data_9DEC
# 
_entry.id   9DEC 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9DEC         pdb_00009dec 10.2210/pdb9dec/pdb 
WWPDB D_1000287936 ?            ?                   
# 
_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       2025-03-26 
_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                        9DEC 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-28 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_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           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              dabaker@gmail.com 
_pdbx_contact_author.name_first         David 
_pdbx_contact_author.name_last          Baker 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7896-6217 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Bera, A.K.' 1 ? 
'Sims, J.'   2 ? 
'Baker, D.'  3 ? 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Biorxiv 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2692-8205 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Massively parallel assessment of designed protein solution properties using mass spectrometry and peptide barcoding.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1101/2025.02.24.639402 
_citation.pdbx_database_id_PubMed   40060547 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Feldman, D.'       1  ?                   
primary 'Sims, J.N.'        2  0000-0002-0479-0367 
primary 'Li, X.'            3  ?                   
primary 'Johnson, R.'       4  ?                   
primary 'Gerben, S.'        5  ?                   
primary 'Kim, D.E.'         6  0000-0002-0023-956X 
primary 'Richardson, C.'    7  ?                   
primary 'Koepnick, B.'      8  ?                   
primary 'Eisenach, H.'      9  ?                   
primary 'Hicks, D.R.'       10 ?                   
primary 'Yang, E.C.'        11 0000-0002-1305-9066 
primary 'Wicky, B.I.M.'     12 ?                   
primary 'Milles, L.F.'      13 0000-0001-8417-3205 
primary 'Bera, A.K.'        14 ?                   
primary 'Kang, A.'          15 ?                   
primary 'Brackenbrough, E.' 16 ?                   
primary 'Joyce, E.'         17 ?                   
primary 'Sankaran, B.'      18 ?                   
primary 'Lubner, J.M.'      19 ?                   
primary 'Goreshnik, I.'     20 ?                   
primary 'Vafeados, D.'      21 ?                   
primary 'Allen, A.'         22 ?                   
primary 'Stewart, L.'       23 ?                   
primary 'MacCoss, M.J.'     24 0000-0003-1853-0256 
primary 'Baker, D.'         25 ?                   
# 
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 D9-threaded 9370.075 3  ? ? ? ? 
2 water   nat water       18.015   15 ? ? ? ? 
# 
_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       
;GGGSIKEITETTQLIVKHLAHNGEEYSEVVKEISEEMEKKGLSKEQVILLLIHFLLLSLVKGLSPETTKLLMKELIKELE
KIK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GGGSIKEITETTQLIVKHLAHNGEEYSEVVKEISEEMEKKGLSKEQVILLLIHFLLLSLVKGLSPETTKLLMKELIKELE
KIK
;
_entity_poly.pdbx_strand_id                 A,B,C 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1  GLY n 
1 2  GLY n 
1 3  GLY n 
1 4  SER n 
1 5  ILE n 
1 6  LYS n 
1 7  GLU n 
1 8  ILE n 
1 9  THR n 
1 10 GLU n 
1 11 THR n 
1 12 THR n 
1 13 GLN n 
1 14 LEU n 
1 15 ILE n 
1 16 VAL n 
1 17 LYS n 
1 18 HIS n 
1 19 LEU n 
1 20 ALA n 
1 21 HIS n 
1 22 ASN n 
1 23 GLY n 
1 24 GLU n 
1 25 GLU n 
1 26 TYR n 
1 27 SER n 
1 28 GLU n 
1 29 VAL n 
1 30 VAL n 
1 31 LYS n 
1 32 GLU n 
1 33 ILE n 
1 34 SER n 
1 35 GLU n 
1 36 GLU n 
1 37 MET n 
1 38 GLU n 
1 39 LYS n 
1 40 LYS n 
1 41 GLY n 
1 42 LEU n 
1 43 SER n 
1 44 LYS n 
1 45 GLU n 
1 46 GLN n 
1 47 VAL n 
1 48 ILE n 
1 49 LEU n 
1 50 LEU n 
1 51 LEU n 
1 52 ILE n 
1 53 HIS n 
1 54 PHE n 
1 55 LEU n 
1 56 LEU n 
1 57 LEU n 
1 58 SER n 
1 59 LEU n 
1 60 VAL n 
1 61 LYS n 
1 62 GLY n 
1 63 LEU n 
1 64 SER n 
1 65 PRO n 
1 66 GLU n 
1 67 THR n 
1 68 THR n 
1 69 LYS n 
1 70 LEU n 
1 71 LEU n 
1 72 MET n 
1 73 LYS n 
1 74 GLU n 
1 75 LEU n 
1 76 ILE n 
1 77 LYS n 
1 78 GLU n 
1 79 LEU n 
1 80 GLU n 
1 81 LYS n 
1 82 ILE n 
1 83 LYS 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                   83 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_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      'synthetic construct' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     32630 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
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 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1  GLY 1  -2 -2 GLY GLY A . n 
A 1 2  GLY 2  -1 -1 GLY GLY A . n 
A 1 3  GLY 3  0  0  GLY GLY A . n 
A 1 4  SER 4  1  1  SER SER A . n 
A 1 5  ILE 5  2  2  ILE ILE A . n 
A 1 6  LYS 6  3  3  LYS LYS A . n 
A 1 7  GLU 7  4  4  GLU GLU A . n 
A 1 8  ILE 8  5  5  ILE ILE A . n 
A 1 9  THR 9  6  6  THR THR A . n 
A 1 10 GLU 10 7  7  GLU GLU A . n 
A 1 11 THR 11 8  8  THR THR A . n 
A 1 12 THR 12 9  9  THR THR A . n 
A 1 13 GLN 13 10 10 GLN GLN A . n 
A 1 14 LEU 14 11 11 LEU LEU A . n 
A 1 15 ILE 15 12 12 ILE ILE A . n 
A 1 16 VAL 16 13 13 VAL VAL A . n 
A 1 17 LYS 17 14 14 LYS LYS A . n 
A 1 18 HIS 18 15 15 HIS HIS A . n 
A 1 19 LEU 19 16 16 LEU LEU A . n 
A 1 20 ALA 20 17 17 ALA ALA A . n 
A 1 21 HIS 21 18 18 HIS HIS A . n 
A 1 22 ASN 22 19 19 ASN ASN A . n 
A 1 23 GLY 23 20 20 GLY GLY A . n 
A 1 24 GLU 24 21 21 GLU GLU A . n 
A 1 25 GLU 25 22 22 GLU GLU A . n 
A 1 26 TYR 26 23 23 TYR TYR A . n 
A 1 27 SER 27 24 24 SER SER A . n 
A 1 28 GLU 28 25 25 GLU GLU A . n 
A 1 29 VAL 29 26 26 VAL VAL A . n 
A 1 30 VAL 30 27 27 VAL VAL A . n 
A 1 31 LYS 31 28 28 LYS LYS A . n 
A 1 32 GLU 32 29 29 GLU GLU A . n 
A 1 33 ILE 33 30 30 ILE ILE A . n 
A 1 34 SER 34 31 31 SER SER A . n 
A 1 35 GLU 35 32 32 GLU GLU A . n 
A 1 36 GLU 36 33 33 GLU GLU A . n 
A 1 37 MET 37 34 34 MET MET A . n 
A 1 38 GLU 38 35 35 GLU GLU A . n 
A 1 39 LYS 39 36 36 LYS LYS A . n 
A 1 40 LYS 40 37 37 LYS LYS A . n 
A 1 41 GLY 41 38 38 GLY GLY A . n 
A 1 42 LEU 42 39 39 LEU LEU A . n 
A 1 43 SER 43 40 40 SER SER A . n 
A 1 44 LYS 44 41 41 LYS LYS A . n 
A 1 45 GLU 45 42 42 GLU GLU A . n 
A 1 46 GLN 46 43 43 GLN GLN A . n 
A 1 47 VAL 47 44 44 VAL VAL A . n 
A 1 48 ILE 48 45 45 ILE ILE A . n 
A 1 49 LEU 49 46 46 LEU LEU A . n 
A 1 50 LEU 50 47 47 LEU LEU A . n 
A 1 51 LEU 51 48 48 LEU LEU A . n 
A 1 52 ILE 52 49 49 ILE ILE A . n 
A 1 53 HIS 53 50 50 HIS HIS A . n 
A 1 54 PHE 54 51 51 PHE PHE A . n 
A 1 55 LEU 55 52 52 LEU LEU A . n 
A 1 56 LEU 56 53 53 LEU LEU A . n 
A 1 57 LEU 57 54 54 LEU LEU A . n 
A 1 58 SER 58 55 55 SER SER A . n 
A 1 59 LEU 59 56 56 LEU LEU A . n 
A 1 60 VAL 60 57 57 VAL VAL A . n 
A 1 61 LYS 61 58 58 LYS LYS A . n 
A 1 62 GLY 62 59 59 GLY GLY A . n 
A 1 63 LEU 63 60 60 LEU LEU A . n 
A 1 64 SER 64 61 61 SER SER A . n 
A 1 65 PRO 65 62 62 PRO PRO A . n 
A 1 66 GLU 66 63 63 GLU GLU A . n 
A 1 67 THR 67 64 64 THR THR A . n 
A 1 68 THR 68 65 65 THR THR A . n 
A 1 69 LYS 69 66 66 LYS LYS A . n 
A 1 70 LEU 70 67 67 LEU LEU A . n 
A 1 71 LEU 71 68 68 LEU LEU A . n 
A 1 72 MET 72 69 69 MET MET A . n 
A 1 73 LYS 73 70 70 LYS LYS A . n 
A 1 74 GLU 74 71 71 GLU GLU A . n 
A 1 75 LEU 75 72 72 LEU LEU A . n 
A 1 76 ILE 76 73 73 ILE ILE A . n 
A 1 77 LYS 77 74 74 LYS LYS A . n 
A 1 78 GLU 78 75 75 GLU GLU A . n 
A 1 79 LEU 79 76 76 LEU LEU A . n 
A 1 80 GLU 80 77 77 GLU GLU A . n 
A 1 81 LYS 81 78 78 LYS LYS A . n 
A 1 82 ILE 82 79 79 ILE ILE A . n 
A 1 83 LYS 83 80 ?  ?   ?   A . n 
B 1 1  GLY 1  -2 ?  ?   ?   B . n 
B 1 2  GLY 2  -1 ?  ?   ?   B . n 
B 1 3  GLY 3  0  ?  ?   ?   B . n 
B 1 4  SER 4  1  1  SER SER B . n 
B 1 5  ILE 5  2  2  ILE ILE B . n 
B 1 6  LYS 6  3  3  LYS LYS B . n 
B 1 7  GLU 7  4  4  GLU GLU B . n 
B 1 8  ILE 8  5  5  ILE ILE B . n 
B 1 9  THR 9  6  6  THR THR B . n 
B 1 10 GLU 10 7  7  GLU GLU B . n 
B 1 11 THR 11 8  8  THR THR B . n 
B 1 12 THR 12 9  9  THR THR B . n 
B 1 13 GLN 13 10 10 GLN GLN B . n 
B 1 14 LEU 14 11 11 LEU LEU B . n 
B 1 15 ILE 15 12 12 ILE ILE B . n 
B 1 16 VAL 16 13 13 VAL VAL B . n 
B 1 17 LYS 17 14 14 LYS LYS B . n 
B 1 18 HIS 18 15 15 HIS HIS B . n 
B 1 19 LEU 19 16 16 LEU LEU B . n 
B 1 20 ALA 20 17 17 ALA ALA B . n 
B 1 21 HIS 21 18 18 HIS HIS B . n 
B 1 22 ASN 22 19 19 ASN ASN B . n 
B 1 23 GLY 23 20 20 GLY GLY B . n 
B 1 24 GLU 24 21 21 GLU GLU B . n 
B 1 25 GLU 25 22 22 GLU GLU B . n 
B 1 26 TYR 26 23 23 TYR TYR B . n 
B 1 27 SER 27 24 24 SER SER B . n 
B 1 28 GLU 28 25 25 GLU GLU B . n 
B 1 29 VAL 29 26 26 VAL VAL B . n 
B 1 30 VAL 30 27 27 VAL VAL B . n 
B 1 31 LYS 31 28 28 LYS LYS B . n 
B 1 32 GLU 32 29 29 GLU GLU B . n 
B 1 33 ILE 33 30 30 ILE ILE B . n 
B 1 34 SER 34 31 31 SER SER B . n 
B 1 35 GLU 35 32 32 GLU GLU B . n 
B 1 36 GLU 36 33 33 GLU GLU B . n 
B 1 37 MET 37 34 34 MET MET B . n 
B 1 38 GLU 38 35 35 GLU GLU B . n 
B 1 39 LYS 39 36 36 LYS LYS B . n 
B 1 40 LYS 40 37 37 LYS LYS B . n 
B 1 41 GLY 41 38 38 GLY GLY B . n 
B 1 42 LEU 42 39 39 LEU LEU B . n 
B 1 43 SER 43 40 40 SER SER B . n 
B 1 44 LYS 44 41 41 LYS LYS B . n 
B 1 45 GLU 45 42 42 GLU GLU B . n 
B 1 46 GLN 46 43 43 GLN GLN B . n 
B 1 47 VAL 47 44 44 VAL VAL B . n 
B 1 48 ILE 48 45 45 ILE ILE B . n 
B 1 49 LEU 49 46 46 LEU LEU B . n 
B 1 50 LEU 50 47 47 LEU LEU B . n 
B 1 51 LEU 51 48 48 LEU LEU B . n 
B 1 52 ILE 52 49 49 ILE ILE B . n 
B 1 53 HIS 53 50 50 HIS HIS B . n 
B 1 54 PHE 54 51 51 PHE PHE B . n 
B 1 55 LEU 55 52 52 LEU LEU B . n 
B 1 56 LEU 56 53 53 LEU LEU B . n 
B 1 57 LEU 57 54 54 LEU LEU B . n 
B 1 58 SER 58 55 55 SER SER B . n 
B 1 59 LEU 59 56 56 LEU LEU B . n 
B 1 60 VAL 60 57 57 VAL VAL B . n 
B 1 61 LYS 61 58 58 LYS LYS B . n 
B 1 62 GLY 62 59 59 GLY GLY B . n 
B 1 63 LEU 63 60 60 LEU LEU B . n 
B 1 64 SER 64 61 61 SER SER B . n 
B 1 65 PRO 65 62 62 PRO PRO B . n 
B 1 66 GLU 66 63 63 GLU GLU B . n 
B 1 67 THR 67 64 64 THR THR B . n 
B 1 68 THR 68 65 65 THR THR B . n 
B 1 69 LYS 69 66 66 LYS LYS B . n 
B 1 70 LEU 70 67 67 LEU LEU B . n 
B 1 71 LEU 71 68 68 LEU LEU B . n 
B 1 72 MET 72 69 69 MET MET B . n 
B 1 73 LYS 73 70 70 LYS LYS B . n 
B 1 74 GLU 74 71 71 GLU GLU B . n 
B 1 75 LEU 75 72 72 LEU LEU B . n 
B 1 76 ILE 76 73 73 ILE ILE B . n 
B 1 77 LYS 77 74 74 LYS LYS B . n 
B 1 78 GLU 78 75 75 GLU GLU B . n 
B 1 79 LEU 79 76 76 LEU LEU B . n 
B 1 80 GLU 80 77 77 GLU GLU B . n 
B 1 81 LYS 81 78 78 LYS LYS B . n 
B 1 82 ILE 82 79 79 ILE ILE B . n 
B 1 83 LYS 83 80 ?  ?   ?   B . n 
C 1 1  GLY 1  -2 ?  ?   ?   C . n 
C 1 2  GLY 2  -1 ?  ?   ?   C . n 
C 1 3  GLY 3  0  ?  ?   ?   C . n 
C 1 4  SER 4  1  1  SER SER C . n 
C 1 5  ILE 5  2  2  ILE ILE C . n 
C 1 6  LYS 6  3  3  LYS LYS C . n 
C 1 7  GLU 7  4  4  GLU GLU C . n 
C 1 8  ILE 8  5  5  ILE ILE C . n 
C 1 9  THR 9  6  6  THR THR C . n 
C 1 10 GLU 10 7  7  GLU GLU C . n 
C 1 11 THR 11 8  8  THR THR C . n 
C 1 12 THR 12 9  9  THR THR C . n 
C 1 13 GLN 13 10 10 GLN GLN C . n 
C 1 14 LEU 14 11 11 LEU LEU C . n 
C 1 15 ILE 15 12 12 ILE ILE C . n 
C 1 16 VAL 16 13 13 VAL VAL C . n 
C 1 17 LYS 17 14 14 LYS LYS C . n 
C 1 18 HIS 18 15 15 HIS HIS C . n 
C 1 19 LEU 19 16 16 LEU LEU C . n 
C 1 20 ALA 20 17 17 ALA ALA C . n 
C 1 21 HIS 21 18 18 HIS HIS C . n 
C 1 22 ASN 22 19 19 ASN ASN C . n 
C 1 23 GLY 23 20 20 GLY GLY C . n 
C 1 24 GLU 24 21 21 GLU GLU C . n 
C 1 25 GLU 25 22 22 GLU GLU C . n 
C 1 26 TYR 26 23 23 TYR TYR C . n 
C 1 27 SER 27 24 24 SER SER C . n 
C 1 28 GLU 28 25 25 GLU GLU C . n 
C 1 29 VAL 29 26 26 VAL VAL C . n 
C 1 30 VAL 30 27 27 VAL VAL C . n 
C 1 31 LYS 31 28 28 LYS LYS C . n 
C 1 32 GLU 32 29 29 GLU GLU C . n 
C 1 33 ILE 33 30 30 ILE ILE C . n 
C 1 34 SER 34 31 31 SER SER C . n 
C 1 35 GLU 35 32 32 GLU GLU C . n 
C 1 36 GLU 36 33 33 GLU GLU C . n 
C 1 37 MET 37 34 34 MET MET C . n 
C 1 38 GLU 38 35 35 GLU GLU C . n 
C 1 39 LYS 39 36 36 LYS LYS C . n 
C 1 40 LYS 40 37 37 LYS LYS C . n 
C 1 41 GLY 41 38 38 GLY GLY C . n 
C 1 42 LEU 42 39 39 LEU LEU C . n 
C 1 43 SER 43 40 40 SER SER C . n 
C 1 44 LYS 44 41 41 LYS LYS C . n 
C 1 45 GLU 45 42 42 GLU GLU C . n 
C 1 46 GLN 46 43 43 GLN GLN C . n 
C 1 47 VAL 47 44 44 VAL VAL C . n 
C 1 48 ILE 48 45 45 ILE ILE C . n 
C 1 49 LEU 49 46 46 LEU LEU C . n 
C 1 50 LEU 50 47 47 LEU LEU C . n 
C 1 51 LEU 51 48 48 LEU LEU C . n 
C 1 52 ILE 52 49 49 ILE ILE C . n 
C 1 53 HIS 53 50 50 HIS HIS C . n 
C 1 54 PHE 54 51 51 PHE PHE C . n 
C 1 55 LEU 55 52 52 LEU LEU C . n 
C 1 56 LEU 56 53 53 LEU LEU C . n 
C 1 57 LEU 57 54 54 LEU LEU C . n 
C 1 58 SER 58 55 55 SER SER C . n 
C 1 59 LEU 59 56 56 LEU LEU C . n 
C 1 60 VAL 60 57 57 VAL VAL C . n 
C 1 61 LYS 61 58 58 LYS LYS C . n 
C 1 62 GLY 62 59 59 GLY GLY C . n 
C 1 63 LEU 63 60 60 LEU LEU C . n 
C 1 64 SER 64 61 61 SER SER C . n 
C 1 65 PRO 65 62 62 PRO PRO C . n 
C 1 66 GLU 66 63 63 GLU GLU C . n 
C 1 67 THR 67 64 64 THR THR C . n 
C 1 68 THR 68 65 65 THR THR C . n 
C 1 69 LYS 69 66 66 LYS LYS C . n 
C 1 70 LEU 70 67 67 LEU LEU C . n 
C 1 71 LEU 71 68 68 LEU LEU C . n 
C 1 72 MET 72 69 69 MET MET C . n 
C 1 73 LYS 73 70 70 LYS LYS C . n 
C 1 74 GLU 74 71 71 GLU GLU C . n 
C 1 75 LEU 75 72 72 LEU LEU C . n 
C 1 76 ILE 76 73 73 ILE ILE C . n 
C 1 77 LYS 77 74 74 LYS LYS C . n 
C 1 78 GLU 78 75 75 GLU GLU C . n 
C 1 79 LEU 79 76 76 LEU LEU C . n 
C 1 80 GLU 80 77 77 GLU GLU C . n 
C 1 81 LYS 81 78 78 LYS LYS C . n 
C 1 82 ILE 82 79 ?  ?   ?   C . n 
C 1 83 LYS 83 80 ?  ?   ?   C . n 
# 
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 HOH 1 101 2  HOH HOH A . 
D 2 HOH 2 102 15 HOH HOH A . 
D 2 HOH 3 103 3  HOH HOH A . 
D 2 HOH 4 104 14 HOH HOH A . 
D 2 HOH 5 105 8  HOH HOH A . 
D 2 HOH 6 106 12 HOH HOH A . 
D 2 HOH 7 107 9  HOH HOH A . 
E 2 HOH 1 101 4  HOH HOH B . 
E 2 HOH 2 102 1  HOH HOH B . 
E 2 HOH 3 103 6  HOH HOH B . 
E 2 HOH 4 104 7  HOH HOH B . 
F 2 HOH 1 101 11 HOH HOH C . 
F 2 HOH 2 102 10 HOH HOH C . 
F 2 HOH 3 103 13 HOH HOH C . 
F 2 HOH 4 104 5  HOH HOH C . 
# 
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 ? ? ? 1.21.1_5286 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9DEC 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     67.973 
_cell.length_a_esd                 ? 
_cell.length_b                     69.276 
_cell.length_b_esd                 ? 
_cell.length_c                     84.467 
_cell.length_c_esd                 ? 
_cell.volume                       397746.449 
_cell.volume_esd                   ? 
_cell.Z_PDB                        24 
_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                         9DEC 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                23 
_symmetry.space_group_name_Hall            'I 2 2' 
_symmetry.space_group_name_H-M             'I 2 2 2' 
_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                   9DEC 
_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             1.77 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          31.30 
_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              6.0 
_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    '21 % w/v PEG 3350, 0.1 M MES pH 6.0 and 0.15 M Sodium chloride' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_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                      'Horizontal pre-focus bimorph mirror & KB bimorph mirrors' 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-07-05 
_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                    'Si(111) DCM' 
_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   0.97936 
_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                        'NSLS-II BEAMLINE 17-ID-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97936 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   17-ID-2 
_diffrn_source.pdbx_synchrotron_site       NSLS-II 
# 
_reflns.B_iso_Wilson_estimate                          38.36 
_reflns.entry_id                                       9DEC 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.04 
_reflns.d_resolution_low                               31.86 
_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                                     13040 
_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                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                10.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.3 
_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                                0.53 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.159 
_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                                    2.04 
_reflns_shell.d_res_low                                     2.15 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.2 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1879 
_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                               11.2 
_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                               0.782 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.416 
_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                                  2.387 
_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                               52.00 
_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                                 9DEC 
_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                            2.04 
_refine.ls_d_res_low                             31.86 
_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                     11792 
_refine.ls_number_reflns_R_free                  1180 
_refine.ls_number_reflns_R_work                  10612 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    90.42 
_refine.ls_percent_reflns_R_free                 10.01 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2276 
_refine.ls_R_factor_R_free                       0.2781 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2220 
_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                          0.01 
_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               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_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             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 32.8132 
_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                            0.3127 
_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.details                          ? 
_refine_hist.d_res_high                       2.04 
_refine_hist.d_res_low                        31.86 
_refine_hist.number_atoms_solvent             15 
_refine_hist.number_atoms_total               1921 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        1906 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
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' ? 0.0022  ? 1921 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.4558  ? 2569 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0323  ? 325  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0026  ? 305  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 14.4313 ? 762  ? f_dihedral_angle_d ? ? 
# 
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' 2.04 2.13  . . 115 1105 75.82 . . . . 0.3138 . . . . . . . . . . . 0.3671 
'X-RAY DIFFRACTION' 2.13 2.25  . . 131 1168 81.70 . . . . 0.3074 . . . . . . . . . . . 0.3667 
'X-RAY DIFFRACTION' 2.25 2.39  . . 132 1260 85.77 . . . . 0.2785 . . . . . . . . . . . 0.3433 
'X-RAY DIFFRACTION' 2.39 2.57  . . 150 1304 89.92 . . . . 0.2588 . . . . . . . . . . . 0.3256 
'X-RAY DIFFRACTION' 2.57 2.83  . . 149 1351 93.46 . . . . 0.2338 . . . . . . . . . . . 0.3445 
'X-RAY DIFFRACTION' 2.83 3.24  . . 163 1415 96.75 . . . . 0.2511 . . . . . . . . . . . 0.3170 
'X-RAY DIFFRACTION' 3.24 4.08  . . 164 1464 99.33 . . . . 0.2246 . . . . . . . . . . . 0.2552 
'X-RAY DIFFRACTION' 4.08 31.86 . . 176 1545 99.59 . . . . 0.1818 . . . . . . . . . . . 0.2365 
# 
_struct.entry_id                     9DEC 
_struct.title                        'Crystal Structure of D9-threaded' 
_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        9DEC 
_struct_keywords.text            'de novo protein, design model, barcoding, mass spec' 
_struct_keywords.pdbx_keywords   'DE NOVO 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 2 ? 
F N N 2 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    PDB 
_struct_ref.db_code                    9DEC 
_struct_ref.pdbx_db_accession          9DEC 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_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 9DEC A 1 ? 83 ? 9DEC -2 ? 80 ? -2 80 
2 1 9DEC B 1 ? 83 ? 9DEC -2 ? 80 ? -2 80 
3 1 9DEC C 1 ? 83 ? 9DEC -2 ? 80 ? -2 80 
# 
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 
2 1 B,E 
3 1 C,F 
# 
_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 ILE A 5  ? ALA A 20 ? ILE A 2  ALA A 17 1 ? 16 
HELX_P HELX_P2  AA2 ASN A 22 ? LYS A 40 ? ASN A 19 LYS A 37 1 ? 19 
HELX_P HELX_P3  AA3 SER A 43 ? VAL A 60 ? SER A 40 VAL A 57 1 ? 18 
HELX_P HELX_P4  AA4 SER A 64 ? ILE A 82 ? SER A 61 ILE A 79 1 ? 19 
HELX_P HELX_P5  AA5 ILE B 5  ? ALA B 20 ? ILE B 2  ALA B 17 1 ? 16 
HELX_P HELX_P6  AA6 ASN B 22 ? LYS B 40 ? ASN B 19 LYS B 37 1 ? 19 
HELX_P HELX_P7  AA7 SER B 43 ? LEU B 59 ? SER B 40 LEU B 56 1 ? 17 
HELX_P HELX_P8  AA8 SER B 64 ? GLU B 80 ? SER B 61 GLU B 77 1 ? 17 
HELX_P HELX_P9  AA9 ILE C 5  ? ALA C 20 ? ILE C 2  ALA C 17 1 ? 16 
HELX_P HELX_P10 AB1 ASN C 22 ? LYS C 40 ? ASN C 19 LYS C 37 1 ? 19 
HELX_P HELX_P11 AB2 SER C 43 ? VAL C 60 ? SER C 40 VAL C 57 1 ? 18 
HELX_P HELX_P12 AB3 SER C 64 ? LYS C 81 ? SER C 61 LYS C 78 1 ? 18 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_pdbx_entry_details.entry_id                   9DEC 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    OG1 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    THR 
_pdbx_validate_symm_contact.auth_seq_id_1     64 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    HIS 
_pdbx_validate_symm_contact.auth_seq_id_2     15 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_565 
_pdbx_validate_symm_contact.dist              2.19 
# 
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 19 ? ? -107.14 45.46  
2 1 LEU B 56 ? ? -116.69 -78.41 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 x,-y,-z             
3 -x,y,-z             
4 -x,-y,z             
5 x+1/2,y+1/2,z+1/2   
6 x+1/2,-y+1/2,-z+1/2 
7 -x+1/2,y+1/2,-z+1/2 
8 -x+1/2,-y+1/2,z+1/2 
# 
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 12.1077220527 30.7047110817 20.6255830184 0.217547927798 ? -0.0294630595245 ? -0.0163577672181 ? 
0.245147412609 ? -0.0131872030513 ? 0.30196680193  ? 5.25062821387 ? 0.369058386174 ? -1.82303469104 ? 6.7952421676  ? 
-1.53150233874 ? 6.24086197115 ? 0.115273993049   ? -0.057251791127  ? 0.425821025391   ? 0.530535036232  ? 0.219771152412  ? 
-0.161461469516 ? -0.521667529226 ? 0.17515440078   ? -0.343156078103 ? 
2 'X-RAY DIFFRACTION' ? refined 3.91423285132 13.7863523301 12.1955950784 0.41937724562  ? 0.00140769886135 ? -0.0204797415769 ? 
0.252832004621 ? -0.0567240776324 ? 0.366154359604 ? 6.09729036433 ? 0.769309459631 ? 2.72361865079  ? 3.94840051362 ? 
0.109541006411 ? 8.00523261501 ? -0.238041138023  ? 0.0170396080643  ? -0.259689554644  ? 0.0248100014069 ? -0.132873730161 ? 
0.336535088279  ? 0.69721298003   ? -0.475971094494 ? 0.363052074807  ? 
3 'X-RAY DIFFRACTION' ? refined 21.2227895133 21.8091764265 3.94920269994 0.276835659331 ? 0.0668436768084  ? 0.088552896758   ? 
0.349839392944 ? 0.0744515861275  ? 0.358372859964 ? 4.52464893523 ? 0.33534082657  ? 1.6459256808   ? 7.16763731086 ? 
-1.82154646613 ? 6.52192417799 ? -0.0382622769286 ? -0.0500193852551 ? -0.0187354720865 ? -0.61042734242  ? -0.245753892053 ? 
-0.458165175522 ? 0.300721606253  ? 0.630632017694  ? 0.15625033562   ? 
# 
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 A 4 A 1 ? A 82 A 79 ? ? '(chain A and resseq 1:79)' 
2 'X-RAY DIFFRACTION' 2 B 1 B 1 ? B 79 B 79 ? ? '(chain B and resseq 1:79)' 
3 'X-RAY DIFFRACTION' 3 C 1 C 1 ? C 78 C 78 ? ? '(chain C and resseq 1:78)' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A LYS 80 ? A LYS 83 
2  1 Y 1 B GLY -2 ? B GLY 1  
3  1 Y 1 B GLY -1 ? B GLY 2  
4  1 Y 1 B GLY 0  ? B GLY 3  
5  1 Y 1 B LYS 80 ? B LYS 83 
6  1 Y 1 C GLY -2 ? C GLY 1  
7  1 Y 1 C GLY -1 ? C GLY 2  
8  1 Y 1 C GLY 0  ? C GLY 3  
9  1 Y 1 C ILE 79 ? C ILE 82 
10 1 Y 1 C LYS 80 ? C LYS 83 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ASN N    N N N 14  
ASN CA   C N S 15  
ASN C    C N N 16  
ASN O    O N N 17  
ASN CB   C N N 18  
ASN CG   C N N 19  
ASN OD1  O N N 20  
ASN ND2  N N N 21  
ASN OXT  O N N 22  
ASN H    H N N 23  
ASN H2   H N N 24  
ASN HA   H N N 25  
ASN HB2  H N N 26  
ASN HB3  H N N 27  
ASN HD21 H N N 28  
ASN HD22 H N N 29  
ASN HXT  H N N 30  
GLN N    N N N 31  
GLN CA   C N S 32  
GLN C    C N N 33  
GLN O    O N N 34  
GLN CB   C N N 35  
GLN CG   C N N 36  
GLN CD   C N N 37  
GLN OE1  O N N 38  
GLN NE2  N N N 39  
GLN OXT  O N N 40  
GLN H    H N N 41  
GLN H2   H N N 42  
GLN HA   H N N 43  
GLN HB2  H N N 44  
GLN HB3  H N N 45  
GLN HG2  H N N 46  
GLN HG3  H N N 47  
GLN HE21 H N N 48  
GLN HE22 H N N 49  
GLN HXT  H N N 50  
GLU N    N N N 51  
GLU CA   C N S 52  
GLU C    C N N 53  
GLU O    O N N 54  
GLU CB   C N N 55  
GLU CG   C N N 56  
GLU CD   C N N 57  
GLU OE1  O N N 58  
GLU OE2  O N N 59  
GLU OXT  O N N 60  
GLU H    H N N 61  
GLU H2   H N N 62  
GLU HA   H N N 63  
GLU HB2  H N N 64  
GLU HB3  H N N 65  
GLU HG2  H N N 66  
GLU HG3  H N N 67  
GLU HE2  H N N 68  
GLU HXT  H N N 69  
GLY N    N N N 70  
GLY CA   C N N 71  
GLY C    C N N 72  
GLY O    O N N 73  
GLY OXT  O N N 74  
GLY H    H N N 75  
GLY H2   H N N 76  
GLY HA2  H N N 77  
GLY HA3  H N N 78  
GLY HXT  H N N 79  
HIS N    N N N 80  
HIS CA   C N S 81  
HIS C    C N N 82  
HIS O    O N N 83  
HIS CB   C N N 84  
HIS CG   C Y N 85  
HIS ND1  N Y N 86  
HIS CD2  C Y N 87  
HIS CE1  C Y N 88  
HIS NE2  N Y N 89  
HIS OXT  O N N 90  
HIS H    H N N 91  
HIS H2   H N N 92  
HIS HA   H N N 93  
HIS HB2  H N N 94  
HIS HB3  H N N 95  
HIS HD1  H N N 96  
HIS HD2  H N N 97  
HIS HE1  H N N 98  
HIS HE2  H N N 99  
HIS HXT  H N N 100 
HOH O    O N N 101 
HOH H1   H N N 102 
HOH H2   H N N 103 
ILE N    N N N 104 
ILE CA   C N S 105 
ILE C    C N N 106 
ILE O    O N N 107 
ILE CB   C N S 108 
ILE CG1  C N N 109 
ILE CG2  C N N 110 
ILE CD1  C N N 111 
ILE OXT  O N N 112 
ILE H    H N N 113 
ILE H2   H N N 114 
ILE HA   H N N 115 
ILE HB   H N N 116 
ILE HG12 H N N 117 
ILE HG13 H N N 118 
ILE HG21 H N N 119 
ILE HG22 H N N 120 
ILE HG23 H N N 121 
ILE HD11 H N N 122 
ILE HD12 H N N 123 
ILE HD13 H N N 124 
ILE HXT  H N N 125 
LEU N    N N N 126 
LEU CA   C N S 127 
LEU C    C N N 128 
LEU O    O N N 129 
LEU CB   C N N 130 
LEU CG   C N N 131 
LEU CD1  C N N 132 
LEU CD2  C N N 133 
LEU OXT  O N N 134 
LEU H    H N N 135 
LEU H2   H N N 136 
LEU HA   H N N 137 
LEU HB2  H N N 138 
LEU HB3  H N N 139 
LEU HG   H N N 140 
LEU HD11 H N N 141 
LEU HD12 H N N 142 
LEU HD13 H N N 143 
LEU HD21 H N N 144 
LEU HD22 H N N 145 
LEU HD23 H N N 146 
LEU HXT  H N N 147 
LYS N    N N N 148 
LYS CA   C N S 149 
LYS C    C N N 150 
LYS O    O N N 151 
LYS CB   C N N 152 
LYS CG   C N N 153 
LYS CD   C N N 154 
LYS CE   C N N 155 
LYS NZ   N N N 156 
LYS OXT  O N N 157 
LYS H    H N N 158 
LYS H2   H N N 159 
LYS HA   H N N 160 
LYS HB2  H N N 161 
LYS HB3  H N N 162 
LYS HG2  H N N 163 
LYS HG3  H N N 164 
LYS HD2  H N N 165 
LYS HD3  H N N 166 
LYS HE2  H N N 167 
LYS HE3  H N N 168 
LYS HZ1  H N N 169 
LYS HZ2  H N N 170 
LYS HZ3  H N N 171 
LYS HXT  H N N 172 
MET N    N N N 173 
MET CA   C N S 174 
MET C    C N N 175 
MET O    O N N 176 
MET CB   C N N 177 
MET CG   C N N 178 
MET SD   S N N 179 
MET CE   C N N 180 
MET OXT  O N N 181 
MET H    H N N 182 
MET H2   H N N 183 
MET HA   H N N 184 
MET HB2  H N N 185 
MET HB3  H N N 186 
MET HG2  H N N 187 
MET HG3  H N N 188 
MET HE1  H N N 189 
MET HE2  H N N 190 
MET HE3  H N N 191 
MET HXT  H N N 192 
PHE N    N N N 193 
PHE CA   C N S 194 
PHE C    C N N 195 
PHE O    O N N 196 
PHE CB   C N N 197 
PHE CG   C Y N 198 
PHE CD1  C Y N 199 
PHE CD2  C Y N 200 
PHE CE1  C Y N 201 
PHE CE2  C Y N 202 
PHE CZ   C Y N 203 
PHE OXT  O N N 204 
PHE H    H N N 205 
PHE H2   H N N 206 
PHE HA   H N N 207 
PHE HB2  H N N 208 
PHE HB3  H N N 209 
PHE HD1  H N N 210 
PHE HD2  H N N 211 
PHE HE1  H N N 212 
PHE HE2  H N N 213 
PHE HZ   H N N 214 
PHE HXT  H N N 215 
PRO N    N N N 216 
PRO CA   C N S 217 
PRO C    C N N 218 
PRO O    O N N 219 
PRO CB   C N N 220 
PRO CG   C N N 221 
PRO CD   C N N 222 
PRO OXT  O N N 223 
PRO H    H N N 224 
PRO HA   H N N 225 
PRO HB2  H N N 226 
PRO HB3  H N N 227 
PRO HG2  H N N 228 
PRO HG3  H N N 229 
PRO HD2  H N N 230 
PRO HD3  H N N 231 
PRO HXT  H N N 232 
SER N    N N N 233 
SER CA   C N S 234 
SER C    C N N 235 
SER O    O N N 236 
SER CB   C N N 237 
SER OG   O N N 238 
SER OXT  O N N 239 
SER H    H N N 240 
SER H2   H N N 241 
SER HA   H N N 242 
SER HB2  H N N 243 
SER HB3  H N N 244 
SER HG   H N N 245 
SER HXT  H N N 246 
THR N    N N N 247 
THR CA   C N S 248 
THR C    C N N 249 
THR O    O N N 250 
THR CB   C N R 251 
THR OG1  O N N 252 
THR CG2  C N N 253 
THR OXT  O N N 254 
THR H    H N N 255 
THR H2   H N N 256 
THR HA   H N N 257 
THR HB   H N N 258 
THR HG1  H N N 259 
THR HG21 H N N 260 
THR HG22 H N N 261 
THR HG23 H N N 262 
THR HXT  H N N 263 
TYR N    N N N 264 
TYR CA   C N S 265 
TYR C    C N N 266 
TYR O    O N N 267 
TYR CB   C N N 268 
TYR CG   C Y N 269 
TYR CD1  C Y N 270 
TYR CD2  C Y N 271 
TYR CE1  C Y N 272 
TYR CE2  C Y N 273 
TYR CZ   C Y N 274 
TYR OH   O N N 275 
TYR OXT  O N N 276 
TYR H    H N N 277 
TYR H2   H N N 278 
TYR HA   H N N 279 
TYR HB2  H N N 280 
TYR HB3  H N N 281 
TYR HD1  H N N 282 
TYR HD2  H N N 283 
TYR HE1  H N N 284 
TYR HE2  H N N 285 
TYR HH   H N N 286 
TYR HXT  H N N 287 
VAL N    N N N 288 
VAL CA   C N S 289 
VAL C    C N N 290 
VAL O    O N N 291 
VAL CB   C N N 292 
VAL CG1  C N N 293 
VAL CG2  C N N 294 
VAL OXT  O N N 295 
VAL H    H N N 296 
VAL H2   H N N 297 
VAL HA   H N N 298 
VAL HB   H N N 299 
VAL HG11 H N N 300 
VAL HG12 H N N 301 
VAL HG13 H N N 302 
VAL HG21 H N N 303 
VAL HG22 H N N 304 
VAL HG23 H N N 305 
VAL HXT  H N N 306 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ASN N   CA   sing N N 13  
ASN N   H    sing N N 14  
ASN N   H2   sing N N 15  
ASN CA  C    sing N N 16  
ASN CA  CB   sing N N 17  
ASN CA  HA   sing N N 18  
ASN C   O    doub N N 19  
ASN C   OXT  sing N N 20  
ASN CB  CG   sing N N 21  
ASN CB  HB2  sing N N 22  
ASN CB  HB3  sing N N 23  
ASN CG  OD1  doub N N 24  
ASN CG  ND2  sing N N 25  
ASN ND2 HD21 sing N N 26  
ASN ND2 HD22 sing N N 27  
ASN OXT HXT  sing N N 28  
GLN N   CA   sing N N 29  
GLN N   H    sing N N 30  
GLN N   H2   sing N N 31  
GLN CA  C    sing N N 32  
GLN CA  CB   sing N N 33  
GLN CA  HA   sing N N 34  
GLN C   O    doub N N 35  
GLN C   OXT  sing N N 36  
GLN CB  CG   sing N N 37  
GLN CB  HB2  sing N N 38  
GLN CB  HB3  sing N N 39  
GLN CG  CD   sing N N 40  
GLN CG  HG2  sing N N 41  
GLN CG  HG3  sing N N 42  
GLN CD  OE1  doub N N 43  
GLN CD  NE2  sing N N 44  
GLN NE2 HE21 sing N N 45  
GLN NE2 HE22 sing N N 46  
GLN OXT HXT  sing N N 47  
GLU N   CA   sing N N 48  
GLU N   H    sing N N 49  
GLU N   H2   sing N N 50  
GLU CA  C    sing N N 51  
GLU CA  CB   sing N N 52  
GLU CA  HA   sing N N 53  
GLU C   O    doub N N 54  
GLU C   OXT  sing N N 55  
GLU CB  CG   sing N N 56  
GLU CB  HB2  sing N N 57  
GLU CB  HB3  sing N N 58  
GLU CG  CD   sing N N 59  
GLU CG  HG2  sing N N 60  
GLU CG  HG3  sing N N 61  
GLU CD  OE1  doub N N 62  
GLU CD  OE2  sing N N 63  
GLU OE2 HE2  sing N N 64  
GLU OXT HXT  sing N N 65  
GLY N   CA   sing N N 66  
GLY N   H    sing N N 67  
GLY N   H2   sing N N 68  
GLY CA  C    sing N N 69  
GLY CA  HA2  sing N N 70  
GLY CA  HA3  sing N N 71  
GLY C   O    doub N N 72  
GLY C   OXT  sing N N 73  
GLY OXT HXT  sing N N 74  
HIS N   CA   sing N N 75  
HIS N   H    sing N N 76  
HIS N   H2   sing N N 77  
HIS CA  C    sing N N 78  
HIS CA  CB   sing N N 79  
HIS CA  HA   sing N N 80  
HIS C   O    doub N N 81  
HIS C   OXT  sing N N 82  
HIS CB  CG   sing N N 83  
HIS CB  HB2  sing N N 84  
HIS CB  HB3  sing N N 85  
HIS CG  ND1  sing Y N 86  
HIS CG  CD2  doub Y N 87  
HIS ND1 CE1  doub Y N 88  
HIS ND1 HD1  sing N N 89  
HIS CD2 NE2  sing Y N 90  
HIS CD2 HD2  sing N N 91  
HIS CE1 NE2  sing Y N 92  
HIS CE1 HE1  sing N N 93  
HIS NE2 HE2  sing N N 94  
HIS OXT HXT  sing N N 95  
HOH O   H1   sing N N 96  
HOH O   H2   sing N N 97  
ILE N   CA   sing N N 98  
ILE N   H    sing N N 99  
ILE N   H2   sing N N 100 
ILE CA  C    sing N N 101 
ILE CA  CB   sing N N 102 
ILE CA  HA   sing N N 103 
ILE C   O    doub N N 104 
ILE C   OXT  sing N N 105 
ILE CB  CG1  sing N N 106 
ILE CB  CG2  sing N N 107 
ILE CB  HB   sing N N 108 
ILE CG1 CD1  sing N N 109 
ILE CG1 HG12 sing N N 110 
ILE CG1 HG13 sing N N 111 
ILE CG2 HG21 sing N N 112 
ILE CG2 HG22 sing N N 113 
ILE CG2 HG23 sing N N 114 
ILE CD1 HD11 sing N N 115 
ILE CD1 HD12 sing N N 116 
ILE CD1 HD13 sing N N 117 
ILE OXT HXT  sing N N 118 
LEU N   CA   sing N N 119 
LEU N   H    sing N N 120 
LEU N   H2   sing N N 121 
LEU CA  C    sing N N 122 
LEU CA  CB   sing N N 123 
LEU CA  HA   sing N N 124 
LEU C   O    doub N N 125 
LEU C   OXT  sing N N 126 
LEU CB  CG   sing N N 127 
LEU CB  HB2  sing N N 128 
LEU CB  HB3  sing N N 129 
LEU CG  CD1  sing N N 130 
LEU CG  CD2  sing N N 131 
LEU CG  HG   sing N N 132 
LEU CD1 HD11 sing N N 133 
LEU CD1 HD12 sing N N 134 
LEU CD1 HD13 sing N N 135 
LEU CD2 HD21 sing N N 136 
LEU CD2 HD22 sing N N 137 
LEU CD2 HD23 sing N N 138 
LEU OXT HXT  sing N N 139 
LYS N   CA   sing N N 140 
LYS N   H    sing N N 141 
LYS N   H2   sing N N 142 
LYS CA  C    sing N N 143 
LYS CA  CB   sing N N 144 
LYS CA  HA   sing N N 145 
LYS C   O    doub N N 146 
LYS C   OXT  sing N N 147 
LYS CB  CG   sing N N 148 
LYS CB  HB2  sing N N 149 
LYS CB  HB3  sing N N 150 
LYS CG  CD   sing N N 151 
LYS CG  HG2  sing N N 152 
LYS CG  HG3  sing N N 153 
LYS CD  CE   sing N N 154 
LYS CD  HD2  sing N N 155 
LYS CD  HD3  sing N N 156 
LYS CE  NZ   sing N N 157 
LYS CE  HE2  sing N N 158 
LYS CE  HE3  sing N N 159 
LYS NZ  HZ1  sing N N 160 
LYS NZ  HZ2  sing N N 161 
LYS NZ  HZ3  sing N N 162 
LYS OXT HXT  sing N N 163 
MET N   CA   sing N N 164 
MET N   H    sing N N 165 
MET N   H2   sing N N 166 
MET CA  C    sing N N 167 
MET CA  CB   sing N N 168 
MET CA  HA   sing N N 169 
MET C   O    doub N N 170 
MET C   OXT  sing N N 171 
MET CB  CG   sing N N 172 
MET CB  HB2  sing N N 173 
MET CB  HB3  sing N N 174 
MET CG  SD   sing N N 175 
MET CG  HG2  sing N N 176 
MET CG  HG3  sing N N 177 
MET SD  CE   sing N N 178 
MET CE  HE1  sing N N 179 
MET CE  HE2  sing N N 180 
MET CE  HE3  sing N N 181 
MET OXT HXT  sing N N 182 
PHE N   CA   sing N N 183 
PHE N   H    sing N N 184 
PHE N   H2   sing N N 185 
PHE CA  C    sing N N 186 
PHE CA  CB   sing N N 187 
PHE CA  HA   sing N N 188 
PHE C   O    doub N N 189 
PHE C   OXT  sing N N 190 
PHE CB  CG   sing N N 191 
PHE CB  HB2  sing N N 192 
PHE CB  HB3  sing N N 193 
PHE CG  CD1  doub Y N 194 
PHE CG  CD2  sing Y N 195 
PHE CD1 CE1  sing Y N 196 
PHE CD1 HD1  sing N N 197 
PHE CD2 CE2  doub Y N 198 
PHE CD2 HD2  sing N N 199 
PHE CE1 CZ   doub Y N 200 
PHE CE1 HE1  sing N N 201 
PHE CE2 CZ   sing Y N 202 
PHE CE2 HE2  sing N N 203 
PHE CZ  HZ   sing N N 204 
PHE OXT HXT  sing N N 205 
PRO N   CA   sing N N 206 
PRO N   CD   sing N N 207 
PRO N   H    sing N N 208 
PRO CA  C    sing N N 209 
PRO CA  CB   sing N N 210 
PRO CA  HA   sing N N 211 
PRO C   O    doub N N 212 
PRO C   OXT  sing N N 213 
PRO CB  CG   sing N N 214 
PRO CB  HB2  sing N N 215 
PRO CB  HB3  sing N N 216 
PRO CG  CD   sing N N 217 
PRO CG  HG2  sing N N 218 
PRO CG  HG3  sing N N 219 
PRO CD  HD2  sing N N 220 
PRO CD  HD3  sing N N 221 
PRO OXT HXT  sing N N 222 
SER N   CA   sing N N 223 
SER N   H    sing N N 224 
SER N   H2   sing N N 225 
SER CA  C    sing N N 226 
SER CA  CB   sing N N 227 
SER CA  HA   sing N N 228 
SER C   O    doub N N 229 
SER C   OXT  sing N N 230 
SER CB  OG   sing N N 231 
SER CB  HB2  sing N N 232 
SER CB  HB3  sing N N 233 
SER OG  HG   sing N N 234 
SER OXT HXT  sing N N 235 
THR N   CA   sing N N 236 
THR N   H    sing N N 237 
THR N   H2   sing N N 238 
THR CA  C    sing N N 239 
THR CA  CB   sing N N 240 
THR CA  HA   sing N N 241 
THR C   O    doub N N 242 
THR C   OXT  sing N N 243 
THR CB  OG1  sing N N 244 
THR CB  CG2  sing N N 245 
THR CB  HB   sing N N 246 
THR OG1 HG1  sing N N 247 
THR CG2 HG21 sing N N 248 
THR CG2 HG22 sing N N 249 
THR CG2 HG23 sing N N 250 
THR OXT HXT  sing N N 251 
TYR N   CA   sing N N 252 
TYR N   H    sing N N 253 
TYR N   H2   sing N N 254 
TYR CA  C    sing N N 255 
TYR CA  CB   sing N N 256 
TYR CA  HA   sing N N 257 
TYR C   O    doub N N 258 
TYR C   OXT  sing N N 259 
TYR CB  CG   sing N N 260 
TYR CB  HB2  sing N N 261 
TYR CB  HB3  sing N N 262 
TYR CG  CD1  doub Y N 263 
TYR CG  CD2  sing Y N 264 
TYR CD1 CE1  sing Y N 265 
TYR CD1 HD1  sing N N 266 
TYR CD2 CE2  doub Y N 267 
TYR CD2 HD2  sing N N 268 
TYR CE1 CZ   doub Y N 269 
TYR CE1 HE1  sing N N 270 
TYR CE2 CZ   sing Y N 271 
TYR CE2 HE2  sing N N 272 
TYR CZ  OH   sing N N 273 
TYR OH  HH   sing N N 274 
TYR OXT HXT  sing N N 275 
VAL N   CA   sing N N 276 
VAL N   H    sing N N 277 
VAL N   H2   sing N N 278 
VAL CA  C    sing N N 279 
VAL CA  CB   sing N N 280 
VAL CA  HA   sing N N 281 
VAL C   O    doub N N 282 
VAL C   OXT  sing N N 283 
VAL CB  CG1  sing N N 284 
VAL CB  CG2  sing N N 285 
VAL CB  HB   sing N N 286 
VAL CG1 HG11 sing N N 287 
VAL CG1 HG12 sing N N 288 
VAL CG1 HG13 sing N N 289 
VAL CG2 HG21 sing N N 290 
VAL CG2 HG22 sing N N 291 
VAL CG2 HG23 sing N N 292 
VAL OXT HXT  sing N N 293 
# 
_pdbx_audit_support.funding_organization   'Howard Hughes Medical Institute (HHMI)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          'de novo designed model' 
# 
_space_group.name_H-M_alt     'I 2 2 2' 
_space_group.name_Hall        'I 2 2' 
_space_group.IT_number        23 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9DEC 
_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]   0.014712 
_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]   0.014435 
_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]   0.011839 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . GLY A 1 1  ? 19.31050  15.02398 25.05844  1.000 64.98467  ? -2  GLY A N   1 
ATOM   2    C CA  . GLY A 1 1  ? 18.73417  14.89442 26.38388  1.000 63.52775  ? -2  GLY A CA  1 
ATOM   3    C C   . GLY A 1 1  ? 18.76275  16.19376 27.16130  1.000 65.77850  ? -2  GLY A C   1 
ATOM   4    O O   . GLY A 1 1  ? 17.76911  16.91314 27.21499  1.000 59.38335  ? -2  GLY A O   1 
ATOM   5    N N   . GLY A 1 2  ? 19.90641  16.50470 27.76233  1.000 63.66958  ? -1  GLY A N   1 
ATOM   6    C CA  . GLY A 1 2  ? 20.02416  17.73535 28.51750  1.000 61.67903  ? -1  GLY A CA  1 
ATOM   7    C C   . GLY A 1 2  ? 21.26177  18.52994 28.16066  1.000 71.25649  ? -1  GLY A C   1 
ATOM   8    O O   . GLY A 1 2  ? 21.82176  18.36100 27.07417  1.000 70.65478  ? -1  GLY A O   1 
ATOM   9    N N   . GLY A 1 3  ? 21.70510  19.39035 29.06788  1.000 68.96309  ? 0   GLY A N   1 
ATOM   10   C CA  . GLY A 1 3  ? 22.88936  20.19846 28.84453  1.000 74.40146  ? 0   GLY A CA  1 
ATOM   11   C C   . GLY A 1 3  ? 22.56301  21.62069 28.43488  1.000 80.83406  ? 0   GLY A C   1 
ATOM   12   O O   . GLY A 1 3  ? 21.42833  22.09497 28.53795  1.000 82.05175  ? 0   GLY A O   1 
ATOM   13   N N   . SER A 1 4  ? 23.59971  22.31529 27.96881  1.000 74.10902  ? 1   SER A N   1 
ATOM   14   C CA  . SER A 1 4  ? 23.43452  23.68913 27.51812  1.000 65.38038  ? 1   SER A CA  1 
ATOM   15   C C   . SER A 1 4  ? 22.72173  23.74121 26.17218  1.000 68.30855  ? 1   SER A C   1 
ATOM   16   O O   . SER A 1 4  ? 22.88356  22.86566 25.31698  1.000 64.32544  ? 1   SER A O   1 
ATOM   17   C CB  . SER A 1 4  ? 24.78876  24.38647 27.40523  1.000 67.10202  ? 1   SER A CB  1 
ATOM   18   O OG  . SER A 1 4  ? 25.16579  24.56399 26.04749  1.000 56.59161  ? 1   SER A OG  1 
ATOM   19   N N   . ILE A 1 5  ? 21.93612  24.79962 25.98405  1.000 64.90422  ? 2   ILE A N   1 
ATOM   20   C CA  . ILE A 1 5  ? 21.20376  25.02721 24.74919  1.000 49.16128  ? 2   ILE A CA  1 
ATOM   21   C C   . ILE A 1 5  ? 21.66921  26.28719 24.03586  1.000 56.93587  ? 2   ILE A C   1 
ATOM   22   O O   . ILE A 1 5  ? 21.01314  26.74351 23.09927  1.000 52.98041  ? 2   ILE A O   1 
ATOM   23   C CB  . ILE A 1 5  ? 19.68467  25.07959 25.00555  1.000 49.77231  ? 2   ILE A CB  1 
ATOM   24   C CG1 . ILE A 1 5  ? 19.34205  26.24885 25.93472  1.000 53.39012  ? 2   ILE A CG1 1 
ATOM   25   C CG2 . ILE A 1 5  ? 19.19509  23.75844 25.58363  1.000 53.66965  ? 2   ILE A CG2 1 
ATOM   26   C CD1 . ILE A 1 5  ? 17.86798  26.34759 26.27543  1.000 54.11645  ? 2   ILE A CD1 1 
ATOM   27   N N   . LYS A 1 6  ? 22.79205  26.86623 24.46799  1.000 51.33641  ? 3   LYS A N   1 
ATOM   28   C CA  . LYS A 1 6  ? 23.26683  28.10305 23.85928  1.000 58.55356  ? 3   LYS A CA  1 
ATOM   29   C C   . LYS A 1 6  ? 23.64293  27.88938 22.39992  1.000 56.78070  ? 3   LYS A C   1 
ATOM   30   O O   . LYS A 1 6  ? 23.44029  28.77533 21.56129  1.000 51.17403  ? 3   LYS A O   1 
ATOM   31   C CB  . LYS A 1 6  ? 24.45621  28.65190 24.64643  1.000 60.41957  ? 3   LYS A CB  1 
ATOM   32   C CG  . LYS A 1 6  ? 24.76277  30.10853 24.34163  1.000 74.28982  ? 3   LYS A CG  1 
ATOM   33   C CD  . LYS A 1 6  ? 23.61194  31.01518 24.76809  1.000 71.98952  ? 3   LYS A CD  1 
ATOM   34   C CE  . LYS A 1 6  ? 23.30148  32.06938 23.70801  1.000 66.57867  ? 3   LYS A CE  1 
ATOM   35   N NZ  . LYS A 1 6  ? 22.11446  32.89563 24.07321  1.000 63.22424  ? 3   LYS A NZ  1 
ATOM   36   N N   . GLU A 1 7  ? 24.19425  26.71822 22.07578  1.000 55.76912  ? 4   GLU A N   1 
ATOM   37   C CA  . GLU A 1 7  ? 24.52450  26.41552 20.68786  1.000 47.93321  ? 4   GLU A CA  1 
ATOM   38   C C   . GLU A 1 7  ? 23.27104  26.34845 19.82481  1.000 54.01323  ? 4   GLU A C   1 
ATOM   39   O O   . GLU A 1 7  ? 23.23343  26.91387 18.72520  1.000 50.80777  ? 4   GLU A O   1 
ATOM   40   C CB  . GLU A 1 7  ? 25.30373  25.10418 20.61862  1.000 58.00877  ? 4   GLU A CB  1 
ATOM   41   C CG  . GLU A 1 7  ? 25.33066  24.45372 19.24430  1.000 62.84626  ? 4   GLU A CG  1 
ATOM   42   C CD  . GLU A 1 7  ? 26.00992  23.09780 19.26341  1.000 76.05682  ? 4   GLU A CD  1 
ATOM   43   O OE1 . GLU A 1 7  ? 27.24729  23.04641 19.42966  1.000 73.75620  ? 4   GLU A OE1 1 
ATOM   44   O OE2 . GLU A 1 7  ? 25.29893  22.07991 19.14365  1.000 71.04053  ? 4   GLU A OE2 1 
ATOM   45   N N   . ILE A 1 8  ? 22.23528  25.66102 20.30974  1.000 41.33206  ? 5   ILE A N   1 
ATOM   46   C CA  . ILE A 1 8  ? 20.95910  25.62400 19.60656  1.000 43.98664  ? 5   ILE A CA  1 
ATOM   47   C C   . ILE A 1 8  ? 20.35604  27.02163 19.52623  1.000 41.65773  ? 5   ILE A C   1 
ATOM   48   O O   . ILE A 1 8  ? 19.79261  27.41433 18.49788  1.000 34.48201  ? 5   ILE A O   1 
ATOM   49   C CB  . ILE A 1 8  ? 20.01324  24.63043 20.30693  1.000 36.02173  ? 5   ILE A CB  1 
ATOM   50   C CG1 . ILE A 1 8  ? 20.72251  23.29290 20.53796  1.000 53.81126  ? 5   ILE A CG1 1 
ATOM   51   C CG2 . ILE A 1 8  ? 18.75512  24.41670 19.49574  1.000 55.33023  ? 5   ILE A CG2 1 
ATOM   52   C CD1 . ILE A 1 8  ? 19.88749  22.27905 21.28455  1.000 65.95625  ? 5   ILE A CD1 1 
ATOM   53   N N   . THR A 1 9  ? 20.47361  27.79701 20.60507  1.000 43.93852  ? 6   THR A N   1 
ATOM   54   C CA  . THR A 1 9  ? 19.89261  29.13583 20.63095  1.000 35.68306  ? 6   THR A CA  1 
ATOM   55   C C   . THR A 1 9  ? 20.59713  30.06773 19.65178  1.000 46.57869  ? 6   THR A C   1 
ATOM   56   O O   . THR A 1 9  ? 19.94531  30.75105 18.85263  1.000 36.74595  ? 6   THR A O   1 
ATOM   57   C CB  . THR A 1 9  ? 19.96145  29.70651 22.04579  1.000 48.87116  ? 6   THR A CB  1 
ATOM   58   O OG1 . THR A 1 9  ? 19.21940  28.86495 22.93552  1.000 49.13631  ? 6   THR A OG1 1 
ATOM   59   C CG2 . THR A 1 9  ? 19.39630  31.12454 22.07355  1.000 38.14947  ? 6   THR A CG2 1 
ATOM   60   N N   . GLU A 1 10 ? 21.93202  30.12020 19.71388  1.000 35.57493  ? 7   GLU A N   1 
ATOM   61   C CA  . GLU A 1 10 ? 22.68842  31.00330 18.83039  1.000 45.69814  ? 7   GLU A CA  1 
ATOM   62   C C   . GLU A 1 10 ? 22.43782  30.67030 17.36729  1.000 43.64401  ? 7   GLU A C   1 
ATOM   63   O O   . GLU A 1 10 ? 22.40572  31.56584 16.51434  1.000 44.14410  ? 7   GLU A O   1 
ATOM   64   C CB  . GLU A 1 10 ? 24.18099  30.91409 19.14896  1.000 38.14891  ? 7   GLU A CB  1 
ATOM   65   C CG  . GLU A 1 10 ? 24.64161  31.81957 20.27761  1.000 61.32635  ? 7   GLU A CG  1 
ATOM   66   C CD  . GLU A 1 10 ? 24.97132  33.22667 19.80843  1.000 74.57257  ? 7   GLU A CD  1 
ATOM   67   O OE1 . GLU A 1 10 ? 24.25503  33.75406 18.93070  1.000 73.89663  ? 7   GLU A OE1 1 
ATOM   68   O OE2 . GLU A 1 10 ? 25.95741  33.80384 20.31401  1.000 64.13604  ? 7   GLU A OE2 1 
ATOM   69   N N   . THR A 1 11 ? 22.26495  29.38499 17.05631  1.000 44.15694  ? 8   THR A N   1 
ATOM   70   C CA  . THR A 1 11 ? 21.94922  28.99900 15.68726  1.000 33.65303  ? 8   THR A CA  1 
ATOM   71   C C   . THR A 1 11 ? 20.59034  29.54136 15.26841  1.000 33.81386  ? 8   THR A C   1 
ATOM   72   O O   . THR A 1 11 ? 20.44081  30.07291 14.16193  1.000 32.43197  ? 8   THR A O   1 
ATOM   73   C CB  . THR A 1 11 ? 21.99097  27.47889 15.54786  1.000 38.94938  ? 8   THR A CB  1 
ATOM   74   O OG1 . THR A 1 11 ? 23.28379  26.99896 15.94110  1.000 40.66477  ? 8   THR A OG1 1 
ATOM   75   C CG2 . THR A 1 11 ? 21.72138  27.07311 14.10785  1.000 33.56949  ? 8   THR A CG2 1 
ATOM   76   N N   . THR A 1 12 ? 19.59020  29.42895 16.14744  1.000 32.96834  ? 9   THR A N   1 
ATOM   77   C CA  . THR A 1 12 ? 18.26666  29.96108 15.83596  1.000 29.05019  ? 9   THR A CA  1 
ATOM   78   C C   . THR A 1 12 ? 18.30570  31.47561 15.67722  1.000 30.76144  ? 9   THR A C   1 
ATOM   79   O O   . THR A 1 12 ? 17.67520  32.02933 14.76892  1.000 34.03214  ? 9   THR A O   1 
ATOM   80   C CB  . THR A 1 12 ? 17.26902  29.56892 16.92491  1.000 28.05236  ? 9   THR A CB  1 
ATOM   81   O OG1 . THR A 1 12 ? 17.31852  28.15262 17.13626  1.000 31.15482  ? 9   THR A OG1 1 
ATOM   82   C CG2 . THR A 1 12 ? 15.85821  29.96514 16.51688  1.000 26.46202  ? 9   THR A CG2 1 
ATOM   83   N N   . GLN A 1 13 ? 19.04170  32.16367 16.55234  1.000 32.18577  ? 10  GLN A N   1 
ATOM   84   C CA  . GLN A 1 13 ? 19.18808  33.60814 16.41193  1.000 36.00717  ? 10  GLN A CA  1 
ATOM   85   C C   . GLN A 1 13 ? 19.77364  33.97293 15.05438  1.000 40.21277  ? 10  GLN A C   1 
ATOM   86   O O   . GLN A 1 13 ? 19.27127  34.87740 14.37662  1.000 38.16593  ? 10  GLN A O   1 
ATOM   87   C CB  . GLN A 1 13 ? 20.05605  34.15638 17.54156  1.000 40.95040  ? 10  GLN A CB  1 
ATOM   88   C CG  . GLN A 1 13 ? 19.41512  34.02784 18.91131  1.000 40.09319  ? 10  GLN A CG  1 
ATOM   89   C CD  . GLN A 1 13 ? 20.33992  34.45887 20.02853  1.000 51.05717  ? 10  GLN A CD  1 
ATOM   90   O OE1 . GLN A 1 13 ? 19.99615  35.32500 20.83369  1.000 74.06450  ? 10  GLN A OE1 1 
ATOM   91   N NE2 . GLN A 1 13 ? 21.52089  33.85470 20.08682  1.000 55.62284  ? 10  GLN A NE2 1 
ATOM   92   N N   . LEU A 1 14 ? 20.82296  33.26482 14.63088  1.000 41.98863  ? 11  LEU A N   1 
ATOM   93   C CA  . LEU A 1 14 ? 21.43356  33.54898 13.33719  1.000 41.19777  ? 11  LEU A CA  1 
ATOM   94   C C   . LEU A 1 14 ? 20.48479  33.21486 12.19197  1.000 43.61094  ? 11  LEU A C   1 
ATOM   95   O O   . LEU A 1 14 ? 20.46399  33.91656 11.17423  1.000 39.42355  ? 11  LEU A O   1 
ATOM   96   C CB  . LEU A 1 14 ? 22.74601  32.77858 13.19619  1.000 44.60054  ? 11  LEU A CB  1 
ATOM   97   C CG  . LEU A 1 14 ? 24.04407  33.50088 13.57258  1.000 42.34491  ? 11  LEU A CG  1 
ATOM   98   C CD1 . LEU A 1 14 ? 23.99174  34.05345 14.98883  1.000 58.95311  ? 11  LEU A CD1 1 
ATOM   99   C CD2 . LEU A 1 14 ? 25.22030  32.55429 13.41108  1.000 59.20400  ? 11  LEU A CD2 1 
ATOM   100  N N   . ILE A 1 15 ? 19.68853  32.15302 12.33883  1.000 33.53554  ? 12  ILE A N   1 
ATOM   101  C CA  . ILE A 1 15 ? 18.74028  31.78822 11.28854  1.000 36.61651  ? 12  ILE A CA  1 
ATOM   102  C C   . ILE A 1 15 ? 17.71299  32.89482 11.10023  1.000 45.38932  ? 12  ILE A C   1 
ATOM   103  O O   . ILE A 1 15 ? 17.41566  33.31167 9.97372   1.000 37.36999  ? 12  ILE A O   1 
ATOM   104  C CB  . ILE A 1 15 ? 18.06438  30.44377 11.61249  1.000 39.25826  ? 12  ILE A CB  1 
ATOM   105  C CG1 . ILE A 1 15 ? 19.04545  29.28927 11.40496  1.000 34.54254  ? 12  ILE A CG1 1 
ATOM   106  C CG2 . ILE A 1 15 ? 16.81189  30.25528 10.75940  1.000 30.54646  ? 12  ILE A CG2 1 
ATOM   107  C CD1 . ILE A 1 15 ? 18.52013  27.94922 11.86950  1.000 33.31585  ? 12  ILE A CD1 1 
ATOM   108  N N   . VAL A 1 16 ? 17.16739  33.40112 12.20530  1.000 34.40901  ? 13  VAL A N   1 
ATOM   109  C CA  . VAL A 1 16 ? 16.10222  34.38651 12.09998  1.000 33.34969  ? 13  VAL A CA  1 
ATOM   110  C C   . VAL A 1 16 ? 16.64834  35.78159 11.81602  1.000 36.06422  ? 13  VAL A C   1 
ATOM   111  O O   . VAL A 1 16 ? 15.93368  36.60841 11.23611  1.000 40.10565  ? 13  VAL A O   1 
