data_2OOB
# 
_entry.id   2OOB 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.377 
_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   2OOB         pdb_00002oob 10.2210/pdb2oob/pdb 
RCSB  RCSB041383   ?            ?                   
WWPDB D_1000041383 ?            ?                   
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 2OO9 .           unspecified 
PDB 2OOA 'Cbl-b UBA' unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        2OOB 
_pdbx_database_status.recvd_initial_deposition_date   2007-01-25 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Kozlov, G.'  1 
'Gehring, K.' 2 
# 
_citation.id                        primary 
_citation.title                     
'Structural basis for ubiquitin-mediated dimerization and activation of the ubiquitin protein ligase Cbl-b.' 
_citation.journal_abbrev            Mol.Cell 
_citation.journal_volume            27 
_citation.page_first                474 
_citation.page_last                 485 
_citation.year                      2007 
_citation.journal_id_ASTM           MOCEFL 
_citation.country                   US 
_citation.journal_id_ISSN           1097-2765 
_citation.journal_id_CSD            2168 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   17679095 
_citation.pdbx_database_id_DOI      10.1016/j.molcel.2007.06.023 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Peschard, P.'   1 ? 
primary 'Kozlov, G.'     2 ? 
primary 'Lin, T.'        3 ? 
primary 'Mirza, I.A.'    4 ? 
primary 'Berghuis, A.M.' 5 ? 
primary 'Lipkowitz, S.'  6 ? 
primary 'Park, M.'       7 ? 
primary 'Gehring, K.'    8 ? 
# 
_cell.entry_id           2OOB 
_cell.length_a           50.608 
_cell.length_b           54.784 
_cell.length_c           94.621 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         2OOB 
_symmetry.space_group_name_H-M             'I 2 2 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                23 
_symmetry.space_group_name_Hall            ? 
# 
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 'E3 ubiquitin-protein ligase CBL-B' 5656.381 1   6.3.2.- ? 'UBA domain' ? 
2 polymer nat Ubiquitin                           8576.831 1   ?       ? ?            ? 
3 water   nat water                               18.015   134 ?       ? ?            ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'Signal transduction protein CBL-B, SH3-binding protein CBL-B, Casitas B-lineage lymphoma proto-oncogene b, RING finger protein 56' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no GSGPEAALENVDAKIAKLMGEGYAFEEVKRALEIAQNNVEVARSILREFAFP                         
GSGPEAALENVDAKIAKLMGEGYAFEEVKRALEIAQNNVEVARSILREFAFP                         A ? 
2 'polypeptide(L)' no no MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG 
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG B ? 
# 
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  SER n 
1 3  GLY n 
1 4  PRO n 
1 5  GLU n 
1 6  ALA n 
1 7  ALA n 
1 8  LEU n 
1 9  GLU n 
1 10 ASN n 
1 11 VAL n 
1 12 ASP n 
1 13 ALA n 
1 14 LYS n 
1 15 ILE n 
1 16 ALA n 
1 17 LYS n 
1 18 LEU n 
1 19 MET n 
1 20 GLY n 
1 21 GLU n 
1 22 GLY n 
1 23 TYR n 
1 24 ALA n 
1 25 PHE n 
1 26 GLU n 
1 27 GLU n 
1 28 VAL n 
1 29 LYS n 
1 30 ARG n 
1 31 ALA n 
1 32 LEU n 
1 33 GLU n 
1 34 ILE n 
1 35 ALA n 
1 36 GLN n 
1 37 ASN n 
1 38 ASN n 
1 39 VAL n 
1 40 GLU n 
1 41 VAL n 
1 42 ALA n 
1 43 ARG n 
1 44 SER n 
1 45 ILE n 
1 46 LEU n 
1 47 ARG n 
1 48 GLU n 
1 49 PHE n 
1 50 ALA n 
1 51 PHE n 
1 52 PRO n 
2 1  MET n 
2 2  GLN n 
2 3  ILE n 
2 4  PHE n 
2 5  VAL n 
2 6  LYS n 
2 7  THR n 
2 8  LEU n 
2 9  THR n 
2 10 GLY n 
2 11 LYS n 
2 12 THR n 
2 13 ILE n 
2 14 THR n 
2 15 LEU n 
2 16 GLU n 
2 17 VAL n 
2 18 GLU n 
2 19 PRO n 
2 20 SER n 
2 21 ASP n 
2 22 THR n 
2 23 ILE n 
2 24 GLU n 
2 25 ASN n 
2 26 VAL n 
2 27 LYS n 
2 28 ALA n 
2 29 LYS n 
2 30 ILE n 
2 31 GLN n 
2 32 ASP n 
2 33 LYS n 
2 34 GLU n 
2 35 GLY n 
2 36 ILE n 
2 37 PRO n 
2 38 PRO n 
2 39 ASP n 
2 40 GLN n 
2 41 GLN n 
2 42 ARG n 
2 43 LEU n 
2 44 ILE n 
2 45 PHE n 
2 46 ALA n 
2 47 GLY n 
2 48 LYS n 
2 49 GLN n 
2 50 LEU n 
2 51 GLU n 
2 52 ASP n 
2 53 GLY n 
2 54 ARG n 
2 55 THR n 
2 56 LEU n 
2 57 SER n 
2 58 ASP n 
2 59 TYR n 
2 60 ASN n 
2 61 ILE n 
2 62 GLN n 
2 63 LYS n 
2 64 GLU n 
2 65 SER n 
2 66 THR n 
2 67 LEU n 
2 68 HIS n 
2 69 LEU n 
2 70 VAL n 
2 71 LEU n 
2 72 ARG n 
2 73 LEU n 
2 74 ARG n 
2 75 GLY n 
2 76 GLY 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                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     Homo 
_entity_src_gen.pdbx_gene_src_gene                 'CBLB, RNF56' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     511693 
_entity_src_gen.host_org_genus                     Escherichia 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   'Escherichia coli' 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               BL21 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pGEX-4T-1 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_entity_src_nat.entity_id                  2 
_entity_src_nat.pdbx_src_id                1 
_entity_src_nat.pdbx_alt_source_flag       sample 
_entity_src_nat.pdbx_beg_seq_num           ? 
_entity_src_nat.pdbx_end_seq_num           ? 
_entity_src_nat.common_name                cattle 
_entity_src_nat.pdbx_organism_scientific   'Bos taurus' 
_entity_src_nat.pdbx_ncbi_taxonomy_id      9913 
_entity_src_nat.genus                      Bos 
_entity_src_nat.species                    ? 
_entity_src_nat.strain                     ? 
_entity_src_nat.tissue                     ? 
_entity_src_nat.tissue_fraction            ? 
_entity_src_nat.pdbx_secretion             ? 
_entity_src_nat.pdbx_fragment              ? 
_entity_src_nat.pdbx_variant               ? 
_entity_src_nat.pdbx_cell_line             ? 
_entity_src_nat.pdbx_atcc                  ? 
_entity_src_nat.pdbx_cellular_location     ? 
_entity_src_nat.pdbx_organ                 ? 
_entity_src_nat.pdbx_organelle             ? 
_entity_src_nat.pdbx_cell                  ? 
_entity_src_nat.pdbx_plasmid_name          ? 
_entity_src_nat.pdbx_plasmid_details       ? 
_entity_src_nat.details                    ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
_struct_ref.pdbx_db_isoform 
1 UNP CBLB_HUMAN Q13191 1 GPEAALENVDAKIAKLMGEGYAFEEVKRALEIAQNNVEVARSILREFAFP                           924 ? 
2 UNP UBIQ_BOVIN P62990 2 MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG 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 2OOB A 3 ? 52 ? Q13191 924 ? 973 ? 924 973 
2 2 2OOB B 1 ? 76 ? P62990 1   ? 76  ? 1   76  
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 2OOB GLY A 1 ? UNP Q13191 ? ? 'cloning artifact' 922 1 
1 2OOB SER A 2 ? UNP Q13191 ? ? 'cloning artifact' 923 2 
# 
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  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
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 
# 
_exptl.entry_id          2OOB 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.30 
_exptl_crystal.density_percent_sol   46.59 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              5.0 
_exptl_crystal_grow.pdbx_details    
'0.2M calcium chloride, 0.1M sodium acetate, 20% PEG6000, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K' 
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               'IMAGE PLATE' 
_diffrn_detector.type                   'RIGAKU RAXIS IV++' 
_diffrn_detector.pdbx_collection_date   2006-04-20 
_diffrn_detector.details                'Osmic multilayer confocal optics' 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    graphite 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.5418 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      'ROTATING ANODE' 
_diffrn_source.type                        RIGAKU 
_diffrn_source.pdbx_synchrotron_site       ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_wavelength             1.5418 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.entry_id                     2OOB 
_reflns.observed_criterion_sigma_F   1.0 
_reflns.observed_criterion_sigma_I   1.0 
_reflns.d_resolution_high            1.90 
_reflns.d_resolution_low             50.0 
_reflns.number_all                   10581 
_reflns.number_obs                   10568 
_reflns.percent_possible_obs         99.9 
_reflns.pdbx_Rmerge_I_obs            0.041 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        29.9 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              6.9 
_reflns.R_free_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.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
_reflns_shell.d_res_high             1.90 
_reflns_shell.d_res_low              1.97 
_reflns_shell.percent_possible_all   92.7 
_reflns_shell.Rmerge_I_obs           0.128 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    10.9 
_reflns_shell.pdbx_redundancy        6.1 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      671 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_diffrn_id         ? 
_reflns_shell.pdbx_ordinal           1 
# 
_refine.entry_id                                 2OOB 
_refine.ls_number_reflns_obs                     10076 
_refine.ls_number_reflns_all                     10581 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             19.15 
_refine.ls_d_res_high                            1.90 
_refine.ls_percent_reflns_obs                    98.65 
_refine.ls_R_factor_obs                          0.199 
_refine.ls_R_factor_all                          0.199 
_refine.ls_R_factor_R_work                       0.19658 
_refine.ls_R_factor_R_free                       0.25636 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.8 
_refine.ls_number_reflns_R_free                  505 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.946 
_refine.correlation_coeff_Fo_to_Fc_free          0.897 
_refine.B_iso_mean                               21.702 
_refine.aniso_B[1][1]                            0.01 
_refine.aniso_B[2][2]                            0.00 
_refine.aniso_B[3][3]                            0.00 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  ? 
_refine.pdbx_starting_model                      'pdb entries 1UBQ, 2OOA' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.162 
_refine.pdbx_overall_ESU_R_Free                  0.161 
_refine.overall_SU_ML                            0.108 
_refine.overall_SU_B                             3.620 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        924 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.number_atoms_solvent             134 
_refine_hist.number_atoms_total               1058 
_refine_hist.d_res_high                       1.90 
_refine_hist.d_res_low                        19.15 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d         0.017  0.022  ? 933  'X-RAY DIFFRACTION' ? 
r_angle_refined_deg      1.753  1.982  ? 1253 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg   6.203  5.000  ? 114  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg   29.879 25.556 ? 45   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg   15.133 15.000 ? 186  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg   17.774 15.000 ? 6    'X-RAY DIFFRACTION' ? 
r_chiral_restr           0.147  0.200  ? 147  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined     0.006  0.020  ? 679  'X-RAY DIFFRACTION' ? 
r_nbd_refined            0.211  0.200  ? 406  'X-RAY DIFFRACTION' ? 
r_nbtor_refined          0.312  0.200  ? 640  'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined    0.176  0.200  ? 112  'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined   0.231  0.200  ? 58   'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined 0.242  0.200  ? 16   'X-RAY DIFFRACTION' ? 
r_mcbond_it              1.042  1.500  ? 593  'X-RAY DIFFRACTION' ? 
r_mcangle_it             1.728  2.000  ? 929  'X-RAY DIFFRACTION' ? 
r_scbond_it              2.888  3.000  ? 373  'X-RAY DIFFRACTION' ? 
r_scangle_it             4.777  4.500  ? 324  'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       1.90 
_refine_ls_shell.d_res_low                        1.948 
_refine_ls_shell.number_reflns_R_work             671 
_refine_ls_shell.R_factor_R_work                  0.223 
_refine_ls_shell.percent_reflns_obs               90.49 
_refine_ls_shell.R_factor_R_free                  0.368 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             43 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.number_reflns_obs                671 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  2OOB 
_struct.title                     'crystal structure of the UBA domain from Cbl-b ubiquitin ligase in complex with ubiquitin' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        2OOB 
_struct_keywords.pdbx_keywords   LIGASE 
_struct_keywords.text            'protein-protein complex, LIGASE' 
# 
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 2 ? 
C N N 3 ? 
D N N 3 ? 
# 
_struct_biol.id   1 
# 
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 1 ASN A 10 ? GLU A 21 ? ASN A 931 GLU A 942 1 ? 12 
HELX_P HELX_P2 2 ALA A 24 ? ALA A 35 ? ALA A 945 ALA A 956 1 ? 12 
HELX_P HELX_P3 3 ASN A 38 ? ALA A 50 ? ASN A 959 ALA A 971 1 ? 13 
HELX_P HELX_P4 4 THR B 22 ? GLY B 35 ? THR B 22  GLY B 35  1 ? 14 
HELX_P HELX_P5 5 PRO B 37 ? ASP B 39 ? PRO B 37  ASP B 39  5 ? 3  
HELX_P HELX_P6 6 LEU B 56 ? ASN B 60 ? LEU B 56  ASN B 60  5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_sheet.id               A 
_struct_sheet.type             ? 
_struct_sheet.number_strands   5 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2 ? anti-parallel 
A 2 3 ? parallel      
A 3 4 ? anti-parallel 
A 4 5 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1 THR B 12 ? GLU B 16 ? THR B 12 GLU B 16 
A 2 GLN B 2  ? LYS B 6  ? GLN B 2  LYS B 6  
A 3 THR B 66 ? LEU B 71 ? THR B 66 LEU B 71 
A 4 GLN B 41 ? PHE B 45 ? GLN B 41 PHE B 45 
A 5 LYS B 48 ? GLN B 49 ? LYS B 48 GLN B 49 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2 O ILE B 13 ? O ILE B 13 N VAL B 5  ? N VAL B 5  
A 2 3 N PHE B 4  ? N PHE B 4  O LEU B 67 ? O LEU B 67 
A 3 4 O VAL B 70 ? O VAL B 70 N ARG B 42 ? N ARG B 42 
A 4 5 N PHE B 45 ? N PHE B 45 O LYS B 48 ? O LYS B 48 
# 
_database_PDB_matrix.entry_id          2OOB 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    2OOB 
_atom_sites.fract_transf_matrix[1][1]   0.019760 
_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]   0.018254 
_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]   0.010568 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . LEU A 1 8  ? 26.117 -5.693  15.769 1.00 29.81 ? 929 LEU A N   1 
ATOM   2    C CA  . LEU A 1 8  ? 27.153 -4.857  15.061 1.00 29.93 ? 929 LEU A CA  1 
ATOM   3    C C   . LEU A 1 8  ? 26.486 -3.835  14.143 1.00 29.74 ? 929 LEU A C   1 
ATOM   4    O O   . LEU A 1 8  ? 26.790 -2.625  14.181 1.00 29.50 ? 929 LEU A O   1 
ATOM   5    C CB  . LEU A 1 8  ? 28.096 -5.742  14.248 1.00 30.37 ? 929 LEU A CB  1 
ATOM   6    C CG  . LEU A 1 8  ? 29.617 -5.471  14.154 1.00 28.52 ? 929 LEU A CG  1 
ATOM   7    C CD1 . LEU A 1 8  ? 30.109 -5.719  12.711 1.00 27.72 ? 929 LEU A CD1 1 
ATOM   8    C CD2 . LEU A 1 8  ? 30.111 -4.134  14.702 1.00 25.22 ? 929 LEU A CD2 1 
ATOM   9    N N   . GLU A 1 9  ? 25.592 -4.316  13.283 1.00 29.50 ? 930 GLU A N   1 
ATOM   10   C CA  . GLU A 1 9  ? 24.720 -3.411  12.581 1.00 29.52 ? 930 GLU A CA  1 
ATOM   11   C C   . GLU A 1 9  ? 23.799 -3.032  13.722 1.00 28.84 ? 930 GLU A C   1 
ATOM   12   O O   . GLU A 1 9  ? 23.834 -3.649  14.790 1.00 30.73 ? 930 GLU A O   1 
ATOM   13   C CB  . GLU A 1 9  ? 24.057 -4.070  11.368 1.00 30.31 ? 930 GLU A CB  1 
ATOM   14   C CG  . GLU A 1 9  ? 25.092 -4.539  10.271 1.00 32.29 ? 930 GLU A CG  1 
ATOM   15   C CD  . GLU A 1 9  ? 26.361 -3.610  10.128 1.00 33.77 ? 930 GLU A CD  1 
ATOM   16   O OE1 . GLU A 1 9  ? 26.199 -2.374  9.952  1.00 35.75 ? 930 GLU A OE1 1 
