 ? 5   PHE   B CD1  1 
ATOM   780  C  CD2  . PHE   B 1 5  ? -5.912  3.650   40.418  1.00 34.53 ? 5   PHE   B CD2  1 
ATOM   781  C  CE1  . PHE   B 1 5  ? -3.257  4.346   40.453  1.00 30.21 ? 5   PHE   B CE1  1 
ATOM   782  C  CE2  . PHE   B 1 5  ? -4.934  2.666   40.491  1.00 32.11 ? 5   PHE   B CE2  1 
ATOM   783  C  CZ   . PHE   B 1 5  ? -3.603  3.019   40.505  1.00 26.28 ? 5   PHE   B CZ   1 
ATOM   784  N  N    . LYS   B 1 6  ? -7.246  8.930   41.735  1.00 31.44 ? 6   LYS   B N    1 
ATOM   785  C  CA   . LYS   B 1 6  ? -7.954  10.197  41.677  1.00 33.11 ? 6   LYS   B CA   1 
ATOM   786  C  C    . LYS   B 1 6  ? -7.293  11.101  40.641  1.00 31.89 ? 6   LYS   B C    1 
ATOM   787  O  O    . LYS   B 1 6  ? -6.100  10.953  40.361  1.00 29.16 ? 6   LYS   B O    1 
ATOM   788  C  CB   . LYS   B 1 6  ? -7.956  10.873  43.055  1.00 35.26 ? 6   LYS   B CB   1 
ATOM   789  C  CG   . LYS   B 1 6  ? -6.853  11.900  43.232  1.00 38.49 ? 6   LYS   B CG   1 
ATOM   790  C  CD   . LYS   B 1 6  ? -7.035  12.761  44.470  1.00 45.62 ? 6   LYS   B CD   1 
ATOM   791  C  CE   . LYS   B 1 6  ? -6.827  11.947  45.724  1.00 41.86 ? 6   LYS   B CE   1 
ATOM   792  N  NZ   . LYS   B 1 6  ? -5.402  11.495  45.797  1.00 42.97 ? 6   LYS   B NZ   1 
ATOM   793  N  N    . PRO   B 1 7  ? -8.042  12.022  40.032  1.00 32.86 ? 7   PRO   B N    1 
ATOM   794  C  CA   . PRO   B 1 7  ? -7.423  12.966  39.096  1.00 33.72 ? 7   PRO   B CA   1 
ATOM   795  C  C    . PRO   B 1 7  ? -6.215  13.655  39.712  1.00 30.91 ? 7   PRO   B C    1 
ATOM   796  O  O    . PRO   B 1 7  ? -6.267  14.148  40.840  1.00 34.23 ? 7   PRO   B O    1 
ATOM   797  C  CB   . PRO   B 1 7  ? -8.556  13.949  38.805  1.00 37.00 ? 7   PRO   B CB   1 
ATOM   798  C  CG   . PRO   B 1 7  ? -9.770  13.110  38.922  1.00 42.30 ? 7   PRO   B CG   1 
ATOM   799  C  CD   . PRO   B 1 7  ? -9.496  12.237  40.121  1.00 35.88 ? 7   PRO   B CD   1 
ATOM   800  N  N    . GLY   B 1 8  ? -5.107  13.652  38.975  1.00 29.34 ? 8   GLY   B N    1 
ATOM   801  C  CA   . GLY   B 1 8  ? -3.876  14.234  39.450  1.00 32.50 ? 8   GLY   B CA   1 
ATOM   802  C  C    . GLY   B 1 8  ? -2.914  13.257  40.090  1.00 36.79 ? 8   GLY   B C    1 
ATOM   803  O  O    . GLY   B 1 8  ? -1.762  13.640  40.341  1.00 32.00 ? 8   GLY   B O    1 
ATOM   804  N  N    . ASP   B 1 9  ? -3.351  12.017  40.370  1.00 26.15 ? 9   ASP   B N    1 
ATOM   805  C  CA   . ASP   B 1 9  ? -2.447  10.996  40.878  1.00 27.22 ? 9   ASP   B CA   1 
ATOM   806  C  C    . ASP   B 1 9  ? -1.358  10.742  39.846  1.00 24.37 ? 9   ASP   B C    1 
ATOM   807  O  O    . ASP   B 1 9  ? -1.623  10.677  38.640  1.00 25.38 ? 9   ASP   B O    1 
ATOM   808  C  CB   . ASP   B 1 9  ? -3.185  9.673   41.157  1.00 26.94 ? 9   ASP   B CB   1 
ATOM   809  C  CG   . ASP   B 1 9  ? -3.909  9.632   42.507  1.00 37.51 ? 9   ASP   B CG   1 
ATOM   810  O  OD1  . ASP   B 1 9  ? -3.726  10.537  43.348  1.00 37.31 ? 9   ASP   B OD1  1 
ATOM   811  O  OD2  . ASP   B 1 9  ? -4.658  8.644   42.744  1.00 28.78 ? 9   ASP   B OD2  1 
ATOM   812  N  N    . LEU   B 1 10 ? -0.128  10.581  40.313  1.00 22.08 ? 10  LEU   B N    1 
ATOM   813  C  CA   . LEU   B 1 10 ? 0.996   10.344  39.421  1.00 24.26 ? 10  LEU   B CA   1 
ATOM   814  C  C    . LEU   B 1 10 ? 1.311   8.862   39.428  1.00 21.86 ? 10  LEU   B C    1 
ATOM   815  O  O    . LEU   B 1 10 ? 1.299   8.229   40.493  1.00 21.30 ? 10  LEU   B O    1 
ATOM   816  C  CB   . LEU   B 1 10 ? 2.221   11.149  39.855  1.00 24.14 ? 10  LEU   B CB   1 
ATOM   817  C  CG   . LEU   B 1 10 ? 1.967   12.651  40.031  1.00 24.28 ? 10  LEU   B CG   1 
ATOM   818  C  CD1  . LEU   B 1 10 ? 3.271   13.388  40.340  1.00 23.80 ? 10  LEU   B CD1  1 
ATOM   819  C  CD2  . LEU   B 1 10 ? 1.311   13.219  38.769  1.00 23.24 ? 10  LEU   B CD2  1 
ATOM   820  N  N    . VAL   B 1 11 ? 1.608   8.309   38.247  1.00 20.22 ? 11  VAL   B N    1 
ATOM   821  C  CA   . VAL   B 1 11 ? 1.788   6.867   38.088  1.00 18.18 ? 11  VAL   B CA   1 
ATOM   822  C  C    . VAL   B 1 11 ? 2.860   6.580   37.043  1.00 21.43 ? 11  VAL   B C    1 
ATOM   823  O  O    . VAL   B 1 11 ? 3.334   7.475   36.337  1.00 21.17 ? 11  VAL   B O    1 
ATOM   824  C  CB   . VAL   B 1 11 ? 0.481   6.150   37.663  1.00 20.12 ? 11  VAL   B CB   1 
ATOM   825  C  CG1  . VAL   B 1 11 ? -0.630  6.282   38.752  1.00 20.19 ? 11  VAL   B CG1  1 
ATOM   826  C  CG2  . VAL   B 1 11 ? 0.028   6.641   36.273  1.00 18.99 ? 11  VAL   B CG2  1 
ATOM   827  N  N    . PHE   B 1 12 ? 3.258   5.305   36.969  1.00 22.20 ? 12  PHE   B N    1 
ATOM   828  C  CA   . PHE   B 1 12 ? 3.790   4.720   35.747  1.00 21.93 ? 12  PHE   B CA   1 
ATOM   829  C  C    . PHE   B 1 12 ? 2.685   3.868   35.150  1.00 21.98 ? 12  PHE   B C    1 
ATOM   830  O  O    . PHE   B 1 12 ? 2.038   3.094   35.876  1.00 23.05 ? 12  PHE   B O    1 
ATOM   831  C  CB   . PHE   B 1 12 ? 5.042   3.885   36.024  1.00 22.53 ? 12  PHE   B CB   1 
ATOM   832  C  CG   . PHE   B 1 12 ? 6.245   4.728   36.379  1.00 25.24 ? 12  PHE   B CG   1 
ATOM   833  C  CD1  . PHE   B 1 12 ? 6.485   5.073   37.703  1.00 27.80 ? 12  PHE   B CD1  1 
ATOM   834  C  CD2  . PHE   B 1 12 ? 7.109   5.194   35.400  1.00 22.68 ? 12  PHE   B CD2  1 
ATOM   835  C  CE1  . PHE   B 1 12 ? 7.573   5.874   38.039  1.00 28.14 ? 12  PHE   B CE1  1 
ATOM   836  C  CE2  . PHE   B 1 12 ? 8.200   5.985   35.738  1.00 29.30 ? 12  PHE   B CE2  1 
ATOM   837  C  CZ   . PHE   B 1 12 ? 8.425   6.319   37.060  1.00 24.39 ? 12  PHE   B CZ   1 
ATOM   838  N  N    . ALA   B 1 13 ? 2.443   4.034   33.849  1.00 17.82 ? 13  ALA   B N    1 
ATOM   839  C  CA   . ALA   B 1 13 ? 1.393   3.312   33.149  1.00 21.42 ? 13  ALA   B CA   1 
ATOM   840  C  C    . ALA   B 1 13 ? 2.012   2.394   32.104  1.00 23.23 ? 13  ALA   B C    1 
ATOM   841  O  O    . ALA   B 1 13 ? 2.881   2.811   31.329  1.00 20.54 ? 13  ALA   B O    1 
ATOM   842  C  CB   . ALA   B 1 13 ? 0.412   4.283   32.490  1.00 21.47 ? 13  ALA   B CB   1 
ATOM   843  N  N    . LYS   B 1 14 ? 1.566   1.152   32.082  1.00 23.02 ? 14  LYS   B N    1 
ATOM   844  C  CA   . LYS   B 1 14 ? 2.185   0.121   31.256  1.00 21.82 ? 14  LYS   B CA   1 
ATOM   845  C  C    . LYS   B 1 14 ? 1.306   -0.154  30.048  1.00 23.61 ? 14  LYS   B C    1 
ATOM   846  O  O    . LYS   B 1 14 ? 0.141   -0.529  30.208  1.00 25.75 ? 14  LYS   B O    1 
ATOM   847  C  CB   . LYS   B 1 14 ? 2.405   -1.165  32.061  1.00 22.61 ? 14  LYS   B CB   1 
ATOM   848  C  CG   . LYS   B 1 14 ? 3.143   -2.278  31.287  1.00 24.12 ? 14  LYS   B CG   1 
ATOM   849  C  CD   . LYS   B 1 14 ? 4.576   -1.840  30.898  1.00 25.74 ? 14  LYS   B CD   1 
ATOM   850  C  CE   . LYS   B 1 14 ? 5.366   -3.027  30.357  1.00 29.05 ? 14  LYS   B CE   1 
ATOM   851  N  NZ   . LYS   B 1 14 ? 4.899   -3.306  28.995  1.00 26.92 ? 14  LYS   B NZ   1 
ATOM   852  N  N    . MET   B 1 15 ? 1.885   -0.001  28.853  1.00 26.10 ? 15  MET   B N    1 
ATOM   853  C  CA   . MET   B 1 15 ? 1.340   -0.445  27.573  1.00 26.53 ? 15  MET   B CA   1 
ATOM   854  C  C    . MET   B 1 15 ? 2.203   -1.554  26.986  1.00 33.10 ? 15  MET   B C    1 
ATOM   855  O  O    . MET   B 1 15 ? 3.430   -1.525  27.103  1.00 31.91 ? 15  MET   B O    1 
ATOM   856  C  CB   . MET   B 1 15 ? 1.288   0.696   26.536  1.00 29.25 ? 15  MET   B CB   1 
ATOM   857  C  CG   . MET   B 1 15 ? 0.592   1.992   26.943  1.00 35.20 ? 15  MET   B CG   1 
ATOM   858  S  SD   . MET   B 1 15 ? -1.113  1.608   27.325  1.00 42.13 ? 15  MET   B SD   1 
ATOM   859  C  CE   . MET   B 1 15 ? -1.869  1.824   25.719  1.00 36.74 ? 15  MET   B CE   1 
ATOM   860  N  N    . LYS   B 1 16 ? 1.546   -2.497  26.300  1.00 33.83 ? 16  LYS   B N    1 
ATOM   861  C  CA   . LYS   B 1 16 ? 2.253   -3.593  25.641  1.00 32.99 ? 16  LYS   B CA   1 
ATOM   862  C  C    . LYS   B 1 16 ? 3.285   -3.017  24.677  1.00 33.09 ? 16  LYS   B C    1 
ATOM   863  O  O    . LYS   B 1 16 ? 2.985   -2.102  23.908  1.00 35.68 ? 16  LYS   B O    1 
ATOM   864  C  CB   . LYS   B 1 16 ? 1.250   -4.487  24.902  1.00 36.46 ? 16  LYS   B CB   1 
ATOM   865  C  CG   . LYS   B 1 16 ? 1.834   -5.732  24.226  1.00 40.67 ? 16  LYS   B CG   1 
ATOM   866  C  CD   . LYS   B 1 16 ? 0.706   -6.584  23.634  1.00 46.92 ? 16  LYS   B CD   1 
ATOM   867  C  CE   . LYS   B 1 16 ? 0.954   -8.090  23.746  1.00 65.80 ? 16  LYS   B CE   1 
ATOM   868  N  NZ   . LYS   B 1 16 ? 2.217   -8.560  23.093  1.00 58.59 ? 16  LYS   B NZ   1 
ATOM   869  N  N    . GLY   B 1 17 ? 4.515   -3.515  24.751  1.00 35.64 ? 17  GLY   B N    1 
ATOM   870  C  CA   . GLY   B 1 17 ? 5.560   -3.043  23.862  1.00 40.39 ? 17  GLY   B CA   1 
ATOM   871  C  C    . GLY   B 1 17 ? 6.231   -1.745  24.264  1.00 38.99 ? 17  GLY   B C    1 
ATOM   872  O  O    . GLY   B 1 17 ? 7.072   -1.250  23.502  1.00 39.26 ? 17  GLY   B O    1 
ATOM   873  N  N    . TYR   B 1 18 ? 5.889   -1.174  25.421  1.00 29.92 ? 18  TYR   B N    1 
ATOM   874  C  CA   . TYR   B 1 18 ? 6.516   0.022   25.954  1.00 27.61 ? 18  TYR   B CA   1 
ATOM   875  C  C    . TYR   B 1 18 ? 6.940   -0.198  27.398  1.00 30.43 ? 18  TYR   B C    1 
ATOM   876  O  O    . TYR   B 1 18 ? 6.273   -0.924  28.146  1.00 29.47 ? 18  TYR   B O    1 
ATOM   877  C  CB   . TYR   B 1 18 ? 5.552   1.217   25.891  1.00 28.83 ? 18  TYR   B CB   1 
ATOM   878  C  CG   . TYR   B 1 18 ? 5.168   1.561   24.480  1.00 35.52 ? 18  TYR   B CG   1 
ATOM   879  C  CD1  . TYR   B 1 18 ? 5.932   2.438   23.715  1.00 27.89 ? 18  TYR   B CD1  1 
ATOM   880  C  CD2  . TYR   B 1 18 ? 4.068   0.958   23.886  1.00 37.43 ? 18  TYR   B CD2  1 
ATOM   881  C  CE1  . TYR   B 1 18 ? 5.585   2.724   22.405  1.00 30.44 ? 18  TYR   B CE1  1 
ATOM   882  C  CE2  . TYR   B 1 18 ? 3.720   1.237   22.574  1.00 42.28 ? 18  TYR   B CE2  1 
ATOM   883  C  CZ   . TYR   B 1 18 ? 4.477   2.119   21.843  1.00 32.78 ? 18  TYR   B CZ   1 
ATOM   884  O  OH   . TYR   B 1 18 ? 4.105   2.389   20.554  1.00 39.50 ? 18  TYR   B OH   1 
ATOM   885  N  N    . PRO   B 1 19 ? 8.030   0.429   27.829  1.00 27.73 ? 19  PRO   B N    1 
ATOM   886  C  CA   . PRO   B 1 19 ? 8.378   0.397   29.253  1.00 28.88 ? 19  PRO   B CA   1 
ATOM   887  C  C    . PRO   B 1 19 ? 7.342   1.147   30.078  1.00 22.87 ? 19  PRO   B C    1 
ATOM   888  O  O    . PRO   B 1 19 ? 6.639   2.032   29.580  1.00 22.99 ? 19  PRO   B O    1 
ATOM   889  C  CB   . PRO   B 1 19 ? 9.734   1.109   29.305  1.00 31.36 ? 19  PRO   B CB   1 
ATOM   890  C  CG   . PRO   B 1 19 ? 9.743   1.997   28.078  1.00 24.25 ? 19  PRO   B CG   1 
ATOM   891  C  CD   . PRO   B 1 19 ? 9.002   1.206   27.033  1.00 31.32 ? 19  PRO   B CD   1 
ATOM   892  N  N    . HIS   B 1 20 ? 7.258   0.785   31.358  1.00 21.37 ? 20  HIS   B N    1 
ATOM   893  C  CA   . HIS   B 1 20 ? 6.431   1.547   32.293  1.00 21.68 ? 20  HIS   B CA   1 
ATOM   894  C  C    . HIS   B 1 20 ? 6.742   3.030   32.141  1.00 24.82 ? 20  HIS   B C    1 
ATOM   895  O  O    . HIS   B 1 20 ? 7.908   3.439   32.202  1.00 25.04 ? 20  HIS   B O    1 
ATOM   896  C  CB   . HIS   B 1 20 ? 6.687   1.080   33.735  1.00 23.05 ? 20  HIS   B CB   1 
ATOM   897  C  CG   . HIS   B 1 20 ? 6.375   -0.376  33.958  1.00 21.67 ? 20  HIS   B CG   1 
ATOM   898  N  ND1  . HIS   B 1 20 ? 7.228   -1.390  33.571  1.00 23.98 ? 20  HIS   B ND1  1 
ATOM   899  C  CD2  . HIS   B 1 20 ? 5.287   -0.986  34.482  1.00 21.33 ? 20  HIS   B CD2  1 
ATOM   900  C  CE1  . HIS   B 1 20 ? 6.690   -2.558  33.871  1.00 23.52 ? 20  HIS   B CE1  1 
ATOM   901  N  NE2  . HIS   B 1 20 ? 5.513   -2.342  34.428  1.00 22.11 ? 20  HIS   B NE2  1 
ATOM   902  N  N    . TRP   B 1 21 ? 5.699   3.830   31.906  1.00 22.05 ? 21  TRP   B N    1 
ATOM   903  C  CA   . TRP   B 1 21 ? 5.860   5.185   31.377  1.00 20.48 ? 21  TRP   B CA   1 
ATOM   904  C  C    . TRP   B 1 21 ? 5.331   6.223   32.363  1.00 20.08 ? 21  TRP   B C    1 
ATOM   905  O  O    . TRP   B 1 21 ? 4.219   6.056   32.869  1.00 20.94 ? 21  TRP   B O    1 
ATOM   906  C  CB   . TRP   B 1 21 ? 5.096   5.293   30.035  1.00 19.41 ? 21  TRP   B CB   1 
ATOM   907  C  CG   . TRP   B 1 21 ? 5.605   6.403   29.177  1.00 23.00 ? 21  TRP   B CG   1 
ATOM   908  C  CD1  . TRP   B 1 21 ? 5.345   7.740   29.331  1.00 22.40 ? 21  TRP   B CD1  1 
ATOM   909  C  CD2  . TRP   B 1 21 ? 6.485   6.286   28.052  1.00 26.58 ? 21  TRP   B CD2  1 
ATOM   910  N  NE1  . TRP   B 1 21 ? 6.006   8.461   28.359  1.00 22.15 ? 21  TRP   B NE1  1 
ATOM   911  C  CE2  . TRP   B 1 21 ? 6.709   7.590   27.562  1.00 24.71 ? 21  TRP   B CE2  1 
ATOM   912  C  CE3  . TRP   B 1 21 ? 7.094   5.205   27.398  1.00 22.48 ? 21  TRP   B CE3  1 
ATOM   913  C  CZ2  . TRP   B 1 21 ? 7.518   7.839   26.468  1.00 23.09 ? 21  TRP   B CZ2  1 
ATOM   914  C  CZ3  . TRP   B 1 21 ? 7.901   5.462   26.302  1.00 27.16 ? 21  TRP   B CZ3  1 
ATOM   915  C  CH2  . TRP   B 1 21 ? 8.107   6.767   25.849  1.00 26.97 ? 21  TRP   B CH2  1 
ATOM   916  N  N    . PRO   B 1 22 ? 6.062   7.313   32.643  1.00 19.85 ? 22  PRO   B N    1 
ATOM   917  C  CA   . PRO   B 1 22 ? 5.541   8.323   33.581  1.00 21.16 ? 22  PRO   B CA   1 
ATOM   918  C  C    . PRO   B 1 22 ? 4.247   8.923   33.049  1.00 19.32 ? 22  PRO   B C    1 
ATOM   919  O  O    . PRO   B 1 22 ? 4.154   9.300   31.881  1.00 23.49 ? 22  PRO   B O    1 
ATOM   920  C  CB   . PRO   B 1 22 ? 6.660   9.374   33.646  1.00 18.38 ? 22  PRO   B CB   1 
ATOM   921  C  CG   . PRO   B 1 22 ? 7.405   9.236   32.306  1.00 19.46 ? 22  PRO   B CG   1 
ATOM   922  C  CD   . PRO   B 1 22 ? 7.322   7.738   31.999  1.00 21.83 ? 22  PRO   B CD   1 
ATOM   923  N  N    . ALA   B 1 23 ? 3.246   9.023   33.914  1.00 17.30 ? 23  ALA   B N    1 
ATOM   924  C  CA   . ALA   B 1 23 ? 1.927   9.429   33.464  1.00 18.06 ? 23  ALA   B CA   1 
ATOM   925  C  C    . ALA   B 1 23 ? 1.150   9.993   34.645  1.00 19.80 ? 23  ALA   B C    1 
ATOM   926  O  O    . ALA   B 1 23 ? 1.620   9.987   35.786  1.00 20.32 ? 23  ALA   B O    1 
ATOM   927  C  CB   . ALA   B 1 23 ? 1.197   8.242   32.830  1.00 18.64 ? 23  ALA   B CB   1 
ATOM   928  N  N    . ARG   B 1 24 ? -0.053  10.484  34.361  1.00 19.63 ? 24  ARG   B N    1 
ATOM   929  C  CA   . ARG   B 1 24 ? -0.950  10.971  35.403  1.00 20.63 ? 24  ARG   B CA   1 
ATOM   930  C  C    . ARG   B 1 24 ? -2.373  10.542  35.093  1.00 21.76 ? 24  ARG   B C    1 
ATOM   931  O  O    . ARG   B 1 24 ? -2.728  10.311  33.935  1.00 22.11 ? 24  ARG   B O    1 
ATOM   932  C  CB   . ARG   B 1 24 ? -0.904  12.494  35.527  1.00 23.19 ? 24  ARG   B CB   1 
ATOM   933  C  CG   . ARG   B 1 24 ? -1.571  13.219  34.352  1.00 22.84 ? 24  ARG   B CG   1 
ATOM   934  C  CD   . ARG   B 1 24 ? -1.461  14.737  34.485  1.00 24.41 ? 24  ARG   B CD   1 
ATOM   935  N  NE   . ARG   B 1 24 ? -2.030  15.394  33.317  1.00 25.68 ? 24  ARG   B NE   1 
ATOM   936  C  CZ   . ARG   B 1 24 ? -1.752  16.627  32.916  1.00 28.37 ? 24  ARG   B CZ   1 
ATOM   937  N  NH1  . ARG   B 1 24 ? -0.892  17.390  33.572  1.00 28.28 ? 24  ARG   B NH1  1 
ATOM   938  N  NH2  . ARG   B 1 24 ? -2.358  17.110  31.827  1.00 28.69 ? 24  ARG   B NH2  1 
ATOM   939  N  N    . ILE   B 1 25 ? -3.185  10.445  36.143  1.00 24.23 ? 25  ILE   B N    1 
ATOM   940  C  CA   . ILE   B 1 25 ? -4.620  10.271  35.980  1.00 24.47 ? 25  ILE   B CA   1 
ATOM   941  C  C    . ILE   B 1 25 ? -5.206  11.629  35.635  1.00 29.90 ? 25  ILE   B C    1 
ATOM   942  O  O    . ILE   B 1 25 ? -5.075  12.589  36.406  1.00 26.62 ? 25  ILE   B O    1 
ATOM   943  C  CB   . ILE   B 1 25 ? -5.280  9.717   37.252  1.00 26.53 ? 25  ILE   B CB   1 
ATOM   944  C  CG1  . ILE   B 1 25 ? -4.592  8.439   37.785  1.00 24.34 ? 25  ILE   B CG1  1 
ATOM   945  C  CG2  . ILE   B 1 25 ? -6.790  9.527   37.007  1.00 27.74 ? 25  ILE   B CG2  1 
ATOM   946  C  CD1  . ILE   B 1 25 ? -4.532  7.270   36.802  1.00 26.06 ? 25  ILE   B CD1  1 
ATOM   947  N  N    . ASP   B 1 26 ? -5.871  11.706  34.495  1.00 33.58 ? 26  ASP   B N    1 
ATOM   948  C  CA   . ASP   B 1 26 ? -6.487  12.946  34.060  1.00 39.20 ? 26  ASP   B CA   1 
ATOM   949  C  C    . ASP   B 1 26 ? -7.883  13.084  34.641  1.00 40.52 ? 26  ASP   B C    1 
ATOM   950  O  O    . ASP   B 1 26 ? -8.512  12.104  35.037  1.00 40.97 ? 26  ASP   B O    1 
ATOM   951  C  CB   . ASP   B 1 26 ? -6.547  13.007  32.540  1.00 37.62 ? 26  ASP   B CB   1 
ATOM   952  C  CG   . ASP   B 1 26 ? -5.434  13.822  31.972  1.00 36.51 ? 26  ASP   B CG   1 
ATOM   953  O  OD1  . ASP   B 1 26 ? -4.677  14.384  32.798  1.00 35.31 ? 26  ASP   B OD1  1 
ATOM   954  O  OD2  . ASP   B 1 26 ? -5.329  13.912  30.734  1.00 37.13 ? 26  ASP   B OD2  1 
ATOM   955  N  N    . ASP   B 1 27 ? -8.346  14.330  34.717  1.00 43.65 ? 27  ASP   B N    1 
ATOM   956  C  CA   . ASP   B 1 27 ? -9.747  14.589  34.979  1.00 52.12 ? 27  ASP   B CA   1 
ATOM   957  C  C    . ASP   B 1 27 ? -10.525 14.448  33.686  1.00 53.32 ? 27  ASP   B C    1 
ATOM   958  O  O    . ASP   B 1 27 ? -9.993  14.652  32.594  1.00 51.21 ? 27  ASP   B O    1 
ATOM   959  C  CB   . ASP   B 1 27 ? -9.953  15.990  35.567  1.00 52.14 ? 27  ASP   B CB   1 
ATOM   960  C  CG   . ASP   B 1 27 ? -10.894 15.991  36.767  1.00 65.33 ? 27  ASP   B CG   1 
ATOM   961  O  OD1  . ASP   B 1 27 ? -11.925 15.278  36.741  1.00 64.23 ? 27  ASP   B OD1  1 
ATOM   962  O  OD2  . ASP   B 1 27 ? -10.597 16.697  37.751  1.00 63.79 ? 27  ASP   B OD2  1 
ATOM   963  N  N    . ILE   B 1 28 ? -11.791 14.077  33.816  1.00 54.41 ? 28  ILE   B N    1 
ATOM   964  C  CA   . ILE   B 1 28 ? -12.691 13.996  32.676  1.00 57.04 ? 28  ILE   B CA   1 
ATOM   965  C  C    . ILE   B 1 28 ? -13.346 15.362  32.543  1.00 63.64 ? 28  ILE   B C    1 
ATOM   966  O  O    . ILE   B 1 28 ? -14.081 15.795  33.434  1.00 68.47 ? 28  ILE   B O    1 
ATOM   967  C  CB   . ILE   B 1 28 ? -13.723 12.877  32.849  1.00 58.22 ? 28  ILE   B CB   1 
ATOM   968  C  CG1  . ILE   B 1 28 ? -13.018 11.519  32.843  1.00 58.99 ? 28  ILE   B CG1  1 
ATOM   969  C  CG2  . ILE   B 1 28 ? -14.720 12.907  31.732  1.00 61.44 ? 28  ILE   B CG2  1 
ATOM   970  C  CD1  . ILE   B 1 28 ? -12.917 10.857  34.204  1.00 62.28 ? 28  ILE   B CD1  1 
ATOM   971  N  N    . ALA   B 1 29 ? -13.042 16.061  31.451  1.00 66.10 ? 29  ALA   B N    1 
ATOM   972  C  CA   . ALA   B 1 29 ? -13.552 17.413  31.275  1.00 65.86 ? 29  ALA   B CA   1 
ATOM   973  C  C    . ALA   B 1 29 ? -15.066 17.391  31.159  1.00 71.97 ? 29  ALA   B C    1 
ATOM   974  O  O    . ALA   B 1 29 ? -15.663 16.396  30.739  1.00 72.23 ? 29  ALA   B O    1 
ATOM   975  C  CB   . ALA   B 1 29 ? -12.944 18.066  30.033  1.00 65.30 ? 29  ALA   B CB   1 
ATOM   976  N  N    . ASP   B 1 30 ? -15.686 18.503  31.541  1.00 87.26 ? 30  ASP   B N    1 
ATOM   977  C  CA   . ASP   B 1 30 ? -17.134 18.622  31.463  1.00 87.48 ? 30  ASP   B CA   1 
ATOM   978  C  C    . ASP   B 1 30 ? -17.592 18.485  30.016  1.00 88.17 ? 30  ASP   B C    1 
ATOM   979  O  O    . ASP   B 1 30 ? -17.164 19.248  29.146  1.00 88.04 ? 30  ASP   B O    1 
ATOM   980  C  CB   . ASP   B 1 30 ? -17.574 19.961  32.047  1.00 92.82 ? 30  ASP   B CB   1 
ATOM   981  N  N    . GLY   B 1 31 ? -18.454 17.496  29.763  1.00 83.52 ? 31  GLY   B N    1 
ATOM   982  C  CA   . GLY   B 1 31 ? -18.953 17.194  28.440  1.00 82.34 ? 31  GLY   B CA   1 
ATOM   983  C  C    . GLY   B 1 31 ? -18.248 16.047  27.742  1.00 77.37 ? 31  GLY   B C    1 
ATOM   984  O  O    . GLY   B 1 31 ? -18.807 15.477  26.799  1.00 78.11 ? 31  GLY   B O    1 
ATOM   985  N  N    . ALA   B 1 32 ? -17.051 15.683  28.193  1.00 74.33 ? 32  ALA   B N    1 
ATOM   986  C  CA   . ALA   B 1 32 ? -16.204 14.744  27.474  1.00 71.42 ? 32  ALA   B CA   1 
ATOM   987  C  C    . ALA   B 1 32 ? -16.741 13.311  27.570  1.00 78.89 ? 32  ALA   B C    1 
ATOM   988  O  O    . ALA   B 1 32 ? -17.628 12.992  28.367  1.00 75.57 ? 32  ALA   B O    1 
ATOM   989  C  CB   . ALA   B 1 32 ? -14.778 14.807  28.014  1.00 67.52 ? 32  ALA   B CB   1 
ATOM   990  N  N    . VAL   B 1 33 ? -16.165 12.439  26.737  1.00 83.49 ? 33  VAL   B N    1 
ATOM   991  C  CA   . VAL   B 1 33 ? -16.498 11.017  26.749  1.00 78.77 ? 33  VAL   B CA   1 
ATOM   992  C  C    . VAL   B 1 33 ? -15.919 10.355  27.995  1.00 78.51 ? 33  VAL   B C    1 
ATOM   993  O  O    . VAL   B 1 33 ? -14.809 10.681  28.439  1.00 71.04 ? 33  VAL   B O    1 
ATOM   994  C  CB   . VAL   B 1 33 ? -15.968 10.346  25.467  1.00 82.12 ? 33  VAL   B CB   1 
ATOM   995  C  CG1  . VAL   B 1 33 ? -14.580 10.879  25.129  1.00 81.08 ? 33  VAL   B CG1  1 
ATOM   996  C  CG2  . VAL   B 1 33 ? -15.937 8.829   25.602  1.00 80.99 ? 33  VAL   B CG2  1 
ATOM   997  N  N    . LYS   B 1 34 ? -16.694 9.375   28.582  1.00 71.84 ? 34  LYS   B N    1 
ATOM   998  C  CA   . LYS   B 1 34 ? -16.287 8.641   29.772  1.00 67.32 ? 34  LYS   B CA   1 
ATOM   999  C  C    . LYS   B 1 34 ? -15.397 7.448   29.410  1.00 60.06 ? 34  LYS   B C    1 
ATOM   1000 O  O    . LYS   B 1 34 ? -15.485 6.909   28.302  1.00 60.56 ? 34  LYS   B O    1 
ATOM   1001 C  CB   . LYS   B 1 34 ? -17.519 8.159   30.533  1.00 67.67 ? 34  LYS   B CB   1 
ATOM   1002 N  N    . PRO   B 1 35 ? -14.514 7.025   30.314  1.00 58.15 ? 35  PRO   B N    1 
ATOM   1003 C  CA   . PRO   B 1 35 ? -13.680 5.836   30.057  1.00 53.94 ? 35  PRO   B CA   1 
ATOM   1004 C  C    . PRO   B 1 35 ? -14.506 4.560   30.082  1.00 56.99 ? 35  PRO   B C    1 
ATOM   1005 O  O    . PRO   B 1 35 ? -15.583 4.526   30.691  1.00 60.78 ? 35  PRO   B O    1 
ATOM   1006 C  CB   . PRO   B 1 35 ? -12.674 5.861   31.220  1.00 50.62 ? 35  PRO   B CB   1 
ATOM   1007 C  CG   . PRO   B 1 35 ? -12.629 7.295   31.640  1.00 50.51 ? 35  PRO   B CG   1 
ATOM   1008 C  CD   . PRO   B 1 35 ? -14.055 7.756   31.507  1.00 59.21 ? 35  PRO   B CD   1 
ATOM   1009 N  N    . PRO   B 1 36 ? -14.025 3.489   29.449  1.00 55.95 ? 36  PRO   B N    1 
ATOM   1010 C  CA   . PRO   B 1 36 ? -14.707 2.185   29.549  1.00 59.15 ? 36  PRO   B CA   1 
ATOM   1011 C  C    . PRO   B 1 36 ? -14.814 1.759   30.998  1.00 59.88 ? 36  PRO   B C    1 
ATOM   1012 O  O    . PRO   B 1 36 ? -14.097 2.300   31.852  1.00 56.93 ? 36  PRO   B O    1 
ATOM   1013 C  CB   . PRO   B 1 36 ? -13.785 1.237   28.764  1.00 57.10 ? 36  PRO   B CB   1 
ATOM   1014 C  CG   . PRO   B 1 36 ? -12.952 2.118   27.904  1.00 54.45 ? 36  PRO   B CG   1 
ATOM   1015 C  CD   . PRO   B 1 36 ? -12.799 3.414   28.639  1.00 56.08 ? 36  PRO   B CD   1 
ATOM   1016 N  N    . PRO   B 1 37 ? -15.688 0.804   31.325  1.00 64.00 ? 37  PRO   B N    1 
ATOM   1017 C  CA   . PRO   B 1 37 ? -15.816 0.385   32.728  1.00 65.17 ? 37  PRO   B CA   1 
ATOM   1018 C  C    . PRO   B 1 37 ? -14.484 -0.093  33.286  1.00 60.82 ? 37  PRO   B C    1 
ATOM   1019 O  O    . PRO   B 1 37 ? -13.694 -0.725  32.584  1.00 60.17 ? 37  PRO   B O    1 
ATOM   1020 C  CB   . PRO   B 1 37 ? -16.850 -0.750  32.671  1.00 70.62 ? 37  PRO   B CB   1 
ATOM   1021 C  CG   . PRO   B 1 37 ? -16.853 -1.208  31.252  1.00 70.98 ? 37  PRO   B CG   1 
ATOM   1022 C  CD   . PRO   B 1 37 ? -16.595 0.043   30.448  1.00 68.16 ? 37  PRO   B CD   1 
ATOM   1023 N  N    . ASN   B 1 38 ? -14.226 0.256   34.547  1.00 59.62 ? 38  ASN   B N    1 
ATOM   1024 C  CA   . ASN   B 1 38 ? -13.045 -0.122  35.321  1.00 55.79 ? 38  ASN   B CA   1 
ATOM   1025 C  C    . ASN   B 1 38 ? -11.775 0.625   34.919  1.00 50.43 ? 38  ASN   B C    1 
ATOM   1026 O  O    . ASN   B 1 38 ? -10.716 0.344   35.485  1.00 47.11 ? 38  ASN   B O    1 
ATOM   1027 C  CB   . ASN   B 1 38 ? -12.751 -1.625  35.234  1.00 56.71 ? 38  ASN   B CB   1 
ATOM   1028 C  CG   . ASN   B 1 38 ? -13.963 -2.479  35.561  1.00 63.98 ? 38  ASN   B CG   1 
ATOM   1029 O  OD1  . ASN   B 1 38 ? -14.480 -2.443  36.676  1.00 64.79 ? 38  ASN   B OD1  1 
ATOM   1030 N  ND2  . ASN   B 1 38 ? -14.441 -3.229  34.572  1.00 66.56 ? 38  ASN   B ND2  1 
ATOM   1031 N  N    . LYS   B 1 39 ? -11.837 1.560   33.977  1.00 39.76 ? 39  LYS   B N    1 
ATOM   1032 C  CA   . LYS   B 1 39 ? -10.654 2.174   33.393  1.00 36.07 ? 39  LYS   B CA   1 
ATOM   1033 C  C    . LYS   B 1 39 ? -10.588 3.658   33.737  1.00 38.12 ? 39  LYS   B C    1 
ATOM   1034 O  O    . LYS   B 1 39 ? -11.584 4.271   34.132  1.00 34.10 ? 39  LYS   B O    1 
ATOM   1035 C  CB   . LYS   B 1 39 ? -10.641 1.971   31.874  1.00 39.12 ? 39  LYS   B CB   1 
ATOM   1036 C  CG   . LYS   B 1 39 ? -10.828 0.503   31.469  1.00 38.58 ? 39  LYS   B CG   1 
ATOM   1037 C  CD   . LYS   B 1 39 ? -9.695  0.010   30.577  1.00 37.43 ? 39  LYS   B CD   1 
ATOM   1038 C  CE   . LYS   B 1 39 ? -9.778  -1.485  30.362  1.00 43.17 ? 39  LYS   B CE   1 
ATOM   1039 N  NZ   . LYS   B 1 39 ? -9.403  -1.848  28.971  1.00 49.32 ? 39  LYS   B NZ   1 
ATOM   1040 N  N    . TYR   B 1 40 ? -9.383  4.220   33.622  1.00 25.93 ? 40  TYR   B N    1 
ATOM   1041 C  CA   . TYR   B 1 40 ? -9.091  5.615   33.948  1.00 29.04 ? 40  TYR   B CA   1 
ATOM   1042 C  C    . TYR   B 1 40 ? -8.491  6.320   32.740  1.00 34.28 ? 40  TYR   B C    1 
ATOM   1043 O  O    . TYR   B 1 40 ? -7.778  5.692   31.943  1.00 29.20 ? 40  TYR   B O    1 
ATOM   1044 C  CB   . TYR   B 1 40 ? -8.097  5.751   35.112  1.00 29.67 ? 40  TYR   B CB   1 
ATOM   1045 C  CG   . TYR   B 1 40 ? -8.588  5.225   36.428  1.00 29.54 ? 40  TYR   B CG   1 
ATOM   1046 C  CD1  . TYR   B 1 40 ? -8.455  3.885   36.757  1.00 24.65 ? 40  TYR   B CD1  1 
ATOM   1047 C  CD2  . TYR   B 1 40 ? -9.183  6.073   37.352  1.00 31.77 ? 40  TYR   B CD2  1 
ATOM   1048 C  CE1  . TYR   B 1 40 ? -8.909  3.410   37.963  1.00 29.82 ? 40  TYR   B CE1  1 
ATOM   1049 C  CE2  . TYR   B 1 40 ? -9.637  5.607   38.560  1.00 32.96 ? 40  TYR   B CE2  1 
ATOM   1050 C  CZ   . TYR   B 1 40 ? -9.501  4.273   38.861  1.00 30.63 ? 40  TYR   B CZ   1 
ATOM   1051 O  OH   . TYR   B 1 40 ? -9.945  3.810   40.081  1.00 30.93 ? 40  TYR   B OH   1 
ATOM   1052 N  N    . PRO   B 1 41 ? -8.752  7.622   32.584  1.00 28.53 ? 41  PRO   B N    1 
ATOM   1053 C  CA   . PRO   B 1 41 ? -8.103  8.416   31.531  1.00 28.96 ? 41  PRO   B CA   1 
ATOM   1054 C  C    . PRO   B 1 41 ? -6.676  8.754   31.933  1.00 28.19 ? 41  PRO   B C    1 
ATOM   1055 O  O    . PRO   B 1 41 ? -6.434  9.391   32.964  1.00 29.42 ? 41  PRO   B O    1 
ATOM   1056 C  CB   . PRO   B 1 41 ? -8.981  9.671   31.446  1.00 31.49 ? 41  PRO   B CB   1 
ATOM   1057 C  CG   . PRO   B 1 41 ? -9.558  9.813   32.797  1.00 33.40 ? 41  PRO   B CG   1 
ATOM   1058 C  CD   . PRO   B 1 41 ? -9.739  8.408   33.341  1.00 32.86 ? 41  PRO   B CD   1 
ATOM   1059 N  N    . ILE   B 1 42 ? -5.728  8.316   31.120  1.00 28.83 ? 42  ILE   B N    1 
ATOM   1060 C  CA   . ILE   B 1 42 ? -4.309  8.417   31.424  1.00 23.96 ? 42  ILE   B CA   1 
ATOM   1061 C  C    . ILE   B 1 42 ? -3.702  9.439   30.479  1.00 22.77 ? 42  ILE   B C    1 
ATOM   1062 O  O    . ILE   B 1 42 ? -4.048  9.471   29.297  1.00 24.18 ? 42  ILE   B O    1 
ATOM   1063 C  CB   . ILE   B 1 42 ? -3.613  7.049   31.260  1.00 25.24 ? 42  ILE   B CB   1 
ATOM   1064 C  CG1  . ILE   B 1 42 ? -4.311  5.951   32.096  1.00 19.67 ? 42  ILE   B CG1  1 
ATOM   1065 C  CG2  . ILE   B 1 42 ? -2.110  7.162   31.552  1.00 25.75 ? 42  ILE   B CG2  1 
ATOM   1066 C  CD1  . ILE   B 1 42 ? -4.583  6.319   33.526  1.00 19.60 ? 42  ILE   B CD1  1 
ATOM   1067 N  N    . PHE   B 1 43 ? -2.789  10.261  30.988  1.00 20.71 ? 43  PHE   B N    1 
ATOM   1068 C  CA   . PHE   B 1 43 ? -2.024  11.200  30.170  1.00 22.64 ? 43  PHE   B CA   1 
ATOM   1069 C  C    . PHE   B 1 43 ? -0.558  10.854  30.329  1.00 20.71 ? 43  PHE   B C    1 
ATOM   1070 O  O    . PHE   B 1 43 ? -0.043  10.878  31.454  1.00 21.59 ? 43  PHE   B O    1 
ATOM   1071 C  CB   . PHE   B 1 43 ? -2.272  12.647  30.608  1.00 24.52 ? 43  PHE   B CB   1 
ATOM   1072 C  CG   . PHE   B 1 43 ? -1.373  13.661  29.934  1.00 28.68 ? 43  PHE   B CG   1 
ATOM   1073 C  CD1  . PHE   B 1 43 ? -1.750  14.252  28.741  1.00 26.71 ? 43  PHE   B CD1  1 
ATOM   1074 C  CD2  . PHE   B 1 43 ? -0.156  14.044  30.511  1.00 28.66 ? 43  PHE   B CD2  1 
ATOM   1075 C  CE1  . PHE   B 1 43 ? -0.928  15.193  28.115  1.00 27.98 ? 43  PHE   B CE1  1 
ATOM   1076 C  CE2  . PHE   B 1 43 ? 0.661   15.005  29.897  1.00 25.21 ? 43  PHE   B CE2  1 
ATOM   1077 C  CZ   . PHE   B 1 43 ? 0.276   15.570  28.703  1.00 27.18 ? 43  PHE   B CZ   1 
ATOM   1078 N  N    . PHE   B 1 44 ? 0.107   10.534  29.220  1.00 21.83 ? 44  PHE   B N    1 
ATOM   1079 C  CA   . PHE   B 1 44 ? 1.507   10.120  29.232  1.00 22.42 ? 44  PHE   B CA   1 
ATOM   1080 C  C    . PHE   B 1 44 ? 2.413   11.340  29.121  1.00 25.30 ? 44  PHE   B C    1 
ATOM   1081 O  O    . PHE   B 1 44 ? 2.350   12.081  28.137  1.00 26.82 ? 44  PHE   B O    1 
ATOM   1082 C  CB   . PHE   B 1 44 ? 1.808   9.145   28.089  1.00 23.03 ? 44  PHE   B CB   1 
ATOM   1083 C  CG   . PHE   B 1 44 ? 1.099   7.821   28.221  1.00 25.72 ? 44  PHE   B CG   1 
ATOM   1084 C  CD1  . PHE   B 1 44 ? 1.636   6.812   29.007  1.00 22.25 ? 44  PHE   B CD1  1 
ATOM   1085 C  CD2  . PHE   B 1 44 ? -0.101  7.586   27.571  1.00 27.68 ? 44  PHE   B CD2  1 
ATOM   1086 C  CE1  . PHE   B 1 44 ? 0.989   5.576   29.135  1.00 24.48 ? 44  PHE   B CE1  1 
ATOM   1087 C  CE2  . PHE   B 1 44 ? -0.752  6.366   27.696  1.00 30.69 ? 44  PHE   B CE2  1 
ATOM   1088 C  CZ   . PHE   B 1 44 ? -0.207  5.360   28.477  1.00 23.38 ? 44  PHE   B CZ   1 
ATOM   1089 N  N    . PHE   B 1 45 ? 3.279   11.524  30.109  1.00 21.96 ? 45  PHE   B N    1 
ATOM   1090 C  CA   . PHE   B 1 45 ? 4.214   12.634  30.070  1.00 22.53 ? 45  PHE   B CA   1 
ATOM   1091 C  C    . PHE   B 1 45 ? 5.196   12.455  28.912  1.00 25.85 ? 45  PHE   B C    1 
ATOM   1092 O  O    . PHE   B 1 45 ? 5.491   11.339  28.494  1.00 24.89 ? 45  PHE   B O    1 
ATOM   1093 C  CB   . PHE   B 1 45 ? 4.954   12.729  31.397  1.00 22.57 ? 45  PHE   B CB   1 
ATOM   1094 C  CG   . PHE   B 1 45 ? 4.095   13.242  32.516  1.00 22.52 ? 45  PHE   B CG   1 
ATOM   1095 C  CD1  . PHE   B 1 45 ? 3.606   14.544  32.483  1.00 23.52 ? 45  PHE   B CD1  1 
ATOM   1096 C  CD2  . PHE   B 1 45 ? 3.746   12.427  33.575  1.00 21.84 ? 45  PHE   B CD2  1 
ATOM   1097 C  CE1  . PHE   B 1 45 ? 2.808   15.044  33.498  1.00 24.45 ? 45  PHE   B CE1  1 
ATOM   1098 C  CE2  . PHE   B 1 45 ? 2.935   12.926  34.607  1.00 22.25 ? 45  PHE   B CE2  1 
ATOM   1099 C  CZ   . PHE   B 1 45 ? 2.473   14.239  34.558  1.00 23.30 ? 45  PHE   B CZ   1 
ATOM   1100 N  N    . GLY   B 1 46 ? 5.703   13.567  28.394  1.00 24.77 ? 46  GLY   B N    1 
ATOM   1101 C  CA   . GLY   B 1 46 ? 6.672   13.488  27.315  1.00 26.80 ? 46  GLY   B CA   1 
ATOM   1102 C  C    . GLY   B 1 46 ? 6.039   13.380  25.942  1.00 29.61 ? 46  GLY   B C    1 
ATOM   1103 O  O    . GLY   B 1 46 ? 6.140   14.314  25.141  1.00 28.50 ? 46  GLY   B O    1 
ATOM   1104 N  N    . THR   B 1 47 ? 5.404   12.238  25.649  1.00 26.15 ? 47  THR   B N    1 
ATOM   1105 C  CA   . THR   B 1 47 ? 4.657   12.109  24.399  1.00 27.26 ? 47  THR   B CA   1 
ATOM   1106 C  C    . THR   B 1 47 ? 3.372   12.927  24.426  1.00 28.00 ? 47  THR   B C    1 
ATOM   1107 O  O    . THR   B 1 47 ? 2.889   13.350  23.372  1.00 29.11 ? 47  THR   B O    1 
ATOM   1108 C  CB   . THR   B 1 47 ? 4.307   10.645  24.120  1.00 27.49 ? 47  THR   B CB   1 
ATOM   1109 O  OG1  . THR   B 1 47 ? 3.352   10.199  25.089  1.00 25.07 ? 47  THR   B OG1  1 
ATOM   1110 C  CG2  . THR   B 1 47 ? 5.546   9.756   24.184  1.00 26.85 ? 47  THR   B CG2  1 
ATOM   1111 N  N    . HIS   B 1 48 ? 2.804   13.140  25.613  1.00 25.96 ? 48  HIS   B N    1 
ATOM   1112 C  CA   . HIS   B 1 48 ? 1.517   13.814  25.792  1.00 28.43 ? 48  HIS   B CA   1 
ATOM   1113 C  C    . HIS   B 1 48 ? 0.381   13.063  25.115  1.00 31.80 ? 48  HIS   B C    1 
ATOM   1114 O  O    . HIS   B 1 48 ? -0.627  13.656  24.726  1.00 34.11 ? 48  HIS   B O    1 
ATOM   1115 C  CB   . HIS   B 1 48 ? 1.552   15.270  25.310  1.00 28.45 ? 48  HIS   B CB   1 
ATOM   1116 C  CG   . HIS   B 1 48 ? 2.747   16.025  25.781  1.00 29.24 ? 48  HIS   B CG   1 
ATOM   1117 N  ND1  . HIS   B 1 48 ? 3.383   16.975  25.008  1.00 34.54 ? 48  HIS   B ND1  1 
ATOM   1118 C  CD2  . HIS   B 1 48 ? 3.434   15.964  26.945  1.00 27.20 ? 48  HIS   B CD2  1 
ATOM   1119 C  CE1  . HIS   B 1 48 ? 4.413   17.462  25.676  1.00 33.43 ? 48  HIS   B CE1  1 
ATOM   1120 N  NE2  . HIS   B 1 48 ? 4.467   16.863  26.854  1.00 32.05 ? 48  HIS   B NE2  1 
ATOM   1121 N  N    . GLU   B 1 49 ? 0.521   11.751  24.970  1.00 26.86 ? 49  GLU   B N    1 
ATOM   1122 C  CA   . GLU   B 1 49 ? -0.578  10.965  24.441  1.00 31.82 ? 49  GLU   B CA   1 
ATOM   1123 C  C    . GLU   B 1 49 ? -1.533  10.605  25.579  1.00 29.35 ? 49  GLU   B C    1 
ATOM   1124 O  O    . GLU   B 1 49 ? -1.232  10.794  26.761  1.00 29.48 ? 49  GLU   B O    1 
ATOM   1125 C  CB   . GLU   B 1 49 ? -0.042  9.716   23.733  1.00 31.64 ? 49  GLU   B CB   1 
ATOM   1126 C  CG   . GLU   B 1 49 ? 0.898   10.048  22.573  1.00 32.71 ? 49  GLU   B CG   1 
ATOM   1127 C  CD   . GLU   B 1 49 ? 1.192   8.865   21.679  1.00 37.97 ? 49  GLU   B CD   1 
ATOM   1128 O  OE1  . GLU   B 1 49 ? 1.212   7.728   22.201  1.00 43.77 ? 49  GLU   B OE1  1 
ATOM   1129 O  OE2  . GLU   B 1 49 ? 1.424   9.068   20.464  1.00 45.73 ? 49  GLU   B OE2  1 
ATOM   1130 N  N    . THR   B 1 50 ? -2.701  10.082  25.210  1.00 26.71 ? 50  THR   B N    1 
ATOM   1131 C  CA   . THR   B 1 50 ? -3.718  9.684   26.166  1.00 26.27 ? 50  THR   B CA   1 
ATOM   1132 C  C    . THR   B 1 50 ? -4.235  8.307   25.790  1.00 36.49 ? 50  THR   B C    1 
ATOM   1133 O  O    . THR   B 1 50 ? -4.293  7.955   24.608  1.00 32.02 ? 50  THR   B O    1 
ATOM   1134 C  CB   . THR   B 1 50 ? -4.889  10.667  26.214  1.00 29.60 ? 50  THR   B CB   1 
ATOM   1135 O  OG1  . THR   B 1 50 ? -5.462  10.754  24.907  1.00 31.39 ? 50  THR   B OG1  1 
ATOM   1136 C  CG2  . THR   B 1 50 ? -4.405  12.056  26.651  1.00 31.21 ? 50  THR   B CG2  1 
ATOM   1137 N  N    . ALA   B 1 51 ? -4.584  7.534   26.815  1.00 30.13 ? 51  ALA   B N    1 
ATOM   1138 C  CA   . ALA   B 1 51 ? -5.194  6.224   26.644  1.00 24.82 ? 51  ALA   B CA   1 
ATOM   1139 C  C    . ALA   B 1 51 ? -6.071  5.947   27.848  1.00 26.53 ? 51  ALA   B C    1 
ATOM   1140 O  O    . ALA   B 1 51 ? -6.020  6.657   28.856  1.00 30.44 ? 51  ALA   B O    1 
ATOM   1141 C  CB   . ALA   B 1 51 ? -4.150  5.117   26.491  1.00 28.09 ? 51  ALA   B CB   1 
ATOM   1142 N  N    . PHE   B 1 52 ? -6.887  4.904   27.737  1.00 27.78 ? 52  PHE   B N    1 
ATOM   1143 C  CA   . PHE   B 1 52 ? -7.659  4.403   28.865  1.00 28.83 ? 52  PHE   B CA   1 
ATOM   1144 C  C    . PHE   B 1 52 ? -6.983  3.146   29.394  1.00 32.06 ? 52  PHE   B C    1 
ATOM   1145 O  O    . PHE   B 1 52 ? -6.669  2.235   28.618  1.00 29.42 ? 52  PHE   B O    1 
ATOM   1146 C  CB   . PHE   B 1 52 ? -9.102  4.098   28.464  1.00 31.24 ? 52  PHE   B CB   1 
ATOM   1147 C  CG   . PHE   B 1 52 ? -9.906  5.316   28.084  1.00 36.43 ? 52  PHE   B CG   1 
ATOM   1148 C  CD1  . PHE   B 1 52 ? -10.074 6.359   28.978  1.00 34.76 ? 52  PHE   B CD1  1 
ATOM   1149 C  CD2  . PHE   B 1 52 ? -10.511 5.403   26.845  1.00 36.78 ? 52  PHE   B CD2  1 
ATOM   1150 C  CE1  . PHE   B 1 52 ? -10.823 7.474   28.635  1.00 40.92 ? 52  PHE   B CE1  1 
ATOM   1151 C  CE2  . PHE   B 1 52 ? -11.260 6.509   26.503  1.00 42.06 ? 52  PHE   B CE2  1 
ATOM   1152 C  CZ   . PHE   B 1 52 ? -11.413 7.545   27.395  1.00 36.06 ? 52  PHE   B CZ   1 
ATOM   1153 N  N    . LEU   B 1 53 ? -6.748  3.105   30.702  1.00 26.76 ? 53  LEU   B N    1 
ATOM   1154 C  CA   . LEU   B 1 53 ? -6.103  1.956   31.325  1.00 31.53 ? 53  LEU   B CA   1 
ATOM   1155 C  C    . LEU   B 1 53 ? -6.815  1.580   32.616  1.00 27.57 ? 53  LEU   B C    1 
ATOM   1156 O  O    . LEU   B 1 53 ? -7.392  2.430   33.303  1.00 26.37 ? 53  LEU   B O    1 
ATOM   1157 C  CB   . LEU   B 1 53 ? -4.624  2.232   31.636  1.00 26.35 ? 53  LEU   B CB   1 
ATOM   1158 C  CG   . LEU   B 1 53 ? -3.691  2.273   30.430  1.00 28.20 ? 53  LEU   B CG   1 
ATOM   1159 C  CD1  . LEU   B 1 53 ? -2.267  2.487   30.903  1.00 24.35 ? 53  LEU   B CD1  1 
ATOM   1160 C  CD2  . LEU   B 1 53 ? -3.831  0.985   29.634  1.00 30.32 ? 53  LEU   B CD2  1 
ATOM   1161 N  N    . GLY   B 1 54 ? -6.735  0.299   32.945  1.00 24.15 ? 54  GLY   B N    1 
ATOM   1162 C  CA   . GLY   B 1 54 ? -7.232  -0.224  34.195  1.00 23.36 ? 54  GLY   B CA   1 
ATOM   1163 C  C    . GLY   B 1 54 ? -6.110  -0.346  35.206  1.00 27.29 ? 54  GLY   B C    1 
ATOM   1164 O  O    . GLY   B 1 54 ? -4.922  -0.259  34.870  1.00 25.74 ? 54  GLY   B O    1 
ATOM   1165 N  N    . PRO   B 1 55 ? -6.468  -0.556  36.471  1.00 29.14 ? 55  PRO   B N    1 
ATOM   1166 C  CA   . PRO   B 1 55 ? -5.455  -0.503  37.534  1.00 25.86 ? 55  PRO   B CA   1 
ATOM   1167 C  C    . PRO   B 1 55 ? -4.375  -1.564  37.461  1.00 23.29 ? 55  PRO   B C    1 
ATOM   1168 O  O    . PRO   B 1 55 ? -3.313  -1.351  38.051  1.00 24.69 ? 55  PRO   B O    1 
ATOM   1169 C  CB   . PRO   B 1 55 ? -6.293  -0.630  38.816  1.00 26.48 ? 55  PRO   B CB   1 
ATOM   1170 C  CG   . PRO   B 1 55 ? -7.624  -1.129  38.369  1.00 32.37 ? 55  PRO   B CG   1 
ATOM   1171 C  CD   . PRO   B 1 55 ? -7.835  -0.553  37.028  1.00 30.55 ? 55  PRO   B CD   1 
ATOM   1172 N  N    . LYS   B 1 56 ? -4.578  -2.689  36.766  1.00 22.60 ? 56  LYS   B N    1 
ATOM   1173 C  CA   . LYS   B 1 56 ? -3.488  -3.658  36.699  1.00 25.34 ? 56  LYS   B CA   1 
ATOM   1174 C  C    . LYS   B 1 56 ? -2.280  -3.087  35.962  1.00 22.29 ? 56  LYS   B C    1 
ATOM   1175 O  O    . LYS   B 1 56 ? -1.170  -3.606  36.115  1.00 24.81 ? 56  LYS   B O    1 
ATOM   1176 C  CB   . LYS   B 1 56 ? -3.969  -4.961  36.045  1.00 27.60 ? 56  LYS   B CB   1 
ATOM   1177 C  CG   . LYS   B 1 56 ? -4.306  -4.814  34.583  1.00 31.35 ? 56  LYS   B CG   1 
ATOM   1178 C  CD   . LYS   B 1 56 ? -4.304  -6.150  33.851  1.00 34.57 ? 56  LYS   B CD   1 
ATOM   1179 C  CE   . LYS   B 1 56 ? -4.483  -5.922  32.339  1.00 38.61 ? 56  LYS   B CE   1 
ATOM   1180 N  NZ   . LYS   B 1 56 ? -3.208  -5.553  31.620  1.00 37.88 ? 56  LYS   B NZ   1 
ATOM   1181 N  N    . ASP   B 1 57 ? -2.473  -2.032  35.173  1.00 21.57 ? 57  ASP   B N    1 
ATOM   1182 C  CA   . ASP   B 1 57 ? -1.397  -1.409  34.415  1.00 21.59 ? 57  ASP   B CA   1 
ATOM   1183 C  C    . ASP   B 1 57 ? -0.953  -0.089  35.024  1.00 21.56 ? 57  ASP   B C    1 
ATOM   1184 O  O    . ASP   B 1 57 ? -0.194  0.660   34.391  1.00 21.87 ? 57  ASP   B O    1 
ATOM   1185 C  CB   . ASP   B 1 57 ? -1.831  -1.196  32.967  1.00 20.53 ? 57  ASP   B CB   1 
ATOM   1186 C  CG   . ASP   B 1 57 ? -1.918  -2.493  32.190  1.00 32.00 ? 57  ASP   B CG   1 
ATOM   1187 O  OD1  . ASP   B 1 57 ? -1.031  -3.359  32.364  1.00 28.44 ? 57  ASP   B OD1  1 
ATOM   1188 O  OD2  . ASP   B 1 57 ? -2.875  -2.643  31.411  1.00 24.86 ? 57  ASP   B OD2  1 
ATOM   1189 N  N    . LEU   B 1 58 ? -1.392  0.219   36.237  1.00 20.39 ? 58  LEU   B N    1 
ATOM   1190 C  CA   . LEU   B 1 58 ? -1.135  1.520   36.849  1.00 20.01 ? 58  LEU   B CA   1 
ATOM   1191 C  C    . LEU   B 1 58 ? -0.351  1.313   38.132  1.00 24.14 ? 58  LEU   B C    1 
ATOM   1192 O  O    . LEU   B 1 58 ? -0.804  0.580   39.025  1.00 23.00 ? 58  LEU   B O    1 
ATOM   1193 C  CB   . LEU   B 1 58 ? -2.448  2.252   37.127  1.00 23.05 ? 58  LEU   B CB   1 
ATOM   1194 C  CG   . LEU   B 1 58 ? -3.249  2.563   35.857  1.00 23.95 ? 58  LEU   B CG   1 
ATOM   1195 C  CD1  . LEU   B 1 58 ? -4.620  3.118   36.239  1.00 22.06 ? 58  LEU   B CD1  1 
ATOM   1196 C  CD2  . LEU   B 1 58 ? -2.480  3.556   34.968  1.00 20.58 ? 58  LEU   B CD2  1 
ATOM   1197 N  N    . PHE   B 1 59 ? 0.820   1.951   38.212  1.00 20.38 ? 59  PHE   B N    1 
ATOM   1198 C  CA   . PHE   B 1 59 ? 1.769   1.789   39.309  1.00 22.89 ? 59  PHE   B CA   1 
ATOM   1199 C  C    . PHE   B 1 59 ? 1.991   3.125   40.004  1.00 22.10 ? 59  PHE   B C    1 
ATOM   1200 O  O    . PHE   B 1 59 ? 2.377   4.099   39.341  1.00 22.09 ? 59  PHE   B O    1 
ATOM   1201 C  CB   . PHE   B 1 59 ? 3.094   1.225   38.790  1.00 21.75 ? 59  PHE   B CB   1 
ATOM   1202 C  CG   . PHE   B 1 59 ? 2.959   -0.148  38.160  1.00 21.74 ? 59  PHE   B CG   1 
ATOM   1203 C  CD1  . PHE   B 1 59 ? 2.481   -0.290  36.864  1.00 20.83 ? 59  PHE   B CD1  1 
ATOM   1204 C  CD2  . PHE   B 1 59 ? 3.267   -1.289  38.892  1.00 23.93 ? 59  PHE   B CD2  1 
ATOM   1205 C  CE1  . PHE   B 1 59 ? 2.336   -1.539  36.285  1.00 21.25 ? 59  PHE   B CE1  1 
ATOM   1206 C  CE2  . PHE   B 1 59 ? 3.131   -2.561  38.315  1.00 23.64 ? 59  PHE   B CE2  1 
ATOM   1207 C  CZ   . PHE   B 1 59 ? 2.651   -2.687  37.020  1.00 23.42 ? 59  PHE   B CZ   1 
ATOM   1208 N  N    . PRO   B 1 60 ? 1.733   3.248   41.305  1.00 26.82 ? 60  PRO   B N    1 
ATOM   1209 C  CA   . PRO   B 1 60 ? 1.884   4.563   41.950  1.00 24.50 ? 60  PRO   B CA   1 
ATOM   1210 C  C    . PRO   B 1 60 ? 3.312   5.080   41.823  1.00 27.46 ? 60  PRO   B C    1 
ATOM   1211 O  O    . PRO   B 1 60 ? 4.281   4.340   41.996  1.00 30.09 ? 60  PRO   B O    1 
ATOM   1212 C  CB   . PRO   B 1 60 ? 1.488   4.313   43.408  1.00 26.59 ? 60  PRO   B CB   1 
ATOM   1213 C  CG   . PRO   B 1 60 ? 0.675   3.060   43.396  1.00 34.81 ? 60  PRO   B CG   1 
ATOM   1214 C  CD   . PRO   B 1 60 ? 1.025   2.269   42.154  1.00 29.06 ? 60  PRO   B CD   1 
ATOM   1215 N  N    . TYR   B 1 61 ? 3.426   6.376   41.508  1.00 28.44 ? 61  TYR   B N    1 
ATOM   1216 C  CA   . TYR   B 1 61 ? 4.713   6.943   41.111  1.00 27.93 ? 61  TYR   B CA   1 
ATOM   1217 C  C    . TYR   B 1 61 ? 5.742   6.898   42.235  1.00 30.96 ? 61  TYR   B C    1 
ATOM   1218 O  O    . TYR   B 1 61 ? 6.882   6.474   42.023  1.00 34.84 ? 61  TYR   B O    1 
ATOM   1219 C  CB   . TYR   B 1 61 ? 4.527   8.377   40.627  1.00 29.72 ? 61  TYR   B CB   1 
ATOM   1220 C  CG   . TYR   B 1 61 ? 5.826   9.094   40.348  1.00 28.57 ? 61  TYR   B CG   1 
ATOM   1221 C  CD1  . TYR   B 1 61 ? 6.557   8.830   39.198  1.00 32.70 ? 61  TYR   B CD1  1 
ATOM   1222 C  CD2  . TYR   B 1 61 ? 6.331   10.007  41.246  1.00 38.52 ? 61  TYR   B CD2  1 