ATOM   112  C CB  . VAL A 1 16 ? 15.23026  34.34005 13.36765  1.000 31.95846  ? 13  VAL A CB  1 
ATOM   113  C CG1 . VAL A 1 16 ? 15.89211  35.08387 14.52449  1.000 30.78417  ? 13  VAL A CG1 1 
ATOM   114  C CG2 . VAL A 1 16 ? 13.83296  34.85964 13.07133  1.000 44.00472  ? 13  VAL A CG2 1 
ATOM   115  N N   . LYS A 1 17 ? 17.90632  36.05919 12.17657  1.000 33.45162  ? 14  LYS A N   1 
ATOM   116  C CA  . LYS A 1 17 ? 18.53033  37.31007 11.76017  1.000 42.00045  ? 14  LYS A CA  1 
ATOM   117  C C   . LYS A 1 17 ? 18.63735  37.40131 10.24505  1.000 41.53613  ? 14  LYS A C   1 
ATOM   118  O O   . LYS A 1 17 ? 18.55279  38.49747 9.68340   1.000 40.03927  ? 14  LYS A O   1 
ATOM   119  C CB  . LYS A 1 17 ? 19.92240  37.45246 12.38224  1.000 46.38470  ? 14  LYS A CB  1 
ATOM   120  C CG  . LYS A 1 17 ? 19.93906  37.89827 13.83252  1.000 46.01054  ? 14  LYS A CG  1 
ATOM   121  C CD  . LYS A 1 17 ? 21.36074  37.88096 14.37887  1.000 54.93609  ? 14  LYS A CD  1 
ATOM   122  C CE  . LYS A 1 17 ? 21.38879  38.11479 15.87834  1.000 59.24037  ? 14  LYS A CE  1 
ATOM   123  N NZ  . LYS A 1 17 ? 22.74874  37.90797 16.44815  1.000 54.68627  ? 14  LYS A NZ  1 
ATOM   124  N N   . HIS A 1 18 ? 18.81869  36.26784 9.56956   1.000 43.15040  ? 15  HIS A N   1 
ATOM   125  C CA  . HIS A 1 18 ? 19.05757  36.26403 8.13225   1.000 42.77837  ? 15  HIS A CA  1 
ATOM   126  C C   . HIS A 1 18 ? 17.78279  36.32177 7.30421   1.000 38.75081  ? 15  HIS A C   1 
ATOM   127  O O   . HIS A 1 18 ? 17.80397  36.85528 6.18808   1.000 41.65885  ? 15  HIS A O   1 
ATOM   128  C CB  . HIS A 1 18 ? 19.85198  35.01664 7.74079   1.000 38.85094  ? 15  HIS A CB  1 
ATOM   129  C CG  . HIS A 1 18 ? 21.27062  35.03491 8.21075   1.000 52.17029  ? 15  HIS A CG  1 
ATOM   130  N ND1 . HIS A 1 18 ? 21.81245  36.10087 8.89888   1.000 58.27172  ? 15  HIS A ND1 1 
ATOM   131  C CD2 . HIS A 1 18 ? 22.26410  34.12423 8.08800   1.000 55.47157  ? 15  HIS A CD2 1 
ATOM   132  C CE1 . HIS A 1 18 ? 23.07579  35.84370 9.18041   1.000 59.39853  ? 15  HIS A CE1 1 
ATOM   133  N NE2 . HIS A 1 18 ? 23.37559  34.64969 8.69948   1.000 58.38897  ? 15  HIS A NE2 1 
ATOM   134  N N   . LEU A 1 19 ? 16.67512  35.79464 7.81914   1.000 36.01042  ? 16  LEU A N   1 
ATOM   135  C CA  . LEU A 1 19 ? 15.48020  35.58227 7.01587   1.000 47.84397  ? 16  LEU A CA  1 
ATOM   136  C C   . LEU A 1 19 ? 14.35354  36.56010 7.31874   1.000 43.43531  ? 16  LEU A C   1 
ATOM   137  O O   . LEU A 1 19 ? 13.28358  36.45743 6.70782   1.000 47.06037  ? 16  LEU A O   1 
ATOM   138  C CB  . LEU A 1 19 ? 14.98452  34.14421 7.20070   1.000 35.31227  ? 16  LEU A CB  1 
ATOM   139  C CG  . LEU A 1 19 ? 16.02246  33.07797 6.84750   1.000 40.08803  ? 16  LEU A CG  1 
ATOM   140  C CD1 . LEU A 1 19 ? 15.38395  31.69919 6.82000   1.000 35.49082  ? 16  LEU A CD1 1 
ATOM   141  C CD2 . LEU A 1 19 ? 16.68913  33.40536 5.51640   1.000 37.54742  ? 16  LEU A CD2 1 
ATOM   142  N N   . ALA A 1 20 ? 14.55785  37.50373 8.23175   1.000 43.38294  ? 17  ALA A N   1 
ATOM   143  C CA  . ALA A 1 20 ? 13.52900  38.46628 8.59252   1.000 39.27202  ? 17  ALA A CA  1 
ATOM   144  C C   . ALA A 1 20 ? 14.10500  39.87078 8.52561   1.000 52.02372  ? 17  ALA A C   1 
ATOM   145  O O   . ALA A 1 20 ? 15.25761  40.09504 8.90774   1.000 49.05125  ? 17  ALA A O   1 
ATOM   146  C CB  . ALA A 1 20 ? 12.97220  38.19076 9.99575   1.000 35.06107  ? 17  ALA A CB  1 
ATOM   147  N N   . HIS A 1 21 ? 13.30018  40.81422 8.02693   1.000 43.74571  ? 18  HIS A N   1 
ATOM   148  C CA  . HIS A 1 21 ? 13.73054  42.20832 8.01487   1.000 47.38484  ? 18  HIS A CA  1 
ATOM   149  C C   . HIS A 1 21 ? 13.94737  42.72687 9.42889   1.000 47.20757  ? 18  HIS A C   1 
ATOM   150  O O   . HIS A 1 21 ? 14.81259  43.58171 9.65323   1.000 49.37034  ? 18  HIS A O   1 
ATOM   151  C CB  . HIS A 1 21 ? 12.71087  43.07529 7.26921   1.000 50.89517  ? 18  HIS A CB  1 
ATOM   152  C CG  . HIS A 1 21 ? 11.33768  43.05951 7.86958   1.000 53.96037  ? 18  HIS A CG  1 
ATOM   153  N ND1 . HIS A 1 21 ? 11.01541  43.75768 9.01403   1.000 63.21125  ? 18  HIS A ND1 1 
ATOM   154  C CD2 . HIS A 1 21 ? 10.19855  42.44204 7.47437   1.000 58.32294  ? 18  HIS A CD2 1 
ATOM   155  C CE1 . HIS A 1 21 ? 9.74087   43.56319 9.30312   1.000 57.02109  ? 18  HIS A CE1 1 
ATOM   156  N NE2 . HIS A 1 21 ? 9.22186   42.76908 8.38398   1.000 49.48789  ? 18  HIS A NE2 1 
ATOM   157  N N   . ASN A 1 22 ? 13.18283  42.21159 10.39089  1.000 46.37910  ? 19  ASN A N   1 
ATOM   158  C CA  . ASN A 1 22 ? 13.36479  42.53083 11.79968  1.000 43.80301  ? 19  ASN A CA  1 
ATOM   159  C C   . ASN A 1 22 ? 13.97437  41.33917 12.52551  1.000 41.91586  ? 19  ASN A C   1 
ATOM   160  O O   . ASN A 1 22 ? 13.51637  40.96432 13.60993  1.000 45.45521  ? 19  ASN A O   1 
ATOM   161  C CB  . ASN A 1 22 ? 12.03066  42.92277 12.43784  1.000 47.88204  ? 19  ASN A CB  1 
ATOM   162  C CG  . ASN A 1 22 ? 10.89974  41.99263 12.03829  1.000 59.97194  ? 19  ASN A CG  1 
ATOM   163  O OD1 . ASN A 1 22 ? 11.08507  41.08609 11.22545  1.000 52.21222  ? 19  ASN A OD1 1 
ATOM   164  N ND2 . ASN A 1 22 ? 9.72131   42.21049 12.61179  1.000 53.92539  ? 19  ASN A ND2 1 
ATOM   165  N N   . GLY A 1 23 ? 15.00387  40.73436 11.92662  1.000 45.22357  ? 20  GLY A N   1 
ATOM   166  C CA  . GLY A 1 23 ? 15.61526  39.55969 12.52426  1.000 39.39712  ? 20  GLY A CA  1 
ATOM   167  C C   . GLY A 1 23 ? 16.23235  39.82713 13.88163  1.000 36.99039  ? 20  GLY A C   1 
ATOM   168  O O   . GLY A 1 23 ? 16.21128  38.95740 14.75711  1.000 37.43041  ? 20  GLY A O   1 
ATOM   169  N N   . GLU A 1 24 ? 16.79065  41.02570 14.07738  1.000 44.96797  ? 21  GLU A N   1 
ATOM   170  C CA  . GLU A 1 24 ? 17.38070  41.36323 15.36917  1.000 42.10256  ? 21  GLU A CA  1 
ATOM   171  C C   . GLU A 1 24 ? 16.33357  41.34163 16.47421  1.000 40.54077  ? 21  GLU A C   1 
ATOM   172  O O   . GLU A 1 24 ? 16.59993  40.86221 17.58273  1.000 39.93312  ? 21  GLU A O   1 
ATOM   173  C CB  . GLU A 1 24 ? 18.06329  42.73063 15.30026  1.000 46.40555  ? 21  GLU A CB  1 
ATOM   174  C CG  . GLU A 1 24 ? 19.46188  42.69816 14.69928  1.000 64.66246  ? 21  GLU A CG  1 
ATOM   175  C CD  . GLU A 1 24 ? 20.43607  41.87875 15.52656  1.000 56.90682  ? 21  GLU A CD  1 
ATOM   176  O OE1 . GLU A 1 24 ? 20.25260  41.79337 16.75981  1.000 57.78113  ? 21  GLU A OE1 1 
ATOM   177  O OE2 . GLU A 1 24 ? 21.38489  41.31717 14.94045  1.000 64.03793  ? 21  GLU A OE2 1 
ATOM   178  N N   . GLU A 1 25 ? 15.13083  41.84579 16.18912  1.000 44.81997  ? 22  GLU A N   1 
ATOM   179  C CA  . GLU A 1 25 ? 14.06841  41.80448 17.18819  1.000 47.84830  ? 22  GLU A CA  1 
ATOM   180  C C   . GLU A 1 25 ? 13.61438  40.37581 17.46284  1.000 43.26822  ? 22  GLU A C   1 
ATOM   181  O O   . GLU A 1 25 ? 13.19563  40.06639 18.58415  1.000 42.58732  ? 22  GLU A O   1 
ATOM   182  C CB  . GLU A 1 25 ? 12.89159  42.67816 16.74570  1.000 51.89732  ? 22  GLU A CB  1 
ATOM   183  C CG  . GLU A 1 25 ? 13.23887  44.16455 16.65578  1.000 63.29421  ? 22  GLU A CG  1 
ATOM   184  C CD  . GLU A 1 25 ? 12.03473  45.04677 16.37151  1.000 86.40035  ? 22  GLU A CD  1 
ATOM   185  O OE1 . GLU A 1 25 ? 11.05766  44.55195 15.77212  1.000 75.68857  ? 22  GLU A OE1 1 
ATOM   186  O OE2 . GLU A 1 25 ? 12.06737  46.23872 16.74910  1.000 85.93434  ? 22  GLU A OE2 1 
ATOM   187  N N   . TYR A 1 26 ? 13.69768  39.49082 16.46552  1.000 43.21774  ? 23  TYR A N   1 
ATOM   188  C CA  . TYR A 1 26 ? 13.38278  38.08583 16.70720  1.000 35.64708  ? 23  TYR A CA  1 
ATOM   189  C C   . TYR A 1 26 ? 14.48377  37.40423 17.50784  1.000 38.04711  ? 23  TYR A C   1 
ATOM   190  O O   . TYR A 1 26 ? 14.20341  36.54311 18.34977  1.000 31.39071  ? 23  TYR A O   1 
ATOM   191  C CB  . TYR A 1 26 ? 13.16934  37.34866 15.38764  1.000 34.61036  ? 23  TYR A CB  1 
ATOM   192  C CG  . TYR A 1 26 ? 11.85367  37.62589 14.70140  1.000 34.95362  ? 23  TYR A CG  1 
ATOM   193  C CD1 . TYR A 1 26 ? 10.65217  37.25725 15.28679  1.000 36.74970  ? 23  TYR A CD1 1 
ATOM   194  C CD2 . TYR A 1 26 ? 11.81622  38.23001 13.45225  1.000 40.60561  ? 23  TYR A CD2 1 
ATOM   195  C CE1 . TYR A 1 26 ? 9.44582   37.50549 14.65676  1.000 46.42564  ? 23  TYR A CE1 1 
ATOM   196  C CE2 . TYR A 1 26 ? 10.61916  38.47684 12.81409  1.000 48.77070  ? 23  TYR A CE2 1 
ATOM   197  C CZ  . TYR A 1 26 ? 9.43628   38.11246 13.41915  1.000 43.37824  ? 23  TYR A CZ  1 
ATOM   198  O OH  . TYR A 1 26 ? 8.24206   38.35923 12.78330  1.000 54.49968  ? 23  TYR A OH  1 
ATOM   199  N N   . SER A 1 27 ? 15.74215  37.76987 17.24604  1.000 37.59273  ? 24  SER A N   1 
ATOM   200  C CA  . SER A 1 27 ? 16.86469  37.17516 17.96395  1.000 35.38676  ? 24  SER A CA  1 
ATOM   201  C C   . SER A 1 27 ? 16.77937  37.45718 19.45836  1.000 43.52873  ? 24  SER A C   1 
ATOM   202  O O   . SER A 1 27 ? 17.07793  36.58239 20.27973  1.000 40.84748  ? 24  SER A O   1 
ATOM   203  C CB  . SER A 1 27 ? 18.18103  37.69925 17.39069  1.000 40.42530  ? 24  SER A CB  1 
ATOM   204  O OG  . SER A 1 27 ? 19.28205  37.31321 18.19231  1.000 51.90295  ? 24  SER A OG  1 
ATOM   205  N N   . GLU A 1 28 ? 16.37932  38.67591 19.83079  1.000 48.46701  ? 25  GLU A N   1 
ATOM   206  C CA  . GLU A 1 28 ? 16.18227  38.98563 21.24309  1.000 55.50915  ? 25  GLU A CA  1 
ATOM   207  C C   . GLU A 1 28 ? 15.08818  38.11408 21.84605  1.000 45.22181  ? 25  GLU A C   1 
ATOM   208  O O   . GLU A 1 28 ? 15.19287  37.67989 22.99974  1.000 46.05555  ? 25  GLU A O   1 
ATOM   209  C CB  . GLU A 1 28 ? 15.84563  40.46686 21.41589  1.000 65.53982  ? 25  GLU A CB  1 
ATOM   210  C CG  . GLU A 1 28 ? 15.54347  40.86935 22.85093  1.000 82.14289  ? 25  GLU A CG  1 
ATOM   211  C CD  . GLU A 1 28 ? 16.72509  40.65959 23.77615  1.000 85.94218  ? 25  GLU A CD  1 
ATOM   212  O OE1 . GLU A 1 28 ? 17.86147  40.98381 23.37184  1.000 74.26464  ? 25  GLU A OE1 1 
ATOM   213  O OE2 . GLU A 1 28 ? 16.51790  40.16645 24.90524  1.000 82.01714  ? 25  GLU A OE2 1 
ATOM   214  N N   . VAL A 1 29 ? 14.02832  37.84784 21.07954  1.000 44.02537  ? 26  VAL A N   1 
ATOM   215  C CA  . VAL A 1 29 ? 12.97783  36.95431 21.55467  1.000 38.05931  ? 26  VAL A CA  1 
ATOM   216  C C   . VAL A 1 29 ? 13.53394  35.55575 21.78159  1.000 38.79827  ? 26  VAL A C   1 
ATOM   217  O O   . VAL A 1 29 ? 13.23530  34.91377 22.79564  1.000 36.10778  ? 26  VAL A O   1 
ATOM   218  C CB  . VAL A 1 29 ? 11.79545  36.94279 20.56900  1.000 36.31932  ? 26  VAL A CB  1 
ATOM   219  C CG1 . VAL A 1 29 ? 10.83040  35.82427 20.91456  1.000 34.32427  ? 26  VAL A CG1 1 
ATOM   220  C CG2 . VAL A 1 29 ? 11.08112  38.28257 20.58694  1.000 38.83773  ? 26  VAL A CG2 1 
ATOM   221  N N   . VAL A 1 30 ? 14.36044  35.06793 20.85068  1.000 37.47057  ? 27  VAL A N   1 
ATOM   222  C CA  . VAL A 1 30 ? 14.97199  33.74980 21.00925  1.000 39.54535  ? 27  VAL A CA  1 
ATOM   223  C C   . VAL A 1 30 ? 15.77794  33.69143 22.29646  1.000 48.35148  ? 27  VAL A C   1 
ATOM   224  O O   . VAL A 1 30 ? 15.75165  32.68491 23.01659  1.000 36.73514  ? 27  VAL A O   1 
ATOM   225  C CB  . VAL A 1 30 ? 15.84566  33.40755 19.78765  1.000 36.96670  ? 27  VAL A CB  1 
ATOM   226  C CG1 . VAL A 1 30 ? 16.46410  32.02400 19.94341  1.000 38.94470  ? 27  VAL A CG1 1 
ATOM   227  C CG2 . VAL A 1 30 ? 15.03278  33.47602 18.52232  1.000 31.58852  ? 27  VAL A CG2 1 
ATOM   228  N N   . LYS A 1 31 ? 16.50191  34.77208 22.60758  1.000 32.67433  ? 28  LYS A N   1 
ATOM   229  C CA  . LYS A 1 31 ? 17.29817  34.82716 23.82857  1.000 39.65453  ? 28  LYS A CA  1 
ATOM   230  C C   . LYS A 1 31 ? 16.41347  34.68940 25.06206  1.000 51.83865  ? 28  LYS A C   1 
ATOM   231  O O   . LYS A 1 31 ? 16.62543  33.80408 25.89931  1.000 42.51821  ? 28  LYS A O   1 
ATOM   232  C CB  . LYS A 1 31 ? 18.08593  36.14027 23.87202  1.000 55.48050  ? 28  LYS A CB  1 
ATOM   233  C CG  . LYS A 1 31 ? 19.51265  36.02367 24.38683  1.000 55.97796  ? 28  LYS A CG  1 
ATOM   234  C CD  . LYS A 1 31 ? 20.15269  37.40064 24.56500  1.000 66.82467  ? 28  LYS A CD  1 
ATOM   235  C CE  . LYS A 1 31 ? 20.17564  38.20616 23.26699  1.000 70.68799  ? 28  LYS A CE  1 
ATOM   236  N NZ  . LYS A 1 31 ? 21.11660  37.65527 22.25071  1.000 73.38231  ? 28  LYS A NZ  1 
ATOM   237  N N   . GLU A 1 32 ? 15.40704  35.56024 25.18479  1.000 53.27783  ? 29  GLU A N   1 
ATOM   238  C CA  . GLU A 1 32 ? 14.50881  35.50918 26.33445  1.000 47.97652  ? 29  GLU A CA  1 
ATOM   239  C C   . GLU A 1 32 ? 13.72671  34.20296 26.38391  1.000 50.61907  ? 29  GLU A C   1 
ATOM   240  O O   . GLU A 1 32 ? 13.43649  33.69647 27.47314  1.000 52.60634  ? 29  GLU A O   1 
ATOM   241  C CB  . GLU A 1 32 ? 13.54877  36.69915 26.30162  1.000 49.70463  ? 29  GLU A CB  1 
ATOM   242  C CG  . GLU A 1 32 ? 12.64089  36.80646 27.51824  1.000 64.07774  ? 29  GLU A CG  1 
ATOM   243  C CD  . GLU A 1 32 ? 11.64185  37.94239 27.40784  1.000 63.66928  ? 29  GLU A CD  1 
ATOM   244  O OE1 . GLU A 1 32 ? 11.65691  38.65654 26.38312  1.000 60.54599  ? 29  GLU A OE1 1 
ATOM   245  O OE2 . GLU A 1 32 ? 10.83936  38.11950 28.34804  1.000 66.01260  ? 29  GLU A OE2 1 
ATOM   246  N N   . ILE A 1 33 ? 13.37411  33.64720 25.22475  1.000 39.57784  ? 30  ILE A N   1 
ATOM   247  C CA  . ILE A 1 33 ? 12.63722  32.38835 25.20248  1.000 43.88343  ? 30  ILE A CA  1 
ATOM   248  C C   . ILE A 1 33 ? 13.54579  31.22865 25.58607  1.000 43.73779  ? 30  ILE A C   1 
ATOM   249  O O   . ILE A 1 33 ? 13.14159  30.32788 26.33000  1.000 40.95215  ? 30  ILE A O   1 
ATOM   250  C CB  . ILE A 1 33 ? 11.98921  32.17873 23.82126  1.000 46.76121  ? 30  ILE A CB  1 
ATOM   251  C CG1 . ILE A 1 33 ? 10.53896  32.66318 23.83496  1.000 42.29667  ? 30  ILE A CG1 1 
ATOM   252  C CG2 . ILE A 1 33 ? 12.05726  30.72129 23.39320  1.000 46.68466  ? 30  ILE A CG2 1 
ATOM   253  C CD1 . ILE A 1 33 ? 10.35951  34.10831 24.23214  1.000 47.26204  ? 30  ILE A CD1 1 
ATOM   254  N N   . SER A 1 34 ? 14.78806  31.23451 25.09706  1.000 38.48987  ? 31  SER A N   1 
ATOM   255  C CA  . SER A 1 34 ? 15.71153  30.14851 25.40683  1.000 44.70516  ? 31  SER A CA  1 
ATOM   256  C C   . SER A 1 34 ? 16.04658  30.10299 26.89191  1.000 53.05363  ? 31  SER A C   1 
ATOM   257  O O   . SER A 1 34 ? 16.09245  29.02099 27.48811  1.000 46.17690  ? 31  SER A O   1 
ATOM   258  C CB  . SER A 1 34 ? 16.98397  30.29665 24.58077  1.000 50.85381  ? 31  SER A CB  1 
ATOM   259  O OG  . SER A 1 34 ? 17.91612  29.27419 24.87797  1.000 63.50623  ? 31  SER A OG  1 
ATOM   260  N N   . GLU A 1 35 ? 16.28102  31.26542 27.50781  1.000 49.08290  ? 32  GLU A N   1 
ATOM   261  C CA  . GLU A 1 35 ? 16.60630  31.28489 28.92913  1.000 53.58400  ? 32  GLU A CA  1 
ATOM   262  C C   . GLU A 1 35 ? 15.43517  30.80071 29.77426  1.000 49.67418  ? 32  GLU A C   1 
ATOM   263  O O   . GLU A 1 35 ? 15.64630  30.23743 30.85323  1.000 46.85197  ? 32  GLU A O   1 
ATOM   264  C CB  . GLU A 1 35 ? 17.04470  32.69085 29.35218  1.000 59.83012  ? 32  GLU A CB  1 
ATOM   265  C CG  . GLU A 1 35 ? 15.95033  33.74666 29.30234  1.000 59.18544  ? 32  GLU A CG  1 
ATOM   266  C CD  . GLU A 1 35 ? 16.47247  35.15288 29.53564  1.000 72.83096  ? 32  GLU A CD  1 
ATOM   267  O OE1 . GLU A 1 35 ? 17.68599  35.37828 29.34958  1.000 72.09998  ? 32  GLU A OE1 1 
ATOM   268  O OE2 . GLU A 1 35 ? 15.66786  36.03408 29.90553  1.000 68.90286  ? 32  GLU A OE2 1 
ATOM   269  N N   . GLU A 1 36 ? 14.20114  30.99602 29.30040  1.000 48.94713  ? 33  GLU A N   1 
ATOM   270  C CA  . GLU A 1 36 ? 13.04516  30.47797 30.02406  1.000 51.93871  ? 33  GLU A CA  1 
ATOM   271  C C   . GLU A 1 36 ? 12.93790  28.96464 29.87089  1.000 55.97912  ? 33  GLU A C   1 
ATOM   272  O O   . GLU A 1 36 ? 12.56280  28.26321 30.81840  1.000 48.98132  ? 33  GLU A O   1 
ATOM   273  C CB  . GLU A 1 36 ? 11.76797  31.16881 29.53928  1.000 46.07361  ? 33  GLU A CB  1 
ATOM   274  C CG  . GLU A 1 36 ? 10.48480  30.62378 30.16472  1.000 63.12066  ? 33  GLU A CG  1 
ATOM   275  C CD  . GLU A 1 36 ? 9.27727   31.50570 29.89415  1.000 63.96012  ? 33  GLU A CD  1 
ATOM   276  O OE1 . GLU A 1 36 ? 9.46884   32.70713 29.60875  1.000 71.86475  ? 33  GLU A OE1 1 
ATOM   277  O OE2 . GLU A 1 36 ? 8.13611   31.00037 29.97154  1.000 63.66725  ? 33  GLU A OE2 1 
ATOM   278  N N   . MET A 1 37 ? 13.26631  28.44163 28.68566  1.000 42.10393  ? 34  MET A N   1 
ATOM   279  C CA  . MET A 1 37 ? 13.24295  26.99512 28.48599  1.000 48.03650  ? 34  MET A CA  1 
ATOM   280  C C   . MET A 1 37 ? 14.28710  26.30240 29.34952  1.000 50.48234  ? 34  MET A C   1 
ATOM   281  O O   . MET A 1 37 ? 14.01935  25.24425 29.93122  1.000 52.37416  ? 34  MET A O   1 
ATOM   282  C CB  . MET A 1 37 ? 13.47518  26.65698 27.01618  1.000 34.33284  ? 34  MET A CB  1 
ATOM   283  C CG  . MET A 1 37 ? 12.51920  27.32725 26.05847  1.000 42.74692  ? 34  MET A CG  1 
ATOM   284  S SD  . MET A 1 37 ? 12.70407  26.65747 24.40619  1.000 35.95725  ? 34  MET A SD  1 
ATOM   285  C CE  . MET A 1 37 ? 12.09855  25.00742 24.72071  1.000 51.52871  ? 34  MET A CE  1 
ATOM   286  N N   . GLU A 1 38 ? 15.48777  26.87862 29.43505  1.000 50.83847  ? 35  GLU A N   1 
ATOM   287  C CA  . GLU A 1 38 ? 16.51034  26.31414 30.30575  1.000 55.98213  ? 35  GLU A CA  1 
ATOM   288  C C   . GLU A 1 38 ? 16.15536  26.51625 31.77236  1.000 58.28161  ? 35  GLU A C   1 
ATOM   289  O O   . GLU A 1 38 ? 16.57296  25.72527 32.62530  1.000 65.43730  ? 35  GLU A O   1 
ATOM   290  C CB  . GLU A 1 38 ? 17.87199  26.92992 29.98109  1.000 55.86487  ? 35  GLU A CB  1 
ATOM   291  C CG  . GLU A 1 38 ? 19.05578  26.13619 30.51336  1.000 81.61416  ? 35  GLU A CG  1 
ATOM   292  C CD  . GLU A 1 38 ? 20.33159  26.39728 29.73388  1.000 82.16986  ? 35  GLU A CD  1 
ATOM   293  O OE1 . GLU A 1 38 ? 20.48118  27.50991 29.18591  1.000 78.40436  ? 35  GLU A OE1 1 
ATOM   294  O OE2 . GLU A 1 38 ? 21.18151  25.48449 29.66034  1.000 85.27468  ? 35  GLU A OE2 1 
ATOM   295  N N   . LYS A 1 39 ? 15.38365  27.56126 32.08062  1.000 62.37747  ? 36  LYS A N   1 
ATOM   296  C CA  . LYS A 1 39 ? 14.87223  27.73776 33.43579  1.000 65.31187  ? 36  LYS A CA  1 
ATOM   297  C C   . LYS A 1 39 ? 13.82519  26.68111 33.76323  1.000 59.95723  ? 36  LYS A C   1 
ATOM   298  O O   . LYS A 1 39 ? 13.86122  26.06563 34.83476  1.000 65.71177  ? 36  LYS A O   1 
ATOM   299  C CB  . LYS A 1 39 ? 14.28687  29.14224 33.59708  1.000 66.07101  ? 36  LYS A CB  1 
ATOM   300  C CG  . LYS A 1 39 ? 13.49655  29.34667 34.88237  1.000 72.68127  ? 36  LYS A CG  1 
ATOM   301  C CD  . LYS A 1 39 ? 12.76651  30.68268 34.88266  1.000 72.64468  ? 36  LYS A CD  1 
ATOM   302  C CE  . LYS A 1 39 ? 11.99181  30.89237 36.17623  1.000 71.89313  ? 36  LYS A CE  1 
ATOM   303  N NZ  . LYS A 1 39 ? 11.01502  29.79610 36.42992  1.000 76.43323  ? 36  LYS A NZ  1 
ATOM   304  N N   . LYS A 1 40 ? 12.88576  26.45206 32.84528  1.000 63.64600  ? 37  LYS A N   1 
ATOM   305  C CA  . LYS A 1 40 ? 11.82515  25.47304 33.05373  1.000 52.21916  ? 37  LYS A CA  1 
ATOM   306  C C   . LYS A 1 40 ? 12.30736  24.03403 32.92020  1.000 53.82711  ? 37  LYS A C   1 
ATOM   307  O O   . LYS A 1 40 ? 11.48230  23.11673 33.00225  1.000 62.76265  ? 37  LYS A O   1 
ATOM   308  C CB  . LYS A 1 40 ? 10.67434  25.72946 32.07585  1.000 62.90966  ? 37  LYS A CB  1 
ATOM   309  C CG  . LYS A 1 40 ? 9.59123   26.67336 32.59927  1.000 67.00807  ? 37  LYS A CG  1 
ATOM   310  C CD  . LYS A 1 40 ? 10.13153  28.06465 32.90014  1.000 61.53791  ? 37  LYS A CD  1 
ATOM   311  C CE  . LYS A 1 40 ? 9.04341   28.98252 33.43572  1.000 68.45669  ? 37  LYS A CE  1 
ATOM   312  N NZ  . LYS A 1 40 ? 7.94642   29.18080 32.44850  1.000 67.25145  ? 37  LYS A NZ  1 
ATOM   313  N N   . GLY A 1 41 ? 13.60414  23.81335 32.71773  1.000 52.65334  ? 38  GLY A N   1 
ATOM   314  C CA  . GLY A 1 41 ? 14.13905  22.46614 32.66549  1.000 50.85304  ? 38  GLY A CA  1 
ATOM   315  C C   . GLY A 1 41 ? 13.68695  21.64183 31.48166  1.000 55.56894  ? 38  GLY A C   1 
ATOM   316  O O   . GLY A 1 41 ? 13.59548  20.41481 31.59070  1.000 51.47778  ? 38  GLY A O   1 
ATOM   317  N N   . LEU A 1 42 ? 13.40251  22.27782 30.34968  1.000 40.78633  ? 39  LEU A N   1 
ATOM   318  C CA  . LEU A 1 42 ? 12.99461  21.54073 29.16495  1.000 46.19129  ? 39  LEU A CA  1 
ATOM   319  C C   . LEU A 1 42 ? 14.20085  20.87149 28.51252  1.000 40.97433  ? 39  LEU A C   1 
ATOM   320  O O   . LEU A 1 42 ? 15.32657  21.37615 28.56579  1.000 47.89561  ? 39  LEU A O   1 
ATOM   321  C CB  . LEU A 1 42 ? 12.29155  22.46846 28.17277  1.000 45.62873  ? 39  LEU A CB  1 
ATOM   322  C CG  . LEU A 1 42 ? 11.02607  23.14453 28.71264  1.000 52.32363  ? 39  LEU A CG  1 
ATOM   323  C CD1 . LEU A 1 42 ? 10.31457  23.93298 27.62595  1.000 48.73566  ? 39  LEU A CD1 1 
ATOM   324  C CD2 . LEU A 1 42 ? 10.08746  22.11860 29.33055  1.000 51.96129  ? 39  LEU A CD2 1 
ATOM   325  N N   . SER A 1 43 ? 13.95573  19.71529 27.90294  1.000 44.30069  ? 40  SER A N   1 
ATOM   326  C CA  . SER A 1 43 ? 15.03314  18.93666 27.31298  1.000 48.59038  ? 40  SER A CA  1 
ATOM   327  C C   . SER A 1 43 ? 15.53628  19.59269 26.02985  1.000 42.16669  ? 40  SER A C   1 
ATOM   328  O O   . SER A 1 43 ? 14.91336  20.50369 25.47803  1.000 34.46128  ? 40  SER A O   1 
ATOM   329  C CB  . SER A 1 43 ? 14.56640  17.51080 27.01699  1.000 47.61582  ? 40  SER A CB  1 
ATOM   330  O OG  . SER A 1 43 ? 13.54761  17.50206 26.03160  1.000 42.30106  ? 40  SER A OG  1 
ATOM   331  N N   . LYS A 1 44 ? 16.69132  19.11204 25.55958  1.000 38.28127  ? 41  LYS A N   1 
ATOM   332  C CA  . LYS A 1 44 ? 17.22671  19.57391 24.28230  1.000 44.90597  ? 41  LYS A CA  1 
ATOM   333  C C   . LYS A 1 44 ? 16.25294  19.30065 23.14535  1.000 36.62031  ? 41  LYS A C   1 
ATOM   334  O O   . LYS A 1 44 ? 16.10771  20.12205 22.23192  1.000 35.62403  ? 41  LYS A O   1 
ATOM   335  C CB  . LYS A 1 44 ? 18.56694  18.89774 23.99476  1.000 37.76139  ? 41  LYS A CB  1 
ATOM   336  C CG  . LYS A 1 44 ? 19.78821  19.74222 24.31298  1.000 63.94370  ? 41  LYS A CG  1 
ATOM   337  C CD  . LYS A 1 44 ? 21.06095  19.03557 23.87056  1.000 50.89430  ? 41  LYS A CD  1 
ATOM   338  C CE  . LYS A 1 44 ? 22.29749  19.86775 24.17107  1.000 73.03702  ? 41  LYS A CE  1 
ATOM   339  N NZ  . LYS A 1 44 ? 22.27835  21.17297 23.45668  1.000 74.90899  ? 41  LYS A NZ  1 
ATOM   340  N N   . GLU A 1 45 ? 15.58695  18.14203 23.17933  1.000 47.42316  ? 42  GLU A N   1 
ATOM   341  C CA  . GLU A 1 45 ? 14.63659  17.79438 22.12732  1.000 41.55265  ? 42  GLU A CA  1 
ATOM   342  C C   . GLU A 1 45 ? 13.44343  18.73972 22.13176  1.000 30.46272  ? 42  GLU A C   1 
ATOM   343  O O   . GLU A 1 45 ? 12.94578  19.13041 21.06952  1.000 32.21555  ? 42  GLU A O   1 
ATOM   344  C CB  . GLU A 1 45 ? 14.17535  16.34459 22.29073  1.000 31.39413  ? 42  GLU A CB  1 
ATOM   345  C CG  . GLU A 1 45 ? 15.23992  15.29950 21.96807  1.000 44.68115  ? 42  GLU A CG  1 
ATOM   346  C CD  . GLU A 1 45 ? 16.26688  15.12568 23.07649  1.000 50.98143  ? 42  GLU A CD  1 
ATOM   347  O OE1 . GLU A 1 45 ? 15.95121  15.43159 24.24569  1.000 54.82421  ? 42  GLU A OE1 1 
ATOM   348  O OE2 . GLU A 1 45 ? 17.39422  14.68113 22.77726  1.000 45.51786  ? 42  GLU A OE2 1 
ATOM   349  N N   . GLN A 1 46 ? 12.96989  19.11938 23.31934  1.000 37.93883  ? 43  GLN A N   1 
ATOM   350  C CA  . GLN A 1 46 ? 11.89716  20.10292 23.39682  1.000 35.21843  ? 43  GLN A CA  1 
ATOM   351  C C   . GLN A 1 46 ? 12.36531  21.47653 22.94097  1.000 27.33940  ? 43  GLN A C   1 
ATOM   352  O O   . GLN A 1 46 ? 11.58616  22.22495 22.34058  1.000 26.79254  ? 43  GLN A O   1 
ATOM   353  C CB  . GLN A 1 46 ? 11.35316  20.18071 24.82095  1.000 32.20124  ? 43  GLN A CB  1 
ATOM   354  C CG  . GLN A 1 46 ? 10.55868  18.96528 25.25254  1.000 30.34487  ? 43  GLN A CG  1 
ATOM   355  C CD  . GLN A 1 46 ? 10.04282  19.09957 26.66656  1.000 43.17898  ? 43  GLN A CD  1 
ATOM   356  O OE1 . GLN A 1 46 ? 10.81080  19.34631 27.59517  1.000 49.29928  ? 43  GLN A OE1 1 
ATOM   357  N NE2 . GLN A 1 46 ? 8.73368   18.95516 26.83786  1.000 39.03588  ? 43  GLN A NE2 1 
ATOM   358  N N   . VAL A 1 47 ? 13.62543  21.82314 23.21344  1.000 28.60164  ? 44  VAL A N   1 
ATOM   359  C CA  . VAL A 1 47 ? 14.13941  23.12828 22.80922  1.000 31.80472  ? 44  VAL A CA  1 
ATOM   360  C C   . VAL A 1 47 ? 14.18432  23.23429 21.29275  1.000 33.53397  ? 44  VAL A C   1 
ATOM   361  O O   . VAL A 1 47 ? 13.70538  24.21475 20.71090  1.000 36.03546  ? 44  VAL A O   1 
ATOM   362  C CB  . VAL A 1 47 ? 15.51886  23.39250 23.43949  1.000 42.92947  ? 44  VAL A CB  1 
ATOM   363  C CG1 . VAL A 1 47 ? 16.14086  24.64810 22.84124  1.000 29.52945  ? 44  VAL A CG1 1 
ATOM   364  C CG2 . VAL A 1 47 ? 15.38985  23.54550 24.94393  1.000 43.97117  ? 44  VAL A CG2 1 
ATOM   365  N N   . ILE A 1 48 ? 14.74844  22.22184 20.62947  1.000 36.71667  ? 45  ILE A N   1 
ATOM   366  C CA  . ILE A 1 48 ? 14.80812  22.23436 19.17053  1.000 36.41515  ? 45  ILE A CA  1 
ATOM   367  C C   . ILE A 1 48 ? 13.40761  22.32696 18.58198  1.000 38.21041  ? 45  ILE A C   1 
ATOM   368  O O   . ILE A 1 48 ? 13.15151  23.13125 17.67786  1.000 39.33542  ? 45  ILE A O   1 
ATOM   369  C CB  . ILE A 1 48 ? 15.55536  20.99417 18.64798  1.000 42.13874  ? 45  ILE A CB  1 
ATOM   370  C CG1 . ILE A 1 48 ? 17.01866  21.02216 19.08676  1.000 51.58295  ? 45  ILE A CG1 1 
ATOM   371  C CG2 . ILE A 1 48 ? 15.46139  20.91971 17.13183  1.000 43.03234  ? 45  ILE A CG2 1 
ATOM   372  C CD1 . ILE A 1 48 ? 17.83702  19.88693 18.51486  1.000 52.71627  ? 45  ILE A CD1 1 
ATOM   373  N N   . LEU A 1 49 ? 12.47972  21.50834 19.08791  1.000 30.74248  ? 46  LEU A N   1 
ATOM   374  C CA  . LEU A 1 49 ? 11.09915  21.56682 18.61891  1.000 34.58910  ? 46  LEU A CA  1 
ATOM   375  C C   . LEU A 1 49 ? 10.52211  22.96621 18.76705  1.000 26.17725  ? 46  LEU A C   1 
ATOM   376  O O   . LEU A 1 49 ? 9.92978   23.50469 17.82479  1.000 28.24620  ? 46  LEU A O   1 
ATOM   377  C CB  . LEU A 1 49 ? 10.24306  20.55974 19.38268  1.000 36.44930  ? 46  LEU A CB  1 
ATOM   378  C CG  . LEU A 1 49 ? 10.38840  19.11700 18.91967  1.000 32.15425  ? 46  LEU A CG  1 
ATOM   379  C CD1 . LEU A 1 49 ? 9.52732   18.20074 19.76583  1.000 31.27690  ? 46  LEU A CD1 1 
ATOM   380  C CD2 . LEU A 1 49 ? 10.00770  19.02482 17.45406  1.000 22.55604  ? 46  LEU A CD2 1 
ATOM   381  N N   . LEU A 1 50 ? 10.69190  23.57530 19.94076  1.000 29.58961  ? 47  LEU A N   1 
ATOM   382  C CA  . LEU A 1 50 ? 10.12428  24.89702 20.17110  1.000 31.68763  ? 47  LEU A CA  1 
ATOM   383  C C   . LEU A 1 50 ? 10.86428  25.98537 19.40659  1.000 31.85080  ? 47  LEU A C   1 
ATOM   384  O O   . LEU A 1 50 ? 10.24567  26.96850 18.98827  1.000 34.39397  ? 47  LEU A O   1 
ATOM   385  C CB  . LEU A 1 50 ? 10.11268  25.21069 21.66473  1.000 28.15771  ? 47  LEU A CB  1 
ATOM   386  C CG  . LEU A 1 50 ? 8.72059   25.03262 22.26425  1.000 46.31621  ? 47  LEU A CG  1 
ATOM   387  C CD1 . LEU A 1 50 ? 8.29500   23.57928 22.16089  1.000 38.17164  ? 47  LEU A CD1 1 
ATOM   388  C CD2 . LEU A 1 50 ? 8.67349   25.51832 23.69962  1.000 51.01731  ? 47  LEU A CD2 1 
ATOM   389  N N   . LEU A 1 51 ? 12.17335  25.83393 19.20532  1.000 32.03185  ? 48  LEU A N   1 
ATOM   390  C CA  . LEU A 1 51 ? 12.89701  26.82133 18.41509  1.000 29.64970  ? 48  LEU A CA  1 
ATOM   391  C C   . LEU A 1 51 ? 12.49704  26.74203 16.94837  1.000 38.55317  ? 48  LEU A C   1 
ATOM   392  O O   . LEU A 1 51 ? 12.40268  27.76972 16.26758  1.000 29.60405  ? 48  LEU A O   1 
ATOM   393  C CB  . LEU A 1 51 ? 14.40305  26.63370 18.58894  1.000 33.84505  ? 48  LEU A CB  1 
ATOM   394  C CG  . LEU A 1 51 ? 14.90807  27.13492 19.94307  1.000 28.10876  ? 48  LEU A CG  1 
ATOM   395  C CD1 . LEU A 1 51 ? 16.41833  27.04447 20.03338  1.000 40.75304  ? 48  LEU A CD1 1 
ATOM   396  C CD2 . LEU A 1 51 ? 14.44161  28.56266 20.19199  1.000 38.74680  ? 48  LEU A CD2 1 
ATOM   397  N N   . ILE A 1 52 ? 12.24121  25.53151 16.44641  1.000 31.64850  ? 49  ILE A N   1 
ATOM   398  C CA  . ILE A 1 52 ? 11.73216  25.39784 15.08473  1.000 31.93997  ? 49  ILE A CA  1 
ATOM   399  C C   . ILE A 1 52 ? 10.29669  25.90064 15.00787  1.000 39.18185  ? 49  ILE A C   1 
ATOM   400  O O   . ILE A 1 52 ? 9.89631   26.54133 14.02669  1.000 32.07390  ? 49  ILE A O   1 
ATOM   401  C CB  . ILE A 1 52 ? 11.85267  23.94000 14.60824  1.000 36.70199  ? 49  ILE A CB  1 
ATOM   402  C CG1 . ILE A 1 52 ? 13.31878  23.51452 14.59392  1.000 37.21353  ? 49  ILE A CG1 1 
ATOM   403  C CG2 . ILE A 1 52 ? 11.24595  23.78276 13.22650  1.000 44.57437  ? 49  ILE A CG2 1 
ATOM   404  C CD1 . ILE A 1 52 ? 13.52396  22.04866 14.28285  1.000 43.51683  ? 49  ILE A CD1 1 
ATOM   405  N N   . HIS A 1 53 ? 9.50615   25.62986 16.04778  1.000 31.86372  ? 50  HIS A N   1 
ATOM   406  C CA  . HIS A 1 53 ? 8.17350   26.21245 16.14911  1.000 39.11302  ? 50  HIS A CA  1 
ATOM   407  C C   . HIS A 1 53 ? 8.23777   27.73435 16.11295  1.000 38.30248  ? 50  HIS A C   1 
ATOM   408  O O   . HIS A 1 53 ? 7.42735   28.38099 15.43901  1.000 40.10062  ? 50  HIS A O   1 
ATOM   409  C CB  . HIS A 1 53 ? 7.50105   25.71949 17.43011  1.000 44.35897  ? 50  HIS A CB  1 
ATOM   410  C CG  . HIS A 1 53 ? 6.20991   26.40594 17.75086  1.000 55.43975  ? 50  HIS A CG  1 
ATOM   411  N ND1 . HIS A 1 53 ? 6.03739   27.16587 18.88753  1.000 62.21076  ? 50  HIS A ND1 1 
ATOM   412  C CD2 . HIS A 1 53 ? 5.02519   26.43611 17.09550  1.000 54.66527  ? 50  HIS A CD2 1 
ATOM   413  C CE1 . HIS A 1 53 ? 4.80441   27.63927 18.91616  1.000 60.91162  ? 50  HIS A CE1 1 
ATOM   414  N NE2 . HIS A 1 53 ? 4.16876   27.20979 17.84110  1.000 59.52326  ? 50  HIS A NE2 1 
ATOM   415  N N   . PHE A 1 54 ? 9.20658   28.32536 16.81769  1.000 33.14670  ? 51  PHE A N   1 
ATOM   416  C CA  . PHE A 1 54 ? 9.37671   29.77339 16.75092  1.000 42.37326  ? 51  PHE A CA  1 
ATOM   417  C C   . PHE A 1 54 ? 9.72663   30.22012 15.33805  1.000 34.89420  ? 51  PHE A C   1 
ATOM   418  O O   . PHE A 1 54 ? 9.21954   31.24164 14.86008  1.000 38.20216  ? 51  PHE A O   1 
ATOM   419  C CB  . PHE A 1 54 ? 10.45216  30.23596 17.73662  1.000 35.66461  ? 51  PHE A CB  1 
ATOM   420  C CG  . PHE A 1 54 ? 10.86055  31.67329 17.55098  1.000 40.69155  ? 51  PHE A CG  1 
ATOM   421  C CD1 . PHE A 1 54 ? 10.14717  32.69533 18.15703  1.000 41.57593  ? 51  PHE A CD1 1 
ATOM   422  C CD2 . PHE A 1 54 ? 11.95131  32.00353 16.75971  1.000 44.47701  ? 51  PHE A CD2 1 
ATOM   423  C CE1 . PHE A 1 54 ? 10.51641  34.01706 17.97949  1.000 41.67639  ? 51  PHE A CE1 1 
ATOM   424  C CE2 . PHE A 1 54 ? 12.31952  33.32329 16.57312  1.000 47.67218  ? 51  PHE A CE2 1 
ATOM   425  C CZ  . PHE A 1 54 ? 11.60726  34.33123 17.18874  1.000 42.34275  ? 51  PHE A CZ  1 
ATOM   426  N N   . LEU A 1 55 ? 10.59727  29.47005 14.65521  1.000 26.70383  ? 52  LEU A N   1 
ATOM   427  C CA  . LEU A 1 55 ? 10.98519  29.83902 13.29802  1.000 31.54062  ? 52  LEU A CA  1 
ATOM   428  C C   . LEU A 1 55 ? 9.78514   29.84333 12.36057  1.000 35.24477  ? 52  LEU A C   1 
ATOM   429  O O   . LEU A 1 55 ? 9.67349   30.71261 11.48910  1.000 33.50770  ? 52  LEU A O   1 
ATOM   430  C CB  . LEU A 1 55 ? 12.07031  28.89196 12.78438  1.000 28.51041  ? 52  LEU A CB  1 
ATOM   431  C CG  . LEU A 1 55 ? 13.45849  29.05118 13.40938  1.000 30.31834  ? 52  LEU A CG  1 
ATOM   432  C CD1 . LEU A 1 55 ? 14.43410  28.04202 12.82560  1.000 36.04145  ? 52  LEU A CD1 1 
ATOM   433  C CD2 . LEU A 1 55 ? 13.98286  30.47041 13.22674  1.000 21.80464  ? 52  LEU A CD2 1 
ATOM   434  N N   . LEU A 1 56 ? 8.86976   28.88793 12.53098  1.000 36.86957  ? 53  LEU A N   1 
ATOM   435  C CA  . LEU A 1 56 ? 7.70040   28.81828 11.66320  1.000 35.59632  ? 53  LEU A CA  1 
ATOM   436  C C   . LEU A 1 56 ? 6.66372   29.88086 12.00578  1.000 39.07178  ? 53  LEU A C   1 
ATOM   437  O O   . LEU A 1 56 ? 5.96374   30.36491 11.11108  1.000 43.08275  ? 53  LEU A O   1 
ATOM   438  C CB  . LEU A 1 56 ? 7.07461   27.42598 11.73733  1.000 42.34174  ? 53  LEU A CB  1 
ATOM   439  C CG  . LEU A 1 56 ? 7.98703   26.26971 11.33874  1.000 35.99428  ? 53  LEU A CG  1 
ATOM   440  C CD1 . LEU A 1 56 ? 7.23247   24.96227 11.40058  1.000 51.05289  ? 53  LEU A CD1 1 
ATOM   441  C CD2 . LEU A 1 56 ? 8.55324   26.49082 9.95031   1.000 46.27631  ? 53  LEU A CD2 1 
ATOM   442  N N   . LEU A 1 57 ? 6.53709   30.24439 13.28250  1.000 37.19756  ? 54  LEU A N   1 
ATOM   443  C CA  . LEU A 1 57 ? 5.66770   31.35533 13.65184  1.000 48.95302  ? 54  LEU A CA  1 
ATOM   444  C C   . LEU A 1 57 ? 6.16314   32.65424 13.03696  1.000 35.97068  ? 54  LEU A C   1 
ATOM   445  O O   . LEU A 1 57 ? 5.39352   33.39978 12.42459  1.000 44.35039  ? 54  LEU A O   1 
ATOM   446  C CB  . LEU A 1 57 ? 5.60055   31.48795 15.17238  1.000 48.76124  ? 54  LEU A CB  1 
ATOM   447  C CG  . LEU A 1 57 ? 4.90027   30.40727 15.99380  1.000 55.98545  ? 54  LEU A CG  1 
ATOM   448  C CD1 . LEU A 1 57 ? 5.17956   30.65051 17.46626  1.000 54.16848  ? 54  LEU A CD1 1 
ATOM   449  C CD2 . LEU A 1 57 ? 3.40684   30.40762 15.72182  1.000 52.15215  ? 54  LEU A CD2 1 
ATOM   450  N N   . SER A 1 58 ? 7.45583   32.93448 13.19418  1.000 33.97952  ? 55  SER A N   1 
ATOM   451  C CA  . SER A 1 58 ? 8.02214   34.20153 12.75130  1.000 43.94445  ? 55  SER A CA  1 
ATOM   452  C C   . SER A 1 58 ? 8.18535   34.25526 11.23634  1.000 41.42255  ? 55  SER A C   1 
ATOM   453  O O   . SER A 1 58 ? 7.69136   35.18263 10.58406  1.000 50.49040  ? 55  SER A O   1 
ATOM   454  C CB  . SER A 1 58 ? 9.36520   34.42430 13.44527  1.000 38.91121  ? 55  SER A CB  1 
ATOM   455  O OG  . SER A 1 58 ? 10.19752  33.28680 13.30230  1.000 43.36595  ? 55  SER A OG  1 
ATOM   456  N N   . LEU A 1 59 ? 8.86729   33.26737 10.65937  1.000 33.39479  ? 56  LEU A N   1 
ATOM   457  C CA  . LEU A 1 59 ? 9.29072   33.35273 9.26787   1.000 38.07529  ? 56  LEU A CA  1 
ATOM   458  C C   . LEU A 1 59 ? 8.24644   32.84754 8.28520   1.000 34.82982  ? 56  LEU A C   1 
ATOM   459  O O   . LEU A 1 59 ? 8.19770   33.32584 7.14527   1.000 43.58020  ? 56  LEU A O   1 
ATOM   460  C CB  . LEU A 1 59 ? 10.59283  32.57524 9.07187   1.000 31.24766  ? 56  LEU A CB  1 
ATOM   461  C CG  . LEU A 1 59 ? 11.73066  33.03570 9.98131   1.000 37.06911  ? 56  LEU A CG  1 
ATOM   462  C CD1 . LEU A 1 59 ? 13.00325  32.25535 9.68921   1.000 38.62446  ? 56  LEU A CD1 1 
ATOM   463  C CD2 . LEU A 1 59 ? 11.96500  34.53480 9.83799   1.000 37.72496  ? 56  LEU A CD2 1 
ATOM   464  N N   . VAL A 1 60 ? 7.41615   31.89490 8.68680   1.000 41.39451  ? 57  VAL A N   1 
ATOM   465  C CA  . VAL A 1 60 ? 6.40867   31.32395 7.80333   1.000 41.68499  ? 57  VAL A CA  1 
ATOM   466  C C   . VAL A 1 60 ? 5.04778   31.96440 8.02853   1.000 45.35683  ? 57  VAL A C   1 
ATOM   467  O O   . VAL A 1 60 ? 4.41810   32.45025 7.08792   1.000 50.84843  ? 57  VAL A O   1 
ATOM   468  C CB  . VAL A 1 60 ? 6.34822   29.79111 7.98351   1.000 54.66632  ? 57  VAL A CB  1 
ATOM   469  C CG1 . VAL A 1 60 ? 5.21072   29.20598 7.16720   1.000 62.83616  ? 57  VAL A CG1 1 
ATOM   470  C CG2 . VAL A 1 60 ? 7.67794   29.16619 7.59248   1.000 37.89673  ? 57  VAL A CG2 1 
ATOM   471  N N   . LYS A 1 61 ? 4.58186   31.98352 9.27933   1.000 46.50621  ? 58  LYS A N   1 
ATOM   472  C CA  . LYS A 1 61 ? 3.29022   32.58239 9.58793   1.000 50.86113  ? 58  LYS A CA  1 
ATOM   473  C C   . LYS A 1 61 ? 3.33401   34.10283 9.64902   1.000 45.64992  ? 58  LYS A C   1 
ATOM   474  O O   . LYS A 1 61 ? 2.27039   34.73180 9.65707   1.000 57.54989  ? 58  LYS A O   1 
ATOM   475  C CB  . LYS A 1 61 ? 2.74625   32.03444 10.90808  1.000 53.38073  ? 58  LYS A CB  1 
ATOM   476  C CG  . LYS A 1 61 ? 1.56198   31.10192 10.72741  1.000 62.76496  ? 58  LYS A CG  1 
ATOM   477  C CD  . LYS A 1 61 ? 0.78727   30.92373 12.01526  1.000 60.91416  ? 58  LYS A CD  1 
ATOM   478  C CE  . LYS A 1 61 ? -0.44572  30.07470 11.78108  1.000 66.12893  ? 58  LYS A CE  1 
ATOM   479  N NZ  . LYS A 1 61 ? -1.21775  30.55332 10.60117  1.000 54.37434  ? 58  LYS A NZ  1 
ATOM   480  N N   . GLY A 1 62 ? 4.51974   34.70304 9.68667   1.000 49.77768  ? 59  GLY A N   1 
ATOM   481  C CA  . GLY A 1 62 ? 4.63154   36.15275 9.65516   1.000 43.26760  ? 59  GLY A CA  1 
ATOM   482  C C   . GLY A 1 62 ? 4.14845   36.84448 10.91043  1.000 44.98777  ? 59  GLY A C   1 
ATOM   483  O O   . GLY A 1 62 ? 3.48073   37.88319 10.82422  1.000 61.68343  ? 59  GLY A O   1 
ATOM   484  N N   . LEU A 1 63 ? 4.46917   36.29608 12.07600  1.000 45.01819  ? 60  LEU A N   1 
ATOM   485  C CA  . LEU A 1 63 ? 4.04663   36.85746 13.35004  1.000 43.13099  ? 60  LEU A CA  1 
ATOM   486  C C   . LEU A 1 63 ? 5.14910   37.73729 13.92325  1.000 42.92013  ? 60  LEU A C   1 
ATOM   487  O O   . LEU A 1 63 ? 6.32969   37.37777 13.88214  1.000 45.44916  ? 60  LEU A O   1 
ATOM   488  C CB  . LEU A 1 63 ? 3.68979   35.74816 14.34089  1.000 38.24191  ? 60  LEU A CB  1 
ATOM   489  C CG  . LEU A 1 63 ? 2.26434   35.18863 14.32833  1.000 51.37951  ? 60  LEU A CG  1 
ATOM   490  C CD1 . LEU A 1 63 ? 1.76565   34.92084 12.91855  1.000 63.04432  ? 60  LEU A CD1 1 
ATOM   491  C CD2 . LEU A 1 63 ? 2.20590   33.91893 15.15484  1.000 42.85831  ? 60  LEU A CD2 1 
ATOM   492  N N   . SER A 1 64 ? 4.75272   38.89203 14.46154  1.000 39.51206  ? 61  SER A N   1 
ATOM   493  C CA  . SER A 1 64 ? 5.70778   39.84668 14.99929  1.000 51.39448  ? 61  SER A CA  1 
ATOM   494  C C   . SER A 1 64 ? 6.51919   39.21809 16.13201  1.000 44.02017  ? 61  SER A C   1 
ATOM   495  O O   . SER A 1 64 ? 6.08316   38.24857 16.75553  1.000 37.86864  ? 61  SER A O   1 
ATOM   496  C CB  . SER A 1 64 ? 4.97890   41.09256 15.49904  1.000 53.77682  ? 61  SER A CB  1 
ATOM   497  O OG  . SER A 1 64 ? 4.02939   40.75838 16.49561  1.000 49.68229  ? 61  SER A OG  1 
ATOM   498  N N   . PRO A 1 65 ? 7.72012   39.74575 16.39952  1.000 45.59682  ? 62  PRO A N   1 
ATOM   499  C CA  . PRO A 1 65 ? 8.51635   39.20753 17.51754  1.000 44.58624  ? 62  PRO A CA  1 
ATOM   500  C C   . PRO A 1 65 ? 7.78480   39.23833 18.84718  1.000 42.55177  ? 62  PRO A C   1 
ATOM   501  O O   . PRO A 1 65 ? 7.92657   38.30678 19.64923  1.000 43.44744  ? 62  PRO A O   1 
ATOM   502  C CB  . PRO A 1 65 ? 9.75535   40.11391 17.52790  1.000 43.96075  ? 62  PRO A CB  1 
ATOM   503  C CG  . PRO A 1 65 ? 9.85665   40.63435 16.13734  1.000 51.31191  ? 62  PRO A CG  1 
ATOM   504  C CD  . PRO A 1 65 ? 8.44793   40.78283 15.64857  1.000 45.08305  ? 62  PRO A CD  1 
ATOM   505  N N   . GLU A 1 66 ? 7.00468   40.29087 19.10397  1.000 48.56134  ? 63  GLU A N   1 
ATOM   506  C CA  . GLU A 1 66 ? 6.21610   40.34732 20.33001  1.000 58.09430  ? 63  GLU A CA  1 
ATOM   507  C C   . GLU A 1 66 ? 5.14502   39.26494 20.34042  1.000 50.48167  ? 63  GLU A C   1 
ATOM   508  O O   . GLU A 1 66 ? 4.91952   38.61278 21.36644  1.000 41.99514  ? 63  GLU A O   1 
ATOM   509  C CB  . GLU A 1 66 ? 5.58343   41.73088 20.48198  1.000 57.34810  ? 63  GLU A CB  1 
ATOM   510  C CG  . GLU A 1 66 ? 4.79499   41.92235 21.76758  1.000 79.12452  ? 63  GLU A CG  1 
ATOM   511  C CD  . GLU A 1 66 ? 5.68717   42.06343 22.98529  1.000 82.46257  ? 63  GLU A CD  1 
ATOM   512  O OE1 . GLU A 1 66 ? 6.88415   42.37873 22.81564  1.000 86.74701  ? 63  GLU A OE1 1 
ATOM   513  O OE2 . GLU A 1 66 ? 5.19189   41.85875 24.11324  1.000 81.79353  ? 63  GLU A OE2 1 
ATOM   514  N N   . THR A 1 67 ? 4.47681   39.05797 19.20378  1.000 40.40730  ? 64  THR A N   1 
ATOM   515  C CA  . THR A 1 67 ? 3.47132   38.00401 19.11508  1.000 42.92197  ? 64  THR A CA  1 
ATOM   516  C C   . THR A 1 67 ? 4.08904   36.63347 19.36425  1.000 42.75370  ? 64  THR A C   1 
ATOM   517  O O   . THR A 1 67 ? 3.60676   35.86774 20.20847  1.000 35.53490  ? 64  THR A O   1 
ATOM   518  C CB  . THR A 1 67 ? 2.78715   38.04290 17.74794  1.000 47.53355  ? 64  THR A CB  1 
ATOM   519  O OG1 . THR A 1 67 ? 1.99012   39.22763 17.64241  1.000 59.60978  ? 64  THR A OG1 1 
ATOM   520  C CG2 . THR A 1 67 ? 1.90020   36.82147 17.56437  1.000 51.95768  ? 64  THR A CG2 1 
ATOM   521  N N   . THR A 1 68 ? 5.16828   36.30859 18.64111  1.000 35.57323  ? 65  THR A N   1 
ATOM   522  C CA  . THR A 1 68 ? 5.80389   35.00377 18.80768  1.000 32.66346  ? 65  THR A CA  1 
ATOM   523  C C   . THR A 1 68 ? 6.27925   34.79927 20.23940  1.000 30.39401  ? 65  THR A C   1 
ATOM   524  O O   . THR A 1 68 ? 6.12349   33.70920 20.80113  1.000 32.91737  ? 65  THR A O   1 
ATOM   525  C CB  . THR A 1 68 ? 6.97719   34.84754 17.83887  1.000 33.33804  ? 65  THR A CB  1 
ATOM   526  O OG1 . THR A 1 68 ? 7.98722   35.81418 18.14912  1.000 42.66294  ? 65  THR A OG1 1 
ATOM   527  C CG2 . THR A 1 68 ? 6.52021   35.04145 16.40470  1.000 37.56949  ? 65  THR A CG2 1 
ATOM   528  N N   . LYS A 1 69 ? 6.85885   35.83735 20.84785  1.000 29.28643  ? 66  LYS A N   1 
ATOM   529  C CA  . LYS A 1 69 ? 7.31989   35.71597 22.22771  1.000 33.82240  ? 66  LYS A CA  1 
ATOM   530  C C   . LYS A 1 69 ? 6.17751   35.33450 23.15953  1.000 36.33091  ? 66  LYS A C   1 
ATOM   531  O O   . LYS A 1 69 ? 6.33557   34.46369 24.02367  1.000 34.64005  ? 66  LYS A O   1 
ATOM   532  C CB  . LYS A 1 69 ? 7.96813   37.02102 22.68364  1.000 40.06620  ? 66  LYS A CB  1 
ATOM   533  C CG  . LYS A 1 69 ? 8.24599   37.07670 24.17817  1.000 47.86041  ? 66  LYS A CG  1 
ATOM   534  C CD  . LYS A 1 69 ? 8.68640   38.46204 24.60530  1.000 47.07641  ? 66  LYS A CD  1 
ATOM   535  C CE  . LYS A 1 69 ? 7.71490   39.51047 24.09832  1.000 56.92484  ? 66  LYS A CE  1 
ATOM   536  N NZ  . LYS A 1 69 ? 6.31363   39.22216 24.51393  1.000 73.88507  ? 66  LYS A NZ  1 
ATOM   537  N N   . LEU A 1 70 ? 5.01690   35.97348 22.99613  1.000 42.59562  ? 67  LEU A N   1 
ATOM   538  C CA  . LEU A 1 70 ? 3.85644   35.61673 23.80477  1.000 37.07018  ? 67  LEU A CA  1 
ATOM   539  C C   . LEU A 1 70 ? 3.45689   34.16153 23.58575  1.000 38.53124  ? 67  LEU A C   1 
ATOM   540  O O   . LEU A 1 70 ? 3.21817   33.42390 24.54910  1.000 35.06290  ? 67  LEU A O   1 
ATOM   541  C CB  . LEU A 1 70 ? 2.69423   36.55639 23.48647  1.000 42.15148  ? 67  LEU A CB  1 
ATOM   542  C CG  . LEU A 1 70 ? 2.89156   38.00392 23.94497  1.000 59.68538  ? 67  LEU A CG  1 
ATOM   543  C CD1 . LEU A 1 70 ? 1.73541   38.88744 23.49779  1.000 60.60649  ? 67  LEU A CD1 1 
ATOM   544  C CD2 . LEU A 1 70 ? 3.05919   38.05908 25.45719  1.000 59.11635  ? 67  LEU A CD2 1 
ATOM   545  N N   . LEU A 1 71 ? 3.40220   33.72306 22.32569  1.000 34.60007  ? 68  LEU A N   1 
ATOM   546  C CA  . LEU A 1 71 ? 2.99330   32.35094 22.04006  1.000 37.33288  ? 68  LEU A CA  1 
ATOM   547  C C   . LEU A 1 71 ? 4.00995   31.34628 22.56614  1.000 31.35274  ? 68  LEU A C   1 
ATOM   548  O O   . LEU A 1 71 ? 3.63336   30.30370 23.11452  1.000 33.54427  ? 68  LEU A O   1 
ATOM   549  C CB  . LEU A 1 71 ? 2.78354   32.16966 20.53889  1.000 33.88749  ? 68  LEU A CB  1 
ATOM   550  C CG  . LEU A 1 71 ? 1.67182   33.03634 19.94302  1.000 39.60930  ? 68  LEU A CG  1 
ATOM   551  C CD1 . LEU A 1 71 ? 1.54518   32.77739 18.45508  1.000 43.99587  ? 68  LEU A CD1 1 
ATOM   552  C CD2 . LEU A 1 71 ? 0.33552   32.81405 20.65843  1.000 54.75837  ? 68  LEU A CD2 1 
ATOM   553  N N   . MET A 1 72 ? 5.30245   31.64276 22.40902  1.000 26.47146  ? 69  MET A N   1 
ATOM   554  C CA  . MET A 1 72 ? 6.33283   30.74897 22.92556  1.000 31.06644  ? 69  MET A CA  1 
ATOM   555  C C   . MET A 1 72 ? 6.26074   30.64698 24.44275  1.000 29.05468  ? 69  MET A C   1 
ATOM   556  O O   . MET A 1 72 ? 6.40434   29.55680 25.00756  1.000 31.73104  ? 69  MET A O   1 
ATOM   557  C CB  . MET A 1 72 ? 7.71378   31.23264 22.48536  1.000 29.09874  ? 69  MET A CB  1 
ATOM   558  C CG  . MET A 1 72 ? 7.93403   31.20046 20.98688  1.000 31.65612  ? 69  MET A CG  1 
ATOM   559  S SD  . MET A 1 72 ? 7.67374   29.55263 20.32094  1.000 39.30270  ? 69  MET A SD  1 
ATOM   560  C CE  . MET A 1 72 ? 8.86871   28.62578 21.28521  1.000 34.44988  ? 69  MET A CE  1 
ATOM   561  N N   . LYS A 1 73 ? 6.04025   31.77418 25.12094  1.000 27.95134  ? 70  LYS A N   1 
ATOM   562  C CA  . LYS A 1 73 ? 5.91742   31.74402 26.57417  1.000 34.08952  ? 70  LYS A CA  1 
ATOM   563  C C   . LYS A 1 73 ? 4.74053   30.88046 27.00975  1.000 33.72306  ? 70  LYS A C   1 
ATOM   564  O O   . LYS A 1 73 ? 4.85148   30.10365 27.96555  1.000 40.18730  ? 70  LYS A O   1 
ATOM   565  C CB  . LYS A 1 73 ? 5.77531   33.16585 27.11954  1.000 32.80461  ? 70  LYS A CB  1 
ATOM   566  C CG  . LYS A 1 73 ? 7.09529   33.88643 27.33079  1.000 37.14951  ? 70  LYS A CG  1 
ATOM   567  C CD  . LYS A 1 73 ? 6.87006   35.30457 27.83415  1.000 57.47718  ? 70  LYS A CD  1 
ATOM   568  C CE  . LYS A 1 73 ? 8.13985   35.89083 28.42961  1.000 56.21092  ? 70  LYS A CE  1 
ATOM   569  N NZ  . LYS A 1 73 ? 8.54096   35.17235 29.67164  1.000 69.95182  ? 70  LYS A NZ  1 
ATOM   570  N N   . GLU A 1 74 ? 3.60266   31.00070 26.31977  1.000 41.24940  ? 71  GLU A N   1 
ATOM   571  C CA  . GLU A 1 74 ? 2.43844   30.19446 26.67305  1.000 37.67186  ? 71  GLU A CA  1 
ATOM   572  C C   . GLU A 1 74 ? 2.65880   28.72391 26.35267  1.000 39.47725  ? 71  GLU A C   1 
ATOM   573  O O   . GLU A 1 74 ? 2.13983   27.85110 27.05848  1.000 36.32071  ? 71  GLU A O   1 
ATOM   574  C CB  . GLU A 1 74 ? 1.19557   30.71553 25.95158  1.000 41.46349  ? 71  GLU A CB  1 
ATOM   575  C CG  . GLU A 1 74 ? 0.60897   31.97120 26.57074  1.000 62.45582  ? 71  GLU A CG  1 
ATOM   576  C CD  . GLU A 1 74 ? 0.06257   31.72951 27.96580  1.000 69.05025  ? 71  GLU A CD  1 
ATOM   577  O OE1 . GLU A 1 74 ? -0.42169  30.60894 28.23199  1.000 72.54220  ? 71  GLU A OE1 1 
ATOM   578  O OE2 . GLU A 1 74 ? 0.12100   32.65822 28.79810  1.000 75.15379  ? 71  GLU A OE2 1 
ATOM   579  N N   . LEU A 1 75 ? 3.42390   28.43206 25.30053  1.000 31.63685  ? 72  LEU A N   1 
ATOM   580  C CA  . LEU A 1 75 ? 3.73460   27.04568 24.97484  1.000 39.24367  ? 72  LEU A CA  1 
ATOM   581  C C   . LEU A 1 75 ? 4.69192   26.44285 25.99577  1.000 35.78146  ? 72  LEU A C   1 
ATOM   582  O O   . LEU A 1 75 ? 4.54541   25.27587 26.37721  1.000 33.45902  ? 72  LEU A O   1 
ATOM   583  C CB  . LEU A 1 75 ? 4.32522   26.96055 23.56872  1.000 37.51424  ? 72  LEU A CB  1 
ATOM   584  C CG  . LEU A 1 75 ? 4.19783   25.61334 22.86144  1.000 46.56876  ? 72  LEU A CG  1 
ATOM   585  C CD1 . LEU A 1 75 ? 2.74058   25.31932 22.54493  1.000 43.43794  ? 72  LEU A CD1 1 
ATOM   586  C CD2 . LEU A 1 75 ? 5.03681   25.60640 21.60115  1.000 47.45252  ? 72  LEU A CD2 1 
ATOM   587  N N   . ILE A 1 76 ? 5.67938   27.22365 26.44415  1.000 29.74657  ? 73  ILE A N   1 
ATOM   588  C CA  . ILE A 1 76 ? 6.59269   26.75862 27.48565  1.000 30.74708  ? 73  ILE A CA  1 
ATOM   589  C C   . ILE A 1 76 ? 5.82499   26.44120 28.75990  1.000 36.88740  ? 73  ILE A C   1 
ATOM   590  O O   . ILE A 1 76 ? 6.09028   25.43440 29.42930  1.000 29.95771  ? 73  ILE A O   1 
ATOM   591  C CB  . ILE A 1 76 ? 7.69550   27.80476 27.73828  1.000 36.15468  ? 73  ILE A CB  1 
ATOM   592  C CG1 . ILE A 1 76 ? 8.60645   27.93624 26.51734  1.000 30.92347  ? 73  ILE A CG1 1 
ATOM   593  C CG2 . ILE A 1 76 ? 8.51285   27.43727 28.96894  1.000 36.55439  ? 73  ILE A CG2 1 
ATOM   594  C CD1 . ILE A 1 76 ? 9.45147   29.19171 26.52390  1.000 37.44007  ? 73  ILE A CD1 1 
ATOM   595  N N   . LYS A 1 77 ? 4.85858   27.28982 29.11697  1.000 33.54800  ? 74  LYS A N   1 
ATOM   596  C CA  . LYS A 1 77 ? 4.06040   27.03417 30.31010  1.000 39.22531  ? 74  LYS A CA  1 
ATOM   597  C C   . LYS A 1 77 ? 3.26492   25.74285 30.16848  1.000 43.36928  ? 74  LYS A C   1 
ATOM   598  O O   . LYS A 1 77 ? 3.24094   24.91426 31.08142  1.000 49.30984  ? 74  LYS A O   1 
ATOM   599  C CB  . LYS A 1 77 ? 3.13225   28.21416 30.58825  1.000 50.89891  ? 74  LYS A CB  1 
ATOM   600  C CG  . LYS A 1 77 ? 3.86045   29.49927 30.92081  1.000 60.19697  ? 74  LYS A CG  1 
ATOM   601  C CD  . LYS A 1 77 ? 2.88333   30.58841 31.30996  1.000 51.72033  ? 74  LYS A CD  1 
ATOM   602  C CE  . LYS A 1 77 ? 3.60029   31.90867 31.49918  1.000 72.79719  ? 74  LYS A CE  1 
ATOM   603  N NZ  . LYS A 1 77 ? 4.74987   31.76798 32.43378  1.000 74.50658  ? 74  LYS A NZ  1 
ATOM   604  N N   . GLU A 1 78 ? 2.61762   25.54909 29.01669  1.000 37.99619  ? 75  GLU A N   1 
ATOM   605  C CA  . GLU A 1 78 ? 1.86559   24.31920 28.78499  1.000 41.09688  ? 75  GLU A CA  1 
ATOM   606  C C   . GLU A 1 78 ? 2.74746   23.08136 28.88028  1.000 37.67686  ? 75  GLU A C   1 
ATOM   607  O O   . GLU A 1 78 ? 2.28268   22.01724 29.30628  1.000 42.01503  ? 75  GLU A O   1 
ATOM   608  C CB  . GLU A 1 78 ? 1.18755   24.37111 27.41448  1.000 54.14198  ? 75  GLU A CB  1 
ATOM   609  C CG  . GLU A 1 78 ? -0.13623  25.11688 27.39003  1.000 56.96259  ? 75  GLU A CG  1 
ATOM   610  C CD  . GLU A 1 78 ? -1.30722  24.24805 27.81653  1.000 70.40316  ? 75  GLU A CD  1 
ATOM   611  O OE1 . GLU A 1 78 ? -1.10446  23.30209 28.60837  1.000 73.11210  ? 75  GLU A OE1 1 
ATOM   612  O OE2 . GLU A 1 78 ? -2.43577  24.50921 27.35054  1.000 82.34016  ? 75  GLU A OE2 1 
ATOM   613  N N   . LEU A 1 79 ? 4.01917   23.19780 28.49457  1.000 29.67767  ? 76  LEU A N   1 
ATOM   614  C CA  . LEU A 1 79 ? 4.90414   22.03920 28.52461  1.000 30.94239  ? 76  LEU A CA  1 
ATOM   615  C C   . LEU A 1 79 ? 5.27621   21.65815 29.95140  1.000 37.05108  ? 76  LEU A C   1 
ATOM   616  O O   . LEU A 1 79 ? 5.36302   20.46966 30.27619  1.000 33.60201  ? 76  LEU A O   1 
ATOM   617  C CB  . LEU A 1 79 ? 6.16107   22.30967 27.69766  1.000 32.22706  ? 76  LEU A CB  1 
ATOM   618  C CG  . LEU A 1 79 ? 6.04635   22.14013 26.18096  1.000 46.28359  ? 76  LEU A CG  1 