ATOM   17   O OE2 . GLU A 1 9  ? 27.517 -4.127  10.199 1.00 32.22 ? 930 GLU A OE2 1 
ATOM   18   N N   . ASN A 1 10 ? 23.064 -1.967  13.629 1.00 27.08 ? 931 ASN A N   1 
ATOM   19   C CA  . ASN A 1 10 ? 22.627 -1.491  14.972 1.00 24.79 ? 931 ASN A CA  1 
ATOM   20   C C   . ASN A 1 10 ? 21.131 -1.716  15.039 1.00 21.71 ? 931 ASN A C   1 
ATOM   21   O O   . ASN A 1 10 ? 20.392 -0.807  15.330 1.00 20.44 ? 931 ASN A O   1 
ATOM   22   C CB  . ASN A 1 10 ? 23.051 -0.021  15.168 1.00 24.40 ? 931 ASN A CB  1 
ATOM   23   C CG  . ASN A 1 10 ? 23.184 0.410   16.651 1.00 25.91 ? 931 ASN A CG  1 
ATOM   24   O OD1 . ASN A 1 10 ? 23.037 -0.377  17.613 1.00 26.29 ? 931 ASN A OD1 1 
ATOM   25   N ND2 . ASN A 1 10 ? 23.449 1.699   16.827 1.00 26.39 ? 931 ASN A ND2 1 
ATOM   26   N N   . VAL A 1 11 ? 20.715 -2.967  14.802 1.00 19.44 ? 932 VAL A N   1 
ATOM   27   C CA  . VAL A 1 11 ? 19.317 -3.241  14.414 1.00 18.49 ? 932 VAL A CA  1 
ATOM   28   C C   . VAL A 1 11 ? 18.230 -2.792  15.396 1.00 16.51 ? 932 VAL A C   1 
ATOM   29   O O   . VAL A 1 11 ? 17.280 -2.124  14.973 1.00 16.08 ? 932 VAL A O   1 
ATOM   30   C CB  . VAL A 1 11 ? 19.089 -4.686  13.880 1.00 19.25 ? 932 VAL A CB  1 
ATOM   31   C CG1 . VAL A 1 11 ? 17.615 -4.913  13.531 1.00 20.18 ? 932 VAL A CG1 1 
ATOM   32   C CG2 . VAL A 1 11 ? 19.942 -4.876  12.601 1.00 20.29 ? 932 VAL A CG2 1 
ATOM   33   N N   . ASP A 1 12 ? 18.390 -3.151  16.665 1.00 14.44 ? 933 ASP A N   1 
ATOM   34   C CA  . ASP A 1 12 ? 17.419 -2.787  17.711 1.00 13.12 ? 933 ASP A CA  1 
ATOM   35   C C   . ASP A 1 12 ? 17.374 -1.266  17.822 1.00 11.75 ? 933 ASP A C   1 
ATOM   36   O O   . ASP A 1 12 ? 16.299 -0.698  17.955 1.00 10.97 ? 933 ASP A O   1 
ATOM   37   C CB  . ASP A 1 12 ? 17.827 -3.363  19.061 1.00 12.60 ? 933 ASP A CB  1 
ATOM   38   C CG  . ASP A 1 12 ? 17.624 -4.878  19.165 1.00 14.67 ? 933 ASP A CG  1 
ATOM   39   O OD1 . ASP A 1 12 ? 18.073 -5.413  20.195 1.00 14.47 ? 933 ASP A OD1 1 
ATOM   40   O OD2 . ASP A 1 12 ? 17.023 -5.511  18.251 1.00 16.37 ? 933 ASP A OD2 1 
ATOM   41   N N   . ALA A 1 13 ? 18.540 -0.603  17.782 1.00 10.80 ? 934 ALA A N   1 
ATOM   42   C CA  . ALA A 1 13 ? 18.553 0.895   17.848 1.00 11.56 ? 934 ALA A CA  1 
ATOM   43   C C   . ALA A 1 13 ? 17.863 1.493   16.630 1.00 12.27 ? 934 ALA A C   1 
ATOM   44   O O   . ALA A 1 13 ? 17.145 2.501   16.753 1.00 12.08 ? 934 ALA A O   1 
ATOM   45   C CB  . ALA A 1 13 ? 20.003 1.474   17.974 1.00 12.40 ? 934 ALA A CB  1 
ATOM   46   N N   . LYS A 1 14 ? 18.070 0.875   15.462 1.00 11.97 ? 935 LYS A N   1 
ATOM   47   C CA  . LYS A 1 14 ? 17.440 1.342   14.211 1.00 12.60 ? 935 LYS A CA  1 
ATOM   48   C C   . LYS A 1 14 ? 15.921 1.104   14.231 1.00 12.45 ? 935 LYS A C   1 
ATOM   49   O O   . LYS A 1 14 ? 15.166 1.992   13.818 1.00 12.53 ? 935 LYS A O   1 
ATOM   50   C CB  . LYS A 1 14 ? 18.088 0.668   12.985 1.00 13.38 ? 935 LYS A CB  1 
ATOM   51   C CG  . LYS A 1 14 ? 19.521 1.152   12.754 1.00 13.04 ? 935 LYS A CG  1 
ATOM   52   C CD  . LYS A 1 14 ? 20.121 0.542   11.509 1.00 13.17 ? 935 LYS A CD  1 
ATOM   53   C CE  . LYS A 1 14 ? 21.534 1.063   11.268 1.00 14.86 ? 935 LYS A CE  1 
ATOM   54   N NZ  . LYS A 1 14 ? 22.026 0.174   10.138 1.00 16.40 ? 935 LYS A NZ  1 
ATOM   55   N N   . ILE A 1 15 ? 15.488 -0.050  14.751 1.00 10.93 ? 936 ILE A N   1 
ATOM   56   C CA  . ILE A 1 15 ? 14.052 -0.297  14.943 1.00 12.45 ? 936 ILE A CA  1 
ATOM   57   C C   . ILE A 1 15 ? 13.452 0.787   15.847 1.00 12.85 ? 936 ILE A C   1 
ATOM   58   O O   . ILE A 1 15 ? 12.435 1.394   15.502 1.00 12.24 ? 936 ILE A O   1 
ATOM   59   C CB  . ILE A 1 15 ? 13.745 -1.704  15.528 1.00 12.04 ? 936 ILE A CB  1 
ATOM   60   C CG1 . ILE A 1 15 ? 14.094 -2.804  14.500 1.00 13.51 ? 936 ILE A CG1 1 
ATOM   61   C CG2 . ILE A 1 15 ? 12.259 -1.812  15.942 1.00 10.62 ? 936 ILE A CG2 1 
ATOM   62   C CD1 . ILE A 1 15 ? 14.188 -4.227  15.098 1.00 13.79 ? 936 ILE A CD1 1 
ATOM   63   N N   . ALA A 1 16 ? 14.092 1.012   16.997 1.00 12.41 ? 937 ALA A N   1 
ATOM   64   C CA  . ALA A 1 16 ? 13.563 1.943   17.992 1.00 13.27 ? 937 ALA A CA  1 
ATOM   65   C C   . ALA A 1 16 ? 13.434 3.345   17.380 1.00 13.70 ? 937 ALA A C   1 
ATOM   66   O O   . ALA A 1 16 ? 12.383 3.988   17.537 1.00 13.87 ? 937 ALA A O   1 
ATOM   67   C CB  . ALA A 1 16 ? 14.461 1.986   19.264 1.00 13.52 ? 937 ALA A CB  1 
ATOM   68   N N   . LYS A 1 17 ? 14.487 3.797   16.709 1.00 13.33 ? 938 LYS A N   1 
ATOM   69   C CA  . LYS A 1 17 ? 14.516 5.135   16.063 1.00 14.79 ? 938 LYS A CA  1 
ATOM   70   C C   . LYS A 1 17 ? 13.353 5.313   15.084 1.00 14.31 ? 938 LYS A C   1 
ATOM   71   O O   . LYS A 1 17 ? 12.597 6.313   15.156 1.00 14.53 ? 938 LYS A O   1 
ATOM   72   C CB  . LYS A 1 17 ? 15.835 5.361   15.333 1.00 14.78 ? 938 LYS A CB  1 
ATOM   73   C CG  . LYS A 1 17 ? 15.955 6.769   14.630 1.00 15.12 ? 938 LYS A CG  1 
ATOM   74   C CD  . LYS A 1 17 ? 17.317 6.902   13.974 1.00 16.87 ? 938 LYS A CD  1 
ATOM   75   C CE  . LYS A 1 17 ? 17.465 8.161   13.137 1.00 19.98 ? 938 LYS A CE  1 
ATOM   76   N NZ  . LYS A 1 17 ? 17.004 9.352   13.922 1.00 20.21 ? 938 LYS A NZ  1 
ATOM   77   N N   . LEU A 1 18 ? 13.174 4.350   14.179 1.00 13.07 ? 939 LEU A N   1 
ATOM   78   C CA  . LEU A 1 18 ? 12.091 4.484   13.203 1.00 12.80 ? 939 LEU A CA  1 
ATOM   79   C C   . LEU A 1 18 ? 10.698 4.340   13.820 1.00 13.35 ? 939 LEU A C   1 
ATOM   80   O O   . LEU A 1 18 ? 9.778  5.053   13.430 1.00 13.43 ? 939 LEU A O   1 
ATOM   81   C CB  . LEU A 1 18 ? 12.298 3.578   11.990 1.00 12.68 ? 939 LEU A CB  1 
ATOM   82   C CG  . LEU A 1 18 ? 13.504 3.935   11.110 1.00 13.83 ? 939 LEU A CG  1 
ATOM   83   C CD1 . LEU A 1 18 ? 13.793 2.730   10.115 1.00 16.52 ? 939 LEU A CD1 1 
ATOM   84   C CD2 . LEU A 1 18 ? 13.330 5.286   10.403 1.00 14.32 ? 939 LEU A CD2 1 
ATOM   85   N N   . MET A 1 19 ? 10.559 3.456   14.808 1.00 14.90 ? 940 MET A N   1 
ATOM   86   C CA  . MET A 1 19 ? 9.319  3.388   15.602 1.00 15.24 ? 940 MET A CA  1 
ATOM   87   C C   . MET A 1 19 ? 9.022  4.781   16.182 1.00 16.41 ? 940 MET A C   1 
ATOM   88   O O   . MET A 1 19 ? 7.882  5.233   16.135 1.00 17.62 ? 940 MET A O   1 
ATOM   89   C CB  . MET A 1 19 ? 9.439  2.354   16.713 1.00 14.52 ? 940 MET A CB  1 
ATOM   90   C CG  . MET A 1 19 ? 9.360  0.917   16.203 1.00 14.63 ? 940 MET A CG  1 
ATOM   91   S SD  . MET A 1 19 ? 9.512  -0.265  17.578 1.00 17.42 ? 940 MET A SD  1 
ATOM   92   C CE  . MET A 1 19 ? 7.976  0.001   18.479 1.00 19.11 ? 940 MET A CE  1 
ATOM   93   N N   . GLY A 1 20 ? 10.055 5.478   16.647 1.00 16.53 ? 941 GLY A N   1 
ATOM   94   C CA  . GLY A 1 20 ? 9.886  6.815   17.255 1.00 17.00 ? 941 GLY A CA  1 
ATOM   95   C C   . GLY A 1 20 ? 9.341  7.837   16.286 1.00 17.76 ? 941 GLY A C   1 
ATOM   96   O O   . GLY A 1 20 ? 8.689  8.788   16.705 1.00 18.57 ? 941 GLY A O   1 
ATOM   97   N N   . GLU A 1 21 ? 9.565  7.631   14.985 1.00 17.82 ? 942 GLU A N   1 
ATOM   98   C CA  . GLU A 1 21 ? 9.040  8.532   13.953 1.00 19.51 ? 942 GLU A CA  1 
ATOM   99   C C   . GLU A 1 21 ? 7.565  8.333   13.637 1.00 20.28 ? 942 GLU A C   1 
ATOM   100  O O   . GLU A 1 21 ? 7.002  9.064   12.826 1.00 21.60 ? 942 GLU A O   1 
ATOM   101  C CB  . GLU A 1 21 ? 9.904  8.492   12.676 1.00 19.05 ? 942 GLU A CB  1 
ATOM   102  C CG  . GLU A 1 21 ? 11.333 8.876   12.955 1.00 19.58 ? 942 GLU A CG  1 
ATOM   103  C CD  . GLU A 1 21 ? 12.249 8.785   11.754 1.00 21.50 ? 942 GLU A CD  1 
ATOM   104  O OE1 . GLU A 1 21 ? 11.761 8.704   10.608 1.00 19.37 ? 942 GLU A OE1 1 
ATOM   105  O OE2 . GLU A 1 21 ? 13.487 8.789   11.974 1.00 20.59 ? 942 GLU A OE2 1 
ATOM   106  N N   . GLY A 1 22 ? 6.937  7.368   14.282 1.00 21.07 ? 943 GLY A N   1 
ATOM   107  C CA  . GLY A 1 22 ? 5.496  7.253   14.259 1.00 22.65 ? 943 GLY A CA  1 
ATOM   108  C C   . GLY A 1 22 ? 5.041  6.006   13.529 1.00 22.38 ? 943 GLY A C   1 
ATOM   109  O O   . GLY A 1 22 ? 3.983  6.009   12.905 1.00 23.50 ? 943 GLY A O   1 
ATOM   110  N N   . TYR A 1 23 ? 5.840  4.947   13.596 1.00 21.26 ? 944 TYR A N   1 
ATOM   111  C CA  . TYR A 1 23 ? 5.524  3.703   12.905 1.00 20.43 ? 944 TYR A CA  1 
ATOM   112  C C   . TYR A 1 23 ? 5.509  2.503   13.852 1.00 20.65 ? 944 TYR A C   1 
ATOM   113  O O   . TYR A 1 23 ? 6.254  2.420   14.838 1.00 19.42 ? 944 TYR A O   1 
ATOM   114  C CB  . TYR A 1 23 ? 6.488  3.451   11.715 1.00 21.14 ? 944 TYR A CB  1 
ATOM   115  C CG  . TYR A 1 23 ? 6.569  4.594   10.759 1.00 20.12 ? 944 TYR A CG  1 
ATOM   116  C CD1 . TYR A 1 23 ? 5.514  4.852   9.858  1.00 20.39 ? 944 TYR A CD1 1 
ATOM   117  C CD2 . TYR A 1 23 ? 7.669  5.455   10.763 1.00 17.96 ? 944 TYR A CD2 1 
ATOM   118  C CE1 . TYR A 1 23 ? 5.560  5.940   8.995  1.00 20.13 ? 944 TYR A CE1 1 
ATOM   119  C CE2 . TYR A 1 23 ? 7.729  6.556   9.868  1.00 21.63 ? 944 TYR A CE2 1 
ATOM   120  C CZ  . TYR A 1 23 ? 6.644  6.782   8.993  1.00 22.12 ? 944 TYR A CZ  1 
ATOM   121  O OH  . TYR A 1 23 ? 6.665  7.842   8.096  1.00 23.64 ? 944 TYR A OH  1 
ATOM   122  N N   . ALA A 1 24 ? 4.668  1.542   13.518 1.00 19.66 ? 945 ALA A N   1 
ATOM   123  C CA  . ALA A 1 24 ? 4.487  0.376   14.355 1.00 19.88 ? 945 ALA A CA  1 
ATOM   124  C C   . ALA A 1 24 ? 5.650  -0.632  14.237 1.00 19.21 ? 945 ALA A C   1 
ATOM   125  O O   . ALA A 1 24 ? 6.300  -0.720  13.198 1.00 18.25 ? 945 ALA A O   1 
ATOM   126  C CB  . ALA A 1 24 ? 3.144  -0.295  13.981 1.00 19.79 ? 945 ALA A CB  1 
ATOM   127  N N   . PHE A 1 25 ? 5.897  -1.397  15.294 1.00 18.98 ? 946 PHE A N   1 
ATOM   128  C CA  . PHE A 1 25 ? 6.998  -2.356  15.297 1.00 19.43 ? 946 PHE A CA  1 
ATOM   129  C C   . PHE A 1 25 ? 7.065  -3.276  14.054 1.00 19.51 ? 946 PHE A C   1 
ATOM   130  O O   . PHE A 1 25 ? 8.126  -3.399  13.424 1.00 18.02 ? 946 PHE A O   1 
ATOM   131  C CB  . PHE A 1 25 ? 7.050  -3.190  16.566 1.00 18.98 ? 946 PHE A CB  1 
ATOM   132  C CG  . PHE A 1 25 ? 8.032  -4.340  16.475 1.00 22.17 ? 946 PHE A CG  1 
ATOM   133  C CD1 . PHE A 1 25 ? 9.391  -4.133  16.691 1.00 18.72 ? 946 PHE A CD1 1 
ATOM   134  C CD2 . PHE A 1 25 ? 7.588  -5.625  16.124 1.00 22.44 ? 946 PHE A CD2 1 
ATOM   135  C CE1 . PHE A 1 25 ? 10.288 -5.174  16.589 1.00 23.37 ? 946 PHE A CE1 1 
ATOM   136  C CE2 . PHE A 1 25 ? 8.480  -6.682  16.018 1.00 22.89 ? 946 PHE A CE2 1 
ATOM   137  C CZ  . PHE A 1 25 ? 9.844  -6.452  16.251 1.00 21.97 ? 946 PHE A CZ  1 
ATOM   138  N N   . GLU A 1 26 ? 5.961  -3.939  13.703 1.00 19.24 ? 947 GLU A N   1 
ATOM   139  C CA  . GLU A 1 26 ? 6.017  -4.883  12.554 1.00 20.13 ? 947 GLU A CA  1 
ATOM   140  C C   . GLU A 1 26 ? 6.348  -4.203  11.217 1.00 19.21 ? 947 GLU A C   1 
ATOM   141  O O   . GLU A 1 26 ? 7.103  -4.748  10.429 1.00 19.28 ? 947 GLU A O   1 
ATOM   142  C CB  . GLU A 1 26 ? 4.719  -5.702  12.420 1.00 21.09 ? 947 GLU A CB  1 
ATOM   143  C CG  . GLU A 1 26 ? 4.296  -6.425  13.711 1.00 27.05 ? 947 GLU A CG  1 
ATOM   144  C CD  . GLU A 1 26 ? 5.158  -7.633  14.106 1.00 35.91 ? 947 GLU A CD  1 
ATOM   145  O OE1 . GLU A 1 26 ? 4.779  -8.300  15.118 1.00 39.48 ? 947 GLU A OE1 1 
ATOM   146  O OE2 . GLU A 1 26 ? 6.191  -7.941  13.432 1.00 39.08 ? 947 GLU A OE2 1 
ATOM   147  N N   . GLU A 1 27 ? 5.770  -3.031  10.967 1.00 19.19 ? 948 GLU A N   1 
ATOM   148  C CA  . GLU A 1 27 ? 6.116  -2.205  9.804  1.00 20.22 ? 948 GLU A CA  1 
ATOM   149  C C   . GLU A 1 27 ? 7.616  -1.862  9.746  1.00 17.76 ? 948 GLU A C   1 
ATOM   150  O O   . GLU A 1 27 ? 8.274  -1.959  8.703  1.00 16.39 ? 948 GLU A O   1 
ATOM   151  C CB  . GLU A 1 27 ? 5.338  -0.882  9.866  1.00 20.14 ? 948 GLU A CB  1 
ATOM   152  C CG  . GLU A 1 27 ? 3.900  -1.009  9.415  1.00 24.52 ? 948 GLU A CG  1 
ATOM   153  C CD  . GLU A 1 27 ? 3.051  0.214   9.756  1.00 25.97 ? 948 GLU A CD  1 
ATOM   154  O OE1 . GLU A 1 27 ? 2.014  0.373   9.085  1.00 31.69 ? 948 GLU A OE1 1 
ATOM   155  O OE2 . GLU A 1 27 ? 3.390  1.002   10.707 1.00 34.37 ? 948 GLU A OE2 1 
ATOM   156  N N   . VAL A 1 28 ? 8.139  -1.407  10.880 1.00 16.09 ? 949 VAL A N   1 
ATOM   157  C CA  . VAL A 1 28 ? 9.543  -0.971  10.944 1.00 14.97 ? 949 VAL A CA  1 
ATOM   158  C C   . VAL A 1 28 ? 10.470 -2.163  10.715 1.00 15.05 ? 949 VAL A C   1 
ATOM   159  O O   . VAL A 1 28 ? 11.378 -2.069  9.914  1.00 14.59 ? 949 VAL A O   1 
ATOM   160  C CB  . VAL A 1 28 ? 9.885  -0.287  12.299 1.00 14.53 ? 949 VAL A CB  1 
ATOM   161  C CG1 . VAL A 1 28 ? 11.407 -0.086  12.418 1.00 13.30 ? 949 VAL A CG1 1 
ATOM   162  C CG2 . VAL A 1 28 ? 9.145  1.049   12.424 1.00 12.58 ? 949 VAL A CG2 1 
ATOM   163  N N   . LYS A 1 29 ? 10.233 -3.258  11.434 1.00 14.97 ? 950 LYS A N   1 
ATOM   164  C CA  . LYS A 1 29 ? 10.988 -4.495  11.256 1.00 17.41 ? 950 LYS A CA  1 
ATOM   165  C C   . LYS A 1 29 ? 11.030 -4.894  9.774  1.00 16.91 ? 950 LYS A C   1 
ATOM   166  O O   . LYS A 1 29 ? 12.105 -5.134  9.231  1.00 16.16 ? 950 LYS A O   1 
ATOM   167  C CB  . LYS A 1 29 ? 10.367 -5.641  12.076 1.00 17.57 ? 950 LYS A CB  1 
ATOM   168  C CG  . LYS A 1 29 ? 11.251 -6.893  12.116 1.00 20.07 ? 950 LYS A CG  1 
ATOM   169  C CD  . LYS A 1 29 ? 10.527 -8.075  12.753 1.00 19.78 ? 950 LYS A CD  1 
ATOM   170  C CE  . LYS A 1 29 ? 11.349 -9.382  12.620 1.00 20.99 ? 950 LYS A CE  1 
ATOM   171  N NZ  . LYS A 1 29 ? 12.620 -9.348  13.459 1.00 20.48 ? 950 LYS A NZ  1 
ATOM   172  N N   . ARG A 1 30 ? 9.845  -4.978  9.161  1.00 16.72 ? 951 ARG A N   1 
ATOM   173  C CA  . ARG A 1 30 ? 9.717  -5.342  7.758  1.00 17.21 ? 951 ARG A CA  1 
ATOM   174  C C   . ARG A 1 30 ? 10.410 -4.348  6.809  1.00 16.86 ? 951 ARG A C   1 
ATOM   175  O O   . ARG A 1 30 ? 11.105 -4.763  5.873  1.00 16.23 ? 951 ARG A O   1 
ATOM   176  C CB  . ARG A 1 30 ? 8.239  -5.487  7.406  1.00 17.88 ? 951 ARG A CB  1 
ATOM   177  C CG  . ARG A 1 30 ? 8.001  -5.912  5.972  1.00 22.11 ? 951 ARG A CG  1 
ATOM   178  C CD  . ARG A 1 30 ? 8.687  -7.252  5.655  1.00 28.39 ? 951 ARG A CD  1 
ATOM   179  N NE  . ARG A 1 30 ? 8.474  -7.591  4.250  1.00 32.90 ? 951 ARG A NE  1 
ATOM   180  C CZ  . ARG A 1 30 ? 9.301  -8.324  3.518  1.00 34.41 ? 951 ARG A CZ  1 
ATOM   181  N NH1 . ARG A 1 30 ? 10.422 -8.811  4.056  1.00 33.89 ? 951 ARG A NH1 1 
ATOM   182  N NH2 . ARG A 1 30 ? 9.008  -8.549  2.236  1.00 35.66 ? 951 ARG A NH2 1 
ATOM   183  N N   . ALA A 1 31 ? 10.219 -3.044  7.031  1.00 15.72 ? 952 ALA A N   1 
ATOM   184  C CA  . ALA A 1 31 ? 10.937 -2.038  6.199  1.00 16.25 ? 952 ALA A CA  1 
ATOM   185  C C   . ALA A 1 31 ? 12.470 -2.146  6.305  1.00 15.97 ? 952 ALA A C   1 
ATOM   186  O O   . ALA A 1 31 ? 13.177 -1.990  5.303  1.00 15.79 ? 952 ALA A O   1 
ATOM   187  C CB  . ALA A 1 31 ? 10.486 -0.595  6.558  1.00 16.07 ? 952 ALA A CB  1 
ATOM   188  N N   . LEU A 1 32 ? 12.997 -2.367  7.514  1.00 16.55 ? 953 LEU A N   1 
ATOM   189  C CA  . LEU A 1 32 ? 14.457 -2.504  7.673  1.00 17.11 ? 953 LEU A CA  1 
ATOM   190  C C   . LEU A 1 32 ? 14.980 -3.734  6.953  1.00 18.12 ? 953 LEU A C   1 
ATOM   191  O O   . LEU A 1 32 ? 16.060 -3.679  6.350  1.00 18.20 ? 953 LEU A O   1 
ATOM   192  C CB  . LEU A 1 32 ? 14.880 -2.533  9.148  1.00 17.29 ? 953 LEU A CB  1 
ATOM   193  C CG  . LEU A 1 32 ? 14.969 -1.147  9.802  1.00 17.83 ? 953 LEU A CG  1 
ATOM   194  C CD1 . LEU A 1 32 ? 15.209 -1.242  11.298 1.00 20.95 ? 953 LEU A CD1 1 
ATOM   195  C CD2 . LEU A 1 32 ? 16.069 -0.334  9.183  1.00 17.11 ? 953 LEU A CD2 1 
ATOM   196  N N   . GLU A 1 33 ? 14.217 -4.824  7.028  1.00 19.06 ? 954 GLU A N   1 
ATOM   197  C CA  . GLU A 1 33 ? 14.517 -6.054  6.258  1.00 20.96 ? 954 GLU A CA  1 
ATOM   198  C C   . GLU A 1 33 ? 14.609 -5.749  4.767  1.00 20.50 ? 954 GLU A C   1 
ATOM   199  O O   . GLU A 1 33 ? 15.634 -6.012  4.138  1.00 21.21 ? 954 GLU A O   1 
ATOM   200  C CB  . GLU A 1 33 ? 13.401 -7.057  6.402  1.00 21.98 ? 954 GLU A CB  1 
ATOM   201  C CG  . GLU A 1 33 ? 13.321 -7.830  7.658  1.00 27.29 ? 954 GLU A CG  1 
ATOM   202  C CD  . GLU A 1 33 ? 12.130 -8.767  7.572  1.00 33.92 ? 954 GLU A CD  1 
ATOM   203  O OE1 . GLU A 1 33 ? 12.101 -9.564  6.595  1.00 36.67 ? 954 GLU A OE1 1 
ATOM   204  O OE2 . GLU A 1 33 ? 11.212 -8.667  8.423  1.00 34.94 ? 954 GLU A OE2 1 
ATOM   205  N N   . ILE A 1 34 ? 13.540 -5.181  4.222  1.00 19.90 ? 955 ILE A N   1 
