data_4BMW
# 
_entry.id   4BMW 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.383 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   4BMW         pdb_00004bmw 10.2210/pdb4bmw/pdb 
PDBE  EBI-56818    ?            ?                   
WWPDB D_1290056818 ?            ?                   
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        4BMW 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.recvd_initial_deposition_date   2013-05-11 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Wagener, S.'              1 ? 
'Kursula, I.'              2 ? 
'Wedderhoff, I.'           3 ? 
'Groves, M.R.'             4 ? 
'Ortiz de Orue Lucana, D.' 5 ? 
# 
_citation.id                        primary 
_citation.title                     
'Iron Binding at Specific Sites within the Octameric Hbps Protects Streptomycetes from Iron-Mediated Oxidative Stress.' 
_citation.journal_abbrev            'Plos One' 
_citation.journal_volume            8 
_citation.page_first                71579 
_citation.page_last                 ? 
_citation.year                      2013 
_citation.journal_id_ASTM           ? 
_citation.country                   US 
_citation.journal_id_ISSN           1932-6203 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   24013686 
_citation.pdbx_database_id_DOI      10.1371/JOURNAL.PONE.0071579 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Wedderhoff, I.'           1 ? 
primary 'Kursula, I.'              2 ? 
primary 'Groves, M.R.'             3 ? 
primary 'Ortiz de Orue Lucana, D.' 4 ? 
# 
_cell.entry_id           4BMW 
_cell.length_a           77.390 
_cell.length_b           77.390 
_cell.length_c           79.860 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              16 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         4BMW 
_symmetry.space_group_name_H-M             'I 4 2 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                97 
# 
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 'EXTRACELLULAR HAEM-BINDING PROTEIN' 15486.170 1   ? YES ? ? 
2 water   nat water                                18.015    111 ? ?   ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        HBPS 
# 
_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       
;GAMADTTEATPAAAPVAARGGELTQSTHLTLEAATKAARAAVEAAEKDGRHVSVAVVDRNGNTLVTLRGDGAGPQSYDSA
DRKAFTAVSWNAPTSELAKRLAQAPTLKDIPGTLFLAGGTPVTAKGAPVAGIGVAGAPSGDLDEQYARAGAAVLGH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GAMADTTEATPAAAPVAARGGELTQSTHLTLEAATKAARAAVEAAEKDGRHVSVAVVDRNGNTLVTLRGDGAGPQSYDSA
DRKAFTAVSWNAPTSELAKRLAQAPTLKDIPGTLFLAGGTPVTAKGAPVAGIGVAGAPSGDLDEQYARAGAAVLGH
;
_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   GLY n 
1 2   ALA n 
1 3   MET n 
1 4   ALA n 
1 5   ASP n 
1 6   THR n 
1 7   THR n 
1 8   GLU n 
1 9   ALA n 
1 10  THR n 
1 11  PRO n 
1 12  ALA n 
1 13  ALA n 
1 14  ALA n 
1 15  PRO n 
1 16  VAL n 
1 17  ALA n 
1 18  ALA n 
1 19  ARG n 
1 20  GLY n 
1 21  GLY n 
1 22  GLU n 
1 23  LEU n 
1 24  THR n 
1 25  GLN n 
1 26  SER n 
1 27  THR n 
1 28  HIS n 
1 29  LEU n 
1 30  THR n 
1 31  LEU n 
1 32  GLU n 
1 33  ALA n 
1 34  ALA n 
1 35  THR n 
1 36  LYS n 
1 37  ALA n 
1 38  ALA n 
1 39  ARG n 
1 40  ALA n 
1 41  ALA n 
1 42  VAL n 
1 43  GLU n 
1 44  ALA n 
1 45  ALA n 
1 46  GLU n 
1 47  LYS n 
1 48  ASP n 
1 49  GLY n 
1 50  ARG n 
1 51  HIS n 
1 52  VAL n 
1 53  SER n 
1 54  VAL n 
1 55  ALA n 
1 56  VAL n 
1 57  VAL n 
1 58  ASP n 
1 59  ARG n 
1 60  ASN n 
1 61  GLY n 
1 62  ASN n 
1 63  THR n 
1 64  LEU n 
1 65  VAL n 
1 66  THR n 
1 67  LEU n 
1 68  ARG n 
1 69  GLY n 
1 70  ASP n 
1 71  GLY n 
1 72  ALA n 
1 73  GLY n 
1 74  PRO n 
1 75  GLN n 
1 76  SER n 
1 77  TYR n 
1 78  ASP n 
1 79  SER n 
1 80  ALA n 
1 81  ASP n 
1 82  ARG n 
1 83  LYS n 
1 84  ALA n 
1 85  PHE n 
1 86  THR n 
1 87  ALA n 
1 88  VAL n 
1 89  SER n 
1 90  TRP n 
1 91  ASN n 
1 92  ALA n 
1 93  PRO n 
1 94  THR n 
1 95  SER n 
1 96  GLU n 
1 97  LEU n 
1 98  ALA n 
1 99  LYS n 
1 100 ARG n 
1 101 LEU n 
1 102 ALA n 
1 103 GLN n 
1 104 ALA n 
1 105 PRO n 
1 106 THR n 
1 107 LEU n 
1 108 LYS n 
1 109 ASP n 
1 110 ILE n 
1 111 PRO n 
1 112 GLY n 
1 113 THR n 
1 114 LEU n 
1 115 PHE n 
1 116 LEU n 
1 117 ALA n 
1 118 GLY n 
1 119 GLY n 
1 120 THR n 
1 121 PRO n 
1 122 VAL n 
1 123 THR n 
1 124 ALA n 
1 125 LYS n 
1 126 GLY n 
1 127 ALA n 
1 128 PRO n 
1 129 VAL n 
1 130 ALA n 
1 131 GLY n 
1 132 ILE n 
1 133 GLY n 
1 134 VAL n 
1 135 ALA n 
1 136 GLY n 
1 137 ALA n 
1 138 PRO n 
1 139 SER n 
1 140 GLY n 
1 141 ASP n 
1 142 LEU n 
1 143 ASP n 
1 144 GLU n 
1 145 GLN n 
1 146 TYR n 
1 147 ALA n 
1 148 ARG n 
1 149 ALA n 
1 150 GLY n 
1 151 ALA n 
1 152 ALA n 
1 153 VAL n 
1 154 LEU n 
1 155 GLY n 
1 156 HIS 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               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'STREPTOMYCES RETICULI' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1926 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'ESCHERICHIA COLI BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              PLYSS 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q9RIM2_STRRE 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           ? 
_struct_ref.pdbx_db_accession          Q9RIM2 
_struct_ref.pdbx_db_isoform            ? 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              4BMW 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 4 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 156 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q9RIM2 
_struct_ref_seq.db_align_beg                  36 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  188 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       4 
_struct_ref_seq.pdbx_auth_seq_align_end       156 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 4BMW GLY A 1  ? UNP Q9RIM2 ?   ?   'expression tag'      1  1 
1 4BMW ALA A 2  ? UNP Q9RIM2 ?   ?   'expression tag'      2  2 
1 4BMW MET A 3  ? UNP Q9RIM2 ?   ?   'expression tag'      3  3 
1 4BMW ASP A 78 ? UNP Q9RIM2 GLU 110 'engineered mutation' 78 4 
1 4BMW ASP A 81 ? UNP Q9RIM2 GLU 113 'engineered mutation' 81 5 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
_exptl.entry_id          4BMW 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.1 
_exptl_crystal.density_percent_sol   42 
_exptl_crystal.description           NONE 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          ? 
_exptl_crystal_grow.temp            ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              8.3 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    '20% (W/V) POLYETHYLENE GLYCOL 3350 AND 0.2 M TRI-POTASSIUM CITRATE, pH 8.3' 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS 6M' 
_diffrn_detector.pdbx_collection_date   2013-05-02 
_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   1.00 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
_diffrn_source.pdbx_synchrotron_beamline   'P13 (MX1)' 
_diffrn_source.pdbx_wavelength             1.00 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.entry_id                     4BMW 
_reflns.observed_criterion_sigma_I   -3.0 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             50.00 
_reflns.d_resolution_high            1.99 
_reflns.number_obs                   8579 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.5 
_reflns.pdbx_Rmerge_I_obs            0.10 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        11.00 
_reflns.B_iso_Wilson_estimate        29.68 
_reflns.pdbx_redundancy              5.6 
# 
_reflns_shell.pdbx_diffrn_id         1 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.d_res_high             1.99 
_reflns_shell.d_res_low              2.04 
_reflns_shell.percent_possible_all   99.7 
_reflns_shell.Rmerge_I_obs           0.87 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    1.84 
_reflns_shell.pdbx_redundancy        5.9 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 4BMW 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     8576 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          2.01 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             54.723 
_refine.ls_d_res_high                            1.990 
_refine.ls_percent_reflns_obs                    99.47 
_refine.ls_R_factor_obs                          0.1849 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1824 
_refine.ls_R_factor_R_free                       0.2344 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_number_reflns_R_free                  429 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               43 
_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                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      'PDB ENTRY 3FPV' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.22 
_refine.pdbx_overall_phase_error                 27.47 
_refine.overall_SU_B                             ? 
_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_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1024 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.number_atoms_solvent             111 
_refine_hist.number_atoms_total               1135 
_refine_hist.d_res_high                       1.990 
_refine_hist.d_res_low                        54.723 
# 
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 
f_bond_d           0.004  ? ? 1080 'X-RAY DIFFRACTION' ? 
f_angle_d          0.827  ? ? 1478 'X-RAY DIFFRACTION' ? 
f_dihedral_angle_d 13.770 ? ? 386  'X-RAY DIFFRACTION' ? 
f_chiral_restr     0.047  ? ? 171  'X-RAY DIFFRACTION' ? 
f_plane_restr      0.003  ? ? 202  'X-RAY DIFFRACTION' ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.R_factor_all 
'X-RAY DIFFRACTION' . 1.9900 2.2780  2651 0.2691 100.00 0.3334 . . 137 . . 
'X-RAY DIFFRACTION' . 2.2780 2.8700  2699 0.2175 100.00 0.2404 . . 141 . . 
'X-RAY DIFFRACTION' . 2.8700 54.7437 2797 0.1493 99.00  0.2054 . . 151 . . 
# 
_struct.entry_id                  4BMW 
_struct.title                     'Crystal structure of the Streptomyces reticuli HbpS E78D, E81D double mutant' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4BMW 
_struct_keywords.pdbx_keywords   'METAL BINDING PROTEIN' 
_struct_keywords.text            'METAL BINDING PROTEIN, OXIDATIVE STRESS, IRON BINDING, HEME' 
# 
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 ? 
# 
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 ARG A 19  ? LEU A 23  ? ARG A 19  LEU A 23  5 ? 5  
HELX_P HELX_P2 2 THR A 30  ? ASP A 48  ? THR A 30  ASP A 48  1 ? 19 
HELX_P HELX_P3 3 GLN A 75  ? ASN A 91  ? GLN A 75  ASN A 91  1 ? 17 
HELX_P HELX_P4 4 PRO A 93  ? ALA A 98  ? PRO A 93  ALA A 98  1 ? 6  
HELX_P HELX_P5 5 LYS A 99  ? GLN A 103 ? LYS A 99  GLN A 103 5 ? 5  
HELX_P HELX_P6 6 ALA A 104 ? ILE A 110 ? ALA A 104 ILE A 110 5 ? 7  
HELX_P HELX_P7 7 SER A 139 ? VAL A 153 ? SER A 139 VAL A 153 1 ? 15 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 ALA 13  A . ? ALA 13  A ALA 14  A ? ALA 14  A 1 4.40  
2 GLY 155 A . ? GLY 155 A HIS 156 A ? HIS 156 A 1 -0.72 
# 
_struct_sheet.id               AA 
_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 
AA 1 2 ? anti-parallel 
AA 2 3 ? anti-parallel 
AA 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 
AA 1 THR A 63  ? ARG A 68  ? THR A 63  ARG A 68  
AA 2 SER A 53  ? ASP A 58  ? SER A 53  ASP A 58  
AA 3 ALA A 127 ? ALA A 135 ? ALA A 127 ALA A 135 
AA 4 GLY A 119 ? ALA A 124 ? GLY A 119 ALA A 124 
# 
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 
AA 1 2 N LEU A 67  ? N LEU A 67  O VAL A 54  ? O VAL A 54  
AA 2 3 N VAL A 57  ? N VAL A 57  O GLY A 131 ? O GLY A 131 
AA 3 4 N ILE A 132 ? N ILE A 132 O THR A 120 ? O THR A 120 
# 
_database_PDB_matrix.entry_id          4BMW 
_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                    4BMW 
_atom_sites.fract_transf_matrix[1][1]   0.012922 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.012922 
_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]   0.012522 
_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 
H 
N 
O 
# 
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    A PRO A 1 11  ? 162.601 -21.151 -10.077 0.46 80.73  ? 11   PRO A N    1 
ATOM   2    C CA   A PRO A 1 11  ? 162.639 -22.443 -9.385  0.46 82.09  ? 11   PRO A CA   1 
ATOM   3    C C    A PRO A 1 11  ? 162.919 -23.598 -10.332 0.46 78.79  ? 11   PRO A C    1 
ATOM   4    O O    A PRO A 1 11  ? 163.140 -24.720 -9.876  0.46 80.73  ? 11   PRO A O    1 
ATOM   5    C CB   A PRO A 1 11  ? 161.215 -22.592 -8.838  0.46 85.72  ? 11   PRO A CB   1 
ATOM   6    C CG   A PRO A 1 11  ? 160.643 -21.228 -8.843  0.46 89.60  ? 11   PRO A CG   1 
ATOM   7    C CD   A PRO A 1 11  ? 161.278 -20.513 -9.981  0.46 83.57  ? 11   PRO A CD   1 
ATOM   8    H HA   A PRO A 1 11  ? 163.281 -22.437 -8.658  0.46 98.71  ? 11   PRO A HA   1 
ATOM   9    H HB2  A PRO A 1 11  ? 160.704 -23.179 -9.416  0.46 103.07 ? 11   PRO A HB2  1 
ATOM   10   H HB3  A PRO A 1 11  ? 161.249 -22.945 -7.935  0.46 103.07 ? 11   PRO A HB3  1 
ATOM   11   H HG2  A PRO A 1 11  ? 159.683 -21.280 -8.968  0.46 107.72 ? 11   PRO A HG2  1 
ATOM   12   H HG3  A PRO A 1 11  ? 160.853 -20.786 -8.005  0.46 107.72 ? 11   PRO A HG3  1 
ATOM   13   H HD2  A PRO A 1 11  ? 160.772 -20.657 -10.797 0.46 100.48 ? 11   PRO A HD2  1 
ATOM   14   H HD3  A PRO A 1 11  ? 161.370 -19.569 -9.780  0.46 100.48 ? 11   PRO A HD3  1 
ATOM   15   N N    A ALA A 1 12  ? 162.924 -23.316 -11.631 0.46 73.71  ? 12   ALA A N    1 
ATOM   16   C CA   A ALA A 1 12  ? 162.791 -24.360 -12.635 0.46 70.54  ? 12   ALA A CA   1 
ATOM   17   C C    A ALA A 1 12  ? 163.720 -24.159 -13.827 0.46 68.39  ? 12   ALA A C    1 
ATOM   18   O O    A ALA A 1 12  ? 164.149 -23.041 -14.115 0.46 69.79  ? 12   ALA A O    1 
ATOM   19   C CB   A ALA A 1 12  ? 161.359 -24.415 -13.089 0.46 70.39  ? 12   ALA A CB   1 
ATOM   20   H H    A ALA A 1 12  ? 163.003 -22.524 -11.956 0.46 88.66  ? 12   ALA A H    1 
ATOM   21   H HA   A ALA A 1 12  ? 163.009 -25.214 -12.230 0.46 84.84  ? 12   ALA A HA   1 
ATOM   22   H HB1  A ALA A 1 12  ? 161.114 -23.556 -13.468 0.46 84.67  ? 12   ALA A HB1  1 
ATOM   23   H HB2  A ALA A 1 12  ? 161.267 -25.111 -13.759 0.46 84.67  ? 12   ALA A HB2  1 
ATOM   24   H HB3  A ALA A 1 12  ? 160.794 -24.614 -12.326 0.46 84.67  ? 12   ALA A HB3  1 
ATOM   25   N N    A ALA A 1 13  ? 163.991 -25.257 -14.530 0.46 63.74  ? 13   ALA A N    1 
ATOM   26   C CA   A ALA A 1 13  ? 165.040 -25.319 -15.544 0.46 60.87  ? 13   ALA A CA   1 
ATOM   27   C C    A ALA A 1 13  ? 165.075 -26.770 -16.029 0.46 57.60  ? 13   ALA A C    1 
ATOM   28   O O    A ALA A 1 13  ? 164.422 -27.609 -15.412 0.46 61.84  ? 13   ALA A O    1 
ATOM   29   C CB   A ALA A 1 13  ? 166.350 -24.930 -14.918 0.46 63.95  ? 13   ALA A CB   1 
ATOM   30   H H    A ALA A 1 13  ? 163.568 -25.999 -14.434 0.46 76.68  ? 13   ALA A H    1 
ATOM   31   H HA   A ALA A 1 13  ? 164.839 -24.727 -16.286 0.46 73.25  ? 13   ALA A HA   1 
ATOM   32   H HB1  A ALA A 1 13  ? 166.550 -25.547 -14.197 0.46 76.94  ? 13   ALA A HB1  1 
ATOM   33   H HB2  A ALA A 1 13  ? 167.046 -24.972 -15.592 0.46 76.94  ? 13   ALA A HB2  1 
ATOM   34   H HB3  A ALA A 1 13  ? 166.278 -24.027 -14.571 0.46 76.94  ? 13   ALA A HB3  1 
ATOM   35   N N    A ALA A 1 14  ? 165.812 -27.116 -17.091 0.46 53.56  ? 14   ALA A N    1 
ATOM   36   C CA   A ALA A 1 14  ? 166.714 -26.252 -17.851 0.46 52.26  ? 14   ALA A CA   1 
ATOM   37   C C    A ALA A 1 14  ? 166.504 -26.593 -19.346 0.46 48.24  ? 14   ALA A C    1 
ATOM   38   O O    A ALA A 1 14  ? 165.655 -27.423 -19.663 0.46 45.48  ? 14   ALA A O    1 
ATOM   39   C CB   A ALA A 1 14  ? 168.149 -26.519 -17.408 0.46 54.80  ? 14   ALA A CB   1 
ATOM   40   H H    A ALA A 1 14  ? 165.800 -27.915 -17.410 0.46 64.47  ? 14   ALA A H    1 
ATOM   41   H HA   A ALA A 1 14  ? 166.497 -25.319 -17.700 0.46 62.91  ? 14   ALA A HA   1 
ATOM   42   H HB1  A ALA A 1 14  ? 168.363 -27.450 -17.575 0.46 65.96  ? 14   ALA A HB1  1 
ATOM   43   H HB2  A ALA A 1 14  ? 168.747 -25.945 -17.912 0.46 65.96  ? 14   ALA A HB2  1 
ATOM   44   H HB3  A ALA A 1 14  ? 168.226 -26.327 -16.460 0.46 65.96  ? 14   ALA A HB3  1 
ATOM   45   N N    A PRO A 1 15  ? 167.269 -25.974 -20.270 0.46 46.90  ? 15   PRO A N    1 
ATOM   46   C CA   A PRO A 1 15  ? 166.897 -26.075 -21.690 0.46 43.60  ? 15   PRO A CA   1 
ATOM   47   C C    A PRO A 1 15  ? 167.438 -27.304 -22.433 0.46 38.58  ? 15   PRO A C    1 
ATOM   48   O O    A PRO A 1 15  ? 168.462 -27.866 -22.045 0.46 32.57  ? 15   PRO A O    1 
ATOM   49   C CB   A PRO A 1 15  ? 167.516 -24.812 -22.276 0.46 46.11  ? 15   PRO A CB   1 
ATOM   50   C CG   A PRO A 1 15  ? 168.770 -24.661 -21.494 0.46 48.49  ? 15   PRO A CG   1 
ATOM   51   C CD   A PRO A 1 15  ? 168.482 -25.154 -20.102 0.46 50.51  ? 15   PRO A CD   1 
ATOM   52   H HA   A PRO A 1 15  ? 165.933 -26.036 -21.790 0.46 52.52  ? 15   PRO A HA   1 
ATOM   53   H HB2  A PRO A 1 15  ? 167.705 -24.940 -23.219 0.46 55.53  ? 15   PRO A HB2  1 
ATOM   54   H HB3  A PRO A 1 15  ? 166.924 -24.056 -22.137 0.46 55.53  ? 15   PRO A HB3  1 
ATOM   55   H HG2  A PRO A 1 15  ? 169.470 -25.195 -21.903 0.46 58.39  ? 15   PRO A HG2  1 
ATOM   56   H HG3  A PRO A 1 15  ? 169.027 -23.726 -21.475 0.46 58.39  ? 15   PRO A HG3  1 
ATOM   57   H HD2  A PRO A 1 15  ? 169.216 -25.699 -19.778 0.46 60.81  ? 15   PRO A HD2  1 
ATOM   58   H HD3  A PRO A 1 15  ? 168.305 -24.407 -19.509 0.46 60.81  ? 15   PRO A HD3  1 
ATOM   59   N N    A VAL A 1 16  ? 166.755 -27.688 -23.511 0.46 37.95  ? 16   VAL A N    1 
ATOM   60   C CA   A VAL A 1 16  ? 167.106 -28.881 -24.286 0.46 37.17  ? 16   VAL A CA   1 
ATOM   61   C C    A VAL A 1 16  ? 168.249 -28.634 -25.269 0.46 35.52  ? 16   VAL A C    1 
ATOM   62   O O    A VAL A 1 16  ? 168.361 -27.558 -25.860 0.46 29.52  ? 16   VAL A O    1 
ATOM   63   C CB   A VAL A 1 16  ? 165.886 -29.415 -25.081 0.46 41.36  ? 16   VAL A CB   1 
ATOM   64   C CG1  A VAL A 1 16  ? 166.266 -30.640 -25.923 0.46 40.42  ? 16   VAL A CG1  1 
ATOM   65   C CG2  A VAL A 1 16  ? 164.749 -29.764 -24.139 0.46 41.11  ? 16   VAL A CG2  1 
ATOM   66   H H    A VAL A 1 16  ? 166.071 -27.267 -23.820 0.46 45.74  ? 16   VAL A H    1 
ATOM   67   H HA   A VAL A 1 16  ? 167.388 -29.578 -23.673 0.46 44.80  ? 16   VAL A HA   1 
ATOM   68   H HB   A VAL A 1 16  ? 165.574 -28.722 -25.684 0.46 49.83  ? 16   VAL A HB   1 
ATOM   69   H HG11 A VAL A 1 16  ? 166.588 -31.340 -25.334 0.46 48.70  ? 16   VAL A HG11 1 
ATOM   70   H HG12 A VAL A 1 16  ? 165.482 -30.946 -26.405 0.46 48.70  ? 16   VAL A HG12 1 
ATOM   71   H HG13 A VAL A 1 16  ? 166.963 -30.388 -26.549 0.46 48.70  ? 16   VAL A HG13 1 
ATOM   72   H HG21 A VAL A 1 16  ? 164.488 -28.967 -23.652 0.46 49.53  ? 16   VAL A HG21 1 
ATOM   73   H HG22 A VAL A 1 16  ? 163.999 -30.095 -24.659 0.46 49.53  ? 16   VAL A HG22 1 
ATOM   74   H HG23 A VAL A 1 16  ? 165.050 -30.447 -23.520 0.46 49.53  ? 16   VAL A HG23 1 
ATOM   75   N N    A ALA A 1 17  ? 169.083 -29.656 -25.439 0.46 38.43  ? 17   ALA A N    1 
ATOM   76   C CA   A ALA A 1 17  ? 170.199 -29.620 -26.377 0.46 37.72  ? 17   ALA A CA   1 
ATOM   77   C C    A ALA A 1 17  ? 169.925 -30.514 -27.583 0.46 32.70  ? 17   ALA A C    1 
ATOM   78   O O    A ALA A 1 17  ? 169.779 -31.729 -27.446 0.46 33.51  ? 17   ALA A O    1 
ATOM   79   C CB   A ALA A 1 17  ? 171.469 -30.068 -25.682 0.46 40.37  ? 17   ALA A CB   1 
ATOM   80   H H    A ALA A 1 17  ? 169.020 -30.400 -25.012 0.46 46.31  ? 17   ALA A H    1 
ATOM   81   H HA   A ALA A 1 17  ? 170.327 -28.711 -26.692 0.46 45.47  ? 17   ALA A HA   1 
ATOM   82   H HB1  A ALA A 1 17  ? 171.347 -30.974 -25.356 0.46 48.65  ? 17   ALA A HB1  1 
ATOM   83   H HB2  A ALA A 1 17  ? 172.202 -30.039 -26.315 0.46 48.65  ? 17   ALA A HB2  1 
ATOM   84   H HB3  A ALA A 1 17  ? 171.649 -29.471 -24.939 0.46 48.65  ? 17   ALA A HB3  1 
ATOM   85   N N    A ALA A 1 18  ? 169.865 -29.908 -28.764 0.46 31.40  ? 18   ALA A N    1 
ATOM   86   C CA   A ALA A 1 18  ? 169.661 -30.656 -29.998 0.46 30.86  ? 18   ALA A CA   1 
ATOM   87   C C    A ALA A 1 18  ? 170.989 -31.228 -30.482 0.46 29.49  ? 18   ALA A C    1 
ATOM   88   O O    A ALA A 1 18  ? 172.054 -30.774 -30.063 0.46 28.96  ? 18   ALA A O    1 
ATOM   89   C CB   A ALA A 1 18  ? 169.056 -29.760 -31.061 0.46 30.00  ? 18   ALA A CB   1 
ATOM   90   H H    A ALA A 1 18  ? 169.940 -29.059 -28.877 0.46 37.88  ? 18   ALA A H    1 
ATOM   91   H HA   A ALA A 1 18  ? 169.052 -31.392 -29.833 0.46 37.23  ? 18   ALA A HA   1 
ATOM   92   H HB1  A ALA A 1 18  ? 169.660 -29.020 -31.230 0.46 36.20  ? 18   ALA A HB1  1 
ATOM   93   H HB2  A ALA A 1 18  ? 168.929 -30.276 -31.873 0.46 36.20  ? 18   ALA A HB2  1 
ATOM   94   H HB3  A ALA A 1 18  ? 168.203 -29.427 -30.744 0.46 36.20  ? 18   ALA A HB3  1 
ATOM   95   N N    A ARG A 1 19  ? 170.924 -32.225 -31.360 0.46 32.67  ? 19   ARG A N    1 
ATOM   96   C CA   A ARG A 1 19  ? 172.136 -32.815 -31.921 0.46 33.91  ? 19   ARG A CA   1 
ATOM   97   C C    A ARG A 1 19  ? 171.874 -33.659 -33.169 0.46 32.20  ? 19   ARG A C    1 
ATOM   98   O O    A ARG A 1 19  ? 170.729 -33.868 -33.568 0.46 33.54  ? 19   ARG A O    1 
ATOM   99   C CB   A ARG A 1 19  ? 172.857 -33.664 -30.869 0.46 36.24  ? 19   ARG A CB   1 
ATOM   100  C CG   A ARG A 1 19  ? 172.160 -34.968 -30.485 0.46 39.70  ? 19   ARG A CG   1 
ATOM   101  C CD   A ARG A 1 19  ? 173.177 -35.964 -29.955 0.46 47.57  ? 19   ARG A CD   1 
ATOM   102  N NE   A ARG A 1 19  ? 172.604 -37.290 -29.723 0.46 51.61  ? 19   ARG A NE   1 
ATOM   103  C CZ   A ARG A 1 19  ? 172.370 -37.825 -28.526 0.46 53.13  ? 19   ARG A CZ   1 
ATOM   104  N NH1  A ARG A 1 19  ? 172.651 -37.163 -27.409 0.46 53.95  ? 19   ARG A NH1  1 
ATOM   105  N NH2  A ARG A 1 19  ? 171.849 -39.041 -28.445 0.46 53.70  ? 19   ARG A NH2  1 
ATOM   106  H H    A ARG A 1 19  ? 170.193 -32.577 -31.647 0.46 39.41  ? 19   ARG A H    1 
ATOM   107  H HA   A ARG A 1 19  ? 172.736 -32.097 -32.177 0.46 40.89  ? 19   ARG A HA   1 
ATOM   108  H HB2  A ARG A 1 19  ? 173.735 -33.893 -31.210 0.46 43.69  ? 19   ARG A HB2  1 
ATOM   109  H HB3  A ARG A 1 19  ? 172.950 -33.136 -30.061 0.46 43.69  ? 19   ARG A HB3  1 
ATOM   110  H HG2  A ARG A 1 19  ? 171.506 -34.795 -29.790 0.46 47.84  ? 19   ARG A HG2  1 
ATOM   111  H HG3  A ARG A 1 19  ? 171.732 -35.350 -31.268 0.46 47.84  ? 19   ARG A HG3  1 
ATOM   112  H HD2  A ARG A 1 19  ? 173.894 -36.057 -30.601 0.46 57.28  ? 19   ARG A HD2  1 
ATOM   113  H HD3  A ARG A 1 19  ? 173.529 -35.638 -29.113 0.46 57.28  ? 19   ARG A HD3  1 
ATOM   114  H HE   A ARG A 1 19  ? 172.403 -37.761 -30.413 0.46 62.14  ? 19   ARG A HE   1 
ATOM   115  H HH11 A ARG A 1 19  ? 172.990 -36.374 -27.450 0.46 64.64  ? 19   ARG A HH11 1 
ATOM   116  H HH12 A ARG A 1 19  ? 172.493 -37.524 -26.644 0.46 64.64  ? 19   ARG A HH12 1 
ATOM   117  H HH21 A ARG A 1 19  ? 171.663 -39.478 -29.163 0.46 64.94  ? 19   ARG A HH21 1 
ATOM   118  H HH22 A ARG A 1 19  ? 171.694 -39.393 -27.676 0.46 64.94  ? 19   ARG A HH22 1 
ATOM   119  N N    . GLY A 1 20  ? 172.956 -34.144 -33.772 1.00 63.24  ? 20   GLY A N    1 
ATOM   120  C CA   . GLY A 1 20  ? 172.872 -35.030 -34.917 1.00 65.09  ? 20   GLY A CA   1 
ATOM   121  C C    . GLY A 1 20  ? 172.309 -34.359 -36.152 1.00 63.11  ? 20   GLY A C    1 
ATOM   122  O O    . GLY A 1 20  ? 172.650 -33.216 -36.465 1.00 56.35  ? 20   GLY A O    1 
ATOM   123  H H    . GLY A 1 20  ? 173.762 -33.967 -33.530 1.00 76.09  ? 20   GLY A H    1 
ATOM   124  H HA2  . GLY A 1 20  ? 173.758 -35.364 -35.129 1.00 78.30  ? 20   GLY A HA2  1 
ATOM   125  H HA3  . GLY A 1 20  ? 172.306 -35.786 -34.696 1.00 78.30  ? 20   GLY A HA3  1 
ATOM   126  N N    . GLY A 1 21  ? 171.442 -35.080 -36.857 1.00 64.69  ? 21   GLY A N    1 
ATOM   127  C CA   . GLY A 1 21  ? 170.847 -34.580 -38.082 1.00 61.84  ? 21   GLY A CA   1 
ATOM   128  C C    . GLY A 1 21  ? 169.726 -33.588 -37.841 1.00 53.67  ? 21   GLY A C    1 
ATOM   129  O O    . GLY A 1 21  ? 169.040 -33.179 -38.778 1.00 55.50  ? 21   GLY A O    1 
ATOM   130  H H    . GLY A 1 21  ? 171.181 -35.870 -36.640 1.00 77.83  ? 21   GLY A H    1 
ATOM   131  H HA2  . GLY A 1 21  ? 171.531 -34.144 -38.615 1.00 74.41  ? 21   GLY A HA2  1 
ATOM   132  H HA3  . GLY A 1 21  ? 170.492 -35.325 -38.592 1.00 74.41  ? 21   GLY A HA3  1 
ATOM   133  N N    . GLU A 1 22  ? 169.530 -33.208 -36.583 1.00 46.44  ? 22   GLU A N    1 
ATOM   134  C CA   . GLU A 1 22  ? 168.594 -32.146 -36.245 1.00 38.65  ? 22   GLU A CA   1 
ATOM   135  C C    . GLU A 1 22  ? 169.258 -30.792 -36.455 1.00 36.38  ? 22   GLU A C    1 
ATOM   136  O O    . GLU A 1 22  ? 168.597 -29.756 -36.391 1.00 35.27  ? 22   GLU A O    1 
ATOM   137  C CB   . GLU A 1 22  ? 168.138 -32.275 -34.794 1.00 38.15  ? 22   GLU A CB   1 
ATOM   138  C CG   . GLU A 1 22  ? 167.383 -33.558 -34.497 1.00 45.32  ? 22   GLU A CG   1 
ATOM   139  C CD   . GLU A 1 22  ? 166.999 -33.687 -33.037 1.00 50.36  ? 22   GLU A CD   1 
ATOM   140  O OE1  . GLU A 1 22  ? 167.632 -33.023 -32.187 1.00 51.52  ? 22   GLU A OE1  1 
ATOM   141  O OE2  . GLU A 1 22  ? 166.057 -34.451 -32.739 1.00 58.10  ? 22   GLU A OE2  1 
ATOM   142  H H    . GLU A 1 22  ? 169.930 -33.552 -35.904 1.00 55.93  ? 22   GLU A H    1 
ATOM   143  H HA   . GLU A 1 22  ? 167.815 -32.202 -36.821 1.00 46.58  ? 22   GLU A HA   1 
ATOM   144  H HB2  . GLU A 1 22  ? 168.918 -32.251 -34.218 1.00 45.98  ? 22   GLU A HB2  1 
ATOM   145  H HB3  . GLU A 1 22  ? 167.551 -31.532 -34.584 1.00 45.98  ? 22   GLU A HB3  1 
ATOM   146  H HG2  . GLU A 1 22  ? 166.569 -33.576 -35.024 1.00 54.58  ? 22   GLU A HG2  1 
ATOM   147  H HG3  . GLU A 1 22  ? 167.944 -34.316 -34.727 1.00 54.58  ? 22   GLU A HG3  1 
ATOM   148  N N    . LEU A 1 23  ? 170.565 -30.812 -36.710 1.00 38.06  ? 23   LEU A N    1 
ATOM   149  C CA   . LEU A 1 23  ? 171.343 -29.590 -36.870 1.00 33.98  ? 23   LEU A CA   1 
ATOM   150  C C    . LEU A 1 23  ? 172.001 -29.492 -38.240 1.00 34.29  ? 23   LEU A C    1 
ATOM   151  O O    . LEU A 1 23  ? 172.335 -30.501 -38.863 1.00 36.71  ? 23   LEU A O    1 
ATOM   152  C CB   . LEU A 1 23  ? 172.422 -29.504 -35.790 1.00 34.15  ? 23   LEU A CB   1 
ATOM   153  C CG   . LEU A 1 23  ? 171.937 -29.417 -34.343 1.00 38.90  ? 23   LEU A CG   1 
ATOM   154  C CD1  . LEU A 1 23  ? 173.117 -29.487 -33.390 1.00 36.22  ? 23   LEU A CD1  1 
ATOM   155  C CD2  . LEU A 1 23  ? 171.138 -28.143 -34.109 1.00 41.13  ? 23   LEU A CD2  1 
ATOM   156  H H    . LEU A 1 23  ? 171.028 -31.532 -36.795 1.00 45.88  ? 23   LEU A H    1 
ATOM   157  H HA   . LEU A 1 23  ? 170.754 -28.826 -36.766 1.00 40.97  ? 23   LEU A HA   1 
ATOM   158  H HB2  . LEU A 1 23  ? 172.982 -30.293 -35.858 1.00 41.18  ? 23   LEU A HB2  1 
ATOM   159  H HB3  . LEU A 1 23  ? 172.959 -28.714 -35.960 1.00 41.18  ? 23   LEU A HB3  1 
ATOM   160  H HG   . LEU A 1 23  ? 171.357 -30.172 -34.158 1.00 46.89  ? 23   LEU A HG   1 
ATOM   161  H HD11 . LEU A 1 23  ? 173.715 -28.745 -33.574 1.00 43.67  ? 23   LEU A HD11 1 
ATOM   162  H HD12 . LEU A 1 23  ? 172.790 -29.430 -32.479 1.00 43.67  ? 23   LEU A HD12 1 
ATOM   163  H HD13 . LEU A 1 23  ? 173.581 -30.328 -33.524 1.00 43.67  ? 23   LEU A HD13 1 
ATOM   164  H HD21 . LEU A 1 23  ? 170.368 -28.140 -34.700 1.00 49.56  ? 23   LEU A HD21 1 
ATOM   165  H HD22 . LEU A 1 23  ? 170.846 -28.119 -33.185 1.00 49.56  ? 23   LEU A HD22 1 
ATOM   166  H HD23 . LEU A 1 23  ? 171.703 -27.377 -34.298 1.00 49.56  ? 23   LEU A HD23 1 
ATOM   167  N N    . THR A 1 24  ? 172.178 -28.256 -38.695 1.00 33.11  ? 24   THR A N    1 
ATOM   168  C CA   . THR A 1 24  ? 172.934 -27.966 -39.903 1.00 32.60  ? 24   THR A CA   1 
ATOM   169  C C    . THR A 1 24  ? 173.705 -26.676 -39.681 1.00 30.37  ? 24   THR A C    1 
ATOM   170  O O    . THR A 1 24  ? 173.366 -25.888 -38.797 1.00 34.04  ? 24   THR A O    1 
ATOM   171  C CB   . THR A 1 24  ? 172.023 -27.811 -41.134 1.00 36.37  ? 24   THR A CB   1 
ATOM   172  O OG1  . THR A 1 24  ? 172.815 -27.456 -42.274 1.00 41.27  ? 24   THR A OG1  1 
ATOM   173  C CG2  . THR A 1 24  ? 170.973 -26.740 -40.900 1.00 35.97  ? 24   THR A CG2  1 
ATOM   174  H H    . THR A 1 24  ? 171.862 -27.555 -38.311 1.00 39.93  ? 24   THR A H    1 
ATOM   175  H HA   . THR A 1 24  ? 173.567 -28.681 -40.072 1.00 39.32  ? 24   THR A HA   1 
ATOM   176  H HB   . THR A 1 24  ? 171.570 -28.651 -41.307 1.00 43.84  ? 24   THR A HB   1 
ATOM   177  H HG1  . THR A 1 24  ? 172.324 -27.370 -42.950 1.00 49.73  ? 24   THR A HG1  1 
ATOM   178  H HG21 . THR A 1 24  ? 171.403 -25.888 -40.726 1.00 43.36  ? 24   THR A HG21 1 
ATOM   179  H HG22 . THR A 1 24  ? 170.407 -26.654 -41.683 1.00 43.36  ? 24   THR A HG22 1 
ATOM   180  H HG23 . THR A 1 24  ? 170.423 -26.977 -40.137 1.00 43.36  ? 24   THR A HG23 1 
ATOM   181  N N    . GLN A 1 25  ? 174.745 -26.469 -40.481 1.00 37.19  ? 25   GLN A N    1 
ATOM   182  C CA   . GLN A 1 25  ? 175.576 -25.280 -40.358 1.00 42.14  ? 25   GLN A CA   1 
ATOM   183  C C    . GLN A 1 25  ? 175.421 -24.373 -41.570 1.00 41.28  ? 25   GLN A C    1 
ATOM   184  O O    . GLN A 1 25  ? 175.152 -24.837 -42.679 1.00 41.93  ? 25   GLN A O    1 
ATOM   185  C CB   . GLN A 1 25  ? 177.045 -25.667 -40.171 1.00 52.32  ? 25   GLN A CB   1 
ATOM   186  C CG   . GLN A 1 25  ? 177.301 -26.539 -38.949 1.00 61.05  ? 25   GLN A CG   1 
ATOM   187  C CD   . GLN A 1 25  ? 178.777 -26.727 -38.662 1.00 73.92  ? 25   GLN A CD   1 
ATOM   188  O OE1  . GLN A 1 25  ? 179.333 -27.803 -38.890 1.00 83.95  ? 25   GLN A OE1  1 
ATOM   189  N NE2  . GLN A 1 25  ? 179.420 -25.683 -38.151 1.00 72.89  ? 25   GLN A NE2  1 
ATOM   190  H H    . GLN A 1 25  ? 174.991 -27.005 -41.106 1.00 44.83  ? 25   GLN A H    1 
ATOM   191  H HA   . GLN A 1 25  ? 175.297 -24.781 -39.574 1.00 50.77  ? 25   GLN A HA   1 
ATOM   192  H HB2  . GLN A 1 25  ? 177.340 -26.160 -40.953 1.00 62.98  ? 25   GLN A HB2  1 
ATOM   193  H HB3  . GLN A 1 25  ? 177.572 -24.859 -40.074 1.00 62.98  ? 25   GLN A HB3  1 
ATOM   194  H HG2  . GLN A 1 25  ? 176.895 -26.122 -38.173 1.00 73.46  ? 25   GLN A HG2  1 
ATOM   195  H HG3  . GLN A 1 25  ? 176.910 -27.414 -39.098 1.00 73.46  ? 25   GLN A HG3  1 
ATOM   196  H HE21 . GLN A 1 25  ? 178.997 -24.949 -38.000 1.00 87.67  ? 25   GLN A HE21 1 
ATOM   197  H HE22 . GLN A 1 25  ? 180.259 -25.740 -37.971 1.00 87.67  ? 25   GLN A HE22 1 
ATOM   198  N N    . SER A 1 26  ? 175.581 -23.074 -41.335 1.00 40.30  ? 26   SER A N    1 
ATOM   199  C CA   . SER A 1 26  ? 175.533 -22.072 -42.390 1.00 38.50  ? 26   SER A CA   1 
ATOM   200  C C    . SER A 1 26  ? 176.826 -21.269 -42.338 1.00 39.13  ? 26   SER A C    1 
ATOM   201  O O    . SER A 1 26  ? 177.530 -21.288 -41.329 1.00 35.21  ? 26   SER A O    1 
ATOM   202  C CB   . SER A 1 26  ? 174.322 -21.156 -42.206 1.00 39.43  ? 26   SER A CB   1 
ATOM   203  O OG   . SER A 1 26  ? 174.521 -20.248 -41.139 1.00 48.01  ? 26   SER A OG   1 
ATOM   204  H H    . SER A 1 26  ? 175.721 -22.743 -40.554 1.00 48.56  ? 26   SER A H    1 
ATOM   205  H HA   . SER A 1 26  ? 175.468 -22.507 -43.255 1.00 46.39  ? 26   SER A HA   1 
ATOM   206  H HB2  . SER A 1 26  ? 174.180 -20.654 -43.023 1.00 47.52  ? 26   SER A HB2  1 
ATOM   207  H HB3  . SER A 1 26  ? 173.542 -21.700 -42.013 1.00 47.52  ? 26   SER A HB3  1 
ATOM   208  H HG   . SER A 1 26  ? 173.847 -19.754 -41.053 1.00 57.81  ? 26   SER A HG   1 
ATOM   209  N N    . THR A 1 27  ? 177.135 -20.574 -43.429 1.00 38.64  ? 27   THR A N    1 
ATOM   210  C CA   . THR A 1 27  ? 178.388 -19.837 -43.551 1.00 30.06  ? 27   THR A CA   1 
ATOM   211  C C    . THR A 1 27  ? 178.124 -18.346 -43.735 1.00 29.36  ? 27   THR A C    1 
ATOM   212  O O    . THR A 1 27  ? 177.144 -17.949 -44.369 1.00 28.94  ? 27   THR A O    1 
ATOM   213  C CB   . THR A 1 27  ? 179.222 -20.375 -44.724 1.00 32.15  ? 27   THR A CB   1 
ATOM   214  O OG1  . THR A 1 27  ? 179.526 -21.755 -44.489 1.00 32.36  ? 27   THR A OG1  1 
ATOM   215  C CG2  . THR A 1 27  ? 180.522 -19.597 -44.884 1.00 32.83  ? 27   THR A CG2  1 
ATOM   216  H H    . THR A 1 27  ? 176.628 -20.513 -44.121 1.00 46.57  ? 27   THR A H    1 
ATOM   217  H HA   . THR A 1 27  ? 178.904 -19.952 -42.737 1.00 36.28  ? 27   THR A HA   1 
ATOM   218  H HB   . THR A 1 27  ? 178.713 -20.293 -45.545 1.00 38.78  ? 27   THR A HB   1 
ATOM   219  H HG1  . THR A 1 27  ? 179.982 -22.061 -45.125 1.00 39.04  ? 27   THR A HG1  1 
ATOM   220  H HG21 . THR A 1 27  ? 181.053 -19.668 -44.076 1.00 39.60  ? 27   THR A HG21 1 
ATOM   221  H HG22 . THR A 1 27  ? 181.031 -19.953 -45.629 1.00 39.60  ? 27   THR A HG22 1 
ATOM   222  H HG23 . THR A 1 27  ? 180.329 -18.661 -45.053 1.00 39.60  ? 27   THR A HG23 1 
ATOM   223  N N    . HIS A 1 28  ? 179.006 -17.527 -43.169 1.00 28.21  ? 28   HIS A N    1 
ATOM   224  C CA   . HIS A 1 28  ? 178.842 -16.078 -43.194 1.00 33.16  ? 28   HIS A CA   1 
ATOM   225  C C    . HIS A 1 28  ? 180.182 -15.383 -43.294 1.00 30.58  ? 28   HIS A C    1 
ATOM   226  O O    . HIS A 1 28  ? 181.217 -15.961 -42.974 1.00 32.77  ? 28   HIS A O    1 
ATOM   227  C CB   . HIS A 1 28  ? 178.171 -15.599 -41.909 1.00 34.77  ? 28   HIS A CB   1 
ATOM   228  C CG   . HIS A 1 28  ? 176.991 -16.419 -41.501 1.00 38.59  ? 28   HIS A CG   1 
ATOM   229  N ND1  . HIS A 1 28  ? 175.695 -16.040 -41.769 1.00 42.84  ? 28   HIS A ND1  1 
ATOM   230  C CD2  . HIS A 1 28  ? 176.911 -17.601 -40.846 1.00 39.85  ? 28   HIS A CD2  1 
ATOM   231  C CE1  . HIS A 1 28  ? 174.865 -16.953 -41.299 1.00 42.05  ? 28   HIS A CE1  1 
ATOM   232  N NE2  . HIS A 1 28  ? 175.578 -17.910 -40.733 1.00 43.04  ? 28   HIS A NE2  1 
ATOM   233  H H    . HIS A 1 28  ? 179.715 -17.789 -42.760 1.00 34.05  ? 28   HIS A H    1 
ATOM   234  H HA   . HIS A 1 28  ? 178.295 -15.819 -43.952 1.00 39.99  ? 28   HIS A HA   1 
ATOM   235  H HB2  . HIS A 1 28  ? 178.818 -15.631 -41.187 1.00 41.92  ? 28   HIS A HB2  1 
ATOM   236  H HB3  . HIS A 1 28  ? 177.867 -14.686 -42.036 1.00 41.92  ? 28   HIS A HB3  1 
ATOM   237  H HD1  . HIS A 1 28  ? 175.462 -15.321 -42.180 1.00 51.61  ? 28   HIS A HD1  1 
ATOM   238  H HD2  . HIS A 1 28  ? 177.625 -18.108 -40.533 1.00 48.02  ? 28   HIS A HD2  1 
ATOM   239  H HE1  . HIS A 1 28  ? 173.937 -16.926 -41.354 1.00 50.66  ? 28   HIS A HE1  1 
ATOM   240  H HE2  . HIS A 1 28  ? 175.259 -18.614 -40.355 1.00 51.85  ? 28   HIS A HE2  1 
ATOM   241  N N    . LEU A 1 29  ? 180.151 -14.131 -43.730 1.00 30.39  ? 29   LEU A N    1 
ATOM   242  C CA   . LEU A 1 29  ? 181.291 -13.250 -43.564 1.00 31.88  ? 29   LEU A CA   1 
ATOM   243  C C    . LEU A 1 29  ? 181.417 -12.923 -42.088 1.00 32.25  ? 29   LEU A C    1 
ATOM   244  O O    . LEU A 1 29  ? 180.414 -12.841 -41.376 1.00 36.09  ? 29   LEU A O    1 
ATOM   245  C CB   . LEU A 1 29  ? 181.099 -11.945 -44.339 1.00 33.43  ? 29   LEU A CB   1 
ATOM   246  C CG   . LEU A 1 29  ? 181.192 -11.937 -45.864 1.00 31.75  ? 29   LEU A CG   1 
ATOM   247  C CD1  . LEU A 1 29  ? 181.065 -10.507 -46.358 1.00 31.49  ? 29   LEU A CD1  1 
ATOM   248  C CD2  . LEU A 1 29  ? 182.493 -12.550 -46.351 1.00 30.67  ? 29   LEU A CD2  1 
ATOM   249  H H    . LEU A 1 29  ? 179.479 -13.768 -44.126 1.00 36.67  ? 29   LEU A H    1 
ATOM   250  H HA   . LEU A 1 29  ? 182.102 -13.688 -43.866 1.00 38.45  ? 29   LEU A HA   1 
ATOM   251  H HB2  . LEU A 1 29  ? 180.219 -11.602 -44.116 1.00 40.31  ? 29   LEU A HB2  1 
ATOM   252  H HB3  . LEU A 1 29  ? 181.767 -11.317 -44.020 1.00 40.31  ? 29   LEU A HB3  1 
ATOM   253  H HG   . LEU A 1 29  ? 180.457 -12.452 -46.233 1.00 38.30  ? 29   LEU A HG   1 
ATOM   254  H HD11 . LEU A 1 29  ? 181.785 -9.977  -45.979 1.00 37.98  ? 29   LEU A HD11 1 
ATOM   255  H HD12 . LEU A 1 29  ? 181.124 -10.501 -47.326 1.00 37.98  ? 29   LEU A HD12 1 
ATOM   256  H HD13 . LEU A 1 29  ? 180.208 -10.151 -46.076 1.00 37.98  ? 29   LEU A HD13 1 
ATOM   257  H HD21 . LEU A 1 29  ? 182.544 -13.468 -46.042 1.00 37.00  ? 29   LEU A HD21 1 
ATOM   258  H HD22 . LEU A 1 29  ? 182.511 -12.525 -47.320 1.00 37.00  ? 29   LEU A HD22 1 
ATOM   259  H HD23 . LEU A 1 29  ? 183.236 -12.039 -45.993 1.00 37.00  ? 29   LEU A HD23 1 
ATOM   260  N N    . THR A 1 30  ? 182.647 -12.742 -41.624 1.00 36.59  ? 30   THR A N    1 
ATOM   261  C CA   . THR A 1 30  ? 182.879 -12.198 -40.294 1.00 35.15  ? 30   THR A CA   1 
ATOM   262  C C    . THR A 1 30  ? 182.503 -10.729 -40.326 1.00 34.13  ? 30   THR A C    1 
ATOM   263  O O    . THR A 1 30  ? 182.475 -10.118 -41.394 1.00 29.01  ? 30   THR A O    1 
ATOM   264  C CB   . THR A 1 30  ? 184.354 -12.305 -39.885 1.00 37.75  ? 30   THR A CB   1 
ATOM   265  O OG1  . THR A 1 30  ? 185.168 -11.642 -40.860 1.00 40.19  ? 30   THR A OG1  1 
ATOM   266  C CG2  . THR A 1 30  ? 184.776 -13.758 -39.772 1.00 32.81  ? 30   THR A CG2  1 
ATOM   267  H H    . THR A 1 30  ? 183.365 -12.926 -42.061 1.00 44.11  ? 30   THR A H    1 
ATOM   268  H HA   . THR A 1 30  ? 182.329 -12.657 -39.641 1.00 42.38  ? 30   THR A HA   1 
ATOM   269  H HB   . THR A 1 30  ? 184.479 -11.882 -39.021 1.00 45.50  ? 30   THR A HB   1 
ATOM   270  H HG1  . THR A 1 30  ? 185.978 -11.696 -40.643 1.00 48.42  ? 30   THR A HG1  1 
ATOM   271  H HG21 . THR A 1 30  ? 184.659 -14.204 -40.625 1.00 39.57  ? 30   THR A HG21 1 
ATOM   272  H HG22 . THR A 1 30  ? 185.709 -13.813 -39.513 1.00 39.57  ? 30   THR A HG22 1 
ATOM   273  H HG23 . THR A 1 30  ? 184.236 -14.209 -39.104 1.00 39.57  ? 30   THR A HG23 1 
ATOM   274  N N    . LEU A 1 31  ? 182.212 -10.162 -39.161 1.00 34.10  ? 31   LEU A N    1 
ATOM   275  C CA   . LEU A 1 31  ? 181.942 -8.735  -39.071 1.00 32.80  ? 31   LEU A CA   1 
ATOM   276  C C    . LEU A 1 31  ? 183.156 -7.952  -39.544 1.00 34.42  ? 31   LEU A C    1 
ATOM   277  O O    . LEU A 1 31  ? 183.023 -6.890  -40.150 1.00 36.73  ? 31   LEU A O    1 
ATOM   278  C CB   . LEU A 1 31  ? 181.609 -8.332  -37.634 1.00 30.06  ? 31   LEU A CB   1 
ATOM   279  C CG   . LEU A 1 31  ? 181.456 -6.823  -37.408 1.00 30.39  ? 31   LEU A CG   1 
ATOM   280  C CD1  . LEU A 1 31  ? 180.353 -6.247  -38.286 1.00 31.64  ? 31   LEU A CD1  1 
ATOM   281  C CD2  . LEU A 1 31  ? 181.184 -6.522  -35.950 1.00 27.32  ? 31   LEU A CD2  1 
ATOM   282  H H    . LEU A 1 31  ? 182.165 -10.580 -38.411 1.00 41.12  ? 31   LEU A H    1 
ATOM   283  H HA   . LEU A 1 31  ? 181.188 -8.510  -39.638 1.00 39.56  ? 31   LEU A HA   1 
ATOM   284  H HB2  . LEU A 1 31  ? 180.772 -8.752  -37.381 1.00 36.27  ? 31   LEU A HB2  1 
ATOM   285  H HB3  . LEU A 1 31  ? 182.320 -8.645  -37.053 1.00 36.27  ? 31   LEU A HB3  1 
ATOM   286  H HG   . LEU A 1 31  ? 182.287 -6.386  -37.651 1.00 36.66  ? 31   LEU A HG   1 
ATOM   287  H HD11 . LEU A 1 31  ? 179.515 -6.685  -38.068 1.00 38.16  ? 31   LEU A HD11 1 
ATOM   288  H HD12 . LEU A 1 31  ? 180.282 -5.294  -38.119 1.00 38.16  ? 31   LEU A HD12 1 
ATOM   289  H HD13 . LEU A 1 31  ? 180.576 -6.405  -39.217 1.00 38.16  ? 31   LEU A HD13 1 
ATOM   290  H HD21 . LEU A 1 31  ? 181.926 -6.849  -35.417 1.00 32.99  ? 31   LEU A HD21 1 
ATOM   291  H HD22 . LEU A 1 31  ? 181.093 -5.563  -35.838 1.00 32.99  ? 31   LEU A HD22 1 
ATOM   292  H HD23 . LEU A 1 31  ? 180.364 -6.966  -35.684 1.00 32.99  ? 31   LEU A HD23 1 
ATOM   293  N N    A GLU A 1 32  ? 184.342 -8.483  -39.263 0.47 32.88  ? 32   GLU A N    1 
ATOM   294  N N    B GLU A 1 32  ? 184.341 -8.481  -39.258 0.53 32.69  ? 32   GLU A N    1 
ATOM   295  C CA   A GLU A 1 32  ? 185.583 -7.810  -39.623 0.47 34.90  ? 32   GLU A CA   1 
ATOM   296  C CA   B GLU A 1 32  ? 185.584 -7.815  -39.621 0.53 34.81  ? 32   GLU A CA   1 
ATOM   297  C C    A GLU A 1 32  ? 185.728 -7.739  -41.138 0.47 33.16  ? 32   GLU A C    1 
ATOM   298  C C    B GLU A 1 32  ? 185.731 -7.741  -41.137 0.53 33.10  ? 32   GLU A C    1 
ATOM   299  O O    A GLU A 1 32  ? 186.151 -6.721  -41.684 0.47 33.33  ? 32   GLU A O    1 
ATOM   300  O O    B GLU A 1 32  ? 186.154 -6.723  -41.681 0.53 33.36  ? 32   GLU A O    1 
ATOM   301  C CB   A GLU A 1 32  ? 186.783 -8.537  -39.011 0.47 41.06  ? 32   GLU A CB   1 
ATOM   302  C CB   B GLU A 1 32  ? 186.776 -8.554  -39.010 0.53 41.14  ? 32   GLU A CB   1 
ATOM   303  C CG   A GLU A 1 32  ? 188.055 -7.699  -38.944 0.47 45.22  ? 32   GLU A CG   1 
ATOM   304  C CG   B GLU A 1 32  ? 188.075 -7.763  -39.024 0.53 45.32  ? 32   GLU A CG   1 
ATOM   305  C CD   A GLU A 1 32  ? 187.917 -6.501  -38.024 0.47 45.48  ? 32   GLU A CD   1 
ATOM   306  C CD   B GLU A 1 32  ? 189.192 -8.467  -38.280 0.53 48.95  ? 32   GLU A CD   1 
ATOM   307  O OE1  A GLU A 1 32  ? 187.510 -6.687  -36.858 0.47 50.81  ? 32   GLU A OE1  1 
ATOM   308  O OE1  B GLU A 1 32  ? 188.972 -8.869  -37.117 0.53 50.89  ? 32   GLU A OE1  1 
ATOM   309  O OE2  A GLU A 1 32  ? 188.210 -5.371  -38.469 0.47 42.39  ? 32   GLU A OE2  1 
ATOM   310  O OE2  B GLU A 1 32  ? 190.291 -8.613  -38.854 0.53 49.08  ? 32   GLU A OE2  1 
ATOM   311  H H    B GLU A 1 32  ? 184.452 -9.230  -38.851 0.53 39.42  ? 32   GLU A H    1 
ATOM   312  H HA   A GLU A 1 32  ? 185.567 -6.904  -39.276 0.47 42.08  ? 32   GLU A HA   1 
ATOM   313  H HA   B GLU A 1 32  ? 185.577 -6.910  -39.272 0.53 41.97  ? 32   GLU A HA   1 
ATOM   314  H HB2  A GLU A 1 32  ? 186.558 -8.803  -38.106 0.47 49.47  ? 32   GLU A HB2  1 
ATOM   315  H HB2  B GLU A 1 32  ? 186.570 -8.767  -38.087 0.53 49.57  ? 32   GLU A HB2  1 
ATOM   316  H HB3  A GLU A 1 32  ? 186.976 -9.323  -39.545 0.47 49.47  ? 32   GLU A HB3  1 
ATOM   317  H HB3  B GLU A 1 32  ? 186.924 -9.372  -39.510 0.53 49.57  ? 32   GLU A HB3  1 
ATOM   318  H HG2  A GLU A 1 32  ? 188.780 -8.251  -38.611 0.47 54.47  ? 32   GLU A HG2  1 
ATOM   319  H HG2  B GLU A 1 32  ? 188.359 -7.636  -39.943 0.53 54.59  ? 32   GLU A HG2  1 
ATOM   320  H HG3  A GLU A 1 32  ? 188.266 -7.373  -39.833 0.47 54.47  ? 32   GLU A HG3  1 
ATOM   321  H HG3  B GLU A 1 32  ? 187.927 -6.903  -38.601 0.53 54.59  ? 32   GLU A HG3  1 
ATOM   322  N N    . ALA A 1 33  ? 185.372 -8.826  -41.814 1.00 32.83  ? 33   ALA A N    1 
ATOM   323  C CA   . ALA A 1 33  ? 185.452 -8.876  -43.266 1.00 31.90  ? 33   ALA A CA   1 
ATOM   324  C C    . ALA A 1 33  ? 184.396 -7.973  -43.895 1.00 31.60  ? 33   ALA A C    1 
ATOM   325  O O    . ALA A 1 33  ? 184.676 -7.240  -44.844 1.00 31.72  ? 33   ALA A O    1 
ATOM   326  C CB   . ALA A 1 33  ? 185.286 -10.295 -43.745 1.00 31.93  ? 33   ALA A CB   1 
ATOM   327  H H    . ALA A 1 33  ? 185.078 -9.549  -41.452 1.00 39.59  ? 33   ALA A H    1 
ATOM   328  H HA   . ALA A 1 33  ? 186.326 -8.562  -43.547 1.00 38.48  ? 33   ALA A HA   1 
ATOM   329  H HB1  . ALA A 1 33  ? 184.419 -10.625 -43.458 1.00 38.52  ? 33   ALA A HB1  1 
