4i6p.cif

data_4I6P
# 
_entry.id   4I6P 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.287 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   4I6P         
RCSB  RCSB076372   
WWPDB D_1000076372 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.db_id          3ZEE 
_pdbx_database_related.details        'Structure of helical assembly' 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        4I6P 
_pdbx_database_status.recvd_initial_deposition_date   2012-11-29 
_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.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Wang, W.' 1 
'Gao, F.'  2 
'Gong, W.' 3 
'Sun, F.'  4 
'Feng, W.' 5 
# 
_citation.id                        primary 
_citation.title                     'Structural insights into the intrinsic self-assembly of par-3 N-terminal domain.' 
_citation.journal_abbrev            Structure 
_citation.journal_volume            21 
_citation.page_first                997 
_citation.page_last                 1006 
_citation.year                      2013 
_citation.journal_id_ASTM           STRUE6 
_citation.country                   UK 
_citation.journal_id_ISSN           0969-2126 
_citation.journal_id_CSD            2005 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   23643951 
_citation.pdbx_database_id_DOI      10.1016/j.str.2013.04.004 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Zhang, Y.'       1  
primary 'Wang, W.'        2  
primary 'Chen, J.'        3  
primary 'Zhang, K.'       4  
primary 'Gao, F.'         5  
primary 'Gao, B.'         6  
primary 'Zhang, S.'       7  
primary 'Dong, M.'        8  
primary 'Besenbacher, F.' 9  
primary 'Gong, W.'        10 
primary 'Zhang, M.'       11 
primary 'Sun, F.'         12 
primary 'Feng, W.'        13 
# 
_cell.entry_id           4I6P 
_cell.length_a           108.780 
_cell.length_b           108.780 
_cell.length_c           46.730 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              16 
_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                         4I6P 
_symmetry.space_group_name_H-M             'P 43 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                96 
_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 'Partitioning defective 3 homolog' 9879.212 2  ? ? 'N-terminal domain of Par3' ? 
2 water   nat water                              18.015   34 ? ? ?                           ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'PAR-3, PARD-3, Atypical PKC isotype-specific-interacting protein, ASIP, Atypical PKC-specific-binding protein, ASBP' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GPGSEFKVTVCFGRTRVVVPCGDGRMKVFSLIQQAVTRYRKAVAKDPNYWIQVHRLEHGDGGILDLDDILCDVADDKDRL
VAVFDEQD
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GPGSEFKVTVCFGRTRVVVPCGDGRMKVFSLIQQAVTRYRKAVAKDPNYWIQVHRLEHGDGGILDLDDILCDVADDKDRL
VAVFDEQD
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
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  PRO n 
1 3  GLY n 
1 4  SER n 
1 5  GLU n 
1 6  PHE n 
1 7  LYS n 
1 8  VAL n 
1 9  THR n 
1 10 VAL n 
1 11 CYS n 
1 12 PHE n 
1 13 GLY n 
1 14 ARG n 
1 15 THR n 
1 16 ARG n 
1 17 VAL n 
1 18 VAL n 
1 19 VAL n 
1 20 PRO n 
1 21 CYS n 
1 22 GLY n 
1 23 ASP n 
1 24 GLY n 
1 25 ARG n 
1 26 MET n 
1 27 LYS n 
1 28 VAL n 
1 29 PHE n 
1 30 SER n 
1 31 LEU n 
1 32 ILE n 
1 33 GLN n 
1 34 GLN n 
1 35 ALA n 
1 36 VAL n 
1 37 THR n 
1 38 ARG n 
1 39 TYR n 
1 40 ARG n 
1 41 LYS n 
1 42 ALA n 
1 43 VAL n 
1 44 ALA n 
1 45 LYS n 
1 46 ASP n 
1 47 PRO n 
1 48 ASN n 
1 49 TYR n 
1 50 TRP n 
1 51 ILE n 
1 52 GLN n 
1 53 VAL n 
1 54 HIS n 
1 55 ARG n 
1 56 LEU n 
1 57 GLU n 
1 58 HIS n 
1 59 GLY n 
1 60 ASP n 
1 61 GLY n 
1 62 GLY n 
1 63 ILE n 
1 64 LEU n 
1 65 ASP n 
1 66 LEU n 
1 67 ASP n 
1 68 ASP n 
1 69 ILE n 
1 70 LEU n 
1 71 CYS n 
1 72 ASP n 
1 73 VAL n 
1 74 ALA n 
1 75 ASP n 
1 76 ASP n 
1 77 LYS n 
1 78 ASP n 
1 79 ARG n 
1 80 LEU n 
1 81 VAL n 
1 82 ALA n 
1 83 VAL n 
1 84 PHE n 
1 85 ASP n 
1 86 GLU n 
1 87 GLN n 
1 88 ASP 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               'brown rat,rat,rats' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'Pard3, Par3' 
_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      'Rattus norvegicus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     10116 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     511693 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21-Codon Plus' 
_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                       pET32a 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    PARD3_RAT 
_struct_ref.pdbx_db_accession          Q9Z340 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;KVTVCFGRTRVVVPCGDGRMKVFSLIQQAVTRYRKAVAKDPNYWIQVHRLEHGDGGILDLDDILCDVADDKDRLVAVFDE
QD
;
_struct_ref.pdbx_align_begin           2 
_struct_ref.pdbx_db_isoform            ? 
# 
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 4I6P A 7 ? 88 ? Q9Z340 2 ? 83 ? 2 83 
2 1 4I6P B 7 ? 88 ? Q9Z340 2 ? 83 ? 2 83 
# 
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 4I6P GLY A 1 ? UNP Q9Z340 ? ? 'EXPRESSION TAG' -4 1  
1 4I6P PRO A 2 ? UNP Q9Z340 ? ? 'EXPRESSION TAG' -3 2  
1 4I6P GLY A 3 ? UNP Q9Z340 ? ? 'EXPRESSION TAG' -2 3  
1 4I6P SER A 4 ? UNP Q9Z340 ? ? 'EXPRESSION TAG' -1 4  
1 4I6P GLU A 5 ? UNP Q9Z340 ? ? 'EXPRESSION TAG' 0  5  
1 4I6P PHE A 6 ? UNP Q9Z340 ? ? 'EXPRESSION TAG' 1  6  
2 4I6P GLY B 1 ? UNP Q9Z340 ? ? 'EXPRESSION TAG' -4 7  
2 4I6P PRO B 2 ? UNP Q9Z340 ? ? 'EXPRESSION TAG' -3 8  
2 4I6P GLY B 3 ? UNP Q9Z340 ? ? 'EXPRESSION TAG' -2 9  
2 4I6P SER B 4 ? UNP Q9Z340 ? ? 'EXPRESSION TAG' -1 10 
2 4I6P GLU B 5 ? UNP Q9Z340 ? ? 'EXPRESSION TAG' 0  11 
2 4I6P PHE B 6 ? UNP Q9Z340 ? ? 'EXPRESSION TAG' 1  12 
# 
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 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
_exptl.entry_id          4I6P 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      3.50 
_exptl_crystal.density_percent_sol   64.84 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.temp            289.15 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pdbx_details    
'1.6 M ammonium sulfate, 100 mM HEPES, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 289.15K' 
_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               CCD 
_diffrn_detector.type                   'RAYONIX MX-225' 
_diffrn_detector.pdbx_collection_date   2010-12-01 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    'Double crystal Si(111)' 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.979 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'SSRF BEAMLINE BL17U' 
_diffrn_source.pdbx_synchrotron_site       SSRF 
_diffrn_source.pdbx_synchrotron_beamline   BL17U 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        0.979 
# 
_reflns.entry_id                     4I6P 
_reflns.observed_criterion_sigma_I   -2 
_reflns.observed_criterion_sigma_F   0 
_reflns.d_resolution_low             50 
_reflns.d_resolution_high            2.9 
_reflns.number_obs                   6406 
_reflns.number_all                   6597 
_reflns.percent_possible_obs         97.1 
_reflns.pdbx_Rmerge_I_obs            0.148 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        17.0 
_reflns.B_iso_Wilson_estimate        48 
_reflns.pdbx_redundancy              7.6 
_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_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_high             2.9 
_reflns_shell.d_res_low              3.0 
_reflns_shell.percent_possible_all   100 
_reflns_shell.Rmerge_I_obs           0.477 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    5.3 
_reflns_shell.pdbx_redundancy        7.9 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      617 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.pdbx_diffrn_id         1 
# 
_refine.entry_id                                 4I6P 
_refine.ls_number_reflns_obs                     6058 
_refine.ls_number_reflns_all                     6289 
_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                             39.94 
_refine.ls_d_res_high                            2.90 
_refine.ls_percent_reflns_obs                    96.33 
_refine.ls_R_factor_obs                          0.23296 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.23005 
_refine.ls_R_factor_R_free                       0.29361 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.7 
_refine.ls_number_reflns_R_free                  301 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.918 
_refine.correlation_coeff_Fo_to_Fc_free          0.860 
_refine.B_iso_mean                               55.809 
_refine.aniso_B[1][1]                            -0.43 
_refine.aniso_B[2][2]                            -0.43 
_refine.aniso_B[3][3]                            0.85 
_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                                  'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT' 
_refine.pdbx_starting_model                      2NS5 
_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                       1.008 
_refine.pdbx_overall_ESU_R_Free                  0.415 
_refine.overall_SU_ML                            0.350 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             19.255 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_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_diffrn_id                           1 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_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        1323 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.number_atoms_solvent             34 
_refine_hist.number_atoms_total               1357 
_refine_hist.d_res_high                       2.90 
_refine_hist.d_res_low                        39.94 
# 
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_restraint_function 
_refine_ls_restr.pdbx_refine_id 
r_bond_refined_d       0.012  0.019  ? 1345 ? 'X-RAY DIFFRACTION' 
r_angle_refined_deg    1.791  1.948  ? 1816 ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_1_deg 7.769  5.000  ? 164  ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_2_deg 34.930 23.333 ? 69   ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_3_deg 19.812 15.000 ? 235  ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_4_deg 17.571 15.000 ? 14   ? 'X-RAY DIFFRACTION' 
r_chiral_restr         0.120  0.200  ? 204  ? 'X-RAY DIFFRACTION' 
r_gen_planes_refined   0.006  0.020  ? 1022 ? 'X-RAY DIFFRACTION' 
# 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       2.900 
_refine_ls_shell.d_res_low                        2.975 
_refine_ls_shell.number_reflns_R_work             343 
_refine_ls_shell.R_factor_R_work                  0.307 
_refine_ls_shell.percent_reflns_obs               89.88 
_refine_ls_shell.R_factor_R_free                  0.325 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             21 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.number_reflns_obs                343 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  4I6P 
_struct.title                     'Crystal structure of Par3-NTD domain' 
_struct.pdbx_descriptor           'Partitioning defective 3 homolog' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4I6P 
_struct_keywords.pdbx_keywords   'SIGNALING PROTEIN' 
_struct_keywords.text            'PB1 like motif, DUF3534, Cell polarity protein, SIGNALING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
# 
_struct_biol.id        1 
_struct_biol.details   
;This protein forms helical filament in solution. Cryo-electron microscopic reconstruction revealed that the dimer in the crystallographic asymmetric unit is the same as the building block of the helical filament.
;
# 
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 LYS A 27 ? ALA A 44 ? LYS A 22 ALA A 39 1 ? 18 
HELX_P HELX_P2 2 ILE A 69 ? ALA A 74 ? ILE A 64 ALA A 69 1 ? 6  
HELX_P HELX_P3 3 LYS B 27 ? ALA B 44 ? LYS B 22 ALA B 39 1 ? 18 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          ALA 
_struct_mon_prot_cis.label_seq_id           44 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           ALA 
_struct_mon_prot_cis.auth_seq_id            39 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   LYS 
_struct_mon_prot_cis.pdbx_label_seq_id_2    45 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    LYS 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     40 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       -1.50 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 5 ? 
B ? 4 ? 
# 
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 ? parallel      
B 1 2 ? anti-parallel 
B 2 3 ? parallel      
B 3 4 ? 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 ILE A 51 ? GLU A 57 ? ILE A 46 GLU A 52 
A 2 ARG A 79 ? GLU A 86 ? ARG A 74 GLU A 81 
A 3 PHE A 6  ? PHE A 12 ? PHE A 1  PHE A 7  
A 4 THR A 15 ? GLY A 22 ? THR A 10 GLY A 17 
A 5 GLY B 62 ? LEU B 64 ? GLY B 57 LEU B 59 
B 1 THR B 15 ? GLY B 22 ? THR B 10 GLY B 17 
B 2 PHE B 6  ? PHE B 12 ? PHE B 1  PHE B 7  
B 3 ARG B 79 ? ASP B 85 ? ARG B 74 ASP B 80 
B 4 GLN B 52 ? GLU B 57 ? GLN B 47 GLU B 52 
# 
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 N GLN A 52 ? N GLN A 47 O ASP A 85 ? O ASP A 80 
A 2 3 O LEU A 80 ? O LEU A 75 N CYS A 11 ? N CYS A 6  
A 3 4 N PHE A 6  ? N PHE A 1  O CYS A 21 ? O CYS A 16 
A 4 5 N VAL A 18 ? N VAL A 13 O ILE B 63 ? O ILE B 58 
B 1 2 O CYS B 21 ? O CYS B 16 N PHE B 6  ? N PHE B 1  
B 2 3 N THR B 9  ? N THR B 4  O LEU B 80 ? O LEU B 75 
B 3 4 O ASP B 85 ? O ASP B 80 N GLN B 52 ? N GLN B 47 
# 
_database_PDB_matrix.entry_id          4I6P 
_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                    4I6P 
_atom_sites.fract_transf_matrix[1][1]   0.009193 
_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]   0.009193 
_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]   0.021400 
_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   . SER A 1 4  ? 7.327   32.198 13.137  1.00 67.08  ? -1  SER A N   1 
ATOM   2    C CA  . SER A 1 4  ? 7.212   33.699 13.019  1.00 75.39  ? -1  SER A CA  1 
ATOM   3    C C   . SER A 1 4  ? 6.310   34.194 11.863  1.00 78.94  ? -1  SER A C   1 
ATOM   4    O O   . SER A 1 4  ? 5.127   33.814 11.713  1.00 74.56  ? -1  SER A O   1 
ATOM   5    C CB  . SER A 1 4  ? 8.602   34.343 12.844  1.00 73.77  ? -1  SER A CB  1 
ATOM   6    O OG  . SER A 1 4  ? 9.149   34.885 14.031  1.00 71.80  ? -1  SER A OG  1 
ATOM   7    N N   . GLU A 1 5  ? 6.890   35.072 11.055  1.00 77.04  ? 0   GLU A N   1 
ATOM   8    C CA  . GLU A 1 5  ? 6.181   35.621 9.931   1.00 77.58  ? 0   GLU A CA  1 
ATOM   9    C C   . GLU A 1 5  ? 6.902   35.310 8.624   1.00 70.23  ? 0   GLU A C   1 
ATOM   10   O O   . GLU A 1 5  ? 6.235   34.988 7.632   1.00 69.54  ? 0   GLU A O   1 
ATOM   11   C CB  . GLU A 1 5  ? 5.828   37.127 10.112  1.00 82.88  ? 0   GLU A CB  1 
ATOM   12   C CG  . GLU A 1 5  ? 6.901   38.029 10.718  1.00 85.25  ? 0   GLU A CG  1 
ATOM   13   C CD  . GLU A 1 5  ? 6.958   37.981 12.249  1.00 99.39  ? 0   GLU A CD  1 
ATOM   14   O OE1 . GLU A 1 5  ? 5.892   38.018 12.922  1.00 93.83  ? 0   GLU A OE1 1 
ATOM   15   O OE2 . GLU A 1 5  ? 8.090   37.917 12.789  1.00 104.08 ? 0   GLU A OE2 1 
ATOM   16   N N   . PHE A 1 6  ? 8.239   35.368 8.622   1.00 57.26  ? 1   PHE A N   1 
ATOM   17   C CA  . PHE A 1 6  ? 8.962   35.378 7.332   1.00 53.48  ? 1   PHE A CA  1 
ATOM   18   C C   . PHE A 1 6  ? 8.653   34.129 6.469   1.00 50.84  ? 1   PHE A C   1 
ATOM   19   O O   . PHE A 1 6  ? 8.698   33.002 6.974   1.00 48.75  ? 1   PHE A O   1 
ATOM   20   C CB  . PHE A 1 6  ? 10.472  35.602 7.511   1.00 47.81  ? 1   PHE A CB  1 
ATOM   21   C CG  . PHE A 1 6  ? 11.147  36.198 6.301   1.00 45.73  ? 1   PHE A CG  1 
ATOM   22   C CD1 . PHE A 1 6  ? 11.221  35.495 5.090   1.00 46.09  ? 1   PHE A CD1 1 
ATOM   23   C CD2 . PHE A 1 6  ? 11.719  37.464 6.361   1.00 45.04  ? 1   PHE A CD2 1 
ATOM   24   C CE1 . PHE A 1 6  ? 11.838  36.050 3.973   1.00 42.27  ? 1   PHE A CE1 1 
ATOM   25   C CE2 . PHE A 1 6  ? 12.332  38.029 5.241   1.00 42.09  ? 1   PHE A CE2 1 
ATOM   26   C CZ  . PHE A 1 6  ? 12.388  37.322 4.046   1.00 41.75  ? 1   PHE A CZ  1 
ATOM   27   N N   . LYS A 1 7  ? 8.293   34.341 5.194   1.00 44.92  ? 2   LYS A N   1 
ATOM   28   C CA  . LYS A 1 7  ? 7.989   33.228 4.265   1.00 45.28  ? 2   LYS A CA  1 
ATOM   29   C C   . LYS A 1 7  ? 8.335   33.579 2.829   1.00 45.65  ? 2   LYS A C   1 
ATOM   30   O O   . LYS A 1 7  ? 8.355   34.758 2.468   1.00 47.71  ? 2   LYS A O   1 
ATOM   31   C CB  . LYS A 1 7  ? 6.521   32.780 4.349   1.00 41.94  ? 2   LYS A CB  1 
ATOM   32   C CG  . LYS A 1 7  ? 5.540   33.853 3.925   1.00 48.25  ? 2   LYS A CG  1 
ATOM   33   C CD  . LYS A 1 7  ? 4.095   33.647 4.372   1.00 48.06  ? 2   LYS A CD  1 
ATOM   34   C CE  . LYS A 1 7  ? 3.433   35.010 4.667   1.00 48.95  ? 2   LYS A CE  1 
ATOM   35   N NZ  . LYS A 1 7  ? 1.942   34.957 4.586   1.00 45.58  ? 2   LYS A NZ  1 
ATOM   36   N N   . VAL A 1 8  ? 8.605   32.553 2.021   1.00 43.86  ? 3   VAL A N   1 
ATOM   37   C CA  . VAL A 1 8  ? 8.852   32.720 0.572   1.00 41.44  ? 3   VAL A CA  1 
ATOM   38   C C   . VAL A 1 8  ? 8.172   31.648 -0.290  1.00 41.47  ? 3   VAL A C   1 
ATOM   39   O O   . VAL A 1 8  ? 7.883   30.525 0.142   1.00 39.90  ? 3   VAL A O   1 
ATOM   40   C CB  . VAL A 1 8  ? 10.368  32.686 0.206   1.00 40.74  ? 3   VAL A CB  1 
ATOM   41   C CG1 . VAL A 1 8  ? 11.072  34.001 0.529   1.00 38.90  ? 3   VAL A CG1 1 
ATOM   42   C CG2 . VAL A 1 8  ? 11.083  31.486 0.829   1.00 36.28  ? 3   VAL A CG2 1 