ATOM   1223 C  CE1  . TYR   B 1 61 ? 7.750   9.498   38.951  1.00 31.25 ? 61  TYR   B CE1  1 
ATOM   1224 C  CE2  . TYR   B 1 61 ? 7.511   10.679  41.011  1.00 41.52 ? 61  TYR   B CE2  1 
ATOM   1225 C  CZ   . TYR   B 1 61 ? 8.220   10.415  39.870  1.00 38.54 ? 61  TYR   B CZ   1 
ATOM   1226 O  OH   . TYR   B 1 61 ? 9.397   11.092  39.659  1.00 34.58 ? 61  TYR   B OH   1 
ATOM   1227 N  N    . ASP   B 1 62 ? 5.391   7.381   43.420  1.00 32.58 ? 62  ASP   B N    1 
ATOM   1228 C  CA   . ASP   B 1 62 ? 6.431   7.492   44.438  1.00 34.12 ? 62  ASP   B CA   1 
ATOM   1229 C  C    . ASP   B 1 62 ? 6.881   6.123   44.934  1.00 33.21 ? 62  ASP   B C    1 
ATOM   1230 O  O    . ASP   B 1 62 ? 8.065   5.938   45.228  1.00 41.51 ? 62  ASP   B O    1 
ATOM   1231 C  CB   . ASP   B 1 62 ? 5.969   8.381   45.592  1.00 40.10 ? 62  ASP   B CB   1 
ATOM   1232 C  CG   . ASP   B 1 62 ? 4.621   7.981   46.123  1.00 53.97 ? 62  ASP   B CG   1 
ATOM   1233 O  OD1  . ASP   B 1 62 ? 3.995   7.069   45.527  1.00 52.47 ? 62  ASP   B OD1  1 
ATOM   1234 O  OD2  . ASP   B 1 62 ? 4.189   8.577   47.132  1.00 61.87 ? 62  ASP   B OD2  1 
ATOM   1235 N  N    . LYS   B 1 63 ? 5.975   5.146   44.988  1.00 34.59 ? 63  LYS   B N    1 
ATOM   1236 C  CA   . LYS   B 1 63 ? 6.380   3.791   45.343  1.00 33.18 ? 63  LYS   B CA   1 
ATOM   1237 C  C    . LYS   B 1 63 ? 7.340   3.199   44.309  1.00 32.06 ? 63  LYS   B C    1 
ATOM   1238 O  O    . LYS   B 1 63 ? 8.268   2.466   44.669  1.00 33.79 ? 63  LYS   B O    1 
ATOM   1239 C  CB   . LYS   B 1 63 ? 5.139   2.896   45.510  1.00 44.26 ? 63  LYS   B CB   1 
ATOM   1240 C  CG   . LYS   B 1 63 ? 5.409   1.353   45.566  1.00 33.24 ? 63  LYS   B CG   1 
ATOM   1241 C  CD   . LYS   B 1 63 ? 4.102   0.544   45.696  1.00 39.35 ? 63  LYS   B CD   1 
ATOM   1242 C  CE   . LYS   B 1 63 ? 4.317   -1.002  45.736  1.00 37.32 ? 63  LYS   B CE   1 
ATOM   1243 N  NZ   . LYS   B 1 63 ? 5.285   -1.489  46.747  1.00 41.66 ? 63  LYS   B NZ   1 
ATOM   1244 N  N    . CYS   B 1 64 ? 7.146   3.504   43.025  1.00 30.40 ? 64  CYS   B N    1 
ATOM   1245 C  CA   . CYS   B 1 64 ? 7.812   2.758   41.956  1.00 30.72 ? 64  CYS   B CA   1 
ATOM   1246 C  C    . CYS   B 1 64 ? 8.842   3.557   41.169  1.00 30.95 ? 64  CYS   B C    1 
ATOM   1247 O  O    . CYS   B 1 64 ? 9.433   3.018   40.223  1.00 30.16 ? 64  CYS   B O    1 
ATOM   1248 C  CB   . CYS   B 1 64 ? 6.760   2.212   40.980  1.00 31.31 ? 64  CYS   B CB   1 
ATOM   1249 S  SG   . CYS   B 1 64 ? 5.614   1.072   41.797  1.00 39.47 ? 64  CYS   B SG   1 
ATOM   1250 N  N    . LYS   B 1 65 ? 9.082   4.814   41.519  1.00 29.30 ? 65  LYS   B N    1 
ATOM   1251 C  CA   . LYS   B 1 65 ? 9.937   5.643   40.678  1.00 29.87 ? 65  LYS   B CA   1 
ATOM   1252 C  C    . LYS   B 1 65 ? 11.377  5.158   40.667  1.00 33.41 ? 65  LYS   B C    1 
ATOM   1253 O  O    . LYS   B 1 65 ? 12.066  5.319   39.658  1.00 37.28 ? 65  LYS   B O    1 
ATOM   1254 C  CB   . LYS   B 1 65 ? 9.836   7.107   41.117  1.00 30.40 ? 65  LYS   B CB   1 
ATOM   1255 C  CG   . LYS   B 1 65 ? 10.285  7.392   42.540  1.00 38.34 ? 65  LYS   B CG   1 
ATOM   1256 C  CD   . LYS   B 1 65 ? 10.266  8.885   42.810  1.00 44.38 ? 65  LYS   B CD   1 
ATOM   1257 C  CE   . LYS   B 1 65 ? 10.712  9.214   44.222  1.00 41.68 ? 65  LYS   B CE   1 
ATOM   1258 N  NZ   . LYS   B 1 65 ? 11.191  10.620  44.337  1.00 51.64 ? 65  LYS   B NZ   1 
ATOM   1259 N  N    . ASP   B 1 66 ? 11.853  4.546   41.749  1.00 33.28 ? 66  ASP   B N    1 
ATOM   1260 C  CA   . ASP   B 1 66 ? 13.227  4.058   41.725  1.00 35.37 ? 66  ASP   B CA   1 
ATOM   1261 C  C    . ASP   B 1 66 ? 13.368  2.840   40.820  1.00 35.26 ? 66  ASP   B C    1 
ATOM   1262 O  O    . ASP   B 1 66 ? 14.421  2.644   40.211  1.00 38.26 ? 66  ASP   B O    1 
ATOM   1263 C  CB   . ASP   B 1 66 ? 13.705  3.761   43.148  1.00 44.86 ? 66  ASP   B CB   1 
ATOM   1264 C  CG   . ASP   B 1 66 ? 13.762  5.021   44.011  1.00 53.30 ? 66  ASP   B CG   1 
ATOM   1265 O  OD1  . ASP   B 1 66 ? 13.537  6.126   43.458  1.00 53.54 ? 66  ASP   B OD1  1 
ATOM   1266 O  OD2  . ASP   B 1 66 ? 14.051  4.915   45.231  1.00 61.65 ? 66  ASP   B OD2  1 
ATOM   1267 N  N    . LYS   B 1 67 ? 12.313  2.037   40.688  1.00 37.19 ? 67  LYS   B N    1 
ATOM   1268 C  CA   . LYS   B 1 67 ? 12.344  0.881   39.797  1.00 34.44 ? 67  LYS   B CA   1 
ATOM   1269 C  C    . LYS   B 1 67 ? 12.198  1.297   38.338  1.00 30.48 ? 67  LYS   B C    1 
ATOM   1270 O  O    . LYS   B 1 67 ? 12.975  0.868   37.481  1.00 34.69 ? 67  LYS   B O    1 
ATOM   1271 C  CB   . LYS   B 1 67 ? 11.232  -0.095  40.174  1.00 42.06 ? 67  LYS   B CB   1 
ATOM   1272 C  CG   . LYS   B 1 67 ? 11.222  -1.370  39.354  1.00 43.10 ? 67  LYS   B CG   1 
ATOM   1273 C  CD   . LYS   B 1 67 ? 10.045  -2.268  39.748  1.00 47.53 ? 67  LYS   B CD   1 
ATOM   1274 C  CE   . LYS   B 1 67 ? 10.016  -3.586  38.954  1.00 44.12 ? 67  LYS   B CE   1 
ATOM   1275 N  NZ   . LYS   B 1 67 ? 11.218  -4.450  39.202  1.00 52.70 ? 67  LYS   B NZ   1 
ATOM   1276 N  N    . TYR   B 1 68 ? 11.207  2.133   38.048  1.00 28.13 ? 68  TYR   B N    1 
ATOM   1277 C  CA   . TYR   B 1 68 ? 10.766  2.429   36.693  1.00 28.75 ? 68  TYR   B CA   1 
ATOM   1278 C  C    . TYR   B 1 68 ? 11.227  3.784   36.183  1.00 35.71 ? 68  TYR   B C    1 
ATOM   1279 O  O    . TYR   B 1 68 ? 11.029  4.081   34.999  1.00 28.81 ? 68  TYR   B O    1 
ATOM   1280 C  CB   . TYR   B 1 68 ? 9.239   2.377   36.623  1.00 24.59 ? 68  TYR   B CB   1 
ATOM   1281 C  CG   . TYR   B 1 68 ? 8.644   0.999   36.903  1.00 24.58 ? 68  TYR   B CG   1 
ATOM   1282 C  CD1  . TYR   B 1 68 ? 9.136   -0.136  36.269  1.00 30.26 ? 68  TYR   B CD1  1 
ATOM   1283 C  CD2  . TYR   B 1 68 ? 7.591   0.852   37.786  1.00 26.82 ? 68  TYR   B CD2  1 
ATOM   1284 C  CE1  . TYR   B 1 68 ? 8.590   -1.399  36.519  1.00 30.89 ? 68  TYR   B CE1  1 
ATOM   1285 C  CE2  . TYR   B 1 68 ? 7.037   -0.390  38.043  1.00 27.47 ? 68  TYR   B CE2  1 
ATOM   1286 C  CZ   . TYR   B 1 68 ? 7.536   -1.505  37.414  1.00 31.29 ? 68  TYR   B CZ   1 
ATOM   1287 O  OH   . TYR   B 1 68 ? 6.967   -2.725  37.689  1.00 33.25 ? 68  TYR   B OH   1 
ATOM   1288 N  N    . GLY   B 1 69 ? 11.807  4.619   37.036  1.00 28.94 ? 69  GLY   B N    1 
ATOM   1289 C  CA   . GLY   B 1 69 ? 12.058  5.984   36.626  1.00 33.72 ? 69  GLY   B CA   1 
ATOM   1290 C  C    . GLY   B 1 69 ? 13.442  6.224   36.068  1.00 39.67 ? 69  GLY   B C    1 
ATOM   1291 O  O    . GLY   B 1 69 ? 14.016  7.294   36.291  1.00 41.24 ? 69  GLY   B O    1 
ATOM   1292 N  N    . LYS   B 1 70 ? 13.988  5.246   35.342  1.00 34.51 ? 70  LYS   B N    1 
ATOM   1293 C  CA   . LYS   B 1 70 ? 15.315  5.344   34.748  1.00 32.08 ? 70  LYS   B CA   1 
ATOM   1294 C  C    . LYS   B 1 70 ? 15.208  5.841   33.317  1.00 38.64 ? 70  LYS   B C    1 
ATOM   1295 O  O    . LYS   B 1 70 ? 14.266  5.475   32.613  1.00 38.27 ? 70  LYS   B O    1 
ATOM   1296 C  CB   . LYS   B 1 70 ? 16.004  3.983   34.744  1.00 45.40 ? 70  LYS   B CB   1 
ATOM   1297 C  CG   . LYS   B 1 70 ? 15.911  3.238   36.053  1.00 46.69 ? 70  LYS   B CG   1 
ATOM   1298 C  CD   . LYS   B 1 70 ? 17.118  3.513   36.918  1.00 47.46 ? 70  LYS   B CD   1 
ATOM   1299 C  CE   . LYS   B 1 70 ? 16.744  3.370   38.370  1.00 48.59 ? 70  LYS   B CE   1 
ATOM   1300 N  NZ   . LYS   B 1 70 ? 16.957  2.000   38.875  1.00 47.26 ? 70  LYS   B NZ   1 
ATOM   1301 N  N    . PRO   B 1 71 ? 16.162  6.647   32.842  1.00 37.57 ? 71  PRO   B N    1 
ATOM   1302 C  CA   . PRO   B 1 71 ? 16.149  7.047   31.428  1.00 35.43 ? 71  PRO   B CA   1 
ATOM   1303 C  C    . PRO   B 1 71 ? 16.292  5.851   30.491  1.00 44.56 ? 71  PRO   B C    1 
ATOM   1304 O  O    . PRO   B 1 71 ? 16.843  4.803   30.845  1.00 35.47 ? 71  PRO   B O    1 
ATOM   1305 C  CB   . PRO   B 1 71 ? 17.358  7.991   31.306  1.00 37.90 ? 71  PRO   B CB   1 
ATOM   1306 C  CG   . PRO   B 1 71 ? 17.653  8.435   32.691  1.00 43.93 ? 71  PRO   B CG   1 
ATOM   1307 C  CD   . PRO   B 1 71 ? 17.264  7.281   33.584  1.00 40.43 ? 71  PRO   B CD   1 
ATOM   1308 N  N    . ASN   B 1 72 ? 15.794  6.029   29.265  1.00 37.81 ? 72  ASN   B N    1 
ATOM   1309 C  CA   . ASN   B 1 72 ? 15.914  5.011   28.229  1.00 36.12 ? 72  ASN   B CA   1 
ATOM   1310 C  C    . ASN   B 1 72 ? 15.890  5.701   26.869  1.00 39.36 ? 72  ASN   B C    1 
ATOM   1311 O  O    . ASN   B 1 72 ? 15.779  6.928   26.773  1.00 42.21 ? 72  ASN   B O    1 
ATOM   1312 C  CB   . ASN   B 1 72 ? 14.818  3.941   28.360  1.00 36.28 ? 72  ASN   B CB   1 
ATOM   1313 C  CG   . ASN   B 1 72 ? 13.416  4.491   28.130  1.00 34.91 ? 72  ASN   B CG   1 
ATOM   1314 O  OD1  . ASN   B 1 72 ? 13.164  5.199   27.153  1.00 32.34 ? 72  ASN   B OD1  1 
ATOM   1315 N  ND2  . ASN   B 1 72 ? 12.492  4.159   29.033  1.00 31.67 ? 72  ASN   B ND2  1 
ATOM   1316 N  N    . LYS   B 1 73 ? 15.943  4.892   25.813  1.00 40.72 ? 73  LYS   B N    1 
ATOM   1317 C  CA   . LYS   B 1 73 ? 16.112  5.376   24.449  1.00 40.51 ? 73  LYS   B CA   1 
ATOM   1318 C  C    . LYS   B 1 73 ? 14.797  5.528   23.692  1.00 35.45 ? 73  LYS   B C    1 
ATOM   1319 O  O    . LYS   B 1 73 ? 14.819  5.680   22.466  1.00 38.17 ? 73  LYS   B O    1 
ATOM   1320 C  CB   . LYS   B 1 73 ? 17.048  4.438   23.680  1.00 33.86 ? 73  LYS   B CB   1 
ATOM   1321 N  N    . ARG   B 1 74 ? 13.657  5.492   24.381  1.00 31.84 ? 74  ARG   B N    1 
ATOM   1322 C  CA   . ARG   B 1 74 ? 12.373  5.638   23.709  1.00 33.12 ? 74  ARG   B CA   1 
ATOM   1323 C  C    . ARG   B 1 74 ? 12.026  7.117   23.557  1.00 32.75 ? 74  ARG   B C    1 
ATOM   1324 O  O    . ARG   B 1 74 ? 12.127  7.888   24.519  1.00 32.76 ? 74  ARG   B O    1 
ATOM   1325 C  CB   . ARG   B 1 74 ? 11.278  4.908   24.488  1.00 30.67 ? 74  ARG   B CB   1 
ATOM   1326 C  CG   . ARG   B 1 74 ? 11.684  3.503   25.012  1.00 28.76 ? 74  ARG   B CG   1 
ATOM   1327 C  CD   . ARG   B 1 74 ? 11.937  2.523   23.879  1.00 37.49 ? 74  ARG   B CD   1 
ATOM   1328 N  NE   . ARG   B 1 74 ? 10.651  2.134   23.330  1.00 53.22 ? 74  ARG   B NE   1 
ATOM   1329 C  CZ   . ARG   B 1 74 ? 10.123  0.923   23.383  1.00 37.20 ? 74  ARG   B CZ   1 
ATOM   1330 N  NH1  . ARG   B 1 74 ? 10.824  -0.125  23.773  1.00 38.57 ? 74  ARG   B NH1  1 
ATOM   1331 N  NH2  . ARG   B 1 74 ? 8.851   0.765   23.042  1.00 41.09 ? 74  ARG   B NH2  1 
ATOM   1332 N  N    . LYS   B 1 75 ? 11.630  7.510   22.343  1.00 33.40 ? 75  LYS   B N    1 
ATOM   1333 C  CA   . LYS   B 1 75 ? 11.302  8.902   22.052  1.00 30.24 ? 75  LYS   B CA   1 
ATOM   1334 C  C    . LYS   B 1 75 ? 10.270  9.418   23.029  1.00 30.01 ? 75  LYS   B C    1 
ATOM   1335 O  O    . LYS   B 1 75 ? 9.186   8.837   23.160  1.00 28.53 ? 75  LYS   B O    1 
ATOM   1336 C  CB   . LYS   B 1 75 ? 10.765  9.040   20.631  1.00 33.12 ? 75  LYS   B CB   1 
ATOM   1337 C  CG   . LYS   B 1 75 ? 10.282  10.456  20.310  1.00 33.56 ? 75  LYS   B CG   1 
ATOM   1338 C  CD   . LYS   B 1 75 ? 10.263  10.704  18.813  1.00 37.92 ? 75  LYS   B CD   1 
ATOM   1339 C  CE   . LYS   B 1 75 ? 9.824   12.121  18.468  1.00 40.76 ? 75  LYS   B CE   1 
ATOM   1340 N  NZ   . LYS   B 1 75 ? 8.818   12.160  17.359  1.00 52.91 ? 75  LYS   B NZ   1 
ATOM   1341 N  N    . GLY   B 1 76 ? 10.620  10.496  23.730  1.00 29.54 ? 76  GLY   B N    1 
ATOM   1342 C  CA   . GLY   B 1 76 ? 9.712   11.151  24.637  1.00 29.94 ? 76  GLY   B CA   1 
ATOM   1343 C  C    . GLY   B 1 76 ? 9.812   10.713  26.080  1.00 32.34 ? 76  GLY   B C    1 
ATOM   1344 O  O    . GLY   B 1 76 ? 9.195   11.351  26.940  1.00 29.50 ? 76  GLY   B O    1 
ATOM   1345 N  N    . PHE   B 1 77 ? 10.576  9.656   26.388  1.00 28.94 ? 77  PHE   B N    1 
ATOM   1346 C  CA   . PHE   B 1 77 ? 10.601  9.153   27.763  1.00 26.70 ? 77  PHE   B CA   1 
ATOM   1347 C  C    . PHE   B 1 77 ? 11.327  10.112  28.696  1.00 27.95 ? 77  PHE   B C    1 
ATOM   1348 O  O    . PHE   B 1 77 ? 10.825  10.440  29.775  1.00 24.62 ? 77  PHE   B O    1 
ATOM   1349 C  CB   . PHE   B 1 77 ? 11.250  7.772   27.824  1.00 29.51 ? 77  PHE   B CB   1 
ATOM   1350 C  CG   . PHE   B 1 77 ? 11.016  7.045   29.128  1.00 25.81 ? 77  PHE   B CG   1 
ATOM   1351 C  CD1  . PHE   B 1 77 ? 9.866   6.306   29.325  1.00 24.89 ? 77  PHE   B CD1  1 
ATOM   1352 C  CD2  . PHE   B 1 77 ? 11.945  7.108   30.145  1.00 30.13 ? 77  PHE   B CD2  1 
ATOM   1353 C  CE1  . PHE   B 1 77 ? 9.641   5.644   30.522  1.00 21.35 ? 77  PHE   B CE1  1 
ATOM   1354 C  CE2  . PHE   B 1 77 ? 11.725  6.439   31.334  1.00 29.12 ? 77  PHE   B CE2  1 
ATOM   1355 C  CZ   . PHE   B 1 77 ? 10.570  5.706   31.511  1.00 27.33 ? 77  PHE   B CZ   1 
ATOM   1356 N  N    . ASN   B 1 78 ? 12.522  10.549  28.319  1.00 30.26 ? 78  ASN   B N    1 
ATOM   1357 C  CA   . ASN   B 1 78 ? 13.275  11.393  29.232  1.00 31.87 ? 78  ASN   B CA   1 
ATOM   1358 C  C    . ASN   B 1 78 ? 12.593  12.745  29.419  1.00 32.05 ? 78  ASN   B C    1 
ATOM   1359 O  O    . ASN   B 1 78 ? 12.705  13.343  30.495  1.00 25.87 ? 78  ASN   B O    1 
ATOM   1360 C  CB   . ASN   B 1 78 ? 14.708  11.568  28.728  1.00 32.66 ? 78  ASN   B CB   1 
ATOM   1361 C  CG   . ASN   B 1 78 ? 15.488  10.256  28.696  1.00 37.73 ? 78  ASN   B CG   1 
ATOM   1362 O  OD1  . ASN   B 1 78 ? 15.135  9.285   29.366  1.00 37.58 ? 78  ASN   B OD1  1 
ATOM   1363 N  ND2  . ASN   B 1 78 ? 16.563  10.236  27.931  1.00 37.17 ? 78  ASN   B ND2  1 
ATOM   1364 N  N    . GLU   B 1 79 ? 11.868  13.233  28.403  1.00 26.44 ? 79  GLU   B N    1 
ATOM   1365 C  CA   . GLU   B 1 79 ? 11.069  14.439  28.609  1.00 29.70 ? 79  GLU   B CA   1 
ATOM   1366 C  C    . GLU   B 1 79 ? 9.923   14.161  29.571  1.00 28.93 ? 79  GLU   B C    1 
ATOM   1367 O  O    . GLU   B 1 79 ? 9.557   15.024  30.373  1.00 34.10 ? 79  GLU   B O    1 
ATOM   1368 C  CB   . GLU   B 1 79 ? 10.535  14.975  27.285  1.00 33.72 ? 79  GLU   B CB   1 
ATOM   1369 N  N    . GLY   B 1 80 ? 9.355   12.959  29.508  1.00 22.88 ? 80  GLY   B N    1 
ATOM   1370 C  CA   . GLY   B 1 80 ? 8.290   12.598  30.438  1.00 23.13 ? 80  GLY   B CA   1 
ATOM   1371 C  C    . GLY   B 1 80 ? 8.762   12.530  31.874  1.00 23.69 ? 80  GLY   B C    1 
ATOM   1372 O  O    . GLY   B 1 80 ? 8.040   12.931  32.793  1.00 24.81 ? 80  GLY   B O    1 
ATOM   1373 N  N    . LEU   B 1 81 ? 9.966   11.989  32.092  1.00 25.66 ? 81  LEU   B N    1 
ATOM   1374 C  CA   . LEU   B 1 81 ? 10.557  12.001  33.429  1.00 27.92 ? 81  LEU   B CA   1 
ATOM   1375 C  C    . LEU   B 1 81 ? 10.763  13.427  33.921  1.00 28.05 ? 81  LEU   B C    1 
ATOM   1376 O  O    . LEU   B 1 81 ? 10.600  13.701  35.113  1.00 30.25 ? 81  LEU   B O    1 
ATOM   1377 C  CB   . LEU   B 1 81 ? 11.891  11.241  33.440  1.00 25.36 ? 81  LEU   B CB   1 
ATOM   1378 C  CG   . LEU   B 1 81 ? 11.832  9.723   33.219  1.00 26.37 ? 81  LEU   B CG   1 
ATOM   1379 C  CD1  . LEU   B 1 81 ? 13.227  9.096   33.303  1.00 28.96 ? 81  LEU   B CD1  1 
ATOM   1380 C  CD2  . LEU   B 1 81 ? 10.871  9.069   34.208  1.00 24.87 ? 81  LEU   B CD2  1 
ATOM   1381 N  N    . TRP   B 1 82 ? 11.139  14.344  33.020  1.00 25.19 ? 82  TRP   B N    1 
ATOM   1382 C  CA   . TRP   B 1 82 ? 11.273  15.749  33.405  1.00 28.34 ? 82  TRP   B CA   1 
ATOM   1383 C  C    . TRP   B 1 82 ? 9.929   16.348  33.794  1.00 28.06 ? 82  TRP   B C    1 
ATOM   1384 O  O    . TRP   B 1 82 ? 9.834   17.079  34.788  1.00 32.46 ? 82  TRP   B O    1 
ATOM   1385 C  CB   . TRP   B 1 82 ? 11.891  16.570  32.277  1.00 29.29 ? 82  TRP   B CB   1 
ATOM   1386 C  CG   . TRP   B 1 82 ? 12.191  17.999  32.720  1.00 34.78 ? 82  TRP   B CG   1 
ATOM   1387 C  CD1  . TRP   B 1 82 ? 13.378  18.475  33.188  1.00 33.13 ? 82  TRP   B CD1  1 
ATOM   1388 C  CD2  . TRP   B 1 82 ? 11.265  19.102  32.781  1.00 38.18 ? 82  TRP   B CD2  1 
ATOM   1389 N  NE1  . TRP   B 1 82 ? 13.258  19.813  33.525  1.00 39.36 ? 82  TRP   B NE1  1 
ATOM   1390 C  CE2  . TRP   B 1 82 ? 11.972  20.217  33.281  1.00 39.42 ? 82  TRP   B CE2  1 
ATOM   1391 C  CE3  . TRP   B 1 82 ? 9.911   19.257  32.455  1.00 36.46 ? 82  TRP   B CE3  1 
ATOM   1392 C  CZ2  . TRP   B 1 82 ? 11.370  21.461  33.464  1.00 35.85 ? 82  TRP   B CZ2  1 
ATOM   1393 C  CZ3  . TRP   B 1 82 ? 9.317   20.504  32.641  1.00 34.90 ? 82  TRP   B CZ3  1 
ATOM   1394 C  CH2  . TRP   B 1 82 ? 10.048  21.581  33.137  1.00 37.72 ? 82  TRP   B CH2  1 
ATOM   1395 N  N    . GLU   B 1 83 ? 8.880   16.066  33.015  1.00 28.36 ? 83  GLU   B N    1 
ATOM   1396 C  CA   . GLU   B 1 83 ? 7.578   16.664  33.286  1.00 22.94 ? 83  GLU   B CA   1 
ATOM   1397 C  C    . GLU   B 1 83 ? 6.993   16.138  34.584  1.00 27.54 ? 83  GLU   B C    1 
ATOM   1398 O  O    . GLU   B 1 83 ? 6.468   16.915  35.392  1.00 27.30 ? 83  GLU   B O    1 
ATOM   1399 C  CB   . GLU   B 1 83 ? 6.621   16.406  32.119  1.00 24.04 ? 83  GLU   B CB   1 
ATOM   1400 C  CG   . GLU   B 1 83 ? 7.062   17.031  30.787  1.00 29.96 ? 83  GLU   B CG   1 
ATOM   1401 C  CD   . GLU   B 1 83 ? 6.115   16.717  29.641  1.00 29.73 ? 83  GLU   B CD   1 
ATOM   1402 O  OE1  . GLU   B 1 83 ? 5.261   15.826  29.813  1.00 28.63 ? 83  GLU   B OE1  1 
ATOM   1403 O  OE2  . GLU   B 1 83 ? 6.230   17.352  28.559  1.00 29.93 ? 83  GLU   B OE2  1 
ATOM   1404 N  N    . ILE   B 1 84 ? 7.098   14.825  34.825  1.00 23.01 ? 84  ILE   B N    1 
ATOM   1405 C  CA   . ILE   B 1 84 ? 6.482   14.262  36.026  1.00 25.15 ? 84  ILE   B CA   1 
ATOM   1406 C  C    . ILE   B 1 84 ? 7.196   14.764  37.268  1.00 25.77 ? 84  ILE   B C    1 
ATOM   1407 O  O    . ILE   B 1 84 ? 6.586   14.886  38.339  1.00 23.16 ? 84  ILE   B O    1 
ATOM   1408 C  CB   . ILE   B 1 84 ? 6.456   12.717  35.972  1.00 21.37 ? 84  ILE   B CB   1 
ATOM   1409 C  CG1  . ILE   B 1 84 ? 5.459   12.158  36.996  1.00 22.59 ? 84  ILE   B CG1  1 
ATOM   1410 C  CG2  . ILE   B 1 84 ? 7.839   12.114  36.191  1.00 22.38 ? 84  ILE   B CG2  1 
ATOM   1411 C  CD1  . ILE   B 1 84 ? 4.910   10.764  36.632  1.00 19.56 ? 84  ILE   B CD1  1 
ATOM   1412 N  N    . GLN   B 1 85 ? 8.486   15.071  37.150  1.00 24.99 ? 85  GLN   B N    1 
ATOM   1413 C  CA   . GLN   B 1 85 ? 9.235   15.630  38.268  1.00 29.11 ? 85  GLN   B CA   1 
ATOM   1414 C  C    . GLN   B 1 85 ? 8.969   17.121  38.452  1.00 25.77 ? 85  GLN   B C    1 
ATOM   1415 O  O    . GLN   B 1 85 ? 8.827   17.590  39.585  1.00 27.63 ? 85  GLN   B O    1 
ATOM   1416 C  CB   . GLN   B 1 85 ? 10.731  15.399  38.054  1.00 31.06 ? 85  GLN   B CB   1 
ATOM   1417 N  N    . ASN   B 1 86 ? 8.936   17.891  37.368  1.00 23.55 ? 86  ASN   B N    1 
ATOM   1418 C  CA   . ASN   B 1 86 ? 9.003   19.341  37.493  1.00 26.32 ? 86  ASN   B CA   1 
ATOM   1419 C  C    . ASN   B 1 86 ? 7.677   20.057  37.307  1.00 28.50 ? 86  ASN   B C    1 
ATOM   1420 O  O    . ASN   B 1 86 ? 7.537   21.177  37.808  1.00 29.55 ? 86  ASN   B O    1 
ATOM   1421 C  CB   . ASN   B 1 86 ? 10.008  19.927  36.497  1.00 32.11 ? 86  ASN   B CB   1 
ATOM   1422 C  CG   . ASN   B 1 86 ? 11.401  19.471  36.772  1.00 36.79 ? 86  ASN   B CG   1 
ATOM   1423 O  OD1  . ASN   B 1 86 ? 12.076  20.043  37.612  1.00 40.77 ? 86  ASN   B OD1  1 
ATOM   1424 N  ND2  . ASN   B 1 86 ? 11.846  18.434  36.074  1.00 31.98 ? 86  ASN   B ND2  1 
ATOM   1425 N  N    . ASN   B 1 87 ? 6.719   19.475  36.585  1.00 24.74 ? 87  ASN   B N    1 
ATOM   1426 C  CA   . ASN   B 1 87 ? 5.429   20.151  36.458  1.00 26.89 ? 87  ASN   B CA   1 
ATOM   1427 C  C    . ASN   B 1 87 ? 4.377   19.123  36.072  1.00 25.90 ? 87  ASN   B C    1 
ATOM   1428 O  O    . ASN   B 1 87 ? 3.825   19.184  34.966  1.00 27.65 ? 87  ASN   B O    1 
ATOM   1429 C  CB   . ASN   B 1 87 ? 5.506   21.288  35.424  1.00 29.55 ? 87  ASN   B CB   1 
ATOM   1430 C  CG   . ASN   B 1 87 ? 4.436   22.371  35.641  1.00 29.96 ? 87  ASN   B CG   1 
ATOM   1431 O  OD1  . ASN   B 1 87 ? 3.444   22.156  36.341  1.00 34.63 ? 87  ASN   B OD1  1 
ATOM   1432 N  ND2  . ASN   B 1 87 ? 4.645   23.532  35.047  1.00 39.35 ? 87  ASN   B ND2  1 
ATOM   1433 N  N    . PRO   B 1 88 ? 4.089   18.152  36.949  1.00 26.22 ? 88  PRO   B N    1 
ATOM   1434 C  CA   . PRO   B 1 88 ? 3.169   17.073  36.568  1.00 19.95 ? 88  PRO   B CA   1 
ATOM   1435 C  C    . PRO   B 1 88 ? 1.764   17.538  36.322  1.00 22.02 ? 88  PRO   B C    1 
ATOM   1436 O  O    . PRO   B 1 88 ? 1.023   16.831  35.630  1.00 22.74 ? 88  PRO   B O    1 
ATOM   1437 C  CB   . PRO   B 1 88 ? 3.224   16.120  37.771  1.00 20.50 ? 88  PRO   B CB   1 
ATOM   1438 C  CG   . PRO   B 1 88 ? 3.593   17.002  38.918  1.00 21.37 ? 88  PRO   B CG   1 
ATOM   1439 C  CD   . PRO   B 1 88 ? 4.572   17.994  38.334  1.00 25.75 ? 88  PRO   B CD   1 
ATOM   1440 N  N    . HIS   B 1 89 ? 1.367   18.705  36.834  1.00 22.20 ? 89  HIS   B N    1 
ATOM   1441 C  CA   . HIS   B 1 89 ? -0.026  19.124  36.773  1.00 23.22 ? 89  HIS   B CA   1 
ATOM   1442 C  C    . HIS   B 1 89 ? -0.309  20.198  35.726  1.00 26.34 ? 89  HIS   B C    1 
ATOM   1443 O  O    . HIS   B 1 89 ? -1.427  20.729  35.691  1.00 27.44 ? 89  HIS   B O    1 
ATOM   1444 C  CB   . HIS   B 1 89 ? -0.476  19.602  38.153  1.00 23.34 ? 89  HIS   B CB   1 
ATOM   1445 C  CG   . HIS   B 1 89 ? -0.331  18.544  39.201  1.00 24.80 ? 89  HIS   B CG   1 
ATOM   1446 N  ND1  . HIS   B 1 89 ? -0.942  17.312  39.092  1.00 21.34 ? 89  HIS   B ND1  1 
ATOM   1447 C  CD2  . HIS   B 1 89 ? 0.363   18.522  40.362  1.00 24.29 ? 89  HIS   B CD2  1 
ATOM   1448 C  CE1  . HIS   B 1 89 ? -0.643  16.582  40.151  1.00 25.55 ? 89  HIS   B CE1  1 
ATOM   1449 N  NE2  . HIS   B 1 89 ? 0.146   17.293  40.937  1.00 23.43 ? 89  HIS   B NE2  1 
ATOM   1450 N  N    . ALA   B 1 90 ? 0.654   20.511  34.862  1.00 26.91 ? 90  ALA   B N    1 
ATOM   1451 C  CA   . ALA   B 1 90 ? 0.479   21.611  33.929  1.00 31.87 ? 90  ALA   B CA   1 
ATOM   1452 C  C    . ALA   B 1 90 ? -0.413  21.211  32.767  1.00 30.78 ? 90  ALA   B C    1 
ATOM   1453 O  O    . ALA   B 1 90 ? -0.644  20.028  32.501  1.00 32.46 ? 90  ALA   B O    1 
ATOM   1454 C  CB   . ALA   B 1 90 ? 1.825   22.085  33.381  1.00 35.52 ? 90  ALA   B CB   1 
ATOM   1455 N  N    . SER   B 1 91 ? -0.896  22.228  32.063  1.00 34.07 ? 91  SER   B N    1 
ATOM   1456 C  CA   . SER   B 1 91 ? -1.588  22.042  30.794  1.00 36.38 ? 91  SER   B CA   1 
ATOM   1457 C  C    . SER   B 1 91 ? -0.560  21.854  29.683  1.00 41.73 ? 91  SER   B C    1 
ATOM   1458 O  O    . SER   B 1 91 ? 0.243   22.759  29.413  1.00 39.47 ? 91  SER   B O    1 
ATOM   1459 C  CB   . SER   B 1 91 ? -2.485  23.242  30.503  1.00 45.17 ? 91  SER   B CB   1 
ATOM   1460 O  OG   . SER   B 1 91 ? -3.153  23.104  29.266  1.00 48.79 ? 91  SER   B OG   1 
ATOM   1461 N  N    . TYR   B 1 92 ? -0.581  20.678  29.048  1.00 34.63 ? 92  TYR   B N    1 
ATOM   1462 C  CA   . TYR   B 1 92 ? 0.288   20.356  27.924  1.00 35.21 ? 92  TYR   B CA   1 
ATOM   1463 C  C    . TYR   B 1 92 ? -0.478  20.345  26.612  1.00 47.69 ? 92  TYR   B C    1 
ATOM   1464 O  O    . TYR   B 1 92 ? -0.048  19.712  25.642  1.00 55.05 ? 92  TYR   B O    1 
ATOM   1465 C  CB   . TYR   B 1 92 ? 0.976   19.013  28.148  1.00 31.85 ? 92  TYR   B CB   1 
ATOM   1466 C  CG   . TYR   B 1 92 ? 1.942   19.065  29.282  1.00 30.03 ? 92  TYR   B CG   1 
ATOM   1467 C  CD1  . TYR   B 1 92 ? 3.230   19.542  29.094  1.00 35.87 ? 92  TYR   B CD1  1 
ATOM   1468 C  CD2  . TYR   B 1 92 ? 1.576   18.637  30.550  1.00 31.43 ? 92  TYR   B CD2  1 
ATOM   1469 C  CE1  . TYR   B 1 92 ? 4.133   19.598  30.135  1.00 35.63 ? 92  TYR   B CE1  1 
ATOM   1470 C  CE2  . TYR   B 1 92 ? 2.479   18.681  31.603  1.00 35.44 ? 92  TYR   B CE2  1 
ATOM   1471 C  CZ   . TYR   B 1 92 ? 3.754   19.174  31.386  1.00 36.32 ? 92  TYR   B CZ   1 
ATOM   1472 O  OH   . TYR   B 1 92 ? 4.657   19.228  32.419  1.00 33.29 ? 92  TYR   B OH   1 
ATOM   1473 N  N    . SER   B 1 93 ? -1.600  21.049  26.578  1.00 52.86 ? 93  SER   B N    1 
ATOM   1474 C  CA   . SER   B 1 93 ? -2.475  21.148  25.429  1.00 56.91 ? 93  SER   B CA   1 
ATOM   1475 C  C    . SER   B 1 93 ? -2.316  22.494  24.720  1.00 65.84 ? 93  SER   B C    1 
ATOM   1476 O  O    . SER   B 1 93 ? -1.322  23.202  24.910  1.00 56.29 ? 93  SER   B O    1 
ATOM   1477 C  CB   . SER   B 1 93 ? -3.921  20.932  25.891  1.00 59.16 ? 93  SER   B CB   1 
ATOM   1478 O  OG   . SER   B 1 93 ? -4.586  22.164  26.117  1.00 70.62 ? 93  SER   B OG   1 
ATOM   1479 N  N    . HIS   C 1 3  ? 9.392   -19.414 27.234  1.00 61.70 ? 3   HIS   C N    1 
ATOM   1480 C  CA   . HIS   C 1 3  ? 9.514   -19.432 28.690  1.00 63.75 ? 3   HIS   C CA   1 
ATOM   1481 C  C    . HIS   C 1 3  ? 10.803  -18.738 29.109  1.00 60.59 ? 3   HIS   C C    1 
ATOM   1482 O  O    . HIS   C 1 3  ? 11.750  -18.682 28.326  1.00 62.55 ? 3   HIS   C O    1 
ATOM   1483 C  CB   . HIS   C 1 3  ? 9.486   -20.865 29.225  1.00 60.32 ? 3   HIS   C CB   1 
ATOM   1484 N  N    . ALA   C 1 4  ? 10.827  -18.230 30.344  1.00 58.23 ? 4   ALA   C N    1 
ATOM   1485 C  CA   . ALA   C 1 4  ? 11.969  -17.474 30.853  1.00 53.42 ? 4   ALA   C CA   1 
ATOM   1486 C  C    . ALA   C 1 4  ? 13.290  -18.184 30.575  1.00 52.02 ? 4   ALA   C C    1 
ATOM   1487 O  O    . ALA   C 1 4  ? 13.427  -19.391 30.794  1.00 56.16 ? 4   ALA   C O    1 
ATOM   1488 C  CB   . ALA   C 1 4  ? 11.811  -17.233 32.357  1.00 57.12 ? 4   ALA   C CB   1 
ATOM   1489 N  N    . PHE   C 1 5  ? 14.256  -17.425 30.067  1.00 49.21 ? 5   PHE   C N    1 
ATOM   1490 C  CA   . PHE   C 1 5  ? 15.585  -17.934 29.780  1.00 47.36 ? 5   PHE   C CA   1 
ATOM   1491 C  C    . PHE   C 1 5  ? 16.437  -17.917 31.052  1.00 52.95 ? 5   PHE   C C    1 
ATOM   1492 O  O    . PHE   C 1 5  ? 16.031  -17.391 32.094  1.00 52.06 ? 5   PHE   C O    1 
ATOM   1493 C  CB   . PHE   C 1 5  ? 16.232  -17.096 28.674  1.00 43.20 ? 5   PHE   C CB   1 
ATOM   1494 C  CG   . PHE   C 1 5  ? 15.429  -17.023 27.400  1.00 41.22 ? 5   PHE   C CG   1 
ATOM   1495 C  CD1  . PHE   C 1 5  ? 14.471  -16.038 27.215  1.00 46.40 ? 5   PHE   C CD1  1 
ATOM   1496 C  CD2  . PHE   C 1 5  ? 15.677  -17.901 26.360  1.00 45.33 ? 5   PHE   C CD2  1 
ATOM   1497 C  CE1  . PHE   C 1 5  ? 13.744  -15.955 26.019  1.00 42.81 ? 5   PHE   C CE1  1 
ATOM   1498 C  CE2  . PHE   C 1 5  ? 14.966  -17.820 25.156  1.00 40.86 ? 5   PHE   C CE2  1 
ATOM   1499 C  CZ   . PHE   C 1 5  ? 14.004  -16.854 24.985  1.00 39.96 ? 5   PHE   C CZ   1 
ATOM   1500 N  N    . LYS   C 1 6  ? 17.627  -18.498 30.968  1.00 49.56 ? 6   LYS   C N    1 
ATOM   1501 C  CA   . LYS   C 1 6  ? 18.564  -18.531 32.082  1.00 52.29 ? 6   LYS   C CA   1 
ATOM   1502 C  C    . LYS   C 1 6  ? 19.970  -18.339 31.533  1.00 54.19 ? 6   LYS   C C    1 
ATOM   1503 O  O    . LYS   C 1 6  ? 20.205  -18.571 30.342  1.00 47.66 ? 6   LYS   C O    1 
ATOM   1504 C  CB   . LYS   C 1 6  ? 18.465  -19.847 32.874  1.00 61.98 ? 6   LYS   C CB   1 
ATOM   1505 C  CG   . LYS   C 1 6  ? 19.011  -21.086 32.171  1.00 60.76 ? 6   LYS   C CG   1 
ATOM   1506 C  CD   . LYS   C 1 6  ? 18.597  -22.349 32.926  1.00 65.20 ? 6   LYS   C CD   1 
ATOM   1507 C  CE   . LYS   C 1 6  ? 19.303  -23.580 32.391  1.00 76.14 ? 6   LYS   C CE   1 
ATOM   1508 N  NZ   . LYS   C 1 6  ? 20.732  -23.617 32.794  1.00 77.84 ? 6   LYS   C NZ   1 
ATOM   1509 N  N    . PRO   C 1 7  ? 20.921  -17.896 32.365  1.00 54.34 ? 7   PRO   C N    1 
ATOM   1510 C  CA   . PRO   C 1 7  ? 22.273  -17.626 31.848  1.00 55.22 ? 7   PRO   C CA   1 
ATOM   1511 C  C    . PRO   C 1 7  ? 22.842  -18.847 31.139  1.00 58.87 ? 7   PRO   C C    1 
ATOM   1512 O  O    . PRO   C 1 7  ? 22.789  -19.966 31.658  1.00 54.71 ? 7   PRO   C O    1 
ATOM   1513 C  CB   . PRO   C 1 7  ? 23.071  -17.280 33.114  1.00 60.02 ? 7   PRO   C CB   1 
ATOM   1514 C  CG   . PRO   C 1 7  ? 22.026  -16.796 34.070  1.00 62.83 ? 7   PRO   C CG   1 
ATOM   1515 C  CD   . PRO   C 1 7  ? 20.892  -17.747 33.833  1.00 61.98 ? 7   PRO   C CD   1 
ATOM   1516 N  N    . GLY   C 1 8  ? 23.354  -18.630 29.918  1.00 54.67 ? 8   GLY   C N    1 
ATOM   1517 C  CA   . GLY   C 1 8  ? 23.860  -19.691 29.076  1.00 53.60 ? 8   GLY   C CA   1 
ATOM   1518 C  C    . GLY   C 1 8  ? 22.924  -20.128 27.961  1.00 54.14 ? 8   GLY   C C    1 
ATOM   1519 O  O    . GLY   C 1 8  ? 23.381  -20.775 27.016  1.00 45.18 ? 8   GLY   C O    1 
ATOM   1520 N  N    . ASP   C 1 9  ? 21.634  -19.806 28.046  1.00 46.18 ? 9   ASP   C N    1 
ATOM   1521 C  CA   . ASP   C 1 9  ? 20.706  -20.149 26.972  1.00 49.01 ? 9   ASP   C CA   1 
ATOM   1522 C  C    . ASP   C 1 9  ? 21.100  -19.457 25.675  1.00 40.19 ? 9   ASP   C C    1 
ATOM   1523 O  O    . ASP   C 1 9  ? 21.445  -18.272 25.667  1.00 37.33 ? 9   ASP   C O    1 
ATOM   1524 C  CB   . ASP   C 1 9  ? 19.279  -19.754 27.354  1.00 44.91 ? 9   ASP   C CB   1 
ATOM   1525 C  CG   . ASP   C 1 9  ? 18.693  -20.662 28.425  1.00 52.37 ? 9   ASP   C CG   1 
ATOM   1526 O  OD1  . ASP   C 1 9  ? 19.416  -21.579 28.879  1.00 49.07 ? 9   ASP   C OD1  1 
ATOM   1527 O  OD2  . ASP   C 1 9  ? 17.524  -20.449 28.823  1.00 49.22 ? 9   ASP   C OD2  1 
ATOM   1528 N  N    . LEU   C 1 10 ? 21.035  -20.205 24.575  1.00 37.15 ? 10  LEU   C N    1 
ATOM   1529 C  CA   . LEU   C 1 10 ? 21.404  -19.707 23.255  1.00 34.04 ? 10  LEU   C CA   1 
ATOM   1530 C  C    . LEU   C 1 10 ? 20.170  -19.161 22.552  1.00 40.96 ? 10  LEU   C C    1 
ATOM   1531 O  O    . LEU   C 1 10 ? 19.099  -19.784 22.592  1.00 40.68 ? 10  LEU   C O    1 
ATOM   1532 C  CB   . LEU   C 1 10 ? 22.006  -20.836 22.428  1.00 40.70 ? 10  LEU   C CB   1 
ATOM   1533 C  CG   . LEU   C 1 10 ? 23.269  -21.427 23.043  1.00 43.39 ? 10  LEU   C CG   1 
ATOM   1534 C  CD1  . LEU   C 1 10 ? 23.898  -22.444 22.091  1.00 39.41 ? 10  LEU   C CD1  1 
ATOM   1535 C  CD2  . LEU   C 1 10 ? 24.245  -20.331 23.449  1.00 42.54 ? 10  LEU   C CD2  1 
ATOM   1536 N  N    . VAL   C 1 11 ? 20.310  -17.986 21.923  1.00 32.21 ? 11  VAL   C N    1 
ATOM   1537 C  CA   . VAL   C 1 11 ? 19.180  -17.260 21.350  1.00 31.72 ? 11  VAL   C CA   1 
ATOM   1538 C  C    . VAL   C 1 11 ? 19.611  -16.523 20.081  1.00 30.79 ? 11  VAL   C C    1 
ATOM   1539 O  O    . VAL   C 1 11 ? 20.798  -16.375 19.787  1.00 25.50 ? 11  VAL   C O    1 
ATOM   1540 C  CB   . VAL   C 1 11 ? 18.595  -16.236 22.345  1.00 31.35 ? 11  VAL   C CB   1 
ATOM   1541 C  CG1  . VAL   C 1 11 ? 18.071  -16.923 23.607  1.00 32.31 ? 11  VAL   C CG1  1 
ATOM   1542 C  CG2  . VAL   C 1 11 ? 19.638  -15.192 22.682  1.00 28.49 ? 11  VAL   C CG2  1 
ATOM   1543 N  N    . PHE   C 1 12 ? 18.620  -16.068 19.315  1.00 27.59 ? 12  PHE   C N    1 
ATOM   1544 C  CA   . PHE   C 1 12 ? 18.778  -14.938 18.411  1.00 26.63 ? 12  PHE   C CA   1 
ATOM   1545 C  C    . PHE   C 1 12 ? 18.151  -13.738 19.093  1.00 24.76 ? 12  PHE   C C    1 
ATOM   1546 O  O    . PHE   C 1 12 ? 17.062  -13.844 19.668  1.00 28.73 ? 12  PHE   C O    1 
ATOM   1547 C  CB   . PHE   C 1 12 ? 18.124  -15.178 17.055  1.00 29.09 ? 12  PHE   C CB   1 
ATOM   1548 C  CG   . PHE   C 1 12 ? 18.776  -16.269 16.259  1.00 26.73 ? 12  PHE   C CG   1 
ATOM   1549 C  CD1  . PHE   C 1 12 ? 18.370  -17.582 16.415  1.00 30.07 ? 12  PHE   C CD1  1 
ATOM   1550 C  CD2  . PHE   C 1 12 ? 19.787  -15.987 15.356  1.00 26.01 ? 12  PHE   C CD2  1 
ATOM   1551 C  CE1  . PHE   C 1 12 ? 18.962  -18.596 15.692  1.00 28.44 ? 12  PHE   C CE1  1 
ATOM   1552 C  CE2  . PHE   C 1 12 ? 20.377  -17.005 14.619  1.00 25.21 ? 12  PHE   C CE2  1 
ATOM   1553 C  CZ   . PHE   C 1 12 ? 19.968  -18.313 14.799  1.00 28.14 ? 12  PHE   C CZ   1 
ATOM   1554 N  N    . ALA   C 1 13 ? 18.856  -12.616 19.071  1.00 24.89 ? 13  ALA   C N    1 
ATOM   1555 C  CA   . ALA   C 1 13 ? 18.446  -11.420 19.796  1.00 24.20 ? 13  ALA   C CA   1 
ATOM   1556 C  C    . ALA   C 1 13 ? 18.211  -10.306 18.793  1.00 27.15 ? 13  ALA   C C    1 
ATOM   1557 O  O    . ALA   C 1 13 ? 19.079  -10.041 17.961  1.00 23.38 ? 13  ALA   C O    1 
ATOM   1558 C  CB   . ALA   C 1 13 ? 19.517  -11.009 20.801  1.00 25.13 ? 13  ALA   C CB   1 
ATOM   1559 N  N    . LYS   C 1 14 ? 17.060  -9.640  18.889  1.00 24.94 ? 14  LYS   C N    1 
ATOM   1560 C  CA   . LYS   C 1 14 ? 16.637  -8.656  17.898  1.00 25.19 ? 14  LYS   C CA   1 
ATOM   1561 C  C    . LYS   C 1 14 ? 16.771  -7.252  18.474  1.00 28.69 ? 14  LYS   C C    1 
ATOM   1562 O  O    . LYS   C 1 14 ? 16.119  -6.921  19.470  1.00 31.12 ? 14  LYS   C O    1 
ATOM   1563 C  CB   . LYS   C 1 14 ? 15.192  -8.901  17.454  1.00 27.09 ? 14  LYS   C CB   1 
ATOM   1564 C  CG   . LYS   C 1 14 ? 14.715  -7.993  16.313  1.00 28.52 ? 14  LYS   C CG   1 
ATOM   1565 C  CD   . LYS   C 1 14 ? 15.537  -8.190  15.062  1.00 26.14 ? 14  LYS   C CD   1 
ATOM   1566 C  CE   . LYS   C 1 14 ? 15.004  -7.383  13.880  1.00 28.01 ? 14  LYS   C CE   1 
ATOM   1567 N  NZ   . LYS   C 1 14 ? 15.342  -5.925  13.970  1.00 28.26 ? 14  LYS   C NZ   1 
ATOM   1568 N  N    . MET   C 1 15 ? 17.606  -6.435  17.837  1.00 25.46 ? 15  MET   C N    1 
ATOM   1569 C  CA   . MET   C 1 15 ? 17.714  -5.008  18.104  1.00 26.80 ? 15  MET   C CA   1 
ATOM   1570 C  C    . MET   C 1 15 ? 17.173  -4.253  16.895  1.00 27.81 ? 15  MET   C C    1 
ATOM   1571 O  O    . MET   C 1 15 ? 17.460  -4.617  15.751  1.00 28.63 ? 15  MET   C O    1 
ATOM   1572 C  CB   . MET   C 1 15 ? 19.174  -4.605  18.317  1.00 29.23 ? 15  MET   C CB   1 
ATOM   1573 C  CG   . MET   C 1 15 ? 19.879  -5.284  19.467  1.00 32.08 ? 15  MET   C CG   1 
ATOM   1574 S  SD   . MET   C 1 15 ? 19.252  -4.765  21.059  1.00 42.21 ? 15  MET   C SD   1 
ATOM   1575 C  CE   . MET   C 1 15 ? 20.115  -3.221  21.290  1.00 37.21 ? 15  MET   C CE   1 
ATOM   1576 N  N    . LYS   C 1 16 ? 16.416  -3.186  17.133  1.00 31.13 ? 16  LYS   C N    1 
ATOM   1577 C  CA   . LYS   C 1 16 ? 15.968  -2.360  16.020  1.00 31.80 ? 16  LYS   C CA   1 
ATOM   1578 C  C    . LYS   C 1 16 ? 17.183  -1.908  15.215  1.00 30.96 ? 16  LYS   C C    1 
ATOM   1579 O  O    . LYS   C 1 16 ? 18.183  -1.454  15.781  1.00 35.82 ? 16  LYS   C O    1 
ATOM   1580 C  CB   . LYS   C 1 16 ? 15.185  -1.155  16.539  1.00 35.59 ? 16  LYS   C CB   1 
ATOM   1581 C  CG   . LYS   C 1 16 ? 14.745  -0.190  15.462  1.00 37.43 ? 16  LYS   C CG   1 
ATOM   1582 C  CD   . LYS   C 1 16 ? 13.243  0.043   15.555  1.00 51.78 ? 16  LYS   C CD   1 
ATOM   1583 C  CE   . LYS   C 1 16 ? 12.625  0.399   14.206  1.00 57.07 ? 16  LYS   C CE   1 
ATOM   1584 N  NZ   . LYS   C 1 16 ? 11.266  -0.205  14.030  1.00 53.04 ? 16  LYS   C NZ   1 
ATOM   1585 N  N    . GLY   C 1 17 ? 17.114  -2.092  13.901  1.00 34.35 ? 17  GLY   C N    1 
ATOM   1586 C  CA   . GLY   C 1 17 ? 18.202  -1.736  13.013  1.00 33.47 ? 17  GLY   C CA   1 
ATOM   1587 C  C    . GLY   C 1 17 ? 19.176  -2.854  12.704  1.00 36.04 ? 17  GLY   C C    1 
ATOM   1588 O  O    . GLY   C 1 17 ? 20.182  -2.608  12.032  1.00 32.05 ? 17  GLY   C O    1 
ATOM   1589 N  N    . TYR   C 1 18 ? 18.925  -4.064  13.186  1.00 27.53 ? 18  TYR   C N    1 
ATOM   1590 C  CA   . TYR   C 1 18 ? 19.865  -5.166  13.063  1.00 26.32 ? 18  TYR   C CA   1 
ATOM   1591 C  C    . TYR   C 1 18 ? 19.093  -6.447  12.790  1.00 28.37 ? 18  TYR   C C    1 
ATOM   1592 O  O    . TYR   C 1 18 ? 17.956  -6.601  13.255  1.00 24.66 ? 18  TYR   C O    1 
ATOM   1593 C  CB   . TYR   C 1 18 ? 20.707  -5.324  14.344  1.00 24.54 ? 18  TYR   C CB   1 
ATOM   1594 C  CG   . TYR   C 1 18 ? 21.615  -4.152  14.613  1.00 26.11 ? 18  TYR   C CG   1 
ATOM   1595 C  CD1  . TYR   C 1 18 ? 21.125  -2.969  15.162  1.00 29.34 ? 18  TYR   C CD1  1 
ATOM   1596 C  CD2  . TYR   C 1 18 ? 22.973  -4.227  14.330  1.00 38.64 ? 18  TYR   C CD2  1 
ATOM   1597 C  CE1  . TYR   C 1 18 ? 21.959  -1.895  15.401  1.00 32.22 ? 18  TYR   C CE1  1 
ATOM   1598 C  CE2  . TYR   C 1 18 ? 23.816  -3.154  14.576  1.00 32.39 ? 18  TYR   C CE2  1 
ATOM   1599 C  CZ   . TYR   C 1 18 ? 23.302  -1.993  15.111  1.00 37.44 ? 18  TYR   C CZ   1 
ATOM   1600 O  OH   . TYR   C 1 18 ? 24.137  -0.913  15.348  1.00 42.31 ? 18  TYR   C OH   1 
ATOM   1601 N  N    . PRO   C 1 19 ? 19.670  -7.368  12.024  1.00 24.72 ? 19  PRO   C N    1 
ATOM   1602 C  CA   . PRO   C 1 19 ? 19.034  -8.674  11.838  1.00 26.45 ? 19  PRO   C CA   1 
ATOM   1603 C  C    . PRO   C 1 19 ? 19.046  -9.436  13.150  1.00 21.75 ? 19  PRO   C C    1 
ATOM   1604 O  O    . PRO   C 1 19 ? 19.861  -9.159  14.032  1.00 24.54 ? 19  PRO   C O    1 
ATOM   1605 C  CB   . PRO   C 1 19 ? 19.933  -9.361  10.815  1.00 22.61 ? 19  PRO   C CB   1 
ATOM   1606 C  CG   . PRO   C 1 19 ? 21.292  -8.759  11.079  1.00 25.54 ? 19  PRO   C CG   1 
ATOM   1607 C  CD   . PRO   C 1 19 ? 21.033  -7.326  11.460  1.00 25.72 ? 19  PRO   C CD   1 
ATOM   1608 N  N    . HIS   C 1 20 ? 18.135  -10.403 13.278  1.00 24.95 ? 20  HIS   C N    1 
ATOM   1609 C  CA   . HIS   C 1 20 ? 18.203  -11.307 14.427  1.00 23.26 ? 20  HIS   C CA   1 
ATOM   1610 C  C    . HIS   C 1 20 ? 19.609  -11.883 14.523  1.00 20.96 ? 20  HIS   C C    1 
ATOM   1611 O  O    . HIS   C 1 20 ? 20.131  -12.429 13.543  1.00 25.25 ? 20  HIS   C O    1 
ATOM   1612 C  CB   . HIS   C 1 20 ? 17.188  -12.434 14.293  1.00 25.83 ? 20  HIS   C CB   1 
ATOM   1613 C  CG   . HIS   C 1 20 ? 15.770  -11.974 14.301  1.00 27.84 ? 20  HIS   C CG   1 
ATOM   1614 N  ND1  . HIS   C 1 20 ? 15.157  -11.431 13.193  1.00 26.07 ? 20  HIS   C ND1  1 
ATOM   1615 C  CD2  . HIS   C 1 20 ? 14.837  -11.991 15.283  1.00 30.00 ? 20  HIS   C CD2  1 
ATOM   1616 C  CE1  . HIS   C 1 20 ? 13.907  -11.126 13.494  1.00 30.56 ? 20  HIS   C CE1  1 
ATOM   1617 N  NE2  . HIS   C 1 20 ? 13.689  -11.454 14.756  1.00 33.65 ? 20  HIS   C NE2  1 
ATOM   1618 N  N    . TRP   C 1 21 ? 20.218  -11.748 15.704  1.00 21.28 ? 21  TRP   C N    1 
ATOM   1619 C  CA   . TRP   C 1 21 ? 21.649  -11.934 15.881  1.00 21.34 ? 21  TRP   C CA   1 
ATOM   1620 C  C    . TRP   C 1 21 ? 21.941  -13.090 16.836  1.00 22.32 ? 21  TRP   C C    1 
ATOM   1621 O  O    . TRP   C 1 21 ? 21.342  -13.158 17.917  1.00 22.88 ? 21  TRP   C O    1 
ATOM   1622 C  CB   . TRP   C 1 21 ? 22.287  -10.660 16.423  1.00 24.41 ? 21  TRP   C CB   1 
ATOM   1623 C  CG   . TRP   C 1 21 ? 23.747  -10.517 16.102  1.00 25.66 ? 21  TRP   C CG   1 
ATOM   1624 C  CD1  . TRP   C 1 21 ? 24.789  -11.162 16.702  1.00 26.88 ? 21  TRP   C CD1  1 
ATOM   1625 C  CD2  . TRP   C 1 21 ? 24.325  -9.657  15.108  1.00 23.61 ? 21  TRP   C CD2  1 
ATOM   1626 N  NE1  . TRP   C 1 21 ? 25.980  -10.772 16.125  1.00 24.95 ? 21  TRP   C NE1  1 
ATOM   1627 C  CE2  . TRP   C 1 21 ? 25.721  -9.845  15.151  1.00 24.69 ? 21  TRP   C CE2  1 
ATOM   1628 C  CE3  . TRP   C 1 21 ? 23.795  -8.740  14.188  1.00 26.18 ? 21  TRP   C CE3  1 
ATOM   1629 C  CZ2  . TRP   C 1 21 ? 26.598  -9.144  14.311  1.00 29.26 ? 21  TRP   C CZ2  1 
ATOM   1630 C  CZ3  . TRP   C 1 21 ? 24.661  -8.055  13.352  1.00 27.13 ? 21  TRP   C CZ3  1 
ATOM   1631 C  CH2  . TRP   C 1 21 ? 26.048  -8.259  13.423  1.00 27.28 ? 21  TRP   C CH2  1 
ATOM   1632 N  N    . PRO   C 1 22 ? 22.862  -13.987 16.492  1.00 21.01 ? 22  PRO   C N    1 
ATOM   1633 C  CA   . PRO   C 1 22 ? 23.186  -15.102 17.393  1.00 21.64 ? 22  PRO   C CA   1 
ATOM   1634 C  C    . PRO   C 1 22 ? 23.746  -14.563 18.698  1.00 23.23 ? 22  PRO   C C    1 
ATOM   1635 O  O    . PRO   C 1 22 ? 24.645  -13.719 18.696  1.00 24.08 ? 22  PRO   C O    1 
ATOM   1636 C  CB   . PRO   C 1 22 ? 24.238  -15.892 16.617  1.00 22.07 ? 22  PRO   C CB   1 
ATOM   1637 C  CG   . PRO   C 1 22 ? 24.862  -14.847 15.676  1.00 20.36 ? 22  PRO   C CG   1 
ATOM   1638 C  CD   . PRO   C 1 22 ? 23.678  -14.015 15.262  1.00 22.83 ? 22  PRO   C CD   1 
ATOM   1639 N  N    . ALA   C 1 23 ? 23.215  -15.063 19.817  1.00 23.57 ? 23  ALA   C N    1 
ATOM   1640 C  CA   . ALA   C 1 23 ? 23.521  -14.469 21.113  1.00 24.48 ? 23  ALA   C CA   1 
ATOM   1641 C  C    . ALA   C 1 23 ? 23.300  -15.499 22.208  1.00 30.76 ? 23  ALA   C C    1 
ATOM   1642 O  O    . ALA   C 1 23 ? 22.805  -16.605 21.968  1.00 27.60 ? 23  ALA   C O    1 
ATOM   1643 C  CB   . ALA   C 1 23 ? 22.656  -13.224 21.380  1.00 24.15 ? 23  ALA   C CB   1 
ATOM   1644 N  N    . ARG   C 1 24 ? 23.673  -15.120 23.426  1.00 28.84 ? 24  ARG   C N    1 
ATOM   1645 C  CA   . ARG   C 1 24 ? 23.404  -15.985 24.557  1.00 31.40 ? 24  ARG   C CA   1 
ATOM   1646 C  C    . ARG   C 1 24 ? 22.999  -15.117 25.732  1.00 32.08 ? 24  ARG   C C    1 
ATOM   1647 O  O    . ARG   C 1 24 ? 23.363  -13.941 25.805  1.00 31.96 ? 24  ARG   C O    1 
ATOM   1648 C  CB   . ARG   C 1 24 ? 24.611  -16.866 24.915  1.00 32.54 ? 24  ARG   C CB   1 
ATOM   1649 C  CG   . ARG   C 1 24 ? 25.871  -16.115 25.221  1.00 33.52 ? 24  ARG   C CG   1 
ATOM   1650 C  CD   . ARG   C 1 24 ? 26.857  -16.980 25.982  1.00 41.80 ? 24  ARG   C CD   1 
ATOM   1651 N  NE   . ARG   C 1 24 ? 27.962  -16.176 26.486  1.00 49.97 ? 24  ARG   C NE   1 
ATOM   1652 C  CZ   . ARG   C 1 24 ? 29.231  -16.556 26.476  1.00 56.05 ? 24  ARG   C CZ   1 
ATOM   1653 N  NH1  . ARG   C 1 24 ? 29.604  -17.701 25.927  1.00 54.11 ? 24  ARG   C NH1  1 
ATOM   1654 N  NH2  . ARG   C 1 24 ? 30.150  -15.764 27.021  1.00 61.68 ? 24  ARG   C NH2  1 
ATOM   1655 N  N    . ILE   C 1 25 ? 22.205  -15.704 26.622  1.00 34.43 ? 25  ILE   C N    1 
ATOM   1656 C  CA   . ILE   C 1 25 ? 21.839  -15.038 27.867  1.00 36.41 ? 25  ILE   C CA   1 
ATOM   1657 C  C    . ILE   C 1 25 ? 23.045  -15.013 28.795  1.00 47.79 ? 25  ILE   C C    1 
ATOM   1658 O  O    . ILE   C 1 25 ? 23.632  -16.061 29.097  1.00 45.24 ? 25  ILE   C O    1 
ATOM   1659 C  CB   . ILE   C 1 25 ? 20.659  -15.761 28.534  1.00 40.43 ? 25  ILE   C CB   1 
ATOM   1660 C  CG1  . ILE   C 1 25 ? 19.467  -15.916 27.589  1.00 39.49 ? 25  ILE   C CG1  1 
ATOM   1661 C  CG2  . ILE   C 1 25 ? 20.274  -15.069 29.822  1.00 41.27 ? 25  ILE   C CG2  1 
ATOM   1662 C  CD1  . ILE   C 1 25 ? 18.889  -14.607 27.065  1.00 35.46 ? 25  ILE   C CD1  1 
ATOM   1663 N  N    . ASP   C 1 26 ? 23.412  -13.824 29.271  1.00 58.67 ? 26  ASP   C N    1 
ATOM   1664 C  CA   . ASP   C 1 26 ? 24.532  -13.680 30.186  1.00 60.59 ? 26  ASP   C CA   1 
ATOM   1665 C  C    . ASP   C 1 26 ? 24.049  -13.771 31.634  1.00 61.71 ? 26  ASP   C C    1 
