data_3LTV
# 
_entry.id   3LTV 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.281 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   3LTV         
RCSB  RCSB057723   
WWPDB D_1000057723 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 3GTT 'MOUSE SOD1'               unspecified 
PDB 3GTV 'HUMAN-MOUSE SOD1 CHIMERA' unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        3LTV 
_pdbx_database_status.recvd_initial_deposition_date   2010-02-16 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Seetharaman, S.V.' 1 
'Taylor, A.B.'      2 
'Hart, P.J.'        3 
# 
_citation.id                        primary 
_citation.title                     'Structures of mouse SOD1 and human/mouse SOD1 chimeras.' 
_citation.journal_abbrev            Arch.Biochem.Biophys. 
_citation.journal_volume            503 
_citation.page_first                183 
_citation.page_last                 190 
_citation.year                      2010 
_citation.journal_id_ASTM           ABBIA4 
_citation.country                   US 
_citation.journal_id_ISSN           0003-9861 
_citation.journal_id_CSD            0158 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   20727846 
_citation.pdbx_database_id_DOI      10.1016/j.abb.2010.08.014 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Seetharaman, S.V.' 1 
primary 'Taylor, A.B.'      2 
primary 'Holloway, S.'      3 
primary 'Hart, P.J.'        4 
# 
_cell.entry_id           3LTV 
_cell.length_a           127.480 
_cell.length_b           127.480 
_cell.length_c           102.494 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        120.00 
_cell.Z_PDB              36 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         3LTV 
_symmetry.space_group_name_H-M             'P 61' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                169 
_symmetry.space_group_name_Hall            ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Superoxide dismutase [Cu-Zn],Superoxide dismutase [Cu-Zn]' 15750.348 6   1.15.1.1,1.15.1.1 ? 
;RESIDUES 2-81 FROM MOUSE PROTEIN, RESIDUES 82-154 FROM HUMAN PROTEIN,RESIDUES 2-81 FROM MOUSE PROTEIN, RESIDUES 82-154 FROM HUMAN PROTEIN
;
? 
2 non-polymer syn 'ZINC ION'                                                  65.409    6   ?                 ? ? ? 
3 water       nat water                                                       18.015    145 ?                 ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Superoxide dismutase 1,hSod1' 
# 
_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       
;AMKAVCVLKGDGPVQGTIHFEQKASGEPVVLSGQITGLTEGQHGFHVHQYGDNTQGCTSAGPHFNPHSKKHGGPADEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;AMKAVCVLKGDGPVQGTIHFEQKASGEPVVLSGQITGLTEGQHGFHVHQYGDNTQGCTSAGPHFNPHSKKHGGPADEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_strand_id                 A,B,C,D,E,F 
_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   ALA n 
1 2   MET n 
1 3   LYS n 
1 4   ALA n 
1 5   VAL n 
1 6   CYS n 
1 7   VAL n 
1 8   LEU n 
1 9   LYS n 
1 10  GLY n 
1 11  ASP n 
1 12  GLY n 
1 13  PRO n 
1 14  VAL n 
1 15  GLN n 
1 16  GLY n 
1 17  THR n 
1 18  ILE n 
1 19  HIS n 
1 20  PHE n 
1 21  GLU n 
1 22  GLN n 
1 23  LYS n 
1 24  ALA n 
1 25  SER n 
1 26  GLY n 
1 27  GLU n 
1 28  PRO n 
1 29  VAL n 
1 30  VAL n 
1 31  LEU n 
1 32  SER n 
1 33  GLY n 
1 34  GLN n 
1 35  ILE n 
1 36  THR n 
1 37  GLY n 
1 38  LEU n 
1 39  THR n 
1 40  GLU n 
1 41  GLY n 
1 42  GLN n 
1 43  HIS n 
1 44  GLY n 
1 45  PHE n 
1 46  HIS n 
1 47  VAL n 
1 48  HIS n 
1 49  GLN n 
1 50  TYR n 
1 51  GLY n 
1 52  ASP n 
1 53  ASN n 
1 54  THR n 
1 55  GLN n 
1 56  GLY n 
1 57  CYS n 
1 58  THR n 
1 59  SER n 
1 60  ALA n 
1 61  GLY n 
1 62  PRO n 
1 63  HIS n 
1 64  PHE n 
1 65  ASN n 
1 66  PRO n 
1 67  HIS n 
1 68  SER n 
1 69  LYS n 
1 70  LYS n 
1 71  HIS n 
1 72  GLY n 
1 73  GLY n 
1 74  PRO n 
1 75  ALA n 
1 76  ASP n 
1 77  GLU n 
1 78  GLU n 
1 79  ARG n 
1 80  HIS n 
1 81  VAL n 
1 82  GLY n 
1 83  ASP n 
1 84  LEU n 
1 85  GLY n 
1 86  ASN n 
1 87  VAL n 
1 88  THR n 
1 89  ALA n 
1 90  ASP n 
1 91  LYS n 
1 92  ASP n 
1 93  GLY n 
1 94  VAL n 
1 95  ALA n 
1 96  ASP n 
1 97  VAL n 
1 98  SER n 
1 99  ILE n 
1 100 GLU n 
1 101 ASP n 
1 102 SER n 
1 103 VAL n 
1 104 ILE n 
1 105 SER n 
1 106 LEU n 
1 107 SER n 
1 108 GLY n 
1 109 ASP n 
1 110 HIS n 
1 111 CYS n 
1 112 ILE n 
1 113 ILE n 
1 114 GLY n 
1 115 ARG n 
1 116 THR n 
1 117 LEU n 
1 118 VAL n 
1 119 VAL n 
1 120 HIS n 
1 121 GLU n 
1 122 LYS n 
1 123 ALA n 
1 124 ASP n 
1 125 ASP n 
1 126 LEU n 
1 127 GLY n 
1 128 LYS n 
1 129 GLY n 
1 130 GLY n 
1 131 ASN n 
1 132 GLU n 
1 133 GLU n 
1 134 SER n 
1 135 THR n 
1 136 LYS n 
1 137 THR n 
1 138 GLY n 
1 139 ASN n 
1 140 ALA n 
1 141 GLY n 
1 142 SER n 
1 143 ARG n 
1 144 LEU n 
1 145 ALA n 
1 146 CYS n 
1 147 GLY n 
1 148 VAL n 
1 149 ILE n 
1 150 GLY n 
1 151 ILE n 
1 152 ALA n 
1 153 GLN n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_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 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1  81  Mouse ? Sod1 ? ? ? ? ? ? 'Mus musculus' 10090 ? ? ? ? ? ? ? ? 'Escherichia coli' 469008 ? 
? ? ? ? ? 'BL21(DE3)' ? ? ? ? ? ? ? PLASMID ? ? ? PKA8H ? ? 
1 2 sample 'Biological sequence' 82 153 Human ? SOD1 ? ? ? ? ? ? 'Homo sapiens' 9606  ? ? ? ? ? ? ? ? 'Escherichia coli' 469008 ? 
? ? ? ? ? 'BL21(DE3)' ? ? ? ? ? ? ? PLASMID ? ? ? PKA8H ? ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP SODC_MOUSE P08228 ? 1 
;AMKAVCVLKGDGPVQGTIHFEQKASGEPVVLSGQITGLTEGQHGFHVHQYGDNTQGCTSAGPHFNPHSKKHGGPADEERH

;
2  
2 UNP SODC_HUMAN P00441 ? 1 VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ           82 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1  1 3LTV A 1  ? 80  ? P08228 2  ? 81  ? 1  80  
2  2 3LTV A 81 ? 153 ? P00441 82 ? 154 ? 81 153 
3  1 3LTV B 1  ? 80  ? P08228 2  ? 81  ? 1  80  
4  2 3LTV B 81 ? 153 ? P00441 82 ? 154 ? 81 153 
5  1 3LTV C 1  ? 80  ? P08228 2  ? 81  ? 1  80  
6  2 3LTV C 81 ? 153 ? P00441 82 ? 154 ? 81 153 
7  1 3LTV D 1  ? 80  ? P08228 2  ? 81  ? 1  80  
8  2 3LTV D 81 ? 153 ? P00441 82 ? 154 ? 81 153 
9  1 3LTV E 1  ? 80  ? P08228 2  ? 81  ? 1  80  
10 2 3LTV E 81 ? 153 ? P00441 82 ? 154 ? 81 153 
11 1 3LTV F 1  ? 80  ? P08228 2  ? 81  ? 1  80  
12 2 3LTV F 81 ? 153 ? P00441 82 ? 154 ? 81 153 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
ZN  non-polymer         . 'ZINC ION'      ? 'Zn 2'           65.409  
# 
_exptl.entry_id          3LTV 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.54 
_exptl_crystal.density_percent_sol   51.65 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              4.6 
_exptl_crystal_grow.pdbx_details    '0.1 M SODIUM ACETATE, 25% PEG 4000, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'ADSC QUANTUM 315' 
_diffrn_detector.pdbx_collection_date   2009-02-21 
_diffrn_detector.details                MIRRORS 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    'SINGLE CRYSTAL SIDE-BOUNCE MONOCHROMATOR' 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.979 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'APS BEAMLINE 24-ID-E' 
_diffrn_source.pdbx_synchrotron_site       APS 
_diffrn_source.pdbx_synchrotron_beamline   24-ID-E 
_diffrn_source.pdbx_wavelength             0.979 
_diffrn_source.pdbx_wavelength_list        0.979 
# 
_reflns.entry_id                     3LTV 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             50.000 
_reflns.d_resolution_high            2.450 
_reflns.number_obs                   34238 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         98.7 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              0.10300 
_reflns.pdbx_netI_over_sigmaI        14.5000 
_reflns.B_iso_Wilson_estimate        38.4 
_reflns.pdbx_redundancy              5.000 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
_reflns_shell.d_res_high             2.45 
_reflns_shell.d_res_low              2.54 
_reflns_shell.percent_possible_all   99.7 
_reflns_shell.Rmerge_I_obs           ? 
_reflns_shell.pdbx_Rsym_value        0.55000 
_reflns_shell.meanI_over_sigI_obs    3.300 
_reflns_shell.pdbx_redundancy        5.00 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      ? 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_diffrn_id         ? 
_reflns_shell.pdbx_ordinal           1 
# 
_refine.entry_id                                 3LTV 
_refine.ls_number_reflns_obs                     34219 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             37.557 
_refine.ls_d_res_high                            2.453 
_refine.ls_percent_reflns_obs                    98.63 
_refine.ls_R_factor_obs                          0.1988 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1953 
_refine.ls_R_factor_R_free                       0.2649 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.04 
_refine.ls_number_reflns_R_free                  1724 
_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                               46.8 
_refine.aniso_B[1][1]                            2.3397 
_refine.aniso_B[2][2]                            2.3397 
_refine.aniso_B[3][3]                            -4.2956 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.0000 
_refine.aniso_B[2][3]                            0.0000 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_ksol                 0.355 
_refine.solvent_model_param_bsol                 36.425 
_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               THROUGHOUT 
_refine.details                                  ? 
_refine.pdbx_starting_model                      2VR7 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             Isotropic 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.37 
_refine.overall_SU_B                             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        6591 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         6 
_refine_hist.number_atoms_solvent             145 
_refine_hist.number_atoms_total               6742 
_refine_hist.d_res_high                       2.453 
_refine_hist.d_res_low                        37.557 
# 
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           0.009  ? ? 6704 'X-RAY DIFFRACTION' ? 
f_angle_d          1.178  ? ? 9046 'X-RAY DIFFRACTION' ? 
f_dihedral_angle_d 19.391 ? ? 2381 'X-RAY DIFFRACTION' ? 
f_chiral_restr     0.075  ? ? 1000 'X-RAY DIFFRACTION' ? 
f_plane_restr      0.004  ? ? 1235 'X-RAY DIFFRACTION' ? 
# 
loop_
_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 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
. 2.4531 2.5253  2610 0.2374 97.00  0.3001 . . 163 . . . . 'X-RAY DIFFRACTION' 
. 2.5253 2.6068  2738 0.2446 100.00 0.3373 . . 138 . . . . 'X-RAY DIFFRACTION' 
. 2.6068 2.6999  2704 0.2462 99.00  0.3591 . . 158 . . . . 'X-RAY DIFFRACTION' 
. 2.6999 2.8080  2711 0.2429 99.00  0.3335 . . 149 . . . . 'X-RAY DIFFRACTION' 
. 2.8080 2.9357  2721 0.2320 99.00  0.3142 . . 133 . . . . 'X-RAY DIFFRACTION' 
. 2.9357 3.0904  2736 0.2234 99.00  0.3187 . . 138 . . . . 'X-RAY DIFFRACTION' 
. 3.0904 3.2840  2694 0.2055 99.00  0.2938 . . 143 . . . . 'X-RAY DIFFRACTION' 
. 3.2840 3.5374  2738 0.1894 99.00  0.2428 . . 126 . . . . 'X-RAY DIFFRACTION' 
. 3.5374 3.8930  2712 0.1761 99.00  0.2256 . . 136 . . . . 'X-RAY DIFFRACTION' 
. 3.8930 4.4555  2689 0.1621 98.00  0.2358 . . 151 . . . . 'X-RAY DIFFRACTION' 
. 4.4555 5.6105  2712 0.1674 98.00  0.2139 . . 154 . . . . 'X-RAY DIFFRACTION' 
. 5.6105 37.5614 2730 0.1702 97.00  0.2302 . . 135 . . . . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  3LTV 
_struct.title                     'Mouse-human sod1 chimera' 
_struct.pdbx_descriptor           'Superoxide dismutase [Cu-Zn] (E.C.1.15.1.1)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3LTV 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
_struct_keywords.text            
'OXIDOREDUCTASE, ANTIOXIDANT, METAL-BINDING, AMYOTROPHIC LATERAL SCLEROSIS, DISEASE MUTATION, PHOSPHOPROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 1 ? 
E N N 1 ? 
F N N 1 ? 
G N N 2 ? 
H N N 2 ? 
I N N 2 ? 
J N N 2 ? 
K N N 2 ? 
L N N 2 ? 
M N N 3 ? 
N N N 3 ? 
O N N 3 ? 
P N N 3 ? 
Q N N 3 ? 
R N N 3 ? 
# 
_struct_biol.id   1 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  1  GLN A 55  ? GLY A 61  ? GLN A 55  GLY A 61  5 ? 7 
HELX_P HELX_P2  2  SER A 107 ? CYS A 111 ? SER A 107 CYS A 111 5 ? 5 
HELX_P HELX_P3  3  ASN A 131 ? GLY A 138 ? ASN A 131 GLY A 138 1 ? 8 
HELX_P HELX_P4  4  GLN B 55  ? GLY B 61  ? GLN B 55  GLY B 61  5 ? 7 
HELX_P HELX_P5  5  SER B 107 ? CYS B 111 ? SER B 107 CYS B 111 5 ? 5 
HELX_P HELX_P6  6  ASN B 131 ? GLY B 138 ? ASN B 131 GLY B 138 1 ? 8 
HELX_P HELX_P7  7  GLN C 55  ? GLY C 61  ? GLN C 55  GLY C 61  5 ? 7 
HELX_P HELX_P8  8  SER C 107 ? CYS C 111 ? SER C 107 CYS C 111 5 ? 5 
HELX_P HELX_P9  9  CYS D 57  ? GLY D 61  ? CYS D 57  GLY D 61  5 ? 5 
HELX_P HELX_P10 10 SER D 107 ? CYS D 111 ? SER D 107 CYS D 111 5 ? 5 
HELX_P HELX_P11 11 GLU D 132 ? LYS D 136 ? GLU D 132 LYS D 136 5 ? 5 
HELX_P HELX_P12 12 GLN E 55  ? GLY E 61  ? GLN E 55  GLY E 61  5 ? 7 
HELX_P HELX_P13 13 ASN E 131 ? THR E 137 ? ASN E 131 THR E 137 1 ? 7 
HELX_P HELX_P14 14 GLN F 55  ? GLY F 61  ? GLN F 55  GLY F 61  5 ? 7 
HELX_P HELX_P15 15 SER F 107 ? CYS F 111 ? SER F 107 CYS F 111 5 ? 5 
HELX_P HELX_P16 16 ASN F 131 ? GLY F 138 ? ASN F 131 GLY F 138 1 ? 8 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1  disulf ? ? A CYS 57 SG  ? ? ? 1_555 A CYS 146 SG ? ? A CYS 57 A CYS 146  1_555 ? ? ? ? ? ? ? 2.109 ? 
disulf2  disulf ? ? B CYS 57 SG  ? ? ? 1_555 B CYS 146 SG ? ? B CYS 57 B CYS 146  1_555 ? ? ? ? ? ? ? 2.066 ? 
disulf3  disulf ? ? C CYS 57 SG  ? ? ? 1_555 C CYS 146 SG ? ? C CYS 57 C CYS 146  1_555 ? ? ? ? ? ? ? 2.050 ? 
disulf4  disulf ? ? D CYS 57 SG  ? ? ? 1_555 D CYS 146 SG ? ? D CYS 57 D CYS 146  1_555 ? ? ? ? ? ? ? 2.077 ? 
disulf5  disulf ? ? E CYS 57 SG  ? ? ? 1_555 E CYS 146 SG ? ? E CYS 57 E CYS 146  1_555 ? ? ? ? ? ? ? 2.072 ? 
disulf6  disulf ? ? F CYS 57 SG  ? ? ? 1_555 F CYS 146 SG ? ? F CYS 57 F CYS 146  1_555 ? ? ? ? ? ? ? 2.076 ? 
metalc1  metalc ? ? D HIS 71 ND1 ? ? ? 1_555 J ZN  .   ZN ? ? D HIS 71 D ZN  1001 1_555 ? ? ? ? ? ? ? 1.874 ? 
metalc2  metalc ? ? B ASP 83 OD2 ? ? ? 1_555 H ZN  .   ZN ? ? B ASP 83 B ZN  1001 1_555 ? ? ? ? ? ? ? 1.920 ? 
metalc3  metalc ? ? E HIS 80 ND1 ? ? ? 1_555 K ZN  .   ZN ? ? E HIS 80 E ZN  1001 1_555 ? ? ? ? ? ? ? 1.925 ? 
metalc4  metalc ? ? D HIS 63 ND1 ? ? ? 1_555 J ZN  .   ZN ? ? D HIS 63 D ZN  1001 1_555 ? ? ? ? ? ? ? 1.954 ? 
metalc5  metalc ? ? F HIS 63 ND1 ? ? ? 1_555 L ZN  .   ZN ? ? F HIS 63 F ZN  1001 1_555 ? ? ? ? ? ? ? 1.977 ? 
metalc6  metalc ? ? A ASP 83 OD2 ? ? ? 1_555 G ZN  .   ZN ? ? A ASP 83 A ZN  1001 1_555 ? ? ? ? ? ? ? 1.982 ? 
metalc7  metalc ? ? F ASP 83 OD2 ? ? ? 1_555 L ZN  .   ZN ? ? F ASP 83 F ZN  1001 1_555 ? ? ? ? ? ? ? 2.016 ? 
metalc8  metalc ? ? A HIS 80 ND1 ? ? ? 1_555 G ZN  .   ZN ? ? A HIS 80 A ZN  1001 1_555 ? ? ? ? ? ? ? 2.055 ? 
metalc9  metalc ? ? A HIS 63 ND1 ? ? ? 1_555 G ZN  .   ZN ? ? A HIS 63 A ZN  1001 1_555 ? ? ? ? ? ? ? 2.102 ? 
metalc10 metalc ? ? B HIS 71 ND1 ? ? ? 1_555 H ZN  .   ZN ? ? B HIS 71 B ZN  1001 1_555 ? ? ? ? ? ? ? 2.105 ? 
metalc11 metalc ? ? D ASP 83 OD1 ? ? ? 1_555 J ZN  .   ZN ? ? D ASP 83 D ZN  1001 1_555 ? ? ? ? ? ? ? 2.110 ? 
metalc12 metalc ? ? F HIS 80 ND1 ? ? ? 1_555 L ZN  .   ZN ? ? F HIS 80 F ZN  1001 1_555 ? ? ? ? ? ? ? 2.114 ? 
metalc13 metalc ? ? F HIS 71 ND1 ? ? ? 1_555 L ZN  .   ZN ? ? F HIS 71 F ZN  1001 1_555 ? ? ? ? ? ? ? 2.120 ? 
metalc14 metalc ? ? B HIS 80 ND1 ? ? ? 1_555 H ZN  .   ZN ? ? B HIS 80 B ZN  1001 1_555 ? ? ? ? ? ? ? 2.123 ? 
metalc15 metalc ? ? A HIS 71 ND1 ? ? ? 1_555 G ZN  .   ZN ? ? A HIS 71 A ZN  1001 1_555 ? ? ? ? ? ? ? 2.129 ? 
metalc16 metalc ? ? C HIS 80 ND1 ? ? ? 1_555 I ZN  .   ZN ? ? C HIS 80 C ZN  1001 1_555 ? ? ? ? ? ? ? 2.136 ? 
metalc17 metalc ? ? B HIS 63 ND1 ? ? ? 1_555 H ZN  .   ZN ? ? B HIS 63 B ZN  1001 1_555 ? ? ? ? ? ? ? 2.200 ? 
metalc18 metalc ? ? E HIS 63 ND1 ? ? ? 1_555 K ZN  .   ZN ? ? E HIS 63 E ZN  1001 1_555 ? ? ? ? ? ? ? 2.219 ? 
metalc19 metalc ? ? E ASP 83 OD2 ? ? ? 1_555 K ZN  .   ZN ? ? E ASP 83 E ZN  1001 1_555 ? ? ? ? ? ? ? 2.297 ? 
metalc20 metalc ? ? E HIS 71 ND1 ? ? ? 1_555 K ZN  .   ZN ? ? E HIS 71 E ZN  1001 1_555 ? ? ? ? ? ? ? 2.394 ? 
metalc21 metalc ? ? E ASP 83 OD1 ? ? ? 1_555 K ZN  .   ZN ? ? E ASP 83 E ZN  1001 1_555 ? ? ? ? ? ? ? 2.500 ? 
metalc22 metalc ? ? C HIS 71 ND1 ? ? ? 1_555 I ZN  .   ZN ? ? C HIS 71 C ZN  1001 1_555 ? ? ? ? ? ? ? 2.596 ? 
metalc23 metalc ? ? C ASP 83 OD1 ? ? ? 1_555 I ZN  .   ZN ? ? C ASP 83 C ZN  1001 1_555 ? ? ? ? ? ? ? 2.628 ? 
metalc24 metalc ? ? D HIS 80 ND1 ? ? ? 1_555 J ZN  .   ZN ? ? D HIS 80 D ZN  1001 1_555 ? ? ? ? ? ? ? 2.682 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 5 ? 
B ? 4 ? 
C ? 5 ? 
D ? 4 ? 
E ? 5 ? 
F ? 4 ? 
G ? 5 ? 
H ? 4 ? 
I ? 5 ? 
J ? 4 ? 
K ? 5 ? 
L ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2 ? anti-parallel 
A 2 3 ? anti-parallel 
A 3 4 ? anti-parallel 
A 4 5 ? anti-parallel 
B 1 2 ? anti-parallel 
B 2 3 ? anti-parallel 
B 3 4 ? anti-parallel 
C 1 2 ? anti-parallel 
C 2 3 ? anti-parallel 
C 3 4 ? anti-parallel 
C 4 5 ? anti-parallel 
D 1 2 ? anti-parallel 
D 2 3 ? anti-parallel 
D 3 4 ? anti-parallel 
E 1 2 ? anti-parallel 
E 2 3 ? anti-parallel 
E 3 4 ? anti-parallel 
E 4 5 ? anti-parallel 
F 1 2 ? anti-parallel 
F 2 3 ? anti-parallel 
F 3 4 ? anti-parallel 
G 1 2 ? anti-parallel 
G 2 3 ? anti-parallel 
G 3 4 ? anti-parallel 
G 4 5 ? anti-parallel 
H 1 2 ? anti-parallel 
H 2 3 ? anti-parallel 
H 3 4 ? anti-parallel 
I 1 2 ? anti-parallel 
I 2 3 ? anti-parallel 
I 3 4 ? anti-parallel 
I 4 5 ? anti-parallel 
J 1 2 ? anti-parallel 
J 2 3 ? anti-parallel 
J 3 4 ? anti-parallel 
K 1 2 ? anti-parallel 
K 2 3 ? anti-parallel 
K 3 4 ? anti-parallel 
K 4 5 ? anti-parallel 
L 1 2 ? anti-parallel 
L 2 3 ? anti-parallel 
L 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1 ALA A 95  ? ASP A 101 ? ALA A 95  ASP A 101 
A 2 VAL A 29  ? THR A 36  ? VAL A 29  THR A 36  
A 3 GLN A 15  ? GLN A 22  ? GLN A 15  GLN A 22  
A 4 MET A 2   ? LYS A 9   ? MET A 2   LYS A 9   
A 5 GLY A 150 ? ILE A 151 ? GLY A 150 ILE A 151 
B 1 ASP A 83  ? ALA A 89  ? ASP A 83  ALA A 89  
B 2 GLY A 41  ? HIS A 48  ? GLY A 41  HIS A 48  
B 3 THR A 116 ? HIS A 120 ? THR A 116 HIS A 120 
B 4 ARG A 143 ? VAL A 148 ? ARG A 143 VAL A 148 
C 1 ALA B 95  ? ASP B 101 ? ALA B 95  ASP B 101 
C 2 VAL B 29  ? THR B 36  ? VAL B 29  THR B 36  
C 3 GLN B 15  ? GLN B 22  ? GLN B 15  GLN B 22  
C 4 MET B 2   ? LYS B 9   ? MET B 2   LYS B 9   
C 5 GLY B 150 ? ILE B 151 ? GLY B 150 ILE B 151 
D 1 ASP B 83  ? ALA B 89  ? ASP B 83  ALA B 89  
D 2 GLY B 41  ? HIS B 48  ? GLY B 41  HIS B 48  
D 3 THR B 116 ? HIS B 120 ? THR B 116 HIS B 120 
D 4 ARG B 143 ? VAL B 148 ? ARG B 143 VAL B 148 
E 1 VAL C 97  ? ASP C 101 ? VAL C 97  ASP C 101 
E 2 VAL C 29  ? THR C 36  ? VAL C 29  THR C 36  
E 3 GLN C 15  ? GLN C 22  ? GLN C 15  GLN C 22  
E 4 MET C 2   ? LEU C 8   ? MET C 2   LEU C 8   
E 5 GLY C 150 ? ILE C 151 ? GLY C 150 ILE C 151 
F 1 ASP C 83  ? ALA C 89  ? ASP C 83  ALA C 89  
F 2 GLY C 41  ? HIS C 48  ? GLY C 41  HIS C 48  
F 3 THR C 116 ? HIS C 120 ? THR C 116 HIS C 120 
F 4 ARG C 143 ? VAL C 148 ? ARG C 143 VAL C 148 
G 1 ALA D 95  ? ASP D 101 ? ALA D 95  ASP D 101 
G 2 VAL D 29  ? THR D 36  ? VAL D 29  THR D 36  
G 3 GLN D 15  ? GLN D 22  ? GLN D 15  GLN D 22  
G 4 MET D 2   ? LEU D 8   ? MET D 2   LEU D 8   
G 5 GLY D 150 ? ILE D 151 ? GLY D 150 ILE D 151 
H 1 ASN D 86  ? ALA D 89  ? ASN D 86  ALA D 89  
H 2 GLY D 41  ? HIS D 48  ? GLY D 41  HIS D 48  
H 3 THR D 116 ? HIS D 120 ? THR D 116 HIS D 120 
H 4 ARG D 143 ? VAL D 148 ? ARG D 143 VAL D 148 
I 1 ALA E 95  ? ASP E 101 ? ALA E 95  ASP E 101 
I 2 VAL E 29  ? THR E 36  ? VAL E 29  THR E 36  
I 3 GLN E 15  ? GLN E 22  ? GLN E 15  GLN E 22  
I 4 MET E 2   ? LEU E 8   ? MET E 2   LEU E 8   
I 5 GLY E 150 ? ILE E 151 ? GLY E 150 ILE E 151 
J 1 ASP E 83  ? ALA E 89  ? ASP E 83  ALA E 89  
J 2 GLY E 41  ? HIS E 48  ? GLY E 41  HIS E 48  
J 3 THR E 116 ? HIS E 120 ? THR E 116 HIS E 120 
J 4 ARG E 143 ? VAL E 148 ? ARG E 143 VAL E 148 
K 1 ALA F 95  ? ASP F 101 ? ALA F 95  ASP F 101 
K 2 VAL F 29  ? THR F 36  ? VAL F 29  THR F 36  
K 3 GLN F 15  ? GLN F 22  ? GLN F 15  GLN F 22  
K 4 MET F 2   ? LYS F 9   ? MET F 2   LYS F 9   
K 5 GLY F 150 ? ILE F 151 ? GLY F 150 ILE F 151 
L 1 ASP F 83  ? ALA F 89  ? ASP F 83  ALA F 89  
L 2 GLY F 41  ? HIS F 48  ? GLY F 41  HIS F 48  
L 3 THR F 116 ? HIS F 120 ? THR F 116 HIS F 120 
L 4 ARG F 143 ? VAL F 148 ? ARG F 143 VAL F 148 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2 O ILE A 99  ? O ILE A 99  N LEU A 31  ? N LEU A 31  
A 2 3 O VAL A 30  ? O VAL A 30  N GLU A 21  ? N GLU A 21  
A 3 4 O PHE A 20  ? O PHE A 20  N ALA A 4   ? N ALA A 4   
A 4 5 N VAL A 5   ? N VAL A 5   O GLY A 150 ? O GLY A 150 
B 1 2 O ALA A 89  ? O ALA A 89  N GLY A 41  ? N GLY A 41  
B 2 3 N HIS A 48  ? N HIS A 48  O THR A 116 ? O THR A 116 
B 3 4 N LEU A 117 ? N LEU A 117 O GLY A 147 ? O GLY A 147 
C 1 2 O ASP B 101 ? O ASP B 101 N VAL B 29  ? N VAL B 29  
C 2 3 O SER B 32  ? O SER B 32  N HIS B 19  ? N HIS B 19  
C 3 4 O GLY B 16  ? O GLY B 16  N LEU B 8   ? N LEU B 8   
C 4 5 N VAL B 5   ? N VAL B 5   O GLY B 150 ? O GLY B 150 
D 1 2 O ALA B 89  ? O ALA B 89  N GLY B 41  ? N GLY B 41  
D 2 3 N HIS B 48  ? N HIS B 48  O THR B 116 ? O THR B 116 
D 3 4 N VAL B 119 ? N VAL B 119 O ALA B 145 ? O ALA B 145 
E 1 2 O ILE C 99  ? O ILE C 99  N LEU C 31  ? N LEU C 31  
E 2 3 O SER C 32  ? O SER C 32  N HIS C 19  ? N HIS C 19  
E 3 4 O GLY C 16  ? O GLY C 16  N LEU C 8   ? N LEU C 8   
E 4 5 N VAL C 5   ? N VAL C 5   O GLY C 150 ? O GLY C 150 
F 1 2 O ALA C 89  ? O ALA C 89  N GLY C 41  ? N GLY C 41  
F 2 3 N HIS C 46  ? N HIS C 46  O VAL C 118 ? O VAL C 118 
F 3 4 N LEU C 117 ? N LEU C 117 O GLY C 147 ? O GLY C 147 
G 1 2 O ALA D 95  ? O ALA D 95  N ILE D 35  ? N ILE D 35  
G 2 3 O THR D 36  ? O THR D 36  N GLN D 15  ? N GLN D 15  
G 3 4 O GLN D 22  ? O GLN D 22  N MET D 2   ? N MET D 2   
G 4 5 N VAL D 5   ? N VAL D 5   O GLY D 150 ? O GLY D 150 
H 1 2 O ALA D 89  ? O ALA D 89  N GLY D 41  ? N GLY D 41  
H 2 3 N HIS D 48  ? N HIS D 48  O THR D 116 ? O THR D 116 
H 3 4 N LEU D 117 ? N LEU D 117 O GLY D 147 ? O GLY D 147 
I 1 2 O ASP E 101 ? O ASP E 101 N VAL E 29  ? N VAL E 29  
I 2 3 O VAL E 30  ? O VAL E 30  N GLU E 21  ? N GLU E 21  
I 3 4 O PHE E 20  ? O PHE E 20  N ALA E 4   ? N ALA E 4   
I 4 5 N VAL E 5   ? N VAL E 5   O GLY E 150 ? O GLY E 150 
J 1 2 O ALA E 89  ? O ALA E 89  N GLY E 41  ? N GLY E 41  
J 2 3 N HIS E 46  ? N HIS E 46  O VAL E 118 ? O VAL E 118 
J 3 4 N LEU E 117 ? N LEU E 117 O GLY E 147 ? O GLY E 147 
K 1 2 O ILE F 99  ? O ILE F 99  N LEU F 31  ? N LEU F 31  
K 2 3 O SER F 32  ? O SER F 32  N HIS F 19  ? N HIS F 19  
K 3 4 O PHE F 20  ? O PHE F 20  N ALA F 4   ? N ALA F 4   
K 4 5 N VAL F 5   ? N VAL F 5   O GLY F 150 ? O GLY F 150 
L 1 2 O ALA F 89  ? O ALA F 89  N GLY F 41  ? N GLY F 41  
L 2 3 N HIS F 48  ? N HIS F 48  O THR F 116 ? O THR F 116 
L 3 4 N VAL F 119 ? N VAL F 119 O ALA F 145 ? O ALA F 145 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN A 1001' 
AC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN B 1001' 
AC3 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN C 1001' 
AC4 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN D 1001' 
AC5 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN E 1001' 
AC6 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN F 1001' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 4 HIS A 63 ? HIS A 63 . ? 1_555 ? 
2  AC1 4 HIS A 71 ? HIS A 71 . ? 1_555 ? 
3  AC1 4 HIS A 80 ? HIS A 80 . ? 1_555 ? 
4  AC1 4 ASP A 83 ? ASP A 83 . ? 1_555 ? 
5  AC2 4 HIS B 63 ? HIS B 63 . ? 1_555 ? 
6  AC2 4 HIS B 71 ? HIS B 71 . ? 1_555 ? 
7  AC2 4 HIS B 80 ? HIS B 80 . ? 1_555 ? 
8  AC2 4 ASP B 83 ? ASP B 83 . ? 1_555 ? 
9  AC3 4 HIS C 63 ? HIS C 63 . ? 1_555 ? 
10 AC3 4 HIS C 71 ? HIS C 71 . ? 1_555 ? 
11 AC3 4 HIS C 80 ? HIS C 80 . ? 1_555 ? 
12 AC3 4 ASP C 83 ? ASP C 83 . ? 1_555 ? 
13 AC4 4 HIS D 63 ? HIS D 63 . ? 1_555 ? 
14 AC4 4 HIS D 71 ? HIS D 71 . ? 1_555 ? 
15 AC4 4 HIS D 80 ? HIS D 80 . ? 1_555 ? 
16 AC4 4 ASP D 83 ? ASP D 83 . ? 1_555 ? 
17 AC5 4 HIS E 63 ? HIS E 63 . ? 1_555 ? 
18 AC5 4 HIS E 71 ? HIS E 71 . ? 1_555 ? 
19 AC5 4 HIS E 80 ? HIS E 80 . ? 1_555 ? 
20 AC5 4 ASP E 83 ? ASP E 83 . ? 1_555 ? 
21 AC6 4 HIS F 63 ? HIS F 63 . ? 1_555 ? 
22 AC6 4 HIS F 71 ? HIS F 71 . ? 1_555 ? 
23 AC6 4 HIS F 80 ? HIS F 80 . ? 1_555 ? 
24 AC6 4 ASP F 83 ? ASP F 83 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          3LTV 
_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                    3LTV 
_atom_sites.fract_transf_matrix[1][1]   0.007844 
_atom_sites.fract_transf_matrix[1][2]   0.004529 
_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]   0.009058 
_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]   0.009757 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ALA A 1 1   ? -16.411 39.026  -13.831 1.00 41.37  ? 1    ALA A N   1 
ATOM   2    C  CA  . ALA A 1 1   ? -16.734 38.951  -12.404 1.00 52.96  ? 1    ALA A CA  1 
ATOM   3    C  C   . ALA A 1 1   ? -16.000 40.027  -11.599 1.00 50.09  ? 1    ALA A C   1 
ATOM   4    O  O   . ALA A 1 1   ? -14.815 40.286  -11.822 1.00 50.47  ? 1    ALA A O   1 
ATOM   5    C  CB  . ALA A 1 1   ? -16.413 37.575  -11.848 1.00 40.92  ? 1    ALA A CB  1 
ATOM   6    N  N   . MET A 1 2   ? -16.713 40.645  -10.663 1.00 44.75  ? 2    MET A N   1 
ATOM   7    C  CA  . MET A 1 2   ? -16.147 41.709  -9.840  1.00 36.74  ? 2    MET A CA  1 
ATOM   8    C  C   . MET A 1 2   ? -16.155 41.328  -8.362  1.00 32.56  ? 2    MET A C   1 
ATOM   9    O  O   . MET A 1 2   ? -17.111 40.738  -7.864  1.00 34.78  ? 2    MET A O   1 
ATOM   10   C  CB  . MET A 1 2   ? -16.920 43.010  -10.063 1.00 34.52  ? 2    MET A CB  1 
ATOM   11   C  CG  . MET A 1 2   ? -16.706 43.635  -11.434 1.00 43.02  ? 2    MET A CG  1 
ATOM   12   S  SD  . MET A 1 2   ? -18.189 44.418  -12.141 1.00 64.43  ? 2    MET A SD  1 
ATOM   13   C  CE  . MET A 1 2   ? -19.144 43.009  -12.714 1.00 42.51  ? 2    MET A CE  1 
ATOM   14   N  N   . LYS A 1 3   ? -15.078 41.676  -7.669  1.00 31.75  ? 3    LYS A N   1 
ATOM   15   C  CA  . LYS A 1 3   ? -14.972 41.443  -6.241  1.00 28.59  ? 3    LYS A CA  1 
ATOM   16   C  C   . LYS A 1 3   ? -14.486 42.678  -5.468  1.00 32.64  ? 3    LYS A C   1 
ATOM   17   O  O   . LYS A 1 3   ? -13.682 43.476  -5.954  1.00 28.77  ? 3    LYS A O   1 
ATOM   18   C  CB  . LYS A 1 3   ? -14.060 40.248  -5.967  1.00 33.01  ? 3    LYS A CB  1 
ATOM   19   C  CG  . LYS A 1 3   ? -14.720 38.917  -6.278  1.00 37.12  ? 3    LYS A CG  1 
ATOM   20   C  CD  . LYS A 1 3   ? -13.779 37.750  -6.146  1.00 44.94  ? 3    LYS A CD  1 
ATOM   21   C  CE  . LYS A 1 3   ? -14.560 36.442  -6.219  1.00 57.56  ? 3    LYS A CE  1 
ATOM   22   N  NZ  . LYS A 1 3   ? -13.667 35.233  -6.228  1.00 63.48  ? 3    LYS A NZ  1 
ATOM   23   N  N   . ALA A 1 4   ? -14.974 42.823  -4.241  1.00 30.79  ? 4    ALA A N   1 
ATOM   24   C  CA  . ALA A 1 4   ? -14.621 43.974  -3.431  1.00 27.83  ? 4    ALA A CA  1 
ATOM   25   C  C   . ALA A 1 4   ? -14.576 43.573  -1.979  1.00 29.14  ? 4    ALA A C   1 
ATOM   26   O  O   . ALA A 1 4   ? -15.176 42.584  -1.562  1.00 29.93  ? 4    ALA A O   1 
ATOM   27   C  CB  . ALA A 1 4   ? -15.613 45.103  -3.648  1.00 25.75  ? 4    ALA A CB  1 
ATOM   28   N  N   . VAL A 1 5   ? -13.857 44.348  -1.197  1.00 28.24  ? 5    VAL A N   1 
ATOM   29   C  CA  . VAL A 1 5   ? -13.771 44.057  0.207   1.00 22.80  ? 5    VAL A CA  1 
ATOM   30   C  C   . VAL A 1 5   ? -13.715 45.344  1.034   1.00 26.41  ? 5    VAL A C   1 
ATOM   31   O  O   . VAL A 1 5   ? -13.290 46.402  0.557   1.00 23.91  ? 5    VAL A O   1 
ATOM   32   C  CB  . VAL A 1 5   ? -12.599 43.116  0.505   1.00 25.75  ? 5    VAL A CB  1 
ATOM   33   C  CG1 . VAL A 1 5   ? -11.283 43.771  0.169   1.00 25.96  ? 5    VAL A CG1 1 
ATOM   34   C  CG2 . VAL A 1 5   ? -12.638 42.665  1.981   1.00 30.69  ? 5    VAL A CG2 1 
ATOM   35   N  N   . CYS A 1 6   ? -14.179 45.247  2.275   1.00 28.38  ? 6    CYS A N   1 
ATOM   36   C  CA  . CYS A 1 6   ? -14.253 46.390  3.166   1.00 24.74  ? 6    CYS A CA  1 
ATOM   37   C  C   . CYS A 1 6   ? -13.918 45.964  4.586   1.00 27.23  ? 6    CYS A C   1 
ATOM   38   O  O   . CYS A 1 6   ? -14.550 45.072  5.156   1.00 30.41  ? 6    CYS A O   1 
ATOM   39   C  CB  . CYS A 1 6   ? -15.651 47.003  3.121   1.00 25.10  ? 6    CYS A CB  1 
ATOM   40   S  SG  . CYS A 1 6   ? -15.852 48.536  4.080   1.00 27.68  ? 6    CYS A SG  1 
ATOM   41   N  N   . VAL A 1 7   ? -12.901 46.593  5.147   1.00 26.19  ? 7    VAL A N   1 
ATOM   42   C  CA  . VAL A 1 7   ? -12.545 46.378  6.532   1.00 29.25  ? 7    VAL A CA  1 
ATOM   43   C  C   . VAL A 1 7   ? -13.172 47.497  7.367   1.00 29.18  ? 7    VAL A C   1 
ATOM   44   O  O   . VAL A 1 7   ? -12.870 48.671  7.177   1.00 28.90  ? 7    VAL A O   1 
ATOM   45   C  CB  . VAL A 1 7   ? -11.014 46.379  6.687   1.00 32.27  ? 7    VAL A CB  1 
ATOM   46   C  CG1 . VAL A 1 7   ? -10.606 46.290  8.170   1.00 26.73  ? 7    VAL A CG1 1 
ATOM   47   C  CG2 . VAL A 1 7   ? -10.410 45.246  5.856   1.00 30.14  ? 7    VAL A CG2 1 
ATOM   48   N  N   . LEU A 1 8   ? -14.072 47.136  8.267   1.00 29.17  ? 8    LEU A N   1 
ATOM   49   C  CA  . LEU A 1 8   ? -14.747 48.130  9.091   1.00 28.24  ? 8    LEU A CA  1 
ATOM   50   C  C   . LEU A 1 8   ? -14.005 48.315  10.417  1.00 27.75  ? 8    LEU A C   1 
ATOM   51   O  O   . LEU A 1 8   ? -13.898 47.380  11.203  1.00 28.79  ? 8    LEU A O   1 
ATOM   52   C  CB  . LEU A 1 8   ? -16.193 47.694  9.354   1.00 26.74  ? 8    LEU A CB  1 
ATOM   53   C  CG  . LEU A 1 8   ? -17.107 47.474  8.140   1.00 29.90  ? 8    LEU A CG  1 
ATOM   54   C  CD1 . LEU A 1 8   ? -18.325 46.572  8.438   1.00 29.58  ? 8    LEU A CD1 1 
ATOM   55   C  CD2 . LEU A 1 8   ? -17.586 48.799  7.599   1.00 25.75  ? 8    LEU A CD2 1 
ATOM   56   N  N   . LYS A 1 9   ? -13.476 49.512  10.651  1.00 29.69  ? 9    LYS A N   1 
ATOM   57   C  CA  . LYS A 1 9   ? -12.946 49.878  11.962  1.00 27.99  ? 9    LYS A CA  1 
ATOM   58   C  C   . LYS A 1 9   ? -13.725 51.054  12.587  1.00 29.78  ? 9    LYS A C   1 
ATOM   59   O  O   . LYS A 1 9   ? -14.293 51.896  11.895  1.00 29.24  ? 9    LYS A O   1 
ATOM   60   C  CB  . LYS A 1 9   ? -11.460 50.229  11.877  1.00 27.66  ? 9    LYS A CB  1 
ATOM   61   C  CG  . LYS A 1 9   ? -10.606 49.293  11.018  1.00 33.49  ? 9    LYS A CG  1 
ATOM   62   C  CD  . LYS A 1 9   ? -10.666 47.819  11.455  1.00 43.22  ? 9    LYS A CD  1 
ATOM   63   C  CE  . LYS A 1 9   ? -9.941  47.540  12.787  1.00 52.48  ? 9    LYS A CE  1 
ATOM   64   N  NZ  . LYS A 1 9   ? -10.249 46.166  13.342  1.00 48.30  ? 9    LYS A NZ  1 
ATOM   65   N  N   . GLY A 1 10  ? -13.749 51.116  13.908  1.00 35.17  ? 10   GLY A N   1 
ATOM   66   C  CA  . GLY A 1 10  ? -14.407 52.213  14.586  1.00 34.67  ? 10   GLY A CA  1 
ATOM   67   C  C   . GLY A 1 10  ? -13.553 52.677  15.737  1.00 36.84  ? 10   GLY A C   1 
ATOM   68   O  O   . GLY A 1 10  ? -12.481 52.126  15.969  1.00 42.88  ? 10   GLY A O   1 
ATOM   69   N  N   . ASP A 1 11  ? -14.020 53.686  16.462  1.00 36.13  ? 11   ASP A N   1 
ATOM   70   C  CA  . ASP A 1 11  ? -13.325 54.135  17.659  1.00 35.71  ? 11   ASP A CA  1 
ATOM   71   C  C   . ASP A 1 11  ? -13.737 53.334  18.888  1.00 37.63  ? 11   ASP A C   1 
ATOM   72   O  O   . ASP A 1 11  ? -13.055 53.367  19.910  1.00 39.23  ? 11   ASP A O   1 
ATOM   73   C  CB  . ASP A 1 11  ? -13.569 55.624  17.874  1.00 39.58  ? 11   ASP A CB  1 
ATOM   74   C  CG  . ASP A 1 11  ? -12.953 56.470  16.772  1.00 46.63  ? 11   ASP A CG  1 
ATOM   75   O  OD1 . ASP A 1 11  ? -11.709 56.453  16.650  1.00 44.73  ? 11   ASP A OD1 1 
ATOM   76   O  OD2 . ASP A 1 11  ? -13.707 57.140  16.022  1.00 51.06  ? 11   ASP A OD2 1 
ATOM   77   N  N   . GLY A 1 12  ? -14.851 52.610  18.781  1.00 32.88  ? 12   GLY A N   1 
ATOM   78   C  CA  . GLY A 1 12  ? -15.363 51.809  19.870  1.00 28.90  ? 12   GLY A CA  1 
ATOM   79   C  C   . GLY A 1 12  ? -15.000 50.361  19.671  1.00 30.67  ? 12   GLY A C   1 
ATOM   80   O  O   . GLY A 1 12  ? -14.020 50.067  19.020  1.00 34.49  ? 12   GLY A O   1 
ATOM   81   N  N   . PRO A 1 13  ? -15.807 49.445  20.213  1.00 29.99  ? 13   PRO A N   1 
ATOM   82   C  CA  . PRO A 1 13  ? -15.505 48.015  20.140  1.00 29.09  ? 13   PRO A CA  1 
ATOM   83   C  C   . PRO A 1 13  ? -15.901 47.337  18.818  1.00 32.14  ? 13   PRO A C   1 
ATOM   84   O  O   . PRO A 1 13  ? -15.657 46.135  18.672  1.00 30.27  ? 13   PRO A O   1 
ATOM   85   C  CB  . PRO A 1 13  ? -16.374 47.441  21.250  1.00 25.90  ? 13   PRO A CB  1 
ATOM   86   C  CG  . PRO A 1 13  ? -17.601 48.284  21.200  1.00 24.25  ? 13   PRO A CG  1 
ATOM   87   C  CD  . PRO A 1 13  ? -17.097 49.700  20.882  1.00 29.59  ? 13   PRO A CD  1 
ATOM   88   N  N   . VAL A 1 14  ? -16.517 48.057  17.885  1.00 31.21  ? 14   VAL A N   1 
ATOM   89   C  CA  . VAL A 1 14  ? -17.045 47.383  16.690  1.00 30.10  ? 14   VAL A CA  1 
ATOM   90   C  C   . VAL A 1 14  ? -15.986 47.282  15.597  1.00 28.10  ? 14   VAL A C   1 
ATOM   91   O  O   . VAL A 1 14  ? -15.310 48.261  15.297  1.00 32.55  ? 14   VAL A O   1 
ATOM   92   C  CB  . VAL A 1 14  ? -18.324 48.086  16.141  1.00 28.47  ? 14   VAL A CB  1 
ATOM   93   C  CG1 . VAL A 1 14  ? -18.781 47.455  14.840  1.00 21.91  ? 14   VAL A CG1 1 
ATOM   94   C  CG2 . VAL A 1 14  ? -19.451 48.075  17.199  1.00 25.88  ? 14   VAL A CG2 1 
ATOM   95   N  N   . GLN A 1 15  ? -15.820 46.084  15.041  1.00 28.22  ? 15   GLN A N   1 
ATOM   96   C  CA  . GLN A 1 15  ? -15.009 45.890  13.843  1.00 30.91  ? 15   GLN A CA  1 
ATOM   97   C  C   . GLN A 1 15  ? -15.556 44.759  12.978  1.00 28.58  ? 15   GLN A C   1 
ATOM   98   O  O   . GLN A 1 15  ? -16.344 43.941  13.439  1.00 28.71  ? 15   GLN A O   1 
ATOM   99   C  CB  . GLN A 1 15  ? -13.559 45.609  14.208  1.00 35.93  ? 15   GLN A CB  1 
ATOM   100  C  CG  . GLN A 1 15  ? -13.373 44.373  15.053  1.00 40.07  ? 15   GLN A CG  1 
ATOM   101  C  CD  . GLN A 1 15  ? -11.966 44.270  15.601  1.00 50.88  ? 15   GLN A CD  1 
ATOM   102  O  OE1 . GLN A 1 15  ? -11.715 44.593  16.770  1.00 53.92  ? 15   GLN A OE1 1 
ATOM   103  N  NE2 . GLN A 1 15  ? -11.034 43.830  14.757  1.00 57.98  ? 15   GLN A NE2 1 
ATOM   104  N  N   . GLY A 1 16  ? -15.148 44.722  11.718  1.00 27.49  ? 16   GLY A N   1 
ATOM   105  C  CA  . GLY A 1 16  ? -15.639 43.699  10.817  1.00 27.58  ? 16   GLY A CA  1 
ATOM   106  C  C   . GLY A 1 16  ? -15.001 43.692  9.442   1.00 26.11  ? 16   GLY A C   1 
ATOM   107  O  O   . GLY A 1 16  ? -14.219 44.579  9.068   1.00 27.82  ? 16   GLY A O   1 
ATOM   108  N  N   . THR A 1 17  ? -15.334 42.663  8.687   1.00 25.20  ? 17   THR A N   1 
ATOM   109  C  CA  . THR A 1 17  ? -14.858 42.521  7.324   1.00 25.86  ? 17   THR A CA  1 
ATOM   110  C  C   . THR A 1 17  ? -15.998 42.072  6.437   1.00 28.68  ? 17   THR A C   1 
ATOM   111  O  O   . THR A 1 17  ? -16.688 41.087  6.732   1.00 29.88  ? 17   THR A O   1 
ATOM   112  C  CB  . THR A 1 17  ? -13.722 41.497  7.198   1.00 28.16  ? 17   THR A CB  1 
ATOM   113  O  OG1 . THR A 1 17  ? -12.560 41.969  7.891   1.00 23.22  ? 17   THR A OG1 1 
ATOM   114  C  CG2 . THR A 1 17  ? -13.358 41.286  5.711   1.00 29.99  ? 17   THR A CG2 1 
ATOM   115  N  N   . ILE A 1 18  ? -16.194 42.801  5.348   1.00 27.21  ? 18   ILE A N   1 
ATOM   116  C  CA  . ILE A 1 18  ? -17.278 42.508  4.431   1.00 26.53  ? 18   ILE A CA  1 
ATOM   117  C  C   . ILE A 1 18  ? -16.768 42.254  3.025   1.00 29.21  ? 18   ILE A C   1 
ATOM   118  O  O   . ILE A 1 18  ? -15.983 43.042  2.483   1.00 29.87  ? 18   ILE A O   1 
ATOM   119  C  CB  . ILE A 1 18  ? -18.303 43.654  4.416   1.00 25.81  ? 18   ILE A CB  1 
ATOM   120  C  CG1 . ILE A 1 18  ? -18.797 43.946  5.853   1.00 25.13  ? 18   ILE A CG1 1 
ATOM   121  C  CG2 . ILE A 1 18  ? -19.420 43.331  3.461   1.00 22.57  ? 18   ILE A CG2 1 
ATOM   122  C  CD1 . ILE A 1 18  ? -19.926 43.040  6.341   1.00 26.43  ? 18   ILE A CD1 1 
ATOM   123  N  N   . HIS A 1 19  ? -17.212 41.145  2.438   1.00 30.00  ? 19   HIS A N   1 
ATOM   124  C  CA  . HIS A 1 19  ? -16.835 40.786  1.073   1.00 29.90  ? 19   HIS A CA  1 
ATOM   125  C  C   . HIS A 1 19  ? -17.990 40.987  0.105   1.00 29.24  ? 19   HIS A C   1 
ATOM   126  O  O   . HIS A 1 19  ? -19.134 40.657  0.427   1.00 31.97  ? 19   HIS A O   1 
ATOM   127  C  CB  . HIS A 1 19  ? -16.377 39.335  1.030   1.00 32.33  ? 19   HIS A CB  1 
ATOM   128  C  CG  . HIS A 1 19  ? -15.119 39.083  1.793   1.00 33.10  ? 19   HIS A CG  1 
ATOM   129  N  ND1 . HIS A 1 19  ? -13.868 39.306  1.256   1.00 30.85  ? 19   HIS A ND1 1 
ATOM   130  C  CD2 . HIS A 1 19  ? -14.918 38.634  3.054   1.00 28.93  ? 19   HIS A CD2 1 
ATOM   131  C  CE1 . HIS A 1 19  ? -12.949 38.999  2.154   1.00 31.08  ? 19   HIS A CE1 1 
ATOM   132  N  NE2 . HIS A 1 19  ? -13.560 38.590  3.251   1.00 34.86  ? 19   HIS A NE2 1 
ATOM   133  N  N   . PHE A 1 20  ? -17.686 41.517  -1.077  1.00 27.93  ? 20   PHE A N   1 
ATOM   134  C  CA  . PHE A 1 20  ? -18.701 41.812  -2.087  1.00 26.29  ? 20   PHE A CA  1 
ATOM   135  C  C   . PHE A 1 20  ? -18.413 41.014  -3.340  1.00 30.42  ? 20   PHE A C   1 
ATOM   136  O  O   . PHE A 1 20  ? -17.260 40.938  -3.781  1.00 27.44  ? 20   PHE A O   1 
ATOM   137  C  CB  . PHE A 1 20  ? -18.662 43.279  -2.506  1.00 26.87  ? 20   PHE A CB  1 
ATOM   138  C  CG  . PHE A 1 20  ? -18.834 44.250  -1.390  1.00 25.73  ? 20   PHE A CG  1 
ATOM   139  C  CD1 . PHE A 1 20  ? -20.036 44.905  -1.210  1.00 29.88  ? 20   PHE A CD1 1 
ATOM   140  C  CD2 . PHE A 1 20  ? -17.786 44.543  -0.540  1.00 27.88  ? 20   PHE A CD2 1 
ATOM   141  C  CE1 . PHE A 1 20  ? -20.201 45.826  -0.172  1.00 31.05  ? 20   PHE A CE1 1 
ATOM   142  C  CE2 . PHE A 1 20  ? -17.933 45.459  0.492   1.00 28.32  ? 20   PHE A CE2 1 
ATOM   143  C  CZ  . PHE A 1 20  ? -19.141 46.109  0.678   1.00 27.45  ? 20   PHE A CZ  1 
ATOM   144  N  N   . GLU A 1 21  ? -19.456 40.452  -3.944  1.00 32.68  ? 21   GLU A N   1 
ATOM   145  C  CA  . GLU A 1 21  ? -19.274 39.760  -5.215  1.00 32.77  ? 21   GLU A CA  1 
ATOM   146  C  C   . GLU A 1 21  ? -20.406 40.036  -6.205  1.00 32.48  ? 21   GLU A C   1 
ATOM   147  O  O   . GLU A 1 21  ? -21.580 39.946  -5.857  1.00 29.76  ? 21   GLU A O   1 
ATOM   148  C  CB  . GLU A 1 21  ? -19.083 38.257  -5.002  1.00 32.61  ? 21   GLU A CB  1 
ATOM   149  C  CG  . GLU A 1 21  ? -18.855 37.510  -6.309  1.00 43.82  ? 21   GLU A CG  1 
ATOM   150  C  CD  . GLU A 1 21  ? -18.396 36.070  -6.109  1.00 54.04  ? 21   GLU A CD  1 
ATOM   151  O  OE1 . GLU A 1 21  ? -17.754 35.770  -5.072  1.00 53.13  ? 21   GLU A OE1 1 
ATOM   152  O  OE2 . GLU A 1 21  ? -18.677 35.240  -7.004  1.00 57.05  ? 21   GLU A OE2 1 
ATOM   153  N  N   . GLN A 1 22  ? -20.033 40.380  -7.439  1.00 33.80  ? 22   GLN A N   1 
ATOM   154  C  CA  . GLN A 1 22  ? -20.988 40.587  -8.524  1.00 34.21  ? 22   GLN A CA  1 
ATOM   155  C  C   . GLN A 1 22  ? -20.513 39.775  -9.737  1.00 37.56  ? 22   GLN A C   1 
ATOM   156  O  O   . GLN A 1 22  ? -19.346 39.848  -10.122 1.00 38.04  ? 22   GLN A O   1 
ATOM   157  C  CB  . GLN A 1 22  ? -21.080 42.072  -8.877  1.00 31.26  ? 22   GLN A CB  1 
ATOM   158  C  CG  . GLN A 1 22  ? -22.308 42.447  -9.673  1.00 36.38  ? 22   GLN A CG  1 
ATOM   159  C  CD  . GLN A 1 22  ? -22.303 43.899  -10.118 1.00 34.70  ? 22   GLN A CD  1 
ATOM   160  O  OE1 . GLN A 1 22  ? -21.267 44.541  -10.150 1.00 35.52  ? 22   GLN A OE1 1 
ATOM   161  N  NE2 . GLN A 1 22  ? -23.461 44.411  -10.472 1.00 33.92  ? 22   GLN A NE2 1 
ATOM   162  N  N   . LYS A 1 23  ? -21.402 38.998  -10.344 1.00 37.20  ? 23   LYS A N   1 
ATOM   163  C  CA  . LYS A 1 23  ? -20.956 38.084  -11.400 1.00 42.23  ? 23   LYS A CA  1 
ATOM   164  C  C   . LYS A 1 23  ? -20.789 38.777  -12.759 1.00 44.93  ? 23   LYS A C   1 
ATOM   165  O  O   . LYS A 1 23  ? -19.890 38.445  -13.528 1.00 46.37  ? 23   LYS A O   1 
ATOM   166  C  CB  . LYS A 1 23  ? -21.856 36.848  -11.490 1.00 41.27  ? 23   LYS A CB  1 
ATOM   167  C  CG  . LYS A 1 23  ? -21.080 35.558  -11.668 1.00 59.73  ? 23   LYS A CG  1 
ATOM   168  C  CD  . LYS A 1 23  ? -21.874 34.328  -11.214 1.00 68.62  ? 23   LYS A CD  1 
ATOM   169  C  CE  . LYS A 1 23  ? -21.250 33.042  -11.754 1.00 68.20  ? 23   LYS A CE  1 
ATOM   170  N  NZ  . LYS A 1 23  ? -21.993 31.833  -11.311 1.00 68.22  ? 23   LYS A NZ  1 
ATOM   171  N  N   . ALA A 1 24  ? -21.647 39.751  -13.032 1.00 39.20  ? 24   ALA A N   1 
ATOM   172  C  CA  . ALA A 1 24  ? -21.515 40.585  -14.215 1.00 43.73  ? 24   ALA A CA  1 
ATOM   173  C  C   . ALA A 1 24  ? -22.279 41.897  -14.013 1.00 49.71  ? 24   ALA A C   1 
ATOM   174  O  O   . ALA A 1 24  ? -23.002 42.050  -13.025 1.00 45.67  ? 24   ALA A O   1 
ATOM   175  C  CB  . ALA A 1 24  ? -22.029 39.859  -15.428 1.00 42.06  ? 24   ALA A CB  1 
ATOM   176  N  N   . SER A 1 25  ? -22.133 42.827  -14.955 1.00 48.46  ? 25   SER A N   1 
ATOM   177  C  CA  . SER A 1 25  ? -22.709 44.163  -14.818 1.00 51.36  ? 25   SER A CA  1 
ATOM   178  C  C   . SER A 1 25  ? -24.189 44.148  -14.441 1.00 53.58  ? 25   SER A C   1 
ATOM   179  O  O   . SER A 1 25  ? -24.655 44.984  -13.664 1.00 56.02  ? 25   SER A O   1 
ATOM   180  C  CB  . SER A 1 25  ? -22.513 44.965  -16.106 1.00 53.54  ? 25   SER A CB  1 
ATOM   181  O  OG  . SER A 1 25  ? -21.140 45.043  -16.444 1.00 55.02  ? 25   SER A OG  1 
ATOM   182  N  N   . GLY A 1 26  ? -24.935 43.202  -14.991 1.00 51.64  ? 26   GLY A N   1 
ATOM   183  C  CA  . GLY A 1 26  ? -26.370 43.188  -14.772 1.00 58.67  ? 26   GLY A CA  1 
ATOM   184  C  C   . GLY A 1 26  ? -26.794 42.648  -13.418 1.00 60.21  ? 26   GLY A C   1 
ATOM   185  O  O   . GLY A 1 26  ? -27.862 43.003  -12.911 1.00 62.37  ? 26   GLY A O   1 
ATOM   186  N  N   . GLU A 1 27  ? -25.948 41.807  -12.827 1.00 49.34  ? 27   GLU A N   1 
ATOM   187  C  CA  . GLU A 1 27  ? -26.359 40.958  -11.717 1.00 48.19  ? 27   GLU A CA  1 
ATOM   188  C  C   . GLU A 1 27  ? -26.207 41.603  -10.342 1.00 48.54  ? 27   GLU A C   1 
ATOM   189  O  O   . GLU A 1 27  ? -25.431 42.539  -10.170 1.00 47.94  ? 27   GLU A O   1 
ATOM   190  C  CB  . GLU A 1 27  ? -25.588 39.632  -11.762 1.00 52.56  ? 27   GLU A CB  1 
ATOM   191  C  CG  . GLU A 1 27  ? -25.644 38.894  -13.104 1.00 52.42  ? 27   GLU A CG  1 
ATOM   192  C  CD  . GLU A 1 27  ? -26.969 38.162  -13.343 1.00 63.45  ? 27   GLU A CD  1 
ATOM   193  O  OE1 . GLU A 1 27  ? -27.513 37.561  -12.380 1.00 57.70  ? 27   GLU A OE1 1 
ATOM   194  O  OE2 . GLU A 1 27  ? -27.458 38.180  -14.503 1.00 66.67  ? 27   GLU A OE2 1 
ATOM   195  N  N   . PRO A 1 28  ? -26.954 41.088  -9.354  1.00 45.73  ? 28   PRO A N   1 
ATOM   196  C  CA  . PRO A 1 28  ? -26.904 41.532  -7.959  1.00 43.39  ? 28   PRO A CA  1 
ATOM   197  C  C   . PRO A 1 28  ? -25.509 41.470  -7.344  1.00 38.08  ? 28   PRO A C   1 
ATOM   198  O  O   . PRO A 1 28  ? -24.661 40.698  -7.788  1.00 37.43  ? 28   PRO A O   1 
ATOM   199  C  CB  . PRO A 1 28  ? -27.807 40.519  -7.248  1.00 44.24  ? 28   PRO A CB  1 
ATOM   200  C  CG  . PRO A 1 28  ? -28.764 40.089  -8.295  1.00 47.45  ? 28   PRO A CG  1 
ATOM   201  C  CD  . PRO A 1 28  ? -27.971 40.044  -9.557  1.00 45.87  ? 28   PRO A CD  1 
ATOM   202  N  N   . VAL A 1 29  ? -25.284 42.297  -6.329  1.00 34.21  ? 29   VAL A N   1 
ATOM   203  C  CA  . VAL A 1 29  ? -24.103 42.177  -5.488  1.00 34.45  ? 29   VAL A CA  1 
ATOM   204  C  C   . VAL A 1 29  ? -24.458 41.295  -4.300  1.00 33.27  ? 29   VAL A C   1 
ATOM   205  O  O   . VAL A 1 29  ? -25.498 41.496  -3.656  1.00 31.77  ? 29   VAL A O   1 
ATOM   206  C  CB  . VAL A 1 29  ? -23.663 43.547  -4.939  1.00 30.13  ? 29   VAL A CB  1 
ATOM   207  C  CG1 . VAL A 1 29  ? -22.302 43.438  -4.263  1.00 25.76  ? 29   VAL A CG1 1 
ATOM   208  C  CG2 . VAL A 1 29  ? -23.646 44.559  -6.053  1.00 34.42  ? 29   VAL A CG2 1 
ATOM   209  N  N   . VAL A 1 30  ? -23.598 40.325  -4.012  1.00 31.51  ? 30   VAL A N   1 
ATOM   210  C  CA  . VAL A 1 30  ? -23.773 39.463  -2.852  1.00 30.24  ? 30   VAL A CA  1 
ATOM   211  C  C   . VAL A 1 30  ? -22.772 39.866  -1.795  1.00 32.94  ? 30   VAL A C   1 
ATOM   212  O  O   . VAL A 1 30  ? -21.565 39.930  -2.080  1.00 34.39  ? 30   VAL A O   1 
ATOM   213  C  CB  . VAL A 1 30  ? -23.528 37.979  -3.195  1.00 31.59  ? 30   VAL A CB  1 
ATOM   214  C  CG1 . VAL A 1 30  ? -23.579 37.153  -1.940  1.00 30.92  ? 30   VAL A CG1 1 
ATOM   215  C  CG2 . VAL A 1 30  ? -24.553 37.487  -4.192  1.00 34.92  ? 30   VAL A CG2 1 
ATOM   216  N  N   . LEU A 1 31  ? -23.269 40.138  -0.585  1.00 28.70  ? 31   LEU A N   1 
ATOM   217  C  CA  . LEU A 1 31  ? -22.424 40.512  0.544   1.00 30.73  ? 31   LEU A CA  1 
ATOM   218  C  C   . LEU A 1 31  ? -22.417 39.460  1.637   1.00 33.07  ? 31   LEU A C   1 
ATOM   219  O  O   . LEU A 1 31  ? -23.466 38.990  2.079   1.00 33.39  ? 31   LEU A O   1 
ATOM   220  C  CB  . LEU A 1 31  ? -22.907 41.806  1.204   1.00 33.22  ? 31   LEU A CB  1 
ATOM   221  C  CG  . LEU A 1 31  ? -22.779 43.194  0.597   1.00 31.90  ? 31   LEU A CG  1 
ATOM   222  C  CD1 . LEU A 1 31  ? -23.716 43.369  -0.586  1.00 28.24  ? 31   LEU A CD1 1 
ATOM   223  C  CD2 . LEU A 1 31  ? -23.099 44.181  1.692   1.00 22.95  ? 31   LEU A CD2 1 
ATOM   224  N  N   . SER A 1 32  ? -21.227 39.152  2.120   1.00 31.74  ? 32   SER A N   1 
ATOM   225  C  CA  . SER A 1 32  ? -21.068 38.222  3.219   1.00 31.89  ? 32   SER A CA  1 
ATOM   226  C  C   . SER A 1 32  ? -19.947 38.776  4.057   1.00 28.45  ? 32   SER A C   1 
ATOM   227  O  O   . SER A 1 32  ? -19.284 39.724  3.653   1.00 31.54  ? 32   SER A O   1 
ATOM   228  C  CB  . SER A 1 32  ? -20.691 36.831  2.700   1.00 35.60  ? 32   SER A CB  1 
ATOM   229  O  OG  . SER A 1 32  ? -19.480 36.883  1.947   1.00 40.79  ? 32   SER A OG  1 
ATOM   230  N  N   . GLY A 1 33  ? -19.730 38.186  5.222   1.00 27.13  ? 33   GLY A N   1 
ATOM   231  C  CA  . GLY A 1 33  ? -18.729 38.682  6.147   1.00 27.86  ? 33   GLY A CA  1 
ATOM   232  C  C   . GLY A 1 33  ? -19.262 38.718  7.567   1.00 28.45  ? 33   GLY A C   1 
ATOM   233  O  O   . GLY A 1 33  ? -20.299 38.142  7.874   1.00 31.10  ? 33   GLY A O   1 
ATOM   234  N  N   . GLN A 1 34  ? -18.561 39.423  8.436   1.00 28.65  ? 34   GLN A N   1 
ATOM   235  C  CA  . GLN A 1 34  ? -18.875 39.357  9.842   1.00 31.51  ? 34   GLN A CA  1 
ATOM   236  C  C   . GLN A 1 34  ? -18.458 40.614  10.557  1.00 29.37  ? 34   GLN A C   1 
ATOM   237  O  O   . GLN A 1 34  ? -17.447 41.229  10.238  1.00 28.23  ? 34   GLN A O   1 
ATOM   238  C  CB  . GLN A 1 34  ? -18.184 38.148  10.461  1.00 31.18  ? 34   GLN A CB  1 
ATOM   239  C  CG  . GLN A 1 34  ? -18.324 38.020  11.961  1.00 33.23  ? 34   GLN A CG  1 
ATOM   240  C  CD  . GLN A 1 34  ? -17.596 36.783  12.484  1.00 43.34  ? 34   GLN A CD  1 
ATOM   241  O  OE1 . GLN A 1 34  ? -16.504 36.880  13.053  1.00 38.06  ? 34   GLN A OE1 1 
ATOM   242  N  NE2 . GLN A 1 34  ? -18.186 35.604  12.257  1.00 43.05  ? 34   GLN A NE2 1 
ATOM   243  N  N   . ILE A 1 35  ? -19.262 40.994  11.530  1.00 31.37  ? 35   ILE A N   1 
ATOM   244  C  CA  . ILE A 1 35  ? -18.967 42.153  12.356  1.00 30.28  ? 35   ILE A CA  1 
ATOM   245  C  C   . ILE A 1 35  ? -19.159 41.716  13.800  1.00 31.23  ? 35   ILE A C   1 
ATOM   246  O  O   . ILE A 1 35  ? -20.008 40.872  14.088  1.00 33.33  ? 35   ILE A O   1 
ATOM   247  C  CB  . ILE A 1 35  ? -19.895 43.308  12.029  1.00 24.04  ? 35   ILE A CB  1 
ATOM   248  C  CG1 . ILE A 1 35  ? -19.901 43.529  10.511  1.00 25.41  ? 35   ILE A CG1 1 
ATOM   249  C  CG2 . ILE A 1 35  ? -19.477 44.554  12.801  1.00 21.79  ? 35   ILE A CG2 1 
ATOM   250  C  CD1 . ILE A 1 35  ? -21.066 44.365  10.023  1.00 24.92  ? 35   ILE A CD1 1 
ATOM   251  N  N   . THR A 1 36  ? -18.346 42.261  14.692  1.00 27.57  ? 36   THR A N   1 
ATOM   252  C  CA  . THR A 1 36  ? -18.335 41.825  16.070  1.00 28.48  ? 36   THR A CA  1 
ATOM   253  C  C   . THR A 1 36  ? -18.384 43.054  16.967  1.00 26.31  ? 36   THR A C   1 
ATOM   254  O  O   . THR A 1 36  ? -18.262 44.173  16.493  1.00 27.73  ? 36   THR A O   1 
ATOM   255  C  CB  . THR A 1 36  ? -17.099 40.934  16.361  1.00 27.04  ? 36   THR A CB  1 
ATOM   256  O  OG1 . THR A 1 36  ? -15.897 41.706  16.285  1.00 28.68  ? 36   THR A OG1 1 
ATOM   257  C  CG2 . THR A 1 36  ? -17.019 39.791  15.339  1.00 29.72  ? 36   THR A CG2 1 
ATOM   258  N  N   . GLY A 1 37  ? -18.606 42.845  18.256  1.00 25.17  ? 37   GLY A N   1 
ATOM   259  C  CA  . GLY A 1 37  ? -18.678 43.937  19.203  1.00 20.34  ? 37   GLY A CA  1 
ATOM   260  C  C   . GLY A 1 37  ? -19.944 44.770  19.116  1.00 25.55  ? 37   GLY A C   1 
ATOM   261  O  O   . GLY A 1 37  ? -19.980 45.873  19.632  1.00 28.59  ? 37   GLY A O   1 
ATOM   262  N  N   . LEU A 1 38  ? -20.990 44.261  18.469  1.00 28.13  ? 38   LEU A N   1 
ATOM   263  C  CA  . LEU A 1 38  ? -22.253 44.993  18.399  1.00 23.35  ? 38   LEU A CA  1 
ATOM   264  C  C   . LEU A 1 38  ? -23.179 44.691  19.577  1.00 32.39  ? 38   LEU A C   1 
ATOM   265  O  O   . LEU A 1 38  ? -23.138 43.599  20.147  1.00 30.58  ? 38   LEU A O   1 
ATOM   266  C  CB  . LEU A 1 38  ? -22.990 44.682  17.093  1.00 23.45  ? 38   LEU A CB  1 
ATOM   267  C  CG  . LEU A 1 38  ? -22.353 45.214  15.801  1.00 25.72  ? 38   LEU A CG  1 
ATOM   268  C  CD1 . LEU A 1 38  ? -22.867 44.427  14.617  1.00 23.86  ? 38   LEU A CD1 1 
ATOM   269  C  CD2 . LEU A 1 38  ? -22.595 46.707  15.628  1.00 19.60  ? 38   LEU A CD2 1 
ATOM   270  N  N   . THR A 1 39  ? -24.035 45.651  19.930  1.00 31.97  ? 39   THR A N   1 
ATOM   271  C  CA  . THR A 1 39  ? -25.134 45.326  20.809  1.00 26.45  ? 39   THR A CA  1 
ATOM   272  C  C   . THR A 1 39  ? -26.058 44.399  20.030  1.00 30.87  ? 39   THR A C   1 
ATOM   273  O  O   . THR A 1 39  ? -26.176 44.507  18.805  1.00 32.39  ? 39   THR A O   1 
ATOM   274  C  CB  . THR A 1 39  ? -25.865 46.574  21.322  1.00 33.45  ? 39   THR A CB  1 
ATOM   275  O  OG1 . THR A 1 39  ? -26.463 47.276  20.225  1.00 34.11  ? 39   THR A OG1 1 
ATOM   276  C  CG2 . THR A 1 39  ? -24.882 47.506  22.101  1.00 26.98  ? 39   THR A CG2 1 
ATOM   277  N  N   . GLU A 1 40  ? -26.678 43.463  20.735  1.00 28.79  ? 40   GLU A N   1 
ATOM   278  C  CA  . GLU A 1 40  ? -27.548 42.485  20.106  1.00 33.54  ? 40   GLU A CA  1 
ATOM   279  C  C   . GLU A 1 40  ? -28.745 43.145  19.424  1.00 32.04  ? 40   GLU A C   1 
ATOM   280  O  O   . GLU A 1 40  ? -29.318 44.095  19.952  1.00 33.92  ? 40   GLU A O   1 
ATOM   281  C  CB  . GLU A 1 40  ? -28.027 41.452  21.129  1.00 31.91  ? 40   GLU A CB  1 
ATOM   282  C  CG  . GLU A 1 40  ? -29.319 40.767  20.717  1.00 35.45  ? 40   GLU A CG  1 
ATOM   283  C  CD  . GLU A 1 40  ? -29.754 39.699  21.696  1.00 41.94  ? 40   GLU A CD  1 
ATOM   284  O  OE1 . GLU A 1 40  ? -29.327 39.764  22.871  1.00 37.93  ? 40   GLU A OE1 1 
ATOM   285  O  OE2 . GLU A 1 40  ? -30.516 38.796  21.283  1.00 40.30  ? 40   GLU A OE2 1 
ATOM   286  N  N   . GLY A 1 41  ? -29.118 42.618  18.258  1.00 29.19  ? 41   GLY A N   1 
ATOM   287  C  CA  . GLY A 1 41  ? -30.201 43.154  17.459  1.00 27.07  ? 41   GLY A CA  1 
ATOM   288  C  C   . GLY A 1 41  ? -29.777 43.813  16.146  1.00 33.33  ? 41   GLY A C   1 
ATOM   289  O  O   . GLY A 1 41  ? -28.669 43.599  15.627  1.00 28.97  ? 41   GLY A O   1 
ATOM   290  N  N   . GLN A 1 42  ? -30.685 44.631  15.612  1.00 31.91  ? 42   GLN A N   1 
ATOM   291  C  CA  . GLN A 1 42  ? -30.541 45.227  14.296  1.00 27.53  ? 42   GLN A CA  1 
ATOM   292  C  C   . GLN A 1 42  ? -29.757 46.518  14.287  1.00 28.43  ? 42   GLN A C   1 
ATOM   293  O  O   . GLN A 1 42  ? -29.804 47.300  15.234  1.00 28.40  ? 42   GLN A O   1 
ATOM   294  C  CB  . GLN A 1 42  ? -31.921 45.467  13.701  1.00 29.31  ? 42   GLN A CB  1 
ATOM   295  C  CG  . GLN A 1 42  ? -32.605 44.176  13.360  1.00 29.56  ? 42   GLN A CG  1 
ATOM   296  C  CD  . GLN A 1 42  ? -33.969 44.368  12.748  1.00 30.92  ? 42   GLN A CD  1 
ATOM   297  O  OE1 . GLN A 1 42  ? -34.520 45.476  12.725  1.00 33.56  ? 42   GLN A OE1 1 
ATOM   298  N  NE2 . GLN A 1 42  ? -34.532 43.275  12.247  1.00 32.06  ? 42   GLN A NE2 1 
ATOM   299  N  N   . HIS A 1 43  ? -29.021 46.725  13.205  1.00 25.77  ? 43   HIS A N   1 
ATOM   300  C  CA  . HIS A 1 43  ? -28.282 47.962  13.019  1.00 26.80  ? 43   HIS A CA  1 
ATOM   301  C  C   . HIS A 1 43  ? -28.380 48.388  11.570  1.00 24.43  ? 43   HIS A C   1 
ATOM   302  O  O   . HIS A 1 43  ? -28.301 47.557  10.665  1.00 23.35  ? 43   HIS A O   1 
ATOM   303  C  CB  . HIS A 1 43  ? -26.798 47.801  13.386  1.00 23.14  ? 43   HIS A CB  1 
ATOM   304  C  CG  . HIS A 1 43  ? -26.542 47.490  14.828  1.00 26.41  ? 43   HIS A CG  1 
ATOM   305  N  ND1 . HIS A 1 43  ? -26.175 48.453  15.744  1.00 30.34  ? 43   HIS A ND1 1 
ATOM   306  C  CD2 . HIS A 1 43  ? -26.552 46.315  15.505  1.00 27.87  ? 43   HIS A CD2 1 
ATOM   307  C  CE1 . HIS A 1 43  ? -25.974 47.888  16.923  1.00 25.91  ? 43   HIS A CE1 1 
ATOM   308  N  NE2 . HIS A 1 43  ? -26.200 46.591  16.805  1.00 26.87  ? 43   HIS A NE2 1 
ATOM   309  N  N   . GLY A 1 44  ? -28.547 49.684  11.352  1.00 23.55  ? 44   GLY A N   1 
ATOM   310  C  CA  . GLY A 1 44  ? -28.457 50.232  10.016  1.00 22.55  ? 44   GLY A CA  1 
ATOM   311  C  C   . GLY A 1 44  ? -27.130 49.840  9.383   1.00 24.18  ? 44   GLY A C   1 
ATOM   312  O  O   . GLY A 1 44  ? -26.094 49.734  10.050  1.00 24.70  ? 44   GLY A O   1 
ATOM   313  N  N   . PHE A 1 45  ? -27.180 49.610  8.084   1.00 20.82  ? 45   PHE A N   1 
ATOM   314  C  CA  . PHE A 1 45  ? -26.061 49.123  7.329   1.00 21.87  ? 45   PHE A CA  1 
ATOM   315  C  C   . PHE A 1 45  ? -26.151 49.859  5.984   1.00 24.73  ? 45   PHE A C   1 
ATOM   316  O  O   . PHE A 1 45  ? -27.021 49.564  5.166   1.00 22.58  ? 45   PHE A O   1 
ATOM   317  C  CB  . PHE A 1 45  ? -26.205 47.610  7.177   1.00 21.06  ? 45   PHE A CB  1 
ATOM   318  C  CG  . PHE A 1 45  ? -24.967 46.920  6.669   1.00 22.65  ? 45   PHE A CG  1 
ATOM   319  C  CD1 . PHE A 1 45  ? -23.788 46.949  7.400   1.00 22.46  ? 45   PHE A CD1 1 
ATOM   320  C  CD2 . PHE A 1 45  ? -24.991 46.226  5.460   1.00 25.08  ? 45   PHE A CD2 1 
ATOM   321  C  CE1 . PHE A 1 45  ? -22.654 46.315  6.939   1.00 23.39  ? 45   PHE A CE1 1 
ATOM   322  C  CE2 . PHE A 1 45  ? -23.859 45.578  4.990   1.00 25.01  ? 45   PHE A CE2 1 
ATOM   323  C  CZ  . PHE A 1 45  ? -22.683 45.624  5.735   1.00 27.01  ? 45   PHE A CZ  1 
ATOM   324  N  N   . HIS A 1 46  ? -25.291 50.857  5.786   1.00 21.25  ? 46   HIS A N   1 
ATOM   325  C  CA  . HIS A 1 46  ? -25.446 51.754  4.650   1.00 22.99  ? 46   HIS A CA  1 
ATOM   326  C  C   . HIS A 1 46  ? -24.157 52.009  3.911   1.00 21.85  ? 46   HIS A C   1 
ATOM   327  O  O   . HIS A 1 46  ? -23.073 52.002  4.490   1.00 19.61  ? 46   HIS A O   1 
ATOM   328  C  CB  . HIS A 1 46  ? -26.017 53.103  5.086   1.00 22.78  ? 46   HIS A CB  1 
ATOM   329  C  CG  . HIS A 1 46  ? -27.184 52.989  6.004   1.00 24.59  ? 46   HIS A CG  1 
ATOM   330  N  ND1 . HIS A 1 46  ? -28.371 52.403  5.624   1.00 26.74  ? 46   HIS A ND1 1 
ATOM   331  C  CD2 . HIS A 1 46  ? -27.347 53.381  7.287   1.00 23.30  ? 46   HIS A CD2 1 
ATOM   332  C  CE1 . HIS A 1 46  ? -29.217 52.429  6.638   1.00 25.62  ? 46   HIS A CE1 1 
ATOM   333  N  NE2 . HIS A 1 46  ? -28.620 53.020  7.658   1.00 27.33  ? 46   HIS A NE2 1 
ATOM   334  N  N   . VAL A 1 47  ? -24.295 52.264  2.619   1.00 18.44  ? 47   VAL A N   1 
ATOM   335  C  CA  . VAL A 1 47  ? -23.173 52.739  1.841   1.00 22.66  ? 47   VAL A CA  1 
ATOM   336  C  C   . VAL A 1 47  ? -23.356 54.236  1.752   1.00 20.86  ? 47   VAL A C   1 
ATOM   337  O  O   . VAL A 1 47  ? -24.370 54.713  1.231   1.00 20.82  ? 47   VAL A O   1 
ATOM   338  C  CB  . VAL A 1 47  ? -23.107 52.092  0.438   1.00 22.19  ? 47   VAL A CB  1 
ATOM   339  C  CG1 . VAL A 1 47  ? -22.025 52.773  -0.426  1.00 17.24  ? 47   VAL A CG1 1 
ATOM   340  C  CG2 . VAL A 1 47  ? -22.868 50.584  0.564   1.00 18.51  ? 47   VAL A CG2 1 
ATOM   341  N  N   . HIS A 1 48  ? -22.404 54.969  2.315   1.00 17.70  ? 48   HIS A N   1 
ATOM   342  C  CA  . HIS A 1 48  ? -22.450 56.424  2.287   1.00 21.67  ? 48   HIS A CA  1 
ATOM   343  C  C   . HIS A 1 48  ? -21.665 56.907  1.072   1.00 23.18  ? 48   HIS A C   1 
ATOM   344  O  O   . HIS A 1 48  ? -20.847 56.177  0.498   1.00 24.25  ? 48   HIS A O   1 
ATOM   345  C  CB  . HIS A 1 48  ? -21.901 57.039  3.587   1.00 19.04  ? 48   HIS A CB  1 
ATOM   346  C  CG  . HIS A 1 48  ? -22.753 56.776  4.790   1.00 20.58  ? 48   HIS A CG  1 
ATOM   347  N  ND1 . HIS A 1 48  ? -23.246 57.787  5.590   1.00 20.79  ? 48   HIS A ND1 1 
ATOM   348  C  CD2 . HIS A 1 48  ? -23.205 55.620  5.328   1.00 19.86  ? 48   HIS A CD2 1 
ATOM   349  C  CE1 . HIS A 1 48  ? -23.955 57.268  6.573   1.00 18.81  ? 48   HIS A CE1 1 
ATOM   350  N  NE2 . HIS A 1 48  ? -23.947 55.954  6.439   1.00 23.59  ? 48   HIS A NE2 1 
ATOM   351  N  N   . GLN A 1 49  ? -21.906 58.153  0.696   1.00 27.90  ? 49   GLN A N   1 
ATOM   352  C  CA  . GLN A 1 49  ? -21.432 58.672  -0.570  1.00 26.39  ? 49   GLN A CA  1 
ATOM   353  C  C   . GLN A 1 49  ? -19.909 58.713  -0.796  1.00 29.97  ? 49   GLN A C   1 
ATOM   354  O  O   . GLN A 1 49  ? -19.423 58.220  -1.806  1.00 29.36  ? 49   GLN A O   1 
ATOM   355  C  CB  . GLN A 1 49  ? -21.986 60.055  -0.769  1.00 28.88  ? 49   GLN A CB  1 
ATOM   356  C  CG  . GLN A 1 49  ? -21.302 60.742  -1.884  1.00 35.06  ? 49   GLN A CG  1 
ATOM   357  C  CD  . GLN A 1 49  ? -22.165 61.790  -2.456  1.00 44.34  ? 49   GLN A CD  1 
ATOM   358  O  OE1 . GLN A 1 49  ? -22.706 62.631  -1.721  1.00 50.34  ? 49   GLN A OE1 1 
ATOM   359  N  NE2 . GLN A 1 49  ? -22.335 61.757  -3.779  1.00 41.76  ? 49   GLN A NE2 1 
ATOM   360  N  N   . TYR A 1 50  ? -19.160 59.303  0.128   1.00 28.98  ? 50   TYR A N   1 
ATOM   361  C  CA  . TYR A 1 50  ? -17.720 59.473  -0.062  1.00 25.84  ? 50   TYR A CA  1 
ATOM   362  C  C   . TYR A 1 50  ? -16.859 58.466  0.693   1.00 27.81  ? 50   TYR A C   1 
ATOM   363  O  O   . TYR A 1 50  ? -17.158 58.104  1.825   1.00 26.50  ? 50   TYR A O   1 
ATOM   364  C  CB  . TYR A 1 50  ? -17.313 60.901  0.314   1.00 29.57  ? 50   TYR A CB  1 
ATOM   365  C  CG  . TYR A 1 50  ? -18.044 61.923  -0.508  1.00 33.16  ? 50   TYR A CG  1 
ATOM   366  C  CD1 . TYR A 1 50  ? -17.728 62.098  -1.850  1.00 33.73  ? 50   TYR A CD1 1 
ATOM   367  C  CD2 . TYR A 1 50  ? -19.081 62.683  0.032   1.00 31.64  ? 50   TYR A CD2 1 
ATOM   368  C  CE1 . TYR A 1 50  ? -18.408 63.008  -2.635  1.00 36.54  ? 50   TYR A CE1 1 
ATOM   369  C  CE2 . TYR A 1 50  ? -19.758 63.610  -0.748  1.00 38.20  ? 50   TYR A CE2 1 
ATOM   370  C  CZ  . TYR A 1 50  ? -19.414 63.762  -2.083  1.00 39.38  ? 50   TYR A CZ  1 
ATOM   371  O  OH  . TYR A 1 50  ? -20.062 64.662  -2.891  1.00 45.00  ? 50   TYR A OH  1 
ATOM   372  N  N   . GLY A 1 51  ? -15.777 58.021  0.064   1.00 25.92  ? 51   GLY A N   1 
ATOM   373  C  CA  . GLY A 1 51  ? -14.823 57.161  0.739   1.00 25.84  ? 51   GLY A CA  1 
ATOM   374  C  C   . GLY A 1 51  ? -13.782 57.978  1.489   1.00 28.15  ? 51   GLY A C   1 
ATOM   375  O  O   . GLY A 1 51  ? -12.582 57.743  1.370   1.00 27.25  ? 51   GLY A O   1 
ATOM   376  N  N   . ASP A 1 52  ? -14.241 58.952  2.260   1.00 25.15  ? 52   ASP A N   1 
ATOM   377  C  CA  . ASP A 1 52  ? -13.339 59.887  2.915   1.00 26.10  ? 52   ASP A CA  1 
ATOM   378  C  C   . ASP A 1 52  ? -13.419 59.649  4.415   1.00 26.16  ? 52   ASP A C   1 
ATOM   379  O  O   . ASP A 1 52  ? -14.450 59.898  5.032   1.00 25.93  ? 52   ASP A O   1 
ATOM   380  C  CB  . ASP A 1 52  ? -13.754 61.317  2.540   1.00 27.55  ? 52   ASP A CB  1 
ATOM   381  C  CG  . ASP A 1 52  ? -12.959 62.404  3.270   1.00 31.29  ? 52   ASP A CG  1 
ATOM   382  O  OD1 . ASP A 1 52  ? -12.150 62.099  4.175   1.00 32.57  ? 52   ASP A OD1 1 
ATOM   383  O  OD2 . ASP A 1 52  ? -13.156 63.591  2.924   1.00 32.19  ? 52   ASP A OD2 1 
ATOM   384  N  N   . ASN A 1 53  ? -12.334 59.154  4.998   1.00 26.78  ? 53   ASN A N   1 
ATOM   385  C  CA  . ASN A 1 53  ? -12.302 58.883  6.434   1.00 27.88  ? 53   ASN A CA  1 
ATOM   386  C  C   . ASN A 1 53  ? -11.318 59.806  7.173   1.00 29.24  ? 53   ASN A C   1 
ATOM   387  O  O   . ASN A 1 53  ? -10.697 59.419  8.163   1.00 28.75  ? 53   ASN A O   1 
ATOM   388  C  CB  . ASN A 1 53  ? -12.044 57.388  6.711   1.00 26.28  ? 53   ASN A CB  1 
ATOM   389  C  CG  . ASN A 1 53  ? -13.177 56.472  6.156   1.00 41.58  ? 53   ASN A CG  1 
ATOM   390  O  OD1 . ASN A 1 53  ? -14.220 56.960  5.679   1.00 35.91  ? 53   ASN A OD1 1 
ATOM   391  N  ND2 . ASN A 1 53  ? -12.965 55.139  6.211   1.00 33.23  ? 53   ASN A ND2 1 
ATOM   392  N  N   . THR A 1 54  ? -11.209 61.046  6.698   1.00 28.01  ? 54   THR A N   1 
ATOM   393  C  CA  . THR A 1 54  ? -10.296 62.014  7.293   1.00 28.21  ? 54   THR A CA  1 
ATOM   394  C  C   . THR A 1 54  ? -10.726 62.434  8.679   1.00 30.06  ? 54   THR A C   1 
ATOM   395  O  O   . THR A 1 54  ? -9.887  62.660  9.533   1.00 36.45  ? 54   THR A O   1 
ATOM   396  C  CB  . THR A 1 54  ? -10.138 63.255  6.427   1.00 28.81  ? 54   THR A CB  1 
ATOM   397  O  OG1 . THR A 1 54  ? -11.432 63.692  6.019   1.00 37.38  ? 54   THR A OG1 1 
ATOM   398  C  CG2 . THR A 1 54  ? -9.326  62.941  5.195   1.00 23.83  ? 54   THR A CG2 1 
ATOM   399  N  N   . GLN A 1 55  ? -12.027 62.532  8.919   1.00 34.32  ? 55   GLN A N   1 
ATOM   400  C  CA  . GLN A 1 55  ? -12.510 62.738  10.288  1.00 35.92  ? 55   GLN A CA  1 
ATOM   401  C  C   . GLN A 1 55  ? -13.423 61.592  10.642  1.00 31.88  ? 55   GLN A C   1 
ATOM   402  O  O   . GLN A 1 55  ? -14.630 61.742  10.737  1.00 38.70  ? 55   GLN A O   1 
ATOM   403  C  CB  . GLN A 1 55  ? -13.273 64.060  10.429  1.00 40.50  ? 55   GLN A CB  1 
ATOM   404  C  CG  . GLN A 1 55  ? -12.982 65.092  9.325   1.00 48.29  ? 55   GLN A CG  1 
ATOM   405  C  CD  . GLN A 1 55  ? -13.786 66.387  9.498   1.00 65.32  ? 55   GLN A CD  1 
ATOM   406  O  OE1 . GLN A 1 55  ? -14.959 66.485  9.087   1.00 60.48  ? 55   GLN A OE1 1 
ATOM   407  N  NE2 . GLN A 1 55  ? -13.157 67.385  10.116  1.00 68.93  ? 55   GLN A NE2 1 
ATOM   408  N  N   . GLY A 1 56  ? -12.850 60.419  10.783  1.00 32.18  ? 56   GLY A N   1 
ATOM   409  C  CA  . GLY A 1 56  ? -13.639 59.262  11.123  1.00 28.37  ? 56   GLY A CA  1 
ATOM   410  C  C   . GLY A 1 56  ? -14.694 58.986  10.073  1.00 32.48  ? 56   GLY A C   1 
ATOM   411  O  O   . GLY A 1 56  ? -14.598 59.424  8.913   1.00 32.51  ? 56   GLY A O   1 
ATOM   412  N  N   . CYS A 1 57  ? -15.701 58.242  10.506  1.00 27.27  ? 57   CYS A N   1 
ATOM   413  C  CA  . CYS A 1 57  ? -16.838 57.898  9.705   1.00 25.79  ? 57   CYS A CA  1 
ATOM   414  C  C   . CYS A 1 57  ? -17.699 59.088  9.307   1.00 27.30  ? 57   CYS A C   1 
ATOM   415  O  O   . CYS A 1 57  ? -18.440 59.007  8.329   1.00 28.02  ? 57   CYS A O   1 
ATOM   416  C  CB  . CYS A 1 57  ? -17.665 56.857  10.446  1.00 27.17  ? 57   CYS A CB  1 
ATOM   417  S  SG  . CYS A 1 57  ? -16.676 55.380  10.831  1.00 36.05  ? 57   CYS A SG  1 
ATOM   418  N  N   . THR A 1 58  ? -17.595 60.210  10.003  1.00 25.30  ? 58   THR A N   1 
ATOM   419  C  CA  . THR A 1 58  ? -18.532 61.283  9.697   1.00 26.42  ? 58   THR A CA  1 
ATOM   420  C  C   . THR A 1 58  ? -18.180 61.967  8.394   1.00 28.99  ? 58   THR A C   1 
ATOM   421  O  O   . THR A 1 58  ? -19.056 62.511  7.733   1.00 33.02  ? 58   THR A O   1 
ATOM   422  C  CB  . THR A 1 58  ? -18.665 62.362  10.812  1.00 36.70  ? 58   THR A CB  1 
ATOM   423  O  OG1 . THR A 1 58  ? -17.670 63.370  10.631  1.00 38.00  ? 58   THR A OG1 1 
ATOM   424  C  CG2 . THR A 1 58  ? -18.559 61.763  12.213  1.00 27.62  ? 58   THR A CG2 1 
ATOM   425  N  N   . SER A 1 59  ? -16.911 61.934  7.999   1.00 28.30  ? 59   SER A N   1 
ATOM   426  C  CA  . SER A 1 59  ? -16.552 62.597  6.761   1.00 24.20  ? 59   SER A CA  1 
ATOM   427  C  C   . SER A 1 59  ? -17.017 61.839  5.514   1.00 26.56  ? 59   SER A C   1 
ATOM   428  O  O   . SER A 1 59  ? -16.822 62.321  4.404   1.00 24.49  ? 59   SER A O   1 
ATOM   429  C  CB  . SER A 1 59  ? -15.068 62.960  6.706   1.00 29.00  ? 59   SER A CB  1 
ATOM   430  O  OG  . SER A 1 59  ? -14.249 61.901  7.135   1.00 33.63  ? 59   SER A OG  1 
ATOM   431  N  N   . ALA A 1 60  ? -17.636 60.667  5.702   1.00 25.43  ? 60   ALA A N   1 
ATOM   432  C  CA  . ALA A 1 60  ? -18.166 59.873  4.580   1.00 23.09  ? 60   ALA A CA  1 
ATOM   433  C  C   . ALA A 1 60  ? -19.403 60.494  3.913   1.00 25.85  ? 60   ALA A C   1 
ATOM   434  O  O   . ALA A 1 60  ? -19.814 60.058  2.847   1.00 24.98  ? 60   ALA A O   1 
ATOM   435  C  CB  . ALA A 1 60  ? -18.475 58.447  5.010   1.00 19.50  ? 60   ALA A CB  1 
ATOM   436  N  N   . GLY A 1 61  ? -20.006 61.499  4.542   1.00 27.02  ? 61   GLY A N   1 
ATOM   437  C  CA  . GLY A 1 61  ? -21.164 62.142  3.966   1.00 23.11  ? 61   GLY A CA  1 
ATOM   438  C  C   . GLY A 1 61  ? -22.429 61.375  4.268   1.00 27.44  ? 61   GLY A C   1 
ATOM   439  O  O   . GLY A 1 61  ? -22.445 60.476  5.125   1.00 22.52  ? 61   GLY A O   1 
ATOM   440  N  N   . PRO A 1 62  ? -23.504 61.705  3.542   1.00 28.60  ? 62   PRO A N   1 
ATOM   441  C  CA  . PRO A 1 62  ? -24.792 61.049  3.749   1.00 27.72  ? 62   PRO A CA  1 
ATOM   442  C  C   . PRO A 1 62  ? -24.830 59.759  2.917   1.00 22.39  ? 62   PRO A C   1 
ATOM   443  O  O   . PRO A 1 62  ? -23.819 59.425  2.305   1.00 24.61  ? 62   PRO A O   1 
ATOM   444  C  CB  . PRO A 1 62  ? -25.785 62.086  3.204   1.00 25.97  ? 62   PRO A CB  1 
ATOM   445  C  CG  . PRO A 1 62  ? -24.968 62.923  2.198   1.00 29.05  ? 62   PRO A CG  1 
ATOM   446  C  CD  . PRO A 1 62  ? -23.515 62.499  2.304   1.00 30.66  ? 62   PRO A CD  1 
ATOM   447  N  N   . HIS A 1 63  ? -25.964 59.069  2.891   1.00 19.42  ? 63   HIS A N   1 
ATOM   448  C  CA  . HIS A 1 63  ? -26.103 57.839  2.110   1.00 24.32  ? 63   HIS A CA  1 
ATOM   449  C  C   . HIS A 1 63  ? -25.909 58.119  0.626   1.00 22.19  ? 63   HIS A C   1 
ATOM   450  O  O   . HIS A 1 63  ? -26.353 59.141  0.127   1.00 22.04  ? 63   HIS A O   1 
ATOM   451  C  CB  . HIS A 1 63  ? -27.472 57.179  2.358   1.00 20.22  ? 63   HIS A CB  1 
ATOM   452  C  CG  . HIS A 1 63  ? -27.699 56.788  3.782   1.00 22.75  ? 63   HIS A CG  1 
ATOM   453  N  ND1 . HIS A 1 63  ? -28.865 56.203  4.223   1.00 27.35  ? 63   HIS A ND1 1 
ATOM   454  C  CD2 . HIS A 1 63  ? -26.904 56.909  4.875   1.00 23.23  ? 63   HIS A CD2 1 
ATOM   455  C  CE1 . HIS A 1 63  ? -28.784 55.986  5.522   1.00 24.94  ? 63   HIS A CE1 1 
ATOM   456  N  NE2 . HIS A 1 63  ? -27.604 56.404  5.942   1.00 21.97  ? 63   HIS A NE2 1 
ATOM   457  N  N   . PHE A 1 64  ? -25.207 57.221  -0.055  1.00 22.72  ? 64   PHE A N   1 
ATOM   458  C  CA  . PHE A 1 64  ? -25.021 57.286  -1.503  1.00 23.52  ? 64   PHE A CA  1 
ATOM   459  C  C   . PHE A 1 64  ? -26.383 57.417  -2.185  1.00 24.90  ? 64   PHE A C   1 
ATOM   460  O  O   . PHE A 1 64  ? -27.219 56.518  -2.100  1.00 26.46  ? 64   PHE A O   1 
ATOM   461  C  CB  . PHE A 1 64  ? -24.300 56.022  -1.960  1.00 25.62  ? 64   PHE A CB  1 
ATOM   462  C  CG  . PHE A 1 64  ? -23.959 56.002  -3.420  1.00 24.82  ? 64   PHE A CG  1 
ATOM   463  C  CD1 . PHE A 1 64  ? -23.625 57.167  -4.086  1.00 24.06  ? 64   PHE A CD1 1 
ATOM   464  C  CD2 . PHE A 1 64  ? -23.942 54.805  -4.116  1.00 22.88  ? 64   PHE A CD2 1 
ATOM   465  C  CE1 . PHE A 1 64  ? -23.302 57.148  -5.443  1.00 22.30  ? 64   PHE A CE1 1 
ATOM   466  C  CE2 . PHE A 1 64  ? -23.605 54.777  -5.466  1.00 28.29  ? 64   PHE A CE2 1 
ATOM   467  C  CZ  . PHE A 1 64  ? -23.289 55.953  -6.126  1.00 25.89  ? 64   PHE A CZ  1 
ATOM   468  N  N   . ASN A 1 65  ? -26.606 58.554  -2.835  1.00 26.45  ? 65   ASN A N   1 
ATOM   469  C  CA  . ASN A 1 65  ? -27.941 58.944  -3.281  1.00 29.28  ? 65   ASN A CA  1 
ATOM   470  C  C   . ASN A 1 65  ? -27.949 59.674  -4.633  1.00 28.41  ? 65   ASN A C   1 
ATOM   471  O  O   . ASN A 1 65  ? -28.502 60.753  -4.745  1.00 28.95  ? 65   ASN A O   1 
ATOM   472  C  CB  . ASN A 1 65  ? -28.598 59.822  -2.206  1.00 26.97  ? 65   ASN A CB  1 
ATOM   473  C  CG  . ASN A 1 65  ? -30.090 60.046  -2.446  1.00 30.41  ? 65   ASN A CG  1 
ATOM   474  O  OD1 . ASN A 1 65  ? -30.726 59.332  -3.214  1.00 33.13  ? 65   ASN A OD1 1 
ATOM   475  N  ND2 . ASN A 1 65  ? -30.650 61.034  -1.769  1.00 27.27  ? 65   ASN A ND2 1 
ATOM   476  N  N   . PRO A 1 66  ? -27.361 59.063  -5.668  1.00 29.17  ? 66   PRO A N   1 
ATOM   477  C  CA  . PRO A 1 66  ? -27.268 59.694  -7.005  1.00 35.65  ? 66   PRO A CA  1 
ATOM   478  C  C   . PRO A 1 66  ? -28.595 60.267  -7.544  1.00 36.90  ? 66   PRO A C   1 
ATOM   479  O  O   . PRO A 1 66  ? -28.589 61.300  -8.208  1.00 38.62  ? 66   PRO A O   1 
ATOM   480  C  CB  . PRO A 1 66  ? -26.805 58.549  -7.930  1.00 27.84  ? 66   PRO A CB  1 
ATOM   481  C  CG  . PRO A 1 66  ? -26.276 57.485  -7.034  1.00 32.10  ? 66   PRO A CG  1 
ATOM   482  C  CD  . PRO A 1 66  ? -26.869 57.673  -5.648  1.00 26.52  ? 66   PRO A CD  1 
ATOM   483  N  N   . HIS A 1 67  ? -29.708 59.592  -7.276  1.00 35.02  ? 67   HIS A N   1 
ATOM   484  C  CA  . HIS A 1 67  ? -30.997 59.964  -7.848  1.00 29.81  ? 67   HIS A CA  1 
ATOM   485  C  C   . HIS A 1 67  ? -31.856 60.843  -6.936  1.00 33.42  ? 67   HIS A C   1 
ATOM   486  O  O   . HIS A 1 67  ? -33.016 61.090  -7.231  1.00 33.99  ? 67   HIS A O   1 
ATOM   487  C  CB  . HIS A 1 67  ? -31.768 58.702  -8.199  1.00 32.12  ? 67   HIS A CB  1 
ATOM   488  C  CG  . HIS A 1 67  ? -30.985 57.729  -9.019  1.00 35.96  ? 67   HIS A CG  1 
ATOM   489  N  ND1 . HIS A 1 67  ? -30.501 58.034  -10.275 1.00 32.96  ? 67   HIS A ND1 1 
ATOM   490  C  CD2 . HIS A 1 67  ? -30.610 56.451  -8.769  1.00 31.90  ? 67   HIS A CD2 1 
ATOM   491  C  CE1 . HIS A 1 67  ? -29.860 56.986  -10.761 1.00 31.10  ? 67   HIS A CE1 1 
ATOM   492  N  NE2 . HIS A 1 67  ? -29.903 56.015  -9.864  1.00 32.05  ? 67   HIS A NE2 1 
ATOM   493  N  N   . SER A 1 68  ? -31.290 61.297  -5.820  1.00 34.47  ? 68   SER A N   1 
ATOM   494  C  CA  . SER A 1 68  ? -31.973 62.238  -4.930  1.00 37.13  ? 68   SER A CA  1 
ATOM   495  C  C   . SER A 1 68  ? -33.303 61.755  -4.384  1.00 36.24  ? 68   SER A C   1 
ATOM   496  O  O   . SER A 1 68  ? -34.249 62.527  -4.259  1.00 37.70  ? 68   SER A O   1 
ATOM   497  C  CB  . SER A 1 68  ? -32.160 63.597  -5.611  1.00 40.79  ? 68   SER A CB  1 
ATOM   498  O  OG  . SER A 1 68  ? -30.912 64.261  -5.744  1.00 42.60  ? 68   SER A OG  1 
ATOM   499  N  N   . LYS A 1 69  ? -33.371 60.480  -4.047  1.00 32.41  ? 69   LYS A N   1 
ATOM   500  C  CA  . LYS A 1 69  ? -34.576 59.949  -3.448  1.00 35.96  ? 69   LYS A CA  1 
ATOM   501  C  C   . LYS A 1 69  ? -34.486 60.095  -1.920  1.00 34.79  ? 69   LYS A C   1 
ATOM   502  O  O   . LYS A 1 69  ? -33.446 60.482  -1.379  1.00 33.00  ? 69   LYS A O   1 
ATOM   503  C  CB  . LYS A 1 69  ? -34.819 58.496  -3.909  1.00 38.94  ? 69   LYS A CB  1 
ATOM   504  C  CG  . LYS A 1 69  ? -34.896 58.354  -5.440  1.00 42.54  ? 69   LYS A CG  1 
ATOM   505  C  CD  . LYS A 1 69  ? -35.758 57.177  -5.929  1.00 48.86  ? 69   LYS A CD  1 
ATOM   506  C  CE  . LYS A 1 69  ? -35.378 55.848  -5.244  1.00 51.68  ? 69   LYS A CE  1 
ATOM   507  N  NZ  . LYS A 1 69  ? -35.421 54.643  -6.147  1.00 42.89  ? 69   LYS A NZ  1 
ATOM   508  N  N   . LYS A 1 70  ? -35.585 59.838  -1.226  1.00 37.98  ? 70   LYS A N   1 
ATOM   509  C  CA  . LYS A 1 70  ? -35.549 59.801  0.234   1.00 35.60  ? 70   LYS A CA  1 
ATOM   510  C  C   . LYS A 1 70  ? -35.175 58.399  0.697   1.00 32.06  ? 70   LYS A C   1 
ATOM   511  O  O   . LYS A 1 70  ? -35.237 57.433  -0.071  1.00 32.28  ? 70   LYS A O   1 
ATOM   512  C  CB  . LYS A 1 70  ? -36.905 60.191  0.814   1.00 39.72  ? 70   LYS A CB  1 
ATOM   513  C  CG  . LYS A 1 70  ? -37.348 61.617  0.499   1.00 42.55  ? 70   LYS A CG  1 
ATOM   514  C  CD  . LYS A 1 70  ? -38.836 61.770  0.766   1.00 53.48  ? 70   LYS A CD  1 
ATOM   515  C  CE  . LYS A 1 70  ? -39.334 63.115  0.295   1.00 60.57  ? 70   LYS A CE  1 
ATOM   516  N  NZ  . LYS A 1 70  ? -38.363 64.155  0.726   1.00 65.00  ? 70   LYS A NZ  1 
ATOM   517  N  N   . HIS A 1 71  ? -34.802 58.296  1.961   1.00 28.08  ? 71   HIS A N   1 
ATOM   518  C  CA  . HIS A 1 71  ? -34.377 57.032  2.542   1.00 26.89  ? 71   HIS A CA  1 
ATOM   519  C  C   . HIS A 1 71  ? -35.499 55.969  2.574   1.00 26.81  ? 71   HIS A C   1 
ATOM   520  O  O   . HIS A 1 71  ? -36.669 56.283  2.777   1.00 27.42  ? 71   HIS A O   1 
ATOM   521  C  CB  . HIS A 1 71  ? -33.816 57.283  3.957   1.00 24.49  ? 71   HIS A CB  1 
ATOM   522  C  CG  . HIS A 1 71  ? -33.406 56.034  4.665   1.00 25.03  ? 71   HIS A CG  1 
ATOM   523  N  ND1 . HIS A 1 71  ? -32.231 55.371  4.383   1.00 24.18  ? 71   HIS A ND1 1 
ATOM   524  C  CD2 . HIS A 1 71  ? -34.038 55.297  5.607   1.00 26.92  ? 71   HIS A CD2 1 
ATOM   525  C  CE1 . HIS A 1 71  ? -32.151 54.288  5.133   1.00 24.27  ? 71   HIS A CE1 1 
ATOM   526  N  NE2 . HIS A 1 71  ? -33.233 54.222  5.887   1.00 26.85  ? 71   HIS A NE2 1 
ATOM   527  N  N   . GLY A 1 72  ? -35.126 54.713  2.375   1.00 22.67  ? 72   GLY A N   1 
ATOM   528  C  CA  . GLY A 1 72  ? -36.035 53.598  2.525   1.00 23.85  ? 72   GLY A CA  1 
ATOM   529  C  C   . GLY A 1 72  ? -35.272 52.319  2.871   1.00 31.34  ? 72   GLY A C   1 
ATOM   530  O  O   . GLY A 1 72  ? -34.047 52.335  3.120   1.00 26.79  ? 72   GLY A O   1 
ATOM   531  N  N   . GLY A 1 73  ? -36.000 51.206  2.902   1.00 30.41  ? 73   GLY A N   1 
ATOM   532  C  CA  . GLY A 1 73  ? -35.388 49.891  2.992   1.00 28.19  ? 73   GLY A CA  1 
ATOM   533  C  C   . GLY A 1 73  ? -34.920 49.426  1.626   1.00 28.83  ? 73   GLY A C   1 
ATOM   534  O  O   . GLY A 1 73  ? -35.279 50.005  0.608   1.00 29.65  ? 73   GLY A O   1 
ATOM   535  N  N   . PRO A 1 74  ? -34.103 48.372  1.590   1.00 30.35  ? 74   PRO A N   1 
ATOM   536  C  CA  . PRO A 1 74  ? -33.621 47.905  0.283   1.00 27.91  ? 74   PRO A CA  1 
ATOM   537  C  C   . PRO A 1 74  ? -34.787 47.487  -0.627  1.00 31.46  ? 74   PRO A C   1 
ATOM   538  O  O   . PRO A 1 74  ? -34.704 47.647  -1.856  1.00 32.17  ? 74   PRO A O   1 
ATOM   539  C  CB  . PRO A 1 74  ? -32.736 46.689  0.623   1.00 24.62  ? 74   PRO A CB  1 
ATOM   540  C  CG  . PRO A 1 74  ? -33.026 46.343  2.072   1.00 25.05  ? 74   PRO A CG  1 
ATOM   541  C  CD  . PRO A 1 74  ? -33.598 47.577  2.728   1.00 26.73  ? 74   PRO A CD  1 
ATOM   542  N  N   . ALA A 1 75  ? -35.863 46.981  -0.021  1.00 32.00  ? 75   ALA A N   1 
ATOM   543  C  CA  . ALA A 1 75  ? -37.028 46.477  -0.754  1.00 29.75  ? 75   ALA A CA  1 
ATOM   544  C  C   . ALA A 1 75  ? -38.099 47.529  -1.075  1.00 33.20  ? 75   ALA A C   1 
ATOM   545  O  O   . ALA A 1 75  ? -38.972 47.307  -1.920  1.00 38.36  ? 75   ALA A O   1 
ATOM   546  C  CB  . ALA A 1 75  ? -37.644 45.309  -0.008  1.00 31.29  ? 75   ALA A CB  1 
ATOM   547  N  N   . ASP A 1 76  ? -38.048 48.665  -0.390  1.00 33.09  ? 76   ASP A N   1 
ATOM   548  C  CA  . ASP A 1 76  ? -38.869 49.807  -0.774  1.00 35.57  ? 76   ASP A CA  1 
ATOM   549  C  C   . ASP A 1 76  ? -38.531 50.312  -2.196  1.00 38.33  ? 76   ASP A C   1 
ATOM   550  O  O   . ASP A 1 76  ? -37.429 50.110  -2.726  1.00 33.96  ? 76   ASP A O   1 
ATOM   551  C  CB  . ASP A 1 76  ? -38.715 50.937  0.246   1.00 32.82  ? 76   ASP A CB  1 
ATOM   552  C  CG  . ASP A 1 76  ? -39.293 50.577  1.602   1.00 39.47  ? 76   ASP A CG  1 
ATOM   553  O  OD1 . ASP A 1 76  ? -40.497 50.229  1.652   1.00 41.71  ? 76   ASP A OD1 1 
ATOM   554  O  OD2 . ASP A 1 76  ? -38.557 50.642  2.619   1.00 36.60  ? 76   ASP A OD2 1 
ATOM   555  N  N   . GLU A 1 77  ? -39.487 50.993  -2.802  1.00 39.29  ? 77   GLU A N   1 
ATOM   556  C  CA  . GLU A 1 77  ? -39.307 51.490  -4.155  1.00 44.56  ? 77   GLU A CA  1 
ATOM   557  C  C   . GLU A 1 77  ? -38.596 52.835  -4.188  1.00 43.14  ? 77   GLU A C   1 
ATOM   558  O  O   . GLU A 1 77  ? -37.766 53.088  -5.065  1.00 44.98  ? 77   GLU A O   1 
ATOM   559  C  CB  . GLU A 1 77  ? -40.654 51.560  -4.870  1.00 48.79  ? 77   GLU A CB  1 
ATOM   560  C  CG  . GLU A 1 77  ? -41.131 50.200  -5.347  1.00 48.63  ? 77   GLU A CG  1 
ATOM   561  C  CD  . GLU A 1 77  ? -42.461 50.291  -6.031  1.00 47.16  ? 77   GLU A CD  1 
ATOM   562  O  OE1 . GLU A 1 77  ? -43.177 51.295  -5.806  1.00 53.61  ? 77   GLU A OE1 1 
ATOM   563  O  OE2 . GLU A 1 77  ? -42.787 49.368  -6.792  1.00 41.62  ? 77   GLU A OE2 1 
ATOM   564  N  N   . GLU A 1 78  ? -38.932 53.699  -3.239  1.00 38.21  ? 78   GLU A N   1 
ATOM   565  C  CA  . GLU A 1 78  ? -38.141 54.893  -3.007  1.00 38.80  ? 78   GLU A CA  1 
ATOM   566  C  C   . GLU A 1 78  ? -37.095 54.554  -1.946  1.00 38.66  ? 78   GLU A C   1 
ATOM   567  O  O   . GLU A 1 78  ? -37.429 54.308  -0.780  1.00 34.98  ? 78   GLU A O   1 
ATOM   568  C  CB  . GLU A 1 78  ? -39.024 56.056  -2.544  1.00 38.16  ? 78   GLU A CB  1 
ATOM   569  C  CG  . GLU A 1 78  ? -38.239 57.290  -2.070  1.00 47.19  ? 78   GLU A CG  1 
ATOM   570  C  CD  . GLU A 1 78  ? -38.601 58.586  -2.813  1.00 48.96  ? 78   GLU A CD  1 
ATOM   571  O  OE1 . GLU A 1 78  ? -39.094 58.517  -3.964  1.00 56.82  ? 78   GLU A OE1 1 
ATOM   572  O  OE2 . GLU A 1 78  ? -38.375 59.679  -2.244  1.00 49.18  ? 78   GLU A OE2 1 
ATOM   573  N  N   . ARG A 1 79  ? -35.834 54.530  -2.360  1.00 37.69  ? 79   ARG A N   1 
ATOM   574  C  CA  . ARG A 1 79  ? -34.710 54.336  -1.448  1.00 31.53  ? 79   ARG A CA  1 
ATOM   575  C  C   . ARG A 1 79  ? -33.485 55.005  -2.052  1.00 32.29  ? 79   ARG A C   1 
ATOM   576  O  O   . ARG A 1 79  ? -33.429 55.223  -3.273  1.00 30.58  ? 79   ARG A O   1 
ATOM   577  C  CB  . ARG A 1 79  ? -34.413 52.845  -1.278  1.00 26.92  ? 79   ARG A CB  1 
ATOM   578  C  CG  . ARG A 1 79  ? -34.161 52.137  -2.589  1.00 23.98  ? 79   ARG A CG  1 
ATOM   579  C  CD  . ARG A 1 79  ? -33.609 50.731  -2.382  1.00 30.10  ? 79   ARG A CD  1 
ATOM   580  N  NE  . ARG A 1 79  ? -32.148 50.707  -2.368  1.00 27.32  ? 79   ARG A NE  1 
ATOM   581  C  CZ  . ARG A 1 79  ? -31.406 49.610  -2.403  1.00 28.69  ? 79   ARG A CZ  1 
ATOM   582  N  NH1 . ARG A 1 79  ? -31.983 48.409  -2.438  1.00 29.59  ? 79   ARG A NH1 1 
ATOM   583  N  NH2 . ARG A 1 79  ? -30.078 49.714  -2.387  1.00 27.64  ? 79   ARG A NH2 1 
ATOM   584  N  N   . HIS A 1 80  ? -32.509 55.318  -1.200  1.00 28.30  ? 80   HIS A N   1 
ATOM   585  C  CA  . HIS A 1 80  ? -31.175 55.684  -1.660  1.00 27.50  ? 80   HIS A CA  1 
ATOM   586  C  C   . HIS A 1 80  ? -30.511 54.452  -2.255  1.00 29.21  ? 80   HIS A C   1 
ATOM   587  O  O   . HIS A 1 80  ? -30.806 53.322  -1.839  1.00 30.07  ? 80   HIS A O   1 
ATOM   588  C  CB  . HIS A 1 80  ? -30.310 56.135  -0.485  1.00 28.27  ? 80   HIS A CB  1 
ATOM   589  C  CG  . HIS A 1 80  ? -30.837 57.322  0.254   1.00 27.31  ? 80   HIS A CG  1 
ATOM   590  N  ND1 . HIS A 1 80  ? -30.920 57.365  1.628   1.00 28.73  ? 80   HIS A ND1 1 
ATOM   591  C  CD2 . HIS A 1 80  ? -31.295 58.515  -0.185  1.00 25.99  ? 80   HIS A CD2 1 
ATOM   592  C  CE1 . HIS A 1 80  ? -31.393 58.535  2.006   1.00 24.57  ? 80   HIS A CE1 1 
ATOM   593  N  NE2 . HIS A 1 80  ? -31.632 59.251  0.925   1.00 26.74  ? 80   HIS A NE2 1 
ATOM   594  N  N   . VAL A 1 81  ? -29.590 54.647  -3.194  1.00 26.69  ? 81   VAL A N   1 
ATOM   595  C  CA  . VAL A 1 81  ? -28.841 53.503  -3.717  1.00 26.02  ? 81   VAL A CA  1 
ATOM   596  C  C   . VAL A 1 81  ? -28.094 52.795  -2.585  1.00 26.26  ? 81   VAL A C   1 
ATOM   597  O  O   . VAL A 1 81  ? -28.078 51.566  -2.497  1.00 27.48  ? 81   VAL A O   1 
ATOM   598  C  CB  . VAL A 1 81  ? -27.827 53.911  -4.813  1.00 28.51  ? 81   VAL A CB  1 
ATOM   599  C  CG1 . VAL A 1 81  ? -26.853 52.779  -5.083  1.00 23.18  ? 81   VAL A CG1 1 
ATOM   600  C  CG2 . VAL A 1 81  ? -28.554 54.322  -6.108  1.00 30.83  ? 81   VAL A CG2 1 
ATOM   601  N  N   . GLY A 1 82  ? -27.457 53.573  -1.720  1.00 25.21  ? 82   GLY A N   1 
ATOM   602  C  CA  . GLY A 1 82  ? -26.683 52.978  -0.647  1.00 24.54  ? 82   GLY A CA  1 
ATOM   603  C  C   . GLY A 1 82  ? -27.512 52.348  0.465   1.00 25.79  ? 82   GLY A C   1 
ATOM   604  O  O   . GLY A 1 82  ? -26.931 51.913  1.445   1.00 24.09  ? 82   GLY A O   1 
ATOM   605  N  N   . ASP A 1 83  ? -28.847 52.295  0.320   1.00 26.29  ? 83   ASP A N   1 
ATOM   606  C  CA  . ASP A 1 83  ? -29.733 51.771  1.372   1.00 22.72  ? 83   ASP A CA  1 
ATOM   607  C  C   . ASP A 1 83  ? -29.839 50.239  1.487   1.00 26.35  ? 83   ASP A C   1 
ATOM   608  O  O   . ASP A 1 83  ? -30.745 49.635  0.915   1.00 24.92  ? 83   ASP A O   1 
ATOM   609  C  CB  . ASP A 1 83  ? -31.132 52.363  1.256   1.00 25.87  ? 83   ASP A CB  1 
ATOM   610  C  CG  . ASP A 1 83  ? -31.186 53.789  1.722   1.00 27.18  ? 83   ASP A CG  1 
ATOM   611  O  OD1 . ASP A 1 83  ? -32.252 54.430  1.577   1.00 26.63  ? 83   ASP A OD1 1 
ATOM   612  O  OD2 . ASP A 1 83  ? -30.147 54.266  2.223   1.00 24.06  ? 83   ASP A OD2 1 
ATOM   613  N  N   . LEU A 1 84  ? -28.941 49.625  2.265   1.00 23.41  ? 84   LEU A N   1 
ATOM   614  C  CA  . LEU A 1 84  ? -28.889 48.170  2.363   1.00 26.18  ? 84   LEU A CA  1 
ATOM   615  C  C   . LEU A 1 84  ? -29.753 47.598  3.473   1.00 27.49  ? 84   LEU A C   1 
ATOM   616  O  O   . LEU A 1 84  ? -29.858 46.392  3.612   1.00 28.65  ? 84   LEU A O   1 
ATOM   617  C  CB  . LEU A 1 84  ? -27.450 47.683  2.551   1.00 24.42  ? 84   LEU A CB  1 
ATOM   618  C  CG  . LEU A 1 84  ? -26.626 47.945  1.308   1.00 23.90  ? 84   LEU A CG  1 
ATOM   619  C  CD1 . LEU A 1 84  ? -25.154 47.473  1.468   1.00 19.23  ? 84   LEU A CD1 1 
ATOM   620  C  CD2 . LEU A 1 84  ? -27.342 47.265  0.129   1.00 21.87  ? 84   LEU A CD2 1 
ATOM   621  N  N   . GLY A 1 85  ? -30.350 48.460  4.277   1.00 25.98  ? 85   GLY A N   1 
ATOM   622  C  CA  . GLY A 1 85  ? -31.260 48.000  5.297   1.00 26.96  ? 85   GLY A CA  1 
ATOM   623  C  C   . GLY A 1 85  ? -30.625 47.764  6.644   1.00 28.49  ? 85   GLY A C   1 
ATOM   624  O  O   . GLY A 1 85  ? -29.871 48.596  7.152   1.00 27.89  ? 85   GLY A O   1 
ATOM   625  N  N   . ASN A 1 86  ? -30.961 46.623  7.237   1.00 28.17  ? 86   ASN A N   1 
ATOM   626  C  CA  . ASN A 1 86  ? -30.446 46.266  8.537   1.00 24.87  ? 86   ASN A CA  1 
ATOM   627  C  C   . ASN A 1 86  ? -29.551 45.040  8.521   1.00 28.68  ? 86   ASN A C   1 
ATOM   628  O  O   . ASN A 1 86  ? -29.677 44.145  7.677   1.00 27.10  ? 86   ASN A O   1 
ATOM   629  C  CB  . ASN A 1 86  ? -31.584 46.039  9.524   1.00 28.27  ? 86   ASN A CB  1 
ATOM   630  C  CG  . ASN A 1 86  ? -32.168 47.327  10.040  1.00 29.62  ? 86   ASN A CG  1 
ATOM   631  O  OD1 . ASN A 1 86  ? -31.571 47.991  10.895  1.00 28.38  ? 86   ASN A OD1 1 
ATOM   632  N  ND2 . ASN A 1 86  ? -33.352 47.688  9.538   1.00 25.59  ? 86   ASN A ND2 1 
ATOM   633  N  N   . VAL A 1 87  ? -28.649 45.017  9.488   1.00 24.77  ? 87   VAL A N   1 
ATOM   634  C  CA  . VAL A 1 87  ? -27.807 43.874  9.717   1.00 29.40  ? 87   VAL A CA  1 
ATOM   635  C  C   . VAL A 1 87  ? -28.061 43.416  11.169  1.00 27.60  ? 87   VAL A C   1 
ATOM   636  O  O   . VAL A 1 87  ? -28.273 44.247  12.059  1.00 29.72  ? 87   VAL A O   1 
ATOM   637  C  CB  . VAL A 1 87  ? -26.348 44.258  9.379   1.00 27.80  ? 87   VAL A CB  1 
ATOM   638  C  CG1 . VAL A 1 87  ? -25.424 44.091  10.553  1.00 30.49  ? 87   VAL A CG1 1 
ATOM   639  C  CG2 . VAL A 1 87  ? -25.865 43.513  8.139   1.00 25.61  ? 87   VAL A CG2 1 
ATOM   640  N  N   . THR A 1 88  ? -28.109 42.111  11.416  1.00 28.78  ? 88   THR A N   1 
ATOM   641  C  CA  . THR A 1 88  ? -28.548 41.651  12.743  1.00 29.69  ? 88   THR A CA  1 
ATOM   642  C  C   . THR A 1 88  ? -27.448 40.977  13.578  1.00 29.70  ? 88   THR A C   1 
ATOM   643  O  O   . THR A 1 88  ? -26.818 40.017  13.141  1.00 28.20  ? 88   THR A O   1 
ATOM   644  C  CB  . THR A 1 88  ? -29.840 40.776  12.660  1.00 32.42  ? 88   THR A CB  1 
ATOM   645  O  OG1 . THR A 1 88  ? -30.912 41.549  12.098  1.00 33.07  ? 88   THR A OG1 1 
ATOM   646  C  CG2 . THR A 1 88  ? -30.265 40.325  14.038  1.00 34.11  ? 88   THR A CG2 1 
ATOM   647  N  N   . ALA A 1 89  ? -27.210 41.513  14.774  1.00 30.07  ? 89   ALA A N   1 
ATOM   648  C  CA  . ALA A 1 89  ? -26.237 40.931  15.702  1.00 32.60  ? 89   ALA A CA  1 
ATOM   649  C  C   . ALA A 1 89  ? -26.899 39.991  16.709  1.00 35.70  ? 89   ALA A C   1 
ATOM   650  O  O   . ALA A 1 89  ? -27.961 40.303  17.258  1.00 30.46  ? 89   ALA A O   1 
ATOM   651  C  CB  . ALA A 1 89  ? -25.471 42.022  16.435  1.00 28.77  ? 89   ALA A CB  1 
ATOM   652  N  N   . ASP A 1 90  ? -26.259 38.844  16.949  1.00 36.60  ? 90   ASP A N   1 
ATOM   653  C  CA  . ASP A 1 90  ? -26.733 37.872  17.940  1.00 35.16  ? 90   ASP A CA  1 
ATOM   654  C  C   . ASP A 1 90  ? -26.349 38.258  19.384  1.00 36.56  ? 90   ASP A C   1 
ATOM   655  O  O   . ASP A 1 90  ? -25.747 39.309  19.621  1.00 37.45  ? 90   ASP A O   1 
ATOM   656  C  CB  . ASP A 1 90  ? -26.274 36.444  17.579  1.00 36.24  ? 90   ASP A CB  1 
ATOM   657  C  CG  . ASP A 1 90  ? -24.761 36.243  17.712  1.00 37.45  ? 90   ASP A CG  1 
ATOM   658  O  OD1 . ASP A 1 90  ? -24.102 36.990  18.467  1.00 37.37  ? 90   ASP A OD1 1 
ATOM   659  O  OD2 . ASP A 1 90  ? -24.230 35.318  17.064  1.00 38.68  ? 90   ASP A OD2 1 
ATOM   660  N  N   . LYS A 1 91  ? -26.703 37.410  20.342  1.00 38.82  ? 91   LYS A N   1 
ATOM   661  C  CA  . LYS A 1 91  ? -26.522 37.741  21.757  1.00 41.50  ? 91   LYS A CA  1 
ATOM   662  C  C   . LYS A 1 91  ? -25.047 38.000  22.094  1.00 41.39  ? 91   LYS A C   1 
ATOM   663  O  O   . LYS A 1 91  ? -24.736 38.742  23.023  1.00 41.67  ? 91   LYS A O   1 
ATOM   664  C  CB  . LYS A 1 91  ? -27.084 36.624  22.645  1.00 39.03  ? 91   LYS A CB  1 