ATOM   206  C CA  . ILE A 1 34 ? 13.510 -4.794  2.809  1.00 19.70 ? 955 ILE A CA  1 
ATOM   207  C C   . ILE A 1 34 ? 14.711 -3.898  2.465  1.00 19.53 ? 955 ILE A C   1 
ATOM   208  O O   . ILE A 1 34 ? 15.399 -4.135  1.459  1.00 19.01 ? 955 ILE A O   1 
ATOM   209  C CB  . ILE A 1 34 ? 12.143 -4.176  2.424  1.00 19.91 ? 955 ILE A CB  1 
ATOM   210  C CG1 . ILE A 1 34 ? 11.039 -5.239  2.467  1.00 21.27 ? 955 ILE A CG1 1 
ATOM   211  C CG2 . ILE A 1 34 ? 12.208 -3.484  1.069  1.00 18.24 ? 955 ILE A CG2 1 
ATOM   212  C CD1 . ILE A 1 34 ? 9.660  -4.667  2.389  1.00 24.83 ? 955 ILE A CD1 1 
ATOM   213  N N   . ALA A 1 35 ? 14.975 -2.892  3.308  1.00 18.89 ? 956 ALA A N   1 
ATOM   214  C CA  . ALA A 1 35 ? 16.082 -1.937  3.123  1.00 19.22 ? 956 ALA A CA  1 
ATOM   215  C C   . ALA A 1 35 ? 17.500 -2.446  3.433  1.00 19.57 ? 956 ALA A C   1 
ATOM   216  O O   . ALA A 1 35 ? 18.461 -1.690  3.343  1.00 19.17 ? 956 ALA A O   1 
ATOM   217  C CB  . ALA A 1 35 ? 15.809 -0.632  3.950  1.00 18.14 ? 956 ALA A CB  1 
ATOM   218  N N   . GLN A 1 36 ? 17.620 -3.708  3.831  1.00 20.22 ? 957 GLN A N   1 
ATOM   219  C CA  . GLN A 1 36 ? 18.905 -4.294  4.193  1.00 21.37 ? 957 GLN A CA  1 
ATOM   220  C C   . GLN A 1 36 ? 19.596 -3.419  5.242  1.00 21.18 ? 957 GLN A C   1 
ATOM   221  O O   . GLN A 1 36 ? 20.784 -3.086  5.128  1.00 21.60 ? 957 GLN A O   1 
ATOM   222  C CB  . GLN A 1 36 ? 19.746 -4.561  2.928  1.00 20.73 ? 957 GLN A CB  1 
ATOM   223  C CG  . GLN A 1 36 ? 18.972 -5.415  1.870  1.00 21.88 ? 957 GLN A CG  1 
ATOM   224  C CD  . GLN A 1 36 ? 19.811 -5.776  0.625  1.00 25.70 ? 957 GLN A CD  1 
ATOM   225  O OE1 . GLN A 1 36 ? 19.351 -6.498  -0.270 1.00 31.58 ? 957 GLN A OE1 1 
ATOM   226  N NE2 . GLN A 1 36 ? 21.026 -5.251  0.555  1.00 29.87 ? 957 GLN A NE2 1 
ATOM   227  N N   . ASN A 1 37 ? 18.803 -3.022  6.256  1.00 20.59 ? 958 ASN A N   1 
ATOM   228  C CA  . ASN A 1 37 ? 19.249 -2.232  7.416  1.00 20.10 ? 958 ASN A CA  1 
ATOM   229  C C   . ASN A 1 37 ? 19.674 -0.776  7.150  1.00 19.50 ? 958 ASN A C   1 
ATOM   230  O O   . ASN A 1 37 ? 20.182 -0.102  8.037  1.00 18.91 ? 958 ASN A O   1 
ATOM   231  C CB  . ASN A 1 37 ? 20.281 -3.017  8.264  1.00 20.82 ? 958 ASN A CB  1 
ATOM   232  C CG  . ASN A 1 37 ? 19.666 -4.225  8.922  1.00 23.32 ? 958 ASN A CG  1 
ATOM   233  O OD1 . ASN A 1 37 ? 18.446 -4.258  9.166  1.00 24.18 ? 958 ASN A OD1 1 
ATOM   234  N ND2 . ASN A 1 37 ? 20.508 -5.253  9.227  1.00 24.54 ? 958 ASN A ND2 1 
ATOM   235  N N   . ASN A 1 38 ? 19.373 -0.265  5.947  1.00 19.30 ? 959 ASN A N   1 
ATOM   236  C CA  . ASN A 1 38 ? 19.645 1.143   5.638  1.00 19.26 ? 959 ASN A CA  1 
ATOM   237  C C   . ASN A 1 38 ? 18.477 1.988   6.176  1.00 18.66 ? 959 ASN A C   1 
ATOM   238  O O   . ASN A 1 38 ? 17.332 1.845   5.702  1.00 17.58 ? 959 ASN A O   1 
ATOM   239  C CB  . ASN A 1 38 ? 19.836 1.336   4.114  1.00 19.54 ? 959 ASN A CB  1 
ATOM   240  C CG  . ASN A 1 38 ? 20.173 2.750   3.750  1.00 20.03 ? 959 ASN A CG  1 
ATOM   241  O OD1 . ASN A 1 38 ? 19.445 3.664   4.093  1.00 20.86 ? 959 ASN A OD1 1 
ATOM   242  N ND2 . ASN A 1 38 ? 21.289 2.944   3.046  1.00 21.48 ? 959 ASN A ND2 1 
ATOM   243  N N   . VAL A 1 39 ? 18.770 2.855   7.154  1.00 17.79 ? 960 VAL A N   1 
ATOM   244  C CA  . VAL A 1 39 ? 17.743 3.633   7.862  1.00 17.46 ? 960 VAL A CA  1 
ATOM   245  C C   . VAL A 1 39 ? 17.036 4.590   6.937  1.00 17.34 ? 960 VAL A C   1 
ATOM   246  O O   . VAL A 1 39 ? 15.819 4.682   6.982  1.00 16.71 ? 960 VAL A O   1 
ATOM   247  C CB  . VAL A 1 39 ? 18.296 4.401   9.100  1.00 17.58 ? 960 VAL A CB  1 
ATOM   248  C CG1 . VAL A 1 39 ? 17.226 5.391   9.666  1.00 17.58 ? 960 VAL A CG1 1 
ATOM   249  C CG2 . VAL A 1 39 ? 18.614 3.420   10.173 1.00 18.59 ? 960 VAL A CG2 1 
ATOM   250  N N   . GLU A 1 40 ? 17.818 5.260   6.081  1.00 18.12 ? 961 GLU A N   1 
ATOM   251  C CA  . GLU A 1 40 ? 17.302 6.244   5.123  1.00 18.73 ? 961 GLU A CA  1 
ATOM   252  C C   . GLU A 1 40 ? 16.330 5.565   4.142  1.00 17.37 ? 961 GLU A C   1 
ATOM   253  O O   . GLU A 1 40 ? 15.257 6.080   3.820  1.00 15.69 ? 961 GLU A O   1 
ATOM   254  C CB  . GLU A 1 40 ? 18.479 6.883   4.366  1.00 20.54 ? 961 GLU A CB  1 
ATOM   255  C CG  . GLU A 1 40 ? 19.542 7.652   5.219  1.00 25.83 ? 961 GLU A CG  1 
ATOM   256  C CD  . GLU A 1 40 ? 20.286 6.835   6.339  1.00 34.48 ? 961 GLU A CD  1 
ATOM   257  O OE1 . GLU A 1 40 ? 20.618 5.618   6.174  1.00 33.46 ? 961 GLU A OE1 1 
ATOM   258  O OE2 . GLU A 1 40 ? 20.574 7.457   7.412  1.00 37.58 ? 961 GLU A OE2 1 
ATOM   259  N N   . VAL A 1 41 ? 16.696 4.379   3.682  1.00 16.06 ? 962 VAL A N   1 
ATOM   260  C CA  . VAL A 1 41 ? 15.821 3.643   2.740  1.00 14.62 ? 962 VAL A CA  1 
ATOM   261  C C   . VAL A 1 41 ? 14.570 3.109   3.422  1.00 13.77 ? 962 VAL A C   1 
ATOM   262  O O   . VAL A 1 41 ? 13.469 3.263   2.888  1.00 12.59 ? 962 VAL A O   1 
ATOM   263  C CB  . VAL A 1 41 ? 16.586 2.517   2.020  1.00 14.95 ? 962 VAL A CB  1 
ATOM   264  C CG1 . VAL A 1 41 ? 15.604 1.636   1.219  1.00 16.20 ? 962 VAL A CG1 1 
ATOM   265  C CG2 . VAL A 1 41 ? 17.646 3.129   1.113  1.00 15.05 ? 962 VAL A CG2 1 
ATOM   266  N N   . ALA A 1 42 ? 14.725 2.501   4.603  1.00 13.06 ? 963 ALA A N   1 
ATOM   267  C CA  . ALA A 1 42 ? 13.558 2.036   5.372  1.00 12.62 ? 963 ALA A CA  1 
ATOM   268  C C   . ALA A 1 42 ? 12.602 3.200   5.638  1.00 13.30 ? 963 ALA A C   1 
ATOM   269  O O   . ALA A 1 42 ? 11.372 3.030   5.594  1.00 12.87 ? 963 ALA A O   1 
ATOM   270  C CB  . ALA A 1 42 ? 14.017 1.460   6.683  1.00 12.30 ? 963 ALA A CB  1 
ATOM   271  N N   . ARG A 1 43 ? 13.166 4.363   5.970  1.00 13.98 ? 964 ARG A N   1 
ATOM   272  C CA  . ARG A 1 43 ? 12.335 5.544   6.280  1.00 14.53 ? 964 ARG A CA  1 
ATOM   273  C C   . ARG A 1 43 ? 11.527 5.917   5.052  1.00 15.51 ? 964 ARG A C   1 
ATOM   274  O O   . ARG A 1 43 ? 10.322 6.171   5.163  1.00 16.48 ? 964 ARG A O   1 
ATOM   275  C CB  . ARG A 1 43 ? 13.184 6.742   6.742  1.00 14.45 ? 964 ARG A CB  1 
ATOM   276  C CG  . ARG A 1 43 ? 12.313 8.033   6.924  1.00 15.17 ? 964 ARG A CG  1 
ATOM   277  C CD  . ARG A 1 43 ? 13.161 9.205   7.412  1.00 16.13 ? 964 ARG A CD  1 
ATOM   278  N NE  . ARG A 1 43 ? 13.790 8.946   8.709  1.00 18.52 ? 964 ARG A NE  1 
ATOM   279  C CZ  . ARG A 1 43 ? 15.095 8.886   8.939  1.00 21.13 ? 964 ARG A CZ  1 
ATOM   280  N NH1 . ARG A 1 43 ? 15.988 9.052   7.960  1.00 23.08 ? 964 ARG A NH1 1 
ATOM   281  N NH2 . ARG A 1 43 ? 15.506 8.633   10.165 1.00 23.86 ? 964 ARG A NH2 1 
ATOM   282  N N   . SER A 1 44 ? 12.179 5.935   3.882  1.00 16.02 ? 965 SER A N   1 
ATOM   283  C CA  . SER A 1 44 ? 11.463 6.232   2.635  1.00 16.76 ? 965 SER A CA  1 
ATOM   284  C C   . SER A 1 44 ? 10.337 5.235   2.375  1.00 16.38 ? 965 SER A C   1 
ATOM   285  O O   . SER A 1 44 ? 9.268  5.613   1.915  1.00 16.10 ? 965 SER A O   1 
ATOM   286  C CB  . SER A 1 44 ? 12.414 6.288   1.441  1.00 16.78 ? 965 SER A CB  1 
ATOM   287  O OG  . SER A 1 44 ? 13.381 7.313   1.601  1.00 18.77 ? 965 SER A OG  1 
ATOM   288  N N   . ILE A 1 45 ? 10.565 3.960   2.688  1.00 16.68 ? 966 ILE A N   1 
ATOM   289  C CA  . ILE A 1 45 ? 9.520  2.951   2.545  1.00 16.83 ? 966 ILE A CA  1 
ATOM   290  C C   . ILE A 1 45 ? 8.338  3.233   3.471  1.00 16.76 ? 966 ILE A C   1 
ATOM   291  O O   . ILE A 1 45 ? 7.189  3.230   3.043  1.00 17.67 ? 966 ILE A O   1 
ATOM   292  C CB  . ILE A 1 45 ? 10.076 1.522   2.751  1.00 17.17 ? 966 ILE A CB  1 
ATOM   293  C CG1 . ILE A 1 45 ? 11.063 1.174   1.616  1.00 17.80 ? 966 ILE A CG1 1 
ATOM   294  C CG2 . ILE A 1 45 ? 8.929  0.499   2.906  1.00 16.81 ? 966 ILE A CG2 1 
ATOM   295  C CD1 . ILE A 1 45 ? 11.973 -0.020  1.936  1.00 16.60 ? 966 ILE A CD1 1 
ATOM   296  N N   . LEU A 1 46 ? 8.635  3.533   4.731  1.00 17.19 ? 967 LEU A N   1 
ATOM   297  C CA  . LEU A 1 46 ? 7.627  3.764   5.731  1.00 17.32 ? 967 LEU A CA  1 
ATOM   298  C C   . LEU A 1 46 ? 6.756  4.987   5.370  1.00 18.40 ? 967 LEU A C   1 
ATOM   299  O O   . LEU A 1 46 ? 5.510  4.943   5.494  1.00 17.81 ? 967 LEU A O   1 
ATOM   300  C CB  . LEU A 1 46 ? 8.310  3.930   7.092  1.00 17.93 ? 967 LEU A CB  1 
ATOM   301  C CG  . LEU A 1 46 ? 8.896  2.623   7.660  1.00 17.63 ? 967 LEU A CG  1 
ATOM   302  C CD1 . LEU A 1 46 ? 9.919  2.883   8.805  1.00 14.10 ? 967 LEU A CD1 1 
ATOM   303  C CD2 . LEU A 1 46 ? 7.760  1.644   8.073  1.00 17.92 ? 967 LEU A CD2 1 
ATOM   304  N N   . ARG A 1 47 ? 7.409  6.044   4.893  1.00 18.46 ? 968 ARG A N   1 
ATOM   305  C CA  . ARG A 1 47 ? 6.708  7.288   4.490  1.00 20.93 ? 968 ARG A CA  1 
ATOM   306  C C   . ARG A 1 47 ? 5.846  7.060   3.263  1.00 21.84 ? 968 ARG A C   1 
ATOM   307  O O   . ARG A 1 47 ? 4.677  7.513   3.190  1.00 22.36 ? 968 ARG A O   1 
ATOM   308  C CB  . ARG A 1 47 ? 7.692  8.402   4.171  1.00 20.14 ? 968 ARG A CB  1 
ATOM   309  C CG  . ARG A 1 47 ? 8.350  8.960   5.402  1.00 25.01 ? 968 ARG A CG  1 
ATOM   310  C CD  . ARG A 1 47 ? 9.139  10.223  5.118  1.00 29.15 ? 968 ARG A CD  1 
ATOM   311  N NE  . ARG A 1 47 ? 9.661  10.700  6.389  1.00 33.37 ? 968 ARG A NE  1 
ATOM   312  C CZ  . ARG A 1 47 ? 10.520 11.700  6.566  1.00 32.20 ? 968 ARG A CZ  1 
ATOM   313  N NH1 . ARG A 1 47 ? 10.908 12.008  7.804  1.00 27.89 ? 968 ARG A NH1 1 
ATOM   314  N NH2 . ARG A 1 47 ? 10.985 12.375  5.523  1.00 33.89 ? 968 ARG A NH2 1 
ATOM   315  N N   . GLU A 1 48 ? 6.425  6.359   2.300  1.00 22.31 ? 969 GLU A N   1 
ATOM   316  C CA  . GLU A 1 48 ? 5.743  6.109   1.036  1.00 24.33 ? 969 GLU A CA  1 
ATOM   317  C C   . GLU A 1 48 ? 4.463  5.289   1.207  1.00 24.53 ? 969 GLU A C   1 
ATOM   318  O O   . GLU A 1 48 ? 3.438  5.560   0.556  1.00 24.35 ? 969 GLU A O   1 
ATOM   319  C CB  . GLU A 1 48 ? 6.678  5.360   0.085  1.00 24.06 ? 969 GLU A CB  1 
ATOM   320  C CG  . GLU A 1 48 ? 6.127  5.244   -1.347 1.00 29.10 ? 969 GLU A CG  1 
ATOM   321  C CD  . GLU A 1 48 ? 6.044  6.577   -2.082 1.00 34.27 ? 969 GLU A CD  1 
ATOM   322  O OE1 . GLU A 1 48 ? 5.378  6.619   -3.129 1.00 39.51 ? 969 GLU A OE1 1 
ATOM   323  O OE2 . GLU A 1 48 ? 6.639  7.578   -1.637 1.00 37.63 ? 969 GLU A OE2 1 
ATOM   324  N N   . PHE A 1 49 ? 4.525  4.273   2.052  1.00 24.55 ? 970 PHE A N   1 
ATOM   325  C CA  . PHE A 1 49 ? 3.456  3.286   2.101  1.00 25.97 ? 970 PHE A CA  1 
ATOM   326  C C   . PHE A 1 49 ? 2.610  3.345   3.363  1.00 27.21 ? 970 PHE A C   1 
ATOM   327  O O   . PHE A 1 49 ? 1.783  2.479   3.595  1.00 26.50 ? 970 PHE A O   1 
ATOM   328  C CB  . PHE A 1 49 ? 4.023  1.890   1.831  1.00 26.09 ? 970 PHE A CB  1 
ATOM   329  C CG  . PHE A 1 49 ? 4.629  1.769   0.463  1.00 26.16 ? 970 PHE A CG  1 
ATOM   330  C CD1 . PHE A 1 49 ? 3.808  1.628   -0.664 1.00 26.05 ? 970 PHE A CD1 1 
ATOM   331  C CD2 . PHE A 1 49 ? 6.009  1.856   0.286  1.00 26.32 ? 970 PHE A CD2 1 
ATOM   332  C CE1 . PHE A 1 49 ? 4.364  1.557   -1.939 1.00 24.95 ? 970 PHE A CE1 1 
ATOM   333  C CE2 . PHE A 1 49 ? 6.577  1.763   -1.002 1.00 28.33 ? 970 PHE A CE2 1 
ATOM   334  C CZ  . PHE A 1 49 ? 5.745  1.613   -2.107 1.00 27.54 ? 970 PHE A CZ  1 
ATOM   335  N N   . ALA A 1 50 ? 2.812  4.398   4.158  1.00 29.22 ? 971 ALA A N   1 
ATOM   336  C CA  . ALA A 1 50 ? 1.981  4.693   5.334  1.00 30.95 ? 971 ALA A CA  1 
ATOM   337  C C   . ALA A 1 50 ? 0.496  4.713   4.985  1.00 32.25 ? 971 ALA A C   1 
ATOM   338  O O   . ALA A 1 50 ? 0.099  5.245   3.938  1.00 32.15 ? 971 ALA A O   1 
ATOM   339  C CB  . ALA A 1 50 ? 2.394  6.027   5.952  1.00 30.98 ? 971 ALA A CB  1 
ATOM   340  N N   . PHE A 1 51 ? -0.302 4.096   5.858  1.00 33.86 ? 972 PHE A N   1 
ATOM   341  C CA  . PHE A 1 51 ? -1.773 4.142   5.799  1.00 34.87 ? 972 PHE A CA  1 
ATOM   342  C C   . PHE A 1 51 ? -2.341 4.236   7.217  1.00 35.41 ? 972 PHE A C   1 
ATOM   343  O O   . PHE A 1 51 ? -2.067 3.351   8.036  1.00 35.98 ? 972 PHE A O   1 
ATOM   344  C CB  . PHE A 1 51 ? -2.356 2.909   5.090  1.00 35.34 ? 972 PHE A CB  1 
ATOM   345  C CG  . PHE A 1 51 ? -3.854 2.735   5.300  1.00 35.30 ? 972 PHE A CG  1 
ATOM   346  C CD1 . PHE A 1 51 ? -4.354 1.620   5.991  1.00 36.88 ? 972 PHE A CD1 1 
ATOM   347  C CD2 . PHE A 1 51 ? -4.757 3.690   4.824  1.00 35.91 ? 972 PHE A CD2 1 
ATOM   348  C CE1 . PHE A 1 51 ? -5.755 1.436   6.202  1.00 36.25 ? 972 PHE A CE1 1 
ATOM   349  C CE2 . PHE A 1 51 ? -6.152 3.528   5.025  1.00 37.16 ? 972 PHE A CE2 1 
ATOM   350  C CZ  . PHE A 1 51 ? -6.655 2.390   5.723  1.00 36.52 ? 972 PHE A CZ  1 
ATOM   351  N N   . MET B 2 1  ? 20.321 -9.325  38.937 1.00 15.91 ? 1   MET B N   1 
ATOM   352  C CA  . MET B 2 1  ? 21.299 -9.028  37.853 1.00 16.40 ? 1   MET B CA  1 
ATOM   353  C C   . MET B 2 1  ? 20.905 -7.682  37.267 1.00 15.70 ? 1   MET B C   1 
ATOM   354  O O   . MET B 2 1  ? 19.831 -7.153  37.582 1.00 16.27 ? 1   MET B O   1 
ATOM   355  C CB  . MET B 2 1  ? 21.305 -10.119 36.761 1.00 16.69 ? 1   MET B CB  1 
ATOM   356  C CG  . MET B 2 1  ? 20.079 -10.100 35.815 1.00 17.98 ? 1   MET B CG  1 
ATOM   357  S SD  . MET B 2 1  ? 20.020 -11.386 34.565 1.00 19.50 ? 1   MET B SD  1 
ATOM   358  C CE  . MET B 2 1  ? 18.488 -11.049 33.684 1.00 17.01 ? 1   MET B CE  1 
ATOM   359  N N   . GLN B 2 2  ? 21.791 -7.106  36.469 1.00 14.74 ? 2   GLN B N   1 
ATOM   360  C CA  . GLN B 2 2  ? 21.512 -5.795  35.892 1.00 14.23 ? 2   GLN B CA  1 
ATOM   361  C C   . GLN B 2 2  ? 21.237 -5.914  34.401 1.00 12.75 ? 2   GLN B C   1 
ATOM   362  O O   . GLN B 2 2  ? 21.849 -6.714  33.695 1.00 13.93 ? 2   GLN B O   1 
ATOM   363  C CB  . GLN B 2 2  ? 22.687 -4.843  36.133 1.00 14.95 ? 2   GLN B CB  1 
ATOM   364  C CG  . GLN B 2 2  ? 22.796 -4.411  37.590 1.00 18.19 ? 2   GLN B CG  1 
ATOM   365  C CD  . GLN B 2 2  ? 23.895 -3.378  37.781 1.00 22.13 ? 2   GLN B CD  1 
ATOM   366  O OE1 . GLN B 2 2  ? 24.858 -3.319  36.991 1.00 23.72 ? 2   GLN B OE1 1 
ATOM   367  N NE2 . GLN B 2 2  ? 23.733 -2.534  38.778 1.00 24.57 ? 2   GLN B NE2 1 
ATOM   368  N N   . ILE B 2 3  ? 20.286 -5.118  33.931 1.00 12.78 ? 3   ILE B N   1 
ATOM   369  C CA  . ILE B 2 3  ? 20.130 -4.925  32.491 1.00 11.71 ? 3   ILE B CA  1 
ATOM   370  C C   . ILE B 2 3  ? 20.059 -3.410  32.263 1.00 11.58 ? 3   ILE B C   1 
ATOM   371  O O   . ILE B 2 3  ? 19.826 -2.633  33.208 1.00 11.80 ? 3   ILE B O   1 
ATOM   372  C CB  . ILE B 2 3  ? 18.851 -5.654  31.903 1.00 11.23 ? 3   ILE B CB  1 
ATOM   373  C CG1 . ILE B 2 3  ? 17.584 -5.070  32.515 1.00 11.17 ? 3   ILE B CG1 1 
ATOM   374  C CG2 . ILE B 2 3  ? 18.933 -7.205  32.098 1.00 9.27  ? 3   ILE B CG2 1 
ATOM   375  C CD1 . ILE B 2 3  ? 16.283 -5.463  31.734 1.00 13.21 ? 3   ILE B CD1 1 
ATOM   376  N N   . PHE B 2 4  ? 20.244 -3.008  31.012 1.00 11.67 ? 4   PHE B N   1 
ATOM   377  C CA  . PHE B 2 4  ? 20.170 -1.599  30.620 1.00 12.26 ? 4   PHE B CA  1 
ATOM   378  C C   . PHE B 2 4  ? 19.021 -1.347  29.680 1.00 11.72 ? 4   PHE B C   1 
ATOM   379  O O   . PHE B 2 4  ? 18.667 -2.199  28.896 1.00 12.11 ? 4   PHE B O   1 
ATOM   380  C CB  . PHE B 2 4  ? 21.488 -1.156  29.947 1.00 11.90 ? 4   PHE B CB  1 
ATOM   381  C CG  . PHE B 2 4  ? 22.704 -1.530  30.759 1.00 12.69 ? 4   PHE B CG  1 
ATOM   382  C CD1 . PHE B 2 4  ? 23.541 -2.564  30.356 1.00 15.11 ? 4   PHE B CD1 1 
ATOM   383  C CD2 . PHE B 2 4  ? 22.936 -0.902  31.981 1.00 15.48 ? 4   PHE B CD2 1 
ATOM   384  C CE1 . PHE B 2 4  ? 24.653 -2.943  31.146 1.00 12.97 ? 4   PHE B CE1 1 
ATOM   385  C CE2 . PHE B 2 4  ? 24.035 -1.287  32.798 1.00 15.06 ? 4   PHE B CE2 1 
ATOM   386  C CZ  . PHE B 2 4  ? 24.870 -2.308  32.372 1.00 12.98 ? 4   PHE B CZ  1 
ATOM   387  N N   . VAL B 2 5  ? 18.476 -0.141  29.757 1.00 12.97 ? 5   VAL B N   1 
ATOM   388  C CA  . VAL B 2 5  ? 17.427 0.305   28.835 1.00 12.93 ? 5   VAL B CA  1 
ATOM   389  C C   . VAL B 2 5  ? 17.846 1.658   28.252 1.00 12.96 ? 5   VAL B C   1 
ATOM   390  O O   . VAL B 2 5  ? 18.009 2.625   28.978 1.00 14.02 ? 5   VAL B O   1 
ATOM   391  C CB  . VAL B 2 5  ? 16.040 0.423   29.538 1.00 13.18 ? 5   VAL B CB  1 
ATOM   392  C CG1 . VAL B 2 5  ? 14.976 0.899   28.508 1.00 13.28 ? 5   VAL B CG1 1 
ATOM   393  C CG2 . VAL B 2 5  ? 15.622 -0.923  30.172 1.00 12.09 ? 5   VAL B CG2 1 
