CNRS Nantes University UFIP UFIP
home |  start a new run |  job status |  references&downloads |  examples |  help  

Should you encounter any unexpected behaviour,
please let us know.


***    ***

elNémo ID: 22031014505041520

Job options:

ID        	=	 22031014505041520
JOBID     	=	 
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


data_1CC8
# 
_entry.id   1CC8 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.286 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   1CC8         
RCSB  RCSB000585   
WWPDB D_1000000585 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        1CC8 
_pdbx_database_status.recvd_initial_deposition_date   1999-03-04 
_pdbx_database_status.deposit_site                    BNL 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Rosenzweig, A.C.' 1 
'Huffman, D.L.'    2 
'Pufahl, M.Y.R.A.' 3 
'Hou, T.V.O.'      4 
'Wernimont, A.K.'  5 
# 
_citation.id                        primary 
_citation.title                     'Crystal structure of the Atx1 metallochaperone protein at 1.02 A resolution.' 
_citation.journal_abbrev            'Structure Fold.Des.' 
_citation.journal_volume            7 
_citation.page_first                605 
_citation.page_last                 617 
_citation.year                      1999 
_citation.journal_id_ASTM           FODEFH 
_citation.country                   UK 
_citation.journal_id_ISSN           0969-2126 
_citation.journal_id_CSD            1263 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   10404590 
_citation.pdbx_database_id_DOI      '10.1016/S0969-2126(99)80082-3' 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Rosenzweig, A.C.' 1 
primary 'Huffman, D.L.'    2 
primary 'Hou, M.Y.'        3 
primary 'Wernimont, A.K.'  4 
primary 'Pufahl, R.A.'     5 
primary 
;O'Halloran, T.V.
;
6 
# 
_cell.entry_id           1CC8 
_cell.length_a           56.650 
_cell.length_b           29.600 
_cell.length_c           40.770 
_cell.angle_alpha        90.00 
_cell.angle_beta         114.83 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         1CC8 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     monoclinic 
_symmetry.Int_Tables_number                5 
# 
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 'PROTEIN (METALLOCHAPERONE ATX1)' 8232.650 1   ? ? ? ? 
2 non-polymer syn 'MERCURY (II) ION'                200.590  1   ? ? ? ? 
3 non-polymer syn BENZAMIDINE                       120.152  2   ? ? ? ? 
4 water       nat water                             18.015   117 ? ? ? ? 
# 
_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       MAEIKHYQFNVVMTCSGCSGAVNKVLTKLEPDVSKIDISLEKQLVDVYTTLPYDFILEKIKKTGKEVRSGKQL 
_entity_poly.pdbx_seq_one_letter_code_can   MAEIKHYQFNVVMTCSGCSGAVNKVLTKLEPDVSKIDISLEKQLVDVYTTLPYDFILEKIKKTGKEVRSGKQL 
_entity_poly.pdbx_strand_id                 A 
_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  MET n 
1 2  ALA n 
1 3  GLU n 
1 4  ILE n 
1 5  LYS n 
1 6  HIS n 
1 7  TYR n 
1 8  GLN n 
1 9  PHE n 
1 10 ASN n 
1 11 VAL n 
1 12 VAL n 
1 13 MET n 
1 14 THR n 
1 15 CYS n 
1 16 SER n 
1 17 GLY n 
1 18 CYS n 
1 19 SER n 
1 20 GLY n 
1 21 ALA n 
1 22 VAL n 
1 23 ASN n 
1 24 LYS n 
1 25 VAL n 
1 26 LEU n 
1 27 THR n 
1 28 LYS n 
1 29 LEU n 
1 30 GLU n 
1 31 PRO n 
1 32 ASP n 
1 33 VAL n 
1 34 SER n 
1 35 LYS n 
1 36 ILE n 
1 37 ASP n 
1 38 ILE n 
1 39 SER n 
1 40 LEU n 
1 41 GLU n 
1 42 LYS n 
1 43 GLN n 
1 44 LEU n 
1 45 VAL n 
1 46 ASP n 
1 47 VAL n 
1 48 TYR n 
1 49 THR n 
1 50 THR n 
1 51 LEU n 
1 52 PRO n 
1 53 TYR n 
1 54 ASP n 
1 55 PHE n 
1 56 ILE n 
1 57 LEU n 
1 58 GLU n 
1 59 LYS n 
1 60 ILE n 
1 61 LYS n 
1 62 LYS n 
1 63 THR n 
1 64 GLY n 
1 65 LYS n 
1 66 GLU n 
1 67 VAL n 
1 68 ARG n 
1 69 SER n 
1 70 GLY n 
1 71 LYS n 
1 72 GLN n 
1 73 LEU 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               
;baker's yeast
;
_entity_src_gen.gene_src_genus                     Saccharomyces 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Saccharomyces cerevisiae' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     4932 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     Escherichia 
_entity_src_gen.pdbx_host_org_gene                 ATX1 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   'Escherichia coli' 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               BL21DE3 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               PET11D 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    ATX1_YEAST 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_db_accession          P38636 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           ? 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              1CC8 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 73 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P38636 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  73 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       73 
# 
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 
BEN non-polymer         . BENZAMIDINE        ? 'C7 H8 N2'       120.152 
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  
HG  non-polymer         . 'MERCURY (II) ION' ? 'Hg 2'           200.590 
HIS 'L-peptide linking' y HISTIDINE          ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER              ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE         ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE            ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE             ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE         ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE      ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE            ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE             ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE          ? 'C4 H9 N O3'     119.119 
TYR 'L-peptide linking' y TYROSINE           ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE             ? 'C5 H11 N O2'    117.146 
# 
_exptl.entry_id          1CC8 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      1.94 
_exptl_crystal.density_percent_sol   36 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          ? 
_exptl_crystal_grow.temp            ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              6.0 
_exptl_crystal_grow.pdbx_details    'pH 6.0' 
_exptl_crystal_grow.pdbx_pH_range   . 
# 
loop_
_exptl_crystal_grow_comp.crystal_id 
_exptl_crystal_grow_comp.id 
_exptl_crystal_grow_comp.sol_id 
_exptl_crystal_grow_comp.name 
_exptl_crystal_grow_comp.volume 
_exptl_crystal_grow_comp.conc 
_exptl_crystal_grow_comp.details 
1 1 1 '(NH4)2SO4' ? ? ? 
1 2 1 BENZAMIDINE ? ? ? 
1 3 1 GLYCEROL    ? ? ? 
1 4 1 MES         ? ? ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           95 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   MARRESEARCH 
_diffrn_detector.pdbx_collection_date   1997-08-01 
_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                    ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0047 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'APS BEAMLINE 5ID-B' 
_diffrn_source.pdbx_synchrotron_site       APS 
_diffrn_source.pdbx_synchrotron_beamline   5ID-B 
_diffrn_source.pdbx_wavelength             1.0047 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.entry_id                     1CC8 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             50 
_reflns.d_resolution_high            1.02 
_reflns.number_obs                   24099 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         95.4 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              0.051 
_reflns.pdbx_netI_over_sigmaI        8.4 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              4 
_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_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
_reflns_shell.d_res_high             1.02 
_reflns_shell.d_res_low              1.05 
_reflns_shell.percent_possible_all   90.2 
_reflns_shell.Rmerge_I_obs           ? 
_reflns_shell.pdbx_Rsym_value        0.106 
_reflns_shell.meanI_over_sigI_obs    5.3 
_reflns_shell.pdbx_redundancy        2.9 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      ? 
_reflns_shell.pdbx_diffrn_id         ? 
_reflns_shell.pdbx_ordinal           1 
# 
_refine.entry_id                                 1CC8 
_refine.ls_number_reflns_obs                     25378 
_refine.ls_number_reflns_all                     25378 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.0 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             50 
_refine.ls_d_res_high                            1.02 
_refine.ls_percent_reflns_obs                    95.4 
_refine.ls_R_factor_obs                          0.1464000 
_refine.ls_R_factor_all                          0.1412000 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_factor_R_free                       0.1717000 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 10.0 
_refine.ls_number_reflns_R_free                  2812 
_refine.ls_number_parameters                     5745 
_refine.ls_number_restraints                     6701 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    'MOEWS & KRETSINGER, J.MOL.BIOL.91(1973)201-228' 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_ls_cross_valid_method               'FREE R' 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'DIRECT METHODS' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'ENGH AND HUBER' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_analyze.entry_id                        1CC8 
_refine_analyze.Luzzati_coordinate_error_obs    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      0 
_refine_analyze.occupancy_sum_hydrogen          596.00 
_refine_analyze.occupancy_sum_non_hydrogen      701.50 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        567 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         19 
_refine_hist.number_atoms_solvent             117 
_refine_hist.number_atoms_total               703 
_refine_hist.d_res_high                       1.02 
_refine_hist.d_res_low                        50 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
s_bond_d               0.010 ? ? ? 'X-RAY DIFFRACTION' ? 
s_angle_d              0.028 ? ? ? 'X-RAY DIFFRACTION' ? 
s_similar_dist         0.000 ? ? ? 'X-RAY DIFFRACTION' ? 
s_from_restr_planes    0.052 ? ? ? 'X-RAY DIFFRACTION' ? 
s_zero_chiral_vol      0.130 ? ? ? 'X-RAY DIFFRACTION' ? 
s_non_zero_chiral_vol  0.108 ? ? ? 'X-RAY DIFFRACTION' ? 
s_anti_bump_dis_restr  0.055 ? ? ? 'X-RAY DIFFRACTION' ? 
s_rigid_bond_adp_cmpnt 0.005 ? ? ? 'X-RAY DIFFRACTION' ? 
s_similar_adp_cmpnt    0.039 ? ? ? 'X-RAY DIFFRACTION' ? 
s_approx_iso_adps      0.000 ? ? ? 'X-RAY DIFFRACTION' ? 
# 
_pdbx_refine.entry_id                                    1CC8 
_pdbx_refine.R_factor_all_no_cutoff                      0.1412000 
_pdbx_refine.R_factor_obs_no_cutoff                      0.1464000 
_pdbx_refine.free_R_factor_no_cutoff                     0.1717000 
_pdbx_refine.free_R_val_test_set_size_perc_no_cutoff     10.0 
_pdbx_refine.free_R_val_test_set_ct_no_cutoff            2812 
_pdbx_refine.R_factor_all_4sig_cutoff                    0.1393000 
_pdbx_refine.R_factor_obs_4sig_cutoff                    0.1447000 
_pdbx_refine.free_R_factor_4sig_cutoff                   0.1772000 
_pdbx_refine.free_R_val_test_set_size_perc_4sig_cutoff   11.1 
_pdbx_refine.free_R_val_test_set_ct_4sig_cutoff          2812 
_pdbx_refine.number_reflns_obs_4sig_cutoff               25378 
_pdbx_refine.number_reflns_obs_no_cutoff                 ? 
_pdbx_refine.pdbx_refine_id                              'X-RAY DIFFRACTION' 
_pdbx_refine.free_R_error_no_cutoff                      ? 
# 
_struct.entry_id                  1CC8 
_struct.title                     'CRYSTAL STRUCTURE OF THE ATX1 METALLOCHAPERONE PROTEIN' 
_struct.pdbx_descriptor           'METALLOCHAPERONE ATX1' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        1CC8 
_struct_keywords.pdbx_keywords   'METAL TRANSPORT' 
_struct_keywords.text            'COPPER TRANSPORT, MERCURY COORDINATION, METAL TRANSPORT' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 4 ? 
# 
_struct_biol.id   1 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 1 SER A 16 ? LEU A 29 ? SER A 16 LEU A 29 1 ? 14 
HELX_P HELX_P2 2 TYR A 53 ? THR A 63 ? TYR A 53 THR A 63 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
metalc1 metalc ? ? B HG . HG ? ? ? 1_555 A THR 14 OG1 ? ? A HG 74 A THR 14   1_555 ? ? ? ? ? ? ? 3.075 ? 
metalc2 metalc ? ? B HG . HG ? ? ? 1_555 A CYS 15 SG  ? ? A HG 74 A CYS 15   1_555 ? ? ? ? ? ? ? 2.329 ? 
metalc3 metalc ? ? B HG . HG ? ? ? 1_555 A CYS 15 N   ? ? A HG 74 A CYS 15   1_555 ? ? ? ? ? ? ? 3.263 ? 
metalc4 metalc ? ? B HG . HG ? ? ? 1_555 A CYS 15 O   ? ? A HG 74 A CYS 15   1_555 ? ? ? ? ? ? ? 3.463 ? 
metalc5 metalc ? ? B HG . HG ? ? ? 1_555 A CYS 18 SG  ? ? A HG 74 A CYS 18   1_555 ? ? ? ? ? ? ? 2.341 ? 
metalc6 metalc ? ? B HG . HG ? ? ? 1_555 A CYS 18 N   ? ? A HG 74 A CYS 18   1_555 ? ? ? ? ? ? ? 3.137 ? 
metalc7 metalc ? ? B HG . HG ? ? ? 1_555 E HOH .  O   ? ? A HG 74 A HOH 1018 1_545 ? ? ? ? ? ? ? 3.115 ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          GLU 
_struct_mon_prot_cis.label_seq_id           30 
_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           GLU 
_struct_mon_prot_cis.auth_seq_id            30 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    31 
_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    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     31 
_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       7.72 
# 
_struct_sheet.id               A 
_struct_sheet.type             ? 
_struct_sheet.number_strands   4 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2 ? anti-parallel 
A 2 3 ? anti-parallel 
A 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 VAL A 67 ? LEU A 73 ? VAL A 67 LEU A 73 
A 2 LYS A 5  ? VAL A 11 ? LYS A 5  VAL A 11 
A 3 LEU A 44 ? THR A 49 ? LEU A 44 THR A 49 
A 4 VAL A 33 ? SER A 39 ? VAL A 33 SER A 39 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2 O ARG A 68 ? O ARG A 68 N ASN A 10 ? N ASN A 10 
A 2 3 O LYS A 5  ? O LYS A 5  N THR A 49 ? N THR A 49 
A 3 4 O LEU A 44 ? O LEU A 44 N SER A 39 ? N SER A 39 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE HG A 74'   
AC2 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE BEN A 186' 
AC3 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE BEN A 187' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 3 THR A 14 ? THR A 14   . ? 1_555 ? 
2  AC1 3 CYS A 15 ? CYS A 15   . ? 1_555 ? 
3  AC1 3 CYS A 18 ? CYS A 18   . ? 1_555 ? 
4  AC2 8 ILE A 4  ? ILE A 4    . ? 4_546 ? 
5  AC2 8 ASN A 23 ? ASN A 23   . ? 1_555 ? 
6  AC2 8 GLU A 30 ? GLU A 30   . ? 1_555 ? 
7  AC2 8 VAL A 33 ? VAL A 33   . ? 1_555 ? 
8  AC2 8 SER A 34 ? SER A 34   . ? 1_555 ? 
9  AC2 8 ILE A 36 ? ILE A 36   . ? 1_555 ? 
10 AC2 8 LEU A 73 ? LEU A 73   . ? 4_546 ? 
11 AC2 8 HOH E .  ? HOH A 1002 . ? 4_546 ? 
12 AC3 7 MET A 13 ? MET A 13   . ? 2_555 ? 
13 AC3 7 LEU A 40 ? LEU A 40   . ? 1_555 ? 
14 AC3 7 GLN A 43 ? GLN A 43   . ? 2_555 ? 
15 AC3 7 GLU A 58 ? GLU A 58   . ? 3_445 ? 
16 AC3 7 HOH E .  ? HOH A 1039 . ? 1_555 ? 
17 AC3 7 HOH E .  ? HOH A 1100 . ? 3_445 ? 
18 AC3 7 HOH E .  ? HOH A 1109 . ? 3_445 ? 
# 
_database_PDB_matrix.entry_id          1CC8 
_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                    1CC8 
_atom_sites.fract_transf_matrix[1][1]   0.017652 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.008168 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.033784 
_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]   0.027026 
_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  
HG 
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   . ALA A 1 2  ? 14.789 27.073 24.130 1.00 28.86 ? 2    ALA A N   1 
ATOM   2   C  CA  . ALA A 1 2  ? 13.936 25.892 24.216 1.00 7.09  ? 2    ALA A CA  1 
ATOM   3   C  C   . ALA A 1 2  ? 12.753 25.845 23.241 1.00 5.37  ? 2    ALA A C   1 
ATOM   4   O  O   . ALA A 1 2  ? 11.656 25.370 23.562 1.00 5.46  ? 2    ALA A O   1 
ATOM   5   C  CB  . ALA A 1 2  ? 13.383 25.878 25.624 1.00 9.53  ? 2    ALA A CB  1 
ATOM   6   N  N   . GLU A 1 3  ? 12.966 26.360 22.030 1.00 5.21  ? 3    GLU A N   1 
ATOM   7   C  CA  . GLU A 1 3  ? 11.910 26.317 21.014 1.00 4.69  ? 3    GLU A CA  1 
ATOM   8   C  C   . GLU A 1 3  ? 11.584 24.887 20.616 1.00 4.64  ? 3    GLU A C   1 
ATOM   9   O  O   . GLU A 1 3  ? 12.499 24.101 20.325 1.00 5.46  ? 3    GLU A O   1 
ATOM   10  C  CB  . GLU A 1 3  ? 12.285 27.145 19.781 1.00 5.64  ? 3    GLU A CB  1 
ATOM   11  C  CG  . GLU A 1 3  ? 11.115 27.144 18.789 1.00 5.94  ? 3    GLU A CG  1 
ATOM   12  C  CD  . GLU A 1 3  ? 11.234 27.841 17.482 1.00 7.46  ? 3    GLU A CD  1 
ATOM   13  O  OE1 . GLU A 1 3  ? 12.372 28.263 17.151 1.00 9.12  ? 3    GLU A OE1 1 
ATOM   14  O  OE2 . GLU A 1 3  ? 10.207 27.911 16.746 1.00 9.19  ? 3    GLU A OE2 1 
ATOM   15  N  N   . ILE A 1 4  ? 10.277 24.574 20.552 1.00 4.55  ? 4    ILE A N   1 
ATOM   16  C  CA  . ILE A 1 4  ? 9.792  23.327 19.967 1.00 4.41  ? 4    ILE A CA  1 
ATOM   17  C  C   . ILE A 1 4  ? 9.357  23.647 18.539 1.00 3.83  ? 4    ILE A C   1 
ATOM   18  O  O   . ILE A 1 4  ? 8.328  24.276 18.300 1.00 4.78  ? 4    ILE A O   1 
ATOM   19  C  CB  . ILE A 1 4  ? 8.616  22.720 20.759 1.00 4.48  ? 4    ILE A CB  1 
ATOM   20  C  CG1 . ILE A 1 4  ? 9.056  22.448 22.225 1.00 6.39  ? 4    ILE A CG1 1 
ATOM   21  C  CG2 . ILE A 1 4  ? 8.114  21.449 20.085 1.00 5.34  ? 4    ILE A CG2 1 
ATOM   22  C  CD1 . ILE A 1 4  ? 7.923  21.909 23.050 1.00 7.37  ? 4    ILE A CD1 1 
ATOM   23  N  N   . LYS A 1 5  ? 10.227 23.280 17.593 1.00 3.51  ? 5    LYS A N   1 
ATOM   24  C  CA  . LYS A 1 5  ? 10.013 23.554 16.172 1.00 4.17  ? 5    LYS A CA  1 
ATOM   25  C  C   . LYS A 1 5  ? 9.068  22.515 15.567 1.00 3.86  ? 5    LYS A C   1 
ATOM   26  O  O   . LYS A 1 5  ? 8.929  21.410 16.084 1.00 5.26  ? 5    LYS A O   1 
ATOM   27  C  CB  . LYS A 1 5  ? 11.389 23.588 15.457 1.00 5.00  ? 5    LYS A CB  1 
ATOM   28  C  CG  . LYS A 1 5  ? 12.243 24.756 15.882 1.00 10.43 ? 5    LYS A CG  1 
ATOM   29  C  CD  . LYS A 1 5  ? 13.682 24.802 15.533 1.00 14.61 ? 5    LYS A CD  1 