ATOM   665  C  CG  . LYS A 1 91  ? -26.292 35.333  22.535  1.00 44.47  ? 91   LYS A CG  1 
ATOM   666  C  CD  . LYS A 1 91  ? -26.995 34.171  23.218  1.00 58.72  ? 91   LYS A CD  1 
ATOM   667  C  CE  . LYS A 1 91  ? -26.535 32.823  22.652  1.00 57.96  ? 91   LYS A CE  1 
ATOM   668  N  NZ  . LYS A 1 91  ? -25.064 32.581  22.821  1.00 60.92  ? 91   LYS A NZ  1 
ATOM   669  N  N   . ASP A 1 92  ? -24.144 37.384  21.339  1.00 38.54  ? 92   ASP A N   1 
ATOM   670  C  CA  . ASP A 1 92  ? -22.711 37.599  21.530  1.00 39.98  ? 92   ASP A CA  1 
ATOM   671  C  C   . ASP A 1 92  ? -22.133 38.822  20.786  1.00 40.31  ? 92   ASP A C   1 
ATOM   672  O  O   . ASP A 1 92  ? -20.930 39.074  20.849  1.00 38.28  ? 92   ASP A O   1 
ATOM   673  C  CB  . ASP A 1 92  ? -21.943 36.335  21.139  1.00 40.66  ? 92   ASP A CB  1 
ATOM   674  C  CG  . ASP A 1 92  ? -22.279 35.161  22.040  1.00 49.80  ? 92   ASP A CG  1 
ATOM   675  O  OD1 . ASP A 1 92  ? -22.337 35.372  23.281  1.00 43.31  ? 92   ASP A OD1 1 
ATOM   676  O  OD2 . ASP A 1 92  ? -22.503 34.046  21.506  1.00 46.94  ? 92   ASP A OD2 1 
ATOM   677  N  N   . GLY A 1 93  ? -22.984 39.566  20.075  1.00 38.90  ? 93   GLY A N   1 
ATOM   678  C  CA  . GLY A 1 93  ? -22.565 40.796  19.416  1.00 34.08  ? 93   GLY A CA  1 
ATOM   679  C  C   . GLY A 1 93  ? -21.965 40.555  18.048  1.00 32.07  ? 93   GLY A C   1 
ATOM   680  O  O   . GLY A 1 93  ? -21.219 41.385  17.534  1.00 28.25  ? 93   GLY A O   1 
ATOM   681  N  N   . VAL A 1 94  ? -22.290 39.402  17.473  1.00 30.58  ? 94   VAL A N   1 
ATOM   682  C  CA  . VAL A 1 94  ? -21.822 39.037  16.149  1.00 34.10  ? 94   VAL A CA  1 
ATOM   683  C  C   . VAL A 1 94  ? -22.943 39.113  15.119  1.00 30.77  ? 94   VAL A C   1 
ATOM   684  O  O   . VAL A 1 94  ? -23.991 38.511  15.298  1.00 31.16  ? 94   VAL A O   1 
ATOM   685  C  CB  . VAL A 1 94  ? -21.234 37.597  16.127  1.00 34.95  ? 94   VAL A CB  1 
ATOM   686  C  CG1 . VAL A 1 94  ? -21.010 37.131  14.696  1.00 33.11  ? 94   VAL A CG1 1 
ATOM   687  C  CG2 . VAL A 1 94  ? -19.945 37.539  16.913  1.00 31.00  ? 94   VAL A CG2 1 
ATOM   688  N  N   . ALA A 1 95  ? -22.706 39.852  14.041  1.00 30.67  ? 95   ALA A N   1 
ATOM   689  C  CA  . ALA A 1 95  ? -23.586 39.821  12.878  1.00 30.25  ? 95   ALA A CA  1 
ATOM   690  C  C   . ALA A 1 95  ? -22.935 39.033  11.734  1.00 30.94  ? 95   ALA A C   1 
ATOM   691  O  O   . ALA A 1 95  ? -21.898 39.436  11.213  1.00 31.98  ? 95   ALA A O   1 
ATOM   692  C  CB  . ALA A 1 95  ? -23.917 41.228  12.436  1.00 26.78  ? 95   ALA A CB  1 
ATOM   693  N  N   . ASP A 1 96  ? -23.527 37.904  11.359  1.00 30.96  ? 96   ASP A N   1 
ATOM   694  C  CA  . ASP A 1 96  ? -23.021 37.142  10.221  1.00 35.51  ? 96   ASP A CA  1 
ATOM   695  C  C   . ASP A 1 96  ? -23.750 37.613  8.982   1.00 36.05  ? 96   ASP A C   1 
ATOM   696  O  O   . ASP A 1 96  ? -24.813 37.092  8.629   1.00 36.99  ? 96   ASP A O   1 
ATOM   697  C  CB  . ASP A 1 96  ? -23.145 35.621  10.427  1.00 33.24  ? 96   ASP A CB  1 
ATOM   698  C  CG  . ASP A 1 96  ? -22.104 35.069  11.441  1.00 43.92  ? 96   ASP A CG  1 
ATOM   699  O  OD1 . ASP A 1 96  ? -20.886 35.360  11.317  1.00 35.25  ? 96   ASP A OD1 1 
ATOM   700  O  OD2 . ASP A 1 96  ? -22.509 34.340  12.373  1.00 48.51  ? 96   ASP A OD2 1 
ATOM   701  N  N   . VAL A 1 97  ? -23.176 38.616  8.329   1.00 31.91  ? 97   VAL A N   1 
ATOM   702  C  CA  . VAL A 1 97  ? -23.894 39.339  7.298   1.00 29.99  ? 97   VAL A CA  1 
ATOM   703  C  C   . VAL A 1 97  ? -24.063 38.474  6.047   1.00 31.76  ? 97   VAL A C   1 
ATOM   704  O  O   . VAL A 1 97  ? -23.147 37.790  5.612   1.00 29.83  ? 97   VAL A O   1 
ATOM   705  C  CB  . VAL A 1 97  ? -23.187 40.664  6.947   1.00 30.52  ? 97   VAL A CB  1 
ATOM   706  C  CG1 . VAL A 1 97  ? -24.004 41.456  5.955   1.00 28.83  ? 97   VAL A CG1 1 
ATOM   707  C  CG2 . VAL A 1 97  ? -22.926 41.501  8.205   1.00 26.48  ? 97   VAL A CG2 1 
ATOM   708  N  N   . SER A 1 98  ? -25.264 38.496  5.491   1.00 33.22  ? 98   SER A N   1 
ATOM   709  C  CA  . SER A 1 98  ? -25.536 37.861  4.207   1.00 35.34  ? 98   SER A CA  1 
ATOM   710  C  C   . SER A 1 98  ? -26.594 38.708  3.530   1.00 34.23  ? 98   SER A C   1 
ATOM   711  O  O   . SER A 1 98  ? -27.711 38.817  4.028   1.00 33.70  ? 98   SER A O   1 
ATOM   712  C  CB  . SER A 1 98  ? -26.067 36.426  4.386   1.00 37.91  ? 98   SER A CB  1 
ATOM   713  O  OG  . SER A 1 98  ? -26.732 35.969  3.205   1.00 35.99  ? 98   SER A OG  1 
ATOM   714  N  N   . ILE A 1 99  ? -26.250 39.316  2.402   1.00 33.51  ? 99   ILE A N   1 
ATOM   715  C  CA  . ILE A 1 99  ? -27.190 40.207  1.748   1.00 32.34  ? 99   ILE A CA  1 
ATOM   716  C  C   . ILE A 1 99  ? -27.046 40.155  0.238   1.00 32.78  ? 99   ILE A C   1 
ATOM   717  O  O   . ILE A 1 99  ? -25.944 40.040  -0.293  1.00 34.16  ? 99   ILE A O   1 
ATOM   718  C  CB  . ILE A 1 99  ? -26.993 41.674  2.195   1.00 31.56  ? 99   ILE A CB  1 
ATOM   719  C  CG1 . ILE A 1 99  ? -27.308 41.852  3.685   1.00 32.93  ? 99   ILE A CG1 1 
ATOM   720  C  CG2 . ILE A 1 99  ? -27.862 42.598  1.348   1.00 29.94  ? 99   ILE A CG2 1 
ATOM   721  C  CD1 . ILE A 1 99  ? -27.018 43.256  4.234   1.00 25.35  ? 99   ILE A CD1 1 
ATOM   722  N  N   . GLU A 1 100 ? -28.169 40.252  -0.452  1.00 32.75  ? 100  GLU A N   1 
ATOM   723  C  CA  . GLU A 1 100 ? -28.155 40.308  -1.899  1.00 33.26  ? 100  GLU A CA  1 
ATOM   724  C  C   . GLU A 1 100 ? -28.881 41.571  -2.294  1.00 33.23  ? 100  GLU A C   1 
ATOM   725  O  O   . GLU A 1 100 ? -30.004 41.815  -1.868  1.00 33.28  ? 100  GLU A O   1 
ATOM   726  C  CB  . GLU A 1 100 ? -28.836 39.081  -2.493  1.00 32.15  ? 100  GLU A CB  1 
ATOM   727  C  CG  . GLU A 1 100 ? -28.772 39.019  -4.000  1.00 44.92  ? 100  GLU A CG  1 
ATOM   728  C  CD  . GLU A 1 100 ? -29.621 37.895  -4.597  1.00 56.88  ? 100  GLU A CD  1 
ATOM   729  O  OE1 . GLU A 1 100 ? -30.063 36.996  -3.842  1.00 56.23  ? 100  GLU A OE1 1 
ATOM   730  O  OE2 . GLU A 1 100 ? -29.850 37.919  -5.829  1.00 59.71  ? 100  GLU A OE2 1 
ATOM   731  N  N   . ASP A 1 101 ? -28.226 42.408  -3.080  1.00 34.50  ? 101  ASP A N   1 
ATOM   732  C  CA  . ASP A 1 101 ? -28.857 43.643  -3.490  1.00 31.83  ? 101  ASP A CA  1 
ATOM   733  C  C   . ASP A 1 101 ? -28.598 43.861  -4.963  1.00 34.39  ? 101  ASP A C   1 
ATOM   734  O  O   . ASP A 1 101 ? -27.505 43.590  -5.462  1.00 33.99  ? 101  ASP A O   1 
ATOM   735  C  CB  . ASP A 1 101 ? -28.357 44.823  -2.660  1.00 24.15  ? 101  ASP A CB  1 
ATOM   736  C  CG  . ASP A 1 101 ? -29.235 46.047  -2.813  1.00 30.79  ? 101  ASP A CG  1 
ATOM   737  O  OD1 . ASP A 1 101 ? -30.325 46.084  -2.208  1.00 36.83  ? 101  ASP A OD1 1 
ATOM   738  O  OD2 . ASP A 1 101 ? -28.850 46.985  -3.540  1.00 31.79  ? 101  ASP A OD2 1 
ATOM   739  N  N   . SER A 1 102 ? -29.614 44.365  -5.648  1.00 33.07  ? 102  SER A N   1 
ATOM   740  C  CA  . SER A 1 102 ? -29.569 44.489  -7.088  1.00 33.47  ? 102  SER A CA  1 
ATOM   741  C  C   . SER A 1 102 ? -29.561 45.956  -7.481  1.00 34.84  ? 102  SER A C   1 
ATOM   742  O  O   . SER A 1 102 ? -29.605 46.272  -8.654  1.00 33.65  ? 102  SER A O   1 
ATOM   743  C  CB  . SER A 1 102 ? -30.804 43.828  -7.695  1.00 40.85  ? 102  SER A CB  1 
ATOM   744  O  OG  . SER A 1 102 ? -31.921 44.704  -7.573  1.00 50.61  ? 102  SER A OG  1 
ATOM   745  N  N   . VAL A 1 103 ? -29.519 46.852  -6.500  1.00 31.07  ? 103  VAL A N   1 
ATOM   746  C  CA  . VAL A 1 103 ? -29.440 48.274  -6.796  1.00 31.30  ? 103  VAL A CA  1 
ATOM   747  C  C   . VAL A 1 103 ? -27.985 48.800  -6.727  1.00 32.26  ? 103  VAL A C   1 
ATOM   748  O  O   . VAL A 1 103 ? -27.541 49.563  -7.588  1.00 29.93  ? 103  VAL A O   1 
ATOM   749  C  CB  . VAL A 1 103 ? -30.389 49.097  -5.886  1.00 31.33  ? 103  VAL A CB  1 
ATOM   750  C  CG1 . VAL A 1 103 ? -30.204 50.577  -6.122  1.00 25.64  ? 103  VAL A CG1 1 
ATOM   751  C  CG2 . VAL A 1 103 ? -31.838 48.671  -6.106  1.00 27.23  ? 103  VAL A CG2 1 
ATOM   752  N  N   . ILE A 1 104 ? -27.236 48.397  -5.712  1.00 29.16  ? 104  ILE A N   1 
ATOM   753  C  CA  . ILE A 1 104 ? -25.830 48.744  -5.711  1.00 28.75  ? 104  ILE A CA  1 
ATOM   754  C  C   . ILE A 1 104 ? -25.157 47.987  -6.840  1.00 26.01  ? 104  ILE A C   1 
ATOM   755  O  O   . ILE A 1 104 ? -25.740 47.092  -7.436  1.00 26.99  ? 104  ILE A O   1 
ATOM   756  C  CB  . ILE A 1 104 ? -25.109 48.383  -4.368  1.00 26.68  ? 104  ILE A CB  1 
ATOM   757  C  CG1 . ILE A 1 104 ? -25.149 46.876  -4.109  1.00 26.01  ? 104  ILE A CG1 1 
ATOM   758  C  CG2 . ILE A 1 104 ? -25.699 49.160  -3.210  1.00 32.22  ? 104  ILE A CG2 1 
ATOM   759  C  CD1 . ILE A 1 104 ? -24.413 46.443  -2.842  1.00 30.04  ? 104  ILE A CD1 1 
ATOM   760  N  N   . SER A 1 105 ? -23.899 48.312  -7.082  1.00 26.83  ? 105  SER A N   1 
ATOM   761  C  CA  . SER A 1 105 ? -23.138 47.659  -8.117  1.00 29.98  ? 105  SER A CA  1 
ATOM   762  C  C   . SER A 1 105 ? -21.658 47.872  -7.889  1.00 28.19  ? 105  SER A C   1 
ATOM   763  O  O   . SER A 1 105 ? -21.262 48.804  -7.211  1.00 28.37  ? 105  SER A O   1 
ATOM   764  C  CB  . SER A 1 105 ? -23.544 48.213  -9.486  1.00 29.46  ? 105  SER A CB  1 
ATOM   765  O  OG  . SER A 1 105 ? -22.741 47.651  -10.498 1.00 40.95  ? 105  SER A OG  1 
ATOM   766  N  N   . LEU A 1 106 ? -20.837 47.001  -8.459  1.00 30.10  ? 106  LEU A N   1 
ATOM   767  C  CA  . LEU A 1 106 ? -19.393 47.171  -8.372  1.00 29.89  ? 106  LEU A CA  1 
ATOM   768  C  C   . LEU A 1 106 ? -18.843 47.856  -9.624  1.00 31.24  ? 106  LEU A C   1 
ATOM   769  O  O   . LEU A 1 106 ? -17.634 48.015  -9.779  1.00 32.60  ? 106  LEU A O   1 
ATOM   770  C  CB  . LEU A 1 106 ? -18.692 45.839  -8.126  1.00 32.22  ? 106  LEU A CB  1 
ATOM   771  C  CG  . LEU A 1 106 ? -19.125 45.073  -6.882  1.00 29.40  ? 106  LEU A CG  1 
ATOM   772  C  CD1 . LEU A 1 106 ? -18.133 43.939  -6.609  1.00 24.20  ? 106  LEU A CD1 1 
ATOM   773  C  CD2 . LEU A 1 106 ? -19.222 46.041  -5.723  1.00 22.10  ? 106  LEU A CD2 1 
ATOM   774  N  N   . SER A 1 107 ? -19.735 48.281  -10.508 1.00 29.72  ? 107  SER A N   1 
ATOM   775  C  CA  . SER A 1 107 ? -19.325 49.162  -11.596 1.00 33.02  ? 107  SER A CA  1 
ATOM   776  C  C   . SER A 1 107 ? -20.475 50.077  -11.998 1.00 37.55  ? 107  SER A C   1 
ATOM   777  O  O   . SER A 1 107 ? -21.613 49.888  -11.553 1.00 36.47  ? 107  SER A O   1 
ATOM   778  C  CB  . SER A 1 107 ? -18.849 48.353  -12.803 1.00 32.56  ? 107  SER A CB  1 
ATOM   779  O  OG  . SER A 1 107 ? -19.912 47.580  -13.329 1.00 42.38  ? 107  SER A OG  1 
ATOM   780  N  N   . GLY A 1 108 ? -20.179 51.075  -12.824 1.00 35.79  ? 108  GLY A N   1 
ATOM   781  C  CA  . GLY A 1 108 ? -21.225 51.904  -13.391 1.00 36.38  ? 108  GLY A CA  1 
ATOM   782  C  C   . GLY A 1 108 ? -21.686 53.045  -12.508 1.00 37.26  ? 108  GLY A C   1 
ATOM   783  O  O   . GLY A 1 108 ? -20.965 53.473  -11.607 1.00 35.42  ? 108  GLY A O   1 
ATOM   784  N  N   . ASP A 1 109 ? -22.897 53.532  -12.779 1.00 38.43  ? 109  ASP A N   1 
ATOM   785  C  CA  . ASP A 1 109 ? -23.468 54.668  -12.063 1.00 40.48  ? 109  ASP A CA  1 
ATOM   786  C  C   . ASP A 1 109 ? -23.793 54.347  -10.609 1.00 40.13  ? 109  ASP A C   1 
ATOM   787  O  O   . ASP A 1 109 ? -23.869 55.248  -9.773  1.00 39.91  ? 109  ASP A O   1 
ATOM   788  C  CB  . ASP A 1 109 ? -24.732 55.176  -12.769 1.00 49.43  ? 109  ASP A CB  1 
ATOM   789  C  CG  . ASP A 1 109 ? -24.435 55.795  -14.135 1.00 59.73  ? 109  ASP A CG  1 
ATOM   790  O  OD1 . ASP A 1 109 ? -23.244 56.064  -14.411 1.00 55.61  ? 109  ASP A OD1 1 
ATOM   791  O  OD2 . ASP A 1 109 ? -25.389 56.015  -14.924 1.00 62.56  ? 109  ASP A OD2 1 
ATOM   792  N  N   . HIS A 1 110 ? -23.997 53.068  -10.313 1.00 33.18  ? 110  HIS A N   1 
ATOM   793  C  CA  . HIS A 1 110 ? -24.316 52.645  -8.956  1.00 31.88  ? 110  HIS A CA  1 
ATOM   794  C  C   . HIS A 1 110 ? -23.093 52.012  -8.308  1.00 33.56  ? 110  HIS A C   1 
ATOM   795  O  O   . HIS A 1 110 ? -23.201 51.298  -7.314  1.00 31.49  ? 110  HIS A O   1 
ATOM   796  C  CB  . HIS A 1 110 ? -25.496 51.666  -8.961  1.00 27.67  ? 110  HIS A CB  1 
ATOM   797  C  CG  . HIS A 1 110 ? -26.807 52.306  -9.289  1.00 27.88  ? 110  HIS A CG  1 
ATOM   798  N  ND1 . HIS A 1 110 ? -28.004 51.628  -9.226  1.00 32.86  ? 110  HIS A ND1 1 
ATOM   799  C  CD2 . HIS A 1 110 ? -27.112 53.567  -9.675  1.00 26.98  ? 110  HIS A CD2 1 
ATOM   800  C  CE1 . HIS A 1 110 ? -28.992 52.444  -9.556  1.00 30.01  ? 110  HIS A CE1 1 
ATOM   801  N  NE2 . HIS A 1 110 ? -28.476 53.627  -9.835  1.00 29.99  ? 110  HIS A NE2 1 
ATOM   802  N  N   . CYS A 1 111 ? -21.926 52.273  -8.883  1.00 32.27  ? 111  CYS A N   1 
ATOM   803  C  CA  . CYS A 1 111 ? -20.705 51.685  -8.382  1.00 30.87  ? 111  CYS A CA  1 
ATOM   804  C  C   . CYS A 1 111 ? -20.432 52.197  -6.958  1.00 30.23  ? 111  CYS A C   1 
ATOM   805  O  O   . CYS A 1 111 ? -20.511 53.393  -6.712  1.00 29.18  ? 111  CYS A O   1 
ATOM   806  C  CB  . CYS A 1 111 ? -19.538 52.005  -9.313  1.00 26.16  ? 111  CYS A CB  1 
ATOM   807  S  SG  . CYS A 1 111 ? -17.973 51.346  -8.711  1.00 32.81  ? 111  CYS A SG  1 
ATOM   808  N  N   . ILE A 1 112 ? -20.109 51.287  -6.041  1.00 23.84  ? 112  ILE A N   1 
ATOM   809  C  CA  . ILE A 1 112 ? -19.845 51.648  -4.655  1.00 28.48  ? 112  ILE A CA  1 
ATOM   810  C  C   . ILE A 1 112 ? -18.390 51.456  -4.296  1.00 28.08  ? 112  ILE A C   1 
ATOM   811  O  O   . ILE A 1 112 ? -18.009 51.620  -3.136  1.00 29.17  ? 112  ILE A O   1 
ATOM   812  C  CB  . ILE A 1 112 ? -20.664 50.813  -3.660  1.00 23.81  ? 112  ILE A CB  1 
ATOM   813  C  CG1 . ILE A 1 112 ? -20.336 49.334  -3.830  1.00 24.72  ? 112  ILE A CG1 1 
ATOM   814  C  CG2 . ILE A 1 112 ? -22.142 51.072  -3.837  1.00 21.84  ? 112  ILE A CG2 1 
ATOM   815  C  CD1 . ILE A 1 112 ? -21.120 48.462  -2.900  1.00 26.25  ? 112  ILE A CD1 1 
ATOM   816  N  N   . ILE A 1 113 ? -17.570 51.122  -5.287  1.00 28.97  ? 113  ILE A N   1 
ATOM   817  C  CA  . ILE A 1 113 ? -16.137 51.039  -5.036  1.00 31.00  ? 113  ILE A CA  1 
ATOM   818  C  C   . ILE A 1 113 ? -15.593 52.432  -4.777  1.00 28.87  ? 113  ILE A C   1 
ATOM   819  O  O   . ILE A 1 113 ? -15.911 53.369  -5.505  1.00 28.97  ? 113  ILE A O   1 
ATOM   820  C  CB  . ILE A 1 113 ? -15.355 50.324  -6.168  1.00 29.67  ? 113  ILE A CB  1 
ATOM   821  C  CG1 . ILE A 1 113 ? -15.548 48.813  -6.041  1.00 28.24  ? 113  ILE A CG1 1 
ATOM   822  C  CG2 . ILE A 1 113 ? -13.868 50.660  -6.091  1.00 23.00  ? 113  ILE A CG2 1 
ATOM   823  C  CD1 . ILE A 1 113 ? -15.497 48.091  -7.344  1.00 29.27  ? 113  ILE A CD1 1 
ATOM   824  N  N   . GLY A 1 114 ? -14.798 52.565  -3.719  1.00 22.74  ? 114  GLY A N   1 
ATOM   825  C  CA  . GLY A 1 114 ? -14.232 53.848  -3.375  1.00 25.60  ? 114  GLY A CA  1 
ATOM   826  C  C   . GLY A 1 114 ? -15.160 54.673  -2.504  1.00 26.48  ? 114  GLY A C   1 
ATOM   827  O  O   . GLY A 1 114 ? -14.884 55.835  -2.214  1.00 26.12  ? 114  GLY A O   1 
ATOM   828  N  N   . ARG A 1 115 ? -16.270 54.070  -2.097  1.00 25.19  ? 115  ARG A N   1 
ATOM   829  C  CA  . ARG A 1 115 ? -17.179 54.698  -1.158  1.00 26.78  ? 115  ARG A CA  1 
ATOM   830  C  C   . ARG A 1 115 ? -17.092 53.981  0.199   1.00 25.61  ? 115  ARG A C   1 
ATOM   831  O  O   . ARG A 1 115 ? -16.392 52.976  0.343   1.00 26.39  ? 115  ARG A O   1 
ATOM   832  C  CB  . ARG A 1 115 ? -18.613 54.687  -1.709  1.00 28.85  ? 115  ARG A CB  1 
ATOM   833  C  CG  . ARG A 1 115 ? -18.736 55.304  -3.111  1.00 26.83  ? 115  ARG A CG  1 
ATOM   834  C  CD  . ARG A 1 115 ? -20.183 55.458  -3.564  1.00 25.54  ? 115  ARG A CD  1 
ATOM   835  N  NE  . ARG A 1 115 ? -20.271 55.954  -4.940  1.00 28.05  ? 115  ARG A NE  1 
ATOM   836  C  CZ  . ARG A 1 115 ? -20.095 57.224  -5.316  1.00 29.67  ? 115  ARG A CZ  1 
ATOM   837  N  NH1 . ARG A 1 115 ? -19.804 58.173  -4.426  1.00 26.16  ? 115  ARG A NH1 1 
ATOM   838  N  NH2 . ARG A 1 115 ? -20.208 57.549  -6.598  1.00 24.20  ? 115  ARG A NH2 1 
ATOM   839  N  N   . THR A 1 116 ? -17.802 54.504  1.182   1.00 20.46  ? 116  THR A N   1 
ATOM   840  C  CA  . THR A 1 116 ? -17.683 54.037  2.555   1.00 23.81  ? 116  THR A CA  1 
ATOM   841  C  C   . THR A 1 116 ? -18.878 53.188  3.008   1.00 24.62  ? 116  THR A C   1 
ATOM   842  O  O   . THR A 1 116 ? -20.044 53.581  2.853   1.00 21.09  ? 116  THR A O   1 
ATOM   843  C  CB  . THR A 1 116 ? -17.512 55.227  3.513   1.00 23.57  ? 116  THR A CB  1 
ATOM   844  O  OG1 . THR A 1 116 ? -16.254 55.856  3.251   1.00 28.00  ? 116  THR A OG1 1 
ATOM   845  C  CG2 . THR A 1 116 ? -17.561 54.765  4.996   1.00 23.76  ? 116  THR A CG2 1 
ATOM   846  N  N   . LEU A 1 117 ? -18.582 52.020  3.557   1.00 19.28  ? 117  LEU A N   1 
ATOM   847  C  CA  . LEU A 1 117 ? -19.624 51.229  4.180   1.00 18.90  ? 117  LEU A CA  1 
ATOM   848  C  C   . LEU A 1 117 ? -19.627 51.560  5.673   1.00 21.59  ? 117  LEU A C   1 
ATOM   849  O  O   . LEU A 1 117 ? -18.571 51.597  6.317   1.00 18.54  ? 117  LEU A O   1 
ATOM   850  C  CB  . LEU A 1 117 ? -19.366 49.755  3.944   1.00 20.16  ? 117  LEU A CB  1 
ATOM   851  C  CG  . LEU A 1 117 ? -20.352 48.713  4.476   1.00 30.87  ? 117  LEU A CG  1 
ATOM   852  C  CD1 . LEU A 1 117 ? -21.720 48.773  3.737   1.00 24.55  ? 117  LEU A CD1 1 
ATOM   853  C  CD2 . LEU A 1 117 ? -19.727 47.303  4.393   1.00 21.38  ? 117  LEU A CD2 1 
ATOM   854  N  N   . VAL A 1 118 ? -20.808 51.846  6.211   1.00 20.20  ? 118  VAL A N   1 
ATOM   855  C  CA  . VAL A 1 118 ? -20.947 52.181  7.612   1.00 17.68  ? 118  VAL A CA  1 
ATOM   856  C  C   . VAL A 1 118 ? -21.939 51.254  8.316   1.00 20.72  ? 118  VAL A C   1 
ATOM   857  O  O   . VAL A 1 118 ? -23.028 50.995  7.805   1.00 21.28  ? 118  VAL A O   1 
ATOM   858  C  CB  . VAL A 1 118 ? -21.417 53.641  7.816   1.00 18.50  ? 118  VAL A CB  1 
ATOM   859  C  CG1 . VAL A 1 118 ? -21.517 53.965  9.302   1.00 16.91  ? 118  VAL A CG1 1 
ATOM   860  C  CG2 . VAL A 1 118 ? -20.496 54.616  7.111   1.00 18.98  ? 118  VAL A CG2 1 
ATOM   861  N  N   . VAL A 1 119 ? -21.563 50.750  9.487   1.00 18.58  ? 119  VAL A N   1 
ATOM   862  C  CA  . VAL A 1 119 ? -22.524 50.067  10.350  1.00 18.98  ? 119  VAL A CA  1 
ATOM   863  C  C   . VAL A 1 119 ? -22.958 51.020  11.485  1.00 20.72  ? 119  VAL A C   1 
ATOM   864  O  O   . VAL A 1 119 ? -22.132 51.620  12.166  1.00 18.30  ? 119  VAL A O   1 
ATOM   865  C  CB  . VAL A 1 119 ? -21.988 48.707  10.861  1.00 19.06  ? 119  VAL A CB  1 
ATOM   866  C  CG1 . VAL A 1 119 ? -20.671 48.871  11.573  1.00 16.87  ? 119  VAL A CG1 1 
ATOM   867  C  CG2 . VAL A 1 119 ? -23.008 48.020  11.745  1.00 19.82  ? 119  VAL A CG2 1 
ATOM   868  N  N   . HIS A 1 120 ? -24.267 51.190  11.636  1.00 23.39  ? 120  HIS A N   1 
ATOM   869  C  CA  . HIS A 1 120 ? -24.816 52.235  12.501  1.00 25.49  ? 120  HIS A CA  1 
ATOM   870  C  C   . HIS A 1 120 ? -25.215 51.729  13.889  1.00 24.71  ? 120  HIS A C   1 
ATOM   871  O  O   . HIS A 1 120 ? -25.379 50.530  14.107  1.00 22.89  ? 120  HIS A O   1 
ATOM   872  C  CB  . HIS A 1 120 ? -25.991 52.960  11.812  1.00 23.80  ? 120  HIS A CB  1 
ATOM   873  C  CG  . HIS A 1 120 ? -25.570 53.871  10.697  1.00 20.48  ? 120  HIS A CG  1 
ATOM   874  N  ND1 . HIS A 1 120 ? -25.342 55.216  10.882  1.00 20.37  ? 120  HIS A ND1 1 
ATOM   875  C  CD2 . HIS A 1 120 ? -25.320 53.625  9.390   1.00 20.59  ? 120  HIS A CD2 1 
ATOM   876  C  CE1 . HIS A 1 120 ? -24.980 55.765  9.736   1.00 23.25  ? 120  HIS A CE1 1 
ATOM   877  N  NE2 . HIS A 1 120 ? -24.961 54.822  8.812   1.00 22.87  ? 120  HIS A NE2 1 
ATOM   878  N  N   . GLU A 1 121 ? -25.363 52.670  14.814  1.00 26.58  ? 121  GLU A N   1 
ATOM   879  C  CA  . GLU A 1 121 ? -25.655 52.375  16.216  1.00 29.55  ? 121  GLU A CA  1 
ATOM   880  C  C   . GLU A 1 121 ? -27.050 51.817  16.479  1.00 30.87  ? 121  GLU A C   1 
ATOM   881  O  O   . GLU A 1 121 ? -27.241 51.031  17.406  1.00 34.05  ? 121  GLU A O   1 
ATOM   882  C  CB  . GLU A 1 121 ? -25.473 53.635  17.046  1.00 26.71  ? 121  GLU A CB  1 
ATOM   883  C  CG  . GLU A 1 121 ? -25.873 53.496  18.481  1.00 25.95  ? 121  GLU A CG  1 
ATOM   884  C  CD  . GLU A 1 121 ? -25.976 54.849  19.163  1.00 36.79  ? 121  GLU A CD  1 
ATOM   885  O  OE1 . GLU A 1 121 ? -26.079 55.874  18.457  1.00 33.95  ? 121  GLU A OE1 1 
ATOM   886  O  OE2 . GLU A 1 121 ? -25.970 54.893  20.411  1.00 44.90  ? 121  GLU A OE2 1 
ATOM   887  N  N   . LYS A 1 122 ? -28.035 52.231  15.695  1.00 27.68  ? 122  LYS A N   1 
ATOM   888  C  CA  . LYS A 1 122 ? -29.389 51.761  15.946  1.00 29.23  ? 122  LYS A CA  1 
ATOM   889  C  C   . LYS A 1 122 ? -29.983 51.073  14.749  1.00 28.17  ? 122  LYS A C   1 
ATOM   890  O  O   . LYS A 1 122 ? -29.387 51.037  13.671  1.00 24.70  ? 122  LYS A O   1 
ATOM   891  C  CB  . LYS A 1 122 ? -30.307 52.909  16.370  1.00 29.46  ? 122  LYS A CB  1 
ATOM   892  C  CG  . LYS A 1 122 ? -29.689 53.857  17.388  1.00 33.85  ? 122  LYS A CG  1 
ATOM   893  C  CD  . LYS A 1 122 ? -30.720 54.417  18.360  1.00 36.49  ? 122  LYS A CD  1 
ATOM   894  C  CE  . LYS A 1 122 ? -30.792 55.931  18.277  1.00 45.68  ? 122  LYS A CE  1 
ATOM   895  N  NZ  . LYS A 1 122 ? -30.761 56.548  19.637  1.00 47.01  ? 122  LYS A NZ  1 
ATOM   896  N  N   . ALA A 1 123 ? -31.174 50.522  14.950  1.00 29.49  ? 123  ALA A N   1 
ATOM   897  C  CA  . ALA A 1 123 ? -31.921 49.933  13.847  1.00 31.62  ? 123  ALA A CA  1 
ATOM   898  C  C   . ALA A 1 123 ? -32.392 51.000  12.842  1.00 27.77  ? 123  ALA A C   1 
ATOM   899  O  O   . ALA A 1 123 ? -32.789 52.108  13.225  1.00 28.47  ? 123  ALA A O   1 
ATOM   900  C  CB  . ALA A 1 123 ? -33.108 49.119  14.375  1.00 26.28  ? 123  ALA A CB  1 
ATOM   901  N  N   . ASP A 1 124 ? -32.320 50.651  11.560  1.00 23.82  ? 124  ASP A N   1 
ATOM   902  C  CA  . ASP A 1 124 ? -32.855 51.462  10.481  1.00 23.95  ? 124  ASP A CA  1 
ATOM   903  C  C   . ASP A 1 124 ? -34.386 51.311  10.433  1.00 29.62  ? 124  ASP A C   1 
ATOM   904  O  O   . ASP A 1 124 ? -34.906 50.186  10.275  1.00 27.93  ? 124  ASP A O   1 
ATOM   905  C  CB  . ASP A 1 124 ? -32.231 50.970  9.171   1.00 24.57  ? 124  ASP A CB  1 
ATOM   906  C  CG  . ASP A 1 124 ? -32.619 51.817  7.960   1.00 27.16  ? 124  ASP A CG  1 
ATOM   907  O  OD1 . ASP A 1 124 ? -33.554 52.657  8.024   1.00 24.66  ? 124  ASP A OD1 1 
ATOM   908  O  OD2 . ASP A 1 124 ? -31.977 51.605  6.922   1.00 28.14  ? 124  ASP A OD2 1 
ATOM   909  N  N   . ASP A 1 125 ? -35.112 52.425  10.569  1.00 28.23  ? 125  ASP A N   1 
ATOM   910  C  CA  . ASP A 1 125 ? -36.585 52.380  10.532  1.00 27.26  ? 125  ASP A CA  1 
ATOM   911  C  C   . ASP A 1 125 ? -37.113 52.281  9.077   1.00 29.87  ? 125  ASP A C   1 
ATOM   912  O  O   . ASP A 1 125 ? -38.314 52.252  8.827   1.00 28.79  ? 125  ASP A O   1 
ATOM   913  C  CB  . ASP A 1 125 ? -37.212 53.559  11.312  1.00 22.60  ? 125  ASP A CB  1 
ATOM   914  C  CG  . ASP A 1 125 ? -37.040 54.927  10.606  1.00 26.69  ? 125  ASP A CG  1 
ATOM   915  O  OD1 . ASP A 1 125 ? -36.775 54.989  9.378   1.00 22.83  ? 125  ASP A OD1 1 
ATOM   916  O  OD2 . ASP A 1 125 ? -37.187 55.959  11.299  1.00 26.78  ? 125  ASP A OD2 1 
ATOM   917  N  N   . LEU A 1 126 ? -36.188 52.228  8.125   1.00 29.61  ? 126  LEU A N   1 
ATOM   918  C  CA  . LEU A 1 126 ? -36.526 51.986  6.725   1.00 29.99  ? 126  LEU A CA  1 
ATOM   919  C  C   . LEU A 1 126 ? -37.326 53.134  6.114   1.00 28.54  ? 126  LEU A C   1 
ATOM   920  O  O   . LEU A 1 126 ? -38.052 52.943  5.142   1.00 31.83  ? 126  LEU A O   1 
ATOM   921  C  CB  . LEU A 1 126 ? -37.258 50.649  6.568   1.00 32.00  ? 126  LEU A CB  1 
ATOM   922  C  CG  . LEU A 1 126 ? -36.536 49.425  7.158   1.00 31.46  ? 126  LEU A CG  1 
ATOM   923  C  CD1 . LEU A 1 126 ? -37.333 48.155  6.909   1.00 23.70  ? 126  LEU A CD1 1 
ATOM   924  C  CD2 . LEU A 1 126 ? -35.155 49.291  6.565   1.00 28.78  ? 126  LEU A CD2 1 
ATOM   925  N  N   . GLY A 1 127 ? -37.173 54.318  6.701   1.00 27.36  ? 127  GLY A N   1 
ATOM   926  C  CA  . GLY A 1 127 ? -37.664 55.564  6.135   1.00 25.67  ? 127  GLY A CA  1 
ATOM   927  C  C   . GLY A 1 127 ? -39.113 55.831  6.479   1.00 28.96  ? 127  GLY A C   1 
ATOM   928  O  O   . GLY A 1 127 ? -39.753 56.672  5.866   1.00 29.47  ? 127  GLY A O   1 
ATOM   929  N  N   . LYS A 1 128 ? -39.622 55.113  7.476   1.00 30.15  ? 128  LYS A N   1 
ATOM   930  C  CA  . LYS A 1 128 ? -41.044 55.111  7.822   1.00 28.77  ? 128  LYS A CA  1 
ATOM   931  C  C   . LYS A 1 128 ? -41.321 55.628  9.218   1.00 25.14  ? 128  LYS A C   1 
ATOM   932  O  O   . LYS A 1 128 ? -42.339 55.264  9.806   1.00 29.34  ? 128  LYS A O   1 
ATOM   933  C  CB  . LYS A 1 128 ? -41.605 53.687  7.733   1.00 25.93  ? 128  LYS A CB  1 
ATOM   934  C  CG  . LYS A 1 128 ? -41.430 53.081  6.363   1.00 30.18  ? 128  LYS A CG  1 
ATOM   935  C  CD  . LYS A 1 128 ? -42.069 51.705  6.299   1.00 39.04  ? 128  LYS A CD  1 
ATOM   936  C  CE  . LYS A 1 128 ? -42.159 51.183  4.858   1.00 38.97  ? 128  LYS A CE  1 
ATOM   937  N  NZ  . LYS A 1 128 ? -40.879 50.602  4.394   1.00 36.14  ? 128  LYS A NZ  1 
ATOM   938  N  N   . GLY A 1 129 ? -40.419 56.448  9.751   1.00 24.55  ? 129  GLY A N   1 
ATOM   939  C  CA  . GLY A 1 129 ? -40.529 56.954  11.115  1.00 25.67  ? 129  GLY A CA  1 
ATOM   940  C  C   . GLY A 1 129 ? -41.314 58.252  11.225  1.00 31.30  ? 129  GLY A C   1 
ATOM   941  O  O   . GLY A 1 129 ? -41.627 58.718  12.331  1.00 27.25  ? 129  GLY A O   1 
ATOM   942  N  N   . GLY A 1 130 ? -41.650 58.829  10.073  1.00 25.69  ? 130  GLY A N   1 
ATOM   943  C  CA  . GLY A 1 130 ? -42.477 60.010  10.039  1.00 25.38  ? 130  GLY A CA  1 
ATOM   944  C  C   . GLY A 1 130 ? -41.819 61.265  10.578  1.00 32.95  ? 130  GLY A C   1 
ATOM   945  O  O   . GLY A 1 130 ? -42.494 62.269  10.773  1.00 35.79  ? 130  GLY A O   1 
ATOM   946  N  N   . ASN A 1 131 ? -40.509 61.229  10.821  1.00 33.27  ? 131  ASN A N   1 
ATOM   947  C  CA  . ASN A 1 131 ? -39.771 62.455  11.150  1.00 31.59  ? 131  ASN A CA  1 
ATOM   948  C  C   . ASN A 1 131 ? -38.749 62.782  10.093  1.00 32.03  ? 131  ASN A C   1 
ATOM   949  O  O   . ASN A 1 131 ? -38.488 61.969  9.200   1.00 36.11  ? 131  ASN A O   1 
ATOM   950  C  CB  . ASN A 1 131 ? -39.104 62.382  12.532  1.00 28.15  ? 131  ASN A CB  1 
ATOM   951  C  CG  . ASN A 1 131 ? -38.125 61.226  12.657  1.00 33.38  ? 131  ASN A CG  1 
ATOM   952  O  OD1 . ASN A 1 131 ? -37.749 60.602  11.664  1.00 36.26  ? 131  ASN A OD1 1 
ATOM   953  N  ND2 . ASN A 1 131 ? -37.707 60.935  13.882  1.00 30.86  ? 131  ASN A ND2 1 
ATOM   954  N  N   . GLU A 1 132 ? -38.165 63.970  10.193  1.00 35.74  ? 132  GLU A N   1 
ATOM   955  C  CA  . GLU A 1 132 ? -37.157 64.415  9.228   1.00 40.77  ? 132  GLU A CA  1 
ATOM   956  C  C   . GLU A 1 132 ? -36.044 63.382  9.093   1.00 36.07  ? 132  GLU A C   1 
ATOM   957  O  O   . GLU A 1 132 ? -35.721 62.924  7.995   1.00 33.95  ? 132  GLU A O   1 
ATOM   958  C  CB  . GLU A 1 132 ? -36.563 65.755  9.671   1.00 46.47  ? 132  GLU A CB  1 
ATOM   959  C  CG  . GLU A 1 132 ? -36.951 66.956  8.790   1.00 56.95  ? 132  GLU A CG  1 
ATOM   960  C  CD  . GLU A 1 132 ? -36.259 66.934  7.431   1.00 65.97  ? 132  GLU A CD  1 
ATOM   961  O  OE1 . GLU A 1 132 ? -35.258 67.682  7.253   1.00 59.98  ? 132  GLU A OE1 1 
ATOM   962  O  OE2 . GLU A 1 132 ? -36.719 66.160  6.552   1.00 64.15  ? 132  GLU A OE2 1 
ATOM   963  N  N   . GLU A 1 133 ? -35.473 63.026  10.236  1.00 30.33  ? 133  GLU A N   1 
ATOM   964  C  CA  . GLU A 1 133 ? -34.377 62.090  10.309  1.00 32.21  ? 133  GLU A CA  1 
ATOM   965  C  C   . GLU A 1 133 ? -34.663 60.762  9.597   1.00 32.20  ? 133  GLU A C   1 
ATOM   966  O  O   . GLU A 1 133 ? -33.804 60.269  8.864   1.00 29.89  ? 133  GLU A O   1 
ATOM   967  C  CB  . GLU A 1 133 ? -34.019 61.833  11.767  1.00 30.37  ? 133  GLU A CB  1 
ATOM   968  C  CG  . GLU A 1 133 ? -32.610 61.291  11.968  1.00 35.54  ? 133  GLU A CG  1 
ATOM   969  C  CD  . GLU A 1 133 ? -31.520 62.145  11.289  1.00 40.63  ? 133  GLU A CD  1 
ATOM   970  O  OE1 . GLU A 1 133 ? -31.735 63.353  11.021  1.00 48.04  ? 133  GLU A OE1 1 
ATOM   971  O  OE2 . GLU A 1 133 ? -30.432 61.597  11.024  1.00 45.21  ? 133  GLU A OE2 1 
ATOM   972  N  N   . SER A 1 134 ? -35.850 60.188  9.806   1.00 27.73  ? 134  SER A N   1 
ATOM   973  C  CA  . SER A 1 134 ? -36.188 58.931  9.138   1.00 29.58  ? 134  SER A CA  1 
ATOM   974  C  C   . SER A 1 134 ? -35.930 59.038  7.659   1.00 26.25  ? 134  SER A C   1 
ATOM   975  O  O   . SER A 1 134 ? -35.354 58.156  7.048   1.00 28.14  ? 134  SER A O   1 
ATOM   976  C  CB  . SER A 1 134 ? -37.652 58.543  9.345   1.00 29.39  ? 134  SER A CB  1 
ATOM   977  O  OG  . SER A 1 134 ? -37.953 57.367  8.611   1.00 25.33  ? 134  SER A OG  1 
ATOM   978  N  N   . THR A 1 135 ? -36.379 60.146  7.106   1.00 31.22  ? 135  THR A N   1 
ATOM   979  C  CA  . THR A 1 135 ? -36.303 60.448  5.691   1.00 31.66  ? 135  THR A CA  1 
ATOM   980  C  C   . THR A 1 135 ? -34.874 60.511  5.130   1.00 29.69  ? 135  THR A C   1 
ATOM   981  O  O   . THR A 1 135 ? -34.668 60.407  3.922   1.00 33.22  ? 135  THR A O   1 
ATOM   982  C  CB  . THR A 1 135 ? -37.064 61.786  5.416   1.00 38.78  ? 135  THR A CB  1 
ATOM   983  O  OG1 . THR A 1 135 ? -37.924 61.615  4.291   1.00 48.94  ? 135  THR A OG1 1 
ATOM   984  C  CG2 . THR A 1 135 ? -36.111 62.954  5.155   1.00 34.42  ? 135  THR A CG2 1 
ATOM   985  N  N   . LYS A 1 136 ? -33.890 60.665  6.004   1.00 29.24  ? 136  LYS A N   1 
ATOM   986  C  CA  . LYS A 1 136 ? -32.497 60.824  5.567   1.00 32.17  ? 136  LYS A CA  1 
ATOM   987  C  C   . LYS A 1 136 ? -31.629 59.624  5.902   1.00 26.87  ? 136  LYS A C   1 
ATOM   988  O  O   . LYS A 1 136 ? -30.854 59.142  5.083   1.00 24.28  ? 136  LYS A O   1 
ATOM   989  C  CB  . LYS A 1 136 ? -31.878 62.066  6.206   1.00 29.52  ? 136  LYS A CB  1 
ATOM   990  C  CG  . LYS A 1 136 ? -32.475 63.359  5.714   1.00 30.01  ? 136  LYS A CG  1 
ATOM   991  C  CD  . LYS A 1 136 ? -31.878 64.522  6.457   1.00 36.82  ? 136  LYS A CD  1 
ATOM   992  C  CE  . LYS A 1 136 ? -32.960 65.427  7.019   1.00 50.15  ? 136  LYS A CE  1 
ATOM   993  N  NZ  . LYS A 1 136 ? -32.377 66.587  7.753   1.00 52.50  ? 136  LYS A NZ  1 
ATOM   994  N  N   . THR A 1 137 ? -31.787 59.131  7.115   1.00 29.44  ? 137  THR A N   1 
ATOM   995  C  CA  . THR A 1 137 ? -30.873 58.137  7.627   1.00 28.82  ? 137  THR A CA  1 
ATOM   996  C  C   . THR A 1 137 ? -31.563 56.985  8.337   1.00 28.03  ? 137  THR A C   1 
ATOM   997  O  O   . THR A 1 137 ? -30.896 56.113  8.900   1.00 27.66  ? 137  THR A O   1 
ATOM   998  C  CB  . THR A 1 137 ? -29.983 58.771  8.652   1.00 27.80  ? 137  THR A CB  1 
ATOM   999  O  OG1 . THR A 1 137 ? -28.859 57.909  8.879   1.00 48.19  ? 137  THR A OG1 1 
ATOM   1000 C  CG2 . THR A 1 137 ? -30.757 58.950  9.913   1.00 18.66  ? 137  THR A CG2 1 
ATOM   1001 N  N   . GLY A 1 138 ? -32.890 56.997  8.333   1.00 24.86  ? 138  GLY A N   1 
ATOM   1002 C  CA  . GLY A 1 138 ? -33.655 55.943  8.963   1.00 24.23  ? 138  GLY A CA  1 
ATOM   1003 C  C   . GLY A 1 138 ? -33.636 55.930  10.492  1.00 26.44  ? 138  GLY A C   1 
ATOM   1004 O  O   . GLY A 1 138 ? -34.004 54.911  11.109  1.00 24.30  ? 138  GLY A O   1 
ATOM   1005 N  N   . ASN A 1 139 ? -33.246 57.049  11.107  1.00 25.33  ? 139  ASN A N   1 
ATOM   1006 C  CA  . ASN A 1 139 ? -32.998 57.097  12.563  1.00 26.11  ? 139  ASN A CA  1 
ATOM   1007 C  C   . ASN A 1 139 ? -32.041 56.010  13.032  1.00 24.01  ? 139  ASN A C   1 
ATOM   1008 O  O   . ASN A 1 139 ? -32.212 55.465  14.119  1.00 25.21  ? 139  ASN A O   1 
ATOM   1009 C  CB  . ASN A 1 139 ? -34.299 57.016  13.403  1.00 25.55  ? 139  ASN A CB  1 
ATOM   1010 C  CG  . ASN A 1 139 ? -35.209 58.239  13.213  1.00 26.43  ? 139  ASN A CG  1 
ATOM   1011 O  OD1 . ASN A 1 139 ? -36.374 58.118  12.819  1.00 29.19  ? 139  ASN A OD1 1 
ATOM   1012 N  ND2 . ASN A 1 139 ? -34.670 59.414  13.476  1.00 26.32  ? 139  ASN A ND2 1 
ATOM   1013 N  N   . ALA A 1 140 ? -31.037 55.708  12.213  1.00 26.38  ? 140  ALA A N   1 
ATOM   1014 C  CA  . ALA A 1 140 ? -30.024 54.702  12.550  1.00 27.14  ? 140  ALA A CA  1 
ATOM   1015 C  C   . ALA A 1 140 ? -28.957 55.183  13.546  1.00 25.91  ? 140  ALA A C   1 
ATOM   1016 O  O   . ALA A 1 140 ? -28.157 54.392  14.044  1.00 27.44  ? 140  ALA A O   1 
ATOM   1017 C  CB  . ALA A 1 140 ? -29.350 54.175  11.282  1.00 26.67  ? 140  ALA A CB  1 
ATOM   1018 N  N   . GLY A 1 141 ? -28.935 56.469  13.847  1.00 25.31  ? 141  GLY A N   1 
ATOM   1019 C  CA  . GLY A 1 141 ? -27.982 56.953  14.828  1.00 26.76  ? 141  GLY A CA  1 
ATOM   1020 C  C   . GLY A 1 141 ? -26.532 56.941  14.363  1.00 28.91  ? 141  GLY A C   1 
ATOM   1021 O  O   . GLY A 1 141 ? -26.213 56.928  13.154  1.00 23.76  ? 141  GLY A O   1 
ATOM   1022 N  N   . SER A 1 142 ? -25.649 56.919  15.351  1.00 27.58  ? 142  SER A N   1 
ATOM   1023 C  CA  . SER A 1 142 ? -24.238 57.210  15.131  1.00 29.26  ? 142  SER A CA  1 
ATOM   1024 C  C   . SER A 1 142 ? -23.535 56.126  14.319  1.00 24.18  ? 142  SER A C   1 
ATOM   1025 O  O   . SER A 1 142 ? -24.033 55.019  14.181  1.00 22.67  ? 142  SER A O   1 
ATOM   1026 C  CB  . SER A 1 142 ? -23.519 57.433  16.480  1.00 30.71  ? 142  SER A CB  1 
ATOM   1027 O  OG  . SER A 1 142 ? -23.324 56.197  17.182  1.00 34.54  ? 142  SER A OG  1 
ATOM   1028 N  N   . ARG A 1 143 ? -22.365 56.468  13.799  1.00 25.58  ? 143  ARG A N   1 
ATOM   1029 C  CA  . ARG A 1 143 ? -21.617 55.603  12.908  1.00 22.85  ? 143  ARG A CA  1 
ATOM   1030 C  C   . ARG A 1 143 ? -20.616 54.828  13.727  1.00 23.84  ? 143  ARG A C   1 
ATOM   1031 O  O   . ARG A 1 143 ? -19.660 55.374  14.262  1.00 25.40  ? 143  ARG A O   1 
ATOM   1032 C  CB  . ARG A 1 143 ? -20.932 56.431  11.831  1.00 20.75  ? 143  ARG A CB  1 
ATOM   1033 C  CG  . ARG A 1 143 ? -21.881 57.450  11.236  1.00 23.46  ? 143  ARG A CG  1 
ATOM   1034 C  CD  . ARG A 1 143 ? -21.271 58.246  10.084  1.00 22.91  ? 143  ARG A CD  1 
ATOM   1035 N  NE  . ARG A 1 143 ? -22.294 59.124  9.515   1.00 26.06  ? 143  ARG A NE  1 
ATOM   1036 C  CZ  . ARG A 1 143 ? -22.169 59.826  8.394   1.00 26.44  ? 143  ARG A CZ  1 
ATOM   1037 N  NH1 . ARG A 1 143 ? -21.037 59.783  7.716   1.00 26.02  ? 143  ARG A NH1 1 
ATOM   1038 N  NH2 . ARG A 1 143 ? -23.183 60.574  7.955   1.00 22.04  ? 143  ARG A NH2 1 
ATOM   1039 N  N   . LEU A 1 144 ? -20.870 53.538  13.837  1.00 24.03  ? 144  LEU A N   1 
ATOM   1040 C  CA  . LEU A 1 144 ? -20.163 52.685  14.765  1.00 24.28  ? 144  LEU A CA  1 
ATOM   1041 C  C   . LEU A 1 144 ? -18.809 52.246  14.189  1.00 26.43  ? 144  LEU A C   1 
ATOM   1042 O  O   . LEU A 1 144 ? -17.802 52.207  14.894  1.00 31.80  ? 144  LEU A O   1 
ATOM   1043 C  CB  . LEU A 1 144 ? -21.074 51.500  15.095  1.00 24.44  ? 144  LEU A CB  1 
ATOM   1044 C  CG  . LEU A 1 144 ? -21.562 51.241  16.536  1.00 31.58  ? 144  LEU A CG  1 
ATOM   1045 C  CD1 . LEU A 1 144 ? -21.813 52.531  17.339  1.00 25.91  ? 144  LEU A CD1 1 
ATOM   1046 C  CD2 . LEU A 1 144 ? -22.760 50.278  16.568  1.00 22.37  ? 144  LEU A CD2 1 
ATOM   1047 N  N   . ALA A 1 145 ? -18.774 51.937  12.898  1.00 25.30  ? 145  ALA A N   1 
ATOM   1048 C  CA  . ALA A 1 145 ? -17.528 51.536  12.248  1.00 24.20  ? 145  ALA A CA  1 
ATOM   1049 C  C   . ALA A 1 145 ? -17.668 51.750  10.757  1.00 25.37  ? 145  ALA A C   1 
ATOM   1050 O  O   . ALA A 1 145 ? -18.785 51.722  10.223  1.00 22.57  ? 145  ALA A O   1 
ATOM   1051 C  CB  . ALA A 1 145 ? -17.204 50.084  12.544  1.00 24.74  ? 145  ALA A CB  1 
ATOM   1052 N  N   . CYS A 1 146 ? -16.545 51.950  10.075  1.00 23.08  ? 146  CYS A N   1 
ATOM   1053 C  CA  . CYS A 1 146 ? -16.606 52.159  8.637   1.00 20.94  ? 146  CYS A CA  1 
ATOM   1054 C  C   . CYS A 1 146 ? -15.310 51.815  7.921   1.00 23.69  ? 146  CYS A C   1 
ATOM   1055 O  O   . CYS A 1 146 ? -14.248 51.688  8.539   1.00 22.06  ? 146  CYS A O   1 
ATOM   1056 C  CB  . CYS A 1 146 ? -17.005 53.594  8.327   1.00 21.19  ? 146  CYS A CB  1 
ATOM   1057 S  SG  . CYS A 1 146 ? -15.843 54.825  8.975   1.00 24.60  ? 146  CYS A SG  1 
ATOM   1058 N  N   . GLY A 1 147 ? -15.416 51.663  6.608   1.00 19.00  ? 147  GLY A N   1 
ATOM   1059 C  CA  . GLY A 1 147 ? -14.260 51.417  5.779   1.00 20.22  ? 147  GLY A CA  1 
ATOM   1060 C  C   . GLY A 1 147 ? -14.545 51.770  4.343   1.00 22.67  ? 147  GLY A C   1 
ATOM   1061 O  O   . GLY A 1 147 ? -15.704 51.770  3.911   1.00 23.50  ? 147  GLY A O   1 
ATOM   1062 N  N   . VAL A 1 148 ? -13.494 52.104  3.604   1.00 22.07  ? 148  VAL A N   1 
ATOM   1063 C  CA  . VAL A 1 148 ? -13.651 52.337  2.182   1.00 23.38  ? 148  VAL A CA  1 
ATOM   1064 C  C   . VAL A 1 148 ? -13.752 51.000  1.463   1.00 23.24  ? 148  VAL A C   1 
ATOM   1065 O  O   . VAL A 1 148 ? -12.986 50.094  1.733   1.00 23.59  ? 148  VAL A O   1 
ATOM   1066 C  CB  . VAL A 1 148 ? -12.486 53.114  1.575   1.00 23.82  ? 148  VAL A CB  1 
ATOM   1067 C  CG1 . VAL A 1 148 ? -12.842 53.513  0.129   1.00 21.26  ? 148  VAL A CG1 1 
ATOM   1068 C  CG2 . VAL A 1 148 ? -12.133 54.325  2.441   1.00 20.47  ? 148  VAL A CG2 1 
ATOM   1069 N  N   . ILE A 1 149 ? -14.706 50.878  0.556   1.00 20.51  ? 149  ILE A N   1 
ATOM   1070 C  CA  . ILE A 1 149 ? -14.858 49.653  -0.215  1.00 23.61  ? 149  ILE A CA  1 
ATOM   1071 C  C   . ILE A 1 149 ? -13.799 49.613  -1.309  1.00 21.42  ? 149  ILE A C   1 
ATOM   1072 O  O   . ILE A 1 149 ? -13.628 50.572  -2.042  1.00 24.14  ? 149  ILE A O   1 
ATOM   1073 C  CB  . ILE A 1 149 ? -16.267 49.575  -0.832  1.00 27.40  ? 149  ILE A CB  1 
ATOM   1074 C  CG1 . ILE A 1 149 ? -17.322 49.573  0.294   1.00 22.70  ? 149  ILE A CG1 1 
ATOM   1075 C  CG2 . ILE A 1 149 ? -16.376 48.379  -1.786  1.00 21.97  ? 149  ILE A CG2 1 
ATOM   1076 C  CD1 . ILE A 1 149 ? -18.672 50.185  -0.113  1.00 21.57  ? 149  ILE A CD1 1 
ATOM   1077 N  N   . GLY A 1 150 ? -13.072 48.510  -1.396  1.00 22.39  ? 150  GLY A N   1 
ATOM   1078 C  CA  . GLY A 1 150 ? -11.913 48.429  -2.266  1.00 27.40  ? 150  GLY A CA  1 
ATOM   1079 C  C   . GLY A 1 150 ? -11.964 47.234  -3.199  1.00 25.95  ? 150  GLY A C   1 
ATOM   1080 O  O   . GLY A 1 150 ? -12.679 46.267  -2.928  1.00 28.88  ? 150  GLY A O   1 
ATOM   1081 N  N   . ILE A 1 151 ? -11.225 47.309  -4.304  1.00 23.65  ? 151  ILE A N   1 
ATOM   1082 C  CA  . ILE A 1 151 ? -11.177 46.233  -5.277  1.00 26.16  ? 151  ILE A CA  1 
ATOM   1083 C  C   . ILE A 1 151 ? -10.414 45.044  -4.685  1.00 29.22  ? 151  ILE A C   1 
ATOM   1084 O  O   . ILE A 1 151 ? -9.346  45.206  -4.071  1.00 25.95  ? 151  ILE A O   1 
ATOM   1085 C  CB  . ILE A 1 151 ? -10.593 46.732  -6.631  1.00 31.61  ? 151  ILE A CB  1 
ATOM   1086 C  CG1 . ILE A 1 151 ? -11.549 47.761  -7.232  1.00 26.85  ? 151  ILE A CG1 1 
ATOM   1087 C  CG2 . ILE A 1 151 ? -10.366 45.571  -7.632  1.00 24.04  ? 151  ILE A CG2 1 
ATOM   1088 C  CD1 . ILE A 1 151 ? -10.865 48.765  -8.121  1.00 30.11  ? 151  ILE A CD1 1 
ATOM   1089 N  N   . ALA A 1 152 ? -10.996 43.856  -4.824  1.00 26.52  ? 152  ALA A N   1 
ATOM   1090 C  CA  . ALA A 1 152 ? -10.369 42.652  -4.294  1.00 30.95  ? 152  ALA A CA  1 
ATOM   1091 C  C   . ALA A 1 152 ? -10.023 41.666  -5.399  1.00 34.46  ? 152  ALA A C   1 
ATOM   1092 O  O   . ALA A 1 152 ? -10.601 41.700  -6.486  1.00 36.00  ? 152  ALA A O   1 
ATOM   1093 C  CB  . ALA A 1 152 ? -11.273 41.992  -3.258  1.00 31.37  ? 152  ALA A CB  1 
ATOM   1094 N  N   . GLN A 1 153 ? -9.075  40.783  -5.115  1.00 38.66  ? 153  GLN A N   1 
ATOM   1095 C  CA  . GLN A 1 153 ? -8.696  39.733  -6.064  1.00 42.29  ? 153  GLN A CA  1 
ATOM   1096 C  C   . GLN A 1 153 ? -9.745  38.616  -6.125  1.00 50.47  ? 153  GLN A C   1 
ATOM   1097 O  O   . GLN A 1 153 ? -10.237 38.152  -5.086  1.00 54.59  ? 153  GLN A O   1 
ATOM   1098 C  CB  . GLN A 1 153 ? -7.346  39.133  -5.676  1.00 43.77  ? 153  GLN A CB  1 
ATOM   1099 C  CG  . GLN A 1 153 ? -6.913  37.951  -6.534  1.00 47.89  ? 153  GLN A CG  1 
ATOM   1100 C  CD  . GLN A 1 153 ? -5.865  37.095  -5.840  1.00 52.97  ? 153  GLN A CD  1 
ATOM   1101 O  OE1 . GLN A 1 153 ? -4.677  37.135  -6.181  1.00 50.10  ? 153  GLN A OE1 1 
ATOM   1102 N  NE2 . GLN A 1 153 ? -6.300  36.320  -4.847  1.00 58.59  ? 153  GLN A NE2 1 
ATOM   1103 O  OXT . GLN A 1 153 ? -10.116 38.137  -7.204  1.00 47.04  ? 153  GLN A OXT 1 
ATOM   1104 N  N   . ALA B 1 1   ? -14.784 67.567  -12.629 1.00 55.46  ? 1    ALA B N   1 
ATOM   1105 C  CA  . ALA B 1 1   ? -13.551 67.356  -11.880 1.00 51.63  ? 1    ALA B CA  1 
ATOM   1106 C  C   . ALA B 1 1   ? -13.738 66.156  -10.982 1.00 49.29  ? 1    ALA B C   1 
ATOM   1107 O  O   . ALA B 1 1   ? -14.845 65.877  -10.542 1.00 51.13  ? 1    ALA B O   1 
ATOM   1108 C  CB  . ALA B 1 1   ? -13.190 68.593  -11.049 1.00 43.36  ? 1    ALA B CB  1 
ATOM   1109 N  N   . MET B 1 2   ? -12.651 65.443  -10.727 1.00 40.61  ? 2    MET B N   1 
ATOM   1110 C  CA  . MET B 1 2   ? -12.678 64.318  -9.817  1.00 39.04  ? 2    MET B CA  1 
ATOM   1111 C  C   . MET B 1 2   ? -11.789 64.630  -8.614  1.00 37.22  ? 2    MET B C   1 
ATOM   1112 O  O   . MET B 1 2   ? -10.736 65.249  -8.765  1.00 38.07  ? 2    MET B O   1 
ATOM   1113 C  CB  . MET B 1 2   ? -12.194 63.056  -10.530 1.00 38.43  ? 2    MET B CB  1 
ATOM   1114 C  CG  . MET B 1 2   ? -13.217 62.462  -11.469 1.00 40.88  ? 2    MET B CG  1 
ATOM   1115 S  SD  . MET B 1 2   ? -14.666 61.890  -10.544 1.00 56.84  ? 2    MET B SD  1 
ATOM   1116 C  CE  . MET B 1 2   ? -13.923 60.645  -9.463  1.00 42.82  ? 2    MET B CE  1 
ATOM   1117 N  N   . LYS B 1 3   ? -12.225 64.240  -7.422  1.00 31.64  ? 3    LYS B N   1 
ATOM   1118 C  CA  . LYS B 1 3   ? -11.346 64.283  -6.260  1.00 33.14  ? 3    LYS B CA  1 
ATOM   1119 C  C   . LYS B 1 3   ? -11.329 62.919  -5.621  1.00 33.12  ? 3    LYS B C   1 
ATOM   1120 O  O   . LYS B 1 3   ? -12.272 62.137  -5.778  1.00 36.31  ? 3    LYS B O   1 
ATOM   1121 C  CB  . LYS B 1 3   ? -11.788 65.325  -5.228  1.00 33.68  ? 3    LYS B CB  1 
ATOM   1122 C  CG  . LYS B 1 3   ? -11.363 66.744  -5.512  1.00 36.98  ? 3    LYS B CG  1 
ATOM   1123 C  CD  . LYS B 1 3   ? -11.824 67.649  -4.366  1.00 52.16  ? 3    LYS B CD  1 
ATOM   1124 C  CE  . LYS B 1 3   ? -11.236 69.059  -4.442  1.00 53.40  ? 3    LYS B CE  1 
ATOM   1125 N  NZ  . LYS B 1 3   ? -11.561 69.736  -5.739  1.00 63.62  ? 3    LYS B NZ  1 
ATOM   1126 N  N   . ALA B 1 4   ? -10.259 62.646  -4.888  1.00 29.25  ? 4    ALA B N   1 
ATOM   1127 C  CA  . ALA B 1 4   ? -10.133 61.411  -4.140  1.00 28.04  ? 4    ALA B CA  1 
ATOM   1128 C  C   . ALA B 1 4   ? -9.360  61.713  -2.870  1.00 29.25  ? 4    ALA B C   1 
ATOM   1129 O  O   . ALA B 1 4   ? -8.742  62.768  -2.761  1.00 28.91  ? 4    ALA B O   1 
ATOM   1130 C  CB  . ALA B 1 4   ? -9.426  60.350  -4.970  1.00 28.84  ? 4    ALA B CB  1 
ATOM   1131 N  N   . VAL B 1 5   ? -9.410  60.806  -1.901  1.00 22.57  ? 5    VAL B N   1 
ATOM   1132 C  CA  . VAL B 1 5   ? -8.638  60.992  -0.695  1.00 25.22  ? 5    VAL B CA  1 
ATOM   1133 C  C   . VAL B 1 5   ? -8.226  59.639  -0.134  1.00 28.85  ? 5    VAL B C   1 
ATOM   1134 O  O   . VAL B 1 5   ? -8.882  58.623  -0.378  1.00 28.00  ? 5    VAL B O   1 
ATOM   1135 C  CB  . VAL B 1 5   ? -9.399  61.843  0.363   1.00 26.00  ? 5    VAL B CB  1 
ATOM   1136 C  CG1 . VAL B 1 5   ? -10.615 61.115  0.876   1.00 28.93  ? 5    VAL B CG1 1 
ATOM   1137 C  CG2 . VAL B 1 5   ? -8.482  62.182  1.523   1.00 29.75  ? 5    VAL B CG2 1 
ATOM   1138 N  N   . CYS B 1 6   ? -7.119  59.620  0.596   1.00 26.91  ? 6    CYS B N   1 
ATOM   1139 C  CA  . CYS B 1 6   ? -6.654  58.392  1.224   1.00 25.28  ? 6    CYS B CA  1 
ATOM   1140 C  C   . CYS B 1 6   ? -6.105  58.690  2.598   1.00 24.18  ? 6    CYS B C   1 
ATOM   1141 O  O   . CYS B 1 6   ? -5.294  59.601  2.765   1.00 26.92  ? 6    CYS B O   1 
ATOM   1142 C  CB  . CYS B 1 6   ? -5.568  57.750  0.369   1.00 29.79  ? 6    CYS B CB  1 
ATOM   1143 S  SG  . CYS B 1 6   ? -4.929  56.188  0.986   1.00 26.88  ? 6    CYS B SG  1 
ATOM   1144 N  N   . VAL B 1 7   ? -6.561  57.934  3.591   1.00 28.39  ? 7    VAL B N   1 
ATOM   1145 C  CA  . VAL B 1 7   ? -5.987  58.012  4.932   1.00 24.08  ? 7    VAL B CA  1 
ATOM   1146 C  C   . VAL B 1 7   ? -5.033  56.841  5.111   1.00 29.60  ? 7    VAL B C   1 
ATOM   1147 O  O   . VAL B 1 7   ? -5.444  55.677  5.085   1.00 29.29  ? 7    VAL B O   1 
ATOM   1148 C  CB  . VAL B 1 7   ? -7.069  57.926  6.034   1.00 24.16  ? 7    VAL B CB  1 
ATOM   1149 C  CG1 . VAL B 1 7   ? -6.416  57.786  7.399   1.00 24.62  ? 7    VAL B CG1 1 
ATOM   1150 C  CG2 . VAL B 1 7   ? -7.987  59.134  5.997   1.00 24.23  ? 7    VAL B CG2 1 
ATOM   1151 N  N   . LEU B 1 8   ? -3.755  57.121  5.300   1.00 28.06  ? 8    LEU B N   1 
ATOM   1152 C  CA  . LEU B 1 8   ? -2.840  56.005  5.496   1.00 31.71  ? 8    LEU B CA  1 
ATOM   1153 C  C   . LEU B 1 8   ? -2.555  55.747  6.974   1.00 29.58  ? 8    LEU B C   1 
ATOM   1154 O  O   . LEU B 1 8   ? -2.315  56.679  7.744   1.00 32.82  ? 8    LEU B O   1 
ATOM   1155 C  CB  . LEU B 1 8   ? -1.515  56.211  4.746   1.00 28.48  ? 8    LEU B CB  1 
ATOM   1156 C  CG  . LEU B 1 8   ? -1.432  56.967  3.432   1.00 29.57  ? 8    LEU B CG  1 
ATOM   1157 C  CD1 . LEU B 1 8   ? -0.082  57.673  3.400   1.00 40.61  ? 8    LEU B CD1 1 
ATOM   1158 C  CD2 . LEU B 1 8   ? -1.561  56.047  2.266   1.00 30.94  ? 8    LEU B CD2 1 
ATOM   1159 N  N   . LYS B 1 9   ? -2.588  54.477  7.357   1.00 29.24  ? 9    LYS B N   1 
ATOM   1160 C  CA  . LYS B 1 9   ? -2.049  54.054  8.641   1.00 32.28  ? 9    LYS B CA  1 
ATOM   1161 C  C   . LYS B 1 9   ? -1.507  52.628  8.562   1.00 34.99  ? 9    LYS B C   1 
ATOM   1162 O  O   . LYS B 1 9   ? -1.813  51.897  7.635   1.00 30.04  ? 9    LYS B O   1 
ATOM   1163 C  CB  . LYS B 1 9   ? -3.062  54.228  9.774   1.00 35.28  ? 9    LYS B CB  1 
ATOM   1164 C  CG  . LYS B 1 9   ? -4.451  53.690  9.504   1.00 35.95  ? 9    LYS B CG  1 
ATOM   1165 C  CD  . LYS B 1 9   ? -5.508  54.787  9.718   1.00 47.45  ? 9    LYS B CD  1 
ATOM   1166 C  CE  . LYS B 1 9   ? -5.397  55.448  11.098  1.00 52.43  ? 9    LYS B CE  1 
ATOM   1167 N  NZ  . LYS B 1 9   ? -5.138  56.918  10.987  1.00 57.89  ? 9    LYS B NZ  1 
ATOM   1168 N  N   . GLY B 1 10  ? -0.662  52.254  9.515   1.00 36.12  ? 10   GLY B N   1 
ATOM   1169 C  CA  . GLY B 1 10  ? -0.108  50.917  9.528   1.00 39.69  ? 10   GLY B CA  1 
ATOM   1170 C  C   . GLY B 1 10  ? 0.039   50.337  10.923  1.00 47.04  ? 10   GLY B C   1 
ATOM   1171 O  O   . GLY B 1 10  ? -0.698  50.703  11.830  1.00 39.04  ? 10   GLY B O   1 
ATOM   1172 N  N   . ASP B 1 11  ? 0.995   49.424  11.086  1.00 52.12  ? 11   ASP B N   1 
ATOM   1173 C  CA  . ASP B 1 11  ? 1.224   48.762  12.372  1.00 57.66  ? 11   ASP B CA  1 
ATOM   1174 C  C   . ASP B 1 11  ? 1.990   49.632  13.368  1.00 58.53  ? 11   ASP B C   1 
ATOM   1175 O  O   . ASP B 1 11  ? 1.875   49.444  14.586  1.00 64.79  ? 11   ASP B O   1 
ATOM   1176 C  CB  . ASP B 1 11  ? 1.931   47.424  12.172  1.00 55.13  ? 11   ASP B CB  1 
ATOM   1177 C  CG  . ASP B 1 11  ? 1.048   46.414  11.470  1.00 66.92  ? 11   ASP B CG  1 
ATOM   1178 O  OD1 . ASP B 1 11  ? -0.173  46.409  11.753  1.00 68.85  ? 11   ASP B OD1 1 
ATOM   1179 O  OD2 . ASP B 1 11  ? 1.563   45.633  10.634  1.00 71.48  ? 11   ASP B OD2 1 
ATOM   1180 N  N   . GLY B 1 12  ? 2.750   50.592  12.853  1.00 45.25  ? 12   GLY B N   1 
ATOM   1181 C  CA  . GLY B 1 12  ? 3.493   51.507  13.698  1.00 43.12  ? 12   GLY B CA  1 
ATOM   1182 C  C   . GLY B 1 12  ? 2.949   52.922  13.708  1.00 39.10  ? 12   GLY B C   1 
ATOM   1183 O  O   . GLY B 1 12  ? 1.752   53.139  13.574  1.00 43.52  ? 12   GLY B O   1 
ATOM   1184 N  N   . PRO B 1 13  ? 3.846   53.899  13.857  1.00 37.97  ? 13   PRO B N   1 
ATOM   1185 C  CA  . PRO B 1 13  ? 3.561   55.322  14.055  1.00 36.79  ? 13   PRO B CA  1 
ATOM   1186 C  C   . PRO B 1 13  ? 3.364   56.137  12.778  1.00 36.39  ? 13   PRO B C   1 
ATOM   1187 O  O   . PRO B 1 13  ? 3.089   57.337  12.881  1.00 38.58  ? 13   PRO B O   1 
ATOM   1188 C  CB  . PRO B 1 13  ? 4.836   55.808  14.737  1.00 33.41  ? 13   PRO B CB  1 
ATOM   1189 C  CG  . PRO B 1 13  ? 5.889   55.017  14.038  1.00 34.93  ? 13   PRO B CG  1 
ATOM   1190 C  CD  . PRO B 1 13  ? 5.292   53.629  13.919  1.00 35.29  ? 13   PRO B CD  1 
ATOM   1191 N  N   . VAL B 1 14  ? 3.530   55.529  11.610  1.00 33.87  ? 14   VAL B N   1 
ATOM   1192 C  CA  . VAL B 1 14  ? 3.340   56.271  10.369  1.00 33.59  ? 14   VAL B CA  1 
ATOM   1193 C  C   . VAL B 1 14  ? 1.861   56.470  10.073  1.00 35.00  ? 14   VAL B C   1 
ATOM   1194 O  O   . VAL B 1 14  ? 1.085   55.519  10.060  1.00 39.71  ? 14   VAL B O   1 
ATOM   1195 C  CB  . VAL B 1 14  ? 4.010   55.584  9.157   1.00 31.04  ? 14   VAL B CB  1 
ATOM   1196 C  CG1 . VAL B 1 14  ? 3.776   56.396  7.903   1.00 29.32  ? 14   VAL B CG1 1 
ATOM   1197 C  CG2 . VAL B 1 14  ? 5.508   55.384  9.401   1.00 30.75  ? 14   VAL B CG2 1 
ATOM   1198 N  N   . GLN B 1 15  ? 1.470   57.710  9.821   1.00 35.55  ? 15   GLN B N   1 
ATOM   1199 C  CA  . GLN B 1 15  ? 0.089   58.004  9.440   1.00 39.00  ? 15   GLN B CA  1 
ATOM   1200 C  C   . GLN B 1 15  ? 0.016   59.280  8.603   1.00 33.63  ? 15   GLN B C   1 
ATOM   1201 O  O   . GLN B 1 15  ? 0.875   60.154  8.707   1.00 36.82  ? 15   GLN B O   1 
ATOM   1202 C  CB  . GLN B 1 15  ? -0.791  58.118  10.691  1.00 42.80  ? 15   GLN B CB  1 
ATOM   1203 C  CG  . GLN B 1 15  ? -0.252  59.074  11.736  1.00 41.41  ? 15   GLN B CG  1 
ATOM   1204 C  CD  . GLN B 1 15  ? -0.900  58.876  13.099  1.00 59.68  ? 15   GLN B CD  1 
ATOM   1205 O  OE1 . GLN B 1 15  ? -0.284  58.330  14.026  1.00 59.37  ? 15   GLN B OE1 1 
ATOM   1206 N  NE2 . GLN B 1 15  ? -2.149  59.315  13.229  1.00 61.72  ? 15   GLN B NE2 1 
ATOM   1207 N  N   . GLY B 1 16  ? -0.995  59.386  7.757   1.00 29.59  ? 16   GLY B N   1 
ATOM   1208 C  CA  . GLY B 1 16  ? -1.155  60.601  6.988   1.00 26.59  ? 16   GLY B CA  1 
ATOM   1209 C  C   . GLY B 1 16  ? -2.379  60.632  6.101   1.00 28.25  ? 16   GLY B C   1 
ATOM   1210 O  O   . GLY B 1 16  ? -3.145  59.672  6.035   1.00 25.49  ? 16   GLY B O   1 
ATOM   1211 N  N   . THR B 1 17  ? -2.546  61.756  5.407   1.00 33.26  ? 17   THR B N   1 
ATOM   1212 C  CA  . THR B 1 17  ? -3.677  61.974  4.514   1.00 31.37  ? 17   THR B CA  1 
ATOM   1213 C  C   . THR B 1 17  ? -3.215  62.526  3.174   1.00 29.54  ? 17   THR B C   1 
ATOM   1214 O  O   . THR B 1 17  ? -2.499  63.532  3.127   1.00 27.53  ? 17   THR B O   1 
ATOM   1215 C  CB  . THR B 1 17  ? -4.661  62.991  5.109   1.00 33.86  ? 17   THR B CB  1 
ATOM   1216 O  OG1 . THR B 1 17  ? -5.055  62.555  6.415   1.00 36.68  ? 17   THR B OG1 1 
ATOM   1217 C  CG2 . THR B 1 17  ? -5.898  63.150  4.196   1.00 28.88  ? 17   THR B CG2 1 
ATOM   1218 N  N   . ILE B 1 18  ? -3.649  61.875  2.097   1.00 26.21  ? 18   ILE B N   1 
ATOM   1219 C  CA  . ILE B 1 18  ? -3.270  62.265  0.749   1.00 24.73  ? 18   ILE B CA  1 
ATOM   1220 C  C   . ILE B 1 18  ? -4.518  62.589  -0.045  1.00 28.24  ? 18   ILE B C   1 
ATOM   1221 O  O   . ILE B 1 18  ? -5.447  61.784  -0.094  1.00 29.53  ? 18   ILE B O   1 
ATOM   1222 C  CB  . ILE B 1 18  ? -2.447  61.149  0.060   1.00 23.57  ? 18   ILE B CB  1 
ATOM   1223 C  CG1 . ILE B 1 18  ? -1.194  60.850  0.876   1.00 27.50  ? 18   ILE B CG1 1 
ATOM   1224 C  CG2 . ILE B 1 18  ? -2.030  61.528  -1.366  1.00 26.97  ? 18   ILE B CG2 1 
ATOM   1225 C  CD1 . ILE B 1 18  ? -0.232  62.006  0.999   1.00 28.06  ? 18   ILE B CD1 1 
ATOM   1226 N  N   . HIS B 1 19  ? -4.552  63.788  -0.621  1.00 26.31  ? 19   HIS B N   1 
ATOM   1227 C  CA  . HIS B 1 19  ? -5.640  64.222  -1.495  1.00 28.41  ? 19   HIS B CA  1 
ATOM   1228 C  C   . HIS B 1 19  ? -5.209  64.160  -2.962  1.00 32.23  ? 19   HIS B C   1 
ATOM   1229 O  O   . HIS B 1 19  ? -4.078  64.526  -3.306  1.00 32.67  ? 19   HIS B O   1 
ATOM   1230 C  CB  . HIS B 1 19  ? -6.039  65.671  -1.194  1.00 28.25  ? 19   HIS B CB  1 
ATOM   1231 C  CG  . HIS B 1 19  ? -6.472  65.907  0.213   1.00 35.22  ? 19   HIS B CG  1 
ATOM   1232 N  ND1 . HIS B 1 19  ? -7.725  65.556  0.677   1.00 32.01  ? 19   HIS B ND1 1 
ATOM   1233 C  CD2 . HIS B 1 19  ? -5.820  66.466  1.263   1.00 37.76  ? 19   HIS B CD2 1 
ATOM   1234 C  CE1 . HIS B 1 19  ? -7.819  65.876  1.954   1.00 36.99  ? 19   HIS B CE1 1 
ATOM   1235 N  NE2 . HIS B 1 19  ? -6.679  66.431  2.334   1.00 41.11  ? 19   HIS B NE2 1 
ATOM   1236 N  N   . PHE B 1 20  ? -6.125  63.725  -3.819  1.00 30.27  ? 20   PHE B N   1 
ATOM   1237 C  CA  . PHE B 1 20  ? -5.891  63.607  -5.251  1.00 26.41  ? 20   PHE B CA  1 
ATOM   1238 C  C   . PHE B 1 20  ? -6.864  64.544  -5.941  1.00 33.42  ? 20   PHE B C   1 
ATOM   1239 O  O   . PHE B 1 20  ? -8.041  64.585  -5.578  1.00 34.25  ? 20   PHE B O   1 
ATOM   1240 C  CB  . PHE B 1 20  ? -6.217  62.195  -5.721  1.00 26.51  ? 20   PHE B CB  1 
ATOM   1241 C  CG  . PHE B 1 20  ? -5.441  61.123  -5.034  1.00 29.17  ? 20   PHE B CG  1 
ATOM   1242 C  CD1 . PHE B 1 20  ? -4.421  60.449  -5.704  1.00 26.28  ? 20   PHE B CD1 1 
ATOM   1243 C  CD2 . PHE B 1 20  ? -5.737  60.762  -3.717  1.00 29.24  ? 20   PHE B CD2 1 
ATOM   1244 C  CE1 . PHE B 1 20  ? -3.706  59.440  -5.067  1.00 31.24  ? 20   PHE B CE1 1 
ATOM   1245 C  CE2 . PHE B 1 20  ? -5.014  59.758  -3.071  1.00 26.02  ? 20   PHE B CE2 1 
ATOM   1246 C  CZ  . PHE B 1 20  ? -4.010  59.091  -3.741  1.00 26.26  ? 20   PHE B CZ  1 
ATOM   1247 N  N   . GLU B 1 21  ? -6.404  65.294  -6.938  1.00 30.60  ? 21   GLU B N   1 
ATOM   1248 C  CA  . GLU B 1 21  ? -7.324  66.136  -7.691  1.00 32.54  ? 21   GLU B CA  1 
ATOM   1249 C  C   . GLU B 1 21  ? -7.078  65.981  -9.185  1.00 38.86  ? 21   GLU B C   1 
ATOM   1250 O  O   . GLU B 1 21  ? -5.927  65.955  -9.649  1.00 34.98  ? 21   GLU B O   1 
ATOM   1251 C  CB  . GLU B 1 21  ? -7.244  67.616  -7.255  1.00 34.59  ? 21   GLU B CB  1 
ATOM   1252 C  CG  . GLU B 1 21  ? -8.184  68.535  -8.065  1.00 45.11  ? 21   GLU B CG  1 
ATOM   1253 C  CD  . GLU B 1 21  ? -8.340  69.957  -7.501  1.00 56.58  ? 21   GLU B CD  1 
ATOM   1254 O  OE1 . GLU B 1 21  ? -7.872  70.234  -6.371  1.00 55.50  ? 21   GLU B OE1 1 
ATOM   1255 O  OE2 . GLU B 1 21  ? -8.946  70.804  -8.202  1.00 59.43  ? 21   GLU B OE2 1 
ATOM   1256 N  N   . GLN B 1 22  ? -8.157  65.866  -9.946  1.00 36.78  ? 22   GLN B N   1 
ATOM   1257 C  CA  . GLN B 1 22  ? -8.012  65.710  -11.384 1.00 36.42  ? 22   GLN B CA  1 
ATOM   1258 C  C   . GLN B 1 22  ? -9.074  66.508  -12.126 1.00 39.51  ? 22   GLN B C   1 
ATOM   1259 O  O   . GLN B 1 22  ? -10.245 66.118  -12.178 1.00 40.96  ? 22   GLN B O   1 
ATOM   1260 C  CB  . GLN B 1 22  ? -8.070  64.241  -11.760 1.00 33.63  ? 22   GLN B CB  1 
ATOM   1261 C  CG  . GLN B 1 22  ? -7.677  63.982  -13.196 1.00 37.76  ? 22   GLN B CG  1 
ATOM   1262 C  CD  . GLN B 1 22  ? -7.835  62.527  -13.589 1.00 37.29  ? 22   GLN B CD  1 
ATOM   1263 O  OE1 . GLN B 1 22  ? -8.599  61.763  -12.969 1.00 31.00  ? 22   GLN B OE1 1 
ATOM   1264 N  NE2 . GLN B 1 22  ? -7.120  62.135  -14.633 1.00 33.41  ? 22   GLN B NE2 1 
ATOM   1265 N  N   . LYS B 1 23  ? -8.660  67.637  -12.688 1.00 41.09  ? 23   LYS B N   1 
ATOM   1266 C  CA  . LYS B 1 23  ? -9.600  68.592  -13.285 1.00 47.15  ? 23   LYS B CA  1 
ATOM   1267 C  C   . LYS B 1 23  ? -10.474 67.964  -14.381 1.00 44.51  ? 23   LYS B C   1 
ATOM   1268 O  O   . LYS B 1 23  ? -11.662 68.264  -14.467 1.00 46.79  ? 23   LYS B O   1 
ATOM   1269 C  CB  . LYS B 1 23  ? -8.846  69.823  -13.808 1.00 54.66  ? 23   LYS B CB  1 
ATOM   1270 C  CG  . LYS B 1 23  ? -9.703  71.004  -14.290 1.00 63.04  ? 23   LYS B CG  1 
ATOM   1271 C  CD  . LYS B 1 23  ? -8.793  72.109  -14.872 1.00 75.79  ? 23   LYS B CD  1 
ATOM   1272 C  CE  . LYS B 1 23  ? -9.553  73.298  -15.464 1.00 75.53  ? 23   LYS B CE  1 
ATOM   1273 N  NZ  . LYS B 1 23  ? -8.614  74.288  -16.114 1.00 75.48  ? 23   LYS B NZ  1 
ATOM   1274 N  N   . ALA B 1 24  ? -9.896  67.093  -15.209 1.00 39.81  ? 24   ALA B N   1 
ATOM   1275 C  CA  . ALA B 1 24  ? -10.666 66.412  -16.259 1.00 44.52  ? 24   ALA B CA  1 
ATOM   1276 C  C   . ALA B 1 24  ? -10.069 65.065  -16.587 1.00 39.84  ? 24   ALA B C   1 
ATOM   1277 O  O   . ALA B 1 24  ? -8.988  64.739  -16.121 1.00 40.29  ? 24   ALA B O   1 
ATOM   1278 C  CB  . ALA B 1 24  ? -10.753 67.270  -17.531 1.00 46.57  ? 24   ALA B CB  1 
ATOM   1279 N  N   . SER B 1 25  ? -10.785 64.292  -17.393 1.00 37.61  ? 25   SER B N   1 
ATOM   1280 C  CA  . SER B 1 25  ? -10.327 62.971  -17.839 1.00 45.35  ? 25   SER B CA  1 
ATOM   1281 C  C   . SER B 1 25  ? -8.865  62.901  -18.285 1.00 39.00  ? 25   SER B C   1 
ATOM   1282 O  O   . SER B 1 25  ? -8.111  62.040  -17.838 1.00 35.41  ? 25   SER B O   1 
ATOM   1283 C  CB  . SER B 1 25  ? -11.211 62.473  -18.988 1.00 49.97  ? 25   SER B CB  1 
ATOM   1284 O  OG  . SER B 1 25  ? -12.237 61.627  -18.505 1.00 53.93  ? 25   SER B OG  1 
ATOM   1285 N  N   . GLY B 1 26  ? -8.482  63.803  -19.180 1.00 39.08  ? 26   GLY B N   1 
ATOM   1286 C  CA  . GLY B 1 26  ? -7.142  63.804  -19.738 1.00 43.33  ? 26   GLY B CA  1 
ATOM   1287 C  C   . GLY B 1 26  ? -6.141  64.713  -19.047 1.00 45.31  ? 26   GLY B C   1 
ATOM   1288 O  O   . GLY B 1 26  ? -5.075  65.022  -19.595 1.00 48.40  ? 26   GLY B O   1 
ATOM   1289 N  N   . GLU B 1 27  ? -6.464  65.150  -17.838 1.00 42.63  ? 27   GLU B N   1 
ATOM   1290 C  CA  . GLU B 1 27  ? -5.516  65.955  -17.086 1.00 40.45  ? 27   GLU B CA  1 
ATOM   1291 C  C   . GLU B 1 27  ? -4.690  65.063  -16.169 1.00 39.91  ? 27   GLU B C   1 
ATOM   1292 O  O   . GLU B 1 27  ? -5.060  63.924  -15.890 1.00 37.17  ? 27   GLU B O   1 
ATOM   1293 C  CB  . GLU B 1 27  ? -6.242  67.026  -16.282 1.00 45.29  ? 27   GLU B CB  1 
ATOM   1294 C  CG  . GLU B 1 27  ? -7.170  67.911  -17.105 1.00 51.43  ? 27   GLU B CG  1 
ATOM   1295 C  CD  . GLU B 1 27  ? -6.527  69.234  -17.492 1.00 61.88  ? 27   GLU B CD  1 
ATOM   1296 O  OE1 . GLU B 1 27  ? -7.048  70.304  -17.067 1.00 63.37  ? 27   GLU B OE1 1 
ATOM   1297 O  OE2 . GLU B 1 27  ? -5.499  69.196  -18.213 1.00 52.91  ? 27   GLU B OE2 1 
ATOM   1298 N  N   . PRO B 1 28  ? -3.548  65.578  -15.714 1.00 40.16  ? 28   PRO B N   1 
ATOM   1299 C  CA  . PRO B 1 28  ? -2.740  64.930  -14.677 1.00 39.54  ? 28   PRO B CA  1 
ATOM   1300 C  C   . PRO B 1 28  ? -3.455  64.934  -13.325 1.00 39.02  ? 28   PRO B C   1 
ATOM   1301 O  O   . PRO B 1 28  ? -4.286  65.810  -13.056 1.00 34.40  ? 28   PRO B O   1 
ATOM   1302 C  CB  . PRO B 1 28  ? -1.509  65.824  -14.591 1.00 40.83  ? 28   PRO B CB  1 
ATOM   1303 C  CG  . PRO B 1 28  ? -1.479  66.562  -15.911 1.00 43.82  ? 28   PRO B CG  1 
ATOM   1304 C  CD  . PRO B 1 28  ? -2.903  66.780  -16.255 1.00 42.74  ? 28   PRO B CD  1 
ATOM   1305 N  N   . VAL B 1 29  ? -3.127  63.950  -12.494 1.00 35.74  ? 29   VAL B N   1 
ATOM   1306 C  CA  . VAL B 1 29  ? -3.598  63.901  -11.124 1.00 36.24  ? 29   VAL B CA  1 
ATOM   1307 C  C   . VAL B 1 29  ? -2.608  64.627  -10.210 1.00 35.01  ? 29   VAL B C   1 
ATOM   1308 O  O   . VAL B 1 29  ? -1.416  64.345  -10.234 1.00 35.43  ? 29   VAL B O   1 
ATOM   1309 C  CB  . VAL B 1 29  ? -3.745  62.450  -10.643 1.00 32.91  ? 29   VAL B CB  1 
ATOM   1310 C  CG1 . VAL B 1 29  ? -4.467  62.411  -9.292  1.00 30.49  ? 29   VAL B CG1 1 
ATOM   1311 C  CG2 . VAL B 1 29  ? -4.487  61.624  -11.682 1.00 29.17  ? 29   VAL B CG2 1 
ATOM   1312 N  N   . VAL B 1 30  ? -3.110  65.558  -9.406  1.00 32.19  ? 30   VAL B N   1 
ATOM   1313 C  CA  . VAL B 1 30  ? -2.296  66.190  -8.374  1.00 35.17  ? 30   VAL B CA  1 
ATOM   1314 C  C   . VAL B 1 30  ? -2.537  65.594  -6.978  1.00 35.11  ? 30   VAL B C   1 
ATOM   1315 O  O   . VAL B 1 30  ? -3.655  65.639  -6.477  1.00 32.89  ? 30   VAL B O   1 
ATOM   1316 C  CB  . VAL B 1 30  ? -2.556  67.699  -8.312  1.00 36.01  ? 30   VAL B CB  1 
ATOM   1317 C  CG1 . VAL B 1 30  ? -1.791  68.307  -7.146  1.00 35.49  ? 30   VAL B CG1 1 
ATOM   1318 C  CG2 . VAL B 1 30  ? -2.141  68.351  -9.625  1.00 37.19  ? 30   VAL B CG2 1 
ATOM   1319 N  N   . LEU B 1 31  ? -1.489  65.030  -6.371  1.00 32.41  ? 31   LEU B N   1 
ATOM   1320 C  CA  . LEU B 1 31  ? -1.520  64.590  -4.976  1.00 31.32  ? 31   LEU B CA  1 
ATOM   1321 C  C   . LEU B 1 31  ? -1.005  65.676  -4.052  1.00 34.32  ? 31   LEU B C   1 
ATOM   1322 O  O   . LEU B 1 31  ? -0.020  66.343  -4.358  1.00 36.94  ? 31   LEU B O   1 
ATOM   1323 C  CB  . LEU B 1 31  ? -0.634  63.367  -4.757  1.00 28.42  ? 31   LEU B CB  1 
ATOM   1324 C  CG  . LEU B 1 31  ? -1.077  62.039  -5.360  1.00 30.47  ? 31   LEU B CG  1 
ATOM   1325 C  CD1 . LEU B 1 31  ? -0.925  62.057  -6.859  1.00 26.87  ? 31   LEU B CD1 1 
ATOM   1326 C  CD2 . LEU B 1 31  ? -0.279  60.892  -4.734  1.00 26.92  ? 31   LEU B CD2 1 
ATOM   1327 N  N   . SER B 1 32  ? -1.642  65.835  -2.902  1.00 31.55  ? 32   SER B N   1 
ATOM   1328 C  CA  . SER B 1 32  ? -1.080  66.696  -1.870  1.00 32.69  ? 32   SER B CA  1 
ATOM   1329 C  C   . SER B 1 32  ? -1.503  66.219  -0.491  1.00 31.66  ? 32   SER B C   1 
ATOM   1330 O  O   . SER B 1 32  ? -2.584  65.666  -0.328  1.00 31.01  ? 32   SER B O   1 
ATOM   1331 C  CB  . SER B 1 32  ? -1.484  68.164  -2.073  1.00 36.87  ? 32   SER B CB  1 
ATOM   1332 O  OG  . SER B 1 32  ? -2.896  68.326  -2.079  1.00 42.09  ? 32   SER B OG  1 
ATOM   1333 N  N   . GLY B 1 33  ? -0.641  66.438  0.496   1.00 28.30  ? 33   GLY B N   1 
ATOM   1334 C  CA  . GLY B 1 33  ? -0.943  66.075  1.856   1.00 29.36  ? 33   GLY B CA  1 
ATOM   1335 C  C   . GLY B 1 33  ? 0.299   66.016  2.702   1.00 31.04  ? 33   GLY B C   1 
ATOM   1336 O  O   . GLY B 1 33  ? 1.312   66.637  2.388   1.00 31.53  ? 33   GLY B O   1 
ATOM   1337 N  N   . GLN B 1 34  ? 0.214   65.242  3.774   1.00 29.40  ? 34   GLN B N   1 
ATOM   1338 C  CA  . GLN B 1 34  ? 1.277   65.155  4.755   1.00 31.74  ? 34   GLN B CA  1 
ATOM   1339 C  C   . GLN B 1 34  ? 1.269   63.751  5.318   1.00 33.64  ? 34   GLN B C   1 
ATOM   1340 O  O   . GLN B 1 34  ? 0.212   63.122  5.400   1.00 36.36  ? 34   GLN B O   1 
ATOM   1341 C  CB  . GLN B 1 34  ? 1.057   66.180  5.875   1.00 32.79  ? 34   GLN B CB  1 
ATOM   1342 C  CG  . GLN B 1 34  ? 2.306   66.478  6.720   1.00 33.26  ? 34   GLN B CG  1 
ATOM   1343 C  CD  . GLN B 1 34  ? 2.116   67.676  7.649   1.00 39.57  ? 34   GLN B CD  1 
ATOM   1344 O  OE1 . GLN B 1 34  ? 1.180   67.712  8.444   1.00 46.17  ? 34   GLN B OE1 1 
ATOM   1345 N  NE2 . GLN B 1 34  ? 3.006   68.660  7.550   1.00 37.49  ? 34   GLN B NE2 1 
ATOM   1346 N  N   . ILE B 1 35  ? 2.453   63.251  5.660   1.00 34.66  ? 35   ILE B N   1 
ATOM   1347 C  CA  . ILE B 1 35  ? 2.617   61.955  6.318   1.00 35.43  ? 35   ILE B CA  1 
ATOM   1348 C  C   . ILE B 1 35  ? 3.564   62.206  7.477   1.00 35.36  ? 35   ILE B C   1 
ATOM   1349 O  O   . ILE B 1 35  ? 4.577   62.882  7.298   1.00 31.52  ? 35   ILE B O   1 
ATOM   1350 C  CB  . ILE B 1 35  ? 3.293   60.918  5.400   1.00 32.97  ? 35   ILE B CB  1 
ATOM   1351 C  CG1 . ILE B 1 35  ? 2.532   60.765  4.097   1.00 28.64  ? 35   ILE B CG1 1 
ATOM   1352 C  CG2 . ILE B 1 35  ? 3.433   59.556  6.097   1.00 29.71  ? 35   ILE B CG2 1 
ATOM   1353 C  CD1 . ILE B 1 35  ? 3.164   59.739  3.192   1.00 28.73  ? 35   ILE B CD1 1 
ATOM   1354 N  N   . THR B 1 36  ? 3.235   61.690  8.658   1.00 30.90  ? 36   THR B N   1 
ATOM   1355 C  CA  . THR B 1 36  ? 4.076   61.919  9.824   1.00 28.71  ? 36   THR B CA  1 
ATOM   1356 C  C   . THR B 1 36  ? 4.509   60.597  10.414  1.00 30.35  ? 36   THR B C   1 
ATOM   1357 O  O   . THR B 1 36  ? 3.911   59.559  10.143  1.00 34.73  ? 36   THR B O   1 
ATOM   1358 C  CB  . THR B 1 36  ? 3.376   62.775  10.898  1.00 31.17  ? 36   THR B CB  1 
ATOM   1359 O  OG1 . THR B 1 36  ? 2.213   62.098  11.395  1.00 32.14  ? 36   THR B OG1 1 
ATOM   1360 C  CG2 . THR B 1 36  ? 2.981   64.146  10.332  1.00 26.73  ? 36   THR B CG2 1 
ATOM   1361 N  N   . GLY B 1 37  ? 5.574   60.627  11.197  1.00 30.95  ? 37   GLY B N   1 
ATOM   1362 C  CA  . GLY B 1 37  ? 6.056   59.419  11.835  1.00 29.38  ? 37   GLY B CA  1 
ATOM   1363 C  C   . GLY B 1 37  ? 7.087   58.687  11.020  1.00 29.74  ? 37   GLY B C   1 
ATOM   1364 O  O   . GLY B 1 37  ? 7.424   57.547  11.327  1.00 32.12  ? 37   GLY B O   1 
ATOM   1365 N  N   . LEU B 1 38  ? 7.606   59.329  9.979   1.00 34.06  ? 38   LEU B N   1 
ATOM   1366 C  CA  . LEU B 1 38  ? 8.591   58.656  9.127   1.00 34.33  ? 38   LEU B CA  1 
ATOM   1367 C  C   . LEU B 1 38  ? 10.014  58.871  9.643   1.00 33.12  ? 38   LEU B C   1 
ATOM   1368 O  O   . LEU B 1 38  ? 10.302  59.880  10.285  1.00 29.48  ? 38   LEU B O   1 
ATOM   1369 C  CB  . LEU B 1 38  ? 8.488   59.158  7.677   1.00 35.27  ? 38   LEU B CB  1 
ATOM   1370 C  CG  . LEU B 1 38  ? 7.216   58.798  6.900   1.00 32.74  ? 38   LEU B CG  1 
ATOM   1371 C  CD1 . LEU B 1 38  ? 7.109   59.637  5.639   1.00 31.71  ? 38   LEU B CD1 1 
ATOM   1372 C  CD2 . LEU B 1 38  ? 7.157   57.308  6.574   1.00 33.28  ? 38   LEU B CD2 1 
ATOM   1373 N  N   . THR B 1 39  ? 10.906  57.926  9.354   1.00 34.82  ? 39   THR B N   1 
ATOM   1374 C  CA  . THR B 1 39  ? 12.340  58.216  9.423   1.00 33.75  ? 39   THR B CA  1 
ATOM   1375 C  C   . THR B 1 39  ? 12.702  59.304  8.418   1.00 33.69  ? 39   THR B C   1 
ATOM   1376 O  O   . THR B 1 39  ? 12.122  59.371  7.318   1.00 33.16  ? 39   THR B O   1 
ATOM   1377 C  CB  . THR B 1 39  ? 13.183  56.983  9.097   1.00 35.80  ? 39   THR B CB  1 
ATOM   1378 O  OG1 . THR B 1 39  ? 12.804  56.469  7.810   1.00 38.30  ? 39   THR B OG1 1 
ATOM   1379 C  CG2 . THR B 1 39  ? 12.979  55.904  10.175  1.00 31.42  ? 39   THR B CG2 1 
ATOM   1380 N  N   . GLU B 1 40  ? 13.650  60.158  8.797   1.00 33.53  ? 40   GLU B N   1 
ATOM   1381 C  CA  . GLU B 1 40  ? 14.151  61.222  7.913   1.00 37.52  ? 40   GLU B CA  1 
ATOM   1382 C  C   . GLU B 1 40  ? 14.687  60.655  6.601   1.00 32.74  ? 40   GLU B C   1 
ATOM   1383 O  O   . GLU B 1 40  ? 15.368  59.629  6.604   1.00 31.56  ? 40   GLU B O   1 
ATOM   1384 C  CB  . GLU B 1 40  ? 15.242  62.043  8.614   1.00 40.10  ? 40   GLU B CB  1 
ATOM   1385 C  CG  . GLU B 1 40  ? 15.879  63.135  7.748   1.00 45.12  ? 40   GLU B CG  1 
ATOM   1386 C  CD  . GLU B 1 40  ? 16.724  64.119  8.558   1.00 51.90  ? 40   GLU B CD  1 
ATOM   1387 O  OE1 . GLU B 1 40  ? 16.878  63.910  9.783   1.00 52.98  ? 40   GLU B OE1 1 
ATOM   1388 O  OE2 . GLU B 1 40  ? 17.223  65.105  7.972   1.00 50.11  ? 40   GLU B OE2 1 
ATOM   1389 N  N   . GLY B 1 41  ? 14.374  61.312  5.483   1.00 36.38  ? 41   GLY B N   1 
ATOM   1390 C  CA  . GLY B 1 41  ? 14.819  60.828  4.182   1.00 30.77  ? 41   GLY B CA  1 
ATOM   1391 C  C   . GLY B 1 41  ? 13.706  60.384  3.246   1.00 33.98  ? 41   GLY B C   1 
ATOM   1392 O  O   . GLY B 1 41  ? 12.536  60.752  3.418   1.00 38.44  ? 41   GLY B O   1 
ATOM   1393 N  N   . GLN B 1 42  ? 14.058  59.583  2.251   1.00 31.68  ? 42   GLN B N   1 
ATOM   1394 C  CA  . GLN B 1 42  ? 13.117  59.263  1.185   1.00 32.66  ? 42   GLN B CA  1 
ATOM   1395 C  C   . GLN B 1 42  ? 12.470  57.915  1.379   1.00 28.09  ? 42   GLN B C   1 
ATOM   1396 O  O   . GLN B 1 42  ? 13.128  56.978  1.806   1.00 30.57  ? 42   GLN B O   1 
ATOM   1397 C  CB  . GLN B 1 42  ? 13.810  59.321  -0.178  1.00 29.52  ? 42   GLN B CB  1 
ATOM   1398 C  CG  . GLN B 1 42  ? 14.041  60.736  -0.666  1.00 31.52  ? 42   GLN B CG  1 
ATOM   1399 C  CD  . GLN B 1 42  ? 14.850  60.787  -1.968  1.00 37.79  ? 42   GLN B CD  1 
ATOM   1400 O  OE1 . GLN B 1 42  ? 15.258  59.752  -2.501  1.00 32.13  ? 42   GLN B OE1 1 
ATOM   1401 N  NE2 . GLN B 1 42  ? 15.083  61.998  -2.476  1.00 31.83  ? 42   GLN B NE2 1 
ATOM   1402 N  N   . HIS B 1 43  ? 11.180  57.819  1.069   1.00 23.94  ? 43   HIS B N   1 
ATOM   1403 C  CA  . HIS B 1 43  ? 10.487  56.534  1.142   1.00 28.32  ? 43   HIS B CA  1 
ATOM   1404 C  C   . HIS B 1 43  ? 9.669   56.261  -0.134  1.00 27.48  ? 43   HIS B C   1 
ATOM   1405 O  O   . HIS B 1 43  ? 9.029   57.154  -0.677  1.00 27.38  ? 43   HIS B O   1 
ATOM   1406 C  CB  . HIS B 1 43  ? 9.571   56.454  2.381   1.00 29.30  ? 43   HIS B CB  1 
ATOM   1407 C  CG  . HIS B 1 43  ? 10.260  56.730  3.688   1.00 33.93  ? 43   HIS B CG  1 
ATOM   1408 N  ND1 . HIS B 1 43  ? 10.641  55.728  4.555   1.00 31.37  ? 43   HIS B ND1 1 
ATOM   1409 C  CD2 . HIS B 1 43  ? 10.608  57.895  4.287   1.00 32.27  ? 43   HIS B CD2 1 
ATOM   1410 C  CE1 . HIS B 1 43  ? 11.210  56.262  5.620   1.00 33.23  ? 43   HIS B CE1 1 
ATOM   1411 N  NE2 . HIS B 1 43  ? 11.202  57.574  5.484   1.00 34.51  ? 43   HIS B NE2 1 
ATOM   1412 N  N   . GLY B 1 44  ? 9.703   55.027  -0.615  1.00 25.65  ? 44   GLY B N   1 
ATOM   1413 C  CA  . GLY B 1 44  ? 8.860   54.626  -1.720  1.00 26.62  ? 44   GLY B CA  1 
ATOM   1414 C  C   . GLY B 1 44  ? 7.412   54.983  -1.440  1.00 29.32  ? 44   GLY B C   1 
ATOM   1415 O  O   . GLY B 1 44  ? 7.002   55.050  -0.288  1.00 29.86  ? 44   GLY B O   1 
ATOM   1416 N  N   . PHE B 1 45  ? 6.656   55.196  -2.513  1.00 27.66  ? 45   PHE B N   1 
ATOM   1417 C  CA  . PHE B 1 45  ? 5.307   55.717  -2.491  1.00 26.94  ? 45   PHE B CA  1 
ATOM   1418 C  C   . PHE B 1 45  ? 4.581   55.161  -3.737  1.00 32.53  ? 45   PHE B C   1 
ATOM   1419 O  O   . PHE B 1 45  ? 4.786   55.674  -4.843  1.00 28.84  ? 45   PHE B O   1 
ATOM   1420 C  CB  . PHE B 1 45  ? 5.377   57.237  -2.579  1.00 28.88  ? 45   PHE B CB  1 
ATOM   1421 C  CG  . PHE B 1 45  ? 4.103   57.941  -2.179  1.00 30.25  ? 45   PHE B CG  1 
ATOM   1422 C  CD1 . PHE B 1 45  ? 3.537   57.724  -0.926  1.00 31.16  ? 45   PHE B CD1 1 
ATOM   1423 C  CD2 . PHE B 1 45  ? 3.509   58.861  -3.032  1.00 25.32  ? 45   PHE B CD2 1 
ATOM   1424 C  CE1 . PHE B 1 45  ? 2.374   58.391  -0.544  1.00 33.43  ? 45   PHE B CE1 1 
ATOM   1425 C  CE2 . PHE B 1 45  ? 2.353   59.531  -2.665  1.00 30.47  ? 45   PHE B CE2 1 
ATOM   1426 C  CZ  . PHE B 1 45  ? 1.777   59.291  -1.413  1.00 32.02  ? 45   PHE B CZ  1 
ATOM   1427 N  N   . HIS B 1 46  ? 3.744   54.128  -3.562  1.00 25.07  ? 46   HIS B N   1 
ATOM   1428 C  CA  . HIS B 1 46  ? 3.168   53.417  -4.695  1.00 27.31  ? 46   HIS B CA  1 
ATOM   1429 C  C   . HIS B 1 46  ? 1.663   53.185  -4.551  1.00 29.65  ? 46   HIS B C   1 
ATOM   1430 O  O   . HIS B 1 46  ? 1.167   53.011  -3.436  1.00 27.51  ? 46   HIS B O   1 
ATOM   1431 C  CB  . HIS B 1 46  ? 3.840   52.054  -4.854  1.00 24.75  ? 46   HIS B CB  1 
ATOM   1432 C  CG  . HIS B 1 46  ? 5.319   52.070  -4.607  1.00 28.10  ? 46   HIS B CG  1 
ATOM   1433 N  ND1 . HIS B 1 46  ? 6.210   52.729  -5.434  1.00 32.70  ? 46   HIS B ND1 1 
ATOM   1434 C  CD2 . HIS B 1 46  ? 6.069   51.463  -3.660  1.00 27.01  ? 46   HIS B CD2 1 
ATOM   1435 C  CE1 . HIS B 1 46  ? 7.442   52.552  -4.986  1.00 28.19  ? 46   HIS B CE1 1 
ATOM   1436 N  NE2 . HIS B 1 46  ? 7.382   51.788  -3.910  1.00 31.21  ? 46   HIS B NE2 1 
ATOM   1437 N  N   . VAL B 1 47  ? 0.950   53.190  -5.680  1.00 20.83  ? 47   VAL B N   1 
ATOM   1438 C  CA  . VAL B 1 47  ? -0.385  52.640  -5.734  1.00 24.73  ? 47   VAL B CA  1 
ATOM   1439 C  C   . VAL B 1 47  ? -0.261  51.144  -5.990  1.00 28.17  ? 47   VAL B C   1 
ATOM   1440 O  O   . VAL B 1 47  ? 0.254   50.734  -7.030  1.00 28.47  ? 47   VAL B O   1 
ATOM   1441 C  CB  . VAL B 1 47  ? -1.275  53.277  -6.838  1.00 25.92  ? 47   VAL B CB  1 
ATOM   1442 C  CG1 . VAL B 1 47  ? -2.611  52.573  -6.901  1.00 21.15  ? 47   VAL B CG1 1 
ATOM   1443 C  CG2 . VAL B 1 47  ? -1.479  54.752  -6.586  1.00 20.62  ? 47   VAL B CG2 1 
ATOM   1444 N  N   . HIS B 1 48  ? -0.708  50.340  -5.024  1.00 24.86  ? 48   HIS B N   1 
ATOM   1445 C  CA  . HIS B 1 48  ? -0.698  48.898  -5.150  1.00 26.43  ? 48   HIS B CA  1 
ATOM   1446 C  C   . HIS B 1 48  ? -2.040  48.425  -5.697  1.00 24.23  ? 48   HIS B C   1 
ATOM   1447 O  O   . HIS B 1 48  ? -3.008  49.162  -5.697  1.00 26.88  ? 48   HIS B O   1 
ATOM   1448 C  CB  . HIS B 1 48  ? -0.406  48.241  -3.809  1.00 26.55  ? 48   HIS B CB  1 
ATOM   1449 C  CG  . HIS B 1 48  ? 0.994   48.443  -3.325  1.00 25.72  ? 48   HIS B CG  1 
ATOM   1450 N  ND1 . HIS B 1 48  ? 1.871   47.397  -3.130  1.00 26.17  ? 48   HIS B ND1 1 
ATOM   1451 C  CD2 . HIS B 1 48  ? 1.656   49.562  -2.949  1.00 27.04  ? 48   HIS B CD2 1 
ATOM   1452 C  CE1 . HIS B 1 48  ? 3.015   47.863  -2.664  1.00 25.33  ? 48   HIS B CE1 1 
ATOM   1453 N  NE2 . HIS B 1 48  ? 2.916   49.176  -2.554  1.00 26.02  ? 48   HIS B NE2 1 
ATOM   1454 N  N   . GLN B 1 49  ? -2.091  47.185  -6.155  1.00 25.13  ? 49   GLN B N   1 
ATOM   1455 C  CA  . GLN B 1 49  ? -3.183  46.738  -6.991  1.00 25.36  ? 49   GLN B CA  1 
ATOM   1456 C  C   . GLN B 1 49  ? -4.558  46.631  -6.310  1.00 28.98  ? 49   GLN B C   1 
ATOM   1457 O  O   . GLN B 1 49  ? -5.560  47.041  -6.879  1.00 26.73  ? 49   GLN B O   1 
ATOM   1458 C  CB  . GLN B 1 49  ? -2.813  45.413  -7.638  1.00 29.25  ? 49   GLN B CB  1 
ATOM   1459 C  CG  . GLN B 1 49  ? -3.750  45.021  -8.783  1.00 32.17  ? 49   GLN B CG  1 
ATOM   1460 C  CD  . GLN B 1 49  ? -3.530  43.602  -9.228  1.00 31.05  ? 49   GLN B CD  1 
ATOM   1461 O  OE1 . GLN B 1 49  ? -2.564  42.965  -8.819  1.00 38.52  ? 49   GLN B OE1 1 
ATOM   1462 N  NE2 . GLN B 1 49  ? -4.432  43.087  -10.048 1.00 30.66  ? 49   GLN B NE2 1 
ATOM   1463 N  N   . TYR B 1 50  ? -4.613  46.093  -5.097  1.00 27.18  ? 50   TYR B N   1 
ATOM   1464 C  CA  . TYR B 1 50  ? -5.908  45.849  -4.471  1.00 28.64  ? 50   TYR B CA  1 
ATOM   1465 C  C   . TYR B 1 50  ? -6.246  46.833  -3.353  1.00 29.41  ? 50   TYR B C   1 
ATOM   1466 O  O   . TYR B 1 50  ? -5.373  47.305  -2.631  1.00 27.56  ? 50   TYR B O   1 
ATOM   1467 C  CB  . TYR B 1 50  ? -6.007  44.388  -4.004  1.00 26.88  ? 50   TYR B CB  1 
ATOM   1468 C  CG  . TYR B 1 50  ? -5.896  43.418  -5.163  1.00 29.59  ? 50   TYR B CG  1 
ATOM   1469 C  CD1 . TYR B 1 50  ? -6.802  43.481  -6.216  1.00 32.52  ? 50   TYR B CD1 1 
ATOM   1470 C  CD2 . TYR B 1 50  ? -4.875  42.469  -5.233  1.00 35.66  ? 50   TYR B CD2 1 
ATOM   1471 C  CE1 . TYR B 1 50  ? -6.714  42.641  -7.292  1.00 32.96  ? 50   TYR B CE1 1 
ATOM   1472 C  CE2 . TYR B 1 50  ? -4.780  41.597  -6.323  1.00 35.95  ? 50   TYR B CE2 1 
ATOM   1473 C  CZ  . TYR B 1 50  ? -5.712  41.702  -7.352  1.00 39.67  ? 50   TYR B CZ  1 
ATOM   1474 O  OH  . TYR B 1 50  ? -5.677  40.872  -8.455  1.00 43.40  ? 50   TYR B OH  1 
ATOM   1475 N  N   . GLY B 1 51  ? -7.522  47.169  -3.234  1.00 28.14  ? 51   GLY B N   1 
ATOM   1476 C  CA  . GLY B 1 51  ? -7.977  47.916  -2.070  1.00 29.34  ? 51   GLY B CA  1 
ATOM   1477 C  C   . GLY B 1 51  ? -8.388  46.944  -0.980  1.00 29.36  ? 51   GLY B C   1 
ATOM   1478 O  O   . GLY B 1 51  ? -9.485  47.020  -0.448  1.00 30.83  ? 51   GLY B O   1 
ATOM   1479 N  N   . ASP B 1 52  ? -7.502  46.007  -0.674  1.00 31.81  ? 52   ASP B N   1 
ATOM   1480 C  CA  . ASP B 1 52  ? -7.787  44.939  0.266   1.00 32.19  ? 52   ASP B CA  1 
ATOM   1481 C  C   . ASP B 1 52  ? -6.817  45.008  1.442   1.00 34.25  ? 52   ASP B C   1 
ATOM   1482 O  O   . ASP B 1 52  ? -5.656  44.649  1.324   1.00 33.59  ? 52   ASP B O   1 
ATOM   1483 C  CB  . ASP B 1 52  ? -7.671  43.583  -0.419  1.00 28.21  ? 52   ASP B CB  1 
ATOM   1484 C  CG  . ASP B 1 52  ? -7.854  42.422  0.559   1.00 37.54  ? 52   ASP B CG  1 
ATOM   1485 O  OD1 . ASP B 1 52  ? -7.945  42.672  1.783   1.00 36.37  ? 52   ASP B OD1 1 
ATOM   1486 O  OD2 . ASP B 1 52  ? -7.911  41.256  0.109   1.00 34.74  ? 52   ASP B OD2 1 
ATOM   1487 N  N   . ASN B 1 53  ? -7.285  45.472  2.587   1.00 33.95  ? 53   ASN B N   1 
ATOM   1488 C  CA  . ASN B 1 53  ? -6.385  45.546  3.721   1.00 37.33  ? 53   ASN B CA  1 
ATOM   1489 C  C   . ASN B 1 53  ? -6.783  44.569  4.851   1.00 37.52  ? 53   ASN B C   1 
ATOM   1490 O  O   . ASN B 1 53  ? -6.423  44.761  6.003   1.00 33.94  ? 53   ASN B O   1 
ATOM   1491 C  CB  . ASN B 1 53  ? -6.199  47.010  4.165   1.00 38.75  ? 53   ASN B CB  1 
ATOM   1492 C  CG  . ASN B 1 53  ? -5.718  47.939  2.988   1.00 48.96  ? 53   ASN B CG  1 
ATOM   1493 O  OD1 . ASN B 1 53  ? -5.133  47.475  1.988   1.00 41.32  ? 53   ASN B OD1 1 
ATOM   1494 N  ND2 . ASN B 1 53  ? -5.967  49.249  3.124   1.00 41.31  ? 53   ASN B ND2 1 
ATOM   1495 N  N   . THR B 1 54  ? -7.481  43.489  4.482   1.00 35.71  ? 54   THR B N   1 
ATOM   1496 C  CA  . THR B 1 54  ? -7.844  42.428  5.430   1.00 38.09  ? 54   THR B CA  1 
ATOM   1497 C  C   . THR B 1 54  ? -6.641  41.843  6.169   1.00 40.16  ? 54   THR B C   1 
ATOM   1498 O  O   . THR B 1 54  ? -6.785  41.308  7.265   1.00 40.82  ? 54   THR B O   1 
ATOM   1499 C  CB  . THR B 1 54  ? -8.623  41.277  4.766   1.00 38.96  ? 54   THR B CB  1 
ATOM   1500 O  OG1 . THR B 1 54  ? -7.828  40.684  3.730   1.00 34.64  ? 54   THR B OG1 1 
ATOM   1501 C  CG2 . THR B 1 54  ? -9.946  41.785  4.187   1.00 36.69  ? 54   THR B CG2 1 
ATOM   1502 N  N   . GLN B 1 55  ? -5.455  41.962  5.583   1.00 38.78  ? 55   GLN B N   1 
ATOM   1503 C  CA  . GLN B 1 55  ? -4.242  41.525  6.256   1.00 38.12  ? 55   GLN B CA  1 
ATOM   1504 C  C   . GLN B 1 55  ? -3.327  42.715  6.421   1.00 37.43  ? 55   GLN B C   1 
ATOM   1505 O  O   . GLN B 1 55  ? -2.112  42.632  6.236   1.00 40.27  ? 55   GLN B O   1 
ATOM   1506 C  CB  . GLN B 1 55  ? -3.566  40.402  5.476   1.00 38.53  ? 55   GLN B CB  1 
ATOM   1507 C  CG  . GLN B 1 55  ? -4.551  39.318  5.050   1.00 48.75  ? 55   GLN B CG  1 
ATOM   1508 C  CD  . GLN B 1 55  ? -3.940  37.932  5.026   1.00 63.03  ? 55   GLN B CD  1 
ATOM   1509 O  OE1 . GLN B 1 55  ? -3.260  37.546  4.066   1.00 65.15  ? 55   GLN B OE1 1 
ATOM   1510 N  NE2 . GLN B 1 55  ? -4.181  37.169  6.088   1.00 64.49  ? 55   GLN B NE2 1 
ATOM   1511 N  N   . GLY B 1 56  ? -3.919  43.840  6.783   1.00 39.28  ? 56   GLY B N   1 
ATOM   1512 C  CA  . GLY B 1 56  ? -3.160  45.067  6.815   1.00 34.59  ? 56   GLY B CA  1 
ATOM   1513 C  C   . GLY B 1 56  ? -2.602  45.234  5.421   1.00 37.41  ? 56   GLY B C   1 
ATOM   1514 O  O   . GLY B 1 56  ? -3.190  44.751  4.447   1.00 37.36  ? 56   GLY B O   1 
ATOM   1515 N  N   . CYS B 1 57  ? -1.446  45.874  5.328   1.00 36.58  ? 57   CYS B N   1 
ATOM   1516 C  CA  . CYS B 1 57  ? -0.936  46.355  4.052   1.00 33.72  ? 57   CYS B CA  1 
ATOM   1517 C  C   . CYS B 1 57  ? -0.563  45.252  3.054   1.00 33.22  ? 57   CYS B C   1 
ATOM   1518 O  O   . CYS B 1 57  ? -0.660  45.433  1.837   1.00 30.95  ? 57   CYS B O   1 
ATOM   1519 C  CB  . CYS B 1 57  ? 0.224   47.319  4.295   1.00 30.66  ? 57   CYS B CB  1 
ATOM   1520 S  SG  . CYS B 1 57  ? -0.349  48.891  4.948   1.00 42.93  ? 57   CYS B SG  1 
ATOM   1521 N  N   . THR B 1 58  ? -0.187  44.093  3.574   1.00 37.12  ? 58   THR B N   1 
ATOM   1522 C  CA  . THR B 1 58  ? 0.290   43.006  2.732   1.00 32.58  ? 58   THR B CA  1 
ATOM   1523 C  C   . THR B 1 58  ? -0.771  42.501  1.740   1.00 33.29  ? 58   THR B C   1 
ATOM   1524 O  O   . THR B 1 58  ? -0.430  41.991  0.666   1.00 32.80  ? 58   THR B O   1 
ATOM   1525 C  CB  . THR B 1 58  ? 0.886   41.849  3.591   1.00 34.92  ? 58   THR B CB  1 
ATOM   1526 O  OG1 . THR B 1 58  ? 0.344   40.596  3.168   1.00 43.56  ? 58   THR B OG1 1 
ATOM   1527 C  CG2 . THR B 1 58  ? 0.553   42.037  5.042   1.00 33.76  ? 58   THR B CG2 1 
ATOM   1528 N  N   . SER B 1 59  ? -2.049  42.668  2.072   1.00 30.92  ? 59   SER B N   1 
ATOM   1529 C  CA  . SER B 1 59  ? -3.114  42.162  1.196   1.00 33.91  ? 59   SER B CA  1 
ATOM   1530 C  C   . SER B 1 59  ? -3.415  43.062  0.005   1.00 30.87  ? 59   SER B C   1 
ATOM   1531 O  O   . SER B 1 59  ? -4.235  42.717  -0.839  1.00 29.41  ? 59   SER B O   1 
ATOM   1532 C  CB  . SER B 1 59  ? -4.396  41.851  1.985   1.00 36.04  ? 59   SER B CB  1 
ATOM   1533 O  OG  . SER B 1 59  ? -4.531  42.703  3.100   1.00 34.28  ? 59   SER B OG  1 
ATOM   1534 N  N   . ALA B 1 60  ? -2.734  44.207  -0.061  1.00 30.41  ? 60   ALA B N   1 
ATOM   1535 C  CA  . ALA B 1 60  ? -2.901  45.158  -1.162  1.00 29.48  ? 60   ALA B CA  1 
ATOM   1536 C  C   . ALA B 1 60  ? -2.319  44.651  -2.499  1.00 30.90  ? 60   ALA B C   1 
ATOM   1537 O  O   . ALA B 1 60  ? -2.539  45.252  -3.564  1.00 30.29  ? 60   ALA B O   1 
ATOM   1538 C  CB  . ALA B 1 60  ? -2.275  46.518  -0.781  1.00 27.62  ? 60   ALA B CB  1 
ATOM   1539 N  N   . GLY B 1 61  ? -1.569  43.555  -2.441  1.00 32.30  ? 61   GLY B N   1 
ATOM   1540 C  CA  . GLY B 1 61  ? -0.948  42.993  -3.626  1.00 30.63  ? 61   GLY B CA  1 
ATOM   1541 C  C   . GLY B 1 61  ? 0.286   43.754  -4.099  1.00 35.21  ? 61   GLY B C   1 
ATOM   1542 O  O   . GLY B 1 61  ? 0.941   44.500  -3.341  1.00 29.43  ? 61   GLY B O   1 
ATOM   1543 N  N   . PRO B 1 62  ? 0.621   43.567  -5.377  1.00 29.28  ? 62   PRO B N   1 
ATOM   1544 C  CA  . PRO B 1 62  ? 1.811   44.177  -5.978  1.00 30.55  ? 62   PRO B CA  1 
ATOM   1545 C  C   . PRO B 1 62  ? 1.527   45.620  -6.379  1.00 27.37  ? 62   PRO B C   1 
ATOM   1546 O  O   . PRO B 1 62  ? 0.385   46.064  -6.268  1.00 29.54  ? 62   PRO B O   1 
ATOM   1547 C  CB  . PRO B 1 62  ? 2.038   43.316  -7.229  1.00 28.89  ? 62   PRO B CB  1 
ATOM   1548 C  CG  . PRO B 1 62  ? 0.656   42.821  -7.629  1.00 28.22  ? 62   PRO B CG  1 
ATOM   1549 C  CD  . PRO B 1 62  ? -0.204  42.838  -6.359  1.00 32.79  ? 62   PRO B CD  1 
ATOM   1550 N  N   . HIS B 1 63  ? 2.538   46.340  -6.841  1.00 23.62  ? 63   HIS B N   1 
ATOM   1551 C  CA  . HIS B 1 63  ? 2.290   47.627  -7.485  1.00 30.27  ? 63   HIS B CA  1 
ATOM   1552 C  C   . HIS B 1 63  ? 1.244   47.515  -8.603  1.00 27.90  ? 63   HIS B C   1 
ATOM   1553 O  O   . HIS B 1 63  ? 1.184   46.520  -9.304  1.00 29.71  ? 63   HIS B O   1 
ATOM   1554 C  CB  . HIS B 1 63  ? 3.590   48.215  -8.027  1.00 26.91  ? 63   HIS B CB  1 
ATOM   1555 C  CG  . HIS B 1 63  ? 4.607   48.482  -6.967  1.00 27.30  ? 63   HIS B CG  1 
ATOM   1556 N  ND1 . HIS B 1 63  ? 5.875   48.934  -7.246  1.00 28.60  ? 63   HIS B ND1 1 
ATOM   1557 C  CD2 . HIS B 1 63  ? 4.545   48.352  -5.622  1.00 30.17  ? 63   HIS B CD2 1 
ATOM   1558 C  CE1 . HIS B 1 63  ? 6.551   49.080  -6.124  1.00 29.54  ? 63   HIS B CE1 1 
ATOM   1559 N  NE2 . HIS B 1 63  ? 5.765   48.738  -5.121  1.00 34.47  ? 63   HIS B NE2 1 
ATOM   1560 N  N   . PHE B 1 64  ? 0.415   48.536  -8.756  1.00 24.87  ? 64   PHE B N   1 
ATOM   1561 C  CA  . PHE B 1 64  ? -0.637  48.490  -9.749  1.00 29.35  ? 64   PHE B CA  1 
ATOM   1562 C  C   . PHE B 1 64  ? -0.022  48.514  -11.171 1.00 33.93  ? 64   PHE B C   1 
ATOM   1563 O  O   . PHE B 1 64  ? 0.603   49.494  -11.579 1.00 31.03  ? 64   PHE B O   1 
ATOM   1564 C  CB  . PHE B 1 64  ? -1.640  49.631  -9.510  1.00 25.25  ? 64   PHE B CB  1 
ATOM   1565 C  CG  . PHE B 1 64  ? -2.738  49.726  -10.553 1.00 27.12  ? 64   PHE B CG  1 
ATOM   1566 C  CD1 . PHE B 1 64  ? -3.392  48.585  -11.014 1.00 24.09  ? 64   PHE B CD1 1 
ATOM   1567 C  CD2 . PHE B 1 64  ? -3.124  50.967  -11.054 1.00 25.67  ? 64   PHE B CD2 1 
ATOM   1568 C  CE1 . PHE B 1 64  ? -4.390  48.671  -11.952 1.00 21.78  ? 64   PHE B CE1 1 
ATOM   1569 C  CE2 . PHE B 1 64  ? -4.146  51.061  -11.999 1.00 25.38  ? 64   PHE B CE2 1 
ATOM   1570 C  CZ  . PHE B 1 64  ? -4.771  49.908  -12.446 1.00 25.47  ? 64   PHE B CZ  1 
ATOM   1571 N  N   . ASN B 1 65  ? -0.237  47.433  -11.918 1.00 30.55  ? 65   ASN B N   1 
ATOM   1572 C  CA  . ASN B 1 65  ? 0.517   47.167  -13.134 1.00 32.15  ? 65   ASN B CA  1 
ATOM   1573 C  C   . ASN B 1 65  ? -0.304  46.525  -14.268 1.00 34.23  ? 65   ASN B C   1 
ATOM   1574 O  O   . ASN B 1 65  ? -0.006  45.402  -14.675 1.00 34.04  ? 65   ASN B O   1 
ATOM   1575 C  CB  . ASN B 1 65  ? 1.697   46.254  -12.774 1.00 31.27  ? 65   ASN B CB  1 
ATOM   1576 C  CG  . ASN B 1 65  ? 2.739   46.194  -13.861 1.00 30.94  ? 65   ASN B CG  1 
ATOM   1577 O  OD1 . ASN B 1 65  ? 2.821   47.088  -14.685 1.00 31.90  ? 65   ASN B OD1 1 
ATOM   1578 N  ND2 . ASN B 1 65  ? 3.546   45.143  -13.862 1.00 30.02  ? 65   ASN B ND2 1 
ATOM   1579 N  N   . PRO B 1 66  ? -1.325  47.241  -14.785 1.00 31.24  ? 66   PRO B N   1 
ATOM   1580 C  CA  . PRO B 1 66  ? -2.222  46.806  -15.863 1.00 37.89  ? 66   PRO B CA  1 
ATOM   1581 C  C   . PRO B 1 66  ? -1.491  46.284  -17.100 1.00 39.52  ? 66   PRO B C   1 
ATOM   1582 O  O   . PRO B 1 66  ? -2.009  45.396  -17.765 1.00 41.23  ? 66   PRO B O   1 
ATOM   1583 C  CB  . PRO B 1 66  ? -2.941  48.100  -16.285 1.00 32.64  ? 66   PRO B CB  1 
ATOM   1584 C  CG  . PRO B 1 66  ? -2.706  49.056  -15.262 1.00 32.52  ? 66   PRO B CG  1 
ATOM   1585 C  CD  . PRO B 1 66  ? -1.494  48.668  -14.487 1.00 33.73  ? 66   PRO B CD  1 
ATOM   1586 N  N   . HIS B 1 67  ? -0.333  46.847  -17.426 1.00 37.25  ? 67   HIS B N   1 
ATOM   1587 C  CA  . HIS B 1 67  ? 0.327   46.512  -18.686 1.00 41.11  ? 67   HIS B CA  1 
ATOM   1588 C  C   . HIS B 1 67  ? 1.496   45.539  -18.518 1.00 39.94  ? 67   HIS B C   1 
ATOM   1589 O  O   . HIS B 1 67  ? 2.256   45.312  -19.453 1.00 39.27  ? 67   HIS B O   1 
ATOM   1590 C  CB  . HIS B 1 67  ? 0.788   47.785  -19.402 1.00 37.77  ? 67   HIS B CB  1 
ATOM   1591 C  CG  . HIS B 1 67  ? -0.268  48.844  -19.490 1.00 38.72  ? 67   HIS B CG  1 
ATOM   1592 N  ND1 . HIS B 1 67  ? -1.484  48.634  -20.107 1.00 41.41  ? 67   HIS B ND1 1 
ATOM   1593 C  CD2 . HIS B 1 67  ? -0.289  50.125  -19.046 1.00 36.48  ? 67   HIS B CD2 1 
ATOM   1594 C  CE1 . HIS B 1 67  ? -2.206  49.742  -20.044 1.00 39.08  ? 67   HIS B CE1 1 
ATOM   1595 N  NE2 . HIS B 1 67  ? -1.504  50.661  -19.404 1.00 35.60  ? 67   HIS B NE2 1 
ATOM   1596 N  N   . SER B 1 68  ? 1.633   44.968  -17.329 1.00 34.50  ? 68   SER B N   1 
ATOM   1597 C  CA  . SER B 1 68  ? 2.673   43.968  -17.081 1.00 40.18  ? 68   SER B CA  1 
ATOM   1598 C  C   . SER B 1 68  ? 4.078   44.471  -17.389 1.00 40.52  ? 68   SER B C   1 
ATOM   1599 O  O   . SER B 1 68  ? 4.948   43.690  -17.771 1.00 43.23  ? 68   SER B O   1 
ATOM   1600 C  CB  . SER B 1 68  ? 2.418   42.684  -17.885 1.00 41.07  ? 68   SER B CB  1 
ATOM   1601 O  OG  . SER B 1 68  ? 1.283   41.977  -17.423 1.00 38.61  ? 68   SER B OG  1 
ATOM   1602 N  N   . LYS B 1 69  ? 4.301   45.769  -17.230 1.00 38.96  ? 69   LYS B N   1 
ATOM   1603 C  CA  . LYS B 1 69  ? 5.636   46.320  -17.409 1.00 36.67  ? 69   LYS B CA  1 