ATOM   394  N N   . LYS B 2 6  ? 18.068 1.675   26.947 1.00 12.80 ? 6   LYS B N   1 
ATOM   395  C CA  . LYS B 2 6  ? 18.452 2.871   26.195 1.00 14.00 ? 6   LYS B CA  1 
ATOM   396  C C   . LYS B 2 6  ? 17.207 3.571   25.690 1.00 13.97 ? 6   LYS B C   1 
ATOM   397  O O   . LYS B 2 6  ? 16.349 2.923   25.088 1.00 12.79 ? 6   LYS B O   1 
ATOM   398  C CB  . LYS B 2 6  ? 19.285 2.428   25.005 1.00 13.69 ? 6   LYS B CB  1 
ATOM   399  C CG  . LYS B 2 6  ? 19.708 3.496   24.002 1.00 20.23 ? 6   LYS B CG  1 
ATOM   400  C CD  . LYS B 2 6  ? 20.974 2.989   23.329 1.00 29.71 ? 6   LYS B CD  1 
ATOM   401  C CE  . LYS B 2 6  ? 21.015 3.192   21.783 1.00 31.41 ? 6   LYS B CE  1 
ATOM   402  N NZ  . LYS B 2 6  ? 21.969 2.227   21.172 1.00 28.51 ? 6   LYS B NZ  1 
ATOM   403  N N   . THR B 2 7  ? 17.114 4.890   25.926 1.00 13.01 ? 7   THR B N   1 
ATOM   404  C CA  . THR B 2 7  ? 15.955 5.683   25.458 1.00 13.24 ? 7   THR B CA  1 
ATOM   405  C C   . THR B 2 7  ? 16.374 6.496   24.228 1.00 13.62 ? 7   THR B C   1 
ATOM   406  O O   . THR B 2 7  ? 17.570 6.659   23.974 1.00 13.94 ? 7   THR B O   1 
ATOM   407  C CB  . THR B 2 7  ? 15.444 6.644   26.529 1.00 12.98 ? 7   THR B CB  1 
ATOM   408  O OG1 . THR B 2 7  ? 16.372 7.736   26.633 1.00 14.88 ? 7   THR B OG1 1 
ATOM   409  C CG2 . THR B 2 7  ? 15.282 5.922   27.921 1.00 14.12 ? 7   THR B CG2 1 
ATOM   410  N N   . LEU B 2 8  ? 15.407 7.033   23.483 1.00 13.25 ? 8   LEU B N   1 
ATOM   411  C CA  . LEU B 2 8  ? 15.754 7.760   22.274 1.00 15.24 ? 8   LEU B CA  1 
ATOM   412  C C   . LEU B 2 8  ? 16.339 9.148   22.562 1.00 16.60 ? 8   LEU B C   1 
ATOM   413  O O   . LEU B 2 8  ? 16.873 9.799   21.653 1.00 15.75 ? 8   LEU B O   1 
ATOM   414  C CB  . LEU B 2 8  ? 14.545 7.870   21.332 1.00 14.86 ? 8   LEU B CB  1 
ATOM   415  C CG  . LEU B 2 8  ? 14.107 6.528   20.732 1.00 15.58 ? 8   LEU B CG  1 
ATOM   416  C CD1 . LEU B 2 8  ? 12.753 6.631   20.075 1.00 17.48 ? 8   LEU B CD1 1 
ATOM   417  C CD2 . LEU B 2 8  ? 15.161 6.117   19.698 1.00 16.07 ? 8   LEU B CD2 1 
ATOM   418  N N   . THR B 2 9  ? 16.202 9.602   23.805 1.00 18.43 ? 9   THR B N   1 
ATOM   419  C CA  . THR B 2 9  ? 16.784 10.888  24.216 1.00 20.26 ? 9   THR B CA  1 
ATOM   420  C C   . THR B 2 9  ? 18.248 10.739  24.626 1.00 21.05 ? 9   THR B C   1 
ATOM   421  O O   . THR B 2 9  ? 18.882 11.714  25.030 1.00 22.09 ? 9   THR B O   1 
ATOM   422  C CB  . THR B 2 9  ? 15.991 11.564  25.345 1.00 20.11 ? 9   THR B CB  1 
ATOM   423  O OG1 . THR B 2 9  ? 16.061 10.777  26.554 1.00 21.14 ? 9   THR B OG1 1 
ATOM   424  C CG2 . THR B 2 9  ? 14.558 11.751  24.910 1.00 19.69 ? 9   THR B CG2 1 
ATOM   425  N N   . GLY B 2 10 ? 18.769 9.527   24.482 1.00 19.19 ? 10  GLY B N   1 
ATOM   426  C CA  . GLY B 2 10 ? 20.146 9.197   24.802 1.00 20.20 ? 10  GLY B CA  1 
ATOM   427  C C   . GLY B 2 10 ? 20.370 8.687   26.216 1.00 19.93 ? 10  GLY B C   1 
ATOM   428  O O   . GLY B 2 10 ? 21.514 8.465   26.602 1.00 20.74 ? 10  GLY B O   1 
ATOM   429  N N   . LYS B 2 11 ? 19.306 8.554   27.019 1.00 18.89 ? 11  LYS B N   1 
ATOM   430  C CA  . LYS B 2 11 ? 19.500 8.068   28.399 1.00 19.18 ? 11  LYS B CA  1 
ATOM   431  C C   . LYS B 2 11 ? 19.715 6.546   28.457 1.00 18.08 ? 11  LYS B C   1 
ATOM   432  O O   . LYS B 2 11 ? 19.099 5.819   27.671 1.00 18.04 ? 11  LYS B O   1 
ATOM   433  C CB  . LYS B 2 11 ? 18.351 8.474   29.346 1.00 19.46 ? 11  LYS B CB  1 
ATOM   434  C CG  . LYS B 2 11 ? 18.521 7.807   30.728 1.00 24.05 ? 11  LYS B CG  1 
ATOM   435  C CD  . LYS B 2 11 ? 17.949 8.515   31.931 1.00 31.27 ? 11  LYS B CD  1 
ATOM   436  C CE  . LYS B 2 11 ? 18.931 8.427   33.159 1.00 33.41 ? 11  LYS B CE  1 
ATOM   437  N NZ  . LYS B 2 11 ? 19.517 7.078   33.510 1.00 33.80 ? 11  LYS B NZ  1 
ATOM   438  N N   . THR B 2 12 ? 20.602 6.091   29.361 1.00 16.97 ? 12  THR B N   1 
ATOM   439  C CA  . THR B 2 12 ? 20.765 4.664   29.717 1.00 16.20 ? 12  THR B CA  1 
ATOM   440  C C   . THR B 2 12 ? 20.286 4.452   31.164 1.00 16.98 ? 12  THR B C   1 
ATOM   441  O O   . THR B 2 12 ? 20.892 4.972   32.132 1.00 17.54 ? 12  THR B O   1 
ATOM   442  C CB  . THR B 2 12 ? 22.215 4.180   29.600 1.00 16.18 ? 12  THR B CB  1 
ATOM   443  O OG1 . THR B 2 12 ? 22.655 4.288   28.241 1.00 15.87 ? 12  THR B OG1 1 
ATOM   444  C CG2 . THR B 2 12 ? 22.359 2.692   30.042 1.00 17.82 ? 12  THR B CG2 1 
ATOM   445  N N   . ILE B 2 13 ? 19.191 3.713   31.301 1.00 15.35 ? 13  ILE B N   1 
ATOM   446  C CA  . ILE B 2 13 ? 18.602 3.373   32.594 1.00 15.55 ? 13  ILE B CA  1 
ATOM   447  C C   . ILE B 2 13 ? 19.157 2.005   32.996 1.00 14.70 ? 13  ILE B C   1 
ATOM   448  O O   . ILE B 2 13 ? 19.183 1.108   32.173 1.00 13.51 ? 13  ILE B O   1 
ATOM   449  C CB  . ILE B 2 13 ? 17.055 3.271   32.470 1.00 15.31 ? 13  ILE B CB  1 
ATOM   450  C CG1 . ILE B 2 13 ? 16.469 4.570   31.870 1.00 17.04 ? 13  ILE B CG1 1 
ATOM   451  C CG2 . ILE B 2 13 ? 16.414 2.926   33.820 1.00 16.42 ? 13  ILE B CG2 1 
ATOM   452  C CD1 . ILE B 2 13 ? 15.091 4.425   31.274 1.00 19.50 ? 13  ILE B CD1 1 
ATOM   453  N N   . THR B 2 14 ? 19.614 1.861   34.237 1.00 13.93 ? 14  THR B N   1 
ATOM   454  C CA  . THR B 2 14 ? 20.043 0.539   34.723 1.00 14.56 ? 14  THR B CA  1 
ATOM   455  C C   . THR B 2 14 ? 18.952 -0.013  35.627 1.00 14.87 ? 14  THR B C   1 
ATOM   456  O O   . THR B 2 14 ? 18.435 0.696   36.510 1.00 15.34 ? 14  THR B O   1 
ATOM   457  C CB  . THR B 2 14 ? 21.367 0.617   35.511 1.00 15.33 ? 14  THR B CB  1 
ATOM   458  O OG1 . THR B 2 14 ? 22.364 1.190   34.676 1.00 14.53 ? 14  THR B OG1 1 
ATOM   459  C CG2 . THR B 2 14 ? 21.848 -0.795  35.914 1.00 15.54 ? 14  THR B CG2 1 
ATOM   460  N N   . LEU B 2 15 ? 18.588 -1.275  35.408 1.00 13.90 ? 15  LEU B N   1 
ATOM   461  C CA  . LEU B 2 15 ? 17.535 -1.891  36.207 1.00 14.97 ? 15  LEU B CA  1 
ATOM   462  C C   . LEU B 2 15 ? 18.125 -3.053  36.960 1.00 14.85 ? 15  LEU B C   1 
ATOM   463  O O   . LEU B 2 15 ? 19.019 -3.723  36.445 1.00 14.36 ? 15  LEU B O   1 
ATOM   464  C CB  . LEU B 2 15 ? 16.443 -2.420  35.279 1.00 14.12 ? 15  LEU B CB  1 
ATOM   465  C CG  . LEU B 2 15 ? 15.231 -1.579  34.875 1.00 18.21 ? 15  LEU B CG  1 
ATOM   466  C CD1 . LEU B 2 15 ? 15.116 -0.048  35.311 1.00 13.78 ? 15  LEU B CD1 1 
ATOM   467  C CD2 . LEU B 2 15 ? 14.719 -1.962  33.470 1.00 15.04 ? 15  LEU B CD2 1 
ATOM   468  N N   . GLU B 2 16 ? 17.585 -3.287  38.151 1.00 14.77 ? 16  GLU B N   1 
ATOM   469  C CA  . GLU B 2 16 ? 17.862 -4.469  38.966 1.00 16.25 ? 16  GLU B CA  1 
ATOM   470  C C   . GLU B 2 16 ? 16.737 -5.492  38.754 1.00 16.07 ? 16  GLU B C   1 
ATOM   471  O O   . GLU B 2 16 ? 15.584 -5.227  39.081 1.00 17.13 ? 16  GLU B O   1 
ATOM   472  C CB  . GLU B 2 16 ? 17.880 -4.025  40.423 1.00 17.13 ? 16  GLU B CB  1 
ATOM   473  C CG  . GLU B 2 16 ? 18.931 -4.662  41.287 1.00 23.20 ? 16  GLU B CG  1 
ATOM   474  C CD  . GLU B 2 16 ? 20.347 -4.659  40.685 1.00 23.29 ? 16  GLU B CD  1 
ATOM   475  O OE1 . GLU B 2 16 ? 21.108 -3.625  40.657 1.00 25.58 ? 16  GLU B OE1 1 
ATOM   476  O OE2 . GLU B 2 16 ? 20.690 -5.752  40.256 1.00 24.18 ? 16  GLU B OE2 1 
ATOM   477  N N   . VAL B 2 17 ? 17.066 -6.629  38.169 1.00 15.60 ? 17  VAL B N   1 
ATOM   478  C CA  . VAL B 2 17 ? 16.038 -7.594  37.731 1.00 15.51 ? 17  VAL B CA  1 
ATOM   479  C C   . VAL B 2 17 ? 16.452 -9.035  38.048 1.00 16.38 ? 17  VAL B C   1 
ATOM   480  O O   . VAL B 2 17 ? 17.625 -9.301  38.332 1.00 17.00 ? 17  VAL B O   1 
ATOM   481  C CB  . VAL B 2 17 ? 15.721 -7.452  36.193 1.00 14.95 ? 17  VAL B CB  1 
ATOM   482  C CG1 . VAL B 2 17 ? 15.222 -6.034  35.841 1.00 13.62 ? 17  VAL B CG1 1 
ATOM   483  C CG2 . VAL B 2 17 ? 16.950 -7.822  35.326 1.00 14.38 ? 17  VAL B CG2 1 
ATOM   484  N N   . GLU B 2 18 ? 15.497 -9.963  37.974 1.00 16.26 ? 18  GLU B N   1 
ATOM   485  C CA  . GLU B 2 18 ? 15.820 -11.380 37.980 1.00 17.82 ? 18  GLU B CA  1 
ATOM   486  C C   . GLU B 2 18 ? 15.400 -11.942 36.640 1.00 17.52 ? 18  GLU B C   1 
ATOM   487  O O   . GLU B 2 18 ? 14.523 -11.365 36.004 1.00 16.89 ? 18  GLU B O   1 
ATOM   488  C CB  . GLU B 2 18 ? 15.067 -12.101 39.128 1.00 19.08 ? 18  GLU B CB  1 
ATOM   489  C CG  . GLU B 2 18 ? 15.542 -11.721 40.530 1.00 23.64 ? 18  GLU B CG  1 
ATOM   490  C CD  . GLU B 2 18 ? 17.028 -11.973 40.789 1.00 28.22 ? 18  GLU B CD  1 
ATOM   491  O OE1 . GLU B 2 18 ? 17.675 -12.767 40.078 1.00 34.41 ? 18  GLU B OE1 1 
ATOM   492  O OE2 . GLU B 2 18 ? 17.567 -11.361 41.717 1.00 32.93 ? 18  GLU B OE2 1 
ATOM   493  N N   . PRO B 2 19 ? 16.000 -13.079 36.205 1.00 17.76 ? 19  PRO B N   1 
ATOM   494  C CA  . PRO B 2 19 ? 15.601 -13.705 34.948 1.00 17.64 ? 19  PRO B CA  1 
ATOM   495  C C   . PRO B 2 19 ? 14.102 -13.986 34.845 1.00 16.53 ? 19  PRO B C   1 
ATOM   496  O O   . PRO B 2 19 ? 13.555 -13.923 33.755 1.00 16.64 ? 19  PRO B O   1 
ATOM   497  C CB  . PRO B 2 19 ? 16.400 -15.025 34.964 1.00 17.83 ? 19  PRO B CB  1 
ATOM   498  C CG  . PRO B 2 19 ? 17.640 -14.650 35.706 1.00 20.25 ? 19  PRO B CG  1 
ATOM   499  C CD  . PRO B 2 19 ? 17.104 -13.833 36.849 1.00 18.14 ? 19  PRO B CD  1 
ATOM   500  N N   . SER B 2 20 ? 13.447 -14.260 35.975 1.00 16.01 ? 20  SER B N   1 
ATOM   501  C CA  . SER B 2 20 ? 12.006 -14.581 36.005 1.00 16.35 ? 20  SER B CA  1 
ATOM   502  C C   . SER B 2 20 ? 11.091 -13.358 35.996 1.00 16.55 ? 20  SER B C   1 
ATOM   503  O O   . SER B 2 20 ? 9.862  -13.504 35.968 1.00 15.67 ? 20  SER B O   1 
ATOM   504  C CB  . SER B 2 20 ? 11.702 -15.445 37.259 1.00 16.18 ? 20  SER B CB  1 
ATOM   505  O OG  . SER B 2 20 ? 12.043 -14.709 38.434 1.00 16.54 ? 20  SER B OG  1 
ATOM   506  N N   . ASP B 2 21 ? 11.659 -12.144 36.052 1.00 16.21 ? 21  ASP B N   1 
ATOM   507  C CA  . ASP B 2 21 ? 10.830 -10.924 36.009 1.00 16.71 ? 21  ASP B CA  1 
ATOM   508  C C   . ASP B 2 21 ? 10.072 -10.896 34.687 1.00 16.47 ? 21  ASP B C   1 
ATOM   509  O O   . ASP B 2 21 ? 10.676 -11.103 33.613 1.00 15.25 ? 21  ASP B O   1 
ATOM   510  C CB  . ASP B 2 21 ? 11.670 -9.626  36.155 1.00 16.96 ? 21  ASP B CB  1 
ATOM   511  C CG  . ASP B 2 21 ? 12.139 -9.360  37.593 1.00 20.97 ? 21  ASP B CG  1 
ATOM   512  O OD1 . ASP B 2 21 ? 11.796 -10.126 38.511 1.00 25.48 ? 21  ASP B OD1 1 
ATOM   513  O OD2 . ASP B 2 21 ? 12.862 -8.372  37.800 1.00 20.86 ? 21  ASP B OD2 1 
ATOM   514  N N   . THR B 2 22 ? 8.771  -10.611 34.767 1.00 16.43 ? 22  THR B N   1 
ATOM   515  C CA  . THR B 2 22 ? 7.955  -10.412 33.564 1.00 16.21 ? 22  THR B CA  1 
ATOM   516  C C   . THR B 2 22 ? 8.250  -9.091  32.916 1.00 15.80 ? 22  THR B C   1 
ATOM   517  O O   . THR B 2 22 ? 8.744  -8.196  33.574 1.00 14.79 ? 22  THR B O   1 
ATOM   518  C CB  . THR B 2 22 ? 6.443  -10.454 33.847 1.00 17.05 ? 22  THR B CB  1 
ATOM   519  O OG1 . THR B 2 22 ? 6.044  -9.344  34.666 1.00 17.18 ? 22  THR B OG1 1 
ATOM   520  C CG2 . THR B 2 22 ? 6.110  -11.763 34.518 1.00 19.08 ? 22  THR B CG2 1 
ATOM   521  N N   . ILE B 2 23 ? 7.883  -8.953  31.642 1.00 14.89 ? 23  ILE B N   1 
ATOM   522  C CA  . ILE B 2 23 ? 8.051  -7.697  30.942 1.00 15.50 ? 23  ILE B CA  1 
ATOM   523  C C   . ILE B 2 23 ? 7.244  -6.592  31.655 1.00 15.93 ? 23  ILE B C   1 
ATOM   524  O O   . ILE B 2 23 ? 7.703  -5.453  31.758 1.00 15.88 ? 23  ILE B O   1 
ATOM   525  C CB  . ILE B 2 23 ? 7.691  -7.825  29.446 1.00 15.10 ? 23  ILE B CB  1 
ATOM   526  C CG1 . ILE B 2 23 ? 8.600  -8.868  28.757 1.00 15.06 ? 23  ILE B CG1 1 
ATOM   527  C CG2 . ILE B 2 23 ? 7.818  -6.463  28.726 1.00 16.29 ? 23  ILE B CG2 1 
ATOM   528  C CD1 . ILE B 2 23 ? 10.102 -8.661  29.000 1.00 15.53 ? 23  ILE B CD1 1 
ATOM   529  N N   . GLU B 2 24 ? 6.063  -6.930  32.170 1.00 15.42 ? 24  GLU B N   1 
ATOM   530  C CA  . GLU B 2 24 ? 5.291  -5.936  32.917 1.00 17.03 ? 24  GLU B CA  1 
ATOM   531  C C   . GLU B 2 24 ? 6.033  -5.475  34.183 1.00 16.28 ? 24  GLU B C   1 
ATOM   532  O O   . GLU B 2 24 ? 6.012  -4.289  34.507 1.00 16.62 ? 24  GLU B O   1 
ATOM   533  C CB  . GLU B 2 24 ? 3.891  -6.472  33.265 1.00 17.92 ? 24  GLU B CB  1 
ATOM   534  C CG  . GLU B 2 24 ? 2.949  -5.431  33.925 1.00 23.25 ? 24  GLU B CG  1 
ATOM   535  C CD  . GLU B 2 24 ? 2.451  -4.325  32.966 1.00 26.62 ? 24  GLU B CD  1 
ATOM   536  O OE1 . GLU B 2 24 ? 2.527  -4.438  31.729 1.00 29.92 ? 24  GLU B OE1 1 
ATOM   537  O OE2 . GLU B 2 24 ? 1.962  -3.307  33.467 1.00 30.11 ? 24  GLU B OE2 1 
ATOM   538  N N   . ASN B 2 25 ? 6.655  -6.409  34.899 1.00 16.22 ? 25  ASN B N   1 
ATOM   539  C CA  . ASN B 2 25 ? 7.526  -6.083  36.031 1.00 16.41 ? 25  ASN B CA  1 
ATOM   540  C C   . ASN B 2 25 ? 8.602  -5.061  35.587 1.00 15.60 ? 25  ASN B C   1 
ATOM   541  O O   . ASN B 2 25 ? 8.905  -4.097  36.306 1.00 15.08 ? 25  ASN B O   1 
ATOM   542  C CB  . ASN B 2 25 ? 8.282  -7.327  36.564 1.00 16.96 ? 25  ASN B CB  1 
ATOM   543  C CG  . ASN B 2 25 ? 7.413  -8.334  37.363 1.00 21.32 ? 25  ASN B CG  1 
ATOM   544  O OD1 . ASN B 2 25 ? 7.842  -9.512  37.609 1.00 22.35 ? 25  ASN B OD1 1 
ATOM   545  N ND2 . ASN B 2 25 ? 6.232  -7.910  37.773 1.00 21.97 ? 25  ASN B ND2 1 
ATOM   546  N N   . VAL B 2 26 ? 9.227  -5.328  34.436 1.00 14.67 ? 26  VAL B N   1 
ATOM   547  C CA  . VAL B 2 26 ? 10.305 -4.467  33.933 1.00 14.54 ? 26  VAL B CA  1 
ATOM   548  C C   . VAL B 2 26 ? 9.775  -3.046  33.646 1.00 15.03 ? 26  VAL B C   1 
ATOM   549  O O   . VAL B 2 26 ? 10.411 -2.029  33.993 1.00 14.94 ? 26  VAL B O   1 
ATOM   550  C CB  . VAL B 2 26 ? 10.979 -5.095  32.701 1.00 14.22 ? 26  VAL B CB  1 
ATOM   551  C CG1 . VAL B 2 26 ? 11.804 -4.071  31.936 1.00 15.08 ? 26  VAL B CG1 1 
ATOM   552  C CG2 . VAL B 2 26 ? 11.841 -6.296  33.129 1.00 15.55 ? 26  VAL B CG2 1 
ATOM   553  N N   . LYS B 2 27 ? 8.605  -2.991  33.020 1.00 14.54 ? 27  LYS B N   1 
ATOM   554  C CA  . LYS B 2 27 ? 7.909  -1.722  32.764 1.00 14.54 ? 27  LYS B CA  1 
ATOM   555  C C   . LYS B 2 27 ? 7.617  -0.940  34.046 1.00 15.23 ? 27  LYS B C   1 
ATOM   556  O O   . LYS B 2 27 ? 7.796  0.282   34.094 1.00 15.55 ? 27  LYS B O   1 
ATOM   557  C CB  . LYS B 2 27 ? 6.620  -2.007  31.995 1.00 15.49 ? 27  LYS B CB  1 
ATOM   558  C CG  . LYS B 2 27 ? 6.895  -2.394  30.518 1.00 14.74 ? 27  LYS B CG  1 
ATOM   559  C CD  . LYS B 2 27 ? 5.561  -2.647  29.710 1.00 14.76 ? 27  LYS B CD  1 
ATOM   560  C CE  . LYS B 2 27 ? 5.846  -3.019  28.255 1.00 15.49 ? 27  LYS B CE  1 
ATOM   561  N NZ  . LYS B 2 27 ? 4.525  -2.903  27.576 1.00 21.95 ? 27  LYS B NZ  1 
ATOM   562  N N   . ALA B 2 28 ? 7.185  -1.660  35.081 1.00 14.94 ? 28  ALA B N   1 
ATOM   563  C CA  . ALA B 2 28 ? 6.938  -1.087  36.411 1.00 15.55 ? 28  ALA B CA  1 
ATOM   564  C C   . ALA B 2 28 ? 8.223  -0.495  37.024 1.00 15.22 ? 28  ALA B C   1 
ATOM   565  O O   . ALA B 2 28 ? 8.191  0.585   37.606 1.00 15.26 ? 28  ALA B O   1 
ATOM   566  C CB  . ALA B 2 28 ? 6.317  -2.161  37.330 1.00 16.07 ? 28  ALA B CB  1 
ATOM   567  N N   . LYS B 2 29 ? 9.342  -1.204  36.892 1.00 14.81 ? 29  LYS B N   1 
ATOM   568  C CA  . LYS B 2 29 ? 10.652 -0.682  37.334 1.00 14.63 ? 29  LYS B CA  1 
ATOM   569  C C   . LYS B 2 29 ? 11.085 0.565   36.579 1.00 15.05 ? 29  LYS B C   1 
ATOM   570  O O   . LYS B 2 29 ? 11.622 1.500   37.157 1.00 14.93 ? 29  LYS B O   1 
ATOM   571  C CB  . LYS B 2 29 ? 11.731 -1.764  37.181 1.00 14.83 ? 29  LYS B CB  1 
ATOM   572  C CG  . LYS B 2 29 ? 11.565 -2.939  38.133 1.00 15.17 ? 29  LYS B CG  1 
ATOM   573  C CD  . LYS B 2 29 ? 12.550 -4.041  37.802 1.00 17.16 ? 29  LYS B CD  1 
ATOM   574  C CE  . LYS B 2 29 ? 12.213 -5.304  38.547 1.00 20.24 ? 29  LYS B CE  1 
ATOM   575  N NZ  . LYS B 2 29 ? 12.605 -5.104  39.938 1.00 23.73 ? 29  LYS B NZ  1 
ATOM   576  N N   . ILE B 2 30 ? 10.886 0.573   35.270 1.00 15.34 ? 30  ILE B N   1 
ATOM   577  C CA  . ILE B 2 30 ? 11.157 1.768   34.476 1.00 15.65 ? 30  ILE B CA  1 
ATOM   578  C C   . ILE B 2 30 ? 10.274 2.938   34.931 1.00 17.37 ? 30  ILE B C   1 
ATOM   579  O O   . ILE B 2 30 ? 10.749 4.083   35.077 1.00 18.37 ? 30  ILE B O   1 
ATOM   580  C CB  . ILE B 2 30 ? 10.946 1.490   32.980 1.00 15.67 ? 30  ILE B CB  1 
ATOM   581  C CG1 . ILE B 2 30 ? 11.958 0.455   32.485 1.00 15.70 ? 30  ILE B CG1 1 