ATOM   1666 O  O    . ASP   C 1 26 ? 22.868  -13.983 31.916  1.00 61.00 ? 26  ASP   C O    1 
ATOM   1667 C  CB   . ASP   C 1 26 ? 25.256  -12.352 29.957  1.00 60.06 ? 26  ASP   C CB   1 
ATOM   1668 C  CG   . ASP   C 1 26 ? 26.667  -12.530 29.409  1.00 61.51 ? 26  ASP   C CG   1 
ATOM   1669 O  OD1  . ASP   C 1 26 ? 27.091  -13.690 29.180  1.00 64.16 ? 26  ASP   C OD1  1 
ATOM   1670 O  OD2  . ASP   C 1 26 ? 27.366  -11.501 29.246  1.00 61.41 ? 26  ASP   C OD2  1 
ATOM   1671 N  N    . ASP   C 1 27 ? 24.980  -13.610 32.567  1.00 63.72 ? 27  ASP   C N    1 
ATOM   1672 C  CA   . ASP   C 1 27 ? 24.666  -13.418 33.974  1.00 64.94 ? 27  ASP   C CA   1 
ATOM   1673 C  C    . ASP   C 1 27 ? 25.078  -12.010 34.380  1.00 64.64 ? 27  ASP   C C    1 
ATOM   1674 O  O    . ASP   C 1 27 ? 25.821  -11.333 33.667  1.00 68.52 ? 27  ASP   C O    1 
ATOM   1675 C  CB   . ASP   C 1 27 ? 25.378  -14.456 34.851  1.00 68.17 ? 27  ASP   C CB   1 
ATOM   1676 N  N    . ILE   C 1 28 ? 24.576  -11.562 35.525  1.00 65.11 ? 28  ILE   C N    1 
ATOM   1677 C  CA   . ILE   C 1 28 ? 24.959  -10.277 36.102  1.00 65.29 ? 28  ILE   C CA   1 
ATOM   1678 C  C    . ILE   C 1 28 ? 25.707  -10.562 37.396  1.00 71.82 ? 28  ILE   C C    1 
ATOM   1679 O  O    . ILE   C 1 28 ? 25.144  -11.154 38.326  1.00 75.91 ? 28  ILE   C O    1 
ATOM   1680 C  CB   . ILE   C 1 28 ? 23.743  -9.372  36.354  1.00 66.35 ? 28  ILE   C CB   1 
ATOM   1681 C  CG1  . ILE   C 1 28 ? 23.300  -8.691  35.060  1.00 64.52 ? 28  ILE   C CG1  1 
ATOM   1682 C  CG2  . ILE   C 1 28 ? 24.069  -8.317  37.399  1.00 71.54 ? 28  ILE   C CG2  1 
ATOM   1683 C  CD1  . ILE   C 1 28 ? 24.435  -8.019  34.294  1.00 73.21 ? 28  ILE   C CD1  1 
ATOM   1684 N  N    . ALA   C 1 29 ? 26.974  -10.156 37.453  1.00 70.19 ? 29  ALA   C N    1 
ATOM   1685 C  CA   . ALA   C 1 29 ? 27.764  -10.363 38.660  1.00 73.62 ? 29  ALA   C CA   1 
ATOM   1686 C  C    . ALA   C 1 29 ? 27.171  -9.571  39.822  1.00 73.91 ? 29  ALA   C C    1 
ATOM   1687 O  O    . ALA   C 1 29 ? 26.583  -8.501  39.638  1.00 72.62 ? 29  ALA   C O    1 
ATOM   1688 C  CB   . ALA   C 1 29 ? 29.220  -9.958  38.427  1.00 75.44 ? 29  ALA   C CB   1 
ATOM   1689 N  N    . ASP   C 1 30 ? 27.308  -10.122 41.030  1.00 76.80 ? 30  ASP   C N    1 
ATOM   1690 C  CA   . ASP   C 1 30 ? 26.839  -9.447  42.237  1.00 78.72 ? 30  ASP   C CA   1 
ATOM   1691 C  C    . ASP   C 1 30 ? 27.593  -8.138  42.453  1.00 78.21 ? 30  ASP   C C    1 
ATOM   1692 O  O    . ASP   C 1 30 ? 28.806  -8.139  42.699  1.00 81.00 ? 30  ASP   C O    1 
ATOM   1693 C  CB   . ASP   C 1 30 ? 26.983  -10.358 43.461  1.00 81.18 ? 30  ASP   C CB   1 
ATOM   1694 N  N    . GLY   C 1 31 ? 26.877  -7.014  42.358  1.00 75.83 ? 31  GLY   C N    1 
ATOM   1695 C  CA   . GLY   C 1 31 ? 27.458  -5.686  42.462  1.00 76.19 ? 31  GLY   C CA   1 
ATOM   1696 C  C    . GLY   C 1 31 ? 27.243  -4.835  41.225  1.00 73.14 ? 31  GLY   C C    1 
ATOM   1697 O  O    . GLY   C 1 31 ? 27.217  -3.605  41.323  1.00 72.67 ? 31  GLY   C O    1 
ATOM   1698 N  N    . ALA   C 1 32 ? 27.084  -5.469  40.065  1.00 71.29 ? 32  ALA   C N    1 
ATOM   1699 C  CA   . ALA   C 1 32 ? 26.873  -4.743  38.822  1.00 68.77 ? 32  ALA   C CA   1 
ATOM   1700 C  C    . ALA   C 1 32 ? 25.491  -4.092  38.808  1.00 68.70 ? 32  ALA   C C    1 
ATOM   1701 O  O    . ALA   C 1 32 ? 24.618  -4.400  39.628  1.00 65.87 ? 32  ALA   C O    1 
ATOM   1702 C  CB   . ALA   C 1 32 ? 27.026  -5.678  37.622  1.00 67.63 ? 32  ALA   C CB   1 
ATOM   1703 N  N    . VAL   C 1 33 ? 25.297  -3.173  37.856  1.00 67.49 ? 33  VAL   C N    1 
ATOM   1704 C  CA   . VAL   C 1 33 ? 23.994  -2.537  37.689  1.00 65.62 ? 33  VAL   C CA   1 
ATOM   1705 C  C    . VAL   C 1 33 ? 23.017  -3.540  37.097  1.00 65.53 ? 33  VAL   C C    1 
ATOM   1706 O  O    . VAL   C 1 33 ? 23.315  -4.212  36.098  1.00 59.30 ? 33  VAL   C O    1 
ATOM   1707 C  CB   . VAL   C 1 33 ? 24.091  -1.276  36.816  1.00 67.77 ? 33  VAL   C CB   1 
ATOM   1708 C  CG1  . VAL   C 1 33 ? 22.904  -0.366  37.089  1.00 66.75 ? 33  VAL   C CG1  1 
ATOM   1709 C  CG2  . VAL   C 1 33 ? 25.375  -0.525  37.098  1.00 73.00 ? 33  VAL   C CG2  1 
ATOM   1710 N  N    . LYS   C 1 34 ? 21.842  -3.642  37.715  1.00 64.40 ? 34  LYS   C N    1 
ATOM   1711 C  CA   . LYS   C 1 34 ? 20.840  -4.597  37.291  1.00 57.54 ? 34  LYS   C CA   1 
ATOM   1712 C  C    . LYS   C 1 34 ? 20.250  -4.176  35.950  1.00 56.80 ? 34  LYS   C C    1 
ATOM   1713 O  O    . LYS   C 1 34 ? 20.311  -3.003  35.570  1.00 54.44 ? 34  LYS   C O    1 
ATOM   1714 C  CB   . LYS   C 1 34 ? 19.739  -4.716  38.345  1.00 57.51 ? 34  LYS   C CB   1 
ATOM   1715 N  N    . PRO   C 1 35 ? 19.691  -5.122  35.204  1.00 54.29 ? 35  PRO   C N    1 
ATOM   1716 C  CA   . PRO   C 1 35 ? 18.972  -4.765  33.988  1.00 52.29 ? 35  PRO   C CA   1 
ATOM   1717 C  C    . PRO   C 1 35 ? 17.760  -3.913  34.316  1.00 53.00 ? 35  PRO   C C    1 
ATOM   1718 O  O    . PRO   C 1 35 ? 17.274  -3.916  35.460  1.00 51.52 ? 35  PRO   C O    1 
ATOM   1719 C  CB   . PRO   C 1 35 ? 18.552  -6.122  33.400  1.00 52.08 ? 35  PRO   C CB   1 
ATOM   1720 C  CG   . PRO   C 1 35 ? 19.273  -7.170  34.194  1.00 54.08 ? 35  PRO   C CG   1 
ATOM   1721 C  CD   . PRO   C 1 35 ? 19.696  -6.572  35.472  1.00 55.39 ? 35  PRO   C CD   1 
ATOM   1722 N  N    . PRO   C 1 36 ? 17.252  -3.160  33.346  1.00 49.58 ? 36  PRO   C N    1 
ATOM   1723 C  CA   . PRO   C 1 36 ? 15.915  -2.581  33.482  1.00 48.38 ? 36  PRO   C CA   1 
ATOM   1724 C  C    . PRO   C 1 36 ? 14.905  -3.670  33.788  1.00 48.25 ? 36  PRO   C C    1 
ATOM   1725 O  O    . PRO   C 1 36 ? 15.178  -4.856  33.548  1.00 48.86 ? 36  PRO   C O    1 
ATOM   1726 C  CB   . PRO   C 1 36 ? 15.660  -1.951  32.105  1.00 47.26 ? 36  PRO   C CB   1 
ATOM   1727 C  CG   . PRO   C 1 36 ? 17.020  -1.662  31.585  1.00 48.02 ? 36  PRO   C CG   1 
ATOM   1728 C  CD   . PRO   C 1 36 ? 17.918  -2.743  32.100  1.00 49.27 ? 36  PRO   C CD   1 
ATOM   1729 N  N    . PRO   C 1 37 ? 13.747  -3.313  34.340  1.00 47.68 ? 37  PRO   C N    1 
ATOM   1730 C  CA   . PRO   C 1 37 ? 12.742  -4.330  34.668  1.00 47.86 ? 37  PRO   C CA   1 
ATOM   1731 C  C    . PRO   C 1 37 ? 12.459  -5.257  33.496  1.00 47.54 ? 37  PRO   C C    1 
ATOM   1732 O  O    . PRO   C 1 37 ? 12.246  -4.817  32.364  1.00 46.57 ? 37  PRO   C O    1 
ATOM   1733 C  CB   . PRO   C 1 37 ? 11.505  -3.506  35.046  1.00 47.02 ? 37  PRO   C CB   1 
ATOM   1734 C  CG   . PRO   C 1 37 ? 12.004  -2.120  35.372  1.00 47.69 ? 37  PRO   C CG   1 
ATOM   1735 C  CD   . PRO   C 1 37 ? 13.437  -1.996  34.922  1.00 51.87 ? 37  PRO   C CD   1 
ATOM   1736 N  N    . ASN   C 1 38 ? 12.491  -6.557  33.789  1.00 48.63 ? 38  ASN   C N    1 
ATOM   1737 C  CA   . ASN   C 1 38 ? 12.112  -7.640  32.891  1.00 48.74 ? 38  ASN   C CA   1 
ATOM   1738 C  C    . ASN   C 1 38 ? 13.049  -7.772  31.690  1.00 48.46 ? 38  ASN   C C    1 
ATOM   1739 O  O    . ASN   C 1 38 ? 12.678  -8.385  30.681  1.00 48.27 ? 38  ASN   C O    1 
ATOM   1740 C  CB   . ASN   C 1 38 ? 10.664  -7.478  32.420  1.00 47.92 ? 38  ASN   C CB   1 
ATOM   1741 C  CG   . ASN   C 1 38 ? 10.053  -8.786  31.958  1.00 52.99 ? 38  ASN   C CG   1 
ATOM   1742 O  OD1  . ASN   C 1 38 ? 9.367   -8.843  30.937  1.00 63.67 ? 38  ASN   C OD1  1 
ATOM   1743 N  ND2  . ASN   C 1 38 ? 10.270  -9.845  32.736  1.00 58.46 ? 38  ASN   C ND2  1 
ATOM   1744 N  N    . LYS   C 1 39 ? 14.260  -7.218  31.770  1.00 40.51 ? 39  LYS   C N    1 
ATOM   1745 C  CA   . LYS   C 1 39 ? 15.266  -7.347  30.721  1.00 37.66 ? 39  LYS   C CA   1 
ATOM   1746 C  C    . LYS   C 1 39 ? 16.308  -8.378  31.143  1.00 38.16 ? 39  LYS   C C    1 
ATOM   1747 O  O    . LYS   C 1 39 ? 16.590  -8.539  32.333  1.00 41.01 ? 39  LYS   C O    1 
ATOM   1748 C  CB   . LYS   C 1 39 ? 15.970  -6.011  30.455  1.00 39.45 ? 39  LYS   C CB   1 
ATOM   1749 C  CG   . LYS   C 1 39 ? 15.188  -4.960  29.656  1.00 41.87 ? 39  LYS   C CG   1 
ATOM   1750 C  CD   . LYS   C 1 39 ? 14.053  -5.568  28.868  1.00 41.88 ? 39  LYS   C CD   1 
ATOM   1751 C  CE   . LYS   C 1 39 ? 13.126  -4.503  28.283  1.00 52.18 ? 39  LYS   C CE   1 
ATOM   1752 N  NZ   . LYS   C 1 39 ? 11.699  -4.949  28.303  1.00 54.20 ? 39  LYS   C NZ   1 
ATOM   1753 N  N    . TYR   C 1 40 ? 16.893  -9.069  30.156  1.00 35.89 ? 40  TYR   C N    1 
ATOM   1754 C  CA   . TYR   C 1 40 ? 17.986  -10.041 30.237  1.00 36.73 ? 40  TYR   C CA   1 
ATOM   1755 C  C    . TYR   C 1 40 ? 19.306  -9.417  29.810  1.00 38.57 ? 40  TYR   C C    1 
ATOM   1756 O  O    . TYR   C 1 40 ? 19.338  -8.640  28.847  1.00 33.42 ? 40  TYR   C O    1 
ATOM   1757 C  CB   . TYR   C 1 40 ? 17.741  -11.250 29.332  1.00 34.87 ? 40  TYR   C CB   1 
ATOM   1758 C  CG   . TYR   C 1 40 ? 16.595  -12.138 29.741  1.00 40.98 ? 40  TYR   C CG   1 
ATOM   1759 C  CD1  . TYR   C 1 40 ? 15.292  -11.841 29.365  1.00 36.36 ? 40  TYR   C CD1  1 
ATOM   1760 C  CD2  . TYR   C 1 40 ? 16.818  -13.279 30.503  1.00 39.64 ? 40  TYR   C CD2  1 
ATOM   1761 C  CE1  . TYR   C 1 40 ? 14.245  -12.654 29.742  1.00 39.81 ? 40  TYR   C CE1  1 
ATOM   1762 C  CE2  . TYR   C 1 40 ? 15.776  -14.103 30.882  1.00 42.06 ? 40  TYR   C CE2  1 
ATOM   1763 C  CZ   . TYR   C 1 40 ? 14.493  -13.784 30.502  1.00 42.21 ? 40  TYR   C CZ   1 
ATOM   1764 O  OH   . TYR   C 1 40 ? 13.453  -14.597 30.885  1.00 45.01 ? 40  TYR   C OH   1 
ATOM   1765 N  N    . PRO   C 1 41 ? 20.413  -9.767  30.468  1.00 36.99 ? 41  PRO   C N    1 
ATOM   1766 C  CA   . PRO   C 1 41 ? 21.737  -9.394  29.941  1.00 36.24 ? 41  PRO   C CA   1 
ATOM   1767 C  C    . PRO   C 1 41 ? 22.088  -10.274 28.752  1.00 39.10 ? 41  PRO   C C    1 
ATOM   1768 O  O    . PRO   C 1 41 ? 22.085  -11.501 28.859  1.00 34.78 ? 41  PRO   C O    1 
ATOM   1769 C  CB   . PRO   C 1 41 ? 22.680  -9.635  31.125  1.00 39.94 ? 41  PRO   C CB   1 
ATOM   1770 C  CG   . PRO   C 1 41 ? 21.968  -10.624 31.991  1.00 45.28 ? 41  PRO   C CG   1 
ATOM   1771 C  CD   . PRO   C 1 41 ? 20.493  -10.492 31.748  1.00 41.79 ? 41  PRO   C CD   1 
ATOM   1772 N  N    . ILE   C 1 42 ? 22.402  -9.644  27.624  1.00 31.55 ? 42  ILE   C N    1 
ATOM   1773 C  CA   . ILE   C 1 42 ? 22.657  -10.346 26.370  1.00 29.44 ? 42  ILE   C CA   1 
ATOM   1774 C  C    . ILE   C 1 42 ? 24.119  -10.167 25.987  1.00 33.51 ? 42  ILE   C C    1 
ATOM   1775 O  O    . ILE   C 1 42 ? 24.679  -9.072  26.121  1.00 31.61 ? 42  ILE   C O    1 
ATOM   1776 C  CB   . ILE   C 1 42 ? 21.740  -9.848  25.237  1.00 29.99 ? 42  ILE   C CB   1 
ATOM   1777 C  CG1  . ILE   C 1 42 ? 20.271  -10.007 25.638  1.00 36.57 ? 42  ILE   C CG1  1 
ATOM   1778 C  CG2  . ILE   C 1 42 ? 22.047  -10.584 23.930  1.00 27.57 ? 42  ILE   C CG2  1 
ATOM   1779 C  CD1  . ILE   C 1 42 ? 19.924  -11.407 26.111  1.00 33.93 ? 42  ILE   C CD1  1 
ATOM   1780 N  N    . PHE   C 1 43 ? 24.730  -11.252 25.514  1.00 29.56 ? 43  PHE   C N    1 
ATOM   1781 C  CA   . PHE   C 1 43 ? 26.041  -11.254 24.873  1.00 32.08 ? 43  PHE   C CA   1 
ATOM   1782 C  C    . PHE   C 1 43 ? 25.857  -11.640 23.414  1.00 33.35 ? 43  PHE   C C    1 
ATOM   1783 O  O    . PHE   C 1 43 ? 25.291  -12.702 23.125  1.00 29.22 ? 43  PHE   C O    1 
ATOM   1784 C  CB   . PHE   C 1 43 ? 26.969  -12.242 25.575  1.00 35.13 ? 43  PHE   C CB   1 
ATOM   1785 C  CG   . PHE   C 1 43 ? 28.327  -12.380 24.938  1.00 33.11 ? 43  PHE   C CG   1 
ATOM   1786 C  CD1  . PHE   C 1 43 ? 29.336  -11.453 25.188  1.00 38.74 ? 43  PHE   C CD1  1 
ATOM   1787 C  CD2  . PHE   C 1 43 ? 28.605  -13.461 24.115  1.00 32.70 ? 43  PHE   C CD2  1 
ATOM   1788 C  CE1  . PHE   C 1 43 ? 30.607  -11.609 24.623  1.00 38.20 ? 43  PHE   C CE1  1 
ATOM   1789 C  CE2  . PHE   C 1 43 ? 29.853  -13.610 23.533  1.00 35.27 ? 43  PHE   C CE2  1 
ATOM   1790 C  CZ   . PHE   C 1 43 ? 30.854  -12.686 23.784  1.00 41.74 ? 43  PHE   C CZ   1 
ATOM   1791 N  N    . PHE   C 1 44 ? 26.325  -10.782 22.498  1.00 26.98 ? 44  PHE   C N    1 
ATOM   1792 C  CA   . PHE   C 1 44 ? 26.201  -11.033 21.064  1.00 26.84 ? 44  PHE   C CA   1 
ATOM   1793 C  C    . PHE   C 1 44 ? 27.446  -11.750 20.551  1.00 30.43 ? 44  PHE   C C    1 
ATOM   1794 O  O    . PHE   C 1 44 ? 28.570  -11.278 20.758  1.00 30.87 ? 44  PHE   C O    1 
ATOM   1795 C  CB   . PHE   C 1 44 ? 25.994  -9.726  20.289  1.00 25.28 ? 44  PHE   C CB   1 
ATOM   1796 C  CG   . PHE   C 1 44 ? 24.710  -9.022  20.623  1.00 24.13 ? 44  PHE   C CG   1 
ATOM   1797 C  CD1  . PHE   C 1 44 ? 23.526  -9.388  20.012  1.00 27.38 ? 44  PHE   C CD1  1 
ATOM   1798 C  CD2  . PHE   C 1 44 ? 24.686  -7.987  21.553  1.00 34.01 ? 44  PHE   C CD2  1 
ATOM   1799 C  CE1  . PHE   C 1 44 ? 22.332  -8.741  20.323  1.00 23.48 ? 44  PHE   C CE1  1 
ATOM   1800 C  CE2  . PHE   C 1 44 ? 23.499  -7.335  21.862  1.00 31.99 ? 44  PHE   C CE2  1 
ATOM   1801 C  CZ   . PHE   C 1 44 ? 22.328  -7.719  21.242  1.00 23.68 ? 44  PHE   C CZ   1 
ATOM   1802 N  N    . PHE   C 1 45 ? 27.245  -12.900 19.900  1.00 30.66 ? 45  PHE   C N    1 
ATOM   1803 C  CA   . PHE   C 1 45 ? 28.370  -13.592 19.285  1.00 29.24 ? 45  PHE   C CA   1 
ATOM   1804 C  C    . PHE   C 1 45 ? 28.926  -12.772 18.125  1.00 26.54 ? 45  PHE   C C    1 
ATOM   1805 O  O    . PHE   C 1 45 ? 28.233  -11.958 17.510  1.00 26.75 ? 45  PHE   C O    1 
ATOM   1806 C  CB   . PHE   C 1 45 ? 27.959  -14.986 18.793  1.00 26.27 ? 45  PHE   C CB   1 
ATOM   1807 C  CG   . PHE   C 1 45 ? 27.695  -15.972 19.910  1.00 30.32 ? 45  PHE   C CG   1 
ATOM   1808 C  CD1  . PHE   C 1 45 ? 28.734  -16.408 20.720  1.00 31.10 ? 45  PHE   C CD1  1 
ATOM   1809 C  CD2  . PHE   C 1 45 ? 26.414  -16.453 20.150  1.00 27.98 ? 45  PHE   C CD2  1 
ATOM   1810 C  CE1  . PHE   C 1 45 ? 28.502  -17.321 21.755  1.00 37.18 ? 45  PHE   C CE1  1 
ATOM   1811 C  CE2  . PHE   C 1 45 ? 26.177  -17.377 21.174  1.00 30.38 ? 45  PHE   C CE2  1 
ATOM   1812 C  CZ   . PHE   C 1 45 ? 27.224  -17.799 21.980  1.00 33.04 ? 45  PHE   C CZ   1 
ATOM   1813 N  N    . GLY   C 1 46 ? 30.198  -12.996 17.826  1.00 26.82 ? 46  GLY   C N    1 
ATOM   1814 C  CA   . GLY   C 1 46 ? 30.806  -12.291 16.720  1.00 26.66 ? 46  GLY   C CA   1 
ATOM   1815 C  C    . GLY   C 1 46 ? 31.346  -10.947 17.155  1.00 33.12 ? 46  GLY   C C    1 
ATOM   1816 O  O    . GLY   C 1 46 ? 32.558  -10.715 17.122  1.00 30.55 ? 46  GLY   C O    1 
ATOM   1817 N  N    . THR   C 1 47 ? 30.454  -10.048 17.571  1.00 27.80 ? 47  THR   C N    1 
ATOM   1818 C  CA   . THR   C 1 47 ? 30.900  -8.739  18.032  1.00 28.18 ? 47  THR   C CA   1 
ATOM   1819 C  C    . THR   C 1 47 ? 31.368  -8.775  19.478  1.00 36.98 ? 47  THR   C C    1 
ATOM   1820 O  O    . THR   C 1 47 ? 32.225  -7.963  19.875  1.00 36.09 ? 47  THR   C O    1 
ATOM   1821 C  CB   . THR   C 1 47 ? 29.772  -7.719  17.892  1.00 30.07 ? 47  THR   C CB   1 
ATOM   1822 O  OG1  . THR   C 1 47 ? 28.697  -8.093  18.762  1.00 27.42 ? 47  THR   C OG1  1 
ATOM   1823 C  CG2  . THR   C 1 47 ? 29.266  -7.661  16.461  1.00 26.28 ? 47  THR   C CG2  1 
ATOM   1824 N  N    . HIS   C 1 48 ? 30.806  -9.693  20.270  1.00 30.35 ? 48  HIS   C N    1 
ATOM   1825 C  CA   . HIS   C 1 48 ? 31.110  -9.823  21.695  1.00 31.54 ? 48  HIS   C CA   1 
ATOM   1826 C  C    . HIS   C 1 48 ? 30.671  -8.593  22.486  1.00 34.33 ? 48  HIS   C C    1 
ATOM   1827 O  O    . HIS   C 1 48 ? 31.188  -8.322  23.575  1.00 35.79 ? 48  HIS   C O    1 
ATOM   1828 C  CB   . HIS   C 1 48 ? 32.588  -10.133 21.936  1.00 34.55 ? 48  HIS   C CB   1 
ATOM   1829 C  CG   . HIS   C 1 48 ? 33.108  -11.274 21.116  1.00 35.77 ? 48  HIS   C CG   1 
ATOM   1830 N  ND1  . HIS   C 1 48 ? 34.383  -11.299 20.594  1.00 43.53 ? 48  HIS   C ND1  1 
ATOM   1831 C  CD2  . HIS   C 1 48 ? 32.510  -12.414 20.697  1.00 37.81 ? 48  HIS   C CD2  1 
ATOM   1832 C  CE1  . HIS   C 1 48 ? 34.556  -12.414 19.910  1.00 41.08 ? 48  HIS   C CE1  1 
ATOM   1833 N  NE2  . HIS   C 1 48 ? 33.433  -13.107 19.953  1.00 42.00 ? 48  HIS   C NE2  1 
ATOM   1834 N  N    . GLU   C 1 49 ? 29.687  -7.864  21.968  1.00 30.43 ? 49  GLU   C N    1 
ATOM   1835 C  CA   . GLU   C 1 49 ? 29.099  -6.733  22.666  1.00 37.73 ? 49  GLU   C CA   1 
ATOM   1836 C  C    . GLU   C 1 49 ? 27.979  -7.212  23.586  1.00 33.53 ? 49  GLU   C C    1 
ATOM   1837 O  O    . GLU   C 1 49 ? 27.596  -8.381  23.579  1.00 35.50 ? 49  GLU   C O    1 
ATOM   1838 C  CB   . GLU   C 1 49 ? 28.584  -5.710  21.660  1.00 38.67 ? 49  GLU   C CB   1 
ATOM   1839 C  CG   . GLU   C 1 49 ? 29.683  -5.167  20.785  1.00 34.75 ? 49  GLU   C CG   1 
ATOM   1840 C  CD   . GLU   C 1 49 ? 29.161  -4.227  19.727  1.00 42.30 ? 49  GLU   C CD   1 
ATOM   1841 O  OE1  . GLU   C 1 49 ? 27.936  -4.201  19.508  1.00 32.86 ? 49  GLU   C OE1  1 
ATOM   1842 O  OE2  . GLU   C 1 49 ? 29.975  -3.512  19.116  1.00 43.59 ? 49  GLU   C OE2  1 
ATOM   1843 N  N    . THR   C 1 50 ? 27.462  -6.302  24.410  1.00 35.04 ? 50  THR   C N    1 
ATOM   1844 C  CA   . THR   C 1 50 ? 26.403  -6.659  25.346  1.00 32.11 ? 50  THR   C CA   1 
ATOM   1845 C  C    . THR   C 1 50 ? 25.289  -5.618  25.321  1.00 37.37 ? 50  THR   C C    1 
ATOM   1846 O  O    . THR   C 1 50 ? 25.487  -4.466  24.921  1.00 36.23 ? 50  THR   C O    1 
ATOM   1847 C  CB   . THR   C 1 50 ? 26.927  -6.803  26.785  1.00 36.84 ? 50  THR   C CB   1 
ATOM   1848 O  OG1  . THR   C 1 50 ? 27.570  -5.588  27.182  1.00 43.48 ? 50  THR   C OG1  1 
ATOM   1849 C  CG2  . THR   C 1 50 ? 27.927  -7.954  26.885  1.00 35.90 ? 50  THR   C CG2  1 
ATOM   1850 N  N    . ALA   C 1 51 ? 24.113  -6.040  25.777  1.00 30.66 ? 51  ALA   C N    1 
ATOM   1851 C  CA   . ALA   C 1 51 ? 22.942  -5.175  25.852  1.00 31.49 ? 51  ALA   C CA   1 
ATOM   1852 C  C    . ALA   C 1 51 ? 21.911  -5.849  26.750  1.00 36.94 ? 51  ALA   C C    1 
ATOM   1853 O  O    . ALA   C 1 51 ? 22.090  -6.987  27.185  1.00 38.77 ? 51  ALA   C O    1 
ATOM   1854 C  CB   . ALA   C 1 51 ? 22.358  -4.895  24.465  1.00 31.77 ? 51  ALA   C CB   1 
ATOM   1855 N  N    . PHE   C 1 52 ? 20.828  -5.132  27.028  1.00 33.14 ? 52  PHE   C N    1 
ATOM   1856 C  CA   . PHE   C 1 52 ? 19.701  -5.680  27.774  1.00 36.18 ? 52  PHE   C CA   1 
ATOM   1857 C  C    . PHE   C 1 52 ? 18.506  -5.804  26.844  1.00 36.92 ? 52  PHE   C C    1 
ATOM   1858 O  O    . PHE   C 1 52 ? 18.195  -4.863  26.105  1.00 33.82 ? 52  PHE   C O    1 
ATOM   1859 C  CB   . PHE   C 1 52 ? 19.339  -4.805  28.974  1.00 34.97 ? 52  PHE   C CB   1 
ATOM   1860 C  CG   . PHE   C 1 52 ? 20.386  -4.794  30.049  1.00 42.80 ? 52  PHE   C CG   1 
ATOM   1861 C  CD1  . PHE   C 1 52 ? 20.730  -5.965  30.712  1.00 38.74 ? 52  PHE   C CD1  1 
ATOM   1862 C  CD2  . PHE   C 1 52 ? 21.012  -3.610  30.416  1.00 45.71 ? 52  PHE   C CD2  1 
ATOM   1863 C  CE1  . PHE   C 1 52 ? 21.696  -5.963  31.710  1.00 47.82 ? 52  PHE   C CE1  1 
ATOM   1864 C  CE2  . PHE   C 1 52 ? 21.971  -3.600  31.417  1.00 49.15 ? 52  PHE   C CE2  1 
ATOM   1865 C  CZ   . PHE   C 1 52 ? 22.317  -4.786  32.060  1.00 47.66 ? 52  PHE   C CZ   1 
ATOM   1866 N  N    . LEU   C 1 53 ? 17.839  -6.957  26.876  1.00 29.93 ? 53  LEU   C N    1 
ATOM   1867 C  CA   . LEU   C 1 53 ? 16.709  -7.192  25.986  1.00 29.62 ? 53  LEU   C CA   1 
ATOM   1868 C  C    . LEU   C 1 53 ? 15.575  -7.887  26.715  1.00 30.44 ? 53  LEU   C C    1 
ATOM   1869 O  O    . LEU   C 1 53 ? 15.799  -8.731  27.586  1.00 32.48 ? 53  LEU   C O    1 
ATOM   1870 C  CB   . LEU   C 1 53 ? 17.106  -8.031  24.767  1.00 31.64 ? 53  LEU   C CB   1 
ATOM   1871 C  CG   . LEU   C 1 53 ? 17.796  -7.267  23.646  1.00 43.73 ? 53  LEU   C CG   1 
ATOM   1872 C  CD1  . LEU   C 1 53 ? 18.249  -8.226  22.580  1.00 36.27 ? 53  LEU   C CD1  1 
ATOM   1873 C  CD2  . LEU   C 1 53 ? 16.819  -6.249  23.064  1.00 38.82 ? 53  LEU   C CD2  1 
ATOM   1874 N  N    . GLY   C 1 54 ? 14.352  -7.533  26.332  1.00 34.01 ? 54  GLY   C N    1 
ATOM   1875 C  CA   . GLY   C 1 54 ? 13.172  -8.173  26.853  1.00 38.94 ? 54  GLY   C CA   1 
ATOM   1876 C  C    . GLY   C 1 54 ? 12.826  -9.421  26.070  1.00 34.18 ? 54  GLY   C C    1 
ATOM   1877 O  O    . GLY   C 1 54 ? 13.314  -9.627  24.957  1.00 30.30 ? 54  GLY   C O    1 
ATOM   1878 N  N    . PRO   C 1 55 ? 11.948  -10.263 26.628  1.00 37.32 ? 55  PRO   C N    1 
ATOM   1879 C  CA   . PRO   C 1 55 ? 11.669  -11.566 25.994  1.00 34.42 ? 55  PRO   C CA   1 
ATOM   1880 C  C    . PRO   C 1 55 ? 11.049  -11.453 24.614  1.00 33.87 ? 55  PRO   C C    1 
ATOM   1881 O  O    . PRO   C 1 55 ? 11.243  -12.352 23.785  1.00 37.32 ? 55  PRO   C O    1 
ATOM   1882 C  CB   . PRO   C 1 55 ? 10.711  -12.250 26.981  1.00 39.40 ? 55  PRO   C CB   1 
ATOM   1883 C  CG   . PRO   C 1 55 ? 10.607  -11.359 28.154  1.00 40.22 ? 55  PRO   C CG   1 
ATOM   1884 C  CD   . PRO   C 1 55 ? 11.112  -10.013 27.811  1.00 36.66 ? 55  PRO   C CD   1 
ATOM   1885 N  N    . LYS   C 1 56 ? 10.331  -10.363 24.328  1.00 34.88 ? 56  LYS   C N    1 
ATOM   1886 C  CA   . LYS   C 1 56 ? 9.747   -10.179 23.002  1.00 40.47 ? 56  LYS   C CA   1 
ATOM   1887 C  C    . LYS   C 1 56 ? 10.804  -10.131 21.901  1.00 37.75 ? 56  LYS   C C    1 
ATOM   1888 O  O    . LYS   C 1 56 ? 10.484  -10.401 20.739  1.00 35.42 ? 56  LYS   C O    1 
ATOM   1889 C  CB   . LYS   C 1 56 ? 8.907   -8.899  22.966  1.00 38.31 ? 56  LYS   C CB   1 
ATOM   1890 N  N    . ASP   C 1 57 ? 12.050  -9.801  22.236  1.00 33.18 ? 57  ASP   C N    1 
ATOM   1891 C  CA   . ASP   C 1 57 ? 13.118  -9.708  21.250  1.00 35.88 ? 57  ASP   C CA   1 
ATOM   1892 C  C    . ASP   C 1 57 ? 14.078  -10.891 21.303  1.00 32.45 ? 57  ASP   C C    1 
ATOM   1893 O  O    . ASP   C 1 57 ? 15.156  -10.812 20.719  1.00 27.75 ? 57  ASP   C O    1 
ATOM   1894 C  CB   . ASP   C 1 57 ? 13.908  -8.409  21.433  1.00 32.43 ? 57  ASP   C CB   1 
ATOM   1895 C  CG   . ASP   C 1 57 ? 13.055  -7.169  21.211  1.00 45.23 ? 57  ASP   C CG   1 
ATOM   1896 O  OD1  . ASP   C 1 57 ? 12.325  -7.129  20.193  1.00 39.22 ? 57  ASP   C OD1  1 
ATOM   1897 O  OD2  . ASP   C 1 57 ? 13.101  -6.249  22.060  1.00 41.30 ? 57  ASP   C OD2  1 
ATOM   1898 N  N    . LEU   C 1 58 ? 13.722  -11.977 21.981  1.00 28.55 ? 58  LEU   C N    1 
ATOM   1899 C  CA   . LEU   C 1 58 ? 14.612  -13.127 22.110  1.00 30.05 ? 58  LEU   C CA   1 
ATOM   1900 C  C    . LEU   C 1 58 ? 13.941  -14.380 21.557  1.00 30.23 ? 58  LEU   C C    1 
ATOM   1901 O  O    . LEU   C 1 58 ? 12.776  -14.655 21.861  1.00 36.99 ? 58  LEU   C O    1 
ATOM   1902 C  CB   . LEU   C 1 58 ? 15.018  -13.344 23.570  1.00 29.34 ? 58  LEU   C CB   1 
ATOM   1903 C  CG   . LEU   C 1 58 ? 15.671  -12.150 24.272  1.00 28.42 ? 58  LEU   C CG   1 
ATOM   1904 C  CD1  . LEU   C 1 58 ? 15.785  -12.388 25.787  1.00 30.38 ? 58  LEU   C CD1  1 
ATOM   1905 C  CD2  . LEU   C 1 58 ? 17.024  -11.842 23.689  1.00 26.62 ? 58  LEU   C CD2  1 
ATOM   1906 N  N    . PHE   C 1 59 ? 14.698  -15.157 20.782  1.00 29.85 ? 59  PHE   C N    1 
ATOM   1907 C  CA   . PHE   C 1 59 ? 14.181  -16.330 20.078  1.00 33.83 ? 59  PHE   C CA   1 
ATOM   1908 C  C    . PHE   C 1 59 ? 15.067  -17.537 20.374  1.00 33.01 ? 59  PHE   C C    1 
ATOM   1909 O  O    . PHE   C 1 59 ? 16.283  -17.487 20.094  1.00 32.05 ? 59  PHE   C O    1 
ATOM   1910 C  CB   . PHE   C 1 59 ? 14.118  -16.045 18.574  1.00 35.62 ? 59  PHE   C CB   1 
ATOM   1911 C  CG   . PHE   C 1 59 ? 13.280  -14.852 18.232  1.00 35.51 ? 59  PHE   C CG   1 
ATOM   1912 C  CD1  . PHE   C 1 59 ? 13.786  -13.568 18.361  1.00 31.42 ? 59  PHE   C CD1  1 
ATOM   1913 C  CD2  . PHE   C 1 59 ? 11.974  -15.011 17.808  1.00 37.77 ? 59  PHE   C CD2  1 
ATOM   1914 C  CE1  . PHE   C 1 59 ? 13.005  -12.473 18.062  1.00 33.72 ? 59  PHE   C CE1  1 
ATOM   1915 C  CE2  . PHE   C 1 59 ? 11.187  -13.914 17.512  1.00 35.28 ? 59  PHE   C CE2  1 
ATOM   1916 C  CZ   . PHE   C 1 59 ? 11.707  -12.644 17.634  1.00 38.16 ? 59  PHE   C CZ   1 
ATOM   1917 N  N    . PRO   C 1 60 ? 14.519  -18.627 20.924  1.00 36.35 ? 60  PRO   C N    1 
ATOM   1918 C  CA   . PRO   C 1 60 ? 15.352  -19.789 21.269  1.00 38.08 ? 60  PRO   C CA   1 
ATOM   1919 C  C    . PRO   C 1 60 ? 16.168  -20.244 20.072  1.00 38.37 ? 60  PRO   C C    1 
ATOM   1920 O  O    . PRO   C 1 60 ? 15.656  -20.347 18.957  1.00 41.79 ? 60  PRO   C O    1 
ATOM   1921 C  CB   . PRO   C 1 60 ? 14.330  -20.857 21.687  1.00 42.48 ? 60  PRO   C CB   1 
ATOM   1922 C  CG   . PRO   C 1 60 ? 13.077  -20.103 22.015  1.00 42.56 ? 60  PRO   C CG   1 
ATOM   1923 C  CD   . PRO   C 1 60 ? 13.084  -18.892 21.120  1.00 39.01 ? 60  PRO   C CD   1 
ATOM   1924 N  N    . TYR   C 1 61 ? 17.454  -20.510 20.307  1.00 42.20 ? 61  TYR   C N    1 
ATOM   1925 C  CA   . TYR   C 1 61 ? 18.360  -20.802 19.201  1.00 36.59 ? 61  TYR   C CA   1 
ATOM   1926 C  C    . TYR   C 1 61 ? 17.902  -22.025 18.418  1.00 42.94 ? 61  TYR   C C    1 
ATOM   1927 O  O    . TYR   C 1 61 ? 17.721  -21.961 17.200  1.00 42.84 ? 61  TYR   C O    1 
ATOM   1928 C  CB   . TYR   C 1 61 ? 19.779  -21.015 19.720  1.00 41.82 ? 61  TYR   C CB   1 
ATOM   1929 C  CG   . TYR   C 1 61 ? 20.748  -21.426 18.639  1.00 39.92 ? 61  TYR   C CG   1 
ATOM   1930 C  CD1  . TYR   C 1 61 ? 20.943  -20.630 17.521  1.00 38.52 ? 61  TYR   C CD1  1 
ATOM   1931 C  CD2  . TYR   C 1 61 ? 21.427  -22.636 18.709  1.00 44.91 ? 61  TYR   C CD2  1 
ATOM   1932 C  CE1  . TYR   C 1 61 ? 21.821  -21.005 16.529  1.00 43.89 ? 61  TYR   C CE1  1 
ATOM   1933 C  CE2  . TYR   C 1 61 ? 22.307  -23.019 17.722  1.00 44.07 ? 61  TYR   C CE2  1 
ATOM   1934 C  CZ   . TYR   C 1 61 ? 22.497  -22.201 16.632  1.00 38.40 ? 61  TYR   C CZ   1 
ATOM   1935 O  OH   . TYR   C 1 61 ? 23.370  -22.581 15.644  1.00 41.25 ? 61  TYR   C OH   1 
ATOM   1936 N  N    . ASP   C 1 62 ? 17.717  -23.159 19.100  1.00 43.42 ? 62  ASP   C N    1 
ATOM   1937 C  CA   . ASP   C 1 62 ? 17.450  -24.399 18.373  1.00 47.61 ? 62  ASP   C CA   1 
ATOM   1938 C  C    . ASP   C 1 62 ? 16.109  -24.372 17.656  1.00 48.60 ? 62  ASP   C C    1 
ATOM   1939 O  O    . ASP   C 1 62 ? 15.943  -25.054 16.637  1.00 52.39 ? 62  ASP   C O    1 
ATOM   1940 C  CB   . ASP   C 1 62 ? 17.514  -25.607 19.317  1.00 52.12 ? 62  ASP   C CB   1 
ATOM   1941 C  CG   . ASP   C 1 62 ? 18.723  -25.564 20.238  1.00 67.60 ? 62  ASP   C CG   1 
ATOM   1942 O  OD1  . ASP   C 1 62 ? 18.634  -24.944 21.324  1.00 71.50 ? 62  ASP   C OD1  1 
ATOM   1943 O  OD2  . ASP   C 1 62 ? 19.767  -26.148 19.866  1.00 65.46 ? 62  ASP   C OD2  1 
ATOM   1944 N  N    . LYS   C 1 63 ? 15.135  -23.628 18.180  1.00 48.20 ? 63  LYS   C N    1 
ATOM   1945 C  CA   . LYS   C 1 63 ? 13.843  -23.544 17.510  1.00 49.31 ? 63  LYS   C CA   1 
ATOM   1946 C  C    . LYS   C 1 63 ? 13.947  -22.747 16.221  1.00 50.52 ? 63  LYS   C C    1 
ATOM   1947 O  O    . LYS   C 1 63 ? 13.348  -23.113 15.201  1.00 49.23 ? 63  LYS   C O    1 
ATOM   1948 C  CB   . LYS   C 1 63 ? 12.810  -22.902 18.435  1.00 56.48 ? 63  LYS   C CB   1 
ATOM   1949 C  CG   . LYS   C 1 63 ? 11.395  -22.835 17.865  1.00 60.09 ? 63  LYS   C CG   1 
ATOM   1950 C  CD   . LYS   C 1 63 ? 10.389  -22.494 18.963  1.00 69.58 ? 63  LYS   C CD   1 
ATOM   1951 C  CE   . LYS   C 1 63 ? 9.256   -21.618 18.436  1.00 67.51 ? 63  LYS   C CE   1 
ATOM   1952 N  NZ   . LYS   C 1 63 ? 8.922   -20.512 19.382  1.00 70.37 ? 63  LYS   C NZ   1 
ATOM   1953 N  N    . CYS   C 1 64 ? 14.725  -21.664 16.241  1.00 42.33 ? 64  CYS   C N    1 
ATOM   1954 C  CA   . CYS   C 1 64 ? 14.665  -20.651 15.204  1.00 42.30 ? 64  CYS   C CA   1 
ATOM   1955 C  C    . CYS   C 1 64 ? 15.892  -20.648 14.292  1.00 42.51 ? 64  CYS   C C    1 
ATOM   1956 O  O    . CYS   C 1 64 ? 15.985  -19.791 13.413  1.00 37.11 ? 64  CYS   C O    1 
ATOM   1957 C  CB   . CYS   C 1 64 ? 14.470  -19.276 15.861  1.00 37.06 ? 64  CYS   C CB   1 
ATOM   1958 S  SG   . CYS   C 1 64 ? 12.960  -19.199 16.919  1.00 40.23 ? 64  CYS   C SG   1 
ATOM   1959 N  N    . LYS   C 1 65 ? 16.817  -21.603 14.446  1.00 41.69 ? 65  LYS   C N    1 
ATOM   1960 C  CA   . LYS   C 1 65 ? 18.052  -21.529 13.666  1.00 41.59 ? 65  LYS   C CA   1 
ATOM   1961 C  C    . LYS   C 1 65 ? 17.794  -21.720 12.181  1.00 44.93 ? 65  LYS   C C    1 
ATOM   1962 O  O    . LYS   C 1 65 ? 18.502  -21.135 11.358  1.00 38.40 ? 65  LYS   C O    1 
ATOM   1963 C  CB   . LYS   C 1 65 ? 19.095  -22.547 14.154  1.00 42.66 ? 65  LYS   C CB   1 
ATOM   1964 C  CG   . LYS   C 1 65 ? 18.588  -23.957 14.300  1.00 44.21 ? 65  LYS   C CG   1 
ATOM   1965 C  CD   . LYS   C 1 65 ? 19.697  -25.004 14.564  1.00 64.09 ? 65  LYS   C CD   1 
ATOM   1966 C  CE   . LYS   C 1 65 ? 20.870  -24.923 13.584  1.00 65.40 ? 65  LYS   C CE   1 
ATOM   1967 N  NZ   . LYS   C 1 65 ? 22.109  -25.594 14.106  1.00 57.47 ? 65  LYS   C NZ   1 
ATOM   1968 N  N    . ASP   C 1 66 ? 16.800  -22.522 11.801  1.00 43.85 ? 66  ASP   C N    1 
ATOM   1969 C  CA   . ASP   C 1 66 ? 16.550  -22.612 10.368  1.00 46.19 ? 66  ASP   C CA   1 
ATOM   1970 C  C    . ASP   C 1 66 ? 15.937  -21.331 9.797   1.00 51.16 ? 66  ASP   C C    1 
ATOM   1971 O  O    . ASP   C 1 66 ? 16.033  -21.113 8.585   1.00 47.86 ? 66  ASP   C O    1 
ATOM   1972 C  CB   . ASP   C 1 66 ? 15.743  -23.882 10.029  1.00 51.34 ? 66  ASP   C CB   1 
ATOM   1973 C  CG   . ASP   C 1 66 ? 14.263  -23.786 10.352  1.00 58.63 ? 66  ASP   C CG   1 
ATOM   1974 O  OD1  . ASP   C 1 66 ? 13.603  -22.776 10.036  1.00 67.47 ? 66  ASP   C OD1  1 
ATOM   1975 O  OD2  . ASP   C 1 66 ? 13.736  -24.804 10.852  1.00 57.19 ? 66  ASP   C OD2  1 
ATOM   1976 N  N    . LYS   C 1 67 ? 15.376  -20.451 10.633  1.00 42.34 ? 67  LYS   C N    1 
ATOM   1977 C  CA   . LYS   C 1 67 ? 14.912  -19.164 10.121  1.00 41.25 ? 67  LYS   C CA   1 
ATOM   1978 C  C    . LYS   C 1 67 ? 15.993  -18.083 10.203  1.00 37.35 ? 67  LYS   C C    1 
ATOM   1979 O  O    . LYS   C 1 67 ? 16.222  -17.351 9.236   1.00 37.33 ? 67  LYS   C O    1 
ATOM   1980 C  CB   . LYS   C 1 67 ? 13.658  -18.706 10.874  1.00 41.77 ? 67  LYS   C CB   1 
ATOM   1981 N  N    . TYR   C 1 68 ? 16.674  -17.966 11.337  1.00 34.63 ? 68  TYR   C N    1 
ATOM   1982 C  CA   . TYR   C 1 68 ? 17.586  -16.847 11.533  1.00 31.51 ? 68  TYR   C CA   1 
ATOM   1983 C  C    . TYR   C 1 68 ? 19.048  -17.218 11.352  1.00 31.47 ? 68  TYR   C C    1 
ATOM   1984 O  O    . TYR   C 1 68 ? 19.876  -16.319 11.149  1.00 28.77 ? 68  TYR   C O    1 
ATOM   1985 C  CB   . TYR   C 1 68 ? 17.378  -16.251 12.929  1.00 29.60 ? 68  TYR   C CB   1 
ATOM   1986 C  CG   . TYR   C 1 68 ? 15.979  -15.704 13.123  1.00 30.65 ? 68  TYR   C CG   1 
ATOM   1987 C  CD1  . TYR   C 1 68 ? 15.382  -14.907 12.148  1.00 35.74 ? 68  TYR   C CD1  1 
ATOM   1988 C  CD2  . TYR   C 1 68 ? 15.239  -16.027 14.246  1.00 33.45 ? 68  TYR   C CD2  1 
ATOM   1989 C  CE1  . TYR   C 1 68 ? 14.097  -14.410 12.318  1.00 34.05 ? 68  TYR   C CE1  1 
ATOM   1990 C  CE2  . TYR   C 1 68 ? 13.950  -15.551 14.421  1.00 32.56 ? 68  TYR   C CE2  1 
ATOM   1991 C  CZ   . TYR   C 1 68 ? 13.386  -14.748 13.454  1.00 42.11 ? 68  TYR   C CZ   1 
ATOM   1992 O  OH   . TYR   C 1 68 ? 12.107  -14.274 13.625  1.00 38.88 ? 68  TYR   C OH   1 
ATOM   1993 N  N    . GLY   C 1 69 ? 19.383  -18.508 11.421  1.00 26.98 ? 69  GLY   C N    1 
ATOM   1994 C  CA   . GLY   C 1 69 ? 20.762  -18.944 11.293  1.00 32.33 ? 69  GLY   C CA   1 
ATOM   1995 C  C    . GLY   C 1 69 ? 21.203  -19.055 9.849   1.00 30.67 ? 69  GLY   C C    1 
ATOM   1996 O  O    . GLY   C 1 69 ? 21.314  -20.167 9.314   1.00 30.78 ? 69  GLY   C O    1 
ATOM   1997 N  N    . LYS   C 1 70 ? 21.425  -17.912 9.199   1.00 24.55 ? 70  LYS   C N    1 
ATOM   1998 C  CA   . LYS   C 1 70 ? 21.901  -17.848 7.825   1.00 25.90 ? 70  LYS   C CA   1 
ATOM   1999 C  C    . LYS   C 1 70 ? 22.875  -16.683 7.728   1.00 30.32 ? 70  LYS   C C    1 
ATOM   2000 O  O    . LYS   C 1 70 ? 22.794  -15.745 8.526   1.00 27.15 ? 70  LYS   C O    1 
ATOM   2001 C  CB   . LYS   C 1 70 ? 20.758  -17.651 6.815   1.00 29.15 ? 70  LYS   C CB   1 
ATOM   2002 C  CG   . LYS   C 1 70 ? 19.538  -16.927 7.388   1.00 34.55 ? 70  LYS   C CG   1 
ATOM   2003 C  CD   . LYS   C 1 70 ? 18.638  -16.407 6.280   1.00 41.12 ? 70  LYS   C CD   1 
ATOM   2004 C  CE   . LYS   C 1 70 ? 17.916  -15.121 6.701   1.00 43.30 ? 70  LYS   C CE   1 
ATOM   2005 N  NZ   . LYS   C 1 70 ? 17.086  -14.566 5.579   1.00 50.78 ? 70  LYS   C NZ   1 
ATOM   2006 N  N    . PRO   C 1 71 ? 23.809  -16.721 6.777   1.00 27.08 ? 71  PRO   C N    1 
ATOM   2007 C  CA   . PRO   C 1 71 ? 24.827  -15.666 6.719   1.00 23.83 ? 71  PRO   C CA   1 
ATOM   2008 C  C    . PRO   C 1 71 ? 24.208  -14.306 6.453   1.00 32.98 ? 71  PRO   C C    1 
ATOM   2009 O  O    . PRO   C 1 71 ? 23.082  -14.189 5.973   1.00 28.92 ? 71  PRO   C O    1 
ATOM   2010 C  CB   . PRO   C 1 71 ? 25.733  -16.098 5.560   1.00 24.66 ? 71  PRO   C CB   1 
ATOM   2011 C  CG   . PRO   C 1 71 ? 25.547  -17.567 5.463   1.00 29.55 ? 71  PRO   C CG   1 
ATOM   2012 C  CD   . PRO   C 1 71 ? 24.090  -17.813 5.835   1.00 24.20 ? 71  PRO   C CD   1 
ATOM   2013 N  N    . ASN   C 1 72 ? 24.985  -13.269 6.749   1.00 26.22 ? 72  ASN   C N    1 
ATOM   2014 C  CA   . ASN   C 1 72 ? 24.496  -11.900 6.706   1.00 29.54 ? 72  ASN   C CA   1 
ATOM   2015 C  C    . ASN   C 1 72 ? 25.704  -10.997 6.506   1.00 29.98 ? 72  ASN   C C    1 
ATOM   2016 O  O    . ASN   C 1 72 ? 26.809  -11.305 6.967   1.00 29.51 ? 72  ASN   C O    1 
ATOM   2017 C  CB   . ASN   C 1 72 ? 23.732  -11.565 7.996   1.00 28.85 ? 72  ASN   C CB   1 
ATOM   2018 C  CG   . ASN   C 1 72 ? 23.010  -10.257 7.929   1.00 34.09 ? 72  ASN   C CG   1 
ATOM   2019 O  OD1  . ASN   C 1 72 ? 23.628  -9.202  7.806   1.00 32.69 ? 72  ASN   C OD1  1 
ATOM   2020 N  ND2  . ASN   C 1 72 ? 21.682  -10.307 8.018   1.00 34.90 ? 72  ASN   C ND2  1 
ATOM   2021 N  N    . LYS   C 1 73 ? 25.504  -9.909  5.770   1.00 30.06 ? 73  LYS   C N    1 
ATOM   2022 C  CA   . LYS   C 1 73 ? 26.640  -9.064  5.426   1.00 31.92 ? 73  LYS   C CA   1 
ATOM   2023 C  C    . LYS   C 1 73 ? 27.106  -8.188  6.578   1.00 31.95 ? 73  LYS   C C    1 
ATOM   2024 O  O    . LYS   C 1 73 ? 28.187  -7.600  6.481   1.00 36.28 ? 73  LYS   C O    1 
ATOM   2025 C  CB   . LYS   C 1 73 ? 26.305  -8.199  4.209   1.00 31.78 ? 73  LYS   C CB   1 
ATOM   2026 C  CG   . LYS   C 1 73 ? 25.678  -8.987  3.063   1.00 40.21 ? 73  LYS   C CG   1 
ATOM   2027 N  N    . ARG   C 1 74 ? 26.347  -8.108  7.665   1.00 31.50 ? 74  ARG   C N    1 
ATOM   2028 C  CA   . ARG   C 1 74 ? 26.705  -7.183  8.732   1.00 33.50 ? 74  ARG   C CA   1 
ATOM   2029 C  C    . ARG   C 1 74 ? 27.991  -7.632  9.418   1.00 34.54 ? 74  ARG   C C    1 
ATOM   2030 O  O    . ARG   C 1 74 ? 28.244  -8.829  9.568   1.00 25.81 ? 74  ARG   C O    1 
ATOM   2031 C  CB   . ARG   C 1 74 ? 25.574  -7.067  9.754   1.00 30.37 ? 74  ARG   C CB   1 
ATOM   2032 C  CG   . ARG   C 1 74 ? 24.215  -6.665  9.173   1.00 31.76 ? 74  ARG   C CG   1 
ATOM   2033 C  CD   . ARG   C 1 74 ? 24.210  -5.263  8.621   1.00 38.64 ? 74  ARG   C CD   1 
ATOM   2034 N  NE   . ARG   C 1 74 ? 24.265  -4.338  9.734   1.00 37.87 ? 74  ARG   C NE   1 
ATOM   2035 C  CZ   . ARG   C 1 74 ? 23.211  -3.791  10.318  1.00 39.95 ? 74  ARG   C CZ   1 
ATOM   2036 N  NH1  . ARG   C 1 74 ? 21.985  -3.970  9.852   1.00 37.07 ? 74  ARG   C NH1  1 
ATOM   2037 N  NH2  . ARG   C 1 74 ? 23.392  -3.057  11.404  1.00 41.07 ? 74  ARG   C NH2  1 
ATOM   2038 N  N    . LYS   C 1 75 ? 28.802  -6.651  9.823   1.00 35.25 ? 75  LYS   C N    1 
ATOM   2039 C  CA   . LYS   C 1 75 ? 30.099  -6.909  10.445  1.00 36.46 ? 75  LYS   C CA   1 
ATOM   2040 C  C    . LYS   C 1 75 ? 29.972  -7.836  11.638  1.00 28.97 ? 75  LYS   C C    1 
ATOM   2041 O  O    . LYS   C 1 75 ? 29.205  -7.573  12.567  1.00 31.72 ? 75  LYS   C O    1 
ATOM   2042 C  CB   . LYS   C 1 75 ? 30.735  -5.583  10.888  1.00 34.46 ? 75  LYS   C CB   1 
ATOM   2043 C  CG   . LYS   C 1 75 ? 32.250  -5.611  11.034  1.00 37.47 ? 75  LYS   C CG   1 
ATOM   2044 N  N    . GLY   C 1 76 ? 30.763  -8.908  11.631  1.00 27.74 ? 76  GLY   C N    1 
ATOM   2045 C  CA   . GLY   C 1 76 ? 30.818  -9.785  12.775  1.00 27.33 ? 76  GLY   C CA   1 
ATOM   2046 C  C    . GLY   C 1 76 ? 29.719  -10.814 12.821  1.00 26.84 ? 76  GLY   C C    1 
ATOM   2047 O  O    . GLY   C 1 76 ? 29.770  -11.715 13.665  1.00 28.05 ? 76  GLY   C O    1 
ATOM   2048 N  N    . PHE   C 1 77 ? 28.735  -10.730 11.926  1.00 25.54 ? 77  PHE   C N    1 
ATOM   2049 C  CA   . PHE   C 1 77 ? 27.615  -11.662 11.992  1.00 23.05 ? 77  PHE   C CA   1 
ATOM   2050 C  C    . PHE   C 1 77 ? 28.070  -13.091 11.746  1.00 26.29 ? 77  PHE   C C    1 
ATOM   2051 O  O    . PHE   C 1 77 ? 27.704  -14.004 12.489  1.00 21.36 ? 77  PHE   C O    1 
ATOM   2052 C  CB   . PHE   C 1 77 ? 26.533  -11.274 10.986  1.00 25.25 ? 77  PHE   C CB   1 
ATOM   2053 C  CG   . PHE   C 1 77 ? 25.230  -11.991 11.213  1.00 23.62 ? 77  PHE   C CG   1 
ATOM   2054 C  CD1  . PHE   C 1 77 ? 25.021  -13.246 10.684  1.00 22.38 ? 77  PHE   C CD1  1 
ATOM   2055 C  CD2  . PHE   C 1 77 ? 24.210  -11.405 11.960  1.00 28.56 ? 77  PHE   C CD2  1 
ATOM   2056 C  CE1  . PHE   C 1 77 ? 23.817  -13.926 10.895  1.00 25.91 ? 77  PHE   C CE1  1 
ATOM   2057 C  CE2  . PHE   C 1 77 ? 22.990  -12.090 12.182  1.00 24.68 ? 77  PHE   C CE2  1 
ATOM   2058 C  CZ   . PHE   C 1 77 ? 22.792  -13.332 11.645  1.00 21.07 ? 77  PHE   C CZ   1 
ATOM   2059 N  N    . ASN   C 1 78 ? 28.858  -13.315 10.695  1.00 23.99 ? 78  ASN   C N    1 
ATOM   2060 C  CA   . ASN   C 1 78 ? 29.126  -14.702 10.327  1.00 26.82 ? 78  ASN   C CA   1 
ATOM   2061 C  C    . ASN   C 1 78 ? 30.128  -15.368 11.267  1.00 27.30 ? 78  ASN   C C    1 
ATOM   2062 O  O    . ASN   C 1 78 ? 30.058  -16.581 11.470  1.00 24.65 ? 78  ASN   C O    1 
ATOM   2063 C  CB   . ASN   C 1 78 ? 29.595  -14.767 8.876   1.00 27.02 ? 78  ASN   C CB   1 
ATOM   2064 C  CG   . ASN   C 1 78 ? 28.522  -14.307 7.921   1.00 30.05 ? 78  ASN   C CG   1 
ATOM   2065 O  OD1  . ASN   C 1 78 ? 27.339  -14.499 8.190   1.00 23.31 ? 78  ASN   C OD1  1 
ATOM   2066 N  ND2  . ASN   C 1 78 ? 28.923  -13.666 6.810   1.00 23.86 ? 78  ASN   C ND2  1 
ATOM   2067 N  N    . GLU   C 1 79 ? 31.069  -14.610 11.838  1.00 27.03 ? 79  GLU   C N    1 
ATOM   2068 C  CA   . GLU   C 1 79 ? 31.862  -15.176 12.928  1.00 25.08 ? 79  GLU   C CA   1 
ATOM   2069 C  C    . GLU   C 1 79 ? 30.961  -15.553 14.100  1.00 28.16 ? 79  GLU   C C    1 
ATOM   2070 O  O    . GLU   C 1 79 ? 31.189  -16.570 14.772  1.00 24.93 ? 79  GLU   C O    1 
ATOM   2071 C  CB   . GLU   C 1 79 ? 32.949  -14.183 13.354  1.00 26.44 ? 79  GLU   C CB   1 
ATOM   2072 C  CG   . GLU   C 1 79 ? 33.694  -14.548 14.639  1.00 28.73 ? 79  GLU   C CG   1 
ATOM   2073 C  CD   . GLU   C 1 79 ? 35.116  -14.011 14.670  1.00 35.11 ? 79  GLU   C CD   1 
ATOM   2074 O  OE1  . GLU   C 1 79 ? 35.362  -12.948 14.065  1.00 34.57 ? 79  GLU   C OE1  1 
ATOM   2075 O  OE2  . GLU   C 1 79 ? 35.981  -14.620 15.336  1.00 35.72 ? 79  GLU   C OE2  1 
ATOM   2076 N  N    . GLY   C 1 80 ? 29.924  -14.744 14.350  1.00 24.99 ? 80  GLY   C N    1 
ATOM   2077 C  CA   . GLY   C 1 80 ? 28.969  -15.063 15.398  1.00 23.67 ? 80  GLY   C CA   1 
ATOM   2078 C  C    . GLY   C 1 80 ? 28.200  -16.342 15.125  1.00 27.64 ? 80  GLY   C C    1 
ATOM   2079 O  O    . GLY   C 1 80 ? 27.923  -17.118 16.046  1.00 28.45 ? 80  GLY   C O    1 
ATOM   2080 N  N    . LEU   C 1 81 ? 27.844  -16.587 13.856  1.00 25.24 ? 81  LEU   C N    1 
ATOM   2081 C  CA   . LEU   C 1 81 ? 27.222  -17.867 13.532  1.00 26.94 ? 81  LEU   C CA   1 
ATOM   2082 C  C    . LEU   C 1 81 ? 28.179  -19.013 13.820  1.00 24.82 ? 81  LEU   C C    1 
ATOM   2083 O  O    . LEU   C 1 81 ? 27.759  -20.069 14.301  1.00 29.68 ? 81  LEU   C O    1 
ATOM   2084 C  CB   . LEU   C 1 81 ? 26.769  -17.918 12.071  1.00 24.39 ? 81  LEU   C CB   1 
ATOM   2085 C  CG   . LEU   C 1 81 ? 25.623  -16.999 11.636  1.00 22.53 ? 81  LEU   C CG   1 
ATOM   2086 C  CD1  . LEU   C 1 81 ? 25.345  -17.190 10.160  1.00 25.55 ? 81  LEU   C CD1  1 
ATOM   2087 C  CD2  . LEU   C 1 81 ? 24.366  -17.265 12.434  1.00 20.58 ? 81  LEU   C CD2  1 
ATOM   2088 N  N    . TRP   C 1 82 ? 29.469  -18.831 13.525  1.00 22.12 ? 82  TRP   C N    1 
ATOM   2089 C  CA   . TRP   C 1 82 ? 30.418  -19.900 13.819  1.00 32.30 ? 82  TRP   C CA   1 
ATOM   2090 C  C    . TRP   C 1 82 ? 30.528  -20.133 15.322  1.00 29.92 ? 82  TRP   C C    1 
ATOM   2091 O  O    . TRP   C 1 82 ? 30.642  -21.278 15.762  1.00 28.24 ? 82  TRP   C O    1 
ATOM   2092 C  CB   . TRP   C 1 82 ? 31.793  -19.588 13.222  1.00 26.90 ? 82  TRP   C CB   1 
ATOM   2093 C  CG   . TRP   C 1 82 ? 32.780  -20.720 13.325  1.00 30.26 ? 82  TRP   C CG   1 
ATOM   2094 C  CD1  . TRP   C 1 82 ? 33.007  -21.712 12.409  1.00 29.68 ? 82  TRP   C CD1  1 
ATOM   2095 C  CD2  . TRP   C 1 82 ? 33.666  -20.972 14.413  1.00 31.25 ? 82  TRP   C CD2  1 
ATOM   2096 N  NE1  . TRP   C 1 82 ? 33.990  -22.562 12.866  1.00 33.82 ? 82  TRP   C NE1  1 
ATOM   2097 C  CE2  . TRP   C 1 82 ? 34.407  -22.129 14.095  1.00 34.05 ? 82  TRP   C CE2  1 
ATOM   2098 C  CE3  . TRP   C 1 82 ? 33.900  -20.333 15.635  1.00 35.12 ? 82  TRP   C CE3  1 
ATOM   2099 C  CZ2  . TRP   C 1 82 ? 35.360  -22.652 14.949  1.00 41.69 ? 82  TRP   C CZ2  1 
ATOM   2100 C  CZ3  . TRP   C 1 82 ? 34.844  -20.856 16.482  1.00 36.36 ? 82  TRP   C CZ3  1 
ATOM   2101 C  CH2  . TRP   C 1 82 ? 35.566  -22.000 16.138  1.00 39.08 ? 82  TRP   C CH2  1 
ATOM   2102 N  N    . GLU   C 1 83 ? 30.479  -19.066 16.129  1.00 28.09 ? 83  GLU   C N    1 
ATOM   2103 C  CA   . GLU   C 1 83 ? 30.658  -19.246 17.570  1.00 28.79 ? 83  GLU   C CA   1 
ATOM   2104 C  C    . GLU   C 1 83 ? 29.466  -19.957 18.197  1.00 31.67 ? 83  GLU   C C    1 
ATOM   2105 O  O    . GLU   C 1 83 ? 29.637  -20.812 19.075  1.00 35.00 ? 83  GLU   C O    1 
ATOM   2106 C  CB   . GLU   C 1 83 ? 30.877  -17.898 18.255  1.00 28.66 ? 83  GLU   C CB   1 
ATOM   2107 C  CG   . GLU   C 1 83 ? 32.240  -17.308 18.016  1.00 30.28 ? 83  GLU   C CG   1 
ATOM   2108 C  CD   . GLU   C 1 83 ? 32.346  -15.855 18.456  1.00 34.70 ? 83  GLU   C CD   1 
ATOM   2109 O  OE1  . GLU   C 1 83 ? 31.334  -15.283 18.959  1.00 29.61 ? 83  GLU   C OE1  1 