ATOM   1604 C  C   . LYS B 1 69  ? 6.531   46.127  -16.184 1.00 37.50  ? 69   LYS B C   1 
ATOM   1605 O  O   . LYS B 1 69  ? 6.132   45.523  -15.186 1.00 39.14  ? 69   LYS B O   1 
ATOM   1606 C  CB  . LYS B 1 69  ? 5.546   47.793  -17.790 1.00 36.33  ? 69   LYS B CB  1 
ATOM   1607 C  CG  . LYS B 1 69  ? 4.620   48.009  -18.969 1.00 40.00  ? 69   LYS B CG  1 
ATOM   1608 C  CD  . LYS B 1 69  ? 5.308   48.739  -20.100 1.00 39.59  ? 69   LYS B CD  1 
ATOM   1609 C  CE  . LYS B 1 69  ? 5.060   50.244  -20.025 1.00 49.44  ? 69   LYS B CE  1 
ATOM   1610 N  NZ  . LYS B 1 69  ? 4.135   50.716  -21.111 1.00 46.96  ? 69   LYS B NZ  1 
ATOM   1611 N  N   . LYS B 1 70  ? 7.756   46.629  -16.279 1.00 36.72  ? 70   LYS B N   1 
ATOM   1612 C  CA  . LYS B 1 70  ? 8.691   46.610  -15.161 1.00 38.67  ? 70   LYS B CA  1 
ATOM   1613 C  C   . LYS B 1 70  ? 8.594   47.867  -14.292 1.00 34.32  ? 70   LYS B C   1 
ATOM   1614 O  O   . LYS B 1 70  ? 8.167   48.934  -14.750 1.00 33.07  ? 70   LYS B O   1 
ATOM   1615 C  CB  . LYS B 1 70  ? 10.133  46.455  -15.670 1.00 46.58  ? 70   LYS B CB  1 
ATOM   1616 C  CG  . LYS B 1 70  ? 10.484  45.051  -16.149 1.00 48.45  ? 70   LYS B CG  1 
ATOM   1617 C  CD  . LYS B 1 70  ? 11.990  44.846  -16.243 1.00 53.77  ? 70   LYS B CD  1 
ATOM   1618 C  CE  . LYS B 1 70  ? 12.332  43.362  -16.480 1.00 68.05  ? 70   LYS B CE  1 
ATOM   1619 N  NZ  . LYS B 1 70  ? 11.804  42.435  -15.407 1.00 67.37  ? 70   LYS B NZ  1 
ATOM   1620 N  N   . HIS B 1 71  ? 9.006   47.724  -13.036 1.00 34.36  ? 71   HIS B N   1 
ATOM   1621 C  CA  . HIS B 1 71  ? 9.094   48.849  -12.110 1.00 34.92  ? 71   HIS B CA  1 
ATOM   1622 C  C   . HIS B 1 71  ? 10.093  49.919  -12.592 1.00 37.77  ? 71   HIS B C   1 
ATOM   1623 O  O   . HIS B 1 71  ? 11.199  49.605  -13.026 1.00 34.41  ? 71   HIS B O   1 
ATOM   1624 C  CB  . HIS B 1 71  ? 9.483   48.352  -10.720 1.00 33.05  ? 71   HIS B CB  1 
ATOM   1625 C  CG  . HIS B 1 71  ? 9.567   49.439  -9.702  1.00 33.63  ? 71   HIS B CG  1 
ATOM   1626 N  ND1 . HIS B 1 71  ? 8.460   49.935  -9.049  1.00 33.48  ? 71   HIS B ND1 1 
ATOM   1627 C  CD2 . HIS B 1 71  ? 10.625  50.137  -9.231  1.00 34.61  ? 71   HIS B CD2 1 
ATOM   1628 C  CE1 . HIS B 1 71  ? 8.829   50.898  -8.225  1.00 31.26  ? 71   HIS B CE1 1 
ATOM   1629 N  NE2 . HIS B 1 71  ? 10.138  51.041  -8.317  1.00 35.00  ? 71   HIS B NE2 1 
ATOM   1630 N  N   . GLY B 1 72  ? 9.687   51.183  -12.522 1.00 35.89  ? 72   GLY B N   1 
ATOM   1631 C  CA  . GLY B 1 72  ? 10.555  52.287  -12.868 1.00 28.36  ? 72   GLY B CA  1 
ATOM   1632 C  C   . GLY B 1 72  ? 10.181  53.515  -12.062 1.00 37.54  ? 72   GLY B C   1 
ATOM   1633 O  O   . GLY B 1 72  ? 9.314   53.462  -11.180 1.00 34.28  ? 72   GLY B O   1 
ATOM   1634 N  N   . GLY B 1 73  ? 10.849  54.626  -12.339 1.00 33.28  ? 73   GLY B N   1 
ATOM   1635 C  CA  . GLY B 1 73  ? 10.508  55.867  -11.684 1.00 29.16  ? 73   GLY B CA  1 
ATOM   1636 C  C   . GLY B 1 73  ? 9.337   56.510  -12.388 1.00 33.43  ? 73   GLY B C   1 
ATOM   1637 O  O   . GLY B 1 73  ? 8.962   56.089  -13.482 1.00 35.57  ? 73   GLY B O   1 
ATOM   1638 N  N   . PRO B 1 74  ? 8.739   57.527  -11.760 1.00 34.47  ? 74   PRO B N   1 
ATOM   1639 C  CA  . PRO B 1 74  ? 7.570   58.200  -12.339 1.00 36.67  ? 74   PRO B CA  1 
ATOM   1640 C  C   . PRO B 1 74  ? 7.869   58.780  -13.721 1.00 35.57  ? 74   PRO B C   1 
ATOM   1641 O  O   . PRO B 1 74  ? 6.962   58.885  -14.548 1.00 33.98  ? 74   PRO B O   1 
ATOM   1642 C  CB  . PRO B 1 74  ? 7.292   59.354  -11.364 1.00 31.19  ? 74   PRO B CB  1 
ATOM   1643 C  CG  . PRO B 1 74  ? 8.019   59.046  -10.146 1.00 30.36  ? 74   PRO B CG  1 
ATOM   1644 C  CD  . PRO B 1 74  ? 9.166   58.130  -10.488 1.00 29.73  ? 74   PRO B CD  1 
ATOM   1645 N  N   . ALA B 1 75  ? 9.117   59.175  -13.959 1.00 35.42  ? 75   ALA B N   1 
ATOM   1646 C  CA  . ALA B 1 75  ? 9.476   59.814  -15.241 1.00 39.33  ? 75   ALA B CA  1 
ATOM   1647 C  C   . ALA B 1 75  ? 9.875   58.809  -16.351 1.00 38.11  ? 75   ALA B C   1 
ATOM   1648 O  O   . ALA B 1 75  ? 10.087  59.183  -17.506 1.00 44.24  ? 75   ALA B O   1 
ATOM   1649 C  CB  . ALA B 1 75  ? 10.557  60.881  -15.029 1.00 28.83  ? 75   ALA B CB  1 
ATOM   1650 N  N   . ASP B 1 76  ? 9.950   57.533  -16.001 1.00 33.07  ? 76   ASP B N   1 
ATOM   1651 C  CA  . ASP B 1 76  ? 10.247  56.503  -16.968 1.00 37.06  ? 76   ASP B CA  1 
ATOM   1652 C  C   . ASP B 1 76  ? 8.984   56.147  -17.756 1.00 44.07  ? 76   ASP B C   1 
ATOM   1653 O  O   . ASP B 1 76  ? 7.860   56.294  -17.262 1.00 42.72  ? 76   ASP B O   1 
ATOM   1654 C  CB  . ASP B 1 76  ? 10.790  55.263  -16.259 1.00 36.80  ? 76   ASP B CB  1 
ATOM   1655 C  CG  . ASP B 1 76  ? 12.113  55.518  -15.571 1.00 36.98  ? 76   ASP B CG  1 
ATOM   1656 O  OD1 . ASP B 1 76  ? 12.706  56.590  -15.793 1.00 40.49  ? 76   ASP B OD1 1 
ATOM   1657 O  OD2 . ASP B 1 76  ? 12.568  54.648  -14.806 1.00 39.11  ? 76   ASP B OD2 1 
ATOM   1658 N  N   . GLU B 1 77  ? 9.171   55.691  -18.989 1.00 40.93  ? 77   GLU B N   1 
ATOM   1659 C  CA  . GLU B 1 77  ? 8.068   55.171  -19.778 1.00 44.00  ? 77   GLU B CA  1 
ATOM   1660 C  C   . GLU B 1 77  ? 7.825   53.734  -19.336 1.00 39.80  ? 77   GLU B C   1 
ATOM   1661 O  O   . GLU B 1 77  ? 6.688   53.254  -19.326 1.00 39.28  ? 77   GLU B O   1 
ATOM   1662 C  CB  . GLU B 1 77  ? 8.396   55.228  -21.278 1.00 47.17  ? 77   GLU B CB  1 
ATOM   1663 C  CG  . GLU B 1 77  ? 7.164   55.187  -22.201 1.00 49.73  ? 77   GLU B CG  1 
ATOM   1664 C  CD  . GLU B 1 77  ? 6.658   53.771  -22.492 1.00 60.15  ? 77   GLU B CD  1 
ATOM   1665 O  OE1 . GLU B 1 77  ? 5.423   53.610  -22.683 1.00 57.04  ? 77   GLU B OE1 1 
ATOM   1666 O  OE2 . GLU B 1 77  ? 7.492   52.824  -22.526 1.00 58.29  ? 77   GLU B OE2 1 
ATOM   1667 N  N   . GLU B 1 78  ? 8.911   53.052  -18.986 1.00 35.69  ? 78   GLU B N   1 
ATOM   1668 C  CA  . GLU B 1 78  ? 8.838   51.708  -18.447 1.00 34.18  ? 78   GLU B CA  1 
ATOM   1669 C  C   . GLU B 1 78  ? 8.635   51.813  -16.936 1.00 38.41  ? 78   GLU B C   1 
ATOM   1670 O  O   . GLU B 1 78  ? 9.603   51.935  -16.181 1.00 37.02  ? 78   GLU B O   1 
ATOM   1671 C  CB  . GLU B 1 78  ? 10.134  50.952  -18.736 1.00 35.12  ? 78   GLU B CB  1 
ATOM   1672 C  CG  . GLU B 1 78  ? 10.104  49.493  -18.300 1.00 34.03  ? 78   GLU B CG  1 
ATOM   1673 C  CD  . GLU B 1 78  ? 9.313   48.623  -19.267 1.00 41.97  ? 78   GLU B CD  1 
ATOM   1674 O  OE1 . GLU B 1 78  ? 9.060   49.086  -20.404 1.00 46.11  ? 78   GLU B OE1 1 
ATOM   1675 O  OE2 . GLU B 1 78  ? 8.951   47.477  -18.905 1.00 42.02  ? 78   GLU B OE2 1 
ATOM   1676 N  N   . ARG B 1 79  ? 7.377   51.788  -16.501 1.00 38.11  ? 79   ARG B N   1 
ATOM   1677 C  CA  . ARG B 1 79  ? 7.034   51.831  -15.079 1.00 33.80  ? 79   ARG B CA  1 
ATOM   1678 C  C   . ARG B 1 79  ? 5.716   51.141  -14.883 1.00 32.13  ? 79   ARG B C   1 
ATOM   1679 O  O   . ARG B 1 79  ? 4.905   51.078  -15.803 1.00 34.64  ? 79   ARG B O   1 
ATOM   1680 C  CB  . ARG B 1 79  ? 6.857   53.269  -14.629 1.00 33.38  ? 79   ARG B CB  1 
ATOM   1681 C  CG  . ARG B 1 79  ? 6.003   54.087  -15.590 1.00 32.79  ? 79   ARG B CG  1 
ATOM   1682 C  CD  . ARG B 1 79  ? 5.638   55.415  -14.973 1.00 33.45  ? 79   ARG B CD  1 
ATOM   1683 N  NE  . ARG B 1 79  ? 4.502   55.314  -14.066 1.00 33.75  ? 79   ARG B NE  1 
ATOM   1684 C  CZ  . ARG B 1 79  ? 3.976   56.360  -13.440 1.00 35.02  ? 79   ARG B CZ  1 
ATOM   1685 N  NH1 . ARG B 1 79  ? 4.504   57.562  -13.612 1.00 32.83  ? 79   ARG B NH1 1 
ATOM   1686 N  NH2 . ARG B 1 79  ? 2.930   56.208  -12.643 1.00 34.65  ? 79   ARG B NH2 1 
ATOM   1687 N  N   . HIS B 1 80  ? 5.479   50.645  -13.678 1.00 34.12  ? 80   HIS B N   1 
ATOM   1688 C  CA  . HIS B 1 80  ? 4.143   50.201  -13.323 1.00 30.42  ? 80   HIS B CA  1 
ATOM   1689 C  C   . HIS B 1 80  ? 3.277   51.470  -13.305 1.00 28.66  ? 80   HIS B C   1 
ATOM   1690 O  O   . HIS B 1 80  ? 3.784   52.571  -13.077 1.00 31.63  ? 80   HIS B O   1 
ATOM   1691 C  CB  . HIS B 1 80  ? 4.165   49.550  -11.945 1.00 31.90  ? 80   HIS B CB  1 
ATOM   1692 C  CG  . HIS B 1 80  ? 5.094   48.386  -11.834 1.00 27.82  ? 80   HIS B CG  1 
ATOM   1693 N  ND1 . HIS B 1 80  ? 5.722   48.051  -10.657 1.00 33.34  ? 80   HIS B ND1 1 
ATOM   1694 C  CD2 . HIS B 1 80  ? 5.475   47.456  -12.739 1.00 31.46  ? 80   HIS B CD2 1 
ATOM   1695 C  CE1 . HIS B 1 80  ? 6.465   46.972  -10.840 1.00 32.61  ? 80   HIS B CE1 1 
ATOM   1696 N  NE2 . HIS B 1 80  ? 6.324   46.586  -12.095 1.00 36.87  ? 80   HIS B NE2 1 
ATOM   1697 N  N   . VAL B 1 81  ? 1.986   51.351  -13.572 1.00 28.08  ? 81   VAL B N   1 
ATOM   1698 C  CA  . VAL B 1 81  ? 1.131   52.527  -13.449 1.00 32.56  ? 81   VAL B CA  1 
ATOM   1699 C  C   . VAL B 1 81  ? 1.196   53.114  -12.023 1.00 31.23  ? 81   VAL B C   1 
ATOM   1700 O  O   . VAL B 1 81  ? 1.120   54.330  -11.837 1.00 27.77  ? 81   VAL B O   1 
ATOM   1701 C  CB  . VAL B 1 81  ? -0.321  52.223  -13.825 1.00 30.75  ? 81   VAL B CB  1 
ATOM   1702 C  CG1 . VAL B 1 81  ? -1.194  53.427  -13.522 1.00 27.74  ? 81   VAL B CG1 1 
ATOM   1703 C  CG2 . VAL B 1 81  ? -0.415  51.820  -15.301 1.00 29.51  ? 81   VAL B CG2 1 
ATOM   1704 N  N   . GLY B 1 82  ? 1.373   52.244  -11.025 1.00 29.30  ? 82   GLY B N   1 
ATOM   1705 C  CA  . GLY B 1 82  ? 1.401   52.664  -9.633  1.00 28.20  ? 82   GLY B CA  1 
ATOM   1706 C  C   . GLY B 1 82  ? 2.676   53.342  -9.148  1.00 31.74  ? 82   GLY B C   1 
ATOM   1707 O  O   . GLY B 1 82  ? 2.717   53.803  -7.996  1.00 30.91  ? 82   GLY B O   1 
ATOM   1708 N  N   . ASP B 1 83  ? 3.701   53.411  -10.008 1.00 27.77  ? 83   ASP B N   1 
ATOM   1709 C  CA  . ASP B 1 83  ? 5.030   53.917  -9.625  1.00 30.30  ? 83   ASP B CA  1 
ATOM   1710 C  C   . ASP B 1 83  ? 5.085   55.435  -9.445  1.00 32.62  ? 83   ASP B C   1 
ATOM   1711 O  O   . ASP B 1 83  ? 5.258   56.178  -10.406 1.00 32.08  ? 83   ASP B O   1 
ATOM   1712 C  CB  . ASP B 1 83  ? 6.108   53.450  -10.622 1.00 30.70  ? 83   ASP B CB  1 
ATOM   1713 C  CG  . ASP B 1 83  ? 6.365   51.956  -10.531 1.00 32.30  ? 83   ASP B CG  1 
ATOM   1714 O  OD1 . ASP B 1 83  ? 6.972   51.360  -11.457 1.00 34.62  ? 83   ASP B OD1 1 
ATOM   1715 O  OD2 . ASP B 1 83  ? 5.941   51.377  -9.516  1.00 26.89  ? 83   ASP B OD2 1 
ATOM   1716 N  N   . LEU B 1 84  ? 4.952   55.903  -8.209  1.00 30.24  ? 84   LEU B N   1 
ATOM   1717 C  CA  . LEU B 1 84  ? 4.920   57.341  -7.999  1.00 32.05  ? 84   LEU B CA  1 
ATOM   1718 C  C   . LEU B 1 84  ? 6.230   57.895  -7.434  1.00 30.85  ? 84   LEU B C   1 
ATOM   1719 O  O   . LEU B 1 84  ? 6.320   59.066  -7.084  1.00 31.55  ? 84   LEU B O   1 
ATOM   1720 C  CB  . LEU B 1 84  ? 3.726   57.728  -7.126  1.00 29.51  ? 84   LEU B CB  1 
ATOM   1721 C  CG  . LEU B 1 84  ? 2.356   57.382  -7.702  1.00 28.55  ? 84   LEU B CG  1 
ATOM   1722 C  CD1 . LEU B 1 84  ? 1.258   57.636  -6.663  1.00 29.06  ? 84   LEU B CD1 1 
ATOM   1723 C  CD2 . LEU B 1 84  ? 2.100   58.199  -8.924  1.00 26.97  ? 84   LEU B CD2 1 
ATOM   1724 N  N   . GLY B 1 85  ? 7.241   57.046  -7.339  1.00 27.31  ? 85   GLY B N   1 
ATOM   1725 C  CA  . GLY B 1 85  ? 8.556   57.495  -6.925  1.00 30.68  ? 85   GLY B CA  1 
ATOM   1726 C  C   . GLY B 1 85  ? 8.763   57.588  -5.425  1.00 32.04  ? 85   GLY B C   1 
ATOM   1727 O  O   . GLY B 1 85  ? 8.425   56.674  -4.660  1.00 30.54  ? 85   GLY B O   1 
ATOM   1728 N  N   . ASN B 1 86  ? 9.333   58.706  -4.998  1.00 32.52  ? 86   ASN B N   1 
ATOM   1729 C  CA  . ASN B 1 86  ? 9.628   58.878  -3.593  1.00 30.37  ? 86   ASN B CA  1 
ATOM   1730 C  C   . ASN B 1 86  ? 8.941   60.060  -2.933  1.00 32.82  ? 86   ASN B C   1 
ATOM   1731 O  O   . ASN B 1 86  ? 8.481   61.007  -3.572  1.00 30.35  ? 86   ASN B O   1 
ATOM   1732 C  CB  . ASN B 1 86  ? 11.134  58.930  -3.353  1.00 30.41  ? 86   ASN B CB  1 
ATOM   1733 C  CG  . ASN B 1 86  ? 11.788  57.596  -3.582  1.00 31.98  ? 86   ASN B CG  1 
ATOM   1734 O  OD1 . ASN B 1 86  ? 11.698  56.695  -2.745  1.00 31.16  ? 86   ASN B OD1 1 
ATOM   1735 N  ND2 . ASN B 1 86  ? 12.430  57.444  -4.733  1.00 28.97  ? 86   ASN B ND2 1 
ATOM   1736 N  N   . VAL B 1 87  ? 8.901   59.970  -1.617  1.00 27.70  ? 87   VAL B N   1 
ATOM   1737 C  CA  . VAL B 1 87  ? 8.278   60.949  -0.790  1.00 26.65  ? 87   VAL B CA  1 
ATOM   1738 C  C   . VAL B 1 87  ? 9.356   61.237  0.253   1.00 27.86  ? 87   VAL B C   1 
ATOM   1739 O  O   . VAL B 1 87  ? 10.162  60.367  0.555   1.00 28.18  ? 87   VAL B O   1 
ATOM   1740 C  CB  . VAL B 1 87  ? 6.925   60.345  -0.258  1.00 32.96  ? 87   VAL B CB  1 
ATOM   1741 C  CG1 . VAL B 1 87  ? 6.890   60.175  1.254   1.00 26.73  ? 87   VAL B CG1 1 
ATOM   1742 C  CG2 . VAL B 1 87  ? 5.693   61.092  -0.859  1.00 24.72  ? 87   VAL B CG2 1 
ATOM   1743 N  N   . THR B 1 88  ? 9.405   62.469  0.754   1.00 31.02  ? 88   THR B N   1 
ATOM   1744 C  CA  . THR B 1 88  ? 10.539  62.934  1.539   1.00 28.74  ? 88   THR B CA  1 
ATOM   1745 C  C   . THR B 1 88  ? 10.190  63.477  2.926   1.00 28.26  ? 88   THR B C   1 
ATOM   1746 O  O   . THR B 1 88  ? 9.500   64.507  3.068   1.00 26.37  ? 88   THR B O   1 
ATOM   1747 C  CB  . THR B 1 88  ? 11.305  64.029  0.754   1.00 33.68  ? 88   THR B CB  1 
ATOM   1748 O  OG1 . THR B 1 88  ? 11.943  63.433  -0.380  1.00 30.35  ? 88   THR B OG1 1 
ATOM   1749 C  CG2 . THR B 1 88  ? 12.363  64.713  1.643   1.00 31.02  ? 88   THR B CG2 1 
ATOM   1750 N  N   . ALA B 1 89  ? 10.696  62.792  3.945   1.00 28.35  ? 89   ALA B N   1 
ATOM   1751 C  CA  . ALA B 1 89  ? 10.480  63.189  5.336   1.00 31.40  ? 89   ALA B CA  1 
ATOM   1752 C  C   . ALA B 1 89  ? 11.612  64.084  5.855   1.00 36.24  ? 89   ALA B C   1 
ATOM   1753 O  O   . ALA B 1 89  ? 12.790  63.815  5.598   1.00 33.23  ? 89   ALA B O   1 
ATOM   1754 C  CB  . ALA B 1 89  ? 10.345  61.947  6.221   1.00 31.53  ? 89   ALA B CB  1 
ATOM   1755 N  N   . ASP B 1 90  ? 11.258  65.131  6.601   1.00 36.84  ? 90   ASP B N   1 
ATOM   1756 C  CA  . ASP B 1 90  ? 12.274  65.976  7.233   1.00 37.34  ? 90   ASP B CA  1 
ATOM   1757 C  C   . ASP B 1 90  ? 12.870  65.374  8.513   1.00 40.06  ? 90   ASP B C   1 
ATOM   1758 O  O   . ASP B 1 90  ? 12.618  64.209  8.851   1.00 39.31  ? 90   ASP B O   1 
ATOM   1759 C  CB  . ASP B 1 90  ? 11.760  67.412  7.467   1.00 33.64  ? 90   ASP B CB  1 
ATOM   1760 C  CG  . ASP B 1 90  ? 10.623  67.493  8.479   1.00 39.65  ? 90   ASP B CG  1 
ATOM   1761 O  OD1 . ASP B 1 90  ? 10.491  66.610  9.367   1.00 40.77  ? 90   ASP B OD1 1 
ATOM   1762 O  OD2 . ASP B 1 90  ? 9.861   68.481  8.394   1.00 37.18  ? 90   ASP B OD2 1 
ATOM   1763 N  N   . LYS B 1 91  ? 13.671  66.176  9.213   1.00 42.98  ? 91   LYS B N   1 
ATOM   1764 C  CA  . LYS B 1 91  ? 14.315  65.727  10.444  1.00 46.25  ? 91   LYS B CA  1 
ATOM   1765 C  C   . LYS B 1 91  ? 13.313  65.354  11.540  1.00 45.48  ? 91   LYS B C   1 
ATOM   1766 O  O   . LYS B 1 91  ? 13.570  64.450  12.343  1.00 49.20  ? 91   LYS B O   1 
ATOM   1767 C  CB  . LYS B 1 91  ? 15.338  66.753  10.948  1.00 46.45  ? 91   LYS B CB  1 
ATOM   1768 C  CG  . LYS B 1 91  ? 14.908  68.205  10.865  1.00 48.98  ? 91   LYS B CG  1 
ATOM   1769 C  CD  . LYS B 1 91  ? 15.976  69.110  11.493  1.00 53.09  ? 91   LYS B CD  1 
ATOM   1770 C  CE  . LYS B 1 91  ? 15.763  70.597  11.181  1.00 55.71  ? 91   LYS B CE  1 
ATOM   1771 N  NZ  . LYS B 1 91  ? 14.466  71.145  11.698  1.00 54.06  ? 91   LYS B NZ  1 
ATOM   1772 N  N   . ASP B 1 92  ? 12.168  66.036  11.552  1.00 42.86  ? 92   ASP B N   1 
ATOM   1773 C  CA  . ASP B 1 92  ? 11.097  65.745  12.503  1.00 38.51  ? 92   ASP B CA  1 
ATOM   1774 C  C   . ASP B 1 92  ? 10.179  64.629  11.992  1.00 38.61  ? 92   ASP B C   1 
ATOM   1775 O  O   . ASP B 1 92  ? 9.128   64.390  12.561  1.00 38.06  ? 92   ASP B O   1 
ATOM   1776 C  CB  . ASP B 1 92  ? 10.270  67.011  12.777  1.00 39.26  ? 92   ASP B CB  1 
ATOM   1777 C  CG  . ASP B 1 92  ? 11.120  68.166  13.316  1.00 43.42  ? 92   ASP B CG  1 
ATOM   1778 O  OD1 . ASP B 1 92  ? 12.299  67.918  13.643  1.00 47.70  ? 92   ASP B OD1 1 
ATOM   1779 O  OD2 . ASP B 1 92  ? 10.621  69.315  13.419  1.00 41.87  ? 92   ASP B OD2 1 
ATOM   1780 N  N   . GLY B 1 93  ? 10.561  63.967  10.902  1.00 37.47  ? 93   GLY B N   1 
ATOM   1781 C  CA  . GLY B 1 93  ? 9.777   62.865  10.374  1.00 31.86  ? 93   GLY B CA  1 
ATOM   1782 C  C   . GLY B 1 93  ? 8.540   63.231  9.564   1.00 32.23  ? 93   GLY B C   1 
ATOM   1783 O  O   . GLY B 1 93  ? 7.694   62.384  9.302   1.00 29.91  ? 93   GLY B O   1 
ATOM   1784 N  N   . VAL B 1 94  ? 8.432   64.489  9.162   1.00 30.33  ? 94   VAL B N   1 
ATOM   1785 C  CA  . VAL B 1 94  ? 7.271   64.943  8.424   1.00 30.69  ? 94   VAL B CA  1 
ATOM   1786 C  C   . VAL B 1 94  ? 7.560   64.994  6.911   1.00 33.51  ? 94   VAL B C   1 
ATOM   1787 O  O   . VAL B 1 94  ? 8.576   65.531  6.468   1.00 30.70  ? 94   VAL B O   1 
ATOM   1788 C  CB  . VAL B 1 94  ? 6.805   66.335  8.881   1.00 32.91  ? 94   VAL B CB  1 
ATOM   1789 C  CG1 . VAL B 1 94  ? 5.496   66.702  8.183   1.00 35.58  ? 94   VAL B CG1 1 
ATOM   1790 C  CG2 . VAL B 1 94  ? 6.650   66.404  10.401  1.00 35.50  ? 94   VAL B CG2 1 
ATOM   1791 N  N   . ALA B 1 95  ? 6.655   64.415  6.137   1.00 29.01  ? 95   ALA B N   1 
ATOM   1792 C  CA  . ALA B 1 95  ? 6.748   64.437  4.697   1.00 32.07  ? 95   ALA B CA  1 
ATOM   1793 C  C   . ALA B 1 95  ? 5.536   65.151  4.137   1.00 31.05  ? 95   ALA B C   1 
ATOM   1794 O  O   . ALA B 1 95  ? 4.442   64.583  4.082   1.00 28.74  ? 95   ALA B O   1 
ATOM   1795 C  CB  . ALA B 1 95  ? 6.854   63.028  4.134   1.00 25.79  ? 95   ALA B CB  1 
ATOM   1796 N  N   . ASP B 1 96  ? 5.741   66.416  3.774   1.00 27.76  ? 96   ASP B N   1 
ATOM   1797 C  CA  . ASP B 1 96  ? 4.827   67.125  2.893   1.00 31.00  ? 96   ASP B CA  1 
ATOM   1798 C  C   . ASP B 1 96  ? 4.898   66.473  1.523   1.00 33.45  ? 96   ASP B C   1 
ATOM   1799 O  O   . ASP B 1 96  ? 5.985   66.105  1.050   1.00 31.99  ? 96   ASP B O   1 
ATOM   1800 C  CB  . ASP B 1 96  ? 5.199   68.607  2.789   1.00 32.99  ? 96   ASP B CB  1 
ATOM   1801 C  CG  . ASP B 1 96  ? 4.994   69.350  4.102   1.00 40.66  ? 96   ASP B CG  1 
ATOM   1802 O  OD1 . ASP B 1 96  ? 3.977   69.090  4.795   1.00 40.42  ? 96   ASP B OD1 1 
ATOM   1803 O  OD2 . ASP B 1 96  ? 5.851   70.190  4.445   1.00 45.16  ? 96   ASP B OD2 1 
ATOM   1804 N  N   . VAL B 1 97  ? 3.740   66.290  0.901   1.00 29.85  ? 97   VAL B N   1 
ATOM   1805 C  CA  . VAL B 1 97  ? 3.704   65.640  -0.392  1.00 27.43  ? 97   VAL B CA  1 
ATOM   1806 C  C   . VAL B 1 97  ? 3.082   66.561  -1.400  1.00 32.72  ? 97   VAL B C   1 
ATOM   1807 O  O   . VAL B 1 97  ? 2.070   67.211  -1.127  1.00 30.17  ? 97   VAL B O   1 
ATOM   1808 C  CB  . VAL B 1 97  ? 2.933   64.318  -0.359  1.00 28.62  ? 97   VAL B CB  1 
ATOM   1809 C  CG1 . VAL B 1 97  ? 2.874   63.698  -1.751  1.00 29.39  ? 97   VAL B CG1 1 
ATOM   1810 C  CG2 . VAL B 1 97  ? 3.592   63.358  0.611   1.00 27.86  ? 97   VAL B CG2 1 
ATOM   1811 N  N   . SER B 1 98  ? 3.703   66.629  -2.569  1.00 31.96  ? 98   SER B N   1 
ATOM   1812 C  CA  . SER B 1 98  ? 3.139   67.406  -3.650  1.00 37.36  ? 98   SER B CA  1 
ATOM   1813 C  C   . SER B 1 98  ? 3.678   66.881  -4.965  1.00 37.85  ? 98   SER B C   1 
ATOM   1814 O  O   . SER B 1 98  ? 4.843   67.097  -5.299  1.00 36.18  ? 98   SER B O   1 
ATOM   1815 C  CB  . SER B 1 98  ? 3.460   68.887  -3.493  1.00 38.93  ? 98   SER B CB  1 
ATOM   1816 O  OG  . SER B 1 98  ? 2.681   69.629  -4.412  1.00 40.19  ? 98   SER B OG  1 
ATOM   1817 N  N   . ILE B 1 99  ? 2.806   66.194  -5.697  1.00 34.26  ? 99   ILE B N   1 
ATOM   1818 C  CA  . ILE B 1 99  ? 3.203   65.386  -6.832  1.00 34.72  ? 99   ILE B CA  1 
ATOM   1819 C  C   . ILE B 1 99  ? 2.201   65.546  -7.958  1.00 36.05  ? 99   ILE B C   1 
ATOM   1820 O  O   . ILE B 1 99  ? 1.009   65.688  -7.727  1.00 39.64  ? 99   ILE B O   1 
ATOM   1821 C  CB  . ILE B 1 99  ? 3.290   63.906  -6.428  1.00 35.14  ? 99   ILE B CB  1 
ATOM   1822 C  CG1 . ILE B 1 99  ? 4.460   63.700  -5.467  1.00 29.28  ? 99   ILE B CG1 1 
ATOM   1823 C  CG2 . ILE B 1 99  ? 3.411   62.993  -7.665  1.00 32.44  ? 99   ILE B CG2 1 
ATOM   1824 C  CD1 . ILE B 1 99  ? 4.614   62.285  -5.000  1.00 24.89  ? 99   ILE B CD1 1 
ATOM   1825 N  N   . GLU B 1 100 ? 2.692   65.554  -9.183  1.00 38.91  ? 100  GLU B N   1 
ATOM   1826 C  CA  . GLU B 1 100 ? 1.806   65.564  -10.331 1.00 36.78  ? 100  GLU B CA  1 
ATOM   1827 C  C   . GLU B 1 100 ? 2.123   64.321  -11.132 1.00 35.43  ? 100  GLU B C   1 
ATOM   1828 O  O   . GLU B 1 100 ? 3.283   63.937  -11.270 1.00 34.61  ? 100  GLU B O   1 
ATOM   1829 C  CB  . GLU B 1 100 ? 2.012   66.815  -11.169 1.00 34.87  ? 100  GLU B CB  1 
ATOM   1830 C  CG  . GLU B 1 100 ? 0.888   67.060  -12.162 1.00 45.21  ? 100  GLU B CG  1 
ATOM   1831 C  CD  . GLU B 1 100 ? 1.013   68.401  -12.870 1.00 59.64  ? 100  GLU B CD  1 
ATOM   1832 O  OE1 . GLU B 1 100 ? 2.159   68.786  -13.199 1.00 65.47  ? 100  GLU B OE1 1 
ATOM   1833 O  OE2 . GLU B 1 100 ? -0.030  69.070  -13.096 1.00 61.24  ? 100  GLU B OE2 1 
ATOM   1834 N  N   . ASP B 1 101 ? 1.096   63.649  -11.620 1.00 34.04  ? 101  ASP B N   1 
ATOM   1835 C  CA  . ASP B 1 101 ? 1.345   62.442  -12.389 1.00 34.04  ? 101  ASP B CA  1 
ATOM   1836 C  C   . ASP B 1 101 ? 0.299   62.290  -13.458 1.00 37.57  ? 101  ASP B C   1 
ATOM   1837 O  O   . ASP B 1 101 ? -0.876  62.561  -13.228 1.00 39.08  ? 101  ASP B O   1 
ATOM   1838 C  CB  . ASP B 1 101 ? 1.386   61.208  -11.509 1.00 31.60  ? 101  ASP B CB  1 
ATOM   1839 C  CG  . ASP B 1 101 ? 1.935   59.998  -12.244 1.00 36.12  ? 101  ASP B CG  1 
ATOM   1840 O  OD1 . ASP B 1 101 ? 3.150   60.001  -12.549 1.00 40.15  ? 101  ASP B OD1 1 
ATOM   1841 O  OD2 . ASP B 1 101 ? 1.161   59.048  -12.521 1.00 33.72  ? 101  ASP B OD2 1 
ATOM   1842 N  N   . SER B 1 102 ? 0.732   61.865  -14.637 1.00 35.37  ? 102  SER B N   1 
ATOM   1843 C  CA  . SER B 1 102 ? -0.162  61.833  -15.774 1.00 39.16  ? 102  SER B CA  1 
ATOM   1844 C  C   . SER B 1 102 ? -0.436  60.415  -16.203 1.00 35.59  ? 102  SER B C   1 
ATOM   1845 O  O   . SER B 1 102 ? -1.173  60.199  -17.161 1.00 39.44  ? 102  SER B O   1 
ATOM   1846 C  CB  . SER B 1 102 ? 0.425   62.635  -16.936 1.00 38.59  ? 102  SER B CB  1 
ATOM   1847 O  OG  . SER B 1 102 ? 1.829   62.463  -16.963 1.00 44.84  ? 102  SER B OG  1 
ATOM   1848 N  N   . VAL B 1 103 ? 0.153   59.455  -15.498 1.00 32.21  ? 103  VAL B N   1 
ATOM   1849 C  CA  . VAL B 1 103 ? -0.074  58.043  -15.820 1.00 35.01  ? 103  VAL B CA  1 
ATOM   1850 C  C   . VAL B 1 103 ? -1.203  57.419  -14.974 1.00 34.20  ? 103  VAL B C   1 
ATOM   1851 O  O   . VAL B 1 103 ? -2.019  56.674  -15.506 1.00 31.88  ? 103  VAL B O   1 
ATOM   1852 C  CB  . VAL B 1 103 ? 1.227   57.206  -15.713 1.00 34.14  ? 103  VAL B CB  1 
ATOM   1853 C  CG1 . VAL B 1 103 ? 0.950   55.720  -15.913 1.00 25.12  ? 103  VAL B CG1 1 
ATOM   1854 C  CG2 . VAL B 1 103 ? 2.254   57.713  -16.709 1.00 32.17  ? 103  VAL B CG2 1 
ATOM   1855 N  N   . ILE B 1 104 ? -1.245  57.708  -13.671 1.00 29.22  ? 104  ILE B N   1 
ATOM   1856 C  CA  . ILE B 1 104 ? -2.401  57.306  -12.853 1.00 29.52  ? 104  ILE B CA  1 
ATOM   1857 C  C   . ILE B 1 104 ? -3.598  58.163  -13.238 1.00 31.46  ? 104  ILE B C   1 
ATOM   1858 O  O   . ILE B 1 104 ? -3.438  59.238  -13.845 1.00 29.08  ? 104  ILE B O   1 
ATOM   1859 C  CB  . ILE B 1 104 ? -2.188  57.472  -11.319 1.00 23.57  ? 104  ILE B CB  1 
ATOM   1860 C  CG1 . ILE B 1 104 ? -1.740  58.900  -10.990 1.00 25.60  ? 104  ILE B CG1 1 
ATOM   1861 C  CG2 . ILE B 1 104 ? -1.241  56.416  -10.787 1.00 23.13  ? 104  ILE B CG2 1 
ATOM   1862 C  CD1 . ILE B 1 104 ? -1.684  59.241  -9.516  1.00 27.82  ? 104  ILE B CD1 1 
ATOM   1863 N  N   . SER B 1 105 ? -4.791  57.694  -12.881 1.00 28.31  ? 105  SER B N   1 
ATOM   1864 C  CA  . SER B 1 105 ? -5.998  58.458  -13.152 1.00 27.65  ? 105  SER B CA  1 
ATOM   1865 C  C   . SER B 1 105 ? -7.068  58.210  -12.095 1.00 26.55  ? 105  SER B C   1 
ATOM   1866 O  O   . SER B 1 105 ? -6.982  57.240  -11.358 1.00 30.51  ? 105  SER B O   1 
ATOM   1867 C  CB  . SER B 1 105 ? -6.514  58.102  -14.534 1.00 25.52  ? 105  SER B CB  1 
ATOM   1868 O  OG  . SER B 1 105 ? -7.520  59.000  -14.923 1.00 29.62  ? 105  SER B OG  1 
ATOM   1869 N  N   . LEU B 1 106 ? -8.065  59.085  -12.009 1.00 28.33  ? 106  LEU B N   1 
ATOM   1870 C  CA  . LEU B 1 106 ? -9.208  58.847  -11.128 1.00 28.90  ? 106  LEU B CA  1 
ATOM   1871 C  C   . LEU B 1 106 ? -10.422 58.304  -11.895 1.00 33.53  ? 106  LEU B C   1 
ATOM   1872 O  O   . LEU B 1 106 ? -11.532 58.213  -11.352 1.00 39.76  ? 106  LEU B O   1 
ATOM   1873 C  CB  . LEU B 1 106 ? -9.600  60.103  -10.373 1.00 27.83  ? 106  LEU B CB  1 
ATOM   1874 C  CG  . LEU B 1 106 ? -8.488  60.788  -9.590  1.00 30.10  ? 106  LEU B CG  1 
ATOM   1875 C  CD1 . LEU B 1 106 ? -9.054  62.034  -8.897  1.00 27.77  ? 106  LEU B CD1 1 
ATOM   1876 C  CD2 . LEU B 1 106 ? -7.811  59.813  -8.611  1.00 25.57  ? 106  LEU B CD2 1 
ATOM   1877 N  N   . SER B 1 107 ? -10.206 57.930  -13.149 1.00 27.12  ? 107  SER B N   1 
ATOM   1878 C  CA  . SER B 1 107 ? -11.227 57.244  -13.931 1.00 32.22  ? 107  SER B CA  1 
ATOM   1879 C  C   . SER B 1 107 ? -10.588 56.516  -15.098 1.00 31.64  ? 107  SER B C   1 
ATOM   1880 O  O   . SER B 1 107 ? -9.413  56.732  -15.398 1.00 29.04  ? 107  SER B O   1 
ATOM   1881 C  CB  . SER B 1 107 ? -12.324 58.213  -14.421 1.00 35.80  ? 107  SER B CB  1 
ATOM   1882 O  OG  . SER B 1 107 ? -11.825 59.260  -15.256 1.00 32.92  ? 107  SER B OG  1 
ATOM   1883 N  N   . GLY B 1 108 ? -11.368 55.648  -15.738 1.00 35.84  ? 108  GLY B N   1 
ATOM   1884 C  CA  . GLY B 1 108 ? -10.918 54.883  -16.888 1.00 37.59  ? 108  GLY B CA  1 
ATOM   1885 C  C   . GLY B 1 108 ? -9.976  53.726  -16.583 1.00 39.87  ? 108  GLY B C   1 
ATOM   1886 O  O   . GLY B 1 108 ? -10.049 53.100  -15.531 1.00 39.79  ? 108  GLY B O   1 
ATOM   1887 N  N   . ASP B 1 109 ? -9.075  53.447  -17.518 1.00 40.60  ? 109  ASP B N   1 
ATOM   1888 C  CA  . ASP B 1 109 ? -8.223  52.262  -17.438 1.00 43.91  ? 109  ASP B CA  1 
ATOM   1889 C  C   . ASP B 1 109 ? -7.264  52.284  -16.259 1.00 38.87  ? 109  ASP B C   1 
ATOM   1890 O  O   . ASP B 1 109 ? -6.949  51.242  -15.690 1.00 38.79  ? 109  ASP B O   1 
ATOM   1891 C  CB  . ASP B 1 109 ? -7.410  52.093  -18.732 1.00 45.45  ? 109  ASP B CB  1 
ATOM   1892 C  CG  . ASP B 1 109 ? -8.200  51.421  -19.845 1.00 57.01  ? 109  ASP B CG  1 
ATOM   1893 O  OD1 . ASP B 1 109 ? -9.369  51.022  -19.603 1.00 57.34  ? 109  ASP B OD1 1 
ATOM   1894 O  OD2 . ASP B 1 109 ? -7.643  51.289  -20.964 1.00 58.71  ? 109  ASP B OD2 1 
ATOM   1895 N  N   . HIS B 1 110 ? -6.773  53.473  -15.933 1.00 34.47  ? 110  HIS B N   1 
ATOM   1896 C  CA  . HIS B 1 110 ? -5.753  53.642  -14.902 1.00 36.67  ? 110  HIS B CA  1 
ATOM   1897 C  C   . HIS B 1 110 ? -6.309  54.164  -13.586 1.00 30.58  ? 110  HIS B C   1 
ATOM   1898 O  O   . HIS B 1 110 ? -5.566  54.673  -12.757 1.00 28.32  ? 110  HIS B O   1 
ATOM   1899 C  CB  . HIS B 1 110 ? -4.653  54.583  -15.398 1.00 30.55  ? 110  HIS B CB  1 
ATOM   1900 C  CG  . HIS B 1 110 ? -3.839  54.004  -16.508 1.00 39.78  ? 110  HIS B CG  1 
ATOM   1901 N  ND1 . HIS B 1 110 ? -2.696  54.604  -16.988 1.00 35.84  ? 110  HIS B ND1 1 
ATOM   1902 C  CD2 . HIS B 1 110 ? -4.006  52.869  -17.232 1.00 38.13  ? 110  HIS B CD2 1 
ATOM   1903 C  CE1 . HIS B 1 110 ? -2.199  53.868  -17.967 1.00 39.56  ? 110  HIS B CE1 1 
ATOM   1904 N  NE2 . HIS B 1 110 ? -2.973  52.809  -18.133 1.00 35.27  ? 110  HIS B NE2 1 
ATOM   1905 N  N   . CYS B 1 111 ? -7.620  54.056  -13.422 1.00 31.61  ? 111  CYS B N   1 
ATOM   1906 C  CA  . CYS B 1 111 ? -8.276  54.478  -12.193 1.00 30.74  ? 111  CYS B CA  1 
ATOM   1907 C  C   . CYS B 1 111 ? -7.655  53.809  -10.958 1.00 25.73  ? 111  CYS B C   1 
ATOM   1908 O  O   . CYS B 1 111 ? -7.535  52.591  -10.878 1.00 26.99  ? 111  CYS B O   1 
ATOM   1909 C  CB  . CYS B 1 111 ? -9.766  54.183  -12.274 1.00 30.39  ? 111  CYS B CB  1 
ATOM   1910 S  SG  . CYS B 1 111 ? -10.695 54.936  -10.956 1.00 39.79  ? 111  CYS B SG  1 
ATOM   1911 N  N   . ILE B 1 112 ? -7.248  54.618  -9.997  1.00 26.18  ? 112  ILE B N   1 
ATOM   1912 C  CA  . ILE B 1 112 ? -6.645  54.097  -8.785  1.00 26.85  ? 112  ILE B CA  1 
ATOM   1913 C  C   . ILE B 1 112 ? -7.638  54.118  -7.631  1.00 29.68  ? 112  ILE B C   1 
ATOM   1914 O  O   . ILE B 1 112 ? -7.281  53.776  -6.488  1.00 31.70  ? 112  ILE B O   1 
ATOM   1915 C  CB  . ILE B 1 112 ? -5.431  54.917  -8.394  1.00 25.65  ? 112  ILE B CB  1 
ATOM   1916 C  CG1 . ILE B 1 112 ? -5.864  56.357  -8.154  1.00 24.50  ? 112  ILE B CG1 1 
ATOM   1917 C  CG2 . ILE B 1 112 ? -4.356  54.827  -9.498  1.00 23.05  ? 112  ILE B CG2 1 
ATOM   1918 C  CD1 . ILE B 1 112 ? -4.781  57.194  -7.574  1.00 31.77  ? 112  ILE B CD1 1 
ATOM   1919 N  N   . ILE B 1 113 ? -8.881  54.513  -7.923  1.00 28.43  ? 113  ILE B N   1 
ATOM   1920 C  CA  . ILE B 1 113 ? -9.916  54.550  -6.893  1.00 27.85  ? 113  ILE B CA  1 
ATOM   1921 C  C   . ILE B 1 113 ? -10.296 53.129  -6.523  1.00 29.41  ? 113  ILE B C   1 
ATOM   1922 O  O   . ILE B 1 113 ? -10.533 52.301  -7.392  1.00 31.73  ? 113  ILE B O   1 
ATOM   1923 C  CB  . ILE B 1 113 ? -11.147 55.365  -7.334  1.00 32.65  ? 113  ILE B CB  1 
ATOM   1924 C  CG1 . ILE B 1 113 ? -10.708 56.804  -7.645  1.00 32.58  ? 113  ILE B CG1 1 
ATOM   1925 C  CG2 . ILE B 1 113 ? -12.244 55.315  -6.254  1.00 29.74  ? 113  ILE B CG2 1 
ATOM   1926 C  CD1 . ILE B 1 113 ? -11.686 57.878  -7.274  1.00 30.88  ? 113  ILE B CD1 1 
ATOM   1927 N  N   . GLY B 1 114 ? -10.305 52.834  -5.227  1.00 24.98  ? 114  GLY B N   1 
ATOM   1928 C  CA  . GLY B 1 114 ? -10.593 51.497  -4.763  1.00 22.71  ? 114  GLY B CA  1 
ATOM   1929 C  C   . GLY B 1 114 ? -9.340  50.660  -4.651  1.00 26.73  ? 114  GLY B C   1 
ATOM   1930 O  O   . GLY B 1 114 ? -9.415  49.463  -4.375  1.00 25.65  ? 114  GLY B O   1 
ATOM   1931 N  N   . ARG B 1 115 ? -8.182  51.281  -4.862  1.00 25.24  ? 115  ARG B N   1 
ATOM   1932 C  CA  . ARG B 1 115 ? -6.914  50.571  -4.732  1.00 26.56  ? 115  ARG B CA  1 
ATOM   1933 C  C   . ARG B 1 115 ? -6.206  51.156  -3.530  1.00 28.17  ? 115  ARG B C   1 
ATOM   1934 O  O   . ARG B 1 115 ? -6.788  51.973  -2.822  1.00 32.67  ? 115  ARG B O   1 
ATOM   1935 C  CB  . ARG B 1 115 ? -6.072  50.697  -6.013  1.00 25.37  ? 115  ARG B CB  1 
ATOM   1936 C  CG  . ARG B 1 115 ? -6.866  50.422  -7.287  1.00 24.17  ? 115  ARG B CG  1 
ATOM   1937 C  CD  . ARG B 1 115 ? -5.968  50.086  -8.483  1.00 25.48  ? 115  ARG B CD  1 
ATOM   1938 N  NE  . ARG B 1 115 ? -6.757  49.906  -9.698  1.00 23.53  ? 115  ARG B NE  1 
ATOM   1939 C  CZ  . ARG B 1 115 ? -7.207  48.735  -10.149 1.00 25.25  ? 115  ARG B CZ  1 
ATOM   1940 N  NH1 . ARG B 1 115 ? -6.944  47.608  -9.504  1.00 22.19  ? 115  ARG B NH1 1 
ATOM   1941 N  NH2 . ARG B 1 115 ? -7.919  48.689  -11.269 1.00 28.16  ? 115  ARG B NH2 1 
ATOM   1942 N  N   . THR B 1 116 ? -4.957  50.778  -3.299  1.00 26.07  ? 116  THR B N   1 
ATOM   1943 C  CA  . THR B 1 116 ? -4.303  51.152  -2.050  1.00 28.16  ? 116  THR B CA  1 
ATOM   1944 C  C   . THR B 1 116 ? -3.033  51.965  -2.251  1.00 31.22  ? 116  THR B C   1 
ATOM   1945 O  O   . THR B 1 116 ? -2.186  51.625  -3.075  1.00 31.38  ? 116  THR B O   1 
ATOM   1946 C  CB  . THR B 1 116 ? -3.969  49.906  -1.207  1.00 30.13  ? 116  THR B CB  1 
ATOM   1947 O  OG1 . THR B 1 116 ? -5.173  49.165  -0.958  1.00 29.79  ? 116  THR B OG1 1 
ATOM   1948 C  CG2 . THR B 1 116 ? -3.297  50.302  0.112   1.00 27.13  ? 116  THR B CG2 1 
ATOM   1949 N  N   . LEU B 1 117 ? -2.913  53.047  -1.496  1.00 26.81  ? 117  LEU B N   1 
ATOM   1950 C  CA  . LEU B 1 117 ? -1.701  53.840  -1.498  1.00 28.10  ? 117  LEU B CA  1 
ATOM   1951 C  C   . LEU B 1 117 ? -0.851  53.329  -0.356  1.00 29.02  ? 117  LEU B C   1 
ATOM   1952 O  O   . LEU B 1 117 ? -1.356  53.116  0.743   1.00 27.95  ? 117  LEU B O   1 
ATOM   1953 C  CB  . LEU B 1 117 ? -2.031  55.307  -1.261  1.00 28.80  ? 117  LEU B CB  1 
ATOM   1954 C  CG  . LEU B 1 117 ? -0.866  56.278  -1.328  1.00 30.96  ? 117  LEU B CG  1 
ATOM   1955 C  CD1 . LEU B 1 117 ? -0.274  56.312  -2.763  1.00 29.17  ? 117  LEU B CD1 1 
ATOM   1956 C  CD2 . LEU B 1 117 ? -1.383  57.631  -0.936  1.00 28.03  ? 117  LEU B CD2 1 
ATOM   1957 N  N   . VAL B 1 118 ? 0.429   53.116  -0.612  1.00 24.23  ? 118  VAL B N   1 
ATOM   1958 C  CA  . VAL B 1 118 ? 1.314   52.604  0.404   1.00 22.33  ? 118  VAL B CA  1 
ATOM   1959 C  C   . VAL B 1 118 ? 2.558   53.472  0.503   1.00 27.62  ? 118  VAL B C   1 
ATOM   1960 O  O   . VAL B 1 118 ? 3.154   53.827  -0.513  1.00 25.98  ? 118  VAL B O   1 
ATOM   1961 C  CB  . VAL B 1 118 ? 1.756   51.172  0.070   1.00 26.33  ? 118  VAL B CB  1 
ATOM   1962 C  CG1 . VAL B 1 118 ? 2.820   50.679  1.057   1.00 24.14  ? 118  VAL B CG1 1 
ATOM   1963 C  CG2 . VAL B 1 118 ? 0.555   50.228  0.006   1.00 26.79  ? 118  VAL B CG2 1 
ATOM   1964 N  N   . VAL B 1 119 ? 2.949   53.824  1.728   1.00 27.50  ? 119  VAL B N   1 
ATOM   1965 C  CA  . VAL B 1 119 ? 4.262   54.407  1.945   1.00 25.10  ? 119  VAL B CA  1 
ATOM   1966 C  C   . VAL B 1 119 ? 5.191   53.339  2.530   1.00 28.80  ? 119  VAL B C   1 
ATOM   1967 O  O   . VAL B 1 119 ? 4.772   52.514  3.350   1.00 30.99  ? 119  VAL B O   1 
ATOM   1968 C  CB  . VAL B 1 119 ? 4.222   55.660  2.827   1.00 28.61  ? 119  VAL B CB  1 
ATOM   1969 C  CG1 . VAL B 1 119 ? 3.559   55.356  4.197   1.00 28.49  ? 119  VAL B CG1 1 
ATOM   1970 C  CG2 . VAL B 1 119 ? 5.639   56.203  2.997   1.00 25.67  ? 119  VAL B CG2 1 
ATOM   1971 N  N   . HIS B 1 120 ? 6.446   53.356  2.102   1.00 28.31  ? 120  HIS B N   1 
ATOM   1972 C  CA  . HIS B 1 120 ? 7.357   52.235  2.327   1.00 30.60  ? 120  HIS B CA  1 
ATOM   1973 C  C   . HIS B 1 120 ? 8.497   52.515  3.317   1.00 30.96  ? 120  HIS B C   1 
ATOM   1974 O  O   . HIS B 1 120 ? 8.834   53.669  3.592   1.00 28.49  ? 120  HIS B O   1 
ATOM   1975 C  CB  . HIS B 1 120 ? 7.930   51.752  0.976   1.00 27.91  ? 120  HIS B CB  1 
ATOM   1976 C  CG  . HIS B 1 120 ? 7.001   50.856  0.217   1.00 26.75  ? 120  HIS B CG  1 
ATOM   1977 N  ND1 . HIS B 1 120 ? 6.938   49.496  0.430   1.00 27.28  ? 120  HIS B ND1 1 
ATOM   1978 C  CD2 . HIS B 1 120 ? 6.074   51.130  -0.731  1.00 25.62  ? 120  HIS B CD2 1 
ATOM   1979 C  CE1 . HIS B 1 120 ? 6.019   48.970  -0.361  1.00 28.80  ? 120  HIS B CE1 1 
ATOM   1980 N  NE2 . HIS B 1 120 ? 5.485   49.940  -1.082  1.00 23.02  ? 120  HIS B NE2 1 
ATOM   1981 N  N   . GLU B 1 121 ? 9.104   51.438  3.822   1.00 32.84  ? 121  GLU B N   1 
ATOM   1982 C  CA  . GLU B 1 121 ? 10.235  51.524  4.750   1.00 34.16  ? 121  GLU B CA  1 
ATOM   1983 C  C   . GLU B 1 121 ? 11.463  52.218  4.151   1.00 34.78  ? 121  GLU B C   1 
ATOM   1984 O  O   . GLU B 1 121 ? 12.041  53.118  4.763   1.00 30.13  ? 121  GLU B O   1 
ATOM   1985 C  CB  . GLU B 1 121 ? 10.629  50.125  5.227   1.00 38.23  ? 121  GLU B CB  1 
ATOM   1986 C  CG  . GLU B 1 121 ? 11.812  50.100  6.209   1.00 38.07  ? 121  GLU B CG  1 
ATOM   1987 C  CD  . GLU B 1 121 ? 12.467  48.718  6.318   1.00 41.88  ? 121  GLU B CD  1 
ATOM   1988 O  OE1 . GLU B 1 121 ? 12.107  47.814  5.522   1.00 36.98  ? 121  GLU B OE1 1 
ATOM   1989 O  OE2 . GLU B 1 121 ? 13.362  48.545  7.185   1.00 47.11  ? 121  GLU B OE2 1 
ATOM   1990 N  N   . LYS B 1 122 ? 11.845  51.797  2.951   1.00 32.82  ? 122  LYS B N   1 
ATOM   1991 C  CA  . LYS B 1 122 ? 13.078  52.261  2.314   1.00 36.03  ? 122  LYS B CA  1 
ATOM   1992 C  C   . LYS B 1 122 ? 12.792  53.070  1.042   1.00 36.94  ? 122  LYS B C   1 
ATOM   1993 O  O   . LYS B 1 122 ? 11.715  52.943  0.444   1.00 34.81  ? 122  LYS B O   1 
ATOM   1994 C  CB  . LYS B 1 122 ? 13.984  51.055  1.975   1.00 32.76  ? 122  LYS B CB  1 
ATOM   1995 C  CG  . LYS B 1 122 ? 14.490  50.252  3.194   1.00 37.86  ? 122  LYS B CG  1 
ATOM   1996 C  CD  . LYS B 1 122 ? 15.282  48.991  2.790   1.00 46.17  ? 122  LYS B CD  1 
ATOM   1997 C  CE  . LYS B 1 122 ? 14.417  48.019  1.959   1.00 47.08  ? 122  LYS B CE  1 
ATOM   1998 N  NZ  . LYS B 1 122 ? 15.101  46.798  1.386   1.00 43.55  ? 122  LYS B NZ  1 
ATOM   1999 N  N   . ALA B 1 123 ? 13.760  53.886  0.621   1.00 33.10  ? 123  ALA B N   1 
ATOM   2000 C  CA  . ALA B 1 123 ? 13.652  54.607  -0.642  1.00 31.35  ? 123  ALA B CA  1 
ATOM   2001 C  C   . ALA B 1 123 ? 13.418  53.649  -1.804  1.00 30.20  ? 123  ALA B C   1 
ATOM   2002 O  O   . ALA B 1 123 ? 13.978  52.559  -1.848  1.00 34.60  ? 123  ALA B O   1 
ATOM   2003 C  CB  . ALA B 1 123 ? 14.901  55.421  -0.895  1.00 30.98  ? 123  ALA B CB  1 
ATOM   2004 N  N   . ASP B 1 124 ? 12.578  54.053  -2.741  1.00 31.00  ? 124  ASP B N   1 
ATOM   2005 C  CA  . ASP B 1 124 ? 12.419  53.322  -3.990  1.00 30.77  ? 124  ASP B CA  1 
ATOM   2006 C  C   . ASP B 1 124 ? 13.612  53.647  -4.890  1.00 29.77  ? 124  ASP B C   1 
ATOM   2007 O  O   . ASP B 1 124 ? 13.903  54.811  -5.108  1.00 31.29  ? 124  ASP B O   1 
ATOM   2008 C  CB  . ASP B 1 124 ? 11.144  53.799  -4.665  1.00 32.25  ? 124  ASP B CB  1 
ATOM   2009 C  CG  . ASP B 1 124 ? 10.898  53.137  -6.017  1.00 35.51  ? 124  ASP B CG  1 
ATOM   2010 O  OD1 . ASP B 1 124 ? 11.761  52.340  -6.472  1.00 35.33  ? 124  ASP B OD1 1 
ATOM   2011 O  OD2 . ASP B 1 124 ? 9.830   53.430  -6.612  1.00 33.98  ? 124  ASP B OD2 1 
ATOM   2012 N  N   . ASP B 1 125 ? 14.296  52.643  -5.423  1.00 26.31  ? 125  ASP B N   1 
ATOM   2013 C  CA  . ASP B 1 125 ? 15.513  52.929  -6.192  1.00 31.27  ? 125  ASP B CA  1 
ATOM   2014 C  C   . ASP B 1 125 ? 15.262  53.245  -7.679  1.00 31.82  ? 125  ASP B C   1 
ATOM   2015 O  O   . ASP B 1 125 ? 16.203  53.489  -8.430  1.00 30.64  ? 125  ASP B O   1 
ATOM   2016 C  CB  . ASP B 1 125 ? 16.555  51.812  -6.039  1.00 26.80  ? 125  ASP B CB  1 
ATOM   2017 C  CG  . ASP B 1 125 ? 16.096  50.477  -6.618  1.00 27.35  ? 125  ASP B CG  1 
ATOM   2018 O  OD1 . ASP B 1 125 ? 15.171  50.448  -7.470  1.00 30.35  ? 125  ASP B OD1 1 
ATOM   2019 O  OD2 . ASP B 1 125 ? 16.685  49.445  -6.231  1.00 27.59  ? 125  ASP B OD2 1 
ATOM   2020 N  N   . LEU B 1 126 ? 13.992  53.211  -8.083  1.00 31.63  ? 126  LEU B N   1 
ATOM   2021 C  CA  . LEU B 1 126 ? 13.568  53.607  -9.424  1.00 29.90  ? 126  LEU B CA  1 
ATOM   2022 C  C   . LEU B 1 126 ? 14.031  52.627  -10.508 1.00 32.15  ? 126  LEU B C   1 
ATOM   2023 O  O   . LEU B 1 126 ? 14.230  53.014  -11.656 1.00 33.24  ? 126  LEU B O   1 
ATOM   2024 C  CB  . LEU B 1 126 ? 14.020  55.045  -9.739  1.00 23.42  ? 126  LEU B CB  1 
ATOM   2025 C  CG  . LEU B 1 126 ? 13.780  56.081  -8.626  1.00 27.85  ? 126  LEU B CG  1 
ATOM   2026 C  CD1 . LEU B 1 126 ? 14.357  57.467  -8.980  1.00 21.11  ? 126  LEU B CD1 1 
ATOM   2027 C  CD2 . LEU B 1 126 ? 12.293  56.180  -8.267  1.00 25.69  ? 126  LEU B CD2 1 
ATOM   2028 N  N   . GLY B 1 127 ? 14.189  51.357  -10.144 1.00 30.72  ? 127  GLY B N   1 
ATOM   2029 C  CA  . GLY B 1 127 ? 14.623  50.346  -11.098 1.00 31.28  ? 127  GLY B CA  1 
ATOM   2030 C  C   . GLY B 1 127 ? 16.136  50.231  -11.332 1.00 32.01  ? 127  GLY B C   1 
ATOM   2031 O  O   . GLY B 1 127 ? 16.577  49.447  -12.166 1.00 33.88  ? 127  GLY B O   1 
ATOM   2032 N  N   . LYS B 1 128 ? 16.939  50.979  -10.579 1.00 34.00  ? 128  LYS B N   1 
ATOM   2033 C  CA  . LYS B 1 128 ? 18.393  51.013  -10.796 1.00 33.37  ? 128  LYS B CA  1 
ATOM   2034 C  C   . LYS B 1 128 ? 19.240  50.298  -9.721  1.00 28.85  ? 128  LYS B C   1 
ATOM   2035 O  O   . LYS B 1 128 ? 20.423  50.597  -9.556  1.00 29.78  ? 128  LYS B O   1 
ATOM   2036 C  CB  . LYS B 1 128 ? 18.834  52.475  -10.927 1.00 31.74  ? 128  LYS B CB  1 
ATOM   2037 C  CG  . LYS B 1 128 ? 17.930  53.261  -11.873 1.00 34.92  ? 128  LYS B CG  1 
ATOM   2038 C  CD  . LYS B 1 128 ? 18.112  54.755  -11.710 1.00 45.55  ? 128  LYS B CD  1 
ATOM   2039 C  CE  . LYS B 1 128 ? 19.185  55.297  -12.652 1.00 51.16  ? 128  LYS B CE  1 
ATOM   2040 N  NZ  . LYS B 1 128 ? 19.622  56.672  -12.250 1.00 52.42  ? 128  LYS B NZ  1 
ATOM   2041 N  N   . GLY B 1 129 ? 18.634  49.372  -8.988  1.00 27.61  ? 129  GLY B N   1 
ATOM   2042 C  CA  . GLY B 1 129 ? 19.321  48.664  -7.916  1.00 30.90  ? 129  GLY B CA  1 
ATOM   2043 C  C   . GLY B 1 129 ? 20.088  47.416  -8.350  1.00 31.56  ? 129  GLY B C   1 
ATOM   2044 O  O   . GLY B 1 129 ? 20.827  46.823  -7.564  1.00 29.68  ? 129  GLY B O   1 
ATOM   2045 N  N   . GLY B 1 130 ? 19.901  47.005  -9.597  1.00 28.38  ? 130  GLY B N   1 
ATOM   2046 C  CA  . GLY B 1 130 ? 20.726  45.966  -10.187 1.00 32.30  ? 130  GLY B CA  1 
ATOM   2047 C  C   . GLY B 1 130 ? 20.502  44.554  -9.690  1.00 33.50  ? 130  GLY B C   1 
ATOM   2048 O  O   . GLY B 1 130 ? 21.293  43.670  -9.976  1.00 36.33  ? 130  GLY B O   1 
ATOM   2049 N  N   . ASN B 1 131 ? 19.445  44.337  -8.918  1.00 35.27  ? 131  ASN B N   1 
ATOM   2050 C  CA  . ASN B 1 131 ? 19.042  42.982  -8.551  1.00 33.39  ? 131  ASN B CA  1 
ATOM   2051 C  C   . ASN B 1 131 ? 17.614  42.764  -9.012  1.00 35.26  ? 131  ASN B C   1 
ATOM   2052 O  O   . ASN B 1 131 ? 16.962  43.695  -9.463  1.00 33.42  ? 131  ASN B O   1 
ATOM   2053 C  CB  . ASN B 1 131 ? 19.142  42.749  -7.049  1.00 30.44  ? 131  ASN B CB  1 
ATOM   2054 C  CG  . ASN B 1 131 ? 18.161  43.597  -6.266  1.00 34.10  ? 131  ASN B CG  1 
ATOM   2055 O  OD1 . ASN B 1 131 ? 17.548  44.514  -6.808  1.00 34.07  ? 131  ASN B OD1 1 
ATOM   2056 N  ND2 . ASN B 1 131 ? 18.015  43.302  -4.994  1.00 30.91  ? 131  ASN B ND2 1 
ATOM   2057 N  N   . GLU B 1 132 ? 17.138  41.534  -8.894  1.00 36.75  ? 132  GLU B N   1 
ATOM   2058 C  CA  . GLU B 1 132 ? 15.819  41.170  -9.382  1.00 41.95  ? 132  GLU B CA  1 
ATOM   2059 C  C   . GLU B 1 132 ? 14.691  42.050  -8.795  1.00 43.25  ? 132  GLU B C   1 
ATOM   2060 O  O   . GLU B 1 132 ? 13.745  42.424  -9.493  1.00 40.94  ? 132  GLU B O   1 
ATOM   2061 C  CB  . GLU B 1 132 ? 15.579  39.697  -9.065  1.00 44.33  ? 132  GLU B CB  1 
ATOM   2062 C  CG  . GLU B 1 132 ? 15.389  38.822  -10.291 1.00 52.44  ? 132  GLU B CG  1 
ATOM   2063 C  CD  . GLU B 1 132 ? 14.056  39.080  -11.002 1.00 69.14  ? 132  GLU B CD  1 
ATOM   2064 O  OE1 . GLU B 1 132 ? 13.448  38.095  -11.499 1.00 69.84  ? 132  GLU B OE1 1 
ATOM   2065 O  OE2 . GLU B 1 132 ? 13.608  40.260  -11.052 1.00 65.02  ? 132  GLU B OE2 1 
ATOM   2066 N  N   . GLU B 1 133 ? 14.822  42.392  -7.515  1.00 36.90  ? 133  GLU B N   1 
ATOM   2067 C  CA  . GLU B 1 133 ? 13.787  43.096  -6.778  1.00 34.11  ? 133  GLU B CA  1 
ATOM   2068 C  C   . GLU B 1 133 ? 13.599  44.536  -7.252  1.00 38.29  ? 133  GLU B C   1 
ATOM   2069 O  O   . GLU B 1 133 ? 12.481  45.043  -7.318  1.00 37.71  ? 133  GLU B O   1 
ATOM   2070 C  CB  . GLU B 1 133 ? 14.135  43.072  -5.297  1.00 36.00  ? 133  GLU B CB  1 
ATOM   2071 C  CG  . GLU B 1 133 ? 13.004  43.452  -4.375  1.00 38.35  ? 133  GLU B CG  1 
ATOM   2072 C  CD  . GLU B 1 133 ? 11.812  42.506  -4.457  1.00 42.45  ? 133  GLU B CD  1 
ATOM   2073 O  OE1 . GLU B 1 133 ? 11.992  41.265  -4.530  1.00 46.45  ? 133  GLU B OE1 1 
ATOM   2074 O  OE2 . GLU B 1 133 ? 10.677  43.017  -4.444  1.00 47.54  ? 133  GLU B OE2 1 
ATOM   2075 N  N   . SER B 1 134 ? 14.698  45.201  -7.584  1.00 39.70  ? 134  SER B N   1 
ATOM   2076 C  CA  . SER B 1 134 ? 14.627  46.567  -8.083  1.00 37.57  ? 134  SER B CA  1 
ATOM   2077 C  C   . SER B 1 134 ? 13.603  46.626  -9.209  1.00 38.31  ? 134  SER B C   1 
ATOM   2078 O  O   . SER B 1 134 ? 12.827  47.580  -9.335  1.00 35.18  ? 134  SER B O   1 
ATOM   2079 C  CB  . SER B 1 134 ? 15.995  47.019  -8.603  1.00 34.11  ? 134  SER B CB  1 
ATOM   2080 O  OG  . SER B 1 134 ? 15.936  48.354  -9.094  1.00 30.62  ? 134  SER B OG  1 
ATOM   2081 N  N   . THR B 1 135 ? 13.619  45.588  -10.030 1.00 35.43  ? 135  THR B N   1 
ATOM   2082 C  CA  . THR B 1 135 ? 12.725  45.511  -11.170 1.00 42.71  ? 135  THR B CA  1 
ATOM   2083 C  C   . THR B 1 135 ? 11.240  45.318  -10.786 1.00 41.91  ? 135  THR B C   1 
ATOM   2084 O  O   . THR B 1 135 ? 10.337  45.701  -11.532 1.00 40.75  ? 135  THR B O   1 
ATOM   2085 C  CB  . THR B 1 135 ? 13.194  44.396  -12.115 1.00 43.11  ? 135  THR B CB  1 
ATOM   2086 O  OG1 . THR B 1 135 ? 13.415  44.955  -13.415 1.00 49.42  ? 135  THR B OG1 1 
ATOM   2087 C  CG2 . THR B 1 135 ? 12.176  43.254  -12.182 1.00 41.20  ? 135  THR B CG2 1 
ATOM   2088 N  N   . LYS B 1 136 ? 11.000  44.721  -9.622  1.00 40.13  ? 136  LYS B N   1 
ATOM   2089 C  CA  . LYS B 1 136 ? 9.642   44.451  -9.160  1.00 41.20  ? 136  LYS B CA  1 
ATOM   2090 C  C   . LYS B 1 136 ? 9.141   45.575  -8.264  1.00 37.89  ? 136  LYS B C   1 
ATOM   2091 O  O   . LYS B 1 136 ? 8.016   46.053  -8.411  1.00 40.16  ? 136  LYS B O   1 
ATOM   2092 C  CB  . LYS B 1 136 ? 9.599   43.147  -8.370  1.00 40.67  ? 136  LYS B CB  1 
ATOM   2093 C  CG  . LYS B 1 136 ? 10.008  41.925  -9.142  1.00 43.35  ? 136  LYS B CG  1 
ATOM   2094 C  CD  . LYS B 1 136 ? 10.221  40.740  -8.190  1.00 46.26  ? 136  LYS B CD  1 
ATOM   2095 C  CE  . LYS B 1 136 ? 10.643  39.482  -8.961  1.00 51.54  ? 136  LYS B CE  1 
ATOM   2096 N  NZ  . LYS B 1 136 ? 11.122  38.400  -8.047  1.00 57.53  ? 136  LYS B NZ  1 
ATOM   2097 N  N   . THR B 1 137 ? 10.031  46.045  -7.399  1.00 39.64  ? 137  THR B N   1 
ATOM   2098 C  CA  . THR B 1 137 ? 9.655   46.709  -6.174  1.00 33.84  ? 137  THR B CA  1 
ATOM   2099 C  C   . THR B 1 137 ? 10.499  47.950  -5.820  1.00 37.29  ? 137  THR B C   1 
ATOM   2100 O  O   . THR B 1 137 ? 10.199  48.668  -4.854  1.00 34.65  ? 137  THR B O   1 
ATOM   2101 C  CB  . THR B 1 137 ? 9.764   45.655  -5.072  1.00 35.91  ? 137  THR B CB  1 
ATOM   2102 O  OG1 . THR B 1 137 ? 8.460   45.350  -4.566  1.00 34.85  ? 137  THR B OG1 1 
ATOM   2103 C  CG2 . THR B 1 137 ? 10.721  46.071  -3.981  1.00 32.62  ? 137  THR B CG2 1 
ATOM   2104 N  N   . GLY B 1 138 ? 11.549  48.218  -6.595  1.00 34.88  ? 138  GLY B N   1 
ATOM   2105 C  CA  . GLY B 1 138 ? 12.456  49.310  -6.266  1.00 30.35  ? 138  GLY B CA  1 
ATOM   2106 C  C   . GLY B 1 138 ? 13.216  49.107  -4.956  1.00 28.66  ? 138  GLY B C   1 
ATOM   2107 O  O   . GLY B 1 138 ? 13.845  50.032  -4.433  1.00 29.48  ? 138  GLY B O   1 
ATOM   2108 N  N   . ASN B 1 139 ? 13.143  47.897  -4.412  1.00 28.80  ? 139  ASN B N   1 
ATOM   2109 C  CA  . ASN B 1 139 ? 13.792  47.582  -3.142  1.00 32.46  ? 139  ASN B CA  1 
ATOM   2110 C  C   . ASN B 1 139 ? 13.317  48.436  -1.961  1.00 32.92  ? 139  ASN B C   1 
ATOM   2111 O  O   . ASN B 1 139 ? 14.036  48.577  -0.984  1.00 32.97  ? 139  ASN B O   1 
ATOM   2112 C  CB  . ASN B 1 139 ? 15.326  47.674  -3.285  1.00 28.70  ? 139  ASN B CB  1 
ATOM   2113 C  CG  . ASN B 1 139 ? 15.899  46.558  -4.149  1.00 32.25  ? 139  ASN B CG  1 
ATOM   2114 O  OD1 . ASN B 1 139 ? 16.390  46.806  -5.251  1.00 36.50  ? 139  ASN B OD1 1 
ATOM   2115 N  ND2 . ASN B 1 139 ? 15.794  45.324  -3.676  1.00 28.30  ? 139  ASN B ND2 1 
ATOM   2116 N  N   . ALA B 1 140 ? 12.115  49.005  -2.052  1.00 33.49  ? 140  ALA B N   1 
ATOM   2117 C  CA  . ALA B 1 140 ? 11.626  49.962  -1.046  1.00 30.80  ? 140  ALA B CA  1 
ATOM   2118 C  C   . ALA B 1 140 ? 11.270  49.322  0.299   1.00 33.67  ? 140  ALA B C   1 
ATOM   2119 O  O   . ALA B 1 140 ? 10.970  50.020  1.273   1.00 31.65  ? 140  ALA B O   1 
ATOM   2120 C  CB  . ALA B 1 140 ? 10.437  50.740  -1.588  1.00 29.01  ? 140  ALA B CB  1 
ATOM   2121 N  N   . GLY B 1 141 ? 11.297  47.996  0.339   1.00 30.67  ? 141  GLY B N   1 
ATOM   2122 C  CA  . GLY B 1 141 ? 11.095  47.270  1.576   1.00 37.75  ? 141  GLY B CA  1 
ATOM   2123 C  C   . GLY B 1 141 ? 9.681   47.210  2.125   1.00 34.81  ? 141  GLY B C   1 
ATOM   2124 O  O   . GLY B 1 141 ? 8.696   47.199  1.388   1.00 33.84  ? 141  GLY B O   1 
ATOM   2125 N  N   . SER B 1 142 ? 9.585   47.185  3.444   1.00 32.41  ? 142  SER B N   1 
ATOM   2126 C  CA  . SER B 1 142 ? 8.318   46.897  4.093   1.00 34.30  ? 142  SER B CA  1 
ATOM   2127 C  C   . SER B 1 142 ? 7.282   48.015  3.905   1.00 34.12  ? 142  SER B C   1 
ATOM   2128 O  O   . SER B 1 142 ? 7.625   49.196  3.751   1.00 35.22  ? 142  SER B O   1 
ATOM   2129 C  CB  . SER B 1 142 ? 8.538   46.623  5.583   1.00 29.37  ? 142  SER B CB  1 
ATOM   2130 O  OG  . SER B 1 142 ? 8.797   47.839  6.264   1.00 33.92  ? 142  SER B OG  1 
ATOM   2131 N  N   . ARG B 1 143 ? 6.013   47.620  3.927   1.00 32.43  ? 143  ARG B N   1 
ATOM   2132 C  CA  . ARG B 1 143 ? 4.898   48.549  3.817   1.00 31.57  ? 143  ARG B CA  1 
ATOM   2133 C  C   . ARG B 1 143 ? 4.575   49.122  5.191   1.00 32.12  ? 143  ARG B C   1 
ATOM   2134 O  O   . ARG B 1 143 ? 4.075   48.409  6.058   1.00 32.67  ? 143  ARG B O   1 
ATOM   2135 C  CB  . ARG B 1 143 ? 3.691   47.837  3.217   1.00 28.51  ? 143  ARG B CB  1 
ATOM   2136 C  CG  . ARG B 1 143 ? 4.077   46.882  2.111   1.00 25.07  ? 143  ARG B CG  1 
ATOM   2137 C  CD  . ARG B 1 143 ? 2.899   46.233  1.437   1.00 26.40  ? 143  ARG B CD  1 
ATOM   2138 N  NE  . ARG B 1 143 ? 3.332   45.501  0.239   1.00 32.12  ? 143  ARG B NE  1 
ATOM   2139 C  CZ  . ARG B 1 143 ? 2.514   44.962  -0.663  1.00 31.55  ? 143  ARG B CZ  1 
ATOM   2140 N  NH1 . ARG B 1 143 ? 1.197   45.079  -0.540  1.00 30.71  ? 143  ARG B NH1 1 
ATOM   2141 N  NH2 . ARG B 1 143 ? 3.016   44.315  -1.704  1.00 31.40  ? 143  ARG B NH2 1 
ATOM   2142 N  N   . LEU B 1 144 ? 4.880   50.409  5.372   1.00 31.44  ? 144  LEU B N   1 
ATOM   2143 C  CA  . LEU B 1 144 ? 4.802   51.096  6.661   1.00 33.38  ? 144  LEU B CA  1 
ATOM   2144 C  C   . LEU B 1 144 ? 3.403   51.603  6.988   1.00 37.82  ? 144  LEU B C   1 
ATOM   2145 O  O   . LEU B 1 144 ? 3.067   51.815  8.155   1.00 35.55  ? 144  LEU B O   1 
ATOM   2146 C  CB  . LEU B 1 144 ? 5.733   52.306  6.653   1.00 33.74  ? 144  LEU B CB  1 
ATOM   2147 C  CG  . LEU B 1 144 ? 7.053   52.349  7.417   1.00 35.97  ? 144  LEU B CG  1 
ATOM   2148 C  CD1 . LEU B 1 144 ? 7.764   51.009  7.490   1.00 31.00  ? 144  LEU B CD1 1 
ATOM   2149 C  CD2 . LEU B 1 144 ? 7.933   53.414  6.762   1.00 32.78  ? 144  LEU B CD2 1 
ATOM   2150 N  N   . ALA B 1 145 ? 2.604   51.836  5.952   1.00 34.39  ? 145  ALA B N   1 
ATOM   2151 C  CA  . ALA B 1 145 ? 1.253   52.351  6.134   1.00 31.46  ? 145  ALA B CA  1 
ATOM   2152 C  C   . ALA B 1 145 ? 0.551   52.481  4.812   1.00 32.13  ? 145  ALA B C   1 
ATOM   2153 O  O   . ALA B 1 145 ? 1.170   52.750  3.776   1.00 29.44  ? 145  ALA B O   1 
ATOM   2154 C  CB  . ALA B 1 145 ? 1.250   53.683  6.858   1.00 30.89  ? 145  ALA B CB  1 
ATOM   2155 N  N   . CYS B 1 146 ? -0.758  52.300  4.859   1.00 29.74  ? 146  CYS B N   1 
ATOM   2156 C  CA  . CYS B 1 146 ? -1.525  52.287  3.649   1.00 27.83  ? 146  CYS B CA  1 
ATOM   2157 C  C   . CYS B 1 146 ? -2.968  52.692  3.898   1.00 27.34  ? 146  CYS B C   1 
ATOM   2158 O  O   . CYS B 1 146 ? -3.383  52.916  5.031   1.00 29.91  ? 146  CYS B O   1 
ATOM   2159 C  CB  . CYS B 1 146 ? -1.446  50.897  3.035   1.00 27.29  ? 146  CYS B CB  1 
ATOM   2160 S  SG  . CYS B 1 146 ? -2.103  49.604  4.121   1.00 33.05  ? 146  CYS B SG  1 
ATOM   2161 N  N   . GLY B 1 147 ? -3.733  52.763  2.819   1.00 26.18  ? 147  GLY B N   1 
ATOM   2162 C  CA  . GLY B 1 147 ? -5.122  53.131  2.883   1.00 23.27  ? 147  GLY B CA  1 
ATOM   2163 C  C   . GLY B 1 147 ? -5.753  52.894  1.534   1.00 28.63  ? 147  GLY B C   1 
ATOM   2164 O  O   . GLY B 1 147 ? -5.085  52.936  0.499   1.00 29.92  ? 147  GLY B O   1 
ATOM   2165 N  N   . VAL B 1 148 ? -7.051  52.648  1.542   1.00 25.91  ? 148  VAL B N   1 
ATOM   2166 C  CA  . VAL B 1 148 ? -7.789  52.545  0.312   1.00 27.25  ? 148  VAL B CA  1 
ATOM   2167 C  C   . VAL B 1 148 ? -8.142  53.935  -0.219  1.00 30.55  ? 148  VAL B C   1 
ATOM   2168 O  O   . VAL B 1 148 ? -8.613  54.805  0.523   1.00 26.50  ? 148  VAL B O   1 
ATOM   2169 C  CB  . VAL B 1 148 ? -9.068  51.708  0.489   1.00 26.38  ? 148  VAL B CB  1 
ATOM   2170 C  CG1 . VAL B 1 148 ? -9.770  51.537  -0.883  1.00 25.08  ? 148  VAL B CG1 1 
ATOM   2171 C  CG2 . VAL B 1 148 ? -8.711  50.374  1.112   1.00 21.19  ? 148  VAL B CG2 1 
ATOM   2172 N  N   . ILE B 1 149 ? -7.911  54.127  -1.516  1.00 29.16  ? 149  ILE B N   1 
ATOM   2173 C  CA  . ILE B 1 149 ? -8.189  55.398  -2.156  1.00 29.31  ? 149  ILE B CA  1 
ATOM   2174 C  C   . ILE B 1 149 ? -9.681  55.501  -2.446  1.00 29.45  ? 149  ILE B C   1 
ATOM   2175 O  O   . ILE B 1 149 ? -10.246 54.716  -3.209  1.00 29.12  ? 149  ILE B O   1 
ATOM   2176 C  CB  . ILE B 1 149 ? -7.359  55.578  -3.455  1.00 28.10  ? 149  ILE B CB  1 
ATOM   2177 C  CG1 . ILE B 1 149 ? -5.867  55.581  -3.139  1.00 28.26  ? 149  ILE B CG1 1 
ATOM   2178 C  CG2 . ILE B 1 149 ? -7.717  56.866  -4.142  1.00 23.78  ? 149  ILE B CG2 1 
ATOM   2179 C  CD1 . ILE B 1 149 ? -5.001  55.256  -4.346  1.00 25.56  ? 149  ILE B CD1 1 
ATOM   2180 N  N   . GLY B 1 150 ? -10.329 56.479  -1.836  1.00 29.10  ? 150  GLY B N   1 
ATOM   2181 C  CA  . GLY B 1 150 ? -11.750 56.620  -2.034  1.00 28.33  ? 150  GLY B CA  1 
ATOM   2182 C  C   . GLY B 1 150 ? -12.165 57.945  -2.634  1.00 26.92  ? 150  GLY B C   1 
ATOM   2183 O  O   . GLY B 1 150 ? -11.406 58.906  -2.656  1.00 27.52  ? 150  GLY B O   1 
ATOM   2184 N  N   . ILE B 1 151 ? -13.402 57.977  -3.109  1.00 25.40  ? 151  ILE B N   1 
ATOM   2185 C  CA  . ILE B 1 151 ? -13.992 59.154  -3.723  1.00 29.57  ? 151  ILE B CA  1 
ATOM   2186 C  C   . ILE B 1 151 ? -14.187 60.298  -2.737  1.00 30.01  ? 151  ILE B C   1 
ATOM   2187 O  O   . ILE B 1 151 ? -14.723 60.109  -1.637  1.00 32.46  ? 151  ILE B O   1 
ATOM   2188 C  CB  . ILE B 1 151 ? -15.322 58.772  -4.357  1.00 32.05  ? 151  ILE B CB  1 
ATOM   2189 C  CG1 . ILE B 1 151 ? -15.032 57.890  -5.577  1.00 32.25  ? 151  ILE B CG1 1 
ATOM   2190 C  CG2 . ILE B 1 151 ? -16.093 60.009  -4.737  1.00 34.69  ? 151  ILE B CG2 1 
ATOM   2191 C  CD1 . ILE B 1 151 ? -16.124 56.902  -5.940  1.00 31.58  ? 151  ILE B CD1 1 
ATOM   2192 N  N   . ALA B 1 152 ? -13.727 61.485  -3.119  1.00 30.79  ? 152  ALA B N   1 
ATOM   2193 C  CA  . ALA B 1 152 ? -13.812 62.645  -2.236  1.00 31.48  ? 152  ALA B CA  1 
ATOM   2194 C  C   . ALA B 1 152 ? -14.728 63.702  -2.845  1.00 34.15  ? 152  ALA B C   1 
ATOM   2195 O  O   . ALA B 1 152 ? -15.068 63.633  -4.024  1.00 34.70  ? 152  ALA B O   1 
ATOM   2196 C  CB  . ALA B 1 152 ? -12.408 63.217  -1.938  1.00 24.38  ? 152  ALA B CB  1 
ATOM   2197 N  N   . GLN B 1 153 ? -15.118 64.685  -2.044  1.00 34.11  ? 153  GLN B N   1 
ATOM   2198 C  CA  . GLN B 1 153 ? -16.059 65.705  -2.501  1.00 43.20  ? 153  GLN B CA  1 
ATOM   2199 C  C   . GLN B 1 153 ? -15.384 66.852  -3.253  1.00 49.70  ? 153  GLN B C   1 
ATOM   2200 O  O   . GLN B 1 153 ? -14.482 67.494  -2.703  1.00 46.95  ? 153  GLN B O   1 
ATOM   2201 C  CB  . GLN B 1 153 ? -16.836 66.255  -1.307  1.00 50.15  ? 153  GLN B CB  1 
ATOM   2202 C  CG  . GLN B 1 153 ? -17.786 67.380  -1.640  1.00 49.90  ? 153  GLN B CG  1 
ATOM   2203 C  CD  . GLN B 1 153 ? -18.372 67.987  -0.379  1.00 61.66  ? 153  GLN B CD  1 
ATOM   2204 O  OE1 . GLN B 1 153 ? -19.583 68.219  -0.290  1.00 57.56  ? 153  GLN B OE1 1 
ATOM   2205 N  NE2 . GLN B 1 153 ? -17.511 68.238  0.616   1.00 62.83  ? 153  GLN B NE2 1 
ATOM   2206 O  OXT . GLN B 1 153 ? -15.732 67.167  -4.404  1.00 51.79  ? 153  GLN B OXT 1 
ATOM   2207 N  N   . ALA C 1 1   ? -16.552 70.869  9.091   1.00 61.64  ? 1    ALA C N   1 
ATOM   2208 C  CA  . ALA C 1 1   ? -17.181 72.109  9.560   1.00 67.33  ? 1    ALA C CA  1 
ATOM   2209 C  C   . ALA C 1 1   ? -16.987 73.294  8.587   1.00 67.10  ? 1    ALA C C   1 
ATOM   2210 O  O   . ALA C 1 1   ? -16.064 74.108  8.739   1.00 62.01  ? 1    ALA C O   1 
ATOM   2211 C  CB  . ALA C 1 1   ? -16.678 72.465  10.964  1.00 57.52  ? 1    ALA C CB  1 
ATOM   2212 N  N   . MET C 1 2   ? -17.870 73.386  7.594   1.00 62.39  ? 2    MET C N   1 
ATOM   2213 C  CA  . MET C 1 2   ? -17.761 74.403  6.544   1.00 60.83  ? 2    MET C CA  1 
ATOM   2214 C  C   . MET C 1 2   ? -18.731 75.581  6.743   1.00 56.89  ? 2    MET C C   1 
ATOM   2215 O  O   . MET C 1 2   ? -19.963 75.408  6.783   1.00 54.00  ? 2    MET C O   1 
ATOM   2216 C  CB  . MET C 1 2   ? -17.983 73.776  5.154   1.00 61.28  ? 2    MET C CB  1 
ATOM   2217 C  CG  . MET C 1 2   ? -16.853 72.882  4.623   1.00 62.53  ? 2    MET C CG  1 
ATOM   2218 S  SD  . MET C 1 2   ? -17.309 71.977  3.102   1.00 71.03  ? 2    MET C SD  1 
ATOM   2219 C  CE  . MET C 1 2   ? -18.401 70.703  3.742   1.00 57.23  ? 2    MET C CE  1 
ATOM   2220 N  N   . LYS C 1 3   ? -18.163 76.778  6.854   1.00 56.30  ? 3    LYS C N   1 
ATOM   2221 C  CA  . LYS C 1 3   ? -18.950 77.994  7.008   1.00 48.99  ? 3    LYS C CA  1 
ATOM   2222 C  C   . LYS C 1 3   ? -18.733 78.953  5.848   1.00 51.06  ? 3    LYS C C   1 
ATOM   2223 O  O   . LYS C 1 3   ? -17.624 79.079  5.319   1.00 48.17  ? 3    LYS C O   1 
ATOM   2224 C  CB  . LYS C 1 3   ? -18.581 78.700  8.308   1.00 54.17  ? 3    LYS C CB  1 
ATOM   2225 C  CG  . LYS C 1 3   ? -19.258 78.150  9.551   1.00 60.24  ? 3    LYS C CG  1 
ATOM   2226 C  CD  . LYS C 1 3   ? -19.033 79.098  10.714  1.00 64.84  ? 3    LYS C CD  1 
ATOM   2227 C  CE  . LYS C 1 3   ? -20.003 78.826  11.856  1.00 76.51  ? 3    LYS C CE  1 
ATOM   2228 N  NZ  . LYS C 1 3   ? -19.737 77.514  12.535  1.00 76.77  ? 3    LYS C NZ  1 
ATOM   2229 N  N   . ALA C 1 4   ? -19.800 79.631  5.448   1.00 48.92  ? 4    ALA C N   1 
ATOM   2230 C  CA  . ALA C 1 4   ? -19.680 80.726  4.497   1.00 46.40  ? 4    ALA C CA  1 
ATOM   2231 C  C   . ALA C 1 4   ? -20.692 81.798  4.864   1.00 46.56  ? 4    ALA C C   1 
ATOM   2232 O  O   . ALA C 1 4   ? -21.627 81.543  5.629   1.00 39.97  ? 4    ALA C O   1 
ATOM   2233 C  CB  . ALA C 1 4   ? -19.897 80.244  3.068   1.00 41.36  ? 4    ALA C CB  1 
ATOM   2234 N  N   . VAL C 1 5   ? -20.507 82.999  4.326   1.00 41.05  ? 5    VAL C N   1 
ATOM   2235 C  CA  . VAL C 1 5   ? -21.428 84.079  4.621   1.00 43.85  ? 5    VAL C CA  1 
ATOM   2236 C  C   . VAL C 1 5   ? -21.617 84.983  3.420   1.00 47.92  ? 5    VAL C C   1 
ATOM   2237 O  O   . VAL C 1 5   ? -20.770 85.050  2.517   1.00 46.88  ? 5    VAL C O   1 
ATOM   2238 C  CB  . VAL C 1 5   ? -20.992 84.900  5.876   1.00 46.58  ? 5    VAL C CB  1 
ATOM   2239 C  CG1 . VAL C 1 5   ? -19.651 85.597  5.649   1.00 39.55  ? 5    VAL C CG1 1 
ATOM   2240 C  CG2 . VAL C 1 5   ? -22.081 85.883  6.284   1.00 42.66  ? 5    VAL C CG2 1 
ATOM   2241 N  N   . CYS C 1 6   ? -22.749 85.670  3.419   1.00 44.93  ? 6    CYS C N   1 
ATOM   2242 C  CA  . CYS C 1 6   ? -23.128 86.514  2.313   1.00 47.61  ? 6    CYS C CA  1 
ATOM   2243 C  C   . CYS C 1 6   ? -23.972 87.673  2.822   1.00 47.21  ? 6    CYS C C   1 
ATOM   2244 O  O   . CYS C 1 6   ? -25.005 87.465  3.456   1.00 49.57  ? 6    CYS C O   1 
ATOM   2245 C  CB  . CYS C 1 6   ? -23.917 85.694  1.292   1.00 47.89  ? 6    CYS C CB  1 
ATOM   2246 S  SG  . CYS C 1 6   ? -24.559 86.657  -0.076  1.00 55.50  ? 6    CYS C SG  1 
ATOM   2247 N  N   . VAL C 1 7   ? -23.523 88.893  2.555   1.00 45.78  ? 7    VAL C N   1 
ATOM   2248 C  CA  . VAL C 1 7   ? -24.324 90.069  2.863   1.00 52.56  ? 7    VAL C CA  1 
ATOM   2249 C  C   . VAL C 1 7   ? -25.030 90.536  1.582   1.00 55.64  ? 7    VAL C C   1 
ATOM   2250 O  O   . VAL C 1 7   ? -24.410 90.658  0.516   1.00 49.92  ? 7    VAL C O   1 
ATOM   2251 C  CB  . VAL C 1 7   ? -23.481 91.213  3.474   1.00 47.10  ? 7    VAL C CB  1 
ATOM   2252 C  CG1 . VAL C 1 7   ? -24.385 92.227  4.110   1.00 55.61  ? 7    VAL C CG1 1 
ATOM   2253 C  CG2 . VAL C 1 7   ? -22.501 90.673  4.503   1.00 42.82  ? 7    VAL C CG2 1 
ATOM   2254 N  N   . LEU C 1 8   ? -26.331 90.772  1.687   1.00 54.68  ? 8    LEU C N   1 
ATOM   2255 C  CA  . LEU C 1 8   ? -27.128 91.135  0.525   1.00 61.83  ? 8    LEU C CA  1 
ATOM   2256 C  C   . LEU C 1 8   ? -27.447 92.624  0.500   1.00 63.54  ? 8    LEU C C   1 
ATOM   2257 O  O   . LEU C 1 8   ? -28.072 93.143  1.421   1.00 66.92  ? 8    LEU C O   1 
ATOM   2258 C  CB  . LEU C 1 8   ? -28.427 90.327  0.515   1.00 65.75  ? 8    LEU C CB  1 
ATOM   2259 C  CG  . LEU C 1 8   ? -28.255 88.804  0.510   1.00 63.87  ? 8    LEU C CG  1 
ATOM   2260 C  CD1 . LEU C 1 8   ? -29.492 88.107  1.049   1.00 64.10  ? 8    LEU C CD1 1 
ATOM   2261 C  CD2 . LEU C 1 8   ? -27.928 88.305  -0.882  1.00 64.00  ? 8    LEU C CD2 1 
ATOM   2262 N  N   . LYS C 1 9   ? -27.009 93.307  -0.553  1.00 63.13  ? 9    LYS C N   1 
ATOM   2263 C  CA  . LYS C 1 9   ? -27.351 94.713  -0.751  1.00 69.80  ? 9    LYS C CA  1 
ATOM   2264 C  C   . LYS C 1 9   ? -28.054 94.866  -2.105  1.00 75.09  ? 9    LYS C C   1 
ATOM   2265 O  O   . LYS C 1 9   ? -27.823 94.083  -3.029  1.00 71.98  ? 9    LYS C O   1 
ATOM   2266 C  CB  . LYS C 1 9   ? -26.097 95.606  -0.729  1.00 69.85  ? 9    LYS C CB  1 
ATOM   2267 C  CG  . LYS C 1 9   ? -24.969 95.178  0.216   1.00 69.77  ? 9    LYS C CG  1 
ATOM   2268 C  CD  . LYS C 1 9   ? -25.110 95.789  1.616   1.00 80.43  ? 9    LYS C CD  1 
ATOM   2269 C  CE  . LYS C 1 9   ? -24.823 97.288  1.628   1.00 81.25  ? 9    LYS C CE  1 
ATOM   2270 N  NZ  . LYS C 1 9   ? -25.105 97.908  2.959   1.00 79.81  ? 9    LYS C NZ  1 
ATOM   2271 N  N   . GLY C 1 10  ? -28.912 95.873  -2.224  1.00 75.20  ? 10   GLY C N   1 
ATOM   2272 C  CA  . GLY C 1 10  ? -29.510 96.202  -3.504  1.00 79.04  ? 10   GLY C CA  1 
ATOM   2273 C  C   . GLY C 1 10  ? -29.437 97.700  -3.707  1.00 89.72  ? 10   GLY C C   1 
ATOM   2274 O  O   . GLY C 1 10  ? -28.845 98.402  -2.889  1.00 92.75  ? 10   GLY C O   1 
ATOM   2275 N  N   . ASP C 1 11  ? -30.027 98.206  -4.786  1.00 91.86  ? 11   ASP C N   1 
ATOM   2276 C  CA  . ASP C 1 11  ? -30.109 99.656  -4.957  1.00 93.96  ? 11   ASP C CA  1 
ATOM   2277 C  C   . ASP C 1 11  ? -31.271 100.230 -4.137  1.00 92.53  ? 11   ASP C C   1 
ATOM   2278 O  O   . ASP C 1 11  ? -31.483 101.441 -4.105  1.00 89.91  ? 11   ASP C O   1 
ATOM   2279 C  CB  . ASP C 1 11  ? -30.212 100.040 -6.438  1.00 91.42  ? 11   ASP C CB  1 
ATOM   2280 C  CG  . ASP C 1 11  ? -28.914 99.787  -7.200  1.00 94.79  ? 11   ASP C CG  1 
ATOM   2281 O  OD1 . ASP C 1 11  ? -27.827 99.882  -6.586  1.00 97.44  ? 11   ASP C OD1 1 
ATOM   2282 O  OD2 . ASP C 1 11  ? -28.976 99.496  -8.415  1.00 93.85  ? 11   ASP C OD2 1 
ATOM   2283 N  N   . GLY C 1 12  ? -32.004 99.343  -3.464  1.00 91.86  ? 12   GLY C N   1 
ATOM   2284 C  CA  . GLY C 1 12  ? -33.105 99.727  -2.596  1.00 91.24  ? 12   GLY C CA  1 
ATOM   2285 C  C   . GLY C 1 12  ? -32.912 99.271  -1.158  1.00 93.97  ? 12   GLY C C   1 
ATOM   2286 O  O   . GLY C 1 12  ? -31.794 98.953  -0.753  1.00 93.69  ? 12   GLY C O   1 
ATOM   2287 N  N   . PRO C 1 13  ? -34.005 99.231  -0.376  1.00 95.54  ? 13   PRO C N   1 
ATOM   2288 C  CA  . PRO C 1 13  ? -33.944 98.926  1.060   1.00 93.32  ? 13   PRO C CA  1 
ATOM   2289 C  C   . PRO C 1 13  ? -33.881 97.423  1.340   1.00 88.57  ? 13   PRO C C   1 
ATOM   2290 O  O   . PRO C 1 13  ? -33.831 97.006  2.498   1.00 86.17  ? 13   PRO C O   1 
ATOM   2291 C  CB  . PRO C 1 13  ? -35.266 99.501  1.600   1.00 95.63  ? 13   PRO C CB  1 
ATOM   2292 C  CG  . PRO C 1 13  ? -35.934 100.203 0.419   1.00 96.28  ? 13   PRO C CG  1 
ATOM   2293 C  CD  . PRO C 1 13  ? -35.376 99.547  -0.799  1.00 93.72  ? 13   PRO C CD  1 
ATOM   2294 N  N   . VAL C 1 14  ? -33.886 96.618  0.287   1.00 86.12  ? 14   VAL C N   1 
ATOM   2295 C  CA  . VAL C 1 14  ? -33.832 95.173  0.446   1.00 84.99  ? 14   VAL C CA  1 
ATOM   2296 C  C   . VAL C 1 14  ? -32.415 94.714  0.777   1.00 86.62  ? 14   VAL C C   1 
ATOM   2297 O  O   . VAL C 1 14  ? -31.545 94.669  -0.099  1.00 82.36  ? 14   VAL C O   1 
ATOM   2298 C  CB  . VAL C 1 14  ? -34.320 94.464  -0.821  1.00 86.56  ? 14   VAL C CB  1 
ATOM   2299 C  CG1 . VAL C 1 14  ? -34.276 92.953  -0.636  1.00 83.95  ? 14   VAL C CG1 1 
ATOM   2300 C  CG2 . VAL C 1 14  ? -35.725 94.929  -1.160  1.00 88.26  ? 14   VAL C CG2 1 
ATOM   2301 N  N   . GLN C 1 15  ? -32.192 94.373  2.044   1.00 84.84  ? 15   GLN C N   1 
ATOM   2302 C  CA  . GLN C 1 15  ? -30.861 94.007  2.526   1.00 79.57  ? 15   GLN C CA  1 
ATOM   2303 C  C   . GLN C 1 15  ? -30.929 92.973  3.642   1.00 76.92  ? 15   GLN C C   1 
ATOM   2304 O  O   . GLN C 1 15  ? -31.979 92.778  4.249   1.00 80.10  ? 15   GLN C O   1 
ATOM   2305 C  CB  . GLN C 1 15  ? -30.113 95.248  3.035   1.00 84.18  ? 15   GLN C CB  1 
ATOM   2306 C  CG  . GLN C 1 15  ? -30.797 95.962  4.209   1.00 81.41  ? 15   GLN C CG  1 
ATOM   2307 C  CD  . GLN C 1 15  ? -29.999 97.152  4.726   1.00 85.41  ? 15   GLN C CD  1 
ATOM   2308 O  OE1 . GLN C 1 15  ? -30.186 98.286  4.273   1.00 76.89  ? 15   GLN C OE1 1 
ATOM   2309 N  NE2 . GLN C 1 15  ? -29.103 96.897  5.685   1.00 83.79  ? 15   GLN C NE2 1 
ATOM   2310 N  N   . GLY C 1 16  ? -29.799 92.328  3.920   1.00 73.76  ? 16   GLY C N   1 
ATOM   2311 C  CA  . GLY C 1 16  ? -29.725 91.343  4.984   1.00 67.14  ? 16   GLY C CA  1 
ATOM   2312 C  C   . GLY C 1 16  ? -28.501 90.451  4.906   1.00 61.68  ? 16   GLY C C   1 
ATOM   2313 O  O   . GLY C 1 16  ? -27.649 90.592  4.028   1.00 64.05  ? 16   GLY C O   1 
ATOM   2314 N  N   . THR C 1 17  ? -28.419 89.510  5.832   1.00 57.02  ? 17   THR C N   1 
ATOM   2315 C  CA  . THR C 1 17  ? -27.255 88.648  5.932   1.00 54.90  ? 17   THR C CA  1 
ATOM   2316 C  C   . THR C 1 17  ? -27.710 87.198  5.952   1.00 58.56  ? 17   THR C C   1 
ATOM   2317 O  O   . THR C 1 17  ? -28.715 86.871  6.590   1.00 58.34  ? 17   THR C O   1 
ATOM   2318 C  CB  . THR C 1 17  ? -26.474 88.951  7.224   1.00 47.31  ? 17   THR C CB  1 
ATOM   2319 O  OG1 . THR C 1 17  ? -26.064 90.321  7.211   1.00 59.40  ? 17   THR C OG1 1 
ATOM   2320 C  CG2 . THR C 1 17  ? -25.249 88.064  7.343   1.00 46.60  ? 17   THR C CG2 1 
ATOM   2321 N  N   . ILE C 1 18  ? -26.979 86.335  5.253   1.00 51.88  ? 18   ILE C N   1 
ATOM   2322 C  CA  . ILE C 1 18  ? -27.289 84.914  5.230   1.00 49.24  ? 18   ILE C CA  1 
ATOM   2323 C  C   . ILE C 1 18  ? -26.063 84.106  5.615   1.00 50.32  ? 18   ILE C C   1 
ATOM   2324 O  O   . ILE C 1 18  ? -24.997 84.277  5.031   1.00 53.48  ? 18   ILE C O   1 
ATOM   2325 C  CB  . ILE C 1 18  ? -27.754 84.478  3.831   1.00 55.37  ? 18   ILE C CB  1 
ATOM   2326 C  CG1 . ILE C 1 18  ? -28.835 85.425  3.319   1.00 53.14  ? 18   ILE C CG1 1 
ATOM   2327 C  CG2 . ILE C 1 18  ? -28.257 83.031  3.847   1.00 55.94  ? 18   ILE C CG2 1 
ATOM   2328 C  CD1 . ILE C 1 18  ? -30.094 85.401  4.146   1.00 57.48  ? 18   ILE C CD1 1 
ATOM   2329 N  N   . HIS C 1 19  ? -26.202 83.231  6.605   1.00 53.64  ? 19   HIS C N   1 
ATOM   2330 C  CA  . HIS C 1 19  ? -25.089 82.369  7.003   1.00 51.67  ? 19   HIS C CA  1 
ATOM   2331 C  C   . HIS C 1 19  ? -25.262 80.956  6.431   1.00 52.62  ? 19   HIS C C   1 
ATOM   2332 O  O   . HIS C 1 19  ? -26.383 80.465  6.313   1.00 53.41  ? 19   HIS C O   1 
ATOM   2333 C  CB  . HIS C 1 19  ? -24.947 82.318  8.529   1.00 47.43  ? 19   HIS C CB  1 
ATOM   2334 C  CG  . HIS C 1 19  ? -24.546 83.622  9.153   1.00 52.77  ? 19   HIS C CG  1 
ATOM   2335 N  ND1 . HIS C 1 19  ? -23.228 83.971  9.365   1.00 51.32  ? 19   HIS C ND1 1 
ATOM   2336 C  CD2 . HIS C 1 19  ? -25.289 84.650  9.632   1.00 50.99  ? 19   HIS C CD2 1 
ATOM   2337 C  CE1 . HIS C 1 19  ? -23.177 85.159  9.943   1.00 50.42  ? 19   HIS C CE1 1 
ATOM   2338 N  NE2 . HIS C 1 19  ? -24.414 85.591  10.119  1.00 52.58  ? 19   HIS C NE2 1 
ATOM   2339 N  N   . PHE C 1 20  ? -24.146 80.314  6.084   1.00 49.87  ? 20   PHE C N   1 
ATOM   2340 C  CA  . PHE C 1 20  ? -24.152 78.994  5.454   1.00 54.65  ? 20   PHE C CA  1 
ATOM   2341 C  C   . PHE C 1 20  ? -23.342 78.000  6.266   1.00 54.23  ? 20   PHE C C   1 
ATOM   2342 O  O   . PHE C 1 20  ? -22.181 78.253  6.586   1.00 51.06  ? 20   PHE C O   1 
ATOM   2343 C  CB  . PHE C 1 20  ? -23.547 79.049  4.038   1.00 50.91  ? 20   PHE C CB  1 
ATOM   2344 C  CG  . PHE C 1 20  ? -24.318 79.902  3.075   1.00 56.91  ? 20   PHE C CG  1 
ATOM   2345 C  CD1 . PHE C 1 20  ? -25.010 79.326  2.022   1.00 58.19  ? 20   PHE C CD1 1 
ATOM   2346 C  CD2 . PHE C 1 20  ? -24.351 81.288  3.223   1.00 58.25  ? 20   PHE C CD2 1 
ATOM   2347 C  CE1 . PHE C 1 20  ? -25.728 80.108  1.132   1.00 57.73  ? 20   PHE C CE1 1 
ATOM   2348 C  CE2 . PHE C 1 20  ? -25.068 82.078  2.337   1.00 57.71  ? 20   PHE C CE2 1 
ATOM   2349 C  CZ  . PHE C 1 20  ? -25.759 81.484  1.285   1.00 59.43  ? 20   PHE C CZ  1 
ATOM   2350 N  N   . GLU C 1 21  ? -23.942 76.853  6.567   1.00 57.60  ? 21   GLU C N   1 
ATOM   2351 C  CA  . GLU C 1 21  ? -23.211 75.792  7.246   1.00 60.19  ? 21   GLU C CA  1 
ATOM   2352 C  C   . GLU C 1 21  ? -23.496 74.414  6.645   1.00 61.69  ? 21   GLU C C   1 
ATOM   2353 O  O   . GLU C 1 21  ? -24.659 74.019  6.454   1.00 55.89  ? 21   GLU C O   1 
ATOM   2354 C  CB  . GLU C 1 21  ? -23.483 75.806  8.756   1.00 60.82  ? 21   GLU C CB  1 
ATOM   2355 C  CG  . GLU C 1 21  ? -22.264 75.416  9.588   1.00 67.34  ? 21   GLU C CG  1 
ATOM   2356 C  CD  . GLU C 1 21  ? -22.493 75.578  11.082  1.00 74.96  ? 21   GLU C CD  1 
ATOM   2357 O  OE1 . GLU C 1 21  ? -23.509 76.210  11.454  1.00 70.82  ? 21   GLU C OE1 1 
ATOM   2358 O  OE2 . GLU C 1 21  ? -21.657 75.079  11.875  1.00 66.71  ? 21   GLU C OE2 1 
ATOM   2359 N  N   . GLN C 1 22  ? -22.410 73.714  6.327   1.00 58.28  ? 22   GLN C N   1 
ATOM   2360 C  CA  . GLN C 1 22  ? -22.461 72.354  5.808   1.00 65.48  ? 22   GLN C CA  1 
ATOM   2361 C  C   . GLN C 1 22  ? -21.494 71.560  6.671   1.00 63.79  ? 22   GLN C C   1 
ATOM   2362 O  O   . GLN C 1 22  ? -20.305 71.881  6.732   1.00 63.59  ? 22   GLN C O   1 
ATOM   2363 C  CB  . GLN C 1 22  ? -22.033 72.312  4.337   1.00 63.68  ? 22   GLN C CB  1 
ATOM   2364 C  CG  . GLN C 1 22  ? -22.580 71.127  3.543   1.00 60.70  ? 22   GLN C CG  1 
ATOM   2365 C  CD  . GLN C 1 22  ? -21.854 70.942  2.214   1.00 65.29  ? 22   GLN C CD  1 
ATOM   2366 O  OE1 . GLN C 1 22  ? -20.959 71.725  1.874   1.00 62.67  ? 22   GLN C OE1 1 
ATOM   2367 N  NE2 . GLN C 1 22  ? -22.230 69.899  1.457   1.00 58.98  ? 22   GLN C NE2 1 
ATOM   2368 N  N   . LYS C 1 23  ? -22.006 70.538  7.351   1.00 62.11  ? 23   LYS C N   1 
ATOM   2369 C  CA  . LYS C 1 23  ? -21.272 69.919  8.456   1.00 62.30  ? 23   LYS C CA  1 
ATOM   2370 C  C   . LYS C 1 23  ? -20.124 69.025  7.991   1.00 57.61  ? 23   LYS C C   1 
ATOM   2371 O  O   . LYS C 1 23  ? -19.064 68.973  8.621   1.00 56.85  ? 23   LYS C O   1 
ATOM   2372 C  CB  . LYS C 1 23  ? -22.237 69.144  9.361   1.00 69.54  ? 23   LYS C CB  1 
ATOM   2373 C  CG  . LYS C 1 23  ? -21.627 68.711  10.686  1.00 79.83  ? 23   LYS C CG  1 
ATOM   2374 C  CD  . LYS C 1 23  ? -22.687 68.188  11.649  1.00 82.27  ? 23   LYS C CD  1 
ATOM   2375 C  CE  . LYS C 1 23  ? -22.057 67.709  12.954  1.00 74.73  ? 23   LYS C CE  1 
ATOM   2376 N  NZ  . LYS C 1 23  ? -23.094 67.244  13.912  1.00 74.11  ? 23   LYS C NZ  1 
ATOM   2377 N  N   . ALA C 1 24  ? -20.356 68.328  6.883   1.00 55.03  ? 24   ALA C N   1 
ATOM   2378 C  CA  . ALA C 1 24  ? -19.375 67.435  6.295   1.00 50.22  ? 24   ALA C CA  1 
ATOM   2379 C  C   . ALA C 1 24  ? -19.695 67.277  4.828   1.00 54.53  ? 24   ALA C C   1 
ATOM   2380 O  O   . ALA C 1 24  ? -20.761 67.699  4.361   1.00 57.98  ? 24   ALA C O   1 
ATOM   2381 C  CB  . ALA C 1 24  ? -19.398 66.081  6.980   1.00 49.98  ? 24   ALA C CB  1 
ATOM   2382 N  N   . SER C 1 25  ? -18.769 66.663  4.105   1.00 51.98  ? 25   SER C N   1 
ATOM   2383 C  CA  . SER C 1 25  ? -18.895 66.492  2.662   1.00 52.96  ? 25   SER C CA  1 
ATOM   2384 C  C   . SER C 1 25  ? -20.247 65.919  2.215   1.00 49.37  ? 25   SER C C   1 
ATOM   2385 O  O   . SER C 1 25  ? -20.828 65.066  2.880   1.00 45.17  ? 25   SER C O   1 
ATOM   2386 C  CB  . SER C 1 25  ? -17.757 65.610  2.157   1.00 50.41  ? 25   SER C CB  1 
ATOM   2387 O  OG  . SER C 1 25  ? -16.559 65.929  2.849   1.00 59.03  ? 25   SER C OG  1 
ATOM   2388 N  N   . GLY C 1 26  ? -20.738 66.402  1.079   1.00 51.99  ? 26   GLY C N   1 
ATOM   2389 C  CA  . GLY C 1 26  ? -21.993 65.941  0.513   1.00 47.41  ? 26   GLY C CA  1 
ATOM   2390 C  C   . GLY C 1 26  ? -23.223 66.245  1.352   1.00 51.82  ? 26   GLY C C   1 
ATOM   2391 O  O   . GLY C 1 26  ? -24.340 65.929  0.936   1.00 48.03  ? 26   GLY C O   1 
ATOM   2392 N  N   . GLU C 1 27  ? -23.027 66.857  2.523   1.00 55.41  ? 27   GLU C N   1 
ATOM   2393 C  CA  . GLU C 1 27  ? -24.134 67.147  3.439   1.00 56.52  ? 27   GLU C CA  1 
ATOM   2394 C  C   . GLU C 1 27  ? -25.021 68.297  2.955   1.00 60.61  ? 27   GLU C C   1 
ATOM   2395 O  O   . GLU C 1 27  ? -24.658 69.029  2.025   1.00 62.84  ? 27   GLU C O   1 
ATOM   2396 C  CB  . GLU C 1 27  ? -23.618 67.436  4.849   1.00 48.53  ? 27   GLU C CB  1 
ATOM   2397 C  CG  . GLU C 1 27  ? -23.002 66.222  5.539   1.00 57.11  ? 27   GLU C CG  1 
ATOM   2398 C  CD  . GLU C 1 27  ? -24.034 65.246  6.129   1.00 54.02  ? 27   GLU C CD  1 
ATOM   2399 O  OE1 . GLU C 1 27  ? -25.210 65.629  6.289   1.00 60.51  ? 27   GLU C OE1 1 
ATOM   2400 O  OE2 . GLU C 1 27  ? -23.658 64.097  6.454   1.00 42.23  ? 27   GLU C OE2 1 
ATOM   2401 N  N   . PRO C 1 28  ? -26.209 68.440  3.566   1.00 64.63  ? 28   PRO C N   1 
ATOM   2402 C  CA  . PRO C 1 28  ? -27.069 69.598  3.280   1.00 67.90  ? 28   PRO C CA  1 
ATOM   2403 C  C   . PRO C 1 28  ? -26.462 70.896  3.808   1.00 64.21  ? 28   PRO C C   1 
ATOM   2404 O  O   . PRO C 1 28  ? -25.645 70.881  4.729   1.00 64.34  ? 28   PRO C O   1 
ATOM   2405 C  CB  . PRO C 1 28  ? -28.362 69.279  4.042   1.00 64.25  ? 28   PRO C CB  1 
ATOM   2406 C  CG  . PRO C 1 28  ? -28.349 67.799  4.218   1.00 64.93  ? 28   PRO C CG  1 
ATOM   2407 C  CD  . PRO C 1 28  ? -26.906 67.417  4.364   1.00 60.11  ? 28   PRO C CD  1 
ATOM   2408 N  N   . VAL C 1 29  ? -26.864 72.013  3.219   1.00 64.15  ? 29   VAL C N   1 
ATOM   2409 C  CA  . VAL C 1 29  ? -26.398 73.311  3.673   1.00 63.58  ? 29   VAL C CA  1 
ATOM   2410 C  C   . VAL C 1 29  ? -27.528 74.034  4.396   1.00 63.78  ? 29   VAL C C   1 
ATOM   2411 O  O   . VAL C 1 29  ? -28.649 74.126  3.891   1.00 63.26  ? 29   VAL C O   1 
ATOM   2412 C  CB  . VAL C 1 29  ? -25.877 74.163  2.493   1.00 66.92  ? 29   VAL C CB  1 
ATOM   2413 C  CG1 . VAL C 1 29  ? -25.594 75.598  2.939   1.00 62.07  ? 29   VAL C CG1 1 
ATOM   2414 C  CG2 . VAL C 1 29  ? -24.628 73.512  1.873   1.00 66.42  ? 29   VAL C CG2 1 
ATOM   2415 N  N   . VAL C 1 30  ? -27.239 74.523  5.597   1.00 64.60  ? 30   VAL C N   1 
ATOM   2416 C  CA  . VAL C 1 30  ? -28.246 75.240  6.366   1.00 62.63  ? 30   VAL C CA  1 
ATOM   2417 C  C   . VAL C 1 30  ? -28.089 76.746  6.181   1.00 61.20  ? 30   VAL C C   1 
ATOM   2418 O  O   . VAL C 1 30  ? -27.001 77.302  6.341   1.00 57.96  ? 30   VAL C O   1 
ATOM   2419 C  CB  . VAL C 1 30  ? -28.199 74.876  7.860   1.00 63.96  ? 30   VAL C CB  1 
ATOM   2420 C  CG1 . VAL C 1 30  ? -29.397 75.483  8.587   1.00 62.71  ? 30   VAL C CG1 1 
ATOM   2421 C  CG2 . VAL C 1 30  ? -28.185 73.367  8.027   1.00 64.67  ? 30   VAL C CG2 1 
ATOM   2422 N  N   . LEU C 1 31  ? -29.194 77.390  5.828   1.00 62.46  ? 31   LEU C N   1 
ATOM   2423 C  CA  . LEU C 1 31  ? -29.222 78.817  5.564   1.00 59.54  ? 31   LEU C CA  1 
ATOM   2424 C  C   . LEU C 1 31  ? -30.083 79.527  6.587   1.00 64.04  ? 31   LEU C C   1 
ATOM   2425 O  O   . LEU C 1 31  ? -31.305 79.372  6.607   1.00 70.33  ? 31   LEU C O   1 
ATOM   2426 C  CB  . LEU C 1 31  ? -29.768 79.098  4.162   1.00 61.25  ? 31   LEU C CB  1 
ATOM   2427 C  CG  . LEU C 1 31  ? -28.810 78.948  2.981   1.00 59.66  ? 31   LEU C CG  1 
ATOM   2428 C  CD1 . LEU C 1 31  ? -28.400 77.494  2.759   1.00 58.89  ? 31   LEU C CD1 1 
ATOM   2429 C  CD2 . LEU C 1 31  ? -29.460 79.524  1.746   1.00 64.27  ? 31   LEU C CD2 1 
ATOM   2430 N  N   . SER C 1 32  ? -29.439 80.310  7.436   1.00 58.82  ? 32   SER C N   1 
ATOM   2431 C  CA  . SER C 1 32  ? -30.151 81.109  8.408   1.00 59.84  ? 32   SER C CA  1 
ATOM   2432 C  C   . SER C 1 32  ? -29.795 82.582  8.232   1.00 64.47  ? 32   SER C C   1 
ATOM   2433 O  O   . SER C 1 32  ? -28.777 82.930  7.622   1.00 58.50  ? 32   SER C O   1 
ATOM   2434 C  CB  . SER C 1 32  ? -29.825 80.639  9.824   1.00 58.82  ? 32   SER C CB  1 
ATOM   2435 O  OG  . SER C 1 32  ? -28.429 80.424  9.976   1.00 61.37  ? 32   SER C OG  1 
ATOM   2436 N  N   . GLY C 1 33  ? -30.641 83.443  8.779   1.00 65.79  ? 33   GLY C N   1 
ATOM   2437 C  CA  . GLY C 1 33  ? -30.485 84.868  8.608   1.00 66.09  ? 33   GLY C CA  1 
ATOM   2438 C  C   . GLY C 1 33  ? -31.826 85.508  8.333   1.00 71.38  ? 33   GLY C C   1 
ATOM   2439 O  O   . GLY C 1 33  ? -32.872 84.928  8.618   1.00 69.34  ? 33   GLY C O   1 
ATOM   2440 N  N   . GLN C 1 34  ? -31.791 86.701  7.755   1.00 74.29  ? 34   GLN C N   1 
ATOM   2441 C  CA  . GLN C 1 34  ? -32.981 87.525  7.637   1.00 77.37  ? 34   GLN C CA  1 
ATOM   2442 C  C   . GLN C 1 34  ? -32.810 88.487  6.475   1.00 74.81  ? 34   GLN C C   1 
ATOM   2443 O  O   . GLN C 1 34  ? -31.694 88.728  6.018   1.00 72.43  ? 34   GLN C O   1 
ATOM   2444 C  CB  . GLN C 1 34  ? -33.174 88.307  8.935   1.00 74.11  ? 34   GLN C CB  1 
ATOM   2445 C  CG  . GLN C 1 34  ? -34.444 89.105  9.018   1.00 79.06  ? 34   GLN C CG  1 
ATOM   2446 C  CD  . GLN C 1 34  ? -34.374 90.162  10.099  1.00 90.43  ? 34   GLN C CD  1 
ATOM   2447 O  OE1 . GLN C 1 34  ? -33.720 91.194  9.925   1.00 88.80  ? 34   GLN C OE1 1 
ATOM   2448 N  NE2 . GLN C 1 34  ? -35.041 89.912  11.228  1.00 91.97  ? 34   GLN C NE2 1 
ATOM   2449 N  N   . ILE C 1 35  ? -33.922 89.024  5.987   1.00 73.96  ? 35   ILE C N   1 
ATOM   2450 C  CA  . ILE C 1 35  ? -33.881 90.101  5.009   1.00 74.51  ? 35   ILE C CA  1 
ATOM   2451 C  C   . ILE C 1 35  ? -34.917 91.163  5.399   1.00 82.72  ? 35   ILE C C   1 
ATOM   2452 O  O   . ILE C 1 35  ? -36.007 90.835  5.864   1.00 84.43  ? 35   ILE C O   1 
ATOM   2453 C  CB  . ILE C 1 35  ? -34.096 89.580  3.574   1.00 75.56  ? 35   ILE C CB  1 
ATOM   2454 C  CG1 . ILE C 1 35  ? -33.103 88.450  3.272   1.00 74.33  ? 35   ILE C CG1 1 
ATOM   2455 C  CG2 . ILE C 1 35  ? -33.959 90.713  2.560   1.00 75.55  ? 35   ILE C CG2 1 
ATOM   2456 C  CD1 . ILE C 1 35  ? -33.143 87.939  1.843   1.00 70.19  ? 35   ILE C CD1 1 
ATOM   2457 N  N   . THR C 1 36  ? -34.562 92.435  5.242   1.00 82.92  ? 36   THR C N   1 
ATOM   2458 C  CA  . THR C 1 36  ? -35.423 93.525  5.681   1.00 80.15  ? 36   THR C CA  1 
ATOM   2459 C  C   . THR C 1 36  ? -35.848 94.366  4.500   1.00 85.49  ? 36   THR C C   1 
ATOM   2460 O  O   . THR C 1 36  ? -35.266 94.262  3.418   1.00 87.87  ? 36   THR C O   1 
ATOM   2461 C  CB  . THR C 1 36  ? -34.691 94.449  6.660   1.00 79.16  ? 36   THR C CB  1 
ATOM   2462 O  OG1 . THR C 1 36  ? -33.485 94.915  6.049   1.00 83.58  ? 36   THR C OG1 1 
ATOM   2463 C  CG2 . THR C 1 36  ? -34.345 93.715  7.943   1.00 82.26  ? 36   THR C CG2 1 
ATOM   2464 N  N   . GLY C 1 37  ? -36.856 95.209  4.713   1.00 84.75  ? 37   GLY C N   1 
ATOM   2465 C  CA  . GLY C 1 37  ? -37.273 96.173  3.710   1.00 85.30  ? 37   GLY C CA  1 
ATOM   2466 C  C   . GLY C 1 37  ? -37.729 95.534  2.414   1.00 88.56  ? 37   GLY C C   1 
ATOM   2467 O  O   . GLY C 1 37  ? -37.396 95.993  1.319   1.00 85.98  ? 37   GLY C O   1 
ATOM   2468 N  N   . LEU C 1 38  ? -38.489 94.455  2.545   1.00 94.48  ? 38   LEU C N   1 
ATOM   2469 C  CA  . LEU C 1 38  ? -39.136 93.829  1.404   1.00 95.09  ? 38   LEU C CA  1 
ATOM   2470 C  C   . LEU C 1 38  ? -40.574 94.317  1.299   1.00 95.50  ? 38   LEU C C   1 
ATOM   2471 O  O   . LEU C 1 38  ? -41.078 95.025  2.175   1.00 91.87  ? 38   LEU C O   1 
ATOM   2472 C  CB  . LEU C 1 38  ? -39.127 92.307  1.559   1.00 91.05  ? 38   LEU C CB  1 
ATOM   2473 C  CG  . LEU C 1 38  ? -37.790 91.620  1.297   1.00 90.98  ? 38   LEU C CG  1 
ATOM   2474 C  CD1 . LEU C 1 38  ? -37.771 90.228  1.896   1.00 88.42  ? 38   LEU C CD1 1 
ATOM   2475 C  CD2 . LEU C 1 38  ? -37.514 91.577  -0.199  1.00 91.36  ? 38   LEU C CD2 1 
ATOM   2476 N  N   . THR C 1 39  ? -41.235 93.945  0.215   1.00 99.41  ? 39   THR C N   1 
ATOM   2477 C  CA  . THR C 1 39  ? -42.679 94.085  0.148   1.00 105.43 ? 39   THR C CA  1 
ATOM   2478 C  C   . THR C 1 39  ? -43.284 92.819  0.766   1.00 103.34 ? 39   THR C C   1 
ATOM   2479 O  O   . THR C 1 39  ? -42.676 91.743  0.713   1.00 98.94  ? 39   THR C O   1 
ATOM   2480 C  CB  . THR C 1 39  ? -43.166 94.293  -1.309  1.00 106.52 ? 39   THR C CB  1 
ATOM   2481 O  OG1 . THR C 1 39  ? -42.149 93.862  -2.226  1.00 99.38  ? 39   THR C OG1 1 
ATOM   2482 C  CG2 . THR C 1 39  ? -43.473 95.768  -1.565  1.00 100.22 ? 39   THR C CG2 1 
ATOM   2483 N  N   . GLU C 1 40  ? -44.458 92.947  1.378   1.00 100.94 ? 40   GLU C N   1 
ATOM   2484 C  CA  . GLU C 1 40  ? -45.099 91.795  2.002   1.00 97.88  ? 40   GLU C CA  1 
ATOM   2485 C  C   . GLU C 1 40  ? -45.258 90.660  0.993   1.00 99.05  ? 40   GLU C C   1 
ATOM   2486 O  O   . GLU C 1 40  ? -45.069 90.849  -0.212  1.00 98.67  ? 40   GLU C O   1 
ATOM   2487 C  CB  . GLU C 1 40  ? -46.452 92.173  2.609   1.00 94.55  ? 40   GLU C CB  1 
ATOM   2488 C  CG  . GLU C 1 40  ? -47.054 91.079  3.477   1.00 97.25  ? 40   GLU C CG  1 
ATOM   2489 C  CD  . GLU C 1 40  ? -48.178 91.581  4.365   1.00 103.77 ? 40   GLU C CD  1 
ATOM   2490 O  OE1 . GLU C 1 40  ? -48.893 92.520  3.951   1.00 105.54 ? 40   GLU C OE1 1 
ATOM   2491 O  OE2 . GLU C 1 40  ? -48.347 91.035  5.478   1.00 98.66  ? 40   GLU C OE2 1 
ATOM   2492 N  N   . GLY C 1 41  ? -45.591 89.476  1.493   1.00 93.85  ? 41   GLY C N   1 
ATOM   2493 C  CA  . GLY C 1 41  ? -45.753 88.319  0.641   1.00 88.18  ? 41   GLY C CA  1 
ATOM   2494 C  C   . GLY C 1 41  ? -44.429 87.658  0.345   1.00 90.18  ? 41   GLY C C   1 
ATOM   2495 O  O   . GLY C 1 41  ? -43.483 87.752  1.124   1.00 89.96  ? 41   GLY C O   1 
ATOM   2496 N  N   . GLN C 1 42  ? -44.362 86.995  -0.801  1.00 92.25  ? 42   GLN C N   1 
ATOM   2497 C  CA  . GLN C 1 42  ? -43.198 86.200  -1.153  1.00 92.20  ? 42   GLN C CA  1 
ATOM   2498 C  C   . GLN C 1 42  ? -42.376 86.830  -2.276  1.00 90.72  ? 42   GLN C C   1 
ATOM   2499 O  O   . GLN C 1 42  ? -42.905 87.561  -3.117  1.00 87.58  ? 42   GLN C O   1 
ATOM   2500 C  CB  . GLN C 1 42  ? -43.625 84.780  -1.537  1.00 90.88  ? 42   GLN C CB  1 
ATOM   2501 C  CG  . GLN C 1 42  ? -44.289 84.002  -0.409  1.00 91.48  ? 42   GLN C CG  1 
ATOM   2502 C  CD  . GLN C 1 42  ? -44.618 82.565  -0.792  1.00 93.57  ? 42   GLN C CD  1 
ATOM   2503 O  OE1 . GLN C 1 42  ? -44.255 82.099  -1.872  1.00 95.20  ? 42   GLN C OE1 1 
ATOM   2504 N  NE2 . GLN C 1 42  ? -45.305 81.856  0.099   1.00 92.16  ? 42   GLN C NE2 1 
ATOM   2505 N  N   . HIS C 1 43  ? -41.077 86.533  -2.262  1.00 90.94  ? 43   HIS C N   1 
ATOM   2506 C  CA  . HIS C 1 43  ? -40.122 87.010  -3.258  1.00 89.90  ? 43   HIS C CA  1 
ATOM   2507 C  C   . HIS C 1 43  ? -39.220 85.842  -3.647  1.00 86.67  ? 43   HIS C C   1 
ATOM   2508 O  O   . HIS C 1 43  ? -38.960 84.966  -2.824  1.00 86.81  ? 43   HIS C O   1 
ATOM   2509 C  CB  . HIS C 1 43  ? -39.261 88.135  -2.674  1.00 88.32  ? 43   HIS C CB  1 
ATOM   2510 C  CG  . HIS C 1 43  ? -40.043 89.318  -2.186  1.00 94.21  ? 43   HIS C CG  1 
ATOM   2511 N  ND1 . HIS C 1 43  ? -40.024 90.539  -2.827  1.00 95.68  ? 43   HIS C ND1 1 
ATOM   2512 C  CD2 . HIS C 1 43  ? -40.859 89.469  -1.115  1.00 94.06  ? 43   HIS C CD2 1 
ATOM   2513 C  CE1 . HIS C 1 43  ? -40.797 91.389  -2.174  1.00 94.76  ? 43   HIS C CE1 1 
ATOM   2514 N  NE2 . HIS C 1 43  ? -41.315 90.765  -1.132  1.00 92.72  ? 43   HIS C NE2 1 
ATOM   2515 N  N   . GLY C 1 44  ? -38.740 85.821  -4.888  1.00 83.06  ? 44   GLY C N   1 
ATOM   2516 C  CA  . GLY C 1 44  ? -37.832 84.770  -5.320  1.00 82.28  ? 44   GLY C CA  1 
ATOM   2517 C  C   . GLY C 1 44  ? -36.580 84.716  -4.456  1.00 83.76  ? 44   GLY C C   1 
ATOM   2518 O  O   . GLY C 1 44  ? -36.260 85.691  -3.778  1.00 86.02  ? 44   GLY C O   1 
ATOM   2519 N  N   . PHE C 1 45  ? -35.872 83.588  -4.469  1.00 78.34  ? 45   PHE C N   1 
ATOM   2520 C  CA  . PHE C 1 45  ? -34.656 83.441  -3.668  1.00 75.78  ? 45   PHE C CA  1 
ATOM   2521 C  C   . PHE C 1 45  ? -33.775 82.330  -4.209  1.00 75.21  ? 45   PHE C C   1 
ATOM   2522 O  O   . PHE C 1 45  ? -33.950 81.166  -3.860  1.00 76.95  ? 45   PHE C O   1 
ATOM   2523 C  CB  . PHE C 1 45  ? -35.001 83.159  -2.200  1.00 79.23  ? 45   PHE C CB  1 
ATOM   2524 C  CG  . PHE C 1 45  ? -33.797 83.062  -1.296  1.00 76.74  ? 45   PHE C CG  1 
ATOM   2525 C  CD1 . PHE C 1 45  ? -33.361 84.165  -0.578  1.00 77.13  ? 45   PHE C CD1 1 
ATOM   2526 C  CD2 . PHE C 1 45  ? -33.101 81.870  -1.163  1.00 73.37  ? 45   PHE C CD2 1 
ATOM   2527 C  CE1 . PHE C 1 45  ? -32.255 84.077  0.261   1.00 71.26  ? 45   PHE C CE1 1 
ATOM   2528 C  CE2 . PHE C 1 45  ? -31.994 81.779  -0.330  1.00 69.56  ? 45   PHE C CE2 1 
ATOM   2529 C  CZ  . PHE C 1 45  ? -31.572 82.884  0.382   1.00 67.07  ? 45   PHE C CZ  1 
ATOM   2530 N  N   . HIS C 1 46  ? -32.815 82.692  -5.050  1.00 78.26  ? 46   HIS C N   1 
ATOM   2531 C  CA  . HIS C 1 46  ? -31.991 81.702  -5.730  1.00 78.11  ? 46   HIS C CA  1 
ATOM   2532 C  C   . HIS C 1 46  ? -30.526 82.102  -5.718  1.00 72.88  ? 46   HIS C C   1 
ATOM   2533 O  O   . HIS C 1 46  ? -30.191 83.251  -5.439  1.00 69.95  ? 46   HIS C O   1 
ATOM   2534 C  CB  . HIS C 1 46  ? -32.461 81.545  -7.174  1.00 78.16  ? 46   HIS C CB  1 
ATOM   2535 C  CG  . HIS C 1 46  ? -33.769 82.213  -7.455  1.00 82.70  ? 46   HIS C CG  1 
ATOM   2536 N  ND1 . HIS C 1 46  ? -34.943 81.512  -7.629  1.00 85.63  ? 46   HIS C ND1 1 
ATOM   2537 C  CD2 . HIS C 1 46  ? -34.093 83.523  -7.577  1.00 80.79  ? 46   HIS C CD2 1 
ATOM   2538 C  CE1 . HIS C 1 46  ? -35.932 82.359  -7.854  1.00 82.56  ? 46   HIS C CE1 1 
ATOM   2539 N  NE2 . HIS C 1 46  ? -35.443 83.585  -7.827  1.00 81.53  ? 46   HIS C NE2 1 
ATOM   2540 N  N   . VAL C 1 47  ? -29.660 81.140  -6.021  1.00 66.59  ? 47   VAL C N   1 
ATOM   2541 C  CA  . VAL C 1 47  ? -28.235 81.390  -6.147  1.00 63.80  ? 47   VAL C CA  1 
ATOM   2542 C  C   . VAL C 1 47  ? -27.890 81.508  -7.623  1.00 72.48  ? 47   VAL C C   1 