ATOM   43   N N   . THR A 1 9  ? 7.946   31.969 -1.542  1.00 42.62  ? 4   THR A N   1 
ATOM   44   C CA  . THR A 1 9  ? 7.536   30.912 -2.429  1.00 48.06  ? 4   THR A CA  1 
ATOM   45   C C   . THR A 1 9  ? 8.706   30.567 -3.347  1.00 49.03  ? 4   THR A C   1 
ATOM   46   O O   . THR A 1 9  ? 9.477   31.462 -3.739  1.00 48.34  ? 4   THR A O   1 
ATOM   47   C CB  . THR A 1 9  ? 6.259   31.276 -3.211  1.00 52.74  ? 4   THR A CB  1 
ATOM   48   O OG1 . THR A 1 9  ? 5.333   31.904 -2.311  1.00 56.70  ? 4   THR A OG1 1 
ATOM   49   C CG2 . THR A 1 9  ? 5.611   30.013 -3.819  1.00 50.71  ? 4   THR A CG2 1 
ATOM   50   N N   . VAL A 1 10 ? 8.841   29.269 -3.640  1.00 44.23  ? 5   VAL A N   1 
ATOM   51   C CA  . VAL A 1 10 ? 9.875   28.758 -4.514  1.00 43.20  ? 5   VAL A CA  1 
ATOM   52   C C   . VAL A 1 10 ? 9.268   27.960 -5.661  1.00 42.27  ? 5   VAL A C   1 
ATOM   53   O O   . VAL A 1 10 ? 8.641   26.935 -5.451  1.00 41.74  ? 5   VAL A O   1 
ATOM   54   C CB  . VAL A 1 10 ? 10.866  27.822 -3.772  1.00 42.70  ? 5   VAL A CB  1 
ATOM   55   C CG1 . VAL A 1 10 ? 11.879  27.270 -4.767  1.00 42.59  ? 5   VAL A CG1 1 
ATOM   56   C CG2 . VAL A 1 10 ? 11.583  28.519 -2.614  1.00 39.13  ? 5   VAL A CG2 1 
ATOM   57   N N   . CYS A 1 11 ? 9.500   28.428 -6.880  1.00 46.80  ? 6   CYS A N   1 
ATOM   58   C CA  . CYS A 1 11 ? 9.137   27.720 -8.126  1.00 42.31  ? 6   CYS A CA  1 
ATOM   59   C C   . CYS A 1 11 ? 10.087  26.599 -8.523  1.00 39.58  ? 6   CYS A C   1 
ATOM   60   O O   . CYS A 1 11 ? 11.220  26.867 -8.904  1.00 39.07  ? 6   CYS A O   1 
ATOM   61   C CB  . CYS A 1 11 ? 9.119   28.726 -9.258  1.00 40.58  ? 6   CYS A CB  1 
ATOM   62   S SG  . CYS A 1 11 ? 8.040   30.121 -8.890  1.00 57.09  ? 6   CYS A SG  1 
ATOM   63   N N   . PHE A 1 12 ? 9.647   25.351 -8.417  1.00 39.06  ? 7   PHE A N   1 
ATOM   64   C CA  . PHE A 1 12 ? 10.297  24.274 -9.159  1.00 42.82  ? 7   PHE A CA  1 
ATOM   65   C C   . PHE A 1 12 ? 9.498   24.069 -10.456 1.00 45.64  ? 7   PHE A C   1 
ATOM   66   O O   . PHE A 1 12 ? 8.366   23.548 -10.465 1.00 44.39  ? 7   PHE A O   1 
ATOM   67   C CB  . PHE A 1 12 ? 10.366  22.959 -8.374  1.00 43.61  ? 7   PHE A CB  1 
ATOM   68   C CG  . PHE A 1 12 ? 10.986  23.074 -7.017  1.00 44.83  ? 7   PHE A CG  1 
ATOM   69   C CD1 . PHE A 1 12 ? 10.252  23.572 -5.925  1.00 45.58  ? 7   PHE A CD1 1 
ATOM   70   C CD2 . PHE A 1 12 ? 12.288  22.629 -6.798  1.00 45.83  ? 7   PHE A CD2 1 
ATOM   71   C CE1 . PHE A 1 12 ? 10.831  23.650 -4.651  1.00 45.08  ? 7   PHE A CE1 1 
ATOM   72   C CE2 . PHE A 1 12 ? 12.869  22.713 -5.518  1.00 47.39  ? 7   PHE A CE2 1 
ATOM   73   C CZ  . PHE A 1 12 ? 12.144  23.224 -4.447  1.00 42.90  ? 7   PHE A CZ  1 
ATOM   74   N N   . GLY A 1 13 ? 10.075  24.495 -11.565 1.00 48.93  ? 8   GLY A N   1 
ATOM   75   C CA  . GLY A 1 13 ? 9.310   24.521 -12.795 1.00 51.52  ? 8   GLY A CA  1 
ATOM   76   C C   . GLY A 1 13 ? 8.080   25.358 -12.515 1.00 52.94  ? 8   GLY A C   1 
ATOM   77   O O   . GLY A 1 13 ? 8.174   26.498 -12.009 1.00 48.71  ? 8   GLY A O   1 
ATOM   78   N N   . ARG A 1 14 ? 6.926   24.780 -12.827 1.00 54.31  ? 9   ARG A N   1 
ATOM   79   C CA  . ARG A 1 14 ? 5.634   25.493 -12.776 1.00 59.28  ? 9   ARG A CA  1 
ATOM   80   C C   . ARG A 1 14 ? 4.954   25.291 -11.422 1.00 60.07  ? 9   ARG A C   1 
ATOM   81   O O   . ARG A 1 14 ? 4.032   26.035 -11.055 1.00 62.29  ? 9   ARG A O   1 
ATOM   82   C CB  . ARG A 1 14 ? 4.726   25.021 -13.916 1.00 55.48  ? 9   ARG A CB  1 
ATOM   83   C CG  . ARG A 1 14 ? 4.845   23.526 -14.161 1.00 59.46  ? 9   ARG A CG  1 
ATOM   84   C CD  . ARG A 1 14 ? 6.316   23.141 -14.342 1.00 62.41  ? 9   ARG A CD  1 
ATOM   85   N NE  . ARG A 1 14 ? 6.517   21.701 -14.410 1.00 62.49  ? 9   ARG A NE  1 
ATOM   86   C CZ  . ARG A 1 14 ? 6.409   21.007 -15.533 1.00 63.14  ? 9   ARG A CZ  1 
ATOM   87   N NH1 . ARG A 1 14 ? 6.109   21.626 -16.666 1.00 64.32  ? 9   ARG A NH1 1 
ATOM   88   N NH2 . ARG A 1 14 ? 6.602   19.702 -15.526 1.00 66.92  ? 9   ARG A NH2 1 
ATOM   89   N N   . THR A 1 15 ? 5.427   24.284 -10.692 1.00 55.81  ? 10  THR A N   1 
ATOM   90   C CA  . THR A 1 15 ? 4.940   23.972 -9.354  1.00 56.21  ? 10  THR A CA  1 
ATOM   91   C C   . THR A 1 15 ? 5.623   24.895 -8.343  1.00 52.81  ? 10  THR A C   1 
ATOM   92   O O   . THR A 1 15 ? 6.824   25.113 -8.400  1.00 53.29  ? 10  THR A O   1 
ATOM   93   C CB  . THR A 1 15 ? 5.173   22.486 -9.024  1.00 58.93  ? 10  THR A CB  1 
ATOM   94   O OG1 . THR A 1 15 ? 6.530   22.146 -9.320  1.00 68.19  ? 10  THR A OG1 1 
ATOM   95   C CG2 . THR A 1 15 ? 4.291   21.605 -9.925  1.00 63.00  ? 10  THR A CG2 1 
ATOM   96   N N   . ARG A 1 16 ? 4.840   25.470 -7.444  1.00 50.41  ? 11  ARG A N   1 
ATOM   97   C CA  . ARG A 1 16 ? 5.324   26.545 -6.593  1.00 49.46  ? 11  ARG A CA  1 
ATOM   98   C C   . ARG A 1 16 ? 5.091   26.211 -5.132  1.00 46.70  ? 11  ARG A C   1 
ATOM   99   O O   . ARG A 1 16 ? 4.032   25.719 -4.746  1.00 45.46  ? 11  ARG A O   1 
ATOM   100  C CB  . ARG A 1 16 ? 4.605   27.854 -6.933  1.00 56.73  ? 11  ARG A CB  1 
ATOM   101  C CG  . ARG A 1 16 ? 4.653   28.299 -8.396  1.00 59.62  ? 11  ARG A CG  1 
ATOM   102  C CD  . ARG A 1 16 ? 4.608   29.818 -8.486  1.00 61.87  ? 11  ARG A CD  1 
ATOM   103  N NE  . ARG A 1 16 ? 3.522   30.297 -9.334  1.00 71.50  ? 11  ARG A NE  1 
ATOM   104  C CZ  . ARG A 1 16 ? 3.663   30.973 -10.476 1.00 72.04  ? 11  ARG A CZ  1 
ATOM   105  N NH1 . ARG A 1 16 ? 4.868   31.268 -10.954 1.00 65.59  ? 11  ARG A NH1 1 
ATOM   106  N NH2 . ARG A 1 16 ? 2.574   31.362 -11.139 1.00 74.21  ? 11  ARG A NH2 1 
ATOM   107  N N   . VAL A 1 17 ? 6.062   26.501 -4.291  1.00 46.60  ? 12  VAL A N   1 
ATOM   108  C CA  . VAL A 1 17 ? 5.977   25.964 -2.944  1.00 47.94  ? 12  VAL A CA  1 
ATOM   109  C C   . VAL A 1 17 ? 6.266   26.978 -1.839  1.00 45.72  ? 12  VAL A C   1 
ATOM   110  O O   . VAL A 1 17 ? 7.301   27.642 -1.845  1.00 48.41  ? 12  VAL A O   1 
ATOM   111  C CB  . VAL A 1 17 ? 6.841   24.694 -2.836  1.00 47.32  ? 12  VAL A CB  1 
ATOM   112  C CG1 . VAL A 1 17 ? 8.116   24.969 -2.067  1.00 43.35  ? 12  VAL A CG1 1 
ATOM   113  C CG2 . VAL A 1 17 ? 6.041   23.567 -2.215  1.00 51.04  ? 12  VAL A CG2 1 
ATOM   114  N N   . VAL A 1 18 ? 5.317   27.115 -0.917  1.00 44.94  ? 13  VAL A N   1 
ATOM   115  C CA  . VAL A 1 18 ? 5.445   28.070 0.182   1.00 45.07  ? 13  VAL A CA  1 
ATOM   116  C C   . VAL A 1 18 ? 6.226   27.455 1.312   1.00 43.06  ? 13  VAL A C   1 
ATOM   117  O O   . VAL A 1 18 ? 5.852   26.387 1.835   1.00 44.73  ? 13  VAL A O   1 
ATOM   118  C CB  . VAL A 1 18 ? 4.091   28.529 0.734   1.00 46.13  ? 13  VAL A CB  1 
ATOM   119  C CG1 . VAL A 1 18 ? 4.288   29.530 1.867   1.00 41.36  ? 13  VAL A CG1 1 
ATOM   120  C CG2 . VAL A 1 18 ? 3.254   29.133 -0.388  1.00 48.72  ? 13  VAL A CG2 1 
ATOM   121  N N   . VAL A 1 19 ? 7.307   28.152 1.662   1.00 39.32  ? 14  VAL A N   1 
ATOM   122  C CA  . VAL A 1 19 ? 8.213   27.765 2.721   1.00 36.56  ? 14  VAL A CA  1 
ATOM   123  C C   . VAL A 1 19 ? 8.218   28.841 3.763   1.00 35.41  ? 14  VAL A C   1 
ATOM   124  O O   . VAL A 1 19 ? 8.503   30.015 3.453   1.00 30.51  ? 14  VAL A O   1 
ATOM   125  C CB  . VAL A 1 19 ? 9.690   27.692 2.282   1.00 38.62  ? 14  VAL A CB  1 
ATOM   126  C CG1 . VAL A 1 19 ? 10.484  26.895 3.320   1.00 35.14  ? 14  VAL A CG1 1 
ATOM   127  C CG2 . VAL A 1 19 ? 9.862   27.199 0.830   1.00 33.87  ? 14  VAL A CG2 1 
ATOM   128  N N   . PRO A 1 20 ? 7.947   28.433 5.017   1.00 39.27  ? 15  PRO A N   1 
ATOM   129  C CA  . PRO A 1 20 ? 8.050   29.260 6.232   1.00 38.49  ? 15  PRO A CA  1 
ATOM   130  C C   . PRO A 1 20 ? 9.513   29.400 6.624   1.00 39.05  ? 15  PRO A C   1 
ATOM   131  O O   . PRO A 1 20 ? 10.236  28.395 6.636   1.00 38.36  ? 15  PRO A O   1 
ATOM   132  C CB  . PRO A 1 20 ? 7.319   28.416 7.263   1.00 39.78  ? 15  PRO A CB  1 
ATOM   133  C CG  . PRO A 1 20 ? 7.631   27.004 6.830   1.00 40.09  ? 15  PRO A CG  1 
ATOM   134  C CD  . PRO A 1 20 ? 7.611   27.027 5.335   1.00 38.49  ? 15  PRO A CD  1 
ATOM   135  N N   . CYS A 1 21 ? 9.962   30.617 6.920   1.00 40.40  ? 16  CYS A N   1 
ATOM   136  C CA  . CYS A 1 21 ? 11.382  30.829 7.250   1.00 45.18  ? 16  CYS A CA  1 
ATOM   137  C C   . CYS A 1 21 ? 11.593  31.393 8.651   1.00 45.47  ? 16  CYS A C   1 
ATOM   138  O O   . CYS A 1 21 ? 12.687  31.884 8.974   1.00 40.62  ? 16  CYS A O   1 
ATOM   139  C CB  . CYS A 1 21 ? 12.022  31.737 6.205   1.00 47.10  ? 16  CYS A CB  1 
ATOM   140  S SG  . CYS A 1 21 ? 11.699  31.164 4.519   1.00 58.55  ? 16  CYS A SG  1 
ATOM   141  N N   . GLY A 1 22 ? 10.535  31.263 9.466   1.00 49.00  ? 17  GLY A N   1 
ATOM   142  C CA  . GLY A 1 22 ? 10.344  31.968 10.747  1.00 51.06  ? 17  GLY A CA  1 
ATOM   143  C C   . GLY A 1 22 ? 10.982  33.345 10.811  1.00 53.85  ? 17  GLY A C   1 
ATOM   144  O O   . GLY A 1 22 ? 10.434  34.360 10.323  1.00 52.05  ? 17  GLY A O   1 
ATOM   145  N N   . ASP A 1 23 ? 12.139  33.338 11.461  1.00 54.77  ? 18  ASP A N   1 
ATOM   146  C CA  . ASP A 1 23 ? 13.139  34.403 11.480  1.00 54.09  ? 18  ASP A CA  1 
ATOM   147  C C   . ASP A 1 23 ? 13.381  35.223 10.164  1.00 53.13  ? 18  ASP A C   1 
ATOM   148  O O   . ASP A 1 23 ? 13.226  36.451 10.140  1.00 47.20  ? 18  ASP A O   1 
ATOM   149  C CB  . ASP A 1 23 ? 14.459  33.760 11.951  1.00 49.80  ? 18  ASP A CB  1 
ATOM   150  C CG  . ASP A 1 23 ? 15.228  34.659 12.838  1.00 54.53  ? 18  ASP A CG  1 
ATOM   151  O OD1 . ASP A 1 23 ? 14.733  35.777 13.079  1.00 51.79  ? 18  ASP A OD1 1 
ATOM   152  O OD2 . ASP A 1 23 ? 16.320  34.272 13.305  1.00 62.88  ? 18  ASP A OD2 1 
ATOM   153  N N   . GLY A 1 24 ? 13.789  34.542 9.088   1.00 51.77  ? 19  GLY A N   1 
ATOM   154  C CA  . GLY A 1 24 ? 14.320  35.220 7.895   1.00 47.48  ? 19  GLY A CA  1 
ATOM   155  C C   . GLY A 1 24 ? 15.833  35.199 7.875   1.00 45.16  ? 19  GLY A C   1 
ATOM   156  O O   . GLY A 1 24 ? 16.439  35.519 6.855   1.00 40.61  ? 19  GLY A O   1 
ATOM   157  N N   . ARG A 1 25 ? 16.418  34.786 9.014   1.00 50.95  ? 20  ARG A N   1 
ATOM   158  C CA  . ARG A 1 25 ? 17.886  34.813 9.305   1.00 48.41  ? 20  ARG A CA  1 
ATOM   159  C C   . ARG A 1 25 ? 18.643  33.560 8.805   1.00 48.72  ? 20  ARG A C   1 
ATOM   160  O O   . ARG A 1 25 ? 19.880  33.513 8.783   1.00 46.20  ? 20  ARG A O   1 
ATOM   161  C CB  . ARG A 1 25 ? 18.168  35.084 10.802  1.00 45.66  ? 20  ARG A CB  1 
ATOM   162  C CG  . ARG A 1 25 ? 17.580  36.385 11.383  1.00 45.52  ? 20  ARG A CG  1 
ATOM   163  C CD  . ARG A 1 25 ? 18.315  37.659 11.001  1.00 46.21  ? 20  ARG A CD  1 
ATOM   164  N NE  . ARG A 1 25 ? 19.761  37.452 11.078  1.00 53.43  ? 20  ARG A NE  1 
ATOM   165  C CZ  . ARG A 1 25 ? 20.687  38.166 10.426  1.00 55.36  ? 20  ARG A CZ  1 
ATOM   166  N NH1 . ARG A 1 25 ? 20.339  39.183 9.633   1.00 55.02  ? 20  ARG A NH1 1 
ATOM   167  N NH2 . ARG A 1 25 ? 21.979  37.853 10.561  1.00 53.00  ? 20  ARG A NH2 1 
ATOM   168  N N   . MET A 1 26 ? 17.867  32.567 8.382   1.00 50.52  ? 21  MET A N   1 
ATOM   169  C CA  . MET A 1 26 ? 18.323  31.384 7.634   1.00 49.07  ? 21  MET A CA  1 
ATOM   170  C C   . MET A 1 26 ? 19.158  31.610 6.328   1.00 47.25  ? 21  MET A C   1 
ATOM   171  O O   . MET A 1 26 ? 18.788  32.422 5.464   1.00 45.55  ? 21  MET A O   1 
ATOM   172  C CB  . MET A 1 26 ? 17.060  30.590 7.312   1.00 48.94  ? 21  MET A CB  1 
ATOM   173  C CG  . MET A 1 26 ? 17.156  29.674 6.116   1.00 47.88  ? 21  MET A CG  1 
ATOM   174  S SD  . MET A 1 26 ? 15.546  28.962 5.810   1.00 49.91  ? 21  MET A SD  1 
ATOM   175  C CE  . MET A 1 26 ? 15.068  28.317 7.438   1.00 55.72  ? 21  MET A CE  1 
ATOM   176  N N   . LYS A 1 27 ? 20.260  30.866 6.191   1.00 42.92  ? 22  LYS A N   1 
ATOM   177  C CA  . LYS A 1 27 ? 21.107  30.864 4.979   1.00 44.28  ? 22  LYS A CA  1 
ATOM   178  C C   . LYS A 1 27 ? 20.471  30.248 3.711   1.00 43.13  ? 22  LYS A C   1 
ATOM   179  O O   . LYS A 1 27 ? 19.726  29.266 3.779   1.00 42.73  ? 22  LYS A O   1 
ATOM   180  C CB  . LYS A 1 27 ? 22.447  30.178 5.274   1.00 47.37  ? 22  LYS A CB  1 
ATOM   181  C CG  . LYS A 1 27 ? 23.429  31.086 6.006   1.00 53.39  ? 22  LYS A CG  1 
ATOM   182  C CD  . LYS A 1 27 ? 24.659  30.346 6.514   1.00 60.84  ? 22  LYS A CD  1 
ATOM   183  C CE  . LYS A 1 27 ? 25.730  31.313 7.025   1.00 65.61  ? 22  LYS A CE  1 
ATOM   184  N NZ  . LYS A 1 27 ? 26.659  30.674 8.007   1.00 66.56  ? 22  LYS A NZ  1 
ATOM   185  N N   . VAL A 1 28 ? 20.781  30.805 2.544   1.00 41.18  ? 23  VAL A N   1 
ATOM   186  C CA  . VAL A 1 28 ? 20.228  30.256 1.295   1.00 43.12  ? 23  VAL A CA  1 
ATOM   187  C C   . VAL A 1 28 ? 20.258  28.697 1.216   1.00 45.33  ? 23  VAL A C   1 
ATOM   188  O O   . VAL A 1 28 ? 19.225  28.082 0.947   1.00 44.79  ? 23  VAL A O   1 
ATOM   189  C CB  . VAL A 1 28 ? 20.840  30.923 0.040   1.00 41.37  ? 23  VAL A CB  1 
ATOM   190  C CG1 . VAL A 1 28 ? 20.453  30.166 -1.221  1.00 43.80  ? 23  VAL A CG1 1 
ATOM   191  C CG2 . VAL A 1 28 ? 20.387  32.366 -0.061  1.00 40.78  ? 23  VAL A CG2 1 
ATOM   192  N N   . PHE A 1 29 ? 21.405  28.059 1.482   1.00 47.58  ? 24  PHE A N   1 
ATOM   193  C CA  . PHE A 1 29 ? 21.460  26.583 1.490   1.00 47.67  ? 24  PHE A CA  1 
ATOM   194  C C   . PHE A 1 29 ? 20.418  25.925 2.420   1.00 44.97  ? 24  PHE A C   1 
ATOM   195  O O   . PHE A 1 29 ? 19.804  24.942 2.024   1.00 46.17  ? 24  PHE A O   1 
ATOM   196  C CB  . PHE A 1 29 ? 22.879  26.020 1.703   1.00 50.89  ? 24  PHE A CB  1 
ATOM   197  C CG  . PHE A 1 29 ? 23.204  25.667 3.148   1.00 65.84  ? 24  PHE A CG  1 
ATOM   198  C CD1 . PHE A 1 29 ? 23.479  26.680 4.113   1.00 70.89  ? 24  PHE A CD1 1 
ATOM   199  C CD2 . PHE A 1 29 ? 23.270  24.324 3.564   1.00 68.33  ? 24  PHE A CD2 1 
ATOM   200  C CE1 . PHE A 1 29 ? 23.808  26.356 5.436   1.00 64.09  ? 24  PHE A CE1 1 
ATOM   201  C CE2 . PHE A 1 29 ? 23.594  24.002 4.897   1.00 66.05  ? 24  PHE A CE2 1 
ATOM   202  C CZ  . PHE A 1 29 ? 23.862  25.014 5.824   1.00 63.95  ? 24  PHE A CZ  1 
ATOM   203  N N   . SER A 1 30 ? 20.180  26.456 3.621   1.00 42.23  ? 25  SER A N   1 
ATOM   204  C CA  . SER A 1 30 ? 19.080  25.908 4.454   1.00 43.34  ? 25  SER A CA  1 
ATOM   205  C C   . SER A 1 30 ? 17.734  25.980 3.736   1.00 41.75  ? 25  SER A C   1 
ATOM   206  O O   . SER A 1 30 ? 17.000  24.985 3.606   1.00 38.89  ? 25  SER A O   1 
ATOM   207  C CB  . SER A 1 30 ? 18.965  26.618 5.795   1.00 43.30  ? 25  SER A CB  1 
ATOM   208  O OG  . SER A 1 30 ? 19.962  26.152 6.675   1.00 48.61  ? 25  SER A OG  1 
ATOM   209  N N   . LEU A 1 31 ? 17.431  27.174 3.249   1.00 42.76  ? 26  LEU A N   1 
ATOM   210  C CA  . LEU A 1 31 ? 16.239  27.387 2.468   1.00 41.89  ? 26  LEU A CA  1 
ATOM   211  C C   . LEU A 1 31 ? 16.102  26.331 1.398   1.00 41.69  ? 26  LEU A C   1 
ATOM   212  O O   . LEU A 1 31 ? 15.026  25.748 1.247   1.00 42.54  ? 26  LEU A O   1 
ATOM   213  C CB  . LEU A 1 31 ? 16.270  28.764 1.820   1.00 43.05  ? 26  LEU A CB  1 
ATOM   214  C CG  . LEU A 1 31 ? 15.081  29.044 0.896   1.00 45.94  ? 26  LEU A CG  1 
ATOM   215  C CD1 . LEU A 1 31 ? 13.787  28.912 1.688   1.00 43.75  ? 26  LEU A CD1 1 
ATOM   216  C CD2 . LEU A 1 31 ? 15.194  30.398 0.189   1.00 43.00  ? 26  LEU A CD2 1 
ATOM   217  N N   . ILE A 1 32 ? 17.189  26.086 0.665   1.00 39.33  ? 27  ILE A N   1 
ATOM   218  C CA  . ILE A 1 32 ? 17.123  25.222 -0.502  1.00 40.20  ? 27  ILE A CA  1 
ATOM   219  C C   . ILE A 1 32 ? 16.579  23.840 -0.147  1.00 42.83  ? 27  ILE A C   1 
ATOM   220  O O   . ILE A 1 32 ? 15.694  23.303 -0.842  1.00 45.58  ? 27  ILE A O   1 
ATOM   221  C CB  . ILE A 1 32 ? 18.476  25.091 -1.204  1.00 39.30  ? 27  ILE A CB  1 
ATOM   222  C CG1 . ILE A 1 32 ? 19.010  26.467 -1.569  1.00 41.42  ? 27  ILE A CG1 1 
ATOM   223  C CG2 . ILE A 1 32 ? 18.325  24.258 -2.463  1.00 39.47  ? 27  ILE A CG2 1 
ATOM   224  C CD1 . ILE A 1 32 ? 20.269  26.433 -2.397  1.00 39.94  ? 27  ILE A CD1 1 
ATOM   225  N N   . GLN A 1 33 ? 17.098  23.280 0.943   1.00 40.65  ? 28  GLN A N   1 
ATOM   226  C CA  . GLN A 1 33 ? 16.678  21.980 1.418   1.00 39.11  ? 28  GLN A CA  1 
ATOM   227  C C   . GLN A 1 33 ? 15.211  22.017 1.781   1.00 40.08  ? 28  GLN A C   1 
ATOM   228  O O   . GLN A 1 33 ? 14.449  21.160 1.346   1.00 39.82  ? 28  GLN A O   1 
ATOM   229  C CB  . GLN A 1 33 ? 17.502  21.590 2.629   1.00 42.04  ? 28  GLN A CB  1 
ATOM   230  C CG  . GLN A 1 33 ? 18.999  21.620 2.378   1.00 40.17  ? 28  GLN A CG  1 
ATOM   231  C CD  . GLN A 1 33 ? 19.788  21.186 3.581   1.00 40.65  ? 28  GLN A CD  1 
ATOM   232  O OE1 . GLN A 1 33 ? 20.583  21.954 4.096   1.00 44.15  ? 28  GLN A OE1 1 
ATOM   233  N NE2 . GLN A 1 33 ? 19.560  19.956 4.050   1.00 40.80  ? 28  GLN A NE2 1 
ATOM   234  N N   . GLN A 1 34 ? 14.820  23.037 2.546   1.00 40.30  ? 29  GLN A N   1 
ATOM   235  C CA  . GLN A 1 34 ? 13.439  23.196 2.991   1.00 41.32  ? 29  GLN A CA  1 
ATOM   236  C C   . GLN A 1 34 ? 12.471  23.243 1.834   1.00 42.69  ? 29  GLN A C   1 
ATOM   237  O O   . GLN A 1 34 ? 11.315  22.825 1.953   1.00 45.68  ? 29  GLN A O   1 
ATOM   238  C CB  . GLN A 1 34 ? 13.282  24.503 3.727   1.00 41.76  ? 29  GLN A CB  1 
ATOM   239  C CG  . GLN A 1 34 ? 14.164  24.659 4.922   1.00 45.89  ? 29  GLN A CG  1 
ATOM   240  C CD  . GLN A 1 34 ? 13.585  23.986 6.128   1.00 49.24  ? 29  GLN A CD  1 
ATOM   241  O OE1 . GLN A 1 34 ? 12.695  23.113 6.013   1.00 48.76  ? 29  GLN A OE1 1 
ATOM   242  N NE2 . GLN A 1 34 ? 14.093  24.371 7.307   1.00 48.73  ? 29  GLN A NE2 1 
ATOM   243  N N   . ALA A 1 35 ? 12.930  23.819 0.729   1.00 40.70  ? 30  ALA A N   1 
ATOM   244  C CA  . ALA A 1 35 ? 12.104  23.952 -0.430  1.00 38.88  ? 30  ALA A CA  1 
ATOM   245  C C   . ALA A 1 35 ? 11.956  22.559 -1.030  1.00 42.51  ? 30  ALA A C   1 