ATOM   30  C  CE  . LYS A 1 5  ? 14.575 23.992 16.439 1.00 19.41 ? 5    LYS A CE  1 
ATOM   31  N  NZ  . LYS A 1 5  ? 13.965 22.712 16.893 1.00 38.72 ? 5    LYS A NZ  1 
ATOM   32  N  N   . HIS A 1 6  ? 8.414  22.903 14.476 1.00 4.20  ? 6    HIS A N   1 
ATOM   33  C  CA  . HIS A 1 6  ? 7.540  22.053 13.674 1.00 3.60  ? 6    HIS A CA  1 
ATOM   34  C  C   . HIS A 1 6  ? 8.176  21.829 12.290 1.00 3.74  ? 6    HIS A C   1 
ATOM   35  O  O   . HIS A 1 6  ? 8.293  22.786 11.525 1.00 4.69  ? 6    HIS A O   1 
ATOM   36  C  CB  . HIS A 1 6  ? 6.136  22.626 13.528 1.00 4.74  ? 6    HIS A CB  1 
ATOM   37  C  CG  . HIS A 1 6  ? 5.147  21.852 12.719 1.00 4.34  ? 6    HIS A CG  1 
ATOM   38  N  ND1 . HIS A 1 6  ? 5.251  20.647 12.086 1.00 5.78  ? 6    HIS A ND1 1 
ATOM   39  C  CD2 . HIS A 1 6  ? 3.856  22.252 12.484 1.00 4.30  ? 6    HIS A CD2 1 
ATOM   40  C  CE1 . HIS A 1 6  ? 4.074  20.410 11.477 1.00 4.14  ? 6    HIS A CE1 1 
ATOM   41  N  NE2 . HIS A 1 6  ? 3.203  21.352 11.720 1.00 6.28  ? 6    HIS A NE2 1 
ATOM   42  N  N   . TYR A 1 7  ? 8.581  20.599 12.002 1.00 3.70  ? 7    TYR A N   1 
ATOM   43  C  CA  . TYR A 1 7  ? 9.081  20.238 10.683 1.00 3.68  ? 7    TYR A CA  1 
ATOM   44  C  C   . TYR A 1 7  ? 8.048  19.325 10.003 1.00 3.44  ? 7    TYR A C   1 
ATOM   45  O  O   . TYR A 1 7  ? 7.392  18.521 10.659 1.00 4.30  ? 7    TYR A O   1 
ATOM   46  C  CB  . TYR A 1 7  ? 10.440 19.521 10.802 1.00 4.48  ? 7    TYR A CB  1 
ATOM   47  C  CG  . TYR A 1 7  ? 11.482 20.202 11.665 1.00 4.07  ? 7    TYR A CG  1 
ATOM   48  C  CD1 . TYR A 1 7  ? 11.674 21.578 11.669 1.00 4.66  ? 7    TYR A CD1 1 
ATOM   49  C  CD2 . TYR A 1 7  ? 12.357 19.470 12.474 1.00 4.94  ? 7    TYR A CD2 1 
ATOM   50  C  CE1 . TYR A 1 7  ? 12.647 22.202 12.431 1.00 4.54  ? 7    TYR A CE1 1 
ATOM   51  C  CE2 . TYR A 1 7  ? 13.324 20.066 13.279 1.00 4.87  ? 7    TYR A CE2 1 
ATOM   52  C  CZ  . TYR A 1 7  ? 13.466 21.438 13.270 1.00 4.69  ? 7    TYR A CZ  1 
ATOM   53  O  OH  . TYR A 1 7  ? 14.414 22.059 14.069 1.00 5.73  ? 7    TYR A OH  1 
ATOM   54  N  N   . GLN A 1 8  ? 7.900  19.488 8.690  1.00 4.23  ? 8    GLN A N   1 
ATOM   55  C  CA  . GLN A 1 8  ? 6.984  18.675 7.906  1.00 4.23  ? 8    GLN A CA  1 
ATOM   56  C  C   . GLN A 1 8  ? 7.702  18.097 6.697  1.00 4.30  ? 8    GLN A C   1 
ATOM   57  O  O   . GLN A 1 8  ? 8.315  18.866 5.973  1.00 6.24  ? 8    GLN A O   1 
ATOM   58  C  CB  . GLN A 1 8  ? 5.747  19.471 7.480  1.00 5.22  ? 8    GLN A CB  1 
ATOM   59  C  CG  . GLN A 1 8  ? 4.683  18.663 6.730  1.00 6.71  ? 8    GLN A CG  1 
ATOM   60  C  CD  . GLN A 1 8  ? 3.461  19.514 6.448  1.00 7.46  ? 8    GLN A CD  1 
ATOM   61  O  OE1 . GLN A 1 8  ? 2.537  19.647 7.282  1.00 11.25 ? 8    GLN A OE1 1 
ATOM   62  N  NE2 . GLN A 1 8  ? 3.448  20.133 5.292  1.00 10.93 ? 8    GLN A NE2 1 
ATOM   63  N  N   . PHE A 1 9  ? 7.536  16.798 6.484  1.00 3.95  ? 9    PHE A N   1 
ATOM   64  C  CA  . PHE A 1 9  ? 8.208  16.090 5.384  1.00 4.45  ? 9    PHE A CA  1 
ATOM   65  C  C   . PHE A 1 9  ? 7.179  15.323 4.556  1.00 4.13  ? 9    PHE A C   1 
ATOM   66  O  O   . PHE A 1 9  ? 6.279  14.697 5.098  1.00 5.48  ? 9    PHE A O   1 
ATOM   67  C  CB  . PHE A 1 9  ? 9.242  15.114 5.962  1.00 4.49  ? 9    PHE A CB  1 
ATOM   68  C  CG  . PHE A 1 9  ? 10.265 15.755 6.880  1.00 4.88  ? 9    PHE A CG  1 
ATOM   69  C  CD1 . PHE A 1 9  ? 11.412 16.392 6.406  1.00 5.28  ? 9    PHE A CD1 1 
ATOM   70  C  CD2 . PHE A 1 9  ? 10.059 15.727 8.257  1.00 5.24  ? 9    PHE A CD2 1 
ATOM   71  C  CE1 . PHE A 1 9  ? 12.307 16.969 7.285  1.00 6.64  ? 9    PHE A CE1 1 
ATOM   72  C  CE2 . PHE A 1 9  ? 10.965 16.277 9.125  1.00 5.56  ? 9    PHE A CE2 1 
ATOM   73  C  CZ  . PHE A 1 9  ? 12.080 16.938 8.652  1.00 5.81  ? 9    PHE A CZ  1 
ATOM   74  N  N   . ASN A 1 10 ? 7.351  15.309 3.240  1.00 4.40  ? 10   ASN A N   1 
ATOM   75  C  CA  . ASN A 1 10 ? 6.641  14.398 2.343  1.00 4.49  ? 10   ASN A CA  1 
ATOM   76  C  C   . ASN A 1 10 ? 7.530  13.156 2.194  1.00 4.59  ? 10   ASN A C   1 
ATOM   77  O  O   . ASN A 1 10 ? 8.627  13.265 1.622  1.00 5.32  ? 10   ASN A O   1 
ATOM   78  C  CB  . ASN A 1 10 ? 6.348  15.062 1.000  1.00 5.76  ? 10   ASN A CB  1 
ATOM   79  C  CG  . ASN A 1 10 ? 5.675  14.199 -0.041 1.00 6.05  ? 10   ASN A CG  1 
ATOM   80  O  OD1 . ASN A 1 10 ? 4.979  13.198 0.211  1.00 7.78  ? 10   ASN A OD1 1 
ATOM   81  N  ND2 . ASN A 1 10 ? 5.899  14.580 -1.288 1.00 7.65  ? 10   ASN A ND2 1 
ATOM   82  N  N   . VAL A 1 11 ? 7.086  12.065 2.788  1.00 4.41  ? 11   VAL A N   1 
ATOM   83  C  CA  . VAL A 1 11 ? 7.845  10.816 2.846  1.00 4.79  ? 11   VAL A CA  1 
ATOM   84  C  C   . VAL A 1 11 ? 7.007  9.732  2.173  1.00 4.57  ? 11   VAL A C   1 
ATOM   85  O  O   . VAL A 1 11 ? 5.803  9.600  2.453  1.00 4.84  ? 11   VAL A O   1 
ATOM   86  C  CB  . VAL A 1 11 ? 8.187  10.397 4.300  1.00 5.11  ? 11   VAL A CB  1 
ATOM   87  C  CG1 . VAL A 1 11 ? 9.089  9.179  4.298  1.00 5.76  ? 11   VAL A CG1 1 
ATOM   88  C  CG2 . VAL A 1 11 ? 8.858  11.533 5.058  1.00 5.19  ? 11   VAL A CG2 1 
ATOM   89  N  N   . VAL A 1 12 ? 7.635  8.994  1.247  1.00 5.69  ? 12   VAL A N   1 
ATOM   90  C  CA  . VAL A 1 12 ? 6.931  7.906  0.557  1.00 5.14  ? 12   VAL A CA  1 
ATOM   91  C  C   . VAL A 1 12 ? 6.780  6.711  1.489  1.00 4.76  ? 12   VAL A C   1 
ATOM   92  O  O   . VAL A 1 12 ? 7.775  6.137  1.954  1.00 6.29  ? 12   VAL A O   1 
ATOM   93  C  CB  . VAL A 1 12 ? 7.675  7.506  -0.719 1.00 5.87  ? 12   VAL A CB  1 
ATOM   94  C  CG1 . VAL A 1 12 ? 6.907  6.395  -1.438 1.00 7.21  ? 12   VAL A CG1 1 
ATOM   95  C  CG2 . VAL A 1 12 ? 7.845  8.724  -1.608 1.00 7.08  ? 12   VAL A CG2 1 
ATOM   96  N  N   . MET A 1 13 ? 5.518  6.379  1.759  1.00 4.92  ? 13   MET A N   1 
ATOM   97  C  CA  . MET A 1 13 ? 5.214  5.328  2.724  1.00 5.27  ? 13   MET A CA  1 
ATOM   98  C  C   . MET A 1 13 ? 4.120  4.418  2.161  1.00 5.44  ? 13   MET A C   1 
ATOM   99  O  O   . MET A 1 13 ? 2.958  4.792  1.978  1.00 6.39  ? 13   MET A O   1 
ATOM   100 C  CB  . MET A 1 13 ? 4.731  5.986  4.027  1.00 5.36  ? 13   MET A CB  1 
ATOM   101 C  CG  . MET A 1 13 ? 5.808  6.810  4.714  1.00 5.58  ? 13   MET A CG  1 
ATOM   102 S  SD  . MET A 1 13 ? 5.246  7.725  6.162  1.00 6.11  ? 13   MET A SD  1 
ATOM   103 C  CE  . MET A 1 13 ? 4.146  8.929  5.403  1.00 5.55  ? 13   MET A CE  1 
ATOM   104 N  N   . THR A 1 14 ? 4.518  3.205  1.742  1.00 6.28  ? 14   THR A N   1 
ATOM   105 C  CA  . THR A 1 14 ? 3.640  2.362  0.936  1.00 7.51  ? 14   THR A CA  1 
ATOM   106 C  C   . THR A 1 14 ? 2.710  1.491  1.778  1.00 8.27  ? 14   THR A C   1 
ATOM   107 O  O   . THR A 1 14 ? 1.795  0.867  1.231  1.00 10.62 ? 14   THR A O   1 
ATOM   108 C  CB  . THR A 1 14 ? 4.490  1.444  0.012  1.00 8.43  ? 14   THR A CB  1 
ATOM   109 O  OG1 . THR A 1 14 ? 5.248  0.531  0.824  1.00 10.67 ? 14   THR A OG1 1 
ATOM   110 C  CG2 . THR A 1 14 ? 5.476  2.261  -0.802 1.00 10.68 ? 14   THR A CG2 1 
ATOM   111 N  N   . CYS A 1 15 ? 3.027  1.377  3.058  1.00 8.39  ? 15   CYS A N   1 
ATOM   112 C  CA  . CYS A 1 15 ? 2.334  0.492  3.979  1.00 9.33  ? 15   CYS A CA  1 
ATOM   113 C  C   . CYS A 1 15 ? 2.633  0.942  5.409  1.00 8.05  ? 15   CYS A C   1 
ATOM   114 O  O   . CYS A 1 15 ? 3.538  1.770  5.603  1.00 6.65  ? 15   CYS A O   1 
ATOM   115 C  CB  . CYS A 1 15 ? 2.717  -0.959 3.746  1.00 10.10 ? 15   CYS A CB  1 
ATOM   116 S  SG  . CYS A 1 15 ? 4.295  -1.582 4.367  1.00 10.15 ? 15   CYS A SG  1 
ATOM   117 N  N   . SER A 1 16 ? 1.954  0.326  6.368  1.00 8.76  ? 16   SER A N   1 
ATOM   118 C  CA  . SER A 1 16 ? 2.236  0.634  7.770  1.00 8.96  ? 16   SER A CA  1 
ATOM   119 C  C   . SER A 1 16 ? 3.663  0.355  8.226  1.00 7.75  ? 16   SER A C   1 
ATOM   120 O  O   . SER A 1 16 ? 4.136  0.918  9.229  1.00 9.28  ? 16   SER A O   1 
ATOM   121 C  CB  . SER A 1 16 ? 1.256  -0.115 8.679  1.00 9.60  ? 16   SER A CB  1 
ATOM   122 O  OG  . SER A 1 16 ? 1.457  -1.531 8.602  1.00 11.11 ? 16   SER A OG  1 
ATOM   123 N  N   . GLY A 1 17 ? 4.400  -0.515 7.533  1.00 7.54  ? 17   GLY A N   1 
ATOM   124 C  CA  . GLY A 1 17 ? 5.791  -0.751 7.871  1.00 8.10  ? 17   GLY A CA  1 
ATOM   125 C  C   . GLY A 1 17 ? 6.672  0.451  7.612  1.00 7.08  ? 17   GLY A C   1 
ATOM   126 O  O   . GLY A 1 17 ? 7.716  0.674  8.236  1.00 8.01  ? 17   GLY A O   1 
ATOM   127 N  N   . CYS A 1 18 ? 6.290  1.268  6.628  1.00 6.44  ? 18   CYS A N   1 
ATOM   128 C  CA  . CYS A 1 18 ? 7.064  2.467  6.286  1.00 5.96  ? 18   CYS A CA  1 
ATOM   129 C  C   . CYS A 1 18 ? 6.862  3.548  7.327  1.00 5.04  ? 18   CYS A C   1 
ATOM   130 O  O   . CYS A 1 18 ? 7.814  4.249  7.732  1.00 6.10  ? 18   CYS A O   1 
ATOM   131 C  CB  . CYS A 1 18 ? 6.718  2.964  4.889  1.00 6.15  ? 18   CYS A CB  1 
ATOM   132 S  SG  . CYS A 1 18 ? 7.264  1.891  3.548  1.00 7.81  ? 18   CYS A SG  1 
ATOM   133 N  N   . SER A 1 19 ? 5.606  3.800  7.697  1.00 6.33  ? 19   SER A N   1 
ATOM   134 C  CA  . SER A 1 19 ? 5.358  4.696  8.833  1.00 6.04  ? 19   SER A CA  1 
ATOM   135 C  C   . SER A 1 19 ? 6.083  4.200  10.078 1.00 5.93  ? 19   SER A C   1 
ATOM   136 O  O   . SER A 1 19 ? 6.623  4.991  10.852 1.00 6.00  ? 19   SER A O   1 
ATOM   137 C  CB  . SER A 1 19 ? 3.860  4.890  9.023  1.00 7.59  ? 19   SER A CB  1 
ATOM   138 O  OG  . SER A 1 19 ? 3.166  3.680  9.117  1.00 11.58 ? 19   SER A OG  1 
ATOM   139 N  N   . GLY A 1 20 ? 6.124  2.886  10.277 1.00 6.30  ? 20   GLY A N   1 
ATOM   140 C  CA  . GLY A 1 20 ? 6.834  2.327  11.416 1.00 6.25  ? 20   GLY A CA  1 
ATOM   141 C  C   . GLY A 1 20 ? 8.328  2.590  11.400 1.00 4.99  ? 20   GLY A C   1 
ATOM   142 O  O   . GLY A 1 20 ? 8.953  2.898  12.415 1.00 5.60  ? 20   GLY A O   1 
ATOM   143 N  N   . ALA A 1 21 ? 8.953  2.496  10.228 1.00 5.53  ? 21   ALA A N   1 
ATOM   144 C  CA  . ALA A 1 21 ? 10.391 2.781  10.119 1.00 5.58  ? 21   ALA A CA  1 
ATOM   145 C  C   . ALA A 1 21 ? 10.720 4.212  10.519 1.00 5.14  ? 21   ALA A C   1 
ATOM   146 O  O   . ALA A 1 21 ? 11.712 4.502  11.209 1.00 6.37  ? 21   ALA A O   1 
ATOM   147 C  CB  . ALA A 1 21 ? 10.850 2.513  8.682  1.00 7.58  ? 21   ALA A CB  1 
ATOM   148 N  N   . VAL A 1 22 ? 9.857  5.130  10.078 1.00 5.02  ? 22   VAL A N   1 
ATOM   149 C  CA  . VAL A 1 22 ? 10.040 6.556  10.372 1.00 4.77  ? 22   VAL A CA  1 
ATOM   150 C  C   . VAL A 1 22 ? 9.831  6.826  11.860 1.00 4.59  ? 22   VAL A C   1 
ATOM   151 O  O   . VAL A 1 22 ? 10.646 7.492  12.522 1.00 5.27  ? 22   VAL A O   1 
ATOM   152 C  CB  . VAL A 1 22 ? 9.108  7.430  9.515  1.00 5.94  ? 22   VAL A CB  1 
ATOM   153 C  CG1 . VAL A 1 22 ? 9.206  8.885  9.956  1.00 7.21  ? 22   VAL A CG1 1 
ATOM   154 C  CG2 . VAL A 1 22 ? 9.459  7.289  8.033  1.00 7.21  ? 22   VAL A CG2 1 
ATOM   155 N  N   . ASN A 1 23 ? 8.708  6.292  12.389 1.00 4.92  ? 23   ASN A N   1 
ATOM   156 C  CA  . ASN A 1 23 ? 8.471  6.397  13.835 1.00 5.51  ? 23   ASN A CA  1 
ATOM   157 C  C   . ASN A 1 23 ? 9.691  5.925  14.628 1.00 5.44  ? 23   ASN A C   1 
ATOM   158 O  O   . ASN A 1 23 ? 10.105 6.590  15.603 1.00 5.52  ? 23   ASN A O   1 
ATOM   159 C  CB  . ASN A 1 23 ? 7.218  5.626  14.249 1.00 5.64  ? 23   ASN A CB  1 
ATOM   160 C  CG  . ASN A 1 23 ? 6.934  5.642  15.753 1.00 6.65  ? 23   ASN A CG  1 
ATOM   161 O  OD1 . ASN A 1 23 ? 6.558  6.672  16.303 1.00 10.39 ? 23   ASN A OD1 1 
ATOM   162 N  ND2 . ASN A 1 23 ? 7.197  4.535  16.408 1.00 8.82  ? 23   ASN A ND2 1 
ATOM   163 N  N   . LYS A 1 24 ? 10.259 4.779  14.263 1.00 5.51  ? 24   LYS A N   1 
ATOM   164 C  CA  . LYS A 1 24 ? 11.332 4.190  15.054 1.00 6.02  ? 24   LYS A CA  1 
ATOM   165 C  C   . LYS A 1 24 ? 12.521 5.141  15.236 1.00 5.39  ? 24   LYS A C   1 
ATOM   166 O  O   . LYS A 1 24 ? 13.033 5.305  16.338 1.00 5.77  ? 24   LYS A O   1 
ATOM   167 C  CB  . LYS A 1 24 ? 11.821 2.881  14.486 1.00 7.49  ? 24   LYS A CB  1 
ATOM   168 C  CG  . LYS A 1 24 ? 12.868 2.168  15.338 1.00 13.79 ? 24   LYS A CG  1 
ATOM   169 C  CD  . LYS A 1 24 ? 13.823 1.380  14.466 1.00 21.11 ? 24   LYS A CD  1 
ATOM   170 C  CE  . LYS A 1 24 ? 13.099 0.289  13.687 1.00 23.71 ? 24   LYS A CE  1 
ATOM   171 N  NZ  . LYS A 1 24 ? 13.010 -0.923 14.546 1.00 19.24 ? 24   LYS A NZ  1 
ATOM   172 N  N   . VAL A 1 25 ? 12.958 5.793  14.149 1.00 5.74  ? 25   VAL A N   1 
ATOM   173 C  CA  . VAL A 1 25 ? 14.159 6.615  14.288 1.00 6.80  ? 25   VAL A CA  1 
ATOM   174 C  C   . VAL A 1 25 ? 13.874 7.828  15.168 1.00 5.58  ? 25   VAL A C   1 
ATOM   175 O  O   . VAL A 1 25 ? 14.738 8.286  15.909 1.00 6.67  ? 25   VAL A O   1 
ATOM   176 C  CB  . VAL A 1 25 ? 14.779 6.948  12.942 1.00 9.44  ? 25   VAL A CB  1 
ATOM   177 C  CG1 . VAL A 1 25 ? 15.106 5.708  12.118 1.00 14.83 ? 25   VAL A CG1 1 
ATOM   178 C  CG2 . VAL A 1 25 ? 13.941 7.890  12.120 1.00 13.52 ? 25   VAL A CG2 1 
ATOM   179 N  N   . LEU A 1 26 ? 12.607 8.278  15.186 1.00 5.40  ? 26   LEU A N   1 
ATOM   180 C  CA  . LEU A 1 26 ? 12.211 9.404  15.997 1.00 5.73  ? 26   LEU A CA  1 
ATOM   181 C  C   . LEU A 1 26 ? 12.097 9.024  17.468 1.00 4.54  ? 26   LEU A C   1 
ATOM   182 O  O   . LEU A 1 26 ? 12.433 9.825  18.348 1.00 5.61  ? 26   LEU A O   1 
ATOM   183 C  CB  . LEU A 1 26 ? 10.967 10.060 15.392 1.00 6.79  ? 26   LEU A CB  1 
ATOM   184 C  CG  . LEU A 1 26 ? 11.135 10.585 13.951 1.00 7.50  ? 26   LEU A CG  1 
ATOM   185 C  CD1 . LEU A 1 26 ? 9.823  10.920 13.288 1.00 8.21  ? 26   LEU A CD1 1 
ATOM   186 C  CD2 . LEU A 1 26 ? 12.045 11.806 13.984 1.00 13.14 ? 26   LEU A CD2 1 
ATOM   187 N  N   . THR A 1 27 ? 11.701 7.795  17.775 1.00 4.84  ? 27   THR A N   1 
ATOM   188 C  CA  . THR A 1 27 ? 11.660 7.318  19.140 1.00 4.91  ? 27   THR A CA  1 
ATOM   189 C  C   . THR A 1 27 ? 13.061 7.340  19.777 1.00 5.26  ? 27   THR A C   1 
ATOM   190 O  O   . THR A 1 27 ? 13.190 7.539  20.985 1.00 7.27  ? 27   THR A O   1 
ATOM   191 C  CB  . THR A 1 27 ? 11.031 5.927  19.297 1.00 4.80  ? 27   THR A CB  1 
ATOM   192 O  OG1 . THR A 1 27 ? 11.875 4.886  18.782 1.00 5.86  ? 27   THR A OG1 1 
ATOM   193 C  CG2 . THR A 1 27 ? 9.633  5.892  18.697 1.00 5.09  ? 27   THR A CG2 1 
ATOM   194 N  N   . LYS A 1 28 ? 14.129 7.151  18.978 1.00 5.15  ? 28   LYS A N   1 
ATOM   195 C  CA  . LYS A 1 28 ? 15.502 7.146  19.514 1.00 5.58  ? 28   LYS A CA  1 
ATOM   196 C  C   . LYS A 1 28 ? 16.002 8.541  19.899 1.00 5.24  ? 28   LYS A C   1 
ATOM   197 O  O   . LYS A 1 28 ? 17.062 8.685  20.541 1.00 6.08  ? 28   LYS A O   1 
ATOM   198 C  CB  . LYS A 1 28 ? 16.442 6.491  18.496 1.00 7.41  ? 28   LYS A CB  1 
ATOM   199 C  CG  . LYS A 1 28 ? 16.115 5.046  18.223 1.00 9.30  ? 28   LYS A CG  1 
ATOM   200 C  CD  . LYS A 1 28 ? 16.916 4.385  17.131 1.00 14.46 ? 28   LYS A CD  1 
ATOM   201 C  CE  . LYS A 1 28 ? 16.469 2.959  16.857 1.00 19.20 ? 28   LYS A CE  1 
ATOM   202 N  NZ  . LYS A 1 28 ? 17.498 2.216  16.081 1.00 21.45 ? 28   LYS A NZ  1 
ATOM   203 N  N   . LEU A 1 29 ? 15.228 9.564  19.537 1.00 4.98  ? 29   LEU A N   1 
ATOM   204 C  CA  . LEU A 1 29 ? 15.543 10.949 19.817 1.00 5.42  ? 29   LEU A CA  1 
ATOM   205 C  C   . LEU A 1 29 ? 14.716 11.541 20.962 1.00 5.33  ? 29   LEU A C   1 
ATOM   206 O  O   . LEU A 1 29 ? 14.833 12.714 21.273 1.00 5.99  ? 29   LEU A O   1 
ATOM   207 C  CB  . LEU A 1 29 ? 15.436 11.771 18.535 1.00 5.37  ? 29   LEU A CB  1 
ATOM   208 C  CG  . LEU A 1 29 ? 16.264 11.218 17.377 1.00 5.54  ? 29   LEU A CG  1 
ATOM   209 C  CD1 . LEU A 1 29 ? 16.093 12.128 16.161 1.00 6.17  ? 29   LEU A CD1 1 
ATOM   210 C  CD2 . LEU A 1 29 ? 17.747 11.058 17.729 1.00 6.36  ? 29   LEU A CD2 1 
ATOM   211 N  N   . GLU A 1 30 ? 13.925 10.695 21.602 1.00 5.99  ? 30   GLU A N   1 
ATOM   212 C  CA  . GLU A 1 30 ? 13.314 11.080 22.870 1.00 6.54  ? 30   GLU A CA  1 
ATOM   213 C  C   . GLU A 1 30 ? 14.463 11.271 23.863 1.00 6.36  ? 30   GLU A C   1 
ATOM   214 O  O   . GLU A 1 30 ? 15.527 10.650 23.720 1.00 8.73  ? 30   GLU A O   1 
ATOM   215 C  CB  . GLU A 1 30 ? 12.272 10.029 23.289 1.00 7.28  ? 30   GLU A CB  1 
ATOM   216 C  CG  . GLU A 1 30 ? 11.065 9.945  22.397 1.00 7.04  ? 30   GLU A CG  1 
ATOM   217 C  CD  . GLU A 1 30 ? 10.040 8.905  22.814 1.00 7.01  ? 30   GLU A CD  1 
ATOM   218 O  OE1 . GLU A 1 30 ? 10.317 7.698  22.650 1.00 12.74 ? 30   GLU A OE1 1 
ATOM   219 O  OE2 . GLU A 1 30 ? 8.942  9.306  23.269 1.00 7.86  ? 30   GLU A OE2 1 
ATOM   220 N  N   . PRO A 1 31 ? 14.337 12.160 24.840 1.00 7.63  ? 31   PRO A N   1 
ATOM   221 C  CA  . PRO A 1 31 ? 13.114 12.891 25.169 1.00 7.72  ? 31   PRO A CA  1 
ATOM   222 C  C   . PRO A 1 31 ? 12.994 14.281 24.563 1.00 8.32  ? 31   PRO A C   1 
ATOM   223 O  O   . PRO A 1 31 ? 12.274 15.120 25.133 1.00 11.06 ? 31   PRO A O   1 
ATOM   224 C  CB  . PRO A 1 31 ? 13.224 12.992 26.707 1.00 11.03 ? 31   PRO A CB  1 
ATOM   225 C  CG  . PRO A 1 31 ? 14.695 13.178 26.943 1.00 13.28 ? 31   PRO A CG  1 
ATOM   226 C  CD  . PRO A 1 31 ? 15.367 12.371 25.878 1.00 11.83 ? 31   PRO A CD  1 
ATOM   227 N  N   . ASP A 1 32 ? 13.579 14.539 23.391 1.00 6.51  ? 32   ASP A N   1 
ATOM   228 C  CA  . ASP A 1 32 ? 13.521 15.839 22.747 1.00 6.56  ? 32   ASP A CA  1 
ATOM   229 C  C   . ASP A 1 32 ? 12.659 15.859 21.494 1.00 6.83  ? 32   ASP A C   1 
ATOM   230 O  O   . ASP A 1 32 ? 12.772 16.782 20.698 1.00 9.92  ? 32   ASP A O   1 
ATOM   231 C  CB  . ASP A 1 32 ? 14.926 16.413 22.506 1.00 8.05  ? 32   ASP A CB  1 
ATOM   232 C  CG  . ASP A 1 32 ? 15.590 16.813 23.818 1.00 11.95 ? 32   ASP A CG  1 
ATOM   233 O  OD1 . ASP A 1 32 ? 15.291 16.300 24.908 1.00 26.39 ? 32   ASP A OD1 1 
ATOM   234 O  OD2 . ASP A 1 32 ? 16.383 17.772 23.836 1.00 13.59 ? 32   ASP A OD2 1 
ATOM   235 N  N   . VAL A 1 33 ? 11.775 14.887 21.332 1.00 7.69  ? 33   VAL A N   1 
ATOM   236 C  CA  . VAL A 1 33 ? 10.718 14.857 20.308 1.00 7.03  ? 33   VAL A CA  1 
ATOM   237 C  C   . VAL A 1 33 ? 9.377  14.898 21.012 1.00 6.40  ? 33   VAL A C   1 
ATOM   238 O  O   . VAL A 1 33 ? 8.999  13.922 21.662 1.00 10.84 ? 33   VAL A O   1 
ATOM   239 C  CB  . VAL A 1 33 ? 10.831 13.691 19.325 1.00 7.83  ? 33   VAL A CB  1 
ATOM   240 C  CG1 . VAL A 1 33 ? 9.673  13.667 18.331 1.00 6.88  ? 33   VAL A CG1 1 
ATOM   241 C  CG2 . VAL A 1 33 ? 12.133 13.814 18.550 1.00 11.39 ? 33   VAL A CG2 1 
ATOM   242 N  N   . SER A 1 34 ? 8.664  16.001 20.938 1.00 5.62  ? 34   SER A N   1 
ATOM   243 C  CA  . SER A 1 34 ? 7.425  16.201 21.677 1.00 6.95  ? 34   SER A CA  1 
ATOM   244 C  C   . SER A 1 34 ? 6.210  15.507 21.054 1.00 5.57  ? 34   SER A C   1 
ATOM   245 O  O   . SER A 1 34 ? 5.281  15.082 21.768 1.00 7.44  ? 34   SER A O   1 