ATOM   2110 O  OE2  . GLU   C 1 83 ? 33.461  -15.302 18.314  1.00 32.68 ? 83  GLU   C OE2  1 
ATOM   2111 N  N    . ILE   C 1 84 ? 28.252  -19.620 17.774  1.00 26.08 ? 84  ILE   C N    1 
ATOM   2112 C  CA   . ILE   C 1 84 ? 27.082  -20.200 18.431  1.00 29.25 ? 84  ILE   C CA   1 
ATOM   2113 C  C    . ILE   C 1 84 ? 26.924  -21.670 18.058  1.00 28.03 ? 84  ILE   C C    1 
ATOM   2114 O  O    . ILE   C 1 84 ? 26.383  -22.465 18.838  1.00 30.76 ? 84  ILE   C O    1 
ATOM   2115 C  CB   . ILE   C 1 84 ? 25.829  -19.364 18.095  1.00 31.30 ? 84  ILE   C CB   1 
ATOM   2116 C  CG1  . ILE   C 1 84 ? 24.647  -19.750 18.997  1.00 33.98 ? 84  ILE   C CG1  1 
ATOM   2117 C  CG2  . ILE   C 1 84 ? 25.484  -19.465 16.615  1.00 28.44 ? 84  ILE   C CG2  1 
ATOM   2118 C  CD1  . ILE   C 1 84 ? 23.598  -18.608 19.195  1.00 29.81 ? 84  ILE   C CD1  1 
ATOM   2119 N  N    . GLN   C 1 85 ? 27.433  -22.074 16.898  1.00 28.06 ? 85  GLN   C N    1 
ATOM   2120 C  CA   . GLN   C 1 85 ? 27.334  -23.461 16.458  1.00 32.63 ? 85  GLN   C CA   1 
ATOM   2121 C  C    . GLN   C 1 85 ? 28.469  -24.327 16.984  1.00 37.26 ? 85  GLN   C C    1 
ATOM   2122 O  O    . GLN   C 1 85 ? 28.272  -25.523 17.245  1.00 37.18 ? 85  GLN   C O    1 
ATOM   2123 C  CB   . GLN   C 1 85 ? 27.348  -23.540 14.925  1.00 29.02 ? 85  GLN   C CB   1 
ATOM   2124 C  CG   . GLN   C 1 85 ? 27.131  -24.952 14.382  1.00 32.31 ? 85  GLN   C CG   1 
ATOM   2125 C  CD   . GLN   C 1 85 ? 26.711  -24.968 12.912  1.00 31.92 ? 85  GLN   C CD   1 
ATOM   2126 O  OE1  . GLN   C 1 85 ? 26.891  -23.987 12.193  1.00 35.18 ? 85  GLN   C OE1  1 
ATOM   2127 N  NE2  . GLN   C 1 85 ? 26.169  -26.093 12.462  1.00 32.31 ? 85  GLN   C NE2  1 
ATOM   2128 N  N    . ASN   C 1 86 ? 29.648  -23.746 17.154  1.00 32.64 ? 86  ASN   C N    1 
ATOM   2129 C  CA   . ASN   C 1 86 ? 30.852  -24.501 17.439  1.00 39.41 ? 86  ASN   C CA   1 
ATOM   2130 C  C    . ASN   C 1 86 ? 31.486  -24.178 18.784  1.00 38.94 ? 86  ASN   C C    1 
ATOM   2131 O  O    . ASN   C 1 86 ? 32.342  -24.939 19.241  1.00 42.99 ? 86  ASN   C O    1 
ATOM   2132 C  CB   . ASN   C 1 86 ? 31.869  -24.257 16.315  1.00 41.08 ? 86  ASN   C CB   1 
ATOM   2133 C  CG   . ASN   C 1 86 ? 31.304  -24.609 14.946  1.00 40.38 ? 86  ASN   C CG   1 
ATOM   2134 O  OD1  . ASN   C 1 86 ? 31.132  -23.746 14.072  1.00 35.90 ? 86  ASN   C OD1  1 
ATOM   2135 N  ND2  . ASN   C 1 86 ? 30.999  -25.878 14.757  1.00 37.33 ? 86  ASN   C ND2  1 
ATOM   2136 N  N    . ASN   C 1 87 ? 31.097  -23.098 19.438  1.00 41.26 ? 87  ASN   C N    1 
ATOM   2137 C  CA   . ASN   C 1 87 ? 31.776  -22.783 20.688  1.00 45.87 ? 87  ASN   C CA   1 
ATOM   2138 C  C    . ASN   C 1 87 ? 30.937  -21.789 21.480  1.00 44.13 ? 87  ASN   C C    1 
ATOM   2139 O  O    . ASN   C 1 87 ? 31.433  -20.718 21.845  1.00 48.66 ? 87  ASN   C O    1 
ATOM   2140 C  CB   . ASN   C 1 87 ? 33.167  -22.217 20.383  1.00 53.05 ? 87  ASN   C CB   1 
ATOM   2141 C  CG   . ASN   C 1 87 ? 34.105  -22.264 21.573  1.00 63.58 ? 87  ASN   C CG   1 
ATOM   2142 O  OD1  . ASN   C 1 87 ? 33.962  -23.101 22.467  1.00 62.99 ? 87  ASN   C OD1  1 
ATOM   2143 N  ND2  . ASN   C 1 87 ? 35.080  -21.356 21.587  1.00 64.77 ? 87  ASN   C ND2  1 
ATOM   2144 N  N    . PRO   C 1 88 ? 29.663  -22.096 21.759  1.00 42.55 ? 88  PRO   C N    1 
ATOM   2145 C  CA   . PRO   C 1 88 ? 28.767  -21.062 22.292  1.00 42.25 ? 88  PRO   C CA   1 
ATOM   2146 C  C    . PRO   C 1 88 ? 28.941  -20.788 23.775  1.00 49.46 ? 88  PRO   C C    1 
ATOM   2147 O  O    . PRO   C 1 88 ? 28.466  -19.749 24.248  1.00 46.56 ? 88  PRO   C O    1 
ATOM   2148 C  CB   . PRO   C 1 88 ? 27.373  -21.627 22.007  1.00 41.04 ? 88  PRO   C CB   1 
ATOM   2149 C  CG   . PRO   C 1 88 ? 27.557  -23.125 21.997  1.00 43.06 ? 88  PRO   C CG   1 
ATOM   2150 C  CD   . PRO   C 1 88 ? 29.005  -23.415 21.675  1.00 46.08 ? 88  PRO   C CD   1 
ATOM   2151 N  N    . HIS   C 1 89 ? 29.612  -21.665 24.522  1.00 52.53 ? 89  HIS   C N    1 
ATOM   2152 C  CA   . HIS   C 1 89 ? 29.715  -21.525 25.971  1.00 53.63 ? 89  HIS   C CA   1 
ATOM   2153 C  C    . HIS   C 1 89 ? 31.120  -21.136 26.425  1.00 56.55 ? 89  HIS   C C    1 
ATOM   2154 O  O    . HIS   C 1 89 ? 31.454  -21.304 27.599  1.00 61.05 ? 89  HIS   C O    1 
ATOM   2155 C  CB   . HIS   C 1 89 ? 29.264  -22.821 26.651  1.00 56.64 ? 89  HIS   C CB   1 
ATOM   2156 C  CG   . HIS   C 1 89 ? 27.861  -23.214 26.307  1.00 56.79 ? 89  HIS   C CG   1 
ATOM   2157 N  ND1  . HIS   C 1 89 ? 26.778  -22.391 26.541  1.00 63.09 ? 89  HIS   C ND1  1 
ATOM   2158 C  CD2  . HIS   C 1 89 ? 27.367  -24.327 25.712  1.00 58.24 ? 89  HIS   C CD2  1 
ATOM   2159 C  CE1  . HIS   C 1 89 ? 25.677  -22.986 26.118  1.00 64.91 ? 89  HIS   C CE1  1 
ATOM   2160 N  NE2  . HIS   C 1 89 ? 26.007  -24.160 25.605  1.00 61.66 ? 89  HIS   C NE2  1 
ATOM   2161 N  N    . ALA   C 1 90 ? 31.943  -20.608 25.523  1.00 54.58 ? 90  ALA   C N    1 
ATOM   2162 C  CA   . ALA   C 1 90 ? 33.304  -20.213 25.846  1.00 58.32 ? 90  ALA   C CA   1 
ATOM   2163 C  C    . ALA   C 1 90 ? 33.347  -18.775 26.343  1.00 63.49 ? 90  ALA   C C    1 
ATOM   2164 O  O    . ALA   C 1 90 ? 32.479  -17.964 26.026  1.00 67.63 ? 90  ALA   C O    1 
ATOM   2165 C  CB   . ALA   C 1 90 ? 34.213  -20.359 24.626  1.00 55.59 ? 90  ALA   C CB   1 
ATOM   2166 N  N    . SER   C 1 91 ? 34.376  -18.464 27.128  1.00 76.00 ? 91  SER   C N    1 
ATOM   2167 C  CA   . SER   C 1 91 ? 34.624  -17.093 27.554  1.00 77.89 ? 91  SER   C CA   1 
ATOM   2168 C  C    . SER   C 1 91 ? 35.243  -16.316 26.397  1.00 76.45 ? 91  SER   C C    1 
ATOM   2169 O  O    . SER   C 1 91 ? 36.289  -16.709 25.869  1.00 83.64 ? 91  SER   C O    1 
ATOM   2170 C  CB   . SER   C 1 91 ? 35.547  -17.070 28.772  1.00 86.03 ? 91  SER   C CB   1 
ATOM   2171 O  OG   . SER   C 1 91 ? 35.237  -18.111 29.684  1.00 87.48 ? 91  SER   C OG   1 
ATOM   2172 N  N    . TYR   C 1 92 ? 34.601  -15.223 25.998  1.00 73.36 ? 92  TYR   C N    1 
ATOM   2173 C  CA   . TYR   C 1 92 ? 35.124  -14.390 24.919  1.00 66.57 ? 92  TYR   C CA   1 
ATOM   2174 C  C    . TYR   C 1 92 ? 35.570  -13.036 25.439  1.00 72.35 ? 92  TYR   C C    1 
ATOM   2175 O  O    . TYR   C 1 92 ? 34.742  -12.228 25.854  1.00 79.01 ? 92  TYR   C O    1 
ATOM   2176 C  CB   . TYR   C 1 92 ? 34.079  -14.196 23.824  1.00 59.62 ? 92  TYR   C CB   1 
ATOM   2177 C  CG   . TYR   C 1 92 ? 33.765  -15.442 23.028  1.00 61.05 ? 92  TYR   C CG   1 
ATOM   2178 C  CD1  . TYR   C 1 92 ? 34.522  -15.788 21.911  1.00 56.87 ? 92  TYR   C CD1  1 
ATOM   2179 C  CD2  . TYR   C 1 92 ? 32.706  -16.267 23.384  1.00 57.00 ? 92  TYR   C CD2  1 
ATOM   2180 C  CE1  . TYR   C 1 92 ? 34.238  -16.925 21.181  1.00 53.02 ? 92  TYR   C CE1  1 
ATOM   2181 C  CE2  . TYR   C 1 92 ? 32.409  -17.402 22.658  1.00 51.74 ? 92  TYR   C CE2  1 
ATOM   2182 C  CZ   . TYR   C 1 92 ? 33.179  -17.730 21.560  1.00 54.52 ? 92  TYR   C CZ   1 
ATOM   2183 O  OH   . TYR   C 1 92 ? 32.888  -18.869 20.838  1.00 51.01 ? 92  TYR   C OH   1 
HETATM 2184 C  C01  . A1D73 D 2 .  ? 18.502  -3.709  6.389   0.59 32.15 ? 101 A1D73 A C01  1 
HETATM 2185 C  C02  . A1D73 D 2 .  ? 19.298  -3.936  7.494   0.59 35.96 ? 101 A1D73 A C02  1 
HETATM 2186 C  C04  . A1D73 D 2 .  ? 20.917  -4.945  6.175   0.59 32.63 ? 101 A1D73 A C04  1 
HETATM 2187 C  C05  . A1D73 D 2 .  ? 20.173  -4.752  5.025   0.59 37.55 ? 101 A1D73 A C05  1 
HETATM 2188 C  C06  . A1D73 D 2 .  ? 18.946  -4.107  5.136   0.59 35.56 ? 101 A1D73 A C06  1 
HETATM 2189 C  C07  . A1D73 D 2 .  ? 18.082  -3.902  3.899   0.59 31.79 ? 101 A1D73 A C07  1 
HETATM 2190 C  C08  . A1D73 D 2 .  ? 18.446  -3.443  2.669   0.59 26.38 ? 101 A1D73 A C08  1 
HETATM 2191 C  C09  . A1D73 D 2 .  ? 17.388  -3.449  1.823   0.59 21.23 ? 101 A1D73 A C09  1 
HETATM 2192 N  N03  . A1D73 D 2 .  ? 20.465  -4.540  7.348   0.59 46.57 ? 101 A1D73 A N03  1 
HETATM 2193 N  N10  . A1D73 D 2 .  ? 16.401  -3.893  2.556   0.59 25.71 ? 101 A1D73 A N10  1 
HETATM 2194 N  N11  . A1D73 D 2 .  ? 16.824  -4.183  3.805   0.59 23.73 ? 101 A1D73 A N11  1 
HETATM 2195 BR BR12 . A1D73 D 2 .  ? 20.151  -2.843  2.098   0.59 51.70 ? 101 A1D73 A BR12 1 
HETATM 2196 S  S    . SO4   E 3 .  ? 11.285  -10.919 -4.612  1.00 50.66 ? 102 SO4   A S    1 
HETATM 2197 O  O1   . SO4   E 3 .  ? 12.417  -11.667 -5.171  1.00 50.80 ? 102 SO4   A O1   1 
HETATM 2198 O  O2   . SO4   E 3 .  ? 10.111  -11.269 -5.416  1.00 49.99 ? 102 SO4   A O2   1 
HETATM 2199 O  O3   . SO4   E 3 .  ? 11.051  -11.255 -3.207  1.00 40.09 ? 102 SO4   A O3   1 
HETATM 2200 O  O4   . SO4   E 3 .  ? 11.583  -9.496  -4.727  1.00 36.49 ? 102 SO4   A O4   1 
HETATM 2201 S  S    . SO4   F 3 .  ? 30.029  -4.010  -1.148  1.00 70.36 ? 103 SO4   A S    1 
HETATM 2202 O  O1   . SO4   F 3 .  ? 30.407  -2.863  -1.983  1.00 61.10 ? 103 SO4   A O1   1 
HETATM 2203 O  O2   . SO4   F 3 .  ? 28.639  -4.352  -1.450  1.00 56.91 ? 103 SO4   A O2   1 
HETATM 2204 O  O3   . SO4   F 3 .  ? 30.856  -5.183  -1.440  1.00 63.77 ? 103 SO4   A O3   1 
HETATM 2205 O  O4   . SO4   F 3 .  ? 30.185  -3.647  0.262   1.00 47.26 ? 103 SO4   A O4   1 
HETATM 2206 C  C01  . A1D73 G 2 .  ? -0.033  5.078   23.630  0.61 33.95 ? 101 A1D73 B C01  1 
HETATM 2207 C  C02  . A1D73 G 2 .  ? -0.899  4.170   23.055  0.61 34.71 ? 101 A1D73 B C02  1 
HETATM 2208 C  C04  . A1D73 G 2 .  ? 0.602   2.448   23.409  0.61 37.60 ? 101 A1D73 B C04  1 
HETATM 2209 C  C05  . A1D73 G 2 .  ? 1.524   3.296   23.995  0.61 34.96 ? 101 A1D73 B C05  1 
HETATM 2210 C  C06  . A1D73 G 2 .  ? 1.192   4.637   24.120  0.61 35.25 ? 101 A1D73 B C06  1 
HETATM 2211 C  C07  . A1D73 G 2 .  ? 2.144   5.650   24.737  0.61 29.16 ? 101 A1D73 B C07  1 
HETATM 2212 C  C08  . A1D73 G 2 .  ? 3.081   5.505   25.741  0.61 25.45 ? 101 A1D73 B C08  1 
HETATM 2213 C  C09  . A1D73 G 2 .  ? 3.669   6.740   25.901  0.61 19.91 ? 101 A1D73 B C09  1 
HETATM 2214 N  N03  . A1D73 G 2 .  ? -0.556  2.899   22.965  0.61 34.65 ? 101 A1D73 B N03  1 
HETATM 2215 N  N10  . A1D73 G 2 .  ? 3.112   7.583   25.048  0.61 22.77 ? 101 A1D73 B N10  1 
HETATM 2216 N  N11  . A1D73 G 2 .  ? 2.182   6.894   24.340  0.61 29.36 ? 101 A1D73 B N11  1 
HETATM 2217 BR BR12 . A1D73 G 2 .  ? 3.584   3.950   26.800  0.61 31.73 ? 101 A1D73 B BR12 1 
HETATM 2218 S  S    . SO4   H 3 .  ? 6.330   -5.617  26.872  1.00 67.15 ? 102 SO4   B S    1 
HETATM 2219 O  O1   . SO4   H 3 .  ? 7.144   -6.120  25.759  1.00 60.99 ? 102 SO4   B O1   1 
HETATM 2220 O  O2   . SO4   H 3 .  ? 4.909   -5.599  26.500  1.00 46.95 ? 102 SO4   B O2   1 
HETATM 2221 O  O3   . SO4   H 3 .  ? 6.532   -6.480  28.040  1.00 72.92 ? 102 SO4   B O3   1 
HETATM 2222 O  O4   . SO4   H 3 .  ? 6.760   -4.263  27.226  1.00 51.10 ? 102 SO4   B O4   1 
HETATM 2223 S  S    . SO4   I 3 .  ? 13.066  12.512  24.645  1.00 68.07 ? 103 SO4   B S    1 
HETATM 2224 O  O1   . SO4   I 3 .  ? 14.503  12.758  24.808  1.00 61.32 ? 103 SO4   B O1   1 
HETATM 2225 O  O2   . SO4   I 3 .  ? 12.825  11.890  23.331  1.00 35.45 ? 103 SO4   B O2   1 
HETATM 2226 O  O3   . SO4   I 3 .  ? 12.667  11.613  25.722  1.00 55.84 ? 103 SO4   B O3   1 
HETATM 2227 O  O4   . SO4   I 3 .  ? 12.296  13.756  24.782  1.00 56.43 ? 103 SO4   B O4   1 
HETATM 2228 C  C01  . A1D73 J 2 .  ? 23.037  -3.578  18.311  1.00 32.89 ? 101 A1D73 C C01  1 
HETATM 2229 C  C02  . A1D73 J 2 .  ? 22.424  -2.437  18.817  1.00 38.46 ? 101 A1D73 C C02  1 
HETATM 2230 C  C04  . A1D73 J 2 .  ? 23.680  -2.575  20.754  1.00 39.69 ? 101 A1D73 C C04  1 
HETATM 2231 C  C05  . A1D73 J 2 .  ? 24.333  -3.718  20.315  1.00 36.64 ? 101 A1D73 C C05  1 
HETATM 2232 C  C06  . A1D73 J 2 .  ? 24.003  -4.230  19.068  1.00 34.00 ? 101 A1D73 C C06  1 
HETATM 2233 C  C07  . A1D73 J 2 .  ? 24.723  -5.476  18.552  1.00 27.80 ? 101 A1D73 C C07  1 
HETATM 2234 C  C08  . A1D73 J 2 .  ? 24.240  -6.539  17.835  1.00 27.17 ? 101 A1D73 C C08  1 
HETATM 2235 C  C09  . A1D73 J 2 .  ? 25.296  -7.394  17.595  1.00 25.85 ? 101 A1D73 C C09  1 
HETATM 2236 N  N03  . A1D73 J 2 .  ? 22.761  -1.978  20.015  1.00 35.98 ? 101 A1D73 C N03  1 
HETATM 2237 N  N10  . A1D73 J 2 .  ? 26.376  -6.849  18.149  1.00 27.57 ? 101 A1D73 C N10  1 
HETATM 2238 N  N11  . A1D73 J 2 .  ? 25.997  -5.681  18.715  1.00 30.80 ? 101 A1D73 C N11  1 
HETATM 2239 BR BR12 . A1D73 J 2 .  ? 22.427  -6.870  17.228  1.00 29.48 ? 101 A1D73 C BR12 1 
HETATM 2240 S  S    . SO4   K 3 .  ? 32.043  -11.805 9.671   1.00 31.60 ? 102 SO4   C S    1 
HETATM 2241 O  O1   . SO4   K 3 .  ? 32.996  -12.519 8.818   1.00 36.11 ? 102 SO4   C O1   1 
HETATM 2242 O  O2   . SO4   K 3 .  ? 30.669  -12.033 9.250   1.00 29.23 ? 102 SO4   C O2   1 
HETATM 2243 O  O3   . SO4   K 3 .  ? 32.172  -12.187 11.075  1.00 28.15 ? 102 SO4   C O3   1 
HETATM 2244 O  O4   . SO4   K 3 .  ? 32.331  -10.353 9.598   1.00 32.74 ? 102 SO4   C O4   1 
HETATM 2245 O  O    . HOH   L 4 .  ? 22.550  24.236  2.517   1.00 40.94 ? 201 HOH   A O    1 
HETATM 2246 O  O    . HOH   L 4 .  ? 22.467  -9.905  4.464   1.00 36.57 ? 202 HOH   A O    1 
HETATM 2247 O  O    . HOH   L 4 .  ? 11.220  -7.812  -6.232  1.00 30.01 ? 203 HOH   A O    1 
HETATM 2248 O  O    . HOH   L 4 .  ? 18.219  19.372  1.353   1.00 48.80 ? 204 HOH   A O    1 
HETATM 2249 O  O    . HOH   L 4 .  ? 21.421  0.937   -11.446 1.00 37.92 ? 205 HOH   A O    1 
HETATM 2250 O  O    . HOH   L 4 .  ? 16.550  17.309  3.387   1.00 34.07 ? 206 HOH   A O    1 
HETATM 2251 O  O    . HOH   L 4 .  ? 10.698  11.924  13.712  1.00 39.48 ? 207 HOH   A O    1 
HETATM 2252 O  O    . HOH   L 4 .  ? 19.276  3.396   18.972  1.00 33.41 ? 208 HOH   A O    1 
HETATM 2253 O  O    . HOH   L 4 .  ? 13.361  10.830  11.835  1.00 35.60 ? 209 HOH   A O    1 
HETATM 2254 O  O    . HOH   L 4 .  ? 8.861   9.073   -6.093  1.00 26.09 ? 210 HOH   A O    1 
HETATM 2255 O  O    . HOH   L 4 .  ? 11.774  3.261   10.996  1.00 33.92 ? 211 HOH   A O    1 
HETATM 2256 O  O    . HOH   L 4 .  ? 5.386   2.117   6.876   1.00 33.75 ? 212 HOH   A O    1 
HETATM 2257 O  O    . HOH   L 4 .  ? 26.120  1.455   5.566   1.00 31.40 ? 213 HOH   A O    1 
HETATM 2258 O  O    . HOH   L 4 .  ? 4.560   -3.375  -1.940  1.00 31.56 ? 214 HOH   A O    1 
HETATM 2259 O  O    . HOH   L 4 .  ? 16.097  13.277  -0.982  1.00 27.69 ? 215 HOH   A O    1 
HETATM 2260 O  O    . HOH   L 4 .  ? 9.534   15.942  7.592   1.00 30.79 ? 216 HOH   A O    1 
HETATM 2261 O  O    . HOH   L 4 .  ? 21.215  0.380   -7.069  1.00 26.52 ? 217 HOH   A O    1 
HETATM 2262 O  O    . HOH   L 4 .  ? 9.085   8.907   5.977   1.00 29.92 ? 218 HOH   A O    1 
HETATM 2263 O  O    . HOH   L 4 .  ? 8.292   -10.739 -7.360  1.00 29.75 ? 219 HOH   A O    1 
HETATM 2264 O  O    . HOH   L 4 .  ? 26.653  7.488   16.286  1.00 41.66 ? 220 HOH   A O    1 
HETATM 2265 O  O    . HOH   L 4 .  ? 15.965  19.780  6.181   1.00 37.83 ? 221 HOH   A O    1 
HETATM 2266 O  O    . HOH   L 4 .  ? 26.103  5.096   7.959   1.00 23.28 ? 222 HOH   A O    1 
HETATM 2267 O  O    . HOH   L 4 .  ? 0.456   5.700   -7.284  1.00 25.26 ? 223 HOH   A O    1 
HETATM 2268 O  O    . HOH   L 4 .  ? 24.867  -0.034  -6.206  1.00 33.90 ? 224 HOH   A O    1 
HETATM 2269 O  O    . HOH   L 4 .  ? 22.083  -0.866  0.327   1.00 19.64 ? 225 HOH   A O    1 
HETATM 2270 O  O    . HOH   L 4 .  ? 14.477  -7.653  -7.249  1.00 34.04 ? 226 HOH   A O    1 
HETATM 2271 O  O    . HOH   L 4 .  ? 17.308  -8.387  -0.031  1.00 30.94 ? 227 HOH   A O    1 
HETATM 2272 O  O    . HOH   L 4 .  ? 18.478  -3.544  -14.776 1.00 40.23 ? 228 HOH   A O    1 
HETATM 2273 O  O    . HOH   L 4 .  ? 24.979  -4.792  5.598   1.00 27.82 ? 229 HOH   A O    1 
HETATM 2274 O  O    . HOH   L 4 .  ? 26.831  9.247   11.273  1.00 36.09 ? 230 HOH   A O    1 
HETATM 2275 O  O    . HOH   L 4 .  ? 18.754  10.613  -11.786 1.00 31.66 ? 231 HOH   A O    1 
HETATM 2276 O  O    . HOH   L 4 .  ? 8.996   4.916   14.629  1.00 30.79 ? 232 HOH   A O    1 
HETATM 2277 O  O    . HOH   L 4 .  ? 3.365   8.330   -1.514  1.00 20.47 ? 233 HOH   A O    1 
HETATM 2278 O  O    . HOH   L 4 .  ? 12.424  3.210   15.699  1.00 35.02 ? 234 HOH   A O    1 
HETATM 2279 O  O    . HOH   L 4 .  ? 12.763  13.532  -1.166  1.00 26.20 ? 235 HOH   A O    1 
HETATM 2280 O  O    . HOH   L 4 .  ? 20.355  -1.329  -9.642  1.00 37.71 ? 236 HOH   A O    1 
HETATM 2281 O  O    . HOH   L 4 .  ? 7.752   9.385   -8.312  1.00 33.69 ? 237 HOH   A O    1 
HETATM 2282 O  O    . HOH   L 4 .  ? 7.316   9.252   4.247   1.00 20.60 ? 238 HOH   A O    1 
HETATM 2283 O  O    . HOH   L 4 .  ? 29.001  -0.290  1.278   1.00 28.22 ? 239 HOH   A O    1 
HETATM 2284 O  O    . HOH   L 4 .  ? 28.744  5.297   0.991   1.00 31.64 ? 240 HOH   A O    1 
HETATM 2285 O  O    . HOH   L 4 .  ? 10.916  1.050   18.464  1.00 44.20 ? 241 HOH   A O    1 
HETATM 2286 O  O    . HOH   L 4 .  ? 14.824  12.883  -4.181  1.00 29.32 ? 242 HOH   A O    1 
HETATM 2287 O  O    . HOH   L 4 .  ? 13.558  -3.871  10.388  1.00 33.99 ? 243 HOH   A O    1 
HETATM 2288 O  O    . HOH   L 4 .  ? 28.545  4.377   -1.684  1.00 35.61 ? 244 HOH   A O    1 
HETATM 2289 O  O    . HOH   L 4 .  ? 11.866  5.008   13.346  1.00 32.46 ? 245 HOH   A O    1 
HETATM 2290 O  O    . HOH   L 4 .  ? 28.642  1.573   3.451   1.00 43.60 ? 246 HOH   A O    1 
HETATM 2291 O  O    . HOH   L 4 .  ? 21.834  9.474   -11.575 1.00 35.18 ? 247 HOH   A O    1 
HETATM 2292 O  O    . HOH   L 4 .  ? 9.337   13.519  -0.375  1.00 24.89 ? 248 HOH   A O    1 
HETATM 2293 O  O    . HOH   L 4 .  ? -0.879  4.330   3.217   1.00 27.80 ? 249 HOH   A O    1 
HETATM 2294 O  O    . HOH   L 4 .  ? 27.839  9.634   8.057   1.00 25.32 ? 250 HOH   A O    1 
HETATM 2295 O  O    . HOH   L 4 .  ? -1.928  4.446   0.191   1.00 41.00 ? 251 HOH   A O    1 
HETATM 2296 O  O    . HOH   L 4 .  ? 10.135  8.296   -10.002 1.00 43.25 ? 252 HOH   A O    1 
HETATM 2297 O  O    . HOH   L 4 .  ? 30.073  -8.380  -1.370  1.00 47.21 ? 253 HOH   A O    1 
HETATM 2298 O  O    . HOH   L 4 .  ? 3.063   3.556   9.702   1.00 40.38 ? 254 HOH   A O    1 
HETATM 2299 O  O    . HOH   L 4 .  ? 27.970  6.885   9.170   1.00 30.32 ? 255 HOH   A O    1 
HETATM 2300 O  O    . HOH   L 4 .  ? 24.831  25.258  -2.665  1.00 45.73 ? 256 HOH   A O    1 
HETATM 2301 O  O    . HOH   L 4 .  ? 26.291  -2.787  7.113   1.00 38.72 ? 257 HOH   A O    1 
HETATM 2302 O  O    . HOH   L 4 .  ? 24.708  -5.724  -7.169  1.00 46.07 ? 258 HOH   A O    1 
HETATM 2303 O  O    . HOH   L 4 .  ? 29.641  2.098   -2.068  1.00 38.71 ? 259 HOH   A O    1 
HETATM 2304 O  O    . HOH   L 4 .  ? 26.537  4.878   16.219  1.00 43.60 ? 260 HOH   A O    1 
HETATM 2305 O  O    . HOH   L 4 .  ? 26.594  -2.462  -5.964  1.00 39.35 ? 261 HOH   A O    1 
HETATM 2306 O  O    . HOH   L 4 .  ? 31.994  7.443   2.708   1.00 30.32 ? 262 HOH   A O    1 
HETATM 2307 O  O    . HOH   L 4 .  ? 30.814  6.003   10.000  1.00 40.95 ? 263 HOH   A O    1 
HETATM 2308 O  O    . HOH   L 4 .  ? 12.174  13.037  -4.775  1.00 26.58 ? 264 HOH   A O    1 
HETATM 2309 O  O    . HOH   L 4 .  ? 10.909  11.435  -6.468  1.00 36.32 ? 265 HOH   A O    1 
HETATM 2310 O  O    . HOH   M 4 .  ? 14.659  13.702  31.683  1.00 37.04 ? 201 HOH   B O    1 
HETATM 2311 O  O    . HOH   M 4 .  ? 0.787   -1.098  23.468  1.00 36.52 ? 202 HOH   B O    1 
HETATM 2312 O  O    . HOH   M 4 .  ? 14.195  8.757   25.983  1.00 33.83 ? 203 HOH   B O    1 
HETATM 2313 O  O    . HOH   M 4 .  ? 13.127  12.931  20.990  1.00 40.79 ? 204 HOH   B O    1 
HETATM 2314 O  O    . HOH   M 4 .  ? 7.737   -1.014  46.079  1.00 44.89 ? 205 HOH   B O    1 
HETATM 2315 O  O    . HOH   M 4 .  ? 11.124  10.004  38.050  1.00 42.42 ? 206 HOH   B O    1 
HETATM 2316 O  O    . HOH   M 4 .  ? -9.576  1.258   40.445  1.00 27.53 ? 207 HOH   B O    1 
HETATM 2317 O  O    . HOH   M 4 .  ? -4.347  16.239  30.017  1.00 33.08 ? 208 HOH   B O    1 
HETATM 2318 O  O    . HOH   M 4 .  ? -5.333  -1.689  31.250  1.00 29.23 ? 209 HOH   B O    1 
HETATM 2319 O  O    . HOH   M 4 .  ? 8.461   -8.078  26.982  1.00 51.71 ? 210 HOH   B O    1 
HETATM 2320 O  O    . HOH   M 4 .  ? 10.263  2.427   32.909  1.00 23.52 ? 211 HOH   B O    1 
HETATM 2321 O  O    . HOH   M 4 .  ? -1.111  -2.853  26.515  1.00 45.28 ? 212 HOH   B O    1 
HETATM 2322 O  O    . HOH   M 4 .  ? 0.189   7.764   42.919  1.00 34.93 ? 213 HOH   B O    1 
HETATM 2323 O  O    . HOH   M 4 .  ? 3.970   1.892   28.955  1.00 21.39 ? 214 HOH   B O    1 
HETATM 2324 O  O    . HOH   M 4 .  ? 2.538   4.879   46.391  1.00 38.17 ? 215 HOH   B O    1 
HETATM 2325 O  O    . HOH   M 4 .  ? 0.748   -4.495  34.174  1.00 31.74 ? 216 HOH   B O    1 
HETATM 2326 O  O    . HOH   M 4 .  ? 6.228   -2.992  40.364  1.00 35.40 ? 217 HOH   B O    1 
HETATM 2327 O  O    . HOH   M 4 .  ? 2.541   -4.784  29.242  1.00 32.63 ? 218 HOH   B O    1 
HETATM 2328 O  O    . HOH   M 4 .  ? 6.690   14.827  41.137  1.00 36.71 ? 219 HOH   B O    1 
HETATM 2329 O  O    . HOH   M 4 .  ? -2.065  -1.870  28.837  1.00 32.66 ? 220 HOH   B O    1 
HETATM 2330 O  O    . HOH   M 4 .  ? 0.619   10.886  43.006  1.00 32.07 ? 221 HOH   B O    1 
HETATM 2331 O  O    . HOH   M 4 .  ? 2.682   20.607  38.561  1.00 25.95 ? 222 HOH   B O    1 
HETATM 2332 O  O    . HOH   M 4 .  ? -13.002 10.167  41.023  1.00 45.84 ? 223 HOH   B O    1 
HETATM 2333 O  O    . HOH   M 4 .  ? -7.254  12.669  29.073  1.00 45.60 ? 224 HOH   B O    1 
HETATM 2334 O  O    . HOH   M 4 .  ? 11.126  1.891   43.298  1.00 35.81 ? 225 HOH   B O    1 
HETATM 2335 O  O    . HOH   M 4 .  ? -0.336  24.908  32.974  1.00 29.50 ? 226 HOH   B O    1 
HETATM 2336 O  O    . HOH   M 4 .  ? -2.986  17.145  37.044  1.00 24.40 ? 227 HOH   B O    1 
HETATM 2337 O  O    . HOH   M 4 .  ? -4.217  14.541  42.859  1.00 44.55 ? 228 HOH   B O    1 
HETATM 2338 O  O    . HOH   M 4 .  ? 14.673  7.254   41.014  1.00 50.45 ? 229 HOH   B O    1 
HETATM 2339 O  O    . HOH   M 4 .  ? 4.040   -4.879  34.486  1.00 41.00 ? 230 HOH   B O    1 
HETATM 2340 O  O    . HOH   M 4 .  ? 12.843  2.607   31.508  1.00 37.66 ? 231 HOH   B O    1 
HETATM 2341 O  O    . HOH   M 4 .  ? -11.024 0.075   38.463  1.00 31.85 ? 232 HOH   B O    1 
HETATM 2342 O  O    . HOH   M 4 .  ? -9.691  13.061  30.013  1.00 43.82 ? 233 HOH   B O    1 
HETATM 2343 O  O    . HOH   M 4 .  ? -0.191  14.786  42.705  1.00 26.50 ? 234 HOH   B O    1 
HETATM 2344 O  O    . HOH   M 4 .  ? -7.116  -3.753  35.411  1.00 32.33 ? 235 HOH   B O    1 
HETATM 2345 O  O    . HOH   M 4 .  ? 8.100   15.059  16.596  1.00 42.15 ? 236 HOH   B O    1 
HETATM 2346 O  O    . HOH   M 4 .  ? -3.273  15.245  24.613  1.00 46.14 ? 237 HOH   B O    1 
HETATM 2347 O  O    . HOH   M 4 .  ? -4.351  13.028  23.048  1.00 49.01 ? 238 HOH   B O    1 
HETATM 2348 O  O    . HOH   M 4 .  ? 13.509  -1.791  24.244  1.00 43.49 ? 239 HOH   B O    1 
HETATM 2349 O  O    . HOH   M 4 .  ? 10.264  -0.502  32.769  1.00 35.83 ? 240 HOH   B O    1 
HETATM 2350 O  O    . HOH   M 4 .  ? 2.151   25.700  34.442  1.00 36.10 ? 241 HOH   B O    1 
HETATM 2351 O  O    . HOH   M 4 .  ? 4.225   -1.597  49.938  1.00 47.32 ? 242 HOH   B O    1 
HETATM 2352 O  O    . HOH   M 4 .  ? 3.659   23.344  29.889  1.00 50.14 ? 243 HOH   B O    1 
HETATM 2353 O  O    . HOH   M 4 .  ? -1.385  -2.494  24.213  1.00 44.04 ? 244 HOH   B O    1 
HETATM 2354 O  O    . HOH   M 4 .  ? -7.920  6.953   24.030  1.00 45.63 ? 245 HOH   B O    1 
HETATM 2355 O  O    . HOH   M 4 .  ? -17.262 19.014  35.070  1.00 61.23 ? 246 HOH   B O    1 
HETATM 2356 O  O    . HOH   M 4 .  ? 5.166   18.917  22.134  1.00 52.16 ? 247 HOH   B O    1 
HETATM 2357 O  O    . HOH   M 4 .  ? -7.314  -3.658  32.530  1.00 40.37 ? 248 HOH   B O    1 
HETATM 2358 O  O    . HOH   M 4 .  ? 14.582  0.574   25.096  1.00 42.89 ? 249 HOH   B O    1 
HETATM 2359 O  O    . HOH   M 4 .  ? -10.727 11.196  28.787  1.00 52.78 ? 250 HOH   B O    1 
HETATM 2360 O  O    . HOH   M 4 .  ? 3.510   11.640  44.027  1.00 32.79 ? 251 HOH   B O    1 
HETATM 2361 O  O    . HOH   M 4 .  ? 13.370  -0.326  29.959  1.00 37.62 ? 252 HOH   B O    1 
HETATM 2362 O  O    . HOH   N 4 .  ? 19.381  -0.793  17.657  1.00 33.52 ? 201 HOH   C O    1 
HETATM 2363 O  O    . HOH   N 4 .  ? 13.720  -4.964  15.428  1.00 33.00 ? 202 HOH   C O    1 
HETATM 2364 O  O    . HOH   N 4 .  ? 35.472  -16.301 17.447  1.00 37.73 ? 203 HOH   C O    1 
HETATM 2365 O  O    . HOH   N 4 .  ? 11.507  -8.569  18.293  1.00 46.23 ? 204 HOH   C O    1 
HETATM 2366 O  O    . HOH   N 4 .  ? 34.752  -11.103 7.628   1.00 37.17 ? 205 HOH   C O    1 
HETATM 2367 O  O    . HOH   N 4 .  ? 23.593  -21.373 13.384  1.00 40.77 ? 206 HOH   C O    1 
HETATM 2368 O  O    . HOH   N 4 .  ? 17.491  -21.267 23.946  1.00 39.78 ? 207 HOH   C O    1 
HETATM 2369 O  O    . HOH   N 4 .  ? 21.431  -22.210 30.369  1.00 57.38 ? 208 HOH   C O    1 
HETATM 2370 O  O    . HOH   N 4 .  ? 26.139  -21.207 12.631  1.00 33.45 ? 209 HOH   C O    1 
HETATM 2371 O  O    . HOH   N 4 .  ? 21.397  -0.298  11.999  1.00 30.23 ? 210 HOH   C O    1 
HETATM 2372 O  O    . HOH   N 4 .  ? 34.089  -11.092 12.477  1.00 32.90 ? 211 HOH   C O    1 
HETATM 2373 O  O    . HOH   N 4 .  ? 30.488  -18.770 10.100  1.00 27.11 ? 212 HOH   C O    1 
HETATM 2374 O  O    . HOH   N 4 .  ? 19.715  -7.866  16.318  1.00 21.65 ? 213 HOH   C O    1 
HETATM 2375 O  O    . HOH   N 4 .  ? 13.689  -5.529  24.527  1.00 36.36 ? 214 HOH   C O    1 
HETATM 2376 O  O    . HOH   N 4 .  ? 19.361  -13.730 11.162  1.00 19.35 ? 215 HOH   C O    1 
HETATM 2377 O  O    . HOH   N 4 .  ? 22.325  -22.274 10.703  1.00 38.09 ? 216 HOH   C O    1 
HETATM 2378 O  O    . HOH   N 4 .  ? 20.273  -22.793 24.926  1.00 45.62 ? 217 HOH   C O    1 
HETATM 2379 O  O    . HOH   N 4 .  ? 11.787  -2.272  31.444  1.00 40.44 ? 218 HOH   C O    1 
HETATM 2380 O  O    . HOH   N 4 .  ? 14.936  -3.227  12.650  1.00 33.25 ? 219 HOH   C O    1 
HETATM 2381 O  O    . HOH   N 4 .  ? 25.287  -24.970 19.384  1.00 33.32 ? 220 HOH   C O    1 
HETATM 2382 O  O    . HOH   N 4 .  ? 27.947  -5.165  13.288  1.00 41.78 ? 221 HOH   C O    1 
HETATM 2383 O  O    . HOH   N 4 .  ? 15.385  -24.387 13.699  1.00 41.40 ? 222 HOH   C O    1 
HETATM 2384 O  O    . HOH   N 4 .  ? 16.502  -10.600 10.803  1.00 28.27 ? 223 HOH   C O    1 
HETATM 2385 O  O    . HOH   N 4 .  ? 28.692  -3.710  24.299  1.00 43.64 ? 224 HOH   C O    1 
HETATM 2386 O  O    . HOH   N 4 .  ? 8.328   -17.799 31.706  1.00 43.42 ? 225 HOH   C O    1 
HETATM 2387 O  O    . HOH   N 4 .  ? 21.212  -2.348  26.356  1.00 38.72 ? 226 HOH   C O    1 
HETATM 2388 O  O    . HOH   N 4 .  ? 15.582  -2.661  20.004  1.00 38.57 ? 227 HOH   C O    1 
HETATM 2389 O  O    . HOH   N 4 .  ? 20.815  -13.381 8.626   1.00 27.42 ? 228 HOH   C O    1 
HETATM 2390 O  O    . HOH   N 4 .  ? 36.200  -21.388 29.408  1.00 42.59 ? 229 HOH   C O    1 
HETATM 2391 O  O    . HOH   N 4 .  ? 15.858  -5.365  10.581  1.00 42.44 ? 230 HOH   C O    1 
HETATM 2392 O  O    . HOH   N 4 .  ? 29.417  -21.663 10.881  1.00 30.77 ? 231 HOH   C O    1 
HETATM 2393 O  O    . HOH   N 4 .  ? 13.222  -2.548  19.309  1.00 43.80 ? 232 HOH   C O    1 
HETATM 2394 O  O    . HOH   N 4 .  ? 27.774  -3.108  11.274  1.00 40.10 ? 233 HOH   C O    1 
HETATM 2395 O  O    . HOH   N 4 .  ? 8.212   2.577   15.463  1.00 35.13 ? 234 HOH   C O    1 
HETATM 2396 O  O    . HOH   N 4 .  ? 17.324  -12.769 9.632   1.00 33.94 ? 235 HOH   C O    1 
HETATM 2397 O  O    . HOH   N 4 .  ? 21.140  1.549   17.446  1.00 35.92 ? 236 HOH   C O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . MET A 1  ? 0.8629 0.6190 1.1902 -0.0660 0.1717  0.0177  1  MET A N   
2    C CA  . MET A 1  ? 0.7879 0.5433 1.1030 -0.0419 0.1565  0.0373  1  MET A CA  
3    C C   . MET A 1  ? 0.7398 0.5329 1.0474 -0.0382 0.1402  0.0166  1  MET A C   
4    O O   . MET A 1  ? 0.9048 0.6998 1.2170 -0.0215 0.1306  0.0135  1  MET A O   
5    C CB  . MET A 1  ? 0.8381 0.5832 1.1204 -0.0304 0.1516  0.0854  1  MET A CB  
6    N N   . PRO A 2  ? 0.6582 0.4829 0.9541 -0.0529 0.1362  0.0028  2  PRO A N   
7    C CA  . PRO A 2  ? 0.5933 0.4567 0.8782 -0.0480 0.1186  -0.0158 2  PRO A CA  
8    C C   . PRO A 2  ? 0.4010 0.2793 0.7118 -0.0522 0.1183  -0.0580 2  PRO A C   
9    O O   . PRO A 2  ? 0.4724 0.3558 0.8043 -0.0663 0.1296  -0.0840 2  PRO A O   
10   C CB  . PRO A 2  ? 0.4943 0.3944 0.7587 -0.0606 0.1136  -0.0201 2  PRO A CB  
11   C CG  . PRO A 2  ? 0.5472 0.4228 0.8079 -0.0700 0.1283  0.0075  2  PRO A CG  
12   C CD  . PRO A 2  ? 0.6521 0.4861 0.9346 -0.0699 0.1433  0.0102  2  PRO A CD  
13   N N   . HIS A 3  ? 0.4594 0.3593 0.7574 -0.0366 0.1026  -0.0632 3  HIS A N   
14   C CA  . HIS A 3  ? 0.3908 0.3174 0.7041 -0.0395 0.0995  -0.1017 3  HIS A CA  
15   C C   . HIS A 3  ? 0.3101 0.2897 0.5950 -0.0413 0.0824  -0.1129 3  HIS A C   
16   O O   . HIS A 3  ? 0.3371 0.3281 0.5954 -0.0396 0.0740  -0.0931 3  HIS A O   
17   C CB  . HIS A 3  ? 0.5605 0.4753 0.8819 -0.0214 0.0964  -0.1002 3  HIS A CB  
18   C CG  . HIS A 3  ? 0.5354 0.4060 0.8827 -0.0152 0.1105  -0.0865 3  HIS A CG  
19   N ND1 . HIS A 3  ? 0.5145 0.3747 0.8673 0.0040  0.1066  -0.0763 3  HIS A ND1 
20   C CD2 . HIS A 3  ? 0.6316 0.4743 0.9955 -0.0248 0.1266  -0.0794 3  HIS A CD2 
21   C CE1 . HIS A 3  ? 0.5799 0.4051 0.9521 0.0066  0.1187  -0.0631 3  HIS A CE1 
22   N NE2 . HIS A 3  ? 0.6114 0.4237 0.9905 -0.0107 0.1317  -0.0641 3  HIS A NE2 
23   N N   . ALA A 4  ? 0.3009 0.3141 0.5918 -0.0441 0.0776  -0.1445 4  ALA A N   
24   C CA  . ALA A 4  ? 0.2921 0.3524 0.5535 -0.0413 0.0604  -0.1483 4  ALA A CA  
25   C C   . ALA A 4  ? 0.2575 0.3151 0.4881 -0.0242 0.0478  -0.1201 4  ALA A C   
26   O O   . ALA A 4  ? 0.3099 0.3409 0.5445 -0.0139 0.0505  -0.1057 4  ALA A O   
27   C CB  . ALA A 4  ? 0.3445 0.4456 0.6159 -0.0476 0.0585  -0.1857 4  ALA A CB  
28   N N   . PHE A 5  ? 0.2147 0.3010 0.4167 -0.0210 0.0343  -0.1127 5  PHE A N   
29   C CA  . PHE A 5  ? 0.2052 0.2913 0.3803 -0.0086 0.0241  -0.0908 5  PHE A CA  
30   C C   . PHE A 5  ? 0.2112 0.3092 0.3878 -0.0042 0.0228  -0.1030 5  PHE A C   
31   O O   . PHE A 5  ? 0.2140 0.3363 0.4011 -0.0107 0.0247  -0.1295 5  PHE A O   
32   C CB  . PHE A 5  ? 0.2089 0.3183 0.3581 -0.0069 0.0125  -0.0822 5  PHE A CB  
33   C CG  . PHE A 5  ? 0.1935 0.2910 0.3384 -0.0079 0.0133  -0.0667 5  PHE A CG  
34   C CD1 . PHE A 5  ? 0.1908 0.2675 0.3245 -0.0021 0.0136  -0.0439 5  PHE A CD1 
35   C CD2 . PHE A 5  ? 0.2060 0.3198 0.3596 -0.0154 0.0143  -0.0778 5  PHE A CD2 
36   C CE1 . PHE A 5  ? 0.2009 0.2725 0.3298 -0.0043 0.0156  -0.0321 5  PHE A CE1 
37   C CE2 . PHE A 5  ? 0.1528 0.2596 0.3042 -0.0173 0.0168  -0.0662 5  PHE A CE2 
38   C CZ  . PHE A 5  ? 0.1706 0.2558 0.3085 -0.0121 0.0178  -0.0432 5  PHE A CZ  
39   N N   . LYS A 6  ? 0.1466 0.2331 0.3143 0.0060  0.0202  -0.0862 6  LYS A N   
40   C CA  . LYS A 6  ? 0.2311 0.3308 0.4027 0.0102  0.0203  -0.0982 6  LYS A CA  
41   C C   . LYS A 6  ? 0.2035 0.3103 0.3501 0.0170  0.0123  -0.0793 6  LYS A C   
42   O O   . LYS A 6  ? 0.1740 0.2678 0.3074 0.0205  0.0085  -0.0574 6  LYS A O   
43   C CB  . LYS A 6  ? 0.2556 0.3310 0.4605 0.0162  0.0306  -0.1057 6  LYS A CB  
44   C CG  . LYS A 6  ? 0.3010 0.3480 0.5060 0.0288  0.0300  -0.0768 6  LYS A CG  
45   C CD  . LYS A 6  ? 0.3549 0.3765 0.5950 0.0391  0.0395  -0.0810 6  LYS A CD  
46   C CE  . LYS A 6  ? 0.3792 0.3795 0.6164 0.0547  0.0367  -0.0478 6  LYS A CE  
47   N NZ  . LYS A 6  ? 0.3898 0.3745 0.6098 0.0489  0.0367  -0.0243 6  LYS A NZ  
48   N N   . PRO A 7  ? 0.1973 0.3287 0.3363 0.0163  0.0107  -0.0896 7  PRO A N   
49   C CA  . PRO A 7  ? 0.1913 0.3301 0.3106 0.0195  0.0059  -0.0750 7  PRO A CA  
50   C C   . PRO A 7  ? 0.2456 0.3659 0.3729 0.0297  0.0055  -0.0590 7  PRO A C   
51   O O   . PRO A 7  ? 0.1813 0.2896 0.3334 0.0382  0.0099  -0.0626 7  PRO A O   
52   C CB  . PRO A 7  ? 0.1597 0.3262 0.2825 0.0170  0.0092  -0.0943 7  PRO A CB  
53   C CG  . PRO A 7  ? 0.2023 0.3861 0.3293 0.0091  0.0115  -0.1152 7  PRO A CG  
54   C CD  . PRO A 7  ? 0.2002 0.3589 0.3483 0.0100  0.0146  -0.1176 7  PRO A CD  
55   N N   . GLY A 8  ? 0.1857 0.3060 0.2930 0.0295  0.0004  -0.0417 8  GLY A N   
56   C CA  . GLY A 8  ? 0.1843 0.2984 0.2940 0.0381  -0.0018 -0.0266 8  GLY A CA  
57   C C   . GLY A 8  ? 0.2150 0.3095 0.3217 0.0396  -0.0024 -0.0106 8  GLY A C   
58   O O   . GLY A 8  ? 0.1520 0.2487 0.2533 0.0449  -0.0053 0.0036  8  GLY A O   
59   N N   . ASP A 9  ? 0.1917 0.2732 0.3020 0.0340  0.0008  -0.0143 9  ASP A N   
60   C CA  . ASP A 9  ? 0.2114 0.2779 0.3189 0.0328  0.0023  -0.0006 9  ASP A CA  
61   C C   . ASP A 9  ? 0.1588 0.2350 0.2444 0.0292  -0.0027 0.0075  9  ASP A C   
62   O O   . ASP A 9  ? 0.1459 0.2316 0.2207 0.0244  -0.0056 0.0007  9  ASP A O   
63   C CB  . ASP A 9  ? 0.1624 0.2202 0.2801 0.0246  0.0075  -0.0112 9  ASP A CB  
64   C CG  . ASP A 9  ? 0.2045 0.2443 0.3494 0.0258  0.0164  -0.0188 9  ASP A CG  
65   O OD1 . ASP A 9  ? 0.2309 0.2601 0.3872 0.0360  0.0182  -0.0113 9  ASP A OD1 
66   O OD2 . ASP A 9  ? 0.2177 0.2550 0.3756 0.0167  0.0221  -0.0338 9  ASP A OD2 
67   N N   . LEU A 10 ? 0.1409 0.2149 0.2208 0.0313  -0.0025 0.0221  10 LEU A N   
68   C CA  . LEU A 10 ? 0.1611 0.2464 0.2243 0.0271  -0.0055 0.0254  10 LEU A CA  
69   C C   . LEU A 10 ? 0.2200 0.2994 0.2817 0.0211  -0.0022 0.0256  10 LEU A C   
70   O O   . LEU A 10 ? 0.1530 0.2223 0.2223 0.0201  0.0032  0.0321  10 LEU A O   
71   C CB  . LEU A 10 ? 0.1751 0.2743 0.2316 0.0322  -0.0077 0.0372  10 LEU A CB  
72   C CG  . LEU A 10 ? 0.1617 0.2737 0.2236 0.0395  -0.0114 0.0350  10 LEU A CG  
73   C CD1 . LEU A 10 ? 0.1551 0.2915 0.2106 0.0455  -0.0157 0.0452  10 LEU A CD1 
74   C CD2 . LEU A 10 ? 0.1631 0.2827 0.2210 0.0324  -0.0123 0.0199  10 LEU A CD2 
75   N N   . VAL A 11 ? 0.1156 0.2007 0.1701 0.0170  -0.0042 0.0185  11 VAL A N   
76   C CA  . VAL A 11 ? 0.1553 0.2397 0.2129 0.0128  -0.0017 0.0146  11 VAL A CA  
77   C C   . VAL A 11 ? 0.2077 0.3000 0.2577 0.0114  -0.0027 0.0112  11 VAL A C   
78   O O   . VAL A 11 ? 0.1955 0.2904 0.2385 0.0117  -0.0047 0.0100  11 VAL A O   
79   C CB  . VAL A 11 ? 0.1605 0.2439 0.2271 0.0122  -0.0031 0.0042  11 VAL A CB  
80   C CG1 . VAL A 11 ? 0.1508 0.2272 0.2301 0.0115  0.0003  0.0010  11 VAL A CG1 
81   C CG2 . VAL A 11 ? 0.1739 0.2613 0.2322 0.0153  -0.0091 0.0008  11 VAL A CG2 
82   N N   . PHE A 12 ? 0.1673 0.2642 0.2221 0.0087  0.0003  0.0069  12 PHE A N   
83   C CA  . PHE A 12 ? 0.1798 0.2804 0.2363 0.0101  -0.0007 -0.0019 12 PHE A CA  
84   C C   . PHE A 12 ? 0.1491 0.2486 0.2148 0.0149  -0.0047 -0.0070 12 PHE A C   
85   O O   . PHE A 12 ? 0.1477 0.2530 0.2224 0.0126  -0.0034 -0.0102 12 PHE A O   
86   C CB  . PHE A 12 ? 0.1575 0.2717 0.2163 0.0056  0.0051  -0.0068 12 PHE A CB  
87   C CG  . PHE A 12 ? 0.2225 0.3481 0.2696 0.0012  0.0079  -0.0034 12 PHE A CG  
88   C CD1 . PHE A 12 ? 0.2103 0.3414 0.2555 0.0000  0.0081  -0.0131 12 PHE A CD1 
89   C CD2 . PHE A 12 ? 0.2226 0.3546 0.2619 -0.0015 0.0104  0.0097  12 PHE A CD2 
90   C CE1 . PHE A 12 ? 0.1976 0.3492 0.2328 -0.0051 0.0100  -0.0140 12 PHE A CE1 
91   C CE2 . PHE A 12 ? 0.2270 0.3785 0.2535 -0.0035 0.0109  0.0146  12 PHE A CE2 
92   C CZ  . PHE A 12 ? 0.2595 0.4250 0.2838 -0.0059 0.0101  0.0006  12 PHE A CZ  
93   N N   . ALA A 13 ? 0.1857 0.2795 0.2498 0.0211  -0.0091 -0.0075 13 ALA A N   
94   C CA  . ALA A 13 ? 0.1710 0.2696 0.2402 0.0284  -0.0152 -0.0087 13 ALA A CA  
95   C C   . ALA A 13 ? 0.1882 0.2880 0.2669 0.0373  -0.0169 -0.0120 13 ALA A C   
96   O O   . ALA A 13 ? 0.1961 0.2824 0.2741 0.0386  -0.0137 -0.0115 13 ALA A O   
97   C CB  . ALA A 13 ? 0.1434 0.2355 0.2007 0.0305  -0.0195 -0.0010 13 ALA A CB  
98   N N   . LYS A 14 ? 0.1766 0.2945 0.2676 0.0437  -0.0213 -0.0179 14 LYS A N   
99   C CA  . LYS A 14 ? 0.1281 0.2526 0.2345 0.0548  -0.0229 -0.0234 14 LYS A CA  
100  C C   . LYS A 14 ? 0.2319 0.3563 0.3377 0.0711  -0.0329 -0.0133 14 LYS A C   
101  O O   . LYS A 14 ? 0.2058 0.3515 0.3097 0.0744  -0.0405 -0.0123 14 LYS A O   
102  C CB  . LYS A 14 ? 0.1668 0.3189 0.2909 0.0515  -0.0205 -0.0383 14 LYS A CB  
103  C CG  . LYS A 14 ? 0.2126 0.3763 0.3574 0.0625  -0.0202 -0.0487 14 LYS A CG  
104  C CD  . LYS A 14 ? 0.1914 0.3349 0.3357 0.0609  -0.0123 -0.0511 14 LYS A CD  
105  C CE  . LYS A 14 ? 0.2071 0.3645 0.3769 0.0705  -0.0094 -0.0670 14 LYS A CE  
106  N NZ  . LYS A 14 ? 0.1752 0.3182 0.3562 0.0923  -0.0171 -0.0597 14 LYS A NZ  
107  N N   . MET A 15 ? 0.2240 0.3257 0.3321 0.0809  -0.0320 -0.0059 15 MET A N   
108  C CA  . MET A 15 ? 0.2206 0.3158 0.3298 0.0998  -0.0400 0.0091  15 MET A CA  
109  C C   . MET A 15 ? 0.2526 0.3510 0.3886 0.1159  -0.0404 0.0011  15 MET A C   
110  O O   . MET A 15 ? 0.2355 0.3258 0.3850 0.1100  -0.0308 -0.0139 15 MET A O   
111  C CB  . MET A 15 ? 0.3404 0.3976 0.4348 0.0978  -0.0350 0.0256  15 MET A CB  
112  C CG  . MET A 15 ? 0.4294 0.4824 0.4980 0.0871  -0.0353 0.0377  15 MET A CG  
113  S SD  . MET A 15 ? 0.3565 0.4446 0.4096 0.0910  -0.0472 0.0453  15 MET A SD  
114  C CE  . MET A 15 ? 0.3808 0.4521 0.4216 0.1085  -0.0522 0.0753  15 MET A CE  
115  N N   . LYS A 16 ? 0.2103 0.3212 0.3527 0.1326  -0.0498 0.0110  16 LYS A N   
116  C CA  . LYS A 16 ? 0.2614 0.3732 0.4294 0.1458  -0.0483 0.0055  16 LYS A CA  
117  C C   . LYS A 16 ? 0.3024 0.3721 0.4814 0.1538  -0.0389 0.0073  16 LYS A C   
118  O O   . LYS A 16 ? 0.2645 0.2996 0.4317 0.1580  -0.0388 0.0257  16 LYS A O   
119  C CB  . LYS A 16 ? 0.2470 0.3737 0.4176 0.1605  -0.0605 0.0211  16 LYS A CB  
120  C CG  . LYS A 16 ? 0.2724 0.3991 0.4724 0.1783  -0.0597 0.0199  16 LYS A CG  
121  C CD  . LYS A 16 ? 0.3092 0.4405 0.5102 0.1956  -0.0746 0.0420  16 LYS A CD  
122  C CE  . LYS A 16 ? 0.4747 0.5974 0.7104 0.2172  -0.0741 0.0464  16 LYS A CE  
123  N NZ  . LYS A 16 ? 0.4145 0.4830 0.6624 0.2228  -0.0621 0.0543  16 LYS A NZ  
124  N N   . GLY A 17 ? 0.2772 0.3484 0.4771 0.1522  -0.0297 -0.0144 17 GLY A N   
125  C CA  . GLY A 17 ? 0.2908 0.3230 0.5039 0.1549  -0.0185 -0.0203 17 GLY A CA  
126  C C   . GLY A 17 ? 0.3405 0.3542 0.5497 0.1338  -0.0080 -0.0322 17 GLY A C   
127  O O   . GLY A 17 ? 0.3585 0.3412 0.5808 0.1310  0.0038  -0.0408 17 GLY A O   
128  N N   . TYR A 18 ? 0.2920 0.3251 0.4761 0.1143  -0.0091 -0.0324 18 TYR A N   
129  C CA  . TYR A 18 ? 0.2793 0.3024 0.4470 0.0913  0.0005  -0.0388 18 TYR A CA  
130  C C   . TYR A 18 ? 0.3140 0.3724 0.4763 0.0757  0.0031  -0.0549 18 TYR A C   
131  O O   . TYR A 18 ? 0.2303 0.3151 0.3904 0.0772  -0.0034 -0.0533 18 TYR A O   
132  C CB  . TYR A 18 ? 0.2758 0.2840 0.4155 0.0841  -0.0032 -0.0171 18 TYR A CB  
133  C CG  . TYR A 18 ? 0.3406 0.3098 0.4790 0.0928  -0.0017 0.0020  18 TYR A CG  
134  C CD1 . TYR A 18 ? 0.4563 0.3932 0.6000 0.0824  0.0114  -0.0035 18 TYR A CD1 
135  C CD2 . TYR A 18 ? 0.3715 0.3384 0.5036 0.1105  -0.0123 0.0258  18 TYR A CD2 
136  C CE1 . TYR A 18 ? 0.4515 0.3474 0.5947 0.0880  0.0158  0.0162  18 TYR A CE1 
137  C CE2 . TYR A 18 ? 0.4374 0.3673 0.5652 0.1184  -0.0098 0.0487  18 TYR A CE2 
138  C CZ  . TYR A 18 ? 0.5400 0.4305 0.6739 0.1066  0.0053  0.0449  18 TYR A CZ  
139  O OH  . TYR A 18 ? 0.5444 0.3928 0.6746 0.1126  0.0105  0.0702  18 TYR A OH  
140  N N   . PRO A 19 ? 0.2797 0.3411 0.4394 0.0597  0.0133  -0.0699 19 PRO A N   
141  C CA  . PRO A 19 ? 0.2157 0.3089 0.3634 0.0447  0.0158  -0.0773 19 PRO A CA  
142  C C   . PRO A 19 ? 0.2192 0.3123 0.3429 0.0388  0.0091  -0.0583 19 PRO A C   
143  O O   . PRO A 19 ? 0.1632 0.2349 0.2766 0.0411  0.0051  -0.0444 19 PRO A O   
144  C CB  . PRO A 19 ? 0.2505 0.3474 0.3969 0.0308  0.0263  -0.0938 19 PRO A CB  
145  C CG  . PRO A 19 ? 0.3080 0.3693 0.4560 0.0325  0.0281  -0.0887 19 PRO A CG  
146  C CD  . PRO A 19 ? 0.3787 0.4150 0.5422 0.0527  0.0229  -0.0776 19 PRO A CD  
147  N N   . HIS A 20 ? 0.2093 0.3258 0.3260 0.0307  0.0095  -0.0583 20 HIS A N   
148  C CA  . HIS A 20 ? 0.1798 0.2943 0.2782 0.0247  0.0056  -0.0433 20 HIS A CA  
149  C C   . HIS A 20 ? 0.2456 0.3481 0.3295 0.0184  0.0068  -0.0380 20 HIS A C   
150  O O   . HIS A 20 ? 0.1810 0.2928 0.2628 0.0107  0.0128  -0.0473 20 HIS A O   
151  C CB  . HIS A 20 ? 0.2583 0.3937 0.3533 0.0148  0.0100  -0.0437 20 HIS A CB  
152  C CG  . HIS A 20 ? 0.1579 0.3097 0.2692 0.0173  0.0105  -0.0517 20 HIS A CG  
153  N ND1 . HIS A 20 ? 0.1883 0.3574 0.3166 0.0197  0.0151  -0.0680 20 HIS A ND1 
154  C CD2 . HIS A 20 ? 0.1825 0.3402 0.2991 0.0171  0.0076  -0.0493 20 HIS A CD2 
155  C CE1 . HIS A 20 ? 0.2353 0.4226 0.3783 0.0210  0.0145  -0.0741 20 HIS A CE1 
156  N NE2 . HIS A 20 ? 0.2266 0.4075 0.3627 0.0186  0.0101  -0.0635 20 HIS A NE2 
157  N N   . TRP A 21 ? 0.2122 0.2998 0.2869 0.0209  0.0015  -0.0257 21 TRP A N   
158  C CA  . TRP A 21 ? 0.1891 0.2643 0.2552 0.0163  0.0030  -0.0230 21 TRP A CA  
159  C C   . TRP A 21 ? 0.2010 0.2828 0.2537 0.0112  0.0005  -0.0143 21 TRP A C   
160  O O   . TRP A 21 ? 0.2348 0.3163 0.2852 0.0146  -0.0039 -0.0067 21 TRP A O   
161  C CB  . TRP A 21 ? 0.2178 0.2694 0.2858 0.0238  0.0008  -0.0155 21 TRP A CB  
162  C CG  . TRP A 21 ? 0.2068 0.2417 0.2740 0.0169  0.0074  -0.0182 21 TRP A CG  
163  C CD1 . TRP A 21 ? 0.1859 0.2206 0.2419 0.0078  0.0090  -0.0148 21 TRP A CD1 
164  C CD2 . TRP A 21 ? 0.2231 0.2394 0.3052 0.0174  0.0151  -0.0278 21 TRP A CD2 
165  N NE1 . TRP A 21 ? 0.2032 0.2217 0.2654 0.0000  0.0179  -0.0220 21 TRP A NE1 
166  C CE2 . TRP A 21 ? 0.2510 0.2550 0.3297 0.0056  0.0223  -0.0300 21 TRP A CE2 
167  C CE3 . TRP A 21 ? 0.2708 0.2804 0.3724 0.0264  0.0178  -0.0371 21 TRP A CE3 
168  C CZ2 . TRP A 21 ? 0.2874 0.2684 0.3819 0.0007  0.0334  -0.0414 21 TRP A CZ2 
169  C CZ3 . TRP A 21 ? 0.3202 0.3058 0.4385 0.0244  0.0281  -0.0479 21 TRP A CZ3 
170  C CH2 . TRP A 21 ? 0.3188 0.2881 0.4335 0.0108  0.0364  -0.0500 21 TRP A CH2 
171  N N   . PRO A 22 ? 0.1575 0.2486 0.2042 0.0039  0.0033  -0.0175 22 PRO A N   
172  C CA  . PRO A 22 ? 0.1622 0.2619 0.2002 0.0028  0.0001  -0.0090 22 PRO A CA  
173  C C   . PRO A 22 ? 0.1723 0.2585 0.2077 0.0051  -0.0027 -0.0030 22 PRO A C   
174  O O   . PRO A 22 ? 0.1347 0.2088 0.1695 0.0026  -0.0004 -0.0045 22 PRO A O   
175  C CB  . PRO A 22 ? 0.1729 0.2916 0.2075 -0.0045 0.0028  -0.0167 22 PRO A CB  