ATOM   330  H HB2  . ALA A 1 33  ? 185.342 -10.310 -44.713 1.00 38.52  ? 33   ALA A HB2  1 
ATOM   331  H HB3  . ALA A 1 33  ? 185.991 -10.842 -43.363 1.00 38.52  ? 33   ALA A HB3  1 
ATOM   332  N N    . ALA A 1 34  ? 183.180 -8.031  -43.363 1.00 28.55  ? 34   ALA A N    1 
ATOM   333  C CA   . ALA A 1 34  ? 182.090 -7.199  -43.855 1.00 29.11  ? 34   ALA A CA   1 
ATOM   334  C C    . ALA A 1 34  ? 182.420 -5.722  -43.678 1.00 29.40  ? 34   ALA A C    1 
ATOM   335  O O    . ALA A 1 34  ? 182.113 -4.902  -44.543 1.00 31.51  ? 34   ALA A O    1 
ATOM   336  C CB   . ALA A 1 34  ? 180.799 -7.543  -43.133 1.00 31.34  ? 34   ALA A CB   1 
ATOM   337  H H    . ALA A 1 34  ? 182.959 -8.549  -42.713 1.00 34.46  ? 34   ALA A H    1 
ATOM   338  H HA   . ALA A 1 34  ? 181.962 -7.369  -44.801 1.00 35.13  ? 34   ALA A HA   1 
ATOM   339  H HB1  . ALA A 1 34  ? 180.918 -7.388  -42.183 1.00 37.81  ? 34   ALA A HB1  1 
ATOM   340  H HB2  . ALA A 1 34  ? 180.088 -6.979  -43.474 1.00 37.81  ? 34   ALA A HB2  1 
ATOM   341  H HB3  . ALA A 1 34  ? 180.588 -8.476  -43.293 1.00 37.81  ? 34   ALA A HB3  1 
ATOM   342  N N    . THR A 1 35  ? 183.050 -5.392  -42.555 1.00 24.08  ? 35   THR A N    1 
ATOM   343  C CA   . THR A 1 35  ? 183.452 -4.021  -42.275 1.00 27.67  ? 35   THR A CA   1 
ATOM   344  C C    . THR A 1 35  ? 184.541 -3.594  -43.249 1.00 32.39  ? 35   THR A C    1 
ATOM   345  O O    . THR A 1 35  ? 184.500 -2.493  -43.800 1.00 33.94  ? 35   THR A O    1 
ATOM   346  C CB   . THR A 1 35  ? 183.976 -3.881  -40.834 1.00 26.12  ? 35   THR A CB   1 
ATOM   347  O OG1  . THR A 1 35  ? 182.928 -4.201  -39.910 1.00 30.77  ? 35   THR A OG1  1 
ATOM   348  C CG2  . THR A 1 35  ? 184.464 -2.466  -40.560 1.00 30.85  ? 35   THR A CG2  1 
ATOM   349  H H    . THR A 1 35  ? 183.258 -5.950  -41.935 1.00 29.10  ? 35   THR A H    1 
ATOM   350  H HA   . THR A 1 35  ? 182.691 -3.430  -42.384 1.00 33.40  ? 35   THR A HA   1 
ATOM   351  H HB   . THR A 1 35  ? 184.718 -4.491  -40.701 1.00 31.54  ? 35   THR A HB   1 
ATOM   352  H HG1  . THR A 1 35  ? 182.667 -4.989  -40.034 1.00 37.12  ? 35   THR A HG1  1 
ATOM   353  H HG21 . THR A 1 35  ? 183.737 -1.836  -40.683 1.00 37.22  ? 35   THR A HG21 1 
ATOM   354  H HG22 . THR A 1 35  ? 184.789 -2.399  -39.649 1.00 37.22  ? 35   THR A HG22 1 
ATOM   355  H HG23 . THR A 1 35  ? 185.184 -2.240  -41.169 1.00 37.22  ? 35   THR A HG23 1 
ATOM   356  N N    . LYS A 1 36  ? 185.512 -4.477  -43.454 1.00 30.54  ? 36   LYS A N    1 
ATOM   357  C CA   . LYS A 1 36  ? 186.615 -4.219  -44.368 1.00 31.20  ? 36   LYS A CA   1 
ATOM   358  C C    . LYS A 1 36  ? 186.090 -3.921  -45.768 1.00 31.32  ? 36   LYS A C    1 
ATOM   359  O O    . LYS A 1 36  ? 186.566 -3.005  -46.439 1.00 31.62  ? 36   LYS A O    1 
ATOM   360  C CB   . LYS A 1 36  ? 187.552 -5.428  -44.408 1.00 33.08  ? 36   LYS A CB   1 
ATOM   361  C CG   . LYS A 1 36  ? 188.814 -5.205  -45.225 1.00 40.60  ? 36   LYS A CG   1 
ATOM   362  C CD   . LYS A 1 36  ? 189.886 -6.239  -44.899 1.00 47.87  ? 36   LYS A CD   1 
ATOM   363  C CE   . LYS A 1 36  ? 189.827 -7.452  -45.814 1.00 51.46  ? 36   LYS A CE   1 
ATOM   364  N NZ   . LYS A 1 36  ? 191.112 -7.622  -46.547 1.00 57.59  ? 36   LYS A NZ   1 
ATOM   365  H H    . LYS A 1 36  ? 185.554 -5.244  -43.068 1.00 36.84  ? 36   LYS A H    1 
ATOM   366  H HA   . LYS A 1 36  ? 187.119 -3.450  -44.058 1.00 37.64  ? 36   LYS A HA   1 
ATOM   367  H HB2  . LYS A 1 36  ? 187.821 -5.644  -43.501 1.00 39.89  ? 36   LYS A HB2  1 
ATOM   368  H HB3  . LYS A 1 36  ? 187.076 -6.178  -44.797 1.00 39.89  ? 36   LYS A HB3  1 
ATOM   369  H HG2  . LYS A 1 36  ? 188.601 -5.276  -46.168 1.00 48.92  ? 36   LYS A HG2  1 
ATOM   370  H HG3  . LYS A 1 36  ? 189.172 -4.325  -45.027 1.00 48.92  ? 36   LYS A HG3  1 
ATOM   371  H HD2  . LYS A 1 36  ? 190.760 -5.830  -44.997 1.00 57.65  ? 36   LYS A HD2  1 
ATOM   372  H HD3  . LYS A 1 36  ? 189.763 -6.545  -43.986 1.00 57.65  ? 36   LYS A HD3  1 
ATOM   373  H HE2  . LYS A 1 36  ? 189.670 -8.248  -45.284 1.00 61.95  ? 36   LYS A HE2  1 
ATOM   374  H HE3  . LYS A 1 36  ? 189.117 -7.331  -46.464 1.00 61.95  ? 36   LYS A HE3  1 
ATOM   375  H HZ1  . LYS A 1 36  ? 191.779 -7.735  -45.969 1.00 69.31  ? 36   LYS A HZ1  1 
ATOM   376  H HZ2  . LYS A 1 36  ? 191.066 -8.334  -47.079 1.00 69.31  ? 36   LYS A HZ2  1 
ATOM   377  H HZ3  . LYS A 1 36  ? 191.277 -6.901  -47.042 1.00 69.31  ? 36   LYS A HZ3  1 
ATOM   378  N N    . ALA A 1 37  ? 185.099 -4.695  -46.195 1.00 27.78  ? 37   ALA A N    1 
ATOM   379  C CA   . ALA A 1 37  ? 184.507 -4.531  -47.515 1.00 29.17  ? 37   ALA A CA   1 
ATOM   380  C C    . ALA A 1 37  ? 183.744 -3.213  -47.627 1.00 29.89  ? 37   ALA A C    1 
ATOM   381  O O    . ALA A 1 37  ? 183.917 -2.468  -48.592 1.00 30.25  ? 37   ALA A O    1 
ATOM   382  C CB   . ALA A 1 37  ? 183.589 -5.695  -47.819 1.00 30.67  ? 37   ALA A CB   1 
ATOM   383  H H    . ALA A 1 37  ? 184.748 -5.330  -45.733 1.00 33.53  ? 37   ALA A H    1 
ATOM   384  H HA   . ALA A 1 37  ? 185.214 -4.525  -48.179 1.00 35.20  ? 37   ALA A HA   1 
ATOM   385  H HB1  . ALA A 1 37  ? 182.886 -5.724  -47.151 1.00 37.00  ? 37   ALA A HB1  1 
ATOM   386  H HB2  . ALA A 1 37  ? 183.203 -5.570  -48.701 1.00 37.00  ? 37   ALA A HB2  1 
ATOM   387  H HB3  . ALA A 1 37  ? 184.103 -6.517  -47.796 1.00 37.00  ? 37   ALA A HB3  1 
ATOM   388  N N    . ALA A 1 38  ? 182.900 -2.931  -46.640 1.00 31.96  ? 38   ALA A N    1 
ATOM   389  C CA   . ALA A 1 38  ? 182.092 -1.718  -46.647 1.00 33.76  ? 38   ALA A CA   1 
ATOM   390  C C    . ALA A 1 38  ? 182.974 -0.476  -46.650 1.00 31.94  ? 38   ALA A C    1 
ATOM   391  O O    . ALA A 1 38  ? 182.706 0.486   -47.369 1.00 35.90  ? 38   ALA A O    1 
ATOM   392  C CB   . ALA A 1 38  ? 181.167 -1.700  -45.451 1.00 32.97  ? 38   ALA A CB   1 
ATOM   393  H H    . ALA A 1 38  ? 182.775 -3.431  -45.951 1.00 38.55  ? 38   ALA A H    1 
ATOM   394  H HA   . ALA A 1 38  ? 181.548 -1.703  -47.450 1.00 40.72  ? 38   ALA A HA   1 
ATOM   395  H HB1  . ALA A 1 38  ? 181.699 -1.728  -44.640 1.00 39.76  ? 38   ALA A HB1  1 
ATOM   396  H HB2  . ALA A 1 38  ? 180.639 -0.887  -45.472 1.00 39.76  ? 38   ALA A HB2  1 
ATOM   397  H HB3  . ALA A 1 38  ? 180.584 -2.475  -45.491 1.00 39.76  ? 38   ALA A HB3  1 
ATOM   398  N N    . ARG A 1 39  ? 184.031 -0.503  -45.845 1.00 31.62  ? 39   ARG A N    1 
ATOM   399  C CA   . ARG A 1 39  ? 184.958 0.619   -45.770 1.00 31.11  ? 39   ARG A CA   1 
ATOM   400  C C    . ARG A 1 39  ? 185.701 0.819   -47.086 1.00 32.98  ? 39   ARG A C    1 
ATOM   401  O O    . ARG A 1 39  ? 186.058 1.941   -47.443 1.00 34.85  ? 39   ARG A O    1 
ATOM   402  C CB   . ARG A 1 39  ? 185.966 0.405   -44.643 1.00 33.92  ? 39   ARG A CB   1 
ATOM   403  C CG   . ARG A 1 39  ? 185.402 0.635   -43.252 1.00 40.66  ? 39   ARG A CG   1 
ATOM   404  C CD   . ARG A 1 39  ? 186.505 0.620   -42.214 1.00 44.56  ? 39   ARG A CD   1 
ATOM   405  N NE   . ARG A 1 39  ? 187.529 1.621   -42.499 1.00 52.18  ? 39   ARG A NE   1 
ATOM   406  C CZ   . ARG A 1 39  ? 188.743 1.625   -41.959 1.00 60.05  ? 39   ARG A CZ   1 
ATOM   407  N NH1  . ARG A 1 39  ? 189.090 0.675   -41.108 1.00 61.02  ? 39   ARG A NH1  1 
ATOM   408  N NH2  . ARG A 1 39  ? 189.614 2.573   -42.276 1.00 68.14  ? 39   ARG A NH2  1 
ATOM   409  H H    . ARG A 1 39  ? 184.233 -1.162  -45.331 1.00 38.14  ? 39   ARG A H    1 
ATOM   410  H HA   . ARG A 1 39  ? 184.460 1.429   -45.579 1.00 37.53  ? 39   ARG A HA   1 
ATOM   411  H HB2  . ARG A 1 39  ? 186.288 -0.509  -44.684 1.00 40.90  ? 39   ARG A HB2  1 
ATOM   412  H HB3  . ARG A 1 39  ? 186.706 1.020   -44.767 1.00 40.90  ? 39   ARG A HB3  1 
ATOM   413  H HG2  . ARG A 1 39  ? 184.965 1.500   -43.221 1.00 48.99  ? 39   ARG A HG2  1 
ATOM   414  H HG3  . ARG A 1 39  ? 184.772 -0.071  -43.040 1.00 48.99  ? 39   ARG A HG3  1 
ATOM   415  H HD2  . ARG A 1 39  ? 186.126 0.813   -41.342 1.00 53.68  ? 39   ARG A HD2  1 
ATOM   416  H HD3  . ARG A 1 39  ? 186.928 -0.254  -42.209 1.00 53.68  ? 39   ARG A HD3  1 
ATOM   417  H HE   . ARG A 1 39  ? 187.334 2.249   -43.053 1.00 62.81  ? 39   ARG A HE   1 
ATOM   418  H HH11 . ARG A 1 39  ? 188.528 0.057   -40.900 1.00 73.43  ? 39   ARG A HH11 1 
ATOM   419  H HH12 . ARG A 1 39  ? 189.876 0.676   -40.758 1.00 73.43  ? 39   ARG A HH12 1 
ATOM   420  H HH21 . ARG A 1 39  ? 189.393 3.192   -42.830 1.00 81.97  ? 39   ARG A HH21 1 
ATOM   421  H HH22 . ARG A 1 39  ? 190.399 2.571   -41.924 1.00 81.97  ? 39   ARG A HH22 1 
ATOM   422  N N    . ALA A 1 40  ? 185.940 -0.272  -47.805 1.00 33.85  ? 40   ALA A N    1 
ATOM   423  C CA   . ALA A 1 40  ? 186.641 -0.199  -49.079 1.00 29.30  ? 40   ALA A CA   1 
ATOM   424  C C    . ALA A 1 40  ? 185.764 0.468   -50.136 1.00 29.14  ? 40   ALA A C    1 
ATOM   425  O O    . ALA A 1 40  ? 186.261 1.173   -51.017 1.00 31.29  ? 40   ALA A O    1 
ATOM   426  C CB   . ALA A 1 40  ? 187.058 -1.582  -49.528 1.00 28.62  ? 40   ALA A CB   1 
ATOM   427  H H    . ALA A 1 40  ? 185.706 -1.067  -47.575 1.00 40.82  ? 40   ALA A H    1 
ATOM   428  H HA   . ALA A 1 40  ? 187.442 0.337   -48.970 1.00 35.36  ? 40   ALA A HA   1 
ATOM   429  H HB1  . ALA A 1 40  ? 186.266 -2.133  -49.628 1.00 34.54  ? 40   ALA A HB1  1 
ATOM   430  H HB2  . ALA A 1 40  ? 187.522 -1.511  -50.377 1.00 34.54  ? 40   ALA A HB2  1 
ATOM   431  H HB3  . ALA A 1 40  ? 187.647 -1.966  -48.860 1.00 34.54  ? 40   ALA A HB3  1 
ATOM   432  N N    . ALA A 1 41  ? 184.458 0.247   -50.043 1.00 27.17  ? 41   ALA A N    1 
ATOM   433  C CA   . ALA A 1 41  ? 183.511 0.874   -50.957 1.00 30.21  ? 41   ALA A CA   1 
ATOM   434  C C    . ALA A 1 41  ? 183.468 2.387   -50.749 1.00 34.56  ? 41   ALA A C    1 
ATOM   435  O O    . ALA A 1 41  ? 183.523 3.153   -51.712 1.00 31.77  ? 41   ALA A O    1 
ATOM   436  C CB   . ALA A 1 41  ? 182.125 0.279   -50.773 1.00 28.05  ? 41   ALA A CB   1 
ATOM   437  H H    . ALA A 1 41  ? 184.092 -0.265  -49.456 1.00 32.80  ? 41   ALA A H    1 
ATOM   438  H HA   . ALA A 1 41  ? 183.792 0.704   -51.870 1.00 36.45  ? 41   ALA A HA   1 
ATOM   439  H HB1  . ALA A 1 41  ? 181.837 0.429   -49.859 1.00 33.86  ? 41   ALA A HB1  1 
ATOM   440  H HB2  . ALA A 1 41  ? 181.512 0.709   -51.389 1.00 33.86  ? 41   ALA A HB2  1 
ATOM   441  H HB3  . ALA A 1 41  ? 182.165 -0.673  -50.955 1.00 33.86  ? 41   ALA A HB3  1 
ATOM   442  N N    . VAL A 1 42  ? 183.365 2.812   -49.492 1.00 29.09  ? 42   VAL A N    1 
ATOM   443  C CA   . VAL A 1 42  ? 183.353 4.234   -49.162 1.00 32.05  ? 42   VAL A CA   1 
ATOM   444  C C    . VAL A 1 42  ? 184.617 4.915   -49.666 1.00 27.35  ? 42   VAL A C    1 
ATOM   445  O O    . VAL A 1 42  ? 184.557 5.972   -50.293 1.00 39.06  ? 42   VAL A O    1 
ATOM   446  C CB   . VAL A 1 42  ? 183.244 4.458   -47.636 1.00 37.51  ? 42   VAL A CB   1 
ATOM   447  C CG1  . VAL A 1 42  ? 183.415 5.933   -47.286 1.00 39.64  ? 42   VAL A CG1  1 
ATOM   448  C CG2  . VAL A 1 42  ? 181.910 3.955   -47.119 1.00 34.63  ? 42   VAL A CG2  1 
ATOM   449  H H    . VAL A 1 42  ? 183.301 2.294   -48.809 1.00 35.11  ? 42   VAL A H    1 
ATOM   450  H HA   . VAL A 1 42  ? 182.589 4.655   -49.587 1.00 38.66  ? 42   VAL A HA   1 
ATOM   451  H HB   . VAL A 1 42  ? 183.947 3.959   -47.191 1.00 45.21  ? 42   VAL A HB   1 
ATOM   452  H HG11 . VAL A 1 42  ? 182.721 6.445   -47.730 1.00 47.76  ? 42   VAL A HG11 1 
ATOM   453  H HG12 . VAL A 1 42  ? 183.342 6.040   -46.325 1.00 47.76  ? 42   VAL A HG12 1 
ATOM   454  H HG13 . VAL A 1 42  ? 184.289 6.229   -47.587 1.00 47.76  ? 42   VAL A HG13 1 
ATOM   455  H HG21 . VAL A 1 42  ? 181.836 3.007   -47.308 1.00 41.76  ? 42   VAL A HG21 1 
ATOM   456  H HG22 . VAL A 1 42  ? 181.866 4.106   -46.161 1.00 41.76  ? 42   VAL A HG22 1 
ATOM   457  H HG23 . VAL A 1 42  ? 181.197 4.439   -47.564 1.00 41.76  ? 42   VAL A HG23 1 
ATOM   458  N N    . GLU A 1 43  ? 185.760 4.300   -49.380 1.00 32.45  ? 43   GLU A N    1 
ATOM   459  C CA   . GLU A 1 43  ? 187.056 4.857   -49.747 1.00 41.53  ? 43   GLU A CA   1 
ATOM   460  C C    . GLU A 1 43  ? 187.156 5.074   -51.251 1.00 39.09  ? 43   GLU A C    1 
ATOM   461  O O    . GLU A 1 43  ? 187.715 6.070   -51.707 1.00 44.78  ? 43   GLU A O    1 
ATOM   462  C CB   . GLU A 1 43  ? 188.177 3.927   -49.283 1.00 47.51  ? 43   GLU A CB   1 
ATOM   463  C CG   . GLU A 1 43  ? 189.573 4.497   -49.474 1.00 61.79  ? 43   GLU A CG   1 
ATOM   464  C CD   . GLU A 1 43  ? 190.649 3.619   -48.865 1.00 73.20  ? 43   GLU A CD   1 
ATOM   465  O OE1  . GLU A 1 43  ? 190.464 2.384   -48.829 1.00 76.42  ? 43   GLU A OE1  1 
ATOM   466  O OE2  . GLU A 1 43  ? 191.683 4.166   -48.423 1.00 75.74  ? 43   GLU A OE2  1 
ATOM   467  H H    . GLU A 1 43  ? 185.811 3.548   -48.967 1.00 39.14  ? 43   GLU A H    1 
ATOM   468  H HA   . GLU A 1 43  ? 187.171 5.714   -49.308 1.00 50.04  ? 43   GLU A HA   1 
ATOM   469  H HB2  . GLU A 1 43  ? 188.059 3.744   -48.338 1.00 57.21  ? 43   GLU A HB2  1 
ATOM   470  H HB3  . GLU A 1 43  ? 188.124 3.099   -49.786 1.00 57.21  ? 43   GLU A HB3  1 
ATOM   471  H HG2  . GLU A 1 43  ? 189.754 4.578   -50.424 1.00 74.34  ? 43   GLU A HG2  1 
ATOM   472  H HG3  . GLU A 1 43  ? 189.620 5.368   -49.051 1.00 74.34  ? 43   GLU A HG3  1 
ATOM   473  N N    . ALA A 1 44  ? 186.611 4.138   -52.019 1.00 35.61  ? 44   ALA A N    1 
ATOM   474  C CA   . ALA A 1 44  ? 186.659 4.228   -53.471 1.00 35.89  ? 44   ALA A CA   1 
ATOM   475  C C    . ALA A 1 44  ? 185.740 5.339   -53.962 1.00 35.27  ? 44   ALA A C    1 
ATOM   476  O O    . ALA A 1 44  ? 186.040 6.020   -54.943 1.00 45.46  ? 44   ALA A O    1 
ATOM   477  C CB   . ALA A 1 44  ? 186.271 2.906   -54.091 1.00 35.23  ? 44   ALA A CB   1 
ATOM   478  H H    . ALA A 1 44  ? 186.206 3.439   -51.723 1.00 42.93  ? 44   ALA A H    1 
ATOM   479  H HA   . ALA A 1 44  ? 187.564 4.439   -53.748 1.00 43.26  ? 44   ALA A HA   1 
ATOM   480  H HB1  . ALA A 1 44  ? 185.370 2.680   -53.813 1.00 42.48  ? 44   ALA A HB1  1 
ATOM   481  H HB2  . ALA A 1 44  ? 186.310 2.987   -55.056 1.00 42.48  ? 44   ALA A HB2  1 
ATOM   482  H HB3  . ALA A 1 44  ? 186.892 2.223   -53.791 1.00 42.48  ? 44   ALA A HB3  1 
ATOM   483  N N    . ALA A 1 45  ? 184.619 5.516   -53.274 1.00 30.66  ? 45   ALA A N    1 
ATOM   484  C CA   . ALA A 1 45  ? 183.682 6.582   -53.602 1.00 37.17  ? 45   ALA A CA   1 
ATOM   485  C C    . ALA A 1 45  ? 184.243 7.937   -53.186 1.00 35.49  ? 45   ALA A C    1 
ATOM   486  O O    . ALA A 1 45  ? 184.175 8.902   -53.946 1.00 37.01  ? 45   ALA A O    1 
ATOM   487  C CB   . ALA A 1 45  ? 182.355 6.336   -52.921 1.00 35.50  ? 45   ALA A CB   1 
ATOM   488  H H    . ALA A 1 45  ? 184.376 5.030   -52.608 1.00 36.99  ? 45   ALA A H    1 
ATOM   489  H HA   . ALA A 1 45  ? 183.535 6.595   -54.560 1.00 44.80  ? 45   ALA A HA   1 
ATOM   490  H HB1  . ALA A 1 45  ? 182.492 6.311   -51.962 1.00 42.80  ? 45   ALA A HB1  1 
ATOM   491  H HB2  . ALA A 1 45  ? 181.745 7.054   -53.151 1.00 42.80  ? 45   ALA A HB2  1 
ATOM   492  H HB3  . ALA A 1 45  ? 181.997 5.487   -53.226 1.00 42.80  ? 45   ALA A HB3  1 
ATOM   493  N N    . GLU A 1 46  ? 184.794 8.004   -51.977 1.00 37.35  ? 46   GLU A N    1 
ATOM   494  C CA   . GLU A 1 46  ? 185.367 9.244   -51.460 1.00 41.91  ? 46   GLU A CA   1 
ATOM   495  C C    . GLU A 1 46  ? 186.501 9.737   -52.348 1.00 42.60  ? 46   GLU A C    1 
ATOM   496  O O    . GLU A 1 46  ? 186.696 10.940  -52.519 1.00 50.23  ? 46   GLU A O    1 
ATOM   497  C CB   . GLU A 1 46  ? 185.883 9.047   -50.033 1.00 48.20  ? 46   GLU A CB   1 
ATOM   498  C CG   . GLU A 1 46  ? 184.886 9.425   -48.947 1.00 52.84  ? 46   GLU A CG   1 
ATOM   499  C CD   . GLU A 1 46  ? 185.558 9.722   -47.620 1.00 65.03  ? 46   GLU A CD   1 
ATOM   500  O OE1  . GLU A 1 46  ? 186.036 8.770   -46.967 1.00 67.97  ? 46   GLU A OE1  1 
ATOM   501  O OE2  . GLU A 1 46  ? 185.616 10.910  -47.232 1.00 67.75  ? 46   GLU A OE2  1 
ATOM   502  H H    . GLU A 1 46  ? 184.848 7.341   -51.433 1.00 45.02  ? 46   GLU A H    1 
ATOM   503  H HA   . GLU A 1 46  ? 184.679 9.928   -51.441 1.00 50.49  ? 46   GLU A HA   1 
ATOM   504  H HB2  . GLU A 1 46  ? 186.111 8.113   -49.911 1.00 58.04  ? 46   GLU A HB2  1 
ATOM   505  H HB3  . GLU A 1 46  ? 186.673 9.596   -49.910 1.00 58.04  ? 46   GLU A HB3  1 
ATOM   506  H HG2  . GLU A 1 46  ? 184.402 10.219  -49.224 1.00 63.60  ? 46   GLU A HG2  1 
ATOM   507  H HG3  . GLU A 1 46  ? 184.268 8.689   -48.814 1.00 63.60  ? 46   GLU A HG3  1 
ATOM   508  N N    . LYS A 1 47  ? 187.248 8.795   -52.908 1.00 44.28  ? 47   LYS A N    1 
ATOM   509  C CA   . LYS A 1 47  ? 188.355 9.113   -53.795 1.00 48.38  ? 47   LYS A CA   1 
ATOM   510  C C    . LYS A 1 47  ? 187.851 9.805   -55.055 1.00 49.99  ? 47   LYS A C    1 
ATOM   511  O O    . LYS A 1 47  ? 188.448 10.777  -55.518 1.00 57.73  ? 47   LYS A O    1 
ATOM   512  C CB   . LYS A 1 47  ? 189.090 7.830   -54.171 1.00 52.04  ? 47   LYS A CB   1 
ATOM   513  C CG   . LYS A 1 47  ? 190.515 8.033   -54.656 1.00 64.90  ? 47   LYS A CG   1 
ATOM   514  C CD   . LYS A 1 47  ? 191.273 6.712   -54.698 1.00 71.87  ? 47   LYS A CD   1 
ATOM   515  C CE   . LYS A 1 47  ? 191.616 6.208   -53.299 1.00 79.39  ? 47   LYS A CE   1 
ATOM   516  N NZ   . LYS A 1 47  ? 191.936 4.756   -53.284 1.00 81.91  ? 47   LYS A NZ   1 
ATOM   517  H H    . LYS A 1 47  ? 187.131 7.951   -52.787 1.00 53.34  ? 47   LYS A H    1 
ATOM   518  H HA   . LYS A 1 47  ? 188.976 9.705   -53.343 1.00 58.26  ? 47   LYS A HA   1 
ATOM   519  H HB2  . LYS A 1 47  ? 189.124 7.254   -53.391 1.00 62.64  ? 47   LYS A HB2  1 
ATOM   520  H HB3  . LYS A 1 47  ? 188.598 7.389   -54.881 1.00 62.64  ? 47   LYS A HB3  1 
ATOM   521  H HG2  . LYS A 1 47  ? 190.499 8.405   -55.552 1.00 78.08  ? 47   LYS A HG2  1 
ATOM   522  H HG3  . LYS A 1 47  ? 190.978 8.632   -54.050 1.00 78.08  ? 47   LYS A HG3  1 
ATOM   523  H HD2  . LYS A 1 47  ? 190.723 6.043   -55.135 1.00 86.44  ? 47   LYS A HD2  1 
ATOM   524  H HD3  . LYS A 1 47  ? 192.101 6.835   -55.187 1.00 86.44  ? 47   LYS A HD3  1 
ATOM   525  H HE2  . LYS A 1 47  ? 192.390 6.690   -52.969 1.00 95.47  ? 47   LYS A HE2  1 
ATOM   526  H HE3  . LYS A 1 47  ? 190.857 6.355   -52.713 1.00 95.47  ? 47   LYS A HE3  1 
ATOM   527  H HZ1  . LYS A 1 47  ? 192.636 4.594   -53.811 1.00 98.49  ? 47   LYS A HZ1  1 
ATOM   528  H HZ2  . LYS A 1 47  ? 192.131 4.496   -52.456 1.00 98.49  ? 47   LYS A HZ2  1 
ATOM   529  H HZ3  . LYS A 1 47  ? 191.239 4.288   -53.578 1.00 98.49  ? 47   LYS A HZ3  1 
ATOM   530  N N    . ASP A 1 48  ? 186.748 9.301   -55.601 1.00 51.65  ? 48   ASP A N    1 
ATOM   531  C CA   . ASP A 1 48  ? 186.162 9.861   -56.815 1.00 52.96  ? 48   ASP A CA   1 
ATOM   532  C C    . ASP A 1 48  ? 185.250 11.045  -56.509 1.00 51.49  ? 48   ASP A C    1 
ATOM   533  O O    . ASP A 1 48  ? 184.568 11.558  -57.393 1.00 53.98  ? 48   ASP A O    1 
ATOM   534  C CB   . ASP A 1 48  ? 185.381 8.787   -57.569 1.00 53.13  ? 48   ASP A CB   1 
ATOM   535  C CG   . ASP A 1 48  ? 186.266 7.659   -58.059 1.00 57.34  ? 48   ASP A CG   1 
ATOM   536  O OD1  . ASP A 1 48  ? 187.480 7.888   -58.242 1.00 57.49  ? 48   ASP A OD1  1 
ATOM   537  O OD2  . ASP A 1 48  ? 185.745 6.544   -58.265 1.00 59.93  ? 48   ASP A OD2  1 
ATOM   538  H H    . ASP A 1 48  ? 186.316 8.628   -55.285 1.00 62.18  ? 48   ASP A H    1 
ATOM   539  H HA   . ASP A 1 48  ? 186.875 10.174  -57.394 1.00 63.76  ? 48   ASP A HA   1 
ATOM   540  H HB2  . ASP A 1 48  ? 184.711 8.408   -56.978 1.00 63.95  ? 48   ASP A HB2  1 
ATOM   541  H HB3  . ASP A 1 48  ? 184.953 9.190   -58.341 1.00 63.95  ? 48   ASP A HB3  1 
ATOM   542  N N    . GLY A 1 49  ? 185.239 11.476  -55.253 1.00 46.33  ? 49   GLY A N    1 
ATOM   543  C CA   . GLY A 1 49  ? 184.466 12.637  -54.857 1.00 43.18  ? 49   GLY A CA   1 
ATOM   544  C C    . GLY A 1 49  ? 182.985 12.361  -54.681 1.00 43.06  ? 49   GLY A C    1 
ATOM   545  O O    . GLY A 1 49  ? 182.180 13.293  -54.644 1.00 48.42  ? 49   GLY A O    1 
ATOM   546  H H    . GLY A 1 49  ? 185.676 11.108  -54.609 1.00 55.80  ? 49   GLY A H    1 
ATOM   547  H HA2  . GLY A 1 49  ? 184.812 12.978  -54.017 1.00 52.02  ? 49   GLY A HA2  1 
ATOM   548  H HA3  . GLY A 1 49  ? 184.566 13.330  -55.529 1.00 52.02  ? 49   GLY A HA3  1 
ATOM   549  N N    . ARG A 1 50  ? 182.620 11.087  -54.573 1.00 37.14  ? 50   ARG A N    1 
ATOM   550  C CA   . ARG A 1 50  ? 181.223 10.708  -54.392 1.00 38.68  ? 50   ARG A CA   1 
ATOM   551  C C    . ARG A 1 50  ? 180.869 10.555  -52.922 1.00 43.22  ? 50   ARG A C    1 
ATOM   552  O O    . ARG A 1 50  ? 181.727 10.264  -52.086 1.00 39.34  ? 50   ARG A O    1 
ATOM   553  C CB   . ARG A 1 50  ? 180.906 9.412   -55.137 1.00 41.00  ? 50   ARG A CB   1 
ATOM   554  C CG   . ARG A 1 50  ? 180.361 9.638   -56.538 1.00 45.90  ? 50   ARG A CG   1 
ATOM   555  C CD   . ARG A 1 50  ? 181.399 10.288  -57.430 1.00 51.36  ? 50   ARG A CD   1 
ATOM   556  N NE   . ARG A 1 50  ? 180.843 10.739  -58.705 1.00 58.23  ? 50   ARG A NE   1 
ATOM   557  C CZ   . ARG A 1 50  ? 180.895 10.056  -59.845 1.00 61.50  ? 50   ARG A CZ   1 
ATOM   558  N NH1  . ARG A 1 50  ? 181.475 8.862   -59.903 1.00 56.83  ? 50   ARG A NH1  1 
ATOM   559  N NH2  . ARG A 1 50  ? 180.362 10.575  -60.942 1.00 66.45  ? 50   ARG A NH2  1 
ATOM   560  H H    . ARG A 1 50  ? 183.164 10.421  -54.602 1.00 44.76  ? 50   ARG A H    1 
ATOM   561  H HA   . ARG A 1 50  ? 180.660 11.407  -54.761 1.00 46.62  ? 50   ARG A HA   1 
ATOM   562  H HB2  . ARG A 1 50  ? 181.718 8.888   -55.215 1.00 49.40  ? 50   ARG A HB2  1 
ATOM   563  H HB3  . ARG A 1 50  ? 180.240 8.916   -54.635 1.00 49.40  ? 50   ARG A HB3  1 
ATOM   564  H HG2  . ARG A 1 50  ? 180.114 8.785   -56.928 1.00 55.28  ? 50   ARG A HG2  1 
ATOM   565  H HG3  . ARG A 1 50  ? 179.588 10.223  -56.491 1.00 55.28  ? 50   ARG A HG3  1 
ATOM   566  H HD2  . ARG A 1 50  ? 181.769 11.060  -56.974 1.00 61.83  ? 50   ARG A HD2  1 
ATOM   567  H HD3  . ARG A 1 50  ? 182.101 9.646   -57.619 1.00 61.83  ? 50   ARG A HD3  1 
ATOM   568  H HE   . ARG A 1 50  ? 180.452 11.505  -58.718 1.00 70.08  ? 50   ARG A HE   1 
ATOM   569  H HH11 . ARG A 1 50  ? 181.826 8.520   -59.197 1.00 68.40  ? 50   ARG A HH11 1 
ATOM   570  H HH12 . ARG A 1 50  ? 181.500 8.432   -60.648 1.00 68.40  ? 50   ARG A HH12 1 
ATOM   571  H HH21 . ARG A 1 50  ? 179.983 11.347  -60.913 1.00 79.94  ? 50   ARG A HH21 1 
ATOM   572  H HH22 . ARG A 1 50  ? 180.389 10.137  -61.682 1.00 79.94  ? 50   ARG A HH22 1 
ATOM   573  N N    . HIS A 1 51  ? 179.588 10.751  -52.627 1.00 40.31  ? 51   HIS A N    1 
ATOM   574  C CA   . HIS A 1 51  ? 179.072 10.669  -51.271 1.00 44.02  ? 51   HIS A CA   1 
ATOM   575  C C    . HIS A 1 51  ? 177.991 9.601   -51.231 1.00 42.10  ? 51   HIS A C    1 
ATOM   576  O O    . HIS A 1 51  ? 176.919 9.767   -51.817 1.00 44.26  ? 51   HIS A O    1 
ATOM   577  C CB   . HIS A 1 51  ? 178.513 12.026  -50.854 1.00 47.79  ? 51   HIS A CB   1 
ATOM   578  C CG   . HIS A 1 51  ? 179.424 13.170  -51.173 1.00 55.07  ? 51   HIS A CG   1 
ATOM   579  N ND1  . HIS A 1 51  ? 180.516 13.492  -50.394 1.00 62.05  ? 51   HIS A ND1  1 
ATOM   580  C CD2  . HIS A 1 51  ? 179.415 14.061  -52.192 1.00 55.63  ? 51   HIS A CD2  1 
ATOM   581  C CE1  . HIS A 1 51  ? 181.135 14.534  -50.917 1.00 63.93  ? 51   HIS A CE1  1 
ATOM   582  N NE2  . HIS A 1 51  ? 180.487 14.900  -52.010 1.00 61.06  ? 51   HIS A NE2  1 
ATOM   583  H H    . HIS A 1 51  ? 178.986 10.937  -53.212 1.00 48.58  ? 51   HIS A H    1 
ATOM   584  H HA   . HIS A 1 51  ? 179.784 10.421  -50.661 1.00 53.02  ? 51   HIS A HA   1 
ATOM   585  H HB2  . HIS A 1 51  ? 177.674 12.176  -51.318 1.00 57.55  ? 51   HIS A HB2  1 
ATOM   586  H HB3  . HIS A 1 51  ? 178.363 12.023  -49.896 1.00 57.55  ? 51   HIS A HB3  1 
ATOM   587  H HD1  . HIS A 1 51  ? 180.755 13.080  -49.679 1.00 74.67  ? 51   HIS A HD1  1 
ATOM   588  H HD2  . HIS A 1 51  ? 178.796 14.099  -52.885 1.00 66.96  ? 51   HIS A HD2  1 
ATOM   589  H HE1  . HIS A 1 51  ? 181.898 14.942  -50.575 1.00 76.91  ? 51   HIS A HE1  1 
ATOM   590  H HE2  . HIS A 1 51  ? 180.701 15.556  -52.523 1.00 73.47  ? 51   HIS A HE2  1 
ATOM   591  N N    . VAL A 1 52  ? 178.282 8.503   -50.540 1.00 36.12  ? 52   VAL A N    1 
ATOM   592  C CA   . VAL A 1 52  ? 177.432 7.320   -50.590 1.00 29.99  ? 52   VAL A CA   1 
ATOM   593  C C    . VAL A 1 52  ? 177.218 6.683   -49.227 1.00 31.41  ? 52   VAL A C    1 
ATOM   594  O O    . VAL A 1 52  ? 178.011 6.876   -48.304 1.00 28.35  ? 52   VAL A O    1 
ATOM   595  C CB   . VAL A 1 52  ? 178.043 6.246   -51.518 1.00 32.35  ? 52   VAL A CB   1 
ATOM   596  C CG1  . VAL A 1 52  ? 178.199 6.784   -52.927 1.00 24.57  ? 52   VAL A CG1  1 
ATOM   597  C CG2  . VAL A 1 52  ? 179.390 5.771   -50.984 1.00 30.15  ? 52   VAL A CG2  1 
ATOM   598  H H    . VAL A 1 52  ? 178.970 8.418   -50.031 1.00 43.54  ? 52   VAL A H    1 
ATOM   599  H HA   . VAL A 1 52  ? 176.565 7.569   -50.947 1.00 36.18  ? 52   VAL A HA   1 
ATOM   600  H HB   . VAL A 1 52  ? 177.447 5.481   -51.552 1.00 39.02  ? 52   VAL A HB   1 
ATOM   601  H HG11 . VAL A 1 52  ? 178.784 7.557   -52.906 1.00 29.68  ? 52   VAL A HG11 1 
ATOM   602  H HG12 . VAL A 1 52  ? 178.583 6.092   -53.488 1.00 29.68  ? 52   VAL A HG12 1 
ATOM   603  H HG13 . VAL A 1 52  ? 177.326 7.038   -53.265 1.00 29.68  ? 52   VAL A HG13 1 
ATOM   604  H HG21 . VAL A 1 52  ? 179.263 5.392   -50.101 1.00 36.38  ? 52   VAL A HG21 1 
ATOM   605  H HG22 . VAL A 1 52  ? 179.748 5.099   -51.585 1.00 36.38  ? 52   VAL A HG22 1 
ATOM   606  H HG23 . VAL A 1 52  ? 179.994 6.528   -50.936 1.00 36.38  ? 52   VAL A HG23 1 
ATOM   607  N N    . SER A 1 53  ? 176.132 5.924   -49.121 1.00 28.64  ? 53   SER A N    1 
ATOM   608  C CA   . SER A 1 53  ? 175.904 5.039   -47.989 1.00 30.64  ? 53   SER A CA   1 
ATOM   609  C C    . SER A 1 53  ? 176.181 3.614   -48.444 1.00 31.07  ? 53   SER A C    1 
ATOM   610  O O    . SER A 1 53  ? 175.933 3.265   -49.602 1.00 30.32  ? 53   SER A O    1 
ATOM   611  C CB   . SER A 1 53  ? 174.466 5.158   -47.485 1.00 29.60  ? 53   SER A CB   1 
ATOM   612  O OG   . SER A 1 53  ? 174.280 6.351   -46.746 1.00 35.98  ? 53   SER A OG   1 
ATOM   613  H H    . SER A 1 53  ? 175.500 5.905   -49.704 1.00 34.56  ? 53   SER A H    1 
ATOM   614  H HA   . SER A 1 53  ? 176.511 5.263   -47.266 1.00 36.97  ? 53   SER A HA   1 
ATOM   615  H HB2  . SER A 1 53  ? 173.865 5.162   -48.247 1.00 35.72  ? 53   SER A HB2  1 
ATOM   616  H HB3  . SER A 1 53  ? 174.269 4.399   -46.913 1.00 35.72  ? 53   SER A HB3  1 
ATOM   617  H HG   . SER A 1 53  ? 173.486 6.401   -46.477 1.00 43.37  ? 53   SER A HG   1 
ATOM   618  N N    . VAL A 1 54  ? 176.698 2.794   -47.535 1.00 24.30  ? 54   VAL A N    1 
ATOM   619  C CA   . VAL A 1 54  ? 177.065 1.422   -47.862 1.00 25.33  ? 54   VAL A CA   1 
ATOM   620  C C    . VAL A 1 54  ? 176.450 0.466   -46.855 1.00 29.56  ? 54   VAL A C    1 
ATOM   621  O O    . VAL A 1 54  ? 176.340 0.787   -45.670 1.00 27.93  ? 54   VAL A O    1 
ATOM   622  C CB   . VAL A 1 54  ? 178.593 1.236   -47.866 1.00 27.32  ? 54   VAL A CB   1 
ATOM   623  C CG1  . VAL A 1 54  ? 178.963 -0.172  -48.316 1.00 31.49  ? 54   VAL A CG1  1 
ATOM   624  C CG2  . VAL A 1 54  ? 179.249 2.264   -48.772 1.00 30.29  ? 54   VAL A CG2  1 
ATOM   625  H H    . VAL A 1 54  ? 176.847 3.011   -46.716 1.00 29.35  ? 54   VAL A H    1 
ATOM   626  H HA   . VAL A 1 54  ? 176.726 1.199   -48.743 1.00 30.59  ? 54   VAL A HA   1 
ATOM   627  H HB   . VAL A 1 54  ? 178.932 1.366   -46.967 1.00 32.99  ? 54   VAL A HB   1 
ATOM   628  H HG11 . VAL A 1 54  ? 178.623 -0.316  -49.213 1.00 37.99  ? 54   VAL A HG11 1 
ATOM   629  H HG12 . VAL A 1 54  ? 179.929 -0.261  -48.309 1.00 37.99  ? 54   VAL A HG12 1 
ATOM   630  H HG13 . VAL A 1 54  ? 178.567 -0.813  -47.705 1.00 37.99  ? 54   VAL A HG13 1 
ATOM   631  H HG21 . VAL A 1 54  ? 179.036 3.153   -48.446 1.00 36.55  ? 54   VAL A HG21 1 
ATOM   632  H HG22 . VAL A 1 54  ? 180.209 2.128   -48.759 1.00 36.55  ? 54   VAL A HG22 1 
ATOM   633  H HG23 . VAL A 1 54  ? 178.911 2.151   -49.674 1.00 36.55  ? 54   VAL A HG23 1 
ATOM   634  N N    . ALA A 1 55  ? 176.048 -0.707  -47.334 1.00 29.79  ? 55   ALA A N    1 
ATOM   635  C CA   . ALA A 1 55  ? 175.460 -1.725  -46.475 1.00 30.12  ? 55   ALA A CA   1 
ATOM   636  C C    . ALA A 1 55  ? 175.912 -3.125  -46.876 1.00 31.02  ? 55   ALA A C    1 
ATOM   637  O O    . ALA A 1 55  ? 176.045 -3.435  -48.061 1.00 25.03  ? 55   ALA A O    1 
ATOM   638  C CB   . ALA A 1 55  ? 173.952 -1.637  -46.515 1.00 24.50  ? 55   ALA A CB   1 
ATOM   639  H H    . ALA A 1 55  ? 176.106 -0.938  -48.161 1.00 35.94  ? 55   ALA A H    1 
ATOM   640  H HA   . ALA A 1 55  ? 175.745 -1.569  -45.561 1.00 36.34  ? 55   ALA A HA   1 
ATOM   641  H HB1  . ALA A 1 55  ? 173.653 -1.775  -47.428 1.00 29.60  ? 55   ALA A HB1  1 
ATOM   642  H HB2  . ALA A 1 55  ? 173.581 -2.322  -45.937 1.00 29.60  ? 55   ALA A HB2  1 
ATOM   643  H HB3  . ALA A 1 55  ? 173.679 -0.759  -46.206 1.00 29.60  ? 55   ALA A HB3  1 
ATOM   644  N N    . VAL A 1 56  ? 176.153 -3.958  -45.869 1.00 29.21  ? 56   VAL A N    1 
ATOM   645  C CA   . VAL A 1 56  ? 176.436 -5.369  -46.076 1.00 27.63  ? 56   VAL A CA   1 
ATOM   646  C C    . VAL A 1 56  ? 175.347 -6.176  -45.385 1.00 30.73  ? 56   VAL A C    1 
ATOM   647  O O    . VAL A 1 56  ? 175.160 -6.063  -44.174 1.00 27.77  ? 56   VAL A O    1 
ATOM   648  C CB   . VAL A 1 56  ? 177.800 -5.772  -45.494 1.00 26.16  ? 56   VAL A CB   1 
ATOM   649  C CG1  . VAL A 1 56  ? 178.097 -7.234  -45.798 1.00 25.90  ? 56   VAL A CG1  1 
ATOM   650  C CG2  . VAL A 1 56  ? 178.896 -4.891  -46.051 1.00 29.99  ? 56   VAL A CG2  1 
ATOM   651  H H    . VAL A 1 56  ? 176.158 -3.722  -45.042 1.00 35.25  ? 56   VAL A H    1 
ATOM   652  H HA   . VAL A 1 56  ? 176.426 -5.573  -47.024 1.00 33.35  ? 56   VAL A HA   1 
ATOM   653  H HB   . VAL A 1 56  ? 177.781 -5.661  -44.531 1.00 31.59  ? 56   VAL A HB   1 
ATOM   654  H HG11 . VAL A 1 56  ? 178.110 -7.359  -46.760 1.00 31.28  ? 56   VAL A HG11 1 
ATOM   655  H HG12 . VAL A 1 56  ? 178.961 -7.465  -45.422 1.00 31.28  ? 56   VAL A HG12 1 
ATOM   656  H HG13 . VAL A 1 56  ? 177.405 -7.785  -45.402 1.00 31.28  ? 56   VAL A HG13 1 
ATOM   657  H HG21 . VAL A 1 56  ? 178.709 -3.969  -45.817 1.00 36.18  ? 56   VAL A HG21 1 
ATOM   658  H HG22 . VAL A 1 56  ? 179.745 -5.165  -45.670 1.00 36.18  ? 56   VAL A HG22 1 
ATOM   659  H HG23 . VAL A 1 56  ? 178.920 -4.990  -47.016 1.00 36.18  ? 56   VAL A HG23 1 
ATOM   660  N N    . VAL A 1 57  ? 174.633 -6.985  -46.162 1.00 32.61  ? 57   VAL A N    1 
ATOM   661  C CA   . VAL A 1 57  ? 173.531 -7.784  -45.641 1.00 29.49  ? 57   VAL A CA   1 
ATOM   662  C C    . VAL A 1 57  ? 173.838 -9.264  -45.794 1.00 33.46  ? 57   VAL A C    1 
ATOM   663  O O    . VAL A 1 57  ? 174.246 -9.721  -46.860 1.00 31.60  ? 57   VAL A O    1 
ATOM   664  C CB   . VAL A 1 57  ? 172.213 -7.458  -46.368 1.00 28.98  ? 57   VAL A CB   1 
ATOM   665  C CG1  . VAL A 1 57  ? 171.088 -8.365  -45.887 1.00 27.92  ? 57   VAL A CG1  1 
ATOM   666  C CG2  . VAL A 1 57  ? 171.841 -6.002  -46.147 1.00 26.75  ? 57   VAL A CG2  1 
ATOM   667  H H    . VAL A 1 57  ? 174.770 -7.090  -47.004 1.00 39.34  ? 57   VAL A H    1 
ATOM   668  H HA   . VAL A 1 57  ? 173.414 -7.593  -44.698 1.00 35.58  ? 57   VAL A HA   1 
ATOM   669  H HB   . VAL A 1 57  ? 172.330 -7.599  -47.320 1.00 34.98  ? 57   VAL A HB   1 
ATOM   670  H HG11 . VAL A 1 57  ? 170.963 -8.235  -44.933 1.00 33.70  ? 57   VAL A HG11 1 
ATOM   671  H HG12 . VAL A 1 57  ? 170.273 -8.136  -46.361 1.00 33.70  ? 57   VAL A HG12 1 
ATOM   672  H HG13 . VAL A 1 57  ? 171.327 -9.287  -46.067 1.00 33.70  ? 57   VAL A HG13 1 
ATOM   673  H HG21 . VAL A 1 57  ? 172.549 -5.439  -46.496 1.00 32.30  ? 57   VAL A HG21 1 
ATOM   674  H HG22 . VAL A 1 57  ? 171.010 -5.815  -46.611 1.00 32.30  ? 57   VAL A HG22 1 
ATOM   675  H HG23 . VAL A 1 57  ? 171.732 -5.845  -45.196 1.00 32.30  ? 57   VAL A HG23 1 
ATOM   676  N N    . ASP A 1 58  ? 173.628 -10.007 -44.716 1.00 34.25  ? 58   ASP A N    1 
ATOM   677  C CA   . ASP A 1 58  ? 173.882 -11.438 -44.702 1.00 29.96  ? 58   ASP A CA   1 
ATOM   678  C C    . ASP A 1 58  ? 172.820 -12.177 -45.501 1.00 23.87  ? 58   ASP A C    1 
ATOM   679  O O    . ASP A 1 58  ? 171.702 -11.690 -45.668 1.00 26.10  ? 58   ASP A O    1 
ATOM   680  C CB   . ASP A 1 58  ? 173.887 -11.943 -43.262 1.00 29.91  ? 58   ASP A CB   1 
ATOM   681  C CG   . ASP A 1 58  ? 174.364 -13.371 -43.144 1.00 30.35  ? 58   ASP A CG   1 
ATOM   682  O OD1  . ASP A 1 58  ? 173.578 -14.294 -43.447 1.00 28.58  ? 58   ASP A OD1  1 
ATOM   683  O OD2  . ASP A 1 58  ? 175.528 -13.572 -42.741 1.00 26.28  ? 58   ASP A OD2  1 
ATOM   684  H H    . ASP A 1 58  ? 173.333 -9.700  -43.968 1.00 41.30  ? 58   ASP A H    1 
ATOM   685  H HA   . ASP A 1 58  ? 174.749 -11.619 -45.097 1.00 36.15  ? 58   ASP A HA   1 
ATOM   686  H HB2  . ASP A 1 58  ? 174.479 -11.384 -42.733 1.00 36.09  ? 58   ASP A HB2  1 
ATOM   687  H HB3  . ASP A 1 58  ? 172.985 -11.897 -42.908 1.00 36.09  ? 58   ASP A HB3  1 
ATOM   688  N N    . ARG A 1 59  ? 173.176 -13.359 -45.990 1.00 26.18  ? 59   ARG A N    1 
ATOM   689  C CA   . ARG A 1 59  ? 172.247 -14.207 -46.729 1.00 27.93  ? 59   ARG A CA   1 
ATOM   690  C C    . ARG A 1 59  ? 171.012 -14.539 -45.891 1.00 34.54  ? 59   ARG A C    1 
ATOM   691  O O    . ARG A 1 59  ? 169.959 -14.871 -46.437 1.00 33.00  ? 59   ARG A O    1 
ATOM   692  C CB   . ARG A 1 59  ? 172.961 -15.488 -47.178 1.00 31.47  ? 59   ARG A CB   1 
ATOM   693  C CG   . ARG A 1 59  ? 172.071 -16.583 -47.759 1.00 31.95  ? 59   ARG A CG   1 
ATOM   694  C CD   . ARG A 1 59  ? 171.371 -16.168 -49.044 1.00 32.94  ? 59   ARG A CD   1 
ATOM   695  N NE   . ARG A 1 59  ? 170.708 -17.312 -49.669 1.00 33.03  ? 59   ARG A NE   1 
ATOM   696  C CZ   . ARG A 1 59  ? 170.101 -17.285 -50.851 1.00 31.70  ? 59   ARG A CZ   1 
ATOM   697  N NH1  . ARG A 1 59  ? 170.062 -16.169 -51.565 1.00 36.24  ? 59   ARG A NH1  1 
ATOM   698  N NH2  . ARG A 1 59  ? 169.533 -18.384 -51.321 1.00 32.45  ? 59   ARG A NH2  1 
ATOM   699  H H    . ARG A 1 59  ? 173.962 -13.698 -45.906 1.00 31.62  ? 59   ARG A H    1 
ATOM   700  H HA   . ARG A 1 59  ? 171.951 -13.735 -47.523 1.00 33.72  ? 59   ARG A HA   1 
ATOM   701  H HB2  . ARG A 1 59  ? 173.610 -15.252 -47.859 1.00 37.96  ? 59   ARG A HB2  1 
ATOM   702  H HB3  . ARG A 1 59  ? 173.420 -15.865 -46.412 1.00 37.96  ? 59   ARG A HB3  1 
ATOM   703  H HG2  . ARG A 1 59  ? 172.616 -17.361 -47.954 1.00 38.54  ? 59   ARG A HG2  1 
ATOM   704  H HG3  . ARG A 1 59  ? 171.389 -16.812 -47.108 1.00 38.54  ? 59   ARG A HG3  1 
ATOM   705  H HD2  . ARG A 1 59  ? 170.700 -15.497 -48.844 1.00 39.72  ? 59   ARG A HD2  1 
ATOM   706  H HD3  . ARG A 1 59  ? 172.026 -15.816 -49.668 1.00 39.72  ? 59   ARG A HD3  1 
ATOM   707  H HE   . ARG A 1 59  ? 170.710 -18.057 -49.239 1.00 39.83  ? 59   ARG A HE   1 
ATOM   708  H HH11 . ARG A 1 59  ? 170.431 -15.453 -51.264 1.00 43.68  ? 59   ARG A HH11 1 
ATOM   709  H HH12 . ARG A 1 59  ? 169.668 -16.161 -52.329 1.00 43.68  ? 59   ARG A HH12 1 
ATOM   710  H HH21 . ARG A 1 59  ? 169.556 -19.110 -50.861 1.00 39.14  ? 59   ARG A HH21 1 
ATOM   711  H HH22 . ARG A 1 59  ? 169.139 -18.372 -52.085 1.00 39.14  ? 59   ARG A HH22 1 
ATOM   712  N N    . ASN A 1 60  ? 171.133 -14.441 -44.569 1.00 31.43  ? 60   ASN A N    1 
ATOM   713  C CA   . ASN A 1 60  ? 170.003 -14.730 -43.689 1.00 27.44  ? 60   ASN A CA   1 
ATOM   714  C C    . ASN A 1 60  ? 169.028 -13.558 -43.590 1.00 25.45  ? 60   ASN A C    1 
ATOM   715  O O    . ASN A 1 60  ? 167.978 -13.669 -42.958 1.00 32.15  ? 60   ASN A O    1 
ATOM   716  C CB   . ASN A 1 60  ? 170.483 -15.151 -42.295 1.00 27.27  ? 60   ASN A CB   1 
ATOM   717  C CG   . ASN A 1 60  ? 171.257 -14.060 -41.577 1.00 30.87  ? 60   ASN A CG   1 
ATOM   718  O OD1  . ASN A 1 60  ? 171.073 -12.870 -41.829 1.00 29.97  ? 60   ASN A OD1  1 
ATOM   719  N ND2  . ASN A 1 60  ? 172.130 -14.470 -40.666 1.00 34.14  ? 60   ASN A ND2  1 
ATOM   720  H H    . ASN A 1 60  ? 171.853 -14.210 -44.159 1.00 37.91  ? 60   ASN A H    1 
ATOM   721  H HA   . ASN A 1 60  ? 169.513 -15.479 -44.063 1.00 33.12  ? 60   ASN A HA   1 
ATOM   722  H HB2  . ASN A 1 60  ? 169.712 -15.377 -41.752 1.00 32.92  ? 60   ASN A HB2  1 
ATOM   723  H HB3  . ASN A 1 60  ? 171.064 -15.922 -42.382 1.00 32.92  ? 60   ASN A HB3  1 
ATOM   724  H HD21 . ASN A 1 60  ? 172.229 -15.310 -40.513 1.00 41.17  ? 60   ASN A HD21 1 
ATOM   725  H HD22 . ASN A 1 60  ? 172.596 -13.895 -40.228 1.00 41.17  ? 60   ASN A HD22 1 
ATOM   726  N N    . GLY A 1 61  ? 169.393 -12.436 -44.205 1.00 27.34  ? 61   GLY A N    1 
ATOM   727  C CA   . GLY A 1 61  ? 168.532 -11.267 -44.255 1.00 28.67  ? 61   GLY A CA   1 
ATOM   728  C C    . GLY A 1 61  ? 168.973 -10.150 -43.329 1.00 31.20  ? 61   GLY A C    1 
ATOM   729  O O    . GLY A 1 61  ? 168.545 -9.005  -43.478 1.00 37.12  ? 61   GLY A O    1 
ATOM   730  H H    . GLY A 1 61  ? 170.146 -12.329 -44.607 1.00 33.00  ? 61   GLY A H    1 
ATOM   731  H HA2  . GLY A 1 61  ? 168.515 -10.921 -45.161 1.00 34.60  ? 61   GLY A HA2  1 
ATOM   732  H HA3  . GLY A 1 61  ? 167.629 -11.524 -44.011 1.00 34.60  ? 61   GLY A HA3  1 
ATOM   733  N N    . ASN A 1 62  ? 169.835 -10.476 -42.372 1.00 30.37  ? 62   ASN A N    1 
ATOM   734  C CA   . ASN A 1 62  ? 170.276 -9.500  -41.386 1.00 32.13  ? 62   ASN A CA   1 
ATOM   735  C C    . ASN A 1 62  ? 171.352 -8.567  -41.914 1.00 30.38  ? 62   ASN A C    1 
ATOM   736  O O    . ASN A 1 62  ? 172.301 -8.997  -42.566 1.00 32.88  ? 62   ASN A O    1 
ATOM   737  C CB   . ASN A 1 62  ? 170.792 -10.202 -40.131 1.00 32.31  ? 62   ASN A CB   1 
ATOM   738  C CG   . ASN A 1 62  ? 169.697 -10.914 -39.377 1.00 32.44  ? 62   ASN A CG   1 
ATOM   739  O OD1  . ASN A 1 62  ? 168.526 -10.550 -39.473 1.00 34.85  ? 62   ASN A OD1  1 
ATOM   740  N ND2  . ASN A 1 62  ? 170.070 -11.937 -38.617 1.00 35.56  ? 62   ASN A ND2  1 
ATOM   741  H H    . ASN A 1 62  ? 170.179 -11.258 -42.273 1.00 36.65  ? 62   ASN A H    1 
ATOM   742  H HA   . ASN A 1 62  ? 169.516 -8.955  -41.127 1.00 38.75  ? 62   ASN A HA   1 
ATOM   743  H HB2  . ASN A 1 62  ? 171.458 -10.860 -40.387 1.00 38.97  ? 62   ASN A HB2  1 
ATOM   744  H HB3  . ASN A 1 62  ? 171.187 -9.543  -39.539 1.00 38.97  ? 62   ASN A HB3  1 
ATOM   745  H HD21 . ASN A 1 62  ? 170.899 -12.161 -38.575 1.00 42.87  ? 62   ASN A HD21 1 
ATOM   746  H HD22 . ASN A 1 62  ? 169.482 -12.375 -38.167 1.00 42.87  ? 62   ASN A HD22 1 
ATOM   747  N N    . THR A 1 63  ? 171.193 -7.283  -41.617 1.00 30.57  ? 63   THR A N    1 
ATOM   748  C CA   . THR A 1 63  ? 172.185 -6.283  -41.977 1.00 28.65  ? 63   THR A CA   1 
ATOM   749  C C    . THR A 1 63  ? 173.333 -6.370  -40.983 1.00 30.27  ? 63   THR A C    1 
ATOM   750  O O    . THR A 1 63  ? 173.117 -6.321  -39.770 1.00 31.39  ? 63   THR A O    1 
ATOM   751  C CB   . THR A 1 63  ? 171.575 -4.870  -41.962 1.00 31.64  ? 63   THR A CB   1 
ATOM   752  O OG1  . THR A 1 63  ? 170.406 -4.848  -42.792 1.00 31.67  ? 63   THR A OG1  1 
ATOM   753  C CG2  . THR A 1 63  ? 172.571 -3.842  -42.469 1.00 31.16  ? 63   THR A CG2  1 
ATOM   754  H H    . THR A 1 63  ? 170.510 -6.964  -41.203 1.00 36.88  ? 63   THR A H    1 
ATOM   755  H HA   . THR A 1 63  ? 172.527 -6.466  -42.866 1.00 34.58  ? 63   THR A HA   1 
ATOM   756  H HB   . THR A 1 63  ? 171.328 -4.635  -41.053 1.00 38.16  ? 63   THR A HB   1 
ATOM   757  H HG1  . THR A 1 63  ? 170.066 -4.080  -42.790 1.00 38.21  ? 63   THR A HG1  1 
ATOM   758  H HG21 . THR A 1 63  ? 172.831 -4.054  -43.379 1.00 37.59  ? 63   THR A HG21 1 
ATOM   759  H HG22 . THR A 1 63  ? 172.172 -2.958  -42.453 1.00 37.59  ? 63   THR A HG22 1 
ATOM   760  H HG23 . THR A 1 63  ? 173.361 -3.841  -41.907 1.00 37.59  ? 63   THR A HG23 1 
ATOM   761  N N    . LEU A 1 64  ? 174.549 -6.509  -41.503 1.00 29.29  ? 64   LEU A N    1 
ATOM   762  C CA   . LEU A 1 64  ? 175.730 -6.717  -40.674 1.00 27.65  ? 64   LEU A CA   1 
ATOM   763  C C    . LEU A 1 64  ? 176.492 -5.419  -40.464 1.00 23.75  ? 64   LEU A C    1 
ATOM   764  O O    . LEU A 1 64  ? 177.062 -5.183  -39.400 1.00 23.78  ? 64   LEU A O    1 
ATOM   765  C CB   . LEU A 1 64  ? 176.659 -7.736  -41.335 1.00 27.11  ? 64   LEU A CB   1 
ATOM   766  C CG   . LEU A 1 64  ? 176.086 -9.126  -41.613 1.00 28.98  ? 64   LEU A CG   1 
ATOM   767  C CD1  . LEU A 1 64  ? 177.161 -10.009 -42.217 1.00 30.16  ? 64   LEU A CD1  1 
ATOM   768  C CD2  . LEU A 1 64  ? 175.535 -9.754  -40.348 1.00 30.99  ? 64   LEU A CD2  1 
ATOM   769  H H    . LEU A 1 64  ? 174.717 -6.485  -42.346 1.00 35.35  ? 64   LEU A H    1 
ATOM   770  H HA   . LEU A 1 64  ? 175.462 -7.060  -39.807 1.00 33.38  ? 64   LEU A HA   1 
ATOM   771  H HB2  . LEU A 1 64  ? 176.949 -7.372  -42.185 1.00 32.74  ? 64   LEU A HB2  1 
ATOM   772  H HB3  . LEU A 1 64  ? 177.431 -7.856  -40.760 1.00 32.74  ? 64   LEU A HB3  1 
ATOM   773  H HG   . LEU A 1 64  ? 175.362 -9.050  -42.254 1.00 34.98  ? 64   LEU A HG   1 
ATOM   774  H HD11 . LEU A 1 64  ? 177.899 -10.080 -41.592 1.00 36.39  ? 64   LEU A HD11 1 
ATOM   775  H HD12 . LEU A 1 64  ? 176.788 -10.887 -42.390 1.00 36.39  ? 64   LEU A HD12 1 
ATOM   776  H HD13 . LEU A 1 64  ? 177.468 -9.610  -43.047 1.00 36.39  ? 64   LEU A HD13 1 
ATOM   777  H HD21 . LEU A 1 64  ? 174.829 -9.188  -39.997 1.00 37.39  ? 64   LEU A HD21 1 
ATOM   778  H HD22 . LEU A 1 64  ? 175.181 -10.631 -40.560 1.00 37.39  ? 64   LEU A HD22 1 
ATOM   779  H HD23 . LEU A 1 64  ? 176.250 -9.833  -39.698 1.00 37.39  ? 64   LEU A HD23 1 
ATOM   780  N N    . VAL A 1 65  ? 176.511 -4.588  -41.498 1.00 25.48  ? 65   VAL A N    1 
ATOM   781  C CA   . VAL A 1 65  ? 177.249 -3.338  -41.465 1.00 27.68  ? 65   VAL A CA   1 
ATOM   782  C C    . VAL A 1 65  ? 176.504 -2.286  -42.263 1.00 31.97  ? 65   VAL A C    1 
ATOM   783  O O    . VAL A 1 65  ? 175.969 -2.577  -43.332 1.00 33.46  ? 65   VAL A O    1 
ATOM   784  C CB   . VAL A 1 65  ? 178.659 -3.498  -42.078 1.00 28.16  ? 65   VAL A CB   1 
ATOM   785  C CG1  . VAL A 1 65  ? 179.395 -2.158  -42.118 1.00 26.18  ? 65   VAL A CG1  1 
ATOM   786  C CG2  . VAL A 1 65  ? 179.470 -4.518  -41.301 1.00 29.43  ? 65   VAL A CG2  1 
ATOM   787  H H    . VAL A 1 65  ? 176.098 -4.729  -42.240 1.00 30.77  ? 65   VAL A H    1 
ATOM   788  H HA   . VAL A 1 65  ? 177.338 -3.032  -40.549 1.00 33.42  ? 65   VAL A HA   1 
ATOM   789  H HB   . VAL A 1 65  ? 178.571 -3.818  -42.990 1.00 34.00  ? 65   VAL A HB   1 