ATOM   2543 O  O   . VAL C 1 47  ? -28.004 80.532  -8.371  1.00 74.63  ? 47   VAL C O   1 
ATOM   2544 C  CB  . VAL C 1 47  ? -27.407 80.235  -5.554  1.00 62.39  ? 47   VAL C CB  1 
ATOM   2545 C  CG1 . VAL C 1 47  ? -25.939 80.356  -5.951  1.00 59.66  ? 47   VAL C CG1 1 
ATOM   2546 C  CG2 . VAL C 1 47  ? -27.555 80.198  -4.053  1.00 66.48  ? 47   VAL C CG2 1 
ATOM   2547 N  N   . HIS C 1 48  ? -27.473 82.695  -8.051  1.00 69.73  ? 48   HIS C N   1 
ATOM   2548 C  CA  . HIS C 1 48  ? -27.077 82.878  -9.440  1.00 64.08  ? 48   HIS C CA  1 
ATOM   2549 C  C   . HIS C 1 48  ? -25.630 82.454  -9.668  1.00 62.33  ? 48   HIS C C   1 
ATOM   2550 O  O   . HIS C 1 48  ? -24.910 82.131  -8.723  1.00 62.36  ? 48   HIS C O   1 
ATOM   2551 C  CB  . HIS C 1 48  ? -27.372 84.296  -9.895  1.00 60.87  ? 48   HIS C CB  1 
ATOM   2552 C  CG  . HIS C 1 48  ? -28.803 84.685  -9.702  1.00 70.00  ? 48   HIS C CG  1 
ATOM   2553 N  ND1 . HIS C 1 48  ? -29.562 85.269  -10.694 1.00 73.81  ? 48   HIS C ND1 1 
ATOM   2554 C  CD2 . HIS C 1 48  ? -29.625 84.543  -8.635  1.00 72.24  ? 48   HIS C CD2 1 
ATOM   2555 C  CE1 . HIS C 1 48  ? -30.783 85.491  -10.239 1.00 72.89  ? 48   HIS C CE1 1 
ATOM   2556 N  NE2 . HIS C 1 48  ? -30.848 85.058  -8.993  1.00 77.22  ? 48   HIS C NE2 1 
ATOM   2557 N  N   . GLN C 1 49  ? -25.222 82.432  -10.928 1.00 65.82  ? 49   GLN C N   1 
ATOM   2558 C  CA  . GLN C 1 49  ? -24.029 81.693  -11.339 1.00 64.69  ? 49   GLN C CA  1 
ATOM   2559 C  C   . GLN C 1 49  ? -22.675 82.329  -11.045 1.00 63.29  ? 49   GLN C C   1 
ATOM   2560 O  O   . GLN C 1 49  ? -21.725 81.638  -10.656 1.00 57.16  ? 49   GLN C O   1 
ATOM   2561 C  CB  . GLN C 1 49  ? -24.097 81.402  -12.834 1.00 60.85  ? 49   GLN C CB  1 
ATOM   2562 C  CG  . GLN C 1 49  ? -22.895 80.640  -13.348 1.00 61.28  ? 49   GLN C CG  1 
ATOM   2563 C  CD  . GLN C 1 49  ? -22.911 80.501  -14.853 1.00 64.31  ? 49   GLN C CD  1 
ATOM   2564 O  OE1 . GLN C 1 49  ? -23.687 81.172  -15.538 1.00 70.25  ? 49   GLN C OE1 1 
ATOM   2565 N  NE2 . GLN C 1 49  ? -22.054 79.634  -15.381 1.00 58.02  ? 49   GLN C NE2 1 
ATOM   2566 N  N   . TYR C 1 50  ? -22.568 83.631  -11.287 1.00 62.25  ? 50   TYR C N   1 
ATOM   2567 C  CA  . TYR C 1 50  ? -21.266 84.295  -11.237 1.00 62.20  ? 50   TYR C CA  1 
ATOM   2568 C  C   . TYR C 1 50  ? -21.144 85.230  -10.039 1.00 57.09  ? 50   TYR C C   1 
ATOM   2569 O  O   . TYR C 1 50  ? -22.063 85.995  -9.730  1.00 58.66  ? 50   TYR C O   1 
ATOM   2570 C  CB  . TYR C 1 50  ? -20.973 85.037  -12.554 1.00 61.27  ? 50   TYR C CB  1 
ATOM   2571 C  CG  . TYR C 1 50  ? -20.548 84.135  -13.705 1.00 60.52  ? 50   TYR C CG  1 
ATOM   2572 C  CD1 . TYR C 1 50  ? -19.291 83.540  -13.711 1.00 60.06  ? 50   TYR C CD1 1 
ATOM   2573 C  CD2 . TYR C 1 50  ? -21.399 83.891  -14.796 1.00 62.18  ? 50   TYR C CD2 1 
ATOM   2574 C  CE1 . TYR C 1 50  ? -18.879 82.713  -14.757 1.00 60.82  ? 50   TYR C CE1 1 
ATOM   2575 C  CE2 . TYR C 1 50  ? -21.002 83.062  -15.851 1.00 57.13  ? 50   TYR C CE2 1 
ATOM   2576 C  CZ  . TYR C 1 50  ? -19.732 82.475  -15.826 1.00 63.82  ? 50   TYR C CZ  1 
ATOM   2577 O  OH  . TYR C 1 50  ? -19.296 81.646  -16.854 1.00 56.84  ? 50   TYR C OH  1 
ATOM   2578 N  N   . GLY C 1 51  ? -20.014 85.146  -9.350  1.00 50.61  ? 51   GLY C N   1 
ATOM   2579 C  CA  . GLY C 1 51  ? -19.773 86.009  -8.208  1.00 58.50  ? 51   GLY C CA  1 
ATOM   2580 C  C   . GLY C 1 51  ? -19.170 87.315  -8.689  1.00 58.00  ? 51   GLY C C   1 
ATOM   2581 O  O   . GLY C 1 51  ? -18.007 87.622  -8.397  1.00 55.38  ? 51   GLY C O   1 
ATOM   2582 N  N   . ASP C 1 52  ? -19.977 88.072  -9.427  1.00 54.65  ? 52   ASP C N   1 
ATOM   2583 C  CA  . ASP C 1 52  ? -19.520 89.240  -10.168 1.00 58.21  ? 52   ASP C CA  1 
ATOM   2584 C  C   . ASP C 1 52  ? -20.559 90.345  -10.076 1.00 58.47  ? 52   ASP C C   1 
ATOM   2585 O  O   . ASP C 1 52  ? -21.656 90.234  -10.608 1.00 53.85  ? 52   ASP C O   1 
ATOM   2586 C  CB  . ASP C 1 52  ? -19.284 88.863  -11.635 1.00 57.94  ? 52   ASP C CB  1 
ATOM   2587 C  CG  . ASP C 1 52  ? -18.944 90.067  -12.518 1.00 56.24  ? 52   ASP C CG  1 
ATOM   2588 O  OD1 . ASP C 1 52  ? -19.708 91.059  -12.524 1.00 54.44  ? 52   ASP C OD1 1 
ATOM   2589 O  OD2 . ASP C 1 52  ? -17.923 89.996  -13.237 1.00 47.33  ? 52   ASP C OD2 1 
ATOM   2590 N  N   . ASN C 1 53  ? -20.210 91.421  -9.391  1.00 60.47  ? 53   ASN C N   1 
ATOM   2591 C  CA  . ASN C 1 53  ? -21.140 92.523  -9.251  1.00 59.12  ? 53   ASN C CA  1 
ATOM   2592 C  C   . ASN C 1 53  ? -20.591 93.815  -9.843  1.00 56.87  ? 53   ASN C C   1 
ATOM   2593 O  O   . ASN C 1 53  ? -21.006 94.902  -9.459  1.00 54.73  ? 53   ASN C O   1 
ATOM   2594 C  CB  . ASN C 1 53  ? -21.572 92.683  -7.791  1.00 61.14  ? 53   ASN C CB  1 
ATOM   2595 C  CG  . ASN C 1 53  ? -22.472 91.531  -7.319  1.00 72.06  ? 53   ASN C CG  1 
ATOM   2596 O  OD1 . ASN C 1 53  ? -23.255 90.976  -8.107  1.00 73.62  ? 53   ASN C OD1 1 
ATOM   2597 N  ND2 . ASN C 1 53  ? -22.362 91.167  -6.034  1.00 60.51  ? 53   ASN C ND2 1 
ATOM   2598 N  N   . THR C 1 54  ? -19.667 93.679  -10.794 1.00 54.54  ? 54   THR C N   1 
ATOM   2599 C  CA  . THR C 1 54  ? -19.181 94.822  -11.573 1.00 57.56  ? 54   THR C CA  1 
ATOM   2600 C  C   . THR C 1 54  ? -20.336 95.604  -12.205 1.00 56.12  ? 54   THR C C   1 
ATOM   2601 O  O   . THR C 1 54  ? -20.190 96.778  -12.526 1.00 54.59  ? 54   THR C O   1 
ATOM   2602 C  CB  . THR C 1 54  ? -18.223 94.391  -12.685 1.00 49.78  ? 54   THR C CB  1 
ATOM   2603 O  OG1 . THR C 1 54  ? -18.932 93.576  -13.622 1.00 58.36  ? 54   THR C OG1 1 
ATOM   2604 C  CG2 . THR C 1 54  ? -17.058 93.599  -12.123 1.00 47.95  ? 54   THR C CG2 1 
ATOM   2605 N  N   . GLN C 1 55  ? -21.482 94.954  -12.379 1.00 60.69  ? 55   GLN C N   1 
ATOM   2606 C  CA  . GLN C 1 55  ? -22.678 95.655  -12.833 1.00 65.18  ? 55   GLN C CA  1 
ATOM   2607 C  C   . GLN C 1 55  ? -23.862 95.368  -11.926 1.00 70.13  ? 55   GLN C C   1 
ATOM   2608 O  O   . GLN C 1 55  ? -24.955 95.039  -12.391 1.00 72.34  ? 55   GLN C O   1 
ATOM   2609 C  CB  . GLN C 1 55  ? -23.008 95.287  -14.274 1.00 72.05  ? 55   GLN C CB  1 
ATOM   2610 C  CG  . GLN C 1 55  ? -21.894 95.627  -15.250 1.00 73.78  ? 55   GLN C CG  1 
ATOM   2611 C  CD  . GLN C 1 55  ? -22.175 95.104  -16.636 1.00 79.70  ? 55   GLN C CD  1 
ATOM   2612 O  OE1 . GLN C 1 55  ? -21.615 94.087  -17.049 1.00 79.96  ? 55   GLN C OE1 1 
ATOM   2613 N  NE2 . GLN C 1 55  ? -23.060 95.789  -17.364 1.00 84.48  ? 55   GLN C NE2 1 
ATOM   2614 N  N   . GLY C 1 56  ? -23.640 95.512  -10.623 1.00 68.04  ? 56   GLY C N   1 
ATOM   2615 C  CA  . GLY C 1 56  ? -24.673 95.226  -9.649  1.00 71.63  ? 56   GLY C CA  1 
ATOM   2616 C  C   . GLY C 1 56  ? -25.066 93.771  -9.761  1.00 71.04  ? 56   GLY C C   1 
ATOM   2617 O  O   . GLY C 1 56  ? -24.229 92.912  -10.051 1.00 66.23  ? 56   GLY C O   1 
ATOM   2618 N  N   . CYS C 1 57  ? -26.345 93.490  -9.550  1.00 71.78  ? 57   CYS C N   1 
ATOM   2619 C  CA  . CYS C 1 57  ? -26.813 92.115  -9.612  1.00 72.71  ? 57   CYS C CA  1 
ATOM   2620 C  C   . CYS C 1 57  ? -26.801 91.570  -11.032 1.00 68.69  ? 57   CYS C C   1 
ATOM   2621 O  O   . CYS C 1 57  ? -26.443 90.415  -11.255 1.00 65.12  ? 57   CYS C O   1 
ATOM   2622 C  CB  . CYS C 1 57  ? -28.201 91.986  -8.988  1.00 71.29  ? 57   CYS C CB  1 
ATOM   2623 S  SG  . CYS C 1 57  ? -28.186 92.259  -7.208  1.00 77.43  ? 57   CYS C SG  1 
ATOM   2624 N  N   . THR C 1 58  ? -27.164 92.406  -11.996 1.00 71.35  ? 58   THR C N   1 
ATOM   2625 C  CA  . THR C 1 58  ? -27.348 91.910  -13.353 1.00 68.06  ? 58   THR C CA  1 
ATOM   2626 C  C   . THR C 1 58  ? -26.169 91.066  -13.834 1.00 69.01  ? 58   THR C C   1 
ATOM   2627 O  O   . THR C 1 58  ? -26.363 90.117  -14.594 1.00 69.31  ? 58   THR C O   1 
ATOM   2628 C  CB  . THR C 1 58  ? -27.675 93.032  -14.365 1.00 68.81  ? 58   THR C CB  1 
ATOM   2629 O  OG1 . THR C 1 58  ? -26.489 93.766  -14.688 1.00 78.32  ? 58   THR C OG1 1 
ATOM   2630 C  CG2 . THR C 1 58  ? -28.733 93.972  -13.801 1.00 68.62  ? 58   THR C CG2 1 
ATOM   2631 N  N   . SER C 1 59  ? -24.959 91.392  -13.380 1.00 68.35  ? 59   SER C N   1 
ATOM   2632 C  CA  . SER C 1 59  ? -23.753 90.687  -13.844 1.00 68.45  ? 59   SER C CA  1 
ATOM   2633 C  C   . SER C 1 59  ? -23.534 89.338  -13.153 1.00 62.29  ? 59   SER C C   1 
ATOM   2634 O  O   . SER C 1 59  ? -22.566 88.624  -13.441 1.00 54.82  ? 59   SER C O   1 
ATOM   2635 C  CB  . SER C 1 59  ? -22.498 91.577  -13.749 1.00 66.10  ? 59   SER C CB  1 
ATOM   2636 O  OG  . SER C 1 59  ? -22.470 92.328  -12.541 1.00 66.25  ? 59   SER C OG  1 
ATOM   2637 N  N   . ALA C 1 60  ? -24.446 88.992  -12.247 1.00 67.73  ? 60   ALA C N   1 
ATOM   2638 C  CA  . ALA C 1 60  ? -24.425 87.678  -11.596 1.00 71.30  ? 60   ALA C CA  1 
ATOM   2639 C  C   . ALA C 1 60  ? -24.595 86.567  -12.637 1.00 71.86  ? 60   ALA C C   1 
ATOM   2640 O  O   . ALA C 1 60  ? -23.774 85.647  -12.734 1.00 68.03  ? 60   ALA C O   1 
ATOM   2641 C  CB  . ALA C 1 60  ? -25.516 87.589  -10.533 1.00 66.71  ? 60   ALA C CB  1 
ATOM   2642 N  N   . GLY C 1 61  ? -25.662 86.669  -13.422 1.00 68.70  ? 61   GLY C N   1 
ATOM   2643 C  CA  . GLY C 1 61  ? -25.882 85.741  -14.509 1.00 70.99  ? 61   GLY C CA  1 
ATOM   2644 C  C   . GLY C 1 61  ? -27.109 84.893  -14.288 1.00 69.95  ? 61   GLY C C   1 
ATOM   2645 O  O   . GLY C 1 61  ? -28.051 85.321  -13.616 1.00 66.01  ? 61   GLY C O   1 
ATOM   2646 N  N   . PRO C 1 62  ? -27.094 83.676  -14.849 1.00 76.31  ? 62   PRO C N   1 
ATOM   2647 C  CA  . PRO C 1 62  ? -28.210 82.722  -14.840 1.00 77.73  ? 62   PRO C CA  1 
ATOM   2648 C  C   . PRO C 1 62  ? -28.207 81.938  -13.535 1.00 74.95  ? 62   PRO C C   1 
ATOM   2649 O  O   . PRO C 1 62  ? -27.117 81.716  -12.998 1.00 72.30  ? 62   PRO C O   1 
ATOM   2650 C  CB  . PRO C 1 62  ? -27.860 81.765  -15.993 1.00 72.33  ? 62   PRO C CB  1 
ATOM   2651 C  CG  . PRO C 1 62  ? -26.463 82.184  -16.494 1.00 69.01  ? 62   PRO C CG  1 
ATOM   2652 C  CD  . PRO C 1 62  ? -25.889 83.091  -15.458 1.00 68.50  ? 62   PRO C CD  1 
ATOM   2653 N  N   . HIS C 1 63  ? -29.372 81.529  -13.034 1.00 72.67  ? 63   HIS C N   1 
ATOM   2654 C  CA  . HIS C 1 63  ? -29.393 80.664  -11.861 1.00 76.02  ? 63   HIS C CA  1 
ATOM   2655 C  C   . HIS C 1 63  ? -28.255 79.662  -12.007 1.00 73.12  ? 63   HIS C C   1 
ATOM   2656 O  O   . HIS C 1 63  ? -27.993 79.175  -13.102 1.00 72.18  ? 63   HIS C O   1 
ATOM   2657 C  CB  . HIS C 1 63  ? -30.727 79.928  -11.726 1.00 77.88  ? 63   HIS C CB  1 
ATOM   2658 C  CG  . HIS C 1 63  ? -31.849 80.782  -11.218 1.00 82.31  ? 63   HIS C CG  1 
ATOM   2659 N  ND1 . HIS C 1 63  ? -33.078 80.846  -11.840 1.00 87.37  ? 63   HIS C ND1 1 
ATOM   2660 C  CD2 . HIS C 1 63  ? -31.931 81.601  -10.143 1.00 82.11  ? 63   HIS C CD2 1 
ATOM   2661 C  CE1 . HIS C 1 63  ? -33.868 81.668  -11.172 1.00 85.53  ? 63   HIS C CE1 1 
ATOM   2662 N  NE2 . HIS C 1 63  ? -33.196 82.141  -10.138 1.00 81.34  ? 63   HIS C NE2 1 
ATOM   2663 N  N   . PHE C 1 64  ? -27.549 79.380  -10.918 1.00 70.38  ? 64   PHE C N   1 
ATOM   2664 C  CA  . PHE C 1 64  ? -26.480 78.396  -10.981 1.00 69.45  ? 64   PHE C CA  1 
ATOM   2665 C  C   . PHE C 1 64  ? -27.109 77.116  -11.519 1.00 78.45  ? 64   PHE C C   1 
ATOM   2666 O  O   . PHE C 1 64  ? -28.068 76.603  -10.940 1.00 77.84  ? 64   PHE C O   1 
ATOM   2667 C  CB  . PHE C 1 64  ? -25.872 78.176  -9.594  1.00 61.35  ? 64   PHE C CB  1 
ATOM   2668 C  CG  . PHE C 1 64  ? -24.590 77.390  -9.605  1.00 59.51  ? 64   PHE C CG  1 
ATOM   2669 C  CD1 . PHE C 1 64  ? -23.784 77.368  -10.723 1.00 61.23  ? 64   PHE C CD1 1 
ATOM   2670 C  CD2 . PHE C 1 64  ? -24.181 76.686  -8.482  1.00 61.16  ? 64   PHE C CD2 1 
ATOM   2671 C  CE1 . PHE C 1 64  ? -22.591 76.645  -10.725 1.00 62.59  ? 64   PHE C CE1 1 
ATOM   2672 C  CE2 . PHE C 1 64  ? -22.999 75.959  -8.478  1.00 59.28  ? 64   PHE C CE2 1 
ATOM   2673 C  CZ  . PHE C 1 64  ? -22.200 75.940  -9.598  1.00 60.68  ? 64   PHE C CZ  1 
ATOM   2674 N  N   . ASN C 1 65  ? -26.608 76.616  -12.645 1.00 80.14  ? 65   ASN C N   1 
ATOM   2675 C  CA  . ASN C 1 65  ? -27.225 75.442  -13.259 1.00 80.83  ? 65   ASN C CA  1 
ATOM   2676 C  C   . ASN C 1 65  ? -26.323 74.680  -14.230 1.00 81.47  ? 65   ASN C C   1 
ATOM   2677 O  O   . ASN C 1 65  ? -26.631 74.593  -15.419 1.00 83.32  ? 65   ASN C O   1 
ATOM   2678 C  CB  . ASN C 1 65  ? -28.525 75.848  -13.959 1.00 79.82  ? 65   ASN C CB  1 
ATOM   2679 C  CG  . ASN C 1 65  ? -29.462 74.682  -14.168 1.00 83.93  ? 65   ASN C CG  1 
ATOM   2680 O  OD1 . ASN C 1 65  ? -29.489 73.741  -13.375 1.00 84.87  ? 65   ASN C OD1 1 
ATOM   2681 N  ND2 . ASN C 1 65  ? -30.241 74.739  -15.236 1.00 83.64  ? 65   ASN C ND2 1 
ATOM   2682 N  N   . PRO C 1 66  ? -25.217 74.109  -13.717 1.00 79.09  ? 66   PRO C N   1 
ATOM   2683 C  CA  . PRO C 1 66  ? -24.220 73.388  -14.524 1.00 82.76  ? 66   PRO C CA  1 
ATOM   2684 C  C   . PRO C 1 66  ? -24.776 72.130  -15.203 1.00 89.20  ? 66   PRO C C   1 
ATOM   2685 O  O   . PRO C 1 66  ? -24.086 71.530  -16.028 1.00 90.07  ? 66   PRO C O   1 
ATOM   2686 C  CB  . PRO C 1 66  ? -23.150 72.984  -13.494 1.00 78.16  ? 66   PRO C CB  1 
ATOM   2687 C  CG  . PRO C 1 66  ? -23.367 73.858  -12.330 1.00 71.81  ? 66   PRO C CG  1 
ATOM   2688 C  CD  . PRO C 1 66  ? -24.842 74.144  -12.294 1.00 73.02  ? 66   PRO C CD  1 
ATOM   2689 N  N   . HIS C 1 67  ? -25.995 71.728  -14.850 1.00 89.15  ? 67   HIS C N   1 
ATOM   2690 C  CA  . HIS C 1 67  ? -26.598 70.538  -15.442 1.00 90.79  ? 67   HIS C CA  1 
ATOM   2691 C  C   . HIS C 1 67  ? -27.436 70.915  -16.644 1.00 89.21  ? 67   HIS C C   1 
ATOM   2692 O  O   . HIS C 1 67  ? -27.927 70.054  -17.368 1.00 81.67  ? 67   HIS C O   1 
ATOM   2693 C  CB  . HIS C 1 67  ? -27.463 69.812  -14.420 1.00 92.20  ? 67   HIS C CB  1 
ATOM   2694 C  CG  . HIS C 1 67  ? -26.699 69.323  -13.234 1.00 92.35  ? 67   HIS C CG  1 
ATOM   2695 N  ND1 . HIS C 1 67  ? -25.554 68.563  -13.352 1.00 88.66  ? 67   HIS C ND1 1 
ATOM   2696 C  CD2 . HIS C 1 67  ? -26.913 69.481  -11.907 1.00 90.31  ? 67   HIS C CD2 1 
ATOM   2697 C  CE1 . HIS C 1 67  ? -25.094 68.275  -12.148 1.00 91.33  ? 67   HIS C CE1 1 
ATOM   2698 N  NE2 . HIS C 1 67  ? -25.900 68.820  -11.254 1.00 97.04  ? 67   HIS C NE2 1 
ATOM   2699 N  N   . SER C 1 68  ? -27.603 72.218  -16.835 1.00 92.99  ? 68   SER C N   1 
ATOM   2700 C  CA  . SER C 1 68  ? -28.348 72.754  -17.967 1.00 93.35  ? 68   SER C CA  1 
ATOM   2701 C  C   . SER C 1 68  ? -29.836 72.449  -17.850 1.00 90.21  ? 68   SER C C   1 
ATOM   2702 O  O   . SER C 1 68  ? -30.598 72.666  -18.790 1.00 89.65  ? 68   SER C O   1 
ATOM   2703 C  CB  . SER C 1 68  ? -27.783 72.209  -19.277 1.00 87.74  ? 68   SER C CB  1 
ATOM   2704 O  OG  . SER C 1 68  ? -26.374 72.368  -19.299 1.00 92.71  ? 68   SER C OG  1 
ATOM   2705 N  N   . LYS C 1 69  ? -30.240 71.958  -16.682 1.00 85.91  ? 69   LYS C N   1 
ATOM   2706 C  CA  . LYS C 1 69  ? -31.637 71.646  -16.416 1.00 89.55  ? 69   LYS C CA  1 
ATOM   2707 C  C   . LYS C 1 69  ? -32.523 72.897  -16.515 1.00 91.24  ? 69   LYS C C   1 
ATOM   2708 O  O   . LYS C 1 69  ? -32.162 73.867  -17.185 1.00 90.42  ? 69   LYS C O   1 
ATOM   2709 C  CB  . LYS C 1 69  ? -31.765 70.973  -15.049 1.00 92.51  ? 69   LYS C CB  1 
ATOM   2710 C  CG  . LYS C 1 69  ? -30.667 69.934  -14.788 1.00 91.42  ? 69   LYS C CG  1 
ATOM   2711 C  CD  . LYS C 1 69  ? -31.153 68.782  -13.909 1.00 94.15  ? 69   LYS C CD  1 
ATOM   2712 C  CE  . LYS C 1 69  ? -31.599 69.258  -12.532 1.00 93.43  ? 69   LYS C CE  1 
ATOM   2713 N  NZ  . LYS C 1 69  ? -32.414 68.229  -11.828 1.00 80.69  ? 69   LYS C NZ  1 
ATOM   2714 N  N   . LYS C 1 70  ? -33.683 72.877  -15.865 1.00 91.11  ? 70   LYS C N   1 
ATOM   2715 C  CA  . LYS C 1 70  ? -34.615 74.003  -15.973 1.00 95.40  ? 70   LYS C CA  1 
ATOM   2716 C  C   . LYS C 1 70  ? -35.155 74.463  -14.625 1.00 93.68  ? 70   LYS C C   1 
ATOM   2717 O  O   . LYS C 1 70  ? -34.746 73.958  -13.580 1.00 91.49  ? 70   LYS C O   1 
ATOM   2718 C  CB  . LYS C 1 70  ? -35.782 73.675  -16.910 1.00 99.94  ? 70   LYS C CB  1 
ATOM   2719 C  CG  . LYS C 1 70  ? -35.419 73.645  -18.378 1.00 98.72  ? 70   LYS C CG  1 
ATOM   2720 C  CD  . LYS C 1 70  ? -36.656 73.441  -19.238 1.00 101.53 ? 70   LYS C CD  1 
ATOM   2721 C  CE  . LYS C 1 70  ? -36.306 73.474  -20.717 1.00 105.39 ? 70   LYS C CE  1 
ATOM   2722 N  NZ  . LYS C 1 70  ? -35.661 74.759  -21.110 1.00 98.72  ? 70   LYS C NZ  1 
ATOM   2723 N  N   . HIS C 1 71  ? -36.097 75.405  -14.670 1.00 93.48  ? 71   HIS C N   1 
ATOM   2724 C  CA  . HIS C 1 71  ? -36.542 76.126  -13.478 1.00 93.60  ? 71   HIS C CA  1 
ATOM   2725 C  C   . HIS C 1 71  ? -37.758 75.516  -12.774 1.00 95.75  ? 71   HIS C C   1 
ATOM   2726 O  O   . HIS C 1 71  ? -38.887 75.601  -13.268 1.00 95.54  ? 71   HIS C O   1 
ATOM   2727 C  CB  . HIS C 1 71  ? -36.824 77.594  -13.823 1.00 94.95  ? 71   HIS C CB  1 
ATOM   2728 C  CG  . HIS C 1 71  ? -37.110 78.451  -12.629 1.00 93.86  ? 71   HIS C CG  1 
ATOM   2729 N  ND1 . HIS C 1 71  ? -36.123 79.130  -11.945 1.00 93.02  ? 71   HIS C ND1 1 
ATOM   2730 C  CD2 . HIS C 1 71  ? -38.270 78.734  -11.993 1.00 91.46  ? 71   HIS C CD2 1 
ATOM   2731 C  CE1 . HIS C 1 71  ? -36.664 79.793  -10.940 1.00 90.02  ? 71   HIS C CE1 1 
ATOM   2732 N  NE2 . HIS C 1 71  ? -37.966 79.569  -10.946 1.00 89.80  ? 71   HIS C NE2 1 
ATOM   2733 N  N   . GLY C 1 72  ? -37.516 74.917  -11.608 1.00 96.53  ? 72   GLY C N   1 
ATOM   2734 C  CA  . GLY C 1 72  ? -38.577 74.396  -10.761 1.00 92.05  ? 72   GLY C CA  1 
ATOM   2735 C  C   . GLY C 1 72  ? -38.434 74.893  -9.331  1.00 92.22  ? 72   GLY C C   1 
ATOM   2736 O  O   . GLY C 1 72  ? -37.741 75.878  -9.077  1.00 90.47  ? 72   GLY C O   1 
ATOM   2737 N  N   . GLY C 1 73  ? -39.090 74.213  -8.395  1.00 93.08  ? 73   GLY C N   1 
ATOM   2738 C  CA  . GLY C 1 73  ? -38.940 74.513  -6.980  1.00 90.59  ? 73   GLY C CA  1 
ATOM   2739 C  C   . GLY C 1 73  ? -37.793 73.767  -6.304  1.00 88.84  ? 73   GLY C C   1 
ATOM   2740 O  O   . GLY C 1 73  ? -37.056 73.013  -6.951  1.00 85.24  ? 73   GLY C O   1 
ATOM   2741 N  N   . PRO C 1 74  ? -37.631 73.982  -4.988  1.00 86.43  ? 74   PRO C N   1 
ATOM   2742 C  CA  . PRO C 1 74  ? -36.578 73.363  -4.168  1.00 86.60  ? 74   PRO C CA  1 
ATOM   2743 C  C   . PRO C 1 74  ? -36.701 71.837  -4.074  1.00 89.82  ? 74   PRO C C   1 
ATOM   2744 O  O   . PRO C 1 74  ? -35.701 71.122  -4.210  1.00 86.94  ? 74   PRO C O   1 
ATOM   2745 C  CB  . PRO C 1 74  ? -36.795 73.991  -2.784  1.00 83.20  ? 74   PRO C CB  1 
ATOM   2746 C  CG  . PRO C 1 74  ? -37.556 75.255  -3.046  1.00 81.96  ? 74   PRO C CG  1 
ATOM   2747 C  CD  . PRO C 1 74  ? -38.425 74.964  -4.227  1.00 82.41  ? 74   PRO C CD  1 
ATOM   2748 N  N   . ALA C 1 75  ? -37.915 71.351  -3.830  1.00 87.37  ? 75   ALA C N   1 
ATOM   2749 C  CA  . ALA C 1 75  ? -38.162 69.919  -3.724  1.00 85.12  ? 75   ALA C CA  1 
ATOM   2750 C  C   . ALA C 1 75  ? -38.083 69.264  -5.099  1.00 87.85  ? 75   ALA C C   1 
ATOM   2751 O  O   . ALA C 1 75  ? -37.445 68.222  -5.266  1.00 87.71  ? 75   ALA C O   1 
ATOM   2752 C  CB  . ALA C 1 75  ? -39.519 69.665  -3.089  1.00 80.55  ? 75   ALA C CB  1 
ATOM   2753 N  N   . ASP C 1 76  ? -38.726 69.900  -6.077  1.00 89.92  ? 76   ASP C N   1 
ATOM   2754 C  CA  . ASP C 1 76  ? -38.790 69.402  -7.453  1.00 90.09  ? 76   ASP C CA  1 
ATOM   2755 C  C   . ASP C 1 76  ? -37.464 68.790  -7.899  1.00 88.87  ? 76   ASP C C   1 
ATOM   2756 O  O   . ASP C 1 76  ? -36.392 69.326  -7.617  1.00 91.37  ? 76   ASP C O   1 
ATOM   2757 C  CB  . ASP C 1 76  ? -39.222 70.522  -8.415  1.00 90.02  ? 76   ASP C CB  1 
ATOM   2758 C  CG  . ASP C 1 76  ? -40.556 71.167  -8.019  1.00 91.11  ? 76   ASP C CG  1 
ATOM   2759 O  OD1 . ASP C 1 76  ? -41.301 70.569  -7.213  1.00 89.45  ? 76   ASP C OD1 1 
ATOM   2760 O  OD2 . ASP C 1 76  ? -40.866 72.275  -8.515  1.00 90.38  ? 76   ASP C OD2 1 
ATOM   2761 N  N   . GLU C 1 77  ? -37.537 67.656  -8.583  1.00 87.74  ? 77   GLU C N   1 
ATOM   2762 C  CA  . GLU C 1 77  ? -36.324 66.992  -9.033  1.00 93.16  ? 77   GLU C CA  1 
ATOM   2763 C  C   . GLU C 1 77  ? -35.671 67.816  -10.147 1.00 96.69  ? 77   GLU C C   1 
ATOM   2764 O  O   . GLU C 1 77  ? -34.455 67.755  -10.362 1.00 97.31  ? 77   GLU C O   1 
ATOM   2765 C  CB  . GLU C 1 77  ? -36.623 65.557  -9.493  1.00 93.74  ? 77   GLU C CB  1 
ATOM   2766 C  CG  . GLU C 1 77  ? -37.275 64.653  -8.423  1.00 96.06  ? 77   GLU C CG  1 
ATOM   2767 C  CD  . GLU C 1 77  ? -36.339 64.298  -7.252  1.00 91.44  ? 77   GLU C CD  1 
ATOM   2768 O  OE1 . GLU C 1 77  ? -36.535 63.222  -6.627  1.00 76.65  ? 77   GLU C OE1 1 
ATOM   2769 O  OE2 . GLU C 1 77  ? -35.410 65.092  -6.960  1.00 87.97  ? 77   GLU C OE2 1 
ATOM   2770 N  N   . GLU C 1 78  ? -36.487 68.601  -10.846 1.00 96.08  ? 78   GLU C N   1 
ATOM   2771 C  CA  . GLU C 1 78  ? -35.992 69.442  -11.930 1.00 94.97  ? 78   GLU C CA  1 
ATOM   2772 C  C   . GLU C 1 78  ? -35.918 70.902  -11.495 1.00 94.28  ? 78   GLU C C   1 
ATOM   2773 O  O   . GLU C 1 78  ? -36.944 71.553  -11.267 1.00 92.84  ? 78   GLU C O   1 
ATOM   2774 C  CB  . GLU C 1 78  ? -36.876 69.300  -13.167 1.00 93.21  ? 78   GLU C CB  1 
ATOM   2775 C  CG  . GLU C 1 78  ? -36.313 69.963  -14.411 1.00 98.68  ? 78   GLU C CG  1 
ATOM   2776 C  CD  . GLU C 1 78  ? -35.078 69.258  -14.953 1.00 101.75 ? 78   GLU C CD  1 
ATOM   2777 O  OE1 . GLU C 1 78  ? -34.469 68.447  -14.213 1.00 98.47  ? 78   GLU C OE1 1 
ATOM   2778 O  OE2 . GLU C 1 78  ? -34.720 69.522  -16.125 1.00 102.01 ? 78   GLU C OE2 1 
ATOM   2779 N  N   . ARG C 1 79  ? -34.695 71.408  -11.386 1.00 91.31  ? 79   ARG C N   1 
ATOM   2780 C  CA  . ARG C 1 79  ? -34.458 72.737  -10.846 1.00 86.85  ? 79   ARG C CA  1 
ATOM   2781 C  C   . ARG C 1 79  ? -33.006 73.139  -11.062 1.00 86.01  ? 79   ARG C C   1 
ATOM   2782 O  O   . ARG C 1 79  ? -32.128 72.286  -11.248 1.00 84.24  ? 79   ARG C O   1 
ATOM   2783 C  CB  . ARG C 1 79  ? -34.787 72.768  -9.349  1.00 84.63  ? 79   ARG C CB  1 
ATOM   2784 C  CG  . ARG C 1 79  ? -34.218 71.576  -8.575  1.00 89.91  ? 79   ARG C CG  1 
ATOM   2785 C  CD  . ARG C 1 79  ? -34.223 71.784  -7.063  1.00 84.18  ? 79   ARG C CD  1 
ATOM   2786 N  NE  . ARG C 1 79  ? -33.117 72.635  -6.635  1.00 82.99  ? 79   ARG C NE  1 
ATOM   2787 C  CZ  . ARG C 1 79  ? -32.778 72.855  -5.369  1.00 80.08  ? 79   ARG C CZ  1 
ATOM   2788 N  NH1 . ARG C 1 79  ? -33.455 72.277  -4.384  1.00 83.10  ? 79   ARG C NH1 1 
ATOM   2789 N  NH2 . ARG C 1 79  ? -31.754 73.652  -5.087  1.00 76.11  ? 79   ARG C NH2 1 
ATOM   2790 N  N   . HIS C 1 80  ? -32.757 74.444  -11.046 1.00 87.04  ? 80   HIS C N   1 
ATOM   2791 C  CA  . HIS C 1 80  ? -31.395 74.935  -11.080 1.00 82.42  ? 80   HIS C CA  1 
ATOM   2792 C  C   . HIS C 1 80  ? -30.806 74.665  -9.714  1.00 80.59  ? 80   HIS C C   1 
ATOM   2793 O  O   . HIS C 1 80  ? -31.478 74.866  -8.703  1.00 74.35  ? 80   HIS C O   1 
ATOM   2794 C  CB  . HIS C 1 80  ? -31.375 76.420  -11.399 1.00 73.32  ? 80   HIS C CB  1 
ATOM   2795 C  CG  . HIS C 1 80  ? -31.959 76.740  -12.734 1.00 83.89  ? 80   HIS C CG  1 
ATOM   2796 N  ND1 . HIS C 1 80  ? -32.420 77.994  -13.070 1.00 88.63  ? 80   HIS C ND1 1 
ATOM   2797 C  CD2 . HIS C 1 80  ? -32.173 75.958  -13.817 1.00 88.54  ? 80   HIS C CD2 1 
ATOM   2798 C  CE1 . HIS C 1 80  ? -32.889 77.973  -14.305 1.00 90.84  ? 80   HIS C CE1 1 
ATOM   2799 N  NE2 . HIS C 1 80  ? -32.747 76.750  -14.783 1.00 92.94  ? 80   HIS C NE2 1 
ATOM   2800 N  N   . VAL C 1 81  ? -29.570 74.171  -9.684  1.00 75.77  ? 81   VAL C N   1 
ATOM   2801 C  CA  . VAL C 1 81  ? -28.881 73.962  -8.420  1.00 74.54  ? 81   VAL C CA  1 
ATOM   2802 C  C   . VAL C 1 81  ? -29.220 75.111  -7.474  1.00 73.92  ? 81   VAL C C   1 
ATOM   2803 O  O   . VAL C 1 81  ? -29.621 74.902  -6.334  1.00 72.57  ? 81   VAL C O   1 
ATOM   2804 C  CB  . VAL C 1 81  ? -27.364 73.900  -8.607  1.00 73.81  ? 81   VAL C CB  1 
ATOM   2805 C  CG1 . VAL C 1 81  ? -26.680 73.646  -7.271  1.00 74.62  ? 81   VAL C CG1 1 
ATOM   2806 C  CG2 . VAL C 1 81  ? -27.003 72.824  -9.611  1.00 77.80  ? 81   VAL C CG2 1 
ATOM   2807 N  N   . GLY C 1 82  ? -29.081 76.331  -7.974  1.00 74.77  ? 82   GLY C N   1 
ATOM   2808 C  CA  . GLY C 1 82  ? -29.384 77.514  -7.193  1.00 74.23  ? 82   GLY C CA  1 
ATOM   2809 C  C   . GLY C 1 82  ? -30.851 77.888  -7.225  1.00 78.40  ? 82   GLY C C   1 
ATOM   2810 O  O   . GLY C 1 82  ? -31.203 79.073  -7.244  1.00 76.94  ? 82   GLY C O   1 
ATOM   2811 N  N   . ASP C 1 83  ? -31.713 76.877  -7.225  1.00 79.09  ? 83   ASP C N   1 
ATOM   2812 C  CA  . ASP C 1 83  ? -33.151 77.114  -7.194  1.00 81.63  ? 83   ASP C CA  1 
ATOM   2813 C  C   . ASP C 1 83  ? -33.697 76.792  -5.806  1.00 79.03  ? 83   ASP C C   1 
ATOM   2814 O  O   . ASP C 1 83  ? -33.989 75.639  -5.495  1.00 78.76  ? 83   ASP C O   1 
ATOM   2815 C  CB  . ASP C 1 83  ? -33.856 76.274  -8.263  1.00 84.05  ? 83   ASP C CB  1 
ATOM   2816 C  CG  . ASP C 1 83  ? -34.915 77.056  -9.017  1.00 85.61  ? 83   ASP C CG  1 
ATOM   2817 O  OD1 . ASP C 1 83  ? -35.377 76.557  -10.069 1.00 82.81  ? 83   ASP C OD1 1 
ATOM   2818 O  OD2 . ASP C 1 83  ? -35.278 78.166  -8.560  1.00 81.91  ? 83   ASP C OD2 1 
ATOM   2819 N  N   . LEU C 1 84  ? -33.829 77.826  -4.980  1.00 82.23  ? 84   LEU C N   1 
ATOM   2820 C  CA  . LEU C 1 84  ? -34.223 77.666  -3.581  1.00 78.48  ? 84   LEU C CA  1 
ATOM   2821 C  C   . LEU C 1 84  ? -35.599 78.266  -3.349  1.00 74.07  ? 84   LEU C C   1 
ATOM   2822 O  O   . LEU C 1 84  ? -35.900 78.805  -2.286  1.00 75.13  ? 84   LEU C O   1 
ATOM   2823 C  CB  . LEU C 1 84  ? -33.190 78.321  -2.670  1.00 73.46  ? 84   LEU C CB  1 
ATOM   2824 C  CG  . LEU C 1 84  ? -31.750 77.991  -3.071  1.00 74.39  ? 84   LEU C CG  1 
ATOM   2825 C  CD1 . LEU C 1 84  ? -30.764 78.844  -2.301  1.00 71.32  ? 84   LEU C CD1 1 
ATOM   2826 C  CD2 . LEU C 1 84  ? -31.449 76.504  -2.888  1.00 71.54  ? 84   LEU C CD2 1 
ATOM   2827 N  N   . GLY C 1 85  ? -36.427 78.170  -4.376  1.00 76.96  ? 85   GLY C N   1 
ATOM   2828 C  CA  . GLY C 1 85  ? -37.813 78.562  -4.281  1.00 78.92  ? 85   GLY C CA  1 
ATOM   2829 C  C   . GLY C 1 85  ? -38.004 79.959  -3.760  1.00 77.29  ? 85   GLY C C   1 
ATOM   2830 O  O   . GLY C 1 85  ? -37.701 80.936  -4.438  1.00 80.35  ? 85   GLY C O   1 
ATOM   2831 N  N   . ASN C 1 86  ? -38.502 80.056  -2.539  1.00 75.54  ? 86   ASN C N   1 
ATOM   2832 C  CA  . ASN C 1 86  ? -38.966 81.333  -2.043  1.00 83.24  ? 86   ASN C CA  1 
ATOM   2833 C  C   . ASN C 1 86  ? -38.580 81.610  -0.605  1.00 84.74  ? 86   ASN C C   1 
ATOM   2834 O  O   . ASN C 1 86  ? -37.919 80.800  0.052   1.00 85.73  ? 86   ASN C O   1 
ATOM   2835 C  CB  . ASN C 1 86  ? -40.493 81.410  -2.169  1.00 89.21  ? 86   ASN C CB  1 
ATOM   2836 C  CG  . ASN C 1 86  ? -40.950 82.380  -3.242  1.00 88.57  ? 86   ASN C CG  1 
ATOM   2837 O  OD1 . ASN C 1 86  ? -41.037 82.026  -4.421  1.00 87.91  ? 86   ASN C OD1 1 
ATOM   2838 N  ND2 . ASN C 1 86  ? -41.258 83.610  -2.837  1.00 84.89  ? 86   ASN C ND2 1 
ATOM   2839 N  N   . VAL C 1 87  ? -39.018 82.778  -0.143  1.00 82.40  ? 87   VAL C N   1 
ATOM   2840 C  CA  . VAL C 1 87  ? -38.913 83.213  1.238   1.00 87.04  ? 87   VAL C CA  1 
ATOM   2841 C  C   . VAL C 1 87  ? -40.066 84.194  1.409   1.00 85.21  ? 87   VAL C C   1 
ATOM   2842 O  O   . VAL C 1 87  ? -40.495 84.799  0.431   1.00 86.34  ? 87   VAL C O   1 
ATOM   2843 C  CB  . VAL C 1 87  ? -37.582 83.948  1.499   1.00 87.25  ? 87   VAL C CB  1 
ATOM   2844 C  CG1 . VAL C 1 87  ? -37.477 84.350  2.966   1.00 84.96  ? 87   VAL C CG1 1 
ATOM   2845 C  CG2 . VAL C 1 87  ? -36.390 83.087  1.083   1.00 79.70  ? 87   VAL C CG2 1 
ATOM   2846 N  N   . THR C 1 88  ? -40.578 84.364  2.624   1.00 83.14  ? 88   THR C N   1 
ATOM   2847 C  CA  . THR C 1 88  ? -41.745 85.231  2.803   1.00 88.12  ? 88   THR C CA  1 
ATOM   2848 C  C   . THR C 1 88  ? -41.544 86.369  3.796   1.00 83.54  ? 88   THR C C   1 
ATOM   2849 O  O   . THR C 1 88  ? -41.046 86.162  4.902   1.00 85.50  ? 88   THR C O   1 
ATOM   2850 C  CB  . THR C 1 88  ? -42.998 84.430  3.205   1.00 93.64  ? 88   THR C CB  1 
ATOM   2851 O  OG1 . THR C 1 88  ? -43.192 83.353  2.279   1.00 95.41  ? 88   THR C OG1 1 
ATOM   2852 C  CG2 . THR C 1 88  ? -44.236 85.329  3.205   1.00 90.47  ? 88   THR C CG2 1 
ATOM   2853 N  N   . ALA C 1 89  ? -41.957 87.567  3.389   1.00 86.11  ? 89   ALA C N   1 
ATOM   2854 C  CA  . ALA C 1 89  ? -41.797 88.772  4.200   1.00 91.57  ? 89   ALA C CA  1 
ATOM   2855 C  C   . ALA C 1 89  ? -43.088 89.141  4.928   1.00 90.27  ? 89   ALA C C   1 
ATOM   2856 O  O   . ALA C 1 89  ? -44.156 89.186  4.320   1.00 90.95  ? 89   ALA C O   1 
ATOM   2857 C  CB  . ALA C 1 89  ? -41.321 89.937  3.333   1.00 91.81  ? 89   ALA C CB  1 
ATOM   2858 N  N   . ASP C 1 90  ? -42.977 89.409  6.228   1.00 91.32  ? 90   ASP C N   1 
ATOM   2859 C  CA  . ASP C 1 90  ? -44.141 89.703  7.066   1.00 94.99  ? 90   ASP C CA  1 
ATOM   2860 C  C   . ASP C 1 90  ? -44.818 91.010  6.673   1.00 95.76  ? 90   ASP C C   1 
ATOM   2861 O  O   . ASP C 1 90  ? -44.730 91.442  5.520   1.00 95.57  ? 90   ASP C O   1 
ATOM   2862 C  CB  . ASP C 1 90  ? -43.759 89.724  8.553   1.00 95.32  ? 90   ASP C CB  1 
ATOM   2863 C  CG  . ASP C 1 90  ? -42.733 90.798  8.883   1.00 98.47  ? 90   ASP C CG  1 
ATOM   2864 O  OD1 . ASP C 1 90  ? -42.463 91.646  8.005   1.00 96.47  ? 90   ASP C OD1 1 
ATOM   2865 O  OD2 . ASP C 1 90  ? -42.198 90.794  10.019  1.00 95.94  ? 90   ASP C OD2 1 
ATOM   2866 N  N   . LYS C 1 91  ? -45.499 91.634  7.630   1.00 94.92  ? 91   LYS C N   1 
ATOM   2867 C  CA  . LYS C 1 91  ? -46.168 92.905  7.371   1.00 100.20 ? 91   LYS C CA  1 
ATOM   2868 C  C   . LYS C 1 91  ? -45.194 94.060  7.541   1.00 100.14 ? 91   LYS C C   1 
ATOM   2869 O  O   . LYS C 1 91  ? -45.384 95.133  6.970   1.00 102.80 ? 91   LYS C O   1 
ATOM   2870 C  CB  . LYS C 1 91  ? -47.391 93.091  8.274   1.00 100.28 ? 91   LYS C CB  1 
ATOM   2871 C  CG  . LYS C 1 91  ? -47.085 93.103  9.756   1.00 101.07 ? 91   LYS C CG  1 
ATOM   2872 C  CD  . LYS C 1 91  ? -48.360 93.236  10.573  1.00 99.38  ? 91   LYS C CD  1 
ATOM   2873 C  CE  . LYS C 1 91  ? -48.072 93.091  12.059  1.00 101.13 ? 91   LYS C CE  1 
ATOM   2874 N  NZ  . LYS C 1 91  ? -47.017 94.045  12.513  1.00 98.92  ? 91   LYS C NZ  1 
ATOM   2875 N  N   . ASP C 1 92  ? -44.146 93.824  8.324   1.00 100.33 ? 92   ASP C N   1 
ATOM   2876 C  CA  . ASP C 1 92  ? -43.077 94.802  8.508   1.00 100.69 ? 92   ASP C CA  1 
ATOM   2877 C  C   . ASP C 1 92  ? -41.888 94.552  7.570   1.00 99.05  ? 92   ASP C C   1 
ATOM   2878 O  O   . ASP C 1 92  ? -40.738 94.774  7.951   1.00 102.70 ? 92   ASP C O   1 
ATOM   2879 C  CB  . ASP C 1 92  ? -42.605 94.816  9.967   1.00 96.72  ? 92   ASP C CB  1 
ATOM   2880 C  CG  . ASP C 1 92  ? -43.587 95.513  10.893  1.00 103.02 ? 92   ASP C CG  1 
ATOM   2881 O  OD1 . ASP C 1 92  ? -44.425 96.294  10.392  1.00 104.86 ? 92   ASP C OD1 1 
ATOM   2882 O  OD2 . ASP C 1 92  ? -43.519 95.287  12.123  1.00 98.46  ? 92   ASP C OD2 1 
ATOM   2883 N  N   . GLY C 1 93  ? -42.168 94.080  6.356   1.00 96.12  ? 93   GLY C N   1 
ATOM   2884 C  CA  . GLY C 1 93  ? -41.148 93.896  5.333   1.00 93.62  ? 93   GLY C CA  1 
ATOM   2885 C  C   . GLY C 1 93  ? -40.075 92.843  5.585   1.00 93.50  ? 93   GLY C C   1 
ATOM   2886 O  O   . GLY C 1 93  ? -39.257 92.558  4.704   1.00 91.60  ? 93   GLY C O   1 
ATOM   2887 N  N   . VAL C 1 94  ? -40.079 92.252  6.778   1.00 93.08  ? 94   VAL C N   1 
ATOM   2888 C  CA  . VAL C 1 94  ? -39.028 91.318  7.188   1.00 90.50  ? 94   VAL C CA  1 
ATOM   2889 C  C   . VAL C 1 94  ? -39.285 89.868  6.755   1.00 86.20  ? 94   VAL C C   1 
ATOM   2890 O  O   . VAL C 1 94  ? -40.373 89.331  6.954   1.00 87.01  ? 94   VAL C O   1 
ATOM   2891 C  CB  . VAL C 1 94  ? -38.814 91.369  8.715   1.00 86.68  ? 94   VAL C CB  1 
ATOM   2892 C  CG1 . VAL C 1 94  ? -37.686 90.446  9.127   1.00 82.95  ? 94   VAL C CG1 1 
ATOM   2893 C  CG2 . VAL C 1 94  ? -38.522 92.790  9.151   1.00 87.40  ? 94   VAL C CG2 1 
ATOM   2894 N  N   . ALA C 1 95  ? -38.268 89.240  6.173   1.00 81.96  ? 95   ALA C N   1 
ATOM   2895 C  CA  . ALA C 1 95  ? -38.374 87.865  5.689   1.00 82.33  ? 95   ALA C CA  1 
ATOM   2896 C  C   . ALA C 1 95  ? -37.367 86.934  6.360   1.00 79.11  ? 95   ALA C C   1 
ATOM   2897 O  O   . ALA C 1 95  ? -36.253 86.756  5.871   1.00 77.80  ? 95   ALA C O   1 
ATOM   2898 C  CB  . ALA C 1 95  ? -38.194 87.821  4.178   1.00 81.33  ? 95   ALA C CB  1 
ATOM   2899 N  N   . ASP C 1 96  ? -37.760 86.332  7.476   1.00 80.58  ? 96   ASP C N   1 
ATOM   2900 C  CA  . ASP C 1 96  ? -36.882 85.389  8.159   1.00 79.06  ? 96   ASP C CA  1 
ATOM   2901 C  C   . ASP C 1 96  ? -36.551 84.204  7.260   1.00 78.57  ? 96   ASP C C   1 
ATOM   2902 O  O   . ASP C 1 96  ? -37.411 83.680  6.548   1.00 81.66  ? 96   ASP C O   1 
ATOM   2903 C  CB  . ASP C 1 96  ? -37.491 84.926  9.482   1.00 76.73  ? 96   ASP C CB  1 
ATOM   2904 C  CG  . ASP C 1 96  ? -37.673 86.068  10.462  1.00 81.99  ? 96   ASP C CG  1 
ATOM   2905 O  OD1 . ASP C 1 96  ? -36.655 86.666  10.872  1.00 85.13  ? 96   ASP C OD1 1 
ATOM   2906 O  OD2 . ASP C 1 96  ? -38.832 86.377  10.814  1.00 82.37  ? 96   ASP C OD2 1 
ATOM   2907 N  N   . VAL C 1 97  ? -35.290 83.797  7.295   1.00 74.10  ? 97   VAL C N   1 
ATOM   2908 C  CA  . VAL C 1 97  ? -34.790 82.762  6.414   1.00 73.89  ? 97   VAL C CA  1 
ATOM   2909 C  C   . VAL C 1 97  ? -34.241 81.599  7.208   1.00 71.25  ? 97   VAL C C   1 
ATOM   2910 O  O   . VAL C 1 97  ? -33.245 81.733  7.909   1.00 73.79  ? 97   VAL C O   1 
ATOM   2911 C  CB  . VAL C 1 97  ? -33.658 83.301  5.514   1.00 75.32  ? 97   VAL C CB  1 
ATOM   2912 C  CG1 . VAL C 1 97  ? -32.831 82.153  4.934   1.00 69.45  ? 97   VAL C CG1 1 
ATOM   2913 C  CG2 . VAL C 1 97  ? -34.224 84.194  4.414   1.00 75.73  ? 97   VAL C CG2 1 
ATOM   2914 N  N   . SER C 1 98  ? -34.899 80.456  7.104   1.00 75.06  ? 98   SER C N   1 
ATOM   2915 C  CA  . SER C 1 98  ? -34.354 79.227  7.651   1.00 75.72  ? 98   SER C CA  1 
ATOM   2916 C  C   . SER C 1 98  ? -34.536 78.158  6.595   1.00 75.82  ? 98   SER C C   1 
ATOM   2917 O  O   . SER C 1 98  ? -35.663 77.857  6.199   1.00 80.58  ? 98   SER C O   1 
ATOM   2918 C  CB  . SER C 1 98  ? -35.063 78.838  8.945   1.00 78.15  ? 98   SER C CB  1 
ATOM   2919 O  OG  . SER C 1 98  ? -34.310 77.862  9.643   1.00 84.93  ? 98   SER C OG  1 
ATOM   2920 N  N   . ILE C 1 99  ? -33.428 77.598  6.126   1.00 72.57  ? 99   ILE C N   1 
ATOM   2921 C  CA  . ILE C 1 99  ? -33.464 76.755  4.942   1.00 68.69  ? 99   ILE C CA  1 
ATOM   2922 C  C   . ILE C 1 99  ? -32.356 75.711  4.915   1.00 65.82  ? 99   ILE C C   1 
ATOM   2923 O  O   . ILE C 1 99  ? -31.185 76.011  5.118   1.00 64.08  ? 99   ILE C O   1 
ATOM   2924 C  CB  . ILE C 1 99  ? -33.410 77.618  3.641   1.00 70.85  ? 99   ILE C CB  1 
ATOM   2925 C  CG1 . ILE C 1 99  ? -34.766 78.295  3.384   1.00 68.03  ? 99   ILE C CG1 1 
ATOM   2926 C  CG2 . ILE C 1 99  ? -32.961 76.779  2.439   1.00 70.62  ? 99   ILE C CG2 1 
ATOM   2927 C  CD1 . ILE C 1 99  ? -34.823 79.138  2.123   1.00 70.34  ? 99   ILE C CD1 1 
ATOM   2928 N  N   . GLU C 1 100 ? -32.745 74.469  4.670   1.00 71.51  ? 100  GLU C N   1 
ATOM   2929 C  CA  . GLU C 1 100 ? -31.781 73.412  4.418   1.00 73.63  ? 100  GLU C CA  1 
ATOM   2930 C  C   . GLU C 1 100 ? -31.897 73.043  2.951   1.00 72.62  ? 100  GLU C C   1 
ATOM   2931 O  O   . GLU C 1 100 ? -32.973 73.147  2.362   1.00 73.56  ? 100  GLU C O   1 
ATOM   2932 C  CB  . GLU C 1 100 ? -32.063 72.191  5.294   1.00 69.02  ? 100  GLU C CB  1 
ATOM   2933 C  CG  . GLU C 1 100 ? -30.905 71.207  5.376   1.00 70.01  ? 100  GLU C CG  1 
ATOM   2934 C  CD  . GLU C 1 100 ? -31.289 69.919  6.087   1.00 73.02  ? 100  GLU C CD  1 
ATOM   2935 O  OE1 . GLU C 1 100 ? -32.343 69.340  5.740   1.00 68.50  ? 100  GLU C OE1 1 
ATOM   2936 O  OE2 . GLU C 1 100 ? -30.535 69.480  6.986   1.00 78.85  ? 100  GLU C OE2 1 
ATOM   2937 N  N   . ASP C 1 101 ? -30.792 72.622  2.353   1.00 71.20  ? 101  ASP C N   1 
ATOM   2938 C  CA  . ASP C 1 101 ? -30.808 72.289  0.942   1.00 68.88  ? 101  ASP C CA  1 
ATOM   2939 C  C   . ASP C 1 101 ? -29.679 71.321  0.659   1.00 66.54  ? 101  ASP C C   1 
ATOM   2940 O  O   . ASP C 1 101 ? -28.534 71.553  1.043   1.00 63.49  ? 101  ASP C O   1 
ATOM   2941 C  CB  . ASP C 1 101 ? -30.686 73.561  0.091   1.00 74.42  ? 101  ASP C CB  1 
ATOM   2942 C  CG  . ASP C 1 101 ? -31.047 73.333  -1.370  1.00 72.94  ? 101  ASP C CG  1 
ATOM   2943 O  OD1 . ASP C 1 101 ? -32.205 73.627  -1.755  1.00 71.71  ? 101  ASP C OD1 1 
ATOM   2944 O  OD2 . ASP C 1 101 ? -30.168 72.869  -2.129  1.00 68.95  ? 101  ASP C OD2 1 
ATOM   2945 N  N   . SER C 1 102 ? -30.017 70.223  -0.002  1.00 68.06  ? 102  SER C N   1 
ATOM   2946 C  CA  . SER C 1 102 ? -29.048 69.175  -0.280  1.00 69.53  ? 102  SER C CA  1 
ATOM   2947 C  C   . SER C 1 102 ? -28.469 69.288  -1.689  1.00 67.14  ? 102  SER C C   1 
ATOM   2948 O  O   . SER C 1 102 ? -27.506 68.588  -2.028  1.00 61.84  ? 102  SER C O   1 
ATOM   2949 C  CB  . SER C 1 102 ? -29.676 67.795  -0.051  1.00 65.26  ? 102  SER C CB  1 
ATOM   2950 O  OG  . SER C 1 102 ? -31.083 67.850  -0.195  1.00 60.37  ? 102  SER C OG  1 
ATOM   2951 N  N   . VAL C 1 103 ? -29.049 70.178  -2.499  1.00 68.89  ? 103  VAL C N   1 
ATOM   2952 C  CA  . VAL C 1 103 ? -28.588 70.377  -3.879  1.00 72.55  ? 103  VAL C CA  1 
ATOM   2953 C  C   . VAL C 1 103 ? -27.292 71.191  -3.922  1.00 72.70  ? 103  VAL C C   1 
ATOM   2954 O  O   . VAL C 1 103 ? -26.318 70.776  -4.551  1.00 74.93  ? 103  VAL C O   1 
ATOM   2955 C  CB  . VAL C 1 103 ? -29.670 71.038  -4.780  1.00 70.06  ? 103  VAL C CB  1 
ATOM   2956 C  CG1 . VAL C 1 103 ? -29.282 70.934  -6.238  1.00 66.16  ? 103  VAL C CG1 1 
ATOM   2957 C  CG2 . VAL C 1 103 ? -31.012 70.380  -4.563  1.00 69.92  ? 103  VAL C CG2 1 
ATOM   2958 N  N   . ILE C 1 104 ? -27.282 72.340  -3.244  1.00 70.88  ? 104  ILE C N   1 
ATOM   2959 C  CA  . ILE C 1 104 ? -26.092 73.195  -3.165  1.00 69.27  ? 104  ILE C CA  1 
ATOM   2960 C  C   . ILE C 1 104 ? -25.004 72.553  -2.306  1.00 64.04  ? 104  ILE C C   1 
ATOM   2961 O  O   . ILE C 1 104 ? -25.204 71.484  -1.738  1.00 66.33  ? 104  ILE C O   1 
ATOM   2962 C  CB  . ILE C 1 104 ? -26.431 74.578  -2.565  1.00 71.83  ? 104  ILE C CB  1 
ATOM   2963 C  CG1 . ILE C 1 104 ? -26.475 74.498  -1.034  1.00 70.05  ? 104  ILE C CG1 1 
ATOM   2964 C  CG2 . ILE C 1 104 ? -27.750 75.117  -3.133  1.00 69.68  ? 104  ILE C CG2 1 
ATOM   2965 C  CD1 . ILE C 1 104 ? -27.374 75.533  -0.396  1.00 67.76  ? 104  ILE C CD1 1 
ATOM   2966 N  N   . SER C 1 105 ? -23.856 73.214  -2.213  1.00 64.08  ? 105  SER C N   1 
ATOM   2967 C  CA  . SER C 1 105 ? -22.741 72.732  -1.396  1.00 60.68  ? 105  SER C CA  1 
ATOM   2968 C  C   . SER C 1 105 ? -21.709 73.848  -1.187  1.00 60.38  ? 105  SER C C   1 
ATOM   2969 O  O   . SER C 1 105 ? -21.853 74.929  -1.758  1.00 60.82  ? 105  SER C O   1 
ATOM   2970 C  CB  . SER C 1 105 ? -22.106 71.507  -2.045  1.00 58.34  ? 105  SER C CB  1 
ATOM   2971 O  OG  . SER C 1 105 ? -20.829 71.236  -1.508  1.00 62.74  ? 105  SER C OG  1 
ATOM   2972 N  N   . LEU C 1 106 ? -20.692 73.599  -0.361  1.00 57.71  ? 106  LEU C N   1 
ATOM   2973 C  CA  . LEU C 1 106 ? -19.669 74.606  -0.071  1.00 57.77  ? 106  LEU C CA  1 
ATOM   2974 C  C   . LEU C 1 106 ? -18.297 74.094  -0.445  1.00 60.41  ? 106  LEU C C   1 
ATOM   2975 O  O   . LEU C 1 106 ? -17.273 74.671  -0.068  1.00 61.45  ? 106  LEU C O   1 
ATOM   2976 C  CB  . LEU C 1 106 ? -19.670 75.015  1.401   1.00 55.53  ? 106  LEU C CB  1 
ATOM   2977 C  CG  . LEU C 1 106 ? -20.963 75.529  2.038   1.00 58.82  ? 106  LEU C CG  1 
ATOM   2978 C  CD1 . LEU C 1 106 ? -20.660 76.039  3.443   1.00 56.10  ? 106  LEU C CD1 1 
ATOM   2979 C  CD2 . LEU C 1 106 ? -21.638 76.612  1.217   1.00 54.92  ? 106  LEU C CD2 1 
ATOM   2980 N  N   . SER C 1 107 ? -18.290 72.982  -1.165  1.00 66.86  ? 107  SER C N   1 
ATOM   2981 C  CA  . SER C 1 107 ? -17.097 72.508  -1.864  1.00 73.74  ? 107  SER C CA  1 
ATOM   2982 C  C   . SER C 1 107 ? -17.528 71.534  -2.959  1.00 70.78  ? 107  SER C C   1 
ATOM   2983 O  O   . SER C 1 107 ? -18.682 71.078  -2.980  1.00 64.10  ? 107  SER C O   1 
ATOM   2984 C  CB  . SER C 1 107 ? -16.096 71.851  -0.910  1.00 69.06  ? 107  SER C CB  1 
ATOM   2985 O  OG  . SER C 1 107 ? -16.653 70.688  -0.319  1.00 71.79  ? 107  SER C OG  1 
ATOM   2986 N  N   . GLY C 1 108 ? -16.607 71.232  -3.872  1.00 70.22  ? 108  GLY C N   1 
ATOM   2987 C  CA  . GLY C 1 108 ? -16.901 70.334  -4.974  1.00 69.92  ? 108  GLY C CA  1 
ATOM   2988 C  C   . GLY C 1 108 ? -17.681 70.975  -6.110  1.00 72.81  ? 108  GLY C C   1 
ATOM   2989 O  O   . GLY C 1 108 ? -17.812 72.197  -6.201  1.00 73.36  ? 108  GLY C O   1 
ATOM   2990 N  N   . ASP C 1 109 ? -18.220 70.132  -6.977  1.00 71.48  ? 109  ASP C N   1 
ATOM   2991 C  CA  . ASP C 1 109 ? -18.811 70.586  -8.223  1.00 70.21  ? 109  ASP C CA  1 
ATOM   2992 C  C   . ASP C 1 109 ? -20.108 71.399  -8.035  1.00 75.42  ? 109  ASP C C   1 
ATOM   2993 O  O   . ASP C 1 109 ? -20.632 71.977  -8.991  1.00 71.17  ? 109  ASP C O   1 
ATOM   2994 C  CB  . ASP C 1 109 ? -19.007 69.387  -9.161  1.00 72.13  ? 109  ASP C CB  1 
ATOM   2995 C  CG  . ASP C 1 109 ? -17.716 68.573  -9.358  1.00 78.49  ? 109  ASP C CG  1 
ATOM   2996 O  OD1 . ASP C 1 109 ? -16.641 69.003  -8.874  1.00 76.52  ? 109  ASP C OD1 1 
ATOM   2997 O  OD2 . ASP C 1 109 ? -17.774 67.500  -10.000 1.00 75.40  ? 109  ASP C OD2 1 
ATOM   2998 N  N   . HIS C 1 110 ? -20.611 71.465  -6.804  1.00 76.70  ? 110  HIS C N   1 
ATOM   2999 C  CA  . HIS C 1 110 ? -21.783 72.303  -6.504  1.00 75.93  ? 110  HIS C CA  1 
ATOM   3000 C  C   . HIS C 1 110 ? -21.494 73.450  -5.511  1.00 69.97  ? 110  HIS C C   1 
ATOM   3001 O  O   . HIS C 1 110 ? -22.410 74.162  -5.080  1.00 63.15  ? 110  HIS C O   1 
ATOM   3002 C  CB  . HIS C 1 110 ? -22.950 71.443  -6.015  1.00 78.66  ? 110  HIS C CB  1 
ATOM   3003 C  CG  . HIS C 1 110 ? -23.783 70.873  -7.119  1.00 85.02  ? 110  HIS C CG  1 
ATOM   3004 N  ND1 . HIS C 1 110 ? -25.138 71.107  -7.226  1.00 84.90  ? 110  HIS C ND1 1 
ATOM   3005 C  CD2 . HIS C 1 110 ? -23.451 70.090  -8.174  1.00 89.52  ? 110  HIS C CD2 1 
ATOM   3006 C  CE1 . HIS C 1 110 ? -25.607 70.481  -8.292  1.00 87.59  ? 110  HIS C CE1 1 
ATOM   3007 N  NE2 . HIS C 1 110 ? -24.604 69.861  -8.887  1.00 91.80  ? 110  HIS C NE2 1 
ATOM   3008 N  N   . CYS C 1 111 ? -20.215 73.609  -5.166  1.00 69.84  ? 111  CYS C N   1 
ATOM   3009 C  CA  . CYS C 1 111 ? -19.719 74.723  -4.350  1.00 68.58  ? 111  CYS C CA  1 
ATOM   3010 C  C   . CYS C 1 111 ? -20.249 76.073  -4.818  1.00 63.87  ? 111  CYS C C   1 
ATOM   3011 O  O   . CYS C 1 111 ? -19.836 76.566  -5.870  1.00 65.14  ? 111  CYS C O   1 
ATOM   3012 C  CB  . CYS C 1 111 ? -18.190 74.752  -4.407  1.00 66.62  ? 111  CYS C CB  1 
ATOM   3013 S  SG  . CYS C 1 111 ? -17.407 76.024  -3.391  1.00 72.08  ? 111  CYS C SG  1 
ATOM   3014 N  N   . ILE C 1 112 ? -21.151 76.669  -4.038  1.00 57.77  ? 112  ILE C N   1 
ATOM   3015 C  CA  . ILE C 1 112 ? -21.738 77.964  -4.389  1.00 59.77  ? 112  ILE C CA  1 
ATOM   3016 C  C   . ILE C 1 112 ? -20.944 79.112  -3.767  1.00 57.23  ? 112  ILE C C   1 
ATOM   3017 O  O   . ILE C 1 112 ? -21.415 80.256  -3.701  1.00 48.35  ? 112  ILE C O   1 
ATOM   3018 C  CB  . ILE C 1 112 ? -23.212 78.081  -3.945  1.00 62.26  ? 112  ILE C CB  1 
ATOM   3019 C  CG1 . ILE C 1 112 ? -23.308 78.180  -2.419  1.00 62.46  ? 112  ILE C CG1 1 
ATOM   3020 C  CG2 . ILE C 1 112 ? -24.029 76.908  -4.471  1.00 64.66  ? 112  ILE C CG2 1 
ATOM   3021 C  CD1 . ILE C 1 112 ? -24.718 78.457  -1.926  1.00 62.83  ? 112  ILE C CD1 1 
ATOM   3022 N  N   . ILE C 1 113 ? -19.739 78.783  -3.311  1.00 51.92  ? 113  ILE C N   1 
ATOM   3023 C  CA  . ILE C 1 113 ? -18.835 79.755  -2.727  1.00 50.20  ? 113  ILE C CA  1 
ATOM   3024 C  C   . ILE C 1 113 ? -18.072 80.487  -3.821  1.00 56.38  ? 113  ILE C C   1 
ATOM   3025 O  O   . ILE C 1 113 ? -17.496 79.857  -4.711  1.00 57.80  ? 113  ILE C O   1 
ATOM   3026 C  CB  . ILE C 1 113 ? -17.835 79.069  -1.802  1.00 48.30  ? 113  ILE C CB  1 
ATOM   3027 C  CG1 . ILE C 1 113 ? -18.391 79.016  -0.372  1.00 42.16  ? 113  ILE C CG1 1 
ATOM   3028 C  CG2 . ILE C 1 113 ? -16.476 79.761  -1.875  1.00 42.93  ? 113  ILE C CG2 1 
ATOM   3029 C  CD1 . ILE C 1 113 ? -17.513 78.227  0.571   1.00 40.39  ? 113  ILE C CD1 1 
ATOM   3030 N  N   . GLY C 1 114 ? -18.065 81.817  -3.749  1.00 50.87  ? 114  GLY C N   1 
ATOM   3031 C  CA  . GLY C 1 114 ? -17.457 82.627  -4.781  1.00 44.93  ? 114  GLY C CA  1 
ATOM   3032 C  C   . GLY C 1 114 ? -18.504 82.971  -5.816  1.00 49.79  ? 114  GLY C C   1 
ATOM   3033 O  O   . GLY C 1 114 ? -18.178 83.460  -6.890  1.00 53.91  ? 114  GLY C O   1 
ATOM   3034 N  N   . ARG C 1 115 ? -19.767 82.717  -5.489  1.00 48.08  ? 115  ARG C N   1 
ATOM   3035 C  CA  . ARG C 1 115 ? -20.875 83.004  -6.395  1.00 52.90  ? 115  ARG C CA  1 
ATOM   3036 C  C   . ARG C 1 115 ? -21.845 83.917  -5.685  1.00 50.57  ? 115  ARG C C   1 
ATOM   3037 O  O   . ARG C 1 115 ? -21.647 84.237  -4.525  1.00 49.65  ? 115  ARG C O   1 
ATOM   3038 C  CB  . ARG C 1 115 ? -21.615 81.722  -6.806  1.00 57.83  ? 115  ARG C CB  1 
ATOM   3039 C  CG  . ARG C 1 115 ? -20.749 80.621  -7.386  1.00 53.94  ? 115  ARG C CG  1 
ATOM   3040 C  CD  . ARG C 1 115 ? -21.569 79.739  -8.336  1.00 58.29  ? 115  ARG C CD  1 
ATOM   3041 N  NE  . ARG C 1 115 ? -20.813 78.559  -8.744  1.00 61.47  ? 115  ARG C NE  1 
ATOM   3042 C  CZ  . ARG C 1 115 ? -19.950 78.525  -9.755  1.00 63.87  ? 115  ARG C CZ  1 
ATOM   3043 N  NH1 . ARG C 1 115 ? -19.732 79.613  -10.489 1.00 65.36  ? 115  ARG C NH1 1 
ATOM   3044 N  NH2 . ARG C 1 115 ? -19.300 77.399  -10.032 1.00 57.55  ? 115  ARG C NH2 1 
ATOM   3045 N  N   . THR C 1 116 ? -22.915 84.296  -6.372  1.00 52.43  ? 116  THR C N   1 
ATOM   3046 C  CA  . THR C 1 116 ? -23.804 85.348  -5.887  1.00 54.38  ? 116  THR C CA  1 
ATOM   3047 C  C   . THR C 1 116 ? -25.148 84.822  -5.442  1.00 57.90  ? 116  THR C C   1 
ATOM   3048 O  O   . THR C 1 116 ? -25.741 83.977  -6.102  1.00 61.87  ? 116  THR C O   1 
ATOM   3049 C  CB  . THR C 1 116 ? -24.060 86.416  -6.976  1.00 57.90  ? 116  THR C CB  1 
ATOM   3050 O  OG1 . THR C 1 116 ? -22.824 87.050  -7.333  1.00 61.46  ? 116  THR C OG1 1 
ATOM   3051 C  CG2 . THR C 1 116 ? -25.040 87.459  -6.478  1.00 55.43  ? 116  THR C CG2 1 
ATOM   3052 N  N   . LEU C 1 117 ? -25.629 85.346  -4.322  1.00 58.46  ? 117  LEU C N   1 
ATOM   3053 C  CA  . LEU C 1 117 ? -26.930 84.992  -3.787  1.00 60.82  ? 117  LEU C CA  1 
ATOM   3054 C  C   . LEU C 1 117 ? -27.892 86.138  -4.079  1.00 60.78  ? 117  LEU C C   1 
ATOM   3055 O  O   . LEU C 1 117 ? -27.591 87.282  -3.770  1.00 63.06  ? 117  LEU C O   1 
ATOM   3056 C  CB  . LEU C 1 117 ? -26.812 84.757  -2.276  1.00 61.95  ? 117  LEU C CB  1 
ATOM   3057 C  CG  . LEU C 1 117 ? -28.062 84.324  -1.502  1.00 65.39  ? 117  LEU C CG  1 
ATOM   3058 C  CD1 . LEU C 1 117 ? -28.361 82.853  -1.748  1.00 67.29  ? 117  LEU C CD1 1 
ATOM   3059 C  CD2 . LEU C 1 117 ? -27.886 84.581  -0.024  1.00 61.29  ? 117  LEU C CD2 1 
ATOM   3060 N  N   . VAL C 1 118 ? -29.043 85.839  -4.674  1.00 65.60  ? 118  VAL C N   1 
ATOM   3061 C  CA  . VAL C 1 118 ? -29.988 86.888  -5.070  1.00 68.40  ? 118  VAL C CA  1 
ATOM   3062 C  C   . VAL C 1 118 ? -31.414 86.686  -4.561  1.00 74.23  ? 118  VAL C C   1 
ATOM   3063 O  O   . VAL C 1 118 ? -31.962 85.584  -4.615  1.00 74.32  ? 118  VAL C O   1 
ATOM   3064 C  CB  . VAL C 1 118 ? -30.072 87.030  -6.609  1.00 72.45  ? 118  VAL C CB  1 
ATOM   3065 C  CG1 . VAL C 1 118 ? -31.159 88.032  -6.995  1.00 71.90  ? 118  VAL C CG1 1 
ATOM   3066 C  CG2 . VAL C 1 118 ? -28.731 87.438  -7.187  1.00 68.85  ? 118  VAL C CG2 1 
ATOM   3067 N  N   . VAL C 1 119 ? -32.010 87.770  -4.079  1.00 75.00  ? 119  VAL C N   1 
ATOM   3068 C  CA  . VAL C 1 119 ? -33.426 87.799  -3.752  1.00 78.27  ? 119  VAL C CA  1 
ATOM   3069 C  C   . VAL C 1 119 ? -34.135 88.649  -4.810  1.00 83.73  ? 119  VAL C C   1 
ATOM   3070 O  O   . VAL C 1 119 ? -33.540 89.586  -5.353  1.00 81.17  ? 119  VAL C O   1 
ATOM   3071 C  CB  . VAL C 1 119 ? -33.667 88.387  -2.349  1.00 78.32  ? 119  VAL C CB  1 
ATOM   3072 C  CG1 . VAL C 1 119 ? -33.151 89.812  -2.277  1.00 79.20  ? 119  VAL C CG1 1 
ATOM   3073 C  CG2 . VAL C 1 119 ? -35.146 88.332  -1.990  1.00 81.72  ? 119  VAL C CG2 1 
ATOM   3074 N  N   . HIS C 1 120 ? -35.394 88.326  -5.111  1.00 86.29  ? 120  HIS C N   1 
ATOM   3075 C  CA  . HIS C 1 120 ? -36.094 88.976  -6.223  1.00 84.33  ? 120  HIS C CA  1 
ATOM   3076 C  C   . HIS C 1 120 ? -37.345 89.769  -5.846  1.00 88.60  ? 120  HIS C C   1 
ATOM   3077 O  O   . HIS C 1 120 ? -37.775 89.782  -4.689  1.00 89.12  ? 120  HIS C O   1 
ATOM   3078 C  CB  . HIS C 1 120 ? -36.414 87.965  -7.321  1.00 81.19  ? 120  HIS C CB  1 
ATOM   3079 C  CG  . HIS C 1 120 ? -35.201 87.425  -8.010  1.00 79.61  ? 120  HIS C CG  1 
ATOM   3080 N  ND1 . HIS C 1 120 ? -34.783 87.875  -9.243  1.00 81.73  ? 120  HIS C ND1 1 
ATOM   3081 C  CD2 . HIS C 1 120 ? -34.309 86.478  -7.632  1.00 80.08  ? 120  HIS C CD2 1 
ATOM   3082 C  CE1 . HIS C 1 120 ? -33.689 87.224  -9.600  1.00 80.75  ? 120  HIS C CE1 1 
ATOM   3083 N  NE2 . HIS C 1 120 ? -33.380 86.370  -8.640  1.00 79.72  ? 120  HIS C NE2 1 
ATOM   3084 N  N   . GLU C 1 121 ? -37.916 90.425  -6.851  1.00 88.50  ? 121  GLU C N   1 
ATOM   3085 C  CA  . GLU C 1 121 ? -39.020 91.362  -6.669  1.00 92.07  ? 121  GLU C CA  1 
ATOM   3086 C  C   . GLU C 1 121 ? -40.335 90.686  -6.285  1.00 94.38  ? 121  GLU C C   1 
ATOM   3087 O  O   . GLU C 1 121 ? -40.940 91.012  -5.259  1.00 90.66  ? 121  GLU C O   1 
ATOM   3088 C  CB  . GLU C 1 121 ? -39.221 92.155  -7.956  1.00 92.07  ? 121  GLU C CB  1 
ATOM   3089 C  CG  . GLU C 1 121 ? -40.264 93.245  -7.868  1.00 93.95  ? 121  GLU C CG  1 
ATOM   3090 C  CD  . GLU C 1 121 ? -40.588 93.821  -9.230  1.00 99.27  ? 121  GLU C CD  1 
ATOM   3091 O  OE1 . GLU C 1 121 ? -40.735 93.024  -10.186 1.00 97.05  ? 121  GLU C OE1 1 
ATOM   3092 O  OE2 . GLU C 1 121 ? -40.691 95.064  -9.346  1.00 103.55 ? 121  GLU C OE2 1 
ATOM   3093 N  N   . LYS C 1 122 ? -40.773 89.756  -7.131  1.00 96.47  ? 122  LYS C N   1 
ATOM   3094 C  CA  . LYS C 1 122 ? -42.029 89.031  -6.936  1.00 96.89  ? 122  LYS C CA  1 
ATOM   3095 C  C   . LYS C 1 122 ? -41.787 87.549  -6.620  1.00 92.63  ? 122  LYS C C   1 
ATOM   3096 O  O   . LYS C 1 122 ? -40.648 87.067  -6.644  1.00 87.34  ? 122  LYS C O   1 
ATOM   3097 C  CB  . LYS C 1 122 ? -42.930 89.182  -8.172  1.00 94.75  ? 122  LYS C CB  1 
ATOM   3098 C  CG  . LYS C 1 122 ? -43.393 90.615  -8.433  1.00 95.80  ? 122  LYS C CG  1 
ATOM   3099 C  CD  . LYS C 1 122 ? -43.824 90.829  -9.880  1.00 95.41  ? 122  LYS C CD  1 
ATOM   3100 C  CE  . LYS C 1 122 ? -42.637 90.759  -10.837 1.00 95.60  ? 122  LYS C CE  1 
ATOM   3101 N  NZ  . LYS C 1 122 ? -43.023 91.066  -12.250 1.00 95.43  ? 122  LYS C NZ  1 
ATOM   3102 N  N   . ALA C 1 123 ? -42.866 86.831  -6.324  1.00 92.64  ? 123  ALA C N   1 
ATOM   3103 C  CA  . ALA C 1 123 ? -42.757 85.437  -5.901  1.00 91.54  ? 123  ALA C CA  1 
ATOM   3104 C  C   . ALA C 1 123 ? -42.313 84.516  -7.034  1.00 90.93  ? 123  ALA C C   1 
ATOM   3105 O  O   . ALA C 1 123 ? -42.802 84.625  -8.157  1.00 90.69  ? 123  ALA C O   1 
ATOM   3106 C  CB  . ALA C 1 123 ? -44.077 84.961  -5.315  1.00 86.34  ? 123  ALA C CB  1 
ATOM   3107 N  N   . ASP C 1 124 ? -41.372 83.623  -6.734  1.00 87.50  ? 124  ASP C N   1 
ATOM   3108 C  CA  . ASP C 1 124 ? -40.984 82.565  -7.658  1.00 86.83  ? 124  ASP C CA  1 
ATOM   3109 C  C   . ASP C 1 124 ? -42.212 81.683  -7.857  1.00 91.99  ? 124  ASP C C   1 
ATOM   3110 O  O   . ASP C 1 124 ? -42.945 81.420  -6.901  1.00 90.87  ? 124  ASP C O   1 
ATOM   3111 C  CB  . ASP C 1 124 ? -39.822 81.751  -7.063  1.00 87.23  ? 124  ASP C CB  1 
ATOM   3112 C  CG  . ASP C 1 124 ? -39.311 80.657  -8.001  1.00 87.51  ? 124  ASP C CG  1 
ATOM   3113 O  OD1 . ASP C 1 124 ? -39.864 80.503  -9.106  1.00 90.73  ? 124  ASP C OD1 1 
ATOM   3114 O  OD2 . ASP C 1 124 ? -38.347 79.947  -7.632  1.00 83.52  ? 124  ASP C OD2 1 
ATOM   3115 N  N   . ASP C 1 125 ? -42.457 81.246  -9.092  1.00 94.18  ? 125  ASP C N   1 
ATOM   3116 C  CA  . ASP C 1 125 ? -43.569 80.328  -9.364  1.00 94.00  ? 125  ASP C CA  1 
ATOM   3117 C  C   . ASP C 1 125 ? -43.090 78.894  -9.659  1.00 93.69  ? 125  ASP C C   1 
ATOM   3118 O  O   . ASP C 1 125 ? -43.895 77.995  -9.898  1.00 94.89  ? 125  ASP C O   1 
ATOM   3119 C  CB  . ASP C 1 125 ? -44.512 80.870  -10.460 1.00 91.81  ? 125  ASP C CB  1 
ATOM   3120 C  CG  . ASP C 1 125 ? -43.930 80.758  -11.866 1.00 96.18  ? 125  ASP C CG  1 
ATOM   3121 O  OD1 . ASP C 1 125 ? -42.868 80.122  -12.039 1.00 98.96  ? 125  ASP C OD1 1 
ATOM   3122 O  OD2 . ASP C 1 125 ? -44.547 81.304  -12.806 1.00 92.16  ? 125  ASP C OD2 1 
ATOM   3123 N  N   . LEU C 1 126 ? -41.774 78.701  -9.645  1.00 92.68  ? 126  LEU C N   1 
ATOM   3124 C  CA  . LEU C 1 126 ? -41.169 77.372  -9.659  1.00 92.45  ? 126  LEU C CA  1 
ATOM   3125 C  C   . LEU C 1 126 ? -41.426 76.563  -10.930 1.00 92.92  ? 126  LEU C C   1 
ATOM   3126 O  O   . LEU C 1 126 ? -41.381 75.333  -10.901 1.00 93.45  ? 126  LEU C O   1 
ATOM   3127 C  CB  . LEU C 1 126 ? -41.635 76.574  -8.438  1.00 93.59  ? 126  LEU C CB  1 
ATOM   3128 C  CG  . LEU C 1 126 ? -41.587 77.320  -7.102  1.00 91.83  ? 126  LEU C CG  1 
ATOM   3129 C  CD1 . LEU C 1 126 ? -42.267 76.511  -6.008  1.00 90.99  ? 126  LEU C CD1 1 
ATOM   3130 C  CD2 . LEU C 1 126 ? -40.154 77.660  -6.720  1.00 86.65  ? 126  LEU C CD2 1 
ATOM   3131 N  N   . GLY C 1 127 ? -41.685 77.243  -12.042 1.00 89.93  ? 127  GLY C N   1 
ATOM   3132 C  CA  . GLY C 1 127 ? -41.935 76.551  -13.296 1.00 96.35  ? 127  GLY C CA  1 
ATOM   3133 C  C   . GLY C 1 127 ? -43.409 76.279  -13.544 1.00 92.84  ? 127  GLY C C   1 
ATOM   3134 O  O   . GLY C 1 127 ? -43.774 75.326  -14.236 1.00 88.69  ? 127  GLY C O   1 
ATOM   3135 N  N   . ASN C 1 131 ? -45.823 79.858  -18.681 1.00 109.08 ? 131  ASN C N   1 
ATOM   3136 C  CA  . ASN C 1 131 ? -45.164 80.628  -19.734 1.00 112.90 ? 131  ASN C CA  1 
ATOM   3137 C  C   . ASN C 1 131 ? -43.655 80.377  -19.832 1.00 112.64 ? 131  ASN C C   1 
ATOM   3138 O  O   . ASN C 1 131 ? -43.053 79.782  -18.932 1.00 108.59 ? 131  ASN C O   1 
ATOM   3139 C  CB  . ASN C 1 131 ? -45.457 82.128  -19.582 1.00 112.34 ? 131  ASN C CB  1 
ATOM   3140 C  CG  . ASN C 1 131 ? -45.145 82.653  -18.188 1.00 112.67 ? 131  ASN C CG  1 
ATOM   3141 O  OD1 . ASN C 1 131 ? -44.620 81.930  -17.338 1.00 113.05 ? 131  ASN C OD1 1 
ATOM   3142 N  ND2 . ASN C 1 131 ? -45.472 83.921  -17.947 1.00 106.98 ? 131  ASN C ND2 1 
ATOM   3143 N  N   . GLU C 1 132 ? -43.059 80.833  -20.934 1.00 113.48 ? 132  GLU C N   1 
ATOM   3144 C  CA  . GLU C 1 132 ? -41.632 80.645  -21.199 1.00 108.52 ? 132  GLU C CA  1 
ATOM   3145 C  C   . GLU C 1 132 ? -40.768 81.243  -20.094 1.00 111.75 ? 132  GLU C C   1 
ATOM   3146 O  O   . GLU C 1 132 ? -39.641 80.796  -19.849 1.00 108.62 ? 132  GLU C O   1 
ATOM   3147 C  CB  . GLU C 1 132 ? -41.251 81.267  -22.543 1.00 107.18 ? 132  GLU C CB  1 
ATOM   3148 C  CG  . GLU C 1 132 ? -40.751 80.262  -23.560 1.00 109.93 ? 132  GLU C CG  1 
ATOM   3149 C  CD  . GLU C 1 132 ? -39.601 79.425  -23.031 1.00 113.03 ? 132  GLU C CD  1 
ATOM   3150 O  OE1 . GLU C 1 132 ? -38.431 79.793  -23.284 1.00 114.01 ? 132  GLU C OE1 1 
ATOM   3151 O  OE2 . GLU C 1 132 ? -39.867 78.401  -22.363 1.00 110.93 ? 132  GLU C OE2 1 
ATOM   3152 N  N   . GLU C 1 133 ? -41.303 82.264  -19.432 1.00 112.43 ? 133  GLU C N   1 
ATOM   3153 C  CA  . GLU C 1 133 ? -40.605 82.899  -18.326 1.00 108.84 ? 133  GLU C CA  1 
ATOM   3154 C  C   . GLU C 1 133 ? -40.373 81.880  -17.216 1.00 105.65 ? 133  GLU C C   1 
ATOM   3155 O  O   . GLU C 1 133 ? -39.235 81.536  -16.898 1.00 107.86 ? 133  GLU C O   1 
ATOM   3156 C  CB  . GLU C 1 133 ? -41.405 84.095  -17.804 1.00 105.99 ? 133  GLU C CB  1 
ATOM   3157 C  CG  . GLU C 1 133 ? -40.550 85.147  -17.129 1.00 106.32 ? 133  GLU C CG  1 
ATOM   3158 C  CD  . GLU C 1 133 ? -39.398 85.602  -18.006 1.00 109.13 ? 133  GLU C CD  1 
ATOM   3159 O  OE1 . GLU C 1 133 ? -39.619 85.807  -19.221 1.00 108.83 ? 133  GLU C OE1 1 
ATOM   3160 O  OE2 . GLU C 1 133 ? -38.272 85.750  -17.482 1.00 106.07 ? 133  GLU C OE2 1 
ATOM   3161 N  N   . SER C 1 134 ? -41.461 81.382  -16.645 1.00 102.78 ? 134  SER C N   1 
ATOM   3162 C  CA  . SER C 1 134 ? -41.381 80.415  -15.560 1.00 101.29 ? 134  SER C CA  1 
ATOM   3163 C  C   . SER C 1 134 ? -40.460 79.220  -15.854 1.00 101.24 ? 134  SER C C   1 
ATOM   3164 O  O   . SER C 1 134 ? -40.005 78.545  -14.929 1.00 99.76  ? 134  SER C O   1 
ATOM   3165 C  CB  . SER C 1 134 ? -42.783 79.928  -15.203 1.00 102.82 ? 134  SER C CB  1 
ATOM   3166 O  OG  . SER C 1 134 ? -42.735 78.996  -14.145 1.00 99.88  ? 134  SER C OG  1 
ATOM   3167 N  N   . THR C 1 135 ? -40.184 78.960  -17.131 1.00 99.16  ? 135  THR C N   1 
ATOM   3168 C  CA  . THR C 1 135 ? -39.299 77.861  -17.509 1.00 98.43  ? 135  THR C CA  1 
ATOM   3169 C  C   . THR C 1 135 ? -37.871 78.140  -17.066 1.00 101.40 ? 135  THR C C   1 
ATOM   3170 O  O   . THR C 1 135 ? -37.030 77.236  -17.029 1.00 102.76 ? 135  THR C O   1 
ATOM   3171 C  CB  . THR C 1 135 ? -39.268 77.642  -19.031 1.00 100.82 ? 135  THR C CB  1 
ATOM   3172 O  OG1 . THR C 1 135 ? -39.069 76.252  -19.310 1.00 97.11  ? 135  THR C OG1 1 
ATOM   3173 C  CG2 . THR C 1 135 ? -38.130 78.441  -19.661 1.00 99.27  ? 135  THR C CG2 1 
ATOM   3174 N  N   . LYS C 1 136 ? -37.599 79.399  -16.738 1.00 98.55  ? 136  LYS C N   1 
ATOM   3175 C  CA  . LYS C 1 136 ? -36.236 79.831  -16.448 1.00 101.22 ? 136  LYS C CA  1 
ATOM   3176 C  C   . LYS C 1 136 ? -36.076 80.611  -15.136 1.00 96.61  ? 136  LYS C C   1 
ATOM   3177 O  O   . LYS C 1 136 ? -35.135 80.360  -14.384 1.00 92.63  ? 136  LYS C O   1 
ATOM   3178 C  CB  . LYS C 1 136 ? -35.675 80.631  -17.631 1.00 102.19 ? 136  LYS C CB  1 
ATOM   3179 C  CG  . LYS C 1 136 ? -36.727 81.387  -18.435 1.00 100.28 ? 136  LYS C CG  1 
ATOM   3180 C  CD  . LYS C 1 136 ? -36.087 82.319  -19.457 1.00 98.31  ? 136  LYS C CD  1 
ATOM   3181 C  CE  . LYS C 1 136 ? -37.128 83.181  -20.157 1.00 101.99 ? 136  LYS C CE  1 
ATOM   3182 N  NZ  . LYS C 1 136 ? -36.516 84.229  -21.026 1.00 93.33  ? 136  LYS C NZ  1 
ATOM   3183 N  N   . THR C 1 137 ? -36.991 81.542  -14.865 1.00 96.41  ? 137  THR C N   1 
ATOM   3184 C  CA  . THR C 1 137 ? -36.870 82.441  -13.710 1.00 97.24  ? 137  THR C CA  1 
ATOM   3185 C  C   . THR C 1 137 ? -38.055 82.402  -12.744 1.00 96.47  ? 137  THR C C   1 
ATOM   3186 O  O   . THR C 1 137 ? -38.018 83.030  -11.681 1.00 91.01  ? 137  THR C O   1 
ATOM   3187 C  CB  . THR C 1 137 ? -36.685 83.915  -14.147 1.00 98.47  ? 137  THR C CB  1 
ATOM   3188 O  OG1 . THR C 1 137 ? -36.537 84.749  -12.989 1.00 95.30  ? 137  THR C OG1 1 
ATOM   3189 C  CG2 . THR C 1 137 ? -37.891 84.388  -14.935 1.00 98.14  ? 137  THR C CG2 1 
ATOM   3190 N  N   . GLY C 1 138 ? -39.110 81.686  -13.118 1.00 95.60  ? 138  GLY C N   1 
ATOM   3191 C  CA  . GLY C 1 138 ? -40.288 81.590  -12.276 1.00 94.25  ? 138  GLY C CA  1 
ATOM   3192 C  C   . GLY C 1 138 ? -40.966 82.926  -12.015 1.00 94.05  ? 138  GLY C C   1 
ATOM   3193 O  O   . GLY C 1 138 ? -41.700 83.082  -11.040 1.00 89.93  ? 138  GLY C O   1 
ATOM   3194 N  N   . ASN C 1 139 ? -40.715 83.894  -12.890 1.00 98.81  ? 139  ASN C N   1 
ATOM   3195 C  CA  . ASN C 1 139 ? -41.394 85.193  -12.846 1.00 99.74  ? 139  ASN C CA  1 
ATOM   3196 C  C   . ASN C 1 139 ? -41.300 85.954  -11.516 1.00 96.61  ? 139  ASN C C   1 
ATOM   3197 O  O   . ASN C 1 139 ? -42.216 86.692  -11.146 1.00 94.88  ? 139  ASN C O   1 
ATOM   3198 C  CB  . ASN C 1 139 ? -42.856 85.056  -13.290 1.00 99.99  ? 139  ASN C CB  1 
ATOM   3199 C  CG  . ASN C 1 139 ? -42.985 84.690  -14.759 1.00 104.00 ? 139  ASN C CG  1 
ATOM   3200 O  OD1 . ASN C 1 139 ? -42.848 83.524  -15.140 1.00 106.54 ? 139  ASN C OD1 1 
ATOM   3201 N  ND2 . ASN C 1 139 ? -43.243 85.690  -15.594 1.00 105.40 ? 139  ASN C ND2 1 
ATOM   3202 N  N   . ALA C 1 140 ? -40.189 85.772  -10.808 1.00 97.27  ? 140  ALA C N   1 
ATOM   3203 C  CA  . ALA C 1 140 ? -39.900 86.568  -9.622  1.00 90.36  ? 140  ALA C CA  1 
ATOM   3204 C  C   . ALA C 1 140 ? -39.601 87.994  -10.069 1.00 90.88  ? 140  ALA C C   1 
ATOM   3205 O  O   . ALA C 1 140 ? -39.991 88.962  -9.421  1.00 87.38  ? 140  ALA C O   1 
ATOM   3206 C  CB  . ALA C 1 140 ? -38.720 85.982  -8.870  1.00 86.57  ? 140  ALA C CB  1 
ATOM   3207 N  N   . GLY C 1 141 ? -38.909 88.112  -11.197 1.00 93.83  ? 141  GLY C N   1 
ATOM   3208 C  CA  . GLY C 1 141 ? -38.646 89.409  -11.785 1.00 90.55  ? 141  GLY C CA  1 
ATOM   3209 C  C   . GLY C 1 141 ? -37.264 89.956  -11.485 1.00 91.72  ? 141  GLY C C   1 
ATOM   3210 O  O   . GLY C 1 141 ? -36.264 89.227  -11.542 1.00 87.04  ? 141  GLY C O   1 
ATOM   3211 N  N   . SER C 1 142 ? -37.221 91.248  -11.160 1.00 90.76  ? 142  SER C N   1 
ATOM   3212 C  CA  . SER C 1 142 ? -35.967 91.979  -10.979 1.00 88.28  ? 142  SER C CA  1 
ATOM   3213 C  C   . SER C 1 142 ? -35.214 91.579  -9.713  1.00 84.39  ? 142  SER C C   1 
ATOM   3214 O  O   . SER C 1 142 ? -35.811 91.140  -8.727  1.00 87.02  ? 142  SER C O   1 
ATOM   3215 C  CB  . SER C 1 142 ? -36.217 93.495  -10.987 1.00 87.42  ? 142  SER C CB  1 
ATOM   3216 O  OG  . SER C 1 142 ? -37.129 93.880  -9.971  1.00 84.08  ? 142  SER C OG  1 
ATOM   3217 N  N   . ARG C 1 143 ? -33.898 91.747  -9.753  1.00 78.59  ? 143  ARG C N   1 
ATOM   3218 C  CA  . ARG C 1 143 ? -33.028 91.367  -8.653  1.00 76.56  ? 143  ARG C CA  1 
ATOM   3219 C  C   . ARG C 1 143 ? -32.911 92.518  -7.656  1.00 76.34  ? 143  ARG C C   1 
ATOM   3220 O  O   . ARG C 1 143 ? -32.332 93.560  -7.969  1.00 74.40  ? 143  ARG C O   1 
ATOM   3221 C  CB  . ARG C 1 143 ? -31.671 90.979  -9.220  1.00 72.83  ? 143  ARG C CB  1 
ATOM   3222 C  CG  . ARG C 1 143 ? -31.807 90.185  -10.516 1.00 71.66  ? 143  ARG C CG  1 
ATOM   3223 C  CD  . ARG C 1 143 ? -30.465 89.828  -11.129 1.00 66.19  ? 143  ARG C CD  1 
ATOM   3224 N  NE  . ARG C 1 143 ? -30.601 88.759  -12.114 1.00 65.73  ? 143  ARG C NE  1 
ATOM   3225 C  CZ  . ARG C 1 143 ? -29.578 88.141  -12.702 1.00 68.95  ? 143  ARG C CZ  1 
ATOM   3226 N  NH1 . ARG C 1 143 ? -28.333 88.490  -12.414 1.00 71.22  ? 143  ARG C NH1 1 
ATOM   3227 N  NH2 . ARG C 1 143 ? -29.795 87.169  -13.579 1.00 61.35  ? 143  ARG C NH2 1 
ATOM   3228 N  N   . LEU C 1 144 ? -33.471 92.319  -6.461  1.00 77.27  ? 144  LEU C N   1 
ATOM   3229 C  CA  . LEU C 1 144 ? -33.619 93.384  -5.457  1.00 79.01  ? 144  LEU C CA  1 
ATOM   3230 C  C   . LEU C 1 144 ? -32.397 93.555  -4.541  1.00 77.18  ? 144  LEU C C   1 
ATOM   3231 O  O   . LEU C 1 144 ? -32.135 94.654  -4.046  1.00 77.36  ? 144  LEU C O   1 
ATOM   3232 C  CB  . LEU C 1 144 ? -34.882 93.144  -4.608  1.00 83.56  ? 144  LEU C CB  1 
ATOM   3233 C  CG  . LEU C 1 144 ? -36.066 94.127  -4.618  1.00 83.17  ? 144  LEU C CG  1 
ATOM   3234 C  CD1 . LEU C 1 144 ? -36.522 94.455  -6.029  1.00 81.70  ? 144  LEU C CD1 1 
ATOM   3235 C  CD2 . LEU C 1 144 ? -37.239 93.586  -3.798  1.00 82.03  ? 144  LEU C CD2 1 
ATOM   3236 N  N   . ALA C 1 145 ? -31.667 92.465  -4.308  1.00 76.40  ? 145  ALA C N   1 
ATOM   3237 C  CA  . ALA C 1 145 ? -30.461 92.488  -3.481  1.00 73.46  ? 145  ALA C CA  1 
ATOM   3238 C  C   . ALA C 1 145 ? -29.549 91.319  -3.838  1.00 71.80  ? 145  ALA C C   1 
ATOM   3239 O  O   . ALA C 1 145 ? -29.992 90.345  -4.449  1.00 70.60  ? 145  ALA C O   1 
ATOM   3240 C  CB  . ALA C 1 145 ? -30.821 92.445  -1.999  1.00 74.72  ? 145  ALA C CB  1 
ATOM   3241 N  N   . CYS C 1 146 ? -28.275 91.418  -3.463  1.00 67.16  ? 146  CYS C N   1 
ATOM   3242 C  CA  . CYS C 1 146 ? -27.332 90.328  -3.693  1.00 60.61  ? 146  CYS C CA  1 
ATOM   3243 C  C   . CYS C 1 146 ? -26.010 90.513  -2.966  1.00 50.32  ? 146  CYS C C   1 
ATOM   3244 O  O   . CYS C 1 146 ? -25.745 91.558  -2.397  1.00 53.87  ? 146  CYS C O   1 
ATOM   3245 C  CB  . CYS C 1 146 ? -27.089 90.114  -5.191  1.00 61.26  ? 146  CYS C CB  1 
ATOM   3246 S  SG  . CYS C 1 146 ? -26.586 91.593  -6.113  1.00 69.11  ? 146  CYS C SG  1 
ATOM   3247 N  N   . GLY C 1 147 ? -25.198 89.468  -2.984  1.00 49.44  ? 147  GLY C N   1 
ATOM   3248 C  CA  . GLY C 1 147 ? -23.853 89.507  -2.451  1.00 48.96  ? 147  GLY C CA  1 
ATOM   3249 C  C   . GLY C 1 147 ? -23.104 88.267  -2.894  1.00 47.21  ? 147  GLY C C   1 
ATOM   3250 O  O   . GLY C 1 147 ? -23.705 87.213  -3.060  1.00 53.06  ? 147  GLY C O   1 
ATOM   3251 N  N   . VAL C 1 148 ? -21.800 88.380  -3.115  1.00 47.09  ? 148  VAL C N   1 
ATOM   3252 C  CA  . VAL C 1 148 ? -20.984 87.187  -3.310  1.00 48.77  ? 148  VAL C CA  1 
ATOM   3253 C  C   . VAL C 1 148 ? -21.003 86.352  -2.020  1.00 48.92  ? 148  VAL C C   1 
ATOM   3254 O  O   . VAL C 1 148 ? -21.243 86.881  -0.938  1.00 49.96  ? 148  VAL C O   1 
ATOM   3255 C  CB  . VAL C 1 148 ? -19.534 87.530  -3.692  1.00 46.45  ? 148  VAL C CB  1 
ATOM   3256 C  CG1 . VAL C 1 148 ? -18.740 86.255  -3.945  1.00 43.63  ? 148  VAL C CG1 1 
ATOM   3257 C  CG2 . VAL C 1 148 ? -19.509 88.418  -4.917  1.00 43.06  ? 148  VAL C CG2 1 
ATOM   3258 N  N   . ILE C 1 149 ? -20.774 85.047  -2.137  1.00 51.00  ? 149  ILE C N   1 
ATOM   3259 C  CA  . ILE C 1 149 ? -20.822 84.147  -0.990  1.00 43.34  ? 149  ILE C CA  1 
ATOM   3260 C  C   . ILE C 1 149 ? -19.403 83.857  -0.538  1.00 38.78  ? 149  ILE C C   1 
ATOM   3261 O  O   . ILE C 1 149 ? -18.641 83.216  -1.245  1.00 39.35  ? 149  ILE C O   1 
ATOM   3262 C  CB  . ILE C 1 149 ? -21.587 82.856  -1.354  1.00 46.15  ? 149  ILE C CB  1 
ATOM   3263 C  CG1 . ILE C 1 149 ? -23.075 83.165  -1.491  1.00 52.55  ? 149  ILE C CG1 1 
ATOM   3264 C  CG2 . ILE C 1 149 ? -21.382 81.774  -0.315  1.00 44.44  ? 149  ILE C CG2 1 
ATOM   3265 C  CD1 . ILE C 1 149 ? -23.879 82.059  -2.152  1.00 57.57  ? 149  ILE C CD1 1 
ATOM   3266 N  N   . GLY C 1 150 ? -19.031 84.360  0.633   1.00 42.82  ? 150  GLY C N   1 
ATOM   3267 C  CA  . GLY C 1 150 ? -17.634 84.314  1.043   1.00 38.45  ? 150  GLY C CA  1 
ATOM   3268 C  C   . GLY C 1 150 ? -17.324 83.304  2.133   1.00 39.70  ? 150  GLY C C   1 
ATOM   3269 O  O   . GLY C 1 150 ? -18.183 82.964  2.932   1.00 43.70  ? 150  GLY C O   1 
ATOM   3270 N  N   . ILE C 1 151 ? -16.085 82.823  2.149   1.00 39.31  ? 151  ILE C N   1 
ATOM   3271 C  CA  . ILE C 1 151 ? -15.585 81.954  3.202   1.00 40.49  ? 151  ILE C CA  1 
ATOM   3272 C  C   . ILE C 1 151 ? -15.656 82.633  4.566   1.00 44.14  ? 151  ILE C C   1 
ATOM   3273 O  O   . ILE C 1 151 ? -15.008 83.661  4.790   1.00 43.60  ? 151  ILE C O   1 
ATOM   3274 C  CB  . ILE C 1 151 ? -14.121 81.567  2.949   1.00 41.37  ? 151  ILE C CB  1 
ATOM   3275 C  CG1 . ILE C 1 151 ? -14.002 80.643  1.733   1.00 46.13  ? 151  ILE C CG1 1 
ATOM   3276 C  CG2 . ILE C 1 151 ? -13.550 80.896  4.162   1.00 44.26  ? 151  ILE C CG2 1 
ATOM   3277 C  CD1 . ILE C 1 151 ? -12.569 80.213  1.426   1.00 42.91  ? 151  ILE C CD1 1 
ATOM   3278 N  N   . ALA C 1 152 ? -16.429 82.049  5.479   1.00 43.96  ? 152  ALA C N   1 
ATOM   3279 C  CA  . ALA C 1 152 ? -16.627 82.635  6.804   1.00 43.83  ? 152  ALA C CA  1 
ATOM   3280 C  C   . ALA C 1 152 ? -15.874 81.884  7.879   1.00 46.15  ? 152  ALA C C   1 
ATOM   3281 O  O   . ALA C 1 152 ? -15.550 80.709  7.718   1.00 44.62  ? 152  ALA C O   1 
ATOM   3282 C  CB  . ALA C 1 152 ? -18.085 82.666  7.137   1.00 43.47  ? 152  ALA C CB  1 
ATOM   3283 N  N   . GLN C 1 153 ? -15.585 82.559  8.984   1.00 50.49  ? 153  GLN C N   1 
ATOM   3284 C  CA  . GLN C 1 153 ? -15.023 81.850  10.122  1.00 49.24  ? 153  GLN C CA  1 
ATOM   3285 C  C   . GLN C 1 153 ? -16.153 81.159  10.871  1.00 56.08  ? 153  GLN C C   1 
ATOM   3286 O  O   . GLN C 1 153 ? -17.202 81.770  11.090  1.00 57.80  ? 153  GLN C O   1 
ATOM   3287 C  CB  . GLN C 1 153 ? -14.244 82.780  11.046  1.00 47.97  ? 153  GLN C CB  1 
ATOM   3288 C  CG  . GLN C 1 153 ? -15.092 83.575  12.026  1.00 50.74  ? 153  GLN C CG  1 
ATOM   3289 C  CD  . GLN C 1 153 ? -14.228 84.478  12.887  1.00 53.50  ? 153  GLN C CD  1 
ATOM   3290 O  OE1 . GLN C 1 153 ? -13.235 84.022  13.476  1.00 48.39  ? 153  GLN C OE1 1 
ATOM   3291 N  NE2 . GLN C 1 153 ? -14.577 85.771  12.944  1.00 43.63  ? 153  GLN C NE2 1 
ATOM   3292 O  OXT . GLN C 1 153 ? -16.057 79.979  11.245  1.00 58.51  ? 153  GLN C OXT 1 
ATOM   3293 N  N   . ALA D 1 1   ? -7.639  77.520  -17.375 1.00 61.97  ? 1    ALA D N   1 
ATOM   3294 C  CA  . ALA D 1 1   ? -8.611  78.557  -17.704 1.00 67.62  ? 1    ALA D CA  1 
ATOM   3295 C  C   . ALA D 1 1   ? -9.517  78.872  -16.508 1.00 69.50  ? 1    ALA D C   1 
ATOM   3296 O  O   . ALA D 1 1   ? -10.605 78.300  -16.375 1.00 69.98  ? 1    ALA D O   1 
ATOM   3297 C  CB  . ALA D 1 1   ? -9.445  78.147  -18.927 1.00 66.14  ? 1    ALA D CB  1 
ATOM   3298 N  N   . MET D 1 2   ? -9.051  79.783  -15.647 1.00 66.67  ? 2    MET D N   1 
ATOM   3299 C  CA  . MET D 1 2   ? -9.795  80.248  -14.468 1.00 61.74  ? 2    MET D CA  1 
ATOM   3300 C  C   . MET D 1 2   ? -9.868  81.786  -14.375 1.00 55.50  ? 2    MET D C   1 
ATOM   3301 O  O   . MET D 1 2   ? -8.833  82.461  -14.380 1.00 46.72  ? 2    MET D O   1 
ATOM   3302 C  CB  . MET D 1 2   ? -9.147  79.698  -13.193 1.00 56.86  ? 2    MET D CB  1 
ATOM   3303 C  CG  . MET D 1 2   ? -9.416  78.226  -12.921 1.00 64.77  ? 2    MET D CG  1 
ATOM   3304 S  SD  . MET D 1 2   ? -7.976  77.370  -12.231 1.00 72.18  ? 2    MET D SD  1 
ATOM   3305 C  CE  . MET D 1 2   ? -6.975  77.220  -13.721 1.00 67.86  ? 2    MET D CE  1 
ATOM   3306 N  N   . LYS D 1 3   ? -11.093 82.313  -14.269 1.00 55.18  ? 3    LYS D N   1 
ATOM   3307 C  CA  . LYS D 1 3   ? -11.362 83.752  -14.158 1.00 53.33  ? 3    LYS D CA  1 
ATOM   3308 C  C   . LYS D 1 3   ? -12.020 84.136  -12.821 1.00 54.96  ? 3    LYS D C   1 
ATOM   3309 O  O   . LYS D 1 3   ? -13.028 83.543  -12.434 1.00 54.72  ? 3    LYS D O   1 
ATOM   3310 C  CB  . LYS D 1 3   ? -12.323 84.181  -15.268 1.00 57.74  ? 3    LYS D CB  1 
ATOM   3311 C  CG  . LYS D 1 3   ? -11.698 84.824  -16.508 1.00 67.90  ? 3    LYS D CG  1 
ATOM   3312 C  CD  . LYS D 1 3   ? -12.765 85.001  -17.622 1.00 61.20  ? 3    LYS D CD  1 
ATOM   3313 C  CE  . LYS D 1 3   ? -12.332 86.020  -18.688 1.00 75.08  ? 3    LYS D CE  1 
ATOM   3314 N  NZ  . LYS D 1 3   ? -10.977 85.766  -19.280 1.00 73.74  ? 3    LYS D NZ  1 
ATOM   3315 N  N   . ALA D 1 4   ? -11.487 85.144  -12.131 1.00 48.44  ? 4    ALA D N   1 
ATOM   3316 C  CA  . ALA D 1 4   ? -12.189 85.703  -10.966 1.00 48.24  ? 4    ALA D CA  1 
ATOM   3317 C  C   . ALA D 1 4   ? -12.208 87.227  -10.983 1.00 46.05  ? 4    ALA D C   1 
ATOM   3318 O  O   . ALA D 1 4   ? -11.266 87.852  -11.488 1.00 47.98  ? 4    ALA D O   1 
ATOM   3319 C  CB  . ALA D 1 4   ? -11.588 85.190  -9.664  1.00 42.18  ? 4    ALA D CB  1 
ATOM   3320 N  N   . VAL D 1 5   ? -13.278 87.813  -10.434 1.00 43.10  ? 5    VAL D N   1 
ATOM   3321 C  CA  . VAL D 1 5   ? -13.430 89.273  -10.343 1.00 37.93  ? 5    VAL D CA  1 
ATOM   3322 C  C   . VAL D 1 5   ? -13.599 89.796  -8.887  1.00 42.20  ? 5    VAL D C   1 
ATOM   3323 O  O   . VAL D 1 5   ? -13.990 89.039  -8.002  1.00 42.10  ? 5    VAL D O   1 
ATOM   3324 C  CB  . VAL D 1 5   ? -14.606 89.762  -11.207 1.00 38.59  ? 5    VAL D CB  1 
ATOM   3325 C  CG1 . VAL D 1 5   ? -15.934 89.343  -10.595 1.00 44.28  ? 5    VAL D CG1 1 
ATOM   3326 C  CG2 . VAL D 1 5   ? -14.556 91.274  -11.387 1.00 39.50  ? 5    VAL D CG2 1 
ATOM   3327 N  N   . CYS D 1 6   ? -13.302 91.080  -8.640  1.00 38.05  ? 6    CYS D N   1 
ATOM   3328 C  CA  . CYS D 1 6   ? -13.479 91.665  -7.303  1.00 35.56  ? 6    CYS D CA  1 
ATOM   3329 C  C   . CYS D 1 6   ? -13.660 93.182  -7.292  1.00 34.87  ? 6    CYS D C   1 
ATOM   3330 O  O   . CYS D 1 6   ? -12.734 93.931  -7.614  1.00 37.35  ? 6    CYS D O   1 
ATOM   3331 C  CB  . CYS D 1 6   ? -12.300 91.294  -6.395  1.00 39.32  ? 6    CYS D CB  1 
ATOM   3332 S  SG  . CYS D 1 6   ? -12.233 92.176  -4.799  1.00 40.12  ? 6    CYS D SG  1 
ATOM   3333 N  N   . VAL D 1 7   ? -14.842 93.630  -6.890  1.00 27.78  ? 7    VAL D N   1 
ATOM   3334 C  CA  . VAL D 1 7   ? -15.113 95.051  -6.688  1.00 31.53  ? 7    VAL D CA  1 
ATOM   3335 C  C   . VAL D 1 7   ? -14.736 95.542  -5.266  1.00 36.61  ? 7    VAL D C   1 
ATOM   3336 O  O   . VAL D 1 7   ? -15.219 95.008  -4.252  1.00 33.54  ? 7    VAL D O   1 
ATOM   3337 C  CB  . VAL D 1 7   ? -16.592 95.340  -6.954  1.00 33.81  ? 7    VAL D CB  1 
ATOM   3338 C  CG1 . VAL D 1 7   ? -16.931 96.805  -6.670  1.00 35.35  ? 7    VAL D CG1 1 
ATOM   3339 C  CG2 . VAL D 1 7   ? -16.936 94.950  -8.383  1.00 41.58  ? 7    VAL D CG2 1 
ATOM   3340 N  N   . LEU D 1 8   ? -13.869 96.549  -5.188  1.00 34.56  ? 8    LEU D N   1 
ATOM   3341 C  CA  . LEU D 1 8   ? -13.468 97.080  -3.888  1.00 32.07  ? 8    LEU D CA  1 
ATOM   3342 C  C   . LEU D 1 8   ? -14.283 98.297  -3.497  1.00 34.05  ? 8    LEU D C   1 
ATOM   3343 O  O   . LEU D 1 8   ? -14.220 99.313  -4.166  1.00 36.72  ? 8    LEU D O   1 
ATOM   3344 C  CB  . LEU D 1 8   ? -11.979 97.420  -3.871  1.00 30.44  ? 8    LEU D CB  1 
ATOM   3345 C  CG  . LEU D 1 8   ? -11.032 96.225  -3.908  1.00 34.88  ? 8    LEU D CG  1 
ATOM   3346 C  CD1 . LEU D 1 8   ? -10.924 95.678  -5.331  1.00 35.97  ? 8    LEU D CD1 1 
ATOM   3347 C  CD2 . LEU D 1 8   ? -9.666  96.569  -3.371  1.00 29.12  ? 8    LEU D CD2 1 
ATOM   3348 N  N   . LYS D 1 9   ? -15.059 98.186  -2.424  1.00 31.24  ? 9    LYS D N   1 
ATOM   3349 C  CA  . LYS D 1 9   ? -15.718 99.344  -1.830  1.00 32.44  ? 9    LYS D CA  1 
ATOM   3350 C  C   . LYS D 1 9   ? -15.240 99.589  -0.390  1.00 34.97  ? 9    LYS D C   1 
ATOM   3351 O  O   . LYS D 1 9   ? -14.671 98.710  0.252   1.00 33.68  ? 9    LYS D O   1 
ATOM   3352 C  CB  . LYS D 1 9   ? -17.235 99.157  -1.800  1.00 40.64  ? 9    LYS D CB  1 
ATOM   3353 C  CG  . LYS D 1 9   ? -17.842 98.562  -3.045  1.00 43.78  ? 9    LYS D CG  1 
ATOM   3354 C  CD  . LYS D 1 9   ? -17.513 99.374  -4.302  1.00 50.08  ? 9    LYS D CD  1 
ATOM   3355 C  CE  . LYS D 1 9   ? -18.265 100.705 -4.354  1.00 51.67  ? 9    LYS D CE  1 
ATOM   3356 N  NZ  . LYS D 1 9   ? -18.092 101.373 -5.679  1.00 49.76  ? 9    LYS D NZ  1 
ATOM   3357 N  N   . GLY D 1 10  ? -15.504 100.784 0.122   1.00 39.88  ? 10   GLY D N   1 
ATOM   3358 C  CA  . GLY D 1 10  ? -15.189 101.127 1.500   1.00 37.75  ? 10   GLY D CA  1 
ATOM   3359 C  C   . GLY D 1 10  ? -16.051 102.285 1.981   1.00 42.61  ? 10   GLY D C   1 
ATOM   3360 O  O   . GLY D 1 10  ? -17.058 102.605 1.360   1.00 43.55  ? 10   GLY D O   1 
ATOM   3361 N  N   . ASP D 1 11  ? -15.663 102.928 3.075   1.00 43.25  ? 11   ASP D N   1 
ATOM   3362 C  CA  . ASP D 1 11  ? -16.457 104.036 3.589   1.00 46.38  ? 11   ASP D CA  1 
ATOM   3363 C  C   . ASP D 1 11  ? -15.986 105.375 3.069   1.00 44.23  ? 11   ASP D C   1 
ATOM   3364 O  O   . ASP D 1 11  ? -16.671 106.390 3.223   1.00 44.84  ? 11   ASP D O   1 
ATOM   3365 C  CB  . ASP D 1 11  ? -16.471 104.034 5.113   1.00 46.14  ? 11   ASP D CB  1 
ATOM   3366 C  CG  . ASP D 1 11  ? -17.470 103.040 5.676   1.00 61.78  ? 11   ASP D CG  1 
ATOM   3367 O  OD1 . ASP D 1 11  ? -18.599 102.954 5.131   1.00 60.59  ? 11   ASP D OD1 1 
ATOM   3368 O  OD2 . ASP D 1 11  ? -17.130 102.342 6.662   1.00 70.30  ? 11   ASP D OD2 1 
ATOM   3369 N  N   . GLY D 1 12  ? -14.815 105.375 2.449   1.00 37.31  ? 12   GLY D N   1 
ATOM   3370 C  CA  . GLY D 1 12  ? -14.257 106.592 1.907   1.00 32.52  ? 12   GLY D CA  1 
ATOM   3371 C  C   . GLY D 1 12  ? -14.287 106.589 0.401   1.00 36.34  ? 12   GLY D C   1 
ATOM   3372 O  O   . GLY D 1 12  ? -14.996 105.793 -0.224  1.00 41.26  ? 12   GLY D O   1 
ATOM   3373 N  N   . PRO D 1 13  ? -13.483 107.461 -0.194  1.00 32.74  ? 13   PRO D N   1 
ATOM   3374 C  CA  . PRO D 1 13  ? -13.542 107.731 -1.634  1.00 31.94  ? 13   PRO D CA  1 
ATOM   3375 C  C   . PRO D 1 13  ? -12.949 106.594 -2.455  1.00 35.96  ? 13   PRO D C   1 
ATOM   3376 O  O   . PRO D 1 13  ? -13.114 106.598 -3.682  1.00 36.63  ? 13   PRO D O   1 
ATOM   3377 C  CB  . PRO D 1 13  ? -12.664 108.978 -1.777  1.00 31.92  ? 13   PRO D CB  1 
ATOM   3378 C  CG  . PRO D 1 13  ? -11.639 108.831 -0.658  1.00 29.65  ? 13   PRO D CG  1 
ATOM   3379 C  CD  . PRO D 1 13  ? -12.412 108.209 0.487   1.00 24.04  ? 13   PRO D CD  1 
ATOM   3380 N  N   . VAL D 1 14  ? -12.258 105.656 -1.802  1.00 33.02  ? 14   VAL D N   1 
ATOM   3381 C  CA  . VAL D 1 14  ? -11.526 104.599 -2.518  1.00 32.15  ? 14   VAL D CA  1 
ATOM   3382 C  C   . VAL D 1 14  ? -12.419 103.480 -3.069  1.00 31.86  ? 14   VAL D C   1 
ATOM   3383 O  O   . VAL D 1 14  ? -13.374 103.066 -2.424  1.00 36.50  ? 14   VAL D O   1 
ATOM   3384 C  CB  . VAL D 1 14  ? -10.438 103.989 -1.641  1.00 30.60  ? 14   VAL D CB  1 
ATOM   3385 C  CG1 . VAL D 1 14  ? -9.808  102.769 -2.320  1.00 21.89  ? 14   VAL D CG1 1 
ATOM   3386 C  CG2 . VAL D 1 14  ? -9.405  105.051 -1.319  1.00 30.87  ? 14   VAL D CG2 1 
ATOM   3387 N  N   . GLN D 1 15  ? -12.109 103.018 -4.277  1.00 31.77  ? 15   GLN D N   1 
ATOM   3388 C  CA  . GLN D 1 15  ? -12.897 101.988 -4.954  1.00 33.44  ? 15   GLN D CA  1 
ATOM   3389 C  C   . GLN D 1 15  ? -12.136 101.443 -6.151  1.00 32.02  ? 15   GLN D C   1 
ATOM   3390 O  O   . GLN D 1 15  ? -11.279 102.120 -6.710  1.00 32.98  ? 15   GLN D O   1 
ATOM   3391 C  CB  . GLN D 1 15  ? -14.262 102.506 -5.395  1.00 33.41  ? 15   GLN D CB  1 
ATOM   3392 C  CG  . GLN D 1 15  ? -14.209 103.728 -6.265  1.00 38.77  ? 15   GLN D CG  1 
ATOM   3393 C  CD  . GLN D 1 15  ? -15.601 104.252 -6.608  1.00 45.95  ? 15   GLN D CD  1 
ATOM   3394 O  OE1 . GLN D 1 15  ? -15.820 105.463 -6.708  1.00 50.96  ? 15   GLN D OE1 1 
ATOM   3395 N  NE2 . GLN D 1 15  ? -16.546 103.341 -6.780  1.00 43.25  ? 15   GLN D NE2 1 
ATOM   3396 N  N   . GLY D 1 16  ? -12.429 100.203 -6.519  1.00 28.31  ? 16   GLY D N   1 
ATOM   3397 C  CA  . GLY D 1 16  ? -11.664 99.537  -7.545  1.00 30.43  ? 16   GLY D CA  1 
ATOM   3398 C  C   . GLY D 1 16  ? -12.401 98.355  -8.125  1.00 32.45  ? 16   GLY D C   1 
ATOM   3399 O  O   . GLY D 1 16  ? -13.437 97.929  -7.612  1.00 32.21  ? 16   GLY D O   1 
ATOM   3400 N  N   . THR D 1 17  ? -11.851 97.850  -9.221  1.00 33.36  ? 17   THR D N   1 
ATOM   3401 C  CA  . THR D 1 17  ? -12.368 96.699  -9.933  1.00 28.82  ? 17   THR D CA  1 
ATOM   3402 C  C   . THR D 1 17  ? -11.134 95.950  -10.394 1.00 31.61  ? 17   THR D C   1 
ATOM   3403 O  O   . THR D 1 17  ? -10.236 96.541  -10.989 1.00 35.05  ? 17   THR D O   1 
ATOM   3404 C  CB  . THR D 1 17  ? -13.249 97.115  -11.127 1.00 31.71  ? 17   THR D CB  1 
ATOM   3405 O  OG1 . THR D 1 17  ? -14.385 97.855  -10.656 1.00 32.62  ? 17   THR D OG1 1 
ATOM   3406 C  CG2 . THR D 1 17  ? -13.766 95.885  -11.879 1.00 35.98  ? 17   THR D CG2 1 
ATOM   3407 N  N   . ILE D 1 18  ? -11.062 94.663  -10.073 1.00 30.85  ? 18   ILE D N   1 
ATOM   3408 C  CA  . ILE D 1 18  ? -9.894  93.848  -10.393 1.00 32.18  ? 18   ILE D CA  1 
ATOM   3409 C  C   . ILE D 1 18  ? -10.319 92.533  -11.054 1.00 36.28  ? 18   ILE D C   1 
ATOM   3410 O  O   . ILE D 1 18  ? -11.421 92.034  -10.828 1.00 38.18  ? 18   ILE D O   1 
ATOM   3411 C  CB  . ILE D 1 18  ? -9.047  93.547  -9.139  1.00 31.32  ? 18   ILE D CB  1 
ATOM   3412 C  CG1 . ILE D 1 18  ? -8.573  94.843  -8.491  1.00 29.53  ? 18   ILE D CG1 1 
ATOM   3413 C  CG2 . ILE D 1 18  ? -7.844  92.665  -9.490  1.00 32.13  ? 18   ILE D CG2 1 
ATOM   3414 C  CD1 . ILE D 1 18  ? -7.227  95.325  -9.005  1.00 33.97  ? 18   ILE D CD1 1 
ATOM   3415 N  N   . HIS D 1 19  ? -9.451  91.992  -11.900 1.00 37.53  ? 19   HIS D N   1 
ATOM   3416 C  CA  . HIS D 1 19  ? -9.721  90.724  -12.574 1.00 40.84  ? 19   HIS D CA  1 
ATOM   3417 C  C   . HIS D 1 19  ? -8.504  89.818  -12.419 1.00 41.99  ? 19   HIS D C   1 
ATOM   3418 O  O   . HIS D 1 19  ? -7.368  90.306  -12.325 1.00 35.75  ? 19   HIS D O   1 
ATOM   3419 C  CB  . HIS D 1 19  ? -10.115 90.946  -14.049 1.00 35.72  ? 19   HIS D CB  1 
ATOM   3420 C  CG  . HIS D 1 19  ? -11.577 91.216  -14.236 1.00 33.98  ? 19   HIS D CG  1 
ATOM   3421 N  ND1 . HIS D 1 19  ? -12.118 92.481  -14.153 1.00 34.70  ? 19   HIS D ND1 1 
ATOM   3422 C  CD2 . HIS D 1 19  ? -12.618 90.380  -14.460 1.00 39.43  ? 19   HIS D CD2 1 
ATOM   3423 C  CE1 . HIS D 1 19  ? -13.424 92.418  -14.334 1.00 33.05  ? 19   HIS D CE1 1 
ATOM   3424 N  NE2 . HIS D 1 19  ? -13.756 91.153  -14.515 1.00 40.24  ? 19   HIS D NE2 1 
ATOM   3425 N  N   . PHE D 1 20  ? -8.743  88.512  -12.318 1.00 40.07  ? 20   PHE D N   1 
ATOM   3426 C  CA  . PHE D 1 20  ? -7.642  87.575  -12.109 1.00 44.80  ? 20   PHE D CA  1 
ATOM   3427 C  C   . PHE D 1 20  ? -7.650  86.552  -13.237 1.00 42.74  ? 20   PHE D C   1 
ATOM   3428 O  O   . PHE D 1 20  ? -8.709  86.080  -13.649 1.00 41.31  ? 20   PHE D O   1 
ATOM   3429 C  CB  . PHE D 1 20  ? -7.763  86.805  -10.774 1.00 43.18  ? 20   PHE D CB  1 
ATOM   3430 C  CG  . PHE D 1 20  ? -7.897  87.670  -9.533  1.00 43.36  ? 20   PHE D CG  1 
ATOM   3431 C  CD1 . PHE D 1 20  ? -6.820  87.843  -8.672  1.00 41.50  ? 20   PHE D CD1 1 
ATOM   3432 C  CD2 . PHE D 1 20  ? -9.110  88.235  -9.191  1.00 37.28  ? 20   PHE D CD2 1 
ATOM   3433 C  CE1 . PHE D 1 20  ? -6.939  88.600  -7.528  1.00 36.49  ? 20   PHE D CE1 1 
ATOM   3434 C  CE2 . PHE D 1 20  ? -9.233  88.986  -8.041  1.00 41.64  ? 20   PHE D CE2 1 
ATOM   3435 C  CZ  . PHE D 1 20  ? -8.146  89.169  -7.208  1.00 37.62  ? 20   PHE D CZ  1 
ATOM   3436 N  N   . GLU D 1 21  ? -6.469  86.184  -13.710 1.00 47.42  ? 21   GLU D N   1 
ATOM   3437 C  CA  . GLU D 1 21  ? -6.369  85.202  -14.776 1.00 53.04  ? 21   GLU D CA  1 
ATOM   3438 C  C   . GLU D 1 21  ? -5.438  84.107  -14.331 1.00 49.48  ? 21   GLU D C   1 
ATOM   3439 O  O   . GLU D 1 21  ? -4.400  84.385  -13.722 1.00 46.98  ? 21   GLU D O   1 
ATOM   3440 C  CB  . GLU D 1 21  ? -5.822  85.839  -16.062 1.00 54.51  ? 21   GLU D CB  1 
ATOM   3441 C  CG  . GLU D 1 21  ? -6.062  85.011  -17.329 1.00 66.02  ? 21   GLU D CG  1 
ATOM   3442 C  CD  . GLU D 1 21  ? -7.179  85.582  -18.210 1.00 78.61  ? 21   GLU D CD  1 
ATOM   3443 O  OE1 . GLU D 1 21  ? -7.167  86.813  -18.461 1.00 81.42  ? 21   GLU D OE1 1 
ATOM   3444 O  OE2 . GLU D 1 21  ? -8.060  84.802  -18.655 1.00 73.93  ? 21   GLU D OE2 1 
ATOM   3445 N  N   . GLN D 1 22  ? -5.826  82.867  -14.624 1.00 49.42  ? 22   GLN D N   1 
ATOM   3446 C  CA  . GLN D 1 22  ? -4.945  81.708  -14.468 1.00 59.34  ? 22   GLN D CA  1 
ATOM   3447 C  C   . GLN D 1 22  ? -5.249  80.671  -15.568 1.00 60.17  ? 22   GLN D C   1 
ATOM   3448 O  O   . GLN D 1 22  ? -6.379  80.188  -15.692 1.00 55.59  ? 22   GLN D O   1 
ATOM   3449 C  CB  . GLN D 1 22  ? -5.081  81.090  -13.063 1.00 52.88  ? 22   GLN D CB  1 
ATOM   3450 C  CG  . GLN D 1 22  ? -3.782  80.541  -12.481 1.00 51.88  ? 22   GLN D CG  1 
ATOM   3451 C  CD  . GLN D 1 22  ? -4.008  79.684  -11.237 1.00 53.97  ? 22   GLN D CD  1 
ATOM   3452 O  OE1 . GLN D 1 22  ? -5.141  79.343  -10.898 1.00 54.19  ? 22   GLN D OE1 1 
ATOM   3453 N  NE2 . GLN D 1 22  ? -2.929  79.340  -10.554 1.00 53.54  ? 22   GLN D NE2 1 
ATOM   3454 N  N   . LYS D 1 23  ? -4.250  80.351  -16.384 1.00 61.50  ? 23   LYS D N   1 
ATOM   3455 C  CA  . LYS D 1 23  ? -4.459  79.366  -17.440 1.00 70.72  ? 23   LYS D CA  1 
ATOM   3456 C  C   . LYS D 1 23  ? -4.442  77.964  -16.851 1.00 70.81  ? 23   LYS D C   1 
ATOM   3457 O  O   . LYS D 1 23  ? -5.351  77.165  -17.087 1.00 66.95  ? 23   LYS D O   1 
ATOM   3458 C  CB  . LYS D 1 23  ? -3.392  79.477  -18.534 1.00 76.53  ? 23   LYS D CB  1 
ATOM   3459 C  CG  . LYS D 1 23  ? -3.489  78.375  -19.606 1.00 82.93  ? 23   LYS D CG  1 
ATOM   3460 C  CD  . LYS D 1 23  ? -2.240  78.319  -20.498 1.00 84.20  ? 23   LYS D CD  1 
ATOM   3461 C  CE  . LYS D 1 23  ? -2.305  77.162  -21.491 1.00 78.76  ? 23   LYS D CE  1 
ATOM   3462 N  NZ  . LYS D 1 23  ? -1.167  77.196  -22.456 1.00 82.36  ? 23   LYS D NZ  1 
ATOM   3463 N  N   . ALA D 1 24  ? -3.403  77.671  -16.073 1.00 70.26  ? 24   ALA D N   1 
ATOM   3464 C  CA  . ALA D 1 24  ? -3.246  76.334  -15.518 1.00 71.40  ? 24   ALA D CA  1 
ATOM   3465 C  C   . ALA D 1 24  ? -3.138  76.334  -13.999 1.00 70.73  ? 24   ALA D C   1 
ATOM   3466 O  O   . ALA D 1 24  ? -2.549  77.240  -13.397 1.00 65.13  ? 24   ALA D O   1 
ATOM   3467 C  CB  . ALA D 1 24  ? -2.049  75.627  -16.144 1.00 73.06  ? 24   ALA D CB  1 
ATOM   3468 N  N   . SER D 1 25  ? -3.705  75.291  -13.400 1.00 67.05  ? 25   SER D N   1 
ATOM   3469 C  CA  . SER D 1 25  ? -3.762  75.146  -11.955 1.00 65.74  ? 25   SER D CA  1 
ATOM   3470 C  C   . SER D 1 25  ? -2.394  75.310  -11.291 1.00 67.55  ? 25   SER D C   1 
ATOM   3471 O  O   . SER D 1 25  ? -2.299  75.760  -10.149 1.00 70.35  ? 25   SER D O   1 
ATOM   3472 C  CB  . SER D 1 25  ? -4.393  73.799  -11.594 1.00 66.68  ? 25   SER D CB  1 
ATOM   3473 O  OG  . SER D 1 25  ? -5.702  73.697  -12.141 1.00 66.86  ? 25   SER D OG  1 
ATOM   3474 N  N   . GLY D 1 26  ? -1.330  74.963  -12.002 1.00 65.39  ? 26   GLY D N   1 
ATOM   3475 C  CA  . GLY D 1 26  ? -0.002  75.118  -11.441 1.00 70.92  ? 26   GLY D CA  1 
ATOM   3476 C  C   . GLY D 1 26  ? 0.663   76.411  -11.879 1.00 73.79  ? 26   GLY D C   1 
ATOM   3477 O  O   . GLY D 1 26  ? 1.805   76.686  -11.506 1.00 72.35  ? 26   GLY D O   1 
ATOM   3478 N  N   . GLU D 1 27  ? -0.062  77.208  -12.663 1.00 70.29  ? 27   GLU D N   1 
ATOM   3479 C  CA  . GLU D 1 27  ? 0.499   78.389  -13.319 1.00 70.16  ? 27   GLU D CA  1 
ATOM   3480 C  C   . GLU D 1 27  ? 0.089   79.717  -12.680 1.00 71.82  ? 27   GLU D C   1 