176  C CG  . PRO A 22 ? 0.1688 0.2780 0.2115 -0.0099 0.0092  -0.0312 22 PRO A CG  
177  C CD  . PRO A 22 ? 0.1651 0.2643 0.2155 -0.0035 0.0095  -0.0318 22 PRO A CD  
178  N N   . ALA A 23 ? 0.1359 0.2241 0.1705 0.0088  -0.0061 0.0033  23 ALA A N   
179  C CA  . ALA A 23 ? 0.1601 0.2422 0.1919 0.0102  -0.0082 0.0059  23 ALA A CA  
180  C C   . ALA A 23 ? 0.1361 0.2256 0.1710 0.0124  -0.0098 0.0071  23 ALA A C   
181  O O   . ALA A 23 ? 0.1408 0.2345 0.1804 0.0145  -0.0093 0.0097  23 ALA A O   
182  C CB  . ALA A 23 ? 0.1879 0.2628 0.2209 0.0150  -0.0110 0.0075  23 ALA A CB  
183  N N   . ARG A 24 ? 0.1370 0.2283 0.1700 0.0123  -0.0106 0.0055  24 ARG A N   
184  C CA  . ARG A 24 ? 0.1846 0.2822 0.2257 0.0150  -0.0106 0.0019  24 ARG A CA  
185  C C   . ARG A 24 ? 0.2114 0.3134 0.2522 0.0146  -0.0118 -0.0040 24 ARG A C   
186  O O   . ARG A 24 ? 0.1866 0.2901 0.2159 0.0128  -0.0133 -0.0011 24 ARG A O   
187  C CB  . ARG A 24 ? 0.1514 0.2602 0.1934 0.0145  -0.0095 -0.0003 24 ARG A CB  
188  C CG  . ARG A 24 ? 0.1929 0.3086 0.2259 0.0081  -0.0074 -0.0039 24 ARG A CG  
189  C CD  . ARG A 24 ? 0.1680 0.3009 0.2051 0.0058  -0.0052 -0.0090 24 ARG A CD  
190  N NE  . ARG A 24 ? 0.2282 0.3690 0.2566 -0.0036 -0.0005 -0.0125 24 ARG A NE  
191  C CZ  . ARG A 24 ? 0.2140 0.3709 0.2441 -0.0106 0.0038  -0.0182 24 ARG A CZ  
192  N NH1 . ARG A 24 ? 0.1775 0.3482 0.2175 -0.0080 0.0021  -0.0221 24 ARG A NH1 
193  N NH2 . ARG A 24 ? 0.2562 0.4196 0.2772 -0.0213 0.0102  -0.0201 24 ARG A NH2 
194  N N   . ILE A 25 ? 0.1636 0.2684 0.2177 0.0162  -0.0104 -0.0122 25 ILE A N   
195  C CA  . ILE A 25 ? 0.1543 0.2735 0.2098 0.0141  -0.0107 -0.0240 25 ILE A CA  
196  C C   . ILE A 25 ? 0.1592 0.2910 0.2094 0.0120  -0.0088 -0.0279 25 ILE A C   
197  O O   . ILE A 25 ? 0.1795 0.3113 0.2408 0.0147  -0.0060 -0.0312 25 ILE A O   
198  C CB  . ILE A 25 ? 0.1983 0.3167 0.2751 0.0139  -0.0070 -0.0373 25 ILE A CB  
199  C CG1 . ILE A 25 ? 0.1926 0.2971 0.2783 0.0135  -0.0055 -0.0332 25 ILE A CG1 
200  C CG2 . ILE A 25 ? 0.1871 0.3296 0.2650 0.0095  -0.0077 -0.0546 25 ILE A CG2 
201  C CD1 . ILE A 25 ? 0.2481 0.3609 0.3249 0.0124  -0.0102 -0.0312 25 ILE A CD1 
202  N N   . ASP A 26 ? 0.2758 0.4944 0.2232 0.0219  0.0238  0.0456  26 ASP A N   
203  C CA  . ASP A 26 ? 0.2731 0.5154 0.2301 0.0220  0.0240  0.0475  26 ASP A CA  
204  C C   . ASP A 26 ? 0.3053 0.5092 0.2653 0.0435  0.0361  0.0605  26 ASP A C   
205  O O   . ASP A 26 ? 0.2896 0.4401 0.2421 0.0479  0.0430  0.0574  26 ASP A O   
206  C CB  . ASP A 26 ? 0.2704 0.4940 0.2255 -0.0040 0.0222  0.0228  26 ASP A CB  
207  C CG  . ASP A 26 ? 0.2959 0.5800 0.2583 -0.0279 0.0199  0.0098  26 ASP A CG  
208  O OD1 . ASP A 26 ? 0.2750 0.6324 0.2422 -0.0260 0.0134  0.0186  26 ASP A OD1 
209  O OD2 . ASP A 26 ? 0.2835 0.5462 0.2473 -0.0496 0.0268  -0.0079 26 ASP A OD2 
210  N N   . ASP A 27 ? 0.2845 0.5210 0.2571 0.0540  0.0417  0.0715  27 ASP A N   
211  C CA  . ASP A 27 ? 0.3673 0.5616 0.3389 0.0664  0.0571  0.0726  27 ASP A CA  
212  C C   . ASP A 27 ? 0.3635 0.5257 0.3214 0.0446  0.0524  0.0506  27 ASP A C   
213  O O   . ASP A 27 ? 0.3646 0.5331 0.3195 0.0239  0.0417  0.0388  27 ASP A O   
214  C CB  . ASP A 27 ? 0.4414 0.6833 0.4343 0.0881  0.0689  0.0930  27 ASP A CB  
215  C CG  . ASP A 27 ? 0.5875 0.8148 0.5903 0.1251  0.0915  0.1209  27 ASP A CG  
216  O OD1 . ASP A 27 ? 0.6263 0.7799 0.6180 0.1301  0.1122  0.1121  27 ASP A OD1 
217  O OD2 . ASP A 27 ? 0.5833 0.8739 0.6045 0.1488  0.0919  0.1518  27 ASP A OD2 
218  N N   . ILE A 28 ? 0.3672 0.4928 0.3148 0.0502  0.0648  0.0462  28 ILE A N   
219  C CA  . ILE A 28 ? 0.3919 0.5000 0.3232 0.0356  0.0630  0.0343  28 ILE A CA  
220  C C   . ILE A 28 ? 0.3963 0.5247 0.3348 0.0432  0.0784  0.0400  28 ILE A C   
221  O O   . ILE A 28 ? 0.3690 0.4875 0.3112 0.0617  0.0968  0.0443  28 ILE A O   
222  C CB  . ILE A 28 ? 0.4089 0.4746 0.3163 0.0310  0.0629  0.0212  28 ILE A CB  
223  C CG1 . ILE A 28 ? 0.4624 0.5191 0.3708 0.0246  0.0490  0.0169  28 ILE A CG1 
224  C CG2 . ILE A 28 ? 0.3921 0.4534 0.2787 0.0212  0.0605  0.0176  28 ILE A CG2 
225  C CD1 . ILE A 28 ? 0.4951 0.5310 0.4058 0.0293  0.0580  0.0127  28 ILE A CD1 
226  N N   . ALA A 29 ? 0.3878 0.5430 0.3321 0.0291  0.0765  0.0401  29 ALA A N   
227  C CA  . ALA A 29 ? 0.3334 0.5160 0.2888 0.0345  0.0930  0.0454  29 ALA A CA  
228  C C   . ALA A 29 ? 0.3617 0.5026 0.2868 0.0354  0.1061  0.0379  29 ALA A C   
229  O O   . ALA A 29 ? 0.3703 0.4769 0.2667 0.0255  0.0973  0.0306  29 ALA A O   
230  C CB  . ALA A 29 ? 0.4282 0.6526 0.4000 0.0117  0.0916  0.0440  29 ALA A CB  
231  N N   . ASP A 30 ? 0.3812 0.5333 0.3126 0.0485  0.1283  0.0402  30 ASP A N   
232  C CA  . ASP A 30 ? 0.4157 0.5383 0.3132 0.0443  0.1436  0.0293  30 ASP A CA  
233  C C   . ASP A 30 ? 0.4195 0.5402 0.2949 0.0232  0.1345  0.0321  30 ASP A C   
234  O O   . ASP A 30 ? 0.4196 0.5658 0.3157 0.0117  0.1329  0.0407  30 ASP A O   
235  C CB  . ASP A 30 ? 0.4383 0.5806 0.3512 0.0602  0.1736  0.0319  30 ASP A CB  
236  C CG  . ASP A 30 ? 0.4676 0.5918 0.3966 0.0876  0.1944  0.0320  30 ASP A CG  
237  O OD1 . ASP A 30 ? 0.5124 0.5913 0.4236 0.0862  0.1915  0.0205  30 ASP A OD1 
238  O OD2 . ASP A 30 ? 0.5514 0.7070 0.5138 0.1117  0.2175  0.0456  30 ASP A OD2 
239  N N   . GLY A 31 ? 0.4455 0.5386 0.2787 0.0173  0.1313  0.0254  31 GLY A N   
240  C CA  . GLY A 31 ? 0.4764 0.5653 0.2853 0.0058  0.1267  0.0381  31 GLY A CA  
241  C C   . GLY A 31 ? 0.4438 0.5211 0.2612 0.0011  0.1077  0.0485  31 GLY A C   
242  O O   . GLY A 31 ? 0.4751 0.5407 0.2742 -0.0023 0.1090  0.0652  31 GLY A O   
243  N N   . ALA A 32 ? 0.4263 0.5045 0.2699 0.0032  0.0945  0.0418  32 ALA A N   
244  C CA  . ALA A 32 ? 0.4559 0.5210 0.3087 -0.0013 0.0816  0.0476  32 ALA A CA  
245  C C   . ALA A 32 ? 0.4933 0.5474 0.3257 0.0062  0.0655  0.0479  32 ALA A C   
246  O O   . ALA A 32 ? 0.4387 0.4982 0.2553 0.0089  0.0614  0.0355  32 ALA A O   
247  C CB  . ALA A 32 ? 0.4101 0.4913 0.2968 -0.0048 0.0756  0.0392  32 ALA A CB  
248  N N   . VAL A 33 ? 0.4947 0.5353 0.3312 0.0081  0.0600  0.0604  33 VAL A N   
249  C CA  . VAL A 33 ? 0.4798 0.5256 0.3075 0.0177  0.0436  0.0647  33 VAL A CA  
250  C C   . VAL A 33 ? 0.4167 0.4701 0.2594 0.0152  0.0317  0.0440  33 VAL A C   
251  O O   . VAL A 33 ? 0.3844 0.4311 0.2513 0.0119  0.0330  0.0372  33 VAL A O   
252  C CB  . VAL A 33 ? 0.5297 0.5553 0.3694 0.0261  0.0478  0.0852  33 VAL A CB  
253  C CG1 . VAL A 33 ? 0.5331 0.5800 0.3714 0.0410  0.0305  0.0941  33 VAL A CG1 
254  C CG2 . VAL A 33 ? 0.5099 0.5163 0.3343 0.0294  0.0679  0.1111  33 VAL A CG2 
255  N N   . LYS A 34 ? 0.4104 0.4812 0.2371 0.0139  0.0220  0.0336  34 LYS A N   
256  C CA  . LYS A 34 ? 0.4225 0.4936 0.2621 0.0079  0.0175  0.0134  34 LYS A CA  
257  C C   . LYS A 34 ? 0.4006 0.4831 0.2583 0.0116  0.0039  0.0183  34 LYS A C   
258  O O   . LYS A 34 ? 0.3962 0.4950 0.2520 0.0217  -0.0037 0.0367  34 LYS A O   
259  C CB  . LYS A 34 ? 0.4446 0.5268 0.2602 -0.0042 0.0201  -0.0089 34 LYS A CB  
260  C CG  . LYS A 34 ? 0.5037 0.5664 0.3068 -0.0062 0.0418  -0.0197 34 LYS A CG  
261  C CD  . LYS A 34 ? 0.5658 0.6256 0.3469 -0.0235 0.0533  -0.0520 34 LYS A CD  
262  C CE  . LYS A 34 ? 0.5509 0.6564 0.2972 -0.0370 0.0383  -0.0595 34 LYS A CE  
263  N NZ  . LYS A 34 ? 0.6035 0.7088 0.3132 -0.0541 0.0577  -0.0888 34 LYS A NZ  
264  N N   . PRO A 35 ? 0.3497 0.4258 0.2264 0.0068  0.0039  0.0057  35 PRO A N   
265  C CA  . PRO A 35 ? 0.3533 0.4439 0.2501 0.0099  -0.0057 0.0084  35 PRO A CA  
266  C C   . PRO A 35 ? 0.3787 0.5112 0.2701 0.0027  -0.0183 0.0002  35 PRO A C   
267  O O   . PRO A 35 ? 0.3742 0.5167 0.2440 -0.0120 -0.0167 -0.0173 35 PRO A O   
268  C CB  . PRO A 35 ? 0.3937 0.4665 0.3072 0.0046  0.0021  -0.0020 35 PRO A CB  
269  C CG  . PRO A 35 ? 0.4528 0.5081 0.3545 -0.0009 0.0147  -0.0119 35 PRO A CG  
270  C CD  . PRO A 35 ? 0.4095 0.4647 0.2925 0.0028  0.0171  -0.0057 35 PRO A CD  
271  N N   . PRO A 36 ? 0.3388 0.5031 0.2506 0.0109  -0.0287 0.0096  36 PRO A N   
272  C CA  . PRO A 36 ? 0.3508 0.5757 0.2658 -0.0006 -0.0428 -0.0018 36 PRO A CA  
273  C C   . PRO A 36 ? 0.3912 0.6039 0.3109 -0.0289 -0.0337 -0.0356 36 PRO A C   
274  O O   . PRO A 36 ? 0.3383 0.4990 0.2651 -0.0293 -0.0179 -0.0392 36 PRO A O   
275  C CB  . PRO A 36 ? 0.3588 0.6145 0.3073 0.0200  -0.0497 0.0190  36 PRO A CB  
276  C CG  . PRO A 36 ? 0.3653 0.5704 0.3171 0.0428  -0.0369 0.0426  36 PRO A CG  
277  C CD  . PRO A 36 ? 0.3266 0.4767 0.2632 0.0286  -0.0245 0.0269  36 PRO A CD  
278  N N   . PRO A 37 ? 0.3790 0.6414 0.2950 -0.0541 -0.0402 -0.0602 37 PRO A N   
279  C CA  . PRO A 37 ? 0.3883 0.6291 0.3130 -0.0854 -0.0228 -0.0943 37 PRO A CA  
280  C C   . PRO A 37 ? 0.3616 0.5841 0.3207 -0.0798 -0.0154 -0.0870 37 PRO A C   
281  O O   . PRO A 37 ? 0.3406 0.6006 0.3242 -0.0625 -0.0287 -0.0683 37 PRO A O   
282  C CB  . PRO A 37 ? 0.4172 0.7371 0.3379 -0.1179 -0.0347 -0.1235 37 PRO A CB  
283  C CG  . PRO A 37 ? 0.4205 0.8092 0.3246 -0.0990 -0.0609 -0.0999 37 PRO A CG  
284  C CD  . PRO A 37 ? 0.3943 0.7420 0.2989 -0.0562 -0.0623 -0.0564 37 PRO A CD  
285  N N   . ASN A 38 ? 0.4029 0.5656 0.3629 -0.0917 0.0104  -0.0995 38 ASN A N   
286  C CA  . ASN A 38 ? 0.3737 0.5153 0.3585 -0.0895 0.0230  -0.0929 38 ASN A CA  
287  C C   . ASN A 38 ? 0.3794 0.5113 0.3706 -0.0579 0.0155  -0.0629 38 ASN A C   
288  O O   . ASN A 38 ? 0.3140 0.4468 0.3244 -0.0546 0.0213  -0.0571 38 ASN A O   
289  C CB  . ASN A 38 ? 0.4285 0.6269 0.4421 -0.1126 0.0185  -0.1101 38 ASN A CB  
290  C CG  . ASN A 38 ? 0.5082 0.7241 0.5155 -0.1548 0.0282  -0.1492 38 ASN A CG  
291  O OD1 . ASN A 38 ? 0.5378 0.8129 0.5328 -0.1659 0.0089  -0.1623 38 ASN A OD1 
292  N ND2 . ASN A 38 ? 0.4417 0.6050 0.4542 -0.1803 0.0619  -0.1688 38 ASN A ND2 
293  N N   . LYS A 39 ? 0.3145 0.4371 0.2891 -0.0385 0.0065  -0.0472 39 LYS A N   
294  C CA  . LYS A 39 ? 0.2937 0.4000 0.2716 -0.0181 0.0065  -0.0280 39 LYS A CA  
295  C C   . LYS A 39 ? 0.2952 0.3662 0.2544 -0.0119 0.0156  -0.0211 39 LYS A C   
296  O O   . LYS A 39 ? 0.3109 0.3684 0.2549 -0.0159 0.0208  -0.0264 39 LYS A O   
297  C CB  . LYS A 39 ? 0.2932 0.4225 0.2766 -0.0012 -0.0065 -0.0139 39 LYS A CB  
298  C CG  . LYS A 39 ? 0.3162 0.4975 0.3246 0.0016  -0.0164 -0.0126 39 LYS A CG  
299  C CD  . LYS A 39 ? 0.3553 0.5369 0.3857 0.0236  -0.0114 0.0030  39 LYS A CD  
300  C CE  . LYS A 39 ? 0.3308 0.5736 0.3958 0.0312  -0.0178 0.0075  39 LYS A CE  
301  N NZ  . LYS A 39 ? 0.3168 0.5889 0.3943 0.0036  -0.0183 -0.0153 39 LYS A NZ  
302  N N   . TYR A 40 ? 0.2111 0.2664 0.1948 -0.0386 -0.0369 -0.0414 40 TYR A N   
303  C CA  . TYR A 40 ? 0.2696 0.3202 0.2548 -0.0368 -0.0175 -0.0432 40 TYR A CA  
304  C C   . TYR A 40 ? 0.2332 0.2767 0.1985 -0.0375 -0.0228 -0.0255 40 TYR A C   
305  O O   . TYR A 40 ? 0.2643 0.2994 0.2306 -0.0305 -0.0395 -0.0107 40 TYR A O   
306  C CB  . TYR A 40 ? 0.1945 0.2411 0.2176 -0.0228 -0.0070 -0.0440 40 TYR A CB  
307  C CG  . TYR A 40 ? 0.1896 0.2364 0.2329 -0.0254 -0.0001 -0.0601 40 TYR A CG  
308  C CD1 . TYR A 40 ? 0.2488 0.3004 0.3058 -0.0270 -0.0097 -0.0612 40 TYR A CD1 
309  C CD2 . TYR A 40 ? 0.2942 0.3368 0.3465 -0.0271 0.0155  -0.0764 40 TYR A CD2 
310  C CE1 . TYR A 40 ? 0.2693 0.3183 0.3451 -0.0332 -0.0037 -0.0759 40 TYR A CE1 
311  C CE2 . TYR A 40 ? 0.2828 0.3184 0.3550 -0.0303 0.0204  -0.0921 40 TYR A CE2 
312  C CZ  . TYR A 40 ? 0.3186 0.3557 0.4006 -0.0350 0.0108  -0.0907 40 TYR A CZ  
313  O OH  . TYR A 40 ? 0.3512 0.3789 0.4537 -0.0421 0.0153  -0.1064 40 TYR A OH  
314  N N   . PRO A 41 ? 0.2823 0.3294 0.2338 -0.0463 -0.0082 -0.0287 41 PRO A N   
315  C CA  . PRO A 41 ? 0.2551 0.2947 0.1933 -0.0496 -0.0109 -0.0123 41 PRO A CA  
316  C C   . PRO A 41 ? 0.3197 0.3550 0.2907 -0.0328 -0.0079 -0.0082 41 PRO A C   
317  O O   . PRO A 41 ? 0.2890 0.3333 0.2842 -0.0260 0.0066  -0.0186 41 PRO A O   
318  C CB  . PRO A 41 ? 0.2399 0.2944 0.1603 -0.0666 0.0083  -0.0227 41 PRO A CB  
319  C CG  . PRO A 41 ? 0.2613 0.3299 0.2063 -0.0612 0.0251  -0.0483 41 PRO A CG  
320  C CD  . PRO A 41 ? 0.2583 0.3186 0.2150 -0.0523 0.0130  -0.0510 41 PRO A CD  
321  N N   . ILE A 42 ? 0.2577 0.2790 0.2300 -0.0253 -0.0233 0.0058  42 ILE A N   
322  C CA  . ILE A 42 ? 0.2703 0.2889 0.2674 -0.0111 -0.0222 0.0078  42 ILE A CA  
323  C C   . ILE A 42 ? 0.2855 0.2955 0.2731 -0.0174 -0.0238 0.0166  42 ILE A C   
324  O O   . ILE A 42 ? 0.3416 0.3342 0.3092 -0.0250 -0.0372 0.0281  42 ILE A O   
325  C CB  . ILE A 42 ? 0.2327 0.2459 0.2438 0.0022  -0.0355 0.0103  42 ILE A CB  
326  C CG1 . ILE A 42 ? 0.1684 0.1928 0.1906 0.0040  -0.0346 0.0019  42 ILE A CG1 
327  C CG2 . ILE A 42 ? 0.1984 0.2133 0.2285 0.0137  -0.0309 0.0091  42 ILE A CG2 
328  C CD1 . ILE A 42 ? 0.1581 0.1912 0.1932 0.0030  -0.0169 -0.0079 42 ILE A CD1 
329  N N   . PHE A 43 ? 0.2099 0.2303 0.2135 -0.0149 -0.0128 0.0121  43 PHE A N   
330  C CA  . PHE A 43 ? 0.2601 0.2755 0.2613 -0.0214 -0.0148 0.0179  43 PHE A CA  
331  C C   . PHE A 43 ? 0.2392 0.2485 0.2559 -0.0072 -0.0223 0.0175  43 PHE A C   
332  O O   . PHE A 43 ? 0.2217 0.2443 0.2554 0.0034  -0.0165 0.0121  43 PHE A O   
333  C CB  . PHE A 43 ? 0.2214 0.2599 0.2338 -0.0293 0.0010  0.0104  43 PHE A CB  
334  C CG  . PHE A 43 ? 0.2690 0.3086 0.2843 -0.0389 -0.0005 0.0142  43 PHE A CG  
335  C CD1 . PHE A 43 ? 0.2785 0.3102 0.2714 -0.0613 -0.0004 0.0224  43 PHE A CD1 
336  C CD2 . PHE A 43 ? 0.2597 0.3083 0.2978 -0.0285 -0.0029 0.0106  43 PHE A CD2 
337  C CE1 . PHE A 43 ? 0.3040 0.3356 0.3023 -0.0734 -0.0016 0.0254  43 PHE A CE1 
338  C CE2 . PHE A 43 ? 0.3113 0.3631 0.3542 -0.0392 -0.0056 0.0117  43 PHE A CE2 
339  C CZ  . PHE A 43 ? 0.2765 0.3195 0.3020 -0.0620 -0.0043 0.0182  43 PHE A CZ  
340  N N   . PHE A 44 ? 0.2182 0.2064 0.2277 -0.0079 -0.0354 0.0229  44 PHE A N   
341  C CA  . PHE A 44 ? 0.2443 0.2279 0.2663 0.0047  -0.0414 0.0172  44 PHE A CA  
342  C C   . PHE A 44 ? 0.2403 0.2281 0.2661 -0.0022 -0.0397 0.0147  44 PHE A C   
343  O O   . PHE A 44 ? 0.2563 0.2313 0.2737 -0.0171 -0.0434 0.0201  44 PHE A O   
344  C CB  . PHE A 44 ? 0.2725 0.2302 0.2925 0.0105  -0.0575 0.0189  44 PHE A CB  
345  C CG  . PHE A 44 ? 0.3094 0.2693 0.3334 0.0197  -0.0626 0.0191  44 PHE A CG  
346  C CD1 . PHE A 44 ? 0.3527 0.3044 0.3600 0.0105  -0.0695 0.0298  44 PHE A CD1 
347  C CD2 . PHE A 44 ? 0.2723 0.2466 0.3155 0.0347  -0.0600 0.0081  44 PHE A CD2 
348  C CE1 . PHE A 44 ? 0.4133 0.3714 0.4264 0.0180  -0.0768 0.0287  44 PHE A CE1 
349  C CE2 . PHE A 44 ? 0.2648 0.2468 0.3177 0.0413  -0.0647 0.0066  44 PHE A CE2 
350  C CZ  . PHE A 44 ? 0.3158 0.2898 0.3554 0.0339  -0.0745 0.0165  44 PHE A CZ  
351  N N   . PHE A 45 ? 0.2435 0.2493 0.2806 0.0064  -0.0355 0.0079  45 PHE A N   
352  C CA  . PHE A 45 ? 0.2257 0.2396 0.2678 0.0002  -0.0375 0.0042  45 PHE A CA  
353  C C   . PHE A 45 ? 0.2315 0.2215 0.2685 -0.0021 -0.0489 -0.0015 45 PHE A C   
354  O O   . PHE A 45 ? 0.2592 0.2322 0.2945 0.0079  -0.0545 -0.0057 45 PHE A O   
355  C CB  . PHE A 45 ? 0.2022 0.2392 0.2525 0.0099  -0.0350 0.0009  45 PHE A CB  
356  C CG  . PHE A 45 ? 0.1922 0.2477 0.2547 0.0132  -0.0266 0.0058  45 PHE A CG  
357  C CD1 . PHE A 45 ? 0.1456 0.2179 0.2230 0.0057  -0.0226 0.0052  45 PHE A CD1 
358  C CD2 . PHE A 45 ? 0.1913 0.2477 0.2545 0.0232  -0.0221 0.0089  45 PHE A CD2 
359  C CE1 . PHE A 45 ? 0.2005 0.2887 0.2959 0.0116  -0.0151 0.0050  45 PHE A CE1 
360  C CE2 . PHE A 45 ? 0.1726 0.2392 0.2507 0.0271  -0.0159 0.0117  45 PHE A CE2 
361  C CZ  . PHE A 45 ? 0.1469 0.2290 0.2428 0.0231  -0.0129 0.0084  45 PHE A CZ  
362  N N   . GLY A 46 ? 0.2602 0.2502 0.2999 -0.0150 -0.0527 -0.0041 46 GLY A N   
363  C CA  . GLY A 46 ? 0.2738 0.2375 0.3114 -0.0193 -0.0641 -0.0124 46 GLY A CA  
364  C C   . GLY A 46 ? 0.3554 0.2818 0.3851 -0.0311 -0.0715 -0.0016 46 GLY A C   
365  O O   . GLY A 46 ? 0.3395 0.2522 0.3680 -0.0506 -0.0754 0.0018  46 GLY A O   
366  N N   . THR A 47 ? 0.3290 0.2388 0.3528 -0.0215 -0.0750 0.0059  47 THR A N   
367  C CA  . THR A 47 ? 0.3637 0.2362 0.3748 -0.0333 -0.0859 0.0217  47 THR A CA  
368  C C   . THR A 47 ? 0.3855 0.2703 0.3799 -0.0538 -0.0762 0.0381  47 THR A C   
369  O O   . THR A 47 ? 0.3788 0.2361 0.3558 -0.0739 -0.0828 0.0540  47 THR A O   
370  C CB  . THR A 47 ? 0.4318 0.2855 0.4448 -0.0149 -0.0973 0.0239  47 THR A CB  
371  O OG1 . THR A 47 ? 0.3481 0.2310 0.3569 -0.0099 -0.0869 0.0279  47 THR A OG1 
372  C CG2 . THR A 47 ? 0.4244 0.2779 0.4585 0.0071  -0.1012 0.0017  47 THR A CG2 
373  N N   . HIS A 48 ? 0.3006 0.2243 0.2990 -0.0499 -0.0606 0.0341  48 HIS A N   
374  C CA  . HIS A 48 ? 0.2874 0.2311 0.2741 -0.0668 -0.0471 0.0418  48 HIS A CA  
375  C C   . HIS A 48 ? 0.3936 0.3167 0.3534 -0.0733 -0.0536 0.0567  48 HIS A C   
376  O O   . HIS A 48 ? 0.4032 0.3329 0.3420 -0.0953 -0.0450 0.0657  48 HIS A O   
377  C CB  . HIS A 48 ? 0.3006 0.2533 0.2889 -0.0922 -0.0400 0.0436  48 HIS A CB  
378  C CG  . HIS A 48 ? 0.2953 0.2676 0.3100 -0.0870 -0.0395 0.0294  48 HIS A CG  
379  N ND1 . HIS A 48 ? 0.3830 0.3484 0.4038 -0.1058 -0.0437 0.0283  48 HIS A ND1 
380  C CD2 . HIS A 48 ? 0.3157 0.3138 0.3499 -0.0669 -0.0375 0.0170  48 HIS A CD2 
381  C CE1 . HIS A 48 ? 0.4655 0.4553 0.5088 -0.0966 -0.0451 0.0137  48 HIS A CE1 
382  N NE2 . HIS A 48 ? 0.3334 0.3424 0.3828 -0.0729 -0.0419 0.0084  48 HIS A NE2 
383  N N   . GLU A 49 ? 0.3531 0.2554 0.3133 -0.0553 -0.0686 0.0585  49 GLU A N   
384  C CA  . GLU A 49 ? 0.3940 0.2803 0.3302 -0.0594 -0.0794 0.0730  49 GLU A CA  
385  C C   . GLU A 49 ? 0.4055 0.3236 0.3437 -0.0507 -0.0683 0.0641  49 GLU A C   
386  O O   . GLU A 49 ? 0.3347 0.2788 0.2960 -0.0374 -0.0556 0.0487  49 GLU A O   
387  C CB  . GLU A 49 ? 0.3649 0.2128 0.3073 -0.0440 -0.1054 0.0793  49 GLU A CB  
388  C CG  . GLU A 49 ? 0.5774 0.3818 0.5105 -0.0588 -0.1196 0.0930  49 GLU A CG  
389  C CD  . GLU A 49 ? 0.6690 0.4466 0.6269 -0.0366 -0.1387 0.0847  49 GLU A CD  
390  O OE1 . GLU A 49 ? 0.6955 0.4842 0.6698 -0.0148 -0.1450 0.0763  49 GLU A OE1 
391  O OE2 . GLU A 49 ? 0.6865 0.4396 0.6507 -0.0421 -0.1441 0.0827  49 GLU A OE2 
392  N N   . THR A 50 ? 0.3459 0.2602 0.2567 -0.0612 -0.0738 0.0747  50 THR A N   
393  C CA  . THR A 50 ? 0.3571 0.2981 0.2676 -0.0566 -0.0648 0.0643  50 THR A CA  
394  C C   . THR A 50 ? 0.4486 0.3761 0.3533 -0.0470 -0.0873 0.0715  50 THR A C   
395  O O   . THR A 50 ? 0.4452 0.3433 0.3296 -0.0530 -0.1094 0.0905  50 THR A O   
396  C CB  . THR A 50 ? 0.4333 0.3938 0.3167 -0.0805 -0.0474 0.0632  50 THR A CB  
397  O OG1 . THR A 50 ? 0.6765 0.6138 0.5199 -0.1040 -0.0585 0.0848  50 THR A OG1 
398  C CG2 . THR A 50 ? 0.3787 0.3627 0.2820 -0.0848 -0.0250 0.0508  50 THR A CG2 
399  N N   . ALA A 51 ? 0.3938 0.3424 0.3188 -0.0327 -0.0836 0.0574  51 ALA A N   
400  C CA  . ALA A 51 ? 0.3361 0.2827 0.2600 -0.0257 -0.1039 0.0609  51 ALA A CA  
401  C C   . ALA A 51 ? 0.3553 0.3312 0.2862 -0.0259 -0.0905 0.0443  51 ALA A C   
402  O O   . ALA A 51 ? 0.3821 0.3742 0.3266 -0.0254 -0.0678 0.0307  51 ALA A O   
403  C CB  . ALA A 51 ? 0.4140 0.3498 0.3724 -0.0023 -0.1212 0.0595  51 ALA A CB  
404  N N   . PHE A 52 ? 0.3302 0.3112 0.2540 -0.0267 -0.1073 0.0454  52 PHE A N   
405  C CA  . PHE A 52 ? 0.2983 0.3039 0.2275 -0.0301 -0.0977 0.0284  52 PHE A CA  
406  C C   . PHE A 52 ? 0.3260 0.3446 0.2987 -0.0118 -0.1039 0.0190  52 PHE A C   
407  O O   . PHE A 52 ? 0.3611 0.3773 0.3458 -0.0020 -0.1281 0.0258  52 PHE A O   
408  C CB  . PHE A 52 ? 0.3922 0.4007 0.2811 -0.0480 -0.1120 0.0331  52 PHE A CB  
409  C CG  . PHE A 52 ? 0.3880 0.3914 0.2300 -0.0713 -0.1008 0.0395  52 PHE A CG  
410  C CD1 . PHE A 52 ? 0.3457 0.3627 0.1911 -0.0780 -0.0699 0.0230  52 PHE A CD1 
411  C CD2 . PHE A 52 ? 0.5167 0.5032 0.3137 -0.0870 -0.1208 0.0621  52 PHE A CD2 
412  C CE1 . PHE A 52 ? 0.5036 0.5245 0.3114 -0.1007 -0.0558 0.0247  52 PHE A CE1 
413  C CE2 . PHE A 52 ? 0.5730 0.5596 0.3309 -0.1110 -0.1039 0.0661  52 PHE A CE2 
414  C CZ  . PHE A 52 ? 0.4853 0.4925 0.2431 -0.1205 -0.0726 0.0471  52 PHE A CZ  
415  N N   . LEU A 53 ? 0.2178 0.2510 0.2158 -0.0079 -0.0832 0.0038  53 LEU A N   
416  C CA  . LEU A 53 ? 0.2476 0.2960 0.2856 0.0051  -0.0846 -0.0043 53 LEU A CA  
417  C C   . LEU A 53 ? 0.2310 0.2957 0.2818 -0.0028 -0.0721 -0.0193 53 LEU A C   
418  O O   . LEU A 53 ? 0.2338 0.2941 0.2714 -0.0123 -0.0563 -0.0258 53 LEU A O   
419  C CB  . LEU A 53 ? 0.1979 0.2434 0.2563 0.0174  -0.0724 -0.0040 53 LEU A CB  
420  C CG  . LEU A 53 ? 0.2881 0.3185 0.3483 0.0287  -0.0856 0.0045  53 LEU A CG  
421  C CD1 . LEU A 53 ? 0.2464 0.2801 0.3238 0.0376  -0.0697 -0.0011 53 LEU A CD1 
422  C CD2 . LEU A 53 ? 0.2825 0.3185 0.3636 0.0397  -0.1092 0.0043  53 LEU A CD2 
423  N N   . GLY A 54 ? 0.1691 0.2531 0.2509 0.0012  -0.0789 -0.0265 54 GLY A N   
424  C CA  . GLY A 54 ? 0.2398 0.3366 0.3397 -0.0081 -0.0669 -0.0403 54 GLY A CA  
425  C C   . GLY A 54 ? 0.1859 0.2847 0.3112 -0.0035 -0.0467 -0.0409 54 GLY A C   
426  O O   . GLY A 54 ? 0.1379 0.2366 0.2698 0.0081  -0.0444 -0.0341 54 GLY A O   
427  N N   . PRO A 55 ? 0.1702 0.2690 0.3076 -0.0140 -0.0329 -0.0488 55 PRO A N   
428  C CA  . PRO A 55 ? 0.1629 0.2591 0.3171 -0.0135 -0.0150 -0.0442 55 PRO A CA  
429  C C   . PRO A 55 ? 0.1580 0.2787 0.3366 -0.0082 -0.0136 -0.0430 55 PRO A C   
430  O O   . PRO A 55 ? 0.1396 0.2582 0.3186 -0.0058 -0.0003 -0.0357 55 PRO A O   
431  C CB  . PRO A 55 ? 0.1517 0.2411 0.3175 -0.0288 -0.0067 -0.0531 55 PRO A CB  
432  C CG  . PRO A 55 ? 0.1784 0.2566 0.3227 -0.0332 -0.0130 -0.0633 55 PRO A CG  
433  C CD  . PRO A 55 ? 0.2659 0.3596 0.3957 -0.0283 -0.0325 -0.0616 55 PRO A CD  
434  N N   . LYS A 56 ? 0.1136 0.2609 0.3140 -0.0064 -0.0271 -0.0514 56 LYS A N   
435  C CA  . LYS A 56 ? 0.1116 0.2889 0.3427 0.0003  -0.0229 -0.0559 56 LYS A CA  
436  C C   . LYS A 56 ? 0.1207 0.2902 0.3404 0.0164  -0.0211 -0.0503 56 LYS A C   
437  O O   . LYS A 56 ? 0.1190 0.3059 0.3516 0.0201  -0.0099 -0.0544 56 LYS A O   
438  C CB  . LYS A 56 ? 0.1208 0.3236 0.3755 0.0045  -0.0409 -0.0651 56 LYS A CB  
439  C CG  . LYS A 56 ? 0.1847 0.3751 0.4257 0.0219  -0.0641 -0.0597 56 LYS A CG  
440  C CD  . LYS A 56 ? 0.2649 0.4726 0.5226 0.0248  -0.0836 -0.0639 56 LYS A CD  
441  C CE  . LYS A 56 ? 0.2893 0.4775 0.5303 0.0392  -0.1076 -0.0538 56 LYS A CE  
442  N NZ  . LYS A 56 ? 0.2605 0.4329 0.5004 0.0545  -0.1017 -0.0513 56 LYS A NZ  
443  N N   . ASP A 57 ? 0.1300 0.2710 0.3197 0.0231  -0.0301 -0.0416 57 ASP A N   
444  C CA  . ASP A 57 ? 0.1579 0.2882 0.3372 0.0362  -0.0311 -0.0379 57 ASP A CA  
445  C C   . ASP A 57 ? 0.1358 0.2447 0.2880 0.0323  -0.0174 -0.0280 57 ASP A C   
446  O O   . ASP A 57 ? 0.1604 0.2578 0.3000 0.0401  -0.0193 -0.0250 57 ASP A O   
447  C CB  . ASP A 57 ? 0.1439 0.2585 0.3134 0.0454  -0.0548 -0.0338 57 ASP A CB  
448  C CG  . ASP A 57 ? 0.2689 0.3960 0.4589 0.0531  -0.0681 -0.0397 57 ASP A CG  
449  O OD1 . ASP A 57 ? 0.2135 0.3593 0.4247 0.0570  -0.0569 -0.0495 57 ASP A OD1 
450  O OD2 . ASP A 57 ? 0.2007 0.3191 0.3830 0.0538  -0.0890 -0.0340 57 ASP A OD2 
451  N N   . LEU A 58 ? 0.0999 0.2028 0.2469 0.0209  -0.0056 -0.0238 58 LEU A N   
452  C CA  . LEU A 58 ? 0.1027 0.1855 0.2300 0.0194  0.0028  -0.0140 58 LEU A CA  
453  C C   . LEU A 58 ? 0.1703 0.2580 0.3015 0.0129  0.0174  -0.0079 58 LEU A C   
454  O O   . LEU A 58 ? 0.1150 0.2078 0.2597 0.0018  0.0241  -0.0086 58 LEU A O   
455  C CB  . LEU A 58 ? 0.1558 0.2219 0.2742 0.0133  0.0013  -0.0142 58 LEU A CB  
456  C CG  . LEU A 58 ? 0.1879 0.2508 0.2931 0.0142  -0.0121 -0.0177 58 LEU A CG  
457  C CD1 . LEU A 58 ? 0.2054 0.2587 0.3009 0.0054  -0.0088 -0.0234 58 LEU A CD1 
458  C CD2 . LEU A 58 ? 0.1614 0.2153 0.2506 0.0214  -0.0175 -0.0110 58 LEU A CD2 
459  N N   . PHE A 59 ? 0.1399 0.2256 0.2568 0.0173  0.0212  -0.0009 59 PHE A N   
460  C CA  . PHE A 59 ? 0.1430 0.2342 0.2538 0.0094  0.0331  0.0084  59 PHE A CA  
461  C C   . PHE A 59 ? 0.1938 0.2629 0.2872 0.0108  0.0309  0.0238  59 PHE A C   
462  O O   . PHE A 59 ? 0.2100 0.2751 0.2931 0.0198  0.0236  0.0232  59 PHE A O   
463  C CB  . PHE A 59 ? 0.1771 0.2931 0.2847 0.0129  0.0383  -0.0002 59 PHE A CB  
464  C CG  . PHE A 59 ? 0.1440 0.2882 0.2790 0.0138  0.0409  -0.0174 59 PHE A CG  
465  C CD1 . PHE A 59 ? 0.1202 0.2649 0.2707 0.0264  0.0266  -0.0290 59 PHE A CD1 
466  C CD2 . PHE A 59 ? 0.1287 0.3004 0.2757 0.0013  0.0566  -0.0210 59 PHE A CD2 
467  C CE1 . PHE A 59 ? 0.1122 0.2847 0.2947 0.0302  0.0248  -0.0446 59 PHE A CE1 
468  C CE2 . PHE A 59 ? 0.1476 0.3525 0.3288 0.0032  0.0588  -0.0397 59 PHE A CE2 
469  C CZ  . PHE A 59 ? 0.1365 0.3399 0.3361 0.0196  0.0409  -0.0512 59 PHE A CZ  
470  N N   . PRO A 60 ? 0.2474 0.3010 0.3404 0.0023  0.0349  0.0379  60 PRO A N   
471  C CA  . PRO A 60 ? 0.2122 0.2452 0.2959 0.0076  0.0281  0.0526  60 PRO A CA  
472  C C   . PRO A 60 ? 0.2282 0.2719 0.2889 0.0111  0.0247  0.0597  60 PRO A C   
473  O O   . PRO A 60 ? 0.2966 0.3575 0.3420 0.0033  0.0320  0.0611  60 PRO A O   
474  C CB  . PRO A 60 ? 0.3124 0.3242 0.4009 -0.0034 0.0315  0.0687  60 PRO A CB  
475  C CG  . PRO A 60 ? 0.4547 0.4840 0.5459 -0.0192 0.0438  0.0652  60 PRO A CG  
476  C CD  . PRO A 60 ? 0.3009 0.3525 0.4061 -0.0128 0.0435  0.0415  60 PRO A CD  
477  N N   . TYR A 61 ? 0.1925 0.2299 0.2518 0.0216  0.0142  0.0615  61 TYR A N   
478  C CA  . TYR A 61 ? 0.2798 0.3299 0.3191 0.0245  0.0082  0.0631  61 TYR A CA  
479  C C   . TYR A 61 ? 0.2741 0.3242 0.2894 0.0164  0.0070  0.0833  61 TYR A C   
480  O O   . TYR A 61 ? 0.2965 0.3652 0.2874 0.0098  0.0115  0.0805  61 TYR A O   
481  C CB  . TYR A 61 ? 0.2198 0.2667 0.2684 0.0347  -0.0031 0.0607  61 TYR A CB  
482  C CG  . TYR A 61 ? 0.2088 0.2683 0.2395 0.0361  -0.0126 0.0630  61 TYR A CG  
483  C CD1 . TYR A 61 ? 0.2849 0.3575 0.3028 0.0344  -0.0110 0.0479  61 TYR A CD1 
484  C CD2 . TYR A 61 ? 0.3018 0.3594 0.3322 0.0400  -0.0256 0.0782  61 TYR A CD2 
485  C CE1 . TYR A 61 ? 0.2530 0.3367 0.2542 0.0336  -0.0200 0.0461  61 TYR A CE1 
486  C CE2 . TYR A 61 ? 0.3185 0.3907 0.3326 0.0397  -0.0369 0.0788  61 TYR A CE2 
487  C CZ  . TYR A 61 ? 0.2769 0.3623 0.2748 0.0352  -0.0332 0.0617  61 TYR A CZ  
488  O OH  . TYR A 61 ? 0.3081 0.4079 0.2890 0.0330  -0.0449 0.0589  61 TYR A OH  
489  N N   . ASP A 62 ? 0.2863 0.3146 0.3070 0.0161  0.0003  0.1034  62 ASP A N   
490  C CA  . ASP A 62 ? 0.3397 0.3633 0.3320 0.0078  -0.0065 0.1288  62 ASP A CA  
491  C C   . ASP A 62 ? 0.3930 0.4242 0.3629 -0.0122 0.0095  0.1356  62 ASP A C   
492  O O   . ASP A 62 ? 0.4578 0.5000 0.3908 -0.0238 0.0096  0.1490  62 ASP A O   
493  C CB  . ASP A 62 ? 0.4382 0.4310 0.4467 0.0150  -0.0219 0.1508  62 ASP A CB  
494  C CG  . ASP A 62 ? 0.5909 0.5580 0.6281 0.0132  -0.0144 0.1493  62 ASP A CG  
495  O OD1 . ASP A 62 ? 0.5328 0.5094 0.5757 0.0051  0.0016  0.1324  62 ASP A OD1 
496  O OD2 . ASP A 62 ? 0.7061 0.6431 0.7624 0.0202  -0.0263 0.1641  62 ASP A OD2 
497  N N   . LYS A 63 ? 0.3201 0.3502 0.3109 -0.0185 0.0235  0.1252  63 LYS A N   
498  C CA  . LYS A 63 ? 0.4053 0.4517 0.3816 -0.0395 0.0415  0.1276  63 LYS A CA  
499  C C   . LYS A 63 ? 0.2979 0.3850 0.2619 -0.0405 0.0533  0.1042  63 LYS A C   
500  O O   . LYS A 63 ? 0.3098 0.4191 0.2478 -0.0578 0.0671  0.1075  63 LYS A O   
501  C CB  . LYS A 63 ? 0.4560 0.4946 0.4646 -0.0464 0.0513  0.1200  63 LYS A CB  
502  C CG  . LYS A 63 ? 0.4664 0.5326 0.4727 -0.0686 0.0724  0.1153  63 LYS A CG  
503  C CD  . LYS A 63 ? 0.4243 0.4913 0.4703 -0.0716 0.0782  0.0991  63 LYS A CD  
504  C CE  . LYS A 63 ? 0.3829 0.4698 0.4341 -0.0986 0.0975  0.1014  63 LYS A CE  
505  N NZ  . LYS A 63 ? 0.4253 0.5660 0.4825 -0.0999 0.1129  0.0767  63 LYS A NZ  
506  N N   . CYS A 64 ? 0.2858 0.3824 0.2677 -0.0232 0.0487  0.0798  64 CYS A N   
507  C CA  . CYS A 64 ? 0.2934 0.4226 0.2766 -0.0207 0.0588  0.0529  64 CYS A CA  
508  C C   . CYS A 64 ? 0.3474 0.4834 0.3116 -0.0111 0.0498  0.0424  64 CYS A C   
509  O O   . CYS A 64 ? 0.2733 0.4308 0.2428 -0.0062 0.0563  0.0167  64 CYS A O   
510  C CB  . CYS A 64 ? 0.2786 0.4115 0.3005 -0.0102 0.0594  0.0320  64 CYS A CB  
511  S SG  . CYS A 64 ? 0.3176 0.4452 0.3661 -0.0221 0.0672  0.0383  64 CYS A SG  
512  N N   . LYS A 65 ? 0.3415 0.4608 0.2878 -0.0080 0.0341  0.0595  65 LYS A N   
513  C CA  . LYS A 65 ? 0.3258 0.4536 0.2576 -0.0012 0.0244  0.0467  65 LYS A CA  
514  C C   . LYS A 65 ? 0.3947 0.5498 0.2902 -0.0132 0.0342  0.0377  65 LYS A C   
515  O O   . LYS A 65 ? 0.3705 0.5380 0.2602 -0.0083 0.0325  0.0141  65 LYS A O   
516  C CB  . LYS A 65 ? 0.3605 0.4711 0.2887 0.0050  0.0036  0.0647  65 LYS A CB  
517  C CG  . LYS A 65 ? 0.4018 0.4991 0.3131 -0.0019 -0.0050 0.0975  65 LYS A CG  
518  C CD  . LYS A 65 ? 0.4921 0.5865 0.3992 0.0061  -0.0286 0.1077  65 LYS A CD  
519  C CE  . LYS A 65 ? 0.6426 0.7241 0.5286 0.0008  -0.0439 0.1426  65 LYS A CE  
520  N NZ  . LYS A 65 ? 0.6818 0.7325 0.5966 0.0058  -0.0459 0.1616  65 LYS A NZ  
521  N N   . ASP A 66 ? 0.3911 0.5555 0.2602 -0.0310 0.0454  0.0547  66 ASP A N   
522  C CA  . ASP A 66 ? 0.4314 0.6275 0.2606 -0.0456 0.0582  0.0432  66 ASP A CA  
523  C C   . ASP A 66 ? 0.4461 0.6713 0.2987 -0.0414 0.0784  0.0034  66 ASP A C   
524  O O   . ASP A 66 ? 0.4500 0.6974 0.2848 -0.0437 0.0849  -0.0217 66 ASP A O   
525  C CB  . ASP A 66 ? 0.4779 0.6741 0.2738 -0.0689 0.0667  0.0712  66 ASP A CB  
526  C CG  . ASP A 66 ? 0.6929 0.9147 0.4629 -0.0826 0.0830  0.0516  66 ASP A CG  
527  O OD1 . ASP A 66 ? 0.7787 1.0058 0.5173 -0.0837 0.0734  0.0456  66 ASP A OD1 
528  O OD2 . ASP A 66 ? 0.8079 1.0463 0.5915 -0.0924 0.1046  0.0412  66 ASP A OD2 
529  N N   . LYS A 67 ? 0.3853 0.6076 0.2830 -0.0333 0.0851  -0.0046 67 LYS A N   
530  C CA  . LYS A 67 ? 0.3774 0.6275 0.3075 -0.0256 0.1001  -0.0411 67 LYS A CA  
531  C C   . LYS A 67 ? 0.3409 0.5743 0.2994 -0.0022 0.0842  -0.0627 67 LYS A C   
532  O O   . LYS A 67 ? 0.3345 0.5846 0.3010 0.0056  0.0892  -0.0951 67 LYS A O   
533  C CB  . LYS A 67 ? 0.3416 0.6008 0.3076 -0.0300 0.1121  -0.0382 67 LYS A CB  
534  C CG  . LYS A 67 ? 0.3396 0.6153 0.3502 -0.0176 0.1174  -0.0711 67 LYS A CG  
535  C CD  . LYS A 67 ? 0.4184 0.6964 0.4669 -0.0199 0.1205  -0.0654 67 LYS A CD  
536  C CE  . LYS A 67 ? 0.4457 0.7399 0.5380 -0.0069 0.1204  -0.0937 67 LYS A CE  
537  N NZ  . LYS A 67 ? 0.4773 0.7982 0.5836 -0.0222 0.1368  -0.0957 67 LYS A NZ  
538  N N   . TYR A 68 ? 0.2635 0.4628 0.2372 0.0077  0.0657  -0.0458 68 TYR A N   
539  C CA  . TYR A 68 ? 0.2828 0.4630 0.2824 0.0254  0.0512  -0.0608 68 TYR A CA  
540  C C   . TYR A 68 ? 0.3019 0.4635 0.2815 0.0278  0.0351  -0.0581 68 TYR A C   
541  O O   . TYR A 68 ? 0.2681 0.4134 0.2645 0.0385  0.0243  -0.0719 68 TYR A O   
542  C CB  . TYR A 68 ? 0.2463 0.4057 0.2744 0.0316  0.0427  -0.0473 68 TYR A CB  
543  C CG  . TYR A 68 ? 0.2600 0.4389 0.3158 0.0298  0.0546  -0.0532 68 TYR A CG  
544  C CD1 . TYR A 68 ? 0.2566 0.4649 0.3349 0.0352  0.0650  -0.0808 68 TYR A CD1 
545  C CD2 . TYR A 68 ? 0.2463 0.4164 0.3108 0.0228  0.0549  -0.0344 68 TYR A CD2 
546  C CE1 . TYR A 68 ? 0.2820 0.5111 0.3912 0.0328  0.0735  -0.0867 68 TYR A CE1 
547  C CE2 . TYR A 68 ? 0.2118 0.4032 0.3050 0.0188  0.0644  -0.0417 68 TYR A CE2 
548  C CZ  . TYR A 68 ? 0.2158 0.4409 0.3332 0.0239  0.0739  -0.0678 68 TYR A CZ  
549  O OH  . TYR A 68 ? 0.1998 0.4414 0.3451 0.0188  0.0794  -0.0728 68 TYR A OH  
550  N N   . GLY A 69 ? 0.3314 0.4942 0.2773 0.0173  0.0313  -0.0398 69 GLY A N   
551  C CA  . GLY A 69 ? 0.3309 0.4793 0.2662 0.0193  0.0132  -0.0349 69 GLY A CA  
552  C C   . GLY A 69 ? 0.3270 0.4871 0.2404 0.0163  0.0098  -0.0576 69 GLY A C   
553  O O   . GLY A 69 ? 0.4294 0.5847 0.3290 0.0134  -0.0056 -0.0515 69 GLY A O   
554  N N   . LYS A 70 ? 0.3449 0.5220 0.2585 0.0171  0.0233  -0.0863 70 LYS A N   
555  C CA  . LYS A 70 ? 0.3604 0.5467 0.2558 0.0147  0.0210  -0.1149 70 LYS A CA  
556  C C   . LYS A 70 ? 0.3759 0.5350 0.3034 0.0272  0.0091  -0.1351 70 LYS A C   
557  O O   . LYS A 70 ? 0.3706 0.5102 0.3331 0.0384  0.0068  -0.1316 70 LYS A O   
558  C CB  . LYS A 70 ? 0.4293 0.6496 0.3117 0.0094  0.0438  -0.1421 70 LYS A CB  
559  C CG  . LYS A 70 ? 0.5002 0.7402 0.3612 -0.0051 0.0584  -0.1162 70 LYS A CG  
560  C CD  . LYS A 70 ? 0.4927 0.7568 0.3483 -0.0153 0.0784  -0.1328 70 LYS A CD  
561  C CE  . LYS A 70 ? 0.6350 0.9124 0.5154 -0.0178 0.0960  -0.1260 70 LYS A CE  
562  N NZ  . LYS A 70 ? 0.6603 0.9643 0.5530 -0.0221 0.1146  -0.1528 70 LYS A NZ  
563  N N   . PRO A 71 ? 0.3967 0.5517 0.3108 0.0233  -0.0011 -0.1542 71 PRO A N   
564  C CA  . PRO A 71 ? 0.3505 0.4731 0.2938 0.0315  -0.0138 -0.1708 71 PRO A CA  
565  C C   . PRO A 71 ? 0.3822 0.4960 0.3599 0.0470  -0.0056 -0.1974 71 PRO A C   
566  O O   . PRO A 71 ? 0.3834 0.5220 0.3630 0.0482  0.0111  -0.2120 71 PRO A O   
567  C CB  . PRO A 71 ? 0.4741 0.6014 0.3927 0.0210  -0.0227 -0.1928 71 PRO A CB  
568  C CG  . PRO A 71 ? 0.4889 0.6458 0.3658 0.0075  -0.0234 -0.1721 71 PRO A CG  
569  C CD  . PRO A 71 ? 0.3988 0.5761 0.2684 0.0087  -0.0045 -0.1585 71 PRO A CD  
570  N N   . ASN A 72 ? 0.3689 0.4450 0.3779 0.0560  -0.0192 -0.1945 72 ASN A N   
571  C CA  . ASN A 72 ? 0.4078 0.4677 0.4561 0.0719  -0.0195 -0.2075 72 ASN A CA  
572  C C   . ASN A 72 ? 0.3776 0.3923 0.4421 0.0732  -0.0382 -0.2119 72 ASN A C   
573  O O   . ASN A 72 ? 0.4349 0.4282 0.4865 0.0630  -0.0509 -0.2017 72 ASN A O   
574  C CB  . ASN A 72 ? 0.3479 0.4074 0.4156 0.0807  -0.0187 -0.1860 72 ASN A CB  
575  C CG  . ASN A 72 ? 0.3916 0.4393 0.4982 0.0931  -0.0238 -0.1886 72 ASN A CG  
576  O OD1 . ASN A 72 ? 0.4610 0.4753 0.5845 0.0981  -0.0389 -0.1922 72 ASN A OD1 
577  N ND2 . ASN A 72 ? 0.5249 0.6004 0.6448 0.0963  -0.0126 -0.1847 72 ASN A ND2 
578  N N   . LYS A 73 ? 0.4106 0.4119 0.5046 0.0838  -0.0406 -0.2257 73 LYS A N   
579  C CA  . LYS A 73 ? 0.4568 0.4141 0.5648 0.0838  -0.0573 -0.2299 73 LYS A CA  
580  C C   . LYS A 73 ? 0.4581 0.3748 0.5768 0.0841  -0.0752 -0.2010 73 LYS A C   
581  O O   . LYS A 73 ? 0.4766 0.3549 0.5953 0.0760  -0.0889 -0.1960 73 LYS A O   
582  C CB  . LYS A 73 ? 0.4307 0.3868 0.5681 0.0967  -0.0555 -0.2544 73 LYS A CB  
583  N N   . ARG A 74 ? 0.3881 0.3130 0.5134 0.0903  -0.0749 -0.1809 74 ARG A N   
584  C CA  . ARG A 74 ? 0.4070 0.2959 0.5399 0.0897  -0.0919 -0.1532 74 ARG A CA  
585  C C   . ARG A 74 ? 0.4414 0.3028 0.5525 0.0718  -0.1005 -0.1355 74 ARG A C   
586  O O   . ARG A 74 ? 0.3810 0.2609 0.4725 0.0621  -0.0932 -0.1376 74 ARG A O   
587  C CB  . ARG A 74 ? 0.3901 0.2993 0.5281 0.0960  -0.0885 -0.1360 74 ARG A CB  
588  C CG  . ARG A 74 ? 0.4918 0.4298 0.6546 0.1094  -0.0809 -0.1518 74 ARG A CG  
589  C CD  . ARG A 74 ? 0.5159 0.4273 0.7050 0.1190  -0.0970 -0.1571 74 ARG A CD  
590  N NE  . ARG A 74 ? 0.5798 0.4711 0.7725 0.1197  -0.1134 -0.1306 74 ARG A NE  
591  C CZ  . ARG A 74 ? 0.5613 0.4753 0.7669 0.1260  -0.1123 -0.1258 74 ARG A CZ  
592  N NH1 . ARG A 74 ? 0.4667 0.4234 0.6857 0.1316  -0.0948 -0.1443 74 ARG A NH1 
593  N NH2 . ARG A 74 ? 0.5645 0.4588 0.7675 0.1244  -0.1288 -0.1020 74 ARG A NH2 
594  N N   . LYS A 75 ? 0.4680 0.2881 0.5819 0.0650  -0.1164 -0.1170 75 LYS A N   
595  C CA  . LYS A 75 ? 0.4574 0.2517 0.5530 0.0424  -0.1232 -0.1004 75 LYS A CA  
596  C C   . LYS A 75 ? 0.3937 0.2105 0.4716 0.0320  -0.1156 -0.0817 75 LYS A C   
597  O O   . LYS A 75 ? 0.4372 0.2653 0.5140 0.0388  -0.1130 -0.0652 75 LYS A O   
598  C CB  . LYS A 75 ? 0.4697 0.2207 0.5669 0.0353  -0.1389 -0.0776 75 LYS A CB  
599  C CG  . LYS A 75 ? 0.4942 0.2224 0.5722 0.0069  -0.1427 -0.0576 75 LYS A CG  
600  N N   . GLY A 76 ? 0.3481 0.1864 0.4121 0.0146  -0.1082 -0.0816 76 GLY A N   
601  C CA  . GLY A 76 ? 0.3552 0.2285 0.4062 0.0051  -0.0967 -0.0617 76 GLY A CA  
602  C C   . GLY A 76 ? 0.3454 0.2634 0.3925 0.0169  -0.0828 -0.0673 76 GLY A C   
603  O O   . GLY A 76 ? 0.3335 0.2788 0.3737 0.0104  -0.0749 -0.0539 76 GLY A O   
604  N N   . PHE A 77 ? 0.2848 0.2172 0.4274 0.0393  -0.1386 -0.0706 77 PHE A N   
605  C CA  . PHE A 77 ? 0.3006 0.2684 0.4293 0.0341  -0.1203 -0.0873 77 PHE A CA  
606  C C   . PHE A 77 ? 0.2885 0.2602 0.4007 0.0217  -0.1058 -0.0822 77 PHE A C   
607  O O   . PHE A 77 ? 0.2569 0.2383 0.3503 0.0130  -0.0935 -0.0750 77 PHE A O   
608  C CB  . PHE A 77 ? 0.3066 0.2979 0.4522 0.0455  -0.1139 -0.1149 77 PHE A CB  
609  C CG  . PHE A 77 ? 0.3499 0.3721 0.4898 0.0381  -0.0885 -0.1270 77 PHE A CG  
610  C CD1 . PHE A 77 ? 0.3175 0.3445 0.4371 0.0276  -0.0686 -0.1325 77 PHE A CD1 
611  C CD2 . PHE A 77 ? 0.2488 0.2911 0.4050 0.0429  -0.0861 -0.1358 77 PHE A CD2 
612  C CE1 . PHE A 77 ? 0.2691 0.3123 0.3860 0.0183  -0.0412 -0.1439 77 PHE A CE1 
613  C CE2 . PHE A 77 ? 0.1909 0.2605 0.3583 0.0317  -0.0598 -0.1492 77 PHE A CE2 
614  C CZ  . PHE A 77 ? 0.2053 0.2709 0.3535 0.0171  -0.0348 -0.1515 77 PHE A CZ  
615  N N   . ASN A 78 ? 0.2750 0.2406 0.3963 0.0241  -0.1113 -0.0897 78 ASN A N   
616  C CA  . ASN A 78 ? 0.2182 0.1900 0.3198 0.0200  -0.1062 -0.0923 78 ASN A CA  
617  C C   . ASN A 78 ? 0.2850 0.2494 0.3911 0.0097  -0.1084 -0.0720 78 ASN A C   
618  O O   . ASN A 78 ? 0.2113 0.1834 0.2959 0.0074  -0.1043 -0.0697 78 ASN A O   
619  C CB  . ASN A 78 ? 0.2575 0.2312 0.3706 0.0294  -0.1159 -0.1121 78 ASN A CB  
620  C CG  . ASN A 78 ? 0.3277 0.3158 0.4369 0.0385  -0.1099 -0.1343 78 ASN A CG  
621  O OD1 . ASN A 78 ? 0.2800 0.2793 0.3703 0.0360  -0.0934 -0.1382 78 ASN A OD1 
622  N ND2 . ASN A 78 ? 0.3101 0.3006 0.4455 0.0481  -0.1215 -0.1516 78 ASN A ND2 
623  N N   . GLU A 79 ? 0.2261 0.1739 0.3614 0.0035  -0.1148 -0.0566 79 GLU A N   
624  C CA  . GLU A 79 ? 0.2374 0.1833 0.3823 -0.0096 -0.1094 -0.0367 79 GLU A CA  
625  C C   . GLU A 79 ? 0.2104 0.1711 0.3214 -0.0104 -0.0946 -0.0249 79 GLU A C   
626  O O   . GLU A 79 ? 0.2388 0.2106 0.3455 -0.0149 -0.0879 -0.0196 79 GLU A O   
627  C CB  . GLU A 79 ? 0.3046 0.2231 0.4771 -0.0170 -0.1063 -0.0142 79 GLU A CB  
628  C CG  . GLU A 79 ? 0.2435 0.1653 0.4266 -0.0304 -0.0881 0.0078  79 GLU A CG  
629  C CD  . GLU A 79 ? 0.3522 0.2453 0.5637 -0.0389 -0.0746 0.0300  79 GLU A CD  
630  O OE1 . GLU A 79 ? 0.4662 0.3317 0.6736 -0.0308 -0.0800 0.0365  79 GLU A OE1 
631  O OE2 . GLU A 79 ? 0.4325 0.3341 0.6673 -0.0513 -0.0551 0.0390  79 GLU A OE2 
632  N N   . GLY A 80 ? 0.2157 0.1791 0.3096 -0.0035 -0.0908 -0.0250 80 GLY A N   
633  C CA  . GLY A 80 ? 0.2111 0.1912 0.2840 -0.0038 -0.0770 -0.0216 80 GLY A CA  
634  C C   . GLY A 80 ? 0.1859 0.1759 0.2458 -0.0062 -0.0662 -0.0320 80 GLY A C   
635  O O   . GLY A 80 ? 0.2317 0.2278 0.2830 -0.0098 -0.0541 -0.0248 80 GLY A O   
636  N N   . LEU A 81 ? 0.2600 0.2479 0.3140 -0.0019 -0.0684 -0.0485 81 LEU A N   
637  C CA  . LEU A 81 ? 0.2231 0.2094 0.2483 -0.0004 -0.0547 -0.0513 81 LEU A CA  
638  C C   . LEU A 81 ? 0.2436 0.2242 0.2588 0.0013  -0.0624 -0.0388 81 LEU A C   
639  O O   . LEU A 81 ? 0.2402 0.2149 0.2336 0.0030  -0.0499 -0.0293 81 LEU A O   
640  C CB  . LEU A 81 ? 0.2218 0.2062 0.2315 0.0078  -0.0556 -0.0711 81 LEU A CB  
641  C CG  . LEU A 81 ? 0.2572 0.2530 0.2808 0.0072  -0.0404 -0.0899 81 LEU A CG  
642  C CD1 . LEU A 81 ? 0.3115 0.3085 0.3179 0.0162  -0.0370 -0.1123 81 LEU A CD1 
643  C CD2 . LEU A 81 ? 0.2983 0.2989 0.3215 -0.0016 -0.0097 -0.0863 81 LEU A CD2 
644  N N   . TRP A 82 ? 0.2012 0.1827 0.2404 0.0015  -0.0830 -0.0414 82 TRP A N   
645  C CA  . TRP A 82 ? 0.2494 0.2343 0.2960 0.0044  -0.0940 -0.0379 82 TRP A CA  
646  C C   . TRP A 82 ? 0.2203 0.2114 0.2790 -0.0036 -0.0801 -0.0205 82 TRP A C   
647  O O   . TRP A 82 ? 0.2187 0.2101 0.2664 0.0026  -0.0790 -0.0161 82 TRP A O   
648  C CB  . TRP A 82 ? 0.2575 0.2462 0.3475 0.0025  -0.1122 -0.0497 82 TRP A CB  
649  C CG  . TRP A 82 ? 0.2279 0.2268 0.3369 0.0074  -0.1214 -0.0539 82 TRP A CG  
650  C CD1 . TRP A 82 ? 0.2711 0.2726 0.3640 0.0253  -0.1386 -0.0709 82 TRP A CD1 
651  C CD2 . TRP A 82 ? 0.1955 0.2059 0.3434 -0.0029 -0.1135 -0.0442 82 TRP A CD2 
652  N NE1 . TRP A 82 ? 0.2480 0.2615 0.3720 0.0274  -0.1449 -0.0745 82 TRP A NE1 
653  C CE2 . TRP A 82 ? 0.2694 0.2901 0.4308 0.0089  -0.1278 -0.0591 82 TRP A CE2 
654  C CE3 . TRP A 82 ? 0.2223 0.2362 0.3930 -0.0194 -0.0946 -0.0259 82 TRP A CE3 
655  C CZ2 . TRP A 82 ? 0.2429 0.2799 0.4478 0.0035  -0.1226 -0.0593 82 TRP A CZ2 
656  C CZ3 . TRP A 82 ? 0.1868 0.2168 0.3946 -0.0256 -0.0850 -0.0234 82 TRP A CZ3 
657  C CH2 . TRP A 82 ? 0.1864 0.2290 0.4152 -0.0147 -0.0989 -0.0416 82 TRP A CH2 
658  N N   . GLU A 83 ? 0.2104 0.2046 0.2866 -0.0136 -0.0704 -0.0113 83 GLU A N   
659  C CA  . GLU A 83 ? 0.2276 0.2314 0.3101 -0.0189 -0.0560 0.0008  83 GLU A CA  
660  C C   . GLU A 83 ? 0.1672 0.1717 0.2272 -0.0149 -0.0439 -0.0003 83 GLU A C   
661  O O   . GLU A 83 ? 0.1674 0.1769 0.2335 -0.0136 -0.0385 0.0027  83 GLU A O   
662  C CB  . GLU A 83 ? 0.1772 0.1795 0.2614 -0.0233 -0.0486 0.0114  83 GLU A CB  
663  C CG  . GLU A 83 ? 0.1894 0.1807 0.3020 -0.0300 -0.0524 0.0189  83 GLU A CG  
664  C CD  . GLU A 83 ? 0.2533 0.2292 0.3536 -0.0296 -0.0438 0.0377  83 GLU A CD  
665  O OE1 . GLU A 83 ? 0.2544 0.2334 0.3213 -0.0197 -0.0431 0.0387  83 GLU A OE1 
666  O OE2 . GLU A 83 ? 0.2572 0.2149 0.3824 -0.0375 -0.0381 0.0509  83 GLU A OE2 
667  N N   . ILE A 84 ? 0.1923 0.1918 0.2362 -0.0138 -0.0371 -0.0073 84 ILE A N   
668  C CA  . ILE A 84 ? 0.1784 0.1765 0.2172 -0.0148 -0.0197 -0.0105 84 ILE A CA  
669  C C   . ILE A 84 ? 0.2268 0.2048 0.2462 -0.0085 -0.0153 -0.0031 84 ILE A C   
670  O O   . ILE A 84 ? 0.2010 0.1707 0.2232 -0.0081 -0.0025 0.0003  84 ILE A O   
671  C CB  . ILE A 84 ? 0.1658 0.1680 0.2086 -0.0173 -0.0103 -0.0256 84 ILE A CB  
672  C CG1 . ILE A 84 ? 0.2035 0.2099 0.2635 -0.0222 0.0086  -0.0357 84 ILE A CG1 
673  C CG2 . ILE A 84 ? 0.2142 0.2018 0.2376 -0.0148 -0.0056 -0.0287 84 ILE A CG2 
674  C CD1 . ILE A 84 ? 0.1358 0.1619 0.2229 -0.0244 0.0121  -0.0609 84 ILE A CD1 
675  N N   . GLN A 85 ? 0.2363 0.2037 0.2334 0.0003  -0.0283 -0.0017 85 GLN A N   
676  C CA  . GLN A 85 ? 0.2901 0.2335 0.2518 0.0146  -0.0286 0.0076  85 GLN A CA  
677  C C   . GLN A 85 ? 0.3166 0.2669 0.2939 0.0249  -0.0501 0.0098  85 GLN A C   