ATOM   246  O O   . ALA A 1 35 ? 10.854  22.155 -1.443  1.00 46.95  ? 30  ALA A O   1 
ATOM   247  C CB  . ALA A 1 35 ? 12.742  24.906 -1.411  1.00 36.63  ? 30  ALA A CB  1 
ATOM   248  N N   . VAL A 1 36 ? 13.048  21.803 -1.050  1.00 38.81  ? 31  VAL A N   1 
ATOM   249  C CA  . VAL A 1 36 ? 13.009  20.517 -1.708  1.00 38.68  ? 31  VAL A CA  1 
ATOM   250  C C   . VAL A 1 36 ? 12.042  19.591 -0.991  1.00 42.66  ? 31  VAL A C   1 
ATOM   251  O O   . VAL A 1 36 ? 11.202  18.972 -1.641  1.00 46.17  ? 31  VAL A O   1 
ATOM   252  C CB  . VAL A 1 36 ? 14.404  19.907 -1.835  1.00 37.39  ? 31  VAL A CB  1 
ATOM   253  C CG1 . VAL A 1 36 ? 14.322  18.414 -2.095  1.00 34.46  ? 31  VAL A CG1 1 
ATOM   254  C CG2 . VAL A 1 36 ? 15.176  20.634 -2.933  1.00 38.56  ? 31  VAL A CG2 1 
ATOM   255  N N   . THR A 1 37 ? 12.138  19.539 0.344   1.00 45.68  ? 32  THR A N   1 
ATOM   256  C CA  . THR A 1 37 ? 11.330  18.650 1.187   1.00 41.89  ? 32  THR A CA  1 
ATOM   257  C C   . THR A 1 37 ? 9.885   18.753 0.778   1.00 39.27  ? 32  THR A C   1 
ATOM   258  O O   . THR A 1 37 ? 9.217   17.742 0.602   1.00 39.38  ? 32  THR A O   1 
ATOM   259  C CB  . THR A 1 37 ? 11.410  19.025 2.688   1.00 46.39  ? 32  THR A CB  1 
ATOM   260  O OG1 . THR A 1 37 ? 12.599  19.768 2.965   1.00 55.38  ? 32  THR A OG1 1 
ATOM   261  C CG2 . THR A 1 37 ? 11.428  17.797 3.550   1.00 51.10  ? 32  THR A CG2 1 
ATOM   262  N N   . ARG A 1 38 ? 9.436   19.995 0.597   1.00 38.91  ? 33  ARG A N   1 
ATOM   263  C CA  . ARG A 1 38 ? 8.020   20.349 0.396   1.00 42.19  ? 33  ARG A CA  1 
ATOM   264  C C   . ARG A 1 38 ? 7.542   20.051 -1.011  1.00 41.95  ? 33  ARG A C   1 
ATOM   265  O O   . ARG A 1 38 ? 6.456   19.484 -1.214  1.00 37.55  ? 33  ARG A O   1 
ATOM   266  C CB  . ARG A 1 38 ? 7.798   21.837 0.730   1.00 43.36  ? 33  ARG A CB  1 
ATOM   267  C CG  . ARG A 1 38 ? 8.163   22.162 2.171   1.00 44.09  ? 33  ARG A CG  1 
ATOM   268  C CD  . ARG A 1 38 ? 7.699   23.528 2.617   1.00 45.96  ? 33  ARG A CD  1 
ATOM   269  N NE  . ARG A 1 38 ? 7.636   23.621 4.076   1.00 47.55  ? 33  ARG A NE  1 
ATOM   270  C CZ  . ARG A 1 38 ? 8.688   23.637 4.894   1.00 46.01  ? 33  ARG A CZ  1 
ATOM   271  N NH1 . ARG A 1 38 ? 9.924   23.559 4.405   1.00 48.13  ? 33  ARG A NH1 1 
ATOM   272  N NH2 . ARG A 1 38 ? 8.500   23.722 6.211   1.00 42.50  ? 33  ARG A NH2 1 
ATOM   273  N N   . TYR A 1 39 ? 8.368   20.476 -1.963  1.00 43.25  ? 34  TYR A N   1 
ATOM   274  C CA  . TYR A 1 39 ? 8.288   20.047 -3.331  1.00 45.00  ? 34  TYR A CA  1 
ATOM   275  C C   . TYR A 1 39 ? 8.168   18.524 -3.469  1.00 49.02  ? 34  TYR A C   1 
ATOM   276  O O   . TYR A 1 39 ? 7.242   18.029 -4.120  1.00 48.18  ? 34  TYR A O   1 
ATOM   277  C CB  . TYR A 1 39 ? 9.514   20.519 -4.069  1.00 45.02  ? 34  TYR A CB  1 
ATOM   278  C CG  . TYR A 1 39 ? 9.487   20.067 -5.491  1.00 50.96  ? 34  TYR A CG  1 
ATOM   279  C CD1 . TYR A 1 39 ? 8.453   20.461 -6.345  1.00 52.06  ? 34  TYR A CD1 1 
ATOM   280  C CD2 . TYR A 1 39 ? 10.475  19.219 -5.996  1.00 53.25  ? 34  TYR A CD2 1 
ATOM   281  C CE1 . TYR A 1 39 ? 8.418   20.033 -7.664  1.00 53.33  ? 34  TYR A CE1 1 
ATOM   282  C CE2 . TYR A 1 39 ? 10.446  18.793 -7.319  1.00 50.50  ? 34  TYR A CE2 1 
ATOM   283  C CZ  . TYR A 1 39 ? 9.416   19.201 -8.137  1.00 50.77  ? 34  TYR A CZ  1 
ATOM   284  O OH  . TYR A 1 39 ? 9.377   18.788 -9.430  1.00 51.75  ? 34  TYR A OH  1 
ATOM   285  N N   . ARG A 1 40 ? 9.109   17.789 -2.869  1.00 55.04  ? 35  ARG A N   1 
ATOM   286  C CA  . ARG A 1 40 ? 9.013   16.322 -2.775  1.00 58.92  ? 35  ARG A CA  1 
ATOM   287  C C   . ARG A 1 40 ? 7.584   15.883 -2.399  1.00 58.71  ? 35  ARG A C   1 
ATOM   288  O O   . ARG A 1 40 ? 6.970   15.051 -3.096  1.00 63.92  ? 35  ARG A O   1 
ATOM   289  C CB  . ARG A 1 40 ? 10.046  15.722 -1.790  1.00 60.68  ? 35  ARG A CB  1 
ATOM   290  C CG  . ARG A 1 40 ? 11.487  15.654 -2.295  1.00 66.36  ? 35  ARG A CG  1 
ATOM   291  C CD  . ARG A 1 40 ? 12.227  14.419 -1.792  1.00 70.32  ? 35  ARG A CD  1 
ATOM   292  N NE  . ARG A 1 40 ? 12.058  13.294 -2.720  1.00 87.95  ? 35  ARG A NE  1 
ATOM   293  C CZ  . ARG A 1 40 ? 12.895  12.252 -2.847  1.00 104.44 ? 35  ARG A CZ  1 
ATOM   294  N NH1 . ARG A 1 40 ? 13.997  12.164 -2.093  1.00 108.24 ? 35  ARG A NH1 1 
ATOM   295  N NH2 . ARG A 1 40 ? 12.632  11.287 -3.736  1.00 93.52  ? 35  ARG A NH2 1 
ATOM   296  N N   . LYS A 1 41 ? 7.051   16.464 -1.324  1.00 52.88  ? 36  LYS A N   1 
ATOM   297  C CA  . LYS A 1 41 ? 5.723   16.102 -0.842  1.00 52.41  ? 36  LYS A CA  1 
ATOM   298  C C   . LYS A 1 41 ? 4.628   16.451 -1.852  1.00 56.44  ? 36  LYS A C   1 
ATOM   299  O O   . LYS A 1 41 ? 3.601   15.768 -1.948  1.00 54.67  ? 36  LYS A O   1 
ATOM   300  C CB  . LYS A 1 41 ? 5.423   16.795 0.473   1.00 48.62  ? 36  LYS A CB  1 
ATOM   301  C CG  . LYS A 1 41 ? 6.344   16.422 1.613   1.00 49.00  ? 36  LYS A CG  1 
ATOM   302  C CD  . LYS A 1 41 ? 5.581   16.622 2.900   1.00 52.62  ? 36  LYS A CD  1 
ATOM   303  C CE  . LYS A 1 41 ? 6.469   17.017 4.065   1.00 58.19  ? 36  LYS A CE  1 
ATOM   304  N NZ  . LYS A 1 41 ? 5.609   17.324 5.259   1.00 57.28  ? 36  LYS A NZ  1 
ATOM   305  N N   . ALA A 1 42 ? 4.847   17.509 -2.619  1.00 56.79  ? 37  ALA A N   1 
ATOM   306  C CA  . ALA A 1 42 ? 3.795   18.006 -3.479  1.00 55.06  ? 37  ALA A CA  1 
ATOM   307  C C   . ALA A 1 42 ? 3.734   17.254 -4.782  1.00 57.31  ? 37  ALA A C   1 
ATOM   308  O O   . ALA A 1 42 ? 2.788   17.416 -5.533  1.00 61.30  ? 37  ALA A O   1 
ATOM   309  C CB  . ALA A 1 42 ? 3.969   19.498 -3.735  1.00 52.19  ? 37  ALA A CB  1 
ATOM   310  N N   . VAL A 1 43 ? 4.717   16.426 -5.080  1.00 59.65  ? 38  VAL A N   1 
ATOM   311  C CA  . VAL A 1 43 ? 4.834   16.079 -6.476  1.00 66.89  ? 38  VAL A CA  1 
ATOM   312  C C   . VAL A 1 43 ? 4.870   14.597 -6.823  1.00 72.87  ? 38  VAL A C   1 
ATOM   313  O O   . VAL A 1 43 ? 4.489   14.239 -7.936  1.00 73.73  ? 38  VAL A O   1 
ATOM   314  C CB  . VAL A 1 43 ? 5.953   16.904 -7.152  1.00 70.81  ? 38  VAL A CB  1 
ATOM   315  C CG1 . VAL A 1 43 ? 7.289   16.168 -7.090  1.00 73.66  ? 38  VAL A CG1 1 
ATOM   316  C CG2 . VAL A 1 43 ? 5.558   17.321 -8.570  1.00 63.56  ? 38  VAL A CG2 1 
ATOM   317  N N   . ALA A 1 44 ? 5.323   13.744 -5.902  1.00 81.25  ? 39  ALA A N   1 
ATOM   318  C CA  . ALA A 1 44 ? 5.102   12.272 -6.014  1.00 94.72  ? 39  ALA A CA  1 
ATOM   319  C C   . ALA A 1 44 ? 5.723   11.486 -7.224  1.00 95.90  ? 39  ALA A C   1 
ATOM   320  O O   . ALA A 1 44 ? 5.688   11.943 -8.372  1.00 89.63  ? 39  ALA A O   1 
ATOM   321  C CB  . ALA A 1 44 ? 3.600   11.947 -5.877  1.00 90.07  ? 39  ALA A CB  1 
ATOM   322  N N   . LYS A 1 45 ? 6.260   10.287 -6.985  1.00 94.48  ? 40  LYS A N   1 
ATOM   323  C CA  . LYS A 1 45 ? 6.359   9.625  -5.671  1.00 99.39  ? 40  LYS A CA  1 
ATOM   324  C C   . LYS A 1 45 ? 7.271   8.428  -5.918  1.00 100.92 ? 40  LYS A C   1 
ATOM   325  O O   . LYS A 1 45 ? 7.458   7.575  -5.037  1.00 102.77 ? 40  LYS A O   1 
ATOM   326  C CB  . LYS A 1 45 ? 4.968   9.182  -5.130  1.00 88.54  ? 40  LYS A CB  1 
ATOM   327  C CG  . LYS A 1 45 ? 4.778   9.024  -3.603  1.00 82.50  ? 40  LYS A CG  1 
ATOM   328  C CD  . LYS A 1 45 ? 5.881   9.544  -2.667  1.00 79.55  ? 40  LYS A CD  1 
ATOM   329  C CE  . LYS A 1 45 ? 6.212   11.039 -2.782  1.00 82.92  ? 40  LYS A CE  1 
ATOM   330  N NZ  . LYS A 1 45 ? 5.069   11.984 -2.617  1.00 73.26  ? 40  LYS A NZ  1 
ATOM   331  N N   . ASP A 1 46 ? 7.853   8.421  -7.126  1.00 97.26  ? 41  ASP A N   1 
ATOM   332  C CA  . ASP A 1 46 ? 8.590   7.287  -7.713  1.00 100.31 ? 41  ASP A CA  1 
ATOM   333  C C   . ASP A 1 46 ? 9.718   6.705  -6.821  1.00 106.06 ? 41  ASP A C   1 
ATOM   334  O O   . ASP A 1 46 ? 10.468  7.469  -6.198  1.00 104.04 ? 41  ASP A O   1 
ATOM   335  C CB  . ASP A 1 46 ? 9.151   7.703  -9.078  1.00 93.93  ? 41  ASP A CB  1 
ATOM   336  C CG  . ASP A 1 46 ? 9.678   6.530  -9.861  1.00 92.21  ? 41  ASP A CG  1 
ATOM   337  O OD1 . ASP A 1 46 ? 8.862   5.863  -10.525 1.00 92.24  ? 41  ASP A OD1 1 
ATOM   338  O OD2 . ASP A 1 46 ? 10.902  6.262  -9.797  1.00 85.18  ? 41  ASP A OD2 1 
ATOM   339  N N   . PRO A 1 47 ? 9.850   5.352  -6.770  1.00 106.91 ? 42  PRO A N   1 
ATOM   340  C CA  . PRO A 1 47 ? 10.788  4.681  -5.839  1.00 103.40 ? 42  PRO A CA  1 
ATOM   341  C C   . PRO A 1 47 ? 12.263  5.153  -5.891  1.00 93.95  ? 42  PRO A C   1 
ATOM   342  O O   . PRO A 1 47 ? 12.939  5.177  -4.856  1.00 79.28  ? 42  PRO A O   1 
ATOM   343  C CB  . PRO A 1 47 ? 10.677  3.195  -6.238  1.00 107.19 ? 42  PRO A CB  1 
ATOM   344  C CG  . PRO A 1 47 ? 10.099  3.201  -7.621  1.00 105.28 ? 42  PRO A CG  1 
ATOM   345  C CD  . PRO A 1 47 ? 9.144   4.362  -7.607  1.00 104.89 ? 42  PRO A CD  1 
ATOM   346  N N   . ASN A 1 48 ? 12.753  5.517  -7.077  1.00 88.06  ? 43  ASN A N   1 
ATOM   347  C CA  . ASN A 1 48 ? 14.141  5.987  -7.216  1.00 88.71  ? 43  ASN A CA  1 
ATOM   348  C C   . ASN A 1 48 ? 14.300  7.488  -7.539  1.00 88.78  ? 43  ASN A C   1 
ATOM   349  O O   . ASN A 1 48 ? 15.332  7.912  -8.080  1.00 81.70  ? 43  ASN A O   1 
ATOM   350  C CB  . ASN A 1 48 ? 14.990  5.076  -8.155  1.00 87.80  ? 43  ASN A CB  1 
ATOM   351  C CG  . ASN A 1 48 ? 14.563  5.122  -9.628  1.00 84.50  ? 43  ASN A CG  1 
ATOM   352  O OD1 . ASN A 1 48 ? 13.468  4.668  -9.994  1.00 81.88  ? 43  ASN A OD1 1 
ATOM   353  N ND2 . ASN A 1 48 ? 15.458  5.623  -10.488 1.00 72.57  ? 43  ASN A ND2 1 
ATOM   354  N N   . TYR A 1 49 ? 13.282  8.278  -7.181  1.00 86.39  ? 44  TYR A N   1 
ATOM   355  C CA  . TYR A 1 49 ? 13.281  9.722  -7.423  1.00 83.73  ? 44  TYR A CA  1 
ATOM   356  C C   . TYR A 1 49 ? 14.545  10.371 -6.898  1.00 82.63  ? 44  TYR A C   1 
ATOM   357  O O   . TYR A 1 49 ? 15.194  9.839  -6.002  1.00 90.16  ? 44  TYR A O   1 
ATOM   358  C CB  . TYR A 1 49 ? 12.079  10.395 -6.754  1.00 90.49  ? 44  TYR A CB  1 
ATOM   359  C CG  . TYR A 1 49 ? 11.886  11.823 -7.210  1.00 94.74  ? 44  TYR A CG  1 
ATOM   360  C CD1 . TYR A 1 49 ? 12.548  12.872 -6.572  1.00 89.35  ? 44  TYR A CD1 1 
ATOM   361  C CD2 . TYR A 1 49 ? 11.056  12.123 -8.301  1.00 94.90  ? 44  TYR A CD2 1 
ATOM   362  C CE1 . TYR A 1 49 ? 12.398  14.176 -7.006  1.00 90.88  ? 44  TYR A CE1 1 
ATOM   363  C CE2 . TYR A 1 49 ? 10.887  13.428 -8.730  1.00 90.41  ? 44  TYR A CE2 1 
ATOM   364  C CZ  . TYR A 1 49 ? 11.564  14.450 -8.080  1.00 89.12  ? 44  TYR A CZ  1 
ATOM   365  O OH  . TYR A 1 49 ? 11.417  15.752 -8.498  1.00 84.89  ? 44  TYR A OH  1 
ATOM   366  N N   . TRP A 1 50 ? 14.887  11.522 -7.463  1.00 79.20  ? 45  TRP A N   1 
ATOM   367  C CA  . TRP A 1 50 ? 15.990  12.329 -6.973  1.00 72.73  ? 45  TRP A CA  1 
ATOM   368  C C   . TRP A 1 50 ? 15.860  13.719 -7.466  1.00 71.68  ? 45  TRP A C   1 
ATOM   369  O O   . TRP A 1 50 ? 15.401  13.951 -8.586  1.00 70.55  ? 45  TRP A O   1 
ATOM   370  C CB  . TRP A 1 50 ? 17.320  11.768 -7.440  1.00 73.76  ? 45  TRP A CB  1 
ATOM   371  C CG  . TRP A 1 50 ? 17.468  11.620 -8.936  1.00 72.60  ? 45  TRP A CG  1 
ATOM   372  C CD1 . TRP A 1 50 ? 17.111  10.525 -9.721  1.00 73.17  ? 45  TRP A CD1 1 
ATOM   373  C CD2 . TRP A 1 50 ? 18.051  12.585 -9.873  1.00 71.50  ? 45  TRP A CD2 1 
ATOM   374  N NE1 . TRP A 1 50 ? 17.416  10.741 -11.039 1.00 76.57  ? 45  TRP A NE1 1 
ATOM   375  C CE2 . TRP A 1 50 ? 17.990  11.955 -11.202 1.00 77.08  ? 45  TRP A CE2 1 
ATOM   376  C CE3 . TRP A 1 50 ? 18.593  13.853 -9.755  1.00 67.73  ? 45  TRP A CE3 1 
ATOM   377  C CZ2 . TRP A 1 50 ? 18.459  12.594 -12.344 1.00 78.18  ? 45  TRP A CZ2 1 
ATOM   378  C CZ3 . TRP A 1 50 ? 19.066  14.487 -10.910 1.00 72.73  ? 45  TRP A CZ3 1 
ATOM   379  C CH2 . TRP A 1 50 ? 18.997  13.873 -12.175 1.00 78.57  ? 45  TRP A CH2 1 
ATOM   380  N N   . ILE A 1 51 ? 16.286  14.666 -6.643  1.00 66.89  ? 46  ILE A N   1 
ATOM   381  C CA  . ILE A 1 51 ? 16.294  16.052 -7.080  1.00 63.35  ? 46  ILE A CA  1 
ATOM   382  C C   . ILE A 1 51 ? 17.628  16.765 -6.782  1.00 59.31  ? 46  ILE A C   1 
ATOM   383  O O   . ILE A 1 51 ? 18.166  16.675 -5.680  1.00 55.22  ? 46  ILE A O   1 
ATOM   384  C CB  . ILE A 1 51 ? 15.026  16.785 -6.581  1.00 60.24  ? 46  ILE A CB  1 
ATOM   385  C CG1 . ILE A 1 51 ? 15.123  18.280 -6.813  1.00 55.54  ? 46  ILE A CG1 1 
ATOM   386  C CG2 . ILE A 1 51 ? 14.751  16.450 -5.125  1.00 58.10  ? 46  ILE A CG2 1 
ATOM   387  C CD1 . ILE A 1 51 ? 13.776  18.900 -7.045  1.00 59.37  ? 46  ILE A CD1 1 
ATOM   388  N N   . GLN A 1 52 ? 18.176  17.437 -7.793  1.00 60.12  ? 47  GLN A N   1 
ATOM   389  C CA  . GLN A 1 52 ? 19.413  18.195 -7.615  1.00 62.46  ? 47  GLN A CA  1 
ATOM   390  C C   . GLN A 1 52 ? 19.207  19.669 -7.894  1.00 59.73  ? 47  GLN A C   1 
ATOM   391  O O   . GLN A 1 52 ? 18.894  20.070 -9.009  1.00 60.43  ? 47  GLN A O   1 
ATOM   392  C CB  . GLN A 1 52 ? 20.563  17.623 -8.456  1.00 65.77  ? 47  GLN A CB  1 
ATOM   393  C CG  . GLN A 1 52 ? 21.295  16.455 -7.789  1.00 71.36  ? 47  GLN A CG  1 
ATOM   394  C CD  . GLN A 1 52 ? 22.112  16.864 -6.557  1.00 76.56  ? 47  GLN A CD  1 
ATOM   395  O OE1 . GLN A 1 52 ? 21.928  16.315 -5.451  1.00 68.28  ? 47  GLN A OE1 1 
ATOM   396  N NE2 . GLN A 1 52 ? 23.024  17.831 -6.744  1.00 76.26  ? 47  GLN A NE2 1 
ATOM   397  N N   . VAL A 1 53 ? 19.368  20.473 -6.859  1.00 54.50  ? 48  VAL A N   1 
ATOM   398  C CA  . VAL A 1 53 ? 19.244  21.909 -7.013  1.00 53.73  ? 48  VAL A CA  1 
ATOM   399  C C   . VAL A 1 53 ? 20.602  22.511 -7.311  1.00 51.28  ? 48  VAL A C   1 
ATOM   400  O O   . VAL A 1 53 ? 21.589  22.241 -6.622  1.00 51.81  ? 48  VAL A O   1 
ATOM   401  C CB  . VAL A 1 53 ? 18.624  22.554 -5.768  1.00 50.26  ? 48  VAL A CB  1 
ATOM   402  C CG1 . VAL A 1 53 ? 18.874  24.039 -5.729  1.00 48.54  ? 48  VAL A CG1 1 
ATOM   403  C CG2 . VAL A 1 53 ? 17.141  22.288 -5.761  1.00 52.95  ? 48  VAL A CG2 1 
ATOM   404  N N   . HIS A 1 54 ? 20.640  23.327 -8.352  1.00 49.05  ? 49  HIS A N   1 
ATOM   405  C CA  . HIS A 1 54 ? 21.869  23.985 -8.740  1.00 50.56  ? 49  HIS A CA  1 
ATOM   406  C C   . HIS A 1 54 ? 21.954  25.337 -8.128  1.00 48.83  ? 49  HIS A C   1 
ATOM   407  O O   . HIS A 1 54 ? 22.927  25.631 -7.441  1.00 51.08  ? 49  HIS A O   1 
ATOM   408  C CB  . HIS A 1 54 ? 22.010  24.011 -10.265 1.00 56.46  ? 49  HIS A CB  1 
ATOM   409  C CG  . HIS A 1 54 ? 21.966  22.638 -10.876 1.00 60.53  ? 49  HIS A CG  1 
ATOM   410  N ND1 . HIS A 1 54 ? 22.862  21.672 -10.550 1.00 58.48  ? 49  HIS A ND1 1 
ATOM   411  C CD2 . HIS A 1 54 ? 21.060  22.060 -11.762 1.00 61.68  ? 49  HIS A CD2 1 
ATOM   412  C CE1 . HIS A 1 54 ? 22.550  20.542 -11.205 1.00 59.77  ? 49  HIS A CE1 1 
ATOM   413  N NE2 . HIS A 1 54 ? 21.451  20.781 -11.954 1.00 63.30  ? 49  HIS A NE2 1 
ATOM   414  N N   . ARG A 1 55 ? 20.923  26.155 -8.340  1.00 49.99  ? 50  ARG A N   1 
ATOM   415  C CA  . ARG A 1 55 ? 20.822  27.461 -7.700  1.00 49.87  ? 50  ARG A CA  1 
ATOM   416  C C   . ARG A 1 55 ? 19.379  27.976 -7.563  1.00 55.61  ? 50  ARG A C   1 
ATOM   417  O O   . ARG A 1 55 ? 18.481  27.539 -8.319  1.00 57.66  ? 50  ARG A O   1 
ATOM   418  C CB  . ARG A 1 55 ? 21.681  28.473 -8.449  1.00 48.14  ? 50  ARG A CB  1 
ATOM   419  C CG  . ARG A 1 55 ? 21.299  28.696 -9.886  1.00 43.97  ? 50  ARG A CG  1 
ATOM   420  C CD  . ARG A 1 55 ? 22.462  29.350 -10.593 1.00 45.53  ? 50  ARG A CD  1 
ATOM   421  N NE  . ARG A 1 55 ? 22.037  29.824 -11.907 1.00 51.45  ? 50  ARG A NE  1 
ATOM   422  C CZ  . ARG A 1 55 ? 21.928  29.051 -12.992 1.00 50.43  ? 50  ARG A CZ  1 
ATOM   423  N NH1 . ARG A 1 55 ? 22.204  27.745 -12.947 1.00 42.79  ? 50  ARG A NH1 1 
ATOM   424  N NH2 . ARG A 1 55 ? 21.513  29.591 -14.132 1.00 55.83  ? 50  ARG A NH2 1 
ATOM   425  N N   . LEU A 1 56 ? 19.180  28.874 -6.578  1.00 49.51  ? 51  LEU A N   1 
ATOM   426  C CA  . LEU A 1 56 ? 17.997  29.728 -6.445  1.00 45.30  ? 51  LEU A CA  1 
ATOM   427  C C   . LEU A 1 56 ? 18.223  31.092 -7.090  1.00 46.12  ? 51  LEU A C   1 
ATOM   428  O O   . LEU A 1 56 ? 19.338  31.607 -7.104  1.00 47.69  ? 51  LEU A O   1 
ATOM   429  C CB  . LEU A 1 56 ? 17.673  29.959 -4.975  1.00 48.22  ? 51  LEU A CB  1 
ATOM   430  C CG  . LEU A 1 56 ? 16.569  29.190 -4.253  1.00 47.52  ? 51  LEU A CG  1 
ATOM   431  C CD1 . LEU A 1 56 ? 16.949  27.727 -4.180  1.00 51.94  ? 51  LEU A CD1 1 
ATOM   432  C CD2 . LEU A 1 56 ? 16.400  29.734 -2.850  1.00 43.87  ? 51  LEU A CD2 1 
ATOM   433  N N   . GLU A 1 57 ? 17.152  31.686 -7.609  1.00 49.79  ? 52  GLU A N   1 
ATOM   434  C CA  . GLU A 1 57 ? 17.204  32.984 -8.308  1.00 50.71  ? 52  GLU A CA  1 
ATOM   435  C C   . GLU A 1 57 ? 16.017  33.884 -7.955  1.00 50.54  ? 52  GLU A C   1 
ATOM   436  O O   . GLU A 1 57 ? 14.987  33.413 -7.436  1.00 44.78  ? 52  GLU A O   1 
ATOM   437  C CB  . GLU A 1 57 ? 17.230  32.794 -9.829  1.00 48.02  ? 52  GLU A CB  1 
ATOM   438  C CG  . GLU A 1 57 ? 18.491  32.142 -10.365 1.00 52.28  ? 52  GLU A CG  1 
ATOM   439  C CD  . GLU A 1 57 ? 18.493  32.071 -11.888 1.00 53.26  ? 52  GLU A CD  1 
ATOM   440  O OE1 . GLU A 1 57 ? 17.394  32.299 -12.464 1.00 45.30  ? 52  GLU A OE1 1 
ATOM   441  O OE2 . GLU A 1 57 ? 19.588  31.811 -12.486 1.00 48.84  ? 52  GLU A OE2 1 
ATOM   442  N N   . HIS A 1 58 ? 16.172  35.181 -8.234  1.00 49.32  ? 53  HIS A N   1 
ATOM   443  C CA  . HIS A 1 58 ? 15.024  36.062 -8.302  1.00 49.70  ? 53  HIS A CA  1 
ATOM   444  C C   . HIS A 1 58 ? 14.399  35.793 -9.625  1.00 48.92  ? 53  HIS A C   1 
ATOM   445  O O   . HIS A 1 58 ? 14.936  35.002 -10.401 1.00 49.96  ? 53  HIS A O   1 
ATOM   446  C CB  . HIS A 1 58 ? 15.434  37.518 -8.118  1.00 49.71  ? 53  HIS A CB  1 
ATOM   447  C CG  . HIS A 1 58 ? 15.628  37.898 -6.669  1.00 51.50  ? 53  HIS A CG  1 
ATOM   448  N ND1 . HIS A 1 58 ? 14.663  37.706 -5.733  1.00 53.06  ? 53  HIS A ND1 1 