ATOM   246 C  CB  . SER A 1 34 ? 7.160  17.724 21.731 1.00 9.48  ? 34   SER A CB  1 
ATOM   247 O  OG  . SER A 1 34 ? 8.013  18.401 22.611 1.00 15.95 ? 34   SER A OG  1 
ATOM   248 N  N   . LYS A 1 35 ? 6.126  15.484 19.737 1.00 5.14  ? 35   LYS A N   1 
ATOM   249 C  CA  . LYS A 1 35 ? 4.946  14.943 19.029 1.00 4.72  ? 35   LYS A CA  1 
ATOM   250 C  C   . LYS A 1 35 ? 5.404  14.535 17.620 1.00 4.33  ? 35   LYS A C   1 
ATOM   251 O  O   . LYS A 1 35 ? 6.199  15.265 17.026 1.00 4.21  ? 35   LYS A O   1 
ATOM   252 C  CB  . LYS A 1 35 ? 3.816  15.989 18.911 1.00 4.66  ? 35   LYS A CB  1 
ATOM   253 C  CG  . LYS A 1 35 ? 2.568  15.547 18.178 1.00 6.06  ? 35   LYS A CG  1 
ATOM   254 C  CD  . LYS A 1 35 ? 1.454  16.559 18.094 1.00 6.76  ? 35   LYS A CD  1 
ATOM   255 C  CE  . LYS A 1 35 ? 0.161  16.082 17.487 1.00 13.41 ? 35   LYS A CE  1 
ATOM   256 N  NZ  . LYS A 1 35 ? -0.809 17.114 17.052 1.00 9.20  ? 35   LYS A NZ  1 
ATOM   257 N  N   . ILE A 1 36 ? 4.842  13.432 17.145 1.00 3.74  ? 36   ILE A N   1 
ATOM   258 C  CA  . ILE A 1 36 ? 4.917  13.124 15.726 1.00 3.98  ? 36   ILE A CA  1 
ATOM   259 C  C   . ILE A 1 36 ? 3.498  12.814 15.215 1.00 4.15  ? 36   ILE A C   1 
ATOM   260 O  O   . ILE A 1 36 ? 2.660  12.243 15.931 1.00 4.59  ? 36   ILE A O   1 
ATOM   261 C  CB  . ILE A 1 36 ? 5.913  12.015 15.376 1.00 5.76  ? 36   ILE A CB  1 
ATOM   262 C  CG1 . ILE A 1 36 ? 5.414  10.613 15.618 1.00 6.81  ? 36   ILE A CG1 1 
ATOM   263 C  CG2 . ILE A 1 36 ? 7.245  12.276 16.060 1.00 7.72  ? 36   ILE A CG2 1 
ATOM   264 C  CD1 . ILE A 1 36 ? 6.360  9.576  15.026 1.00 8.84  ? 36   ILE A CD1 1 
ATOM   265 N  N   . ASP A 1 37 ? 3.248  13.192 13.967 1.00 4.14  ? 37   ASP A N   1 
ATOM   266 C  CA  . ASP A 1 37 ? 1.997  12.842 13.257 1.00 4.17  ? 37   ASP A CA  1 
ATOM   267 C  C   . ASP A 1 37 ? 2.425  12.229 11.924 1.00 4.49  ? 37   ASP A C   1 
ATOM   268 O  O   . ASP A 1 37 ? 3.173  12.879 11.196 1.00 7.38  ? 37   ASP A O   1 
ATOM   269 C  CB  . ASP A 1 37 ? 1.072  14.019 13.057 1.00 6.66  ? 37   ASP A CB  1 
ATOM   270 C  CG  . ASP A 1 37 ? -0.283 13.788 12.438 1.00 8.48  ? 37   ASP A CG  1 
ATOM   271 O  OD1 . ASP A 1 37 ? -0.304 13.152 11.355 1.00 9.80  ? 37   ASP A OD1 1 
ATOM   272 O  OD2 . ASP A 1 37 ? -1.353 14.145 12.986 1.00 12.36 ? 37   ASP A OD2 1 
ATOM   273 N  N   . ILE A 1 38 ? 1.952  11.031 11.632 1.00 3.96  ? 38   ILE A N   1 
ATOM   274 C  CA  . ILE A 1 38 ? 2.213  10.420 10.324 1.00 4.50  ? 38   ILE A CA  1 
ATOM   275 C  C   . ILE A 1 38 ? 0.856  10.158 9.653  1.00 4.86  ? 38   ILE A C   1 
ATOM   276 O  O   . ILE A 1 38 ? -0.045 9.542  10.243 1.00 6.06  ? 38   ILE A O   1 
ATOM   277 C  CB  . ILE A 1 38 ? 3.081  9.159  10.426 1.00 4.97  ? 38   ILE A CB  1 
ATOM   278 C  CG1 . ILE A 1 38 ? 4.403  9.431  11.136 1.00 5.37  ? 38   ILE A CG1 1 
ATOM   279 C  CG2 . ILE A 1 38 ? 3.292  8.573  9.037  1.00 7.02  ? 38   ILE A CG2 1 
ATOM   280 C  CD1 . ILE A 1 38 ? 5.408  8.309  11.149 1.00 7.44  ? 38   ILE A CD1 1 
ATOM   281 N  N   . SER A 1 39 ? 0.670  10.666 8.442  1.00 5.46  ? 39   SER A N   1 
ATOM   282 C  CA  . SER A 1 39 ? -0.500 10.425 7.615  1.00 6.35  ? 39   SER A CA  1 
ATOM   283 C  C   . SER A 1 39 ? -0.137 9.699  6.321  1.00 5.67  ? 39   SER A C   1 
ATOM   284 O  O   . SER A 1 39 ? 0.532  10.250 5.451  1.00 6.22  ? 39   SER A O   1 
ATOM   285 C  CB  . SER A 1 39 ? -1.191 11.743 7.255  1.00 7.79  ? 39   SER A CB  1 
ATOM   286 O  OG  . SER A 1 39 ? -2.325 11.423 6.466  1.00 10.08 ? 39   SER A OG  1 
ATOM   287 N  N   . LEU A 1 40 ? -0.610 8.455  6.192  1.00 5.93  ? 40   LEU A N   1 
ATOM   288 C  CA  . LEU A 1 40 ? -0.479 7.742  4.937  1.00 6.41  ? 40   LEU A CA  1 
ATOM   289 C  C   . LEU A 1 40 ? -1.382 8.354  3.874  1.00 5.70  ? 40   LEU A C   1 
ATOM   290 O  O   . LEU A 1 40 ? -1.016 8.330  2.694  1.00 5.66  ? 40   LEU A O   1 
ATOM   291 C  CB  . LEU A 1 40 ? -0.768 6.250  5.096  1.00 7.84  ? 40   LEU A CB  1 
ATOM   292 C  CG  . LEU A 1 40 ? 0.080  5.489  6.129  1.00 8.63  ? 40   LEU A CG  1 
ATOM   293 C  CD1 . LEU A 1 40 ? -0.434 4.065  6.265  1.00 11.70 ? 40   LEU A CD1 1 
ATOM   294 C  CD2 . LEU A 1 40 ? 1.522  5.475  5.678  1.00 11.80 ? 40   LEU A CD2 1 
ATOM   295 N  N   . GLU A 1 41 ? -2.517 8.926  4.268  1.00 5.81  ? 41   GLU A N   1 
ATOM   296 C  CA  . GLU A 1 41 ? -3.484 9.528  3.350  1.00 5.95  ? 41   GLU A CA  1 
ATOM   297 C  C   . GLU A 1 41 ? -3.025 10.831 2.720  1.00 5.57  ? 41   GLU A C   1 
ATOM   298 O  O   . GLU A 1 41 ? -3.585 11.215 1.683  1.00 7.09  ? 41   GLU A O   1 
ATOM   299 C  CB  . GLU A 1 41 ? -4.833 9.741  4.064  1.00 8.35  ? 41   GLU A CB  1 
ATOM   300 C  CG  . GLU A 1 41 ? -5.456 8.460  4.547  1.00 13.01 ? 41   GLU A CG  1 
ATOM   301 C  CD  . GLU A 1 41 ? -5.146 7.988  5.946  1.00 26.08 ? 41   GLU A CD  1 
ATOM   302 O  OE1 . GLU A 1 41 ? -4.142 8.375  6.584  1.00 24.65 ? 41   GLU A OE1 1 
ATOM   303 O  OE2 . GLU A 1 41 ? -6.002 7.210  6.460  1.00 40.32 ? 41   GLU A OE2 1 
ATOM   304 N  N   . LYS A 1 42 ? -1.988 11.477 3.209  1.00 5.54  ? 42   LYS A N   1 
ATOM   305 C  CA  . LYS A 1 42 ? -1.344 12.665 2.737  1.00 6.26  ? 42   LYS A CA  1 
ATOM   306 C  C   . LYS A 1 42 ? 0.154  12.448 2.481  1.00 5.14  ? 42   LYS A C   1 
ATOM   307 O  O   . LYS A 1 42 ? 0.831  13.334 1.954  1.00 6.10  ? 42   LYS A O   1 
ATOM   308 C  CB  . LYS A 1 42 ? -1.589 13.856 3.630  1.00 7.64  ? 42   LYS A CB  1 
ATOM   309 C  CG  . LYS A 1 42 ? -3.024 14.308 3.780  1.00 12.24 ? 42   LYS A CG  1 
ATOM   310 C  CD  . LYS A 1 42 ? -3.230 15.579 4.520  1.00 17.13 ? 42   LYS A CD  1 
ATOM   311 C  CE  . LYS A 1 42 ? -2.426 16.805 4.204  1.00 26.23 ? 42   LYS A CE  1 
ATOM   312 N  NZ  . LYS A 1 42 ? -2.995 17.672 3.140  1.00 38.73 ? 42   LYS A NZ  1 
ATOM   313 N  N   . GLN A 1 43 ? 0.714  11.294 2.815  1.00 4.71  ? 43   GLN A N   1 
ATOM   314 C  CA  . GLN A 1 43 ? 2.130  10.995 2.696  1.00 4.94  ? 43   GLN A CA  1 
ATOM   315 C  C   . GLN A 1 43 ? 2.988  12.037 3.404  1.00 4.22  ? 43   GLN A C   1 
ATOM   316 O  O   . GLN A 1 43 ? 4.013  12.523 2.929  1.00 4.55  ? 43   GLN A O   1 
ATOM   317 C  CB  . GLN A 1 43 ? 2.563  10.738 1.243  1.00 5.01  ? 43   GLN A CB  1 
ATOM   318 C  CG  . GLN A 1 43 ? 1.816  9.592  0.584  1.00 4.93  ? 43   GLN A CG  1 
ATOM   319 C  CD  . GLN A 1 43 ? 2.384  8.230  0.903  1.00 5.18  ? 43   GLN A CD  1 
ATOM   320 O  OE1 . GLN A 1 43 ? 3.511  7.928  0.460  1.00 5.93  ? 43   GLN A OE1 1 
ATOM   321 N  NE2 . GLN A 1 43 ? 1.677  7.439  1.697  1.00 5.44  ? 43   GLN A NE2 1 
ATOM   322 N  N   . LEU A 1 44 ? 2.558  12.417 4.629  1.00 4.97  ? 44   LEU A N   1 
ATOM   323 C  CA  . LEU A 1 44 ? 3.171  13.463 5.406  1.00 5.15  ? 44   LEU A CA  1 
ATOM   324 C  C   . LEU A 1 44 ? 3.632  12.973 6.781  1.00 4.51  ? 44   LEU A C   1 
ATOM   325 O  O   . LEU A 1 44 ? 2.912  12.214 7.428  1.00 6.82  ? 44   LEU A O   1 
ATOM   326 C  CB  . LEU A 1 44 ? 2.200  14.612 5.600  1.00 7.77  ? 44   LEU A CB  1 
ATOM   327 C  CG  . LEU A 1 44 ? 1.927  15.518 4.401  1.00 8.90  ? 44   LEU A CG  1 
ATOM   328 C  CD1 . LEU A 1 44 ? 0.944  16.611 4.818  1.00 17.01 ? 44   LEU A CD1 1 
ATOM   329 C  CD2 . LEU A 1 44 ? 3.222  16.153 3.875  1.00 15.20 ? 44   LEU A CD2 1 
ATOM   330 N  N   . VAL A 1 45 ? 4.780  13.485 7.221  1.00 4.14  ? 45   VAL A N   1 
ATOM   331 C  CA  . VAL A 1 45 ? 5.355  13.271 8.547  1.00 4.23  ? 45   VAL A CA  1 
ATOM   332 C  C   . VAL A 1 45 ? 5.561  14.652 9.180  1.00 3.97  ? 45   VAL A C   1 
ATOM   333 O  O   . VAL A 1 45 ? 6.323  15.462 8.643  1.00 5.26  ? 45   VAL A O   1 
ATOM   334 C  CB  . VAL A 1 45 ? 6.684  12.497 8.507  1.00 4.71  ? 45   VAL A CB  1 
ATOM   335 C  CG1 . VAL A 1 45 ? 7.304  12.362 9.886  1.00 5.23  ? 45   VAL A CG1 1 
ATOM   336 C  CG2 . VAL A 1 45 ? 6.508  11.137 7.858  1.00 4.78  ? 45   VAL A CG2 1 
ATOM   337 N  N   . ASP A 1 46 ? 4.925  14.880 10.313 1.00 4.01  ? 46   ASP A N   1 
ATOM   338 C  CA  . ASP A 1 46 ? 5.096  16.123 11.085 1.00 3.99  ? 46   ASP A CA  1 
ATOM   339 C  C   . ASP A 1 46 ? 5.880  15.768 12.361 1.00 4.02  ? 46   ASP A C   1 
ATOM   340 O  O   . ASP A 1 46 ? 5.501  14.819 13.057 1.00 5.16  ? 46   ASP A O   1 
ATOM   341 C  CB  . ASP A 1 46 ? 3.742  16.750 11.416 1.00 5.32  ? 46   ASP A CB  1 
ATOM   342 C  CG  . ASP A 1 46 ? 3.037  17.265 10.181 1.00 6.74  ? 46   ASP A CG  1 
ATOM   343 O  OD1 . ASP A 1 46 ? 3.316  18.391 9.784  1.00 6.49  ? 46   ASP A OD1 1 
ATOM   344 O  OD2 . ASP A 1 46 ? 2.243  16.529 9.560  1.00 18.09 ? 46   ASP A OD2 1 
ATOM   345 N  N   . VAL A 1 47 ? 6.947  16.502 12.662 1.00 3.54  ? 47   VAL A N   1 
ATOM   346 C  CA  . VAL A 1 47 ? 7.827  16.302 13.811 1.00 3.66  ? 47   VAL A CA  1 
ATOM   347 C  C   . VAL A 1 47 ? 7.884  17.620 14.610 1.00 3.80  ? 47   VAL A C   1 
ATOM   348 O  O   . VAL A 1 47 ? 8.258  18.656 14.068 1.00 4.46  ? 47   VAL A O   1 
ATOM   349 C  CB  . VAL A 1 47 ? 9.258  15.899 13.423 1.00 4.33  ? 47   VAL A CB  1 
ATOM   350 C  CG1 . VAL A 1 47 ? 10.135 15.605 14.624 1.00 5.29  ? 47   VAL A CG1 1 
ATOM   351 C  CG2 . VAL A 1 47 ? 9.226  14.692 12.472 1.00 5.56  ? 47   VAL A CG2 1 
ATOM   352 N  N   . TYR A 1 48 ? 7.567  17.543 15.891 1.00 3.45  ? 48   TYR A N   1 
ATOM   353 C  CA  . TYR A 1 48 ? 7.676  18.685 16.808 1.00 3.47  ? 48   TYR A CA  1 
ATOM   354 C  C   . TYR A 1 48 ? 8.835  18.369 17.774 1.00 4.06  ? 48   TYR A C   1 
ATOM   355 O  O   . TYR A 1 48 ? 8.769  17.363 18.496 1.00 4.72  ? 48   TYR A O   1 
ATOM   356 C  CB  . TYR A 1 48 ? 6.345  18.905 17.547 1.00 4.10  ? 48   TYR A CB  1 
ATOM   357 C  CG  . TYR A 1 48 ? 5.176  19.220 16.626 1.00 4.15  ? 48   TYR A CG  1 
ATOM   358 C  CD1 . TYR A 1 48 ? 4.431  18.256 15.955 1.00 5.00  ? 48   TYR A CD1 1 
ATOM   359 C  CD2 . TYR A 1 48 ? 4.769  20.534 16.442 1.00 4.59  ? 48   TYR A CD2 1 
ATOM   360 C  CE1 . TYR A 1 48 ? 3.353  18.563 15.125 1.00 5.18  ? 48   TYR A CE1 1 
ATOM   361 C  CE2 . TYR A 1 48 ? 3.681  20.866 15.636 1.00 5.14  ? 48   TYR A CE2 1 
ATOM   362 C  CZ  . TYR A 1 48 ? 2.973  19.879 14.987 1.00 5.08  ? 48   TYR A CZ  1 
ATOM   363 O  OH  . TYR A 1 48 ? 1.857  20.154 14.194 1.00 6.20  ? 48   TYR A OH  1 
ATOM   364 N  N   . THR A 1 49 ? 9.906  19.161 17.726 1.00 3.81  ? 49   THR A N   1 
ATOM   365 C  CA  . THR A 1 49 ? 11.169 18.814 18.400 1.00 3.92  ? 49   THR A CA  1 
ATOM   366 C  C   . THR A 1 49 ? 12.013 20.050 18.689 1.00 4.19  ? 49   THR A C   1 
ATOM   367 O  O   . THR A 1 49 ? 11.956 21.042 17.968 1.00 3.96  ? 49   THR A O   1 
ATOM   368 C  CB  . THR A 1 49 ? 11.970 17.834 17.516 1.00 4.52  ? 49   THR A CB  1 
ATOM   369 O  OG1 . THR A 1 49 ? 13.221 17.453 18.106 1.00 5.03  ? 49   THR A OG1 1 
ATOM   370 C  CG2 . THR A 1 49 ? 12.315 18.462 16.167 1.00 5.25  ? 49   THR A CG2 1 
ATOM   371 N  N   . THR A 1 50 ? 12.913 19.952 19.682 1.00 4.48  ? 50   THR A N   1 
ATOM   372 C  CA  . THR A 1 50 ? 13.928 20.945 19.917 1.00 5.02  ? 50   THR A CA  1 
ATOM   373 C  C   . THR A 1 50 ? 15.200 20.746 19.096 1.00 5.07  ? 50   THR A C   1 
ATOM   374 O  O   . THR A 1 50 ? 16.070 21.623 19.098 1.00 7.29  ? 50   THR A O   1 
ATOM   375 C  CB  . THR A 1 50 ? 14.362 21.016 21.405 1.00 6.51  ? 50   THR A CB  1 
ATOM   376 O  OG1 . THR A 1 50 ? 14.931 19.739 21.710 1.00 8.44  ? 50   THR A OG1 1 
ATOM   377 C  CG2 . THR A 1 50 ? 13.185 21.317 22.301 1.00 8.28  ? 50   THR A CG2 1 
ATOM   378 N  N   . LEU A 1 51 ? 15.320 19.619 18.416 1.00 4.98  ? 51   LEU A N   1 
ATOM   379 C  CA  . LEU A 1 51 ? 16.532 19.238 17.697 1.00 4.77  ? 51   LEU A CA  1 
ATOM   380 C  C   . LEU A 1 51 ? 16.590 19.907 16.324 1.00 4.82  ? 51   LEU A C   1 
ATOM   381 O  O   . LEU A 1 51 ? 15.552 20.362 15.807 1.00 5.32  ? 51   LEU A O   1 
ATOM   382 C  CB  . LEU A 1 51 ? 16.588 17.715 17.560 1.00 5.46  ? 51   LEU A CB  1 
ATOM   383 C  CG  . LEU A 1 51 ? 16.556 16.962 18.887 1.00 4.93  ? 51   LEU A CG  1 
ATOM   384 C  CD1 . LEU A 1 51 ? 16.506 15.467 18.615 1.00 7.52  ? 51   LEU A CD1 1 
ATOM   385 C  CD2 . LEU A 1 51 ? 17.757 17.303 19.760 1.00 7.09  ? 51   LEU A CD2 1 
ATOM   386 N  N   . PRO A 1 52 ? 17.783 20.016 15.734 1.00 5.44  ? 52   PRO A N   1 
ATOM   387 C  CA  . PRO A 1 52 ? 17.915 20.746 14.478 1.00 5.79  ? 52   PRO A CA  1 
ATOM   388 C  C   . PRO A 1 52 ? 17.289 20.039 13.277 1.00 5.26  ? 52   PRO A C   1 
ATOM   389 O  O   . PRO A 1 52 ? 17.273 18.803 13.190 1.00 5.35  ? 52   PRO A O   1 
ATOM   390 C  CB  . PRO A 1 52 ? 19.416 20.919 14.283 1.00 9.74  ? 52   PRO A CB  1 
ATOM   391 C  CG  . PRO A 1 52 ? 20.130 20.292 15.405 1.00 9.41  ? 52   PRO A CG  1 
ATOM   392 C  CD  . PRO A 1 52 ? 19.101 19.700 16.309 1.00 6.08  ? 52   PRO A CD  1 
ATOM   393 N  N   . TYR A 1 53 ? 16.776 20.833 12.331 1.00 5.82  ? 53   TYR A N   1 
ATOM   394 C  CA  . TYR A 1 53 ? 16.162 20.346 11.105 1.00 5.57  ? 53   TYR A CA  1 
ATOM   395 C  C   . TYR A 1 53 ? 17.063 19.378 10.371 1.00 5.34  ? 53   TYR A C   1 
ATOM   396 O  O   . TYR A 1 53 ? 16.617 18.304 9.956  1.00 5.77  ? 53   TYR A O   1 
ATOM   397 C  CB  . TYR A 1 53 ? 15.781 21.541 10.213 1.00 5.54  ? 53   TYR A CB  1 
ATOM   398 C  CG  . TYR A 1 53 ? 15.187 21.118 8.892  1.00 5.61  ? 53   TYR A CG  1 
ATOM   399 C  CD1 . TYR A 1 53 ? 13.842 20.784 8.774  1.00 6.73  ? 53   TYR A CD1 1 
ATOM   400 C  CD2 . TYR A 1 53 ? 15.986 21.028 7.740  1.00 7.41  ? 53   TYR A CD2 1 
ATOM   401 C  CE1 . TYR A 1 53 ? 13.280 20.395 7.571  1.00 7.12  ? 53   TYR A CE1 1 
ATOM   402 C  CE2 . TYR A 1 53 ? 15.456 20.573 6.553  1.00 6.70  ? 53   TYR A CE2 1 
ATOM   403 C  CZ  . TYR A 1 53 ? 14.115 20.257 6.473  1.00 6.96  ? 53   TYR A CZ  1 
ATOM   404 O  OH  . TYR A 1 53 ? 13.520 19.854 5.297  1.00 8.76  ? 53   TYR A OH  1 
ATOM   405 N  N   . ASP A 1 54 ? 18.340 19.755 10.172 1.00 5.67  ? 54   ASP A N   1 
ATOM   406 C  CA  . ASP A 1 54 ? 19.254 18.910 9.396  1.00 6.50  ? 54   ASP A CA  1 
ATOM   407 C  C   . ASP A 1 54 ? 19.380 17.525 9.996  1.00 6.04  ? 54   ASP A C   1 
ATOM   408 O  O   . ASP A 1 54 ? 19.514 16.527 9.287  1.00 6.88  ? 54   ASP A O   1 
ATOM   409 C  CB  . ASP A 1 54 ? 20.653 19.533 9.272  1.00 7.84  ? 54   ASP A CB  1 
ATOM   410 C  CG  . ASP A 1 54 ? 21.453 19.490 10.557 1.00 10.53 ? 54   ASP A CG  1 
ATOM   411 O  OD1 . ASP A 1 54 ? 21.119 20.254 11.482 1.00 11.45 ? 54   ASP A OD1 1 
ATOM   412 O  OD2 . ASP A 1 54 ? 22.329 18.604 10.710 1.00 15.59 ? 54   ASP A OD2 1 
ATOM   413 N  N   . PHE A 1 55 ? 19.407 17.450 11.328 1.00 5.56  ? 55   PHE A N   1 
ATOM   414 C  CA  . PHE A 1 55 ? 19.585 16.192 12.040 1.00 5.41  ? 55   PHE A CA  1 
ATOM   415 C  C   . PHE A 1 55 ? 18.355 15.301 11.868 1.00 4.89  ? 55   PHE A C   1 
ATOM   416 O  O   . PHE A 1 55 ? 18.479 14.112 11.583 1.00 5.30  ? 55   PHE A O   1 
ATOM   417 C  CB  . PHE A 1 55 ? 19.880 16.487 13.504 1.00 5.88  ? 55   PHE A CB  1 
ATOM   418 C  CG  . PHE A 1 55 ? 20.157 15.274 14.349 1.00 5.34  ? 55   PHE A CG  1 
ATOM   419 C  CD1 . PHE A 1 55 ? 21.251 14.443 14.111 1.00 5.94  ? 55   PHE A CD1 1 
ATOM   420 C  CD2 . PHE A 1 55 ? 19.324 15.001 15.420 1.00 6.18  ? 55   PHE A CD2 1 
ATOM   421 C  CE1 . PHE A 1 55 ? 21.475 13.342 14.917 1.00 7.20  ? 55   PHE A CE1 1 
ATOM   422 C  CE2 . PHE A 1 55 ? 19.561 13.902 16.217 1.00 8.27  ? 55   PHE A CE2 1 
ATOM   423 C  CZ  . PHE A 1 55 ? 20.645 13.063 15.983 1.00 7.60  ? 55   PHE A CZ  1 
ATOM   424 N  N   . ILE A 1 56 ? 17.152 15.870 12.054 1.00 5.16  ? 56   ILE A N   1 
ATOM   425 C  CA  . ILE A 1 56 ? 15.911 15.110 11.856 1.00 4.54  ? 56   ILE A CA  1 
ATOM   426 C  C   . ILE A 1 56 ? 15.817 14.592 10.424 1.00 4.81  ? 56   ILE A C   1 
ATOM   427 O  O   . ILE A 1 56 ? 15.511 13.432 10.185 1.00 4.97  ? 56   ILE A O   1 
ATOM   428 C  CB  . ILE A 1 56 ? 14.658 15.953 12.215 1.00 4.88  ? 56   ILE A CB  1 
ATOM   429 C  CG1 . ILE A 1 56 ? 14.675 16.404 13.684 1.00 4.50  ? 56   ILE A CG1 1 
ATOM   430 C  CG2 . ILE A 1 56 ? 13.370 15.205 11.865 1.00 5.46  ? 56   ILE A CG2 1 
ATOM   431 C  CD1 . ILE A 1 56 ? 14.707 15.264 14.677 1.00 5.53  ? 56   ILE A CD1 1 
ATOM   432 N  N   . LEU A 1 57 ? 16.081 15.461 9.450  1.00 4.96  ? 57   LEU A N   1 
ATOM   433 C  CA  . LEU A 1 57 ? 16.031 15.083 8.049  1.00 5.13  ? 57   LEU A CA  1 
ATOM   434 C  C   . LEU A 1 57 ? 16.996 13.930 7.777  1.00 5.55  ? 57   LEU A C   1 
ATOM   435 O  O   . LEU A 1 57 ? 16.591 12.949 7.150  1.00 5.68  ? 57   LEU A O   1 
ATOM   436 C  CB  . LEU A 1 57 ? 16.359 16.295 7.184  1.00 5.03  ? 57   LEU A CB  1 
ATOM   437 C  CG  . LEU A 1 57 ? 16.425 16.033 5.667  1.00 5.86  ? 57   LEU A CG  1 
ATOM   438 C  CD1 . LEU A 1 57 ? 15.145 15.418 5.132  1.00 7.29  ? 57   LEU A CD1 1 
ATOM   439 C  CD2 . LEU A 1 57 ? 16.770 17.332 4.963  1.00 9.17  ? 57   LEU A CD2 1 
ATOM   440 N  N   . GLU A 1 58 ? 18.245 14.053 8.255  1.00 5.45  ? 58   GLU A N   1 
ATOM   441 C  CA  . GLU A 1 58 ? 19.235 13.015 8.044  1.00 7.19  ? 58   GLU A CA  1 
ATOM   442 C  C   . GLU A 1 58 ? 18.787 11.682 8.607  1.00 6.21  ? 58   GLU A C   1 
ATOM   443 O  O   . GLU A 1 58 ? 18.945 10.610 7.990  1.00 7.48  ? 58   GLU A O   1 
ATOM   444 C  CB  . GLU A 1 58 ? 20.604 13.426 8.617  1.00 12.41 ? 58   GLU A CB  1 
ATOM   445 C  CG  . GLU A 1 58 ? 21.141 14.685 7.961  1.00 26.38 ? 58   GLU A CG  1 
ATOM   446 C  CD  . GLU A 1 58 ? 22.447 15.147 8.572  1.00 33.21 ? 58   GLU A CD  1 
ATOM   447 O  OE1 . GLU A 1 58 ? 22.517 15.276 9.811  1.00 36.06 ? 58   GLU A OE1 1 
ATOM   448 O  OE2 . GLU A 1 58 ? 23.330 15.398 7.729  1.00 36.75 ? 58   GLU A OE2 1 
ATOM   449 N  N   . LYS A 1 59 ? 18.296 11.698 9.847  1.00 6.15  ? 59   LYS A N   1 
ATOM   450 C  CA  . LYS A 1 59 ? 17.859 10.436 10.468 1.00 6.12  ? 59   LYS A CA  1 
ATOM   451 C  C   . LYS A 1 59 ? 16.685 9.802  9.739  1.00 6.18  ? 59   LYS A C   1 
ATOM   452 O  O   . LYS A 1 59 ? 16.656 8.559  9.595  1.00 6.76  ? 59   LYS A O   1 
ATOM   453 C  CB  . LYS A 1 59 ? 17.580 10.635 11.951 1.00 8.27  ? 59   LYS A CB  1 
ATOM   454 C  CG  . LYS A 1 59 ? 18.802 10.938 12.799 1.00 8.32  ? 59   LYS A CG  1 
ATOM   455 C  CD  . LYS A 1 59 ? 19.783 9.774  12.744 1.00 9.97  ? 59   LYS A CD  1 
ATOM   456 C  CE  . LYS A 1 59 ? 20.807 9.770  13.830 1.00 9.75  ? 59   LYS A CE  1 
ATOM   457 N  NZ  . LYS A 1 59 ? 21.884 8.753  13.662 1.00 9.84  ? 59   LYS A NZ  1 
ATOM   458 N  N   . ILE A 1 60 ? 15.740 10.604 9.251  1.00 5.74  ? 60   ILE A N   1 
ATOM   459 C  CA  . ILE A 1 60 ? 14.641 10.033 8.458  1.00 5.97  ? 60   ILE A CA  1 
ATOM   460 C  C   . ILE A 1 60 ? 15.167 9.486  7.141  1.00 6.43  ? 60   ILE A C   1 