ATOM   3481 O  O   . GLU D 1 27  ? -1.035  79.847  -12.188 1.00 68.86  ? 27   GLU D O   1 
ATOM   3482 C  CB  . GLU D 1 27  ? 0.092   78.402  -14.791 1.00 70.05  ? 27   GLU D CB  1 
ATOM   3483 C  CG  . GLU D 1 27  ? 0.891   77.455  -15.662 1.00 75.81  ? 27   GLU D CG  1 
ATOM   3484 C  CD  . GLU D 1 27  ? 0.569   77.623  -17.135 1.00 82.04  ? 27   GLU D CD  1 
ATOM   3485 O  OE1 . GLU D 1 27  ? -0.442  78.298  -17.452 1.00 77.18  ? 27   GLU D OE1 1 
ATOM   3486 O  OE2 . GLU D 1 27  ? 1.328   77.081  -17.971 1.00 84.32  ? 27   GLU D OE2 1 
ATOM   3487 N  N   . PRO D 1 28  ? 0.997   80.716  -12.717 1.00 66.78  ? 28   PRO D N   1 
ATOM   3488 C  CA  . PRO D 1 28  ? 0.818   82.058  -12.142 1.00 56.48  ? 28   PRO D CA  1 
ATOM   3489 C  C   . PRO D 1 28  ? -0.571  82.669  -12.331 1.00 52.98  ? 28   PRO D C   1 
ATOM   3490 O  O   . PRO D 1 28  ? -1.277  82.334  -13.285 1.00 56.79  ? 28   PRO D O   1 
ATOM   3491 C  CB  . PRO D 1 28  ? 1.864   82.885  -12.884 1.00 58.95  ? 28   PRO D CB  1 
ATOM   3492 C  CG  . PRO D 1 28  ? 2.977   81.918  -13.118 1.00 60.43  ? 28   PRO D CG  1 
ATOM   3493 C  CD  . PRO D 1 28  ? 2.326   80.568  -13.340 1.00 65.11  ? 28   PRO D CD  1 
ATOM   3494 N  N   . VAL D 1 29  ? -0.957  83.542  -11.399 1.00 53.04  ? 29   VAL D N   1 
ATOM   3495 C  CA  . VAL D 1 29  ? -2.200  84.307  -11.513 1.00 51.51  ? 29   VAL D CA  1 
ATOM   3496 C  C   . VAL D 1 29  ? -1.902  85.747  -11.910 1.00 43.89  ? 29   VAL D C   1 
ATOM   3497 O  O   . VAL D 1 29  ? -0.973  86.364  -11.386 1.00 44.39  ? 29   VAL D O   1 
ATOM   3498 C  CB  . VAL D 1 29  ? -3.016  84.331  -10.202 1.00 50.41  ? 29   VAL D CB  1 
ATOM   3499 C  CG1 . VAL D 1 29  ? -4.479  84.664  -10.508 1.00 45.59  ? 29   VAL D CG1 1 
ATOM   3500 C  CG2 . VAL D 1 29  ? -2.909  83.002  -9.476  1.00 49.26  ? 29   VAL D CG2 1 
ATOM   3501 N  N   . VAL D 1 30  ? -2.682  86.273  -12.848 1.00 44.29  ? 30   VAL D N   1 
ATOM   3502 C  CA  . VAL D 1 30  ? -2.527  87.663  -13.254 1.00 44.23  ? 30   VAL D CA  1 
ATOM   3503 C  C   . VAL D 1 30  ? -3.715  88.504  -12.779 1.00 41.90  ? 30   VAL D C   1 
ATOM   3504 O  O   . VAL D 1 30  ? -4.879  88.121  -12.962 1.00 35.68  ? 30   VAL D O   1 
ATOM   3505 C  CB  . VAL D 1 30  ? -2.305  87.801  -14.784 1.00 48.81  ? 30   VAL D CB  1 
ATOM   3506 C  CG1 . VAL D 1 30  ? -2.275  89.270  -15.196 1.00 47.84  ? 30   VAL D CG1 1 
ATOM   3507 C  CG2 . VAL D 1 30  ? -1.008  87.108  -15.191 1.00 43.33  ? 30   VAL D CG2 1 
ATOM   3508 N  N   . LEU D 1 31  ? -3.394  89.619  -12.120 1.00 38.62  ? 31   LEU D N   1 
ATOM   3509 C  CA  . LEU D 1 31  ? -4.390  90.603  -11.693 1.00 38.35  ? 31   LEU D CA  1 
ATOM   3510 C  C   . LEU D 1 31  ? -4.255  91.851  -12.526 1.00 36.01  ? 31   LEU D C   1 
ATOM   3511 O  O   . LEU D 1 31  ? -3.140  92.289  -12.809 1.00 36.55  ? 31   LEU D O   1 
ATOM   3512 C  CB  . LEU D 1 31  ? -4.151  91.044  -10.247 1.00 41.34  ? 31   LEU D CB  1 
ATOM   3513 C  CG  . LEU D 1 31  ? -4.392  90.086  -9.102  1.00 43.46  ? 31   LEU D CG  1 
ATOM   3514 C  CD1 . LEU D 1 31  ? -3.209  89.122  -8.961  1.00 44.94  ? 31   LEU D CD1 1 
ATOM   3515 C  CD2 . LEU D 1 31  ? -4.613  90.913  -7.850  1.00 46.30  ? 31   LEU D CD2 1 
ATOM   3516 N  N   . SER D 1 32  ? -5.381  92.455  -12.873 1.00 33.66  ? 32   SER D N   1 
ATOM   3517 C  CA  . SER D 1 32  ? -5.343  93.723  -13.569 1.00 36.83  ? 32   SER D CA  1 
ATOM   3518 C  C   . SER D 1 32  ? -6.589  94.524  -13.263 1.00 34.77  ? 32   SER D C   1 
ATOM   3519 O  O   . SER D 1 32  ? -7.624  93.967  -12.916 1.00 38.26  ? 32   SER D O   1 
ATOM   3520 C  CB  . SER D 1 32  ? -5.185  93.512  -15.079 1.00 37.96  ? 32   SER D CB  1 
ATOM   3521 O  OG  . SER D 1 32  ? -6.204  92.668  -15.558 1.00 40.70  ? 32   SER D OG  1 
ATOM   3522 N  N   . GLY D 1 33  ? -6.481  95.838  -13.390 1.00 32.35  ? 33   GLY D N   1 
ATOM   3523 C  CA  . GLY D 1 33  ? -7.623  96.715  -13.184 1.00 31.18  ? 33   GLY D CA  1 
ATOM   3524 C  C   . GLY D 1 33  ? -7.156  97.984  -12.507 1.00 29.47  ? 33   GLY D C   1 
ATOM   3525 O  O   . GLY D 1 33  ? -5.957  98.258  -12.390 1.00 32.15  ? 33   GLY D O   1 
ATOM   3526 N  N   . GLN D 1 34  ? -8.093  98.779  -12.043 1.00 28.48  ? 34   GLN D N   1 
ATOM   3527 C  CA  . GLN D 1 34  ? -7.687  100.016 -11.404 1.00 33.85  ? 34   GLN D CA  1 
ATOM   3528 C  C   . GLN D 1 34  ? -8.330  100.178 -10.052 1.00 26.42  ? 34   GLN D C   1 
ATOM   3529 O  O   . GLN D 1 34  ? -9.453  99.726  -9.834  1.00 28.02  ? 34   GLN D O   1 
ATOM   3530 C  CB  . GLN D 1 34  ? -7.985  101.238 -12.304 1.00 28.84  ? 34   GLN D CB  1 
ATOM   3531 C  CG  . GLN D 1 34  ? -7.168  101.235 -13.586 1.00 29.54  ? 34   GLN D CG  1 
ATOM   3532 C  CD  . GLN D 1 34  ? -7.756  100.308 -14.627 1.00 29.18  ? 34   GLN D CD  1 
ATOM   3533 O  OE1 . GLN D 1 34  ? -8.975  100.264 -14.803 1.00 29.11  ? 34   GLN D OE1 1 
ATOM   3534 N  NE2 . GLN D 1 34  ? -6.894  99.575  -15.335 1.00 28.34  ? 34   GLN D NE2 1 
ATOM   3535 N  N   . ILE D 1 35  ? -7.593  100.821 -9.157  1.00 26.23  ? 35   ILE D N   1 
ATOM   3536 C  CA  . ILE D 1 35  ? -8.137  101.344 -7.912  1.00 26.21  ? 35   ILE D CA  1 
ATOM   3537 C  C   . ILE D 1 35  ? -8.022  102.864 -7.906  1.00 26.09  ? 35   ILE D C   1 
ATOM   3538 O  O   . ILE D 1 35  ? -6.944  103.428 -8.128  1.00 28.09  ? 35   ILE D O   1 
ATOM   3539 C  CB  . ILE D 1 35  ? -7.387  100.776 -6.700  1.00 28.31  ? 35   ILE D CB  1 
ATOM   3540 C  CG1 . ILE D 1 35  ? -7.352  99.250  -6.783  1.00 26.38  ? 35   ILE D CG1 1 
ATOM   3541 C  CG2 . ILE D 1 35  ? -8.050  101.228 -5.398  1.00 24.58  ? 35   ILE D CG2 1 
ATOM   3542 C  CD1 . ILE D 1 35  ? -6.135  98.641  -6.127  1.00 25.76  ? 35   ILE D CD1 1 
ATOM   3543 N  N   . THR D 1 36  ? -9.135  103.530 -7.660  1.00 24.17  ? 36   THR D N   1 
ATOM   3544 C  CA  . THR D 1 36  ? -9.126  104.981 -7.624  1.00 28.25  ? 36   THR D CA  1 
ATOM   3545 C  C   . THR D 1 36  ? -9.364  105.555 -6.216  1.00 28.56  ? 36   THR D C   1 
ATOM   3546 O  O   . THR D 1 36  ? -9.725  104.825 -5.272  1.00 26.65  ? 36   THR D O   1 
ATOM   3547 C  CB  . THR D 1 36  ? -10.189 105.556 -8.580  1.00 25.68  ? 36   THR D CB  1 
ATOM   3548 O  OG1 . THR D 1 36  ? -11.478 105.233 -8.076  1.00 29.99  ? 36   THR D OG1 1 
ATOM   3549 C  CG2 . THR D 1 36  ? -10.046 104.960 -9.997  1.00 28.02  ? 36   THR D CG2 1 
ATOM   3550 N  N   . GLY D 1 37  ? -9.152  106.868 -6.096  1.00 25.20  ? 37   GLY D N   1 
ATOM   3551 C  CA  . GLY D 1 37  ? -9.428  107.610 -4.877  1.00 27.46  ? 37   GLY D CA  1 
ATOM   3552 C  C   . GLY D 1 37  ? -8.335  107.512 -3.824  1.00 27.24  ? 37   GLY D C   1 
ATOM   3553 O  O   . GLY D 1 37  ? -8.565  107.840 -2.664  1.00 28.39  ? 37   GLY D O   1 
ATOM   3554 N  N   . LEU D 1 38  ? -7.146  107.080 -4.230  1.00 23.60  ? 38   LEU D N   1 
ATOM   3555 C  CA  . LEU D 1 38  ? -6.048  106.881 -3.292  1.00 27.07  ? 38   LEU D CA  1 
ATOM   3556 C  C   . LEU D 1 38  ? -5.121  108.089 -3.163  1.00 27.45  ? 38   LEU D C   1 
ATOM   3557 O  O   . LEU D 1 38  ? -4.891  108.808 -4.118  1.00 32.28  ? 38   LEU D O   1 
ATOM   3558 C  CB  . LEU D 1 38  ? -5.207  105.663 -3.690  1.00 26.77  ? 38   LEU D CB  1 
ATOM   3559 C  CG  . LEU D 1 38  ? -5.898  104.310 -3.610  1.00 27.94  ? 38   LEU D CG  1 
ATOM   3560 C  CD1 . LEU D 1 38  ? -5.226  103.372 -4.569  1.00 25.20  ? 38   LEU D CD1 1 
ATOM   3561 C  CD2 . LEU D 1 38  ? -5.926  103.760 -2.150  1.00 22.96  ? 38   LEU D CD2 1 
ATOM   3562 N  N   . THR D 1 39  ? -4.573  108.290 -1.975  1.00 27.79  ? 39   THR D N   1 
ATOM   3563 C  CA  . THR D 1 39  ? -3.476  109.221 -1.816  1.00 27.16  ? 39   THR D CA  1 
ATOM   3564 C  C   . THR D 1 39  ? -2.335  108.685 -2.649  1.00 28.00  ? 39   THR D C   1 
ATOM   3565 O  O   . THR D 1 39  ? -2.253  107.484 -2.923  1.00 30.02  ? 39   THR D O   1 
ATOM   3566 C  CB  . THR D 1 39  ? -3.014  109.302 -0.364  1.00 31.93  ? 39   THR D CB  1 
ATOM   3567 O  OG1 . THR D 1 39  ? -2.667  107.986 0.092   1.00 31.47  ? 39   THR D OG1 1 
ATOM   3568 C  CG2 . THR D 1 39  ? -4.134  109.892 0.527   1.00 28.10  ? 39   THR D CG2 1 
ATOM   3569 N  N   . GLU D 1 40  ? -1.456  109.576 -3.063  1.00 25.93  ? 40   GLU D N   1 
ATOM   3570 C  CA  . GLU D 1 40  ? -0.400  109.201 -3.966  1.00 30.77  ? 40   GLU D CA  1 
ATOM   3571 C  C   . GLU D 1 40  ? 0.670   108.413 -3.233  1.00 29.92  ? 40   GLU D C   1 
ATOM   3572 O  O   . GLU D 1 40  ? 0.977   108.694 -2.086  1.00 28.28  ? 40   GLU D O   1 
ATOM   3573 C  CB  . GLU D 1 40  ? 0.215   110.442 -4.613  1.00 32.47  ? 40   GLU D CB  1 
ATOM   3574 C  CG  . GLU D 1 40  ? 1.328   110.090 -5.574  1.00 40.67  ? 40   GLU D CG  1 
ATOM   3575 C  CD  . GLU D 1 40  ? 1.878   111.284 -6.336  1.00 48.41  ? 40   GLU D CD  1 
ATOM   3576 O  OE1 . GLU D 1 40  ? 1.772   112.427 -5.824  1.00 44.13  ? 40   GLU D OE1 1 
ATOM   3577 O  OE2 . GLU D 1 40  ? 2.418   111.058 -7.448  1.00 46.90  ? 40   GLU D OE2 1 
ATOM   3578 N  N   . GLY D 1 41  ? 1.245   107.433 -3.915  1.00 27.91  ? 41   GLY D N   1 
ATOM   3579 C  CA  . GLY D 1 41  ? 2.279   106.605 -3.333  1.00 27.46  ? 41   GLY D CA  1 
ATOM   3580 C  C   . GLY D 1 41  ? 1.842   105.152 -3.202  1.00 28.78  ? 41   GLY D C   1 
ATOM   3581 O  O   . GLY D 1 41  ? 0.864   104.710 -3.826  1.00 26.64  ? 41   GLY D O   1 
ATOM   3582 N  N   . GLN D 1 42  ? 2.578   104.418 -2.376  1.00 28.92  ? 42   GLN D N   1 
ATOM   3583 C  CA  . GLN D 1 42  ? 2.398   102.976 -2.238  1.00 30.02  ? 42   GLN D CA  1 
ATOM   3584 C  C   . GLN D 1 42  ? 1.336   102.583 -1.225  1.00 27.63  ? 42   GLN D C   1 
ATOM   3585 O  O   . GLN D 1 42  ? 1.114   103.249 -0.217  1.00 28.07  ? 42   GLN D O   1 
ATOM   3586 C  CB  . GLN D 1 42  ? 3.714   102.312 -1.866  1.00 32.41  ? 42   GLN D CB  1 
ATOM   3587 C  CG  . GLN D 1 42  ? 4.774   102.346 -2.957  1.00 35.18  ? 42   GLN D CG  1 
ATOM   3588 C  CD  . GLN D 1 42  ? 6.036   101.618 -2.521  1.00 47.07  ? 42   GLN D CD  1 
ATOM   3589 O  OE1 . GLN D 1 42  ? 6.480   101.757 -1.374  1.00 44.19  ? 42   GLN D OE1 1 
ATOM   3590 N  NE2 . GLN D 1 42  ? 6.619   100.839 -3.428  1.00 46.38  ? 42   GLN D NE2 1 
ATOM   3591 N  N   . HIS D 1 43  ? 0.676   101.478 -1.514  1.00 28.51  ? 43   HIS D N   1 
ATOM   3592 C  CA  . HIS D 1 43  ? -0.452  101.043 -0.725  1.00 30.14  ? 43   HIS D CA  1 
ATOM   3593 C  C   . HIS D 1 43  ? -0.427  99.525  -0.623  1.00 32.34  ? 43   HIS D C   1 
ATOM   3594 O  O   . HIS D 1 43  ? -0.431  98.816  -1.641  1.00 30.63  ? 43   HIS D O   1 
ATOM   3595 C  CB  . HIS D 1 43  ? -1.762  101.560 -1.341  1.00 28.03  ? 43   HIS D CB  1 
ATOM   3596 C  CG  . HIS D 1 43  ? -1.916  103.043 -1.231  1.00 28.72  ? 43   HIS D CG  1 
ATOM   3597 N  ND1 . HIS D 1 43  ? -2.665  103.641 -0.238  1.00 25.37  ? 43   HIS D ND1 1 
ATOM   3598 C  CD2 . HIS D 1 43  ? -1.363  104.051 -1.947  1.00 28.79  ? 43   HIS D CD2 1 
ATOM   3599 C  CE1 . HIS D 1 43  ? -2.578  104.953 -0.358  1.00 27.19  ? 43   HIS D CE1 1 
ATOM   3600 N  NE2 . HIS D 1 43  ? -1.788  105.229 -1.381  1.00 28.04  ? 43   HIS D NE2 1 
ATOM   3601 N  N   . GLY D 1 44  ? -0.366  99.040  0.615   1.00 27.92  ? 44   GLY D N   1 
ATOM   3602 C  CA  . GLY D 1 44  ? -0.379  97.619  0.879   1.00 27.03  ? 44   GLY D CA  1 
ATOM   3603 C  C   . GLY D 1 44  ? -1.595  97.035  0.204   1.00 28.09  ? 44   GLY D C   1 
ATOM   3604 O  O   . GLY D 1 44  ? -2.657  97.654  0.175   1.00 28.35  ? 44   GLY D O   1 
ATOM   3605 N  N   . PHE D 1 45  ? -1.438  95.834  -0.331  1.00 26.82  ? 45   PHE D N   1 
ATOM   3606 C  CA  . PHE D 1 45  ? -2.450  95.236  -1.177  1.00 29.75  ? 45   PHE D CA  1 
ATOM   3607 C  C   . PHE D 1 45  ? -2.351  93.732  -0.938  1.00 30.97  ? 45   PHE D C   1 
ATOM   3608 O  O   . PHE D 1 45  ? -1.321  93.124  -1.257  1.00 31.52  ? 45   PHE D O   1 
ATOM   3609 C  CB  . PHE D 1 45  ? -2.139  95.614  -2.634  1.00 30.13  ? 45   PHE D CB  1 
ATOM   3610 C  CG  . PHE D 1 45  ? -3.222  95.258  -3.606  1.00 26.36  ? 45   PHE D CG  1 
ATOM   3611 C  CD1 . PHE D 1 45  ? -4.454  95.868  -3.536  1.00 25.86  ? 45   PHE D CD1 1 
ATOM   3612 C  CD2 . PHE D 1 45  ? -2.999  94.319  -4.598  1.00 27.82  ? 45   PHE D CD2 1 
ATOM   3613 C  CE1 . PHE D 1 45  ? -5.457  95.547  -4.435  1.00 29.46  ? 45   PHE D CE1 1 
ATOM   3614 C  CE2 . PHE D 1 45  ? -3.988  93.994  -5.502  1.00 30.11  ? 45   PHE D CE2 1 
ATOM   3615 C  CZ  . PHE D 1 45  ? -5.221  94.608  -5.428  1.00 33.59  ? 45   PHE D CZ  1 
ATOM   3616 N  N   . HIS D 1 46  ? -3.388  93.144  -0.339  1.00 26.05  ? 46   HIS D N   1 
ATOM   3617 C  CA  . HIS D 1 46  ? -3.263  91.805  0.247   1.00 28.75  ? 46   HIS D CA  1 
ATOM   3618 C  C   . HIS D 1 46  ? -4.519  90.985  0.070   1.00 31.18  ? 46   HIS D C   1 
ATOM   3619 O  O   . HIS D 1 46  ? -5.626  91.539  0.029   1.00 29.26  ? 46   HIS D O   1 
ATOM   3620 C  CB  . HIS D 1 46  ? -3.000  91.856  1.762   1.00 26.39  ? 46   HIS D CB  1 
ATOM   3621 C  CG  . HIS D 1 46  ? -1.935  92.813  2.174   1.00 25.55  ? 46   HIS D CG  1 
ATOM   3622 N  ND1 . HIS D 1 46  ? -0.662  92.783  1.654   1.00 27.91  ? 46   HIS D ND1 1 
ATOM   3623 C  CD2 . HIS D 1 46  ? -1.947  93.818  3.080   1.00 28.84  ? 46   HIS D CD2 1 
ATOM   3624 C  CE1 . HIS D 1 46  ? 0.063   93.736  2.210   1.00 28.73  ? 46   HIS D CE1 1 
ATOM   3625 N  NE2 . HIS D 1 46  ? -0.695  94.379  3.081   1.00 29.64  ? 46   HIS D NE2 1 
ATOM   3626 N  N   . VAL D 1 47  ? -4.355  89.662  -0.003  1.00 29.29  ? 47   VAL D N   1 
ATOM   3627 C  CA  . VAL D 1 47  ? -5.506  88.778  0.107   1.00 31.79  ? 47   VAL D CA  1 
ATOM   3628 C  C   . VAL D 1 47  ? -5.678  88.392  1.563   1.00 33.02  ? 47   VAL D C   1 
ATOM   3629 O  O   . VAL D 1 47  ? -4.760  87.864  2.202   1.00 34.18  ? 47   VAL D O   1 
ATOM   3630 C  CB  . VAL D 1 47  ? -5.386  87.519  -0.763  1.00 37.13  ? 47   VAL D CB  1 
ATOM   3631 C  CG1 . VAL D 1 47  ? -6.749  86.798  -0.846  1.00 33.14  ? 47   VAL D CG1 1 
ATOM   3632 C  CG2 . VAL D 1 47  ? -4.889  87.896  -2.131  1.00 36.25  ? 47   VAL D CG2 1 
ATOM   3633 N  N   . HIS D 1 48  ? -6.853  88.698  2.091   1.00 31.61  ? 48   HIS D N   1 
ATOM   3634 C  CA  . HIS D 1 48  ? -7.143  88.449  3.489   1.00 32.86  ? 48   HIS D CA  1 
ATOM   3635 C  C   . HIS D 1 48  ? -7.895  87.126  3.635   1.00 39.18  ? 48   HIS D C   1 
ATOM   3636 O  O   . HIS D 1 48  ? -8.404  86.577  2.654   1.00 38.76  ? 48   HIS D O   1 
ATOM   3637 C  CB  . HIS D 1 48  ? -7.887  89.649  4.112   1.00 32.18  ? 48   HIS D CB  1 
ATOM   3638 C  CG  . HIS D 1 48  ? -6.989  90.815  4.432   1.00 32.60  ? 48   HIS D CG  1 
ATOM   3639 N  ND1 . HIS D 1 48  ? -6.644  91.162  5.723   1.00 29.79  ? 48   HIS D ND1 1 
ATOM   3640 C  CD2 . HIS D 1 48  ? -6.340  91.694  3.626   1.00 30.86  ? 48   HIS D CD2 1 
ATOM   3641 C  CE1 . HIS D 1 48  ? -5.831  92.205  5.703   1.00 26.17  ? 48   HIS D CE1 1 
ATOM   3642 N  NE2 . HIS D 1 48  ? -5.636  92.553  4.444   1.00 34.06  ? 48   HIS D NE2 1 
ATOM   3643 N  N   . GLN D 1 49  ? -7.959  86.606  4.855   1.00 41.78  ? 49   GLN D N   1 
ATOM   3644 C  CA  . GLN D 1 49  ? -8.477  85.260  5.068   1.00 39.80  ? 49   GLN D CA  1 
ATOM   3645 C  C   . GLN D 1 49  ? -9.934  85.010  4.666   1.00 36.83  ? 49   GLN D C   1 
ATOM   3646 O  O   . GLN D 1 49  ? -10.213 84.064  3.931   1.00 38.52  ? 49   GLN D O   1 
ATOM   3647 C  CB  . GLN D 1 49  ? -8.252  84.809  6.509   1.00 39.50  ? 49   GLN D CB  1 
ATOM   3648 C  CG  . GLN D 1 49  ? -8.780  83.405  6.769   1.00 41.02  ? 49   GLN D CG  1 
ATOM   3649 C  CD  . GLN D 1 49  ? -8.016  82.702  7.862   1.00 41.94  ? 49   GLN D CD  1 
ATOM   3650 O  OE1 . GLN D 1 49  ? -7.005  83.206  8.345   1.00 40.87  ? 49   GLN D OE1 1 
ATOM   3651 N  NE2 . GLN D 1 49  ? -8.491  81.528  8.256   1.00 40.61  ? 49   GLN D NE2 1 
ATOM   3652 N  N   . TYR D 1 50  ? -10.864 85.829  5.144   1.00 34.98  ? 50   TYR D N   1 
ATOM   3653 C  CA  . TYR D 1 50  ? -12.277 85.475  5.000   1.00 35.53  ? 50   TYR D CA  1 
ATOM   3654 C  C   . TYR D 1 50  ? -12.994 86.361  4.015   1.00 38.45  ? 50   TYR D C   1 
ATOM   3655 O  O   . TYR D 1 50  ? -12.570 87.479  3.760   1.00 38.05  ? 50   TYR D O   1 
ATOM   3656 C  CB  . TYR D 1 50  ? -13.001 85.533  6.344   1.00 40.41  ? 50   TYR D CB  1 
ATOM   3657 C  CG  . TYR D 1 50  ? -12.409 84.641  7.415   1.00 39.76  ? 50   TYR D CG  1 
ATOM   3658 C  CD1 . TYR D 1 50  ? -12.502 83.257  7.317   1.00 43.32  ? 50   TYR D CD1 1 
ATOM   3659 C  CD2 . TYR D 1 50  ? -11.781 85.182  8.534   1.00 41.42  ? 50   TYR D CD2 1 
ATOM   3660 C  CE1 . TYR D 1 50  ? -11.965 82.426  8.293   1.00 45.34  ? 50   TYR D CE1 1 
ATOM   3661 C  CE2 . TYR D 1 50  ? -11.247 84.359  9.532   1.00 49.21  ? 50   TYR D CE2 1 
ATOM   3662 C  CZ  . TYR D 1 50  ? -11.339 82.978  9.394   1.00 49.96  ? 50   TYR D CZ  1 
ATOM   3663 O  OH  . TYR D 1 50  ? -10.828 82.141  10.354  1.00 54.43  ? 50   TYR D OH  1 
ATOM   3664 N  N   . GLY D 1 51  ? -14.090 85.853  3.464   1.00 39.69  ? 51   GLY D N   1 
ATOM   3665 C  CA  . GLY D 1 51  ? -14.912 86.619  2.548   1.00 36.67  ? 51   GLY D CA  1 
ATOM   3666 C  C   . GLY D 1 51  ? -16.087 87.186  3.301   1.00 38.08  ? 51   GLY D C   1 
ATOM   3667 O  O   . GLY D 1 51  ? -17.213 87.216  2.804   1.00 38.76  ? 51   GLY D O   1 
ATOM   3668 N  N   . ASP D 1 52  ? -15.800 87.650  4.512   1.00 38.72  ? 52   ASP D N   1 
ATOM   3669 C  CA  . ASP D 1 52  ? -16.821 88.069  5.462   1.00 37.56  ? 52   ASP D CA  1 
ATOM   3670 C  C   . ASP D 1 52  ? -16.879 89.596  5.549   1.00 39.02  ? 52   ASP D C   1 
ATOM   3671 O  O   . ASP D 1 52  ? -15.951 90.239  6.047   1.00 35.59  ? 52   ASP D O   1 
ATOM   3672 C  CB  . ASP D 1 52  ? -16.498 87.455  6.834   1.00 38.23  ? 52   ASP D CB  1 
ATOM   3673 C  CG  . ASP D 1 52  ? -17.610 87.631  7.840   1.00 40.20  ? 52   ASP D CG  1 
ATOM   3674 O  OD1 . ASP D 1 52  ? -18.339 88.645  7.755   1.00 42.77  ? 52   ASP D OD1 1 
ATOM   3675 O  OD2 . ASP D 1 52  ? -17.750 86.754  8.730   1.00 41.94  ? 52   ASP D OD2 1 
ATOM   3676 N  N   . ASN D 1 53  ? -17.972 90.175  5.066   1.00 39.57  ? 53   ASN D N   1 
ATOM   3677 C  CA  . ASN D 1 53  ? -18.131 91.623  5.113   1.00 41.64  ? 53   ASN D CA  1 
ATOM   3678 C  C   . ASN D 1 53  ? -19.226 92.135  6.043   1.00 39.43  ? 53   ASN D C   1 
ATOM   3679 O  O   . ASN D 1 53  ? -19.727 93.241  5.866   1.00 40.45  ? 53   ASN D O   1 
ATOM   3680 C  CB  . ASN D 1 53  ? -18.267 92.205  3.694   1.00 46.38  ? 53   ASN D CB  1 
ATOM   3681 C  CG  . ASN D 1 53  ? -16.902 92.480  3.054   1.00 52.00  ? 53   ASN D CG  1 
ATOM   3682 O  OD1 . ASN D 1 53  ? -15.863 92.403  3.738   1.00 48.15  ? 53   ASN D OD1 1 
ATOM   3683 N  ND2 . ASN D 1 53  ? -16.890 92.797  1.750   1.00 44.93  ? 53   ASN D ND2 1 
ATOM   3684 N  N   . THR D 1 54  ? -19.577 91.346  7.056   1.00 44.19  ? 54   THR D N   1 
ATOM   3685 C  CA  . THR D 1 54  ? -20.617 91.757  7.997   1.00 38.19  ? 54   THR D CA  1 
ATOM   3686 C  C   . THR D 1 54  ? -20.155 92.968  8.779   1.00 36.20  ? 54   THR D C   1 
ATOM   3687 O  O   . THR D 1 54  ? -20.972 93.769  9.236   1.00 36.40  ? 54   THR D O   1 
ATOM   3688 C  CB  . THR D 1 54  ? -21.022 90.631  8.994   1.00 38.55  ? 54   THR D CB  1 
ATOM   3689 O  OG1 . THR D 1 54  ? -19.853 90.052  9.580   1.00 35.87  ? 54   THR D OG1 1 
ATOM   3690 C  CG2 . THR D 1 54  ? -21.838 89.549  8.299   1.00 37.95  ? 54   THR D CG2 1 
ATOM   3691 N  N   . GLN D 1 55  ? -18.842 93.101  8.923   1.00 32.95  ? 55   GLN D N   1 
ATOM   3692 C  CA  . GLN D 1 55  ? -18.277 94.242  9.627   1.00 36.19  ? 55   GLN D CA  1 
ATOM   3693 C  C   . GLN D 1 55  ? -17.289 94.972  8.740   1.00 34.96  ? 55   GLN D C   1 
ATOM   3694 O  O   . GLN D 1 55  ? -16.104 95.101  9.084   1.00 38.29  ? 55   GLN D O   1 
ATOM   3695 C  CB  . GLN D 1 55  ? -17.624 93.803  10.952  1.00 32.36  ? 55   GLN D CB  1 
ATOM   3696 C  CG  . GLN D 1 55  ? -18.612 93.139  11.886  1.00 32.55  ? 55   GLN D CG  1 
ATOM   3697 C  CD  . GLN D 1 55  ? -18.019 92.745  13.230  1.00 34.66  ? 55   GLN D CD  1 
ATOM   3698 O  OE1 . GLN D 1 55  ? -17.156 91.871  13.311  1.00 35.35  ? 55   GLN D OE1 1 
ATOM   3699 N  NE2 . GLN D 1 55  ? -18.500 93.374  14.294  1.00 30.26  ? 55   GLN D NE2 1 
ATOM   3700 N  N   . GLY D 1 56  ? -17.776 95.438  7.593   1.00 36.20  ? 56   GLY D N   1 
ATOM   3701 C  CA  . GLY D 1 56  ? -16.941 96.144  6.636   1.00 30.82  ? 56   GLY D CA  1 
ATOM   3702 C  C   . GLY D 1 56  ? -15.682 95.359  6.330   1.00 35.26  ? 56   GLY D C   1 
ATOM   3703 O  O   . GLY D 1 56  ? -15.720 94.154  6.120   1.00 39.77  ? 56   GLY D O   1 
ATOM   3704 N  N   . CYS D 1 57  ? -14.547 96.029  6.312   1.00 34.34  ? 57   CYS D N   1 
ATOM   3705 C  CA  . CYS D 1 57  ? -13.315 95.330  5.998   1.00 33.75  ? 57   CYS D CA  1 
ATOM   3706 C  C   . CYS D 1 57  ? -12.710 94.611  7.192   1.00 34.23  ? 57   CYS D C   1 
ATOM   3707 O  O   . CYS D 1 57  ? -11.851 93.737  7.035   1.00 35.11  ? 57   CYS D O   1 
ATOM   3708 C  CB  . CYS D 1 57  ? -12.311 96.286  5.356   1.00 35.54  ? 57   CYS D CB  1 
ATOM   3709 S  SG  . CYS D 1 57  ? -12.833 96.729  3.654   1.00 48.68  ? 57   CYS D SG  1 
ATOM   3710 N  N   . THR D 1 58  ? -13.159 94.945  8.395   1.00 35.93  ? 58   THR D N   1 
ATOM   3711 C  CA  . THR D 1 58  ? -12.511 94.354  9.571   1.00 36.69  ? 58   THR D CA  1 
ATOM   3712 C  C   . THR D 1 58  ? -12.769 92.839  9.740   1.00 37.09  ? 58   THR D C   1 
ATOM   3713 O  O   . THR D 1 58  ? -11.883 92.120  10.195  1.00 31.62  ? 58   THR D O   1 
ATOM   3714 C  CB  . THR D 1 58  ? -12.807 95.131  10.856  1.00 35.11  ? 58   THR D CB  1 
ATOM   3715 O  OG1 . THR D 1 58  ? -13.987 94.611  11.477  1.00 45.31  ? 58   THR D OG1 1 
ATOM   3716 C  CG2 . THR D 1 58  ? -12.987 96.603  10.551  1.00 26.94  ? 58   THR D CG2 1 
ATOM   3717 N  N   . SER D 1 59  ? -13.950 92.358  9.336   1.00 35.54  ? 59   SER D N   1 
ATOM   3718 C  CA  . SER D 1 59  ? -14.268 90.929  9.434   1.00 34.09  ? 59   SER D CA  1 
ATOM   3719 C  C   . SER D 1 59  ? -13.661 90.058  8.331   1.00 41.46  ? 59   SER D C   1 
ATOM   3720 O  O   . SER D 1 59  ? -13.995 88.875  8.215   1.00 40.70  ? 59   SER D O   1 
ATOM   3721 C  CB  . SER D 1 59  ? -15.783 90.695  9.488   1.00 35.33  ? 59   SER D CB  1 
ATOM   3722 O  OG  . SER D 1 59  ? -16.445 91.407  8.463   1.00 39.67  ? 59   SER D OG  1 
ATOM   3723 N  N   . ALA D 1 60  ? -12.786 90.626  7.514   1.00 33.41  ? 60   ALA D N   1 
ATOM   3724 C  CA  . ALA D 1 60  ? -12.087 89.807  6.551   1.00 36.38  ? 60   ALA D CA  1 
ATOM   3725 C  C   . ALA D 1 60  ? -10.941 89.091  7.263   1.00 37.41  ? 60   ALA D C   1 
ATOM   3726 O  O   . ALA D 1 60  ? -10.309 88.194  6.703   1.00 34.24  ? 60   ALA D O   1 
ATOM   3727 C  CB  . ALA D 1 60  ? -11.572 90.654  5.370   1.00 32.82  ? 60   ALA D CB  1 
ATOM   3728 N  N   . GLY D 1 61  ? -10.679 89.501  8.500   1.00 33.02  ? 61   GLY D N   1 
ATOM   3729 C  CA  . GLY D 1 61  ? -9.599  88.923  9.276   1.00 34.55  ? 61   GLY D CA  1 
ATOM   3730 C  C   . GLY D 1 61  ? -8.199  89.259  8.790   1.00 37.90  ? 61   GLY D C   1 
ATOM   3731 O  O   . GLY D 1 61  ? -7.967  90.293  8.160   1.00 37.46  ? 61   GLY D O   1 
ATOM   3732 N  N   . PRO D 1 62  ? -7.242  88.375  9.072   1.00 39.46  ? 62   PRO D N   1 
ATOM   3733 C  CA  . PRO D 1 62  ? -5.847  88.657  8.722   1.00 38.82  ? 62   PRO D CA  1 
ATOM   3734 C  C   . PRO D 1 62  ? -5.513  88.209  7.296   1.00 36.14  ? 62   PRO D C   1 
ATOM   3735 O  O   . PRO D 1 62  ? -6.369  87.686  6.581   1.00 36.66  ? 62   PRO D O   1 
ATOM   3736 C  CB  . PRO D 1 62  ? -5.067  87.782  9.709   1.00 38.89  ? 62   PRO D CB  1 
ATOM   3737 C  CG  . PRO D 1 62  ? -6.072  86.663  10.130  1.00 39.20  ? 62   PRO D CG  1 
ATOM   3738 C  CD  . PRO D 1 62  ? -7.418  86.985  9.526   1.00 36.89  ? 62   PRO D CD  1 
ATOM   3739 N  N   . HIS D 1 63  ? -4.266  88.419  6.901   1.00 33.73  ? 63   HIS D N   1 
ATOM   3740 C  CA  . HIS D 1 63  ? -3.741  87.882  5.655   1.00 38.33  ? 63   HIS D CA  1 
ATOM   3741 C  C   . HIS D 1 63  ? -3.958  86.369  5.547   1.00 44.88  ? 63   HIS D C   1 
ATOM   3742 O  O   . HIS D 1 63  ? -3.795  85.630  6.536   1.00 42.94  ? 63   HIS D O   1 
ATOM   3743 C  CB  . HIS D 1 63  ? -2.243  88.187  5.546   1.00 38.24  ? 63   HIS D CB  1 
ATOM   3744 C  CG  . HIS D 1 63  ? -1.932  89.645  5.495   1.00 34.58  ? 63   HIS D CG  1 
ATOM   3745 N  ND1 . HIS D 1 63  ? -0.653  90.128  5.362   1.00 35.89  ? 63   HIS D ND1 1 
ATOM   3746 C  CD2 . HIS D 1 63  ? -2.737  90.734  5.563   1.00 31.81  ? 63   HIS D CD2 1 
ATOM   3747 C  CE1 . HIS D 1 63  ? -0.675  91.450  5.349   1.00 31.64  ? 63   HIS D CE1 1 
ATOM   3748 N  NE2 . HIS D 1 63  ? -1.929  91.842  5.465   1.00 30.43  ? 63   HIS D NE2 1 
ATOM   3749 N  N   . PHE D 1 64  ? -4.329  85.921  4.346   1.00 39.79  ? 64   PHE D N   1 
ATOM   3750 C  CA  . PHE D 1 64  ? -4.465  84.503  4.055   1.00 38.71  ? 64   PHE D CA  1 
ATOM   3751 C  C   . PHE D 1 64  ? -3.136  83.830  4.346   1.00 45.49  ? 64   PHE D C   1 
ATOM   3752 O  O   . PHE D 1 64  ? -2.133  84.131  3.691   1.00 47.82  ? 64   PHE D O   1 
ATOM   3753 C  CB  . PHE D 1 64  ? -4.846  84.324  2.590   1.00 45.99  ? 64   PHE D CB  1 
ATOM   3754 C  CG  . PHE D 1 64  ? -5.206  82.915  2.214   1.00 50.66  ? 64   PHE D CG  1 
ATOM   3755 C  CD1 . PHE D 1 64  ? -5.884  82.092  3.103   1.00 54.40  ? 64   PHE D CD1 1 
ATOM   3756 C  CD2 . PHE D 1 64  ? -4.892  82.424  0.955   1.00 49.30  ? 64   PHE D CD2 1 
ATOM   3757 C  CE1 . PHE D 1 64  ? -6.232  80.794  2.747   1.00 55.25  ? 64   PHE D CE1 1 
ATOM   3758 C  CE2 . PHE D 1 64  ? -5.240  81.127  0.592   1.00 55.38  ? 64   PHE D CE2 1 
ATOM   3759 C  CZ  . PHE D 1 64  ? -5.908  80.310  1.490   1.00 52.60  ? 64   PHE D CZ  1 
ATOM   3760 N  N   . ASN D 1 65  ? -3.106  82.948  5.345   1.00 49.62  ? 65   ASN D N   1 
ATOM   3761 C  CA  . ASN D 1 65  ? -1.836  82.350  5.771   1.00 48.78  ? 65   ASN D CA  1 
ATOM   3762 C  C   . ASN D 1 65  ? -1.906  80.860  6.106   1.00 52.90  ? 65   ASN D C   1 
ATOM   3763 O  O   . ASN D 1 65  ? -1.749  80.455  7.264   1.00 48.95  ? 65   ASN D O   1 
ATOM   3764 C  CB  . ASN D 1 65  ? -1.252  83.120  6.942   1.00 40.71  ? 65   ASN D CB  1 
ATOM   3765 C  CG  . ASN D 1 65  ? 0.184   82.776  7.184   1.00 48.84  ? 65   ASN D CG  1 
ATOM   3766 O  OD1 . ASN D 1 65  ? 0.787   82.031  6.415   1.00 52.32  ? 65   ASN D OD1 1 
ATOM   3767 N  ND2 . ASN D 1 65  ? 0.750   83.311  8.256   1.00 48.83  ? 65   ASN D ND2 1 
ATOM   3768 N  N   . PRO D 1 66  ? -2.108  80.040  5.074   1.00 52.01  ? 66   PRO D N   1 
ATOM   3769 C  CA  . PRO D 1 66  ? -2.364  78.599  5.152   1.00 50.28  ? 66   PRO D CA  1 
ATOM   3770 C  C   . PRO D 1 66  ? -1.193  77.873  5.796   1.00 53.28  ? 66   PRO D C   1 
ATOM   3771 O  O   . PRO D 1 66  ? -1.395  76.934  6.563   1.00 58.42  ? 66   PRO D O   1 
ATOM   3772 C  CB  . PRO D 1 66  ? -2.485  78.184  3.683   1.00 54.05  ? 66   PRO D CB  1 
ATOM   3773 C  CG  . PRO D 1 66  ? -2.687  79.466  2.919   1.00 56.10  ? 66   PRO D CG  1 
ATOM   3774 C  CD  . PRO D 1 66  ? -1.916  80.489  3.691   1.00 51.24  ? 66   PRO D CD  1 
ATOM   3775 N  N   . HIS D 1 67  ? 0.020   78.322  5.496   1.00 53.14  ? 67   HIS D N   1 
ATOM   3776 C  CA  . HIS D 1 67  ? 1.230   77.679  5.999   1.00 51.91  ? 67   HIS D CA  1 
ATOM   3777 C  C   . HIS D 1 67  ? 1.724   78.346  7.266   1.00 47.87  ? 67   HIS D C   1 
ATOM   3778 O  O   . HIS D 1 67  ? 2.833   78.094  7.704   1.00 50.75  ? 67   HIS D O   1 
ATOM   3779 C  CB  . HIS D 1 67  ? 2.347   77.716  4.946   1.00 53.40  ? 67   HIS D CB  1 
ATOM   3780 C  CG  . HIS D 1 67  ? 1.974   77.079  3.641   1.00 57.21  ? 67   HIS D CG  1 
ATOM   3781 N  ND1 . HIS D 1 67  ? 1.163   75.966  3.558   1.00 57.81  ? 67   HIS D ND1 1 
ATOM   3782 C  CD2 . HIS D 1 67  ? 2.308   77.395  2.368   1.00 53.79  ? 67   HIS D CD2 1 
ATOM   3783 C  CE1 . HIS D 1 67  ? 1.008   75.628  2.290   1.00 59.42  ? 67   HIS D CE1 1 
ATOM   3784 N  NE2 . HIS D 1 67  ? 1.697   76.477  1.547   1.00 63.55  ? 67   HIS D NE2 1 
ATOM   3785 N  N   . SER D 1 68  ? 0.912   79.218  7.841   1.00 51.90  ? 68   SER D N   1 
ATOM   3786 C  CA  . SER D 1 68  ? 1.330   79.959  9.024   1.00 50.22  ? 68   SER D CA  1 
ATOM   3787 C  C   . SER D 1 68  ? 2.786   80.420  8.911   1.00 50.23  ? 68   SER D C   1 
ATOM   3788 O  O   . SER D 1 68  ? 3.605   80.106  9.773   1.00 51.12  ? 68   SER D O   1 
ATOM   3789 C  CB  . SER D 1 68  ? 1.145   79.098  10.282  1.00 53.15  ? 68   SER D CB  1 
ATOM   3790 O  OG  . SER D 1 68  ? 0.077   78.171  10.125  1.00 49.34  ? 68   SER D OG  1 
ATOM   3791 N  N   . LYS D 1 69  ? 3.112   81.154  7.846   1.00 53.53  ? 69   LYS D N   1 
ATOM   3792 C  CA  . LYS D 1 69  ? 4.430   81.806  7.731   1.00 51.32  ? 69   LYS D CA  1 
ATOM   3793 C  C   . LYS D 1 69  ? 4.351   83.246  8.265   1.00 47.39  ? 69   LYS D C   1 
ATOM   3794 O  O   . LYS D 1 69  ? 3.270   83.727  8.603   1.00 43.72  ? 69   LYS D O   1 
ATOM   3795 C  CB  . LYS D 1 69  ? 4.943   81.803  6.272   1.00 48.98  ? 69   LYS D CB  1 
ATOM   3796 C  CG  . LYS D 1 69  ? 5.138   80.407  5.633   1.00 52.83  ? 69   LYS D CG  1 
ATOM   3797 C  CD  . LYS D 1 69  ? 6.217   80.412  4.512   1.00 57.56  ? 69   LYS D CD  1 
ATOM   3798 C  CE  . LYS D 1 69  ? 5.648   80.653  3.086   1.00 55.88  ? 69   LYS D CE  1 
ATOM   3799 N  NZ  . LYS D 1 69  ? 6.710   80.896  2.032   1.00 37.92  ? 69   LYS D NZ  1 
ATOM   3800 N  N   . LYS D 1 70  ? 5.491   83.926  8.344   1.00 48.19  ? 70   LYS D N   1 
ATOM   3801 C  CA  . LYS D 1 70  ? 5.522   85.351  8.679   1.00 41.90  ? 70   LYS D CA  1 
ATOM   3802 C  C   . LYS D 1 70  ? 5.219   86.201  7.444   1.00 51.01  ? 70   LYS D C   1 
ATOM   3803 O  O   . LYS D 1 70  ? 5.366   85.744  6.296   1.00 46.08  ? 70   LYS D O   1 
ATOM   3804 C  CB  . LYS D 1 70  ? 6.900   85.760  9.205   1.00 47.41  ? 70   LYS D CB  1 
ATOM   3805 C  CG  . LYS D 1 70  ? 7.335   85.060  10.477  1.00 52.97  ? 70   LYS D CG  1 
ATOM   3806 C  CD  . LYS D 1 70  ? 8.647   85.622  11.011  1.00 58.10  ? 70   LYS D CD  1 
ATOM   3807 C  CE  . LYS D 1 70  ? 9.086   84.879  12.288  1.00 72.61  ? 70   LYS D CE  1 
ATOM   3808 N  NZ  . LYS D 1 70  ? 7.993   84.712  13.310  1.00 56.30  ? 70   LYS D NZ  1 
ATOM   3809 N  N   . HIS D 1 71  ? 4.822   87.450  7.675   1.00 47.49  ? 71   HIS D N   1 
ATOM   3810 C  CA  . HIS D 1 71  ? 4.509   88.337  6.570   1.00 43.94  ? 71   HIS D CA  1 
ATOM   3811 C  C   . HIS D 1 71  ? 5.756   88.683  5.764   1.00 44.16  ? 71   HIS D C   1 
ATOM   3812 O  O   . HIS D 1 71  ? 6.838   88.857  6.334   1.00 44.20  ? 71   HIS D O   1 
ATOM   3813 C  CB  . HIS D 1 71  ? 3.850   89.631  7.051   1.00 41.91  ? 71   HIS D CB  1 
ATOM   3814 C  CG  . HIS D 1 71  ? 3.551   90.575  5.935   1.00 38.37  ? 71   HIS D CG  1 
ATOM   3815 N  ND1 . HIS D 1 71  ? 2.449   90.428  5.125   1.00 29.97  ? 71   HIS D ND1 1 
ATOM   3816 C  CD2 . HIS D 1 71  ? 4.246   91.628  5.441   1.00 37.45  ? 71   HIS D CD2 1 
ATOM   3817 C  CE1 . HIS D 1 71  ? 2.458   91.367  4.198   1.00 32.42  ? 71   HIS D CE1 1 
ATOM   3818 N  NE2 . HIS D 1 71  ? 3.536   92.111  4.369   1.00 34.06  ? 71   HIS D NE2 1 
ATOM   3819 N  N   . GLY D 1 72  ? 5.593   88.799  4.444   1.00 39.28  ? 72   GLY D N   1 
ATOM   3820 C  CA  . GLY D 1 72  ? 6.665   89.284  3.586   1.00 40.52  ? 72   GLY D CA  1 
ATOM   3821 C  C   . GLY D 1 72  ? 6.208   89.884  2.263   1.00 39.97  ? 72   GLY D C   1 
ATOM   3822 O  O   . GLY D 1 72  ? 5.017   90.025  2.006   1.00 33.68  ? 72   GLY D O   1 
ATOM   3823 N  N   . GLY D 1 73  ? 7.174   90.237  1.420   1.00 44.18  ? 73   GLY D N   1 
ATOM   3824 C  CA  . GLY D 1 73  ? 6.904   90.733  0.083   1.00 42.32  ? 73   GLY D CA  1 
ATOM   3825 C  C   . GLY D 1 73  ? 6.551   89.599  -0.864  1.00 48.31  ? 73   GLY D C   1 
ATOM   3826 O  O   . GLY D 1 73  ? 6.786   88.434  -0.551  1.00 50.40  ? 73   GLY D O   1 
ATOM   3827 N  N   . PRO D 1 74  ? 5.980   89.929  -2.033  1.00 49.23  ? 74   PRO D N   1 
ATOM   3828 C  CA  . PRO D 1 74  ? 5.529   88.866  -2.937  1.00 47.64  ? 74   PRO D CA  1 
ATOM   3829 C  C   . PRO D 1 74  ? 6.680   87.975  -3.409  1.00 46.75  ? 74   PRO D C   1 
ATOM   3830 O  O   . PRO D 1 74  ? 6.455   86.855  -3.855  1.00 48.98  ? 74   PRO D O   1 
ATOM   3831 C  CB  . PRO D 1 74  ? 4.919   89.641  -4.127  1.00 47.88  ? 74   PRO D CB  1 
ATOM   3832 C  CG  . PRO D 1 74  ? 4.691   91.045  -3.632  1.00 43.14  ? 74   PRO D CG  1 
ATOM   3833 C  CD  . PRO D 1 74  ? 5.779   91.274  -2.608  1.00 46.18  ? 74   PRO D CD  1 
ATOM   3834 N  N   . ALA D 1 75  ? 7.905   88.467  -3.298  1.00 49.05  ? 75   ALA D N   1 
ATOM   3835 C  CA  . ALA D 1 75  ? 9.058   87.741  -3.806  1.00 50.95  ? 75   ALA D CA  1 
ATOM   3836 C  C   . ALA D 1 75  ? 9.878   87.100  -2.688  1.00 53.97  ? 75   ALA D C   1 
ATOM   3837 O  O   . ALA D 1 75  ? 10.803  86.331  -2.955  1.00 56.71  ? 75   ALA D O   1 
ATOM   3838 C  CB  . ALA D 1 75  ? 9.937   88.664  -4.672  1.00 43.03  ? 75   ALA D CB  1 
ATOM   3839 N  N   . ASP D 1 76  ? 9.553   87.409  -1.438  1.00 48.24  ? 76   ASP D N   1 
ATOM   3840 C  CA  . ASP D 1 76  ? 10.283  86.807  -0.326  1.00 50.35  ? 76   ASP D CA  1 
ATOM   3841 C  C   . ASP D 1 76  ? 10.008  85.312  -0.205  1.00 52.90  ? 76   ASP D C   1 
ATOM   3842 O  O   . ASP D 1 76  ? 8.877   84.850  -0.415  1.00 50.74  ? 76   ASP D O   1 
ATOM   3843 C  CB  . ASP D 1 76  ? 9.972   87.515  0.994   1.00 45.32  ? 76   ASP D CB  1 
ATOM   3844 C  CG  . ASP D 1 76  ? 10.507  88.925  1.027   1.00 52.78  ? 76   ASP D CG  1 
ATOM   3845 O  OD1 . ASP D 1 76  ? 11.700  89.120  0.697   1.00 55.78  ? 76   ASP D OD1 1 
ATOM   3846 O  OD2 . ASP D 1 76  ? 9.737   89.846  1.369   1.00 53.60  ? 76   ASP D OD2 1 
ATOM   3847 N  N   . GLU D 1 77  ? 11.052  84.559  0.132   1.00 51.57  ? 77   GLU D N   1 
ATOM   3848 C  CA  . GLU D 1 77  ? 10.898  83.128  0.385   1.00 51.29  ? 77   GLU D CA  1 
ATOM   3849 C  C   . GLU D 1 77  ? 9.927   82.937  1.559   1.00 46.60  ? 77   GLU D C   1 
ATOM   3850 O  O   . GLU D 1 77  ? 9.085   82.042  1.550   1.00 52.37  ? 77   GLU D O   1 
ATOM   3851 C  CB  . GLU D 1 77  ? 12.267  82.469  0.651   1.00 47.88  ? 77   GLU D CB  1 
ATOM   3852 C  CG  . GLU D 1 77  ? 13.274  82.609  -0.521  1.00 40.93  ? 77   GLU D CG  1 
ATOM   3853 C  CD  . GLU D 1 77  ? 14.672  82.028  -0.222  1.00 44.97  ? 77   GLU D CD  1 
ATOM   3854 O  OE1 . GLU D 1 77  ? 15.562  82.794  0.234   1.00 41.84  ? 77   GLU D OE1 1 
ATOM   3855 O  OE2 . GLU D 1 77  ? 14.885  80.807  -0.463  1.00 40.28  ? 77   GLU D OE2 1 
ATOM   3856 N  N   . GLU D 1 78  ? 10.034  83.819  2.546   1.00 45.77  ? 78   GLU D N   1 
ATOM   3857 C  CA  . GLU D 1 78  ? 9.176   83.798  3.726   1.00 47.27  ? 78   GLU D CA  1 
ATOM   3858 C  C   . GLU D 1 78  ? 8.045   84.859  3.630   1.00 49.04  ? 78   GLU D C   1 
ATOM   3859 O  O   . GLU D 1 78  ? 8.277   86.065  3.820   1.00 40.83  ? 78   GLU D O   1 
ATOM   3860 C  CB  . GLU D 1 78  ? 10.051  84.005  4.974   1.00 49.61  ? 78   GLU D CB  1 
ATOM   3861 C  CG  . GLU D 1 78  ? 9.299   84.120  6.295   1.00 49.13  ? 78   GLU D CG  1 
ATOM   3862 C  CD  . GLU D 1 78  ? 8.575   82.841  6.675   1.00 56.21  ? 78   GLU D CD  1 
ATOM   3863 O  OE1 . GLU D 1 78  ? 8.393   81.977  5.785   1.00 56.11  ? 78   GLU D OE1 1 
ATOM   3864 O  OE2 . GLU D 1 78  ? 8.195   82.698  7.865   1.00 52.44  ? 78   GLU D OE2 1 
ATOM   3865 N  N   . ARG D 1 79  ? 6.828   84.399  3.329   1.00 44.58  ? 79   ARG D N   1 
ATOM   3866 C  CA  . ARG D 1 79  ? 5.686   85.287  3.098   1.00 41.15  ? 79   ARG D CA  1 
ATOM   3867 C  C   . ARG D 1 79  ? 4.388   84.530  3.268   1.00 42.41  ? 79   ARG D C   1 
ATOM   3868 O  O   . ARG D 1 79  ? 4.373   83.310  3.179   1.00 40.83  ? 79   ARG D O   1 
ATOM   3869 C  CB  . ARG D 1 79  ? 5.720   85.869  1.672   1.00 44.30  ? 79   ARG D CB  1 
ATOM   3870 C  CG  . ARG D 1 79  ? 5.698   84.812  0.561   1.00 41.75  ? 79   ARG D CG  1 
ATOM   3871 C  CD  . ARG D 1 79  ? 5.322   85.379  -0.809  1.00 44.06  ? 79   ARG D CD  1 
ATOM   3872 N  NE  . ARG D 1 79  ? 3.874   85.426  -0.998  1.00 42.76  ? 79   ARG D NE  1 
ATOM   3873 C  CZ  . ARG D 1 79  ? 3.261   85.679  -2.149  1.00 40.05  ? 79   ARG D CZ  1 
ATOM   3874 N  NH1 . ARG D 1 79  ? 3.961   85.909  -3.247  1.00 44.62  ? 79   ARG D NH1 1 
ATOM   3875 N  NH2 . ARG D 1 79  ? 1.937   85.703  -2.202  1.00 39.49  ? 79   ARG D NH2 1 
ATOM   3876 N  N   . HIS D 1 80  ? 3.293   85.256  3.503   1.00 43.60  ? 80   HIS D N   1 
ATOM   3877 C  CA  . HIS D 1 80  ? 1.960   84.650  3.508   1.00 41.29  ? 80   HIS D CA  1 
ATOM   3878 C  C   . HIS D 1 80  ? 1.533   84.440  2.065   1.00 39.87  ? 80   HIS D C   1 
ATOM   3879 O  O   . HIS D 1 80  ? 2.035   85.107  1.168   1.00 40.32  ? 80   HIS D O   1 
ATOM   3880 C  CB  . HIS D 1 80  ? 0.934   85.543  4.230   1.00 43.31  ? 80   HIS D CB  1 
ATOM   3881 C  CG  . HIS D 1 80  ? 1.327   85.925  5.630   1.00 48.83  ? 80   HIS D CG  1 
ATOM   3882 N  ND1 . HIS D 1 80  ? 0.720   86.954  6.321   1.00 45.87  ? 80   HIS D ND1 1 
ATOM   3883 C  CD2 . HIS D 1 80  ? 2.266   85.420  6.466   1.00 49.17  ? 80   HIS D CD2 1 
ATOM   3884 C  CE1 . HIS D 1 80  ? 1.266   87.069  7.517   1.00 42.33  ? 80   HIS D CE1 1 
ATOM   3885 N  NE2 . HIS D 1 80  ? 2.212   86.155  7.628   1.00 51.97  ? 80   HIS D NE2 1 
ATOM   3886 N  N   . VAL D 1 81  ? 0.610   83.518  1.833   1.00 40.12  ? 81   VAL D N   1 
ATOM   3887 C  CA  . VAL D 1 81  ? 0.067   83.351  0.491   1.00 42.73  ? 81   VAL D CA  1 
ATOM   3888 C  C   . VAL D 1 81  ? -0.429  84.685  -0.104  1.00 40.24  ? 81   VAL D C   1 
ATOM   3889 O  O   . VAL D 1 81  ? -0.058  85.052  -1.216  1.00 41.80  ? 81   VAL D O   1 
ATOM   3890 C  CB  . VAL D 1 81  ? -1.051  82.284  0.458   1.00 44.38  ? 81   VAL D CB  1 
ATOM   3891 C  CG1 . VAL D 1 81  ? -1.779  82.296  -0.885  1.00 46.72  ? 81   VAL D CG1 1 
ATOM   3892 C  CG2 . VAL D 1 81  ? -0.468  80.910  0.724   1.00 48.40  ? 81   VAL D CG2 1 
ATOM   3893 N  N   . GLY D 1 82  ? -1.246  85.409  0.655   1.00 38.99  ? 82   GLY D N   1 
ATOM   3894 C  CA  . GLY D 1 82  ? -1.879  86.632  0.180   1.00 40.78  ? 82   GLY D CA  1 
ATOM   3895 C  C   . GLY D 1 82  ? -1.039  87.908  0.159   1.00 37.46  ? 82   GLY D C   1 
ATOM   3896 O  O   . GLY D 1 82  ? -1.563  89.002  -0.054  1.00 38.19  ? 82   GLY D O   1 
ATOM   3897 N  N   . ASP D 1 83  ? 0.262   87.776  0.370   1.00 35.67  ? 83   ASP D N   1 
ATOM   3898 C  CA  . ASP D 1 83  ? 1.142   88.928  0.354   1.00 37.97  ? 83   ASP D CA  1 
ATOM   3899 C  C   . ASP D 1 83  ? 1.434   89.437  -1.060  1.00 39.49  ? 83   ASP D C   1 
ATOM   3900 O  O   . ASP D 1 83  ? 2.526   89.206  -1.603  1.00 38.93  ? 83   ASP D O   1 
ATOM   3901 C  CB  . ASP D 1 83  ? 2.444   88.622  1.102   1.00 38.57  ? 83   ASP D CB  1 
ATOM   3902 C  CG  . ASP D 1 83  ? 2.236   88.524  2.594   1.00 39.32  ? 83   ASP D CG  1 
ATOM   3903 O  OD1 . ASP D 1 83  ? 1.052   88.418  2.980   1.00 39.18  ? 83   ASP D OD1 1 
ATOM   3904 O  OD2 . ASP D 1 83  ? 3.235   88.540  3.367   1.00 38.91  ? 83   ASP D OD2 1 
ATOM   3905 N  N   . LEU D 1 84  ? 0.470   90.153  -1.643  1.00 31.79  ? 84   LEU D N   1 
ATOM   3906 C  CA  . LEU D 1 84  ? 0.663   90.686  -2.995  1.00 38.56  ? 84   LEU D CA  1 
ATOM   3907 C  C   . LEU D 1 84  ? 1.423   92.013  -3.039  1.00 38.20  ? 84   LEU D C   1 
ATOM   3908 O  O   . LEU D 1 84  ? 1.344   92.741  -4.030  1.00 42.72  ? 84   LEU D O   1 
ATOM   3909 C  CB  . LEU D 1 84  ? -0.665  90.818  -3.739  1.00 32.02  ? 84   LEU D CB  1 
ATOM   3910 C  CG  . LEU D 1 84  ? -1.357  89.496  -4.056  1.00 37.41  ? 84   LEU D CG  1 
ATOM   3911 C  CD1 . LEU D 1 84  ? -2.743  89.712  -4.712  1.00 33.36  ? 84   LEU D CD1 1 
ATOM   3912 C  CD2 . LEU D 1 84  ? -0.438  88.666  -4.949  1.00 38.68  ? 84   LEU D CD2 1 
ATOM   3913 N  N   . GLY D 1 85  ? 2.148   92.329  -1.972  1.00 33.86  ? 85   GLY D N   1 
ATOM   3914 C  CA  . GLY D 1 85  ? 2.971   93.524  -1.916  1.00 29.48  ? 85   GLY D CA  1 
ATOM   3915 C  C   . GLY D 1 85  ? 2.266   94.870  -2.006  1.00 32.11  ? 85   GLY D C   1 
ATOM   3916 O  O   . GLY D 1 85  ? 1.237   95.099  -1.368  1.00 30.43  ? 85   GLY D O   1 
ATOM   3917 N  N   . ASN D 1 86  ? 2.848   95.758  -2.814  1.00 37.36  ? 86   ASN D N   1 
ATOM   3918 C  CA  . ASN D 1 86  ? 2.385   97.134  -2.988  1.00 34.21  ? 86   ASN D CA  1 
ATOM   3919 C  C   . ASN D 1 86  ? 1.873   97.508  -4.373  1.00 33.58  ? 86   ASN D C   1 
ATOM   3920 O  O   . ASN D 1 86  ? 2.460   97.184  -5.397  1.00 35.85  ? 86   ASN D O   1 
ATOM   3921 C  CB  . ASN D 1 86  ? 3.484   98.120  -2.605  1.00 29.54  ? 86   ASN D CB  1 
ATOM   3922 C  CG  . ASN D 1 86  ? 3.577   98.308  -1.126  1.00 32.37  ? 86   ASN D CG  1 
ATOM   3923 O  OD1 . ASN D 1 86  ? 2.624   98.750  -0.491  1.00 34.92  ? 86   ASN D OD1 1 
ATOM   3924 N  ND2 . ASN D 1 86  ? 4.717   97.969  -0.560  1.00 29.32  ? 86   ASN D ND2 1 
ATOM   3925 N  N   . VAL D 1 87  ? 0.781   98.245  -4.361  1.00 30.67  ? 87   VAL D N   1 
ATOM   3926 C  CA  . VAL D 1 87  ? 0.218   98.882  -5.524  1.00 28.35  ? 87   VAL D CA  1 
ATOM   3927 C  C   . VAL D 1 87  ? 0.550   100.400 -5.441  1.00 34.28  ? 87   VAL D C   1 
ATOM   3928 O  O   . VAL D 1 87  ? 0.707   100.948 -4.343  1.00 32.88  ? 87   VAL D O   1 
ATOM   3929 C  CB  . VAL D 1 87  ? -1.283  98.614  -5.472  1.00 32.67  ? 87   VAL D CB  1 
ATOM   3930 C  CG1 . VAL D 1 87  ? -2.061  99.890  -5.486  1.00 35.96  ? 87   VAL D CG1 1 
ATOM   3931 C  CG2 . VAL D 1 87  ? -1.718  97.615  -6.543  1.00 29.59  ? 87   VAL D CG2 1 
ATOM   3932 N  N   . THR D 1 88  ? 0.694   101.075 -6.579  1.00 29.08  ? 88   THR D N   1 
ATOM   3933 C  CA  . THR D 1 88  ? 1.085   102.490 -6.576  1.00 28.89  ? 88   THR D CA  1 
ATOM   3934 C  C   . THR D 1 88  ? 0.030   103.471 -7.155  1.00 30.14  ? 88   THR D C   1 
ATOM   3935 O  O   . THR D 1 88  ? -0.360  103.371 -8.318  1.00 28.75  ? 88   THR D O   1 
ATOM   3936 C  CB  . THR D 1 88  ? 2.434   102.708 -7.320  1.00 31.21  ? 88   THR D CB  1 
ATOM   3937 O  OG1 . THR D 1 88  ? 3.467   101.923 -6.705  1.00 28.71  ? 88   THR D OG1 1 
ATOM   3938 C  CG2 . THR D 1 88  ? 2.838   104.181 -7.270  1.00 30.57  ? 88   THR D CG2 1 
ATOM   3939 N  N   . ALA D 1 89  ? -0.435  104.420 -6.346  1.00 30.15  ? 89   ALA D N   1 
ATOM   3940 C  CA  . ALA D 1 89  ? -1.350  105.440 -6.852  1.00 26.67  ? 89   ALA D CA  1 
ATOM   3941 C  C   . ALA D 1 89  ? -0.555  106.637 -7.390  1.00 29.21  ? 89   ALA D C   1 
ATOM   3942 O  O   . ALA D 1 89  ? 0.441   107.026 -6.799  1.00 24.85  ? 89   ALA D O   1 
ATOM   3943 C  CB  . ALA D 1 89  ? -2.297  105.874 -5.793  1.00 21.82  ? 89   ALA D CB  1 
ATOM   3944 N  N   . ASP D 1 90  ? -0.986  107.187 -8.528  1.00 31.91  ? 90   ASP D N   1 
ATOM   3945 C  CA  . ASP D 1 90  ? -0.385  108.394 -9.109  1.00 33.75  ? 90   ASP D CA  1 
ATOM   3946 C  C   . ASP D 1 90  ? -0.954  109.686 -8.480  1.00 36.64  ? 90   ASP D C   1 
ATOM   3947 O  O   . ASP D 1 90  ? -1.756  109.617 -7.555  1.00 36.32  ? 90   ASP D O   1 
ATOM   3948 C  CB  . ASP D 1 90  ? -0.512  108.398 -10.651 1.00 36.58  ? 90   ASP D CB  1 
ATOM   3949 C  CG  . ASP D 1 90  ? -1.966  108.612 -11.153 1.00 41.78  ? 90   ASP D CG  1 
ATOM   3950 O  OD1 . ASP D 1 90  ? -2.793  109.180 -10.412 1.00 41.18  ? 90   ASP D OD1 1 
ATOM   3951 O  OD2 . ASP D 1 90  ? -2.288  108.223 -12.308 1.00 45.75  ? 90   ASP D OD2 1 
ATOM   3952 N  N   . LYS D 1 91  ? -0.536  110.850 -8.980  1.00 40.85  ? 91   LYS D N   1 
ATOM   3953 C  CA  . LYS D 1 91  ? -0.943  112.137 -8.409  1.00 39.07  ? 91   LYS D CA  1 
ATOM   3954 C  C   . LYS D 1 91  ? -2.450  112.351 -8.482  1.00 41.93  ? 91   LYS D C   1 
ATOM   3955 O  O   . LYS D 1 91  ? -2.992  113.201 -7.785  1.00 43.51  ? 91   LYS D O   1 
ATOM   3956 C  CB  . LYS D 1 91  ? -0.271  113.286 -9.148  1.00 42.07  ? 91   LYS D CB  1 
ATOM   3957 C  CG  . LYS D 1 91  ? -0.770  113.387 -10.595 1.00 54.97  ? 91   LYS D CG  1 
ATOM   3958 C  CD  . LYS D 1 91  ? -0.171  114.562 -11.372 1.00 62.22  ? 91   LYS D CD  1 
ATOM   3959 C  CE  . LYS D 1 91  ? -0.619  114.544 -12.856 1.00 67.04  ? 91   LYS D CE  1 
ATOM   3960 N  NZ  . LYS D 1 91  ? -2.088  114.806 -13.088 1.00 55.53  ? 91   LYS D NZ  1 
ATOM   3961 N  N   . ASP D 1 92  ? -3.135  111.604 -9.335  1.00 38.51  ? 92   ASP D N   1 
ATOM   3962 C  CA  . ASP D 1 92  ? -4.581  111.788 -9.464  1.00 42.23  ? 92   ASP D CA  1 
ATOM   3963 C  C   . ASP D 1 92  ? -5.392  110.748 -8.710  1.00 38.89  ? 92   ASP D C   1 
ATOM   3964 O  O   . ASP D 1 92  ? -6.599  110.618 -8.924  1.00 37.92  ? 92   ASP D O   1 
ATOM   3965 C  CB  . ASP D 1 92  ? -5.017  111.860 -10.937 1.00 45.95  ? 92   ASP D CB  1 
ATOM   3966 C  CG  . ASP D 1 92  ? -5.052  113.301 -11.466 1.00 57.54  ? 92   ASP D CG  1 
ATOM   3967 O  OD1 . ASP D 1 92  ? -5.737  114.167 -10.849 1.00 50.93  ? 92   ASP D OD1 1 
ATOM   3968 O  OD2 . ASP D 1 92  ? -4.382  113.564 -12.493 1.00 60.20  ? 92   ASP D OD2 1 
ATOM   3969 N  N   . GLY D 1 93  ? -4.725  110.012 -7.830  1.00 30.90  ? 93   GLY D N   1 
ATOM   3970 C  CA  . GLY D 1 93  ? -5.410  109.073 -6.976  1.00 34.74  ? 93   GLY D CA  1 
ATOM   3971 C  C   . GLY D 1 93  ? -5.646  107.686 -7.536  1.00 33.17  ? 93   GLY D C   1 
ATOM   3972 O  O   . GLY D 1 93  ? -6.334  106.901 -6.899  1.00 34.49  ? 93   GLY D O   1 
ATOM   3973 N  N   . VAL D 1 94  ? -5.071  107.384 -8.700  1.00 31.34  ? 94   VAL D N   1 
ATOM   3974 C  CA  . VAL D 1 94  ? -5.282  106.104 -9.389  1.00 27.47  ? 94   VAL D CA  1 
ATOM   3975 C  C   . VAL D 1 94  ? -4.091  105.132 -9.271  1.00 27.78  ? 94   VAL D C   1 
ATOM   3976 O  O   . VAL D 1 94  ? -2.929  105.509 -9.467  1.00 26.83  ? 94   VAL D O   1 
ATOM   3977 C  CB  . VAL D 1 94  ? -5.605  106.324 -10.897 1.00 31.96  ? 94   VAL D CB  1 
ATOM   3978 C  CG1 . VAL D 1 94  ? -5.774  104.983 -11.615 1.00 31.05  ? 94   VAL D CG1 1 
ATOM   3979 C  CG2 . VAL D 1 94  ? -6.849  107.204 -11.080 1.00 26.83  ? 94   VAL D CG2 1 
ATOM   3980 N  N   . ALA D 1 95  ? -4.372  103.883 -8.922  1.00 26.93  ? 95   ALA D N   1 
ATOM   3981 C  CA  . ALA D 1 95  ? -3.347  102.841 -9.041  1.00 32.38  ? 95   ALA D CA  1 
ATOM   3982 C  C   . ALA D 1 95  ? -3.728  101.849 -10.138 1.00 27.80  ? 95   ALA D C   1 
ATOM   3983 O  O   . ALA D 1 95  ? -4.818  101.291 -10.126 1.00 26.43  ? 95   ALA D O   1 
ATOM   3984 C  CB  . ALA D 1 95  ? -3.117  102.115 -7.713  1.00 26.18  ? 95   ALA D CB  1 
ATOM   3985 N  N   . ASP D 1 96  ? -2.837  101.651 -11.097 1.00 29.23  ? 96   ASP D N   1 
ATOM   3986 C  CA  . ASP D 1 96  ? -3.079  100.656 -12.130 1.00 33.14  ? 96   ASP D CA  1 
ATOM   3987 C  C   . ASP D 1 96  ? -2.433  99.348  -11.697 1.00 36.65  ? 96   ASP D C   1 
ATOM   3988 O  O   . ASP D 1 96  ? -1.218  99.297  -11.446 1.00 36.57  ? 96   ASP D O   1 
ATOM   3989 C  CB  . ASP D 1 96  ? -2.540  101.100 -13.494 1.00 36.08  ? 96   ASP D CB  1 
ATOM   3990 C  CG  . ASP D 1 96  ? -2.764  100.045 -14.578 1.00 40.00  ? 96   ASP D CG  1 
ATOM   3991 O  OD1 . ASP D 1 96  ? -3.933  99.824  -15.000 1.00 35.89  ? 96   ASP D OD1 1 
ATOM   3992 O  OD2 . ASP D 1 96  ? -1.764  99.425  -15.001 1.00 45.41  ? 96   ASP D OD2 1 
ATOM   3993 N  N   . VAL D 1 97  ? -3.250  98.298  -11.618 1.00 31.89  ? 97   VAL D N   1 
ATOM   3994 C  CA  . VAL D 1 97  ? -2.813  97.026  -11.066 1.00 36.10  ? 97   VAL D CA  1 
ATOM   3995 C  C   . VAL D 1 97  ? -2.392  95.984  -12.100 1.00 35.80  ? 97   VAL D C   1 
ATOM   3996 O  O   . VAL D 1 97  ? -3.192  95.522  -12.892 1.00 37.92  ? 97   VAL D O   1 
ATOM   3997 C  CB  . VAL D 1 97  ? -3.896  96.425  -10.193 1.00 38.10  ? 97   VAL D CB  1 
ATOM   3998 C  CG1 . VAL D 1 97  ? -3.377  95.140  -9.566  1.00 34.33  ? 97   VAL D CG1 1 
ATOM   3999 C  CG2 . VAL D 1 97  ? -4.323  97.452  -9.128  1.00 33.36  ? 97   VAL D CG2 1 
ATOM   4000 N  N   . SER D 1 98  ? -1.126  95.612  -12.058 1.00 34.90  ? 98   SER D N   1 
ATOM   4001 C  CA  . SER D 1 98  ? -0.565  94.640  -12.978 1.00 39.83  ? 98   SER D CA  1 
ATOM   4002 C  C   . SER D 1 98  ? 0.372   93.731  -12.191 1.00 37.14  ? 98   SER D C   1 
ATOM   4003 O  O   . SER D 1 98  ? 1.491   94.110  -11.846 1.00 39.76  ? 98   SER D O   1 
ATOM   4004 C  CB  . SER D 1 98  ? 0.216   95.343  -14.090 1.00 38.22  ? 98   SER D CB  1 
ATOM   4005 O  OG  . SER D 1 98  ? 0.890   94.382  -14.887 1.00 49.38  ? 98   SER D OG  1 
ATOM   4006 N  N   . ILE D 1 99  ? -0.091  92.533  -11.887 1.00 36.85  ? 99   ILE D N   1 
ATOM   4007 C  CA  . ILE D 1 99  ? 0.624   91.693  -10.944 1.00 39.30  ? 99   ILE D CA  1 
ATOM   4008 C  C   . ILE D 1 99  ? 0.533   90.244  -11.368 1.00 40.94  ? 99   ILE D C   1 
ATOM   4009 O  O   . ILE D 1 99  ? -0.567  89.715  -11.598 1.00 40.72  ? 99   ILE D O   1 
ATOM   4010 C  CB  . ILE D 1 99  ? 0.039   91.814  -9.515  1.00 36.33  ? 99   ILE D CB  1 
ATOM   4011 C  CG1 . ILE D 1 99  ? 0.137   93.252  -8.997  1.00 33.52  ? 99   ILE D CG1 1 
ATOM   4012 C  CG2 . ILE D 1 99  ? 0.773   90.878  -8.558  1.00 43.54  ? 99   ILE D CG2 1 
ATOM   4013 C  CD1 . ILE D 1 99  ? -0.470  93.444  -7.621  1.00 34.21  ? 99   ILE D CD1 1 
ATOM   4014 N  N   . GLU D 1 100 ? 1.699   89.613  -11.461 1.00 41.37  ? 100  GLU D N   1 
ATOM   4015 C  CA  . GLU D 1 100 ? 1.801   88.196  -11.759 1.00 47.14  ? 100  GLU D CA  1 
ATOM   4016 C  C   . GLU D 1 100 ? 2.241   87.467  -10.492 1.00 46.91  ? 100  GLU D C   1 
ATOM   4017 O  O   . GLU D 1 100 ? 3.319   87.752  -9.951  1.00 40.07  ? 100  GLU D O   1 
ATOM   4018 C  CB  . GLU D 1 100 ? 2.812   87.966  -12.892 1.00 43.51  ? 100  GLU D CB  1 
ATOM   4019 C  CG  . GLU D 1 100 ? 3.111   86.496  -13.192 1.00 53.97  ? 100  GLU D CG  1 
ATOM   4020 C  CD  . GLU D 1 100 ? 3.151   86.177  -14.685 1.00 62.66  ? 100  GLU D CD  1 
ATOM   4021 O  OE1 . GLU D 1 100 ? 3.253   87.123  -15.509 1.00 63.85  ? 100  GLU D OE1 1 
ATOM   4022 O  OE2 . GLU D 1 100 ? 3.077   84.975  -15.029 1.00 54.98  ? 100  GLU D OE2 1 
ATOM   4023 N  N   . ASP D 1 101 ? 1.418   86.539  -10.005 1.00 40.53  ? 101  ASP D N   1 
ATOM   4024 C  CA  . ASP D 1 101 ? 1.790   85.851  -8.772  1.00 50.67  ? 101  ASP D CA  1 
ATOM   4025 C  C   . ASP D 1 101 ? 1.781   84.332  -8.859  1.00 49.24  ? 101  ASP D C   1 
ATOM   4026 O  O   . ASP D 1 101 ? 0.803   83.715  -9.295  1.00 43.91  ? 101  ASP D O   1 
ATOM   4027 C  CB  . ASP D 1 101 ? 0.950   86.324  -7.569  1.00 47.93  ? 101  ASP D CB  1 
ATOM   4028 C  CG  . ASP D 1 101 ? 1.540   85.872  -6.234  1.00 46.08  ? 101  ASP D CG  1 
ATOM   4029 O  OD1 . ASP D 1 101 ? 2.503   86.507  -5.755  1.00 44.65  ? 101  ASP D OD1 1 
ATOM   4030 O  OD2 . ASP D 1 101 ? 1.054   84.872  -5.669  1.00 48.59  ? 101  ASP D OD2 1 
ATOM   4031 N  N   . SER D 1 102 ? 2.881   83.737  -8.416  1.00 51.19  ? 102  SER D N   1 
ATOM   4032 C  CA  . SER D 1 102 ? 2.988   82.286  -8.401  1.00 60.03  ? 102  SER D CA  1 
ATOM   4033 C  C   . SER D 1 102 ? 2.180   81.675  -7.248  1.00 57.24  ? 102  SER D C   1 
ATOM   4034 O  O   . SER D 1 102 ? 1.352   80.780  -7.462  1.00 53.55  ? 102  SER D O   1 
ATOM   4035 C  CB  . SER D 1 102 ? 4.454   81.861  -8.334  1.00 60.31  ? 102  SER D CB  1 
ATOM   4036 O  OG  . SER D 1 102 ? 5.162   82.640  -7.387  1.00 66.82  ? 102  SER D OG  1 
ATOM   4037 N  N   . VAL D 1 103 ? 2.390   82.191  -6.040  1.00 54.09  ? 103  VAL D N   1 
ATOM   4038 C  CA  . VAL D 1 103 ? 1.785   81.611  -4.835  1.00 49.95  ? 103  VAL D CA  1 
ATOM   4039 C  C   . VAL D 1 103 ? 0.245   81.569  -4.736  1.00 50.50  ? 103  VAL D C   1 
ATOM   4040 O  O   . VAL D 1 103 ? -0.329  80.521  -4.455  1.00 49.64  ? 103  VAL D O   1 
ATOM   4041 C  CB  . VAL D 1 103 ? 2.327   82.271  -3.589  1.00 48.55  ? 103  VAL D CB  1 
ATOM   4042 C  CG1 . VAL D 1 103 ? 1.857   81.512  -2.364  1.00 48.20  ? 103  VAL D CG1 1 
ATOM   4043 C  CG2 . VAL D 1 103 ? 3.852   82.330  -3.660  1.00 49.79  ? 103  VAL D CG2 1 
ATOM   4044 N  N   . ILE D 1 104 ? -0.437  82.691  -4.928  1.00 50.66  ? 104  ILE D N   1 
ATOM   4045 C  CA  . ILE D 1 104 ? -1.899  82.635  -4.895  1.00 49.35  ? 104  ILE D CA  1 
ATOM   4046 C  C   . ILE D 1 104 ? -2.389  81.742  -6.028  1.00 51.96  ? 104  ILE D C   1 
ATOM   4047 O  O   . ILE D 1 104 ? -1.623  81.397  -6.930  1.00 49.11  ? 104  ILE D O   1 
ATOM   4048 C  CB  . ILE D 1 104 ? -2.545  84.017  -5.037  1.00 44.99  ? 104  ILE D CB  1 
ATOM   4049 C  CG1 . ILE D 1 104 ? -2.053  84.704  -6.311  1.00 47.15  ? 104  ILE D CG1 1 
ATOM   4050 C  CG2 . ILE D 1 104 ? -2.255  84.880  -3.798  1.00 48.94  ? 104  ILE D CG2 1 
ATOM   4051 C  CD1 . ILE D 1 104 ? -2.888  85.915  -6.721  1.00 48.05  ? 104  ILE D CD1 1 
ATOM   4052 N  N   . SER D 1 105 ? -3.663  81.375  -5.996  1.00 45.66  ? 105  SER D N   1 
ATOM   4053 C  CA  . SER D 1 105 ? -4.203  80.533  -7.049  1.00 47.72  ? 105  SER D CA  1 
ATOM   4054 C  C   . SER D 1 105 ? -5.706  80.627  -7.063  1.00 50.03  ? 105  SER D C   1 
ATOM   4055 O  O   . SER D 1 105 ? -6.319  81.022  -6.076  1.00 49.80  ? 105  SER D O   1 
ATOM   4056 C  CB  . SER D 1 105 ? -3.768  79.072  -6.860  1.00 54.07  ? 105  SER D CB  1 
ATOM   4057 O  OG  . SER D 1 105 ? -4.602  78.195  -7.607  1.00 56.26  ? 105  SER D OG  1 
ATOM   4058 N  N   . LEU D 1 106 ? -6.311  80.257  -8.183  1.00 54.75  ? 106  LEU D N   1 
ATOM   4059 C  CA  . LEU D 1 106 ? -7.761  80.312  -8.272  1.00 53.55  ? 106  LEU D CA  1 
ATOM   4060 C  C   . LEU D 1 106 ? -8.373  78.946  -7.977  1.00 54.52  ? 106  LEU D C   1 
ATOM   4061 O  O   . LEU D 1 106 ? -9.576  78.729  -8.162  1.00 57.03  ? 106  LEU D O   1 
ATOM   4062 C  CB  . LEU D 1 106 ? -8.215  80.890  -9.614  1.00 49.13  ? 106  LEU D CB  1 
ATOM   4063 C  CG  . LEU D 1 106 ? -7.741  82.341  -9.814  1.00 52.44  ? 106  LEU D CG  1 
ATOM   4064 C  CD1 . LEU D 1 106 ? -8.320  82.945  -11.093 1.00 49.23  ? 106  LEU D CD1 1 
ATOM   4065 C  CD2 . LEU D 1 106 ? -8.067  83.236  -8.602  1.00 45.57  ? 106  LEU D CD2 1 
ATOM   4066 N  N   . SER D 1 107 ? -7.542  78.037  -7.477  1.00 49.61  ? 107  SER D N   1 
ATOM   4067 C  CA  . SER D 1 107 ? -8.046  76.740  -7.045  1.00 56.09  ? 107  SER D CA  1 
ATOM   4068 C  C   . SER D 1 107 ? -7.015  75.954  -6.247  1.00 57.18  ? 107  SER D C   1 
ATOM   4069 O  O   . SER D 1 107 ? -5.836  76.328  -6.163  1.00 54.74  ? 107  SER D O   1 
ATOM   4070 C  CB  . SER D 1 107 ? -8.505  75.909  -8.246  1.00 57.39  ? 107  SER D CB  1 
ATOM   4071 O  OG  . SER D 1 107 ? -7.393  75.302  -8.880  1.00 59.06  ? 107  SER D OG  1 
ATOM   4072 N  N   . GLY D 1 108 ? -7.472  74.853  -5.660  1.00 60.76  ? 108  GLY D N   1 
ATOM   4073 C  CA  . GLY D 1 108 ? -6.591  73.992  -4.899  1.00 57.71  ? 108  GLY D CA  1 
ATOM   4074 C  C   . GLY D 1 108 ? -6.346  74.510  -3.499  1.00 57.57  ? 108  GLY D C   1 
ATOM   4075 O  O   . GLY D 1 108 ? -7.231  75.124  -2.893  1.00 57.39  ? 108  GLY D O   1 
ATOM   4076 N  N   . ASP D 1 109 ? -5.137  74.261  -2.998  1.00 56.79  ? 109  ASP D N   1 
ATOM   4077 C  CA  . ASP D 1 109 ? -4.778  74.547  -1.612  1.00 57.02  ? 109  ASP D CA  1 
ATOM   4078 C  C   . ASP D 1 109 ? -4.709  76.055  -1.350  1.00 60.53  ? 109  ASP D C   1 
ATOM   4079 O  O   . ASP D 1 109 ? -5.055  76.532  -0.263  1.00 59.94  ? 109  ASP D O   1 
ATOM   4080 C  CB  . ASP D 1 109 ? -3.435  73.884  -1.253  1.00 59.35  ? 109  ASP D CB  1 
ATOM   4081 C  CG  . ASP D 1 109 ? -3.475  72.340  -1.336  1.00 68.81  ? 109  ASP D CG  1 
ATOM   4082 O  OD1 . ASP D 1 109 ? -4.564  71.752  -1.555  1.00 59.19  ? 109  ASP D OD1 1 
ATOM   4083 O  OD2 . ASP D 1 109 ? -2.397  71.714  -1.171  1.00 60.31  ? 109  ASP D OD2 1 
ATOM   4084 N  N   . HIS D 1 110 ? -4.271  76.803  -2.356  1.00 54.29  ? 110  HIS D N   1 
ATOM   4085 C  CA  . HIS D 1 110 ? -4.095  78.235  -2.209  1.00 48.59  ? 110  HIS D CA  1 
ATOM   4086 C  C   . HIS D 1 110 ? -5.256  79.043  -2.780  1.00 47.88  ? 110  HIS D C   1 
ATOM   4087 O  O   . HIS D 1 110 ? -5.179  80.259  -2.874  1.00 46.27  ? 110  HIS D O   1 
ATOM   4088 C  CB  . HIS D 1 110 ? -2.782  78.657  -2.857  1.00 42.51  ? 110  HIS D CB  1 
ATOM   4089 C  CG  . HIS D 1 110 ? -1.572  78.212  -2.102  1.00 41.93  ? 110  HIS D CG  1 
ATOM   4090 N  ND1 . HIS D 1 110 ? -0.289  78.494  -2.517  1.00 44.74  ? 110  HIS D ND1 1 
ATOM   4091 C  CD2 . HIS D 1 110 ? -1.450  77.524  -0.943  1.00 49.06  ? 110  HIS D CD2 1 
ATOM   4092 C  CE1 . HIS D 1 110 ? 0.574   77.989  -1.652  1.00 51.43  ? 110  HIS D CE1 1 
ATOM   4093 N  NE2 . HIS D 1 110 ? -0.105  77.398  -0.685  1.00 50.78  ? 110  HIS D NE2 1 
ATOM   4094 N  N   . CYS D 1 111 ? -6.333  78.373  -3.165  1.00 51.63  ? 111  CYS D N   1 
ATOM   4095 C  CA  . CYS D 1 111 ? -7.443  79.076  -3.792  1.00 50.10  ? 111  CYS D CA  1 
ATOM   4096 C  C   . CYS D 1 111 ? -7.749  80.331  -2.983  1.00 52.36  ? 111  CYS D C   1 
ATOM   4097 O  O   . CYS D 1 111 ? -7.858  80.266  -1.754  1.00 50.69  ? 111  CYS D O   1 
ATOM   4098 C  CB  . CYS D 1 111 ? -8.665  78.182  -3.851  1.00 39.71  ? 111  CYS D CB  1 
ATOM   4099 S  SG  . CYS D 1 111 ? -10.056 78.878  -4.742  1.00 49.86  ? 111  CYS D SG  1 
ATOM   4100 N  N   . ILE D 1 112 ? -7.865  81.472  -3.663  1.00 46.59  ? 112  ILE D N   1 
ATOM   4101 C  CA  . ILE D 1 112 ? -8.145  82.739  -2.987  1.00 42.72  ? 112  ILE D CA  1 
ATOM   4102 C  C   . ILE D 1 112 ? -9.547  83.208  -3.281  1.00 41.10  ? 112  ILE D C   1 
ATOM   4103 O  O   . ILE D 1 112 ? -9.914  84.325  -2.942  1.00 38.71  ? 112  ILE D O   1 
ATOM   4104 C  CB  . ILE D 1 112 ? -7.189  83.851  -3.424  1.00 39.98  ? 112  ILE D CB  1 
ATOM   4105 C  CG1 . ILE D 1 112 ? -7.436  84.200  -4.898  1.00 43.78  ? 112  ILE D CG1 1 
ATOM   4106 C  CG2 . ILE D 1 112 ? -5.752  83.435  -3.202  1.00 41.29  ? 112  ILE D CG2 1 
ATOM   4107 C  CD1 . ILE D 1 112 ? -6.496  85.234  -5.451  1.00 39.39  ? 112  ILE D CD1 1 
ATOM   4108 N  N   . ILE D 1 113 ? -10.332 82.359  -3.927  1.00 41.78  ? 113  ILE D N   1 
ATOM   4109 C  CA  . ILE D 1 113 ? -11.708 82.716  -4.252  1.00 39.43  ? 113  ILE D CA  1 
ATOM   4110 C  C   . ILE D 1 113 ? -12.617 82.560  -3.045  1.00 38.98  ? 113  ILE D C   1 
ATOM   4111 O  O   . ILE D 1 113 ? -12.491 81.596  -2.294  1.00 41.74  ? 113  ILE D O   1 
ATOM   4112 C  CB  . ILE D 1 113 ? -12.223 81.872  -5.411  1.00 42.68  ? 113  ILE D CB  1 
ATOM   4113 C  CG1 . ILE D 1 113 ? -11.796 82.518  -6.725  1.00 46.16  ? 113  ILE D CG1 1 
ATOM   4114 C  CG2 . ILE D 1 113 ? -13.740 81.732  -5.355  1.00 41.64  ? 113  ILE D CG2 1 
ATOM   4115 C  CD1 . ILE D 1 113 ? -11.793 81.561  -7.892  1.00 53.15  ? 113  ILE D CD1 1 
ATOM   4116 N  N   . GLY D 1 114 ? -13.538 83.503  -2.861  1.00 40.19  ? 114  GLY D N   1 
ATOM   4117 C  CA  . GLY D 1 114 ? -14.397 83.515  -1.690  1.00 34.18  ? 114  GLY D CA  1 
ATOM   4118 C  C   . GLY D 1 114 ? -13.664 84.175  -0.525  1.00 37.21  ? 114  GLY D C   1 
ATOM   4119 O  O   . GLY D 1 114 ? -14.201 84.351  0.564   1.00 35.97  ? 114  GLY D O   1 
ATOM   4120 N  N   . ARG D 1 115 ? -12.411 84.525  -0.759  1.00 34.17  ? 115  ARG D N   1 
ATOM   4121 C  CA  . ARG D 1 115 ? -11.648 85.269  0.216   1.00 35.97  ? 115  ARG D CA  1 
ATOM   4122 C  C   . ARG D 1 115 ? -11.793 86.761  -0.101  1.00 38.59  ? 115  ARG D C   1 
ATOM   4123 O  O   . ARG D 1 115 ? -12.648 87.143  -0.908  1.00 36.84  ? 115  ARG D O   1 
ATOM   4124 C  CB  . ARG D 1 115 ? -10.197 84.807  0.200   1.00 36.83  ? 115  ARG D CB  1 
ATOM   4125 C  CG  . ARG D 1 115 ? -10.087 83.305  0.413   1.00 39.44  ? 115  ARG D CG  1 
ATOM   4126 C  CD  . ARG D 1 115 ? -8.790  82.912  1.085   1.00 47.13  ? 115  ARG D CD  1 
ATOM   4127 N  NE  . ARG D 1 115 ? -8.650  81.461  1.172   1.00 55.27  ? 115  ARG D NE  1 
ATOM   4128 C  CZ  . ARG D 1 115 ? -9.252  80.694  2.079   1.00 55.26  ? 115  ARG D CZ  1 
ATOM   4129 N  NH1 . ARG D 1 115 ? -10.058 81.230  2.991   1.00 53.67  ? 115  ARG D NH1 1 
ATOM   4130 N  NH2 . ARG D 1 115 ? -9.053  79.383  2.066   1.00 49.00  ? 115  ARG D NH2 1 
ATOM   4131 N  N   . THR D 1 116 ? -10.994 87.608  0.539   1.00 39.22  ? 116  THR D N   1 
ATOM   4132 C  CA  . THR D 1 116 ? -11.191 89.052  0.399   1.00 32.32  ? 116  THR D CA  1 
ATOM   4133 C  C   . THR D 1 116 ? -9.931  89.796  0.003   1.00 31.77  ? 116  THR D C   1 
ATOM   4134 O  O   . THR D 1 116 ? -8.864  89.567  0.572   1.00 32.08  ? 116  THR D O   1 
ATOM   4135 C  CB  . THR D 1 116 ? -11.813 89.674  1.659   1.00 28.52  ? 116  THR D CB  1 
ATOM   4136 O  OG1 . THR D 1 116 ? -13.189 89.286  1.734   1.00 31.66  ? 116  THR D OG1 1 
ATOM   4137 C  CG2 . THR D 1 116 ? -11.736 91.178  1.617   1.00 26.93  ? 116  THR D CG2 1 
ATOM   4138 N  N   . LEU D 1 117 ? -10.067 90.667  -1.002  1.00 31.64  ? 117  LEU D N   1 
ATOM   4139 C  CA  . LEU D 1 117 ? -8.996  91.569  -1.402  1.00 29.93  ? 117  LEU D CA  1 
ATOM   4140 C  C   . LEU D 1 117 ? -9.144  92.922  -0.697  1.00 28.62  ? 117  LEU D C   1 
ATOM   4141 O  O   . LEU D 1 117 ? -10.250 93.477  -0.598  1.00 25.94  ? 117  LEU D O   1 
ATOM   4142 C  CB  . LEU D 1 117 ? -8.985  91.759  -2.921  1.00 28.57  ? 117  LEU D CB  1 
ATOM   4143 C  CG  . LEU D 1 117 ? -7.748  92.461  -3.479  1.00 28.08  ? 117  LEU D CG  1 
ATOM   4144 C  CD1 . LEU D 1 117 ? -6.463  91.701  -3.135  1.00 29.23  ? 117  LEU D CD1 1 
ATOM   4145 C  CD2 . LEU D 1 117 ? -7.872  92.663  -4.993  1.00 32.33  ? 117  LEU D CD2 1 
ATOM   4146 N  N   . VAL D 1 118 ? -8.014  93.443  -0.229  1.00 25.49  ? 118  VAL D N   1 
ATOM   4147 C  CA  . VAL D 1 118 ? -7.972  94.671  0.550   1.00 25.59  ? 118  VAL D CA  1 
ATOM   4148 C  C   . VAL D 1 118 ? -6.848  95.582  0.088   1.00 24.54  ? 118  VAL D C   1 
ATOM   4149 O  O   . VAL D 1 118 ? -5.715  95.138  -0.066  1.00 22.09  ? 118  VAL D O   1 
ATOM   4150 C  CB  . VAL D 1 118 ? -7.740  94.362  2.056   1.00 27.67  ? 118  VAL D CB  1 
ATOM   4151 C  CG1 . VAL D 1 118 ? -7.625  95.644  2.844   1.00 27.71  ? 118  VAL D CG1 1 
ATOM   4152 C  CG2 . VAL D 1 118 ? -8.852  93.468  2.604   1.00 21.94  ? 118  VAL D CG2 1 
ATOM   4153 N  N   . VAL D 1 119 ? -7.182  96.847  -0.175  1.00 23.11  ? 119  VAL D N   1 
ATOM   4154 C  CA  . VAL D 1 119 ? -6.171  97.873  -0.376  1.00 23.19  ? 119  VAL D CA  1 
ATOM   4155 C  C   . VAL D 1 119 ? -6.054  98.701  0.912   1.00 26.83  ? 119  VAL D C   1 
ATOM   4156 O  O   . VAL D 1 119 ? -7.058  99.067  1.516   1.00 22.59  ? 119  VAL D O   1 
ATOM   4157 C  CB  . VAL D 1 119 ? -6.429  98.780  -1.614  1.00 22.08  ? 119  VAL D CB  1 
ATOM   4158 C  CG1 . VAL D 1 119 ? -7.779  99.501  -1.526  1.00 21.28  ? 119  VAL D CG1 1 
ATOM   4159 C  CG2 . VAL D 1 119 ? -5.316  99.769  -1.746  1.00 21.98  ? 119  VAL D CG2 1 
ATOM   4160 N  N   . HIS D 1 120 ? -4.818  98.963  1.321   1.00 24.94  ? 120  HIS D N   1 
ATOM   4161 C  CA  . HIS D 1 120 ? -4.525  99.510  2.633   1.00 28.55  ? 120  HIS D CA  1 
ATOM   4162 C  C   . HIS D 1 120 ? -4.092  100.964 2.585   1.00 29.29  ? 120  HIS D C   1 
ATOM   4163 O  O   . HIS D 1 120 ? -3.766  101.512 1.526   1.00 26.84  ? 120  HIS D O   1 
ATOM   4164 C  CB  . HIS D 1 120 ? -3.427  98.675  3.315   1.00 30.45  ? 120  HIS D CB  1 
ATOM   4165 C  CG  . HIS D 1 120 ? -3.906  97.350  3.823   1.00 30.03  ? 120  HIS D CG  1 
ATOM   4166 N  ND1 . HIS D 1 120 ? -4.335  97.162  5.118   1.00 30.42  ? 120  HIS D ND1 1 
ATOM   4167 C  CD2 . HIS D 1 120 ? -4.048  96.152  3.204   1.00 30.77  ? 120  HIS D CD2 1 
ATOM   4168 C  CE1 . HIS D 1 120 ? -4.719  95.907  5.279   1.00 28.27  ? 120  HIS D CE1 1 
ATOM   4169 N  NE2 . HIS D 1 120 ? -4.546  95.269  4.136   1.00 31.15  ? 120  HIS D NE2 1 
ATOM   4170 N  N   . GLU D 1 121 ? -4.054  101.551 3.773   1.00 30.68  ? 121  GLU D N   1 
ATOM   4171 C  CA  . GLU D 1 121 ? -3.815  102.970 3.976   1.00 29.40  ? 121  GLU D CA  1 
ATOM   4172 C  C   . GLU D 1 121 ? -2.399  103.405 3.610   1.00 30.04  ? 121  GLU D C   1 
ATOM   4173 O  O   . GLU D 1 121 ? -2.192  104.508 3.092   1.00 29.02  ? 121  GLU D O   1 
ATOM   4174 C  CB  . GLU D 1 121 ? -4.106  103.298 5.441   1.00 34.47  ? 121  GLU D CB  1 
ATOM   4175 C  CG  . GLU D 1 121 ? -3.839  104.738 5.852   1.00 39.19  ? 121  GLU D CG  1 
ATOM   4176 C  CD  . GLU D 1 121 ? -3.822  104.932 7.366   1.00 39.71  ? 121  GLU D CD  1 
ATOM   4177 O  OE1 . GLU D 1 121 ? -3.902  103.937 8.128   1.00 40.97  ? 121  GLU D OE1 1 
ATOM   4178 O  OE2 . GLU D 1 121 ? -3.695  106.090 7.796   1.00 47.47  ? 121  GLU D OE2 1 
ATOM   4179 N  N   . LYS D 1 122 ? -1.416  102.555 3.886   1.00 29.35  ? 122  LYS D N   1 
ATOM   4180 C  CA  . LYS D 1 122 ? -0.037  102.925 3.595   1.00 33.00  ? 122  LYS D CA  1 
ATOM   4181 C  C   . LYS D 1 122 ? 0.757   101.814 2.948   1.00 30.09  ? 122  LYS D C   1 
ATOM   4182 O  O   . LYS D 1 122 ? 0.231   100.744 2.652   1.00 33.54  ? 122  LYS D O   1 
ATOM   4183 C  CB  . LYS D 1 122 ? 0.703   103.451 4.834   1.00 34.38  ? 122  LYS D CB  1 
ATOM   4184 C  CG  . LYS D 1 122 ? 0.104   103.076 6.169   1.00 35.28  ? 122  LYS D CG  1 
ATOM   4185 C  CD  . LYS D 1 122 ? 1.021   103.518 7.301   1.00 42.19  ? 122  LYS D CD  1 
ATOM   4186 C  CE  . LYS D 1 122 ? 0.325   103.466 8.649   1.00 44.51  ? 122  LYS D CE  1 
ATOM   4187 N  NZ  . LYS D 1 122 ? 1.324   103.242 9.741   1.00 53.31  ? 122  LYS D NZ  1 
ATOM   4188 N  N   . ALA D 1 123 ? 2.028   102.098 2.721   1.00 26.09  ? 123  ALA D N   1 
ATOM   4189 C  CA  . ALA D 1 123 ? 2.959   101.127 2.185   1.00 30.96  ? 123  ALA D CA  1 
ATOM   4190 C  C   . ALA D 1 123 ? 3.131   99.862  3.049   1.00 33.27  ? 123  ALA D C   1 
ATOM   4191 O  O   . ALA D 1 123 ? 3.144   99.917  4.281   1.00 33.34  ? 123  ALA D O   1 
ATOM   4192 C  CB  . ALA D 1 123 ? 4.300   101.789 1.964   1.00 27.60  ? 123  ALA D CB  1 
ATOM   4193 N  N   . ASP D 1 124 ? 3.250   98.732  2.361   1.00 30.77  ? 124  ASP D N   1 
ATOM   4194 C  CA  . ASP D 1 124 ? 3.704   97.477  2.923   1.00 32.27  ? 124  ASP D CA  1 
ATOM   4195 C  C   . ASP D 1 124 ? 5.222   97.511  3.057   1.00 35.36  ? 124  ASP D C   1 
ATOM   4196 O  O   . ASP D 1 124 ? 5.917   97.718  2.066   1.00 35.28  ? 124  ASP D O   1 
ATOM   4197 C  CB  . ASP D 1 124 ? 3.320   96.350  1.977   1.00 29.73  ? 124  ASP D CB  1 
ATOM   4198 C  CG  . ASP D 1 124 ? 3.469   94.981  2.603   1.00 36.81  ? 124  ASP D CG  1 
ATOM   4199 O  OD1 . ASP D 1 124 ? 4.243   94.836  3.588   1.00 36.57  ? 124  ASP D OD1 1 
ATOM   4200 O  OD2 . ASP D 1 124 ? 2.798   94.052  2.099   1.00 37.65  ? 124  ASP D OD2 1 
ATOM   4201 N  N   . ASP D 1 125 ? 5.746   97.324  4.270   1.00 34.35  ? 125  ASP D N   1 
ATOM   4202 C  CA  . ASP D 1 125 ? 7.202   97.298  4.454   1.00 34.44  ? 125  ASP D CA  1 
ATOM   4203 C  C   . ASP D 1 125 ? 7.748   95.908  4.172   1.00 35.92  ? 125  ASP D C   1 
ATOM   4204 O  O   . ASP D 1 125 ? 8.926   95.639  4.388   1.00 41.92  ? 125  ASP D O   1 
ATOM   4205 C  CB  . ASP D 1 125 ? 7.649   97.776  5.852   1.00 36.35  ? 125  ASP D CB  1 
ATOM   4206 C  CG  . ASP D 1 125 ? 7.270   96.795  6.989   1.00 38.91  ? 125  ASP D CG  1 
ATOM   4207 O  OD1 . ASP D 1 125 ? 6.893   95.617  6.744   1.00 35.24  ? 125  ASP D OD1 1 
ATOM   4208 O  OD2 . ASP D 1 125 ? 7.350   97.229  8.153   1.00 40.89  ? 125  ASP D OD2 1 
ATOM   4209 N  N   . LEU D 1 126 ? 6.880   95.023  3.706   1.00 34.22  ? 126  LEU D N   1 
ATOM   4210 C  CA  . LEU D 1 126 ? 7.319   93.717  3.215   1.00 41.32  ? 126  LEU D CA  1 
ATOM   4211 C  C   . LEU D 1 126 ? 7.816   92.760  4.309   1.00 43.59  ? 126  LEU D C   1 
ATOM   4212 O  O   . LEU D 1 126 ? 8.368   91.712  4.000   1.00 44.65  ? 126  LEU D O   1 
ATOM   4213 C  CB  . LEU D 1 126 ? 8.404   93.896  2.145   1.00 37.47  ? 126  LEU D CB  1 
ATOM   4214 C  CG  . LEU D 1 126 ? 8.020   94.825  0.987   1.00 37.51  ? 126  LEU D CG  1 
ATOM   4215 C  CD1 . LEU D 1 126 ? 9.170   95.004  0.011   1.00 37.10  ? 126  LEU D CD1 1 
ATOM   4216 C  CD2 . LEU D 1 126 ? 6.771   94.312  0.281   1.00 35.00  ? 126  LEU D CD2 1 
ATOM   4217 N  N   . GLY D 1 127 ? 7.625   93.118  5.576   1.00 40.03  ? 127  GLY D N   1 
ATOM   4218 C  CA  . GLY D 1 127 ? 7.991   92.229  6.661   1.00 40.25  ? 127  GLY D CA  1 
ATOM   4219 C  C   . GLY D 1 127 ? 9.439   92.417  7.058   1.00 42.68  ? 127  GLY D C   1 
ATOM   4220 O  O   . GLY D 1 127 ? 10.092  91.504  7.579   1.00 40.11  ? 127  GLY D O   1 
ATOM   4221 N  N   . LYS D 1 128 ? 9.938   93.621  6.824   1.00 39.01  ? 128  LYS D N   1 
ATOM   4222 C  CA  . LYS D 1 128 ? 11.308  93.962  7.165   1.00 35.78  ? 128  LYS D CA  1 
ATOM   4223 C  C   . LYS D 1 128 ? 11.333  95.127  8.150   1.00 38.92  ? 128  LYS D C   1 
ATOM   4224 O  O   . LYS D 1 128 ? 12.394  95.716  8.412   1.00 37.17  ? 128  LYS D O   1 
ATOM   4225 C  CB  . LYS D 1 128 ? 12.069  94.314  5.894   1.00 40.86  ? 128  LYS D CB  1 
ATOM   4226 C  CG  . LYS D 1 128 ? 11.886  93.261  4.814   1.00 43.44  ? 128  LYS D CG  1 
ATOM   4227 C  CD  . LYS D 1 128 ? 12.761  93.528  3.604   1.00 47.80  ? 128  LYS D CD  1 
ATOM   4228 C  CE  . LYS D 1 128 ? 13.175  92.211  2.955   1.00 57.13  ? 128  LYS D CE  1 
ATOM   4229 N  NZ  . LYS D 1 128 ? 12.023  91.262  2.840   1.00 50.76  ? 128  LYS D NZ  1 
ATOM   4230 N  N   . GLY D 1 129 ? 10.162  95.459  8.698   1.00 32.41  ? 129  GLY D N   1 
ATOM   4231 C  CA  . GLY D 1 129 ? 10.071  96.523  9.681   1.00 36.77  ? 129  GLY D CA  1 
ATOM   4232 C  C   . GLY D 1 129 ? 10.751  96.210  11.011  1.00 42.23  ? 129  GLY D C   1 
ATOM   4233 O  O   . GLY D 1 129 ? 11.013  97.115  11.810  1.00 46.56  ? 129  GLY D O   1 
ATOM   4234 N  N   . GLY D 1 130 ? 11.034  94.934  11.259  1.00 35.74  ? 130  GLY D N   1 
ATOM   4235 C  CA  . GLY D 1 130 ? 11.722  94.542  12.474  1.00 38.79  ? 130  GLY D CA  1 
ATOM   4236 C  C   . GLY D 1 130 ? 10.797  94.230  13.642  1.00 43.90  ? 130  GLY D C   1 
ATOM   4237 O  O   . GLY D 1 130 ? 11.127  93.395  14.494  1.00 43.71  ? 130  GLY D O   1 
ATOM   4238 N  N   . ASN D 1 131 ? 9.644   94.898  13.694  1.00 40.34  ? 131  ASN D N   1 
ATOM   4239 C  CA  . ASN D 1 131 ? 8.717   94.701  14.806  1.00 38.80  ? 131  ASN D CA  1 
ATOM   4240 C  C   . ASN D 1 131 ? 7.669   93.646  14.509  1.00 37.61  ? 131  ASN D C   1 
ATOM   4241 O  O   . ASN D 1 131 ? 7.589   93.138  13.399  1.00 42.18  ? 131  ASN D O   1 
ATOM   4242 C  CB  . ASN D 1 131 ? 8.075   96.027  15.253  1.00 41.68  ? 131  ASN D CB  1 
ATOM   4243 C  CG  . ASN D 1 131 ? 6.895   96.472  14.365  1.00 47.43  ? 131  ASN D CG  1 
ATOM   4244 O  OD1 . ASN D 1 131 ? 6.519   95.806  13.389  1.00 45.41  ? 131  ASN D OD1 1 
ATOM   4245 N  ND2 . ASN D 1 131 ? 6.302   97.613  14.719  1.00 46.29  ? 131  ASN D ND2 1 
ATOM   4246 N  N   . GLU D 1 132 ? 6.863   93.322  15.506  1.00 37.58  ? 132  GLU D N   1 
ATOM   4247 C  CA  . GLU D 1 132 ? 5.887   92.256  15.378  1.00 41.97  ? 132  GLU D CA  1 
ATOM   4248 C  C   . GLU D 1 132 ? 4.864   92.559  14.303  1.00 41.78  ? 132  GLU D C   1 
ATOM   4249 O  O   . GLU D 1 132 ? 4.452   91.677  13.556  1.00 40.99  ? 132  GLU D O   1 
ATOM   4250 C  CB  . GLU D 1 132 ? 5.161   92.062  16.702  1.00 37.10  ? 132  GLU D CB  1 
ATOM   4251 C  CG  . GLU D 1 132 ? 4.019   91.088  16.634  1.00 33.21  ? 132  GLU D CG  1 
ATOM   4252 C  CD  . GLU D 1 132 ? 3.290   90.983  17.970  1.00 46.14  ? 132  GLU D CD  1 
ATOM   4253 O  OE1 . GLU D 1 132 ? 3.492   91.885  18.832  1.00 42.05  ? 132  GLU D OE1 1 
ATOM   4254 O  OE2 . GLU D 1 132 ? 2.525   90.002  18.158  1.00 41.94  ? 132  GLU D OE2 1 
ATOM   4255 N  N   . GLU D 1 133 ? 4.431   93.813  14.258  1.00 43.47  ? 133  GLU D N   1 
ATOM   4256 C  CA  . GLU D 1 133 ? 3.355   94.212  13.361  1.00 44.87  ? 133  GLU D CA  1 
ATOM   4257 C  C   . GLU D 1 133 ? 3.791   93.962  11.918  1.00 41.96  ? 133  GLU D C   1 
ATOM   4258 O  O   . GLU D 1 133 ? 3.064   93.366  11.128  1.00 39.44  ? 133  GLU D O   1 
ATOM   4259 C  CB  . GLU D 1 133 ? 2.975   95.684  13.612  1.00 47.80  ? 133  GLU D CB  1 
ATOM   4260 C  CG  . GLU D 1 133 ? 1.736   96.198  12.867  1.00 44.27  ? 133  GLU D CG  1 
ATOM   4261 C  CD  . GLU D 1 133 ? 0.478   95.401  13.169  1.00 49.62  ? 133  GLU D CD  1 
ATOM   4262 O  OE1 . GLU D 1 133 ? 0.600   94.243  13.623  1.00 53.24  ? 133  GLU D OE1 1 
ATOM   4263 O  OE2 . GLU D 1 133 ? -0.637  95.930  12.940  1.00 50.62  ? 133  GLU D OE2 1 
ATOM   4264 N  N   . SER D 1 134 ? 5.002   94.413  11.604  1.00 41.29  ? 134  SER D N   1 
ATOM   4265 C  CA  . SER D 1 134 ? 5.644   94.166  10.321  1.00 38.98  ? 134  SER D CA  1 
ATOM   4266 C  C   . SER D 1 134 ? 5.566   92.696  9.908   1.00 43.80  ? 134  SER D C   1 
ATOM   4267 O  O   . SER D 1 134 ? 5.563   92.375  8.718   1.00 44.68  ? 134  SER D O   1 
ATOM   4268 C  CB  . SER D 1 134 ? 7.106   94.595  10.407  1.00 36.94  ? 134  SER D CB  1 
ATOM   4269 O  OG  . SER D 1 134 ? 7.837   94.121  9.304   1.00 33.29  ? 134  SER D OG  1 
ATOM   4270 N  N   . THR D 1 135 ? 5.488   91.827  10.915  1.00 40.89  ? 135  THR D N   1 
ATOM   4271 C  CA  . THR D 1 135 ? 5.561   90.378  10.790  1.00 36.22  ? 135  THR D CA  1 
ATOM   4272 C  C   . THR D 1 135 ? 4.188   89.780  10.491  1.00 42.13  ? 135  THR D C   1 
ATOM   4273 O  O   . THR D 1 135 ? 4.061   88.609  10.110  1.00 42.34  ? 135  THR D O   1 
ATOM   4274 C  CB  . THR D 1 135 ? 6.046   89.798  12.149  1.00 43.20  ? 135  THR D CB  1 
ATOM   4275 O  OG1 . THR D 1 135 ? 7.382   89.302  12.033  1.00 44.88  ? 135  THR D OG1 1 
ATOM   4276 C  CG2 . THR D 1 135 ? 5.107   88.722  12.682  1.00 33.31  ? 135  THR D CG2 1 
ATOM   4277 N  N   . LYS D 1 136 ? 3.154   90.586  10.691  1.00 39.67  ? 136  LYS D N   1 
ATOM   4278 C  CA  . LYS D 1 136 ? 1.790   90.125  10.494  1.00 39.23  ? 136  LYS D CA  1 
ATOM   4279 C  C   . LYS D 1 136 ? 1.120   90.868  9.345   1.00 40.55  ? 136  LYS D C   1 
ATOM   4280 O  O   . LYS D 1 136 ? 0.267   90.322  8.622   1.00 37.11  ? 136  LYS D O   1 
ATOM   4281 C  CB  . LYS D 1 136 ? 0.987   90.361  11.765  1.00 39.78  ? 136  LYS D CB  1 
ATOM   4282 C  CG  . LYS D 1 136 ? 1.562   89.666  12.972  1.00 47.20  ? 136  LYS D CG  1 
ATOM   4283 C  CD  . LYS D 1 136 ? 0.640   89.741  14.188  1.00 47.29  ? 136  LYS D CD  1 
ATOM   4284 C  CE  . LYS D 1 136 ? 1.110   88.743  15.254  1.00 50.02  ? 136  LYS D CE  1 
ATOM   4285 N  NZ  . LYS D 1 136 ? 1.208   87.343  14.686  1.00 45.97  ? 136  LYS D NZ  1 
ATOM   4286 N  N   . THR D 1 137 ? 1.547   92.111  9.162   1.00 36.96  ? 137  THR D N   1 
ATOM   4287 C  CA  . THR D 1 137 ? 0.706   93.098  8.522   1.00 35.52  ? 137  THR D CA  1 
ATOM   4288 C  C   . THR D 1 137 ? 1.436   93.973  7.497   1.00 37.31  ? 137  THR D C   1 
ATOM   4289 O  O   . THR D 1 137 ? 0.806   94.569  6.623   1.00 37.55  ? 137  THR D O   1 
ATOM   4290 C  CB  . THR D 1 137 ? 0.015   93.942  9.633   1.00 37.73  ? 137  THR D CB  1 
ATOM   4291 O  OG1 . THR D 1 137 ? -1.411  93.787  9.555   1.00 36.89  ? 137  THR D OG1 1 
ATOM   4292 C  CG2 . THR D 1 137 ? 0.427   95.400  9.587   1.00 30.47  ? 137  THR D CG2 1 
ATOM   4293 N  N   . GLY D 1 138 ? 2.762   94.022  7.593   1.00 34.64  ? 138  GLY D N   1 
ATOM   4294 C  CA  . GLY D 1 138 ? 3.570   94.898  6.767   1.00 34.48  ? 138  GLY D CA  1 
ATOM   4295 C  C   . GLY D 1 138 ? 3.502   96.345  7.232   1.00 38.64  ? 138  GLY D C   1 
ATOM   4296 O  O   . GLY D 1 138 ? 4.050   97.259  6.598   1.00 36.84  ? 138  GLY D O   1 
ATOM   4297 N  N   . ASN D 1 139 ? 2.818   96.560  8.349   1.00 38.48  ? 139  ASN D N   1 
ATOM   4298 C  CA  . ASN D 1 139 ? 2.565   97.907  8.837   1.00 38.66  ? 139  ASN D CA  1 
ATOM   4299 C  C   . ASN D 1 139 ? 1.877   98.764  7.767   1.00 39.04  ? 139  ASN D C   1 
ATOM   4300 O  O   . ASN D 1 139 ? 2.224   99.930  7.594   1.00 37.97  ? 139  ASN D O   1 
ATOM   4301 C  CB  . ASN D 1 139 ? 3.866   98.567  9.301   1.00 36.17  ? 139  ASN D CB  1 
ATOM   4302 C  CG  . ASN D 1 139 ? 4.476   97.874  10.526  1.00 43.72  ? 139  ASN D CG  1 
ATOM   4303 O  OD1 . ASN D 1 139 ? 5.605   97.362  10.475  1.00 41.06  ? 139  ASN D OD1 1 
ATOM   4304 N  ND2 . ASN D 1 139 ? 3.732   97.863  11.635  1.00 42.60  ? 139  ASN D ND2 1 
ATOM   4305 N  N   . ALA D 1 140 ? 0.909   98.179  7.058   1.00 31.93  ? 140  ALA D N   1 
ATOM   4306 C  CA  . ALA D 1 140 ? 0.244   98.864  5.949   1.00 36.62  ? 140  ALA D CA  1 
ATOM   4307 C  C   . ALA D 1 140 ? -0.948  99.691  6.424   1.00 34.59  ? 140  ALA D C   1 
ATOM   4308 O  O   . ALA D 1 140 ? -1.574  100.408 5.646   1.00 33.68  ? 140  ALA D O   1 
ATOM   4309 C  CB  . ALA D 1 140 ? -0.185  97.858  4.852   1.00 29.91  ? 140  ALA D CB  1 
ATOM   4310 N  N   . GLY D 1 141 ? -1.261  99.567  7.706   1.00 37.40  ? 141  GLY D N   1 
ATOM   4311 C  CA  . GLY D 1 141 ? -2.275  100.390 8.327   1.00 33.11  ? 141  GLY D CA  1 
ATOM   4312 C  C   . GLY D 1 141 ? -3.668  99.945  7.962   1.00 34.16  ? 141  GLY D C   1 
ATOM   4313 O  O   . GLY D 1 141 ? -3.891  98.772  7.630   1.00 29.05  ? 141  GLY D O   1 
ATOM   4314 N  N   . SER D 1 142 ? -4.598  100.900 7.993   1.00 31.32  ? 142  SER D N   1 
ATOM   4315 C  CA  . SER D 1 142 ? -6.016  100.593 7.903   1.00 28.19  ? 142  SER D CA  1 
ATOM   4316 C  C   . SER D 1 142 ? -6.470  100.082 6.542   1.00 29.90  ? 142  SER D C   1 
ATOM   4317 O  O   . SER D 1 142 ? -5.713  100.067 5.571   1.00 31.36  ? 142  SER D O   1 
ATOM   4318 C  CB  . SER D 1 142 ? -6.868  101.789 8.345   1.00 31.20  ? 142  SER D CB  1 
ATOM   4319 O  OG  . SER D 1 142 ? -6.911  102.787 7.340   1.00 41.16  ? 142  SER D OG  1 
ATOM   4320 N  N   . ARG D 1 143 ? -7.727  99.657  6.504   1.00 28.56  ? 143  ARG D N   1 
ATOM   4321 C  CA  . ARG D 1 143 ? -8.332  99.039  5.341   1.00 24.21  ? 143  ARG D CA  1 
ATOM   4322 C  C   . ARG D 1 143 ? -9.250  100.036 4.651   1.00 27.64  ? 143  ARG D C   1 
ATOM   4323 O  O   . ARG D 1 143 ? -10.353 100.327 5.116   1.00 25.48  ? 143  ARG D O   1 
ATOM   4324 C  CB  . ARG D 1 143 ? -9.084  97.773  5.766   1.00 24.39  ? 143  ARG D CB  1 
ATOM   4325 C  CG  . ARG D 1 143 ? -8.198  96.847  6.577   1.00 24.14  ? 143  ARG D CG  1 
ATOM   4326 C  CD  . ARG D 1 143 ? -8.879  95.607  7.127   1.00 22.98  ? 143  ARG D CD  1 
ATOM   4327 N  NE  . ARG D 1 143 ? -7.880  94.875  7.893   1.00 29.23  ? 143  ARG D NE  1 
ATOM   4328 C  CZ  . ARG D 1 143 ? -7.977  93.614  8.292   1.00 30.66  ? 143  ARG D CZ  1 
ATOM   4329 N  NH1 . ARG D 1 143 ? -9.053  92.889  7.986   1.00 27.10  ? 143  ARG D NH1 1 
ATOM   4330 N  NH2 . ARG D 1 143 ? -6.977  93.087  8.993   1.00 23.46  ? 143  ARG D NH2 1 
ATOM   4331 N  N   . LEU D 1 144 ? -8.761  100.567 3.539   1.00 28.34  ? 144  LEU D N   1 
ATOM   4332 C  CA  . LEU D 1 144 ? -9.453  101.591 2.771   1.00 30.56  ? 144  LEU D CA  1 
ATOM   4333 C  C   . LEU D 1 144 ? -10.706 101.043 2.065   1.00 28.69  ? 144  LEU D C   1 
ATOM   4334 O  O   . LEU D 1 144 ? -11.790 101.615 2.162   1.00 29.28  ? 144  LEU D O   1 
ATOM   4335 C  CB  . LEU D 1 144 ? -8.471  102.177 1.742   1.00 30.89  ? 144  LEU D CB  1 
ATOM   4336 C  CG  . LEU D 1 144 ? -7.704  103.451 2.089   1.00 31.16  ? 144  LEU D CG  1 
ATOM   4337 C  CD1 . LEU D 1 144 ? -7.663  103.696 3.586   1.00 30.15  ? 144  LEU D CD1 1 
ATOM   4338 C  CD2 . LEU D 1 144 ? -6.312  103.397 1.512   1.00 28.14  ? 144  LEU D CD2 1 
ATOM   4339 N  N   . ALA D 1 145 ? -10.535 99.925  1.366   1.00 28.54  ? 145  ALA D N   1 
ATOM   4340 C  CA  . ALA D 1 145 ? -11.579 99.314  0.549   1.00 29.00  ? 145  ALA D CA  1 
ATOM   4341 C  C   . ALA D 1 145 ? -11.298 97.828  0.366   1.00 27.97  ? 145  ALA D C   1 
ATOM   4342 O  O   . ALA D 1 145 ? -10.142 97.392  0.296   1.00 25.06  ? 145  ALA D O   1 
ATOM   4343 C  CB  . ALA D 1 145 ? -11.657 99.994  -0.836  1.00 26.54  ? 145  ALA D CB  1 
ATOM   4344 N  N   . CYS D 1 146 ? -12.360 97.051  0.245   1.00 25.05  ? 146  CYS D N   1 
ATOM   4345 C  CA  . CYS D 1 146 ? -12.191 95.625  0.113   1.00 27.58  ? 146  CYS D CA  1 
ATOM   4346 C  C   . CYS D 1 146 ? -13.379 95.015  -0.625  1.00 30.75  ? 146  CYS D C   1 
ATOM   4347 O  O   . CYS D 1 146 ? -14.461 95.615  -0.719  1.00 25.86  ? 146  CYS D O   1 
ATOM   4348 C  CB  . CYS D 1 146 ? -12.064 95.001  1.507   1.00 25.19  ? 146  CYS D CB  1 
ATOM   4349 S  SG  . CYS D 1 146 ? -13.571 95.175  2.490   1.00 28.14  ? 146  CYS D SG  1 
ATOM   4350 N  N   . GLY D 1 147 ? -13.175 93.806  -1.131  1.00 29.58  ? 147  GLY D N   1 
ATOM   4351 C  CA  . GLY D 1 147 ? -14.273 93.041  -1.683  1.00 31.38  ? 147  GLY D CA  1 
ATOM   4352 C  C   . GLY D 1 147 ? -14.004 91.554  -1.675  1.00 33.00  ? 147  GLY D C   1 
ATOM   4353 O  O   . GLY D 1 147 ? -12.848 91.116  -1.640  1.00 27.29  ? 147  GLY D O   1 
ATOM   4354 N  N   . VAL D 1 148 ? -15.094 90.791  -1.707  1.00 34.29  ? 148  VAL D N   1 
ATOM   4355 C  CA  . VAL D 1 148 ? -15.051 89.340  -1.804  1.00 30.35  ? 148  VAL D CA  1 
ATOM   4356 C  C   . VAL D 1 148 ? -14.672 88.942  -3.223  1.00 35.01  ? 148  VAL D C   1 
ATOM   4357 O  O   . VAL D 1 148 ? -15.280 89.392  -4.183  1.00 39.32  ? 148  VAL D O   1 
ATOM   4358 C  CB  . VAL D 1 148 ? -16.430 88.727  -1.475  1.00 37.91  ? 148  VAL D CB  1 
ATOM   4359 C  CG1 . VAL D 1 148 ? -16.414 87.231  -1.717  1.00 41.09  ? 148  VAL D CG1 1 
ATOM   4360 C  CG2 . VAL D 1 148 ? -16.861 89.068  -0.025  1.00 30.36  ? 148  VAL D CG2 1 
ATOM   4361 N  N   . ILE D 1 149 ? -13.663 88.097  -3.347  1.00 35.19  ? 149  ILE D N   1 
ATOM   4362 C  CA  . ILE D 1 149 ? -13.183 87.650  -4.638  1.00 35.71  ? 149  ILE D CA  1 
ATOM   4363 C  C   . ILE D 1 149 ? -14.088 86.585  -5.251  1.00 40.98  ? 149  ILE D C   1 
ATOM   4364 O  O   . ILE D 1 149 ? -14.137 85.448  -4.788  1.00 41.96  ? 149  ILE D O   1 
ATOM   4365 C  CB  . ILE D 1 149 ? -11.785 87.106  -4.510  1.00 32.12  ? 149  ILE D CB  1 
ATOM   4366 C  CG1 . ILE D 1 149 ? -10.885 88.195  -3.925  1.00 32.28  ? 149  ILE D CG1 1 
ATOM   4367 C  CG2 . ILE D 1 149 ? -11.291 86.653  -5.865  1.00 39.45  ? 149  ILE D CG2 1 
ATOM   4368 C  CD1 . ILE D 1 149 ? -9.509  87.726  -3.591  1.00 28.11  ? 149  ILE D CD1 1 
ATOM   4369 N  N   . GLY D 1 150 ? -14.812 86.962  -6.296  1.00 40.98  ? 150  GLY D N   1 
ATOM   4370 C  CA  . GLY D 1 150 ? -15.847 86.110  -6.852  1.00 43.56  ? 150  GLY D CA  1 
ATOM   4371 C  C   . GLY D 1 150 ? -15.437 85.416  -8.138  1.00 49.29  ? 150  GLY D C   1 
ATOM   4372 O  O   . GLY D 1 150 ? -14.466 85.812  -8.808  1.00 46.79  ? 150  GLY D O   1 
ATOM   4373 N  N   . ILE D 1 151 ? -16.184 84.373  -8.485  1.00 47.84  ? 151  ILE D N   1 
ATOM   4374 C  CA  . ILE D 1 151 ? -15.969 83.657  -9.733  1.00 49.95  ? 151  ILE D CA  1 
ATOM   4375 C  C   . ILE D 1 151 ? -16.600 84.421  -10.895 1.00 53.18  ? 151  ILE D C   1 
ATOM   4376 O  O   . ILE D 1 151 ? -17.762 84.846  -10.835 1.00 49.68  ? 151  ILE D O   1 
ATOM   4377 C  CB  . ILE D 1 151 ? -16.490 82.212  -9.655  1.00 55.84  ? 151  ILE D CB  1 
ATOM   4378 C  CG1 . ILE D 1 151 ? -15.410 81.308  -9.045  1.00 54.19  ? 151  ILE D CG1 1 
ATOM   4379 C  CG2 . ILE D 1 151 ? -16.890 81.707  -11.031 1.00 54.21  ? 151  ILE D CG2 1 
ATOM   4380 C  CD1 . ILE D 1 151 ? -15.923 80.382  -7.942  1.00 53.24  ? 151  ILE D CD1 1 
ATOM   4381 N  N   . ALA D 1 152 ? -15.809 84.618  -11.944 1.00 49.70  ? 152  ALA D N   1 
ATOM   4382 C  CA  . ALA D 1 152 ? -16.238 85.452  -13.052 1.00 57.49  ? 152  ALA D CA  1 
ATOM   4383 C  C   . ALA D 1 152 ? -16.328 84.644  -14.347 1.00 52.80  ? 152  ALA D C   1 
ATOM   4384 O  O   . ALA D 1 152 ? -15.440 83.845  -14.645 1.00 51.84  ? 152  ALA D O   1 
ATOM   4385 C  CB  . ALA D 1 152 ? -15.283 86.637  -13.208 1.00 48.69  ? 152  ALA D CB  1 
ATOM   4386 N  N   . ALA E 1 1   ? -77.597 65.885  4.549   1.00 58.13  ? 1    ALA E N   1 
ATOM   4387 C  CA  . ALA E 1 1   ? -77.710 66.748  5.731   1.00 66.78  ? 1    ALA E CA  1 
ATOM   4388 C  C   . ALA E 1 1   ? -76.359 66.906  6.437   1.00 63.31  ? 1    ALA E C   1 
ATOM   4389 O  O   . ALA E 1 1   ? -75.880 65.979  7.087   1.00 59.89  ? 1    ALA E O   1 
ATOM   4390 C  CB  . ALA E 1 1   ? -78.754 66.203  6.702   1.00 58.85  ? 1    ALA E CB  1 
ATOM   4391 N  N   . MET E 1 2   ? -75.756 68.084  6.302   1.00 64.16  ? 2    MET E N   1 
ATOM   4392 C  CA  . MET E 1 2   ? -74.450 68.373  6.889   1.00 55.76  ? 2    MET E CA  1 
ATOM   4393 C  C   . MET E 1 2   ? -74.581 68.749  8.358   1.00 52.03  ? 2    MET E C   1 
ATOM   4394 O  O   . MET E 1 2   ? -75.384 69.610  8.713   1.00 54.30  ? 2    MET E O   1 
ATOM   4395 C  CB  . MET E 1 2   ? -73.784 69.512  6.124   1.00 57.28  ? 2    MET E CB  1 
ATOM   4396 C  CG  . MET E 1 2   ? -73.405 69.159  4.687   1.00 64.05  ? 2    MET E CG  1 
ATOM   4397 S  SD  . MET E 1 2   ? -73.393 70.575  3.540   1.00 78.69  ? 2    MET E SD  1 
ATOM   4398 C  CE  . MET E 1 2   ? -75.136 70.694  3.126   1.00 66.75  ? 2    MET E CE  1 
ATOM   4399 N  N   . LYS E 1 3   ? -73.798 68.093  9.209   1.00 49.14  ? 3    LYS E N   1 
ATOM   4400 C  CA  . LYS E 1 3   ? -73.767 68.403  10.636  1.00 47.65  ? 3    LYS E CA  1 
ATOM   4401 C  C   . LYS E 1 3   ? -72.362 68.856  11.046  1.00 47.48  ? 3    LYS E C   1 
ATOM   4402 O  O   . LYS E 1 3   ? -71.366 68.407  10.481  1.00 47.70  ? 3    LYS E O   1 
ATOM   4403 C  CB  . LYS E 1 3   ? -74.188 67.184  11.474  1.00 54.25  ? 3    LYS E CB  1 
ATOM   4404 C  CG  . LYS E 1 3   ? -75.631 66.700  11.269  1.00 59.38  ? 3    LYS E CG  1 
ATOM   4405 C  CD  . LYS E 1 3   ? -75.937 65.441  12.113  1.00 66.38  ? 3    LYS E CD  1 
ATOM   4406 C  CE  . LYS E 1 3   ? -76.887 65.718  13.295  1.00 65.71  ? 3    LYS E CE  1 
ATOM   4407 N  NZ  . LYS E 1 3   ? -78.200 65.016  13.143  1.00 64.82  ? 3    LYS E NZ  1 
ATOM   4408 N  N   . ALA E 1 4   ? -72.280 69.748  12.029  1.00 49.23  ? 4    ALA E N   1 
ATOM   4409 C  CA  . ALA E 1 4   ? -70.992 70.190  12.551  1.00 42.03  ? 4    ALA E CA  1 
ATOM   4410 C  C   . ALA E 1 4   ? -71.100 70.473  14.031  1.00 46.18  ? 4    ALA E C   1 
ATOM   4411 O  O   . ALA E 1 4   ? -72.200 70.584  14.576  1.00 48.12  ? 4    ALA E O   1 
ATOM   4412 C  CB  . ALA E 1 4   ? -70.514 71.419  11.821  1.00 44.63  ? 4    ALA E CB  1 
ATOM   4413 N  N   . VAL E 1 5   ? -69.957 70.590  14.692  1.00 44.54  ? 5    VAL E N   1 
ATOM   4414 C  CA  . VAL E 1 5   ? -69.964 70.937  16.106  1.00 41.37  ? 5    VAL E CA  1 
ATOM   4415 C  C   . VAL E 1 5   ? -68.710 71.701  16.519  1.00 41.90  ? 5    VAL E C   1 
ATOM   4416 O  O   . VAL E 1 5   ? -67.631 71.538  15.942  1.00 38.53  ? 5    VAL E O   1 
ATOM   4417 C  CB  . VAL E 1 5   ? -70.154 69.699  17.007  1.00 39.59  ? 5    VAL E CB  1 
ATOM   4418 C  CG1 . VAL E 1 5   ? -68.996 68.718  16.832  1.00 40.41  ? 5    VAL E CG1 1 
ATOM   4419 C  CG2 . VAL E 1 5   ? -70.295 70.125  18.457  1.00 37.62  ? 5    VAL E CG2 1 