ATOM   449  C CD2 . HIS A 1 58 ? 16.724  38.444 -5.997  1.00 53.85  ? 53  HIS A CD2 1 
ATOM   450  C CE1 . HIS A 1 58 ? 15.111  38.121 -4.529  1.00 56.27  ? 53  HIS A CE1 1 
ATOM   451  N NE2 . HIS A 1 58 ? 16.374  38.579 -4.689  1.00 59.14  ? 53  HIS A NE2 1 
ATOM   452  N N   . GLY A 1 59 ? 13.242  36.389 -9.886  1.00 50.28  ? 54  GLY A N   1 
ATOM   453  C CA  . GLY A 1 59 ? 12.644  36.319 -11.223 1.00 50.26  ? 54  GLY A CA  1 
ATOM   454  C C   . GLY A 1 59 ? 13.558  36.886 -12.306 1.00 51.41  ? 54  GLY A C   1 
ATOM   455  O O   . GLY A 1 59 ? 13.483  36.455 -13.457 1.00 53.29  ? 54  GLY A O   1 
ATOM   456  N N   . ASP A 1 60 ? 14.400  37.857 -11.918 1.00 51.03  ? 55  ASP A N   1 
ATOM   457  C CA  . ASP A 1 60 ? 15.519  38.412 -12.707 1.00 51.93  ? 55  ASP A CA  1 
ATOM   458  C C   . ASP A 1 60 ? 16.457  37.396 -13.346 1.00 55.35  ? 55  ASP A C   1 
ATOM   459  O O   . ASP A 1 60 ? 16.984  37.634 -14.448 1.00 59.55  ? 55  ASP A O   1 
ATOM   460  C CB  . ASP A 1 60 ? 16.428  39.249 -11.804 1.00 50.78  ? 55  ASP A CB  1 
ATOM   461  C CG  . ASP A 1 60 ? 16.051  40.688 -11.781 1.00 54.09  ? 55  ASP A CG  1 
ATOM   462  O OD1 . ASP A 1 60 ? 14.887  40.975 -11.458 1.00 58.73  ? 55  ASP A OD1 1 
ATOM   463  O OD2 . ASP A 1 60 ? 16.919  41.544 -12.064 1.00 57.59  ? 55  ASP A OD2 1 
ATOM   464  N N   . GLY A 1 61 ? 16.694  36.293 -12.635 1.00 48.79  ? 56  GLY A N   1 
ATOM   465  C CA  . GLY A 1 61 ? 17.852  35.454 -12.887 1.00 49.21  ? 56  GLY A CA  1 
ATOM   466  C C   . GLY A 1 61 ? 18.990  35.898 -11.975 1.00 50.43  ? 56  GLY A C   1 
ATOM   467  O O   . GLY A 1 61 ? 20.122  35.362 -12.054 1.00 51.80  ? 56  GLY A O   1 
ATOM   468  N N   . GLY A 1 62 ? 18.690  36.895 -11.132 1.00 47.08  ? 57  GLY A N   1 
ATOM   469  C CA  . GLY A 1 62 ? 19.575  37.329 -10.046 1.00 46.51  ? 57  GLY A CA  1 
ATOM   470  C C   . GLY A 1 62 ? 19.885  36.148 -9.164  1.00 45.33  ? 57  GLY A C   1 
ATOM   471  O O   . GLY A 1 62 ? 18.978  35.530 -8.647  1.00 48.40  ? 57  GLY A O   1 
ATOM   472  N N   . ILE A 1 63 ? 21.163  35.823 -9.015  1.00 45.41  ? 58  ILE A N   1 
ATOM   473  C CA  . ILE A 1 63 ? 21.570  34.582 -8.367  1.00 47.08  ? 58  ILE A CA  1 
ATOM   474  C C   . ILE A 1 63 ? 21.967  34.764 -6.908  1.00 45.14  ? 58  ILE A C   1 
ATOM   475  O O   . ILE A 1 63 ? 22.936  35.486 -6.599  1.00 44.77  ? 58  ILE A O   1 
ATOM   476  C CB  . ILE A 1 63 ? 22.715  33.878 -9.138  1.00 47.76  ? 58  ILE A CB  1 
ATOM   477  C CG1 . ILE A 1 63 ? 22.260  33.538 -10.563 1.00 52.68  ? 58  ILE A CG1 1 
ATOM   478  C CG2 . ILE A 1 63 ? 23.155  32.613 -8.405  1.00 45.42  ? 58  ILE A CG2 1 
ATOM   479  C CD1 . ILE A 1 63 ? 23.375  33.273 -11.559 1.00 52.25  ? 58  ILE A CD1 1 
ATOM   480  N N   . LEU A 1 64 ? 21.241  34.047 -6.038  1.00 45.33  ? 59  LEU A N   1 
ATOM   481  C CA  . LEU A 1 64 ? 21.408  34.079 -4.558  1.00 45.56  ? 59  LEU A CA  1 
ATOM   482  C C   . LEU A 1 64 ? 22.546  33.223 -4.039  1.00 44.26  ? 59  LEU A C   1 
ATOM   483  O O   . LEU A 1 64 ? 22.535  32.005 -4.201  1.00 42.42  ? 59  LEU A O   1 
ATOM   484  C CB  . LEU A 1 64 ? 20.129  33.623 -3.858  1.00 45.54  ? 59  LEU A CB  1 
ATOM   485  C CG  . LEU A 1 64 ? 18.893  34.538 -3.780  1.00 48.24  ? 59  LEU A CG  1 
ATOM   486  C CD1 . LEU A 1 64 ? 18.441  35.101 -5.127  1.00 49.48  ? 59  LEU A CD1 1 
ATOM   487  C CD2 . LEU A 1 64 ? 17.752  33.785 -3.110  1.00 44.60  ? 59  LEU A CD2 1 
ATOM   488  N N   . ASP A 1 65 ? 23.523  33.857 -3.393  1.00 48.55  ? 60  ASP A N   1 
ATOM   489  C CA  . ASP A 1 65 ? 24.669  33.103 -2.869  1.00 47.35  ? 60  ASP A CA  1 
ATOM   490  C C   . ASP A 1 65 ? 24.322  32.170 -1.699  1.00 45.58  ? 60  ASP A C   1 
ATOM   491  O O   . ASP A 1 65 ? 23.692  32.575 -0.726  1.00 45.32  ? 60  ASP A O   1 
ATOM   492  C CB  . ASP A 1 65 ? 25.851  34.010 -2.513  1.00 48.21  ? 60  ASP A CB  1 
ATOM   493  C CG  . ASP A 1 65 ? 27.043  33.213 -2.042  1.00 50.22  ? 60  ASP A CG  1 
ATOM   494  O OD1 . ASP A 1 65 ? 27.075  32.897 -0.833  1.00 54.84  ? 60  ASP A OD1 1 
ATOM   495  O OD2 . ASP A 1 65 ? 27.899  32.834 -2.879  1.00 48.72  ? 60  ASP A OD2 1 
ATOM   496  N N   . LEU A 1 66 ? 24.769  30.925 -1.815  1.00 42.41  ? 61  LEU A N   1 
ATOM   497  C CA  . LEU A 1 66 ? 24.450  29.880 -0.864  1.00 41.33  ? 61  LEU A CA  1 
ATOM   498  C C   . LEU A 1 66 ? 24.676  30.180 0.608   1.00 42.31  ? 61  LEU A C   1 
ATOM   499  O O   . LEU A 1 66 ? 24.066  29.542 1.473   1.00 42.48  ? 61  LEU A O   1 
ATOM   500  C CB  . LEU A 1 66 ? 25.249  28.634 -1.192  1.00 40.47  ? 61  LEU A CB  1 
ATOM   501  C CG  . LEU A 1 66 ? 24.986  27.900 -2.488  1.00 39.01  ? 61  LEU A CG  1 
ATOM   502  C CD1 . LEU A 1 66 ? 25.753  26.601 -2.375  1.00 40.63  ? 61  LEU A CD1 1 
ATOM   503  C CD2 . LEU A 1 66 ? 23.509  27.644 -2.676  1.00 37.77  ? 61  LEU A CD2 1 
ATOM   504  N N   . ASP A 1 67 ? 25.567  31.111 0.905   1.00 41.67  ? 62  ASP A N   1 
ATOM   505  C CA  . ASP A 1 67 ? 25.912  31.333 2.291   1.00 47.14  ? 62  ASP A CA  1 
ATOM   506  C C   . ASP A 1 67 ? 25.357  32.634 2.846   1.00 44.59  ? 62  ASP A C   1 
ATOM   507  O O   . ASP A 1 67 ? 25.620  33.006 4.005   1.00 40.74  ? 62  ASP A O   1 
ATOM   508  C CB  . ASP A 1 67 ? 27.423  31.207 2.495   1.00 55.95  ? 62  ASP A CB  1 
ATOM   509  C CG  . ASP A 1 67 ? 27.807  29.979 3.333   1.00 66.02  ? 62  ASP A CG  1 
ATOM   510  O OD1 . ASP A 1 67 ? 27.355  29.869 4.508   1.00 64.95  ? 62  ASP A OD1 1 
ATOM   511  O OD2 . ASP A 1 67 ? 28.590  29.144 2.818   1.00 73.00  ? 62  ASP A OD2 1 
ATOM   512  N N   . ASP A 1 68 ? 24.571  33.300 2.005   1.00 43.66  ? 63  ASP A N   1 
ATOM   513  C CA  . ASP A 1 68 ? 23.935  34.569 2.329   1.00 44.24  ? 63  ASP A CA  1 
ATOM   514  C C   . ASP A 1 68 ? 22.716  34.319 3.173   1.00 44.72  ? 63  ASP A C   1 
ATOM   515  O O   . ASP A 1 68 ? 22.007  33.325 2.942   1.00 42.79  ? 63  ASP A O   1 
ATOM   516  C CB  . ASP A 1 68 ? 23.515  35.306 1.057   1.00 41.91  ? 63  ASP A CB  1 
ATOM   517  C CG  . ASP A 1 68 ? 24.605  36.202 0.512   1.00 42.26  ? 63  ASP A CG  1 
ATOM   518  O OD1 . ASP A 1 68 ? 25.501  36.582 1.268   1.00 39.98  ? 63  ASP A OD1 1 
ATOM   519  O OD2 . ASP A 1 68 ? 24.582  36.532 -0.687  1.00 48.43  ? 63  ASP A OD2 1 
ATOM   520  N N   . ILE A 1 69 ? 22.496  35.214 4.149   1.00 44.68  ? 64  ILE A N   1 
ATOM   521  C CA  . ILE A 1 69 ? 21.313  35.200 5.028   1.00 44.69  ? 64  ILE A CA  1 
ATOM   522  C C   . ILE A 1 69 ? 20.131  35.494 4.124   1.00 43.45  ? 64  ILE A C   1 
ATOM   523  O O   . ILE A 1 69 ? 20.275  36.266 3.187   1.00 44.05  ? 64  ILE A O   1 
ATOM   524  C CB  . ILE A 1 69 ? 21.378  36.333 6.081   1.00 44.36  ? 64  ILE A CB  1 
ATOM   525  C CG1 . ILE A 1 69 ? 22.765  36.444 6.729   1.00 46.31  ? 64  ILE A CG1 1 
ATOM   526  C CG2 . ILE A 1 69 ? 20.235  36.236 7.068   1.00 42.30  ? 64  ILE A CG2 1 
ATOM   527  C CD1 . ILE A 1 69 ? 23.126  35.356 7.721   1.00 52.69  ? 64  ILE A CD1 1 
ATOM   528  N N   . LEU A 1 70 ? 18.962  34.928 4.385   1.00 41.83  ? 65  LEU A N   1 
ATOM   529  C CA  . LEU A 1 70 ? 17.874  35.113 3.421   1.00 42.21  ? 65  LEU A CA  1 
ATOM   530  C C   . LEU A 1 70 ? 17.256  36.529 3.367   1.00 41.33  ? 65  LEU A C   1 
ATOM   531  O O   . LEU A 1 70 ? 17.035  37.080 2.295   1.00 43.47  ? 65  LEU A O   1 
ATOM   532  C CB  . LEU A 1 70 ? 16.797  34.043 3.599   1.00 43.17  ? 65  LEU A CB  1 
ATOM   533  C CG  . LEU A 1 70 ? 15.620  34.062 2.625   1.00 43.09  ? 65  LEU A CG  1 
ATOM   534  C CD1 . LEU A 1 70 ? 16.051  33.885 1.167   1.00 46.37  ? 65  LEU A CD1 1 
ATOM   535  C CD2 . LEU A 1 70 ? 14.636  32.991 3.037   1.00 44.15  ? 65  LEU A CD2 1 
ATOM   536  N N   . CYS A 1 71 ? 16.984  37.115 4.515   1.00 40.54  ? 66  CYS A N   1 
ATOM   537  C CA  . CYS A 1 71 ? 16.280  38.375 4.537   1.00 40.03  ? 66  CYS A CA  1 
ATOM   538  C C   . CYS A 1 71 ? 17.171  39.487 3.993   1.00 39.20  ? 66  CYS A C   1 
ATOM   539  O O   . CYS A 1 71 ? 16.686  40.575 3.695   1.00 40.03  ? 66  CYS A O   1 
ATOM   540  C CB  . CYS A 1 71 ? 15.794  38.681 5.967   1.00 41.39  ? 66  CYS A CB  1 
ATOM   541  S SG  . CYS A 1 71 ? 17.134  38.676 7.191   1.00 49.24  ? 66  CYS A SG  1 
ATOM   542  N N   . ASP A 1 72 ? 18.474  39.226 3.883   1.00 39.77  ? 67  ASP A N   1 
ATOM   543  C CA  . ASP A 1 72 ? 19.405  40.220 3.328   1.00 43.07  ? 67  ASP A CA  1 
ATOM   544  C C   . ASP A 1 72 ? 19.373  40.159 1.792   1.00 45.45  ? 67  ASP A C   1 
ATOM   545  O O   . ASP A 1 72 ? 19.689  41.129 1.115   1.00 50.59  ? 67  ASP A O   1 
ATOM   546  C CB  . ASP A 1 72 ? 20.860  40.027 3.816   1.00 41.79  ? 67  ASP A CB  1 
ATOM   547  C CG  . ASP A 1 72 ? 21.041  40.177 5.351   1.00 45.77  ? 67  ASP A CG  1 
ATOM   548  O OD1 . ASP A 1 72 ? 20.279  40.920 6.037   1.00 46.35  ? 67  ASP A OD1 1 
ATOM   549  O OD2 . ASP A 1 72 ? 21.999  39.544 5.875   1.00 44.39  ? 67  ASP A OD2 1 
ATOM   550  N N   . VAL A 1 73 ? 18.988  39.013 1.251   1.00 46.49  ? 68  VAL A N   1 
ATOM   551  C CA  . VAL A 1 73 ? 19.110  38.746 -0.170  1.00 47.01  ? 68  VAL A CA  1 
ATOM   552  C C   . VAL A 1 73 ? 17.743  38.705 -0.850  1.00 51.80  ? 68  VAL A C   1 
ATOM   553  O O   . VAL A 1 73 ? 17.633  38.725 -2.092  1.00 52.99  ? 68  VAL A O   1 
ATOM   554  C CB  . VAL A 1 73 ? 19.873  37.441 -0.392  1.00 44.90  ? 68  VAL A CB  1 
ATOM   555  C CG1 . VAL A 1 73 ? 20.096  37.195 -1.865  1.00 53.02  ? 68  VAL A CG1 1 
ATOM   556  C CG2 . VAL A 1 73 ? 21.228  37.576 0.232   1.00 46.86  ? 68  VAL A CG2 1 
ATOM   557  N N   . ALA A 1 74 ? 16.694  38.671 -0.038  1.00 50.87  ? 69  ALA A N   1 
ATOM   558  C CA  . ALA A 1 74 ? 15.352  38.691 -0.573  1.00 50.64  ? 69  ALA A CA  1 
ATOM   559  C C   . ALA A 1 74 ? 14.392  39.380 0.390   1.00 47.65  ? 69  ALA A C   1 
ATOM   560  O O   . ALA A 1 74 ? 14.777  39.721 1.493   1.00 51.09  ? 69  ALA A O   1 
ATOM   561  C CB  . ALA A 1 74 ? 14.907  37.268 -0.895  1.00 53.03  ? 69  ALA A CB  1 
ATOM   562  N N   . ASP A 1 75 ? 13.149  39.584 -0.039  1.00 48.16  ? 70  ASP A N   1 
ATOM   563  C CA  . ASP A 1 75 ? 12.113  40.160 0.814   1.00 46.92  ? 70  ASP A CA  1 
ATOM   564  C C   . ASP A 1 75 ? 11.088  39.127 1.250   1.00 45.27  ? 70  ASP A C   1 
ATOM   565  O O   . ASP A 1 75 ? 11.006  38.028 0.677   1.00 40.33  ? 70  ASP A O   1 
ATOM   566  C CB  . ASP A 1 75 ? 11.415  41.321 0.113   1.00 51.44  ? 70  ASP A CB  1 
ATOM   567  C CG  . ASP A 1 75 ? 12.289  42.558 0.030   1.00 58.02  ? 70  ASP A CG  1 
ATOM   568  O OD1 . ASP A 1 75 ? 13.135  42.763 0.932   1.00 58.01  ? 70  ASP A OD1 1 
ATOM   569  O OD2 . ASP A 1 75 ? 12.130  43.324 -0.944  1.00 58.96  ? 70  ASP A OD2 1 
ATOM   570  N N   . ASP A 1 76 ? 10.326  39.480 2.286   1.00 43.60  ? 71  ASP A N   1 
ATOM   571  C CA  . ASP A 1 76 ? 9.257   38.628 2.765   1.00 43.09  ? 71  ASP A CA  1 
ATOM   572  C C   . ASP A 1 76 ? 8.299   38.410 1.600   1.00 43.22  ? 71  ASP A C   1 
ATOM   573  O O   . ASP A 1 76 ? 7.932   39.351 0.891   1.00 40.49  ? 71  ASP A O   1 
ATOM   574  C CB  . ASP A 1 76 ? 8.543   39.246 3.979   1.00 41.46  ? 71  ASP A CB  1 
ATOM   575  C CG  . ASP A 1 76 ? 7.599   38.270 4.671   1.00 45.11  ? 71  ASP A CG  1 
ATOM   576  O OD1 . ASP A 1 76 ? 7.555   37.078 4.320   1.00 51.36  ? 71  ASP A OD1 1 
ATOM   577  O OD2 . ASP A 1 76 ? 6.895   38.676 5.598   1.00 49.65  ? 71  ASP A OD2 1 
ATOM   578  N N   . LYS A 1 77 ? 7.937   37.151 1.385   1.00 44.46  ? 72  LYS A N   1 
ATOM   579  C CA  . LYS A 1 77 ? 6.934   36.796 0.400   1.00 44.90  ? 72  LYS A CA  1 
ATOM   580  C C   . LYS A 1 77 ? 7.435   37.021 -1.027  1.00 43.62  ? 72  LYS A C   1 
ATOM   581  O O   . LYS A 1 77 ? 6.669   37.410 -1.883  1.00 44.47  ? 72  LYS A O   1 
ATOM   582  C CB  . LYS A 1 77 ? 5.644   37.599 0.641   1.00 46.12  ? 72  LYS A CB  1 
ATOM   583  C CG  . LYS A 1 77 ? 4.816   37.160 1.822   1.00 48.85  ? 72  LYS A CG  1 
ATOM   584  C CD  . LYS A 1 77 ? 3.571   38.010 1.991   1.00 52.03  ? 72  LYS A CD  1 
ATOM   585  C CE  . LYS A 1 77 ? 3.803   39.198 2.921   1.00 56.89  ? 72  LYS A CE  1 
ATOM   586  N NZ  . LYS A 1 77 ? 2.516   39.698 3.505   1.00 56.47  ? 72  LYS A NZ  1 
ATOM   587  N N   . ASP A 1 78 ? 8.718   36.786 -1.279  1.00 45.27  ? 73  ASP A N   1 
ATOM   588  C CA  . ASP A 1 78 ? 9.261   36.835 -2.644  1.00 43.57  ? 73  ASP A CA  1 
ATOM   589  C C   . ASP A 1 78 ? 9.098   35.481 -3.357  1.00 44.96  ? 73  ASP A C   1 
ATOM   590  O O   . ASP A 1 78 ? 9.333   34.404 -2.764  1.00 45.64  ? 73  ASP A O   1 
ATOM   591  C CB  . ASP A 1 78 ? 10.752  37.256 -2.664  1.00 44.56  ? 73  ASP A CB  1 
ATOM   592  C CG  . ASP A 1 78 ? 10.973  38.768 -2.448  1.00 44.73  ? 73  ASP A CG  1 
ATOM   593  O OD1 . ASP A 1 78 ? 9.996   39.497 -2.162  1.00 51.52  ? 73  ASP A OD1 1 
ATOM   594  O OD2 . ASP A 1 78 ? 12.133  39.228 -2.562  1.00 40.29  ? 73  ASP A OD2 1 
ATOM   595  N N   . ARG A 1 79 ? 8.679   35.548 -4.623  1.00 44.26  ? 74  ARG A N   1 
ATOM   596  C CA  . ARG A 1 79 ? 8.759   34.424 -5.557  1.00 45.56  ? 74  ARG A CA  1 
ATOM   597  C C   . ARG A 1 79 ? 10.222  34.224 -6.027  1.00 45.12  ? 74  ARG A C   1 
ATOM   598  O O   . ARG A 1 79 ? 10.909  35.184 -6.442  1.00 44.42  ? 74  ARG A O   1 
ATOM   599  C CB  . ARG A 1 79 ? 7.840   34.682 -6.749  1.00 50.40  ? 74  ARG A CB  1 
ATOM   600  C CG  . ARG A 1 79 ? 8.102   33.828 -7.985  1.00 53.16  ? 74  ARG A CG  1 
ATOM   601  C CD  . ARG A 1 79 ? 7.151   34.221 -9.095  1.00 57.28  ? 74  ARG A CD  1 
ATOM   602  N NE  . ARG A 1 79 ? 5.762   33.750 -8.915  1.00 58.32  ? 74  ARG A NE  1 
ATOM   603  C CZ  . ARG A 1 79 ? 4.723   34.488 -8.501  1.00 51.33  ? 74  ARG A CZ  1 
ATOM   604  N NH1 . ARG A 1 79 ? 4.876   35.754 -8.153  1.00 52.47  ? 74  ARG A NH1 1 
ATOM   605  N NH2 . ARG A 1 79 ? 3.521   33.949 -8.420  1.00 48.22  ? 74  ARG A NH2 1 
ATOM   606  N N   . LEU A 1 80 ? 10.693  32.979 -5.920  1.00 42.20  ? 75  LEU A N   1 
ATOM   607  C CA  . LEU A 1 80 ? 12.083  32.620 -6.234  1.00 41.15  ? 75  LEU A CA  1 
ATOM   608  C C   . LEU A 1 80 ? 12.017  31.376 -7.074  1.00 40.48  ? 75  LEU A C   1 
ATOM   609  O O   . LEU A 1 80 ? 11.206  30.498 -6.787  1.00 40.88  ? 75  LEU A O   1 
ATOM   610  C CB  . LEU A 1 80 ? 12.932  32.334 -4.966  1.00 39.85  ? 75  LEU A CB  1 
ATOM   611  C CG  . LEU A 1 80 ? 12.946  33.252 -3.727  1.00 37.78  ? 75  LEU A CG  1 
ATOM   612  C CD1 . LEU A 1 80 ? 13.556  32.519 -2.557  1.00 35.84  ? 75  LEU A CD1 1 
ATOM   613  C CD2 . LEU A 1 80 ? 13.667  34.580 -3.960  1.00 38.95  ? 75  LEU A CD2 1 
ATOM   614  N N   . VAL A 1 81 ? 12.860  31.312 -8.103  1.00 40.55  ? 76  VAL A N   1 
ATOM   615  C CA  . VAL A 1 81 ? 12.911  30.162 -9.006  1.00 43.45  ? 76  VAL A CA  1 
ATOM   616  C C   . VAL A 1 81 ? 14.087  29.230 -8.658  1.00 47.77  ? 76  VAL A C   1 
ATOM   617  O O   . VAL A 1 81 ? 15.173  29.683 -8.284  1.00 51.66  ? 76  VAL A O   1 
ATOM   618  C CB  . VAL A 1 81 ? 12.971  30.579 -10.494 1.00 40.57  ? 76  VAL A CB  1 
ATOM   619  C CG1 . VAL A 1 81 ? 12.540  32.032 -10.671 1.00 41.74  ? 76  VAL A CG1 1 
ATOM   620  C CG2 . VAL A 1 81 ? 14.356  30.390 -11.052 1.00 38.12  ? 76  VAL A CG2 1 
ATOM   621  N N   . ALA A 1 82 ? 13.866  27.923 -8.747  1.00 49.17  ? 77  ALA A N   1 
ATOM   622  C CA  . ALA A 1 82 ? 14.971  26.982 -8.579  1.00 48.11  ? 77  ALA A CA  1 
ATOM   623  C C   . ALA A 1 82 ? 15.442  26.455 -9.961  1.00 45.80  ? 77  ALA A C   1 
ATOM   624  O O   . ALA A 1 82 ? 14.638  26.165 -10.859 1.00 45.86  ? 77  ALA A O   1 
ATOM   625  C CB  . ALA A 1 82 ? 14.584  25.854 -7.613  1.00 43.78  ? 77  ALA A CB  1 
ATOM   626  N N   . VAL A 1 83 ? 16.750  26.393 -10.136 1.00 44.87  ? 78  VAL A N   1 
ATOM   627  C CA  . VAL A 1 83 ? 17.350  25.792 -11.322 1.00 45.05  ? 78  VAL A CA  1 
ATOM   628  C C   . VAL A 1 83 ? 17.834  24.419 -10.818 1.00 48.36  ? 78  VAL A C   1 
ATOM   629  O O   . VAL A 1 83 ? 18.677  24.327 -9.897  1.00 46.37  ? 78  VAL A O   1 
ATOM   630  C CB  . VAL A 1 83 ? 18.476  26.714 -11.875 1.00 40.18  ? 78  VAL A CB  1 
ATOM   631  C CG1 . VAL A 1 83 ? 19.462  25.959 -12.749 1.00 36.07  ? 78  VAL A CG1 1 
ATOM   632  C CG2 . VAL A 1 83 ? 17.870  27.903 -12.607 1.00 37.94  ? 78  VAL A CG2 1 
ATOM   633  N N   . PHE A 1 84 ? 17.257  23.349 -11.365 1.00 49.55  ? 79  PHE A N   1 
ATOM   634  C CA  . PHE A 1 84 ? 17.389  22.024 -10.719 1.00 49.25  ? 79  PHE A CA  1 
ATOM   635  C C   . PHE A 1 84 ? 17.256  20.924 -11.740 1.00 48.26  ? 79  PHE A C   1 
ATOM   636  O O   . PHE A 1 84 ? 16.812  21.178 -12.844 1.00 45.26  ? 79  PHE A O   1 
ATOM   637  C CB  . PHE A 1 84 ? 16.298  21.818 -9.633  1.00 44.10  ? 79  PHE A CB  1 
ATOM   638  C CG  . PHE A 1 84 ? 14.880  21.722 -10.195 1.00 43.39  ? 79  PHE A CG  1 
ATOM   639  C CD1 . PHE A 1 84 ? 14.164  22.873 -10.562 1.00 40.85  ? 79  PHE A CD1 1 
ATOM   640  C CD2 . PHE A 1 84 ? 14.259  20.484 -10.377 1.00 43.22  ? 79  PHE A CD2 1 
ATOM   641  C CE1 . PHE A 1 84 ? 12.869  22.789 -11.079 1.00 39.58  ? 79  PHE A CE1 1 
ATOM   642  C CE2 . PHE A 1 84 ? 12.963  20.399 -10.902 1.00 41.20  ? 79  PHE A CE2 1 
ATOM   643  C CZ  . PHE A 1 84 ? 12.266  21.551 -11.251 1.00 39.65  ? 79  PHE A CZ  1 
ATOM   644  N N   . ASP A 1 85 ? 17.624  19.707 -11.331 1.00 57.16  ? 80  ASP A N   1 
ATOM   645  C CA  . ASP A 1 85 ? 17.281  18.454 -12.025 1.00 58.83  ? 80  ASP A CA  1 
ATOM   646  C C   . ASP A 1 85 ? 16.570  17.456 -11.073 1.00 59.42  ? 80  ASP A C   1 
ATOM   647  O O   . ASP A 1 85 ? 16.646  17.593 -9.838  1.00 49.28  ? 80  ASP A O   1 
ATOM   648  C CB  . ASP A 1 85 ? 18.524  17.789 -12.635 1.00 61.07  ? 80  ASP A CB  1 
ATOM   649  C CG  . ASP A 1 85 ? 19.332  18.728 -13.542 1.00 64.18  ? 80  ASP A CG  1 
ATOM   650  O OD1 . ASP A 1 85 ? 19.126  19.966 -13.501 1.00 64.13  ? 80  ASP A OD1 1 
ATOM   651  O OD2 . ASP A 1 85 ? 20.209  18.218 -14.284 1.00 59.08  ? 80  ASP A OD2 1 