ATOM   619  C CD1 . LEU A 1 79 ? 7.34397   22.54738 25.50768  1.000 44.64568  ? 76  LEU A CD1 1 
ATOM   620  C CD2 . LEU A 1 79 ? 5.68985   20.70488 25.82755  1.000 33.84185  ? 76  LEU A CD2 1 
ATOM   621  N N   . GLU A 1 80 ? 5.50607   22.64489 30.81950  1.000 41.22463  ? 77  GLU A N   1 
ATOM   622  C CA  . GLU A 1 80 ? 5.89272   22.31622 32.18567  1.000 53.60241  ? 77  GLU A CA  1 
ATOM   623  C C   . GLU A 1 80 ? 4.74772   21.69703 32.97662  1.000 52.62252  ? 77  GLU A C   1 
ATOM   624  O O   . GLU A 1 80 ? 5.00180   21.03045 33.98570  1.000 59.71970  ? 77  GLU A O   1 
ATOM   625  C CB  . GLU A 1 80 ? 6.42854   23.55675 32.90453  1.000 55.21896  ? 77  GLU A CB  1 
ATOM   626  C CG  . GLU A 1 80 ? 5.37780   24.56417 33.33264  1.000 69.50742  ? 77  GLU A CG  1 
ATOM   627  C CD  . GLU A 1 80 ? 5.98550   25.76152 34.03527  1.000 75.15711  ? 77  GLU A CD  1 
ATOM   628  O OE1 . GLU A 1 80 ? 7.15779   25.66674 34.45439  1.000 81.21511  ? 77  GLU A OE1 1 
ATOM   629  O OE2 . GLU A 1 80 ? 5.29732   26.79676 34.16294  1.000 73.14344  ? 77  GLU A OE2 1 
ATOM   630  N N   . LYS A 1 81 ? 3.49885   21.88967 32.54155  1.000 40.53901  ? 78  LYS A N   1 
ATOM   631  C CA  . LYS A 1 81 ? 2.38144   21.23539 33.21137  1.000 52.55077  ? 78  LYS A CA  1 
ATOM   632  C C   . LYS A 1 81 ? 2.37608   19.73347 32.96984  1.000 47.08823  ? 78  LYS A C   1 
ATOM   633  O O   . LYS A 1 81 ? 1.80975   18.98882 33.77579  1.000 56.94156  ? 78  LYS A O   1 
ATOM   634  C CB  . LYS A 1 81 ? 1.04952   21.84181 32.75936  1.000 48.26938  ? 78  LYS A CB  1 
ATOM   635  C CG  . LYS A 1 81 ? 0.59425   23.05035 33.57945  1.000 63.59738  ? 78  LYS A CG  1 
ATOM   636  C CD  . LYS A 1 81 ? 1.44517   24.26751 33.27653  1.000 63.21837  ? 78  LYS A CD  1 
ATOM   637  C CE  . LYS A 1 81 ? 1.21102   25.42970 34.22628  1.000 77.60834  ? 78  LYS A CE  1 
ATOM   638  N NZ  . LYS A 1 81 ? 2.14010   26.56063 33.91599  1.000 66.89186  ? 78  LYS A NZ  1 
ATOM   639  N N   . ILE A 1 82 ? 2.99060   19.27702 31.88545  1.000 39.68494  ? 79  ILE A N   1 
ATOM   640  C CA  . ILE A 1 82 ? 3.10284   17.85485 31.60396  1.000 51.42688  ? 79  ILE A CA  1 
ATOM   641  C C   . ILE A 1 82 ? 4.53967   17.40401 31.84318  1.000 49.68539  ? 79  ILE A C   1 
ATOM   642  O O   . ILE A 1 82 ? 4.85385   16.22035 31.73424  1.000 49.24796  ? 79  ILE A O   1 
ATOM   643  C CB  . ILE A 1 82 ? 2.65281   17.53220 30.16733  1.000 47.99612  ? 79  ILE A CB  1 
ATOM   644  C CG1 . ILE A 1 82 ? 3.61946   18.14807 29.15394  1.000 47.69041  ? 79  ILE A CG1 1 
ATOM   645  C CG2 . ILE A 1 82 ? 1.24050   18.04450 29.92534  1.000 39.56810  ? 79  ILE A CG2 1 
ATOM   646  C CD1 . ILE A 1 82 ? 3.25190   17.87794 27.71250  1.000 46.43226  ? 79  ILE A CD1 1 
ATOM   647  N N   . SER B 1 4  ? 11.69020  9.69673  25.45629  1.000 50.20677  ? 1   SER B N   1 
ATOM   648  C CA  . SER B 1 4  ? 12.00125  10.92973 24.74716  1.000 50.24374  ? 1   SER B CA  1 
ATOM   649  C C   . SER B 1 4  ? 11.15984  11.06818 23.47871  1.000 45.92695  ? 1   SER B C   1 
ATOM   650  O O   . SER B 1 4  ? 10.75008  12.17109 23.12705  1.000 42.47061  ? 1   SER B O   1 
ATOM   651  C CB  . SER B 1 4  ? 13.49138  10.99344 24.40473  1.000 61.63740  ? 1   SER B CB  1 
ATOM   652  O OG  . SER B 1 4  ? 13.81081  12.20617 23.74354  1.000 44.02763  ? 1   SER B OG  1 
ATOM   653  N N   . ILE B 1 5  ? 10.90741  9.94971  22.79184  1.000 46.75547  ? 2   ILE B N   1 
ATOM   654  C CA  . ILE B 1 5  ? 10.02850  9.98385  21.62394  1.000 43.85165  ? 2   ILE B CA  1 
ATOM   655  C C   . ILE B 1 5  ? 8.62785   10.42047 22.03204  1.000 43.19774  ? 2   ILE B C   1 
ATOM   656  O O   . ILE B 1 5  ? 7.97700   11.20569 21.33261  1.000 44.22035  ? 2   ILE B O   1 
ATOM   657  C CB  . ILE B 1 5  ? 10.00799  8.61525  20.91718  1.000 54.82341  ? 2   ILE B CB  1 
ATOM   658  C CG1 . ILE B 1 5  ? 11.38809  8.27755  20.35265  1.000 57.87433  ? 2   ILE B CG1 1 
ATOM   659  C CG2 . ILE B 1 5  ? 8.96865   8.60140  19.80553  1.000 38.47253  ? 2   ILE B CG2 1 
ATOM   660  C CD1 . ILE B 1 5  ? 11.84555  9.21647  19.26040  1.000 52.89132  ? 2   ILE B CD1 1 
ATOM   661  N N   . LYS B 1 6  ? 8.14311   9.91513  23.16877  1.000 39.45687  ? 3   LYS B N   1 
ATOM   662  C CA  . LYS B 1 6  ? 6.88382   10.40659 23.71908  1.000 44.20141  ? 3   LYS B CA  1 
ATOM   663  C C   . LYS B 1 6  ? 6.96655   11.89547 24.02187  1.000 43.90353  ? 3   LYS B C   1 
ATOM   664  O O   . LYS B 1 6  ? 6.03643   12.65029 23.71412  1.000 47.94466  ? 3   LYS B O   1 
ATOM   665  C CB  . LYS B 1 6  ? 6.52018   9.62684  24.98377  1.000 50.77748  ? 3   LYS B CB  1 
ATOM   666  C CG  . LYS B 1 6  ? 5.26126   10.12660 25.68805  1.000 51.87655  ? 3   LYS B CG  1 
ATOM   667  C CD  . LYS B 1 6  ? 5.10081   9.50891  27.07065  1.000 57.77135  ? 3   LYS B CD  1 
ATOM   668  C CE  . LYS B 1 6  ? 6.19241   9.98395  28.02454  1.000 67.34800  ? 3   LYS B CE  1 
ATOM   669  N NZ  . LYS B 1 6  ? 6.00758   9.45375  29.40636  1.000 57.35261  ? 3   LYS B NZ  1 
ATOM   670  N N   . GLU B 1 7  ? 8.07842   12.33529 24.61756  1.000 41.25997  ? 4   GLU B N   1 
ATOM   671  C CA  . GLU B 1 7  ? 8.25963   13.75064 24.92151  1.000 38.05637  ? 4   GLU B CA  1 
ATOM   672  C C   . GLU B 1 7  ? 8.25202   14.59032 23.65128  1.000 41.12441  ? 4   GLU B C   1 
ATOM   673  O O   . GLU B 1 7  ? 7.68910   15.69031 23.62715  1.000 35.54953  ? 4   GLU B O   1 
ATOM   674  C CB  . GLU B 1 7  ? 9.56544   13.94890 25.69082  1.000 45.47890  ? 4   GLU B CB  1 
ATOM   675  C CG  . GLU B 1 7  ? 9.78865   15.36090 26.19871  1.000 47.22078  ? 4   GLU B CG  1 
ATOM   676  C CD  . GLU B 1 7  ? 11.16079  15.54401 26.80607  1.000 52.84588  ? 4   GLU B CD  1 
ATOM   677  O OE1 . GLU B 1 7  ? 12.15957  15.36719 26.07718  1.000 57.24619  ? 4   GLU B OE1 1 
ATOM   678  O OE2 . GLU B 1 7  ? 11.23970  15.85188 28.01380  1.000 51.82353  ? 4   GLU B OE2 1 
ATOM   679  N N   . ILE B 1 8  ? 8.86918   14.08272 22.58267  1.000 44.97160  ? 5   ILE B N   1 
ATOM   680  C CA  . ILE B 1 8  ? 8.87509   14.79570 21.30947  1.000 36.60620  ? 5   ILE B CA  1 
ATOM   681  C C   . ILE B 1 8  ? 7.47929   14.81588 20.70050  1.000 40.12291  ? 5   ILE B C   1 
ATOM   682  O O   . ILE B 1 8  ? 7.03634   15.83525 20.15544  1.000 37.21027  ? 5   ILE B O   1 
ATOM   683  C CB  . ILE B 1 8  ? 9.90351   14.15324 20.36220  1.000 35.43479  ? 5   ILE B CB  1 
ATOM   684  C CG1 . ILE B 1 8  ? 11.31927  14.46876 20.83969  1.000 46.04580  ? 5   ILE B CG1 1 
ATOM   685  C CG2 . ILE B 1 8  ? 9.69137   14.61018 18.92992  1.000 34.78127  ? 5   ILE B CG2 1 
ATOM   686  C CD1 . ILE B 1 8  ? 12.38707  13.76467 20.05499  1.000 57.49044  ? 5   ILE B CD1 1 
ATOM   687  N N   . THR B 1 9  ? 6.76489   13.69277 20.78422  1.000 38.66023  ? 6   THR B N   1 
ATOM   688  C CA  . THR B 1 9  ? 5.41106   13.62270 20.24438  1.000 40.83972  ? 6   THR B CA  1 
ATOM   689  C C   . THR B 1 9  ? 4.46375   14.54106 21.00632  1.000 33.23619  ? 6   THR B C   1 
ATOM   690  O O   . THR B 1 9  ? 3.71393   15.31694 20.40077  1.000 40.28780  ? 6   THR B O   1 
ATOM   691  C CB  . THR B 1 9  ? 4.90885   12.18216 20.29217  1.000 36.75189  ? 6   THR B CB  1 
ATOM   692  O OG1 . THR B 1 9  ? 5.81340   11.34058 19.56813  1.000 39.81521  ? 6   THR B OG1 1 
ATOM   693  C CG2 . THR B 1 9  ? 3.51263   12.08503 19.68279  1.000 47.40675  ? 6   THR B CG2 1 
ATOM   694  N N   . GLU B 1 10 ? 4.48144   14.46196 22.34073  1.000 35.07947  ? 7   GLU B N   1 
ATOM   695  C CA  . GLU B 1 10 ? 3.62403   15.32500 23.14712  1.000 40.76870  ? 7   GLU B CA  1 
ATOM   696  C C   . GLU B 1 10 ? 3.96474   16.79494 22.94735  1.000 36.66880  ? 7   GLU B C   1 
ATOM   697  O O   . GLU B 1 10 ? 3.07085   17.64956 22.98338  1.000 37.15601  ? 7   GLU B O   1 
ATOM   698  C CB  . GLU B 1 10 ? 3.73688   14.95018 24.62650  1.000 39.20167  ? 7   GLU B CB  1 
ATOM   699  C CG  . GLU B 1 10 ? 3.22794   13.55460 24.95926  1.000 58.88654  ? 7   GLU B CG  1 
ATOM   700  C CD  . GLU B 1 10 ? 3.44087   13.18757 26.41644  1.000 60.58382  ? 7   GLU B CD  1 
ATOM   701  O OE1 . GLU B 1 10 ? 4.10571   13.96378 27.13540  1.000 64.33102  ? 7   GLU B OE1 1 
ATOM   702  O OE2 . GLU B 1 10 ? 2.94379   12.12394 26.84284  1.000 61.68628  ? 7   GLU B OE2 1 
ATOM   703  N N   . THR B 1 11 ? 5.24542   17.11027 22.73673  1.000 33.12733  ? 8   THR B N   1 
ATOM   704  C CA  . THR B 1 11 ? 5.62291   18.49388 22.47336  1.000 35.76461  ? 8   THR B CA  1 
ATOM   705  C C   . THR B 1 11 ? 5.10496   18.95194 21.11821  1.000 31.85181  ? 8   THR B C   1 
ATOM   706  O O   . THR B 1 11 ? 4.54626   20.04815 21.00036  1.000 32.73602  ? 8   THR B O   1 
ATOM   707  C CB  . THR B 1 11 ? 7.13991   18.65709 22.54725  1.000 34.85667  ? 8   THR B CB  1 
ATOM   708  O OG1 . THR B 1 11 ? 7.59085   18.32880 23.86681  1.000 34.77334  ? 8   THR B OG1 1 
ATOM   709  C CG2 . THR B 1 11 ? 7.53418   20.09460 22.22992  1.000 34.23968  ? 8   THR B CG2 1 
ATOM   710  N N   . THR B 1 12 ? 5.28046   18.12520 20.08453  1.000 33.80818  ? 9   THR B N   1 
ATOM   711  C CA  . THR B 1 12 ? 4.75770   18.46744 18.76640  1.000 32.80051  ? 9   THR B CA  1 
ATOM   712  C C   . THR B 1 12 ? 3.23605   18.55259 18.77476  1.000 37.41164  ? 9   THR B C   1 
ATOM   713  O O   . THR B 1 12 ? 2.65667   19.37105 18.05139  1.000 47.94666  ? 9   THR B O   1 
ATOM   714  C CB  . THR B 1 12 ? 5.24259   17.44724 17.73375  1.000 29.26844  ? 9   THR B CB  1 
ATOM   715  O OG1 . THR B 1 12 ? 6.67482   17.44457 17.71206  1.000 33.94582  ? 9   THR B OG1 1 
ATOM   716  C CG2 . THR B 1 12 ? 4.73613   17.79235 16.34303  1.000 30.52894  ? 9   THR B CG2 1 
ATOM   717  N N   . GLN B 1 13 ? 2.57359   17.73444 19.59581  1.000 37.22678  ? 10  GLN B N   1 
ATOM   718  C CA  . GLN B 1 13 ? 1.12283   17.83464 19.72319  1.000 42.76453  ? 10  GLN B CA  1 
ATOM   719  C C   . GLN B 1 13 ? 0.71123   19.17479 20.31845  1.000 40.08088  ? 10  GLN B C   1 
ATOM   720  O O   . GLN B 1 13 ? -0.23439  19.80966 19.83892  1.000 47.48397  ? 10  GLN B O   1 
ATOM   721  C CB  . GLN B 1 13 ? 0.58920   16.68282 20.57240  1.000 36.27905  ? 10  GLN B CB  1 
ATOM   722  C CG  . GLN B 1 13 ? 0.53941   15.35174 19.83971  1.000 43.04571  ? 10  GLN B CG  1 
ATOM   723  C CD  . GLN B 1 13 ? 0.08963   14.21467 20.73342  1.000 54.19071  ? 10  GLN B CD  1 
ATOM   724  O OE1 . GLN B 1 13 ? 0.65393   13.99238 21.80454  1.000 42.26801  ? 10  GLN B OE1 1 
ATOM   725  N NE2 . GLN B 1 13 ? -0.93286  13.48922 20.29864  1.000 40.51727  ? 10  GLN B NE2 1 
ATOM   726  N N   . LEU B 1 14 ? 1.40367   19.61896 21.37048  1.000 38.05604  ? 11  LEU B N   1 
ATOM   727  C CA  . LEU B 1 14 ? 1.13490   20.94531 21.91582  1.000 40.95278  ? 11  LEU B CA  1 
ATOM   728  C C   . LEU B 1 14 ? 1.48617   22.03929 20.91876  1.000 48.43182  ? 11  LEU B C   1 
ATOM   729  O O   . LEU B 1 14 ? 0.81767   23.07825 20.87660  1.000 53.97987  ? 11  LEU B O   1 
ATOM   730  C CB  . LEU B 1 14 ? 1.91165   21.15265 23.21539  1.000 41.89214  ? 11  LEU B CB  1 
ATOM   731  C CG  . LEU B 1 14 ? 1.14161   20.91894 24.51397  1.000 46.88790  ? 11  LEU B CG  1 
ATOM   732  C CD1 . LEU B 1 14 ? 2.05177   21.09446 25.71858  1.000 52.56951  ? 11  LEU B CD1 1 
ATOM   733  C CD2 . LEU B 1 14 ? -0.04424  21.86446 24.59788  1.000 48.67002  ? 11  LEU B CD2 1 
ATOM   734  N N   . ILE B 1 15 ? 2.52828   21.82534 20.11429  1.000 43.60727  ? 12  ILE B N   1 
ATOM   735  C CA  . ILE B 1 15 ? 2.91594   22.81145 19.11175  1.000 43.81587  ? 12  ILE B CA  1 
ATOM   736  C C   . ILE B 1 15 ? 1.79703   23.01704 18.09489  1.000 51.75604  ? 12  ILE B C   1 
ATOM   737  O O   . ILE B 1 15 ? 1.44395   24.15466 17.76466  1.000 51.30389  ? 12  ILE B O   1 
ATOM   738  C CB  . ILE B 1 15 ? 4.23810   22.38869 18.44208  1.000 48.15516  ? 12  ILE B CB  1 
ATOM   739  C CG1 . ILE B 1 15 ? 5.41930   22.70189 19.36674  1.000 48.31551  ? 12  ILE B CG1 1 
ATOM   740  C CG2 . ILE B 1 15 ? 4.40627   23.05087 17.08123  1.000 47.01058  ? 12  ILE B CG2 1 
ATOM   741  C CD1 . ILE B 1 15 ? 6.76915   22.28832 18.81459  1.000 37.70872  ? 12  ILE B CD1 1 
ATOM   742  N N   . VAL B 1 16 ? 1.20994   21.92594 17.59594  1.000 45.57422  ? 13  VAL B N   1 
ATOM   743  C CA  . VAL B 1 16 ? 0.16406   22.06945 16.58650  1.000 51.15972  ? 13  VAL B CA  1 
ATOM   744  C C   . VAL B 1 16 ? -1.16005  22.50090 17.20997  1.000 49.61436  ? 13  VAL B C   1 
ATOM   745  O O   . VAL B 1 16 ? -1.96936  23.16013 16.54831  1.000 59.56275  ? 13  VAL B O   1 
ATOM   746  C CB  . VAL B 1 16 ? 0.00303   20.77032 15.77711  1.000 48.17745  ? 13  VAL B CB  1 
ATOM   747  C CG1 . VAL B 1 16 ? 1.31895   20.38251 15.14205  1.000 39.79230  ? 13  VAL B CG1 1 
ATOM   748  C CG2 . VAL B 1 16 ? -0.52859  19.64553 16.64817  1.000 40.51744  ? 13  VAL B CG2 1 
ATOM   749  N N   . LYS B 1 17 ? -1.40990  22.15468 18.47576  1.000 50.63863  ? 14  LYS B N   1 
ATOM   750  C CA  . LYS B 1 17 ? -2.64303  22.58757 19.12397  1.000 54.97079  ? 14  LYS B CA  1 
ATOM   751  C C   . LYS B 1 17 ? -2.63624  24.06955 19.46821  1.000 72.12702  ? 14  LYS B C   1 
ATOM   752  O O   . LYS B 1 17 ? -3.69024  24.60939 19.82190  1.000 75.51836  ? 14  LYS B O   1 
ATOM   753  C CB  . LYS B 1 17 ? -2.90292  21.76436 20.38762  1.000 53.85989  ? 14  LYS B CB  1 
ATOM   754  C CG  . LYS B 1 17 ? -3.38896  20.35239 20.10604  1.000 58.25054  ? 14  LYS B CG  1 
ATOM   755  C CD  . LYS B 1 17 ? -3.95833  19.69377 21.35114  1.000 67.57710  ? 14  LYS B CD  1 
ATOM   756  C CE  . LYS B 1 17 ? -2.89493  19.49840 22.41638  1.000 67.61703  ? 14  LYS B CE  1 
ATOM   757  N NZ  . LYS B 1 17 ? -3.44771  18.81395 23.61744  1.000 82.21811  ? 14  LYS B NZ  1 
ATOM   758  N N   . HIS B 1 18 ? -1.48541  24.73521 19.37049  1.000 70.98782  ? 15  HIS B N   1 
ATOM   759  C CA  . HIS B 1 18 ? -1.38850  26.16809 19.59772  1.000 69.90162  ? 15  HIS B CA  1 
ATOM   760  C C   . HIS B 1 18 ? -1.05721  26.95784 18.33922  1.000 73.51638  ? 15  HIS B C   1 
ATOM   761  O O   . HIS B 1 18 ? -1.09632  28.19207 18.37761  1.000 84.90157  ? 15  HIS B O   1 
ATOM   762  C CB  . HIS B 1 18 ? -0.33120  26.46431 20.67298  1.000 69.42613  ? 15  HIS B CB  1 
ATOM   763  C CG  . HIS B 1 18 ? -0.77214  26.13088 22.06471  1.000 90.80161  ? 15  HIS B CG  1 
ATOM   764  N ND1 . HIS B 1 18 ? -1.28702  24.89947 22.41114  1.000 89.03544  ? 15  HIS B ND1 1 
ATOM   765  C CD2 . HIS B 1 18 ? -0.77331  26.87079 23.19882  1.000 90.95395  ? 15  HIS B CD2 1 
ATOM   766  C CE1 . HIS B 1 18 ? -1.58795  24.89679 23.69754  1.000 95.38434  ? 15  HIS B CE1 1 
ATOM   767  N NE2 . HIS B 1 18 ? -1.28552  26.08096 24.19902  1.000 95.80242  ? 15  HIS B NE2 1 
ATOM   768  N N   . LEU B 1 19 ? -0.74588  26.28755 17.22899  1.000 63.21822  ? 16  LEU B N   1 
ATOM   769  C CA  . LEU B 1 19 ? -0.30625  26.94665 16.00537  1.000 73.23126  ? 16  LEU B CA  1 
ATOM   770  C C   . LEU B 1 19 ? -1.28525  26.75411 14.84906  1.000 73.40123  ? 16  LEU B C   1 
ATOM   771  O O   . LEU B 1 19 ? -1.75399  27.73572 14.26742  1.000 76.12593  ? 16  LEU B O   1 
ATOM   772  C CB  . LEU B 1 19 ? 1.08915   26.43276 15.61402  1.000 74.96933  ? 16  LEU B CB  1 
ATOM   773  C CG  . LEU B 1 19 ? 1.63296   26.71167 14.20878  1.000 79.35179  ? 16  LEU B CG  1 
ATOM   774  C CD1 . LEU B 1 19 ? 3.09630   27.10312 14.28121  1.000 70.92531  ? 16  LEU B CD1 1 
ATOM   775  C CD2 . LEU B 1 19 ? 1.46987   25.49597 13.30802  1.000 79.93462  ? 16  LEU B CD2 1 
ATOM   776  N N   . ALA B 1 20 ? -1.60162  25.51176 14.50171  1.000 60.09855  ? 17  ALA B N   1 
ATOM   777  C CA  . ALA B 1 20 ? -2.35240  25.21779 13.29035  1.000 63.44862  ? 17  ALA B CA  1 
ATOM   778  C C   . ALA B 1 20 ? -3.85454  25.20612 13.55034  1.000 65.42620  ? 17  ALA B C   1 
ATOM   779  O O   . ALA B 1 20 ? -4.31369  24.94890 14.66680  1.000 63.68895  ? 17  ALA B O   1 
ATOM   780  C CB  . ALA B 1 20 ? -1.91793  23.87085 12.71015  1.000 65.93544  ? 17  ALA B CB  1 
ATOM   781  N N   . HIS B 1 21 ? -4.61930  25.49716 12.49988  1.000 55.11106  ? 18  HIS B N   1 
ATOM   782  C CA  . HIS B 1 21 ? -6.06314  25.32846 12.56768  1.000 63.73681  ? 18  HIS B CA  1 
ATOM   783  C C   . HIS B 1 21 ? -6.39970  23.85298 12.74244  1.000 59.54227  ? 18  HIS B C   1 
ATOM   784  O O   . HIS B 1 21 ? -5.66833  22.97085 12.28516  1.000 58.36635  ? 18  HIS B O   1 
ATOM   785  C CB  . HIS B 1 21 ? -6.72962  25.87721 11.30614  1.000 61.78282  ? 18  HIS B CB  1 
ATOM   786  C CG  . HIS B 1 21 ? -6.42550  27.31874 11.03880  1.000 69.95342  ? 18  HIS B CG  1 
ATOM   787  N ND1 . HIS B 1 21 ? -5.26577  27.73159 10.41840  1.000 70.20190  ? 18  HIS B ND1 1 
ATOM   788  C CD2 . HIS B 1 21 ? -7.12902  28.44435 11.30715  1.000 60.31410  ? 18  HIS B CD2 1 
ATOM   789  C CE1 . HIS B 1 21 ? -5.26917  29.04834 10.31455  1.000 66.39894  ? 18  HIS B CE1 1 
ATOM   790  N NE2 . HIS B 1 21 ? -6.38817  29.50577 10.84723  1.000 60.87464  ? 18  HIS B NE2 1 
ATOM   791  N N   . ASN B 1 22 ? -7.52295  23.59089 13.41009  1.000 53.00485  ? 19  ASN B N   1 
ATOM   792  C CA  . ASN B 1 22 ? -7.90325  22.23537 13.80566  1.000 56.28891  ? 19  ASN B CA  1 
ATOM   793  C C   . ASN B 1 22 ? -6.74091  21.54755 14.51830  1.000 58.15041  ? 19  ASN B C   1 
ATOM   794  O O   . ASN B 1 22 ? -6.34570  20.42689 14.18643  1.000 46.26603  ? 19  ASN B O   1 
ATOM   795  C CB  . ASN B 1 22 ? -8.37441  21.41621 12.60119  1.000 54.95304  ? 19  ASN B CB  1 
ATOM   796  C CG  . ASN B 1 22 ? -9.35750  22.16902 11.73203  1.000 66.55592  ? 19  ASN B CG  1 
ATOM   797  O OD1 . ASN B 1 22 ? -10.56284 22.15817 11.98204  1.000 63.24495  ? 19  ASN B OD1 1 
ATOM   798  N ND2 . ASN B 1 22 ? -8.84669  22.82553 10.69799  1.000 70.41283  ? 19  ASN B ND2 1 
ATOM   799  N N   . GLY B 1 23 ? -6.17782  22.25364 15.50376  1.000 49.50245  ? 20  GLY B N   1 
ATOM   800  C CA  . GLY B 1 23 ? -5.00122  21.75616 16.19309  1.000 54.45354  ? 20  GLY B CA  1 
ATOM   801  C C   . GLY B 1 23 ? -5.19830  20.39991 16.83769  1.000 54.10126  ? 20  GLY B C   1 
ATOM   802  O O   . GLY B 1 23 ? -4.26295  19.59948 16.89557  1.000 51.95216  ? 20  GLY B O   1 
ATOM   803  N N   . GLU B 1 24 ? -6.40832  20.12093 17.32865  1.000 49.43593  ? 21  GLU B N   1 
ATOM   804  C CA  . GLU B 1 24 ? -6.66828  18.79851 17.88392  1.000 60.22743  ? 21  GLU B CA  1 
ATOM   805  C C   . GLU B 1 24 ? -6.63757  17.73356 16.79835  1.000 49.37026  ? 21  GLU B C   1 
ATOM   806  O O   . GLU B 1 24 ? -6.23991  16.59487 17.06396  1.000 55.66860  ? 21  GLU B O   1 
ATOM   807  C CB  . GLU B 1 24 ? -8.00979  18.77890 18.62013  1.000 67.41529  ? 21  GLU B CB  1 
ATOM   808  C CG  . GLU B 1 24 ? -7.96878  18.05317 19.96597  1.000 73.50810  ? 21  GLU B CG  1 
ATOM   809  C CD  . GLU B 1 24 ? -7.66801  16.56543 19.84255  1.000 73.24866  ? 21  GLU B CD  1 
ATOM   810  O OE1 . GLU B 1 24 ? -8.35644  15.87217 19.06328  1.000 74.61013  ? 21  GLU B OE1 1 
ATOM   811  O OE2 . GLU B 1 24 ? -6.74300  16.08682 20.53213  1.000 68.16998  ? 21  GLU B OE2 1 
ATOM   812  N N   . GLU B 1 25 ? -7.03939  18.08309 15.57396  1.000 55.24042  ? 22  GLU B N   1 
ATOM   813  C CA  . GLU B 1 25 ? -6.95485  17.12874 14.47354  1.000 49.22499  ? 22  GLU B CA  1 
ATOM   814  C C   . GLU B 1 25 ? -5.50690  16.79950 14.13766  1.000 42.70138  ? 22  GLU B C   1 
ATOM   815  O O   . GLU B 1 25 ? -5.16712  15.63021 13.92386  1.000 47.12540  ? 22  GLU B O   1 
ATOM   816  C CB  . GLU B 1 25 ? -7.67287  17.67346 13.24076  1.000 50.91056  ? 22  GLU B CB  1 
ATOM   817  C CG  . GLU B 1 25 ? -9.18983  17.59658 13.29801  1.000 60.99782  ? 22  GLU B CG  1 
ATOM   818  C CD  . GLU B 1 25 ? -9.83489  17.93881 11.96866  1.000 73.20756  ? 22  GLU B CD  1 
ATOM   819  O OE1 . GLU B 1 25 ? -9.10470  18.03774 10.96222  1.000 70.13270  ? 22  GLU B OE1 1 
ATOM   820  O OE2 . GLU B 1 25 ? -11.07051 18.11144 11.92834  1.000 86.10965  ? 22  GLU B OE2 1 
ATOM   821  N N   . TYR B 1 26 ? -4.63995  17.81333 14.08395  1.000 46.33609  ? 23  TYR B N   1 
ATOM   822  C CA  . TYR B 1 26 ? -3.23490  17.55983 13.77955  1.000 51.25902  ? 23  TYR B CA  1 
ATOM   823  C C   . TYR B 1 26 ? -2.55196  16.79250 14.90245  1.000 38.74118  ? 23  TYR B C   1 
ATOM   824  O O   . TYR B 1 26 ? -1.70536  15.93015 14.64164  1.000 40.00179  ? 23  TYR B O   1 
ATOM   825  C CB  . TYR B 1 26 ? -2.49965  18.87242 13.51433  1.000 44.81107  ? 23  TYR B CB  1 
ATOM   826  C CG  . TYR B 1 26 ? -2.78297  19.46670 12.15723  1.000 56.92992  ? 23  TYR B CG  1 
ATOM   827  C CD1 . TYR B 1 26 ? -2.25700  18.89743 11.00536  1.000 53.58714  ? 23  TYR B CD1 1 
ATOM   828  C CD2 . TYR B 1 26 ? -3.56899  20.60091 12.02676  1.000 57.26134  ? 23  TYR B CD2 1 
ATOM   829  C CE1 . TYR B 1 26 ? -2.51369  19.43888 9.76248   1.000 54.64603  ? 23  TYR B CE1 1 
ATOM   830  C CE2 . TYR B 1 26 ? -3.82820  21.14817 10.79000  1.000 59.49221  ? 23  TYR B CE2 1 
ATOM   831  C CZ  . TYR B 1 26 ? -3.30076  20.56624 9.66204   1.000 58.96075  ? 23  TYR B CZ  1 
ATOM   832  O OH  . TYR B 1 26 ? -3.56666  21.11941 8.43107   1.000 58.58318  ? 23  TYR B OH  1 
ATOM   833  N N   . SER B 1 27 ? -2.89597  17.09641 16.15733  1.000 45.35092  ? 24  SER B N   1 
ATOM   834  C CA  . SER B 1 27 ? -2.24923  16.41962 17.27777  1.000 43.95000  ? 24  SER B CA  1 
ATOM   835  C C   . SER B 1 27 ? -2.53717  14.92338 17.25592  1.000 48.11876  ? 24  SER B C   1 
ATOM   836  O O   . SER B 1 27 ? -1.65308  14.10991 17.55020  1.000 41.26299  ? 24  SER B O   1 
ATOM   837  C CB  . SER B 1 27 ? -2.69582  17.03698 18.60411  1.000 45.25133  ? 24  SER B CB  1 
ATOM   838  O OG  . SER B 1 27 ? -4.00564  16.62219 18.94877  1.000 69.48239  ? 24  SER B OG  1 
ATOM   839  N N   . GLU B 1 28 ? -3.76758  14.53821 16.90334  1.000 41.58394  ? 25  GLU B N   1 
ATOM   840  C CA  . GLU B 1 28 ? -4.06622  13.11889 16.75078  1.000 43.25724  ? 25  GLU B CA  1 
ATOM   841  C C   . GLU B 1 28 ? -3.30982  12.51785 15.57364  1.000 48.79267  ? 25  GLU B C   1 
ATOM   842  O O   . GLU B 1 28 ? -2.90742  11.34999 15.62897  1.000 41.49981  ? 25  GLU B O   1 
ATOM   843  C CB  . GLU B 1 28 ? -5.57213  12.90394 16.59181  1.000 48.97322  ? 25  GLU B CB  1 
ATOM   844  C CG  . GLU B 1 28 ? -6.37882  13.31982 17.81417  1.000 59.17347  ? 25  GLU B CG  1 
ATOM   845  C CD  . GLU B 1 28 ? -7.37152  12.25833 18.25693  1.000 81.15236  ? 25  GLU B CD  1 
ATOM   846  O OE1 . GLU B 1 28 ? -7.40936  11.17861 17.62944  1.000 84.60578  ? 25  GLU B OE1 1 
ATOM   847  O OE2 . GLU B 1 28 ? -8.11477  12.50454 19.23297  1.000 76.35407  ? 25  GLU B OE2 1 
ATOM   848  N N   . VAL B 1 29 ? -3.09939  13.29513 14.50895  1.000 42.40208  ? 26  VAL B N   1 
ATOM   849  C CA  . VAL B 1 29 ? -2.25722  12.82593 13.41366  1.000 40.59595  ? 26  VAL B CA  1 
ATOM   850  C C   . VAL B 1 29 ? -0.81849  12.66066 13.88659  1.000 42.34037  ? 26  VAL B C   1 
ATOM   851  O O   . VAL B 1 29 ? -0.14137  11.68858 13.52746  1.000 38.73721  ? 26  VAL B O   1 
ATOM   852  C CB  . VAL B 1 29 ? -2.35663  13.78296 12.21121  1.000 45.47483  ? 26  VAL B CB  1 
ATOM   853  C CG1 . VAL B 1 29 ? -1.34784  13.40087 11.14173  1.000 45.41872  ? 26  VAL B CG1 1 
ATOM   854  C CG2 . VAL B 1 29 ? -3.76584  13.77024 11.63807  1.000 41.15609  ? 26  VAL B CG2 1 
ATOM   855  N N   . VAL B 1 30 ? -0.33174  13.59724 14.70696  1.000 34.97851  ? 27  VAL B N   1 
ATOM   856  C CA  . VAL B 1 30 ? 1.01902   13.48740 15.25600  1.000 37.58650  ? 27  VAL B CA  1 
ATOM   857  C C   . VAL B 1 30 ? 1.16632   12.19094 16.04128  1.000 33.43064  ? 27  VAL B C   1 
ATOM   858  O O   . VAL B 1 30 ? 2.14435   11.45417 15.87937  1.000 40.84887  ? 27  VAL B O   1 
ATOM   859  C CB  . VAL B 1 30 ? 1.35108   14.70896 16.13259  1.000 42.17521  ? 27  VAL B CB  1 
ATOM   860  C CG1 . VAL B 1 30 ? 2.65948   14.48679 16.88664  1.000 39.77262  ? 27  VAL B CG1 1 
ATOM   861  C CG2 . VAL B 1 30 ? 1.44410   15.95384 15.29056  1.000 38.93348  ? 27  VAL B CG2 1 
ATOM   862  N N   . LYS B 1 31 ? 0.18629   11.89273 16.89762  1.000 36.02171  ? 28  LYS B N   1 
ATOM   863  C CA  . LYS B 1 31 ? 0.24602   10.67316 17.69836  1.000 52.03146  ? 28  LYS B CA  1 
ATOM   864  C C   . LYS B 1 31 ? 0.27275   9.42783  16.82028  1.000 42.62187  ? 28  LYS B C   1 
ATOM   865  O O   . LYS B 1 31 ? 1.07350   8.51540  17.05606  1.000 52.70580  ? 28  LYS B O   1 
ATOM   866  C CB  . LYS B 1 31 ? -0.93680  10.62491 18.66513  1.000 41.74874  ? 28  LYS B CB  1 
ATOM   867  C CG  . LYS B 1 31 ? -0.98259  9.38332  19.54614  1.000 48.91756  ? 28  LYS B CG  1 
ATOM   868  C CD  . LYS B 1 31 ? -2.11005  9.46564  20.55863  1.000 53.61436  ? 28  LYS B CD  1 
ATOM   869  C CE  . LYS B 1 31 ? -2.30761  8.14230  21.27193  1.000 67.23833  ? 28  LYS B CE  1 
ATOM   870  N NZ  . LYS B 1 31 ? -2.67967  7.05449  20.32305  1.000 60.35838  ? 28  LYS B NZ  1 
ATOM   871  N N   . GLU B 1 32 ? -0.58642  9.37397  15.79833  1.000 42.03243  ? 29  GLU B N   1 
ATOM   872  C CA  . GLU B 1 32 ? -0.63556  8.19693  14.93427  1.000 45.85842  ? 29  GLU B CA  1 
ATOM   873  C C   . GLU B 1 32 ? 0.63156   8.07104  14.09558  1.000 49.39496  ? 29  GLU B C   1 
ATOM   874  O O   . GLU B 1 32 ? 1.12109   6.95984  13.86174  1.000 52.95407  ? 29  GLU B O   1 
ATOM   875  C CB  . GLU B 1 32 ? -1.87270  8.25390  14.03548  1.000 43.55573  ? 29  GLU B CB  1 
ATOM   876  C CG  . GLU B 1 32 ? -2.07584  7.00670  13.18404  1.000 58.38093  ? 29  GLU B CG  1 
ATOM   877  C CD  . GLU B 1 32 ? -3.32342  7.07523  12.32689  1.000 65.18762  ? 29  GLU B CD  1 
ATOM   878  O OE1 . GLU B 1 32 ? -3.93091  8.16312  12.24295  1.000 65.40500  ? 29  GLU B OE1 1 
ATOM   879  O OE2 . GLU B 1 32 ? -3.69606  6.03828  11.73815  1.000 66.06207  ? 29  GLU B OE2 1 
ATOM   880  N N   . ILE B 1 33 ? 1.17789   9.19731  13.63581  1.000 44.42455  ? 30  ILE B N   1 
ATOM   881  C CA  . ILE B 1 33 ? 2.39330   9.15759  12.82812  1.000 42.53994  ? 30  ILE B CA  1 
ATOM   882  C C   . ILE B 1 33 ? 3.60072   8.80813  13.69047  1.000 47.60143  ? 30  ILE B C   1 
ATOM   883  O O   . ILE B 1 33 ? 4.49802   8.07280  13.25933  1.000 53.67951  ? 30  ILE B O   1 
ATOM   884  C CB  . ILE B 1 33 ? 2.57827   10.49806 12.09412  1.000 49.70420  ? 30  ILE B CB  1 
ATOM   885  C CG1 . ILE B 1 33 ? 1.53328   10.63614 10.98689  1.000 42.13432  ? 30  ILE B CG1 1 
ATOM   886  C CG2 . ILE B 1 33 ? 3.98561   10.62787 11.53786  1.000 54.10030  ? 30  ILE B CG2 1 
ATOM   887  C CD1 . ILE B 1 33 ? 1.52368   9.47891  10.01481  1.000 47.30285  ? 30  ILE B CD1 1 
ATOM   888  N N   . SER B 1 34 ? 3.63816   9.31795  14.92368  1.000 42.92638  ? 31  SER B N   1 
ATOM   889  C CA  . SER B 1 34 ? 4.74335   9.00686  15.82411  1.000 45.10835  ? 31  SER B CA  1 
ATOM   890  C C   . SER B 1 34 ? 4.81491   7.51409  16.11697  1.000 52.32234  ? 31  SER B C   1 
ATOM   891  O O   . SER B 1 34 ? 5.88941   6.90779  16.04214  1.000 59.75980  ? 31  SER B O   1 
ATOM   892  C CB  . SER B 1 34 ? 4.60200   9.80018  17.11995  1.000 42.58914  ? 31  SER B CB  1 
ATOM   893  O OG  . SER B 1 34 ? 4.77853   11.18669 16.88583  1.000 58.30767  ? 31  SER B OG  1 
ATOM   894  N N   . GLU B 1 35 ? 3.67676   6.90116  16.45549  1.000 58.01848  ? 32  GLU B N   1 
ATOM   895  C CA  . GLU B 1 35 ? 3.67680   5.47489  16.75807  1.000 44.55037  ? 32  GLU B CA  1 
ATOM   896  C C   . GLU B 1 35 ? 3.95446   4.62551  15.52419  1.000 51.24676  ? 32  GLU B C   1 
ATOM   897  O O   . GLU B 1 35 ? 4.41020   3.48580  15.66427  1.000 63.17262  ? 32  GLU B O   1 
ATOM   898  C CB  . GLU B 1 35 ? 2.34992   5.06522  17.40683  1.000 53.14448  ? 32  GLU B CB  1 
ATOM   899  C CG  . GLU B 1 35 ? 1.12686   5.21425  16.51898  1.000 61.34660  ? 32  GLU B CG  1 
ATOM   900  C CD  . GLU B 1 35 ? -0.16200  4.84421  17.23138  1.000 68.69583  ? 32  GLU B CD  1 
ATOM   901  O OE1 . GLU B 1 35 ? -0.14670  4.73092  18.47523  1.000 71.72065  ? 32  GLU B OE1 1 
ATOM   902  O OE2 . GLU B 1 35 ? -1.19107  4.66514  16.54622  1.000 75.02315  ? 32  GLU B OE2 1 
ATOM   903  N N   . GLU B 1 36 ? 3.70014   5.15046  14.32228  1.000 54.41161  ? 33  GLU B N   1 
ATOM   904  C CA  . GLU B 1 36 ? 4.12549   4.44481  13.11751  1.000 58.36043  ? 33  GLU B CA  1 
ATOM   905  C C   . GLU B 1 36 ? 5.63207   4.55628  12.92423  1.000 60.83833  ? 33  GLU B C   1 
ATOM   906  O O   . GLU B 1 36 ? 6.29323   3.57286  12.57035  1.000 62.67629  ? 33  GLU B O   1 
ATOM   907  C CB  . GLU B 1 36 ? 3.38589   4.98000  11.89087  1.000 57.50390  ? 33  GLU B CB  1 
ATOM   908  C CG  . GLU B 1 36 ? 4.04019   4.58342  10.57081  1.000 72.05007  ? 33  GLU B CG  1 
ATOM   909  C CD  . GLU B 1 36 ? 3.06946   4.55838  9.40678   1.000 88.76108  ? 33  GLU B CD  1 
ATOM   910  O OE1 . GLU B 1 36 ? 1.85910   4.76246  9.63419   1.000 99.96579  ? 33  GLU B OE1 1 
ATOM   911  O OE2 . GLU B 1 36 ? 3.51816   4.32747  8.26310   1.000 78.23357  ? 33  GLU B OE2 1 
ATOM   912  N N   . MET B 1 37 ? 6.19284   5.74637  13.15380  1.000 49.92743  ? 34  MET B N   1 
ATOM   913  C CA  . MET B 1 37 ? 7.64128   5.90256  13.08805  1.000 51.00813  ? 34  MET B CA  1 
ATOM   914  C C   . MET B 1 37 ? 8.33317   5.09754  14.17648  1.000 58.34772  ? 34  MET B C   1 
ATOM   915  O O   . MET B 1 37 ? 9.44806   4.60442  13.97183  1.000 64.97724  ? 34  MET B O   1 
ATOM   916  C CB  . MET B 1 37 ? 8.02050   7.37889  13.20095  1.000 52.36244  ? 34  MET B CB  1 
ATOM   917  C CG  . MET B 1 37 ? 7.55371   8.23223  12.03545  1.000 49.84708  ? 34  MET B CG  1 
ATOM   918  S SD  . MET B 1 37 ? 8.08650   9.94685  12.17872  1.000 48.92757  ? 34  MET B SD  1 
ATOM   919  C CE  . MET B 1 37 ? 7.31747   10.40747 13.72443  1.000 43.48366  ? 34  MET B CE  1 
ATOM   920  N N   . GLU B 1 38 ? 7.69059   4.95407  15.33674  1.000 60.81461  ? 35  GLU B N   1 
ATOM   921  C CA  . GLU B 1 38 ? 8.24877   4.11257  16.38835  1.000 71.96850  ? 35  GLU B CA  1 
ATOM   922  C C   . GLU B 1 38 ? 8.15402   2.63819  16.01694  1.000 69.29708  ? 35  GLU B C   1 
ATOM   923  O O   . GLU B 1 38 ? 9.04729   1.85042  16.34914  1.000 70.32788  ? 35  GLU B O   1 
ATOM   924  C CB  . GLU B 1 38 ? 7.53187   4.38236  17.71013  1.000 77.41565  ? 35  GLU B CB  1 
ATOM   925  C CG  . GLU B 1 38 ? 8.29936   3.93166  18.93981  1.000 91.64500  ? 35  GLU B CG  1 
ATOM   926  C CD  . GLU B 1 38 ? 7.49087   4.08310  20.21235  1.000 103.21868 ? 35  GLU B CD  1 
ATOM   927  O OE1 . GLU B 1 38 ? 6.65004   3.20209  20.49246  1.000 102.83089 ? 35  GLU B OE1 1 
ATOM   928  O OE2 . GLU B 1 38 ? 7.68809   5.08866  20.92698  1.000 96.24085  ? 35  GLU B OE2 1 
ATOM   929  N N   . LYS B 1 39 ? 7.07988   2.24715  15.32468  1.000 62.38225  ? 36  LYS B N   1 
ATOM   930  C CA  . LYS B 1 39 ? 6.94812   0.86078  14.88716  1.000 73.22204  ? 36  LYS B CA  1 
ATOM   931  C C   . LYS B 1 39 ? 7.94355   0.54166  13.77786  1.000 73.53605  ? 36  LYS B C   1 
ATOM   932  O O   . LYS B 1 39 ? 8.49629   -0.56365 13.73091  1.000 69.35042  ? 36  LYS B O   1 
ATOM   933  C CB  . LYS B 1 39 ? 5.51231   0.58943  14.43012  1.000 70.19891  ? 36  LYS B CB  1 
ATOM   934  C CG  . LYS B 1 39 ? 5.06830   -0.87022 14.52632  1.000 78.24609  ? 36  LYS B CG  1 
ATOM   935  C CD  . LYS B 1 39 ? 5.46708   -1.68165 13.29907  1.000 87.64043  ? 36  LYS B CD  1 
ATOM   936  C CE  . LYS B 1 39 ? 5.00185   -3.12702 13.41190  1.000 77.33348  ? 36  LYS B CE  1 
ATOM   937  N NZ  . LYS B 1 39 ? 5.37851   -3.92987 12.21422  1.000 80.68466  ? 36  LYS B NZ  1 
ATOM   938  N N   . LYS B 1 40 ? 8.19003   1.49829  12.87993  1.000 64.40975  ? 37  LYS B N   1 
ATOM   939  C CA  . LYS B 1 40 ? 9.19470   1.32976  11.83536  1.000 56.76001  ? 37  LYS B CA  1 
ATOM   940  C C   . LYS B 1 40 ? 10.62163  1.42198  12.36086  1.000 61.32421  ? 37  LYS B C   1 
ATOM   941  O O   . LYS B 1 40 ? 11.56022  1.30511  11.56423  1.000 68.19645  ? 37  LYS B O   1 
ATOM   942  C CB  . LYS B 1 40 ? 8.99188   2.36943  10.73025  1.000 65.11886  ? 37  LYS B CB  1 
ATOM   943  C CG  . LYS B 1 40 ? 8.18756   1.87776  9.53427   1.000 77.64151  ? 37  LYS B CG  1 
ATOM   944  C CD  . LYS B 1 40 ? 6.71507   1.69819  9.86677   1.000 79.04603  ? 37  LYS B CD  1 
ATOM   945  C CE  . LYS B 1 40 ? 5.92278   1.30874  8.62691   1.000 85.60959  ? 37  LYS B CE  1 
ATOM   946  N NZ  . LYS B 1 40 ? 4.45803   1.25438  8.88744   1.000 90.01107  ? 37  LYS B NZ  1 
ATOM   947  N N   . GLY B 1 41 ? 10.81083  1.63212  13.66208  1.000 58.53676  ? 38  GLY B N   1 
ATOM   948  C CA  . GLY B 1 41 ? 12.14562  1.70132  14.22092  1.000 64.77850  ? 38  GLY B CA  1 
ATOM   949  C C   . GLY B 1 41 ? 12.94022  2.92575  13.83175  1.000 66.41959  ? 38  GLY B C   1 
ATOM   950  O O   . GLY B 1 41 ? 14.16829  2.91431  13.94787  1.000 67.65247  ? 38  GLY B O   1 
ATOM   951  N N   . LEU B 1 42 ? 12.27762  3.98417  13.37119  1.000 60.36630  ? 39  LEU B N   1 
ATOM   952  C CA  . LEU B 1 42 ? 12.98079  5.19654  12.97912  1.000 58.19319  ? 39  LEU B CA  1 
ATOM   953  C C   . LEU B 1 42 ? 13.62890  5.85823  14.18945  1.000 54.52385  ? 39  LEU B C   1 
ATOM   954  O O   . LEU B 1 42 ? 13.10260  5.81966  15.30441  1.000 59.09665  ? 39  LEU B O   1 
ATOM   955  C CB  . LEU B 1 42 ? 12.02527  6.17368  12.29547  1.000 62.27359  ? 39  LEU B CB  1 
ATOM   956  C CG  . LEU B 1 42 ? 11.47861  5.73797  10.93550  1.000 60.69950  ? 39  LEU B CG  1 
ATOM   957  C CD1 . LEU B 1 42 ? 10.59154  6.82243  10.34930  1.000 56.70475  ? 39  LEU B CD1 1 
ATOM   958  C CD2 . LEU B 1 42 ? 12.61681  5.39543  9.98474   1.000 69.92883  ? 39  LEU B CD2 1 
ATOM   959  N N   . SER B 1 43 ? 14.78486  6.47442  13.95535  1.000 59.95654  ? 40  SER B N   1 
ATOM   960  C CA  . SER B 1 43 ? 15.55782  7.06584  15.03454  1.000 66.38154  ? 40  SER B CA  1 
ATOM   961  C C   . SER B 1 43 ? 14.87279  8.32575  15.56241  1.000 58.94164  ? 40  SER B C   1 
ATOM   962  O O   . SER B 1 43 ? 13.92086  8.84962  14.97495  1.000 57.10727  ? 40  SER B O   1 
ATOM   963  C CB  . SER B 1 43 ? 16.97431  7.39169  14.56195  1.000 63.50708  ? 40  SER B CB  1 
ATOM   964  O OG  . SER B 1 43 ? 16.95769  8.38749  13.55393  1.000 48.18545  ? 40  SER B OG  1 
ATOM   965  N N   . LYS B 1 44 ? 15.37886  8.81155  16.69922  1.000 59.56266  ? 41  LYS B N   1 
ATOM   966  C CA  . LYS B 1 44 ? 14.83368  10.02589 17.29655  1.000 46.87006  ? 41  LYS B CA  1 
ATOM   967  C C   . LYS B 1 44 ? 15.05938  11.23075 16.39139  1.000 50.83591  ? 41  LYS B C   1 
ATOM   968  O O   . LYS B 1 44 ? 14.20774  12.12401 16.30699  1.000 46.45765  ? 41  LYS B O   1 
ATOM   969  C CB  . LYS B 1 44 ? 15.45789  10.25181 18.67603  1.000 58.16482  ? 41  LYS B CB  1 
ATOM   970  C CG  . LYS B 1 44 ? 14.97560  11.50443 19.38615  1.000 48.00181  ? 41  LYS B CG  1 
ATOM   971  C CD  . LYS B 1 44 ? 15.29245  11.47783 20.87884  1.000 54.87512  ? 41  LYS B CD  1 
ATOM   972  C CE  . LYS B 1 44 ? 16.78986  11.51887 21.14926  1.000 57.51278  ? 41  LYS B CE  1 
ATOM   973  N NZ  . LYS B 1 44 ? 17.41148  12.81222 20.74767  1.000 55.46725  ? 41  LYS B NZ  1 
ATOM   974  N N   . GLU B 1 45 ? 16.19812  11.26726 15.69605  1.000 48.19402  ? 42  GLU B N   1 
ATOM   975  C CA  . GLU B 1 45 ? 16.46275  12.36784 14.77614  1.000 50.56606  ? 42  GLU B CA  1 
ATOM   976  C C   . GLU B 1 45 ? 15.49593  12.34663 13.59863  1.000 45.42199  ? 42  GLU B C   1 
ATOM   977  O O   . GLU B 1 45 ? 15.00142  13.39844 13.17602  1.000 53.93265  ? 42  GLU B O   1 
ATOM   978  C CB  . GLU B 1 45 ? 17.91110  12.31198 14.29070  1.000 52.38162  ? 42  GLU B CB  1 
ATOM   979  C CG  . GLU B 1 45 ? 18.94176  12.66310 15.35812  1.000 63.08760  ? 42  GLU B CG  1 
ATOM   980  C CD  . GLU B 1 45 ? 19.15878  11.54592 16.36016  1.000 59.79142  ? 42  GLU B CD  1 
ATOM   981  O OE1 . GLU B 1 45 ? 19.16065  10.36749 15.94588  1.000 66.54717  ? 42  GLU B OE1 1 
ATOM   982  O OE2 . GLU B 1 45 ? 19.32153  11.84610 17.56196  1.000 59.69455  ? 42  GLU B OE2 1 
ATOM   983  N N   . GLN B 1 46 ? 15.20548  11.15885 13.06189  1.000 50.43656  ? 43  GLN B N   1 
ATOM   984  C CA  . GLN B 1 46 ? 14.24884  11.06485 11.96431  1.000 42.28908  ? 43  GLN B CA  1 
ATOM   985  C C   . GLN B 1 46 ? 12.84508  11.45197 12.40722  1.000 44.07398  ? 43  GLN B C   1 
ATOM   986  O O   . GLN B 1 46 ? 12.09355  12.04400 11.62404  1.000 44.78228  ? 43  GLN B O   1 
ATOM   987  C CB  . GLN B 1 46 ? 14.25060  9.65363  11.38260  1.000 50.95080  ? 43  GLN B CB  1 
ATOM   988  C CG  . GLN B 1 46 ? 15.55856  9.26735  10.72471  1.000 50.85570  ? 43  GLN B CG  1 
ATOM   989  C CD  . GLN B 1 46 ? 15.54544  7.84561  10.21401  1.000 60.10612  ? 43  GLN B CD  1 
ATOM   990  O OE1 . GLN B 1 46 ? 15.41957  6.89718  10.98829  1.000 72.08973  ? 43  GLN B OE1 1 
ATOM   991  N NE2 . GLN B 1 46 ? 15.66641  7.68797  8.90153   1.000 67.56494  ? 43  GLN B NE2 1 
ATOM   992  N N   . VAL B 1 47 ? 12.47367  11.12904 13.64820  1.000 48.15252  ? 44  VAL B N   1 
ATOM   993  C CA  . VAL B 1 47 ? 11.17643  11.55484 14.16819  1.000 38.92063  ? 44  VAL B CA  1 
ATOM   994  C C   . VAL B 1 47 ? 11.08884  13.07421 14.17829  1.000 42.26759  ? 44  VAL B C   1 
ATOM   995  O O   . VAL B 1 47 ? 10.10811  13.66125 13.70529  1.000 40.22631  ? 44  VAL B O   1 
ATOM   996  C CB  . VAL B 1 47 ? 10.93754  10.96482 15.56980  1.000 40.75497  ? 44  VAL B CB  1 
ATOM   997  C CG1 . VAL B 1 47 ? 9.71510   11.60131 16.21327  1.000 36.97181  ? 44  VAL B CG1 1 
ATOM   998  C CG2 . VAL B 1 47 ? 10.77104  9.45608  15.48767  1.000 43.22946  ? 44  VAL B CG2 1 
ATOM   999  N N   . ILE B 1 48 ? 12.12252  13.73461 14.70686  1.000 44.47682  ? 45  ILE B N   1 
ATOM   1000 C CA  . ILE B 1 48 ? 12.14702  15.19520 14.73387  1.000 39.28349  ? 45  ILE B CA  1 
ATOM   1001 C C   . ILE B 1 48 ? 12.05418  15.75569 13.31987  1.000 39.83843  ? 45  ILE B C   1 
ATOM   1002 O O   . ILE B 1 48 ? 11.26768  16.66946 13.04584  1.000 42.62566  ? 45  ILE B O   1 
ATOM   1003 C CB  . ILE B 1 48 ? 13.41045  15.69744 15.45487  1.000 45.20846  ? 45  ILE B CB  1 
ATOM   1004 C CG1 . ILE B 1 48 ? 13.37444  15.29671 16.93001  1.000 47.94747  ? 45  ILE B CG1 1 
ATOM   1005 C CG2 . ILE B 1 48 ? 13.55091  17.20797 15.30162  1.000 42.81289  ? 45  ILE B CG2 1 
ATOM   1006 C CD1 . ILE B 1 48 ? 14.63063  15.65387 17.69474  1.000 47.82485  ? 45  ILE B CD1 1 
ATOM   1007 N N   . LEU B 1 49 ? 12.85584  15.21075 12.40015  1.000 39.45941  ? 46  LEU B N   1 
ATOM   1008 C CA  . LEU B 1 49 ? 12.85270  15.70560 11.02557  1.000 50.24299  ? 46  LEU B CA  1 
ATOM   1009 C C   . LEU B 1 49 ? 11.48911  15.52967 10.37305  1.000 36.70766  ? 46  LEU B C   1 
ATOM   1010 O O   . LEU B 1 49 ? 10.99596  16.43897 9.69599   1.000 37.27365  ? 46  LEU B O   1 
ATOM   1011 C CB  . LEU B 1 49 ? 13.92563  14.99251 10.20440  1.000 35.87081  ? 46  LEU B CB  1 
ATOM   1012 C CG  . LEU B 1 49 ? 15.35460  15.51270 10.34029  1.000 38.13731  ? 46  LEU B CG  1 
ATOM   1013 C CD1 . LEU B 1 49 ? 16.30215  14.58268 9.61798   1.000 49.72192  ? 46  LEU B CD1 1 
ATOM   1014 C CD2 . LEU B 1 49 ? 15.45795  16.92192 9.78400   1.000 37.02571  ? 46  LEU B CD2 1 
ATOM   1015 N N   . LEU B 1 50 ? 10.86344  14.36677 10.56549  1.000 38.50617  ? 47  LEU B N   1 
ATOM   1016 C CA  . LEU B 1 50 ? 9.55902   14.12755 9.95915   1.000 44.56006  ? 47  LEU B CA  1 
ATOM   1017 C C   . LEU B 1 50 ? 8.47034   14.95178 10.62940  1.000 38.53453  ? 47  LEU B C   1 
ATOM   1018 O O   . LEU B 1 50 ? 7.53205   15.39367 9.95857   1.000 41.14795  ? 47  LEU B O   1 
ATOM   1019 C CB  . LEU B 1 50 ? 9.21548   12.63892 10.01351  1.000 36.16018  ? 47  LEU B CB  1 
ATOM   1020 C CG  . LEU B 1 50 ? 9.58609   11.82280 8.77343   1.000 48.85543  ? 47  LEU B CG  1 
ATOM   1021 C CD1 . LEU B 1 50 ? 8.63371   12.12277 7.62873   1.000 56.03735  ? 47  LEU B CD1 1 
ATOM   1022 C CD2 . LEU B 1 50 ? 11.01532  12.10688 8.35140   1.000 54.82544  ? 47  LEU B CD2 1 
ATOM   1023 N N   . LEU B 1 51 ? 8.57656   15.17507 11.94125  1.000 41.12972  ? 48  LEU B N   1 
ATOM   1024 C CA  . LEU B 1 51 ? 7.59619   16.01625 12.61886  1.000 41.00958  ? 48  LEU B CA  1 
ATOM   1025 C C   . LEU B 1 51 ? 7.75451   17.48446 12.24081  1.000 49.59840  ? 48  LEU B C   1 
ATOM   1026 O O   . LEU B 1 51 ? 6.77640   18.23908 12.28205  1.000 47.88860  ? 48  LEU B O   1 
ATOM   1027 C CB  . LEU B 1 51 ? 7.69988   15.83664 14.13246  1.000 40.76277  ? 48  LEU B CB  1 
ATOM   1028 C CG  . LEU B 1 51 ? 7.17252   14.50953 14.68201  1.000 39.60009  ? 48  LEU B CG  1 
ATOM   1029 C CD1 . LEU B 1 51 ? 7.31433   14.46461 16.19264  1.000 40.09330  ? 48  LEU B CD1 1 
ATOM   1030 C CD2 . LEU B 1 51 ? 5.72447   14.28470 14.27027  1.000 38.73102  ? 48  LEU B CD2 1 
ATOM   1031 N N   . ILE B 1 52 ? 8.96609   17.91490 11.87883  1.000 47.96363  ? 49  ILE B N   1 
ATOM   1032 C CA  . ILE B 1 52 ? 9.12220   19.26072 11.33305  1.000 51.09573  ? 49  ILE B CA  1 
ATOM   1033 C C   . ILE B 1 52 ? 8.60860   19.30769 9.90055   1.000 48.04331  ? 49  ILE B C   1 
ATOM   1034 O O   . ILE B 1 52 ? 7.94389   20.26844 9.49455   1.000 42.58676  ? 49  ILE B O   1 
ATOM   1035 C CB  . ILE B 1 52 ? 10.58690  19.72371 11.42353  1.000 42.47129  ? 49  ILE B CB  1 
ATOM   1036 C CG1 . ILE B 1 52 ? 11.04172  19.77927 12.88336  1.000 52.28898  ? 49  ILE B CG1 1 
ATOM   1037 C CG2 . ILE B 1 52 ? 10.75471  21.07274 10.74860  1.000 39.92324  ? 49  ILE B CG2 1 
ATOM   1038 C CD1 . ILE B 1 52 ? 10.06602  20.46538 13.80791  1.000 55.20098  ? 49  ILE B CD1 1 
ATOM   1039 N N   . HIS B 1 53 ? 8.91669   18.27423 9.11210   1.000 42.75634  ? 50  HIS B N   1 
ATOM   1040 C CA  . HIS B 1 53 ? 8.26571   18.10497 7.81732   1.000 53.60433  ? 50  HIS B CA  1 
ATOM   1041 C C   . HIS B 1 53 ? 6.75146   18.06740 7.97307   1.000 50.57714  ? 50  HIS B C   1 
ATOM   1042 O O   . HIS B 1 53 ? 6.01797   18.56788 7.11284   1.000 53.47911  ? 50  HIS B O   1 
ATOM   1043 C CB  . HIS B 1 53 ? 8.77844   16.83025 7.14626   1.000 53.76476  ? 50  HIS B CB  1 
ATOM   1044 C CG  . HIS B 1 53 ? 7.87815   16.30060 6.07300   1.000 56.29141  ? 50  HIS B CG  1 
ATOM   1045 N ND1 . HIS B 1 53 ? 7.18237   15.11763 6.20456   1.000 56.96134  ? 50  HIS B ND1 1 
ATOM   1046 C CD2 . HIS B 1 53 ? 7.56402   16.78729 4.84942   1.000 63.48537  ? 50  HIS B CD2 1 
ATOM   1047 C CE1 . HIS B 1 53 ? 6.47545   14.90065 5.10989   1.000 60.39979  ? 50  HIS B CE1 1 
ATOM   1048 N NE2 . HIS B 1 53 ? 6.69010   15.89793 4.27109   1.000 68.24926  ? 50  HIS B NE2 1 
ATOM   1049 N N   . PHE B 1 54 ? 6.26539   17.47680 9.06727   1.000 49.97394  ? 51  PHE B N   1 
ATOM   1050 C CA  . PHE B 1 54 ? 4.84659   17.55811 9.39474   1.000 51.94047  ? 51  PHE B CA  1 
ATOM   1051 C C   . PHE B 1 54 ? 4.43134   19.00404 9.63903   1.000 55.29473  ? 51  PHE B C   1 
ATOM   1052 O O   . PHE B 1 54 ? 3.38807   19.45538 9.15453   1.000 51.49509  ? 51  PHE B O   1 
ATOM   1053 C CB  . PHE B 1 54 ? 4.54314   16.69164 10.62124  1.000 46.93832  ? 51  PHE B CB  1 
ATOM   1054 C CG  . PHE B 1 54 ? 3.14711   16.85068 11.14971  1.000 39.06658  ? 51  PHE B CG  1 
ATOM   1055 C CD1 . PHE B 1 54 ? 2.84649   17.84165 12.07173  1.000 45.09309  ? 51  PHE B CD1 1 
ATOM   1056 C CD2 . PHE B 1 54 ? 2.13724   16.00147 10.73465  1.000 45.84346  ? 51  PHE B CD2 1 
ATOM   1057 C CE1 . PHE B 1 54 ? 1.56161   17.99416 12.55075  1.000 56.44358  ? 51  PHE B CE1 1 
ATOM   1058 C CE2 . PHE B 1 54 ? 0.85084   16.14653 11.21591  1.000 47.34748  ? 51  PHE B CE2 1 
ATOM   1059 C CZ  . PHE B 1 54 ? 0.56299   17.14248 12.12486  1.000 50.29188  ? 51  PHE B CZ  1 
ATOM   1060 N N   . LEU B 1 55 ? 5.24019   19.74360 10.40468  1.000 48.30310  ? 52  LEU B N   1 
ATOM   1061 C CA  . LEU B 1 55 ? 4.91325   21.13604 10.69681  1.000 55.93528  ? 52  LEU B CA  1 
ATOM   1062 C C   . LEU B 1 55 ? 4.89646   21.98610 9.43276   1.000 58.56879  ? 52  LEU B C   1 
ATOM   1063 O O   . LEU B 1 55 ? 4.11415   22.93849 9.33508   1.000 69.87438  ? 52  LEU B O   1 
ATOM   1064 C CB  . LEU B 1 55 ? 5.90322   21.70807 11.71347  1.000 54.84250  ? 52  LEU B CB  1 
ATOM   1065 C CG  . LEU B 1 55 ? 5.81974   21.19733 13.15504  1.000 51.53412  ? 52  LEU B CG  1 
ATOM   1066 C CD1 . LEU B 1 55 ? 6.79321   21.93632 14.06607  1.000 54.32362  ? 52  LEU B CD1 1 
ATOM   1067 C CD2 . LEU B 1 55 ? 4.40773   21.32347 13.68335  1.000 53.11921  ? 52  LEU B CD2 1 
ATOM   1068 N N   . LEU B 1 56 ? 5.74157   21.65661 8.45440   1.000 58.05268  ? 53  LEU B N   1 
ATOM   1069 C CA  . LEU B 1 56 ? 5.70499   22.36603 7.18004   1.000 64.21490  ? 53  LEU B CA  1 
ATOM   1070 C C   . LEU B 1 56 ? 4.42770   22.05339 6.41160   1.000 74.21558  ? 53  LEU B C   1 
ATOM   1071 O O   . LEU B 1 56 ? 3.81776   22.94974 5.81771   1.000 77.55258  ? 53  LEU B O   1 
ATOM   1072 C CB  . LEU B 1 56 ? 6.93273   22.00447 6.34633   1.000 69.80404  ? 53  LEU B CB  1 
ATOM   1073 C CG  . LEU B 1 56 ? 8.27840   22.38310 6.96295   1.000 67.80123  ? 53  LEU B CG  1 
ATOM   1074 C CD1 . LEU B 1 56 ? 9.39933   21.61433 6.29056   1.000 66.26707  ? 53  LEU B CD1 1 
ATOM   1075 C CD2 . LEU B 1 56 ? 8.50654   23.88129 6.84723   1.000 66.23449  ? 53  LEU B CD2 1 
ATOM   1076 N N   . LEU B 1 57 ? 4.00955   20.78630 6.40972   1.000 64.03184  ? 54  LEU B N   1 
ATOM   1077 C CA  . LEU B 1 57 ? 2.80018   20.40556 5.68830   1.000 70.55269  ? 54  LEU B CA  1 
ATOM   1078 C C   . LEU B 1 57 ? 1.58004   21.13056 6.23653   1.000 62.97428  ? 54  LEU B C   1 
ATOM   1079 O O   . LEU B 1 57 ? 0.72695   21.59512 5.47132   1.000 72.50813  ? 54  LEU B O   1 
ATOM   1080 C CB  . LEU B 1 57 ? 2.60275   18.89216 5.76468   1.000 59.06373  ? 54  LEU B CB  1 
ATOM   1081 C CG  . LEU B 1 57 ? 3.16459   18.03326 4.63088   1.000 63.23534  ? 54  LEU B CG  1 
ATOM   1082 C CD1 . LEU B 1 57 ? 4.56201   18.47682 4.24134   1.000 66.50151  ? 54  LEU B CD1 1 
ATOM   1083 C CD2 . LEU B 1 57 ? 3.16245   16.56583 5.03184   1.000 58.43299  ? 54  LEU B CD2 1 
ATOM   1084 N N   . SER B 1 58 ? 1.48517   21.24542 7.56046   1.000 65.11714  ? 55  SER B N   1 
ATOM   1085 C CA  . SER B 1 58 ? 0.33243   21.88217 8.17972   1.000 73.41945  ? 55  SER B CA  1 
ATOM   1086 C C   . SER B 1 58 ? 0.35759   23.40086 8.06727   1.000 82.62307  ? 55  SER B C   1 
ATOM   1087 O O   . SER B 1 58 ? -0.68942  24.03475 8.23921   1.000 84.14404  ? 55  SER B O   1 
ATOM   1088 C CB  . SER B 1 58 ? 0.24449   21.48225 9.65449   1.000 77.69774  ? 55  SER B CB  1 
ATOM   1089 O OG  . SER B 1 58 ? 1.39573   21.90062 10.36743  1.000 82.02166  ? 55  SER B OG  1 
ATOM   1090 N N   . LEU B 1 59 ? 1.51474   23.99940 7.77994   1.000 84.91168  ? 56  LEU B N   1 
ATOM   1091 C CA  . LEU B 1 59 ? 1.63157   25.45223 7.84132   1.000 75.27416  ? 56  LEU B CA  1 
ATOM   1092 C C   . LEU B 1 59 ? 1.94467   26.08231 6.48777   1.000 75.54031  ? 56  LEU B C   1 
ATOM   1093 O O   . LEU B 1 59 ? 1.04971   26.63378 5.83701   1.000 77.43356  ? 56  LEU B O   1 
ATOM   1094 C CB  . LEU B 1 59 ? 2.69786   25.85141 8.86340   1.000 74.16960  ? 56  LEU B CB  1 
ATOM   1095 C CG  . LEU B 1 59 ? 2.65750   27.32810 9.24856   1.000 78.73745  ? 56  LEU B CG  1 
ATOM   1096 C CD1 . LEU B 1 59 ? 1.23187   27.72955 9.58492   1.000 79.22625  ? 56  LEU B CD1 1 
ATOM   1097 C CD2 . LEU B 1 59 ? 3.58360   27.60485 10.41741  1.000 82.14761  ? 56  LEU B CD2 1 
ATOM   1098 N N   . VAL B 1 60 ? 3.21004   26.01806 6.06022   1.000 76.66597  ? 57  VAL B N   1 
ATOM   1099 C CA  . VAL B 1 60 ? 3.61143   26.70161 4.83110   1.000 81.00515  ? 57  VAL B CA  1 
ATOM   1100 C C   . VAL B 1 60 ? 2.85311   26.14045 3.63504   1.000 77.49109  ? 57  VAL B C   1 
ATOM   1101 O O   . VAL B 1 60 ? 2.49981   26.87486 2.70373   1.000 86.23456  ? 57  VAL B O   1 
ATOM   1102 C CB  . VAL B 1 60 ? 5.13953   26.61923 4.63571   1.000 70.75401  ? 57  VAL B CB  1 
ATOM   1103 C CG1 . VAL B 1 60 ? 5.62469   25.18400 4.68753   1.000 68.97362  ? 57  VAL B CG1 1 
ATOM   1104 C CG2 . VAL B 1 60 ? 5.55064   27.27630 3.32016   1.000 76.85540  ? 57  VAL B CG2 1 
ATOM   1105 N N   . LYS B 1 61 ? 2.57252   24.83941 3.64725   1.000 81.89884  ? 58  LYS B N   1 
ATOM   1106 C CA  . LYS B 1 61 ? 1.73098   24.24884 2.61823   1.000 80.01574  ? 58  LYS B CA  1 
ATOM   1107 C C   . LYS B 1 61 ? 0.24873   24.32978 2.95417   1.000 72.29339  ? 58  LYS B C   1 
ATOM   1108 O O   . LYS B 1 61 ? -0.58223  24.27435 2.04043   1.000 68.80539  ? 58  LYS B O   1 
ATOM   1109 C CB  . LYS B 1 61 ? 2.13422   22.79078 2.37669   1.000 73.31623  ? 58  LYS B CB  1 
ATOM   1110 C CG  . LYS B 1 61 ? 3.44349   22.63846 1.61207   1.000 71.58546  ? 58  LYS B CG  1 
ATOM   1111 C CD  . LYS B 1 61 ? 3.38357   23.37527 0.27947   1.000 70.22002  ? 58  LYS B CD  1 
ATOM   1112 C CE  . LYS B 1 61 ? 4.67225   23.21611 -0.51348  1.000 68.13753  ? 58  LYS B CE  1 
ATOM   1113 N NZ  . LYS B 1 61 ? 4.60526   23.92565 -1.82320  1.000 65.37320  ? 58  LYS B NZ  1 
ATOM   1114 N N   . GLY B 1 62 ? -0.09862  24.47669 4.23125   1.000 70.32067  ? 59  GLY B N   1 
ATOM   1115 C CA  . GLY B 1 62 ? -1.49212  24.62895 4.61529   1.000 73.45964  ? 59  GLY B CA  1 
ATOM   1116 C C   . GLY B 1 62 ? -2.35122  23.42527 4.30839   1.000 63.00836  ? 59  GLY B C   1 
ATOM   1117 O O   . GLY B 1 62 ? -3.55018  23.57428 4.04801   1.000 66.57736  ? 59  GLY B O   1 
ATOM   1118 N N   . LEU B 1 63 ? -1.76884  22.23167 4.33120   1.000 63.61559  ? 60  LEU B N   1 
ATOM   1119 C CA  . LEU B 1 63 ? -2.49998  21.01954 4.00297   1.000 62.20835  ? 60  LEU B CA  1 
ATOM   1120 C C   . LEU B 1 63 ? -3.32938  20.55056 5.19104   1.000 58.30102  ? 60  LEU B C   1 
ATOM   1121 O O   . LEU B 1 63 ? -2.94249  20.71491 6.35159   1.000 61.52001  ? 60  LEU B O   1 
ATOM   1122 C CB  . LEU B 1 63 ? -1.53318  19.91840 3.57312   1.000 52.26944  ? 60  LEU B CB  1 
ATOM   1123 C CG  . LEU B 1 63 ? -0.61247  20.30633 2.41697   1.000 61.37775  ? 60  LEU B CG  1 
ATOM   1124 C CD1 . LEU B 1 63 ? 0.35938   19.18705 2.11140   1.000 50.44378  ? 60  LEU B CD1 1 
ATOM   1125 C CD2 . LEU B 1 63 ? -1.42978  20.65953 1.18757   1.000 61.07113  ? 60  LEU B CD2 1 