ATOM   582  C CG2 . ILE B 2 30 ? 11.060 2.804   32.162 1.00 15.16 ? 30  ILE B CG2 1 
ATOM   583  C CD1 . ILE B 2 30 ? 11.792 0.123   31.004 1.00 11.25 ? 30  ILE B CD1 1 
ATOM   584  N N   . GLN B 2 31 ? 9.004  2.663   35.178 1.00 18.29 ? 31  GLN B N   1 
ATOM   585  C CA  . GLN B 2 31 ? 8.119  3.688   35.755 1.00 20.51 ? 31  GLN B CA  1 
ATOM   586  C C   . GLN B 2 31 ? 8.627  4.220   37.100 1.00 21.50 ? 31  GLN B C   1 
ATOM   587  O O   . GLN B 2 31 ? 8.598  5.417   37.319 1.00 21.57 ? 31  GLN B O   1 
ATOM   588  C CB  . GLN B 2 31 ? 6.713  3.131   35.943 1.00 20.55 ? 31  GLN B CB  1 
ATOM   589  C CG  . GLN B 2 31 ? 5.721  4.104   36.593 1.00 22.20 ? 31  GLN B CG  1 
ATOM   590  C CD  . GLN B 2 31 ? 4.377  3.475   36.784 1.00 22.00 ? 31  GLN B CD  1 
ATOM   591  O OE1 . GLN B 2 31 ? 4.271  2.268   36.997 1.00 26.92 ? 31  GLN B OE1 1 
ATOM   592  N NE2 . GLN B 2 31 ? 3.329  4.275   36.685 1.00 23.37 ? 31  GLN B NE2 1 
ATOM   593  N N   . ASP B 2 32 ? 9.039  3.329   38.004 1.00 22.74 ? 32  ASP B N   1 
ATOM   594  C CA  . ASP B 2 32 ? 9.551  3.744   39.332 1.00 25.02 ? 32  ASP B CA  1 
ATOM   595  C C   . ASP B 2 32 ? 10.720 4.673   39.203 1.00 26.50 ? 32  ASP B C   1 
ATOM   596  O O   . ASP B 2 32 ? 10.798 5.683   39.902 1.00 26.87 ? 32  ASP B O   1 
ATOM   597  C CB  . ASP B 2 32 ? 9.944  2.548   40.191 1.00 25.21 ? 32  ASP B CB  1 
ATOM   598  C CG  . ASP B 2 32 ? 8.746  1.744   40.632 1.00 26.49 ? 32  ASP B CG  1 
ATOM   599  O OD1 . ASP B 2 32 ? 8.930  0.636   41.159 1.00 28.74 ? 32  ASP B OD1 1 
ATOM   600  O OD2 . ASP B 2 32 ? 7.607  2.221   40.446 1.00 28.32 ? 32  ASP B OD2 1 
ATOM   601  N N   . LYS B 2 33 ? 11.632 4.380   38.292 1.00 28.14 ? 33  LYS B N   1 
ATOM   602  C CA  . LYS B 2 33 ? 12.768 5.278   38.214 1.00 30.00 ? 33  LYS B CA  1 
ATOM   603  C C   . LYS B 2 33 ? 12.706 6.460   37.225 1.00 30.34 ? 33  LYS B C   1 
ATOM   604  O O   . LYS B 2 33 ? 13.441 7.432   37.409 1.00 30.91 ? 33  LYS B O   1 
ATOM   605  C CB  . LYS B 2 33 ? 14.088 4.523   38.217 1.00 30.67 ? 33  LYS B CB  1 
ATOM   606  C CG  . LYS B 2 33 ? 14.464 3.806   36.989 1.00 31.19 ? 33  LYS B CG  1 
ATOM   607  C CD  . LYS B 2 33 ? 15.953 3.581   37.087 1.00 32.07 ? 33  LYS B CD  1 
ATOM   608  C CE  . LYS B 2 33 ? 16.342 2.813   38.335 1.00 31.66 ? 33  LYS B CE  1 
ATOM   609  N NZ  . LYS B 2 33 ? 17.812 2.883   38.485 1.00 31.25 ? 33  LYS B NZ  1 
ATOM   610  N N   . GLU B 2 34 ? 11.787 6.414   36.262 1.00 30.72 ? 34  GLU B N   1 
ATOM   611  C CA  . GLU B 2 34 ? 11.649 7.453   35.240 1.00 31.62 ? 34  GLU B CA  1 
ATOM   612  C C   . GLU B 2 34 ? 10.294 8.164   35.125 1.00 31.65 ? 34  GLU B C   1 
ATOM   613  O O   . GLU B 2 34 ? 10.196 9.194   34.462 1.00 32.00 ? 34  GLU B O   1 
ATOM   614  C CB  . GLU B 2 34 ? 12.047 6.886   33.867 1.00 32.17 ? 34  GLU B CB  1 
ATOM   615  C CG  . GLU B 2 34 ? 13.501 6.419   33.817 1.00 32.97 ? 34  GLU B CG  1 
ATOM   616  C CD  . GLU B 2 34 ? 14.459 7.569   33.652 1.00 37.21 ? 34  GLU B CD  1 
ATOM   617  O OE1 . GLU B 2 34 ? 14.128 8.471   32.841 1.00 38.91 ? 34  GLU B OE1 1 
ATOM   618  O OE2 . GLU B 2 34 ? 15.519 7.586   34.331 1.00 37.72 ? 34  GLU B OE2 1 
ATOM   619  N N   . GLY B 2 35 ? 9.245  7.618   35.727 1.00 31.32 ? 35  GLY B N   1 
ATOM   620  C CA  . GLY B 2 35 ? 7.917  8.229   35.617 1.00 31.36 ? 35  GLY B CA  1 
ATOM   621  C C   . GLY B 2 35 ? 7.029  7.882   34.430 1.00 31.77 ? 35  GLY B C   1 
ATOM   622  O O   . GLY B 2 35 ? 5.921  8.424   34.301 1.00 32.59 ? 35  GLY B O   1 
ATOM   623  N N   . ILE B 2 36 ? 7.478  6.972   33.564 1.00 31.04 ? 36  ILE B N   1 
ATOM   624  C CA  . ILE B 2 36 ? 6.678  6.585   32.409 1.00 30.20 ? 36  ILE B CA  1 
ATOM   625  C C   . ILE B 2 36 ? 5.754  5.436   32.767 1.00 29.37 ? 36  ILE B C   1 
ATOM   626  O O   . ILE B 2 36 ? 6.252  4.397   33.197 1.00 29.40 ? 36  ILE B O   1 
ATOM   627  C CB  . ILE B 2 36 ? 7.576  6.132   31.218 1.00 30.44 ? 36  ILE B CB  1 
ATOM   628  C CG1 . ILE B 2 36 ? 8.696  7.150   30.982 1.00 31.04 ? 36  ILE B CG1 1 
ATOM   629  C CG2 . ILE B 2 36 ? 6.702  5.904   29.954 1.00 29.85 ? 36  ILE B CG2 1 
ATOM   630  C CD1 . ILE B 2 36 ? 10.019 6.576   30.547 1.00 30.80 ? 36  ILE B CD1 1 
ATOM   631  N N   . PRO B 2 37 ? 4.419  5.603   32.567 1.00 28.29 ? 37  PRO B N   1 
ATOM   632  C CA  . PRO B 2 37 ? 3.463  4.528   32.750 1.00 27.75 ? 37  PRO B CA  1 
ATOM   633  C C   . PRO B 2 37 ? 3.795  3.353   31.832 1.00 26.72 ? 37  PRO B C   1 
ATOM   634  O O   . PRO B 2 37 ? 4.243  3.579   30.699 1.00 25.06 ? 37  PRO B O   1 
ATOM   635  C CB  . PRO B 2 37 ? 2.131  5.160   32.341 1.00 27.98 ? 37  PRO B CB  1 
ATOM   636  C CG  . PRO B 2 37 ? 2.349  6.638   32.572 1.00 29.61 ? 37  PRO B CG  1 
ATOM   637  C CD  . PRO B 2 37 ? 3.748  6.847   32.141 1.00 29.11 ? 37  PRO B CD  1 
ATOM   638  N N   . PRO B 2 38 ? 3.630  2.112   32.343 1.00 26.76 ? 38  PRO B N   1 
ATOM   639  C CA  . PRO B 2 38 ? 3.782  0.895   31.552 1.00 27.16 ? 38  PRO B CA  1 
ATOM   640  C C   . PRO B 2 38 ? 3.072  0.916   30.191 1.00 28.28 ? 38  PRO B C   1 
ATOM   641  O O   . PRO B 2 38 ? 3.617  0.388   29.233 1.00 28.29 ? 38  PRO B O   1 
ATOM   642  C CB  . PRO B 2 38 ? 3.233  -0.182  32.477 1.00 27.53 ? 38  PRO B CB  1 
ATOM   643  C CG  . PRO B 2 38 ? 3.655  0.308   33.833 1.00 27.04 ? 38  PRO B CG  1 
ATOM   644  C CD  . PRO B 2 38 ? 3.378  1.796   33.767 1.00 26.73 ? 38  PRO B CD  1 
ATOM   645  N N   . ASP B 2 39 ? 1.892  1.534   30.082 1.00 29.12 ? 39  ASP B N   1 
ATOM   646  C CA  . ASP B 2 39 ? 1.203  1.526   28.784 1.00 29.42 ? 39  ASP B CA  1 
ATOM   647  C C   . ASP B 2 39 ? 1.763  2.486   27.734 1.00 28.73 ? 39  ASP B C   1 
ATOM   648  O O   . ASP B 2 39 ? 1.391  2.397   26.552 1.00 30.24 ? 39  ASP B O   1 
ATOM   649  C CB  . ASP B 2 39 ? -0.316 1.689   28.901 1.00 30.44 ? 39  ASP B CB  1 
ATOM   650  C CG  . ASP B 2 39 ? -0.711 2.815   29.777 1.00 31.39 ? 39  ASP B CG  1 
ATOM   651  O OD1 . ASP B 2 39 ? -1.710 2.618   30.475 1.00 34.65 ? 39  ASP B OD1 1 
ATOM   652  O OD2 . ASP B 2 39 ? -0.037 3.874   29.804 1.00 33.73 ? 39  ASP B OD2 1 
ATOM   653  N N   . GLN B 2 40 ? 2.624  3.407   28.143 1.00 27.04 ? 40  GLN B N   1 
ATOM   654  C CA  . GLN B 2 40 ? 3.356  4.207   27.169 1.00 25.59 ? 40  GLN B CA  1 
ATOM   655  C C   . GLN B 2 40 ? 4.691  3.622   26.712 1.00 22.77 ? 40  GLN B C   1 
ATOM   656  O O   . GLN B 2 40 ? 5.397  4.256   25.942 1.00 21.80 ? 40  GLN B O   1 
ATOM   657  C CB  . GLN B 2 40 ? 3.539  5.623   27.659 1.00 26.47 ? 40  GLN B CB  1 
ATOM   658  C CG  . GLN B 2 40 ? 2.194  6.356   27.593 1.00 30.34 ? 40  GLN B CG  1 
ATOM   659  C CD  . GLN B 2 40 ? 2.044  7.350   28.667 1.00 33.09 ? 40  GLN B CD  1 
ATOM   660  O OE1 . GLN B 2 40 ? 0.974  7.437   29.300 1.00 38.76 ? 40  GLN B OE1 1 
ATOM   661  N NE2 . GLN B 2 40 ? 3.100  8.128   28.908 1.00 34.76 ? 40  GLN B NE2 1 
ATOM   662  N N   . GLN B 2 41 ? 5.010  2.422   27.169 1.00 18.59 ? 41  GLN B N   1 
ATOM   663  C CA  . GLN B 2 41 ? 6.344  1.873   26.962 1.00 16.63 ? 41  GLN B CA  1 
ATOM   664  C C   . GLN B 2 41 ? 6.296  0.780   25.884 1.00 16.44 ? 41  GLN B C   1 
ATOM   665  O O   . GLN B 2 41 ? 5.459  -0.128  25.926 1.00 17.03 ? 41  GLN B O   1 
ATOM   666  C CB  . GLN B 2 41 ? 6.861  1.288   28.272 1.00 15.78 ? 41  GLN B CB  1 
ATOM   667  C CG  . GLN B 2 41 ? 7.216  2.349   29.341 1.00 14.03 ? 41  GLN B CG  1 
ATOM   668  C CD  . GLN B 2 41 ? 7.708  1.710   30.597 1.00 17.41 ? 41  GLN B CD  1 
ATOM   669  O OE1 . GLN B 2 41 ? 8.464  0.736   30.554 1.00 14.32 ? 41  GLN B OE1 1 
ATOM   670  N NE2 . GLN B 2 41 ? 7.260  2.236   31.749 1.00 16.33 ? 41  GLN B NE2 1 
ATOM   671  N N   . ARG B 2 42 ? 7.201  0.852   24.926 1.00 16.11 ? 42  ARG B N   1 
ATOM   672  C CA  . ARG B 2 42 ? 7.443  -0.316  24.072 1.00 15.66 ? 42  ARG B CA  1 
ATOM   673  C C   . ARG B 2 42 ? 8.908  -0.692  24.229 1.00 15.54 ? 42  ARG B C   1 
ATOM   674  O O   . ARG B 2 42 ? 9.776  0.192   24.132 1.00 14.66 ? 42  ARG B O   1 
ATOM   675  C CB  . ARG B 2 42 ? 7.139  0.019   22.624 1.00 17.32 ? 42  ARG B CB  1 
ATOM   676  C CG  . ARG B 2 42 ? 5.684  0.346   22.378 1.00 21.67 ? 42  ARG B CG  1 
ATOM   677  C CD  . ARG B 2 42 ? 4.786  -0.854  22.733 1.00 26.53 ? 42  ARG B CD  1 
ATOM   678  N NE  . ARG B 2 42 ? 3.425  -0.485  22.379 1.00 33.24 ? 42  ARG B NE  1 
ATOM   679  C CZ  . ARG B 2 42 ? 2.576  0.130   23.197 1.00 35.30 ? 42  ARG B CZ  1 
ATOM   680  N NH1 . ARG B 2 42 ? 2.911  0.411   24.452 1.00 36.06 ? 42  ARG B NH1 1 
ATOM   681  N NH2 . ARG B 2 42 ? 1.381  0.468   22.743 1.00 38.14 ? 42  ARG B NH2 1 
ATOM   682  N N   . LEU B 2 43 ? 9.175  -1.975  24.485 1.00 14.42 ? 43  LEU B N   1 
ATOM   683  C CA  . LEU B 2 43 ? 10.552 -2.492  24.637 1.00 13.08 ? 43  LEU B CA  1 
ATOM   684  C C   . LEU B 2 43 ? 10.942 -3.463  23.511 1.00 14.56 ? 43  LEU B C   1 
ATOM   685  O O   . LEU B 2 43 ? 10.197 -4.406  23.174 1.00 15.26 ? 43  LEU B O   1 
ATOM   686  C CB  . LEU B 2 43 ? 10.703 -3.138  26.018 1.00 13.28 ? 43  LEU B CB  1 
ATOM   687  C CG  . LEU B 2 43 ? 10.553 -2.228  27.258 1.00 11.40 ? 43  LEU B CG  1 
ATOM   688  C CD1 . LEU B 2 43 ? 10.383 -3.118  28.538 1.00 11.57 ? 43  LEU B CD1 1 
ATOM   689  C CD2 . LEU B 2 43 ? 11.809 -1.326  27.362 1.00 12.18 ? 43  LEU B CD2 1 
ATOM   690  N N   . ILE B 2 44 ? 12.116 -3.226  22.950 1.00 14.10 ? 44  ILE B N   1 
ATOM   691  C CA  . ILE B 2 44 ? 12.657 -3.927  21.798 1.00 15.53 ? 44  ILE B CA  1 
ATOM   692  C C   . ILE B 2 44 ? 13.939 -4.626  22.266 1.00 14.99 ? 44  ILE B C   1 
ATOM   693  O O   . ILE B 2 44 ? 14.827 -3.998  22.850 1.00 14.40 ? 44  ILE B O   1 
ATOM   694  C CB  . ILE B 2 44 ? 13.020 -2.926  20.653 1.00 15.41 ? 44  ILE B CB  1 
ATOM   695  C CG1 . ILE B 2 44 ? 11.792 -2.097  20.236 1.00 17.78 ? 44  ILE B CG1 1 
ATOM   696  C CG2 . ILE B 2 44 ? 13.679 -3.612  19.426 1.00 16.49 ? 44  ILE B CG2 1 
ATOM   697  C CD1 . ILE B 2 44 ? 10.537 -2.943  19.936 1.00 16.67 ? 44  ILE B CD1 1 
ATOM   698  N N   . PHE B 2 45 ? 14.049 -5.907  21.977 1.00 14.59 ? 45  PHE B N   1 
ATOM   699  C CA  . PHE B 2 45 ? 15.312 -6.597  22.180 1.00 15.95 ? 45  PHE B CA  1 
ATOM   700  C C   . PHE B 2 45 ? 15.434 -7.694  21.147 1.00 15.76 ? 45  PHE B C   1 
ATOM   701  O O   . PHE B 2 45 ? 14.484 -8.479  20.929 1.00 16.96 ? 45  PHE B O   1 
ATOM   702  C CB  . PHE B 2 45 ? 15.438 -7.165  23.609 1.00 16.29 ? 45  PHE B CB  1 
ATOM   703  C CG  . PHE B 2 45 ? 16.732 -7.938  23.858 1.00 17.30 ? 45  PHE B CG  1 
ATOM   704  C CD1 . PHE B 2 45 ? 17.930 -7.265  24.073 1.00 16.45 ? 45  PHE B CD1 1 
ATOM   705  C CD2 . PHE B 2 45 ? 16.740 -9.343  23.825 1.00 18.21 ? 45  PHE B CD2 1 
ATOM   706  C CE1 . PHE B 2 45 ? 19.132 -7.972  24.295 1.00 18.52 ? 45  PHE B CE1 1 
ATOM   707  C CE2 . PHE B 2 45 ? 17.926 -10.054 24.048 1.00 21.91 ? 45  PHE B CE2 1 
ATOM   708  C CZ  . PHE B 2 45 ? 19.125 -9.370  24.266 1.00 19.60 ? 45  PHE B CZ  1 
ATOM   709  N N   . ALA B 2 46 ? 16.586 -7.716  20.494 1.00 16.30 ? 46  ALA B N   1 
ATOM   710  C CA  . ALA B 2 46 ? 16.955 -8.778  19.550 1.00 17.28 ? 46  ALA B CA  1 
ATOM   711  C C   . ALA B 2 46 ? 15.897 -8.954  18.449 1.00 17.99 ? 46  ALA B C   1 
ATOM   712  O O   . ALA B 2 46 ? 15.427 -10.078 18.167 1.00 18.58 ? 46  ALA B O   1 
ATOM   713  C CB  . ALA B 2 46 ? 17.205 -10.078 20.321 1.00 17.19 ? 46  ALA B CB  1 
ATOM   714  N N   . GLY B 2 47 ? 15.514 -7.831  17.833 1.00 17.29 ? 47  GLY B N   1 
ATOM   715  C CA  . GLY B 2 47 ? 14.511 -7.808  16.754 1.00 17.86 ? 47  GLY B CA  1 
ATOM   716  C C   . GLY B 2 47 ? 13.097 -8.229  17.153 1.00 17.41 ? 47  GLY B C   1 
ATOM   717  O O   . GLY B 2 47 ? 12.301 -8.620  16.297 1.00 18.26 ? 47  GLY B O   1 
ATOM   718  N N   . LYS B 2 48 ? 12.793 -8.177  18.445 1.00 17.51 ? 48  LYS B N   1 
ATOM   719  C CA  . LYS B 2 48 ? 11.472 -8.524  18.963 1.00 18.45 ? 48  LYS B CA  1 
ATOM   720  C C   . LYS B 2 48 ? 10.888 -7.429  19.844 1.00 19.17 ? 48  LYS B C   1 
ATOM   721  O O   . LYS B 2 48 ? 11.634 -6.705  20.532 1.00 18.35 ? 48  LYS B O   1 
ATOM   722  C CB  . LYS B 2 48 ? 11.531 -9.830  19.756 1.00 19.20 ? 48  LYS B CB  1 
ATOM   723  C CG  . LYS B 2 48 ? 11.712 -11.093 18.899 1.00 20.13 ? 48  LYS B CG  1 
ATOM   724  C CD  . LYS B 2 48 ? 12.024 -12.281 19.801 1.00 24.25 ? 48  LYS B CD  1 
ATOM   725  C CE  . LYS B 2 48 ? 13.317 -12.025 20.563 1.00 27.33 ? 48  LYS B CE  1 
ATOM   726  N NZ  . LYS B 2 48 ? 14.511 -12.343 19.708 1.00 30.69 ? 48  LYS B NZ  1 
ATOM   727  N N   . GLN B 2 49 ? 9.564  -7.284  19.806 1.00 18.99 ? 49  GLN B N   1 
ATOM   728  C CA  . GLN B 2 49 ? 8.897  -6.375  20.719 1.00 20.14 ? 49  GLN B CA  1 
ATOM   729  C C   . GLN B 2 49 ? 8.431  -7.235  21.895 1.00 20.60 ? 49  GLN B C   1 
ATOM   730  O O   . GLN B 2 49 ? 7.759  -8.245  21.713 1.00 21.08 ? 49  GLN B O   1 
ATOM   731  C CB  . GLN B 2 49 ? 7.737  -5.635  20.039 1.00 20.15 ? 49  GLN B CB  1 
ATOM   732  C CG  . GLN B 2 49 ? 7.228  -4.434  20.869 1.00 22.50 ? 49  GLN B CG  1 
ATOM   733  C CD  . GLN B 2 49 ? 6.088  -3.708  20.192 1.00 22.28 ? 49  GLN B CD  1 
ATOM   734  O OE1 . GLN B 2 49 ? 5.001  -4.284  19.992 1.00 30.17 ? 49  GLN B OE1 1 
ATOM   735  N NE2 . GLN B 2 49 ? 6.304  -2.449  19.845 1.00 19.72 ? 49  GLN B NE2 1 
ATOM   736  N N   . LEU B 2 50 ? 8.815  -6.849  23.101 1.00 19.44 ? 50  LEU B N   1 
ATOM   737  C CA  . LEU B 2 50 ? 8.647  -7.704  24.277 1.00 19.67 ? 50  LEU B CA  1 
ATOM   738  C C   . LEU B 2 50 ? 7.212  -7.659  24.809 1.00 20.08 ? 50  LEU B C   1 
ATOM   739  O O   . LEU B 2 50 ? 6.690  -6.594  25.055 1.00 19.17 ? 50  LEU B O   1 
ATOM   740  C CB  . LEU B 2 50 ? 9.649  -7.300  25.367 1.00 17.99 ? 50  LEU B CB  1 
ATOM   741  C CG  . LEU B 2 50 ? 11.093 -7.247  24.870 1.00 18.50 ? 50  LEU B CG  1 
ATOM   742  C CD1 . LEU B 2 50 ? 12.069 -6.950  26.045 1.00 17.08 ? 50  LEU B CD1 1 
ATOM   743  C CD2 . LEU B 2 50 ? 11.521 -8.499  24.100 1.00 19.32 ? 50  LEU B CD2 1 
ATOM   744  N N   . GLU B 2 51 ? 6.612  -8.835  25.008 1.00 20.34 ? 51  GLU B N   1 
ATOM   745  C CA  . GLU B 2 51 ? 5.221  -8.965  25.481 1.00 21.72 ? 51  GLU B CA  1 
ATOM   746  C C   . GLU B 2 51 ? 5.084  -9.063  27.004 1.00 22.57 ? 51  GLU B C   1 
ATOM   747  O O   . GLU B 2 51 ? 5.860  -9.760  27.658 1.00 22.17 ? 51  GLU B O   1 
ATOM   748  C CB  . GLU B 2 51 ? 4.576  -10.210 24.853 1.00 21.60 ? 51  GLU B CB  1 
ATOM   749  C CG  . GLU B 2 51 ? 4.343  -10.091 23.396 1.00 24.66 ? 51  GLU B CG  1 
ATOM   750  C CD  . GLU B 2 51 ? 3.899  -11.422 22.782 1.00 30.94 ? 51  GLU B CD  1 
ATOM   751  O OE1 . GLU B 2 51 ? 3.330  -12.273 23.522 1.00 30.67 ? 51  GLU B OE1 1 
ATOM   752  O OE2 . GLU B 2 51 ? 4.147  -11.603 21.574 1.00 33.57 ? 51  GLU B OE2 1 
ATOM   753  N N   . ASP B 2 52 ? 4.046  -8.427  27.551 1.00 23.58 ? 52  ASP B N   1 
ATOM   754  C CA  . ASP B 2 52 ? 3.909  -8.196  29.013 1.00 24.76 ? 52  ASP B CA  1 
ATOM   755  C C   . ASP B 2 52 ? 3.977  -9.415  29.917 1.00 24.35 ? 52  ASP B C   1 
ATOM   756  O O   . ASP B 2 52 ? 4.549  -9.329  31.009 1.00 23.01 ? 52  ASP B O   1 
ATOM   757  C CB  . ASP B 2 52 ? 2.578  -7.550  29.334 1.00 26.18 ? 52  ASP B CB  1 
ATOM   758  C CG  . ASP B 2 52 ? 2.565  -6.071  29.097 1.00 28.70 ? 52  ASP B CG  1 
ATOM   759  O OD1 . ASP B 2 52 ? 1.466  -5.540  29.270 1.00 33.62 ? 52  ASP B OD1 1 
ATOM   760  O OD2 . ASP B 2 52 ? 3.599  -5.438  28.745 1.00 32.48 ? 52  ASP B OD2 1 
ATOM   761  N N   . GLY B 2 53 ? 3.332  -10.516 29.508 1.00 23.26 ? 53  GLY B N   1 
ATOM   762  C CA  . GLY B 2 53 ? 3.204  -11.677 30.401 1.00 23.37 ? 53  GLY B CA  1 
ATOM   763  C C   . GLY B 2 53 ? 4.368  -12.642 30.378 1.00 23.32 ? 53  GLY B C   1 
ATOM   764  O O   . GLY B 2 53 ? 4.415  -13.588 31.188 1.00 24.92 ? 53  GLY B O   1 
ATOM   765  N N   . ARG B 2 54 ? 5.309  -12.414 29.459 1.00 21.54 ? 54  ARG B N   1 
ATOM   766  C CA  . ARG B 2 54 ? 6.501  -13.259 29.294 1.00 19.86 ? 54  ARG B CA  1 
ATOM   767  C C   . ARG B 2 54 ? 7.608  -12.678 30.153 1.00 19.28 ? 54  ARG B C   1 
ATOM   768  O O   . ARG B 2 54 ? 7.490  -11.541 30.628 1.00 19.24 ? 54  ARG B O   1 
ATOM   769  C CB  . ARG B 2 54 ? 6.943  -13.275 27.831 1.00 20.00 ? 54  ARG B CB  1 
ATOM   770  C CG  . ARG B 2 54 ? 5.771  -13.569 26.903 1.00 23.44 ? 54  ARG B CG  1 