ATOM   461 O  O   . ILE A 1 60 ? 14.827 8.378  6.694  1.00 6.84  ? 60   ILE A O   1 
ATOM   462 C  CB  . ILE A 1 60 ? 13.487 11.045 8.247  1.00 5.79  ? 60   ILE A CB  1 
ATOM   463 C  CG1 . ILE A 1 60 ? 12.863 11.449 9.585  1.00 6.41  ? 60   ILE A CG1 1 
ATOM   464 C  CG2 . ILE A 1 60 ? 12.414 10.483 7.306  1.00 8.64  ? 60   ILE A CG2 1 
ATOM   465 C  CD1 . ILE A 1 60 ? 11.805 12.515 9.470  1.00 7.91  ? 60   ILE A CD1 1 
ATOM   466 N  N   . LYS A 1 61 ? 16.051 10.219 6.469  1.00 6.27  ? 61   LYS A N   1 
ATOM   467 C  CA  . LYS A 1 61 ? 16.570 9.753  5.192  1.00 6.41  ? 61   LYS A CA  1 
ATOM   468 C  C   . LYS A 1 61 ? 17.299 8.426  5.322  1.00 6.41  ? 61   LYS A C   1 
ATOM   469 O  O   . LYS A 1 61 ? 17.294 7.607  4.419  1.00 7.79  ? 61   LYS A O   1 
ATOM   470 C  CB  . LYS A 1 61 ? 17.497 10.790 4.560  1.00 6.90  ? 61   LYS A CB  1 
ATOM   471 C  CG  . LYS A 1 61 ? 16.768 11.992 3.994  1.00 8.30  ? 61   LYS A CG  1 
ATOM   472 C  CD  . LYS A 1 61 ? 17.678 13.046 3.417  1.00 10.18 ? 61   LYS A CD  1 
ATOM   473 C  CE  . LYS A 1 61 ? 18.353 12.594 2.138  1.00 12.92 ? 61   LYS A CE  1 
ATOM   474 N  NZ  . LYS A 1 61 ? 17.448 12.693 0.961  1.00 15.09 ? 61   LYS A NZ  1 
ATOM   475 N  N   . LYS A 1 62 ? 17.978 8.196  6.447  1.00 7.22  ? 62   LYS A N   1 
ATOM   476 C  CA  . LYS A 1 62 ? 18.716 6.954  6.621  1.00 8.73  ? 62   LYS A CA  1 
ATOM   477 C  C   . LYS A 1 62 ? 17.866 5.731  6.872  1.00 8.90  ? 62   LYS A C   1 
ATOM   478 O  O   . LYS A 1 62 ? 18.416 4.612  6.787  1.00 11.18 ? 62   LYS A O   1 
ATOM   479 C  CB  . LYS A 1 62 ? 19.769 7.133  7.733  1.00 9.72  ? 62   LYS A CB  1 
ATOM   480 C  CG  . LYS A 1 62 ? 20.948 8.012  7.349  1.00 13.56 ? 62   LYS A CG  1 
ATOM   481 C  CD  . LYS A 1 62 ? 21.713 7.620  6.104  1.00 23.28 ? 62   LYS A CD  1 
ATOM   482 C  CE  . LYS A 1 62 ? 21.818 8.748  5.091  1.00 32.45 ? 62   LYS A CE  1 
ATOM   483 N  NZ  . LYS A 1 62 ? 20.804 8.719  4.004  1.00 40.97 ? 62   LYS A NZ  1 
ATOM   484 N  N   . THR A 1 63 ? 16.549 5.899  6.959  1.00 7.96  ? 63   THR A N   1 
ATOM   485 C  CA  . THR A 1 63 ? 15.654 4.756  6.914  1.00 7.84  ? 63   THR A CA  1 
ATOM   486 C  C   . THR A 1 63 ? 15.606 4.122  5.527  1.00 7.79  ? 63   THR A C   1 
ATOM   487 O  O   . THR A 1 63 ? 15.107 3.015  5.386  1.00 9.22  ? 63   THR A O   1 
ATOM   488 C  CB  . THR A 1 63 ? 14.188 5.085  7.273  1.00 8.00  ? 63   THR A CB  1 
ATOM   489 O  OG1 . THR A 1 63 ? 13.626 6.064  6.402  1.00 7.78  ? 63   THR A OG1 1 
ATOM   490 C  CG2 . THR A 1 63 ? 14.129 5.707  8.661  1.00 9.99  ? 63   THR A CG2 1 
ATOM   491 N  N   . GLY A 1 64 ? 15.989 4.881  4.509  1.00 7.62  ? 64   GLY A N   1 
ATOM   492 C  CA  . GLY A 1 64 ? 15.825 4.452  3.119  1.00 6.80  ? 64   GLY A CA  1 
ATOM   493 C  C   . GLY A 1 64 ? 14.500 4.734  2.483  1.00 6.55  ? 64   GLY A C   1 
ATOM   494 O  O   . GLY A 1 64 ? 14.266 4.453  1.303  1.00 8.09  ? 64   GLY A O   1 
ATOM   495 N  N   . LYS A 1 65 ? 13.439 5.119  3.105  1.00 7.47  ? 65   LYS A N   1 
ATOM   496 C  CA  . LYS A 1 65 ? 12.188 5.682  2.694  1.00 7.25  ? 65   LYS A CA  1 
ATOM   497 C  C   . LYS A 1 65 ? 12.433 7.056  2.070  1.00 7.62  ? 65   LYS A C   1 
ATOM   498 O  O   . LYS A 1 65 ? 13.065 7.912  2.699  1.00 10.59 ? 65   LYS A O   1 
ATOM   499 C  CB  . LYS A 1 65 ? 11.157 5.781  3.819  1.00 9.73  ? 65   LYS A CB  1 
ATOM   500 C  CG  . LYS A 1 65 ? 10.977 4.532  4.639  1.00 10.05 ? 65   LYS A CG  1 
ATOM   501 C  CD  . LYS A 1 65 ? 10.873 3.267  3.839  1.00 13.31 ? 65   LYS A CD  1 
ATOM   502 C  CE  . LYS A 1 65 ? 10.898 2.062  4.788  1.00 12.85 ? 65   LYS A CE  1 
ATOM   503 N  NZ  . LYS A 1 65 ? 11.010 0.835  3.951  1.00 18.00 ? 65   LYS A NZ  1 
ATOM   504 N  N   . GLU A 1 66 ? 12.000 7.228  0.841  1.00 6.90  ? 66   GLU A N   1 
ATOM   505 C  CA  . GLU A 1 66 ? 12.303 8.450  0.122  1.00 7.25  ? 66   GLU A CA  1 
ATOM   506 C  C   . GLU A 1 66 ? 11.670 9.689  0.733  1.00 5.33  ? 66   GLU A C   1 
ATOM   507 O  O   . GLU A 1 66 ? 10.453 9.744  0.938  1.00 6.35  ? 66   GLU A O   1 
ATOM   508 C  CB  . GLU A 1 66 ? 11.812 8.309  -1.318 1.00 7.10  ? 66   GLU A CB  1 
ATOM   509 C  CG  . GLU A 1 66 ? 12.036 9.527  -2.196 1.00 10.23 ? 66   GLU A CG  1 
ATOM   510 C  CD  . GLU A 1 66 ? 11.455 9.372  -3.591 1.00 13.96 ? 66   GLU A CD  1 
ATOM   511 O  OE1 . GLU A 1 66 ? 10.956 8.283  -3.963 1.00 19.00 ? 66   GLU A OE1 1 
ATOM   512 O  OE2 . GLU A 1 66 ? 11.587 10.332 -4.388 1.00 19.77 ? 66   GLU A OE2 1 
ATOM   513 N  N   . VAL A 1 67 ? 12.508 10.679 1.027  1.00 6.19  ? 67   VAL A N   1 
ATOM   514 C  CA  . VAL A 1 67 ? 12.017 11.976 1.496  1.00 5.61  ? 67   VAL A CA  1 
ATOM   515 C  C   . VAL A 1 67 ? 12.004 12.918 0.304  1.00 6.04  ? 67   VAL A C   1 
ATOM   516 O  O   . VAL A 1 67 ? 13.066 13.265 -0.227 1.00 9.09  ? 67   VAL A O   1 
ATOM   517 C  CB  . VAL A 1 67 ? 12.855 12.560 2.644  1.00 6.48  ? 67   VAL A CB  1 
ATOM   518 C  CG1 . VAL A 1 67 ? 12.264 13.902 3.087  1.00 7.86  ? 67   VAL A CG1 1 
ATOM   519 C  CG2 . VAL A 1 67 ? 12.940 11.611 3.826  1.00 8.39  ? 67   VAL A CG2 1 
ATOM   520 N  N   . ARG A 1 68 ? 10.807 13.276 -0.158 1.00 6.01  ? 68   ARG A N   1 
ATOM   521 C  CA  . ARG A 1 68 ? 10.607 14.095 -1.347 1.00 6.99  ? 68   ARG A CA  1 
ATOM   522 C  C   . ARG A 1 68 ? 10.887 15.559 -1.085 1.00 7.57  ? 68   ARG A C   1 
ATOM   523 O  O   . ARG A 1 68 ? 11.401 16.268 -1.957 1.00 11.29 ? 68   ARG A O   1 
ATOM   524 C  CB  . ARG A 1 68 ? 9.184  13.962 -1.904 1.00 10.48 ? 68   ARG A CB  1 
ATOM   525 C  CG  . ARG A 1 68 ? 8.775  12.602 -2.408 1.00 13.71 ? 68   ARG A CG  1 
ATOM   526 C  CD  . ARG A 1 68 ? 9.259  12.294 -3.790 1.00 18.98 ? 68   ARG A CD  1 
ATOM   527 N  NE  . ARG A 1 68 ? 8.807  13.230 -4.786 1.00 18.68 ? 68   ARG A NE  1 
ATOM   528 C  CZ  . ARG A 1 68 ? 7.769  13.266 -5.593 1.00 20.12 ? 68   ARG A CZ  1 
ATOM   529 N  NH1 . ARG A 1 68 ? 6.837  12.332 -5.636 1.00 16.67 ? 68   ARG A NH1 1 
ATOM   530 N  NH2 . ARG A 1 68 ? 7.625  14.319 -6.393 1.00 24.80 ? 68   ARG A NH2 1 
ATOM   531 N  N   . SER A 1 69 ? 10.578 16.023 0.113  1.00 5.96  ? 69   SER A N   1 
ATOM   532 C  CA  . SER A 1 69 ? 10.732 17.421 0.476  1.00 7.46  ? 69   SER A CA  1 
ATOM   533 C  C   . SER A 1 69 ? 10.556 17.568 1.981  1.00 5.68  ? 69   SER A C   1 
ATOM   534 O  O   . SER A 1 69 ? 9.965  16.699 2.649  1.00 5.80  ? 69   SER A O   1 
ATOM   535 C  CB  . SER A 1 69 ? 9.705  18.273 -0.245 1.00 11.06 ? 69   SER A CB  1 
ATOM   536 O  OG  . SER A 1 69 ? 8.399  18.028 0.253  1.00 13.17 ? 69   SER A OG  1 
ATOM   537 N  N   . GLY A 1 70 ? 10.975 18.696 2.522  1.00 6.33  ? 70   GLY A N   1 
ATOM   538 C  CA  . GLY A 1 70 ? 10.692 19.073 3.891  1.00 6.86  ? 70   GLY A CA  1 
ATOM   539 C  C   . GLY A 1 70 ? 10.662 20.576 4.022  1.00 6.31  ? 70   GLY A C   1 
ATOM   540 O  O   . GLY A 1 70 ? 11.256 21.320 3.223  1.00 7.28  ? 70   GLY A O   1 
ATOM   541 N  N   . LYS A 1 71 ? 10.068 21.016 5.118  1.00 5.82  ? 71   LYS A N   1 
ATOM   542 C  CA  . LYS A 1 71 ? 10.043 22.435 5.445  1.00 7.15  ? 71   LYS A CA  1 
ATOM   543 C  C   . LYS A 1 71 ? 9.763  22.618 6.936  1.00 5.37  ? 71   LYS A C   1 
ATOM   544 O  O   . LYS A 1 71 ? 9.405  21.714 7.658  1.00 5.83  ? 71   LYS A O   1 
ATOM   545 C  CB  . LYS A 1 71 ? 9.031  23.196 4.599  1.00 10.00 ? 71   LYS A CB  1 
ATOM   546 C  CG  . LYS A 1 71 ? 7.572  22.914 4.887  1.00 13.44 ? 71   LYS A CG  1 
ATOM   547 C  CD  . LYS A 1 71 ? 6.659  23.491 3.826  1.00 26.85 ? 71   LYS A CD  1 
ATOM   548 C  CE  . LYS A 1 71 ? 7.327  24.195 2.670  1.00 38.68 ? 71   LYS A CE  1 
ATOM   549 N  NZ  . LYS A 1 71 ? 7.726  23.290 1.551  1.00 46.87 ? 71   LYS A NZ  1 
ATOM   550 N  N   . GLN A 1 72 ? 9.965  23.850 7.375  1.00 6.89  ? 72   GLN A N   1 
ATOM   551 C  CA  . GLN A 1 72 ? 9.665  24.303 8.718  1.00 6.42  ? 72   GLN A CA  1 
ATOM   552 C  C   . GLN A 1 72 ? 8.374  25.123 8.751  1.00 6.85  ? 72   GLN A C   1 
ATOM   553 O  O   . GLN A 1 72 ? 8.162  25.976 7.885  1.00 10.11 ? 72   GLN A O   1 
ATOM   554 C  CB  . GLN A 1 72 ? 10.861 25.024 9.327  1.00 8.10  ? 72   GLN A CB  1 
ATOM   555 C  CG  . GLN A 1 72 ? 10.682 25.231 10.815 1.00 12.23 ? 72   GLN A CG  1 
ATOM   556 C  CD  . GLN A 1 72 ? 11.924 25.684 11.543 1.00 13.99 ? 72   GLN A CD  1 
ATOM   557 O  OE1 . GLN A 1 72 ? 13.051 25.847 11.046 1.00 19.15 ? 72   GLN A OE1 1 
ATOM   558 N  NE2 . GLN A 1 72 ? 11.617 25.941 12.795 1.00 15.03 ? 72   GLN A NE2 1 
ATOM   559 N  N   . LEU A 1 73 ? 7.512  24.889 9.738  1.00 6.95  ? 73   LEU A N   1 
ATOM   560 C  CA  . LEU A 1 73 ? 6.232  25.568 9.883  1.00 7.34  ? 73   LEU A CA  1 
ATOM   561 C  C   . LEU A 1 73 ? 6.094  26.305 11.192 1.00 8.25  ? 73   LEU A C   1 
ATOM   562 O  O   . LEU A 1 73 ? 7.013  26.268 12.048 1.00 11.22 ? 73   LEU A O   1 
ATOM   563 C  CB  . LEU A 1 73 ? 5.112  24.529 9.739  1.00 7.88  ? 73   LEU A CB  1 
ATOM   564 C  CG  . LEU A 1 73 ? 4.927  23.861 8.378  1.00 10.53 ? 73   LEU A CG  1 
ATOM   565 C  CD1 . LEU A 1 73 ? 6.062  22.894 8.049  1.00 35.37 ? 73   LEU A CD1 1 
ATOM   566 C  CD2 . LEU A 1 73 ? 3.675  22.956 8.370  1.00 16.09 ? 73   LEU A CD2 1 
ATOM   567 O  OXT . LEU A 1 73 ? 5.031  26.950 11.382 1.00 9.79  ? 73   LEU A OXT 1 
HETATM 568 HG HG  . HG  B 2 .  ? 5.897  0.005  3.783  1.00 10.60 ? 74   HG  A HG  1 
HETATM 569 C  C1  . BEN C 3 .  ? 6.778  10.510 20.665 1.00 4.96  ? 186  BEN A C1  1 
HETATM 570 C  C2  . BEN C 3 .  ? 5.994  9.710  19.842 1.00 5.48  ? 186  BEN A C2  1 
HETATM 571 C  C3  . BEN C 3 .  ? 6.562  9.055  18.751 1.00 5.92  ? 186  BEN A C3  1 
HETATM 572 C  C4  . BEN C 3 .  ? 7.916  9.259  18.444 1.00 6.52  ? 186  BEN A C4  1 
HETATM 573 C  C5  . BEN C 3 .  ? 8.711  10.120 19.210 1.00 5.95  ? 186  BEN A C5  1 
HETATM 574 C  C6  . BEN C 3 .  ? 8.128  10.734 20.335 1.00 5.84  ? 186  BEN A C6  1 
HETATM 575 C  C   . BEN C 3 .  ? 6.244  11.152 21.851 1.00 5.51  ? 186  BEN A C   1 
HETATM 576 N  N1  . BEN C 3 .  ? 7.014  11.257 22.910 1.00 6.98  ? 186  BEN A N1  1 
HETATM 577 N  N2  . BEN C 3 .  ? 4.965  11.590 21.821 1.00 6.99  ? 186  BEN A N2  1 
HETATM 578 C  C1  . BEN D 3 .  ? -2.553 3.433  3.188  1.00 13.65 ? 187  BEN A C1  1 
HETATM 579 C  C2  . BEN D 3 .  ? -1.337 3.205  2.508  1.00 14.92 ? 187  BEN A C2  1 
HETATM 580 C  C3  . BEN D 3 .  ? -0.791 4.128  1.629  1.00 13.52 ? 187  BEN A C3  1 
HETATM 581 C  C4  . BEN D 3 .  ? -1.550 5.259  1.337  1.00 12.54 ? 187  BEN A C4  1 
HETATM 582 C  C5  . BEN D 3 .  ? -2.797 5.495  1.902  1.00 9.96  ? 187  BEN A C5  1 
HETATM 583 C  C6  . BEN D 3 .  ? -3.296 4.579  2.847  1.00 13.84 ? 187  BEN A C6  1 
HETATM 584 C  C   . BEN D 3 .  ? -3.074 2.290  3.932  1.00 22.17 ? 187  BEN A C   1 
HETATM 585 N  N1  . BEN D 3 .  ? -3.970 2.454  4.841  1.00 23.93 ? 187  BEN A N1  1 
HETATM 586 N  N2  . BEN D 3 .  ? -2.208 1.221  3.932  1.00 29.56 ? 187  BEN A N2  1 
HETATM 587 O  O   . HOH E 4 .  ? 17.616 8.247  15.310 1.00 7.94  ? 1001 HOH A O   1 
HETATM 588 O  O   . HOH E 4 .  ? 7.788  26.848 17.598 1.00 5.64  ? 1002 HOH A O   1 
HETATM 589 O  O   . HOH E 4 .  ? 19.740 7.804  17.090 1.00 8.59  ? 1003 HOH A O   1 
HETATM 590 O  O   . HOH E 4 .  ? 15.306 24.210 20.260 1.00 11.37 ? 1004 HOH A O   1 
HETATM 591 O  O   . HOH E 4 .  ? 9.088  25.617 13.651 1.00 9.23  ? 1005 HOH A O   1 
HETATM 592 O  O   . HOH E 4 .  ? 18.284 6.706  10.932 1.00 9.47  ? 1006 HOH A O   1 
HETATM 593 O  O   . HOH E 4 .  ? 15.474 10.474 0.756  1.00 9.84  ? 1007 HOH A O   1 
HETATM 594 O  O   . HOH E 4 .  ? -4.607 12.567 8.831  1.00 8.57  ? 1008 HOH A O   1 
HETATM 595 O  O   . HOH E 4 .  ? 0.991  14.171 9.092  1.00 9.40  ? 1009 HOH A O   1 
HETATM 596 O  O   . HOH E 4 .  ? 8.186  2.217  14.943 1.00 8.96  ? 1010 HOH A O   1 
HETATM 597 O  O   . HOH E 4 .  ? 15.781 8.125  2.080  1.00 11.19 ? 1011 HOH A O   1 
HETATM 598 O  O   . HOH E 4 .  ? 9.043  27.744 2.341  1.00 8.14  ? 1012 HOH A O   1 
HETATM 599 O  O   . HOH E 4 .  ? 18.168 6.153  13.551 1.00 12.87 ? 1013 HOH A O   1 
HETATM 600 O  O   . HOH E 4 .  ? 14.958 20.095 3.073  1.00 12.55 ? 1014 HOH A O   1 
HETATM 601 O  O   . HOH E 4 .  ? 15.221 5.279  -0.979 1.00 13.31 ? 1015 HOH A O   1 
HETATM 602 O  O   . HOH E 4 .  ? 10.901 4.955  -0.726 1.00 12.77 ? 1016 HOH A O   1 
HETATM 603 O  O   . HOH E 4 .  ? -0.368 -1.085 5.462  1.00 14.79 ? 1017 HOH A O   1 
HETATM 604 O  O   . HOH E 4 .  ? 7.866  27.802 5.388  1.00 17.16 ? 1018 HOH A O   1 
HETATM 605 O  O   . HOH E 4 .  ? 10.513 5.777  -3.346 1.00 14.90 ? 1019 HOH A O   1 
HETATM 606 O  O   . HOH E 4 .  ? 19.321 22.451 10.785 1.00 14.94 ? 1020 HOH A O   1 
HETATM 607 O  O   . HOH E 4 .  ? 13.882 2.702  11.385 1.00 14.52 ? 1021 HOH A O   1 
HETATM 608 O  O   . HOH E 4 .  ? -0.005 18.132 14.411 1.00 15.92 ? 1022 HOH A O   1 
HETATM 609 O  O   . HOH E 4 .  ? 8.700  3.800  0.678  1.00 15.06 ? 1023 HOH A O   1 
HETATM 610 O  O   . HOH E 4 .  ? 11.137 25.942 5.586  1.00 15.64 ? 1024 HOH A O   1 
HETATM 611 O  O   . HOH E 4 .  ? 23.043 21.198 13.218 1.00 12.49 ? 1025 HOH A O   1 
HETATM 612 O  O   . HOH E 4 .  ? 10.351 12.943 23.642 1.00 14.56 ? 1026 HOH A O   1 
HETATM 613 O  O   . HOH E 4 .  ? 17.408 23.420 22.024 1.00 22.66 ? 1027 HOH A O   1 
HETATM 614 O  O   . HOH E 4 .  ? 10.645 18.582 21.891 1.00 16.24 ? 1028 HOH A O   1 
HETATM 615 O  O   . HOH E 4 .  ? 6.814  17.051 -1.761 1.00 16.27 ? 1029 HOH A O   1 
HETATM 616 O  O   . HOH E 4 .  ? 24.879 21.422 11.090 1.00 19.36 ? 1030 HOH A O   1 
HETATM 617 O  O   . HOH E 4 .  ? 2.062  -2.830 10.994 1.00 13.70 ? 1031 HOH A O   1 
HETATM 618 O  O   . HOH E 4 .  ? 17.840 4.071  9.868  1.00 23.49 ? 1032 HOH A O   1 
HETATM 619 O  O   . HOH E 4 .  ? 12.679 6.080  23.452 1.00 18.88 ? 1033 HOH A O   1 
HETATM 620 O  O   . HOH E 4 .  ? 13.989 1.203  3.508  1.00 16.88 ? 1034 HOH A O   1 
HETATM 621 O  O   . HOH E 4 .  ? 4.973  29.360 12.493 1.00 13.56 ? 1035 HOH A O   1 
HETATM 622 O  O   . HOH E 4 .  ? 17.267 23.789 12.875 1.00 16.28 ? 1036 HOH A O   1 
HETATM 623 O  O   . HOH E 4 .  ? -2.194 15.327 15.082 1.00 19.05 ? 1037 HOH A O   1 
HETATM 624 O  O   . HOH E 4 .  ? 17.725 22.862 17.146 1.00 17.23 ? 1038 HOH A O   1 
HETATM 625 O  O   . HOH E 4 .  ? -1.066 0.180  1.359  1.00 19.12 ? 1039 HOH A O   1 
HETATM 626 O  O   . HOH E 4 .  ? 13.599 22.701 3.492  1.00 24.22 ? 1040 HOH A O   1 
HETATM 627 O  O   . HOH E 4 .  ? 14.167 1.345  7.218  1.00 20.56 ? 1041 HOH A O   1 
HETATM 628 O  O   . HOH E 4 .  ? 15.108 7.248  23.019 1.00 20.34 ? 1042 HOH A O   1 
HETATM 629 O  O   . HOH E 4 .  ? 9.833  29.184 14.302 1.00 20.92 ? 1043 HOH A O   1 
HETATM 630 O  O   . HOH E 4 .  ? 12.756 16.878 27.310 1.00 16.27 ? 1044 HOH A O   1 
HETATM 631 O  O   . HOH E 4 .  ? 0.358  3.935  9.734  1.00 26.51 ? 1045 HOH A O   1 
HETATM 632 O  O   . HOH E 4 .  ? 15.402 27.809 21.589 1.00 20.37 ? 1046 HOH A O   1 
HETATM 633 O  O   . HOH E 4 .  ? 22.105 5.095  14.239 1.00 33.84 ? 1047 HOH A O   1 
HETATM 634 O  O   . HOH E 4 .  ? 3.366  1.920  11.836 1.00 15.34 ? 1048 HOH A O   1 
HETATM 635 O  O   . HOH E 4 .  ? 13.969 26.024 8.265  1.00 19.99 ? 1049 HOH A O   1 
HETATM 636 O  O   . HOH E 4 .  ? 7.367  19.311 3.002  1.00 24.37 ? 1050 HOH A O   1 
HETATM 637 O  O   . HOH E 4 .  ? 13.629 1.422  -1.238 1.00 38.99 ? 1051 HOH A O   1 
HETATM 638 O  O   . HOH E 4 .  ? 9.816  -1.158 9.253  1.00 34.42 ? 1052 HOH A O   1 
HETATM 639 O  O   . HOH E 4 .  ? 8.217  1.109  0.522  1.00 17.09 ? 1053 HOH A O   1 
HETATM 640 O  O   . HOH E 4 .  ? -1.422 15.069 7.675  1.00 27.26 ? 1054 HOH A O   1 
HETATM 641 O  O   . HOH E 4 .  ? 15.533 25.642 12.903 1.00 28.86 ? 1055 HOH A O   1 
HETATM 642 O  O   . HOH E 4 .  ? -2.456 7.357  8.315  1.00 32.29 ? 1056 HOH A O   1 
HETATM 643 O  O   . HOH E 4 .  ? -3.865 4.934  7.261  1.00 25.36 ? 1057 HOH A O   1 
HETATM 644 O  O   . HOH E 4 .  ? 10.154 15.808 -5.074 1.00 32.28 ? 1058 HOH A O   1 
HETATM 645 O  O   . HOH E 4 .  ? 14.392 24.062 6.799  1.00 31.43 ? 1059 HOH A O   1 
HETATM 646 O  O   . HOH E 4 .  ? 8.212  2.856  -2.729 1.00 37.74 ? 1060 HOH A O   1 
HETATM 647 O  O   . HOH E 4 .  ? 8.669  28.931 12.142 1.00 19.02 ? 1061 HOH A O   1 
HETATM 648 O  O   . HOH E 4 .  ? 16.476 26.837 19.562 1.00 26.77 ? 1062 HOH A O   1 
HETATM 649 O  O   . HOH E 4 .  ? 14.493 30.605 19.958 1.00 31.26 ? 1063 HOH A O   1 
HETATM 650 O  O   . HOH E 4 .  ? 4.811  19.687 2.798  1.00 19.34 ? 1064 HOH A O   1 
HETATM 651 O  O   . HOH E 4 .  ? 26.289 12.649 6.622  1.00 27.59 ? 1065 HOH A O   1 
HETATM 652 O  O   . HOH E 4 .  ? 21.051 6.421  10.619 1.00 20.88 ? 1066 HOH A O   1 
HETATM 653 O  O   . HOH E 4 .  ? 16.739 2.308  11.902 1.00 27.03 ? 1067 HOH A O   1 
HETATM 654 O  O   . HOH E 4 .  ? 11.027 28.995 11.387 1.00 34.49 ? 1068 HOH A O   1 
HETATM 655 O  O   . HOH E 4 .  ? 0.659  -5.373 10.338 1.00 20.19 ? 1069 HOH A O   1 
HETATM 656 O  O   . HOH E 4 .  ? 13.126 12.568 -4.040 1.00 30.85 ? 1070 HOH A O   1 
HETATM 657 O  O   . HOH E 4 .  ? 4.262  -2.108 0.738  1.00 28.30 ? 1071 HOH A O   1 
HETATM 658 O  O   . HOH E 4 .  ? 17.019 7.517  -0.249 1.00 22.35 ? 1072 HOH A O   1 
HETATM 659 O  O   . HOH E 4 .  ? 0.989  1.466  12.601 1.00 23.75 ? 1073 HOH A O   1 
HETATM 660 O  O   . HOH E 4 .  ? 22.437 8.753  10.589 1.00 35.20 ? 1074 HOH A O   1 
HETATM 661 O  O   . HOH E 4 .  ? 8.127  17.699 -4.165 1.00 25.84 ? 1075 HOH A O   1 
HETATM 662 O  O   . HOH E 4 .  ? 0.252  22.153 7.142  1.00 29.72 ? 1076 HOH A O   1 
HETATM 663 O  O   . HOH E 4 .  ? 20.247 5.579  16.818 1.00 39.86 ? 1077 HOH A O   1 
HETATM 664 O  O   . HOH E 4 .  ? 28.047 20.920 10.605 1.00 49.11 ? 1078 HOH A O   1 
HETATM 665 O  O   . HOH E 4 .  ? 17.087 28.399 23.725 1.00 29.54 ? 1079 HOH A O   1 
HETATM 666 O  O   . HOH E 4 .  ? -1.538 3.888  12.049 1.00 42.97 ? 1080 HOH A O   1 
HETATM 667 O  O   . HOH E 4 .  ? 22.919 10.104 8.434  1.00 30.92 ? 1081 HOH A O   1 
HETATM 668 O  O   . HOH E 4 .  ? 2.561  22.712 4.893  1.00 35.03 ? 1082 HOH A O   1 
HETATM 669 O  O   . HOH E 4 .  ? -0.344 17.832 9.512  1.00 34.60 ? 1083 HOH A O   1 
HETATM 670 O  O   . HOH E 4 .  ? 8.152  17.267 -8.285 1.00 29.67 ? 1084 HOH A O   1 
HETATM 671 O  O   . HOH E 4 .  ? -4.543 16.188 7.860  1.00 38.10 ? 1085 HOH A O   1 
HETATM 672 O  O   . HOH E 4 .  ? 18.721 9.864  1.672  1.00 31.64 ? 1086 HOH A O   1 
HETATM 673 O  O   . HOH E 4 .  ? 7.824  1.096  -4.715 1.00 44.70 ? 1087 HOH A O   1 
HETATM 674 O  O   . HOH E 4 .  ? 2.661  24.863 3.932  1.00 30.82 ? 1088 HOH A O   1 
HETATM 675 O  O   . HOH E 4 .  ? 0.175  -7.724 10.899 1.00 28.44 ? 1089 HOH A O   1 
HETATM 676 O  O   . HOH E 4 .  ? 24.737 11.092 4.411  1.00 34.84 ? 1090 HOH A O   1 