ATOM   4420 N  N   . CYS E 1 6   ? -68.859 72.543  17.526  1.00 38.66  ? 6    CYS E N   1 
ATOM   4421 C  CA  . CYS E 1 6   ? -67.745 73.333  17.989  1.00 41.94  ? 6    CYS E CA  1 
ATOM   4422 C  C   . CYS E 1 6   ? -67.746 73.399  19.505  1.00 45.59  ? 6    CYS E C   1 
ATOM   4423 O  O   . CYS E 1 6   ? -68.715 73.832  20.123  1.00 47.09  ? 6    CYS E O   1 
ATOM   4424 C  CB  . CYS E 1 6   ? -67.798 74.732  17.380  1.00 41.49  ? 6    CYS E CB  1 
ATOM   4425 S  SG  . CYS E 1 6   ? -66.517 75.821  17.997  1.00 49.63  ? 6    CYS E SG  1 
ATOM   4426 N  N   . VAL E 1 7   ? -66.660 72.929  20.103  1.00 51.16  ? 7    VAL E N   1 
ATOM   4427 C  CA  . VAL E 1 7   ? -66.503 73.010  21.545  1.00 51.13  ? 7    VAL E CA  1 
ATOM   4428 C  C   . VAL E 1 7   ? -65.691 74.252  21.803  1.00 50.79  ? 7    VAL E C   1 
ATOM   4429 O  O   . VAL E 1 7   ? -64.612 74.424  21.234  1.00 48.27  ? 7    VAL E O   1 
ATOM   4430 C  CB  . VAL E 1 7   ? -65.782 71.779  22.119  1.00 50.16  ? 7    VAL E CB  1 
ATOM   4431 C  CG1 . VAL E 1 7   ? -65.670 71.884  23.622  1.00 48.04  ? 7    VAL E CG1 1 
ATOM   4432 C  CG2 . VAL E 1 7   ? -66.516 70.499  21.715  1.00 50.95  ? 7    VAL E CG2 1 
ATOM   4433 N  N   . LEU E 1 8   ? -66.237 75.138  22.627  1.00 54.09  ? 8    LEU E N   1 
ATOM   4434 C  CA  . LEU E 1 8   ? -65.584 76.405  22.929  1.00 57.18  ? 8    LEU E CA  1 
ATOM   4435 C  C   . LEU E 1 8   ? -64.888 76.315  24.279  1.00 59.72  ? 8    LEU E C   1 
ATOM   4436 O  O   . LEU E 1 8   ? -65.515 76.021  25.300  1.00 59.66  ? 8    LEU E O   1 
ATOM   4437 C  CB  . LEU E 1 8   ? -66.600 77.556  22.915  1.00 57.98  ? 8    LEU E CB  1 
ATOM   4438 C  CG  . LEU E 1 8   ? -67.364 77.804  21.607  1.00 52.96  ? 8    LEU E CG  1 
ATOM   4439 C  CD1 . LEU E 1 8   ? -68.679 78.508  21.873  1.00 53.29  ? 8    LEU E CD1 1 
ATOM   4440 C  CD2 . LEU E 1 8   ? -66.519 78.589  20.614  1.00 48.71  ? 8    LEU E CD2 1 
ATOM   4441 N  N   . LYS E 1 9   ? -63.579 76.534  24.268  1.00 59.30  ? 9    LYS E N   1 
ATOM   4442 C  CA  . LYS E 1 9   ? -62.809 76.583  25.497  1.00 63.19  ? 9    LYS E CA  1 
ATOM   4443 C  C   . LYS E 1 9   ? -62.105 77.932  25.540  1.00 66.70  ? 9    LYS E C   1 
ATOM   4444 O  O   . LYS E 1 9   ? -61.981 78.605  24.516  1.00 63.90  ? 9    LYS E O   1 
ATOM   4445 C  CB  . LYS E 1 9   ? -61.792 75.439  25.546  1.00 64.66  ? 9    LYS E CB  1 
ATOM   4446 C  CG  . LYS E 1 9   ? -62.369 74.065  25.237  1.00 62.77  ? 9    LYS E CG  1 
ATOM   4447 C  CD  . LYS E 1 9   ? -63.492 73.674  26.206  1.00 67.97  ? 9    LYS E CD  1 
ATOM   4448 C  CE  . LYS E 1 9   ? -62.978 72.797  27.345  1.00 70.19  ? 9    LYS E CE  1 
ATOM   4449 N  NZ  . LYS E 1 9   ? -64.083 72.199  28.160  1.00 71.03  ? 9    LYS E NZ  1 
ATOM   4450 N  N   . GLY E 1 10  ? -61.659 78.339  26.720  1.00 68.16  ? 10   GLY E N   1 
ATOM   4451 C  CA  . GLY E 1 10  ? -60.969 79.605  26.851  1.00 65.08  ? 10   GLY E CA  1 
ATOM   4452 C  C   . GLY E 1 10  ? -60.256 79.659  28.176  1.00 79.63  ? 10   GLY E C   1 
ATOM   4453 O  O   . GLY E 1 10  ? -60.656 78.971  29.122  1.00 81.03  ? 10   GLY E O   1 
ATOM   4454 N  N   . ASP E 1 11  ? -59.202 80.469  28.245  1.00 81.07  ? 11   ASP E N   1 
ATOM   4455 C  CA  . ASP E 1 11  ? -58.431 80.614  29.476  1.00 80.73  ? 11   ASP E CA  1 
ATOM   4456 C  C   . ASP E 1 11  ? -59.356 80.833  30.668  1.00 78.57  ? 11   ASP E C   1 
ATOM   4457 O  O   . ASP E 1 11  ? -59.084 80.358  31.769  1.00 77.41  ? 11   ASP E O   1 
ATOM   4458 C  CB  . ASP E 1 11  ? -57.410 81.748  29.346  1.00 79.54  ? 11   ASP E CB  1 
ATOM   4459 C  CG  . ASP E 1 11  ? -56.309 81.421  28.346  1.00 82.78  ? 11   ASP E CG  1 
ATOM   4460 O  OD1 . ASP E 1 11  ? -56.103 80.217  28.068  1.00 81.97  ? 11   ASP E OD1 1 
ATOM   4461 O  OD2 . ASP E 1 11  ? -55.650 82.356  27.839  1.00 78.25  ? 11   ASP E OD2 1 
ATOM   4462 N  N   . GLY E 1 12  ? -60.463 81.528  30.429  1.00 77.00  ? 12   GLY E N   1 
ATOM   4463 C  CA  . GLY E 1 12  ? -61.462 81.753  31.456  1.00 78.55  ? 12   GLY E CA  1 
ATOM   4464 C  C   . GLY E 1 12  ? -62.221 80.488  31.810  1.00 78.52  ? 12   GLY E C   1 
ATOM   4465 O  O   . GLY E 1 12  ? -61.805 79.390  31.437  1.00 77.18  ? 12   GLY E O   1 
ATOM   4466 N  N   . PRO E 1 13  ? -63.334 80.639  32.549  1.00 77.85  ? 13   PRO E N   1 
ATOM   4467 C  CA  . PRO E 1 13  ? -64.254 79.561  32.920  1.00 76.15  ? 13   PRO E CA  1 
ATOM   4468 C  C   . PRO E 1 13  ? -65.336 79.415  31.860  1.00 73.89  ? 13   PRO E C   1 
ATOM   4469 O  O   . PRO E 1 13  ? -66.192 78.525  31.956  1.00 75.26  ? 13   PRO E O   1 
ATOM   4470 C  CB  . PRO E 1 13  ? -64.885 80.070  34.226  1.00 71.27  ? 13   PRO E CB  1 
ATOM   4471 C  CG  . PRO E 1 13  ? -64.198 81.379  34.537  1.00 74.53  ? 13   PRO E CG  1 
ATOM   4472 C  CD  . PRO E 1 13  ? -63.692 81.887  33.233  1.00 77.38  ? 13   PRO E CD  1 
ATOM   4473 N  N   . VAL E 1 14  ? -65.298 80.296  30.863  1.00 72.76  ? 14   VAL E N   1 
ATOM   4474 C  CA  . VAL E 1 14  ? -66.226 80.220  29.738  1.00 71.80  ? 14   VAL E CA  1 
ATOM   4475 C  C   . VAL E 1 14  ? -66.011 78.914  28.980  1.00 68.33  ? 14   VAL E C   1 
ATOM   4476 O  O   . VAL E 1 14  ? -64.875 78.479  28.787  1.00 68.20  ? 14   VAL E O   1 
ATOM   4477 C  CB  . VAL E 1 14  ? -66.066 81.420  28.771  1.00 70.26  ? 14   VAL E CB  1 
ATOM   4478 C  CG1 . VAL E 1 14  ? -67.040 81.308  27.591  1.00 64.92  ? 14   VAL E CG1 1 
ATOM   4479 C  CG2 . VAL E 1 14  ? -66.270 82.733  29.517  1.00 70.38  ? 14   VAL E CG2 1 
ATOM   4480 N  N   . GLN E 1 15  ? -67.110 78.289  28.569  1.00 68.03  ? 15   GLN E N   1 
ATOM   4481 C  CA  . GLN E 1 15  ? -67.062 77.033  27.835  1.00 67.18  ? 15   GLN E CA  1 
ATOM   4482 C  C   . GLN E 1 15  ? -68.457 76.678  27.339  1.00 69.34  ? 15   GLN E C   1 
ATOM   4483 O  O   . GLN E 1 15  ? -69.454 77.158  27.883  1.00 68.35  ? 15   GLN E O   1 
ATOM   4484 C  CB  . GLN E 1 15  ? -66.547 75.915  28.737  1.00 74.76  ? 15   GLN E CB  1 
ATOM   4485 C  CG  . GLN E 1 15  ? -67.557 75.468  29.783  1.00 76.04  ? 15   GLN E CG  1 
ATOM   4486 C  CD  . GLN E 1 15  ? -67.024 74.365  30.673  1.00 79.03  ? 15   GLN E CD  1 
ATOM   4487 O  OE1 . GLN E 1 15  ? -66.108 74.582  31.472  1.00 79.43  ? 15   GLN E OE1 1 
ATOM   4488 N  NE2 . GLN E 1 15  ? -67.597 73.172  30.542  1.00 79.89  ? 15   GLN E NE2 1 
ATOM   4489 N  N   . GLY E 1 16  ? -68.528 75.837  26.309  1.00 65.59  ? 16   GLY E N   1 
ATOM   4490 C  CA  . GLY E 1 16  ? -69.807 75.364  25.812  1.00 57.51  ? 16   GLY E CA  1 
ATOM   4491 C  C   . GLY E 1 16  ? -69.693 74.484  24.585  1.00 58.09  ? 16   GLY E C   1 
ATOM   4492 O  O   . GLY E 1 16  ? -68.591 74.150  24.141  1.00 58.06  ? 16   GLY E O   1 
ATOM   4493 N  N   . THR E 1 17  ? -70.842 74.109  24.033  1.00 53.69  ? 17   THR E N   1 
ATOM   4494 C  CA  . THR E 1 17  ? -70.880 73.273  22.848  1.00 51.34  ? 17   THR E CA  1 
ATOM   4495 C  C   . THR E 1 17  ? -71.971 73.745  21.895  1.00 51.42  ? 17   THR E C   1 
ATOM   4496 O  O   . THR E 1 17  ? -73.129 73.872  22.288  1.00 51.01  ? 17   THR E O   1 
ATOM   4497 C  CB  . THR E 1 17  ? -71.127 71.804  23.212  1.00 52.21  ? 17   THR E CB  1 
ATOM   4498 O  OG1 . THR E 1 17  ? -70.202 71.403  24.235  1.00 50.45  ? 17   THR E OG1 1 
ATOM   4499 C  CG2 . THR E 1 17  ? -70.955 70.917  21.974  1.00 48.19  ? 17   THR E CG2 1 
ATOM   4500 N  N   . ILE E 1 18  ? -71.592 74.010  20.647  1.00 48.17  ? 18   ILE E N   1 
ATOM   4501 C  CA  . ILE E 1 18  ? -72.538 74.471  19.637  1.00 48.17  ? 18   ILE E CA  1 
ATOM   4502 C  C   . ILE E 1 18  ? -72.671 73.449  18.512  1.00 48.37  ? 18   ILE E C   1 
ATOM   4503 O  O   . ILE E 1 18  ? -71.672 72.924  18.014  1.00 44.10  ? 18   ILE E O   1 
ATOM   4504 C  CB  . ILE E 1 18  ? -72.122 75.838  19.048  1.00 47.79  ? 18   ILE E CB  1 
ATOM   4505 C  CG1 . ILE E 1 18  ? -71.973 76.877  20.162  1.00 51.63  ? 18   ILE E CG1 1 
ATOM   4506 C  CG2 . ILE E 1 18  ? -73.118 76.304  17.994  1.00 47.56  ? 18   ILE E CG2 1 
ATOM   4507 C  CD1 . ILE E 1 18  ? -73.198 77.021  21.051  1.00 54.57  ? 18   ILE E CD1 1 
ATOM   4508 N  N   . HIS E 1 19  ? -73.915 73.175  18.123  1.00 50.01  ? 19   HIS E N   1 
ATOM   4509 C  CA  . HIS E 1 19  ? -74.203 72.214  17.065  1.00 48.16  ? 19   HIS E CA  1 
ATOM   4510 C  C   . HIS E 1 19  ? -74.738 72.900  15.830  1.00 45.88  ? 19   HIS E C   1 
ATOM   4511 O  O   . HIS E 1 19  ? -75.550 73.808  15.924  1.00 50.73  ? 19   HIS E O   1 
ATOM   4512 C  CB  . HIS E 1 19  ? -75.188 71.161  17.553  1.00 46.58  ? 19   HIS E CB  1 
ATOM   4513 C  CG  . HIS E 1 19  ? -74.678 70.376  18.714  1.00 44.15  ? 19   HIS E CG  1 
ATOM   4514 N  ND1 . HIS E 1 19  ? -73.928 69.230  18.565  1.00 42.95  ? 19   HIS E ND1 1 
ATOM   4515 C  CD2 . HIS E 1 19  ? -74.788 70.585  20.047  1.00 48.63  ? 19   HIS E CD2 1 
ATOM   4516 C  CE1 . HIS E 1 19  ? -73.610 68.758  19.757  1.00 50.89  ? 19   HIS E CE1 1 
ATOM   4517 N  NE2 . HIS E 1 19  ? -74.119 69.564  20.674  1.00 48.70  ? 19   HIS E NE2 1 
ATOM   4518 N  N   . PHE E 1 20  ? -74.256 72.462  14.675  1.00 45.65  ? 20   PHE E N   1 
ATOM   4519 C  CA  . PHE E 1 20  ? -74.631 73.050  13.405  1.00 46.64  ? 20   PHE E CA  1 
ATOM   4520 C  C   . PHE E 1 20  ? -75.371 72.018  12.590  1.00 52.62  ? 20   PHE E C   1 
ATOM   4521 O  O   . PHE E 1 20  ? -75.058 70.819  12.658  1.00 53.06  ? 20   PHE E O   1 
ATOM   4522 C  CB  . PHE E 1 20  ? -73.397 73.476  12.616  1.00 48.92  ? 20   PHE E CB  1 
ATOM   4523 C  CG  . PHE E 1 20  ? -72.558 74.512  13.302  1.00 48.63  ? 20   PHE E CG  1 
ATOM   4524 C  CD1 . PHE E 1 20  ? -72.444 75.784  12.770  1.00 46.74  ? 20   PHE E CD1 1 
ATOM   4525 C  CD2 . PHE E 1 20  ? -71.870 74.210  14.471  1.00 46.32  ? 20   PHE E CD2 1 
ATOM   4526 C  CE1 . PHE E 1 20  ? -71.663 76.740  13.397  1.00 47.34  ? 20   PHE E CE1 1 
ATOM   4527 C  CE2 . PHE E 1 20  ? -71.093 75.148  15.096  1.00 42.62  ? 20   PHE E CE2 1 
ATOM   4528 C  CZ  . PHE E 1 20  ? -70.985 76.419  14.562  1.00 44.97  ? 20   PHE E CZ  1 
ATOM   4529 N  N   . GLU E 1 21  ? -76.356 72.488  11.832  1.00 49.46  ? 21   GLU E N   1 
ATOM   4530 C  CA  . GLU E 1 21  ? -77.053 71.653  10.878  1.00 52.13  ? 21   GLU E CA  1 
ATOM   4531 C  C   . GLU E 1 21  ? -77.498 72.482  9.688   1.00 55.93  ? 21   GLU E C   1 
ATOM   4532 O  O   . GLU E 1 21  ? -77.847 73.648  9.821   1.00 57.40  ? 21   GLU E O   1 
ATOM   4533 C  CB  . GLU E 1 21  ? -78.251 70.952  11.514  1.00 57.73  ? 21   GLU E CB  1 
ATOM   4534 C  CG  . GLU E 1 21  ? -78.924 69.961  10.556  1.00 63.88  ? 21   GLU E CG  1 
ATOM   4535 C  CD  . GLU E 1 21  ? -79.502 68.747  11.265  1.00 76.36  ? 21   GLU E CD  1 
ATOM   4536 O  OE1 . GLU E 1 21  ? -79.611 68.780  12.517  1.00 77.14  ? 21   GLU E OE1 1 
ATOM   4537 O  OE2 . GLU E 1 21  ? -79.841 67.760  10.567  1.00 73.62  ? 21   GLU E OE2 1 
ATOM   4538 N  N   . GLN E 1 22  ? -77.472 71.867  8.517   1.00 57.68  ? 22   GLN E N   1 
ATOM   4539 C  CA  . GLN E 1 22  ? -77.860 72.531  7.291   1.00 57.66  ? 22   GLN E CA  1 
ATOM   4540 C  C   . GLN E 1 22  ? -78.342 71.430  6.366   1.00 61.28  ? 22   GLN E C   1 
ATOM   4541 O  O   . GLN E 1 22  ? -77.547 70.649  5.836   1.00 62.73  ? 22   GLN E O   1 
ATOM   4542 C  CB  . GLN E 1 22  ? -76.674 73.289  6.694   1.00 59.95  ? 22   GLN E CB  1 
ATOM   4543 C  CG  . GLN E 1 22  ? -76.946 73.971  5.366   1.00 62.29  ? 22   GLN E CG  1 
ATOM   4544 C  CD  . GLN E 1 22  ? -75.677 74.516  4.720   1.00 62.29  ? 22   GLN E CD  1 
ATOM   4545 O  OE1 . GLN E 1 22  ? -74.804 73.761  4.284   1.00 59.79  ? 22   GLN E OE1 1 
ATOM   4546 N  NE2 . GLN E 1 22  ? -75.573 75.835  4.656   1.00 62.85  ? 22   GLN E NE2 1 
ATOM   4547 N  N   . LYS E 1 23  ? -79.659 71.359  6.206   1.00 68.65  ? 23   LYS E N   1 
ATOM   4548 C  CA  . LYS E 1 23  ? -80.299 70.253  5.502   1.00 67.74  ? 23   LYS E CA  1 
ATOM   4549 C  C   . LYS E 1 23  ? -79.652 70.027  4.145   1.00 68.29  ? 23   LYS E C   1 
ATOM   4550 O  O   . LYS E 1 23  ? -79.239 68.911  3.828   1.00 71.28  ? 23   LYS E O   1 
ATOM   4551 C  CB  . LYS E 1 23  ? -81.815 70.487  5.376   1.00 66.88  ? 23   LYS E CB  1 
ATOM   4552 C  CG  . LYS E 1 23  ? -82.369 70.423  3.944   1.00 72.53  ? 23   LYS E CG  1 
ATOM   4553 C  CD  . LYS E 1 23  ? -83.900 70.416  3.917   1.00 63.96  ? 23   LYS E CD  1 
ATOM   4554 C  CE  . LYS E 1 23  ? -84.449 68.988  3.917   1.00 63.59  ? 23   LYS E CE  1 
ATOM   4555 N  NZ  . LYS E 1 23  ? -85.925 68.947  4.129   1.00 62.72  ? 23   LYS E NZ  1 
ATOM   4556 N  N   . ALA E 1 24  ? -79.537 71.095  3.363   1.00 65.23  ? 24   ALA E N   1 
ATOM   4557 C  CA  . ALA E 1 24  ? -79.034 70.986  2.006   1.00 67.47  ? 24   ALA E CA  1 
ATOM   4558 C  C   . ALA E 1 24  ? -78.212 72.214  1.671   1.00 67.73  ? 24   ALA E C   1 
ATOM   4559 O  O   . ALA E 1 24  ? -78.197 73.171  2.441   1.00 68.63  ? 24   ALA E O   1 
ATOM   4560 C  CB  . ALA E 1 24  ? -80.185 70.834  1.035   1.00 67.70  ? 24   ALA E CB  1 
ATOM   4561 N  N   . SER E 1 25  ? -77.538 72.172  0.522   1.00 67.25  ? 25   SER E N   1 
ATOM   4562 C  CA  . SER E 1 25  ? -76.618 73.227  0.086   1.00 68.48  ? 25   SER E CA  1 
ATOM   4563 C  C   . SER E 1 25  ? -77.081 74.631  0.480   1.00 71.44  ? 25   SER E C   1 
ATOM   4564 O  O   . SER E 1 25  ? -77.023 75.009  1.653   1.00 69.41  ? 25   SER E O   1 
ATOM   4565 C  CB  . SER E 1 25  ? -76.402 73.150  -1.431  1.00 68.99  ? 25   SER E CB  1 
ATOM   4566 O  OG  . SER E 1 25  ? -75.021 73.123  -1.764  1.00 64.01  ? 25   SER E OG  1 
ATOM   4567 N  N   . GLY E 1 26  ? -77.520 75.409  -0.504  1.00 71.59  ? 26   GLY E N   1 
ATOM   4568 C  CA  . GLY E 1 26  ? -78.079 76.720  -0.229  1.00 73.17  ? 26   GLY E CA  1 
ATOM   4569 C  C   . GLY E 1 26  ? -79.265 76.569  0.706   1.00 76.84  ? 26   GLY E C   1 
ATOM   4570 O  O   . GLY E 1 26  ? -80.391 76.315  0.264   1.00 73.72  ? 26   GLY E O   1 
ATOM   4571 N  N   . GLU E 1 27  ? -79.001 76.706  2.003   1.00 70.68  ? 27   GLU E N   1 
ATOM   4572 C  CA  . GLU E 1 27  ? -80.008 76.506  3.037   1.00 68.81  ? 27   GLU E CA  1 
ATOM   4573 C  C   . GLU E 1 27  ? -79.528 77.141  4.331   1.00 68.31  ? 27   GLU E C   1 
ATOM   4574 O  O   . GLU E 1 27  ? -78.324 77.224  4.573   1.00 69.13  ? 27   GLU E O   1 
ATOM   4575 C  CB  . GLU E 1 27  ? -80.244 75.010  3.273   1.00 69.18  ? 27   GLU E CB  1 
ATOM   4576 C  CG  . GLU E 1 27  ? -81.216 74.353  2.307   1.00 72.22  ? 27   GLU E CG  1 
ATOM   4577 C  CD  . GLU E 1 27  ? -82.663 74.746  2.578   1.00 79.38  ? 27   GLU E CD  1 
ATOM   4578 O  OE1 . GLU E 1 27  ? -83.367 73.984  3.281   1.00 78.93  ? 27   GLU E OE1 1 
ATOM   4579 O  OE2 . GLU E 1 27  ? -83.096 75.820  2.094   1.00 78.04  ? 27   GLU E OE2 1 
ATOM   4580 N  N   . PRO E 1 28  ? -80.468 77.585  5.176   1.00 67.61  ? 28   PRO E N   1 
ATOM   4581 C  CA  . PRO E 1 28  ? -80.107 78.106  6.498   1.00 66.76  ? 28   PRO E CA  1 
ATOM   4582 C  C   . PRO E 1 28  ? -79.246 77.109  7.268   1.00 62.97  ? 28   PRO E C   1 
ATOM   4583 O  O   . PRO E 1 28  ? -79.448 75.898  7.151   1.00 62.20  ? 28   PRO E O   1 
ATOM   4584 C  CB  . PRO E 1 28  ? -81.460 78.244  7.203   1.00 64.16  ? 28   PRO E CB  1 
ATOM   4585 C  CG  . PRO E 1 28  ? -82.448 78.380  6.110   1.00 66.55  ? 28   PRO E CG  1 
ATOM   4586 C  CD  . PRO E 1 28  ? -81.923 77.591  4.951   1.00 64.80  ? 28   PRO E CD  1 
ATOM   4587 N  N   . VAL E 1 29  ? -78.283 77.615  8.029   1.00 62.54  ? 29   VAL E N   1 
ATOM   4588 C  CA  . VAL E 1 29  ? -77.581 76.793  9.001   1.00 60.70  ? 29   VAL E CA  1 
ATOM   4589 C  C   . VAL E 1 29  ? -78.221 77.034  10.353  1.00 53.59  ? 29   VAL E C   1 
ATOM   4590 O  O   . VAL E 1 29  ? -78.439 78.176  10.757  1.00 55.24  ? 29   VAL E O   1 
ATOM   4591 C  CB  . VAL E 1 29  ? -76.084 77.126  9.091   1.00 56.90  ? 29   VAL E CB  1 
ATOM   4592 C  CG1 . VAL E 1 29  ? -75.444 76.322  10.215  1.00 51.30  ? 29   VAL E CG1 1 
ATOM   4593 C  CG2 . VAL E 1 29  ? -75.407 76.851  7.768   1.00 55.37  ? 29   VAL E CG2 1 
ATOM   4594 N  N   . VAL E 1 30  ? -78.539 75.959  11.053  1.00 53.94  ? 30   VAL E N   1 
ATOM   4595 C  CA  . VAL E 1 30  ? -79.156 76.115  12.353  1.00 58.29  ? 30   VAL E CA  1 
ATOM   4596 C  C   . VAL E 1 30  ? -78.191 75.789  13.478  1.00 55.68  ? 30   VAL E C   1 
ATOM   4597 O  O   . VAL E 1 30  ? -77.628 74.697  13.540  1.00 52.56  ? 30   VAL E O   1 
ATOM   4598 C  CB  . VAL E 1 30  ? -80.437 75.288  12.478  1.00 54.15  ? 30   VAL E CB  1 
ATOM   4599 C  CG1 . VAL E 1 30  ? -80.988 75.395  13.885  1.00 46.60  ? 30   VAL E CG1 1 
ATOM   4600 C  CG2 . VAL E 1 30  ? -81.456 75.777  11.463  1.00 54.06  ? 30   VAL E CG2 1 
ATOM   4601 N  N   . LEU E 1 31  ? -78.002 76.762  14.361  1.00 57.24  ? 31   LEU E N   1 
ATOM   4602 C  CA  . LEU E 1 31  ? -77.161 76.584  15.536  1.00 58.92  ? 31   LEU E CA  1 
ATOM   4603 C  C   . LEU E 1 31  ? -78.008 76.371  16.778  1.00 56.35  ? 31   LEU E C   1 
ATOM   4604 O  O   . LEU E 1 31  ? -78.991 77.082  17.001  1.00 59.38  ? 31   LEU E O   1 
ATOM   4605 C  CB  . LEU E 1 31  ? -76.275 77.810  15.754  1.00 59.13  ? 31   LEU E CB  1 
ATOM   4606 C  CG  . LEU E 1 31  ? -75.088 78.057  14.828  1.00 55.84  ? 31   LEU E CG  1 
ATOM   4607 C  CD1 . LEU E 1 31  ? -75.529 78.263  13.381  1.00 50.82  ? 31   LEU E CD1 1 
ATOM   4608 C  CD2 . LEU E 1 31  ? -74.297 79.251  15.347  1.00 49.80  ? 31   LEU E CD2 1 
ATOM   4609 N  N   . SER E 1 32  ? -77.628 75.388  17.582  1.00 55.05  ? 32   SER E N   1 
ATOM   4610 C  CA  . SER E 1 32  ? -78.229 75.224  18.900  1.00 62.11  ? 32   SER E CA  1 
ATOM   4611 C  C   . SER E 1 32  ? -77.172 74.773  19.894  1.00 56.28  ? 32   SER E C   1 
ATOM   4612 O  O   . SER E 1 32  ? -76.056 74.437  19.507  1.00 54.48  ? 32   SER E O   1 
ATOM   4613 C  CB  . SER E 1 32  ? -79.416 74.256  18.868  1.00 60.60  ? 32   SER E CB  1 
ATOM   4614 O  OG  . SER E 1 32  ? -79.006 72.951  18.510  1.00 67.12  ? 32   SER E OG  1 
ATOM   4615 N  N   . GLY E 1 33  ? -77.518 74.785  21.175  1.00 58.24  ? 33   GLY E N   1 
ATOM   4616 C  CA  . GLY E 1 33  ? -76.556 74.471  22.213  1.00 62.36  ? 33   GLY E CA  1 
ATOM   4617 C  C   . GLY E 1 33  ? -76.640 75.422  23.394  1.00 66.63  ? 33   GLY E C   1 
ATOM   4618 O  O   . GLY E 1 33  ? -77.706 75.963  23.692  1.00 69.00  ? 33   GLY E O   1 
ATOM   4619 N  N   . GLN E 1 34  ? -75.510 75.637  24.060  1.00 64.94  ? 34   GLN E N   1 
ATOM   4620 C  CA  . GLN E 1 34  ? -75.510 76.370  25.314  1.00 65.21  ? 34   GLN E CA  1 
ATOM   4621 C  C   . GLN E 1 34  ? -74.110 76.686  25.831  1.00 64.11  ? 34   GLN E C   1 
ATOM   4622 O  O   . GLN E 1 34  ? -73.267 75.800  25.966  1.00 62.83  ? 34   GLN E O   1 
ATOM   4623 C  CB  . GLN E 1 34  ? -76.274 75.570  26.366  1.00 68.53  ? 34   GLN E CB  1 
ATOM   4624 C  CG  . GLN E 1 34  ? -76.176 76.129  27.763  1.00 69.37  ? 34   GLN E CG  1 
ATOM   4625 C  CD  . GLN E 1 34  ? -76.695 75.157  28.794  1.00 74.32  ? 34   GLN E CD  1 
ATOM   4626 O  OE1 . GLN E 1 34  ? -76.042 74.906  29.811  1.00 72.23  ? 34   GLN E OE1 1 
ATOM   4627 N  NE2 . GLN E 1 34  ? -77.873 74.589  28.534  1.00 73.03  ? 34   GLN E NE2 1 
ATOM   4628 N  N   . ILE E 1 35  ? -73.884 77.959  26.138  1.00 67.83  ? 35   ILE E N   1 
ATOM   4629 C  CA  . ILE E 1 35  ? -72.617 78.421  26.698  1.00 67.05  ? 35   ILE E CA  1 
ATOM   4630 C  C   . ILE E 1 35  ? -72.785 78.757  28.182  1.00 65.83  ? 35   ILE E C   1 
ATOM   4631 O  O   . ILE E 1 35  ? -73.864 79.147  28.624  1.00 64.91  ? 35   ILE E O   1 
ATOM   4632 C  CB  . ILE E 1 35  ? -72.097 79.655  25.936  1.00 64.19  ? 35   ILE E CB  1 
ATOM   4633 C  CG1 . ILE E 1 35  ? -72.225 79.424  24.425  1.00 63.08  ? 35   ILE E CG1 1 
ATOM   4634 C  CG2 . ILE E 1 35  ? -70.660 79.967  26.337  1.00 60.55  ? 35   ILE E CG2 1 
ATOM   4635 C  CD1 . ILE E 1 35  ? -72.064 80.670  23.583  1.00 62.70  ? 35   ILE E CD1 1 
ATOM   4636 N  N   . THR E 1 36  ? -71.715 78.591  28.948  1.00 64.93  ? 36   THR E N   1 
ATOM   4637 C  CA  . THR E 1 36  ? -71.776 78.797  30.387  1.00 68.16  ? 36   THR E CA  1 
ATOM   4638 C  C   . THR E 1 36  ? -70.560 79.575  30.888  1.00 72.82  ? 36   THR E C   1 
ATOM   4639 O  O   . THR E 1 36  ? -69.549 79.683  30.185  1.00 69.93  ? 36   THR E O   1 
ATOM   4640 C  CB  . THR E 1 36  ? -71.880 77.456  31.135  1.00 64.40  ? 36   THR E CB  1 
ATOM   4641 O  OG1 . THR E 1 36  ? -70.620 76.777  31.085  1.00 65.16  ? 36   THR E OG1 1 
ATOM   4642 C  CG2 . THR E 1 36  ? -72.959 76.582  30.515  1.00 58.84  ? 36   THR E CG2 1 
ATOM   4643 N  N   . GLY E 1 37  ? -70.667 80.117  32.102  1.00 72.65  ? 37   GLY E N   1 
ATOM   4644 C  CA  . GLY E 1 37  ? -69.600 80.913  32.689  1.00 69.23  ? 37   GLY E CA  1 
ATOM   4645 C  C   . GLY E 1 37  ? -69.478 82.320  32.120  1.00 73.49  ? 37   GLY E C   1 
ATOM   4646 O  O   . GLY E 1 37  ? -68.389 82.901  32.105  1.00 74.57  ? 37   GLY E O   1 
ATOM   4647 N  N   . LEU E 1 38  ? -70.595 82.873  31.653  1.00 72.01  ? 38   LEU E N   1 
ATOM   4648 C  CA  . LEU E 1 38  ? -70.607 84.206  31.054  1.00 76.49  ? 38   LEU E CA  1 
ATOM   4649 C  C   . LEU E 1 38  ? -71.168 85.263  32.014  1.00 80.48  ? 38   LEU E C   1 
ATOM   4650 O  O   . LEU E 1 38  ? -71.880 84.933  32.969  1.00 79.69  ? 38   LEU E O   1 
ATOM   4651 C  CB  . LEU E 1 38  ? -71.423 84.199  29.754  1.00 74.69  ? 38   LEU E CB  1 
ATOM   4652 C  CG  . LEU E 1 38  ? -70.738 83.839  28.427  1.00 71.10  ? 38   LEU E CG  1 
ATOM   4653 C  CD1 . LEU E 1 38  ? -71.756 83.416  27.376  1.00 65.65  ? 38   LEU E CD1 1 
ATOM   4654 C  CD2 . LEU E 1 38  ? -69.891 84.988  27.909  1.00 64.14  ? 38   LEU E CD2 1 
ATOM   4655 N  N   . THR E 1 39  ? -70.834 86.530  31.760  1.00 81.21  ? 39   THR E N   1 
ATOM   4656 C  CA  . THR E 1 39  ? -71.434 87.656  32.484  1.00 81.79  ? 39   THR E CA  1 
ATOM   4657 C  C   . THR E 1 39  ? -72.808 87.963  31.890  1.00 78.67  ? 39   THR E C   1 
ATOM   4658 O  O   . THR E 1 39  ? -72.973 87.956  30.667  1.00 77.44  ? 39   THR E O   1 
ATOM   4659 C  CB  . THR E 1 39  ? -70.549 88.940  32.438  1.00 76.50  ? 39   THR E CB  1 
ATOM   4660 O  OG1 . THR E 1 39  ? -70.566 89.508  31.119  1.00 68.30  ? 39   THR E OG1 1 
ATOM   4661 C  CG2 . THR E 1 39  ? -69.105 88.634  32.859  1.00 75.26  ? 39   THR E CG2 1 
ATOM   4662 N  N   . GLU E 1 40  ? -73.791 88.219  32.749  1.00 76.40  ? 40   GLU E N   1 
ATOM   4663 C  CA  . GLU E 1 40  ? -75.151 88.481  32.284  1.00 78.50  ? 40   GLU E CA  1 
ATOM   4664 C  C   . GLU E 1 40  ? -75.191 89.522  31.162  1.00 79.60  ? 40   GLU E C   1 
ATOM   4665 O  O   . GLU E 1 40  ? -74.586 90.589  31.275  1.00 76.77  ? 40   GLU E O   1 
ATOM   4666 C  CB  . GLU E 1 40  ? -76.029 88.933  33.444  1.00 81.26  ? 40   GLU E CB  1 
ATOM   4667 C  CG  . GLU E 1 40  ? -77.439 89.304  33.033  1.00 84.59  ? 40   GLU E CG  1 
ATOM   4668 C  CD  . GLU E 1 40  ? -78.283 89.737  34.212  1.00 91.12  ? 40   GLU E CD  1 
ATOM   4669 O  OE1 . GLU E 1 40  ? -77.725 90.368  35.138  1.00 91.56  ? 40   GLU E OE1 1 
ATOM   4670 O  OE2 . GLU E 1 40  ? -79.500 89.442  34.215  1.00 93.44  ? 40   GLU E OE2 1 
ATOM   4671 N  N   . GLY E 1 41  ? -75.891 89.201  30.074  1.00 76.99  ? 41   GLY E N   1 
ATOM   4672 C  CA  . GLY E 1 41  ? -76.049 90.133  28.970  1.00 74.19  ? 41   GLY E CA  1 
ATOM   4673 C  C   . GLY E 1 41  ? -75.649 89.605  27.601  1.00 73.04  ? 41   GLY E C   1 
ATOM   4674 O  O   . GLY E 1 41  ? -75.501 88.397  27.406  1.00 70.68  ? 41   GLY E O   1 
ATOM   4675 N  N   . GLN E 1 42  ? -75.469 90.528  26.656  1.00 68.29  ? 42   GLN E N   1 
ATOM   4676 C  CA  . GLN E 1 42  ? -75.135 90.193  25.275  1.00 63.45  ? 42   GLN E CA  1 
ATOM   4677 C  C   . GLN E 1 42  ? -73.635 90.078  25.040  1.00 66.31  ? 42   GLN E C   1 
ATOM   4678 O  O   . GLN E 1 42  ? -72.838 90.800  25.643  1.00 67.82  ? 42   GLN E O   1 
ATOM   4679 C  CB  . GLN E 1 42  ? -75.719 91.232  24.318  1.00 63.87  ? 42   GLN E CB  1 
ATOM   4680 C  CG  . GLN E 1 42  ? -77.229 91.133  24.129  1.00 70.82  ? 42   GLN E CG  1 
ATOM   4681 C  CD  . GLN E 1 42  ? -77.770 92.163  23.143  1.00 74.78  ? 42   GLN E CD  1 
ATOM   4682 O  OE1 . GLN E 1 42  ? -78.565 91.834  22.258  1.00 70.98  ? 42   GLN E OE1 1 
ATOM   4683 N  NE2 . GLN E 1 42  ? -77.336 93.414  23.290  1.00 68.89  ? 42   GLN E NE2 1 
ATOM   4684 N  N   . HIS E 1 43  ? -73.265 89.169  24.140  1.00 67.15  ? 43   HIS E N   1 
ATOM   4685 C  CA  . HIS E 1 43  ? -71.868 88.903  23.815  1.00 61.90  ? 43   HIS E CA  1 
ATOM   4686 C  C   . HIS E 1 43  ? -71.665 88.745  22.318  1.00 61.76  ? 43   HIS E C   1 
ATOM   4687 O  O   . HIS E 1 43  ? -72.448 88.069  21.649  1.00 62.37  ? 43   HIS E O   1 
ATOM   4688 C  CB  . HIS E 1 43  ? -71.398 87.636  24.527  1.00 59.22  ? 43   HIS E CB  1 
ATOM   4689 C  CG  . HIS E 1 43  ? -71.339 87.775  26.014  1.00 64.32  ? 43   HIS E CG  1 
ATOM   4690 N  ND1 . HIS E 1 43  ? -70.206 88.194  26.676  1.00 62.28  ? 43   HIS E ND1 1 
ATOM   4691 C  CD2 . HIS E 1 43  ? -72.280 87.572  26.967  1.00 64.29  ? 43   HIS E CD2 1 
ATOM   4692 C  CE1 . HIS E 1 43  ? -70.448 88.235  27.973  1.00 65.55  ? 43   HIS E CE1 1 
ATOM   4693 N  NE2 . HIS E 1 43  ? -71.697 87.859  28.177  1.00 67.74  ? 43   HIS E NE2 1 
ATOM   4694 N  N   . GLY E 1 44  ? -70.619 89.378  21.790  1.00 62.06  ? 44   GLY E N   1 
ATOM   4695 C  CA  . GLY E 1 44  ? -70.216 89.150  20.411  1.00 60.18  ? 44   GLY E CA  1 
ATOM   4696 C  C   . GLY E 1 44  ? -70.086 87.659  20.134  1.00 56.71  ? 44   GLY E C   1 
ATOM   4697 O  O   . GLY E 1 44  ? -69.615 86.892  20.975  1.00 55.60  ? 44   GLY E O   1 
ATOM   4698 N  N   . PHE E 1 45  ? -70.516 87.247  18.950  1.00 53.80  ? 45   PHE E N   1 
ATOM   4699 C  CA  . PHE E 1 45  ? -70.564 85.840  18.590  1.00 53.54  ? 45   PHE E CA  1 
ATOM   4700 C  C   . PHE E 1 45  ? -70.261 85.773  17.111  1.00 53.53  ? 45   PHE E C   1 
ATOM   4701 O  O   . PHE E 1 45  ? -71.066 86.213  16.288  1.00 53.58  ? 45   PHE E O   1 
ATOM   4702 C  CB  . PHE E 1 45  ? -71.964 85.310  18.857  1.00 54.46  ? 45   PHE E CB  1 
ATOM   4703 C  CG  . PHE E 1 45  ? -72.067 83.812  18.886  1.00 57.26  ? 45   PHE E CG  1 
ATOM   4704 C  CD1 . PHE E 1 45  ? -71.558 83.089  19.952  1.00 58.51  ? 45   PHE E CD1 1 
ATOM   4705 C  CD2 . PHE E 1 45  ? -72.719 83.128  17.868  1.00 56.79  ? 45   PHE E CD2 1 
ATOM   4706 C  CE1 . PHE E 1 45  ? -71.679 81.707  19.992  1.00 60.20  ? 45   PHE E CE1 1 
ATOM   4707 C  CE2 . PHE E 1 45  ? -72.843 81.752  17.901  1.00 54.35  ? 45   PHE E CE2 1 
ATOM   4708 C  CZ  . PHE E 1 45  ? -72.326 81.039  18.964  1.00 58.54  ? 45   PHE E CZ  1 
ATOM   4709 N  N   . HIS E 1 46  ? -69.091 85.257  16.761  1.00 48.62  ? 46   HIS E N   1 
ATOM   4710 C  CA  . HIS E 1 46  ? -68.652 85.357  15.378  1.00 51.42  ? 46   HIS E CA  1 
ATOM   4711 C  C   . HIS E 1 46  ? -67.862 84.140  14.924  1.00 49.70  ? 46   HIS E C   1 
ATOM   4712 O  O   . HIS E 1 46  ? -67.238 83.440  15.728  1.00 43.10  ? 46   HIS E O   1 
ATOM   4713 C  CB  . HIS E 1 46  ? -67.796 86.620  15.162  1.00 48.92  ? 46   HIS E CB  1 
ATOM   4714 C  CG  . HIS E 1 46  ? -68.243 87.808  15.960  1.00 54.45  ? 46   HIS E CG  1 
ATOM   4715 N  ND1 . HIS E 1 46  ? -69.056 88.792  15.440  1.00 53.90  ? 46   HIS E ND1 1 
ATOM   4716 C  CD2 . HIS E 1 46  ? -67.981 88.173  17.238  1.00 53.71  ? 46   HIS E CD2 1 
ATOM   4717 C  CE1 . HIS E 1 46  ? -69.284 89.705  16.368  1.00 56.21  ? 46   HIS E CE1 1 
ATOM   4718 N  NE2 . HIS E 1 46  ? -68.643 89.354  17.467  1.00 54.44  ? 46   HIS E NE2 1 
ATOM   4719 N  N   . VAL E 1 47  ? -67.896 83.896  13.622  1.00 48.65  ? 47   VAL E N   1 
ATOM   4720 C  CA  . VAL E 1 47  ? -66.967 82.970  13.026  1.00 46.01  ? 47   VAL E CA  1 
ATOM   4721 C  C   . VAL E 1 47  ? -65.797 83.789  12.551  1.00 48.53  ? 47   VAL E C   1 
ATOM   4722 O  O   . VAL E 1 47  ? -65.947 84.658  11.689  1.00 53.09  ? 47   VAL E O   1 
ATOM   4723 C  CB  . VAL E 1 47  ? -67.553 82.229  11.827  1.00 45.84  ? 47   VAL E CB  1 
ATOM   4724 C  CG1 . VAL E 1 47  ? -66.555 81.189  11.335  1.00 43.26  ? 47   VAL E CG1 1 
ATOM   4725 C  CG2 . VAL E 1 47  ? -68.874 81.571  12.198  1.00 47.51  ? 47   VAL E CG2 1 
ATOM   4726 N  N   . HIS E 1 48  ? -64.631 83.524  13.122  1.00 47.09  ? 48   HIS E N   1 
ATOM   4727 C  CA  . HIS E 1 48  ? -63.410 84.155  12.653  1.00 51.00  ? 48   HIS E CA  1 
ATOM   4728 C  C   . HIS E 1 48  ? -62.807 83.344  11.512  1.00 48.38  ? 48   HIS E C   1 
ATOM   4729 O  O   . HIS E 1 48  ? -63.197 82.196  11.277  1.00 43.99  ? 48   HIS E O   1 
ATOM   4730 C  CB  . HIS E 1 48  ? -62.416 84.323  13.796  1.00 52.18  ? 48   HIS E CB  1 
ATOM   4731 C  CG  . HIS E 1 48  ? -62.860 85.294  14.844  1.00 51.99  ? 48   HIS E CG  1 
ATOM   4732 N  ND1 . HIS E 1 48  ? -62.119 86.403  15.195  1.00 55.29  ? 48   HIS E ND1 1 
ATOM   4733 C  CD2 . HIS E 1 48  ? -63.974 85.330  15.611  1.00 50.54  ? 48   HIS E CD2 1 
ATOM   4734 C  CE1 . HIS E 1 48  ? -62.749 87.071  16.144  1.00 51.29  ? 48   HIS E CE1 1 
ATOM   4735 N  NE2 . HIS E 1 48  ? -63.877 86.441  16.416  1.00 54.53  ? 48   HIS E NE2 1 
ATOM   4736 N  N   . GLN E 1 49  ? -61.853 83.954  10.814  1.00 48.55  ? 49   GLN E N   1 
ATOM   4737 C  CA  . GLN E 1 49  ? -61.345 83.419  9.559   1.00 47.93  ? 49   GLN E CA  1 
ATOM   4738 C  C   . GLN E 1 49  ? -60.607 82.080  9.679   1.00 48.82  ? 49   GLN E C   1 
ATOM   4739 O  O   . GLN E 1 49  ? -60.872 81.149  8.912   1.00 44.42  ? 49   GLN E O   1 
ATOM   4740 C  CB  . GLN E 1 49  ? -60.451 84.454  8.870   1.00 49.81  ? 49   GLN E CB  1 
ATOM   4741 C  CG  . GLN E 1 49  ? -59.935 84.011  7.505   1.00 52.04  ? 49   GLN E CG  1 
ATOM   4742 C  CD  . GLN E 1 49  ? -59.106 85.086  6.802   1.00 56.99  ? 49   GLN E CD  1 
ATOM   4743 O  OE1 . GLN E 1 49  ? -58.659 86.062  7.426   1.00 52.35  ? 49   GLN E OE1 1 
ATOM   4744 N  NE2 . GLN E 1 49  ? -58.902 84.910  5.490   1.00 48.46  ? 49   GLN E NE2 1 
ATOM   4745 N  N   . TYR E 1 50  ? -59.691 81.974  10.639  1.00 49.51  ? 50   TYR E N   1 
ATOM   4746 C  CA  . TYR E 1 50  ? -58.790 80.815  10.689  1.00 45.22  ? 50   TYR E CA  1 
ATOM   4747 C  C   . TYR E 1 50  ? -59.085 79.824  11.800  1.00 41.07  ? 50   TYR E C   1 
ATOM   4748 O  O   . TYR E 1 50  ? -59.301 80.208  12.940  1.00 43.54  ? 50   TYR E O   1 
ATOM   4749 C  CB  . TYR E 1 50  ? -57.341 81.279  10.766  1.00 46.05  ? 50   TYR E CB  1 
ATOM   4750 C  CG  . TYR E 1 50  ? -56.947 82.103  9.572   1.00 45.76  ? 50   TYR E CG  1 
ATOM   4751 C  CD1 . TYR E 1 50  ? -56.903 81.532  8.304   1.00 46.00  ? 50   TYR E CD1 1 
ATOM   4752 C  CD2 . TYR E 1 50  ? -56.636 83.451  9.703   1.00 47.69  ? 50   TYR E CD2 1 
ATOM   4753 C  CE1 . TYR E 1 50  ? -56.553 82.269  7.203   1.00 45.88  ? 50   TYR E CE1 1 
ATOM   4754 C  CE2 . TYR E 1 50  ? -56.283 84.208  8.596   1.00 53.30  ? 50   TYR E CE2 1 
ATOM   4755 C  CZ  . TYR E 1 50  ? -56.247 83.608  7.347   1.00 55.07  ? 50   TYR E CZ  1 
ATOM   4756 O  OH  . TYR E 1 50  ? -55.892 84.341  6.233   1.00 60.77  ? 50   TYR E OH  1 
ATOM   4757 N  N   . GLY E 1 51  ? -59.098 78.541  11.455  1.00 41.96  ? 51   GLY E N   1 
ATOM   4758 C  CA  . GLY E 1 51  ? -59.306 77.500  12.443  1.00 41.68  ? 51   GLY E CA  1 
ATOM   4759 C  C   . GLY E 1 51  ? -57.955 77.193  13.045  1.00 46.01  ? 51   GLY E C   1 
ATOM   4760 O  O   . GLY E 1 51  ? -57.449 76.074  12.942  1.00 47.08  ? 51   GLY E O   1 
ATOM   4761 N  N   . ASP E 1 52  ? -57.376 78.215  13.666  1.00 46.55  ? 52   ASP E N   1 
ATOM   4762 C  CA  . ASP E 1 52  ? -55.994 78.214  14.114  1.00 43.90  ? 52   ASP E CA  1 
ATOM   4763 C  C   . ASP E 1 52  ? -55.961 78.688  15.560  1.00 47.63  ? 52   ASP E C   1 
ATOM   4764 O  O   . ASP E 1 52  ? -56.244 79.850  15.851  1.00 46.14  ? 52   ASP E O   1 
ATOM   4765 C  CB  . ASP E 1 52  ? -55.176 79.145  13.218  1.00 46.35  ? 52   ASP E CB  1 
ATOM   4766 C  CG  . ASP E 1 52  ? -53.676 79.180  13.577  1.00 50.86  ? 52   ASP E CG  1 
ATOM   4767 O  OD1 . ASP E 1 52  ? -53.305 78.931  14.745  1.00 49.28  ? 52   ASP E OD1 1 
ATOM   4768 O  OD2 . ASP E 1 52  ? -52.865 79.484  12.674  1.00 46.95  ? 52   ASP E OD2 1 
ATOM   4769 N  N   . ASN E 1 53  ? -55.649 77.777  16.472  1.00 46.68  ? 53   ASN E N   1 
ATOM   4770 C  CA  . ASN E 1 53  ? -55.601 78.125  17.881  1.00 51.20  ? 53   ASN E CA  1 
ATOM   4771 C  C   . ASN E 1 53  ? -54.195 77.954  18.427  1.00 49.00  ? 53   ASN E C   1 
ATOM   4772 O  O   . ASN E 1 53  ? -54.002 77.597  19.590  1.00 51.86  ? 53   ASN E O   1 
ATOM   4773 C  CB  . ASN E 1 53  ? -56.644 77.333  18.692  1.00 50.76  ? 53   ASN E CB  1 
ATOM   4774 C  CG  . ASN E 1 53  ? -58.097 77.782  18.392  1.00 62.83  ? 53   ASN E CG  1 
ATOM   4775 O  OD1 . ASN E 1 53  ? -58.351 78.554  17.447  1.00 56.49  ? 53   ASN E OD1 1 
ATOM   4776 N  ND2 . ASN E 1 53  ? -59.052 77.295  19.199  1.00 60.35  ? 53   ASN E ND2 1 
ATOM   4777 N  N   . THR E 1 54  ? -53.212 78.220  17.577  1.00 46.02  ? 54   THR E N   1 
ATOM   4778 C  CA  . THR E 1 54  ? -51.822 78.110  17.993  1.00 55.66  ? 54   THR E CA  1 
ATOM   4779 C  C   . THR E 1 54  ? -51.539 79.033  19.173  1.00 57.96  ? 54   THR E C   1 
ATOM   4780 O  O   . THR E 1 54  ? -50.973 78.604  20.175  1.00 59.87  ? 54   THR E O   1 
ATOM   4781 C  CB  . THR E 1 54  ? -50.837 78.386  16.844  1.00 55.60  ? 54   THR E CB  1 
ATOM   4782 O  OG1 . THR E 1 54  ? -51.258 79.548  16.120  1.00 58.03  ? 54   THR E OG1 1 
ATOM   4783 C  CG2 . THR E 1 54  ? -50.767 77.182  15.888  1.00 52.02  ? 54   THR E CG2 1 
ATOM   4784 N  N   . GLN E 1 55  ? -51.957 80.292  19.060  1.00 60.96  ? 55   GLN E N   1 
ATOM   4785 C  CA  . GLN E 1 55  ? -51.819 81.250  20.157  1.00 62.23  ? 55   GLN E CA  1 
ATOM   4786 C  C   . GLN E 1 55  ? -53.183 81.642  20.698  1.00 64.24  ? 55   GLN E C   1 
ATOM   4787 O  O   . GLN E 1 55  ? -53.573 82.808  20.609  1.00 68.27  ? 55   GLN E O   1 
ATOM   4788 C  CB  . GLN E 1 55  ? -51.088 82.502  19.689  1.00 60.59  ? 55   GLN E CB  1 
ATOM   4789 C  CG  . GLN E 1 55  ? -49.757 82.212  19.043  1.00 69.97  ? 55   GLN E CG  1 
ATOM   4790 C  CD  . GLN E 1 55  ? -49.143 83.438  18.399  1.00 80.45  ? 55   GLN E CD  1 
ATOM   4791 O  OE1 . GLN E 1 55  ? -49.766 84.088  17.553  1.00 78.72  ? 55   GLN E OE1 1 
ATOM   4792 N  NE2 . GLN E 1 55  ? -47.909 83.760  18.790  1.00 78.24  ? 55   GLN E NE2 1 
ATOM   4793 N  N   . GLY E 1 56  ? -53.901 80.668  21.258  1.00 62.43  ? 56   GLY E N   1 
ATOM   4794 C  CA  . GLY E 1 56  ? -55.257 80.882  21.740  1.00 60.84  ? 56   GLY E CA  1 
ATOM   4795 C  C   . GLY E 1 56  ? -56.216 81.290  20.630  1.00 57.51  ? 56   GLY E C   1 
ATOM   4796 O  O   . GLY E 1 56  ? -56.053 80.898  19.472  1.00 53.95  ? 56   GLY E O   1 
ATOM   4797 N  N   . CYS E 1 57  ? -57.211 82.098  20.985  1.00 57.00  ? 57   CYS E N   1 
ATOM   4798 C  CA  . CYS E 1 57  ? -58.222 82.537  20.028  1.00 54.29  ? 57   CYS E CA  1 
ATOM   4799 C  C   . CYS E 1 57  ? -57.692 83.614  19.105  1.00 51.38  ? 57   CYS E C   1 
ATOM   4800 O  O   . CYS E 1 57  ? -58.255 83.874  18.034  1.00 48.26  ? 57   CYS E O   1 
ATOM   4801 C  CB  . CYS E 1 57  ? -59.447 83.045  20.775  1.00 49.39  ? 57   CYS E CB  1 
ATOM   4802 S  SG  . CYS E 1 57  ? -60.100 81.797  21.887  1.00 59.50  ? 57   CYS E SG  1 
ATOM   4803 N  N   . THR E 1 58  ? -56.589 84.221  19.521  1.00 50.92  ? 58   THR E N   1 
ATOM   4804 C  CA  . THR E 1 58  ? -56.042 85.364  18.814  1.00 52.00  ? 58   THR E CA  1 
ATOM   4805 C  C   . THR E 1 58  ? -55.504 84.952  17.449  1.00 48.64  ? 58   THR E C   1 
ATOM   4806 O  O   . THR E 1 58  ? -55.538 85.740  16.502  1.00 49.81  ? 58   THR E O   1 
ATOM   4807 C  CB  . THR E 1 58  ? -54.985 86.123  19.670  1.00 59.33  ? 58   THR E CB  1 
ATOM   4808 O  OG1 . THR E 1 58  ? -53.666 85.652  19.369  1.00 58.21  ? 58   THR E OG1 1 
ATOM   4809 C  CG2 . THR E 1 58  ? -55.278 85.948  21.176  1.00 58.81  ? 58   THR E CG2 1 
ATOM   4810 N  N   . SER E 1 59  ? -55.055 83.708  17.327  1.00 48.64  ? 59   SER E N   1 
ATOM   4811 C  CA  . SER E 1 59  ? -54.562 83.226  16.033  1.00 50.98  ? 59   SER E CA  1 
ATOM   4812 C  C   . SER E 1 59  ? -55.685 82.920  15.015  1.00 48.09  ? 59   SER E C   1 
ATOM   4813 O  O   . SER E 1 59  ? -55.415 82.744  13.817  1.00 40.81  ? 59   SER E O   1 
ATOM   4814 C  CB  . SER E 1 59  ? -53.604 82.039  16.211  1.00 49.45  ? 59   SER E CB  1 
ATOM   4815 O  OG  . SER E 1 59  ? -53.935 81.288  17.364  1.00 52.98  ? 59   SER E OG  1 
ATOM   4816 N  N   . ALA E 1 60  ? -56.933 82.888  15.494  1.00 42.20  ? 60   ALA E N   1 
ATOM   4817 C  CA  . ALA E 1 60  ? -58.098 82.721  14.615  1.00 48.14  ? 60   ALA E CA  1 
ATOM   4818 C  C   . ALA E 1 60  ? -58.222 83.835  13.575  1.00 50.54  ? 60   ALA E C   1 
ATOM   4819 O  O   . ALA E 1 60  ? -58.840 83.648  12.522  1.00 46.47  ? 60   ALA E O   1 
ATOM   4820 C  CB  . ALA E 1 60  ? -59.395 82.605  15.426  1.00 40.98  ? 60   ALA E CB  1 
ATOM   4821 N  N   . GLY E 1 61  ? -57.642 84.994  13.883  1.00 53.12  ? 61   GLY E N   1 
ATOM   4822 C  CA  . GLY E 1 61  ? -57.695 86.139  12.990  1.00 51.88  ? 61   GLY E CA  1 
ATOM   4823 C  C   . GLY E 1 61  ? -58.964 86.973  13.094  1.00 50.72  ? 61   GLY E C   1 
ATOM   4824 O  O   . GLY E 1 61  ? -59.612 87.026  14.142  1.00 48.32  ? 61   GLY E O   1 
ATOM   4825 N  N   . PRO E 1 62  ? -59.324 87.635  11.988  1.00 53.59  ? 62   PRO E N   1 
ATOM   4826 C  CA  . PRO E 1 62  ? -60.475 88.541  11.902  1.00 57.47  ? 62   PRO E CA  1 
ATOM   4827 C  C   . PRO E 1 62  ? -61.794 87.778  11.775  1.00 58.46  ? 62   PRO E C   1 
ATOM   4828 O  O   . PRO E 1 62  ? -61.783 86.546  11.645  1.00 58.31  ? 62   PRO E O   1 
ATOM   4829 C  CB  . PRO E 1 62  ? -60.216 89.318  10.595  1.00 55.42  ? 62   PRO E CB  1 
ATOM   4830 C  CG  . PRO E 1 62  ? -58.866 88.864  10.083  1.00 53.71  ? 62   PRO E CG  1 
ATOM   4831 C  CD  . PRO E 1 62  ? -58.607 87.535  10.705  1.00 53.51  ? 62   PRO E CD  1 
ATOM   4832 N  N   . HIS E 1 63  ? -62.910 88.508  11.801  1.00 58.67  ? 63   HIS E N   1 
ATOM   4833 C  CA  . HIS E 1 63  ? -64.222 87.930  11.505  1.00 57.71  ? 63   HIS E CA  1 
ATOM   4834 C  C   . HIS E 1 63  ? -64.177 87.350  10.085  1.00 55.38  ? 63   HIS E C   1 
ATOM   4835 O  O   . HIS E 1 63  ? -63.612 87.959  9.187   1.00 54.18  ? 63   HIS E O   1 
ATOM   4836 C  CB  . HIS E 1 63  ? -65.328 88.998  11.631  1.00 54.51  ? 63   HIS E CB  1 
ATOM   4837 C  CG  . HIS E 1 63  ? -65.577 89.473  13.039  1.00 55.78  ? 63   HIS E CG  1 
ATOM   4838 N  ND1 . HIS E 1 63  ? -66.580 90.369  13.357  1.00 56.20  ? 63   HIS E ND1 1 
ATOM   4839 C  CD2 . HIS E 1 63  ? -64.966 89.168  14.210  1.00 55.62  ? 63   HIS E CD2 1 
ATOM   4840 C  CE1 . HIS E 1 63  ? -66.574 90.597  14.659  1.00 57.07  ? 63   HIS E CE1 1 
ATOM   4841 N  NE2 . HIS E 1 63  ? -65.607 89.878  15.203  1.00 57.46  ? 63   HIS E NE2 1 
ATOM   4842 N  N   . PHE E 1 64  ? -64.731 86.161  9.879   1.00 52.37  ? 64   PHE E N   1 
ATOM   4843 C  CA  . PHE E 1 64  ? -64.739 85.586  8.539   1.00 53.02  ? 64   PHE E CA  1 
ATOM   4844 C  C   . PHE E 1 64  ? -65.334 86.602  7.552   1.00 54.57  ? 64   PHE E C   1 
ATOM   4845 O  O   . PHE E 1 64  ? -66.378 87.178  7.820   1.00 53.95  ? 64   PHE E O   1 
ATOM   4846 C  CB  . PHE E 1 64  ? -65.521 84.263  8.527   1.00 51.21  ? 64   PHE E CB  1 
ATOM   4847 C  CG  . PHE E 1 64  ? -65.480 83.541  7.202   1.00 47.84  ? 64   PHE E CG  1 
ATOM   4848 C  CD1 . PHE E 1 64  ? -64.453 83.775  6.298   1.00 49.30  ? 64   PHE E CD1 1 
ATOM   4849 C  CD2 . PHE E 1 64  ? -66.470 82.634  6.862   1.00 46.17  ? 64   PHE E CD2 1 
ATOM   4850 C  CE1 . PHE E 1 64  ? -64.413 83.121  5.072   1.00 48.51  ? 64   PHE E CE1 1 
ATOM   4851 C  CE2 . PHE E 1 64  ? -66.439 81.974  5.652   1.00 46.66  ? 64   PHE E CE2 1 
ATOM   4852 C  CZ  . PHE E 1 64  ? -65.407 82.210  4.753   1.00 49.17  ? 64   PHE E CZ  1 
ATOM   4853 N  N   . ASN E 1 65  ? -64.671 86.827  6.421   1.00 56.07  ? 65   ASN E N   1 
ATOM   4854 C  CA  . ASN E 1 65  ? -65.091 87.886  5.503   1.00 58.09  ? 65   ASN E CA  1 
ATOM   4855 C  C   . ASN E 1 65  ? -64.484 87.798  4.094   1.00 59.31  ? 65   ASN E C   1 
ATOM   4856 O  O   . ASN E 1 65  ? -63.579 88.555  3.760   1.00 61.43  ? 65   ASN E O   1 
ATOM   4857 C  CB  . ASN E 1 65  ? -64.772 89.250  6.124   1.00 60.59  ? 65   ASN E CB  1 
ATOM   4858 C  CG  . ASN E 1 65  ? -65.389 90.412  5.353   1.00 65.88  ? 65   ASN E CG  1 
ATOM   4859 O  OD1 . ASN E 1 65  ? -66.283 90.226  4.518   1.00 64.99  ? 65   ASN E OD1 1 
ATOM   4860 N  ND2 . ASN E 1 65  ? -64.914 91.623  5.638   1.00 59.64  ? 65   ASN E ND2 1 
ATOM   4861 N  N   . PRO E 1 66  ? -65.004 86.889  3.254   1.00 59.79  ? 66   PRO E N   1 
ATOM   4862 C  CA  . PRO E 1 66  ? -64.485 86.627  1.904   1.00 63.30  ? 66   PRO E CA  1 
ATOM   4863 C  C   . PRO E 1 66  ? -64.848 87.716  0.893   1.00 68.97  ? 66   PRO E C   1 
ATOM   4864 O  O   . PRO E 1 66  ? -64.389 87.674  -0.249  1.00 67.72  ? 66   PRO E O   1 
ATOM   4865 C  CB  . PRO E 1 66  ? -65.195 85.323  1.494   1.00 61.28  ? 66   PRO E CB  1 
ATOM   4866 C  CG  . PRO E 1 66  ? -65.937 84.849  2.715   1.00 59.86  ? 66   PRO E CG  1 
ATOM   4867 C  CD  . PRO E 1 66  ? -66.178 86.056  3.554   1.00 58.96  ? 66   PRO E CD  1 
ATOM   4868 N  N   . HIS E 1 67  ? -65.680 88.667  1.299   1.00 69.18  ? 67   HIS E N   1 
ATOM   4869 C  CA  . HIS E 1 67  ? -66.132 89.707  0.381   1.00 73.33  ? 67   HIS E CA  1 
ATOM   4870 C  C   . HIS E 1 67  ? -65.844 91.092  0.934   1.00 71.46  ? 67   HIS E C   1 
ATOM   4871 O  O   . HIS E 1 67  ? -66.529 92.059  0.595   1.00 74.02  ? 67   HIS E O   1 
ATOM   4872 C  CB  . HIS E 1 67  ? -67.624 89.545  0.072   1.00 75.32  ? 67   HIS E CB  1 
ATOM   4873 C  CG  . HIS E 1 67  ? -67.966 88.235  -0.570  1.00 72.86  ? 67   HIS E CG  1 
ATOM   4874 N  ND1 . HIS E 1 67  ? -67.396 87.816  -1.754  1.00 73.61  ? 67   HIS E ND1 1 
ATOM   4875 C  CD2 . HIS E 1 67  ? -68.822 87.255  -0.196  1.00 67.20  ? 67   HIS E CD2 1 
ATOM   4876 C  CE1 . HIS E 1 67  ? -67.885 86.633  -2.080  1.00 79.23  ? 67   HIS E CE1 1 
ATOM   4877 N  NE2 . HIS E 1 67  ? -68.754 86.271  -1.152  1.00 79.09  ? 67   HIS E NE2 1 
ATOM   4878 N  N   . SER E 1 68  ? -64.823 91.160  1.788   1.00 68.79  ? 68   SER E N   1 
ATOM   4879 C  CA  . SER E 1 68  ? -64.345 92.403  2.404   1.00 68.67  ? 68   SER E CA  1 
ATOM   4880 C  C   . SER E 1 68  ? -65.399 93.492  2.590   1.00 71.51  ? 68   SER E C   1 
ATOM   4881 O  O   . SER E 1 68  ? -65.231 94.616  2.117   1.00 74.14  ? 68   SER E O   1 
ATOM   4882 C  CB  . SER E 1 68  ? -63.140 92.959  1.642   1.00 67.51  ? 68   SER E CB  1 
ATOM   4883 O  OG  . SER E 1 68  ? -62.009 92.126  1.813   1.00 65.22  ? 68   SER E OG  1 
ATOM   4884 N  N   . LYS E 1 69  ? -66.484 93.148  3.275   1.00 72.46  ? 69   LYS E N   1 
ATOM   4885 C  CA  . LYS E 1 69  ? -67.468 94.131  3.687   1.00 67.37  ? 69   LYS E CA  1 
ATOM   4886 C  C   . LYS E 1 69  ? -67.103 94.576  5.100   1.00 67.84  ? 69   LYS E C   1 
ATOM   4887 O  O   . LYS E 1 69  ? -66.111 94.116  5.657   1.00 64.68  ? 69   LYS E O   1 
ATOM   4888 C  CB  . LYS E 1 69  ? -68.884 93.554  3.607   1.00 66.34  ? 69   LYS E CB  1 
ATOM   4889 C  CG  . LYS E 1 69  ? -69.226 92.984  2.221   1.00 74.36  ? 69   LYS E CG  1 
ATOM   4890 C  CD  . LYS E 1 69  ? -70.722 93.096  1.871   1.00 78.96  ? 69   LYS E CD  1 
ATOM   4891 C  CE  . LYS E 1 69  ? -71.619 92.278  2.811   1.00 74.56  ? 69   LYS E CE  1 
ATOM   4892 N  NZ  . LYS E 1 69  ? -72.416 91.229  2.083   1.00 73.56  ? 69   LYS E NZ  1 
ATOM   4893 N  N   . LYS E 1 70  ? -67.878 95.492  5.667   1.00 68.93  ? 70   LYS E N   1 
ATOM   4894 C  CA  . LYS E 1 70  ? -67.589 95.997  6.999   1.00 66.50  ? 70   LYS E CA  1 
ATOM   4895 C  C   . LYS E 1 70  ? -68.474 95.274  7.999   1.00 61.84  ? 70   LYS E C   1 
ATOM   4896 O  O   . LYS E 1 70  ? -69.434 94.622  7.615   1.00 65.79  ? 70   LYS E O   1 
ATOM   4897 C  CB  . LYS E 1 70  ? -67.818 97.509  7.059   1.00 71.15  ? 70   LYS E CB  1 
ATOM   4898 C  CG  . LYS E 1 70  ? -66.812 98.324  6.261   1.00 73.05  ? 70   LYS E CG  1 
ATOM   4899 C  CD  . LYS E 1 70  ? -67.140 99.818  6.300   1.00 79.15  ? 70   LYS E CD  1 
ATOM   4900 C  CE  . LYS E 1 70  ? -65.994 100.688 5.750   1.00 84.94  ? 70   LYS E CE  1 
ATOM   4901 N  NZ  . LYS E 1 70  ? -64.745 100.660 6.589   1.00 78.23  ? 70   LYS E NZ  1 
ATOM   4902 N  N   . HIS E 1 71  ? -68.154 95.393  9.280   1.00 61.69  ? 71   HIS E N   1 
ATOM   4903 C  CA  . HIS E 1 71  ? -68.836 94.612  10.310  1.00 65.03  ? 71   HIS E CA  1 
ATOM   4904 C  C   . HIS E 1 71  ? -70.334 94.895  10.369  1.00 66.98  ? 71   HIS E C   1 
ATOM   4905 O  O   . HIS E 1 71  ? -70.759 96.048  10.440  1.00 70.93  ? 71   HIS E O   1 
ATOM   4906 C  CB  . HIS E 1 71  ? -68.186 94.841  11.683  1.00 62.88  ? 71   HIS E CB  1 
ATOM   4907 C  CG  . HIS E 1 71  ? -68.903 94.172  12.817  1.00 61.64  ? 71   HIS E CG  1 
ATOM   4908 N  ND1 . HIS E 1 71  ? -68.798 92.822  13.075  1.00 63.75  ? 71   HIS E ND1 1 
ATOM   4909 C  CD2 . HIS E 1 71  ? -69.727 94.671  13.767  1.00 66.15  ? 71   HIS E CD2 1 
ATOM   4910 C  CE1 . HIS E 1 71  ? -69.530 92.518  14.131  1.00 63.81  ? 71   HIS E CE1 1 
ATOM   4911 N  NE2 . HIS E 1 71  ? -70.105 93.623  14.570  1.00 64.42  ? 71   HIS E NE2 1 
ATOM   4912 N  N   . GLY E 1 72  ? -71.134 93.837  10.346  1.00 65.00  ? 72   GLY E N   1 
ATOM   4913 C  CA  . GLY E 1 72  ? -72.569 93.991  10.472  1.00 68.57  ? 72   GLY E CA  1 
ATOM   4914 C  C   . GLY E 1 72  ? -73.176 93.064  11.504  1.00 68.40  ? 72   GLY E C   1 
ATOM   4915 O  O   . GLY E 1 72  ? -72.566 92.068  11.898  1.00 67.87  ? 72   GLY E O   1 
ATOM   4916 N  N   . GLY E 1 73  ? -74.374 93.410  11.964  1.00 66.31  ? 73   GLY E N   1 
ATOM   4917 C  CA  . GLY E 1 73  ? -75.200 92.472  12.695  1.00 62.73  ? 73   GLY E CA  1 
ATOM   4918 C  C   . GLY E 1 73  ? -75.696 91.485  11.658  1.00 63.71  ? 73   GLY E C   1 
ATOM   4919 O  O   . GLY E 1 73  ? -75.620 91.765  10.460  1.00 62.41  ? 73   GLY E O   1 
ATOM   4920 N  N   . PRO E 1 74  ? -76.202 90.323  12.101  1.00 64.88  ? 74   PRO E N   1 
ATOM   4921 C  CA  . PRO E 1 74  ? -76.586 89.263  11.158  1.00 62.26  ? 74   PRO E CA  1 
ATOM   4922 C  C   . PRO E 1 74  ? -77.601 89.776  10.146  1.00 66.52  ? 74   PRO E C   1 
ATOM   4923 O  O   . PRO E 1 74  ? -77.569 89.388  8.968   1.00 64.54  ? 74   PRO E O   1 
ATOM   4924 C  CB  . PRO E 1 74  ? -77.247 88.210  12.053  1.00 59.69  ? 74   PRO E CB  1 
ATOM   4925 C  CG  . PRO E 1 74  ? -76.791 88.517  13.441  1.00 63.89  ? 74   PRO E CG  1 
ATOM   4926 C  CD  . PRO E 1 74  ? -76.546 89.993  13.495  1.00 61.15  ? 74   PRO E CD  1 
ATOM   4927 N  N   . ALA E 1 75  ? -78.485 90.654  10.621  1.00 68.28  ? 75   ALA E N   1 
ATOM   4928 C  CA  . ALA E 1 75  ? -79.597 91.183  9.831   1.00 69.63  ? 75   ALA E CA  1 
ATOM   4929 C  C   . ALA E 1 75  ? -79.146 92.132  8.725   1.00 70.05  ? 75   ALA E C   1 
ATOM   4930 O  O   . ALA E 1 75  ? -79.693 92.109  7.622   1.00 74.98  ? 75   ALA E O   1 
ATOM   4931 C  CB  . ALA E 1 75  ? -80.605 91.872  10.740  1.00 65.08  ? 75   ALA E CB  1 
ATOM   4932 N  N   . ASP E 1 76  ? -78.141 92.950  9.025   1.00 68.51  ? 76   ASP E N   1 
ATOM   4933 C  CA  . ASP E 1 76  ? -77.647 93.972  8.101   1.00 70.88  ? 76   ASP E CA  1 
ATOM   4934 C  C   . ASP E 1 76  ? -77.432 93.504  6.660   1.00 70.04  ? 76   ASP E C   1 
ATOM   4935 O  O   . ASP E 1 76  ? -77.415 92.311  6.364   1.00 71.43  ? 76   ASP E O   1 
ATOM   4936 C  CB  . ASP E 1 76  ? -76.352 94.593  8.639   1.00 72.89  ? 76   ASP E CB  1 
ATOM   4937 C  CG  . ASP E 1 76  ? -76.583 95.465  9.865   1.00 75.91  ? 76   ASP E CG  1 
ATOM   4938 O  OD1 . ASP E 1 76  ? -77.702 95.999  10.033  1.00 78.59  ? 76   ASP E OD1 1 
ATOM   4939 O  OD2 . ASP E 1 76  ? -75.635 95.623  10.662  1.00 82.16  ? 76   ASP E OD2 1 
ATOM   4940 N  N   . GLU E 1 77  ? -77.278 94.470  5.765   1.00 72.89  ? 77   GLU E N   1 
ATOM   4941 C  CA  . GLU E 1 77  ? -76.960 94.182  4.380   1.00 73.84  ? 77   GLU E CA  1 
ATOM   4942 C  C   . GLU E 1 77  ? -75.445 94.095  4.233   1.00 75.45  ? 77   GLU E C   1 
ATOM   4943 O  O   . GLU E 1 77  ? -74.919 93.243  3.508   1.00 74.05  ? 77   GLU E O   1 
ATOM   4944 C  CB  . GLU E 1 77  ? -77.499 95.289  3.476   1.00 71.90  ? 77   GLU E CB  1 
ATOM   4945 C  CG  . GLU E 1 77  ? -78.419 94.800  2.368   1.00 69.35  ? 77   GLU E CG  1 
ATOM   4946 C  CD  . GLU E 1 77  ? -77.955 93.489  1.737   1.00 72.14  ? 77   GLU E CD  1 
ATOM   4947 O  OE1 . GLU E 1 77  ? -78.820 92.766  1.195   1.00 68.16  ? 77   GLU E OE1 1 
ATOM   4948 O  OE2 . GLU E 1 77  ? -76.741 93.172  1.781   1.00 76.59  ? 77   GLU E OE2 1 
ATOM   4949 N  N   . GLU E 1 78  ? -74.758 94.998  4.928   1.00 71.37  ? 78   GLU E N   1 
ATOM   4950 C  CA  . GLU E 1 78  ? -73.304 95.049  4.935   1.00 72.61  ? 78   GLU E CA  1 
ATOM   4951 C  C   . GLU E 1 78  ? -72.751 94.363  6.189   1.00 73.38  ? 78   GLU E C   1 
ATOM   4952 O  O   . GLU E 1 78  ? -72.822 94.910  7.297   1.00 73.78  ? 78   GLU E O   1 
ATOM   4953 C  CB  . GLU E 1 78  ? -72.842 96.505  4.887   1.00 71.23  ? 78   GLU E CB  1 
ATOM   4954 C  CG  . GLU E 1 78  ? -71.346 96.696  4.696   1.00 73.38  ? 78   GLU E CG  1 
ATOM   4955 C  CD  . GLU E 1 78  ? -70.900 96.500  3.254   1.00 77.42  ? 78   GLU E CD  1 
ATOM   4956 O  OE1 . GLU E 1 78  ? -71.743 96.105  2.412   1.00 78.09  ? 78   GLU E OE1 1 
ATOM   4957 O  OE2 . GLU E 1 78  ? -69.702 96.741  2.967   1.00 73.60  ? 78   GLU E OE2 1 
ATOM   4958 N  N   . ARG E 1 79  ? -72.213 93.158  6.013   1.00 70.85  ? 79   ARG E N   1 
ATOM   4959 C  CA  . ARG E 1 79  ? -71.658 92.398  7.129   1.00 64.52  ? 79   ARG E CA  1 
ATOM   4960 C  C   . ARG E 1 79  ? -70.572 91.441  6.670   1.00 60.42  ? 79   ARG E C   1 
ATOM   4961 O  O   . ARG E 1 79  ? -70.443 91.148  5.481   1.00 64.08  ? 79   ARG E O   1 
ATOM   4962 C  CB  . ARG E 1 79  ? -72.753 91.600  7.847   1.00 65.42  ? 79   ARG E CB  1 
ATOM   4963 C  CG  . ARG E 1 79  ? -73.508 90.629  6.950   1.00 58.97  ? 79   ARG E CG  1 
ATOM   4964 C  CD  . ARG E 1 79  ? -74.369 89.660  7.751   1.00 59.73  ? 79   ARG E CD  1 
ATOM   4965 N  NE  . ARG E 1 79  ? -73.730 88.349  7.869   1.00 62.30  ? 79   ARG E NE  1 
ATOM   4966 C  CZ  . ARG E 1 79  ? -74.318 87.261  8.358   1.00 59.87  ? 79   ARG E CZ  1 
ATOM   4967 N  NH1 . ARG E 1 79  ? -75.574 87.309  8.785   1.00 62.85  ? 79   ARG E NH1 1 
ATOM   4968 N  NH2 . ARG E 1 79  ? -73.650 86.119  8.417   1.00 54.82  ? 79   ARG E NH2 1 
ATOM   4969 N  N   . HIS E 1 80  ? -69.787 90.955  7.623   1.00 58.96  ? 80   HIS E N   1 
ATOM   4970 C  CA  . HIS E 1 80  ? -68.894 89.848  7.351   1.00 55.46  ? 80   HIS E CA  1 
ATOM   4971 C  C   . HIS E 1 80  ? -69.728 88.595  7.387   1.00 53.43  ? 80   HIS E C   1 
ATOM   4972 O  O   . HIS E 1 80  ? -70.689 88.518  8.144   1.00 55.67  ? 80   HIS E O   1 
ATOM   4973 C  CB  . HIS E 1 80  ? -67.845 89.741  8.434   1.00 56.35  ? 80   HIS E CB  1 
ATOM   4974 C  CG  . HIS E 1 80  ? -67.107 91.007  8.680   1.00 56.08  ? 80   HIS E CG  1 
ATOM   4975 N  ND1 . HIS E 1 80  ? -67.113 91.643  9.899   1.00 54.86  ? 80   HIS E ND1 1 
ATOM   4976 C  CD2 . HIS E 1 80  ? -66.340 91.762  7.863   1.00 59.21  ? 80   HIS E CD2 1 
ATOM   4977 C  CE1 . HIS E 1 80  ? -66.371 92.731  9.830   1.00 60.13  ? 80   HIS E CE1 1 
ATOM   4978 N  NE2 . HIS E 1 80  ? -65.895 92.831  8.602   1.00 62.95  ? 80   HIS E NE2 1 
ATOM   4979 N  N   . VAL E 1 81  ? -69.366 87.604  6.585   1.00 56.76  ? 81   VAL E N   1 
ATOM   4980 C  CA  . VAL E 1 81  ? -70.022 86.307  6.699   1.00 55.44  ? 81   VAL E CA  1 
ATOM   4981 C  C   . VAL E 1 81  ? -70.082 85.832  8.166   1.00 54.22  ? 81   VAL E C   1 
ATOM   4982 O  O   . VAL E 1 81  ? -71.140 85.438  8.649   1.00 56.85  ? 81   VAL E O   1 
ATOM   4983 C  CB  . VAL E 1 81  ? -69.361 85.248  5.804   1.00 52.45  ? 81   VAL E CB  1 
ATOM   4984 C  CG1 . VAL E 1 81  ? -69.917 83.863  6.118   1.00 56.89  ? 81   VAL E CG1 1 
ATOM   4985 C  CG2 . VAL E 1 81  ? -69.558 85.595  4.333   1.00 53.61  ? 81   VAL E CG2 1 
ATOM   4986 N  N   . GLY E 1 82  ? -68.966 85.920  8.885   1.00 53.72  ? 82   GLY E N   1 
ATOM   4987 C  CA  . GLY E 1 82  ? -68.878 85.385  10.237  1.00 52.38  ? 82   GLY E CA  1 
ATOM   4988 C  C   . GLY E 1 82  ? -69.655 86.096  11.334  1.00 53.47  ? 82   GLY E C   1 
ATOM   4989 O  O   . GLY E 1 82  ? -69.476 85.796  12.519  1.00 48.32  ? 82   GLY E O   1 
ATOM   4990 N  N   . ASP E 1 83  ? -70.532 87.023  10.952  1.00 59.45  ? 83   ASP E N   1 
ATOM   4991 C  CA  . ASP E 1 83  ? -71.288 87.809  11.935  1.00 59.59  ? 83   ASP E CA  1 
ATOM   4992 C  C   . ASP E 1 83  ? -72.631 87.195  12.311  1.00 59.36  ? 83   ASP E C   1 
ATOM   4993 O  O   . ASP E 1 83  ? -73.545 87.112  11.487  1.00 59.09  ? 83   ASP E O   1 
ATOM   4994 C  CB  . ASP E 1 83  ? -71.476 89.239  11.445  1.00 59.38  ? 83   ASP E CB  1 
ATOM   4995 C  CG  . ASP E 1 83  ? -70.185 90.016  11.465  1.00 61.45  ? 83   ASP E CG  1 
ATOM   4996 O  OD1 . ASP E 1 83  ? -69.884 90.702  10.465  1.00 61.60  ? 83   ASP E OD1 1 
ATOM   4997 O  OD2 . ASP E 1 83  ? -69.462 89.912  12.485  1.00 61.65  ? 83   ASP E OD2 1 
ATOM   4998 N  N   . LEU E 1 84  ? -72.740 86.771  13.563  1.00 53.51  ? 84   LEU E N   1 
ATOM   4999 C  CA  . LEU E 1 84  ? -73.957 86.150  14.057  1.00 56.23  ? 84   LEU E CA  1 
ATOM   5000 C  C   . LEU E 1 84  ? -74.543 87.000  15.176  1.00 56.01  ? 84   LEU E C   1 
ATOM   5001 O  O   . LEU E 1 84  ? -75.550 86.641  15.790  1.00 57.37  ? 84   LEU E O   1 
ATOM   5002 C  CB  . LEU E 1 84  ? -73.664 84.724  14.532  1.00 49.59  ? 84   LEU E CB  1 
ATOM   5003 C  CG  . LEU E 1 84  ? -72.936 83.852  13.502  1.00 52.47  ? 84   LEU E CG  1 
ATOM   5004 C  CD1 . LEU E 1 84  ? -72.643 82.476  14.074  1.00 55.18  ? 84   LEU E CD1 1 
ATOM   5005 C  CD2 . LEU E 1 84  ? -73.715 83.722  12.200  1.00 48.07  ? 84   LEU E CD2 1 
ATOM   5006 N  N   . GLY E 1 85  ? -73.894 88.134  15.429  1.00 60.45  ? 85   GLY E N   1 
ATOM   5007 C  CA  . GLY E 1 85  ? -74.396 89.132  16.358  1.00 58.77  ? 85   GLY E CA  1 
ATOM   5008 C  C   . GLY E 1 85  ? -74.189 88.815  17.828  1.00 62.12  ? 85   GLY E C   1 
ATOM   5009 O  O   . GLY E 1 85  ? -73.061 88.669  18.292  1.00 63.53  ? 85   GLY E O   1 
ATOM   5010 N  N   . ASN E 1 86  ? -75.277 88.710  18.579  1.00 58.40  ? 86   ASN E N   1 
ATOM   5011 C  CA  . ASN E 1 86  ? -75.139 88.560  20.015  1.00 62.32  ? 86   ASN E CA  1 
ATOM   5012 C  C   . ASN E 1 86  ? -75.759 87.302  20.591  1.00 60.51  ? 86   ASN E C   1 
ATOM   5013 O  O   . ASN E 1 86  ? -76.671 86.714  20.016  1.00 55.91  ? 86   ASN E O   1 
ATOM   5014 C  CB  . ASN E 1 86  ? -75.675 89.795  20.750  1.00 66.40  ? 86   ASN E CB  1 
ATOM   5015 C  CG  . ASN E 1 86  ? -74.644 90.897  20.859  1.00 66.10  ? 86   ASN E CG  1 
ATOM   5016 O  OD1 . ASN E 1 86  ? -74.018 91.078  21.904  1.00 64.80  ? 86   ASN E OD1 1 
ATOM   5017 N  ND2 . ASN E 1 86  ? -74.453 91.636  19.772  1.00 68.31  ? 86   ASN E ND2 1 
ATOM   5018 N  N   . VAL E 1 87  ? -75.232 86.916  21.747  1.00 63.19  ? 87   VAL E N   1 
ATOM   5019 C  CA  . VAL E 1 87  ? -75.718 85.786  22.524  1.00 67.75  ? 87   VAL E CA  1 
ATOM   5020 C  C   . VAL E 1 87  ? -75.937 86.264  23.960  1.00 65.72  ? 87   VAL E C   1 
ATOM   5021 O  O   . VAL E 1 87  ? -75.004 86.721  24.624  1.00 63.26  ? 87   VAL E O   1 
ATOM   5022 C  CB  . VAL E 1 87  ? -74.707 84.605  22.499  1.00 66.77  ? 87   VAL E CB  1 
ATOM   5023 C  CG1 . VAL E 1 87  ? -74.825 83.764  23.761  1.00 72.08  ? 87   VAL E CG1 1 
ATOM   5024 C  CG2 . VAL E 1 87  ? -74.887 83.747  21.238  1.00 55.59  ? 87   VAL E CG2 1 
ATOM   5025 N  N   . THR E 1 88  ? -77.174 86.169  24.433  1.00 68.30  ? 88   THR E N   1 
ATOM   5026 C  CA  . THR E 1 88  ? -77.525 86.734  25.733  1.00 69.41  ? 88   THR E CA  1 
ATOM   5027 C  C   . THR E 1 88  ? -77.343 85.739  26.873  1.00 67.61  ? 88   THR E C   1 
ATOM   5028 O  O   . THR E 1 88  ? -78.057 84.737  26.954  1.00 68.80  ? 88   THR E O   1 
ATOM   5029 C  CB  . THR E 1 88  ? -78.981 87.234  25.751  1.00 65.80  ? 88   THR E CB  1 
ATOM   5030 O  OG1 . THR E 1 88  ? -79.328 87.753  24.463  1.00 66.68  ? 88   THR E OG1 1 
ATOM   5031 C  CG2 . THR E 1 88  ? -79.159 88.312  26.800  1.00 67.79  ? 88   THR E CG2 1 
ATOM   5032 N  N   . ALA E 1 89  ? -76.387 86.021  27.750  1.00 66.08  ? 89   ALA E N   1 
ATOM   5033 C  CA  . ALA E 1 89  ? -76.219 85.237  28.967  1.00 74.10  ? 89   ALA E CA  1 
ATOM   5034 C  C   . ALA E 1 89  ? -77.247 85.688  29.997  1.00 75.92  ? 89   ALA E C   1 
ATOM   5035 O  O   . ALA E 1 89  ? -77.585 86.870  30.061  1.00 77.22  ? 89   ALA E O   1 
ATOM   5036 C  CB  . ALA E 1 89  ? -74.814 85.393  29.515  1.00 73.16  ? 89   ALA E CB  1 
ATOM   5037 N  N   . ASP E 1 90  ? -77.758 84.755  30.793  1.00 73.85  ? 90   ASP E N   1 
ATOM   5038 C  CA  . ASP E 1 90  ? -78.722 85.119  31.822  1.00 79.70  ? 90   ASP E CA  1 
ATOM   5039 C  C   . ASP E 1 90  ? -78.032 85.391  33.156  1.00 82.37  ? 90   ASP E C   1 
ATOM   5040 O  O   . ASP E 1 90  ? -76.809 85.496  33.226  1.00 82.66  ? 90   ASP E O   1 
ATOM   5041 C  CB  . ASP E 1 90  ? -79.828 84.063  31.964  1.00 80.64  ? 90   ASP E CB  1 
ATOM   5042 C  CG  . ASP E 1 90  ? -79.347 82.789  32.623  1.00 80.49  ? 90   ASP E CG  1 
ATOM   5043 O  OD1 . ASP E 1 90  ? -78.190 82.754  33.084  1.00 80.72  ? 90   ASP E OD1 1 
ATOM   5044 O  OD2 . ASP E 1 90  ? -80.132 81.820  32.681  1.00 80.87  ? 90   ASP E OD2 1 
ATOM   5045 N  N   . LYS E 1 91  ? -78.824 85.509  34.212  1.00 87.20  ? 91   LYS E N   1 
ATOM   5046 C  CA  . LYS E 1 91  ? -78.300 85.854  35.528  1.00 90.17  ? 91   LYS E CA  1 
ATOM   5047 C  C   . LYS E 1 91  ? -77.341 84.797  36.086  1.00 93.53  ? 91   LYS E C   1 
ATOM   5048 O  O   . LYS E 1 91  ? -76.569 85.072  37.011  1.00 92.32  ? 91   LYS E O   1 
ATOM   5049 C  CB  . LYS E 1 91  ? -79.459 86.085  36.497  1.00 92.17  ? 91   LYS E CB  1 
ATOM   5050 C  CG  . LYS E 1 91  ? -80.522 84.998  36.434  1.00 94.39  ? 91   LYS E CG  1 
ATOM   5051 C  CD  . LYS E 1 91  ? -81.658 85.277  37.401  1.00 94.07  ? 91   LYS E CD  1 
ATOM   5052 C  CE  . LYS E 1 91  ? -82.179 83.979  37.980  1.00 92.84  ? 91   LYS E CE  1 
ATOM   5053 N  NZ  . LYS E 1 91  ? -81.073 83.199  38.612  1.00 83.14  ? 91   LYS E NZ  1 
ATOM   5054 N  N   . ASP E 1 92  ? -77.387 83.594  35.517  1.00 89.60  ? 92   ASP E N   1 
ATOM   5055 C  CA  . ASP E 1 92  ? -76.564 82.484  35.991  1.00 87.62  ? 92   ASP E CA  1 
ATOM   5056 C  C   . ASP E 1 92  ? -75.272 82.345  35.185  1.00 86.34  ? 92   ASP E C   1 
ATOM   5057 O  O   . ASP E 1 92  ? -74.422 81.510  35.500  1.00 86.82  ? 92   ASP E O   1 
ATOM   5058 C  CB  . ASP E 1 92  ? -77.353 81.174  35.919  1.00 89.27  ? 92   ASP E CB  1 
ATOM   5059 C  CG  . ASP E 1 92  ? -78.760 81.311  36.464  1.00 92.16  ? 92   ASP E CG  1 
ATOM   5060 O  OD1 . ASP E 1 92  ? -78.928 82.004  37.490  1.00 91.84  ? 92   ASP E OD1 1 
ATOM   5061 O  OD2 . ASP E 1 92  ? -79.695 80.728  35.867  1.00 88.62  ? 92   ASP E OD2 1 
ATOM   5062 N  N   . GLY E 1 93  ? -75.128 83.159  34.143  1.00 81.76  ? 93   GLY E N   1 
ATOM   5063 C  CA  . GLY E 1 93  ? -73.998 83.040  33.236  1.00 81.01  ? 93   GLY E CA  1 
ATOM   5064 C  C   . GLY E 1 93  ? -74.272 82.096  32.071  1.00 80.96  ? 93   GLY E C   1 
ATOM   5065 O  O   . GLY E 1 93  ? -73.438 81.932  31.172  1.00 74.77  ? 93   GLY E O   1 
ATOM   5066 N  N   . VAL E 1 94  ? -75.448 81.474  32.086  1.00 79.48  ? 94   VAL E N   1 
ATOM   5067 C  CA  . VAL E 1 94  ? -75.853 80.581  31.008  1.00 75.64  ? 94   VAL E CA  1 
ATOM   5068 C  C   . VAL E 1 94  ? -76.527 81.336  29.864  1.00 73.80  ? 94   VAL E C   1 
ATOM   5069 O  O   . VAL E 1 94  ? -77.454 82.118  30.073  1.00 76.39  ? 94   VAL E O   1 
ATOM   5070 C  CB  . VAL E 1 94  ? -76.810 79.487  31.507  1.00 76.54  ? 94   VAL E CB  1 
ATOM   5071 C  CG1 . VAL E 1 94  ? -77.037 78.460  30.413  1.00 73.28  ? 94   VAL E CG1 1 
ATOM   5072 C  CG2 . VAL E 1 94  ? -76.256 78.826  32.760  1.00 76.81  ? 94   VAL E CG2 1 
ATOM   5073 N  N   . ALA E 1 95  ? -76.053 81.095  28.650  1.00 71.28  ? 95   ALA E N   1 
ATOM   5074 C  CA  . ALA E 1 95  ? -76.644 81.704  27.467  1.00 72.58  ? 95   ALA E CA  1 
ATOM   5075 C  C   . ALA E 1 95  ? -77.096 80.620  26.491  1.00 70.97  ? 95   ALA E C   1 
ATOM   5076 O  O   . ALA E 1 95  ? -76.264 79.968  25.865  1.00 74.81  ? 95   ALA E O   1 
ATOM   5077 C  CB  . ALA E 1 95  ? -75.638 82.627  26.801  1.00 68.91  ? 95   ALA E CB  1 
ATOM   5078 N  N   . ASP E 1 96  ? -78.404 80.416  26.367  1.00 68.02  ? 96   ASP E N   1 
ATOM   5079 C  CA  . ASP E 1 96  ? -78.920 79.375  25.478  1.00 72.76  ? 96   ASP E CA  1 
ATOM   5080 C  C   . ASP E 1 96  ? -78.894 79.843  24.027  1.00 70.21  ? 96   ASP E C   1 
ATOM   5081 O  O   . ASP E 1 96  ? -79.563 80.805  23.666  1.00 72.26  ? 96   ASP E O   1 
ATOM   5082 C  CB  . ASP E 1 96  ? -80.335 78.938  25.883  1.00 73.60  ? 96   ASP E CB  1 
ATOM   5083 C  CG  . ASP E 1 96  ? -80.337 77.969  27.057  1.00 77.67  ? 96   ASP E CG  1 
ATOM   5084 O  OD1 . ASP E 1 96  ? -79.418 77.122  27.130  1.00 78.95  ? 96   ASP E OD1 1 
ATOM   5085 O  OD2 . ASP E 1 96  ? -81.259 78.052  27.904  1.00 78.12  ? 96   ASP E OD2 1 
ATOM   5086 N  N   . VAL E 1 97  ? -78.122 79.151  23.197  1.00 66.35  ? 97   VAL E N   1 
ATOM   5087 C  CA  . VAL E 1 97  ? -77.873 79.615  21.843  1.00 65.15  ? 97   VAL E CA  1 
ATOM   5088 C  C   . VAL E 1 97  ? -78.754 78.933  20.825  1.00 62.87  ? 97   VAL E C   1 
ATOM   5089 O  O   . VAL E 1 97  ? -78.722 77.719  20.686  1.00 64.83  ? 97   VAL E O   1 
ATOM   5090 C  CB  . VAL E 1 97  ? -76.424 79.379  21.431  1.00 60.86  ? 97   VAL E CB  1 
ATOM   5091 C  CG1 . VAL E 1 97  ? -76.224 79.823  19.994  1.00 63.42  ? 97   VAL E CG1 1 
ATOM   5092 C  CG2 . VAL E 1 97  ? -75.487 80.124  22.371  1.00 61.79  ? 97   VAL E CG2 1 
ATOM   5093 N  N   . SER E 1 98  ? -79.535 79.733  20.109  1.00 63.99  ? 98   SER E N   1 
ATOM   5094 C  CA  . SER E 1 98  ? -80.367 79.234  19.023  1.00 62.11  ? 98   SER E CA  1 
ATOM   5095 C  C   . SER E 1 98  ? -80.375 80.244  17.895  1.00 53.55  ? 98   SER E C   1 
ATOM   5096 O  O   . SER E 1 98  ? -81.009 81.287  17.994  1.00 56.18  ? 98   SER E O   1 
ATOM   5097 C  CB  . SER E 1 98  ? -81.800 78.982  19.508  1.00 71.39  ? 98   SER E CB  1 
ATOM   5098 O  OG  . SER E 1 98  ? -82.698 78.835  18.413  1.00 68.54  ? 98   SER E OG  1 
ATOM   5099 N  N   . ILE E 1 99  ? -79.670 79.935  16.819  1.00 56.95  ? 99   ILE E N   1 
ATOM   5100 C  CA  . ILE E 1 99  ? -79.548 80.870  15.709  1.00 58.63  ? 99   ILE E CA  1 
ATOM   5101 C  C   . ILE E 1 99  ? -79.847 80.191  14.384  1.00 53.66  ? 99   ILE E C   1 
ATOM   5102 O  O   . ILE E 1 99  ? -79.672 78.987  14.232  1.00 58.75  ? 99   ILE E O   1 
ATOM   5103 C  CB  . ILE E 1 99  ? -78.136 81.497  15.659  1.00 52.88  ? 99   ILE E CB  1 
ATOM   5104 C  CG1 . ILE E 1 99  ? -77.888 82.349  16.902  1.00 51.15  ? 99   ILE E CG1 1 
ATOM   5105 C  CG2 . ILE E 1 99  ? -77.951 82.332  14.412  1.00 46.00  ? 99   ILE E CG2 1 
ATOM   5106 C  CD1 . ILE E 1 99  ? -76.525 83.010  16.921  1.00 54.19  ? 99   ILE E CD1 1 
ATOM   5107 N  N   . GLU E 1 100 ? -80.314 80.966  13.425  1.00 49.86  ? 100  GLU E N   1 
ATOM   5108 C  CA  . GLU E 1 100 ? -80.500 80.446  12.087  1.00 61.29  ? 100  GLU E CA  1 
ATOM   5109 C  C   . GLU E 1 100 ? -79.985 81.491  11.112  1.00 60.87  ? 100  GLU E C   1 
ATOM   5110 O  O   . GLU E 1 100 ? -80.394 82.654  11.166  1.00 61.78  ? 100  GLU E O   1 
ATOM   5111 C  CB  . GLU E 1 100 ? -81.972 80.135  11.826  1.00 59.83  ? 100  GLU E CB  1 
ATOM   5112 C  CG  . GLU E 1 100 ? -82.206 79.463  10.491  1.00 66.25  ? 100  GLU E CG  1 
ATOM   5113 C  CD  . GLU E 1 100 ? -83.642 79.002  10.310  1.00 78.40  ? 100  GLU E CD  1 
ATOM   5114 O  OE1 . GLU E 1 100 ? -84.487 79.371  11.156  1.00 84.39  ? 100  GLU E OE1 1 
ATOM   5115 O  OE2 . GLU E 1 100 ? -83.923 78.275  9.326   1.00 76.41  ? 100  GLU E OE2 1 
ATOM   5116 N  N   . ASP E 1 101 ? -79.077 81.083  10.235  1.00 55.77  ? 101  ASP E N   1 
ATOM   5117 C  CA  . ASP E 1 101 ? -78.385 82.031  9.374   1.00 58.37  ? 101  ASP E CA  1 
ATOM   5118 C  C   . ASP E 1 101 ? -78.226 81.461  7.967   1.00 60.66  ? 101  ASP E C   1 
ATOM   5119 O  O   . ASP E 1 101 ? -77.844 80.305  7.795   1.00 60.93  ? 101  ASP E O   1 
ATOM   5120 C  CB  . ASP E 1 101 ? -77.020 82.372  9.983   1.00 57.80  ? 101  ASP E CB  1 
ATOM   5121 C  CG  . ASP E 1 101 ? -76.499 83.737  9.550   1.00 57.09  ? 101  ASP E CG  1 
ATOM   5122 O  OD1 . ASP E 1 101 ? -76.918 84.760  10.138  1.00 56.51  ? 101  ASP E OD1 1 
ATOM   5123 O  OD2 . ASP E 1 101 ? -75.653 83.780  8.634   1.00 57.82  ? 101  ASP E OD2 1 
ATOM   5124 N  N   . SER E 1 102 ? -78.524 82.274  6.960   1.00 62.15  ? 102  SER E N   1 
ATOM   5125 C  CA  . SER E 1 102 ? -78.509 81.801  5.582   1.00 64.15  ? 102  SER E CA  1 
ATOM   5126 C  C   . SER E 1 102 ? -77.293 82.318  4.823   1.00 64.01  ? 102  SER E C   1 
ATOM   5127 O  O   . SER E 1 102 ? -77.083 81.971  3.657   1.00 70.53  ? 102  SER E O   1 
ATOM   5128 C  CB  . SER E 1 102 ? -79.814 82.180  4.861   1.00 64.22  ? 102  SER E CB  1 
ATOM   5129 O  OG  . SER E 1 102 ? -80.135 83.549  5.050   1.00 70.78  ? 102  SER E OG  1 
ATOM   5130 N  N   . VAL E 1 103 ? -76.495 83.143  5.494   1.00 63.47  ? 103  VAL E N   1 
ATOM   5131 C  CA  . VAL E 1 103 ? -75.258 83.678  4.917   1.00 66.12  ? 103  VAL E CA  1 
ATOM   5132 C  C   . VAL E 1 103 ? -74.081 82.707  5.108   1.00 66.80  ? 103  VAL E C   1 
ATOM   5133 O  O   . VAL E 1 103 ? -73.321 82.448  4.172   1.00 67.42  ? 103  VAL E O   1 
ATOM   5134 C  CB  . VAL E 1 103 ? -74.919 85.072  5.506   1.00 64.98  ? 103  VAL E CB  1 
ATOM   5135 C  CG1 . VAL E 1 103 ? -73.448 85.402  5.325   1.00 60.08  ? 103  VAL E CG1 1 
ATOM   5136 C  CG2 . VAL E 1 103 ? -75.792 86.140  4.869   1.00 66.43  ? 103  VAL E CG2 1 
ATOM   5137 N  N   . ILE E 1 104 ? -73.938 82.168  6.319   1.00 63.02  ? 104  ILE E N   1 
ATOM   5138 C  CA  . ILE E 1 104 ? -72.967 81.102  6.566   1.00 63.07  ? 104  ILE E CA  1 
ATOM   5139 C  C   . ILE E 1 104 ? -73.430 79.776  5.945   1.00 60.84  ? 104  ILE E C   1 
ATOM   5140 O  O   . ILE E 1 104 ? -74.565 79.648  5.489   1.00 60.73  ? 104  ILE E O   1 
ATOM   5141 C  CB  . ILE E 1 104 ? -72.688 80.898  8.080   1.00 56.54  ? 104  ILE E CB  1 
ATOM   5142 C  CG1 . ILE E 1 104 ? -73.849 80.151  8.747   1.00 53.27  ? 104  ILE E CG1 1 
ATOM   5143 C  CG2 . ILE E 1 104 ? -72.390 82.234  8.757   1.00 49.64  ? 104  ILE E CG2 1 
ATOM   5144 C  CD1 . ILE E 1 104 ? -73.671 79.957  10.233  1.00 51.74  ? 104  ILE E CD1 1 
ATOM   5145 N  N   . SER E 1 105 ? -72.546 78.788  5.943   1.00 58.23  ? 105  SER E N   1 
ATOM   5146 C  CA  . SER E 1 105 ? -72.810 77.537  5.256   1.00 55.92  ? 105  SER E CA  1 
ATOM   5147 C  C   . SER E 1 105 ? -71.873 76.433  5.752   1.00 58.71  ? 105  SER E C   1 
ATOM   5148 O  O   . SER E 1 105 ? -70.772 76.708  6.241   1.00 51.33  ? 105  SER E O   1 
ATOM   5149 C  CB  . SER E 1 105 ? -72.632 77.734  3.746   1.00 53.85  ? 105  SER E CB  1 
ATOM   5150 O  OG  . SER E 1 105 ? -72.785 76.510  3.054   1.00 54.53  ? 105  SER E OG  1 
ATOM   5151 N  N   . LEU E 1 106 ? -72.319 75.185  5.624   1.00 59.95  ? 106  LEU E N   1 
ATOM   5152 C  CA  . LEU E 1 106 ? -71.497 74.035  5.965   1.00 53.17  ? 106  LEU E CA  1 
ATOM   5153 C  C   . LEU E 1 106 ? -70.873 73.428  4.719   1.00 52.78  ? 106  LEU E C   1 
ATOM   5154 O  O   . LEU E 1 106 ? -70.539 72.247  4.699   1.00 56.62  ? 106  LEU E O   1 
ATOM   5155 C  CB  . LEU E 1 106 ? -72.316 72.995  6.715   1.00 51.86  ? 106  LEU E CB  1 
ATOM   5156 C  CG  . LEU E 1 106 ? -72.814 73.486  8.074   1.00 53.61  ? 106  LEU E CG  1 
ATOM   5157 C  CD1 . LEU E 1 106 ? -73.355 72.312  8.898   1.00 50.25  ? 106  LEU E CD1 1 
ATOM   5158 C  CD2 . LEU E 1 106 ? -71.702 74.204  8.828   1.00 44.21  ? 106  LEU E CD2 1 
ATOM   5159 N  N   . SER E 1 107 ? -70.728 74.251  3.685   1.00 52.39  ? 107  SER E N   1 
ATOM   5160 C  CA  . SER E 1 107 ? -70.013 73.886  2.459   1.00 60.36  ? 107  SER E CA  1 
ATOM   5161 C  C   . SER E 1 107 ? -70.115 75.030  1.446   1.00 56.25  ? 107  SER E C   1 
ATOM   5162 O  O   . SER E 1 107 ? -70.946 75.913  1.595   1.00 56.51  ? 107  SER E O   1 
ATOM   5163 C  CB  . SER E 1 107 ? -70.538 72.577  1.857   1.00 59.02  ? 107  SER E CB  1 
ATOM   5164 O  OG  . SER E 1 107 ? -71.505 72.826  0.852   1.00 61.09  ? 107  SER E OG  1 
ATOM   5165 N  N   . GLY E 1 108 ? -69.258 75.022  0.429   1.00 60.24  ? 108  GLY E N   1 
ATOM   5166 C  CA  . GLY E 1 108 ? -69.228 76.099  -0.549  1.00 63.14  ? 108  GLY E CA  1 
ATOM   5167 C  C   . GLY E 1 108 ? -68.375 77.283  -0.126  1.00 60.96  ? 108  GLY E C   1 
ATOM   5168 O  O   . GLY E 1 108 ? -67.718 77.237  0.904   1.00 60.68  ? 108  GLY E O   1 
ATOM   5169 N  N   . ASP E 1 109 ? -68.395 78.348  -0.921  1.00 64.34  ? 109  ASP E N   1 
ATOM   5170 C  CA  . ASP E 1 109 ? -67.556 79.523  -0.671  1.00 66.54  ? 109  ASP E CA  1 
ATOM   5171 C  C   . ASP E 1 109 ? -67.689 80.061  0.748   1.00 63.69  ? 109  ASP E C   1 
ATOM   5172 O  O   . ASP E 1 109 ? -66.746 80.629  1.293   1.00 64.46  ? 109  ASP E O   1 
ATOM   5173 C  CB  . ASP E 1 109 ? -67.862 80.645  -1.676  1.00 68.96  ? 109  ASP E CB  1 
ATOM   5174 C  CG  . ASP E 1 109 ? -67.434 80.295  -3.095  1.00 78.67  ? 109  ASP E CG  1 
ATOM   5175 O  OD1 . ASP E 1 109 ? -66.444 79.541  -3.247  1.00 77.66  ? 109  ASP E OD1 1 
ATOM   5176 O  OD2 . ASP E 1 109 ? -68.082 80.773  -4.056  1.00 82.30  ? 109  ASP E OD2 1 
ATOM   5177 N  N   . HIS E 1 110 ? -68.863 79.895  1.343   1.00 59.26  ? 110  HIS E N   1 
ATOM   5178 C  CA  . HIS E 1 110 ? -69.095 80.422  2.679   1.00 60.50  ? 110  HIS E CA  1 
ATOM   5179 C  C   . HIS E 1 110 ? -68.891 79.364  3.770   1.00 56.44  ? 110  HIS E C   1 
ATOM   5180 O  O   . HIS E 1 110 ? -69.240 79.586  4.931   1.00 54.07  ? 110  HIS E O   1 
ATOM   5181 C  CB  . HIS E 1 110 ? -70.491 81.050  2.769   1.00 63.08  ? 110  HIS E CB  1 
ATOM   5182 C  CG  . HIS E 1 110 ? -70.601 82.369  2.068   1.00 67.23  ? 110  HIS E CG  1 
ATOM   5183 N  ND1 . HIS E 1 110 ? -71.409 83.391  2.522   1.00 68.13  ? 110  HIS E ND1 1 
ATOM   5184 C  CD2 . HIS E 1 110 ? -69.988 82.841  0.957   1.00 67.12  ? 110  HIS E CD2 1 
ATOM   5185 C  CE1 . HIS E 1 110 ? -71.297 84.431  1.715   1.00 66.16  ? 110  HIS E CE1 1 
ATOM   5186 N  NE2 . HIS E 1 110 ? -70.442 84.123  0.756   1.00 71.69  ? 110  HIS E NE2 1 
ATOM   5187 N  N   . CYS E 1 111 ? -68.317 78.225  3.387   1.00 54.49  ? 111  CYS E N   1 
ATOM   5188 C  CA  . CYS E 1 111 ? -68.073 77.121  4.312   1.00 54.36  ? 111  CYS E CA  1 
ATOM   5189 C  C   . CYS E 1 111 ? -67.309 77.576  5.552   1.00 51.33  ? 111  CYS E C   1 
ATOM   5190 O  O   . CYS E 1 111 ? -66.252 78.203  5.448   1.00 51.83  ? 111  CYS E O   1 
ATOM   5191 C  CB  . CYS E 1 111 ? -67.303 76.001  3.612   1.00 53.90  ? 111  CYS E CB  1 
ATOM   5192 S  SG  . CYS E 1 111 ? -67.075 74.531  4.621   1.00 60.03  ? 111  CYS E SG  1 
ATOM   5193 N  N   . ILE E 1 112 ? -67.847 77.264  6.725   1.00 46.57  ? 112  ILE E N   1 
ATOM   5194 C  CA  . ILE E 1 112 ? -67.202 77.648  7.975   1.00 45.59  ? 112  ILE E CA  1 
ATOM   5195 C  C   . ILE E 1 112 ? -66.593 76.451  8.682   1.00 44.80  ? 112  ILE E C   1 
ATOM   5196 O  O   . ILE E 1 112 ? -66.142 76.561  9.824   1.00 42.21  ? 112  ILE E O   1 
ATOM   5197 C  CB  . ILE E 1 112 ? -68.176 78.326  8.948   1.00 44.68  ? 112  ILE E CB  1 
ATOM   5198 C  CG1 . ILE E 1 112 ? -69.279 77.356  9.369   1.00 43.59  ? 112  ILE E CG1 1 
ATOM   5199 C  CG2 . ILE E 1 112 ? -68.756 79.592  8.321   1.00 52.75  ? 112  ILE E CG2 1 
ATOM   5200 C  CD1 . ILE E 1 112 ? -70.151 77.871  10.497  1.00 45.90  ? 112  ILE E CD1 1 
ATOM   5201 N  N   . ILE E 1 113 ? -66.581 75.305  8.008   1.00 42.53  ? 113  ILE E N   1 
ATOM   5202 C  CA  . ILE E 1 113 ? -65.971 74.124  8.600   1.00 42.32  ? 113  ILE E CA  1 
ATOM   5203 C  C   . ILE E 1 113 ? -64.442 74.183  8.581   1.00 39.94  ? 113  ILE E C   1 
ATOM   5204 O  O   . ILE E 1 113 ? -63.816 74.357  7.531   1.00 42.88  ? 113  ILE E O   1 
ATOM   5205 C  CB  . ILE E 1 113 ? -66.521 72.838  8.001   1.00 36.29  ? 113  ILE E CB  1 
ATOM   5206 C  CG1 . ILE E 1 113 ? -67.891 72.568  8.636   1.00 48.02  ? 113  ILE E CG1 1 
ATOM   5207 C  CG2 . ILE E 1 113 ? -65.605 71.685  8.321   1.00 37.71  ? 113  ILE E CG2 1 
ATOM   5208 C  CD1 . ILE E 1 113 ? -68.762 71.544  7.919   1.00 46.83  ? 113  ILE E CD1 1 
ATOM   5209 N  N   . GLY E 1 114 ? -63.850 74.060  9.762   1.00 37.95  ? 114  GLY E N   1 
ATOM   5210 C  CA  . GLY E 1 114 ? -62.427 74.296  9.929   1.00 38.79  ? 114  GLY E CA  1 
ATOM   5211 C  C   . GLY E 1 114 ? -62.130 75.760  10.227  1.00 42.40  ? 114  GLY E C   1 
ATOM   5212 O  O   . GLY E 1 114 ? -60.978 76.201  10.180  1.00 42.06  ? 114  GLY E O   1 
ATOM   5213 N  N   . ARG E 1 115 ? -63.175 76.529  10.512  1.00 41.57  ? 115  ARG E N   1 
ATOM   5214 C  CA  . ARG E 1 115 ? -62.986 77.905  10.953  1.00 43.69  ? 115  ARG E CA  1 
ATOM   5215 C  C   . ARG E 1 115 ? -63.318 78.001  12.430  1.00 41.86  ? 115  ARG E C   1 
ATOM   5216 O  O   . ARG E 1 115 ? -63.752 77.024  13.032  1.00 44.78  ? 115  ARG E O   1 
ATOM   5217 C  CB  . ARG E 1 115 ? -63.787 78.881  10.091  1.00 40.74  ? 115  ARG E CB  1 
ATOM   5218 C  CG  . ARG E 1 115 ? -63.318 78.842  8.654   1.00 41.69  ? 115  ARG E CG  1 
ATOM   5219 C  CD  . ARG E 1 115 ? -63.938 79.909  7.771   1.00 44.58  ? 115  ARG E CD  1 
ATOM   5220 N  NE  . ARG E 1 115 ? -63.759 79.561  6.360   1.00 39.36  ? 115  ARG E NE  1 
ATOM   5221 C  CZ  . ARG E 1 115 ? -62.743 79.970  5.603   1.00 44.67  ? 115  ARG E CZ  1 
ATOM   5222 N  NH1 . ARG E 1 115 ? -61.809 80.767  6.108   1.00 46.32  ? 115  ARG E NH1 1 
ATOM   5223 N  NH2 . ARG E 1 115 ? -62.663 79.595  4.331   1.00 42.53  ? 115  ARG E NH2 1 
ATOM   5224 N  N   . THR E 1 116 ? -63.089 79.158  13.027  1.00 43.49  ? 116  THR E N   1 
ATOM   5225 C  CA  . THR E 1 116 ? -63.142 79.249  14.479  1.00 43.28  ? 116  THR E CA  1 
ATOM   5226 C  C   . THR E 1 116 ? -64.318 80.071  14.954  1.00 45.69  ? 116  THR E C   1 
ATOM   5227 O  O   . THR E 1 116 ? -64.442 81.248  14.615  1.00 50.48  ? 116  THR E O   1 
ATOM   5228 C  CB  . THR E 1 116 ? -61.851 79.887  15.061  1.00 47.23  ? 116  THR E CB  1 
ATOM   5229 O  OG1 . THR E 1 116 ? -60.705 79.118  14.678  1.00 45.69  ? 116  THR E OG1 1 
ATOM   5230 C  CG2 . THR E 1 116 ? -61.930 79.983  16.600  1.00 43.34  ? 116  THR E CG2 1 
ATOM   5231 N  N   . LEU E 1 117 ? -65.167 79.453  15.758  1.00 43.69  ? 117  LEU E N   1 
ATOM   5232 C  CA  . LEU E 1 117 ? -66.268 80.153  16.392  1.00 43.65  ? 117  LEU E CA  1 
ATOM   5233 C  C   . LEU E 1 117 ? -65.773 80.862  17.658  1.00 49.38  ? 117  LEU E C   1 
ATOM   5234 O  O   . LEU E 1 117 ? -65.075 80.260  18.483  1.00 45.21  ? 117  LEU E O   1 
ATOM   5235 C  CB  . LEU E 1 117 ? -67.366 79.155  16.749  1.00 44.53  ? 117  LEU E CB  1 
ATOM   5236 C  CG  . LEU E 1 117 ? -68.574 79.726  17.480  1.00 44.48  ? 117  LEU E CG  1 
ATOM   5237 C  CD1 . LEU E 1 117 ? -69.347 80.588  16.515  1.00 47.11  ? 117  LEU E CD1 1 
ATOM   5238 C  CD2 . LEU E 1 117 ? -69.437 78.612  18.045  1.00 45.25  ? 117  LEU E CD2 1 
ATOM   5239 N  N   . VAL E 1 118 ? -66.134 82.137  17.818  1.00 50.80  ? 118  VAL E N   1 
ATOM   5240 C  CA  . VAL E 1 118 ? -65.721 82.892  19.006  1.00 50.75  ? 118  VAL E CA  1 
ATOM   5241 C  C   . VAL E 1 118 ? -66.859 83.643  19.709  1.00 53.28  ? 118  VAL E C   1 
ATOM   5242 O  O   . VAL E 1 118 ? -67.632 84.362  19.073  1.00 56.18  ? 118  VAL E O   1 
ATOM   5243 C  CB  . VAL E 1 118 ? -64.575 83.892  18.681  1.00 52.74  ? 118  VAL E CB  1 
ATOM   5244 C  CG1 . VAL E 1 118 ? -64.011 84.511  19.968  1.00 50.17  ? 118  VAL E CG1 1 
ATOM   5245 C  CG2 . VAL E 1 118 ? -63.471 83.205  17.886  1.00 47.50  ? 118  VAL E CG2 1 
ATOM   5246 N  N   . VAL E 1 119 ? -66.946 83.456  21.026  1.00 52.14  ? 119  VAL E N   1 
ATOM   5247 C  CA  . VAL E 1 119 ? -67.784 84.269  21.901  1.00 51.11  ? 119  VAL E CA  1 
ATOM   5248 C  C   . VAL E 1 119 ? -66.889 85.355  22.518  1.00 59.28  ? 119  VAL E C   1 
ATOM   5249 O  O   . VAL E 1 119 ? -65.793 85.069  23.008  1.00 59.77  ? 119  VAL E O   1 
ATOM   5250 C  CB  . VAL E 1 119 ? -68.475 83.405  23.010  1.00 56.89  ? 119  VAL E CB  1 
ATOM   5251 C  CG1 . VAL E 1 119 ? -67.447 82.767  23.952  1.00 54.38  ? 119  VAL E CG1 1 
ATOM   5252 C  CG2 . VAL E 1 119 ? -69.482 84.220  23.799  1.00 49.59  ? 119  VAL E CG2 1 
ATOM   5253 N  N   . HIS E 1 120 ? -67.334 86.607  22.472  1.00 61.81  ? 120  HIS E N   1 
ATOM   5254 C  CA  . HIS E 1 120 ? -66.488 87.715  22.906  1.00 60.14  ? 120  HIS E CA  1 
ATOM   5255 C  C   . HIS E 1 120 ? -66.843 88.214  24.304  1.00 62.21  ? 120  HIS E C   1 
ATOM   5256 O  O   . HIS E 1 120 ? -67.793 87.741  24.924  1.00 64.10  ? 120  HIS E O   1 
ATOM   5257 C  CB  . HIS E 1 120 ? -66.520 88.858  21.888  1.00 59.95  ? 120  HIS E CB  1 
ATOM   5258 C  CG  . HIS E 1 120 ? -65.829 88.542  20.595  1.00 58.67  ? 120  HIS E CG  1 
ATOM   5259 N  ND1 . HIS E 1 120 ? -64.568 89.006  20.293  1.00 60.03  ? 120  HIS E ND1 1 
ATOM   5260 C  CD2 . HIS E 1 120 ? -66.226 87.816  19.522  1.00 58.73  ? 120  HIS E CD2 1 
ATOM   5261 C  CE1 . HIS E 1 120 ? -64.217 88.580  19.092  1.00 56.30  ? 120  HIS E CE1 1 
ATOM   5262 N  NE2 . HIS E 1 120 ? -65.207 87.858  18.600  1.00 53.57  ? 120  HIS E NE2 1 
ATOM   5263 N  N   . GLU E 1 121 ? -66.059 89.168  24.792  1.00 68.34  ? 121  GLU E N   1 
ATOM   5264 C  CA  . GLU E 1 121 ? -66.173 89.655  26.167  1.00 70.38  ? 121  GLU E CA  1 
ATOM   5265 C  C   . GLU E 1 121 ? -67.354 90.605  26.351  1.00 71.10  ? 121  GLU E C   1 
ATOM   5266 O  O   . GLU E 1 121 ? -68.016 90.600  27.397  1.00 67.09  ? 121  GLU E O   1 
ATOM   5267 C  CB  . GLU E 1 121 ? -64.880 90.370  26.562  1.00 73.14  ? 121  GLU E CB  1 
ATOM   5268 C  CG  . GLU E 1 121 ? -64.804 90.796  28.020  1.00 74.87  ? 121  GLU E CG  1 
ATOM   5269 C  CD  . GLU E 1 121 ? -63.847 91.958  28.222  1.00 70.82  ? 121  GLU E CD  1 
ATOM   5270 O  OE1 . GLU E 1 121 ? -63.363 92.519  27.210  1.00 69.15  ? 121  GLU E OE1 1 
ATOM   5271 O  OE2 . GLU E 1 121 ? -63.592 92.316  29.390  1.00 67.53  ? 121  GLU E OE2 1 
ATOM   5272 N  N   . LYS E 1 122 ? -67.603 91.419  25.327  1.00 68.59  ? 122  LYS E N   1 
ATOM   5273 C  CA  . LYS E 1 122 ? -68.661 92.420  25.368  1.00 69.82  ? 122  LYS E CA  1 
ATOM   5274 C  C   . LYS E 1 122 ? -69.692 92.195  24.257  1.00 70.94  ? 122  LYS E C   1 
ATOM   5275 O  O   . LYS E 1 122 ? -69.415 91.518  23.256  1.00 68.60  ? 122  LYS E O   1 
ATOM   5276 C  CB  . LYS E 1 122 ? -68.057 93.829  25.256  1.00 66.96  ? 122  LYS E CB  1 
ATOM   5277 C  CG  . LYS E 1 122 ? -67.213 94.244  26.452  1.00 66.86  ? 122  LYS E CG  1 
ATOM   5278 C  CD  . LYS E 1 122 ? -66.598 95.625  26.259  1.00 70.96  ? 122  LYS E CD  1 
ATOM   5279 C  CE  . LYS E 1 122 ? -65.522 95.627  25.179  1.00 68.67  ? 122  LYS E CE  1 
ATOM   5280 N  NZ  . LYS E 1 122 ? -64.867 96.963  25.038  1.00 71.09  ? 122  LYS E NZ  1 
ATOM   5281 N  N   . ALA E 1 123 ? -70.883 92.759  24.443  1.00 65.57  ? 123  ALA E N   1 
ATOM   5282 C  CA  . ALA E 1 123 ? -71.890 92.769  23.392  1.00 62.47  ? 123  ALA E CA  1 
ATOM   5283 C  C   . ALA E 1 123 ? -71.349 93.385  22.094  1.00 64.88  ? 123  ALA E C   1 
ATOM   5284 O  O   . ALA E 1 123 ? -70.434 94.209  22.099  1.00 65.39  ? 123  ALA E O   1 
ATOM   5285 C  CB  . ALA E 1 123 ? -73.124 93.504  23.858  1.00 60.93  ? 123  ALA E CB  1 
ATOM   5286 N  N   . ASP E 1 124 ? -71.924 92.962  20.979  1.00 65.15  ? 124  ASP E N   1 
ATOM   5287 C  CA  . ASP E 1 124 ? -71.516 93.419  19.660  1.00 66.53  ? 124  ASP E CA  1 
ATOM   5288 C  C   . ASP E 1 124 ? -72.503 94.485  19.172  1.00 71.86  ? 124  ASP E C   1 
ATOM   5289 O  O   . ASP E 1 124 ? -73.709 94.243  19.118  1.00 74.56  ? 124  ASP E O   1 
ATOM   5290 C  CB  . ASP E 1 124 ? -71.491 92.214  18.711  1.00 61.31  ? 124  ASP E CB  1 
ATOM   5291 C  CG  . ASP E 1 124 ? -71.317 92.601  17.267  1.00 64.08  ? 124  ASP E CG  1 
ATOM   5292 O  OD1 . ASP E 1 124 ? -71.018 93.783  16.995  1.00 68.01  ? 124  ASP E OD1 1 
ATOM   5293 O  OD2 . ASP E 1 124 ? -71.476 91.712  16.399  1.00 64.66  ? 124  ASP E OD2 1 
ATOM   5294 N  N   . ASP E 1 125 ? -72.003 95.664  18.818  1.00 69.89  ? 125  ASP E N   1 
ATOM   5295 C  CA  . ASP E 1 125 ? -72.886 96.745  18.387  1.00 67.77  ? 125  ASP E CA  1 
ATOM   5296 C  C   . ASP E 1 125 ? -73.317 96.639  16.919  1.00 70.61  ? 125  ASP E C   1 
ATOM   5297 O  O   . ASP E 1 125 ? -73.844 97.591  16.347  1.00 74.70  ? 125  ASP E O   1 
ATOM   5298 C  CB  . ASP E 1 125 ? -72.257 98.111  18.677  1.00 69.58  ? 125  ASP E CB  1 
ATOM   5299 C  CG  . ASP E 1 125 ? -71.056 98.406  17.804  1.00 72.03  ? 125  ASP E CG  1 
ATOM   5300 O  OD1 . ASP E 1 125 ? -71.127 98.192  16.571  1.00 70.49  ? 125  ASP E OD1 1 
ATOM   5301 O  OD2 . ASP E 1 125 ? -70.041 98.872  18.360  1.00 72.57  ? 125  ASP E OD2 1 
ATOM   5302 N  N   . LEU E 1 126 ? -73.080 95.484  16.309  1.00 66.69  ? 126  LEU E N   1 
ATOM   5303 C  CA  . LEU E 1 126 ? -73.588 95.217  14.966  1.00 70.86  ? 126  LEU E CA  1 
ATOM   5304 C  C   . LEU E 1 126 ? -73.070 96.194  13.903  1.00 69.83  ? 126  LEU E C   1 
ATOM   5305 O  O   . LEU E 1 126 ? -73.559 96.217  12.773  1.00 69.36  ? 126  LEU E O   1 
ATOM   5306 C  CB  . LEU E 1 126 ? -75.119 95.209  14.981  1.00 71.03  ? 126  LEU E CB  1 
ATOM   5307 C  CG  . LEU E 1 126 ? -75.763 94.517  16.188  1.00 72.85  ? 126  LEU E CG  1 
ATOM   5308 C  CD1 . LEU E 1 126 ? -77.289 94.529  16.095  1.00 68.26  ? 126  LEU E CD1 1 
ATOM   5309 C  CD2 . LEU E 1 126 ? -75.248 93.087  16.336  1.00 72.60  ? 126  LEU E CD2 1 
ATOM   5310 N  N   . GLY E 1 127 ? -72.073 96.991  14.265  1.00 74.89  ? 127  GLY E N   1 
ATOM   5311 C  CA  . GLY E 1 127 ? -71.441 97.893  13.317  1.00 73.35  ? 127  GLY E CA  1 
ATOM   5312 C  C   . GLY E 1 127 ? -72.051 99.279  13.346  1.00 74.84  ? 127  GLY E C   1 
ATOM   5313 O  O   . GLY E 1 127 ? -72.055 99.981  12.333  1.00 72.54  ? 127  GLY E O   1 
ATOM   5314 N  N   . LYS E 1 128 ? -72.554 99.677  14.515  1.00 75.92  ? 128  LYS E N   1 
ATOM   5315 C  CA  . LYS E 1 128 ? -73.319 100.920 14.649  1.00 78.84  ? 128  LYS E CA  1 
ATOM   5316 C  C   . LYS E 1 128 ? -72.937 101.738 15.887  1.00 77.62  ? 128  LYS E C   1 
ATOM   5317 O  O   . LYS E 1 128 ? -73.767 101.971 16.767  1.00 76.38  ? 128  LYS E O   1 
ATOM   5318 C  CB  . LYS E 1 128 ? -74.824 100.611 14.673  1.00 75.78  ? 128  LYS E CB  1 
ATOM   5319 C  CG  . LYS E 1 128 ? -75.376 100.070 13.361  1.00 74.16  ? 128  LYS E CG  1 
ATOM   5320 C  CD  . LYS E 1 128 ? -76.698 99.346  13.569  1.00 76.32  ? 128  LYS E CD  1 
ATOM   5321 C  CE  . LYS E 1 128 ? -77.355 98.970  12.244  1.00 78.15  ? 128  LYS E CE  1 
ATOM   5322 N  NZ  . LYS E 1 128 ? -76.447 98.216  11.331  1.00 77.05  ? 128  LYS E NZ  1 
ATOM   5323 N  N   . GLY E 1 129 ? -71.683 102.178 15.941  1.00 78.54  ? 129  GLY E N   1 
ATOM   5324 C  CA  . GLY E 1 129 ? -71.185 102.965 17.056  1.00 76.24  ? 129  GLY E CA  1 
ATOM   5325 C  C   . GLY E 1 129 ? -70.404 104.168 16.567  1.00 79.69  ? 129  GLY E C   1 
ATOM   5326 O  O   . GLY E 1 129 ? -69.883 104.952 17.363  1.00 81.01  ? 129  GLY E O   1 
ATOM   5327 N  N   . GLY E 1 130 ? -70.307 104.298 15.246  1.00 81.02  ? 130  GLY E N   1 
ATOM   5328 C  CA  . GLY E 1 130 ? -69.753 105.489 14.625  1.00 84.25  ? 130  GLY E CA  1 
ATOM   5329 C  C   . GLY E 1 130 ? -68.245 105.545 14.440  1.00 88.28  ? 130  GLY E C   1 
ATOM   5330 O  O   . GLY E 1 130 ? -67.729 106.506 13.865  1.00 88.53  ? 130  GLY E O   1 
ATOM   5331 N  N   . ASN E 1 131 ? -67.530 104.531 14.922  1.00 89.83  ? 131  ASN E N   1 
ATOM   5332 C  CA  . ASN E 1 131 ? -66.069 104.524 14.809  1.00 84.65  ? 131  ASN E CA  1 
ATOM   5333 C  C   . ASN E 1 131 ? -65.495 103.343 14.023  1.00 81.97  ? 131  ASN E C   1 
ATOM   5334 O  O   . ASN E 1 131 ? -66.219 102.423 13.636  1.00 79.68  ? 131  ASN E O   1 
ATOM   5335 C  CB  . ASN E 1 131 ? -65.407 104.633 16.193  1.00 80.99  ? 131  ASN E CB  1 
ATOM   5336 C  CG  . ASN E 1 131 ? -65.952 103.624 17.190  1.00 80.94  ? 131  ASN E CG  1 
ATOM   5337 O  OD1 . ASN E 1 131 ? -66.133 102.448 16.871  1.00 80.86  ? 131  ASN E OD1 1 
ATOM   5338 N  ND2 . ASN E 1 131 ? -66.209 104.082 18.411  1.00 75.00  ? 131  ASN E ND2 1 
ATOM   5339 N  N   . GLU E 1 132 ? -64.187 103.389 13.785  1.00 85.64  ? 132  GLU E N   1 
ATOM   5340 C  CA  . GLU E 1 132 ? -63.480 102.303 13.108  1.00 84.27  ? 132  GLU E CA  1 
ATOM   5341 C  C   . GLU E 1 132 ? -63.694 100.947 13.790  1.00 76.65  ? 132  GLU E C   1 
ATOM   5342 O  O   . GLU E 1 132 ? -63.945 99.943  13.123  1.00 73.14  ? 132  GLU E O   1 
ATOM   5343 C  CB  . GLU E 1 132 ? -61.976 102.605 13.015  1.00 82.50  ? 132  GLU E CB  1 
ATOM   5344 C  CG  . GLU E 1 132 ? -61.563 103.481 11.842  1.00 86.34  ? 132  GLU E CG  1 
ATOM   5345 C  CD  . GLU E 1 132 ? -61.578 102.743 10.509  1.00 89.98  ? 132  GLU E CD  1 
ATOM   5346 O  OE1 . GLU E 1 132 ? -60.485 102.540 9.928   1.00 82.94  ? 132  GLU E OE1 1 
ATOM   5347 O  OE2 . GLU E 1 132 ? -62.680 102.373 10.039  1.00 87.96  ? 132  GLU E OE2 1 
ATOM   5348 N  N   . GLU E 1 133 ? -63.591 100.907 15.114  1.00 70.60  ? 133  GLU E N   1 
ATOM   5349 C  CA  . GLU E 1 133 ? -63.635 99.618  15.788  1.00 75.84  ? 133  GLU E CA  1 
ATOM   5350 C  C   . GLU E 1 133 ? -65.043 99.027  15.791  1.00 74.74  ? 133  GLU E C   1 
ATOM   5351 O  O   . GLU E 1 133 ? -65.231 97.849  16.100  1.00 73.96  ? 133  GLU E O   1 
ATOM   5352 C  CB  . GLU E 1 133 ? -63.033 99.681  17.197  1.00 78.60  ? 133  GLU E CB  1 
ATOM   5353 C  CG  . GLU E 1 133 ? -62.407 98.353  17.668  1.00 75.94  ? 133  GLU E CG  1 
ATOM   5354 C  CD  . GLU E 1 133 ? -61.439 97.736  16.645  1.00 78.90  ? 133  GLU E CD  1 
ATOM   5355 O  OE1 . GLU E 1 133 ? -60.769 98.489  15.897  1.00 80.12  ? 133  GLU E OE1 1 
ATOM   5356 O  OE2 . GLU E 1 133 ? -61.345 96.489  16.595  1.00 74.57  ? 133  GLU E OE2 1 
ATOM   5357 N  N   . SER E 1 134 ? -66.033 99.834  15.436  1.00 72.88  ? 134  SER E N   1 
ATOM   5358 C  CA  . SER E 1 134 ? -67.348 99.275  15.188  1.00 72.78  ? 134  SER E CA  1 