ATOM   771  C CD  . ARG B 2 54 ? 6.116  -14.363 25.709 1.00 24.41 ? 54  ARG B CD  1 
ATOM   772  N NE  . ARG B 2 54 ? 4.941  -14.451 24.839 1.00 28.73 ? 54  ARG B NE  1 
ATOM   773  C CZ  . ARG B 2 54 ? 4.102  -15.480 24.788 1.00 29.09 ? 54  ARG B CZ  1 
ATOM   774  N NH1 . ARG B 2 54 ? 3.070  -15.436 23.949 1.00 29.99 ? 54  ARG B NH1 1 
ATOM   775  N NH2 . ARG B 2 54 ? 4.283  -16.551 25.561 1.00 29.67 ? 54  ARG B NH2 1 
ATOM   776  N N   . THR B 2 55 ? 8.657  -13.450 30.369 1.00 17.51 ? 55  THR B N   1 
ATOM   777  C CA  . THR B 2 55 ? 9.722  -13.024 31.270 1.00 16.43 ? 55  THR B CA  1 
ATOM   778  C C   . THR B 2 55 ? 10.960 -12.647 30.477 1.00 15.25 ? 55  THR B C   1 
ATOM   779  O O   . THR B 2 55 ? 11.051 -12.931 29.282 1.00 15.23 ? 55  THR B O   1 
ATOM   780  C CB  . THR B 2 55 ? 10.101 -14.118 32.226 1.00 15.82 ? 55  THR B CB  1 
ATOM   781  O OG1 . THR B 2 55 ? 10.629 -15.210 31.461 1.00 17.34 ? 55  THR B OG1 1 
ATOM   782  C CG2 . THR B 2 55 ? 8.832  -14.591 33.020 1.00 18.65 ? 55  THR B CG2 1 
ATOM   783  N N   . LEU B 2 56 ? 11.920 -12.012 31.146 1.00 14.38 ? 56  LEU B N   1 
ATOM   784  C CA  . LEU B 2 56 ? 13.206 -11.703 30.486 1.00 13.29 ? 56  LEU B CA  1 
ATOM   785  C C   . LEU B 2 56 ? 13.842 -12.960 29.914 1.00 13.81 ? 56  LEU B C   1 
ATOM   786  O O   . LEU B 2 56 ? 14.292 -12.961 28.762 1.00 13.68 ? 56  LEU B O   1 
ATOM   787  C CB  . LEU B 2 56 ? 14.146 -11.035 31.477 1.00 12.80 ? 56  LEU B CB  1 
ATOM   788  C CG  . LEU B 2 56 ? 13.695 -9.650  31.940 1.00 14.86 ? 56  LEU B CG  1 
ATOM   789  C CD1 . LEU B 2 56 ? 14.649 -9.263  33.090 1.00 13.74 ? 56  LEU B CD1 1 
ATOM   790  C CD2 . LEU B 2 56 ? 13.817 -8.641  30.797 1.00 14.17 ? 56  LEU B CD2 1 
ATOM   791  N N   . SER B 2 57 ? 13.838 -14.043 30.709 1.00 13.54 ? 57  SER B N   1 
ATOM   792  C CA  . SER B 2 57 ? 14.412 -15.299 30.300 1.00 15.80 ? 57  SER B CA  1 
ATOM   793  C C   . SER B 2 57 ? 13.737 -15.922 29.076 1.00 15.57 ? 57  SER B C   1 
ATOM   794  O O   . SER B 2 57 ? 14.411 -16.543 28.275 1.00 16.68 ? 57  SER B O   1 
ATOM   795  C CB  . SER B 2 57 ? 14.465 -16.280 31.481 1.00 16.71 ? 57  SER B CB  1 
ATOM   796  O OG  . SER B 2 57 ? 15.429 -15.800 32.423 1.00 21.58 ? 57  SER B OG  1 
ATOM   797  N N   . ASP B 2 58 ? 12.435 -15.713 28.912 1.00 14.80 ? 58  ASP B N   1 
ATOM   798  C CA  . ASP B 2 58 ? 11.730 -16.232 27.721 1.00 15.95 ? 58  ASP B CA  1 
ATOM   799  C C   . ASP B 2 58 ? 12.318 -15.650 26.427 1.00 16.24 ? 58  ASP B C   1 
ATOM   800  O O   . ASP B 2 58 ? 12.256 -16.276 25.365 1.00 15.94 ? 58  ASP B O   1 
ATOM   801  C CB  . ASP B 2 58 ? 10.253 -15.909 27.796 1.00 14.27 ? 58  ASP B CB  1 
ATOM   802  C CG  . ASP B 2 58 ? 9.511  -16.729 28.865 1.00 16.32 ? 58  ASP B CG  1 
ATOM   803  O OD1 . ASP B 2 58 ? 8.463  -16.253 29.282 1.00 17.61 ? 58  ASP B OD1 1 
ATOM   804  O OD2 . ASP B 2 58 ? 9.965  -17.807 29.300 1.00 16.01 ? 58  ASP B OD2 1 
ATOM   805  N N   . TYR B 2 59 ? 12.901 -14.454 26.541 1.00 16.79 ? 59  TYR B N   1 
ATOM   806  C CA  . TYR B 2 59 ? 13.594 -13.794 25.419 1.00 17.79 ? 59  TYR B CA  1 
ATOM   807  C C   . TYR B 2 59 ? 15.113 -13.944 25.443 1.00 18.93 ? 59  TYR B C   1 
ATOM   808  O O   . TYR B 2 59 ? 15.811 -13.218 24.715 1.00 20.93 ? 59  TYR B O   1 
ATOM   809  C CB  . TYR B 2 59 ? 13.237 -12.316 25.417 1.00 17.79 ? 59  TYR B CB  1 
ATOM   810  C CG  . TYR B 2 59 ? 11.780 -12.078 25.121 1.00 16.31 ? 59  TYR B CG  1 
ATOM   811  C CD1 . TYR B 2 59 ? 10.899 -11.678 26.108 1.00 17.56 ? 59  TYR B CD1 1 
ATOM   812  C CD2 . TYR B 2 59 ? 11.294 -12.240 23.835 1.00 16.66 ? 59  TYR B CD2 1 
ATOM   813  C CE1 . TYR B 2 59 ? 9.551  -11.461 25.821 1.00 16.84 ? 59  TYR B CE1 1 
ATOM   814  C CE2 . TYR B 2 59 ? 9.925  -12.056 23.534 1.00 16.51 ? 59  TYR B CE2 1 
ATOM   815  C CZ  . TYR B 2 59 ? 9.075  -11.659 24.540 1.00 17.97 ? 59  TYR B CZ  1 
ATOM   816  O OH  . TYR B 2 59 ? 7.755  -11.434 24.231 1.00 18.36 ? 59  TYR B OH  1 
ATOM   817  N N   . ASN B 2 60 ? 15.628 -14.868 26.250 1.00 18.82 ? 60  ASN B N   1 
ATOM   818  C CA  . ASN B 2 60 ? 17.072 -15.090 26.398 1.00 19.89 ? 60  ASN B CA  1 
ATOM   819  C C   . ASN B 2 60 ? 17.818 -13.767 26.714 1.00 19.88 ? 60  ASN B C   1 
ATOM   820  O O   . ASN B 2 60 ? 18.980 -13.540 26.302 1.00 21.50 ? 60  ASN B O   1 
ATOM   821  C CB  . ASN B 2 60 ? 17.637 -15.829 25.175 1.00 20.49 ? 60  ASN B CB  1 
ATOM   822  C CG  . ASN B 2 60 ? 18.622 -16.932 25.548 1.00 25.38 ? 60  ASN B CG  1 
ATOM   823  O OD1 . ASN B 2 60 ? 19.299 -17.489 24.680 1.00 30.47 ? 60  ASN B OD1 1 
ATOM   824  N ND2 . ASN B 2 60 ? 18.740 -17.229 26.845 1.00 27.83 ? 60  ASN B ND2 1 
ATOM   825  N N   . ILE B 2 61 ? 17.130 -12.880 27.428 1.00 18.78 ? 61  ILE B N   1 
ATOM   826  C CA  . ILE B 2 61 ? 17.738 -11.650 27.962 1.00 17.96 ? 61  ILE B CA  1 
ATOM   827  C C   . ILE B 2 61 ? 18.584 -12.006 29.198 1.00 18.30 ? 61  ILE B C   1 
ATOM   828  O O   . ILE B 2 61 ? 18.084 -12.504 30.202 1.00 17.90 ? 61  ILE B O   1 
ATOM   829  C CB  . ILE B 2 61 ? 16.674 -10.605 28.274 1.00 17.14 ? 61  ILE B CB  1 
ATOM   830  C CG1 . ILE B 2 61 ? 15.984 -10.131 26.990 1.00 18.25 ? 61  ILE B CG1 1 
ATOM   831  C CG2 . ILE B 2 61 ? 17.239 -9.383  29.018 1.00 16.21 ? 61  ILE B CG2 1 
ATOM   832  C CD1 . ILE B 2 61 ? 14.724 -9.337  27.289 1.00 16.05 ? 61  ILE B CD1 1 
ATOM   833  N N   . GLN B 2 62 ? 19.889 -11.782 29.095 1.00 19.14 ? 62  GLN B N   1 
ATOM   834  C CA  . GLN B 2 62 ? 20.822 -12.162 30.141 1.00 19.96 ? 62  GLN B CA  1 
ATOM   835  C C   . GLN B 2 62 ? 21.397 -10.917 30.822 1.00 17.75 ? 62  GLN B C   1 
ATOM   836  O O   . GLN B 2 62 ? 21.132 -9.801  30.382 1.00 17.73 ? 62  GLN B O   1 
ATOM   837  C CB  . GLN B 2 62 ? 21.921 -13.074 29.546 1.00 19.98 ? 62  GLN B CB  1 
ATOM   838  C CG  . GLN B 2 62 ? 21.415 -14.518 29.228 1.00 24.03 ? 62  GLN B CG  1 
ATOM   839  C CD  . GLN B 2 62 ? 22.538 -15.566 29.017 1.00 25.39 ? 62  GLN B CD  1 
ATOM   840  O OE1 . GLN B 2 62 ? 22.495 -16.337 28.058 1.00 34.54 ? 62  GLN B OE1 1 
ATOM   841  N NE2 . GLN B 2 62 ? 23.506 -15.627 29.939 1.00 32.07 ? 62  GLN B NE2 1 
ATOM   842  N N   . LYS B 2 63 ? 22.202 -11.103 31.873 1.00 15.63 ? 63  LYS B N   1 
ATOM   843  C CA  . LYS B 2 63 ? 22.872 -9.981  32.531 1.00 15.57 ? 63  LYS B CA  1 
ATOM   844  C C   . LYS B 2 63 ? 23.594 -9.072  31.533 1.00 13.49 ? 63  LYS B C   1 
ATOM   845  O O   . LYS B 2 63 ? 24.193 -9.525  30.526 1.00 13.46 ? 63  LYS B O   1 
ATOM   846  C CB  . LYS B 2 63 ? 23.856 -10.449 33.602 1.00 16.14 ? 63  LYS B CB  1 
ATOM   847  C CG  . LYS B 2 63 ? 25.126 -11.111 33.028 1.00 16.50 ? 63  LYS B CG  1 
ATOM   848  C CD  . LYS B 2 63 ? 26.123 -11.408 34.201 1.00 20.85 ? 63  LYS B CD  1 
ATOM   849  C CE  . LYS B 2 63 ? 27.437 -11.965 33.676 1.00 26.59 ? 63  LYS B CE  1 
ATOM   850  N NZ  . LYS B 2 63 ? 28.268 -10.887 33.080 1.00 32.10 ? 63  LYS B NZ  1 
ATOM   851  N N   . GLU B 2 64 ? 23.483 -7.785  31.793 1.00 13.35 ? 64  GLU B N   1 
ATOM   852  C CA  . GLU B 2 64 ? 24.086 -6.751  30.926 1.00 15.82 ? 64  GLU B CA  1 
ATOM   853  C C   . GLU B 2 64 ? 23.525 -6.589  29.497 1.00 14.60 ? 64  GLU B C   1 
ATOM   854  O O   . GLU B 2 64 ? 24.065 -5.838  28.682 1.00 14.49 ? 64  GLU B O   1 
ATOM   855  C CB  . GLU B 2 64 ? 25.632 -6.827  30.970 1.00 15.96 ? 64  GLU B CB  1 
ATOM   856  C CG  . GLU B 2 64 ? 26.133 -6.340  32.312 1.00 19.60 ? 64  GLU B CG  1 
ATOM   857  C CD  . GLU B 2 64 ? 26.598 -7.418  33.281 1.00 28.16 ? 64  GLU B CD  1 
ATOM   858  O OE1 . GLU B 2 64 ? 27.508 -8.195  32.867 1.00 28.71 ? 64  GLU B OE1 1 
ATOM   859  O OE2 . GLU B 2 64 ? 26.137 -7.406  34.481 1.00 27.69 ? 64  GLU B OE2 1 
ATOM   860  N N   . SER B 2 65 ? 22.390 -7.223  29.214 1.00 14.40 ? 65  SER B N   1 
ATOM   861  C CA  . SER B 2 65 ? 21.688 -6.990  27.960 1.00 14.09 ? 65  SER B CA  1 
ATOM   862  C C   . SER B 2 65 ? 21.168 -5.562  27.917 1.00 13.97 ? 65  SER B C   1 
ATOM   863  O O   . SER B 2 65 ? 20.849 -4.984  28.955 1.00 14.11 ? 65  SER B O   1 
ATOM   864  C CB  . SER B 2 65 ? 20.480 -7.923  27.843 1.00 13.03 ? 65  SER B CB  1 
ATOM   865  O OG  . SER B 2 65 ? 20.911 -9.254  27.634 1.00 15.27 ? 65  SER B OG  1 
ATOM   866  N N   . THR B 2 66 ? 21.066 -5.002  26.715 1.00 14.26 ? 66  THR B N   1 
ATOM   867  C CA  . THR B 2 66 ? 20.548 -3.634  26.540 1.00 14.61 ? 66  THR B CA  1 
ATOM   868  C C   . THR B 2 66 ? 19.236 -3.721  25.763 1.00 13.88 ? 66  THR B C   1 
ATOM   869  O O   . THR B 2 66 ? 19.211 -4.200  24.632 1.00 15.09 ? 66  THR B O   1 
ATOM   870  C CB  . THR B 2 66 ? 21.550 -2.676  25.819 1.00 15.34 ? 66  THR B CB  1 
ATOM   871  O OG1 . THR B 2 66 ? 22.745 -2.555  26.597 1.00 15.29 ? 66  THR B OG1 1 
ATOM   872  C CG2 . THR B 2 66 ? 20.947 -1.238  25.671 1.00 14.64 ? 66  THR B CG2 1 
ATOM   873  N N   . LEU B 2 67 ? 18.163 -3.269  26.383 1.00 14.02 ? 67  LEU B N   1 
ATOM   874  C CA  . LEU B 2 67 ? 16.864 -3.139  25.718 1.00 14.21 ? 67  LEU B CA  1 
ATOM   875  C C   . LEU B 2 67 ? 16.722 -1.717  25.176 1.00 14.16 ? 67  LEU B C   1 
ATOM   876  O O   . LEU B 2 67 ? 17.380 -0.791  25.698 1.00 14.09 ? 67  LEU B O   1 
ATOM   877  C CB  . LEU B 2 67 ? 15.728 -3.374  26.712 1.00 13.85 ? 67  LEU B CB  1 
ATOM   878  C CG  . LEU B 2 67 ? 15.727 -4.527  27.743 1.00 17.53 ? 67  LEU B CG  1 
ATOM   879  C CD1 . LEU B 2 67 ? 14.289 -4.759  28.356 1.00 13.56 ? 67  LEU B CD1 1 
ATOM   880  C CD2 . LEU B 2 67 ? 16.334 -5.800  27.270 1.00 15.62 ? 67  LEU B CD2 1 
ATOM   881  N N   . HIS B 2 68 ? 15.883 -1.548  24.142 1.00 12.94 ? 68  HIS B N   1 
ATOM   882  C CA  . HIS B 2 68 ? 15.591 -0.219  23.631 1.00 13.32 ? 68  HIS B CA  1 
ATOM   883  C C   . HIS B 2 68 ? 14.121 0.156   23.896 1.00 13.58 ? 68  HIS B C   1 
ATOM   884  O O   . HIS B 2 68 ? 13.189 -0.586  23.550 1.00 13.76 ? 68  HIS B O   1 
ATOM   885  C CB  . HIS B 2 68 ? 15.952 -0.066  22.151 1.00 13.62 ? 68  HIS B CB  1 
ATOM   886  C CG  . HIS B 2 68 ? 17.430 -0.145  21.896 1.00 15.18 ? 68  HIS B CG  1 
ATOM   887  N ND1 . HIS B 2 68 ? 18.210 0.955   21.584 1.00 19.72 ? 68  HIS B ND1 1 
ATOM   888  C CD2 . HIS B 2 68 ? 18.273 -1.189  21.974 1.00 15.21 ? 68  HIS B CD2 1 
ATOM   889  C CE1 . HIS B 2 68 ? 19.465 0.573   21.436 1.00 14.46 ? 68  HIS B CE1 1 
ATOM   890  N NE2 . HIS B 2 68 ? 19.535 -0.720  21.686 1.00 19.23 ? 68  HIS B NE2 1 
ATOM   891  N N   . LEU B 2 69 ? 13.945 1.313   24.531 1.00 13.37 ? 69  LEU B N   1 
ATOM   892  C CA  . LEU B 2 69 ? 12.615 1.811   24.876 1.00 12.49 ? 69  LEU B CA  1 
ATOM   893  C C   . LEU B 2 69 ? 12.121 2.840   23.873 1.00 14.09 ? 69  LEU B C   1 
ATOM   894  O O   . LEU B 2 69 ? 12.850 3.741   23.481 1.00 13.91 ? 69  LEU B O   1 
ATOM   895  C CB  . LEU B 2 69 ? 12.664 2.463   26.250 1.00 13.05 ? 69  LEU B CB  1 
ATOM   896  C CG  . LEU B 2 69 ? 11.387 3.199   26.721 1.00 13.35 ? 69  LEU B CG  1 
ATOM   897  C CD1 . LEU B 2 69 ? 10.205 2.249   26.900 1.00 13.45 ? 69  LEU B CD1 1 
ATOM   898  C CD2 . LEU B 2 69 ? 11.687 3.974   28.021 1.00 12.71 ? 69  LEU B CD2 1 
ATOM   899  N N   . VAL B 2 70 ? 10.865 2.702   23.461 1.00 15.24 ? 70  VAL B N   1 
ATOM   900  C CA  . VAL B 2 70 ? 10.202 3.725   22.644 1.00 16.94 ? 70  VAL B CA  1 
ATOM   901  C C   . VAL B 2 70 ? 8.907  4.084   23.338 1.00 18.01 ? 70  VAL B C   1 
ATOM   902  O O   . VAL B 2 70 ? 8.175  3.205   23.805 1.00 17.45 ? 70  VAL B O   1 
ATOM   903  C CB  . VAL B 2 70 ? 9.826  3.219   21.235 1.00 17.09 ? 70  VAL B CB  1 
ATOM   904  C CG1 . VAL B 2 70 ? 9.240  4.348   20.378 1.00 18.23 ? 70  VAL B CG1 1 
ATOM   905  C CG2 . VAL B 2 70 ? 11.035 2.657   20.512 1.00 17.63 ? 70  VAL B CG2 1 
ATOM   906  N N   . LEU B 2 71 ? 8.604  5.371   23.374 1.00 19.59 ? 71  LEU B N   1 
ATOM   907  C CA  . LEU B 2 71 ? 7.394  5.810   24.027 1.00 22.46 ? 71  LEU B CA  1 
ATOM   908  C C   . LEU B 2 71 ? 6.250  5.806   23.006 1.00 24.37 ? 71  LEU B C   1 
ATOM   909  O O   . LEU B 2 71 ? 6.475  5.911   21.776 1.00 23.74 ? 71  LEU B O   1 
ATOM   910  C CB  . LEU B 2 71 ? 7.620  7.181   24.664 1.00 23.30 ? 71  LEU B CB  1 
ATOM   911  C CG  . LEU B 2 71 ? 8.157  7.264   26.105 1.00 24.51 ? 71  LEU B CG  1 
ATOM   912  C CD1 . LEU B 2 71 ? 8.656  5.938   26.700 1.00 23.98 ? 71  LEU B CD1 1 
ATOM   913  C CD2 . LEU B 2 71 ? 9.199  8.358   26.203 1.00 28.65 ? 71  LEU B CD2 1 
ATOM   914  N N   . ARG B 2 72 ? 5.034  5.575   23.479 1.00 25.38 ? 72  ARG B N   1 
ATOM   915  C CA  . ARG B 2 72 ? 3.918  5.633   22.555 1.00 28.72 ? 72  ARG B CA  1 
ATOM   916  C C   . ARG B 2 72 ? 3.404  7.079   22.524 1.00 28.98 ? 72  ARG B C   1 
ATOM   917  O O   . ARG B 2 72 ? 2.548  7.492   23.343 1.00 30.87 ? 72  ARG B O   1 
ATOM   918  C CB  . ARG B 2 72 ? 2.818  4.673   22.954 1.00 29.48 ? 72  ARG B CB  1 
ATOM   919  C CG  . ARG B 2 72 ? 2.038  4.176   21.766 1.00 35.17 ? 72  ARG B CG  1 
ATOM   920  C CD  . ARG B 2 72 ? 0.501  4.250   21.994 1.00 41.46 ? 72  ARG B CD  1 
ATOM   921  N NE  . ARG B 2 72 ? -0.221 3.505   20.963 1.00 44.48 ? 72  ARG B NE  1 
ATOM   922  C CZ  . ARG B 2 72 ? -1.501 3.137   21.035 1.00 46.24 ? 72  ARG B CZ  1 
ATOM   923  N NH1 . ARG B 2 72 ? -2.031 2.454   20.031 1.00 45.28 ? 72  ARG B NH1 1 
ATOM   924  N NH2 . ARG B 2 72 ? -2.249 3.447   22.095 1.00 45.90 ? 72  ARG B NH2 1 
HETATM 925  O O   . HOH C 3 .  ? 18.014 4.698   18.339 1.00 13.26 ? 2   HOH A O   1 
HETATM 926  O O   . HOH C 3 .  ? 15.488 -6.300  0.065  1.00 18.59 ? 3   HOH A O   1 
HETATM 927  O O   . HOH C 3 .  ? 21.121 -2.028  18.577 1.00 17.18 ? 4   HOH A O   1 
HETATM 928  O O   . HOH C 3 .  ? 20.702 -4.770  17.806 1.00 15.75 ? 5   HOH A O   1 
HETATM 929  O O   . HOH C 3 .  ? 14.259 9.987   14.238 1.00 20.27 ? 7   HOH A O   1 
HETATM 930  O O   . HOH C 3 .  ? 13.084 8.653   16.620 1.00 18.50 ? 9   HOH A O   1 
HETATM 931  O O   . HOH C 3 .  ? 28.861 -3.130  7.974  1.00 19.50 ? 14  HOH A O   1 
HETATM 932  O O   . HOH C 3 .  ? 18.435 -7.056  16.378 1.00 19.10 ? 18  HOH A O   1 
HETATM 933  O O   . HOH C 3 .  ? 3.479  -3.722  14.908 1.00 30.37 ? 21  HOH A O   1 
HETATM 934  O O   . HOH C 3 .  ? 7.496  -7.545  10.517 1.00 24.86 ? 23  HOH A O   1 
HETATM 935  O O   . HOH C 3 .  ? 22.636 -5.836  15.375 1.00 30.66 ? 24  HOH A O   1 
HETATM 936  O O   . HOH C 3 .  ? 8.986  8.012   0.718  1.00 27.37 ? 27  HOH A O   1 
HETATM 937  O O   . HOH C 3 .  ? 14.449 -5.989  10.483 1.00 25.76 ? 29  HOH A O   1 
HETATM 938  O O   . HOH C 3 .  ? 18.029 -3.722  22.189 1.00 26.23 ? 36  HOH A O   1 
HETATM 939  O O   . HOH C 3 .  ? 18.362 10.018  15.885 1.00 35.08 ? 43  HOH A O   1 
HETATM 940  O O   . HOH C 3 .  ? 5.692  3.426   17.744 1.00 34.61 ? 45  HOH A O   1 
HETATM 941  O O   . HOH C 3 .  ? 4.797  -0.809  17.876 1.00 37.98 ? 48  HOH A O   1 
HETATM 942  O O   . HOH C 3 .  ? 23.830 -2.053  8.539  1.00 41.53 ? 49  HOH A O   1 
HETATM 943  O O   . HOH C 3 .  ? 14.880 8.867   3.884  1.00 30.65 ? 55  HOH A O   1 
HETATM 944  O O   . HOH C 3 .  ? 24.038 -7.064  16.769 1.00 27.14 ? 56  HOH A O   1 
HETATM 945  O O   . HOH C 3 .  ? 6.559  9.671   0.693  1.00 36.04 ? 64  HOH A O   1 
HETATM 946  O O   . HOH C 3 .  ? 16.084 10.283  5.447  1.00 37.99 ? 66  HOH A O   1 
HETATM 947  O O   . HOH C 3 .  ? 19.933 -0.745  1.171  1.00 30.50 ? 67  HOH A O   1 
HETATM 948  O O   . HOH C 3 .  ? 7.380  11.024  17.748 1.00 31.59 ? 70  HOH A O   1 
HETATM 949  O O   . HOH C 3 .  ? 1.131  6.265   0.419  1.00 39.26 ? 72  HOH A O   1 
HETATM 950  O O   . HOH C 3 .  ? 14.516 -7.354  13.101 1.00 28.52 ? 73  HOH A O   1 
HETATM 951  O O   . HOH C 3 .  ? 16.715 -6.321  9.603  1.00 22.31 ? 75  HOH A O   1 
HETATM 952  O O   . HOH C 3 .  ? 17.914 -8.216  11.225 1.00 30.17 ? 76  HOH A O   1 
HETATM 953  O O   . HOH C 3 .  ? -0.197 5.893   8.505  1.00 52.08 ? 78  HOH A O   1 
HETATM 954  O O   . HOH C 3 .  ? 16.841 -8.222  14.190 1.00 33.00 ? 80  HOH A O   1 
HETATM 955  O O   . HOH C 3 .  ? 13.587 -8.935  10.575 1.00 33.51 ? 86  HOH A O   1 
HETATM 956  O O   . HOH C 3 .  ? 19.226 -10.051 17.133 1.00 38.34 ? 88  HOH A O   1 
HETATM 957  O O   . HOH C 3 .  ? 12.191 9.647   3.742  1.00 32.40 ? 90  HOH A O   1 
HETATM 958  O O   . HOH C 3 .  ? 9.886  9.885   9.388  1.00 29.83 ? 93  HOH A O   1 