ATOM   790  H HG11 . VAL A 1 65  ? 179.482 -1.818  -41.214 1.00 31.62  ? 65   VAL A HG11 1 
ATOM   791  H HG12 . VAL A 1 65  ? 180.274 -2.292  -42.507 1.00 31.62  ? 65   VAL A HG12 1 
ATOM   792  H HG13 . VAL A 1 65  ? 178.886 -1.534  -42.659 1.00 31.62  ? 65   VAL A HG13 1 
ATOM   793  H HG21 . VAL A 1 65  ? 179.012 -5.373  -41.330 1.00 35.52  ? 65   VAL A HG21 1 
ATOM   794  H HG22 . VAL A 1 65  ? 180.347 -4.599  -41.706 1.00 35.52  ? 65   VAL A HG22 1 
ATOM   795  H HG23 . VAL A 1 65  ? 179.555 -4.219  -40.382 1.00 35.52  ? 65   VAL A HG23 1 
ATOM   796  N N    . THR A 1 66  ? 176.456 -1.069  -41.732 1.00 28.51  ? 66   THR A N    1 
ATOM   797  C CA   . THR A 1 66  ? 176.048 0.083   -42.522 1.00 29.61  ? 66   THR A CA   1 
ATOM   798  C C    . THR A 1 66  ? 176.980 1.249   -42.235 1.00 31.60  ? 66   THR A C    1 
ATOM   799  O O    . THR A 1 66  ? 177.469 1.408   -41.115 1.00 26.35  ? 66   THR A O    1 
ATOM   800  C CB   . THR A 1 66  ? 174.587 0.521   -42.264 1.00 27.09  ? 66   THR A CB   1 
ATOM   801  O OG1  . THR A 1 66  ? 174.491 1.209   -41.008 1.00 31.09  ? 66   THR A OG1  1 
ATOM   802  C CG2  . THR A 1 66  ? 173.642 -0.673  -42.289 1.00 28.23  ? 66   THR A CG2  1 
ATOM   803  H H    . THR A 1 66  ? 176.654 -0.885  -40.915 1.00 34.41  ? 66   THR A H    1 
ATOM   804  H HA   . THR A 1 66  ? 176.130 -0.138  -43.463 1.00 35.73  ? 66   THR A HA   1 
ATOM   805  H HB   . THR A 1 66  ? 174.315 1.127   -42.971 1.00 32.71  ? 66   THR A HB   1 
ATOM   806  H HG1  . THR A 1 66  ? 174.737 0.704   -40.384 1.00 37.51  ? 66   THR A HG1  1 
ATOM   807  H HG21 . THR A 1 66  ? 173.896 -1.311  -41.604 1.00 34.07  ? 66   THR A HG21 1 
ATOM   808  H HG22 . THR A 1 66  ? 172.732 -0.379  -42.126 1.00 34.07  ? 66   THR A HG22 1 
ATOM   809  H HG23 . THR A 1 66  ? 173.682 -1.108  -43.155 1.00 34.07  ? 66   THR A HG23 1 
ATOM   810  N N    . LEU A 1 67  ? 177.232 2.044   -43.267 1.00 27.22  ? 67   LEU A N    1 
ATOM   811  C CA   . LEU A 1 67  ? 178.058 3.233   -43.152 1.00 23.36  ? 67   LEU A CA   1 
ATOM   812  C C    . LEU A 1 67  ? 177.415 4.342   -43.969 1.00 29.43  ? 67   LEU A C    1 
ATOM   813  O O    . LEU A 1 67  ? 177.218 4.189   -45.174 1.00 30.61  ? 67   LEU A O    1 
ATOM   814  C CB   . LEU A 1 67  ? 179.463 2.957   -43.685 1.00 27.55  ? 67   LEU A CB   1 
ATOM   815  C CG   . LEU A 1 67  ? 180.261 1.816   -43.050 1.00 30.96  ? 67   LEU A CG   1 
ATOM   816  C CD1  . LEU A 1 67  ? 181.511 1.536   -43.870 1.00 26.68  ? 67   LEU A CD1  1 
ATOM   817  C CD2  . LEU A 1 67  ? 180.639 2.146   -41.618 1.00 33.61  ? 67   LEU A CD2  1 
ATOM   818  H H    . LEU A 1 67  ? 176.928 1.912   -44.060 1.00 32.87  ? 67   LEU A H    1 
ATOM   819  H HA   . LEU A 1 67  ? 178.117 3.512   -42.225 1.00 28.23  ? 67   LEU A HA   1 
ATOM   820  H HB2  . LEU A 1 67  ? 179.389 2.757   -44.631 1.00 33.25  ? 67   LEU A HB2  1 
ATOM   821  H HB3  . LEU A 1 67  ? 179.988 3.765   -43.573 1.00 33.25  ? 67   LEU A HB3  1 
ATOM   822  H HG   . LEU A 1 67  ? 179.718 1.012   -43.043 1.00 37.35  ? 67   LEU A HG   1 
ATOM   823  H HD11 . LEU A 1 67  ? 182.058 2.337   -43.896 1.00 32.21  ? 67   LEU A HD11 1 
ATOM   824  H HD12 . LEU A 1 67  ? 182.005 0.811   -43.455 1.00 32.21  ? 67   LEU A HD12 1 
ATOM   825  H HD13 . LEU A 1 67  ? 181.249 1.285   -44.770 1.00 32.21  ? 67   LEU A HD13 1 
ATOM   826  H HD21 . LEU A 1 67  ? 179.829 2.288   -41.103 1.00 40.53  ? 67   LEU A HD21 1 
ATOM   827  H HD22 . LEU A 1 67  ? 181.143 1.405   -41.245 1.00 40.53  ? 67   LEU A HD22 1 
ATOM   828  H HD23 . LEU A 1 67  ? 181.181 2.951   -41.612 1.00 40.53  ? 67   LEU A HD23 1 
ATOM   829  N N    . ARG A 1 68  ? 177.073 5.448   -43.313 1.00 30.25  ? 68   ARG A N    1 
ATOM   830  C CA   . ARG A 1 68  ? 176.503 6.601   -44.003 1.00 29.37  ? 68   ARG A CA   1 
ATOM   831  C C    . ARG A 1 68  ? 177.589 7.628   -44.286 1.00 31.59  ? 68   ARG A C    1 
ATOM   832  O O    . ARG A 1 68  ? 178.116 8.266   -43.373 1.00 29.52  ? 68   ARG A O    1 
ATOM   833  C CB   . ARG A 1 68  ? 175.383 7.239   -43.183 1.00 29.48  ? 68   ARG A CB   1 
ATOM   834  C CG   . ARG A 1 68  ? 174.671 8.377   -43.911 1.00 33.46  ? 68   ARG A CG   1 
ATOM   835  C CD   . ARG A 1 68  ? 173.654 9.068   -43.021 1.00 38.63  ? 68   ARG A CD   1 
ATOM   836  N NE   . ARG A 1 68  ? 172.714 8.121   -42.421 1.00 46.36  ? 68   ARG A NE   1 
ATOM   837  C CZ   . ARG A 1 68  ? 171.402 8.083   -42.656 1.00 46.80  ? 68   ARG A CZ   1 
ATOM   838  N NH1  . ARG A 1 68  ? 170.823 8.945   -43.486 1.00 42.92  ? 68   ARG A NH1  1 
ATOM   839  N NH2  . ARG A 1 68  ? 170.657 7.172   -42.043 1.00 43.75  ? 68   ARG A NH2  1 
ATOM   840  H H    . ARG A 1 68  ? 177.162 5.556   -42.465 1.00 36.50  ? 68   ARG A H    1 
ATOM   841  H HA   . ARG A 1 68  ? 176.130 6.312   -44.851 1.00 35.44  ? 68   ARG A HA   1 
ATOM   842  H HB2  . ARG A 1 68  ? 174.722 6.561   -42.971 1.00 35.57  ? 68   ARG A HB2  1 
ATOM   843  H HB3  . ARG A 1 68  ? 175.759 7.600   -42.364 1.00 35.57  ? 68   ARG A HB3  1 
ATOM   844  H HG2  . ARG A 1 68  ? 175.326 9.035   -44.192 1.00 40.36  ? 68   ARG A HG2  1 
ATOM   845  H HG3  . ARG A 1 68  ? 174.204 8.018   -44.683 1.00 40.36  ? 68   ARG A HG3  1 
ATOM   846  H HD2  . ARG A 1 68  ? 174.119 9.528   -42.304 1.00 46.56  ? 68   ARG A HD2  1 
ATOM   847  H HD3  . ARG A 1 68  ? 173.147 9.703   -43.551 1.00 46.56  ? 68   ARG A HD3  1 
ATOM   848  H HE   . ARG A 1 68  ? 173.033 7.542   -41.871 1.00 55.84  ? 68   ARG A HE   1 
ATOM   849  H HH11 . ARG A 1 68  ? 171.297 9.540   -43.887 1.00 51.71  ? 68   ARG A HH11 1 
ATOM   850  H HH12 . ARG A 1 68  ? 169.975 8.905   -43.624 1.00 51.71  ? 68   ARG A HH12 1 
ATOM   851  H HH21 . ARG A 1 68  ? 171.022 6.610   -41.503 1.00 52.70  ? 68   ARG A HH21 1 
ATOM   852  H HH22 . ARG A 1 68  ? 169.810 7.140   -42.188 1.00 52.70  ? 68   ARG A HH22 1 
ATOM   853  N N    . GLY A 1 69  ? 177.916 7.780   -45.563 1.00 31.93  ? 69   GLY A N    1 
ATOM   854  C CA   . GLY A 1 69  ? 178.941 8.714   -45.984 1.00 33.91  ? 69   GLY A CA   1 
ATOM   855  C C    . GLY A 1 69  ? 178.610 10.150  -45.642 1.00 31.48  ? 69   GLY A C    1 
ATOM   856  O O    . GLY A 1 69  ? 177.442 10.527  -45.535 1.00 36.49  ? 69   GLY A O    1 
ATOM   857  H H    . GLY A 1 69  ? 177.553 7.346   -46.211 1.00 38.51  ? 69   GLY A H    1 
ATOM   858  H HA2  . GLY A 1 69  ? 179.780 8.484   -45.556 1.00 40.90  ? 69   GLY A HA2  1 
ATOM   859  H HA3  . GLY A 1 69  ? 179.059 8.649   -46.945 1.00 40.90  ? 69   GLY A HA3  1 
ATOM   860  N N    . ASP A 1 70  ? 179.654 10.951  -45.465 1.00 30.53  ? 70   ASP A N    1 
ATOM   861  C CA   . ASP A 1 70  ? 179.495 12.374  -45.246 1.00 31.39  ? 70   ASP A CA   1 
ATOM   862  C C    . ASP A 1 70  ? 178.950 13.007  -46.517 1.00 40.57  ? 70   ASP A C    1 
ATOM   863  O O    . ASP A 1 70  ? 179.510 12.828  -47.600 1.00 48.24  ? 70   ASP A O    1 
ATOM   864  C CB   . ASP A 1 70  ? 180.834 13.010  -44.884 1.00 37.19  ? 70   ASP A CB   1 
ATOM   865  C CG   . ASP A 1 70  ? 181.479 12.367  -43.672 1.00 44.44  ? 70   ASP A CG   1 
ATOM   866  O OD1  . ASP A 1 70  ? 180.744 11.942  -42.757 1.00 43.20  ? 70   ASP A OD1  1 
ATOM   867  O OD2  . ASP A 1 70  ? 182.725 12.290  -43.637 1.00 48.65  ? 70   ASP A OD2  1 
ATOM   868  H H    . ASP A 1 70  ? 180.473 10.687  -45.467 1.00 36.83  ? 70   ASP A H    1 
ATOM   869  H HA   . ASP A 1 70  ? 178.867 12.529  -44.522 1.00 37.86  ? 70   ASP A HA   1 
ATOM   870  H HB2  . ASP A 1 70  ? 181.442 12.914  -45.633 1.00 44.82  ? 70   ASP A HB2  1 
ATOM   871  H HB3  . ASP A 1 70  ? 180.696 13.950  -44.687 1.00 44.82  ? 70   ASP A HB3  1 
ATOM   872  N N    . GLY A 1 71  ? 177.851 13.740  -46.383 1.00 36.25  ? 71   GLY A N    1 
ATOM   873  C CA   . GLY A 1 71  ? 177.249 14.424  -47.512 1.00 38.28  ? 71   GLY A CA   1 
ATOM   874  C C    . GLY A 1 71  ? 176.326 13.543  -48.332 1.00 34.28  ? 71   GLY A C    1 
ATOM   875  O O    . GLY A 1 71  ? 175.749 13.989  -49.321 1.00 37.65  ? 71   GLY A O    1 
ATOM   876  H H    . GLY A 1 71  ? 177.433 13.857  -45.640 1.00 43.70  ? 71   GLY A H    1 
ATOM   877  H HA2  . GLY A 1 71  ? 176.738 15.183  -47.191 1.00 46.13  ? 71   GLY A HA2  1 
ATOM   878  H HA3  . GLY A 1 71  ? 177.950 14.755  -48.096 1.00 46.13  ? 71   GLY A HA3  1 
ATOM   879  N N    . ALA A 1 72  ? 176.183 12.288  -47.921 1.00 34.43  ? 72   ALA A N    1 
ATOM   880  C CA   . ALA A 1 72  ? 175.320 11.353  -48.628 1.00 32.86  ? 72   ALA A CA   1 
ATOM   881  C C    . ALA A 1 72  ? 173.871 11.801  -48.547 1.00 35.97  ? 72   ALA A C    1 
ATOM   882  O O    . ALA A 1 72  ? 173.463 12.452  -47.585 1.00 38.82  ? 72   ALA A O    1 
ATOM   883  C CB   . ALA A 1 72  ? 175.465 9.971   -48.048 1.00 28.86  ? 72   ALA A CB   1 
ATOM   884  H H    . ALA A 1 72  ? 176.577 11.954  -47.233 1.00 41.51  ? 72   ALA A H    1 
ATOM   885  H HA   . ALA A 1 72  ? 175.579 11.320  -49.562 1.00 39.63  ? 72   ALA A HA   1 
ATOM   886  H HB1  . ALA A 1 72  ? 175.214 9.994   -47.111 1.00 34.83  ? 72   ALA A HB1  1 
ATOM   887  H HB2  . ALA A 1 72  ? 174.883 9.364   -48.532 1.00 34.83  ? 72   ALA A HB2  1 
ATOM   888  H HB3  . ALA A 1 72  ? 176.388 9.687   -48.137 1.00 34.83  ? 72   ALA A HB3  1 
ATOM   889  N N    . GLY A 1 73  ? 173.096 11.447  -49.566 1.00 35.73  ? 73   GLY A N    1 
ATOM   890  C CA   . GLY A 1 73  ? 171.687 11.781  -49.599 1.00 29.79  ? 73   GLY A CA   1 
ATOM   891  C C    . GLY A 1 73  ? 170.927 10.996  -48.550 1.00 31.35  ? 73   GLY A C    1 
ATOM   892  O O    . GLY A 1 73  ? 171.321 9.882   -48.204 1.00 33.87  ? 73   GLY A O    1 
ATOM   893  H H    . GLY A 1 73  ? 173.370 11.009  -50.254 1.00 43.08  ? 73   GLY A H    1 
ATOM   894  H HA2  . GLY A 1 73  ? 171.569 12.728  -49.428 1.00 35.95  ? 73   GLY A HA2  1 
ATOM   895  H HA3  . GLY A 1 73  ? 171.320 11.572  -50.473 1.00 35.95  ? 73   GLY A HA3  1 
ATOM   896  N N    . PRO A 1 74  ? 169.822 11.563  -48.044 1.00 36.07  ? 74   PRO A N    1 
ATOM   897  C CA   . PRO A 1 74  ? 169.089 10.922  -46.948 1.00 37.80  ? 74   PRO A CA   1 
ATOM   898  C C    . PRO A 1 74  ? 168.363 9.657   -47.389 1.00 39.01  ? 74   PRO A C    1 
ATOM   899  O O    . PRO A 1 74  ? 167.862 8.914   -46.547 1.00 39.27  ? 74   PRO A O    1 
ATOM   900  C CB   . PRO A 1 74  ? 168.090 11.999  -46.521 1.00 37.09  ? 74   PRO A CB   1 
ATOM   901  C CG   . PRO A 1 74  ? 167.857 12.799  -47.743 1.00 40.15  ? 74   PRO A CG   1 
ATOM   902  C CD   . PRO A 1 74  ? 169.140 12.777  -48.528 1.00 35.15  ? 74   PRO A CD   1 
ATOM   903  H HA   . PRO A 1 74  ? 169.685 10.718  -46.210 1.00 45.56  ? 74   PRO A HA   1 
ATOM   904  H HB2  . PRO A 1 74  ? 167.267 11.582  -46.220 1.00 44.70  ? 74   PRO A HB2  1 
ATOM   905  H HB3  . PRO A 1 74  ? 168.477 12.546  -45.820 1.00 44.70  ? 74   PRO A HB3  1 
ATOM   906  H HG2  . PRO A 1 74  ? 167.138 12.400  -48.257 1.00 48.38  ? 74   PRO A HG2  1 
ATOM   907  H HG3  . PRO A 1 74  ? 167.629 13.709  -47.493 1.00 48.38  ? 74   PRO A HG3  1 
ATOM   908  H HD2  . PRO A 1 74  ? 168.954 12.704  -49.477 1.00 42.38  ? 74   PRO A HD2  1 
ATOM   909  H HD3  . PRO A 1 74  ? 169.671 13.564  -48.330 1.00 42.38  ? 74   PRO A HD3  1 
ATOM   910  N N    . GLN A 1 75  ? 168.309 9.423   -48.696 1.00 39.12  ? 75   GLN A N    1 
ATOM   911  C CA   . GLN A 1 75  ? 167.670 8.232   -49.244 1.00 36.66  ? 75   GLN A CA   1 
ATOM   912  C C    . GLN A 1 75  ? 168.655 7.080   -49.433 1.00 34.10  ? 75   GLN A C    1 
ATOM   913  O O    . GLN A 1 75  ? 168.252 5.927   -49.591 1.00 35.62  ? 75   GLN A O    1 
ATOM   914  C CB   . GLN A 1 75  ? 166.998 8.563   -50.582 1.00 33.91  ? 75   GLN A CB   1 
ATOM   915  C CG   . GLN A 1 75  ? 167.926 8.609   -51.797 1.00 26.64  ? 75   GLN A CG   1 
ATOM   916  C CD   . GLN A 1 75  ? 168.984 9.690   -51.712 1.00 37.27  ? 75   GLN A CD   1 
ATOM   917  O OE1  . GLN A 1 75  ? 168.992 10.502  -50.787 1.00 42.38  ? 75   GLN A OE1  1 
ATOM   918  N NE2  . GLN A 1 75  ? 169.883 9.709   -52.688 1.00 47.33  ? 75   GLN A NE2  1 
ATOM   919  H H    . GLN A 1 75  ? 168.640 9.945   -49.293 1.00 47.14  ? 75   GLN A H    1 
ATOM   920  H HA   . GLN A 1 75  ? 166.980 7.935   -48.629 1.00 44.19  ? 75   GLN A HA   1 
ATOM   921  H HB2  . GLN A 1 75  ? 166.320 7.892   -50.759 1.00 40.89  ? 75   GLN A HB2  1 
ATOM   922  H HB3  . GLN A 1 75  ? 166.577 9.434   -50.506 1.00 40.89  ? 75   GLN A HB3  1 
ATOM   923  H HG2  . GLN A 1 75  ? 168.379 7.755   -51.877 1.00 32.17  ? 75   GLN A HG2  1 
ATOM   924  H HG3  . GLN A 1 75  ? 167.395 8.775   -52.591 1.00 32.17  ? 75   GLN A HG3  1 
ATOM   925  H HE21 . GLN A 1 75  ? 169.842 9.129   -53.321 1.00 57.00  ? 75   GLN A HE21 1 
ATOM   926  H HE22 . GLN A 1 75  ? 170.505 10.302  -52.688 1.00 57.00  ? 75   GLN A HE22 1 
ATOM   927  N N    . SER A 1 76  ? 169.945 7.396   -49.417 1.00 35.91  ? 76   SER A N    1 
ATOM   928  C CA   . SER A 1 76  ? 170.983 6.425   -49.756 1.00 34.01  ? 76   SER A CA   1 
ATOM   929  C C    . SER A 1 76  ? 171.137 5.284   -48.746 1.00 32.04  ? 76   SER A C    1 
ATOM   930  O O    . SER A 1 76  ? 171.493 4.166   -49.118 1.00 29.41  ? 76   SER A O    1 
ATOM   931  C CB   . SER A 1 76  ? 172.321 7.147   -49.920 1.00 36.30  ? 76   SER A CB   1 
ATOM   932  O OG   . SER A 1 76  ? 172.624 7.918   -48.772 1.00 32.74  ? 76   SER A OG   1 
ATOM   933  H H    . SER A 1 76  ? 170.250 8.174   -49.211 1.00 43.29  ? 76   SER A H    1 
ATOM   934  H HA   . SER A 1 76  ? 170.761 6.027   -50.612 1.00 41.01  ? 76   SER A HA   1 
ATOM   935  H HB2  . SER A 1 76  ? 173.021 6.488   -50.051 1.00 43.76  ? 76   SER A HB2  1 
ATOM   936  H HB3  . SER A 1 76  ? 172.270 7.735   -50.690 1.00 43.76  ? 76   SER A HB3  1 
ATOM   937  H HG   . SER A 1 76  ? 172.670 7.421   -48.096 1.00 39.49  ? 76   SER A HG   1 
ATOM   938  N N    . TYR A 1 77  ? 170.878 5.566   -47.474 1.00 33.18  ? 77   TYR A N    1 
ATOM   939  C CA   . TYR A 1 77  ? 171.083 4.585   -46.412 1.00 29.79  ? 77   TYR A CA   1 
ATOM   940  C C    . TYR A 1 77  ? 170.194 3.356   -46.605 1.00 29.89  ? 77   TYR A C    1 
ATOM   941  O O    . TYR A 1 77  ? 170.689 2.233   -46.716 1.00 25.24  ? 77   TYR A O    1 
ATOM   942  C CB   . TYR A 1 77  ? 170.811 5.236   -45.052 1.00 31.42  ? 77   TYR A CB   1 
ATOM   943  C CG   . TYR A 1 77  ? 171.173 4.394   -43.847 1.00 30.55  ? 77   TYR A CG   1 
ATOM   944  C CD1  . TYR A 1 77  ? 172.481 4.330   -43.384 1.00 32.52  ? 77   TYR A CD1  1 
ATOM   945  C CD2  . TYR A 1 77  ? 170.201 3.685   -43.155 1.00 34.44  ? 77   TYR A CD2  1 
ATOM   946  C CE1  . TYR A 1 77  ? 172.810 3.574   -42.277 1.00 26.26  ? 77   TYR A CE1  1 
ATOM   947  C CE2  . TYR A 1 77  ? 170.523 2.925   -42.050 1.00 32.17  ? 77   TYR A CE2  1 
ATOM   948  C CZ   . TYR A 1 77  ? 171.829 2.873   -41.615 1.00 32.68  ? 77   TYR A CZ   1 
ATOM   949  O OH   . TYR A 1 77  ? 172.149 2.117   -40.508 1.00 33.95  ? 77   TYR A OH   1 
ATOM   950  H H    . TYR A 1 77  ? 170.579 6.324   -47.197 1.00 40.02  ? 77   TYR A H    1 
ATOM   951  H HA   . TYR A 1 77  ? 172.007 4.293   -46.426 1.00 35.95  ? 77   TYR A HA   1 
ATOM   952  H HB2  . TYR A 1 77  ? 171.324 6.058   -44.998 1.00 37.90  ? 77   TYR A HB2  1 
ATOM   953  H HB3  . TYR A 1 77  ? 169.865 5.440   -44.992 1.00 37.90  ? 77   TYR A HB3  1 
ATOM   954  H HD1  . TYR A 1 77  ? 173.147 4.802   -43.830 1.00 39.23  ? 77   TYR A HD1  1 
ATOM   955  H HD2  . TYR A 1 77  ? 169.319 3.717   -43.447 1.00 41.53  ? 77   TYR A HD2  1 
ATOM   956  H HE1  . TYR A 1 77  ? 173.691 3.536   -41.981 1.00 31.71  ? 77   TYR A HE1  1 
ATOM   957  H HE2  . TYR A 1 77  ? 169.861 2.452   -41.600 1.00 38.80  ? 77   TYR A HE2  1 
ATOM   958  H HH   . TYR A 1 77  ? 172.972 2.173   -40.350 1.00 40.94  ? 77   TYR A HH   1 
ATOM   959  N N    . ASP A 1 78  ? 168.883 3.572   -46.657 1.00 28.97  ? 78   ASP A N    1 
ATOM   960  C CA   . ASP A 1 78  ? 167.933 2.474   -46.808 1.00 32.51  ? 78   ASP A CA   1 
ATOM   961  C C    . ASP A 1 78  ? 168.042 1.809   -48.178 1.00 31.99  ? 78   ASP A C    1 
ATOM   962  O O    . ASP A 1 78  ? 167.815 0.608   -48.313 1.00 33.39  ? 78   ASP A O    1 
ATOM   963  C CB   . ASP A 1 78  ? 166.502 2.968   -46.586 1.00 39.70  ? 78   ASP A CB   1 
ATOM   964  C CG   . ASP A 1 78  ? 166.252 3.413   -45.155 1.00 40.81  ? 78   ASP A CG   1 
ATOM   965  O OD1  . ASP A 1 78  ? 166.981 2.957   -44.248 1.00 37.24  ? 78   ASP A OD1  1 
ATOM   966  O OD2  . ASP A 1 78  ? 165.321 4.217   -44.938 1.00 40.26  ? 78   ASP A OD2  1 
ATOM   967  H H    . ASP A 1 78  ? 168.517 4.348   -46.607 1.00 34.97  ? 78   ASP A H    1 
ATOM   968  H HA   . ASP A 1 78  ? 168.123 1.801   -46.136 1.00 39.22  ? 78   ASP A HA   1 
ATOM   969  H HB2  . ASP A 1 78  ? 166.335 3.725   -47.169 1.00 47.83  ? 78   ASP A HB2  1 
ATOM   970  H HB3  . ASP A 1 78  ? 165.884 2.249   -46.789 1.00 47.83  ? 78   ASP A HB3  1 
ATOM   971  N N    A SER A 1 79  ? 168.392 2.599   -49.186 0.56 33.41  ? 79   SER A N    1 
ATOM   972  N N    B SER A 1 79  ? 168.390 2.593   -49.195 0.44 33.06  ? 79   SER A N    1 
ATOM   973  C CA   A SER A 1 79  ? 168.544 2.089   -50.541 0.56 31.40  ? 79   SER A CA   1 
ATOM   974  C CA   B SER A 1 79  ? 168.543 2.062   -50.546 0.44 31.73  ? 79   SER A CA   1 
ATOM   975  C C    A SER A 1 79  ? 169.681 1.075   -50.619 0.56 29.83  ? 79   SER A C    1 
ATOM   976  C C    B SER A 1 79  ? 169.681 1.055   -50.605 0.44 30.02  ? 79   SER A C    1 
ATOM   977  O O    A SER A 1 79  ? 169.528 0.004   -51.204 0.56 30.30  ? 79   SER A O    1 
ATOM   978  O O    B SER A 1 79  ? 169.530 -0.029  -51.167 0.44 30.12  ? 79   SER A O    1 
ATOM   979  C CB   A SER A 1 79  ? 168.799 3.242   -51.512 0.56 34.30  ? 79   SER A CB   1 
ATOM   980  C CB   B SER A 1 79  ? 168.807 3.189   -51.545 0.44 33.96  ? 79   SER A CB   1 
ATOM   981  O OG   A SER A 1 79  ? 169.016 2.765   -52.827 0.56 34.78  ? 79   SER A OG   1 
ATOM   982  O OG   B SER A 1 79  ? 167.682 4.038   -51.660 0.44 34.12  ? 79   SER A OG   1 
ATOM   983  H H    A SER A 1 79  ? 168.548 3.441   -49.110 0.56 40.29  ? 79   SER A H    1 
ATOM   984  H H    B SER A 1 79  ? 168.543 3.436   -49.129 0.44 39.87  ? 79   SER A H    1 
ATOM   985  H HA   A SER A 1 79  ? 167.724 1.644   -50.808 0.56 37.88  ? 79   SER A HA   1 
ATOM   986  H HA   B SER A 1 79  ? 167.725 1.611   -50.806 0.44 38.27  ? 79   SER A HA   1 
ATOM   987  H HB2  A SER A 1 79  ? 168.027 3.829   -51.514 0.56 41.35  ? 79   SER A HB2  1 
ATOM   988  H HB2  B SER A 1 79  ? 169.565 3.710   -51.239 0.44 40.95  ? 79   SER A HB2  1 
ATOM   989  H HB3  A SER A 1 79  ? 169.585 3.731   -51.221 0.56 41.35  ? 79   SER A HB3  1 
ATOM   990  H HB3  B SER A 1 79  ? 169.000 2.802   -52.413 0.44 40.95  ? 79   SER A HB3  1 
ATOM   991  H HG   A SER A 1 79  ? 169.155 3.409   -53.348 0.56 41.94  ? 79   SER A HG   1 
ATOM   992  H HG   B SER A 1 79  ? 167.840 4.652   -52.211 0.44 41.15  ? 79   SER A HG   1 
ATOM   993  N N    . ALA A 1 80  ? 170.818 1.418   -50.021 1.00 30.63  ? 80   ALA A N    1 
ATOM   994  C CA   . ALA A 1 80  ? 171.973 0.531   -49.995 1.00 29.93  ? 80   ALA A CA   1 
ATOM   995  C C    . ALA A 1 80  ? 171.631 -0.764  -49.272 1.00 28.48  ? 80   ALA A C    1 
ATOM   996  O O    . ALA A 1 80  ? 172.084 -1.841  -49.656 1.00 30.27  ? 80   ALA A O    1 
ATOM   997  C CB   . ALA A 1 80  ? 173.133 1.215   -49.316 1.00 31.79  ? 80   ALA A CB   1 
ATOM   998  H H    . ALA A 1 80  ? 170.945 2.170   -49.625 1.00 36.96  ? 80   ALA A H    1 
ATOM   999  H HA   . ALA A 1 80  ? 172.235 0.315   -50.904 1.00 36.12  ? 80   ALA A HA   1 
ATOM   1000 H HB1  . ALA A 1 80  ? 172.878 1.439   -48.407 1.00 38.34  ? 80   ALA A HB1  1 
ATOM   1001 H HB2  . ALA A 1 80  ? 173.893 0.612   -49.307 1.00 38.34  ? 80   ALA A HB2  1 
ATOM   1002 H HB3  . ALA A 1 80  ? 173.355 2.021   -49.806 1.00 38.34  ? 80   ALA A HB3  1 
ATOM   1003 N N    . ASP A 1 81  ? 170.823 -0.651  -48.224 1.00 25.93  ? 81   ASP A N    1 
ATOM   1004 C CA   . ASP A 1 81  ? 170.419 -1.813  -47.447 1.00 29.16  ? 81   ASP A CA   1 
ATOM   1005 C C    . ASP A 1 81  ? 169.566 -2.748  -48.296 1.00 28.09  ? 81   ASP A C    1 
ATOM   1006 O O    . ASP A 1 81  ? 169.813 -3.952  -48.348 1.00 33.97  ? 81   ASP A O    1 
ATOM   1007 C CB   . ASP A 1 81  ? 169.636 -1.374  -46.210 1.00 34.49  ? 81   ASP A CB   1 
ATOM   1008 C CG   . ASP A 1 81  ? 169.845 -2.298  -45.026 1.00 40.71  ? 81   ASP A CG   1 
ATOM   1009 O OD1  . ASP A 1 81  ? 170.177 -3.483  -45.234 1.00 44.77  ? 81   ASP A OD1  1 
ATOM   1010 O OD2  . ASP A 1 81  ? 169.677 -1.835  -43.878 1.00 49.88  ? 81   ASP A OD2  1 
ATOM   1011 H H    . ASP A 1 81  ? 170.495 0.092   -47.942 1.00 31.31  ? 81   ASP A H    1 
ATOM   1012 H HA   . ASP A 1 81  ? 171.208 -2.297  -47.156 1.00 35.19  ? 81   ASP A HA   1 
ATOM   1013 H HB2  . ASP A 1 81  ? 169.926 -0.485  -45.951 1.00 41.59  ? 81   ASP A HB2  1 
ATOM   1014 H HB3  . ASP A 1 81  ? 168.690 -1.366  -46.421 1.00 41.59  ? 81   ASP A HB3  1 
ATOM   1015 N N    . ARG A 1 82  ? 168.564 -2.186  -48.964 1.00 30.77  ? 82   ARG A N    1 
ATOM   1016 C CA   . ARG A 1 82  ? 167.661 -2.976  -49.793 1.00 32.48  ? 82   ARG A CA   1 
ATOM   1017 C C    . ARG A 1 82  ? 168.379 -3.570  -51.002 1.00 28.65  ? 82   ARG A C    1 
ATOM   1018 O O    . ARG A 1 82  ? 168.019 -4.646  -51.479 1.00 32.88  ? 82   ARG A O    1 
ATOM   1019 C CB   . ARG A 1 82  ? 166.473 -2.131  -50.255 1.00 29.36  ? 82   ARG A CB   1 
ATOM   1020 C CG   . ARG A 1 82  ? 165.528 -1.711  -49.138 1.00 29.62  ? 82   ARG A CG   1 
ATOM   1021 C CD   . ARG A 1 82  ? 164.135 -1.453  -49.677 1.00 40.48  ? 82   ARG A CD   1 
ATOM   1022 N NE   . ARG A 1 82  ? 163.255 -0.873  -48.665 1.00 51.19  ? 82   ARG A NE   1 
ATOM   1023 C CZ   . ARG A 1 82  ? 161.933 -1.025  -48.638 1.00 62.24  ? 82   ARG A CZ   1 
ATOM   1024 N NH1  . ARG A 1 82  ? 161.318 -1.754  -49.562 1.00 67.89  ? 82   ARG A NH1  1 
ATOM   1025 N NH2  . ARG A 1 82  ? 161.221 -0.453  -47.676 1.00 66.33  ? 82   ARG A NH2  1 
ATOM   1026 H H    . ARG A 1 82  ? 168.386 -1.344  -48.955 1.00 37.12  ? 82   ARG A H    1 
ATOM   1027 H HA   . ARG A 1 82  ? 167.314 -3.711  -49.263 1.00 39.17  ? 82   ARG A HA   1 
ATOM   1028 H HB2  . ARG A 1 82  ? 166.810 -1.324  -50.675 1.00 35.43  ? 82   ARG A HB2  1 
ATOM   1029 H HB3  . ARG A 1 82  ? 165.959 -2.644  -50.899 1.00 35.43  ? 82   ARG A HB3  1 
ATOM   1030 H HG2  . ARG A 1 82  ? 165.474 -2.419  -48.478 1.00 35.74  ? 82   ARG A HG2  1 
ATOM   1031 H HG3  . ARG A 1 82  ? 165.854 -0.893  -48.731 1.00 35.74  ? 82   ARG A HG3  1 
ATOM   1032 H HD2  . ARG A 1 82  ? 164.191 -0.832  -50.420 1.00 48.78  ? 82   ARG A HD2  1 
ATOM   1033 H HD3  . ARG A 1 82  ? 163.746 -2.292  -49.970 1.00 48.78  ? 82   ARG A HD3  1 
ATOM   1034 H HE   . ARG A 1 82  ? 163.616 -0.400  -48.044 1.00 61.62  ? 82   ARG A HE   1 
ATOM   1035 H HH11 . ARG A 1 82  ? 161.774 -2.127  -50.189 1.00 81.66  ? 82   ARG A HH11 1 
ATOM   1036 H HH12 . ARG A 1 82  ? 160.464 -1.849  -49.536 1.00 81.66  ? 82   ARG A HH12 1 
ATOM   1037 H HH21 . ARG A 1 82  ? 161.614 0.018   -47.073 1.00 79.80  ? 82   ARG A HH21 1 
ATOM   1038 H HH22 . ARG A 1 82  ? 160.367 -0.554  -47.655 1.00 79.80  ? 82   ARG A HH22 1 
ATOM   1039 N N    . LYS A 1 83  ? 169.395 -2.869  -51.493 1.00 25.05  ? 83   LYS A N    1 
ATOM   1040 C CA   . LYS A 1 83  ? 170.168 -3.347  -52.635 1.00 26.45  ? 83   LYS A CA   1 
ATOM   1041 C C    . LYS A 1 83  ? 171.001 -4.569  -52.269 1.00 27.51  ? 83   LYS A C    1 
ATOM   1042 O O    . LYS A 1 83  ? 171.099 -5.520  -53.044 1.00 31.89  ? 83   LYS A O    1 
ATOM   1043 C CB   . LYS A 1 83  ? 171.088 -2.247  -53.154 1.00 23.74  ? 83   LYS A CB   1 
ATOM   1044 C CG   . LYS A 1 83  ? 170.406 -1.232  -54.043 1.00 27.34  ? 83   LYS A CG   1 
ATOM   1045 C CD   . LYS A 1 83  ? 171.396 -0.181  -54.489 1.00 30.40  ? 83   LYS A CD   1 
ATOM   1046 C CE   . LYS A 1 83  ? 170.731 0.940   -55.255 1.00 32.49  ? 83   LYS A CE   1 
ATOM   1047 N NZ   . LYS A 1 83  ? 171.699 2.025   -55.570 1.00 34.40  ? 83   LYS A NZ   1 
ATOM   1048 H H    . LYS A 1 83  ? 169.658 -2.111  -51.184 1.00 30.25  ? 83   LYS A H    1 
ATOM   1049 H HA   . LYS A 1 83  ? 169.561 -3.597  -53.349 1.00 31.94  ? 83   LYS A HA   1 
ATOM   1050 H HB2  . LYS A 1 83  ? 171.462 -1.771  -52.396 1.00 28.69  ? 83   LYS A HB2  1 
ATOM   1051 H HB3  . LYS A 1 83  ? 171.802 -2.656  -53.668 1.00 28.69  ? 83   LYS A HB3  1 
ATOM   1052 H HG2  . LYS A 1 83  ? 170.052 -1.676  -54.830 1.00 33.01  ? 83   LYS A HG2  1 
ATOM   1053 H HG3  . LYS A 1 83  ? 169.694 -0.796  -53.550 1.00 33.01  ? 83   LYS A HG3  1 
ATOM   1054 H HD2  . LYS A 1 83  ? 171.827 0.201   -53.708 1.00 36.68  ? 83   LYS A HD2  1 
ATOM   1055 H HD3  . LYS A 1 83  ? 172.057 -0.592  -55.067 1.00 36.68  ? 83   LYS A HD3  1 
ATOM   1056 H HE2  . LYS A 1 83  ? 170.379 0.594   -56.090 1.00 39.19  ? 83   LYS A HE2  1 
ATOM   1057 H HE3  . LYS A 1 83  ? 170.016 1.316   -54.719 1.00 39.19  ? 83   LYS A HE3  1 
ATOM   1058 H HZ1  . LYS A 1 83  ? 172.365 1.703   -56.065 1.00 41.47  ? 83   LYS A HZ1  1 
ATOM   1059 H HZ2  . LYS A 1 83  ? 171.291 2.675   -56.021 1.00 41.47  ? 83   LYS A HZ2  1 
ATOM   1060 H HZ3  . LYS A 1 83  ? 172.034 2.361   -54.817 1.00 41.47  ? 83   LYS A HZ3  1 
ATOM   1061 N N    . ALA A 1 84  ? 171.609 -4.530  -51.088 1.00 27.29  ? 84   ALA A N    1 
ATOM   1062 C CA   . ALA A 1 84  ? 172.422 -5.635  -50.608 1.00 25.27  ? 84   ALA A CA   1 
ATOM   1063 C C    . ALA A 1 84  ? 171.537 -6.847  -50.350 1.00 26.93  ? 84   ALA A C    1 
ATOM   1064 O O    . ALA A 1 84  ? 171.897 -7.979  -50.673 1.00 32.59  ? 84   ALA A O    1 
ATOM   1065 C CB   . ALA A 1 84  ? 173.145 -5.230  -49.343 1.00 32.51  ? 84   ALA A CB   1 
ATOM   1066 H H    . ALA A 1 84  ? 171.564 -3.866  -50.543 1.00 32.95  ? 84   ALA A H    1 
ATOM   1067 H HA   . ALA A 1 84  ? 173.081 -5.870  -51.279 1.00 30.52  ? 84   ALA A HA   1 
ATOM   1068 H HB1  . ALA A 1 84  ? 172.490 -4.992  -48.668 1.00 39.21  ? 84   ALA A HB1  1 
ATOM   1069 H HB2  . ALA A 1 84  ? 173.682 -5.976  -49.034 1.00 39.21  ? 84   ALA A HB2  1 
ATOM   1070 H HB3  . ALA A 1 84  ? 173.714 -4.468  -49.535 1.00 39.21  ? 84   ALA A HB3  1 
ATOM   1071 N N    . PHE A 1 85  ? 170.375 -6.591  -49.762 1.00 25.95  ? 85   PHE A N    1 
ATOM   1072 C CA   . PHE A 1 85  ? 169.385 -7.624  -49.488 1.00 27.78  ? 85   PHE A CA   1 
ATOM   1073 C C    . PHE A 1 85  ? 168.927 -8.290  -50.784 1.00 29.44  ? 85   PHE A C    1 
ATOM   1074 O O    . PHE A 1 85  ? 168.757 -9.508  -50.847 1.00 29.70  ? 85   PHE A O    1 
ATOM   1075 C CB   . PHE A 1 85  ? 168.195 -6.992  -48.765 1.00 25.05  ? 85   PHE A CB   1 
ATOM   1076 C CG   . PHE A 1 85  ? 167.074 -7.947  -48.469 1.00 26.85  ? 85   PHE A CG   1 
ATOM   1077 C CD1  . PHE A 1 85  ? 167.054 -8.668  -47.288 1.00 29.89  ? 85   PHE A CD1  1 
ATOM   1078 C CD2  . PHE A 1 85  ? 166.028 -8.104  -49.360 1.00 26.10  ? 85   PHE A CD2  1 
ATOM   1079 C CE1  . PHE A 1 85  ? 166.020 -9.538  -47.012 1.00 30.21  ? 85   PHE A CE1  1 
ATOM   1080 C CE2  . PHE A 1 85  ? 164.995 -8.972  -49.087 1.00 27.76  ? 85   PHE A CE2  1 
ATOM   1081 C CZ   . PHE A 1 85  ? 164.991 -9.691  -47.913 1.00 31.44  ? 85   PHE A CZ   1 
ATOM   1082 H H    . PHE A 1 85  ? 170.131 -5.807  -49.505 1.00 31.34  ? 85   PHE A H    1 
ATOM   1083 H HA   . PHE A 1 85  ? 169.772 -8.302  -48.913 1.00 33.54  ? 85   PHE A HA   1 
ATOM   1084 H HB2  . PHE A 1 85  ? 168.502 -6.627  -47.920 1.00 30.26  ? 85   PHE A HB2  1 
ATOM   1085 H HB3  . PHE A 1 85  ? 167.837 -6.280  -49.318 1.00 30.26  ? 85   PHE A HB3  1 
ATOM   1086 H HD1  . PHE A 1 85  ? 167.748 -8.570  -46.677 1.00 36.07  ? 85   PHE A HD1  1 
ATOM   1087 H HD2  . PHE A 1 85  ? 166.027 -7.623  -50.156 1.00 31.52  ? 85   PHE A HD2  1 
ATOM   1088 H HE1  . PHE A 1 85  ? 166.019 -10.022 -46.218 1.00 36.46  ? 85   PHE A HE1  1 
ATOM   1089 H HE2  . PHE A 1 85  ? 164.300 -9.074  -49.697 1.00 33.51  ? 85   PHE A HE2  1 
ATOM   1090 H HZ   . PHE A 1 85  ? 164.293 -10.277 -47.728 1.00 37.93  ? 85   PHE A HZ   1 
ATOM   1091 N N    . THR A 1 86  ? 168.741 -7.480  -51.818 1.00 31.76  ? 86   THR A N    1 
ATOM   1092 C CA   . THR A 1 86  ? 168.269 -7.968  -53.106 1.00 30.81  ? 86   THR A CA   1 
ATOM   1093 C C    . THR A 1 86  ? 169.344 -8.795  -53.805 1.00 29.70  ? 86   THR A C    1 
ATOM   1094 O O    . THR A 1 86  ? 169.052 -9.826  -54.408 1.00 33.07  ? 86   THR A O    1 
ATOM   1095 C CB   . THR A 1 86  ? 167.862 -6.796  -54.015 1.00 30.59  ? 86   THR A CB   1 
ATOM   1096 O OG1  . THR A 1 86  ? 166.904 -5.974  -53.337 1.00 34.68  ? 86   THR A OG1  1 
ATOM   1097 C CG2  . THR A 1 86  ? 167.255 -7.299  -55.308 1.00 32.41  ? 86   THR A CG2  1 
ATOM   1098 H H    . THR A 1 86  ? 168.883 -6.632  -51.799 1.00 38.31  ? 86   THR A H    1 
ATOM   1099 H HA   . THR A 1 86  ? 167.492 -8.531  -52.970 1.00 37.17  ? 86   THR A HA   1 
ATOM   1100 H HB   . THR A 1 86  ? 168.647 -6.267  -54.230 1.00 36.91  ? 86   THR A HB   1 
ATOM   1101 H HG1  . THR A 1 86  ? 167.236 -5.670  -52.628 1.00 41.81  ? 86   THR A HG1  1 
ATOM   1102 H HG21 . THR A 1 86  ? 166.465 -7.829  -55.119 1.00 39.09  ? 86   THR A HG21 1 
ATOM   1103 H HG22 . THR A 1 86  ? 167.004 -6.549  -55.870 1.00 39.09  ? 86   THR A HG22 1 
ATOM   1104 H HG23 . THR A 1 86  ? 167.897 -7.848  -55.784 1.00 39.09  ? 86   THR A HG23 1 
ATOM   1105 N N    . ALA A 1 87  ? 170.588 -8.338  -53.720 1.00 28.61  ? 87   ALA A N    1 
ATOM   1106 C CA   . ALA A 1 87  ? 171.694 -9.017  -54.383 1.00 31.18  ? 87   ALA A CA   1 
ATOM   1107 C C    . ALA A 1 87  ? 171.989 -10.385 -53.768 1.00 32.00  ? 87   ALA A C    1 
ATOM   1108 O O    . ALA A 1 87  ? 172.304 -11.336 -54.481 1.00 30.50  ? 87   ALA A O    1 
ATOM   1109 C CB   . ALA A 1 87  ? 172.939 -8.146  -54.350 1.00 29.32  ? 87   ALA A CB   1 
ATOM   1110 H H    . ALA A 1 87  ? 170.818 -7.634  -53.284 1.00 34.53  ? 87   ALA A H    1 
ATOM   1111 H HA   . ALA A 1 87  ? 171.459 -9.158  -55.313 1.00 37.61  ? 87   ALA A HA   1 
ATOM   1112 H HB1  . ALA A 1 87  ? 173.177 -7.970  -53.426 1.00 35.38  ? 87   ALA A HB1  1 
ATOM   1113 H HB2  . ALA A 1 87  ? 173.663 -8.614  -54.795 1.00 35.38  ? 87   ALA A HB2  1 
ATOM   1114 H HB3  . ALA A 1 87  ? 172.753 -7.312  -54.809 1.00 35.38  ? 87   ALA A HB3  1 
ATOM   1115 N N    . VAL A 1 88  ? 171.888 -10.482 -52.447 1.00 29.73  ? 88   VAL A N    1 
ATOM   1116 C CA   . VAL A 1 88  ? 172.198 -11.729 -51.759 1.00 30.92  ? 88   VAL A CA   1 
ATOM   1117 C C    . VAL A 1 88  ? 171.030 -12.713 -51.842 1.00 30.38  ? 88   VAL A C    1 
ATOM   1118 O O    . VAL A 1 88  ? 171.216 -13.923 -51.712 1.00 32.93  ? 88   VAL A O    1 
ATOM   1119 C CB   . VAL A 1 88  ? 172.585 -11.475 -50.284 1.00 33.20  ? 88   VAL A CB   1 
ATOM   1120 C CG1  . VAL A 1 88  ? 171.362 -11.136 -49.436 1.00 30.39  ? 88   VAL A CG1  1 
ATOM   1121 C CG2  . VAL A 1 88  ? 173.307 -12.674 -49.714 1.00 29.53  ? 88   VAL A CG2  1 
ATOM   1122 H H    . VAL A 1 88  ? 171.643 -9.842  -51.927 1.00 35.87  ? 88   VAL A H    1 
ATOM   1123 H HA   . VAL A 1 88  ? 172.960 -12.141 -52.195 1.00 37.30  ? 88   VAL A HA   1 
ATOM   1124 H HB   . VAL A 1 88  ? 173.191 -10.718 -50.246 1.00 40.04  ? 88   VAL A HB   1 
ATOM   1125 H HG11 . VAL A 1 88  ? 170.739 -11.879 -49.471 1.00 36.67  ? 88   VAL A HG11 1 
ATOM   1126 H HG12 . VAL A 1 88  ? 171.646 -10.984 -48.521 1.00 36.67  ? 88   VAL A HG12 1 
ATOM   1127 H HG13 . VAL A 1 88  ? 170.944 -10.336 -49.790 1.00 36.67  ? 88   VAL A HG13 1 
ATOM   1128 H HG21 . VAL A 1 88  ? 174.111 -12.834 -50.232 1.00 35.63  ? 88   VAL A HG21 1 
ATOM   1129 H HG22 . VAL A 1 88  ? 173.539 -12.492 -48.790 1.00 35.63  ? 88   VAL A HG22 1 
ATOM   1130 H HG23 . VAL A 1 88  ? 172.723 -13.447 -49.762 1.00 35.63  ? 88   VAL A HG23 1 
ATOM   1131 N N    . SER A 1 89  ? 169.830 -12.188 -52.068 1.00 31.74  ? 89   SER A N    1 
ATOM   1132 C CA   . SER A 1 89  ? 168.637 -13.022 -52.171 1.00 32.13  ? 89   SER A CA   1 
ATOM   1133 C C    . SER A 1 89  ? 168.624 -13.829 -53.465 1.00 32.86  ? 89   SER A C    1 
ATOM   1134 O O    . SER A 1 89  ? 168.218 -14.993 -53.476 1.00 31.45  ? 89   SER A O    1 
ATOM   1135 C CB   . SER A 1 89  ? 167.377 -12.159 -52.089 1.00 36.99  ? 89   SER A CB   1 
ATOM   1136 O OG   . SER A 1 89  ? 167.116 -11.759 -50.754 1.00 37.40  ? 89   SER A OG   1 
ATOM   1137 H H    . SER A 1 89  ? 169.679 -11.347 -52.166 1.00 38.29  ? 89   SER A H    1 
ATOM   1138 H HA   . SER A 1 89  ? 168.623 -13.645 -51.428 1.00 38.76  ? 89   SER A HA   1 
ATOM   1139 H HB2  . SER A 1 89  ? 167.502 -11.368 -52.636 1.00 44.58  ? 89   SER A HB2  1 
ATOM   1140 H HB3  . SER A 1 89  ? 166.623 -12.673 -52.417 1.00 44.58  ? 89   SER A HB3  1 
ATOM   1141 H HG   . SER A 1 89  ? 167.762 -11.312 -50.456 1.00 45.08  ? 89   SER A HG   1 
ATOM   1142 N N    . TRP A 1 90  ? 169.069 -13.205 -54.551 1.00 33.15  ? 90   TRP A N    1 
ATOM   1143 C CA   . TRP A 1 90  ? 169.065 -13.840 -55.867 1.00 37.12  ? 90   TRP A CA   1 
ATOM   1144 C C    . TRP A 1 90  ? 170.475 -14.177 -56.345 1.00 37.60  ? 90   TRP A C    1 
ATOM   1145 O O    . TRP A 1 90  ? 170.655 -14.710 -57.441 1.00 37.09  ? 90   TRP A O    1 
ATOM   1146 C CB   . TRP A 1 90  ? 168.370 -12.931 -56.881 1.00 34.25  ? 90   TRP A CB   1 
ATOM   1147 C CG   . TRP A 1 90  ? 166.881 -13.018 -56.819 1.00 33.06  ? 90   TRP A CG   1 
ATOM   1148 C CD1  . TRP A 1 90  ? 166.092 -13.926 -57.456 1.00 40.48  ? 90   TRP A CD1  1 
ATOM   1149 C CD2  . TRP A 1 90  ? 165.996 -12.167 -56.079 1.00 32.78  ? 90   TRP A CD2  1 
ATOM   1150 N NE1  . TRP A 1 90  ? 164.771 -13.698 -57.159 1.00 41.65  ? 90   TRP A NE1  1 
ATOM   1151 C CE2  . TRP A 1 90  ? 164.685 -12.623 -56.317 1.00 39.58  ? 90   TRP A CE2  1 
ATOM   1152 C CE3  . TRP A 1 90  ? 166.184 -11.066 -55.239 1.00 32.54  ? 90   TRP A CE3  1 
ATOM   1153 C CZ2  . TRP A 1 90  ? 163.570 -12.016 -55.745 1.00 39.69  ? 90   TRP A CZ2  1 
ATOM   1154 C CZ3  . TRP A 1 90  ? 165.075 -10.467 -54.673 1.00 32.56  ? 90   TRP A CZ3  1 
ATOM   1155 C CH2  . TRP A 1 90  ? 163.786 -10.942 -54.928 1.00 33.69  ? 90   TRP A CH2  1 
ATOM   1156 H H    . TRP A 1 90  ? 169.383 -12.405 -54.553 1.00 39.98  ? 90   TRP A H    1 
ATOM   1157 H HA   . TRP A 1 90  ? 168.563 -14.668 -55.815 1.00 44.74  ? 90   TRP A HA   1 
ATOM   1158 H HB2  . TRP A 1 90  ? 168.623 -12.011 -56.705 1.00 41.30  ? 90   TRP A HB2  1 
ATOM   1159 H HB3  . TRP A 1 90  ? 168.648 -13.185 -57.775 1.00 41.30  ? 90   TRP A HB3  1 
ATOM   1160 H HD1  . TRP A 1 90  ? 166.403 -14.605 -58.010 1.00 48.78  ? 90   TRP A HD1  1 
ATOM   1161 H HE1  . TRP A 1 90  ? 164.106 -14.155 -57.456 1.00 50.18  ? 90   TRP A HE1  1 
ATOM   1162 H HE3  . TRP A 1 90  ? 167.039 -10.744 -55.064 1.00 39.24  ? 90   TRP A HE3  1 
ATOM   1163 H HZ2  . TRP A 1 90  ? 162.711 -12.330 -55.913 1.00 47.82  ? 90   TRP A HZ2  1 
ATOM   1164 H HZ3  . TRP A 1 90  ? 165.188 -9.733  -54.113 1.00 39.27  ? 90   TRP A HZ3  1 
ATOM   1165 H HH2  . TRP A 1 90  ? 163.059 -10.518 -54.534 1.00 40.63  ? 90   TRP A HH2  1 
ATOM   1166 N N    . ASN A 1 91  ? 171.465 -13.880 -55.507 1.00 30.82  ? 91   ASN A N    1 
ATOM   1167 C CA   . ASN A 1 91  ? 172.868 -14.108 -55.839 1.00 30.53  ? 91   ASN A CA   1 
ATOM   1168 C C    . ASN A 1 91  ? 173.241 -13.525 -57.200 1.00 32.80  ? 91   ASN A C    1 
ATOM   1169 O O    . ASN A 1 91  ? 173.765 -14.223 -58.070 1.00 33.49  ? 91   ASN A O    1 
ATOM   1170 C CB   . ASN A 1 91  ? 173.189 -15.603 -55.793 1.00 29.39  ? 91   ASN A CB   1 
ATOM   1171 C CG   . ASN A 1 91  ? 174.675 -15.880 -55.809 1.00 30.25  ? 91   ASN A CG   1 
ATOM   1172 O OD1  . ASN A 1 91  ? 175.476 -15.058 -55.363 1.00 36.16  ? 91   ASN A OD1  1 
ATOM   1173 N ND2  . ASN A 1 91  ? 175.055 -17.041 -56.326 1.00 34.73  ? 91   ASN A ND2  1 
ATOM   1174 H H    . ASN A 1 91  ? 171.346 -13.539 -54.726 1.00 37.19  ? 91   ASN A H    1 
ATOM   1175 H HA   . ASN A 1 91  ? 173.419 -13.669 -55.172 1.00 36.83  ? 91   ASN A HA   1 
ATOM   1176 H HB2  . ASN A 1 91  ? 172.822 -15.980 -54.978 1.00 35.47  ? 91   ASN A HB2  1 
ATOM   1177 H HB3  . ASN A 1 91  ? 172.794 -16.036 -56.566 1.00 35.47  ? 91   ASN A HB3  1 
ATOM   1178 H HD21 . ASN A 1 91  ? 174.466 -17.589 -56.629 1.00 41.88  ? 91   ASN A HD21 1 
ATOM   1179 H HD22 . ASN A 1 91  ? 175.890 -17.245 -56.358 1.00 41.88  ? 91   ASN A HD22 1 
ATOM   1180 N N    . ALA A 1 92  ? 172.964 -12.239 -57.374 1.00 32.95  ? 92   ALA A N    1 
ATOM   1181 C CA   . ALA A 1 92  ? 173.255 -11.564 -58.628 1.00 36.10  ? 92   ALA A CA   1 
ATOM   1182 C C    . ALA A 1 92  ? 173.319 -10.058 -58.426 1.00 29.12  ? 92   ALA A C    1 
ATOM   1183 O O    . ALA A 1 92  ? 172.708 -9.531  -57.498 1.00 28.88  ? 92   ALA A O    1 
ATOM   1184 C CB   . ALA A 1 92  ? 172.197 -11.903 -59.656 1.00 41.68  ? 92   ALA A CB   1 
ATOM   1185 H H    . ALA A 1 92  ? 172.606 -11.733 -56.778 1.00 39.73  ? 92   ALA A H    1 
ATOM   1186 H HA   . ALA A 1 92  ? 174.114 -11.865 -58.963 1.00 43.52  ? 92   ALA A HA   1 
ATOM   1187 H HB1  . ALA A 1 92  ? 171.333 -11.612 -59.326 1.00 50.22  ? 92   ALA A HB1  1 
ATOM   1188 H HB2  . ALA A 1 92  ? 172.406 -11.446 -60.485 1.00 50.22  ? 92   ALA A HB2  1 
ATOM   1189 H HB3  . ALA A 1 92  ? 172.192 -12.862 -59.799 1.00 50.22  ? 92   ALA A HB3  1 
ATOM   1190 N N    . PRO A 1 93  ? 174.064 -9.358  -59.297 1.00 33.09  ? 93   PRO A N    1 
ATOM   1191 C CA   . PRO A 1 93  ? 174.082 -7.894  -59.243 1.00 28.32  ? 93   PRO A CA   1 
ATOM   1192 C C    . PRO A 1 93  ? 172.689 -7.319  -59.438 1.00 30.66  ? 93   PRO A C    1 
ATOM   1193 O O    . PRO A 1 93  ? 171.930 -7.834  -60.260 1.00 32.66  ? 93   PRO A O    1 
ATOM   1194 C CB   . PRO A 1 93  ? 174.977 -7.507  -60.422 1.00 36.98  ? 93   PRO A CB   1 
ATOM   1195 C CG   . PRO A 1 93  ? 175.807 -8.696  -60.690 1.00 41.86  ? 93   PRO A CG   1 
ATOM   1196 C CD   . PRO A 1 93  ? 174.972 -9.882  -60.331 1.00 40.62  ? 93   PRO A CD   1 
ATOM   1197 H HA   . PRO A 1 93  ? 174.465 -7.577  -58.410 1.00 34.19  ? 93   PRO A HA   1 
ATOM   1198 H HB2  . PRO A 1 93  ? 174.427 -7.293  -61.192 1.00 44.57  ? 93   PRO A HB2  1 
ATOM   1199 H HB3  . PRO A 1 93  ? 175.531 -6.751  -60.176 1.00 44.57  ? 93   PRO A HB3  1 
ATOM   1200 H HG2  . PRO A 1 93  ? 176.044 -8.720  -61.630 1.00 50.43  ? 93   PRO A HG2  1 
ATOM   1201 H HG3  . PRO A 1 93  ? 176.605 -8.664  -60.140 1.00 50.43  ? 93   PRO A HG3  1 
ATOM   1202 H HD2  . PRO A 1 93  ? 174.468 -10.187 -61.101 1.00 48.95  ? 93   PRO A HD2  1 
ATOM   1203 H HD3  . PRO A 1 93  ? 175.528 -10.589 -59.966 1.00 48.95  ? 93   PRO A HD3  1 
ATOM   1204 N N    . THR A 1 94  ? 172.355 -6.269  -58.696 1.00 27.63  ? 94   THR A N    1 
ATOM   1205 C CA   . THR A 1 94  ? 171.043 -5.647  -58.821 1.00 27.31  ? 94   THR A CA   1 
ATOM   1206 C C    . THR A 1 94  ? 170.881 -4.975  -60.183 1.00 30.38  ? 94   THR A C    1 
ATOM   1207 O O    . THR A 1 94  ? 169.764 -4.673  -60.605 1.00 35.51  ? 94   THR A O    1 
ATOM   1208 C CB   . THR A 1 94  ? 170.795 -4.618  -57.706 1.00 27.56  ? 94   THR A CB   1 
ATOM   1209 O OG1  . THR A 1 94  ? 171.879 -3.683  -57.656 1.00 33.38  ? 94   THR A OG1  1 
ATOM   1210 C CG2  . THR A 1 94  ? 170.668 -5.309  -56.363 1.00 30.17  ? 94   THR A CG2  1 
ATOM   1211 H H    . THR A 1 94  ? 172.869 -5.900  -58.113 1.00 33.36  ? 94   THR A H    1 
ATOM   1212 H HA   . THR A 1 94  ? 170.363 -6.335  -58.747 1.00 32.97  ? 94   THR A HA   1 
ATOM   1213 H HB   . THR A 1 94  ? 169.968 -4.143  -57.884 1.00 33.27  ? 94   THR A HB   1 
ATOM   1214 H HG1  . THR A 1 94  ? 171.745 -3.120  -57.047 1.00 40.25  ? 94   THR A HG1  1 
ATOM   1215 H HG21 . THR A 1 94  ? 171.484 -5.795  -56.162 1.00 36.40  ? 94   THR A HG21 1 
ATOM   1216 H HG22 . THR A 1 94  ? 170.512 -4.654  -55.666 1.00 36.40  ? 94   THR A HG22 1 
ATOM   1217 H HG23 . THR A 1 94  ? 169.926 -5.934  -56.381 1.00 36.40  ? 94   THR A HG23 1 
ATOM   1218 N N    . SER A 1 95  ? 171.998 -4.739  -60.865 1.00 29.63  ? 95   SER A N    1 
ATOM   1219 C CA   . SER A 1 95  ? 171.975 -4.201  -62.219 1.00 31.90  ? 95   SER A CA   1 
ATOM   1220 C C    . SER A 1 95  ? 171.342 -5.215  -63.161 1.00 34.70  ? 95   SER A C    1 
ATOM   1221 O O    . SER A 1 95  ? 170.560 -4.860  -64.043 1.00 39.28  ? 95   SER A O    1 
ATOM   1222 C CB   . SER A 1 95  ? 173.396 -3.885  -62.685 1.00 33.89  ? 95   SER A CB   1 
ATOM   1223 O OG   . SER A 1 95  ? 174.237 -5.015  -62.538 1.00 39.30  ? 95   SER A OG   1 
ATOM   1224 H H    . SER A 1 95  ? 172.789 -4.884  -60.561 1.00 35.75  ? 95   SER A H    1 
ATOM   1225 H HA   . SER A 1 95  ? 171.451 -3.386  -62.240 1.00 38.48  ? 95   SER A HA   1 
ATOM   1226 H HB2  . SER A 1 95  ? 173.372 -3.629  -63.620 1.00 40.87  ? 95   SER A HB2  1 
ATOM   1227 H HB3  . SER A 1 95  ? 173.749 -3.157  -62.150 1.00 40.87  ? 95   SER A HB3  1 
ATOM   1228 H HG   . SER A 1 95  ? 175.014 -4.830  -62.797 1.00 47.36  ? 95   SER A HG   1 
ATOM   1229 N N    A GLU A 1 96  ? 171.704 -6.479  -62.961 0.51 36.16  ? 96   GLU A N    1 
ATOM   1230 N N    B GLU A 1 96  ? 171.677 -6.487  -62.969 0.49 36.12  ? 96   GLU A N    1 
ATOM   1231 C CA   A GLU A 1 96  ? 171.186 -7.589  -63.749 0.51 40.38  ? 96   GLU A CA   1 
ATOM   1232 C CA   B GLU A 1 96  ? 171.140 -7.547  -63.812 0.49 40.43  ? 96   GLU A CA   1 
ATOM   1233 C C    A GLU A 1 96  ? 169.733 -7.860  -63.384 0.51 40.53  ? 96   GLU A C    1 
ATOM   1234 C C    B GLU A 1 96  ? 169.724 -7.926  -63.388 0.49 40.62  ? 96   GLU A C    1 
ATOM   1235 O O    A GLU A 1 96  ? 168.879 -8.021  -64.256 0.51 44.14  ? 96   GLU A O    1 
ATOM   1236 O O    B GLU A 1 96  ? 168.878 -8.226  -64.232 0.49 44.62  ? 96   GLU A O    1 
ATOM   1237 C CB   A GLU A 1 96  ? 172.040 -8.835  -63.487 0.51 42.27  ? 96   GLU A CB   1 
ATOM   1238 C CB   B GLU A 1 96  ? 172.053 -8.775  -63.775 0.49 42.89  ? 96   GLU A CB   1 
ATOM   1239 C CG   A GLU A 1 96  ? 171.422 -10.165 -63.909 0.51 44.17  ? 96   GLU A CG   1 
ATOM   1240 C CG   B GLU A 1 96  ? 173.432 -8.535  -64.371 0.49 44.21  ? 96   GLU A CG   1 
ATOM   1241 C CD   A GLU A 1 96  ? 172.126 -11.353 -63.284 0.51 42.28  ? 96   GLU A CD   1 
ATOM   1242 C CD   B GLU A 1 96  ? 173.379 -8.161  -65.842 0.49 44.39  ? 96   GLU A CD   1 
ATOM   1243 O OE1  A GLU A 1 96  ? 173.375 -11.367 -63.258 0.51 40.52  ? 96   GLU A OE1  1 
ATOM   1244 O OE1  B GLU A 1 96  ? 173.010 -9.026  -66.665 0.49 49.91  ? 96   GLU A OE1  1 
ATOM   1245 O OE2  A GLU A 1 96  ? 171.427 -12.274 -62.813 0.51 40.70  ? 96   GLU A OE2  1 
ATOM   1246 O OE2  B GLU A 1 96  ? 173.704 -7.002  -66.177 0.49 35.43  ? 96   GLU A OE2  1 
ATOM   1247 H H    A GLU A 1 96  ? 172.265 -6.723  -62.357 0.51 43.59  ? 96   GLU A H    1 
ATOM   1248 H H    B GLU A 1 96  ? 172.213 -6.762  -62.356 0.49 43.54  ? 96   GLU A H    1 
ATOM   1249 H HA   A GLU A 1 96  ? 171.234 -7.371  -64.693 0.51 48.65  ? 96   GLU A HA   1 
ATOM   1250 H HA   B GLU A 1 96  ? 171.102 -7.231  -64.729 0.49 48.71  ? 96   GLU A HA   1 