ATOM   5359 C  C   . SER E 1 134 ? -67.394 98.759  13.760  1.00 72.09  ? 134  SER E C   1 
ATOM   5360 O  O   . SER E 1 134 ? -68.044 97.752  13.468  1.00 72.40  ? 134  SER E O   1 
ATOM   5361 C  CB  . SER E 1 134 ? -68.452 100.298 15.414  1.00 74.94  ? 134  SER E CB  1 
ATOM   5362 O  OG  . SER E 1 134 ? -69.717 99.700  15.190  1.00 72.15  ? 134  SER E OG  1 
ATOM   5363 N  N   . THR E 1 135 ? -66.686 99.442  12.872  1.00 69.37  ? 135  THR E N   1 
ATOM   5364 C  CA  . THR E 1 135 ? -66.681 99.044  11.476  1.00 70.06  ? 135  THR E CA  1 
ATOM   5365 C  C   . THR E 1 135 ? -65.990 97.691  11.289  1.00 69.15  ? 135  THR E C   1 
ATOM   5366 O  O   . THR E 1 135 ? -66.263 96.971  10.329  1.00 65.32  ? 135  THR E O   1 
ATOM   5367 C  CB  . THR E 1 135 ? -66.032 100.126 10.569  1.00 75.01  ? 135  THR E CB  1 
ATOM   5368 O  OG1 . THR E 1 135 ? -66.547 100.003 9.241   1.00 79.37  ? 135  THR E OG1 1 
ATOM   5369 C  CG2 . THR E 1 135 ? -64.509 99.993  10.521  1.00 73.45  ? 135  THR E CG2 1 
ATOM   5370 N  N   . LYS E 1 136 ? -65.102 97.345  12.215  1.00 66.45  ? 136  LYS E N   1 
ATOM   5371 C  CA  . LYS E 1 136 ? -64.315 96.127  12.076  1.00 71.30  ? 136  LYS E CA  1 
ATOM   5372 C  C   . LYS E 1 136 ? -64.690 95.023  13.070  1.00 71.84  ? 136  LYS E C   1 
ATOM   5373 O  O   . LYS E 1 136 ? -64.894 93.875  12.667  1.00 65.60  ? 136  LYS E O   1 
ATOM   5374 C  CB  . LYS E 1 136 ? -62.817 96.439  12.173  1.00 71.56  ? 136  LYS E CB  1 
ATOM   5375 C  CG  . LYS E 1 136 ? -62.219 97.071  10.922  1.00 72.40  ? 136  LYS E CG  1 
ATOM   5376 C  CD  . LYS E 1 136 ? -60.791 97.520  11.183  1.00 73.32  ? 136  LYS E CD  1 
ATOM   5377 C  CE  . LYS E 1 136 ? -60.748 98.533  12.329  1.00 78.74  ? 136  LYS E CE  1 
ATOM   5378 N  NZ  . LYS E 1 136 ? -59.400 98.637  12.967  1.00 79.94  ? 136  LYS E NZ  1 
ATOM   5379 N  N   . THR E 1 137 ? -64.784 95.365  14.355  1.00 67.17  ? 137  THR E N   1 
ATOM   5380 C  CA  . THR E 1 137 ? -64.964 94.354  15.394  1.00 66.37  ? 137  THR E CA  1 
ATOM   5381 C  C   . THR E 1 137 ? -66.328 94.419  16.098  1.00 66.37  ? 137  THR E C   1 
ATOM   5382 O  O   . THR E 1 137 ? -66.652 93.561  16.926  1.00 63.15  ? 137  THR E O   1 
ATOM   5383 C  CB  . THR E 1 137 ? -63.807 94.417  16.443  1.00 65.91  ? 137  THR E CB  1 
ATOM   5384 O  OG1 . THR E 1 137 ? -63.652 93.145  17.078  1.00 68.21  ? 137  THR E OG1 1 
ATOM   5385 C  CG2 . THR E 1 137 ? -64.073 95.461  17.505  1.00 68.16  ? 137  THR E CG2 1 
ATOM   5386 N  N   . GLY E 1 138 ? -67.124 95.433  15.767  1.00 68.93  ? 138  GLY E N   1 
ATOM   5387 C  CA  . GLY E 1 138 ? -68.371 95.682  16.473  1.00 66.23  ? 138  GLY E CA  1 
ATOM   5388 C  C   . GLY E 1 138 ? -68.121 95.967  17.943  1.00 67.74  ? 138  GLY E C   1 
ATOM   5389 O  O   . GLY E 1 138 ? -69.049 96.003  18.759  1.00 64.90  ? 138  GLY E O   1 
ATOM   5390 N  N   . ASN E 1 139 ? -66.850 96.165  18.277  1.00 67.58  ? 139  ASN E N   1 
ATOM   5391 C  CA  . ASN E 1 139 ? -66.434 96.420  19.647  1.00 66.40  ? 139  ASN E CA  1 
ATOM   5392 C  C   . ASN E 1 139 ? -66.798 95.270  20.581  1.00 72.22  ? 139  ASN E C   1 
ATOM   5393 O  O   . ASN E 1 139 ? -67.122 95.470  21.760  1.00 69.24  ? 139  ASN E O   1 
ATOM   5394 C  CB  . ASN E 1 139 ? -66.999 97.756  20.133  1.00 74.68  ? 139  ASN E CB  1 
ATOM   5395 C  CG  . ASN E 1 139 ? -66.390 98.944  19.398  1.00 76.01  ? 139  ASN E CG  1 
ATOM   5396 O  OD1 . ASN E 1 139 ? -67.096 99.742  18.776  1.00 71.46  ? 139  ASN E OD1 1 
ATOM   5397 N  ND2 . ASN E 1 139 ? -65.062 99.053  19.455  1.00 77.09  ? 139  ASN E ND2 1 
ATOM   5398 N  N   . ALA E 1 140 ? -66.722 94.058  20.037  1.00 73.08  ? 140  ALA E N   1 
ATOM   5399 C  CA  . ALA E 1 140 ? -67.009 92.845  20.791  1.00 67.08  ? 140  ALA E CA  1 
ATOM   5400 C  C   . ALA E 1 140 ? -65.997 92.632  21.919  1.00 65.16  ? 140  ALA E C   1 
ATOM   5401 O  O   . ALA E 1 140 ? -66.240 91.869  22.861  1.00 65.17  ? 140  ALA E O   1 
ATOM   5402 C  CB  . ALA E 1 140 ? -67.019 91.647  19.852  1.00 68.89  ? 140  ALA E CB  1 
ATOM   5403 N  N   . GLY E 1 141 ? -64.862 93.316  21.825  1.00 66.55  ? 141  GLY E N   1 
ATOM   5404 C  CA  . GLY E 1 141 ? -63.825 93.181  22.832  1.00 68.78  ? 141  GLY E CA  1 
ATOM   5405 C  C   . GLY E 1 141 ? -63.007 91.916  22.632  1.00 67.82  ? 141  GLY E C   1 
ATOM   5406 O  O   . GLY E 1 141 ? -62.882 91.412  21.511  1.00 66.03  ? 141  GLY E O   1 
ATOM   5407 N  N   . SER E 1 142 ? -62.453 91.384  23.716  1.00 68.59  ? 142  SER E N   1 
ATOM   5408 C  CA  . SER E 1 142 ? -61.565 90.230  23.594  1.00 71.11  ? 142  SER E CA  1 
ATOM   5409 C  C   . SER E 1 142 ? -62.315 88.899  23.416  1.00 68.42  ? 142  SER E C   1 
ATOM   5410 O  O   . SER E 1 142 ? -63.555 88.855  23.376  1.00 63.49  ? 142  SER E O   1 
ATOM   5411 C  CB  . SER E 1 142 ? -60.557 90.167  24.756  1.00 67.85  ? 142  SER E CB  1 
ATOM   5412 O  OG  . SER E 1 142 ? -61.209 89.999  26.003  1.00 68.38  ? 142  SER E OG  1 
ATOM   5413 N  N   . ARG E 1 143 ? -61.537 87.824  23.309  1.00 64.66  ? 143  ARG E N   1 
ATOM   5414 C  CA  . ARG E 1 143 ? -62.041 86.507  22.961  1.00 53.66  ? 143  ARG E CA  1 
ATOM   5415 C  C   . ARG E 1 143 ? -62.109 85.576  24.177  1.00 57.78  ? 143  ARG E C   1 
ATOM   5416 O  O   . ARG E 1 143 ? -61.111 84.979  24.569  1.00 56.52  ? 143  ARG E O   1 
ATOM   5417 C  CB  . ARG E 1 143 ? -61.146 85.946  21.866  1.00 47.98  ? 143  ARG E CB  1 
ATOM   5418 C  CG  . ARG E 1 143 ? -60.954 86.969  20.780  1.00 49.08  ? 143  ARG E CG  1 
ATOM   5419 C  CD  . ARG E 1 143 ? -60.167 86.484  19.598  1.00 46.37  ? 143  ARG E CD  1 
ATOM   5420 N  NE  . ARG E 1 143 ? -60.075 87.551  18.607  1.00 46.13  ? 143  ARG E NE  1 
ATOM   5421 C  CZ  . ARG E 1 143 ? -59.600 87.399  17.375  1.00 50.79  ? 143  ARG E CZ  1 
ATOM   5422 N  NH1 . ARG E 1 143 ? -59.166 86.213  16.975  1.00 54.87  ? 143  ARG E NH1 1 
ATOM   5423 N  NH2 . ARG E 1 143 ? -59.556 88.431  16.540  1.00 47.76  ? 143  ARG E NH2 1 
ATOM   5424 N  N   . LEU E 1 144 ? -63.295 85.470  24.774  1.00 58.80  ? 144  LEU E N   1 
ATOM   5425 C  CA  . LEU E 1 144 ? -63.489 84.695  25.994  1.00 55.67  ? 144  LEU E CA  1 
ATOM   5426 C  C   . LEU E 1 144 ? -63.252 83.208  25.771  1.00 60.36  ? 144  LEU E C   1 
ATOM   5427 O  O   . LEU E 1 144 ? -62.749 82.511  26.655  1.00 61.10  ? 144  LEU E O   1 
ATOM   5428 C  CB  . LEU E 1 144 ? -64.903 84.915  26.542  1.00 62.02  ? 144  LEU E CB  1 
ATOM   5429 C  CG  . LEU E 1 144 ? -65.144 85.929  27.669  1.00 67.51  ? 144  LEU E CG  1 
ATOM   5430 C  CD1 . LEU E 1 144 ? -64.090 87.035  27.677  1.00 66.93  ? 144  LEU E CD1 1 
ATOM   5431 C  CD2 . LEU E 1 144 ? -66.563 86.509  27.593  1.00 59.42  ? 144  LEU E CD2 1 
ATOM   5432 N  N   . ALA E 1 145 ? -63.627 82.723  24.589  1.00 56.38  ? 145  ALA E N   1 
ATOM   5433 C  CA  . ALA E 1 145 ? -63.531 81.296  24.272  1.00 58.50  ? 145  ALA E CA  1 
ATOM   5434 C  C   . ALA E 1 145 ? -63.707 81.045  22.780  1.00 55.87  ? 145  ALA E C   1 
ATOM   5435 O  O   . ALA E 1 145 ? -64.303 81.846  22.066  1.00 52.34  ? 145  ALA E O   1 
ATOM   5436 C  CB  . ALA E 1 145 ? -64.545 80.482  25.076  1.00 48.58  ? 145  ALA E CB  1 
ATOM   5437 N  N   . CYS E 1 146 ? -63.172 79.927  22.312  1.00 54.98  ? 146  CYS E N   1 
ATOM   5438 C  CA  . CYS E 1 146 ? -63.244 79.597  20.902  1.00 54.48  ? 146  CYS E CA  1 
ATOM   5439 C  C   . CYS E 1 146 ? -63.042 78.103  20.678  1.00 53.44  ? 146  CYS E C   1 
ATOM   5440 O  O   . CYS E 1 146 ? -62.763 77.351  21.614  1.00 51.77  ? 146  CYS E O   1 
ATOM   5441 C  CB  . CYS E 1 146 ? -62.209 80.400  20.112  1.00 51.77  ? 146  CYS E CB  1 
ATOM   5442 S  SG  . CYS E 1 146 ? -60.513 80.162  20.683  1.00 61.41  ? 146  CYS E SG  1 
ATOM   5443 N  N   . GLY E 1 147 ? -63.193 77.686  19.428  1.00 47.99  ? 147  GLY E N   1 
ATOM   5444 C  CA  . GLY E 1 147 ? -63.024 76.302  19.048  1.00 46.81  ? 147  GLY E CA  1 
ATOM   5445 C  C   . GLY E 1 147 ? -63.113 76.218  17.545  1.00 44.19  ? 147  GLY E C   1 
ATOM   5446 O  O   . GLY E 1 147 ? -63.771 77.044  16.912  1.00 42.05  ? 147  GLY E O   1 
ATOM   5447 N  N   . VAL E 1 148 ? -62.441 75.232  16.965  1.00 41.15  ? 148  VAL E N   1 
ATOM   5448 C  CA  . VAL E 1 148 ? -62.536 75.022  15.535  1.00 38.82  ? 148  VAL E CA  1 
ATOM   5449 C  C   . VAL E 1 148 ? -63.848 74.304  15.230  1.00 41.81  ? 148  VAL E C   1 
ATOM   5450 O  O   . VAL E 1 148 ? -64.321 73.474  16.015  1.00 40.51  ? 148  VAL E O   1 
ATOM   5451 C  CB  . VAL E 1 148 ? -61.331 74.237  14.977  1.00 40.19  ? 148  VAL E CB  1 
ATOM   5452 C  CG1 . VAL E 1 148 ? -61.304 74.307  13.453  1.00 36.49  ? 148  VAL E CG1 1 
ATOM   5453 C  CG2 . VAL E 1 148 ? -60.025 74.793  15.534  1.00 41.44  ? 148  VAL E CG2 1 
ATOM   5454 N  N   . ILE E 1 149 ? -64.453 74.662  14.102  1.00 41.25  ? 149  ILE E N   1 
ATOM   5455 C  CA  . ILE E 1 149 ? -65.699 74.053  13.681  1.00 42.68  ? 149  ILE E CA  1 
ATOM   5456 C  C   . ILE E 1 149 ? -65.388 72.775  12.921  1.00 40.00  ? 149  ILE E C   1 
ATOM   5457 O  O   . ILE E 1 149 ? -64.759 72.816  11.859  1.00 39.84  ? 149  ILE E O   1 
ATOM   5458 C  CB  . ILE E 1 149 ? -66.541 75.027  12.824  1.00 44.09  ? 149  ILE E CB  1 
ATOM   5459 C  CG1 . ILE E 1 149 ? -66.910 76.270  13.648  1.00 45.28  ? 149  ILE E CG1 1 
ATOM   5460 C  CG2 . ILE E 1 149 ? -67.794 74.340  12.305  1.00 42.19  ? 149  ILE E CG2 1 
ATOM   5461 C  CD1 . ILE E 1 149 ? -67.499 77.405  12.827  1.00 42.21  ? 149  ILE E CD1 1 
ATOM   5462 N  N   . GLY E 1 150 ? -65.822 71.646  13.482  1.00 36.20  ? 150  GLY E N   1 
ATOM   5463 C  CA  . GLY E 1 150 ? -65.536 70.330  12.925  1.00 39.77  ? 150  GLY E CA  1 
ATOM   5464 C  C   . GLY E 1 150 ? -66.722 69.502  12.451  1.00 36.31  ? 150  GLY E C   1 
ATOM   5465 O  O   . GLY E 1 150 ? -67.864 69.753  12.825  1.00 41.27  ? 150  GLY E O   1 
ATOM   5466 N  N   . ILE E 1 151 ? -66.439 68.505  11.618  1.00 39.87  ? 151  ILE E N   1 
ATOM   5467 C  CA  . ILE E 1 151 ? -67.468 67.638  11.043  1.00 38.23  ? 151  ILE E CA  1 
ATOM   5468 C  C   . ILE E 1 151 ? -68.045 66.683  12.089  1.00 42.21  ? 151  ILE E C   1 
ATOM   5469 O  O   . ILE E 1 151 ? -67.307 66.080  12.878  1.00 39.39  ? 151  ILE E O   1 
ATOM   5470 C  CB  . ILE E 1 151 ? -66.945 66.857  9.827   1.00 36.95  ? 151  ILE E CB  1 
ATOM   5471 C  CG1 . ILE E 1 151 ? -66.573 67.820  8.708   1.00 35.03  ? 151  ILE E CG1 1 
ATOM   5472 C  CG2 . ILE E 1 151 ? -68.009 65.914  9.293   1.00 39.36  ? 151  ILE E CG2 1 
ATOM   5473 C  CD1 . ILE E 1 151 ? -65.997 67.124  7.482   1.00 37.30  ? 151  ILE E CD1 1 
ATOM   5474 N  N   . ALA E 1 152 ? -69.373 66.577  12.109  1.00 41.92  ? 152  ALA E N   1 
ATOM   5475 C  CA  . ALA E 1 152 ? -70.057 65.817  13.154  1.00 45.40  ? 152  ALA E CA  1 
ATOM   5476 C  C   . ALA E 1 152 ? -70.851 64.642  12.586  1.00 42.83  ? 152  ALA E C   1 
ATOM   5477 O  O   . ALA E 1 152 ? -71.108 64.569  11.388  1.00 43.96  ? 152  ALA E O   1 
ATOM   5478 C  CB  . ALA E 1 152 ? -70.966 66.734  13.962  1.00 41.70  ? 152  ALA E CB  1 
ATOM   5479 N  N   . GLN E 1 153 ? -71.234 63.721  13.454  1.00 43.89  ? 153  GLN E N   1 
ATOM   5480 C  CA  . GLN E 1 153 ? -72.013 62.572  13.019  1.00 54.29  ? 153  GLN E CA  1 
ATOM   5481 C  C   . GLN E 1 153 ? -73.506 62.891  13.012  1.00 61.48  ? 153  GLN E C   1 
ATOM   5482 O  O   . GLN E 1 153 ? -74.085 63.264  14.046  1.00 64.85  ? 153  GLN E O   1 
ATOM   5483 C  CB  . GLN E 1 153 ? -71.742 61.375  13.925  1.00 55.41  ? 153  GLN E CB  1 
ATOM   5484 C  CG  . GLN E 1 153 ? -72.401 60.097  13.453  1.00 54.71  ? 153  GLN E CG  1 
ATOM   5485 C  CD  . GLN E 1 153 ? -72.196 58.960  14.433  1.00 61.73  ? 153  GLN E CD  1 
ATOM   5486 O  OE1 . GLN E 1 153 ? -71.693 57.895  14.067  1.00 65.21  ? 153  GLN E OE1 1 
ATOM   5487 N  NE2 . GLN E 1 153 ? -72.579 59.181  15.694  1.00 55.96  ? 153  GLN E NE2 1 
ATOM   5488 O  OXT . GLN E 1 153 ? -74.160 62.783  11.970  1.00 58.00  ? 153  GLN E OXT 1 
ATOM   5489 N  N   . ALA F 1 1   ? -53.355 77.548  -3.507  1.00 55.19  ? 1    ALA F N   1 
ATOM   5490 C  CA  . ALA F 1 1   ? -52.469 76.936  -2.522  1.00 56.97  ? 1    ALA F CA  1 
ATOM   5491 C  C   . ALA F 1 1   ? -53.165 76.825  -1.166  1.00 61.67  ? 1    ALA F C   1 
ATOM   5492 O  O   . ALA F 1 1   ? -53.480 77.838  -0.533  1.00 61.86  ? 1    ALA F O   1 
ATOM   5493 C  CB  . ALA F 1 1   ? -51.183 77.732  -2.393  1.00 53.47  ? 1    ALA F CB  1 
ATOM   5494 N  N   . MET F 1 2   ? -53.395 75.594  -0.719  1.00 53.46  ? 2    MET F N   1 
ATOM   5495 C  CA  . MET F 1 2   ? -54.166 75.364  0.493   1.00 50.31  ? 2    MET F CA  1 
ATOM   5496 C  C   . MET F 1 2   ? -53.262 75.078  1.693   1.00 43.86  ? 2    MET F C   1 
ATOM   5497 O  O   . MET F 1 2   ? -52.286 74.343  1.580   1.00 44.19  ? 2    MET F O   1 
ATOM   5498 C  CB  . MET F 1 2   ? -55.160 74.218  0.260   1.00 50.20  ? 2    MET F CB  1 
ATOM   5499 C  CG  . MET F 1 2   ? -56.220 74.517  -0.811  1.00 46.29  ? 2    MET F CG  1 
ATOM   5500 S  SD  . MET F 1 2   ? -56.840 73.062  -1.715  1.00 53.70  ? 2    MET F SD  1 
ATOM   5501 C  CE  . MET F 1 2   ? -55.426 72.636  -2.756  1.00 46.65  ? 2    MET F CE  1 
ATOM   5502 N  N   . LYS F 1 3   ? -53.589 75.669  2.836   1.00 39.07  ? 3    LYS F N   1 
ATOM   5503 C  CA  . LYS F 1 3   ? -52.840 75.433  4.065   1.00 42.04  ? 3    LYS F CA  1 
ATOM   5504 C  C   . LYS F 1 3   ? -53.761 75.053  5.225   1.00 42.45  ? 3    LYS F C   1 
ATOM   5505 O  O   . LYS F 1 3   ? -54.911 75.494  5.290   1.00 34.16  ? 3    LYS F O   1 
ATOM   5506 C  CB  . LYS F 1 3   ? -52.029 76.675  4.447   1.00 50.54  ? 3    LYS F CB  1 
ATOM   5507 C  CG  . LYS F 1 3   ? -50.725 76.873  3.659   1.00 54.54  ? 3    LYS F CG  1 
ATOM   5508 C  CD  . LYS F 1 3   ? -49.845 77.930  4.330   1.00 63.31  ? 3    LYS F CD  1 
ATOM   5509 C  CE  . LYS F 1 3   ? -48.407 77.906  3.818   1.00 73.28  ? 3    LYS F CE  1 
ATOM   5510 N  NZ  . LYS F 1 3   ? -48.223 78.597  2.502   1.00 79.17  ? 3    LYS F NZ  1 
ATOM   5511 N  N   . ALA F 1 4   ? -53.246 74.256  6.160   1.00 40.70  ? 4    ALA F N   1 
ATOM   5512 C  CA  . ALA F 1 4   ? -54.044 73.829  7.311   1.00 37.74  ? 4    ALA F CA  1 
ATOM   5513 C  C   . ALA F 1 4   ? -53.197 73.709  8.554   1.00 39.45  ? 4    ALA F C   1 
ATOM   5514 O  O   . ALA F 1 4   ? -51.966 73.701  8.474   1.00 39.46  ? 4    ALA F O   1 
ATOM   5515 C  CB  . ALA F 1 4   ? -54.767 72.494  7.030   1.00 35.59  ? 4    ALA F CB  1 
ATOM   5516 N  N   . VAL F 1 5   ? -53.870 73.588  9.697   1.00 36.73  ? 5    VAL F N   1 
ATOM   5517 C  CA  . VAL F 1 5   ? -53.207 73.571  10.983  1.00 34.63  ? 5    VAL F CA  1 
ATOM   5518 C  C   . VAL F 1 5   ? -54.055 72.847  12.019  1.00 38.88  ? 5    VAL F C   1 
ATOM   5519 O  O   . VAL F 1 5   ? -55.294 72.840  11.937  1.00 38.30  ? 5    VAL F O   1 
ATOM   5520 C  CB  . VAL F 1 5   ? -52.883 75.003  11.476  1.00 40.28  ? 5    VAL F CB  1 
ATOM   5521 C  CG1 . VAL F 1 5   ? -54.154 75.742  11.880  1.00 40.79  ? 5    VAL F CG1 1 
ATOM   5522 C  CG2 . VAL F 1 5   ? -51.889 74.969  12.640  1.00 36.74  ? 5    VAL F CG2 1 
ATOM   5523 N  N   . CYS F 1 6   ? -53.374 72.241  12.993  1.00 36.89  ? 6    CYS F N   1 
ATOM   5524 C  CA  . CYS F 1 6   ? -54.023 71.458  14.037  1.00 38.92  ? 6    CYS F CA  1 
ATOM   5525 C  C   . CYS F 1 6   ? -53.252 71.565  15.339  1.00 37.16  ? 6    CYS F C   1 
ATOM   5526 O  O   . CYS F 1 6   ? -52.041 71.424  15.358  1.00 40.38  ? 6    CYS F O   1 
ATOM   5527 C  CB  . CYS F 1 6   ? -54.103 69.982  13.633  1.00 32.57  ? 6    CYS F CB  1 
ATOM   5528 S  SG  . CYS F 1 6   ? -54.859 68.937  14.917  1.00 41.84  ? 6    CYS F SG  1 
ATOM   5529 N  N   . VAL F 1 7   ? -53.949 71.807  16.434  1.00 40.03  ? 7    VAL F N   1 
ATOM   5530 C  CA  . VAL F 1 7   ? -53.290 71.828  17.729  1.00 39.60  ? 7    VAL F CA  1 
ATOM   5531 C  C   . VAL F 1 7   ? -53.742 70.611  18.518  1.00 41.68  ? 7    VAL F C   1 
ATOM   5532 O  O   . VAL F 1 7   ? -54.934 70.459  18.794  1.00 42.82  ? 7    VAL F O   1 
ATOM   5533 C  CB  . VAL F 1 7   ? -53.611 73.127  18.506  1.00 43.44  ? 7    VAL F CB  1 
ATOM   5534 C  CG1 . VAL F 1 7   ? -53.117 73.040  19.967  1.00 41.05  ? 7    VAL F CG1 1 
ATOM   5535 C  CG2 . VAL F 1 7   ? -53.014 74.323  17.793  1.00 40.14  ? 7    VAL F CG2 1 
ATOM   5536 N  N   . LEU F 1 8   ? -52.801 69.735  18.867  1.00 37.35  ? 8    LEU F N   1 
ATOM   5537 C  CA  . LEU F 1 8   ? -53.148 68.528  19.606  1.00 40.59  ? 8    LEU F CA  1 
ATOM   5538 C  C   . LEU F 1 8   ? -52.997 68.716  21.119  1.00 43.00  ? 8    LEU F C   1 
ATOM   5539 O  O   . LEU F 1 8   ? -51.956 69.145  21.604  1.00 43.25  ? 8    LEU F O   1 
ATOM   5540 C  CB  . LEU F 1 8   ? -52.303 67.346  19.133  1.00 41.58  ? 8    LEU F CB  1 
ATOM   5541 C  CG  . LEU F 1 8   ? -52.155 67.229  17.615  1.00 43.29  ? 8    LEU F CG  1 
ATOM   5542 C  CD1 . LEU F 1 8   ? -50.818 66.609  17.250  1.00 39.40  ? 8    LEU F CD1 1 
ATOM   5543 C  CD2 . LEU F 1 8   ? -53.297 66.421  17.028  1.00 39.05  ? 8    LEU F CD2 1 
ATOM   5544 N  N   . LYS F 1 9   ? -54.049 68.388  21.854  1.00 39.95  ? 9    LYS F N   1 
ATOM   5545 C  CA  . LYS F 1 9   ? -54.034 68.466  23.299  1.00 41.91  ? 9    LYS F CA  1 
ATOM   5546 C  C   . LYS F 1 9   ? -54.817 67.267  23.785  1.00 42.96  ? 9    LYS F C   1 
ATOM   5547 O  O   . LYS F 1 9   ? -55.734 66.811  23.103  1.00 44.17  ? 9    LYS F O   1 
ATOM   5548 C  CB  . LYS F 1 9   ? -54.730 69.744  23.777  1.00 43.53  ? 9    LYS F CB  1 
ATOM   5549 C  CG  . LYS F 1 9   ? -54.201 71.036  23.166  1.00 47.21  ? 9    LYS F CG  1 
ATOM   5550 C  CD  . LYS F 1 9   ? -52.870 71.467  23.775  1.00 52.03  ? 9    LYS F CD  1 
ATOM   5551 C  CE  . LYS F 1 9   ? -53.034 71.966  25.213  1.00 63.18  ? 9    LYS F CE  1 
ATOM   5552 N  NZ  . LYS F 1 9   ? -51.785 72.608  25.751  1.00 62.51  ? 9    LYS F NZ  1 
ATOM   5553 N  N   . GLY F 1 10  ? -54.464 66.763  24.963  1.00 44.34  ? 10   GLY F N   1 
ATOM   5554 C  CA  . GLY F 1 10  ? -55.180 65.656  25.568  1.00 45.89  ? 10   GLY F CA  1 
ATOM   5555 C  C   . GLY F 1 10  ? -55.214 65.755  27.077  1.00 50.98  ? 10   GLY F C   1 
ATOM   5556 O  O   . GLY F 1 10  ? -54.962 66.821  27.645  1.00 51.65  ? 10   GLY F O   1 
ATOM   5557 N  N   . ASP F 1 11  ? -55.519 64.631  27.721  1.00 56.86  ? 11   ASP F N   1 
ATOM   5558 C  CA  . ASP F 1 11  ? -55.640 64.557  29.178  1.00 53.35  ? 11   ASP F CA  1 
ATOM   5559 C  C   . ASP F 1 11  ? -54.287 64.608  29.878  1.00 52.13  ? 11   ASP F C   1 
ATOM   5560 O  O   . ASP F 1 11  ? -54.164 65.132  30.981  1.00 59.13  ? 11   ASP F O   1 
ATOM   5561 C  CB  . ASP F 1 11  ? -56.377 63.273  29.587  1.00 52.83  ? 11   ASP F CB  1 
ATOM   5562 C  CG  . ASP F 1 11  ? -57.887 63.381  29.416  1.00 64.18  ? 11   ASP F CG  1 
ATOM   5563 O  OD1 . ASP F 1 11  ? -58.451 64.467  29.687  1.00 66.64  ? 11   ASP F OD1 1 
ATOM   5564 O  OD2 . ASP F 1 11  ? -58.518 62.375  29.024  1.00 65.45  ? 11   ASP F OD2 1 
ATOM   5565 N  N   . GLY F 1 12  ? -53.270 64.047  29.243  1.00 49.47  ? 12   GLY F N   1 
ATOM   5566 C  CA  . GLY F 1 12  ? -51.953 63.996  29.842  1.00 46.56  ? 12   GLY F CA  1 
ATOM   5567 C  C   . GLY F 1 12  ? -51.038 65.094  29.347  1.00 44.67  ? 12   GLY F C   1 
ATOM   5568 O  O   . GLY F 1 12  ? -51.491 66.189  29.042  1.00 45.57  ? 12   GLY F O   1 
ATOM   5569 N  N   . PRO F 1 13  ? -49.735 64.794  29.273  1.00 46.45  ? 13   PRO F N   1 
ATOM   5570 C  CA  . PRO F 1 13  ? -48.646 65.712  28.928  1.00 45.31  ? 13   PRO F CA  1 
ATOM   5571 C  C   . PRO F 1 13  ? -48.482 65.933  27.438  1.00 48.51  ? 13   PRO F C   1 
ATOM   5572 O  O   . PRO F 1 13  ? -47.662 66.769  27.030  1.00 46.85  ? 13   PRO F O   1 
ATOM   5573 C  CB  . PRO F 1 13  ? -47.391 64.980  29.435  1.00 45.78  ? 13   PRO F CB  1 
ATOM   5574 C  CG  . PRO F 1 13  ? -47.883 63.820  30.225  1.00 50.06  ? 13   PRO F CG  1 
ATOM   5575 C  CD  . PRO F 1 13  ? -49.225 63.483  29.704  1.00 45.57  ? 13   PRO F CD  1 
ATOM   5576 N  N   . VAL F 1 14  ? -49.212 65.185  26.621  1.00 46.02  ? 14   VAL F N   1 
ATOM   5577 C  CA  . VAL F 1 14  ? -48.910 65.238  25.199  1.00 44.09  ? 14   VAL F CA  1 
ATOM   5578 C  C   . VAL F 1 14  ? -49.593 66.411  24.536  1.00 43.82  ? 14   VAL F C   1 
ATOM   5579 O  O   . VAL F 1 14  ? -50.791 66.632  24.728  1.00 48.17  ? 14   VAL F O   1 
ATOM   5580 C  CB  . VAL F 1 14  ? -49.241 63.925  24.468  1.00 40.59  ? 14   VAL F CB  1 
ATOM   5581 C  CG1 . VAL F 1 14  ? -48.985 64.082  22.957  1.00 31.57  ? 14   VAL F CG1 1 
ATOM   5582 C  CG2 . VAL F 1 14  ? -48.412 62.783  25.059  1.00 38.15  ? 14   VAL F CG2 1 
ATOM   5583 N  N   . GLN F 1 15  ? -48.817 67.165  23.763  1.00 40.42  ? 15   GLN F N   1 
ATOM   5584 C  CA  . GLN F 1 15  ? -49.339 68.301  23.013  1.00 43.73  ? 15   GLN F CA  1 
ATOM   5585 C  C   . GLN F 1 15  ? -48.430 68.599  21.825  1.00 42.28  ? 15   GLN F C   1 
ATOM   5586 O  O   . GLN F 1 15  ? -47.297 68.128  21.775  1.00 41.38  ? 15   GLN F O   1 
ATOM   5587 C  CB  . GLN F 1 15  ? -49.477 69.534  23.919  1.00 47.33  ? 15   GLN F CB  1 
ATOM   5588 C  CG  . GLN F 1 15  ? -48.166 70.235  24.252  1.00 50.98  ? 15   GLN F CG  1 
ATOM   5589 C  CD  . GLN F 1 15  ? -48.285 71.159  25.468  1.00 56.22  ? 15   GLN F CD  1 
ATOM   5590 O  OE1 . GLN F 1 15  ? -47.622 70.953  26.486  1.00 54.19  ? 15   GLN F OE1 1 
ATOM   5591 N  NE2 . GLN F 1 15  ? -49.141 72.171  25.366  1.00 58.37  ? 15   GLN F NE2 1 
ATOM   5592 N  N   . GLY F 1 16  ? -48.931 69.370  20.864  1.00 40.89  ? 16   GLY F N   1 
ATOM   5593 C  CA  . GLY F 1 16  ? -48.161 69.689  19.678  1.00 36.12  ? 16   GLY F CA  1 
ATOM   5594 C  C   . GLY F 1 16  ? -48.952 70.488  18.663  1.00 40.27  ? 16   GLY F C   1 
ATOM   5595 O  O   . GLY F 1 16  ? -50.088 70.882  18.907  1.00 39.84  ? 16   GLY F O   1 
ATOM   5596 N  N   . THR F 1 17  ? -48.344 70.706  17.506  1.00 34.38  ? 17   THR F N   1 
ATOM   5597 C  CA  . THR F 1 17  ? -48.874 71.596  16.510  1.00 32.44  ? 17   THR F CA  1 
ATOM   5598 C  C   . THR F 1 17  ? -48.418 71.064  15.172  1.00 38.88  ? 17   THR F C   1 
ATOM   5599 O  O   . THR F 1 17  ? -47.225 70.842  14.962  1.00 41.45  ? 17   THR F O   1 
ATOM   5600 C  CB  . THR F 1 17  ? -48.337 73.043  16.721  1.00 39.02  ? 17   THR F CB  1 
ATOM   5601 O  OG1 . THR F 1 17  ? -49.069 73.671  17.780  1.00 44.73  ? 17   THR F OG1 1 
ATOM   5602 C  CG2 . THR F 1 17  ? -48.468 73.894  15.457  1.00 32.46  ? 17   THR F CG2 1 
ATOM   5603 N  N   . ILE F 1 18  ? -49.363 70.850  14.266  1.00 37.44  ? 18   ILE F N   1 
ATOM   5604 C  CA  . ILE F 1 18  ? -49.038 70.284  12.966  1.00 38.74  ? 18   ILE F CA  1 
ATOM   5605 C  C   . ILE F 1 18  ? -49.515 71.234  11.883  1.00 39.77  ? 18   ILE F C   1 
ATOM   5606 O  O   . ILE F 1 18  ? -50.608 71.800  11.989  1.00 41.69  ? 18   ILE F O   1 
ATOM   5607 C  CB  . ILE F 1 18  ? -49.687 68.885  12.777  1.00 38.22  ? 18   ILE F CB  1 
ATOM   5608 C  CG1 . ILE F 1 18  ? -49.240 67.923  13.883  1.00 33.09  ? 18   ILE F CG1 1 
ATOM   5609 C  CG2 . ILE F 1 18  ? -49.350 68.318  11.403  1.00 34.46  ? 18   ILE F CG2 1 
ATOM   5610 C  CD1 . ILE F 1 18  ? -47.800 67.466  13.719  1.00 36.16  ? 18   ILE F CD1 1 
ATOM   5611 N  N   . HIS F 1 19  ? -48.689 71.417  10.856  1.00 37.21  ? 19   HIS F N   1 
ATOM   5612 C  CA  . HIS F 1 19  ? -49.009 72.302  9.732   1.00 36.38  ? 19   HIS F CA  1 
ATOM   5613 C  C   . HIS F 1 19  ? -49.151 71.506  8.460   1.00 35.87  ? 19   HIS F C   1 
ATOM   5614 O  O   . HIS F 1 19  ? -48.306 70.668  8.146   1.00 41.42  ? 19   HIS F O   1 
ATOM   5615 C  CB  . HIS F 1 19  ? -47.927 73.376  9.550   1.00 38.62  ? 19   HIS F CB  1 
ATOM   5616 C  CG  . HIS F 1 19  ? -47.777 74.267  10.738  1.00 40.95  ? 19   HIS F CG  1 
ATOM   5617 N  ND1 . HIS F 1 19  ? -48.512 75.422  10.899  1.00 45.24  ? 19   HIS F ND1 1 
ATOM   5618 C  CD2 . HIS F 1 19  ? -47.011 74.150  11.850  1.00 41.59  ? 19   HIS F CD2 1 
ATOM   5619 C  CE1 . HIS F 1 19  ? -48.197 75.986  12.052  1.00 40.21  ? 19   HIS F CE1 1 
ATOM   5620 N  NE2 . HIS F 1 19  ? -47.293 75.231  12.650  1.00 44.26  ? 19   HIS F NE2 1 
ATOM   5621 N  N   . PHE F 1 20  ? -50.229 71.747  7.727   1.00 37.49  ? 20   PHE F N   1 
ATOM   5622 C  CA  . PHE F 1 20  ? -50.455 71.003  6.495   1.00 38.06  ? 20   PHE F CA  1 
ATOM   5623 C  C   . PHE F 1 20  ? -50.287 71.945  5.330   1.00 37.14  ? 20   PHE F C   1 
ATOM   5624 O  O   . PHE F 1 20  ? -50.662 73.111  5.422   1.00 39.82  ? 20   PHE F O   1 
ATOM   5625 C  CB  . PHE F 1 20  ? -51.865 70.407  6.451   1.00 32.97  ? 20   PHE F CB  1 
ATOM   5626 C  CG  . PHE F 1 20  ? -52.186 69.498  7.598   1.00 34.46  ? 20   PHE F CG  1 
ATOM   5627 C  CD1 . PHE F 1 20  ? -52.212 68.123  7.427   1.00 31.24  ? 20   PHE F CD1 1 
ATOM   5628 C  CD2 . PHE F 1 20  ? -52.502 70.022  8.849   1.00 35.94  ? 20   PHE F CD2 1 
ATOM   5629 C  CE1 . PHE F 1 20  ? -52.525 67.293  8.491   1.00 35.02  ? 20   PHE F CE1 1 
ATOM   5630 C  CE2 . PHE F 1 20  ? -52.819 69.197  9.907   1.00 32.76  ? 20   PHE F CE2 1 
ATOM   5631 C  CZ  . PHE F 1 20  ? -52.837 67.831  9.731   1.00 32.06  ? 20   PHE F CZ  1 
ATOM   5632 N  N   . GLU F 1 21  ? -49.742 71.441  4.231   1.00 38.31  ? 21   GLU F N   1 
ATOM   5633 C  CA  . GLU F 1 21  ? -49.607 72.258  3.038   1.00 40.28  ? 21   GLU F CA  1 
ATOM   5634 C  C   . GLU F 1 21  ? -49.771 71.461  1.748   1.00 40.55  ? 21   GLU F C   1 
ATOM   5635 O  O   . GLU F 1 21  ? -49.111 70.445  1.523   1.00 38.06  ? 21   GLU F O   1 
ATOM   5636 C  CB  . GLU F 1 21  ? -48.282 73.032  3.039   1.00 46.93  ? 21   GLU F CB  1 
ATOM   5637 C  CG  . GLU F 1 21  ? -48.087 73.895  1.779   1.00 53.24  ? 21   GLU F CG  1 
ATOM   5638 C  CD  . GLU F 1 21  ? -46.949 74.908  1.893   1.00 66.12  ? 21   GLU F CD  1 
ATOM   5639 O  OE1 . GLU F 1 21  ? -46.326 75.010  2.979   1.00 70.27  ? 21   GLU F OE1 1 
ATOM   5640 O  OE2 . GLU F 1 21  ? -46.682 75.608  0.888   1.00 69.76  ? 21   GLU F OE2 1 
ATOM   5641 N  N   . GLN F 1 22  ? -50.663 71.943  0.896   1.00 42.06  ? 22   GLN F N   1 
ATOM   5642 C  CA  . GLN F 1 22  ? -50.953 71.272  -0.350  1.00 40.80  ? 22   GLN F CA  1 
ATOM   5643 C  C   . GLN F 1 22  ? -50.858 72.337  -1.406  1.00 44.03  ? 22   GLN F C   1 
ATOM   5644 O  O   . GLN F 1 22  ? -51.476 73.394  -1.280  1.00 46.12  ? 22   GLN F O   1 
ATOM   5645 C  CB  . GLN F 1 22  ? -52.357 70.668  -0.312  1.00 36.18  ? 22   GLN F CB  1 
ATOM   5646 C  CG  . GLN F 1 22  ? -52.711 69.864  -1.554  1.00 40.30  ? 22   GLN F CG  1 
ATOM   5647 C  CD  . GLN F 1 22  ? -54.065 69.178  -1.451  1.00 38.51  ? 22   GLN F CD  1 
ATOM   5648 O  OE1 . GLN F 1 22  ? -55.023 69.724  -0.892  1.00 38.51  ? 22   GLN F OE1 1 
ATOM   5649 N  NE2 . GLN F 1 22  ? -54.147 67.976  -1.992  1.00 36.12  ? 22   GLN F NE2 1 
ATOM   5650 N  N   . LYS F 1 23  ? -50.069 72.077  -2.440  1.00 47.66  ? 23   LYS F N   1 
ATOM   5651 C  CA  . LYS F 1 23  ? -49.773 73.109  -3.425  1.00 52.12  ? 23   LYS F CA  1 
ATOM   5652 C  C   . LYS F 1 23  ? -50.953 73.362  -4.341  1.00 52.29  ? 23   LYS F C   1 
ATOM   5653 O  O   . LYS F 1 23  ? -51.181 74.488  -4.783  1.00 57.53  ? 23   LYS F O   1 
ATOM   5654 C  CB  . LYS F 1 23  ? -48.548 72.747  -4.262  1.00 54.28  ? 23   LYS F CB  1 
ATOM   5655 C  CG  . LYS F 1 23  ? -48.675 73.259  -5.693  1.00 70.21  ? 23   LYS F CG  1 
ATOM   5656 C  CD  . LYS F 1 23  ? -47.371 73.225  -6.471  1.00 78.60  ? 23   LYS F CD  1 
ATOM   5657 C  CE  . LYS F 1 23  ? -47.509 74.022  -7.766  1.00 81.62  ? 23   LYS F CE  1 
ATOM   5658 N  NZ  . LYS F 1 23  ? -46.183 74.291  -8.397  1.00 90.81  ? 23   LYS F NZ  1 
ATOM   5659 N  N   . ALA F 1 24  ? -51.698 72.303  -4.626  1.00 51.47  ? 24   ALA F N   1 
ATOM   5660 C  CA  . ALA F 1 24  ? -52.790 72.364  -5.587  1.00 51.02  ? 24   ALA F CA  1 
ATOM   5661 C  C   . ALA F 1 24  ? -53.659 71.110  -5.499  1.00 49.18  ? 24   ALA F C   1 
ATOM   5662 O  O   . ALA F 1 24  ? -53.212 70.060  -5.022  1.00 46.90  ? 24   ALA F O   1 
ATOM   5663 C  CB  . ALA F 1 24  ? -52.239 72.537  -7.004  1.00 50.91  ? 24   ALA F CB  1 
ATOM   5664 N  N   . SER F 1 25  ? -54.879 71.229  -6.020  1.00 48.77  ? 25   SER F N   1 
ATOM   5665 C  CA  . SER F 1 25  ? -55.974 70.294  -5.769  1.00 45.14  ? 25   SER F CA  1 
ATOM   5666 C  C   . SER F 1 25  ? -55.627 68.908  -5.264  1.00 46.76  ? 25   SER F C   1 
ATOM   5667 O  O   . SER F 1 25  ? -55.626 68.683  -4.059  1.00 53.17  ? 25   SER F O   1 
ATOM   5668 C  CB  . SER F 1 25  ? -56.930 70.206  -6.952  1.00 49.34  ? 25   SER F CB  1 
ATOM   5669 O  OG  . SER F 1 25  ? -58.138 70.850  -6.599  1.00 46.68  ? 25   SER F OG  1 
ATOM   5670 N  N   . GLY F 1 26  ? -55.374 67.972  -6.163  1.00 43.76  ? 26   GLY F N   1 
ATOM   5671 C  CA  . GLY F 1 26  ? -55.207 66.596  -5.737  1.00 38.06  ? 26   GLY F CA  1 
ATOM   5672 C  C   . GLY F 1 26  ? -53.749 66.231  -5.576  1.00 42.55  ? 26   GLY F C   1 
ATOM   5673 O  O   . GLY F 1 26  ? -53.355 65.090  -5.798  1.00 41.26  ? 26   GLY F O   1 
ATOM   5674 N  N   . GLU F 1 27  ? -52.942 67.205  -5.181  1.00 41.86  ? 27   GLU F N   1 
ATOM   5675 C  CA  . GLU F 1 27  ? -51.510 66.980  -5.059  1.00 44.79  ? 27   GLU F CA  1 
ATOM   5676 C  C   . GLU F 1 27  ? -51.134 66.631  -3.624  1.00 41.03  ? 27   GLU F C   1 
ATOM   5677 O  O   . GLU F 1 27  ? -51.907 66.889  -2.698  1.00 41.14  ? 27   GLU F O   1 
ATOM   5678 C  CB  . GLU F 1 27  ? -50.749 68.198  -5.582  1.00 49.08  ? 27   GLU F CB  1 
ATOM   5679 C  CG  . GLU F 1 27  ? -51.126 68.518  -7.030  1.00 54.75  ? 27   GLU F CG  1 
ATOM   5680 C  CD  . GLU F 1 27  ? -50.136 69.430  -7.731  1.00 68.15  ? 27   GLU F CD  1 
ATOM   5681 O  OE1 . GLU F 1 27  ? -49.880 70.548  -7.219  1.00 66.78  ? 27   GLU F OE1 1 
ATOM   5682 O  OE2 . GLU F 1 27  ? -49.625 69.025  -8.805  1.00 75.39  ? 27   GLU F OE2 1 
ATOM   5683 N  N   . PRO F 1 28  ? -49.954 66.023  -3.430  1.00 37.69  ? 28   PRO F N   1 
ATOM   5684 C  CA  . PRO F 1 28  ? -49.647 65.523  -2.080  1.00 40.26  ? 28   PRO F CA  1 
ATOM   5685 C  C   . PRO F 1 28  ? -49.748 66.608  -0.995  1.00 35.41  ? 28   PRO F C   1 
ATOM   5686 O  O   . PRO F 1 28  ? -49.557 67.776  -1.269  1.00 33.61  ? 28   PRO F O   1 
ATOM   5687 C  CB  . PRO F 1 28  ? -48.218 64.983  -2.215  1.00 36.87  ? 28   PRO F CB  1 
ATOM   5688 C  CG  . PRO F 1 28  ? -48.060 64.694  -3.667  1.00 35.09  ? 28   PRO F CG  1 
ATOM   5689 C  CD  . PRO F 1 28  ? -48.900 65.694  -4.402  1.00 32.94  ? 28   PRO F CD  1 
ATOM   5690 N  N   . VAL F 1 29  ? -50.102 66.208  0.218   1.00 35.37  ? 29   VAL F N   1 
ATOM   5691 C  CA  . VAL F 1 29  ? -50.151 67.132  1.331   1.00 33.79  ? 29   VAL F CA  1 
ATOM   5692 C  C   . VAL F 1 29  ? -48.890 66.938  2.147   1.00 34.74  ? 29   VAL F C   1 
ATOM   5693 O  O   . VAL F 1 29  ? -48.543 65.812  2.506   1.00 35.06  ? 29   VAL F O   1 
ATOM   5694 C  CB  . VAL F 1 29  ? -51.376 66.890  2.210   1.00 31.55  ? 29   VAL F CB  1 
ATOM   5695 C  CG1 . VAL F 1 29  ? -51.345 67.804  3.454   1.00 28.16  ? 29   VAL F CG1 1 
ATOM   5696 C  CG2 . VAL F 1 29  ? -52.652 67.092  1.392   1.00 30.38  ? 29   VAL F CG2 1 
ATOM   5697 N  N   . VAL F 1 30  ? -48.194 68.035  2.413   1.00 32.59  ? 30   VAL F N   1 
ATOM   5698 C  CA  . VAL F 1 30  ? -46.972 67.988  3.196   1.00 32.59  ? 30   VAL F CA  1 
ATOM   5699 C  C   . VAL F 1 30  ? -47.269 68.365  4.637   1.00 31.61  ? 30   VAL F C   1 
ATOM   5700 O  O   . VAL F 1 30  ? -47.841 69.423  4.923   1.00 37.54  ? 30   VAL F O   1 
ATOM   5701 C  CB  . VAL F 1 30  ? -45.861 68.926  2.606   1.00 33.03  ? 30   VAL F CB  1 
ATOM   5702 C  CG1 . VAL F 1 30  ? -44.667 69.025  3.556   1.00 31.64  ? 30   VAL F CG1 1 
ATOM   5703 C  CG2 . VAL F 1 30  ? -45.424 68.445  1.253   1.00 31.80  ? 30   VAL F CG2 1 
ATOM   5704 N  N   . LEU F 1 31  ? -46.885 67.488  5.553   1.00 34.99  ? 31   LEU F N   1 
ATOM   5705 C  CA  . LEU F 1 31  ? -47.117 67.733  6.968   1.00 39.05  ? 31   LEU F CA  1 
ATOM   5706 C  C   . LEU F 1 31  ? -45.815 68.067  7.668   1.00 39.48  ? 31   LEU F C   1 
ATOM   5707 O  O   . LEU F 1 31  ? -44.747 67.561  7.298   1.00 42.74  ? 31   LEU F O   1 
ATOM   5708 C  CB  . LEU F 1 31  ? -47.731 66.509  7.649   1.00 36.21  ? 31   LEU F CB  1 
ATOM   5709 C  CG  . LEU F 1 31  ? -49.179 66.098  7.421   1.00 39.38  ? 31   LEU F CG  1 
ATOM   5710 C  CD1 . LEU F 1 31  ? -49.271 65.184  6.198   1.00 37.96  ? 31   LEU F CD1 1 
ATOM   5711 C  CD2 . LEU F 1 31  ? -49.681 65.380  8.668   1.00 35.40  ? 31   LEU F CD2 1 
ATOM   5712 N  N   . SER F 1 32  ? -45.907 68.891  8.703   1.00 34.11  ? 32   SER F N   1 
ATOM   5713 C  CA  . SER F 1 32  ? -44.735 69.190  9.507   1.00 38.04  ? 32   SER F CA  1 
ATOM   5714 C  C   . SER F 1 32  ? -45.154 69.891  10.768  1.00 34.85  ? 32   SER F C   1 
ATOM   5715 O  O   . SER F 1 32  ? -46.225 70.469  10.832  1.00 37.70  ? 32   SER F O   1 
ATOM   5716 C  CB  . SER F 1 32  ? -43.767 70.078  8.734   1.00 38.21  ? 32   SER F CB  1 
ATOM   5717 O  OG  . SER F 1 32  ? -44.379 71.323  8.457   1.00 43.74  ? 32   SER F OG  1 
ATOM   5718 N  N   . GLY F 1 33  ? -44.289 69.863  11.767  1.00 34.68  ? 33   GLY F N   1 
ATOM   5719 C  CA  . GLY F 1 33  ? -44.615 70.444  13.051  1.00 36.97  ? 33   GLY F CA  1 
ATOM   5720 C  C   . GLY F 1 33  ? -43.960 69.635  14.142  1.00 35.81  ? 33   GLY F C   1 
ATOM   5721 O  O   . GLY F 1 33  ? -43.075 68.833  13.888  1.00 39.00  ? 33   GLY F O   1 
ATOM   5722 N  N   . GLN F 1 34  ? -44.401 69.821  15.369  1.00 41.33  ? 34   GLN F N   1 
ATOM   5723 C  CA  . GLN F 1 34  ? -43.728 69.149  16.458  1.00 42.45  ? 34   GLN F CA  1 
ATOM   5724 C  C   . GLN F 1 34  ? -44.709 68.701  17.505  1.00 36.29  ? 34   GLN F C   1 
ATOM   5725 O  O   . GLN F 1 34  ? -45.653 69.405  17.815  1.00 40.97  ? 34   GLN F O   1 
ATOM   5726 C  CB  . GLN F 1 34  ? -42.661 70.060  17.066  1.00 42.91  ? 34   GLN F CB  1 
ATOM   5727 C  CG  . GLN F 1 34  ? -41.881 69.413  18.183  1.00 49.31  ? 34   GLN F CG  1 
ATOM   5728 C  CD  . GLN F 1 34  ? -40.906 70.371  18.848  1.00 55.57  ? 34   GLN F CD  1 
ATOM   5729 O  OE1 . GLN F 1 34  ? -41.253 71.057  19.811  1.00 53.87  ? 34   GLN F OE1 1 
ATOM   5730 N  NE2 . GLN F 1 34  ? -39.680 70.420  18.334  1.00 58.98  ? 34   GLN F NE2 1 
ATOM   5731 N  N   . ILE F 1 35  ? -44.494 67.506  18.024  1.00 35.21  ? 35   ILE F N   1 
ATOM   5732 C  CA  . ILE F 1 35  ? -45.267 67.023  19.148  1.00 38.27  ? 35   ILE F CA  1 
ATOM   5733 C  C   . ILE F 1 35  ? -44.267 66.790  20.268  1.00 41.75  ? 35   ILE F C   1 
ATOM   5734 O  O   . ILE F 1 35  ? -43.100 66.490  19.998  1.00 41.92  ? 35   ILE F O   1 
ATOM   5735 C  CB  . ILE F 1 35  ? -46.012 65.721  18.799  1.00 38.35  ? 35   ILE F CB  1 
ATOM   5736 C  CG1 . ILE F 1 35  ? -46.537 65.776  17.357  1.00 37.71  ? 35   ILE F CG1 1 
ATOM   5737 C  CG2 . ILE F 1 35  ? -47.131 65.472  19.780  1.00 37.38  ? 35   ILE F CG2 1 
ATOM   5738 C  CD1 . ILE F 1 35  ? -47.366 64.580  16.945  1.00 31.78  ? 35   ILE F CD1 1 
ATOM   5739 N  N   . THR F 1 36  ? -44.710 66.962  21.513  1.00 39.92  ? 36   THR F N   1 
ATOM   5740 C  CA  . THR F 1 36  ? -43.829 66.843  22.674  1.00 40.18  ? 36   THR F CA  1 
ATOM   5741 C  C   . THR F 1 36  ? -44.530 65.997  23.716  1.00 37.26  ? 36   THR F C   1 
ATOM   5742 O  O   . THR F 1 36  ? -45.684 65.648  23.535  1.00 41.18  ? 36   THR F O   1 
ATOM   5743 C  CB  . THR F 1 36  ? -43.409 68.246  23.276  1.00 41.95  ? 36   THR F CB  1 
ATOM   5744 O  OG1 . THR F 1 36  ? -44.550 68.947  23.790  1.00 43.96  ? 36   THR F OG1 1 
ATOM   5745 C  CG2 . THR F 1 36  ? -42.741 69.115  22.236  1.00 40.79  ? 36   THR F CG2 1 
ATOM   5746 N  N   . GLY F 1 37  ? -43.843 65.655  24.801  1.00 37.52  ? 37   GLY F N   1 
ATOM   5747 C  CA  . GLY F 1 37  ? -44.468 64.890  25.872  1.00 42.27  ? 37   GLY F CA  1 
ATOM   5748 C  C   . GLY F 1 37  ? -44.694 63.402  25.610  1.00 40.65  ? 37   GLY F C   1 
ATOM   5749 O  O   . GLY F 1 37  ? -45.459 62.743  26.321  1.00 45.35  ? 37   GLY F O   1 
ATOM   5750 N  N   . LEU F 1 38  ? -44.013 62.858  24.608  1.00 40.96  ? 38   LEU F N   1 
ATOM   5751 C  CA  . LEU F 1 38  ? -44.234 61.477  24.192  1.00 38.69  ? 38   LEU F CA  1 
ATOM   5752 C  C   . LEU F 1 38  ? -43.156 60.543  24.708  1.00 39.13  ? 38   LEU F C   1 
ATOM   5753 O  O   . LEU F 1 38  ? -42.028 60.964  24.979  1.00 42.61  ? 38   LEU F O   1 
ATOM   5754 C  CB  . LEU F 1 38  ? -44.251 61.383  22.661  1.00 40.02  ? 38   LEU F CB  1 
ATOM   5755 C  CG  . LEU F 1 38  ? -45.481 61.882  21.909  1.00 37.90  ? 38   LEU F CG  1 
ATOM   5756 C  CD1 . LEU F 1 38  ? -45.211 61.944  20.413  1.00 32.55  ? 38   LEU F CD1 1 
ATOM   5757 C  CD2 . LEU F 1 38  ? -46.695 61.010  22.222  1.00 35.96  ? 38   LEU F CD2 1 
ATOM   5758 N  N   . THR F 1 39  ? -43.495 59.262  24.808  1.00 37.15  ? 39   THR F N   1 
ATOM   5759 C  CA  . THR F 1 39  ? -42.496 58.237  25.087  1.00 34.37  ? 39   THR F CA  1 
ATOM   5760 C  C   . THR F 1 39  ? -41.604 58.112  23.863  1.00 40.03  ? 39   THR F C   1 
ATOM   5761 O  O   . THR F 1 39  ? -42.070 58.292  22.734  1.00 41.07  ? 39   THR F O   1 
ATOM   5762 C  CB  . THR F 1 39  ? -43.176 56.909  25.347  1.00 35.89  ? 39   THR F CB  1 
ATOM   5763 O  OG1 . THR F 1 39  ? -44.141 56.686  24.320  1.00 35.90  ? 39   THR F OG1 1 
ATOM   5764 C  CG2 . THR F 1 39  ? -43.907 56.951  26.671  1.00 26.08  ? 39   THR F CG2 1 
ATOM   5765 N  N   . GLU F 1 40  ? -40.322 57.829  24.058  1.00 39.73  ? 40   GLU F N   1 
ATOM   5766 C  CA  . GLU F 1 40  ? -39.445 57.719  22.911  1.00 36.98  ? 40   GLU F CA  1 
ATOM   5767 C  C   . GLU F 1 40  ? -39.980 56.590  22.038  1.00 36.69  ? 40   GLU F C   1 
ATOM   5768 O  O   . GLU F 1 40  ? -40.538 55.615  22.543  1.00 38.08  ? 40   GLU F O   1 
ATOM   5769 C  CB  . GLU F 1 40  ? -37.995 57.451  23.325  1.00 38.85  ? 40   GLU F CB  1 
ATOM   5770 C  CG  . GLU F 1 40  ? -37.113 57.089  22.124  1.00 43.87  ? 40   GLU F CG  1 
ATOM   5771 C  CD  . GLU F 1 40  ? -35.608 57.067  22.407  1.00 51.21  ? 40   GLU F CD  1 
ATOM   5772 O  OE1 . GLU F 1 40  ? -35.190 56.876  23.578  1.00 51.80  ? 40   GLU F OE1 1 
ATOM   5773 O  OE2 . GLU F 1 40  ? -34.844 57.226  21.427  1.00 47.50  ? 40   GLU F OE2 1 
ATOM   5774 N  N   . GLY F 1 41  ? -39.830 56.717  20.727  1.00 35.50  ? 41   GLY F N   1 
ATOM   5775 C  CA  . GLY F 1 41  ? -40.283 55.665  19.835  1.00 33.79  ? 41   GLY F CA  1 
ATOM   5776 C  C   . GLY F 1 41  ? -41.361 56.077  18.851  1.00 35.45  ? 41   GLY F C   1 
ATOM   5777 O  O   . GLY F 1 41  ? -41.606 57.271  18.638  1.00 33.09  ? 41   GLY F O   1 
ATOM   5778 N  N   . GLN F 1 42  ? -42.001 55.076  18.249  1.00 33.54  ? 42   GLN F N   1 
ATOM   5779 C  CA  . GLN F 1 42  ? -43.020 55.307  17.234  1.00 31.36  ? 42   GLN F CA  1 
ATOM   5780 C  C   . GLN F 1 42  ? -44.443 55.396  17.783  1.00 31.99  ? 42   GLN F C   1 
ATOM   5781 O  O   . GLN F 1 42  ? -44.821 54.627  18.669  1.00 30.50  ? 42   GLN F O   1 
ATOM   5782 C  CB  . GLN F 1 42  ? -42.932 54.256  16.139  1.00 26.55  ? 42   GLN F CB  1 
ATOM   5783 C  CG  . GLN F 1 42  ? -41.859 54.576  15.116  1.00 30.11  ? 42   GLN F CG  1 
ATOM   5784 C  CD  . GLN F 1 42  ? -41.742 53.520  14.042  1.00 33.64  ? 42   GLN F CD  1 
ATOM   5785 O  OE1 . GLN F 1 42  ? -42.448 52.521  14.073  1.00 36.08  ? 42   GLN F OE1 1 
ATOM   5786 N  NE2 . GLN F 1 42  ? -40.846 53.737  13.079  1.00 35.79  ? 42   GLN F NE2 1 
ATOM   5787 N  N   . HIS F 1 43  ? -45.220 56.349  17.259  1.00 27.65  ? 43   HIS F N   1 
ATOM   5788 C  CA  . HIS F 1 43  ? -46.620 56.494  17.656  1.00 31.36  ? 43   HIS F CA  1 
ATOM   5789 C  C   . HIS F 1 43  ? -47.591 56.567  16.489  1.00 25.95  ? 43   HIS F C   1 
ATOM   5790 O  O   . HIS F 1 43  ? -47.402 57.353  15.576  1.00 25.97  ? 43   HIS F O   1 
ATOM   5791 C  CB  . HIS F 1 43  ? -46.795 57.715  18.550  1.00 29.60  ? 43   HIS F CB  1 
ATOM   5792 C  CG  . HIS F 1 43  ? -46.100 57.587  19.864  1.00 32.61  ? 43   HIS F CG  1 
ATOM   5793 N  ND1 . HIS F 1 43  ? -46.725 57.100  20.988  1.00 32.34  ? 43   HIS F ND1 1 
ATOM   5794 C  CD2 . HIS F 1 43  ? -44.825 57.859  20.227  1.00 34.27  ? 43   HIS F CD2 1 
ATOM   5795 C  CE1 . HIS F 1 43  ? -45.871 57.089  21.992  1.00 32.51  ? 43   HIS F CE1 1 
ATOM   5796 N  NE2 . HIS F 1 43  ? -44.708 57.539  21.555  1.00 35.22  ? 43   HIS F NE2 1 
ATOM   5797 N  N   . GLY F 1 44  ? -48.632 55.743  16.537  1.00 25.35  ? 44   GLY F N   1 
ATOM   5798 C  CA  . GLY F 1 44  ? -49.650 55.756  15.509  1.00 26.60  ? 44   GLY F CA  1 
ATOM   5799 C  C   . GLY F 1 44  ? -50.085 57.193  15.307  1.00 29.42  ? 44   GLY F C   1 
ATOM   5800 O  O   . GLY F 1 44  ? -50.187 57.959  16.283  1.00 28.42  ? 44   GLY F O   1 
ATOM   5801 N  N   . PHE F 1 45  ? -50.331 57.558  14.053  1.00 23.13  ? 45   PHE F N   1 
ATOM   5802 C  CA  . PHE F 1 45  ? -50.611 58.942  13.683  1.00 29.78  ? 45   PHE F CA  1 
ATOM   5803 C  C   . PHE F 1 45  ? -51.679 58.986  12.592  1.00 27.60  ? 45   PHE F C   1 
ATOM   5804 O  O   . PHE F 1 45  ? -51.383 58.739  11.415  1.00 28.33  ? 45   PHE F O   1 
ATOM   5805 C  CB  . PHE F 1 45  ? -49.322 59.597  13.184  1.00 29.05  ? 45   PHE F CB  1 
ATOM   5806 C  CG  . PHE F 1 45  ? -49.401 61.098  13.043  1.00 28.01  ? 45   PHE F CG  1 
ATOM   5807 C  CD1 . PHE F 1 45  ? -49.682 61.896  14.130  1.00 27.69  ? 45   PHE F CD1 1 
ATOM   5808 C  CD2 . PHE F 1 45  ? -49.126 61.709  11.829  1.00 28.29  ? 45   PHE F CD2 1 
ATOM   5809 C  CE1 . PHE F 1 45  ? -49.716 63.277  14.008  1.00 30.22  ? 45   PHE F CE1 1 
ATOM   5810 C  CE2 . PHE F 1 45  ? -49.162 63.091  11.705  1.00 31.75  ? 45   PHE F CE2 1 
ATOM   5811 C  CZ  . PHE F 1 45  ? -49.461 63.871  12.792  1.00 30.01  ? 45   PHE F CZ  1 
ATOM   5812 N  N   . HIS F 1 46  ? -52.914 59.294  12.971  1.00 26.83  ? 46   HIS F N   1 
ATOM   5813 C  CA  . HIS F 1 46  ? -54.039 59.096  12.056  1.00 26.09  ? 46   HIS F CA  1 
ATOM   5814 C  C   . HIS F 1 46  ? -54.988 60.275  11.967  1.00 27.79  ? 46   HIS F C   1 
ATOM   5815 O  O   . HIS F 1 46  ? -55.189 61.002  12.940  1.00 29.28  ? 46   HIS F O   1 
ATOM   5816 C  CB  . HIS F 1 46  ? -54.846 57.864  12.476  1.00 25.61  ? 46   HIS F CB  1 
ATOM   5817 C  CG  . HIS F 1 46  ? -54.006 56.672  12.780  1.00 25.86  ? 46   HIS F CG  1 
ATOM   5818 N  ND1 . HIS F 1 46  ? -53.361 55.947  11.798  1.00 30.74  ? 46   HIS F ND1 1 
ATOM   5819 C  CD2 . HIS F 1 46  ? -53.684 56.088  13.955  1.00 26.86  ? 46   HIS F CD2 1 
ATOM   5820 C  CE1 . HIS F 1 46  ? -52.682 54.960  12.359  1.00 29.39  ? 46   HIS F CE1 1 
ATOM   5821 N  NE2 . HIS F 1 46  ? -52.864 55.020  13.666  1.00 29.69  ? 46   HIS F NE2 1 
ATOM   5822 N  N   . VAL F 1 47  ? -55.598 60.444  10.799  1.00 26.34  ? 47   VAL F N   1 
ATOM   5823 C  CA  . VAL F 1 47  ? -56.747 61.323  10.691  1.00 29.77  ? 47   VAL F CA  1 
ATOM   5824 C  C   . VAL F 1 47  ? -58.014 60.516  10.963  1.00 28.14  ? 47   VAL F C   1 
ATOM   5825 O  O   . VAL F 1 47  ? -58.238 59.493  10.332  1.00 26.75  ? 47   VAL F O   1 
ATOM   5826 C  CB  . VAL F 1 47  ? -56.840 61.975  9.313   1.00 31.88  ? 47   VAL F CB  1 
ATOM   5827 C  CG1 . VAL F 1 47  ? -58.033 62.915  9.265   1.00 27.52  ? 47   VAL F CG1 1 
ATOM   5828 C  CG2 . VAL F 1 47  ? -55.554 62.726  9.009   1.00 26.29  ? 47   VAL F CG2 1 
ATOM   5829 N  N   . HIS F 1 48  ? -58.823 60.976  11.913  1.00 26.44  ? 48   HIS F N   1 
ATOM   5830 C  CA  . HIS F 1 48  ? -60.063 60.290  12.281  1.00 27.53  ? 48   HIS F CA  1 
ATOM   5831 C  C   . HIS F 1 48  ? -61.284 60.961  11.677  1.00 29.67  ? 48   HIS F C   1 
ATOM   5832 O  O   . HIS F 1 48  ? -61.281 62.162  11.384  1.00 29.30  ? 48   HIS F O   1 
ATOM   5833 C  CB  . HIS F 1 48  ? -60.209 60.196  13.806  1.00 29.02  ? 48   HIS F CB  1 
ATOM   5834 C  CG  . HIS F 1 48  ? -59.305 59.180  14.441  1.00 28.00  ? 48   HIS F CG  1 
ATOM   5835 N  ND1 . HIS F 1 48  ? -59.782 58.092  15.138  1.00 25.68  ? 48   HIS F ND1 1 
ATOM   5836 C  CD2 . HIS F 1 48  ? -57.952 59.090  14.484  1.00 28.58  ? 48   HIS F CD2 1 
ATOM   5837 C  CE1 . HIS F 1 48  ? -58.767 57.369  15.575  1.00 26.41  ? 48   HIS F CE1 1 
ATOM   5838 N  NE2 . HIS F 1 48  ? -57.645 57.956  15.199  1.00 28.65  ? 48   HIS F NE2 1 
ATOM   5839 N  N   . GLN F 1 49  ? -62.338 60.176  11.505  1.00 30.01  ? 49   GLN F N   1 
ATOM   5840 C  CA  . GLN F 1 49  ? -63.497 60.618  10.757  1.00 28.96  ? 49   GLN F CA  1 
ATOM   5841 C  C   . GLN F 1 49  ? -64.069 61.995  11.148  1.00 31.00  ? 49   GLN F C   1 
ATOM   5842 O  O   . GLN F 1 49  ? -64.165 62.869  10.292  1.00 29.65  ? 49   GLN F O   1 
ATOM   5843 C  CB  . GLN F 1 49  ? -64.580 59.541  10.780  1.00 32.02  ? 49   GLN F CB  1 
ATOM   5844 C  CG  . GLN F 1 49  ? -65.804 59.907  9.970   1.00 32.67  ? 49   GLN F CG  1 
ATOM   5845 C  CD  . GLN F 1 49  ? -66.761 58.756  9.836   1.00 38.37  ? 49   GLN F CD  1 
ATOM   5846 O  OE1 . GLN F 1 49  ? -66.566 57.697  10.443  1.00 40.53  ? 49   GLN F OE1 1 
ATOM   5847 N  NE2 . GLN F 1 49  ? -67.800 58.941  9.025   1.00 38.22  ? 49   GLN F NE2 1 
ATOM   5848 N  N   . TYR F 1 50  ? -64.428 62.190  12.424  1.00 31.46  ? 50   TYR F N   1 
ATOM   5849 C  CA  . TYR F 1 50  ? -65.172 63.387  12.852  1.00 28.77  ? 50   TYR F CA  1 
ATOM   5850 C  C   . TYR F 1 50  ? -64.343 64.423  13.630  1.00 35.54  ? 50   TYR F C   1 
ATOM   5851 O  O   . TYR F 1 50  ? -63.444 64.064  14.400  1.00 35.28  ? 50   TYR F O   1 
ATOM   5852 C  CB  . TYR F 1 50  ? -66.377 62.994  13.717  1.00 30.48  ? 50   TYR F CB  1 
ATOM   5853 C  CG  . TYR F 1 50  ? -67.310 61.973  13.104  1.00 35.27  ? 50   TYR F CG  1 
ATOM   5854 C  CD1 . TYR F 1 50  ? -68.031 62.259  11.948  1.00 44.08  ? 50   TYR F CD1 1 
ATOM   5855 C  CD2 . TYR F 1 50  ? -67.481 60.727  13.684  1.00 36.79  ? 50   TYR F CD2 1 
ATOM   5856 C  CE1 . TYR F 1 50  ? -68.886 61.317  11.378  1.00 43.51  ? 50   TYR F CE1 1 
ATOM   5857 C  CE2 . TYR F 1 50  ? -68.332 59.782  13.120  1.00 40.89  ? 50   TYR F CE2 1 
ATOM   5858 C  CZ  . TYR F 1 50  ? -69.029 60.084  11.970  1.00 43.90  ? 50   TYR F CZ  1 
ATOM   5859 O  OH  . TYR F 1 50  ? -69.880 59.151  11.417  1.00 50.49  ? 50   TYR F OH  1 
ATOM   5860 N  N   . GLY F 1 51  ? -64.686 65.702  13.460  1.00 33.69  ? 51   GLY F N   1 
ATOM   5861 C  CA  . GLY F 1 51  ? -64.058 66.788  14.202  1.00 34.28  ? 51   GLY F CA  1 
ATOM   5862 C  C   . GLY F 1 51  ? -64.832 67.130  15.465  1.00 38.00  ? 51   GLY F C   1 
ATOM   5863 O  O   . GLY F 1 51  ? -65.056 68.294  15.809  1.00 38.34  ? 51   GLY F O   1 
ATOM   5864 N  N   . ASP F 1 52  ? -65.246 66.084  16.161  1.00 39.56  ? 52   ASP F N   1 
ATOM   5865 C  CA  . ASP F 1 52  ? -66.110 66.201  17.313  1.00 38.20  ? 52   ASP F CA  1 
ATOM   5866 C  C   . ASP F 1 52  ? -65.302 65.852  18.549  1.00 40.51  ? 52   ASP F C   1 
ATOM   5867 O  O   . ASP F 1 52  ? -64.953 64.686  18.779  1.00 40.74  ? 52   ASP F O   1 
ATOM   5868 C  CB  . ASP F 1 52  ? -67.299 65.246  17.150  1.00 39.69  ? 52   ASP F CB  1 
ATOM   5869 C  CG  . ASP F 1 52  ? -68.189 65.201  18.377  1.00 44.44  ? 52   ASP F CG  1 
ATOM   5870 O  OD1 . ASP F 1 52  ? -67.737 65.614  19.464  1.00 45.92  ? 52   ASP F OD1 1 
ATOM   5871 O  OD2 . ASP F 1 52  ? -69.345 64.751  18.260  1.00 49.31  ? 52   ASP F OD2 1 
ATOM   5872 N  N   . ASN F 1 53  ? -64.984 66.866  19.342  1.00 43.68  ? 53   ASN F N   1 
ATOM   5873 C  CA  . ASN F 1 53  ? -64.159 66.640  20.517  1.00 46.82  ? 53   ASN F CA  1 
ATOM   5874 C  C   . ASN F 1 53  ? -64.950 66.897  21.807  1.00 47.67  ? 53   ASN F C   1 
ATOM   5875 O  O   . ASN F 1 53  ? -64.420 67.408  22.796  1.00 50.94  ? 53   ASN F O   1 
ATOM   5876 C  CB  . ASN F 1 53  ? -62.816 67.403  20.411  1.00 47.10  ? 53   ASN F CB  1 
ATOM   5877 C  CG  . ASN F 1 53  ? -61.854 66.795  19.315  1.00 53.89  ? 53   ASN F CG  1 
ATOM   5878 O  OD1 . ASN F 1 53  ? -62.063 65.664  18.831  1.00 49.15  ? 53   ASN F OD1 1 
ATOM   5879 N  ND2 . ASN F 1 53  ? -60.800 67.547  18.948  1.00 39.13  ? 53   ASN F ND2 1 
ATOM   5880 N  N   . THR F 1 54  ? -66.224 66.501  21.768  1.00 43.05  ? 54   THR F N   1 
ATOM   5881 C  CA  . THR F 1 54  ? -67.164 66.685  22.872  1.00 44.42  ? 54   THR F CA  1 
ATOM   5882 C  C   . THR F 1 54  ? -66.982 65.615  23.947  1.00 49.74  ? 54   THR F C   1 
ATOM   5883 O  O   . THR F 1 54  ? -67.132 65.892  25.137  1.00 49.16  ? 54   THR F O   1 
ATOM   5884 C  CB  . THR F 1 54  ? -68.634 66.651  22.397  1.00 44.71  ? 54   THR F CB  1 
ATOM   5885 O  OG1 . THR F 1 54  ? -68.955 65.346  21.902  1.00 41.55  ? 54   THR F OG1 1 
ATOM   5886 C  CG2 . THR F 1 54  ? -68.892 67.701  21.315  1.00 42.38  ? 54   THR F CG2 1 
ATOM   5887 N  N   . GLN F 1 55  ? -66.668 64.391  23.538  1.00 44.53  ? 55   GLN F N   1 
ATOM   5888 C  CA  . GLN F 1 55  ? -66.205 63.408  24.503  1.00 45.23  ? 55   GLN F CA  1 
ATOM   5889 C  C   . GLN F 1 55  ? -64.717 63.176  24.335  1.00 44.51  ? 55   GLN F C   1 
ATOM   5890 O  O   . GLN F 1 55  ? -64.273 62.043  24.203  1.00 49.50  ? 55   GLN F O   1 
ATOM   5891 C  CB  . GLN F 1 55  ? -66.967 62.100  24.374  1.00 47.15  ? 55   GLN F CB  1 
ATOM   5892 C  CG  . GLN F 1 55  ? -68.267 62.097  25.141  1.00 54.33  ? 55   GLN F CG  1 
ATOM   5893 C  CD  . GLN F 1 55  ? -69.356 61.319  24.425  1.00 71.83  ? 55   GLN F CD  1 
ATOM   5894 O  OE1 . GLN F 1 55  ? -69.086 60.586  23.462  1.00 71.78  ? 55   GLN F OE1 1 
ATOM   5895 N  NE2 . GLN F 1 55  ? -70.599 61.477  24.887  1.00 69.42  ? 55   GLN F NE2 1 
ATOM   5896 N  N   . GLY F 1 56  ? -63.949 64.261  24.327  1.00 46.69  ? 56   GLY F N   1 
ATOM   5897 C  CA  . GLY F 1 56  ? -62.514 64.185  24.104  1.00 45.14  ? 56   GLY F CA  1 
ATOM   5898 C  C   . GLY F 1 56  ? -62.162 63.583  22.755  1.00 48.41  ? 56   GLY F C   1 
ATOM   5899 O  O   . GLY F 1 56  ? -62.891 63.750  21.767  1.00 49.30  ? 56   GLY F O   1 
ATOM   5900 N  N   . CYS F 1 57  ? -61.041 62.870  22.721  1.00 44.20  ? 57   CYS F N   1 
ATOM   5901 C  CA  . CYS F 1 57  ? -60.520 62.274  21.493  1.00 39.11  ? 57   CYS F CA  1 
ATOM   5902 C  C   . CYS F 1 57  ? -61.350 61.097  20.995  1.00 38.26  ? 57   CYS F C   1 
ATOM   5903 O  O   . CYS F 1 57  ? -61.305 60.747  19.817  1.00 37.76  ? 57   CYS F O   1 
ATOM   5904 C  CB  . CYS F 1 57  ? -59.076 61.832  21.710  1.00 38.85  ? 57   CYS F CB  1 
ATOM   5905 S  SG  . CYS F 1 57  ? -57.961 63.225  21.778  1.00 49.43  ? 57   CYS F SG  1 
ATOM   5906 N  N   . THR F 1 58  ? -62.134 60.503  21.884  1.00 41.09  ? 58   THR F N   1 
ATOM   5907 C  CA  . THR F 1 58  ? -62.836 59.272  21.546  1.00 38.44  ? 58   THR F CA  1 
ATOM   5908 C  C   . THR F 1 58  ? -64.058 59.471  20.652  1.00 36.52  ? 58   THR F C   1 
ATOM   5909 O  O   . THR F 1 58  ? -64.509 58.538  20.009  1.00 39.16  ? 58   THR F O   1 
ATOM   5910 C  CB  . THR F 1 58  ? -63.235 58.475  22.791  1.00 39.97  ? 58   THR F CB  1 
ATOM   5911 O  OG1 . THR F 1 58  ? -64.632 58.170  22.724  1.00 41.76  ? 58   THR F OG1 1 
ATOM   5912 C  CG2 . THR F 1 58  ? -62.924 59.259  24.066  1.00 42.71  ? 58   THR F CG2 1 
ATOM   5913 N  N   . SER F 1 59  ? -64.583 60.684  20.597  1.00 40.96  ? 59   SER F N   1 
ATOM   5914 C  CA  . SER F 1 59  ? -65.748 60.953  19.764  1.00 38.58  ? 59   SER F CA  1 
ATOM   5915 C  C   . SER F 1 59  ? -65.365 61.506  18.385  1.00 36.67  ? 59   SER F C   1 
ATOM   5916 O  O   . SER F 1 59  ? -66.228 61.876  17.606  1.00 35.19  ? 59   SER F O   1 
ATOM   5917 C  CB  . SER F 1 59  ? -66.707 61.895  20.490  1.00 41.53  ? 59   SER F CB  1 
ATOM   5918 O  OG  . SER F 1 59  ? -66.034 63.072  20.895  1.00 43.26  ? 59   SER F OG  1 
ATOM   5919 N  N   . ALA F 1 60  ? -64.066 61.562  18.098  1.00 38.02  ? 60   ALA F N   1 
ATOM   5920 C  CA  . ALA F 1 60  ? -63.567 61.789  16.736  1.00 34.39  ? 60   ALA F CA  1 
ATOM   5921 C  C   . ALA F 1 60  ? -63.917 60.615  15.806  1.00 33.82  ? 60   ALA F C   1 
ATOM   5922 O  O   . ALA F 1 60  ? -63.930 60.754  14.572  1.00 35.86  ? 60   ALA F O   1 
ATOM   5923 C  CB  . ALA F 1 60  ? -62.045 62.008  16.757  1.00 32.12  ? 60   ALA F CB  1 
ATOM   5924 N  N   . GLY F 1 61  ? -64.192 59.459  16.404  1.00 34.08  ? 61   GLY F N   1 
ATOM   5925 C  CA  . GLY F 1 61  ? -64.573 58.272  15.663  1.00 31.94  ? 61   GLY F CA  1 
ATOM   5926 C  C   . GLY F 1 61  ? -63.365 57.455  15.254  1.00 31.76  ? 61   GLY F C   1 
ATOM   5927 O  O   . GLY F 1 61  ? -62.272 57.620  15.810  1.00 29.19  ? 61   GLY F O   1 
ATOM   5928 N  N   . PRO F 1 62  ? -63.552 56.582  14.256  1.00 30.42  ? 62   PRO F N   1 
ATOM   5929 C  CA  . PRO F 1 62  ? -62.532 55.681  13.708  1.00 30.48  ? 62   PRO F CA  1 
ATOM   5930 C  C   . PRO F 1 62  ? -61.696 56.417  12.669  1.00 27.87  ? 62   PRO F C   1 
ATOM   5931 O  O   . PRO F 1 62  ? -61.970 57.586  12.370  1.00 27.10  ? 62   PRO F O   1 
ATOM   5932 C  CB  . PRO F 1 62  ? -63.363 54.598  13.020  1.00 25.80  ? 62   PRO F CB  1 
ATOM   5933 C  CG  . PRO F 1 62  ? -64.726 55.240  12.788  1.00 31.22  ? 62   PRO F CG  1 
ATOM   5934 C  CD  . PRO F 1 62  ? -64.763 56.589  13.426  1.00 27.44  ? 62   PRO F CD  1 
ATOM   5935 N  N   . HIS F 1 63  ? -60.697 55.753  12.106  1.00 25.54  ? 63   HIS F N   1 
ATOM   5936 C  CA  . HIS F 1 63  ? -59.934 56.408  11.047  1.00 28.22  ? 63   HIS F CA  1 
ATOM   5937 C  C   . HIS F 1 63  ? -60.890 56.846  9.945   1.00 29.47  ? 63   HIS F C   1 
ATOM   5938 O  O   . HIS F 1 63  ? -61.872 56.164  9.664   1.00 25.32  ? 63   HIS F O   1 
ATOM   5939 C  CB  . HIS F 1 63  ? -58.859 55.488  10.486  1.00 25.33  ? 63   HIS F CB  1 
ATOM   5940 C  CG  . HIS F 1 63  ? -57.903 54.991  11.518  1.00 27.58  ? 63   HIS F CG  1 
ATOM   5941 N  ND1 . HIS F 1 63  ? -57.019 53.968  11.281  1.00 24.33  ? 63   HIS F ND1 1 
ATOM   5942 C  CD2 . HIS F 1 63  ? -57.680 55.390  12.792  1.00 24.94  ? 63   HIS F CD2 1 
ATOM   5943 C  CE1 . HIS F 1 63  ? -56.300 53.746  12.361  1.00 22.78  ? 63   HIS F CE1 1 
ATOM   5944 N  NE2 . HIS F 1 63  ? -56.677 54.598  13.290  1.00 27.23  ? 63   HIS F NE2 1 
ATOM   5945 N  N   . PHE F 1 64  ? -60.622 58.012  9.367   1.00 26.69  ? 64   PHE F N   1 
ATOM   5946 C  CA  . PHE F 1 64  ? -61.360 58.477  8.211   1.00 27.91  ? 64   PHE F CA  1 
ATOM   5947 C  C   . PHE F 1 64  ? -61.247 57.416  7.122   1.00 26.87  ? 64   PHE F C   1 
ATOM   5948 O  O   . PHE F 1 64  ? -60.156 57.003  6.765   1.00 25.85  ? 64   PHE F O   1 
ATOM   5949 C  CB  . PHE F 1 64  ? -60.782 59.812  7.732   1.00 28.75  ? 64   PHE F CB  1 
ATOM   5950 C  CG  . PHE F 1 64  ? -61.489 60.387  6.535   1.00 29.07  ? 64   PHE F CG  1 
ATOM   5951 C  CD1 . PHE F 1 64  ? -62.875 60.377  6.459   1.00 28.96  ? 64   PHE F CD1 1 
ATOM   5952 C  CD2 . PHE F 1 64  ? -60.771 60.964  5.508   1.00 26.38  ? 64   PHE F CD2 1 
ATOM   5953 C  CE1 . PHE F 1 64  ? -63.533 60.920  5.363   1.00 31.01  ? 64   PHE F CE1 1 
ATOM   5954 C  CE2 . PHE F 1 64  ? -61.420 61.522  4.422   1.00 29.66  ? 64   PHE F CE2 1 
ATOM   5955 C  CZ  . PHE F 1 64  ? -62.806 61.490  4.347   1.00 31.35  ? 64   PHE F CZ  1 
ATOM   5956 N  N   . ASN F 1 65  ? -62.375 56.969  6.596   1.00 27.51  ? 65   ASN F N   1 
ATOM   5957 C  CA  . ASN F 1 65  ? -62.365 55.775  5.757   1.00 28.92  ? 65   ASN F CA  1 
ATOM   5958 C  C   . ASN F 1 65  ? -63.518 55.715  4.770   1.00 30.89  ? 65   ASN F C   1 
ATOM   5959 O  O   . ASN F 1 65  ? -64.309 54.783  4.778   1.00 32.40  ? 65   ASN F O   1 
ATOM   5960 C  CB  . ASN F 1 65  ? -62.401 54.543  6.641   1.00 27.41  ? 65   ASN F CB  1 
ATOM   5961 C  CG  . ASN F 1 65  ? -62.183 53.292  5.873   1.00 32.12  ? 65   ASN F CG  1 
ATOM   5962 O  OD1 . ASN F 1 65  ? -61.683 53.326  4.746   1.00 31.72  ? 65   ASN F OD1 1 
ATOM   5963 N  ND2 . ASN F 1 65  ? -62.563 52.158  6.464   1.00 31.17  ? 65   ASN F ND2 1 
ATOM   5964 N  N   . PRO F 1 66  ? -63.603 56.709  3.899   1.00 29.56  ? 66   PRO F N   1 
ATOM   5965 C  CA  . PRO F 1 66  ? -64.750 56.866  2.999   1.00 31.31  ? 66   PRO F CA  1 
ATOM   5966 C  C   . PRO F 1 66  ? -64.930 55.661  2.078   1.00 34.69  ? 66   PRO F C   1 
ATOM   5967 O  O   . PRO F 1 66  ? -66.046 55.378  1.664   1.00 40.25  ? 66   PRO F O   1 
ATOM   5968 C  CB  . PRO F 1 66  ? -64.386 58.088  2.164   1.00 32.53  ? 66   PRO F CB  1 
ATOM   5969 C  CG  . PRO F 1 66  ? -63.260 58.753  2.879   1.00 36.87  ? 66   PRO F CG  1 
ATOM   5970 C  CD  . PRO F 1 66  ? -62.554 57.714  3.680   1.00 29.91  ? 66   PRO F CD  1 
ATOM   5971 N  N   . HIS F 1 67  ? -63.854 54.956  1.766   1.00 32.77  ? 67   HIS F N   1 
ATOM   5972 C  CA  . HIS F 1 67  ? -63.945 53.822  0.852   1.00 31.93  ? 67   HIS F CA  1 
ATOM   5973 C  C   . HIS F 1 67  ? -64.019 52.471  1.563   1.00 34.19  ? 67   HIS F C   1 
ATOM   5974 O  O   . HIS F 1 67  ? -63.830 51.426  0.942   1.00 31.54  ? 67   HIS F O   1 
ATOM   5975 C  CB  . HIS F 1 67  ? -62.782 53.851  -0.139  1.00 29.69  ? 67   HIS F CB  1 
ATOM   5976 C  CG  . HIS F 1 67  ? -62.597 55.185  -0.785  1.00 34.89  ? 67   HIS F CG  1 
ATOM   5977 N  ND1 . HIS F 1 67  ? -63.617 55.835  -1.447  1.00 38.94  ? 67   HIS F ND1 1 
ATOM   5978 C  CD2 . HIS F 1 67  ? -61.527 56.007  -0.846  1.00 34.29  ? 67   HIS F CD2 1 
ATOM   5979 C  CE1 . HIS F 1 67  ? -63.180 56.997  -1.893  1.00 36.87  ? 67   HIS F CE1 1 
ATOM   5980 N  NE2 . HIS F 1 67  ? -61.915 57.127  -1.542  1.00 39.25  ? 67   HIS F NE2 1 
ATOM   5981 N  N   . SER F 1 68  ? -64.260 52.501  2.869   1.00 33.06  ? 68   SER F N   1 
ATOM   5982 C  CA  . SER F 1 68  ? -64.535 51.285  3.616   1.00 30.98  ? 68   SER F CA  1 
ATOM   5983 C  C   . SER F 1 68  ? -63.477 50.238  3.417   1.00 34.56  ? 68   SER F C   1 
ATOM   5984 O  O   . SER F 1 68  ? -63.822 49.072  3.218   1.00 36.83  ? 68   SER F O   1 
ATOM   5985 C  CB  . SER F 1 68  ? -65.883 50.687  3.191   1.00 30.36  ? 68   SER F CB  1 
ATOM   5986 O  OG  . SER F 1 68  ? -66.934 51.641  3.317   1.00 30.43  ? 68   SER F OG  1 
ATOM   5987 N  N   . LYS F 1 69  ? -62.202 50.635  3.469   1.00 34.85  ? 69   LYS F N   1 
ATOM   5988 C  CA  . LYS F 1 69  ? -61.095 49.679  3.325   1.00 32.29  ? 69   LYS F CA  1 
ATOM   5989 C  C   . LYS F 1 69  ? -60.551 49.206  4.683   1.00 34.25  ? 69   LYS F C   1 
ATOM   5990 O  O   . LYS F 1 69  ? -60.975 49.690  5.742   1.00 33.75  ? 69   LYS F O   1 
ATOM   5991 C  CB  . LYS F 1 69  ? -59.986 50.232  2.396   1.00 30.49  ? 69   LYS F CB  1 
ATOM   5992 C  CG  . LYS F 1 69  ? -60.488 50.473  0.941   1.00 34.90  ? 69   LYS F CG  1 
ATOM   5993 C  CD  . LYS F 1 69  ? -59.406 50.391  -0.149  1.00 44.22  ? 69   LYS F CD  1 
ATOM   5994 C  CE  . LYS F 1 69  ? -58.514 51.663  -0.215  1.00 52.56  ? 69   LYS F CE  1 
ATOM   5995 N  NZ  . LYS F 1 69  ? -57.020 51.388  -0.420  1.00 39.50  ? 69   LYS F NZ  1 
ATOM   5996 N  N   . LYS F 1 70  ? -59.654 48.226  4.662   1.00 32.46  ? 70   LYS F N   1 
ATOM   5997 C  CA  . LYS F 1 70  ? -58.971 47.817  5.887   1.00 32.60  ? 70   LYS F CA  1 
ATOM   5998 C  C   . LYS F 1 70  ? -57.801 48.749  6.161   1.00 31.47  ? 70   LYS F C   1 
ATOM   5999 O  O   . LYS F 1 70  ? -57.244 49.348  5.240   1.00 28.84  ? 70   LYS F O   1 
ATOM   6000 C  CB  . LYS F 1 70  ? -58.455 46.379  5.781   1.00 38.13  ? 70   LYS F CB  1 
ATOM   6001 C  CG  . LYS F 1 70  ? -59.551 45.323  5.678   1.00 42.93  ? 70   LYS F CG  1 
ATOM   6002 C  CD  . LYS F 1 70  ? -58.977 43.898  5.635   1.00 53.52  ? 70   LYS F CD  1 
ATOM   6003 C  CE  . LYS F 1 70  ? -60.089 42.836  5.756   1.00 60.74  ? 70   LYS F CE  1 
ATOM   6004 N  NZ  . LYS F 1 70  ? -60.825 42.908  7.069   1.00 60.98  ? 70   LYS F NZ  1 
ATOM   6005 N  N   . HIS F 1 71  ? -57.425 48.854  7.429   1.00 27.48  ? 71   HIS F N   1 
ATOM   6006 C  CA  . HIS F 1 71  ? -56.294 49.678  7.831   1.00 29.69  ? 71   HIS F CA  1 
ATOM   6007 C  C   . HIS F 1 71  ? -54.963 49.268  7.168   1.00 27.92  ? 71   HIS F C   1 
ATOM   6008 O  O   . HIS F 1 71  ? -54.730 48.100  6.888   1.00 31.08  ? 71   HIS F O   1 
ATOM   6009 C  CB  . HIS F 1 71  ? -56.160 49.633  9.357   1.00 30.87  ? 71   HIS F CB  1 
ATOM   6010 C  CG  . HIS F 1 71  ? -54.947 50.333  9.875   1.00 27.30  ? 71   HIS F CG  1 
ATOM   6011 N  ND1 . HIS F 1 71  ? -54.914 51.690  10.101  1.00 25.40  ? 71   HIS F ND1 1 
ATOM   6012 C  CD2 . HIS F 1 71  ? -53.720 49.866  10.200  1.00 24.70  ? 71   HIS F CD2 1 
ATOM   6013 C  CE1 . HIS F 1 71  ? -53.722 52.029  10.556  1.00 27.04  ? 71   HIS F CE1 1 
ATOM   6014 N  NE2 . HIS F 1 71  ? -52.978 50.939  10.625  1.00 24.88  ? 71   HIS F NE2 1 
ATOM   6015 N  N   . GLY F 1 72  ? -54.079 50.229  6.927   1.00 30.01  ? 72   GLY F N   1 
ATOM   6016 C  CA  . GLY F 1 72  ? -52.742 49.903  6.440   1.00 27.26  ? 72   GLY F CA  1 
ATOM   6017 C  C   . GLY F 1 72  ? -51.714 50.973  6.790   1.00 28.63  ? 72   GLY F C   1 
ATOM   6018 O  O   . GLY F 1 72  ? -52.004 51.913  7.534   1.00 22.48  ? 72   GLY F O   1 
ATOM   6019 N  N   . GLY F 1 73  ? -50.501 50.818  6.271   1.00 24.12  ? 73   GLY F N   1 
ATOM   6020 C  CA  . GLY F 1 73  ? -49.534 51.888  6.329   1.00 27.50  ? 73   GLY F CA  1 
ATOM   6021 C  C   . GLY F 1 73  ? -49.740 52.778  5.116   1.00 32.15  ? 73   GLY F C   1 
ATOM   6022 O  O   . GLY F 1 73  ? -50.336 52.342  4.119   1.00 29.42  ? 73   GLY F O   1 
ATOM   6023 N  N   . PRO F 1 74  ? -49.234 54.019  5.183   1.00 31.99  ? 74   PRO F N   1 
ATOM   6024 C  CA  . PRO F 1 74  ? -49.377 55.055  4.149   1.00 28.90  ? 74   PRO F CA  1 
ATOM   6025 C  C   . PRO F 1 74  ? -49.071 54.518  2.760   1.00 30.44  ? 74   PRO F C   1 
ATOM   6026 O  O   . PRO F 1 74  ? -49.653 54.981  1.781   1.00 32.96  ? 74   PRO F O   1 
ATOM   6027 C  CB  . PRO F 1 74  ? -48.308 56.095  4.516   1.00 28.60  ? 74   PRO F CB  1 
ATOM   6028 C  CG  . PRO F 1 74  ? -47.916 55.837  5.881   1.00 26.81  ? 74   PRO F CG  1 
ATOM   6029 C  CD  . PRO F 1 74  ? -48.368 54.447  6.291   1.00 32.00  ? 74   PRO F CD  1 
ATOM   6030 N  N   . ALA F 1 75  ? -48.158 53.560  2.668   1.00 31.68  ? 75   ALA F N   1 
ATOM   6031 C  CA  . ALA F 1 75  ? -47.677 53.113  1.358   1.00 31.95  ? 75   ALA F CA  1 
ATOM   6032 C  C   . ALA F 1 75  ? -48.401 51.875  0.824   1.00 39.20  ? 75   ALA F C   1 
ATOM   6033 O  O   . ALA F 1 75  ? -48.156 51.440  -0.307  1.00 38.86  ? 75   ALA F O   1 
ATOM   6034 C  CB  . ALA F 1 75  ? -46.165 52.872  1.401   1.00 26.71  ? 75   ALA F CB  1 
ATOM   6035 N  N   . ASP F 1 76  ? -49.274 51.293  1.641   1.00 39.12  ? 76   ASP F N   1 
ATOM   6036 C  CA  . ASP F 1 76  ? -49.989 50.087  1.250   1.00 37.19  ? 76   ASP F CA  1 
ATOM   6037 C  C   . ASP F 1 76  ? -51.112 50.430  0.287   1.00 35.88  ? 76   ASP F C   1 
ATOM   6038 O  O   . ASP F 1 76  ? -51.763 51.474  0.429   1.00 36.25  ? 76   ASP F O   1 
ATOM   6039 C  CB  . ASP F 1 76  ? -50.559 49.388  2.494   1.00 41.23  ? 76   ASP F CB  1 
ATOM   6040 C  CG  . ASP F 1 76  ? -49.518 48.554  3.230   1.00 42.36  ? 76   ASP F CG  1 
ATOM   6041 O  OD1 . ASP F 1 76  ? -48.818 47.762  2.556   1.00 48.22  ? 76   ASP F OD1 1 
ATOM   6042 O  OD2 . ASP F 1 76  ? -49.411 48.673  4.480   1.00 39.40  ? 76   ASP F OD2 1 
ATOM   6043 N  N   . GLU F 1 77  ? -51.353 49.558  -0.689  1.00 43.29  ? 77   GLU F N   1 
ATOM   6044 C  CA  . GLU F 1 77  ? -52.429 49.796  -1.655  1.00 43.11  ? 77   GLU F CA  1 
ATOM   6045 C  C   . GLU F 1 77  ? -53.774 49.769  -0.935  1.00 42.68  ? 77   GLU F C   1 
ATOM   6046 O  O   . GLU F 1 77  ? -54.754 50.380  -1.379  1.00 38.60  ? 77   GLU F O   1 
ATOM   6047 C  CB  . GLU F 1 77  ? -52.418 48.753  -2.776  1.00 45.49  ? 77   GLU F CB  1 
ATOM   6048 C  CG  . GLU F 1 77  ? -52.254 49.345  -4.202  1.00 56.48  ? 77   GLU F CG  1 
ATOM   6049 C  CD  . GLU F 1 77  ? -53.095 50.623  -4.488  1.00 56.11  ? 77   GLU F CD  1 
ATOM   6050 O  OE1 . GLU F 1 77  ? -52.630 51.458  -5.324  1.00 45.50  ? 77   GLU F OE1 1 
ATOM   6051 O  OE2 . GLU F 1 77  ? -54.204 50.792  -3.898  1.00 48.52  ? 77   GLU F OE2 1 
ATOM   6052 N  N   . GLU F 1 78  ? -53.795 49.060  0.190   1.00 39.57  ? 78   GLU F N   1 
ATOM   6053 C  CA  . GLU F 1 78  ? -54.985 48.921  1.023   1.00 38.51  ? 78   GLU F CA  1 
ATOM   6054 C  C   . GLU F 1 78  ? -54.812 49.692  2.329   1.00 32.67  ? 78   GLU F C   1 
ATOM   6055 O  O   . GLU F 1 78  ? -54.007 49.311  3.185   1.00 29.90  ? 78   GLU F O   1 
ATOM   6056 C  CB  . GLU F 1 78  ? -55.206 47.440  1.324   1.00 39.14  ? 78   GLU F CB  1 
ATOM   6057 C  CG  . GLU F 1 78  ? -56.318 47.156  2.295   1.00 44.13  ? 78   GLU F CG  1 
ATOM   6058 C  CD  . GLU F 1 78  ? -57.650 47.025  1.611   1.00 45.51  ? 78   GLU F CD  1 
ATOM   6059 O  OE1 . GLU F 1 78  ? -57.702 47.222  0.374   1.00 50.05  ? 78   GLU F OE1 1 
ATOM   6060 O  OE2 . GLU F 1 78  ? -58.638 46.724  2.311   1.00 46.49  ? 78   GLU F OE2 1 
ATOM   6061 N  N   . ARG F 1 79  ? -55.562 50.777  2.471   1.00 29.93  ? 79   ARG F N   1 
ATOM   6062 C  CA  . ARG F 1 79  ? -55.470 51.636  3.649   1.00 27.52  ? 79   ARG F CA  1 
ATOM   6063 C  C   . ARG F 1 79  ? -56.701 52.526  3.763   1.00 31.10  ? 79   ARG F C   1 
ATOM   6064 O  O   . ARG F 1 79  ? -57.442 52.722  2.782   1.00 29.24  ? 79   ARG F O   1 
ATOM   6065 C  CB  . ARG F 1 79  ? -54.218 52.528  3.594   1.00 27.00  ? 79   ARG F CB  1 
ATOM   6066 C  CG  . ARG F 1 79  ? -54.091 53.303  2.277   1.00 27.30  ? 79   ARG F CG  1 
ATOM   6067 C  CD  . ARG F 1 79  ? -53.022 54.388  2.315   1.00 27.79  ? 79   ARG F CD  1 
ATOM   6068 N  NE  . ARG F 1 79  ? -53.548 55.609  2.900   1.00 24.76  ? 79   ARG F NE  1 
ATOM   6069 C  CZ  . ARG F 1 79  ? -52.865 56.733  3.021   1.00 28.65  ? 79   ARG F CZ  1 
ATOM   6070 N  NH1 . ARG F 1 79  ? -51.620 56.796  2.584   1.00 28.94  ? 79   ARG F NH1 1 
ATOM   6071 N  NH2 . ARG F 1 79  ? -53.432 57.794  3.577   1.00 30.75  ? 79   ARG F NH2 1 
ATOM   6072 N  N   . HIS F 1 80  ? -56.903 53.061  4.969   1.00 27.52  ? 80   HIS F N   1 
ATOM   6073 C  CA  . HIS F 1 80  ? -57.918 54.063  5.211   1.00 26.18  ? 80   HIS F CA  1 
ATOM   6074 C  C   . HIS F 1 80  ? -57.316 55.348  4.689   1.00 28.53  ? 80   HIS F C   1 
ATOM   6075 O  O   . HIS F 1 80  ? -56.098 55.477  4.637   1.00 27.97  ? 80   HIS F O   1 
ATOM   6076 C  CB  . HIS F 1 80  ? -58.208 54.205  6.713   1.00 26.76  ? 80   HIS F CB  1 
ATOM   6077 C  CG  . HIS F 1 80  ? -58.694 52.945  7.363   1.00 28.95  ? 80   HIS F CG  1 
ATOM   6078 N  ND1 . HIS F 1 80  ? -58.257 52.530  8.603   1.00 27.23  ? 80   HIS F ND1 1 
ATOM   6079 C  CD2 . HIS F 1 80  ? -59.579 52.008  6.947   1.00 29.33  ? 80   HIS F CD2 1 
ATOM   6080 C  CE1 . HIS F 1 80  ? -58.842 51.389  8.917   1.00 28.47  ? 80   HIS F CE1 1 
ATOM   6081 N  NE2 . HIS F 1 80  ? -59.646 51.048  7.926   1.00 31.58  ? 80   HIS F NE2 1 
ATOM   6082 N  N   . VAL F 1 81  ? -58.162 56.297  4.309   1.00 27.78  ? 81   VAL F N   1 
ATOM   6083 C  CA  . VAL F 1 81  ? -57.679 57.584  3.849   1.00 28.77  ? 81   VAL F CA  1 
ATOM   6084 C  C   . VAL F 1 81  ? -56.868 58.306  4.945   1.00 26.64  ? 81   VAL F C   1 
ATOM   6085 O  O   . VAL F 1 81  ? -55.808 58.850  4.672   1.00 30.31  ? 81   VAL F O   1 
ATOM   6086 C  CB  . VAL F 1 81  ? -58.828 58.443  3.262   1.00 29.44  ? 81   VAL F CB  1 
ATOM   6087 C  CG1 . VAL F 1 81  ? -58.366 59.876  2.977   1.00 25.56  ? 81   VAL F CG1 1 
ATOM   6088 C  CG2 . VAL F 1 81  ? -59.361 57.777  1.991   1.00 26.47  ? 81   VAL F CG2 1 
ATOM   6089 N  N   . GLY F 1 82  ? -57.322 58.254  6.189   1.00 27.92  ? 82   GLY F N   1 
ATOM   6090 C  CA  . GLY F 1 82  ? -56.567 58.857  7.272   1.00 27.41  ? 82   GLY F CA  1 
ATOM   6091 C  C   . GLY F 1 82  ? -55.374 58.096  7.850   1.00 28.15  ? 82   GLY F C   1 
ATOM   6092 O  O   . GLY F 1 82  ? -54.910 58.464  8.921   1.00 29.55  ? 82   GLY F O   1 
ATOM   6093 N  N   . ASP F 1 83  ? -54.877 57.055  7.174   1.00 23.45  ? 83   ASP F N   1 
ATOM   6094 C  CA  . ASP F 1 83  ? -53.725 56.281  7.666   1.00 21.36  ? 83   ASP F CA  1 
ATOM   6095 C  C   . ASP F 1 83  ? -52.387 56.918  7.336   1.00 26.53  ? 83   ASP F C   1 
ATOM   6096 O  O   . ASP F 1 83  ? -51.793 56.645  6.290   1.00 27.19  ? 83   ASP F O   1 
ATOM   6097 C  CB  . ASP F 1 83  ? -53.721 54.856  7.109   1.00 23.87  ? 83   ASP F CB  1 
ATOM   6098 C  CG  . ASP F 1 83  ? -54.843 54.030  7.654   1.00 27.45  ? 83   ASP F CG  1 
ATOM   6099 O  OD1 . ASP F 1 83  ? -55.139 52.949  7.101   1.00 25.80  ? 83   ASP F OD1 1 
ATOM   6100 O  OD2 . ASP F 1 83  ? -55.441 54.479  8.660   1.00 31.01  ? 83   ASP F OD2 1 
ATOM   6101 N  N   . LEU F 1 84  ? -51.889 57.752  8.231   1.00 25.52  ? 84   LEU F N   1 
ATOM   6102 C  CA  . LEU F 1 84  ? -50.609 58.377  7.991   1.00 26.39  ? 84   LEU F CA  1 
ATOM   6103 C  C   . LEU F 1 84  ? -49.409 57.584  8.516   1.00 28.49  ? 84   LEU F C   1 
ATOM   6104 O  O   . LEU F 1 84  ? -48.286 58.052  8.422   1.00 35.22  ? 84   LEU F O   1 
ATOM   6105 C  CB  . LEU F 1 84  ? -50.598 59.791  8.568   1.00 29.12  ? 84   LEU F CB  1 
ATOM   6106 C  CG  . LEU F 1 84  ? -51.671 60.705  7.966   1.00 29.68  ? 84   LEU F CG  1 
ATOM   6107 C  CD1 . LEU F 1 84  ? -51.773 62.017  8.728   1.00 28.32  ? 84   LEU F CD1 1 
ATOM   6108 C  CD2 . LEU F 1 84  ? -51.418 60.938  6.484   1.00 29.81  ? 84   LEU F CD2 1 
ATOM   6109 N  N   . GLY F 1 85  ? -49.627 56.394  9.060   1.00 27.50  ? 85   GLY F N   1 
ATOM   6110 C  CA  . GLY F 1 85  ? -48.531 55.618  9.615   1.00 27.60  ? 85   GLY F CA  1 
ATOM   6111 C  C   . GLY F 1 85  ? -48.056 56.037  11.012  1.00 31.30  ? 85   GLY F C   1 
ATOM   6112 O  O   . GLY F 1 85  ? -48.854 56.207  11.943  1.00 30.50  ? 85   GLY F O   1 
ATOM   6113 N  N   . ASN F 1 86  ? -46.742 56.198  11.160  1.00 27.96  ? 86   ASN F N   1 
ATOM   6114 C  CA  . ASN F 1 86  ? -46.156 56.473  12.459  1.00 28.25  ? 86   ASN F CA  1 
ATOM   6115 C  C   . ASN F 1 86  ? -45.416 57.801  12.574  1.00 28.89  ? 86   ASN F C   1 
ATOM   6116 O  O   . ASN F 1 86  ? -45.030 58.419  11.589  1.00 31.67  ? 86   ASN F O   1 
ATOM   6117 C  CB  . ASN F 1 86  ? -45.228 55.331  12.864  1.00 26.89  ? 86   ASN F CB  1 
ATOM   6118 C  CG  . ASN F 1 86  ? -45.980 54.121  13.312  1.00 26.63  ? 86   ASN F CG  1 
ATOM   6119 O  OD1 . ASN F 1 86  ? -46.552 54.109  14.399  1.00 31.65  ? 86   ASN F OD1 1 
ATOM   6120 N  ND2 . ASN F 1 86  ? -45.998 53.095  12.485  1.00 23.73  ? 86   ASN F ND2 1 
ATOM   6121 N  N   . VAL F 1 87  ? -45.202 58.209  13.809  1.00 27.19  ? 87   VAL F N   1 
ATOM   6122 C  CA  . VAL F 1 87  ? -44.502 59.437  14.104  1.00 30.60  ? 87   VAL F CA  1 
ATOM   6123 C  C   . VAL F 1 87  ? -43.463 59.040  15.162  1.00 32.61  ? 87   VAL F C   1 
ATOM   6124 O  O   . VAL F 1 87  ? -43.709 58.118  15.943  1.00 32.36  ? 87   VAL F O   1 
ATOM   6125 C  CB  . VAL F 1 87  ? -45.531 60.494  14.579  1.00 30.10  ? 87   VAL F CB  1 
ATOM   6126 C  CG1 . VAL F 1 87  ? -45.323 60.877  15.994  1.00 28.97  ? 87   VAL F CG1 1 
ATOM   6127 C  CG2 . VAL F 1 87  ? -45.542 61.695  13.659  1.00 29.45  ? 87   VAL F CG2 1 
ATOM   6128 N  N   . THR F 1 88  ? -42.288 59.670  15.167  1.00 36.39  ? 88   THR F N   1 
ATOM   6129 C  CA  . THR F 1 88  ? -41.202 59.184  16.037  1.00 35.94  ? 88   THR F CA  1 
ATOM   6130 C  C   . THR F 1 88  ? -40.715 60.151  17.113  1.00 33.66  ? 88   THR F C   1 
ATOM   6131 O  O   . THR F 1 88  ? -40.217 61.230  16.816  1.00 33.95  ? 88   THR F O   1 
ATOM   6132 C  CB  . THR F 1 88  ? -39.980 58.751  15.229  1.00 35.96  ? 88   THR F CB  1 
ATOM   6133 O  OG1 . THR F 1 88  ? -40.379 57.780  14.265  1.00 30.39  ? 88   THR F OG1 1 
ATOM   6134 C  CG2 . THR F 1 88  ? -38.921 58.151  16.159  1.00 32.52  ? 88   THR F CG2 1 
ATOM   6135 N  N   . ALA F 1 89  ? -40.848 59.741  18.367  1.00 35.99  ? 89   ALA F N   1 
ATOM   6136 C  CA  . ALA F 1 89  ? -40.372 60.552  19.474  1.00 39.60  ? 89   ALA F CA  1 
ATOM   6137 C  C   . ALA F 1 89  ? -38.920 60.194  19.817  1.00 39.67  ? 89   ALA F C   1 
ATOM   6138 O  O   . ALA F 1 89  ? -38.555 59.021  19.888  1.00 37.70  ? 89   ALA F O   1 
ATOM   6139 C  CB  . ALA F 1 89  ? -41.273 60.378  20.674  1.00 36.83  ? 89   ALA F CB  1 
ATOM   6140 N  N   . ASP F 1 90  ? -38.090 61.209  20.003  1.00 44.28  ? 90   ASP F N   1 
ATOM   6141 C  CA  . ASP F 1 90  ? -36.707 60.975  20.406  1.00 43.75  ? 90   ASP F CA  1 
ATOM   6142 C  C   . ASP F 1 90  ? -36.625 60.883  21.925  1.00 43.90  ? 90   ASP F C   1 
ATOM   6143 O  O   . ASP F 1 90  ? -37.656 60.854  22.593  1.00 43.80  ? 90   ASP F O   1 
ATOM   6144 C  CB  . ASP F 1 90  ? -35.762 62.042  19.830  1.00 39.55  ? 90   ASP F CB  1 
ATOM   6145 C  CG  . ASP F 1 90  ? -35.992 63.414  20.414  1.00 46.10  ? 90   ASP F CG  1 
ATOM   6146 O  OD1 . ASP F 1 90  ? -36.488 63.513  21.564  1.00 42.77  ? 90   ASP F OD1 1 
ATOM   6147 O  OD2 . ASP F 1 90  ? -35.658 64.396  19.710  1.00 49.58  ? 90   ASP F OD2 1 
ATOM   6148 N  N   . LYS F 1 91  ? -35.405 60.832  22.456  1.00 47.47  ? 91   LYS F N   1 
ATOM   6149 C  CA  . LYS F 1 91  ? -35.164 60.605  23.881  1.00 47.13  ? 91   LYS F CA  1 
ATOM   6150 C  C   . LYS F 1 91  ? -35.768 61.685  24.774  1.00 50.96  ? 91   LYS F C   1 
ATOM   6151 O  O   . LYS F 1 91  ? -36.136 61.417  25.922  1.00 57.65  ? 91   LYS F O   1 
ATOM   6152 C  CB  . LYS F 1 91  ? -33.664 60.526  24.147  1.00 56.16  ? 91   LYS F CB  1 
ATOM   6153 C  CG  . LYS F 1 91  ? -32.979 61.883  24.088  1.00 60.39  ? 91   LYS F CG  1 
ATOM   6154 C  CD  . LYS F 1 91  ? -31.467 61.759  24.077  1.00 64.81  ? 91   LYS F CD  1 
ATOM   6155 C  CE  . LYS F 1 91  ? -30.809 63.127  24.246  1.00 69.84  ? 91   LYS F CE  1 
ATOM   6156 N  NZ  . LYS F 1 91  ? -31.203 63.794  25.536  1.00 65.69  ? 91   LYS F NZ  1 
ATOM   6157 N  N   . ASP F 1 92  ? -35.865 62.903  24.250  1.00 49.13  ? 92   ASP F N   1 
ATOM   6158 C  CA  . ASP F 1 92  ? -36.510 64.012  24.960  1.00 52.83  ? 92   ASP F CA  1 
ATOM   6159 C  C   . ASP F 1 92  ? -38.037 63.970  24.807  1.00 53.35  ? 92   ASP F C   1 
ATOM   6160 O  O   . ASP F 1 92  ? -38.756 64.764  25.412  1.00 51.01  ? 92   ASP F O   1 
ATOM   6161 C  CB  . ASP F 1 92  ? -35.964 65.360  24.463  1.00 54.34  ? 92   ASP F CB  1 
ATOM   6162 C  CG  . ASP F 1 92  ? -34.472 65.528  24.737  1.00 59.11  ? 92   ASP F CG  1 
ATOM   6163 O  OD1 . ASP F 1 92  ? -34.065 65.408  25.912  1.00 58.66  ? 92   ASP F OD1 1 
ATOM   6164 O  OD2 . ASP F 1 92  ? -33.704 65.779  23.781  1.00 59.00  ? 92   ASP F OD2 1 
ATOM   6165 N  N   . GLY F 1 93  ? -38.525 63.045  23.983  1.00 49.95  ? 93   GLY F N   1 
ATOM   6166 C  CA  . GLY F 1 93  ? -39.953 62.856  23.808  1.00 46.94  ? 93   GLY F CA  1 
ATOM   6167 C  C   . GLY F 1 93  ? -40.514 63.708  22.693  1.00 42.65  ? 93   GLY F C   1 
ATOM   6168 O  O   . GLY F 1 93  ? -41.722 63.867  22.571  1.00 47.29  ? 93   GLY F O   1 
ATOM   6169 N  N   . VAL F 1 94  ? -39.629 64.238  21.863  1.00 44.01  ? 94   VAL F N   1 
ATOM   6170 C  CA  . VAL F 1 94  ? -40.017 65.177  20.823  1.00 43.71  ? 94   VAL F CA  1 
ATOM   6171 C  C   . VAL F 1 94  ? -40.075 64.546  19.438  1.00 44.35  ? 94   VAL F C   1 
ATOM   6172 O  O   . VAL F 1 94  ? -39.070 64.080  18.906  1.00 44.96  ? 94   VAL F O   1 
ATOM   6173 C  CB  . VAL F 1 94  ? -39.052 66.370  20.763  1.00 42.44  ? 94   VAL F CB  1 
ATOM   6174 C  CG1 . VAL F 1 94  ? -39.413 67.275  19.605  1.00 49.20  ? 94   VAL F CG1 1 
ATOM   6175 C  CG2 . VAL F 1 94  ? -39.095 67.136  22.058  1.00 45.98  ? 94   VAL F CG2 1 
ATOM   6176 N  N   . ALA F 1 95  ? -41.265 64.541  18.855  1.00 45.01  ? 95   ALA F N   1 
ATOM   6177 C  CA  . ALA F 1 95  ? -41.435 64.073  17.492  1.00 38.61  ? 95   ALA F CA  1 
ATOM   6178 C  C   . ALA F 1 95  ? -41.441 65.281  16.599  1.00 40.85  ? 95   ALA F C   1 
ATOM   6179 O  O   . ALA F 1 95  ? -42.359 66.099  16.658  1.00 39.83  ? 95   ALA F O   1 
ATOM   6180 C  CB  . ALA F 1 95  ? -42.735 63.296  17.331  1.00 33.29  ? 95   ALA F CB  1 
ATOM   6181 N  N   . ASP F 1 96  ? -40.396 65.400  15.794  1.00 38.63  ? 96   ASP F N   1 
ATOM   6182 C  CA  . ASP F 1 96  ? -40.350 66.391  14.750  1.00 38.21  ? 96   ASP F CA  1 
ATOM   6183 C  C   . ASP F 1 96  ? -41.008 65.779  13.528  1.00 41.62  ? 96   ASP F C   1 
ATOM   6184 O  O   . ASP F 1 96  ? -40.385 65.036  12.779  1.00 43.88  ? 96   ASP F O   1 
ATOM   6185 C  CB  . ASP F 1 96  ? -38.897 66.774  14.445  1.00 44.10  ? 96   ASP F CB  1 
ATOM   6186 C  CG  . ASP F 1 96  ? -38.236 67.524  15.604  1.00 61.47  ? 96   ASP F CG  1 
ATOM   6187 O  OD1 . ASP F 1 96  ? -38.973 68.211  16.357  1.00 55.77  ? 96   ASP F OD1 1 
ATOM   6188 O  OD2 . ASP F 1 96  ? -36.988 67.425  15.768  1.00 68.12  ? 96   ASP F OD2 1 
ATOM   6189 N  N   . VAL F 1 97  ? -42.273 66.098  13.312  1.00 41.69  ? 97   VAL F N   1 
ATOM   6190 C  CA  . VAL F 1 97  ? -43.018 65.455  12.238  1.00 38.75  ? 97   VAL F CA  1 
ATOM   6191 C  C   . VAL F 1 97  ? -42.614 65.914  10.844  1.00 34.18  ? 97   VAL F C   1 
ATOM   6192 O  O   . VAL F 1 97  ? -42.436 67.095  10.590  1.00 34.29  ? 97   VAL F O   1 
ATOM   6193 C  CB  . VAL F 1 97  ? -44.513 65.672  12.429  1.00 38.99  ? 97   VAL F CB  1 
ATOM   6194 C  CG1 . VAL F 1 97  ? -45.278 65.050  11.276  1.00 34.60  ? 97   VAL F CG1 1 
ATOM   6195 C  CG2 . VAL F 1 97  ? -44.935 65.088  13.782  1.00 35.24  ? 97   VAL F CG2 1 
ATOM   6196 N  N   . SER F 1 98  ? -42.465 64.966  9.935   1.00 35.33  ? 98   SER F N   1 
ATOM   6197 C  CA  . SER F 1 98  ? -42.234 65.316  8.545   1.00 37.32  ? 98   SER F CA  1 
ATOM   6198 C  C   . SER F 1 98  ? -42.782 64.225  7.617   1.00 39.32  ? 98   SER F C   1 
ATOM   6199 O  O   . SER F 1 98  ? -42.130 63.203  7.349   1.00 37.14  ? 98   SER F O   1 
ATOM   6200 C  CB  . SER F 1 98  ? -40.757 65.590  8.281   1.00 36.74  ? 98   SER F CB  1 
ATOM   6201 O  OG  . SER F 1 98  ? -40.586 66.171  7.004   1.00 46.52  ? 98   SER F OG  1 
ATOM   6202 N  N   . ILE F 1 99  ? -44.000 64.460  7.141   1.00 38.04  ? 99   ILE F N   1 
ATOM   6203 C  CA  . ILE F 1 99  ? -44.716 63.500  6.312   1.00 33.59  ? 99   ILE F CA  1 
ATOM   6204 C  C   . ILE F 1 99  ? -45.228 64.133  5.022   1.00 33.52  ? 99   ILE F C   1 
ATOM   6205 O  O   . ILE F 1 99  ? -45.706 65.265  4.978   1.00 32.29  ? 99   ILE F O   1 
ATOM   6206 C  CB  . ILE F 1 99  ? -45.911 62.883  7.086   1.00 38.87  ? 99   ILE F CB  1 
ATOM   6207 C  CG1 . ILE F 1 99  ? -45.413 62.189  8.363   1.00 36.73  ? 99   ILE F CG1 1 
ATOM   6208 C  CG2 . ILE F 1 99  ? -46.723 61.949  6.197   1.00 31.98  ? 99   ILE F CG2 1 
ATOM   6209 C  CD1 . ILE F 1 99  ? -46.449 61.344  9.077   1.00 34.52  ? 99   ILE F CD1 1 
ATOM   6210 N  N   . GLU F 1 100 ? -45.101 63.384  3.953   1.00 35.39  ? 100  GLU F N   1 
ATOM   6211 C  CA  . GLU F 1 100 ? -45.720 63.751  2.717   1.00 34.98  ? 100  GLU F CA  1 
ATOM   6212 C  C   . GLU F 1 100 ? -46.694 62.615  2.363   1.00 35.12  ? 100  GLU F C   1 
ATOM   6213 O  O   . GLU F 1 100 ? -46.304 61.451  2.254   1.00 34.00  ? 100  GLU F O   1 
ATOM   6214 C  CB  . GLU F 1 100 ? -44.645 63.925  1.661   1.00 32.04  ? 100  GLU F CB  1 
ATOM   6215 C  CG  . GLU F 1 100 ? -45.186 64.224  0.292   1.00 43.41  ? 100  GLU F CG  1 
ATOM   6216 C  CD  . GLU F 1 100 ? -44.092 64.329  -0.737  1.00 55.29  ? 100  GLU F CD  1 
ATOM   6217 O  OE1 . GLU F 1 100 ? -43.094 63.579  -0.625  1.00 59.12  ? 100  GLU F OE1 1 
ATOM   6218 O  OE2 . GLU F 1 100 ? -44.230 65.169  -1.650  1.00 60.48  ? 100  GLU F OE2 1 
ATOM   6219 N  N   . ASP F 1 101 ? -47.971 62.933  2.223   1.00 36.80  ? 101  ASP F N   1 
ATOM   6220 C  CA  . ASP F 1 101 ? -48.928 61.891  1.859   1.00 36.51  ? 101  ASP F CA  1 
ATOM   6221 C  C   . ASP F 1 101 ? -49.784 62.290  0.673   1.00 34.82  ? 101  ASP F C   1 
ATOM   6222 O  O   . ASP F 1 101 ? -50.295 63.406  0.621   1.00 34.01  ? 101  ASP F O   1 
ATOM   6223 C  CB  . ASP F 1 101 ? -49.817 61.525  3.039   1.00 34.35  ? 101  ASP F CB  1 
ATOM   6224 C  CG  . ASP F 1 101 ? -50.677 60.316  2.745   1.00 36.01  ? 101  ASP F CG  1 
ATOM   6225 O  OD1 . ASP F 1 101 ? -50.133 59.195  2.712   1.00 36.09  ? 101  ASP F OD1 1 
ATOM   6226 O  OD2 . ASP F 1 101 ? -51.893 60.493  2.524   1.00 33.64  ? 101  ASP F OD2 1 
ATOM   6227 N  N   . SER F 1 102 ? -49.955 61.377  -0.276  1.00 34.86  ? 102  SER F N   1 
ATOM   6228 C  CA  . SER F 1 102 ? -50.658 61.730  -1.498  1.00 32.58  ? 102  SER F CA  1 
ATOM   6229 C  C   . SER F 1 102 ? -52.103 61.224  -1.570  1.00 36.38  ? 102  SER F C   1 
ATOM   6230 O  O   . SER F 1 102 ? -52.749 61.379  -2.605  1.00 34.44  ? 102  SER F O   1 
ATOM   6231 C  CB  . SER F 1 102 ? -49.856 61.294  -2.728  1.00 33.66  ? 102  SER F CB  1 
ATOM   6232 O  OG  . SER F 1 102 ? -49.771 59.887  -2.803  1.00 37.60  ? 102  SER F OG  1 
ATOM   6233 N  N   . VAL F 1 103 ? -52.611 60.644  -0.478  1.00 33.48  ? 103  VAL F N   1 
ATOM   6234 C  CA  . VAL F 1 103 ? -53.998 60.149  -0.441  1.00 32.60  ? 103  VAL F CA  1 
ATOM   6235 C  C   . VAL F 1 103 ? -54.968 61.101  0.265   1.00 30.85  ? 103  VAL F C   1 
ATOM   6236 O  O   . VAL F 1 103 ? -56.082 61.337  -0.206  1.00 27.58  ? 103  VAL F O   1 
ATOM   6237 C  CB  . VAL F 1 103 ? -54.095 58.744  0.195   1.00 33.37  ? 103  VAL F CB  1 
ATOM   6238 C  CG1 . VAL F 1 103 ? -55.568 58.321  0.373   1.00 29.13  ? 103  VAL F CG1 1 
ATOM   6239 C  CG2 . VAL F 1 103 ? -53.329 57.733  -0.648  1.00 27.73  ? 103  VAL F CG2 1 
ATOM   6240 N  N   . ILE F 1 104 ? -54.548 61.633  1.407   1.00 31.68  ? 104  ILE F N   1 
ATOM   6241 C  CA  . ILE F 1 104 ? -55.319 62.673  2.064   1.00 30.51  ? 104  ILE F CA  1 
ATOM   6242 C  C   . ILE F 1 104 ? -55.342 63.940  1.190   1.00 33.16  ? 104  ILE F C   1 
ATOM   6243 O  O   . ILE F 1 104 ? -54.522 64.095  0.285   1.00 28.22  ? 104  ILE F O   1 
ATOM   6244 C  CB  . ILE F 1 104 ? -54.748 63.014  3.449   1.00 29.38  ? 104  ILE F CB  1 
ATOM   6245 C  CG1 . ILE F 1 104 ? -53.251 63.319  3.355   1.00 31.03  ? 104  ILE F CG1 1 
ATOM   6246 C  CG2 . ILE F 1 104 ? -55.029 61.881  4.454   1.00 25.81  ? 104  ILE F CG2 1 
ATOM   6247 C  CD1 . ILE F 1 104 ? -52.764 64.336  4.377   1.00 26.48  ? 104  ILE F CD1 1 
ATOM   6248 N  N   . SER F 1 105 ? -56.294 64.832  1.448   1.00 30.86  ? 105  SER F N   1 
ATOM   6249 C  CA  . SER F 1 105 ? -56.315 66.110  0.753   1.00 30.44  ? 105  SER F CA  1 
ATOM   6250 C  C   . SER F 1 105 ? -56.810 67.236  1.649   1.00 32.01  ? 105  SER F C   1 
ATOM   6251 O  O   . SER F 1 105 ? -57.300 66.993  2.763   1.00 32.55  ? 105  SER F O   1 
ATOM   6252 C  CB  . SER F 1 105 ? -57.165 66.030  -0.518  1.00 33.21  ? 105  SER F CB  1 
ATOM   6253 O  OG  . SER F 1 105 ? -57.198 67.285  -1.187  1.00 31.71  ? 105  SER F OG  1 
ATOM   6254 N  N   . LEU F 1 106 ? -56.670 68.468  1.164   1.00 31.27  ? 106  LEU F N   1 
ATOM   6255 C  CA  . LEU F 1 106 ? -57.275 69.629  1.820   1.00 34.75  ? 106  LEU F CA  1 
ATOM   6256 C  C   . LEU F 1 106 ? -58.576 70.045  1.120   1.00 36.09  ? 106  LEU F C   1 
ATOM   6257 O  O   . LEU F 1 106 ? -59.246 70.987  1.543   1.00 34.12  ? 106  LEU F O   1 
ATOM   6258 C  CB  . LEU F 1 106 ? -56.288 70.793  1.908   1.00 31.45  ? 106  LEU F CB  1 
ATOM   6259 C  CG  . LEU F 1 106 ? -55.009 70.424  2.673   1.00 40.19  ? 106  LEU F CG  1 
ATOM   6260 C  CD1 . LEU F 1 106 ? -54.030 71.585  2.719   1.00 42.25  ? 106  LEU F CD1 1 
ATOM   6261 C  CD2 . LEU F 1 106 ? -55.312 69.938  4.098   1.00 34.82  ? 106  LEU F CD2 1 
ATOM   6262 N  N   . SER F 1 107 ? -58.941 69.326  0.059   1.00 33.61  ? 107  SER F N   1 
ATOM   6263 C  CA  . SER F 1 107 ? -60.259 69.524  -0.563  1.00 37.94  ? 107  SER F CA  1 
ATOM   6264 C  C   . SER F 1 107 ? -60.828 68.255  -1.222  1.00 32.85  ? 107  SER F C   1 
ATOM   6265 O  O   . SER F 1 107 ? -60.176 67.217  -1.279  1.00 32.17  ? 107  SER F O   1 
ATOM   6266 C  CB  . SER F 1 107 ? -60.220 70.675  -1.572  1.00 32.51  ? 107  SER F CB  1 
ATOM   6267 O  OG  . SER F 1 107 ? -59.614 70.237  -2.780  1.00 42.57  ? 107  SER F OG  1 
ATOM   6268 N  N   . GLY F 1 108 ? -62.065 68.345  -1.698  1.00 36.73  ? 108  GLY F N   1 
ATOM   6269 C  CA  . GLY F 1 108 ? -62.717 67.228  -2.360  1.00 27.08  ? 108  GLY F CA  1 
ATOM   6270 C  C   . GLY F 1 108 ? -63.089 66.141  -1.378  1.00 34.39  ? 108  GLY F C   1 
ATOM   6271 O  O   . GLY F 1 108 ? -63.132 66.362  -0.168  1.00 32.55  ? 108  GLY F O   1 
ATOM   6272 N  N   . ASP F 1 109 ? -63.353 64.956  -1.911  1.00 36.86  ? 109  ASP F N   1 
ATOM   6273 C  CA  . ASP F 1 109 ? -63.825 63.822  -1.125  1.00 34.00  ? 109  ASP F CA  1 
ATOM   6274 C  C   . ASP F 1 109 ? -62.883 63.409  -0.016  1.00 35.41  ? 109  ASP F C   1 
ATOM   6275 O  O   . ASP F 1 109 ? -63.338 62.938  1.030   1.00 37.54  ? 109  ASP F O   1 
ATOM   6276 C  CB  . ASP F 1 109 ? -64.050 62.615  -2.037  1.00 35.43  ? 109  ASP F CB  1 
ATOM   6277 C  CG  . ASP F 1 109 ? -65.175 62.834  -2.990  1.00 41.53  ? 109  ASP F CG  1 
ATOM   6278 O  OD1 . ASP F 1 109 ? -65.888 63.848  -2.822  1.00 34.97  ? 109  ASP F OD1 1 
ATOM   6279 O  OD2 . ASP F 1 109 ? -65.338 62.006  -3.906  1.00 48.52  ? 109  ASP F OD2 1 
ATOM   6280 N  N   . HIS F 1 110 ? -61.581 63.566  -0.254  1.00 33.22  ? 110  HIS F N   1 
ATOM   6281 C  CA  . HIS F 1 110 ? -60.560 63.128  0.695   1.00 31.76  ? 110  HIS F CA  1 
ATOM   6282 C  C   . HIS F 1 110 ? -60.114 64.256  1.601   1.00 29.94  ? 110  HIS F C   1 
ATOM   6283 O  O   . HIS F 1 110 ? -59.058 64.183  2.215   1.00 33.35  ? 110  HIS F O   1 
ATOM   6284 C  CB  . HIS F 1 110 ? -59.351 62.547  -0.040  1.00 30.26  ? 110  HIS F CB  1 
ATOM   6285 C  CG  . HIS F 1 110 ? -59.600 61.203  -0.638  1.00 29.96  ? 110  HIS F CG  1 
ATOM   6286 N  ND1 . HIS F 1 110 ? -58.622 60.480  -1.287  1.00 34.32  ? 110  HIS F ND1 1 
ATOM   6287 C  CD2 . HIS F 1 110 ? -60.720 60.442  -0.678  1.00 31.87  ? 110  HIS F CD2 1 
ATOM   6288 C  CE1 . HIS F 1 110 ? -59.129 59.334  -1.706  1.00 35.63  ? 110  HIS F CE1 1 
ATOM   6289 N  NE2 . HIS F 1 110 ? -60.400 59.285  -1.350  1.00 30.68  ? 110  HIS F NE2 1 
ATOM   6290 N  N   . CYS F 1 111 ? -60.918 65.307  1.663   1.00 32.48  ? 111  CYS F N   1 
ATOM   6291 C  CA  . CYS F 1 111 ? -60.587 66.498  2.440   1.00 34.95  ? 111  CYS F CA  1 
ATOM   6292 C  C   . CYS F 1 111 ? -60.609 66.209  3.946   1.00 33.32  ? 111  CYS F C   1 
ATOM   6293 O  O   . CYS F 1 111 ? -61.503 65.528  4.435   1.00 34.09  ? 111  CYS F O   1 
ATOM   6294 C  CB  . CYS F 1 111 ? -61.557 67.627  2.089   1.00 31.20  ? 111  CYS F CB  1 
ATOM   6295 S  SG  . CYS F 1 111 ? -61.483 69.038  3.191   1.00 40.45  ? 111  CYS F SG  1 
ATOM   6296 N  N   . ILE F 1 112 ? -59.631 66.728  4.679   1.00 30.41  ? 112  ILE F N   1 
ATOM   6297 C  CA  . ILE F 1 112 ? -59.476 66.348  6.083   1.00 31.32  ? 112  ILE F CA  1 