HETATM 959  O O   . HOH C 3 .  ? 2.954  8.709   11.667 1.00 41.41 ? 97  HOH A O   1 
HETATM 960  O O   . HOH C 3 .  ? 3.013  5.753   -2.650 1.00 55.27 ? 99  HOH A O   1 
HETATM 961  O O   . HOH C 3 .  ? 3.573  8.982   5.257  1.00 47.27 ? 102 HOH A O   1 
HETATM 962  O O   . HOH C 3 .  ? 4.922  10.229  11.986 1.00 36.12 ? 107 HOH A O   1 
HETATM 963  O O   . HOH C 3 .  ? 21.903 -8.026  14.127 1.00 38.18 ? 108 HOH A O   1 
HETATM 964  O O   . HOH C 3 .  ? 0.000  3.072   0.001  0.50 41.89 ? 110 HOH A O   1 
HETATM 965  O O   . HOH C 3 .  ? 17.120 -8.211  7.388  1.00 40.09 ? 113 HOH A O   1 
HETATM 966  O O   . HOH C 3 .  ? -1.291 4.416   1.752  1.00 49.83 ? 115 HOH A O   1 
HETATM 967  O O   . HOH C 3 .  ? 24.473 -8.375  14.381 1.00 48.95 ? 116 HOH A O   1 
HETATM 968  O O   . HOH C 3 .  ? 26.090 -10.069 14.806 1.00 36.80 ? 118 HOH A O   1 
HETATM 969  O O   . HOH C 3 .  ? 23.217 -11.912 15.145 1.00 35.01 ? 121 HOH A O   1 
HETATM 970  O O   . HOH C 3 .  ? 25.474 -13.292 14.633 1.00 34.35 ? 122 HOH A O   1 
HETATM 971  O O   . HOH C 3 .  ? 4.333  2.894   6.864  1.00 36.00 ? 123 HOH A O   1 
HETATM 972  O O   . HOH C 3 .  ? 18.864 8.662   9.120  1.00 41.76 ? 127 HOH A O   1 
HETATM 973  O O   . HOH C 3 .  ? -1.601 7.254   6.479  1.00 31.16 ? 129 HOH A O   1 
HETATM 974  O O   . HOH C 3 .  ? 9.128  -9.055  9.126  1.00 37.48 ? 132 HOH A O   1 
HETATM 975  O O   . HOH C 3 .  ? 17.604 -7.619  4.955  1.00 33.58 ? 144 HOH A O   1 
HETATM 976  O O   . HOH C 3 .  ? 7.401  9.828   9.409  1.00 35.20 ? 148 HOH A O   1 
HETATM 977  O O   . HOH D 3 .  ? 15.348 -1.296  39.150 1.00 7.50  ? 77  HOH B O   1 
HETATM 978  O O   . HOH D 3 .  ? 22.485 -6.409  24.476 1.00 15.10 ? 78  HOH B O   1 
HETATM 979  O O   . HOH D 3 .  ? 15.538 3.516   22.561 1.00 13.82 ? 79  HOH B O   1 
HETATM 980  O O   . HOH D 3 .  ? 12.645 6.309   24.093 1.00 17.87 ? 80  HOH B O   1 
HETATM 981  O O   . HOH D 3 .  ? 13.119 0.649   39.381 1.00 19.59 ? 81  HOH B O   1 
HETATM 982  O O   . HOH D 3 .  ? 8.255  -9.516  18.334 1.00 24.39 ? 82  HOH B O   1 
HETATM 983  O O   . HOH D 3 .  ? 19.436 3.965   36.204 1.00 20.36 ? 83  HOH B O   1 
HETATM 984  O O   . HOH D 3 .  ? 24.436 -8.297  36.550 1.00 17.87 ? 84  HOH B O   1 
HETATM 985  O O   . HOH D 3 .  ? 22.301 3.693   33.962 1.00 17.83 ? 85  HOH B O   1 
HETATM 986  O O   . HOH D 3 .  ? 10.570 7.712   22.640 1.00 19.03 ? 86  HOH B O   1 
HETATM 987  O O   . HOH D 3 .  ? 6.942  -3.891  24.839 1.00 20.75 ? 87  HOH B O   1 
HETATM 988  O O   . HOH D 3 .  ? 26.524 -4.806  35.695 1.00 20.63 ? 88  HOH B O   1 
HETATM 989  O O   . HOH D 3 .  ? 18.674 14.406  25.029 1.00 31.95 ? 89  HOH B O   1 
HETATM 990  O O   . HOH D 3 .  ? 22.509 -13.676 32.943 1.00 23.11 ? 90  HOH B O   1 
HETATM 991  O O   . HOH D 3 .  ? 13.847 -17.221 23.582 1.00 21.55 ? 91  HOH B O   1 
HETATM 992  O O   . HOH D 3 .  ? 20.217 -15.108 33.080 1.00 21.00 ? 92  HOH B O   1 
HETATM 993  O O   . HOH D 3 .  ? 23.372 6.768   27.681 1.00 22.97 ? 93  HOH B O   1 
HETATM 994  O O   . HOH D 3 .  ? 14.337 9.313   27.942 1.00 24.43 ? 94  HOH B O   1 
HETATM 995  O O   . HOH D 3 .  ? 22.600 -7.131  40.425 1.00 26.95 ? 95  HOH B O   1 
HETATM 996  O O   . HOH D 3 .  ? 18.081 -14.783 31.633 1.00 26.89 ? 96  HOH B O   1 
HETATM 997  O O   . HOH D 3 .  ? 17.824 4.146   21.093 1.00 27.63 ? 97  HOH B O   1 
HETATM 998  O O   . HOH D 3 .  ? 10.871 -12.418 39.321 1.00 26.74 ? 98  HOH B O   1 
HETATM 999  O O   . HOH D 3 .  ? 15.521 -18.698 27.008 1.00 27.19 ? 99  HOH B O   1 
HETATM 1000 O O   . HOH D 3 .  ? 13.477 -8.271  40.651 1.00 29.65 ? 100 HOH B O   1 
HETATM 1001 O O   . HOH D 3 .  ? 22.569 -9.582  25.410 1.00 34.00 ? 101 HOH B O   1 
HETATM 1002 O O   . HOH D 3 .  ? 20.083 -11.864 39.745 1.00 32.26 ? 102 HOH B O   1 
HETATM 1003 O O   . HOH D 3 .  ? 11.299 -0.384  41.293 1.00 28.64 ? 103 HOH B O   1 
HETATM 1004 O O   . HOH D 3 .  ? -0.072 -1.809  32.498 1.00 29.16 ? 104 HOH B O   1 
HETATM 1005 O O   . HOH D 3 .  ? 3.045  -0.815  27.148 1.00 26.58 ? 105 HOH B O   1 
HETATM 1006 O O   . HOH D 3 .  ? 15.857 -7.776  41.329 1.00 30.19 ? 106 HOH B O   1 
HETATM 1007 O O   . HOH D 3 .  ? 8.025  -15.707 36.395 1.00 29.00 ? 107 HOH B O   1 
HETATM 1008 O O   . HOH D 3 .  ? 1.940  -7.420  26.085 1.00 34.07 ? 108 HOH B O   1 
HETATM 1009 O O   . HOH D 3 .  ? 5.572  1.173   38.979 1.00 28.93 ? 109 HOH B O   1 
HETATM 1010 O O   . HOH D 3 .  ? 24.525 -4.491  26.510 1.00 27.91 ? 110 HOH B O   1 
HETATM 1011 O O   . HOH D 3 .  ? 24.720 -7.077  38.749 1.00 35.73 ? 111 HOH B O   1 
HETATM 1012 O O   . HOH D 3 .  ? 23.287 -13.350 35.988 1.00 27.10 ? 112 HOH B O   1 
HETATM 1013 O O   . HOH D 3 .  ? 19.280 -7.551  41.030 1.00 32.21 ? 113 HOH B O   1 
HETATM 1014 O O   . HOH D 3 .  ? 26.039 -1.043  36.421 1.00 25.43 ? 114 HOH B O   1 
HETATM 1015 O O   . HOH D 3 .  ? -0.115 8.449   23.163 1.00 40.48 ? 115 HOH B O   1 
HETATM 1016 O O   . HOH D 3 .  ? 4.080  7.507   36.057 1.00 33.58 ? 116 HOH B O   1 
HETATM 1017 O O   . HOH D 3 .  ? 25.499 -11.696 29.562 1.00 29.45 ? 117 HOH B O   1 
HETATM 1018 O O   . HOH D 3 .  ? 3.669  -6.717  21.634 1.00 35.55 ? 118 HOH B O   1 
HETATM 1019 O O   . HOH D 3 .  ? 24.392 -11.120 37.362 1.00 25.58 ? 119 HOH B O   1 
HETATM 1020 O O   . HOH D 3 .  ? 16.262 -13.020 22.012 1.00 28.01 ? 120 HOH B O   1 
HETATM 1021 O O   . HOH D 3 .  ? 24.065 -0.249  27.243 1.00 40.43 ? 121 HOH B O   1 
HETATM 1022 O O   . HOH D 3 .  ? 12.581 8.417   25.604 1.00 31.64 ? 122 HOH B O   1 
HETATM 1023 O O   . HOH D 3 .  ? 3.722  -9.695  35.946 1.00 28.26 ? 123 HOH B O   1 
HETATM 1024 O O   . HOH D 3 .  ? 13.705 2.547   41.297 1.00 34.54 ? 124 HOH B O   1 
HETATM 1025 O O   . HOH D 3 .  ? 17.914 -0.021  40.277 1.00 37.95 ? 125 HOH B O   1 
HETATM 1026 O O   . HOH D 3 .  ? 0.585  6.734   20.212 1.00 28.36 ? 126 HOH B O   1 
HETATM 1027 O O   . HOH D 3 .  ? 14.499 -15.311 21.639 1.00 34.10 ? 127 HOH B O   1 
HETATM 1028 O O   . HOH D 3 .  ? 23.516 2.511   26.478 1.00 30.61 ? 128 HOH B O   1 
HETATM 1029 O O   . HOH D 3 .  ? 4.060  -5.224  37.643 1.00 33.23 ? 129 HOH B O   1 
HETATM 1030 O O   . HOH D 3 .  ? -4.315 3.982   24.425 1.00 40.15 ? 130 HOH B O   1 
HETATM 1031 O O   . HOH D 3 .  ? 0.469  2.151   24.107 1.00 32.68 ? 131 HOH B O   1 
HETATM 1032 O O   . HOH D 3 .  ? 2.410  -7.284  36.911 1.00 31.26 ? 132 HOH B O   1 
HETATM 1033 O O   . HOH D 3 .  ? 2.807  7.773   19.884 1.00 37.79 ? 133 HOH B O   1 
HETATM 1034 O O   . HOH D 3 .  ? 9.585  -10.336 15.998 1.00 34.01 ? 134 HOH B O   1 
HETATM 1035 O O   . HOH D 3 .  ? 3.615  -19.683 25.826 1.00 38.16 ? 135 HOH B O   1 
HETATM 1036 O O   . HOH D 3 .  ? 18.375 12.368  28.142 1.00 37.77 ? 136 HOH B O   1 
HETATM 1037 O O   . HOH D 3 .  ? 20.656 -12.961 24.320 1.00 33.45 ? 137 HOH B O   1 
HETATM 1038 O O   . HOH D 3 .  ? 14.253 -2.849  41.469 1.00 29.02 ? 138 HOH B O   1 
HETATM 1039 O O   . HOH D 3 .  ? 19.271 6.269   21.821 1.00 38.85 ? 139 HOH B O   1 
HETATM 1040 O O   . HOH D 3 .  ? 11.372 -3.221  41.435 1.00 35.76 ? 140 HOH B O   1 
HETATM 1041 O O   . HOH D 3 .  ? 18.057 -15.223 40.145 1.00 43.64 ? 141 HOH B O   1 
HETATM 1042 O O   . HOH D 3 .  ? 5.766  -8.518  19.540 1.00 32.90 ? 142 HOH B O   1 
HETATM 1043 O O   . HOH D 3 .  ? 24.655 -13.319 27.237 1.00 37.34 ? 143 HOH B O   1 
HETATM 1044 O O   . HOH D 3 .  ? 19.170 -15.213 42.203 1.00 70.19 ? 144 HOH B O   1 
HETATM 1045 O O   . HOH D 3 .  ? 8.412  7.693   39.469 1.00 41.70 ? 145 HOH B O   1 
HETATM 1046 O O   . HOH D 3 .  ? 8.630  -12.217 19.929 1.00 41.86 ? 146 HOH B O   1 
HETATM 1047 O O   . HOH D 3 .  ? 3.660  -2.633  35.032 1.00 33.92 ? 147 HOH B O   1 
HETATM 1048 O O   . HOH D 3 .  ? 8.158  -2.419  40.716 1.00 39.53 ? 148 HOH B O   1 
HETATM 1049 O O   . HOH D 3 .  ? 27.534 -1.275  38.956 1.00 35.02 ? 149 HOH B O   1 
HETATM 1050 O O   . HOH D 3 .  ? 0.000  0.000   34.953 0.50 17.69 ? 150 HOH B O   1 
HETATM 1051 O O   . HOH D 3 .  ? 7.073  -10.732 21.009 1.00 61.51 ? 151 HOH B O   1 
HETATM 1052 O O   . HOH D 3 .  ? 1.482  -19.049 26.022 1.00 54.93 ? 152 HOH B O   1 
HETATM 1053 O O   . HOH D 3 .  ? 8.201  -5.128  38.987 1.00 41.62 ? 153 HOH B O   1 
HETATM 1054 O O   . HOH D 3 .  ? 29.060 -10.445 30.687 1.00 41.62 ? 154 HOH B O   1 
HETATM 1055 O O   . HOH D 3 .  ? 19.056 9.882   20.362 1.00 46.29 ? 155 HOH B O   1 
HETATM 1056 O O   . HOH D 3 .  ? 1.730  1.390   19.923 1.00 32.83 ? 156 HOH B O   1 
HETATM 1057 O O   . HOH D 3 .  ? 28.434 -8.079  30.909 1.00 16.79 ? 157 HOH B O   1 
HETATM 1058 O O   . HOH D 3 .  ? 11.931 -12.428 15.742 1.00 41.52 ? 158 HOH B O   1 
# 
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  922 ?   ?   ?   A . n 
A 1 2  SER 2  923 ?   ?   ?   A . n 
A 1 3  GLY 3  924 ?   ?   ?   A . n 
A 1 4  PRO 4  925 ?   ?   ?   A . n 
A 1 5  GLU 5  926 ?   ?   ?   A . n 
A 1 6  ALA 6  927 ?   ?   ?   A . n 
A 1 7  ALA 7  928 ?   ?   ?   A . n 
A 1 8  LEU 8  929 929 LEU LEU A . n 
A 1 9  GLU 9  930 930 GLU GLU A . n 
A 1 10 ASN 10 931 931 ASN ASN A . n 
A 1 11 VAL 11 932 932 VAL VAL A . n 
A 1 12 ASP 12 933 933 ASP ASP A . n 
A 1 13 ALA 13 934 934 ALA ALA A . n 
A 1 14 LYS 14 935 935 LYS LYS A . n 
A 1 15 ILE 15 936 936 ILE ILE A . n 
A 1 16 ALA 16 937 937 ALA ALA A . n 
A 1 17 LYS 17 938 938 LYS LYS A . n 
A 1 18 LEU 18 939 939 LEU LEU A . n 
A 1 19 MET 19 940 940 MET MET A . n 
A 1 20 GLY 20 941 941 GLY GLY A . n 
A 1 21 GLU 21 942 942 GLU GLU A . n 
A 1 22 GLY 22 943 943 GLY GLY A . n 
A 1 23 TYR 23 944 944 TYR TYR A . n 
A 1 24 ALA 24 945 945 ALA ALA A . n 
A 1 25 PHE 25 946 946 PHE PHE A . n 
A 1 26 GLU 26 947 947 GLU GLU A . n 
A 1 27 GLU 27 948 948 GLU GLU A . n 
A 1 28 VAL 28 949 949 VAL VAL A . n 
A 1 29 LYS 29 950 950 LYS LYS A . n 
A 1 30 ARG 30 951 951 ARG ARG A . n 
A 1 31 ALA 31 952 952 ALA ALA A . n 
A 1 32 LEU 32 953 953 LEU LEU A . n 
A 1 33 GLU 33 954 954 GLU GLU A . n 
A 1 34 ILE 34 955 955 ILE ILE A . n 
A 1 35 ALA 35 956 956 ALA ALA A . n 
A 1 36 GLN 36 957 957 GLN GLN A . n 
A 1 37 ASN 37 958 958 ASN ASN A . n 
A 1 38 ASN 38 959 959 ASN ASN A . n 
A 1 39 VAL 39 960 960 VAL VAL A . n 
A 1 40 GLU 40 961 961 GLU GLU A . n 
A 1 41 VAL 41 962 962 VAL VAL A . n 
A 1 42 ALA 42 963 963 ALA ALA A . n 
A 1 43 ARG 43 964 964 ARG ARG A . n 
A 1 44 SER 44 965 965 SER SER A . n 
A 1 45 ILE 45 966 966 ILE ILE A . n 
A 1 46 LEU 46 967 967 LEU LEU A . n 
A 1 47 ARG 47 968 968 ARG ARG A . n 
A 1 48 GLU 48 969 969 GLU GLU A . n 
A 1 49 PHE 49 970 970 PHE PHE A . n 
A 1 50 ALA 50 971 971 ALA ALA A . n 
A 1 51 PHE 51 972 972 PHE PHE A . n 
A 1 52 PRO 52 973 ?   ?   ?   A . n 
B 2 1  MET 1  1   1   MET MET B . n 
B 2 2  GLN 2  2   2   GLN GLN B . n 
B 2 3  ILE 3  3   3   ILE ILE B . n 
B 2 4  PHE 4  4   4   PHE PHE B . n 
B 2 5  VAL 5  5   5   VAL VAL B . n 
B 2 6  LYS 6  6   6   LYS LYS B . n 
B 2 7  THR 7  7   7   THR THR B . n 
B 2 8  LEU 8  8   8   LEU LEU B . n 
B 2 9  THR 9  9   9   THR THR B . n 
B 2 10 GLY 10 10  10  GLY GLY B . n 
B 2 11 LYS 11 11  11  LYS LYS B . n 
B 2 12 THR 12 12  12  THR THR B . n 
B 2 13 ILE 13 13  13  ILE ILE B . n 
B 2 14 THR 14 14  14  THR THR B . n 
B 2 15 LEU 15 15  15  LEU LEU B . n 
B 2 16 GLU 16 16  16  GLU GLU B . n 
B 2 17 VAL 17 17  17  VAL VAL B . n 
B 2 18 GLU 18 18  18  GLU GLU B . n 
B 2 19 PRO 19 19  19  PRO PRO B . n 
B 2 20 SER 20 20  20  SER SER B . n 
B 2 21 ASP 21 21  21  ASP ASP B . n 
B 2 22 THR 22 22  22  THR THR B . n 
B 2 23 ILE 23 23  23  ILE ILE B . n 
B 2 24 GLU 24 24  24  GLU GLU B . n 
B 2 25 ASN 25 25  25  ASN ASN B . n 
B 2 26 VAL 26 26  26  VAL VAL B . n 
B 2 27 LYS 27 27  27  LYS LYS B . n 
B 2 28 ALA 28 28  28  ALA ALA B . n 
B 2 29 LYS 29 29  29  LYS LYS B . n 
B 2 30 ILE 30 30  30  ILE ILE B . n 
B 2 31 GLN 31 31  31  GLN GLN B . n 
B 2 32 ASP 32 32  32  ASP ASP B . n 
B 2 33 LYS 33 33  33  LYS LYS B . n 
B 2 34 GLU 34 34  34  GLU GLU B . n 
B 2 35 GLY 35 35  35  GLY GLY B . n 
B 2 36 ILE 36 36  36  ILE ILE B . n 
B 2 37 PRO 37 37  37  PRO PRO B . n 
B 2 38 PRO 38 38  38  PRO PRO B . n 
B 2 39 ASP 39 39  39  ASP ASP B . n 
B 2 40 GLN 40 40  40  GLN GLN B . n 
B 2 41 GLN 41 41  41  GLN GLN B . n 
B 2 42 ARG 42 42  42  ARG ARG B . n 
B 2 43 LEU 43 43  43  LEU LEU B . n 
B 2 44 ILE 44 44  44  ILE ILE B . n 
B 2 45 PHE 45 45  45  PHE PHE B . n 
B 2 46 ALA 46 46  46  ALA ALA B . n 
B 2 47 GLY 47 47  47  GLY GLY B . n 
B 2 48 LYS 48 48  48  LYS LYS B . n 
B 2 49 GLN 49 49  49  GLN GLN B . n 
B 2 50 LEU 50 50  50  LEU LEU B . n 
B 2 51 GLU 51 51  51  GLU GLU B . n 
B 2 52 ASP 52 52  52  ASP ASP B . n 
B 2 53 GLY 53 53  53  GLY GLY B . n 
B 2 54 ARG 54 54  54  ARG ARG B . n 
B 2 55 THR 55 55  55  THR THR B . n 
B 2 56 LEU 56 56  56  LEU LEU B . n 
B 2 57 SER 57 57  57  SER SER B . n 
B 2 58 ASP 58 58  58  ASP ASP B . n 
B 2 59 TYR 59 59  59  TYR TYR B . n 
B 2 60 ASN 60 60  60  ASN ASN B . n 
B 2 61 ILE 61 61  61  ILE ILE B . n 
B 2 62 GLN 62 62  62  GLN GLN B . n 
B 2 63 LYS 63 63  63  LYS LYS B . n 
B 2 64 GLU 64 64  64  GLU GLU B . n 
B 2 65 SER 65 65  65  SER SER B . n 
B 2 66 THR 66 66  66  THR THR B . n 
B 2 67 LEU 67 67  67  LEU LEU B . n 
B 2 68 HIS 68 68  68  HIS HIS B . n 
B 2 69 LEU 69 69  69  LEU LEU B . n 
B 2 70 VAL 70 70  70  VAL VAL B . n 
B 2 71 LEU 71 71  71  LEU LEU B . n 
B 2 72 ARG 72 72  72  ARG ARG B . n 
B 2 73 LEU 73 73  ?   ?   ?   B . n 
B 2 74 ARG 74 74  ?   ?   ?   B . n 
B 2 75 GLY 75 75  ?   ?   ?   B . n 
B 2 76 GLY 76 76  ?   ?   ?   B . 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 
C 3 HOH 1  2   2   HOH HOH A . 
C 3 HOH 2  3   3   HOH HOH A . 
C 3 HOH 3  4   4   HOH HOH A . 
C 3 HOH 4  5   5   HOH HOH A . 
C 3 HOH 5  7   7   HOH HOH A . 
C 3 HOH 6  9   9   HOH HOH A . 
C 3 HOH 7  14  14  HOH HOH A . 
C 3 HOH 8  18  18  HOH HOH A . 
C 3 HOH 9  21  21  HOH HOH A . 
C 3 HOH 10 23  23  HOH HOH A . 
C 3 HOH 11 24  24  HOH HOH A . 
C 3 HOH 12 27  27  HOH HOH A . 
C 3 HOH 13 29  29  HOH HOH A . 
C 3 HOH 14 36  36  HOH HOH A . 
C 3 HOH 15 43  43  HOH HOH A . 
C 3 HOH 16 45  45  HOH HOH A . 
C 3 HOH 17 48  48  HOH HOH A . 
C 3 HOH 18 49  49  HOH HOH A . 
C 3 HOH 19 55  55  HOH HOH A . 
C 3 HOH 20 56  56  HOH HOH A . 
C 3 HOH 21 64  64  HOH HOH A . 
C 3 HOH 22 66  66  HOH HOH A . 
C 3 HOH 23 67  67  HOH HOH A . 
C 3 HOH 24 70  70  HOH HOH A . 
C 3 HOH 25 72  72  HOH HOH A . 
C 3 HOH 26 73  73  HOH HOH A . 
C 3 HOH 27 75  75  HOH HOH A . 
C 3 HOH 28 76  76  HOH HOH A . 
C 3 HOH 29 78  78  HOH HOH A . 
C 3 HOH 30 80  80  HOH HOH A . 
C 3 HOH 31 86  86  HOH HOH A . 
C 3 HOH 32 88  88  HOH HOH A . 
C 3 HOH 33 90  90  HOH HOH A . 
C 3 HOH 34 93  93  HOH HOH A . 
C 3 HOH 35 97  97  HOH HOH A . 
C 3 HOH 36 99  99  HOH HOH A . 
C 3 HOH 37 102 102 HOH HOH A . 
C 3 HOH 38 107 107 HOH HOH A . 
C 3 HOH 39 108 108 HOH HOH A . 
C 3 HOH 40 110 110 HOH HOH A . 
C 3 HOH 41 113 113 HOH HOH A . 
C 3 HOH 42 115 115 HOH HOH A . 
C 3 HOH 43 116 116 HOH HOH A . 
C 3 HOH 44 118 118 HOH HOH A . 
C 3 HOH 45 121 121 HOH HOH A . 
C 3 HOH 46 122 122 HOH HOH A . 
C 3 HOH 47 123 123 HOH HOH A . 
C 3 HOH 48 127 127 HOH HOH A . 
C 3 HOH 49 129 129 HOH HOH A . 
C 3 HOH 50 132 132 HOH HOH A . 
C 3 HOH 51 144 144 HOH HOH A . 
C 3 HOH 52 148 148 HOH HOH A . 
D 3 HOH 1  77  1   HOH HOH B . 
D 3 HOH 2  78  6   HOH HOH B . 
D 3 HOH 3  79  8   HOH HOH B . 
D 3 HOH 4  80  10  HOH HOH B . 
D 3 HOH 5  81  11  HOH HOH B . 
D 3 HOH 6  82  12  HOH HOH B . 
D 3 HOH 7  83  13  HOH HOH B . 
D 3 HOH 8  84  15  HOH HOH B . 
D 3 HOH 9  85  16  HOH HOH B . 
D 3 HOH 10 86  17  HOH HOH B . 
D 3 HOH 11 87  19  HOH HOH B . 
D 3 HOH 12 88  20  HOH HOH B . 
D 3 HOH 13 89  22  HOH HOH B . 
D 3 HOH 14 90  25  HOH HOH B . 
D 3 HOH 15 91  26  HOH HOH B . 
D 3 HOH 16 92  28  HOH HOH B . 
D 3 HOH 17 93  30  HOH HOH B . 
D 3 HOH 18 94  31  HOH HOH B . 
D 3 HOH 19 95  32  HOH HOH B . 
D 3 HOH 20 96  33  HOH HOH B . 
D 3 HOH 21 97  34  HOH HOH B . 
D 3 HOH 22 98  35  HOH HOH B . 
D 3 HOH 23 99  37  HOH HOH B . 
D 3 HOH 24 100 38  HOH HOH B . 
D 3 HOH 25 101 39  HOH HOH B . 
D 3 HOH 26 102 40  HOH HOH B . 
D 3 HOH 27 103 41  HOH HOH B . 
D 3 HOH 28 104 42  HOH HOH B . 
D 3 HOH 29 105 44  HOH HOH B . 
D 3 HOH 30 106 46  HOH HOH B . 
D 3 HOH 31 107 47  HOH HOH B . 