ATOM   1126 N N   . SER B 1 64 ? -4.48113  19.95201 4.88461   1.000 48.93949  ? 61  SER B N   1 
ATOM   1127 C CA  . SER B 1 64 ? -5.38331  19.47415 5.91728   1.000 54.81826  ? 61  SER B CA  1 
ATOM   1128 C C   . SER B 1 64 ? -4.72326  18.36351 6.73634   1.000 61.32208  ? 61  SER B C   1 
ATOM   1129 O O   . SER B 1 64 ? -3.73675  17.75912 6.30467   1.000 44.50190  ? 61  SER B O   1 
ATOM   1130 C CB  . SER B 1 64 ? -6.68149  18.96869 5.28758   1.000 58.11910  ? 61  SER B CB  1 
ATOM   1131 O OG  . SER B 1 64 ? -6.45743  17.79907 4.52145   1.000 52.70855  ? 61  SER B OG  1 
ATOM   1132 N N   . PRO B 1 65 ? -5.24393  18.09134 7.93848   1.000 55.53429  ? 62  PRO B N   1 
ATOM   1133 C CA  . PRO B 1 65 ? -4.68924  16.98074 8.73145   1.000 56.35812  ? 62  PRO B CA  1 
ATOM   1134 C C   . PRO B 1 65 ? -4.74241  15.64231 8.01760   1.000 48.73288  ? 62  PRO B C   1 
ATOM   1135 O O   . PRO B 1 65 ? -3.80407  14.84490 8.14091   1.000 46.19116  ? 62  PRO B O   1 
ATOM   1136 C CB  . PRO B 1 65 ? -5.56128  16.99366 9.99398   1.000 58.53460  ? 62  PRO B CB  1 
ATOM   1137 C CG  . PRO B 1 65 ? -6.00915  18.40429 10.11387  1.000 56.69700  ? 62  PRO B CG  1 
ATOM   1138 C CD  . PRO B 1 65 ? -6.21995  18.88224 8.70847   1.000 52.96226  ? 62  PRO B CD  1 
ATOM   1139 N N   . GLU B 1 66 ? -5.81488  15.37344 7.26914   1.000 44.96602  ? 63  GLU B N   1 
ATOM   1140 C CA  . GLU B 1 66 ? -5.89741  14.12336 6.52182   1.000 50.91258  ? 63  GLU B CA  1 
ATOM   1141 C C   . GLU B 1 66 ? -4.87372  14.09734 5.39360   1.000 52.22934  ? 63  GLU B C   1 
ATOM   1142 O O   . GLU B 1 66 ? -4.17495  13.09643 5.19755   1.000 50.24605  ? 63  GLU B O   1 
ATOM   1143 C CB  . GLU B 1 66 ? -7.31313  13.92719 5.97564   1.000 47.71092  ? 63  GLU B CB  1 
ATOM   1144 C CG  . GLU B 1 66 ? -7.49828  12.62383 5.22741   1.000 66.39159  ? 63  GLU B CG  1 
ATOM   1145 C CD  . GLU B 1 66 ? -7.28402  11.41195 6.11284   1.000 71.17849  ? 63  GLU B CD  1 
ATOM   1146 O OE1 . GLU B 1 66 ? -7.56386  11.50246 7.32603   1.000 63.62751  ? 63  GLU B OE1 1 
ATOM   1147 O OE2 . GLU B 1 66 ? -6.83002  10.36872 5.59912   1.000 78.98592  ? 63  GLU B OE2 1 
ATOM   1148 N N   . THR B 1 67 ? -4.77430  15.19434 4.63756   1.000 53.09258  ? 64  THR B N   1 
ATOM   1149 C CA  . THR B 1 67 ? -3.77243  15.28521 3.57892   1.000 51.52155  ? 64  THR B CA  1 
ATOM   1150 C C   . THR B 1 67 ? -2.36235  15.17356 4.14371   1.000 46.08179  ? 64  THR B C   1 
ATOM   1151 O O   . THR B 1 67 ? -1.51452  14.46330 3.58887   1.000 42.43466  ? 64  THR B O   1 
ATOM   1152 C CB  . THR B 1 67 ? -3.93698  16.60044 2.81689   1.000 53.51303  ? 64  THR B CB  1 
ATOM   1153 O OG1 . THR B 1 67 ? -5.13461  16.55431 2.03423   1.000 59.25549  ? 64  THR B OG1 1 
ATOM   1154 C CG2 . THR B 1 67 ? -2.74635  16.85194 1.90546   1.000 55.11702  ? 64  THR B CG2 1 
ATOM   1155 N N   . THR B 1 68 ? -2.09797  15.86319 5.25422   1.000 43.14431  ? 65  THR B N   1 
ATOM   1156 C CA  . THR B 1 68 ? -0.78582  15.78654 5.88495   1.000 44.94513  ? 65  THR B CA  1 
ATOM   1157 C C   . THR B 1 68 ? -0.48728  14.37360 6.36647   1.000 48.85508  ? 65  THR B C   1 
ATOM   1158 O O   . THR B 1 68 ? 0.63710   13.88325 6.21426   1.000 48.39888  ? 65  THR B O   1 
ATOM   1159 C CB  . THR B 1 68 ? -0.70949  16.77233 7.04834   1.000 46.12262  ? 65  THR B CB  1 
ATOM   1160 O OG1 . THR B 1 68 ? -0.85865  18.10716 6.55274   1.000 52.69988  ? 65  THR B OG1 1 
ATOM   1161 C CG2 . THR B 1 68 ? 0.62312   16.65212 7.75653   1.000 46.38418  ? 65  THR B CG2 1 
ATOM   1162 N N   . LYS B 1 69 ? -1.48788  13.69835 6.93724   1.000 43.68263  ? 66  LYS B N   1 
ATOM   1163 C CA  . LYS B 1 69 ? -1.28103  12.33936 7.42717   1.000 46.43000  ? 66  LYS B CA  1 
ATOM   1164 C C   . LYS B 1 69 ? -0.89287  11.39502 6.29551   1.000 46.19566  ? 66  LYS B C   1 
ATOM   1165 O O   . LYS B 1 69 ? -0.02549  10.53021 6.46903   1.000 51.68347  ? 66  LYS B O   1 
ATOM   1166 C CB  . LYS B 1 69 ? -2.54237  11.84206 8.13340   1.000 50.82211  ? 66  LYS B CB  1 
ATOM   1167 C CG  . LYS B 1 69 ? -2.33566  10.58325 8.95810   1.000 50.92316  ? 66  LYS B CG  1 
ATOM   1168 C CD  . LYS B 1 69 ? -3.58421  10.23158 9.74992   1.000 60.47788  ? 66  LYS B CD  1 
ATOM   1169 C CE  . LYS B 1 69 ? -4.75641  9.92756  8.83232   1.000 62.21174  ? 66  LYS B CE  1 
ATOM   1170 N NZ  . LYS B 1 69 ? -5.98442  9.58508  9.60263   1.000 67.96204  ? 66  LYS B NZ  1 
ATOM   1171 N N   . LEU B 1 70 ? -1.52521  11.54561 5.12859   1.000 47.63051  ? 67  LEU B N   1 
ATOM   1172 C CA  . LEU B 1 70 ? -1.21067  10.68375 3.99263   1.000 46.96990  ? 67  LEU B CA  1 
ATOM   1173 C C   . LEU B 1 70 ? 0.22917   10.88172 3.53925   1.000 42.96881  ? 67  LEU B C   1 
ATOM   1174 O O   . LEU B 1 70 ? 0.97429   9.91213  3.35645   1.000 51.42036  ? 67  LEU B O   1 
ATOM   1175 C CB  . LEU B 1 70 ? -2.17782  10.96020 2.84173   1.000 44.35295  ? 67  LEU B CB  1 
ATOM   1176 C CG  . LEU B 1 70 ? -3.66764  10.74560 3.11480   1.000 56.33158  ? 67  LEU B CG  1 
ATOM   1177 C CD1 . LEU B 1 70 ? -4.49827  11.57134 2.15065   1.000 60.33857  ? 67  LEU B CD1 1 
ATOM   1178 C CD2 . LEU B 1 70 ? -4.04067  9.27229  3.01794   1.000 59.34632  ? 67  LEU B CD2 1 
ATOM   1179 N N   . LEU B 1 71 ? 0.63868   12.13891 3.35377   1.000 44.63686  ? 68  LEU B N   1 
ATOM   1180 C CA  . LEU B 1 71 ? 2.01436   12.42119 2.96087   1.000 40.90749  ? 68  LEU B CA  1 
ATOM   1181 C C   . LEU B 1 71 ? 3.01128   11.97045 4.01730   1.000 44.74456  ? 68  LEU B C   1 
ATOM   1182 O O   . LEU B 1 71 ? 4.11479   11.53382 3.67270   1.000 45.89467  ? 68  LEU B O   1 
ATOM   1183 C CB  . LEU B 1 71 ? 2.18624   13.91093 2.68355   1.000 46.97885  ? 68  LEU B CB  1 
ATOM   1184 C CG  . LEU B 1 71 ? 1.44154   14.45787 1.47060   1.000 50.67292  ? 68  LEU B CG  1 
ATOM   1185 C CD1 . LEU B 1 71 ? 1.63260   15.95039 1.39022   1.000 51.62093  ? 68  LEU B CD1 1 
ATOM   1186 C CD2 . LEU B 1 71 ? 1.93589   13.77892 0.20677   1.000 48.96550  ? 68  LEU B CD2 1 
ATOM   1187 N N   . MET B 1 72 ? 2.65486   12.09166 5.29779   1.000 45.63360  ? 69  MET B N   1 
ATOM   1188 C CA  . MET B 1 72 ? 3.51930   11.59151 6.35923   1.000 42.02554  ? 69  MET B CA  1 
ATOM   1189 C C   . MET B 1 72 ? 3.69203   10.08496 6.24799   1.000 47.27814  ? 69  MET B C   1 
ATOM   1190 O O   . MET B 1 72 ? 4.81705   9.57591  6.27358   1.000 53.06912  ? 69  MET B O   1 
ATOM   1191 C CB  . MET B 1 72 ? 2.94663   11.97481 7.72303   1.000 48.11139  ? 69  MET B CB  1 
ATOM   1192 C CG  . MET B 1 72 ? 3.10134   13.44884 8.04923   1.000 37.49863  ? 69  MET B CG  1 
ATOM   1193 S SD  . MET B 1 72 ? 4.82268   13.96475 7.95886   1.000 60.07656  ? 69  MET B SD  1 
ATOM   1194 C CE  . MET B 1 72 ? 5.54759   12.93752 9.23600   1.000 48.93563  ? 69  MET B CE  1 
ATOM   1195 N N   . LYS B 1 73 ? 2.58013   9.35506  6.12123   1.000 47.20298  ? 70  LYS B N   1 
ATOM   1196 C CA  . LYS B 1 73 ? 2.65072   7.90455  5.96855   1.000 53.52061  ? 70  LYS B CA  1 
ATOM   1197 C C   . LYS B 1 73 ? 3.45939   7.51296  4.73864   1.000 51.49382  ? 70  LYS B C   1 
ATOM   1198 O O   . LYS B 1 73 ? 4.16196   6.49522  4.74572   1.000 56.91596  ? 70  LYS B O   1 
ATOM   1199 C CB  . LYS B 1 73 ? 1.24215   7.31984  5.88152   1.000 45.89614  ? 70  LYS B CB  1 
ATOM   1200 C CG  . LYS B 1 73 ? 0.44329   7.38396  7.17101   1.000 53.38001  ? 70  LYS B CG  1 
ATOM   1201 C CD  . LYS B 1 73 ? -1.04327  7.25086  6.87428   1.000 63.99320  ? 70  LYS B CD  1 
ATOM   1202 C CE  . LYS B 1 73 ? -1.86184  7.05321  8.13857   1.000 70.90942  ? 70  LYS B CE  1 
ATOM   1203 N NZ  . LYS B 1 73 ? -1.71649  5.67610  8.68393   1.000 74.70759  ? 70  LYS B NZ  1 
ATOM   1204 N N   . GLU B 1 74 ? 3.37478   8.30866  3.67166   1.000 47.41403  ? 71  GLU B N   1 
ATOM   1205 C CA  . GLU B 1 74 ? 4.09010   7.97085  2.44599   1.000 55.30764  ? 71  GLU B CA  1 
ATOM   1206 C C   . GLU B 1 74 ? 5.59439   8.12583  2.62483   1.000 54.15004  ? 71  GLU B C   1 
ATOM   1207 O O   . GLU B 1 74 ? 6.36744   7.24182  2.23872   1.000 53.66432  ? 71  GLU B O   1 
ATOM   1208 C CB  . GLU B 1 74 ? 3.58772   8.83102  1.28675   1.000 55.48315  ? 71  GLU B CB  1 
ATOM   1209 C CG  . GLU B 1 74 ? 2.27147   8.35175  0.70401   1.000 64.10074  ? 71  GLU B CG  1 
ATOM   1210 C CD  . GLU B 1 74 ? 2.36688   6.94412  0.14745   1.000 72.46224  ? 71  GLU B CD  1 
ATOM   1211 O OE1 . GLU B 1 74 ? 3.43452   6.58931  -0.39572  1.000 79.77864  ? 71  GLU B OE1 1 
ATOM   1212 O OE2 . GLU B 1 74 ? 1.37883   6.18930  0.25888   1.000 69.83152  ? 71  GLU B OE2 1 
ATOM   1213 N N   . LEU B 1 75 ? 6.03075   9.24180  3.21376   1.000 42.93552  ? 72  LEU B N   1 
ATOM   1214 C CA  . LEU B 1 75 ? 7.45885   9.43259  3.44059   1.000 56.51468  ? 72  LEU B CA  1 
ATOM   1215 C C   . LEU B 1 75 ? 8.00671   8.43087  4.44852   1.000 56.52975  ? 72  LEU B C   1 
ATOM   1216 O O   . LEU B 1 75 ? 9.18417   8.06266  4.37187   1.000 60.78928  ? 72  LEU B O   1 
ATOM   1217 C CB  . LEU B 1 75 ? 7.74168   10.86334 3.89941   1.000 43.01795  ? 72  LEU B CB  1 
ATOM   1218 C CG  . LEU B 1 75 ? 8.05456   11.86781 2.78439   1.000 67.10050  ? 72  LEU B CG  1 
ATOM   1219 C CD1 . LEU B 1 75 ? 6.80320   12.26210 2.00684   1.000 66.24681  ? 72  LEU B CD1 1 
ATOM   1220 C CD2 . LEU B 1 75 ? 8.76548   13.09446 3.33788   1.000 69.64884  ? 72  LEU B CD2 1 
ATOM   1221 N N   . ILE B 1 76 ? 7.17896   7.97939  5.39406   1.000 52.61903  ? 73  ILE B N   1 
ATOM   1222 C CA  . ILE B 1 76 ? 7.60920   6.91902  6.30115   1.000 62.46188  ? 73  ILE B CA  1 
ATOM   1223 C C   . ILE B 1 76 ? 7.85904   5.63074  5.52711   1.000 51.15030  ? 73  ILE B C   1 
ATOM   1224 O O   . ILE B 1 76 ? 8.82245   4.90316  5.79643   1.000 63.86604  ? 73  ILE B O   1 
ATOM   1225 C CB  . ILE B 1 76 ? 6.57263   6.72060  7.42231   1.000 48.10170  ? 73  ILE B CB  1 
ATOM   1226 C CG1 . ILE B 1 76 ? 6.53726   7.94804  8.33471   1.000 50.81286  ? 73  ILE B CG1 1 
ATOM   1227 C CG2 . ILE B 1 76 ? 6.88421   5.46849  8.22833   1.000 56.93126  ? 73  ILE B CG2 1 
ATOM   1228 C CD1 . ILE B 1 76 ? 5.30828   8.02223  9.21240   1.000 49.28459  ? 73  ILE B CD1 1 
ATOM   1229 N N   . LYS B 1 77 ? 7.00851   5.33839  4.54098   1.000 47.33993  ? 74  LYS B N   1 
ATOM   1230 C CA  . LYS B 1 77 ? 7.20987   4.15347  3.71498   1.000 57.09523  ? 74  LYS B CA  1 
ATOM   1231 C C   . LYS B 1 77 ? 8.42658   4.29808  2.80881   1.000 59.55278  ? 74  LYS B C   1 
ATOM   1232 O O   . LYS B 1 77 ? 9.01780   3.29094  2.40456   1.000 76.58960  ? 74  LYS B O   1 
ATOM   1233 C CB  . LYS B 1 77 ? 5.95237   3.87517  2.89346   1.000 59.81720  ? 74  LYS B CB  1 
ATOM   1234 C CG  . LYS B 1 77 ? 4.71906   3.63705  3.74729   1.000 59.42126  ? 74  LYS B CG  1 
ATOM   1235 C CD  . LYS B 1 77 ? 3.44063   3.79476  2.94641   1.000 70.38606  ? 74  LYS B CD  1 
ATOM   1236 C CE  . LYS B 1 77 ? 2.23835   3.93551  3.86729   1.000 75.23197  ? 74  LYS B CE  1 
ATOM   1237 N NZ  . LYS B 1 77 ? 2.10723   2.78002  4.79802   1.000 75.52917  ? 74  LYS B NZ  1 
ATOM   1238 N N   . GLU B 1 78 ? 8.81622   5.53153  2.47892   1.000 69.48573  ? 75  GLU B N   1 
ATOM   1239 C CA  . GLU B 1 78 ? 10.03797  5.74783  1.71401   1.000 65.25790  ? 75  GLU B CA  1 
ATOM   1240 C C   . GLU B 1 78 ? 11.27992  5.76642  2.59646   1.000 67.97288  ? 75  GLU B C   1 
ATOM   1241 O O   . GLU B 1 78 ? 12.38924  5.57779  2.08572   1.000 73.70183  ? 75  GLU B O   1 
ATOM   1242 C CB  . GLU B 1 78 ? 9.94843   7.05597  0.92153   1.000 69.46617  ? 75  GLU B CB  1 
ATOM   1243 C CG  . GLU B 1 78 ? 8.70120   7.20153  0.04679   1.000 71.03534  ? 75  GLU B CG  1 
ATOM   1244 C CD  . GLU B 1 78 ? 8.76827   6.40902  -1.25106  1.000 87.58444  ? 75  GLU B CD  1 
ATOM   1245 O OE1 . GLU B 1 78 ? 9.08192   5.20075  -1.21120  1.000 82.16493  ? 75  GLU B OE1 1 
ATOM   1246 O OE2 . GLU B 1 78 ? 8.50164   7.00020  -2.31903  1.000 90.16692  ? 75  GLU B OE2 1 
ATOM   1247 N N   . LEU B 1 79 ? 11.12107  5.99533  3.90245   1.000 63.27166  ? 76  LEU B N   1 
ATOM   1248 C CA  . LEU B 1 79 ? 12.25144  5.90358  4.82085   1.000 68.54698  ? 76  LEU B CA  1 
ATOM   1249 C C   . LEU B 1 79 ? 12.60535  4.45262  5.11709   1.000 79.16948  ? 76  LEU B C   1 
ATOM   1250 O O   . LEU B 1 79 ? 13.78392  4.08056  5.11112   1.000 88.48425  ? 76  LEU B O   1 
ATOM   1251 C CB  . LEU B 1 79 ? 11.94251  6.64989  6.11701   1.000 58.73245  ? 76  LEU B CB  1 
ATOM   1252 C CG  . LEU B 1 79 ? 12.04715  8.17169  6.05932   1.000 61.83836  ? 76  LEU B CG  1 
ATOM   1253 C CD1 . LEU B 1 79 ? 11.50627  8.76468  7.33971   1.000 62.54362  ? 76  LEU B CD1 1 
ATOM   1254 C CD2 . LEU B 1 79 ? 13.49015  8.59569  5.83644   1.000 64.24042  ? 76  LEU B CD2 1 
ATOM   1255 N N   . GLU B 1 80 ? 11.59559  3.62084  5.38779   1.000 91.78359  ? 77  GLU B N   1 
ATOM   1256 C CA  . GLU B 1 80 ? 11.83667  2.19395  5.55202   1.000 97.10262  ? 77  GLU B CA  1 
ATOM   1257 C C   . GLU B 1 80 ? 12.27778  1.54190  4.25045   1.000 104.23346 ? 77  GLU B C   1 
ATOM   1258 O O   . GLU B 1 80 ? 12.79909  0.42243  4.27844   1.000 110.10975 ? 77  GLU B O   1 
ATOM   1259 C CB  . GLU B 1 80 ? 10.58214  1.50046  6.08684   1.000 96.38278  ? 77  GLU B CB  1 
ATOM   1260 C CG  . GLU B 1 80 ? 9.36987   1.62387  5.17920   1.000 99.04050  ? 77  GLU B CG  1 
ATOM   1261 C CD  . GLU B 1 80 ? 8.18556   0.81329  5.67256   1.000 113.59680 ? 77  GLU B CD  1 
ATOM   1262 O OE1 . GLU B 1 80 ? 8.40293   -0.17748 6.40185   1.000 133.56815 ? 77  GLU B OE1 1 
ATOM   1263 O OE2 . GLU B 1 80 ? 7.03637   1.16851  5.33527   1.000 116.40055 ? 77  GLU B OE2 1 
ATOM   1264 N N   . LYS B 1 81 ? 12.07721  2.21754  3.11560   1.000 92.39711  ? 78  LYS B N   1 
ATOM   1265 C CA  . LYS B 1 81 ? 12.53629  1.72324  1.82472   1.000 86.76961  ? 78  LYS B CA  1 
ATOM   1266 C C   . LYS B 1 81 ? 14.05538  1.73518  1.69924   1.000 90.32112  ? 78  LYS B C   1 
ATOM   1267 O O   . LYS B 1 81 ? 14.58706  1.09953  0.78403   1.000 95.30147  ? 78  LYS B O   1 
ATOM   1268 C CB  . LYS B 1 81 ? 11.90536  2.55496  0.70014   1.000 84.52153  ? 78  LYS B CB  1 
ATOM   1269 C CG  . LYS B 1 81 ? 11.85659  1.86400  -0.65851  1.000 76.88378  ? 78  LYS B CG  1 
ATOM   1270 C CD  . LYS B 1 81 ? 11.16289  2.73094  -1.69993  1.000 71.06017  ? 78  LYS B CD  1 
ATOM   1271 C CE  . LYS B 1 81 ? 10.98076  1.99219  -3.01891  1.000 89.04912  ? 78  LYS B CE  1 
ATOM   1272 N NZ  . LYS B 1 81 ? 10.12856  0.77898  -2.86723  1.000 90.27901  ? 78  LYS B NZ  1 
ATOM   1273 N N   . ILE B 1 82 ? 14.76265  2.44123  2.57718   1.000 90.91607  ? 79  ILE B N   1 
ATOM   1274 C CA  . ILE B 1 82 ? 16.22050  2.44292  2.54574   1.000 92.35096  ? 79  ILE B CA  1 
ATOM   1275 C C   . ILE B 1 82 ? 16.76655  1.65629  3.73201   1.000 90.46418  ? 79  ILE B C   1 
ATOM   1276 O O   . ILE B 1 82 ? 16.02332  1.29569  4.64359   1.000 92.69786  ? 79  ILE B O   1 
ATOM   1277 C CB  . ILE B 1 82 ? 16.78315  3.87523  2.53310   1.000 86.35862  ? 79  ILE B CB  1 
ATOM   1278 C CG1 . ILE B 1 82 ? 16.83507  4.44506  3.95133   1.000 94.56448  ? 79  ILE B CG1 1 
ATOM   1279 C CG2 . ILE B 1 82 ? 15.94428  4.77241  1.62542   1.000 86.49330  ? 79  ILE B CG2 1 
ATOM   1280 C CD1 . ILE B 1 82 ? 17.49632  5.80097  4.03938   1.000 89.33437  ? 79  ILE B CD1 1 
ATOM   1281 N N   . SER C 1 4  ? 26.96338  9.01943  10.93930  1.000 88.51086  ? 1   SER C N   1 
ATOM   1282 C CA  . SER C 1 4  ? 26.17214  9.39560  12.10478  1.000 88.34608  ? 1   SER C CA  1 
ATOM   1283 C C   . SER C 1 4  ? 25.07947  10.38929 11.72342  1.000 90.38019  ? 1   SER C C   1 
ATOM   1284 O O   . SER C 1 4  ? 23.89274  10.12354 11.91694  1.000 87.86968  ? 1   SER C O   1 
ATOM   1285 C CB  . SER C 1 4  ? 27.06917  9.98545  13.19466  1.000 104.27598 ? 1   SER C CB  1 
ATOM   1286 O OG  . SER C 1 4  ? 27.79837  11.09766 12.70681  1.000 124.51425 ? 1   SER C OG  1 
ATOM   1287 N N   . ILE C 1 5  ? 25.48792  11.54060 11.17987  1.000 80.57415  ? 2   ILE C N   1 
ATOM   1288 C CA  . ILE C 1 5  ? 24.52349  12.54118 10.72663  1.000 74.43172  ? 2   ILE C CA  1 
ATOM   1289 C C   . ILE C 1 5  ? 24.01016  12.26693 9.32438   1.000 67.71968  ? 2   ILE C C   1 
ATOM   1290 O O   . ILE C 1 5  ? 23.12006  12.98526 8.85153   1.000 74.91817  ? 2   ILE C O   1 
ATOM   1291 C CB  . ILE C 1 5  ? 25.11197  13.96471 10.74091  1.000 71.37849  ? 2   ILE C CB  1 
ATOM   1292 C CG1 . ILE C 1 5  ? 25.99520  14.18937 9.51115   1.000 66.01138  ? 2   ILE C CG1 1 
ATOM   1293 C CG2 . ILE C 1 5  ? 25.90125  14.20438 12.01775  1.000 78.29646  ? 2   ILE C CG2 1 
ATOM   1294 C CD1 . ILE C 1 5  ? 26.40214  15.63132 9.30665   1.000 60.91345  ? 2   ILE C CD1 1 
ATOM   1295 N N   . LYS C 1 6  ? 24.54932  11.25560 8.63966   1.000 64.31630  ? 3   LYS C N   1 
ATOM   1296 C CA  . LYS C 1 6  ? 24.07448  10.93981 7.29877   1.000 63.58894  ? 3   LYS C CA  1 
ATOM   1297 C C   . LYS C 1 6  ? 22.64170  10.42799 7.31239   1.000 60.85476  ? 3   LYS C C   1 
ATOM   1298 O O   . LYS C 1 6  ? 21.95731  10.50336 6.28640   1.000 49.83722  ? 3   LYS C O   1 
ATOM   1299 C CB  . LYS C 1 6  ? 24.99533  9.91177  6.64355   1.000 55.96899  ? 3   LYS C CB  1 
ATOM   1300 C CG  . LYS C 1 6  ? 24.68467  8.47487  7.01397   1.000 56.73367  ? 3   LYS C CG  1 
ATOM   1301 C CD  . LYS C 1 6  ? 25.87441  7.57489  6.74263   1.000 64.32346  ? 3   LYS C CD  1 
ATOM   1302 C CE  . LYS C 1 6  ? 26.39711  7.76057  5.32921   1.000 66.98610  ? 3   LYS C CE  1 
ATOM   1303 N NZ  . LYS C 1 6  ? 27.65388  6.99423  5.10807   1.000 86.36123  ? 3   LYS C NZ  1 
ATOM   1304 N N   . GLU C 1 7  ? 22.17655  9.90337  8.44918   1.000 52.57446  ? 4   GLU C N   1 
ATOM   1305 C CA  . GLU C 1 7  ? 20.76798  9.54867  8.57569   1.000 54.73644  ? 4   GLU C CA  1 
ATOM   1306 C C   . GLU C 1 7  ? 19.89928  10.79871 8.59680   1.000 51.90797  ? 4   GLU C C   1 
ATOM   1307 O O   . GLU C 1 7  ? 18.83769  10.83754 7.96356   1.000 48.92817  ? 4   GLU C O   1 
ATOM   1308 C CB  . GLU C 1 7  ? 20.55089  8.71341  9.83839   1.000 62.78125  ? 4   GLU C CB  1 
ATOM   1309 C CG  . GLU C 1 7  ? 19.16326  8.10017  9.95963   1.000 69.24613  ? 4   GLU C CG  1 
ATOM   1310 C CD  . GLU C 1 7  ? 19.00122  7.26620  11.21806  1.000 74.79703  ? 4   GLU C CD  1 
ATOM   1311 O OE1 . GLU C 1 7  ? 19.61901  7.61289  12.24703  1.000 78.19225  ? 4   GLU C OE1 1 
ATOM   1312 O OE2 . GLU C 1 7  ? 18.26052  6.26041  11.17654  1.000 72.59486  ? 4   GLU C OE2 1 
ATOM   1313 N N   . ILE C 1 8  ? 20.34223  11.83147 9.31814   1.000 51.94271  ? 5   ILE C N   1 
ATOM   1314 C CA  . ILE C 1 8  ? 19.65851  13.12100 9.29380   1.000 43.70364  ? 5   ILE C CA  1 
ATOM   1315 C C   . ILE C 1 8  ? 19.66749  13.69698 7.88427   1.000 52.52860  ? 5   ILE C C   1 
ATOM   1316 O O   . ILE C 1 8  ? 18.67573  14.27661 7.42462   1.000 46.77099  ? 5   ILE C O   1 
ATOM   1317 C CB  . ILE C 1 8  ? 20.31370  14.08086 10.30573  1.000 40.36754  ? 5   ILE C CB  1 
ATOM   1318 C CG1 . ILE C 1 8  ? 20.17221  13.53493 11.72801  1.000 47.61617  ? 5   ILE C CG1 1 
ATOM   1319 C CG2 . ILE C 1 8  ? 19.72360  15.47318 10.20232  1.000 42.45439  ? 5   ILE C CG2 1 
ATOM   1320 C CD1 . ILE C 1 8  ? 20.88368  14.36647 12.77082  1.000 52.92811  ? 5   ILE C CD1 1 
ATOM   1321 N N   . THR C 1 9  ? 20.78176  13.52888 7.17080   1.000 49.38411  ? 6   THR C N   1 
ATOM   1322 C CA  . THR C 1 9  ? 20.91355  14.09490 5.83242   1.000 49.97038  ? 6   THR C CA  1 
ATOM   1323 C C   . THR C 1 9  ? 20.00358  13.38437 4.83889   1.000 51.47243  ? 6   THR C C   1 
ATOM   1324 O O   . THR C 1 9  ? 19.17394  14.01759 4.17540   1.000 44.93205  ? 6   THR C O   1 
ATOM   1325 C CB  . THR C 1 9  ? 22.36867  14.01129 5.37181   1.000 51.43003  ? 6   THR C CB  1 
ATOM   1326 O OG1 . THR C 1 9  ? 23.19896  14.75641 6.27083   1.000 51.93348  ? 6   THR C OG1 1 
ATOM   1327 C CG2 . THR C 1 9  ? 22.50556  14.56855 3.96109   1.000 43.51755  ? 6   THR C CG2 1 
ATOM   1328 N N   . GLU C 1 10 ? 20.15986  12.06164 4.71194   1.000 44.90180  ? 7   GLU C N   1 
ATOM   1329 C CA  . GLU C 1 10 ? 19.36983  11.30714 3.74363   1.000 50.46599  ? 7   GLU C CA  1 
ATOM   1330 C C   . GLU C 1 10 ? 17.87780  11.44975 4.00716   1.000 49.07342  ? 7   GLU C C   1 
ATOM   1331 O O   . GLU C 1 10 ? 17.07589  11.43759 3.06586   1.000 49.00723  ? 7   GLU C O   1 
ATOM   1332 C CB  . GLU C 1 10 ? 19.78383  9.83430  3.76326   1.000 52.04927  ? 7   GLU C CB  1 
ATOM   1333 C CG  . GLU C 1 10 ? 21.20099  9.59308  3.26378   1.000 53.79865  ? 7   GLU C CG  1 
ATOM   1334 C CD  . GLU C 1 10 ? 21.59162  8.12754  3.28092   1.000 75.37043  ? 7   GLU C CD  1 
ATOM   1335 O OE1 . GLU C 1 10 ? 20.82405  7.30921  3.82958   1.000 75.20927  ? 7   GLU C OE1 1 
ATOM   1336 O OE2 . GLU C 1 10 ? 22.66848  7.79387  2.74288   1.000 74.33747  ? 7   GLU C OE2 1 
ATOM   1337 N N   . THR C 1 11 ? 17.48875  11.59683 5.27377   1.000 43.33817  ? 8   THR C N   1 
ATOM   1338 C CA  . THR C 1 11 ? 16.08871  11.84502 5.59141   1.000 40.93186  ? 8   THR C CA  1 
ATOM   1339 C C   . THR C 1 11 ? 15.64291  13.19752 5.05021   1.000 43.05163  ? 8   THR C C   1 
ATOM   1340 O O   . THR C 1 11 ? 14.59345  13.30398 4.40581   1.000 40.39110  ? 8   THR C O   1 
ATOM   1341 C CB  . THR C 1 11 ? 15.87439  11.76095 7.10283   1.000 43.72548  ? 8   THR C CB  1 
ATOM   1342 O OG1 . THR C 1 11 ? 16.11521  10.41762 7.54555   1.000 46.13836  ? 8   THR C OG1 1 
ATOM   1343 C CG2 . THR C 1 11 ? 14.45817  12.16008 7.46399   1.000 38.16017  ? 8   THR C CG2 1 
ATOM   1344 N N   . THR C 1 12 ? 16.43899  14.24266 5.29152   1.000 34.02401  ? 9   THR C N   1 
ATOM   1345 C CA  . THR C 1 12 ? 16.11897  15.55755 4.74722   1.000 39.52720  ? 9   THR C CA  1 
ATOM   1346 C C   . THR C 1 12 ? 16.16205  15.54248 3.22488   1.000 38.00580  ? 9   THR C C   1 
ATOM   1347 O O   . THR C 1 12 ? 15.32834  16.17542 2.56632   1.000 42.17595  ? 9   THR C O   1 
ATOM   1348 C CB  . THR C 1 12 ? 17.08113  16.60409 5.30991   1.000 35.90087  ? 9   THR C CB  1 
ATOM   1349 O OG1 . THR C 1 12 ? 17.00406  16.59482 6.74058   1.000 45.06708  ? 9   THR C OG1 1 
ATOM   1350 C CG2 . THR C 1 12 ? 16.72485  17.99295 4.80402   1.000 38.90791  ? 9   THR C CG2 1 
ATOM   1351 N N   . GLN C 1 13 ? 17.12241  14.81707 2.64696   1.000 40.14989  ? 10  GLN C N   1 
ATOM   1352 C CA  . GLN C 1 13 ? 17.13491  14.63417 1.19884   1.000 47.64967  ? 10  GLN C CA  1 
ATOM   1353 C C   . GLN C 1 13 ? 15.83236  14.01082 0.71393   1.000 39.56585  ? 10  GLN C C   1 
ATOM   1354 O O   . GLN C 1 13 ? 15.27775  14.43045 -0.30791  1.000 43.64024  ? 10  GLN C O   1 
ATOM   1355 C CB  . GLN C 1 13 ? 18.32696  13.77145 0.78346   1.000 41.48573  ? 10  GLN C CB  1 
ATOM   1356 C CG  . GLN C 1 13 ? 19.67809  14.42683 1.01136   1.000 45.51879  ? 10  GLN C CG  1 
ATOM   1357 C CD  . GLN C 1 13 ? 20.82340  13.62747 0.42274   1.000 45.39091  ? 10  GLN C CD  1 
ATOM   1358 O OE1 . GLN C 1 13 ? 21.63156  13.05078 1.15025   1.000 55.41820  ? 10  GLN C OE1 1 
ATOM   1359 N NE2 . GLN C 1 13 ? 20.90386  13.59603 -0.90304  1.000 56.48916  ? 10  GLN C NE2 1 
ATOM   1360 N N   . LEU C 1 14 ? 15.32066  13.01780 1.44564   1.000 41.57712  ? 11  LEU C N   1 
ATOM   1361 C CA  . LEU C 1 14 ? 14.05742  12.38984 1.07096   1.000 50.41690  ? 11  LEU C CA  1 
ATOM   1362 C C   . LEU C 1 14 ? 12.88642  13.35001 1.25434   1.000 44.64111  ? 11  LEU C C   1 
ATOM   1363 O O   . LEU C 1 14 ? 11.99091  13.41335 0.40417   1.000 54.03400  ? 11  LEU C O   1 
ATOM   1364 C CB  . LEU C 1 14 ? 13.85462  11.11219 1.88911   1.000 55.51760  ? 11  LEU C CB  1 
ATOM   1365 C CG  . LEU C 1 14 ? 12.71316  10.15416 1.53365   1.000 64.38148  ? 11  LEU C CG  1 
ATOM   1366 C CD1 . LEU C 1 14 ? 11.42961  10.50845 2.27446   1.000 68.09732  ? 11  LEU C CD1 1 
ATOM   1367 C CD2 . LEU C 1 14 ? 12.48013  10.12260 0.02912   1.000 57.33961  ? 11  LEU C CD2 1 
ATOM   1368 N N   . ILE C 1 15 ? 12.87364  14.10021 2.35894   1.000 44.39314  ? 12  ILE C N   1 
ATOM   1369 C CA  . ILE C 1 15 ? 11.82120  15.08872 2.58163   1.000 47.31949  ? 12  ILE C CA  1 
ATOM   1370 C C   . ILE C 1 15 ? 11.84232  16.14060 1.48146   1.000 56.77829  ? 12  ILE C C   1 
ATOM   1371 O O   . ILE C 1 15 ? 10.79384  16.63647 1.04925   1.000 56.40852  ? 12  ILE C O   1 
ATOM   1372 C CB  . ILE C 1 15 ? 11.98022  15.72633 3.97495   1.000 46.24157  ? 12  ILE C CB  1 
ATOM   1373 C CG1 . ILE C 1 15 ? 11.82801  14.67098 5.06953   1.000 52.52659  ? 12  ILE C CG1 1 
ATOM   1374 C CG2 . ILE C 1 15 ? 10.97538  16.85311 4.17770   1.000 60.41203  ? 12  ILE C CG2 1 
ATOM   1375 C CD1 . ILE C 1 15 ? 12.13715  15.19209 6.45598   1.000 49.10432  ? 12  ILE C CD1 1 
ATOM   1376 N N   . VAL C 1 16 ? 13.03759  16.48603 1.00231   1.000 49.08375  ? 13  VAL C N   1 
ATOM   1377 C CA  . VAL C 1 16 ? 13.16901  17.53256 -0.00356  1.000 41.28530  ? 13  VAL C CA  1 
ATOM   1378 C C   . VAL C 1 16 ? 12.71488  17.03247 -1.37236  1.000 47.37921  ? 13  VAL C C   1 
ATOM   1379 O O   . VAL C 1 16 ? 12.03101  17.75084 -2.11181  1.000 45.37142  ? 13  VAL C O   1 
ATOM   1380 C CB  . VAL C 1 16 ? 14.61883  18.04790 -0.02599  1.000 29.60123  ? 13  VAL C CB  1 
ATOM   1381 C CG1 . VAL C 1 16 ? 14.91220  18.75236 -1.32453  1.000 37.27390  ? 13  VAL C CG1 1 
ATOM   1382 C CG2 . VAL C 1 16 ? 14.86063  18.97884 1.15398   1.000 40.16416  ? 13  VAL C CG2 1 
ATOM   1383 N N   . LYS C 1 17 ? 13.07530  15.79373 -1.72792  1.000 45.51982  ? 14  LYS C N   1 
ATOM   1384 C CA  . LYS C 1 17 ? 12.70222  15.25341 -3.03360  1.000 54.92748  ? 14  LYS C CA  1 
ATOM   1385 C C   . LYS C 1 17 ? 11.19213  15.18695 -3.21392  1.000 53.05560  ? 14  LYS C C   1 
ATOM   1386 O O   . LYS C 1 17 ? 10.69561  15.33392 -4.33645  1.000 51.49669  ? 14  LYS C O   1 
ATOM   1387 C CB  . LYS C 1 17 ? 13.30240  13.86020 -3.22727  1.000 48.92576  ? 14  LYS C CB  1 
ATOM   1388 C CG  . LYS C 1 17 ? 14.81186  13.81603 -3.36236  1.000 40.99767  ? 14  LYS C CG  1 
ATOM   1389 C CD  . LYS C 1 17 ? 15.28220  12.37663 -3.50192  1.000 50.56010  ? 14  LYS C CD  1 
ATOM   1390 C CE  . LYS C 1 17 ? 16.76750  12.23721 -3.22297  1.000 54.75562  ? 14  LYS C CE  1 
ATOM   1391 N NZ  . LYS C 1 17 ? 17.16640  10.80998 -3.06449  1.000 64.01192  ? 14  LYS C NZ  1 
ATOM   1392 N N   . HIS C 1 18 ? 10.44907  14.95256 -2.13520  1.000 61.32948  ? 15  HIS C N   1 
ATOM   1393 C CA  . HIS C 1 18 ? 9.00104   14.84726 -2.23437  1.000 63.54902  ? 15  HIS C CA  1 
ATOM   1394 C C   . HIS C 1 18 ? 8.31267   16.19929 -2.14002  1.000 56.25775  ? 15  HIS C C   1 
ATOM   1395 O O   . HIS C 1 18 ? 7.28457   16.40956 -2.79298  1.000 61.14869  ? 15  HIS C O   1 
ATOM   1396 C CB  . HIS C 1 18 ? 8.46593   13.91135 -1.14479  1.000 64.80223  ? 15  HIS C CB  1 
ATOM   1397 C CG  . HIS C 1 18 ? 8.65003   12.45831 -1.45495  1.000 70.87562  ? 15  HIS C CG  1 
ATOM   1398 N ND1 . HIS C 1 18 ? 9.83655   11.94240 -1.92900  1.000 69.17950  ? 15  HIS C ND1 1 
ATOM   1399 C CD2 . HIS C 1 18 ? 7.79427   11.41305 -1.36498  1.000 75.89112  ? 15  HIS C CD2 1 
ATOM   1400 C CE1 . HIS C 1 18 ? 9.70419   10.64118 -2.11639  1.000 83.59087  ? 15  HIS C CE1 1 
ATOM   1401 N NE2 . HIS C 1 18 ? 8.47443   10.29502 -1.78189  1.000 91.19995  ? 15  HIS C NE2 1 
ATOM   1402 N N   . LEU C 1 19 ? 8.87232   17.12996 -1.37085  1.000 51.21406  ? 16  LEU C N   1 
ATOM   1403 C CA  . LEU C 1 19 ? 8.21043   18.39283 -1.06804  1.000 57.48902  ? 16  LEU C CA  1 
ATOM   1404 C C   . LEU C 1 19 ? 8.61041   19.53207 -1.99690  1.000 49.83090  ? 16  LEU C C   1 
ATOM   1405 O O   . LEU C 1 19 ? 7.75040   20.31656 -2.41001  1.000 56.99585  ? 16  LEU C O   1 
ATOM   1406 C CB  . LEU C 1 19 ? 8.50272   18.79928 0.37907   1.000 49.42061  ? 16  LEU C CB  1 
ATOM   1407 C CG  . LEU C 1 19 ? 7.40256   19.59303 1.07464   1.000 65.17855  ? 16  LEU C CG  1 
ATOM   1408 C CD1 . LEU C 1 19 ? 6.10886   18.79273 1.03958   1.000 64.90607  ? 16  LEU C CD1 1 
ATOM   1409 C CD2 . LEU C 1 19 ? 7.79587   19.92673 2.50483   1.000 64.36282  ? 16  LEU C CD2 1 
ATOM   1410 N N   . ALA C 1 20 ? 9.89092   19.64598 -2.33642  1.000 48.07735  ? 17  ALA C N   1 
ATOM   1411 C CA  . ALA C 1 20 ? 10.39243  20.80430 -3.06192  1.000 47.74592  ? 17  ALA C CA  1 
ATOM   1412 C C   . ALA C 1 20 ? 10.29934  20.59815 -4.56804  1.000 43.42412  ? 17  ALA C C   1 
ATOM   1413 O O   . ALA C 1 20 ? 10.55843  19.50399 -5.07805  1.000 43.28450  ? 17  ALA C O   1 
ATOM   1414 C CB  . ALA C 1 20 ? 11.84290  21.09828 -2.66876  1.000 49.23807  ? 17  ALA C CB  1 
ATOM   1415 N N   . HIS C 1 21 ? 9.91737   21.65953 -5.27575  1.000 45.17735  ? 18  HIS C N   1 
ATOM   1416 C CA  . HIS C 1 21 ? 10.08610  21.67661 -6.72079  1.000 52.43501  ? 18  HIS C CA  1 
ATOM   1417 C C   . HIS C 1 21 ? 11.57205  21.61903 -7.04851  1.000 53.18103  ? 18  HIS C C   1 
ATOM   1418 O O   . HIS C 1 21 ? 12.39977  22.20369 -6.34230  1.000 50.88671  ? 18  HIS C O   1 
ATOM   1419 C CB  . HIS C 1 21 ? 9.45727   22.93243 -7.32446  1.000 51.18655  ? 18  HIS C CB  1 
ATOM   1420 C CG  . HIS C 1 21 ? 7.97430   23.02460 -7.13402  1.000 59.14903  ? 18  HIS C CG  1 
ATOM   1421 N ND1 . HIS C 1 21 ? 7.39635   23.40413 -5.94118  1.000 54.09803  ? 18  HIS C ND1 1 
ATOM   1422 C CD2 . HIS C 1 21 ? 6.95100   22.79319 -7.99007  1.000 53.02373  ? 18  HIS C CD2 1 
ATOM   1423 C CE1 . HIS C 1 21 ? 6.08150   23.40024 -6.07006  1.000 51.15144  ? 18  HIS C CE1 1 
ATOM   1424 N NE2 . HIS C 1 21 ? 5.78532   23.03315 -7.30387  1.000 54.97572  ? 18  HIS C NE2 1 
ATOM   1425 N N   . ASN C 1 22 ? 11.90710  20.90329 -8.12259  1.000 56.76093  ? 19  ASN C N   1 
ATOM   1426 C CA  . ASN C 1 22 ? 13.29618  20.59220 -8.45864  1.000 52.97018  ? 19  ASN C CA  1 
ATOM   1427 C C   . ASN C 1 22 ? 14.00826  20.00105 -7.24544  1.000 45.88441  ? 19  ASN C C   1 
ATOM   1428 O O   . ASN C 1 22 ? 15.10783  20.41486 -6.86907  1.000 41.23628  ? 19  ASN C O   1 
ATOM   1429 C CB  . ASN C 1 22 ? 14.03260  21.82629 -8.98061  1.000 44.28274  ? 19  ASN C CB  1 
ATOM   1430 C CG  . ASN C 1 22 ? 13.15346  22.70658 -9.84278  1.000 62.38593  ? 19  ASN C CG  1 
ATOM   1431 O OD1 . ASN C 1 22 ? 12.53480  23.65068 -9.35280  1.000 61.11232  ? 19  ASN C OD1 1 
ATOM   1432 N ND2 . ASN C 1 22 ? 13.09161  22.40225 -11.13326 1.000 62.15264  ? 19  ASN C ND2 1 
ATOM   1433 N N   . GLY C 1 23 ? 13.34541  19.02853 -6.61550  1.000 44.18519  ? 20  GLY C N   1 
ATOM   1434 C CA  . GLY C 1 23 ? 13.84976  18.48276 -5.36792  1.000 45.20080  ? 20  GLY C CA  1 
ATOM   1435 C C   . GLY C 1 23 ? 15.21048  17.83023 -5.49106  1.000 41.29915  ? 20  GLY C C   1 
ATOM   1436 O O   . GLY C 1 23 ? 15.99564  17.85006 -4.54091  1.000 46.57994  ? 20  GLY C O   1 
ATOM   1437 N N   . GLU C 1 24 ? 15.51281  17.24992 -6.65443  1.000 42.64446  ? 21  GLU C N   1 
ATOM   1438 C CA  . GLU C 1 24 ? 16.80632  16.59947 -6.83146  1.000 44.33819  ? 21  GLU C CA  1 
ATOM   1439 C C   . GLU C 1 24 ? 17.94180  17.61275 -6.78329  1.000 43.25146  ? 21  GLU C C   1 
ATOM   1440 O O   . GLU C 1 24 ? 19.02150  17.32013 -6.25688  1.000 43.06855  ? 21  GLU C O   1 
ATOM   1441 C CB  . GLU C 1 24 ? 16.83158  15.81321 -8.14368  1.000 49.10211  ? 21  GLU C CB  1 
ATOM   1442 C CG  . GLU C 1 24 ? 16.65862  14.31016 -7.95909  1.000 57.91974  ? 21  GLU C CG  1 
ATOM   1443 C CD  . GLU C 1 24 ? 17.78846  13.68208 -7.15958  1.000 63.25461  ? 21  GLU C CD  1 
ATOM   1444 O OE1 . GLU C 1 24 ? 18.90289  14.24812 -7.14526  1.000 59.77688  ? 21  GLU C OE1 1 
ATOM   1445 O OE2 . GLU C 1 24 ? 17.56124  12.61955 -6.54308  1.000 63.80598  ? 21  GLU C OE2 1 
ATOM   1446 N N   . GLU C 1 25 ? 17.71970  18.81196 -7.32443  1.000 43.04970  ? 22  GLU C N   1 
ATOM   1447 C CA  . GLU C 1 25 ? 18.72928  19.85768 -7.19969  1.000 47.51300  ? 22  GLU C CA  1 
ATOM   1448 C C   . GLU C 1 25 ? 18.88492  20.29492 -5.74942  1.000 38.45659  ? 22  GLU C C   1 
ATOM   1449 O O   . GLU C 1 25 ? 20.00916  20.46440 -5.26322  1.000 39.26367  ? 22  GLU C O   1 
ATOM   1450 C CB  . GLU C 1 25 ? 18.37807  21.05009 -8.08865  1.000 43.37493  ? 22  GLU C CB  1 
ATOM   1451 C CG  . GLU C 1 25 ? 18.49781  20.77043 -9.57850  1.000 52.44854  ? 22  GLU C CG  1 
ATOM   1452 C CD  . GLU C 1 25 ? 18.70961  22.03377 -10.39297 1.000 56.81895  ? 22  GLU C CD  1 
ATOM   1453 O OE1 . GLU C 1 25 ? 18.99232  23.09223 -9.79083  1.000 63.26388  ? 22  GLU C OE1 1 
ATOM   1454 O OE2 . GLU C 1 25 ? 18.59850  21.96806 -11.63551 1.000 69.64053  ? 22  GLU C OE2 1 
ATOM   1455 N N   . TYR C 1 26 ? 17.77070  20.46963 -5.03665  1.000 36.03585  ? 23  TYR C N   1 
ATOM   1456 C CA  . TYR C 1 26 ? 17.86428  20.81337 -3.62241  1.000 36.83667  ? 23  TYR C CA  1 
ATOM   1457 C C   . TYR C 1 26 ? 18.41861  19.65109 -2.80728  1.000 34.21489  ? 23  TYR C C   1 
ATOM   1458 O O   . TYR C 1 26 ? 19.16465  19.86379 -1.84528  1.000 40.17771  ? 23  TYR C O   1 
ATOM   1459 C CB  . TYR C 1 26 ? 16.49937  21.24267 -3.08584  1.000 38.49376  ? 23  TYR C CB  1 
ATOM   1460 C CG  . TYR C 1 26 ? 16.04898  22.60643 -3.54715  1.000 38.09871  ? 23  TYR C CG  1 
ATOM   1461 C CD1 . TYR C 1 26 ? 16.63145  23.75816 -3.03843  1.000 30.38913  ? 23  TYR C CD1 1 
ATOM   1462 C CD2 . TYR C 1 26 ? 15.03431  22.74221 -4.48346  1.000 37.79503  ? 23  TYR C CD2 1 
ATOM   1463 C CE1 . TYR C 1 26 ? 16.22131  25.00996 -3.45638  1.000 41.82659  ? 23  TYR C CE1 1 
ATOM   1464 C CE2 . TYR C 1 26 ? 14.61543  23.98921 -4.90697  1.000 38.71906  ? 23  TYR C CE2 1 
ATOM   1465 C CZ  . TYR C 1 26 ? 15.21143  25.11920 -4.38952  1.000 43.72688  ? 23  TYR C CZ  1 
ATOM   1466 O OH  . TYR C 1 26 ? 14.79808  26.36116 -4.80855  1.000 34.20071  ? 23  TYR C OH  1 
ATOM   1467 N N   . SER C 1 27 ? 18.06711  18.41556 -3.17545  1.000 36.88404  ? 24  SER C N   1 
ATOM   1468 C CA  . SER C 1 27 ? 18.57926  17.25479 -2.45205  1.000 43.30765  ? 24  SER C CA  1 
ATOM   1469 C C   . SER C 1 27 ? 20.09242  17.14208 -2.59052  1.000 48.05694  ? 24  SER C C   1 
ATOM   1470 O O   . SER C 1 27 ? 20.78552  16.76177 -1.63795  1.000 38.68339  ? 24  SER C O   1 
ATOM   1471 C CB  . SER C 1 27 ? 17.90129  15.97956 -2.95391  1.000 37.84025  ? 24  SER C CB  1 
ATOM   1472 O OG  . SER C 1 27 ? 18.43878  14.83574 -2.31737  1.000 54.74309  ? 24  SER C OG  1 
ATOM   1473 N N   . GLU C 1 28 ? 20.62135  17.45367 -3.77697  1.000 39.45794  ? 25  GLU C N   1 
ATOM   1474 C CA  . GLU C 1 28 ? 22.06830  17.47152 -3.95811  1.000 40.91922  ? 25  GLU C CA  1 
ATOM   1475 C C   . GLU C 1 28 ? 22.71600  18.54579 -3.09687  1.000 48.88616  ? 25  GLU C C   1 
ATOM   1476 O O   . GLU C 1 28 ? 23.83496  18.35815 -2.60404  1.000 39.91523  ? 25  GLU C O   1 
ATOM   1477 C CB  . GLU C 1 28 ? 22.40876  17.68272 -5.43549  1.000 44.52395  ? 25  GLU C CB  1 
ATOM   1478 C CG  . GLU C 1 28 ? 23.88731  17.89995 -5.72303  1.000 55.47869  ? 25  GLU C CG  1 
ATOM   1479 C CD  . GLU C 1 28 ? 24.74902  16.72502 -5.30366  1.000 66.35381  ? 25  GLU C CD  1 
ATOM   1480 O OE1 . GLU C 1 28 ? 24.26750  15.57332 -5.36631  1.000 63.54531  ? 25  GLU C OE1 1 
ATOM   1481 O OE2 . GLU C 1 28 ? 25.91099  16.95574 -4.90908  1.000 75.35785  ? 25  GLU C OE2 1 
ATOM   1482 N N   . VAL C 1 29 ? 22.02228  19.66676 -2.88967  1.000 36.31727  ? 26  VAL C N   1 
ATOM   1483 C CA  . VAL C 1 29 ? 22.54536  20.71249 -2.01861  1.000 43.22720  ? 26  VAL C CA  1 
ATOM   1484 C C   . VAL C 1 29 ? 22.59166  20.22852 -0.57476  1.000 40.03948  ? 26  VAL C C   1 
ATOM   1485 O O   . VAL C 1 29 ? 23.55963  20.49214 0.14902   1.000 34.48078  ? 26  VAL C O   1 
ATOM   1486 C CB  . VAL C 1 29 ? 21.70833  21.99584 -2.16568  1.000 39.53470  ? 26  VAL C CB  1 
ATOM   1487 C CG1 . VAL C 1 29 ? 22.14529  23.03291 -1.14960  1.000 31.71309  ? 26  VAL C CG1 1 
ATOM   1488 C CG2 . VAL C 1 29 ? 21.83371  22.54726 -3.57846  1.000 35.56130  ? 26  VAL C CG2 1 
ATOM   1489 N N   . VAL C 1 30 ? 21.55367  19.50787 -0.13548  1.000 37.35875  ? 27  VAL C N   1 
ATOM   1490 C CA  . VAL C 1 30 ? 21.55902  18.93046 1.20770   1.000 41.08462  ? 27  VAL C CA  1 
ATOM   1491 C C   . VAL C 1 30 ? 22.77014  18.02787 1.39311   1.000 34.11840  ? 27  VAL C C   1 
ATOM   1492 O O   . VAL C 1 30 ? 23.40276  18.02419 2.45572   1.000 43.95236  ? 27  VAL C O   1 
ATOM   1493 C CB  . VAL C 1 30 ? 20.24658  18.17025 1.47615   1.000 40.93177  ? 27  VAL C CB  1 
ATOM   1494 C CG1 . VAL C 1 30 ? 20.28066  17.52081 2.84955   1.000 35.76893  ? 27  VAL C CG1 1 
ATOM   1495 C CG2 . VAL C 1 30 ? 19.06060  19.10367 1.36509   1.000 34.26122  ? 27  VAL C CG2 1 
ATOM   1496 N N   . LYS C 1 31 ? 23.11615  17.25521 0.36096   1.000 40.62172  ? 28  LYS C N   1 
ATOM   1497 C CA  . LYS C 1 31 ? 24.29808  16.40309 0.43280   1.000 44.69030  ? 28  LYS C CA  1 
ATOM   1498 C C   . LYS C 1 31 ? 25.56307  17.24141 0.57736   1.000 47.65245  ? 28  LYS C C   1 
ATOM   1499 O O   . LYS C 1 31 ? 26.39851  16.97990 1.45091   1.000 49.82842  ? 28  LYS C O   1 
ATOM   1500 C CB  . LYS C 1 31 ? 24.37589  15.51164 -0.81050  1.000 43.56586  ? 28  LYS C CB  1 
ATOM   1501 C CG  . LYS C 1 31 ? 24.88123  14.09560 -0.54590  1.000 50.43285  ? 28  LYS C CG  1 
ATOM   1502 C CD  . LYS C 1 31 ? 26.33727  14.07567 -0.10000  1.000 67.06039  ? 28  LYS C CD  1 
ATOM   1503 C CE  . LYS C 1 31 ? 26.77427  12.68242 0.32506   1.000 62.66314  ? 28  LYS C CE  1 
ATOM   1504 N NZ  . LYS C 1 31 ? 28.18929  12.66258 0.79202   1.000 54.91213  ? 28  LYS C NZ  1 
ATOM   1505 N N   . GLU C 1 32 ? 25.71874  18.25866 -0.27612  1.000 45.49685  ? 29  GLU C N   1 
ATOM   1506 C CA  . GLU C 1 32 ? 26.92070  19.08647 -0.23039  1.000 50.59769  ? 29  GLU C CA  1 
ATOM   1507 C C   . GLU C 1 32 ? 27.03208  19.82516 1.09678   1.000 49.36498  ? 29  GLU C C   1 
ATOM   1508 O O   . GLU C 1 32 ? 28.10363  19.85183 1.71305   1.000 42.50699  ? 29  GLU C O   1 
ATOM   1509 C CB  . GLU C 1 32 ? 26.92629  20.07878 -1.39427  1.000 51.00679  ? 29  GLU C CB  1 
ATOM   1510 C CG  . GLU C 1 32 ? 26.84828  19.43761 -2.76769  1.000 54.23137  ? 29  GLU C CG  1 
ATOM   1511 C CD  . GLU C 1 32 ? 26.83800  20.46439 -3.88347  1.000 73.00899  ? 29  GLU C CD  1 
ATOM   1512 O OE1 . GLU C 1 32 ? 27.64374  21.41743 -3.82231  1.000 71.54772  ? 29  GLU C OE1 1 
ATOM   1513 O OE2 . GLU C 1 32 ? 26.02270  20.32160 -4.81932  1.000 78.13770  ? 29  GLU C OE2 1 
ATOM   1514 N N   . ILE C 1 33 ? 25.93420  20.43064 1.55316   1.000 40.89040  ? 30  ILE C N   1 
ATOM   1515 C CA  . ILE C 1 33 ? 25.96538  21.16261 2.81418   1.000 41.53685  ? 30  ILE C CA  1 
ATOM   1516 C C   . ILE C 1 33 ? 26.23947  20.22627 3.98592   1.000 48.33833  ? 30  ILE C C   1 
ATOM   1517 O O   . ILE C 1 33 ? 26.93846  20.60082 4.93490   1.000 44.81702  ? 30  ILE C O   1 
ATOM   1518 C CB  . ILE C 1 33 ? 24.65222  21.94539 2.99966   1.000 39.46016  ? 30  ILE C CB  1 
ATOM   1519 C CG1 . ILE C 1 33 ? 24.47237  22.95335 1.86336   1.000 32.13950  ? 30  ILE C CG1 1 
ATOM   1520 C CG2 . ILE C 1 33 ? 24.63108  22.66760 4.33901   1.000 47.66421  ? 30  ILE C CG2 1 
ATOM   1521 C CD1 . ILE C 1 33 ? 25.68601  23.82975 1.63248   1.000 37.59277  ? 30  ILE C CD1 1 
ATOM   1522 N N   . SER C 1 34 ? 25.71764  18.99710 3.93874   1.000 41.55158  ? 31  SER C N   1 
ATOM   1523 C CA  . SER C 1 34 ? 25.95525  18.05744 5.02934   1.000 52.44401  ? 31  SER C CA  1 
ATOM   1524 C C   . SER C 1 34 ? 27.42593  17.67269 5.11522   1.000 49.06355  ? 31  SER C C   1 
ATOM   1525 O O   . SER C 1 34 ? 27.95884  17.49121 6.21571   1.000 44.51918  ? 31  SER C O   1 
ATOM   1526 C CB  . SER C 1 34 ? 25.08474  16.81519 4.85502   1.000 39.96900  ? 31  SER C CB  1 
ATOM   1527 O OG  . SER C 1 34 ? 25.43314  16.10427 3.67847   1.000 61.18108  ? 31  SER C OG  1 
ATOM   1528 N N   . GLU C 1 35 ? 28.09589  17.53940 3.96634   1.000 54.60846  ? 32  GLU C N   1 
ATOM   1529 C CA  . GLU C 1 35 ? 29.52847  17.25722 3.97419   1.000 53.43067  ? 32  GLU C CA  1 
ATOM   1530 C C   . GLU C 1 35 ? 30.29935  18.35456 4.69736   1.000 60.15176  ? 32  GLU C C   1 
ATOM   1531 O O   . GLU C 1 35 ? 31.19013  18.06997 5.50777   1.000 58.12023  ? 32  GLU C O   1 
ATOM   1532 C CB  . GLU C 1 35 ? 30.04189  17.09852 2.54239   1.000 56.90417  ? 32  GLU C CB  1 
ATOM   1533 C CG  . GLU C 1 35 ? 29.44079  15.92637 1.78470   1.000 66.17359  ? 32  GLU C CG  1 
ATOM   1534 C CD  . GLU C 1 35 ? 29.89061  15.88205 0.33685   1.000 72.43065  ? 32  GLU C CD  1 
ATOM   1535 O OE1 . GLU C 1 35 ? 30.68543  16.75778 -0.06900  1.000 76.14408  ? 32  GLU C OE1 1 
ATOM   1536 O OE2 . GLU C 1 35 ? 29.44817  14.97276 -0.39557  1.000 70.82465  ? 32  GLU C OE2 1 
ATOM   1537 N N   . GLU C 1 36 ? 29.96609  19.61730 4.41724   1.000 44.73523  ? 33  GLU C N   1 
ATOM   1538 C CA  . GLU C 1 36 ? 30.62560  20.73007 5.09293   1.000 59.62207  ? 33  GLU C CA  1 
ATOM   1539 C C   . GLU C 1 36 ? 30.31190  20.73143 6.58469   1.000 59.52520  ? 33  GLU C C   1 
ATOM   1540 O O   . GLU C 1 36 ? 31.19089  21.00788 7.41013   1.000 49.40688  ? 33  GLU C O   1 
ATOM   1541 C CB  . GLU C 1 36 ? 30.20952  22.05251 4.44331   1.000 55.09196  ? 33  GLU C CB  1 
ATOM   1542 C CG  . GLU C 1 36 ? 30.86461  23.29124 5.03902   1.000 63.41186  ? 33  GLU C CG  1 
ATOM   1543 C CD  . GLU C 1 36 ? 30.68292  24.52040 4.16599   1.000 77.24732  ? 33  GLU C CD  1 
ATOM   1544 O OE1 . GLU C 1 36 ? 30.46766  24.35785 2.94539   1.000 76.02241  ? 33  GLU C OE1 1 
ATOM   1545 O OE2 . GLU C 1 36 ? 30.75614  25.64860 4.69851   1.000 72.99466  ? 33  GLU C OE2 1 
ATOM   1546 N N   . MET C 1 37 ? 29.06684  20.41641 6.95034   1.000 49.73337  ? 34  MET C N   1 
ATOM   1547 C CA  . MET C 1 37 ? 28.71161  20.34416 8.36314   1.000 47.44504  ? 34  MET C CA  1 
ATOM   1548 C C   . MET C 1 37 ? 29.39447  19.17142 9.05201   1.000 51.21601  ? 34  MET C C   1 
ATOM   1549 O O   . MET C 1 37 ? 29.66940  19.23596 10.25541  1.000 50.70478  ? 34  MET C O   1 
ATOM   1550 C CB  . MET C 1 37 ? 27.19464  20.24318 8.52262   1.000 44.20282  ? 34  MET C CB  1 
ATOM   1551 C CG  . MET C 1 37 ? 26.43655  21.43883 7.97369   1.000 39.60749  ? 34  MET C CG  1 
ATOM   1552 S SD  . MET C 1 37 ? 24.67353  21.42354 8.35314   1.000 56.10448  ? 34  MET C SD  1 
ATOM   1553 C CE  . MET C 1 37 ? 24.16876  19.89416 7.57385   1.000 38.48009  ? 34  MET C CE  1 
ATOM   1554 N N   . GLU C 1 38 ? 29.67425  18.09749 8.31250   1.000 51.26833  ? 35  GLU C N   1 
ATOM   1555 C CA  . GLU C 1 38 ? 30.36212  16.95351 8.89679   1.000 47.75756  ? 35  GLU C CA  1 
ATOM   1556 C C   . GLU C 1 38 ? 31.85988  17.20855 9.01574   1.000 59.27378  ? 35  GLU C C   1 
ATOM   1557 O O   . GLU C 1 38 ? 32.49432  16.75646 9.97579   1.000 59.21157  ? 35  GLU C O   1 
ATOM   1558 C CB  . GLU C 1 38 ? 30.09005  15.70192 8.06364   1.000 52.39682  ? 35  GLU C CB  1 
ATOM   1559 C CG  . GLU C 1 38 ? 30.62349  14.41886 8.67364   1.000 68.68181  ? 35  GLU C CG  1 
ATOM   1560 C CD  . GLU C 1 38 ? 30.18524  13.19057 7.90445   1.000 75.45716  ? 35  GLU C CD  1 
ATOM   1561 O OE1 . GLU C 1 38 ? 29.53625  13.35084 6.84906   1.000 81.50474  ? 35  GLU C OE1 1 
ATOM   1562 O OE2 . GLU C 1 38 ? 30.48571  12.06614 8.35582   1.000 87.74117  ? 35  GLU C OE2 1 
ATOM   1563 N N   . LYS C 1 39 ? 32.44076  17.93046 8.05259   1.000 58.91241  ? 36  LYS C N   1 
ATOM   1564 C CA  . LYS C 1 39 ? 33.84794  18.30095 8.14757   1.000 62.38127  ? 36  LYS C CA  1 
ATOM   1565 C C   . LYS C 1 39 ? 34.11425  19.26025 9.29957   1.000 60.19242  ? 36  LYS C C   1 
ATOM   1566 O O   . LYS C 1 39 ? 35.25456  19.34533 9.76594   1.000 60.62125  ? 36  LYS C O   1 
ATOM   1567 C CB  . LYS C 1 39 ? 34.32824  18.93025 6.83629   1.000 69.85822  ? 36  LYS C CB  1 
ATOM   1568 C CG  . LYS C 1 39 ? 34.38905  17.98055 5.64727   1.000 64.35634  ? 36  LYS C CG  1 
ATOM   1569 C CD  . LYS C 1 39 ? 34.77163  18.73369 4.37687   1.000 80.42586  ? 36  LYS C CD  1 
ATOM   1570 C CE  . LYS C 1 39 ? 34.66565  17.85490 3.13824   1.000 81.99450  ? 36  LYS C CE  1 
ATOM   1571 N NZ  . LYS C 1 39 ? 35.59027  16.69027 3.19138   1.000 99.71938  ? 36  LYS C NZ  1 
ATOM   1572 N N   . LYS C 1 40 ? 33.09722  19.98202 9.76696   1.000 54.65908  ? 37  LYS C N   1 
ATOM   1573 C CA  . LYS C 1 40 ? 33.25780  20.92577 10.86348  1.000 64.82907  ? 37  LYS C CA  1 
ATOM   1574 C C   . LYS C 1 40 ? 32.78266  20.37305 12.19917  1.000 57.31581  ? 37  LYS C C   1 
ATOM   1575 O O   . LYS C 1 40 ? 32.78100  21.10671 13.19273  1.000 60.14463  ? 37  LYS C O   1 
ATOM   1576 C CB  . LYS C 1 40 ? 32.52248  22.23020 10.54788  1.000 57.60393  ? 37  LYS C CB  1 
ATOM   1577 C CG  . LYS C 1 40 ? 33.11074  22.97201 9.36967   1.000 66.28071  ? 37  LYS C CG  1 
ATOM   1578 C CD  . LYS C 1 40 ? 32.56855  24.38114 9.27598   1.000 72.34970  ? 37  LYS C CD  1 
ATOM   1579 C CE  . LYS C 1 40 ? 33.20729  25.12752 8.11744   1.000 74.41883  ? 37  LYS C CE  1 
ATOM   1580 N NZ  . LYS C 1 40 ? 32.74791  26.54067 8.05860   1.000 77.62387  ? 37  LYS C NZ  1 
ATOM   1581 N N   . GLY C 1 41 ? 32.38533  19.10460 12.24809  1.000 54.84360  ? 38  GLY C N   1 
ATOM   1582 C CA  . GLY C 1 41 ? 32.00309  18.48860 13.50719  1.000 66.94442  ? 38  GLY C CA  1 
ATOM   1583 C C   . GLY C 1 41 ? 30.82341  19.14161 14.18906  1.000 58.36209  ? 38  GLY C C   1 
ATOM   1584 O O   . GLY C 1 41 ? 30.72014  19.09142 15.42022  1.000 57.60720  ? 38  GLY C O   1 
ATOM   1585 N N   . LEU C 1 42 ? 29.93556  19.76973 13.42248  1.000 58.16415  ? 39  LEU C N   1 
ATOM   1586 C CA  . LEU C 1 42 ? 28.73413  20.35173 14.00101  1.000 53.69627  ? 39  LEU C CA  1 
ATOM   1587 C C   . LEU C 1 42 ? 27.88024  19.26549 14.64190  1.000 55.31985  ? 39  LEU C C   1 
ATOM   1588 O O   . LEU C 1 42 ? 27.74615  18.16038 14.10886  1.000 60.38372  ? 39  LEU C O   1 
ATOM   1589 C CB  . LEU C 1 42 ? 27.93070  21.08935 12.92936  1.000 48.50213  ? 39  LEU C CB  1 
ATOM   1590 C CG  . LEU C 1 42 ? 28.66560  22.17563 12.14354  1.000 51.49304  ? 39  LEU C CG  1 
ATOM   1591 C CD1 . LEU C 1 42 ? 27.74022  22.80810 11.11867  1.000 50.20120  ? 39  LEU C CD1 1 
ATOM   1592 C CD2 . LEU C 1 42 ? 29.23022  23.23001 13.08099  1.000 47.51200  ? 39  LEU C CD2 1 
ATOM   1593 N N   . SER C 1 43 ? 27.30640  19.58624 15.79749  1.000 42.53977  ? 40  SER C N   1 
ATOM   1594 C CA  . SER C 1 43 ? 26.47270  18.63770 16.51613  1.000 50.65744  ? 40  SER C CA  1 
ATOM   1595 C C   . SER C 1 43 ? 25.21359  18.30892 15.71817  1.000 52.64289  ? 40  SER C C   1 
ATOM   1596 O O   . SER C 1 43 ? 24.80695  19.04149 14.81197  1.000 53.56988  ? 40  SER C O   1 
ATOM   1597 C CB  . SER C 1 43 ? 26.08081  19.19770 17.88114  1.000 56.08834  ? 40  SER C CB  1 
ATOM   1598 O OG  . SER C 1 43 ? 25.27972  20.35837 17.73186  1.000 57.67071  ? 40  SER C OG  1 
ATOM   1599 N N   . LYS C 1 44 ? 24.59640  17.17724 16.06786  1.000 53.90204  ? 41  LYS C N   1 
ATOM   1600 C CA  . LYS C 1 44 ? 23.33387  16.80248 15.43903  1.000 53.00480  ? 41  LYS C CA  1 
ATOM   1601 C C   . LYS C 1 44 ? 22.24911  17.83989 15.69375  1.000 52.24626  ? 41  LYS C C   1 
ATOM   1602 O O   . LYS C 1 44 ? 21.40770  18.07950 14.81989  1.000 47.09060  ? 41  LYS C O   1 
ATOM   1603 C CB  . LYS C 1 44 ? 22.87863  15.43002 15.93525  1.000 49.04258  ? 41  LYS C CB  1 
ATOM   1604 C CG  . LYS C 1 44 ? 23.61916  14.25504 15.31009  1.000 67.58044  ? 41  LYS C CG  1 
ATOM   1605 C CD  . LYS C 1 44 ? 22.95548  12.93206 15.65579  1.000 65.17920  ? 41  LYS C CD  1 
ATOM   1606 C CE  . LYS C 1 44 ? 23.47221  11.80298 14.76977  1.000 74.12006  ? 41  LYS C CE  1 
ATOM   1607 N NZ  . LYS C 1 44 ? 22.72609  10.52889 14.98841  1.000 67.45464  ? 41  LYS C NZ  1 
ATOM   1608 N N   . GLU C 1 45 ? 22.25476  18.46588 16.87524  1.000 56.58579  ? 42  GLU C N   1 
ATOM   1609 C CA  . GLU C 1 45 ? 21.30815  19.54179 17.15337  1.000 48.59446  ? 42  GLU C CA  1 
ATOM   1610 C C   . GLU C 1 45 ? 21.49528  20.69507 16.17788  1.000 50.08143  ? 42  GLU C C   1 
ATOM   1611 O O   . GLU C 1 45 ? 20.51743  21.28333 15.70165  1.000 46.26861  ? 42  GLU C O   1 
ATOM   1612 C CB  . GLU C 1 45 ? 21.47010  20.03007 18.59659  1.000 52.93128  ? 42  GLU C CB  1 
ATOM   1613 C CG  . GLU C 1 45 ? 21.22234  18.97258 19.67046  1.000 55.59498  ? 42  GLU C CG  1 
ATOM   1614 C CD  . GLU C 1 45 ? 22.44110  18.10376 19.94532  1.000 66.31830  ? 42  GLU C CD  1 
ATOM   1615 O OE1 . GLU C 1 45 ? 23.09954  17.66194 18.97984  1.000 58.28839  ? 42  GLU C OE1 1 
ATOM   1616 O OE2 . GLU C 1 45 ? 22.74690  17.86738 21.13356  1.000 76.87083  ? 42  GLU C OE2 1 
ATOM   1617 N N   . GLN C 1 46 ? 22.74879  21.02417 15.86156  1.000 45.12137  ? 43  GLN C N   1 
ATOM   1618 C CA  . GLN C 1 46 ? 23.02030  22.11684 14.93565  1.000 45.89249  ? 43  GLN C CA  1 
ATOM   1619 C C   . GLN C 1 46 ? 22.67182  21.72613 13.50501  1.000 43.00436  ? 43  GLN C C   1 
ATOM   1620 O O   . GLN C 1 46 ? 22.10997  22.53176 12.75491  1.000 37.65637  ? 43  GLN C O   1 
ATOM   1621 C CB  . GLN C 1 46 ? 24.48748  22.52846 15.04060  1.000 47.65738  ? 43  GLN C CB  1 
ATOM   1622 C CG  . GLN C 1 46 ? 24.70701  24.01829 15.21635  1.000 53.87160  ? 43  GLN C CG  1 
ATOM   1623 C CD  . GLN C 1 46 ? 26.14795  24.35161 15.54709  1.000 65.87643  ? 43  GLN C CD  1 
ATOM   1624 O OE1 . GLN C 1 46 ? 27.01052  23.47325 15.56606  1.000 61.85404  ? 43  GLN C OE1 1 
ATOM   1625 N NE2 . GLN C 1 46 ? 26.41584  25.62381 15.81465  1.000 62.70426  ? 43  GLN C NE2 1 
ATOM   1626 N N   . VAL C 1 47 ? 22.99895  20.49367 13.11107  1.000 45.28570  ? 44  VAL C N   1 
ATOM   1627 C CA  . VAL C 1 47 ? 22.68349  20.02995 11.76201  1.000 39.08286  ? 44  VAL C CA  1 
ATOM   1628 C C   . VAL C 1 47 ? 21.18430  20.11692 11.50142  1.000 35.07316  ? 44  VAL C C   1 
ATOM   1629 O O   . VAL C 1 47 ? 20.74998  20.56352 10.43163  1.000 33.16221  ? 44  VAL C O   1 
ATOM   1630 C CB  . VAL C 1 47 ? 23.21780  18.59979 11.55768  1.000 40.24611  ? 44  VAL C CB  1 
ATOM   1631 C CG1 . VAL C 1 47 ? 22.65823  17.99241 10.28188  1.000 37.94704  ? 44  VAL C CG1 1 