ATOM   1251 H HB2  A GLU A 1 96  ? 172.877 -8.739  -63.967 0.51 50.92  ? 96   GLU A HB2  1 
ATOM   1252 H HB2  B GLU A 1 96  ? 172.172 -9.048  -62.852 0.49 51.66  ? 96   GLU A HB2  1 
ATOM   1253 H HB3  A GLU A 1 96  ? 172.219 -8.889  -62.535 0.51 50.92  ? 96   GLU A HB3  1 
ATOM   1254 H HB3  B GLU A 1 96  ? 171.634 -9.491  -64.278 0.49 51.66  ? 96   GLU A HB3  1 
ATOM   1255 H HG2  A GLU A 1 96  ? 170.493 -10.186 -63.632 0.51 53.21  ? 96   GLU A HG2  1 
ATOM   1256 H HG2  B GLU A 1 96  ? 173.861 -7.808  -63.892 0.49 53.25  ? 96   GLU A HG2  1 
ATOM   1257 H HG3  A GLU A 1 96  ? 171.484 -10.252 -64.873 0.51 53.21  ? 96   GLU A HG3  1 
ATOM   1258 H HG3  B GLU A 1 96  ? 173.959 -9.345  -64.286 0.49 53.25  ? 96   GLU A HG3  1 
ATOM   1259 N N    . LEU A 1 97  ? 169.467 -7.914  -62.084 1.00 35.90  ? 97   LEU A N    1 
ATOM   1260 C CA   . LEU A 1 97  ? 168.142 -8.240  -61.572 1.00 36.92  ? 97   LEU A CA   1 
ATOM   1261 C C    . LEU A 1 97  ? 167.098 -7.225  -62.030 1.00 39.34  ? 97   LEU A C    1 
ATOM   1262 O O    . LEU A 1 97  ? 165.928 -7.563  -62.207 1.00 40.92  ? 97   LEU A O    1 
ATOM   1263 C CB   . LEU A 1 97  ? 168.173 -8.308  -60.044 1.00 33.01  ? 97   LEU A CB   1 
ATOM   1264 C CG   . LEU A 1 97  ? 169.051 -9.409  -59.444 1.00 32.92  ? 97   LEU A CG   1 
ATOM   1265 C CD1  . LEU A 1 97  ? 169.206 -9.210  -57.949 1.00 33.01  ? 97   LEU A CD1  1 
ATOM   1266 C CD2  . LEU A 1 97  ? 168.467 -10.777 -59.730 1.00 35.64  ? 97   LEU A CD2  1 
ATOM   1267 H H    . LEU A 1 97  ? 170.046 -7.743  -61.471 1.00 43.28  ? 97   LEU A H    1 
ATOM   1268 H HA   . LEU A 1 97  ? 167.880 -9.112  -61.906 1.00 44.51  ? 97   LEU A HA   1 
ATOM   1269 H HB2  . LEU A 1 97  ? 168.500 -7.460  -59.707 1.00 39.81  ? 97   LEU A HB2  1 
ATOM   1270 H HB3  . LEU A 1 97  ? 167.268 -8.455  -59.727 1.00 39.81  ? 97   LEU A HB3  1 
ATOM   1271 H HG   . LEU A 1 97  ? 169.932 -9.367  -59.847 1.00 39.70  ? 97   LEU A HG   1 
ATOM   1272 H HD11 . LEU A 1 97  ? 168.330 -9.239  -57.534 1.00 39.82  ? 97   LEU A HD11 1 
ATOM   1273 H HD12 . LEU A 1 97  ? 169.766 -9.918  -57.593 1.00 39.82  ? 97   LEU A HD12 1 
ATOM   1274 H HD13 . LEU A 1 97  ? 169.620 -8.347  -57.787 1.00 39.82  ? 97   LEU A HD13 1 
ATOM   1275 H HD21 . LEU A 1 97  ? 168.413 -10.903 -60.690 1.00 42.96  ? 97   LEU A HD21 1 
ATOM   1276 H HD22 . LEU A 1 97  ? 169.041 -11.454 -59.339 1.00 42.96  ? 97   LEU A HD22 1 
ATOM   1277 H HD23 . LEU A 1 97  ? 167.580 -10.830 -59.339 1.00 42.96  ? 97   LEU A HD23 1 
ATOM   1278 N N    . ALA A 1 98  ? 167.526 -5.982  -62.226 1.00 38.74  ? 98   ALA A N    1 
ATOM   1279 C CA   . ALA A 1 98  ? 166.622 -4.923  -62.662 1.00 38.47  ? 98   ALA A CA   1 
ATOM   1280 C C    . ALA A 1 98  ? 166.078 -5.186  -64.064 1.00 38.54  ? 98   ALA A C    1 
ATOM   1281 O O    . ALA A 1 98  ? 165.027 -4.665  -64.438 1.00 43.01  ? 98   ALA A O    1 
ATOM   1282 C CB   . ALA A 1 98  ? 167.332 -3.583  -62.625 1.00 39.90  ? 98   ALA A CB   1 
ATOM   1283 H H    . ALA A 1 98  ? 168.339 -5.725  -62.114 1.00 46.68  ? 98   ALA A H    1 
ATOM   1284 H HA   . ALA A 1 98  ? 165.869 -4.880  -62.052 1.00 46.37  ? 98   ALA A HA   1 
ATOM   1285 H HB1  . ALA A 1 98  ? 168.099 -3.616  -63.217 1.00 48.08  ? 98   ALA A HB1  1 
ATOM   1286 H HB2  . ALA A 1 98  ? 166.717 -2.892  -62.917 1.00 48.08  ? 98   ALA A HB2  1 
ATOM   1287 H HB3  . ALA A 1 98  ? 167.622 -3.405  -61.716 1.00 48.08  ? 98   ALA A HB3  1 
ATOM   1288 N N    . LYS A 1 99  ? 166.795 -5.999  -64.833 1.00 37.10  ? 99   LYS A N    1 
ATOM   1289 C CA   . LYS A 1 99  ? 166.438 -6.253  -66.224 1.00 39.54  ? 99   LYS A CA   1 
ATOM   1290 C C    . LYS A 1 99  ? 165.502 -7.446  -66.383 1.00 39.01  ? 99   LYS A C    1 
ATOM   1291 O O    . LYS A 1 99  ? 164.917 -7.641  -67.448 1.00 41.24  ? 99   LYS A O    1 
ATOM   1292 C CB   . LYS A 1 99  ? 167.704 -6.447  -67.056 1.00 44.78  ? 99   LYS A CB   1 
ATOM   1293 C CG   . LYS A 1 99  ? 168.536 -5.183  -67.145 1.00 45.57  ? 99   LYS A CG   1 
ATOM   1294 C CD   . LYS A 1 99  ? 169.905 -5.428  -67.738 1.00 48.15  ? 99   LYS A CD   1 
ATOM   1295 C CE   . LYS A 1 99  ? 170.703 -4.137  -67.765 1.00 52.21  ? 99   LYS A CE   1 
ATOM   1296 N NZ   . LYS A 1 99  ? 172.066 -4.317  -68.325 1.00 55.83  ? 99   LYS A NZ   1 
ATOM   1297 H H    . LYS A 1 99  ? 167.498 -6.420  -64.570 1.00 44.72  ? 99   LYS A H    1 
ATOM   1298 H HA   . LYS A 1 99  ? 165.977 -5.473  -66.571 1.00 47.65  ? 99   LYS A HA   1 
ATOM   1299 H HB2  . LYS A 1 99  ? 168.249 -7.138  -66.647 1.00 53.94  ? 99   LYS A HB2  1 
ATOM   1300 H HB3  . LYS A 1 99  ? 167.455 -6.708  -67.956 1.00 53.94  ? 99   LYS A HB3  1 
ATOM   1301 H HG2  . LYS A 1 99  ? 168.076 -4.540  -67.707 1.00 54.89  ? 99   LYS A HG2  1 
ATOM   1302 H HG3  . LYS A 1 99  ? 168.656 -4.820  -66.253 1.00 54.89  ? 99   LYS A HG3  1 
ATOM   1303 H HD2  . LYS A 1 99  ? 170.383 -6.074  -67.195 1.00 57.98  ? 99   LYS A HD2  1 
ATOM   1304 H HD3  . LYS A 1 99  ? 169.811 -5.751  -68.647 1.00 57.98  ? 99   LYS A HD3  1 
ATOM   1305 H HE2  . LYS A 1 99  ? 170.235 -3.488  -68.314 1.00 62.85  ? 99   LYS A HE2  1 
ATOM   1306 H HE3  . LYS A 1 99  ? 170.792 -3.802  -66.859 1.00 62.85  ? 99   LYS A HE3  1 
ATOM   1307 H HZ1  . LYS A 1 99  ? 172.013 -4.617  -69.161 1.00 67.19  ? 99   LYS A HZ1  1 
ATOM   1308 H HZ2  . LYS A 1 99  ? 172.500 -3.540  -68.324 1.00 67.19  ? 99   LYS A HZ2  1 
ATOM   1309 H HZ3  . LYS A 1 99  ? 172.521 -4.903  -67.835 1.00 67.19  ? 99   LYS A HZ3  1 
ATOM   1310 N N    . ARG A 1 100 ? 165.356 -8.237  -65.325 1.00 37.38  ? 100  ARG A N    1 
ATOM   1311 C CA   . ARG A 1 100 ? 164.398 -9.337  -65.324 1.00 40.56  ? 100  ARG A CA   1 
ATOM   1312 C C    . ARG A 1 100 ? 162.974 -8.806  -65.219 1.00 39.20  ? 100  ARG A C    1 
ATOM   1313 O O    . ARG A 1 100 ? 162.014 -9.517  -65.519 1.00 46.61  ? 100  ARG A O    1 
ATOM   1314 C CB   . ARG A 1 100 ? 164.667 -10.280 -64.153 1.00 41.99  ? 100  ARG A CB   1 
ATOM   1315 C CG   . ARG A 1 100 ? 166.019 -10.963 -64.194 1.00 49.02  ? 100  ARG A CG   1 
ATOM   1316 C CD   . ARG A 1 100 ? 166.135 -11.985 -63.079 1.00 50.97  ? 100  ARG A CD   1 
ATOM   1317 N NE   . ARG A 1 100 ? 167.505 -12.454 -62.899 1.00 56.19  ? 100  ARG A NE   1 
ATOM   1318 C CZ   . ARG A 1 100 ? 167.867 -13.394 -62.032 1.00 58.36  ? 100  ARG A CZ   1 
ATOM   1319 N NH1  . ARG A 1 100 ? 166.958 -13.977 -61.261 1.00 61.00  ? 100  ARG A NH1  1 
ATOM   1320 N NH2  . ARG A 1 100 ? 169.139 -13.756 -61.938 1.00 57.70  ? 100  ARG A NH2  1 
ATOM   1321 H H    . ARG A 1 100 ? 165.802 -8.158  -64.593 1.00 45.05  ? 100  ARG A H    1 
ATOM   1322 H HA   . ARG A 1 100 ? 164.480 -9.839  -66.149 1.00 48.87  ? 100  ARG A HA   1 
ATOM   1323 H HB2  . ARG A 1 100 ? 164.620 -9.772  -63.328 1.00 50.59  ? 100  ARG A HB2  1 
ATOM   1324 H HB3  . ARG A 1 100 ? 163.988 -10.972 -64.150 1.00 50.59  ? 100  ARG A HB3  1 
ATOM   1325 H HG2  . ARG A 1 100 ? 166.123 -11.422 -65.042 1.00 59.02  ? 100  ARG A HG2  1 
ATOM   1326 H HG3  . ARG A 1 100 ? 166.718 -10.302 -64.078 1.00 59.02  ? 100  ARG A HG3  1 
ATOM   1327 H HD2  . ARG A 1 100 ? 165.842 -11.582 -62.247 1.00 61.36  ? 100  ARG A HD2  1 
ATOM   1328 H HD3  . ARG A 1 100 ? 165.580 -12.752 -63.292 1.00 61.36  ? 100  ARG A HD3  1 
ATOM   1329 H HE   . ARG A 1 100 ? 168.119 -12.098 -63.385 1.00 67.63  ? 100  ARG A HE   1 
ATOM   1330 H HH11 . ARG A 1 100 ? 166.132 -13.745 -61.319 1.00 73.40  ? 100  ARG A HH11 1 
ATOM   1331 H HH12 . ARG A 1 100 ? 167.195 -14.585 -60.701 1.00 73.40  ? 100  ARG A HH12 1 
ATOM   1332 H HH21 . ARG A 1 100 ? 169.730 -13.381 -62.437 1.00 69.44  ? 100  ARG A HH21 1 
ATOM   1333 H HH22 . ARG A 1 100 ? 169.373 -14.365 -61.378 1.00 69.44  ? 100  ARG A HH22 1 
ATOM   1334 N N    . LEU A 1 101 ? 162.843 -7.555  -64.788 1.00 36.81  ? 101  LEU A N    1 
ATOM   1335 C CA   . LEU A 1 101 ? 161.536 -6.941  -64.581 1.00 39.20  ? 101  LEU A CA   1 
ATOM   1336 C C    . LEU A 1 101 ? 160.761 -6.784  -65.884 1.00 42.28  ? 101  LEU A C    1 
ATOM   1337 O O    . LEU A 1 101 ? 159.553 -6.557  -65.869 1.00 47.70  ? 101  LEU A O    1 
ATOM   1338 C CB   . LEU A 1 101 ? 161.694 -5.573  -63.916 1.00 37.74  ? 101  LEU A CB   1 
ATOM   1339 C CG   . LEU A 1 101 ? 162.328 -5.547  -62.524 1.00 36.29  ? 101  LEU A CG   1 
ATOM   1340 C CD1  . LEU A 1 101 ? 162.494 -4.113  -62.061 1.00 32.77  ? 101  LEU A CD1  1 
ATOM   1341 C CD2  . LEU A 1 101 ? 161.496 -6.330  -61.524 1.00 34.06  ? 101  LEU A CD2  1 
ATOM   1342 H H    . LEU A 1 101 ? 163.504 -7.035  -64.607 1.00 44.37  ? 101  LEU A H    1 
ATOM   1343 H HA   . LEU A 1 101 ? 161.014 -7.504  -63.988 1.00 47.24  ? 101  LEU A HA   1 
ATOM   1344 H HB2  . LEU A 1 101 ? 162.244 -5.020  -64.491 1.00 45.49  ? 101  LEU A HB2  1 
ATOM   1345 H HB3  . LEU A 1 101 ? 160.813 -5.173  -63.836 1.00 45.49  ? 101  LEU A HB3  1 
ATOM   1346 H HG   . LEU A 1 101 ? 163.208 -5.954  -62.568 1.00 43.75  ? 101  LEU A HG   1 
ATOM   1347 H HD11 . LEU A 1 101 ? 161.623 -3.689  -62.028 1.00 39.52  ? 101  LEU A HD11 1 
ATOM   1348 H HD12 . LEU A 1 101 ? 162.897 -4.112  -61.178 1.00 39.52  ? 101  LEU A HD12 1 
ATOM   1349 H HD13 . LEU A 1 101 ? 163.067 -3.644  -62.687 1.00 39.52  ? 101  LEU A HD13 1 
ATOM   1350 H HD21 . LEU A 1 101 ? 161.431 -7.251  -61.821 1.00 41.07  ? 101  LEU A HD21 1 
ATOM   1351 H HD22 . LEU A 1 101 ? 161.928 -6.291  -60.656 1.00 41.07  ? 101  LEU A HD22 1 
ATOM   1352 H HD23 . LEU A 1 101 ? 160.612 -5.935  -61.472 1.00 41.07  ? 101  LEU A HD23 1 
ATOM   1353 N N    . ALA A 1 102 ? 161.457 -6.891  -67.011 1.00 45.29  ? 102  ALA A N    1 
ATOM   1354 C CA   . ALA A 1 102 ? 160.805 -6.797  -68.308 1.00 42.41  ? 102  ALA A CA   1 
ATOM   1355 C C    . ALA A 1 102 ? 159.839 -7.962  -68.491 1.00 43.91  ? 102  ALA A C    1 
ATOM   1356 O O    . ALA A 1 102 ? 158.721 -7.784  -68.977 1.00 47.15  ? 102  ALA A O    1 
ATOM   1357 C CB   . ALA A 1 102 ? 161.839 -6.784  -69.418 1.00 48.36  ? 102  ALA A CB   1 
ATOM   1358 H H    . ALA A 1 102 ? 162.306 -7.019  -67.050 1.00 54.55  ? 102  ALA A H    1 
ATOM   1359 H HA   . ALA A 1 102 ? 160.298 -5.971  -68.354 1.00 51.09  ? 102  ALA A HA   1 
ATOM   1360 H HB1  . ALA A 1 102 ? 162.355 -7.605  -69.377 1.00 58.24  ? 102  ALA A HB1  1 
ATOM   1361 H HB2  . ALA A 1 102 ? 161.385 -6.721  -70.273 1.00 58.24  ? 102  ALA A HB2  1 
ATOM   1362 H HB3  . ALA A 1 102 ? 162.423 -6.020  -69.296 1.00 58.24  ? 102  ALA A HB3  1 
ATOM   1363 N N    . GLN A 1 103 ? 160.280 -9.151  -68.088 1.00 44.58  ? 103  GLN A N    1 
ATOM   1364 C CA   . GLN A 1 103 ? 159.480 -10.365 -68.220 1.00 53.85  ? 103  GLN A CA   1 
ATOM   1365 C C    . GLN A 1 103 ? 158.862 -10.778 -66.887 1.00 51.22  ? 103  GLN A C    1 
ATOM   1366 O O    . GLN A 1 103 ? 157.858 -11.490 -66.857 1.00 57.60  ? 103  GLN A O    1 
ATOM   1367 C CB   . GLN A 1 103 ? 160.342 -11.504 -68.768 1.00 62.44  ? 103  GLN A CB   1 
ATOM   1368 C CG   . GLN A 1 103 ? 160.942 -11.220 -70.139 1.00 71.44  ? 103  GLN A CG   1 
ATOM   1369 C CD   . GLN A 1 103 ? 159.892 -10.854 -71.170 1.00 83.92  ? 103  GLN A CD   1 
ATOM   1370 O OE1  . GLN A 1 103 ? 159.952 -9.789  -71.785 1.00 86.12  ? 103  GLN A OE1  1 
ATOM   1371 N NE2  . GLN A 1 103 ? 158.922 -11.740 -71.365 1.00 91.00  ? 103  GLN A NE2  1 
ATOM   1372 H H    . GLN A 1 103 ? 161.051 -9.282  -67.731 1.00 53.70  ? 103  GLN A H    1 
ATOM   1373 H HA   . GLN A 1 103 ? 158.759 -10.203 -68.848 1.00 64.81  ? 103  GLN A HA   1 
ATOM   1374 H HB2  . GLN A 1 103 ? 161.074 -11.666 -68.153 1.00 75.12  ? 103  GLN A HB2  1 
ATOM   1375 H HB3  . GLN A 1 103 ? 159.795 -12.302 -68.844 1.00 75.12  ? 103  GLN A HB3  1 
ATOM   1376 H HG2  . GLN A 1 103 ? 161.562 -10.478 -70.066 1.00 85.93  ? 103  GLN A HG2  1 
ATOM   1377 H HG3  . GLN A 1 103 ? 161.406 -12.013 -70.452 1.00 85.93  ? 103  GLN A HG3  1 
ATOM   1378 H HE21 . GLN A 1 103 ? 158.914 -12.475 -70.918 1.00 109.40 ? 103  GLN A HE21 1 
ATOM   1379 H HE22 . GLN A 1 103 ? 158.302 -11.580 -71.939 1.00 109.40 ? 103  GLN A HE22 1 
ATOM   1380 N N    . ALA A 1 104 ? 159.467 -10.327 -65.792 1.00 45.03  ? 104  ALA A N    1 
ATOM   1381 C CA   . ALA A 1 104 ? 158.975 -10.628 -64.451 1.00 49.59  ? 104  ALA A CA   1 
ATOM   1382 C C    . ALA A 1 104 ? 158.863 -9.341  -63.645 1.00 46.72  ? 104  ALA A C    1 
ATOM   1383 O O    . ALA A 1 104 ? 159.617 -9.131  -62.697 1.00 47.60  ? 104  ALA A O    1 
ATOM   1384 C CB   . ALA A 1 104 ? 159.908 -11.596 -63.765 1.00 53.92  ? 104  ALA A CB   1 
ATOM   1385 H H    . ALA A 1 104 ? 160.174 -9.837  -65.799 1.00 54.23  ? 104  ALA A H    1 
ATOM   1386 H HA   . ALA A 1 104 ? 158.096 -11.035 -64.510 1.00 59.70  ? 104  ALA A HA   1 
ATOM   1387 H HB1  . ALA A 1 104 ? 160.789 -11.195 -63.704 1.00 64.90  ? 104  ALA A HB1  1 
ATOM   1388 H HB2  . ALA A 1 104 ? 159.568 -11.786 -62.876 1.00 64.90  ? 104  ALA A HB2  1 
ATOM   1389 H HB3  . ALA A 1 104 ? 159.952 -12.414 -64.285 1.00 64.90  ? 104  ALA A HB3  1 
ATOM   1390 N N    . PRO A 1 105 ? 157.909 -8.475  -64.015 1.00 44.04  ? 105  PRO A N    1 
ATOM   1391 C CA   . PRO A 1 105 ? 157.856 -7.124  -63.451 1.00 40.75  ? 105  PRO A CA   1 
ATOM   1392 C C    . PRO A 1 105 ? 157.388 -7.078  -62.004 1.00 42.20  ? 105  PRO A C    1 
ATOM   1393 O O    . PRO A 1 105 ? 157.600 -6.063  -61.349 1.00 38.26  ? 105  PRO A O    1 
ATOM   1394 C CB   . PRO A 1 105 ? 156.831 -6.408  -64.342 1.00 39.44  ? 105  PRO A CB   1 
ATOM   1395 C CG   . PRO A 1 105 ? 156.499 -7.360  -65.451 1.00 42.71  ? 105  PRO A CG   1 
ATOM   1396 C CD   . PRO A 1 105 ? 156.788 -8.718  -64.932 1.00 43.74  ? 105  PRO A CD   1 
ATOM   1397 H HA   . PRO A 1 105 ? 158.718 -6.686  -63.530 1.00 49.10  ? 105  PRO A HA   1 
ATOM   1398 H HB2  . PRO A 1 105 ? 156.038 -6.202  -63.822 1.00 47.53  ? 105  PRO A HB2  1 
ATOM   1399 H HB3  . PRO A 1 105 ? 157.224 -5.595  -64.698 1.00 47.53  ? 105  PRO A HB3  1 
ATOM   1400 H HG2  . PRO A 1 105 ? 155.560 -7.276  -65.680 1.00 51.46  ? 105  PRO A HG2  1 
ATOM   1401 H HG3  . PRO A 1 105 ? 157.055 -7.166  -66.222 1.00 51.46  ? 105  PRO A HG3  1 
ATOM   1402 H HD2  . PRO A 1 105 ? 156.023 -9.068  -64.449 1.00 52.69  ? 105  PRO A HD2  1 
ATOM   1403 H HD3  . PRO A 1 105 ? 157.059 -9.308  -65.652 1.00 52.69  ? 105  PRO A HD3  1 
ATOM   1404 N N    . THR A 1 106 ? 156.757 -8.142  -61.518 1.00 43.40  ? 106  THR A N    1 
ATOM   1405 C CA   . THR A 1 106 ? 156.222 -8.145  -60.159 1.00 40.49  ? 106  THR A CA   1 
ATOM   1406 C C    . THR A 1 106 ? 157.250 -8.599  -59.122 1.00 38.18  ? 106  THR A C    1 
ATOM   1407 O O    . THR A 1 106 ? 156.938 -8.706  -57.938 1.00 39.15  ? 106  THR A O    1 
ATOM   1408 C CB   . THR A 1 106 ? 154.965 -9.022  -60.054 1.00 42.60  ? 106  THR A CB   1 
ATOM   1409 O OG1  . THR A 1 106 ? 155.227 -10.311 -60.621 1.00 47.58  ? 106  THR A OG1  1 
ATOM   1410 C CG2  . THR A 1 106 ? 153.812 -8.368  -60.794 1.00 40.00  ? 106  THR A CG2  1 
ATOM   1411 H H    . THR A 1 106 ? 156.624 -8.872  -61.953 1.00 52.28  ? 106  THR A H    1 
ATOM   1412 H HA   . THR A 1 106 ? 155.963 -7.238  -59.931 1.00 48.79  ? 106  THR A HA   1 
ATOM   1413 H HB   . THR A 1 106 ? 154.716 -9.122  -59.122 1.00 51.32  ? 106  THR A HB   1 
ATOM   1414 H HG1  . THR A 1 106 ? 154.541 -10.793 -60.565 1.00 57.30  ? 106  THR A HG1  1 
ATOM   1415 H HG21 . THR A 1 106 ? 154.041 -8.255  -61.730 1.00 48.20  ? 106  THR A HG21 1 
ATOM   1416 H HG22 . THR A 1 106 ? 153.019 -8.923  -60.728 1.00 48.20  ? 106  THR A HG22 1 
ATOM   1417 H HG23 . THR A 1 106 ? 153.622 -7.499  -60.409 1.00 48.20  ? 106  THR A HG23 1 
ATOM   1418 N N    . LEU A 1 107 ? 158.474 -8.864  -59.568 1.00 29.87  ? 107  LEU A N    1 
ATOM   1419 C CA   . LEU A 1 107 ? 159.556 -9.201  -58.653 1.00 32.07  ? 107  LEU A CA   1 
ATOM   1420 C C    . LEU A 1 107 ? 159.818 -8.047  -57.691 1.00 37.83  ? 107  LEU A C    1 
ATOM   1421 O O    . LEU A 1 107 ? 160.143 -8.267  -56.524 1.00 38.03  ? 107  LEU A O    1 
ATOM   1422 C CB   . LEU A 1 107 ? 160.834 -9.522  -59.427 1.00 30.64  ? 107  LEU A CB   1 
ATOM   1423 C CG   . LEU A 1 107 ? 160.824 -10.774 -60.307 1.00 37.98  ? 107  LEU A CG   1 
ATOM   1424 C CD1  . LEU A 1 107 ? 162.024 -10.763 -61.235 1.00 36.65  ? 107  LEU A CD1  1 
ATOM   1425 C CD2  . LEU A 1 107 ? 160.834 -12.031 -59.466 1.00 40.72  ? 107  LEU A CD2  1 
ATOM   1426 H H    . LEU A 1 107 ? 158.702 -8.857  -60.397 1.00 36.04  ? 107  LEU A H    1 
ATOM   1427 H HA   . LEU A 1 107 ? 159.307 -9.981  -58.134 1.00 38.69  ? 107  LEU A HA   1 
ATOM   1428 H HB2  . LEU A 1 107 ? 161.032 -8.769  -60.005 1.00 36.97  ? 107  LEU A HB2  1 
ATOM   1429 H HB3  . LEU A 1 107 ? 161.554 -9.630  -58.786 1.00 36.97  ? 107  LEU A HB3  1 
ATOM   1430 H HG   . LEU A 1 107 ? 160.021 -10.778 -60.850 1.00 45.78  ? 107  LEU A HG   1 
ATOM   1431 H HD11 . LEU A 1 107 ? 162.834 -10.748 -60.702 1.00 44.18  ? 107  LEU A HD11 1 
ATOM   1432 H HD12 . LEU A 1 107 ? 162.004 -11.562 -61.785 1.00 44.18  ? 107  LEU A HD12 1 
ATOM   1433 H HD13 . LEU A 1 107 ? 161.981 -9.973  -61.796 1.00 44.18  ? 107  LEU A HD13 1 
ATOM   1434 H HD21 . LEU A 1 107 ? 160.046 -12.039 -58.901 1.00 49.07  ? 107  LEU A HD21 1 
ATOM   1435 H HD22 . LEU A 1 107 ? 160.828 -12.804 -60.053 1.00 49.07  ? 107  LEU A HD22 1 
ATOM   1436 H HD23 . LEU A 1 107 ? 161.634 -12.038 -58.918 1.00 49.07  ? 107  LEU A HD23 1 
ATOM   1437 N N    . LYS A 1 108 ? 159.675 -6.818  -58.183 1.00 37.85  ? 108  LYS A N    1 
ATOM   1438 C CA   . LYS A 1 108 ? 159.899 -5.629  -57.362 1.00 32.56  ? 108  LYS A CA   1 
ATOM   1439 C C    . LYS A 1 108 ? 158.875 -5.504  -56.241 1.00 28.68  ? 108  LYS A C    1 
ATOM   1440 O O    . LYS A 1 108 ? 159.071 -4.735  -55.301 1.00 33.29  ? 108  LYS A O    1 
ATOM   1441 C CB   . LYS A 1 108 ? 159.862 -4.365  -58.225 1.00 39.82  ? 108  LYS A CB   1 
ATOM   1442 C CG   . LYS A 1 108 ? 158.576 -4.184  -59.010 1.00 48.51  ? 108  LYS A CG   1 
ATOM   1443 C CD   . LYS A 1 108 ? 158.283 -2.722  -59.306 1.00 57.96  ? 108  LYS A CD   1 
ATOM   1444 C CE   . LYS A 1 108 ? 157.593 -2.026  -58.142 1.00 70.05  ? 108  LYS A CE   1 
ATOM   1445 N NZ   . LYS A 1 108 ? 156.238 -2.582  -57.878 1.00 75.73  ? 108  LYS A NZ   1 
ATOM   1446 H H    . LYS A 1 108 ? 159.448 -6.645  -58.994 1.00 45.61  ? 108  LYS A H    1 
ATOM   1447 H HA   . LYS A 1 108 ? 160.778 -5.689  -56.957 1.00 39.27  ? 108  LYS A HA   1 
ATOM   1448 H HB2  . LYS A 1 108 ? 159.967 -3.592  -57.648 1.00 47.98  ? 108  LYS A HB2  1 
ATOM   1449 H HB3  . LYS A 1 108 ? 160.593 -4.401  -58.861 1.00 47.98  ? 108  LYS A HB3  1 
ATOM   1450 H HG2  . LYS A 1 108 ? 158.651 -4.653  -59.856 1.00 58.41  ? 108  LYS A HG2  1 
ATOM   1451 H HG3  . LYS A 1 108 ? 157.836 -4.541  -58.495 1.00 58.41  ? 108  LYS A HG3  1 
ATOM   1452 H HD2  . LYS A 1 108 ? 159.118 -2.260  -59.481 1.00 69.75  ? 108  LYS A HD2  1 
ATOM   1453 H HD3  . LYS A 1 108 ? 157.702 -2.664  -60.080 1.00 69.75  ? 108  LYS A HD3  1 
ATOM   1454 H HE2  . LYS A 1 108 ? 158.127 -2.141  -57.341 1.00 84.26  ? 108  LYS A HE2  1 
ATOM   1455 H HE3  . LYS A 1 108 ? 157.497 -1.083  -58.347 1.00 84.26  ? 108  LYS A HE3  1 
ATOM   1456 H HZ1  . LYS A 1 108 ? 156.298 -3.448  -57.681 1.00 91.07  ? 108  LYS A HZ1  1 
ATOM   1457 H HZ2  . LYS A 1 108 ? 155.863 -2.155  -57.194 1.00 91.07  ? 108  LYS A HZ2  1 
ATOM   1458 H HZ3  . LYS A 1 108 ? 155.724 -2.484  -58.598 1.00 91.07  ? 108  LYS A HZ3  1 
ATOM   1459 N N    . ASP A 1 109 ? 157.781 -6.253  -56.343 1.00 35.06  ? 109  ASP A N    1 
ATOM   1460 C CA   . ASP A 1 109 ? 156.727 -6.203  -55.336 1.00 37.30  ? 109  ASP A CA   1 
ATOM   1461 C C    . ASP A 1 109 ? 157.070 -7.078  -54.135 1.00 35.47  ? 109  ASP A C    1 
ATOM   1462 O O    . ASP A 1 109 ? 156.342 -7.100  -53.142 1.00 31.97  ? 109  ASP A O    1 
ATOM   1463 C CB   . ASP A 1 109 ? 155.388 -6.625  -55.939 1.00 43.26  ? 109  ASP A CB   1 
ATOM   1464 C CG   . ASP A 1 109 ? 154.920 -5.681  -57.031 1.00 46.69  ? 109  ASP A CG   1 
ATOM   1465 O OD1  . ASP A 1 109 ? 155.090 -4.453  -56.867 1.00 49.24  ? 109  ASP A OD1  1 
ATOM   1466 O OD2  . ASP A 1 109 ? 154.389 -6.164  -58.052 1.00 42.54  ? 109  ASP A OD2  1 
ATOM   1467 H H    . ASP A 1 109 ? 157.625 -6.801  -56.987 1.00 42.27  ? 109  ASP A H    1 
ATOM   1468 H HA   . ASP A 1 109 ? 156.637 -5.289  -55.022 1.00 44.96  ? 109  ASP A HA   1 
ATOM   1469 H HB2  . ASP A 1 109 ? 155.480 -7.510  -56.326 1.00 52.11  ? 109  ASP A HB2  1 
ATOM   1470 H HB3  . ASP A 1 109 ? 154.714 -6.636  -55.241 1.00 52.11  ? 109  ASP A HB3  1 
ATOM   1471 N N    . ILE A 1 110 ? 158.182 -7.798  -54.232 1.00 36.05  ? 110  ILE A N    1 
ATOM   1472 C CA   . ILE A 1 110 ? 158.671 -8.592  -53.117 1.00 33.63  ? 110  ILE A CA   1 
ATOM   1473 C C    . ILE A 1 110 ? 159.166 -7.641  -52.030 1.00 32.59  ? 110  ILE A C    1 
ATOM   1474 O O    . ILE A 1 110 ? 159.933 -6.723  -52.321 1.00 35.60  ? 110  ILE A O    1 
ATOM   1475 C CB   . ILE A 1 110 ? 159.813 -9.526  -53.555 1.00 35.41  ? 110  ILE A CB   1 
ATOM   1476 C CG1  . ILE A 1 110 ? 159.276 -10.579 -54.527 1.00 37.44  ? 110  ILE A CG1  1 
ATOM   1477 C CG2  . ILE A 1 110 ? 160.456 -10.197 -52.342 1.00 34.11  ? 110  ILE A CG2  1 
ATOM   1478 C CD1  . ILE A 1 110 ? 160.336 -11.472 -55.139 1.00 38.35  ? 110  ILE A CD1  1 
ATOM   1479 H H    . ILE A 1 110 ? 158.672 -7.843  -54.937 1.00 43.46  ? 110  ILE A H    1 
ATOM   1480 H HA   . ILE A 1 110 ? 157.949 -9.130  -52.756 1.00 40.56  ? 110  ILE A HA   1 
ATOM   1481 H HB   . ILE A 1 110 ? 160.488 -8.999  -54.011 1.00 42.70  ? 110  ILE A HB   1 
ATOM   1482 H HG12 . ILE A 1 110 ? 158.650 -11.149 -54.052 1.00 45.13  ? 110  ILE A HG12 1 
ATOM   1483 H HG13 . ILE A 1 110 ? 158.819 -10.126 -55.253 1.00 45.13  ? 110  ILE A HG13 1 
ATOM   1484 H HG21 . ILE A 1 110 ? 159.782 -10.716 -51.875 1.00 41.13  ? 110  ILE A HG21 1 
ATOM   1485 H HG22 . ILE A 1 110 ? 161.170 -10.779 -52.645 1.00 41.13  ? 110  ILE A HG22 1 
ATOM   1486 H HG23 . ILE A 1 110 ? 160.813 -9.512  -51.755 1.00 41.13  ? 110  ILE A HG23 1 
ATOM   1487 H HD11 . ILE A 1 110 ? 160.796 -11.947 -54.429 1.00 46.22  ? 110  ILE A HD11 1 
ATOM   1488 H HD12 . ILE A 1 110 ? 159.908 -12.104 -55.737 1.00 46.22  ? 110  ILE A HD12 1 
ATOM   1489 H HD13 . ILE A 1 110 ? 160.965 -10.923 -55.632 1.00 46.22  ? 110  ILE A HD13 1 
ATOM   1490 N N    . PRO A 1 111 ? 158.731 -7.851  -50.774 1.00 33.93  ? 111  PRO A N    1 
ATOM   1491 C CA   . PRO A 1 111 ? 159.145 -6.939  -49.700 1.00 39.52  ? 111  PRO A CA   1 
ATOM   1492 C C    . PRO A 1 111 ? 160.655 -6.891  -49.495 1.00 36.97  ? 111  PRO A C    1 
ATOM   1493 O O    . PRO A 1 111 ? 161.336 -7.903  -49.670 1.00 38.80  ? 111  PRO A O    1 
ATOM   1494 C CB   . PRO A 1 111 ? 158.478 -7.535  -48.454 1.00 36.70  ? 111  PRO A CB   1 
ATOM   1495 C CG   . PRO A 1 111 ? 157.365 -8.357  -48.961 1.00 40.88  ? 111  PRO A CG   1 
ATOM   1496 C CD   . PRO A 1 111 ? 157.815 -8.894  -50.278 1.00 38.21  ? 111  PRO A CD   1 
ATOM   1497 H HA   . PRO A 1 111 ? 158.805 -6.045  -49.858 1.00 47.62  ? 111  PRO A HA   1 
ATOM   1498 H HB2  . PRO A 1 111 ? 159.117 -8.084  -47.973 1.00 44.23  ? 111  PRO A HB2  1 
ATOM   1499 H HB3  . PRO A 1 111 ? 158.146 -6.820  -47.888 1.00 44.23  ? 111  PRO A HB3  1 
ATOM   1500 H HG2  . PRO A 1 111 ? 157.187 -9.081  -48.340 1.00 49.25  ? 111  PRO A HG2  1 
ATOM   1501 H HG3  . PRO A 1 111 ? 156.576 -7.803  -49.071 1.00 49.25  ? 111  PRO A HG3  1 
ATOM   1502 H HD2  . PRO A 1 111 ? 158.289 -9.732  -50.158 1.00 46.05  ? 111  PRO A HD2  1 
ATOM   1503 H HD3  . PRO A 1 111 ? 157.060 -8.995  -50.879 1.00 46.05  ? 111  PRO A HD3  1 
ATOM   1504 N N    . GLY A 1 112 ? 161.165 -5.719  -49.131 1.00 36.84  ? 112  GLY A N    1 
ATOM   1505 C CA   . GLY A 1 112 ? 162.561 -5.571  -48.763 1.00 34.58  ? 112  GLY A CA   1 
ATOM   1506 C C    . GLY A 1 112 ? 163.514 -5.392  -49.928 1.00 31.16  ? 112  GLY A C    1 
ATOM   1507 O O    . GLY A 1 112 ? 164.723 -5.269  -49.723 1.00 30.41  ? 112  GLY A O    1 
ATOM   1508 H H    . GLY A 1 112 ? 160.714 -4.988  -49.089 1.00 44.41  ? 112  GLY A H    1 
ATOM   1509 H HA2  . GLY A 1 112 ? 162.653 -4.801  -48.181 1.00 41.69  ? 112  GLY A HA2  1 
ATOM   1510 H HA3  . GLY A 1 112 ? 162.841 -6.357  -48.268 1.00 41.69  ? 112  GLY A HA3  1 
ATOM   1511 N N    . THR A 1 113 ? 162.981 -5.359  -51.146 1.00 34.02  ? 113  THR A N    1 
ATOM   1512 C CA   . THR A 1 113 ? 163.823 -5.340  -52.340 1.00 34.25  ? 113  THR A CA   1 
ATOM   1513 C C    . THR A 1 113 ? 163.872 -3.981  -53.024 1.00 32.15  ? 113  THR A C    1 
ATOM   1514 O O    . THR A 1 113 ? 162.967 -3.159  -52.886 1.00 34.96  ? 113  THR A O    1 
ATOM   1515 C CB   . THR A 1 113 ? 163.346 -6.370  -53.379 1.00 32.84  ? 113  THR A CB   1 
ATOM   1516 O OG1  . THR A 1 113 ? 162.099 -5.946  -53.942 1.00 33.02  ? 113  THR A OG1  1 
ATOM   1517 C CG2  . THR A 1 113 ? 163.183 -7.740  -52.737 1.00 31.11  ? 113  THR A CG2  1 
ATOM   1518 H H    . THR A 1 113 ? 162.137 -5.348  -51.308 1.00 41.02  ? 113  THR A H    1 
ATOM   1519 H HA   . THR A 1 113 ? 164.729 -5.575  -52.085 1.00 41.30  ? 113  THR A HA   1 
ATOM   1520 H HB   . THR A 1 113 ? 164.008 -6.443  -54.085 1.00 39.61  ? 113  THR A HB   1 
ATOM   1521 H HG1  . THR A 1 113 ? 161.520 -5.876  -53.338 1.00 39.83  ? 113  THR A HG1  1 
ATOM   1522 H HG21 . THR A 1 113 ? 162.529 -7.695  -52.022 1.00 37.53  ? 113  THR A HG21 1 
ATOM   1523 H HG22 . THR A 1 113 ? 162.882 -8.382  -53.399 1.00 37.53  ? 113  THR A HG22 1 
ATOM   1524 H HG23 . THR A 1 113 ? 164.030 -8.037  -52.371 1.00 37.53  ? 113  THR A HG23 1 
ATOM   1525 N N    . LEU A 1 114 ? 164.953 -3.767  -53.764 1.00 31.93  ? 114  LEU A N    1 
ATOM   1526 C CA   . LEU A 1 114 ? 165.121 -2.586  -54.596 1.00 31.81  ? 114  LEU A CA   1 
ATOM   1527 C C    . LEU A 1 114 ? 165.914 -2.996  -55.830 1.00 32.66  ? 114  LEU A C    1 
ATOM   1528 O O    . LEU A 1 114 ? 167.137 -3.121  -55.780 1.00 33.52  ? 114  LEU A O    1 
ATOM   1529 C CB   . LEU A 1 114 ? 165.848 -1.485  -53.824 1.00 27.41  ? 114  LEU A CB   1 
ATOM   1530 C CG   . LEU A 1 114 ? 166.231 -0.220  -54.598 1.00 23.21  ? 114  LEU A CG   1 
ATOM   1531 C CD1  . LEU A 1 114 ? 165.023 0.411   -55.271 1.00 26.05  ? 114  LEU A CD1  1 
ATOM   1532 C CD2  . LEU A 1 114 ? 166.893 0.778   -53.667 1.00 28.36  ? 114  LEU A CD2  1 
ATOM   1533 H H    . LEU A 1 114 ? 165.620 -4.308  -53.802 1.00 38.52  ? 114  LEU A H    1 
ATOM   1534 H HA   . LEU A 1 114 ? 164.254 -2.253  -54.876 1.00 38.37  ? 114  LEU A HA   1 
ATOM   1535 H HB2  . LEU A 1 114 ? 165.280 -1.208  -53.088 1.00 33.09  ? 114  LEU A HB2  1 
ATOM   1536 H HB3  . LEU A 1 114 ? 166.669 -1.860  -53.468 1.00 33.09  ? 114  LEU A HB3  1 
ATOM   1537 H HG   . LEU A 1 114 ? 166.870 -0.455  -55.289 1.00 28.05  ? 114  LEU A HG   1 
ATOM   1538 H HD11 . LEU A 1 114 ? 164.372 0.648   -54.592 1.00 31.46  ? 114  LEU A HD11 1 
ATOM   1539 H HD12 . LEU A 1 114 ? 165.308 1.206   -55.748 1.00 31.46  ? 114  LEU A HD12 1 
ATOM   1540 H HD13 . LEU A 1 114 ? 164.638 -0.228  -55.891 1.00 31.46  ? 114  LEU A HD13 1 
ATOM   1541 H HD21 . LEU A 1 114 ? 167.691 0.376   -53.290 1.00 34.23  ? 114  LEU A HD21 1 
ATOM   1542 H HD22 . LEU A 1 114 ? 167.129 1.572   -54.172 1.00 34.23  ? 114  LEU A HD22 1 
ATOM   1543 H HD23 . LEU A 1 114 ? 166.272 1.008   -52.958 1.00 34.23  ? 114  LEU A HD23 1 
ATOM   1544 N N    . PHE A 1 115 ? 165.206 -3.220  -56.932 1.00 31.64  ? 115  PHE A N    1 
ATOM   1545 C CA   . PHE A 1 115 ? 165.821 -3.730  -58.149 1.00 31.22  ? 115  PHE A CA   1 
ATOM   1546 C C    . PHE A 1 115 ? 166.473 -2.597  -58.927 1.00 30.07  ? 115  PHE A C    1 
ATOM   1547 O O    . PHE A 1 115 ? 165.975 -2.151  -59.960 1.00 31.50  ? 115  PHE A O    1 
ATOM   1548 C CB   . PHE A 1 115 ? 164.786 -4.466  -58.994 1.00 32.40  ? 115  PHE A CB   1 
ATOM   1549 C CG   . PHE A 1 115 ? 164.438 -5.825  -58.460 1.00 33.77  ? 115  PHE A CG   1 
ATOM   1550 C CD1  . PHE A 1 115 ? 163.710 -5.960  -57.293 1.00 32.69  ? 115  PHE A CD1  1 
ATOM   1551 C CD2  . PHE A 1 115 ? 164.852 -6.967  -59.119 1.00 32.02  ? 115  PHE A CD2  1 
ATOM   1552 C CE1  . PHE A 1 115 ? 163.395 -7.209  -56.798 1.00 33.04  ? 115  PHE A CE1  1 
ATOM   1553 C CE2  . PHE A 1 115 ? 164.541 -8.216  -58.627 1.00 30.67  ? 115  PHE A CE2  1 
ATOM   1554 C CZ   . PHE A 1 115 ? 163.811 -8.337  -57.467 1.00 31.72  ? 115  PHE A CZ   1 
ATOM   1555 H H    . PHE A 1 115 ? 164.359 -3.082  -57.000 1.00 38.16  ? 115  PHE A H    1 
ATOM   1556 H HA   . PHE A 1 115 ? 166.515 -4.364  -57.908 1.00 37.66  ? 115  PHE A HA   1 
ATOM   1557 H HB2  . PHE A 1 115 ? 163.972 -3.940  -59.022 1.00 39.08  ? 115  PHE A HB2  1 
ATOM   1558 H HB3  . PHE A 1 115 ? 165.137 -4.580  -59.891 1.00 39.08  ? 115  PHE A HB3  1 
ATOM   1559 H HD1  . PHE A 1 115 ? 163.426 -5.200  -56.838 1.00 39.43  ? 115  PHE A HD1  1 
ATOM   1560 H HD2  . PHE A 1 115 ? 165.345 -6.891  -59.904 1.00 38.62  ? 115  PHE A HD2  1 
ATOM   1561 H HE1  . PHE A 1 115 ? 162.902 -7.288  -56.013 1.00 39.85  ? 115  PHE A HE1  1 
ATOM   1562 H HE2  . PHE A 1 115 ? 164.822 -8.978  -59.081 1.00 37.00  ? 115  PHE A HE2  1 
ATOM   1563 H HZ   . PHE A 1 115 ? 163.599 -9.180  -57.135 1.00 38.26  ? 115  PHE A HZ   1 
ATOM   1564 N N    . LEU A 1 116 ? 167.607 -2.147  -58.406 1.00 29.74  ? 116  LEU A N    1 
ATOM   1565 C CA   . LEU A 1 116 ? 168.308 -0.993  -58.937 1.00 31.07  ? 116  LEU A CA   1 
ATOM   1566 C C    . LEU A 1 116 ? 169.796 -1.196  -58.713 1.00 33.56  ? 116  LEU A C    1 
ATOM   1567 O O    . LEU A 1 116 ? 170.210 -1.608  -57.629 1.00 38.31  ? 116  LEU A O    1 
ATOM   1568 C CB   . LEU A 1 116 ? 167.832 0.268   -58.216 1.00 26.98  ? 116  LEU A CB   1 
ATOM   1569 C CG   . LEU A 1 116 ? 168.439 1.606   -58.634 1.00 26.96  ? 116  LEU A CG   1 
ATOM   1570 C CD1  . LEU A 1 116 ? 168.064 1.940   -60.064 1.00 34.43  ? 116  LEU A CD1  1 
ATOM   1571 C CD2  . LEU A 1 116 ? 167.973 2.699   -57.692 1.00 28.34  ? 116  LEU A CD2  1 
ATOM   1572 H H    . LEU A 1 116 ? 167.997 -2.504  -57.729 1.00 35.88  ? 116  LEU A H    1 
ATOM   1573 H HA   . LEU A 1 116 ? 168.137 -0.903  -59.887 1.00 37.48  ? 116  LEU A HA   1 
ATOM   1574 H HB2  . LEU A 1 116 ? 166.874 0.341   -58.345 1.00 32.57  ? 116  LEU A HB2  1 
ATOM   1575 H HB3  . LEU A 1 116 ? 168.017 0.158   -57.270 1.00 32.57  ? 116  LEU A HB3  1 
ATOM   1576 H HG   . LEU A 1 116 ? 169.406 1.550   -58.579 1.00 32.55  ? 116  LEU A HG   1 
ATOM   1577 H HD11 . LEU A 1 116 ? 167.098 1.994   -60.132 1.00 41.51  ? 116  LEU A HD11 1 
ATOM   1578 H HD12 . LEU A 1 116 ? 168.461 2.792   -60.303 1.00 41.51  ? 116  LEU A HD12 1 
ATOM   1579 H HD13 . LEU A 1 116 ? 168.400 1.242   -60.649 1.00 41.51  ? 116  LEU A HD13 1 
ATOM   1580 H HD21 . LEU A 1 116 ? 168.257 2.481   -56.790 1.00 34.20  ? 116  LEU A HD21 1 
ATOM   1581 H HD22 . LEU A 1 116 ? 168.365 3.542   -57.968 1.00 34.20  ? 116  LEU A HD22 1 
ATOM   1582 H HD23 . LEU A 1 116 ? 167.005 2.756   -57.729 1.00 34.20  ? 116  LEU A HD23 1 
ATOM   1583 N N    . ALA A 1 117 ? 170.592 -0.912  -59.741 1.00 27.72  ? 117  ALA A N    1 
ATOM   1584 C CA   . ALA A 1 117 ? 172.035 -1.118  -59.687 1.00 28.94  ? 117  ALA A CA   1 
ATOM   1585 C C    . ALA A 1 117 ? 172.653 -0.496  -58.441 1.00 30.15  ? 117  ALA A C    1 
ATOM   1586 O O    . ALA A 1 117 ? 172.258 0.589   -58.013 1.00 29.24  ? 117  ALA A O    1 
ATOM   1587 C CB   . ALA A 1 117 ? 172.691 -0.555  -60.932 1.00 26.34  ? 117  ALA A CB   1 
ATOM   1588 H H    . ALA A 1 117 ? 170.315 -0.594  -60.490 1.00 33.46  ? 117  ALA A H    1 
ATOM   1589 H HA   . ALA A 1 117 ? 172.214 -2.072  -59.662 1.00 34.93  ? 117  ALA A HA   1 
ATOM   1590 H HB1  . ALA A 1 117 ? 172.504 0.395   -60.985 1.00 31.80  ? 117  ALA A HB1  1 
ATOM   1591 H HB2  . ALA A 1 117 ? 173.649 -0.702  -60.878 1.00 31.80  ? 117  ALA A HB2  1 
ATOM   1592 H HB3  . ALA A 1 117 ? 172.331 -1.008  -61.711 1.00 31.80  ? 117  ALA A HB3  1 
ATOM   1593 N N    . GLY A 1 118 ? 173.617 -1.207  -57.861 1.00 29.37  ? 118  GLY A N    1 
ATOM   1594 C CA   . GLY A 1 118 ? 174.319 -0.745  -56.677 1.00 26.67  ? 118  GLY A CA   1 
ATOM   1595 C C    . GLY A 1 118 ? 174.608 -1.867  -55.696 1.00 31.20  ? 118  GLY A C    1 
ATOM   1596 O O    . GLY A 1 118 ? 175.378 -1.688  -54.754 1.00 30.17  ? 118  GLY A O    1 
ATOM   1597 H H    . GLY A 1 118 ? 173.885 -1.973  -58.144 1.00 35.44  ? 118  GLY A H    1 
ATOM   1598 H HA2  . GLY A 1 118 ? 175.162 -0.342  -56.938 1.00 32.20  ? 118  GLY A HA2  1 
ATOM   1599 H HA3  . GLY A 1 118 ? 173.784 -0.074  -56.226 1.00 32.20  ? 118  GLY A HA3  1 
ATOM   1600 N N    . GLY A 1 119 ? 173.993 -3.025  -55.924 1.00 33.34  ? 119  GLY A N    1 
ATOM   1601 C CA   . GLY A 1 119 ? 174.156 -4.178  -55.057 1.00 32.76  ? 119  GLY A CA   1 
ATOM   1602 C C    . GLY A 1 119 ? 174.803 -5.340  -55.783 1.00 31.39  ? 119  GLY A C    1 
ATOM   1603 O O    . GLY A 1 119 ? 174.434 -5.646  -56.918 1.00 33.02  ? 119  GLY A O    1 
ATOM   1604 H H    . GLY A 1 119 ? 173.466 -3.166  -56.589 1.00 40.21  ? 119  GLY A H    1 
ATOM   1605 H HA2  . GLY A 1 119 ? 174.713 -3.939  -54.299 1.00 39.51  ? 119  GLY A HA2  1 
ATOM   1606 H HA3  . GLY A 1 119 ? 173.290 -4.463  -54.727 1.00 39.51  ? 119  GLY A HA3  1 
ATOM   1607 N N    . THR A 1 120 ? 175.769 -5.985  -55.134 1.00 26.39  ? 120  THR A N    1 
ATOM   1608 C CA   . THR A 1 120 ? 176.450 -7.135  -55.717 1.00 28.85  ? 120  THR A CA   1 
ATOM   1609 C C    . THR A 1 120 ? 176.710 -8.197  -54.646 1.00 28.70  ? 120  THR A C    1 
ATOM   1610 O O    . THR A 1 120 ? 176.996 -7.862  -53.494 1.00 29.99  ? 120  THR A O    1 
ATOM   1611 C CB   . THR A 1 120 ? 177.780 -6.726  -56.384 1.00 29.55  ? 120  THR A CB   1 
ATOM   1612 O OG1  . THR A 1 120 ? 178.365 -7.862  -57.031 1.00 36.39  ? 120  THR A OG1  1 
ATOM   1613 C CG2  . THR A 1 120 ? 178.754 -6.171  -55.359 1.00 29.98  ? 120  THR A CG2  1 
ATOM   1614 H H    . THR A 1 120 ? 176.051 -5.773  -54.349 1.00 31.87  ? 120  THR A H    1 
ATOM   1615 H HA   . THR A 1 120 ? 175.881 -7.528  -56.398 1.00 34.81  ? 120  THR A HA   1 
ATOM   1616 H HB   . THR A 1 120 ? 177.608 -6.036  -57.043 1.00 35.66  ? 120  THR A HB   1 
ATOM   1617 H HG1  . THR A 1 120 ? 179.089 -7.643  -57.395 1.00 43.86  ? 120  THR A HG1  1 
ATOM   1618 H HG21 . THR A 1 120 ? 178.942 -6.841  -54.684 1.00 36.17  ? 120  THR A HG21 1 
ATOM   1619 H HG22 . THR A 1 120 ? 179.583 -5.918  -55.793 1.00 36.17  ? 120  THR A HG22 1 
ATOM   1620 H HG23 . THR A 1 120 ? 178.372 -5.389  -54.929 1.00 36.17  ? 120  THR A HG23 1 
ATOM   1621 N N    . PRO A 1 121 ? 176.603 -9.483  -55.021 1.00 31.58  ? 121  PRO A N    1 
ATOM   1622 C CA   . PRO A 1 121 ? 176.742 -10.560 -54.038 1.00 33.76  ? 121  PRO A CA   1 
ATOM   1623 C C    . PRO A 1 121 ? 178.179 -10.997 -53.763 1.00 33.43  ? 121  PRO A C    1 
ATOM   1624 O O    . PRO A 1 121 ? 179.082 -10.771 -54.570 1.00 33.53  ? 121  PRO A O    1 
ATOM   1625 C CB   . PRO A 1 121 ? 175.975 -11.709 -54.688 1.00 37.09  ? 121  PRO A CB   1 
ATOM   1626 C CG   . PRO A 1 121 ? 176.155 -11.483 -56.132 1.00 39.72  ? 121  PRO A CG   1 
ATOM   1627 C CD   . PRO A 1 121 ? 176.139 -9.998  -56.321 1.00 36.17  ? 121  PRO A CD   1 
ATOM   1628 H HA   . PRO A 1 121 ? 176.313 -10.316 -53.203 1.00 40.71  ? 121  PRO A HA   1 
ATOM   1629 H HB2  . PRO A 1 121 ? 176.361 -12.558 -54.419 1.00 44.70  ? 121  PRO A HB2  1 
ATOM   1630 H HB3  . PRO A 1 121 ? 175.038 -11.661 -54.444 1.00 44.70  ? 121  PRO A HB3  1 
ATOM   1631 H HG2  . PRO A 1 121 ? 177.006 -11.853 -56.415 1.00 47.86  ? 121  PRO A HG2  1 
ATOM   1632 H HG3  . PRO A 1 121 ? 175.425 -11.896 -56.619 1.00 47.86  ? 121  PRO A HG3  1 
ATOM   1633 H HD2  . PRO A 1 121 ? 176.754 -9.740  -57.025 1.00 43.60  ? 121  PRO A HD2  1 
ATOM   1634 H HD3  . PRO A 1 121 ? 175.238 -9.691  -56.504 1.00 43.60  ? 121  PRO A HD3  1 
ATOM   1635 N N    . VAL A 1 122 ? 178.361 -11.623 -52.605 1.00 30.88  ? 122  VAL A N    1 
ATOM   1636 C CA   . VAL A 1 122 ? 179.616 -12.257 -52.226 1.00 29.34  ? 122  VAL A CA   1 
ATOM   1637 C C    . VAL A 1 122 ? 179.298 -13.700 -51.873 1.00 29.41  ? 122  VAL A C    1 
ATOM   1638 O O    . VAL A 1 122 ? 178.291 -13.968 -51.214 1.00 32.56  ? 122  VAL A O    1 
ATOM   1639 C CB   . VAL A 1 122 ? 180.257 -11.560 -51.011 1.00 33.12  ? 122  VAL A CB   1 
ATOM   1640 C CG1  . VAL A 1 122 ? 181.555 -12.251 -50.610 1.00 34.33  ? 122  VAL A CG1  1 
ATOM   1641 C CG2  . VAL A 1 122 ? 180.517 -10.097 -51.318 1.00 37.64  ? 122  VAL A CG2  1 
ATOM   1642 H H    . VAL A 1 122 ? 177.751 -11.695 -52.004 1.00 37.25  ? 122  VAL A H    1 
ATOM   1643 H HA   . VAL A 1 122 ? 180.238 -12.240 -52.970 1.00 35.41  ? 122  VAL A HA   1 
ATOM   1644 H HB   . VAL A 1 122 ? 179.646 -11.607 -50.260 1.00 39.94  ? 122  VAL A HB   1 
ATOM   1645 H HG11 . VAL A 1 122 ? 182.174 -12.217 -51.356 1.00 41.39  ? 122  VAL A HG11 1 
ATOM   1646 H HG12 . VAL A 1 122 ? 181.933 -11.791 -49.845 1.00 41.39  ? 122  VAL A HG12 1 
ATOM   1647 H HG13 . VAL A 1 122 ? 181.363 -13.174 -50.380 1.00 41.39  ? 122  VAL A HG13 1 
ATOM   1648 H HG21 . VAL A 1 122 ? 179.674 -9.664  -51.527 1.00 45.37  ? 122  VAL A HG21 1 
ATOM   1649 H HG22 . VAL A 1 122 ? 180.920 -9.679  -50.541 1.00 45.37  ? 122  VAL A HG22 1 
ATOM   1650 H HG23 . VAL A 1 122 ? 181.118 -10.035 -52.076 1.00 45.37  ? 122  VAL A HG23 1 
ATOM   1651 N N    . THR A 1 123 ? 180.151 -14.627 -52.302 1.00 26.64  ? 123  THR A N    1 
ATOM   1652 C CA   . THR A 1 123 ? 179.874 -16.050 -52.139 1.00 27.07  ? 123  THR A CA   1 
ATOM   1653 C C    . THR A 1 123 ? 180.900 -16.766 -51.269 1.00 32.29  ? 123  THR A C    1 
ATOM   1654 O O    . THR A 1 123 ? 182.000 -16.268 -51.027 1.00 33.75  ? 123  THR A O    1 
ATOM   1655 C CB   . THR A 1 123 ? 179.832 -16.789 -53.497 1.00 31.54  ? 123  THR A CB   1 
ATOM   1656 O OG1  . THR A 1 123 ? 181.154 -16.879 -54.040 1.00 31.55  ? 123  THR A OG1  1 
ATOM   1657 C CG2  . THR A 1 123 ? 178.918 -16.078 -54.480 1.00 33.54  ? 123  THR A CG2  1 
ATOM   1658 H H    . THR A 1 123 ? 180.899 -14.456 -52.691 1.00 32.16  ? 123  THR A H    1 
ATOM   1659 H HA   . THR A 1 123 ? 179.006 -16.153 -51.718 1.00 32.68  ? 123  THR A HA   1 
ATOM   1660 H HB   . THR A 1 123 ? 179.486 -17.684 -53.359 1.00 38.04  ? 123  THR A HB   1 
ATOM   1661 H HG1  . THR A 1 123 ? 181.135 -17.280 -54.778 1.00 38.06  ? 123  THR A HG1  1 
ATOM   1662 H HG21 . THR A 1 123 ? 179.236 -15.175 -54.634 1.00 40.45  ? 123  THR A HG21 1 
ATOM   1663 H HG22 . THR A 1 123 ? 178.905 -16.556 -55.324 1.00 40.45  ? 123  THR A HG22 1 
ATOM   1664 H HG23 . THR A 1 123 ? 178.016 -16.040 -54.126 1.00 40.45  ? 123  THR A HG23 1 
ATOM   1665 N N    . ALA A 1 124 ? 180.503 -17.944 -50.803 1.00 36.35  ? 124  ALA A N    1 
ATOM   1666 C CA   . ALA A 1 124 ? 181.400 -18.886 -50.157 1.00 37.50  ? 124  ALA A CA   1 
ATOM   1667 C C    . ALA A 1 124 ? 180.977 -20.285 -50.584 1.00 39.92  ? 124  ALA A C    1 
ATOM   1668 O O    . ALA A 1 124 ? 179.830 -20.684 -50.378 1.00 46.40  ? 124  ALA A O    1 
ATOM   1669 C CB   . ALA A 1 124 ? 181.333 -18.744 -48.654 1.00 40.60  ? 124  ALA A CB   1 
ATOM   1670 H H    . ALA A 1 124 ? 179.692 -18.227 -50.853 1.00 43.81  ? 124  ALA A H    1 
ATOM   1671 H HA   . ALA A 1 124 ? 182.312 -18.729 -50.448 1.00 45.20  ? 124  ALA A HA   1 
ATOM   1672 H HB1  . ALA A 1 124 ? 180.426 -18.919 -48.361 1.00 48.92  ? 124  ALA A HB1  1 
ATOM   1673 H HB2  . ALA A 1 124 ? 181.941 -19.383 -48.249 1.00 48.92  ? 124  ALA A HB2  1 
ATOM   1674 H HB3  . ALA A 1 124 ? 181.592 -17.841 -48.411 1.00 48.92  ? 124  ALA A HB3  1 
ATOM   1675 N N    . LYS A 1 125 ? 181.909 -21.022 -51.180 1.00 41.47  ? 125  LYS A N    1 
ATOM   1676 C CA   . LYS A 1 125 ? 181.625 -22.334 -51.755 1.00 48.81  ? 125  LYS A CA   1 
ATOM   1677 C C    . LYS A 1 125 ? 180.468 -22.277 -52.763 1.00 47.14  ? 125  LYS A C    1 
ATOM   1678 O O    . LYS A 1 125 ? 179.584 -23.133 -52.772 1.00 52.11  ? 125  LYS A O    1 
ATOM   1679 C CB   . LYS A 1 125 ? 181.360 -23.365 -50.645 1.00 58.73  ? 125  LYS A CB   1 
ATOM   1680 C CG   . LYS A 1 125 ? 182.360 -24.517 -50.638 1.00 72.70  ? 125  LYS A CG   1 
ATOM   1681 C CD   . LYS A 1 125 ? 181.733 -25.831 -50.189 1.00 79.80  ? 125  LYS A CD   1 
ATOM   1682 C CE   . LYS A 1 125 ? 181.418 -25.837 -48.704 1.00 79.33  ? 125  LYS A CE   1 
ATOM   1683 N NZ   . LYS A 1 125 ? 180.840 -27.143 -48.280 1.00 79.73  ? 125  LYS A NZ   1 
ATOM   1684 H H    . LYS A 1 125 ? 182.729 -20.779 -51.266 1.00 49.96  ? 125  LYS A H    1 
ATOM   1685 H HA   . LYS A 1 125 ? 182.412 -22.629 -52.239 1.00 58.77  ? 125  LYS A HA   1 
ATOM   1686 H HB2  . LYS A 1 125 ? 181.412 -22.920 -49.785 1.00 70.68  ? 125  LYS A HB2  1 
ATOM   1687 H HB3  . LYS A 1 125 ? 180.474 -23.740 -50.770 1.00 70.68  ? 125  LYS A HB3  1 
ATOM   1688 H HG2  . LYS A 1 125 ? 182.708 -24.641 -51.535 1.00 87.44  ? 125  LYS A HG2  1 
ATOM   1689 H HG3  . LYS A 1 125 ? 183.083 -24.305 -50.027 1.00 87.44  ? 125  LYS A HG3  1 
ATOM   1690 H HD2  . LYS A 1 125 ? 180.904 -25.969 -50.674 1.00 95.96  ? 125  LYS A HD2  1 
ATOM   1691 H HD3  . LYS A 1 125 ? 182.351 -26.556 -50.370 1.00 95.96  ? 125  LYS A HD3  1 
ATOM   1692 H HE2  . LYS A 1 125 ? 182.235 -25.689 -48.202 1.00 95.39  ? 125  LYS A HE2  1 
ATOM   1693 H HE3  . LYS A 1 125 ? 180.772 -25.140 -48.510 1.00 95.39  ? 125  LYS A HE3  1 
ATOM   1694 H HZ1  . LYS A 1 125 ? 181.417 -27.799 -48.446 1.00 95.87  ? 125  LYS A HZ1  1 
ATOM   1695 H HZ2  . LYS A 1 125 ? 180.662 -27.128 -47.408 1.00 95.87  ? 125  LYS A HZ2  1 
ATOM   1696 H HZ3  . LYS A 1 125 ? 180.086 -27.300 -48.726 1.00 95.87  ? 125  LYS A HZ3  1 
ATOM   1697 N N    . GLY A 1 126 ? 180.488 -21.261 -53.622 1.00 43.02  ? 126  GLY A N    1 
ATOM   1698 C CA   . GLY A 1 126 ? 179.511 -21.145 -54.691 1.00 51.57  ? 126  GLY A CA   1 
ATOM   1699 C C    . GLY A 1 126 ? 178.123 -20.736 -54.234 1.00 50.34  ? 126  GLY A C    1 
ATOM   1700 O O    . GLY A 1 126 ? 177.191 -20.695 -55.038 1.00 52.99  ? 126  GLY A O    1 
ATOM   1701 H H    . GLY A 1 126 ? 181.064 -20.623 -53.604 1.00 51.82  ? 126  GLY A H    1 
ATOM   1702 H HA2  . GLY A 1 126 ? 179.821 -20.487 -55.333 1.00 62.09  ? 126  GLY A HA2  1 
ATOM   1703 H HA3  . GLY A 1 126 ? 179.437 -21.998 -55.147 1.00 62.09  ? 126  GLY A HA3  1 
ATOM   1704 N N    . ALA A 1 127 ? 177.984 -20.436 -52.947 1.00 42.59  ? 127  ALA A N    1 
ATOM   1705 C CA   . ALA A 1 127 ? 176.701 -20.033 -52.389 1.00 35.83  ? 127  ALA A CA   1 
ATOM   1706 C C    . ALA A 1 127 ? 176.789 -18.611 -51.859 1.00 31.62  ? 127  ALA A C    1 
ATOM   1707 O O    . ALA A 1 127 ? 177.810 -18.226 -51.293 1.00 33.51  ? 127  ALA A O    1 
ATOM   1708 C CB   . ALA A 1 127 ? 176.299 -20.972 -51.281 1.00 40.81  ? 127  ALA A CB   1 
ATOM   1709 H H    . ALA A 1 127 ? 178.624 -20.460 -52.372 1.00 51.30  ? 127  ALA A H    1 
ATOM   1710 H HA   . ALA A 1 127 ? 176.022 -20.064 -53.081 1.00 43.20  ? 127  ALA A HA   1 