HETATM 677 O  O   . HOH E 4 .  ? 16.708 30.878 21.040 1.00 39.21 ? 1091 HOH A O   1 
HETATM 678 O  O   . HOH E 4 .  ? 13.119 3.560  -0.566 1.00 34.87 ? 1092 HOH A O   1 
HETATM 679 O  O   . HOH E 4 .  ? -5.018 19.100 2.687  1.00 64.30 ? 1093 HOH A O   1 
HETATM 680 O  O   . HOH E 4 .  ? 16.851 27.903 15.081 1.00 20.67 ? 1094 HOH A O   1 
HETATM 681 O  O   . HOH E 4 .  ? 15.528 2.201  9.313  1.00 29.43 ? 1095 HOH A O   1 
HETATM 682 O  O   . HOH E 4 .  ? 5.414  22.388 -0.132 1.00 47.90 ? 1096 HOH A O   1 
HETATM 683 O  O   . HOH E 4 .  ? -3.613 9.137  9.430  1.00 26.58 ? 1097 HOH A O   1 
HETATM 684 O  O   . HOH E 4 .  ? -1.637 -5.500 10.285 1.00 31.85 ? 1098 HOH A O   1 
HETATM 685 O  O   . HOH E 4 .  ? 14.574 7.143  25.450 1.00 46.35 ? 1099 HOH A O   1 
HETATM 686 O  O   . HOH E 4 .  ? 26.128 14.886 6.158  1.00 49.82 ? 1100 HOH A O   1 
HETATM 687 O  O   . HOH E 4 .  ? 28.667 11.791 6.490  1.00 40.09 ? 1101 HOH A O   1 
HETATM 688 O  O   . HOH E 4 .  ? 19.855 23.936 16.260 1.00 37.69 ? 1102 HOH A O   1 
HETATM 689 O  O   . HOH E 4 .  ? -0.301 -2.484 1.174  0.50 33.56 ? 1103 HOH A O   1 
HETATM 690 O  O   . HOH E 4 .  ? -3.492 14.956 11.321 1.00 28.59 ? 1104 HOH A O   1 
HETATM 691 O  O   . HOH E 4 .  ? 14.744 26.844 17.123 1.00 51.02 ? 1105 HOH A O   1 
HETATM 692 O  O   . HOH E 4 .  ? 14.544 12.895 -2.262 1.00 32.47 ? 1106 HOH A O   1 
HETATM 693 O  O   . HOH E 4 .  ? 10.065 9.307  -6.233 1.00 35.80 ? 1107 HOH A O   1 
HETATM 694 O  O   . HOH E 4 .  ? 23.449 5.213  9.064  1.00 38.80 ? 1108 HOH A O   1 
HETATM 695 O  O   . HOH E 4 .  ? 24.477 13.613 4.617  1.00 35.58 ? 1109 HOH A O   1 
HETATM 696 O  O   . HOH E 4 .  ? 19.307 2.563  12.439 1.00 30.95 ? 1110 HOH A O   1 
HETATM 697 O  O   . HOH E 4 .  ? 11.668 2.082  0.348  1.00 53.60 ? 1111 HOH A O   1 
HETATM 698 O  O   . HOH E 4 .  ? 2.128  15.527 0.790  1.00 40.18 ? 1112 HOH A O   1 
HETATM 699 O  O   . HOH E 4 .  ? 11.617 28.291 6.349  0.50 24.45 ? 1113 HOH A O   1 
HETATM 700 O  O   . HOH E 4 .  ? 17.590 28.365 21.334 1.00 34.65 ? 1114 HOH A O   1 
HETATM 701 O  O   . HOH E 4 .  ? 24.804 19.497 9.633  1.00 49.69 ? 1115 HOH A O   1 
HETATM 702 O  O   . HOH E 4 .  ? 9.141  4.823  -4.924 0.50 34.59 ? 1116 HOH A O   1 
HETATM 703 O  O   . HOH E 4 .  ? 7.126  17.929 -6.363 1.00 45.52 ? 1117 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1   N  N   . ALA A 2  ? 0.3076 0.5049 0.2840 -0.2878 -0.0759 0.0351  2    ALA A N   
2   C  CA  . ALA A 2  ? 0.0553 0.1356 0.0784 0.0614  -0.0124 -0.0316 2    ALA A CA  
3   C  C   . ALA A 2  ? 0.0588 0.0916 0.0538 0.0215  -0.0043 -0.0189 2    ALA A C   
4   O  O   . ALA A 2  ? 0.0640 0.0967 0.0469 0.0129  -0.0016 -0.0098 2    ALA A O   
5   C  CB  . ALA A 2  ? 0.0769 0.2252 0.0598 0.0578  -0.0420 -0.0408 2    ALA A CB  
6   N  N   . GLU A 3  ? 0.0592 0.0679 0.0706 0.0000  -0.0063 -0.0089 3    GLU A N   
7   C  CA  . GLU A 3  ? 0.0631 0.0581 0.0571 0.0079  -0.0001 -0.0080 3    GLU A CA  
8   C  C   . GLU A 3  ? 0.0616 0.0679 0.0469 0.0045  -0.0073 -0.0040 3    GLU A C   
9   O  O   . GLU A 3  ? 0.0689 0.0464 0.0922 0.0117  -0.0094 -0.0054 3    GLU A O   
10  C  CB  . GLU A 3  ? 0.0822 0.0683 0.0639 0.0069  0.0126  -0.0037 3    GLU A CB  
11  C  CG  . GLU A 3  ? 0.1079 0.0486 0.0692 0.0074  -0.0002 0.0020  3    GLU A CG  
12  C  CD  . GLU A 3  ? 0.0995 0.1044 0.0798 -0.0062 -0.0037 0.0131  3    GLU A CD  
13  O  OE1 . GLU A 3  ? 0.1241 0.1040 0.1185 -0.0539 0.0148  0.0041  3    GLU A OE1 
14  O  OE2 . GLU A 3  ? 0.1066 0.1386 0.1038 -0.0077 -0.0128 0.0353  3    GLU A OE2 
15  N  N   . ILE A 4  ? 0.0564 0.0662 0.0505 0.0032  -0.0015 -0.0074 4    ILE A N   
16  C  CA  . ILE A 4  ? 0.0475 0.0691 0.0510 0.0069  -0.0006 -0.0126 4    ILE A CA  
17  C  C   . ILE A 4  ? 0.0475 0.0444 0.0537 0.0003  0.0022  0.0000  4    ILE A C   
18  O  O   . ILE A 4  ? 0.0656 0.0601 0.0560 0.0171  -0.0029 0.0002  4    ILE A O   
19  C  CB  . ILE A 4  ? 0.0718 0.0455 0.0528 0.0003  0.0074  -0.0041 4    ILE A CB  
20  C  CG1 . ILE A 4  ? 0.1068 0.0843 0.0517 -0.0112 0.0008  -0.0035 4    ILE A CG1 
21  C  CG2 . ILE A 4  ? 0.0762 0.0619 0.0650 -0.0103 0.0037  -0.0143 4    ILE A CG2 
22  C  CD1 . ILE A 4  ? 0.1152 0.0896 0.0754 -0.0051 0.0195  0.0092  4    ILE A CD1 
23  N  N   . LYS A 5  ? 0.0497 0.0391 0.0446 0.0005  -0.0051 -0.0007 5    LYS A N   
24  C  CA  . LYS A 5  ? 0.0579 0.0529 0.0478 -0.0025 0.0032  -0.0051 5    LYS A CA  
25  C  C   . LYS A 5  ? 0.0600 0.0434 0.0431 0.0040  0.0029  0.0023  5    LYS A C   
26  O  O   . LYS A 5  ? 0.0876 0.0500 0.0622 -0.0133 -0.0261 0.0140  5    LYS A O   
27  C  CB  . LYS A 5  ? 0.0617 0.0727 0.0556 0.0050  0.0066  0.0075  5    LYS A CB  
28  C  CG  . LYS A 5  ? 0.1207 0.1595 0.1163 -0.0895 -0.0040 0.0353  5    LYS A CG  
29  C  CD  . LYS A 5  ? 0.1030 0.2809 0.1713 -0.0664 -0.0082 -0.0281 5    LYS A CD  
30  C  CE  . LYS A 5  ? 0.2451 0.2284 0.2639 0.0664  -0.1203 -0.1621 5    LYS A CE  
31  N  NZ  . LYS A 5  ? 0.5436 0.3848 0.5425 0.0160  -0.1237 0.1370  5    LYS A NZ  
32  N  N   . HIS A 6  ? 0.0736 0.0432 0.0428 -0.0034 -0.0042 -0.0006 6    HIS A N   
33  C  CA  . HIS A 6  ? 0.0605 0.0280 0.0483 -0.0022 0.0040  -0.0023 6    HIS A CA  
34  C  C   . HIS A 6  ? 0.0556 0.0473 0.0393 -0.0026 -0.0022 0.0024  6    HIS A C   
35  O  O   . HIS A 6  ? 0.0872 0.0449 0.0460 0.0157  0.0024  0.0049  6    HIS A O   
36  C  CB  . HIS A 6  ? 0.0632 0.0665 0.0505 0.0053  0.0089  -0.0094 6    HIS A CB  
37  C  CG  . HIS A 6  ? 0.0540 0.0651 0.0460 0.0072  0.0062  -0.0038 6    HIS A CG  
38  N  ND1 . HIS A 6  ? 0.0742 0.0693 0.0760 0.0070  -0.0017 -0.0116 6    HIS A ND1 
39  C  CD2 . HIS A 6  ? 0.0643 0.0506 0.0485 0.0167  0.0006  0.0010  6    HIS A CD2 
40  C  CE1 . HIS A 6  ? 0.0528 0.0563 0.0481 -0.0006 -0.0002 0.0004  6    HIS A CE1 
41  N  NE2 . HIS A 6  ? 0.0740 0.0753 0.0893 -0.0027 -0.0048 -0.0023 6    HIS A NE2 
42  N  N   . TYR A 7  ? 0.0559 0.0455 0.0392 -0.0083 0.0049  0.0078  7    TYR A N   
43  C  CA  . TYR A 7  ? 0.0554 0.0431 0.0413 -0.0058 0.0028  -0.0019 7    TYR A CA  
44  C  C   . TYR A 7  ? 0.0511 0.0407 0.0389 -0.0019 0.0077  0.0016  7    TYR A C   
45  O  O   . TYR A 7  ? 0.0671 0.0505 0.0459 -0.0117 0.0041  0.0110  7    TYR A O   
46  C  CB  . TYR A 7  ? 0.0538 0.0578 0.0588 0.0012  -0.0051 0.0008  7    TYR A CB  
47  C  CG  . TYR A 7  ? 0.0454 0.0582 0.0511 0.0043  0.0068  -0.0030 7    TYR A CG  
48  C  CD1 . TYR A 7  ? 0.0631 0.0541 0.0599 0.0100  -0.0057 -0.0052 7    TYR A CD1 
49  C  CD2 . TYR A 7  ? 0.0647 0.0622 0.0610 0.0073  -0.0108 -0.0010 7    TYR A CD2 
50  C  CE1 . TYR A 7  ? 0.0565 0.0516 0.0644 0.0072  0.0000  -0.0089 7    TYR A CE1 
51  C  CE2 . TYR A 7  ? 0.0619 0.0633 0.0598 0.0021  -0.0050 0.0032  7    TYR A CE2 
52  C  CZ  . TYR A 7  ? 0.0523 0.0682 0.0577 -0.0029 0.0015  0.0020  7    TYR A CZ  
53  O  OH  . TYR A 7  ? 0.0789 0.0678 0.0709 0.0004  -0.0160 -0.0068 7    TYR A OH  
54  N  N   . GLN A 8  ? 0.0797 0.0450 0.0358 -0.0117 -0.0025 0.0064  8    GLN A N   
55  C  CA  . GLN A 8  ? 0.0601 0.0512 0.0495 -0.0145 0.0057  -0.0037 8    GLN A CA  
56  C  C   . GLN A 8  ? 0.0627 0.0575 0.0433 -0.0191 -0.0020 -0.0028 8    GLN A C   
57  O  O   . GLN A 8  ? 0.1219 0.0618 0.0533 -0.0270 0.0336  -0.0110 8    GLN A O   
58  C  CB  . GLN A 8  ? 0.0806 0.0631 0.0546 -0.0018 -0.0026 -0.0057 8    GLN A CB  
59  C  CG  . GLN A 8  ? 0.0973 0.0921 0.0656 -0.0124 -0.0282 -0.0140 8    GLN A CG  
60  C  CD  . GLN A 8  ? 0.1054 0.0677 0.1102 -0.0171 -0.0375 0.0012  8    GLN A CD  
61  O  OE1 . GLN A 8  ? 0.1271 0.1341 0.1661 0.0114  -0.0076 -0.0178 8    GLN A OE1 
62  N  NE2 . GLN A 8  ? 0.1810 0.1140 0.1202 -0.0124 -0.0652 0.0251  8    GLN A NE2 
63  N  N   . PHE A 9  ? 0.0630 0.0516 0.0354 -0.0104 0.0058  -0.0013 9    PHE A N   
64  C  CA  . PHE A 9  ? 0.0630 0.0646 0.0416 -0.0070 0.0095  -0.0082 9    PHE A CA  
65  C  C   . PHE A 9  ? 0.0728 0.0402 0.0440 -0.0141 0.0047  -0.0004 9    PHE A C   
66  O  O   . PHE A 9  ? 0.0859 0.0862 0.0361 -0.0277 0.0017  0.0090  9    PHE A O   
67  C  CB  . PHE A 9  ? 0.0649 0.0564 0.0493 -0.0067 0.0105  -0.0002 9    PHE A CB  
68  C  CG  . PHE A 9  ? 0.0562 0.0742 0.0551 0.0070  0.0031  -0.0069 9    PHE A CG  
69  C  CD1 . PHE A 9  ? 0.0684 0.0565 0.0759 -0.0041 0.0080  -0.0224 9    PHE A CD1 
70  C  CD2 . PHE A 9  ? 0.0719 0.0739 0.0533 0.0072  0.0045  -0.0114 9    PHE A CD2 
71  C  CE1 . PHE A 9  ? 0.0533 0.1197 0.0795 0.0040  -0.0037 -0.0328 9    PHE A CE1 
72  C  CE2 . PHE A 9  ? 0.0821 0.0595 0.0698 0.0135  -0.0146 -0.0054 9    PHE A CE2 
73  C  CZ  . PHE A 9  ? 0.0677 0.0736 0.0794 0.0198  -0.0069 -0.0084 9    PHE A CZ  
74  N  N   . ASN A 10 ? 0.0762 0.0445 0.0464 -0.0049 0.0010  0.0031  10   ASN A N   
75  C  CA  . ASN A 10 ? 0.0747 0.0549 0.0409 -0.0095 0.0026  0.0042  10   ASN A CA  
76  C  C   . ASN A 10 ? 0.0673 0.0604 0.0466 -0.0085 -0.0036 -0.0065 10   ASN A C   
77  O  O   . ASN A 10 ? 0.0720 0.0686 0.0615 -0.0063 0.0072  0.0020  10   ASN A O   
78  C  CB  . ASN A 10 ? 0.1027 0.0742 0.0421 0.0077  -0.0063 0.0071  10   ASN A CB  
79  C  CG  . ASN A 10 ? 0.0914 0.0906 0.0477 -0.0079 -0.0097 0.0109  10   ASN A CG  
80  O  OD1 . ASN A 10 ? 0.1321 0.0943 0.0692 -0.0251 0.0015  0.0095  10   ASN A OD1 
81  N  ND2 . ASN A 10 ? 0.1303 0.1174 0.0428 -0.0522 -0.0272 0.0177  10   ASN A ND2 
82  N  N   . VAL A 11 ? 0.0670 0.0605 0.0401 -0.0002 -0.0018 -0.0012 11   VAL A N   
83  C  CA  . VAL A 11 ? 0.0614 0.0682 0.0524 -0.0076 -0.0013 0.0037  11   VAL A CA  
84  C  C   . VAL A 11 ? 0.0704 0.0560 0.0472 -0.0024 -0.0020 -0.0047 11   VAL A C   
85  O  O   . VAL A 11 ? 0.0680 0.0634 0.0525 -0.0075 0.0030  -0.0060 11   VAL A O   
86  C  CB  . VAL A 11 ? 0.0749 0.0755 0.0439 0.0043  -0.0078 -0.0027 11   VAL A CB  
87  C  CG1 . VAL A 11 ? 0.0826 0.0738 0.0624 0.0028  -0.0117 -0.0008 11   VAL A CG1 
88  C  CG2 . VAL A 11 ? 0.0781 0.0740 0.0453 -0.0110 -0.0040 0.0065  11   VAL A CG2 
89  N  N   . VAL A 12 ? 0.0711 0.0657 0.0794 -0.0057 0.0069  -0.0148 12   VAL A N   
90  C  CA  . VAL A 12 ? 0.0749 0.0655 0.0550 -0.0023 -0.0051 -0.0106 12   VAL A CA  
91  C  C   . VAL A 12 ? 0.0665 0.0637 0.0507 -0.0069 -0.0041 -0.0159 12   VAL A C   
92  O  O   . VAL A 12 ? 0.0674 0.0928 0.0788 0.0032  -0.0047 0.0069  12   VAL A O   
93  C  CB  . VAL A 12 ? 0.0856 0.0856 0.0517 -0.0055 0.0011  -0.0077 12   VAL A CB  
94  C  CG1 . VAL A 12 ? 0.1216 0.1051 0.0473 -0.0111 -0.0019 -0.0176 12   VAL A CG1 
95  C  CG2 . VAL A 12 ? 0.1018 0.1023 0.0651 -0.0004 0.0095  0.0031  12   VAL A CG2 
96  N  N   . MET A 13 ? 0.0626 0.0588 0.0654 0.0039  -0.0044 -0.0029 13   MET A N   
97  C  CA  . MET A 13 ? 0.0886 0.0669 0.0446 -0.0001 -0.0027 -0.0012 13   MET A CA  
98  C  C   . MET A 13 ? 0.0864 0.0635 0.0568 0.0051  -0.0031 -0.0029 13   MET A C   
99  O  O   . MET A 13 ? 0.0804 0.0704 0.0921 0.0006  0.0013  0.0060  13   MET A O   
100 C  CB  . MET A 13 ? 0.0705 0.0808 0.0525 0.0088  -0.0040 -0.0126 13   MET A CB  
101 C  CG  . MET A 13 ? 0.0813 0.0680 0.0626 0.0029  -0.0082 -0.0136 13   MET A CG  
102 S  SD  . MET A 13 ? 0.1001 0.0821 0.0499 0.0060  -0.0025 -0.0073 13   MET A SD  
103 C  CE  . MET A 13 ? 0.0788 0.0683 0.0639 -0.0042 0.0007  -0.0037 13   MET A CE  
104 N  N   . THR A 14 ? 0.0883 0.0673 0.0829 0.0073  -0.0155 -0.0202 14   THR A N   
105 C  CA  . THR A 14 ? 0.0957 0.0796 0.1099 0.0000  -0.0278 -0.0224 14   THR A CA  
106 C  C   . THR A 14 ? 0.1168 0.0754 0.1222 -0.0123 -0.0351 -0.0177 14   THR A C   
107 O  O   . THR A 14 ? 0.1058 0.1439 0.1540 -0.0311 -0.0525 -0.0116 14   THR A O   
108 C  CB  . THR A 14 ? 0.1394 0.0839 0.0970 0.0178  -0.0436 -0.0344 14   THR A CB  
109 O  OG1 . THR A 14 ? 0.1699 0.1325 0.1032 0.0668  -0.0427 -0.0471 14   THR A OG1 
110 C  CG2 . THR A 14 ? 0.1570 0.1690 0.0800 0.0121  -0.0087 -0.0470 14   THR A CG2 
111 N  N   . CYS A 15 ? 0.0940 0.1083 0.1167 -0.0341 -0.0156 -0.0286 15   CYS A N   
112 C  CA  . CYS A 15 ? 0.1200 0.1053 0.1292 -0.0338 -0.0235 -0.0125 15   CYS A CA  
113 C  C   . CYS A 15 ? 0.0906 0.0906 0.1246 -0.0205 -0.0030 -0.0198 15   CYS A C   
114 O  O   . CYS A 15 ? 0.0866 0.0632 0.1030 -0.0087 -0.0138 0.0031  15   CYS A O   
115 C  CB  . CYS A 15 ? 0.1576 0.1044 0.1218 -0.0367 -0.0299 -0.0370 15   CYS A CB  
116 S  SG  . CYS A 15 ? 0.1694 0.0975 0.1187 -0.0103 -0.0134 -0.0385 15   CYS A SG  
117 N  N   . SER A 16 ? 0.1116 0.0899 0.1312 -0.0299 -0.0076 -0.0018 16   SER A N   
118 C  CA  . SER A 16 ? 0.1149 0.0981 0.1275 -0.0301 0.0004  0.0052  16   SER A CA  
119 C  C   . SER A 16 ? 0.1138 0.0890 0.0916 -0.0299 0.0093  -0.0088 16   SER A C   
120 O  O   . SER A 16 ? 0.1266 0.1141 0.1118 -0.0509 0.0131  -0.0349 16   SER A O   
121 C  CB  . SER A 16 ? 0.1083 0.1305 0.1260 -0.0301 -0.0044 0.0152  16   SER A CB  
122 O  OG  . SER A 16 ? 0.1685 0.1224 0.1311 -0.0542 -0.0172 0.0278  16   SER A OG  
123 N  N   . GLY A 17 ? 0.1279 0.0712 0.0875 -0.0179 -0.0146 -0.0104 17   GLY A N   
124 C  CA  . GLY A 17 ? 0.1453 0.0625 0.1000 0.0024  -0.0217 0.0017  17   GLY A CA  
125 C  C   . GLY A 17 ? 0.1073 0.0739 0.0879 0.0059  -0.0016 0.0002  17   GLY A C   
126 O  O   . GLY A 17 ? 0.1503 0.0690 0.0852 0.0038  -0.0273 0.0000  17   GLY A O   
127 N  N   . CYS A 18 ? 0.0934 0.0678 0.0833 0.0005  -0.0080 -0.0055 18   CYS A N   
128 C  CA  . CYS A 18 ? 0.0904 0.0705 0.0657 0.0019  -0.0084 -0.0081 18   CYS A CA  
129 C  C   . CYS A 18 ? 0.0828 0.0471 0.0615 0.0045  -0.0110 0.0087  18   CYS A C   
130 O  O   . CYS A 18 ? 0.0924 0.0676 0.0718 -0.0070 -0.0075 -0.0026 18   CYS A O   
131 C  CB  . CYS A 18 ? 0.1001 0.0612 0.0722 -0.0031 -0.0215 -0.0057 18   CYS A CB  
132 S  SG  . CYS A 18 ? 0.1067 0.1152 0.0747 0.0148  -0.0112 -0.0174 18   CYS A SG  
133 N  N   . SER A 19 ? 0.0856 0.0753 0.0796 0.0031  -0.0061 -0.0057 19   SER A N   
134 C  CA  . SER A 19 ? 0.0805 0.0696 0.0792 -0.0016 -0.0113 -0.0155 19   SER A CA  
135 C  C   . SER A 19 ? 0.0836 0.0679 0.0741 -0.0210 0.0026  -0.0058 19   SER A C   
136 O  O   . SER A 19 ? 0.0747 0.0734 0.0798 -0.0021 -0.0111 -0.0139 19   SER A O   
137 C  CB  . SER A 19 ? 0.0794 0.0982 0.1107 -0.0064 0.0018  -0.0333 19   SER A CB  
138 O  OG  . SER A 19 ? 0.1117 0.1157 0.2128 -0.0304 0.0161  -0.0390 19   SER A OG  
139 N  N   . GLY A 20 ? 0.1036 0.0717 0.0638 -0.0272 0.0057  0.0060  20   GLY A N   
140 C  CA  . GLY A 20 ? 0.1012 0.0735 0.0630 -0.0121 0.0073  -0.0090 20   GLY A CA  
141 C  C   . GLY A 20 ? 0.1012 0.0405 0.0478 -0.0023 0.0083  0.0078  20   GLY A C   
142 O  O   . GLY A 20 ? 0.1000 0.0583 0.0545 -0.0107 0.0048  -0.0012 20   GLY A O   
143 N  N   . ALA A 21 ? 0.0973 0.0539 0.0589 0.0027  0.0061  0.0126  21   ALA A N   
144 C  CA  . ALA A 21 ? 0.0853 0.0595 0.0674 0.0198  0.0044  0.0062  21   ALA A CA  
145 C  C   . ALA A 21 ? 0.0837 0.0554 0.0564 0.0045  0.0133  0.0157  21   ALA A C   
146 O  O   . ALA A 21 ? 0.0835 0.0613 0.0973 0.0061  -0.0061 0.0119  21   ALA A O   
147 C  CB  . ALA A 21 ? 0.1146 0.1030 0.0703 -0.0010 0.0169  -0.0216 21   ALA A CB  
148 N  N   . VAL A 22 ? 0.0782 0.0532 0.0592 0.0050  0.0040  0.0015  22   VAL A N   
149 C  CA  . VAL A 22 ? 0.0657 0.0489 0.0666 -0.0053 -0.0041 0.0066  22   VAL A CA  
150 C  C   . VAL A 22 ? 0.0617 0.0439 0.0689 -0.0010 -0.0021 0.0036  22   VAL A C   
151 O  O   . VAL A 22 ? 0.0665 0.0596 0.0742 -0.0013 -0.0076 0.0018  22   VAL A O   
152 C  CB  . VAL A 22 ? 0.1019 0.0493 0.0746 0.0032  -0.0160 0.0006  22   VAL A CB  
153 C  CG1 . VAL A 22 ? 0.1367 0.0379 0.0993 -0.0048 -0.0439 0.0186  22   VAL A CG1 
154 C  CG2 . VAL A 22 ? 0.1310 0.0777 0.0650 -0.0097 -0.0027 0.0265  22   VAL A CG2 
155 N  N   . ASN A 23 ? 0.0683 0.0589 0.0599 -0.0055 -0.0077 -0.0090 23   ASN A N   
156 C  CA  . ASN A 23 ? 0.0646 0.0878 0.0570 -0.0011 0.0034  -0.0092 23   ASN A CA  
157 C  C   . ASN A 23 ? 0.0611 0.0963 0.0494 -0.0002 0.0124  -0.0094 23   ASN A C   
158 O  O   . ASN A 23 ? 0.0677 0.0904 0.0518 -0.0036 0.0032  -0.0070 23   ASN A O   
159 C  CB  . ASN A 23 ? 0.0660 0.0803 0.0680 -0.0057 0.0013  -0.0157 23   ASN A CB  
160 C  CG  . ASN A 23 ? 0.0551 0.1171 0.0803 -0.0237 0.0137  -0.0261 23   ASN A CG  
161 O  OD1 . ASN A 23 ? 0.1009 0.1760 0.1177 0.0187  0.0050  -0.0715 23   ASN A OD1 
162 N  ND2 . ASN A 23 ? 0.1471 0.1327 0.0553 -0.0529 0.0169  -0.0073 23   ASN A ND2 
163 N  N   . LYS A 24 ? 0.0671 0.0960 0.0462 -0.0003 -0.0005 -0.0061 24   LYS A N   
164 C  CA  . LYS A 24 ? 0.0947 0.0834 0.0505 -0.0051 -0.0106 0.0142  24   LYS A CA  
165 C  C   . LYS A 24 ? 0.0657 0.0743 0.0646 0.0165  -0.0065 0.0083  24   LYS A C   
166 O  O   . LYS A 24 ? 0.0759 0.0882 0.0551 0.0118  0.0001  0.0064  24   LYS A O   
167 C  CB  . LYS A 24 ? 0.1096 0.0808 0.0943 -0.0010 -0.0167 0.0159  24   LYS A CB  
168 C  CG  . LYS A 24 ? 0.1949 0.1012 0.2280 0.0274  -0.0972 0.0367  24   LYS A CG  
169 C  CD  . LYS A 24 ? 0.2700 0.1606 0.3716 0.1235  -0.0975 -0.0088 24   LYS A CD  
170 C  CE  . LYS A 24 ? 0.4921 0.1128 0.2960 0.0578  -0.0613 0.0133  24   LYS A CE  
171 N  NZ  . LYS A 24 ? 0.3050 0.2871 0.1389 -0.0489 0.0193  0.0735  24   LYS A NZ  
172 N  N   . VAL A 25 ? 0.0721 0.0931 0.0528 -0.0032 -0.0016 -0.0156 25   VAL A N   
173 C  CA  . VAL A 25 ? 0.0688 0.1275 0.0619 -0.0196 0.0086  -0.0189 25   VAL A CA  
174 C  C   . VAL A 25 ? 0.0601 0.0938 0.0581 -0.0141 -0.0003 0.0000  25   VAL A C   
175 O  O   . VAL A 25 ? 0.0636 0.0887 0.1013 -0.0067 -0.0123 -0.0126 25   VAL A O   
176 C  CB  . VAL A 25 ? 0.1111 0.1829 0.0648 -0.0462 0.0160  -0.0268 25   VAL A CB  
177 C  CG1 . VAL A 25 ? 0.1993 0.2505 0.1138 -0.0802 0.0814  -0.0908 25   VAL A CG1 
178 C  CG2 . VAL A 25 ? 0.1224 0.2664 0.1250 -0.0832 -0.0130 0.0667  25   VAL A CG2 
179 N  N   . LEU A 26 ? 0.0643 0.0864 0.0543 -0.0103 -0.0025 0.0184  26   LEU A N   
180 C  CA  . LEU A 26 ? 0.0602 0.0682 0.0892 -0.0192 -0.0052 0.0135  26   LEU A CA  
181 C  C   . LEU A 26 ? 0.0514 0.0480 0.0731 -0.0093 -0.0012 -0.0030 26   LEU A C   
182 O  O   . LEU A 26 ? 0.0716 0.0462 0.0954 -0.0057 -0.0040 -0.0015 26   LEU A O   
183 C  CB  . LEU A 26 ? 0.0792 0.0580 0.1206 -0.0136 -0.0162 0.0306  26   LEU A CB  
184 C  CG  . LEU A 26 ? 0.1035 0.0746 0.1070 -0.0009 -0.0042 0.0113  26   LEU A CG  
185 C  CD1 . LEU A 26 ? 0.1167 0.1044 0.0908 0.0055  -0.0053 0.0173  26   LEU A CD1 
186 C  CD2 . LEU A 26 ? 0.1554 0.1546 0.1893 -0.0744 -0.0276 0.0985  26   LEU A CD2 
187 N  N   . THR A 27 ? 0.0692 0.0561 0.0584 -0.0132 0.0035  -0.0039 27   THR A N   
188 C  CA  . THR A 27 ? 0.0671 0.0681 0.0513 -0.0047 0.0079  -0.0075 27   THR A CA  