D 3 HOH 32 108 50  HOH HOH B . 
D 3 HOH 33 109 51  HOH HOH B . 
D 3 HOH 34 110 52  HOH HOH B . 
D 3 HOH 35 111 53  HOH HOH B . 
D 3 HOH 36 112 54  HOH HOH B . 
D 3 HOH 37 113 57  HOH HOH B . 
D 3 HOH 38 114 58  HOH HOH B . 
D 3 HOH 39 115 59  HOH HOH B . 
D 3 HOH 40 116 60  HOH HOH B . 
D 3 HOH 41 117 61  HOH HOH B . 
D 3 HOH 42 118 62  HOH HOH B . 
D 3 HOH 43 119 63  HOH HOH B . 
D 3 HOH 44 120 65  HOH HOH B . 
D 3 HOH 45 121 68  HOH HOH B . 
D 3 HOH 46 122 69  HOH HOH B . 
D 3 HOH 47 123 71  HOH HOH B . 
D 3 HOH 48 124 74  HOH HOH B . 
D 3 HOH 49 125 77  HOH HOH B . 
D 3 HOH 50 126 79  HOH HOH B . 
D 3 HOH 51 127 81  HOH HOH B . 
D 3 HOH 52 128 83  HOH HOH B . 
D 3 HOH 53 129 84  HOH HOH B . 
D 3 HOH 54 130 85  HOH HOH B . 
D 3 HOH 55 131 87  HOH HOH B . 
D 3 HOH 56 132 89  HOH HOH B . 
D 3 HOH 57 133 91  HOH HOH B . 
D 3 HOH 58 134 92  HOH HOH B . 
D 3 HOH 59 135 94  HOH HOH B . 
D 3 HOH 60 136 96  HOH HOH B . 
D 3 HOH 61 137 98  HOH HOH B . 
D 3 HOH 62 138 100 HOH HOH B . 
D 3 HOH 63 139 104 HOH HOH B . 
D 3 HOH 64 140 105 HOH HOH B . 
D 3 HOH 65 141 111 HOH HOH B . 
D 3 HOH 66 142 112 HOH HOH B . 
D 3 HOH 67 143 117 HOH HOH B . 
D 3 HOH 68 144 119 HOH HOH B . 
D 3 HOH 69 145 120 HOH HOH B . 
D 3 HOH 70 146 124 HOH HOH B . 
D 3 HOH 71 147 125 HOH HOH B . 
D 3 HOH 72 148 130 HOH HOH B . 
D 3 HOH 73 149 133 HOH HOH B . 
D 3 HOH 74 150 134 HOH HOH B . 
D 3 HOH 75 151 139 HOH HOH B . 
D 3 HOH 76 152 141 HOH HOH B . 
D 3 HOH 77 153 143 HOH HOH B . 
D 3 HOH 78 154 145 HOH HOH B . 
D 3 HOH 79 155 146 HOH HOH B . 
D 3 HOH 80 156 147 HOH HOH B . 
D 3 HOH 81 157 149 HOH HOH B . 
D 3 HOH 82 158 150 HOH HOH B . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_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_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 110 ? C HOH . 
2 1 B HOH 150 ? D HOH . 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2007-02-06 
2 'Structure model' 1 1 2008-05-01 
3 'Structure model' 1 2 2011-07-13 
4 'Structure model' 1 3 2023-08-30 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' 'Version format compliance' 
3 4 'Structure model' 'Data collection'           
4 4 'Structure model' 'Database references'       
5 4 'Structure model' 'Refinement description'    
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 4 'Structure model' chem_comp_atom                
2 4 'Structure model' chem_comp_bond                
3 4 'Structure model' database_2                    
4 4 'Structure model' pdbx_initial_refinement_model 
5 4 'Structure model' struct_ref_seq_dif            
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 4 'Structure model' '_database_2.pdbx_DOI'                
2 4 'Structure model' '_database_2.pdbx_database_accession' 
3 4 'Structure model' '_struct_ref_seq_dif.details'         
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
REFMAC       refinement        5.2.0005       ? 1 
CrystalClear 'data collection' '(MSC/RIGAKU)' ? 2 
HKL-2000     'data reduction'  .              ? 3 
HKL-2000     'data scaling'    .              ? 4 
PHASER       phasing           .              ? 5 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OE1 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   GLU 
_pdbx_validate_close_contact.auth_seq_id_1    64 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    157 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.17 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    ASN 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     931 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -111.80 
_pdbx_validate_torsion.psi             55.37 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 922 ? A GLY 1  
2  1 Y 1 A SER 923 ? A SER 2  
3  1 Y 1 A GLY 924 ? A GLY 3  
4  1 Y 1 A PRO 925 ? A PRO 4  
5  1 Y 1 A GLU 926 ? A GLU 5  
6  1 Y 1 A ALA 927 ? A ALA 6  
7  1 Y 1 A ALA 928 ? A ALA 7  
8  1 Y 1 A PRO 973 ? A PRO 52 
9  1 Y 1 B LEU 73  ? B LEU 73 
10 1 Y 1 B ARG 74  ? B ARG 74 
11 1 Y 1 B GLY 75  ? B GLY 75 
12 1 Y 1 B GLY 76  ? B GLY 76 
# 
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  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
GLN N    N N N 74  
GLN CA   C N S 75  
GLN C    C N N 76  
GLN O    O N N 77  
GLN CB   C N N 78  
GLN CG   C N N 79  
GLN CD   C N N 80  
GLN OE1  O N N 81  
GLN NE2  N N N 82  
GLN OXT  O N N 83  
GLN H    H N N 84  
GLN H2   H N N 85  
GLN HA   H N N 86  
GLN HB2  H N N 87  
GLN HB3  H N N 88  
GLN HG2  H N N 89  
GLN HG3  H N N 90  
GLN HE21 H N N 91  
GLN HE22 H N N 92  
GLN HXT  H N N 93  
GLU N    N N N 94  
GLU CA   C N S 95  
GLU C    C N N 96  
GLU O    O N N 97  
GLU CB   C N N 98  
GLU CG   C N N 99  
GLU CD   C N N 100 
GLU OE1  O N N 101 
GLU OE2  O N N 102 
GLU OXT  O N N 103 
GLU H    H N N 104 
GLU H2   H N N 105 
GLU HA   H N N 106 
GLU HB2  H N N 107 
GLU HB3  H N N 108 
GLU HG2  H N N 109 
GLU HG3  H N N 110 
GLU HE2  H N N 111 
GLU HXT  H N N 112 
GLY N    N N N 113 
GLY CA   C N N 114 
GLY C    C N N 115 
GLY O    O N N 116 
GLY OXT  O N N 117 
GLY H    H N N 118 
GLY H2   H N N 119 
GLY HA2  H N N 120 
GLY HA3  H N N 121 
GLY HXT  H N N 122 
HIS N    N N N 123 
HIS CA   C N S 124 
HIS C    C N N 125 
HIS O    O N N 126 
HIS CB   C N N 127 
HIS CG   C Y N 128 
HIS ND1  N Y N 129 
HIS CD2  C Y N 130 
HIS CE1  C Y N 131 
HIS NE2  N Y N 132 
HIS OXT  O N N 133 
HIS H    H N N 134 
HIS H2   H N N 135 
HIS HA   H N N 136 
HIS HB2  H N N 137 
HIS HB3  H N N 138 
HIS HD1  H N N 139 
HIS HD2  H N N 140 
HIS HE1  H N N 141 
HIS HE2  H N N 142 
HIS HXT  H N N 143 
HOH O    O N N 144 
HOH H1   H N N 145 
HOH H2   H N N 146 
ILE N    N N N 147 
ILE CA   C N S 148 
ILE C    C N N 149 
ILE O    O N N 150 
ILE CB   C N S 151 
ILE CG1  C N N 152 
ILE CG2  C N N 153 
ILE CD1  C N N 154 
ILE OXT  O N N 155 
ILE H    H N N 156 
ILE H2   H N N 157 
ILE HA   H N N 158 
ILE HB   H N N 159 
ILE HG12 H N N 160 
ILE HG13 H N N 161 
ILE HG21 H N N 162 
ILE HG22 H N N 163 
ILE HG23 H N N 164 
ILE HD11 H N N 165 
ILE HD12 H N N 166 
ILE HD13 H N N 167 
ILE HXT  H N N 168 
LEU N    N N N 169 
LEU CA   C N S 170 
LEU C    C N N 171 
LEU O    O N N 172 
LEU CB   C N N 173 
LEU CG   C N N 174 
LEU CD1  C N N 175 
LEU CD2  C N N 176 
LEU OXT  O N N 177 
LEU H    H N N 178 
LEU H2   H N N 179 
LEU HA   H N N 180 
LEU HB2  H N N 181 
LEU HB3  H N N 182 
LEU HG   H N N 183 
LEU HD11 H N N 184 
LEU HD12 H N N 185 
LEU HD13 H N N 186 
LEU HD21 H N N 187 
LEU HD22 H N N 188 
LEU HD23 H N N 189 
LEU HXT  H N N 190 
LYS N    N N N 191 
LYS CA   C N S 192 
LYS C    C N N 193 
LYS O    O N N 194 
LYS CB   C N N 195 
LYS CG   C N N 196 
LYS CD   C N N 197 
LYS CE   C N N 198 
LYS NZ   N N N 199 
LYS OXT  O N N 200 
LYS H    H N N 201 
LYS H2   H N N 202 
LYS HA   H N N 203 
LYS HB2  H N N 204 
LYS HB3  H N N 205 
LYS HG2  H N N 206 
LYS HG3  H N N 207 
LYS HD2  H N N 208 
LYS HD3  H N N 209 
LYS HE2  H N N 210 
LYS HE3  H N N 211 
LYS HZ1  H N N 212 
LYS HZ2  H N N 213 
LYS HZ3  H N N 214 
LYS HXT  H N N 215 
MET N    N N N 216 
MET CA   C N S 217 
MET C    C N N 218 
MET O    O N N 219 
MET CB   C N N 220 
MET CG   C N N 221 
MET SD   S N N 222 
MET CE   C N N 223 
MET OXT  O N N 224 
MET H    H N N 225 
MET H2   H N N 226 
MET HA   H N N 227 
MET HB2  H N N 228 
MET HB3  H N N 229 
MET HG2  H N N 230 
MET HG3  H N N 231 
MET HE1  H N N 232 
MET HE2  H N N 233 
MET HE3  H N N 234 
MET HXT  H N N 235 
PHE N    N N N 236 
PHE CA   C N S 237 
PHE C    C N N 238 
PHE O    O N N 239 
PHE CB   C N N 240 
PHE CG   C Y N 241 
PHE CD1  C Y N 242 
PHE CD2  C Y N 243 
PHE CE1  C Y N 244 
PHE CE2  C Y N 245 
PHE CZ   C Y N 246 
PHE OXT  O N N 247 
PHE H    H N N 248 
PHE H2   H N N 249 
PHE HA   H N N 250 
PHE HB2  H N N 251 
PHE HB3  H N N 252 
PHE HD1  H N N 253 
PHE HD2  H N N 254 
PHE HE1  H N N 255 
PHE HE2  H N N 256 
PHE HZ   H N N 257 
PHE HXT  H N N 258 
PRO N    N N N 259 
PRO CA   C N S 260 
PRO C    C N N 261 
PRO O    O N N 262 
PRO CB   C N N 263 
PRO CG   C N N 264 
PRO CD   C N N 265 
PRO OXT  O N N 266 
PRO H    H N N 267 
PRO HA   H N N 268 
PRO HB2  H N N 269 
PRO HB3  H N N 270 
PRO HG2  H N N 271 
PRO HG3  H N N 272 
PRO HD2  H N N 273 
PRO HD3  H N N 274 
PRO HXT  H N N 275 
SER N    N N N 276 
SER CA   C N S 277 
SER C    C N N 278 
SER O    O N N 279 
SER CB   C N N 280 
SER OG   O N N 281 
SER OXT  O N N 282 
SER H    H N N 283 
SER H2   H N N 284 
SER HA   H N N 285 
SER HB2  H N N 286 
SER HB3  H N N 287 
SER HG   H N N 288 
SER HXT  H N N 289 
THR N    N N N 290 
THR CA   C N S 291 
THR C    C N N 292 
THR O    O N N 293 
THR CB   C N R 294 
THR OG1  O N N 295 
THR CG2  C N N 296 
THR OXT  O N N 297 
THR H    H N N 298 
THR H2   H N N 299 
THR HA   H N N 300 
THR HB   H N N 301 
THR HG1  H N N 302 
THR HG21 H N N 303 
THR HG22 H N N 304 
THR HG23 H N N 305 
THR HXT  H N N 306 
TYR N    N N N 307 
TYR CA   C N S 308 
TYR C    C N N 309 
TYR O    O N N 310 
TYR CB   C N N 311 
TYR CG   C Y N 312 
TYR CD1  C Y N 313 
TYR CD2  C Y N 314 
TYR CE1  C Y N 315 
TYR CE2  C Y N 316 
TYR CZ   C Y N 317 
TYR OH   O N N 318 
TYR OXT  O N N 319 
TYR H    H N N 320 
TYR H2   H N N 321 
TYR HA   H N N 322 
TYR HB2  H N N 323 
TYR HB3  H N N 324 
TYR HD1  H N N 325 
TYR HD2  H N N 326 
TYR HE1  H N N 327 
TYR HE2  H N N 328 
TYR HH   H N N 329 
TYR HXT  H N N 330 
VAL N    N N N 331 
VAL CA   C N S 332 
VAL C    C N N 333 
VAL O    O N N 334 
VAL CB   C N N 335 
VAL CG1  C N N 336 
VAL CG2  C N N 337 
VAL OXT  O N N 338 
VAL H    H N N 339 
VAL H2   H N N 340 
VAL HA   H N N 341 
VAL HB   H N N 342 
VAL HG11 H N N 343 
VAL HG12 H N N 344 
VAL HG13 H N N 345 
VAL HG21 H N N 346 
VAL HG22 H N N 347 
VAL HG23 H N N 348 
VAL HXT  H N N 349 
# 
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  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
GLN N   CA   sing N N 70  
GLN N   H    sing N N 71  
GLN N   H2   sing N N 72  
GLN CA  C    sing N N 73  
GLN CA  CB   sing N N 74  
GLN CA  HA   sing N N 75  
GLN C   O    doub N N 76  
GLN C   OXT  sing N N 77  
GLN CB  CG   sing N N 78  
GLN CB  HB2  sing N N 79  
GLN CB  HB3  sing N N 80  
GLN CG  CD   sing N N 81  
GLN CG  HG2  sing N N 82  
GLN CG  HG3  sing N N 83  
GLN CD  OE1  doub N N 84  
GLN CD  NE2  sing N N 85  
GLN NE2 HE21 sing N N 86  
GLN NE2 HE22 sing N N 87  
GLN OXT HXT  sing N N 88  
GLU N   CA   sing N N 89  
GLU N   H    sing N N 90  
GLU N   H2   sing N N 91  
GLU CA  C    sing N N 92  
GLU CA  CB   sing N N 93  
GLU CA  HA   sing N N 94  
GLU C   O    doub N N 95  
GLU C   OXT  sing N N 96  
GLU CB  CG   sing N N 97  
GLU CB  HB2  sing N N 98  
GLU CB  HB3  sing N N 99  
GLU CG  CD   sing N N 100 
GLU CG  HG2  sing N N 101 
GLU CG  HG3  sing N N 102 
GLU CD  OE1  doub N N 103 
GLU CD  OE2  sing N N 104 
GLU OE2 HE2  sing N N 105 
GLU OXT HXT  sing N N 106 
GLY N   CA   sing N N 107 
GLY N   H    sing N N 108 
GLY N   H2   sing N N 109 
GLY CA  C    sing N N 110 
GLY CA  HA2  sing N N 111 
GLY CA  HA3  sing N N 112 
GLY C   O    doub N N 113 
GLY C   OXT  sing N N 114 
GLY OXT HXT  sing N N 115 
HIS N   CA   sing N N 116 
HIS N   H    sing N N 117 
HIS N   H2   sing N N 118 
HIS CA  C    sing N N 119 
HIS CA  CB   sing N N 120 
HIS CA  HA   sing N N 121 
HIS C   O    doub N N 122 
HIS C   OXT  sing N N 123 
HIS CB  CG   sing N N 124 
HIS CB  HB2  sing N N 125 
HIS CB  HB3  sing N N 126 
HIS CG  ND1  sing Y N 127 
HIS CG  CD2  doub Y N 128 
HIS ND1 CE1  doub Y N 129 
HIS ND1 HD1  sing N N 130 
HIS CD2 NE2  sing Y N 131 
HIS CD2 HD2  sing N N 132 
HIS CE1 NE2  sing Y N 133 
HIS CE1 HE1  sing N N 134 
HIS NE2 HE2  sing N N 135 
HIS OXT HXT  sing N N 136 
HOH O   H1   sing N N 137 
HOH O   H2   sing N N 138 
ILE N   CA   sing N N 139 
ILE N   H    sing N N 140 
ILE N   H2   sing N N 141 
ILE CA  C    sing N N 142 
ILE CA  CB   sing N N 143 
ILE CA  HA   sing N N 144 
ILE C   O    doub N N 145 
ILE C   OXT  sing N N 146 
ILE CB  CG1  sing N N 147 
ILE CB  CG2  sing N N 148 
ILE CB  HB   sing N N 149 
ILE CG1 CD1  sing N N 150 
ILE CG1 HG12 sing N N 151 
ILE CG1 HG13 sing N N 152 
ILE CG2 HG21 sing N N 153 
ILE CG2 HG22 sing N N 154 
ILE CG2 HG23 sing N N 155 
ILE CD1 HD11 sing N N 156 
ILE CD1 HD12 sing N N 157 
ILE CD1 HD13 sing N N 158 
ILE OXT HXT  sing N N 159 
LEU N   CA   sing N N 160 
LEU N   H    sing N N 161 
LEU N   H2   sing N N 162 
LEU CA  C    sing N N 163 
LEU CA  CB   sing N N 164 
LEU CA  HA   sing N N 165 
LEU C   O    doub N N 166 
LEU C   OXT  sing N N 167 
LEU CB  CG   sing N N 168 
LEU CB  HB2  sing N N 169 
LEU CB  HB3  sing N N 170 
LEU CG  CD1  sing N N 171 
LEU CG  CD2  sing N N 172 
LEU CG  HG   sing N N 173 
LEU CD1 HD11 sing N N 174 
LEU CD1 HD12 sing N N 175 
LEU CD1 HD13 sing N N 176 
LEU CD2 HD21 sing N N 177 
LEU CD2 HD22 sing N N 178 
LEU CD2 HD23 sing N N 179 
LEU OXT HXT  sing N N 180 
LYS N   CA   sing N N 181 
LYS N   H    sing N N 182 
LYS N   H2   sing N N 183 
LYS CA  C    sing N N 184 
LYS CA  CB   sing N N 185 
LYS CA  HA   sing N N 186 
LYS C   O    doub N N 187 
LYS C   OXT  sing N N 188 
LYS CB  CG   sing N N 189 
LYS CB  HB2  sing N N 190 
LYS CB  HB3  sing N N 191 
LYS CG  CD   sing N N 192 
LYS CG  HG2  sing N N 193 
LYS CG  HG3  sing N N 194 
LYS CD  CE   sing N N 195 
LYS CD  HD2  sing N N 196 
LYS CD  HD3  sing N N 197 
LYS CE  NZ   sing N N 198 
LYS CE  HE2  sing N N 199 
LYS CE  HE3  sing N N 200 
LYS NZ  HZ1  sing N N 201 
LYS NZ  HZ2  sing N N 202 
LYS NZ  HZ3  sing N N 203 
LYS OXT HXT  sing N N 204 
MET N   CA   sing N N 205 
MET N   H    sing N N 206 
MET N   H2   sing N N 207 
MET CA  C    sing N N 208 
MET CA  CB   sing N N 209 
MET CA  HA   sing N N 210 
MET C   O    doub N N 211 
MET C   OXT  sing N N 212 
MET CB  CG   sing N N 213 
MET CB  HB2  sing N N 214 
MET CB  HB3  sing N N 215 
MET CG  SD   sing N N 216 
MET CG  HG2  sing N N 217 
MET CG  HG3  sing N N 218 
MET SD  CE   sing N N 219 
MET CE  HE1  sing N N 220 
MET CE  HE2  sing N N 221 
MET CE  HE3  sing N N 222 
MET OXT HXT  sing N N 223 
PHE N   CA   sing N N 224 
PHE N   H    sing N N 225 
PHE N   H2   sing N N 226 
PHE CA  C    sing N N 227 
PHE CA  CB   sing N N 228 
PHE CA  HA   sing N N 229 
PHE C   O    doub N N 230 
PHE C   OXT  sing N N 231 
PHE CB  CG   sing N N 232 
PHE CB  HB2  sing N N 233 
PHE CB  HB3  sing N N 234 
PHE CG  CD1  doub Y N 235 
PHE CG  CD2  sing Y N 236 
PHE CD1 CE1  sing Y N 237 
PHE CD1 HD1  sing N N 238 
PHE CD2 CE2  doub Y N 239 
PHE CD2 HD2  sing N N 240 
PHE CE1 CZ   doub Y N 241 
PHE CE1 HE1  sing N N 242 
PHE CE2 CZ   sing Y N 243 
PHE CE2 HE2  sing N N 244 
PHE CZ  HZ   sing N N 245 
PHE OXT HXT  sing N N 246 
PRO N   CA   sing N N 247 
PRO N   CD   sing N N 248 
PRO N   H    sing N N 249 
PRO CA  C    sing N N 250 
PRO CA  CB   sing N N 251 
PRO CA  HA   sing N N 252 
PRO C   O    doub N N 253 
PRO C   OXT  sing N N 254 
PRO CB  CG   sing N N 255 
PRO CB  HB2  sing N N 256 
PRO CB  HB3  sing N N 257 
PRO CG  CD   sing N N 258 
PRO CG  HG2  sing N N 259 
PRO CG  HG3  sing N N 260 
PRO CD  HD2  sing N N 261 
PRO CD  HD3  sing N N 262 
PRO OXT HXT  sing N N 263 
SER N   CA   sing N N 264 
SER N   H    sing N N 265 
SER N   H2   sing N N 266 
SER CA  C    sing N N 267 
SER CA  CB   sing N N 268 
SER CA  HA   sing N N 269 
SER C   O    doub N N 270 
SER C   OXT  sing N N 271 
SER CB  OG   sing N N 272 
SER CB  HB2  sing N N 273 
SER CB  HB3  sing N N 274 
SER OG  HG   sing N N 275 
SER OXT HXT  sing N N 276 
THR N   CA   sing N N 277 
THR N   H    sing N N 278 
THR N   H2   sing N N 279 
THR CA  C    sing N N 280 
THR CA  CB   sing N N 281 
THR CA  HA   sing N N 282 
THR C   O    doub N N 283 
THR C   OXT  sing N N 284 
THR CB  OG1  sing N N 285 
THR CB  CG2  sing N N 286 
THR CB  HB   sing N N 287 
THR OG1 HG1  sing N N 288 
THR CG2 HG21 sing N N 289 
THR CG2 HG22 sing N N 290 
THR CG2 HG23 sing N N 291 
THR OXT HXT  sing N N 292 
TYR N   CA   sing N N 293 
TYR N   H    sing N N 294 
TYR N   H2   sing N N 295 
TYR CA  C    sing N N 296 
TYR CA  CB   sing N N 297 
TYR CA  HA   sing N N 298 
TYR C   O    doub N N 299 
TYR C   OXT  sing N N 300 
TYR CB  CG   sing N N 301 
TYR CB  HB2  sing N N 302 
TYR CB  HB3  sing N N 303 
TYR CG  CD1  doub Y N 304 
TYR CG  CD2  sing Y N 305 
TYR CD1 CE1  sing Y N 306 
TYR CD1 HD1  sing N N 307 
TYR CD2 CE2  doub Y N 308 
TYR CD2 HD2  sing N N 309 
TYR CE1 CZ   doub Y N 310 
TYR CE1 HE1  sing N N 311 
TYR CE2 CZ   sing Y N 312 
TYR CE2 HE2  sing N N 313 
TYR CZ  OH   sing N N 314 
TYR OH  HH   sing N N 315 
TYR OXT HXT  sing N N 316 
VAL N   CA   sing N N 317 
VAL N   H    sing N N 318 
VAL N   H2   sing N N 319 
VAL CA  C    sing N N 320 
VAL CA  CB   sing N N 321 
VAL CA  HA   sing N N 322 
VAL C   O    doub N N 323 
VAL C   OXT  sing N N 324 
VAL CB  CG1  sing N N 325 
VAL CB  CG2  sing N N 326 
VAL CB  HB   sing N N 327 
VAL CG1 HG11 sing N N 328 
VAL CG1 HG12 sing N N 329 
VAL CG1 HG13 sing N N 330 
VAL CG2 HG21 sing N N 331 
VAL CG2 HG22 sing N N 332 
VAL CG2 HG23 sing N N 333 
VAL OXT HXT  sing N N 334 
# 
_pdbx_entity_nonpoly.entity_id   3 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_pdbx_initial_refinement_model.id 
_pdbx_initial_refinement_model.entity_id_list 
_pdbx_initial_refinement_model.type 
_pdbx_initial_refinement_model.source_name 
_pdbx_initial_refinement_model.accession_code 
_pdbx_initial_refinement_model.details 
1 ? 'experimental model' PDB 1UBQ 'pdb entries 1UBQ, 2OOA' 
2 ? 'experimental model' PDB 2OOA 'pdb entries 1UBQ, 2OOA' 
# 