ATOM   1711 H HB1  . ALA A 1 127 ? 176.975 -20.946 -50.585 1.00 49.18  ? 127  ALA A HB1  1 
ATOM   1712 H HB2  . ALA A 1 127 ? 175.444 -20.688 -50.922 1.00 49.18  ? 127  ALA A HB2  1 
ATOM   1713 H HB3  . ALA A 1 127 ? 176.227 -21.870 -51.639 1.00 49.18  ? 127  ALA A HB3  1 
ATOM   1714 N N    . PRO A 1 128 ? 175.713 -17.826 -52.027 1.00 28.26  ? 128  PRO A N    1 
ATOM   1715 C CA   . PRO A 1 128 ? 175.726 -16.450 -51.527 1.00 29.62  ? 128  PRO A CA   1 
ATOM   1716 C C    . PRO A 1 128 ? 175.772 -16.411 -50.005 1.00 31.21  ? 128  PRO A C    1 
ATOM   1717 O O    . PRO A 1 128 ? 175.067 -17.185 -49.356 1.00 29.55  ? 128  PRO A O    1 
ATOM   1718 C CB   . PRO A 1 128 ? 174.396 -15.886 -52.030 1.00 28.20  ? 128  PRO A CB   1 
ATOM   1719 C CG   . PRO A 1 128 ? 173.513 -17.070 -52.152 1.00 30.76  ? 128  PRO A CG   1 
ATOM   1720 C CD   . PRO A 1 128 ? 174.402 -18.191 -52.591 1.00 32.24  ? 128  PRO A CD   1 
ATOM   1721 H HA   . PRO A 1 128 ? 176.466 -15.947 -51.901 1.00 35.74  ? 128  PRO A HA   1 
ATOM   1722 H HB2  . PRO A 1 128 ? 174.041 -15.256 -51.384 1.00 34.04  ? 128  PRO A HB2  1 
ATOM   1723 H HB3  . PRO A 1 128 ? 174.525 -15.461 -52.892 1.00 34.04  ? 128  PRO A HB3  1 
ATOM   1724 H HG2  . PRO A 1 128 ? 173.113 -17.268 -51.291 1.00 37.11  ? 128  PRO A HG2  1 
ATOM   1725 H HG3  . PRO A 1 128 ? 172.828 -16.897 -52.816 1.00 37.11  ? 128  PRO A HG3  1 
ATOM   1726 H HD2  . PRO A 1 128 ? 174.095 -19.032 -52.218 1.00 38.89  ? 128  PRO A HD2  1 
ATOM   1727 H HD3  . PRO A 1 128 ? 174.448 -18.227 -53.559 1.00 38.89  ? 128  PRO A HD3  1 
ATOM   1728 N N    . VAL A 1 129 ? 176.596 -15.526 -49.453 1.00 33.02  ? 129  VAL A N    1 
ATOM   1729 C CA   . VAL A 1 129 ? 176.706 -15.372 -48.006 1.00 32.99  ? 129  VAL A CA   1 
ATOM   1730 C C    . VAL A 1 129 ? 176.449 -13.929 -47.598 1.00 28.64  ? 129  VAL A C    1 
ATOM   1731 O O    . VAL A 1 129 ? 176.080 -13.650 -46.458 1.00 27.86  ? 129  VAL A O    1 
ATOM   1732 C CB   . VAL A 1 129 ? 178.093 -15.796 -47.487 1.00 30.16  ? 129  VAL A CB   1 
ATOM   1733 C CG1  . VAL A 1 129 ? 178.232 -17.306 -47.522 1.00 29.50  ? 129  VAL A CG1  1 
ATOM   1734 C CG2  . VAL A 1 129 ? 179.202 -15.124 -48.287 1.00 33.58  ? 129  VAL A CG2  1 
ATOM   1735 H H    . VAL A 1 129 ? 177.107 -14.997 -49.899 1.00 39.82  ? 129  VAL A H    1 
ATOM   1736 H HA   . VAL A 1 129 ? 176.039 -15.931 -47.576 1.00 39.79  ? 129  VAL A HA   1 
ATOM   1737 H HB   . VAL A 1 129 ? 178.181 -15.512 -46.564 1.00 36.39  ? 129  VAL A HB   1 
ATOM   1738 H HG11 . VAL A 1 129 ? 178.125 -17.612 -48.436 1.00 35.60  ? 129  VAL A HG11 1 
ATOM   1739 H HG12 . VAL A 1 129 ? 179.111 -17.550 -47.192 1.00 35.60  ? 129  VAL A HG12 1 
ATOM   1740 H HG13 . VAL A 1 129 ? 177.547 -17.699 -46.959 1.00 35.60  ? 129  VAL A HG13 1 
ATOM   1741 H HG21 . VAL A 1 129 ? 179.114 -14.162 -48.203 1.00 40.49  ? 129  VAL A HG21 1 
ATOM   1742 H HG22 . VAL A 1 129 ? 180.061 -15.410 -47.938 1.00 40.49  ? 129  VAL A HG22 1 
ATOM   1743 H HG23 . VAL A 1 129 ? 179.121 -15.383 -49.219 1.00 40.49  ? 129  VAL A HG23 1 
ATOM   1744 N N    . ALA A 1 130 ? 176.648 -13.014 -48.536 1.00 27.26  ? 130  ALA A N    1 
ATOM   1745 C CA   . ALA A 1 130 ? 176.432 -11.604 -48.267 1.00 27.05  ? 130  ALA A CA   1 
ATOM   1746 C C    . ALA A 1 130 ? 176.150 -10.840 -49.546 1.00 28.78  ? 130  ALA A C    1 
ATOM   1747 O O    . ALA A 1 130 ? 176.496 -11.282 -50.642 1.00 27.79  ? 130  ALA A O    1 
ATOM   1748 C CB   . ALA A 1 130 ? 177.637 -11.008 -47.565 1.00 28.02  ? 130  ALA A CB   1 
ATOM   1749 H H    . ALA A 1 130 ? 176.909 -13.185 -49.337 1.00 32.91  ? 130  ALA A H    1 
ATOM   1750 H HA   . ALA A 1 130 ? 175.664 -11.507 -47.682 1.00 32.67  ? 130  ALA A HA   1 
ATOM   1751 H HB1  . ALA A 1 130 ? 178.415 -11.109 -48.135 1.00 33.82  ? 130  ALA A HB1  1 
ATOM   1752 H HB2  . ALA A 1 130 ? 177.470 -10.068 -47.395 1.00 33.82  ? 130  ALA A HB2  1 
ATOM   1753 H HB3  . ALA A 1 130 ? 177.777 -11.476 -46.727 1.00 33.82  ? 130  ALA A HB3  1 
ATOM   1754 N N    . GLY A 1 131 ? 175.504 -9.692  -49.384 1.00 26.62  ? 131  GLY A N    1 
ATOM   1755 C CA   . GLY A 1 131 ? 175.344 -8.730  -50.453 1.00 26.41  ? 131  GLY A CA   1 
ATOM   1756 C C    . GLY A 1 131 ? 175.940 -7.419  -49.993 1.00 26.04  ? 131  GLY A C    1 
ATOM   1757 O O    . GLY A 1 131 ? 175.821 -7.060  -48.823 1.00 26.38  ? 131  GLY A O    1 
ATOM   1758 H H    . GLY A 1 131 ? 175.142 -9.446  -48.643 1.00 32.15  ? 131  GLY A H    1 
ATOM   1759 H HA2  . GLY A 1 131 ? 175.806 -9.031  -51.251 1.00 31.89  ? 131  GLY A HA2  1 
ATOM   1760 H HA3  . GLY A 1 131 ? 174.404 -8.603  -50.655 1.00 31.89  ? 131  GLY A HA3  1 
ATOM   1761 N N    . ILE A 1 132 ? 176.601 -6.719  -50.906 1.00 25.79  ? 132  ILE A N    1 
ATOM   1762 C CA   . ILE A 1 132 ? 177.161 -5.407  -50.614 1.00 24.84  ? 132  ILE A CA   1 
ATOM   1763 C C    . ILE A 1 132 ? 176.409 -4.376  -51.437 1.00 29.05  ? 132  ILE A C    1 
ATOM   1764 O O    . ILE A 1 132 ? 176.405 -4.438  -52.665 1.00 31.86  ? 132  ILE A O    1 
ATOM   1765 C CB   . ILE A 1 132 ? 178.656 -5.337  -50.950 1.00 28.89  ? 132  ILE A CB   1 
ATOM   1766 C CG1  . ILE A 1 132 ? 179.428 -6.394  -50.162 1.00 29.99  ? 132  ILE A CG1  1 
ATOM   1767 C CG2  . ILE A 1 132 ? 179.207 -3.958  -50.623 1.00 27.04  ? 132  ILE A CG2  1 
ATOM   1768 C CD1  . ILE A 1 132 ? 180.829 -6.626  -50.673 1.00 34.79  ? 132  ILE A CD1  1 
ATOM   1769 H H    . ILE A 1 132 ? 176.742 -6.986  -51.712 1.00 31.15  ? 132  ILE A H    1 
ATOM   1770 H HA   . ILE A 1 132 ? 177.042 -5.202  -49.674 1.00 30.01  ? 132  ILE A HA   1 
ATOM   1771 H HB   . ILE A 1 132 ? 178.773 -5.505  -51.899 1.00 34.87  ? 132  ILE A HB   1 
ATOM   1772 H HG12 . ILE A 1 132 ? 179.493 -6.110  -49.237 1.00 36.18  ? 132  ILE A HG12 1 
ATOM   1773 H HG13 . ILE A 1 132 ? 178.949 -7.236  -50.215 1.00 36.18  ? 132  ILE A HG13 1 
ATOM   1774 H HG21 . ILE A 1 132 ? 179.083 -3.785  -49.676 1.00 32.65  ? 132  ILE A HG21 1 
ATOM   1775 H HG22 . ILE A 1 132 ? 180.152 -3.935  -50.842 1.00 32.65  ? 132  ILE A HG22 1 
ATOM   1776 H HG23 . ILE A 1 132 ? 178.730 -3.295  -51.146 1.00 32.65  ? 132  ILE A HG23 1 
ATOM   1777 H HD11 . ILE A 1 132 ? 181.326 -5.795  -50.617 1.00 41.95  ? 132  ILE A HD11 1 
ATOM   1778 H HD12 . ILE A 1 132 ? 181.255 -7.305  -50.128 1.00 41.95  ? 132  ILE A HD12 1 
ATOM   1779 H HD13 . ILE A 1 132 ? 180.783 -6.922  -51.596 1.00 41.95  ? 132  ILE A HD13 1 
ATOM   1780 N N    . GLY A 1 133 ? 175.777 -3.431  -50.748 1.00 26.81  ? 133  GLY A N    1 
ATOM   1781 C CA   . GLY A 1 133 ? 174.952 -2.427  -51.391 1.00 25.70  ? 133  GLY A CA   1 
ATOM   1782 C C    . GLY A 1 133 ? 175.504 -1.026  -51.232 1.00 28.68  ? 133  GLY A C    1 
ATOM   1783 O O    . GLY A 1 133 ? 176.022 -0.662  -50.177 1.00 27.70  ? 133  GLY A O    1 
ATOM   1784 H H    . GLY A 1 133 ? 175.813 -3.353  -49.892 1.00 32.37  ? 133  GLY A H    1 
ATOM   1785 H HA2  . GLY A 1 133 ? 174.885 -2.624  -52.339 1.00 31.04  ? 133  GLY A HA2  1 
ATOM   1786 H HA3  . GLY A 1 133 ? 174.061 -2.450  -51.010 1.00 31.04  ? 133  GLY A HA3  1 
ATOM   1787 N N    . VAL A 1 134 ? 175.388 -0.241  -52.297 1.00 28.20  ? 134  VAL A N    1 
ATOM   1788 C CA   . VAL A 1 134 ? 175.839 1.142   -52.298 1.00 26.52  ? 134  VAL A CA   1 
ATOM   1789 C C    . VAL A 1 134 ? 174.777 2.015   -52.949 1.00 27.30  ? 134  VAL A C    1 
ATOM   1790 O O    . VAL A 1 134 ? 174.088 1.587   -53.875 1.00 29.20  ? 134  VAL A O    1 
ATOM   1791 C CB   . VAL A 1 134 ? 177.168 1.295   -53.062 1.00 30.40  ? 134  VAL A CB   1 
ATOM   1792 C CG1  . VAL A 1 134 ? 177.653 2.738   -53.026 1.00 31.58  ? 134  VAL A CG1  1 
ATOM   1793 C CG2  . VAL A 1 134 ? 178.222 0.382   -52.470 1.00 29.82  ? 134  VAL A CG2  1 
ATOM   1794 H H    . VAL A 1 134 ? 175.045 -0.493  -53.044 1.00 34.04  ? 134  VAL A H    1 
ATOM   1795 H HA   . VAL A 1 134 ? 175.970 1.442   -51.385 1.00 32.02  ? 134  VAL A HA   1 
ATOM   1796 H HB   . VAL A 1 134 ? 177.034 1.043   -53.989 1.00 36.68  ? 134  VAL A HB   1 
ATOM   1797 H HG11 . VAL A 1 134 ? 177.787 3.002   -52.102 1.00 38.10  ? 134  VAL A HG11 1 
ATOM   1798 H HG12 . VAL A 1 134 ? 178.489 2.802   -53.514 1.00 38.10  ? 134  VAL A HG12 1 
ATOM   1799 H HG13 . VAL A 1 134 ? 176.984 3.306   -53.439 1.00 38.10  ? 134  VAL A HG13 1 
ATOM   1800 H HG21 . VAL A 1 134 ? 177.918 -0.537  -52.537 1.00 35.98  ? 134  VAL A HG21 1 
ATOM   1801 H HG22 . VAL A 1 134 ? 179.050 0.494   -52.964 1.00 35.98  ? 134  VAL A HG22 1 
ATOM   1802 H HG23 . VAL A 1 134 ? 178.358 0.619   -51.539 1.00 35.98  ? 134  VAL A HG23 1 
ATOM   1803 N N    . ALA A 1 135 ? 174.645 3.237   -52.448 1.00 27.46  ? 135  ALA A N    1 
ATOM   1804 C CA   . ALA A 1 135 ? 173.694 4.196   -52.989 1.00 28.70  ? 135  ALA A CA   1 
ATOM   1805 C C    . ALA A 1 135 ? 174.193 5.605   -52.711 1.00 29.78  ? 135  ALA A C    1 
ATOM   1806 O O    . ALA A 1 135 ? 174.818 5.853   -51.681 1.00 28.84  ? 135  ALA A O    1 
ATOM   1807 C CB   . ALA A 1 135 ? 172.326 3.988   -52.365 1.00 37.41  ? 135  ALA A CB   1 
ATOM   1808 H H    . ALA A 1 135 ? 175.103 3.539   -51.785 1.00 33.15  ? 135  ALA A H    1 
ATOM   1809 H HA   . ALA A 1 135 ? 173.619 4.077   -53.948 1.00 34.64  ? 135  ALA A HA   1 
ATOM   1810 H HB1  . ALA A 1 135 ? 172.395 4.110   -51.405 1.00 45.09  ? 135  ALA A HB1  1 
ATOM   1811 H HB2  . ALA A 1 135 ? 171.707 4.635   -52.737 1.00 45.09  ? 135  ALA A HB2  1 
ATOM   1812 H HB3  . ALA A 1 135 ? 172.023 3.088   -52.563 1.00 45.09  ? 135  ALA A HB3  1 
ATOM   1813 N N    . GLY A 1 136 ? 173.923 6.523   -53.635 1.00 30.30  ? 136  GLY A N    1 
ATOM   1814 C CA   . GLY A 1 136 ? 174.297 7.917   -53.460 1.00 29.36  ? 136  GLY A CA   1 
ATOM   1815 C C    . GLY A 1 136 ? 174.978 8.537   -54.662 1.00 28.67  ? 136  GLY A C    1 
ATOM   1816 O O    . GLY A 1 136 ? 174.914 9.750   -54.855 1.00 35.07  ? 136  GLY A O    1 
ATOM   1817 H H    . GLY A 1 136 ? 173.521 6.360   -54.378 1.00 36.56  ? 136  GLY A H    1 
ATOM   1818 H HA2  . GLY A 1 136 ? 173.502 8.436   -53.264 1.00 35.43  ? 136  GLY A HA2  1 
ATOM   1819 H HA3  . GLY A 1 136 ? 174.899 7.990   -52.703 1.00 35.43  ? 136  GLY A HA3  1 
ATOM   1820 N N    . ALA A 1 137 ? 175.636 7.715   -55.470 1.00 27.24  ? 137  ALA A N    1 
ATOM   1821 C CA   . ALA A 1 137 ? 176.317 8.216   -56.655 1.00 31.89  ? 137  ALA A CA   1 
ATOM   1822 C C    . ALA A 1 137 ? 175.288 8.620   -57.708 1.00 31.85  ? 137  ALA A C    1 
ATOM   1823 O O    . ALA A 1 137 ? 174.121 8.239   -57.612 1.00 36.82  ? 137  ALA A O    1 
ATOM   1824 C CB   . ALA A 1 137 ? 177.254 7.166   -57.201 1.00 27.84  ? 137  ALA A CB   1 
ATOM   1825 H H    . ALA A 1 137 ? 175.703 6.866   -55.355 1.00 32.89  ? 137  ALA A H    1 
ATOM   1826 H HA   . ALA A 1 137 ? 176.839 8.999   -56.421 1.00 38.47  ? 137  ALA A HA   1 
ATOM   1827 H HB1  . ALA A 1 137 ? 176.741 6.377   -57.435 1.00 33.60  ? 137  ALA A HB1  1 
ATOM   1828 H HB2  . ALA A 1 137 ? 177.698 7.518   -57.989 1.00 33.60  ? 137  ALA A HB2  1 
ATOM   1829 H HB3  . ALA A 1 137 ? 177.911 6.945   -56.522 1.00 33.60  ? 137  ALA A HB3  1 
ATOM   1830 N N    . PRO A 1 138 ? 175.713 9.402   -58.716 1.00 35.73  ? 138  PRO A N    1 
ATOM   1831 C CA   . PRO A 1 138 ? 174.798 9.876   -59.761 1.00 34.37  ? 138  PRO A CA   1 
ATOM   1832 C C    . PRO A 1 138 ? 174.048 8.762   -60.487 1.00 37.42  ? 138  PRO A C    1 
ATOM   1833 O O    . PRO A 1 138 ? 173.048 9.041   -61.148 1.00 42.40  ? 138  PRO A O    1 
ATOM   1834 C CB   . PRO A 1 138 ? 175.733 10.599  -60.729 1.00 37.14  ? 138  PRO A CB   1 
ATOM   1835 C CG   . PRO A 1 138 ? 176.834 11.084  -59.878 1.00 39.00  ? 138  PRO A CG   1 
ATOM   1836 C CD   . PRO A 1 138 ? 177.047 10.014  -58.848 1.00 35.61  ? 138  PRO A CD   1 
ATOM   1837 H HA   . PRO A 1 138 ? 174.162 10.509  -59.393 1.00 41.44  ? 138  PRO A HA   1 
ATOM   1838 H HB2  . PRO A 1 138 ? 176.062 9.976   -61.397 1.00 44.77  ? 138  PRO A HB2  1 
ATOM   1839 H HB3  . PRO A 1 138 ? 175.267 11.340  -61.146 1.00 44.77  ? 138  PRO A HB3  1 
ATOM   1840 H HG2  . PRO A 1 138 ? 177.632 11.204  -60.416 1.00 47.00  ? 138  PRO A HG2  1 
ATOM   1841 H HG3  . PRO A 1 138 ? 176.576 11.918  -59.457 1.00 47.00  ? 138  PRO A HG3  1 
ATOM   1842 H HD2  . PRO A 1 138 ? 177.690 9.361   -59.165 1.00 42.93  ? 138  PRO A HD2  1 
ATOM   1843 H HD3  . PRO A 1 138 ? 177.324 10.407  -58.005 1.00 42.93  ? 138  PRO A HD3  1 
ATOM   1844 N N    . SER A 1 139 ? 174.523 7.526   -60.365 1.00 32.34  ? 139  SER A N    1 
ATOM   1845 C CA   . SER A 1 139 ? 173.870 6.388   -61.001 1.00 29.52  ? 139  SER A CA   1 
ATOM   1846 C C    . SER A 1 139 ? 174.138 5.110   -60.225 1.00 31.63  ? 139  SER A C    1 
ATOM   1847 O O    . SER A 1 139 ? 175.120 5.016   -59.488 1.00 34.76  ? 139  SER A O    1 
ATOM   1848 C CB   . SER A 1 139 ? 174.367 6.226   -62.435 1.00 33.33  ? 139  SER A CB   1 
ATOM   1849 O OG   . SER A 1 139 ? 175.763 5.999   -62.458 1.00 42.75  ? 139  SER A OG   1 
ATOM   1850 H H    . SER A 1 139 ? 175.226 7.320   -59.915 1.00 39.01  ? 139  SER A H    1 
ATOM   1851 H HA   . SER A 1 139 ? 172.912 6.538   -61.024 1.00 35.63  ? 139  SER A HA   1 
ATOM   1852 H HB2  . SER A 1 139 ? 173.917 5.469   -62.842 1.00 40.20  ? 139  SER A HB2  1 
ATOM   1853 H HB3  . SER A 1 139 ? 174.170 7.036   -62.931 1.00 40.20  ? 139  SER A HB3  1 
ATOM   1854 H HG   . SER A 1 139 ? 176.027 5.911   -63.251 1.00 51.50  ? 139  SER A HG   1 
ATOM   1855 N N    . GLY A 1 140 ? 173.260 4.126   -60.400 1.00 35.30  ? 140  GLY A N    1 
ATOM   1856 C CA   . GLY A 1 140 ? 173.404 2.839   -59.746 1.00 35.40  ? 140  GLY A CA   1 
ATOM   1857 C C    . GLY A 1 140 ? 174.577 2.032   -60.271 1.00 36.87  ? 140  GLY A C    1 
ATOM   1858 O O    . GLY A 1 140 ? 175.172 1.248   -59.532 1.00 40.35  ? 140  GLY A O    1 
ATOM   1859 H H    . GLY A 1 140 ? 172.563 4.185   -60.901 1.00 42.56  ? 140  GLY A H    1 
ATOM   1860 H HA2  . GLY A 1 140 ? 173.530 2.975   -58.794 1.00 42.68  ? 140  GLY A HA2  1 
ATOM   1861 H HA3  . GLY A 1 140 ? 172.595 2.320   -59.877 1.00 42.68  ? 140  GLY A HA3  1 
ATOM   1862 N N    . ASP A 1 141 ? 174.908 2.207   -61.546 1.00 36.64  ? 141  ASP A N    1 
ATOM   1863 C CA   . ASP A 1 141 ? 176.049 1.509   -62.126 1.00 38.55  ? 141  ASP A CA   1 
ATOM   1864 C C    . ASP A 1 141 ? 177.338 1.954   -61.448 1.00 36.34  ? 141  ASP A C    1 
ATOM   1865 O O    . ASP A 1 141 ? 178.247 1.151   -61.230 1.00 40.91  ? 141  ASP A O    1 
ATOM   1866 C CB   . ASP A 1 141 ? 176.133 1.756   -63.631 1.00 46.51  ? 141  ASP A CB   1 
ATOM   1867 C CG   . ASP A 1 141 ? 175.044 1.035   -64.403 1.00 56.68  ? 141  ASP A CG   1 
ATOM   1868 O OD1  . ASP A 1 141 ? 174.616 -0.053  -63.961 1.00 52.67  ? 141  ASP A OD1  1 
ATOM   1869 O OD2  . ASP A 1 141 ? 174.623 1.552   -65.458 1.00 64.51  ? 141  ASP A OD2  1 
ATOM   1870 H H    . ASP A 1 141 ? 174.491 2.722   -62.094 1.00 44.16  ? 141  ASP A H    1 
ATOM   1871 H HA   . ASP A 1 141 ? 175.946 0.555   -61.983 1.00 46.46  ? 141  ASP A HA   1 
ATOM   1872 H HB2  . ASP A 1 141 ? 176.041 2.707   -63.801 1.00 56.01  ? 141  ASP A HB2  1 
ATOM   1873 H HB3  . ASP A 1 141 ? 176.990 1.442   -63.957 1.00 56.01  ? 141  ASP A HB3  1 
ATOM   1874 N N    . LEU A 1 142 ? 177.409 3.236   -61.107 1.00 31.28  ? 142  LEU A N    1 
ATOM   1875 C CA   . LEU A 1 142 ? 178.561 3.765   -60.390 1.00 31.82  ? 142  LEU A CA   1 
ATOM   1876 C C    . LEU A 1 142 ? 178.550 3.304   -58.938 1.00 33.25  ? 142  LEU A C    1 
ATOM   1877 O O    . LEU A 1 142 ? 179.602 3.000   -58.379 1.00 38.08  ? 142  LEU A O    1 
ATOM   1878 C CB   . LEU A 1 142 ? 178.586 5.290   -60.465 1.00 31.07  ? 142  LEU A CB   1 
ATOM   1879 C CG   . LEU A 1 142 ? 178.826 5.873   -61.860 1.00 39.64  ? 142  LEU A CG   1 
ATOM   1880 C CD1  . LEU A 1 142 ? 178.653 7.382   -61.840 1.00 41.93  ? 142  LEU A CD1  1 
ATOM   1881 C CD2  . LEU A 1 142 ? 180.205 5.508   -62.382 1.00 43.03  ? 142  LEU A CD2  1 
ATOM   1882 H H    . LEU A 1 142 ? 176.802 3.820   -61.279 1.00 37.73  ? 142  LEU A H    1 
ATOM   1883 H HA   . LEU A 1 142 ? 179.371 3.431   -60.805 1.00 38.38  ? 142  LEU A HA   1 
ATOM   1884 H HB2  . LEU A 1 142 ? 177.733 5.628   -60.151 1.00 37.49  ? 142  LEU A HB2  1 
ATOM   1885 H HB3  . LEU A 1 142 ? 179.295 5.615   -59.888 1.00 37.49  ? 142  LEU A HB3  1 
ATOM   1886 H HG   . LEU A 1 142 ? 178.169 5.505   -62.471 1.00 47.77  ? 142  LEU A HG   1 
ATOM   1887 H HD11 . LEU A 1 142 ? 179.292 7.764   -61.219 1.00 50.52  ? 142  LEU A HD11 1 
ATOM   1888 H HD12 . LEU A 1 142 ? 178.809 7.729   -62.733 1.00 50.52  ? 142  LEU A HD12 1 
ATOM   1889 H HD13 . LEU A 1 142 ? 177.749 7.591   -61.557 1.00 50.52  ? 142  LEU A HD13 1 
ATOM   1890 H HD21 . LEU A 1 142 ? 180.279 4.542   -62.430 1.00 51.84  ? 142  LEU A HD21 1 
ATOM   1891 H HD22 . LEU A 1 142 ? 180.320 5.893   -63.265 1.00 51.84  ? 142  LEU A HD22 1 
ATOM   1892 H HD23 . LEU A 1 142 ? 180.875 5.862   -61.776 1.00 51.84  ? 142  LEU A HD23 1 
ATOM   1893 N N    . ASP A 1 143 ? 177.367 3.260   -58.329 1.00 33.66  ? 143  ASP A N    1 
ATOM   1894 C CA   . ASP A 1 143 ? 177.217 2.673   -57.002 1.00 30.50  ? 143  ASP A CA   1 
ATOM   1895 C C    . ASP A 1 143 ? 177.797 1.268   -56.998 1.00 31.61  ? 143  ASP A C    1 
ATOM   1896 O O    . ASP A 1 143 ? 178.497 0.872   -56.066 1.00 31.58  ? 143  ASP A O    1 
ATOM   1897 C CB   . ASP A 1 143 ? 175.743 2.597   -56.592 1.00 31.07  ? 143  ASP A CB   1 
ATOM   1898 C CG   . ASP A 1 143 ? 175.152 3.953   -56.260 1.00 34.16  ? 143  ASP A CG   1 
ATOM   1899 O OD1  . ASP A 1 143 ? 175.890 4.822   -55.751 1.00 37.63  ? 143  ASP A OD1  1 
ATOM   1900 O OD2  . ASP A 1 143 ? 173.942 4.145   -56.502 1.00 31.06  ? 143  ASP A OD2  1 
ATOM   1901 H H    . ASP A 1 143 ? 176.635 3.565   -58.664 1.00 40.59  ? 143  ASP A H    1 
ATOM   1902 H HA   . ASP A 1 143 ? 177.695 3.209   -56.350 1.00 36.80  ? 143  ASP A HA   1 
ATOM   1903 H HB2  . ASP A 1 143 ? 175.232 2.219   -57.324 1.00 37.49  ? 143  ASP A HB2  1 
ATOM   1904 H HB3  . ASP A 1 143 ? 175.663 2.034   -55.806 1.00 37.49  ? 143  ASP A HB3  1 
ATOM   1905 N N    . GLU A 1 144 ? 177.506 0.520   -58.057 1.00 31.79  ? 144  GLU A N    1 
ATOM   1906 C CA   . GLU A 1 144 ? 177.890 -0.880  -58.120 1.00 32.85  ? 144  GLU A CA   1 
ATOM   1907 C C    . GLU A 1 144 ? 179.399 -1.033  -58.281 1.00 32.83  ? 144  GLU A C    1 
ATOM   1908 O O    . GLU A 1 144 ? 179.989 -1.951  -57.720 1.00 39.76  ? 144  GLU A O    1 
ATOM   1909 C CB   . GLU A 1 144 ? 177.140 -1.594  -59.246 1.00 33.97  ? 144  GLU A CB   1 
ATOM   1910 C CG   . GLU A 1 144 ? 176.808 -3.042  -58.924 1.00 32.40  ? 144  GLU A CG   1 
ATOM   1911 C CD   . GLU A 1 144 ? 175.795 -3.643  -59.872 1.00 38.02  ? 144  GLU A CD   1 
ATOM   1912 O OE1  . GLU A 1 144 ? 174.581 -3.456  -59.642 1.00 39.01  ? 144  GLU A OE1  1 
ATOM   1913 O OE2  . GLU A 1 144 ? 176.210 -4.304  -60.845 1.00 44.50  ? 144  GLU A OE2  1 
ATOM   1914 H H    . GLU A 1 144 ? 177.087 0.803   -58.753 1.00 38.34  ? 144  GLU A H    1 
ATOM   1915 H HA   . GLU A 1 144 ? 177.640 -1.307  -57.285 1.00 39.62  ? 144  GLU A HA   1 
ATOM   1916 H HB2  . GLU A 1 144 ? 176.307 -1.126  -59.414 1.00 40.96  ? 144  GLU A HB2  1 
ATOM   1917 H HB3  . GLU A 1 144 ? 177.691 -1.585  -60.045 1.00 40.96  ? 144  GLU A HB3  1 
ATOM   1918 H HG2  . GLU A 1 144 ? 177.619 -3.571  -58.979 1.00 39.08  ? 144  GLU A HG2  1 
ATOM   1919 H HG3  . GLU A 1 144 ? 176.442 -3.089  -58.027 1.00 39.08  ? 144  GLU A HG3  1 
ATOM   1920 N N    . GLN A 1 145 ? 180.018 -0.128  -59.034 1.00 29.82  ? 145  GLN A N    1 
ATOM   1921 C CA   . GLN A 1 145 ? 181.471 -0.111  -59.178 1.00 35.07  ? 145  GLN A CA   1 
ATOM   1922 C C    . GLN A 1 145 ? 182.136 -0.079  -57.803 1.00 36.34  ? 145  GLN A C    1 
ATOM   1923 O O    . GLN A 1 145 ? 183.109 -0.793  -57.550 1.00 41.32  ? 145  GLN A O    1 
ATOM   1924 C CB   . GLN A 1 145 ? 181.908 1.106   -59.998 1.00 38.86  ? 145  GLN A CB   1 
ATOM   1925 C CG   . GLN A 1 145 ? 183.419 1.262   -60.138 1.00 46.12  ? 145  GLN A CG   1 
ATOM   1926 C CD   . GLN A 1 145 ? 183.817 2.489   -60.947 1.00 52.52  ? 145  GLN A CD   1 
ATOM   1927 O OE1  . GLN A 1 145 ? 184.769 3.190   -60.602 1.00 54.82  ? 145  GLN A OE1  1 
ATOM   1928 N NE2  . GLN A 1 145 ? 183.095 2.747   -62.032 1.00 51.90  ? 145  GLN A NE2  1 
ATOM   1929 H H    . GLN A 1 145 ? 179.616 0.491   -59.475 1.00 35.98  ? 145  GLN A H    1 
ATOM   1930 H HA   . GLN A 1 145 ? 181.759 -0.914  -59.641 1.00 42.28  ? 145  GLN A HA   1 
ATOM   1931 H HB2  . GLN A 1 145 ? 181.536 1.028   -60.890 1.00 46.83  ? 145  GLN A HB2  1 
ATOM   1932 H HB3  . GLN A 1 145 ? 181.567 1.907   -59.570 1.00 46.83  ? 145  GLN A HB3  1 
ATOM   1933 H HG2  . GLN A 1 145 ? 183.810 1.347   -59.254 1.00 55.55  ? 145  GLN A HG2  1 
ATOM   1934 H HG3  . GLN A 1 145 ? 183.777 0.480   -60.585 1.00 55.55  ? 145  GLN A HG3  1 
ATOM   1935 H HE21 . GLN A 1 145 ? 182.440 2.232   -62.246 1.00 62.48  ? 145  GLN A HE21 1 
ATOM   1936 H HE22 . GLN A 1 145 ? 183.282 3.430   -62.521 1.00 62.48  ? 145  GLN A HE22 1 
ATOM   1937 N N    . TYR A 1 146 ? 181.598 0.748   -56.916 1.00 33.25  ? 146  TYR A N    1 
ATOM   1938 C CA   . TYR A 1 146 ? 182.136 0.884   -55.568 1.00 31.56  ? 146  TYR A CA   1 
ATOM   1939 C C    . TYR A 1 146 ? 181.819 -0.337  -54.712 1.00 31.11  ? 146  TYR A C    1 
ATOM   1940 O O    . TYR A 1 146 ? 182.606 -0.717  -53.844 1.00 35.32  ? 146  TYR A O    1 
ATOM   1941 C CB   . TYR A 1 146 ? 181.591 2.154   -54.920 1.00 31.47  ? 146  TYR A CB   1 
ATOM   1942 C CG   . TYR A 1 146 ? 181.938 3.402   -55.699 1.00 30.91  ? 146  TYR A CG   1 
ATOM   1943 C CD1  . TYR A 1 146 ? 183.226 3.612   -56.165 1.00 33.91  ? 146  TYR A CD1  1 
ATOM   1944 C CD2  . TYR A 1 146 ? 180.976 4.359   -55.985 1.00 28.16  ? 146  TYR A CD2  1 
ATOM   1945 C CE1  . TYR A 1 146 ? 183.550 4.739   -56.882 1.00 36.30  ? 146  TYR A CE1  1 
ATOM   1946 C CE2  . TYR A 1 146 ? 181.293 5.493   -56.704 1.00 31.73  ? 146  TYR A CE2  1 
ATOM   1947 C CZ   . TYR A 1 146 ? 182.583 5.676   -57.150 1.00 37.60  ? 146  TYR A CZ   1 
ATOM   1948 O OH   . TYR A 1 146 ? 182.914 6.802   -57.869 1.00 48.38  ? 146  TYR A OH   1 
ATOM   1949 H H    . TYR A 1 146 ? 180.914 1.247   -57.071 1.00 40.10  ? 146  TYR A H    1 
ATOM   1950 H HA   . TYR A 1 146 ? 183.101 0.967   -55.623 1.00 38.07  ? 146  TYR A HA   1 
ATOM   1951 H HB2  . TYR A 1 146 ? 180.625 2.092   -54.867 1.00 37.96  ? 146  TYR A HB2  1 
ATOM   1952 H HB3  . TYR A 1 146 ? 181.968 2.242   -54.031 1.00 37.96  ? 146  TYR A HB3  1 
ATOM   1953 H HD1  . TYR A 1 146 ? 183.885 2.981   -55.986 1.00 40.89  ? 146  TYR A HD1  1 
ATOM   1954 H HD2  . TYR A 1 146 ? 180.104 4.236   -55.685 1.00 33.99  ? 146  TYR A HD2  1 
ATOM   1955 H HE1  . TYR A 1 146 ? 184.420 4.866   -57.184 1.00 43.75  ? 146  TYR A HE1  1 
ATOM   1956 H HE2  . TYR A 1 146 ? 180.640 6.129   -56.887 1.00 38.27  ? 146  TYR A HE2  1 
ATOM   1957 H HH   . TYR A 1 146 ? 183.728 6.783   -58.074 1.00 58.25  ? 146  TYR A HH   1 
ATOM   1958 N N    . ALA A 1 147 ? 180.668 -0.953  -54.957 1.00 30.08  ? 147  ALA A N    1 
ATOM   1959 C CA   . ALA A 1 147 ? 180.306 -2.180  -54.259 1.00 33.75  ? 147  ALA A CA   1 
ATOM   1960 C C    . ALA A 1 147 ? 181.250 -3.306  -54.665 1.00 33.03  ? 147  ALA A C    1 
ATOM   1961 O O    . ALA A 1 147 ? 181.607 -4.149  -53.842 1.00 35.59  ? 147  ALA A O    1 
ATOM   1962 C CB   . ALA A 1 147 ? 178.871 -2.559  -54.559 1.00 35.08  ? 147  ALA A CB   1 
ATOM   1963 H H    . ALA A 1 147 ? 180.079 -0.681  -55.522 1.00 36.29  ? 147  ALA A H    1 
ATOM   1964 H HA   . ALA A 1 147 ? 180.391 -2.042  -53.303 1.00 40.70  ? 147  ALA A HA   1 
ATOM   1965 H HB1  . ALA A 1 147 ? 178.773 -2.695  -55.514 1.00 42.29  ? 147  ALA A HB1  1 
ATOM   1966 H HB2  . ALA A 1 147 ? 178.655 -3.377  -54.084 1.00 42.29  ? 147  ALA A HB2  1 
ATOM   1967 H HB3  . ALA A 1 147 ? 178.287 -1.842  -54.265 1.00 42.29  ? 147  ALA A HB3  1 
ATOM   1968 N N    A ARG A 1 148 ? 181.647 -3.317  -55.936 0.87 30.61  ? 148  ARG A N    1 
ATOM   1969 N N    B ARG A 1 148 ? 181.651 -3.317  -55.933 0.13 31.31  ? 148  ARG A N    1 
ATOM   1970 C CA   A ARG A 1 148 ? 182.601 -4.304  -56.428 0.87 32.41  ? 148  ARG A CA   1 
ATOM   1971 C CA   B ARG A 1 148 ? 182.608 -4.303  -56.420 0.13 33.17  ? 148  ARG A CA   1 
ATOM   1972 C C    A ARG A 1 148 ? 183.972 -4.073  -55.799 0.87 32.20  ? 148  ARG A C    1 
ATOM   1973 C C    B ARG A 1 148 ? 183.971 -4.074  -55.785 0.13 32.70  ? 148  ARG A C    1 
ATOM   1974 O O    A ARG A 1 148 ? 184.681 -5.025  -55.469 0.87 34.59  ? 148  ARG A O    1 
ATOM   1975 O O    B ARG A 1 148 ? 184.673 -5.024  -55.439 0.13 34.09  ? 148  ARG A O    1 
ATOM   1976 C CB   A ARG A 1 148 ? 182.704 -4.256  -57.958 0.87 38.87  ? 148  ARG A CB   1 
ATOM   1977 C CB   B ARG A 1 148 ? 182.729 -4.239  -57.942 0.13 37.85  ? 148  ARG A CB   1 
ATOM   1978 C CG   A ARG A 1 148 ? 181.442 -4.702  -58.690 0.87 40.67  ? 148  ARG A CG   1 
ATOM   1979 C CG   B ARG A 1 148 ? 181.494 -4.719  -58.675 0.13 40.25  ? 148  ARG A CG   1 
ATOM   1980 C CD   A ARG A 1 148 ? 181.732 -5.133  -60.122 0.87 45.56  ? 148  ARG A CD   1 
ATOM   1981 C CD   B ARG A 1 148 ? 181.714 -4.808  -60.171 0.13 44.97  ? 148  ARG A CD   1 
ATOM   1982 N NE   A ARG A 1 148 ? 182.257 -4.045  -60.946 0.87 47.93  ? 148  ARG A NE   1 
ATOM   1983 N NE   B ARG A 1 148 ? 180.440 -4.970  -60.869 0.13 45.37  ? 148  ARG A NE   1 
ATOM   1984 C CZ   A ARG A 1 148 ? 181.508 -3.130  -61.555 0.87 46.83  ? 148  ARG A CZ   1 
ATOM   1985 C CZ   B ARG A 1 148 ? 179.779 -3.993  -61.486 0.13 43.61  ? 148  ARG A CZ   1 
ATOM   1986 N NH1  A ARG A 1 148 ? 180.187 -3.150  -61.437 0.87 41.81  ? 148  ARG A NH1  1 
ATOM   1987 N NH1  B ARG A 1 148 ? 180.267 -2.759  -61.529 0.13 42.74  ? 148  ARG A NH1  1 
ATOM   1988 N NH2  A ARG A 1 148 ? 182.085 -2.185  -62.285 0.87 52.01  ? 148  ARG A NH2  1 
ATOM   1989 N NH2  B ARG A 1 148 ? 178.625 -4.257  -62.078 0.13 44.79  ? 148  ARG A NH2  1 
ATOM   1990 H H    A ARG A 1 148 ? 181.378 -2.760  -56.534 0.87 36.93  ? 148  ARG A H    1 
ATOM   1991 H H    B ARG A 1 148 ? 181.382 -2.762  -56.533 0.13 37.78  ? 148  ARG A H    1 
ATOM   1992 H HA   A ARG A 1 148 ? 182.298 -5.190  -56.175 0.87 39.09  ? 148  ARG A HA   1 
ATOM   1993 H HA   B ARG A 1 148 ? 182.304 -5.192  -56.176 0.13 40.01  ? 148  ARG A HA   1 
ATOM   1994 H HB2  A ARG A 1 148 ? 182.894 -3.344  -58.228 0.87 46.84  ? 148  ARG A HB2  1 
ATOM   1995 H HB2  B ARG A 1 148 ? 182.890 -3.319  -58.204 0.13 45.62  ? 148  ARG A HB2  1 
ATOM   1996 H HB3  A ARG A 1 148 ? 183.428 -4.838  -58.238 0.87 46.84  ? 148  ARG A HB3  1 
ATOM   1997 H HB3  B ARG A 1 148 ? 183.474 -4.795  -58.220 0.13 45.62  ? 148  ARG A HB3  1 
ATOM   1998 H HG2  A ARG A 1 148 ? 181.052 -5.456  -58.221 0.87 49.00  ? 148  ARG A HG2  1 
ATOM   1999 H HG2  B ARG A 1 148 ? 181.256 -5.602  -58.351 0.13 48.50  ? 148  ARG A HG2  1 
ATOM   2000 H HG3  A ARG A 1 148 ? 180.813 -3.964  -58.718 0.87 49.00  ? 148  ARG A HG3  1 
ATOM   2001 H HG3  B ARG A 1 148 ? 180.767 -4.097  -58.513 0.13 48.50  ? 148  ARG A HG3  1 
ATOM   2002 H HD2  A ARG A 1 148 ? 182.390 -5.845  -60.111 0.87 54.88  ? 148  ARG A HD2  1 
ATOM   2003 H HD2  B ARG A 1 148 ? 182.134 -3.992  -60.485 0.13 54.16  ? 148  ARG A HD2  1 
ATOM   2004 H HD3  A ARG A 1 148 ? 180.910 -5.447  -60.530 0.87 54.88  ? 148  ARG A HD3  1 
ATOM   2005 H HD3  B ARG A 1 148 ? 182.272 -5.576  -60.370 0.13 54.16  ? 148  ARG A HD3  1 
ATOM   2006 H HE   A ARG A 1 148 ? 183.110 -3.993  -61.043 0.87 57.72  ? 148  ARG A HE   1 
ATOM   2007 H HE   B ARG A 1 148 ? 180.091 -5.756  -60.882 0.13 54.64  ? 148  ARG A HE   1 
ATOM   2008 H HH11 A ARG A 1 148 ? 179.807 -3.761  -60.966 0.87 50.37  ? 148  ARG A HH11 1 
ATOM   2009 H HH11 B ARG A 1 148 ? 181.015 -2.579  -61.146 0.13 51.48  ? 148  ARG A HH11 1 
ATOM   2010 H HH12 A ARG A 1 148 ? 179.710 -2.554  -61.833 0.87 50.37  ? 148  ARG A HH12 1 
ATOM   2011 H HH12 B ARG A 1 148 ? 179.831 -2.139  -61.935 0.13 51.48  ? 148  ARG A HH12 1 
ATOM   2012 H HH21 A ARG A 1 148 ? 182.941 -2.165  -62.364 0.87 62.62  ? 148  ARG A HH21 1 
ATOM   2013 H HH21 B ARG A 1 148 ? 178.304 -5.055  -62.059 0.13 53.95  ? 148  ARG A HH21 1 
ATOM   2014 H HH22 A ARG A 1 148 ? 181.603 -1.591  -62.677 0.87 62.62  ? 148  ARG A HH22 1 
ATOM   2015 H HH22 B ARG A 1 148 ? 178.197 -3.632  -62.485 0.13 53.95  ? 148  ARG A HH22 1 
ATOM   2016 N N    . ALA A 1 149 ? 184.343 -2.807  -55.640 1.00 32.09  ? 149  ALA A N    1 
ATOM   2017 C CA   . ALA A 1 149 ? 185.602 -2.455  -54.997 1.00 35.90  ? 149  ALA A CA   1 
ATOM   2018 C C    . ALA A 1 149 ? 185.569 -2.939  -53.558 1.00 29.72  ? 149  ALA A C    1 
ATOM   2019 O O    . ALA A 1 149 ? 186.581 -3.376  -53.012 1.00 37.15  ? 149  ALA A O    1 
ATOM   2020 C CB   . ALA A 1 149 ? 185.812 -0.966  -55.042 1.00 35.33  ? 149  ALA A CB   1 
ATOM   2021 H H    . ALA A 1 149 ? 183.880 -2.130  -55.901 1.00 38.70  ? 149  ALA A H    1 
ATOM   2022 H HA   . ALA A 1 149 ? 186.338 -2.889  -55.457 1.00 43.27  ? 149  ALA A HA   1 
ATOM   2023 H HB1  . ALA A 1 149 ? 185.081 -0.530  -54.576 1.00 42.59  ? 149  ALA A HB1  1 
ATOM   2024 H HB2  . ALA A 1 149 ? 186.654 -0.753  -54.610 1.00 42.59  ? 149  ALA A HB2  1 
ATOM   2025 H HB3  . ALA A 1 149 ? 185.833 -0.678  -55.968 1.00 42.59  ? 149  ALA A HB3  1 
ATOM   2026 N N    . GLY A 1 150 ? 184.392 -2.855  -52.948 1.00 33.21  ? 150  GLY A N    1 
ATOM   2027 C CA   . GLY A 1 150 ? 184.184 -3.380  -51.613 1.00 30.88  ? 150  GLY A CA   1 
ATOM   2028 C C    . GLY A 1 150 ? 184.372 -4.881  -51.578 1.00 33.53  ? 150  GLY A C    1 
ATOM   2029 O O    . GLY A 1 150 ? 185.039 -5.411  -50.694 1.00 34.33  ? 150  GLY A O    1 
ATOM   2030 H H    . GLY A 1 150 ? 183.692 -2.493  -53.294 1.00 40.05  ? 150  GLY A H    1 
ATOM   2031 H HA2  . GLY A 1 150 ? 184.815 -2.972  -51.000 1.00 37.26  ? 150  GLY A HA2  1 
ATOM   2032 H HA3  . GLY A 1 150 ? 183.284 -3.172  -51.317 1.00 37.26  ? 150  GLY A HA3  1 
ATOM   2033 N N    . ALA A 1 151 ? 183.773 -5.573  -52.539 1.00 32.72  ? 151  ALA A N    1 
ATOM   2034 C CA   . ALA A 1 151 ? 183.899 -7.021  -52.620 1.00 26.00  ? 151  ALA A CA   1 
ATOM   2035 C C    . ALA A 1 151 ? 185.334 -7.442  -52.919 1.00 30.17  ? 151  ALA A C    1 
ATOM   2036 O O    . ALA A 1 151 ? 185.773 -8.510  -52.498 1.00 33.05  ? 151  ALA A O    1 
ATOM   2037 C CB   . ALA A 1 151 ? 182.962 -7.566  -53.683 1.00 27.11  ? 151  ALA A CB   1 
ATOM   2038 H H    . ALA A 1 151 ? 183.288 -5.227  -53.159 1.00 39.47  ? 151  ALA A H    1 
ATOM   2039 H HA   . ALA A 1 151 ? 183.644 -7.408  -51.768 1.00 31.40  ? 151  ALA A HA   1 
ATOM   2040 H HB1  . ALA A 1 151 ? 183.194 -7.173  -54.539 1.00 32.73  ? 151  ALA A HB1  1 
ATOM   2041 H HB2  . ALA A 1 151 ? 183.059 -8.530  -53.723 1.00 32.73  ? 151  ALA A HB2  1 
ATOM   2042 H HB3  . ALA A 1 151 ? 182.050 -7.334  -53.448 1.00 32.73  ? 151  ALA A HB3  1 
ATOM   2043 N N    . ALA A 1 152 ? 186.071 -6.594  -53.628 1.00 33.95  ? 152  ALA A N    1 
ATOM   2044 C CA   . ALA A 1 152 ? 187.368 -6.985  -54.176 1.00 38.29  ? 152  ALA A CA   1 
ATOM   2045 C C    . ALA A 1 152 ? 188.477 -7.122  -53.134 1.00 36.95  ? 152  ALA A C    1 
ATOM   2046 O O    . ALA A 1 152 ? 189.483 -7.780  -53.393 1.00 37.91  ? 152  ALA A O    1 
ATOM   2047 C CB   . ALA A 1 152 ? 187.789 -6.011  -55.261 1.00 45.80  ? 152  ALA A CB   1 
ATOM   2048 H H    . ALA A 1 152 ? 185.843 -5.784  -53.808 1.00 40.94  ? 152  ALA A H    1 
ATOM   2049 H HA   . ALA A 1 152 ? 187.266 -7.853  -54.596 1.00 46.14  ? 152  ALA A HA   1 
ATOM   2050 H HB1  . ALA A 1 152 ? 187.855 -5.122  -54.879 1.00 55.16  ? 152  ALA A HB1  1 
ATOM   2051 H HB2  . ALA A 1 152 ? 188.650 -6.285  -55.614 1.00 55.16  ? 152  ALA A HB2  1 
ATOM   2052 H HB3  . ALA A 1 152 ? 187.124 -6.019  -55.968 1.00 55.16  ? 152  ALA A HB3  1 
ATOM   2053 N N    . VAL A 1 153 ? 188.314 -6.503  -51.968 1.00 38.08  ? 153  VAL A N    1 
ATOM   2054 C CA   . VAL A 1 153 ? 189.314 -6.648  -50.910 1.00 38.70  ? 153  VAL A CA   1 
ATOM   2055 C C    . VAL A 1 153 ? 189.159 -7.990  -50.202 1.00 34.39  ? 153  VAL A C    1 
ATOM   2056 O O    . VAL A 1 153 ? 190.064 -8.438  -49.499 1.00 41.30  ? 153  VAL A O    1 
ATOM   2057 C CB   . VAL A 1 153 ? 189.253 -5.504  -49.872 1.00 38.46  ? 153  VAL A CB   1 
ATOM   2058 C CG1  . VAL A 1 153 ? 189.534 -4.170  -50.540 1.00 40.71  ? 153  VAL A CG1  1 
ATOM   2059 C CG2  . VAL A 1 153 ? 187.910 -5.477  -49.163 1.00 37.46  ? 153  VAL A CG2  1 
ATOM   2060 H H    . VAL A 1 153 ? 187.645 -6.002  -51.765 1.00 45.90  ? 153  VAL A H    1 
ATOM   2061 H HA   . VAL A 1 153 ? 190.195 -6.629  -51.314 1.00 46.64  ? 153  VAL A HA   1 
ATOM   2062 H HB   . VAL A 1 153 ? 189.939 -5.652  -49.203 1.00 46.35  ? 153  VAL A HB   1 
ATOM   2063 H HG11 . VAL A 1 153 ? 188.867 -4.015  -51.227 1.00 49.05  ? 153  VAL A HG11 1 
ATOM   2064 H HG12 . VAL A 1 153 ? 189.490 -3.468  -49.872 1.00 49.05  ? 153  VAL A HG12 1 
ATOM   2065 H HG13 . VAL A 1 153 ? 190.419 -4.196  -50.936 1.00 49.05  ? 153  VAL A HG13 1 
ATOM   2066 H HG21 . VAL A 1 153 ? 187.778 -6.323  -48.706 1.00 45.15  ? 153  VAL A HG21 1 
ATOM   2067 H HG22 . VAL A 1 153 ? 187.907 -4.750  -48.521 1.00 45.15  ? 153  VAL A HG22 1 
ATOM   2068 H HG23 . VAL A 1 153 ? 187.209 -5.342  -49.819 1.00 45.15  ? 153  VAL A HG23 1 
ATOM   2069 N N    . LEU A 1 154 ? 188.005 -8.624  -50.388 1.00 30.74  ? 154  LEU A N    1 
ATOM   2070 C CA   . LEU A 1 154 ? 187.775 -9.961  -49.859 1.00 38.30  ? 154  LEU A CA   1 
ATOM   2071 C C    . LEU A 1 154 ? 188.409 -10.971 -50.807 1.00 47.06  ? 154  LEU A C    1 
ATOM   2072 O O    . LEU A 1 154 ? 188.516 -10.716 -52.003 1.00 47.67  ? 154  LEU A O    1 
ATOM   2073 C CB   . LEU A 1 154 ? 186.280 -10.234 -49.710 1.00 34.12  ? 154  LEU A CB   1 
ATOM   2074 C CG   . LEU A 1 154 ? 185.510 -9.228  -48.850 1.00 35.09  ? 154  LEU A CG   1 
ATOM   2075 C CD1  . LEU A 1 154 ? 184.039 -9.592  -48.791 1.00 34.03  ? 154  LEU A CD1  1 
ATOM   2076 C CD2  . LEU A 1 154 ? 186.092 -9.146  -47.449 1.00 35.80  ? 154  LEU A CD2  1 
ATOM   2077 H H    . LEU A 1 154 ? 187.336 -8.298  -50.819 1.00 37.09  ? 154  LEU A H    1 
ATOM   2078 H HA   . LEU A 1 154 ? 188.195 -10.046 -48.989 1.00 46.16  ? 154  LEU A HA   1 
ATOM   2079 H HB2  . LEU A 1 154 ? 185.877 -10.230 -50.593 1.00 41.14  ? 154  LEU A HB2  1 
ATOM   2080 H HB3  . LEU A 1 154 ? 186.166 -11.109 -49.306 1.00 41.14  ? 154  LEU A HB3  1 
ATOM   2081 H HG   . LEU A 1 154 ? 185.583 -8.349  -49.254 1.00 42.31  ? 154  LEU A HG   1 
ATOM   2082 H HD11 . LEU A 1 154 ? 183.948 -10.477 -48.404 1.00 41.04  ? 154  LEU A HD11 1 
ATOM   2083 H HD12 . LEU A 1 154 ? 183.574 -8.941  -48.241 1.00 41.04  ? 154  LEU A HD12 1 
ATOM   2084 H HD13 . LEU A 1 154 ? 183.676 -9.585  -49.690 1.00 41.04  ? 154  LEU A HD13 1 
ATOM   2085 H HD21 . LEU A 1 154 ? 187.018 -8.865  -47.509 1.00 43.16  ? 154  LEU A HD21 1 
ATOM   2086 H HD22 . LEU A 1 154 ? 185.583 -8.502  -46.933 1.00 43.16  ? 154  LEU A HD22 1 
ATOM   2087 H HD23 . LEU A 1 154 ? 186.037 -10.021 -47.034 1.00 43.16  ? 154  LEU A HD23 1 
ATOM   2088 N N    . GLY A 1 155 ? 188.821 -12.115 -50.271 1.00 55.05  ? 155  GLY A N    1 
ATOM   2089 C CA   . GLY A 1 155 ? 189.588 -13.080 -51.037 1.00 70.06  ? 155  GLY A CA   1 
ATOM   2090 C C    . GLY A 1 155 ? 191.073 -12.829 -50.833 1.00 82.36  ? 155  GLY A C    1 
ATOM   2091 O O    . GLY A 1 155 ? 191.445 -12.290 -49.791 1.00 81.11  ? 155  GLY A O    1 
ATOM   2092 H H    . GLY A 1 155 ? 188.667 -12.354 -49.460 1.00 66.26  ? 155  GLY A H    1 
ATOM   2093 H HA2  . GLY A 1 155 ? 189.376 -13.980 -50.745 1.00 84.27  ? 155  GLY A HA2  1 
ATOM   2094 H HA3  . GLY A 1 155 ? 189.380 -12.996 -51.981 1.00 84.27  ? 155  GLY A HA3  1 
ATOM   2095 N N    . HIS A 1 156 ? 191.935 -13.201 -51.783 1.00 97.22  ? 156  HIS A N    1 
ATOM   2096 C CA   . HIS A 1 156 ? 191.572 -13.863 -53.038 1.00 111.21 ? 156  HIS A CA   1 
ATOM   2097 C C    . HIS A 1 156 ? 192.447 -15.087 -53.238 1.00 120.53 ? 156  HIS A C    1 
ATOM   2098 O O    . HIS A 1 156 ? 193.571 -15.149 -52.743 1.00 123.40 ? 156  HIS A O    1 
ATOM   2099 C CB   . HIS A 1 156 ? 191.785 -12.923 -54.222 1.00 118.99 ? 156  HIS A CB   1 
ATOM   2100 C CG   . HIS A 1 156 ? 190.730 -11.876 -54.367 1.00 120.41 ? 156  HIS A CG   1 
ATOM   2101 N ND1  . HIS A 1 156 ? 189.510 -12.124 -54.965 1.00 122.13 ? 156  HIS A ND1  1 
ATOM   2102 C CD2  . HIS A 1 156 ? 190.711 -10.570 -54.011 1.00 117.68 ? 156  HIS A CD2  1 
ATOM   2103 C CE1  . HIS A 1 156 ? 188.789 -11.022 -54.962 1.00 118.08 ? 156  HIS A CE1  1 
ATOM   2104 N NE2  . HIS A 1 156 ? 189.493 -10.062 -54.387 1.00 115.76 ? 156  HIS A NE2  1 
ATOM   2105 O OXT  . HIS A 1 156 ? 192.057 -16.045 -53.903 1.00 125.19 ? 156  HIS A OXT  1 
ATOM   2106 H H    . HIS A 1 156 ? 192.782 -13.071 -51.717 1.00 116.86 ? 156  HIS A H    1 
ATOM   2107 H HA   . HIS A 1 156 ? 190.642 -14.138 -53.013 1.00 133.65 ? 156  HIS A HA   1 
ATOM   2108 H HB2  . HIS A 1 156 ? 192.636 -12.471 -54.112 1.00 142.99 ? 156  HIS A HB2  1 
ATOM   2109 H HB3  . HIS A 1 156 ? 191.795 -13.447 -55.038 1.00 142.99 ? 156  HIS A HB3  1 
ATOM   2110 H HD1  . HIS A 1 156 ? 189.260 -12.881 -55.287 1.00 146.75 ? 156  HIS A HD1  1 
ATOM   2111 H HD2  . HIS A 1 156 ? 191.395 -10.105 -53.585 1.00 141.41 ? 156  HIS A HD2  1 
ATOM   2112 H HE1  . HIS A 1 156 ? 187.929 -10.934 -55.304 1.00 141.90 ? 156  HIS A HE1  1 
ATOM   2113 H HE2  . HIS A 1 156 ? 189.231 -9.251  -54.269 1.00 139.11 ? 156  HIS A HE2  1 
HETATM 2114 O O    . HOH B 2 .   ? 166.366 -30.192 -19.979 1.00 46.01  ? 2001 HOH A O    1 
HETATM 2115 O O    . HOH B 2 .   ? 169.070 -30.336 -21.738 1.00 46.49  ? 2002 HOH A O    1 
HETATM 2116 O O    . HOH B 2 .   ? 168.715 -32.110 -23.669 1.00 36.80  ? 2003 HOH A O    1 
HETATM 2117 O O    . HOH B 2 .   ? 170.348 -34.202 -24.862 1.00 88.36  ? 2004 HOH A O    1 
HETATM 2118 O O    . HOH B 2 .   ? 169.823 -32.121 -19.685 1.00 42.62  ? 2005 HOH A O    1 
HETATM 2119 O O    . HOH B 2 .   ? 175.621 -32.827 -32.627 1.00 53.02  ? 2006 HOH A O    1 
HETATM 2120 O O    . HOH B 2 .   ? 166.735 -33.073 -39.101 1.00 43.12  ? 2007 HOH A O    1 
HETATM 2121 O O    . HOH B 2 .   ? 173.127 -14.174 -36.516 1.00 49.75  ? 2008 HOH A O    1 
HETATM 2122 O O    . HOH B 2 .   ? 186.721 -11.804 -36.735 1.00 43.30  ? 2009 HOH A O    1 
HETATM 2123 O O    . HOH B 2 .   ? 171.514 -18.668 -42.454 1.00 49.01  ? 2010 HOH A O    1 
HETATM 2124 O O    . HOH B 2 .   ? 175.260 -20.996 -45.497 1.00 42.81  ? 2011 HOH A O    1 
HETATM 2125 O O    . HOH B 2 .   ? 174.882 -16.778 -44.577 1.00 41.36  ? 2012 HOH A O    1 
HETATM 2126 O O    . HOH B 2 .   ? 175.771 -13.346 -39.774 1.00 35.43  ? 2013 HOH A O    1 
HETATM 2127 O O    . HOH B 2 .   ? 175.909 -15.609 -38.343 1.00 53.81  ? 2014 HOH A O    1 
HETATM 2128 O O    . HOH B 2 .   ? 172.114 -17.334 -39.930 0.50 30.85  ? 2015 HOH A O    1 
HETATM 2129 O O    . HOH B 2 .   ? 177.571 -13.060 -44.389 1.00 26.97  ? 2016 HOH A O    1 
HETATM 2130 O O    . HOH B 2 .   ? 178.578 -12.810 -39.178 1.00 35.83  ? 2017 HOH A O    1 
HETATM 2131 O O    . HOH B 2 .   ? 187.812 -4.859  -40.729 1.00 53.39  ? 2018 HOH A O    1 
HETATM 2132 O O    . HOH B 2 .   ? 184.909 -6.385  -36.152 1.00 37.15  ? 2019 HOH A O    1 
HETATM 2133 O O    . HOH B 2 .   ? 186.557 -3.766  -37.973 0.69 44.78  ? 2020 HOH A O    1 
HETATM 2134 O O    . HOH B 2 .   ? 190.180 -5.950  -41.332 1.00 50.70  ? 2021 HOH A O    1 
HETATM 2135 O O    . HOH B 2 .   ? 188.315 -11.856 -38.389 1.00 51.20  ? 2022 HOH A O    1 
HETATM 2136 O O    . HOH B 2 .   ? 164.266 -6.899  -45.555 1.00 39.99  ? 2023 HOH A O    1 
HETATM 2137 O O    . HOH B 2 .   ? 165.904 -6.104  -42.354 1.00 47.47  ? 2024 HOH A O    1 
HETATM 2138 O O    . HOH B 2 .   ? 184.053 -4.380  -37.308 1.00 42.25  ? 2025 HOH A O    1 
HETATM 2139 O O    . HOH B 2 .   ? 188.768 -2.099  -46.276 1.00 41.15  ? 2026 HOH A O    1 
HETATM 2140 O O    . HOH B 2 .   ? 167.841 0.000   -39.930 0.50 73.69  ? 2027 HOH A O    1 
HETATM 2141 O O    . HOH B 2 .   ? 191.796 0.000   -39.930 0.50 48.97  ? 2028 HOH A O    1 
HETATM 2142 O O    . HOH B 2 .   ? 170.315 5.647   -58.550 1.00 42.81  ? 2029 HOH A O    1 
HETATM 2143 O O    . HOH B 2 .   ? 188.711 0.932   -51.531 1.00 35.83  ? 2030 HOH A O    1 
HETATM 2144 O O    . HOH B 2 .   ? 176.838 -16.637 -59.895 0.50 47.07  ? 2031 HOH A O    1 
HETATM 2145 O O    . HOH B 2 .   ? 187.766 4.833   -56.634 1.00 41.67  ? 2032 HOH A O    1 
HETATM 2146 O O    . HOH B 2 .   ? 184.436 8.535   -44.875 1.00 41.15  ? 2033 HOH A O    1 
HETATM 2147 O O    . HOH B 2 .   ? 157.798 -15.885 -66.936 1.00 55.10  ? 2034 HOH A O    1 
HETATM 2148 O O    . HOH B 2 .   ? 154.146 -10.671 -65.012 1.00 47.34  ? 2035 HOH A O    1 
HETATM 2149 O O    . HOH B 2 .   ? 154.780 0.000   -52.192 0.50 62.13  ? 2036 HOH A O    1 
HETATM 2150 O O    . HOH B 2 .   ? 181.241 8.574   -49.493 1.00 57.07  ? 2037 HOH A O    1 
HETATM 2151 O O    . HOH B 2 .   ? 183.227 12.130  -50.827 1.00 54.29  ? 2038 HOH A O    1 
HETATM 2152 O O    . HOH B 2 .   ? 177.564 11.003  -54.859 1.00 43.73  ? 2039 HOH A O    1 
HETATM 2153 O O    . HOH B 2 .   ? 174.344 11.123  -52.087 1.00 42.41  ? 2040 HOH A O    1 
HETATM 2154 O O    . HOH B 2 .   ? 181.284 15.252  -47.578 1.00 46.21  ? 2041 HOH A O    1 
HETATM 2155 O O    . HOH B 2 .   ? 182.388 -7.951  -57.405 1.00 39.65  ? 2042 HOH A O    1 
HETATM 2156 O O    . HOH B 2 .   ? 171.445 -19.872 -48.327 1.00 58.29  ? 2043 HOH A O    1 
HETATM 2157 O O    . HOH B 2 .   ? 169.061 -17.812 -54.141 1.00 48.97  ? 2044 HOH A O    1 
HETATM 2158 O O    . HOH B 2 .   ? 173.150 -12.424 -38.625 1.00 34.26  ? 2045 HOH A O    1 
HETATM 2159 O O    . HOH B 2 .   ? 165.371 -8.513  -43.666 1.00 55.00  ? 2046 HOH A O    1 
HETATM 2160 O O    . HOH B 2 .   ? 168.311 -6.371  -43.353 1.00 17.25  ? 2047 HOH A O    1 
HETATM 2161 O O    . HOH B 2 .   ? 166.818 -8.002  -39.265 1.00 44.61  ? 2048 HOH A O    1 
HETATM 2162 O O    . HOH B 2 .   ? 166.426 -11.197 -37.929 1.00 40.35  ? 2049 HOH A O    1 
HETATM 2163 O O    . HOH B 2 .   ? 168.794 -6.221  -40.408 1.00 34.59  ? 2050 HOH A O    1 
HETATM 2164 O O    . HOH B 2 .   ? 168.380 -3.629  -40.579 1.00 36.03  ? 2051 HOH A O    1 
HETATM 2165 O O    . HOH B 2 .   ? 167.081 -3.616  -43.103 1.00 38.00  ? 2052 HOH A O    1 
HETATM 2166 O O    . HOH B 2 .   ? 178.346 10.667  -42.375 1.00 40.11  ? 2053 HOH A O    1 
HETATM 2167 O O    . HOH B 2 .   ? 167.753 9.612   -43.671 1.00 45.10  ? 2054 HOH A O    1 
HETATM 2168 O O    . HOH B 2 .   ? 168.129 6.398   -42.986 1.00 41.08  ? 2055 HOH A O    1 
HETATM 2169 O O    . HOH B 2 .   ? 176.081 11.702  -42.643 0.97 59.67  ? 2056 HOH A O    1 
HETATM 2170 O O    . HOH B 2 .   ? 174.412 12.302  -44.536 1.00 51.99  ? 2057 HOH A O    1 