189 C  C   . THR A 27 ? 0.0744 0.0745 0.0510 -0.0087 0.0044  -0.0023 27   THR A C   
190 O  O   . THR A 27 ? 0.0863 0.1294 0.0604 -0.0151 -0.0033 -0.0090 27   THR A O   
191 C  CB  . THR A 27 ? 0.0721 0.0718 0.0384 -0.0034 0.0120  0.0056  27   THR A CB  
192 O  OG1 . THR A 27 ? 0.0761 0.0643 0.0823 0.0005  0.0013  0.0044  27   THR A OG1 
193 C  CG2 . THR A 27 ? 0.0751 0.0535 0.0649 -0.0132 0.0119  0.0078  27   THR A CG2 
194 N  N   . LYS A 28 ? 0.0706 0.0552 0.0698 -0.0025 0.0050  -0.0008 28   LYS A N   
195 C  CA  . LYS A 28 ? 0.0729 0.0701 0.0688 0.0090  -0.0072 -0.0005 28   LYS A CA  
196 C  C   . LYS A 28 ? 0.0629 0.0721 0.0642 0.0000  -0.0004 0.0063  28   LYS A C   
197 O  O   . LYS A 28 ? 0.0733 0.0821 0.0757 -0.0050 -0.0145 0.0081  28   LYS A O   
198 C  CB  . LYS A 28 ? 0.0796 0.1154 0.0864 0.0410  -0.0163 -0.0151 28   LYS A CB  
199 C  CG  . LYS A 28 ? 0.1089 0.1097 0.1347 0.0566  -0.0358 -0.0343 28   LYS A CG  
200 C  CD  . LYS A 28 ? 0.1882 0.1610 0.2001 0.0733  0.0143  -0.0558 28   LYS A CD  
201 C  CE  . LYS A 28 ? 0.2729 0.2114 0.2454 0.0342  -0.0218 -0.1503 28   LYS A CE  
202 N  NZ  . LYS A 28 ? 0.2372 0.1474 0.4306 -0.0414 0.0931  -0.1223 28   LYS A NZ  
203 N  N   . LEU A 29 ? 0.0565 0.0630 0.0698 -0.0076 -0.0119 -0.0069 29   LEU A N   
204 C  CA  . LEU A 29 ? 0.0658 0.0622 0.0778 -0.0060 0.0117  0.0011  29   LEU A CA  
205 C  C   . LEU A 29 ? 0.0676 0.0687 0.0664 -0.0228 -0.0014 -0.0171 29   LEU A C   
206 O  O   . LEU A 29 ? 0.0673 0.0767 0.0837 -0.0185 0.0028  -0.0186 29   LEU A O   
207 C  CB  . LEU A 29 ? 0.0697 0.0557 0.0785 -0.0025 0.0091  0.0004  29   LEU A CB  
208 C  CG  . LEU A 29 ? 0.0785 0.0665 0.0655 -0.0013 0.0008  0.0010  29   LEU A CG  
209 C  CD1 . LEU A 29 ? 0.0994 0.0644 0.0704 -0.0094 -0.0039 0.0073  29   LEU A CD1 
210 C  CD2 . LEU A 29 ? 0.0737 0.1007 0.0673 0.0063  0.0127  0.0022  29   LEU A CD2 
211 N  N   . GLU A 30 ? 0.0739 0.0800 0.0737 -0.0223 0.0083  -0.0170 30   GLU A N   
212 C  CA  . GLU A 30 ? 0.0868 0.0820 0.0799 -0.0245 0.0118  -0.0133 30   GLU A CA  
213 C  C   . GLU A 30 ? 0.0794 0.0873 0.0751 -0.0175 0.0139  -0.0062 30   GLU A C   
214 O  O   . GLU A 30 ? 0.0902 0.1122 0.1292 -0.0054 -0.0116 -0.0157 30   GLU A O   
215 C  CB  . GLU A 30 ? 0.0883 0.1029 0.0856 -0.0286 0.0050  0.0091  30   GLU A CB  
216 C  CG  . GLU A 30 ? 0.0753 0.0928 0.0994 -0.0144 0.0049  -0.0022 30   GLU A CG  
217 C  CD  . GLU A 30 ? 0.0884 0.0880 0.0900 -0.0190 -0.0009 -0.0108 30   GLU A CD  
218 O  OE1 . GLU A 30 ? 0.1056 0.0922 0.2864 -0.0359 0.0237  -0.0337 30   GLU A OE1 
219 O  OE2 . GLU A 30 ? 0.0746 0.1204 0.1035 -0.0194 0.0013  0.0138  30   GLU A OE2 
220 N  N   . PRO A 31 ? 0.1084 0.1017 0.0800 -0.0207 -0.0010 -0.0113 31   PRO A N   
221 C  CA  . PRO A 31 ? 0.1297 0.0977 0.0661 -0.0218 0.0239  -0.0270 31   PRO A CA  
222 C  C   . PRO A 31 ? 0.1154 0.1021 0.0985 -0.0034 0.0172  -0.0254 31   PRO A C   
223 O  O   . PRO A 31 ? 0.1753 0.1381 0.1069 0.0380  0.0347  -0.0113 31   PRO A O   
224 C  CB  . PRO A 31 ? 0.2150 0.1356 0.0686 -0.0233 -0.0012 -0.0372 31   PRO A CB  
225 C  CG  . PRO A 31 ? 0.2194 0.1788 0.1062 0.0294  -0.0446 -0.0416 31   PRO A CG  
226 C  CD  . PRO A 31 ? 0.1963 0.1609 0.0923 0.0253  -0.0541 -0.0264 31   PRO A CD  
227 N  N   . ASP A 32 ? 0.0799 0.0958 0.0716 0.0000  -0.0112 -0.0189 32   ASP A N   
228 C  CA  . ASP A 32 ? 0.0604 0.0994 0.0895 0.0184  -0.0240 -0.0194 32   ASP A CA  
229 C  C   . ASP A 32 ? 0.0916 0.0931 0.0749 -0.0014 -0.0283 -0.0205 32   ASP A C   
230 O  O   . ASP A 32 ? 0.1341 0.1499 0.0930 -0.0630 -0.0563 0.0131  32   ASP A O   
231 C  CB  . ASP A 32 ? 0.0811 0.1039 0.1208 -0.0100 -0.0291 0.0012  32   ASP A CB  
232 C  CG  . ASP A 32 ? 0.1113 0.1990 0.1439 -0.0643 -0.0239 -0.0307 32   ASP A CG  
233 O  OD1 . ASP A 32 ? 0.4716 0.3995 0.1315 -0.2828 -0.1059 0.0189  32   ASP A OD1 
234 O  OD2 . ASP A 32 ? 0.1515 0.1791 0.1856 -0.0645 -0.0554 -0.0344 32   ASP A OD2 
235 N  N   . VAL A 33 ? 0.1327 0.0556 0.1041 0.0094  -0.0734 -0.0072 33   VAL A N   
236 C  CA  . VAL A 33 ? 0.1029 0.0578 0.1064 0.0207  -0.0573 -0.0160 33   VAL A CA  
237 C  C   . VAL A 33 ? 0.1201 0.0619 0.0613 -0.0119 -0.0344 0.0017  33   VAL A C   
238 O  O   . VAL A 33 ? 0.2522 0.0694 0.0904 -0.0235 -0.0252 0.0176  33   VAL A O   
239 C  CB  . VAL A 33 ? 0.1068 0.0635 0.1271 0.0238  -0.0668 -0.0343 33   VAL A CB  
240 C  CG1 . VAL A 33 ? 0.0829 0.0868 0.0919 -0.0077 -0.0335 -0.0087 33   VAL A CG1 
241 C  CG2 . VAL A 33 ? 0.0826 0.1287 0.2213 0.0332  -0.0498 -0.1112 33   VAL A CG2 
242 N  N   . SER A 34 ? 0.0858 0.0704 0.0573 -0.0225 -0.0171 0.0082  34   SER A N   
243 C  CA  . SER A 34 ? 0.0954 0.1201 0.0485 -0.0232 -0.0067 -0.0146 34   SER A CA  
244 C  C   . SER A 34 ? 0.0905 0.0827 0.0385 -0.0176 -0.0017 -0.0030 34   SER A C   
245 O  O   . SER A 34 ? 0.1029 0.1355 0.0443 -0.0316 0.0058  -0.0119 34   SER A O   
246 C  CB  . SER A 34 ? 0.1205 0.1125 0.1274 -0.0248 0.0274  -0.0546 34   SER A CB  
247 O  OG  . SER A 34 ? 0.1653 0.1680 0.2727 -0.0110 -0.0415 -0.1141 34   SER A OG  
248 N  N   . LYS A 35 ? 0.0738 0.0752 0.0462 -0.0170 -0.0020 -0.0006 35   LYS A N   
249 C  CA  . LYS A 35 ? 0.0700 0.0671 0.0422 -0.0058 0.0024  -0.0085 35   LYS A CA  
250 C  C   . LYS A 35 ? 0.0626 0.0598 0.0420 -0.0075 -0.0008 -0.0025 35   LYS A C   
251 O  O   . LYS A 35 ? 0.0702 0.0448 0.0449 -0.0132 0.0029  -0.0084 35   LYS A O   
252 C  CB  . LYS A 35 ? 0.0740 0.0541 0.0491 -0.0106 0.0078  -0.0047 35   LYS A CB  
253 C  CG  . LYS A 35 ? 0.0752 0.0540 0.1012 -0.0126 -0.0129 0.0052  35   LYS A CG  
254 C  CD  . LYS A 35 ? 0.0871 0.0560 0.1136 -0.0039 -0.0071 -0.0177 35   LYS A CD  
255 C  CE  . LYS A 35 ? 0.1139 0.1189 0.2767 0.0376  -0.0887 -0.0792 35   LYS A CE  
256 N  NZ  . LYS A 35 ? 0.1086 0.1061 0.1347 -0.0001 -0.0275 -0.0004 35   LYS A NZ  
257 N  N   . ILE A 36 ? 0.0448 0.0632 0.0339 -0.0149 0.0028  0.0023  36   ILE A N   
258 C  CA  . ILE A 36 ? 0.0561 0.0637 0.0314 -0.0011 0.0002  0.0021  36   ILE A CA  
259 C  C   . ILE A 36 ? 0.0613 0.0473 0.0490 -0.0065 -0.0060 0.0010  36   ILE A C   
260 O  O   . ILE A 36 ? 0.0581 0.0654 0.0509 -0.0134 -0.0010 0.0009  36   ILE A O   
261 C  CB  . ILE A 36 ? 0.0714 0.0735 0.0741 0.0077  -0.0055 -0.0330 36   ILE A CB  
262 C  CG1 . ILE A 36 ? 0.0908 0.0761 0.0919 0.0168  -0.0140 0.0011  36   ILE A CG1 
263 C  CG2 . ILE A 36 ? 0.0739 0.1382 0.0814 0.0214  -0.0232 -0.0375 36   ILE A CG2 
264 C  CD1 . ILE A 36 ? 0.1227 0.0715 0.1416 0.0236  -0.0265 -0.0223 36   ILE A CD1 
265 N  N   . ASP A 37 ? 0.0588 0.0612 0.0373 -0.0155 0.0005  -0.0035 37   ASP A N   
266 C  CA  . ASP A 37 ? 0.0553 0.0591 0.0442 -0.0232 -0.0043 0.0011  37   ASP A CA  
267 C  C   . ASP A 37 ? 0.0615 0.0667 0.0423 -0.0288 -0.0038 0.0009  37   ASP A C   
268 O  O   . ASP A 37 ? 0.1250 0.0971 0.0583 -0.0685 0.0182  -0.0120 37   ASP A O   
269 C  CB  . ASP A 37 ? 0.0882 0.0867 0.0781 0.0047  -0.0075 0.0069  37   ASP A CB  
270 C  CG  . ASP A 37 ? 0.0898 0.1380 0.0943 0.0138  -0.0277 0.0174  37   ASP A CG  
271 O  OD1 . ASP A 37 ? 0.1279 0.1361 0.1084 -0.0142 -0.0388 0.0135  37   ASP A OD1 
272 O  OD2 . ASP A 37 ? 0.1020 0.1959 0.1715 0.0141  0.0012  0.0179  37   ASP A OD2 
273 N  N   . ILE A 38 ? 0.0525 0.0604 0.0376 -0.0167 0.0033  0.0067  38   ILE A N   
274 C  CA  . ILE A 38 ? 0.0754 0.0577 0.0378 -0.0182 -0.0010 0.0007  38   ILE A CA  
275 C  C   . ILE A 38 ? 0.0778 0.0700 0.0370 -0.0185 -0.0022 -0.0006 38   ILE A C   
276 O  O   . ILE A 38 ? 0.0793 0.0948 0.0561 -0.0354 -0.0109 0.0097  38   ILE A O   
277 C  CB  . ILE A 38 ? 0.0785 0.0636 0.0468 -0.0161 0.0074  -0.0035 38   ILE A CB  
278 C  CG1 . ILE A 38 ? 0.0746 0.0744 0.0549 -0.0045 -0.0004 0.0093  38   ILE A CG1 
279 C  CG2 . ILE A 38 ? 0.1173 0.1024 0.0470 0.0199  -0.0098 -0.0131 38   ILE A CG2 
280 C  CD1 . ILE A 38 ? 0.1007 0.0907 0.0914 0.0191  0.0107  -0.0086 38   ILE A CD1 
281 N  N   . SER A 39 ? 0.0772 0.0819 0.0485 -0.0250 -0.0051 0.0051  39   SER A N   
282 C  CA  . SER A 39 ? 0.0757 0.1173 0.0482 -0.0228 -0.0102 0.0004  39   SER A CA  
283 C  C   . SER A 39 ? 0.0668 0.0956 0.0531 -0.0095 -0.0133 0.0089  39   SER A C   
284 O  O   . SER A 39 ? 0.0898 0.0986 0.0479 -0.0233 -0.0053 -0.0027 39   SER A O   
285 C  CB  . SER A 39 ? 0.0970 0.1568 0.0423 0.0248  -0.0179 -0.0224 39   SER A CB  
286 O  OG  . SER A 39 ? 0.1158 0.1848 0.0823 0.0383  -0.0428 -0.0456 39   SER A OG  
287 N  N   . LEU A 40 ? 0.0692 0.0884 0.0676 -0.0062 -0.0112 0.0100  40   LEU A N   
288 C  CA  . LEU A 40 ? 0.0700 0.1001 0.0735 -0.0145 -0.0109 -0.0030 40   LEU A CA  
289 C  C   . LEU A 40 ? 0.0694 0.0835 0.0635 -0.0048 -0.0055 -0.0113 40   LEU A C   
290 O  O   . LEU A 40 ? 0.0662 0.0874 0.0615 -0.0036 0.0009  -0.0056 40   LEU A O   
291 C  CB  . LEU A 40 ? 0.1148 0.0941 0.0891 -0.0104 -0.0230 0.0012  40   LEU A CB  
292 C  CG  . LEU A 40 ? 0.1023 0.1242 0.1016 -0.0134 -0.0176 0.0204  40   LEU A CG  
293 C  CD1 . LEU A 40 ? 0.1709 0.1072 0.1666 -0.0024 0.0167  0.0341  40   LEU A CD1 
294 C  CD2 . LEU A 40 ? 0.1102 0.1644 0.1737 0.0165  0.0112  0.0300  40   LEU A CD2 
295 N  N   . GLU A 41 ? 0.0588 0.1073 0.0547 -0.0046 -0.0048 -0.0076 41   GLU A N   
296 C  CA  . GLU A 41 ? 0.0551 0.1168 0.0540 0.0000  -0.0048 -0.0165 41   GLU A CA  
297 C  C   . GLU A 41 ? 0.0508 0.1156 0.0455 0.0076  0.0061  -0.0132 41   GLU A C   
298 O  O   . GLU A 41 ? 0.0739 0.1374 0.0581 -0.0093 -0.0244 -0.0114 41   GLU A O   
299 C  CB  . GLU A 41 ? 0.0419 0.2065 0.0687 -0.0070 -0.0064 -0.0023 41   GLU A CB  
300 C  CG  . GLU A 41 ? 0.0806 0.2276 0.1861 -0.0417 0.0469  -0.0081 41   GLU A CG  
301 C  CD  . GLU A 41 ? 0.3050 0.3665 0.3192 -0.0322 -0.0041 0.2025  41   GLU A CD  
302 O  OE1 . GLU A 41 ? 0.2347 0.5305 0.1713 0.0702  0.0400  0.1487  41   GLU A OE1 
303 O  OE2 . GLU A 41 ? 0.5144 0.5739 0.4437 -0.1774 0.0585  0.2818  41   GLU A OE2 
304 N  N   . LYS A 42 ? 0.0691 0.0871 0.0542 0.0141  -0.0161 -0.0126 42   LYS A N   
305 C  CA  . LYS A 42 ? 0.0785 0.0912 0.0683 0.0062  -0.0059 -0.0064 42   LYS A CA  
306 C  C   . LYS A 42 ? 0.0761 0.0707 0.0484 0.0042  -0.0150 -0.0119 42   LYS A C   
307 O  O   . LYS A 42 ? 0.0870 0.0679 0.0768 0.0021  -0.0036 -0.0004 42   LYS A O   
308 C  CB  . LYS A 42 ? 0.0846 0.0927 0.1132 0.0067  0.0062  -0.0182 42   LYS A CB  
309 C  CG  . LYS A 42 ? 0.0961 0.2375 0.1314 0.0462  0.0016  -0.0795 42   LYS A CG  
310 C  CD  . LYS A 42 ? 0.1554 0.2373 0.2582 0.0720  0.0366  -0.1014 42   LYS A CD  
311 C  CE  . LYS A 42 ? 0.4005 0.2480 0.3481 -0.0203 0.0082  -0.0788 42   LYS A CE  
312 N  NZ  . LYS A 42 ? 0.6485 0.4165 0.4068 -0.0381 0.0059  0.0712  42   LYS A NZ  
313 N  N   . GLN A 43 ? 0.0669 0.0752 0.0367 0.0018  -0.0111 -0.0042 43   GLN A N   
314 C  CA  . GLN A 43 ? 0.0565 0.0828 0.0486 0.0019  -0.0088 -0.0040 43   GLN A CA  
315 C  C   . GLN A 43 ? 0.0521 0.0674 0.0407 0.0080  -0.0085 0.0081  43   GLN A C   
316 O  O   . GLN A 43 ? 0.0674 0.0576 0.0477 0.0021  0.0003  -0.0013 43   GLN A O   
317 C  CB  . GLN A 43 ? 0.0745 0.0735 0.0422 0.0016  -0.0023 -0.0031 43   GLN A CB  
318 C  CG  . GLN A 43 ? 0.0623 0.0835 0.0417 -0.0036 0.0087  -0.0054 43   GLN A CG  
319 C  CD  . GLN A 43 ? 0.0618 0.0848 0.0501 -0.0022 -0.0110 -0.0189 43   GLN A CD  
320 O  OE1 . GLN A 43 ? 0.0666 0.0906 0.0682 0.0021  0.0022  -0.0088 43   GLN A OE1 
321 N  NE2 . GLN A 43 ? 0.0598 0.0741 0.0729 0.0086  -0.0014 -0.0047 43   GLN A NE2 
322 N  N   . LEU A 44 ? 0.0574 0.0880 0.0436 -0.0139 -0.0039 0.0023  44   LEU A N   
323 C  CA  . LEU A 44 ? 0.0695 0.0817 0.0446 -0.0046 0.0013  -0.0009 44   LEU A CA  
324 C  C   . LEU A 44 ? 0.0701 0.0574 0.0440 -0.0112 -0.0005 -0.0084 44   LEU A C   
325 O  O   . LEU A 44 ? 0.0971 0.1166 0.0456 -0.0558 -0.0136 0.0112  44   LEU A O   
326 C  CB  . LEU A 44 ? 0.1026 0.1133 0.0794 0.0298  -0.0178 -0.0153 44   LEU A CB  
327 C  CG  . LEU A 44 ? 0.1403 0.0816 0.1163 0.0099  -0.0516 -0.0116 44   LEU A CG  
328 C  CD1 . LEU A 44 ? 0.1465 0.0822 0.4178 0.0452  -0.0732 -0.0209 44   LEU A CD1 
329 C  CD2 . LEU A 44 ? 0.1675 0.1269 0.2833 0.0049  -0.0329 0.1063  44   LEU A CD2 
330 N  N   . VAL A 45 ? 0.0666 0.0549 0.0357 -0.0165 0.0039  -0.0001 45   VAL A N   
331 C  CA  . VAL A 45 ? 0.0752 0.0470 0.0385 -0.0066 0.0004  0.0044  45   VAL A CA  
332 C  C   . VAL A 45 ? 0.0610 0.0580 0.0318 -0.0081 -0.0097 0.0044  45   VAL A C   
333 O  O   . VAL A 45 ? 0.1040 0.0520 0.0438 -0.0217 0.0102  -0.0072 45   VAL A O   
334 C  CB  . VAL A 45 ? 0.0703 0.0519 0.0569 -0.0111 0.0000  0.0044  45   VAL A CB  
335 C  CG1 . VAL A 45 ? 0.0902 0.0442 0.0644 -0.0077 -0.0196 -0.0046 45   VAL A CG1 
336 C  CG2 . VAL A 45 ? 0.0762 0.0570 0.0486 0.0003  0.0074  -0.0069 45   VAL A CG2 
337 N  N   . ASP A 46 ? 0.0656 0.0411 0.0458 -0.0142 -0.0033 0.0036  46   ASP A N   
338 C  CA  . ASP A 46 ? 0.0610 0.0463 0.0443 -0.0110 -0.0009 -0.0008 46   ASP A CA  
339 C  C   . ASP A 46 ? 0.0692 0.0447 0.0387 -0.0167 0.0050  0.0009  46   ASP A C   
340 O  O   . ASP A 46 ? 0.0870 0.0670 0.0420 -0.0273 -0.0072 0.0109  46   ASP A O   
341 C  CB  . ASP A 46 ? 0.0638 0.0566 0.0815 -0.0060 0.0085  -0.0024 46   ASP A CB  
342 C  CG  . ASP A 46 ? 0.0852 0.0592 0.1119 0.0041  -0.0364 -0.0110 46   ASP A CG  
343 O  OD1 . ASP A 46 ? 0.0861 0.0710 0.0893 -0.0011 -0.0293 -0.0087 46   ASP A OD1 
344 O  OD2 . ASP A 46 ? 0.2654 0.0993 0.3226 -0.0694 -0.2201 0.0436  46   ASP A OD2 
345 N  N   . VAL A 47 ? 0.0622 0.0395 0.0327 -0.0001 0.0001  0.0062  47   VAL A N   
346 C  CA  . VAL A 47 ? 0.0672 0.0414 0.0305 0.0012  0.0041  0.0051  47   VAL A CA  
347 C  C   . VAL A 47 ? 0.0645 0.0423 0.0374 -0.0117 0.0042  -0.0015 47   VAL A C   
348 O  O   . VAL A 47 ? 0.0901 0.0451 0.0344 -0.0122 0.0010  -0.0027 47   VAL A O   
349 C  CB  . VAL A 47 ? 0.0605 0.0417 0.0625 -0.0040 -0.0028 -0.0083 47   VAL A CB  
350 C  CG1 . VAL A 47 ? 0.0788 0.0551 0.0672 0.0053  -0.0114 -0.0039 47   VAL A CG1 
351 C  CG2 . VAL A 47 ? 0.0694 0.0685 0.0735 0.0152  -0.0074 -0.0286 47   VAL A CG2 
352 N  N   . TYR A 48 ? 0.0637 0.0266 0.0409 -0.0015 0.0024  0.0033  48   TYR A N   
353 C  CA  . TYR A 48 ? 0.0559 0.0493 0.0266 -0.0062 0.0017  -0.0003 48   TYR A CA  
354 C  C   . TYR A 48 ? 0.0615 0.0572 0.0356 -0.0038 0.0011  0.0000  48   TYR A C   
355 O  O   . TYR A 48 ? 0.0806 0.0512 0.0477 -0.0036 -0.0086 0.0067  48   TYR A O   
356 C  CB  . TYR A 48 ? 0.0681 0.0412 0.0466 0.0020  0.0067  -0.0074 48   TYR A CB  
357 C  CG  . TYR A 48 ? 0.0551 0.0581 0.0443 0.0076  0.0131  -0.0126 48   TYR A CG  
358 C  CD1 . TYR A 48 ? 0.0725 0.0723 0.0452 0.0049  -0.0003 -0.0146 48   TYR A CD1 
359 C  CD2 . TYR A 48 ? 0.0714 0.0572 0.0458 -0.0021 0.0147  0.0049  48   TYR A CD2 
360 C  CE1 . TYR A 48 ? 0.0716 0.0676 0.0574 -0.0037 -0.0034 -0.0028 48   TYR A CE1 
361 C  CE2 . TYR A 48 ? 0.0707 0.0551 0.0694 0.0039  0.0166  0.0090  48   TYR A CE2 
362 C  CZ  . TYR A 48 ? 0.0600 0.0840 0.0489 0.0013  0.0135  0.0029  48   TYR A CZ  
363 O  OH  . TYR A 48 ? 0.0791 0.0842 0.0724 0.0096  -0.0017 0.0129  48   TYR A OH  
364 N  N   . THR A 49 ? 0.0498 0.0550 0.0398 0.0048  0.0017  0.0071  49   THR A N   
365 C  CA  . THR A 49 ? 0.0573 0.0483 0.0434 0.0043  -0.0065 -0.0027 49   THR A CA  
366 C  C   . THR A 49 ? 0.0686 0.0536 0.0370 0.0017  -0.0035 -0.0084 49   THR A C   
367 O  O   . THR A 49 ? 0.0478 0.0421 0.0604 0.0039  -0.0104 -0.0038 49   THR A O   
368 C  CB  . THR A 49 ? 0.0611 0.0502 0.0603 0.0090  -0.0080 -0.0064 49   THR A CB  
369 O  OG1 . THR A 49 ? 0.0561 0.0513 0.0838 0.0056  0.0003  0.0003  49   THR A OG1 
370 C  CG2 . THR A 49 ? 0.0619 0.0795 0.0583 0.0029  0.0114  -0.0179 49   THR A CG2 
371 N  N   . THR A 50 ? 0.0701 0.0508 0.0492 0.0015  -0.0135 -0.0066 50   THR A N   
372 C  CA  . THR A 50 ? 0.0668 0.0561 0.0677 0.0017  -0.0199 -0.0087 50   THR A CA  
373 C  C   . THR A 50 ? 0.0823 0.0481 0.0622 -0.0055 -0.0103 -0.0021 50   THR A C   
374 O  O   . THR A 50 ? 0.0850 0.0854 0.1064 -0.0193 -0.0063 -0.0276 50   THR A O   
375 C  CB  . THR A 50 ? 0.1029 0.0849 0.0595 -0.0162 -0.0248 -0.0126 50   THR A CB  
376 O  OG1 . THR A 50 ? 0.1220 0.1083 0.0903 0.0139  -0.0484 0.0017  50   THR A OG1 
377 C  CG2 . THR A 50 ? 0.1176 0.1296 0.0674 0.0007  -0.0214 -0.0279 50   THR A CG2 
378 N  N   . LEU A 51 ? 0.0617 0.0558 0.0717 0.0024  -0.0158 -0.0070 51   LEU A N   
379 C  CA  . LEU A 51 ? 0.0514 0.0576 0.0723 0.0028  -0.0240 -0.0015 51   LEU A CA  
380 C  C   . LEU A 51 ? 0.0559 0.0611 0.0659 -0.0039 -0.0155 -0.0076 51   LEU A C   
381 O  O   . LEU A 51 ? 0.0604 0.0691 0.0727 -0.0006 -0.0190 0.0102  51   LEU A O   
382 C  CB  . LEU A 51 ? 0.0684 0.0603 0.0790 0.0082  -0.0121 -0.0053 51   LEU A CB  
383 C  CG  . LEU A 51 ? 0.0501 0.0579 0.0794 0.0100  -0.0146 0.0022  51   LEU A CG  
384 C  CD1 . LEU A 51 ? 0.1228 0.0633 0.0997 0.0002  0.0114  -0.0040 51   LEU A CD1 
385 C  CD2 . LEU A 51 ? 0.0782 0.0975 0.0936 -0.0248 -0.0235 0.0342  51   LEU A CD2 
386 N  N   . PRO A 52 ? 0.0598 0.0686 0.0785 -0.0070 -0.0157 0.0011  52   PRO A N   
387 C  CA  . PRO A 52 ? 0.0687 0.0627 0.0887 -0.0095 -0.0092 0.0092  52   PRO A CA  
388 C  C   . PRO A 52 ? 0.0693 0.0567 0.0740 0.0004  -0.0017 0.0045  52   PRO A C   
389 O  O   . PRO A 52 ? 0.0712 0.0598 0.0721 -0.0001 0.0045  0.0045  52   PRO A O   
390 C  CB  . PRO A 52 ? 0.0723 0.1647 0.1330 -0.0450 -0.0195 0.0574  52   PRO A CB  
391 C  CG  . PRO A 52 ? 0.0689 0.1131 0.1754 -0.0024 -0.0060 0.0756  52   PRO A CG  
392 C  CD  . PRO A 52 ? 0.0638 0.0664 0.1009 -0.0049 -0.0148 0.0048  52   PRO A CD  
393 N  N   . TYR A 53 ? 0.0979 0.0537 0.0694 -0.0029 -0.0016 0.0032  53   TYR A N   
394 C  CA  . TYR A 53 ? 0.0833 0.0645 0.0641 0.0064  0.0024  -0.0008 53   TYR A CA  
395 C  C   . TYR A 53 ? 0.0798 0.0564 0.0667 0.0011  0.0017  0.0073  53   TYR A C   
396 O  O   . TYR A 53 ? 0.0819 0.0631 0.0743 0.0021  -0.0010 0.0030  53   TYR A O   
397 C  CB  . TYR A 53 ? 0.0918 0.0467 0.0721 0.0015  0.0068  -0.0001 53   TYR A CB  
398 C  CG  . TYR A 53 ? 0.0751 0.0740 0.0640 0.0052  0.0055  0.0114  53   TYR A CG  
399 C  CD1 . TYR A 53 ? 0.0878 0.0928 0.0751 -0.0143 0.0168  -0.0101 53   TYR A CD1 
400 C  CD2 . TYR A 53 ? 0.0870 0.1254 0.0693 -0.0097 0.0106  0.0108  53   TYR A CD2 
401 C  CE1 . TYR A 53 ? 0.0906 0.1011 0.0789 -0.0278 0.0114  -0.0051 53   TYR A CE1 
402 C  CE2 . TYR A 53 ? 0.0887 0.1004 0.0656 0.0117  0.0130  0.0094  53   TYR A CE2 
403 C  CZ  . TYR A 53 ? 0.0994 0.1023 0.0629 0.0004  0.0038  0.0139  53   TYR A CZ  
404 O  OH  . TYR A 53 ? 0.1177 0.1384 0.0766 -0.0279 0.0020  0.0024  53   TYR A OH  