678  O O   . GLN A 85 ? 0.2775 0.2079 0.2360 0.0386  -0.0500 0.0196  85 GLN A O   
679  C CB  . GLN A 85 ? 0.3064 0.2378 0.2261 0.0261  -0.0352 0.0030  85 GLN A CB  
680  C CG  . GLN A 85 ? 0.4826 0.3853 0.3465 0.0495  -0.0412 0.0148  85 GLN A CG  
681  C CD  . GLN A 85 ? 0.5899 0.4769 0.3942 0.0624  -0.0361 0.0115  85 GLN A CD  
682  O OE1 . GLN A 85 ? 0.6806 0.5311 0.4205 0.0779  -0.0189 0.0295  85 GLN A OE1 
683  N NE2 . GLN A 85 ? 0.5104 0.4209 0.3324 0.0579  -0.0484 -0.0109 85 GLN A NE2 
684  N N   . ASN A 86 ? 0.2297 0.2061 0.2471 0.0187  -0.0663 0.0005  86 ASN A N   
685  C CA  . ASN A 86 ? 0.2103 0.2012 0.2575 0.0279  -0.0875 -0.0060 86 ASN A CA  
686  C C   . ASN A 86 ? 0.2103 0.2243 0.3064 0.0164  -0.0767 -0.0059 86 ASN A C   
687  O O   . ASN A 86 ? 0.2096 0.2355 0.3332 0.0262  -0.0879 -0.0124 86 ASN A O   
688  C CB  . ASN A 86 ? 0.2113 0.2160 0.2809 0.0302  -0.1126 -0.0235 86 ASN A CB  
689  C CG  . ASN A 86 ? 0.2836 0.2705 0.2991 0.0498  -0.1288 -0.0302 86 ASN A CG  
690  O OD1 . ASN A 86 ? 0.3528 0.3352 0.3533 0.0449  -0.1255 -0.0362 86 ASN A OD1 
691  N ND2 . ASN A 86 ? 0.2868 0.2603 0.2648 0.0753  -0.1443 -0.0282 86 ASN A ND2 
692  N N   . ASN A 87 ? 0.1647 0.1868 0.2694 -0.0003 -0.0563 -0.0008 87 ASN A N   
693  C CA  . ASN A 87 ? 0.1893 0.2327 0.3253 -0.0077 -0.0412 -0.0006 87 ASN A CA  
694  C C   . ASN A 87 ? 0.1995 0.2436 0.3154 -0.0156 -0.0223 0.0042  87 ASN A C   
695  O O   . ASN A 87 ? 0.2311 0.2845 0.3513 -0.0235 -0.0133 0.0099  87 ASN A O   
696  C CB  . ASN A 87 ? 0.1409 0.2053 0.3253 -0.0169 -0.0423 -0.0046 87 ASN A CB  
697  C CG  . ASN A 87 ? 0.1974 0.2884 0.4227 -0.0189 -0.0284 -0.0106 87 ASN A CG  
698  O OD1 . ASN A 87 ? 0.1655 0.2602 0.3766 -0.0160 -0.0143 -0.0100 87 ASN A OD1 
699  N ND2 . ASN A 87 ? 0.1835 0.2950 0.4654 -0.0244 -0.0304 -0.0214 87 ASN A ND2 
700  N N   . PRO A 88 ? 0.1696 0.2020 0.2641 -0.0119 -0.0160 0.0010  88 PRO A N   
701  C CA  . PRO A 88 ? 0.1432 0.1819 0.2256 -0.0158 -0.0064 -0.0043 88 PRO A CA  
702  C C   . PRO A 88 ? 0.1971 0.2589 0.2860 -0.0153 0.0044  -0.0099 88 PRO A C   
703  O O   . PRO A 88 ? 0.1640 0.2350 0.2355 -0.0128 0.0060  -0.0152 88 PRO A O   
704  C CB  . PRO A 88 ? 0.1614 0.1839 0.2388 -0.0145 0.0006  -0.0124 88 PRO A CB  
705  C CG  . PRO A 88 ? 0.1614 0.1667 0.2430 -0.0075 0.0009  -0.0062 88 PRO A CG  
706  C CD  . PRO A 88 ? 0.1759 0.1856 0.2589 -0.0028 -0.0167 0.0015  88 PRO A CD  
707  N N   . HIS A 89 ? 0.1319 0.2050 0.2430 -0.0137 0.0104  -0.0123 89 HIS A N   
708  C CA  . HIS A 89 ? 0.1363 0.2342 0.2517 -0.0112 0.0247  -0.0225 89 HIS A CA  
709  C C   . HIS A 89 ? 0.1542 0.2691 0.2773 -0.0163 0.0379  -0.0116 89 HIS A C   
710  O O   . HIS A 89 ? 0.1485 0.2863 0.2726 -0.0136 0.0557  -0.0194 89 HIS A O   
711  C CB  . HIS A 89 ? 0.1148 0.2147 0.2584 -0.0049 0.0273  -0.0384 89 HIS A CB  
712  C CG  . HIS A 89 ? 0.1628 0.2395 0.3054 -0.0032 0.0244  -0.0470 89 HIS A CG  
713  N ND1 . HIS A 89 ? 0.1759 0.2587 0.3098 -0.0046 0.0267  -0.0627 89 HIS A ND1 
714  C CD2 . HIS A 89 ? 0.1515 0.1965 0.3023 0.0002  0.0220  -0.0419 89 HIS A CD2 
715  C CE1 . HIS A 89 ? 0.1980 0.2567 0.3477 -0.0073 0.0307  -0.0695 89 HIS A CE1 
716  N NE2 . HIS A 89 ? 0.1679 0.1985 0.3211 -0.0043 0.0306  -0.0526 89 HIS A NE2 
717  N N   . ALA A 90 ? 0.1874 0.2915 0.3198 -0.0244 0.0333  0.0038  90 ALA A N   
718  C CA  . ALA A 90 ? 0.1717 0.2870 0.3261 -0.0344 0.0525  0.0146  90 ALA A CA  
719  C C   . ALA A 90 ? 0.2115 0.3225 0.3177 -0.0334 0.0727  0.0311  90 ALA A C   
720  O O   . ALA A 90 ? 0.2597 0.3597 0.3183 -0.0229 0.0618  0.0320  90 ALA A O   
721  C CB  . ALA A 90 ? 0.1878 0.2896 0.3745 -0.0438 0.0402  0.0213  90 ALA A CB  
722  N N   . SER A 91 ? 0.2099 0.3291 0.3296 -0.0427 0.1030  0.0435  91 SER A N   
723  C CA  . SER A 91 ? 0.3855 0.4882 0.4494 -0.0402 0.1270  0.0697  91 SER A CA  
724  C C   . SER A 91 ? 0.4076 0.4731 0.4798 -0.0503 0.1225  0.0937  91 SER A C   
725  O O   . SER A 91 ? 0.4446 0.5097 0.5829 -0.0686 0.1305  0.0941  91 SER A O   
726  C CB  . SER A 91 ? 0.4035 0.5271 0.4753 -0.0470 0.1723  0.0754  91 SER A CB  
727  O OG  . SER A 91 ? 0.5166 0.6092 0.5360 -0.0481 0.1976  0.1088  91 SER A OG  
728  N N   . TYR A 92 ? 0.4307 0.4675 0.4458 -0.0369 0.1059  0.1075  92 TYR A N   
729  C CA  . TYR A 92 ? 0.3753 0.3718 0.3969 -0.0431 0.1017  0.1300  92 TYR A CA  
730  C C   . TYR A 92 ? 0.6039 0.5649 0.5715 -0.0385 0.1335  0.1698  92 TYR A C   
731  O O   . TYR A 92 ? 0.7134 0.6310 0.6654 -0.0350 0.1247  0.1895  92 TYR A O   
732  C CB  . TYR A 92 ? 0.4181 0.4033 0.4235 -0.0298 0.0609  0.1172  92 TYR A CB  
733  C CG  . TYR A 92 ? 0.3901 0.3966 0.4450 -0.0367 0.0383  0.0874  92 TYR A CG  
734  C CD1 . TYR A 92 ? 0.4442 0.4422 0.5529 -0.0494 0.0288  0.0819  92 TYR A CD1 
735  C CD2 . TYR A 92 ? 0.3389 0.3704 0.3848 -0.0284 0.0273  0.0644  92 TYR A CD2 
736  C CE1 . TYR A 92 ? 0.4144 0.4281 0.5501 -0.0489 0.0069  0.0571  92 TYR A CE1 
737  C CE2 . TYR A 92 ? 0.2344 0.2740 0.3114 -0.0314 0.0111  0.0452  92 TYR A CE2 
738  C CZ  . TYR A 92 ? 0.3976 0.4282 0.5113 -0.0393 0.0002  0.0432  92 TYR A CZ  
739  O OH  . TYR A 92 ? 0.3365 0.3715 0.4634 -0.0358 -0.0170 0.0267  92 TYR A OH  
740  N N   . SER A 93 ? 0.7066 0.6839 0.6445 -0.0371 0.1646  0.1732  93 SER A N   
741  C CA  . SER A 93 ? 0.8106 0.7586 0.6926 -0.0335 0.1902  0.1995  93 SER A CA  
742  C C   . SER A 93 ? 1.0193 0.9237 0.8230 -0.0081 0.1683  0.2222  93 SER A C   
743  O O   . SER A 93 ? 1.1240 0.9836 0.9297 -0.0139 0.1718  0.2461  93 SER A O   
744  C CB  . SER A 93 ? 0.8303 0.7620 0.7772 -0.0619 0.2163  0.2091  93 SER A CB  
745  O OG  . SER A 93 ? 0.8524 0.7630 0.8573 -0.0728 0.1938  0.2046  93 SER A OG  
746  N N   . MET B 1  ? 0.4948 0.8384 0.8574 0.2049  0.3025  0.1069  1  MET B N   
747  C CA  . MET B 1  ? 0.5283 0.8583 0.8657 0.1872  0.3231  0.1114  1  MET B CA  
748  C C   . MET B 1  ? 0.4955 0.7661 0.7671 0.1731  0.3129  0.1035  1  MET B C   
749  O O   . MET B 1  ? 0.5641 0.8293 0.8422 0.1607  0.2903  0.1002  1  MET B O   
750  C CB  . MET B 1  ? 0.4954 0.8852 0.9065 0.1606  0.3267  0.1264  1  MET B CB  
751  N N   . PRO B 2  ? 0.5308 0.7593 0.7393 0.1761  0.3286  0.1003  2  PRO B N   
752  C CA  . PRO B 2  ? 0.5227 0.6956 0.6673 0.1650  0.3167  0.0924  2  PRO B CA  
753  C C   . PRO B 2  ? 0.4931 0.6764 0.6612 0.1343  0.3115  0.1033  2  PRO B C   
754  O O   . PRO B 2  ? 0.5033 0.7172 0.7072 0.1210  0.3264  0.1178  2  PRO B O   
755  C CB  . PRO B 2  ? 0.5768 0.7146 0.6568 0.1773  0.3341  0.0877  2  PRO B CB  
756  C CG  . PRO B 2  ? 0.6146 0.7835 0.7187 0.1975  0.3567  0.0905  2  PRO B CG  
757  C CD  . PRO B 2  ? 0.5861 0.8131 0.7730 0.1973  0.3543  0.0995  2  PRO B CD  
758  N N   . HIS B 3  ? 0.5379 0.6938 0.6875 0.1229  0.2910  0.0962  3  HIS B N   
759  C CA  . HIS B 3  ? 0.4710 0.6274 0.6391 0.0943  0.2843  0.1035  3  HIS B CA  
760  C C   . HIS B 3  ? 0.4718 0.5715 0.5696 0.0906  0.2789  0.0987  3  HIS B C   
761  O O   . HIS B 3  ? 0.4920 0.5570 0.5312 0.1075  0.2781  0.0889  3  HIS B O   
762  C CB  . HIS B 3  ? 0.4528 0.6354 0.6716 0.0825  0.2642  0.0994  3  HIS B CB  
763  C CG  . HIS B 3  ? 0.5010 0.7481 0.7978 0.0824  0.2630  0.1054  3  HIS B CG  
764  N ND1 . HIS B 3  ? 0.5733 0.8558 0.9067 0.0808  0.2814  0.1172  3  HIS B ND1 
765  C CD2 . HIS B 3  ? 0.5278 0.8141 0.8738 0.0846  0.2434  0.1021  3  HIS B CD2 
766  C CE1 . HIS B 3  ? 0.5120 0.8528 0.9158 0.0806  0.2724  0.1197  3  HIS B CE1 
767  N NE2 . HIS B 3  ? 0.5599 0.9048 0.9720 0.0833  0.2474  0.1108  3  HIS B NE2 
768  N N   . ALA B 4  ? 0.4330 0.5236 0.5404 0.0673  0.2734  0.1052  4  ALA B N   
769  C CA  . ALA B 4  ? 0.4435 0.4857 0.4915 0.0644  0.2660  0.1030  4  ALA B CA  
770  C C   . ALA B 4  ? 0.4885 0.5000 0.4951 0.0747  0.2482  0.0853  4  ALA B C   
771  O O   . ALA B 4  ? 0.5601 0.5354 0.5090 0.0822  0.2419  0.0790  4  ALA B O   
772  C CB  . ALA B 4  ? 0.4309 0.4669 0.5040 0.0389  0.2613  0.1121  4  ALA B CB  
773  N N   . PHE B 5  ? 0.3975 0.4253 0.4353 0.0739  0.2384  0.0776  5  PHE B N   
774  C CA  . PHE B 5  ? 0.3888 0.3890 0.3928 0.0827  0.2172  0.0614  5  PHE B CA  
775  C C   . PHE B 5  ? 0.4774 0.4931 0.4909 0.1062  0.2231  0.0573  5  PHE B C   
776  O O   . PHE B 5  ? 0.3923 0.4531 0.4592 0.1101  0.2319  0.0651  5  PHE B O   
777  C CB  . PHE B 5  ? 0.3567 0.3584 0.3820 0.0642  0.1891  0.0542  5  PHE B CB  
778  C CG  . PHE B 5  ? 0.3946 0.3698 0.4022 0.0469  0.1815  0.0542  5  PHE B CG  
779  C CD1 . PHE B 5  ? 0.4211 0.3599 0.3827 0.0490  0.1690  0.0463  5  PHE B CD1 
780  C CD2 . PHE B 5  ? 0.4282 0.4146 0.4692 0.0290  0.1881  0.0636  5  PHE B CD2 
781  C CE1 . PHE B 5  ? 0.4262 0.3446 0.3770 0.0367  0.1627  0.0481  5  PHE B CE1 
782  C CE2 . PHE B 5  ? 0.4117 0.3697 0.4385 0.0165  0.1823  0.0648  5  PHE B CE2 
783  C CZ  . PHE B 5  ? 0.3636 0.2897 0.3454 0.0222  0.1696  0.0573  5  PHE B CZ  
784  N N   . LYS B 6  ? 0.4169 0.3948 0.3827 0.1210  0.2165  0.0454  6  LYS B N   
785  C CA  . LYS B 6  ? 0.4351 0.4165 0.4066 0.1431  0.2187  0.0411  6  LYS B CA  
786  C C   . LYS B 6  ? 0.4323 0.3886 0.3910 0.1495  0.2002  0.0326  6  LYS B C   
787  O O   . LYS B 6  ? 0.4177 0.3435 0.3467 0.1346  0.1827  0.0264  6  LYS B O   
788  C CB  . LYS B 6  ? 0.4855 0.4404 0.4136 0.1550  0.2284  0.0345  6  LYS B CB  
789  C CG  . LYS B 6  ? 0.5617 0.4640 0.4369 0.1590  0.2138  0.0186  6  LYS B CG  
790  C CD  . LYS B 6  ? 0.6713 0.5516 0.5103 0.1734  0.2232  0.0085  6  LYS B CD  
791  C CE  . LYS B 6  ? 0.6330 0.5139 0.4434 0.1668  0.2326  0.0116  6  LYS B CE  
792  N NZ  . LYS B 6  ? 0.6679 0.5211 0.4437 0.1504  0.2142  0.0075  6  LYS B NZ  
793  N N   . PRO B 7  ? 0.4314 0.4015 0.4157 0.1682  0.1983  0.0346  7  PRO B N   
794  C CA  . PRO B 7  ? 0.4572 0.3978 0.4260 0.1718  0.1770  0.0307  7  PRO B CA  
795  C C   . PRO B 7  ? 0.4614 0.3411 0.3720 0.1706  0.1743  0.0173  7  PRO B C   
796  O O   . PRO B 7  ? 0.5186 0.3786 0.4034 0.1755  0.1822  0.0095  7  PRO B O   
797  C CB  . PRO B 7  ? 0.4819 0.4416 0.4824 0.2002  0.1837  0.0372  7  PRO B CB  
798  C CG  . PRO B 7  ? 0.5096 0.5326 0.5649 0.1999  0.1958  0.0475  7  PRO B CG  
799  C CD  . PRO B 7  ? 0.4386 0.4539 0.4706 0.1834  0.2105  0.0436  7  PRO B CD  
800  N N   . GLY B 8  ? 0.4544 0.3117 0.3488 0.1543  0.1541  0.0154  8  GLY B N   
801  C CA  . GLY B 8  ? 0.5268 0.3325 0.3757 0.1485  0.1481  0.0035  8  GLY B CA  
802  C C   . GLY B 8  ? 0.5905 0.3911 0.4162 0.1287  0.1447  -0.0012 8  GLY B C   
803  O O   . GLY B 8  ? 0.5517 0.3174 0.3467 0.1197  0.1341  -0.0101 8  GLY B O   
804  N N   . ASP B 9  ? 0.4386 0.2732 0.2819 0.1215  0.1528  0.0059  9  ASP B N   
805  C CA  . ASP B 9  ? 0.4594 0.2896 0.2852 0.1046  0.1486  0.0059  9  ASP B CA  
806  C C   . ASP B 9  ? 0.4233 0.2483 0.2545 0.0872  0.1278  0.0059  9  ASP B C   
807  O O   . ASP B 9  ? 0.4210 0.2642 0.2793 0.0836  0.1199  0.0104  9  ASP B O   
808  C CB  . ASP B 9  ? 0.4353 0.3004 0.2879 0.0987  0.1615  0.0174  9  ASP B CB  
809  C CG  . ASP B 9  ? 0.5716 0.4420 0.4114 0.1098  0.1819  0.0208  9  ASP B CG  
810  O OD1 . ASP B 9  ? 0.5883 0.4351 0.3944 0.1195  0.1807  0.0117  9  ASP B OD1 
811  O OD2 . ASP B 9  ? 0.4419 0.3420 0.3096 0.1051  0.1958  0.0333  9  ASP B OD2 
812  N N   . LEU B 10 ? 0.4101 0.2138 0.2151 0.0775  0.1189  0.0012  10 LEU B N   
813  C CA  . LEU B 10 ? 0.4360 0.2377 0.2481 0.0627  0.1029  0.0018  10 LEU B CA  
814  C C   . LEU B 10 ? 0.3954 0.2147 0.2206 0.0522  0.1027  0.0078  10 LEU B C   
815  O O   . LEU B 10 ? 0.3930 0.2110 0.2054 0.0535  0.1096  0.0111  10 LEU B O   
816  C CB  . LEU B 10 ? 0.4535 0.2248 0.2388 0.0579  0.0915  -0.0064 10 LEU B CB  
817  C CG  . LEU B 10 ? 0.4707 0.2120 0.2397 0.0677  0.0923  -0.0149 10 LEU B CG  
818  C CD1 . LEU B 10 ? 0.4809 0.1922 0.2311 0.0565  0.0776  -0.0242 10 LEU B CD1 
819  C CD2 . LEU B 10 ? 0.4471 0.1954 0.2404 0.0736  0.0936  -0.0072 10 LEU B CD2 
820  N N   . VAL B 11 ? 0.3626 0.1956 0.2101 0.0430  0.0956  0.0094  11 VAL B N   
821  C CA  . VAL B 11 ? 0.3271 0.1722 0.1915 0.0343  0.0966  0.0127  11 VAL B CA  
822  C C   . VAL B 11 ? 0.3658 0.2117 0.2369 0.0263  0.0868  0.0096  11 VAL B C   
823  O O   . VAL B 11 ? 0.3655 0.2078 0.2309 0.0260  0.0807  0.0076  11 VAL B O   
824  C CB  . VAL B 11 ? 0.3343 0.2023 0.2279 0.0325  0.1037  0.0150  11 VAL B CB  
825  C CG1 . VAL B 11 ? 0.3326 0.2073 0.2271 0.0409  0.1190  0.0212  11 VAL B CG1 
826  C CG2 . VAL B 11 ? 0.3102 0.1937 0.2177 0.0324  0.0952  0.0106  11 VAL B CG2 
827  N N   . PHE B 12 ? 0.3703 0.2193 0.2539 0.0207  0.0878  0.0104  12 PHE B N   
828  C CA  . PHE B 12 ? 0.3605 0.2160 0.2566 0.0154  0.0840  0.0045  12 PHE B CA  
829  C C   . PHE B 12 ? 0.3507 0.2176 0.2666 0.0108  0.0865  -0.0005 12 PHE B C   
830  O O   . PHE B 12 ? 0.3604 0.2262 0.2891 0.0083  0.0932  0.0040  12 PHE B O   
831  C CB  . PHE B 12 ? 0.3694 0.2177 0.2691 0.0146  0.0833  0.0065  12 PHE B CB  
832  C CG  . PHE B 12 ? 0.4084 0.2536 0.2970 0.0159  0.0766  0.0098  12 PHE B CG  
833  C CD1 . PHE B 12 ? 0.4487 0.2852 0.3222 0.0184  0.0727  0.0153  12 PHE B CD1 
834  C CD2 . PHE B 12 ? 0.3721 0.2246 0.2650 0.0134  0.0742  0.0072  12 PHE B CD2 
835  C CE1 . PHE B 12 ? 0.4559 0.2908 0.3225 0.0162  0.0625  0.0156  12 PHE B CE1 
836  C CE2 . PHE B 12 ? 0.4565 0.3090 0.3479 0.0107  0.0677  0.0110  12 PHE B CE2 
837  C CZ  . PHE B 12 ? 0.4011 0.2446 0.2811 0.0110  0.0599  0.0139  12 PHE B CZ  
838  N N   . ALA B 13 ? 0.2934 0.1723 0.2115 0.0087  0.0806  -0.0088 13 ALA B N   
839  C CA  . ALA B 13 ? 0.3280 0.2212 0.2646 0.0020  0.0774  -0.0173 13 ALA B CA  
840  C C   . ALA B 13 ? 0.3527 0.2416 0.2884 -0.0030 0.0742  -0.0315 13 ALA B C   
841  O O   . ALA B 13 ? 0.3249 0.2137 0.2419 0.0012  0.0728  -0.0345 13 ALA B O   
842  C CB  . ALA B 13 ? 0.3216 0.2361 0.2581 0.0060  0.0699  -0.0165 13 ALA B CB  
843  N N   . LYS B 14 ? 0.3450 0.2287 0.3009 -0.0119 0.0750  -0.0403 14 LYS B N   
844  C CA  . LYS B 14 ? 0.3348 0.2052 0.2893 -0.0151 0.0746  -0.0572 14 LYS B CA  
845  C C   . LYS B 14 ? 0.3521 0.2370 0.3079 -0.0236 0.0623  -0.0764 14 LYS B C   
846  O O   . LYS B 14 ? 0.3673 0.2625 0.3487 -0.0346 0.0567  -0.0789 14 LYS B O   
847  C CB  . LYS B 14 ? 0.3462 0.1912 0.3218 -0.0191 0.0834  -0.0554 14 LYS B CB  
848  C CG  . LYS B 14 ? 0.3725 0.1958 0.3481 -0.0187 0.0857  -0.0742 14 LYS B CG  
849  C CD  . LYS B 14 ? 0.3999 0.2240 0.3542 -0.0044 0.0907  -0.0735 14 LYS B CD  
850  C CE  . LYS B 14 ? 0.4483 0.2489 0.4066 0.0009  0.0981  -0.0901 14 LYS B CE  
851  N NZ  . LYS B 14 ? 0.4258 0.2282 0.3687 -0.0045 0.0920  -0.1176 14 LYS B NZ  
852  N N   . MET B 15 ? 0.3918 0.2798 0.3202 -0.0189 0.0583  -0.0897 15 MET B N   
853  C CA  . MET B 15 ? 0.3978 0.2950 0.3153 -0.0254 0.0453  -0.1133 15 MET B CA  
854  C C   . MET B 15 ? 0.4934 0.3646 0.3996 -0.0243 0.0521  -0.1357 15 MET B C   
855  O O   . MET B 15 ? 0.4861 0.3449 0.3815 -0.0126 0.0663  -0.1302 15 MET B O   
856  C CB  . MET B 15 ? 0.4351 0.3577 0.3185 -0.0171 0.0363  -0.1103 15 MET B CB  
857  C CG  . MET B 15 ? 0.5012 0.4460 0.3903 -0.0122 0.0310  -0.0874 15 MET B CG  
858  S SD  . MET B 15 ? 0.5674 0.5347 0.4989 -0.0249 0.0170  -0.0904 15 MET B SD  
859  C CE  . MET B 15 ? 0.4956 0.4953 0.4052 -0.0258 -0.0086 -0.1052 15 MET B CE  
860  N N   . LYS B 16 ? 0.5036 0.3681 0.4137 -0.0361 0.0410  -0.1625 16 LYS B N   
861  C CA  . LYS B 16 ? 0.5076 0.3420 0.4039 -0.0340 0.0473  -0.1899 16 LYS B CA  
862  C C   . LYS B 16 ? 0.5212 0.3646 0.3713 -0.0169 0.0555  -0.1937 16 LYS B C   
863  O O   . LYS B 16 ? 0.5545 0.4266 0.3747 -0.0141 0.0457  -0.1906 16 LYS B O   
864  C CB  . LYS B 16 ? 0.5518 0.3804 0.4532 -0.0518 0.0289  -0.2223 16 LYS B CB  
865  C CG  . LYS B 16 ? 0.6228 0.4123 0.5101 -0.0501 0.0339  -0.2552 16 LYS B CG  
866  C CD  . LYS B 16 ? 0.7001 0.4842 0.5982 -0.0708 0.0102  -0.2814 16 LYS B CD  
867  C CE  . LYS B 16 ? 0.9494 0.6852 0.8654 -0.0734 0.0144  -0.2920 16 LYS B CE  
868  N NZ  . LYS B 16 ? 0.8791 0.5895 0.7577 -0.0496 0.0275  -0.3016 16 LYS B NZ  
869  N N   . GLY B 17 ? 0.5618 0.3833 0.4092 -0.0040 0.0749  -0.1965 17 GLY B N   
870  C CA  . GLY B 17 ? 0.6304 0.4636 0.4405 0.0124  0.0877  -0.1981 17 GLY B CA  
871  C C   . GLY B 17 ? 0.6049 0.4625 0.4141 0.0205  0.0964  -0.1647 17 GLY B C   
872  O O   . GLY B 17 ? 0.6128 0.4844 0.3945 0.0319  0.1088  -0.1618 17 GLY B O   
873  N N   . TYR B 18 ? 0.4788 0.3413 0.3166 0.0145  0.0912  -0.1400 18 TYR B N   
874  C CA  . TYR B 18 ? 0.4431 0.3216 0.2841 0.0196  0.0971  -0.1111 18 TYR B CA  
875  C C   . TYR B 18 ? 0.4714 0.3373 0.3474 0.0196  0.1016  -0.0952 18 TYR B C   
876  O O   . TYR B 18 ? 0.4575 0.3075 0.3546 0.0129  0.0966  -0.0978 18 TYR B O   
877  C CB  . TYR B 18 ? 0.4558 0.3536 0.2862 0.0143  0.0833  -0.0971 18 TYR B CB  
878  C CG  . TYR B 18 ? 0.5478 0.4622 0.3394 0.0165  0.0765  -0.1069 18 TYR B CG  
879  C CD1 . TYR B 18 ? 0.4564 0.3842 0.2191 0.0251  0.0864  -0.0942 18 TYR B CD1 
880  C CD2 . TYR B 18 ? 0.5737 0.4914 0.3570 0.0092  0.0597  -0.1285 18 TYR B CD2 
881  C CE1 . TYR B 18 ? 0.4979 0.4412 0.2175 0.0291  0.0806  -0.1006 18 TYR B CE1 
882  C CE2 . TYR B 18 ? 0.6432 0.5786 0.3848 0.0122  0.0498  -0.1383 18 TYR B CE2 
883  C CZ  . TYR B 18 ? 0.5306 0.4780 0.2370 0.0236  0.0608  -0.1234 18 TYR B CZ  
884  O OH  . TYR B 18 ? 0.6256 0.5909 0.2842 0.0282  0.0510  -0.1302 18 TYR B OH  
885  N N   . PRO B 19 ? 0.4321 0.3065 0.3152 0.0261  0.1101  -0.0772 19 PRO B N   
886  C CA  . PRO B 19 ? 0.4401 0.3072 0.3499 0.0261  0.1092  -0.0606 19 PRO B CA  
887  C C   . PRO B 19 ? 0.3639 0.2318 0.2734 0.0177  0.0979  -0.0490 19 PRO B C   
888  O O   . PRO B 19 ? 0.3670 0.2461 0.2605 0.0142  0.0917  -0.0477 19 PRO B O   
889  C CB  . PRO B 19 ? 0.4640 0.3477 0.3800 0.0321  0.1168  -0.0464 19 PRO B CB  
890  C CG  . PRO B 19 ? 0.3769 0.2773 0.2670 0.0314  0.1207  -0.0472 19 PRO B CG  
891  C CD  . PRO B 19 ? 0.4761 0.3697 0.3441 0.0326  0.1206  -0.0703 19 PRO B CD  
892  N N   . HIS B 20 ? 0.3431 0.1995 0.2694 0.0169  0.0964  -0.0393 20 HIS B N   
893  C CA  . HIS B 20 ? 0.3474 0.2051 0.2713 0.0123  0.0900  -0.0275 20 HIS B CA  
894  C C   . HIS B 20 ? 0.3881 0.2575 0.2975 0.0129  0.0867  -0.0190 20 HIS B C   
895  O O   . HIS B 20 ? 0.3887 0.2625 0.3001 0.0152  0.0885  -0.0127 20 HIS B O   
896  C CB  . HIS B 20 ? 0.3651 0.2108 0.3000 0.0146  0.0910  -0.0149 20 HIS B CB  
897  C CG  . HIS B 20 ? 0.3479 0.1760 0.2996 0.0137  0.0960  -0.0182 20 HIS B CG  
898  N ND1 . HIS B 20 ? 0.3768 0.1935 0.3406 0.0201  0.1015  -0.0245 20 HIS B ND1 
899  C CD2 . HIS B 20 ? 0.3433 0.1617 0.3054 0.0070  0.0981  -0.0156 20 HIS B CD2 
900  C CE1 . HIS B 20 ? 0.3734 0.1681 0.3524 0.0170  0.1055  -0.0259 20 HIS B CE1 
901  N NE2 . HIS B 20 ? 0.3546 0.1514 0.3342 0.0074  0.1036  -0.0196 20 HIS B NE2 
902  N N   . TRP B 21 ? 0.3545 0.2293 0.2539 0.0108  0.0818  -0.0182 21 TRP B N   
903  C CA  . TRP B 21 ? 0.3374 0.2184 0.2222 0.0121  0.0796  -0.0111 21 TRP B CA  
904  C C   . TRP B 21 ? 0.3362 0.2090 0.2176 0.0132  0.0760  -0.0020 21 TRP B C   
905  O O   . TRP B 21 ? 0.3455 0.2187 0.2313 0.0146  0.0750  -0.0031 21 TRP B O   
906  C CB  . TRP B 21 ? 0.3238 0.2176 0.1959 0.0129  0.0762  -0.0173 21 TRP B CB  
907  C CG  . TRP B 21 ? 0.3734 0.2725 0.2281 0.0154  0.0778  -0.0075 21 TRP B CG  
908  C CD1 . TRP B 21 ? 0.3696 0.2635 0.2180 0.0175  0.0750  0.0063  21 TRP B CD1 
909  C CD2 . TRP B 21 ? 0.4202 0.3282 0.2616 0.0168  0.0855  -0.0088 21 TRP B CD2 
910  N NE1 . TRP B 21 ? 0.3700 0.2676 0.2038 0.0183  0.0797  0.0164  21 TRP B NE1 
911  C CE2 . TRP B 21 ? 0.4004 0.3098 0.2286 0.0180  0.0872  0.0080  21 TRP B CE2 
912  C CE3 . TRP B 21 ? 0.3675 0.2807 0.2061 0.0186  0.0932  -0.0225 21 TRP B CE3 
913  C CZ2 . TRP B 21 ? 0.3818 0.3014 0.1941 0.0196  0.0976  0.0146  21 TRP B CZ2 
914  C CZ3 . TRP B 21 ? 0.4289 0.3534 0.2495 0.0224  0.1041  -0.0193 21 TRP B CZ3 
915  C CH2 . TRP B 21 ? 0.4293 0.3589 0.2367 0.0223  0.1069  0.0006  21 TRP B CH2 
916  N N   . PRO B 22 ? 0.3380 0.2028 0.2132 0.0125  0.0749  0.0059  22 PRO B N   
917  C CA  . PRO B 22 ? 0.3621 0.2122 0.2296 0.0151  0.0718  0.0098  22 PRO B CA  
918  C C   . PRO B 22 ? 0.3390 0.1929 0.2023 0.0218  0.0712  0.0117  22 PRO B C   
919  O O   . PRO B 22 ? 0.3906 0.2527 0.2493 0.0232  0.0698  0.0157  22 PRO B O   
920  C CB  . PRO B 22 ? 0.3316 0.1705 0.1962 0.0098  0.0693  0.0154  22 PRO B CB  
921  C CG  . PRO B 22 ? 0.3386 0.1926 0.2083 0.0064  0.0740  0.0197  22 PRO B CG  
922  C CD  . PRO B 22 ? 0.3614 0.2303 0.2378 0.0088  0.0775  0.0110  22 PRO B CD  
923  N N   . ALA B 23 ? 0.3140 0.1647 0.1788 0.0278  0.0729  0.0106  23 ALA B N   
924  C CA  . ALA B 23 ? 0.3177 0.1803 0.1881 0.0363  0.0722  0.0132  23 ALA B CA  
925  C C   . ALA B 23 ? 0.3435 0.1960 0.2128 0.0459  0.0783  0.0137  23 ALA B C   
926  O O   . ALA B 23 ? 0.3596 0.1951 0.2173 0.0449  0.0821  0.0105  23 ALA B O   
927  C CB  . ALA B 23 ? 0.3107 0.1996 0.1980 0.0322  0.0699  0.0079  23 ALA B CB  
928  N N   . ARG B 24 ? 0.3334 0.1989 0.2135 0.0570  0.0792  0.0177  24 ARG B N   
929  C CA  . ARG B 24 ? 0.3467 0.2080 0.2293 0.0700  0.0891  0.0177  24 ARG B CA  
930  C C   . ARG B 24 ? 0.3380 0.2366 0.2519 0.0760  0.0912  0.0215  24 ARG B C   
931  O O   . ARG B 24 ? 0.3295 0.2523 0.2582 0.0731  0.0801  0.0240  24 ARG B O   
932  C CB  . ARG B 24 ? 0.3941 0.2260 0.2613 0.0830  0.0901  0.0198  24 ARG B CB  
933  C CG  . ARG B 24 ? 0.3816 0.2251 0.2611 0.0939  0.0837  0.0307  24 ARG B CG  
934  C CD  . ARG B 24 ? 0.4189 0.2239 0.2847 0.1073  0.0860  0.0346  24 ARG B CD  
935  N NE  . ARG B 24 ? 0.4281 0.2434 0.3041 0.1193  0.0791  0.0500  24 ARG B NE  
936  C CZ  . ARG B 24 ? 0.4768 0.2585 0.3426 0.1275  0.0777  0.0604  24 ARG B CZ  
937  N NH1 . ARG B 24 ? 0.4979 0.2311 0.3455 0.1224  0.0820  0.0539  24 ARG B NH1 
938  N NH2 . ARG B 24 ? 0.4732 0.2693 0.3475 0.1407  0.0706  0.0785  24 ARG B NH2 
939  N N   . ILE B 25 ? 0.3637 0.2696 0.2875 0.0841  0.1053  0.0218  25 ILE B N   
940  C CA  . ILE B 25 ? 0.3407 0.2862 0.3027 0.0919  0.1096  0.0274  25 ILE B CA  
941  C C   . ILE B 25 ? 0.4091 0.3528 0.3740 0.1138  0.1085  0.0330  25 ILE B C   
942  O O   . ILE B 25 ? 0.3852 0.2975 0.3287 0.1286  0.1193  0.0307  25 ILE B O   
943  C CB  . ILE B 25 ? 0.3591 0.3159 0.3329 0.0943  0.1302  0.0290  25 ILE B CB  
944  C CG1 . ILE B 25 ? 0.3371 0.2854 0.3023 0.0754  0.1333  0.0274  25 ILE B CG1 
945  C CG2 . ILE B 25 ? 0.3406 0.3474 0.3661 0.1004  0.1351  0.0366  25 ILE B CG2 
946  C CD1 . ILE B 25 ? 0.3440 0.3112 0.3349 0.0555  0.1200  0.0255  25 ILE B CD1 
947  N N   . ASP B 26 ? 0.3943 0.5901 0.2915 0.1372  0.1234  0.0492  26 ASP B N   
948  C CA  . ASP B 26 ? 0.4475 0.6425 0.3995 0.1472  0.1126  0.0828  26 ASP B CA  
949  C C   . ASP B 26 ? 0.4214 0.6481 0.4699 0.1811  0.1341  0.1152  26 ASP B C   
950  O O   . ASP B 26 ? 0.4017 0.6687 0.4863 0.1801  0.1457  0.1248  26 ASP B O   
951  C CB  . ASP B 26 ? 0.4160 0.6382 0.3752 0.1077  0.0601  0.1074  26 ASP B CB  
952  C CG  . ASP B 26 ? 0.4341 0.6298 0.3233 0.0864  0.0394  0.0941  26 ASP B CG  
953  O OD1 . ASP B 26 ? 0.4513 0.6010 0.2895 0.1030  0.0655  0.0679  26 ASP B OD1 
954  O OD2 . ASP B 26 ? 0.4340 0.6580 0.3189 0.0518  -0.0034 0.1121  26 ASP B OD2 
955  N N   . ASP B 27 ? 0.4544 0.6644 0.5397 0.2122  0.1361  0.1321  27 ASP B N   
956  C CA  . ASP B 27 ? 0.5134 0.7722 0.6947 0.2469  0.1461  0.1671  27 ASP B CA  
957  C C   . ASP B 27 ? 0.4941 0.7994 0.7323 0.2158  0.1030  0.2088  27 ASP B C   
958  O O   . ASP B 27 ? 0.4857 0.7698 0.6903 0.1790  0.0641  0.2116  27 ASP B O   
959  C CB  . ASP B 27 ? 0.5244 0.7415 0.7152 0.3028  0.1587  0.1639  27 ASP B CB  
960  C CG  . ASP B 27 ? 0.6711 0.9141 0.8971 0.3328  0.1866  0.1580  27 ASP B CG  
961  O OD1 . ASP B 27 ? 0.6111 0.9300 0.8992 0.3246  0.1890  0.1847  27 ASP B OD1 
962  O OD2 . ASP B 27 ? 0.6851 0.8712 0.8674 0.3500  0.1959  0.1251  27 ASP B OD2 
963  N N   . ILE B 28 ? 0.4548 0.8329 0.7797 0.2288  0.1097  0.2431  28 ILE B N   
964  C CA  . ILE B 28 ? 0.4498 0.8782 0.8394 0.2046  0.0712  0.2865  28 ILE B CA  
965  C C   . ILE B 28 ? 0.5198 0.9429 0.9551 0.2481  0.0643  0.3052  28 ILE B C   
966  O O   . ILE B 28 ? 0.5569 1.0092 1.0355 0.3015  0.0935  0.3085  28 ILE B O   
967  C CB  . ILE B 28 ? 0.4137 0.9280 0.8705 0.1902  0.0763  0.3185  28 ILE B CB  
968  C CG1 . ILE B 28 ? 0.4490 0.9463 0.8460 0.1445  0.0679  0.2986  28 ILE B CG1 
969  C CG2 . ILE B 28 ? 0.4126 0.9810 0.9410 0.1697  0.0382  0.3652  28 ILE B CG2 
970  C CD1 . ILE B 28 ? 0.4930 0.9986 0.8749 0.1599  0.1101  0.2810  28 ILE B CD1 
971  N N   . ALA B 29 ? 0.5712 0.9535 0.9869 0.2261  0.0225  0.3137  29 ALA B N   
972  C CA  . ALA B 29 ? 0.5680 0.9231 1.0113 0.2661  0.0057  0.3286  29 ALA B CA  
973  C C   . ALA B 29 ? 0.5836 1.0238 1.1270 0.2923  0.0051  0.3661  29 ALA B C   
974  O O   . ALA B 29 ? 0.5503 1.0595 1.1347 0.2554  0.0010  0.3883  29 ALA B O   
975  C CB  . ALA B 29 ? 0.5932 0.8932 0.9946 0.2249  -0.0453 0.3369  29 ALA B CB  
976  N N   . ASP B 30 ? 0.7827 1.1975 1.3353 0.3433  0.0064  0.3575  30 ASP B N   
977  C CA  . ASP B 30 ? 0.7412 1.2241 1.3583 0.3620  0.0057  0.3753  30 ASP B CA  
978  C C   . ASP B 30 ? 0.7285 1.2376 1.3840 0.3181  -0.0362 0.4129  30 ASP B C   
979  O O   . ASP B 30 ? 0.7549 1.2028 1.3875 0.3069  -0.0762 0.4194  30 ASP B O   
980  C CB  . ASP B 30 ? 0.8270 1.2663 1.4335 0.4294  0.0024  0.3519  30 ASP B CB  
981  N N   . GLY B 31 ? 0.6245 1.2189 1.3301 0.2873  -0.0297 0.4380  31 GLY B N   
982  C CA  . GLY B 31 ? 0.5908 1.2107 1.3273 0.2401  -0.0652 0.4697  31 GLY B CA  
983  C C   . GLY B 31 ? 0.5373 1.1544 1.2481 0.1724  -0.0819 0.4761  31 GLY B C   
984  O O   . GLY B 31 ? 0.5299 1.1753 1.2625 0.1299  -0.1042 0.4993  31 GLY B O   
985  N N   . ALA B 32 ? 0.5283 1.1093 1.1865 0.1645  -0.0726 0.4524  32 ALA B N   
986  C CA  . ALA B 32 ? 0.5108 1.0780 1.1249 0.1074  -0.0970 0.4473  32 ALA B CA  
987  C C   . ALA B 32 ? 0.5839 1.1992 1.2142 0.0741  -0.0921 0.4592  32 ALA B C   
988  O O   . ALA B 32 ? 0.5109 1.1763 1.1841 0.0919  -0.0648 0.4736  32 ALA B O   
989  C CB  . ALA B 32 ? 0.4999 1.0196 1.0458 0.1145  -0.0886 0.4160  32 ALA B CB  
990  N N   . VAL B 33 ? 0.6649 1.2588 1.2487 0.0244  -0.1226 0.4510  33 VAL B N   
991  C CA  . VAL B 33 ? 0.6006 1.2133 1.1788 -0.0104 -0.1305 0.4587  33 VAL B CA  
992  C C   . VAL B 33 ? 0.6024 1.2218 1.1590 0.0023  -0.1056 0.4408  33 VAL B C   
993  O O   . VAL B 33 ? 0.5318 1.1232 1.0441 0.0216  -0.0943 0.4101  33 VAL B O   
994  C CB  . VAL B 33 ? 0.6780 1.2473 1.1950 -0.0565 -0.1709 0.4429  33 VAL B CB  
995  C CG1 . VAL B 33 ? 0.7030 1.2282 1.1494 -0.0551 -0.1793 0.4048  33 VAL B CG1 
996  C CG2 . VAL B 33 ? 0.6778 1.2381 1.1615 -0.0864 -0.1855 0.4372  33 VAL B CG2 
997  N N   . LYS B 34 ? 0.4952 1.1541 1.0803 -0.0117 -0.0980 0.4634  34 LYS B N   
998  C CA  . LYS B 34 ? 0.4395 1.1099 1.0085 -0.0061 -0.0754 0.4514  34 LYS B CA  
999  C C   . LYS B 34 ? 0.3873 1.0122 0.8824 -0.0454 -0.1150 0.4284  34 LYS B C   
1000 O O   . LYS B 34 ? 0.4160 1.0057 0.8792 -0.0815 -0.1572 0.4289  34 LYS B O   
1001 C CB  . LYS B 34 ? 0.4051 1.1380 1.0279 -0.0091 -0.0558 0.4888  34 LYS B CB  
1002 N N   . PRO B 35 ? 0.4022 0.9804 0.8269 -0.0361 -0.0919 0.3872  35 PRO B N   
1003 C CA  . PRO B 35 ? 0.4004 0.9168 0.7323 -0.0664 -0.1299 0.3548  35 PRO B CA  
1004 C C   . PRO B 35 ? 0.4262 0.9604 0.7790 -0.1080 -0.1671 0.3921  35 PRO B C   
1005 O O   . PRO B 35 ? 0.4251 1.0268 0.8575 -0.1128 -0.1475 0.4387  35 PRO B O   
1006 C CB  . PRO B 35 ? 0.3972 0.8664 0.6596 -0.0385 -0.0859 0.3047  35 PRO B CB  
1007 C CG  . PRO B 35 ? 0.3786 0.8641 0.6763 0.0047  -0.0366 0.3001  35 PRO B CG  
1008 C CD  . PRO B 35 ? 0.4248 0.9897 0.8353 0.0093  -0.0327 0.3580  35 PRO B CD  
1009 N N   . PRO B 36 ? 0.4593 0.9317 0.7350 -0.1379 -0.2215 0.3706  36 PRO B N   
1010 C CA  . PRO B 36 ? 0.5100 0.9592 0.7782 -0.1801 -0.2552 0.3946  36 PRO B CA  
1011 C C   . PRO B 36 ? 0.5084 0.9820 0.7846 -0.1816 -0.2334 0.4101  36 PRO B C   
1012 O O   . PRO B 36 ? 0.4852 0.9444 0.7336 -0.1436 -0.1791 0.3713  36 PRO B O   
1013 C CB  . PRO B 36 ? 0.5604 0.8963 0.7129 -0.1857 -0.2914 0.3310  36 PRO B CB  
1014 C CG  . PRO B 36 ? 0.5402 0.8649 0.6636 -0.1552 -0.2779 0.2882  36 PRO B CG  
1015 C CD  . PRO B 36 ? 0.5212 0.9147 0.6948 -0.1283 -0.2369 0.3048  36 PRO B CD  
1016 N N   . PRO B 37 ? 0.5451 1.0389 0.8478 -0.2257 -0.2630 0.4582  37 PRO B N   
1017 C CA  . PRO B 37 ? 0.5560 1.0629 0.8572 -0.2300 -0.2292 0.4669  37 PRO B CA  
1018 C C   . PRO B 37 ? 0.5746 0.9788 0.7576 -0.2114 -0.2263 0.3985  37 PRO B C   
1019 O O   . PRO B 37 ? 0.6266 0.9426 0.7169 -0.2172 -0.2797 0.3581  37 PRO B O   
1020 C CB  . PRO B 37 ? 0.6094 1.1374 0.9365 -0.2959 -0.2867 0.5313  37 PRO B CB  
1021 C CG  . PRO B 37 ? 0.6592 1.0983 0.9393 -0.3151 -0.3329 0.5118  37 PRO B CG  
1022 C CD  . PRO B 37 ? 0.6035 1.0713 0.9148 -0.2721 -0.3044 0.4900  37 PRO B CD  
1023 N N   . ASN B 38 ? 0.5524 0.9747 0.7382 -0.1832 -0.1628 0.3831  38 ASN B N   
1024 C CA  . ASN B 38 ? 0.5652 0.9046 0.6499 -0.1628 -0.1476 0.3223  38 ASN B CA  
1025 C C   . ASN B 38 ? 0.5349 0.8255 0.5559 -0.1164 -0.1271 0.2538  38 ASN B C   
1026 O O   . ASN B 38 ? 0.5439 0.7695 0.4765 -0.0968 -0.1153 0.1995  38 ASN B O   
1027 C CB  . ASN B 38 ? 0.6393 0.8852 0.6301 -0.2038 -0.2208 0.3126  38 ASN B CB  
1028 C CG  . ASN B 38 ? 0.7018 0.9862 0.7428 -0.2635 -0.2558 0.3860  38 ASN B CG  
1029 O OD1 . ASN B 38 ? 0.6752 1.0224 0.7643 -0.2710 -0.2133 0.4185  38 ASN B OD1 
1030 N ND2 . ASN B 38 ? 0.7480 1.0023 0.7787 -0.3079 -0.3353 0.4153  38 ASN B ND2 
1031 N N   . LYS B 39 ? 0.4851 0.4822 0.5435 0.0030  0.0569  0.0668  39 LYS B N   
1032 C CA  . LYS B 39 ? 0.4564 0.4421 0.4721 0.0043  0.0494  0.0530  39 LYS B CA  
1033 C C   . LYS B 39 ? 0.4845 0.4695 0.4944 0.0177  0.0604  0.0590  39 LYS B C   
1034 O O   . LYS B 39 ? 0.4191 0.4155 0.4611 0.0249  0.0707  0.0737  39 LYS B O   
1035 C CB  . LYS B 39 ? 0.4934 0.4890 0.5038 -0.0101 0.0249  0.0464  39 LYS B CB  
1036 C CG  . LYS B 39 ? 0.4838 0.4778 0.5040 -0.0256 0.0140  0.0364  39 LYS B CG  
1037 C CD  . LYS B 39 ? 0.4880 0.4659 0.4683 -0.0340 0.0057  0.0146  39 LYS B CD  
1038 C CE  . LYS B 39 ? 0.5599 0.5285 0.5519 -0.0478 0.0007  0.0012  39 LYS B CE  
1039 N NZ  . LYS B 39 ? 0.6492 0.6129 0.6120 -0.0625 -0.0153 -0.0190 39 LYS B NZ  
1040 N N   . TYR B 40 ? 0.3470 0.3171 0.3212 0.0212  0.0605  0.0469  40 TYR B N   
1041 C CA  . TYR B 40 ? 0.3910 0.3544 0.3582 0.0324  0.0710  0.0478  40 TYR B CA  
1042 C C   . TYR B 40 ? 0.4603 0.4261 0.4160 0.0287  0.0585  0.0462  40 TYR B C   
1043 O O   . TYR B 40 ? 0.4039 0.3672 0.3384 0.0195  0.0469  0.0368  40 TYR B O   
1044 C CB  . TYR B 40 ? 0.4163 0.3577 0.3531 0.0399  0.0838  0.0349  40 TYR B CB  
1045 C CG  . TYR B 40 ? 0.4166 0.3527 0.3531 0.0456  0.0995  0.0383  40 TYR B CG  
1046 C CD1 . TYR B 40 ? 0.3570 0.2910 0.2885 0.0406  0.0970  0.0386  40 TYR B CD1 
1047 C CD2 . TYR B 40 ? 0.4452 0.3761 0.3859 0.0565  0.1197  0.0420  40 TYR B CD2 
1048 C CE1 . TYR B 40 ? 0.4249 0.3541 0.3540 0.0464  0.1133  0.0460  40 TYR B CE1 
1049 C CE2 . TYR B 40 ? 0.4647 0.3895 0.3980 0.0622  0.1377  0.0462  40 TYR B CE2 
1050 C CZ  . TYR B 40 ? 0.4374 0.3624 0.3639 0.0571  0.1340  0.0499  40 TYR B CZ  
1051 O OH  . TYR B 40 ? 0.4467 0.3654 0.3631 0.0633  0.1538  0.0580  40 TYR B OH  
1052 N N   . PRO B 41 ? 0.3817 0.3504 0.3518 0.0363  0.0637  0.0561  41 PRO B N   
1053 C CA  . PRO B 41 ? 0.3910 0.3596 0.3499 0.0346  0.0559  0.0583  41 PRO B CA  
1054 C C   . PRO B 41 ? 0.3974 0.3440 0.3297 0.0372  0.0641  0.0414  41 PRO B C   
1055 O O   . PRO B 41 ? 0.4171 0.3495 0.3511 0.0454  0.0777  0.0346  41 PRO B O   
1056 C CB  . PRO B 41 ? 0.4078 0.3858 0.4028 0.0438  0.0619  0.0780  41 PRO B CB  
1057 C CG  . PRO B 41 ? 0.4284 0.3988 0.4418 0.0535  0.0818  0.0756  41 PRO B CG  
1058 C CD  . PRO B 41 ? 0.4245 0.3966 0.4274 0.0475  0.0798  0.0679  41 PRO B CD  
1059 N N   . ILE B 42 ? 0.4144 0.3580 0.3232 0.0295  0.0560  0.0335  42 ILE B N   
1060 C CA  . ILE B 42 ? 0.3640 0.2907 0.2556 0.0301  0.0615  0.0182  42 ILE B CA  
1061 C C   . ILE B 42 ? 0.3495 0.2748 0.2408 0.0301  0.0632  0.0245  42 ILE B C   
1062 O O   . ILE B 42 ? 0.3654 0.3023 0.2511 0.0255  0.0561  0.0365  42 ILE B O   
1063 C CB  . ILE B 42 ? 0.3875 0.3107 0.2608 0.0227  0.0562  0.0054  42 ILE B CB  
1064 C CG1 . ILE B 42 ? 0.3148 0.2398 0.1929 0.0221  0.0550  0.0040  42 ILE B CG1 
1065 C CG2 . ILE B 42 ? 0.4010 0.3105 0.2669 0.0239  0.0610  -0.0073 42 ILE B CG2 
1066 C CD1 . ILE B 42 ? 0.3143 0.2329 0.1975 0.0311  0.0644  0.0045  42 ILE B CD1 
1067 N N   . PHE B 43 ? 0.3262 0.2375 0.2230 0.0344  0.0720  0.0171  43 PHE B N   
1068 C CA  . PHE B 43 ? 0.3503 0.2577 0.2522 0.0340  0.0769  0.0232  43 PHE B CA  
1069 C C   . PHE B 43 ? 0.3315 0.2286 0.2267 0.0304  0.0794  0.0072  43 PHE B C   
1070 O O   . PHE B 43 ? 0.3441 0.2314 0.2448 0.0324  0.0796  -0.0066 43 PHE B O   
1071 C CB  . PHE B 43 ? 0.3678 0.2669 0.2970 0.0416  0.0864  0.0297  43 PHE B CB  
1072 C CG  . PHE B 43 ? 0.4186 0.3103 0.3610 0.0412  0.0941  0.0361  43 PHE B CG  
1073 C CD1 . PHE B 43 ? 0.3886 0.2897 0.3366 0.0420  0.0953  0.0606  43 PHE B CD1 
1074 C CD2 . PHE B 43 ? 0.4202 0.2966 0.3723 0.0396  0.0993  0.0198  43 PHE B CD2 
1075 C CE1 . PHE B 43 ? 0.4023 0.2960 0.3646 0.0420  0.1055  0.0704  43 PHE B CE1 
1076 C CE2 . PHE B 43 ? 0.3717 0.2414 0.3448 0.0386  0.1085  0.0273  43 PHE B CE2 
1077 C CZ  . PHE B 43 ? 0.3925 0.2698 0.3704 0.0402  0.1136  0.0532  43 PHE B CZ  
1078 N N   . PHE B 44 ? 0.3487 0.2486 0.2322 0.0253  0.0815  0.0097  44 PHE B N   
1079 C CA  . PHE B 44 ? 0.3578 0.2506 0.2434 0.0224  0.0865  -0.0029 44 PHE B CA  
1080 C C   . PHE B 44 ? 0.3884 0.2740 0.2988 0.0237  0.0963  0.0007  44 PHE B C   
1081 O O   . PHE B 44 ? 0.4066 0.2941 0.3181 0.0238  0.1044  0.0165  44 PHE B O   
1082 C CB  . PHE B 44 ? 0.3721 0.2684 0.2344 0.0165  0.0897  -0.0043 44 PHE B CB  
1083 C CG  . PHE B 44 ? 0.4109 0.3109 0.2556 0.0131  0.0804  -0.0120 44 PHE B CG  
1084 C CD1 . PHE B 44 ? 0.3663 0.2608 0.2181 0.0133  0.0789  -0.0256 44 PHE B CD1 
1085 C CD2 . PHE B 44 ? 0.4385 0.3481 0.2649 0.0092  0.0719  -0.0038 44 PHE B CD2 
1086 C CE1 . PHE B 44 ? 0.3975 0.2932 0.2395 0.0099  0.0724  -0.0312 44 PHE B CE1 
1087 C CE2 . PHE B 44 ? 0.4787 0.3909 0.2963 0.0043  0.0632  -0.0118 44 PHE B CE2 
1088 C CZ  . PHE B 44 ? 0.3862 0.2899 0.2121 0.0048  0.0652  -0.0257 44 PHE B CZ  
1089 N N   . PHE B 45 ? 0.3417 0.2196 0.2730 0.0240  0.0944  -0.0128 45 PHE B N   
1090 C CA  . PHE B 45 ? 0.3409 0.2115 0.3038 0.0231  0.1022  -0.0120 45 PHE B CA  
1091 C C   . PHE B 45 ? 0.3797 0.2535 0.3488 0.0198  0.1155  -0.0050 45 PHE B C   
1092 O O   . PHE B 45 ? 0.3716 0.2501 0.3240 0.0180  0.1173  -0.0093 45 PHE B O   
1093 C CB  . PHE B 45 ? 0.3373 0.2011 0.3190 0.0216  0.0921  -0.0304 45 PHE B CB  
1094 C CG  . PHE B 45 ? 0.3422 0.1975 0.3162 0.0248  0.0854  -0.0383 45 PHE B CG  
1095 C CD1 . PHE B 45 ? 0.3526 0.1979 0.3432 0.0273  0.0939  -0.0336 45 PHE B CD1 
1096 C CD2 . PHE B 45 ? 0.3411 0.1970 0.2919 0.0262  0.0739  -0.0490 45 PHE B CD2 
1097 C CE1 . PHE B 45 ? 0.3700 0.2044 0.3546 0.0311  0.0930  -0.0431 45 PHE B CE1 
1098 C CE2 . PHE B 45 ? 0.3534 0.1995 0.2923 0.0298  0.0729  -0.0569 45 PHE B CE2 
1099 C CZ  . PHE B 45 ? 0.3650 0.1996 0.3209 0.0323  0.0834  -0.0556 45 PHE B CZ  
1100 N N   . GLY B 46 ? 0.3588 0.2283 0.3541 0.0193  0.1281  0.0059  46 GLY B N   
1101 C CA  . GLY B 46 ? 0.3813 0.2529 0.3841 0.0168  0.1459  0.0145  46 GLY B CA  
1102 C C   . GLY B 46 ? 0.4284 0.3048 0.3917 0.0175  0.1564  0.0332  46 GLY B C   
1103 O O   . GLY B 46 ? 0.4124 0.2872 0.3832 0.0183  0.1705  0.0534  46 GLY B O   
1104 N N   . THR B 47 ? 0.3970 0.2789 0.3179 0.0164  0.1490  0.0272  47 THR B N   
1105 C CA  . THR B 47 ? 0.4241 0.3116 0.3001 0.0149  0.1522  0.0425  47 THR B CA  
1106 C C   . THR B 47 ? 0.4324 0.3258 0.3058 0.0181  0.1397  0.0606  47 THR B C   
1107 O O   . THR B 47 ? 0.4523 0.3517 0.3021 0.0180  0.1422  0.0827  47 THR B O   
1108 C CB  . THR B 47 ? 0.4396 0.3296 0.2752 0.0106  0.1454  0.0272  47 THR B CB  
1109 O OG1 . THR B 47 ? 0.4070 0.3008 0.2447 0.0114  0.1247  0.0187  47 THR B OG1 
1110 C CG2 . THR B 47 ? 0.4302 0.3131 0.2770 0.0092  0.1593  0.0091  47 THR B CG2 
1111 N N   . HIS B 48 ? 0.3991 0.2913 0.2959 0.0215  0.1270  0.0528  48 HIS B N   
1112 C CA  . HIS B 48 ? 0.4264 0.3241 0.3296 0.0261  0.1174  0.0680  48 HIS B CA  
1113 C C   . HIS B 48 ? 0.4764 0.3891 0.3429 0.0233  0.1034  0.0762  48 HIS B C   
1114 O O   . HIS B 48 ? 0.5012 0.4239 0.3708 0.0263  0.0962  0.0982  48 HIS B O   
1115 C CB  . HIS B 48 ? 0.4189 0.3131 0.3490 0.0306  0.1286  0.0927  48 HIS B CB  
1116 C CG  . HIS B 48 ? 0.4206 0.3000 0.3904 0.0306  0.1426  0.0849  48 HIS B CG  
1117 N ND1 . HIS B 48 ? 0.4825 0.3571 0.4728 0.0310  0.1596  0.1050  48 HIS B ND1 
1118 C CD2 . HIS B 48 ? 0.3899 0.2591 0.3844 0.0290  0.1404  0.0600  48 HIS B CD2 
1119 C CE1 . HIS B 48 ? 0.4587 0.3208 0.4907 0.0289  0.1675  0.0911  48 HIS B CE1 
1120 N NE2 . HIS B 48 ? 0.4418 0.3011 0.4749 0.0273  0.1541  0.0631  48 HIS B NE2 
1121 N N   . GLU B 49 ? 0.4232 0.3376 0.2598 0.0171  0.0983  0.0589  49 GLU B N   
1122 C CA  . GLU B 49 ? 0.4918 0.4191 0.2980 0.0119  0.0820  0.0618  49 GLU B CA  
1123 C C   . GLU B 49 ? 0.4520 0.3837 0.2793 0.0144  0.0696  0.0549  49 GLU B C   
1124 O O   . GLU B 49 ? 0.4481 0.3707 0.3012 0.0197  0.0746  0.0442  49 GLU B O   
1125 C CB  . GLU B 49 ? 0.5042 0.4274 0.2707 0.0031  0.0846  0.0443  49 GLU B CB  
1126 C CG  . GLU B 49 ? 0.5281 0.4456 0.2691 0.0011  0.1025  0.0513  49 GLU B CG  
1127 C CD  . GLU B 49 ? 0.6125 0.5249 0.3055 -0.0079 0.1068  0.0342  49 GLU B CD  
1128 O OE1 . GLU B 49 ? 0.6869 0.5938 0.3823 -0.0112 0.1028  0.0111  49 GLU B OE1 
1129 O OE2 . GLU B 49 ? 0.7245 0.6363 0.3767 -0.0115 0.1161  0.0438  49 GLU B OE2 
1130 N N   . THR B 50 ? 0.4177 0.3642 0.2331 0.0099  0.0532  0.0614  50 THR B N   
1131 C CA  . THR B 50 ? 0.4024 0.3555 0.2403 0.0119  0.0439  0.0584  50 THR B CA  
1132 C C   . THR B 50 ? 0.5367 0.4969 0.3527 0.0011  0.0300  0.0474  50 THR B C   
1133 O O   . THR B 50 ? 0.4891 0.4550 0.2723 -0.0081 0.0212  0.0488  50 THR B O   
1134 C CB  . THR B 50 ? 0.4296 0.3970 0.2980 0.0185  0.0380  0.0833  50 THR B CB  
1135 O OG1 . THR B 50 ? 0.4526 0.4375 0.3026 0.0125  0.0228  0.1029  50 THR B OG1 
1136 C CG2 . THR B 50 ? 0.4448 0.4004 0.3407 0.0290  0.0541  0.0916  50 THR B CG2 
1137 N N   . ALA B 51 ? 0.4514 0.4093 0.2842 0.0016  0.0290  0.0357  51 ALA B N   
1138 C CA  . ALA B 51 ? 0.3848 0.3480 0.2101 -0.0087 0.0168  0.0257  51 ALA B CA  
1139 C C   . ALA B 51 ? 0.3934 0.3614 0.2530 -0.0041 0.0166  0.0286  51 ALA B C   
1140 O O   . ALA B 51 ? 0.4381 0.4011 0.3173 0.0069  0.0283  0.0330  51 ALA B O   
1141 C CB  . ALA B 51 ? 0.4398 0.3859 0.2416 -0.0147 0.0239  0.0021  51 ALA B CB  
1142 N N   . PHE B 52 ? 0.4042 0.3806 0.2706 -0.0135 0.0048  0.0251  52 PHE B N   
1143 C CA  . PHE B 52 ? 0.4056 0.3850 0.3046 -0.0103 0.0084  0.0276  52 PHE B CA  
1144 C C   . PHE B 52 ? 0.4551 0.4174 0.3457 -0.0137 0.0151  0.0092  52 PHE B C   
1145 O O   . PHE B 52 ? 0.4295 0.3859 0.3027 -0.0249 0.0085  -0.0050 52 PHE B O   
1146 C CB  . PHE B 52 ? 0.4193 0.4218 0.3460 -0.0185 -0.0088 0.0402  52 PHE B CB  
1147 C CG  . PHE B 52 ? 0.4710 0.4938 0.4194 -0.0130 -0.0158 0.0643  52 PHE B CG  
1148 C CD1 . PHE B 52 ? 0.4419 0.4630 0.4157 0.0025  0.0014  0.0765  52 PHE B CD1 
1149 C CD2 . PHE B 52 ? 0.4701 0.5131 0.4141 -0.0234 -0.0400 0.0749  52 PHE B CD2 
1150 C CE1 . PHE B 52 ? 0.5047 0.5430 0.5072 0.0090  -0.0025 0.1002  52 PHE B CE1 
1151 C CE2 . PHE B 52 ? 0.5212 0.5850 0.4918 -0.0172 -0.0478 0.1019  52 PHE B CE2 
1152 C CZ  . PHE B 52 ? 0.4350 0.4961 0.4390 -0.0002 -0.0276 0.1152  52 PHE B CZ  
1153 N N   . LEU B 53 ? 0.3874 0.3404 0.2888 -0.0039 0.0288  0.0095  53 LEU B N   
1154 C CA  . LEU B 53 ? 0.4539 0.3919 0.3523 -0.0049 0.0349  -0.0019 53 LEU B CA  
1155 C C   . LEU B 53 ? 0.3960 0.3352 0.3165 0.0009  0.0433  0.0080  53 LEU B C   
1156 O O   . LEU B 53 ? 0.3757 0.3208 0.3055 0.0097  0.0510  0.0193  53 LEU B O   
1157 C CB  . LEU B 53 ? 0.3998 0.3225 0.2791 0.0017  0.0430  -0.0113 53 LEU B CB  
1158 C CG  . LEU B 53 ? 0.4316 0.3489 0.2909 -0.0039 0.0414  -0.0227 53 LEU B CG  
1159 C CD1 . LEU B 53 ? 0.3884 0.2934 0.2434 0.0031  0.0501  -0.0293 53 LEU B CD1 
1160 C CD2 . LEU B 53 ? 0.4613 0.3741 0.3167 -0.0159 0.0366  -0.0348 53 LEU B CD2 
1161 N N   . GLY B 54 ? 0.3524 0.2837 0.2813 -0.0036 0.0450  0.0040  54 GLY B N   
1162 C CA  . GLY B 54 ? 0.3375 0.2670 0.2831 0.0021  0.0559  0.0154  54 GLY B CA  
1163 C C   . GLY B 54 ? 0.3991 0.3134 0.3245 0.0115  0.0639  0.0137  54 GLY B C   
1164 O O   . GLY B 54 ? 0.3878 0.2936 0.2966 0.0120  0.0600  0.0025  54 GLY B O   
1165 N N   . PRO B 55 ? 0.4227 0.3346 0.3497 0.0191  0.0752  0.0264  55 PRO B N   
1166 C CA  . PRO B 55 ? 0.3937 0.2941 0.2949 0.0283  0.0787  0.0272  55 PRO B CA  
1167 C C   . PRO B 55 ? 0.3634 0.2538 0.2677 0.0262  0.0730  0.0235  55 PRO B C   
1168 O O   . PRO B 55 ? 0.3892 0.2737 0.2750 0.0324  0.0693  0.0222  55 PRO B O   
1169 C CB  . PRO B 55 ? 0.4022 0.3028 0.3011 0.0356  0.0938  0.0439  55 PRO B CB  
1170 C CG  . PRO B 55 ? 0.4604 0.3720 0.3975 0.0289  0.0987  0.0529  55 PRO B CG  
1171 C CD  . PRO B 55 ? 0.4301 0.3518 0.3790 0.0210  0.0862  0.0419  55 PRO B CD  
1172 N N   . LYS B 56 ? 0.3468 0.2345 0.2772 0.0175  0.0715  0.0212  56 LYS B N   
1173 C CA  . LYS B 56 ? 0.3826 0.2582 0.3218 0.0174  0.0696  0.0174  56 LYS B CA  
1174 C C   . LYS B 56 ? 0.3490 0.2221 0.2757 0.0175  0.0635  0.0013  56 LYS B C   
1175 O O   . LYS B 56 ? 0.3807 0.2461 0.3156 0.0211  0.0628  0.0003  56 LYS B O   
1176 C CB  . LYS B 56 ? 0.4025 0.2714 0.3748 0.0070  0.0719  0.0137  56 LYS B CB  
1177 C CG  . LYS B 56 ? 0.4489 0.3203 0.4218 -0.0057 0.0653  -0.0061 56 LYS B CG  
1178 C CD  . LYS B 56 ? 0.4859 0.3431 0.4846 -0.0170 0.0666  -0.0189 56 LYS B CD  
1179 C CE  . LYS B 56 ? 0.5415 0.3998 0.5255 -0.0303 0.0581  -0.0421 56 LYS B CE  