HETATM 2171 O O    . HOH B 2 .   ? 182.295 9.617   -45.886 1.00 43.03  ? 2058 HOH A O    1 
HETATM 2172 O O    . HOH B 2 .   ? 184.703 10.384  -42.998 1.00 38.64  ? 2059 HOH A O    1 
HETATM 2173 O O    . HOH B 2 .   ? 171.856 13.606  -46.063 1.00 44.41  ? 2060 HOH A O    1 
HETATM 2174 O O    . HOH B 2 .   ? 167.465 6.208   -45.961 1.00 33.83  ? 2061 HOH A O    1 
HETATM 2175 O O    . HOH B 2 .   ? 170.999 7.713   -55.426 1.00 41.57  ? 2062 HOH A O    1 
HETATM 2176 O O    . HOH B 2 .   ? 169.702 1.455   -39.050 1.00 34.00  ? 2063 HOH A O    1 
HETATM 2177 O O    . HOH B 2 .   ? 167.663 0.631   -43.507 1.00 39.59  ? 2064 HOH A O    1 
HETATM 2178 O O    . HOH B 2 .   ? 164.607 6.431   -46.035 1.00 42.63  ? 2065 HOH A O    1 
HETATM 2179 O O    . HOH B 2 .   ? 170.152 4.401   -55.829 1.00 48.83  ? 2066 HOH A O    1 
HETATM 2180 O O    . HOH B 2 .   ? 169.379 5.932   -53.753 1.00 24.10  ? 2067 HOH A O    1 
HETATM 2181 O O    . HOH B 2 .   ? 168.136 -5.291  -45.767 1.00 34.50  ? 2068 HOH A O    1 
HETATM 2182 O O    . HOH B 2 .   ? 159.479 -3.294  -48.725 1.00 37.50  ? 2069 HOH A O    1 
HETATM 2183 O O    . HOH B 2 .   ? 159.744 -3.409  -46.405 1.00 49.01  ? 2070 HOH A O    1 
HETATM 2184 O O    . HOH B 2 .   ? 166.446 -16.970 -53.656 1.00 36.17  ? 2071 HOH A O    1 
HETATM 2185 O O    . HOH B 2 .   ? 169.011 -15.764 -59.673 1.00 56.29  ? 2072 HOH A O    1 
HETATM 2186 O O    . HOH B 2 .   ? 168.720 -17.687 -56.656 1.00 53.54  ? 2073 HOH A O    1 
HETATM 2187 O O    . HOH B 2 .   ? 172.607 -16.177 -59.242 1.00 40.34  ? 2074 HOH A O    1 
HETATM 2188 O O    . HOH B 2 .   ? 162.926 -14.853 -59.218 1.00 48.32  ? 2075 HOH A O    1 
HETATM 2189 O O    . HOH B 2 .   ? 164.706 -17.075 -56.566 1.00 57.08  ? 2076 HOH A O    1 
HETATM 2190 O O    . HOH B 2 .   ? 176.215 -14.010 -59.555 1.00 47.57  ? 2077 HOH A O    1 
HETATM 2191 O O    . HOH B 2 .   ? 177.533 -18.577 -57.316 1.00 39.66  ? 2078 HOH A O    1 
HETATM 2192 O O    . HOH B 2 .   ? 176.941 -14.306 -56.681 0.43 36.62  ? 2079 HOH A O    1 
HETATM 2193 O O    . HOH B 2 .   ? 169.990 -2.016  -64.400 1.00 48.92  ? 2080 HOH A O    1 
HETATM 2194 O O    . HOH B 2 .   ? 175.263 -5.652  -65.021 1.00 47.97  ? 2081 HOH A O    1 
HETATM 2195 O O    . HOH B 2 .   ? 168.982 -10.501 -65.700 1.00 53.25  ? 2082 HOH A O    1 
HETATM 2196 O O    . HOH B 2 .   ? 169.499 -12.415 -64.473 1.00 66.65  ? 2083 HOH A O    1 
HETATM 2197 O O    . HOH B 2 .   ? 175.388 -13.281 -61.901 1.00 34.11  ? 2084 HOH A O    1 
HETATM 2198 O O    . HOH B 2 .   ? 158.920 -3.705  -66.470 1.00 48.00  ? 2085 HOH A O    1 
HETATM 2199 O O    . HOH B 2 .   ? 157.038 -13.601 -65.871 1.00 45.20  ? 2086 HOH A O    1 
HETATM 2200 O O    . HOH B 2 .   ? 156.190 -11.160 -62.866 1.00 38.61  ? 2087 HOH A O    1 
HETATM 2201 O O    . HOH B 2 .   ? 155.057 -4.360  -60.204 1.00 37.11  ? 2088 HOH A O    1 
HETATM 2202 O O    . HOH B 2 .   ? 158.553 -2.254  -53.876 1.00 41.22  ? 2089 HOH A O    1 
HETATM 2203 O O    . HOH B 2 .   ? 159.268 -3.975  -52.006 1.00 52.56  ? 2090 HOH A O    1 
HETATM 2204 O O    . HOH B 2 .   ? 161.327 -2.923  -54.918 1.00 32.63  ? 2091 HOH A O    1 
HETATM 2205 O O    . HOH B 2 .   ? 156.227 -1.804  -54.333 1.00 63.29  ? 2092 HOH A O    1 
HETATM 2206 O O    . HOH B 2 .   ? 154.780 0.000   -61.103 0.50 63.31  ? 2093 HOH A O    1 
HETATM 2207 O O    . HOH B 2 .   ? 154.324 -7.651  -52.191 1.00 40.88  ? 2094 HOH A O    1 
HETATM 2208 O O    . HOH B 2 .   ? 160.629 -10.508 -48.939 1.00 38.82  ? 2095 HOH A O    1 
HETATM 2209 O O    . HOH B 2 .   ? 165.264 -5.209  -47.204 1.00 35.43  ? 2096 HOH A O    1 
HETATM 2210 O O    . HOH B 2 .   ? 162.611 -2.290  -57.025 1.00 34.41  ? 2097 HOH A O    1 
HETATM 2211 O O    . HOH B 2 .   ? 169.285 -0.388  -62.478 1.00 35.97  ? 2098 HOH A O    1 
HETATM 2212 O O    . HOH B 2 .   ? 180.833 -9.308  -56.109 1.00 52.92  ? 2099 HOH A O    1 
HETATM 2213 O O    . HOH B 2 .   ? 182.158 -19.071 -53.958 1.00 29.65  ? 2100 HOH A O    1 
HETATM 2214 O O    . HOH B 2 .   ? 181.592 -16.324 -56.561 0.94 46.07  ? 2101 HOH A O    1 
HETATM 2215 O O    . HOH B 2 .   ? 174.995 -19.297 -48.054 1.00 39.55  ? 2102 HOH A O    1 
HETATM 2216 O O    . HOH B 2 .   ? 172.502 6.222   -56.912 1.00 34.19  ? 2103 HOH A O    1 
HETATM 2217 O O    . HOH B 2 .   ? 173.380 11.830  -56.126 1.00 52.44  ? 2104 HOH A O    1 
HETATM 2218 O O    . HOH B 2 .   ? 170.424 4.844   -61.300 1.00 44.98  ? 2105 HOH A O    1 
HETATM 2219 O O    . HOH B 2 .   ? 178.940 -0.676  -62.665 1.00 56.56  ? 2106 HOH A O    1 
HETATM 2220 O O    . HOH B 2 .   ? 172.664 -1.150  -65.381 1.00 53.05  ? 2107 HOH A O    1 
HETATM 2221 O O    . HOH B 2 .   ? 177.151 -2.223  -62.959 1.00 54.08  ? 2108 HOH A O    1 
HETATM 2222 O O    . HOH B 2 .   ? 184.966 -1.327  -59.155 1.00 36.50  ? 2109 HOH A O    1 
HETATM 2223 O O    . HOH B 2 .   ? 184.841 -7.059  -57.433 1.00 41.57  ? 2110 HOH A O    1 
HETATM 2224 O O    . HOH B 2 .   ? 184.926 -5.611  -62.053 1.00 59.24  ? 2111 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   A PRO A 11  ? 1.3060 1.0909 0.6704 -0.1885 0.0833  -0.2911 11  PRO A N   
2    C CA  A PRO A 11  ? 1.3305 1.1390 0.6495 -0.2009 0.0713  -0.2623 11  PRO A CA  
3    C C   A PRO A 11  ? 1.2809 1.0922 0.6205 -0.1986 0.0582  -0.2206 11  PRO A C   
4    O O   A PRO A 11  ? 1.3098 1.1364 0.6212 -0.2083 0.0429  -0.1922 11  PRO A O   
5    C CB  A PRO A 11  ? 1.3758 1.2028 0.6784 -0.1950 0.1018  -0.2680 11  PRO A CB  
6    C CG  A PRO A 11  ? 1.4223 1.2356 0.7466 -0.1835 0.1257  -0.3077 11  PRO A CG  
7    C CD  A PRO A 11  ? 1.3368 1.1240 0.7143 -0.1750 0.1186  -0.3129 11  PRO A CD  
15   N N   A ALA A 12  ? 1.2049 1.0010 0.5949 -0.1856 0.0638  -0.2169 12  ALA A N   
16   C CA  A ALA A 12  ? 1.1560 0.9554 0.5687 -0.1793 0.0615  -0.1816 12  ALA A CA  
17   C C   A ALA A 12  ? 1.1216 0.9029 0.5740 -0.1747 0.0452  -0.1741 12  ALA A C   
18   O O   A ALA A 12  ? 1.1359 0.9015 0.6143 -0.1715 0.0442  -0.1980 12  ALA A O   
19   C CB  A ALA A 12  ? 1.1433 0.9521 0.5792 -0.1653 0.0943  -0.1802 12  ALA A CB  
25   N N   A ALA A 13  ? 1.0590 0.8429 0.5198 -0.1734 0.0324  -0.1404 13  ALA A N   
26   C CA  A ALA A 13  ? 1.0171 0.7881 0.5077 -0.1711 0.0100  -0.1276 13  ALA A CA  
27   C C   A ALA A 13  ? 0.9733 0.7518 0.4634 -0.1692 -0.0010 -0.0891 13  ALA A C   
28   O O   A ALA A 13  ? 1.0298 0.8223 0.4973 -0.1720 0.0058  -0.0751 13  ALA A O   
29   C CB  A ALA A 13  ? 1.0616 0.8286 0.5395 -0.1831 -0.0212 -0.1341 13  ALA A CB  
35   N N   A ALA A 14  ? 0.9151 0.6861 0.4339 -0.1638 -0.0188 -0.0713 14  ALA A N   
36   C CA  A ALA A 14  ? 0.8902 0.6493 0.4462 -0.1606 -0.0332 -0.0822 14  ALA A CA  
37   C C   A ALA A 14  ? 0.8126 0.5833 0.4373 -0.1390 -0.0241 -0.0612 14  ALA A C   
38   O O   A ALA A 14  ? 0.7760 0.5542 0.3978 -0.1332 -0.0081 -0.0461 14  ALA A O   
39   C CB  A ALA A 14  ? 0.9235 0.6855 0.4731 -0.1699 -0.0729 -0.0683 14  ALA A CB  
45   N N   A PRO A 15  ? 0.7738 0.5488 0.4595 -0.1287 -0.0345 -0.0596 15  PRO A N   
46   C CA  A PRO A 15  ? 0.7056 0.4966 0.4546 -0.1098 -0.0200 -0.0452 15  PRO A CA  
47   C C   A PRO A 15  ? 0.6301 0.4354 0.4003 -0.1016 -0.0367 -0.0143 15  PRO A C   
48   O O   A PRO A 15  ? 0.5593 0.3628 0.3153 -0.1071 -0.0656 -0.0018 15  PRO A O   
49   C CB  A PRO A 15  ? 0.7188 0.5110 0.5222 -0.1049 -0.0245 -0.0565 15  PRO A CB  
50   C CG  A PRO A 15  ? 0.7598 0.5427 0.5398 -0.1186 -0.0572 -0.0602 15  PRO A CG  
51   C CD  A PRO A 15  ? 0.8160 0.5857 0.5174 -0.1352 -0.0598 -0.0691 15  PRO A CD  
59   N N   A VAL A 16  ? 0.6050 0.4255 0.4115 -0.0884 -0.0184 -0.0031 16  VAL A N   
60   C CA  A VAL A 16  ? 0.5839 0.4170 0.4114 -0.0798 -0.0292 0.0213  16  VAL A CA  
61   C C   A VAL A 16  ? 0.5377 0.3890 0.4228 -0.0695 -0.0465 0.0298  16  VAL A C   
62   O O   A VAL A 16  ? 0.4443 0.3068 0.3705 -0.0649 -0.0401 0.0219  16  VAL A O   
63   C CB  A VAL A 16  ? 0.6283 0.4733 0.4699 -0.0722 -0.0025 0.0279  16  VAL A CB  
64   C CG1 A VAL A 16  ? 0.6049 0.4609 0.4698 -0.0637 -0.0132 0.0482  16  VAL A CG1 
65   C CG2 A VAL A 16  ? 0.6478 0.4795 0.4347 -0.0826 0.0148  0.0230  16  VAL A CG2 
75   N N   A ALA A 17  ? 0.5713 0.4268 0.4618 -0.0656 -0.0679 0.0475  17  ALA A N   
76   C CA  A ALA A 17  ? 0.5370 0.4147 0.4815 -0.0547 -0.0838 0.0574  17  ALA A CA  
77   C C   A ALA A 17  ? 0.4555 0.3530 0.4340 -0.0411 -0.0734 0.0687  17  ALA A C   
78   O O   A ALA A 17  ? 0.4752 0.3630 0.4351 -0.0397 -0.0770 0.0784  17  ALA A O   
79   C CB  A ALA A 17  ? 0.5771 0.4482 0.5087 -0.0592 -0.1167 0.0678  17  ALA A CB  
85   N N   A ALA A 18  ? 0.4128 0.3387 0.4417 -0.0322 -0.0613 0.0676  18  ALA A N   
86   C CA  A ALA A 18  ? 0.3859 0.3391 0.4474 -0.0205 -0.0503 0.0733  18  ALA A CA  
87   C C   A ALA A 18  ? 0.3525 0.3284 0.4398 -0.0130 -0.0645 0.0734  18  ALA A C   
88   O O   A ALA A 18  ? 0.3440 0.3190 0.4374 -0.0160 -0.0816 0.0744  18  ALA A O   
89   C CB  A ALA A 18  ? 0.3517 0.3365 0.4517 -0.0163 -0.0293 0.0691  18  ALA A CB  
95   N N   A ARG A 19  ? 0.3839 0.3754 0.4821 -0.0064 -0.0541 0.0703  19  ARG A N   
96   C CA  A ARG A 19  ? 0.3906 0.3940 0.5039 -0.0011 -0.0582 0.0673  19  ARG A CA  
97   C C   A ARG A 19  ? 0.3611 0.3785 0.4836 0.0047  -0.0434 0.0619  19  ARG A C   
98   O O   A ARG A 19  ? 0.3774 0.3980 0.4990 0.0033  -0.0312 0.0617  19  ARG A O   
99   C CB  A ARG A 19  ? 0.4333 0.4154 0.5283 -0.0006 -0.0770 0.0726  19  ARG A CB  
100  C CG  A ARG A 19  ? 0.4918 0.4529 0.5638 0.0011  -0.0766 0.0760  19  ARG A CG  
101  C CD  A ARG A 19  ? 0.5950 0.5463 0.6659 0.0043  -0.0914 0.0814  19  ARG A CD  
102  N NE  A ARG A 19  ? 0.6578 0.5896 0.7137 0.0062  -0.0905 0.0855  19  ARG A NE  
103  C CZ  A ARG A 19  ? 0.6954 0.6022 0.7211 -0.0011 -0.1005 0.0950  19  ARG A CZ  
104  N NH1 A ARG A 19  ? 0.7140 0.6048 0.7312 0.0003  -0.0977 0.0990  19  ARG A NH1 
105  N NH2 A ARG A 19  ? 0.7133 0.6109 0.7162 -0.0114 -0.1141 0.1007  19  ARG A NH2 
119  N N   . GLY A 20  ? 0.8931 0.4760 1.0339 0.0854  0.1592  0.0650  20  GLY A N   
120  C CA  . GLY A 20  ? 0.8984 0.4816 1.0930 0.0587  0.2239  0.0162  20  GLY A CA  
121  C C   . GLY A 20  ? 0.8816 0.5034 1.0128 0.0269  0.2395  -0.0365 20  GLY A C   
122  O O   . GLY A 20  ? 0.7958 0.4494 0.8957 0.0352  0.2075  -0.0361 20  GLY A O   
126  N N   . GLY A 21  ? 0.9067 0.5355 1.0158 -0.0182 0.2856  -0.0767 21  GLY A N   
127  C CA  . GLY A 21  ? 0.8713 0.5592 0.9193 -0.0680 0.2955  -0.1158 21  GLY A CA  
128  C C   . GLY A 21  ? 0.7683 0.5286 0.7422 -0.0616 0.2492  -0.0861 21  GLY A C   
129  O O   . GLY A 21  ? 0.7808 0.6136 0.7143 -0.1057 0.2501  -0.0968 21  GLY A O   
133  N N   . GLU A 22  ? 0.6880 0.4293 0.6474 -0.0116 0.2143  -0.0424 22  GLU A N   
134  C CA  . GLU A 22  ? 0.5927 0.3811 0.4947 0.0061  0.1870  -0.0092 22  GLU A CA  
135  C C   . GLU A 22  ? 0.5642 0.3652 0.4529 0.0302  0.1613  -0.0012 22  GLU A C   
136  O O   . GLU A 22  ? 0.5495 0.3869 0.4037 0.0453  0.1525  0.0257  22  GLU A O   
137  C CB  . GLU A 22  ? 0.6109 0.3524 0.4861 0.0412  0.1749  0.0263  22  GLU A CB  
138  C CG  . GLU A 22  ? 0.7012 0.4320 0.5888 0.0213  0.1990  0.0242  22  GLU A CG  
139  C CD  . GLU A 22  ? 0.7916 0.4734 0.6486 0.0533  0.1868  0.0602  22  GLU A CD  
140  O OE1 . GLU A 22  ? 0.8310 0.4681 0.6583 0.0816  0.1604  0.0811  22  GLU A OE1 
141  O OE2 . GLU A 22  ? 0.8890 0.5760 0.7424 0.0416  0.2043  0.0674  22  GLU A OE2 
148  N N   . LEU A 23  ? 0.5834 0.3526 0.5103 0.0348  0.1562  -0.0196 23  LEU A N   
149  C CA  . LEU A 23  ? 0.5338 0.3074 0.4498 0.0549  0.1303  -0.0135 23  LEU A CA  
150  C C   . LEU A 23  ? 0.5139 0.3239 0.4652 0.0266  0.1447  -0.0481 23  LEU A C   
151  O O   . LEU A 23  ? 0.5346 0.3318 0.5285 -0.0042 0.1797  -0.0809 23  LEU A O   
152  C CB  . LEU A 23  ? 0.5549 0.2630 0.4797 0.0832  0.1008  0.0099  23  LEU A CB  
153  C CG  . LEU A 23  ? 0.6509 0.3122 0.5151 0.1002  0.0828  0.0443  23  LEU A CG  
154  C CD1 . LEU A 23  ? 0.6291 0.2430 0.5041 0.1053  0.0461  0.0753  23  LEU A CD1 
155  C CD2 . LEU A 23  ? 0.7059 0.3688 0.4881 0.1123  0.0847  0.0546  23  LEU A CD2 
167  N N   . THR A 24  ? 0.4939 0.3401 0.4239 0.0346  0.1261  -0.0417 24  THR A N   
168  C CA  . THR A 24  ? 0.4684 0.3457 0.4246 0.0110  0.1339  -0.0702 24  THR A CA  
169  C C   . THR A 24  ? 0.4467 0.3145 0.3929 0.0447  0.1018  -0.0524 24  THR A C   
170  O O   . THR A 24  ? 0.5150 0.3614 0.4168 0.0745  0.0827  -0.0220 24  THR A O   
171  C CB  . THR A 24  ? 0.4935 0.4613 0.4269 -0.0407 0.1485  -0.0797 24  THR A CB  
172  O OG1 . THR A 24  ? 0.5427 0.5361 0.4893 -0.0684 0.1555  -0.1077 24  THR A OG1 
173  C CG2 . THR A 24  ? 0.4780 0.5060 0.3826 -0.0207 0.1286  -0.0296 24  THR A CG2 
181  N N   . GLN A 25  ? 0.5189 0.3932 0.5009 0.0352  0.1039  -0.0740 25  GLN A N   
182  C CA  . GLN A 25  ? 0.5869 0.4526 0.5618 0.0604  0.0738  -0.0597 25  GLN A CA  
183  C C   . GLN A 25  ? 0.5559 0.4913 0.5211 0.0421  0.0773  -0.0688 25  GLN A C   
184  O O   . GLN A 25  ? 0.5437 0.5296 0.5198 -0.0016 0.1020  -0.0943 25  GLN A O   
185  C CB  . GLN A 25  ? 0.7086 0.5312 0.7482 0.0698  0.0664  -0.0609 25  GLN A CB  
186  C CG  . GLN A 25  ? 0.8278 0.5973 0.8945 0.0850  0.0560  -0.0325 25  GLN A CG  
187  C CD  . GLN A 25  ? 0.9704 0.7185 1.1197 0.0960  0.0390  -0.0051 25  GLN A CD  
188  O OE1 . GLN A 25  ? 1.0686 0.8041 1.3169 0.0953  0.0733  -0.0038 25  GLN A OE1 
189  N NE2 . GLN A 25  ? 0.9705 0.7134 1.0857 0.1029  -0.0086 0.0228  25  GLN A NE2 
198  N N   . SER A 26  ? 0.5532 0.4872 0.4907 0.0678  0.0556  -0.0460 26  SER A N   
199  C CA  . SER A 26  ? 0.5078 0.5080 0.4469 0.0575  0.0558  -0.0423 26  SER A CA  
200  C C   . SER A 26  ? 0.5253 0.4892 0.4722 0.0755  0.0349  -0.0467 26  SER A C   
201  O O   . SER A 26  ? 0.5023 0.3963 0.4392 0.0943  0.0152  -0.0398 26  SER A O   
202  C CB  . SER A 26  ? 0.5159 0.5536 0.4286 0.0744  0.0624  0.0015  26  SER A CB  
203  O OG  . SER A 26  ? 0.6637 0.6236 0.5367 0.1136  0.0589  0.0196  26  SER A OG  
209  N N   . THR A 27  ? 0.4955 0.5143 0.4583 0.0619  0.0356  -0.0524 27  THR A N   
210  C CA  . THR A 27  ? 0.3904 0.3847 0.3671 0.0736  0.0172  -0.0579 27  THR A CA  
211  C C   . THR A 27  ? 0.3834 0.3989 0.3332 0.0898  0.0128  -0.0318 27  THR A C   
212  O O   . THR A 27  ? 0.3530 0.4399 0.3064 0.0824  0.0277  -0.0091 27  THR A O   
213  C CB  . THR A 27  ? 0.3889 0.4152 0.4176 0.0429  0.0318  -0.0923 27  THR A CB  
214  O OG1 . THR A 27  ? 0.3916 0.3792 0.4588 0.0330  0.0528  -0.1132 27  THR A OG1 
215  C CG2 . THR A 27  ? 0.3947 0.4042 0.4486 0.0562  0.0126  -0.0919 27  THR A CG2 
223  N N   . HIS A 28  ? 0.3957 0.3518 0.3242 0.1076  -0.0059 -0.0274 28  HIS A N   
224  C CA  . HIS A 28  ? 0.4709 0.4191 0.3698 0.1243  0.0015  -0.0053 28  HIS A CA  
225  C C   . HIS A 28  ? 0.4483 0.3667 0.3470 0.1218  -0.0222 -0.0155 28  HIS A C   
226  O O   . HIS A 28  ? 0.4795 0.3703 0.3952 0.1117  -0.0489 -0.0277 28  HIS A O   
227  C CB  . HIS A 28  ? 0.5428 0.4061 0.3720 0.1439  0.0199  0.0141  28  HIS A CB  
228  C CG  . HIS A 28  ? 0.5883 0.4627 0.4153 0.1483  0.0392  0.0254  28  HIS A CG  
229  N ND1 . HIS A 28  ? 0.6196 0.5425 0.4657 0.1631  0.0757  0.0617  28  HIS A ND1 
230  C CD2 . HIS A 28  ? 0.6156 0.4644 0.4341 0.1399  0.0279  0.0132  28  HIS A CD2 
231  C CE1 . HIS A 28  ? 0.6097 0.5357 0.4522 0.1616  0.0840  0.0669  28  HIS A CE1 
232  N NE2 . HIS A 28  ? 0.6458 0.5229 0.4668 0.1478  0.0562  0.0339  28  HIS A NE2 
241  N N   . LEU A 29  ? 0.4449 0.3741 0.3359 0.1312  -0.0104 -0.0012 29  LEU A N   
242  C CA  . LEU A 29  ? 0.4874 0.3678 0.3560 0.1280  -0.0294 -0.0065 29  LEU A CA  
243  C C   . LEU A 29  ? 0.5614 0.3259 0.3381 0.1228  -0.0325 -0.0036 29  LEU A C   
244  O O   . LEU A 29  ? 0.6425 0.3594 0.3694 0.1329  0.0003  0.0062  29  LEU A O   
245  C CB  . LEU A 29  ? 0.4927 0.4042 0.3732 0.1398  -0.0064 0.0113  29  LEU A CB  
246  C CG  . LEU A 29  ? 0.4084 0.4356 0.3622 0.1302  -0.0097 0.0136  29  LEU A CG  
247  C CD1 . LEU A 29  ? 0.3965 0.4399 0.3600 0.1450  0.0114  0.0436  29  LEU A CD1 
248  C CD2 . LEU A 29  ? 0.3784 0.4205 0.3664 0.1090  -0.0402 -0.0191 29  LEU A CD2 
260  N N   . THR A 30  ? 0.6396 0.3603 0.3905 0.0990  -0.0706 -0.0081 30  THR A N   
261  C CA  . THR A 30  ? 0.6966 0.3055 0.3334 0.0710  -0.0763 -0.0045 30  THR A CA  
262  C C   . THR A 30  ? 0.7262 0.2713 0.2993 0.0765  -0.0268 -0.0072 30  THR A C   
263  O O   . THR A 30  ? 0.6217 0.2240 0.2566 0.0995  -0.0098 -0.0034 30  THR A O   
264  C CB  . THR A 30  ? 0.7341 0.3338 0.3665 0.0309  -0.1376 0.0056  30  THR A CB  
265  O OG1 . THR A 30  ? 0.7318 0.3766 0.4184 0.0349  -0.1478 0.0027  30  THR A OG1 
266  C CG2 . THR A 30  ? 0.6240 0.2806 0.3419 0.0301  -0.1751 0.0222  30  THR A CG2 
274  N N   . LEU A 31  ? 0.4912 0.4403 0.3643 -0.0783 -0.0668 -0.0154 31  LEU A N   
275  C CA  . LEU A 31  ? 0.4762 0.4332 0.3368 -0.0820 -0.0636 -0.0250 31  LEU A CA  
276  C C   . LEU A 31  ? 0.4821 0.4500 0.3757 -0.0762 -0.0682 -0.0141 31  LEU A C   
277  O O   . LEU A 31  ? 0.5098 0.4824 0.4034 -0.0717 -0.0607 -0.0223 31  LEU A O   
278  C CB  . LEU A 31  ? 0.4573 0.4041 0.2807 -0.0999 -0.0766 -0.0250 31  LEU A CB  
279  C CG  . LEU A 31  ? 0.4746 0.4103 0.2697 -0.1009 -0.0767 -0.0353 31  LEU A CG  
280  C CD1 . LEU A 31  ? 0.4911 0.4360 0.2749 -0.0854 -0.0535 -0.0523 31  LEU A CD1 
281  C CD2 . LEU A 31  ? 0.4593 0.3743 0.2046 -0.1143 -0.0895 -0.0361 31  LEU A CD2 
293  N N   A GLU A 32  ? 0.4499 0.4260 0.3734 -0.0768 -0.0813 0.0087  32  GLU A N   
294  N N   B GLU A 32  ? 0.4475 0.4235 0.3709 -0.0769 -0.0813 0.0087  32  GLU A N   
295  C CA  A GLU A 32  ? 0.4548 0.4546 0.4166 -0.0751 -0.0889 0.0297  32  GLU A CA  
296  C CA  B GLU A 32  ? 0.4536 0.4534 0.4155 -0.0751 -0.0890 0.0297  32  GLU A CA  
297  C C   A GLU A 32  ? 0.4162 0.4366 0.4071 -0.0492 -0.0674 0.0277  32  GLU A C   
298  C C   B GLU A 32  ? 0.4153 0.4358 0.4063 -0.0492 -0.0675 0.0278  32  GLU A C   
299  O O   A GLU A 32  ? 0.4059 0.4449 0.4154 -0.0497 -0.0675 0.0343  32  GLU A O   
300  O O   B GLU A 32  ? 0.4063 0.4453 0.4158 -0.0498 -0.0675 0.0344  32  GLU A O   
301  C CB  A GLU A 32  ? 0.5169 0.5334 0.5099 -0.0780 -0.1055 0.0614  32  GLU A CB  
302  C CB  B GLU A 32  ? 0.5180 0.5343 0.5108 -0.0778 -0.1054 0.0613  32  GLU A CB  
303  C CG  A GLU A 32  ? 0.5470 0.5953 0.5760 -0.0899 -0.1237 0.0925  32  GLU A CG  
304  C CG  B GLU A 32  ? 0.5467 0.5969 0.5785 -0.0874 -0.1220 0.0930  32  GLU A CG  
305  C CD  A GLU A 32  ? 0.5713 0.5942 0.5627 -0.1243 -0.1480 0.0877  32  GLU A CD  
306  C CD  B GLU A 32  ? 0.5741 0.6486 0.6370 -0.0927 -0.1402 0.1296  32  GLU A CD  
307  O OE1 A GLU A 32  ? 0.6619 0.6557 0.6129 -0.1419 -0.1615 0.0798  32  GLU A OE1 
308  O OE1 B GLU A 32  ? 0.6153 0.6674 0.6509 -0.1114 -0.1561 0.1283  32  GLU A OE1 
309  O OE2 A GLU A 32  ? 0.5291 0.5559 0.5256 -0.1332 -0.1543 0.0920  32  GLU A OE2 
310  O OE2 B GLU A 32  ? 0.5425 0.6640 0.6584 -0.0766 -0.1378 0.1629  32  GLU A OE2 
322  N N   . ALA A 33  ? 0.4153 0.4275 0.4044 -0.0278 -0.0509 0.0194  33  ALA A N   
323  C CA  . ALA A 33  ? 0.3941 0.4187 0.3994 -0.0006 -0.0296 0.0152  33  ALA A CA  
324  C C   . ALA A 33  ? 0.3978 0.4198 0.3832 -0.0050 -0.0182 -0.0087 33  ALA A C   
325  O O   . ALA A 33  ? 0.3849 0.4294 0.3909 0.0061  -0.0080 -0.0062 33  ALA A O   
326  C CB  . ALA A 33  ? 0.4083 0.4062 0.3987 0.0214  -0.0191 0.0098  33  ALA A CB  
332  N N   . ALA A 34  ? 0.3791 0.3794 0.3264 -0.0201 -0.0193 -0.0277 34  ALA A N   
333  C CA  . ALA A 34  ? 0.3916 0.3947 0.3197 -0.0221 -0.0076 -0.0462 34  ALA A CA  
334  C C   . ALA A 34  ? 0.3908 0.4019 0.3242 -0.0288 -0.0131 -0.0431 34  ALA A C   
335  O O   . ALA A 34  ? 0.4129 0.4343 0.3503 -0.0209 -0.0015 -0.0500 34  ALA A O   
336  C CB  . ALA A 34  ? 0.4369 0.4271 0.3269 -0.0360 -0.0086 -0.0579 34  ALA A CB  
342  N N   . THR A 35  ? 0.3284 0.3294 0.2573 -0.0453 -0.0334 -0.0317 35  THR A N   
343  C CA  . THR A 35  ? 0.3790 0.3711 0.3011 -0.0574 -0.0463 -0.0271 35  THR A CA  
344  C C   . THR A 35  ? 0.4128 0.4352 0.3828 -0.0515 -0.0470 -0.0069 35  THR A C   
345  O O   . THR A 35  ? 0.4325 0.4545 0.4025 -0.0525 -0.0458 -0.0083 35  THR A O   
346  C CB  . THR A 35  ? 0.3746 0.3433 0.2746 -0.0808 -0.0731 -0.0167 35  THR A CB  
347  O OG1 . THR A 35  ? 0.4570 0.4024 0.3096 -0.0838 -0.0704 -0.0336 35  THR A OG1 
348  C CG2 . THR A 35  ? 0.4485 0.3932 0.3306 -0.0980 -0.0929 -0.0108 35  THR A CG2 
356  N N   . LYS A 36  ? 0.3665 0.4171 0.3767 -0.0432 -0.0481 0.0149  36  LYS A N   
357  C CA  . LYS A 36  ? 0.3436 0.4374 0.4046 -0.0325 -0.0457 0.0416  36  LYS A CA  
358  C C   . LYS A 36  ? 0.3386 0.4458 0.4056 -0.0111 -0.0208 0.0279  36  LYS A C   
359  O O   . LYS A 36  ? 0.3258 0.4581 0.4177 -0.0120 -0.0215 0.0423  36  LYS A O   
360  C CB  . LYS A 36  ? 0.3463 0.4683 0.4423 -0.0146 -0.0427 0.0656  36  LYS A CB  
361  C CG  . LYS A 36  ? 0.4030 0.5837 0.5560 0.0003  -0.0393 0.1028  36  LYS A CG  
362  C CD  . LYS A 36  ? 0.4736 0.6851 0.6603 0.0162  -0.0416 0.1355  36  LYS A CD  
363  C CE  . LYS A 36  ? 0.5201 0.7302 0.7050 0.0628  -0.0115 0.1279  36  LYS A CE  
364  N NZ  . LYS A 36  ? 0.5579 0.8339 0.7963 0.0951  0.0008  0.1701  36  LYS A NZ  
378  N N   . ALA A 37  ? 0.3075 0.3979 0.3501 0.0047  -0.0017 0.0027  37  ALA A N   
379  C CA  . ALA A 37  ? 0.3220 0.4225 0.3639 0.0232  0.0205  -0.0111 37  ALA A CA  
380  C C   . ALA A 37  ? 0.3392 0.4321 0.3642 0.0113  0.0204  -0.0237 37  ALA A C   
381  O O   . ALA A 37  ? 0.3299 0.4451 0.3743 0.0188  0.0286  -0.0181 37  ALA A O   
382  C CB  . ALA A 37  ? 0.3587 0.4359 0.3706 0.0344  0.0335  -0.0322 37  ALA A CB  
388  N N   . ALA A 38  ? 0.3888 0.4503 0.3752 -0.0040 0.0125  -0.0389 38  ALA A N   
389  C CA  . ALA A 38  ? 0.4255 0.4718 0.3856 -0.0081 0.0148  -0.0513 38  ALA A CA  
390  C C   . ALA A 38  ? 0.3996 0.4417 0.3722 -0.0197 -0.0015 -0.0349 38  ALA A C   
391  O O   . ALA A 38  ? 0.4494 0.4929 0.4219 -0.0151 0.0049  -0.0371 38  ALA A O   
392  C CB  . ALA A 38  ? 0.4420 0.4566 0.3541 -0.0166 0.0102  -0.0658 38  ALA A CB  
398  N N   . ARG A 39  ? 0.3938 0.4308 0.3767 -0.0375 -0.0252 -0.0153 39  ARG A N   
399  C CA  . ARG A 39  ? 0.3856 0.4173 0.3792 -0.0575 -0.0487 0.0070  39  ARG A CA  
400  C C   . ARG A 39  ? 0.3727 0.4580 0.4224 -0.0478 -0.0400 0.0301  39  ARG A C   
401  O O   . ARG A 39  ? 0.3949 0.4783 0.4510 -0.0606 -0.0522 0.0441  39  ARG A O   
402  C CB  . ARG A 39  ? 0.4226 0.4468 0.4194 -0.0826 -0.0788 0.0291  39  ARG A CB  
403  C CG  . ARG A 39  ? 0.5506 0.5126 0.4817 -0.0986 -0.0950 0.0106  39  ARG A CG  
404  C CD  . ARG A 39  ? 0.6024 0.5558 0.5350 -0.1295 -0.1304 0.0367  39  ARG A CD  
405  N NE  . ARG A 39  ? 0.6900 0.6489 0.6436 -0.1547 -0.1572 0.0674  39  ARG A NE  
406  C CZ  . ARG A 39  ? 0.7754 0.7525 0.7539 -0.1848 -0.1898 0.1047  39  ARG A CZ  
407  N NH1 . ARG A 39  ? 0.7811 0.7710 0.7665 -0.1897 -0.1974 0.1135  39  ARG A NH1 
408  N NH2 . ARG A 39  ? 0.8682 0.8543 0.8665 -0.2122 -0.2168 0.1372  39  ARG A NH2 
422  N N   . ALA A 40  ? 0.3573 0.4864 0.4423 -0.0241 -0.0195 0.0352  40  ALA A N   
423  C CA  . ALA A 40  ? 0.2648 0.4495 0.3989 -0.0074 -0.0063 0.0578  40  ALA A CA  
424  C C   . ALA A 40  ? 0.2669 0.4502 0.3901 0.0043  0.0124  0.0395  40  ALA A C   
425  O O   . ALA A 40  ? 0.2723 0.4899 0.4266 0.0060  0.0143  0.0597  40  ALA A O   
426  C CB  . ALA A 40  ? 0.2375 0.4546 0.3953 0.0217  0.0128  0.0642  40  ALA A CB  
432  N N   . ALA A 41  ? 0.2670 0.4168 0.3485 0.0113  0.0255  0.0056  41  ALA A N   
433  C CA  . ALA A 41  ? 0.3095 0.4597 0.3787 0.0215  0.0424  -0.0101 41  ALA A CA  
434  C C   . ALA A 41  ? 0.3775 0.5022 0.4332 0.0050  0.0270  -0.0051 41  ALA A C   
435  O O   . ALA A 41  ? 0.3297 0.4743 0.4033 0.0093  0.0328  0.0039  41  ALA A O   
436  C CB  . ALA A 41  ? 0.3025 0.4306 0.3326 0.0291  0.0565  -0.0398 41  ALA A CB  
442  N N   . VAL A 42  ? 0.3378 0.4122 0.3553 -0.0131 0.0064  -0.0109 42  VAL A N   
443  C CA  . VAL A 42  ? 0.4011 0.4289 0.3878 -0.0287 -0.0126 -0.0082 42  VAL A CA  
444  C C   . VAL A 42  ? 0.3195 0.3717 0.3478 -0.0476 -0.0328 0.0272  42  VAL A C   
445  O O   . VAL A 42  ? 0.4713 0.5146 0.4984 -0.0508 -0.0362 0.0342  42  VAL A O   
446  C CB  . VAL A 42  ? 0.5111 0.4732 0.4408 -0.0455 -0.0351 -0.0183 42  VAL A CB  
447  C CG1 . VAL A 42  ? 0.5746 0.4711 0.4604 -0.0633 -0.0606 -0.0139 42  VAL A CG1 
448  C CG2 . VAL A 42  ? 0.4951 0.4388 0.3819 -0.0260 -0.0144 -0.0482 42  VAL A CG2 
458  N N   . GLU A 43  ? 0.3598 0.4469 0.4264 -0.0602 -0.0469 0.0538  43  GLU A N   
459  C CA  . GLU A 43  ? 0.4464 0.5718 0.5598 -0.0816 -0.0689 0.0975  43  GLU A CA  
460  C C   . GLU A 43  ? 0.3803 0.5656 0.5393 -0.0626 -0.0469 0.1115  43  GLU A C   
461  O O   . GLU A 43  ? 0.4418 0.6392 0.6205 -0.0812 -0.0638 0.1398  43  GLU A O   
462  C CB  . GLU A 43  ? 0.4926 0.6648 0.6478 -0.0883 -0.0792 0.1270  43  GLU A CB  
463  C CG  . GLU A 43  ? 0.6397 0.8615 0.8464 -0.1156 -0.1068 0.1820  43  GLU A CG  
464  C CD  . GLU A 43  ? 0.7551 1.0249 1.0013 -0.1221 -0.1187 0.2154  43  GLU A CD  
465  O OE1 . GLU A 43  ? 0.7872 1.0756 1.0406 -0.0911 -0.0933 0.2004  43  GLU A OE1 
466  O OE2 . GLU A 43  ? 0.7738 1.0615 1.0425 -0.1597 -0.1555 0.2594  43  GLU A OE2 
473  N N   . ALA A 44  ? 0.3210 0.5400 0.4919 -0.0279 -0.0115 0.0929  44  ALA A N   
474  C CA  . ALA A 44  ? 0.2942 0.5686 0.5007 -0.0063 0.0118  0.1033  44  ALA A CA  
475  C C   . ALA A 44  ? 0.3061 0.5485 0.4855 -0.0084 0.0150  0.0872  44  ALA A C   
476  O O   . ALA A 44  ? 0.4137 0.6915 0.6221 -0.0078 0.0178  0.1083  44  ALA A O   
477  C CB  . ALA A 44  ? 0.2761 0.5770 0.4855 0.0291  0.0446  0.0844  44  ALA A CB  
483  N N   . ALA A 45  ? 0.2872 0.4665 0.4113 -0.0083 0.0156  0.0530  45  ALA A N   
484  C CA  . ALA A 45  ? 0.3921 0.5358 0.4845 -0.0052 0.0196  0.0386  45  ALA A CA  
485  C C   . ALA A 45  ? 0.3917 0.4888 0.4680 -0.0341 -0.0139 0.0584  45  ALA A C   
486  O O   . ALA A 45  ? 0.4091 0.5061 0.4911 -0.0359 -0.0155 0.0697  45  ALA A O   
487  C CB  . ALA A 45  ? 0.4042 0.5022 0.4425 0.0079  0.0319  0.0024  45  ALA A CB  
493  N N   . GLU A 46  ? 0.4383 0.4909 0.4898 -0.0590 -0.0434 0.0637  46  GLU A N   
494  C CA  . GLU A 46  ? 0.5261 0.5180 0.5484 -0.0933 -0.0830 0.0827  46  GLU A CA  
495  C C   . GLU A 46  ? 0.4948 0.5451 0.5788 -0.1144 -0.0989 0.1297  46  GLU A C   
496  O O   . GLU A 46  ? 0.6105 0.6208 0.6772 -0.1368 -0.1236 0.1462  46  GLU A O   
497  C CB  . GLU A 46  ? 0.6337 0.5764 0.6213 -0.1199 -0.1142 0.0840  46  GLU A CB  
498  C CG  . GLU A 46  ? 0.7563 0.5989 0.6523 -0.1130 -0.1176 0.0462  46  GLU A CG  
499  C CD  . GLU A 46  ? 0.9504 0.7233 0.7973 -0.1494 -0.1606 0.0540  46  GLU A CD  
500  O OE1 . GLU A 46  ? 0.9709 0.7738 0.8378 -0.1580 -0.1654 0.0597  46  GLU A OE1 
501  O OE2 . GLU A 46  ? 1.0362 0.7187 0.8195 -0.1702 -0.1913 0.0552  46  GLU A OE2 
508  N N   . LYS A 47  ? 0.4618 0.6060 0.6148 -0.1053 -0.0843 0.1533  47  LYS A N   
509  C CA  . LYS A 47  ? 0.4656 0.6872 0.6856 -0.1186 -0.0932 0.2040  47  LYS A CA  
510  C C   . LYS A 47  ? 0.4760 0.7163 0.7070 -0.1033 -0.0746 0.2038  47  LYS A C   
511  O O   . LYS A 47  ? 0.5625 0.8158 0.8153 -0.1283 -0.0969 0.2406  47  LYS A O   
512  C CB  . LYS A 47  ? 0.4594 0.7764 0.7413 -0.0962 -0.0709 0.2239  47  LYS A CB  
513  C CG  . LYS A 47  ? 0.5778 0.9700 0.9183 -0.1105 -0.0850 0.2838  47  LYS A CG  
514  C CD  . LYS A 47  ? 0.6480 1.0811 1.0014 -0.0791 -0.0616 0.2910  47  LYS A CD  
515  C CE  . LYS A 47  ? 0.7504 1.1656 1.1004 -0.1009 -0.0857 0.2952  47  LYS A CE  
516  N NZ  . LYS A 47  ? 0.7699 1.2144 1.1279 -0.0640 -0.0571 0.2887  47  LYS A NZ  
530  N N   . ASP A 48  ? 0.5399 0.7240 0.6986 -0.2425 0.1033  0.0777  48  ASP A N   
531  C CA  . ASP A 48  ? 0.5819 0.7357 0.6948 -0.2452 0.1170  0.0863  48  ASP A CA  
532  C C   . ASP A 48  ? 0.5942 0.6970 0.6653 -0.2566 0.0968  0.0905  48  ASP A C   
533  O O   . ASP A 48  ? 0.6512 0.7210 0.6788 -0.2577 0.1019  0.0972  48  ASP A O   
534  C CB  . ASP A 48  ? 0.5928 0.7492 0.6765 -0.2248 0.1324  0.0798  48  ASP A CB  
535  C CG  . ASP A 48  ? 0.6212 0.8188 0.7387 -0.2116 0.1535  0.0765  48  ASP A CG  
536  O OD1 . ASP A 48  ? 0.6019 0.8227 0.7596 -0.2201 0.1637  0.0837  48  ASP A OD1 
537  O OD2 . ASP A 48  ? 0.6557 0.8607 0.7608 -0.1924 0.1594  0.0671  48  ASP A OD2 
542  N N   . GLY A 49  ? 0.5295 0.6195 0.6114 -0.2581 0.0711  0.0847  49  GLY A N   
543  C CA  . GLY A 49  ? 0.5198 0.5563 0.5647 -0.2611 0.0496  0.0856  49  GLY A CA  
544  C C   . GLY A 49  ? 0.5416 0.5489 0.5458 -0.2359 0.0422  0.0752  49  GLY A C   
545  O O   . GLY A 49  ? 0.6360 0.5979 0.6058 -0.2349 0.0292  0.0765  49  GLY A O   
549  N N   . ARG A 50  ? 0.4555 0.4889 0.4666 -0.2156 0.0500  0.0653  50  ARG A N   
550  C CA  . ARG A 50  ? 0.4922 0.5045 0.4731 -0.1923 0.0442  0.0562  50  ARG A CA  
551  C C   . ARG A 50  ? 0.5507 0.5556 0.5357 -0.1801 0.0266  0.0440  50  ARG A C   
552  O O   . ARG A 50  ? 0.4854 0.5110 0.4984 -0.1850 0.0204  0.0403  50  ARG A O   
553  C CB  . ARG A 50  ? 0.5128 0.5513 0.4938 -0.1776 0.0613  0.0529  50  ARG A CB  
554  C CG  . ARG A 50  ? 0.5925 0.6116 0.5398 -0.1788 0.0719  0.0613  50  ARG A CG  
555  C CD  . ARG A 50  ? 0.6597 0.6825 0.6093 -0.2023 0.0859  0.0750  50  ARG A CD  
556  N NE  . ARG A 50  ? 0.7713 0.7631 0.6781 -0.2058 0.0923  0.0847  50  ARG A NE  
557  C CZ  . ARG A 50  ? 0.8152 0.8162 0.7051 -0.2032 0.1115  0.0877  50  ARG A CZ  
558  N NH1 . ARG A 50  ? 0.7342 0.7762 0.6491 -0.1957 0.1280  0.0809  50  ARG A NH1 
559  N NH2 . ARG A 50  ? 0.9053 0.8700 0.7496 -0.2075 0.1132  0.0972  50  ARG A NH2 
573  N N   . HIS A 51  ? 0.5337 0.5081 0.4900 -0.1638 0.0188  0.0381  51  HIS A N   
574  C CA  . HIS A 51  ? 0.5869 0.5478 0.5378 -0.1504 0.0058  0.0267  51  HIS A CA  
575  C C   . HIS A 51  ? 0.5607 0.5320 0.5068 -0.1277 0.0128  0.0195  51  HIS A C   
576  O O   . HIS A 51  ? 0.5999 0.5541 0.5278 -0.1178 0.0149  0.0209  51  HIS A O   
577  C CB  . HIS A 51  ? 0.6604 0.5720 0.5834 -0.1517 -0.0088 0.0261  51  HIS A CB  
578  C CG  . HIS A 51  ? 0.7578 0.6529 0.6816 -0.1759 -0.0161 0.0359  51  HIS A CG  
579  N ND1 . HIS A 51  ? 0.8396 0.7376 0.7806 -0.1914 -0.0278 0.0355  51  HIS A ND1 
580  C CD2 . HIS A 51  ? 0.7767 0.6507 0.6864 -0.1886 -0.0146 0.0475  51  HIS A CD2 
581  C CE1 . HIS A 51  ? 0.8688 0.7504 0.8097 -0.2134 -0.0325 0.0466  51  HIS A CE1 
582  N NE2 . HIS A 51  ? 0.8446 0.7105 0.7647 -0.2122 -0.0237 0.0543  51  HIS A NE2 
591  N N   . VAL A 52  ? 0.4698 0.4685 0.4340 -0.1203 0.0147  0.0127  52  VAL A N   
592  C CA  . VAL A 52  ? 0.3867 0.4008 0.3518 -0.1020 0.0224  0.0077  52  VAL A CA  
593  C C   . VAL A 52  ? 0.4035 0.4196 0.3702 -0.0906 0.0167  -0.0016 52  VAL A C   
594  O O   . VAL A 52  ? 0.3640 0.3779 0.3352 -0.0976 0.0069  -0.0045 52  VAL A O   
595  C CB  . VAL A 52  ? 0.3977 0.4486 0.3829 -0.1039 0.0354  0.0106  52  VAL A CB  
596  C CG1 . VAL A 52  ? 0.3039 0.3499 0.2798 -0.1144 0.0441  0.0201  52  VAL A CG1 
597  C CG2 . VAL A 52  ? 0.3503 0.4300 0.3652 -0.1123 0.0343  0.0091  52  VAL A CG2 
607  N N   . SER A 53  ? 0.3693 0.3876 0.3310 -0.0740 0.0219  -0.0053 53  SER A N   
608  C CA  . SER A 53  ? 0.3922 0.4168 0.3552 -0.0632 0.0207  -0.0122 53  SER A CA  
609  C C   . SER A 53  ? 0.3794 0.4380 0.3630 -0.0595 0.0276  -0.0119 53  SER A C   
610  O O   . SER A 53  ? 0.3644 0.4345 0.3532 -0.0583 0.0352  -0.0081 53  SER A O   
611  C CB  . SER A 53  ? 0.3915 0.3954 0.3378 -0.0477 0.0236  -0.0158 53  SER A CB  
612  O OG  . SER A 53  ? 0.4909 0.4606 0.4156 -0.0480 0.0170  -0.0192 53  SER A OG  
618  N N   . VAL A 54  ? 0.2869 0.3575 0.2788 -0.0572 0.0233  -0.0160 54  VAL A N   
619  C CA  . VAL A 54  ? 0.2834 0.3836 0.2954 -0.0528 0.0278  -0.0166 54  VAL A CA  
620  C C   . VAL A 54  ? 0.3400 0.4375 0.3455 -0.0411 0.0258  -0.0206 54  VAL A C   
621  O O   . VAL A 54  ? 0.3315 0.4094 0.3204 -0.0399 0.0191  -0.0236 54  VAL A O   
622  C CB  . VAL A 54  ? 0.2927 0.4157 0.3298 -0.0632 0.0234  -0.0160 54  VAL A CB  
623  C CG1 . VAL A 54  ? 0.3285 0.4809 0.3870 -0.0563 0.0292  -0.0175 54  VAL A CG1 
624  C CG2 . VAL A 54  ? 0.3272 0.4523 0.3713 -0.0775 0.0272  -0.0104 54  VAL A CG2 
634  N N   . ALA A 55  ? 0.3343 0.4480 0.3494 -0.0330 0.0316  -0.0204 55  ALA A N   
635  C CA  . ALA A 55  ? 0.3407 0.4525 0.3512 -0.0234 0.0306  -0.0224 55  ALA A CA  
636  C C   . ALA A 55  ? 0.3383 0.4730 0.3673 -0.0195 0.0305  -0.0230 55  ALA A C   
637  O O   . ALA A 55  ? 0.2541 0.4028 0.2941 -0.0194 0.0361  -0.0222 55  ALA A O   
638  C CB  . ALA A 55  ? 0.2774 0.3764 0.2772 -0.0152 0.0377  -0.0207 55  ALA A CB  
644  N N   . VAL A 56  ? 0.3158 0.4500 0.3440 -0.0159 0.0236  -0.0247 56  VAL A N   
645  C CA  . VAL A 56  ? 0.2856 0.4356 0.3285 -0.0100 0.0217  -0.0256 56  VAL A CA  
646  C C   . VAL A 56  ? 0.3334 0.4709 0.3631 -0.0029 0.0224  -0.0237 56  VAL A C   
647  O O   . VAL A 56  ? 0.3077 0.4282 0.3194 -0.0028 0.0187  -0.0232 56  VAL A O   
648  C CB  . VAL A 56  ? 0.2585 0.4193 0.3162 -0.0123 0.0101  -0.0280 56  VAL A CB  
649  C CG1 . VAL A 56  ? 0.2447 0.4204 0.3190 -0.0043 0.0079  -0.0296 56  VAL A CG1 
650  C CG2 . VAL A 56  ? 0.2959 0.4713 0.3721 -0.0215 0.0102  -0.0284 56  VAL A CG2 
660  N N   . VAL A 57  ? 0.3529 0.4966 0.3897 0.0023  0.0270  -0.0224 57  VAL A N   
661  C CA  . VAL A 57  ? 0.3185 0.4531 0.3488 0.0071  0.0286  -0.0188 57  VAL A CA  
662  C C   . VAL A 57  ? 0.3632 0.5048 0.4034 0.0115  0.0220  -0.0194 57  VAL A C   
663  O O   . VAL A 57  ? 0.3314 0.4849 0.3842 0.0137  0.0213  -0.0224 57  VAL A O   
664  C CB  . VAL A 57  ? 0.3121 0.4443 0.3448 0.0088  0.0365  -0.0155 57  VAL A CB  
665  C CG1 . VAL A 57  ? 0.2996 0.4270 0.3341 0.0124  0.0386  -0.0105 57  VAL A CG1 
666  C CG2 . VAL A 57  ? 0.2906 0.4125 0.3134 0.0065  0.0423  -0.0152 57  VAL A CG2 
676  N N   . ASP A 58  ? 0.3798 0.5107 0.4108 0.0130  0.0177  -0.0164 58  ASP A N   
677  C CA  . ASP A 58  ? 0.3229 0.4549 0.3606 0.0172  0.0091  -0.0162 58  ASP A CA  
678  C C   . ASP A 58  ? 0.2431 0.3755 0.2885 0.0194  0.0121  -0.0133 58  ASP A C   
679  O O   . ASP A 58  ? 0.2724 0.4021 0.3173 0.0175  0.0202  -0.0092 58  ASP A O   
680  C CB  . ASP A 58  ? 0.3340 0.4487 0.3538 0.0165  0.0029  -0.0121 58  ASP A CB  
681  C CG  . ASP A 58  ? 0.3384 0.4509 0.3639 0.0208  -0.0096 -0.0118 58  ASP A CG  
682  O OD1 . ASP A 58  ? 0.3162 0.4246 0.3450 0.0223  -0.0089 -0.0080 58  ASP A OD1 
683  O OD2 . ASP A 58  ? 0.2854 0.3991 0.3139 0.0226  -0.0218 -0.0152 58  ASP A OD2 
688  N N   . ARG A 59  ? 0.2689 0.4033 0.3227 0.0240  0.0040  -0.0156 59  ARG A N   
689  C CA  . ARG A 59  ? 0.2907 0.4207 0.3499 0.0255  0.0021  -0.0133 59  ARG A CA  
690  C C   . ARG A 59  ? 0.3792 0.4981 0.4349 0.0213  0.0046  -0.0035 59  ARG A C   
691  O O   . ARG A 59  ? 0.3573 0.4746 0.4220 0.0197  0.0047  0.0007  59  ARG A O   
692  C CB  . ARG A 59  ? 0.3343 0.4626 0.3987 0.0322  -0.0087 -0.0184 59  ARG A CB  
693  C CG  . ARG A 59  ? 0.3437 0.4604 0.4100 0.0332  -0.0155 -0.0160 59  ARG A CG  
694  C CD  . ARG A 59  ? 0.3552 0.4732 0.4230 0.0323  -0.0125 -0.0176 59  ARG A CD  
695  N NE  . ARG A 59  ? 0.3609 0.4646 0.4294 0.0335  -0.0237 -0.0169 59  ARG A NE  
696  C CZ  . ARG A 59  ? 0.3471 0.4445 0.4131 0.0333  -0.0275 -0.0188 59  ARG A CZ  
697  N NH1 . ARG A 59  ? 0.4036 0.5079 0.4654 0.0322  -0.0200 -0.0208 59  ARG A NH1 
698  N NH2 . ARG A 59  ? 0.3624 0.4428 0.4277 0.0337  -0.0410 -0.0182 59  ARG A NH2 
712  N N   . ASN A 60  ? 0.3472 0.4575 0.3894 0.0190  0.0065  0.0005  60  ASN A N   
713  C CA  . ASN A 60  ? 0.3022 0.4018 0.3385 0.0147  0.0134  0.0105  60  ASN A CA  
714  C C   . ASN A 60  ? 0.2747 0.3789 0.3133 0.0126  0.0292  0.0135  60  ASN A C   
715  O O   . ASN A 60  ? 0.3607 0.4605 0.4002 0.0097  0.0395  0.0219  60  ASN A O   
716  C CB  . ASN A 60  ? 0.3136 0.3961 0.3264 0.0133  0.0099  0.0142  60  ASN A CB  
717  C CG  . ASN A 60  ? 0.3669 0.4454 0.3608 0.0135  0.0119  0.0096  60  ASN A CG  
718  O OD1 . ASN A 60  ? 0.3526 0.4381 0.3479 0.0132  0.0214  0.0064  60  ASN A OD1 
719  N ND2 . ASN A 60  ? 0.4193 0.4833 0.3944 0.0137  0.0003  0.0095  60  ASN A ND2 
726  N N   . GLY A 61  ? 0.2950 0.4078 0.3358 0.0143  0.0317  0.0070  61  GLY A N   
727  C CA  . GLY A 61  ? 0.3097 0.4252 0.3543 0.0141  0.0442  0.0086  61  GLY A CA  
728  C C   . GLY A 61  ? 0.3523 0.4584 0.3747 0.0143  0.0513  0.0054  61  GLY A C   
729  O O   . GLY A 61  ? 0.4270 0.5334 0.4501 0.0156  0.0595  0.0040  61  GLY A O   
733  N N   . ASN A 62  ? 0.3528 0.4473 0.3539 0.0133  0.0457  0.0042  62  ASN A N   
734  C CA  . ASN A 62  ? 0.3891 0.4682 0.3633 0.0127  0.0489  0.0010  62  ASN A CA  
735  C C   . ASN A 62  ? 0.3645 0.4490 0.3406 0.0112  0.0408  -0.0067 62  ASN A C   
736  O O   . ASN A 62  ? 0.3872 0.4844 0.3775 0.0105  0.0297  -0.0099 62  ASN A O   
737  C CB  . ASN A 62  ? 0.4070 0.4668 0.3539 0.0112  0.0423  0.0033  62  ASN A CB  
738  C CG  . ASN A 62  ? 0.4156 0.4646 0.3525 0.0108  0.0545  0.0124  62  ASN A CG  
739  O OD1 . ASN A 62  ? 0.4410 0.4952 0.3881 0.0121  0.0715  0.0162  62  ASN A OD1 
740  N ND2 . ASN A 62  ? 0.4660 0.5002 0.3850 0.0087  0.0458  0.0168  62  ASN A ND2 
747  N N   . THR A 63  ? 0.3748 0.4492 0.3374 0.0110  0.0474  -0.0094 63  THR A N   
748  C CA  . THR A 63  ? 0.3502 0.4259 0.3125 0.0073  0.0398  -0.0152 63  THR A CA  
749  C C   . THR A 63  ? 0.3814 0.4440 0.3246 0.0039  0.0262  -0.0179 63  THR A C   
750  O O   . THR A 63  ? 0.4141 0.4525 0.3262 0.0046  0.0272  -0.0172 63  THR A O   
751  C CB  . THR A 63  ? 0.3952 0.4592 0.3476 0.0083  0.0493  -0.0170 63  THR A CB  
752  O OG1 . THR A 63  ? 0.3854 0.4603 0.3577 0.0124  0.0595  -0.0136 63  THR A OG1 
753  C CG2 . THR A 63  ? 0.3881 0.4531 0.3427 0.0023  0.0407  -0.0214 63  THR A CG2 
761  N N   . LEU A 64  ? 0.3578 0.4357 0.3195 0.0003  0.0135  -0.0207 64  LEU A N   
762  C CA  . LEU A 64  ? 0.3422 0.4124 0.2960 -0.0029 -0.0039 -0.0226 64  LEU A CA  
763  C C   . LEU A 64  ? 0.2977 0.3596 0.2452 -0.0100 -0.0116 -0.0265 64  LEU A C   
764  O O   . LEU A 64  ? 0.3127 0.3531 0.2375 -0.0132 -0.0254 -0.0280 64  LEU A O   
765  C CB  . LEU A 64  ? 0.3164 0.4115 0.3023 -0.0015 -0.0136 -0.0233 64  LEU A CB  
766  C CG  . LEU A 64  ? 0.3356 0.4366 0.3291 0.0050  -0.0105 -0.0202 64  LEU A CG  
767  C CD1 . LEU A 64  ? 0.3335 0.4557 0.3568 0.0082  -0.0210 -0.0231 64  LEU A CD1 
768  C CD2 . LEU A 64  ? 0.3797 0.4549 0.3428 0.0063  -0.0131 -0.0155 64  LEU A CD2 
780  N N   . VAL A 65  ? 0.3089 0.3849 0.2744 -0.0132 -0.0046 -0.0276 65  VAL A N   
781  C CA  . VAL A 65  ? 0.3395 0.4089 0.3035 -0.0219 -0.0121 -0.0300 65  VAL A CA  
782  C C   . VAL A 65  ? 0.3950 0.4619 0.3578 -0.0227 0.0012  -0.0297 65  VAL A C   
783  O O   . VAL A 65  ? 0.4024 0.4868 0.3822 -0.0194 0.0122  -0.0274 65  VAL A O   
784  C CB  . VAL A 65  ? 0.3241 0.4212 0.3249 -0.0285 -0.0226 -0.0303 65  VAL A CB  
785  C CG1 . VAL A 65  ? 0.2998 0.3914 0.3037 -0.0402 -0.0301 -0.0311 65  VAL A CG1 
786  C CG2 . VAL A 65  ? 0.3371 0.4369 0.3443 -0.0266 -0.0393 -0.0307 65  VAL A CG2 
796  N N   . THR A 66  ? 0.3674 0.4086 0.3072 -0.0267 -0.0020 -0.0320 66  THR A N   
797  C CA  . THR A 66  ? 0.3824 0.4193 0.3235 -0.0294 0.0055  -0.0315 66  THR A CA  
798  C C   . THR A 66  ? 0.4152 0.4362 0.3494 -0.0409 -0.0080 -0.0334 66  THR A C   
799  O O   . THR A 66  ? 0.3628 0.3622 0.2762 -0.0437 -0.0216 -0.0367 66  THR A O   
800  C CB  . THR A 66  ? 0.3648 0.3807 0.2838 -0.0194 0.0190  -0.0324 66  THR A CB  
801  O OG1 . THR A 66  ? 0.4396 0.4199 0.3219 -0.0179 0.0150  -0.0371 66  THR A OG1 
802  C CG2 . THR A 66  ? 0.3724 0.4015 0.2986 -0.0096 0.0304  -0.0296 66  THR A CG2 
810  N N   . LEU A 67  ? 0.3516 0.3810 0.3017 -0.0486 -0.0056 -0.0306 67  LEU A N   
811  C CA  . LEU A 67  ? 0.3087 0.3231 0.2558 -0.0618 -0.0179 -0.0307 67  LEU A CA  
812  C C   . LEU A 67  ? 0.3924 0.3933 0.3323 -0.0634 -0.0099 -0.0285 67  LEU A C   
813  O O   . LEU A 67  ? 0.3946 0.4159 0.3527 -0.0638 0.0006  -0.0236 67  LEU A O   
814  C CB  . LEU A 67  ? 0.3385 0.3845 0.3236 -0.0743 -0.0255 -0.0270 67  LEU A CB  
815  C CG  . LEU A 67  ? 0.3700 0.4343 0.3720 -0.0727 -0.0360 -0.0284 67  LEU A CG  
816  C CD1 . LEU A 67  ? 0.2870 0.3903 0.3364 -0.0822 -0.0370 -0.0244 67  LEU A CD1 
817  C CD2 . LEU A 67  ? 0.4227 0.4555 0.3988 -0.0759 -0.0570 -0.0325 67  LEU A CD2 
829  N N   . ARG A 68  ? 0.4256 0.3883 0.3356 -0.0634 -0.0159 -0.0322 68  ARG A N   
830  C CA  . ARG A 68  ? 0.4234 0.3675 0.3250 -0.0646 -0.0118 -0.0302 68  ARG A CA  
831  C C   . ARG A 68  ? 0.4524 0.3878 0.3600 -0.0835 -0.0251 -0.0266 68  ARG A C   
832  O O   . ARG A 68  ? 0.4412 0.3494 0.3312 -0.0902 -0.0408 -0.0307 68  ARG A O   
833  C CB  . ARG A 68  ? 0.4494 0.3548 0.3159 -0.0511 -0.0085 -0.0369 68  ARG A CB  
834  C CG  . ARG A 68  ? 0.5087 0.3939 0.3689 -0.0490 -0.0051 -0.0350 68  ARG A CG  
835  C CD  . ARG A 68  ? 0.5981 0.4440 0.4258 -0.0341 -0.0014 -0.0431 68  ARG A CD  
836  N NE  . ARG A 68  ? 0.6936 0.5493 0.5187 -0.0174 0.0136  -0.0465 68  ARG A NE  
837  C CZ  . ARG A 68  ? 0.6963 0.5541 0.5278 -0.0018 0.0283  -0.0465 68  ARG A CZ  
838  N NH1 . ARG A 68  ? 0.6479 0.4962 0.4868 0.0014  0.0284  -0.0440 68  ARG A NH1 
839  N NH2 . ARG A 68  ? 0.6537 0.5226 0.4859 0.0105  0.0423  -0.0482 68  ARG A NH2 
853  N N   . GLY A 69  ? 0.4420 0.3985 0.3726 -0.0928 -0.0190 -0.0186 69  GLY A N   
854  C CA  . GLY A 69  ? 0.4648 0.4176 0.4062 -0.1129 -0.0283 -0.0126 69  GLY A CA  
855  C C   . GLY A 69  ? 0.4599 0.3651 0.3712 -0.1166 -0.0390 -0.0142 69  GLY A C   
856  O O   . GLY A 69  ? 0.5404 0.4195 0.4266 -0.1023 -0.0341 -0.0183 69  GLY A O   
860  N N   . ASP A 70  ? 0.4497 0.3436 0.3665 -0.1358 -0.0543 -0.0111 70  ASP A N   
861  C CA  . ASP A 70  ? 0.4858 0.3318 0.3750 -0.1424 -0.0670 -0.0117 70  ASP A CA  
862  C C   . ASP A 70  ? 0.6045 0.4448 0.4920 -0.1445 -0.0567 -0.0033 70  ASP A C   
863  O O   . ASP A 70  ? 0.6834 0.5531 0.5963 -0.1570 -0.0480 0.0072  70  ASP A O   
864  C CB  . ASP A 70  ? 0.5573 0.3963 0.4594 -0.1660 -0.0876 -0.0081 70  ASP A CB  
865  C CG  . ASP A 70  ? 0.6465 0.4903 0.5516 -0.1656 -0.1024 -0.0153 70  ASP A CG  
866  O OD1 . ASP A 70  ? 0.6472 0.4724 0.5217 -0.1473 -0.1018 -0.0256 70  ASP A OD1 
867  O OD2 . ASP A 70  ? 0.6814 0.5470 0.6201 -0.1840 -0.1148 -0.0099 70  ASP A OD2 
872  N N   . GLY A 71  ? 0.5734 0.3743 0.4297 -0.1313 -0.0574 -0.0079 71  GLY A N   
873  C CA  . GLY A 71  ? 0.6055 0.3931 0.4559 -0.1318 -0.0522 -0.0001 71  GLY A CA  
874  C C   . GLY A 71  ? 0.5427 0.3573 0.4026 -0.1164 -0.0349 0.0020  71  GLY A C   
875  O O   . GLY A 71  ? 0.5910 0.3947 0.4449 -0.1152 -0.0319 0.0088  71  GLY A O   
879  N N   . ALA A 72  ? 0.5293 0.3761 0.4028 -0.1051 -0.0257 -0.0034 72  ALA A N   
880  C CA  . ALA A 72  ? 0.4976 0.3696 0.3815 -0.0912 -0.0117 -0.0019 72  ALA A CA  