ATOM   1632 C CG2 . VAL C 1 47 ? 24.74018  18.60200 11.53174  1.000 50.80907  ? 44  VAL C CG2 1 
ATOM   1633 N N   . ILE C 1 48 ? 20.36779  19.71140 12.47817  1.000 32.14066  ? 45  ILE C N   1 
ATOM   1634 C CA  . ILE C 1 48 ? 18.91783  19.74341 12.30136  1.000 40.37845  ? 45  ILE C CA  1 
ATOM   1635 C C   . ILE C 1 48 ? 18.43751  21.17520 12.08849  1.000 40.75374  ? 45  ILE C C   1 
ATOM   1636 O O   . ILE C 1 48 ? 17.59511  21.44272 11.22489  1.000 36.16316  ? 45  ILE C O   1 
ATOM   1637 C CB  . ILE C 1 48 ? 18.20937  19.08857 13.50064  1.000 42.19694  ? 45  ILE C CB  1 
ATOM   1638 C CG1 . ILE C 1 48 ? 18.48983  17.58694 13.54151  1.000 37.67458  ? 45  ILE C CG1 1 
ATOM   1639 C CG2 . ILE C 1 48 ? 16.70561  19.34396 13.44154  1.000 36.85000  ? 45  ILE C CG2 1 
ATOM   1640 C CD1 . ILE C 1 48 ? 17.82441  16.88419 14.70466  1.000 46.20853  ? 45  ILE C CD1 1 
ATOM   1641 N N   . LEU C 1 49 ? 18.96307  22.11478 12.88135  1.000 33.38555  ? 46  LEU C N   1 
ATOM   1642 C CA  . LEU C 1 49 ? 18.56757  23.51137 12.72188  1.000 38.44301  ? 46  LEU C CA  1 
ATOM   1643 C C   . LEU C 1 49 ? 19.00872  24.05623 11.37280  1.000 33.68347  ? 46  LEU C C   1 
ATOM   1644 O O   . LEU C 1 49 ? 18.26101  24.78985 10.71639  1.000 30.89219  ? 46  LEU C O   1 
ATOM   1645 C CB  . LEU C 1 49 ? 19.14766  24.36440 13.84763  1.000 34.91435  ? 46  LEU C CB  1 
ATOM   1646 C CG  . LEU C 1 49 ? 18.47965  24.28597 15.21779  1.000 36.85264  ? 46  LEU C CG  1 
ATOM   1647 C CD1 . LEU C 1 49 ? 18.99092  25.41987 16.07758  1.000 38.11405  ? 46  LEU C CD1 1 
ATOM   1648 C CD2 . LEU C 1 49 ? 16.96567  24.34053 15.09706  1.000 37.93209  ? 46  LEU C CD2 1 
ATOM   1649 N N   . LEU C 1 50 ? 20.22158  23.71001 10.94098  1.000 33.07801  ? 47  LEU C N   1 
ATOM   1650 C CA  . LEU C 1 50 ? 20.68742  24.17257 9.64023   1.000 34.34701  ? 47  LEU C CA  1 
ATOM   1651 C C   . LEU C 1 50 ? 19.81658  23.62478 8.51849   1.000 27.39053  ? 47  LEU C C   1 
ATOM   1652 O O   . LEU C 1 50 ? 19.49083  24.34862 7.57193   1.000 27.81438  ? 47  LEU C O   1 
ATOM   1653 C CB  . LEU C 1 50 ? 22.14851  23.78068 9.43341   1.000 26.87897  ? 47  LEU C CB  1 
ATOM   1654 C CG  . LEU C 1 50 ? 23.17809  24.81884 9.87955   1.000 45.59915  ? 47  LEU C CG  1 
ATOM   1655 C CD1 . LEU C 1 50 ? 23.04274  26.07929 9.05189   1.000 44.08675  ? 47  LEU C CD1 1 
ATOM   1656 C CD2 . LEU C 1 50 ? 23.02024  25.14359 11.34939  1.000 47.06593  ? 47  LEU C CD2 1 
ATOM   1657 N N   . LEU C 1 51 ? 19.42425  22.35207 8.61097   1.000 31.79113  ? 48  LEU C N   1 
ATOM   1658 C CA  . LEU C 1 51 ? 18.55179  21.77410 7.59468   1.000 39.23474  ? 48  LEU C CA  1 
ATOM   1659 C C   . LEU C 1 51 ? 17.15386  22.37776 7.64352   1.000 29.60602  ? 48  LEU C C   1 
ATOM   1660 O O   . LEU C 1 51 ? 16.47167  22.43351 6.61530   1.000 36.24571  ? 48  LEU C O   1 
ATOM   1661 C CB  . LEU C 1 51 ? 18.49065  20.25653 7.75945   1.000 28.00648  ? 48  LEU C CB  1 
ATOM   1662 C CG  . LEU C 1 51 ? 19.81399  19.54286 7.46888   1.000 36.88583  ? 48  LEU C CG  1 
ATOM   1663 C CD1 . LEU C 1 51 ? 19.68166  18.05032 7.68652   1.000 45.04540  ? 48  LEU C CD1 1 
ATOM   1664 C CD2 . LEU C 1 51 ? 20.28141  19.83998 6.05306   1.000 39.64430  ? 48  LEU C CD2 1 
ATOM   1665 N N   . ILE C 1 52 ? 16.70488  22.81896 8.82051   1.000 37.39467  ? 49  ILE C N   1 
ATOM   1666 C CA  . ILE C 1 52 ? 15.46441  23.58412 8.89268   1.000 36.80303  ? 49  ILE C CA  1 
ATOM   1667 C C   . ILE C 1 52 ? 15.65196  24.94226 8.23198   1.000 36.24777  ? 49  ILE C C   1 
ATOM   1668 O O   . ILE C 1 52 ? 14.77565  25.42240 7.50319   1.000 32.88742  ? 49  ILE C O   1 
ATOM   1669 C CB  . ILE C 1 52 ? 14.99765  23.71356 10.35457  1.000 39.00402  ? 49  ILE C CB  1 
ATOM   1670 C CG1 . ILE C 1 52 ? 13.98967  22.61552 10.70177  1.000 41.81740  ? 49  ILE C CG1 1 
ATOM   1671 C CG2 . ILE C 1 52 ? 14.38153  25.08071 10.61004  1.000 37.85868  ? 49  ILE C CG2 1 
ATOM   1672 C CD1 . ILE C 1 52 ? 14.53583  21.19984 10.61634  1.000 45.02954  ? 49  ILE C CD1 1 
ATOM   1673 N N   . HIS C 1 53 ? 16.80893  25.57151 8.45581   1.000 39.58564  ? 50  HIS C N   1 
ATOM   1674 C CA  . HIS C 1 53 ? 17.15026  26.78199 7.71916   1.000 33.65246  ? 50  HIS C CA  1 
ATOM   1675 C C   . HIS C 1 53 ? 17.17939  26.52543 6.21987   1.000 36.09704  ? 50  HIS C C   1 
ATOM   1676 O O   . HIS C 1 53 ? 16.77141  27.38908 5.43485   1.000 26.66464  ? 50  HIS C O   1 
ATOM   1677 C CB  . HIS C 1 53 ? 18.50076  27.31449 8.19949   1.000 32.38562  ? 50  HIS C CB  1 
ATOM   1678 C CG  . HIS C 1 53 ? 18.94085  28.57232 7.51509   1.000 34.07933  ? 50  HIS C CG  1 
ATOM   1679 N ND1 . HIS C 1 53 ? 18.38785  29.80347 7.79328   1.000 38.32554  ? 50  HIS C ND1 1 
ATOM   1680 C CD2 . HIS C 1 53 ? 19.88379  28.79008 6.56765   1.000 33.92487  ? 50  HIS C CD2 1 
ATOM   1681 C CE1 . HIS C 1 53 ? 18.97076  30.72570 7.04831   1.000 42.48398  ? 50  HIS C CE1 1 
ATOM   1682 N NE2 . HIS C 1 53 ? 19.88290  30.13718 6.29576   1.000 32.49188  ? 50  HIS C NE2 1 
ATOM   1683 N N   . PHE C 1 54 ? 17.65496  25.34786 5.80614   1.000 35.41219  ? 51  PHE C N   1 
ATOM   1684 C CA  . PHE C 1 54 ? 17.63324  24.99062 4.39143   1.000 38.93472  ? 51  PHE C CA  1 
ATOM   1685 C C   . PHE C 1 54 ? 16.20715  24.94009 3.86380   1.000 32.21789  ? 51  PHE C C   1 
ATOM   1686 O O   . PHE C 1 54 ? 15.92409  25.41564 2.75861   1.000 31.20180  ? 51  PHE C O   1 
ATOM   1687 C CB  . PHE C 1 54 ? 18.32378  23.64215 4.17505   1.000 34.66988  ? 51  PHE C CB  1 
ATOM   1688 C CG  . PHE C 1 54 ? 18.22273  23.13247 2.76176   1.000 28.31201  ? 51  PHE C CG  1 
ATOM   1689 C CD1 . PHE C 1 54 ? 17.14529  22.35361 2.36113   1.000 30.53856  ? 51  PHE C CD1 1 
ATOM   1690 C CD2 . PHE C 1 54 ? 19.19571  23.44425 1.83195   1.000 33.49420  ? 51  PHE C CD2 1 
ATOM   1691 C CE1 . PHE C 1 54 ? 17.04177  21.90304 1.06306   1.000 33.08840  ? 51  PHE C CE1 1 
ATOM   1692 C CE2 . PHE C 1 54 ? 19.09848  22.99048 0.53148   1.000 36.96220  ? 51  PHE C CE2 1 
ATOM   1693 C CZ  . PHE C 1 54 ? 18.02167  22.21939 0.14687   1.000 29.07501  ? 51  PHE C CZ  1 
ATOM   1694 N N   . LEU C 1 55 ? 15.30088  24.32754 4.62805   1.000 31.44241  ? 52  LEU C N   1 
ATOM   1695 C CA  . LEU C 1 55 ? 13.91994  24.21174 4.17696   1.000 39.87256  ? 52  LEU C CA  1 
ATOM   1696 C C   . LEU C 1 55 ? 13.25335  25.57597 4.08082   1.000 37.12665  ? 52  LEU C C   1 
ATOM   1697 O O   . LEU C 1 55 ? 12.44778  25.81141 3.17322   1.000 39.77525  ? 52  LEU C O   1 
ATOM   1698 C CB  . LEU C 1 55 ? 13.14376  23.28722 5.11380   1.000 42.88106  ? 52  LEU C CB  1 
ATOM   1699 C CG  . LEU C 1 55 ? 13.66288  21.84683 5.17729   1.000 44.01181  ? 52  LEU C CG  1 
ATOM   1700 C CD1 . LEU C 1 55 ? 12.99917  21.06954 6.30228   1.000 45.15458  ? 52  LEU C CD1 1 
ATOM   1701 C CD2 . LEU C 1 55 ? 13.46885  21.13443 3.84526   1.000 37.12742  ? 52  LEU C CD2 1 
ATOM   1702 N N   . LEU C 1 56 ? 13.58610  26.48947 4.99343   1.000 40.03621  ? 53  LEU C N   1 
ATOM   1703 C CA  . LEU C 1 56 ? 13.07967  27.85324 4.89466   1.000 31.03677  ? 53  LEU C CA  1 
ATOM   1704 C C   . LEU C 1 56 ? 13.59116  28.53409 3.63189   1.000 36.19752  ? 53  LEU C C   1 
ATOM   1705 O O   . LEU C 1 56 ? 12.81514  29.13529 2.87986   1.000 34.32073  ? 53  LEU C O   1 
ATOM   1706 C CB  . LEU C 1 56 ? 13.48163  28.64591 6.13739   1.000 36.24744  ? 53  LEU C CB  1 
ATOM   1707 C CG  . LEU C 1 56 ? 12.93918  28.09820 7.45673   1.000 33.59168  ? 53  LEU C CG  1 
ATOM   1708 C CD1 . LEU C 1 56 ? 13.61561  28.77268 8.63701   1.000 33.08669  ? 53  LEU C CD1 1 
ATOM   1709 C CD2 . LEU C 1 56 ? 11.43175  28.28142 7.51425   1.000 37.63153  ? 53  LEU C CD2 1 
ATOM   1710 N N   . LEU C 1 57 ? 14.90039  28.44226 3.38282   1.000 32.16815  ? 54  LEU C N   1 
ATOM   1711 C CA  . LEU C 1 57 ? 15.48590  29.05689 2.19568   1.000 33.64968  ? 54  LEU C CA  1 
ATOM   1712 C C   . LEU C 1 57 ? 14.85573  28.52040 0.91929   1.000 33.42181  ? 54  LEU C C   1 
ATOM   1713 O O   . LEU C 1 57 ? 14.57140  29.28359 -0.01213  1.000 38.93573  ? 54  LEU C O   1 
ATOM   1714 C CB  . LEU C 1 57 ? 16.99104  28.80792 2.17283   1.000 30.38851  ? 54  LEU C CB  1 
ATOM   1715 C CG  . LEU C 1 57 ? 17.83284  29.53452 3.21129   1.000 37.16417  ? 54  LEU C CG  1 
ATOM   1716 C CD1 . LEU C 1 57 ? 19.26690  29.04901 3.13217   1.000 34.98171  ? 54  LEU C CD1 1 
ATOM   1717 C CD2 . LEU C 1 57 ? 17.74796  31.02695 2.96469   1.000 32.90237  ? 54  LEU C CD2 1 
ATOM   1718 N N   . SER C 1 58 ? 14.63824  27.20867 0.85693   1.000 28.42270  ? 55  SER C N   1 
ATOM   1719 C CA  . SER C 1 58 ? 14.18588  26.55154 -0.36076  1.000 41.17504  ? 55  SER C CA  1 
ATOM   1720 C C   . SER C 1 58 ? 12.66682  26.56505 -0.49335  1.000 37.80942  ? 55  SER C C   1 
ATOM   1721 O O   . SER C 1 58 ? 12.13593  27.00390 -1.51721  1.000 44.29166  ? 55  SER C O   1 
ATOM   1722 C CB  . SER C 1 58 ? 14.71315  25.11357 -0.39453  1.000 27.01726  ? 55  SER C CB  1 
ATOM   1723 O OG  . SER C 1 58 ? 14.46687  24.44900 0.83210   1.000 36.09337  ? 55  SER C OG  1 
ATOM   1724 N N   . LEU C 1 59 ? 11.95748  26.08813 0.53145   1.000 43.70759  ? 56  LEU C N   1 
ATOM   1725 C CA  . LEU C 1 59 ? 10.50601  25.95640 0.44578   1.000 41.51430  ? 56  LEU C CA  1 
ATOM   1726 C C   . LEU C 1 59 ? 9.79209   27.27263 0.72300   1.000 40.76018  ? 56  LEU C C   1 
ATOM   1727 O O   . LEU C 1 59 ? 8.83611   27.61944 0.02119   1.000 43.97226  ? 56  LEU C O   1 
ATOM   1728 C CB  . LEU C 1 59 ? 10.01795  24.88906 1.42308   1.000 40.60416  ? 56  LEU C CB  1 
ATOM   1729 C CG  . LEU C 1 59 ? 10.60657  23.49612 1.22917   1.000 44.31563  ? 56  LEU C CG  1 
ATOM   1730 C CD1 . LEU C 1 59 ? 10.26155  22.61534 2.41286   1.000 54.18039  ? 56  LEU C CD1 1 
ATOM   1731 C CD2 . LEU C 1 59 ? 10.08724  22.89364 -0.06053  1.000 55.28865  ? 56  LEU C CD2 1 
ATOM   1732 N N   . VAL C 1 60 ? 10.22936  28.01205 1.74160   1.000 38.98301  ? 57  VAL C N   1 
ATOM   1733 C CA  . VAL C 1 60 ? 9.51553   29.22265 2.13436   1.000 41.41147  ? 57  VAL C CA  1 
ATOM   1734 C C   . VAL C 1 60 ? 9.96603   30.41334 1.29804   1.000 38.82701  ? 57  VAL C C   1 
ATOM   1735 O O   . VAL C 1 60 ? 9.14186   31.13313 0.72319   1.000 40.32834  ? 57  VAL C O   1 
ATOM   1736 C CB  . VAL C 1 60 ? 9.69975   29.48526 3.63981   1.000 39.88172  ? 57  VAL C CB  1 
ATOM   1737 C CG1 . VAL C 1 60 ? 8.82251   30.64453 4.08402   1.000 41.01940  ? 57  VAL C CG1 1 
ATOM   1738 C CG2 . VAL C 1 60 ? 9.38364   28.22830 4.43548   1.000 48.13197  ? 57  VAL C CG2 1 
ATOM   1739 N N   . LYS C 1 61 ? 11.27802  30.64351 1.21966   1.000 37.68291  ? 58  LYS C N   1 
ATOM   1740 C CA  . LYS C 1 61 ? 11.79959  31.76658 0.44993   1.000 36.89076  ? 58  LYS C CA  1 
ATOM   1741 C C   . LYS C 1 61 ? 11.84699  31.48549 -1.04540  1.000 39.98826  ? 58  LYS C C   1 
ATOM   1742 O O   . LYS C 1 61 ? 11.97176  32.42701 -1.83434  1.000 42.47635  ? 58  LYS C O   1 
ATOM   1743 C CB  . LYS C 1 61 ? 13.20014  32.13930 0.94236   1.000 37.53732  ? 58  LYS C CB  1 
ATOM   1744 C CG  . LYS C 1 61 ? 13.24786  32.59672 2.38983   1.000 35.21679  ? 58  LYS C CG  1 
ATOM   1745 C CD  . LYS C 1 61 ? 12.30467  33.76323 2.61532   1.000 48.23105  ? 58  LYS C CD  1 
ATOM   1746 C CE  . LYS C 1 61 ? 12.41152  34.30355 4.02939   1.000 50.18750  ? 58  LYS C CE  1 
ATOM   1747 N NZ  . LYS C 1 61 ? 11.59213  35.53440 4.19738   1.000 51.00657  ? 58  LYS C NZ  1 
ATOM   1748 N N   . GLY C 1 62 ? 11.75531  30.22215 -1.45263  1.000 33.42656  ? 59  GLY C N   1 
ATOM   1749 C CA  . GLY C 1 62 ? 11.80806  29.90229 -2.86447  1.000 38.22891  ? 59  GLY C CA  1 
ATOM   1750 C C   . GLY C 1 62 ? 13.12079  30.21672 -3.54098  1.000 38.79623  ? 59  GLY C C   1 
ATOM   1751 O O   . GLY C 1 62 ? 13.14767  30.40173 -4.76024  1.000 45.93452  ? 59  GLY C O   1 
ATOM   1752 N N   . LEU C 1 63 ? 14.21315  30.28845 -2.78542  1.000 33.31022  ? 60  LEU C N   1 
ATOM   1753 C CA  . LEU C 1 63 ? 15.51375  30.55390 -3.37936  1.000 37.48262  ? 60  LEU C CA  1 
ATOM   1754 C C   . LEU C 1 63 ? 16.00331  29.33373 -4.14906  1.000 34.13334  ? 60  LEU C C   1 
ATOM   1755 O O   . LEU C 1 63 ? 15.68559  28.19012 -3.81447  1.000 32.74077  ? 60  LEU C O   1 
ATOM   1756 C CB  . LEU C 1 63 ? 16.52526  30.93881 -2.30108  1.000 33.01987  ? 60  LEU C CB  1 
ATOM   1757 C CG  . LEU C 1 63 ? 16.09948  32.11535 -1.42137  1.000 37.54613  ? 60  LEU C CG  1 
ATOM   1758 C CD1 . LEU C 1 63 ? 17.18030  32.45306 -0.41335  1.000 39.82981  ? 60  LEU C CD1 1 
ATOM   1759 C CD2 . LEU C 1 63 ? 15.76207  33.32480 -2.27819  1.000 37.81011  ? 60  LEU C CD2 1 
ATOM   1760 N N   . SER C 1 64 ? 16.78148  29.58912 -5.19926  1.000 36.85866  ? 61  SER C N   1 
ATOM   1761 C CA  . SER C 1 64 ? 17.29863  28.50577 -6.01535  1.000 40.73370  ? 61  SER C CA  1 
ATOM   1762 C C   . SER C 1 64 ? 18.21455  27.60783 -5.18592  1.000 41.19716  ? 61  SER C C   1 
ATOM   1763 O O   . SER C 1 64 ? 18.70535  28.01105 -4.12853  1.000 40.06435  ? 61  SER C O   1 
ATOM   1764 C CB  . SER C 1 64 ? 18.05318  29.06177 -7.22251  1.000 44.76080  ? 61  SER C CB  1 
ATOM   1765 O OG  . SER C 1 64 ? 19.20545  29.78913 -6.83072  1.000 42.42460  ? 61  SER C OG  1 
ATOM   1766 N N   . PRO C 1 65 ? 18.43715  26.37018 -5.63470  1.000 36.41700  ? 62  PRO C N   1 
ATOM   1767 C CA  . PRO C 1 65 ? 19.38981  25.50445 -4.92300  1.000 47.32882  ? 62  PRO C CA  1 
ATOM   1768 C C   . PRO C 1 65 ? 20.77554  26.11110 -4.80639  1.000 42.88028  ? 62  PRO C C   1 
ATOM   1769 O O   . PRO C 1 65 ? 21.44067  25.91817 -3.78087  1.000 38.41450  ? 62  PRO C O   1 
ATOM   1770 C CB  . PRO C 1 65 ? 19.39678  24.22602 -5.77267  1.000 51.52240  ? 62  PRO C CB  1 
ATOM   1771 C CG  . PRO C 1 65 ? 18.06256  24.21543 -6.43642  1.000 47.68111  ? 62  PRO C CG  1 
ATOM   1772 C CD  . PRO C 1 65 ? 17.73647  25.65254 -6.71432  1.000 47.76035  ? 62  PRO C CD  1 
ATOM   1773 N N   . GLU C 1 66 ? 21.22206  26.85340 -5.82352  1.000 39.24197  ? 63  GLU C N   1 
ATOM   1774 C CA  . GLU C 1 66 ? 22.54800  27.46239 -5.78075  1.000 45.51281  ? 63  GLU C CA  1 
ATOM   1775 C C   . GLU C 1 66 ? 22.59690  28.62391 -4.79498  1.000 46.48608  ? 63  GLU C C   1 
ATOM   1776 O O   . GLU C 1 66 ? 23.57691  28.77750 -4.05604  1.000 46.74036  ? 63  GLU C O   1 
ATOM   1777 C CB  . GLU C 1 66 ? 22.95606  27.92960 -7.17790  1.000 47.50030  ? 63  GLU C CB  1 
ATOM   1778 C CG  . GLU C 1 66 ? 24.30253  28.62436 -7.20916  1.000 69.07237  ? 63  GLU C CG  1 
ATOM   1779 C CD  . GLU C 1 66 ? 25.39663  27.77851 -6.58929  1.000 81.67225  ? 63  GLU C CD  1 
ATOM   1780 O OE1 . GLU C 1 66 ? 25.56322  26.61631 -7.01455  1.000 78.70832  ? 63  GLU C OE1 1 
ATOM   1781 O OE2 . GLU C 1 66 ? 26.08157  28.26944 -5.66746  1.000 70.60926  ? 63  GLU C OE2 1 
ATOM   1782 N N   . THR C 1 67 ? 21.55672  29.46017 -4.77644  1.000 40.15222  ? 64  THR C N   1 
ATOM   1783 C CA  . THR C 1 67 ? 21.49855  30.53642 -3.79227  1.000 38.06734  ? 64  THR C CA  1 
ATOM   1784 C C   . THR C 1 67 ? 21.30911  29.97896 -2.38733  1.000 39.68783  ? 64  THR C C   1 
ATOM   1785 O O   . THR C 1 67 ? 21.90611  30.47920 -1.42587  1.000 38.22242  ? 64  THR C O   1 
ATOM   1786 C CB  . THR C 1 67 ? 20.37485  31.51036 -4.14823  1.000 38.52792  ? 64  THR C CB  1 
ATOM   1787 O OG1 . THR C 1 67 ? 20.66622  32.13447 -5.40494  1.000 41.90494  ? 64  THR C OG1 1 
ATOM   1788 C CG2 . THR C 1 67 ? 20.22564  32.57888 -3.07674  1.000 42.16406  ? 64  THR C CG2 1 
ATOM   1789 N N   . THR C 1 68 ? 20.49100  28.93326 -2.25472  1.000 35.07514  ? 65  THR C N   1 
ATOM   1790 C CA  . THR C 1 68 ? 20.32259  28.27321 -0.96520  1.000 35.01774  ? 65  THR C CA  1 
ATOM   1791 C C   . THR C 1 68 ? 21.64240  27.69347 -0.47413  1.000 39.89173  ? 65  THR C C   1 
ATOM   1792 O O   . THR C 1 68 ? 22.01874  27.87502 0.68968   1.000 35.60505  ? 65  THR C O   1 
ATOM   1793 C CB  . THR C 1 68 ? 19.26210  27.17715 -1.07459  1.000 35.05775  ? 65  THR C CB  1 
ATOM   1794 O OG1 . THR C 1 68 ? 18.02303  27.74723 -1.51925  1.000 36.96208  ? 65  THR C OG1 1 
ATOM   1795 C CG2 . THR C 1 68 ? 19.05414  26.51037 0.26678   1.000 37.41262  ? 65  THR C CG2 1 
ATOM   1796 N N   . LYS C 1 69 ? 22.36116  26.98932 -1.35415  1.000 40.42262  ? 66  LYS C N   1 
ATOM   1797 C CA  . LYS C 1 69 ? 23.67081  26.45706 -0.98934  1.000 39.22498  ? 66  LYS C CA  1 
ATOM   1798 C C   . LYS C 1 69 ? 24.61675  27.57172 -0.56211  1.000 39.07202  ? 66  LYS C C   1 
ATOM   1799 O O   . LYS C 1 69 ? 25.36591  27.42319 0.41075   1.000 41.34821  ? 66  LYS C O   1 
ATOM   1800 C CB  . LYS C 1 69 ? 24.26285  25.66893 -2.15986  1.000 40.82132  ? 66  LYS C CB  1 
ATOM   1801 C CG  . LYS C 1 69 ? 25.68144  25.17680 -1.92446  1.000 45.13026  ? 66  LYS C CG  1 
ATOM   1802 C CD  . LYS C 1 69 ? 26.06503  24.09264 -2.91952  1.000 59.72062  ? 66  LYS C CD  1 
ATOM   1803 C CE  . LYS C 1 69 ? 25.95700  24.57884 -4.35662  1.000 50.23180  ? 66  LYS C CE  1 
ATOM   1804 N NZ  . LYS C 1 69 ? 26.23882  23.48371 -5.32989  1.000 70.11803  ? 66  LYS C NZ  1 
ATOM   1805 N N   . LEU C 1 70 ? 24.58467  28.70165 -1.27109  1.000 41.98922  ? 67  LEU C N   1 
ATOM   1806 C CA  . LEU C 1 70 ? 25.44054  29.82919 -0.91781  1.000 50.48639  ? 67  LEU C CA  1 
ATOM   1807 C C   . LEU C 1 70 ? 25.10906  30.34769 0.47784   1.000 43.44237  ? 67  LEU C C   1 
ATOM   1808 O O   . LEU C 1 70 ? 26.00162  30.53068 1.31396   1.000 38.83366  ? 67  LEU C O   1 
ATOM   1809 C CB  . LEU C 1 70 ? 25.29710  30.93166 -1.97130  1.000 46.30230  ? 67  LEU C CB  1 
ATOM   1810 C CG  . LEU C 1 70 ? 26.29045  32.09763 -2.01750  1.000 52.40216  ? 67  LEU C CG  1 
ATOM   1811 C CD1 . LEU C 1 70 ? 25.87191  33.22659 -1.08774  1.000 50.03199  ? 67  LEU C CD1 1 
ATOM   1812 C CD2 . LEU C 1 70 ? 27.69929  31.62332 -1.69091  1.000 55.74281  ? 67  LEU C CD2 1 
ATOM   1813 N N   . LEU C 1 71 ? 23.82231  30.57096 0.75578   1.000 38.26931  ? 68  LEU C N   1 
ATOM   1814 C CA  . LEU C 1 71 ? 23.43424  31.06427 2.07236   1.000 34.33271  ? 68  LEU C CA  1 
ATOM   1815 C C   . LEU C 1 71 ? 23.65475  30.01709 3.15580   1.000 35.84223  ? 68  LEU C C   1 
ATOM   1816 O O   . LEU C 1 71 ? 23.92572  30.37175 4.30804   1.000 39.60316  ? 68  LEU C O   1 
ATOM   1817 C CB  . LEU C 1 71 ? 21.97635  31.51952 2.05633   1.000 34.02604  ? 68  LEU C CB  1 
ATOM   1818 C CG  . LEU C 1 71 ? 21.71304  32.80745 1.27228   1.000 43.05404  ? 68  LEU C CG  1 
ATOM   1819 C CD1 . LEU C 1 71 ? 20.25204  33.20567 1.36592   1.000 41.25182  ? 68  LEU C CD1 1 
ATOM   1820 C CD2 . LEU C 1 71 ? 22.60818  33.93488 1.76508   1.000 43.38587  ? 68  LEU C CD2 1 
ATOM   1821 N N   . MET C 1 72 ? 23.54134  28.73150 2.81623   1.000 37.35151  ? 69  MET C N   1 
ATOM   1822 C CA  . MET C 1 72 ? 23.85324  27.69353 3.79288   1.000 35.91935  ? 69  MET C CA  1 
ATOM   1823 C C   . MET C 1 72 ? 25.32634  27.73486 4.17940   1.000 38.16235  ? 69  MET C C   1 
ATOM   1824 O O   . MET C 1 72 ? 25.66751  27.64426 5.36399   1.000 36.69125  ? 69  MET C O   1 
ATOM   1825 C CB  . MET C 1 72 ? 23.48534  26.31471 3.24475   1.000 35.99855  ? 69  MET C CB  1 
ATOM   1826 C CG  . MET C 1 72 ? 21.99039  26.04181 3.12404   1.000 36.40743  ? 69  MET C CG  1 
ATOM   1827 S SD  . MET C 1 72 ? 21.11335  26.17122 4.68681   1.000 38.60039  ? 69  MET C SD  1 
ATOM   1828 C CE  . MET C 1 72 ? 22.01581  24.98645 5.68137   1.000 35.09201  ? 69  MET C CE  1 
ATOM   1829 N N   . LYS C 1 73 ? 26.21370  27.88918 3.19520   1.000 45.41600  ? 70  LYS C N   1 
ATOM   1830 C CA  . LYS C 1 73 ? 27.63849  27.95506 3.50103   1.000 46.71124  ? 70  LYS C CA  1 
ATOM   1831 C C   . LYS C 1 73 ? 27.99201  29.22653 4.26276   1.000 42.08118  ? 70  LYS C C   1 
ATOM   1832 O O   . LYS C 1 73 ? 28.96894  29.23999 5.01995   1.000 50.45546  ? 70  LYS C O   1 
ATOM   1833 C CB  . LYS C 1 73 ? 28.45585  27.84706 2.21484   1.000 48.17923  ? 70  LYS C CB  1 
ATOM   1834 C CG  . LYS C 1 73 ? 28.30427  26.50765 1.51316   1.000 43.33038  ? 70  LYS C CG  1 
ATOM   1835 C CD  . LYS C 1 73 ? 29.31822  26.34905 0.40037   1.000 59.88186  ? 70  LYS C CD  1 
ATOM   1836 C CE  . LYS C 1 73 ? 29.15441  25.01196 -0.29600  1.000 62.39059  ? 70  LYS C CE  1 
ATOM   1837 N NZ  . LYS C 1 73 ? 30.26254  24.75045 -1.25407  1.000 75.36937  ? 70  LYS C NZ  1 
ATOM   1838 N N   . GLU C 1 74 ? 27.21142  30.29556 4.08791   1.000 41.63956  ? 71  GLU C N   1 
ATOM   1839 C CA  . GLU C 1 74 ? 27.44804  31.51282 4.85706   1.000 47.90103  ? 71  GLU C CA  1 
ATOM   1840 C C   . GLU C 1 74 ? 27.03291  31.33528 6.31069   1.000 50.33647  ? 71  GLU C C   1 
ATOM   1841 O O   . GLU C 1 74 ? 27.72873  31.79987 7.22168   1.000 55.31361  ? 71  GLU C O   1 
ATOM   1842 C CB  . GLU C 1 74 ? 26.70493  32.68883 4.22542   1.000 44.78799  ? 71  GLU C CB  1 
ATOM   1843 C CG  . GLU C 1 74 ? 27.47883  33.35992 3.11416   1.000 61.06380  ? 71  GLU C CG  1 
ATOM   1844 C CD  . GLU C 1 74 ? 28.84550  33.82331 3.57834   1.000 63.90003  ? 71  GLU C CD  1 
ATOM   1845 O OE1 . GLU C 1 74 ? 28.90453  34.66768 4.49769   1.000 63.15946  ? 71  GLU C OE1 1 
ATOM   1846 O OE2 . GLU C 1 74 ? 29.85932  33.33239 3.03804   1.000 81.41912  ? 71  GLU C OE2 1 
ATOM   1847 N N   . LEU C 1 75 ? 25.90509  30.66152 6.54904   1.000 42.84704  ? 72  LEU C N   1 
ATOM   1848 C CA  . LEU C 1 75 ? 25.48512  30.40291 7.92156   1.000 42.95638  ? 72  LEU C CA  1 
ATOM   1849 C C   . LEU C 1 75 ? 26.43389  29.43034 8.61117   1.000 44.80119  ? 72  LEU C C   1 
ATOM   1850 O O   . LEU C 1 75 ? 26.71049  29.56915 9.80824   1.000 47.84099  ? 72  LEU C O   1 
ATOM   1851 C CB  . LEU C 1 75 ? 24.05257  29.87228 7.94441   1.000 48.02973  ? 72  LEU C CB  1 
ATOM   1852 C CG  . LEU C 1 75 ? 23.40695  29.78211 9.32609   1.000 47.45049  ? 72  LEU C CG  1 
ATOM   1853 C CD1 . LEU C 1 75 ? 23.66189  31.05405 10.11777  1.000 46.11976  ? 72  LEU C CD1 1 
ATOM   1854 C CD2 . LEU C 1 75 ? 21.91813  29.53343 9.19057   1.000 47.32645  ? 72  LEU C CD2 1 
ATOM   1855 N N   . ILE C 1 76 ? 26.94128  28.43952 7.87358   1.000 39.77971  ? 73  ILE C N   1 
ATOM   1856 C CA  . ILE C 1 76 ? 27.95967  27.55035 8.42631   1.000 51.56467  ? 73  ILE C CA  1 
ATOM   1857 C C   . ILE C 1 76 ? 29.21512  28.33913 8.77487   1.000 46.51640  ? 73  ILE C C   1 
ATOM   1858 O O   . ILE C 1 76 ? 29.83795  28.11392 9.81975   1.000 58.89770  ? 73  ILE C O   1 
ATOM   1859 C CB  . ILE C 1 76 ? 28.26284  26.40453 7.44287   1.000 50.40104  ? 73  ILE C CB  1 
ATOM   1860 C CG1 . ILE C 1 76 ? 27.04086  25.50193 7.28139   1.000 47.14428  ? 73  ILE C CG1 1 
ATOM   1861 C CG2 . ILE C 1 76 ? 29.45490  25.58793 7.91664   1.000 52.54549  ? 73  ILE C CG2 1 
ATOM   1862 C CD1 . ILE C 1 76 ? 27.20371  24.45856 6.20645   1.000 44.18643  ? 73  ILE C CD1 1 
ATOM   1863 N N   . LYS C 1 77 ? 29.59955  29.28199 7.90862   1.000 43.97438  ? 74  LYS C N   1 
ATOM   1864 C CA  . LYS C 1 77 ? 30.72860  30.15820 8.20780   1.000 55.22490  ? 74  LYS C CA  1 
ATOM   1865 C C   . LYS C 1 77 ? 30.50417  30.92228 9.50649   1.000 61.47451  ? 74  LYS C C   1 
ATOM   1866 O O   . LYS C 1 77 ? 31.42692  31.07391 10.31467  1.000 59.94766  ? 74  LYS C O   1 
ATOM   1867 C CB  . LYS C 1 77 ? 30.95945  31.12820 7.04779   1.000 49.88983  ? 74  LYS C CB  1 
ATOM   1868 C CG  . LYS C 1 77 ? 32.03161  32.17008 7.30749   1.000 71.89794  ? 74  LYS C CG  1 
ATOM   1869 C CD  . LYS C 1 77 ? 33.40881  31.53465 7.37354   1.000 74.51557  ? 74  LYS C CD  1 
ATOM   1870 C CE  . LYS C 1 77 ? 34.47259  32.55644 7.73787   1.000 69.81486  ? 74  LYS C CE  1 
ATOM   1871 N NZ  . LYS C 1 77 ? 35.83043  31.94908 7.73975   1.000 68.49220  ? 74  LYS C NZ  1 
ATOM   1872 N N   . GLU C 1 78 ? 29.28405  31.40339 9.72936   1.000 51.85764  ? 75  GLU C N   1 
ATOM   1873 C CA  . GLU C 1 78 ? 28.96021  32.10910 10.96092  1.000 63.76049  ? 75  GLU C CA  1 
ATOM   1874 C C   . GLU C 1 78 ? 28.76481  31.17273 12.14650  1.000 68.50423  ? 75  GLU C C   1 
ATOM   1875 O O   . GLU C 1 78 ? 28.60677  31.65582 13.27233  1.000 76.21886  ? 75  GLU C O   1 
ATOM   1876 C CB  . GLU C 1 78 ? 27.70704  32.96482 10.75762  1.000 61.05805  ? 75  GLU C CB  1 
ATOM   1877 C CG  . GLU C 1 78 ? 27.90062  34.11657 9.78476   1.000 60.55171  ? 75  GLU C CG  1 
ATOM   1878 C CD  . GLU C 1 78 ? 26.58704  34.69575 9.30295   1.000 67.82235  ? 75  GLU C CD  1 
ATOM   1879 O OE1 . GLU C 1 78 ? 25.58170  33.95615 9.30265   1.000 62.52021  ? 75  GLU C OE1 1 
ATOM   1880 O OE2 . GLU C 1 78 ? 26.55794  35.88724 8.92760   1.000 84.05530  ? 75  GLU C OE2 1 
ATOM   1881 N N   . LEU C 1 79 ? 28.76857  29.85502 11.92869  1.000 56.89968  ? 76  LEU C N   1 
ATOM   1882 C CA  . LEU C 1 79 ? 28.65247  28.92275 13.04545  1.000 67.35611  ? 76  LEU C CA  1 
ATOM   1883 C C   . LEU C 1 79 ? 29.97744  28.76074 13.77843  1.000 71.16873  ? 76  LEU C C   1 
ATOM   1884 O O   . LEU C 1 79 ? 30.03276  28.89567 15.00544  1.000 67.18009  ? 76  LEU C O   1 
ATOM   1885 C CB  . LEU C 1 79 ? 28.14911  27.56583 12.55940  1.000 63.73954  ? 76  LEU C CB  1 
ATOM   1886 C CG  . LEU C 1 79 ? 26.65325  27.44867 12.27951  1.000 61.96556  ? 76  LEU C CG  1 
ATOM   1887 C CD1 . LEU C 1 79 ? 26.26130  25.98905 12.29331  1.000 64.43564  ? 76  LEU C CD1 1 
ATOM   1888 C CD2 . LEU C 1 79 ? 25.84024  28.24731 13.29082  1.000 47.58588  ? 76  LEU C CD2 1 
ATOM   1889 N N   . GLU C 1 80 ? 31.05117  28.45463 13.04300  1.000 83.29471  ? 77  GLU C N   1 
ATOM   1890 C CA  . GLU C 1 80 ? 32.37259  28.37133 13.65621  1.000 97.32055  ? 77  GLU C CA  1 
ATOM   1891 C C   . GLU C 1 80 ? 32.78173  29.70123 14.27486  1.000 92.78026  ? 77  GLU C C   1 
ATOM   1892 O O   . GLU C 1 80 ? 33.61736  29.73224 15.18514  1.000 102.28682 ? 77  GLU C O   1 
ATOM   1893 C CB  . GLU C 1 80 ? 33.40162  27.92193 12.61819  1.000 91.57683  ? 77  GLU C CB  1 
ATOM   1894 C CG  . GLU C 1 80 ? 33.48276  28.82978 11.40313  1.000 88.99977  ? 77  GLU C CG  1 
ATOM   1895 C CD  . GLU C 1 80 ? 34.40697  28.29295 10.33135  1.000 98.83707  ? 77  GLU C CD  1 
ATOM   1896 O OE1 . GLU C 1 80 ? 34.69375  27.07769 10.34649  1.000 104.97861 ? 77  GLU C OE1 1 
ATOM   1897 O OE2 . GLU C 1 80 ? 34.84743  29.08788 9.47459   1.000 100.00799 ? 77  GLU C OE2 1 
ATOM   1898 N N   . LYS C 1 81 ? 32.20841  30.80143 13.79768  1.000 87.80791  ? 78  LYS C N   1 
ATOM   1899 C CA  . LYS C 1 81 ? 32.43820  32.11503 14.38081  1.000 92.87290  ? 78  LYS C CA  1 
ATOM   1900 C C   . LYS C 1 81 ? 31.13619  32.90464 14.45475  1.000 96.56619  ? 78  LYS C C   1 
ATOM   1901 O O   . LYS C 1 81 ? 30.30483  32.66744 15.33210  1.000 93.15261  ? 78  LYS C O   1 
ATOM   1902 C CB  . LYS C 1 81 ? 33.48318  32.88564 13.57529  1.000 107.29756 ? 78  LYS C CB  1 
ATOM   1903 C CG  . LYS C 1 81 ? 34.89722  32.72405 14.10094  1.000 114.10573 ? 78  LYS C CG  1 
ATOM   1904 C CD  . LYS C 1 81 ? 34.97116  33.16045 15.55573  1.000 108.46484 ? 78  LYS C CD  1 
ATOM   1905 C CE  . LYS C 1 81 ? 36.40460  33.37912 16.01210  1.000 109.26144 ? 78  LYS C CE  1 
ATOM   1906 N NZ  . LYS C 1 81 ? 36.45963  34.17427 17.27122  1.000 105.66365 ? 78  LYS C NZ  1 
HETATM 1907 O O   . HOH D 2 .  ? 9.20509   44.12559 14.57521  1.000 46.66176  ? 101 HOH A O   1 
HETATM 1908 O O   . HOH D 2 .  ? 18.88848  40.89871 10.51089  1.000 41.43201  ? 102 HOH A O   1 
HETATM 1909 O O   . HOH D 2 .  ? 7.13788   18.86677 29.31493  1.000 37.05152  ? 103 HOH A O   1 
HETATM 1910 O O   . HOH D 2 .  ? 23.23599  23.54899 22.60773  1.000 58.92384  ? 104 HOH A O   1 
HETATM 1911 O O   . HOH D 2 .  ? 16.90779  42.82661 11.62358  1.000 41.47434  ? 105 HOH A O   1 
HETATM 1912 O O   . HOH D 2 .  ? -2.84976  24.41546 30.63464  1.000 66.72491  ? 106 HOH A O   1 
HETATM 1913 O O   . HOH D 2 .  ? 21.57950  39.26777 18.91204  1.000 51.86884  ? 107 HOH A O   1 
HETATM 1914 O O   . HOH E 2 .  ? 13.80394  13.63352 26.51624  1.000 47.89213  ? 101 HOH B O   1 
HETATM 1915 O O   . HOH E 2 .  ? -3.57438  25.67642 16.92208  1.000 55.14433  ? 102 HOH B O   1 
HETATM 1916 O O   . HOH E 2 .  ? -5.14249  19.80860 2.49037   1.000 39.81023  ? 103 HOH B O   1 
HETATM 1917 O O   . HOH E 2 .  ? 9.15489   7.67441  24.47780  1.000 41.41120  ? 104 HOH B O   1 
HETATM 1918 O O   . HOH F 2 .  ? 9.38033   17.21977 -5.42989  1.000 46.29077  ? 101 HOH C O   1 
HETATM 1919 O O   . HOH F 2 .  ? 19.21844  22.74417 -14.48279 1.000 45.78347  ? 102 HOH C O   1 
HETATM 1920 O O   . HOH F 2 .  ? 20.09677  26.54064 -8.77959  1.000 42.85865  ? 103 HOH C O   1 
HETATM 1921 O O   . HOH F 2 .  ? 21.16034  21.99960 -13.52028 1.000 52.33004  ? 104 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 
13   N N   . SER A 4  ? 0.74019 1.10071 0.97490 0.07298  -0.27625 0.04917  1  SER A N   
14   C CA  . SER A 4  ? 0.63056 0.98878 0.86482 0.03525  -0.26938 0.02212  1  SER A CA  
15   C C   . SER A 4  ? 0.67031 0.99867 0.92644 0.03431  -0.23471 0.01259  1  SER A C   
16   O O   . SER A 4  ? 0.60358 0.93859 0.90190 0.05751  -0.21461 0.02151  1  SER A O   
17   C CB  . SER A 4  ? 0.61104 1.03917 0.89936 0.01787  -0.28050 0.01351  1  SER A CB  
18   O OG  . SER A 4  ? 0.45020 0.89939 0.80063 0.01452  -0.25155 0.00903  1  SER A OG  
19   N N   . ILE A 5  ? 0.64914 0.94322 0.87371 0.00821  -0.22658 -0.00734 2  ILE A N   
20   C CA  . ILE A 5  ? 0.45327 0.72326 0.69138 0.00436  -0.19511 -0.01730 2  ILE A CA  
21   C C   . ILE A 5  ? 0.53628 0.82439 0.80263 -0.02472 -0.18358 -0.03151 2  ILE A C   
22   O O   . ILE A 5  ? 0.49405 0.75903 0.75994 -0.03239 -0.15845 -0.03911 2  ILE A O   
23   C CB  . ILE A 5  ? 0.50678 0.71058 0.67376 0.00380  -0.17708 -0.01990 2  ILE A CB  
24   C CG1 . ILE A 5  ? 0.57834 0.75681 0.69343 -0.01869 -0.18942 -0.03377 2  ILE A CG1 
25   C CG2 . ILE A 5  ? 0.57427 0.75314 0.71179 0.02985  -0.17740 -0.00192 2  ILE A CG2 
26   C CD1 . ILE A 5  ? 0.62798 0.74789 0.68031 -0.01567 -0.16774 -0.03415 2  ILE A CD1 
27   N N   . LYS A 6  ? 0.44496 0.77350 0.73209 -0.04206 -0.19983 -0.03295 3  LYS A N   
28   C CA  . LYS A 6  ? 0.52477 0.86448 0.83552 -0.07289 -0.18829 -0.04431 3  LYS A CA  
29   C C   . LYS A 6  ? 0.47709 0.83956 0.84076 -0.06569 -0.15715 -0.03740 3  LYS A C   
30   O O   . LYS A 6  ? 0.41028 0.75623 0.77787 -0.08408 -0.13592 -0.04355 3  LYS A O   
31   C CB  . LYS A 6  ? 0.52736 0.91389 0.85442 -0.09430 -0.21383 -0.04914 3  LYS A CB  
32   C CG  . LYS A 6  ? 0.70309 1.08307 1.03651 -0.13400 -0.20623 -0.06505 3  LYS A CG  
33   C CD  . LYS A 6  ? 0.72135 1.02556 0.98837 -0.15063 -0.20376 -0.08304 3  LYS A CD  
34   C CE  . LYS A 6  ? 0.66088 0.93027 0.93853 -0.17054 -0.17510 -0.08608 3  LYS A CE  
35   N NZ  . LYS A 6  ? 0.66409 0.85586 0.88228 -0.17944 -0.16857 -0.10279 3  LYS A NZ  
36   N N   . GLU A 7  ? 0.44044 0.83689 0.84164 -0.03737 -0.15196 -0.02433 4  GLU A N   
37   C CA  . GLU A 7  ? 0.32195 0.73458 0.76471 -0.02766 -0.11860 -0.02099 4  GLU A CA  
38   C C   . GLU A 7  ? 0.42638 0.78840 0.83748 -0.02434 -0.09425 -0.02842 4  GLU A C   
39   O O   . GLU A 7  ? 0.38389 0.74306 0.80351 -0.03615 -0.06820 -0.03177 4  GLU A O   
40   C CB  . GLU A 7  ? 0.42315 0.87328 0.90764 0.00657  -0.11588 -0.00823 4  GLU A CB  
41   C CG  . GLU A 7  ? 0.47723 0.92388 0.98676 0.02527  -0.07688 -0.00887 4  GLU A CG  
42   C CD  . GLU A 7  ? 0.62537 1.09449 1.16995 0.06416  -0.07091 0.00208  4  GLU A CD  
43   O OE1 . GLU A 7  ? 0.56048 1.08822 1.15370 0.07124  -0.07602 0.00990  4  GLU A OE1 
44   O OE2 . GLU A 7  ? 0.58287 1.00933 1.10701 0.08821  -0.06117 0.00179  4  GLU A OE2 
45   N N   . ILE A 8  ? 0.29044 0.61575 0.66424 -0.00920 -0.10282 -0.02971 5  ILE A N   
46   C CA  . ILE A 8  ? 0.35600 0.63160 0.68369 -0.00967 -0.08081 -0.03402 5  ILE A CA  
47   C C   . ILE A 8  ? 0.34318 0.59557 0.64405 -0.03571 -0.07765 -0.04009 5  ILE A C   
48   O O   . ILE A 8  ? 0.26291 0.49743 0.54982 -0.04195 -0.05494 -0.03994 5  ILE A O   
49   C CB  . ILE A 8  ? 0.28354 0.51937 0.56576 0.00793  -0.08808 -0.02886 5  ILE A CB  
50   C CG1 . ILE A 8  ? 0.49417 0.74606 0.80435 0.03598  -0.09220 -0.01959 5  ILE A CG1 
51   C CG2 . ILE A 8  ? 0.55470 0.74938 0.79821 0.00605  -0.06634 -0.03126 5  ILE A CG2 
52   C CD1 . ILE A 8  ? 0.67681 0.88528 0.94395 0.05192  -0.09771 -0.01091 5  ILE A CD1 
53   N N   . THR A 9  ? 0.37709 0.62586 0.66651 -0.05049 -0.10021 -0.04509 6  THR A N   
54   C CA  . THR A 9  ? 0.29354 0.50781 0.55445 -0.07233 -0.09381 -0.05197 6  THR A CA  
55   C C   . THR A 9  ? 0.41213 0.64535 0.71229 -0.09290 -0.07730 -0.05282 6  THR A C   
56   O O   . THR A 9  ? 0.30345 0.50736 0.58537 -0.09871 -0.05498 -0.04893 6  THR A O   
57   C CB  . THR A 9  ? 0.47547 0.67393 0.70748 -0.08507 -0.11996 -0.06214 6  THR A CB  
58   O OG1 . THR A 9  ? 0.50124 0.67707 0.68865 -0.06541 -0.12968 -0.05788 6  THR A OG1 
59   C CG2 . THR A 9  ? 0.36550 0.51692 0.56709 -0.10578 -0.10773 -0.07165 6  THR A CG2 
60   N N   . GLU A 10 ? 0.24371 0.52132 0.58665 -0.10186 -0.08508 -0.05088 7  GLU A N   
61   C CA  . GLU A 10 ? 0.35643 0.64940 0.73050 -0.12229 -0.06588 -0.04679 7  GLU A CA  
62   C C   . GLU A 10 ? 0.32628 0.62204 0.70995 -0.11090 -0.03254 -0.03887 7  GLU A C   
63   O O   . GLU A 10 ? 0.33667 0.61938 0.72123 -0.12672 -0.01027 -0.03413 7  GLU A O   
64   C CB  . GLU A 10 ? 0.22642 0.57639 0.64667 -0.13047 -0.07902 -0.04212 7  GLU A CB  
65   C CG  . GLU A 10 ? 0.52336 0.87188 0.93487 -0.15997 -0.10673 -0.05110 7  GLU A CG  
66   C CD  . GLU A 10 ? 0.69395 1.02450 1.11497 -0.19461 -0.09362 -0.05276 7  GLU A CD  
67   O OE1 . GLU A 10 ? 0.70373 0.99365 1.11036 -0.19510 -0.06630 -0.05047 7  GLU A OE1 
68   O OE2 . GLU A 10 ? 0.54517 0.90339 0.98832 -0.22251 -0.11076 -0.05499 7  GLU A OE2 
69   N N   . THR A 11 ? 0.32738 0.63617 0.71421 -0.08456 -0.02752 -0.03746 8  THR A N   
70   C CA  . THR A 11 ? 0.19696 0.50266 0.57905 -0.07569 0.00402  -0.03451 8  THR A CA  
71   C C   . THR A 11 ? 0.23678 0.49036 0.55764 -0.07964 0.01117  -0.03038 8  THR A C   
72   O O   . THR A 11 ? 0.22659 0.47139 0.53430 -0.08702 0.03436  -0.02248 8  THR A O   
73   C CB  . THR A 11 ? 0.26132 0.57474 0.64384 -0.04682 0.00746  -0.03650 8  THR A CB  
74   O OG1 . THR A 11 ? 0.24778 0.60988 0.68741 -0.03684 0.00138  -0.03364 8  THR A OG1 
75   C CG2 . THR A 11 ? 0.20657 0.50572 0.56319 -0.04010 0.04042  -0.03661 8  THR A CG2 
76   N N   . THR A 12 ? 0.24874 0.47066 0.53324 -0.07350 -0.00769 -0.03257 9  THR A N   
77   C CA  . THR A 12 ? 0.22759 0.40970 0.46648 -0.07409 -0.00183 -0.02526 9  THR A CA  
78   C C   . THR A 12 ? 0.25539 0.41847 0.49494 -0.09269 0.00741  -0.01928 9  THR A C   
79   O O   . THR A 12 ? 0.31009 0.45484 0.52813 -0.09324 0.02316  -0.00579 9  THR A O   
80   C CB  . THR A 12 ? 0.23288 0.39046 0.44252 -0.06355 -0.01919 -0.02771 9  THR A CB  
81   O OG1 . THR A 12 ? 0.26817 0.43675 0.47883 -0.04802 -0.02637 -0.03140 9  THR A OG1 
82   C CG2 . THR A 12 ? 0.23328 0.36296 0.40920 -0.05997 -0.01148 -0.01672 9  THR A CG2 
83   N N   . GLN A 13 ? 0.26554 0.42998 0.52739 -0.10911 -0.00336 -0.02837 10 GLN A N   
84   C CA  . GLN A 13 ? 0.32245 0.45929 0.58637 -0.13085 0.00825  -0.02515 10 GLN A CA  
85   C C   . GLN A 13 ? 0.36305 0.51641 0.64844 -0.14049 0.03465  -0.01146 10 GLN A C   
86   O O   . GLN A 13 ? 0.35549 0.47484 0.61980 -0.14469 0.05317  0.00373  10 GLN A O   
87   C CB  . GLN A 13 ? 0.37664 0.51662 0.66267 -0.15389 -0.01078 -0.04217 10 GLN A CB  
88   C CG  . GLN A 13 ? 0.38851 0.49913 0.63571 -0.14677 -0.03298 -0.05540 10 GLN A CG  
89   C CD  . GLN A 13 ? 0.52075 0.63869 0.78050 -0.17224 -0.05807 -0.07473 10 GLN A CD  
90   O OE1 . GLN A 13 ? 0.84149 0.90837 1.06425 -0.18562 -0.06211 -0.08830 10 GLN A OE1 
91   N NE2 . GLN A 13 ? 0.54465 0.72242 0.84634 -0.17571 -0.07421 -0.07276 10 GLN A NE2 
92   N N   . LEU A 14 ? 0.35487 0.55949 0.68102 -0.14113 0.03961  -0.01387 11 LEU A N   
93   C CA  . LEU A 14 ? 0.33328 0.55533 0.67672 -0.14954 0.07067  -0.00081 11 LEU A CA  
94   C C   . LEU A 14 ? 0.38825 0.58994 0.67883 -0.13205 0.08712  0.01284  11 LEU A C   
95   O O   . LEU A 14 ? 0.34508 0.53314 0.61969 -0.13996 0.11142  0.03027  11 LEU A O   
96   C CB  . LEU A 14 ? 0.34218 0.62094 0.73149 -0.14507 0.07298  -0.00460 11 LEU A CB  
97   C CG  . LEU A 14 ? 0.29093 0.59590 0.72208 -0.16687 0.06690  -0.00294 11 LEU A CG  
98   C CD1 . LEU A 14 ? 0.50792 0.79535 0.93668 -0.18212 0.03319  -0.01481 11 LEU A CD1 
99   C CD2 . LEU A 14 ? 0.46845 0.83535 0.94568 -0.15410 0.07014  -0.00252 11 LEU A CD2 
100  N N   . ILE A 15 ? 0.27156 0.47041 0.53223 -0.11065 0.07291  0.00639  12 ILE A N   
101  C CA  . ILE A 15 ? 0.33280 0.51651 0.54196 -0.09915 0.08141  0.01665  12 ILE A CA  
102  C C   . ILE A 15 ? 0.46653 0.61397 0.64409 -0.10161 0.08091  0.03634  12 ILE A C   
103  O O   . ILE A 15 ? 0.37796 0.51689 0.52504 -0.10245 0.09623  0.05549  12 ILE A O   
104  C CB  . ILE A 15 ? 0.37249 0.55744 0.56170 -0.08178 0.06399  0.00400  12 ILE A CB  
105  C CG1 . ILE A 15 ? 0.29593 0.50852 0.50801 -0.07341 0.07384  -0.01058 12 ILE A CG1 
106  C CG2 . ILE A 15 ? 0.28572 0.45346 0.42146 -0.07665 0.06202  0.01422  12 ILE A CG2 
107  C CD1 . ILE A 15 ? 0.28797 0.49240 0.48549 -0.05763 0.05868  -0.02336 12 ILE A CD1 
108  N N   . VAL A 16 ? 0.33383 0.45772 0.51583 -0.10055 0.06502  0.03359  13 VAL A N   
109  C CA  . VAL A 16 ? 0.34084 0.42849 0.49780 -0.09545 0.06725  0.05347  13 VAL A CA  
110  C C   . VAL A 16 ? 0.38129 0.44072 0.54826 -0.11144 0.08766  0.06710  13 VAL A C   
111  O O   . VAL A 16 ? 0.44975 0.48027 0.59381 -0.10478 0.09802  0.09256  13 VAL A O   
112  C CB  . VAL A 16 ? 0.33077 0.39924 0.48426 -0.08452 0.04974  0.04478  13 VAL A CB  
113  C CG1 . VAL A 16 ? 0.31774 0.36207 0.48984 -0.09852 0.04792  0.02875  13 VAL A CG1 
114  C CG2 . VAL A 16 ? 0.49775 0.54584 0.62839 -0.06818 0.05130  0.06824  13 VAL A CG2 
115  N N   . LYS A 17 ? 0.33273 0.40149 0.53680 -0.13311 0.09361  0.05340  14 LYS A N   
116  C CA  . LYS A 17 ? 0.44518 0.48813 0.66252 -0.15470 0.11679  0.06685  14 LYS A CA  
117  C C   . LYS A 17 ? 0.44289 0.49464 0.64065 -0.15333 0.14206  0.09321  14 LYS A C   
118  O O   . LYS A 17 ? 0.44054 0.45483 0.62594 -0.16061 0.16273  0.11788  14 LYS A O   
119  C CB  . LYS A 17 ? 0.47506 0.54167 0.74567 -0.18322 0.11532  0.04659  14 LYS A CB  
120  C CG  . LYS A 17 ? 0.47647 0.51620 0.75551 -0.19548 0.09389  0.02378  14 LYS A CG  
121  C CD  . LYS A 17 ? 0.56155 0.64093 0.88484 -0.21973 0.07976  0.00645  14 LYS A CD  
122  C CE  . LYS A 17 ? 0.62472 0.68366 0.94248 -0.23094 0.05074  -0.01863 14 LYS A CE  
123  N NZ  . LYS A 17 ? 0.53753 0.64751 0.89279 -0.24873 0.02722  -0.02946 14 LYS A NZ  
124  N N   . HIS A 18 ? 0.45235 0.54658 0.64059 -0.14368 0.14282  0.08875  15 HIS A N   
125  C CA  . HIS A 18 ? 0.45403 0.55728 0.61407 -0.14444 0.16925  0.10921  15 HIS A CA  
126  C C   . HIS A 18 ? 0.43063 0.51432 0.52741 -0.12633 0.16351  0.13375  15 HIS A C   
127  O O   . HIS A 18 ? 0.48270 0.55486 0.54529 -0.12882 0.18484  0.16127  15 HIS A O   
128  C CB  . HIS A 18 ? 0.38461 0.53547 0.55608 -0.14140 0.17718  0.09035  15 HIS A CB  
129  C CG  . HIS A 18 ? 0.51843 0.70356 0.76025 -0.15860 0.18914  0.07635  15 HIS A CG  
130  N ND1 . HIS A 18 ? 0.58762 0.76009 0.86635 -0.17911 0.18356  0.07705  15 HIS A ND1 
131  C CD2 . HIS A 18 ? 0.53306 0.76518 0.80943 -0.15454 0.19857  0.06129  15 HIS A CD2 
132  C CE1 . HIS A 18 ? 0.57069 0.78681 0.89937 -0.18716 0.18139  0.06463  15 HIS A CE1 
133  N NE2 . HIS A 18 ? 0.54426 0.79831 0.87594 -0.16963 0.19092  0.05715  15 HIS A NE2 
134  N N   . LEU A 19 ? 0.40098 0.48449 0.48276 -0.10911 0.13473  0.12718  16 LEU A N   
135  C CA  . LEU A 19 ? 0.56769 0.65213 0.59803 -0.09372 0.12218  0.14761  16 LEU A CA  
136  C C   . LEU A 19 ? 0.52266 0.57780 0.54989 -0.07978 0.11237  0.17442  16 LEU A C   
137  O O   . LEU A 19 ? 0.57612 0.64119 0.57077 -0.06568 0.09729  0.19622  16 LEU A O   
138  C CB  . LEU A 19 ? 0.40321 0.51619 0.42231 -0.08607 0.09857  0.12317  16 LEU A CB  
139  C CG  . LEU A 19 ? 0.45611 0.59176 0.47530 -0.09317 0.11164  0.09716  16 LEU A CG  
140  C CD1 . LEU A 19 ? 0.40159 0.55061 0.39629 -0.08641 0.09114  0.07677  16 LEU A CD1 
141  C CD2 . LEU A 19 ? 0.43525 0.57112 0.42026 -0.10122 0.14200  0.11245  16 LEU A CD2 
142  N N   . ALA A 20 ? 0.52276 0.54244 0.58316 -0.08314 0.12060  0.17332  17 ALA A N   
143  C CA  . ALA A 20 ? 0.48294 0.46602 0.54320 -0.06548 0.11860  0.19700  17 ALA A CA  
144  C C   . ALA A 20 ? 0.65998 0.58839 0.72829 -0.07613 0.14696  0.21461  17 ALA A C   
145  O O   . ALA A 20 ? 0.61749 0.53524 0.71099 -0.10156 0.16050  0.19406  17 ALA A O   
146  C CB  . ALA A 20 ? 0.42319 0.40113 0.50784 -0.05613 0.10261  0.17296  17 ALA A CB  
147  N N   . HIS A 21 ? 0.57233 0.46715 0.62265 -0.05723 0.15547  0.25479  18 HIS A N   
148  C CA  . HIS A 21 ? 0.63853 0.46991 0.69197 -0.06477 0.18032  0.26691  18 HIS A CA  
149  C C   . HIS A 21 ? 0.64169 0.42681 0.72518 -0.07398 0.18522  0.23679  18 HIS A C   
150  O O   . HIS A 21 ? 0.67945 0.42474 0.77166 -0.09717 0.19965  0.22383  18 HIS A O   
151  C CB  . HIS A 21 ? 0.69936 0.50799 0.72643 -0.03508 0.17987  0.30697  18 HIS A CB  
152  C CG  . HIS A 21 ? 0.73309 0.54490 0.77225 -0.00115 0.16461  0.31607  18 HIS A CG  
153  N ND1 . HIS A 21 ? 0.85927 0.62142 0.92105 0.00892  0.17471  0.30174  18 HIS A ND1 
154  C CD2 . HIS A 21 ? 0.77337 0.63609 0.80654 0.02390  0.14043  0.33639  18 HIS A CD2 
155  C CE1 . HIS A 21 ? 0.76978 0.55390 0.84286 0.04160  0.16185  0.31422  18 HIS A CE1 
156  N NE2 . HIS A 21 ? 0.65673 0.50583 0.71775 0.04991  0.13875  0.33593  18 HIS A NE2 
157  N N   . ASN A 22 ? 0.62512 0.41770 0.71937 -0.05786 0.17026  0.22176  19 ASN A N   
158  C CA  . ASN A 22 ? 0.60125 0.35254 0.71053 -0.06704 0.17178  0.18659  19 ASN A CA  
159  C C   . ASN A 22 ? 0.55551 0.35903 0.67807 -0.08397 0.14792  0.14499  19 ASN A C   
160  O O   . ASN A 22 ? 0.60092 0.40290 0.72326 -0.07487 0.13508  0.12197  19 ASN A O   
161  C CB  . ASN A 22 ? 0.66539 0.38401 0.76989 -0.03153 0.17424  0.19680  19 ASN A CB  
162  C CG  . ASN A 22 ? 0.79666 0.58101 0.90099 -0.00201 0.15250  0.21551  19 ASN A CG  
163  O OD1 . ASN A 22 ? 0.68026 0.52512 0.77845 -0.00908 0.13513  0.21975  19 ASN A OD1 
164  N ND2 . ASN A 22 ? 0.72160 0.49370 0.83361 0.02974  0.15513  0.22551  19 ASN A ND2 
165  N N   . GLY A 23 ? 0.57861 0.42752 0.71215 -0.10588 0.14482  0.13789  20 GLY A N   
166  C CA  . GLY A 23 ? 0.48198 0.38244 0.63249 -0.11657 0.12340  0.10424  20 GLY A CA  
167  C C   . GLY A 23 ? 0.45372 0.33108 0.62067 -0.13671 0.11547  0.07019  20 GLY A C   
168  O O   . GLY A 23 ? 0.44961 0.35375 0.61883 -0.13288 0.09347  0.04625  20 GLY A O   
169  N N   . GLU A 24 ? 0.56995 0.39443 0.74420 -0.16046 0.13234  0.06786  21 GLU A N   
170  C CA  . GLU A 24 ? 0.54006 0.33803 0.72161 -0.18555 0.12134  0.03242  21 GLU A CA  
171  C C   . GLU A 24 ? 0.54393 0.30472 0.69172 -0.16271 0.11302  0.01814  21 GLU A C   
172  O O   . GLU A 24 ? 0.53441 0.30630 0.67657 -0.17121 0.09128  -0.01225 21 GLU A O   
173  C CB  . GLU A 24 ? 0.61132 0.35700 0.79488 -0.21248 0.13659  0.03233  21 GLU A CB  
174  C CG  . GLU A 24 ? 0.81315 0.61044 1.03329 -0.24123 0.13374  0.03340  21 GLU A CG  
175  C CD  . GLU A 24 ? 0.68412 0.54260 0.93547 -0.26021 0.10308  0.00382  21 GLU A CD  
176  O OE1 . GLU A 24 ? 0.70643 0.54669 0.94230 -0.26333 0.08195  -0.02307 21 GLU A OE1 
177  O OE2 . GLU A 24 ? 0.73999 0.66514 1.02803 -0.26879 0.10050  0.00957  21 GLU A OE2 
178  N N   . GLU A 25 ? 0.61915 0.33902 0.74478 -0.13167 0.13114  0.04249  22 GLU A N   
179  C CA  . GLU A 25 ? 0.67636 0.36626 0.77540 -0.10589 0.13034  0.03226  22 GLU A CA  
180  C C   . GLU A 25 ? 0.59527 0.35328 0.69544 -0.08813 0.10618  0.02742  22 GLU A C   
181  O O   . GLU A 25 ? 0.59720 0.34375 0.67717 -0.07989 0.09927  0.00731  22 GLU A O   
182  C CB  . GLU A 25 ? 0.74772 0.38769 0.83645 -0.07260 0.15773  0.06513  22 GLU A CB  
183  C CG  . GLU A 25 ? 0.92256 0.48000 1.00234 -0.08578 0.18391  0.06797  22 GLU A CG  
184  C CD  . GLU A 25 ? 1.23155 0.75066 1.30062 -0.04428 0.20596  0.09785  22 GLU A CD  
185  O OE1 . GLU A 25 ? 1.07813 0.63835 1.15934 -0.01052 0.20434  0.13107  22 GLU A OE1 
186  O OE2 . GLU A 25 ? 1.25336 0.70678 1.30497 -0.04600 0.22309  0.08828  22 GLU A OE2 
187  N N   . TYR A 26 ? 0.56708 0.38980 0.68519 -0.08351 0.09563  0.04469  23 TYR A N   
188  C CA  . TYR A 26 ? 0.45183 0.33128 0.57132 -0.07201 0.07384  0.03744  23 TYR A CA  
189  C C   . TYR A 26 ? 0.47160 0.37534 0.59868 -0.09356 0.05357  0.00665  23 TYR A C   
190  O O   . TYR A 26 ? 0.38541 0.30531 0.50198 -0.08478 0.03814  -0.00643 23 TYR A O   
191  C CB  . TYR A 26 ? 0.41850 0.34975 0.54679 -0.06357 0.06961  0.06047  23 TYR A CB  
192  C CG  . TYR A 26 ? 0.42550 0.35585 0.54673 -0.03765 0.07678  0.09314  23 TYR A CG  
193  C CD1 . TYR A 26 ? 0.44603 0.38388 0.56641 -0.01525 0.07194  0.09715  23 TYR A CD1 
194  C CD2 . TYR A 26 ? 0.49889 0.42716 0.61677 -0.03551 0.08778  0.12326  23 TYR A CD2 
195  C CE1 . TYR A 26 ? 0.56248 0.51288 0.68860 0.00864  0.07524  0.13022  23 TYR A CE1 
196  C CE2 . TYR A 26 ? 0.60094 0.53719 0.71494 -0.01049 0.08857  0.15739  23 TYR A CE2 
197  C CZ  . TYR A 26 ? 0.52458 0.47601 0.64759 0.01152  0.08076  0.16070  23 TYR A CZ  
198  O OH  . TYR A 26 ? 0.65599 0.62789 0.78686 0.03656  0.07854  0.19770  23 TYR A OH  
199  N N   . SER A 27 ? 0.45629 0.36677 0.60529 -0.12143 0.05352  -0.00161 24 SER A N   
200  C CA  . SER A 27 ? 0.41068 0.35561 0.57825 -0.14125 0.03111  -0.02635 24 SER A CA  
201  C C   . SER A 27 ? 0.53577 0.44372 0.67440 -0.14797 0.01775  -0.05184 24 SER A C   
202  O O   . SER A 27 ? 0.49305 0.43094 0.62802 -0.14693 -0.00632 -0.06626 24 SER A O   
203  C CB  . SER A 27 ? 0.45568 0.41797 0.66233 -0.17225 0.03697  -0.02735 24 SER A CB  
204  O OG  . SER A 27 ? 0.57994 0.57892 0.81321 -0.19315 0.01247  -0.04974 24 SER A OG  
205  N N   . GLU A 28 ? 0.63067 0.46810 0.74276 -0.15387 0.03469  -0.05725 25 GLU A N   
206  C CA  . GLU A 28 ? 0.74992 0.54048 0.81870 -0.15895 0.02696  -0.08439 25 GLU A CA  
207  C C   . GLU A 28 ? 0.62697 0.42513 0.66613 -0.12589 0.02451  -0.08070 25 GLU A C   
208  O O   . GLU A 28 ? 0.64882 0.44468 0.65640 -0.12870 0.00689  -0.10085 25 GLU A O   
209  C CB  . GLU A 28 ? 0.91591 0.61672 0.95758 -0.16700 0.05418  -0.09076 25 GLU A CB  
210  C CG  . GLU A 28 ? 1.16687 0.80469 1.14949 -0.17084 0.05325  -0.12236 25 GLU A CG  
211  C CD  . GLU A 28 ? 1.21189 0.86875 1.18477 -0.20889 0.01725  -0.15537 25 GLU A CD  
212  O OE1 . GLU A 28 ? 1.03986 0.72776 1.05411 -0.23742 0.00259  -0.15550 25 GLU A OE1 
213  O OE2 . GLU A 28 ? 1.17894 0.83185 1.10548 -0.20342 0.00084  -0.17390 25 GLU A OE2 
214  N N   . VAL A 29 ? 0.60483 0.41446 0.65348 -0.09627 0.04122  -0.05328 26 VAL A N   
215  C CA  . VAL A 29 ? 0.52916 0.35519 0.56173 -0.06883 0.04022  -0.04663 26 VAL A CA  
216  C C   . VAL A 29 ? 0.51593 0.39992 0.55831 -0.07236 0.01236  -0.05211 26 VAL A C   
217  O O   . VAL A 29 ? 0.49159 0.37430 0.50604 -0.06440 0.00375  -0.06082 26 VAL A O   
218  C CB  . VAL A 29 ? 0.49611 0.33569 0.54817 -0.04190 0.05816  -0.01428 26 VAL A CB  
219  C CG1 . VAL A 29 ? 0.46027 0.33350 0.51040 -0.02118 0.05343  -0.00610 26 VAL A CG1 
220  C CG2 . VAL A 29 ? 0.55255 0.32968 0.59343 -0.02842 0.08822  -0.00525 26 VAL A CG2 
221  N N   . VAL A 30 ? 0.47085 0.40213 0.55073 -0.08238 0.00149  -0.04564 27 VAL A N   
222  C CA  . VAL A 30 ? 0.47570 0.45705 0.56980 -0.08191 -0.02109 -0.04958 27 VAL A CA  
223  C C   . VAL A 30 ? 0.59438 0.57192 0.67084 -0.09575 -0.04387 -0.07123 27 VAL A C   
224  O O   . VAL A 30 ? 0.44620 0.44088 0.50868 -0.08539 -0.05996 -0.07263 27 VAL A O   
225  C CB  . VAL A 30 ? 0.41381 0.43987 0.55088 -0.08985 -0.02179 -0.04168 27 VAL A CB  
226  C CG1 . VAL A 30 ? 0.41787 0.48944 0.57241 -0.08350 -0.04007 -0.04485 27 VAL A CG1 
227  C CG2 . VAL A 30 ? 0.34394 0.37190 0.48438 -0.07820 -0.00317 -0.02053 27 VAL A CG2 
228  N N   . LYS A 31 ? 0.40469 0.35791 0.47887 -0.12125 -0.04694 -0.08736 28 LYS A N   
229  C CA  . LYS A 31 ? 0.50076 0.45234 0.55360 -0.14040 -0.07452 -0.10994 28 LYS A CA  
230  C C   . LYS A 31 ? 0.69178 0.60038 0.67747 -0.12631 -0.07415 -0.11884 28 LYS A C   
231  O O   . LYS A 31 ? 0.57332 0.50364 0.53854 -0.12039 -0.09737 -0.12094 28 LYS A O   
232  C CB  . LYS A 31 ? 0.70843 0.63187 0.76771 -0.17640 -0.07508 -0.12805 28 LYS A CB  
233  C CG  . LYS A 31 ? 0.69003 0.65998 0.77690 -0.20685 -0.11179 -0.14332 28 LYS A CG  
234  C CD  . LYS A 31 ? 0.84047 0.77146 0.92711 -0.24050 -0.11196 -0.15975 28 LYS A CD  
235  C CE  . LYS A 31 ? 0.88171 0.79750 1.00661 -0.24917 -0.07932 -0.14480 28 LYS A CE  
236  N NZ  . LYS A 31 ? 0.86648 0.85925 1.06247 -0.25054 -0.08233 -0.12310 28 LYS A NZ  
237  N N   . GLU A 32 ? 0.74255 0.58873 0.69303 -0.11813 -0.04462 -0.12141 29 GLU A N   
238  C CA  . GLU A 32 ? 0.71185 0.51371 0.59733 -0.10282 -0.03477 -0.12971 29 GLU A CA  
239  C C   . GLU A 32 ? 0.73291 0.56925 0.62114 -0.07443 -0.03296 -0.10825 29 GLU A C   
240  O O   . GLU A 32 ? 0.77881 0.60220 0.61779 -0.06667 -0.03786 -0.11306 29 GLU A O   
241  C CB  . GLU A 32 ? 0.76560 0.49690 0.62605 -0.09331 0.00424  -0.13264 29 GLU A CB  
242  C CG  . GLU A 32 ? 0.98871 0.66683 0.77912 -0.07700 0.02352  -0.14420 29 GLU A CG  
243  C CD  . GLU A 32 ? 1.01067 0.62145 0.78703 -0.05952 0.06845  -0.14321 29 GLU A CD  
244  O OE1 . GLU A 32 ? 0.95903 0.56294 0.77850 -0.06029 0.08140  -0.13099 29 GLU A OE1 
245  O OE2 . GLU A 32 ? 1.07444 0.63786 0.79588 -0.04255 0.09353  -0.15242 29 GLU A OE2 
246  N N   . ILE A 33 ? 0.56251 0.43876 0.50251 -0.06129 -0.02538 -0.08488 30 ILE A N   
247  C CA  . ILE A 33 ? 0.60534 0.51070 0.55133 -0.04054 -0.02392 -0.06643 30 ILE A CA  
248  C C   . ILE A 33 ? 0.59001 0.53224 0.53959 -0.04408 -0.05421 -0.06731 30 ILE A C   