1180 N NZ  . LYS B 56 ? 0.5436 0.3933 0.5025 -0.0276 0.0610  -0.0581 56 LYS B NZ  
1181 N N   . ASP B 57 ? 0.3423 0.2225 0.2546 0.0143  0.0603  -0.0084 57 ASP B N   
1182 C CA  . ASP B 57 ? 0.3466 0.2249 0.2488 0.0141  0.0579  -0.0212 57 ASP B CA  
1183 C C   . ASP B 57 ? 0.3503 0.2331 0.2357 0.0216  0.0554  -0.0187 57 ASP B C   
1184 O O   . ASP B 57 ? 0.3557 0.2386 0.2364 0.0210  0.0546  -0.0270 57 ASP B O   
1185 C CB  . ASP B 57 ? 0.3342 0.2154 0.2304 0.0042  0.0565  -0.0326 57 ASP B CB  
1186 C CG  . ASP B 57 ? 0.4787 0.3503 0.3869 -0.0055 0.0584  -0.0438 57 ASP B CG  
1187 O OD1 . ASP B 57 ? 0.4329 0.2920 0.3558 -0.0031 0.0647  -0.0480 57 ASP B OD1 
1188 O OD2 . ASP B 57 ? 0.3875 0.2638 0.2934 -0.0158 0.0530  -0.0486 57 ASP B OD2 
1189 N N   . LEU B 58 ? 0.3382 0.2227 0.2139 0.0280  0.0559  -0.0084 58 LEU B N   
1190 C CA  . LEU B 58 ? 0.3393 0.2245 0.1965 0.0335  0.0543  -0.0103 58 LEU B CA  
1191 C C   . LEU B 58 ? 0.3971 0.2779 0.2423 0.0395  0.0485  -0.0059 58 LEU B C   
1192 O O   . LEU B 58 ? 0.3852 0.2645 0.2241 0.0428  0.0512  0.0063  58 LEU B O   
1193 C CB  . LEU B 58 ? 0.3786 0.2682 0.2291 0.0357  0.0619  -0.0049 58 LEU B CB  
1194 C CG  . LEU B 58 ? 0.3824 0.2807 0.2470 0.0297  0.0625  -0.0055 58 LEU B CG  
1195 C CD1 . LEU B 58 ? 0.3539 0.2592 0.2249 0.0332  0.0708  0.0044  58 LEU B CD1 
1196 C CD2 . LEU B 58 ? 0.3409 0.2389 0.2020 0.0281  0.0591  -0.0141 58 LEU B CD2 
1197 N N   . PHE B 59 ? 0.3503 0.2302 0.1938 0.0402  0.0397  -0.0140 59 PHE B N   
1198 C CA  . PHE B 59 ? 0.3853 0.2643 0.2202 0.0439  0.0273  -0.0105 59 PHE B CA  
1199 C C   . PHE B 59 ? 0.3844 0.2604 0.1950 0.0447  0.0213  -0.0205 59 PHE B C   
1200 O O   . PHE B 59 ? 0.3808 0.2564 0.2023 0.0414  0.0214  -0.0322 59 PHE B O   
1201 C CB  . PHE B 59 ? 0.3593 0.2412 0.2258 0.0426  0.0196  -0.0116 59 PHE B CB  
1202 C CG  . PHE B 59 ? 0.3515 0.2313 0.2431 0.0418  0.0277  -0.0053 59 PHE B CG  
1203 C CD1 . PHE B 59 ? 0.3376 0.2148 0.2389 0.0362  0.0394  -0.0141 59 PHE B CD1 
1204 C CD2 . PHE B 59 ? 0.3755 0.2545 0.2792 0.0462  0.0230  0.0098  59 PHE B CD2 
1205 C CE1 . PHE B 59 ? 0.3380 0.2095 0.2599 0.0336  0.0469  -0.0134 59 PHE B CE1 
1206 C CE2 . PHE B 59 ? 0.3643 0.2373 0.2966 0.0451  0.0327  0.0137  59 PHE B CE2 
1207 C CZ  . PHE B 59 ? 0.3604 0.2283 0.3010 0.0381  0.0450  -0.0004 59 PHE B CZ  
1208 N N   . PRO B 60 ? 0.4571 0.3289 0.2332 0.0483  0.0178  -0.0173 60 PRO B N   
1209 C CA  . PRO B 60 ? 0.4390 0.3035 0.1885 0.0476  0.0138  -0.0325 60 PRO B CA  
1210 C C   . PRO B 60 ? 0.4695 0.3370 0.2369 0.0425  -0.0054 -0.0434 60 PRO B C   
1211 O O   . PRO B 60 ? 0.4947 0.3706 0.2780 0.0420  -0.0214 -0.0356 60 PRO B O   
1212 C CB  . PRO B 60 ? 0.4833 0.3419 0.1853 0.0520  0.0128  -0.0264 60 PRO B CB  
1213 C CG  . PRO B 60 ? 0.5840 0.4466 0.2921 0.0562  0.0249  -0.0054 60 PRO B CG  
1214 C CD  . PRO B 60 ? 0.4921 0.3629 0.2491 0.0531  0.0234  -0.0003 60 PRO B CD  
1215 N N   . TYR B 61 ? 0.4823 0.3435 0.2548 0.0389  -0.0028 -0.0598 61 TYR B N   
1216 C CA  . TYR B 61 ? 0.4640 0.3291 0.2681 0.0328  -0.0165 -0.0692 61 TYR B CA  
1217 C C   . TYR B 61 ? 0.5053 0.3736 0.2975 0.0294  -0.0434 -0.0733 61 TYR B C   
1218 O O   . TYR B 61 ? 0.5383 0.4190 0.3663 0.0269  -0.0590 -0.0680 61 TYR B O   
1219 C CB  . TYR B 61 ? 0.4868 0.3420 0.3004 0.0297  -0.0062 -0.0838 61 TYR B CB  
1220 C CG  . TYR B 61 ? 0.4596 0.3171 0.3087 0.0223  -0.0189 -0.0938 61 TYR B CG  
1221 C CD1 . TYR B 61 ? 0.4935 0.3614 0.3874 0.0207  -0.0149 -0.0861 61 TYR B CD1 
1222 C CD2 . TYR B 61 ? 0.5922 0.4408 0.4307 0.0163  -0.0338 -0.1118 61 TYR B CD2 
1223 C CE1 . TYR B 61 ? 0.4608 0.3319 0.3946 0.0140  -0.0235 -0.0931 61 TYR B CE1 
1224 C CE2 . TYR B 61 ? 0.6155 0.4671 0.4948 0.0080  -0.0463 -0.1209 61 TYR B CE2 
1225 C CZ  . TYR B 61 ? 0.5567 0.4208 0.4868 0.0073  -0.0405 -0.1097 61 TYR B CZ  
1226 O OH  . TYR B 61 ? 0.4894 0.3575 0.4669 -0.0010 -0.0504 -0.1167 61 TYR B OH  
1227 N N   . ASP B 62 ? 0.5456 0.4033 0.2892 0.0289  -0.0496 -0.0834 62 ASP B N   
1228 C CA  . ASP B 62 ? 0.5687 0.4302 0.2977 0.0231  -0.0806 -0.0900 62 ASP B CA  
1229 C C   . ASP B 62 ? 0.5526 0.4294 0.2799 0.0272  -0.0977 -0.0664 62 ASP B C   
1230 O O   . ASP B 62 ? 0.6455 0.5358 0.3958 0.0227  -0.1259 -0.0630 62 ASP B O   
1231 C CB  . ASP B 62 ? 0.6709 0.5138 0.3388 0.0202  -0.0827 -0.1105 62 ASP B CB  
1232 C CG  . ASP B 62 ? 0.8669 0.6995 0.4842 0.0292  -0.0595 -0.1025 62 ASP B CG  
1233 O OD1 . ASP B 62 ? 0.8392 0.6797 0.4749 0.0364  -0.0429 -0.0814 62 ASP B OD1 
1234 O OD2 . ASP B 62 ? 0.9915 0.8071 0.5521 0.0285  -0.0564 -0.1184 62 ASP B OD2 
1235 N N   . LYS B 63 ? 0.5762 0.4523 0.2859 0.0355  -0.0811 -0.0480 63 LYS B N   
1236 C CA  . LYS B 63 ? 0.5510 0.4399 0.2697 0.0404  -0.0936 -0.0221 63 LYS B CA  
1237 C C   . LYS B 63 ? 0.5083 0.4111 0.2987 0.0402  -0.0975 -0.0136 63 LYS B C   
1238 O O   . LYS B 63 ? 0.5176 0.4341 0.3323 0.0417  -0.1186 0.0025  63 LYS B O   
1239 C CB  . LYS B 63 ? 0.7015 0.5845 0.3959 0.0485  -0.0705 -0.0044 63 LYS B CB  
1240 C CG  . LYS B 63 ? 0.5497 0.4429 0.2703 0.0546  -0.0748 0.0253  63 LYS B CG  
1241 C CD  . LYS B 63 ? 0.6355 0.5211 0.3386 0.0608  -0.0495 0.0416  63 LYS B CD  
1242 C CE  . LYS B 63 ? 0.5967 0.4887 0.3325 0.0665  -0.0507 0.0713  63 LYS B CE  
1243 N NZ  . LYS B 63 ? 0.6514 0.5535 0.3780 0.0697  -0.0789 0.0917  63 LYS B NZ  
1244 N N   . CYS B 64 ? 0.4768 0.3764 0.3019 0.0389  -0.0765 -0.0228 64 CYS B N   
1245 C CA  . CYS B 64 ? 0.4583 0.3665 0.3426 0.0403  -0.0700 -0.0146 64 CYS B CA  
1246 C C   . CYS B 64 ? 0.4442 0.3581 0.3739 0.0345  -0.0726 -0.0271 64 CYS B C   
1247 O O   . CYS B 64 ? 0.4162 0.3356 0.3941 0.0360  -0.0624 -0.0222 64 CYS B O   
1248 C CB  . CYS B 64 ? 0.4678 0.3679 0.3540 0.0431  -0.0415 -0.0124 64 CYS B CB  
1249 S SG  . CYS B 64 ? 0.5842 0.4792 0.4364 0.0495  -0.0350 0.0067  64 CYS B SG  
1250 N N   . LYS B 65 ? 0.4281 0.3391 0.3461 0.0278  -0.0833 -0.0435 65 LYS B N   
1251 C CA  . LYS B 65 ? 0.4182 0.3329 0.3837 0.0218  -0.0806 -0.0539 65 LYS B CA  
1252 C C   . LYS B 65 ? 0.4373 0.3703 0.4620 0.0208  -0.0979 -0.0444 65 LYS B C   
1253 O O   . LYS B 65 ? 0.4672 0.4051 0.5441 0.0194  -0.0848 -0.0451 65 LYS B O   
1254 C CB  . LYS B 65 ? 0.4352 0.3398 0.3800 0.0141  -0.0876 -0.0743 65 LYS B CB  
1255 C CG  . LYS B 65 ? 0.5442 0.4509 0.4616 0.0086  -0.1205 -0.0817 65 LYS B CG  
1256 C CD  . LYS B 65 ? 0.6294 0.5219 0.5350 -0.0007 -0.1240 -0.1072 65 LYS B CD  
1257 C CE  . LYS B 65 ? 0.6072 0.4991 0.4773 -0.0086 -0.1586 -0.1200 65 LYS B CE  
1258 N NZ  . LYS B 65 ? 0.7316 0.6128 0.6176 -0.0213 -0.1679 -0.1468 65 LYS B NZ  
1259 N N   . ASP B 66 ? 0.4332 0.3775 0.4537 0.0221  -0.1261 -0.0329 66 ASP B N   
1260 C CA  . ASP B 66 ? 0.4302 0.3953 0.5183 0.0221  -0.1437 -0.0201 66 ASP B CA  
1261 C C   . ASP B 66 ? 0.4136 0.3813 0.5448 0.0315  -0.1198 -0.0042 66 ASP B C   
1262 O O   . ASP B 66 ? 0.4244 0.4042 0.6249 0.0324  -0.1158 0.0012  66 ASP B O   
1263 C CB  . ASP B 66 ? 0.5512 0.5301 0.6229 0.0207  -0.1847 -0.0090 66 ASP B CB  
1264 C CG  . ASP B 66 ? 0.6728 0.6476 0.7048 0.0087  -0.2103 -0.0306 66 ASP B CG  
1265 O OD1 . ASP B 66 ? 0.6801 0.6420 0.7122 0.0022  -0.1947 -0.0526 66 ASP B OD1 
1266 O OD2 . ASP B 66 ? 0.7859 0.7695 0.7869 0.0054  -0.2461 -0.0256 66 ASP B OD2 
1267 N N   . LYS B 67 ? 0.4545 0.4095 0.5491 0.0382  -0.1014 0.0018  67 LYS B N   
1268 C CA  . LYS B 67 ? 0.4086 0.3606 0.5394 0.0455  -0.0766 0.0116  67 LYS B CA  
1269 C C   . LYS B 67 ? 0.3577 0.2995 0.5010 0.0429  -0.0443 -0.0039 67 LYS B C   
1270 O O   . LYS B 67 ? 0.3924 0.3370 0.5886 0.0455  -0.0276 -0.0022 67 LYS B O   
1271 C CB  . LYS B 67 ? 0.5223 0.4632 0.6125 0.0512  -0.0694 0.0221  67 LYS B CB  
1272 C CG  . LYS B 67 ? 0.5255 0.4593 0.6527 0.0574  -0.0454 0.0297  67 LYS B CG  
1273 C CD  . LYS B 67 ? 0.5977 0.5197 0.6887 0.0611  -0.0384 0.0395  67 LYS B CD  
1274 C CE  . LYS B 67 ? 0.5449 0.4559 0.6757 0.0657  -0.0147 0.0440  67 LYS B CE  
1275 N NZ  . LYS B 67 ? 0.6284 0.5490 0.8251 0.0736  -0.0218 0.0629  67 LYS B NZ  
1276 N N   . TYR B 68 ? 0.3480 0.2779 0.4429 0.0384  -0.0342 -0.0176 68 TYR B N   
1277 C CA  . TYR B 68 ? 0.3607 0.2802 0.4513 0.0364  -0.0049 -0.0283 68 TYR B CA  
1278 C C   . TYR B 68 ? 0.4440 0.3651 0.5479 0.0303  -0.0009 -0.0385 68 TYR B C   
1279 O O   . TYR B 68 ? 0.3591 0.2734 0.4620 0.0289  0.0233  -0.0436 68 TYR B O   
1280 C CB  . TYR B 68 ? 0.3308 0.2380 0.3654 0.0362  0.0041  -0.0317 68 TYR B CB  
1281 C CG  . TYR B 68 ? 0.3350 0.2377 0.3610 0.0411  0.0066  -0.0217 68 TYR B CG  
1282 C CD1 . TYR B 68 ? 0.3957 0.2959 0.4583 0.0443  0.0199  -0.0179 68 TYR B CD1 
1283 C CD2 . TYR B 68 ? 0.3784 0.2775 0.3632 0.0424  -0.0008 -0.0162 68 TYR B CD2 
1284 C CE1 . TYR B 68 ? 0.4064 0.2997 0.4678 0.0480  0.0235  -0.0090 68 TYR B CE1 
1285 C CE2 . TYR B 68 ? 0.3887 0.2833 0.3716 0.0462  0.0033  -0.0047 68 TYR B CE2 
1286 C CZ  . TYR B 68 ? 0.4250 0.3164 0.4475 0.0486  0.0143  -0.0012 68 TYR B CZ  
1287 O OH  . TYR B 68 ? 0.4511 0.3354 0.4769 0.0517  0.0191  0.0100  68 TYR B OH  
1288 N N   . GLY B 69 ? 0.3247 0.3995 0.3754 0.0497  0.0540  0.0035  69 GLY B N   
1289 C CA  . GLY B 69 ? 0.3755 0.4674 0.4385 0.0313  0.0581  -0.0035 69 GLY B CA  
1290 C C   . GLY B 69 ? 0.4289 0.5563 0.5220 0.0308  0.0675  -0.0117 69 GLY B C   
1291 O O   . GLY B 69 ? 0.4338 0.5878 0.5454 0.0160  0.0686  -0.0194 69 GLY B O   
1292 N N   . LYS B 70 ? 0.3611 0.4897 0.4603 0.0449  0.0764  -0.0130 70 LYS B N   
1293 C CA  . LYS B 70 ? 0.3068 0.4745 0.4374 0.0455  0.0876  -0.0238 70 LYS B CA  
1294 C C   . LYS B 70 ? 0.3999 0.5500 0.5181 0.0281  0.1073  -0.0273 70 LYS B C   
1295 O O   . LYS B 70 ? 0.4188 0.5293 0.5062 0.0281  0.1116  -0.0217 70 LYS B O   
1296 C CB  . LYS B 70 ? 0.4669 0.6465 0.6116 0.0741  0.0875  -0.0248 70 LYS B CB  
1297 C CG  . LYS B 70 ? 0.4844 0.6638 0.6257 0.0972  0.0686  -0.0151 70 LYS B CG  
1298 C CD  . LYS B 70 ? 0.4603 0.7044 0.6387 0.1080  0.0565  -0.0226 70 LYS B CD  
1299 C CE  . LYS B 70 ? 0.4794 0.7232 0.6434 0.1190  0.0352  -0.0115 70 LYS B CE  
1300 N NZ  . LYS B 70 ? 0.4707 0.7006 0.6244 0.1559  0.0268  0.0008  70 LYS B NZ  
1301 N N   . PRO B 71 ? 0.3693 0.5494 0.5088 0.0123  0.1207  -0.0374 71 PRO B N   
1302 C CA  . PRO B 71 ? 0.3547 0.5155 0.4760 -0.0033 0.1420  -0.0387 71 PRO B CA  
1303 C C   . PRO B 71 ? 0.4735 0.6292 0.5904 0.0119  0.1522  -0.0421 71 PRO B C   
1304 O O   . PRO B 71 ? 0.3436 0.5204 0.4835 0.0340  0.1479  -0.0473 71 PRO B O   
1305 C CB  . PRO B 71 ? 0.3629 0.5636 0.5138 -0.0240 0.1567  -0.0517 71 PRO B CB  
1306 C CG  . PRO B 71 ? 0.4198 0.6524 0.5972 -0.0252 0.1405  -0.0567 71 PRO B CG  
1307 C CD  . PRO B 71 ? 0.3746 0.6087 0.5531 0.0047  0.1183  -0.0497 71 PRO B CD  
1308 N N   . ASN B 72 ? 0.4087 0.5347 0.4931 0.0011  0.1662  -0.0395 72 ASN B N   
1309 C CA  . ASN B 72 ? 0.3915 0.5127 0.4683 0.0105  0.1794  -0.0463 72 ASN B CA  
1310 C C   . ASN B 72 ? 0.4470 0.5545 0.4940 -0.0089 0.1964  -0.0453 72 ASN B C   
1311 O O   . ASN B 72 ? 0.4921 0.5880 0.5237 -0.0272 0.1988  -0.0375 72 ASN B O   
1312 C CB  . ASN B 72 ? 0.4124 0.4994 0.4667 0.0262  0.1685  -0.0419 72 ASN B CB  
1313 C CG  . ASN B 72 ? 0.4206 0.4720 0.4341 0.0156  0.1608  -0.0320 72 ASN B CG  
1314 O OD1 . ASN B 72 ? 0.4002 0.4412 0.3873 0.0025  0.1700  -0.0295 72 ASN B OD1 
1315 N ND2 . ASN B 72 ? 0.3875 0.4215 0.3941 0.0227  0.1440  -0.0264 72 ASN B ND2 
1316 N N   . LYS B 73 ? 0.4703 0.5728 0.5039 -0.0035 0.2031  -0.0512 73 LYS B N   
1317 C CA  . LYS B 73 ? 0.4794 0.5744 0.4853 -0.0182 0.2147  -0.0500 73 LYS B CA  
1318 C C   . LYS B 73 ? 0.4441 0.5028 0.4001 -0.0209 0.2095  -0.0406 73 LYS B C   
1319 O O   . LYS B 73 ? 0.4895 0.5426 0.4184 -0.0279 0.2175  -0.0400 73 LYS B O   
1320 C CB  . LYS B 73 ? 0.3817 0.5005 0.4045 -0.0111 0.2258  -0.0645 73 LYS B CB  
1321 N N   . ARG B 74 ? 0.4095 0.4477 0.3528 -0.0145 0.1958  -0.0341 74 ARG B N   
1322 C CA  . ARG B 74 ? 0.4485 0.4620 0.3481 -0.0146 0.1878  -0.0277 74 ARG B CA  
1323 C C   . ARG B 74 ? 0.4598 0.4535 0.3309 -0.0243 0.1865  -0.0114 74 ARG B C   
1324 O O   . ARG B 74 ? 0.4576 0.4456 0.3414 -0.0283 0.1842  -0.0046 74 ARG B O   
1325 C CB  . ARG B 74 ? 0.4210 0.4239 0.3202 -0.0040 0.1739  -0.0307 74 ARG B CB  
1326 C CG  . ARG B 74 ? 0.3842 0.3947 0.3136 0.0073  0.1758  -0.0435 74 ARG B CG  
1327 C CD  . ARG B 74 ? 0.4952 0.5100 0.4194 0.0089  0.1840  -0.0564 74 ARG B CD  
1328 N NE  . ARG B 74 ? 0.7086 0.7103 0.6031 0.0068  0.1758  -0.0608 74 ARG B NE  
1329 C CZ  . ARG B 74 ? 0.5087 0.5001 0.4048 0.0107  0.1740  -0.0729 74 ARG B CZ  
1330 N NH1 . ARG B 74 ? 0.5199 0.5055 0.4402 0.0198  0.1816  -0.0807 74 ARG B NH1 
1331 N NH2 . ARG B 74 ? 0.5672 0.5539 0.4402 0.0059  0.1645  -0.0776 74 ARG B NH2 
1332 N N   . LYS B 75 ? 0.4852 0.4671 0.3166 -0.0270 0.1884  -0.0051 75 LYS B N   
1333 C CA  . LYS B 75 ? 0.4657 0.4202 0.2631 -0.0324 0.1880  0.0129  75 LYS B CA  
1334 C C   . LYS B 75 ? 0.4715 0.4069 0.2619 -0.0243 0.1727  0.0213  75 LYS B C   
1335 O O   . LYS B 75 ? 0.4548 0.3935 0.2357 -0.0125 0.1586  0.0169  75 LYS B O   
1336 C CB  . LYS B 75 ? 0.5201 0.4672 0.2712 -0.0295 0.1876  0.0189  75 LYS B CB  
1337 C CG  . LYS B 75 ? 0.5512 0.4628 0.2610 -0.0291 0.1847  0.0403  75 LYS B CG  
1338 C CD  . LYS B 75 ? 0.6222 0.5295 0.2890 -0.0299 0.1906  0.0479  75 LYS B CD  
1339 C CE  . LYS B 75 ? 0.6868 0.5520 0.3098 -0.0263 0.1881  0.0715  75 LYS B CE  
1340 N NZ  . LYS B 75 ? 0.8567 0.7225 0.4310 -0.0118 0.1756  0.0796  75 LYS B NZ  
1341 N N   . GLY B 76 ? 0.4690 0.3867 0.2665 -0.0321 0.1763  0.0306  76 GLY B N   
1342 C CA  . GLY B 76 ? 0.4839 0.3803 0.2733 -0.0248 0.1638  0.0390  76 GLY B CA  
1343 C C   . GLY B 76 ? 0.4908 0.4094 0.3285 -0.0238 0.1519  0.0286  76 GLY B C   
1344 O O   . GLY B 76 ? 0.4575 0.3643 0.2990 -0.0200 0.1384  0.0327  76 GLY B O   
1345 N N   . PHE B 77 ? 0.4254 0.3753 0.2989 -0.0252 0.1561  0.0155  77 PHE B N   
1346 C CA  . PHE B 77 ? 0.3778 0.3469 0.2897 -0.0203 0.1422  0.0084  77 PHE B CA  
1347 C C   . PHE B 77 ? 0.3835 0.3580 0.3204 -0.0316 0.1438  0.0090  77 PHE B C   
1348 O O   . PHE B 77 ? 0.3385 0.3114 0.2854 -0.0292 0.1291  0.0096  77 PHE B O   
1349 C CB  . PHE B 77 ? 0.3959 0.3910 0.3345 -0.0137 0.1461  -0.0035 77 PHE B CB  
1350 C CG  . PHE B 77 ? 0.3371 0.3426 0.3008 -0.0036 0.1304  -0.0069 77 PHE B CG  
1351 C CD1 . PHE B 77 ? 0.3346 0.3273 0.2839 0.0045  0.1193  -0.0083 77 PHE B CD1 
1352 C CD2 . PHE B 77 ? 0.3721 0.4018 0.3710 -0.0034 0.1276  -0.0097 77 PHE B CD2 
1353 C CE1 . PHE B 77 ? 0.2835 0.2791 0.2485 0.0116  0.1080  -0.0095 77 PHE B CE1 
1354 C CE2 . PHE B 77 ? 0.3522 0.3884 0.3657 0.0076  0.1130  -0.0099 77 PHE B CE2 
1355 C CZ  . PHE B 77 ? 0.3432 0.3580 0.3372 0.0145  0.1045  -0.0084 77 PHE B CZ  
1356 N N   . ASN B 78 ? 0.4051 0.3904 0.3542 -0.0464 0.1630  0.0056  78 ASN B N   
1357 C CA  . ASN B 78 ? 0.4115 0.4100 0.3893 -0.0609 0.1658  0.0004  78 ASN B CA  
1358 C C   . ASN B 78 ? 0.4365 0.3931 0.3882 -0.0688 0.1646  0.0105  78 ASN B C   
1359 O O   . ASN B 78 ? 0.3493 0.3119 0.3220 -0.0760 0.1584  0.0049  78 ASN B O   
1360 C CB  . ASN B 78 ? 0.4058 0.4304 0.4047 -0.0788 0.1897  -0.0097 78 ASN B CB  
1361 C CG  . ASN B 78 ? 0.4431 0.5144 0.4761 -0.0669 0.1901  -0.0226 78 ASN B CG  
1362 O OD1 . ASN B 78 ? 0.4325 0.5165 0.4791 -0.0468 0.1719  -0.0239 78 ASN B OD1 
1363 N ND2 . ASN B 78 ? 0.4255 0.5174 0.4696 -0.0760 0.2050  -0.0309 78 ASN B ND2 
1364 N N   . GLU B 79 ? 0.3953 0.3095 0.2997 -0.0652 0.1696  0.0246  79 GLU B N   
1365 C CA  . GLU B 79 ? 0.4607 0.3300 0.3377 -0.0643 0.1655  0.0356  79 GLU B CA  
1366 C C   . GLU B 79 ? 0.4460 0.3217 0.3314 -0.0467 0.1394  0.0334  79 GLU B C   
1367 O O   . GLU B 79 ? 0.5161 0.3747 0.4047 -0.0484 0.1338  0.0330  79 GLU B O   
1368 C CB  . GLU B 79 ? 0.5458 0.3695 0.3660 -0.0582 0.1743  0.0536  79 GLU B CB  
1369 N N   . GLY B 80 ? 0.3604 0.2598 0.2493 -0.0318 0.1259  0.0298  80 GLY B N   
1370 C CA  . GLY B 80 ? 0.3575 0.2662 0.2551 -0.0193 0.1046  0.0254  80 GLY B CA  
1371 C C   . GLY B 80 ? 0.3438 0.2769 0.2794 -0.0263 0.0983  0.0155  80 GLY B C   
1372 O O   . GLY B 80 ? 0.3579 0.2877 0.2972 -0.0231 0.0861  0.0128  80 GLY B O   
1373 N N   . LEU B 81 ? 0.3495 0.3121 0.3136 -0.0341 0.1056  0.0088  81 LEU B N   
1374 C CA  . LEU B 81 ? 0.3568 0.3489 0.3551 -0.0397 0.0988  -0.0007 81 LEU B CA  
1375 C C   . LEU B 81 ? 0.3617 0.3403 0.3637 -0.0557 0.1041  -0.0043 81 LEU B C   
1376 O O   . LEU B 81 ? 0.3801 0.3716 0.3975 -0.0581 0.0934  -0.0118 81 LEU B O   
1377 C CB  . LEU B 81 ? 0.3010 0.3326 0.3298 -0.0415 0.1055  -0.0082 81 LEU B CB  
1378 C CG  . LEU B 81 ? 0.3091 0.3529 0.3398 -0.0239 0.1007  -0.0073 81 LEU B CG  
1379 C CD1 . LEU B 81 ? 0.3169 0.4019 0.3816 -0.0211 0.1067  -0.0159 81 LEU B CD1 
1380 C CD2 . LEU B 81 ? 0.2930 0.3331 0.3187 -0.0119 0.0826  -0.0051 81 LEU B CD2 
1381 N N   . TRP B 82 ? 0.3408 0.2904 0.3260 -0.0684 0.1228  0.0003  82 TRP B N   
1382 C CA  . TRP B 82 ? 0.3902 0.3133 0.3732 -0.0853 0.1322  -0.0031 82 TRP B CA  
1383 C C   . TRP B 82 ? 0.4058 0.2937 0.3665 -0.0724 0.1195  0.0024  82 TRP B C   
1384 O O   . TRP B 82 ? 0.4581 0.3434 0.4316 -0.0803 0.1166  -0.0074 82 TRP B O   
1385 C CB  . TRP B 82 ? 0.4215 0.3091 0.3821 -0.1018 0.1585  0.0036  82 TRP B CB  
1386 C CG  . TRP B 82 ? 0.5021 0.3573 0.4622 -0.1242 0.1735  -0.0027 82 TRP B CG  
1387 C CD1 . TRP B 82 ? 0.4624 0.3424 0.4542 -0.1532 0.1894  -0.0209 82 TRP B CD1 
1388 C CD2 . TRP B 82 ? 0.5762 0.3700 0.5044 -0.1188 0.1740  0.0062  82 TRP B CD2 
1389 N NE1 . TRP B 82 ? 0.5598 0.3965 0.5393 -0.1650 0.1971  -0.0252 82 TRP B NE1 
1390 C CE2 . TRP B 82 ? 0.5935 0.3706 0.5336 -0.1464 0.1921  -0.0071 82 TRP B CE2 
1391 C CE3 . TRP B 82 ? 0.5793 0.3342 0.4717 -0.0915 0.1603  0.0219  82 TRP B CE3 
1392 C CZ2 . TRP B 82 ? 0.5759 0.2947 0.4915 -0.1439 0.1958  -0.0042 82 TRP B CZ2 
1393 C CZ3 . TRP B 82 ? 0.5868 0.2835 0.4559 -0.0889 0.1652  0.0263  82 TRP B CZ3 
1394 C CH2 . TRP B 82 ? 0.6274 0.2994 0.5065 -0.1163 0.1854  0.0145  82 TRP B CH2 
1395 N N   . GLU B 83 ? 0.4277 0.2929 0.3568 -0.0522 0.1120  0.0153  83 GLU B N   
1396 C CA  . GLU B 83 ? 0.3747 0.2122 0.2847 -0.0366 0.0998  0.0188  83 GLU B CA  
1397 C C   . GLU B 83 ? 0.4131 0.2850 0.3484 -0.0315 0.0813  0.0061  83 GLU B C   
1398 O O   . GLU B 83 ? 0.4128 0.2731 0.3515 -0.0310 0.0765  -0.0007 83 GLU B O   
1399 C CB  . GLU B 83 ? 0.4071 0.2260 0.2802 -0.0150 0.0941  0.0324  83 GLU B CB  
1400 C CG  . GLU B 83 ? 0.5084 0.2858 0.3442 -0.0176 0.1124  0.0484  83 GLU B CG  
1401 C CD  . GLU B 83 ? 0.5215 0.2896 0.3185 0.0057  0.1036  0.0607  83 GLU B CD  
1402 O OE1 . GLU B 83 ? 0.4933 0.2953 0.2992 0.0194  0.0855  0.0531  83 GLU B OE1 
1403 O OE2 . GLU B 83 ? 0.5514 0.2790 0.3066 0.0091  0.1158  0.0772  83 GLU B OE2 
1404 N N   . ILE B 84 ? 0.3375 0.2482 0.2884 -0.0283 0.0728  0.0026  84 ILE B N   
1405 C CA  . ILE B 84 ? 0.3507 0.2879 0.3169 -0.0241 0.0574  -0.0067 84 ILE B CA  
1406 C C   . ILE B 84 ? 0.3442 0.2995 0.3356 -0.0388 0.0574  -0.0181 84 ILE B C   
1407 O O   . ILE B 84 ? 0.3056 0.2712 0.3030 -0.0381 0.0474  -0.0267 84 ILE B O   
1408 C CB  . ILE B 84 ? 0.2926 0.2559 0.2633 -0.0176 0.0516  -0.0059 84 ILE B CB  
1409 C CG1 . ILE B 84 ? 0.3025 0.2803 0.2756 -0.0128 0.0384  -0.0126 84 ILE B CG1 
1410 C CG2 . ILE B 84 ? 0.2895 0.2783 0.2824 -0.0247 0.0570  -0.0073 84 ILE B CG2 
1411 C CD1 . ILE B 84 ? 0.2648 0.2495 0.2290 -0.0057 0.0358  -0.0115 84 ILE B CD1 
1412 N N   . GLN B 85 ? 0.3262 0.2905 0.3329 -0.0538 0.0693  -0.0210 85 GLN B N   
1413 C CA  . GLN B 85 ? 0.3619 0.3503 0.3940 -0.0703 0.0698  -0.0359 85 GLN B CA  
1414 C C   . GLN B 85 ? 0.3340 0.2860 0.3590 -0.0818 0.0790  -0.0428 85 GLN B C   
1415 O O   . GLN B 85 ? 0.3493 0.3137 0.3867 -0.0892 0.0735  -0.0571 85 GLN B O   
1416 C CB  . GLN B 85 ? 0.3677 0.3886 0.4238 -0.0832 0.0799  -0.0412 85 GLN B CB  
1417 N N   . ASN B 86 ? 0.3294 0.2333 0.3319 -0.0837 0.0945  -0.0330 86 ASN B N   
1418 C CA  . ASN B 86 ? 0.3812 0.2422 0.3766 -0.0981 0.1093  -0.0395 86 ASN B CA  
1419 C C   . ASN B 86 ? 0.4356 0.2455 0.4019 -0.0786 0.1052  -0.0317 86 ASN B C   
1420 O O   . ASN B 86 ? 0.4601 0.2377 0.4249 -0.0865 0.1133  -0.0414 86 ASN B O   
1421 C CB  . ASN B 86 ? 0.4672 0.2995 0.4532 -0.1171 0.1348  -0.0344 86 ASN B CB  
1422 C CG  . ASN B 86 ? 0.4959 0.3840 0.5178 -0.1389 0.1414  -0.0487 86 ASN B CG  
1423 O OD1 . ASN B 86 ? 0.5308 0.4400 0.5784 -0.1618 0.1476  -0.0694 86 ASN B OD1 
1424 N ND2 . ASN B 86 ? 0.4243 0.3409 0.4500 -0.1314 0.1401  -0.0405 86 ASN B ND2 
1425 N N   . ASN B 87 ? 0.3975 0.2006 0.3417 -0.0530 0.0937  -0.0168 87 ASN B N   
1426 C CA  . ASN B 87 ? 0.4450 0.2105 0.3661 -0.0302 0.0869  -0.0122 87 ASN B CA  
1427 C C   . ASN B 87 ? 0.4261 0.2187 0.3392 -0.0059 0.0681  -0.0060 87 ASN B C   
1428 O O   . ASN B 87 ? 0.4662 0.2349 0.3495 0.0132  0.0666  0.0087  87 ASN B O   
1429 C CB  . ASN B 87 ? 0.5145 0.2091 0.3990 -0.0261 0.1044  0.0035  87 ASN B CB  
1430 C CG  . ASN B 87 ? 0.5413 0.1890 0.4079 -0.0050 0.1013  0.0032  87 ASN B CG  
1431 O OD1 . ASN B 87 ? 0.5868 0.2618 0.4671 0.0112  0.0837  -0.0079 87 ASN B OD1 
1432 N ND2 . ASN B 87 ? 0.6948 0.2703 0.5302 -0.0050 0.1202  0.0149  87 ASN B ND2 
1433 N N   . PRO B 88 ? 0.4058 0.2482 0.3422 -0.0074 0.0546  -0.0176 88 PRO B N   
1434 C CA  . PRO B 88 ? 0.3197 0.1884 0.2499 0.0090  0.0410  -0.0150 88 PRO B CA  
1435 C C   . PRO B 88 ? 0.3545 0.2123 0.2698 0.0329  0.0309  -0.0164 88 PRO B C   
1436 O O   . PRO B 88 ? 0.3615 0.2366 0.2661 0.0469  0.0220  -0.0137 88 PRO B O   
1437 C CB  . PRO B 88 ? 0.3034 0.2169 0.2586 -0.0016 0.0331  -0.0275 88 PRO B CB  
1438 C CG  . PRO B 88 ? 0.3097 0.2216 0.2809 -0.0147 0.0362  -0.0399 88 PRO B CG  
1439 C CD  . PRO B 88 ? 0.3790 0.2549 0.3447 -0.0250 0.0522  -0.0340 88 PRO B CD  
1440 N N   . HIS B 89 ? 0.3654 0.1974 0.2806 0.0390  0.0321  -0.0227 89 HIS B N   
1441 C CA  . HIS B 89 ? 0.3811 0.2122 0.2888 0.0657  0.0203  -0.0282 89 HIS B CA  
1442 C C   . HIS B 89 ? 0.4497 0.2269 0.3243 0.0901  0.0234  -0.0122 89 HIS B C   
1443 O O   . HIS B 89 ? 0.4669 0.2403 0.3355 0.1177  0.0131  -0.0167 89 HIS B O   
1444 C CB  . HIS B 89 ? 0.3707 0.2145 0.3018 0.0613  0.0180  -0.0493 89 HIS B CB  
1445 C CG  . HIS B 89 ? 0.3643 0.2587 0.3193 0.0408  0.0140  -0.0624 89 HIS B CG  
1446 N ND1 . HIS B 89 ? 0.3061 0.2409 0.2639 0.0429  0.0050  -0.0650 89 HIS B ND1 
1447 C CD2 . HIS B 89 ? 0.3471 0.2559 0.3200 0.0182  0.0184  -0.0731 89 HIS B CD2 
1448 C CE1 . HIS B 89 ? 0.3445 0.3088 0.3174 0.0236  0.0052  -0.0737 89 HIS B CE1 
1449 N NE2 . HIS B 89 ? 0.3185 0.2712 0.3004 0.0101  0.0115  -0.0783 89 HIS B NE2 
1450 N N   . ALA B 90 ? 0.4783 0.2146 0.3294 0.0821  0.0377  0.0065  90 ALA B N   
1451 C CA  . ALA B 90 ? 0.5757 0.2483 0.3870 0.1036  0.0441  0.0251  90 ALA B CA  
1452 C C   . ALA B 90 ? 0.5672 0.2525 0.3499 0.1350  0.0288  0.0375  90 ALA B C   
1453 O O   . ALA B 90 ? 0.5671 0.3063 0.3598 0.1324  0.0184  0.0322  90 ALA B O   
1454 C CB  . ALA B 90 ? 0.6448 0.2681 0.4366 0.0802  0.0684  0.0403  90 ALA B CB  
1455 N N   . SER B 91 ? 0.6391 0.2718 0.3835 0.1652  0.0284  0.0539  91 SER B N   
1456 C CA  . SER B 91 ? 0.6795 0.3167 0.3861 0.1972  0.0149  0.0698  91 SER B CA  
1457 C C   . SER B 91 ? 0.7693 0.3765 0.4400 0.1817  0.0309  0.0922  91 SER B C   
1458 O O   . SER B 91 ? 0.7661 0.3163 0.4171 0.1673  0.0518  0.1054  91 SER B O   
1459 C CB  . SER B 91 ? 0.8089 0.4141 0.4934 0.2320  0.0075  0.0770  91 SER B CB  
1460 O OG  . SER B 91 ? 0.8586 0.4832 0.5119 0.2580  -0.0064 0.0884  91 SER B OG  
1461 N N   . TYR B 92 ? 0.6616 0.3211 0.3333 0.1770  0.0229  0.0899  92 TYR B N   
1462 C CA  . TYR B 92 ? 0.6855 0.3282 0.3242 0.1640  0.0368  0.1075  92 TYR B CA  
1463 C C   . TYR B 92 ? 0.8524 0.5069 0.4527 0.1925  0.0232  0.1179  92 TYR B C   
1464 O O   . TYR B 92 ? 0.9464 0.6160 0.5292 0.1828  0.0281  0.1233  92 TYR B O   
1465 C CB  . TYR B 92 ? 0.6126 0.3100 0.2876 0.1324  0.0411  0.0919  92 TYR B CB  
1466 C CG  . TYR B 92 ? 0.5771 0.2716 0.2923 0.1004  0.0556  0.0808  92 TYR B CG  
1467 C CD1 . TYR B 92 ? 0.6669 0.3222 0.3738 0.0754  0.0806  0.0904  92 TYR B CD1 
1468 C CD2 . TYR B 92 ? 0.5661 0.3013 0.3267 0.0939  0.0450  0.0592  92 TYR B CD2 
1469 C CE1 . TYR B 92 ? 0.6482 0.3111 0.3944 0.0464  0.0921  0.0768  92 TYR B CE1 
1470 C CE2 . TYR B 92 ? 0.6047 0.3428 0.3991 0.0663  0.0561  0.0487  92 TYR B CE2 
1471 C CZ  . TYR B 92 ? 0.6288 0.3336 0.4174 0.0436  0.0784  0.0567  92 TYR B CZ  
1472 O OH  . TYR B 92 ? 0.5743 0.2919 0.3986 0.0169  0.0877  0.0432  92 TYR B OH  
1473 N N   . SER B 93 ? 0.9196 0.5751 0.5138 0.2250  0.0066  0.1164  93 SER B N   
1474 C CA  . SER B 93 ? 0.9736 0.6493 0.5395 0.2537  -0.0089 0.1217  93 SER B CA  
1475 C C   . SER B 93 ? 1.1222 0.7319 0.6476 0.2658  0.0018  0.1441  93 SER B C   
1476 O O   . SER B 93 ? 1.0238 0.5743 0.5406 0.2440  0.0253  0.1554  93 SER B O   
1477 C CB  . SER B 93 ? 0.9742 0.7082 0.5655 0.2823  -0.0355 0.1006  93 SER B CB  
1478 O OG  . SER B 93 ? 1.1318 0.8349 0.7165 0.3084  -0.0401 0.1045  93 SER B OG  
1479 N N   . HIS C 3  ? 0.7656 0.8501 0.7286 0.0241  0.3703  0.0731  3  HIS C N   
1480 C CA  . HIS C 3  ? 0.8142 0.8827 0.7256 0.0435  0.3835  0.0923  3  HIS C CA  
1481 C C   . HIS C 3  ? 0.8000 0.8388 0.6634 0.0770  0.3606  0.1004  3  HIS C C   
1482 O O   . HIS C 3  ? 0.8313 0.8456 0.6998 0.0811  0.3423  0.0999  3  HIS C O   
1483 C CB  . HIS C 3  ? 0.7884 0.8159 0.6876 0.0282  0.4120  0.1197  3  HIS C CB  
1484 N N   . ALA C 4  ? 0.7833 0.8288 0.6003 0.0990  0.3616  0.1059  4  ALA C N   
1485 C CA  . ALA C 4  ? 0.7442 0.7726 0.5130 0.1306  0.3365  0.1089  4  ALA C CA  
1486 C C   . ALA C 4  ? 0.7481 0.7280 0.5003 0.1379  0.3273  0.1321  4  ALA C C   
1487 O O   . ALA C 4  ? 0.8127 0.7602 0.5610 0.1297  0.3470  0.1585  4  ALA C O   
1488 C CB  . ALA C 4  ? 0.8051 0.8438 0.5214 0.1468  0.3445  0.1163  4  ALA C CB  
1489 N N   . PHE C 5  ? 0.7164 0.6915 0.4619 0.1536  0.2979  0.1211  5  PHE C N   
1490 C CA  . PHE C 5  ? 0.7099 0.6483 0.4414 0.1638  0.2864  0.1388  5  PHE C CA  
1491 C C   . PHE C 5  ? 0.8038 0.7335 0.4746 0.1923  0.2753  0.1585  5  PHE C C   
1492 O O   . PHE C 5  ? 0.7957 0.7481 0.4342 0.2020  0.2748  0.1540  5  PHE C O   
1493 C CB  . PHE C 5  ? 0.6489 0.5932 0.3993 0.1655  0.2595  0.1159  5  PHE C CB  
1494 C CG  . PHE C 5  ? 0.5983 0.5600 0.4077 0.1381  0.2650  0.0953  5  PHE C CG  
1495 C CD1 . PHE C 5  ? 0.6442 0.6449 0.4737 0.1357  0.2587  0.0709  5  PHE C CD1 
1496 C CD2 . PHE C 5  ? 0.6448 0.5868 0.4909 0.1158  0.2741  0.0985  5  PHE C CD2 
1497 C CE1 . PHE C 5  ? 0.5725 0.5979 0.4563 0.1128  0.2600  0.0539  5  PHE C CE1 
1498 C CE2 . PHE C 5  ? 0.5624 0.5286 0.4614 0.0881  0.2745  0.0770  5  PHE C CE2 
1499 C CZ  . PHE C 5  ? 0.5304 0.5409 0.4471 0.0874  0.2667  0.0567  5  PHE C CZ  
1500 N N   . LYS C 6  ? 0.7746 0.6760 0.4325 0.2053  0.2656  0.1789  6  LYS C N   
1501 C CA  . LYS C 6  ? 0.8261 0.7275 0.4331 0.2325  0.2487  0.1974  6  LYS C CA  
1502 C C   . LYS C 6  ? 0.8526 0.7474 0.4591 0.2470  0.2187  0.1954  6  LYS C C   
1503 O O   . LYS C 6  ? 0.7635 0.6409 0.4066 0.2350  0.2212  0.1906  6  LYS C O   
1504 C CB  . LYS C 6  ? 0.9622 0.8377 0.5550 0.2350  0.2736  0.2356  6  LYS C CB  
1505 C CG  . LYS C 6  ? 0.9509 0.7822 0.5753 0.2314  0.2867  0.2581  6  LYS C CG  
1506 C CD  . LYS C 6  ? 1.0198 0.8220 0.6354 0.2288  0.3169  0.2921  6  LYS C CD  
1507 C CE  . LYS C 6  ? 1.1644 0.9196 0.8089 0.2313  0.3275  0.3136  6  LYS C CE  
1508 N NZ  . LYS C 6  ? 1.1925 0.9508 0.8142 0.2639  0.2986  0.3297  6  LYS C NZ  
1509 N N   . PRO C 7  ? 0.8608 0.7746 0.4293 0.2696  0.1895  0.1959  7  PRO C N   
1510 C CA  . PRO C 7  ? 0.8689 0.7863 0.4430 0.2806  0.1569  0.1886  7  PRO C CA  
1511 C C   . PRO C 7  ? 0.9159 0.7987 0.5223 0.2805  0.1690  0.2141  7  PRO C C   
1512 O O   . PRO C 7  ? 0.8708 0.7319 0.4760 0.2864  0.1895  0.2448  7  PRO C O   
1513 C CB  . PRO C 7  ? 0.9332 0.8811 0.4663 0.3009  0.1305  0.1900  7  PRO C CB  
1514 C CG  . PRO C 7  ? 0.9734 0.9378 0.4763 0.2975  0.1435  0.1822  7  PRO C CG  
1515 C CD  . PRO C 7  ? 0.9658 0.9016 0.4875 0.2836  0.1848  0.2039  7  PRO C CD  
1516 N N   . GLY C 8  ? 0.8548 0.7298 0.4925 0.2724  0.1576  0.1999  8  GLY C N   
1517 C CA  . GLY C 8  ? 0.8377 0.6797 0.5191 0.2677  0.1694  0.2141  8  GLY C CA  
1518 C C   . GLY C 8  ? 0.8350 0.6541 0.5680 0.2330  0.1987  0.2004  8  GLY C C   
1519 O O   . GLY C 8  ? 0.7134 0.5117 0.4913 0.2219  0.2040  0.1962  8  GLY C O   
1520 N N   . ASP C 9  ? 0.7325 0.5601 0.4621 0.2156  0.2183  0.1912  9  ASP C N   
1521 C CA  . ASP C 9  ? 0.7543 0.5732 0.5347 0.1806  0.2425  0.1745  9  ASP C CA  
1522 C C   . ASP C 9  ? 0.6229 0.4605 0.4437 0.1619  0.2156  0.1385  9  ASP C C   
1523 O O   . ASP C 9  ? 0.5817 0.4471 0.3897 0.1685  0.1829  0.1186  9  ASP C O   
1524 C CB  . ASP C 9  ? 0.6983 0.5380 0.4699 0.1687  0.2629  0.1683  9  ASP C CB  
1525 C CG  . ASP C 9  ? 0.8055 0.6270 0.5572 0.1732  0.2908  0.1970  9  ASP C CG  
1526 O OD1 . ASP C 9  ? 0.7784 0.5680 0.5180 0.1888  0.2959  0.2252  9  ASP C OD1 
1527 O OD2 . ASP C 9  ? 0.7581 0.6007 0.5113 0.1609  0.3033  0.1888  9  ASP C OD2 
1528 N N   . LEU C 10 ? 0.5742 0.3948 0.4424 0.1366  0.2316  0.1298  10 LEU C N   
1529 C CA  . LEU C 10 ? 0.5168 0.3550 0.4217 0.1152  0.2107  0.0984  10 LEU C CA  
1530 C C   . LEU C 10 ? 0.5875 0.4538 0.5148 0.0872  0.2150  0.0760  10 LEU C C   
1531 O O   . LEU C 10 ? 0.5804 0.4435 0.5217 0.0711  0.2463  0.0804  10 LEU C O   
1532 C CB  . LEU C 10 ? 0.5982 0.4075 0.5408 0.1025  0.2270  0.0974  10 LEU C CB  
1533 C CG  . LEU C 10 ? 0.6448 0.4294 0.5743 0.1345  0.2219  0.1209  10 LEU C CG  
1534 C CD1 . LEU C 10 ? 0.5884 0.3460 0.5631 0.1228  0.2379  0.1129  10 LEU C CD1 
1535 C CD2 . LEU C 10 ? 0.6324 0.4490 0.5350 0.1573  0.1797  0.1155  10 LEU C CD2 
1536 N N   . VAL C 11 ? 0.4656 0.3610 0.3973 0.0816  0.1835  0.0534  11 VAL C N   
1537 C CA  . VAL C 11 ? 0.4428 0.3704 0.3921 0.0638  0.1803  0.0359  11 VAL C CA  
1538 C C   . VAL C 11 ? 0.4182 0.3641 0.3876 0.0463  0.1525  0.0144  11 VAL C C   
1539 O O   . VAL C 11 ? 0.3558 0.2922 0.3210 0.0494  0.1342  0.0107  11 VAL C O   
1540 C CB  . VAL C 11 ? 0.4427 0.3871 0.3612 0.0864  0.1710  0.0378  11 VAL C CB  
1541 C CG1 . VAL C 11 ? 0.4673 0.3998 0.3605 0.1011  0.2010  0.0598  11 VAL C CG1 
1542 C CG2 . VAL C 11 ? 0.4172 0.3591 0.3062 0.1068  0.1363  0.0320  11 VAL C CG2 
1543 N N   . PHE C 12 ? 0.3598 0.3365 0.3521 0.0274  0.1499  0.0013  12 PHE C N   
1544 C CA  . PHE C 12 ? 0.3389 0.3366 0.3364 0.0198  0.1187  -0.0124 12 PHE C CA  
1545 C C   . PHE C 12 ? 0.3171 0.3262 0.2973 0.0425  0.1043  -0.0114 12 PHE C C   
1546 O O   . PHE C 12 ? 0.3610 0.3851 0.3457 0.0495  0.1219  -0.0080 12 PHE C O   
1547 C CB  . PHE C 12 ? 0.3480 0.3766 0.3807 -0.0135 0.1216  -0.0255 12 PHE C CB  
1548 C CG  . PHE C 12 ? 0.3158 0.3335 0.3666 -0.0386 0.1359  -0.0339 12 PHE C CG  
1549 C CD1 . PHE C 12 ? 0.3560 0.3614 0.4252 -0.0514 0.1708  -0.0334 12 PHE C CD1 
1550 C CD2 . PHE C 12 ? 0.3066 0.3245 0.3572 -0.0507 0.1174  -0.0437 12 PHE C CD2 
1551 C CE1 . PHE C 12 ? 0.3340 0.3240 0.4227 -0.0733 0.1870  -0.0447 12 PHE C CE1 
1552 C CE2 . PHE C 12 ? 0.2926 0.3027 0.3624 -0.0729 0.1337  -0.0558 12 PHE C CE2 
1553 C CZ  . PHE C 12 ? 0.3286 0.3226 0.4181 -0.0828 0.1685  -0.0573 12 PHE C CZ  
1554 N N   . ALA C 13 ? 0.3279 0.3283 0.2897 0.0536  0.0752  -0.0162 13 ALA C N   
1555 C CA  . ALA C 13 ? 0.3252 0.3257 0.2684 0.0777  0.0620  -0.0189 13 ALA C CA  
1556 C C   . ALA C 13 ? 0.3543 0.3654 0.3119 0.0702  0.0376  -0.0257 13 ALA C C   
1557 O O   . ALA C 13 ? 0.3094 0.3119 0.2670 0.0547  0.0200  -0.0282 13 ALA C O   
1558 C CB  . ALA C 13 ? 0.3582 0.3331 0.2636 0.0983  0.0498  -0.0197 13 ALA C CB  
1559 N N   . LYS C 14 ? 0.3159 0.3461 0.2856 0.0827  0.0371  -0.0270 14 LYS C N   
1560 C CA  . LYS C 14 ? 0.3089 0.3519 0.2963 0.0791  0.0153  -0.0273 14 LYS C CA  
1561 C C   . LYS C 14 ? 0.3688 0.3836 0.3375 0.1053  -0.0025 -0.0322 14 LYS C C   
1562 O O   . LYS C 14 ? 0.4009 0.4168 0.3646 0.1305  0.0076  -0.0377 14 LYS C O   
1563 C CB  . LYS C 14 ? 0.3047 0.3961 0.3286 0.0758  0.0255  -0.0252 14 LYS C CB  
1564 C CG  . LYS C 14 ? 0.3089 0.4219 0.3528 0.0731  0.0008  -0.0201 14 LYS C CG  
1565 C CD  . LYS C 14 ? 0.2806 0.3919 0.3207 0.0421  -0.0137 -0.0166 14 LYS C CD  
1566 C CE  . LYS C 14 ? 0.2902 0.4286 0.3454 0.0379  -0.0379 -0.0061 14 LYS C CE  
1567 N NZ  . LYS C 14 ? 0.3128 0.4101 0.3508 0.0603  -0.0611 0.0024  14 LYS C NZ  
1568 N N   . MET C 15 ? 0.3400 0.3288 0.2987 0.0973  -0.0262 -0.0318 15 MET C N   
1569 C CA  . MET C 15 ? 0.3720 0.3274 0.3187 0.1163  -0.0439 -0.0367 15 MET C CA  
1570 C C   . MET C 15 ? 0.3754 0.3378 0.3435 0.1119  -0.0616 -0.0238 15 MET C C   
1571 O O   . MET C 15 ? 0.3780 0.3565 0.3532 0.0851  -0.0690 -0.0137 15 MET C O   
1572 C CB  . MET C 15 ? 0.4254 0.3418 0.3436 0.1071  -0.0570 -0.0450 15 MET C CB  
1573 C CG  . MET C 15 ? 0.4706 0.3838 0.3646 0.1128  -0.0458 -0.0549 15 MET C CG  
1574 S SD  . MET C 15 ? 0.6087 0.5136 0.4816 0.1479  -0.0353 -0.0698 15 MET C SD  
1575 C CE  . MET C 15 ? 0.5681 0.4253 0.4203 0.1512  -0.0584 -0.0889 15 MET C CE  
1576 N N   . LYS C 16 ? 0.4184 0.3690 0.3956 0.1392  -0.0683 -0.0236 16 LYS C N   
1577 C CA  . LYS C 16 ? 0.4207 0.3723 0.4153 0.1402  -0.0881 -0.0059 16 LYS C CA  
1578 C C   . LYS C 16 ? 0.4298 0.3440 0.4025 0.1143  -0.1058 0.0019  16 LYS C C   
1579 O O   . LYS C 16 ? 0.5149 0.3831 0.4631 0.1118  -0.1083 -0.0105 16 LYS C O   
1580 C CB  . LYS C 16 ? 0.4725 0.4012 0.4787 0.1788  -0.0922 -0.0083 16 LYS C CB  
1581 C CG  . LYS C 16 ? 0.4926 0.4138 0.5157 0.1868  -0.1143 0.0152  16 LYS C CG  
1582 C CD  . LYS C 16 ? 0.6468 0.6106 0.7102 0.2212  -0.1113 0.0201  16 LYS C CD  
1583 C CE  . LYS C 16 ? 0.6955 0.6907 0.7822 0.2219  -0.1337 0.0508  16 LYS C CE  
1584 N NZ  . LYS C 16 ? 0.6014 0.6820 0.7319 0.2336  -0.1281 0.0536  16 LYS C NZ  
1585 N N   . GLY C 17 ? 0.4612 0.4017 0.4421 0.0919  -0.1169 0.0206  17 GLY C N   
1586 C CA  . GLY C 17 ? 0.4658 0.3797 0.4261 0.0631  -0.1307 0.0300  17 GLY C CA  
1587 C C   . GLY C 17 ? 0.4951 0.4285 0.4458 0.0286  -0.1213 0.0205  17 GLY C C   
1588 O O   . GLY C 17 ? 0.4559 0.3713 0.3904 0.0028  -0.1295 0.0244  17 GLY C O   
1589 N N   . TYR C 18 ? 0.3724 0.3396 0.3339 0.0277  -0.1024 0.0081  18 TYR C N   
1590 C CA  . TYR C 18 ? 0.3552 0.3334 0.3114 0.0017  -0.0903 -0.0028 18 TYR C CA  
1591 C C   . TYR C 18 ? 0.3572 0.3849 0.3357 -0.0081 -0.0727 -0.0056 18 TYR C C   
1592 O O   . TYR C 18 ? 0.2974 0.3466 0.2929 0.0105  -0.0644 -0.0049 18 TYR C O   
1593 C CB  . TYR C 18 ? 0.3476 0.2963 0.2885 0.0143  -0.0821 -0.0183 18 TYR C CB  
1594 C CG  . TYR C 18 ? 0.3894 0.2928 0.3099 0.0163  -0.0979 -0.0225 18 TYR C CG  
1595 C CD1 . TYR C 18 ? 0.4432 0.3137 0.3580 0.0408  -0.1067 -0.0226 18 TYR C CD1 
1596 C CD2 . TYR C 18 ? 0.5546 0.4485 0.4649 -0.0074 -0.1022 -0.0293 18 TYR C CD2 
1597 C CE1 . TYR C 18 ? 0.5008 0.3250 0.3986 0.0384  -0.1190 -0.0300 18 TYR C CE1 
1598 C CE2 . TYR C 18 ? 0.4936 0.3488 0.3884 -0.0107 -0.1153 -0.0359 18 TYR C CE2 
1599 C CZ  . TYR C 18 ? 0.5724 0.3901 0.4599 0.0107  -0.1234 -0.0367 18 TYR C CZ  
1600 O OH  . TYR C 18 ? 0.6533 0.4273 0.5268 0.0035  -0.1343 -0.0466 18 TYR C OH  
1601 N N   . PRO C 19 ? 0.3035 0.3507 0.2848 -0.0387 -0.0647 -0.0112 19 PRO C N   
1602 C CA  . PRO C 19 ? 0.3052 0.3913 0.3086 -0.0516 -0.0437 -0.0193 19 PRO C CA  
1603 C C   . PRO C 19 ? 0.2505 0.3202 0.2557 -0.0333 -0.0218 -0.0268 19 PRO C C   
1604 O O   . PRO C 19 ? 0.3039 0.3384 0.2901 -0.0172 -0.0237 -0.0286 19 PRO C O   
1605 C CB  . PRO C 19 ? 0.2533 0.3506 0.2550 -0.0870 -0.0392 -0.0280 19 PRO C CB  
1606 C CG  . PRO C 19 ? 0.3107 0.3686 0.2910 -0.0848 -0.0491 -0.0285 19 PRO C CG  
1607 C CD  . PRO C 19 ? 0.3266 0.3577 0.2928 -0.0624 -0.0700 -0.0153 19 PRO C CD  
1608 N N   . HIS C 20 ? 0.2745 0.3722 0.3014 -0.0374 -0.0006 -0.0308 20 HIS C N   
1609 C CA  . HIS C 20 ? 0.2595 0.3393 0.2852 -0.0249 0.0244  -0.0338 20 HIS C CA  
1610 C C   . HIS C 20 ? 0.2442 0.2948 0.2572 -0.0317 0.0291  -0.0382 20 HIS C C   
1611 O O   . HIS C 20 ? 0.2921 0.3522 0.3151 -0.0584 0.0321  -0.0463 20 HIS C O   
1612 C CB  . HIS C 20 ? 0.2722 0.3834 0.3259 -0.0401 0.0505  -0.0387 20 HIS C CB  
1613 C CG  . HIS C 20 ? 0.2778 0.4285 0.3513 -0.0319 0.0481  -0.0360 20 HIS C CG  
1614 N ND1 . HIS C 20 ? 0.2360 0.4290 0.3255 -0.0442 0.0289  -0.0354 20 HIS C ND1 
1615 C CD2 . HIS C 20 ? 0.2995 0.4596 0.3809 -0.0115 0.0631  -0.0333 20 HIS C CD2 
1616 C CE1 . HIS C 20 ? 0.2737 0.5023 0.3850 -0.0294 0.0306  -0.0329 20 HIS C CE1 
1617 N NE2 . HIS C 20 ? 0.3204 0.5300 0.4282 -0.0105 0.0527  -0.0332 20 HIS C NE2 
1618 N N   . TRP C 21 ? 0.2653 0.2859 0.2573 -0.0067 0.0293  -0.0345 21 TRP C N   
1619 C CA  . TRP C 21 ? 0.2775 0.2763 0.2570 -0.0060 0.0245  -0.0374 21 TRP C CA  
1620 C C   . TRP C 21 ? 0.2957 0.2793 0.2730 0.0081  0.0471  -0.0320 21 TRP C C   
1621 O O   . TRP C 21 ? 0.3093 0.2863 0.2735 0.0297  0.0569  -0.0234 21 TRP C O   
1622 C CB  . TRP C 21 ? 0.3308 0.3115 0.2853 0.0106  -0.0002 -0.0380 21 TRP C CB  
1623 C CG  . TRP C 21 ? 0.3506 0.3238 0.3006 0.0001  -0.0127 -0.0449 21 TRP C CG  
1624 C CD1 . TRP C 21 ? 0.3689 0.3365 0.3158 0.0091  -0.0083 -0.0467 21 TRP C CD1 
1625 C CD2 . TRP C 21 ? 0.3242 0.2989 0.2739 -0.0213 -0.0313 -0.0496 21 TRP C CD2 
1626 N NE1 . TRP C 21 ? 0.3423 0.3136 0.2922 -0.0061 -0.0226 -0.0558 21 TRP C NE1 
1627 C CE2 . TRP C 21 ? 0.3383 0.3117 0.2880 -0.0269 -0.0354 -0.0577 21 TRP C CE2 
1628 C CE3 . TRP C 21 ? 0.3557 0.3338 0.3051 -0.0354 -0.0448 -0.0453 21 TRP C CE3 
1629 C CZ2 . TRP C 21 ? 0.3954 0.3713 0.3450 -0.0501 -0.0497 -0.0641 21 TRP C CZ2 
1630 C CZ3 . TRP C 21 ? 0.3707 0.3451 0.3149 -0.0573 -0.0593 -0.0474 21 TRP C CZ3 
1631 C CH2 . TRP C 21 ? 0.3729 0.3463 0.3172 -0.0664 -0.0603 -0.0580 21 TRP C CH2 
1632 N N   . PRO C 22 ? 0.2775 0.2545 0.2662 -0.0016 0.0566  -0.0355 22 PRO C N   
1633 C CA  . PRO C 22 ? 0.2928 0.2497 0.2799 0.0159  0.0776  -0.0251 22 PRO C CA  
1634 C C   . PRO C 22 ? 0.3273 0.2735 0.2820 0.0479  0.0631  -0.0153 22 PRO C C   
1635 O O   . PRO C 22 ? 0.3403 0.2907 0.2840 0.0512  0.0384  -0.0227 22 PRO C O   
1636 C CB  . PRO C 22 ? 0.2916 0.2457 0.3011 0.0016  0.0844  -0.0342 22 PRO C CB  
1637 C CG  . PRO C 22 ? 0.2637 0.2370 0.2728 -0.0164 0.0584  -0.0483 22 PRO C CG  
1638 C CD  . PRO C 22 ? 0.2920 0.2797 0.2958 -0.0276 0.0496  -0.0485 22 PRO C CD  
1639 N N   . ALA C 23 ? 0.3408 0.2756 0.2790 0.0688  0.0798  0.0005  23 ALA C N   
1640 C CA  . ALA C 23 ? 0.3658 0.2979 0.2663 0.0980  0.0663  0.0079  23 ALA C CA  
1641 C C   . ALA C 23 ? 0.4562 0.3733 0.3394 0.1186  0.0902  0.0311  23 ALA C C   
1642 O O   . ALA C 23 ? 0.4141 0.3176 0.3171 0.1092  0.1190  0.0413  23 ALA C O   
1643 C CB  . ALA C 23 ? 0.3639 0.3054 0.2484 0.1018  0.0544  -0.0011 23 ALA C CB  
1644 N N   . ARG C 24 ? 0.4441 0.3635 0.2881 0.1454  0.0788  0.0393  24 ARG C N   
1645 C CA  . ARG C 24 ? 0.4894 0.3964 0.3072 0.1665  0.1005  0.0658  24 ARG C CA  
1646 C C   . ARG C 24 ? 0.5087 0.4293 0.2808 0.1856  0.0922  0.0644  24 ARG C C   
1647 O O   . ARG C 24 ? 0.5067 0.4417 0.2660 0.1880  0.0649  0.0432  24 ARG C O   
1648 C CB  . ARG C 24 ? 0.5085 0.4054 0.3226 0.1853  0.0980  0.0852  24 ARG C CB  
1649 C CG  . ARG C 24 ? 0.5183 0.4383 0.3170 0.1994  0.0621  0.0747  24 ARG C CG  
1650 C CD  . ARG C 24 ? 0.6277 0.5472 0.4133 0.2284  0.0597  0.1009  24 ARG C CD  
1651 N NE  . ARG C 24 ? 0.7262 0.6802 0.4922 0.2425  0.0233  0.0891  24 ARG C NE  
1652 C CZ  . ARG C 24 ? 0.7923 0.7637 0.5738 0.2570  0.0071  0.0941  24 ARG C CZ  
1653 N NH1 . ARG C 24 ? 0.7615 0.7141 0.5803 0.2613  0.0244  0.1097  24 ARG C NH1 
1654 N NH2 . ARG C 24 ? 0.8567 0.8676 0.6193 0.2671  -0.0265 0.0805  24 ARG C NH2 
1655 N N   . ILE C 25 ? 0.5485 0.4628 0.2968 0.1965  0.1188  0.0852  25 ILE C N   
1656 C CA  . ILE C 25 ? 0.5850 0.5145 0.2840 0.2161  0.1162  0.0846  25 ILE C CA  
1657 C C   . ILE C 25 ? 0.7401 0.6781 0.3974 0.2410  0.0940  0.0946  25 ILE C C   
1658 O O   . ILE C 25 ? 0.7139 0.6402 0.3647 0.2537  0.1014  0.1240  25 ILE C O   
1659 C CB  . ILE C 25 ? 0.6425 0.5665 0.3273 0.2178  0.1551  0.1061  25 ILE C CB  
1660 C CG1 . ILE C 25 ? 0.6142 0.5391 0.3472 0.1911  0.1774  0.0958  25 ILE C CG1 
1661 C CG2 . ILE C 25 ? 0.6643 0.6084 0.2954 0.2374  0.1551  0.1026  25 ILE C CG2 
1662 C CD1 . ILE C 25 ? 0.5492 0.4975 0.3004 0.1840  0.1600  0.0634  25 ILE C CD1 
1663 N N   . ASP C 26 ? 0.6131 1.0089 0.6072 0.2224  0.0486  0.0468  26 ASP C N   
1664 C CA  . ASP C 26 ? 0.6445 1.0519 0.6057 0.2223  0.0262  0.0738  26 ASP C CA  
1665 C C   . ASP C 26 ? 0.7022 1.0358 0.6066 0.2100  0.0354  0.0784  26 ASP C C   
1666 O O   . ASP C 26 ? 0.7179 0.9893 0.6104 0.2004  0.0614  0.0612  26 ASP C O   
1667 C CB  . ASP C 26 ? 0.6138 1.0805 0.5876 0.2034  0.0028  0.0819  26 ASP C CB  
1668 C CG  . ASP C 26 ? 0.5991 1.1393 0.5988 0.2219  -0.0195 0.0975  26 ASP C CG  
1669 O OD1 . ASP C 26 ? 0.6277 1.1748 0.6352 0.2513  -0.0191 0.1031  26 ASP C OD1 
1670 O OD2 . ASP C 26 ? 0.5771 1.1666 0.5895 0.2062  -0.0359 0.1033  26 ASP C OD2 
1671 N N   . ASP C 27 ? 0.7366 1.0790 0.6055 0.2112  0.0142  0.0999  27 ASP C N   
1672 C CA  . ASP C 27 ? 0.7912 1.0746 0.6017 0.1977  0.0172  0.1061  27 ASP C CA  
1673 C C   . ASP C 27 ? 0.7774 1.0964 0.5822 0.1690  -0.0052 0.1088  27 ASP C C   
1674 O O   . ASP C 27 ? 0.7907 1.1800 0.6330 0.1640  -0.0236 0.1102  27 ASP C O   
1675 C CB  . ASP C 27 ? 0.8550 1.1146 0.6205 0.2275  0.0118  0.1276  27 ASP C CB  
1676 N N   . ILE C 28 ? 0.8157 1.0840 0.5742 0.1490  -0.0008 0.1082  28 ILE C N   
1677 C CA  . ILE C 28 ? 0.8123 1.1080 0.5605 0.1210  -0.0204 0.1093  28 ILE C CA  
1678 C C   . ILE C 28 ? 0.9158 1.2031 0.6100 0.1328  -0.0379 0.1256  28 ILE C C   
1679 O O   . ILE C 28 ? 1.0086 1.2251 0.6505 0.1398  -0.0230 0.1298  28 ILE C O   
1680 C CB  . ILE C 28 ? 0.8436 1.0932 0.5841 0.0865  -0.0025 0.0922  28 ILE C CB  
1681 C CG1 . ILE C 28 ? 0.7917 1.0732 0.5865 0.0744  0.0047  0.0772  28 ILE C CG1 