881  C C   . ALA A 72  ? 0.5512 0.3964 0.4191 -0.0722 -0.0105 -0.0058 72  ALA A C   
882  O O   . ALA A 72  ? 0.6040 0.4179 0.4531 -0.0636 -0.0157 -0.0137 72  ALA A O   
883  C CB  . ALA A 72  ? 0.4304 0.3361 0.3300 -0.0836 -0.0047 -0.0071 72  ALA A CB  
889  N N   . GLY A 73  ? 0.5417 0.3985 0.4175 -0.0650 -0.0040 -0.0005 73  GLY A N   
890  C CA  . GLY A 73  ? 0.4744 0.3124 0.3452 -0.0463 -0.0036 -0.0029 73  GLY A CA  
891  C C   . GLY A 73  ? 0.4878 0.3376 0.3656 -0.0280 0.0054  -0.0122 73  GLY A C   
892  O O   . GLY A 73  ? 0.5062 0.3856 0.3953 -0.0291 0.0119  -0.0140 73  GLY A O   
896  N N   . PRO A 74  ? 0.5573 0.3840 0.4292 -0.0106 0.0068  -0.0178 74  PRO A N   
897  C CA  . PRO A 74  ? 0.5752 0.4101 0.4510 0.0064  0.0189  -0.0261 74  PRO A CA  
898  C C   . PRO A 74  ? 0.5685 0.4409 0.4729 0.0142  0.0284  -0.0223 74  PRO A C   
899  O O   . PRO A 74  ? 0.5653 0.4506 0.4761 0.0249  0.0399  -0.0269 74  PRO A O   
900  C CB  . PRO A 74  ? 0.5813 0.3812 0.4467 0.0231  0.0194  -0.0320 74  PRO A CB  
901  C CG  . PRO A 74  ? 0.6233 0.4091 0.4930 0.0195  0.0078  -0.0240 74  PRO A CG  
902  C CD  . PRO A 74  ? 0.5598 0.3525 0.4233 -0.0047 -0.0013 -0.0158 74  PRO A CD  
910  N N   . GLN A 75  ? 0.5607 0.4469 0.4788 0.0082  0.0231  -0.0136 75  GLN A N   
911  C CA  . GLN A 75  ? 0.5108 0.4283 0.4538 0.0137  0.0280  -0.0097 75  GLN A CA  
912  C C   . GLN A 75  ? 0.4678 0.4135 0.4142 0.0020  0.0305  -0.0081 75  GLN A C   
913  O O   . GLN A 75  ? 0.4731 0.4436 0.4369 0.0065  0.0351  -0.0069 75  GLN A O   
914  C CB  . GLN A 75  ? 0.4752 0.3868 0.4264 0.0151  0.0182  -0.0018 75  GLN A CB  
915  C CG  . GLN A 75  ? 0.3880 0.2987 0.3254 -0.0022 0.0106  0.0058  75  GLN A CG  
916  C CD  . GLN A 75  ? 0.5384 0.4254 0.4523 -0.0163 0.0062  0.0065  75  GLN A CD  
917  O OE1 . GLN A 75  ? 0.6135 0.4790 0.5179 -0.0128 0.0053  0.0008  75  GLN A OE1 
918  N NE2 . GLN A 75  ? 0.6686 0.5578 0.5720 -0.0327 0.0040  0.0138  75  GLN A NE2 
927  N N   . SER A 76  ? 0.5132 0.3721 0.4791 0.0447  0.0290  0.0565  76  SER A N   
928  C CA  . SER A 76  ? 0.4960 0.3786 0.4176 0.0291  0.0261  0.0562  76  SER A CA  
929  C C   . SER A 76  ? 0.4566 0.3759 0.3847 0.0249  0.0385  0.0394  76  SER A C   
930  O O   . SER A 76  ? 0.4207 0.3630 0.3338 0.0219  0.0286  0.0403  76  SER A O   
931  C CB  . SER A 76  ? 0.5483 0.4097 0.4214 0.0091  0.0370  0.0552  76  SER A CB  
932  O OG  . SER A 76  ? 0.5045 0.3549 0.3846 0.0021  0.0636  0.0380  76  SER A OG  
938  N N   . TYR A 77  ? 0.4626 0.3861 0.4121 0.0234  0.0601  0.0241  77  TYR A N   
939  C CA  . TYR A 77  ? 0.4108 0.3642 0.3570 0.0159  0.0721  0.0125  77  TYR A CA  
940  C C   . TYR A 77  ? 0.3983 0.3707 0.3665 0.0236  0.0598  0.0172  77  TYR A C   
941  O O   . TYR A 77  ? 0.3417 0.3273 0.2901 0.0202  0.0525  0.0204  77  TYR A O   
942  C CB  . TYR A 77  ? 0.4237 0.3814 0.3888 0.0089  0.0984  -0.0056 77  TYR A CB  
943  C CG  . TYR A 77  ? 0.4082 0.3951 0.3573 -0.0038 0.1117  -0.0145 77  TYR A CG  
944  C CD1 . TYR A 77  ? 0.4429 0.4413 0.3515 -0.0159 0.1181  -0.0190 77  TYR A CD1 
945  C CD2 . TYR A 77  ? 0.4438 0.4483 0.4166 -0.0053 0.1174  -0.0183 77  TYR A CD2 
946  C CE1 . TYR A 77  ? 0.3607 0.3854 0.2516 -0.0257 0.1258  -0.0225 77  TYR A CE1 
947  C CE2 . TYR A 77  ? 0.4155 0.4410 0.3657 -0.0195 0.1279  -0.0209 77  TYR A CE2 
948  C CZ  . TYR A 77  ? 0.4329 0.4674 0.3414 -0.0280 0.1302  -0.0208 77  TYR A CZ  
949  O OH  . TYR A 77  ? 0.4505 0.5058 0.3336 -0.0401 0.1360  -0.0190 77  TYR A OH  
959  N N   . ASP A 78  ? 0.3714 0.3454 0.3841 0.0341  0.0576  0.0151  78  ASP A N   
960  C CA  . ASP A 78  ? 0.4008 0.3959 0.4387 0.0379  0.0494  0.0149  78  ASP A CA  
961  C C   . ASP A 78  ? 0.3969 0.3951 0.4235 0.0434  0.0244  0.0277  78  ASP A C   
962  O O   . ASP A 78  ? 0.4084 0.4222 0.4380 0.0400  0.0196  0.0264  78  ASP A O   
963  C CB  . ASP A 78  ? 0.4697 0.4746 0.5640 0.0479  0.0529  0.0037  78  ASP A CB  
964  C CG  . ASP A 78  ? 0.4755 0.4882 0.5869 0.0376  0.0813  -0.0164 78  ASP A CG  
965  O OD1 . ASP A 78  ? 0.4398 0.4575 0.5177 0.0203  0.0968  -0.0191 78  ASP A OD1 
966  O OD2 . ASP A 78  ? 0.4507 0.4680 0.6109 0.0468  0.0874  -0.0311 78  ASP A OD2 
971  N N   A SER A 79  ? 0.4250 0.4074 0.4371 0.0488  0.0099  0.0391  79  SER A N   
972  N N   B SER A 79  ? 0.4204 0.4030 0.4325 0.0488  0.0097  0.0392  79  SER A N   
973  C CA  A SER A 79  ? 0.4019 0.3927 0.3985 0.0494  -0.0131 0.0495  79  SER A CA  
974  C CA  B SER A 79  ? 0.4059 0.3971 0.4025 0.0493  -0.0132 0.0494  79  SER A CA  
975  C C   A SER A 79  ? 0.3902 0.3908 0.3525 0.0371  -0.0115 0.0448  79  SER A C   
976  C C   B SER A 79  ? 0.3925 0.3933 0.3549 0.0371  -0.0113 0.0446  79  SER A C   
977  O O   A SER A 79  ? 0.3883 0.4075 0.3554 0.0358  -0.0218 0.0419  79  SER A O   
978  O O   B SER A 79  ? 0.3858 0.4052 0.3533 0.0357  -0.0213 0.0416  79  SER A O   
979  C CB  A SER A 79  ? 0.4529 0.4204 0.4298 0.0523  -0.0270 0.0655  79  SER A CB  
980  C CB  B SER A 79  ? 0.4484 0.4171 0.4248 0.0520  -0.0276 0.0655  79  SER A CB  
981  O OG  A SER A 79  ? 0.4619 0.4431 0.4166 0.0474  -0.0480 0.0745  79  SER A OG  
982  O OG  B SER A 79  ? 0.4412 0.3998 0.4554 0.0692  -0.0364 0.0722  79  SER A OG  
993  N N   . ALA A 80  ? 0.4138 0.4043 0.3458 0.0288  0.0016  0.0409  80  ALA A N   
994  C CA  . ALA A 80  ? 0.4096 0.4126 0.3150 0.0210  0.0019  0.0333  80  ALA A CA  
995  C C   . ALA A 80  ? 0.3823 0.3951 0.3047 0.0237  0.0052  0.0288  80  ALA A C   
996  O O   . ALA A 80  ? 0.4032 0.4257 0.3213 0.0233  -0.0031 0.0242  80  ALA A O   
997  C CB  . ALA A 80  ? 0.4446 0.4420 0.3211 0.0127  0.0161  0.0270  80  ALA A CB  
1003 N N   . ASP A 81  ? 0.3448 0.3535 0.2869 0.0246  0.0184  0.0288  81  ASP A N   
1004 C CA  . ASP A 81  ? 0.3815 0.3932 0.3334 0.0219  0.0240  0.0277  81  ASP A CA  
1005 C C   . ASP A 81  ? 0.3571 0.3761 0.3342 0.0242  0.0124  0.0267  81  ASP A C   
1006 O O   . ASP A 81  ? 0.4332 0.4501 0.4074 0.0221  0.0085  0.0255  81  ASP A O   
1007 C CB  . ASP A 81  ? 0.4442 0.4555 0.4108 0.0164  0.0432  0.0246  81  ASP A CB  
1008 C CG  . ASP A 81  ? 0.5292 0.5385 0.4790 0.0066  0.0535  0.0274  81  ASP A CG  
1009 O OD1 . ASP A 81  ? 0.5861 0.5884 0.5264 0.0077  0.0437  0.0333  81  ASP A OD1 
1010 O OD2 . ASP A 81  ? 0.6454 0.6590 0.5909 -0.0032 0.0712  0.0237  81  ASP A OD2 
1015 N N   . ARG A 82  ? 0.3789 0.4070 0.3832 0.0291  0.0062  0.0260  82  ARG A N   
1016 C CA  . ARG A 82  ? 0.3860 0.4306 0.4175 0.0296  -0.0047 0.0215  82  ARG A CA  
1017 C C   . ARG A 82  ? 0.3400 0.3928 0.3557 0.0283  -0.0208 0.0198  82  ARG A C   
1018 O O   . ARG A 82  ? 0.3846 0.4489 0.4159 0.0240  -0.0253 0.0114  82  ARG A O   
1019 C CB  . ARG A 82  ? 0.3301 0.3897 0.3958 0.0383  -0.0119 0.0208  82  ARG A CB  
1020 C CG  . ARG A 82  ? 0.3222 0.3845 0.4187 0.0385  0.0054  0.0129  82  ARG A CG  
1021 C CD  . ARG A 82  ? 0.4343 0.5239 0.5799 0.0479  -0.0044 0.0047  82  ARG A CD  
1022 N NE  . ARG A 82  ? 0.5550 0.6529 0.7370 0.0492  0.0125  -0.0088 82  ARG A NE  
1023 C CZ  . ARG A 82  ? 0.6674 0.7976 0.8999 0.0511  0.0137  -0.0260 82  ARG A CZ  
1024 N NH1 . ARG A 82  ? 0.7237 0.8809 0.9747 0.0517  -0.0014 -0.0304 82  ARG A NH1 
1025 N NH2 . ARG A 82  ? 0.7037 0.8453 0.9712 0.0504  0.0317  -0.0435 82  ARG A NH2 
1039 N N   . LYS A 83  ? 0.3056 0.3546 0.2915 0.0286  -0.0271 0.0242  83  LYS A N   
1040 C CA  . LYS A 83  ? 0.3242 0.3874 0.2934 0.0232  -0.0397 0.0177  83  LYS A CA  
1041 C C   . LYS A 83  ? 0.3398 0.4003 0.3050 0.0212  -0.0353 0.0064  83  LYS A C   
1042 O O   . LYS A 83  ? 0.3871 0.4621 0.3625 0.0174  -0.0426 -0.0064 83  LYS A O   
1043 C CB  . LYS A 83  ? 0.3027 0.3621 0.2372 0.0189  -0.0438 0.0234  83  LYS A CB  
1044 C CG  . LYS A 83  ? 0.3485 0.4089 0.2815 0.0201  -0.0570 0.0371  83  LYS A CG  
1045 C CD  . LYS A 83  ? 0.4057 0.4527 0.2967 0.0106  -0.0579 0.0446  83  LYS A CD  
1046 C CE  . LYS A 83  ? 0.4385 0.4731 0.3231 0.0134  -0.0725 0.0654  83  LYS A CE  
1047 N NZ  . LYS A 83  ? 0.4859 0.4962 0.3248 0.0002  -0.0695 0.0748  83  LYS A NZ  
1061 N N   . ALA A 84  ? 0.3473 0.3904 0.2992 0.0242  -0.0244 0.0101  84  ALA A N   
1062 C CA  . ALA A 84  ? 0.3253 0.3613 0.2736 0.0271  -0.0239 0.0038  84  ALA A CA  
1063 C C   . ALA A 84  ? 0.3420 0.3655 0.3156 0.0262  -0.0216 0.0038  84  ALA A C   
1064 O O   . ALA A 84  ? 0.4116 0.4311 0.3955 0.0278  -0.0271 -0.0059 84  ALA A O   
1065 C CB  . ALA A 84  ? 0.4282 0.4528 0.3541 0.0300  -0.0149 0.0110  84  ALA A CB  
1071 N N   . PHE A 85  ? 0.3275 0.3448 0.3138 0.0221  -0.0120 0.0119  85  PHE A N   
1072 C CA  . PHE A 85  ? 0.3465 0.3535 0.3556 0.0152  -0.0057 0.0104  85  PHE A CA  
1073 C C   . PHE A 85  ? 0.3526 0.3785 0.3874 0.0117  -0.0149 -0.0051 85  PHE A C   
1074 O O   . PHE A 85  ? 0.3553 0.3684 0.4046 0.0064  -0.0127 -0.0128 85  PHE A O   
1075 C CB  . PHE A 85  ? 0.3064 0.3170 0.3284 0.0090  0.0075  0.0148  85  PHE A CB  
1076 C CG  . PHE A 85  ? 0.3232 0.3286 0.3684 -0.0038 0.0177  0.0097  85  PHE A CG  
1077 C CD1 . PHE A 85  ? 0.3767 0.3527 0.4065 -0.0145 0.0310  0.0191  85  PHE A CD1 
1078 C CD2 . PHE A 85  ? 0.2935 0.3252 0.3731 -0.0076 0.0141  -0.0043 85  PHE A CD2 
1079 C CE1 . PHE A 85  ? 0.3778 0.3456 0.4245 -0.0319 0.0434  0.0140  85  PHE A CE1 
1080 C CE2 . PHE A 85  ? 0.3073 0.3380 0.4093 -0.0232 0.0263  -0.0134 85  PHE A CE2 
1081 C CZ  . PHE A 85  ? 0.3712 0.3674 0.4560 -0.0368 0.0425  -0.0045 85  PHE A CZ  
1091 N N   . THR A 86  ? 0.3710 0.4262 0.4096 0.0131  -0.0252 -0.0094 86  THR A N   
1092 C CA  . THR A 86  ? 0.3423 0.4265 0.4018 0.0071  -0.0353 -0.0248 86  THR A CA  
1093 C C   . THR A 86  ? 0.3290 0.4167 0.3828 0.0050  -0.0414 -0.0404 86  THR A C   
1094 O O   . THR A 86  ? 0.3606 0.4583 0.4378 -0.0026 -0.0419 -0.0585 86  THR A O   
1095 C CB  . THR A 86  ? 0.3306 0.4443 0.3875 0.0094  -0.0486 -0.0198 86  THR A CB  
1096 O OG1 . THR A 86  ? 0.3789 0.4893 0.4494 0.0155  -0.0438 -0.0090 86  THR A OG1 
1097 C CG2 . THR A 86  ? 0.3341 0.4864 0.4109 0.0010  -0.0605 -0.0350 86  THR A CG2 
1105 N N   . ALA A 87  ? 0.3258 0.4088 0.3525 0.0106  -0.0445 -0.0378 87  ALA A N   
1106 C CA  . ALA A 87  ? 0.3548 0.4490 0.3808 0.0094  -0.0500 -0.0582 87  ALA A CA  
1107 C C   . ALA A 87  ? 0.3685 0.4335 0.4140 0.0157  -0.0455 -0.0660 87  ALA A C   
1108 O O   . ALA A 87  ? 0.3390 0.4135 0.4064 0.0129  -0.0485 -0.0900 87  ALA A O   
1109 C CB  . ALA A 87  ? 0.3397 0.4403 0.3339 0.0124  -0.0527 -0.0565 87  ALA A CB  
1115 N N   . VAL A 88  ? 0.3548 0.3830 0.3917 0.0230  -0.0385 -0.0459 88  VAL A N   
1116 C CA  . VAL A 88  ? 0.3791 0.3692 0.4266 0.0299  -0.0370 -0.0450 88  VAL A CA  
1117 C C   . VAL A 88  ? 0.3693 0.3413 0.4437 0.0181  -0.0286 -0.0492 88  VAL A C   
1118 O O   . VAL A 88  ? 0.4068 0.3466 0.4979 0.0203  -0.0280 -0.0555 88  VAL A O   
1119 C CB  . VAL A 88  ? 0.4275 0.3867 0.4472 0.0387  -0.0340 -0.0189 88  VAL A CB  
1120 C CG1 . VAL A 88  ? 0.3992 0.3438 0.4117 0.0271  -0.0204 0.0002  88  VAL A CG1 
1121 C CG2 . VAL A 88  ? 0.3920 0.3136 0.4163 0.0514  -0.0405 -0.0157 88  VAL A CG2 
1131 N N   . SER A 89  ? 0.3775 0.3700 0.4585 0.0058  -0.0223 -0.0475 89  SER A N   
1132 C CA  . SER A 89  ? 0.3757 0.3613 0.4838 -0.0094 -0.0121 -0.0562 89  SER A CA  
1133 C C   . SER A 89  ? 0.3667 0.3765 0.5054 -0.0169 -0.0161 -0.0873 89  SER A C   
1134 O O   . SER A 89  ? 0.3487 0.3352 0.5110 -0.0267 -0.0073 -0.0998 89  SER A O   
1135 C CB  . SER A 89  ? 0.4263 0.4393 0.5398 -0.0181 -0.0062 -0.0511 89  SER A CB  
1136 O OG  . SER A 89  ? 0.4462 0.4334 0.5413 -0.0186 0.0047  -0.0295 89  SER A OG  
1142 N N   . TRP A 90  ? 0.3558 0.4119 0.4919 -0.0154 -0.0278 -0.1008 90  TRP A N   
1143 C CA  . TRP A 90  ? 0.3852 0.4778 0.5472 -0.0268 -0.0313 -0.1340 90  TRP A CA  
1144 C C   . TRP A 90  ? 0.3899 0.4869 0.5517 -0.0194 -0.0381 -0.1530 90  TRP A C   
1145 O O   . TRP A 90  ? 0.3649 0.4961 0.5484 -0.0303 -0.0396 -0.1859 90  TRP A O   
1146 C CB  . TRP A 90  ? 0.3304 0.4818 0.4890 -0.0366 -0.0403 -0.1377 90  TRP A CB  
1147 C CG  . TRP A 90  ? 0.3034 0.4687 0.4840 -0.0468 -0.0345 -0.1378 90  TRP A CG  
1148 C CD1 . TRP A 90  ? 0.3781 0.5675 0.5926 -0.0641 -0.0286 -0.1652 90  TRP A CD1 
1149 C CD2 . TRP A 90  ? 0.3026 0.4647 0.4781 -0.0417 -0.0326 -0.1150 90  TRP A CD2 
1150 N NE1 . TRP A 90  ? 0.3826 0.5871 0.6127 -0.0701 -0.0238 -0.1607 90  TRP A NE1 
1151 C CE2 . TRP A 90  ? 0.3689 0.5574 0.5776 -0.0557 -0.0265 -0.1307 90  TRP A CE2 
1152 C CE3 . TRP A 90  ? 0.3142 0.4575 0.4646 -0.0280 -0.0341 -0.0874 90  TRP A CE3 
1153 C CZ2 . TRP A 90  ? 0.3629 0.5621 0.5829 -0.0545 -0.0229 -0.1209 90  TRP A CZ2 
1154 C CZ3 . TRP A 90  ? 0.3083 0.4586 0.4703 -0.0270 -0.0296 -0.0776 90  TRP A CZ3 
1155 C CH2 . TRP A 90  ? 0.3010 0.4803 0.4988 -0.0393 -0.0245 -0.0948 90  TRP A CH2 
1166 N N   . ASN A 91  ? 0.4640 0.2712 0.4360 -0.0243 0.0580  -0.0728 91  ASN A N   
1167 C CA  . ASN A 91  ? 0.4625 0.2714 0.4259 0.0086  0.0767  -0.0670 91  ASN A CA  
1168 C C   . ASN A 91  ? 0.5004 0.3206 0.4253 0.0360  0.0874  -0.0821 91  ASN A C   
1169 O O   . ASN A 91  ? 0.5277 0.3223 0.4226 0.0710  0.0929  -0.0991 91  ASN A O   
1170 C CB  . ASN A 91  ? 0.4658 0.2189 0.4321 0.0259  0.0702  -0.0724 91  ASN A CB  
1171 C CG  . ASN A 91  ? 0.4699 0.2391 0.4405 0.0624  0.0932  -0.0555 91  ASN A CG  
1172 O OD1 . ASN A 91  ? 0.5178 0.3499 0.5062 0.0600  0.1100  -0.0263 91  ASN A OD1 
1173 N ND2 . ASN A 91  ? 0.5513 0.2629 0.5054 0.0974  0.0923  -0.0728 91  ASN A ND2 
1180 N N   . ALA A 92  ? 0.4884 0.3492 0.4142 0.0226  0.0899  -0.0748 92  ALA A N   
1181 C CA  . ALA A 92  ? 0.5290 0.4156 0.4269 0.0431  0.0981  -0.0785 92  ALA A CA  
1182 C C   . ALA A 92  ? 0.4181 0.3513 0.3370 0.0251  0.1012  -0.0542 92  ALA A C   
1183 O O   . ALA A 92  ? 0.4080 0.3396 0.3496 -0.0020 0.0933  -0.0502 92  ALA A O   
1184 C CB  . ALA A 92  ? 0.6217 0.4780 0.4840 0.0450  0.0828  -0.1108 92  ALA A CB  
1190 N N   . PRO A 93  ? 0.4567 0.4324 0.3680 0.0417  0.1114  -0.0367 93  PRO A N   
1191 C CA  . PRO A 93  ? 0.3779 0.3866 0.3117 0.0225  0.1079  -0.0117 93  PRO A CA  
1192 C C   . PRO A 93  ? 0.4139 0.4050 0.3462 0.0063  0.0942  -0.0280 93  PRO A C   
1193 O O   . PRO A 93  ? 0.4516 0.4314 0.3579 0.0150  0.0893  -0.0497 93  PRO A O   
1194 C CB  . PRO A 93  ? 0.4726 0.5357 0.3968 0.0461  0.1187  0.0127  93  PRO A CB  
1195 C CG  . PRO A 93  ? 0.5399 0.6078 0.4427 0.0807  0.1343  0.0065  93  PRO A CG  
1196 C CD  . PRO A 93  ? 0.5533 0.5529 0.4373 0.0811  0.1263  -0.0352 93  PRO A CD  
1204 N N   . THR A 94  ? 0.3677 0.3565 0.3257 -0.0154 0.0870  -0.0182 94  THR A N   
1205 C CA  . THR A 94  ? 0.3657 0.3440 0.3278 -0.0244 0.0770  -0.0289 94  THR A CA  
1206 C C   . THR A 94  ? 0.3968 0.4036 0.3539 -0.0151 0.0751  -0.0153 94  THR A C   
1207 O O   . THR A 94  ? 0.4617 0.4689 0.4188 -0.0176 0.0677  -0.0215 94  THR A O   
1208 C CB  . THR A 94  ? 0.3655 0.3302 0.3516 -0.0407 0.0713  -0.0254 94  THR A CB  
1209 O OG1 . THR A 94  ? 0.4309 0.4049 0.4325 -0.0470 0.0689  0.0002  94  THR A OG1 
1210 C CG2 . THR A 94  ? 0.4027 0.3533 0.3904 -0.0501 0.0725  -0.0395 94  THR A CG2 
1218 N N   . SER A 95  ? 0.3757 0.4180 0.3321 -0.0043 0.0818  0.0098  95  SER A N   
1219 C CA  . SER A 95  ? 0.3912 0.4783 0.3425 0.0063  0.0812  0.0297  95  SER A CA  
1220 C C   . SER A 95  ? 0.4400 0.5306 0.3480 0.0228  0.0823  0.0007  95  SER A C   
1221 O O   . SER A 95  ? 0.4929 0.6059 0.3938 0.0225  0.0750  0.0030  95  SER A O   
1222 C CB  . SER A 95  ? 0.3954 0.5361 0.3561 0.0161  0.0897  0.0688  95  SER A CB  
1223 O OG  . SER A 95  ? 0.4701 0.6152 0.4080 0.0360  0.1042  0.0579  95  SER A OG  
1229 N N   A GLU A 96  ? 0.4763 0.5418 0.3558 0.0363  0.0887  -0.0258 96  GLU A N   
1230 N N   B GLU A 96  ? 0.4761 0.5411 0.3552 0.0362  0.0884  -0.0264 96  GLU A N   
1231 C CA  A GLU A 96  ? 0.5516 0.5996 0.3831 0.0510  0.0841  -0.0618 96  GLU A CA  
1232 C CA  B GLU A 96  ? 0.5517 0.6018 0.3826 0.0508  0.0835  -0.0614 96  GLU A CA  
1233 C C   A GLU A 96  ? 0.5662 0.5740 0.4000 0.0264  0.0652  -0.0838 96  GLU A C   
1234 C C   B GLU A 96  ? 0.5685 0.5743 0.4006 0.0267  0.0649  -0.0855 96  GLU A C   
1235 O O   A GLU A 96  ? 0.6181 0.6326 0.4266 0.0236  0.0525  -0.0971 96  GLU A O   
1236 O O   B GLU A 96  ? 0.6282 0.6351 0.4319 0.0243  0.0516  -0.1024 96  GLU A O   
1237 C CB  A GLU A 96  ? 0.5934 0.6115 0.4011 0.0740  0.0939  -0.0821 96  GLU A CB  
1238 C CB  B GLU A 96  ? 0.6001 0.6280 0.4013 0.0782  0.0945  -0.0817 96  GLU A CB  
1239 C CG  A GLU A 96  ? 0.6514 0.6147 0.4122 0.0831  0.0811  -0.1287 96  GLU A CG  
1240 C CG  B GLU A 96  ? 0.5981 0.6881 0.3936 0.1097  0.1153  -0.0547 96  GLU A CG  
1241 C CD  A GLU A 96  ? 0.6459 0.5600 0.4005 0.1008  0.0871  -0.1451 96  GLU A CD  
1242 C CD  B GLU A 96  ? 0.5902 0.7397 0.3569 0.1268  0.1160  -0.0483 96  GLU A CD  
1243 O OE1 A GLU A 96  ? 0.6111 0.5565 0.3721 0.1274  0.1078  -0.1263 96  GLU A OE1 
1244 O OE1 B GLU A 96  ? 0.6824 0.8080 0.4061 0.1397  0.1075  -0.0841 96  GLU A OE1 
1245 O OE2 A GLU A 96  ? 0.6486 0.4978 0.3998 0.0856  0.0689  -0.1700 96  GLU A OE2 
1246 O OE2 B GLU A 96  ? 0.4447 0.6601 0.2414 0.1202  0.1192  -0.0032 96  GLU A OE2 
1259 N N   . LEU A 97  ? 0.5078 0.4841 0.3723 0.0079  0.0628  -0.0834 97  LEU A N   
1260 C CA  . LEU A 97  ? 0.5257 0.4777 0.3995 -0.0144 0.0468  -0.0958 97  LEU A CA  
1261 C C   . LEU A 97  ? 0.5405 0.5250 0.4293 -0.0241 0.0395  -0.0813 97  LEU A C   
1262 O O   . LEU A 97  ? 0.5618 0.5456 0.4475 -0.0382 0.0240  -0.0883 97  LEU A O   
1263 C CB  . LEU A 97  ? 0.4713 0.4054 0.3775 -0.0279 0.0499  -0.0904 97  LEU A CB  
1264 C CG  . LEU A 97  ? 0.4817 0.3861 0.3828 -0.0220 0.0547  -0.0984 97  LEU A CG  
1265 C CD1 . LEU A 97  ? 0.4708 0.3781 0.4055 -0.0360 0.0595  -0.0851 97  LEU A CD1 
1266 C CD2 . LEU A 97  ? 0.5373 0.4000 0.4167 -0.0263 0.0372  -0.1217 97  LEU A CD2 
1278 N N   . ALA A 98  ? 0.5158 0.5304 0.4256 -0.0176 0.0485  -0.0561 98  ALA A N   
1279 C CA  . ALA A 98  ? 0.4955 0.5392 0.4271 -0.0221 0.0426  -0.0366 98  ALA A CA  
1280 C C   . ALA A 98  ? 0.4946 0.5717 0.3979 -0.0201 0.0327  -0.0376 98  ALA A C   
1281 O O   . ALA A 98  ? 0.5373 0.6409 0.4560 -0.0274 0.0238  -0.0236 98  ALA A O   
1282 C CB  . ALA A 98  ? 0.4985 0.5568 0.4608 -0.0170 0.0494  -0.0068 98  ALA A CB  
1288 N N   . LYS A 99  ? 0.4902 0.5696 0.3499 -0.0076 0.0344  -0.0544 99  LYS A N   
1289 C CA  . LYS A 99  ? 0.5223 0.6376 0.3425 -0.0026 0.0246  -0.0604 99  LYS A CA  
1290 C C   . LYS A 99  ? 0.5392 0.6195 0.3234 -0.0176 0.0027  -0.0955 99  LYS A C   
1291 O O   . LYS A 99  ? 0.5699 0.6767 0.3203 -0.0220 -0.0127 -0.1029 99  LYS A O   
1292 C CB  . LYS A 99  ? 0.5907 0.7355 0.3754 0.0253  0.0384  -0.0616 99  LYS A CB  
1293 C CG  . LYS A 99  ? 0.5698 0.7666 0.3951 0.0327  0.0526  -0.0140 99  LYS A CG  
1294 C CD  . LYS A 99  ? 0.5975 0.8350 0.3968 0.0615  0.0693  -0.0064 99  LYS A CD  
1295 C CE  . LYS A 99  ? 0.6136 0.9061 0.4639 0.0596  0.0770  0.0516  99  LYS A CE  
1296 N NZ  . LYS A 99  ? 0.6448 0.9981 0.4783 0.0875  0.0943  0.0718  99  LYS A NZ  
1310 N N   . ARG A 100 ? 0.5345 0.5583 0.3273 -0.0290 -0.0022 -0.1134 100 ARG A N   
1311 C CA  . ARG A 100 ? 0.5942 0.5807 0.3661 -0.0518 -0.0296 -0.1374 100 ARG A CA  
1312 C C   . ARG A 100 ? 0.5531 0.5767 0.3596 -0.0783 -0.0445 -0.1119 100 ARG A C   
1313 O O   . ARG A 100 ? 0.6546 0.6702 0.4461 -0.1033 -0.0728 -0.1204 100 ARG A O   
1314 C CB  . ARG A 100 ? 0.6287 0.5542 0.4126 -0.0582 -0.0313 -0.1515 100 ARG A CB  
1315 C CG  . ARG A 100 ? 0.7407 0.6275 0.4943 -0.0297 -0.0175 -0.1745 100 ARG A CG  
1316 C CD  . ARG A 100 ? 0.7794 0.6072 0.5500 -0.0398 -0.0243 -0.1832 100 ARG A CD  
1317 N NE  . ARG A 100 ? 0.8586 0.6603 0.6162 -0.0087 -0.0049 -0.1937 100 ARG A NE  
1318 C CZ  . ARG A 100 ? 0.8971 0.6503 0.6701 -0.0096 -0.0077 -0.1982 100 ARG A CZ  
1319 N NH1 . ARG A 100 ? 0.9271 0.6581 0.7325 -0.0421 -0.0303 -0.1906 100 ARG A NH1 
1320 N NH2 . ARG A 100 ? 0.8919 0.6383 0.6622 0.0221  0.0125  -0.2001 100 ARG A NH2 
1334 N N   . LEU A 101 ? 0.4938 0.5571 0.3477 -0.0721 -0.0273 -0.0790 101 LEU A N   
1335 C CA  . LEU A 101 ? 0.4972 0.6015 0.3906 -0.0868 -0.0350 -0.0506 101 LEU A CA  
1336 C C   . LEU A 101 ? 0.5255 0.6791 0.4018 -0.0968 -0.0529 -0.0388 101 LEU A C   
1337 O O   . LEU A 101 ? 0.5718 0.7650 0.4757 -0.1130 -0.0654 -0.0143 101 LEU A O   
1338 C CB  . LEU A 101 ? 0.4565 0.5798 0.3977 -0.0690 -0.0123 -0.0243 101 LEU A CB  
1339 C CG  . LEU A 101 ? 0.4449 0.5299 0.4043 -0.0619 0.0033  -0.0331 101 LEU A CG  
1340 C CD1 . LEU A 101 ? 0.3853 0.4788 0.3810 -0.0444 0.0193  -0.0135 101 LEU A CD1 
1341 C CD2 . LEU A 101 ? 0.4139 0.4934 0.3869 -0.0786 -0.0054 -0.0365 101 LEU A CD2 
1353 N N   . ALA A 102 ? 0.5759 0.7382 0.4068 -0.0856 -0.0535 -0.0526 102 ALA A N   
1354 C CA  . ALA A 102 ? 0.5297 0.7462 0.3354 -0.0956 -0.0720 -0.0435 102 ALA A CA  
1355 C C   . ALA A 102 ? 0.5664 0.7610 0.3411 -0.1289 -0.1078 -0.0649 102 ALA A C   
1356 O O   . ALA A 102 ? 0.5868 0.8324 0.3723 -0.1519 -0.1284 -0.0409 102 ALA A O   
1357 C CB  . ALA A 102 ? 0.6153 0.8517 0.3706 -0.0728 -0.0638 -0.0573 102 ALA A CB  
1363 N N   . GLN A 103 ? 0.6117 0.7300 0.3522 -0.1331 -0.1178 -0.1058 103 GLN A N   
1364 C CA  . GLN A 103 ? 0.7524 0.8303 0.4631 -0.1688 -0.1588 -0.1284 103 GLN A CA  
1365 C C   . GLN A 103 ? 0.7098 0.7627 0.4734 -0.1928 -0.1668 -0.1109 103 GLN A C   
1366 O O   . GLN A 103 ? 0.7898 0.8366 0.5621 -0.2269 -0.2000 -0.1030 103 GLN A O   
1367 C CB  . GLN A 103 ? 0.9099 0.9109 0.5516 -0.1511 -0.1684 -0.1841 103 GLN A CB  
1368 C CG  . GLN A 103 ? 1.0325 1.0653 0.6167 -0.1208 -0.1604 -0.2004 103 GLN A CG  
1369 C CD  . GLN A 103 ? 1.1709 1.2687 0.7490 -0.1416 -0.1826 -0.1795 103 GLN A CD  
1370 O OE1 . GLN A 103 ? 1.1677 1.3505 0.7541 -0.1324 -0.1657 -0.1491 103 GLN A OE1 
1371 N NE2 . GLN A 103 ? 1.2730 1.3385 0.8462 -0.1693 -0.2206 -0.1911 103 GLN A NE2 
1380 N N   . ALA A 104 ? 0.6204 0.6653 0.4251 -0.1712 -0.1345 -0.0998 104 ALA A N   
1381 C CA  . ALA A 104 ? 0.6640 0.7013 0.5188 -0.1878 -0.1363 -0.0801 104 ALA A CA  
1382 C C   . ALA A 104 ? 0.5910 0.6829 0.5011 -0.1667 -0.1029 -0.0460 104 ALA A C   
1383 O O   . ALA A 104 ? 0.6040 0.6739 0.5306 -0.1480 -0.0787 -0.0504 104 ALA A O   
1384 C CB  . ALA A 104 ? 0.7493 0.7093 0.5901 -0.1822 -0.1342 -0.1089 104 ALA A CB  
1390 N N   . PRO A 105 ? 0.5246 0.6863 0.4623 -0.1685 -0.1031 -0.0124 105 PRO A N   
1391 C CA  . PRO A 105 ? 0.4546 0.6565 0.4372 -0.1397 -0.0721 0.0137  105 PRO A CA  
1392 C C   . PRO A 105 ? 0.4540 0.6699 0.4795 -0.1368 -0.0608 0.0295  105 PRO A C   
1393 O O   . PRO A 105 ? 0.3927 0.6178 0.4433 -0.1076 -0.0341 0.0363  105 PRO A O   
1394 C CB  . PRO A 105 ? 0.4082 0.6816 0.4088 -0.1432 -0.0806 0.0481  105 PRO A CB  
1395 C CG  . PRO A 105 ? 0.4647 0.7373 0.4210 -0.1760 -0.1162 0.0360  105 PRO A CG  
1396 C CD  . PRO A 105 ? 0.5085 0.7143 0.4391 -0.1978 -0.1349 0.0050  105 PRO A CD  
1404 N N   . THR A 106 ? 0.4654 0.6849 0.4986 -0.1667 -0.0830 0.0366  106 THR A N   
1405 C CA  . THR A 106 ? 0.4026 0.6579 0.4780 -0.1642 -0.0727 0.0594  106 THR A CA  
1406 C C   . THR A 106 ? 0.3930 0.5965 0.4611 -0.1574 -0.0595 0.0357  106 THR A C   
1407 O O   . THR A 106 ? 0.3849 0.6204 0.4822 -0.1558 -0.0511 0.0524  106 THR A O   
1408 C CB  . THR A 106 ? 0.4043 0.7096 0.5049 -0.2036 -0.1050 0.0942  106 THR A CB  
1409 O OG1 . THR A 106 ? 0.4994 0.7423 0.5662 -0.2413 -0.1415 0.0731  106 THR A OG1 
1410 C CG2 . THR A 106 ? 0.3379 0.7214 0.4607 -0.2056 -0.1121 0.1309  106 THR A CG2 
1418 N N   . LEU A 107 ? 0.3235 0.4580 0.3534 -0.1516 -0.0568 0.0010  107 LEU A N   
1419 C CA  . LEU A 107 ? 0.3675 0.4586 0.3926 -0.1426 -0.0425 -0.0171 107 LEU A CA  
1420 C C   . LEU A 107 ? 0.4256 0.5409 0.4711 -0.1136 -0.0117 -0.0126 107 LEU A C   
1421 O O   . LEU A 107 ? 0.4240 0.5400 0.4808 -0.1118 -0.0021 -0.0126 107 LEU A O   
1422 C CB  . LEU A 107 ? 0.3850 0.4121 0.3672 -0.1335 -0.0410 -0.0497 107 LEU A CB  
1423 C CG  . LEU A 107 ? 0.5051 0.4857 0.4523 -0.1541 -0.0711 -0.0692 107 LEU A CG  
1424 C CD1 . LEU A 107 ? 0.5171 0.4574 0.4181 -0.1304 -0.0612 -0.0998 107 LEU A CD1 
1425 C CD2 . LEU A 107 ? 0.5477 0.4920 0.5076 -0.1757 -0.0884 -0.0683 107 LEU A CD2 
1437 N N   . LYS A 108 ? 0.4186 0.5516 0.4678 -0.0915 0.0012  -0.0087 108 LYS A N   
1438 C CA  . LYS A 108 ? 0.3447 0.4841 0.4083 -0.0624 0.0252  -0.0102 108 LYS A CA  
1439 C C   . LYS A 108 ? 0.2674 0.4633 0.3590 -0.0538 0.0328  0.0072  108 LYS A C   
1440 O O   . LYS A 108 ? 0.3244 0.5213 0.4192 -0.0288 0.0513  -0.0022 108 LYS A O   
1441 C CB  . LYS A 108 ? 0.4346 0.5753 0.5028 -0.0417 0.0318  -0.0042 108 LYS A CB  
1442 C CG  . LYS A 108 ? 0.5203 0.7154 0.6075 -0.0442 0.0219  0.0232  108 LYS A CG  
1443 C CD  . LYS A 108 ? 0.6279 0.8361 0.7382 -0.0138 0.0343  0.0377  108 LYS A CD  
1444 C CE  . LYS A 108 ? 0.7647 0.9968 0.9001 0.0167  0.0516  0.0422  108 LYS A CE  
1445 N NZ  . LYS A 108 ? 0.8032 1.1126 0.9615 0.0110  0.0474  0.0702  108 LYS A NZ  
1459 N N   . ASP A 109 ? 0.3251 0.5720 0.4351 -0.0745 0.0167  0.0334  109 ASP A N   
1460 C CA  . ASP A 109 ? 0.3175 0.6409 0.4588 -0.0655 0.0243  0.0603  109 ASP A CA  
1461 C C   . ASP A 109 ? 0.2908 0.6217 0.4350 -0.0793 0.0242  0.0606  109 ASP A C   
1462 O O   . ASP A 109 ? 0.2141 0.6186 0.3820 -0.0704 0.0328  0.0840  109 ASP A O   
1463 C CB  . ASP A 109 ? 0.3616 0.7522 0.5298 -0.0866 0.0039  0.1004  109 ASP A CB  
1464 C CG  . ASP A 109 ? 0.3993 0.8029 0.5719 -0.0703 0.0059  0.1092  109 ASP A CG  
1465 O OD1 . ASP A 109 ? 0.4333 0.8291 0.6084 -0.0293 0.0302  0.0991  109 ASP A OD1 
1466 O OD2 . ASP A 109 ? 0.3412 0.7605 0.5147 -0.0997 -0.0196 0.1269  109 ASP A OD2 
1471 N N   . ILE A 110 ? 0.2879 0.5875 0.4943 -0.0697 0.0269  0.0293  110 ILE A N   
1472 C CA  . ILE A 110 ? 0.2721 0.5485 0.4573 -0.0811 0.0433  0.0299  110 ILE A CA  
1473 C C   . ILE A 110 ? 0.2677 0.5342 0.4364 -0.0576 0.0650  0.0266  110 ILE A C   
1474 O O   . ILE A 110 ? 0.3215 0.5626 0.4685 -0.0382 0.0617  0.0194  110 ILE A O   
1475 C CB  . ILE A 110 ? 0.3273 0.5478 0.4704 -0.0943 0.0314  0.0232  110 ILE A CB  
1476 C CG1 . ILE A 110 ? 0.3487 0.5721 0.5019 -0.1197 0.0104  0.0245  110 ILE A CG1 
1477 C CG2 . ILE A 110 ? 0.3289 0.5203 0.4468 -0.1009 0.0467  0.0249  110 ILE A CG2 
1478 C CD1 . ILE A 110 ? 0.3928 0.5600 0.5043 -0.1288 -0.0021 0.0150  110 ILE A CD1 
1490 N N   . PRO A 111 ? 0.2762 0.5609 0.4521 -0.0608 0.0869  0.0322  111 PRO A N   
1491 C CA  . PRO A 111 ? 0.3580 0.6309 0.5127 -0.0389 0.1072  0.0274  111 PRO A CA  
1492 C C   . PRO A 111 ? 0.3625 0.5757 0.4664 -0.0348 0.1031  0.0197  111 PRO A C   
1493 O O   . PRO A 111 ? 0.4023 0.5855 0.4862 -0.0519 0.0935  0.0206  111 PRO A O   
1494 C CB  . PRO A 111 ? 0.3109 0.6093 0.4741 -0.0511 0.1301  0.0360  111 PRO A CB  
1495 C CG  . PRO A 111 ? 0.3340 0.6774 0.5417 -0.0737 0.1235  0.0467  111 PRO A CG  
1496 C CD  . PRO A 111 ? 0.3112 0.6281 0.5126 -0.0860 0.0943  0.0436  111 PRO A CD  
1504 N N   . GLY A 112 ? 0.3729 0.5691 0.4579 -0.0118 0.1095  0.0123  112 GLY A N   
1505 C CA  . GLY A 112 ? 0.3754 0.5218 0.4165 -0.0085 0.1067  0.0063  112 GLY A CA  
1506 C C   . GLY A 112 ? 0.3451 0.4645 0.3744 -0.0070 0.0869  0.0017  112 GLY A C   
1507 O O   . GLY A 112 ? 0.3577 0.4413 0.3566 -0.0050 0.0834  -0.0024 112 GLY A O   
1511 N N   . THR A 113 ? 0.3669 0.5056 0.4200 -0.0085 0.0738  0.0029  113 THR A N   
1512 C CA  . THR A 113 ? 0.3822 0.4979 0.4212 -0.0101 0.0565  -0.0007 113 THR A CA  
1513 C C   . THR A 113 ? 0.3558 0.4703 0.3955 0.0076  0.0498  -0.0025 113 THR A C   
1514 O O   . THR A 113 ? 0.3765 0.5144 0.4376 0.0213  0.0538  -0.0006 113 THR A O   
1515 C CB  . THR A 113 ? 0.3557 0.4834 0.4088 -0.0275 0.0427  0.0013  113 THR A CB  
1516 O OG1 . THR A 113 ? 0.3335 0.5005 0.4207 -0.0244 0.0369  0.0059  113 THR A OG1 
1517 C CG2 . THR A 113 ? 0.3347 0.4596 0.3878 -0.0469 0.0473  0.0046  113 THR A CG2 
1525 N N   . LEU A 114 ? 0.3700 0.4568 0.3866 0.0074  0.0399  -0.0055 114 LEU A N   
1526 C CA  . LEU A 114 ? 0.3722 0.4521 0.3843 0.0192  0.0307  -0.0047 114 LEU A CA  
1527 C C   . LEU A 114 ? 0.3934 0.4589 0.3884 0.0092  0.0184  -0.0056 114 LEU A C   
1528 O O   . LEU A 114 ? 0.4198 0.4613 0.3924 0.0060  0.0204  -0.0087 114 LEU A O   
1529 C CB  . LEU A 114 ? 0.3317 0.3855 0.3242 0.0319  0.0375  -0.0073 114 LEU A CB  
1530 C CG  . LEU A 114 ? 0.2881 0.3242 0.2695 0.0415  0.0274  -0.0050 114 LEU A CG  
1531 C CD1 . LEU A 114 ? 0.3090 0.3669 0.3139 0.0531  0.0195  0.0000  114 LEU A CD1 
1532 C CD2 . LEU A 114 ? 0.3700 0.3764 0.3310 0.0509  0.0334  -0.0085 114 LEU A CD2 
1544 N N   . PHE A 115 ? 0.3712 0.4537 0.3771 0.0043  0.0058  -0.0030 115 PHE A N   
1545 C CA  . PHE A 115 ? 0.3769 0.4468 0.3624 -0.0058 -0.0047 -0.0055 115 PHE A CA  
1546 C C   . PHE A 115 ? 0.3740 0.4286 0.3399 0.0016  -0.0104 -0.0021 115 PHE A C   
1547 O O   . PHE A 115 ? 0.3901 0.4517 0.3549 0.0026  -0.0235 0.0030  115 PHE A O   
1548 C CB  . PHE A 115 ? 0.3805 0.4712 0.3795 -0.0168 -0.0181 -0.0046 115 PHE A CB  
1549 C CG  . PHE A 115 ? 0.3927 0.4886 0.4019 -0.0311 -0.0146 -0.0081 115 PHE A CG  
1550 C CD1 . PHE A 115 ? 0.3637 0.4795 0.3989 -0.0308 -0.0041 -0.0042 115 PHE A CD1 
1551 C CD2 . PHE A 115 ? 0.3830 0.4608 0.3728 -0.0450 -0.0211 -0.0151 115 PHE A CD2 
1552 C CE1 . PHE A 115 ? 0.3650 0.4830 0.4074 -0.0469 -0.0012 -0.0048 115 PHE A CE1 
1553 C CE2 . PHE A 115 ? 0.3646 0.4397 0.3611 -0.0592 -0.0198 -0.0174 115 PHE A CE2 
1554 C CZ  . PHE A 115 ? 0.3623 0.4576 0.3854 -0.0616 -0.0104 -0.0109 115 PHE A CZ  
1564 N N   . LEU A 116 ? 0.3822 0.4156 0.3321 0.0052  -0.0016 -0.0034 116 LEU A N   
1565 C CA  . LEU A 116 ? 0.4105 0.4272 0.3427 0.0096  -0.0052 0.0018  116 LEU A CA  
1566 C C   . LEU A 116 ? 0.4536 0.4535 0.3681 0.0040  0.0030  -0.0015 116 LEU A C   
1567 O O   . LEU A 116 ? 0.5138 0.5095 0.4325 0.0041  0.0115  -0.0058 116 LEU A O   
1568 C CB  . LEU A 116 ? 0.3576 0.3687 0.2987 0.0238  -0.0047 0.0061  116 LEU A CB  
1569 C CG  . LEU A 116 ? 0.3716 0.3585 0.2943 0.0280  -0.0105 0.0131  116 LEU A CG  
1570 C CD1 . LEU A 116 ? 0.4675 0.4579 0.3826 0.0261  -0.0248 0.0217  116 LEU A CD1 
1571 C CD2 . LEU A 116 ? 0.3910 0.3652 0.3204 0.0437  -0.0086 0.0135  116 LEU A CD2 
1583 N N   . ALA A 117 ? 0.3882 0.3812 0.2838 -0.0012 0.0002  0.0016  117 ALA A N   
1584 C CA  . ALA A 117 ? 0.4097 0.3955 0.2943 -0.0066 0.0085  -0.0004 117 ALA A CA  
1585 C C   . ALA A 117 ? 0.4272 0.4016 0.3166 -0.0039 0.0130  0.0010  117 ALA A C   
1586 O O   . ALA A 117 ? 0.4195 0.3825 0.3089 0.0016  0.0090  0.0056  117 ALA A O   
1587 C CB  . ALA A 117 ? 0.3844 0.3675 0.2488 -0.0124 0.0065  0.0060  117 ALA A CB  
1593 N N   . GLY A 118 ? 0.4163 0.3914 0.3082 -0.0069 0.0199  -0.0036 118 GLY A N   
1594 C CA  . GLY A 118 ? 0.3850 0.3496 0.2787 -0.0067 0.0216  -0.0025 118 GLY A CA  
1595 C C   . GLY A 118 ? 0.4391 0.4059 0.3403 -0.0059 0.0261  -0.0085 118 GLY A C   
1596 O O   . GLY A 118 ? 0.4286 0.3881 0.3294 -0.0072 0.0258  -0.0076 118 GLY A O   
1600 N N   . GLY A 119 ? 0.4621 0.4363 0.3683 -0.0051 0.0280  -0.0136 119 GLY A N   
1601 C CA  . GLY A 119 ? 0.4540 0.4256 0.3650 -0.0050 0.0308  -0.0175 119 GLY A CA  
1602 C C   . GLY A 119 ? 0.4356 0.4101 0.3471 -0.0056 0.0327  -0.0228 119 GLY A C   
1603 O O   . GLY A 119 ? 0.4564 0.4352 0.3631 -0.0070 0.0321  -0.0264 119 GLY A O   
1607 N N   . THR A 120 ? 0.3723 0.3428 0.2878 -0.0034 0.0339  -0.0236 120 THR A N   
1608 C CA  . THR A 120 ? 0.4028 0.3731 0.3201 0.0004  0.0365  -0.0300 120 THR A CA  
1609 C C   . THR A 120 ? 0.4038 0.3611 0.3254 0.0034  0.0341  -0.0301 120 THR A C   
1610 O O   . THR A 120 ? 0.4206 0.3746 0.3442 0.0028  0.0311  -0.0239 120 THR A O   
1611 C CB  . THR A 120 ? 0.4051 0.3904 0.3272 0.0034  0.0411  -0.0293 120 THR A CB  
1612 O OG1 . THR A 120 ? 0.4912 0.4770 0.4143 0.0109  0.0462  -0.0379 120 THR A OG1 
1613 C CG2 . THR A 120 ? 0.4051 0.3954 0.3385 0.0030  0.0382  -0.0219 120 THR A CG2 
1621 N N   . PRO A 121 ? 0.4452 0.3904 0.3643 0.0062  0.0340  -0.0370 121 PRO A N   
1622 C CA  . PRO A 121 ? 0.4788 0.4051 0.3989 0.0083  0.0299  -0.0354 121 PRO A CA  
1623 C C   . PRO A 121 ? 0.4709 0.3979 0.4014 0.0199  0.0288  -0.0350 121 PRO A C   
1624 O O   . PRO A 121 ? 0.4638 0.4075 0.4026 0.0274  0.0341  -0.0392 121 PRO A O   
1625 C CB  . PRO A 121 ? 0.5299 0.4380 0.4412 0.0053  0.0283  -0.0433 121 PRO A CB  
1626 C CG  . PRO A 121 ? 0.5616 0.4797 0.4678 0.0084  0.0327  -0.0525 121 PRO A CG  
1627 C CD  . PRO A 121 ? 0.5075 0.4496 0.4172 0.0054  0.0356  -0.0464 121 PRO A CD  
1635 N N   . VAL A 122 ? 0.4439 0.3547 0.3745 0.0212  0.0220  -0.0288 122 VAL A N   
1636 C CA  . VAL A 122 ? 0.4211 0.3297 0.3640 0.0339  0.0173  -0.0270 122 VAL A CA  
1637 C C   . VAL A 122 ? 0.4364 0.3107 0.3704 0.0369  0.0114  -0.0278 122 VAL A C   
1638 O O   . VAL A 122 ? 0.4872 0.3430 0.4068 0.0248  0.0082  -0.0223 122 VAL A O   
1639 C CB  . VAL A 122 ? 0.4642 0.3817 0.4124 0.0317  0.0095  -0.0154 122 VAL A CB  
1640 C CG1 . VAL A 122 ? 0.4731 0.3923 0.4388 0.0455  0.0015  -0.0118 122 VAL A CG1 
1641 C CG2 . VAL A 122 ? 0.5108 0.4548 0.4646 0.0258  0.0133  -0.0141 122 VAL A CG2 
1651 N N   . THR A 123 ? 0.4013 0.2667 0.3440 0.0531  0.0105  -0.0341 123 THR A N   
1652 C CA  . THR A 123 ? 0.4240 0.2487 0.3558 0.0571  0.0038  -0.0363 123 THR A CA  
1653 C C   . THR A 123 ? 0.4910 0.3024 0.4334 0.0720  -0.0070 -0.0284 123 THR A C   
1654 O O   . THR A 123 ? 0.4929 0.3325 0.4569 0.0827  -0.0085 -0.0241 123 THR A O   
1655 C CB  . THR A 123 ? 0.4873 0.2981 0.4128 0.0662  0.0103  -0.0540 123 THR A CB  
1656 O OG1 . THR A 123 ? 0.4752 0.3041 0.4195 0.0888  0.0162  -0.0612 123 THR A OG1 
1657 C CG2 . THR A 123 ? 0.5113 0.3372 0.4260 0.0527  0.0184  -0.0614 123 THR A CG2 
1665 N N   . ALA A 124 ? 0.5620 0.3296 0.4894 0.0712  -0.0162 -0.0251 124 ALA A N   
1666 C CA  . ALA A 124 ? 0.5822 0.3262 0.5165 0.0884  -0.0288 -0.0186 124 ALA A CA  
1667 C C   . ALA A 124 ? 0.6359 0.3276 0.5534 0.0928  -0.0329 -0.0267 124 ALA A C   
1668 O O   . ALA A 124 ? 0.7354 0.3976 0.6298 0.0723  -0.0357 -0.0231 124 ALA A O   
1669 C CB  . ALA A 124 ? 0.6270 0.3633 0.5523 0.0776  -0.0415 0.0015  124 ALA A CB  
1675 N N   . LYS A 125 ? 0.6551 0.3356 0.5849 0.1195  -0.0330 -0.0377 125 LYS A N   
1676 C CA  . LYS A 125 ? 0.7725 0.3980 0.6839 0.1273  -0.0366 -0.0499 125 LYS A CA  
1677 C C   . LYS A 125 ? 0.7621 0.3782 0.6509 0.1082  -0.0279 -0.0642 125 LYS A C   
1678 O O   . LYS A 125 ? 0.8493 0.4171 0.7137 0.0938  -0.0359 -0.0652 125 LYS A O   
1679 C CB  . LYS A 125 ? 0.9220 0.4928 0.8168 0.1219  -0.0555 -0.0337 125 LYS A CB  
1680 C CG  . LYS A 125 ? 1.1091 0.6418 1.0114 0.1537  -0.0659 -0.0374 125 LYS A CG  
1681 C CD  . LYS A 125 ? 1.2347 0.6907 1.1067 0.1452  -0.0823 -0.0306 125 LYS A CD  
1682 C CE  . LYS A 125 ? 1.2365 0.6802 1.0974 0.1258  -0.0971 -0.0020 125 LYS A CE  
1683 N NZ  . LYS A 125 ? 1.2700 0.6532 1.1060 0.1125  -0.1095 0.0072  125 LYS A NZ  
1697 N N   . GLY A 126 ? 0.6918 0.3539 0.5888 0.1066  -0.0132 -0.0738 126 GLY A N   
1698 C CA  . GLY A 126 ? 0.8084 0.4661 0.6851 0.0912  -0.0067 -0.0875 126 GLY A CA  
1699 C C   . GLY A 126 ? 0.7958 0.4554 0.6615 0.0592  -0.0112 -0.0760 126 GLY A C   
1700 O O   . GLY A 126 ? 0.8354 0.4914 0.6864 0.0439  -0.0097 -0.0848 126 GLY A O   
1704 N N   . ALA A 127 ? 0.6929 0.3598 0.5654 0.0494  -0.0167 -0.0562 127 ALA A N   
1705 C CA  . ALA A 127 ? 0.6074 0.2814 0.4726 0.0214  -0.0179 -0.0444 127 ALA A CA  
1706 C C   . ALA A 127 ? 0.5331 0.2560 0.4122 0.0182  -0.0105 -0.0350 127 ALA A C   
1707 O O   . ALA A 127 ? 0.5481 0.2859 0.4391 0.0317  -0.0113 -0.0292 127 ALA A O   
1708 C CB  . ALA A 127 ? 0.6881 0.3219 0.5407 0.0098  -0.0293 -0.0292 127 ALA A CB  
1714 N N   . PRO A 128 ? 0.4828 0.2297 0.3611 0.0005  -0.0048 -0.0335 128 PRO A N   
1715 C CA  . PRO A 128 ? 0.4837 0.2699 0.3716 -0.0016 0.0018  -0.0261 128 PRO A CA  
1716 C C   . PRO A 128 ? 0.5077 0.2878 0.3905 -0.0067 -0.0020 -0.0098 128 PRO A C   
1717 O O   . PRO A 128 ? 0.4988 0.2544 0.3694 -0.0197 -0.0060 -0.0010 128 PRO A O   
1718 C CB  . PRO A 128 ? 0.4597 0.2645 0.3473 -0.0179 0.0069  -0.0279 128 PRO A CB  
1719 C CG  . PRO A 128 ? 0.5054 0.2800 0.3832 -0.0322 0.0005  -0.0282 128 PRO A CG  
1720 C CD  . PRO A 128 ? 0.5393 0.2768 0.4089 -0.0186 -0.0061 -0.0373 128 PRO A CD  
1728 N N   . VAL A 129 ? 0.5216 0.3222 0.4107 0.0016  -0.0016 -0.0053 129 VAL A N   
1729 C CA  . VAL A 129 ? 0.5270 0.3216 0.4051 -0.0032 -0.0064 0.0090  129 VAL A CA  
1730 C C   . VAL A 129 ? 0.4627 0.2861 0.3395 -0.0082 0.0006  0.0107  129 VAL A C   
1731 O O   . VAL A 129 ? 0.4595 0.2790 0.3199 -0.0164 0.0010  0.0201  129 VAL A O   
1732 C CB  . VAL A 129 ? 0.4930 0.2768 0.3759 0.0120  -0.0183 0.0142  129 VAL A CB  
1733 C CG1 . VAL A 129 ? 0.4997 0.2438 0.3775 0.0174  -0.0272 0.0159  129 VAL A CG1 
1734 C CG2 . VAL A 129 ? 0.5186 0.3320 0.4251 0.0273  -0.0163 0.0053  129 VAL A CG2 
1744 N N   . ALA A 130 ? 0.4321 0.2809 0.3225 -0.0031 0.0062  0.0014  130 ALA A N   
1745 C CA  . ALA A 130 ? 0.4232 0.2931 0.3116 -0.0064 0.0114  0.0018  130 ALA A CA  
1746 C C   . ALA A 130 ? 0.4341 0.3252 0.3343 -0.0049 0.0183  -0.0074 130 ALA A C   
1747 O O   . ALA A 130 ? 0.4177 0.3111 0.3271 0.0007  0.0187  -0.0147 130 ALA A O   
1748 C CB  . ALA A 130 ? 0.4341 0.3080 0.3224 -0.0008 0.0035  0.0063  130 ALA A CB  
1754 N N   . GLY A 131 ? 0.4037 0.3075 0.3002 -0.0090 0.0235  -0.0071 131 GLY A N   
1755 C CA  . GLY A 131 ? 0.3924 0.3140 0.2970 -0.0072 0.0274  -0.0127 131 GLY A CA  
1756 C C   . GLY A 131 ? 0.3873 0.3140 0.2882 -0.0056 0.0257  -0.0105 131 GLY A C   
1757 O O   . GLY A 131 ? 0.3991 0.3166 0.2866 -0.0078 0.0247  -0.0067 131 GLY A O   
1761 N N   . ILE A 132 ? 0.3773 0.3161 0.2866 -0.0033 0.0252  -0.0126 132 ILE A N   
1762 C CA  . ILE A 132 ? 0.3659 0.3064 0.2715 -0.0050 0.0219  -0.0100 132 ILE A CA  
1763 C C   . ILE A 132 ? 0.4182 0.3637 0.3222 -0.0056 0.0257  -0.0117 132 ILE A C   
1764 O O   . ILE A 132 ? 0.4477 0.4042 0.3587 -0.0052 0.0281  -0.0135 132 ILE A O   
1765 C CB  . ILE A 132 ? 0.4088 0.3611 0.3277 -0.0045 0.0172  -0.0076 132 ILE A CB  
1766 C CG1 . ILE A 132 ? 0.4222 0.3707 0.3465 -0.0008 0.0109  -0.0048 132 ILE A CG1 
1767 C CG2 . ILE A 132 ? 0.3873 0.3385 0.3017 -0.0108 0.0114  -0.0036 132 ILE A CG2 
1768 C CD1 . ILE A 132 ? 0.4687 0.4374 0.4157 0.0037  0.0084  -0.0032 132 ILE A CD1 
1780 N N   . GLY A 133 ? 0.3970 0.3323 0.2892 -0.0055 0.0259  -0.0114 133 GLY A N   
1781 C CA  . GLY A 133 ? 0.3830 0.3194 0.2741 -0.0030 0.0279  -0.0122 133 GLY A CA  
1782 C C   . GLY A 133 ? 0.4287 0.3514 0.3096 -0.0047 0.0222  -0.0101 133 GLY A C   
1783 O O   . GLY A 133 ? 0.4255 0.3330 0.2939 -0.0070 0.0179  -0.0103 133 GLY A O   
1787 N N   . VAL A 134 ? 0.4213 0.3460 0.3043 -0.0049 0.0206  -0.0076 134 VAL A N   
1788 C CA  . VAL A 134 ? 0.4096 0.3162 0.2817 -0.0084 0.0139  -0.0041 134 VAL A CA  
1789 C C   . VAL A 134 ? 0.4233 0.3223 0.2919 -0.0010 0.0134  -0.0031 134 VAL A C   
1790 O O   . VAL A 134 ? 0.4385 0.3542 0.3168 0.0023  0.0159  -0.0021 134 VAL A O   
1791 C CB  . VAL A 134 ? 0.4532 0.3697 0.3320 -0.0197 0.0100  0.0026  134 VAL A CB  
1792 C CG1 . VAL A 134 ? 0.4797 0.3741 0.3463 -0.0278 0.0013  0.0082  134 VAL A CG1 
1793 C CG2 . VAL A 134 ? 0.4382 0.3675 0.3272 -0.0238 0.0094  0.0023  134 VAL A CG2 
1803 N N   . ALA A 135 ? 0.4395 0.3109 0.2930 0.0020  0.0084  -0.0035 135 ALA A N   
1804 C CA  . ALA A 135 ? 0.4604 0.3195 0.3107 0.0121  0.0058  -0.0018 135 ALA A CA  
1805 C C   . ALA A 135 ? 0.4936 0.3142 0.3236 0.0090  -0.0037 0.0003  135 ALA A C   
1806 O O   . ALA A 135 ? 0.4931 0.2938 0.3088 0.0039  -0.0066 -0.0042 135 ALA A O   
1807 C CB  . ALA A 135 ? 0.5667 0.4319 0.4229 0.0284  0.0138  -0.0091 135 ALA A CB  
1813 N N   . GLY A 136 ? 0.5062 0.3128 0.3323 0.0109  -0.0108 0.0079  136 GLY A N   
1814 C CA  . GLY A 136 ? 0.5161 0.2786 0.3208 0.0076  -0.0218 0.0109  136 GLY A CA  
1815 C C   . GLY A 136 ? 0.5109 0.2669 0.3115 -0.0077 -0.0308 0.0261  136 GLY A C   
1816 O O   . GLY A 136 ? 0.6107 0.3276 0.3943 -0.0077 -0.0414 0.0318  136 GLY A O   
1820 N N   . ALA A 137 ? 0.4766 0.2682 0.2903 -0.0207 -0.0259 0.0327  137 ALA A N   
1821 C CA  . ALA A 137 ? 0.5373 0.3288 0.3455 -0.0369 -0.0308 0.0480  137 ALA A CA  
1822 C C   . ALA A 137 ? 0.5407 0.3263 0.3432 -0.0264 -0.0352 0.0553  137 ALA A C   
1823 O O   . ALA A 137 ? 0.5975 0.3925 0.4090 -0.0075 -0.0331 0.0479  137 ALA A O   
1824 C CB  . ALA A 137 ? 0.4669 0.3008 0.2899 -0.0497 -0.0211 0.0506  137 ALA A CB  
1830 N N   . PRO A 138 ? 0.5994 0.3709 0.3874 -0.0397 -0.0425 0.0713  138 PRO A N   
1831 C CA  . PRO A 138 ? 0.5886 0.3503 0.3669 -0.0310 -0.0506 0.0813  138 PRO A CA  
1832 C C   . PRO A 138 ? 0.6098 0.4117 0.4002 -0.0220 -0.0445 0.0774  138 PRO A C   
1833 O O   . PRO A 138 ? 0.6755 0.4730 0.4627 -0.0105 -0.0534 0.0828  138 PRO A O   
1834 C CB  . PRO A 138 ? 0.6344 0.3834 0.3935 -0.0544 -0.0557 0.1008  138 PRO A CB  
1835 C CG  . PRO A 138 ? 0.6644 0.3954 0.4220 -0.0708 -0.0568 0.1007  138 PRO A CG  
1836 C CD  . PRO A 138 ? 0.6046 0.3648 0.3835 -0.0648 -0.0458 0.0830  138 PRO A CD  
1844 N N   . SER A 139 ? 0.5290 0.3670 0.3329 -0.0271 -0.0315 0.0682  139 SER A N   
1845 C CA  . SER A 139 ? 0.4795 0.3503 0.2920 -0.0210 -0.0267 0.0625  139 SER A CA  
1846 C C   . SER A 139 ? 0.4916 0.3880 0.3224 -0.0194 -0.0144 0.0478  139 SER A C   
1847 O O   . SER A 139 ? 0.5299 0.4258 0.3651 -0.0267 -0.0087 0.0448  139 SER A O   
1848 C CB  . SER A 139 ? 0.5293 0.4129 0.3242 -0.0346 -0.0254 0.0729  139 SER A CB  
1849 O OG  . SER A 139 ? 0.6448 0.5406 0.4388 -0.0506 -0.0141 0.0745  139 SER A OG  
1855 N N   . GLY A 140 ? 0.5039 0.4866 0.3507 -0.0790 -0.0207 0.0803  140 GLY A N   
1856 C CA  . GLY A 140 ? 0.5146 0.4978 0.3326 -0.0783 -0.0264 0.0648  140 GLY A CA  
1857 C C   . GLY A 140 ? 0.5554 0.5056 0.3398 -0.0762 -0.0079 0.0533  140 GLY A C   
1858 O O   . GLY A 140 ? 0.5971 0.5496 0.3864 -0.0696 -0.0074 0.0351  140 GLY A O   
1862 N N   . ASP A 141 ? 0.5723 0.4987 0.3209 -0.0767 0.0087  0.0667  141 ASP A N   
1863 C CA  . ASP A 141 ? 0.6160 0.5224 0.3264 -0.0609 0.0327  0.0581  141 ASP A CA  
1864 C C   . ASP A 141 ? 0.5513 0.4910 0.3384 -0.0499 0.0550  0.0538  141 ASP A C   
1865 O O   . ASP A 141 ? 0.6134 0.5493 0.3915 -0.0350 0.0688  0.0403  141 ASP A O   
1866 C CB  . ASP A 141 ? 0.7391 0.6338 0.3943 -0.0547 0.0501  0.0794  141 ASP A CB  
1867 C CG  . ASP A 141 ? 0.9161 0.7620 0.4756 -0.0631 0.0211  0.0781  141 ASP A CG  
1868 O OD1 . ASP A 141 ? 0.8845 0.6979 0.4189 -0.0663 -0.0091 0.0574  141 ASP A OD1 
1869 O OD2 . ASP A 141 ? 1.0196 0.8715 0.5601 -0.0642 0.0228  0.0986  141 ASP A OD2 
1874 N N   . LEU A 142 ? 0.4519 0.4191 0.3174 -0.0573 0.0522  0.0666  142 LEU A N   