ATOM   652  N N   . GLU A 1 86 ? 15.906  16.451 -11.672 1.00 64.44  ? 81  GLU A N   1 
ATOM   653  C CA  . GLU A 1 86 ? 15.038  15.482 -10.959 1.00 63.12  ? 81  GLU A CA  1 
ATOM   654  C C   . GLU A 1 86 ? 14.789  14.162 -11.722 1.00 60.61  ? 81  GLU A C   1 
ATOM   655  O O   . GLU A 1 86 ? 15.216  14.016 -12.888 1.00 57.35  ? 81  GLU A O   1 
ATOM   656  C CB  . GLU A 1 86 ? 13.680  16.122 -10.635 1.00 61.20  ? 81  GLU A CB  1 
ATOM   657  C CG  . GLU A 1 86 ? 12.704  16.065 -11.804 1.00 58.47  ? 81  GLU A CG  1 
ATOM   658  C CD  . GLU A 1 86 ? 11.468  16.929 -11.652 1.00 56.10  ? 81  GLU A CD  1 
ATOM   659  O OE1 . GLU A 1 86 ? 11.407  17.795 -10.777 1.00 57.00  ? 81  GLU A OE1 1 
ATOM   660  O OE2 . GLU A 1 86 ? 10.534  16.745 -12.439 1.00 63.43  ? 81  GLU A OE2 1 
ATOM   661  N N   . GLN A 1 87 ? 14.085  13.244 -11.032 1.00 58.23  ? 82  GLN A N   1 
ATOM   662  C CA  . GLN A 1 87 ? 13.572  11.933 -11.525 1.00 62.95  ? 82  GLN A CA  1 
ATOM   663  C C   . GLN A 1 87 ? 14.172  10.675 -10.862 1.00 58.75  ? 82  GLN A C   1 
ATOM   664  O O   . GLN A 1 87 ? 13.617  9.568  -10.963 1.00 50.28  ? 82  GLN A O   1 
ATOM   665  C CB  . GLN A 1 87 ? 13.618  11.805 -13.054 1.00 62.28  ? 82  GLN A CB  1 
ATOM   666  C CG  . GLN A 1 87 ? 12.357  12.328 -13.708 1.00 65.52  ? 82  GLN A CG  1 
ATOM   667  C CD  . GLN A 1 87 ? 11.909  11.476 -14.883 1.00 68.04  ? 82  GLN A CD  1 
ATOM   668  O OE1 . GLN A 1 87 ? 12.731  10.885 -15.600 1.00 68.83  ? 82  GLN A OE1 1 
ATOM   669  N NE2 . GLN A 1 87 ? 10.596  11.408 -15.087 1.00 58.50  ? 82  GLN A NE2 1 
ATOM   670  N N   . GLU B 1 5  ? -8.269  35.398 17.104  1.00 50.23  ? 0   GLU B N   1 
ATOM   671  C CA  . GLU B 1 5  ? -9.267  35.863 16.093  1.00 49.27  ? 0   GLU B CA  1 
ATOM   672  C C   . GLU B 1 5  ? -8.826  35.722 14.605  1.00 49.43  ? 0   GLU B C   1 
ATOM   673  O O   . GLU B 1 5  ? -9.506  36.208 13.705  1.00 50.96  ? 0   GLU B O   1 
ATOM   674  C CB  . GLU B 1 5  ? -9.772  37.269 16.449  1.00 52.25  ? 0   GLU B CB  1 
ATOM   675  C CG  . GLU B 1 5  ? -10.752 37.249 17.642  1.00 58.06  ? 0   GLU B CG  1 
ATOM   676  C CD  . GLU B 1 5  ? -11.338 38.618 18.063  1.00 57.26  ? 0   GLU B CD  1 
ATOM   677  O OE1 . GLU B 1 5  ? -10.633 39.663 17.996  1.00 50.47  ? 0   GLU B OE1 1 
ATOM   678  O OE2 . GLU B 1 5  ? -12.522 38.632 18.489  1.00 52.81  ? 0   GLU B OE2 1 
ATOM   679  N N   . PHE B 1 6  ? -7.714  35.024 14.364  1.00 46.58  ? 1   PHE B N   1 
ATOM   680  C CA  . PHE B 1 6  ? -7.223  34.680 13.017  1.00 44.89  ? 1   PHE B CA  1 
ATOM   681  C C   . PHE B 1 6  ? -8.293  33.933 12.177  1.00 43.25  ? 1   PHE B C   1 
ATOM   682  O O   . PHE B 1 6  ? -9.097  33.140 12.724  1.00 40.22  ? 1   PHE B O   1 
ATOM   683  C CB  . PHE B 1 6  ? -5.931  33.834 13.170  1.00 47.49  ? 1   PHE B CB  1 
ATOM   684  C CG  . PHE B 1 6  ? -5.089  33.685 11.895  1.00 50.28  ? 1   PHE B CG  1 
ATOM   685  C CD1 . PHE B 1 6  ? -5.550  32.945 10.782  1.00 46.96  ? 1   PHE B CD1 1 
ATOM   686  C CD2 . PHE B 1 6  ? -3.795  34.227 11.834  1.00 47.61  ? 1   PHE B CD2 1 
ATOM   687  C CE1 . PHE B 1 6  ? -4.763  32.797 9.655   1.00 42.12  ? 1   PHE B CE1 1 
ATOM   688  C CE2 . PHE B 1 6  ? -3.014  34.079 10.702  1.00 44.19  ? 1   PHE B CE2 1 
ATOM   689  C CZ  . PHE B 1 6  ? -3.500  33.369 9.615   1.00 44.32  ? 1   PHE B CZ  1 
ATOM   690  N N   . LYS B 1 7  ? -8.287  34.195 10.857  1.00 39.76  ? 2   LYS B N   1 
ATOM   691  C CA  . LYS B 1 7  ? -9.268  33.624 9.898   1.00 38.83  ? 2   LYS B CA  1 
ATOM   692  C C   . LYS B 1 7  ? -8.841  33.712 8.454   1.00 36.40  ? 2   LYS B C   1 
ATOM   693  O O   . LYS B 1 7  ? -8.099  34.615 8.072   1.00 38.35  ? 2   LYS B O   1 
ATOM   694  C CB  . LYS B 1 7  ? -10.633 34.332 9.997   1.00 41.69  ? 2   LYS B CB  1 
ATOM   695  C CG  . LYS B 1 7  ? -10.621 35.822 9.658   1.00 45.95  ? 2   LYS B CG  1 
ATOM   696  C CD  . LYS B 1 7  ? -12.013 36.363 9.383   1.00 51.14  ? 2   LYS B CD  1 
ATOM   697  C CE  . LYS B 1 7  ? -12.012 37.840 8.986   1.00 56.15  ? 2   LYS B CE  1 
ATOM   698  N NZ  . LYS B 1 7  ? -12.043 38.776 10.154  1.00 60.07  ? 2   LYS B NZ  1 
ATOM   699  N N   . VAL B 1 8  ? -9.383  32.820 7.634   1.00 34.88  ? 3   VAL B N   1 
ATOM   700  C CA  . VAL B 1 8  ? -9.093  32.785 6.195   1.00 33.86  ? 3   VAL B CA  1 
ATOM   701  C C   . VAL B 1 8  ? -10.328 32.441 5.340   1.00 36.67  ? 3   VAL B C   1 
ATOM   702  O O   . VAL B 1 8  ? -11.262 31.789 5.810   1.00 36.48  ? 3   VAL B O   1 
ATOM   703  C CB  . VAL B 1 8  ? -8.003  31.751 5.890   1.00 31.85  ? 3   VAL B CB  1 
ATOM   704  C CG1 . VAL B 1 8  ? -6.646  32.228 6.360   1.00 28.95  ? 3   VAL B CG1 1 
ATOM   705  C CG2 . VAL B 1 8  ? -8.336  30.402 6.520   1.00 32.53  ? 3   VAL B CG2 1 
ATOM   706  N N   . THR B 1 9  ? -10.344 32.875 4.083   1.00 39.84  ? 4   THR B N   1 
ATOM   707  C CA  . THR B 1 9  ? -11.354 32.366 3.146   1.00 44.01  ? 4   THR B CA  1 
ATOM   708  C C   . THR B 1 9  ? -10.792 31.238 2.301   1.00 48.04  ? 4   THR B C   1 
ATOM   709  O O   . THR B 1 9  ? -9.656  31.324 1.826   1.00 54.37  ? 4   THR B O   1 
ATOM   710  C CB  . THR B 1 9  ? -11.836 33.437 2.176   1.00 45.27  ? 4   THR B CB  1 
ATOM   711  O OG1 . THR B 1 9  ? -12.269 34.564 2.928   1.00 47.07  ? 4   THR B OG1 1 
ATOM   712  C CG2 . THR B 1 9  ? -13.005 32.906 1.300   1.00 46.02  ? 4   THR B CG2 1 
ATOM   713  N N   . VAL B 1 10 ? -11.589 30.191 2.098   1.00 46.34  ? 5   VAL B N   1 
ATOM   714  C CA  . VAL B 1 10 ? -11.175 29.072 1.250   1.00 46.39  ? 5   VAL B CA  1 
ATOM   715  C C   . VAL B 1 10 ? -12.050 29.006 -0.020  1.00 45.09  ? 5   VAL B C   1 
ATOM   716  O O   . VAL B 1 10 ? -13.257 29.172 0.064   1.00 47.25  ? 5   VAL B O   1 
ATOM   717  C CB  . VAL B 1 10 ? -11.142 27.747 2.059   1.00 42.74  ? 5   VAL B CB  1 
ATOM   718  C CG1 . VAL B 1 10 ? -10.906 26.557 1.145   1.00 43.00  ? 5   VAL B CG1 1 
ATOM   719  C CG2 . VAL B 1 10 ? -10.056 27.796 3.131   1.00 39.78  ? 5   VAL B CG2 1 
ATOM   720  N N   . CYS B 1 11 ? -11.447 28.790 -1.187  1.00 44.31  ? 6   CYS B N   1 
ATOM   721  C CA  . CYS B 1 11 ? -12.221 28.769 -2.435  1.00 46.80  ? 6   CYS B CA  1 
ATOM   722  C C   . CYS B 1 11 ? -12.478 27.393 -3.006  1.00 46.86  ? 6   CYS B C   1 
ATOM   723  O O   . CYS B 1 11 ? -11.566 26.723 -3.476  1.00 53.98  ? 6   CYS B O   1 
ATOM   724  C CB  . CYS B 1 11 ? -11.577 29.648 -3.490  1.00 49.26  ? 6   CYS B CB  1 
ATOM   725  S SG  . CYS B 1 11 ? -11.741 31.375 -3.018  1.00 64.13  ? 6   CYS B SG  1 
ATOM   726  N N   . PHE B 1 12 ? -13.731 26.976 -2.964  1.00 43.05  ? 7   PHE B N   1 
ATOM   727  C CA  . PHE B 1 12 ? -14.130 25.753 -3.603  1.00 43.52  ? 7   PHE B CA  1 
ATOM   728  C C   . PHE B 1 12 ? -14.852 26.133 -4.876  1.00 48.79  ? 7   PHE B C   1 
ATOM   729  O O   . PHE B 1 12 ? -16.075 26.292 -4.903  1.00 55.56  ? 7   PHE B O   1 
ATOM   730  C CB  . PHE B 1 12 ? -15.066 24.981 -2.709  1.00 42.23  ? 7   PHE B CB  1 
ATOM   731  C CG  . PHE B 1 12 ? -14.428 24.475 -1.447  1.00 43.21  ? 7   PHE B CG  1 
ATOM   732  C CD1 . PHE B 1 12 ? -13.715 23.288 -1.439  1.00 41.01  ? 7   PHE B CD1 1 
ATOM   733  C CD2 . PHE B 1 12 ? -14.569 25.172 -0.243  1.00 42.92  ? 7   PHE B CD2 1 
ATOM   734  C CE1 . PHE B 1 12 ? -13.150 22.824 -0.255  1.00 45.37  ? 7   PHE B CE1 1 
ATOM   735  C CE2 . PHE B 1 12 ? -14.006 24.700 0.943   1.00 40.96  ? 7   PHE B CE2 1 
ATOM   736  C CZ  . PHE B 1 12 ? -13.290 23.529 0.942   1.00 39.66  ? 7   PHE B CZ  1 
ATOM   737  N N   . GLY B 1 13 ? -14.095 26.295 -5.946  1.00 49.49  ? 8   GLY B N   1 
ATOM   738  C CA  . GLY B 1 13 ? -14.693 26.759 -7.168  1.00 44.50  ? 8   GLY B CA  1 
ATOM   739  C C   . GLY B 1 13 ? -15.089 28.144 -6.821  1.00 45.55  ? 8   GLY B C   1 
ATOM   740  O O   . GLY B 1 13 ? -14.276 28.901 -6.297  1.00 45.92  ? 8   GLY B O   1 
ATOM   741  N N   . ARG B 1 14 ? -16.346 28.468 -7.063  1.00 51.54  ? 9   ARG B N   1 
ATOM   742  C CA  . ARG B 1 14 ? -16.764 29.873 -7.015  1.00 55.15  ? 9   ARG B CA  1 
ATOM   743  C C   . ARG B 1 14 ? -17.336 30.219 -5.658  1.00 52.47  ? 9   ARG B C   1 
ATOM   744  O O   . ARG B 1 14 ? -17.458 31.403 -5.296  1.00 53.12  ? 9   ARG B O   1 
ATOM   745  C CB  . ARG B 1 14 ? -17.713 30.209 -8.183  1.00 59.36  ? 9   ARG B CB  1 
ATOM   746  C CG  . ARG B 1 14 ? -17.006 30.074 -9.532  1.00 73.23  ? 9   ARG B CG  1 
ATOM   747  C CD  . ARG B 1 14 ? -17.900 29.843 -10.761 1.00 85.86  ? 9   ARG B CD  1 
ATOM   748  N NE  . ARG B 1 14 ? -18.811 28.674 -10.736 1.00 89.75  ? 9   ARG B NE  1 
ATOM   749  C CZ  . ARG B 1 14 ? -18.463 27.382 -10.638 1.00 86.97  ? 9   ARG B CZ  1 
ATOM   750  N NH1 . ARG B 1 14 ? -17.197 26.991 -10.499 1.00 79.41  ? 9   ARG B NH1 1 
ATOM   751  N NH2 . ARG B 1 14 ? -19.413 26.462 -10.646 1.00 87.50  ? 9   ARG B NH2 1 
ATOM   752  N N   . THR B 1 15 ? -17.661 29.172 -4.907  1.00 49.87  ? 10  THR B N   1 
ATOM   753  C CA  . THR B 1 15 ? -18.149 29.315 -3.549  1.00 54.18  ? 10  THR B CA  1 
ATOM   754  C C   . THR B 1 15 ? -16.980 29.628 -2.612  1.00 56.08  ? 10  THR B C   1 
ATOM   755  O O   . THR B 1 15 ? -15.976 28.901 -2.576  1.00 56.55  ? 10  THR B O   1 
ATOM   756  C CB  . THR B 1 15 ? -18.840 28.043 -3.026  1.00 58.67  ? 10  THR B CB  1 
ATOM   757  O OG1 . THR B 1 15 ? -18.922 27.045 -4.059  1.00 66.83  ? 10  THR B OG1 1 
ATOM   758  C CG2 . THR B 1 15 ? -20.223 28.383 -2.513  1.00 59.73  ? 10  THR B CG2 1 
ATOM   759  N N   . ARG B 1 16 ? -17.112 30.723 -1.872  1.00 50.67  ? 11  ARG B N   1 
ATOM   760  C CA  . ARG B 1 16 ? -16.102 31.119 -0.924  1.00 47.77  ? 11  ARG B CA  1 
ATOM   761  C C   . ARG B 1 16 ? -16.657 30.928 0.470   1.00 45.84  ? 11  ARG B C   1 
ATOM   762  O O   . ARG B 1 16 ? -17.749 31.392 0.781   1.00 49.36  ? 11  ARG B O   1 
ATOM   763  C CB  . ARG B 1 16 ? -15.700 32.571 -1.158  1.00 45.48  ? 11  ARG B CB  1 
ATOM   764  C CG  . ARG B 1 16 ? -14.895 32.764 -2.419  1.00 44.44  ? 11  ARG B CG  1 
ATOM   765  C CD  . ARG B 1 16 ? -14.760 34.229 -2.764  1.00 45.72  ? 11  ARG B CD  1 
ATOM   766  N NE  . ARG B 1 16 ? -13.978 34.398 -3.987  1.00 52.10  ? 11  ARG B NE  1 
ATOM   767  C CZ  . ARG B 1 16 ? -13.730 35.570 -4.570  1.00 57.32  ? 11  ARG B CZ  1 
ATOM   768  N NH1 . ARG B 1 16 ? -14.219 36.698 -4.058  1.00 62.11  ? 11  ARG B NH1 1 
ATOM   769  N NH2 . ARG B 1 16 ? -12.994 35.620 -5.672  1.00 55.86  ? 11  ARG B NH2 1 
ATOM   770  N N   . VAL B 1 17 ? -15.912 30.238 1.312   1.00 42.29  ? 12  VAL B N   1 
ATOM   771  C CA  . VAL B 1 17 ? -16.347 30.034 2.681   1.00 43.01  ? 12  VAL B CA  1 
ATOM   772  C C   . VAL B 1 17 ? -15.316 30.629 3.669   1.00 41.59  ? 12  VAL B C   1 
ATOM   773  O O   . VAL B 1 17 ? -14.117 30.561 3.427   1.00 45.25  ? 12  VAL B O   1 
ATOM   774  C CB  . VAL B 1 17 ? -16.701 28.535 2.923   1.00 42.07  ? 12  VAL B CB  1 
ATOM   775  C CG1 . VAL B 1 17 ? -15.457 27.711 3.190   1.00 42.52  ? 12  VAL B CG1 1 
ATOM   776  C CG2 . VAL B 1 17 ? -17.702 28.367 4.056   1.00 44.73  ? 12  VAL B CG2 1 
ATOM   777  N N   . VAL B 1 18 ? -15.799 31.241 4.748   1.00 39.23  ? 13  VAL B N   1 
ATOM   778  C CA  . VAL B 1 18 ? -14.945 31.835 5.786   1.00 40.57  ? 13  VAL B CA  1 
ATOM   779  C C   . VAL B 1 18 ? -14.770 30.889 6.964   1.00 39.97  ? 13  VAL B C   1 
ATOM   780  O O   . VAL B 1 18 ? -15.751 30.565 7.647   1.00 45.48  ? 13  VAL B O   1 
ATOM   781  C CB  . VAL B 1 18 ? -15.598 33.104 6.378   1.00 42.13  ? 13  VAL B CB  1 
ATOM   782  C CG1 . VAL B 1 18 ? -14.601 33.910 7.224   1.00 35.84  ? 13  VAL B CG1 1 
ATOM   783  C CG2 . VAL B 1 18 ? -16.288 33.923 5.276   1.00 42.45  ? 13  VAL B CG2 1 
ATOM   784  N N   . VAL B 1 19 ? -13.523 30.510 7.226   1.00 40.08  ? 14  VAL B N   1 
ATOM   785  C CA  . VAL B 1 19 ? -13.125 29.657 8.375   1.00 39.47  ? 14  VAL B CA  1 
ATOM   786  C C   . VAL B 1 19 ? -12.351 30.418 9.441   1.00 36.14  ? 14  VAL B C   1 
ATOM   787  O O   . VAL B 1 19 ? -11.324 31.019 9.127   1.00 31.20  ? 14  VAL B O   1 
ATOM   788  C CB  . VAL B 1 19 ? -12.128 28.570 7.936   1.00 40.06  ? 14  VAL B CB  1 
ATOM   789  C CG1 . VAL B 1 19 ? -11.876 27.581 9.076   1.00 36.31  ? 14  VAL B CG1 1 
ATOM   790  C CG2 . VAL B 1 19 ? -12.585 27.913 6.630   1.00 38.23  ? 14  VAL B CG2 1 
ATOM   791  N N   . PRO B 1 20 ? -12.806 30.349 10.704  1.00 38.91  ? 15  PRO B N   1 
ATOM   792  C CA  . PRO B 1 20 ? -12.053 30.859 11.886  1.00 41.41  ? 15  PRO B CA  1 
ATOM   793  C C   . PRO B 1 20 ? -10.915 29.933 12.315  1.00 38.12  ? 15  PRO B C   1 
ATOM   794  O O   . PRO B 1 20 ? -11.064 28.708 12.260  1.00 34.88  ? 15  PRO B O   1 
ATOM   795  C CB  . PRO B 1 20 ? -13.111 30.896 12.997  1.00 42.63  ? 15  PRO B CB  1 
ATOM   796  C CG  . PRO B 1 20 ? -14.104 29.853 12.606  1.00 41.29  ? 15  PRO B CG  1 
ATOM   797  C CD  . PRO B 1 20 ? -14.110 29.781 11.085  1.00 40.27  ? 15  PRO B CD  1 
ATOM   798  N N   . CYS B 1 21 ? -9.805  30.501 12.762  1.00 39.48  ? 16  CYS B N   1 
ATOM   799  C CA  . CYS B 1 21 ? -8.675  29.646 13.132  1.00 46.91  ? 16  CYS B CA  1 
ATOM   800  C C   . CYS B 1 21 ? -8.123  29.738 14.559  1.00 47.86  ? 16  CYS B C   1 
ATOM   801  O O   . CYS B 1 21 ? -7.098  29.122 14.863  1.00 46.88  ? 16  CYS B O   1 
ATOM   802  C CB  . CYS B 1 21 ? -7.550  29.865 12.149  1.00 51.13  ? 16  CYS B CB  1 
ATOM   803  S SG  . CYS B 1 21 ? -8.089  29.553 10.460  1.00 61.77  ? 16  CYS B SG  1 
ATOM   804  N N   . GLY B 1 22 ? -8.804  30.482 15.427  1.00 46.86  ? 17  GLY B N   1 
ATOM   805  C CA  . GLY B 1 22 ? -8.264  30.787 16.728  1.00 48.69  ? 17  GLY B CA  1 
ATOM   806  C C   . GLY B 1 22 ? -7.082  31.710 16.555  1.00 52.40  ? 17  GLY B C   1 
ATOM   807  O O   . GLY B 1 22 ? -7.262  32.870 16.190  1.00 54.50  ? 17  GLY B O   1 
ATOM   808  N N   . ASP B 1 23 ? -5.875  31.203 16.807  1.00 55.45  ? 18  ASP B N   1 
ATOM   809  C CA  . ASP B 1 23 ? -4.649  31.998 16.608  1.00 59.58  ? 18  ASP B CA  1 
ATOM   810  C C   . ASP B 1 23 ? -3.920  31.744 15.272  1.00 64.03  ? 18  ASP B C   1 
ATOM   811  O O   . ASP B 1 23 ? -2.992  32.476 14.939  1.00 73.19  ? 18  ASP B O   1 
ATOM   812  C CB  . ASP B 1 23 ? -3.664  31.905 17.800  1.00 57.30  ? 18  ASP B CB  1 
ATOM   813  C CG  . ASP B 1 23 ? -3.872  30.665 18.651  1.00 60.77  ? 18  ASP B CG  1 
ATOM   814  O OD1 . ASP B 1 23 ? -5.034  30.228 18.798  1.00 63.60  ? 18  ASP B OD1 1 
ATOM   815  O OD2 . ASP B 1 23 ? -2.878  30.128 19.192  1.00 61.26  ? 18  ASP B OD2 1 
ATOM   816  N N   . GLY B 1 24 ? -4.342  30.732 14.510  1.00 59.90  ? 19  GLY B N   1 
ATOM   817  C CA  . GLY B 1 24 ? -3.653  30.362 13.271  1.00 54.37  ? 19  GLY B CA  1 
ATOM   818  C C   . GLY B 1 24 ? -2.525  29.354 13.438  1.00 52.46  ? 19  GLY B C   1 
ATOM   819  O O   . GLY B 1 24 ? -1.749  29.126 12.509  1.00 48.73  ? 19  GLY B O   1 
ATOM   820  N N   . ARG B 1 25 ? -2.464  28.741 14.621  1.00 55.59  ? 20  ARG B N   1 
ATOM   821  C CA  . ARG B 1 25 ? -1.413  27.796 14.997  1.00 56.37  ? 20  ARG B CA  1 
ATOM   822  C C   . ARG B 1 25 ? -1.801  26.352 14.658  1.00 53.64  ? 20  ARG B C   1 
ATOM   823  O O   . ARG B 1 25 ? -1.036  25.418 14.873  1.00 50.46  ? 20  ARG B O   1 
ATOM   824  C CB  . ARG B 1 25 ? -1.068  27.949 16.484  1.00 66.11  ? 20  ARG B CB  1 
ATOM   825  C CG  . ARG B 1 25 ? -0.529  29.331 16.875  1.00 75.01  ? 20  ARG B CG  1 
ATOM   826  C CD  . ARG B 1 25 ? 0.995   29.370 16.958  1.00 84.03  ? 20  ARG B CD  1 
ATOM   827  N NE  . ARG B 1 25 ? 1.526   28.349 17.871  1.00 95.09  ? 20  ARG B NE  1 
ATOM   828  C CZ  . ARG B 1 25 ? 1.750   28.528 19.174  1.00 101.03 ? 20  ARG B CZ  1 
ATOM   829  N NH1 . ARG B 1 25 ? 1.504   29.702 19.749  1.00 92.36  ? 20  ARG B NH1 1 
ATOM   830  N NH2 . ARG B 1 25 ? 2.227   27.526 19.909  1.00 102.86 ? 20  ARG B NH2 1 
ATOM   831  N N   . MET B 1 26 ? -2.983  26.181 14.084  1.00 53.59  ? 21  MET B N   1 
ATOM   832  C CA  . MET B 1 26 ? -3.394  24.889 13.537  1.00 50.90  ? 21  MET B CA  1 
ATOM   833  C C   . MET B 1 26 ? -2.706  24.504 12.216  1.00 49.05  ? 21  MET B C   1 
ATOM   834  O O   . MET B 1 26 ? -2.385  25.369 11.399  1.00 49.03  ? 21  MET B O   1 
ATOM   835  C CB  . MET B 1 26 ? -4.891  24.905 13.323  1.00 51.22  ? 21  MET B CB  1 
ATOM   836  C CG  . MET B 1 26 ? -5.398  25.932 12.331  1.00 50.27  ? 21  MET B CG  1 
ATOM   837  S SD  . MET B 1 26 ? -6.972  25.263 11.751  1.00 62.85  ? 21  MET B SD  1 
ATOM   838  C CE  . MET B 1 26 ? -7.235  26.252 10.301  1.00 55.39  ? 21  MET B CE  1 
ATOM   839  N N   . LYS B 1 27 ? -2.510  23.204 11.999  1.00 46.38  ? 22  LYS B N   1 
ATOM   840  C CA  . LYS B 1 27 ? -1.910  22.714 10.757  1.00 47.03  ? 22  LYS B CA  1 
ATOM   841  C C   . LYS B 1 27 ? -2.746  23.019 9.499   1.00 46.78  ? 22  LYS B C   1 
ATOM   842  O O   . LYS B 1 27 ? -3.959  23.271 9.582   1.00 43.28  ? 22  LYS B O   1 
ATOM   843  C CB  . LYS B 1 27 ? -1.650  21.215 10.837  1.00 47.71  ? 22  LYS B CB  1 
ATOM   844  C CG  . LYS B 1 27 ? -0.246  20.862 11.255  1.00 50.50  ? 22  LYS B CG  1 
ATOM   845  C CD  . LYS B 1 27 ? -0.144  20.643 12.759  1.00 56.63  ? 22  LYS B CD  1 
ATOM   846  C CE  . LYS B 1 27 ? 1.255   20.982 13.283  1.00 55.88  ? 22  LYS B CE  1 
ATOM   847  N NZ  . LYS B 1 27 ? 2.348   20.343 12.489  1.00 57.52  ? 22  LYS B NZ  1 
ATOM   848  N N   . VAL B 1 28 ? -2.084  22.972 8.338   1.00 44.26  ? 23  VAL B N   1 
ATOM   849  C CA  . VAL B 1 28 ? -2.745  23.190 7.051   1.00 41.55  ? 23  VAL B CA  1 
ATOM   850  C C   . VAL B 1 28 ? -3.779  22.059 6.835   1.00 41.47  ? 23  VAL B C   1 
ATOM   851  O O   . VAL B 1 28 ? -4.853  22.277 6.298   1.00 41.13  ? 23  VAL B O   1 
ATOM   852  C CB  . VAL B 1 28 ? -1.713  23.428 5.880   1.00 40.35  ? 23  VAL B CB  1 
ATOM   853  C CG1 . VAL B 1 28 ? -2.376  23.497 4.516   1.00 39.88  ? 23  VAL B CG1 1 