249  O O   . ILE A 33 ? 0.56389 0.50544 0.48666 -0.03180 -0.05716 -0.06040 30 ILE A O   
250  C CB  . ILE A 33 ? 0.61656 0.55007 0.61008 -0.03032 -0.01008 -0.04474 30 ILE A CB  
251  C CG1 . ILE A 33 ? 0.56988 0.48029 0.55691 -0.01177 0.01921  -0.03157 30 ILE A CG1 
252  C CG2 . ILE A 33 ? 0.59313 0.57060 0.61007 -0.02483 -0.02326 -0.03337 30 ILE A CG2 
253  C CD1 . ILE A 33 ? 0.65967 0.51423 0.62185 -0.01140 0.04006  -0.04208 30 ILE A CD1 
254  N N   . SER A 34 ? 0.50045 0.47573 0.48626 -0.05919 -0.07466 -0.07278 31 SER A N   
255  C CA  . SER A 34 ? 0.56080 0.57654 0.56125 -0.05718 -0.10243 -0.06970 31 SER A CA  
256  C C   . SER A 34 ? 0.68935 0.68973 0.63671 -0.06139 -0.12543 -0.07994 31 SER A C   
257  O O   . SER A 34 ? 0.60308 0.61612 0.53532 -0.04696 -0.13902 -0.06840 31 SER A O   
258  C CB  . SER A 34 ? 0.60450 0.66445 0.66326 -0.07148 -0.11495 -0.07245 31 SER A CB  
259  O OG  . SER A 34 ? 0.74222 0.84598 0.82474 -0.06460 -0.14017 -0.06675 31 SER A OG  
260  N N   . GLU A 35 ? 0.66160 0.62933 0.57400 -0.08194 -0.12992 -0.10143 32 GLU A N   
261  C CA  . GLU A 35 ? 0.74605 0.69580 0.59410 -0.08987 -0.15466 -0.11455 32 GLU A CA  
262  C C   . GLU A 35 ? 0.73183 0.64153 0.51403 -0.06807 -0.13525 -0.10649 32 GLU A C   
263  O O   . GLU A 35 ? 0.71396 0.62156 0.44464 -0.06445 -0.15618 -0.10452 32 GLU A O   
264  C CB  . GLU A 35 ? 0.84797 0.76010 0.66521 -0.12150 -0.16067 -0.14479 32 GLU A CB  
265  C CG  . GLU A 35 ? 0.87636 0.71617 0.65625 -0.11882 -0.11884 -0.15599 32 GLU A CG  
266  C CD  . GLU A 35 ? 1.07226 0.86581 0.82918 -0.15254 -0.12104 -0.18703 32 GLU A CD  
267  O OE1 . GLU A 35 ? 1.03800 0.86836 0.83311 -0.18204 -0.15202 -0.19639 32 GLU A OE1 
268  O OE2 . GLU A 35 ? 1.06502 0.78416 0.76882 -0.14987 -0.08949 -0.20197 32 GLU A OE2 
269  N N   . GLU A 36 ? 0.73068 0.61303 0.51605 -0.05309 -0.09544 -0.09852 33 GLU A N   
270  C CA  . GLU A 36 ? 0.79402 0.64799 0.53142 -0.03262 -0.07165 -0.08696 33 GLU A CA  
271  C C   . GLU A 36 ? 0.82461 0.71511 0.58723 -0.01635 -0.07912 -0.06048 33 GLU A C   
272  O O   . GLU A 36 ? 0.75754 0.63254 0.47098 -0.00546 -0.07705 -0.04987 33 GLU A O   
273  C CB  . GLU A 36 ? 0.72594 0.55095 0.47370 -0.02105 -0.02776 -0.08342 33 GLU A CB  
274  C CG  . GLU A 36 ? 0.95812 0.76538 0.67479 0.00013  0.00305  -0.06764 33 GLU A CG  
275  C CD  . GLU A 36 ? 0.97460 0.75471 0.70089 0.01353  0.04658  -0.06529 33 GLU A CD  
276  O OE1 . GLU A 36 ? 1.08412 0.83524 0.81117 0.00687  0.05428  -0.08165 33 GLU A OE1 
277  O OE2 . GLU A 36 ? 0.96438 0.75283 0.70185 0.03103  0.07414  -0.04506 33 GLU A OE2 
278  N N   . MET A 37 ? 0.61125 0.54363 0.44488 -0.01494 -0.08490 -0.04974 34 MET A N   
279  C CA  . MET A 37 ? 0.67072 0.62729 0.52716 -0.00103 -0.09032 -0.02831 34 MET A CA  
280  C C   . MET A 37 ? 0.70450 0.67479 0.53881 0.00220  -0.12416 -0.02362 34 MET A C   
281  O O   . MET A 37 ? 0.73937 0.70104 0.54958 0.01682  -0.12431 -0.00463 34 MET A O   
282  C CB  . MET A 37 ? 0.46209 0.45322 0.38918 -0.00166 -0.08816 -0.02358 34 MET A CB  
283  C CG  . MET A 37 ? 0.56243 0.54865 0.51311 -0.00451 -0.06173 -0.02372 34 MET A CG  
284  S SD  . MET A 37 ? 0.44393 0.46601 0.45627 -0.00520 -0.06051 -0.01678 34 MET A SD  
285  C CE  . MET A 37 ? 0.64575 0.66151 0.65059 0.00650  -0.05714 -0.00056 34 MET A CE  
286  N N   . GLU A 38 ? 0.69709 0.69138 0.54316 -0.01179 -0.15381 -0.03780 35 GLU A N   
287  C CA  . GLU A 38 ? 0.76014 0.77779 0.58914 -0.00854 -0.19218 -0.03083 35 GLU A CA  
288  C C   . GLU A 38 ? 0.83445 0.81192 0.56807 -0.01004 -0.19916 -0.03424 35 GLU A C   
289  O O   . GLU A 38 ? 0.93340 0.91901 0.63391 0.00126  -0.22414 -0.01739 35 GLU A O   
290  C CB  . GLU A 38 ? 0.72681 0.79157 0.60424 -0.02736 -0.22330 -0.04463 35 GLU A CB  
291  C CG  . GLU A 38 ? 1.03007 1.14453 0.92636 -0.01834 -0.26535 -0.02927 35 GLU A CG  
292  C CD  . GLU A 38 ? 0.98595 1.16610 0.97003 -0.02941 -0.27855 -0.03330 35 GLU A CD  
293  O OE1 . GLU A 38 ? 0.93105 1.11137 0.93658 -0.05511 -0.26926 -0.05450 35 GLU A OE1 
294  O OE2 . GLU A 38 ? 0.99293 1.22231 1.02481 -0.01074 -0.28913 -0.01296 35 GLU A OE2 
295  N N   . LYS A 39 ? 0.91816 0.84894 0.60296 -0.02147 -0.17511 -0.05436 36 LYS A N   
296  C CA  . LYS A 39 ? 1.00527 0.88754 0.58875 -0.02047 -0.17024 -0.05931 36 LYS A CA  
297  C C   . LYS A 39 ? 0.95223 0.81456 0.51132 0.00372  -0.14134 -0.03114 36 LYS A C   
298  O O   . LYS A 39 ? 1.05254 0.89970 0.54450 0.01242  -0.15234 -0.01695 36 LYS A O   
299  C CB  . LYS A 39 ? 1.04587 0.87647 0.58806 -0.03524 -0.14322 -0.08943 36 LYS A CB  
300  C CG  . LYS A 39 ? 1.18591 0.95578 0.61987 -0.02970 -0.12133 -0.09609 36 LYS A CG  
301  C CD  . LYS A 39 ? 1.21438 0.92678 0.61900 -0.03642 -0.08228 -0.12373 36 LYS A CD  
302  C CE  . LYS A 39 ? 1.26390 0.91192 0.55579 -0.02854 -0.05354 -0.13268 36 LYS A CE  
303  N NZ  . LYS A 39 ? 1.32112 0.97488 0.60811 -0.00185 -0.02379 -0.09812 36 LYS A NZ  
304  N N   . LYS A 40 ? 0.98070 0.84418 0.59338 0.01267  -0.10536 -0.02098 37 LYS A N   
305  C CA  . LYS A 40 ? 0.84446 0.69248 0.44715 0.02934  -0.07541 0.00523  37 LYS A CA  
306  C C   . LYS A 40 ? 0.84788 0.71866 0.47865 0.04147  -0.09425 0.03238  37 LYS A C   
307  O O   . LYS A 40 ? 0.96633 0.82204 0.59632 0.05152  -0.06986 0.05535  37 LYS A O   
308  C CB  . LYS A 40 ? 0.96068 0.81103 0.61857 0.03068  -0.03647 0.00684  37 LYS A CB  
309  C CG  . LYS A 40 ? 1.03892 0.85199 0.65510 0.03307  0.00275  -0.00264 37 LYS A CG  
310  C CD  . LYS A 40 ? 0.99093 0.77832 0.56891 0.02144  -0.00539 -0.03461 37 LYS A CD  
311  C CE  . LYS A 40 ? 1.10884 0.84942 0.64278 0.02915  0.04034  -0.04468 37 LYS A CE  
312  N NZ  . LYS A 40 ? 1.06249 0.82197 0.67079 0.03983  0.07502  -0.03139 37 LYS A NZ  
313  N N   . GLY A 41 ? 0.81180 0.71729 0.47149 0.04103  -0.13409 0.03143  38 GLY A N   
314  C CA  . GLY A 41 ? 0.77532 0.69677 0.46010 0.05838  -0.15012 0.05851  38 GLY A CA  
315  C C   . GLY A 41 ? 0.81013 0.73705 0.56418 0.06426  -0.12706 0.06830  38 GLY A C   
316  O O   . GLY A 41 ? 0.76220 0.67486 0.51885 0.07908  -0.12242 0.09303  38 GLY A O   
317  N N   . LEU A 42 ? 0.60073 0.54318 0.40579 0.05199  -0.11273 0.04975  39 LEU A N   
318  C CA  . LEU A 42 ? 0.64838 0.59616 0.51051 0.05323  -0.09471 0.05481  39 LEU A CA  
319  C C   . LEU A 42 ? 0.55685 0.53195 0.46804 0.06343  -0.11484 0.05713  39 LEU A C   
320  O O   . LEU A 42 ? 0.62816 0.63622 0.55544 0.06344  -0.14075 0.04881  39 LEU A O   
321  C CB  . LEU A 42 ? 0.62751 0.58537 0.52080 0.03815  -0.07554 0.03761  39 LEU A CB  
322  C CG  . LEU A 42 ? 0.73134 0.66652 0.59020 0.03338  -0.04939 0.03755  39 LEU A CG  
323  C CD1 . LEU A 42 ? 0.66702 0.61748 0.56723 0.02392  -0.03225 0.02808  39 LEU A CD1 
324  C CD2 . LEU A 42 ? 0.74287 0.65281 0.57861 0.03927  -0.02882 0.06010  39 LEU A CD2 
325  N N   . SER A 43 ? 0.59529 0.55562 0.53232 0.07137  -0.10064 0.06811  40 SER A N   
326  C CA  . SER A 43 ? 0.62961 0.60602 0.61058 0.08707  -0.11116 0.07172  40 SER A CA  
327  C C   . SER A 43 ? 0.51932 0.53143 0.55139 0.07700  -0.10943 0.04933  40 SER A C   
328  O O   . SER A 43 ? 0.41946 0.43717 0.45274 0.05793  -0.09879 0.03404  40 SER A O   
329  C CB  . SER A 43 ? 0.62965 0.56441 0.61512 0.09672  -0.09104 0.08617  40 SER A CB  
330  O OG  . SER A 43 ? 0.56234 0.48390 0.56101 0.07651  -0.06716 0.07244  40 SER A OG  
331  N N   . LYS A 44 ? 0.44743 0.48412 0.52297 0.09273  -0.11764 0.05068  41 LYS A N   
332  C CA  . LYS A 44 ? 0.50517 0.57311 0.62794 0.08531  -0.10948 0.03226  41 LYS A CA  
333  C C   . LYS A 44 ? 0.41056 0.45039 0.53046 0.07249  -0.08205 0.02074  41 LYS A C   
334  O O   . LYS A 44 ? 0.38801 0.44553 0.52001 0.05602  -0.07437 0.00560  41 LYS A O   
335  C CB  . LYS A 44 ? 0.38836 0.48503 0.56137 0.10961  -0.11498 0.03891  41 LYS A CB  
336  C CG  . LYS A 44 ? 0.68647 0.84618 0.89692 0.10862  -0.14118 0.03810  41 LYS A CG  
337  C CD  . LYS A 44 ? 0.48689 0.68427 0.76259 0.13552  -0.14016 0.04690  41 LYS A CD  
338  C CE  . LYS A 44 ? 0.72521 0.99806 1.05181 0.13035  -0.16824 0.04790  41 LYS A CE  
339  N NZ  . LYS A 44 ? 0.73800 1.03190 1.07630 0.09719  -0.16038 0.02530  41 LYS A NZ  
340  N N   . GLU A 45 ? 0.56807 0.56324 0.67055 0.07795  -0.06847 0.02893  42 GLU A N   
341  C CA  . GLU A 45 ? 0.50372 0.47360 0.60149 0.06053  -0.04772 0.01662  42 GLU A CA  
342  C C   . GLU A 45 ? 0.36639 0.34436 0.44669 0.03690  -0.04624 0.01340  42 GLU A C   
343  O O   . GLU A 45 ? 0.38295 0.37088 0.47021 0.02020  -0.03877 0.00094  42 GLU A O   
344  C CB  . GLU A 45 ? 0.39817 0.31332 0.48134 0.06645  -0.03451 0.02588  42 GLU A CB  
345  C CG  . GLU A 45 ? 0.56603 0.46173 0.66992 0.09261  -0.02695 0.02682  42 GLU A CG  
346  C CD  . GLU A 45 ? 0.63676 0.54859 0.75171 0.12372  -0.04460 0.05016  42 GLU A CD  
347  O OE1 . GLU A 45 ? 0.69338 0.60829 0.78140 0.12317  -0.06028 0.06744  42 GLU A OE1 
348  O OE2 . GLU A 45 ? 0.55189 0.47569 0.70190 0.14967  -0.04263 0.05214  42 GLU A OE2 
349  N N   . GLN A 46 ? 0.47070 0.44456 0.52624 0.03744  -0.05211 0.02609  43 GLN A N   
350  C CA  . GLN A 46 ? 0.43680 0.41995 0.48139 0.02140  -0.04626 0.02456  43 GLN A CA  
351  C C   . GLN A 46 ? 0.32194 0.33721 0.37963 0.01613  -0.05303 0.01192  43 GLN A C   
352  O O   . GLN A 46 ? 0.30968 0.33518 0.37313 0.00409  -0.04492 0.00842  43 GLN A O   
353  C CB  . GLN A 46 ? 0.41661 0.38185 0.42504 0.02615  -0.04452 0.03957  43 GLN A CB  
354  C CG  . GLN A 46 ? 0.40911 0.33979 0.40407 0.02550  -0.03054 0.05625  43 GLN A CG  
355  C CD  . GLN A 46 ? 0.59174 0.50470 0.54416 0.03092  -0.02392 0.07292  43 GLN A CD  
356  O OE1 . GLN A 46 ? 0.68076 0.59102 0.60137 0.04449  -0.03868 0.07713  43 GLN A OE1 
357  N NE2 . GLN A 46 ? 0.54271 0.44687 0.49361 0.01911  -0.00162 0.08274  43 GLN A NE2 
358  N N   . VAL A 47 ? 0.32915 0.36208 0.39550 0.02439  -0.06813 0.00752  44 VAL A N   
359  C CA  . VAL A 47 ? 0.35622 0.41497 0.43725 0.01503  -0.07286 -0.00409 44 VAL A CA  
360  C C   . VAL A 47 ? 0.36423 0.43762 0.47230 0.00725  -0.06138 -0.01204 44 VAL A C   
361  O O   . VAL A 47 ? 0.39354 0.47313 0.50251 -0.00406 -0.05452 -0.01496 44 VAL A O   
362  C CB  . VAL A 47 ? 0.48568 0.56740 0.57805 0.02044  -0.09420 -0.00656 44 VAL A CB  
363  C CG1 . VAL A 47 ? 0.29929 0.40656 0.41613 0.00554  -0.09579 -0.01903 44 VAL A CG1 
364  C CG2 . VAL A 47 ? 0.51863 0.58418 0.56790 0.02355  -0.10858 -0.00079 44 VAL A CG2 
365  N N   . ILE A 48 ? 0.39834 0.47299 0.52374 0.01503  -0.05711 -0.01456 45 ILE A N   
366  C CA  . ILE A 48 ? 0.38766 0.47066 0.52530 0.00743  -0.04380 -0.02411 45 ILE A CA  
367  C C   . ILE A 48 ? 0.42110 0.49185 0.53887 -0.00745 -0.03700 -0.02306 45 ILE A C   
368  O O   . ILE A 48 ? 0.43038 0.51566 0.54852 -0.01810 -0.03282 -0.02497 45 ILE A O   
369  C CB  . ILE A 48 ? 0.45875 0.53293 0.60939 0.02095  -0.03477 -0.02952 45 ILE A CB  
370  C CG1 . ILE A 48 ? 0.55661 0.66018 0.74313 0.03800  -0.04203 -0.02665 45 ILE A CG1 
371  C CG2 . ILE A 48 ? 0.47232 0.54503 0.61769 0.01104  -0.01790 -0.04244 45 ILE A CG2 
372  C CD1 . ILE A 48 ? 0.56578 0.66337 0.77383 0.05788  -0.02698 -0.03032 45 ILE A CD1 
373  N N   . LEU A 49 ? 0.33919 0.38647 0.44241 -0.00889 -0.03641 -0.01689 46 LEU A N   
374  C CA  . LEU A 49 ? 0.39031 0.43773 0.48618 -0.02511 -0.03324 -0.01312 46 LEU A CA  
375  C C   . LEU A 49 ? 0.27544 0.34413 0.37505 -0.02784 -0.03421 -0.00460 46 LEU A C   
376  O O   . LEU A 49 ? 0.29438 0.38077 0.39808 -0.03747 -0.03377 -0.00215 46 LEU A O   
377  C CB  . LEU A 49 ? 0.42487 0.44737 0.51267 -0.02796 -0.03037 -0.00455 46 LEU A CB  
378  C CG  . LEU A 49 ? 0.38329 0.37337 0.46505 -0.03204 -0.02528 -0.01325 46 LEU A CG  
379  C CD1 . LEU A 49 ? 0.38390 0.34513 0.45934 -0.03774 -0.01993 -0.00107 46 LEU A CD1 
380  C CD2 . LEU A 49 ? 0.26086 0.25784 0.33833 -0.05186 -0.02508 -0.02767 46 LEU A CD2 
381  N N   . LEU A 50 ? 0.32224 0.38580 0.41623 -0.01843 -0.03529 0.00037  47 LEU A N   
382  C CA  . LEU A 50 ? 0.34662 0.41716 0.44020 -0.01829 -0.03057 0.00652  47 LEU A CA  
383  C C   . LEU A 50 ? 0.34180 0.42409 0.44430 -0.02116 -0.03136 0.00106  47 LEU A C   
384  O O   . LEU A 50 ? 0.37072 0.45849 0.47761 -0.02242 -0.02498 0.00906  47 LEU A O   
385  C CB  . LEU A 50 ? 0.31560 0.36658 0.38768 -0.00943 -0.02870 0.00857  47 LEU A CB  
386  C CG  . LEU A 50 ? 0.54934 0.59433 0.61613 -0.00737 -0.01484 0.02203  47 LEU A CG  
387  C CD1 . LEU A 50 ? 0.44521 0.48760 0.51754 -0.01327 -0.01497 0.02798  47 LEU A CD1 
388  C CD2 . LEU A 50 ? 0.62836 0.64861 0.66146 0.00212  -0.00730 0.02233  47 LEU A CD2 
389  N N   . LEU A 51 ? 0.33994 0.42750 0.44962 -0.02118 -0.03695 -0.00930 48 LEU A N   
390  C CA  . LEU A 51 ? 0.30151 0.40144 0.42361 -0.02748 -0.03358 -0.01245 48 LEU A CA  
391  C C   . LEU A 51 ? 0.41025 0.52203 0.53256 -0.03361 -0.02670 -0.00821 48 LEU A C   
392  O O   . LEU A 51 ? 0.29512 0.41145 0.41825 -0.03812 -0.02059 -0.00080 48 LEU A O   
393  C CB  . LEU A 51 ? 0.34418 0.45722 0.48456 -0.02676 -0.03970 -0.02235 48 LEU A CB  
394  C CG  . LEU A 51 ? 0.27492 0.38199 0.41110 -0.02680 -0.05245 -0.02657 48 LEU A CG  
395  C CD1 . LEU A 51 ? 0.41535 0.55058 0.58250 -0.02866 -0.06304 -0.03319 48 LEU A CD1 
396  C CD2 . LEU A 51 ? 0.42069 0.50829 0.54322 -0.03552 -0.04650 -0.02671 48 LEU A CD2 
397  N N   . ILE A 52 ? 0.32501 0.43682 0.44068 -0.03488 -0.02771 -0.01250 49 ILE A N   
398  C CA  . ILE A 52 ? 0.32997 0.45060 0.43300 -0.04447 -0.02527 -0.01091 49 ILE A CA  
399  C C   . ILE A 52 ? 0.41887 0.54931 0.52055 -0.04835 -0.03078 0.00558  49 ILE A C   
400  O O   . ILE A 52 ? 0.32606 0.47140 0.42120 -0.05310 -0.03179 0.01630  49 ILE A O   
401  C CB  . ILE A 52 ? 0.39867 0.50711 0.48873 -0.04811 -0.02420 -0.02510 49 ILE A CB  
402  C CG1 . ILE A 52 ? 0.40297 0.50737 0.50360 -0.03772 -0.01432 -0.03757 49 ILE A CG1 
403  C CG2 . ILE A 52 ? 0.50492 0.61940 0.56930 -0.06286 -0.02555 -0.02710 49 ILE A CG2 
404  C CD1 . ILE A 52 ? 0.49497 0.57488 0.58360 -0.03498 -0.00754 -0.05219 49 ILE A CD1 
405  N N   . HIS A 53 ? 0.32521 0.45054 0.43494 -0.04452 -0.03315 0.01111  50 HIS A N   
406  C CA  . HIS A 53 ? 0.40749 0.54922 0.52940 -0.04331 -0.03385 0.02989  50 HIS A CA  
407  C C   . HIS A 53 ? 0.39551 0.53709 0.52272 -0.03311 -0.02626 0.04192  50 HIS A C   
408  O O   . HIS A 53 ? 0.40867 0.57009 0.54488 -0.03092 -0.02764 0.06064  50 HIS A O   
409  C CB  . HIS A 53 ? 0.47436 0.60714 0.60394 -0.03863 -0.02947 0.03347  50 HIS A CB  
410  C CG  . HIS A 53 ? 0.60128 0.75300 0.75217 -0.03177 -0.02270 0.05387  50 HIS A CG  
411  N ND1 . HIS A 53 ? 0.69312 0.82757 0.84303 -0.01606 -0.00728 0.05866  50 HIS A ND1 
412  C CD2 . HIS A 53 ? 0.57076 0.75967 0.74660 -0.03727 -0.02842 0.07122  50 HIS A CD2 
413  C CE1 . HIS A 53 ? 0.65982 0.81796 0.83659 -0.00834 0.00151  0.07877  50 HIS A CE1 
414  N NE2 . HIS A 53 ? 0.62205 0.81917 0.82039 -0.02091 -0.01329 0.08879  50 HIS A NE2 
415  N N   . PHE A 54 ? 0.33962 0.45795 0.46186 -0.02766 -0.01939 0.03243  51 PHE A N   
416  C CA  . PHE A 54 ? 0.46007 0.56579 0.58413 -0.02228 -0.00967 0.04047  51 PHE A CA  
417  C C   . PHE A 54 ? 0.36205 0.48004 0.48373 -0.02858 -0.00940 0.04897  51 PHE A C   
418  O O   . PHE A 54 ? 0.40344 0.51990 0.52816 -0.02216 -0.00308 0.06867  51 PHE A O   
419  C CB  . PHE A 54 ? 0.38646 0.46512 0.50351 -0.02362 -0.00656 0.02400  51 PHE A CB  
420  C CG  . PHE A 54 ? 0.45723 0.51412 0.57474 -0.02558 0.00428  0.02736  51 PHE A CG  
421  C CD1 . PHE A 54 ? 0.48022 0.50723 0.59225 -0.01499 0.01785  0.03452  51 PHE A CD1 
422  C CD2 . PHE A 54 ? 0.50126 0.56328 0.62538 -0.03785 0.00541  0.02398  51 PHE A CD2 
423  C CE1 . PHE A 54 ? 0.49285 0.48764 0.60302 -0.01779 0.03072  0.03718  51 PHE A CE1 
424  C CE2 . PHE A 54 ? 0.54973 0.58616 0.67544 -0.04339 0.01781  0.02885  51 PHE A CE2 
425  C CZ  . PHE A 54 ? 0.49761 0.49635 0.61487 -0.03402 0.02965  0.03483  51 PHE A CZ  
426  N N   . LEU A 55 ? 0.25785 0.38514 0.37164 -0.03868 -0.01311 0.03630  52 LEU A N   
427  C CA  . LEU A 55 ? 0.32004 0.45652 0.42183 -0.04520 -0.00847 0.04383  52 LEU A CA  
428  C C   . LEU A 55 ? 0.36414 0.52115 0.45386 -0.04515 -0.01779 0.06377  52 LEU A C   
429  O O   . LEU A 55 ? 0.34448 0.50475 0.42390 -0.04367 -0.01404 0.08367  52 LEU A O   
430  C CB  . LEU A 55 ? 0.28250 0.42431 0.37645 -0.05295 -0.00538 0.02452  52 LEU A CB  
431  C CG  . LEU A 55 ? 0.29974 0.43674 0.41548 -0.05355 0.00255  0.01093  52 LEU A CG  
432  C CD1 . LEU A 55 ? 0.36852 0.51634 0.48455 -0.05486 0.00988  -0.00438 52 LEU A CD1 
433  C CD2 . LEU A 55 ? 0.19130 0.32066 0.31652 -0.05912 0.01444  0.02143  52 LEU A CD2 
434  N N   . LEU A 56 ? 0.37862 0.55145 0.47081 -0.04814 -0.03136 0.06119  53 LEU A N   
435  C CA  . LEU A 56 ? 0.35396 0.55749 0.44105 -0.05257 -0.04688 0.07983  53 LEU A CA  
436  C C   . LEU A 56 ? 0.38380 0.60111 0.49964 -0.03581 -0.04618 0.10967  53 LEU A C   
437  O O   . LEU A 56 ? 0.42611 0.67037 0.54047 -0.03305 -0.05687 0.13521  53 LEU A O   
438  C CB  . LEU A 56 ? 0.43533 0.65175 0.52172 -0.06713 -0.06153 0.06596  53 LEU A CB  
439  C CG  . LEU A 56 ? 0.37216 0.56713 0.42833 -0.08049 -0.05907 0.03637  53 LEU A CG  
440  C CD1 . LEU A 56 ? 0.56256 0.76030 0.61692 -0.09753 -0.07224 0.02419  53 LEU A CD1 
441  C CD2 . LEU A 56 ? 0.51559 0.71137 0.53133 -0.08766 -0.05709 0.03467  53 LEU A CD2 
442  N N   . LEU A 57 ? 0.35841 0.55714 0.49779 -0.02263 -0.03307 0.10803  54 LEU A N   
443  C CA  . LEU A 57 ? 0.49794 0.69880 0.66326 -0.00147 -0.02324 0.13433  54 LEU A CA  
444  C C   . LEU A 57 ? 0.34490 0.52279 0.49903 0.00759  -0.01213 0.15048  54 LEU A C   
445  O O   . LEU A 57 ? 0.44136 0.63635 0.60740 0.02190  -0.01388 0.18271  54 LEU A O   
446  C CB  . LEU A 57 ? 0.50106 0.67344 0.67821 0.00961  -0.00579 0.12297  54 LEU A CB  
447  C CG  . LEU A 57 ? 0.58185 0.77160 0.77374 0.00579  -0.00880 0.11592  54 LEU A CG  
448  C CD1 . LEU A 57 ? 0.57551 0.72463 0.75802 0.01588  0.01081  0.10181  54 LEU A CD1 
449  C CD2 . LEU A 57 ? 0.50337 0.74266 0.73552 0.01339  -0.01362 0.14416  54 LEU A CD2 
450  N N   . SER A 58 ? 0.33835 0.47923 0.47348 -0.00089 -0.00064 0.13111  55 SER A N   
451  C CA  . SER A 58 ? 0.47766 0.58743 0.60460 0.00316  0.01491  0.14478  55 SER A CA  
452  C C   . SER A 58 ? 0.44662 0.57651 0.55073 -0.00383 0.00784  0.16340  55 SER A C   
453  O O   . SER A 58 ? 0.56274 0.69041 0.66525 0.00929  0.01154  0.19672  55 SER A O   
454  C CB  . SER A 58 ? 0.42827 0.50052 0.54965 -0.00972 0.02718  0.11712  55 SER A CB  
455  O OG  . SER A 58 ? 0.48057 0.57266 0.59448 -0.02600 0.01718  0.09341  55 SER A OG  
456  N N   . LEU A 59 ? 0.34688 0.49309 0.42888 -0.02223 -0.00033 0.14369  56 LEU A N   
457  C CA  . LEU A 59 ? 0.41506 0.56951 0.46211 -0.03117 0.00031  0.15540  56 LEU A CA  
458  C C   . LEU A 59 ? 0.36806 0.56246 0.39286 -0.03230 -0.02418 0.17298  56 LEU A C   
459  O O   . LEU A 59 ? 0.48774 0.68842 0.47969 -0.03238 -0.02604 0.19750  56 LEU A O   
460  C CB  . LEU A 59 ? 0.33528 0.48494 0.36705 -0.04824 0.00954  0.12466  56 LEU A CB  
461  C CG  . LEU A 59 ? 0.40881 0.53175 0.46790 -0.05173 0.02778  0.10793  56 LEU A CG  
462  C CD1 . LEU A 59 ? 0.42691 0.55805 0.48259 -0.06440 0.03741  0.08350  56 LEU A CD1 
463  C CD2 . LEU A 59 ? 0.42551 0.51837 0.48950 -0.04936 0.04604  0.13111  56 LEU A CD2 
464  N N   . VAL A 60 ? 0.43702 0.65906 0.47672 -0.03581 -0.04406 0.16218  57 VAL A N   
465  C CA  . VAL A 60 ? 0.43187 0.69741 0.45455 -0.04431 -0.07288 0.17470  57 VAL A CA  
466  C C   . VAL A 60 ? 0.45279 0.75305 0.51752 -0.02562 -0.08643 0.21111  57 VAL A C   
467  O O   . VAL A 60 ? 0.51612 0.84663 0.56926 -0.02001 -0.10347 0.24468  57 VAL A O   
468  C CB  . VAL A 60 ? 0.59602 0.87027 0.61078 -0.06564 -0.08599 0.13972  57 VAL A CB  
469  C CG1 . VAL A 60 ? 0.68857 1.00884 0.69008 -0.08115 -0.11979 0.14974  57 VAL A CG1 
470  C CG2 . VAL A 60 ? 0.40791 0.65006 0.38193 -0.07832 -0.06982 0.10790  57 VAL A CG2 
471  N N   . LYS A 61 ? 0.45170 0.74981 0.56551 -0.01350 -0.07763 0.20731  58 LYS A N   
472  C CA  . LYS A 61 ? 0.47861 0.81167 0.64221 0.00883  -0.08295 0.24191  58 LYS A CA  
473  C C   . LYS A 61 ? 0.41892 0.72180 0.59376 0.03893  -0.06070 0.27291  58 LYS A C   
474  O O   . LYS A 61 ? 0.55084 0.87503 0.76076 0.05986  -0.05919 0.30001  58 LYS A O   
475  C CB  . LYS A 61 ? 0.49407 0.83266 0.70150 0.01177  -0.07481 0.22705  58 LYS A CB  
476  C CG  . LYS A 61 ? 0.59234 0.97485 0.81759 -0.00422 -0.09431 0.22450  58 LYS A CG  
477  C CD  . LYS A 61 ? 0.55393 0.93734 0.82318 0.00601  -0.07709 0.22201  58 LYS A CD  
478  C CE  . LYS A 61 ? 0.59995 1.02381 0.88884 -0.01079 -0.09421 0.22295  58 LYS A CE  
479  N NZ  . LYS A 61 ? 0.43650 0.90010 0.72938 -0.00918 -0.11434 0.24906  58 LYS A NZ  
480  N N   . GLY A 62 ? 0.50043 0.74531 0.64559 0.03724  -0.03754 0.26059  59 GLY A N   
481  C CA  . GLY A 62 ? 0.43007 0.63406 0.57984 0.06077  -0.01440 0.28880  59 GLY A CA  
482  C C   . GLY A 62 ? 0.44861 0.62214 0.63858 0.08586  0.00994  0.29074  59 GLY A C   
483  O O   . GLY A 62 ? 0.65634 0.81984 0.86751 0.11397  0.02263  0.32311  59 GLY A O   
484  N N   . LEU A 63 ? 0.45356 0.60812 0.64880 0.07646  0.01914  0.25347  60 LEU A N   
485  C CA  . LEU A 63 ? 0.43306 0.55309 0.65263 0.09769  0.04487  0.24884  60 LEU A CA  
486  C C   . LEU A 63 ? 0.46576 0.50615 0.65886 0.09257  0.07069  0.22738  60 LEU A C   
487  O O   . LEU A 63 ? 0.51180 0.53665 0.67841 0.06545  0.06560  0.19955  60 LEU A O   
488  C CB  . LEU A 63 ? 0.35865 0.50287 0.59150 0.08949  0.03980  0.22327  60 LEU A CB  
489  C CG  . LEU A 63 ? 0.48688 0.69919 0.76612 0.10118  0.02805  0.24629  60 LEU A CG  
490  C CD1 . LEU A 63 ? 0.61215 0.88547 0.89778 0.09353  -0.00354 0.27310  60 LEU A CD1 
491  C CD2 . LEU A 63 ? 0.37322 0.60137 0.65383 0.08252  0.02249  0.21777  60 LEU A CD2 
492  N N   . SER A 64 ? 0.43582 0.42617 0.63928 0.11831  0.09927  0.24016  61 SER A N   
493  C CA  . SER A 64 ? 0.62286 0.52988 0.80001 0.11003  0.12400  0.21938  61 SER A CA  
494  C C   . SER A 64 ? 0.54307 0.43139 0.69811 0.08491  0.12113  0.17082  61 SER A C   
495  O O   . SER A 64 ? 0.45110 0.37533 0.61241 0.08532  0.11089  0.15786  61 SER A O   
496  C CB  . SER A 64 ? 0.66838 0.51765 0.85724 0.14450  0.15846  0.23738  61 SER A CB  
497  O OG  . SER A 64 ? 0.60513 0.47122 0.81135 0.16355  0.16828  0.22871  61 SER A OG  
498  N N   . PRO A 65 ? 0.58899 0.42399 0.71949 0.06111  0.12846  0.14588  62 PRO A N   
499  C CA  . PRO A 65 ? 0.58754 0.40928 0.69725 0.03801  0.12080  0.10269  62 PRO A CA  
500  C C   . PRO A 65 ? 0.57542 0.36887 0.67248 0.05518  0.13578  0.08771  62 PRO A C   
501  O O   . PRO A 65 ? 0.58411 0.39823 0.66847 0.04612  0.12250  0.06510  62 PRO A O   
502  C CB  . PRO A 65 ? 0.60339 0.36943 0.69749 0.01133  0.12924  0.08552  62 PRO A CB  
503  C CG  . PRO A 65 ? 0.68988 0.46257 0.79717 0.01276  0.13443  0.11924  62 PRO A CG  
504  C CD  . PRO A 65 ? 0.59937 0.39105 0.72253 0.05066  0.14103  0.15818  62 PRO A CD  
505  N N   . GLU A 66 ? 0.66814 0.41107 0.76590 0.08213  0.16667  0.10147  63 GLU A N   
506  C CA  . GLU A 66 ? 0.80306 0.51771 0.88654 0.10292  0.18903  0.08892  63 GLU A CA  
507  C C   . GLU A 66 ? 0.67045 0.46161 0.78602 0.12097  0.18031  0.10764  63 GLU A C   
508  O O   . GLU A 66 ? 0.56751 0.36261 0.66550 0.12040  0.18320  0.08871  63 GLU A O   
509  C CB  . GLU A 66 ? 0.81830 0.45990 0.90076 0.13317  0.23008  0.10248  63 GLU A CB  
510  C CG  . GLU A 66 ? 1.11090 0.72567 1.16980 0.15175  0.25730  0.08514  63 GLU A CG  
511  C CD  . GLU A 66 ? 1.19883 0.74299 1.19138 0.12495  0.26070  0.03503  63 GLU A CD  
512  O OE1 . GLU A 66 ? 1.27239 0.78034 1.24326 0.09152  0.24575  0.01391  63 GLU A OE1 
513  O OE2 . GLU A 66 ? 1.20535 0.73580 1.16663 0.13415  0.27641  0.01768  63 GLU A OE2 
514  N N   . THR A 67 ? 0.50741 0.35996 0.66792 0.13437  0.16865  0.14571  64 THR A N   
515  C CA  . THR A 67 ? 0.50081 0.43186 0.69817 0.14372  0.15599  0.16328  64 THR A CA  
516  C C   . THR A 67 ? 0.49350 0.45783 0.67312 0.11275  0.12797  0.13741  64 THR A C   
517  O O   . THR A 67 ? 0.39636 0.37743 0.57638 0.11435  0.13181  0.12900  64 THR A O   
518  C CB  . THR A 67 ? 0.52367 0.51657 0.76582 0.15603  0.13965  0.20642  64 THR A CB  
519  O OG1 . THR A 67 ? 0.67690 0.64966 0.93834 0.18680  0.16554  0.23217  64 THR A OG1 
520  C CG2 . THR A 67 ? 0.53848 0.61758 0.81810 0.15266  0.11798  0.21904  64 THR A CG2 
521  N N   . THR A 68 ? 0.40519 0.37676 0.56967 0.08621  0.10336  0.12656  65 THR A N   
522  C CA  . THR A 68 ? 0.36333 0.36301 0.51473 0.06162  0.07923  0.10445  65 THR A CA  
523  C C   . THR A 68 ? 0.35921 0.31960 0.47602 0.05556  0.08649  0.07391  65 THR A C   
524  O O   . THR A 68 ? 0.38526 0.36791 0.49754 0.05053  0.07781  0.06618  65 THR A O   
525  C CB  . THR A 68 ? 0.37247 0.37971 0.51451 0.03878  0.06012  0.09722  65 THR A CB  
526  O OG1 . THR A 68 ? 0.51558 0.46876 0.63666 0.02952  0.07071  0.08101  65 THR A OG1 
527  C CG2 . THR A 68 ? 0.40787 0.45055 0.56905 0.04368  0.05223  0.12790  65 THR A CG2 
528  N N   . LYS A 69 ? 0.37565 0.27393 0.46317 0.05416  0.10170  0.05672  66 LYS A N   
529  C CA  . LYS A 69 ? 0.46080 0.32003 0.50427 0.04618  0.10477  0.02658  66 LYS A CA  
530  C C   . LYS A 69 ? 0.49431 0.35494 0.53116 0.06697  0.12494  0.03198  66 LYS A C   
531  O O   . LYS A 69 ? 0.48032 0.34538 0.49046 0.05980  0.11706  0.01865  66 LYS A O   
532  C CB  . LYS A 69 ? 0.57522 0.36164 0.58548 0.03866  0.11927  0.00606  66 LYS A CB  
533  C CG  . LYS A 69 ? 0.70930 0.44743 0.66175 0.03189  0.12444  -0.02569 66 LYS A CG  
534  C CD  . LYS A 69 ? 0.73887 0.39502 0.65481 0.02311  0.14253  -0.04809 66 LYS A CD  
535  C CE  . LYS A 69 ? 0.86803 0.48918 0.80568 0.05226  0.17986  -0.02540 66 LYS A CE  
536  N NZ  . LYS A 69 ? 1.07461 0.71031 1.02237 0.08858  0.20695  -0.00693 66 LYS A NZ  
537  N N   . LEU A 70 ? 0.56524 0.42422 0.62898 0.09461  0.15307  0.05493  67 LEU A N   
538  C CA  . LEU A 70 ? 0.48945 0.35973 0.55932 0.11593  0.17806  0.06452  67 LEU A CA  
539  C C   . LEU A 70 ? 0.47470 0.41500 0.57432 0.10626  0.15732  0.07740  67 LEU A C   
540  O O   . LEU A 70 ? 0.43852 0.37767 0.51604 0.10489  0.16505  0.07032  67 LEU A O   
541  C CB  . LEU A 70 ? 0.53988 0.41008 0.65160 0.15064  0.21108  0.09298  67 LEU A CB  
542  C CG  . LEU A 70 ? 0.80327 0.58519 0.87931 0.16565  0.24401  0.07888  67 LEU A CG  
543  C CD1 . LEU A 70 ? 0.79587 0.58784 0.91906 0.19922  0.27122  0.11294  67 LEU A CD1 
544  C CD2 . LEU A 70 ? 0.84050 0.55917 0.84649 0.16380  0.26719  0.04458  67 LEU A CD2 
545  N N   . LEU A 71 ? 0.39204 0.38753 0.53507 0.09736  0.13171  0.09554  68 LEU A N   
546  C CA  . LEU A 71 ? 0.39835 0.45223 0.56790 0.08409  0.11244  0.10483  68 LEU A CA  
547  C C   . LEU A 71 ? 0.34163 0.37947 0.47015 0.06194  0.09352  0.07988  68 LEU A C   
548  O O   . LEU A 71 ? 0.36463 0.41741 0.49249 0.05670  0.09400  0.08162  68 LEU A O   
549  C CB  . LEU A 71 ? 0.32298 0.43054 0.53404 0.07646  0.08762  0.12472  68 LEU A CB  
550  C CG  . LEU A 71 ? 0.36875 0.50725 0.62898 0.10095  0.09997  0.15828  68 LEU A CG  
551  C CD1 . LEU A 71 ? 0.39732 0.58983 0.68448 0.08931  0.06849  0.17713  68 LEU A CD1 
552  C CD2 . LEU A 71 ? 0.53598 0.70716 0.83743 0.11868  0.12400  0.17674  68 LEU A CD2 
553  N N   . MET A 72 ? 0.29924 0.30852 0.39803 0.04939  0.07778  0.05963  69 MET A N   
554  C CA  . MET A 72 ? 0.37122 0.37077 0.43839 0.03321  0.05861  0.03964  69 MET A CA  
555  C C   . MET A 72 ? 0.37295 0.33634 0.39465 0.03917  0.07259  0.02872  69 MET A C   
556  O O   . MET A 72 ? 0.41060 0.37907 0.41597 0.03381  0.06393  0.02740  69 MET A O   
557  C CB  . MET A 72 ? 0.35497 0.33992 0.41074 0.01961  0.04150  0.02282  69 MET A CB  
558  C CG  . MET A 72 ? 0.36547 0.38330 0.45402 0.01220  0.02941  0.03287  69 MET A CG  
559  S SD  . MET A 72 ? 0.44110 0.50358 0.54865 0.00333  0.01210  0.03909  69 MET A SD  
560  C CE  . MET A 72 ? 0.39452 0.43971 0.47470 -0.00351 -0.00104 0.01846  69 MET A CE  
561  N N   . LYS A 73 ? 0.38245 0.30273 0.37684 0.05083  0.09622  0.02111  70 LYS A N   
562  C CA  . LYS A 73 ? 0.49263 0.37266 0.42995 0.05657  0.11289  0.00893  70 LYS A CA  
563  C C   . LYS A 73 ? 0.47516 0.37971 0.42646 0.06792  0.13335  0.02949  70 LYS A C   
564  O O   . LYS A 73 ? 0.57496 0.46691 0.48506 0.06478  0.13334  0.02634  70 LYS A O   
565  C CB  . LYS A 73 ? 0.50755 0.32862 0.41026 0.06771  0.14087  -0.00541 70 LYS A CB  
566  C CG  . LYS A 73 ? 0.59074 0.36911 0.45166 0.04777  0.12120  -0.03499 70 LYS A CG  
567  C CD  . LYS A 73 ? 0.88440 0.59173 0.70774 0.05647  0.15285  -0.05174 70 LYS A CD  
568  C CE  . LYS A 73 ? 0.90411 0.56208 0.66957 0.02929  0.13233  -0.08739 70 LYS A CE  
569  N NZ  . LYS A 73 ? 1.10334 0.75252 0.80199 0.01956  0.11614  -0.10383 70 LYS A NZ  
570  N N   . GLU A 74 ? 0.53760 0.48047 0.54922 0.08025  0.15033  0.05356  71 GLU A N   
571  C CA  . GLU A 74 ? 0.47212 0.44796 0.51128 0.08667  0.17066  0.07525  71 GLU A CA  
572  C C   . GLU A 74 ? 0.47917 0.48778 0.53301 0.06534  0.14361  0.08104  71 GLU A C   
573  O O   . GLU A 74 ? 0.44030 0.45249 0.48724 0.06313  0.15730  0.09109  71 GLU A O   
574  C CB  . GLU A 74 ? 0.48077 0.50189 0.59276 0.10369  0.19012  0.10188  71 GLU A CB  
575  C CG  . GLU A 74 ? 0.76224 0.74699 0.86381 0.13363  0.23335  0.10275  71 GLU A CG  
576  C CD  . GLU A 74 ? 0.86830 0.82559 0.92971 0.14494  0.27274  0.10044  71 GLU A CD  
577  O OE1 . GLU A 74 ? 0.89477 0.88788 0.97363 0.13486  0.27411  0.11473  71 GLU A OE1 
578  O OE2 . GLU A 74 ? 0.98455 0.87904 0.99191 0.16245  0.30457  0.08368  71 GLU A OE2 
579  N N   . LEU A 75 ? 0.36801 0.39475 0.43929 0.04994  0.10951  0.07508  72 LEU A N   
580  C CA  . LEU A 75 ? 0.45592 0.50043 0.53473 0.03135  0.08689  0.07628  72 LEU A CA  
581  C C   . LEU A 75 ? 0.44482 0.44954 0.46516 0.02884  0.07888  0.06320  72 LEU A C   
582  O O   . LEU A 75 ? 0.41793 0.42108 0.43229 0.02234  0.07853  0.07165  72 LEU A O   
583  C CB  . LEU A 75 ? 0.41701 0.48584 0.52253 0.01864  0.05835  0.07117  72 LEU A CB  
584  C CG  . LEU A 75 ? 0.51591 0.60921 0.64428 -0.00035 0.04150  0.07492  72 LEU A CG  
585  C CD1 . LEU A 75 ? 0.44550 0.58180 0.62315 -0.00640 0.05127  0.09607  72 LEU A CD1 
586  C CD2 . LEU A 75 ? 0.52198 0.62524 0.65576 -0.01038 0.01763  0.06361  72 LEU A CD2 
587  N N   . ILE A 76 ? 0.39333 0.36583 0.37108 0.03267  0.07085  0.04434  73 ILE A N   
588  C CA  . ILE A 76 ? 0.43527 0.37699 0.35598 0.03134  0.05813  0.03432  73 ILE A CA  
589  C C   . ILE A 76 ? 0.53531 0.45270 0.41354 0.04035  0.08487  0.04472  73 ILE A C   
590  O O   . ILE A 76 ? 0.46183 0.36719 0.30924 0.03897  0.07820  0.05246  73 ILE A O   
591  C CB  . ILE A 76 ? 0.52308 0.44061 0.41002 0.02863  0.04300  0.01101  73 ILE A CB  
592  C CG1 . ILE A 76 ? 0.43396 0.37794 0.36305 0.01798  0.01830  0.00380  73 ILE A CG1 
593  C CG2 . ILE A 76 ? 0.55839 0.44931 0.38120 0.02745  0.02721  0.00262  73 ILE A CG2 
594  C CD1 . ILE A 76 ? 0.52762 0.45271 0.44222 0.01082  0.01055  -0.01622 73 ILE A CD1 
595  N N   . LYS A 77 ? 0.49726 0.40493 0.37249 0.05212  0.11908  0.04754  74 LYS A N   
596  C CA  . LYS A 77 ? 0.59027 0.47549 0.42463 0.06209  0.15304  0.05833  74 LYS A CA  
597  C C   . LYS A 77 ? 0.61915 0.53484 0.49385 0.05563  0.16219  0.08484  74 LYS A C   
598  O O   . LYS A 77 ? 0.71606 0.60996 0.54752 0.05501  0.17053  0.09533  74 LYS A O   
599  C CB  . LYS A 77 ? 0.74224 0.61422 0.57746 0.07988  0.19442  0.05697  74 LYS A CB  
600  C CG  . LYS A 77 ? 0.89420 0.71719 0.67581 0.08378  0.19205  0.02788  74 LYS A CG  
601  C CD  . LYS A 77 ? 0.79764 0.59416 0.57334 0.10616  0.24141  0.02685  74 LYS A CD  
602  C CE  . LYS A 77 ? 1.10063 0.83890 0.82643 0.10621  0.23978  -0.00471 74 LYS A CE  
603  N NZ  . LYS A 77 ? 1.16731 0.86243 0.80117 0.08857  0.21239  -0.03101 74 LYS A NZ  
604  N N   . GLU A 78 ? 0.50819 0.47250 0.46300 0.04825  0.15926  0.09658  75 GLU A N   
605  C CA  . GLU A 78 ? 0.52359 0.51643 0.52148 0.03430  0.16456  0.11829  75 GLU A CA  
606  C C   . GLU A 78 ? 0.49735 0.46709 0.46711 0.02180  0.13898  0.11693  75 GLU A C   
607  O O   . GLU A 78 ? 0.55475 0.51728 0.52434 0.01331  0.15203  0.13478  75 GLU A O   
608  C CB  . GLU A 78 ? 0.64145 0.69200 0.72370 0.02350  0.15448  0.12609  75 GLU A CB  
609  C CG  . GLU A 78 ? 0.64643 0.73656 0.78133 0.03585  0.18665  0.14378  75 GLU A CG  
610  C CD  . GLU A 78 ? 0.79398 0.91305 0.96797 0.02584  0.21405  0.16899  75 GLU A CD  
611  O OE1 . GLU A 78 ? 0.85319 0.93862 0.98612 0.01694  0.22178  0.17260  75 GLU A OE1 
612  O OE2 . GLU A 78 ? 0.90313 1.07732 1.14811 0.02658  0.22285  0.18465  75 GLU A OE2 
613  N N   . LEU A 79 ? 0.40677 0.36414 0.35671 0.02159  0.10544  0.09828  76 LEU A N   
614  C CA  . LEU A 79 ? 0.43521 0.37328 0.36718 0.01589  0.08264  0.09915  76 LEU A CA  
615  C C   . LEU A 79 ? 0.55030 0.44698 0.41049 0.02671  0.08852  0.10792  76 LEU A C   
616  O O   . LEU A 79 ? 0.51723 0.39391 0.36558 0.02435  0.08806  0.12418  76 LEU A O   
617  C CB  . LEU A 79 ? 0.44607 0.39174 0.38667 0.01530  0.04902  0.07923  76 LEU A CB  
618  C CG  . LEU A 79 ? 0.59406 0.57165 0.59285 0.00201  0.03767  0.07340  76 LEU A CG  
619  C CD1 . LEU A 79 ? 0.57093 0.55404 0.57136 0.00416  0.01237  0.05490  76 LEU A CD1 
620  C CD2 . LEU A 79 ? 0.43195 0.40339 0.45050 -0.01156 0.03866  0.08331  76 LEU A CD2 
621  N N   . GLU A 80 ? 0.62759 0.50556 0.43320 0.03806  0.09401  0.09766  77 GLU A N   
622  C CA  . GLU A 80 ? 0.82452 0.66336 0.54876 0.04708  0.09525  0.10555  77 GLU A CA  
623  C C   . GLU A 80 ? 0.82397 0.64635 0.52910 0.04862  0.13598  0.13147  77 GLU A C   
624  O O   . GLU A 80 ? 0.94632 0.73516 0.58760 0.05449  0.13764  0.14743  77 GLU A O   
625  C CB  . GLU A 80 ? 0.87308 0.69095 0.53404 0.05364  0.08936  0.08274  77 GLU A CB  
626  C CG  . GLU A 80 ? 1.06433 0.86894 0.70770 0.06027  0.13179  0.07705  77 GLU A CG  
627  C CD  . GLU A 80 ? 1.17166 0.94116 0.74281 0.06321  0.12563  0.04885  77 GLU A CD  
628  O OE1 . GLU A 80 ? 1.26799 1.02593 0.79188 0.05794  0.08723  0.03832  77 GLU A OE1 
629  O OE2 . GLU A 80 ? 1.15397 0.90733 0.71782 0.07037  0.15880  0.03716  77 GLU A OE2 
630  N N   . LYS A 81 ? 0.64317 0.49223 0.40489 0.04356  0.16878  0.13933  78 LYS A N   
631  C CA  . LYS A 81 ? 0.79813 0.64085 0.55771 0.04139  0.21063  0.16676  78 LYS A CA  
632  C C   . LYS A 81 ? 0.72280 0.55920 0.50714 0.02634  0.20321  0.18827  78 LYS A C   
633  O O   . LYS A 81 ? 0.86377 0.67714 0.62260 0.02403  0.23279  0.21418  78 LYS A O   
634  C CB  . LYS A 81 ? 0.70597 0.59207 0.53598 0.03989  0.24573  0.17211  78 LYS A CB  
635  C CG  . LYS A 81 ? 0.91932 0.79044 0.70664 0.06063  0.28258  0.16440  78 LYS A CG  
636  C CD  . LYS A 81 ? 0.92650 0.78534 0.69017 0.07005  0.25718  0.13248  78 LYS A CD  
637  C CE  . LYS A 81 ? 1.14367 0.96414 0.84095 0.08959  0.29210  0.11808  78 LYS A CE  
638  N NZ  . LYS A 81 ? 1.02291 0.82284 0.69584 0.09220  0.26420  0.08531  78 LYS A NZ  
639  N N   . ILE A 82 ? 0.60939 0.45946 0.43899 0.01604  0.16846  0.17802  79 ILE A N   
640  C CA  . ILE A 82 ? 0.75865 0.58918 0.60616 0.00276  0.16158  0.19335  79 ILE A CA  
641  C C   . ILE A 82 ? 0.76383 0.56032 0.56366 0.01751  0.12781  0.18993  79 ILE A C   
642  O O   . ILE A 82 ? 0.76699 0.53424 0.56997 0.01445  0.12186  0.20346  79 ILE A O   
643  C CB  . ILE A 82 ? 0.67509 0.54143 0.60711 -0.02082 0.15164  0.18405  79 ILE A CB  
644  C CG1 . ILE A 82 ? 0.65947 0.54545 0.60710 -0.01580 0.11516  0.15574  79 ILE A CG1 
645  C CG2 . ILE A 82 ? 0.53311 0.44788 0.52242 -0.03360 0.17934  0.19122  79 ILE A CG2 
646  C CD1 . ILE A 82 ? 0.61076 0.52850 0.62496 -0.03853 0.10292  0.14456  79 ILE A CD1 
647  N N   . SER B 4  ? 0.87698 0.50939 0.52126 0.08118  -0.05416 0.16702  1  SER B N   
648  C CA  . SER B 4  ? 0.84526 0.52837 0.53540 0.09218  -0.05793 0.13946  1  SER B CA  
649  C C   . SER B 4  ? 0.77855 0.46462 0.50184 0.08318  -0.04076 0.11535  1  SER B C   
650  O O   . SER B 4  ? 0.71372 0.43896 0.46102 0.07800  -0.03861 0.09203  1  SER B O   
651  C CB  . SER B 4  ? 0.97656 0.67101 0.69437 0.12306  -0.07922 0.14747  1  SER B CB  
652  O OG  . SER B 4  ? 0.72384 0.46672 0.48229 0.12546  -0.08447 0.12660  1  SER B OG  
653  N N   . ILE B 5  ? 0.80499 0.44459 0.52692 0.08194  -0.03225 0.12063  2  ILE B N   
654  C CA  . ILE B 5  ? 0.75924 0.40083 0.50610 0.06957  -0.01784 0.09820  2  ILE B CA  
655  C C   . ILE B 5  ? 0.74375 0.41335 0.48422 0.03895  -0.00242 0.08676  2  ILE B C   
656  O O   . ILE B 5  ? 0.73475 0.44004 0.50538 0.03386  0.00281  0.06289  2  ILE B O   
657  C CB  . ILE B 5  ? 0.92248 0.50003 0.66053 0.07198  -0.01466 0.10369  2  ILE B CB  
658  C CG1 . ILE B 5  ? 0.96015 0.52505 0.71375 0.11112  -0.02766 0.10605  2  ILE B CG1 
659  C CG2 . ILE B 5  ? 0.70823 0.28860 0.46495 0.05269  -0.00155 0.08037  2  ILE B CG2 
660  C CD1 . ILE B 5  ? 0.86449 0.48464 0.66050 0.12470  -0.02734 0.08460  2  ILE B CD1 
661  N N   . LYS B 6  ? 0.71297 0.37196 0.41425 0.01886  0.00454  0.10464  3  LYS B N   
662  C CA  . LYS B 6  ? 0.75886 0.46508 0.45551 -0.00720 0.02174  0.09235  3  LYS B CA  
663  C C   . LYS B 6  ? 0.73020 0.49381 0.44412 0.00850  0.01594  0.06805  3  LYS B C   
664  O O   . LYS B 6  ? 0.75828 0.56525 0.49815 0.00368  0.02471  0.04169  3  LYS B O   
665  C CB  . LYS B 6  ? 0.86399 0.55681 0.50851 -0.03287 0.03045  0.12030  3  LYS B CB  
666  C CG  . LYS B 6  ? 0.85782 0.61759 0.49565 -0.05884 0.05238  0.10701  3  LYS B CG  
667  C CD  . LYS B 6  ? 0.95311 0.71114 0.53080 -0.08406 0.06035  0.13791  3  LYS B CD  
668  C CE  . LYS B 6  ? 1.08555 0.84305 0.63031 -0.05973 0.04216  0.14680  3  LYS B CE  
669  N NZ  . LYS B 6  ? 0.97951 0.74164 0.45799 -0.08548 0.04907  0.17767  3  LYS B NZ  
670  N N   . GLU B 7  ? 0.70172 0.46365 0.40233 0.02817  -0.00229 0.07577  4  GLU B N   
671  C CA  . GLU B 7  ? 0.64393 0.44599 0.35606 0.04124  -0.01386 0.05220  4  GLU B CA  
672  C C   . GLU B 7  ? 0.66279 0.47538 0.42437 0.05194  -0.02165 0.03038  4  GLU B C   
673  O O   . GLU B 7  ? 0.57717 0.41884 0.35472 0.05549  -0.02477 0.00402  4  GLU B O   
674  C CB  . GLU B 7  ? 0.74777 0.54220 0.43802 0.05574  -0.03659 0.06767  4  GLU B CB  
675  C CG  . GLU B 7  ? 0.75932 0.58448 0.45037 0.06420  -0.05303 0.04371  4  GLU B CG  
676  C CD  . GLU B 7  ? 0.83698 0.65775 0.51318 0.07476  -0.07994 0.05967  4  GLU B CD  
677  O OE1 . GLU B 7  ? 0.88571 0.69774 0.59165 0.08544  -0.09348 0.07377  4  GLU B OE1 
678  O OE2 . GLU B 7  ? 0.83374 0.66680 0.46852 0.07218  -0.08744 0.05723  4  GLU B OE2 
679  N N   . ILE B 8  ? 0.71238 0.50063 0.49571 0.05864  -0.02597 0.04075  5  ILE B N   
680  C CA  . ILE B 8  ? 0.58923 0.38901 0.41263 0.06435  -0.03273 0.02535  5  ILE B CA  
681  C C   . ILE B 8  ? 0.62394 0.43682 0.46373 0.05133  -0.01818 0.00694  5  ILE B C   
682  O O   . ILE B 8  ? 0.57116 0.40584 0.43683 0.05494  -0.02619 -0.01207 5  ILE B O   
683  C CB  . ILE B 8  ? 0.57620 0.35699 0.41317 0.07546  -0.03717 0.03959  5  ILE B CB  
684  C CG1 . ILE B 8  ? 0.70763 0.49771 0.54419 0.09025  -0.05599 0.05418  5  ILE B CG1 
685  C CG2 . ILE B 8  ? 0.55320 0.34612 0.42221 0.07458  -0.03808 0.02649  5  ILE B CG2 
686  C CD1 . ILE B 8  ? 0.84883 0.63449 0.70106 0.10681  -0.05789 0.06677  5  ILE B CD1 
687  N N   . THR B 9  ? 0.61490 0.41357 0.44044 0.03460  0.00008  0.01398  6  THR B N   
688  C CA  . THR B 9  ? 0.62888 0.44945 0.47339 0.01776  0.01306  -0.00214 6  THR B CA  
689  C C   . THR B 9  ? 0.51310 0.38549 0.36423 0.01701  0.01829  -0.02262 6  THR B C   
690  O O   . THR B 9  ? 0.58086 0.48493 0.46496 0.02208  0.01450  -0.04481 6  THR B O   
691  C CB  . THR B 9  ? 0.59374 0.38462 0.41805 -0.00693 0.02878  0.01290  6  THR B CB  
692  O OG1 . THR B 9  ? 0.65288 0.38984 0.47007 0.00183  0.02181  0.02546  6  THR B OG1 
693  C CG2 . THR B 9  ? 0.71011 0.53207 0.55906 -0.02934 0.04001  -0.00331 6  THR B CG2 
694  N N   . GLU B 10 ? 0.54367 0.42727 0.36192 0.01337  0.02600  -0.01663 7  GLU B N   
695  C CA  . GLU B 10 ? 0.59665 0.53572 0.41666 0.01762  0.03341  -0.04160 7  GLU B CA  
696  C C   . GLU B 10 ? 0.53588 0.48087 0.37649 0.04615  0.01010  -0.06648 7  GLU B C   
697  O O   . GLU B 10 ? 0.52126 0.50638 0.38412 0.05798  0.01041  -0.09636 7  GLU B O   
698  C CB  . GLU B 10 ? 0.59001 0.53913 0.36034 0.00795  0.04515  -0.02915 7  GLU B CB  
699  C CG  . GLU B 10 ? 0.85010 0.79266 0.59466 -0.02675 0.06705  -0.00142 7  GLU B CG  
700  C CD  . GLU B 10 ? 0.88876 0.83739 0.57576 -0.03860 0.07543  0.01786  7  GLU B CD  
701  O OE1 . GLU B 10 ? 0.94131 0.89563 0.60735 -0.01746 0.06246  0.00850  7  GLU B OE1 
702  O OE2 . GLU B 10 ? 0.91297 0.85865 0.57218 -0.07221 0.09279  0.04384  7  GLU B OE2 
703  N N   . THR B 11 ? 0.50586 0.41186 0.34096 0.05728  -0.01215 -0.05443 8  THR B N   
704  C CA  . THR B 11 ? 0.53507 0.43601 0.38781 0.07653  -0.03879 -0.07289 8  THR B CA  
705  C C   . THR B 11 ? 0.47111 0.37341 0.36570 0.08012  -0.04740 -0.08234 8  THR B C   
706  O O   . THR B 11 ? 0.47238 0.38542 0.38602 0.09539  -0.06176 -0.10723 8  THR B O   
707  C CB  . THR B 11 ? 0.53845 0.40735 0.37860 0.07964  -0.06035 -0.05313 8  THR B CB  
708  O OG1 . THR B 11 ? 0.55074 0.42076 0.34973 0.07807  -0.05755 -0.04515 8  THR B OG1 
709  C CG2 . THR B 11 ? 0.52901 0.38597 0.38597 0.09073  -0.09126 -0.06809 8  THR B CG2 
710  N N   . THR B 12 ? 0.49661 0.38522 0.40273 0.06828  -0.04121 -0.06386 9  THR B N   
711  C CA  . THR B 12 ? 0.47134 0.36453 0.41040 0.06858  -0.04951 -0.07071 9  THR B CA  
712  C C   . THR B 12 ? 0.50869 0.44336 0.46943 0.06843  -0.03844 -0.09344 9  THR B C   
713  O O   . THR B 12 ? 0.62854 0.57490 0.61832 0.07922  -0.05449 -0.10793 9  THR B O   
714  C CB  . THR B 12 ? 0.43334 0.30658 0.37215 0.05617  -0.04249 -0.05081 9  THR B CB  
715  O OG1 . THR B 12 ? 0.50415 0.35465 0.43099 0.06101  -0.05251 -0.03215 9  THR B OG1 
716  C CG2 . THR B 12 ? 0.43814 0.31860 0.40322 0.05414  -0.05246 -0.05686 9  THR B CG2 
717  N N   . GLN B 13 ? 0.50158 0.46321 0.44966 0.05546  -0.01272 -0.09484 10 GLN B N   
718  C CA  . GLN B 13 ? 0.54352 0.56391 0.51742 0.05375  0.00036  -0.11711 10 GLN B CA  
719  C C   . GLN B 13 ? 0.49556 0.54500 0.48234 0.08417  -0.01177 -0.14852 10 GLN B C   
720  O O   . GLN B 13 ? 0.56464 0.64988 0.58966 0.09937  -0.01981 -0.17101 10 GLN B O   
721  C CB  . GLN B 13 ? 0.45941 0.50664 0.41239 0.02663  0.03128  -0.10708 10 GLN B CB  
722  C CG  . GLN B 13 ? 0.55548 0.57559 0.50446 -0.00437 0.04087  -0.08432 10 GLN B CG  
723  C CD  . GLN B 13 ? 0.70167 0.73399 0.62335 -0.03705 0.06670  -0.06782 10 GLN B CD  
724  O OE1 . GLN B 13 ? 0.56899 0.58596 0.45104 -0.03832 0.07327  -0.05371 10 GLN B OE1 
725  N NE2 . GLN B 13 ? 0.51298 0.57296 0.45354 -0.06738 0.07902  -0.06703 10 GLN B NE2 
726  N N   . LEU B 14 ? 0.48618 0.51920 0.44058 0.09576  -0.01596 -0.15263 11 LEU B N   
727  C CA  . LEU B 14 ? 0.51700 0.56184 0.47718 0.12811  -0.03265 -0.18732 11 LEU B CA  
728  C C   . LEU B 14 ? 0.61876 0.61871 0.60272 0.14649  -0.07074 -0.19158 11 LEU B C   
729  O O   . LEU B 14 ? 0.67778 0.68830 0.68491 0.17538  -0.08826 -0.22215 11 LEU B O   
730  C CB  . LEU B 14 ? 0.55000 0.57889 0.46282 0.13259  -0.03312 -0.19051 11 LEU B CB  
731  C CG  . LEU B 14 ? 0.59998 0.69165 0.48990 0.13395  -0.00393 -0.21101 11 LEU B CG  
732  C CD1 . LEU B 14 ? 0.69796 0.76677 0.53267 0.13577  -0.00923 -0.21050 11 LEU B CD1 
733  C CD2 . LEU B 14 ? 0.59337 0.73899 0.51687 0.16652  -0.00446 -0.25755 11 LEU B CD2 
734  N N   . ILE B 15 ? 0.57598 0.52714 0.55376 0.13078  -0.08468 -0.16074 12 ILE B N   
735  C CA  . ILE B 15 ? 0.58647 0.49679 0.58154 0.13925  -0.12029 -0.15653 12 ILE B CA  
736  C C   . ILE B 15 ? 0.66574 0.60070 0.70006 0.14742  -0.12658 -0.16629 12 ILE B C   
737  O O   . ILE B 15 ? 0.65939 0.57780 0.71212 0.17034  -0.15686 -0.18204 12 ILE B O   
738  C CB  . ILE B 15 ? 0.65813 0.53201 0.63954 0.11699  -0.12650 -0.12003 12 ILE B CB  
739  C CG1 . ILE B 15 ? 0.67913 0.52580 0.63084 0.11558  -0.13727 -0.11350 12 ILE B CG1 
740  C CG2 . ILE B 15 ? 0.64526 0.49482 0.64610 0.11425  -0.15381 -0.10723 12 ILE B CG2 
741  C CD1 . ILE B 15 ? 0.55332 0.38128 0.49816 0.09679  -0.14190 -0.07932 12 ILE B CD1 
742  N N   . VAL B 16 ? 0.57128 0.54240 0.61793 0.12885  -0.10193 -0.15718 13 VAL B N   
743  C CA  . VAL B 16 ? 0.61972 0.62002 0.70409 0.13350  -0.11073 -0.16499 13 VAL B CA  
744  C C   . VAL B 16 ? 0.56934 0.63106 0.68471 0.15860  -0.10509 -0.20069 13 VAL B C   
745  O O   . VAL B 16 ? 0.67691 0.75766 0.82855 0.17872  -0.12637 -0.21464 13 VAL B O   
746  C CB  . VAL B 16 ? 0.57677 0.59161 0.66214 0.10229  -0.09065 -0.14572 13 VAL B CB  
747  C CG1 . VAL B 16 ? 0.49733 0.46013 0.55447 0.08561  -0.09507 -0.11655 13 VAL B CG1 
748  C CG2 . VAL B 16 ? 0.46856 0.52388 0.54704 0.08401  -0.05412 -0.14921 13 VAL B CG2 
749  N N   . LYS B 17 ? 0.57415 0.67371 0.67618 0.15956  -0.07728 -0.21594 14 LYS B N   
750  C CA  . LYS B 17 ? 0.59434 0.76765 0.72664 0.18600  -0.06775 -0.25358 14 LYS B CA  
751  C C   . LYS B 17 ? 0.81852 0.96588 0.95610 0.23279  -0.09938 -0.28568 14 LYS B C   
752  O O   . LYS B 17 ? 0.83057 1.03781 1.00097 0.26639  -0.09826 -0.32291 14 LYS B O   
753  C CB  . LYS B 17 ? 0.56960 0.79759 0.67925 0.16902  -0.02634 -0.25831 14 LYS B CB  
754  C CG  . LYS B 17 ? 0.60974 0.87800 0.72551 0.12504  0.00365  -0.23471 14 LYS B CG  
755  C CD  . LYS B 17 ? 0.70949 1.04825 0.80988 0.10772  0.04278  -0.24069 14 LYS B CD  
756  C CE  . LYS B 17 ? 0.74626 1.03819 0.78469 0.10124  0.05081  -0.22713 14 LYS B CE  
757  N NZ  . LYS B 17 ? 0.91609 1.27682 0.93101 0.07908  0.08875  -0.22707 14 LYS B NZ  
758  N N   . HIS B 18 ? 0.84281 0.90396 0.95045 0.23581  -0.12879 -0.27343 15 HIS B N   
759  C CA  . HIS B 18 ? 0.84496 0.86294 0.94804 0.26306  -0.16486 -0.28937 15 HIS B CA  
760  C C   . HIS B 18 ? 0.90867 0.86454 1.02009 0.25838  -0.20691 -0.26543 15 HIS B C   
761  O O   . HIS B 18 ? 1.06651 0.98591 1.17346 0.27322  -0.23906 -0.27344 15 HIS B O   
762  C CB  . HIS B 18 ? 0.86940 0.84379 0.92469 0.25840  -0.16726 -0.28939 15 HIS B CB  
763  C CG  . HIS B 18 ? 1.12645 1.15941 1.16418 0.26803  -0.13416 -0.31762 15 HIS B CG  
764  N ND1 . HIS B 18 ? 1.07997 1.18431 1.11866 0.25551  -0.09020 -0.32174 15 HIS B ND1 
765  C CD2 . HIS B 18 ? 1.13577 1.16943 1.15063 0.28560  -0.13816 -0.34184 15 HIS B CD2 
766  C CE1 . HIS B 18 ? 1.15301 1.30324 1.16792 0.26215  -0.06745 -0.34326 15 HIS B CE1 
767  N NE2 . HIS B 18 ? 1.17720 1.28497 1.17789 0.28282  -0.09599 -0.35781 15 HIS B NE2 
768  N N   . LEU B 19 ? 0.77953 0.72312 0.89936 0.23696  -0.20759 -0.23681 16 LEU B N   
769  C CA  . LEU B 19 ? 0.92554 0.81424 1.04268 0.22371  -0.24323 -0.20813 16 LEU B CA  
770  C C   . LEU B 19 ? 0.90490 0.82664 1.05738 0.22700  -0.24989 -0.20471 16 LEU B C   
771  O O   . LEU B 19 ? 0.94391 0.84503 1.10350 0.23685  -0.27902 -0.20591 16 LEU B O   
772  C CB  . LEU B 19 ? 0.97157 0.81659 1.06033 0.19174  -0.24209 -0.17178 16 LEU B CB  
773  C CG  . LEU B 19 ? 1.04093 0.84995 1.12413 0.16735  -0.26582 -0.13570 16 LEU B CG  
774  C CD1 . LEU B 19 ? 0.96094 0.72158 1.01232 0.14204  -0.27777 -0.10996 16 LEU B CD1 
775  C CD2 . LEU B 19 ? 1.03322 0.87705 1.12688 0.15120  -0.24573 -0.11847 16 LEU B CD2 
776  N N   . ALA B 20 ? 0.71333 0.68575 0.88439 0.21440  -0.22376 -0.19916 17 ALA B N   
777  C CA  . ALA B 20 ? 0.73606 0.74035 0.93435 0.20669  -0.23246 -0.18906 17 ALA B CA  
778  C C   . ALA B 20 ? 0.71669 0.80403 0.96517 0.23262  -0.22540 -0.22232 17 ALA B C   
779  O O   . ALA B 20 ? 0.67418 0.81321 0.93250 0.24329  -0.19656 -0.24901 17 ALA B O   
780  C CB  . ALA B 20 ? 0.77050 0.78599 0.94876 0.16272  -0.20362 -0.16295 17 ALA B CB  
781  N N   . HIS B 21 ? 0.57279 0.67597 0.84521 0.23599  -0.24806 -0.21716 18 HIS B N   
782  C CA  . HIS B 21 ? 0.63555 0.82928 0.95688 0.25084  -0.23830 -0.24240 18 HIS B CA  
783  C C   . HIS B 21 ? 0.55073 0.82195 0.88965 0.21802  -0.19926 -0.24318 18 HIS B C   
784  O O   . HIS B 21 ? 0.55988 0.79564 0.86213 0.17653  -0.18512 -0.21566 18 HIS B O   
785  C CB  . HIS B 21 ? 0.60907 0.79553 0.94287 0.25410  -0.26977 -0.22963 18 HIS B CB  
786  C CG  . HIS B 21 ? 0.75007 0.85113 1.05672 0.27276  -0.30474 -0.22249 18 HIS B CG  
787  N ND1 . HIS B 21 ? 0.79766 0.81014 1.05955 0.25177  -0.32447 -0.19006 18 HIS B ND1 
788  C CD2 . HIS B 21 ? 0.62612 0.72041 0.94513 0.30729  -0.32423 -0.24395 18 HIS B CD2 
789  C CE1 . HIS B 21 ? 0.77335 0.72732 1.02219 0.26849  -0.35521 -0.19084 18 HIS B CE1 
790  N NE2 . HIS B 21 ? 0.67771 0.67531 0.95994 0.30463  -0.35765 -0.22439 18 HIS B NE2 
791  N N   . ASN B 22 ? 0.42046 0.79016 0.80332 0.22843  -0.17660 -0.27164 19 ASN B N   
792  C CA  . ASN B 22 ? 0.44023 0.87395 0.82454 0.18427  -0.13219 -0.26805 19 ASN B CA  
793  C C   . ASN B 22 ? 0.50474 0.87648 0.82822 0.15501  -0.10346 -0.24926 19 ASN B C   
794  O O   . ASN B 22 ? 0.37091 0.72006 0.66693 0.11088  -0.08611 -0.22532 19 ASN B O   
795  C CB  . ASN B 22 ? 0.41044 0.86803 0.80950 0.14700  -0.13858 -0.25041 19 ASN B CB  
796  C CG  . ASN B 22 ? 0.52286 1.02935 0.97661 0.17692  -0.17687 -0.26255 19 ASN B CG  
797  O OD1 . ASN B 22 ? 0.43339 1.03419 0.93544 0.18521  -0.16765 -0.28222 19 ASN B OD1 
798  N ND2 . ASN B 22 ? 0.60318 1.03582 1.03637 0.18802  -0.21687 -0.24397 19 ASN B ND2 
799  N N   . GLY B 23 ? 0.41305 0.75339 0.71443 0.18295  -0.10229 -0.26209 20 GLY B N   
800  C CA  . GLY B 23 ? 0.51465 0.79502 0.75931 0.16123  -0.08258 -0.24376 20 GLY B CA  
801  C C   . GLY B 23 ? 0.50158 0.82279 0.73122 0.11995  -0.03979 -0.23355 20 GLY B C   