1875 C CA  . LEU A 142 ? 0.4231 0.4148 0.3711 -0.0534 0.0580  0.0658  142 LEU A CA  
1876 C C   . LEU A 142 ? 0.4337 0.4295 0.4003 -0.0494 0.0390  0.0319  142 LEU A C   
1877 O O   . LEU A 142 ? 0.4792 0.4875 0.4800 -0.0437 0.0464  0.0249  142 LEU A O   
1878 C CB  . LEU A 142 ? 0.3836 0.3865 0.4105 -0.0638 0.0446  0.0885  142 LEU A CB  
1879 C CG  . LEU A 142 ? 0.4851 0.5036 0.5175 -0.0699 0.0647  0.1369  142 LEU A CG  
1880 C CD1 . LEU A 142 ? 0.4846 0.5047 0.6040 -0.0848 0.0380  0.1612  142 LEU A CD1 
1881 C CD2 . LEU A 142 ? 0.5113 0.5655 0.5583 -0.0589 0.0996  0.1654  142 LEU A CD2 
1893 N N   . ASP A 143 ? 0.4449 0.4416 0.3924 -0.0505 0.0156  0.0176  143 ASP A N   
1894 C CA  . ASP A 143 ? 0.3961 0.4136 0.3491 -0.0428 0.0001  -0.0063 143 ASP A CA  
1895 C C   . ASP A 143 ? 0.4244 0.4326 0.3441 -0.0432 0.0106  -0.0104 143 ASP A C   
1896 O O   . ASP A 143 ? 0.4084 0.4345 0.3570 -0.0374 0.0090  -0.0242 143 ASP A O   
1897 C CB  . ASP A 143 ? 0.4047 0.4433 0.3326 -0.0409 -0.0201 -0.0036 143 ASP A CB  
1898 C CG  . ASP A 143 ? 0.4276 0.4800 0.3903 -0.0269 -0.0338 -0.0086 143 ASP A CG  
1899 O OD1 . ASP A 143 ? 0.4575 0.5033 0.4689 -0.0157 -0.0418 -0.0279 143 ASP A OD1 
1900 O OD2 . ASP A 143 ? 0.3902 0.4565 0.3333 -0.0257 -0.0418 0.0077  143 ASP A OD2 
1905 N N   . GLU A 144 ? 0.4594 0.4335 0.3149 -0.0476 0.0165  -0.0002 144 GLU A N   
1906 C CA  . GLU A 144 ? 0.4960 0.4432 0.3090 -0.0427 0.0158  -0.0089 144 GLU A CA  
1907 C C   . GLU A 144 ? 0.4881 0.4371 0.3220 -0.0248 0.0463  -0.0135 144 GLU A C   
1908 O O   . GLU A 144 ? 0.5753 0.5218 0.4135 -0.0169 0.0452  -0.0248 144 GLU A O   
1909 C CB  . GLU A 144 ? 0.5561 0.4503 0.2842 -0.0471 0.0021  -0.0032 144 GLU A CB  
1910 C CG  . GLU A 144 ? 0.5600 0.4192 0.2517 -0.0524 -0.0308 -0.0098 144 GLU A CG  
1911 C CD  . GLU A 144 ? 0.6767 0.4763 0.2914 -0.0647 -0.0657 -0.0019 144 GLU A CD  
1912 O OE1 . GLU A 144 ? 0.6771 0.4984 0.3068 -0.0888 -0.0940 0.0226  144 GLU A OE1 
1913 O OE2 . GLU A 144 ? 0.8059 0.5393 0.3455 -0.0463 -0.0668 -0.0194 144 GLU A OE2 
1920 N N   . GLN A 145 ? 0.4382 0.4007 0.2942 -0.0187 0.0723  0.0036  145 GLN A N   
1921 C CA  . GLN A 145 ? 0.4831 0.4707 0.3785 -0.0017 0.1033  0.0155  145 GLN A CA  
1922 C C   . GLN A 145 ? 0.4646 0.4806 0.4356 -0.0077 0.0922  0.0060  145 GLN A C   
1923 O O   . GLN A 145 ? 0.5194 0.5457 0.5047 0.0064  0.1068  0.0054  145 GLN A O   
1924 C CB  . GLN A 145 ? 0.5065 0.5254 0.4446 -0.0036 0.1236  0.0523  145 GLN A CB  
1925 C CG  . GLN A 145 ? 0.5614 0.6285 0.5626 0.0108  0.1543  0.0837  145 GLN A CG  
1926 C CD  . GLN A 145 ? 0.6080 0.7190 0.6686 0.0032  0.1680  0.1367  145 GLN A CD  
1927 O OE1 . GLN A 145 ? 0.5888 0.7427 0.7514 -0.0076 0.1664  0.1713  145 GLN A OE1 
1928 N NE2 . GLN A 145 ? 0.6222 0.7246 0.6253 0.0056  0.1762  0.1498  145 GLN A NE2 
1937 N N   . TYR A 146 ? 0.4069 0.4354 0.4212 -0.0236 0.0645  -0.0030 146 TYR A N   
1938 C CA  . TYR A 146 ? 0.3571 0.4103 0.4316 -0.0262 0.0462  -0.0170 146 TYR A CA  
1939 C C   . TYR A 146 ? 0.3603 0.4176 0.4043 -0.0228 0.0349  -0.0359 146 TYR A C   
1940 O O   . TYR A 146 ? 0.3938 0.4729 0.4754 -0.0206 0.0313  -0.0411 146 TYR A O   
1941 C CB  . TYR A 146 ? 0.3420 0.3996 0.4541 -0.0322 0.0152  -0.0284 146 TYR A CB  
1942 C CG  . TYR A 146 ? 0.3216 0.3711 0.4816 -0.0407 0.0153  -0.0031 146 TYR A CG  
1943 C CD1 . TYR A 146 ? 0.3342 0.4014 0.5528 -0.0459 0.0319  0.0311  146 TYR A CD1 
1944 C CD2 . TYR A 146 ? 0.2940 0.3266 0.4494 -0.0433 -0.0021 -0.0042 146 TYR A CD2 
1945 C CE1 . TYR A 146 ? 0.3435 0.4152 0.6204 -0.0581 0.0277  0.0689  146 TYR A CE1 
1946 C CE2 . TYR A 146 ? 0.3235 0.3489 0.5332 -0.0545 -0.0077 0.0262  146 TYR A CE2 
1947 C CZ  . TYR A 146 ? 0.3697 0.4164 0.6426 -0.0642 0.0057  0.0655  146 TYR A CZ  
1948 O OH  . TYR A 146 ? 0.4817 0.5330 0.8233 -0.0797 -0.0040 0.1102  146 TYR A OH  
1958 N N   . ALA A 147 ? 0.3730 0.4130 0.3568 -0.0259 0.0245  -0.0385 147 ALA A N   
1959 C CA  . ALA A 147 ? 0.4241 0.4701 0.3883 -0.0281 0.0071  -0.0423 147 ALA A CA  
1960 C C   . ALA A 147 ? 0.4301 0.4460 0.3788 -0.0178 0.0215  -0.0428 147 ALA A C   
1961 O O   . ALA A 147 ? 0.4511 0.4811 0.4203 -0.0175 0.0108  -0.0446 147 ALA A O   
1962 C CB  . ALA A 147 ? 0.4612 0.4953 0.3763 -0.0389 -0.0148 -0.0319 147 ALA A CB  
1968 N N   A ARG A 148 ? 0.4244 0.4036 0.3350 -0.0040 0.0458  -0.0399 148 ARG A N   
1969 N N   B ARG A 148 ? 0.4333 0.4125 0.3440 -0.0040 0.0458  -0.0399 148 ARG A N   
1970 C CA  A ARG A 148 ? 0.4645 0.4161 0.3507 0.0212  0.0645  -0.0439 148 ARG A CA  
1971 C CA  B ARG A 148 ? 0.4739 0.4258 0.3607 0.0212  0.0645  -0.0439 148 ARG A CA  
1972 C C   A ARG A 148 ? 0.4200 0.4197 0.3838 0.0298  0.0868  -0.0346 148 ARG A C   
1973 C C   B ARG A 148 ? 0.4260 0.4260 0.3903 0.0296  0.0865  -0.0346 148 ARG A C   
1974 O O   A ARG A 148 ? 0.4485 0.4446 0.4210 0.0447  0.0902  -0.0380 148 ARG A O   
1975 O O   B ARG A 148 ? 0.4416 0.4383 0.4152 0.0441  0.0895  -0.0381 148 ARG A O   
1976 C CB  A ARG A 148 ? 0.5813 0.4971 0.3985 0.0456  0.0894  -0.0419 148 ARG A CB  
1977 C CB  B ARG A 148 ? 0.5672 0.4845 0.3865 0.0455  0.0900  -0.0415 148 ARG A CB  
1978 C CG  A ARG A 148 ? 0.6542 0.5078 0.3833 0.0388  0.0598  -0.0525 148 ARG A CG  
1979 C CG  B ARG A 148 ? 0.6481 0.5024 0.3787 0.0397  0.0607  -0.0527 148 ARG A CG  
1980 C CD  A ARG A 148 ? 0.7637 0.5676 0.3999 0.0768  0.0779  -0.0621 148 ARG A CD  
1981 C CD  B ARG A 148 ? 0.7483 0.5656 0.3946 0.0732  0.0836  -0.0564 148 ARG A CD  
1982 N NE  A ARG A 148 ? 0.7738 0.6257 0.4216 0.0909  0.1220  -0.0385 148 ARG A NE  
1983 N NE  B ARG A 148 ? 0.7982 0.5590 0.3666 0.0591  0.0489  -0.0628 148 ARG A NE  
1984 C CZ  A ARG A 148 ? 0.7614 0.6214 0.3966 0.0729  0.1204  -0.0227 148 ARG A CZ  
1985 C CZ  B ARG A 148 ? 0.7738 0.5506 0.3326 0.0438  0.0537  -0.0456 148 ARG A CZ  
1986 N NH1 A ARG A 148 ? 0.7182 0.5437 0.3267 0.0423  0.0799  -0.0292 148 ARG A NH1 
1987 N NH1 B ARG A 148 ? 0.7194 0.5617 0.3427 0.0408  0.0890  -0.0211 148 ARG A NH1 
1988 N NH2 A ARG A 148 ? 0.8021 0.7135 0.4607 0.0847  0.1584  0.0084  148 ARG A NH2 
1989 N NH2 B ARG A 148 ? 0.8292 0.5536 0.3191 0.0291  0.0167  -0.0486 148 ARG A NH2 
2016 N N   . ALA A 149 ? 0.3843 0.4252 0.4096 0.0189  0.0956  -0.0196 149 ALA A N   
2017 C CA  . ALA A 149 ? 0.3888 0.4756 0.4995 0.0187  0.1048  -0.0036 149 ALA A CA  
2018 C C   . ALA A 149 ? 0.2952 0.3984 0.4357 0.0068  0.0757  -0.0198 149 ALA A C   
2019 O O   . ALA A 149 ? 0.3651 0.4935 0.5530 0.0119  0.0811  -0.0111 149 ALA A O   
2020 C CB  . ALA A 149 ? 0.3523 0.4645 0.5255 0.0022  0.0997  0.0157  149 ALA A CB  
2026 N N   . GLY A 150 ? 0.3493 0.4489 0.4637 -0.0067 0.0460  -0.0374 150 GLY A N   
2027 C CA  . GLY A 150 ? 0.3039 0.4340 0.4355 -0.0135 0.0195  -0.0464 150 GLY A CA  
2028 C C   . GLY A 150 ? 0.3486 0.4635 0.4619 -0.0075 0.0195  -0.0416 150 GLY A C   
2029 O O   . GLY A 150 ? 0.3349 0.4794 0.4900 -0.0081 0.0128  -0.0371 150 GLY A O   
2033 N N   . ALA A 151 ? 0.3770 0.4392 0.4272 -0.0017 0.0204  -0.0430 151 ALA A N   
2034 C CA  . ALA A 151 ? 0.3121 0.3365 0.3392 0.0068  0.0084  -0.0426 151 ALA A CA  
2035 C C   . ALA A 151 ? 0.3597 0.3775 0.4090 0.0348  0.0388  -0.0420 151 ALA A C   
2036 O O   . ALA A 151 ? 0.3948 0.4022 0.4586 0.0429  0.0277  -0.0403 151 ALA A O   
2037 C CB  . ALA A 151 ? 0.3769 0.3296 0.3237 0.0093  -0.0078 -0.0490 151 ALA A CB  
2043 N N   . ALA A 152 ? 0.3991 0.4314 0.4594 0.0504  0.0761  -0.0359 152 ALA A N   
2044 C CA  . ALA A 152 ? 0.4480 0.4849 0.5217 0.0867  0.1128  -0.0257 152 ALA A CA  
2045 C C   . ALA A 152 ? 0.3827 0.4752 0.5462 0.0829  0.1160  -0.0077 152 ALA A C   
2046 O O   . ALA A 152 ? 0.3882 0.4860 0.5662 0.1159  0.1408  0.0028  152 ALA A O   
2047 C CB  . ALA A 152 ? 0.5376 0.5954 0.6071 0.1031  0.1518  -0.0078 152 ALA A CB  
2053 N N   . VAL A 153 ? 0.3640 0.4992 0.5838 0.0482  0.0901  -0.0045 153 VAL A N   
2054 C CA  . VAL A 153 ? 0.3279 0.5139 0.6286 0.0411  0.0843  0.0118  153 VAL A CA  
2055 C C   . VAL A 153 ? 0.2788 0.4538 0.5741 0.0422  0.0621  0.0064  153 VAL A C   
2056 O O   . VAL A 153 ? 0.3347 0.5444 0.6899 0.0437  0.0614  0.0225  153 VAL A O   
2057 C CB  . VAL A 153 ? 0.2930 0.5226 0.6458 0.0099  0.0562  0.0116  153 VAL A CB  
2058 C CG1 . VAL A 153 ? 0.3113 0.5460 0.6893 0.0050  0.0677  0.0244  153 VAL A CG1 
2059 C CG2 . VAL A 153 ? 0.2958 0.5222 0.6052 -0.0059 0.0220  -0.0124 153 VAL A CG2 
2069 N N   . LEU A 154 ? 0.2691 0.3980 0.5011 0.0379  0.0390  -0.0092 154 LEU A N   
2070 C CA  . LEU A 154 ? 0.3711 0.4812 0.6031 0.0358  0.0092  -0.0054 154 LEU A CA  
2071 C C   . LEU A 154 ? 0.5148 0.5584 0.7147 0.0767  0.0250  -0.0132 154 LEU A C   
2072 O O   . LEU A 154 ? 0.5541 0.5581 0.6990 0.1062  0.0532  -0.0268 154 LEU A O   
2073 C CB  . LEU A 154 ? 0.3386 0.4299 0.5278 0.0120  -0.0302 -0.0068 154 LEU A CB  
2074 C CG  . LEU A 154 ? 0.3226 0.4834 0.5273 -0.0137 -0.0424 -0.0020 154 LEU A CG  
2075 C CD1 . LEU A 154 ? 0.3223 0.4790 0.4919 -0.0322 -0.0770 0.0099  154 LEU A CD1 
2076 C CD2 . LEU A 154 ? 0.2830 0.5235 0.5537 -0.0234 -0.0519 0.0112  154 LEU A CD2 
2088 N N   . GLY A 155 ? 0.6092 0.6423 0.8401 0.0835  0.0052  -0.0046 155 GLY A N   
2089 C CA  . GLY A 155 ? 0.8284 0.7998 1.0339 0.1339  0.0193  -0.0156 155 GLY A CA  
2090 C C   . GLY A 155 ? 0.9387 0.9758 1.2147 0.1584  0.0638  0.0056  155 GLY A C   
2091 O O   . GLY A 155 ? 0.8702 0.9867 1.2250 0.1251  0.0616  0.0300  155 GLY A O   
2095 N N   . HIS A 156 ? 1.1445 1.1558 1.3937 0.2188  0.1020  -0.0001 156 HIS A N   
2096 C CA  . HIS A 156 ? 1.3916 1.3026 1.5313 0.2704  0.1016  -0.0368 156 HIS A CA  
2097 C C   . HIS A 156 ? 1.5256 1.3931 1.6610 0.3330  0.1058  -0.0455 156 HIS A C   
2098 O O   . HIS A 156 ? 1.5111 1.4487 1.7287 0.3481  0.1348  -0.0149 156 HIS A O   
2099 C CB  . HIS A 156 ? 1.4997 1.4325 1.5889 0.3031  0.1545  -0.0381 156 HIS A CB  
2100 C CG  . HIS A 156 ? 1.5242 1.4631 1.5877 0.2550  0.1434  -0.0414 156 HIS A CG  
2101 N ND1 . HIS A 156 ? 1.6059 1.4591 1.5753 0.2482  0.1085  -0.0733 156 HIS A ND1 
2102 C CD2 . HIS A 156 ? 1.4448 1.4605 1.5659 0.2136  0.1578  -0.0160 156 HIS A CD2 
2103 C CE1 . HIS A 156 ? 1.5426 1.4287 1.5153 0.2065  0.1086  -0.0651 156 HIS A CE1 
2104 N NE2 . HIS A 156 ? 1.4524 1.4319 1.5140 0.1869  0.1370  -0.0338 156 HIS A NE2 
2105 O OXT . HIS A 156 ? 1.6502 1.4068 1.6995 0.3725  0.0759  -0.0837 156 HIS A OXT 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   1   ?   ?   ?   A . n 
A 1 2   ALA 2   2   ?   ?   ?   A . n 
A 1 3   MET 3   3   ?   ?   ?   A . n 
A 1 4   ALA 4   4   ?   ?   ?   A . n 
A 1 5   ASP 5   5   ?   ?   ?   A . n 
A 1 6   THR 6   6   ?   ?   ?   A . n 
A 1 7   THR 7   7   ?   ?   ?   A . n 
A 1 8   GLU 8   8   ?   ?   ?   A . n 
A 1 9   ALA 9   9   ?   ?   ?   A . n 
A 1 10  THR 10  10  ?   ?   ?   A . n 
A 1 11  PRO 11  11  11  PRO PRO A . n 
A 1 12  ALA 12  12  12  ALA ALA A . n 
A 1 13  ALA 13  13  13  ALA ALA A . n 
A 1 14  ALA 14  14  14  ALA ALA A . n 
A 1 15  PRO 15  15  15  PRO PRO A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  ALA 17  17  17  ALA ALA A . n 
A 1 18  ALA 18  18  18  ALA ALA A . n 
A 1 19  ARG 19  19  19  ARG ARG A . n 
A 1 20  GLY 20  20  20  GLY GLY A . n 
A 1 21  GLY 21  21  21  GLY GLY A . n 
A 1 22  GLU 22  22  22  GLU GLU A . n 
A 1 23  LEU 23  23  23  LEU LEU A . n 
A 1 24  THR 24  24  24  THR THR A . n 
A 1 25  GLN 25  25  25  GLN GLN A . n 
A 1 26  SER 26  26  26  SER SER A . n 
A 1 27  THR 27  27  27  THR THR A . n 
A 1 28  HIS 28  28  28  HIS HIS A . n 
A 1 29  LEU 29  29  29  LEU LEU A . n 
A 1 30  THR 30  30  30  THR THR A . n 
A 1 31  LEU 31  31  31  LEU LEU A . n 
A 1 32  GLU 32  32  32  GLU GLU A . n 
A 1 33  ALA 33  33  33  ALA ALA A . n 
A 1 34  ALA 34  34  34  ALA ALA A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  LYS 36  36  36  LYS LYS A . n 
A 1 37  ALA 37  37  37  ALA ALA A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  ARG 39  39  39  ARG ARG A . n 
A 1 40  ALA 40  40  40  ALA ALA A . n 
A 1 41  ALA 41  41  41  ALA ALA A . n 
A 1 42  VAL 42  42  42  VAL VAL A . n 
A 1 43  GLU 43  43  43  GLU GLU A . n 
A 1 44  ALA 44  44  44  ALA ALA A . n 
A 1 45  ALA 45  45  45  ALA ALA A . n 
A 1 46  GLU 46  46  46  GLU GLU A . n 
A 1 47  LYS 47  47  47  LYS LYS A . n 
A 1 48  ASP 48  48  48  ASP ASP A . n 
A 1 49  GLY 49  49  49  GLY GLY A . n 
A 1 50  ARG 50  50  50  ARG ARG A . n 
A 1 51  HIS 51  51  51  HIS HIS A . n 
A 1 52  VAL 52  52  52  VAL VAL A . n 
A 1 53  SER 53  53  53  SER SER A . n 
A 1 54  VAL 54  54  54  VAL VAL A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  VAL 56  56  56  VAL VAL A . n 
A 1 57  VAL 57  57  57  VAL VAL A . n 
A 1 58  ASP 58  58  58  ASP ASP A . n 
A 1 59  ARG 59  59  59  ARG ARG A . n 
A 1 60  ASN 60  60  60  ASN ASN A . n 
A 1 61  GLY 61  61  61  GLY GLY A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  THR 63  63  63  THR THR A . n 
A 1 64  LEU 64  64  64  LEU LEU A . n 
A 1 65  VAL 65  65  65  VAL VAL A . n 
A 1 66  THR 66  66  66  THR THR A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  ARG 68  68  68  ARG ARG A . n 
A 1 69  GLY 69  69  69  GLY GLY A . n 
A 1 70  ASP 70  70  70  ASP ASP A . n 
A 1 71  GLY 71  71  71  GLY GLY A . n 
A 1 72  ALA 72  72  72  ALA ALA A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  GLN 75  75  75  GLN GLN A . n 
A 1 76  SER 76  76  76  SER SER A . n 
A 1 77  TYR 77  77  77  TYR TYR A . n 
A 1 78  ASP 78  78  78  ASP ASP A . n 
A 1 79  SER 79  79  79  SER SER A . n 
A 1 80  ALA 80  80  80  ALA ALA A . n 
A 1 81  ASP 81  81  81  ASP ASP A . n 
A 1 82  ARG 82  82  82  ARG ARG A . n 
A 1 83  LYS 83  83  83  LYS LYS A . n 
A 1 84  ALA 84  84  84  ALA ALA A . n 
A 1 85  PHE 85  85  85  PHE PHE A . n 
A 1 86  THR 86  86  86  THR THR A . n 
A 1 87  ALA 87  87  87  ALA ALA A . n 
A 1 88  VAL 88  88  88  VAL VAL A . n 
A 1 89  SER 89  89  89  SER SER A . n 
A 1 90  TRP 90  90  90  TRP TRP A . n 
A 1 91  ASN 91  91  91  ASN ASN A . n 
A 1 92  ALA 92  92  92  ALA ALA A . n 
A 1 93  PRO 93  93  93  PRO PRO A . n 
A 1 94  THR 94  94  94  THR THR A . n 
A 1 95  SER 95  95  95  SER SER A . n 
A 1 96  GLU 96  96  96  GLU GLU A . n 
A 1 97  LEU 97  97  97  LEU LEU A . n 
A 1 98  ALA 98  98  98  ALA ALA A . n 
A 1 99  LYS 99  99  99  LYS LYS A . n 
A 1 100 ARG 100 100 100 ARG ARG A . n 
A 1 101 LEU 101 101 101 LEU LEU A . n 
A 1 102 ALA 102 102 102 ALA ALA A . n 
A 1 103 GLN 103 103 103 GLN GLN A . n 
A 1 104 ALA 104 104 104 ALA ALA A . n 
A 1 105 PRO 105 105 105 PRO PRO A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 LEU 107 107 107 LEU LEU A . n 
A 1 108 LYS 108 108 108 LYS LYS A . n 
A 1 109 ASP 109 109 109 ASP ASP A . n 
A 1 110 ILE 110 110 110 ILE ILE A . n 
A 1 111 PRO 111 111 111 PRO PRO A . n 
A 1 112 GLY 112 112 112 GLY GLY A . n 
A 1 113 THR 113 113 113 THR THR A . n 
A 1 114 LEU 114 114 114 LEU LEU A . n 
A 1 115 PHE 115 115 115 PHE PHE A . n 
A 1 116 LEU 116 116 116 LEU LEU A . n 
A 1 117 ALA 117 117 117 ALA ALA A . n 
A 1 118 GLY 118 118 118 GLY GLY A . n 
A 1 119 GLY 119 119 119 GLY GLY A . n 
A 1 120 THR 120 120 120 THR THR A . n 
A 1 121 PRO 121 121 121 PRO PRO A . n 
A 1 122 VAL 122 122 122 VAL VAL A . n 
A 1 123 THR 123 123 123 THR THR A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 LYS 125 125 125 LYS LYS A . n 
A 1 126 GLY 126 126 126 GLY GLY A . n 
A 1 127 ALA 127 127 127 ALA ALA A . n 
A 1 128 PRO 128 128 128 PRO PRO A . n 
A 1 129 VAL 129 129 129 VAL VAL A . n 
A 1 130 ALA 130 130 130 ALA ALA A . n 
A 1 131 GLY 131 131 131 GLY GLY A . n 
A 1 132 ILE 132 132 132 ILE ILE A . n 
A 1 133 GLY 133 133 133 GLY GLY A . n 
A 1 134 VAL 134 134 134 VAL VAL A . n 
A 1 135 ALA 135 135 135 ALA ALA A . n 
A 1 136 GLY 136 136 136 GLY GLY A . n 
A 1 137 ALA 137 137 137 ALA ALA A . n 
A 1 138 PRO 138 138 138 PRO PRO A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 GLY 140 140 140 GLY GLY A . n 
A 1 141 ASP 141 141 141 ASP ASP A . n 
A 1 142 LEU 142 142 142 LEU LEU A . n 
A 1 143 ASP 143 143 143 ASP ASP A . n 
A 1 144 GLU 144 144 144 GLU GLU A . n 
A 1 145 GLN 145 145 145 GLN GLN A . n 
A 1 146 TYR 146 146 146 TYR TYR A . n 
A 1 147 ALA 147 147 147 ALA ALA A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 ALA 149 149 149 ALA ALA A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 ALA 151 151 151 ALA ALA A . n 
A 1 152 ALA 152 152 152 ALA ALA A . n 
A 1 153 VAL 153 153 153 VAL VAL A . n 
A 1 154 LEU 154 154 154 LEU LEU A . n 
A 1 155 GLY 155 155 155 GLY GLY A . n 
A 1 156 HIS 156 156 156 HIS HIS 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 HOH 1   2001 2001 HOH HOH A . 
B 2 HOH 2   2002 2002 HOH HOH A . 
B 2 HOH 3   2003 2003 HOH HOH A . 
B 2 HOH 4   2004 2004 HOH HOH A . 
B 2 HOH 5   2005 2005 HOH HOH A . 
B 2 HOH 6   2006 2006 HOH HOH A . 
B 2 HOH 7   2007 2007 HOH HOH A . 
B 2 HOH 8   2008 2008 HOH HOH A . 
B 2 HOH 9   2009 2009 HOH HOH A . 
B 2 HOH 10  2010 2010 HOH HOH A . 
B 2 HOH 11  2011 2011 HOH HOH A . 
B 2 HOH 12  2012 2012 HOH HOH A . 
B 2 HOH 13  2013 2013 HOH HOH A . 
B 2 HOH 14  2014 2014 HOH HOH A . 
B 2 HOH 15  2015 2015 HOH HOH A . 
B 2 HOH 16  2016 2016 HOH HOH A . 
B 2 HOH 17  2017 2017 HOH HOH A . 
B 2 HOH 18  2018 2018 HOH HOH A . 
B 2 HOH 19  2019 2019 HOH HOH A . 
B 2 HOH 20  2020 2020 HOH HOH A . 
B 2 HOH 21  2021 2021 HOH HOH A . 
B 2 HOH 22  2022 2022 HOH HOH A . 
B 2 HOH 23  2023 2023 HOH HOH A . 
B 2 HOH 24  2024 2024 HOH HOH A . 
B 2 HOH 25  2025 2025 HOH HOH A . 
B 2 HOH 26  2026 2026 HOH HOH A . 
B 2 HOH 27  2027 2027 HOH HOH A . 
B 2 HOH 28  2028 2028 HOH HOH A . 
B 2 HOH 29  2029 2029 HOH HOH A . 
B 2 HOH 30  2030 2030 HOH HOH A . 
B 2 HOH 31  2031 2031 HOH HOH A . 
B 2 HOH 32  2032 2032 HOH HOH A . 
B 2 HOH 33  2033 2033 HOH HOH A . 
B 2 HOH 34  2034 2034 HOH HOH A . 
B 2 HOH 35  2035 2035 HOH HOH A . 
B 2 HOH 36  2036 2036 HOH HOH A . 
B 2 HOH 37  2037 2037 HOH HOH A . 
B 2 HOH 38  2038 2038 HOH HOH A . 
B 2 HOH 39  2039 2039 HOH HOH A . 
B 2 HOH 40  2040 2040 HOH HOH A . 
B 2 HOH 41  2041 2041 HOH HOH A . 
B 2 HOH 42  2042 2042 HOH HOH A . 
B 2 HOH 43  2043 2043 HOH HOH A . 
B 2 HOH 44  2044 2044 HOH HOH A . 
B 2 HOH 45  2045 2045 HOH HOH A . 
B 2 HOH 46  2046 2046 HOH HOH A . 
B 2 HOH 47  2047 2047 HOH HOH A . 
B 2 HOH 48  2048 2048 HOH HOH A . 
B 2 HOH 49  2049 2049 HOH HOH A . 
B 2 HOH 50  2050 2050 HOH HOH A . 
B 2 HOH 51  2051 2051 HOH HOH A . 
B 2 HOH 52  2052 2052 HOH HOH A . 
B 2 HOH 53  2053 2053 HOH HOH A . 
B 2 HOH 54  2054 2054 HOH HOH A . 
B 2 HOH 55  2055 2055 HOH HOH A . 
B 2 HOH 56  2056 2056 HOH HOH A . 
B 2 HOH 57  2057 2057 HOH HOH A . 
B 2 HOH 58  2058 2058 HOH HOH A . 
B 2 HOH 59  2059 2059 HOH HOH A . 
B 2 HOH 60  2060 2060 HOH HOH A . 
B 2 HOH 61  2061 2061 HOH HOH A . 
B 2 HOH 62  2062 2062 HOH HOH A . 
B 2 HOH 63  2063 2063 HOH HOH A . 
B 2 HOH 64  2064 2064 HOH HOH A . 
B 2 HOH 65  2065 2065 HOH HOH A . 
B 2 HOH 66  2066 2066 HOH HOH A . 
B 2 HOH 67  2067 2067 HOH HOH A . 
B 2 HOH 68  2068 2068 HOH HOH A . 
B 2 HOH 69  2069 2069 HOH HOH A . 
B 2 HOH 70  2070 2070 HOH HOH A . 
B 2 HOH 71  2071 2071 HOH HOH A . 
B 2 HOH 72  2072 2072 HOH HOH A . 
B 2 HOH 73  2073 2073 HOH HOH A . 
B 2 HOH 74  2074 2074 HOH HOH A . 
B 2 HOH 75  2075 2075 HOH HOH A . 
B 2 HOH 76  2076 2076 HOH HOH A . 
B 2 HOH 77  2077 2077 HOH HOH A . 
B 2 HOH 78  2078 2078 HOH HOH A . 
B 2 HOH 79  2079 2079 HOH HOH A . 
B 2 HOH 80  2080 2080 HOH HOH A . 
B 2 HOH 81  2081 2081 HOH HOH A . 
B 2 HOH 82  2082 2082 HOH HOH A . 
B 2 HOH 83  2083 2083 HOH HOH A . 
B 2 HOH 84  2084 2084 HOH HOH A . 
B 2 HOH 85  2085 2085 HOH HOH A . 
B 2 HOH 86  2086 2086 HOH HOH A . 
B 2 HOH 87  2087 2087 HOH HOH A . 
B 2 HOH 88  2088 2088 HOH HOH A . 
B 2 HOH 89  2089 2089 HOH HOH A . 
B 2 HOH 90  2090 2090 HOH HOH A . 
B 2 HOH 91  2091 2091 HOH HOH A . 
B 2 HOH 92  2092 2092 HOH HOH A . 
B 2 HOH 93  2093 2093 HOH HOH A . 
B 2 HOH 94  2094 2094 HOH HOH A . 
B 2 HOH 95  2095 2095 HOH HOH A . 
B 2 HOH 96  2096 2096 HOH HOH A . 
B 2 HOH 97  2097 2097 HOH HOH A . 
B 2 HOH 98  2098 2098 HOH HOH A . 
B 2 HOH 99  2099 2099 HOH HOH A . 
B 2 HOH 100 2100 2100 HOH HOH A . 
B 2 HOH 101 2101 2101 HOH HOH A . 
B 2 HOH 102 2102 2102 HOH HOH A . 
B 2 HOH 103 2103 2103 HOH HOH A . 
B 2 HOH 104 2104 2104 HOH HOH A . 
B 2 HOH 105 2105 2105 HOH HOH A . 
B 2 HOH 106 2106 2106 HOH HOH A . 
B 2 HOH 107 2107 2107 HOH HOH A . 
B 2 HOH 108 2108 2108 HOH HOH A . 
B 2 HOH 109 2109 2109 HOH HOH A . 
B 2 HOH 110 2110 2110 HOH HOH A . 
B 2 HOH 111 2111 2111 HOH HOH A . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   octameric 
_pdbx_struct_assembly.oligomeric_count     8 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2,3,4,5,6,7,8 
_pdbx_struct_assembly_gen.asym_id_list      A,B 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 20140 ? 
1 MORE         -94.4 ? 
1 'SSA (A^2)'  39260 ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z          1.0000000000  0.0000000000  0.0000000000 0.0000000000   0.0000000000  
1.0000000000  0.0000000000 0.0000000000    0.0000000000 0.0000000000 1.0000000000  0.0000000000   
2 'crystal symmetry operation' 3_735 -y+2,x-2,z     0.0000000000  -1.0000000000 0.0000000000 154.7800000000 1.0000000000  
0.0000000000  0.0000000000 -154.7800000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000   
3 'crystal symmetry operation' 6_554 x,-y,-z-1      1.0000000000  0.0000000000  0.0000000000 0.0000000000   0.0000000000  
-1.0000000000 0.0000000000 0.0000000000    0.0000000000 0.0000000000 -1.0000000000 -79.8600000000 
4 'crystal symmetry operation' 2_955 -x+4,-y,z      -1.0000000000 0.0000000000  0.0000000000 309.5600000000 0.0000000000  
-1.0000000000 0.0000000000 0.0000000000    0.0000000000 0.0000000000 1.0000000000  0.0000000000   
5 'crystal symmetry operation' 5_954 -x+4,y,-z-1    -1.0000000000 0.0000000000  0.0000000000 309.5600000000 0.0000000000  
1.0000000000  0.0000000000 0.0000000000    0.0000000000 0.0000000000 -1.0000000000 -79.8600000000 
6 'crystal symmetry operation' 8_774 -y+2,-x+2,-z-1 0.0000000000  -1.0000000000 0.0000000000 154.7800000000 -1.0000000000 
0.0000000000  0.0000000000 154.7800000000  0.0000000000 0.0000000000 -1.0000000000 -79.8600000000 
7 'crystal symmetry operation' 4_775 y+2,-x+2,z     0.0000000000  1.0000000000  0.0000000000 154.7800000000 -1.0000000000 
0.0000000000  0.0000000000 154.7800000000  0.0000000000 0.0000000000 1.0000000000  0.0000000000   
8 'crystal symmetry operation' 7_734 y+2,x-2,-z-1   0.0000000000  1.0000000000  0.0000000000 154.7800000000 1.0000000000  
0.0000000000  0.0000000000 -154.7800000000 0.0000000000 0.0000000000 -1.0000000000 -79.8600000000 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A PRO 15   ? A PRO 15 
2 1 A HOH 2015 ? B HOH .  
3 1 A HOH 2027 ? B HOH .  
4 1 A HOH 2028 ? B HOH .  
5 1 A HOH 2031 ? B HOH .  
6 1 A HOH 2036 ? B HOH .  
7 1 A HOH 2093 ? B HOH .  
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2013-09-25 
2 'Structure model' 1 1 2014-08-20 
3 'Structure model' 1 2 2015-07-15 
4 'Structure model' 1 3 2018-02-07 
5 'Structure model' 1 4 2023-12-20 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1  2 'Structure model' 'Data collection'        
2  3 'Structure model' 'Data collection'        
3  4 'Structure model' 'Data collection'        
4  4 'Structure model' 'Database references'    
5  4 'Structure model' 'Source and taxonomy'    
6  5 'Structure model' 'Data collection'        
7  5 'Structure model' 'Database references'    
8  5 'Structure model' 'Derived calculations'   
9  5 'Structure model' Other                    
10 5 'Structure model' 'Refinement description' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 4 'Structure model' citation_author               
2 4 'Structure model' diffrn_source                 
3 4 'Structure model' entity_src_gen                
4 5 'Structure model' chem_comp_atom                
5 5 'Structure model' chem_comp_bond                
6 5 'Structure model' database_2                    
7 5 'Structure model' pdbx_database_status          
8 5 'Structure model' pdbx_initial_refinement_model 
9 5 'Structure model' pdbx_struct_special_symmetry  
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 4 'Structure model' '_citation_author.name'                         
2 4 'Structure model' '_diffrn_source.pdbx_synchrotron_site'          
3 4 'Structure model' '_entity_src_gen.pdbx_host_org_scientific_name' 
4 4 'Structure model' '_entity_src_gen.pdbx_host_org_strain'          
5 5 'Structure model' '_database_2.pdbx_DOI'                          
6 5 'Structure model' '_database_2.pdbx_database_accession'           
7 5 'Structure model' '_pdbx_database_status.status_code_sf'          
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
'X-RAY DIFFRACTION' 1 ? refined 167.4679 -28.3919 -21.8363 0.4804 0.2810 0.2095 -0.1083 -0.0473 -0.0004 4.7664 1.7592 2.1089 
1.1022  0.2792  -0.9520 0.3596  -0.9878 0.3908  1.3087  -0.3480 -0.3089 -0.0496 0.0265  0.1464  
'X-RAY DIFFRACTION' 2 ? refined 175.6089 -23.4007 -39.9085 0.4243 0.2837 0.3368 0.0913  0.0428  -0.0290 9.1671 9.6681 6.7041 
8.1585  -6.7621 -7.4069 -0.4720 0.6532  -0.8973 0.7776  0.4479  -0.6548 0.0882  -0.6455 0.1502  
'X-RAY DIFFRACTION' 3 ? refined 185.7054 -0.5354  -46.1978 0.2925 0.3741 0.3355 -0.0448 -0.0400 0.0248  2.4292 3.1084 7.2209 
-0.3528 1.4165  -4.2212 0.1071  0.1109  0.1203  0.6895  -0.7895 -0.9180 -0.4198 0.6978  0.7387  
'X-RAY DIFFRACTION' 4 ? refined 175.5371 1.3344   -46.9126 0.2252 0.3012 0.2138 -0.0388 0.0285  -0.0198 1.3854 4.4397 2.1759 
0.0267  0.9118  -0.3785 -0.0784 0.0352  0.1715  0.2548  0.0388  -0.2593 -0.4402 0.2700  0.0454  
'X-RAY DIFFRACTION' 5 ? refined 169.1300 -3.8503  -50.3617 0.2540 0.2943 0.2518 0.0261  -0.0133 0.0202  5.6806 2.8628 4.5774 
2.2644  -0.3880 2.7720  0.0222  0.2705  -0.1250 0.0632  -0.0311 0.6832  -0.0227 -0.1724 -0.0115 
'X-RAY DIFFRACTION' 6 ? refined 165.2410 -8.2198  -62.0343 0.3753 0.3448 0.2576 -0.0513 0.0111  -0.0976 8.7576 2.7735 7.3380 
-0.5784 2.4628  -4.4541 0.2858  0.9983  -0.2612 -0.6874 -0.0328 0.2589  0.8136  -0.2883 -0.2875 
'X-RAY DIFFRACTION' 7 ? refined 173.1445 -6.7458  -53.7019 0.2709 0.2328 0.1883 -0.0093 0.0334  -0.0222 2.5862 3.6479 4.0563 
0.4106  0.8865  -0.6269 0.0063  0.1209  -0.1589 0.0259  0.0113  0.0844  0.1420  -0.1328 -0.0270 
'X-RAY DIFFRACTION' 8 ? refined 182.7029 -3.0703  -56.3218 0.3757 0.3652 0.3091 0.0110  0.0744  -0.0329 9.7525 5.6199 6.9362 
-3.3133 5.7633  -5.9393 0.3168  0.4976  0.2461  -1.1679 -0.3319 -0.8960 0.6989  0.4789  0.0384  
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1 1 ? ? ? ? ? ? ? ? ? 'CHAIN A AND (RESID 11 THROUGH 19 )'   
'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? 'CHAIN A AND (RESID 20 THROUGH 30 )'   
'X-RAY DIFFRACTION' 3 3 ? ? ? ? ? ? ? ? ? 'CHAIN A AND (RESID 31 THROUGH 47 )'   
'X-RAY DIFFRACTION' 4 4 ? ? ? ? ? ? ? ? ? 'CHAIN A AND (RESID 48 THROUGH 75 )'   
'X-RAY DIFFRACTION' 5 5 ? ? ? ? ? ? ? ? ? 'CHAIN A AND (RESID 76 THROUGH 90 )'   
'X-RAY DIFFRACTION' 6 6 ? ? ? ? ? ? ? ? ? 'CHAIN A AND (RESID 91 THROUGH 109 )'  
'X-RAY DIFFRACTION' 7 7 ? ? ? ? ? ? ? ? ? 'CHAIN A AND (RESID 110 THROUGH 139 )' 
'X-RAY DIFFRACTION' 8 8 ? ? ? ? ? ? ? ? ? 'CHAIN A AND (RESID 140 THROUGH 156 )' 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
_software.date 
_software.type 
_software.location 
_software.language 
PHENIX refinement       '(PHENIX.REFINE)' ? 1 ? ? ? ? 
XDS    'data reduction' .                 ? 2 ? ? ? ? 
XSCALE 'data scaling'   .                 ? 3 ? ? ? ? 
PHASER phasing          .                 ? 4 ? ? ? ? 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    ALA 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     13 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    A 
_pdbx_validate_torsion.phi             176.21 
_pdbx_validate_torsion.psi             170.97 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       2036 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.41 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 1  ? A GLY 1  
2  1 Y 1 A ALA 2  ? A ALA 2  
3  1 Y 1 A MET 3  ? A MET 3  
4  1 Y 1 A ALA 4  ? A ALA 4  
5  1 Y 1 A ASP 5  ? A ASP 5  
6  1 Y 1 A THR 6  ? A THR 6  
7  1 Y 1 A THR 7  ? A THR 7  
8  1 Y 1 A GLU 8  ? A GLU 8  
9  1 Y 1 A ALA 9  ? A ALA 9  
10 1 Y 1 A THR 10 ? A THR 10 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
GLN N    N N N 74  
GLN CA   C N S 75  
GLN C    C N N 76  
GLN O    O N N 77  
GLN CB   C N N 78  
GLN CG   C N N 79  
GLN CD   C N N 80  
GLN OE1  O N N 81  
GLN NE2  N N N 82  
GLN OXT  O N N 83  
GLN H    H N N 84  
GLN H2   H N N 85  
GLN HA   H N N 86  
GLN HB2  H N N 87  
GLN HB3  H N N 88  
GLN HG2  H N N 89  
GLN HG3  H N N 90  
GLN HE21 H N N 91  
GLN HE22 H N N 92  
GLN HXT  H N N 93  
GLU N    N N N 94  
GLU CA   C N S 95  
GLU C    C N N 96  
GLU O    O N N 97  
GLU CB   C N N 98  
GLU CG   C N N 99  
GLU CD   C N N 100 
GLU OE1  O N N 101 
GLU OE2  O N N 102 
GLU OXT  O N N 103 
GLU H    H N N 104 
GLU H2   H N N 105 
GLU HA   H N N 106 
GLU HB2  H N N 107 
GLU HB3  H N N 108 
GLU HG2  H N N 109 
GLU HG3  H N N 110 
GLU HE2  H N N 111 
GLU HXT  H N N 112 
GLY N    N N N 113 
GLY CA   C N N 114 
GLY C    C N N 115 
GLY O    O N N 116 
GLY OXT  O N N 117 
GLY H    H N N 118 
GLY H2   H N N 119 
GLY HA2  H N N 120 
GLY HA3  H N N 121 
GLY HXT  H N N 122 
HIS N    N N N 123 
HIS CA   C N S 124 
HIS C    C N N 125 
HIS O    O N N 126 
HIS CB   C N N 127 
HIS CG   C Y N 128 
HIS ND1  N Y N 129 
HIS CD2  C Y N 130 
HIS CE1  C Y N 131 
HIS NE2  N Y N 132 
HIS OXT  O N N 133 
HIS H    H N N 134 
HIS H2   H N N 135 
HIS HA   H N N 136 
HIS HB2  H N N 137 
HIS HB3  H N N 138 
HIS HD1  H N N 139 
HIS HD2  H N N 140 
HIS HE1  H N N 141 
HIS HE2  H N N 142 
HIS HXT  H N N 143 
HOH O    O N N 144 
HOH H1   H N N 145 
HOH H2   H N N 146 
ILE N    N N N 147 
ILE CA   C N S 148 
ILE C    C N N 149 
ILE O    O N N 150 
ILE CB   C N S 151 
ILE CG1  C N N 152 
ILE CG2  C N N 153 
ILE CD1  C N N 154 
ILE OXT  O N N 155 
ILE H    H N N 156 
ILE H2   H N N 157 
ILE HA   H N N 158 
ILE HB   H N N 159 
ILE HG12 H N N 160 
ILE HG13 H N N 161 
ILE HG21 H N N 162 
ILE HG22 H N N 163 
ILE HG23 H N N 164 
ILE HD11 H N N 165 
ILE HD12 H N N 166 
ILE HD13 H N N 167 
ILE HXT  H N N 168 
LEU N    N N N 169 
LEU CA   C N S 170 
LEU C    C N N 171 
LEU O    O N N 172 
LEU CB   C N N 173 
LEU CG   C N N 174 
LEU CD1  C N N 175 
LEU CD2  C N N 176 
LEU OXT  O N N 177 
LEU H    H N N 178 
LEU H2   H N N 179 
LEU HA   H N N 180 
LEU HB2  H N N 181 
LEU HB3  H N N 182 
LEU HG   H N N 183 
LEU HD11 H N N 184 
LEU HD12 H N N 185 
LEU HD13 H N N 186 
LEU HD21 H N N 187 
LEU HD22 H N N 188 
LEU HD23 H N N 189 
LEU HXT  H N N 190 
LYS N    N N N 191 
LYS CA   C N S 192 
LYS C    C N N 193 
LYS O    O N N 194 
LYS CB   C N N 195 
LYS CG   C N N 196 
LYS CD   C N N 197 
LYS CE   C N N 198 
LYS NZ   N N N 199 
LYS OXT  O N N 200 
LYS H    H N N 201 
LYS H2   H N N 202 
LYS HA   H N N 203 
LYS HB2  H N N 204 
LYS HB3  H N N 205 
LYS HG2  H N N 206 
LYS HG3  H N N 207 
LYS HD2  H N N 208 
LYS HD3  H N N 209 
LYS HE2  H N N 210 
LYS HE3  H N N 211 
LYS HZ1  H N N 212 
LYS HZ2  H N N 213 
LYS HZ3  H N N 214 
LYS HXT  H N N 215 
MET N    N N N 216 
MET CA   C N S 217 
MET C    C N N 218 
MET O    O N N 219 
MET CB   C N N 220 
MET CG   C N N 221 
MET SD   S N N 222 
MET CE   C N N 223 
MET OXT  O N N 224 
MET H    H N N 225 
MET H2   H N N 226 
MET HA   H N N 227 
MET HB2  H N N 228 
MET HB3  H N N 229 
MET HG2  H N N 230 
MET HG3  H N N 231 
MET HE1  H N N 232 
MET HE2  H N N 233 
MET HE3  H N N 234 
MET HXT  H N N 235 
PHE N    N N N 236 
PHE CA   C N S 237 
PHE C    C N N 238 
PHE O    O N N 239 
PHE CB   C N N 240 
PHE CG   C Y N 241 
PHE CD1  C Y N 242 
PHE CD2  C Y N 243 
PHE CE1  C Y N 244 
PHE CE2  C Y N 245 
PHE CZ   C Y N 246 
PHE OXT  O N N 247 
PHE H    H N N 248 
PHE H2   H N N 249 
PHE HA   H N N 250 
PHE HB2  H N N 251 
PHE HB3  H N N 252 
PHE HD1  H N N 253 
PHE HD2  H N N 254 
PHE HE1  H N N 255 
PHE HE2  H N N 256 
PHE HZ   H N N 257 
PHE HXT  H N N 258 
PRO N    N N N 259 
PRO CA   C N S 260 
PRO C    C N N 261 
PRO O    O N N 262 
PRO CB   C N N 263 
PRO CG   C N N 264 
PRO CD   C N N 265 
PRO OXT  O N N 266 
PRO H    H N N 267 
PRO HA   H N N 268 
PRO HB2  H N N 269 
PRO HB3  H N N 270 
PRO HG2  H N N 271 
PRO HG3  H N N 272 
PRO HD2  H N N 273 
PRO HD3  H N N 274 
PRO HXT  H N N 275 
SER N    N N N 276 
SER CA   C N S 277 
SER C    C N N 278 
SER O    O N N 279 
SER CB   C N N 280 
SER OG   O N N 281 
SER OXT  O N N 282 
SER H    H N N 283 
SER H2   H N N 284 
SER HA   H N N 285 
SER HB2  H N N 286 
SER HB3  H N N 287 
SER HG   H N N 288 
SER HXT  H N N 289 
THR N    N N N 290 
THR CA   C N S 291 
THR C    C N N 292 
THR O    O N N 293 
THR CB   C N R 294 
THR OG1  O N N 295 
THR CG2  C N N 296 
THR OXT  O N N 297 
THR H    H N N 298 
THR H2   H N N 299 
THR HA   H N N 300 
THR HB   H N N 301 
THR HG1  H N N 302 
THR HG21 H N N 303 
THR HG22 H N N 304 
THR HG23 H N N 305 
THR HXT  H N N 306 
TRP N    N N N 307 
TRP CA   C N S 308 
TRP C    C N N 309 
TRP O    O N N 310 
TRP CB   C N N 311 
TRP CG   C Y N 312 
TRP CD1  C Y N 313 
TRP CD2  C Y N 314 
TRP NE1  N Y N 315 
TRP CE2  C Y N 316 
TRP CE3  C Y N 317 
TRP CZ2  C Y N 318 
TRP CZ3  C Y N 319 
TRP CH2  C Y N 320 
TRP OXT  O N N 321 
TRP H    H N N 322 
TRP H2   H N N 323 
TRP HA   H N N 324 
TRP HB2  H N N 325 
TRP HB3  H N N 326 
TRP HD1  H N N 327 
TRP HE1  H N N 328 
TRP HE3  H N N 329 
TRP HZ2  H N N 330 
TRP HZ3  H N N 331 
TRP HH2  H N N 332 
TRP HXT  H N N 333 
TYR N    N N N 334 
TYR CA   C N S 335 
TYR C    C N N 336 
TYR O    O N N 337 
TYR CB   C N N 338 
TYR CG   C Y N 339 
TYR CD1  C Y N 340 
TYR CD2  C Y N 341 
TYR CE1  C Y N 342 
TYR CE2  C Y N 343 
TYR CZ   C Y N 344 
TYR OH   O N N 345 
TYR OXT  O N N 346 
TYR H    H N N 347 
TYR H2   H N N 348 
TYR HA   H N N 349 
TYR HB2  H N N 350 
TYR HB3  H N N 351 
TYR HD1  H N N 352 
TYR HD2  H N N 353 
TYR HE1  H N N 354 
TYR HE2  H N N 355 
TYR HH   H N N 356 
TYR HXT  H N N 357 
VAL N    N N N 358 
VAL CA   C N S 359 
VAL C    C N N 360 
VAL O    O N N 361 
VAL CB   C N N 362 
VAL CG1  C N N 363 
VAL CG2  C N N 364 
VAL OXT  O N N 365 
VAL H    H N N 366 
VAL H2   H N N 367 
VAL HA   H N N 368 
VAL HB   H N N 369 
VAL HG11 H N N 370 
VAL HG12 H N N 371 
VAL HG13 H N N 372 
VAL HG21 H N N 373 
VAL HG22 H N N 374 
VAL HG23 H N N 375 
VAL HXT  H N N 376 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
GLN N   CA   sing N N 70  
GLN N   H    sing N N 71  
GLN N   H2   sing N N 72  
GLN CA  C    sing N N 73  
GLN CA  CB   sing N N 74  
GLN CA  HA   sing N N 75  
GLN C   O    doub N N 76  
GLN C   OXT  sing N N 77  
GLN CB  CG   sing N N 78  
GLN CB  HB2  sing N N 79  
GLN CB  HB3  sing N N 80  
GLN CG  CD   sing N N 81  
GLN CG  HG2  sing N N 82  
GLN CG  HG3  sing N N 83  
GLN CD  OE1  doub N N 84  
GLN CD  NE2  sing N N 85  
GLN NE2 HE21 sing N N 86  
GLN NE2 HE22 sing N N 87  
GLN OXT HXT  sing N N 88  
GLU N   CA   sing N N 89  
GLU N   H    sing N N 90  
GLU N   H2   sing N N 91  
GLU CA  C    sing N N 92  
GLU CA  CB   sing N N 93  
GLU CA  HA   sing N N 94  
GLU C   O    doub N N 95  
GLU C   OXT  sing N N 96  
GLU CB  CG   sing N N 97  
GLU CB  HB2  sing N N 98  
GLU CB  HB3  sing N N 99  
GLU CG  CD   sing N N 100 
GLU CG  HG2  sing N N 101 
GLU CG  HG3  sing N N 102 
GLU CD  OE1  doub N N 103 
GLU CD  OE2  sing N N 104 
GLU OE2 HE2  sing N N 105 
GLU OXT HXT  sing N N 106 
GLY N   CA   sing N N 107 
GLY N   H    sing N N 108 
GLY N   H2   sing N N 109 
GLY CA  C    sing N N 110 
GLY CA  HA2  sing N N 111 
GLY CA  HA3  sing N N 112 
GLY C   O    doub N N 113 
GLY C   OXT  sing N N 114 
GLY OXT HXT  sing N N 115 
HIS N   CA   sing N N 116 
HIS N   H    sing N N 117 
HIS N   H2   sing N N 118 
HIS CA  C    sing N N 119 
HIS CA  CB   sing N N 120 
HIS CA  HA   sing N N 121 
HIS C   O    doub N N 122 
HIS C   OXT  sing N N 123 
HIS CB  CG   sing N N 124 
HIS CB  HB2  sing N N 125 
HIS CB  HB3  sing N N 126 
HIS CG  ND1  sing Y N 127 
HIS CG  CD2  doub Y N 128 
HIS ND1 CE1  doub Y N 129 
HIS ND1 HD1  sing N N 130 
HIS CD2 NE2  sing Y N 131 
HIS CD2 HD2  sing N N 132 
HIS CE1 NE2  sing Y N 133 
HIS CE1 HE1  sing N N 134 
HIS NE2 HE2  sing N N 135 
HIS OXT HXT  sing N N 136 
HOH O   H1   sing N N 137 
HOH O   H2   sing N N 138 
ILE N   CA   sing N N 139 
ILE N   H    sing N N 140 
ILE N   H2   sing N N 141 
ILE CA  C    sing N N 142 
ILE CA  CB   sing N N 143 
ILE CA  HA   sing N N 144 
ILE C   O    doub N N 145 
ILE C   OXT  sing N N 146 
ILE CB  CG1  sing N N 147 
ILE CB  CG2  sing N N 148 
ILE CB  HB   sing N N 149 
ILE CG1 CD1  sing N N 150 
ILE CG1 HG12 sing N N 151 
ILE CG1 HG13 sing N N 152 
ILE CG2 HG21 sing N N 153 
ILE CG2 HG22 sing N N 154 
ILE CG2 HG23 sing N N 155 
ILE CD1 HD11 sing N N 156 
ILE CD1 HD12 sing N N 157 
ILE CD1 HD13 sing N N 158 
ILE OXT HXT  sing N N 159 
LEU N   CA   sing N N 160 
LEU N   H    sing N N 161 
LEU N   H2   sing N N 162 
LEU CA  C    sing N N 163 
LEU CA  CB   sing N N 164 
LEU CA  HA   sing N N 165 
LEU C   O    doub N N 166 
LEU C   OXT  sing N N 167 
LEU CB  CG   sing N N 168 
LEU CB  HB2  sing N N 169 
LEU CB  HB3  sing N N 170 
LEU CG  CD1  sing N N 171 
LEU CG  CD2  sing N N 172 
LEU CG  HG   sing N N 173 
LEU CD1 HD11 sing N N 174 
LEU CD1 HD12 sing N N 175 
LEU CD1 HD13 sing N N 176 
LEU CD2 HD21 sing N N 177 
LEU CD2 HD22 sing N N 178 
LEU CD2 HD23 sing N N 179 
LEU OXT HXT  sing N N 180 
LYS N   CA   sing N N 181 
LYS N   H    sing N N 182 
LYS N   H2   sing N N 183 
LYS CA  C    sing N N 184 
LYS CA  CB   sing N N 185 
LYS CA  HA   sing N N 186 
LYS C   O    doub N N 187 
LYS C   OXT  sing N N 188 
LYS CB  CG   sing N N 189 
LYS CB  HB2  sing N N 190 
LYS CB  HB3  sing N N 191 
LYS CG  CD   sing N N 192 
LYS CG  HG2  sing N N 193 
LYS CG  HG3  sing N N 194 
LYS CD  CE   sing N N 195 
LYS CD  HD2  sing N N 196 
LYS CD  HD3  sing N N 197 
LYS CE  NZ   sing N N 198 
LYS CE  HE2  sing N N 199 
LYS CE  HE3  sing N N 200 
LYS NZ  HZ1  sing N N 201 
LYS NZ  HZ2  sing N N 202 
LYS NZ  HZ3  sing N N 203 
LYS OXT HXT  sing N N 204 
MET N   CA   sing N N 205 
MET N   H    sing N N 206 
MET N   H2   sing N N 207 
MET CA  C    sing N N 208 
MET CA  CB   sing N N 209 
MET CA  HA   sing N N 210 
MET C   O    doub N N 211 
MET C   OXT  sing N N 212 
MET CB  CG   sing N N 213 
MET CB  HB2  sing N N 214 
MET CB  HB3  sing N N 215 
MET CG  SD   sing N N 216 
MET CG  HG2  sing N N 217 
MET CG  HG3  sing N N 218 
MET SD  CE   sing N N 219 
MET CE  HE1  sing N N 220 
MET CE  HE2  sing N N 221 
MET CE  HE3  sing N N 222 
MET OXT HXT  sing N N 223 
PHE N   CA   sing N N 224 
PHE N   H    sing N N 225 
PHE N   H2   sing N N 226 
PHE CA  C    sing N N 227 
PHE CA  CB   sing N N 228 
PHE CA  HA   sing N N 229 
PHE C   O    doub N N 230 
PHE C   OXT  sing N N 231 
PHE CB  CG   sing N N 232 
PHE CB  HB2  sing N N 233 
PHE CB  HB3  sing N N 234 
PHE CG  CD1  doub Y N 235 
PHE CG  CD2  sing Y N 236 
PHE CD1 CE1  sing Y N 237 
PHE CD1 HD1  sing N N 238 
PHE CD2 CE2  doub Y N 239 
PHE CD2 HD2  sing N N 240 
PHE CE1 CZ   doub Y N 241 
PHE CE1 HE1  sing N N 242 
PHE CE2 CZ   sing Y N 243 
PHE CE2 HE2  sing N N 244 
PHE CZ  HZ   sing N N 245 
PHE OXT HXT  sing N N 246 
PRO N   CA   sing N N 247 
PRO N   CD   sing N N 248 
PRO N   H    sing N N 249 
PRO CA  C    sing N N 250 
PRO CA  CB   sing N N 251 
PRO CA  HA   sing N N 252 
PRO C   O    doub N N 253 
PRO C   OXT  sing N N 254 
PRO CB  CG   sing N N 255 
PRO CB  HB2  sing N N 256 
PRO CB  HB3  sing N N 257 
PRO CG  CD   sing N N 258 
PRO CG  HG2  sing N N 259 
PRO CG  HG3  sing N N 260 
PRO CD  HD2  sing N N 261 
PRO CD  HD3  sing N N 262 
PRO OXT HXT  sing N N 263 
SER N   CA   sing N N 264 
SER N   H    sing N N 265 
SER N   H2   sing N N 266 
SER CA  C    sing N N 267 
SER CA  CB   sing N N 268 
SER CA  HA   sing N N 269 
SER C   O    doub N N 270 
SER C   OXT  sing N N 271 
SER CB  OG   sing N N 272 
SER CB  HB2  sing N N 273 
SER CB  HB3  sing N N 274 
SER OG  HG   sing N N 275 
SER OXT HXT  sing N N 276 
THR N   CA   sing N N 277 
THR N   H    sing N N 278 
THR N   H2   sing N N 279 
THR CA  C    sing N N 280 
THR CA  CB   sing N N 281 
THR CA  HA   sing N N 282 
THR C   O    doub N N 283 
THR C   OXT  sing N N 284 
THR CB  OG1  sing N N 285 
THR CB  CG2  sing N N 286 
THR CB  HB   sing N N 287 
THR OG1 HG1  sing N N 288 
THR CG2 HG21 sing N N 289 
THR CG2 HG22 sing N N 290 
THR CG2 HG23 sing N N 291 
THR OXT HXT  sing N N 292 
TRP N   CA   sing N N 293 
TRP N   H    sing N N 294 
TRP N   H2   sing N N 295 
TRP CA  C    sing N N 296 
TRP CA  CB   sing N N 297 
TRP CA  HA   sing N N 298 
TRP C   O    doub N N 299 
TRP C   OXT  sing N N 300 
TRP CB  CG   sing N N 301 
TRP CB  HB2  sing N N 302 
TRP CB  HB3  sing N N 303 
TRP CG  CD1  doub Y N 304 
TRP CG  CD2  sing Y N 305 
TRP CD1 NE1  sing Y N 306 
TRP CD1 HD1  sing N N 307 
TRP CD2 CE2  doub Y N 308 
TRP CD2 CE3  sing Y N 309 
TRP NE1 CE2  sing Y N 310 
TRP NE1 HE1  sing N N 311 
TRP CE2 CZ2  sing Y N 312 
TRP CE3 CZ3  doub Y N 313 
TRP CE3 HE3  sing N N 314 
TRP CZ2 CH2  doub Y N 315 
TRP CZ2 HZ2  sing N N 316 
TRP CZ3 CH2  sing Y N 317 
TRP CZ3 HZ3  sing N N 318 
TRP CH2 HH2  sing N N 319 
TRP OXT HXT  sing N N 320 
TYR N   CA   sing N N 321 
TYR N   H    sing N N 322 
TYR N   H2   sing N N 323 
TYR CA  C    sing N N 324 
TYR CA  CB   sing N N 325 
TYR CA  HA   sing N N 326 
TYR C   O    doub N N 327 
TYR C   OXT  sing N N 328 
TYR CB  CG   sing N N 329 
TYR CB  HB2  sing N N 330 
TYR CB  HB3  sing N N 331 
TYR CG  CD1  doub Y N 332 
TYR CG  CD2  sing Y N 333 
TYR CD1 CE1  sing Y N 334 
TYR CD1 HD1  sing N N 335 
TYR CD2 CE2  doub Y N 336 
TYR CD2 HD2  sing N N 337 
TYR CE1 CZ   doub Y N 338 
TYR CE1 HE1  sing N N 339 
TYR CE2 CZ   sing Y N 340 
TYR CE2 HE2  sing N N 341 
TYR CZ  OH   sing N N 342 
TYR OH  HH   sing N N 343 
TYR OXT HXT  sing N N 344 
VAL N   CA   sing N N 345 
VAL N   H    sing N N 346 
VAL N   H2   sing N N 347 
VAL CA  C    sing N N 348 
VAL CA  CB   sing N N 349 
VAL CA  HA   sing N N 350 
VAL C   O    doub N N 351 
VAL C   OXT  sing N N 352 
VAL CB  CG1  sing N N 353 
VAL CB  CG2  sing N N 354 
VAL CB  HB   sing N N 355 
VAL CG1 HG11 sing N N 356 
VAL CG1 HG12 sing N N 357 
VAL CG1 HG13 sing N N 358 
VAL CG2 HG21 sing N N 359 
VAL CG2 HG22 sing N N 360 
VAL CG2 HG23 sing N N 361 
VAL OXT HXT  sing N N 362 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   3FPV 
_pdbx_initial_refinement_model.details          'PDB ENTRY 3FPV' 
# 