ATOM   854  C CG2 . VAL B 1 28 ? -0.929  24.725 6.073   1.00 38.37  ? 23  VAL B CG2 1 
ATOM   855  N N   . PHE B 1 29 ? -3.508  20.857 7.312   1.00 46.62  ? 24  PHE B N   1 
ATOM   856  C CA  . PHE B 1 29 ? -4.540  19.828 7.193   1.00 53.46  ? 24  PHE B CA  1 
ATOM   857  C C   . PHE B 1 29 ? -5.810  20.117 8.046   1.00 55.05  ? 24  PHE B C   1 
ATOM   858  O O   . PHE B 1 29 ? -6.913  19.933 7.548   1.00 60.87  ? 24  PHE B O   1 
ATOM   859  C CB  . PHE B 1 29 ? -3.978  18.392 7.364   1.00 61.09  ? 24  PHE B CB  1 
ATOM   860  C CG  . PHE B 1 29 ? -3.665  18.012 8.793   1.00 67.71  ? 24  PHE B CG  1 
ATOM   861  C CD1 . PHE B 1 29 ? -4.682  17.648 9.680   1.00 68.15  ? 24  PHE B CD1 1 
ATOM   862  C CD2 . PHE B 1 29 ? -2.351  18.007 9.254   1.00 73.11  ? 24  PHE B CD2 1 
ATOM   863  C CE1 . PHE B 1 29 ? -4.398  17.302 10.993  1.00 68.94  ? 24  PHE B CE1 1 
ATOM   864  C CE2 . PHE B 1 29 ? -2.057  17.656 10.574  1.00 69.84  ? 24  PHE B CE2 1 
ATOM   865  C CZ  . PHE B 1 29 ? -3.083  17.302 11.438  1.00 69.49  ? 24  PHE B CZ  1 
ATOM   866  N N   . SER B 1 30 ? -5.664  20.582 9.294   1.00 53.39  ? 25  SER B N   1 
ATOM   867  C CA  . SER B 1 30 ? -6.817  20.998 10.124  1.00 52.78  ? 25  SER B CA  1 
ATOM   868  C C   . SER B 1 30 ? -7.701  22.003 9.393   1.00 51.04  ? 25  SER B C   1 
ATOM   869  O O   . SER B 1 30 ? -8.926  21.817 9.256   1.00 47.97  ? 25  SER B O   1 
ATOM   870  C CB  . SER B 1 30 ? -6.367  21.631 11.446  1.00 58.54  ? 25  SER B CB  1 
ATOM   871  O OG  . SER B 1 30 ? -5.670  20.712 12.272  1.00 68.15  ? 25  SER B OG  1 
ATOM   872  N N   . LEU B 1 31 ? -7.076  23.075 8.923   1.00 48.69  ? 26  LEU B N   1 
ATOM   873  C CA  . LEU B 1 31 ? -7.756  23.965 7.996   1.00 52.00  ? 26  LEU B CA  1 
ATOM   874  C C   . LEU B 1 31 ? -8.652  23.234 6.983   1.00 51.26  ? 26  LEU B C   1 
ATOM   875  O O   . LEU B 1 31 ? -9.815  23.607 6.812   1.00 50.13  ? 26  LEU B O   1 
ATOM   876  C CB  . LEU B 1 31 ? -6.767  24.864 7.251   1.00 51.25  ? 26  LEU B CB  1 
ATOM   877  C CG  . LEU B 1 31 ? -7.403  25.985 6.410   1.00 53.85  ? 26  LEU B CG  1 
ATOM   878  C CD1 . LEU B 1 31 ? -8.586  26.642 7.119   1.00 55.33  ? 26  LEU B CD1 1 
ATOM   879  C CD2 . LEU B 1 31 ? -6.381  27.048 6.045   1.00 53.77  ? 26  LEU B CD2 1 
ATOM   880  N N   . ILE B 1 32 ? -8.128  22.210 6.312   1.00 47.39  ? 27  ILE B N   1 
ATOM   881  C CA  . ILE B 1 32 ? -8.913  21.589 5.256   1.00 50.11  ? 27  ILE B CA  1 
ATOM   882  C C   . ILE B 1 32 ? -10.165 20.902 5.812   1.00 49.82  ? 27  ILE B C   1 
ATOM   883  O O   . ILE B 1 32 ? -11.267 21.035 5.251   1.00 47.30  ? 27  ILE B O   1 
ATOM   884  C CB  . ILE B 1 32 ? -8.075  20.679 4.340   1.00 53.49  ? 27  ILE B CB  1 
ATOM   885  C CG1 . ILE B 1 32 ? -6.811  21.406 3.870   1.00 51.54  ? 27  ILE B CG1 1 
ATOM   886  C CG2 . ILE B 1 32 ? -8.875  20.312 3.100   1.00 55.58  ? 27  ILE B CG2 1 
ATOM   887  C CD1 . ILE B 1 32 ? -5.821  20.518 3.133   1.00 51.02  ? 27  ILE B CD1 1 
ATOM   888  N N   . GLN B 1 33 ? -10.001 20.212 6.937   1.00 50.29  ? 28  GLN B N   1 
ATOM   889  C CA  . GLN B 1 33 ? -11.137 19.612 7.644   1.00 53.54  ? 28  GLN B CA  1 
ATOM   890  C C   . GLN B 1 33 ? -12.214 20.652 7.940   1.00 53.92  ? 28  GLN B C   1 
ATOM   891  O O   . GLN B 1 33 ? -13.384 20.458 7.575   1.00 56.24  ? 28  GLN B O   1 
ATOM   892  C CB  . GLN B 1 33 ? -10.683 18.919 8.924   1.00 53.99  ? 28  GLN B CB  1 
ATOM   893  C CG  . GLN B 1 33 ? -9.861  17.662 8.654   1.00 62.45  ? 28  GLN B CG  1 
ATOM   894  C CD  . GLN B 1 33 ? -9.010  17.213 9.845   1.00 68.95  ? 28  GLN B CD  1 
ATOM   895  O OE1 . GLN B 1 33 ? -8.765  16.017 10.019  1.00 73.54  ? 28  GLN B OE1 1 
ATOM   896  N NE2 . GLN B 1 33 ? -8.558  18.165 10.668  1.00 69.24  ? 28  GLN B NE2 1 
ATOM   897  N N   . GLN B 1 34 ? -11.803 21.758 8.563   1.00 49.27  ? 29  GLN B N   1 
ATOM   898  C CA  . GLN B 1 34 ? -12.675 22.904 8.801   1.00 47.21  ? 29  GLN B CA  1 
ATOM   899  C C   . GLN B 1 34 ? -13.418 23.415 7.580   1.00 46.87  ? 29  GLN B C   1 
ATOM   900  O O   . GLN B 1 34 ? -14.617 23.695 7.657   1.00 46.19  ? 29  GLN B O   1 
ATOM   901  C CB  . GLN B 1 34 ? -11.861 24.052 9.364   1.00 48.78  ? 29  GLN B CB  1 
ATOM   902  C CG  . GLN B 1 34 ? -11.271 23.737 10.706  1.00 52.00  ? 29  GLN B CG  1 
ATOM   903  C CD  . GLN B 1 34 ? -12.301 23.109 11.584  1.00 53.18  ? 29  GLN B CD  1 
ATOM   904  O OE1 . GLN B 1 34 ? -13.310 23.729 11.908  1.00 55.74  ? 29  GLN B OE1 1 
ATOM   905  N NE2 . GLN B 1 34 ? -12.078 21.861 11.947  1.00 55.93  ? 29  GLN B NE2 1 
ATOM   906  N N   . ALA B 1 35 ? -12.701 23.536 6.461   1.00 48.52  ? 30  ALA B N   1 
ATOM   907  C CA  . ALA B 1 35 ? -13.227 24.182 5.245   1.00 48.85  ? 30  ALA B CA  1 
ATOM   908  C C   . ALA B 1 35 ? -14.175 23.283 4.470   1.00 50.28  ? 30  ALA B C   1 
ATOM   909  O O   . ALA B 1 35 ? -15.203 23.743 3.966   1.00 48.96  ? 30  ALA B O   1 
ATOM   910  C CB  . ALA B 1 35 ? -12.094 24.647 4.344   1.00 46.95  ? 30  ALA B CB  1 
ATOM   911  N N   . VAL B 1 36 ? -13.819 22.006 4.364   1.00 50.86  ? 31  VAL B N   1 
ATOM   912  C CA  . VAL B 1 36 ? -14.678 21.047 3.703   1.00 53.28  ? 31  VAL B CA  1 
ATOM   913  C C   . VAL B 1 36 ? -16.039 21.153 4.375   1.00 54.58  ? 31  VAL B C   1 
ATOM   914  O O   . VAL B 1 36 ? -17.036 21.475 3.715   1.00 57.72  ? 31  VAL B O   1 
ATOM   915  C CB  . VAL B 1 36 ? -14.142 19.606 3.839   1.00 54.55  ? 31  VAL B CB  1 
ATOM   916  C CG1 . VAL B 1 36 ? -15.203 18.605 3.423   1.00 50.40  ? 31  VAL B CG1 1 
ATOM   917  C CG2 . VAL B 1 36 ? -12.886 19.415 3.003   1.00 55.69  ? 31  VAL B CG2 1 
ATOM   918  N N   . THR B 1 37 ? -16.038 20.922 5.693   1.00 51.43  ? 32  THR B N   1 
ATOM   919  C CA  . THR B 1 37 ? -17.223 20.875 6.551   1.00 47.27  ? 32  THR B CA  1 
ATOM   920  C C   . THR B 1 37 ? -18.128 22.056 6.319   1.00 48.00  ? 32  THR B C   1 
ATOM   921  O O   . THR B 1 37 ? -19.340 21.905 6.093   1.00 48.45  ? 32  THR B O   1 
ATOM   922  C CB  . THR B 1 37 ? -16.776 20.905 8.012   1.00 47.18  ? 32  THR B CB  1 
ATOM   923  O OG1 . THR B 1 37 ? -16.017 19.726 8.277   1.00 49.36  ? 32  THR B OG1 1 
ATOM   924  C CG2 . THR B 1 37 ? -17.969 21.017 8.980   1.00 46.76  ? 32  THR B CG2 1 
ATOM   925  N N   . ARG B 1 38 ? -17.526 23.236 6.389   1.00 44.60  ? 33  ARG B N   1 
ATOM   926  C CA  . ARG B 1 38 ? -18.248 24.455 6.158   1.00 45.25  ? 33  ARG B CA  1 
ATOM   927  C C   . ARG B 1 38 ? -18.818 24.555 4.744   1.00 47.72  ? 33  ARG B C   1 
ATOM   928  O O   . ARG B 1 38 ? -19.975 24.972 4.585   1.00 51.80  ? 33  ARG B O   1 
ATOM   929  C CB  . ARG B 1 38 ? -17.360 25.642 6.462   1.00 44.59  ? 33  ARG B CB  1 
ATOM   930  C CG  . ARG B 1 38 ? -17.084 25.774 7.928   1.00 44.56  ? 33  ARG B CG  1 
ATOM   931  C CD  . ARG B 1 38 ? -16.790 27.222 8.267   1.00 48.35  ? 33  ARG B CD  1 
ATOM   932  N NE  . ARG B 1 38 ? -16.775 27.436 9.717   1.00 46.45  ? 33  ARG B NE  1 
ATOM   933  C CZ  . ARG B 1 38 ? -15.970 26.807 10.569  1.00 40.79  ? 33  ARG B CZ  1 
ATOM   934  N NH1 . ARG B 1 38 ? -15.102 25.908 10.148  1.00 39.41  ? 33  ARG B NH1 1 
ATOM   935  N NH2 . ARG B 1 38 ? -16.050 27.068 11.853  1.00 40.22  ? 33  ARG B NH2 1 
ATOM   936  N N   . TYR B 1 39 ? -18.015 24.172 3.742   1.00 44.55  ? 34  TYR B N   1 
ATOM   937  C CA  . TYR B 1 39 ? -18.425 24.210 2.345   1.00 45.81  ? 34  TYR B CA  1 
ATOM   938  C C   . TYR B 1 39 ? -19.565 23.253 2.050   1.00 50.11  ? 34  TYR B C   1 
ATOM   939  O O   . TYR B 1 39 ? -20.454 23.580 1.263   1.00 52.19  ? 34  TYR B O   1 
ATOM   940  C CB  . TYR B 1 39 ? -17.259 23.867 1.435   1.00 46.96  ? 34  TYR B CB  1 
ATOM   941  C CG  . TYR B 1 39 ? -17.633 23.574 -0.020  1.00 46.70  ? 34  TYR B CG  1 
ATOM   942  C CD1 . TYR B 1 39 ? -18.121 24.575 -0.851  1.00 48.79  ? 34  TYR B CD1 1 
ATOM   943  C CD2 . TYR B 1 39 ? -17.461 22.301 -0.564  1.00 46.96  ? 34  TYR B CD2 1 
ATOM   944  C CE1 . TYR B 1 39 ? -18.443 24.317 -2.176  1.00 51.87  ? 34  TYR B CE1 1 
ATOM   945  C CE2 . TYR B 1 39 ? -17.790 22.032 -1.876  1.00 48.35  ? 34  TYR B CE2 1 
ATOM   946  C CZ  . TYR B 1 39 ? -18.284 23.043 -2.683  1.00 51.46  ? 34  TYR B CZ  1 
ATOM   947  O OH  . TYR B 1 39 ? -18.608 22.787 -4.008  1.00 55.94  ? 34  TYR B OH  1 
ATOM   948  N N   . ARG B 1 40 ? -19.521 22.064 2.651   1.00 52.89  ? 35  ARG B N   1 
ATOM   949  C CA  . ARG B 1 40 ? -20.651 21.131 2.596   1.00 55.65  ? 35  ARG B CA  1 
ATOM   950  C C   . ARG B 1 40 ? -21.944 21.844 2.993   1.00 54.02  ? 35  ARG B C   1 
ATOM   951  O O   . ARG B 1 40 ? -22.859 21.955 2.177   1.00 59.10  ? 35  ARG B O   1 
ATOM   952  C CB  . ARG B 1 40 ? -20.412 19.885 3.471   1.00 60.58  ? 35  ARG B CB  1 
ATOM   953  C CG  . ARG B 1 40 ? -19.410 18.915 2.873   1.00 61.36  ? 35  ARG B CG  1 
ATOM   954  C CD  . ARG B 1 40 ? -19.475 17.544 3.521   1.00 69.06  ? 35  ARG B CD  1 
ATOM   955  N NE  . ARG B 1 40 ? -18.799 16.539 2.685   1.00 77.80  ? 35  ARG B NE  1 
ATOM   956  C CZ  . ARG B 1 40 ? -19.374 15.819 1.710   1.00 79.90  ? 35  ARG B CZ  1 
ATOM   957  N NH1 . ARG B 1 40 ? -20.665 15.945 1.407   1.00 77.39  ? 35  ARG B NH1 1 
ATOM   958  N NH2 . ARG B 1 40 ? -18.644 14.948 1.028   1.00 82.92  ? 35  ARG B NH2 1 
ATOM   959  N N   . LYS B 1 41 ? -22.000 22.353 4.219   1.00 48.52  ? 36  LYS B N   1 
ATOM   960  C CA  . LYS B 1 41 ? -23.134 23.150 4.668   1.00 49.85  ? 36  LYS B CA  1 
ATOM   961  C C   . LYS B 1 41 ? -23.611 24.241 3.681   1.00 49.03  ? 36  LYS B C   1 
ATOM   962  O O   . LYS B 1 41 ? -24.788 24.322 3.352   1.00 48.53  ? 36  LYS B O   1 
ATOM   963  C CB  . LYS B 1 41 ? -22.789 23.799 5.993   1.00 49.59  ? 36  LYS B CB  1 
ATOM   964  C CG  . LYS B 1 41 ? -22.586 22.822 7.113   1.00 45.37  ? 36  LYS B CG  1 
ATOM   965  C CD  . LYS B 1 41 ? -22.551 23.602 8.394   1.00 47.86  ? 36  LYS B CD  1 
ATOM   966  C CE  . LYS B 1 41 ? -21.975 22.747 9.492   1.00 54.54  ? 36  LYS B CE  1 
ATOM   967  N NZ  . LYS B 1 41 ? -20.811 23.406 10.151  1.00 60.78  ? 36  LYS B NZ  1 
ATOM   968  N N   . ALA B 1 42 ? -22.689 25.080 3.229   1.00 50.61  ? 37  ALA B N   1 
ATOM   969  C CA  . ALA B 1 42 ? -23.010 26.235 2.389   1.00 54.28  ? 37  ALA B CA  1 
ATOM   970  C C   . ALA B 1 42 ? -23.650 25.912 1.040   1.00 55.43  ? 37  ALA B C   1 
ATOM   971  O O   . ALA B 1 42 ? -24.380 26.745 0.508   1.00 55.10  ? 37  ALA B O   1 
ATOM   972  C CB  . ALA B 1 42 ? -21.761 27.066 2.161   1.00 56.65  ? 37  ALA B CB  1 
ATOM   973  N N   . VAL B 1 43 ? -23.342 24.742 0.477   1.00 55.12  ? 38  VAL B N   1 
ATOM   974  C CA  . VAL B 1 43 ? -23.974 24.293 -0.762  1.00 59.47  ? 38  VAL B CA  1 
ATOM   975  C C   . VAL B 1 43 ? -24.858 23.041 -0.611  1.00 70.96  ? 38  VAL B C   1 
ATOM   976  O O   . VAL B 1 43 ? -25.625 22.724 -1.539  1.00 72.07  ? 38  VAL B O   1 
ATOM   977  C CB  . VAL B 1 43 ? -22.963 24.074 -1.920  1.00 60.17  ? 38  VAL B CB  1 
ATOM   978  C CG1 . VAL B 1 43 ? -22.388 25.398 -2.418  1.00 60.57  ? 38  VAL B CG1 1 
ATOM   979  C CG2 . VAL B 1 43 ? -21.877 23.073 -1.542  1.00 60.36  ? 38  VAL B CG2 1 
ATOM   980  N N   . ALA B 1 44 ? -24.748 22.349 0.541   1.00 76.90  ? 39  ALA B N   1 
ATOM   981  C CA  . ALA B 1 44 ? -25.471 21.083 0.859   1.00 78.17  ? 39  ALA B CA  1 
ATOM   982  C C   . ALA B 1 44 ? -25.833 20.288 -0.399  1.00 89.21  ? 39  ALA B C   1 
ATOM   983  O O   . ALA B 1 44 ? -26.997 20.261 -0.826  1.00 81.59  ? 39  ALA B O   1 
ATOM   984  C CB  . ALA B 1 44 ? -26.705 21.341 1.731   1.00 67.03  ? 39  ALA B CB  1 
ATOM   985  N N   . LYS B 1 45 ? -24.817 19.654 -0.990  1.00 105.21 ? 40  LYS B N   1 
ATOM   986  C CA  . LYS B 1 45 ? -24.941 19.020 -2.315  1.00 118.67 ? 40  LYS B CA  1 
ATOM   987  C C   . LYS B 1 45 ? -25.822 17.763 -2.317  1.00 122.95 ? 40  LYS B C   1 
ATOM   988  O O   . LYS B 1 45 ? -26.718 17.632 -3.160  1.00 122.77 ? 40  LYS B O   1 
ATOM   989  C CB  . LYS B 1 45 ? -23.554 18.708 -2.927  1.00 128.86 ? 40  LYS B CB  1 
ATOM   990  C CG  . LYS B 1 45 ? -22.654 19.904 -3.283  1.00 128.99 ? 40  LYS B CG  1 
ATOM   991  C CD  . LYS B 1 45 ? -22.986 20.554 -4.629  1.00 122.83 ? 40  LYS B CD  1 
ATOM   992  C CE  . LYS B 1 45 ? -23.965 21.708 -4.446  1.00 119.60 ? 40  LYS B CE  1 
ATOM   993  N NZ  . LYS B 1 45 ? -24.487 22.239 -5.751  1.00 129.68 ? 40  LYS B NZ  1 
ATOM   994  N N   . ASP B 1 46 ? -25.567 16.854 -1.367  1.00 131.64 ? 41  ASP B N   1 
ATOM   995  C CA  . ASP B 1 46 ? -26.246 15.547 -1.303  1.00 125.17 ? 41  ASP B CA  1 
ATOM   996  C C   . ASP B 1 46 ? -26.005 14.843 0.048   1.00 125.17 ? 41  ASP B C   1 
ATOM   997  O O   . ASP B 1 46 ? -25.004 15.118 0.738   1.00 111.45 ? 41  ASP B O   1 
ATOM   998  C CB  . ASP B 1 46 ? -25.730 14.646 -2.442  1.00 116.14 ? 41  ASP B CB  1 
ATOM   999  C CG  . ASP B 1 46 ? -26.803 13.748 -3.047  1.00 106.83 ? 41  ASP B CG  1 
ATOM   1000 O OD1 . ASP B 1 46 ? -27.386 12.902 -2.336  1.00 101.07 ? 41  ASP B OD1 1 
ATOM   1001 O OD2 . ASP B 1 46 ? -27.016 13.857 -4.273  1.00 99.93  ? 41  ASP B OD2 1 
ATOM   1002 N N   . PRO B 1 47 ? -26.945 13.957 0.445   1.00 130.98 ? 42  PRO B N   1 
ATOM   1003 C CA  . PRO B 1 47 ? -26.633 12.878 1.399   1.00 128.92 ? 42  PRO B CA  1 
ATOM   1004 C C   . PRO B 1 47 ? -25.471 11.931 0.968   1.00 128.25 ? 42  PRO B C   1 
ATOM   1005 O O   . PRO B 1 47 ? -24.678 11.517 1.828   1.00 120.06 ? 42  PRO B O   1 
ATOM   1006 C CB  . PRO B 1 47 ? -27.964 12.122 1.502   1.00 117.55 ? 42  PRO B CB  1 
ATOM   1007 C CG  . PRO B 1 47 ? -28.997 13.191 1.306   1.00 116.23 ? 42  PRO B CG  1 
ATOM   1008 C CD  . PRO B 1 47 ? -28.405 14.186 0.339   1.00 120.65 ? 42  PRO B CD  1 
ATOM   1009 N N   . ASN B 1 48 ? -25.366 11.600 -0.329  1.00 125.18 ? 43  ASN B N   1 
ATOM   1010 C CA  . ASN B 1 48 ? -24.279 10.712 -0.824  1.00 120.97 ? 43  ASN B CA  1 
ATOM   1011 C C   . ASN B 1 48 ? -22.949 11.413 -1.213  1.00 118.71 ? 43  ASN B C   1 
ATOM   1012 O O   . ASN B 1 48 ? -21.873 10.914 -0.874  1.00 111.39 ? 43  ASN B O   1 
ATOM   1013 C CB  . ASN B 1 48 ? -24.764 9.670  -1.888  1.00 112.47 ? 43  ASN B CB  1 
ATOM   1014 C CG  . ASN B 1 48 ? -25.242 10.301 -3.210  1.00 106.00 ? 43  ASN B CG  1 
ATOM   1015 O OD1 . ASN B 1 48 ? -25.056 11.487 -3.471  1.00 105.47 ? 43  ASN B OD1 1 
ATOM   1016 N ND2 . ASN B 1 48 ? -25.844 9.479  -4.061  1.00 92.41  ? 43  ASN B ND2 1 
ATOM   1017 N N   . TYR B 1 49 ? -23.049 12.557 -1.902  1.00 118.70 ? 44  TYR B N   1 
ATOM   1018 C CA  . TYR B 1 49 ? -21.914 13.425 -2.311  1.00 116.77 ? 44  TYR B CA  1 
ATOM   1019 C C   . TYR B 1 49 ? -20.612 13.293 -1.475  1.00 115.86 ? 44  TYR B C   1 
ATOM   1020 O O   . TYR B 1 49 ? -20.609 13.479 -0.246  1.00 109.69 ? 44  TYR B O   1 
ATOM   1021 C CB  . TYR B 1 49 ? -22.402 14.891 -2.390  1.00 118.83 ? 44  TYR B CB  1 
ATOM   1022 C CG  . TYR B 1 49 ? -21.367 15.946 -2.726  1.00 120.61 ? 44  TYR B CG  1 
ATOM   1023 C CD1 . TYR B 1 49 ? -20.913 16.113 -4.036  1.00 122.31 ? 44  TYR B CD1 1 
ATOM   1024 C CD2 . TYR B 1 49 ? -20.868 16.806 -1.730  1.00 123.92 ? 44  TYR B CD2 1 
ATOM   1025 C CE1 . TYR B 1 49 ? -19.976 17.084 -4.345  1.00 126.78 ? 44  TYR B CE1 1 
ATOM   1026 C CE2 . TYR B 1 49 ? -19.927 17.778 -2.025  1.00 126.99 ? 44  TYR B CE2 1 
ATOM   1027 C CZ  . TYR B 1 49 ? -19.485 17.911 -3.335  1.00 135.28 ? 44  TYR B CZ  1 
ATOM   1028 O OH  . TYR B 1 49 ? -18.551 18.872 -3.638  1.00 134.85 ? 44  TYR B OH  1 
ATOM   1029 N N   . TRP B 1 50 ? -19.523 12.991 -2.190  1.00 106.80 ? 45  TRP B N   1 
ATOM   1030 C CA  . TRP B 1 50 ? -18.185 12.696 -1.661  1.00 97.71  ? 45  TRP B CA  1 
ATOM   1031 C C   . TRP B 1 50 ? -17.233 13.801 -2.065  1.00 94.26  ? 45  TRP B C   1 
ATOM   1032 O O   . TRP B 1 50 ? -17.380 14.384 -3.160  1.00 90.21  ? 45  TRP B O   1 
ATOM   1033 C CB  . TRP B 1 50 ? -17.717 11.430 -2.351  1.00 106.80 ? 45  TRP B CB  1 
ATOM   1034 C CG  . TRP B 1 50 ? -17.631 11.676 -3.844  1.00 115.99 ? 45  TRP B CG  1 
ATOM   1035 C CD1 . TRP B 1 50 ? -18.691 11.851 -4.756  1.00 113.99 ? 45  TRP B CD1 1 
ATOM   1036 C CD2 . TRP B 1 50 ? -16.411 11.881 -4.631  1.00 112.72 ? 45  TRP B CD2 1 
ATOM   1037 N NE1 . TRP B 1 50 ? -18.213 12.111 -6.017  1.00 114.42 ? 45  TRP B NE1 1 
ATOM   1038 C CE2 . TRP B 1 50 ? -16.853 12.140 -6.015  1.00 116.91 ? 45  TRP B CE2 1 
ATOM   1039 C CE3 . TRP B 1 50 ? -15.048 11.861 -4.344  1.00 102.62 ? 45  TRP B CE3 1 
ATOM   1040 C CZ2 . TRP B 1 50 ? -15.945 12.355 -7.044  1.00 117.38 ? 45  TRP B CZ2 1 
ATOM   1041 C CZ3 . TRP B 1 50 ? -14.146 12.083 -5.388  1.00 109.30 ? 45  TRP B CZ3 1 
ATOM   1042 C CH2 . TRP B 1 50 ? -14.583 12.323 -6.705  1.00 115.86 ? 45  TRP B CH2 1 
ATOM   1043 N N   . ILE B 1 51 ? -16.224 14.092 -1.239  1.00 85.77  ? 46  ILE B N   1 
ATOM   1044 C CA  . ILE B 1 51 ? -15.245 15.138 -1.621  1.00 81.43  ? 46  ILE B CA  1 
ATOM   1045 C C   . ILE B 1 51 ? -13.782 14.892 -1.217  1.00 76.94  ? 46  ILE B C   1 
ATOM   1046 O O   . ILE B 1 51 ? -13.503 14.536 -0.065  1.00 68.02  ? 46  ILE B O   1 
ATOM   1047 C CB  . ILE B 1 51 ? -15.690 16.538 -1.149  1.00 76.87  ? 46  ILE B CB  1 
ATOM   1048 C CG1 . ILE B 1 51 ? -14.978 17.631 -1.955  1.00 78.83  ? 46  ILE B CG1 1 
ATOM   1049 C CG2 . ILE B 1 51 ? -15.460 16.690 0.344   1.00 75.44  ? 46  ILE B CG2 1 
ATOM   1050 C CD1 . ILE B 1 51 ? -15.602 19.002 -1.810  1.00 80.41  ? 46  ILE B CD1 1 
ATOM   1051 N N   . GLN B 1 52 ? -12.865 15.089 -2.177  1.00 74.52  ? 47  GLN B N   1 
ATOM   1052 C CA  . GLN B 1 52 ? -11.425 15.065 -1.884  1.00 73.17  ? 47  GLN B CA  1 
ATOM   1053 C C   . GLN B 1 52 ? -10.694 16.296 -2.339  1.00 68.78  ? 47  GLN B C   1 
ATOM   1054 O O   . GLN B 1 52 ? -10.749 16.675 -3.510  1.00 65.83  ? 47  GLN B O   1 
ATOM   1055 C CB  . GLN B 1 52 ? -10.709 13.818 -2.418  1.00 78.29  ? 47  GLN B CB  1 
ATOM   1056 C CG  . GLN B 1 52 ? -10.205 12.904 -1.302  1.00 79.31  ? 47  GLN B CG  1 