802  O O   . GLY B 23 ? 0.50782 0.77245 0.69368 0.09094  -0.02811 -0.20701 20 GLY B O   
803  N N   . GLU B 24 ? 0.39703 0.81798 0.66333 0.11633  -0.01731 -0.25295 21 GLU B N   
804  C CA  . GLU B 24 ? 0.52665 0.98440 0.77731 0.06812  0.02071  -0.23731 21 GLU B CA  
805  C C   . GLU B 24 ? 0.40047 0.82776 0.64761 0.02430  0.01753  -0.21086 21 GLU B C   
806  O O   . GLU B 24 ? 0.50372 0.89777 0.71366 -0.01621 0.03783  -0.18719 21 GLU B O   
807  C CB  . GLU B 24 ? 0.56037 1.14627 0.85483 0.06913  0.04635  -0.26263 21 GLU B CB  
808  C CG  . GLU B 24 ? 0.63910 1.25736 0.89651 0.04043  0.08699  -0.25472 21 GLU B CG  
809  C CD  . GLU B 24 ? 0.66137 1.23868 0.88306 -0.02295 0.10394  -0.21449 21 GLU B CD  
810  O OE1 . GLU B 24 ? 0.65898 1.26526 0.91061 -0.05754 0.10325  -0.20548 21 GLU B OE1 
811  O OE2 . GLU B 24 ? 0.63833 1.15090 0.80092 -0.03742 0.11479  -0.19253 21 GLU B OE2 
812  N N   . GLU B 25 ? 0.46179 0.89427 0.74282 0.03292  -0.01054 -0.21513 22 GLU B N   
813  C CA  . GLU B 25 ? 0.40067 0.79856 0.67110 -0.00604 -0.01683 -0.19500 22 GLU B CA  
814  C C   . GLU B 25 ? 0.37401 0.66201 0.58644 -0.01206 -0.02212 -0.17153 22 GLU B C   
815  O O   . GLU B 25 ? 0.45368 0.70139 0.63548 -0.04836 -0.00975 -0.15443 22 GLU B O   
816  C CB  . GLU B 25 ? 0.39652 0.82720 0.71065 0.00716  -0.04916 -0.20495 22 GLU B CB  
817  C CG  . GLU B 25 ? 0.46290 1.01357 0.84117 0.00010  -0.04418 -0.22416 22 GLU B CG  
818  C CD  . GLU B 25 ? 0.59622 1.17323 1.01211 0.00671  -0.08018 -0.22860 22 GLU B CD  
819  O OE1 . GLU B 25 ? 0.59454 1.09281 0.97737 0.00684  -0.10466 -0.21360 22 GLU B OE1 
820  O OE2 . GLU B 25 ? 0.70331 1.38665 1.18182 0.01170  -0.08430 -0.24658 22 GLU B OE2 
821  N N   . TYR B 26 ? 0.44104 0.68040 0.63912 0.02317  -0.04188 -0.17111 23 TYR B N   
822  C CA  . TYR B 26 ? 0.54829 0.70079 0.69853 0.01844  -0.04588 -0.14913 23 TYR B CA  
823  C C   . TYR B 26 ? 0.41180 0.53620 0.52398 0.00452  -0.01892 -0.13715 23 TYR B C   
824  O O   . TYR B 26 ? 0.45802 0.52632 0.53555 -0.01281 -0.01292 -0.11842 23 TYR B O   
825  C CB  . TYR B 26 ? 0.48038 0.59511 0.62713 0.05245  -0.07482 -0.14851 23 TYR B CB  
826  C CG  . TYR B 26 ? 0.62818 0.74146 0.79343 0.05962  -0.10658 -0.14669 23 TYR B CG  
827  C CD1 . TYR B 26 ? 0.60493 0.68455 0.74659 0.03837  -0.11211 -0.12928 23 TYR B CD1 
828  C CD2 . TYR B 26 ? 0.60919 0.75423 0.81225 0.09008  -0.13268 -0.16301 23 TYR B CD2 
829  C CE1 . TYR B 26 ? 0.61475 0.69597 0.76559 0.04201  -0.14182 -0.12490 23 TYR B CE1 
830  C CE2 . TYR B 26 ? 0.63498 0.77485 0.85060 0.09608  -0.16601 -0.15650 23 TYR B CE2 
831  C CZ  . TYR B 26 ? 0.64780 0.75741 0.83503 0.06942  -0.17008 -0.13576 23 TYR B CZ  
832  O OH  . TYR B 26 ? 0.64178 0.74954 0.83457 0.07287  -0.20408 -0.12689 23 TYR B OH  
833  N N   . SER B 27 ? 0.48119 0.64486 0.59707 0.01458  -0.00376 -0.14859 24 SER B N   
834  C CA  . SER B 27 ? 0.48593 0.62395 0.56002 0.00119  0.01857  -0.13403 24 SER B CA  
835  C C   . SER B 27 ? 0.54661 0.67719 0.60449 -0.04279 0.03925  -0.11599 24 SER B C   
836  O O   . SER B 27 ? 0.49398 0.56366 0.51016 -0.05571 0.04606  -0.09404 24 SER B O   
837  C CB  . SER B 27 ? 0.48333 0.67570 0.56032 0.01838  0.03182  -0.15274 24 SER B CB  
838  O OG  . SER B 27 ? 0.75253 1.02995 0.85753 -0.00083 0.05387  -0.16374 24 SER B OG  
839  N N   . GLU B 28 ? 0.43296 0.62273 0.52431 -0.06656 0.04617  -0.12452 25 GLU B N   
840  C CA  . GLU B 28 ? 0.46581 0.63688 0.54089 -0.11447 0.05964  -0.10702 25 GLU B CA  
841  C C   . GLU B 28 ? 0.57078 0.65947 0.62365 -0.12023 0.04329  -0.09721 25 GLU B C   
842  O O   . GLU B 28 ? 0.51086 0.53836 0.52758 -0.14655 0.05037  -0.07958 25 GLU B O   
843  C CB  . GLU B 28 ? 0.49239 0.75470 0.61368 -0.14284 0.06771  -0.11910 25 GLU B CB  
844  C CG  . GLU B 28 ? 0.58218 0.94136 0.72479 -0.14062 0.09086  -0.13014 25 GLU B CG  
845  C CD  . GLU B 28 ? 0.83898 1.25574 0.98870 -0.19812 0.11499  -0.11771 25 GLU B CD  
846  O OE1 . GLU B 28 ? 0.90421 1.27098 1.03945 -0.24081 0.11008  -0.10032 25 GLU B OE1 
847  O OE2 . GLU B 28 ? 0.74002 1.25298 0.90812 -0.20221 0.13854  -0.12610 25 GLU B OE2 
848  N N   . VAL B 29 ? 0.48539 0.56975 0.55595 -0.09491 0.02053  -0.10853 26 VAL B N   
849  C CA  . VAL B 29 ? 0.49448 0.50931 0.53867 -0.09546 0.00775  -0.10170 26 VAL B CA  
850  C C   . VAL B 29 ? 0.55204 0.50081 0.55589 -0.07794 0.01177  -0.08568 26 VAL B C   
851  O O   . VAL B 29 ? 0.53751 0.42467 0.50966 -0.08659 0.01387  -0.07654 26 VAL B O   
852  C CB  . VAL B 29 ? 0.54219 0.57579 0.60986 -0.07495 -0.01752 -0.11311 26 VAL B CB  
853  C CG1 . VAL B 29 ? 0.57313 0.54488 0.60770 -0.07245 -0.02692 -0.10658 26 VAL B CG1 
854  C CG2 . VAL B 29 ? 0.45253 0.55094 0.56027 -0.09343 -0.02540 -0.12766 26 VAL B CG2 
855  N N   . VAL B 30 ? 0.45412 0.41552 0.45938 -0.05141 0.01083  -0.08428 27 VAL B N   
856  C CA  . VAL B 30 ? 0.51515 0.42595 0.48702 -0.03605 0.01232  -0.06834 27 VAL B CA  
857  C C   . VAL B 30 ? 0.48594 0.35962 0.42465 -0.05782 0.02956  -0.05163 27 VAL B C   
858  O O   . VAL B 30 ? 0.60910 0.42333 0.51964 -0.05333 0.02816  -0.03853 27 VAL B O   
859  C CB  . VAL B 30 ? 0.56365 0.49747 0.54134 -0.01008 0.00615  -0.07244 27 VAL B CB  
860  C CG1 . VAL B 30 ? 0.55857 0.45010 0.50250 0.00008  0.00759  -0.05455 27 VAL B CG1 
861  C CG2 . VAL B 30 ? 0.51049 0.45604 0.51276 0.01116  -0.01758 -0.08267 27 VAL B CG2 
862  N N   . LYS B 31 ? 0.50547 0.41601 0.44718 -0.08142 0.04514  -0.05093 28 LYS B N   
863  C CA  . LYS B 31 ? 0.73327 0.60522 0.63847 -0.10882 0.05912  -0.02885 28 LYS B CA  
864  C C   . LYS B 31 ? 0.64077 0.44851 0.53016 -0.13162 0.05488  -0.02286 28 LYS B C   
865  O O   . LYS B 31 ? 0.80562 0.53948 0.65748 -0.13179 0.05337  -0.00474 28 LYS B O   
866  C CB  . LYS B 31 ? 0.57800 0.51678 0.49148 -0.13723 0.07839  -0.02842 28 LYS B CB  
867  C CG  . LYS B 31 ? 0.69553 0.59658 0.56654 -0.17456 0.09195  0.00099  28 LYS B CG  
868  C CD  . LYS B 31 ? 0.72420 0.71032 0.60258 -0.20397 0.11468  0.00262  28 LYS B CD  
869  C CE  . LYS B 31 ? 0.92424 0.87138 0.75913 -0.25385 0.12617  0.03778  28 LYS B CE  
870  N NZ  . LYS B 31 ? 0.85519 0.74652 0.69163 -0.29074 0.11718  0.04457  28 LYS B NZ  
871  N N   . GLU B 32 ? 0.61633 0.44817 0.53254 -0.14860 0.04981  -0.03975 29 GLU B N   
872  C CA  . GLU B 32 ? 0.69242 0.46030 0.58969 -0.17225 0.04331  -0.04006 29 GLU B CA  
873  C C   . GLU B 32 ? 0.76517 0.46991 0.64170 -0.13834 0.03133  -0.04476 29 GLU B C   
874  O O   . GLU B 32 ? 0.84780 0.47326 0.69095 -0.14297 0.02798  -0.04017 29 GLU B O   
875  C CB  . GLU B 32 ? 0.63501 0.45350 0.56641 -0.19926 0.03773  -0.05906 29 GLU B CB  
876  C CG  . GLU B 32 ? 0.85257 0.60454 0.76110 -0.23101 0.02875  -0.06337 29 GLU B CG  
877  C CD  . GLU B 32 ? 0.90801 0.71763 0.85119 -0.26139 0.01994  -0.08180 29 GLU B CD  
878  O OE1 . GLU B 32 ? 0.86556 0.76601 0.85352 -0.24849 0.01858  -0.09221 29 GLU B OE1 
879  O OE2 . GLU B 32 ? 0.94109 0.70252 0.86645 -0.29719 0.01128  -0.08680 29 GLU B OE2 
880  N N   . ILE B 33 ? 0.68430 0.42379 0.57984 -0.10409 0.02408  -0.05410 30 ILE B N   
881  C CA  . ILE B 33 ? 0.67879 0.37899 0.55854 -0.07411 0.01602  -0.05763 30 ILE B CA  
882  C C   . ILE B 33 ? 0.76561 0.42248 0.62054 -0.05154 0.01966  -0.03918 30 ILE B C   
883  O O   . ILE B 33 ? 0.86764 0.47132 0.70061 -0.03415 0.01687  -0.03981 30 ILE B O   
884  C CB  . ILE B 33 ? 0.74294 0.49650 0.64909 -0.05279 0.00554  -0.06691 30 ILE B CB  
885  C CG1 . ILE B 33 ? 0.63101 0.41518 0.55472 -0.07133 -0.00362 -0.08444 30 ILE B CG1 
886  C CG2 . ILE B 33 ? 0.81027 0.54282 0.70247 -0.02300 0.00145  -0.06407 30 ILE B CG2 
887  C CD1 . ILE B 33 ? 0.72162 0.45692 0.61875 -0.08573 -0.00559 -0.09678 30 ILE B CD1 
888  N N   . SER B 34 ? 0.69711 0.37922 0.55467 -0.04896 0.02468  -0.02463 31 SER B N   
889  C CA  . SER B 34 ? 0.74470 0.39120 0.57801 -0.02926 0.02450  -0.00480 31 SER B CA  
890  C C   . SER B 34 ? 0.87389 0.44261 0.67152 -0.04266 0.02599  0.00890  31 SER B C   
891  O O   . SER B 34 ? 0.99145 0.50851 0.77064 -0.01667 0.01932  0.01555  31 SER B O   
892  C CB  . SER B 34 ? 0.69777 0.38695 0.53347 -0.02947 0.02856  0.00542  31 SER B CB  
893  O OG  . SER B 34 ? 0.87021 0.61139 0.73382 -0.01072 0.02091  -0.00693 31 SER B OG  
894  N N   . GLU B 35 ? 0.95200 0.51175 0.74069 -0.08347 0.03289  0.01404  32 GLU B N   
895  C CA  . GLU B 35 ? 0.82319 0.29622 0.57330 -0.10334 0.02993  0.03121  32 GLU B CA  
896  C C   . GLU B 35 ? 0.93409 0.33942 0.67364 -0.09509 0.01947  0.01235  32 GLU B C   
897  O O   . GLU B 35 ? 1.12717 0.44113 0.83197 -0.09171 0.01052  0.02281  32 GLU B O   
898  C CB  . GLU B 35 ? 0.92893 0.41728 0.67303 -0.15812 0.04000  0.04429  32 GLU B CB  
899  C CG  . GLU B 35 ? 1.00707 0.54141 0.78241 -0.18958 0.04287  0.02139  32 GLU B CG  
900  C CD  . GLU B 35 ? 1.08803 0.65741 0.86469 -0.24611 0.05491  0.03611  32 GLU B CD  
901  O OE1 . GLU B 35 ? 1.13155 0.70750 0.88601 -0.25865 0.06495  0.06294  32 GLU B OE1 
902  O OE2 . GLU B 35 ? 1.15130 0.74851 0.95073 -0.28016 0.05417  0.02166  32 GLU B OE2 
903  N N   . GLU B 36 ? 0.95273 0.39720 0.71747 -0.08986 0.01832  -0.01600 33 GLU B N   
904  C CA  . GLU B 36 ? 1.02657 0.41479 0.77607 -0.07446 0.00941  -0.03906 33 GLU B CA  
905  C C   . GLU B 36 ? 1.06324 0.43972 0.80862 -0.02003 0.00686  -0.04153 33 GLU B C   
906  O O   . GLU B 36 ? 1.11087 0.43104 0.83951 0.00221  -0.00008 -0.04914 33 GLU B O   
907  C CB  . GLU B 36 ? 0.99103 0.43092 0.76293 -0.08787 0.00780  -0.06647 33 GLU B CB  
908  C CG  . GLU B 36 ? 1.19197 0.59831 0.94729 -0.06189 0.00118  -0.09450 33 GLU B CG  
909  C CD  . GLU B 36 ? 1.39676 0.82073 1.15502 -0.09005 -0.00561 -0.12034 33 GLU B CD  
910  O OE1 . GLU B 36 ? 1.51989 0.98044 1.29792 -0.13067 -0.00658 -0.11554 33 GLU B OE1 
911  O OE2 . GLU B 36 ? 1.27468 0.68248 1.01537 -0.07105 -0.01014 -0.14646 33 GLU B OE2 
912  N N   . MET B 37 ? 0.89165 0.34167 0.66369 0.00224  0.01094  -0.03529 34 MET B N   
913  C CA  . MET B 37 ? 0.90271 0.35791 0.67746 0.04865  0.00874  -0.03325 34 MET B CA  
914  C C   . MET B 37 ? 1.02289 0.41898 0.77508 0.06536  0.00311  -0.00996 34 MET B C   
915  O O   . MET B 37 ? 1.10880 0.49565 0.86439 0.10274  -0.00205 -0.01301 34 MET B O   
916  C CB  . MET B 37 ? 0.88014 0.42234 0.68705 0.05871  0.01033  -0.02743 34 MET B CB  
917  C CG  . MET B 37 ? 0.82365 0.41982 0.65049 0.04927  0.01068  -0.04610 34 MET B CG  
918  S SD  . MET B 37 ? 0.77422 0.45156 0.63324 0.05937  0.00576  -0.03527 34 MET B SD  
919  C CE  . MET B 37 ? 0.70113 0.38653 0.56453 0.04094  0.00561  -0.01999 34 MET B CE  
920  N N   . GLU B 38 ? 1.06384 0.44448 0.80237 0.03615  0.00360  0.01425  35 GLU B N   
921  C CA  . GLU B 38 ? 1.22921 0.56008 0.94519 0.04557  -0.00520 0.04092  35 GLU B CA  
922  C C   . GLU B 38 ? 1.22156 0.48616 0.92525 0.04121  -0.01421 0.03537  35 GLU B C   
923  O O   . GLU B 38 ? 1.24581 0.47965 0.94667 0.06900  -0.02525 0.04474  35 GLU B O   
924  C CB  . GLU B 38 ? 1.30309 0.63912 0.99923 0.01090  -0.00036 0.06961  35 GLU B CB  
925  C CG  . GLU B 38 ? 1.49785 0.81097 1.17328 0.02527  -0.01092 0.10135  35 GLU B CG  
926  C CD  . GLU B 38 ? 1.65357 0.97064 1.29764 -0.01497 -0.00380 0.13015  35 GLU B CD  
927  O OE1 . GLU B 38 ? 1.66952 0.94639 1.29120 -0.05470 -0.00214 0.14388  35 GLU B OE1 
928  O OE2 . GLU B 38 ? 1.53872 0.92545 1.19255 -0.00863 0.00032  0.13451  35 GLU B OE2 
929  N N   . LYS B 39 ? 1.14355 0.38535 0.84134 0.00648  -0.01175 0.01936  36 LYS B N   
930  C CA  . LYS B 39 ? 1.30759 0.48173 0.99278 0.00110  -0.02272 0.01087  36 LYS B CA  
931  C C   . LYS B 39 ? 1.30863 0.47963 1.00578 0.04822  -0.02646 -0.01989 36 LYS B C   
932  O O   . LYS B 39 ? 1.27697 0.39227 0.96576 0.06900  -0.03735 -0.02261 36 LYS B O   
933  C CB  . LYS B 39 ? 1.27576 0.43688 0.95460 -0.05241 -0.02090 0.00135  36 LYS B CB  
934  C CG  . LYS B 39 ? 1.41060 0.49345 1.06894 -0.07742 -0.03405 0.00827  36 LYS B CG  
935  C CD  . LYS B 39 ? 1.54392 0.58429 1.20173 -0.05180 -0.04381 -0.02664 36 LYS B CD  
936  C CE  . LYS B 39 ? 1.45015 0.40281 1.08535 -0.07789 -0.05926 -0.02026 36 LYS B CE  
937  N NZ  . LYS B 39 ? 1.50964 0.41576 1.14025 -0.05189 -0.06865 -0.05855 36 LYS B NZ  
938  N N   . LYS B 40 ? 1.16710 0.39818 0.88200 0.06538  -0.01706 -0.04312 37 LYS B N   
939  C CA  . LYS B 40 ? 1.06237 0.30745 0.78680 0.10955  -0.01604 -0.07154 37 LYS B CA  
940  C C   . LYS B 40 ? 1.10696 0.37627 0.84681 0.15665  -0.01766 -0.05915 37 LYS B C   
941  O O   . LYS B 40 ? 1.18256 0.47510 0.93350 0.19574  -0.01444 -0.08148 37 LYS B O   
942  C CB  . LYS B 40 ? 1.14456 0.45133 0.87834 0.10848  -0.00545 -0.09581 37 LYS B CB  
943  C CG  . LYS B 40 ? 1.31507 0.59996 1.03500 0.08736  -0.00722 -0.12762 37 LYS B CG  
944  C CD  . LYS B 40 ? 1.34443 0.60265 1.05631 0.03149  -0.01244 -0.11839 37 LYS B CD  
945  C CE  . LYS B 40 ? 1.43419 0.68251 1.13607 0.00900  -0.01727 -0.15066 37 LYS B CE  
946  N NZ  . LYS B 40 ? 1.49163 0.73421 1.19417 -0.04838 -0.02253 -0.14183 37 LYS B NZ  
947  N N   . GLY B 41 ? 1.07078 0.34194 0.81141 0.15311  -0.02243 -0.02520 38 GLY B N   
948  C CA  . GLY B 41 ? 1.13498 0.43363 0.89268 0.19443  -0.02767 -0.01192 38 GLY B CA  
949  C C   . GLY B 41 ? 1.11744 0.50363 0.90257 0.21882  -0.01885 -0.01829 38 GLY B C   
950  O O   . GLY B 41 ? 1.11467 0.53524 0.92058 0.25704  -0.02242 -0.01569 38 GLY B O   
951  N N   . LEU B 42 ? 1.02724 0.45193 0.81448 0.19699  -0.00876 -0.02540 39 LEU B N   
952  C CA  . LEU B 42 ? 0.96531 0.46934 0.77643 0.21632  -0.00217 -0.02804 39 LEU B CA  
953  C C   . LEU B 42 ? 0.90189 0.44199 0.72778 0.22327  -0.01000 0.00220  39 LEU B C   
954  O O   . LEU B 42 ? 0.97414 0.48620 0.78506 0.20063  -0.01608 0.02408  39 LEU B O   
955  C CB  . LEU B 42 ? 1.00855 0.53955 0.81802 0.18702  0.00621  -0.03904 39 LEU B CB  
956  C CG  . LEU B 42 ? 0.99963 0.51248 0.79420 0.18047  0.01245  -0.07181 39 LEU B CG  
957  C CD1 . LEU B 42 ? 0.92574 0.49548 0.73331 0.14427  0.01585  -0.07529 39 LEU B CD1 
958  C CD2 . LEU B 42 ? 1.10557 0.64599 0.90542 0.22366  0.01852  -0.09423 39 LEU B CD2 
959  N N   . SER B 43 ? 0.93835 0.54714 0.79258 0.25325  -0.00992 0.00311  40 SER B N   
960  C CA  . SER B 43 ? 0.99999 0.65043 0.87178 0.26033  -0.02125 0.02966  40 SER B CA  
961  C C   . SER B 43 ? 0.89627 0.57494 0.76830 0.22482  -0.02283 0.04241  40 SER B C   
962  O O   . SER B 43 ? 0.87115 0.55688 0.74179 0.19546  -0.01455 0.03007  40 SER B O   
963  C CB  . SER B 43 ? 0.92448 0.65483 0.83367 0.29646  -0.02131 0.02685  40 SER B CB  
964  O OG  . SER B 43 ? 0.70148 0.49996 0.62939 0.28357  -0.01033 0.01619  40 SER B OG  
965  N N   . LYS B 44 ? 0.89492 0.59651 0.77168 0.22532  -0.03591 0.06502  41 LYS B N   
966  C CA  . LYS B 44 ? 0.72322 0.45589 0.60174 0.19238  -0.03987 0.07192  41 LYS B CA  
967  C C   . LYS B 44 ? 0.74038 0.54052 0.65063 0.18149  -0.03863 0.06263  41 LYS B C   
968  O O   . LYS B 44 ? 0.68240 0.49040 0.59238 0.15391  -0.03849 0.05680  41 LYS B O   
969  C CB  . LYS B 44 ? 0.86528 0.60777 0.73695 0.19756  -0.05692 0.09487  41 LYS B CB  
970  C CG  . LYS B 44 ? 0.72845 0.49852 0.59689 0.16873  -0.06345 0.09654  41 LYS B CG  
971  C CD  . LYS B 44 ? 0.82648 0.58881 0.66972 0.16968  -0.07870 0.11626  41 LYS B CD  
972  C CE  . LYS B 44 ? 0.83898 0.64181 0.70443 0.19509  -0.09802 0.13137  41 LYS B CE  
973  N NZ  . LYS B 44 ? 0.77822 0.64893 0.68035 0.18512  -0.10775 0.12596  41 LYS B NZ  
974  N N   . GLU B 45 ? 0.68057 0.53208 0.61851 0.20309  -0.03855 0.06215  42 GLU B N   
975  C CA  . GLU B 45 ? 0.68046 0.59659 0.64423 0.18695  -0.03775 0.05925  42 GLU B CA  
976  C C   . GLU B 45 ? 0.62423 0.52440 0.57719 0.17202  -0.02425 0.04029  42 GLU B C   
977  O O   . GLU B 45 ? 0.72350 0.64383 0.68186 0.14521  -0.02883 0.04068  42 GLU B O   
978  C CB  . GLU B 45 ? 0.66843 0.65683 0.66500 0.21104  -0.03705 0.06436  42 GLU B CB  
979  C CG  . GLU B 45 ? 0.78443 0.81131 0.80130 0.21820  -0.05608 0.08560  42 GLU B CG  
980  C CD  . GLU B 45 ? 0.76380 0.74321 0.76479 0.24955  -0.06266 0.09164  42 GLU B CD  
981  O OE1 . GLU B 45 ? 0.86452 0.80779 0.85618 0.28050  -0.05193 0.07953  42 GLU B OE1 
982  O OE2 . GLU B 45 ? 0.76718 0.74024 0.76069 0.24289  -0.08102 0.10849  42 GLU B OE2 
983  N N   . GLN B 46 ? 0.70737 0.56618 0.64281 0.18918  -0.01137 0.02335  43 GLN B N   
984  C CA  . GLN B 46 ? 0.61440 0.45668 0.53572 0.17315  -0.00145 0.00366  43 GLN B CA  
985  C C   . GLN B 46 ? 0.65337 0.45939 0.56185 0.14156  -0.00590 0.00347  43 GLN B C   
986  O O   . GLN B 46 ? 0.65738 0.47714 0.56701 0.12076  -0.00600 -0.00492 43 GLN B O   
987  C CB  . GLN B 46 ? 0.74637 0.54219 0.64734 0.19788  0.00949  -0.01797 43 GLN B CB  
988  C CG  . GLN B 46 ? 0.72435 0.56763 0.64031 0.23562  0.01733  -0.02689 43 GLN B CG  
989  C CD  . GLN B 46 ? 0.86934 0.65330 0.76112 0.26653  0.02488  -0.05431 43 GLN B CD  
990  O OE1 . GLN B 46 ? 1.05201 0.76003 0.92704 0.28135  0.01730  -0.05196 43 GLN B OE1 
991  N NE2 . GLN B 46 ? 0.95632 0.76970 0.84114 0.27531  0.03792  -0.08059 43 GLN B NE2 
992  N N   . VAL B 47 ? 0.72231 0.48869 0.61858 0.13834  -0.00989 0.01310  44 VAL B N   
993  C CA  . VAL B 47 ? 0.61314 0.36369 0.50198 0.11029  -0.01125 0.01174  44 VAL B CA  
994  C C   . VAL B 47 ? 0.63323 0.43042 0.54232 0.09728  -0.02240 0.01513  44 VAL B C   
995  O O   . VAL B 47 ? 0.60303 0.40781 0.51757 0.08002  -0.02429 0.00516  44 VAL B O   
996  C CB  . VAL B 47 ? 0.65635 0.36788 0.52427 0.10817  -0.01171 0.02463  44 VAL B CB  
997  C CG1 . VAL B 47 ? 0.60653 0.32628 0.47195 0.08184  -0.01064 0.02197  44 VAL B CG1 
998  C CG2 . VAL B 47 ? 0.71758 0.36453 0.56041 0.11371  -0.00513 0.02276  44 VAL B CG2 
999  N N   . ILE B 48 ? 0.64751 0.47387 0.56854 0.10561  -0.03357 0.02929  45 ILE B N   
1000 C CA  . ILE B 48 ? 0.56611 0.42358 0.50291 0.09182  -0.04967 0.03321  45 ILE B CA  
1001 C C   . ILE B 48 ? 0.56082 0.44323 0.50963 0.08164  -0.05150 0.02965  45 ILE B C   
1002 O O   . ILE B 48 ? 0.59476 0.47681 0.54801 0.06677  -0.06245 0.02534  45 ILE B O   
1003 C CB  . ILE B 48 ? 0.62874 0.51318 0.57580 0.09828  -0.06395 0.04985  45 ILE B CB  
1004 C CG1 . ILE B 48 ? 0.67814 0.53776 0.60589 0.10509  -0.06643 0.05445  45 ILE B CG1 
1005 C CG2 . ILE B 48 ? 0.58589 0.49324 0.54757 0.07995  -0.08490 0.05464  45 ILE B CG2 
1006 C CD1 . ILE B 48 ? 0.66480 0.55185 0.60048 0.11202  -0.08337 0.07049  45 ILE B CD1 
1007 N N   . LEU B 49 ? 0.54690 0.45319 0.49919 0.09166  -0.04168 0.03103  46 LEU B N   
1008 C CA  . LEU B 49 ? 0.67183 0.60914 0.62804 0.07961  -0.04205 0.03042  46 LEU B CA  
1009 C C   . LEU B 49 ? 0.51394 0.42401 0.45678 0.06864  -0.03921 0.01385  46 LEU B C   
1010 O O   . LEU B 49 ? 0.51611 0.43827 0.46184 0.05167  -0.05190 0.01708  46 LEU B O   
1011 C CB  . LEU B 49 ? 0.47625 0.45200 0.43468 0.09657  -0.02672 0.02910  46 LEU B CB  
1012 C CG  . LEU B 49 ? 0.47645 0.51371 0.45888 0.09922  -0.03171 0.04897  46 LEU B CG  
1013 C CD1 . LEU B 49 ? 0.60715 0.68780 0.59425 0.12565  -0.01172 0.04015  46 LEU B CD1 
1014 C CD2 . LEU B 49 ? 0.44787 0.51983 0.43911 0.06667  -0.04821 0.06788  46 LEU B CD2 
1015 N N   . LEU B 50 ? 0.55433 0.42624 0.48249 0.07618  -0.02597 -0.00200 47 LEU B N   
1016 C CA  . LEU B 50 ? 0.64045 0.49328 0.55935 0.06190  -0.02471 -0.01813 47 LEU B CA  
1017 C C   . LEU B 50 ? 0.56136 0.41040 0.49238 0.04838  -0.03683 -0.01798 47 LEU B C   
1018 O O   . LEU B 50 ? 0.58987 0.44768 0.52589 0.03607  -0.04533 -0.02541 47 LEU B O   
1019 C CB  . LEU B 50 ? 0.55543 0.36387 0.45462 0.06779  -0.01019 -0.03369 47 LEU B CB  
1020 C CG  . LEU B 50 ? 0.72311 0.52891 0.60427 0.07717  -0.00082 -0.05029 47 LEU B CG  
1021 C CD1 . LEU B 50 ? 0.81209 0.63081 0.68626 0.05648  -0.00652 -0.06284 47 LEU B CD1 
1022 C CD2 . LEU B 50 ? 0.78104 0.63274 0.66933 0.09688  0.00332  -0.04217 47 LEU B CD2 
1023 N N   . LEU B 51 ? 0.59566 0.43611 0.53098 0.05308  -0.03879 -0.01144 48 LEU B N   
1024 C CA  . LEU B 51 ? 0.58903 0.43349 0.53566 0.04629  -0.04879 -0.01680 48 LEU B CA  
1025 C C   . LEU B 51 ? 0.68711 0.54904 0.64836 0.04446  -0.07222 -0.01063 48 LEU B C   
1026 O O   . LEU B 51 ? 0.66023 0.52562 0.63369 0.04263  -0.08477 -0.02020 48 LEU B O   
1027 C CB  . LEU B 51 ? 0.59236 0.42523 0.53121 0.05179  -0.04365 -0.01375 48 LEU B CB  
1028 C CG  . LEU B 51 ? 0.59152 0.40015 0.51296 0.04620  -0.02465 -0.01643 48 LEU B CG  
1029 C CD1 . LEU B 51 ? 0.60444 0.40723 0.51169 0.04909  -0.02170 -0.00883 48 LEU B CD1 
1030 C CD2 . LEU B 51 ? 0.57516 0.39168 0.50476 0.02916  -0.01883 -0.03166 48 LEU B CD2 
1031 N N   . ILE B 52 ? 0.66236 0.53612 0.62392 0.04458  -0.08023 0.00599  49 ILE B N   
1032 C CA  . ILE B 52 ? 0.69624 0.57834 0.66682 0.03491  -0.10560 0.01725  49 ILE B CA  
1033 C C   . ILE B 52 ? 0.65499 0.54805 0.62239 0.02487  -0.10911 0.01757  49 ILE B C   
1034 O O   . ILE B 52 ? 0.58580 0.47281 0.55950 0.01904  -0.13198 0.01949  49 ILE B O   
1035 C CB  . ILE B 52 ? 0.58035 0.47981 0.55356 0.02979  -0.11381 0.03890  49 ILE B CB  
1036 C CG1 . ILE B 52 ? 0.70807 0.59670 0.68197 0.03850  -0.11652 0.03808  49 ILE B CG1 
1037 C CG2 . ILE B 52 ? 0.54604 0.44702 0.52384 0.01141  -0.14233 0.05609  49 ILE B CG2 
1038 C CD1 . ILE B 52 ? 0.75448 0.61538 0.72752 0.04317  -0.12971 0.02181  49 ILE B CD1 
1039 N N   . HIS B 53 ? 0.58765 0.49452 0.54238 0.02493  -0.08911 0.01450  50 HIS B N   
1040 C CA  . HIS B 53 ? 0.72542 0.64167 0.66963 0.01556  -0.09034 0.00859  50 HIS B CA  
1041 C C   . HIS B 53 ? 0.68886 0.59081 0.64203 0.01455  -0.09664 -0.00907 50 HIS B C   
1042 O O   . HIS B 53 ? 0.72249 0.63286 0.67661 0.00630  -0.11353 -0.00901 50 HIS B O   
1043 C CB  . HIS B 53 ? 0.73075 0.65637 0.65569 0.02097  -0.06585 -0.00165 50 HIS B CB  
1044 C CG  . HIS B 53 ? 0.76868 0.69310 0.67704 0.01262  -0.06421 -0.01822 50 HIS B CG  
1045 N ND1 . HIS B 53 ? 0.78894 0.68642 0.68892 0.01495  -0.05088 -0.04127 50 HIS B ND1 
1046 C CD2 . HIS B 53 ? 0.85711 0.80256 0.75248 -0.00127 -0.07713 -0.01373 50 HIS B CD2 
1047 C CE1 . HIS B 53 ? 0.83545 0.73925 0.72022 0.00294  -0.05601 -0.05343 50 HIS B CE1 
1048 N NE2 . HIS B 53 ? 0.92596 0.86067 0.80653 -0.00544 -0.07164 -0.03708 50 HIS B NE2 
1049 N N   . PHE B 54 ? 0.68385 0.57073 0.64420 0.02166  -0.08396 -0.02240 51 PHE B N   
1050 C CA  . PHE B 54 ? 0.70221 0.59225 0.67905 0.01968  -0.08844 -0.03820 51 PHE B CA  
1051 C C   . PHE B 54 ? 0.73614 0.63157 0.73323 0.02713  -0.11521 -0.03552 51 PHE B C   
1052 O O   . PHE B 54 ? 0.67816 0.58732 0.69111 0.02737  -0.13109 -0.04354 51 PHE B O   
1053 C CB  . PHE B 54 ? 0.64251 0.52187 0.61906 0.02144  -0.06770 -0.04770 51 PHE B CB  
1054 C CG  . PHE B 54 ? 0.52867 0.42869 0.52699 0.01845  -0.06844 -0.06313 51 PHE B CG  
1055 C CD1 . PHE B 54 ? 0.59522 0.50773 0.61038 0.03202  -0.07791 -0.06813 51 PHE B CD1 
1056 C CD2 . PHE B 54 ? 0.60915 0.52078 0.61191 0.00200  -0.05992 -0.07506 51 PHE B CD2 
1057 C CE1 . PHE B 54 ? 0.71965 0.66597 0.75898 0.03371  -0.07576 -0.08592 51 PHE B CE1 
1058 C CE2 . PHE B 54 ? 0.60706 0.55508 0.63685 -0.00247 -0.05901 -0.08871 51 PHE B CE2 
1059 C CZ  . PHE B 54 ? 0.63025 0.60068 0.67993 0.01561  -0.06517 -0.09472 51 PHE B CZ  
1060 N N   . LEU B 55 ? 0.65208 0.53418 0.64903 0.03480  -0.12371 -0.02566 52 LEU B N   
1061 C CA  . LEU B 55 ? 0.74731 0.61916 0.75882 0.04425  -0.15318 -0.02638 52 LEU B CA  
1062 C C   . LEU B 55 ? 0.78258 0.64970 0.79306 0.03609  -0.18184 -0.01008 52 LEU B C   
1063 O O   . LEU B 55 ? 0.92395 0.78140 0.94955 0.04650  -0.20952 -0.01520 52 LEU B O   
1064 C CB  . LEU B 55 ? 0.74219 0.59420 0.74737 0.04886  -0.15965 -0.01926 52 LEU B CB  
1065 C CG  . LEU B 55 ? 0.70080 0.55452 0.70274 0.05923  -0.14006 -0.03460 52 LEU B CG  
1066 C CD1 . LEU B 55 ? 0.74574 0.57959 0.73872 0.06237  -0.15459 -0.02837 52 LEU B CD1 
1067 C CD2 . LEU B 55 ? 0.71010 0.57966 0.72852 0.07250  -0.13732 -0.06098 52 LEU B CD2 
1068 N N   . LEU B 56 ? 0.77959 0.65533 0.77082 0.01915  -0.17648 0.00963  53 LEU B N   
1069 C CA  . LEU B 56 ? 0.86045 0.73710 0.84232 0.00590  -0.20174 0.02930  53 LEU B CA  
1070 C C   . LEU B 56 ? 0.98016 0.87235 0.96735 0.00775  -0.20673 0.01566  53 LEU B C   
1071 O O   . LEU B 56 ? 1.02337 0.90773 1.01555 0.00881  -0.23942 0.02420  53 LEU B O   
1072 C CB  . LEU B 56 ? 0.93225 0.83012 0.88987 -0.01331 -0.18872 0.05117  53 LEU B CB  
1073 C CG  . LEU B 56 ? 0.90717 0.80402 0.86494 -0.01966 -0.18761 0.06918  53 LEU B CG  
1074 C CD1 . LEU B 56 ? 0.87884 0.81773 0.82128 -0.02996 -0.16202 0.07995  53 LEU B CD1 
1075 C CD2 . LEU B 56 ? 0.89637 0.76582 0.85441 -0.03403 -0.22729 0.09470  53 LEU B CD2 
1076 N N   . LEU B 57 ? 0.84525 0.75659 0.83108 0.00701  -0.17836 -0.00438 54 LEU B N   
1077 C CA  . LEU B 57 ? 0.91895 0.85051 0.91122 0.00346  -0.18398 -0.01850 54 LEU B CA  
1078 C C   . LEU B 57 ? 0.80831 0.74699 0.83744 0.02071  -0.20483 -0.03193 54 LEU B C   
1079 O O   . LEU B 57 ? 0.92074 0.87363 0.96060 0.02240  -0.23109 -0.03134 54 LEU B O   
1080 C CB  . LEU B 57 ? 0.77330 0.71371 0.75715 -0.00426 -0.15164 -0.03854 54 LEU B CB  
1081 C CG  . LEU B 57 ? 0.83711 0.78072 0.78482 -0.01843 -0.13914 -0.03800 54 LEU B CG  
1082 C CD1 . LEU B 57 ? 0.88601 0.82933 0.81141 -0.01971 -0.13803 -0.01509 54 LEU B CD1 
1083 C CD2 . LEU B 57 ? 0.78396 0.71388 0.72234 -0.02107 -0.10940 -0.05848 54 LEU B CD2 
1084 N N   . SER B 58 ? 0.83063 0.76454 0.87898 0.03614  -0.19434 -0.04525 55 SER B N   
1085 C CA  . SER B 58 ? 0.91748 0.86932 1.00281 0.05814  -0.20883 -0.06474 55 SER B CA  
1086 C C   . SER B 58 ? 1.04127 0.96342 1.13461 0.07737  -0.25017 -0.05548 55 SER B C   
1087 O O   . SER B 58 ? 1.04441 0.98243 1.17024 0.10161  -0.27077 -0.07236 55 SER B O   
1088 C CB  . SER B 58 ? 0.96510 0.92640 1.06066 0.06746  -0.18149 -0.08359 55 SER B CB  
1089 O OG  . SER B 58 ? 1.03891 0.96283 1.11471 0.07171  -0.18069 -0.07328 55 SER B OG  
1090 N N   . LEU B 59 ? 1.09332 0.97351 1.15942 0.06707  -0.26459 -0.02908 56 LEU B N   
1091 C CA  . LEU B 59 ? 0.98614 0.82171 1.05222 0.07727  -0.29648 -0.02001 56 LEU B CA  
1092 C C   . LEU B 59 ? 1.00393 0.81953 1.04673 0.05476  -0.31410 0.01145  56 LEU B C   
1093 O O   . LEU B 59 ? 1.02487 0.84019 1.07706 0.06261  -0.33338 0.01104  56 LEU B O   
1094 C CB  . LEU B 59 ? 0.98793 0.78911 1.04106 0.07525  -0.29140 -0.01787 56 LEU B CB  
1095 C CG  . LEU B 59 ? 1.06163 0.81569 1.11435 0.08297  -0.31658 -0.02371 56 LEU B CG  
1096 C CD1 . LEU B 59 ? 1.05386 0.82127 1.13510 0.11654  -0.32682 -0.05584 56 LEU B CD1 
1097 C CD2 . LEU B 59 ? 1.11651 0.84673 1.15799 0.08105  -0.31333 -0.02951 56 LEU B CD2 
1098 N N   . VAL B 60 ? 1.03135 0.83663 1.04497 0.02718  -0.30789 0.03945  57 VAL B N   
1099 C CA  . VAL B 60 ? 1.09868 0.89037 1.08878 0.00236  -0.32377 0.07152  57 VAL B CA  
1100 C C   . VAL B 60 ? 1.04516 0.87184 1.02731 -0.00178 -0.32593 0.07515  57 VAL B C   
1101 O O   . VAL B 60 ? 1.16302 0.97773 1.13578 -0.00899 -0.34727 0.09207  57 VAL B O   
1102 C CB  . VAL B 60 ? 0.97610 0.77088 0.94135 -0.02763 -0.31225 0.09918  57 VAL B CB  
1103 C CG1 . VAL B 60 ? 0.94195 0.78109 0.89764 -0.02986 -0.28396 0.09420  57 VAL B CG1 
1104 C CG2 . VAL B 60 ? 1.06254 0.85480 1.00281 -0.05749 -0.32686 0.13382  57 VAL B CG2 
1105 N N   . LYS B 61 ? 1.08668 0.95455 1.07056 0.00077  -0.30739 0.05782  58 LYS B N   
1106 C CA  . LYS B 61 ? 1.05335 0.95598 1.03090 -0.00455 -0.31180 0.05290  58 LYS B CA  
1107 C C   . LYS B 61 ? 0.93641 0.85576 0.95464 0.02020  -0.32291 0.02666  58 LYS B C   
1108 O O   . LYS B 61 ? 0.88403 0.82776 0.90250 0.01734  -0.33568 0.02708  58 LYS B O   
1109 C CB  . LYS B 61 ? 0.96497 0.89970 0.92102 -0.01975 -0.28263 0.04071  58 LYS B CB  
1110 C CG  . LYS B 61 ? 0.95571 0.89614 0.86808 -0.04386 -0.26962 0.06551  58 LYS B CG  
1111 C CD  . LYS B 61 ? 0.94650 0.89137 0.83018 -0.06149 -0.29551 0.09465  58 LYS B CD  
1112 C CE  . LYS B 61 ? 0.92749 0.89480 0.76663 -0.08816 -0.28088 0.11944  58 LYS B CE  
1113 N NZ  . LYS B 61 ? 0.89901 0.87365 0.71123 -0.10674 -0.29520 0.14593  58 LYS B NZ  
1114 N N   . GLY B 62 ? 0.90162 0.81614 0.95410 0.04436  -0.31815 0.00359  59 GLY B N   
1115 C CA  . GLY B 62 ? 0.91698 0.86112 1.01303 0.06999  -0.32628 -0.02274 59 GLY B CA  
1116 C C   . GLY B 62 ? 0.75840 0.76346 0.87217 0.06091  -0.31664 -0.04274 59 GLY B C   
1117 O O   . GLY B 62 ? 0.78070 0.82342 0.92551 0.07236  -0.32813 -0.05458 59 GLY B O   
1118 N N   . LEU B 63 ? 0.77169 0.78332 0.86209 0.03691  -0.28407 -0.04689 60 LEU B N   
1119 C CA  . LEU B 63 ? 0.73808 0.79164 0.83391 0.01840  -0.26475 -0.06559 60 LEU B CA  
1120 C C   . LEU B 63 ? 0.66228 0.75207 0.80082 0.02696  -0.24210 -0.09266 60 LEU B C   
1121 O O   . LEU B 63 ? 0.70562 0.78090 0.85096 0.04039  -0.22457 -0.09783 60 LEU B O   
1122 C CB  . LEU B 63 ? 0.63464 0.66830 0.68307 -0.00803 -0.23514 -0.06137 60 LEU B CB  
1123 C CG  . LEU B 63 ? 0.77225 0.78507 0.77476 -0.01932 -0.24969 -0.03529 60 LEU B CG  
1124 C CD1 . LEU B 63 ? 0.65125 0.65308 0.61231 -0.03650 -0.21629 -0.03888 60 LEU B CD1 
1125 C CD2 . LEU B 63 ? 0.76212 0.79882 0.75949 -0.02637 -0.28478 -0.02868 60 LEU B CD2 
1126 N N   . SER B 64 ? 0.51699 0.65997 0.68253 0.01540  -0.24297 -0.10904 61 SER B N   
1127 C CA  . SER B 64 ? 0.56013 0.75412 0.76859 0.01603  -0.22096 -0.13199 61 SER B CA  
1128 C C   . SER B 64 ? 0.66058 0.82735 0.84203 -0.00543 -0.17872 -0.13388 61 SER B C   
1129 O O   . SER B 64 ? 0.47992 0.59641 0.61453 -0.02143 -0.16779 -0.12266 61 SER B O   
1130 C CB  . SER B 64 ? 0.56837 0.82976 0.81013 -0.00170 -0.23209 -0.14532 61 SER B CB  
1131 O OG  . SER B 64 ? 0.51913 0.76125 0.72231 -0.04076 -0.22141 -0.14378 61 SER B OG  
1132 N N   . PRO B 65 ? 0.56627 0.76815 0.77563 -0.00410 -0.15515 -0.14760 62 PRO B N   
1133 C CA  . PRO B 65 ? 0.59614 0.76863 0.77658 -0.02709 -0.11887 -0.14486 62 PRO B CA  
1134 C C   . PRO B 65 ? 0.51442 0.66821 0.66900 -0.06632 -0.10971 -0.14418 62 PRO B C   
1135 O O   . PRO B 65 ? 0.51623 0.61069 0.62813 -0.07761 -0.09205 -0.13611 62 PRO B O   
1136 C CB  . PRO B 65 ? 0.59034 0.82444 0.80927 -0.02348 -0.09969 -0.15927 62 PRO B CB  
1137 C CG  . PRO B 65 ? 0.54236 0.81216 0.79971 0.01864  -0.12381 -0.17065 62 PRO B CG  
1138 C CD  . PRO B 65 ? 0.49421 0.76041 0.75771 0.02354  -0.16067 -0.16511 62 PRO B CD  
1139 N N   . GLU B 66 ? 0.44253 0.64396 0.62201 -0.08576 -0.12416 -0.15434 63 GLU B N   
1140 C CA  . GLU B 66 ? 0.53597 0.71198 0.68649 -0.12481 -0.12075 -0.15797 63 GLU B CA  
1141 C C   . GLU B 66 ? 0.58983 0.70584 0.68880 -0.11937 -0.13249 -0.15164 63 GLU B C   
1142 O O   . GLU B 66 ? 0.59881 0.65695 0.65337 -0.13479 -0.11791 -0.15303 63 GLU B O   
1143 C CB  . GLU B 66 ? 0.45720 0.70644 0.64916 -0.14907 -0.13792 -0.17112 63 GLU B CB  
1144 C CG  . GLU B 66 ? 0.71401 0.93364 0.87492 -0.19427 -0.13854 -0.17875 63 GLU B CG  
1145 C CD  . GLU B 66 ? 0.79692 0.97173 0.93580 -0.22500 -0.10846 -0.17645 63 GLU B CD  
1146 O OE1 . GLU B 66 ? 0.68116 0.88892 0.84747 -0.22457 -0.08791 -0.17060 63 GLU B OE1 
1147 O OE2 . GLU B 66 ? 0.93558 1.03941 1.02611 -0.24851 -0.10668 -0.18076 63 GLU B OE2 
1148 N N   . THR B 67 ? 0.59478 0.72487 0.69763 -0.09669 -0.15960 -0.14447 64 THR B N   
1149 C CA  . THR B 67 ? 0.60616 0.69283 0.65859 -0.09330 -0.16863 -0.13494 64 THR B CA  
1150 C C   . THR B 67 ? 0.56605 0.59852 0.58634 -0.07977 -0.14509 -0.12394 64 THR B C   
1151 O O   . THR B 67 ? 0.54751 0.54153 0.52328 -0.08650 -0.13394 -0.12553 64 THR B O   
1152 C CB  . THR B 67 ? 0.62003 0.73075 0.68247 -0.07414 -0.20413 -0.12154 64 THR B CB  
1153 O OG1 . THR B 67 ? 0.66915 0.82928 0.75301 -0.08775 -0.23004 -0.13125 64 THR B OG1 
1154 C CG2 . THR B 67 ? 0.67098 0.74348 0.67974 -0.07197 -0.20892 -0.10479 64 THR B CG2 
1155 N N   . THR B 68 ? 0.52109 0.55407 0.56413 -0.05865 -0.13829 -0.11544 65 THR B N   
1156 C CA  . THR B 68 ? 0.56674 0.55631 0.58466 -0.04664 -0.11903 -0.10420 65 THR B CA  
1157 C C   . THR B 68 ? 0.63511 0.59034 0.63082 -0.06162 -0.09109 -0.11209 65 THR B C   
1158 O O   . THR B 68 ? 0.65366 0.56968 0.61559 -0.05608 -0.07895 -0.10757 65 THR B O   
1159 C CB  . THR B 68 ? 0.56983 0.56752 0.61510 -0.02400 -0.12053 -0.09787 65 THR B CB  
1160 O OG1 . THR B 68 ? 0.64388 0.65458 0.70389 -0.00764 -0.15176 -0.08926 65 THR B OG1 
1161 C CG2 . THR B 68 ? 0.59422 0.55278 0.61539 -0.01467 -0.10327 -0.08606 65 THR B CG2 
1162 N N   . LYS B 69 ? 0.55792 0.52881 0.57301 -0.08102 -0.08214 -0.12286 66 LYS B N   
1163 C CA  . LYS B 69 ? 0.61566 0.54213 0.60633 -0.09969 -0.06052 -0.12612 66 LYS B CA  
1164 C C   . LYS B 69 ? 0.64081 0.52362 0.59080 -0.11132 -0.06280 -0.13724 66 LYS B C   
1165 O O   . LYS B 69 ? 0.74062 0.56592 0.65720 -0.10684 -0.04894 -0.13751 66 LYS B O   
1166 C CB  . LYS B 69 ? 0.65074 0.61033 0.66993 -0.12782 -0.05329 -0.13198 66 LYS B CB  
1167 C CG  . LYS B 69 ? 0.67759 0.58587 0.67139 -0.14919 -0.03250 -0.12652 66 LYS B CG  
1168 C CD  . LYS B 69 ? 0.77285 0.72831 0.79672 -0.18243 -0.02343 -0.12641 66 LYS B CD  
1169 C CE  . LYS B 69 ? 0.77413 0.76954 0.82009 -0.21483 -0.03874 -0.14138 66 LYS B CE  
1170 N NZ  . LYS B 69 ? 0.81416 0.87205 0.89604 -0.25180 -0.02835 -0.13975 66 LYS B NZ  
1171 N N   . LEU B 70 ? 0.64991 0.55940 0.60043 -0.12337 -0.08210 -0.14853 67 LEU B N   
1172 C CA  . LEU B 70 ? 0.66900 0.54064 0.57501 -0.13381 -0.08552 -0.16499 67 LEU B CA  
1173 C C   . LEU B 70 ? 0.63816 0.48513 0.50933 -0.10519 -0.07797 -0.16002 67 LEU B C   
1174 O O   . LEU B 70 ? 0.77453 0.57024 0.60897 -0.09958 -0.06525 -0.17214 67 LEU B O   
1175 C CB  . LEU B 70 ? 0.61947 0.53453 0.53121 -0.15203 -0.11114 -0.17623 67 LEU B CB  
1176 C CG  . LEU B 70 ? 0.74319 0.70108 0.69608 -0.18312 -0.12146 -0.18339 67 LEU B CG  
1177 C CD1 . LEU B 70 ? 0.76551 0.78743 0.73965 -0.18561 -0.15217 -0.18530 67 LEU B CD1 
1178 C CD2 . LEU B 70 ? 0.80540 0.71595 0.73353 -0.22023 -0.11677 -0.20177 67 LEU B CD2 
1179 N N   . LEU B 71 ? 0.64272 0.52706 0.52622 -0.08679 -0.08698 -0.14224 68 LEU B N   
1180 C CA  . LEU B 71 ? 0.60688 0.48398 0.46344 -0.06527 -0.07900 -0.13296 68 LEU B CA  
1181 C C   . LEU B 71 ? 0.66728 0.50996 0.52285 -0.04678 -0.05691 -0.12679 68 LEU B C   
1182 O O   . LEU B 71 ? 0.69601 0.52315 0.52463 -0.03056 -0.04436 -0.13069 68 LEU B O   
1183 C CB  . LEU B 71 ? 0.66493 0.58313 0.53692 -0.05716 -0.09699 -0.10922 68 LEU B CB  
1184 C CG  . LEU B 71 ? 0.70325 0.65442 0.56766 -0.07079 -0.12355 -0.10887 68 LEU B CG  
1185 C CD1 . LEU B 71 ? 0.70215 0.67720 0.58201 -0.06211 -0.14514 -0.08018 68 LEU B CD1 
1186 C CD2 . LEU B 71 ? 0.70014 0.64807 0.51226 -0.07759 -0.11847 -0.12319 68 LEU B CD2 
1187 N N   . MET B 72 ? 0.67061 0.50820 0.55506 -0.04702 -0.05246 -0.11752 69 MET B N   
1188 C CA  . MET B 72 ? 0.63796 0.44104 0.51778 -0.03174 -0.03500 -0.10984 69 MET B CA  
1189 C C   . MET B 72 ? 0.73427 0.47917 0.58291 -0.03495 -0.02375 -0.12663 69 MET B C   
1190 O O   . MET B 72 ? 0.82352 0.54041 0.65246 -0.01189 -0.01347 -0.12762 69 MET B O   
1191 C CB  . MET B 72 ? 0.70202 0.51474 0.61125 -0.03572 -0.03305 -0.09865 69 MET B CB  
1192 C CG  . MET B 72 ? 0.54604 0.39793 0.48081 -0.02232 -0.04471 -0.08437 69 MET B CG  
1193 S SD  . MET B 72 ? 0.83732 0.68623 0.75908 0.00081  -0.04322 -0.06728 69 MET B SD  
1194 C CE  . MET B 72 ? 0.71347 0.52213 0.62373 0.01205  -0.02379 -0.06307 69 MET B CE  
1195 N N   . LYS B 73 ? 0.74083 0.46643 0.58624 -0.06325 -0.02802 -0.14055 70 LYS B N   
1196 C CA  . LYS B 73 ? 0.85584 0.51054 0.66716 -0.07082 -0.02333 -0.15788 70 LYS B CA  
1197 C C   . LYS B 73 ? 0.84794 0.48560 0.62299 -0.05099 -0.02308 -0.18012 70 LYS B C   
1198 O O   . LYS B 73 ? 0.94679 0.52310 0.69265 -0.03342 -0.01607 -0.19330 70 LYS B O   
1199 C CB  . LYS B 73 ? 0.76068 0.40665 0.57652 -0.11346 -0.03252 -0.16854 70 LYS B CB  
1200 C CG  . LYS B 73 ? 0.84008 0.50188 0.68624 -0.13607 -0.02715 -0.14955 70 LYS B CG  
1201 C CD  . LYS B 73 ? 0.95548 0.65287 0.82310 -0.17889 -0.03806 -0.15873 70 LYS B CD  
1202 C CE  . LYS B 73 ? 1.02845 0.74445 0.92134 -0.20751 -0.02834 -0.14199 70 LYS B CE  
1203 N NZ  . LYS B 73 ? 1.11735 0.74618 0.97502 -0.23089 -0.02263 -0.13600 70 LYS B NZ  
1204 N N   . GLU B 74 ? 0.77843 0.47057 0.55252 -0.05165 -0.03148 -0.18493 71 GLU B N   
1205 C CA  . GLU B 74 ? 0.89236 0.58206 0.62702 -0.03546 -0.02876 -0.20766 71 GLU B CA  
1206 C C   . GLU B 74 ? 0.87504 0.57581 0.60660 0.00340  -0.01213 -0.19939 71 GLU B C   
1207 O O   . GLU B 74 ? 0.88981 0.55778 0.59142 0.02778  -0.00189 -0.22250 71 GLU B O   
1208 C CB  . GLU B 74 ? 0.87599 0.62618 0.60594 -0.05062 -0.04368 -0.20874 71 GLU B CB  
1209 C CG  . GLU B 74 ? 0.99205 0.73117 0.71231 -0.08510 -0.06178 -0.22912 71 GLU B CG  
1210 C CD  . GLU B 74 ? 1.13641 0.80791 0.80892 -0.08719 -0.05945 -0.26701 71 GLU B CD  
1211 O OE1 . GLU B 74 ? 1.24506 0.90378 0.88238 -0.05752 -0.04662 -0.28419 71 GLU B OE1 
1212 O OE2 . GLU B 74 ? 1.11680 0.74896 0.78751 -0.11858 -0.07114 -0.28095 71 GLU B OE2 
1213 N N   . LEU B 75 ? 0.70635 0.45479 0.47022 0.01070  -0.01088 -0.16857 72 LEU B N   
1214 C CA  . LEU B 75 ? 0.86979 0.63981 0.63770 0.04256  0.00285  -0.15783 72 LEU B CA  
1215 C C   . LEU B 75 ? 0.88931 0.60131 0.65726 0.06524  0.01249  -0.16068 72 LEU B C   
1216 O O   . LEU B 75 ? 0.94343 0.66076 0.70553 0.09861  0.02401  -0.16634 72 LEU B O   
1217 C CB  . LEU B 75 ? 0.66943 0.49453 0.47053 0.03868  -0.00339 -0.12379 72 LEU B CB  
1218 C CG  . LEU B 75 ? 0.95575 0.84414 0.74962 0.03087  -0.00938 -0.11337 72 LEU B CG  
1219 C CD1 . LEU B 75 ? 0.94533 0.84110 0.73065 0.00351  -0.02841 -0.11763 72 LEU B CD1 
1220 C CD2 . LEU B 75 ? 0.96519 0.89343 0.78772 0.03188  -0.01464 -0.07944 72 LEU B CD2 
1221 N N   . ILE B 76 ? 0.85440 0.51575 0.62913 0.04783  0.00723  -0.15522 73 ILE B N   
1222 C CA  . ILE B 76 ? 1.00481 0.59823 0.77022 0.06509  0.01199  -0.15479 73 ILE B CA  
1223 C C   . ILE B 76 ? 0.89508 0.42639 0.62202 0.08170  0.01345  -0.18908 73 ILE B C   
1224 O O   . ILE B 76 ? 1.07181 0.56591 0.78890 0.11843  0.01840  -0.19513 73 ILE B O   
1225 C CB  . ILE B 76 ? 0.83158 0.38959 0.60648 0.03432  0.00655  -0.13852 73 ILE B CB  
1226 C CG1 . ILE B 76 ? 0.83538 0.45053 0.64474 0.02995  0.00643  -0.11007 73 ILE B CG1 
1227 C CG2 . ILE B 76 ? 0.97909 0.45141 0.73263 0.04471  0.00702  -0.13591 73 ILE B CG2 
1228 C CD1 . ILE B 76 ? 0.81281 0.42477 0.63500 -0.00335 0.00385  -0.09935 73 ILE B CD1 
1229 N N   . LYS B 77 ? 0.85854 0.37745 0.56271 0.05770  0.00657  -0.21439 74 LYS B N   
1230 C CA  . LYS B 77 ? 1.01058 0.47796 0.68081 0.07151  0.00585  -0.25056 74 LYS B CA  
1231 C C   . LYS B 77 ? 1.03053 0.54484 0.68736 0.11401  0.01940  -0.27066 74 LYS B C   
1232 O O   . LYS B 77 ? 1.25691 0.74735 0.90580 0.13860  0.02440  -0.29335 74 LYS B O   
1233 C CB  . LYS B 77 ? 1.05343 0.51075 0.70860 0.03005  -0.00736 -0.27049 74 LYS B CB  
1234 C CG  . LYS B 77 ? 1.05240 0.47879 0.72655 -0.01413 -0.01888 -0.25159 74 LYS B CG  
1235 C CD  . LYS B 77 ? 1.18450 0.63417 0.85568 -0.05660 -0.03344 -0.26537 74 LYS B CD  
1236 C CE  . LYS B 77 ? 1.23511 0.68799 0.93537 -0.10016 -0.04064 -0.24197 74 LYS B CE  
1237 N NZ  . LYS B 77 ? 1.26005 0.64644 0.96328 -0.11026 -0.04090 -0.22969 74 LYS B NZ  
1238 N N   . GLU B 78 ? 1.12154 0.72547 0.79314 0.11616  0.02626  -0.25463 75 GLU B N   
1239 C CA  . GLU B 78 ? 1.04832 0.71762 0.71357 0.15196  0.04243  -0.26640 75 GLU B CA  
1240 C C   . GLU B 78 ? 1.06619 0.75433 0.76214 0.19076  0.05293  -0.24823 75 GLU B C   
1241 O O   . GLU B 78 ? 1.12473 0.85783 0.81778 0.22947  0.06799  -0.26480 75 GLU B O   
1242 C CB  . GLU B 78 ? 1.06750 0.83285 0.73905 0.12816  0.04289  -0.24855 75 GLU B CB  
1243 C CG  . GLU B 78 ? 1.09785 0.85786 0.74331 0.08937  0.02774  -0.26078 75 GLU B CG  
1244 C CD  . GLU B 78 ? 1.32850 1.07943 0.91987 0.09958  0.03225  -0.30723 75 GLU B CD  
1245 O OE1 . GLU B 78 ? 1.28899 0.97408 0.85882 0.12680  0.03765  -0.34131 75 GLU B OE1 
1246 O OE2 . GLU B 78 ? 1.35018 1.15744 0.91831 0.08026  0.02833  -0.30927 75 GLU B OE2 
1247 N N   . LEU B 79 ? 1.00509 0.66845 0.73050 0.18158  0.04529  -0.21559 76 LEU B N   
1248 C CA  . LEU B 79 ? 1.05985 0.73319 0.81144 0.21753  0.05020  -0.19841 76 LEU B CA  
1249 C C   . LEU B 79 ? 1.22417 0.81941 0.96450 0.24772  0.04750  -0.21681 76 LEU B C   
1250 O O   . LEU B 79 ? 1.32614 0.95201 1.08386 0.28737  0.05460  -0.22108 76 LEU B O   
1251 C CB  . LEU B 79 ? 0.92443 0.60073 0.70640 0.19407  0.04088  -0.15750 76 LEU B CB  
1252 C CG  . LEU B 79 ? 0.92477 0.68959 0.73522 0.17192  0.04005  -0.13047 76 LEU B CG  
1253 C CD1 . LEU B 79 ? 0.93199 0.68148 0.76290 0.14961  0.02894  -0.10096 76 LEU B CD1 
1254 C CD2 . LEU B 79 ? 0.92130 0.76624 0.75331 0.20023  0.05015  -0.12277 76 LEU B CD2 
1255 N N   . GLU B 80 ? 1.41646 0.92872 1.14218 0.21877  0.03510  -0.21981 77 GLU B N   
1256 C CA  . GLU B 80 ? 1.50769 0.95238 1.22939 0.23429  0.02869  -0.23153 77 GLU B CA  
1257 C C   . GLU B 80 ? 1.60106 1.05424 1.30510 0.25798  0.03706  -0.27337 77 GLU B C   
1258 O O   . GLU B 80 ? 1.69130 1.09839 1.39398 0.28477  0.03382  -0.28751 77 GLU B O   
1259 C CB  . GLU B 80 ? 1.53041 0.89238 1.23932 0.19177  0.01354  -0.22316 77 GLU B CB  
1260 C CG  . GLU B 80 ? 1.57259 0.92972 1.26078 0.15136  0.01027  -0.24382 77 GLU B CG  
1261 C CD  . GLU B 80 ? 1.78369 1.06808 1.46439 0.10882  -0.00469 -0.23620 77 GLU B CD  
1262 O OE1 . GLU B 80 ? 2.05786 1.27915 1.73796 0.11613  -0.01239 -0.22525 77 GLU B OE1 
1263 O OE2 . GLU B 80 ? 1.81767 1.11163 1.49339 0.06696  -0.00995 -0.23954 77 GLU B OE2 
1264 N N   . LYS B 81 ? 1.43771 0.94826 1.12470 0.24874  0.04702  -0.29332 78 LYS B N   
1265 C CA  . LYS B 81 ? 1.36593 0.89957 1.03135 0.26980  0.05842  -0.33305 78 LYS B CA  
1266 C C   . LYS B 81 ? 1.38097 0.98268 1.06814 0.32124  0.07468  -0.33720 78 LYS B C   
1267 O O   . LYS B 81 ? 1.44484 1.05883 1.11735 0.34650  0.08504  -0.37095 78 LYS B O   
1268 C CB  . LYS B 81 ? 1.32891 0.91626 0.96626 0.24130  0.06336  -0.34659 78 LYS B CB  
1269 C CG  . LYS B 81 ? 1.24572 0.82977 0.84575 0.24426  0.06966  -0.39001 78 LYS B CG  
1270 C CD  . LYS B 81 ? 1.16466 0.80256 0.73274 0.21067  0.06995  -0.39679 78 LYS B CD  
1271 C CE  . LYS B 81 ? 1.41162 1.03689 0.93496 0.20757  0.07377  -0.43954 78 LYS B CE  
1272 N NZ  . LYS B 81 ? 1.46588 0.98523 0.97908 0.18929  0.05650  -0.46037 78 LYS B NZ  
1273 N N   . ILE B 82 ? 1.36020 1.01140 1.08280 0.33648  0.07694  -0.30484 79 ILE B N   
1274 C CA  . ILE B 82 ? 1.34336 1.06983 1.09573 0.38258  0.09003  -0.30576 79 ILE B CA  
1275 C C   . ILE B 82 ? 1.32910 1.00084 1.10729 0.40895  0.07644  -0.28950 79 ILE B C   
1276 O O   . ILE B 82 ? 1.38781 0.97392 1.16037 0.38694  0.05886  -0.27080 79 ILE B O   
1277 C CB  . ILE B 82 ? 1.21973 1.06493 0.99657 0.37989  0.10254  -0.28118 79 ILE B CB  
1278 C CG1 . ILE B 82 ? 1.31651 1.15247 1.12404 0.37490  0.09010  -0.23999 79 ILE B CG1 
1279 C CG2 . ILE B 82 ? 1.21982 1.10112 0.96541 0.34215  0.10817  -0.28567 79 ILE B CG2 
1280 C CD1 . ILE B 82 ? 1.20143 1.15396 1.03890 0.37409  0.10036  -0.21411 79 ILE B CD1 
1281 N N   . SER C 4  ? 1.06819 1.05472 1.24010 0.27905  0.02679  0.24337  1  SER C N   
1282 C CA  . SER C 4  ? 1.06818 1.06869 1.21987 0.24203  0.00425  0.26017  1  SER C CA  
1283 C C   . SER C 4  ? 1.10046 1.10797 1.22561 0.20480  0.01623  0.23422  1  SER C C   
1284 O O   . SER C 4  ? 1.09651 1.06306 1.17907 0.17764  0.01190  0.23076  1  SER C O   
1285 C CB  . SER C 4  ? 1.22987 1.30881 1.42333 0.23729  -0.01747 0.28152  1  SER C CB  
1286 O OG  . SER C 4  ? 1.44694 1.59556 1.68847 0.23865  -0.00481 0.26915  1  SER C OG  
1287 N N   . ILE C 5  ? 0.94804 1.00987 1.10354 0.20340  0.03045  0.21884  2  ILE C N   
1288 C CA  . ILE C 5  ? 0.87582 0.94173 1.01052 0.17381  0.04030  0.19485  2  ILE C CA  
1289 C C   . ILE C 5  ? 0.81806 0.82935 0.92562 0.18290  0.06009  0.17351  2  ILE C C   
1290 O O   . ILE C 5  ? 0.91689 0.92384 1.00581 0.16013  0.06472  0.15548  2  ILE C O   
1291 C CB  . ILE C 5  ? 0.80148 0.93763 0.97295 0.16353  0.04276  0.18871  2  ILE C CB  
1292 C CG1 . ILE C 5  ? 0.71791 0.86962 0.92060 0.18873  0.06656  0.18258  2  ILE C CG1 
1293 C CG2 . ILE C 5  ? 0.86235 1.05095 1.06161 0.15821  0.01871  0.20972  2  ILE C CG2 
1294 C CD1 . ILE C 5  ? 0.62394 0.83289 0.85761 0.17127  0.07030  0.17678  2  ILE C CD1 
1295 N N   . LYS C 6  ? 0.79220 0.75806 0.89347 0.21750  0.07036  0.17432  3  LYS C N   
1296 C CA  . LYS C 6  ? 0.81810 0.72024 0.87775 0.22619  0.08668  0.15153  3  LYS C CA  
1297 C C   . LYS C 6  ? 0.82137 0.65892 0.83191 0.19647  0.07048  0.14487  3  LYS C C   
1298 O O   . LYS C 6  ? 0.70819 0.50290 0.68250 0.18841  0.07536  0.12461  3  LYS C O   
1299 C CB  . LYS C 6  ? 0.73689 0.59676 0.79291 0.27455  0.10259  0.15121  3  LYS C CB  
1300 C CG  . LYS C 6  ? 0.78493 0.56254 0.80815 0.28505  0.08506  0.16002  3  LYS C CG  
1301 C CD  . LYS C 6  ? 0.87923 0.64706 0.91770 0.32410  0.09299  0.15711  3  LYS C CD  
1302 C CE  . LYS C 6  ? 0.91906 0.68308 0.94303 0.34650  0.12553  0.13049  3  LYS C CE  
1303 N NZ  . LYS C 6  ? 1.15312 0.92522 1.20300 0.38553  0.13745  0.12957  3  LYS C NZ  
1304 N N   . GLU C 7  ? 0.71900 0.55081 0.72779 0.17784  0.05009  0.16423  4  GLU C N   
1305 C CA  . GLU C 7  ? 0.77098 0.56153 0.74722 0.14211  0.03601  0.16334  4  GLU C CA  
1306 C C   . GLU C 7  ? 0.71363 0.55727 0.70137 0.11085  0.03855  0.15153  4  GLU C C   
1307 O O   . GLU C 7  ? 0.69168 0.50721 0.66015 0.09014  0.03429  0.13929  4  GLU C O   
1308 C CB  . GLU C 7  ? 0.87833 0.65666 0.85041 0.12863  0.01786  0.19215  4  GLU C CB  
1309 C CG  . GLU C 7  ? 0.98515 0.71730 0.92859 0.09093  0.00438  0.19815  4  GLU C CG  
1310 C CD  . GLU C 7  ? 1.06238 0.78199 0.99757 0.07530  -0.01095 0.23197  4  GLU C CD  
1311 O OE1 . GLU C 7  ? 1.08197 0.85531 1.03367 0.08069  -0.01169 0.24857  4  GLU C OE1 
1312 O OE2 . GLU C 7  ? 1.06580 0.71824 0.97423 0.05496  -0.02485 0.24366  4  GLU C OE2 
1313 N N   . ILE C 8  ? 0.67890 0.59630 0.69839 0.10796  0.04242  0.15496  5  ILE C N   
1314 C CA  . ILE C 8  ? 0.55582 0.51821 0.58651 0.08634  0.04614  0.14064  5  ILE C CA  
1315 C C   . ILE C 8  ? 0.67447 0.62196 0.69941 0.09446  0.05625  0.11948  5  ILE C C   
1316 O O   . ILE C 8  ? 0.60387 0.55023 0.62299 0.07623  0.05355  0.10701  5  ILE C O   
1317 C CB  . ILE C 8  ? 0.48264 0.51181 0.53934 0.08461  0.04526  0.14597  5  ILE C CB  
1318 C CG1 . ILE C 8  ? 0.57414 0.61358 0.62148 0.07304  0.03382  0.16735  5  ILE C CG1 
1319 C CG2 . ILE C 8  ? 0.49442 0.55867 0.55999 0.06854  0.04924  0.12783  5  ILE C CG2 
1320 C CD1 . ILE C 8  ? 0.61902 0.71319 0.67882 0.07081  0.02691  0.17222  5  ILE C CD1 
1321 N N   . THR C 9  ? 0.63745 0.57494 0.66398 0.12310  0.06864  0.11722  6  THR C N   
1322 C CA  . THR C 9  ? 0.65384 0.57829 0.66652 0.13125  0.08222  0.10016  6  THR C CA  
1323 C C   . THR C 9  ? 0.71471 0.56367 0.67734 0.12631  0.07615  0.08702  6  THR C C   
1324 O O   . THR C 9  ? 0.63936 0.48079 0.58706 0.10868  0.07028  0.07510  6  THR C O   
1325 C CB  . THR C 9  ? 0.66169 0.60171 0.69070 0.16461  0.10303  0.10402  6  THR C CB  
1326 O OG1 . THR C 9  ? 0.62612 0.64029 0.70683 0.16282  0.10182  0.11786  6  THR C OG1 
1327 C CG2 . THR C 9  ? 0.57468 0.49938 0.57940 0.17163  0.12168  0.08901  6  THR C CG2 
1328 N N   . GLU C 10 ? 0.66158 0.44853 0.59595 0.14187  0.07358  0.08937  7  GLU C N   
1329 C CA  . GLU C 10 ? 0.77909 0.48122 0.65717 0.13566  0.06282  0.07514  7  GLU C CA  
1330 C C   . GLU C 10 ? 0.76090 0.46274 0.64092 0.09406  0.03805  0.07698  7  GLU C C   
1331 O O   . GLU C 10 ? 0.78595 0.44441 0.63169 0.07947  0.02491  0.06373  7  GLU C O   
1332 C CB  . GLU C 10 ? 0.83398 0.46178 0.68188 0.15850  0.06025  0.07829  7  GLU C CB  
1333 C CG  . GLU C 10 ? 0.85887 0.48119 0.70404 0.20728  0.08837  0.07329  7  GLU C CG  
1334 C CD  . GLU C 10 ? 1.16955 0.70978 0.98440 0.23649  0.08520  0.07451  7  GLU C CD  
1335 O OE1 . GLU C 10 ? 1.18951 0.67940 0.98869 0.21413  0.05827  0.08399  7  GLU C OE1 
1336 O OE2 . GLU C 10 ? 1.16156 0.69152 0.97141 0.28003  0.10978  0.06659  7  GLU C OE2 
1337 N N   . THR C 11 ? 0.65785 0.41105 0.57775 0.07488  0.03159  0.09427  8  THR C N   
1338 C CA  . THR C 11 ? 0.61570 0.38851 0.55101 0.03819  0.01534  0.09818  8  THR C CA  
1339 C C   . THR C 11 ? 0.62282 0.43821 0.57473 0.03142  0.01734  0.08455  8  THR C C   
1340 O O   . THR C 11 ? 0.59659 0.39569 0.54240 0.01170  0.00077  0.07843  8  THR C O   
1341 C CB  . THR C 11 ? 0.62359 0.44640 0.59138 0.02363  0.01602  0.11957  8  THR C CB  
1342 O OG1 . THR C 11 ? 0.67799 0.44938 0.62569 0.02513  0.00803  0.13658  8  THR C OG1 
1343 C CG2 . THR C 11 ? 0.53158 0.39289 0.52544 -0.00994 0.00820  0.12391  8  THR C CG2 
1344 N N   . THR C 12 ? 0.48378 0.35097 0.45801 0.04653  0.03361  0.08145  9  THR C N   
1345 C CA  . THR C 12 ? 0.53970 0.43634 0.52581 0.04228  0.03404  0.06989  9  THR C CA  
1346 C C   . THR C 12 ? 0.55279 0.39563 0.49563 0.04906  0.03085  0.05712  9  THR C C   
1347 O O   . THR C 12 ? 0.60779 0.44763 0.54708 0.03614  0.01716  0.05044  9  THR C O   
1348 C CB  . THR C 12 ? 0.46660 0.41743 0.48004 0.05403  0.04886  0.07066  9  THR C CB  
1349 O OG1 . THR C 12 ? 0.56013 0.55291 0.59931 0.04672  0.04900  0.08067  9  THR C OG1 
1350 C CG2 . THR C 12 ? 0.49415 0.46594 0.51823 0.04847  0.04650  0.06041  9  THR C CG2 
1351 N N   . GLN C 13 ? 0.60668 0.40546 0.51337 0.07147  0.04346  0.05392  10 GLN C N   
1352 C CA  . GLN C 13 ? 0.74228 0.47823 0.58996 0.07893  0.04273  0.03995  10 GLN C CA  
1353 C C   . GLN C 13 ? 0.66860 0.34949 0.48523 0.05449  0.01154  0.03457  10 GLN C C   
1354 O O   . GLN C 13 ? 0.74020 0.39396 0.52397 0.04498  -0.00293 0.02543  10 GLN C O   