1682 C CG2 . ILE C 28 ? 0.9176 1.1726 0.6280 0.0604  -0.0187 0.0949  28 ILE C CG2 
1683 C CD1 . ILE C 28 ? 0.8610 1.2256 0.6951 0.0738  -0.0174 0.0845  28 ILE C CD1 
1684 N N   . ALA C 29 ? 0.8669 1.2268 0.5732 0.1368  -0.0685 0.1333  29 ALA C N   
1685 C CA  . ALA C 29 ? 0.9252 1.2898 0.5821 0.1515  -0.0901 0.1455  29 ALA C CA  
1686 C C   . ALA C 29 ? 0.9586 1.2794 0.5701 0.1233  -0.0871 0.1393  29 ALA C C   
1687 O O   . ALA C 29 ? 0.9361 1.2550 0.5682 0.0868  -0.0795 0.1250  29 ALA C O   
1688 C CB  . ALA C 29 ? 0.9050 1.3667 0.5945 0.1574  -0.1238 0.1475  29 ALA C CB  
1689 N N   . ASP C 30 ? 1.0299 1.3122 0.5758 0.1426  -0.0920 0.1507  30 ASP C N   
1690 C CA  . ASP C 30 ? 1.0843 1.3265 0.5803 0.1199  -0.0910 0.1457  30 ASP C CA  
1691 C C   . ASP C 30 ? 1.0451 1.3616 0.5651 0.0924  -0.1191 0.1338  30 ASP C C   
1692 O O   . ASP C 30 ? 1.0569 1.4410 0.5796 0.1092  -0.1496 0.1369  30 ASP C O   
1693 C CB  . ASP C 30 ? 1.1591 1.3503 0.5751 0.1532  -0.0923 0.1626  30 ASP C CB  
1694 N N   . GLY C 31 ? 1.0121 1.3173 0.5519 0.0501  -0.1076 0.1180  31 GLY C N   
1695 C CA  . GLY C 31 ? 0.9857 1.3538 0.5553 0.0182  -0.1263 0.1038  31 GLY C CA  
1696 C C   . GLY C 31 ? 0.9147 1.3128 0.5516 -0.0091 -0.1152 0.0930  31 GLY C C   
1697 O O   . GLY C 31 ? 0.8958 1.3134 0.5520 -0.0447 -0.1161 0.0794  31 GLY C O   
1698 N N   . ALA C 32 ? 0.8794 1.2794 0.5501 0.0084  -0.1034 0.0987  32 ALA C N   
1699 C CA  . ALA C 32 ? 0.8193 1.2457 0.5480 -0.0104 -0.0919 0.0906  32 ALA C CA  
1700 C C   . ALA C 32 ? 0.8416 1.2056 0.5633 -0.0383 -0.0663 0.0791  32 ALA C C   
1701 O O   . ALA C 32 ? 0.8431 1.1398 0.5199 -0.0408 -0.0540 0.0774  32 ALA C O   
1702 C CB  . ALA C 32 ? 0.7878 1.2322 0.5497 0.0196  -0.0865 0.0984  32 ALA C CB  
1703 N N   . VAL C 33 ? 0.8042 1.1902 0.5699 -0.0580 -0.0570 0.0711  33 VAL C N   
1704 C CA  . VAL C 33 ? 0.7988 1.1318 0.5627 -0.0801 -0.0336 0.0592  33 VAL C CA  
1705 C C   . VAL C 33 ? 0.8126 1.1013 0.5761 -0.0576 -0.0143 0.0571  33 VAL C C   
1706 O O   . VAL C 33 ? 0.7140 1.0320 0.5073 -0.0325 -0.0145 0.0619  33 VAL C O   
1707 C CB  . VAL C 33 ? 0.8006 1.1674 0.6070 -0.1024 -0.0278 0.0529  33 VAL C CB  
1708 C CG1 . VAL C 33 ? 0.8098 1.1233 0.6032 -0.1305 -0.0091 0.0398  33 VAL C CG1 
1709 C CG2 . VAL C 33 ? 0.8402 1.2696 0.6639 -0.1181 -0.0461 0.0541  33 VAL C CG2 
1710 N N   . LYS C 34 ? 0.8317 1.0512 0.5640 -0.0676 0.0035  0.0473  34 LYS C N   
1711 C CA  . LYS C 34 ? 0.7598 0.9339 0.4928 -0.0498 0.0250  0.0393  34 LYS C CA  
1712 C C   . LYS C 34 ? 0.7291 0.9209 0.5082 -0.0493 0.0365  0.0264  34 LYS C C   
1713 O O   . LYS C 34 ? 0.6848 0.9011 0.4827 -0.0682 0.0339  0.0234  34 LYS C O   
1714 C CB  . LYS C 34 ? 0.7997 0.8959 0.4894 -0.0644 0.0435  0.0288  34 LYS C CB  
1715 N N   . PRO C 35 ? 0.6950 0.8754 0.4922 -0.0259 0.0503  0.0180  35 PRO C N   
1716 C CA  . PRO C 35 ? 0.6523 0.8463 0.4880 -0.0217 0.0617  0.0016  35 PRO C CA  
1717 C C   . PRO C 35 ? 0.6797 0.8290 0.5052 -0.0465 0.0769  -0.0179 35 PRO C C   
1718 O O   . PRO C 35 ? 0.6901 0.7875 0.4800 -0.0643 0.0842  -0.0221 35 PRO C O   
1719 C CB  . PRO C 35 ? 0.6476 0.8316 0.4998 0.0075  0.0746  -0.0083 35 PRO C CB  
1720 C CG  . PRO C 35 ? 0.6866 0.8574 0.5109 0.0209  0.0689  0.0089  35 PRO C CG  
1721 C CD  . PRO C 35 ? 0.7230 0.8766 0.5048 -0.0008 0.0574  0.0219  35 PRO C CD  
1722 N N   . PRO C 36 ? 0.6210 0.7884 0.4745 -0.0466 0.0822  -0.0299 36 PRO C N   
1723 C CA  . PRO C 36 ? 0.6214 0.7460 0.4706 -0.0617 0.0989  -0.0538 36 PRO C CA  
1724 C C   . PRO C 36 ? 0.6371 0.7146 0.4816 -0.0538 0.1178  -0.0756 36 PRO C C   
1725 O O   . PRO C 36 ? 0.6397 0.7237 0.4929 -0.0315 0.1199  -0.0736 36 PRO C O   
1726 C CB  . PRO C 36 ? 0.5835 0.7455 0.4666 -0.0472 0.1003  -0.0618 36 PRO C CB  
1727 C CG  . PRO C 36 ? 0.5707 0.7881 0.4658 -0.0405 0.0841  -0.0361 36 PRO C CG  
1728 C CD  . PRO C 36 ? 0.5859 0.8134 0.4728 -0.0316 0.0734  -0.0211 36 PRO C CD  
1729 N N   . PRO C 37 ? 0.6505 0.6788 0.4825 -0.0726 0.1338  -0.0976 37 PRO C N   
1730 C CA  . PRO C 37 ? 0.6692 0.6493 0.4997 -0.0685 0.1568  -0.1223 37 PRO C CA  
1731 C C   . PRO C 37 ? 0.6418 0.6501 0.5143 -0.0377 0.1643  -0.1405 37 PRO C C   
1732 O O   . PRO C 37 ? 0.6045 0.6551 0.5099 -0.0234 0.1594  -0.1520 37 PRO C O   
1733 C CB  . PRO C 37 ? 0.6732 0.6145 0.4986 -0.0916 0.1709  -0.1483 37 PRO C CB  
1734 C CG  . PRO C 37 ? 0.6834 0.6372 0.4915 -0.1135 0.1552  -0.1299 37 PRO C CG  
1735 C CD  . PRO C 37 ? 0.7160 0.7252 0.5297 -0.1023 0.1328  -0.0987 37 PRO C CD  
1736 N N   . ASN C 38 ? 0.6651 0.6486 0.5339 -0.0261 0.1772  -0.1424 38 ASN C N   
1737 C CA  . ASN C 38 ? 0.6486 0.6468 0.5564 -0.0001 0.1907  -0.1651 38 ASN C CA  
1738 C C   . ASN C 38 ? 0.6111 0.6809 0.5492 0.0273  0.1709  -0.1505 38 ASN C C   
1739 O O   . ASN C 38 ? 0.5861 0.6836 0.5642 0.0501  0.1781  -0.1736 38 ASN C O   
1740 C CB  . ASN C 38 ? 0.6312 0.6194 0.5703 -0.0023 0.2098  -0.2111 38 ASN C CB  
1741 C CG  . ASN C 38 ? 0.6862 0.6671 0.6600 0.0157  0.2335  -0.2431 38 ASN C CG  
1742 O OD1 . ASN C 38 ? 0.7956 0.8108 0.8127 0.0312  0.2312  -0.2699 38 ASN C OD1 
1743 N ND2 . ASN C 38 ? 0.7785 0.7119 0.7309 0.0142  0.2509  -0.2340 38 ASN C ND2 
1744 N N   . LYS C 39 ? 0.4411 0.7015 0.3965 0.1662  0.1551  -0.0481 39 LYS C N   
1745 C CA  . LYS C 39 ? 0.4143 0.6423 0.3744 0.1574  0.1318  -0.0445 39 LYS C CA  
1746 C C   . LYS C 39 ? 0.4364 0.6708 0.3428 0.1707  0.1271  -0.0263 39 LYS C C   
1747 O O   . LYS C 39 ? 0.4736 0.7480 0.3365 0.1915  0.1340  -0.0296 39 LYS C O   
1748 C CB  . LYS C 39 ? 0.4285 0.6569 0.4135 0.1542  0.1172  -0.0857 39 LYS C CB  
1749 C CG  . LYS C 39 ? 0.4498 0.6514 0.4896 0.1454  0.1186  -0.0958 39 LYS C CG  
1750 C CD  . LYS C 39 ? 0.4474 0.6333 0.5104 0.1385  0.1219  -0.0619 39 LYS C CD  
1751 C CE  . LYS C 39 ? 0.5641 0.7401 0.6785 0.1414  0.1234  -0.0698 39 LYS C CE  
1752 N NZ  . LYS C 39 ? 0.5730 0.7738 0.7127 0.1425  0.1350  -0.0533 39 LYS C NZ  
1753 N N   . TYR C 40 ? 0.4189 0.6178 0.3271 0.1623  0.1153  -0.0071 40 TYR C N   
1754 C CA  . TYR C 40 ? 0.4438 0.6394 0.3122 0.1771  0.1081  0.0110  40 TYR C CA  
1755 C C   . TYR C 40 ? 0.4592 0.6700 0.3362 0.1766  0.0833  -0.0197 40 TYR C C   
1756 O O   . TYR C 40 ? 0.3874 0.5776 0.3047 0.1553  0.0744  -0.0378 40 TYR C O   
1757 C CB  . TYR C 40 ? 0.4363 0.5794 0.3091 0.1652  0.1156  0.0468  40 TYR C CB  
1758 C CG  . TYR C 40 ? 0.5227 0.6467 0.3875 0.1616  0.1460  0.0785  40 TYR C CG  
1759 C CD1 . TYR C 40 ? 0.4510 0.5718 0.3587 0.1384  0.1572  0.0744  40 TYR C CD1 
1760 C CD2 . TYR C 40 ? 0.5267 0.6369 0.3425 0.1826  0.1661  0.1133  40 TYR C CD2 
1761 C CE1 . TYR C 40 ? 0.4983 0.6079 0.4064 0.1296  0.1889  0.0981  40 TYR C CE1 
1762 C CE2 . TYR C 40 ? 0.5677 0.6528 0.3777 0.1748  0.2018  0.1431  40 TYR C CE2 
1763 C CZ  . TYR C 40 ? 0.5524 0.6398 0.4117 0.1449  0.2137  0.1323  40 TYR C CZ  
1764 O OH  . TYR C 40 ? 0.5934 0.6623 0.4547 0.1318  0.2529  0.1567  40 TYR C OH  
1765 N N   . PRO C 41 ? 0.4386 0.6877 0.2792 0.2007  0.0734  -0.0244 41 PRO C N   
1766 C CA  . PRO C 41 ? 0.4181 0.6856 0.2733 0.1972  0.0518  -0.0529 41 PRO C CA  
1767 C C   . PRO C 41 ? 0.4678 0.6865 0.3314 0.1891  0.0484  -0.0264 41 PRO C C   
1768 O O   . PRO C 41 ? 0.4297 0.6277 0.2641 0.2067  0.0564  0.0103  41 PRO C O   
1769 C CB  . PRO C 41 ? 0.4552 0.7916 0.2709 0.2295  0.0403  -0.0632 41 PRO C CB  
1770 C CG  . PRO C 41 ? 0.5409 0.8676 0.3119 0.2535  0.0564  -0.0176 41 PRO C CG  
1771 C CD  . PRO C 41 ? 0.5066 0.7914 0.2901 0.2348  0.0824  -0.0036 41 PRO C CD  
1772 N N   . ILE C 42 ? 0.3665 0.5639 0.2684 0.1629  0.0400  -0.0453 42 ILE C N   
1773 C CA  . ILE C 42 ? 0.3508 0.5049 0.2629 0.1506  0.0377  -0.0266 42 ILE C CA  
1774 C C   . ILE C 42 ? 0.3904 0.5720 0.3109 0.1513  0.0233  -0.0518 42 ILE C C   
1775 O O   . ILE C 42 ? 0.3484 0.5627 0.2899 0.1407  0.0173  -0.0900 42 ILE C O   
1776 C CB  . ILE C 42 ? 0.3614 0.4719 0.3061 0.1210  0.0416  -0.0224 42 ILE C CB  
1777 C CG1 . ILE C 42 ? 0.4486 0.5466 0.3944 0.1201  0.0556  -0.0031 42 ILE C CG1 
1778 C CG2 . ILE C 42 ? 0.3403 0.4163 0.2908 0.1078  0.0386  -0.0087 42 ILE C CG2 
1779 C CD1 . ILE C 42 ? 0.4291 0.5132 0.3469 0.1330  0.0698  0.0288  42 ILE C CD1 
1780 N N   . PHE C 43 ? 0.3487 0.5170 0.2575 0.1623  0.0214  -0.0336 43 PHE C N   
1781 C CA  . PHE C 43 ? 0.3686 0.5581 0.2922 0.1603  0.0107  -0.0543 43 PHE C CA  
1782 C C   . PHE C 43 ? 0.3980 0.5326 0.3364 0.1363  0.0161  -0.0413 43 PHE C C   
1783 O O   . PHE C 43 ? 0.3640 0.4570 0.2891 0.1408  0.0252  -0.0120 43 PHE C O   
1784 C CB  . PHE C 43 ? 0.4034 0.6315 0.2999 0.2015  0.0040  -0.0455 43 PHE C CB  
1785 C CG  . PHE C 43 ? 0.3611 0.6197 0.2771 0.2039  -0.0061 -0.0673 43 PHE C CG  
1786 C CD1 . PHE C 43 ? 0.4000 0.7310 0.3409 0.1981  -0.0187 -0.1139 43 PHE C CD1 
1787 C CD2 . PHE C 43 ? 0.3698 0.5888 0.2836 0.2109  -0.0002 -0.0461 43 PHE C CD2 
1788 C CE1 . PHE C 43 ? 0.3726 0.7416 0.3371 0.1996  -0.0258 -0.1369 43 PHE C CE1 
1789 C CE2 . PHE C 43 ? 0.3847 0.6366 0.3189 0.2150  -0.0074 -0.0679 43 PHE C CE2 
1790 C CZ  . PHE C 43 ? 0.4320 0.7615 0.3923 0.2095  -0.0204 -0.1122 43 PHE C CZ  
1791 N N   . PHE C 44 ? 0.3084 0.4431 0.2736 0.1095  0.0135  -0.0645 44 PHE C N   
1792 C CA  . PHE C 44 ? 0.3176 0.4108 0.2913 0.0870  0.0179  -0.0549 44 PHE C CA  
1793 C C   . PHE C 44 ? 0.3573 0.4663 0.3326 0.0946  0.0157  -0.0642 44 PHE C C   
1794 O O   . PHE C 44 ? 0.3422 0.4984 0.3325 0.0968  0.0107  -0.0926 44 PHE C O   
1795 C CB  . PHE C 44 ? 0.2958 0.3745 0.2902 0.0575  0.0211  -0.0669 44 PHE C CB  
1796 C CG  . PHE C 44 ? 0.2866 0.3461 0.2843 0.0535  0.0242  -0.0564 44 PHE C CG  
1797 C CD1 . PHE C 44 ? 0.3394 0.3677 0.3331 0.0478  0.0256  -0.0310 44 PHE C CD1 
1798 C CD2 . PHE C 44 ? 0.4010 0.4809 0.4103 0.0557  0.0262  -0.0772 44 PHE C CD2 
1799 C CE1 . PHE C 44 ? 0.2898 0.3102 0.2923 0.0480  0.0280  -0.0229 44 PHE C CE1 
1800 C CE2 . PHE C 44 ? 0.3789 0.4417 0.3948 0.0555  0.0312  -0.0693 44 PHE C CE2 
1801 C CZ  . PHE C 44 ? 0.2841 0.3185 0.2972 0.0534  0.0315  -0.0403 44 PHE C CZ  
1802 N N   . PHE C 45 ? 0.3754 0.4492 0.3403 0.0978  0.0214  -0.0452 45 PHE C N   
1803 C CA  . PHE C 45 ? 0.3524 0.4366 0.3221 0.1053  0.0223  -0.0558 45 PHE C CA  
1804 C C   . PHE C 45 ? 0.3093 0.4013 0.2977 0.0739  0.0241  -0.0775 45 PHE C C   
1805 O O   . PHE C 45 ? 0.3189 0.3883 0.3092 0.0474  0.0268  -0.0736 45 PHE C O   
1806 C CB  . PHE C 45 ? 0.3351 0.3707 0.2925 0.1121  0.0332  -0.0355 45 PHE C CB  
1807 C CG  . PHE C 45 ? 0.3982 0.4184 0.3353 0.1475  0.0396  -0.0102 45 PHE C CG  
1808 C CD1 . PHE C 45 ? 0.3989 0.4549 0.3278 0.1890  0.0348  -0.0095 45 PHE C CD1 
1809 C CD2 . PHE C 45 ? 0.3875 0.3618 0.3138 0.1409  0.0521  0.0139  45 PHE C CD2 
1810 C CE1 . PHE C 45 ? 0.4912 0.5288 0.3926 0.2278  0.0437  0.0221  45 PHE C CE1 
1811 C CE2 . PHE C 45 ? 0.4329 0.3846 0.3368 0.1725  0.0653  0.0422  45 PHE C CE2 
1812 C CZ  . PHE C 45 ? 0.4629 0.4425 0.3500 0.2180  0.0614  0.0497  45 PHE C CZ  
1813 N N   . GLY C 46 ? 0.2971 0.4233 0.2987 0.0800  0.0245  -0.0985 46 GLY C N   
1814 C CA  . GLY C 46 ? 0.2872 0.4211 0.3047 0.0493  0.0322  -0.1179 46 GLY C CA  
1815 C C   . GLY C 46 ? 0.3485 0.5202 0.3897 0.0336  0.0330  -0.1436 46 GLY C C   
1816 O O   . GLY C 46 ? 0.2907 0.5127 0.3573 0.0300  0.0360  -0.1742 46 GLY C O   
1817 N N   . THR C 47 ? 0.2895 0.4391 0.3278 0.0229  0.0329  -0.1355 47 THR C N   
1818 C CA  . THR C 47 ? 0.2766 0.4527 0.3414 0.0052  0.0386  -0.1645 47 THR C CA  
1819 C C   . THR C 47 ? 0.3635 0.6030 0.4384 0.0294  0.0254  -0.1891 47 THR C C   
1820 O O   . THR C 47 ? 0.3249 0.6150 0.4314 0.0161  0.0287  -0.2302 47 THR C O   
1821 C CB  . THR C 47 ? 0.3194 0.4437 0.3795 -0.0120 0.0465  -0.1478 47 THR C CB  
1822 O OG1 . THR C 47 ? 0.2950 0.4095 0.3375 0.0104  0.0351  -0.1284 47 THR C OG1 
1823 C CG2 . THR C 47 ? 0.2942 0.3668 0.3376 -0.0296 0.0562  -0.1202 47 THR C CG2 
1824 N N   . HIS C 48 ? 0.2884 0.5285 0.3363 0.0637  0.0128  -0.1661 48 HIS C N   
1825 C CA  . HIS C 48 ? 0.2844 0.5865 0.3276 0.0946  -0.0009 -0.1807 48 HIS C CA  
1826 C C   . HIS C 48 ? 0.3115 0.6268 0.3659 0.0799  0.0010  -0.2037 48 HIS C C   
1827 O O   . HIS C 48 ? 0.3045 0.6907 0.3649 0.0947  -0.0091 -0.2350 48 HIS C O   
1828 C CB  . HIS C 48 ? 0.2881 0.6727 0.3518 0.1121  -0.0104 -0.2132 48 HIS C CB  
1829 C CG  . HIS C 48 ? 0.3094 0.6810 0.3687 0.1274  -0.0088 -0.1963 48 HIS C CG  
1830 N ND1 . HIS C 48 ? 0.3795 0.8035 0.4710 0.1228  -0.0075 -0.2276 48 HIS C ND1 
1831 C CD2 . HIS C 48 ? 0.3649 0.6759 0.3959 0.1444  -0.0046 -0.1560 48 HIS C CD2 
1832 C CE1 . HIS C 48 ? 0.3614 0.7575 0.4421 0.1404  -0.0038 -0.2062 48 HIS C CE1 
1833 N NE2 . HIS C 48 ? 0.4089 0.7335 0.4532 0.1524  -0.0013 -0.1639 48 HIS C NE2 
1834 N N   . GLU C 49 ? 0.2829 0.5340 0.3391 0.0544  0.0135  -0.1894 49 GLU C N   
1835 C CA  . GLU C 49 ? 0.3727 0.6210 0.4400 0.0434  0.0195  -0.2076 49 GLU C CA  
1836 C C   . GLU C 49 ? 0.3323 0.5733 0.3685 0.0703  0.0130  -0.1811 49 GLU C C   
1837 O O   . GLU C 49 ? 0.3716 0.5980 0.3791 0.0924  0.0077  -0.1455 49 GLU C O   
1838 C CB  . GLU C 49 ? 0.4012 0.5824 0.4858 0.0106  0.0384  -0.2005 49 GLU C CB  
1839 C CG  . GLU C 49 ? 0.3411 0.5251 0.4541 -0.0191 0.0523  -0.2246 49 GLU C CG  
1840 C CD  . GLU C 49 ? 0.4596 0.5689 0.5787 -0.0453 0.0743  -0.2059 49 GLU C CD  
1841 O OE1 . GLU C 49 ? 0.3626 0.4237 0.4622 -0.0356 0.0728  -0.1698 49 GLU C OE1 
1842 O OE2 . GLU C 49 ? 0.4703 0.5718 0.6141 -0.0742 0.0946  -0.2261 49 GLU C OE2 
1843 N N   . THR C 50 ? 0.3459 0.5958 0.3896 0.0669  0.0177  -0.2013 50 THR C N   
1844 C CA  . THR C 50 ? 0.3181 0.5679 0.3338 0.0903  0.0157  -0.1802 50 THR C CA  
1845 C C   . THR C 50 ? 0.3937 0.6004 0.4259 0.0749  0.0295  -0.1811 50 THR C C   
1846 O O   . THR C 50 ? 0.3753 0.5615 0.4397 0.0506  0.0410  -0.2069 50 THR C O   
1847 C CB  . THR C 50 ? 0.3569 0.6882 0.3546 0.1168  0.0049  -0.2067 50 THR C CB  
1848 O OG1 . THR C 50 ? 0.4170 0.7834 0.4518 0.0928  0.0044  -0.2557 50 THR C OG1 
1849 C CG2 . THR C 50 ? 0.3371 0.7130 0.3139 0.1448  -0.0100 -0.1966 50 THR C CG2 
1850 N N   . ALA C 51 ? 0.3205 0.5124 0.3321 0.0907  0.0317  -0.1524 51 ALA C N   
1851 C CA  . ALA C 51 ? 0.3361 0.4961 0.3643 0.0843  0.0440  -0.1510 51 ALA C CA  
1852 C C   . ALA C 51 ? 0.4092 0.5831 0.4114 0.1059  0.0464  -0.1285 51 ALA C C   
1853 O O   . ALA C 51 ? 0.4365 0.6309 0.4058 0.1238  0.0414  -0.1080 51 ALA C O   
1854 C CB  . ALA C 51 ? 0.3543 0.4523 0.4005 0.0684  0.0489  -0.1243 51 ALA C CB  
1855 N N   . PHE C 52 ? 0.3602 0.5204 0.3785 0.1053  0.0577  -0.1312 52 PHE C N   
1856 C CA  . PHE C 52 ? 0.4008 0.5722 0.4017 0.1208  0.0657  -0.1100 52 PHE C CA  
1857 C C   . PHE C 52 ? 0.4167 0.5472 0.4391 0.1130  0.0702  -0.0787 52 PHE C C   
1858 O O   . PHE C 52 ? 0.3764 0.4784 0.4302 0.1043  0.0716  -0.0839 52 PHE C O   
1859 C CB  . PHE C 52 ? 0.3727 0.5786 0.3773 0.1294  0.0763  -0.1441 52 PHE C CB  
1860 C CG  . PHE C 52 ? 0.4603 0.7277 0.4384 0.1404  0.0698  -0.1784 52 PHE C CG  
1861 C CD1 . PHE C 52 ? 0.4131 0.7155 0.3435 0.1617  0.0629  -0.1549 52 PHE C CD1 
1862 C CD2 . PHE C 52 ? 0.4841 0.7657 0.4870 0.1249  0.0679  -0.2257 52 PHE C CD2 
1863 C CE1 . PHE C 52 ? 0.5165 0.8738 0.4266 0.1696  0.0470  -0.1745 52 PHE C CE1 
1864 C CE2 . PHE C 52 ? 0.5135 0.8539 0.5000 0.1269  0.0530  -0.2498 52 PHE C CE2 
1865 C CZ  . PHE C 52 ? 0.4955 0.8793 0.4362 0.1518  0.0400  -0.2241 52 PHE C CZ  
1866 N N   . LEU C 53 ? 0.3339 0.4632 0.3402 0.1169  0.0742  -0.0468 53 LEU C N   
1867 C CA  . LEU C 53 ? 0.3291 0.4363 0.3601 0.1071  0.0765  -0.0237 53 LEU C CA  
1868 C C   . LEU C 53 ? 0.3348 0.4595 0.3623 0.1117  0.0931  -0.0079 53 LEU C C   
1869 O O   . LEU C 53 ? 0.3685 0.5041 0.3617 0.1205  0.1033  0.0025  53 LEU C O   
1870 C CB  . LEU C 53 ? 0.3646 0.4457 0.3918 0.0938  0.0663  -0.0047 53 LEU C CB  
1871 C CG  . LEU C 53 ? 0.5207 0.5802 0.5607 0.0840  0.0541  -0.0130 53 LEU C CG  
1872 C CD1 . LEU C 53 ? 0.4354 0.4779 0.4650 0.0722  0.0462  0.0019  53 LEU C CD1 
1873 C CD2 . LEU C 53 ? 0.4509 0.5013 0.5226 0.0843  0.0542  -0.0104 53 LEU C CD2 
1874 N N   . GLY C 54 ? 0.3665 0.4957 0.4301 0.1072  0.0975  -0.0044 54 GLY C N   
1875 C CA  . GLY C 54 ? 0.4189 0.5691 0.4916 0.1052  0.1163  0.0076  54 GLY C CA  
1876 C C   . GLY C 54 ? 0.3615 0.4978 0.4394 0.0861  0.1187  0.0290  54 GLY C C   
1877 O O   . GLY C 54 ? 0.3185 0.4338 0.3991 0.0760  0.1022  0.0323  54 GLY C O   
1878 N N   . PRO C 55 ? 0.3960 0.5443 0.4777 0.0783  0.1430  0.0405  55 PRO C N   
1879 C CA  . PRO C 55 ? 0.3634 0.4923 0.4521 0.0551  0.1528  0.0553  55 PRO C CA  
1880 C C   . PRO C 55 ? 0.3364 0.4801 0.4705 0.0370  0.1352  0.0458  55 PRO C C   
1881 O O   . PRO C 55 ? 0.3862 0.5100 0.5217 0.0177  0.1333  0.0486  55 PRO C O   
1882 C CB  . PRO C 55 ? 0.4213 0.5632 0.5127 0.0482  0.1894  0.0659  55 PRO C CB  
1883 C CG  . PRO C 55 ? 0.4269 0.5979 0.5032 0.0714  0.1961  0.0584  55 PRO C CG  
1884 C CD  . PRO C 55 ? 0.3757 0.5563 0.4610 0.0870  0.1665  0.0368  55 PRO C CD  
1885 N N   . LYS C 56 ? 0.3250 0.5055 0.4949 0.0460  0.1221  0.0337  56 LYS C N   
1886 C CA  . LYS C 56 ? 0.3747 0.5811 0.5821 0.0372  0.1013  0.0275  56 LYS C CA  
1887 C C   . LYS C 56 ? 0.3589 0.5335 0.5419 0.0355  0.0776  0.0309  56 LYS C C   
1888 O O   . LYS C 56 ? 0.3173 0.5107 0.5177 0.0230  0.0628  0.0273  56 LYS C O   
1889 C CB  . LYS C 56 ? 0.3215 0.5684 0.5655 0.0592  0.0914  0.0200  56 LYS C CB  
1890 N N   . ASP C 57 ? 0.3268 0.4624 0.4713 0.0470  0.0744  0.0342  57 ASP C N   
1891 C CA  . ASP C 57 ? 0.3774 0.4853 0.5005 0.0444  0.0564  0.0357  57 ASP C CA  
1892 C C   . ASP C 57 ? 0.3550 0.4310 0.4471 0.0334  0.0637  0.0394  57 ASP C C   
1893 O O   . ASP C 57 ? 0.3095 0.3639 0.3812 0.0337  0.0526  0.0380  57 ASP C O   
1894 C CB  . ASP C 57 ? 0.3435 0.4339 0.4548 0.0626  0.0490  0.0315  57 ASP C CB  
1895 C CG  . ASP C 57 ? 0.4899 0.5972 0.6315 0.0785  0.0437  0.0311  57 ASP C CG  
1896 O OD1 . ASP C 57 ? 0.3999 0.5292 0.5610 0.0782  0.0312  0.0388  57 ASP C OD1 
1897 O OD2 . ASP C 57 ? 0.4403 0.5423 0.5866 0.0937  0.0525  0.0215  57 ASP C OD2 
1898 N N   . LEU C 58 ? 0.3085 0.3785 0.3977 0.0252  0.0855  0.0453  58 LEU C N   
1899 C CA  . LEU C 58 ? 0.3503 0.3819 0.4097 0.0222  0.0967  0.0535  58 LEU C CA  
1900 C C   . LEU C 58 ? 0.3496 0.3701 0.4289 -0.0049 0.1129  0.0523  58 LEU C C   
1901 O O   . LEU C 58 ? 0.4190 0.4596 0.5270 -0.0190 0.1301  0.0506  58 LEU C O   
1902 C CB  . LEU C 58 ? 0.3556 0.3768 0.3824 0.0432  0.1145  0.0667  58 LEU C CB  
1903 C CG  . LEU C 58 ? 0.3428 0.3841 0.3531 0.0666  0.1013  0.0579  58 LEU C CG  
1904 C CD1 . LEU C 58 ? 0.3758 0.4257 0.3529 0.0878  0.1194  0.0683  58 LEU C CD1 
1905 C CD2 . LEU C 58 ? 0.3283 0.3592 0.3240 0.0719  0.0816  0.0486  58 LEU C CD2 
1906 N N   . PHE C 59 ? 0.3590 0.3487 0.4266 -0.0139 0.1110  0.0490  59 PHE C N   
1907 C CA  . PHE C 59 ? 0.4064 0.3824 0.4967 -0.0441 0.1267  0.0380  59 PHE C CA  
1908 C C   . PHE C 59 ? 0.4260 0.3392 0.4892 -0.0392 0.1500  0.0499  59 PHE C C   
1909 O O   . PHE C 59 ? 0.4287 0.3240 0.4652 -0.0220 0.1366  0.0515  59 PHE C O   
1910 C CB  . PHE C 59 ? 0.4133 0.4198 0.5204 -0.0604 0.1004  0.0154  59 PHE C CB  
1911 C CG  . PHE C 59 ? 0.3845 0.4502 0.5143 -0.0561 0.0772  0.0105  59 PHE C CG  
1912 C CD1 . PHE C 59 ? 0.3366 0.4084 0.4487 -0.0301 0.0579  0.0211  59 PHE C CD1 
1913 C CD2 . PHE C 59 ? 0.3819 0.4984 0.5548 -0.0767 0.0770  -0.0063 59 PHE C CD2 
1914 C CE1 . PHE C 59 ? 0.3441 0.4598 0.4772 -0.0203 0.0408  0.0208  59 PHE C CE1 
1915 C CE2 . PHE C 59 ? 0.3235 0.4987 0.5183 -0.0641 0.0549  -0.0076 59 PHE C CE2 
1916 C CZ  . PHE C 59 ? 0.3695 0.5382 0.5422 -0.0336 0.0377  0.0090  59 PHE C CZ  
1917 N N   . PRO C 60 ? 0.4777 0.3549 0.5487 -0.0522 0.1876  0.0590  60 PRO C N   
1918 C CA  . PRO C 60 ? 0.5325 0.3392 0.5752 -0.0397 0.2145  0.0775  60 PRO C CA  
1919 C C   . PRO C 60 ? 0.5421 0.3290 0.5869 -0.0475 0.2028  0.0566  60 PRO C C   
1920 O O   . PRO C 60 ? 0.5671 0.3764 0.6445 -0.0806 0.1950  0.0250  60 PRO C O   
1921 C CB  . PRO C 60 ? 0.5927 0.3626 0.6586 -0.0666 0.2617  0.0832  60 PRO C CB  
1922 C CG  . PRO C 60 ? 0.5630 0.3943 0.6599 -0.0825 0.2589  0.0750  60 PRO C CG  
1923 C CD  . PRO C 60 ? 0.4905 0.3893 0.6024 -0.0816 0.2104  0.0507  60 PRO C CD  
1924 N N   . TYR C 61 ? 0.6134 0.3672 0.6230 -0.0149 0.2009  0.0721  61 TYR C N   
1925 C CA  . TYR C 61 ? 0.5457 0.2889 0.5556 -0.0177 0.1883  0.0509  61 TYR C CA  
1926 C C   . TYR C 61 ? 0.6309 0.3310 0.6694 -0.0520 0.2167  0.0284  61 TYR C C   
1927 O O   . TYR C 61 ? 0.6130 0.3413 0.6734 -0.0807 0.2021  -0.0072 61 TYR C O   
1928 C CB  . TYR C 61 ? 0.6320 0.3511 0.6058 0.0264  0.1865  0.0711  61 TYR C CB  
1929 C CG  . TYR C 61 ? 0.6110 0.3178 0.5880 0.0255  0.1795  0.0486  61 TYR C CG  
1930 C CD1 . TYR C 61 ? 0.5740 0.3283 0.5614 0.0065  0.1503  0.0198  61 TYR C CD1 
1931 C CD2 . TYR C 61 ? 0.6976 0.3422 0.6666 0.0447  0.2062  0.0572  61 TYR C CD2 
1932 C CE1 . TYR C 61 ? 0.6440 0.3916 0.6321 0.0045  0.1471  -0.0021 61 TYR C CE1 
1933 C CE2 . TYR C 61 ? 0.6876 0.3240 0.6627 0.0448  0.2022  0.0328  61 TYR C CE2 
1934 C CZ  . TYR C 61 ? 0.5945 0.2857 0.5788 0.0227  0.1725  0.0015  61 TYR C CZ  
1935 O OH  . TYR C 61 ? 0.6306 0.3181 0.6187 0.0218  0.1715  -0.0242 61 TYR C OH  
1936 N N   . ASP C 62 ? 0.6608 0.2911 0.6978 -0.0494 0.2604  0.0478  62 ASP C N   
1937 C CA  . ASP C 62 ? 0.7214 0.2996 0.7878 -0.0815 0.2929  0.0216  62 ASP C CA  
1938 C C   . ASP C 62 ? 0.7019 0.3277 0.8168 -0.1349 0.2922  -0.0190 62 ASP C C   
1939 O O   . ASP C 62 ? 0.7402 0.3694 0.8808 -0.1632 0.2962  -0.0599 62 ASP C O   
1940 C CB  . ASP C 62 ? 0.8035 0.3219 0.8549 -0.0583 0.3307  0.0501  62 ASP C CB  
1941 C CG  . ASP C 62 ? 1.0235 0.5197 1.0252 0.0014  0.3264  0.0939  62 ASP C CG  
1942 O OD1 . ASP C 62 ? 1.0753 0.5924 1.0490 0.0270  0.3203  0.1266  62 ASP C OD1 
1943 O OD2 . ASP C 62 ? 1.0091 0.4772 1.0007 0.0236  0.3274  0.0921  62 ASP C OD2 
1944 N N   . LYS C 63 ? 0.6767 0.3488 0.8058 -0.1462 0.2870  -0.0110 63 LYS C N   
1945 C CA  . LYS C 63 ? 0.6531 0.3888 0.8318 -0.1908 0.2809  -0.0512 63 LYS C CA  
1946 C C   . LYS C 63 ? 0.6409 0.4502 0.8285 -0.2023 0.2360  -0.0850 63 LYS C C   
1947 O O   . LYS C 63 ? 0.6000 0.4474 0.8232 -0.2400 0.2332  -0.1307 63 LYS C O   
1948 C CB  . LYS C 63 ? 0.7256 0.5017 0.9185 -0.1926 0.2848  -0.0334 63 LYS C CB  
1949 C CG  . LYS C 63 ? 0.7278 0.5797 0.9758 -0.2324 0.2780  -0.0741 63 LYS C CG  
1950 C CD  . LYS C 63 ? 0.8349 0.7118 1.0971 -0.2312 0.2932  -0.0549 63 LYS C CD  
1951 C CE  . LYS C 63 ? 0.7559 0.7416 1.0677 -0.2515 0.2659  -0.0850 63 LYS C CE  
1952 N NZ  . LYS C 63 ? 0.7797 0.8038 1.0904 -0.2289 0.2613  -0.0569 63 LYS C NZ  
1953 N N   . CYS C 64 ? 0.5408 0.3767 0.6909 -0.1657 0.1987  -0.0638 64 CYS C N   
1954 C CA  . CYS C 64 ? 0.5152 0.4269 0.6650 -0.1672 0.1549  -0.0825 64 CYS C CA  
1955 C C   . CYS C 64 ? 0.5317 0.4317 0.6517 -0.1563 0.1384  -0.0920 64 CYS C C   
1956 O O   . CYS C 64 ? 0.4484 0.4034 0.5583 -0.1541 0.1056  -0.1010 64 CYS C O   
1957 C CB  . CYS C 64 ? 0.4397 0.3918 0.5767 -0.1390 0.1301  -0.0541 64 CYS C CB  
1958 S SG  . CYS C 64 ? 0.4580 0.4369 0.6334 -0.1509 0.1505  -0.0466 64 CYS C SG  
1959 N N   . LYS C 65 ? 0.5491 0.3796 0.6553 -0.1481 0.1630  -0.0896 65 LYS C N   
1960 C CA  . LYS C 65 ? 0.5581 0.3840 0.6382 -0.1341 0.1485  -0.0983 65 LYS C CA  
1961 C C   . LYS C 65 ? 0.5819 0.4508 0.6743 -0.1662 0.1369  -0.1436 65 LYS C C   
1962 O O   . LYS C 65 ? 0.4971 0.3969 0.5650 -0.1578 0.1135  -0.1496 65 LYS C O   
1963 C CB  . LYS C 65 ? 0.6023 0.3495 0.6690 -0.1121 0.1778  -0.0867 65 LYS C CB  
1964 C CG  . LYS C 65 ? 0.6347 0.3168 0.7282 -0.1345 0.2221  -0.1002 65 LYS C CG  
1965 C CD  . LYS C 65 ? 0.9188 0.5179 0.9985 -0.1068 0.2521  -0.0894 65 LYS C CD  
1966 C CE  . LYS C 65 ? 0.9345 0.5501 1.0004 -0.0952 0.2341  -0.1122 65 LYS C CE  
1967 N NZ  . LYS C 65 ? 0.8605 0.4144 0.9087 -0.0500 0.2531  -0.0898 65 LYS C NZ  
1968 N N   . ASP C 66 ? 0.5532 0.4302 0.6826 -0.2047 0.1543  -0.1788 66 ASP C N   
1969 C CA  . ASP C 66 ? 0.5604 0.4973 0.6974 -0.2335 0.1378  -0.2266 66 ASP C CA  
1970 C C   . ASP C 66 ? 0.5945 0.6272 0.7221 -0.2294 0.0949  -0.2221 66 ASP C C   
1971 O O   . ASP C 66 ? 0.5392 0.6276 0.6516 -0.2380 0.0733  -0.2480 66 ASP C O   
1972 C CB  . ASP C 66 ? 0.6141 0.5452 0.7912 -0.2684 0.1663  -0.2678 66 ASP C CB  
1973 C CG  . ASP C 66 ? 0.6771 0.6587 0.8920 -0.2883 0.1659  -0.2744 66 ASP C CG  
1974 O OD1 . ASP C 66 ? 0.7592 0.8258 0.9786 -0.2905 0.1316  -0.2764 66 ASP C OD1 
1975 O OD2 . ASP C 66 ? 0.6638 0.6036 0.9055 -0.3009 0.2019  -0.2804 66 ASP C OD2 
1976 N N   . LYS C 67 ? 0.4753 0.5264 0.6068 -0.2115 0.0832  -0.1873 67 LYS C N   
1977 C CA  . LYS C 67 ? 0.4395 0.5688 0.5590 -0.1977 0.0449  -0.1756 67 LYS C CA  
1978 C C   . LYS C 67 ? 0.4117 0.5216 0.4856 -0.1616 0.0286  -0.1375 67 LYS C C   
1979 O O   . LYS C 67 ? 0.4068 0.5582 0.4535 -0.1538 0.0050  -0.1358 67 LYS C O   
1980 C CB  . LYS C 67 ? 0.4220 0.5891 0.5761 -0.1973 0.0417  -0.1641 67 LYS C CB  
1981 N N   . TYR C 68 ? 0.4003 0.4507 0.4649 -0.1400 0.0426  -0.1080 68 TYR C N   
1982 C CA  . TYR C 68 ? 0.3745 0.4155 0.4071 -0.1108 0.0288  -0.0784 68 TYR C CA  
1983 C C   . TYR C 68 ? 0.3957 0.3962 0.4039 -0.1027 0.0383  -0.0810 68 TYR C C   
1984 O O   . TYR C 68 ? 0.3679 0.3726 0.3524 -0.0874 0.0275  -0.0672 68 TYR C O   
1985 C CB  . TYR C 68 ? 0.3542 0.3770 0.3937 -0.0900 0.0331  -0.0493 68 TYR C CB  
1986 C CG  . TYR C 68 ? 0.3432 0.4122 0.4091 -0.0929 0.0235  -0.0457 68 TYR C CG  
1987 C CD1 . TYR C 68 ? 0.3883 0.5155 0.4539 -0.0917 -0.0014 -0.0480 68 TYR C CD1 
1988 C CD2 . TYR C 68 ? 0.3737 0.4328 0.4644 -0.0944 0.0408  -0.0395 68 TYR C CD2 
1989 C CE1 . TYR C 68 ? 0.3403 0.5184 0.4349 -0.0885 -0.0116 -0.0455 68 TYR C CE1 
1990 C CE2 . TYR C 68 ? 0.3355 0.4447 0.4570 -0.0969 0.0338  -0.0401 68 TYR C CE2 
1991 C CZ  . TYR C 68 ? 0.4343 0.6050 0.5605 -0.0929 0.0063  -0.0445 68 TYR C CZ  
1992 O OH  . TYR C 68 ? 0.3624 0.5911 0.5237 -0.0897 -0.0019 -0.0457 68 TYR C OH  
1993 N N   . GLY C 69 ? 0.2996 0.4010 0.3243 -0.0149 0.1255  -0.0043 69 GLY C N   
1994 C CA  . GLY C 69 ? 0.3866 0.4454 0.3965 -0.0171 0.1276  -0.0008 69 GLY C CA  
1995 C C   . GLY C 69 ? 0.3650 0.4267 0.3735 -0.0303 0.1210  -0.0122 69 GLY C C   
1996 O O   . GLY C 69 ? 0.3659 0.4200 0.3835 -0.0496 0.1332  -0.0236 69 GLY C O   
1997 N N   . LYS C 70 ? 0.2916 0.3580 0.2832 -0.0207 0.1049  -0.0095 70 LYS C N   
1998 C CA  . LYS C 70 ? 0.3141 0.3790 0.2910 -0.0315 0.1005  -0.0170 70 LYS C CA  
1999 C C   . LYS C 70 ? 0.3873 0.4246 0.3401 -0.0209 0.0952  -0.0072 70 LYS C C   
2000 O O   . LYS C 70 ? 0.3525 0.3797 0.2992 -0.0046 0.0895  0.0026  70 LYS C O   
2001 C CB  . LYS C 70 ? 0.3431 0.4491 0.3154 -0.0347 0.0871  -0.0244 70 LYS C CB  
2002 C CG  . LYS C 70 ? 0.3964 0.5365 0.3800 -0.0148 0.0753  -0.0179 70 LYS C CG  
2003 C CD  . LYS C 70 ? 0.4688 0.6522 0.4412 -0.0057 0.0540  -0.0213 70 LYS C CD  
2004 C CE  . LYS C 70 ? 0.4945 0.6889 0.4618 0.0303  0.0397  -0.0064 70 LYS C CE  
2005 N NZ  . LYS C 70 ? 0.5811 0.8171 0.5312 0.0494  0.0143  -0.0053 70 LYS C NZ  
2006 N N   . PRO C 71 ? 0.3557 0.3786 0.2948 -0.0330 0.1010  -0.0126 71 PRO C N   
2007 C CA  . PRO C 71 ? 0.3296 0.3248 0.2509 -0.0313 0.1032  -0.0064 71 PRO C CA  
2008 C C   . PRO C 71 ? 0.4617 0.4418 0.3494 -0.0179 0.0929  0.0078  71 PRO C C   
2009 O O   . PRO C 71 ? 0.4083 0.4075 0.2832 -0.0075 0.0808  0.0127  71 PRO C O   
2010 C CB  . PRO C 71 ? 0.3447 0.3349 0.2576 -0.0502 0.1168  -0.0171 71 PRO C CB  
2011 C CG  . PRO C 71 ? 0.3931 0.4001 0.3297 -0.0580 0.1234  -0.0313 71 PRO C CG  
2012 C CD  . PRO C 71 ? 0.3162 0.3447 0.2588 -0.0521 0.1117  -0.0285 71 PRO C CD  
2013 N N   . ASN C 72 ? 0.3923 0.3376 0.2664 -0.0177 0.0981  0.0128  72 ASN C N   
2014 C CA  . ASN C 72 ? 0.4572 0.3686 0.2966 -0.0017 0.0929  0.0274  72 ASN C CA  
2015 C C   . ASN C 72 ? 0.4851 0.3493 0.3049 -0.0188 0.1093  0.0271  72 ASN C C   
2016 O O   . ASN C 72 ? 0.4661 0.3392 0.3158 -0.0370 0.1189  0.0119  72 ASN C O   
2017 C CB  . ASN C 72 ? 0.4407 0.3589 0.2964 0.0202  0.0837  0.0287  72 ASN C CB  
2018 C CG  . ASN C 72 ? 0.5295 0.4136 0.3521 0.0448  0.0783  0.0426  72 ASN C CG  
2019 O OD1 . ASN C 72 ? 0.5406 0.3682 0.3334 0.0412  0.0881  0.0477  72 ASN C OD1 
2020 N ND2 . ASN C 72 ? 0.5262 0.4436 0.3562 0.0704  0.0650  0.0476  72 ASN C ND2 
2021 N N   . LYS C 73 ? 0.5192 0.3344 0.2886 -0.0130 0.1139  0.0437  73 LYS C N   
2022 C CA  . LYS C 73 ? 0.5678 0.3306 0.3142 -0.0374 0.1373  0.0432  73 LYS C CA  
2023 C C   . LYS C 73 ? 0.5734 0.3059 0.3344 -0.0422 0.1430  0.0328  73 LYS C C   
2024 O O   . LYS C 73 ? 0.6397 0.3405 0.3983 -0.0715 0.1647  0.0230  73 LYS C O   
2025 C CB  . LYS C 73 ? 0.6093 0.3143 0.2837 -0.0301 0.1452  0.0685  73 LYS C CB  
2026 C CG  . LYS C 73 ? 0.7123 0.4529 0.3627 -0.0216 0.1335  0.0766  73 LYS C CG  
2027 N N   . ARG C 74 ? 0.5579 0.3035 0.3355 -0.0180 0.1266  0.0304  74 ARG C N   
2028 C CA  . ARG C 74 ? 0.5934 0.3052 0.3744 -0.0217 0.1319  0.0173  74 ARG C CA  
2029 C C   . ARG C 74 ? 0.5786 0.3284 0.4054 -0.0509 0.1356  -0.0104 74 ARG C C   
2030 O O   . ARG C 74 ? 0.4357 0.2459 0.2990 -0.0514 0.1265  -0.0171 74 ARG C O   
2031 C CB  . ARG C 74 ? 0.5483 0.2714 0.3342 0.0123  0.1157  0.0187  74 ARG C CB  
2032 C CG  . ARG C 74 ? 0.5824 0.2880 0.3364 0.0489  0.1075  0.0426  74 ARG C CG  
2033 C CD  . ARG C 74 ? 0.7178 0.3334 0.4171 0.0571  0.1214  0.0578  74 ARG C CD  
2034 N NE  . ARG C 74 ? 0.7233 0.2950 0.4206 0.0618  0.1291  0.0429  74 ARG C NE  
2035 C CZ  . ARG C 74 ? 0.7570 0.3148 0.4461 0.1008  0.1228  0.0464  74 ARG C CZ  
2036 N NH1 . ARG C 74 ? 0.7121 0.2990 0.3973 0.1410  0.1073  0.0662  74 ARG C NH1 
2037 N NH2 . ARG C 74 ? 0.7836 0.3048 0.4719 0.0993  0.1320  0.0255  74 ARG C NH2 
2038 N N   . LYS C 75 ? 0.6006 0.3136 0.4252 -0.0743 0.1493  -0.0278 75 LYS C N   
2039 C CA  . LYS C 75 ? 0.5850 0.3434 0.4570 -0.1030 0.1506  -0.0591 75 LYS C CA  
2040 C C   . LYS C 75 ? 0.4566 0.2812 0.3628 -0.0821 0.1248  -0.0696 75 LYS C C   
2041 O O   . LYS C 75 ? 0.4996 0.3147 0.3909 -0.0599 0.1131  -0.0689 75 LYS C O   
2042 C CB  . LYS C 75 ? 0.5794 0.2875 0.4424 -0.1313 0.1669  -0.0817 75 LYS C CB  
2043 C CG  . LYS C 75 ? 0.5859 0.3392 0.4985 -0.1738 0.1766  -0.1166 75 LYS C CG  
2044 N N   . GLY C 76 ? 0.4058 0.2939 0.3544 -0.0876 0.1187  -0.0792 76 GLY C N   
2045 C CA  . GLY C 76 ? 0.3742 0.3167 0.3476 -0.0666 0.0961  -0.0864 76 GLY C CA  
2046 C C   . GLY C 76 ? 0.3688 0.3195 0.3315 -0.0366 0.0874  -0.0621 76 GLY C C   
2047 O O   . GLY C 76 ? 0.3674 0.3544 0.3441 -0.0187 0.0737  -0.0622 76 GLY C O   
2048 N N   . PHE C 77 ? 0.3712 0.2906 0.3084 -0.0311 0.0953  -0.0418 77 PHE C N   
2049 C CA  . PHE C 77 ? 0.3360 0.2700 0.2697 -0.0091 0.0887  -0.0249 77 PHE C CA  
2050 C C   . PHE C 77 ? 0.3561 0.3252 0.3176 -0.0098 0.0889  -0.0251 77 PHE C C   
2051 O O   . PHE C 77 ? 0.2857 0.2718 0.2539 0.0060  0.0831  -0.0197 77 PHE C O   
2052 C CB  . PHE C 77 ? 0.3814 0.2896 0.2882 -0.0034 0.0931  -0.0081 77 PHE C CB  
2053 C CG  . PHE C 77 ? 0.3522 0.2835 0.2618 0.0160  0.0864  0.0025  77 PHE C CG  
2054 C CD1 . PHE C 77 ? 0.3217 0.2807 0.2478 0.0112  0.0879  0.0047  77 PHE C CD1 
2055 C CD2 . PHE C 77 ? 0.4204 0.3462 0.3188 0.0367  0.0822  0.0066  77 PHE C CD2 
2056 C CE1 . PHE C 77 ? 0.3559 0.3386 0.2901 0.0210  0.0859  0.0099  77 PHE C CE1 
2057 C CE2 . PHE C 77 ? 0.3567 0.3145 0.2666 0.0501  0.0803  0.0127  77 PHE C CE2 
2058 C CZ  . PHE C 77 ? 0.2951 0.2817 0.2238 0.0395  0.0824  0.0140  77 PHE C CZ  
2059 N N   . ASN C 78 ? 0.3212 0.2950 0.2953 -0.0274 0.0997  -0.0310 78 ASN C N   
2060 C CA  . ASN C 78 ? 0.3415 0.3392 0.3383 -0.0246 0.1036  -0.0319 78 ASN C CA  
2061 C C   . ASN C 78 ? 0.3261 0.3557 0.3553 -0.0127 0.0958  -0.0420 78 ASN C C   
2062 O O   . ASN C 78 ? 0.2868 0.3236 0.3263 0.0025  0.0958  -0.0364 78 ASN C O   
2063 C CB  . ASN C 78 ? 0.3457 0.3394 0.3414 -0.0448 0.1203  -0.0372 78 ASN C CB  
2064 C CG  . ASN C 78 ? 0.4065 0.3733 0.3618 -0.0487 0.1227  -0.0238 78 ASN C CG  
2065 O OD1 . ASN C 78 ? 0.3249 0.2916 0.2691 -0.0346 0.1125  -0.0134 78 ASN C OD1 
2066 N ND2 . ASN C 78 ? 0.3427 0.2896 0.2744 -0.0667 0.1367  -0.0239 78 ASN C ND2 
2067 N N   . GLU C 79 ? 0.3113 0.3598 0.3560 -0.0186 0.0890  -0.0578 79 GLU C N   
2068 C CA  . GLU C 79 ? 0.2650 0.3532 0.3348 0.0012  0.0727  -0.0661 79 GLU C CA  
2069 C C   . GLU C 79 ? 0.3185 0.3934 0.3582 0.0271  0.0598  -0.0490 79 GLU C C   
2070 O O   . GLU C 79 ? 0.2719 0.3601 0.3151 0.0525  0.0516  -0.0410 79 GLU C O   
2071 C CB  . GLU C 79 ? 0.2634 0.3843 0.3568 -0.0146 0.0650  -0.0927 79 GLU C CB  
2072 C CG  . GLU C 79 ? 0.2688 0.4412 0.3816 0.0092  0.0392  -0.1041 79 GLU C CG  
2073 C CD  . GLU C 79 ? 0.3122 0.5459 0.4760 -0.0095 0.0337  -0.1392 79 GLU C CD  
2074 O OE1 . GLU C 79 ? 0.3077 0.5279 0.4779 -0.0479 0.0508  -0.1560 79 GLU C OE1 
2075 O OE2 . GLU C 79 ? 0.2880 0.5842 0.4848 0.0144  0.0126  -0.1505 79 GLU C OE2 
2076 N N   . GLY C 80 ? 0.2991 0.3443 0.3061 0.0232  0.0608  -0.0421 80 GLY C N   
2077 C CA  . GLY C 80 ? 0.2959 0.3298 0.2738 0.0440  0.0557  -0.0271 80 GLY C CA  
2078 C C   . GLY C 80 ? 0.3517 0.3722 0.3264 0.0526  0.0673  -0.0077 80 GLY C C   
2079 O O   . GLY C 80 ? 0.3692 0.3845 0.3273 0.0715  0.0666  0.0055  80 GLY C O   
2080 N N   . LEU C 81 ? 0.3208 0.3319 0.3065 0.0368  0.0801  -0.0065 81 LEU C N   
2081 C CA  . LEU C 81 ? 0.3455 0.3448 0.3332 0.0382  0.0930  0.0041  81 LEU C CA  
2082 C C   . LEU C 81 ? 0.3142 0.3135 0.3153 0.0538  0.0942  0.0060  81 LEU C C   
2083 O O   . LEU C 81 ? 0.3873 0.3637 0.3767 0.0653  0.1036  0.0200  81 LEU C O   
2084 C CB  . LEU C 81 ? 0.3119 0.3083 0.3065 0.0174  0.1033  -0.0012 81 LEU C CB  
2085 C CG  . LEU C 81 ? 0.2932 0.2902 0.2726 0.0101  0.1009  0.0012  81 LEU C CG  
2086 C CD1 . LEU C 81 ? 0.3304 0.3304 0.3101 -0.0067 0.1065  -0.0044 81 LEU C CD1 
2087 C CD2 . LEU C 81 ? 0.2695 0.2697 0.2427 0.0180  0.1038  0.0101  81 LEU C CD2 
2088 N N   . TRP C 82 ? 0.2635 0.2870 0.2900 0.0553  0.0873  -0.0081 82 TRP C N   
2089 C CA  . TRP C 82 ? 0.3842 0.4147 0.4285 0.0792  0.0859  -0.0068 82 TRP C CA  
2090 C C   . TRP C 82 ? 0.3616 0.3930 0.3821 0.1106  0.0697  0.0077  82 TRP C C   
2091 O O   . TRP C 82 ? 0.3518 0.3598 0.3615 0.1367  0.0740  0.0239  82 TRP C O   
2092 C CB  . TRP C 82 ? 0.2878 0.3604 0.3741 0.0750  0.0821  -0.0294 82 TRP C CB  
2093 C CG  . TRP C 82 ? 0.3164 0.4030 0.4304 0.1048  0.0820  -0.0310 82 TRP C CG  
2094 C CD1 . TRP C 82 ? 0.3088 0.3782 0.4408 0.1068  0.1025  -0.0353 82 TRP C CD1 
2095 C CD2 . TRP C 82 ? 0.3139 0.4347 0.4386 0.1417  0.0591  -0.0293 82 TRP C CD2 
2096 N NE1 . TRP C 82 ? 0.3474 0.4339 0.5036 0.1460  0.0958  -0.0350 82 TRP C NE1 
2097 C CE2 . TRP C 82 ? 0.3399 0.4618 0.4919 0.1699  0.0669  -0.0298 82 TRP C CE2 
2098 C CE3 . TRP C 82 ? 0.3571 0.5094 0.4679 0.1561  0.0315  -0.0291 82 TRP C CE3 
2099 C CZ2 . TRP C 82 ? 0.4200 0.5763 0.5876 0.2167  0.0454  -0.0265 82 TRP C CZ2 
2100 C CZ3 . TRP C 82 ? 0.3560 0.5469 0.4787 0.1984  0.0084  -0.0279 82 TRP C CZ3 
2101 C CH2 . TRP C 82 ? 0.3795 0.5740 0.5313 0.2309  0.0140  -0.0248 82 TRP C CH2 
2102 N N   . GLU C 83 ? 0.3370 0.3884 0.3418 0.1095  0.0528  0.0026  83 GLU C N   
2103 C CA  . GLU C 83 ? 0.3542 0.4119 0.3278 0.1401  0.0351  0.0137  83 GLU C CA  
2104 C C   . GLU C 83 ? 0.4228 0.4308 0.3495 0.1494  0.0512  0.0416  83 GLU C C   
2105 O O   . GLU C 83 ? 0.4815 0.4711 0.3771 0.1804  0.0485  0.0622  83 GLU C O   
2106 C CB  . GLU C 83 ? 0.3446 0.4343 0.3099 0.1321  0.0154  -0.0054 83 GLU C CB  
2107 C CG  . GLU C 83 ? 0.3312 0.4774 0.3417 0.1248  -0.0019 -0.0351 83 GLU C CG  
2108 C CD  . GLU C 83 ? 0.3830 0.5476 0.3879 0.1031  -0.0132 -0.0606 83 GLU C CD  
2109 O OE1 . GLU C 83 ? 0.3436 0.4745 0.3068 0.0990  -0.0082 -0.0541 83 GLU C OE1 
2110 O OE2 . GLU C 83 ? 0.3275 0.5414 0.3727 0.0896  -0.0248 -0.0899 83 GLU C OE2 
2111 N N   . ILE C 84 ? 0.3614 0.3483 0.2813 0.1242  0.0693  0.0433  84 ILE C N   
2112 C CA  . ILE C 84 ? 0.4261 0.3766 0.3086 0.1270  0.0886  0.0648  84 ILE C CA  
2113 C C   . ILE C 84 ? 0.4246 0.3327 0.3078 0.1293  0.1114  0.0810  84 ILE C C   
2114 O O   . ILE C 84 ? 0.4853 0.3529 0.3306 0.1394  0.1287  0.1037  84 ILE C O   
2115 C CB  . ILE C 84 ? 0.4492 0.4049 0.3351 0.1021  0.0995  0.0572  84 ILE C CB  
2116 C CG1 . ILE C 84 ? 0.5019 0.4360 0.3533 0.1040  0.1203  0.0740  84 ILE C CG1 
2117 C CG2 . ILE C 84 ? 0.3998 0.3584 0.3224 0.0768  0.1095  0.0469  84 ILE C CG2 
2118 C CD1 . ILE C 84 ? 0.4427 0.3975 0.2923 0.0946  0.1233  0.0635  84 ILE C CD1 
2119 N N   . GLN C 85 ? 0.4119 0.3216 0.3328 0.1196  0.1153  0.0690  85 GLN C N   
2120 C CA  . GLN C 85 ? 0.4850 0.3472 0.4076 0.1198  0.1395  0.0782  85 GLN C CA  
2121 C C   . GLN C 85 ? 0.5537 0.3956 0.4666 0.1609  0.1328  0.0921  85 GLN C C   
2122 O O   . GLN C 85 ? 0.5816 0.3613 0.4697 0.1738  0.1549  0.1122  85 GLN C O   
2123 C CB  . GLN C 85 ? 0.4228 0.2947 0.3853 0.0918  0.1486  0.0551  85 GLN C CB  
2124 C CG  . GLN C 85 ? 0.4817 0.2999 0.4460 0.0849  0.1775  0.0567  85 GLN C CG  
2125 C CD  . GLN C 85 ? 0.4637 0.2938 0.4554 0.0483  0.1886  0.0307  85 GLN C CD  
2126 O OE1 . GLN C 85 ? 0.4842 0.3598 0.4927 0.0359  0.1733  0.0149  85 GLN C OE1 
2127 N NE2 . GLN C 85 ? 0.4842 0.2687 0.4747 0.0303  0.2163  0.0255  85 GLN C NE2 
2128 N N   . ASN C 86 ? 0.4715 0.3645 0.4043 0.1826  0.1035  0.0811  86 ASN C N   
2129 C CA  . ASN C 86 ? 0.5541 0.4490 0.4943 0.2259  0.0919  0.0879  86 ASN C CA  
2130 C C   . ASN C 86 ? 0.5473 0.4741 0.4582 0.2653  0.0597  0.0994  86 ASN C C   
2131 O O   . ASN C 86 ? 0.6017 0.5255 0.5062 0.3120  0.0477  0.1128  86 ASN C O   
2132 C CB  . ASN C 86 ? 0.5376 0.4823 0.5412 0.2185  0.0861  0.0575  86 ASN C CB  
2133 C CG  . ASN C 86 ? 0.5319 0.4469 0.5553 0.1818  0.1162  0.0440  86 ASN C CG  
2134 O OD1 . ASN C 86 ? 0.4572 0.4038 0.5029 0.1463  0.1169  0.0228  86 ASN C OD1 
2135 N ND2 . ASN C 86 ? 0.5199 0.3693 0.5293 0.1900  0.1419  0.0560  86 ASN C ND2 
2136 N N   . ASN C 87 ? 0.6580 0.4124 0.4974 0.2365  0.1382  0.0844  87 ASN C N   
2137 C CA  . ASN C 87 ? 0.7081 0.5035 0.5310 0.2976  0.0963  0.0840  87 ASN C CA  
2138 C C   . ASN C 87 ? 0.6855 0.5042 0.4870 0.3031  0.0593  0.0586  87 ASN C C   
2139 O O   . ASN C 87 ? 0.7180 0.5834 0.5473 0.3114  0.0009  0.0319  87 ASN C O   
2140 C CB  . ASN C 87 ? 0.7582 0.6107 0.6466 0.3016  0.0505  0.0740  87 ASN C CB  
2141 C CG  . ASN C 87 ? 0.8808 0.7836 0.7515 0.3653  0.0175  0.0830  87 ASN C CG  
2142 O OD1 . ASN C 87 ? 0.8981 0.7858 0.7093 0.4000  0.0429  0.1064  87 ASN C OD1 
2143 N ND2 . ASN C 87 ? 0.8550 0.8273 0.7788 0.3619  -0.0407 0.0621  87 ASN C ND2 
2144 N N   . PRO C 88 ? 0.6919 0.4799 0.4451 0.2968  0.0937  0.0636  88 PRO C N   
2145 C CA  . PRO C 88 ? 0.6824 0.4949 0.4280 0.2974  0.0637  0.0353  88 PRO C CA  
2146 C C   . PRO C 88 ? 0.7812 0.6227 0.4756 0.3542  0.0355  0.0251  88 PRO C C   
2147 O O   . PRO C 88 ? 0.7366 0.6012 0.4312 0.3595  0.0021  -0.0084 88 PRO C O   
2148 C CB  . PRO C 88 ? 0.6870 0.4697 0.4026 0.2686  0.1170  0.0484  88 PRO C CB  
2149 C CG  . PRO C 88 ? 0.7445 0.4770 0.4146 0.2746  0.1758  0.0854  88 PRO C CG  
2150 C CD  . PRO C 88 ? 0.7732 0.5033 0.4743 0.2908  0.1636  0.0949  88 PRO C CD  
2151 N N   . HIS C 89 ? 0.8350 0.6768 0.4841 0.3981  0.0482  0.0528  89 HIS C N   
2152 C CA  . HIS C 89 ? 0.8577 0.7343 0.4456 0.4504  0.0252  0.0484  89 HIS C CA  
2153 C C   . HIS C 89 ? 0.8696 0.8023 0.4768 0.4796  -0.0291 0.0405  89 HIS C C   
2154 O O   . HIS C 89 ? 0.9322 0.9017 0.4858 0.5212  -0.0434 0.0469  89 HIS C O   
2155 C CB  . HIS C 89 ? 0.9334 0.7764 0.4424 0.4809  0.0807  0.0931  89 HIS C CB  
2156 C CG  . HIS C 89 ? 0.9574 0.7569 0.4435 0.4470  0.1339  0.0998  89 HIS C CG  
2157 N ND1 . HIS C 89 ? 1.0309 0.8535 0.5128 0.4335  0.1251  0.0678  89 HIS C ND1 
2158 C CD2 . HIS C 89 ? 1.0015 0.7402 0.4711 0.4208  0.1971  0.1328  89 HIS C CD2 
2159 C CE1 . HIS C 89 ? 1.0676 0.8596 0.5390 0.3984  0.1763  0.0845  89 HIS C CE1 
2160 N NE2 . HIS C 89 ? 1.0436 0.7833 0.5160 0.3815  0.2148  0.1212  89 HIS C NE2 
2161 N N   . ALA C 90 ? 0.8135 0.7631 0.4973 0.4501  -0.0588 0.0260  90 ALA C N   
2162 C CA  . ALA C 90 ? 0.8289 0.8440 0.5431 0.4621  -0.1087 0.0165  90 ALA C CA  
2163 C C   . ALA C 90 ? 0.8792 0.9325 0.6005 0.4559  -0.1728 -0.0371 90 ALA C C   
2164 O O   . ALA C 90 ? 0.9386 0.9588 0.6722 0.4255  -0.1765 -0.0689 90 ALA C O   
2165 C CB  . ALA C 90 ? 0.7659 0.7868 0.5593 0.4328  -0.1074 0.0276  90 ALA C CB  
2166 N N   . SER C 91 ? 1.0166 1.1358 0.7353 0.4679  -0.2132 -0.0496 91 SER C N   
2167 C CA  . SER C 91 ? 1.0265 1.1775 0.7556 0.4499  -0.2728 -0.1057 91 SER C CA  
2168 C C   . SER C 91 ? 0.9781 1.1304 0.7961 0.3993  -0.3025 -0.1238 91 SER C C   
2169 O O   . SER C 91 ? 1.0399 1.2296 0.9083 0.3873  -0.3019 -0.0993 91 SER C O   
2170 C CB  . SER C 91 ? 1.1150 1.3392 0.8143 0.4689  -0.2990 -0.1110 91 SER C CB  
2171 O OG  . SER C 91 ? 1.1547 1.3851 0.7839 0.5145  -0.2635 -0.0749 91 SER C OG  
2172 N N   . TYR C 92 ? 0.9459 1.0563 0.7849 0.3680  -0.3239 -0.1642 92 TYR C N   
2173 C CA  . TYR C 92 ? 0.8351 0.9387 0.7556 0.3129  -0.3509 -0.1799 92 TYR C CA  
2174 C C   . TYR C 92 ? 0.9032 1.0144 0.8314 0.2845  -0.3979 -0.2317 92 TYR C C   
2175 O O   . TYR C 92 ? 1.0123 1.0775 0.9122 0.2868  -0.4084 -0.2703 92 TYR C O   
2176 C CB  . TYR C 92 ? 0.7604 0.7925 0.7124 0.2800  -0.3188 -0.1727 92 TYR C CB  
2177 C CG  . TYR C 92 ? 0.7822 0.7971 0.7403 0.2806  -0.2607 -0.1231 92 TYR C CG  
2178 C CD1 . TYR C 92 ? 0.7043 0.7336 0.7229 0.2488  -0.2516 -0.0995 92 TYR C CD1 
2179 C CD2 . TYR C 92 ? 0.7605 0.7437 0.6617 0.3087  -0.2121 -0.1028 92 TYR C CD2 
2180 C CE1 . TYR C 92 ? 0.6637 0.6690 0.6818 0.2461  -0.1950 -0.0613 92 TYR C CE1 
2181 C CE2 . TYR C 92 ? 0.7022 0.6601 0.6038 0.3018  -0.1569 -0.0624 92 TYR C CE2 
2182 C CZ  . TYR C 92 ? 0.7160 0.6813 0.6741 0.2710  -0.1481 -0.0439 92 TYR C CZ  
2183 O OH  . TYR C 92 ? 0.6846 0.6168 0.6369 0.2613  -0.0896 -0.0103 92 TYR C OH  
# 