ATOM   1057 C CD  . GLN B 1 52 ? -8.790  12.404 -1.536  1.00 80.40  ? 47  GLN B CD  1 
ATOM   1058 O OE1 . GLN B 1 52 ? -7.845  12.845 -0.878  1.00 82.15  ? 47  GLN B OE1 1 
ATOM   1059 N NE2 . GLN B 1 52 ? -8.634  11.487 -2.481  1.00 78.32  ? 47  GLN B NE2 1 
ATOM   1060 N N   . VAL B 1 53 ? -9.998  16.887 -1.371  1.00 67.11  ? 48  VAL B N   1 
ATOM   1061 C CA  . VAL B 1 53 ? -9.192  18.090 -1.546  1.00 65.17  ? 48  VAL B CA  1 
ATOM   1062 C C   . VAL B 1 53 ? -7.764  17.639 -1.643  1.00 61.15  ? 48  VAL B C   1 
ATOM   1063 O O   . VAL B 1 53 ? -7.232  17.046 -0.701  1.00 58.52  ? 48  VAL B O   1 
ATOM   1064 C CB  . VAL B 1 53 ? -9.281  19.021 -0.313  1.00 62.57  ? 48  VAL B CB  1 
ATOM   1065 C CG1 . VAL B 1 53 ? -8.266  20.142 -0.409  1.00 59.77  ? 48  VAL B CG1 1 
ATOM   1066 C CG2 . VAL B 1 53 ? -10.678 19.598 -0.168  1.00 65.06  ? 48  VAL B CG2 1 
ATOM   1067 N N   . HIS B 1 54 ? -7.134  17.941 -2.766  1.00 59.50  ? 49  HIS B N   1 
ATOM   1068 C CA  . HIS B 1 54 ? -5.753  17.519 -2.969  1.00 64.73  ? 49  HIS B CA  1 
ATOM   1069 C C   . HIS B 1 54 ? -4.792  18.468 -2.338  1.00 66.57  ? 49  HIS B C   1 
ATOM   1070 O O   . HIS B 1 54 ? -3.989  18.066 -1.499  1.00 68.04  ? 49  HIS B O   1 
ATOM   1071 C CB  . HIS B 1 54 ? -5.489  17.199 -4.438  1.00 63.24  ? 49  HIS B CB  1 
ATOM   1072 C CG  . HIS B 1 54 ? -6.429  16.138 -4.943  1.00 68.67  ? 49  HIS B CG  1 
ATOM   1073 N ND1 . HIS B 1 54 ? -7.488  16.417 -5.745  1.00 69.10  ? 49  HIS B ND1 1 
ATOM   1074 C CD2 . HIS B 1 54 ? -6.530  14.783 -4.609  1.00 65.89  ? 49  HIS B CD2 1 
ATOM   1075 C CE1 . HIS B 1 54 ? -8.196  15.289 -5.952  1.00 69.96  ? 49  HIS B CE1 1 
ATOM   1076 N NE2 . HIS B 1 54 ? -7.610  14.290 -5.255  1.00 71.66  ? 49  HIS B NE2 1 
ATOM   1077 N N   . ARG B 1 55 ? -4.910  19.749 -2.660  1.00 68.34  ? 50  ARG B N   1 
ATOM   1078 C CA  . ARG B 1 55 ? -4.014  20.728 -2.080  1.00 61.00  ? 50  ARG B CA  1 
ATOM   1079 C C   . ARG B 1 55 ? -4.690  22.063 -1.853  1.00 58.75  ? 50  ARG B C   1 
ATOM   1080 O O   . ARG B 1 55 ? -5.733  22.369 -2.469  1.00 56.33  ? 50  ARG B O   1 
ATOM   1081 C CB  . ARG B 1 55 ? -2.780  20.897 -2.973  1.00 63.07  ? 50  ARG B CB  1 
ATOM   1082 C CG  . ARG B 1 55 ? -3.101  21.190 -4.425  1.00 62.75  ? 50  ARG B CG  1 
ATOM   1083 C CD  . ARG B 1 55 ? -1.860  21.054 -5.279  1.00 63.44  ? 50  ARG B CD  1 
ATOM   1084 N NE  . ARG B 1 55 ? -2.066  21.731 -6.553  1.00 67.13  ? 50  ARG B NE  1 
ATOM   1085 C CZ  . ARG B 1 55 ? -2.443  21.122 -7.671  1.00 67.73  ? 50  ARG B CZ  1 
ATOM   1086 N NH1 . ARG B 1 55 ? -2.637  19.813 -7.666  1.00 68.53  ? 50  ARG B NH1 1 
ATOM   1087 N NH2 . ARG B 1 55 ? -2.631  21.819 -8.787  1.00 67.80  ? 50  ARG B NH2 1 
ATOM   1088 N N   . LEU B 1 56 ? -4.063  22.854 -0.978  1.00 53.14  ? 51  LEU B N   1 
ATOM   1089 C CA  . LEU B 1 56 ? -4.461  24.230 -0.731  1.00 51.01  ? 51  LEU B CA  1 
ATOM   1090 C C   . LEU B 1 56 ? -3.467  25.256 -1.320  1.00 48.26  ? 51  LEU B C   1 
ATOM   1091 O O   . LEU B 1 56 ? -2.292  25.229 -0.989  1.00 51.16  ? 51  LEU B O   1 
ATOM   1092 C CB  . LEU B 1 56 ? -4.627  24.410 0.768   1.00 51.85  ? 51  LEU B CB  1 
ATOM   1093 C CG  . LEU B 1 56 ? -5.457  25.593 1.242   1.00 54.98  ? 51  LEU B CG  1 
ATOM   1094 C CD1 . LEU B 1 56 ? -6.795  25.646 0.516   1.00 58.02  ? 51  LEU B CD1 1 
ATOM   1095 C CD2 . LEU B 1 56 ? -5.635  25.471 2.745   1.00 54.62  ? 51  LEU B CD2 1 
ATOM   1096 N N   . GLU B 1 57 ? -3.930  26.145 -2.198  1.00 45.22  ? 52  GLU B N   1 
ATOM   1097 C CA  . GLU B 1 57 ? -3.052  27.155 -2.803  1.00 44.63  ? 52  GLU B CA  1 
ATOM   1098 C C   . GLU B 1 57 ? -3.357  28.604 -2.372  1.00 49.45  ? 52  GLU B C   1 
ATOM   1099 O O   . GLU B 1 57 ? -4.452  28.920 -1.823  1.00 45.82  ? 52  GLU B O   1 
ATOM   1100 C CB  . GLU B 1 57 ? -3.048  27.044 -4.332  1.00 42.27  ? 52  GLU B CB  1 
ATOM   1101 C CG  . GLU B 1 57 ? -2.496  25.706 -4.820  1.00 45.80  ? 52  GLU B CG  1 
ATOM   1102 C CD  . GLU B 1 57 ? -2.481  25.500 -6.353  1.00 46.78  ? 52  GLU B CD  1 
ATOM   1103 O OE1 . GLU B 1 57 ? -2.737  26.435 -7.174  1.00 45.37  ? 52  GLU B OE1 1 
ATOM   1104 O OE2 . GLU B 1 57 ? -2.188  24.350 -6.742  1.00 44.02  ? 52  GLU B OE2 1 
ATOM   1105 N N   . HIS B 1 58 ? -2.362  29.470 -2.602  1.00 48.23  ? 53  HIS B N   1 
ATOM   1106 C CA  . HIS B 1 58 ? -2.556  30.905 -2.563  1.00 46.10  ? 53  HIS B CA  1 
ATOM   1107 C C   . HIS B 1 58 ? -2.956  31.261 -3.960  1.00 45.56  ? 53  HIS B C   1 
ATOM   1108 O O   . HIS B 1 58 ? -2.980  30.388 -4.843  1.00 44.83  ? 53  HIS B O   1 
ATOM   1109 C CB  . HIS B 1 58 ? -1.251  31.627 -2.210  1.00 48.92  ? 53  HIS B CB  1 
ATOM   1110 C CG  . HIS B 1 58 ? -1.003  31.795 -0.716  1.00 52.33  ? 53  HIS B CG  1 
ATOM   1111 N ND1 . HIS B 1 58 ? -0.174  30.983 -0.014  1.00 53.49  ? 53  HIS B ND1 1 
ATOM   1112 C CD2 . HIS B 1 58 ? -1.478  32.741 0.194   1.00 51.25  ? 53  HIS B CD2 1 
ATOM   1113 C CE1 . HIS B 1 58 ? -0.133  31.380 1.274   1.00 49.51  ? 53  HIS B CE1 1 
ATOM   1114 N NE2 . HIS B 1 58 ? -0.932  32.453 1.403   1.00 50.40  ? 53  HIS B NE2 1 
ATOM   1115 N N   . GLY B 1 59 ? -3.275  32.539 -4.163  1.00 46.01  ? 54  GLY B N   1 
ATOM   1116 C CA  . GLY B 1 59 ? -3.494  33.130 -5.473  1.00 46.01  ? 54  GLY B CA  1 
ATOM   1117 C C   . GLY B 1 59 ? -2.445  32.762 -6.506  1.00 53.58  ? 54  GLY B C   1 
ATOM   1118 O O   . GLY B 1 59 ? -2.817  32.314 -7.598  1.00 57.86  ? 54  GLY B O   1 
ATOM   1119 N N   . ASP B 1 60 ? -1.145  32.918 -6.186  1.00 52.92  ? 55  ASP B N   1 
ATOM   1120 C CA  . ASP B 1 60 ? -0.090  32.642 -7.176  1.00 50.24  ? 55  ASP B CA  1 
ATOM   1121 C C   . ASP B 1 60 ? -0.083  31.225 -7.635  1.00 51.91  ? 55  ASP B C   1 
ATOM   1122 O O   . ASP B 1 60 ? 0.328   30.944 -8.752  1.00 61.30  ? 55  ASP B O   1 
ATOM   1123 C CB  . ASP B 1 60 ? 1.338   32.911 -6.696  1.00 52.89  ? 55  ASP B CB  1 
ATOM   1124 C CG  . ASP B 1 60 ? 1.430   33.157 -5.240  1.00 54.58  ? 55  ASP B CG  1 
ATOM   1125 O OD1 . ASP B 1 60 ? 1.194   32.217 -4.436  1.00 54.96  ? 55  ASP B OD1 1 
ATOM   1126 O OD2 . ASP B 1 60 ? 1.809   34.308 -4.924  1.00 55.33  ? 55  ASP B OD2 1 
ATOM   1127 N N   . GLY B 1 61 ? -0.502  30.328 -6.759  1.00 50.28  ? 56  GLY B N   1 
ATOM   1128 C CA  . GLY B 1 61 ? -0.414  28.899 -7.018  1.00 50.75  ? 56  GLY B CA  1 
ATOM   1129 C C   . GLY B 1 61 ? 0.529   28.276 -6.012  1.00 51.25  ? 56  GLY B C   1 
ATOM   1130 O O   . GLY B 1 61 ? 0.935   27.133 -6.166  1.00 51.25  ? 56  GLY B O   1 
ATOM   1131 N N   . GLY B 1 62 ? 0.863   29.043 -4.971  1.00 52.40  ? 57  GLY B N   1 
ATOM   1132 C CA  . GLY B 1 62 ? 1.835   28.640 -3.973  1.00 44.83  ? 57  GLY B CA  1 
ATOM   1133 C C   . GLY B 1 62 ? 1.264   27.632 -3.017  1.00 43.13  ? 57  GLY B C   1 
ATOM   1134 O O   . GLY B 1 62 ? 0.495   27.995 -2.130  1.00 42.39  ? 57  GLY B O   1 
ATOM   1135 N N   . ILE B 1 63 ? 1.657   26.370 -3.207  1.00 42.21  ? 58  ILE B N   1 
ATOM   1136 C CA  . ILE B 1 63 ? 1.252   25.254 -2.351  1.00 42.24  ? 58  ILE B CA  1 
ATOM   1137 C C   . ILE B 1 63 ? 1.614   25.520 -0.903  1.00 41.17  ? 58  ILE B C   1 
ATOM   1138 O O   . ILE B 1 63 ? 2.693   26.042 -0.603  1.00 41.85  ? 58  ILE B O   1 
ATOM   1139 C CB  . ILE B 1 63 ? 1.947   23.923 -2.745  1.00 45.51  ? 58  ILE B CB  1 
ATOM   1140 C CG1 . ILE B 1 63 ? 1.818   23.627 -4.239  1.00 41.71  ? 58  ILE B CG1 1 
ATOM   1141 C CG2 . ILE B 1 63 ? 1.399   22.762 -1.918  1.00 43.81  ? 58  ILE B CG2 1 
ATOM   1142 C CD1 . ILE B 1 63 ? 0.403   23.342 -4.666  1.00 45.89  ? 58  ILE B CD1 1 
ATOM   1143 N N   . LEU B 1 64 ? 0.702   25.121 -0.022  1.00 39.78  ? 59  LEU B N   1 
ATOM   1144 C CA  . LEU B 1 64 ? 0.860   25.204 1.419   1.00 37.15  ? 59  LEU B CA  1 
ATOM   1145 C C   . LEU B 1 64 ? 1.025   23.765 1.915   1.00 39.78  ? 59  LEU B C   1 
ATOM   1146 O O   . LEU B 1 64 ? 0.128   22.945 1.774   1.00 42.21  ? 59  LEU B O   1 
ATOM   1147 C CB  . LEU B 1 64 ? -0.410  25.813 2.014   1.00 34.91  ? 59  LEU B CB  1 
ATOM   1148 C CG  . LEU B 1 64 ? -0.863  27.293 1.913   1.00 35.54  ? 59  LEU B CG  1 
ATOM   1149 C CD1 . LEU B 1 64 ? -1.376  27.785 0.555   1.00 34.24  ? 59  LEU B CD1 1 
ATOM   1150 C CD2 . LEU B 1 64 ? -1.956  27.508 2.951   1.00 35.41  ? 59  LEU B CD2 1 
ATOM   1151 N N   . ASP B 1 65 ? 2.163   23.431 2.494   1.00 44.01  ? 60  ASP B N   1 
ATOM   1152 C CA  . ASP B 1 65 ? 2.322   22.067 3.035   1.00 48.36  ? 60  ASP B CA  1 
ATOM   1153 C C   . ASP B 1 65 ? 1.440   21.660 4.239   1.00 46.37  ? 60  ASP B C   1 
ATOM   1154 O O   . ASP B 1 65 ? 1.380   22.355 5.244   1.00 44.36  ? 60  ASP B O   1 
ATOM   1155 C CB  . ASP B 1 65 ? 3.770   21.799 3.401   1.00 52.71  ? 60  ASP B CB  1 
ATOM   1156 C CG  . ASP B 1 65 ? 4.017   20.357 3.640   1.00 53.51  ? 60  ASP B CG  1 
ATOM   1157 O OD1 . ASP B 1 65 ? 3.706   19.908 4.771   1.00 53.32  ? 60  ASP B OD1 1 
ATOM   1158 O OD2 . ASP B 1 65 ? 4.478   19.692 2.676   1.00 52.88  ? 60  ASP B OD2 1 
ATOM   1159 N N   . LEU B 1 66 ? 0.840   20.483 4.150   1.00 44.70  ? 61  LEU B N   1 
ATOM   1160 C CA  . LEU B 1 66 ? -0.146  20.053 5.124   1.00 45.11  ? 61  LEU B CA  1 
ATOM   1161 C C   . LEU B 1 66 ? 0.308   20.067 6.574   1.00 43.10  ? 61  LEU B C   1 
ATOM   1162 O O   . LEU B 1 66 ? -0.515  20.245 7.481   1.00 42.13  ? 61  LEU B O   1 
ATOM   1163 C CB  . LEU B 1 66 ? -0.650  18.655 4.798   1.00 48.81  ? 61  LEU B CB  1 
ATOM   1164 C CG  . LEU B 1 66 ? -1.081  18.328 3.370   1.00 49.87  ? 61  LEU B CG  1 
ATOM   1165 C CD1 . LEU B 1 66 ? -0.819  16.841 3.139   1.00 51.80  ? 61  LEU B CD1 1 
ATOM   1166 C CD2 . LEU B 1 66 ? -2.530  18.720 3.080   1.00 45.23  ? 61  LEU B CD2 1 
ATOM   1167 N N   . ASP B 1 67 ? 1.594   19.874 6.811   1.00 41.09  ? 62  ASP B N   1 
ATOM   1168 C CA  . ASP B 1 67 ? 2.043   19.771 8.201   1.00 44.17  ? 62  ASP B CA  1 
ATOM   1169 C C   . ASP B 1 67 ? 2.606   21.068 8.768   1.00 45.22  ? 62  ASP B C   1 
ATOM   1170 O O   . ASP B 1 67 ? 3.085   21.096 9.904   1.00 41.83  ? 62  ASP B O   1 
ATOM   1171 C CB  . ASP B 1 67 ? 3.041   18.638 8.380   1.00 47.20  ? 62  ASP B CB  1 
ATOM   1172 C CG  . ASP B 1 67 ? 2.633   17.384 7.640   1.00 51.18  ? 62  ASP B CG  1 
ATOM   1173 O OD1 . ASP B 1 67 ? 1.541   16.837 7.936   1.00 52.14  ? 62  ASP B OD1 1 
ATOM   1174 O OD2 . ASP B 1 67 ? 3.416   16.951 6.757   1.00 50.65  ? 62  ASP B OD2 1 
ATOM   1175 N N   . ASP B 1 68 ? 2.517   22.134 7.969   1.00 47.29  ? 63  ASP B N   1 
ATOM   1176 C CA  . ASP B 1 68 ? 2.977   23.462 8.343   1.00 47.25  ? 63  ASP B CA  1 
ATOM   1177 C C   . ASP B 1 68 ? 1.896   24.169 9.118   1.00 46.46  ? 63  ASP B C   1 
ATOM   1178 O O   . ASP B 1 68 ? 0.714   23.965 8.850   1.00 42.30  ? 63  ASP B O   1 
ATOM   1179 C CB  . ASP B 1 68 ? 3.303   24.282 7.094   1.00 51.04  ? 63  ASP B CB  1 
ATOM   1180 C CG  . ASP B 1 68 ? 4.605   23.855 6.422   1.00 54.79  ? 63  ASP B CG  1 
ATOM   1181 O OD1 . ASP B 1 68 ? 5.344   23.023 7.009   1.00 53.89  ? 63  ASP B OD1 1 
ATOM   1182 O OD2 . ASP B 1 68 ? 4.889   24.370 5.306   1.00 55.18  ? 63  ASP B OD2 1 
ATOM   1183 N N   . ILE B 1 69 ? 2.325   24.985 10.085  1.00 50.67  ? 64  ILE B N   1 
ATOM   1184 C CA  . ILE B 1 69 ? 1.457   25.875 10.883  1.00 49.93  ? 64  ILE B CA  1 
ATOM   1185 C C   . ILE B 1 69 ? 0.848   26.892 9.921   1.00 54.24  ? 64  ILE B C   1 
ATOM   1186 O O   . ILE B 1 69 ? 1.526   27.374 8.996   1.00 54.96  ? 64  ILE B O   1 
ATOM   1187 C CB  . ILE B 1 69 ? 2.258   26.669 11.948  1.00 47.01  ? 64  ILE B CB  1 
ATOM   1188 C CG1 . ILE B 1 69 ? 3.309   25.806 12.664  1.00 45.23  ? 64  ILE B CG1 1 
ATOM   1189 C CG2 . ILE B 1 69 ? 1.340   27.429 12.890  1.00 46.59  ? 64  ILE B CG2 1 
ATOM   1190 C CD1 . ILE B 1 69 ? 2.820   24.457 13.130  1.00 48.37  ? 64  ILE B CD1 1 
ATOM   1191 N N   . LEU B 1 70 ? -0.422  27.225 10.123  1.00 52.60  ? 65  LEU B N   1 
ATOM   1192 C CA  . LEU B 1 70 ? -1.094  28.066 9.161   1.00 49.27  ? 65  LEU B CA  1 
ATOM   1193 C C   . LEU B 1 70 ? -0.524  29.497 9.194   1.00 48.79  ? 65  LEU B C   1 
ATOM   1194 O O   . LEU B 1 70 ? -0.005  29.980 8.188   1.00 47.19  ? 65  LEU B O   1 
ATOM   1195 C CB  . LEU B 1 70 ? -2.611  27.993 9.353   1.00 49.25  ? 65  LEU B CB  1 
ATOM   1196 C CG  . LEU B 1 70 ? -3.573  28.943 8.616   1.00 48.21  ? 65  LEU B CG  1 
ATOM   1197 C CD1 . LEU B 1 70 ? -3.495  28.906 7.101   1.00 42.19  ? 65  LEU B CD1 1 
ATOM   1198 C CD2 . LEU B 1 70 ? -4.975  28.620 9.081   1.00 47.32  ? 65  LEU B CD2 1 
ATOM   1199 N N   . CYS B 1 71 ? -0.582  30.151 10.350  1.00 47.91  ? 66  CYS B N   1 
ATOM   1200 C CA  . CYS B 1 71 ? -0.080  31.523 10.488  1.00 47.35  ? 66  CYS B CA  1 
ATOM   1201 C C   . CYS B 1 71 ? 1.376   31.674 10.034  1.00 49.01  ? 66  CYS B C   1 
ATOM   1202 O O   . CYS B 1 71 ? 1.866   32.804 9.892   1.00 49.12  ? 66  CYS B O   1 
ATOM   1203 C CB  . CYS B 1 71 ? -0.214  32.010 11.938  1.00 47.62  ? 66  CYS B CB  1 
ATOM   1204 S SG  . CYS B 1 71 ? 0.820   31.117 13.141  1.00 43.32  ? 66  CYS B SG  1 
ATOM   1205 N N   . ASP B 1 72 ? 2.060   30.543 9.831   1.00 45.93  ? 67  ASP B N   1 
ATOM   1206 C CA  . ASP B 1 72 ? 3.432   30.546 9.329   1.00 48.56  ? 67  ASP B CA  1 
ATOM   1207 C C   . ASP B 1 72 ? 3.566   30.612 7.807   1.00 50.57  ? 67  ASP B C   1 
ATOM   1208 O O   . ASP B 1 72 ? 4.618   30.950 7.279   1.00 48.94  ? 67  ASP B O   1 
ATOM   1209 C CB  . ASP B 1 72 ? 4.140   29.297 9.800   1.00 48.24  ? 67  ASP B CB  1 
ATOM   1210 C CG  . ASP B 1 72 ? 4.656   29.438 11.177  1.00 47.58  ? 67  ASP B CG  1 
ATOM   1211 O OD1 . ASP B 1 72 ? 4.789   30.598 11.608  1.00 48.62  ? 67  ASP B OD1 1 
ATOM   1212 O OD2 . ASP B 1 72 ? 4.941   28.410 11.817  1.00 45.36  ? 67  ASP B OD2 1 
ATOM   1213 N N   . VAL B 1 73 ? 2.481   30.276 7.128   1.00 50.68  ? 68  VAL B N   1 
ATOM   1214 C CA  . VAL B 1 73 ? 2.498   29.905 5.736   1.00 49.05  ? 68  VAL B CA  1 
ATOM   1215 C C   . VAL B 1 73 ? 1.446   30.773 5.035   1.00 50.94  ? 68  VAL B C   1 
ATOM   1216 O O   . VAL B 1 73 ? 1.416   30.875 3.799   1.00 54.21  ? 68  VAL B O   1 
ATOM   1217 C CB  . VAL B 1 73 ? 2.259   28.367 5.622   1.00 48.52  ? 68  VAL B CB  1 
ATOM   1218 C CG1 . VAL B 1 73 ? 1.367   27.987 4.472   1.00 51.03  ? 68  VAL B CG1 1 
ATOM   1219 C CG2 . VAL B 1 73 ? 3.574   27.630 5.482   1.00 49.15  ? 68  VAL B CG2 1 
ATOM   1220 N N   . ALA B 1 74 ? 0.613   31.435 5.835   1.00 44.87  ? 69  ALA B N   1 
ATOM   1221 C CA  . ALA B 1 74 ? -0.391  32.335 5.305   1.00 44.42  ? 69  ALA B CA  1 
ATOM   1222 C C   . ALA B 1 74 ? -0.614  33.511 6.255   1.00 44.67  ? 69  ALA B C   1 
ATOM   1223 O O   . ALA B 1 74 ? -0.128  33.491 7.369   1.00 46.84  ? 69  ALA B O   1 
ATOM   1224 C CB  . ALA B 1 74 ? -1.684  31.578 5.041   1.00 44.33  ? 69  ALA B CB  1 
ATOM   1225 N N   . ASP B 1 75 ? -1.331  34.536 5.807   1.00 47.83  ? 70  ASP B N   1 
ATOM   1226 C CA  . ASP B 1 75 ? -1.563  35.730 6.622   1.00 49.54  ? 70  ASP B CA  1 
ATOM   1227 C C   . ASP B 1 75 ? -3.015  35.787 7.016   1.00 48.13  ? 70  ASP B C   1 
ATOM   1228 O O   . ASP B 1 75 ? -3.888  35.287 6.294   1.00 41.45  ? 70  ASP B O   1 
ATOM   1229 C CB  . ASP B 1 75 ? -1.189  37.032 5.881   1.00 50.43  ? 70  ASP B CB  1 
ATOM   1230 C CG  . ASP B 1 75 ? 0.301   37.138 5.575   1.00 52.71  ? 70  ASP B CG  1 
ATOM   1231 O OD1 . ASP B 1 75 ? 1.116   36.943 6.497   1.00 55.28  ? 70  ASP B OD1 1 
ATOM   1232 O OD2 . ASP B 1 75 ? 0.667   37.414 4.407   1.00 55.09  ? 70  ASP B OD2 1 
ATOM   1233 N N   . ASP B 1 76 ? -3.262  36.404 8.169   1.00 48.49  ? 71  ASP B N   1 
ATOM   1234 C CA  . ASP B 1 76 ? -4.615  36.633 8.623   1.00 47.80  ? 71  ASP B CA  1 
ATOM   1235 C C   . ASP B 1 76 ? -5.407  37.279 7.511   1.00 46.85  ? 71  ASP B C   1 
ATOM   1236 O O   . ASP B 1 76 ? -4.897  38.146 6.797   1.00 46.10  ? 71  ASP B O   1 
ATOM   1237 C CB  . ASP B 1 76 ? -4.641  37.510 9.865   1.00 48.51  ? 71  ASP B CB  1 
ATOM   1238 C CG  . ASP B 1 76 ? -6.040  37.640 10.469  1.00 51.66  ? 71  ASP B CG  1 
ATOM   1239 O OD1 . ASP B 1 76 ? -6.980  36.926 10.018  1.00 51.18  ? 71  ASP B OD1 1 
ATOM   1240 O OD2 . ASP B 1 76 ? -6.187  38.457 11.411  1.00 50.25  ? 71  ASP B OD2 1 
ATOM   1241 N N   . LYS B 1 77 ? -6.639  36.806 7.357   1.00 45.65  ? 72  LYS B N   1 
ATOM   1242 C CA  . LYS B 1 77 ? -7.534  37.240 6.292   1.00 48.29  ? 72  LYS B CA  1 
ATOM   1243 C C   . LYS B 1 77 ? -7.118  36.907 4.844   1.00 45.56  ? 72  LYS B C   1 
ATOM   1244 O O   . LYS B 1 77 ? -7.674  37.477 3.936   1.00 44.89  ? 72  LYS B O   1 
ATOM   1245 C CB  . LYS B 1 77 ? -7.835  38.737 6.420   1.00 48.19  ? 72  LYS B CB  1 
ATOM   1246 C CG  . LYS B 1 77 ? -8.653  39.108 7.640   1.00 48.18  ? 72  LYS B CG  1 
ATOM   1247 C CD  . LYS B 1 77 ? -8.951  40.589 7.604   1.00 50.07  ? 72  LYS B CD  1 
ATOM   1248 C CE  . LYS B 1 77 ? -8.667  41.226 8.952   1.00 55.67  ? 72  LYS B CE  1 
ATOM   1249 N NZ  . LYS B 1 77 ? -8.642  42.709 8.804   1.00 59.61  ? 72  LYS B NZ  1 
ATOM   1250 N N   . ASP B 1 78 ? -6.168  36.003 4.628   1.00 46.24  ? 73  ASP B N   1 
ATOM   1251 C CA  . ASP B 1 78 ? -5.792  35.609 3.263   1.00 47.58  ? 73  ASP B CA  1 
ATOM   1252 C C   . ASP B 1 78 ? -6.919  34.847 2.591   1.00 50.45  ? 73  ASP B C   1 
ATOM   1253 O O   . ASP B 1 78 ? -7.715  34.162 3.263   1.00 51.02  ? 73  ASP B O   1 
ATOM   1254 C CB  . ASP B 1 78 ? -4.537  34.721 3.238   1.00 49.83  ? 73  ASP B CB  1 
ATOM   1255 C CG  . ASP B 1 78 ? -3.233  35.518 3.256   1.00 51.55  ? 73  ASP B CG  1 
ATOM   1256 O OD1 . ASP B 1 78 ? -3.281  36.766 3.339   1.00 59.07  ? 73  ASP B OD1 1 
ATOM   1257 O OD2 . ASP B 1 78 ? -2.154  34.894 3.185   1.00 44.96  ? 73  ASP B OD2 1 
ATOM   1258 N N   . ARG B 1 79 ? -6.970  34.975 1.264   1.00 48.72  ? 74  ARG B N   1 
ATOM   1259 C CA  . ARG B 1 79 ? -7.896  34.221 0.422   1.00 48.42  ? 74  ARG B CA  1 