1355 C CB  . GLN C 13 ? 0.68959 0.38430 0.50237 0.11198  0.06550  0.03585  10 GLN C CB  
1356 C CG  . GLN C 13 ? 0.70882 0.46349 0.55719 0.13545  0.09577  0.04327  10 GLN C CG  
1357 C CD  . GLN C 13 ? 0.72816 0.44907 0.54742 0.17349  0.12301  0.03885  10 GLN C CD  
1358 O OE1 . GLN C 13 ? 0.83740 0.57850 0.68974 0.19476  0.13308  0.04936  10 GLN C OE1 
1359 N NE2 . GLN C 13 ? 0.90725 0.57661 0.66247 0.18465  0.13557  0.02369  10 GLN C NE2 
1360 N N   . LEU C 14 ? 0.69590 0.36035 0.52349 0.04081  -0.00241 0.04325  11 LEU C N   
1361 C CA  . LEU C 14 ? 0.82941 0.44774 0.63846 0.01055  -0.03598 0.04255  11 LEU C CA  
1362 C C   . LEU C 14 ? 0.71840 0.39920 0.57856 -0.01592 -0.05286 0.04867  11 LEU C C   
1363 O O   . LEU C 14 ? 0.85240 0.50564 0.69501 -0.03487 -0.08100 0.04373  11 LEU C O   
1364 C CB  . LEU C 14 ? 0.90245 0.49091 0.71605 -0.00102 -0.04530 0.05581  11 LEU C CB  
1365 C CG  . LEU C 14 ? 1.04355 0.56864 0.83402 -0.03572 -0.08238 0.05836  11 LEU C CG  
1366 C CD1 . LEU C 14 ? 1.04337 0.64068 0.90334 -0.07387 -0.09814 0.07751  11 LEU C CD1 
1367 C CD2 . LEU C 14 ? 1.00218 0.45261 0.72385 -0.03682 -0.10283 0.03653  11 LEU C CD2 
1368 N N   . ILE C 15 ? 0.66721 0.43031 0.58922 -0.01572 -0.03757 0.05887  12 ILE C N   
1369 C CA  . ILE C 15 ? 0.66616 0.49141 0.64036 -0.03182 -0.04771 0.06231  12 ILE C CA  
1370 C C   . ILE C 15 ? 0.79461 0.61207 0.75064 -0.02316 -0.05450 0.05043  12 ILE C C   
1371 O O   . ILE C 15 ? 0.77820 0.60966 0.75541 -0.03775 -0.07812 0.05140  12 ILE C O   
1372 C CB  . ILE C 15 ? 0.60899 0.51190 0.63608 -0.02645 -0.02515 0.07009  12 ILE C CB  
1373 C CG1 . ILE C 15 ? 0.68237 0.59200 0.72141 -0.03948 -0.02094 0.08673  12 ILE C CG1 
1374 C CG2 . ILE C 15 ? 0.75083 0.71488 0.82967 -0.03339 -0.03007 0.06916  12 ILE C CG2 
1375 C CD1 . ILE C 15 ? 0.60690 0.58143 0.67741 -0.03285 0.00165  0.09352  12 ILE C CD1 
1376 N N   . VAL C 16 ? 0.71617 0.51340 0.63539 0.00018  -0.03459 0.04232  13 VAL C N   
1377 C CA  . VAL C 16 ? 0.62756 0.41653 0.52456 0.00675  -0.03765 0.03564  13 VAL C CA  
1378 C C   . VAL C 16 ? 0.75145 0.46641 0.58233 -0.00197 -0.06292 0.02835  13 VAL C C   
1379 O O   . VAL C 16 ? 0.72947 0.44020 0.55424 -0.01123 -0.08617 0.02840  13 VAL C O   
1380 C CB  . VAL C 16 ? 0.48022 0.27963 0.36486 0.02994  -0.00553 0.03410  13 VAL C CB  
1381 C CG1 . VAL C 16 ? 0.60402 0.37134 0.44088 0.03492  -0.00572 0.03000  13 VAL C CG1 
1382 C CG2 . VAL C 16 ? 0.56977 0.44017 0.51612 0.03225  0.00701  0.03958  13 VAL C CG2 
1383 N N   . LYS C 17 ? 0.76815 0.41754 0.54385 0.00165  -0.06186 0.02158  14 LYS C N   
1384 C CA  . LYS C 17 ? 0.94219 0.50697 0.63783 -0.00645 -0.08728 0.01038  14 LYS C CA  
1385 C C   . LYS C 17 ? 0.91117 0.47548 0.62923 -0.04027 -0.13466 0.01624  14 LYS C C   
1386 O O   . LYS C 17 ? 0.92460 0.44146 0.59058 -0.05107 -0.16474 0.01069  14 LYS C O   
1387 C CB  . LYS C 17 ? 0.91275 0.39984 0.54637 0.00547  -0.07862 -0.00063 14 LYS C CB  
1388 C CG  . LYS C 17 ? 0.82504 0.30428 0.42840 0.04368  -0.03316 -0.00750 14 LYS C CG  
1389 C CD  . LYS C 17 ? 0.99206 0.38977 0.53923 0.06015  -0.02727 -0.01935 14 LYS C CD  
1390 C CE  . LYS C 17 ? 1.03666 0.45353 0.59028 0.10150  0.01992  -0.01969 14 LYS C CE  
1391 N NZ  . LYS C 17 ? 1.18929 0.53444 0.70843 0.12124  0.02364  -0.02767 14 LYS C NZ  
1392 N N   . HIS C 18 ? 0.97219 0.59115 0.76690 -0.05820 -0.14243 0.02947  15 HIS C N   
1393 C CA  . HIS C 18 ? 0.98211 0.61656 0.81590 -0.09158 -0.18517 0.03943  15 HIS C CA  
1394 C C   . HIS C 18 ? 0.84160 0.55315 0.74279 -0.09128 -0.19286 0.04773  15 HIS C C   
1395 O O   . HIS C 18 ? 0.89976 0.61063 0.81298 -0.11052 -0.23350 0.05304  15 HIS C O   
1396 C CB  . HIS C 18 ? 0.97165 0.63218 0.85836 -0.11344 -0.18715 0.05373  15 HIS C CB  
1397 C CG  . HIS C 18 ? 1.10184 0.66794 0.92318 -0.12557 -0.20185 0.04854  15 HIS C CG  
1398 N ND1 . HIS C 18 ? 1.13408 0.62220 0.87222 -0.09782 -0.18161 0.03103  15 HIS C ND1 
1399 C CD2 . HIS C 18 ? 1.17405 0.70773 1.00173 -0.16210 -0.23536 0.05882  15 HIS C CD2 
1400 C CE1 . HIS C 18 ? 1.36086 0.76418 1.05103 -0.11285 -0.20238 0.02760  15 HIS C CE1 
1401 N NE2 . HIS C 18 ? 1.43260 0.85853 1.17405 -0.15501 -0.23737 0.04504  15 HIS C NE2 
1402 N N   . LEU C 19 ? 0.74340 0.51601 0.68649 -0.06889 -0.15813 0.04861  16 LEU C N   
1403 C CA  . LEU C 19 ? 0.77614 0.61962 0.78856 -0.06420 -0.16206 0.05476  16 LEU C CA  
1404 C C   . LEU C 19 ? 0.69838 0.51980 0.67517 -0.04825 -0.16636 0.04954  16 LEU C C   
1405 O O   . LEU C 19 ? 0.77212 0.61345 0.78001 -0.05127 -0.19410 0.05557  16 LEU C O   
1406 C CB  . LEU C 19 ? 0.63012 0.54493 0.70271 -0.05104 -0.12533 0.05710  16 LEU C CB  
1407 C CG  . LEU C 19 ? 0.77366 0.76905 0.93378 -0.05143 -0.12878 0.06428  16 LEU C CG  
1408 C CD1 . LEU C 19 ? 0.74856 0.76521 0.95237 -0.08018 -0.15722 0.07839  16 LEU C CD1 
1409 C CD2 . LEU C 19 ? 0.73264 0.78399 0.92886 -0.03750 -0.09023 0.06241  16 LEU C CD2 
1410 N N   . ALA C 20 ? 0.70901 0.49245 0.62526 -0.03150 -0.13982 0.04159  17 ALA C N   
1411 C CA  . ALA C 20 ? 0.71902 0.48892 0.60619 -0.01879 -0.13673 0.04148  17 ALA C CA  
1412 C C   . ALA C 20 ? 0.71831 0.41278 0.51883 -0.02646 -0.16306 0.03985  17 ALA C C   
1413 O O   . ALA C 20 ? 0.75785 0.39394 0.49283 -0.03121 -0.16429 0.03149  17 ALA C O   
1414 C CB  . ALA C 20 ? 0.74006 0.51761 0.61315 -0.00040 -0.09347 0.03820  17 ALA C CB  
1415 N N   . HIS C 21 ? 0.74444 0.43359 0.53850 -0.02667 -0.18580 0.04755  18 HIS C N   
1416 C CA  . HIS C 21 ? 0.89424 0.50870 0.58935 -0.03130 -0.20416 0.04785  18 HIS C CA  
1417 C C   . HIS C 21 ? 0.93641 0.52027 0.56395 -0.01573 -0.15781 0.04235  18 HIS C C   
1418 O O   . HIS C 21 ? 0.87880 0.50699 0.54766 -0.00286 -0.12219 0.04548  18 HIS C O   
1419 C CB  . HIS C 21 ? 0.87426 0.49139 0.57920 -0.03312 -0.23716 0.06218  18 HIS C CB  
1420 C CG  . HIS C 21 ? 0.93879 0.59198 0.71662 -0.04472 -0.28459 0.07015  18 HIS C CG  
1421 N ND1 . HIS C 21 ? 0.81070 0.54443 0.70035 -0.03743 -0.27786 0.07271  18 HIS C ND1 
1422 C CD2 . HIS C 21 ? 0.87774 0.50180 0.63512 -0.06276 -0.33949 0.07730  18 HIS C CD2 
1423 C CE1 . HIS C 21 ? 0.74631 0.50690 0.69031 -0.04842 -0.32235 0.08239  18 HIS C CE1 
1424 N NE2 . HIS C 21 ? 0.84120 0.53742 0.71020 -0.06560 -0.36379 0.08646  18 HIS C NE2 
1425 N N   . ASN C 22 ? 1.04154 0.55022 0.56489 -0.01693 -0.15858 0.03396  19 ASN C N   
1426 C CA  . ASN C 22 ? 1.02352 0.50577 0.48334 0.00168  -0.10913 0.02710  19 ASN C CA  
1427 C C   . ASN C 22 ? 0.89699 0.42669 0.41972 0.01604  -0.07177 0.02144  19 ASN C C   
1428 O O   . ASN C 22 ? 0.81779 0.38527 0.36374 0.03123  -0.03085 0.02658  19 ASN C O   
1429 C CB  . ASN C 22 ? 0.91708 0.40904 0.35642 0.00721  -0.08769 0.04215  19 ASN C CB  
1430 C CG  . ASN C 22 ? 1.16593 0.62951 0.57494 -0.00844 -0.13282 0.05547  19 ASN C CG  
1431 O OD1 . ASN C 22 ? 1.11046 0.61694 0.59459 -0.01355 -0.15565 0.06759  19 ASN C OD1 
1432 N ND2 . ASN C 22 ? 1.22673 0.61372 0.52107 -0.01393 -0.14699 0.05294  19 ASN C ND2 
1433 N N   . GLY C 23 ? 0.86563 0.39449 0.41872 0.00800  -0.08999 0.01401  20 GLY C N   
1434 C CA  . GLY C 23 ? 0.84274 0.41657 0.45811 0.01833  -0.06276 0.01290  20 GLY C CA  
1435 C C   . GLY C 23 ? 0.81490 0.36617 0.38811 0.04398  -0.01893 0.00533  20 GLY C C   
1436 O O   . GLY C 23 ? 0.84553 0.44949 0.47480 0.05748  0.01022  0.01054  20 GLY C O   
1437 N N   . GLU C 24 ? 0.89108 0.36466 0.36455 0.05289  -0.01397 -0.00714 21 GLU C N   
1438 C CA  . GLU C 24 ? 0.93190 0.38565 0.36710 0.08420  0.03242  -0.01555 21 GLU C CA  
1439 C C   . GLU C 24 ? 0.88604 0.40371 0.35361 0.09860  0.07427  -0.00133 21 GLU C C   
1440 O O   . GLU C 24 ? 0.85974 0.41423 0.36244 0.12189  0.11200  0.00147  21 GLU C O   
1441 C CB  . GLU C 24 ? 1.06864 0.41868 0.37834 0.09323  0.03102  -0.03548 21 GLU C CB  
1442 C CG  . GLU C 24 ? 1.21432 0.49550 0.49087 0.10068  0.02060  -0.05391 21 GLU C CG  
1443 C CD  . GLU C 24 ? 1.25761 0.56802 0.57776 0.13454  0.06383  -0.05384 21 GLU C CD  
1444 O OE1 . GLU C 24 ? 1.18673 0.55264 0.53188 0.15842  0.10906  -0.04523 21 GLU C OE1 
1445 O OE2 . GLU C 24 ? 1.27099 0.54974 0.60360 0.13570  0.05009  -0.05947 21 GLU C OE2 
1446 N N   . GLU C 25 ? 0.88136 0.41299 0.34134 0.08346  0.06513  0.01053  22 GLU C N   
1447 C CA  . GLU C 25 ? 0.90412 0.49742 0.40374 0.08873  0.09903  0.02820  22 GLU C CA  
1448 C C   . GLU C 25 ? 0.72562 0.39921 0.33635 0.08450  0.09860  0.03787  22 GLU C C   
1449 O O   . GLU C 25 ? 0.70356 0.42939 0.35889 0.09673  0.13190  0.04709  22 GLU C O   
1450 C CB  . GLU C 25 ? 0.86899 0.44767 0.33140 0.07035  0.08345  0.04135  22 GLU C CB  
1451 C CG  . GLU C 25 ? 1.05018 0.55314 0.38949 0.07524  0.09238  0.03568  22 GLU C CG  
1452 C CD  . GLU C 25 ? 1.11630 0.61997 0.42259 0.06161  0.09646  0.05767  22 GLU C CD  
1453 O OE1 . GLU C 25 ? 1.15205 0.71611 0.53558 0.05133  0.09949  0.07697  22 GLU C OE1 
1454 O OE2 . GLU C 25 ? 1.33733 0.77477 0.53393 0.05984  0.09499  0.05616  22 GLU C OE2 
1455 N N   . TYR C 26 ? 0.67559 0.36202 0.33159 0.06740  0.06120  0.03627  23 TYR C N   
1456 C CA  . TYR C 26 ? 0.63289 0.38737 0.37937 0.06477  0.06181  0.04193  23 TYR C CA  
1457 C C   . TYR C 26 ? 0.58800 0.35529 0.35672 0.08046  0.07927  0.03743  23 TYR C C   
1458 O O   . TYR C 26 ? 0.62572 0.44881 0.45204 0.08609  0.09490  0.04526  23 TYR C O   
1459 C CB  . TYR C 26 ? 0.63653 0.40352 0.42254 0.04695  0.02388  0.04059  23 TYR C CB  
1460 C CG  . TYR C 26 ? 0.62959 0.39866 0.41933 0.03600  0.00557  0.04845  23 TYR C CG  
1461 C CD1 . TYR C 26 ? 0.50431 0.31358 0.33676 0.03476  0.01617  0.05727  23 TYR C CD1 
1462 C CD2 . TYR C 26 ? 0.65352 0.37919 0.40333 0.02594  -0.02717 0.04819  23 TYR C CD2 
1463 C CE1 . TYR C 26 ? 0.65187 0.45200 0.48535 0.02595  -0.00306 0.06530  23 TYR C CE1 
1464 C CE2 . TYR C 26 ? 0.66461 0.38777 0.41877 0.01870  -0.04741 0.05815  23 TYR C CE2 
1465 C CZ  . TYR C 26 ? 0.70281 0.46040 0.49822 0.01983  -0.03415 0.06649  23 TYR C CZ  
1466 O OH  . TYR C 26 ? 0.58595 0.33032 0.38320 0.01379  -0.05655 0.07714  23 TYR C OH  
1467 N N   . SER C 27 ? 0.65679 0.36711 0.37753 0.08662  0.07266  0.02577  24 SER C N   
1468 C CA  . SER C 27 ? 0.73310 0.44290 0.46949 0.10340  0.08614  0.02335  24 SER C CA  
1469 C C   . SER C 27 ? 0.78488 0.51680 0.52427 0.13231  0.12819  0.02798  24 SER C C   
1470 O O   . SER C 27 ? 0.63550 0.40797 0.42632 0.14555  0.14051  0.03558  24 SER C O   
1471 C CB  . SER C 27 ? 0.71171 0.33964 0.38640 0.10269  0.06742  0.00928  24 SER C CB  
1472 O OG  . SER C 27 ? 0.92693 0.54216 0.61090 0.12133  0.07945  0.00833  24 SER C OG  
1473 N N   . GLU C 28 ? 0.70163 0.41052 0.38708 0.14260  0.15075  0.02577  25 GLU C N   
1474 C CA  . GLU C 28 ? 0.70282 0.44895 0.40298 0.16947  0.19589  0.03407  25 GLU C CA  
1475 C C   . GLU C 28 ? 0.74377 0.58128 0.53240 0.15809  0.20185  0.05483  25 GLU C C   
1476 O O   . GLU C 28 ? 0.59522 0.48581 0.43556 0.17663  0.22691  0.06582  25 GLU C O   
1477 C CB  . GLU C 28 ? 0.78922 0.49491 0.40758 0.17879  0.22188  0.02977  25 GLU C CB  
1478 C CG  . GLU C 28 ? 0.90210 0.66205 0.54379 0.20328  0.27452  0.04331  25 GLU C CG  
1479 C CD  . GLU C 28 ? 1.02784 0.79730 0.69600 0.24226  0.30013  0.03839  25 GLU C CD  
1480 O OE1 . GLU C 28 ? 1.03324 0.72933 0.65186 0.25761  0.28784  0.01804  25 GLU C OE1 
1481 O OE2 . GLU C 28 ? 1.08809 0.93873 0.83644 0.24910  0.31839  0.05688  25 GLU C OE2 
1482 N N   . VAL C 29 ? 0.57254 0.42671 0.38063 0.12839  0.17589  0.06022  26 VAL C N   
1483 C CA  . VAL C 29 ? 0.61109 0.53717 0.49418 0.11437  0.17464  0.07610  26 VAL C CA  
1484 C C   . VAL C 29 ? 0.53888 0.50169 0.48075 0.11704  0.16240  0.07648  26 VAL C C   
1485 O O   . VAL C 29 ? 0.42953 0.45167 0.42891 0.11944  0.17198  0.08965  26 VAL C O   
1486 C CB  . VAL C 29 ? 0.56733 0.48654 0.44827 0.08656  0.14787  0.07822  26 VAL C CB  
1487 C CG1 . VAL C 29 ? 0.42545 0.40348 0.37602 0.07126  0.14053  0.08940  26 VAL C CG1 
1488 C CG2 . VAL C 29 ? 0.54823 0.43370 0.36924 0.08227  0.16006  0.08462  26 VAL C CG2 
1489 N N   . VAL C 30 ? 0.52095 0.45010 0.44841 0.11397  0.13936  0.06477  27 VAL C N   
1490 C CA  . VAL C 30 ? 0.54459 0.50145 0.51499 0.11585  0.12945  0.06778  27 VAL C CA  
1491 C C   . VAL C 30 ? 0.44541 0.41819 0.43274 0.14384  0.15245  0.07589  27 VAL C C   
1492 O O   . VAL C 30 ? 0.53582 0.55882 0.57534 0.14616  0.15009  0.08780  27 VAL C O   
1493 C CB  . VAL C 30 ? 0.56443 0.47899 0.51180 0.10622  0.10543  0.05795  27 VAL C CB  
1494 C CG1 . VAL C 30 ? 0.47877 0.41865 0.46164 0.10672  0.09819  0.06525  27 VAL C CG1 
1495 C CG2 . VAL C 30 ? 0.48028 0.39372 0.42777 0.08273  0.08300  0.05244  27 VAL C CG2 
1496 N N   . LYS C 31 ? 0.55793 0.48632 0.49919 0.16768  0.17392  0.06921  28 LYS C N   
1497 C CA  . LYS C 31 ? 0.59796 0.54136 0.55871 0.20252  0.19997  0.07606  28 LYS C CA  
1498 C C   . LYS C 31 ? 0.58620 0.61347 0.61091 0.20618  0.22152  0.09526  28 LYS C C   
1499 O O   . LYS C 31 ? 0.57574 0.65583 0.66168 0.21845  0.22248  0.11009  28 LYS C O   
1500 C CB  . LYS C 31 ? 0.63225 0.50334 0.51972 0.23044  0.22259  0.06026  28 LYS C CB  
1501 C CG  . LYS C 31 ? 0.73087 0.56994 0.61541 0.26773  0.23214  0.05735  28 LYS C CG  
1502 C CD  . LYS C 31 ? 0.89072 0.80868 0.84858 0.28761  0.25116  0.07628  28 LYS C CD  
1503 C CE  . LYS C 31 ? 0.84326 0.73243 0.80522 0.31530  0.24657  0.07559  28 LYS C CE  
1504 N NZ  . LYS C 31 ? 0.69336 0.66224 0.73081 0.32983  0.25675  0.09451  28 LYS C NZ  
1505 N N   . GLU C 32 ? 0.55856 0.59899 0.57112 0.19277  0.23576  0.09833  29 GLU C N   
1506 C CA  . GLU C 32 ? 0.57606 0.69543 0.65100 0.18881  0.25450  0.11987  29 GLU C CA  
1507 C C   . GLU C 32 ? 0.51820 0.69551 0.66194 0.16360  0.22559  0.13242  29 GLU C C   
1508 O O   . GLU C 32 ? 0.39239 0.62673 0.59596 0.16380  0.22153  0.14716  29 GLU C O   
1509 C CB  . GLU C 32 ? 0.59522 0.70743 0.63537 0.17257  0.27164  0.12374  29 GLU C CB  
1510 C CG  . GLU C 32 ? 0.68432 0.73410 0.64212 0.19364  0.29687  0.10988  29 GLU C CG  
1511 C CD  . GLU C 32 ? 0.93861 0.97987 0.85553 0.17403  0.31040  0.11746  29 GLU C CD  
1512 O OE1 . GLU C 32 ? 0.88130 0.98450 0.85269 0.15446  0.31535  0.13822  29 GLU C OE1 
1513 O OE2 . GLU C 32 ? 1.05835 1.02621 0.88432 0.17548  0.31221  0.10374  29 GLU C OE2 
1514 N N   . ILE C 33 ? 0.42620 0.57656 0.55089 0.13566  0.19330  0.12179  30 ILE C N   
1515 C CA  . ILE C 33 ? 0.40456 0.59641 0.57725 0.11228  0.16511  0.12788  30 ILE C CA  
1516 C C   . ILE C 33 ? 0.47400 0.68656 0.67608 0.12611  0.15335  0.13231  30 ILE C C   
1517 O O   . ILE C 33 ? 0.39466 0.66042 0.64777 0.11647  0.13904  0.14556  30 ILE C O   
1518 C CB  . ILE C 33 ? 0.40134 0.55539 0.54258 0.08750  0.13875  0.11234  30 ILE C CB  
1519 C CG1 . ILE C 33 ? 0.32447 0.45725 0.43944 0.07359  0.14525  0.11314  30 ILE C CG1 
1520 C CG2 . ILE C 33 ? 0.48293 0.66875 0.65935 0.06747  0.11206  0.11293  30 ILE C CG2 
1521 C CD1 . ILE C 33 ? 0.36350 0.54526 0.51959 0.06134  0.15831  0.13417  30 ILE C CD1 
1522 N N   . SER C 34 ? 0.41492 0.58155 0.58229 0.14658  0.15550  0.12329  31 SER C N   
1523 C CA  . SER C 34 ? 0.54192 0.71958 0.73114 0.15935  0.14266  0.13147  31 SER C CA  
1524 C C   . SER C 34 ? 0.46187 0.69434 0.70798 0.18511  0.15796  0.15167  31 SER C C   
1525 O O   . SER C 34 ? 0.37921 0.64850 0.66382 0.18327  0.13753  0.16561  31 SER C O   
1526 C CB  . SER C 34 ? 0.42441 0.53182 0.56241 0.17282  0.14064  0.12001  31 SER C CB  
1527 O OG  . SER C 34 ? 0.71541 0.78490 0.82430 0.20183  0.16732  0.11382  31 SER C OG  
1528 N N   . GLU C 35 ? 0.53716 0.76392 0.77379 0.20021  0.18552  0.14965  32 GLU C N   
1529 C CA  . GLU C 35 ? 0.49117 0.76449 0.77446 0.21436  0.19421  0.16398  32 GLU C CA  
1530 C C   . GLU C 35 ? 0.53167 0.87709 0.87673 0.18602  0.17558  0.18116  32 GLU C C   
1531 O O   . GLU C 35 ? 0.47533 0.86383 0.86914 0.19036  0.16108  0.19621  32 GLU C O   
1532 C CB  . GLU C 35 ? 0.54787 0.80708 0.80715 0.23281  0.23051  0.15823  32 GLU C CB  
1533 C CG  . GLU C 35 ? 0.71461 0.89425 0.90544 0.26264  0.24695  0.13897  32 GLU C CG  
1534 C CD  . GLU C 35 ? 0.81180 0.97401 0.96622 0.27857  0.28268  0.13112  32 GLU C CD  
1535 O OE1 . GLU C 35 ? 0.82890 1.04675 1.01747 0.26645  0.29689  0.14366  32 GLU C OE1 
1536 O OE2 . GLU C 35 ? 0.83787 0.92743 0.92572 0.30168  0.29540  0.11251  32 GLU C OE2 
1537 N N   . GLU C 36 ? 0.33434 0.68903 0.67637 0.15612  0.17296  0.17957  33 GLU C N   
1538 C CA  . GLU C 36 ? 0.48670 0.89797 0.88069 0.12505  0.15116  0.19407  33 GLU C CA  
1539 C C   . GLU C 36 ? 0.47706 0.89973 0.88490 0.11245  0.11394  0.19601  33 GLU C C   
1540 O O   . GLU C 36 ? 0.31773 0.78761 0.77190 0.09992  0.09140  0.21082  33 GLU C O   
1541 C CB  . GLU C 36 ? 0.43597 0.84087 0.81641 0.09589  0.15504  0.19154  33 GLU C CB  
1542 C CG  . GLU C 36 ? 0.50938 0.96138 0.93861 0.05948  0.13067  0.20595  33 GLU C CG  
1543 C CD  . GLU C 36 ? 0.69120 1.13390 1.10994 0.03269  0.13963  0.20922  33 GLU C CD  
1544 O OE1 . GLU C 36 ? 0.69673 1.11268 1.07909 0.04562  0.17102  0.20616  33 GLU C OE1 
1545 O OE2 . GLU C 36 ? 0.62508 1.08149 1.06689 -0.00262 0.11319  0.21549  33 GLU C OE2 
1546 N N   . MET C 37 ? 0.38071 0.76174 0.74720 0.11498  0.10637  0.18226  34 MET C N   
1547 C CA  . MET C 37 ? 0.34800 0.73774 0.71696 0.10451  0.07346  0.18432  34 MET C CA  
1548 C C   . MET C 37 ? 0.38425 0.78825 0.77348 0.12749  0.06450  0.19954  34 MET C C   
1549 O O   . MET C 37 ? 0.36319 0.79432 0.76904 0.11605  0.03308  0.21067  34 MET C O   
1550 C CB  . MET C 37 ? 0.35223 0.67539 0.65188 0.09656  0.06801  0.16029  34 MET C CB  
1551 C CG  . MET C 37 ? 0.31132 0.60929 0.58430 0.07350  0.06904  0.14261  34 MET C CG  
1552 S SD  . MET C 37 ? 0.55946 0.80030 0.77195 0.06463  0.05958  0.11797  34 MET C SD  
1553 C CE  . MET C 37 ? 0.36015 0.55784 0.54408 0.09072  0.07899  0.11719  34 MET C CE  
1554 N N   . GLU C 38 ? 0.39553 0.77532 0.77712 0.15939  0.08904  0.19942  35 GLU C N   
1555 C CA  . GLU C 38 ? 0.34237 0.72854 0.74366 0.18365  0.08049  0.21351  35 GLU C CA  
1556 C C   . GLU C 38 ? 0.44656 0.89527 0.91031 0.18302  0.07605  0.23030  35 GLU C C   
1557 O O   . GLU C 38 ? 0.42713 0.90194 0.92071 0.18775  0.05146  0.24641  35 GLU C O   
1558 C CB  . GLU C 38 ? 0.43154 0.76058 0.79872 0.21905  0.10635  0.20430  35 GLU C CB  
1559 C CG  . GLU C 38 ? 0.63671 0.95622 1.01667 0.24646  0.09542  0.21703  35 GLU C CG  
1560 C CD  . GLU C 38 ? 0.76227 1.00784 1.09692 0.27833  0.11567  0.20407  35 GLU C CD  
1561 O OE1 . GLU C 38 ? 0.86634 1.07158 1.15889 0.27897  0.13875  0.18508  35 GLU C OE1 
1562 O OE2 . GLU C 38 ? 0.92502 1.14681 1.26193 0.30164  0.10526  0.21244  35 GLU C OE2 
1563 N N   . LYS C 39 ? 0.42658 0.90067 0.91116 0.17637  0.09822  0.22920  36 LYS C N   
1564 C CA  . LYS C 39 ? 0.42610 0.96694 0.97716 0.17127  0.09406  0.24789  36 LYS C CA  
1565 C C   . LYS C 39 ? 0.37559 0.95569 0.95575 0.13410  0.05253  0.25909  36 LYS C C   
1566 O O   . LYS C 39 ? 0.34418 0.97803 0.98112 0.12976  0.03624  0.27768  36 LYS C O   
1567 C CB  . LYS C 39 ? 0.51119 1.06956 1.07354 0.16861  0.12805  0.24698  36 LYS C CB  
1568 C CG  . LYS C 39 ? 0.46022 0.98815 0.99688 0.20725  0.16961  0.23733  36 LYS C CG  
1569 C CD  . LYS C 39 ? 0.65774 1.20251 1.19557 0.19980  0.20219  0.23770  36 LYS C CD  
1570 C CE  . LYS C 39 ? 0.70653 1.20930 1.19959 0.23637  0.24331  0.22351  36 LYS C CE  
1571 N NZ  . LYS C 39 ? 0.91301 1.43561 1.44026 0.27635  0.25596  0.22901  36 LYS C NZ  
1572 N N   . LYS C 40 ? 0.32694 0.88086 0.86899 0.10760  0.03380  0.24743  37 LYS C N   
1573 C CA  . LYS C 40 ? 0.44270 1.02218 0.99833 0.07127  -0.00803 0.25308  37 LYS C CA  
1574 C C   . LYS C 40 ? 0.36139 0.92673 0.88962 0.07188  -0.04169 0.25471  37 LYS C C   
1575 O O   . LYS C 40 ? 0.39603 0.97182 0.91737 0.04180  -0.07968 0.25544  37 LYS C O   
1576 C CB  . LYS C 40 ? 0.36531 0.92660 0.89677 0.03939  -0.00988 0.23858  37 LYS C CB  
1577 C CG  . LYS C 40 ? 0.46057 1.03902 1.01877 0.02986  0.01525  0.24328  37 LYS C CG  
1578 C CD  . LYS C 40 ? 0.54811 1.11008 1.09077 -0.00792 0.00201  0.23427  37 LYS C CD  
1579 C CE  . LYS C 40 ? 0.56040 1.13886 1.12832 -0.02039 0.02535  0.24468  37 LYS C CE  
1580 N NZ  . LYS C 40 ? 0.61289 1.16879 1.16767 -0.06027 0.00764  0.23922  37 LYS C NZ  
1581 N N   . GLY C 41 ? 0.34724 0.88358 0.85299 0.10381  -0.03049 0.25567  38 GLY C N   
1582 C CA  . GLY C 41 ? 0.51502 1.03696 0.99160 0.10473  -0.06196 0.26327  38 GLY C CA  
1583 C C   . GLY C 41 ? 0.43178 0.93135 0.85436 0.07970  -0.08102 0.25098  38 GLY C C   
1584 O O   . GLY C 41 ? 0.43190 0.93110 0.82581 0.06636  -0.11640 0.25835  38 GLY C O   
1585 N N   . LEU C 42 ? 0.44807 0.91883 0.84307 0.07136  -0.05732 0.22816  39 LEU C N   
1586 C CA  . LEU C 42 ? 0.43236 0.85421 0.75364 0.04810  -0.06494 0.20218  39 LEU C CA  
1587 C C   . LEU C 42 ? 0.48431 0.86562 0.75197 0.05989  -0.06377 0.20259  39 LEU C C   
1588 O O   . LEU C 42 ? 0.55341 0.91561 0.82529 0.08583  -0.04462 0.21082  39 LEU C O   
1589 C CB  . LEU C 42 ? 0.38314 0.77349 0.68623 0.04214  -0.03751 0.17765  39 LEU C CB  
1590 C CG  . LEU C 42 ? 0.39550 0.81634 0.74465 0.02759  -0.03418 0.17983  39 LEU C CG  
1591 C CD1 . LEU C 42 ? 0.40332 0.78178 0.72232 0.02357  -0.01036 0.15792  39 LEU C CD1 
1592 C CD2 . LEU C 42 ? 0.33462 0.77785 0.69276 -0.00503 -0.07280 0.18110  39 LEU C CD2 
1593 N N   . SER C 43 ? 0.34641 0.71079 0.55911 0.03966  -0.08392 0.19394  40 SER C N   
1594 C CA  . SER C 43 ? 0.47838 0.80907 0.63730 0.04415  -0.08209 0.19849  40 SER C CA  
1595 C C   . SER C 43 ? 0.52507 0.81490 0.66022 0.05058  -0.04850 0.18166  40 SER C C   
1596 O O   . SER C 43 ? 0.53610 0.81900 0.68031 0.04776  -0.03097 0.16113  40 SER C O   
1597 C CB  . SER C 43 ? 0.57029 0.89358 0.66723 0.02021  -0.10428 0.19000  40 SER C CB  
1598 O OG  . SER C 43 ? 0.60520 0.91172 0.67430 0.00543  -0.09219 0.15719  40 SER C OG  
1599 N N   . LYS C 44 ? 0.56074 0.82181 0.66548 0.05686  -0.04344 0.19368  41 LYS C N   
1600 C CA  . LYS C 44 ? 0.56892 0.79301 0.65200 0.05663  -0.01821 0.18104  41 LYS C CA  
1601 C C   . LYS C 44 ? 0.56927 0.79334 0.62251 0.03733  -0.00882 0.15527  41 LYS C C   
1602 O O   . LYS C 44 ? 0.50743 0.71623 0.56557 0.03735  0.00945  0.13873  41 LYS C O   
1603 C CB  . LYS C 44 ? 0.53850 0.73121 0.59369 0.05930  -0.01946 0.20289  41 LYS C CB  
1604 C CG  . LYS C 44 ? 0.77159 0.94203 0.85413 0.08607  -0.02105 0.22210  41 LYS C CG  
1605 C CD  . LYS C 44 ? 0.76848 0.89038 0.81765 0.08445  -0.02255 0.24131  41 LYS C CD  
1606 C CE  . LYS C 44 ? 0.88928 0.96884 0.95811 0.11456  -0.01964 0.25076  41 LYS C CE  
1607 N NZ  . LYS C 44 ? 0.83760 0.85491 0.87046 0.10851  -0.02360 0.26789  41 LYS C NZ  
1608 N N   . GLU C 45 ? 0.63049 0.86908 0.65043 0.02297  -0.02224 0.15093  42 GLU C N   
1609 C CA  . GLU C 45 ? 0.53931 0.77633 0.53073 0.01137  -0.01136 0.12282  42 GLU C CA  
1610 C C   . GLU C 45 ? 0.54700 0.78529 0.57058 0.01290  -0.00918 0.10095  42 GLU C C   
1611 O O   . GLU C 45 ? 0.50302 0.73033 0.52465 0.01302  0.00714  0.08036  42 GLU C O   
1612 C CB  . GLU C 45 ? 0.60948 0.85332 0.54835 -0.00144 -0.02785 0.11918  42 GLU C CB  
1613 C CG  . GLU C 45 ? 0.65954 0.89972 0.55309 -0.00648 -0.02979 0.14353  42 GLU C CG  
1614 C CD  . GLU C 45 ? 0.78863 1.03423 0.69693 -0.00161 -0.05852 0.17643  42 GLU C CD  
1615 O OE1 . GLU C 45 ? 0.66661 0.91574 0.63234 0.01339  -0.06058 0.18719  42 GLU C OE1 
1616 O OE2 . GLU C 45 ? 0.93799 1.18424 0.79852 -0.01073 -0.07901 0.19192  42 GLU C OE2 
1617 N N   . GLN C 46 ? 0.46753 0.72181 0.52507 0.01346  -0.02632 0.10858  43 GLN C N   
1618 C CA  . GLN C 46 ? 0.46737 0.72196 0.55438 0.01041  -0.02501 0.09382  43 GLN C CA  
1619 C C   . GLN C 46 ? 0.42613 0.66809 0.53975 0.02359  -0.00221 0.09466  43 GLN C C   
1620 O O   . GLN C 46 ? 0.36302 0.58935 0.47840 0.02132  0.00650  0.07769  43 GLN C O   
1621 C CB  . GLN C 46 ? 0.46817 0.75223 0.59036 0.00257  -0.04921 0.10743  43 GLN C CB  
1622 C CG  . GLN C 46 ? 0.55092 0.82879 0.66717 -0.01755 -0.06674 0.08872  43 GLN C CG  
1623 C CD  . GLN C 46 ? 0.67932 0.99186 0.83183 -0.03282 -0.09791 0.10650  43 GLN C CD  
1624 O OE1 . GLN C 46 ? 0.60319 0.95240 0.79458 -0.02370 -0.10360 0.13395  43 GLN C OE1 
1625 N NE2 . GLN C 46 ? 0.64632 0.94652 0.78964 -0.05609 -0.12066 0.09182  43 GLN C NE2 
1626 N N   . VAL C 47 ? 0.45007 0.69189 0.57870 0.03846  0.00528  0.11387  44 VAL C N   
1627 C CA  . VAL C 47 ? 0.37544 0.59482 0.51471 0.05143  0.02517  0.11227  44 VAL C CA  
1628 C C   . VAL C 47 ? 0.34272 0.53409 0.45581 0.04572  0.03513  0.09566  44 VAL C C   
1629 O O   . VAL C 47 ? 0.32300 0.49753 0.43948 0.04679  0.04345  0.08452  44 VAL C O   
1630 C CB  . VAL C 47 ? 0.38980 0.60115 0.53821 0.07123  0.02977  0.13239  44 VAL C CB  
1631 C CG1 . VAL C 47 ? 0.37761 0.54871 0.51549 0.08308  0.04810  0.12577  44 VAL C CG1 
1632 C CG2 . VAL C 47 ? 0.49618 0.74585 0.68848 0.08269  0.02382  0.14970  44 VAL C CG2 
1633 N N   . ILE C 48 ? 0.31419 0.50429 0.40272 0.03864  0.03393  0.09639  45 ILE C N   
1634 C CA  . ILE C 48 ? 0.42651 0.60400 0.50368 0.03268  0.04432  0.08482  45 ILE C CA  
1635 C C   . ILE C 48 ? 0.42815 0.61056 0.50975 0.02944  0.04515  0.06190  45 ILE C C   
1636 O O   . ILE C 48 ? 0.37120 0.54092 0.46191 0.03075  0.05034  0.05256  45 ILE C O   
1637 C CB  . ILE C 48 ? 0.45467 0.64057 0.50805 0.02372  0.04730  0.09411  45 ILE C CB  
1638 C CG1 . ILE C 48 ? 0.40580 0.57204 0.45362 0.02615  0.04424  0.11908  45 ILE C CG1 
1639 C CG2 . ILE C 48 ? 0.38454 0.57595 0.43964 0.01662  0.06039  0.08272  45 ILE C CG2 
1640 C CD1 . ILE C 48 ? 0.52102 0.69253 0.54216 0.01292  0.04699  0.13492  45 ILE C CD1 
1641 N N   . LEU C 49 ? 0.33348 0.52880 0.40622 0.02506  0.03602  0.05287  46 LEU C N   
1642 C CA  . LEU C 49 ? 0.40007 0.58781 0.47277 0.02393  0.03398  0.02997  46 LEU C CA  
1643 C C   . LEU C 49 ? 0.33709 0.50940 0.43333 0.02534  0.03078  0.03000  46 LEU C C   
1644 O O   . LEU C 49 ? 0.30572 0.46144 0.40660 0.02808  0.03238  0.01727  46 LEU C O   
1645 C CB  . LEU C 49 ? 0.36203 0.55360 0.41096 0.01659  0.02002  0.01904  46 LEU C CB  
1646 C CG  . LEU C 49 ? 0.39775 0.59671 0.40577 0.01605  0.02632  0.00975  46 LEU C CG  
1647 C CD1 . LEU C 49 ? 0.42934 0.61484 0.40398 0.00943  0.00899  -0.00977 46 LEU C CD1 
1648 C CD2 . LEU C 49 ? 0.40925 0.61161 0.42038 0.02546  0.04908  -0.00256 46 LEU C CD2 
1649 N N   . LEU C 50 ? 0.32162 0.50146 0.43373 0.02468  0.02717  0.04639  47 LEU C N   
1650 C CA  . LEU C 50 ? 0.33564 0.50440 0.46499 0.02505  0.02998  0.04997  47 LEU C CA  
1651 C C   . LEU C 50 ? 0.25805 0.40230 0.38037 0.03360  0.04146  0.04909  47 LEU C C   
1652 O O   . LEU C 50 ? 0.27081 0.39452 0.39149 0.03217  0.04069  0.04354  47 LEU C O   
1653 C CB  . LEU C 50 ? 0.22467 0.41786 0.37874 0.02605  0.03053  0.07009  47 LEU C CB  
1654 C CG  . LEU C 50 ? 0.44817 0.66238 0.62201 0.00973  0.01373  0.07350  47 LEU C CG  
1655 C CD1 . LEU C 50 ? 0.43625 0.62768 0.61117 -0.00141 0.01162  0.06587  47 LEU C CD1 
1656 C CD2 . LEU C 50 ? 0.47256 0.69026 0.62547 0.00027  -0.00565 0.06273  47 LEU C CD2 
1657 N N   . LEU C 51 ? 0.31771 0.45823 0.43198 0.04019  0.04802  0.05583  48 LEU C N   
1658 C CA  . LEU C 51 ? 0.42555 0.53681 0.52838 0.04380  0.05234  0.05416  48 LEU C CA  
1659 C C   . LEU C 51 ? 0.30375 0.41232 0.40882 0.03845  0.04662  0.04114  48 LEU C C   
1660 O O   . LEU C 51 ? 0.39691 0.48255 0.49771 0.03841  0.04238  0.03830  48 LEU C O   
1661 C CB  . LEU C 51 ? 0.29059 0.39035 0.38317 0.04869  0.05627  0.06515  48 LEU C CB  
1662 C CG  . LEU C 51 ? 0.40350 0.50044 0.49756 0.06279  0.06381  0.07774  48 LEU C CG  
1663 C CD1 . LEU C 51 ? 0.51965 0.59220 0.59967 0.06981  0.06423  0.08770  48 LEU C CD1 
1664 C CD2 . LEU C 51 ? 0.44769 0.52487 0.53374 0.07084  0.07370  0.07508  48 LEU C CD2 
1665 N N   . ILE C 52 ? 0.39257 0.52506 0.50320 0.03569  0.04636  0.03340  49 ILE C N   
1666 C CA  . ILE C 52 ? 0.37968 0.51727 0.50140 0.03719  0.04483  0.01955  49 ILE C CA  
1667 C C   . ILE C 52 ? 0.37796 0.49638 0.50291 0.04038  0.03556  0.00915  49 ILE C C   
1668 O O   . ILE C 52 ? 0.33599 0.44213 0.47145 0.04451  0.02884  0.00419  49 ILE C O   
1669 C CB  . ILE C 52 ? 0.39874 0.56557 0.51766 0.03762  0.05337  0.01200  49 ILE C CB  
1670 C CG1 . ILE C 52 ? 0.42499 0.61178 0.55210 0.03231  0.06307  0.02269  49 ILE C CG1 
1671 C CG2 . ILE C 52 ? 0.38173 0.54955 0.50718 0.04695  0.05277  -0.00942 49 ILE C CG2 
1672 C CD1 . ILE C 52 ? 0.47387 0.64850 0.58855 0.02437  0.06190  0.04323  49 ILE C CD1 
1673 N N   . HIS C 53 ? 0.42377 0.53836 0.54194 0.03640  0.03161  0.00891  50 HIS C N   
1674 C CA  . HIS C 53 ? 0.35668 0.44612 0.47584 0.03378  0.02132  0.00533  50 HIS C CA  
1675 C C   . HIS C 53 ? 0.39654 0.46385 0.51113 0.03331  0.02136  0.01750  50 HIS C C   
1676 O O   . HIS C 53 ? 0.28661 0.32761 0.39891 0.03363  0.01132  0.01535  50 HIS C O   
1677 C CB  . HIS C 53 ? 0.33930 0.43376 0.45745 0.02265  0.01537  0.00903  50 HIS C CB  
1678 C CG  . HIS C 53 ? 0.36950 0.43610 0.48926 0.01348  0.00355  0.00969  50 HIS C CG  
1679 N ND1 . HIS C 53 ? 0.43514 0.47220 0.54886 0.01502  -0.00989 -0.00786 50 HIS C ND1 
1680 C CD2 . HIS C 53 ? 0.36727 0.42890 0.49282 0.00248  0.00436  0.02759  50 HIS C CD2 
1681 C CE1 . HIS C 53 ? 0.49684 0.50603 0.61133 0.00230  -0.02103 0.00080  50 HIS C CE1 
1682 N NE2 . HIS C 53 ? 0.36144 0.38928 0.48382 -0.00720 -0.01105 0.02371  50 HIS C NE2 
1683 N N   . PHE C 54 ? 0.38910 0.46050 0.49590 0.03415  0.03165  0.02998  51 PHE C N   
1684 C CA  . PHE C 54 ? 0.44974 0.49268 0.53693 0.03564  0.03375  0.03795  51 PHE C CA  
1685 C C   . PHE C 54 ? 0.37250 0.39636 0.45527 0.03719  0.02102  0.03181  51 PHE C C   
1686 O O   . PHE C 54 ? 0.37521 0.36922 0.44110 0.03582  0.01121  0.03448  51 PHE C O   
1687 C CB  . PHE C 54 ? 0.39955 0.44336 0.47439 0.04176  0.04829  0.04748  51 PHE C CB  
1688 C CG  . PHE C 54 ? 0.34382 0.34874 0.38317 0.04581  0.05203  0.05070  51 PHE C CG  
1689 C CD1 . PHE C 54 ? 0.38774 0.36497 0.40762 0.04533  0.04160  0.04572  51 PHE C CD1 
1690 C CD2 . PHE C 54 ? 0.41831 0.41383 0.44049 0.04788  0.06546  0.05942  51 PHE C CD2 
1691 C CE1 . PHE C 54 ? 0.45038 0.38200 0.42483 0.04742  0.04040  0.04588  51 PHE C CE1 
1692 C CE2 . PHE C 54 ? 0.49190 0.44574 0.46676 0.05281  0.07103  0.06021  51 PHE C CE2 
1693 C CZ  . PHE C 54 ? 0.41385 0.33095 0.35992 0.05289  0.05646  0.05167  51 PHE C CZ  
1694 N N   . LEU C 55 ? 0.35072 0.39429 0.44966 0.03825  0.01991  0.02693  52 LEU C N   
1695 C CA  . LEU C 55 ? 0.45591 0.49412 0.56495 0.03729  0.00594  0.02478  52 LEU C CA  
1696 C C   . LEU C 55 ? 0.41416 0.45278 0.54370 0.04355  -0.00671 0.01692  52 LEU C C   
1697 O O   . LEU C 55 ? 0.45276 0.47401 0.58451 0.04392  -0.02497 0.01966  52 LEU C O   
1698 C CB  . LEU C 55 ? 0.47652 0.54581 0.60696 0.03362  0.01110  0.02574  52 LEU C CB  
1699 C CG  . LEU C 55 ? 0.50223 0.55911 0.61090 0.02789  0.01841  0.03548  52 LEU C CG  
1700 C CD1 . LEU C 55 ? 0.49942 0.58803 0.62822 0.02052  0.02471  0.04083  52 LEU C CD1 
1701 C CD2 . LEU C 55 ? 0.44056 0.45105 0.51906 0.02314  0.00569  0.03928  52 LEU C CD2 
1702 N N   . LEU C 56 ? 0.44261 0.49475 0.58384 0.04924  -0.00072 0.00699  53 LEU C N   
1703 C CA  . LEU C 56 ? 0.32839 0.36721 0.48366 0.05898  -0.01337 -0.00235 53 LEU C CA  
1704 C C   . LEU C 56 ? 0.41671 0.41072 0.54791 0.05346  -0.02775 0.00769  53 LEU C C   
1705 O O   . LEU C 56 ? 0.39814 0.37088 0.53501 0.05929  -0.04684 0.01002  53 LEU C O   
1706 C CB  . LEU C 56 ? 0.39063 0.43816 0.54844 0.06459  -0.00543 -0.01801 53 LEU C CB  
1707 C CG  . LEU C 56 ? 0.33851 0.42854 0.50927 0.07087  0.01164  -0.02790 53 LEU C CG  
1708 C CD1 . LEU C 56 ? 0.33940 0.42658 0.49117 0.07245  0.01713  -0.04352 53 LEU C CD1 
1709 C CD2 . LEU C 56 ? 0.36927 0.48326 0.57730 0.08684  0.01206  -0.03451 53 LEU C CD2 
1710 N N   . LEU C 57 ? 0.37778 0.36050 0.48397 0.04212  -0.01858 0.01671  54 LEU C N   
1711 C CA  . LEU C 57 ? 0.41802 0.36295 0.49756 0.03365  -0.02584 0.03047  54 LEU C CA  
1712 C C   . LEU C 57 ? 0.43199 0.35232 0.48556 0.03359  -0.03587 0.03980  54 LEU C C   
1713 O O   . LEU C 57 ? 0.51976 0.40418 0.55544 0.03171  -0.05365 0.04825  54 LEU C O   
1714 C CB  . LEU C 57 ? 0.37771 0.33205 0.44486 0.02215  -0.00750 0.04162  54 LEU C CB  
1715 C CG  . LEU C 57 ? 0.45169 0.42179 0.53859 0.01442  -0.00655 0.03748  54 LEU C CG  
1716 C CD1 . LEU C 57 ? 0.41519 0.41019 0.50376 0.00406  0.01101  0.05312  54 LEU C CD1 
1717 C CD2 . LEU C 57 ? 0.41121 0.34283 0.49610 0.00780  -0.02567 0.03745  54 LEU C CD2 
1718 N N   . SER C 58 ? 0.36751 0.29958 0.41284 0.03404  -0.02829 0.03917  55 SER C N   
1719 C CA  . SER C 58 ? 0.55257 0.45210 0.55979 0.03065  -0.03969 0.04585  55 SER C CA  
1720 C C   . SER C 58 ? 0.50096 0.40307 0.53256 0.03282  -0.06774 0.04296  55 SER C C   
1721 O O   . SER C 58 ? 0.60089 0.47045 0.61154 0.03070  -0.09246 0.05047  55 SER C O   
1722 C CB  . SER C 58 ? 0.38167 0.28080 0.36407 0.02996  -0.02140 0.04536  55 SER C CB  
1723 O OG  . SER C 58 ? 0.47140 0.40856 0.49143 0.03225  -0.01377 0.03854  55 SER C OG  
1724 N N   . LEU C 59 ? 0.54617 0.49058 0.62394 0.03616  -0.06471 0.03508  56 LEU C N   
1725 C CA  . LEU C 59 ? 0.49996 0.46241 0.61498 0.03656  -0.08836 0.03590  56 LEU C CA  
1726 C C   . LEU C 59 ? 0.46980 0.44863 0.63027 0.05211  -0.10079 0.03219  56 LEU C C   
1727 O O   . LEU C 59 ? 0.50679 0.47943 0.68452 0.05507  -0.13024 0.03904  56 LEU C O   
1728 C CB  . LEU C 59 ? 0.46257 0.46871 0.61150 0.03158  -0.07615 0.03331  56 LEU C CB  
1729 C CG  . LEU C 59 ? 0.53124 0.51398 0.63858 0.01891  -0.06730 0.03676  56 LEU C CG  
1730 C CD1 . LEU C 59 ? 0.63082 0.65557 0.77222 0.01335  -0.05279 0.03756  56 LEU C CD1 
1731 C CD2 . LEU C 59 ? 0.69729 0.63523 0.76819 0.00638  -0.09594 0.04254  56 LEU C CD2 
1732 N N   . VAL C 60 ? 0.43556 0.43138 0.61424 0.06351  -0.08165 0.02089  57 VAL C N   
1733 C CA  . VAL C 60 ? 0.44940 0.45475 0.66929 0.08393  -0.09052 0.01239  57 VAL C CA  
1734 C C   . VAL C 60 ? 0.44512 0.39392 0.63621 0.08637  -0.10944 0.01823  57 VAL C C   
1735 O O   . VAL C 60 ? 0.46259 0.39631 0.67339 0.09851  -0.13606 0.02350  57 VAL C O   
1736 C CB  . VAL C 60 ? 0.41201 0.45052 0.65279 0.09554  -0.06340 -0.00593 57 VAL C CB  
1737 C CG1 . VAL C 60 ? 0.40987 0.45649 0.69219 0.12321  -0.06891 -0.01930 57 VAL C CG1 
1738 C CG2 . VAL C 60 ? 0.49361 0.58332 0.75187 0.08801  -0.04318 -0.00568 57 VAL C CG2 
1739 N N   . LYS C 61 ? 0.45491 0.37378 0.60309 0.07393  -0.09738 0.02073  58 LYS C N   
1740 C CA  . LYS C 61 ? 0.47271 0.33731 0.59165 0.06986  -0.11307 0.03110  58 LYS C CA  
1741 C C   . LYS C 61 ? 0.53934 0.36760 0.61242 0.05669  -0.12961 0.05237  58 LYS C C   
1742 O O   . LYS C 61 ? 0.59483 0.37593 0.64315 0.05362  -0.14860 0.06610  58 LYS C O   
1743 C CB  . LYS C 61 ? 0.49125 0.34564 0.58936 0.05669  -0.09434 0.02971  58 LYS C CB  
1744 C CG  . LYS C 61 ? 0.44600 0.32014 0.57194 0.06723  -0.08410 0.00740  58 LYS C CG  
1745 C CD  . LYS C 61 ? 0.61075 0.46061 0.76120 0.09031  -0.10313 -0.00501 58 LYS C CD  
1746 C CE  . LYS C 61 ? 0.62998 0.48572 0.79120 0.10240  -0.09178 -0.03147 58 LYS C CE  
1747 N NZ  . LYS C 61 ? 0.64658 0.46596 0.82547 0.12996  -0.10878 -0.04624 58 LYS C NZ  
1748 N N   . GLY C 62 ? 0.45837 0.29986 0.51184 0.04821  -0.12403 0.05546  59 GLY C N   
1749 C CA  . GLY C 62 ? 0.55297 0.35206 0.54749 0.03642  -0.13904 0.07164  59 GLY C CA  
1750 C C   . GLY C 62 ? 0.59109 0.35516 0.52783 0.02326  -0.12174 0.08502  59 GLY C C   
1751 O O   . GLY C 62 ? 0.71529 0.43427 0.59574 0.01498  -0.13588 0.10116  59 GLY C O   
1752 N N   . LEU C 63 ? 0.50982 0.29657 0.45924 0.01974  -0.09194 0.08103  60 LEU C N   
1753 C CA  . LEU C 63 ? 0.58213 0.35106 0.49098 0.00552  -0.07139 0.09729  60 LEU C CA  
1754 C C   . LEU C 63 ? 0.55846 0.32293 0.41552 0.00328  -0.04973 0.10070  60 LEU C C   
1755 O O   . LEU C 63 ? 0.53280 0.31527 0.39593 0.01101  -0.04398 0.08711  60 LEU C O   
1756 C CB  . LEU C 63 ? 0.50174 0.30376 0.44910 0.00065  -0.05080 0.09339  60 LEU C CB  
1757 C CG  . LEU C 63 ? 0.54724 0.34357 0.53577 0.00490  -0.07074 0.08352  60 LEU C CG  
1758 C CD1 . LEU C 63 ? 0.55935 0.38043 0.57357 -0.00526 -0.05568 0.07965  60 LEU C CD1 
1759 C CD2 . LEU C 63 ? 0.57647 0.31663 0.54351 0.00013  -0.09777 0.09920  60 LEU C CD2 
1760 N N   . SER C 64 ? 0.62099 0.35678 0.42269 -0.00710 -0.03653 0.11947  61 SER C N   
1761 C CA  . SER C 64 ? 0.69425 0.41785 0.43559 -0.00446 -0.01134 0.12040  61 SER C CA  
1762 C C   . SER C 64 ? 0.67258 0.44485 0.44788 0.00464  0.02434  0.11068  61 SER C C   
1763 O O   . SER C 64 ? 0.62333 0.43864 0.46029 0.00257  0.03130  0.10993  61 SER C O   
1764 C CB  . SER C 64 ? 0.77776 0.46896 0.45399 -0.01651 0.00412  0.14450  61 SER C CB  
1765 O OG  . SER C 64 ? 0.72438 0.44989 0.43767 -0.02762 0.02911  0.16028  61 SER C OG  
1766 N N   . PRO C 65 ? 0.63023 0.39072 0.36274 0.01586  0.04372  0.10249  62 PRO C N   
1767 C CA  . PRO C 65 ? 0.74355 0.54670 0.50803 0.02863  0.07724  0.09669  62 PRO C CA  
1768 C C   . PRO C 65 ? 0.66295 0.50920 0.45711 0.02379  0.10900  0.11516  62 PRO C C   
1769 O O   . PRO C 65 ? 0.56876 0.46687 0.42395 0.02788  0.12105  0.11443  62 PRO C O   
1770 C CB  . PRO C 65 ? 0.83435 0.59560 0.52766 0.04335  0.09161  0.08611  62 PRO C CB  
1771 C CG  . PRO C 65 ? 0.82021 0.52580 0.46566 0.03473  0.05150  0.07926  62 PRO C CG  
1772 C CD  . PRO C 65 ? 0.81952 0.52174 0.47341 0.01869  0.02973  0.09569  62 PRO C CD  
1773 N N   . GLU C 66 ? 0.63649 0.46439 0.39013 0.01224  0.12051  0.13479  63 GLU C N   
1774 C CA  . GLU C 66 ? 0.68869 0.56365 0.47694 0.00183  0.15103  0.15781  63 GLU C CA  
1775 C C   . GLU C 66 ? 0.66918 0.57049 0.52659 -0.01891 0.12645  0.16499  63 GLU C C   
1776 O O   . GLU C 66 ? 0.63345 0.59062 0.55185 -0.02516 0.14045  0.17378  63 GLU C O   
1777 C CB  . GLU C 66 ? 0.74663 0.59229 0.46588 -0.00830 0.17206  0.18038  63 GLU C CB  
1778 C CG  . GLU C 66 ? 0.98778 0.88805 0.74860 -0.02507 0.20459  0.21042  63 GLU C CG  
1779 C CD  . GLU C 66 ? 1.10306 1.07597 0.92414 -0.00676 0.24164  0.20876  63 GLU C CD  
1780 O OE1 . GLU C 66 ? 1.07995 1.04715 0.86345 0.02267  0.27078  0.19550  63 GLU C OE1 
1781 O OE2 . GLU C 66 ? 0.91558 0.94698 0.82027 -0.02096 0.23821  0.22028  63 GLU C OE2 
1782 N N   . THR C 67 ? 0.60608 0.46522 0.45430 -0.02872 0.08762  0.16107  64 THR C N   
1783 C CA  . THR C 67 ? 0.55737 0.42729 0.46173 -0.04332 0.06254  0.16100  64 THR C CA  
1784 C C   . THR C 67 ? 0.54764 0.45531 0.50501 -0.03083 0.05624  0.13770  64 THR C C   
1785 O O   . THR C 67 ? 0.50247 0.44134 0.50846 -0.04158 0.05233  0.13853  64 THR C O   
1786 C CB  . THR C 67 ? 0.59050 0.40195 0.47143 -0.04861 0.02407  0.16074  64 THR C CB  
1787 O OG1 . THR C 67 ? 0.66343 0.43725 0.49151 -0.06468 0.02785  0.18818  64 THR C OG1 
1788 C CG2 . THR C 67 ? 0.61976 0.43064 0.55164 -0.05702 -0.00169 0.15371  64 THR C CG2 
1789 N N   . THR C 68 ? 0.49539 0.39778 0.43952 -0.01120 0.05331  0.11850  65 THR C N   
1790 C CA  . THR C 68 ? 0.46890 0.40661 0.45501 -0.00052 0.05128  0.10065  65 THR C CA  
1791 C C   . THR C 68 ? 0.50341 0.49200 0.52030 0.00137  0.07796  0.10877  65 THR C C   
1792 O O   . THR C 68 ? 0.42278 0.44599 0.48406 -0.00309 0.07150  0.10521  65 THR C O   
1793 C CB  . THR C 68 ? 0.48258 0.40307 0.44638 0.01501  0.04477  0.08503  65 THR C CB  
1794 O OG1 . THR C 68 ? 0.52435 0.40788 0.47216 0.01320  0.01613  0.08059  65 THR C OG1 
1795 C CG2 . THR C 68 ? 0.48763 0.44307 0.49080 0.02281  0.04382  0.07127  65 THR C CG2 
1796 N N   . LYS C 69 ? 0.51681 0.51015 0.50892 0.01000  0.10760  0.11964  66 LYS C N   
1797 C CA  . LYS C 69 ? 0.47018 0.51896 0.50123 0.01652  0.13489  0.13085  66 LYS C CA  
1798 C C   . LYS C 69 ? 0.43795 0.52688 0.51973 -0.00790 0.13165  0.14979  66 LYS C C   
1799 O O   . LYS C 69 ? 0.43180 0.57152 0.56772 -0.00970 0.13068  0.15377  66 LYS C O   
1800 C CB  . LYS C 69 ? 0.50551 0.54862 0.49689 0.03380  0.17224  0.13881  66 LYS C CB  
1801 C CG  . LYS C 69 ? 0.52178 0.63028 0.56268 0.04571  0.20522  0.15396  66 LYS C CG  
1802 C CD  . LYS C 69 ? 0.72655 0.82076 0.72180 0.07580  0.24449  0.15176  66 LYS C CD  
1803 C CE  . LYS C 69 ? 0.64368 0.69719 0.56771 0.06847  0.26221  0.15979  66 LYS C CE  
1804 N NZ  . LYS C 69 ? 0.92560 0.95169 0.78688 0.10090  0.30074  0.15117  66 LYS C NZ  
1805 N N   . LEU C 70 ? 0.48978 0.55245 0.55316 -0.02959 0.12531  0.16350  67 LEU C N   
1806 C CA  . LEU C 70 ? 0.57314 0.66336 0.68176 -0.05947 0.11711  0.18339  67 LEU C CA  
1807 C C   . LEU C 70 ? 0.47279 0.56283 0.61499 -0.06870 0.08115  0.16629  67 LEU C C   
1808 O O   . LEU C 70 ? 0.38221 0.51801 0.57528 -0.08257 0.07537  0.17412  67 LEU C O   
1809 C CB  . LEU C 70 ? 0.54733 0.59285 0.61910 -0.08186 0.11279  0.20205  67 LEU C CB  
1810 C CG  . LEU C 70 ? 0.60580 0.67131 0.71393 -0.11941 0.11013  0.23229  67 LEU C CG  
1811 C CD1 . LEU C 70 ? 0.58155 0.61147 0.70797 -0.14007 0.06458  0.22130  67 LEU C CD1 
1812 C CD2 . LEU C 70 ? 0.59716 0.75015 0.77067 -0.12377 0.13799  0.25163  67 LEU C CD2 
1813 N N   . LEU C 71 ? 0.43331 0.47396 0.54679 -0.06010 0.05664  0.14268  68 LEU C N   
1814 C CA  . LEU C 71 ? 0.37826 0.41398 0.51224 -0.06405 0.02805  0.12270  68 LEU C CA  
1815 C C   . LEU C 71 ? 0.37428 0.45525 0.53230 -0.04978 0.03333  0.11158  68 LEU C C   
1816 O O   . LEU C 71 ? 0.41003 0.50506 0.58965 -0.05950 0.01491  0.10361  68 LEU C O   
1817 C CB  . LEU C 71 ? 0.40281 0.38343 0.50659 -0.05255 0.00700  0.10149  68 LEU C CB  
1818 C CG  . LEU C 71 ? 0.54216 0.46808 0.62562 -0.06742 -0.01046 0.11179  68 LEU C CG  
1819 C CD1 . LEU C 71 ? 0.54017 0.42050 0.60671 -0.04919 -0.03270 0.09049  68 LEU C CD1 
1820 C CD2 . LEU C 71 ? 0.54032 0.46104 0.64711 -0.09690 -0.02657 0.12164  68 LEU C CD2 
1821 N N   . MET C 72 ? 0.39167 0.48804 0.53948 -0.02757 0.05538  0.11105  69 MET C N   
1822 C CA  . MET C 72 ? 0.35310 0.48854 0.52314 -0.01454 0.05958  0.10641  69 MET C CA  
1823 C C   . MET C 72 ? 0.34625 0.53829 0.56546 -0.02583 0.06408  0.12705  69 MET C C   
1824 O O   . MET C 72 ? 0.31036 0.52960 0.55415 -0.03026 0.04742  0.12415  69 MET C O   
1825 C CB  . MET C 72 ? 0.36437 0.49280 0.51061 0.01067  0.08027  0.10337  69 MET C CB  
1826 C CG  . MET C 72 ? 0.39615 0.48100 0.50616 0.01935  0.06976  0.08429  69 MET C CG  
1827 S SD  . MET C 72 ? 0.41758 0.50926 0.53980 0.01814  0.04818  0.06520  69 MET C SD  
1828 C CE  . MET C 72 ? 0.35128 0.48632 0.49574 0.02645  0.05638  0.07374  69 MET C CE  
1829 N N   . LYS C 73 ? 0.42572 0.63948 0.66040 -0.03170 0.08593  0.15001  70 LYS C N   
1830 C CA  . LYS C 73 ? 0.39912 0.68004 0.69566 -0.04365 0.09110  0.17437  70 LYS C CA  
1831 C C   . LYS C 73 ? 0.33061 0.61466 0.65362 -0.08018 0.05660  0.17828  70 LYS C C   
1832 O O   . LYS C 73 ? 0.40124 0.73889 0.77694 -0.09325 0.04380  0.19197  70 LYS C O   
1833 C CB  . LYS C 73 ? 0.40460 0.71352 0.71247 -0.04073 0.12933  0.19957  70 LYS C CB  
1834 C CG  . LYS C 73 ? 0.35506 0.65810 0.63320 -0.00176 0.16402  0.19355  70 LYS C CG  
1835 C CD  . LYS C 73 ? 0.55021 0.88666 0.83837 0.00589  0.20406  0.21447  70 LYS C CD  
1836 C CE  . LYS C 73 ? 0.60591 0.91641 0.84823 0.04698  0.23307  0.19981  70 LYS C CE  
1837 N NZ  . LYS C 73 ? 0.76026 1.09708 1.00635 0.05909  0.26568  0.20973  70 LYS C NZ  
1838 N N   . GLU C 74 ? 0.35747 0.58061 0.64403 -0.09647 0.03751  0.16630  71 GLU C N   
1839 C CA  . GLU C 74 ? 0.43800 0.64465 0.73737 -0.12939 0.00087  0.16406  71 GLU C CA  
1840 C C   . GLU C 74 ? 0.47502 0.67393 0.76361 -0.12293 -0.02588 0.13751  71 GLU C C   
1841 O O   . GLU C 74 ? 0.52440 0.74047 0.83680 -0.14647 -0.05375 0.14014  71 GLU C O   
1842 C CB  . GLU C 74 ? 0.43591 0.56981 0.69602 -0.14297 -0.01189 0.15833  71 GLU C CB  
1843 C CG  . GLU C 74 ? 0.63439 0.77518 0.91058 -0.17000 0.00034  0.19265  71 GLU C CG  
1844 C CD  . GLU C 74 ? 0.63147 0.82619 0.97026 -0.20666 -0.01231 0.21833  71 GLU C CD  
1845 O OE1 . GLU C 74 ? 0.63045 0.79664 0.97268 -0.23142 -0.05250 0.20741  71 GLU C OE1 
1846 O OE2 . GLU C 74 ? 0.81399 1.08033 1.19924 -0.21006 0.01735  0.24890  71 GLU C OE2 
1847 N N   . LEU C 75 ? 0.40133 0.57495 0.65171 -0.09368 -0.01866 0.11334  72 LEU C N   
1848 C CA  . LEU C 75 ? 0.40929 0.57972 0.64314 -0.08642 -0.03697 0.09078  72 LEU C CA  
1849 C C   . LEU C 75 ? 0.40053 0.63299 0.66872 -0.08336 -0.03665 0.10600  72 LEU C C   
1850 O O   . LEU C 75 ? 0.43733 0.67753 0.70287 -0.09414 -0.06286 0.09901  72 LEU C O   
1851 C CB  . LEU C 75 ? 0.49737 0.63622 0.69133 -0.05860 -0.02525 0.06752  72 LEU C CB  
1852 C CG  . LEU C 75 ? 0.50220 0.63150 0.66920 -0.05149 -0.03882 0.04294  72 LEU C CG  
1853 C CD1 . LEU C 75 ? 0.50013 0.59909 0.65313 -0.07289 -0.06918 0.02849  72 LEU C CD1 
1854 C CD2 . LEU C 75 ? 0.51904 0.62099 0.65816 -0.02871 -0.02612 0.02338  72 LEU C CD2 
1855 N N   . ILE C 76 ? 0.31412 0.58693 0.61040 -0.06664 -0.00862 0.12641  73 ILE C N   
1856 C CA  . ILE C 76 ? 0.42821 0.76277 0.76825 -0.05994 -0.00898 0.14542  73 ILE C CA  
1857 C C   . ILE C 76 ? 0.33179 0.71032 0.72530 -0.09222 -0.03294 0.16635  73 ILE C C   
1858 O O   . ILE C 76 ? 0.46927 0.88239 0.88619 -0.09953 -0.05878 0.17309  73 ILE C O   
1859 C CB  . ILE C 76 ? 0.39865 0.75961 0.75674 -0.03055 0.02917  0.16078  73 ILE C CB  
1860 C CG1 . ILE C 76 ? 0.39041 0.70519 0.69567 -0.00374 0.04329  0.14069  73 ILE C CG1 
1861 C CG2 . ILE C 76 ? 0.38336 0.81292 0.80021 -0.01992 0.02908  0.18444  73 ILE C CG2 
1862 C CD1 . ILE C 76 ? 0.35244 0.66980 0.65664 0.02441  0.07814  0.14911  73 ILE C CD1 
1863 N N   . LYS C 77 ? 0.29371 0.67059 0.70652 -0.11531 -0.02802 0.17960  74 LYS C N   
1864 C CA  . LYS C 77 ? 0.40591 0.82037 0.87201 -0.15474 -0.05493 0.20151  74 LYS C CA  
1865 C C   . LYS C 77 ? 0.50885 0.88331 0.94359 -0.17929 -0.10428 0.17980  74 LYS C C   
1866 O O   . LYS C 77 ? 0.46317 0.87794 0.93663 -0.20306 -0.13704 0.19332  74 LYS C O   
1867 C CB  . LYS C 77 ? 0.33853 0.74091 0.81615 -0.17935 -0.04172 0.21874  74 LYS C CB  
1868 C CG  . LYS C 77 ? 0.59950 1.01787 1.11443 -0.22170 -0.07132 0.23669  74 LYS C CG  
1869 C CD  . LYS C 77 ? 0.58852 1.08314 1.15960 -0.21150 -0.06048 0.25940  74 LYS C CD  
1870 C CE  . LYS C 77 ? 0.51318 1.02134 1.11813 -0.25283 -0.09346 0.27561  74 LYS C CE  
1871 N NZ  . LYS C 77 ? 0.44791 1.03678 1.11771 -0.24327 -0.08225 0.30094  74 LYS C NZ  
1872 N N   . GLU C 78 ? 0.43707 0.73256 0.80072 -0.17249 -0.11089 0.14566  75 GLU C N   
1873 C CA  . GLU C 78 ? 0.61900 0.86614 0.93747 -0.18855 -0.15151 0.11847  75 GLU C CA  
1874 C C   . GLU C 78 ? 0.68183 0.94567 0.97535 -0.16930 -0.15960 0.10619  75 GLU C C   
1875 O O   . GLU C 78 ? 0.80619 1.03484 1.05494 -0.18204 -0.19260 0.08439  75 GLU C O   
1876 C CB  . GLU C 78 ? 0.63459 0.79481 0.89052 -0.18143 -0.15072 0.08632  75 GLU C CB  
1877 C CG  . GLU C 78 ? 0.63577 0.76097 0.90395 -0.20707 -0.15549 0.09830  75 GLU C CG  
1878 C CD  . GLU C 78 ? 0.77052 0.81912 0.98730 -0.18783 -0.14687 0.07302  75 GLU C CD  
1879 O OE1 . GLU C 78 ? 0.71286 0.75872 0.90390 -0.15182 -0.12380 0.05575  75 GLU C OE1 
1880 O OE2 . GLU C 78 ? 0.99881 0.99025 1.20466 -0.20948 -0.16548 0.07269  75 GLU C OE2 
1881 N N   . LEU C 79 ? 0.51303 0.82218 0.82673 -0.13935 -0.13117 0.11950  76 LEU C N   
1882 C CA  . LEU C 79 ? 0.64823 0.97210 0.93890 -0.12391 -0.14069 0.11476  76 LEU C CA  
1883 C C   . LEU C 79 ? 0.66143 1.04308 0.99958 -0.14358 -0.17478 0.14020  76 LEU C C   
1884 O O   . LEU C 79 ? 0.62828 0.99589 0.92837 -0.15624 -0.21035 0.12967  76 LEU C O   
1885 C CB  . LEU C 79 ? 0.59681 0.93619 0.88881 -0.08637 -0.10277 0.12067  76 LEU C CB  
1886 C CG  . LEU C 79 ? 0.61068 0.89651 0.84721 -0.06637 -0.07884 0.09405  76 LEU C CG  
1887 C CD1 . LEU C 79 ? 0.63949 0.93845 0.87032 -0.03773 -0.05668 0.10099  76 LEU C CD1 
1888 C CD2 . LEU C 79 ? 0.46497 0.70232 0.64076 -0.07537 -0.09848 0.06283  76 LEU C CD2 
1889 N N   . GLU C 80 ? 0.76472 1.21439 1.18570 -0.14515 -0.16419 0.17468  77 GLU C N   
1890 C CA  . GLU C 80 ? 0.90553 1.41193 1.38028 -0.16181 -0.19507 0.20029  77 GLU C CA  
1891 C C   . GLU C 80 ? 0.86406 1.33922 1.32195 -0.20653 -0.24024 0.19131  77 GLU C C   
1892 O O   . GLU C 80 ? 0.97734 1.46770 1.44139 -0.22069 -0.27439 0.19919  77 GLU C O   
1893 C CB  . GLU C 80 ? 0.79258 1.35101 1.33591 -0.14530 -0.15915 0.22810  77 GLU C CB  
1894 C CG  . GLU C 80 ? 0.75697 1.30675 1.31787 -0.16161 -0.13629 0.23267  77 GLU C CG  
1895 C CD  . GLU C 80 ? 0.84722 1.44674 1.46139 -0.14066 -0.09542 0.25703  77 GLU C CD  
1896 O OE1 . GLU C 80 ? 0.91017 1.53837 1.54017 -0.10475 -0.07650 0.26396  77 GLU C OE1 
1897 O OE2 . GLU C 80 ? 0.85277 1.45846 1.48862 -0.16002 -0.08282 0.26878  77 GLU C OE2 
1898 N N   . LYS C 81 ? 0.82647 1.25040 1.25943 -0.22858 -0.24270 0.17467  78 LYS C N   
1899 C CA  . LYS C 81 ? 0.91946 1.28963 1.31966 -0.26840 -0.28578 0.15961  78 LYS C CA  
1900 C C   . LYS C 81 ? 1.02371 1.30163 1.34373 -0.27044 -0.29049 0.11952  78 LYS C C   
1901 O O   . LYS C 81 ? 1.02040 1.25422 1.26476 -0.25077 -0.29371 0.08809  78 LYS C O   
1902 C CB  . LYS C 81 ? 1.07592 1.46690 1.53400 -0.29335 -0.28165 0.18577  78 LYS C CB  
1903 C CG  . LYS C 81 ? 1.12604 1.57401 1.63544 -0.30621 -0.30316 0.21208  78 LYS C CG  
1904 C CD  . LYS C 81 ? 1.08729 1.49223 1.54165 -0.32831 -0.35787 0.19173  78 LYS C CD  
1905 C CE  . LYS C 81 ? 1.06537 1.51468 1.57138 -0.35355 -0.38866 0.21853  78 LYS C CE  
1906 N NZ  . LYS C 81 ? 1.06241 1.44911 1.50323 -0.38388 -0.44455 0.19582  78 LYS C NZ  
# 