405 N  N   . ASP A 54 ? 0.0742 0.0700 0.0712 0.0045  -0.0021 0.0064  54   ASP A N   
406 C  CA  . ASP A 54 ? 0.0861 0.0800 0.0808 -0.0049 0.0196  0.0061  54   ASP A CA  
407 C  C   . ASP A 54 ? 0.0730 0.0740 0.0824 0.0040  -0.0052 -0.0029 54   ASP A C   
408 O  O   . ASP A 54 ? 0.0919 0.0807 0.0888 0.0017  0.0065  -0.0074 54   ASP A O   
409 C  CB  . ASP A 54 ? 0.0881 0.1008 0.1091 -0.0112 0.0282  0.0115  54   ASP A CB  
410 C  CG  . ASP A 54 ? 0.1063 0.1535 0.1405 0.0042  -0.0066 -0.0316 54   ASP A CG  
411 O  OD1 . ASP A 54 ? 0.1406 0.1494 0.1452 0.0114  -0.0047 -0.0275 54   ASP A OD1 
412 O  OD2 . ASP A 54 ? 0.1867 0.2408 0.1648 0.0929  -0.0284 -0.0297 54   ASP A OD2 
413 N  N   . PHE A 55 ? 0.0748 0.0518 0.0847 0.0118  0.0044  -0.0078 55   PHE A N   
414 C  CA  . PHE A 55 ? 0.0650 0.0538 0.0869 0.0145  -0.0037 -0.0070 55   PHE A CA  
415 C  C   . PHE A 55 ? 0.0751 0.0547 0.0560 0.0127  -0.0127 -0.0020 55   PHE A C   
416 O  O   . PHE A 55 ? 0.0645 0.0602 0.0769 0.0105  -0.0067 -0.0095 55   PHE A O   
417 C  CB  . PHE A 55 ? 0.0724 0.0597 0.0914 -0.0016 -0.0128 -0.0070 55   PHE A CB  
418 C  CG  . PHE A 55 ? 0.0554 0.0634 0.0843 -0.0008 -0.0216 -0.0170 55   PHE A CG  
419 C  CD1 . PHE A 55 ? 0.0591 0.0627 0.1040 0.0018  -0.0234 -0.0140 55   PHE A CD1 
420 C  CD2 . PHE A 55 ? 0.0722 0.0593 0.1032 -0.0090 -0.0118 -0.0122 55   PHE A CD2 
421 C  CE1 . PHE A 55 ? 0.0739 0.0736 0.1261 0.0124  -0.0249 -0.0070 55   PHE A CE1 
422 C  CE2 . PHE A 55 ? 0.1178 0.0923 0.1040 0.0137  -0.0010 0.0058  55   PHE A CE2 
423 C  CZ  . PHE A 55 ? 0.0863 0.0865 0.1158 -0.0019 -0.0337 0.0108  55   PHE A CZ  
424 N  N   . ILE A 56 ? 0.0631 0.0636 0.0693 0.0014  0.0013  -0.0146 56   ILE A N   
425 C  CA  . ILE A 56 ? 0.0732 0.0448 0.0546 0.0084  -0.0040 0.0032  56   ILE A CA  
426 C  C   . ILE A 56 ? 0.0655 0.0573 0.0599 0.0052  0.0001  -0.0030 56   ILE A C   
427 O  O   . ILE A 56 ? 0.0717 0.0495 0.0677 0.0075  0.0032  -0.0072 56   ILE A O   
428 C  CB  . ILE A 56 ? 0.0624 0.0651 0.0578 -0.0026 0.0154  0.0028  56   ILE A CB  
429 C  CG1 . ILE A 56 ? 0.0697 0.0462 0.0552 0.0025  0.0044  -0.0022 56   ILE A CG1 
430 C  CG2 . ILE A 56 ? 0.0619 0.0920 0.0534 0.0101  -0.0041 -0.0108 56   ILE A CG2 
431 C  CD1 . ILE A 56 ? 0.0903 0.0608 0.0592 -0.0080 -0.0005 0.0001  56   ILE A CD1 
432 N  N   . LEU A 57 ? 0.0763 0.0551 0.0570 -0.0071 0.0078  -0.0099 57   LEU A N   
433 C  CA  . LEU A 57 ? 0.0691 0.0668 0.0588 0.0040  0.0113  -0.0078 57   LEU A CA  
434 C  C   . LEU A 57 ? 0.0837 0.0640 0.0633 0.0096  0.0025  -0.0071 57   LEU A C   
435 O  O   . LEU A 57 ? 0.0930 0.0605 0.0625 0.0107  0.0055  -0.0094 57   LEU A O   
436 C  CB  . LEU A 57 ? 0.0655 0.0615 0.0643 -0.0018 0.0055  -0.0057 57   LEU A CB  
437 C  CG  . LEU A 57 ? 0.0867 0.0770 0.0589 0.0039  0.0111  -0.0076 57   LEU A CG  
438 C  CD1 . LEU A 57 ? 0.0929 0.1235 0.0608 0.0082  -0.0019 -0.0254 57   LEU A CD1 
439 C  CD2 . LEU A 57 ? 0.1732 0.1041 0.0713 -0.0097 0.0128  0.0145  57   LEU A CD2 
440 N  N   . GLU A 58 ? 0.0760 0.0653 0.0658 0.0013  0.0078  -0.0075 58   GLU A N   
441 C  CA  . GLU A 58 ? 0.0764 0.0990 0.0979 0.0152  0.0176  -0.0060 58   GLU A CA  
442 C  C   . GLU A 58 ? 0.0769 0.0860 0.0729 0.0345  -0.0049 -0.0017 58   GLU A C   
443 O  O   . GLU A 58 ? 0.1015 0.1002 0.0825 0.0141  0.0064  -0.0238 58   GLU A O   
444 C  CB  . GLU A 58 ? 0.0721 0.1319 0.2674 0.0208  0.0051  -0.0341 58   GLU A CB  
445 C  CG  . GLU A 58 ? 0.2523 0.2641 0.4859 -0.1541 0.0399  0.0235  58   GLU A CG  
446 C  CD  . GLU A 58 ? 0.3357 0.4027 0.5236 -0.2382 -0.0140 0.0214  58   GLU A CD  
447 O  OE1 . GLU A 58 ? 0.1808 0.6321 0.5573 0.0833  0.0384  -0.2540 58   GLU A OE1 
448 O  OE2 . GLU A 58 ? 0.2515 0.5911 0.5539 -0.2329 -0.0474 0.0670  58   GLU A OE2 
449 N  N   . LYS A 59 ? 0.0945 0.0688 0.0704 0.0289  -0.0121 -0.0079 59   LYS A N   
450 C  CA  . LYS A 59 ? 0.1076 0.0654 0.0594 0.0327  -0.0018 -0.0127 59   LYS A CA  
451 C  C   . LYS A 59 ? 0.0967 0.0739 0.0642 0.0174  0.0137  -0.0064 59   LYS A C   
452 O  O   . LYS A 59 ? 0.1096 0.0674 0.0800 0.0158  0.0057  0.0016  59   LYS A O   
453 C  CB  . LYS A 59 ? 0.1449 0.1089 0.0604 0.0384  -0.0025 -0.0148 59   LYS A CB  
454 C  CG  . LYS A 59 ? 0.1585 0.0878 0.0697 0.0533  -0.0232 -0.0113 59   LYS A CG  
455 C  CD  . LYS A 59 ? 0.1696 0.1116 0.0977 0.0720  -0.0242 -0.0124 59   LYS A CD  
456 C  CE  . LYS A 59 ? 0.1321 0.1434 0.0948 0.0537  -0.0083 -0.0107 59   LYS A CE  
457 N  NZ  . LYS A 59 ? 0.1149 0.1180 0.1410 0.0295  -0.0419 -0.0050 59   LYS A NZ  
458 N  N   . ILE A 60 ? 0.0844 0.0696 0.0642 0.0057  0.0118  -0.0036 60   ILE A N   
459 C  CA  . ILE A 60 ? 0.0990 0.0662 0.0618 -0.0025 0.0117  -0.0007 60   ILE A CA  
460 C  C   . ILE A 60 ? 0.1072 0.0693 0.0677 -0.0039 0.0091  -0.0096 60   ILE A C   
461 O  O   . ILE A 60 ? 0.0979 0.0792 0.0830 -0.0095 0.0080  -0.0144 60   ILE A O   
462 C  CB  . ILE A 60 ? 0.0825 0.0671 0.0703 -0.0129 0.0072  -0.0061 60   ILE A CB  
463 C  CG1 . ILE A 60 ? 0.0808 0.0948 0.0680 -0.0113 0.0198  -0.0012 60   ILE A CG1 
464 C  CG2 . ILE A 60 ? 0.1062 0.1562 0.0658 -0.0294 -0.0023 -0.0108 60   ILE A CG2 
465 C  CD1 . ILE A 60 ? 0.0830 0.0989 0.1187 -0.0074 0.0194  -0.0070 60   ILE A CD1 
466 N  N   . LYS A 61 ? 0.0910 0.0749 0.0723 0.0018  0.0141  -0.0128 61   LYS A N   
467 C  CA  . LYS A 61 ? 0.0843 0.0845 0.0748 -0.0032 0.0070  -0.0217 61   LYS A CA  
468 C  C   . LYS A 61 ? 0.0943 0.0803 0.0689 -0.0034 0.0167  -0.0162 61   LYS A C   
469 O  O   . LYS A 61 ? 0.1496 0.0766 0.0696 -0.0023 0.0204  -0.0208 61   LYS A O   
470 C  CB  . LYS A 61 ? 0.0811 0.0891 0.0921 0.0054  0.0212  -0.0123 61   LYS A CB  
471 C  CG  . LYS A 61 ? 0.1123 0.1030 0.1002 0.0212  0.0253  0.0033  61   LYS A CG  
472 C  CD  . LYS A 61 ? 0.1307 0.1246 0.1316 -0.0016 0.0215  0.0202  61   LYS A CD  
473 C  CE  . LYS A 61 ? 0.1829 0.1876 0.1203 -0.0318 0.0426  0.0193  61   LYS A CE  
474 N  NZ  . LYS A 61 ? 0.2462 0.2002 0.1270 -0.0495 0.0111  0.0152  61   LYS A NZ  
475 N  N   . LYS A 62 ? 0.0980 0.1005 0.0760 0.0165  0.0116  -0.0239 62   LYS A N   
476 C  CA  . LYS A 62 ? 0.1273 0.0987 0.1057 0.0221  0.0038  -0.0179 62   LYS A CA  
477 C  C   . LYS A 62 ? 0.1367 0.0926 0.1090 0.0279  -0.0176 -0.0176 62   LYS A C   
478 O  O   . LYS A 62 ? 0.1669 0.0849 0.1728 0.0330  -0.0375 -0.0166 62   LYS A O   
479 C  CB  . LYS A 62 ? 0.1126 0.1121 0.1444 0.0388  -0.0130 -0.0273 62   LYS A CB  
480 C  CG  . LYS A 62 ? 0.0987 0.1727 0.2438 0.0302  0.0118  -0.0457 62   LYS A CG  
481 C  CD  . LYS A 62 ? 0.2518 0.3485 0.2842 0.0091  0.1286  -0.0095 62   LYS A CD  
482 C  CE  . LYS A 62 ? 0.5744 0.4321 0.2265 0.0284  0.0489  0.0272  62   LYS A CE  
483 N  NZ  . LYS A 62 ? 0.5528 0.7104 0.2937 0.2119  0.0187  -0.0283 62   LYS A NZ  
484 N  N   . THR A 63 ? 0.1356 0.0959 0.0709 0.0065  0.0107  -0.0137 63   THR A N   
485 C  CA  . THR A 63 ? 0.1559 0.0764 0.0657 0.0081  0.0029  0.0103  63   THR A CA  
486 C  C   . THR A 63 ? 0.1319 0.0882 0.0760 0.0176  0.0089  -0.0128 63   THR A C   
487 O  O   . THR A 63 ? 0.1581 0.0990 0.0933 -0.0010 0.0271  -0.0183 63   THR A O   
488 C  CB  . THR A 63 ? 0.1553 0.0815 0.0672 -0.0076 0.0291  -0.0060 63   THR A CB  
489 O  OG1 . THR A 63 ? 0.1062 0.1071 0.0823 -0.0198 0.0150  0.0001  63   THR A OG1 
490 C  CG2 . THR A 63 ? 0.1968 0.1224 0.0606 -0.0184 0.0387  0.0018  63   THR A CG2 
491 N  N   . GLY A 64 ? 0.1332 0.0879 0.0685 0.0094  0.0145  -0.0199 64   GLY A N   
492 C  CA  . GLY A 64 ? 0.1194 0.0715 0.0674 0.0071  0.0141  -0.0184 64   GLY A CA  
493 C  C   . GLY A 64 ? 0.1169 0.0704 0.0614 0.0083  0.0267  -0.0061 64   GLY A C   
494 O  O   . GLY A 64 ? 0.1494 0.0959 0.0620 -0.0034 0.0104  -0.0085 64   GLY A O   
495 N  N   . LYS A 65 ? 0.1087 0.0916 0.0836 0.0063  0.0198  0.0214  65   LYS A N   
496 C  CA  . LYS A 65 ? 0.1114 0.0786 0.0856 0.0086  0.0088  -0.0068 65   LYS A CA  
497 C  C   . LYS A 65 ? 0.1339 0.0603 0.0952 0.0178  0.0057  -0.0135 65   LYS A C   
498 O  O   . LYS A 65 ? 0.1847 0.0810 0.1367 -0.0129 -0.0519 0.0149  65   LYS A O   
499 C  CB  . LYS A 65 ? 0.1206 0.1545 0.0945 0.0240  0.0217  0.0088  65   LYS A CB  
500 C  CG  . LYS A 65 ? 0.1007 0.1676 0.1136 -0.0114 0.0328  0.0148  65   LYS A CG  
501 C  CD  . LYS A 65 ? 0.1942 0.1862 0.1251 -0.1046 -0.0036 0.0138  65   LYS A CD  
502 C  CE  . LYS A 65 ? 0.1810 0.1662 0.1412 -0.0556 0.0017  0.0086  65   LYS A CE  
503 N  NZ  . LYS A 65 ? 0.3082 0.1873 0.1883 -0.0838 -0.0417 -0.0361 65   LYS A NZ  
504 N  N   . GLU A 66 ? 0.1061 0.0653 0.0907 0.0086  0.0204  -0.0096 66   GLU A N   
505 C  CA  . GLU A 66 ? 0.1089 0.0853 0.0812 0.0012  0.0285  -0.0091 66   GLU A CA  
506 C  C   . GLU A 66 ? 0.0746 0.0658 0.0622 0.0006  0.0091  0.0134  66   GLU A C   
507 O  O   . GLU A 66 ? 0.0721 0.0748 0.0943 -0.0098 0.0045  -0.0113 66   GLU A O   
508 C  CB  . GLU A 66 ? 0.1081 0.0816 0.0801 0.0200  0.0305  -0.0171 66   GLU A CB  
509 C  CG  . GLU A 66 ? 0.1761 0.1039 0.1086 0.0081  0.0500  0.0131  66   GLU A CG  
510 C  CD  . GLU A 66 ? 0.2544 0.1962 0.0796 0.0171  0.0647  0.0192  66   GLU A CD  
511 O  OE1 . GLU A 66 ? 0.4210 0.2137 0.0873 0.0156  -0.0010 -0.0315 66   GLU A OE1 
512 O  OE2 . GLU A 66 ? 0.4208 0.2003 0.1300 0.0994  0.0607  0.0523  66   GLU A OE2 
513 N  N   . VAL A 67 ? 0.0698 0.0755 0.0899 -0.0071 0.0298  -0.0055 67   VAL A N   
514 C  CA  . VAL A 67 ? 0.0700 0.0757 0.0674 0.0024  0.0163  0.0002  67   VAL A CA  
515 C  C   . VAL A 67 ? 0.0966 0.0697 0.0630 -0.0227 0.0241  -0.0023 67   VAL A C   
516 O  O   . VAL A 67 ? 0.1006 0.1339 0.1110 -0.0320 0.0402  0.0132  67   VAL A O   
517 C  CB  . VAL A 67 ? 0.0780 0.0817 0.0865 -0.0202 0.0083  0.0040  67   VAL A CB  
518 C  CG1 . VAL A 67 ? 0.1100 0.0918 0.0971 -0.0136 -0.0128 -0.0209 67   VAL A CG1 
519 C  CG2 . VAL A 67 ? 0.1060 0.1302 0.0825 0.0077  -0.0011 0.0181  67   VAL A CG2 
520 N  N   . ARG A 68 ? 0.1007 0.0699 0.0577 -0.0010 0.0242  0.0082  68   ARG A N   
521 C  CA  . ARG A 68 ? 0.1525 0.0640 0.0491 -0.0123 0.0279  0.0097  68   ARG A CA  
522 C  C   . ARG A 68 ? 0.1711 0.0706 0.0460 -0.0110 0.0129  0.0023  68   ARG A C   
523 O  O   . ARG A 68 ? 0.2879 0.0652 0.0760 -0.0368 0.0702  -0.0029 68   ARG A O   
524 C  CB  . ARG A 68 ? 0.2196 0.0998 0.0786 -0.0419 -0.0485 0.0331  68   ARG A CB  
525 C  CG  . ARG A 68 ? 0.2565 0.1412 0.1232 -0.0717 -0.0334 -0.0176 68   ARG A CG  
526 C  CD  . ARG A 68 ? 0.2886 0.3143 0.1181 0.0428  -0.0881 -0.0799 68   ARG A CD  
527 N  NE  . ARG A 68 ? 0.1876 0.4036 0.1187 -0.0032 -0.0216 0.0044  68   ARG A NE  
528 C  CZ  . ARG A 68 ? 0.2007 0.4223 0.1415 -0.0469 -0.0335 0.0822  68   ARG A CZ  
529 N  NH1 . ARG A 68 ? 0.1397 0.3514 0.1425 0.0208  -0.0032 0.0291  68   ARG A NH1 
530 N  NH2 . ARG A 68 ? 0.2792 0.4760 0.1870 -0.0634 -0.0293 0.1465  68   ARG A NH2 
531 N  N   . SER A 69 ? 0.1091 0.0685 0.0488 -0.0117 0.0087  -0.0017 69   SER A N   
532 C  CA  . SER A 69 ? 0.1560 0.0691 0.0583 -0.0204 0.0179  -0.0040 69   SER A CA  
533 C  C   . SER A 69 ? 0.0931 0.0598 0.0630 -0.0053 0.0182  -0.0035 69   SER A C   
534 O  O   . SER A 69 ? 0.0908 0.0675 0.0619 -0.0128 0.0168  -0.0035 69   SER A O   
535 C  CB  . SER A 69 ? 0.2766 0.0755 0.0682 0.0271  -0.0118 0.0016  69   SER A CB  
536 O  OG  . SER A 69 ? 0.1924 0.0996 0.2083 0.0074  -0.1030 -0.0010 69   SER A OG  
537 N  N   . GLY A 70 ? 0.1162 0.0725 0.0518 -0.0214 0.0281  -0.0040 70   GLY A N   
538 C  CA  . GLY A 70 ? 0.1360 0.0737 0.0509 -0.0023 0.0218  -0.0065 70   GLY A CA  
539 C  C   . GLY A 70 ? 0.1046 0.0723 0.0628 -0.0248 0.0137  -0.0101 70   GLY A C   
540 O  O   . GLY A 70 ? 0.1351 0.0824 0.0592 -0.0258 0.0273  -0.0031 70   GLY A O   
541 N  N   . LYS A 71 ? 0.0940 0.0635 0.0635 -0.0096 0.0148  -0.0049 71   LYS A N   
542 C  CA  . LYS A 71 ? 0.1539 0.0615 0.0561 -0.0220 0.0035  -0.0034 71   LYS A CA  
543 C  C   . LYS A 71 ? 0.0889 0.0541 0.0611 -0.0148 0.0050  0.0048  71   LYS A C   
544 O  O   . LYS A 71 ? 0.1115 0.0546 0.0554 -0.0163 0.0097  -0.0009 71   LYS A O   
545 C  CB  . LYS A 71 ? 0.2209 0.0950 0.0639 0.0295  -0.0085 0.0037  71   LYS A CB  
546 C  CG  . LYS A 71 ? 0.1928 0.2011 0.1169 0.0654  -0.0244 -0.0183 71   LYS A CG  
547 C  CD  . LYS A 71 ? 0.2855 0.4573 0.2774 0.0838  -0.1224 0.0881  71   LYS A CD  
548 C  CE  . LYS A 71 ? 0.5346 0.5535 0.3817 0.0150  -0.1822 0.2874  71   LYS A CE  
549 N  NZ  . LYS A 71 ? 0.6669 0.8995 0.2144 -0.1201 -0.0522 0.2540  71   LYS A NZ  
550 N  N   . GLN A 72 ? 0.1401 0.0637 0.0579 -0.0205 0.0154  -0.0063 72   GLN A N   
551 C  CA  . GLN A 72 ? 0.1394 0.0538 0.0508 -0.0150 0.0164  0.0044  72   GLN A CA  
552 C  C   . GLN A 72 ? 0.1380 0.0662 0.0562 -0.0114 0.0036  0.0066  72   GLN A C   
553 O  O   . GLN A 72 ? 0.2096 0.0767 0.0979 0.0170  0.0243  0.0427  72   GLN A O   
554 C  CB  . GLN A 72 ? 0.1407 0.0624 0.1046 -0.0043 0.0010  -0.0213 72   GLN A CB  
555 C  CG  . GLN A 72 ? 0.2296 0.1378 0.0973 -0.0940 -0.0096 -0.0062 72   GLN A CG  
556 C  CD  . GLN A 72 ? 0.2142 0.2093 0.1080 -0.0840 -0.0310 0.0312  72   GLN A CD  
557 O  OE1 . GLN A 72 ? 0.2333 0.3203 0.1739 -0.1360 -0.0103 0.0755  72   GLN A OE1 
558 N  NE2 . GLN A 72 ? 0.1717 0.2812 0.1182 -0.0162 -0.0670 -0.0054 72   GLN A NE2 
559 N  N   . LEU A 73 ? 0.1315 0.0700 0.0625 0.0100  0.0020  0.0186  73   LEU A N   
560 C  CA  . LEU A 73 ? 0.1314 0.0631 0.0845 0.0104  -0.0050 0.0131  73   LEU A CA  
561 C  C   . LEU A 73 ? 0.1325 0.0870 0.0941 0.0203  -0.0184 -0.0112 73   LEU A C   
562 O  O   . LEU A 73 ? 0.1497 0.1482 0.1285 0.0114  -0.0475 -0.0222 73   LEU A O   
563 C  CB  . LEU A 73 ? 0.1387 0.0880 0.0726 -0.0011 -0.0271 0.0188  73   LEU A CB  
564 C  CG  . LEU A 73 ? 0.1715 0.1358 0.0928 -0.0018 -0.0311 -0.0126 73   LEU A CG  
565 C  CD1 . LEU A 73 ? 0.3072 0.6275 0.4091 0.2135  -0.0527 -0.3333 73   LEU A CD1 
566 C  CD2 . LEU A 73 ? 0.2993 0.1398 0.1723 -0.0857 -0.0240 -0.0516 73   LEU A CD2 
567 O  OXT . LEU A 73 ? 0.1783 0.0966 0.0971 0.0519  -0.0234 -0.0088 73   LEU A OXT 
568 HG HG  . HG  B .  ? 0.1577 0.1132 0.1320 0.0005  -0.0120 -0.0260 74   HG  A HG  
569 C  C1  . BEN C .  ? 0.0813 0.0498 0.0574 -0.0009 -0.0069 0.0117  186  BEN A C1  
570 C  C2  . BEN C .  ? 0.0899 0.0595 0.0588 -0.0045 -0.0207 0.0097  186  BEN A C2  
571 C  C3  . BEN C .  ? 0.0957 0.0769 0.0524 -0.0016 -0.0165 0.0126  186  BEN A C3  
572 C  C4  . BEN C .  ? 0.0933 0.0874 0.0672 0.0071  -0.0207 0.0054  186  BEN A C4  
573 C  C5  . BEN C .  ? 0.0860 0.0655 0.0745 0.0018  0.0003  0.0179  186  BEN A C5  
574 C  C6  . BEN C .  ? 0.0830 0.0599 0.0789 -0.0026 -0.0092 0.0006  186  BEN A C6  
575 C  C   . BEN C .  ? 0.0899 0.0493 0.0700 -0.0026 -0.0067 -0.0037 186  BEN A C   
576 N  N1  . BEN C .  ? 0.1213 0.0829 0.0611 -0.0176 -0.0186 0.0069  186  BEN A N1  
577 N  N2  . BEN C .  ? 0.0925 0.0831 0.0899 0.0019  -0.0001 -0.0193 186  BEN A N2  
578 C  C1  . BEN D .  ? 0.2212 0.1428 0.1546 -0.0784 -0.0551 0.0418  187  BEN A C1  
579 C  C2  . BEN D .  ? 0.2080 0.1994 0.1595 -0.0402 -0.0697 0.0423  187  BEN A C2  
580 C  C3  . BEN D .  ? 0.2237 0.1750 0.1150 0.0267  -0.0132 0.0159  187  BEN A C3  
581 C  C4  . BEN D .  ? 0.1769 0.1845 0.1150 0.0141  -0.0370 0.0113  187  BEN A C4  
582 C  C5  . BEN D .  ? 0.1462 0.1280 0.1042 -0.0335 -0.0575 0.0031  187  BEN A C5  
583 C  C6  . BEN D .  ? 0.1846 0.1682 0.1732 -0.0707 -0.0538 0.0342  187  BEN A C6  
584 C  C   . BEN D .  ? 0.4745 0.1664 0.2013 -0.0517 0.0982  0.0523  187  BEN A C   
585 N  N1  . BEN D .  ? 0.5527 0.1978 0.1589 -0.0757 0.1200  0.0052  187  BEN A N1  
586 N  N2  . BEN D .  ? 0.7488 0.1359 0.2385 0.0393  0.1779  0.0447  187  BEN A N2  
587 O  O   . HOH E .  ? 0.1006 0.1006 0.1006 0.0000  0.0000  0.0000  1001 HOH A O   
588 O  O   . HOH E .  ? 0.0714 0.0714 0.0714 0.0000  0.0000  0.0000  1002 HOH A O   
589 O  O   . HOH E .  ? 0.1088 0.1088 0.1088 0.0000  0.0000  0.0000  1003 HOH A O   
590 O  O   . HOH E .  ? 0.1440 0.1440 0.1440 0.0000  0.0000  0.0000  1004 HOH A O   
591 O  O   . HOH E .  ? 0.1169 0.1169 0.1169 0.0000  0.0000  0.0000  1005 HOH A O   
592 O  O   . HOH E .  ? 0.1199 0.1199 0.1199 0.0000  0.0000  0.0000  1006 HOH A O   
593 O  O   . HOH E .  ? 0.1246 0.1246 0.1246 0.0000  0.0000  0.0000  1007 HOH A O   
594 O  O   . HOH E .  ? 0.1085 0.1085 0.1085 0.0000  0.0000  0.0000  1008 HOH A O   
595 O  O   . HOH E .  ? 0.1191 0.1191 0.1191 0.0000  0.0000  0.0000  1009 HOH A O   
596 O  O   . HOH E .  ? 0.1135 0.1135 0.1135 0.0000  0.0000  0.0000  1010 HOH A O   
597 O  O   . HOH E .  ? 0.1417 0.1417 0.1417 0.0000  0.0000  0.0000  1011 HOH A O   
598 O  O   . HOH E .  ? 0.1031 0.1031 0.1031 0.0000  0.0000  0.0000  1012 HOH A O   
599 O  O   . HOH E .  ? 0.1630 0.1630 0.1630 0.0000  0.0000  0.0000  1013 HOH A O   
600 O  O   . HOH E .  ? 0.1589 0.1589 0.1589 0.0000  0.0000  0.0000  1014 HOH A O   
601 O  O   . HOH E .  ? 0.1686 0.1686 0.1686 0.0000  0.0000  0.0000  1015 HOH A O   
602 O  O   . HOH E .  ? 0.1617 0.1617 0.1617 0.0000  0.0000  0.0000  1016 HOH A O   
603 O  O   . HOH E .  ? 0.1873 0.1873 0.1873 0.0000  0.0000  0.0000  1017 HOH A O   
604 O  O   . HOH E .  ? 0.2173 0.2173 0.2173 0.0000  0.0000  0.0000  1018 HOH A O   
605 O  O   . HOH E .  ? 0.1887 0.1887 0.1887 0.0000  0.0000  0.0000  1019 HOH A O   
606 O  O   . HOH E .  ? 0.1892 0.1892 0.1892 0.0000  0.0000  0.0000  1020 HOH A O   
607 O  O   . HOH E .  ? 0.1839 0.1839 0.1839 0.0000  0.0000  0.0000  1021 HOH A O   
608 O  O   . HOH E .  ? 0.2016 0.2016 0.2016 0.0000  0.0000  0.0000  1022 HOH A O   
609 O  O   . HOH E .  ? 0.1907 0.1907 0.1907 0.0000  0.0000  0.0000  1023 HOH A O   
610 O  O   . HOH E .  ? 0.1981 0.1981 0.1981 0.0000  0.0000  0.0000  1024 HOH A O   
611 O  O   . HOH E .  ? 0.1582 0.1582 0.1582 0.0000  0.0000  0.0000  1025 HOH A O   
612 O  O   . HOH E .  ? 0.1844 0.1844 0.1844 0.0000  0.0000  0.0000  1026 HOH A O   
613 O  O   . HOH E .  ? 0.2870 0.2870 0.2870 0.0000  0.0000  0.0000  1027 HOH A O   
614 O  O   . HOH E .  ? 0.2057 0.2057 0.2057 0.0000  0.0000  0.0000  1028 HOH A O   
615 O  O   . HOH E .  ? 0.2061 0.2061 0.2061 0.0000  0.0000  0.0000  1029 HOH A O   
616 O  O   . HOH E .  ? 0.2452 0.2452 0.2452 0.0000  0.0000  0.0000  1030 HOH A O   
617 O  O   . HOH E .  ? 0.1735 0.1735 0.1735 0.0000  0.0000  0.0000  1031 HOH A O   
618 O  O   . HOH E .  ? 0.2975 0.2975 0.2975 0.0000  0.0000  0.0000  1032 HOH A O   
619 O  O   . HOH E .  ? 0.2391 0.2391 0.2391 0.0000  0.0000  0.0000  1033 HOH A O   