ATOM   1260 C C   . ARG B 1 79 ? -7.164  33.044 -0.248  1.00 47.77  ? 74  ARG B C   1 
ATOM   1261 O O   . ARG B 1 79 ? -6.177  33.237 -0.966  1.00 44.99  ? 74  ARG B O   1 
ATOM   1262 C CB  . ARG B 1 79 ? -8.517  35.150 -0.628  1.00 53.64  ? 74  ARG B CB  1 
ATOM   1263 C CG  . ARG B 1 79 ? -9.634  34.565 -1.497  1.00 54.31  ? 74  ARG B CG  1 
ATOM   1264 C CD  . ARG B 1 79 ? -9.883  35.434 -2.724  1.00 57.06  ? 74  ARG B CD  1 
ATOM   1265 N NE  . ARG B 1 79 ? -10.568 36.705 -2.423  1.00 59.07  ? 74  ARG B NE  1 
ATOM   1266 C CZ  . ARG B 1 79 ? -10.884 37.631 -3.336  1.00 62.03  ? 74  ARG B CZ  1 
ATOM   1267 N NH1 . ARG B 1 79 ? -10.580 37.456 -4.623  1.00 67.47  ? 74  ARG B NH1 1 
ATOM   1268 N NH2 . ARG B 1 79 ? -11.517 38.739 -2.973  1.00 59.89  ? 74  ARG B NH2 1 
ATOM   1269 N N   . LEU B 1 80 ? -7.660  31.828 -0.015  1.00 47.28  ? 75  LEU B N   1 
ATOM   1270 C CA  . LEU B 1 80 ? -6.994  30.603 -0.471  1.00 46.53  ? 75  LEU B CA  1 
ATOM   1271 C C   . LEU B 1 80 ? -7.886  29.802 -1.373  1.00 48.81  ? 75  LEU B C   1 
ATOM   1272 O O   . LEU B 1 80 ? -9.088  29.665 -1.097  1.00 46.81  ? 75  LEU B O   1 
ATOM   1273 C CB  . LEU B 1 80 ? -6.602  29.722 0.713   1.00 45.31  ? 75  LEU B CB  1 
ATOM   1274 C CG  . LEU B 1 80 ? -5.725  30.403 1.755   1.00 42.65  ? 75  LEU B CG  1 
ATOM   1275 C CD1 . LEU B 1 80 ? -5.656  29.599 3.033   1.00 39.52  ? 75  LEU B CD1 1 
ATOM   1276 C CD2 . LEU B 1 80 ? -4.348  30.597 1.145   1.00 45.48  ? 75  LEU B CD2 1 
ATOM   1277 N N   . VAL B 1 81 ? -7.285  29.263 -2.440  1.00 51.56  ? 76  VAL B N   1 
ATOM   1278 C CA  . VAL B 1 81 ? -7.991  28.395 -3.395  1.00 50.15  ? 76  VAL B CA  1 
ATOM   1279 C C   . VAL B 1 81 ? -7.758  26.918 -3.077  1.00 51.12  ? 76  VAL B C   1 
ATOM   1280 O O   . VAL B 1 81 ? -6.616  26.489 -2.904  1.00 51.71  ? 76  VAL B O   1 
ATOM   1281 C CB  . VAL B 1 81 ? -7.688  28.741 -4.881  1.00 45.96  ? 76  VAL B CB  1 
ATOM   1282 C CG1 . VAL B 1 81 ? -6.436  29.589 -5.019  1.00 42.56  ? 76  VAL B CG1 1 
ATOM   1283 C CG2 . VAL B 1 81 ? -7.631  27.483 -5.751  1.00 45.46  ? 76  VAL B CG2 1 
ATOM   1284 N N   . ALA B 1 82 ? -8.858  26.170 -2.946  1.00 53.60  ? 77  ALA B N   1 
ATOM   1285 C CA  . ALA B 1 82 ? -8.811  24.717 -2.761  1.00 58.68  ? 77  ALA B CA  1 
ATOM   1286 C C   . ALA B 1 82 ? -8.799  24.027 -4.123  1.00 66.05  ? 77  ALA B C   1 
ATOM   1287 O O   . ALA B 1 82 ? -9.540  24.413 -5.043  1.00 69.10  ? 77  ALA B O   1 
ATOM   1288 C CB  . ALA B 1 82 ? -9.991  24.233 -1.939  1.00 53.48  ? 77  ALA B CB  1 
ATOM   1289 N N   . VAL B 1 83 ? -7.921  23.038 -4.251  1.00 68.62  ? 78  VAL B N   1 
ATOM   1290 C CA  . VAL B 1 83 ? -7.843  22.200 -5.441  1.00 65.56  ? 78  VAL B CA  1 
ATOM   1291 C C   . VAL B 1 83 ? -8.387  20.842 -5.008  1.00 67.25  ? 78  VAL B C   1 
ATOM   1292 O O   . VAL B 1 83 ? -7.831  20.174 -4.111  1.00 67.15  ? 78  VAL B O   1 
ATOM   1293 C CB  . VAL B 1 83 ? -6.399  22.079 -5.952  1.00 63.08  ? 78  VAL B CB  1 
ATOM   1294 C CG1 . VAL B 1 83 ? -6.381  21.340 -7.276  1.00 60.50  ? 78  VAL B CG1 1 
ATOM   1295 C CG2 . VAL B 1 83 ? -5.780  23.460 -6.094  1.00 61.43  ? 78  VAL B CG2 1 
ATOM   1296 N N   . PHE B 1 84 ? -9.502  20.451 -5.612  1.00 61.78  ? 79  PHE B N   1 
ATOM   1297 C CA  . PHE B 1 84 ? -10.316 19.394 -5.023  1.00 60.48  ? 79  PHE B CA  1 
ATOM   1298 C C   . PHE B 1 84 ? -11.075 18.648 -6.098  1.00 56.60  ? 79  PHE B C   1 
ATOM   1299 O O   . PHE B 1 84 ? -11.233 19.157 -7.209  1.00 50.89  ? 79  PHE B O   1 
ATOM   1300 C CB  . PHE B 1 84 ? -11.297 19.996 -3.977  1.00 58.46  ? 79  PHE B CB  1 
ATOM   1301 C CG  . PHE B 1 84 ? -12.435 20.794 -4.582  1.00 57.14  ? 79  PHE B CG  1 
ATOM   1302 C CD1 . PHE B 1 84 ? -12.208 22.019 -5.210  1.00 60.54  ? 79  PHE B CD1 1 
ATOM   1303 C CD2 . PHE B 1 84 ? -13.739 20.309 -4.550  1.00 56.94  ? 79  PHE B CD2 1 
ATOM   1304 C CE1 . PHE B 1 84 ? -13.261 22.751 -5.782  1.00 60.59  ? 79  PHE B CE1 1 
ATOM   1305 C CE2 . PHE B 1 84 ? -14.788 21.031 -5.124  1.00 56.76  ? 79  PHE B CE2 1 
ATOM   1306 C CZ  . PHE B 1 84 ? -14.556 22.258 -5.734  1.00 55.92  ? 79  PHE B CZ  1 
ATOM   1307 N N   . ASP B 1 85 ? -11.561 17.458 -5.751  1.00 61.19  ? 80  ASP B N   1 
ATOM   1308 C CA  . ASP B 1 85 ? -12.533 16.754 -6.593  1.00 66.13  ? 80  ASP B CA  1 
ATOM   1309 C C   . ASP B 1 85 ? -13.870 16.406 -5.912  1.00 68.77  ? 80  ASP B C   1 
ATOM   1310 O O   . ASP B 1 85 ? -13.907 16.047 -4.707  1.00 61.61  ? 80  ASP B O   1 
ATOM   1311 C CB  . ASP B 1 85 ? -11.897 15.516 -7.235  1.00 68.55  ? 80  ASP B CB  1 
ATOM   1312 C CG  . ASP B 1 85 ? -10.986 15.873 -8.395  1.00 62.83  ? 80  ASP B CG  1 
ATOM   1313 O OD1 . ASP B 1 85 ? -11.500 16.249 -9.479  1.00 58.08  ? 80  ASP B OD1 1 
ATOM   1314 O OD2 . ASP B 1 85 ? -9.755  15.789 -8.205  1.00 63.59  ? 80  ASP B OD2 1 
ATOM   1315 N N   . GLU B 1 86 ? -14.938 16.501 -6.724  1.00 69.69  ? 81  GLU B N   1 
ATOM   1316 C CA  . GLU B 1 86 ? -16.337 16.236 -6.322  1.00 73.36  ? 81  GLU B CA  1 
ATOM   1317 C C   . GLU B 1 86 ? -17.161 15.513 -7.413  1.00 69.18  ? 81  GLU B C   1 
ATOM   1318 O O   . GLU B 1 86 ? -18.170 14.847 -7.125  1.00 64.04  ? 81  GLU B O   1 
ATOM   1319 C CB  . GLU B 1 86 ? -17.036 17.548 -5.904  1.00 74.40  ? 81  GLU B CB  1 
ATOM   1320 C CG  . GLU B 1 86 ? -17.023 18.655 -6.961  1.00 72.63  ? 81  GLU B CG  1 
ATOM   1321 C CD  . GLU B 1 86 ? -17.835 19.902 -6.595  1.00 72.24  ? 81  GLU B CD  1 
ATOM   1322 O OE1 . GLU B 1 86 ? -18.135 20.133 -5.397  1.00 60.25  ? 81  GLU B OE1 1 
ATOM   1323 O OE2 . GLU B 1 86 ? -18.166 20.677 -7.531  1.00 73.02  ? 81  GLU B OE2 1 
HETATM 1324 O O   . HOH C 2 .  ? 11.232  41.260 4.116   1.00 26.83  ? 101 HOH A O   1 
HETATM 1325 O O   . HOH C 2 .  ? 0.775   39.166 0.984   1.00 45.95  ? 102 HOH A O   1 
HETATM 1326 O O   . HOH C 2 .  ? 15.345  17.395 -14.053 1.00 37.02  ? 103 HOH A O   1 
HETATM 1327 O O   . HOH C 2 .  ? 16.606  24.473 9.270   1.00 49.81  ? 104 HOH A O   1 
HETATM 1328 O O   . HOH C 2 .  ? 16.482  10.425 -14.930 1.00 37.62  ? 105 HOH A O   1 
HETATM 1329 O O   . HOH C 2 .  ? 10.845  27.464 -12.325 1.00 29.53  ? 106 HOH A O   1 
HETATM 1330 O O   . HOH C 2 .  ? 23.464  28.010 -5.788  1.00 55.93  ? 107 HOH A O   1 
HETATM 1331 O O   . HOH C 2 .  ? 20.150  28.636 9.264   1.00 50.92  ? 108 HOH A O   1 
HETATM 1332 O O   . HOH C 2 .  ? 15.103  33.773 -13.495 1.00 31.63  ? 109 HOH A O   1 
HETATM 1333 O O   . HOH C 2 .  ? 8.064   26.750 -16.021 1.00 41.40  ? 110 HOH A O   1 
HETATM 1334 O O   . HOH C 2 .  ? 9.008   37.819 -5.526  1.00 32.42  ? 111 HOH A O   1 
HETATM 1335 O O   . HOH C 2 .  ? 2.566   33.579 2.175   1.00 59.75  ? 112 HOH A O   1 
HETATM 1336 O O   . HOH C 2 .  ? 13.824  1.868  -13.004 1.00 27.83  ? 113 HOH A O   1 
HETATM 1337 O O   . HOH D 2 .  ? 2.928   34.060 7.689   1.00 40.35  ? 101 HOH B O   1 
HETATM 1338 O O   . HOH D 2 .  ? 4.528   22.265 0.516   1.00 52.26  ? 102 HOH B O   1 
HETATM 1339 O O   . HOH D 2 .  ? -3.842  28.584 16.892  1.00 45.44  ? 103 HOH B O   1 
HETATM 1340 O O   . HOH D 2 .  ? -15.171 20.733 10.939  1.00 34.88  ? 104 HOH B O   1 
HETATM 1341 O O   . HOH D 2 .  ? 0.415   35.209 9.138   1.00 34.36  ? 105 HOH B O   1 
HETATM 1342 O O   . HOH D 2 .  ? 6.967   30.981 9.140   1.00 69.58  ? 106 HOH B O   1 
HETATM 1343 O O   . HOH D 2 .  ? 1.377   23.014 15.460  1.00 48.51  ? 107 HOH B O   1 
HETATM 1344 O O   . HOH D 2 .  ? -10.846 29.102 -6.711  1.00 49.70  ? 108 HOH B O   1 
HETATM 1345 O O   . HOH D 2 .  ? -9.957  19.633 12.378  1.00 42.33  ? 109 HOH B O   1 
HETATM 1346 O O   . HOH D 2 .  ? -7.755  17.255 6.181   1.00 45.67  ? 110 HOH B O   1 
HETATM 1347 O O   . HOH D 2 .  ? -10.600 35.547 5.148   1.00 53.39  ? 111 HOH B O   1 
HETATM 1348 O O   . HOH D 2 .  ? 3.070   25.465 17.621  1.00 45.69  ? 112 HOH B O   1 
HETATM 1349 O O   . HOH D 2 .  ? -8.994  38.041 11.510  1.00 39.50  ? 113 HOH B O   1 
HETATM 1350 O O   . HOH D 2 .  ? -21.019 30.703 -10.480 1.00 38.41  ? 114 HOH B O   1 
HETATM 1351 O O   . HOH D 2 .  ? -22.929 13.405 2.455   1.00 43.67  ? 115 HOH B O   1 
HETATM 1352 O O   . HOH D 2 .  ? -3.524  33.708 -1.406  1.00 38.97  ? 116 HOH B O   1 
HETATM 1353 O O   . HOH D 2 .  ? 4.862   34.564 -5.247  1.00 43.40  ? 117 HOH B O   1 
HETATM 1354 O O   . HOH D 2 .  ? -7.090  28.521 19.194  1.00 25.63  ? 118 HOH B O   1 
HETATM 1355 O O   . HOH D 2 .  ? -20.668 20.684 11.758  0.50 47.64  ? 119 HOH B O   1 
HETATM 1356 O O   . HOH D 2 .  ? -14.160 31.856 -5.936  1.00 51.69  ? 120 HOH B O   1 
HETATM 1357 O O   . HOH D 2 .  ? -18.527 34.197 -4.021  1.00 28.02  ? 121 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  -4 ?  ?   ?   A . n 
A 1 2  PRO 2  -3 ?  ?   ?   A . n 
A 1 3  GLY 3  -2 ?  ?   ?   A . n 
A 1 4  SER 4  -1 -1 SER SER A . n 
A 1 5  GLU 5  0  0  GLU GLU A . n 
A 1 6  PHE 6  1  1  PHE PHE A . n 
A 1 7  LYS 7  2  2  LYS LYS A . n 
A 1 8  VAL 8  3  3  VAL VAL A . n 
A 1 9  THR 9  4  4  THR THR A . n 
A 1 10 VAL 10 5  5  VAL VAL A . n 
A 1 11 CYS 11 6  6  CYS CYS A . n 
A 1 12 PHE 12 7  7  PHE PHE A . n 
A 1 13 GLY 13 8  8  GLY GLY A . n 
A 1 14 ARG 14 9  9  ARG ARG A . n 
A 1 15 THR 15 10 10 THR THR A . n 
A 1 16 ARG 16 11 11 ARG ARG A . n 
A 1 17 VAL 17 12 12 VAL VAL A . n 
A 1 18 VAL 18 13 13 VAL VAL A . n 
A 1 19 VAL 19 14 14 VAL VAL A . n 
A 1 20 PRO 20 15 15 PRO PRO A . n 
A 1 21 CYS 21 16 16 CYS CYS A . n 
A 1 22 GLY 22 17 17 GLY GLY A . n 
A 1 23 ASP 23 18 18 ASP ASP A . n 
A 1 24 GLY 24 19 19 GLY GLY A . n 
A 1 25 ARG 25 20 20 ARG ARG A . n 
A 1 26 MET 26 21 21 MET MET A . n 
A 1 27 LYS 27 22 22 LYS LYS A . n 
A 1 28 VAL 28 23 23 VAL VAL A . n 
A 1 29 PHE 29 24 24 PHE PHE A . n 
A 1 30 SER 30 25 25 SER SER A . n 
A 1 31 LEU 31 26 26 LEU LEU A . n 
A 1 32 ILE 32 27 27 ILE ILE A . n 
A 1 33 GLN 33 28 28 GLN GLN A . n 
A 1 34 GLN 34 29 29 GLN GLN A . n 
A 1 35 ALA 35 30 30 ALA ALA A . n 
A 1 36 VAL 36 31 31 VAL VAL A . n 
A 1 37 THR 37 32 32 THR THR A . n 
A 1 38 ARG 38 33 33 ARG ARG A . n 
A 1 39 TYR 39 34 34 TYR TYR A . n 
A 1 40 ARG 40 35 35 ARG ARG A . n 
A 1 41 LYS 41 36 36 LYS LYS A . n 
A 1 42 ALA 42 37 37 ALA ALA A . n 
A 1 43 VAL 43 38 38 VAL VAL A . n 
A 1 44 ALA 44 39 39 ALA ALA A . n 
A 1 45 LYS 45 40 40 LYS LYS A . n 
A 1 46 ASP 46 41 41 ASP ASP A . n 
A 1 47 PRO 47 42 42 PRO PRO A . n 
A 1 48 ASN 48 43 43 ASN ASN A . n 
A 1 49 TYR 49 44 44 TYR TYR A . n 
A 1 50 TRP 50 45 45 TRP TRP A . n 
A 1 51 ILE 51 46 46 ILE ILE A . n 
A 1 52 GLN 52 47 47 GLN GLN A . n 
A 1 53 VAL 53 48 48 VAL VAL A . n 
A 1 54 HIS 54 49 49 HIS HIS A . n 
A 1 55 ARG 55 50 50 ARG ARG A . n 
A 1 56 LEU 56 51 51 LEU LEU A . n 
A 1 57 GLU 57 52 52 GLU GLU A . n 
A 1 58 HIS 58 53 53 HIS HIS A . n 
A 1 59 GLY 59 54 54 GLY GLY A . n 
A 1 60 ASP 60 55 55 ASP ASP A . n 
A 1 61 GLY 61 56 56 GLY GLY A . n 
A 1 62 GLY 62 57 57 GLY GLY A . n 
A 1 63 ILE 63 58 58 ILE ILE A . n 
A 1 64 LEU 64 59 59 LEU LEU A . n 
A 1 65 ASP 65 60 60 ASP ASP A . n 
A 1 66 LEU 66 61 61 LEU LEU A . n 
A 1 67 ASP 67 62 62 ASP ASP A . n 
A 1 68 ASP 68 63 63 ASP ASP A . n 
A 1 69 ILE 69 64 64 ILE ILE A . n 
A 1 70 LEU 70 65 65 LEU LEU A . n 
A 1 71 CYS 71 66 66 CYS CYS A . n 
A 1 72 ASP 72 67 67 ASP ASP A . n 
A 1 73 VAL 73 68 68 VAL VAL A . n 
A 1 74 ALA 74 69 69 ALA ALA A . n 
A 1 75 ASP 75 70 70 ASP ASP A . n 
A 1 76 ASP 76 71 71 ASP ASP A . n 
A 1 77 LYS 77 72 72 LYS LYS A . n 
A 1 78 ASP 78 73 73 ASP ASP A . n 
A 1 79 ARG 79 74 74 ARG ARG A . n 
A 1 80 LEU 80 75 75 LEU LEU A . n 
A 1 81 VAL 81 76 76 VAL VAL A . n 
A 1 82 ALA 82 77 77 ALA ALA A . n 
A 1 83 VAL 83 78 78 VAL VAL A . n 
A 1 84 PHE 84 79 79 PHE PHE A . n 
A 1 85 ASP 85 80 80 ASP ASP A . n 
A 1 86 GLU 86 81 81 GLU GLU A . n 
A 1 87 GLN 87 82 82 GLN GLN A . n 
A 1 88 ASP 88 83 ?  ?   ?   A . n 
B 1 1  GLY 1  -4 ?  ?   ?   B . n 
B 1 2  PRO 2  -3 ?  ?   ?   B . n 
B 1 3  GLY 3  -2 ?  ?   ?   B . n 
B 1 4  SER 4  -1 ?  ?   ?   B . n 
B 1 5  GLU 5  0  0  GLU GLU B . n 
B 1 6  PHE 6  1  1  PHE PHE B . n 
B 1 7  LYS 7  2  2  LYS LYS B . n 
B 1 8  VAL 8  3  3  VAL VAL B . n 
B 1 9  THR 9  4  4  THR THR B . n 
B 1 10 VAL 10 5  5  VAL VAL B . n 
B 1 11 CYS 11 6  6  CYS CYS B . n 
B 1 12 PHE 12 7  7  PHE PHE B . n 
B 1 13 GLY 13 8  8  GLY GLY B . n 
B 1 14 ARG 14 9  9  ARG ARG B . n 
B 1 15 THR 15 10 10 THR THR B . n 
B 1 16 ARG 16 11 11 ARG ARG B . n 
B 1 17 VAL 17 12 12 VAL VAL B . n 
B 1 18 VAL 18 13 13 VAL VAL B . n 
B 1 19 VAL 19 14 14 VAL VAL B . n 
B 1 20 PRO 20 15 15 PRO PRO B . n 
B 1 21 CYS 21 16 16 CYS CYS B . n 
B 1 22 GLY 22 17 17 GLY GLY B . n 
B 1 23 ASP 23 18 18 ASP ASP B . n 
B 1 24 GLY 24 19 19 GLY GLY B . n 
B 1 25 ARG 25 20 20 ARG ARG B . n 
B 1 26 MET 26 21 21 MET MET B . n 
B 1 27 LYS 27 22 22 LYS LYS B . n 
B 1 28 VAL 28 23 23 VAL VAL B . n 
B 1 29 PHE 29 24 24 PHE PHE B . n 
B 1 30 SER 30 25 25 SER SER B . n 
B 1 31 LEU 31 26 26 LEU LEU B . n 
B 1 32 ILE 32 27 27 ILE ILE B . n 
B 1 33 GLN 33 28 28 GLN GLN B . n 
B 1 34 GLN 34 29 29 GLN GLN B . n 
B 1 35 ALA 35 30 30 ALA ALA B . n 
B 1 36 VAL 36 31 31 VAL VAL B . n 
B 1 37 THR 37 32 32 THR THR B . n 
B 1 38 ARG 38 33 33 ARG ARG B . n 
B 1 39 TYR 39 34 34 TYR TYR B . n 
B 1 40 ARG 40 35 35 ARG ARG B . n 
B 1 41 LYS 41 36 36 LYS LYS B . n 
B 1 42 ALA 42 37 37 ALA ALA B . n 
B 1 43 VAL 43 38 38 VAL VAL B . n 
B 1 44 ALA 44 39 39 ALA ALA B . n 
B 1 45 LYS 45 40 40 LYS LYS B . n 
B 1 46 ASP 46 41 41 ASP ASP B . n 
B 1 47 PRO 47 42 42 PRO PRO B . n 
B 1 48 ASN 48 43 43 ASN ASN B . n 
B 1 49 TYR 49 44 44 TYR TYR B . n 
B 1 50 TRP 50 45 45 TRP TRP B . n 
B 1 51 ILE 51 46 46 ILE ILE B . n 
B 1 52 GLN 52 47 47 GLN GLN B . n 
B 1 53 VAL 53 48 48 VAL VAL B . n 
B 1 54 HIS 54 49 49 HIS HIS B . n 
B 1 55 ARG 55 50 50 ARG ARG B . n 
B 1 56 LEU 56 51 51 LEU LEU B . n 
B 1 57 GLU 57 52 52 GLU GLU B . n 
B 1 58 HIS 58 53 53 HIS HIS B . n 
B 1 59 GLY 59 54 54 GLY GLY B . n 
B 1 60 ASP 60 55 55 ASP ASP B . n 
B 1 61 GLY 61 56 56 GLY GLY B . n 
B 1 62 GLY 62 57 57 GLY GLY B . n 
B 1 63 ILE 63 58 58 ILE ILE B . n 
B 1 64 LEU 64 59 59 LEU LEU B . n 
B 1 65 ASP 65 60 60 ASP ASP B . n 
B 1 66 LEU 66 61 61 LEU LEU B . n 
B 1 67 ASP 67 62 62 ASP ASP B . n 
B 1 68 ASP 68 63 63 ASP ASP B . n 
B 1 69 ILE 69 64 64 ILE ILE B . n 
B 1 70 LEU 70 65 65 LEU LEU B . n 
B 1 71 CYS 71 66 66 CYS CYS B . n 
B 1 72 ASP 72 67 67 ASP ASP B . n 
B 1 73 VAL 73 68 68 VAL VAL B . n 
B 1 74 ALA 74 69 69 ALA ALA B . n 
B 1 75 ASP 75 70 70 ASP ASP B . n 
B 1 76 ASP 76 71 71 ASP ASP B . n 
B 1 77 LYS 77 72 72 LYS LYS B . n 
B 1 78 ASP 78 73 73 ASP ASP B . n 
B 1 79 ARG 79 74 74 ARG ARG B . n 
B 1 80 LEU 80 75 75 LEU LEU B . n 
B 1 81 VAL 81 76 76 VAL VAL B . n 
B 1 82 ALA 82 77 77 ALA ALA B . n 
B 1 83 VAL 83 78 78 VAL VAL B . n 
B 1 84 PHE 84 79 79 PHE PHE B . n 
B 1 85 ASP 85 80 80 ASP ASP B . n 
B 1 86 GLU 86 81 81 GLU GLU B . n 
B 1 87 GLN 87 82 ?  ?   ?   B . n 
B 1 88 ASP 88 83 ?  ?   ?   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 2 HOH 1  101 2  HOH HOH A . 
C 2 HOH 2  102 5  HOH HOH A . 
C 2 HOH 3  103 9  HOH HOH A . 
C 2 HOH 4  104 12 HOH HOH A . 
C 2 HOH 5  105 16 HOH HOH A . 
C 2 HOH 6  106 18 HOH HOH A . 
C 2 HOH 7  107 19 HOH HOH A . 
C 2 HOH 8  108 20 HOH HOH A . 
C 2 HOH 9  109 21 HOH HOH A . 
C 2 HOH 10 110 25 HOH HOH A . 
C 2 HOH 11 111 29 HOH HOH A . 
C 2 HOH 12 112 34 HOH HOH A . 
C 2 HOH 13 113 35 HOH HOH A . 
D 2 HOH 1  101 1  HOH HOH B . 
D 2 HOH 2  102 3  HOH HOH B . 
D 2 HOH 3  103 4  HOH HOH B . 
D 2 HOH 4  104 6  HOH HOH B . 
D 2 HOH 5  105 7  HOH HOH B . 
D 2 HOH 6  106 8  HOH HOH B . 
D 2 HOH 7  107 10 HOH HOH B . 
D 2 HOH 8  108 13 HOH HOH B . 
D 2 HOH 9  109 15 HOH HOH B . 
D 2 HOH 10 110 17 HOH HOH B . 
D 2 HOH 11 111 22 HOH HOH B . 
D 2 HOH 12 112 23 HOH HOH B . 
D 2 HOH 13 113 24 HOH HOH B . 
D 2 HOH 14 114 26 HOH HOH B . 
D 2 HOH 15 115 27 HOH HOH B . 
D 2 HOH 16 116 28 HOH HOH B . 
D 2 HOH 17 117 30 HOH HOH B . 
D 2 HOH 18 118 31 HOH HOH B . 
D 2 HOH 19 119 32 HOH HOH B . 
D 2 HOH 20 120 36 HOH HOH B . 
D 2 HOH 21 121 37 HOH HOH B . 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly              ?    dimeric   2 
2 author_and_software_defined_assembly PISA monomeric 1 
3 author_and_software_defined_assembly PISA monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,C,D 
2 1 A,C     
3 1 B,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 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    B 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     119 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   D 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
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 2013-07-17 
2 'Structure model' 1 1 2017-10-25 
# 
_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_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Author supporting evidence' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            pdbx_struct_assembly_auth_evidence 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
ADSC     'data collection' Quantum  ? 1 
PHASER   phasing           .        ? 2 
REFMAC   refinement        5.6.0117 ? 3 
HKL-2000 'data reduction'  .        ? 4 
HKL-2000 'data scaling'    .        ? 5 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ALA A 39 ? ? 62.79   139.13 
2 1 LYS A 40 ? ? -169.76 8.98   
3 1 ALA B 39 ? ? 26.73   74.47  
4 1 TYR B 44 ? ? -23.01  123.78 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY -4 ? A GLY 1  
2  1 Y 1 A PRO -3 ? A PRO 2  
3  1 Y 1 A GLY -2 ? A GLY 3  
4  1 Y 1 A ASP 83 ? A ASP 88 
5  1 Y 1 B GLY -4 ? B GLY 1  
6  1 Y 1 B PRO -3 ? B PRO 2  
7  1 Y 1 B GLY -2 ? B GLY 3  
8  1 Y 1 B SER -1 ? B SER 4  
9  1 Y 1 B GLN 82 ? B GLN 87 
10 1 Y 1 B ASP 83 ? B ASP 88 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'scanning transmission electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                ? 
#