620 O  O   . HOH E .  ? 0.2138 0.2138 0.2138 0.0000  0.0000  0.0000  1034 HOH A O   
621 O  O   . HOH E .  ? 0.1717 0.1717 0.1717 0.0000  0.0000  0.0000  1035 HOH A O   
622 O  O   . HOH E .  ? 0.2062 0.2062 0.2062 0.0000  0.0000  0.0000  1036 HOH A O   
623 O  O   . HOH E .  ? 0.2413 0.2413 0.2413 0.0000  0.0000  0.0000  1037 HOH A O   
624 O  O   . HOH E .  ? 0.2182 0.2182 0.2182 0.0000  0.0000  0.0000  1038 HOH A O   
625 O  O   . HOH E .  ? 0.2422 0.2422 0.2422 0.0000  0.0000  0.0000  1039 HOH A O   
626 O  O   . HOH E .  ? 0.3067 0.3067 0.3067 0.0000  0.0000  0.0000  1040 HOH A O   
627 O  O   . HOH E .  ? 0.2604 0.2604 0.2604 0.0000  0.0000  0.0000  1041 HOH A O   
628 O  O   . HOH E .  ? 0.2576 0.2576 0.2576 0.0000  0.0000  0.0000  1042 HOH A O   
629 O  O   . HOH E .  ? 0.2650 0.2650 0.2650 0.0000  0.0000  0.0000  1043 HOH A O   
630 O  O   . HOH E .  ? 0.2061 0.2061 0.2061 0.0000  0.0000  0.0000  1044 HOH A O   
631 O  O   . HOH E .  ? 0.3358 0.3358 0.3358 0.0000  0.0000  0.0000  1045 HOH A O   
632 O  O   . HOH E .  ? 0.2580 0.2580 0.2580 0.0000  0.0000  0.0000  1046 HOH A O   
633 O  O   . HOH E .  ? 0.4286 0.4286 0.4286 0.0000  0.0000  0.0000  1047 HOH A O   
634 O  O   . HOH E .  ? 0.1943 0.1943 0.1943 0.0000  0.0000  0.0000  1048 HOH A O   
635 O  O   . HOH E .  ? 0.2532 0.2532 0.2532 0.0000  0.0000  0.0000  1049 HOH A O   
636 O  O   . HOH E .  ? 0.3086 0.3086 0.3086 0.0000  0.0000  0.0000  1050 HOH A O   
637 O  O   . HOH E .  ? 0.4938 0.4938 0.4938 0.0000  0.0000  0.0000  1051 HOH A O   
638 O  O   . HOH E .  ? 0.4359 0.4359 0.4359 0.0000  0.0000  0.0000  1052 HOH A O   
639 O  O   . HOH E .  ? 0.2164 0.2164 0.2164 0.0000  0.0000  0.0000  1053 HOH A O   
640 O  O   . HOH E .  ? 0.3453 0.3453 0.3453 0.0000  0.0000  0.0000  1054 HOH A O   
641 O  O   . HOH E .  ? 0.3655 0.3655 0.3655 0.0000  0.0000  0.0000  1055 HOH A O   
642 O  O   . HOH E .  ? 0.4090 0.4090 0.4090 0.0000  0.0000  0.0000  1056 HOH A O   
643 O  O   . HOH E .  ? 0.3212 0.3212 0.3212 0.0000  0.0000  0.0000  1057 HOH A O   
644 O  O   . HOH E .  ? 0.4088 0.4088 0.4088 0.0000  0.0000  0.0000  1058 HOH A O   
645 O  O   . HOH E .  ? 0.3981 0.3981 0.3981 0.0000  0.0000  0.0000  1059 HOH A O   
646 O  O   . HOH E .  ? 0.4780 0.4780 0.4780 0.0000  0.0000  0.0000  1060 HOH A O   
647 O  O   . HOH E .  ? 0.2409 0.2409 0.2409 0.0000  0.0000  0.0000  1061 HOH A O   
648 O  O   . HOH E .  ? 0.3390 0.3390 0.3390 0.0000  0.0000  0.0000  1062 HOH A O   
649 O  O   . HOH E .  ? 0.3959 0.3959 0.3959 0.0000  0.0000  0.0000  1063 HOH A O   
650 O  O   . HOH E .  ? 0.2449 0.2449 0.2449 0.0000  0.0000  0.0000  1064 HOH A O   
651 O  O   . HOH E .  ? 0.3494 0.3494 0.3494 0.0000  0.0000  0.0000  1065 HOH A O   
652 O  O   . HOH E .  ? 0.2644 0.2644 0.2644 0.0000  0.0000  0.0000  1066 HOH A O   
653 O  O   . HOH E .  ? 0.3423 0.3423 0.3423 0.0000  0.0000  0.0000  1067 HOH A O   
654 O  O   . HOH E .  ? 0.4368 0.4368 0.4368 0.0000  0.0000  0.0000  1068 HOH A O   
655 O  O   . HOH E .  ? 0.2557 0.2557 0.2557 0.0000  0.0000  0.0000  1069 HOH A O   
656 O  O   . HOH E .  ? 0.3907 0.3907 0.3907 0.0000  0.0000  0.0000  1070 HOH A O   
657 O  O   . HOH E .  ? 0.3584 0.3584 0.3584 0.0000  0.0000  0.0000  1071 HOH A O   
658 O  O   . HOH E .  ? 0.2831 0.2831 0.2831 0.0000  0.0000  0.0000  1072 HOH A O   
659 O  O   . HOH E .  ? 0.3008 0.3008 0.3008 0.0000  0.0000  0.0000  1073 HOH A O   
660 O  O   . HOH E .  ? 0.4458 0.4458 0.4458 0.0000  0.0000  0.0000  1074 HOH A O   
661 O  O   . HOH E .  ? 0.3273 0.3273 0.3273 0.0000  0.0000  0.0000  1075 HOH A O   
662 O  O   . HOH E .  ? 0.3764 0.3764 0.3764 0.0000  0.0000  0.0000  1076 HOH A O   
663 O  O   . HOH E .  ? 0.5048 0.5048 0.5048 0.0000  0.0000  0.0000  1077 HOH A O   
664 O  O   . HOH E .  ? 0.6220 0.6220 0.6220 0.0000  0.0000  0.0000  1078 HOH A O   
665 O  O   . HOH E .  ? 0.3741 0.3741 0.3741 0.0000  0.0000  0.0000  1079 HOH A O   
666 O  O   . HOH E .  ? 0.5442 0.5442 0.5442 0.0000  0.0000  0.0000  1080 HOH A O   
667 O  O   . HOH E .  ? 0.3916 0.3916 0.3916 0.0000  0.0000  0.0000  1081 HOH A O   
668 O  O   . HOH E .  ? 0.4437 0.4437 0.4437 0.0000  0.0000  0.0000  1082 HOH A O   
669 O  O   . HOH E .  ? 0.4382 0.4382 0.4382 0.0000  0.0000  0.0000  1083 HOH A O   
670 O  O   . HOH E .  ? 0.3758 0.3758 0.3758 0.0000  0.0000  0.0000  1084 HOH A O   
671 O  O   . HOH E .  ? 0.4825 0.4825 0.4825 0.0000  0.0000  0.0000  1085 HOH A O   
672 O  O   . HOH E .  ? 0.4007 0.4007 0.4007 0.0000  0.0000  0.0000  1086 HOH A O   
673 O  O   . HOH E .  ? 0.5661 0.5661 0.5661 0.0000  0.0000  0.0000  1087 HOH A O   
674 O  O   . HOH E .  ? 0.3903 0.3903 0.3903 0.0000  0.0000  0.0000  1088 HOH A O   
675 O  O   . HOH E .  ? 0.3602 0.3602 0.3602 0.0000  0.0000  0.0000  1089 HOH A O   
676 O  O   . HOH E .  ? 0.4413 0.4413 0.4413 0.0000  0.0000  0.0000  1090 HOH A O   
677 O  O   . HOH E .  ? 0.4966 0.4966 0.4966 0.0000  0.0000  0.0000  1091 HOH A O   
678 O  O   . HOH E .  ? 0.4416 0.4416 0.4416 0.0000  0.0000  0.0000  1092 HOH A O   
679 O  O   . HOH E .  ? 0.8144 0.8144 0.8144 0.0000  0.0000  0.0000  1093 HOH A O   
680 O  O   . HOH E .  ? 0.2618 0.2618 0.2618 0.0000  0.0000  0.0000  1094 HOH A O   
681 O  O   . HOH E .  ? 0.3727 0.3727 0.3727 0.0000  0.0000  0.0000  1095 HOH A O   
682 O  O   . HOH E .  ? 0.6067 0.6067 0.6067 0.0000  0.0000  0.0000  1096 HOH A O   
683 O  O   . HOH E .  ? 0.3366 0.3366 0.3366 0.0000  0.0000  0.0000  1097 HOH A O   
684 O  O   . HOH E .  ? 0.4034 0.4034 0.4034 0.0000  0.0000  0.0000  1098 HOH A O   
685 O  O   . HOH E .  ? 0.5870 0.5870 0.5870 0.0000  0.0000  0.0000  1099 HOH A O   
686 O  O   . HOH E .  ? 0.6310 0.6310 0.6310 0.0000  0.0000  0.0000  1100 HOH A O   
687 O  O   . HOH E .  ? 0.5077 0.5077 0.5077 0.0000  0.0000  0.0000  1101 HOH A O   
688 O  O   . HOH E .  ? 0.4773 0.4773 0.4773 0.0000  0.0000  0.0000  1102 HOH A O   
689 O  O   . HOH E .  ? 0.4250 0.4250 0.4250 0.0000  0.0000  0.0000  1103 HOH A O   
690 O  O   . HOH E .  ? 0.3621 0.3621 0.3621 0.0000  0.0000  0.0000  1104 HOH A O   
691 O  O   . HOH E .  ? 0.6462 0.6462 0.6462 0.0000  0.0000  0.0000  1105 HOH A O   
692 O  O   . HOH E .  ? 0.4112 0.4112 0.4112 0.0000  0.0000  0.0000  1106 HOH A O   
693 O  O   . HOH E .  ? 0.4534 0.4534 0.4534 0.0000  0.0000  0.0000  1107 HOH A O   
694 O  O   . HOH E .  ? 0.4914 0.4914 0.4914 0.0000  0.0000  0.0000  1108 HOH A O   
695 O  O   . HOH E .  ? 0.4506 0.4506 0.4506 0.0000  0.0000  0.0000  1109 HOH A O   
696 O  O   . HOH E .  ? 0.3920 0.3920 0.3920 0.0000  0.0000  0.0000  1110 HOH A O   
697 O  O   . HOH E .  ? 0.6789 0.6789 0.6789 0.0000  0.0000  0.0000  1111 HOH A O   
698 O  O   . HOH E .  ? 0.5089 0.5089 0.5089 0.0000  0.0000  0.0000  1112 HOH A O   
699 O  O   . HOH E .  ? 0.3097 0.3097 0.3097 0.0000  0.0000  0.0000  1113 HOH A O   
700 O  O   . HOH E .  ? 0.4388 0.4388 0.4388 0.0000  0.0000  0.0000  1114 HOH A O   
701 O  O   . HOH E .  ? 0.6293 0.6293 0.6293 0.0000  0.0000  0.0000  1115 HOH A O   
702 O  O   . HOH E .  ? 0.4381 0.4381 0.4381 0.0000  0.0000  0.0000  1116 HOH A O   
703 O  O   . HOH E .  ? 0.5765 0.5765 0.5765 0.0000  0.0000  0.0000  1117 HOH A O   
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1  MET 1  1  ?  ?   ?   A . n 
A 1 2  ALA 2  2  2  ALA ALA A . n 
A 1 3  GLU 3  3  3  GLU GLU A . n 
A 1 4  ILE 4  4  4  ILE ILE A . n 
A 1 5  LYS 5  5  5  LYS LYS A . n 
A 1 6  HIS 6  6  6  HIS HIS A . n 
A 1 7  TYR 7  7  7  TYR TYR A . n 
A 1 8  GLN 8  8  8  GLN GLN A . n 
A 1 9  PHE 9  9  9  PHE PHE A . n 
A 1 10 ASN 10 10 10 ASN ASN A . n 
A 1 11 VAL 11 11 11 VAL VAL A . n 
A 1 12 VAL 12 12 12 VAL VAL A . n 
A 1 13 MET 13 13 13 MET MET A . n 
A 1 14 THR 14 14 14 THR THR A . n 
A 1 15 CYS 15 15 15 CYS CYS A . n 
A 1 16 SER 16 16 16 SER SER A . n 
A 1 17 GLY 17 17 17 GLY GLY A . n 
A 1 18 CYS 18 18 18 CYS CYS A . n 
A 1 19 SER 19 19 19 SER SER A . n 
A 1 20 GLY 20 20 20 GLY GLY A . n 
A 1 21 ALA 21 21 21 ALA ALA A . n 
A 1 22 VAL 22 22 22 VAL VAL A . n 
A 1 23 ASN 23 23 23 ASN ASN A . n 
A 1 24 LYS 24 24 24 LYS LYS A . n 
A 1 25 VAL 25 25 25 VAL VAL A . n 
A 1 26 LEU 26 26 26 LEU LEU A . n 
A 1 27 THR 27 27 27 THR THR A . n 
A 1 28 LYS 28 28 28 LYS LYS A . n 
A 1 29 LEU 29 29 29 LEU LEU A . n 
A 1 30 GLU 30 30 30 GLU GLU A . n 
A 1 31 PRO 31 31 31 PRO PRO A . n 
A 1 32 ASP 32 32 32 ASP ASP A . n 
A 1 33 VAL 33 33 33 VAL VAL A . n 
A 1 34 SER 34 34 34 SER SER A . n 
A 1 35 LYS 35 35 35 LYS LYS A . n 
A 1 36 ILE 36 36 36 ILE ILE A . n 
A 1 37 ASP 37 37 37 ASP ASP A . n 
A 1 38 ILE 38 38 38 ILE ILE A . n 
A 1 39 SER 39 39 39 SER SER A . n 
A 1 40 LEU 40 40 40 LEU LEU A . n 
A 1 41 GLU 41 41 41 GLU GLU A . n 
A 1 42 LYS 42 42 42 LYS LYS A . n 
A 1 43 GLN 43 43 43 GLN GLN A . n 
A 1 44 LEU 44 44 44 LEU LEU A . n 
A 1 45 VAL 45 45 45 VAL VAL A . n 
A 1 46 ASP 46 46 46 ASP ASP A . n 
A 1 47 VAL 47 47 47 VAL VAL A . n 
A 1 48 TYR 48 48 48 TYR TYR A . n 
A 1 49 THR 49 49 49 THR THR A . n 
A 1 50 THR 50 50 50 THR THR A . n 
A 1 51 LEU 51 51 51 LEU LEU A . n 
A 1 52 PRO 52 52 52 PRO PRO A . n 
A 1 53 TYR 53 53 53 TYR TYR A . n 
A 1 54 ASP 54 54 54 ASP ASP A . n 
A 1 55 PHE 55 55 55 PHE PHE A . n 
A 1 56 ILE 56 56 56 ILE ILE A . n 
A 1 57 LEU 57 57 57 LEU LEU A . n 
A 1 58 GLU 58 58 58 GLU GLU A . n 
A 1 59 LYS 59 59 59 LYS LYS A . n 
A 1 60 ILE 60 60 60 ILE ILE A . n 
A 1 61 LYS 61 61 61 LYS LYS A . n 
A 1 62 LYS 62 62 62 LYS LYS A . n 
A 1 63 THR 63 63 63 THR THR A . n 
A 1 64 GLY 64 64 64 GLY GLY A . n 
A 1 65 LYS 65 65 65 LYS LYS A . n 
A 1 66 GLU 66 66 66 GLU GLU A . n 
A 1 67 VAL 67 67 67 VAL VAL A . n 
A 1 68 ARG 68 68 68 ARG ARG A . n 
A 1 69 SER 69 69 69 SER SER A . n 
A 1 70 GLY 70 70 70 GLY GLY A . n 
A 1 71 LYS 71 71 71 LYS LYS A . n 
A 1 72 GLN 72 72 72 GLN GLN A . n 
A 1 73 LEU 73 73 73 LEU LEU A . 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 
B 2 HG  1   74   74   HG  HG  A . 
C 3 BEN 1   186  186  BEN BEN A . 
D 3 BEN 1   187  187  BEN BEN A . 
E 4 HOH 1   1001 1001 HOH HOH A . 
E 4 HOH 2   1002 1002 HOH HOH A . 
E 4 HOH 3   1003 1003 HOH HOH A . 
E 4 HOH 4   1004 1004 HOH HOH A . 
E 4 HOH 5   1005 1005 HOH HOH A . 
E 4 HOH 6   1006 1006 HOH HOH A . 
E 4 HOH 7   1007 1007 HOH HOH A . 
E 4 HOH 8   1008 1008 HOH HOH A . 
E 4 HOH 9   1009 1009 HOH HOH A . 
E 4 HOH 10  1010 1010 HOH HOH A . 
E 4 HOH 11  1011 1011 HOH HOH A . 
E 4 HOH 12  1012 1012 HOH HOH A . 
E 4 HOH 13  1013 1013 HOH HOH A . 
E 4 HOH 14  1014 1014 HOH HOH A . 
E 4 HOH 15  1015 1015 HOH HOH A . 
E 4 HOH 16  1016 1016 HOH HOH A . 
E 4 HOH 17  1017 1017 HOH HOH A . 
E 4 HOH 18  1018 1018 HOH HOH A . 
E 4 HOH 19  1019 1019 HOH HOH A . 
E 4 HOH 20  1020 1020 HOH HOH A . 
E 4 HOH 21  1021 1021 HOH HOH A . 
E 4 HOH 22  1022 1022 HOH HOH A . 
E 4 HOH 23  1023 1023 HOH HOH A . 
E 4 HOH 24  1024 1024 HOH HOH A . 
E 4 HOH 25  1025 1025 HOH HOH A . 
E 4 HOH 26  1026 1026 HOH HOH A . 
E 4 HOH 27  1027 1027 HOH HOH A . 
E 4 HOH 28  1028 1028 HOH HOH A . 
E 4 HOH 29  1029 1029 HOH HOH A . 
E 4 HOH 30  1030 1030 HOH HOH A . 
E 4 HOH 31  1031 1031 HOH HOH A . 
E 4 HOH 32  1032 1032 HOH HOH A . 
E 4 HOH 33  1033 1033 HOH HOH A . 
E 4 HOH 34  1034 1034 HOH HOH A . 
E 4 HOH 35  1035 1035 HOH HOH A . 
E 4 HOH 36  1036 1036 HOH HOH A . 
E 4 HOH 37  1037 1037 HOH HOH A . 
E 4 HOH 38  1038 1038 HOH HOH A . 
E 4 HOH 39  1039 1039 HOH HOH A . 
E 4 HOH 40  1040 1040 HOH HOH A . 
E 4 HOH 41  1041 1041 HOH HOH A . 
E 4 HOH 42  1042 1042 HOH HOH A . 
E 4 HOH 43  1043 1043 HOH HOH A . 
E 4 HOH 44  1044 1044 HOH HOH A . 
E 4 HOH 45  1045 1045 HOH HOH A . 
E 4 HOH 46  1046 1046 HOH HOH A . 
E 4 HOH 47  1047 1047 HOH HOH A . 
E 4 HOH 48  1048 1048 HOH HOH A . 
E 4 HOH 49  1049 1049 HOH HOH A . 
E 4 HOH 50  1050 1050 HOH HOH A . 
E 4 HOH 51  1051 1051 HOH HOH A . 
E 4 HOH 52  1052 1052 HOH HOH A . 
E 4 HOH 53  1053 1053 HOH HOH A . 
E 4 HOH 54  1054 1054 HOH HOH A . 
E 4 HOH 55  1055 1055 HOH HOH A . 
E 4 HOH 56  1056 1056 HOH HOH A . 
E 4 HOH 57  1057 1057 HOH HOH A . 
E 4 HOH 58  1058 1058 HOH HOH A . 
E 4 HOH 59  1059 1059 HOH HOH A . 
E 4 HOH 60  1060 1060 HOH HOH A . 
E 4 HOH 61  1061 1061 HOH HOH A . 
E 4 HOH 62  1062 1062 HOH HOH A . 
E 4 HOH 63  1063 1063 HOH HOH A . 
E 4 HOH 64  1064 1064 HOH HOH A . 
E 4 HOH 65  1065 1065 HOH HOH A . 
E 4 HOH 66  1066 1066 HOH HOH A . 
E 4 HOH 67  1067 1067 HOH HOH A . 
E 4 HOH 68  1068 1068 HOH HOH A . 
E 4 HOH 69  1069 1069 HOH HOH A . 
E 4 HOH 70  1070 1070 HOH HOH A . 
E 4 HOH 71  1071 1071 HOH HOH A . 
E 4 HOH 72  1072 1072 HOH HOH A . 
E 4 HOH 73  1073 1073 HOH HOH A . 
E 4 HOH 74  1074 1074 HOH HOH A . 
E 4 HOH 75  1075 1075 HOH HOH A . 
E 4 HOH 76  1076 1076 HOH HOH A . 
E 4 HOH 77  1077 1077 HOH HOH A . 
E 4 HOH 78  1078 1078 HOH HOH A . 
E 4 HOH 79  1079 1079 HOH HOH A . 
E 4 HOH 80  1080 1080 HOH HOH A . 
E 4 HOH 81  1081 1081 HOH HOH A . 
E 4 HOH 82  1082 1082 HOH HOH A . 
E 4 HOH 83  1083 1083 HOH HOH A . 
E 4 HOH 84  1084 1084 HOH HOH A . 
E 4 HOH 85  1085 1085 HOH HOH A . 
E 4 HOH 86  1086 1086 HOH HOH A . 
E 4 HOH 87  1087 1087 HOH HOH A . 
E 4 HOH 88  1088 1088 HOH HOH A . 
E 4 HOH 89  1089 1089 HOH HOH A . 
E 4 HOH 90  1090 1090 HOH HOH A . 
E 4 HOH 91  1091 1091 HOH HOH A . 
E 4 HOH 92  1092 1092 HOH HOH A . 
E 4 HOH 93  1093 1093 HOH HOH A . 
E 4 HOH 94  1094 1094 HOH HOH A . 
E 4 HOH 95  1095 1095 HOH HOH A . 
E 4 HOH 96  1096 1096 HOH HOH A . 
E 4 HOH 97  1097 1097 HOH HOH A . 
E 4 HOH 98  1098 1098 HOH HOH A . 
E 4 HOH 99  1099 1099 HOH HOH A . 
E 4 HOH 100 1100 1100 HOH HOH A . 
E 4 HOH 101 1101 1101 HOH HOH A . 
E 4 HOH 102 1102 1102 HOH HOH A . 
E 4 HOH 103 1103 1103 HOH HOH A . 
E 4 HOH 104 1104 1104 HOH HOH A . 
E 4 HOH 105 1105 1105 HOH HOH A . 
E 4 HOH 106 1106 1106 HOH HOH A . 
E 4 HOH 107 1107 1107 HOH HOH A . 
E 4 HOH 108 1108 1108 HOH HOH A . 
E 4 HOH 109 1109 1109 HOH HOH A . 
E 4 HOH 110 1110 1110 HOH HOH A . 
E 4 HOH 111 1111 1111 HOH HOH A . 
E 4 HOH 112 1112 1112 HOH HOH A . 
E 4 HOH 113 1113 1113 HOH HOH A . 
E 4 HOH 114 1114 1114 HOH HOH A . 
E 4 HOH 115 1115 1115 HOH HOH A . 
E 4 HOH 116 1116 1116 HOH HOH A . 
E 4 HOH 117 1117 1117 HOH HOH A . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OG1 ? A THR 14 ? A THR 14 ? 1_555 HG ? B HG . ? A HG 74 ? 1_555 SG ? A CYS 15 ? A CYS 15   ? 1_555 102.3 ? 
2  OG1 ? A THR 14 ? A THR 14 ? 1_555 HG ? B HG . ? A HG 74 ? 1_555 N  ? A CYS 15 ? A CYS 15   ? 1_555 61.9  ? 
3  SG  ? A CYS 15 ? A CYS 15 ? 1_555 HG ? B HG . ? A HG 74 ? 1_555 N  ? A CYS 15 ? A CYS 15   ? 1_555 74.8  ? 
4  OG1 ? A THR 14 ? A THR 14 ? 1_555 HG ? B HG . ? A HG 74 ? 1_555 O  ? A CYS 15 ? A CYS 15   ? 1_555 106.0 ? 
5  SG  ? A CYS 15 ? A CYS 15 ? 1_555 HG ? B HG . ? A HG 74 ? 1_555 O  ? A CYS 15 ? A CYS 15   ? 1_555 75.3  ? 
6  N   ? A CYS 15 ? A CYS 15 ? 1_555 HG ? B HG . ? A HG 74 ? 1_555 O  ? A CYS 15 ? A CYS 15   ? 1_555 45.8  ? 
7  OG1 ? A THR 14 ? A THR 14 ? 1_555 HG ? B HG . ? A HG 74 ? 1_555 SG ? A CYS 18 ? A CYS 18   ? 1_555 83.6  ? 
8  SG  ? A CYS 15 ? A CYS 15 ? 1_555 HG ? B HG . ? A HG 74 ? 1_555 SG ? A CYS 18 ? A CYS 18   ? 1_555 167.3 ? 
9  N   ? A CYS 15 ? A CYS 15 ? 1_555 HG ? B HG . ? A HG 74 ? 1_555 SG ? A CYS 18 ? A CYS 18   ? 1_555 98.8  ? 
10 O   ? A CYS 15 ? A CYS 15 ? 1_555 HG ? B HG . ? A HG 74 ? 1_555 SG ? A CYS 18 ? A CYS 18   ? 1_555 92.3  ? 
11 OG1 ? A THR 14 ? A THR 14 ? 1_555 HG ? B HG . ? A HG 74 ? 1_555 N  ? A CYS 18 ? A CYS 18   ? 1_555 146.1 ? 
12 SG  ? A CYS 15 ? A CYS 15 ? 1_555 HG ? B HG . ? A HG 74 ? 1_555 N  ? A CYS 18 ? A CYS 18   ? 1_555 97.6  ? 
13 N   ? A CYS 15 ? A CYS 15 ? 1_555 HG ? B HG . ? A HG 74 ? 1_555 N  ? A CYS 18 ? A CYS 18   ? 1_555 98.2  ? 
14 O   ? A CYS 15 ? A CYS 15 ? 1_555 HG ? B HG . ? A HG 74 ? 1_555 N  ? A CYS 18 ? A CYS 18   ? 1_555 53.4  ? 
15 SG  ? A CYS 18 ? A CYS 18 ? 1_555 HG ? B HG . ? A HG 74 ? 1_555 N  ? A CYS 18 ? A CYS 18   ? 1_555 72.2  ? 
16 OG1 ? A THR 14 ? A THR 14 ? 1_555 HG ? B HG . ? A HG 74 ? 1_555 O  ? E HOH .  ? A HOH 1018 ? 1_545 136.7 ? 
17 SG  ? A CYS 15 ? A CYS 15 ? 1_555 HG ? B HG . ? A HG 74 ? 1_555 O  ? E HOH .  ? A HOH 1018 ? 1_545 84.9  ? 
18 N   ? A CYS 15 ? A CYS 15 ? 1_555 HG ? B HG . ? A HG 74 ? 1_555 O  ? E HOH .  ? A HOH 1018 ? 1_545 156.0 ? 
19 O   ? A CYS 15 ? A CYS 15 ? 1_555 HG ? B HG . ? A HG 74 ? 1_555 O  ? E HOH .  ? A HOH 1018 ? 1_545 117.1 ? 
20 SG  ? A CYS 18 ? A CYS 18 ? 1_555 HG ? B HG . ? A HG 74 ? 1_555 O  ? E HOH .  ? A HOH 1018 ? 1_545 98.6  ? 
21 N   ? A CYS 18 ? A CYS 18 ? 1_555 HG ? B HG . ? A HG 74 ? 1_555 O  ? E HOH .  ? A HOH 1018 ? 1_545 71.7  ? 
# 
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 1999-12-12 
2 'Structure model' 1 1 2008-04-26 
3 'Structure model' 1 2 2011-07-13 
4 'Structure model' 1 3 2017-10-04 
# 
_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         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' 'Version format compliance' 
3 4 'Structure model' 'Refinement description'    
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    4 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            software 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
SHAKE     'model building' . ? 1 
SnB       phasing          . ? 2 
SHELXL-97 refinement       . ? 3 
DENZO     'data reduction' . ? 4 
SCALEPACK 'data scaling'   . ? 5 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 O  A GLY 64 ? ? C  A GLY 64 ? ? N   A LYS 65 ? ? 111.90 122.70 -10.80 1.60 Y 
2 1 CD A ARG 68 ? ? NE A ARG 68 ? ? CZ  A ARG 68 ? ? 133.64 123.60 10.04  1.40 N 
3 1 NE A ARG 68 ? ? CZ A ARG 68 ? ? NH1 A ARG 68 ? ? 123.90 120.30 3.60   0.50 N 
# 
_pdbx_unobs_or_zero_occ_residues.id               1 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num    1 
_pdbx_unobs_or_zero_occ_residues.polymer_flag     Y 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag   1 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id     A 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id     MET 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id      1 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code     ? 
_pdbx_unobs_or_zero_occ_residues.label_asym_id    A 
_pdbx_unobs_or_zero_occ_residues.label_comp_id    MET 
_pdbx_unobs_or_zero_occ_residues.label_seq_id     1 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'MERCURY (II) ION' HG  
3 BENZAMIDINE        BEN 
4 water              HOH 
# 



If you find results from this site helpful for your research, please cite one of our papers:

elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.