ATOM   6298 C  C   . ILE F 1 112 ? -59.692 67.535  6.997   1.00 32.56  ? 112  ILE F C   1 
ATOM   6299 O  O   . ILE F 1 112 ? -59.561 67.434  8.208   1.00 32.23  ? 112  ILE F O   1 
ATOM   6300 C  CB  . ILE F 1 112 ? -58.099 65.688  6.369   1.00 30.24  ? 112  ILE F CB  1 
ATOM   6301 C  CG1 . ILE F 1 112 ? -56.952 66.683  6.160   1.00 28.57  ? 112  ILE F CG1 1 
ATOM   6302 C  CG2 . ILE F 1 112 ? -57.908 64.431  5.509   1.00 25.08  ? 112  ILE F CG2 1 
ATOM   6303 C  CD1 . ILE F 1 112 ? -55.580 66.073  6.383   1.00 27.33  ? 112  ILE F CD1 1 
ATOM   6304 N  N   . ILE F 1 113 ? -60.024 68.669  6.398   1.00 34.94  ? 113  ILE F N   1 
ATOM   6305 C  CA  . ILE F 1 113 ? -60.326 69.854  7.167   1.00 34.26  ? 113  ILE F CA  1 
ATOM   6306 C  C   . ILE F 1 113 ? -61.640 69.619  7.875   1.00 34.08  ? 113  ILE F C   1 
ATOM   6307 O  O   . ILE F 1 113 ? -62.587 69.112  7.281   1.00 36.42  ? 113  ILE F O   1 
ATOM   6308 C  CB  . ILE F 1 113 ? -60.361 71.112  6.273   1.00 35.72  ? 113  ILE F CB  1 
ATOM   6309 C  CG1 . ILE F 1 113 ? -58.927 71.602  6.023   1.00 37.55  ? 113  ILE F CG1 1 
ATOM   6310 C  CG2 . ILE F 1 113 ? -61.185 72.219  6.918   1.00 34.10  ? 113  ILE F CG2 1 
ATOM   6311 C  CD1 . ILE F 1 113 ? -58.606 71.798  4.565   1.00 40.32  ? 113  ILE F CD1 1 
ATOM   6312 N  N   . GLY F 1 114 ? -61.686 69.954  9.156   1.00 31.54  ? 114  GLY F N   1 
ATOM   6313 C  CA  . GLY F 1 114 ? -62.846 69.636  9.956   1.00 32.81  ? 114  GLY F CA  1 
ATOM   6314 C  C   . GLY F 1 114 ? -62.806 68.259  10.590  1.00 32.58  ? 114  GLY F C   1 
ATOM   6315 O  O   . GLY F 1 114 ? -63.708 67.895  11.341  1.00 28.50  ? 114  GLY F O   1 
ATOM   6316 N  N   . ARG F 1 115 ? -61.761 67.491  10.304  1.00 32.13  ? 115  ARG F N   1 
ATOM   6317 C  CA  . ARG F 1 115 ? -61.633 66.157  10.886  1.00 31.20  ? 115  ARG F CA  1 
ATOM   6318 C  C   . ARG F 1 115 ? -60.547 66.162  11.963  1.00 36.21  ? 115  ARG F C   1 
ATOM   6319 O  O   . ARG F 1 115 ? -59.872 67.177  12.164  1.00 35.08  ? 115  ARG F O   1 
ATOM   6320 C  CB  . ARG F 1 115 ? -61.360 65.123  9.808   1.00 29.44  ? 115  ARG F CB  1 
ATOM   6321 C  CG  . ARG F 1 115 ? -62.224 65.301  8.552   1.00 29.88  ? 115  ARG F CG  1 
ATOM   6322 C  CD  . ARG F 1 115 ? -62.278 64.017  7.720   1.00 31.38  ? 115  ARG F CD  1 
ATOM   6323 N  NE  . ARG F 1 115 ? -63.182 64.091  6.571   1.00 30.22  ? 115  ARG F NE  1 
ATOM   6324 C  CZ  . ARG F 1 115 ? -64.448 63.673  6.565   1.00 33.71  ? 115  ARG F CZ  1 
ATOM   6325 N  NH1 . ARG F 1 115 ? -65.007 63.134  7.653   1.00 33.03  ? 115  ARG F NH1 1 
ATOM   6326 N  NH2 . ARG F 1 115 ? -65.159 63.778  5.452   1.00 30.10  ? 115  ARG F NH2 1 
ATOM   6327 N  N   . THR F 1 116 ? -60.389 65.061  12.691  1.00 33.89  ? 116  THR F N   1 
ATOM   6328 C  CA  . THR F 1 116 ? -59.491 65.111  13.838  1.00 30.89  ? 116  THR F CA  1 
ATOM   6329 C  C   . THR F 1 116 ? -58.196 64.379  13.621  1.00 30.83  ? 116  THR F C   1 
ATOM   6330 O  O   . THR F 1 116 ? -58.183 63.235  13.168  1.00 32.03  ? 116  THR F O   1 
ATOM   6331 C  CB  . THR F 1 116 ? -60.138 64.590  15.101  1.00 31.39  ? 116  THR F CB  1 
ATOM   6332 O  OG1 . THR F 1 116 ? -61.267 65.401  15.398  1.00 34.22  ? 116  THR F OG1 1 
ATOM   6333 C  CG2 . THR F 1 116 ? -59.152 64.661  16.260  1.00 32.77  ? 116  THR F CG2 1 
ATOM   6334 N  N   . LEU F 1 117 ? -57.106 65.063  13.949  1.00 33.14  ? 117  LEU F N   1 
ATOM   6335 C  CA  . LEU F 1 117 ? -55.780 64.474  13.938  1.00 29.84  ? 117  LEU F CA  1 
ATOM   6336 C  C   . LEU F 1 117 ? -55.546 63.890  15.318  1.00 32.32  ? 117  LEU F C   1 
ATOM   6337 O  O   . LEU F 1 117 ? -55.773 64.564  16.331  1.00 33.15  ? 117  LEU F O   1 
ATOM   6338 C  CB  . LEU F 1 117 ? -54.720 65.530  13.638  1.00 32.60  ? 117  LEU F CB  1 
ATOM   6339 C  CG  . LEU F 1 117 ? -53.304 64.959  13.432  1.00 34.90  ? 117  LEU F CG  1 
ATOM   6340 C  CD1 . LEU F 1 117 ? -53.300 63.822  12.411  1.00 26.97  ? 117  LEU F CD1 1 
ATOM   6341 C  CD2 . LEU F 1 117 ? -52.327 66.032  13.025  1.00 30.92  ? 117  LEU F CD2 1 
ATOM   6342 N  N   . VAL F 1 118 ? -55.120 62.632  15.366  1.00 33.36  ? 118  VAL F N   1 
ATOM   6343 C  CA  . VAL F 1 118 ? -54.926 61.949  16.642  1.00 28.22  ? 118  VAL F CA  1 
ATOM   6344 C  C   . VAL F 1 118 ? -53.552 61.310  16.709  1.00 33.37  ? 118  VAL F C   1 
ATOM   6345 O  O   . VAL F 1 118 ? -53.128 60.613  15.772  1.00 27.28  ? 118  VAL F O   1 
ATOM   6346 C  CB  . VAL F 1 118 ? -55.953 60.833  16.876  1.00 27.89  ? 118  VAL F CB  1 
ATOM   6347 C  CG1 . VAL F 1 118 ? -55.815 60.300  18.302  1.00 29.30  ? 118  VAL F CG1 1 
ATOM   6348 C  CG2 . VAL F 1 118 ? -57.384 61.308  16.590  1.00 27.09  ? 118  VAL F CG2 1 
ATOM   6349 N  N   . VAL F 1 119 ? -52.857 61.534  17.823  1.00 31.70  ? 119  VAL F N   1 
ATOM   6350 C  CA  . VAL F 1 119 ? -51.612 60.824  18.055  1.00 28.87  ? 119  VAL F CA  1 
ATOM   6351 C  C   . VAL F 1 119 ? -51.862 59.799  19.142  1.00 29.43  ? 119  VAL F C   1 
ATOM   6352 O  O   . VAL F 1 119 ? -52.555 60.099  20.097  1.00 35.94  ? 119  VAL F O   1 
ATOM   6353 C  CB  . VAL F 1 119 ? -50.455 61.761  18.411  1.00 29.82  ? 119  VAL F CB  1 
ATOM   6354 C  CG1 . VAL F 1 119 ? -50.764 62.553  19.671  1.00 29.15  ? 119  VAL F CG1 1 
ATOM   6355 C  CG2 . VAL F 1 119 ? -49.179 60.955  18.550  1.00 32.06  ? 119  VAL F CG2 1 
ATOM   6356 N  N   . HIS F 1 120 ? -51.313 58.594  18.976  1.00 30.55  ? 120  HIS F N   1 
ATOM   6357 C  CA  . HIS F 1 120 ? -51.702 57.418  19.759  1.00 29.91  ? 120  HIS F CA  1 
ATOM   6358 C  C   . HIS F 1 120 ? -50.616 56.877  20.701  1.00 30.77  ? 120  HIS F C   1 
ATOM   6359 O  O   . HIS F 1 120 ? -49.421 57.159  20.553  1.00 30.61  ? 120  HIS F O   1 
ATOM   6360 C  CB  . HIS F 1 120 ? -52.153 56.280  18.830  1.00 30.28  ? 120  HIS F CB  1 
ATOM   6361 C  CG  . HIS F 1 120 ? -53.422 56.559  18.081  1.00 29.06  ? 120  HIS F CG  1 
ATOM   6362 N  ND1 . HIS F 1 120 ? -54.636 56.015  18.446  1.00 28.22  ? 120  HIS F ND1 1 
ATOM   6363 C  CD2 . HIS F 1 120 ? -53.661 57.292  16.966  1.00 27.57  ? 120  HIS F CD2 1 
ATOM   6364 C  CE1 . HIS F 1 120 ? -55.568 56.409  17.597  1.00 28.46  ? 120  HIS F CE1 1 
ATOM   6365 N  NE2 . HIS F 1 120 ? -55.002 57.183  16.687  1.00 29.84  ? 120  HIS F NE2 1 
ATOM   6366 N  N   . GLU F 1 121 ? -51.059 56.079  21.664  1.00 31.35  ? 121  GLU F N   1 
ATOM   6367 C  CA  . GLU F 1 121 ? -50.204 55.530  22.719  1.00 34.59  ? 121  GLU F CA  1 
ATOM   6368 C  C   . GLU F 1 121 ? -49.087 54.620  22.163  1.00 35.53  ? 121  GLU F C   1 
ATOM   6369 O  O   . GLU F 1 121 ? -47.918 54.749  22.535  1.00 35.69  ? 121  GLU F O   1 
ATOM   6370 C  CB  . GLU F 1 121 ? -51.108 54.806  23.734  1.00 35.07  ? 121  GLU F CB  1 
ATOM   6371 C  CG  . GLU F 1 121 ? -50.444 53.914  24.768  1.00 39.46  ? 121  GLU F CG  1 
ATOM   6372 C  CD  . GLU F 1 121 ? -51.366 52.766  25.233  1.00 44.25  ? 121  GLU F CD  1 
ATOM   6373 O  OE1 . GLU F 1 121 ? -52.315 52.420  24.496  1.00 38.55  ? 121  GLU F OE1 1 
ATOM   6374 O  OE2 . GLU F 1 121 ? -51.140 52.198  26.331  1.00 54.50  ? 121  GLU F OE2 1 
ATOM   6375 N  N   . LYS F 1 122 ? -49.437 53.726  21.244  1.00 32.15  ? 122  LYS F N   1 
ATOM   6376 C  CA  . LYS F 1 122 ? -48.467 52.757  20.733  1.00 32.99  ? 122  LYS F CA  1 
ATOM   6377 C  C   . LYS F 1 122 ? -48.183 52.943  19.235  1.00 31.55  ? 122  LYS F C   1 
ATOM   6378 O  O   . LYS F 1 122 ? -48.833 53.750  18.556  1.00 30.59  ? 122  LYS F O   1 
ATOM   6379 C  CB  . LYS F 1 122 ? -48.937 51.318  21.034  1.00 34.04  ? 122  LYS F CB  1 
ATOM   6380 C  CG  . LYS F 1 122 ? -49.111 51.018  22.526  1.00 40.19  ? 122  LYS F CG  1 
ATOM   6381 C  CD  . LYS F 1 122 ? -49.529 49.574  22.782  1.00 53.63  ? 122  LYS F CD  1 
ATOM   6382 C  CE  . LYS F 1 122 ? -50.043 49.343  24.231  1.00 61.36  ? 122  LYS F CE  1 
ATOM   6383 N  NZ  . LYS F 1 122 ? -50.752 47.993  24.410  1.00 55.83  ? 122  LYS F NZ  1 
ATOM   6384 N  N   . ALA F 1 123 ? -47.205 52.208  18.717  1.00 30.43  ? 123  ALA F N   1 
ATOM   6385 C  CA  . ALA F 1 123 ? -46.948 52.243  17.279  1.00 29.70  ? 123  ALA F CA  1 
ATOM   6386 C  C   . ALA F 1 123 ? -48.073 51.587  16.478  1.00 28.32  ? 123  ALA F C   1 
ATOM   6387 O  O   . ALA F 1 123 ? -48.701 50.620  16.917  1.00 27.08  ? 123  ALA F O   1 
ATOM   6388 C  CB  . ALA F 1 123 ? -45.631 51.600  16.952  1.00 28.01  ? 123  ALA F CB  1 
ATOM   6389 N  N   . ASP F 1 124 ? -48.327 52.156  15.306  1.00 29.55  ? 124  ASP F N   1 
ATOM   6390 C  CA  . ASP F 1 124 ? -49.199 51.575  14.292  1.00 26.68  ? 124  ASP F CA  1 
ATOM   6391 C  C   . ASP F 1 124 ? -48.409 50.439  13.646  1.00 27.08  ? 124  ASP F C   1 
ATOM   6392 O  O   . ASP F 1 124 ? -47.283 50.645  13.169  1.00 24.29  ? 124  ASP F O   1 
ATOM   6393 C  CB  . ASP F 1 124 ? -49.522 52.659  13.256  1.00 28.13  ? 124  ASP F CB  1 
ATOM   6394 C  CG  . ASP F 1 124 ? -50.441 52.185  12.141  1.00 27.64  ? 124  ASP F CG  1 
ATOM   6395 O  OD1 . ASP F 1 124 ? -50.567 50.976  11.896  1.00 27.86  ? 124  ASP F OD1 1 
ATOM   6396 O  OD2 . ASP F 1 124 ? -51.027 53.049  11.473  1.00 31.99  ? 124  ASP F OD2 1 
ATOM   6397 N  N   . ASP F 1 125 ? -48.980 49.236  13.655  1.00 27.92  ? 125  ASP F N   1 
ATOM   6398 C  CA  . ASP F 1 125 ? -48.305 48.085  13.066  1.00 26.19  ? 125  ASP F CA  1 
ATOM   6399 C  C   . ASP F 1 125 ? -48.634 47.943  11.566  1.00 25.81  ? 125  ASP F C   1 
ATOM   6400 O  O   . ASP F 1 125 ? -48.367 46.924  10.959  1.00 26.54  ? 125  ASP F O   1 
ATOM   6401 C  CB  . ASP F 1 125 ? -48.589 46.801  13.867  1.00 23.03  ? 125  ASP F CB  1 
ATOM   6402 C  CG  . ASP F 1 125 ? -50.040 46.312  13.742  1.00 29.17  ? 125  ASP F CG  1 
ATOM   6403 O  OD1 . ASP F 1 125 ? -50.756 46.678  12.777  1.00 27.57  ? 125  ASP F OD1 1 
ATOM   6404 O  OD2 . ASP F 1 125 ? -50.460 45.525  14.614  1.00 33.71  ? 125  ASP F OD2 1 
ATOM   6405 N  N   . LEU F 1 126 ? -49.234 48.979  10.992  1.00 26.75  ? 126  LEU F N   1 
ATOM   6406 C  CA  . LEU F 1 126 ? -49.508 49.031  9.554   1.00 28.09  ? 126  LEU F CA  1 
ATOM   6407 C  C   . LEU F 1 126 ? -50.323 47.840  9.028   1.00 29.95  ? 126  LEU F C   1 
ATOM   6408 O  O   . LEU F 1 126 ? -50.186 47.446  7.864   1.00 30.23  ? 126  LEU F O   1 
ATOM   6409 C  CB  . LEU F 1 126 ? -48.196 49.179  8.771   1.00 31.62  ? 126  LEU F CB  1 
ATOM   6410 C  CG  . LEU F 1 126 ? -47.140 50.094  9.424   1.00 28.72  ? 126  LEU F CG  1 
ATOM   6411 C  CD1 . LEU F 1 126 ? -45.845 50.130  8.613   1.00 21.05  ? 126  LEU F CD1 1 
ATOM   6412 C  CD2 . LEU F 1 126 ? -47.701 51.492  9.611   1.00 26.86  ? 126  LEU F CD2 1 
ATOM   6413 N  N   . GLY F 1 127 ? -51.179 47.280  9.882   1.00 29.12  ? 127  GLY F N   1 
ATOM   6414 C  CA  . GLY F 1 127 ? -52.093 46.235  9.461   1.00 25.69  ? 127  GLY F CA  1 
ATOM   6415 C  C   . GLY F 1 127 ? -51.453 44.856  9.411   1.00 28.83  ? 127  GLY F C   1 
ATOM   6416 O  O   . GLY F 1 127 ? -51.999 43.948  8.802   1.00 27.28  ? 127  GLY F O   1 
ATOM   6417 N  N   . LYS F 1 128 ? -50.306 44.695  10.069  1.00 28.33  ? 128  LYS F N   1 
ATOM   6418 C  CA  . LYS F 1 128 ? -49.541 43.454  10.000  1.00 27.78  ? 128  LYS F CA  1 
ATOM   6419 C  C   . LYS F 1 128 ? -49.281 42.828  11.380  1.00 34.70  ? 128  LYS F C   1 
ATOM   6420 O  O   . LYS F 1 128 ? -48.289 42.111  11.583  1.00 33.63  ? 128  LYS F O   1 
ATOM   6421 C  CB  . LYS F 1 128 ? -48.224 43.720  9.260   1.00 29.13  ? 128  LYS F CB  1 
ATOM   6422 C  CG  . LYS F 1 128 ? -48.489 44.394  7.900   1.00 37.35  ? 128  LYS F CG  1 
ATOM   6423 C  CD  . LYS F 1 128 ? -47.441 44.128  6.830   1.00 40.59  ? 128  LYS F CD  1 
ATOM   6424 C  CE  . LYS F 1 128 ? -47.770 44.922  5.559   1.00 48.46  ? 128  LYS F CE  1 
ATOM   6425 N  NZ  . LYS F 1 128 ? -48.003 46.401  5.841   1.00 43.03  ? 128  LYS F NZ  1 
ATOM   6426 N  N   . GLY F 1 129 ? -50.169 43.111  12.328  1.00 32.73  ? 129  GLY F N   1 
ATOM   6427 C  CA  . GLY F 1 129 ? -50.032 42.579  13.668  1.00 32.59  ? 129  GLY F CA  1 
ATOM   6428 C  C   . GLY F 1 129 ? -50.654 41.196  13.817  1.00 37.83  ? 129  GLY F C   1 
ATOM   6429 O  O   . GLY F 1 129 ? -50.570 40.600  14.884  1.00 34.62  ? 129  GLY F O   1 
ATOM   6430 N  N   . GLY F 1 130 ? -51.287 40.685  12.761  1.00 31.15  ? 130  GLY F N   1 
ATOM   6431 C  CA  . GLY F 1 130 ? -51.777 39.325  12.802  1.00 31.42  ? 130  GLY F CA  1 
ATOM   6432 C  C   . GLY F 1 130 ? -53.053 39.120  13.600  1.00 38.82  ? 130  GLY F C   1 
ATOM   6433 O  O   . GLY F 1 130 ? -53.293 38.024  14.102  1.00 39.67  ? 130  GLY F O   1 
ATOM   6434 N  N   . ASN F 1 131 ? -53.869 40.165  13.723  1.00 38.33  ? 131  ASN F N   1 
ATOM   6435 C  CA  . ASN F 1 131 ? -55.213 40.036  14.291  1.00 35.33  ? 131  ASN F CA  1 
ATOM   6436 C  C   . ASN F 1 131 ? -56.198 41.037  13.673  1.00 38.76  ? 131  ASN F C   1 
ATOM   6437 O  O   . ASN F 1 131 ? -55.820 41.866  12.834  1.00 38.18  ? 131  ASN F O   1 
ATOM   6438 C  CB  . ASN F 1 131 ? -55.193 40.168  15.812  1.00 32.38  ? 131  ASN F CB  1 
ATOM   6439 C  CG  . ASN F 1 131 ? -54.662 41.507  16.270  1.00 42.33  ? 131  ASN F CG  1 
ATOM   6440 O  OD1 . ASN F 1 131 ? -54.970 42.534  15.670  1.00 38.03  ? 131  ASN F OD1 1 
ATOM   6441 N  ND2 . ASN F 1 131 ? -53.859 41.508  17.347  1.00 39.80  ? 131  ASN F ND2 1 
ATOM   6442 N  N   . GLU F 1 132 ? -57.459 40.942  14.083  1.00 39.56  ? 132  GLU F N   1 
ATOM   6443 C  CA  . GLU F 1 132 ? -58.509 41.847  13.620  1.00 43.08  ? 132  GLU F CA  1 
ATOM   6444 C  C   . GLU F 1 132 ? -58.275 43.295  14.027  1.00 39.39  ? 132  GLU F C   1 
ATOM   6445 O  O   . GLU F 1 132 ? -58.633 44.208  13.285  1.00 42.83  ? 132  GLU F O   1 
ATOM   6446 C  CB  . GLU F 1 132 ? -59.882 41.406  14.133  1.00 45.34  ? 132  GLU F CB  1 
ATOM   6447 C  CG  . GLU F 1 132 ? -60.592 40.397  13.257  1.00 58.98  ? 132  GLU F CG  1 
ATOM   6448 C  CD  . GLU F 1 132 ? -61.209 41.033  12.021  1.00 74.12  ? 132  GLU F CD  1 
ATOM   6449 O  OE1 . GLU F 1 132 ? -62.102 41.906  12.184  1.00 72.35  ? 132  GLU F OE1 1 
ATOM   6450 O  OE2 . GLU F 1 132 ? -60.798 40.655  10.893  1.00 67.76  ? 132  GLU F OE2 1 
ATOM   6451 N  N   . GLU F 1 133 ? -57.694 43.515  15.200  1.00 36.10  ? 133  GLU F N   1 
ATOM   6452 C  CA  . GLU F 1 133 ? -57.476 44.886  15.649  1.00 40.35  ? 133  GLU F CA  1 
ATOM   6453 C  C   . GLU F 1 133 ? -56.487 45.605  14.719  1.00 35.79  ? 133  GLU F C   1 
ATOM   6454 O  O   . GLU F 1 133 ? -56.647 46.796  14.422  1.00 35.02  ? 133  GLU F O   1 
ATOM   6455 C  CB  . GLU F 1 133 ? -57.005 44.940  17.108  1.00 36.08  ? 133  GLU F CB  1 
ATOM   6456 C  CG  . GLU F 1 133 ? -57.242 46.291  17.787  1.00 37.72  ? 133  GLU F CG  1 
ATOM   6457 C  CD  . GLU F 1 133 ? -58.696 46.751  17.674  1.00 48.94  ? 133  GLU F CD  1 
ATOM   6458 O  OE1 . GLU F 1 133 ? -59.622 45.923  17.852  1.00 53.34  ? 133  GLU F OE1 1 
ATOM   6459 O  OE2 . GLU F 1 133 ? -58.918 47.944  17.388  1.00 48.48  ? 133  GLU F OE2 1 
ATOM   6460 N  N   . SER F 1 134 ? -55.488 44.862  14.254  1.00 29.58  ? 134  SER F N   1 
ATOM   6461 C  CA  . SER F 1 134 ? -54.464 45.394  13.366  1.00 32.15  ? 134  SER F CA  1 
ATOM   6462 C  C   . SER F 1 134 ? -55.115 45.905  12.084  1.00 32.19  ? 134  SER F C   1 
ATOM   6463 O  O   . SER F 1 134 ? -54.768 46.945  11.545  1.00 28.68  ? 134  SER F O   1 
ATOM   6464 C  CB  . SER F 1 134 ? -53.483 44.283  13.024  1.00 33.69  ? 134  SER F CB  1 
ATOM   6465 O  OG  . SER F 1 134 ? -52.548 44.718  12.074  1.00 27.80  ? 134  SER F OG  1 
ATOM   6466 N  N   . THR F 1 135 ? -56.081 45.134  11.628  1.00 33.49  ? 135  THR F N   1 
ATOM   6467 C  CA  . THR F 1 135 ? -56.786 45.366  10.395  1.00 32.69  ? 135  THR F CA  1 
ATOM   6468 C  C   . THR F 1 135 ? -57.621 46.629  10.521  1.00 34.58  ? 135  THR F C   1 
ATOM   6469 O  O   . THR F 1 135 ? -58.077 47.184  9.521   1.00 34.89  ? 135  THR F O   1 
ATOM   6470 C  CB  . THR F 1 135 ? -57.690 44.127  10.114  1.00 37.50  ? 135  THR F CB  1 
ATOM   6471 O  OG1 . THR F 1 135 ? -56.964 43.180  9.323   1.00 36.19  ? 135  THR F OG1 1 
ATOM   6472 C  CG2 . THR F 1 135 ? -58.989 44.508  9.417   1.00 42.57  ? 135  THR F CG2 1 
ATOM   6473 N  N   . LYS F 1 136 ? -57.831 47.085  11.751  1.00 30.72  ? 136  LYS F N   1 
ATOM   6474 C  CA  . LYS F 1 136 ? -58.719 48.223  11.957  1.00 33.51  ? 136  LYS F CA  1 
ATOM   6475 C  C   . LYS F 1 136 ? -57.983 49.470  12.422  1.00 34.32  ? 136  LYS F C   1 
ATOM   6476 O  O   . LYS F 1 136 ? -58.248 50.579  11.930  1.00 28.47  ? 136  LYS F O   1 
ATOM   6477 C  CB  . LYS F 1 136 ? -59.819 47.892  12.969  1.00 38.72  ? 136  LYS F CB  1 
ATOM   6478 C  CG  . LYS F 1 136 ? -60.939 47.004  12.438  1.00 44.06  ? 136  LYS F CG  1 
ATOM   6479 C  CD  . LYS F 1 136 ? -62.074 46.847  13.469  1.00 45.95  ? 136  LYS F CD  1 
ATOM   6480 C  CE  . LYS F 1 136 ? -61.616 46.033  14.684  1.00 52.26  ? 136  LYS F CE  1 
ATOM   6481 N  NZ  . LYS F 1 136 ? -62.611 46.046  15.801  1.00 55.09  ? 136  LYS F NZ  1 
ATOM   6482 N  N   . THR F 1 137 ? -57.066 49.287  13.368  1.00 28.46  ? 137  THR F N   1 
ATOM   6483 C  CA  . THR F 1 137 ? -56.517 50.413  14.100  1.00 28.87  ? 137  THR F CA  1 
ATOM   6484 C  C   . THR F 1 137 ? -54.998 50.389  14.086  1.00 29.27  ? 137  THR F C   1 
ATOM   6485 O  O   . THR F 1 137 ? -54.334 51.270  14.656  1.00 25.52  ? 137  THR F O   1 
ATOM   6486 C  CB  . THR F 1 137 ? -57.014 50.406  15.574  1.00 30.28  ? 137  THR F CB  1 
ATOM   6487 O  OG1 . THR F 1 137 ? -56.736 51.671  16.171  1.00 43.26  ? 137  THR F OG1 1 
ATOM   6488 C  CG2 . THR F 1 137 ? -56.313 49.336  16.396  1.00 25.13  ? 137  THR F CG2 1 
ATOM   6489 N  N   . GLY F 1 138 ? -54.456 49.363  13.443  1.00 26.08  ? 138  GLY F N   1 
ATOM   6490 C  CA  . GLY F 1 138 ? -53.036 49.086  13.508  1.00 25.66  ? 138  GLY F CA  1 
ATOM   6491 C  C   . GLY F 1 138 ? -52.480 48.915  14.914  1.00 28.08  ? 138  GLY F C   1 
ATOM   6492 O  O   . GLY F 1 138 ? -51.306 49.211  15.148  1.00 31.15  ? 138  GLY F O   1 
ATOM   6493 N  N   . ASN F 1 139 ? -53.314 48.432  15.837  1.00 26.24  ? 139  ASN F N   1 
ATOM   6494 C  CA  . ASN F 1 139 ? -52.985 48.323  17.268  1.00 28.30  ? 139  ASN F CA  1 
ATOM   6495 C  C   . ASN F 1 139 ? -52.244 49.490  17.892  1.00 29.48  ? 139  ASN F C   1 
ATOM   6496 O  O   . ASN F 1 139 ? -51.465 49.284  18.822  1.00 25.97  ? 139  ASN F O   1 
ATOM   6497 C  CB  . ASN F 1 139 ? -52.245 47.024  17.599  1.00 27.66  ? 139  ASN F CB  1 
ATOM   6498 C  CG  . ASN F 1 139 ? -53.098 45.795  17.349  1.00 38.40  ? 139  ASN F CG  1 
ATOM   6499 O  OD1 . ASN F 1 139 ? -52.818 44.979  16.447  1.00 36.09  ? 139  ASN F OD1 1 
ATOM   6500 N  ND2 . ASN F 1 139 ? -54.158 45.664  18.129  1.00 34.67  ? 139  ASN F ND2 1 
ATOM   6501 N  N   . ALA F 1 140 ? -52.502 50.699  17.390  1.00 25.13  ? 140  ALA F N   1 
ATOM   6502 C  CA  . ALA F 1 140 ? -51.927 51.934  17.946  1.00 27.69  ? 140  ALA F CA  1 
ATOM   6503 C  C   . ALA F 1 140 ? -52.360 52.275  19.393  1.00 26.87  ? 140  ALA F C   1 
ATOM   6504 O  O   . ALA F 1 140 ? -51.734 53.094  20.058  1.00 30.53  ? 140  ALA F O   1 
ATOM   6505 C  CB  . ALA F 1 140 ? -52.230 53.125  17.015  1.00 29.78  ? 140  ALA F CB  1 
ATOM   6506 N  N   . GLY F 1 141 ? -53.446 51.685  19.864  1.00 29.41  ? 141  GLY F N   1 
ATOM   6507 C  CA  . GLY F 1 141 ? -53.872 51.900  21.236  1.00 27.87  ? 141  GLY F CA  1 
ATOM   6508 C  C   . GLY F 1 141 ? -54.601 53.204  21.509  1.00 31.92  ? 141  GLY F C   1 
ATOM   6509 O  O   . GLY F 1 141 ? -55.267 53.778  20.640  1.00 34.81  ? 141  GLY F O   1 
ATOM   6510 N  N   . SER F 1 142 ? -54.480 53.670  22.743  1.00 31.06  ? 142  SER F N   1 
ATOM   6511 C  CA  . SER F 1 142 ? -55.249 54.823  23.227  1.00 34.88  ? 142  SER F CA  1 
ATOM   6512 C  C   . SER F 1 142 ? -54.877 56.120  22.526  1.00 29.22  ? 142  SER F C   1 
ATOM   6513 O  O   . SER F 1 142 ? -53.815 56.246  21.945  1.00 33.23  ? 142  SER F O   1 
ATOM   6514 C  CB  . SER F 1 142 ? -55.047 54.995  24.740  1.00 31.82  ? 142  SER F CB  1 
ATOM   6515 O  OG  . SER F 1 142 ? -53.684 55.270  25.029  1.00 31.00  ? 142  SER F OG  1 
ATOM   6516 N  N   . ARG F 1 143 ? -55.762 57.095  22.615  1.00 35.13  ? 143  ARG F N   1 
ATOM   6517 C  CA  . ARG F 1 143 ? -55.581 58.363  21.926  1.00 34.27  ? 143  ARG F CA  1 
ATOM   6518 C  C   . ARG F 1 143 ? -54.965 59.371  22.903  1.00 38.13  ? 143  ARG F C   1 
ATOM   6519 O  O   . ARG F 1 143 ? -55.622 59.818  23.842  1.00 37.48  ? 143  ARG F O   1 
ATOM   6520 C  CB  . ARG F 1 143 ? -56.942 58.842  21.388  1.00 35.12  ? 143  ARG F CB  1 
ATOM   6521 C  CG  . ARG F 1 143 ? -57.647 57.780  20.507  1.00 31.59  ? 143  ARG F CG  1 
ATOM   6522 C  CD  . ARG F 1 143 ? -59.007 58.184  19.937  1.00 27.07  ? 143  ARG F CD  1 
ATOM   6523 N  NE  . ARG F 1 143 ? -59.564 57.066  19.176  1.00 35.51  ? 143  ARG F NE  1 
ATOM   6524 C  CZ  . ARG F 1 143 ? -60.720 57.063  18.511  1.00 31.27  ? 143  ARG F CZ  1 
ATOM   6525 N  NH1 . ARG F 1 143 ? -61.503 58.123  18.491  1.00 28.51  ? 143  ARG F NH1 1 
ATOM   6526 N  NH2 . ARG F 1 143 ? -61.098 55.969  17.872  1.00 26.49  ? 143  ARG F NH2 1 
ATOM   6527 N  N   . LEU F 1 144 ? -53.696 59.707  22.697  1.00 33.80  ? 144  LEU F N   1 
ATOM   6528 C  CA  . LEU F 1 144 ? -52.980 60.560  23.636  1.00 34.74  ? 144  LEU F CA  1 
ATOM   6529 C  C   . LEU F 1 144 ? -53.369 62.029  23.527  1.00 39.26  ? 144  LEU F C   1 
ATOM   6530 O  O   . LEU F 1 144 ? -53.376 62.754  24.520  1.00 42.06  ? 144  LEU F O   1 
ATOM   6531 C  CB  . LEU F 1 144 ? -51.477 60.445  23.404  1.00 37.22  ? 144  LEU F CB  1 
ATOM   6532 C  CG  . LEU F 1 144 ? -50.701 59.363  24.150  1.00 37.16  ? 144  LEU F CG  1 
ATOM   6533 C  CD1 . LEU F 1 144 ? -51.616 58.381  24.923  1.00 31.88  ? 144  LEU F CD1 1 
ATOM   6534 C  CD2 . LEU F 1 144 ? -49.812 58.654  23.170  1.00 32.22  ? 144  LEU F CD2 1 
ATOM   6535 N  N   . ALA F 1 145 ? -53.669 62.468  22.312  1.00 37.26  ? 145  ALA F N   1 
ATOM   6536 C  CA  . ALA F 1 145 ? -53.941 63.871  22.067  1.00 36.17  ? 145  ALA F CA  1 
ATOM   6537 C  C   . ALA F 1 145 ? -54.543 64.035  20.690  1.00 35.87  ? 145  ALA F C   1 
ATOM   6538 O  O   . ALA F 1 145 ? -54.258 63.260  19.782  1.00 37.07  ? 145  ALA F O   1 
ATOM   6539 C  CB  . ALA F 1 145 ? -52.660 64.691  22.179  1.00 34.00  ? 145  ALA F CB  1 
ATOM   6540 N  N   . CYS F 1 146 ? -55.356 65.066  20.525  1.00 39.48  ? 146  CYS F N   1 
ATOM   6541 C  CA  . CYS F 1 146 ? -55.994 65.321  19.247  1.00 36.38  ? 146  CYS F CA  1 
ATOM   6542 C  C   . CYS F 1 146 ? -56.405 66.780  19.131  1.00 38.67  ? 146  CYS F C   1 
ATOM   6543 O  O   . CYS F 1 146 ? -56.410 67.522  20.115  1.00 40.69  ? 146  CYS F O   1 
ATOM   6544 C  CB  . CYS F 1 146 ? -57.216 64.426  19.096  1.00 36.18  ? 146  CYS F CB  1 
ATOM   6545 S  SG  . CYS F 1 146 ? -58.422 64.695  20.387  1.00 38.12  ? 146  CYS F SG  1 
ATOM   6546 N  N   . GLY F 1 147 ? -56.748 67.181  17.914  1.00 38.40  ? 147  GLY F N   1 
ATOM   6547 C  CA  . GLY F 1 147 ? -57.213 68.526  17.631  1.00 35.33  ? 147  GLY F CA  1 
ATOM   6548 C  C   . GLY F 1 147 ? -57.908 68.517  16.288  1.00 36.95  ? 147  GLY F C   1 
ATOM   6549 O  O   . GLY F 1 147 ? -57.591 67.681  15.434  1.00 37.38  ? 147  GLY F O   1 
ATOM   6550 N  N   . VAL F 1 148 ? -58.867 69.418  16.099  1.00 34.37  ? 148  VAL F N   1 
ATOM   6551 C  CA  . VAL F 1 148 ? -59.575 69.512  14.826  1.00 33.90  ? 148  VAL F CA  1 
ATOM   6552 C  C   . VAL F 1 148 ? -58.737 70.241  13.777  1.00 35.43  ? 148  VAL F C   1 
ATOM   6553 O  O   . VAL F 1 148 ? -58.155 71.293  14.042  1.00 43.08  ? 148  VAL F O   1 
ATOM   6554 C  CB  . VAL F 1 148 ? -60.932 70.211  14.979  1.00 38.15  ? 148  VAL F CB  1 
ATOM   6555 C  CG1 . VAL F 1 148 ? -61.701 70.214  13.632  1.00 30.95  ? 148  VAL F CG1 1 
ATOM   6556 C  CG2 . VAL F 1 148 ? -61.735 69.536  16.062  1.00 33.63  ? 148  VAL F CG2 1 
ATOM   6557 N  N   . ILE F 1 149 ? -58.664 69.663  12.588  1.00 32.66  ? 149  ILE F N   1 
ATOM   6558 C  CA  . ILE F 1 149 ? -57.813 70.187  11.535  1.00 35.29  ? 149  ILE F CA  1 
ATOM   6559 C  C   . ILE F 1 149 ? -58.459 71.423  10.953  1.00 39.34  ? 149  ILE F C   1 
ATOM   6560 O  O   . ILE F 1 149 ? -59.590 71.366  10.466  1.00 38.39  ? 149  ILE F O   1 
ATOM   6561 C  CB  . ILE F 1 149 ? -57.619 69.144  10.420  1.00 37.76  ? 149  ILE F CB  1 
ATOM   6562 C  CG1 . ILE F 1 149 ? -57.046 67.840  11.002  1.00 33.87  ? 149  ILE F CG1 1 
ATOM   6563 C  CG2 . ILE F 1 149 ? -56.766 69.720  9.279   1.00 35.62  ? 149  ILE F CG2 1 
ATOM   6564 C  CD1 . ILE F 1 149 ? -56.933 66.702  9.997   1.00 30.98  ? 149  ILE F CD1 1 
ATOM   6565 N  N   . GLY F 1 150 ? -57.739 72.540  10.993  1.00 42.23  ? 150  GLY F N   1 
ATOM   6566 C  CA  . GLY F 1 150 ? -58.316 73.814  10.598  1.00 39.57  ? 150  GLY F CA  1 
ATOM   6567 C  C   . GLY F 1 150 ? -57.670 74.489  9.405   1.00 39.52  ? 150  GLY F C   1 
ATOM   6568 O  O   . GLY F 1 150 ? -56.532 74.182  9.032   1.00 40.73  ? 150  GLY F O   1 
ATOM   6569 N  N   . ILE F 1 151 ? -58.421 75.403  8.796   1.00 40.25  ? 151  ILE F N   1 
ATOM   6570 C  CA  . ILE F 1 151 ? -57.923 76.249  7.731   1.00 37.01  ? 151  ILE F CA  1 
ATOM   6571 C  C   . ILE F 1 151 ? -56.911 77.222  8.319   1.00 39.27  ? 151  ILE F C   1 
ATOM   6572 O  O   . ILE F 1 151 ? -57.132 77.751  9.413   1.00 40.69  ? 151  ILE F O   1 
ATOM   6573 C  CB  . ILE F 1 151 ? -59.059 77.065  7.138   1.00 40.77  ? 151  ILE F CB  1 
ATOM   6574 C  CG1 . ILE F 1 151 ? -60.009 76.159  6.346   1.00 42.44  ? 151  ILE F CG1 1 
ATOM   6575 C  CG2 . ILE F 1 151 ? -58.502 78.186  6.277   1.00 41.78  ? 151  ILE F CG2 1 
ATOM   6576 C  CD1 . ILE F 1 151 ? -61.452 76.683  6.275   1.00 39.03  ? 151  ILE F CD1 1 
ATOM   6577 N  N   . ALA F 1 152 ? -55.814 77.457  7.595   1.00 38.33  ? 152  ALA F N   1 
ATOM   6578 C  CA  . ALA F 1 152 ? -54.731 78.315  8.077   1.00 44.63  ? 152  ALA F CA  1 
ATOM   6579 C  C   . ALA F 1 152 ? -54.265 79.377  7.075   1.00 48.73  ? 152  ALA F C   1 
ATOM   6580 O  O   . ALA F 1 152 ? -54.500 79.272  5.868   1.00 43.77  ? 152  ALA F O   1 
ATOM   6581 C  CB  . ALA F 1 152 ? -53.537 77.461  8.533   1.00 40.97  ? 152  ALA F CB  1 
ATOM   6582 N  N   . GLN F 1 153 ? -53.571 80.387  7.591   1.00 54.13  ? 153  GLN F N   1 
ATOM   6583 C  CA  . GLN F 1 153 ? -53.078 81.491  6.769   1.00 57.08  ? 153  GLN F CA  1 
ATOM   6584 C  C   . GLN F 1 153 ? -51.877 81.116  5.892   1.00 60.34  ? 153  GLN F C   1 
ATOM   6585 O  O   . GLN F 1 153 ? -51.025 80.296  6.261   1.00 61.34  ? 153  GLN F O   1 
ATOM   6586 C  CB  . GLN F 1 153 ? -52.729 82.689  7.653   1.00 60.58  ? 153  GLN F CB  1 
ATOM   6587 C  CG  . GLN F 1 153 ? -52.366 83.947  6.879   1.00 61.35  ? 153  GLN F CG  1 
ATOM   6588 C  CD  . GLN F 1 153 ? -52.268 85.162  7.783   1.00 67.35  ? 153  GLN F CD  1 
ATOM   6589 O  OE1 . GLN F 1 153 ? -53.036 86.118  7.644   1.00 67.65  ? 153  GLN F OE1 1 
ATOM   6590 N  NE2 . GLN F 1 153 ? -51.330 85.125  8.729   1.00 62.17  ? 153  GLN F NE2 1 
ATOM   6591 O  OXT . GLN F 1 153 ? -51.732 81.638  4.779   1.00 59.60  ? 153  GLN F OXT 1 
HETATM 6592 ZN ZN  . ZN  G 2 .   ? -30.633 55.971  3.110   1.00 23.94  ? 1001 ZN  A ZN  1 
HETATM 6593 ZN ZN  . ZN  H 2 .   ? 6.410   49.528  -9.296  1.00 30.63  ? 1001 ZN  B ZN  1 
HETATM 6594 ZN ZN  . ZN  I 2 .   ? -33.779 78.140  -11.428 1.00 98.39  ? 1001 ZN  C ZN  1 
HETATM 6595 ZN ZN  . ZN  J 2 .   ? 1.025   89.226  4.929   1.00 38.82  ? 1001 ZN  D ZN  1 
HETATM 6596 ZN ZN  . ZN  K 2 .   ? -67.747 91.200  11.662  1.00 60.90  ? 1001 ZN  E ZN  1 
HETATM 6597 ZN ZN  . ZN  L 2 .   ? -56.476 53.041  9.621   1.00 25.50  ? 1001 ZN  F ZN  1 
HETATM 6598 O  O   . HOH M 3 .   ? -17.026 50.958  17.481  1.00 25.46  ? 154  HOH A O   1 
HETATM 6599 O  O   . HOH M 3 .   ? -31.212 44.340  5.299   1.00 31.39  ? 155  HOH A O   1 
HETATM 6600 O  O   . HOH M 3 .   ? -31.771 51.073  4.364   1.00 26.84  ? 156  HOH A O   1 
HETATM 6601 O  O   . HOH M 3 .   ? -10.356 58.081  3.179   1.00 25.27  ? 157  HOH A O   1 
HETATM 6602 O  O   . HOH M 3 .   ? -16.812 54.782  16.614  1.00 28.50  ? 158  HOH A O   1 
HETATM 6603 O  O   . HOH M 3 .   ? -38.552 55.539  13.506  1.00 29.52  ? 159  HOH A O   1 
HETATM 6604 O  O   . HOH M 3 .   ? -11.553 48.890  3.640   1.00 23.01  ? 160  HOH A O   1 
HETATM 6605 O  O   . HOH M 3 .   ? -28.416 59.857  4.423   1.00 22.40  ? 161  HOH A O   1 
HETATM 6606 O  O   . HOH M 3 .   ? -16.342 53.818  -8.131  1.00 35.69  ? 162  HOH A O   1 
HETATM 6607 O  O   . HOH M 3 .   ? -19.834 37.780  -1.207  1.00 33.47  ? 163  HOH A O   1 
HETATM 6608 O  O   . HOH M 3 .   ? -39.039 55.627  1.272   1.00 27.99  ? 164  HOH A O   1 
HETATM 6609 O  O   . HOH M 3 .   ? -24.125 50.939  -11.751 1.00 37.07  ? 165  HOH A O   1 
HETATM 6610 O  O   . HOH M 3 .   ? -14.955 43.303  17.783  1.00 34.13  ? 166  HOH A O   1 
HETATM 6611 O  O   . HOH M 3 .   ? -40.465 51.702  10.266  1.00 35.72  ? 167  HOH A O   1 
HETATM 6612 O  O   . HOH M 3 .   ? -31.298 43.954  -0.852  1.00 35.70  ? 168  HOH A O   1 
HETATM 6613 O  O   . HOH M 3 .   ? -14.722 64.396  0.779   1.00 34.07  ? 169  HOH A O   1 
HETATM 6614 O  O   . HOH M 3 .   ? -24.555 35.013  14.529  1.00 41.04  ? 170  HOH A O   1 
HETATM 6615 O  O   . HOH M 3 .   ? -35.826 49.139  -4.948  1.00 40.25  ? 171  HOH A O   1 
HETATM 6616 O  O   . HOH M 3 .   ? -12.211 41.888  -8.963  1.00 38.53  ? 172  HOH A O   1 
HETATM 6617 O  O   . HOH M 3 .   ? -19.531 42.555  -16.756 1.00 45.09  ? 173  HOH A O   1 
HETATM 6618 O  O   . HOH M 3 .   ? -11.180 51.497  4.603   1.00 29.93  ? 174  HOH A O   1 
HETATM 6619 O  O   . HOH M 3 .   ? -20.270 55.313  -8.679  1.00 38.52  ? 175  HOH A O   1 
HETATM 6620 O  O   . HOH M 3 .   ? -36.136 64.399  12.616  1.00 40.31  ? 176  HOH A O   1 
HETATM 6621 O  O   . HOH M 3 .   ? -33.686 45.222  17.195  1.00 37.69  ? 177  HOH A O   1 
HETATM 6622 O  O   . HOH M 3 .   ? -35.381 46.652  15.635  1.00 33.08  ? 178  HOH A O   1 
HETATM 6623 O  O   . HOH M 3 .   ? -32.515 50.312  17.796  1.00 37.03  ? 179  HOH A O   1 
HETATM 6624 O  O   . HOH M 3 .   ? -32.870 61.787  1.942   1.00 35.58  ? 180  HOH A O   1 
HETATM 6625 O  O   . HOH M 3 .   ? -31.005 47.787  18.021  1.00 38.36  ? 181  HOH A O   1 
HETATM 6626 O  O   . HOH M 3 .   ? -21.579 59.170  14.082  1.00 24.63  ? 182  HOH A O   1 
HETATM 6627 O  O   . HOH M 3 .   ? -24.466 60.051  11.540  1.00 33.56  ? 183  HOH A O   1 
HETATM 6628 O  O   . HOH M 3 .   ? -38.356 58.134  4.201   1.00 35.55  ? 184  HOH A O   1 
HETATM 6629 O  O   . HOH M 3 .   ? -33.560 53.569  -7.441  1.00 42.47  ? 185  HOH A O   1 
HETATM 6630 O  O   . HOH M 3 .   ? -34.100 53.370  15.417  1.00 39.23  ? 186  HOH A O   1 
HETATM 6631 O  O   . HOH M 3 .   ? -30.251 57.347  -5.047  1.00 35.02  ? 187  HOH A O   1 
HETATM 6632 O  O   . HOH M 3 .   ? -13.555 39.722  -1.448  1.00 38.93  ? 188  HOH A O   1 
HETATM 6633 O  O   . HOH M 3 .   ? -31.284 42.493  3.642   1.00 29.75  ? 189  HOH A O   1 
HETATM 6634 O  O   . HOH M 3 .   ? -15.526 57.478  13.505  1.00 40.78  ? 190  HOH A O   1 
HETATM 6635 O  O   . HOH M 3 .   ? -39.665 50.228  12.226  1.00 39.37  ? 191  HOH A O   1 
HETATM 6636 O  O   . HOH M 3 .   ? -26.966 58.008  18.396  1.00 36.40  ? 192  HOH A O   1 
HETATM 6637 O  O   . HOH M 3 .   ? -9.157  60.623  11.045  1.00 39.94  ? 193  HOH A O   1 
HETATM 6638 O  O   . HOH M 3 .   ? -34.196 45.437  5.187   1.00 30.95  ? 194  HOH A O   1 
HETATM 6639 O  O   . HOH N 3 .   ? -8.601  55.851  2.873   1.00 22.15  ? 154  HOH B O   1 
HETATM 6640 O  O   . HOH N 3 .   ? -10.263 46.649  2.454   1.00 27.19  ? 155  HOH B O   1 
HETATM 6641 O  O   . HOH N 3 .   ? 5.616   66.102  -9.339  1.00 35.65  ? 156  HOH B O   1 
HETATM 6642 O  O   . HOH N 3 .   ? -7.318  44.794  -10.783 1.00 34.07  ? 157  HOH B O   1 
HETATM 6643 O  O   . HOH N 3 .   ? 8.848   55.022  10.934  1.00 29.40  ? 158  HOH B O   1 
HETATM 6644 O  O   . HOH N 3 .   ? 8.159   54.758  -8.582  1.00 31.37  ? 159  HOH B O   1 
HETATM 6645 O  O   . HOH N 3 .   ? 1.454   48.696  -15.912 1.00 35.36  ? 160  HOH B O   1 
HETATM 6646 O  O   . HOH N 3 .   ? 2.179   51.083  -17.002 1.00 27.70  ? 161  HOH B O   1 
HETATM 6647 O  O   . HOH N 3 .   ? 6.774   62.565  12.589  1.00 29.58  ? 162  HOH B O   1 
HETATM 6648 O  O   . HOH N 3 .   ? -7.522  55.757  -17.075 1.00 37.22  ? 163  HOH B O   1 
HETATM 6649 O  O   . HOH N 3 .   ? -15.018 63.670  -7.008  1.00 36.51  ? 164  HOH B O   1 
HETATM 6650 O  O   . HOH N 3 .   ? -1.808  45.355  -11.408 1.00 33.10  ? 165  HOH B O   1 
HETATM 6651 O  O   . HOH N 3 .   ? 5.528   45.174  -7.200  1.00 31.69  ? 166  HOH B O   1 
HETATM 6652 O  O   . HOH N 3 .   ? 21.985  53.024  -8.769  1.00 28.89  ? 167  HOH B O   1 
HETATM 6653 O  O   . HOH N 3 .   ? -1.845  40.044  -8.596  1.00 41.50  ? 168  HOH B O   1 
HETATM 6654 O  O   . HOH N 3 .   ? 0.905   46.257  7.771   1.00 43.36  ? 169  HOH B O   1 
HETATM 6655 O  O   . HOH N 3 .   ? 8.767   61.518  -6.358  1.00 35.38  ? 170  HOH B O   1 
HETATM 6656 O  O   . HOH N 3 .   ? 2.180   48.462  8.816   1.00 47.48  ? 171  HOH B O   1 
HETATM 6657 O  O   . HOH N 3 .   ? -15.700 66.585  -6.889  1.00 49.12  ? 172  HOH B O   1 
HETATM 6658 O  O   . HOH N 3 .   ? -4.274  68.186  -4.444  1.00 37.46  ? 173  HOH B O   1 
HETATM 6659 O  O   . HOH N 3 .   ? 7.585   64.311  -0.609  1.00 33.83  ? 174  HOH B O   1 
HETATM 6660 O  O   . HOH N 3 .   ? 9.617   55.509  8.690   1.00 35.61  ? 175  HOH B O   1 
HETATM 6661 O  O   . HOH N 3 .   ? 2.753   59.792  12.865  1.00 39.43  ? 176  HOH B O   1 
HETATM 6662 O  O   . HOH N 3 .   ? 11.446  58.826  -12.522 1.00 33.61  ? 177  HOH B O   1 
HETATM 6663 O  O   . HOH N 3 .   ? 16.657  51.284  -1.431  1.00 35.00  ? 178  HOH B O   1 
HETATM 6664 O  O   . HOH N 3 .   ? 7.935   69.915  9.941   1.00 39.41  ? 179  HOH B O   1 
HETATM 6665 O  O   . HOH N 3 .   ? 4.073   64.905  -14.667 1.00 38.46  ? 180  HOH B O   1 
HETATM 6666 O  O   . HOH N 3 .   ? -7.736  40.793  -2.511  1.00 37.50  ? 181  HOH B O   1 
HETATM 6667 O  O   . HOH N 3 .   ? -0.060  70.375  -4.282  1.00 35.58  ? 182  HOH B O   1 
HETATM 6668 O  O   . HOH N 3 .   ? -4.869  39.937  -2.402  1.00 43.96  ? 183  HOH B O   1 
HETATM 6669 O  O   . HOH N 3 .   ? 3.989   62.344  -14.777 1.00 34.02  ? 184  HOH B O   1 
HETATM 6670 O  O   . HOH N 3 .   ? 1.462   69.500  3.777   1.00 37.64  ? 185  HOH B O   1 
HETATM 6671 O  O   . HOH N 3 .   ? 18.068  46.646  0.764   1.00 43.80  ? 186  HOH B O   1 
HETATM 6672 O  O   . HOH O 3 .   ? -21.471 88.905  1.127   1.00 35.02  ? 154  HOH C O   1 
HETATM 6673 O  O   . HOH O 3 .   ? -26.859 66.666  0.489   1.00 52.97  ? 155  HOH C O   1 
HETATM 6674 O  O   . HOH O 3 .   ? -25.708 62.055  7.101   1.00 34.89  ? 156  HOH C O   1 
HETATM 6675 O  O   . HOH O 3 .   ? -20.108 79.020  -13.795 1.00 48.55  ? 157  HOH C O   1 
HETATM 6676 O  O   . HOH O 3 .   ? -26.564 78.586  9.069   1.00 52.07  ? 158  HOH C O   1 
HETATM 6677 O  O   . HOH O 3 .   ? -31.053 96.387  -7.803  1.00 59.40  ? 159  HOH C O   1 
HETATM 6678 O  O   . HOH O 3 .   ? -25.487 68.441  -3.893  1.00 49.84  ? 160  HOH C O   1 
HETATM 6679 O  O   . HOH O 3 .   ? -21.838 63.443  7.952   1.00 35.24  ? 161  HOH C O   1 
HETATM 6680 O  O   . HOH P 3 .   ? -14.906 91.122  1.799   1.00 37.23  ? 154  HOH D O   1 
HETATM 6681 O  O   . HOH P 3 .   ? -15.901 103.055 -1.880  1.00 38.81  ? 155  HOH D O   1 
HETATM 6682 O  O   . HOH P 3 .   ? -0.326  102.415 -10.804 1.00 30.86  ? 156  HOH D O   1 
HETATM 6683 O  O   . HOH P 3 .   ? 0.777   99.675  -9.279  1.00 34.31  ? 157  HOH D O   1 
HETATM 6684 O  O   . HOH P 3 .   ? -5.702  106.665 0.255   1.00 28.76  ? 158  HOH D O   1 
HETATM 6685 O  O   . HOH P 3 .   ? -4.087  106.702 2.359   1.00 29.89  ? 159  HOH D O   1 
HETATM 6686 O  O   . HOH P 3 .   ? -19.308 88.489  2.931   1.00 33.89  ? 160  HOH D O   1 
HETATM 6687 O  O   . HOH P 3 .   ? -2.220  89.304  8.764   1.00 35.58  ? 161  HOH D O   1 
HETATM 6688 O  O   . HOH P 3 .   ? -17.265 95.737  0.334   1.00 39.68  ? 162  HOH D O   1 
HETATM 6689 O  O   . HOH P 3 .   ? -9.221  108.803 -8.429  1.00 32.34  ? 163  HOH D O   1 
HETATM 6690 O  O   . HOH P 3 .   ? -13.125 106.892 -6.633  1.00 31.44  ? 164  HOH D O   1 
HETATM 6691 O  O   . HOH P 3 .   ? -4.458  94.481  8.273   1.00 37.66  ? 165  HOH D O   1 
HETATM 6692 O  O   . HOH P 3 .   ? -17.646 97.296  2.457   1.00 42.43  ? 166  HOH D O   1 
HETATM 6693 O  O   . HOH P 3 .   ? 2.438   95.756  -7.430  1.00 37.92  ? 167  HOH D O   1 
HETATM 6694 O  O   . HOH P 3 .   ? 6.071   102.790 -6.198  1.00 47.17  ? 168  HOH D O   1 
HETATM 6695 O  O   . HOH P 3 .   ? 8.222   83.778  -2.497  1.00 50.87  ? 169  HOH D O   1 
HETATM 6696 O  O   . HOH P 3 .   ? -4.145  109.846 -12.748 1.00 41.40  ? 170  HOH D O   1 
HETATM 6697 O  O   . HOH P 3 .   ? -17.337 97.898  -11.757 1.00 47.42  ? 171  HOH D O   1 
HETATM 6698 O  O   . HOH P 3 .   ? -1.466  104.527 -11.973 1.00 34.42  ? 172  HOH D O   1 
HETATM 6699 O  O   . HOH P 3 .   ? 4.226   101.798 6.358   1.00 41.86  ? 173  HOH D O   1 
HETATM 6700 O  O   . HOH P 3 .   ? 0.999   97.042  -10.091 1.00 39.92  ? 174  HOH D O   1 
HETATM 6701 O  O   . HOH P 3 .   ? 9.190   99.379  11.657  1.00 43.33  ? 175  HOH D O   1 
HETATM 6702 O  O   . HOH P 3 .   ? -1.113  93.014  -15.415 1.00 41.04  ? 176  HOH D O   1 
HETATM 6703 O  O   . HOH P 3 .   ? 4.060   91.303  -10.568 1.00 43.85  ? 177  HOH D O   1 
HETATM 6704 O  O   . HOH P 3 .   ? -2.439  75.556  -7.186  1.00 51.10  ? 178  HOH D O   1 
HETATM 6705 O  O   . HOH P 3 .   ? -7.769  108.101 0.100   1.00 32.13  ? 179  HOH D O   1 
HETATM 6706 O  O   . HOH Q 3 .   ? -72.460 90.389  14.244  1.00 55.31  ? 154  HOH E O   1 
HETATM 6707 O  O   . HOH Q 3 .   ? -80.684 73.803  7.492   1.00 52.45  ? 155  HOH E O   1 
HETATM 6708 O  O   . HOH Q 3 .   ? -72.521 65.492  8.432   1.00 45.02  ? 156  HOH E O   1 
HETATM 6709 O  O   . HOH Q 3 .   ? -74.765 104.038 18.993  1.00 46.07  ? 157  HOH E O   1 
HETATM 6710 O  O   . HOH R 3 .   ? -45.418 57.388  9.042   1.00 29.09  ? 154  HOH F O   1 
HETATM 6711 O  O   . HOH R 3 .   ? -61.112 55.123  3.070   1.00 28.32  ? 155  HOH F O   1 
HETATM 6712 O  O   . HOH R 3 .   ? -64.896 57.378  7.782   1.00 32.18  ? 156  HOH F O   1 
HETATM 6713 O  O   . HOH R 3 .   ? -51.823 63.421  -4.522  1.00 33.70  ? 157  HOH F O   1 
HETATM 6714 O  O   . HOH R 3 .   ? -47.338 59.213  3.778   1.00 39.45  ? 158  HOH F O   1 
HETATM 6715 O  O   . HOH R 3 .   ? -58.911 54.512  1.469   1.00 29.14  ? 159  HOH F O   1 
HETATM 6716 O  O   . HOH R 3 .   ? -56.236 73.618  15.607  1.00 41.78  ? 160  HOH F O   1 
HETATM 6717 O  O   . HOH R 3 .   ? -53.494 46.988  4.214   1.00 34.54  ? 161  HOH F O   1 
HETATM 6718 O  O   . HOH R 3 .   ? -48.630 58.712  0.222   1.00 38.34  ? 162  HOH F O   1 
HETATM 6719 O  O   . HOH R 3 .   ? -51.257 54.115  9.173   1.00 24.46  ? 163  HOH F O   1 
HETATM 6720 O  O   . HOH R 3 .   ? -48.489 44.649  16.116  1.00 33.19  ? 164  HOH F O   1 
HETATM 6721 O  O   . HOH R 3 .   ? -36.621 65.129  17.357  1.00 45.83  ? 165  HOH F O   1 
HETATM 6722 O  O   . HOH R 3 .   ? -45.643 68.328  26.440  1.00 49.01  ? 166  HOH F O   1 
HETATM 6723 O  O   . HOH R 3 .   ? -54.561 64.993  -2.416  1.00 36.80  ? 167  HOH F O   1 
HETATM 6724 O  O   . HOH R 3 .   ? -63.272 70.590  -2.112  1.00 42.20  ? 168  HOH F O   1 
HETATM 6725 O  O   . HOH R 3 .   ? -65.618 69.777  18.203  1.00 38.18  ? 169  HOH F O   1 
HETATM 6726 O  O   . HOH R 3 .   ? -58.188 41.480  17.109  1.00 38.93  ? 170  HOH F O   1 
HETATM 6727 O  O   . HOH R 3 .   ? -42.790 50.900  11.262  1.00 37.34  ? 171  HOH F O   1 
HETATM 6728 O  O   . HOH R 3 .   ? -55.223 53.828  15.731  1.00 32.46  ? 172  HOH F O   1 
HETATM 6729 O  O   . HOH R 3 .   ? -40.789 66.274  25.632  1.00 43.01  ? 173  HOH F O   1 
HETATM 6730 O  O   . HOH R 3 .   ? -52.651 41.415  10.313  1.00 35.27  ? 174  HOH F O   1 
HETATM 6731 O  O   . HOH R 3 .   ? -60.317 52.578  12.841  1.00 27.51  ? 175  HOH F O   1 
HETATM 6732 O  O   . HOH R 3 .   ? -50.064 76.164  8.872   1.00 36.61  ? 176  HOH F O   1 
HETATM 6733 O  O   . HOH R 3 .   ? -58.019 54.236  17.279  1.00 38.25  ? 177  HOH F O   1 
HETATM 6734 O  O   . HOH R 3 .   ? -61.516 48.660  9.038   1.00 36.34  ? 178  HOH F O   1 
HETATM 6735 O  O   . HOH R 3 .   ? -52.071 67.838  26.791  1.00 41.17  ? 179  HOH F O   1 
HETATM 6736 O  O   . HOH R 3 .   ? -50.360 62.455  -6.301  1.00 39.80  ? 180  HOH F O   1 
HETATM 6737 O  O   . HOH R 3 .   ? -67.806 61.910  7.515   1.00 38.17  ? 181  HOH F O   1 
HETATM 6738 O  O   . HOH R 3 .   ? -63.561 52.578  9.209   1.00 37.65  ? 182  HOH F O   1 
HETATM 6739 O  O   . HOH R 3 .   ? -46.642 60.214  -1.268  1.00 41.34  ? 183  HOH F O   1 
HETATM 6740 O  O   . HOH R 3 .   ? -63.808 48.036  7.184   1.00 43.07  ? 184  HOH F O   1 
HETATM 6741 O  O   . HOH R 3 .   ? -46.576 71.744  6.179   1.00 39.73  ? 185  HOH F O   1 
HETATM 6742 O  O   . HOH R 3 .   ? -45.665 41.481  11.074  1.00 32.84  ? 186  HOH F O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ALA 1   1   1   ALA ALA A . n 
A 1 2   MET 2   2   2   MET MET A . n 
A 1 3   LYS 3   3   3   LYS LYS A . n 
A 1 4   ALA 4   4   4   ALA ALA A . n 
A 1 5   VAL 5   5   5   VAL VAL A . n 
A 1 6   CYS 6   6   6   CYS CYS A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   LEU 8   8   8   LEU LEU A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  GLY 10  10  10  GLY GLY A . n 
A 1 11  ASP 11  11  11  ASP ASP A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  VAL 14  14  14  VAL VAL A . n 
A 1 15  GLN 15  15  15  GLN GLN A . n 
A 1 16  GLY 16  16  16  GLY GLY A . n 
A 1 17  THR 17  17  17  THR THR A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  HIS 19  19  19  HIS HIS A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  GLU 21  21  21  GLU GLU A . n 
A 1 22  GLN 22  22  22  GLN GLN A . n 
A 1 23  LYS 23  23  23  LYS LYS A . n 
A 1 24  ALA 24  24  24  ALA ALA A . n 
A 1 25  SER 25  25  25  SER SER A . n 
A 1 26  GLY 26  26  26  GLY GLY A . n 
A 1 27  GLU 27  27  27  GLU GLU A . n 
A 1 28  PRO 28  28  28  PRO PRO A . n 
A 1 29  VAL 29  29  29  VAL VAL A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  LEU 31  31  31  LEU LEU A . n 
A 1 32  SER 32  32  32  SER SER A . n 
A 1 33  GLY 33  33  33  GLY GLY A . n 
A 1 34  GLN 34  34  34  GLN GLN A . n 
A 1 35  ILE 35  35  35  ILE ILE A . n 
A 1 36  THR 36  36  36  THR THR A . n 
A 1 37  GLY 37  37  37  GLY GLY A . n 
A 1 38  LEU 38  38  38  LEU LEU A . n 
A 1 39  THR 39  39  39  THR THR A . n 
A 1 40  GLU 40  40  40  GLU GLU A . n 
A 1 41  GLY 41  41  41  GLY GLY A . n 
A 1 42  GLN 42  42  42  GLN GLN A . n 
A 1 43  HIS 43  43  43  HIS HIS A . n 
A 1 44  GLY 44  44  44  GLY GLY A . n 
A 1 45  PHE 45  45  45  PHE PHE A . n 
A 1 46  HIS 46  46  46  HIS HIS A . n 
A 1 47  VAL 47  47  47  VAL VAL A . n 
A 1 48  HIS 48  48  48  HIS HIS A . n 
A 1 49  GLN 49  49  49  GLN GLN A . n 
A 1 50  TYR 50  50  50  TYR TYR A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  THR 54  54  54  THR THR A . n 
A 1 55  GLN 55  55  55  GLN GLN A . n 
A 1 56  GLY 56  56  56  GLY GLY A . n 
A 1 57  CYS 57  57  57  CYS CYS A . n 
A 1 58  THR 58  58  58  THR THR A . n 
A 1 59  SER 59  59  59  SER SER A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  GLY 61  61  61  GLY GLY A . n 
A 1 62  PRO 62  62  62  PRO PRO A . n 
A 1 63  HIS 63  63  63  HIS HIS A . n 
A 1 64  PHE 64  64  64  PHE PHE A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  PRO 66  66  66  PRO PRO A . n 
A 1 67  HIS 67  67  67  HIS HIS A . n 
A 1 68  SER 68  68  68  SER SER A . n 
A 1 69  LYS 69  69  69  LYS LYS A . n 
A 1 70  LYS 70  70  70  LYS LYS A . n 
A 1 71  HIS 71  71  71  HIS HIS A . n 
A 1 72  GLY 72  72  72  GLY GLY 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  ALA 75  75  75  ALA ALA A . n 
A 1 76  ASP 76  76  76  ASP ASP A . n 
A 1 77  GLU 77  77  77  GLU GLU A . n 
A 1 78  GLU 78  78  78  GLU GLU A . n 
A 1 79  ARG 79  79  79  ARG ARG A . n 
A 1 80  HIS 80  80  80  HIS HIS A . n 
A 1 81  VAL 81  81  81  VAL VAL A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  ASP 83  83  83  ASP ASP A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  ASN 86  86  86  ASN ASN A . n 
A 1 87  VAL 87  87  87  VAL VAL A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  ASP 90  90  90  ASP ASP A . n 
A 1 91  LYS 91  91  91  LYS LYS A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  GLY 93  93  93  GLY GLY A . n 
A 1 94  VAL 94  94  94  VAL VAL A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  ASP 96  96  96  ASP ASP A . n 
A 1 97  VAL 97  97  97  VAL VAL A . n 
A 1 98  SER 98  98  98  SER SER A . n 
A 1 99  ILE 99  99  99  ILE ILE A . n 
A 1 100 GLU 100 100 100 GLU GLU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 SER 102 102 102 SER SER A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 ILE 104 104 104 ILE ILE A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 SER 107 107 107 SER SER A . n 
A 1 108 GLY 108 108 108 GLY GLY A . n 
A 1 109 ASP 109 109 109 ASP ASP A . n 
A 1 110 HIS 110 110 110 HIS HIS A . n 
A 1 111 CYS 111 111 111 CYS CYS A . n 
A 1 112 ILE 112 112 112 ILE ILE A . n 
A 1 113 ILE 113 113 113 ILE ILE A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 ARG 115 115 115 ARG ARG A . n 
A 1 116 THR 116 116 116 THR THR A . n 
A 1 117 LEU 117 117 117 LEU LEU A . n 
A 1 118 VAL 118 118 118 VAL VAL A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 HIS 120 120 120 HIS HIS A . n 
A 1 121 GLU 121 121 121 GLU GLU A . n 
A 1 122 LYS 122 122 122 LYS LYS A . n 
A 1 123 ALA 123 123 123 ALA ALA A . n 
A 1 124 ASP 124 124 124 ASP ASP A . n 
A 1 125 ASP 125 125 125 ASP ASP A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 GLY 127 127 127 GLY GLY A . n 
A 1 128 LYS 128 128 128 LYS LYS A . n 
A 1 129 GLY 129 129 129 GLY GLY A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ASN 131 131 131 ASN ASN A . n 
A 1 132 GLU 132 132 132 GLU GLU A . n 
A 1 133 GLU 133 133 133 GLU GLU A . n 
A 1 134 SER 134 134 134 SER SER A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 LYS 136 136 136 LYS LYS A . n 
A 1 137 THR 137 137 137 THR THR A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 ASN 139 139 139 ASN ASN A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 GLY 141 141 141 GLY GLY A . n 
A 1 142 SER 142 142 142 SER SER A . n 
A 1 143 ARG 143 143 143 ARG ARG A . n 
A 1 144 LEU 144 144 144 LEU LEU A . n 
A 1 145 ALA 145 145 145 ALA ALA A . n 
A 1 146 CYS 146 146 146 CYS CYS A . n 
A 1 147 GLY 147 147 147 GLY GLY A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 ILE 149 149 149 ILE ILE A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 ILE 151 151 151 ILE ILE A . n 
A 1 152 ALA 152 152 152 ALA ALA A . n 
A 1 153 GLN 153 153 153 GLN GLN A . n 
B 1 1   ALA 1   1   1   ALA ALA B . n 
B 1 2   MET 2   2   2   MET MET B . n 
B 1 3   LYS 3   3   3   LYS LYS B . n 
B 1 4   ALA 4   4   4   ALA ALA B . n 
B 1 5   VAL 5   5   5   VAL VAL B . n 
B 1 6   CYS 6   6   6   CYS CYS B . n 
B 1 7   VAL 7   7   7   VAL VAL B . n 
B 1 8   LEU 8   8   8   LEU LEU B . n 
B 1 9   LYS 9   9   9   LYS LYS B . n 
B 1 10  GLY 10  10  10  GLY GLY B . n 
B 1 11  ASP 11  11  11  ASP ASP B . n 
B 1 12  GLY 12  12  12  GLY GLY B . n 
B 1 13  PRO 13  13  13  PRO PRO B . n 
B 1 14  VAL 14  14  14  VAL VAL B . n 
B 1 15  GLN 15  15  15  GLN GLN B . n 
B 1 16  GLY 16  16  16  GLY GLY B . n 
B 1 17  THR 17  17  17  THR THR B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  HIS 19  19  19  HIS HIS B . n 
B 1 20  PHE 20  20  20  PHE PHE B . n 
B 1 21  GLU 21  21  21  GLU GLU B . n 
B 1 22  GLN 22  22  22  GLN GLN B . n 
B 1 23  LYS 23  23  23  LYS LYS B . n 
B 1 24  ALA 24  24  24  ALA ALA B . n 
B 1 25  SER 25  25  25  SER SER B . n 
B 1 26  GLY 26  26  26  GLY GLY B . n 
B 1 27  GLU 27  27  27  GLU GLU B . n 
B 1 28  PRO 28  28  28  PRO PRO B . n 
B 1 29  VAL 29  29  29  VAL VAL B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  LEU 31  31  31  LEU LEU B . n 
B 1 32  SER 32  32  32  SER SER B . n 
B 1 33  GLY 33  33  33  GLY GLY B . n 
B 1 34  GLN 34  34  34  GLN GLN B . n 
B 1 35  ILE 35  35  35  ILE ILE B . n 
B 1 36  THR 36  36  36  THR THR B . n 
B 1 37  GLY 37  37  37  GLY GLY B . n 
B 1 38  LEU 38  38  38  LEU LEU B . n 
B 1 39  THR 39  39  39  THR THR B . n 
B 1 40  GLU 40  40  40  GLU GLU B . n 
B 1 41  GLY 41  41  41  GLY GLY B . n 
B 1 42  GLN 42  42  42  GLN GLN B . n 
B 1 43  HIS 43  43  43  HIS HIS B . n 
B 1 44  GLY 44  44  44  GLY GLY B . n 
B 1 45  PHE 45  45  45  PHE PHE B . n 
B 1 46  HIS 46  46  46  HIS HIS B . n 
B 1 47  VAL 47  47  47  VAL VAL B . n 
B 1 48  HIS 48  48  48  HIS HIS B . n 
B 1 49  GLN 49  49  49  GLN GLN B . n 
B 1 50  TYR 50  50  50  TYR TYR B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ASP 52  52  52  ASP ASP B . n 
B 1 53  ASN 53  53  53  ASN ASN B . n 
B 1 54  THR 54  54  54  THR THR B . n 
B 1 55  GLN 55  55  55  GLN GLN B . n 
B 1 56  GLY 56  56  56  GLY GLY B . n 
B 1 57  CYS 57  57  57  CYS CYS B . n 
B 1 58  THR 58  58  58  THR THR B . n 
B 1 59  SER 59  59  59  SER SER B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  GLY 61  61  61  GLY GLY B . n 
B 1 62  PRO 62  62  62  PRO PRO B . n 
B 1 63  HIS 63  63  63  HIS HIS B . n 
B 1 64  PHE 64  64  64  PHE PHE B . n 
B 1 65  ASN 65  65  65  ASN ASN B . n 
B 1 66  PRO 66  66  66  PRO PRO B . n 
B 1 67  HIS 67  67  67  HIS HIS B . n 
B 1 68  SER 68  68  68  SER SER B . n 
B 1 69  LYS 69  69  69  LYS LYS B . n 
B 1 70  LYS 70  70  70  LYS LYS B . n 
B 1 71  HIS 71  71  71  HIS HIS B . n 
B 1 72  GLY 72  72  72  GLY GLY B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  ALA 75  75  75  ALA ALA B . n 
B 1 76  ASP 76  76  76  ASP ASP B . n 
B 1 77  GLU 77  77  77  GLU GLU B . n 
B 1 78  GLU 78  78  78  GLU GLU B . n 
B 1 79  ARG 79  79  79  ARG ARG B . n 
B 1 80  HIS 80  80  80  HIS HIS B . n 
B 1 81  VAL 81  81  81  VAL VAL B . n 
B 1 82  GLY 82  82  82  GLY GLY B . n 
B 1 83  ASP 83  83  83  ASP ASP B . n 
B 1 84  LEU 84  84  84  LEU LEU B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  ASN 86  86  86  ASN ASN B . n 
B 1 87  VAL 87  87  87  VAL VAL B . n 
B 1 88  THR 88  88  88  THR THR B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  ASP 90  90  90  ASP ASP B . n 
B 1 91  LYS 91  91  91  LYS LYS B . n 
B 1 92  ASP 92  92  92  ASP ASP B . n 
B 1 93  GLY 93  93  93  GLY GLY B . n 
B 1 94  VAL 94  94  94  VAL VAL B . n 
B 1 95  ALA 95  95  95  ALA ALA B . n 
B 1 96  ASP 96  96  96  ASP ASP B . n 
B 1 97  VAL 97  97  97  VAL VAL B . n 
B 1 98  SER 98  98  98  SER SER B . n 
B 1 99  ILE 99  99  99  ILE ILE B . n 
B 1 100 GLU 100 100 100 GLU GLU B . n 
B 1 101 ASP 101 101 101 ASP ASP B . n 
B 1 102 SER 102 102 102 SER SER B . n 
B 1 103 VAL 103 103 103 VAL VAL B . n 
B 1 104 ILE 104 104 104 ILE ILE B . n 
B 1 105 SER 105 105 105 SER SER B . n 
B 1 106 LEU 106 106 106 LEU LEU B . n 
B 1 107 SER 107 107 107 SER SER B . n 
B 1 108 GLY 108 108 108 GLY GLY B . n 
B 1 109 ASP 109 109 109 ASP ASP B . n 
B 1 110 HIS 110 110 110 HIS HIS B . n 
B 1 111 CYS 111 111 111 CYS CYS B . n 
B 1 112 ILE 112 112 112 ILE ILE B . n 
B 1 113 ILE 113 113 113 ILE ILE B . n 
B 1 114 GLY 114 114 114 GLY GLY B . n 
B 1 115 ARG 115 115 115 ARG ARG B . n 
B 1 116 THR 116 116 116 THR THR B . n 
B 1 117 LEU 117 117 117 LEU LEU B . n 
B 1 118 VAL 118 118 118 VAL VAL B . n 
B 1 119 VAL 119 119 119 VAL VAL B . n 
B 1 120 HIS 120 120 120 HIS HIS B . n 
B 1 121 GLU 121 121 121 GLU GLU B . n 
B 1 122 LYS 122 122 122 LYS LYS B . n 
B 1 123 ALA 123 123 123 ALA ALA B . n 
B 1 124 ASP 124 124 124 ASP ASP B . n 
B 1 125 ASP 125 125 125 ASP ASP B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 GLY 127 127 127 GLY GLY B . n 
B 1 128 LYS 128 128 128 LYS LYS B . n 
B 1 129 GLY 129 129 129 GLY GLY B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 ASN 131 131 131 ASN ASN B . n 
B 1 132 GLU 132 132 132 GLU GLU B . n 
B 1 133 GLU 133 133 133 GLU GLU B . n 
B 1 134 SER 134 134 134 SER SER B . n 
B 1 135 THR 135 135 135 THR THR B . n 
B 1 136 LYS 136 136 136 LYS LYS B . n 
B 1 137 THR 137 137 137 THR THR B . n 
B 1 138 GLY 138 138 138 GLY GLY B . n 
B 1 139 ASN 139 139 139 ASN ASN B . n 
B 1 140 ALA 140 140 140 ALA ALA B . n 
B 1 141 GLY 141 141 141 GLY GLY B . n 
B 1 142 SER 142 142 142 SER SER B . n 
B 1 143 ARG 143 143 143 ARG ARG B . n 
B 1 144 LEU 144 144 144 LEU LEU B . n 
B 1 145 ALA 145 145 145 ALA ALA B . n 
B 1 146 CYS 146 146 146 CYS CYS B . n 
B 1 147 GLY 147 147 147 GLY GLY B . n 
B 1 148 VAL 148 148 148 VAL VAL B . n 
B 1 149 ILE 149 149 149 ILE ILE B . n 
B 1 150 GLY 150 150 150 GLY GLY B . n 
B 1 151 ILE 151 151 151 ILE ILE B . n 
B 1 152 ALA 152 152 152 ALA ALA B . n 
B 1 153 GLN 153 153 153 GLN GLN B . n 
C 1 1   ALA 1   1   1   ALA ALA C . n 
C 1 2   MET 2   2   2   MET MET C . n 
C 1 3   LYS 3   3   3   LYS LYS C . n 
C 1 4   ALA 4   4   4   ALA ALA C . n 
C 1 5   VAL 5   5   5   VAL VAL C . n 
C 1 6   CYS 6   6   6   CYS CYS C . n 
C 1 7   VAL 7   7   7   VAL VAL C . n 
C 1 8   LEU 8   8   8   LEU LEU C . n 
C 1 9   LYS 9   9   9   LYS LYS C . n 
C 1 10  GLY 10  10  10  GLY GLY C . n 
C 1 11  ASP 11  11  11  ASP ASP C . n 
C 1 12  GLY 12  12  12  GLY GLY C . n 
C 1 13  PRO 13  13  13  PRO PRO C . n 
C 1 14  VAL 14  14  14  VAL VAL C . n 
C 1 15  GLN 15  15  15  GLN GLN C . n 
C 1 16  GLY 16  16  16  GLY GLY C . n 
C 1 17  THR 17  17  17  THR THR C . n 
C 1 18  ILE 18  18  18  ILE ILE C . n 
C 1 19  HIS 19  19  19  HIS HIS C . n 
C 1 20  PHE 20  20  20  PHE PHE C . n 
C 1 21  GLU 21  21  21  GLU GLU C . n 
C 1 22  GLN 22  22  22  GLN GLN C . n 
C 1 23  LYS 23  23  23  LYS LYS C . n 
C 1 24  ALA 24  24  24  ALA ALA C . n 
C 1 25  SER 25  25  25  SER SER C . n 
C 1 26  GLY 26  26  26  GLY GLY C . n 
C 1 27  GLU 27  27  27  GLU GLU C . n 
C 1 28  PRO 28  28  28  PRO PRO C . n 
C 1 29  VAL 29  29  29  VAL VAL C . n 
C 1 30  VAL 30  30  30  VAL VAL C . n 
C 1 31  LEU 31  31  31  LEU LEU C . n 
C 1 32  SER 32  32  32  SER SER C . n 
C 1 33  GLY 33  33  33  GLY GLY C . n 
C 1 34  GLN 34  34  34  GLN GLN C . n 
C 1 35  ILE 35  35  35  ILE ILE C . n 
C 1 36  THR 36  36  36  THR THR C . n 
C 1 37  GLY 37  37  37  GLY GLY C . n 
C 1 38  LEU 38  38  38  LEU LEU C . n 
C 1 39  THR 39  39  39  THR THR C . n 
C 1 40  GLU 40  40  40  GLU GLU C . n 
C 1 41  GLY 41  41  41  GLY GLY C . n 
C 1 42  GLN 42  42  42  GLN GLN C . n 
C 1 43  HIS 43  43  43  HIS HIS C . n 
C 1 44  GLY 44  44  44  GLY GLY C . n 
C 1 45  PHE 45  45  45  PHE PHE C . n 
C 1 46  HIS 46  46  46  HIS HIS C . n 
C 1 47  VAL 47  47  47  VAL VAL C . n 
C 1 48  HIS 48  48  48  HIS HIS C . n 
C 1 49  GLN 49  49  49  GLN GLN C . n 
C 1 50  TYR 50  50  50  TYR TYR C . n 
C 1 51  GLY 51  51  51  GLY GLY C . n 
C 1 52  ASP 52  52  52  ASP ASP C . n 
C 1 53  ASN 53  53  53  ASN ASN C . n 
C 1 54  THR 54  54  54  THR THR C . n 
C 1 55  GLN 55  55  55  GLN GLN C . n 
C 1 56  GLY 56  56  56  GLY GLY C . n 
C 1 57  CYS 57  57  57  CYS CYS C . n 
C 1 58  THR 58  58  58  THR THR C . n 
C 1 59  SER 59  59  59  SER SER C . n 
C 1 60  ALA 60  60  60  ALA ALA C . n 
C 1 61  GLY 61  61  61  GLY GLY C . n 
C 1 62  PRO 62  62  62  PRO PRO C . n 
C 1 63  HIS 63  63  63  HIS HIS C . n 
C 1 64  PHE 64  64  64  PHE PHE C . n 
C 1 65  ASN 65  65  65  ASN ASN C . n 
C 1 66  PRO 66  66  66  PRO PRO C . n 
C 1 67  HIS 67  67  67  HIS HIS C . n 
C 1 68  SER 68  68  68  SER SER C . n 
C 1 69  LYS 69  69  69  LYS LYS C . n 
C 1 70  LYS 70  70  70  LYS LYS C . n 
C 1 71  HIS 71  71  71  HIS HIS C . n 
C 1 72  GLY 72  72  72  GLY GLY C . n 
C 1 73  GLY 73  73  73  GLY GLY C . n 
C 1 74  PRO 74  74  74  PRO PRO C . n 
C 1 75  ALA 75  75  75  ALA ALA C . n 
C 1 76  ASP 76  76  76  ASP ASP C . n 
C 1 77  GLU 77  77  77  GLU GLU C . n 
C 1 78  GLU 78  78  78  GLU GLU C . n 
C 1 79  ARG 79  79  79  ARG ARG C . n 
C 1 80  HIS 80  80  80  HIS HIS C . n 
C 1 81  VAL 81  81  81  VAL VAL C . n 
C 1 82  GLY 82  82  82  GLY GLY C . n 
C 1 83  ASP 83  83  83  ASP ASP C . n 
C 1 84  LEU 84  84  84  LEU LEU C . n 
C 1 85  GLY 85  85  85  GLY GLY C . n 
C 1 86  ASN 86  86  86  ASN ASN C . n 
C 1 87  VAL 87  87  87  VAL VAL C . n 
C 1 88  THR 88  88  88  THR THR C . n 
C 1 89  ALA 89  89  89  ALA ALA C . n 
C 1 90  ASP 90  90  90  ASP ASP C . n 
C 1 91  LYS 91  91  91  LYS LYS C . n 
C 1 92  ASP 92  92  92  ASP ASP C . n 
C 1 93  GLY 93  93  93  GLY GLY C . n 
C 1 94  VAL 94  94  94  VAL VAL C . n 
C 1 95  ALA 95  95  95  ALA ALA C . n 
C 1 96  ASP 96  96  96  ASP ASP C . n 
C 1 97  VAL 97  97  97  VAL VAL C . n 
C 1 98  SER 98  98  98  SER SER C . n 
C 1 99  ILE 99  99  99  ILE ILE C . n 
C 1 100 GLU 100 100 100 GLU GLU C . n 
C 1 101 ASP 101 101 101 ASP ASP C . n 
C 1 102 SER 102 102 102 SER SER C . n 
C 1 103 VAL 103 103 103 VAL VAL C . n 
C 1 104 ILE 104 104 104 ILE ILE C . n 
C 1 105 SER 105 105 105 SER SER C . n 
C 1 106 LEU 106 106 106 LEU LEU C . n 
C 1 107 SER 107 107 107 SER SER C . n 
C 1 108 GLY 108 108 108 GLY GLY C . n 
C 1 109 ASP 109 109 109 ASP ASP C . n 
C 1 110 HIS 110 110 110 HIS HIS C . n 
C 1 111 CYS 111 111 111 CYS CYS C . n 
C 1 112 ILE 112 112 112 ILE ILE C . n 
C 1 113 ILE 113 113 113 ILE ILE C . n 
C 1 114 GLY 114 114 114 GLY GLY C . n 
C 1 115 ARG 115 115 115 ARG ARG C . n 
C 1 116 THR 116 116 116 THR THR C . n 
C 1 117 LEU 117 117 117 LEU LEU C . n 
C 1 118 VAL 118 118 118 VAL VAL C . n 
C 1 119 VAL 119 119 119 VAL VAL C . n 
C 1 120 HIS 120 120 120 HIS HIS C . n 
C 1 121 GLU 121 121 121 GLU GLU C . n 
C 1 122 LYS 122 122 122 LYS LYS C . n 
C 1 123 ALA 123 123 123 ALA ALA C . n 
C 1 124 ASP 124 124 124 ASP ASP C . n 
C 1 125 ASP 125 125 125 ASP ASP C . n 
C 1 126 LEU 126 126 126 LEU LEU C . n 
C 1 127 GLY 127 127 127 GLY GLY C . n 
C 1 128 LYS 128 128 ?   ?   ?   C . n 
C 1 129 GLY 129 129 ?   ?   ?   C . n 
C 1 130 GLY 130 130 ?   ?   ?   C . n 
C 1 131 ASN 131 131 131 ASN ASN C . n 
C 1 132 GLU 132 132 132 GLU GLU C . n 
C 1 133 GLU 133 133 133 GLU GLU C . n 
C 1 134 SER 134 134 134 SER SER C . n 
C 1 135 THR 135 135 135 THR THR C . n 
C 1 136 LYS 136 136 136 LYS LYS C . n 
C 1 137 THR 137 137 137 THR THR C . n 
C 1 138 GLY 138 138 138 GLY GLY C . n 
C 1 139 ASN 139 139 139 ASN ASN C . n 
C 1 140 ALA 140 140 140 ALA ALA C . n 
C 1 141 GLY 141 141 141 GLY GLY C . n 
C 1 142 SER 142 142 142 SER SER C . n 
C 1 143 ARG 143 143 143 ARG ARG C . n 
C 1 144 LEU 144 144 144 LEU LEU C . n 
C 1 145 ALA 145 145 145 ALA ALA C . n 
C 1 146 CYS 146 146 146 CYS CYS C . n 
C 1 147 GLY 147 147 147 GLY GLY C . n 
C 1 148 VAL 148 148 148 VAL VAL C . n 
C 1 149 ILE 149 149 149 ILE ILE C . n 
C 1 150 GLY 150 150 150 GLY GLY C . n 
C 1 151 ILE 151 151 151 ILE ILE C . n 
C 1 152 ALA 152 152 152 ALA ALA C . n 
C 1 153 GLN 153 153 153 GLN GLN C . n 
D 1 1   ALA 1   1   1   ALA ALA D . n 
D 1 2   MET 2   2   2   MET MET D . n 
D 1 3   LYS 3   3   3   LYS LYS D . n 
D 1 4   ALA 4   4   4   ALA ALA D . n 
D 1 5   VAL 5   5   5   VAL VAL D . n 
D 1 6   CYS 6   6   6   CYS CYS D . n 
D 1 7   VAL 7   7   7   VAL VAL D . n 
D 1 8   LEU 8   8   8   LEU LEU D . n 
D 1 9   LYS 9   9   9   LYS LYS D . n 
D 1 10  GLY 10  10  10  GLY GLY D . n 
D 1 11  ASP 11  11  11  ASP ASP D . n 
D 1 12  GLY 12  12  12  GLY GLY D . n 
D 1 13  PRO 13  13  13  PRO PRO D . n 
D 1 14  VAL 14  14  14  VAL VAL D . n 
D 1 15  GLN 15  15  15  GLN GLN D . n 
D 1 16  GLY 16  16  16  GLY GLY D . n 
D 1 17  THR 17  17  17  THR THR D . n 
D 1 18  ILE 18  18  18  ILE ILE D . n 
D 1 19  HIS 19  19  19  HIS HIS D . n 
D 1 20  PHE 20  20  20  PHE PHE D . n 
D 1 21  GLU 21  21  21  GLU GLU D . n 
D 1 22  GLN 22  22  22  GLN GLN D . n 
D 1 23  LYS 23  23  23  LYS LYS D . n 
D 1 24  ALA 24  24  24  ALA ALA D . n 
D 1 25  SER 25  25  25  SER SER D . n 
D 1 26  GLY 26  26  26  GLY GLY D . n 
D 1 27  GLU 27  27  27  GLU GLU D . n 
D 1 28  PRO 28  28  28  PRO PRO D . n 
D 1 29  VAL 29  29  29  VAL VAL D . n 
D 1 30  VAL 30  30  30  VAL VAL D . n 
D 1 31  LEU 31  31  31  LEU LEU D . n 
D 1 32  SER 32  32  32  SER SER D . n 
D 1 33  GLY 33  33  33  GLY GLY D . n 
D 1 34  GLN 34  34  34  GLN GLN D . n 
D 1 35  ILE 35  35  35  ILE ILE D . n 
D 1 36  THR 36  36  36  THR THR D . n 
D 1 37  GLY 37  37  37  GLY GLY D . n 
D 1 38  LEU 38  38  38  LEU LEU D . n 
D 1 39  THR 39  39  39  THR THR D . n 
D 1 40  GLU 40  40  40  GLU GLU D . n 
D 1 41  GLY 41  41  41  GLY GLY D . n 
D 1 42  GLN 42  42  42  GLN GLN D . n 
D 1 43  HIS 43  43  43  HIS HIS D . n 
D 1 44  GLY 44  44  44  GLY GLY D . n 
D 1 45  PHE 45  45  45  PHE PHE D . n 
D 1 46  HIS 46  46  46  HIS HIS D . n 
D 1 47  VAL 47  47  47  VAL VAL D . n 
D 1 48  HIS 48  48  48  HIS HIS D . n 
D 1 49  GLN 49  49  49  GLN GLN D . n 
D 1 50  TYR 50  50  50  TYR TYR D . n 
D 1 51  GLY 51  51  51  GLY GLY D . n 
D 1 52  ASP 52  52  52  ASP ASP D . n 
D 1 53  ASN 53  53  53  ASN ASN D . n 
D 1 54  THR 54  54  54  THR THR D . n 
D 1 55  GLN 55  55  55  GLN GLN D . n 
D 1 56  GLY 56  56  56  GLY GLY D . n 
D 1 57  CYS 57  57  57  CYS CYS D . n 
D 1 58  THR 58  58  58  THR THR D . n 
D 1 59  SER 59  59  59  SER SER D . n 
D 1 60  ALA 60  60  60  ALA ALA D . n 
D 1 61  GLY 61  61  61  GLY GLY D . n 
D 1 62  PRO 62  62  62  PRO PRO D . n 
D 1 63  HIS 63  63  63  HIS HIS D . n 
D 1 64  PHE 64  64  64  PHE PHE D . n 
D 1 65  ASN 65  65  65  ASN ASN D . n 
D 1 66  PRO 66  66  66  PRO PRO D . n 
D 1 67  HIS 67  67  67  HIS HIS D . n 
D 1 68  SER 68  68  68  SER SER D . n 
D 1 69  LYS 69  69  69  LYS LYS D . n 
D 1 70  LYS 70  70  70  LYS LYS D . n 
D 1 71  HIS 71  71  71  HIS HIS D . n 
D 1 72  GLY 72  72  72  GLY GLY D . n 
D 1 73  GLY 73  73  73  GLY GLY D . n 
D 1 74  PRO 74  74  74  PRO PRO D . n 
D 1 75  ALA 75  75  75  ALA ALA D . n 
D 1 76  ASP 76  76  76  ASP ASP D . n 
D 1 77  GLU 77  77  77  GLU GLU D . n 
D 1 78  GLU 78  78  78  GLU GLU D . n 
D 1 79  ARG 79  79  79  ARG ARG D . n 
D 1 80  HIS 80  80  80  HIS HIS D . n 
D 1 81  VAL 81  81  81  VAL VAL D . n 
D 1 82  GLY 82  82  82  GLY GLY D . n 
D 1 83  ASP 83  83  83  ASP ASP D . n 
D 1 84  LEU 84  84  84  LEU LEU D . n 
D 1 85  GLY 85  85  85  GLY GLY D . n 
D 1 86  ASN 86  86  86  ASN ASN D . n 
D 1 87  VAL 87  87  87  VAL VAL D . n 
D 1 88  THR 88  88  88  THR THR D . n 
D 1 89  ALA 89  89  89  ALA ALA D . n 
D 1 90  ASP 90  90  90  ASP ASP D . n 
D 1 91  LYS 91  91  91  LYS LYS D . n 
D 1 92  ASP 92  92  92  ASP ASP D . n 
D 1 93  GLY 93  93  93  GLY GLY D . n 
D 1 94  VAL 94  94  94  VAL VAL D . n 
D 1 95  ALA 95  95  95  ALA ALA D . n 
D 1 96  ASP 96  96  96  ASP ASP D . n 
D 1 97  VAL 97  97  97  VAL VAL D . n 
D 1 98  SER 98  98  98  SER SER D . n 
D 1 99  ILE 99  99  99  ILE ILE D . n 
D 1 100 GLU 100 100 100 GLU GLU D . n 
D 1 101 ASP 101 101 101 ASP ASP D . n 
D 1 102 SER 102 102 102 SER SER D . n 
D 1 103 VAL 103 103 103 VAL VAL D . n 
D 1 104 ILE 104 104 104 ILE ILE D . n 
D 1 105 SER 105 105 105 SER SER D . n 
D 1 106 LEU 106 106 106 LEU LEU D . n 
D 1 107 SER 107 107 107 SER SER D . n 
D 1 108 GLY 108 108 108 GLY GLY D . n 
D 1 109 ASP 109 109 109 ASP ASP D . n 
D 1 110 HIS 110 110 110 HIS HIS D . n 
D 1 111 CYS 111 111 111 CYS CYS D . n 
D 1 112 ILE 112 112 112 ILE ILE D . n 
D 1 113 ILE 113 113 113 ILE ILE D . n 
D 1 114 GLY 114 114 114 GLY GLY D . n 
D 1 115 ARG 115 115 115 ARG ARG D . n 
D 1 116 THR 116 116 116 THR THR D . n 
D 1 117 LEU 117 117 117 LEU LEU D . n 
D 1 118 VAL 118 118 118 VAL VAL D . n 
D 1 119 VAL 119 119 119 VAL VAL D . n 
D 1 120 HIS 120 120 120 HIS HIS D . n 
D 1 121 GLU 121 121 121 GLU GLU D . n 
D 1 122 LYS 122 122 122 LYS LYS D . n 
D 1 123 ALA 123 123 123 ALA ALA D . n 
D 1 124 ASP 124 124 124 ASP ASP D . n 
D 1 125 ASP 125 125 125 ASP ASP D . n 
D 1 126 LEU 126 126 126 LEU LEU D . n 
D 1 127 GLY 127 127 127 GLY GLY D . n 
D 1 128 LYS 128 128 128 LYS LYS D . n 
D 1 129 GLY 129 129 129 GLY GLY D . n 
D 1 130 GLY 130 130 130 GLY GLY D . n 
D 1 131 ASN 131 131 131 ASN ASN D . n 
D 1 132 GLU 132 132 132 GLU GLU D . n 
D 1 133 GLU 133 133 133 GLU GLU D . n 
D 1 134 SER 134 134 134 SER SER D . n 
D 1 135 THR 135 135 135 THR THR D . n 
D 1 136 LYS 136 136 136 LYS LYS D . n 
D 1 137 THR 137 137 137 THR THR D . n 
D 1 138 GLY 138 138 138 GLY GLY D . n 
D 1 139 ASN 139 139 139 ASN ASN D . n 
D 1 140 ALA 140 140 140 ALA ALA D . n 
D 1 141 GLY 141 141 141 GLY GLY D . n 
D 1 142 SER 142 142 142 SER SER D . n 
D 1 143 ARG 143 143 143 ARG ARG D . n 
D 1 144 LEU 144 144 144 LEU LEU D . n 
D 1 145 ALA 145 145 145 ALA ALA D . n 
D 1 146 CYS 146 146 146 CYS CYS D . n 
D 1 147 GLY 147 147 147 GLY GLY D . n 
D 1 148 VAL 148 148 148 VAL VAL D . n 
D 1 149 ILE 149 149 149 ILE ILE D . n 
D 1 150 GLY 150 150 150 GLY GLY D . n 
D 1 151 ILE 151 151 151 ILE ILE D . n 
D 1 152 ALA 152 152 152 ALA ALA D . n 
D 1 153 GLN 153 153 ?   ?   ?   D . n 
E 1 1   ALA 1   1   1   ALA ALA E . n 
E 1 2   MET 2   2   2   MET MET E . n 
E 1 3   LYS 3   3   3   LYS LYS E . n 
E 1 4   ALA 4   4   4   ALA ALA E . n 
E 1 5   VAL 5   5   5   VAL VAL E . n 
E 1 6   CYS 6   6   6   CYS CYS E . n 
E 1 7   VAL 7   7   7   VAL VAL E . n 
E 1 8   LEU 8   8   8   LEU LEU E . n 
E 1 9   LYS 9   9   9   LYS LYS E . n 
E 1 10  GLY 10  10  10  GLY GLY E . n 
E 1 11  ASP 11  11  11  ASP ASP E . n 
E 1 12  GLY 12  12  12  GLY GLY E . n 
E 1 13  PRO 13  13  13  PRO PRO E . n 
E 1 14  VAL 14  14  14  VAL VAL E . n 
E 1 15  GLN 15  15  15  GLN GLN E . n 
E 1 16  GLY 16  16  16  GLY GLY E . n 
E 1 17  THR 17  17  17  THR THR E . n 
E 1 18  ILE 18  18  18  ILE ILE E . n 
E 1 19  HIS 19  19  19  HIS HIS E . n 
E 1 20  PHE 20  20  20  PHE PHE E . n 
E 1 21  GLU 21  21  21  GLU GLU E . n 
E 1 22  GLN 22  22  22  GLN GLN E . n 
E 1 23  LYS 23  23  23  LYS LYS E . n 
E 1 24  ALA 24  24  24  ALA ALA E . n 
E 1 25  SER 25  25  25  SER SER E . n 
E 1 26  GLY 26  26  26  GLY GLY E . n 
E 1 27  GLU 27  27  27  GLU GLU E . n 
E 1 28  PRO 28  28  28  PRO PRO E . n 
E 1 29  VAL 29  29  29  VAL VAL E . n 
E 1 30  VAL 30  30  30  VAL VAL E . n 
E 1 31  LEU 31  31  31  LEU LEU E . n 
E 1 32  SER 32  32  32  SER SER E . n 
E 1 33  GLY 33  33  33  GLY GLY E . n 
E 1 34  GLN 34  34  34  GLN GLN E . n 
E 1 35  ILE 35  35  35  ILE ILE E . n 
E 1 36  THR 36  36  36  THR THR E . n 
E 1 37  GLY 37  37  37  GLY GLY E . n 
E 1 38  LEU 38  38  38  LEU LEU E . n 
E 1 39  THR 39  39  39  THR THR E . n 
E 1 40  GLU 40  40  40  GLU GLU E . n 
E 1 41  GLY 41  41  41  GLY GLY E . n 
E 1 42  GLN 42  42  42  GLN GLN E . n 
E 1 43  HIS 43  43  43  HIS HIS E . n 
E 1 44  GLY 44  44  44  GLY GLY E . n 
E 1 45  PHE 45  45  45  PHE PHE E . n 
E 1 46  HIS 46  46  46  HIS HIS E . n 
E 1 47  VAL 47  47  47  VAL VAL E . n 
E 1 48  HIS 48  48  48  HIS HIS E . n 
E 1 49  GLN 49  49  49  GLN GLN E . n 
E 1 50  TYR 50  50  50  TYR TYR E . n 
E 1 51  GLY 51  51  51  GLY GLY E . n 
E 1 52  ASP 52  52  52  ASP ASP E . n 
E 1 53  ASN 53  53  53  ASN ASN E . n 
E 1 54  THR 54  54  54  THR THR E . n 
E 1 55  GLN 55  55  55  GLN GLN E . n 
E 1 56  GLY 56  56  56  GLY GLY E . n 
E 1 57  CYS 57  57  57  CYS CYS E . n 
E 1 58  THR 58  58  58  THR THR E . n 
E 1 59  SER 59  59  59  SER SER E . n 
E 1 60  ALA 60  60  60  ALA ALA E . n 
E 1 61  GLY 61  61  61  GLY GLY E . n 
E 1 62  PRO 62  62  62  PRO PRO E . n 
E 1 63  HIS 63  63  63  HIS HIS E . n 
E 1 64  PHE 64  64  64  PHE PHE E . n 
E 1 65  ASN 65  65  65  ASN ASN E . n 
E 1 66  PRO 66  66  66  PRO PRO E . n 
E 1 67  HIS 67  67  67  HIS HIS E . n 
E 1 68  SER 68  68  68  SER SER E . n 
E 1 69  LYS 69  69  69  LYS LYS E . n 
E 1 70  LYS 70  70  70  LYS LYS E . n 
E 1 71  HIS 71  71  71  HIS HIS E . n 
E 1 72  GLY 72  72  72  GLY GLY E . n 
E 1 73  GLY 73  73  73  GLY GLY E . n 
E 1 74  PRO 74  74  74  PRO PRO E . n 
E 1 75  ALA 75  75  75  ALA ALA E . n 
E 1 76  ASP 76  76  76  ASP ASP E . n 
E 1 77  GLU 77  77  77  GLU GLU E . n 
E 1 78  GLU 78  78  78  GLU GLU E . n 
E 1 79  ARG 79  79  79  ARG ARG E . n 
E 1 80  HIS 80  80  80  HIS HIS E . n 
E 1 81  VAL 81  81  81  VAL VAL E . n 
E 1 82  GLY 82  82  82  GLY GLY E . n 
E 1 83  ASP 83  83  83  ASP ASP E . n 
E 1 84  LEU 84  84  84  LEU LEU E . n 
E 1 85  GLY 85  85  85  GLY GLY E . n 
E 1 86  ASN 86  86  86  ASN ASN E . n 
E 1 87  VAL 87  87  87  VAL VAL E . n 
E 1 88  THR 88  88  88  THR THR E . n 
E 1 89  ALA 89  89  89  ALA ALA E . n 
E 1 90  ASP 90  90  90  ASP ASP E . n 
E 1 91  LYS 91  91  91  LYS LYS E . n 
E 1 92  ASP 92  92  92  ASP ASP E . n 
E 1 93  GLY 93  93  93  GLY GLY E . n 
E 1 94  VAL 94  94  94  VAL VAL E . n 
E 1 95  ALA 95  95  95  ALA ALA E . n 
E 1 96  ASP 96  96  96  ASP ASP E . n 
E 1 97  VAL 97  97  97  VAL VAL E . n 
E 1 98  SER 98  98  98  SER SER E . n 
E 1 99  ILE 99  99  99  ILE ILE E . n 
E 1 100 GLU 100 100 100 GLU GLU E . n 
E 1 101 ASP 101 101 101 ASP ASP E . n 
E 1 102 SER 102 102 102 SER SER E . n 
E 1 103 VAL 103 103 103 VAL VAL E . n 
E 1 104 ILE 104 104 104 ILE ILE E . n 
E 1 105 SER 105 105 105 SER SER E . n 
E 1 106 LEU 106 106 106 LEU LEU E . n 
E 1 107 SER 107 107 107 SER SER E . n 
E 1 108 GLY 108 108 108 GLY GLY E . n 
E 1 109 ASP 109 109 109 ASP ASP E . n 
E 1 110 HIS 110 110 110 HIS HIS E . n 
E 1 111 CYS 111 111 111 CYS CYS E . n 
E 1 112 ILE 112 112 112 ILE ILE E . n 
E 1 113 ILE 113 113 113 ILE ILE E . n 
E 1 114 GLY 114 114 114 GLY GLY E . n 
E 1 115 ARG 115 115 115 ARG ARG E . n 
E 1 116 THR 116 116 116 THR THR E . n 
E 1 117 LEU 117 117 117 LEU LEU E . n 
E 1 118 VAL 118 118 118 VAL VAL E . n 
E 1 119 VAL 119 119 119 VAL VAL E . n 
E 1 120 HIS 120 120 120 HIS HIS E . n 
E 1 121 GLU 121 121 121 GLU GLU E . n 
E 1 122 LYS 122 122 122 LYS LYS E . n 
E 1 123 ALA 123 123 123 ALA ALA E . n 
E 1 124 ASP 124 124 124 ASP ASP E . n 
E 1 125 ASP 125 125 125 ASP ASP E . n 
E 1 126 LEU 126 126 126 LEU LEU E . n 
E 1 127 GLY 127 127 127 GLY GLY E . n 
E 1 128 LYS 128 128 128 LYS LYS E . n 
E 1 129 GLY 129 129 129 GLY GLY E . n 
E 1 130 GLY 130 130 130 GLY GLY E . n 
E 1 131 ASN 131 131 131 ASN ASN E . n 
E 1 132 GLU 132 132 132 GLU GLU E . n 
E 1 133 GLU 133 133 133 GLU GLU E . n 
E 1 134 SER 134 134 134 SER SER E . n 
E 1 135 THR 135 135 135 THR THR E . n 
E 1 136 LYS 136 136 136 LYS LYS E . n 
E 1 137 THR 137 137 137 THR THR E . n 
E 1 138 GLY 138 138 138 GLY GLY E . n 
E 1 139 ASN 139 139 139 ASN ASN E . n 
E 1 140 ALA 140 140 140 ALA ALA E . n 
E 1 141 GLY 141 141 141 GLY GLY E . n 
E 1 142 SER 142 142 142 SER SER E . n 
E 1 143 ARG 143 143 143 ARG ARG E . n 
E 1 144 LEU 144 144 144 LEU LEU E . n 
E 1 145 ALA 145 145 145 ALA ALA E . n 
E 1 146 CYS 146 146 146 CYS CYS E . n 
E 1 147 GLY 147 147 147 GLY GLY E . n 
E 1 148 VAL 148 148 148 VAL VAL E . n 
E 1 149 ILE 149 149 149 ILE ILE E . n 
E 1 150 GLY 150 150 150 GLY GLY E . n 
E 1 151 ILE 151 151 151 ILE ILE E . n 
E 1 152 ALA 152 152 152 ALA ALA E . n 
E 1 153 GLN 153 153 153 GLN GLN E . n 
F 1 1   ALA 1   1   1   ALA ALA F . n 
F 1 2   MET 2   2   2   MET MET F . n 
F 1 3   LYS 3   3   3   LYS LYS F . n 
F 1 4   ALA 4   4   4   ALA ALA F . n 
F 1 5   VAL 5   5   5   VAL VAL F . n 
F 1 6   CYS 6   6   6   CYS CYS F . n 
F 1 7   VAL 7   7   7   VAL VAL F . n 
F 1 8   LEU 8   8   8   LEU LEU F . n 
F 1 9   LYS 9   9   9   LYS LYS F . n 
F 1 10  GLY 10  10  10  GLY GLY F . n 
F 1 11  ASP 11  11  11  ASP ASP F . n 
F 1 12  GLY 12  12  12  GLY GLY F . n 
F 1 13  PRO 13  13  13  PRO PRO F . n 
F 1 14  VAL 14  14  14  VAL VAL F . n 
F 1 15  GLN 15  15  15  GLN GLN F . n 
F 1 16  GLY 16  16  16  GLY GLY F . n 
F 1 17  THR 17  17  17  THR THR F . n 
F 1 18  ILE 18  18  18  ILE ILE F . n 
F 1 19  HIS 19  19  19  HIS HIS F . n 
F 1 20  PHE 20  20  20  PHE PHE F . n 
F 1 21  GLU 21  21  21  GLU GLU F . n 
F 1 22  GLN 22  22  22  GLN GLN F . n 
F 1 23  LYS 23  23  23  LYS LYS F . n 
F 1 24  ALA 24  24  24  ALA ALA F . n 
F 1 25  SER 25  25  25  SER SER F . n 
F 1 26  GLY 26  26  26  GLY GLY F . n 
F 1 27  GLU 27  27  27  GLU GLU F . n 
F 1 28  PRO 28  28  28  PRO PRO F . n 
F 1 29  VAL 29  29  29  VAL VAL F . n 
F 1 30  VAL 30  30  30  VAL VAL F . n 
F 1 31  LEU 31  31  31  LEU LEU F . n 
F 1 32  SER 32  32  32  SER SER F . n 
F 1 33  GLY 33  33  33  GLY GLY F . n 
F 1 34  GLN 34  34  34  GLN GLN F . n 
F 1 35  ILE 35  35  35  ILE ILE F . n 
F 1 36  THR 36  36  36  THR THR F . n 
F 1 37  GLY 37  37  37  GLY GLY F . n 
F 1 38  LEU 38  38  38  LEU LEU F . n 
F 1 39  THR 39  39  39  THR THR F . n 
F 1 40  GLU 40  40  40  GLU GLU F . n 
F 1 41  GLY 41  41  41  GLY GLY F . n 
F 1 42  GLN 42  42  42  GLN GLN F . n 
F 1 43  HIS 43  43  43  HIS HIS F . n 
F 1 44  GLY 44  44  44  GLY GLY F . n 
F 1 45  PHE 45  45  45  PHE PHE F . n 
F 1 46  HIS 46  46  46  HIS HIS F . n 
F 1 47  VAL 47  47  47  VAL VAL F . n 
F 1 48  HIS 48  48  48  HIS HIS F . n 
F 1 49  GLN 49  49  49  GLN GLN F . n 
F 1 50  TYR 50  50  50  TYR TYR F . n 
F 1 51  GLY 51  51  51  GLY GLY F . n 
F 1 52  ASP 52  52  52  ASP ASP F . n 
F 1 53  ASN 53  53  53  ASN ASN F . n 
F 1 54  THR 54  54  54  THR THR F . n 
F 1 55  GLN 55  55  55  GLN GLN F . n 
F 1 56  GLY 56  56  56  GLY GLY F . n 
F 1 57  CYS 57  57  57  CYS CYS F . n 
F 1 58  THR 58  58  58  THR THR F . n 
F 1 59  SER 59  59  59  SER SER F . n 
F 1 60  ALA 60  60  60  ALA ALA F . n 
F 1 61  GLY 61  61  61  GLY GLY F . n 
F 1 62  PRO 62  62  62  PRO PRO F . n 
F 1 63  HIS 63  63  63  HIS HIS F . n 
F 1 64  PHE 64  64  64  PHE PHE F . n 
F 1 65  ASN 65  65  65  ASN ASN F . n 
F 1 66  PRO 66  66  66  PRO PRO F . n 
F 1 67  HIS 67  67  67  HIS HIS F . n 
F 1 68  SER 68  68  68  SER SER F . n 
F 1 69  LYS 69  69  69  LYS LYS F . n 
F 1 70  LYS 70  70  70  LYS LYS F . n 
F 1 71  HIS 71  71  71  HIS HIS F . n 
F 1 72  GLY 72  72  72  GLY GLY F . n 
F 1 73  GLY 73  73  73  GLY GLY F . n 
F 1 74  PRO 74  74  74  PRO PRO F . n 
F 1 75  ALA 75  75  75  ALA ALA F . n 
F 1 76  ASP 76  76  76  ASP ASP F . n 
F 1 77  GLU 77  77  77  GLU GLU F . n 
F 1 78  GLU 78  78  78  GLU GLU F . n 
F 1 79  ARG 79  79  79  ARG ARG F . n 
F 1 80  HIS 80  80  80  HIS HIS F . n 
F 1 81  VAL 81  81  81  VAL VAL F . n 
F 1 82  GLY 82  82  82  GLY GLY F . n 
F 1 83  ASP 83  83  83  ASP ASP F . n 
F 1 84  LEU 84  84  84  LEU LEU F . n 
F 1 85  GLY 85  85  85  GLY GLY F . n 
F 1 86  ASN 86  86  86  ASN ASN F . n 
F 1 87  VAL 87  87  87  VAL VAL F . n 
F 1 88  THR 88  88  88  THR THR F . n 
F 1 89  ALA 89  89  89  ALA ALA F . n 
F 1 90  ASP 90  90  90  ASP ASP F . n 
F 1 91  LYS 91  91  91  LYS LYS F . n 
F 1 92  ASP 92  92  92  ASP ASP F . n 
F 1 93  GLY 93  93  93  GLY GLY F . n 
F 1 94  VAL 94  94  94  VAL VAL F . n 
F 1 95  ALA 95  95  95  ALA ALA F . n 
F 1 96  ASP 96  96  96  ASP ASP F . n 
F 1 97  VAL 97  97  97  VAL VAL F . n 
F 1 98  SER 98  98  98  SER SER F . n 
F 1 99  ILE 99  99  99  ILE ILE F . n 
F 1 100 GLU 100 100 100 GLU GLU F . n 
F 1 101 ASP 101 101 101 ASP ASP F . n 
F 1 102 SER 102 102 102 SER SER F . n 
F 1 103 VAL 103 103 103 VAL VAL F . n 
F 1 104 ILE 104 104 104 ILE ILE F . n 
F 1 105 SER 105 105 105 SER SER F . n 
F 1 106 LEU 106 106 106 LEU LEU F . n 
F 1 107 SER 107 107 107 SER SER F . n 
F 1 108 GLY 108 108 108 GLY GLY F . n 
F 1 109 ASP 109 109 109 ASP ASP F . n 
F 1 110 HIS 110 110 110 HIS HIS F . n 
F 1 111 CYS 111 111 111 CYS CYS F . n 
F 1 112 ILE 112 112 112 ILE ILE F . n 
F 1 113 ILE 113 113 113 ILE ILE F . n 
F 1 114 GLY 114 114 114 GLY GLY F . n 
F 1 115 ARG 115 115 115 ARG ARG F . n 
F 1 116 THR 116 116 116 THR THR F . n 
F 1 117 LEU 117 117 117 LEU LEU F . n 
F 1 118 VAL 118 118 118 VAL VAL F . n 
F 1 119 VAL 119 119 119 VAL VAL F . n 
F 1 120 HIS 120 120 120 HIS HIS F . n 
F 1 121 GLU 121 121 121 GLU GLU F . n 
F 1 122 LYS 122 122 122 LYS LYS F . n 
F 1 123 ALA 123 123 123 ALA ALA F . n 
F 1 124 ASP 124 124 124 ASP ASP F . n 
F 1 125 ASP 125 125 125 ASP ASP F . n 
F 1 126 LEU 126 126 126 LEU LEU F . n 
F 1 127 GLY 127 127 127 GLY GLY F . n 
F 1 128 LYS 128 128 128 LYS LYS F . n 
F 1 129 GLY 129 129 129 GLY GLY F . n 
F 1 130 GLY 130 130 130 GLY GLY F . n 
F 1 131 ASN 131 131 131 ASN ASN F . n 
F 1 132 GLU 132 132 132 GLU GLU F . n 
F 1 133 GLU 133 133 133 GLU GLU F . n 
F 1 134 SER 134 134 134 SER SER F . n 
F 1 135 THR 135 135 135 THR THR F . n 
F 1 136 LYS 136 136 136 LYS LYS F . n 
F 1 137 THR 137 137 137 THR THR F . n 
F 1 138 GLY 138 138 138 GLY GLY F . n 
F 1 139 ASN 139 139 139 ASN ASN F . n 
F 1 140 ALA 140 140 140 ALA ALA F . n 
F 1 141 GLY 141 141 141 GLY GLY F . n 
F 1 142 SER 142 142 142 SER SER F . n 
F 1 143 ARG 143 143 143 ARG ARG F . n 
F 1 144 LEU 144 144 144 LEU LEU F . n 
F 1 145 ALA 145 145 145 ALA ALA F . n 
F 1 146 CYS 146 146 146 CYS CYS F . n 
F 1 147 GLY 147 147 147 GLY GLY F . n 
F 1 148 VAL 148 148 148 VAL VAL F . n 
F 1 149 ILE 149 149 149 ILE ILE F . n 
F 1 150 GLY 150 150 150 GLY GLY F . n 
F 1 151 ILE 151 151 151 ILE ILE F . n 
F 1 152 ALA 152 152 152 ALA ALA F . n 
F 1 153 GLN 153 153 153 GLN GLN F . 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 
G 2 ZN  1  1001 1001 ZN  ZN  A . 
H 2 ZN  1  1001 1001 ZN  ZN  B . 
I 2 ZN  1  1001 1001 ZN  ZN  C . 
J 2 ZN  1  1001 1001 ZN  ZN  D . 
K 2 ZN  1  1001 1001 ZN  ZN  E . 
L 2 ZN  1  1001 1001 ZN  ZN  F . 
M 3 HOH 1  154  1    HOH HOH A . 
M 3 HOH 2  155  8    HOH HOH A . 
M 3 HOH 3  156  9    HOH HOH A . 
M 3 HOH 4  157  11   HOH HOH A . 
M 3 HOH 5  158  12   HOH HOH A . 
M 3 HOH 6  159  15   HOH HOH A . 
M 3 HOH 7  160  21   HOH HOH A . 
M 3 HOH 8  161  22   HOH HOH A . 
M 3 HOH 9  162  23   HOH HOH A . 
M 3 HOH 10 163  31   HOH HOH A . 
M 3 HOH 11 164  32   HOH HOH A . 
M 3 HOH 12 165  33   HOH HOH A . 
M 3 HOH 13 166  48   HOH HOH A . 
M 3 HOH 14 167  50   HOH HOH A . 
M 3 HOH 15 168  53   HOH HOH A . 
M 3 HOH 16 169  56   HOH HOH A . 
M 3 HOH 17 170  58   HOH HOH A . 
M 3 HOH 18 171  61   HOH HOH A . 
M 3 HOH 19 172  63   HOH HOH A . 
M 3 HOH 20 173  77   HOH HOH A . 
M 3 HOH 21 174  80   HOH HOH A . 
M 3 HOH 22 175  83   HOH HOH A . 
M 3 HOH 23 176  84   HOH HOH A . 
M 3 HOH 24 177  85   HOH HOH A . 
M 3 HOH 25 178  86   HOH HOH A . 
M 3 HOH 26 179  90   HOH HOH A . 
M 3 HOH 27 180  92   HOH HOH A . 
M 3 HOH 28 181  98   HOH HOH A . 
M 3 HOH 29 182  99   HOH HOH A . 
M 3 HOH 30 183  101  HOH HOH A . 
M 3 HOH 31 184  104  HOH HOH A . 
M 3 HOH 32 185  105  HOH HOH A . 
M 3 HOH 33 186  115  HOH HOH A . 
M 3 HOH 34 187  116  HOH HOH A . 
M 3 HOH 35 188  119  HOH HOH A . 
M 3 HOH 36 189  120  HOH HOH A . 
M 3 HOH 37 190  124  HOH HOH A . 
M 3 HOH 38 191  125  HOH HOH A . 
M 3 HOH 39 192  135  HOH HOH A . 
M 3 HOH 40 193  143  HOH HOH A . 
M 3 HOH 41 194  145  HOH HOH A . 
N 3 HOH 1  154  2    HOH HOH B . 
N 3 HOH 2  155  6    HOH HOH B . 
N 3 HOH 3  156  13   HOH HOH B . 
N 3 HOH 4  157  16   HOH HOH B . 
N 3 HOH 5  158  26   HOH HOH B . 
N 3 HOH 6  159  27   HOH HOH B . 
N 3 HOH 7  160  35   HOH HOH B . 
N 3 HOH 8  161  46   HOH HOH B . 
N 3 HOH 9  162  47   HOH HOH B . 
N 3 HOH 10 163  52   HOH HOH B . 
N 3 HOH 11 164  66   HOH HOH B . 
N 3 HOH 12 165  68   HOH HOH B . 
N 3 HOH 13 166  69   HOH HOH B . 
N 3 HOH 14 167  70   HOH HOH B . 
N 3 HOH 15 168  72   HOH HOH B . 
N 3 HOH 16 169  76   HOH HOH B . 
N 3 HOH 17 170  79   HOH HOH B . 
N 3 HOH 18 171  81   HOH HOH B . 
N 3 HOH 19 172  89   HOH HOH B . 
N 3 HOH 20 173  94   HOH HOH B . 
N 3 HOH 21 174  100  HOH HOH B . 
N 3 HOH 22 175  103  HOH HOH B . 
N 3 HOH 23 176  108  HOH HOH B . 
N 3 HOH 24 177  111  HOH HOH B . 
N 3 HOH 25 178  113  HOH HOH B . 
N 3 HOH 26 179  114  HOH HOH B . 
N 3 HOH 27 180  118  HOH HOH B . 
N 3 HOH 28 181  128  HOH HOH B . 
N 3 HOH 29 182  130  HOH HOH B . 
N 3 HOH 30 183  131  HOH HOH B . 
N 3 HOH 31 184  134  HOH HOH B . 
N 3 HOH 32 185  139  HOH HOH B . 
N 3 HOH 33 186  141  HOH HOH B . 
O 3 HOH 1  154  3    HOH HOH C . 
O 3 HOH 2  155  29   HOH HOH C . 
O 3 HOH 3  156  39   HOH HOH C . 
O 3 HOH 4  157  44   HOH HOH C . 
O 3 HOH 5  158  54   HOH HOH C . 
O 3 HOH 6  159  65   HOH HOH C . 
O 3 HOH 7  160  87   HOH HOH C . 
O 3 HOH 8  161  132  HOH HOH C . 
P 3 HOH 1  154  4    HOH HOH D . 
P 3 HOH 2  155  5    HOH HOH D . 
P 3 HOH 3  156  18   HOH HOH D . 
P 3 HOH 4  157  19   HOH HOH D . 
P 3 HOH 5  158  20   HOH HOH D . 
P 3 HOH 6  159  41   HOH HOH D . 
P 3 HOH 7  160  43   HOH HOH D . 
P 3 HOH 8  161  49   HOH HOH D . 
P 3 HOH 9  162  59   HOH HOH D . 
P 3 HOH 10 163  60   HOH HOH D . 
P 3 HOH 11 164  62   HOH HOH D . 
P 3 HOH 12 165  64   HOH HOH D . 
P 3 HOH 13 166  67   HOH HOH D . 
P 3 HOH 14 167  74   HOH HOH D . 
P 3 HOH 15 168  91   HOH HOH D . 
P 3 HOH 16 169  96   HOH HOH D . 
P 3 HOH 17 170  106  HOH HOH D . 
P 3 HOH 18 171  109  HOH HOH D . 
P 3 HOH 19 172  110  HOH HOH D . 
P 3 HOH 20 173  112  HOH HOH D . 
P 3 HOH 21 174  123  HOH HOH D . 
P 3 HOH 22 175  127  HOH HOH D . 
P 3 HOH 23 176  129  HOH HOH D . 
P 3 HOH 24 177  137  HOH HOH D . 
P 3 HOH 25 178  138  HOH HOH D . 
P 3 HOH 26 179  144  HOH HOH D . 
Q 3 HOH 1  154  17   HOH HOH E . 
Q 3 HOH 2  155  24   HOH HOH E . 
Q 3 HOH 3  156  117  HOH HOH E . 
Q 3 HOH 4  157  133  HOH HOH E . 
R 3 HOH 1  154  7    HOH HOH F . 
R 3 HOH 2  155  10   HOH HOH F . 
R 3 HOH 3  156  14   HOH HOH F . 
R 3 HOH 4  157  25   HOH HOH F . 
R 3 HOH 5  158  28   HOH HOH F . 
R 3 HOH 6  159  30   HOH HOH F . 
R 3 HOH 7  160  34   HOH HOH F . 
R 3 HOH 8  161  36   HOH HOH F . 
R 3 HOH 9  162  37   HOH HOH F . 
R 3 HOH 10 163  38   HOH HOH F . 
R 3 HOH 11 164  40   HOH HOH F . 
R 3 HOH 12 165  42   HOH HOH F . 
R 3 HOH 13 166  45   HOH HOH F . 
R 3 HOH 14 167  51   HOH HOH F . 
R 3 HOH 15 168  55   HOH HOH F . 
R 3 HOH 16 169  57   HOH HOH F . 
R 3 HOH 17 170  71   HOH HOH F . 
R 3 HOH 18 171  73   HOH HOH F . 
R 3 HOH 19 172  75   HOH HOH F . 
R 3 HOH 20 173  78   HOH HOH F . 
R 3 HOH 21 174  82   HOH HOH F . 
R 3 HOH 22 175  88   HOH HOH F . 
R 3 HOH 23 176  93   HOH HOH F . 
R 3 HOH 24 177  95   HOH HOH F . 
R 3 HOH 25 178  97   HOH HOH F . 
R 3 HOH 26 179  102  HOH HOH F . 
R 3 HOH 27 180  107  HOH HOH F . 
R 3 HOH 28 181  121  HOH HOH F . 
R 3 HOH 29 182  122  HOH HOH F . 
R 3 HOH 30 183  126  HOH HOH F . 
R 3 HOH 31 184  136  HOH HOH F . 
R 3 HOH 32 185  140  HOH HOH F . 
R 3 HOH 33 186  142  HOH HOH F . 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA dimeric 2 
2 author_and_software_defined_assembly PISA dimeric 2 
3 author_and_software_defined_assembly PISA dimeric 2 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,G,H,M,N 
2 1 C,D,I,J,O,P 
3 1 E,F,K,L,Q,R 
# 
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)' 1300  ? 
1 MORE         -11   ? 
1 'SSA (A^2)'  13670 ? 
2 'ABSA (A^2)' 1260  ? 
2 MORE         -10   ? 
2 'SSA (A^2)'  13520 ? 
3 'ABSA (A^2)' 1310  ? 
3 MORE         -10   ? 
3 'SSA (A^2)'  13610 ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  ND1 ? D HIS 71 ? D HIS 71 ? 1_555 ZN ? J ZN . ? D ZN 1001 ? 1_555 ND1 ? D HIS 63 ? D HIS 63 ? 1_555 109.5 ? 
2  ND1 ? D HIS 71 ? D HIS 71 ? 1_555 ZN ? J ZN . ? D ZN 1001 ? 1_555 OD1 ? D ASP 83 ? D ASP 83 ? 1_555 109.4 ? 
3  ND1 ? D HIS 63 ? D HIS 63 ? 1_555 ZN ? J ZN . ? D ZN 1001 ? 1_555 OD1 ? D ASP 83 ? D ASP 83 ? 1_555 113.1 ? 
4  ND1 ? D HIS 71 ? D HIS 71 ? 1_555 ZN ? J ZN . ? D ZN 1001 ? 1_555 ND1 ? D HIS 80 ? D HIS 80 ? 1_555 125.1 ? 
5  ND1 ? D HIS 63 ? D HIS 63 ? 1_555 ZN ? J ZN . ? D ZN 1001 ? 1_555 ND1 ? D HIS 80 ? D HIS 80 ? 1_555 100.3 ? 
6  OD1 ? D ASP 83 ? D ASP 83 ? 1_555 ZN ? J ZN . ? D ZN 1001 ? 1_555 ND1 ? D HIS 80 ? D HIS 80 ? 1_555 99.0  ? 
7  OD2 ? B ASP 83 ? B ASP 83 ? 1_555 ZN ? H ZN . ? B ZN 1001 ? 1_555 ND1 ? B HIS 71 ? B HIS 71 ? 1_555 93.7  ? 
8  OD2 ? B ASP 83 ? B ASP 83 ? 1_555 ZN ? H ZN . ? B ZN 1001 ? 1_555 ND1 ? B HIS 80 ? B HIS 80 ? 1_555 121.2 ? 
9  ND1 ? B HIS 71 ? B HIS 71 ? 1_555 ZN ? H ZN . ? B ZN 1001 ? 1_555 ND1 ? B HIS 80 ? B HIS 80 ? 1_555 121.7 ? 
10 OD2 ? B ASP 83 ? B ASP 83 ? 1_555 ZN ? H ZN . ? B ZN 1001 ? 1_555 ND1 ? B HIS 63 ? B HIS 63 ? 1_555 107.9 ? 
11 ND1 ? B HIS 71 ? B HIS 71 ? 1_555 ZN ? H ZN . ? B ZN 1001 ? 1_555 ND1 ? B HIS 63 ? B HIS 63 ? 1_555 100.4 ? 
12 ND1 ? B HIS 80 ? B HIS 80 ? 1_555 ZN ? H ZN . ? B ZN 1001 ? 1_555 ND1 ? B HIS 63 ? B HIS 63 ? 1_555 109.3 ? 
13 ND1 ? E HIS 80 ? E HIS 80 ? 1_555 ZN ? K ZN . ? E ZN 1001 ? 1_555 ND1 ? E HIS 63 ? E HIS 63 ? 1_555 127.8 ? 
14 ND1 ? E HIS 80 ? E HIS 80 ? 1_555 ZN ? K ZN . ? E ZN 1001 ? 1_555 OD2 ? E ASP 83 ? E ASP 83 ? 1_555 134.7 ? 
15 ND1 ? E HIS 63 ? E HIS 63 ? 1_555 ZN ? K ZN . ? E ZN 1001 ? 1_555 OD2 ? E ASP 83 ? E ASP 83 ? 1_555 84.8  ? 
16 ND1 ? E HIS 80 ? E HIS 80 ? 1_555 ZN ? K ZN . ? E ZN 1001 ? 1_555 ND1 ? E HIS 71 ? E HIS 71 ? 1_555 121.9 ? 
17 ND1 ? E HIS 63 ? E HIS 63 ? 1_555 ZN ? K ZN . ? E ZN 1001 ? 1_555 ND1 ? E HIS 71 ? E HIS 71 ? 1_555 91.9  ? 
18 OD2 ? E ASP 83 ? E ASP 83 ? 1_555 ZN ? K ZN . ? E ZN 1001 ? 1_555 ND1 ? E HIS 71 ? E HIS 71 ? 1_555 80.8  ? 
19 ND1 ? E HIS 80 ? E HIS 80 ? 1_555 ZN ? K ZN . ? E ZN 1001 ? 1_555 OD1 ? E ASP 83 ? E ASP 83 ? 1_555 83.6  ? 
20 ND1 ? E HIS 63 ? E HIS 63 ? 1_555 ZN ? K ZN . ? E ZN 1001 ? 1_555 OD1 ? E ASP 83 ? E ASP 83 ? 1_555 137.8 ? 
21 OD2 ? E ASP 83 ? E ASP 83 ? 1_555 ZN ? K ZN . ? E ZN 1001 ? 1_555 OD1 ? E ASP 83 ? E ASP 83 ? 1_555 54.7  ? 
22 ND1 ? E HIS 71 ? E HIS 71 ? 1_555 ZN ? K ZN . ? E ZN 1001 ? 1_555 OD1 ? E ASP 83 ? E ASP 83 ? 1_555 92.4  ? 
23 ND1 ? F HIS 63 ? F HIS 63 ? 1_555 ZN ? L ZN . ? F ZN 1001 ? 1_555 OD2 ? F ASP 83 ? F ASP 83 ? 1_555 101.9 ? 
24 ND1 ? F HIS 63 ? F HIS 63 ? 1_555 ZN ? L ZN . ? F ZN 1001 ? 1_555 ND1 ? F HIS 80 ? F HIS 80 ? 1_555 106.6 ? 
25 OD2 ? F ASP 83 ? F ASP 83 ? 1_555 ZN ? L ZN . ? F ZN 1001 ? 1_555 ND1 ? F HIS 80 ? F HIS 80 ? 1_555 112.1 ? 
26 ND1 ? F HIS 63 ? F HIS 63 ? 1_555 ZN ? L ZN . ? F ZN 1001 ? 1_555 ND1 ? F HIS 71 ? F HIS 71 ? 1_555 108.1 ? 
27 OD2 ? F ASP 83 ? F ASP 83 ? 1_555 ZN ? L ZN . ? F ZN 1001 ? 1_555 ND1 ? F HIS 71 ? F HIS 71 ? 1_555 100.6 ? 
28 ND1 ? F HIS 80 ? F HIS 80 ? 1_555 ZN ? L ZN . ? F ZN 1001 ? 1_555 ND1 ? F HIS 71 ? F HIS 71 ? 1_555 125.1 ? 
29 OD2 ? A ASP 83 ? A ASP 83 ? 1_555 ZN ? G ZN . ? A ZN 1001 ? 1_555 ND1 ? A HIS 80 ? A HIS 80 ? 1_555 107.2 ? 
30 OD2 ? A ASP 83 ? A ASP 83 ? 1_555 ZN ? G ZN . ? A ZN 1001 ? 1_555 ND1 ? A HIS 63 ? A HIS 63 ? 1_555 97.2  ? 
31 ND1 ? A HIS 80 ? A HIS 80 ? 1_555 ZN ? G ZN . ? A ZN 1001 ? 1_555 ND1 ? A HIS 63 ? A HIS 63 ? 1_555 115.1 ? 
32 OD2 ? A ASP 83 ? A ASP 83 ? 1_555 ZN ? G ZN . ? A ZN 1001 ? 1_555 ND1 ? A HIS 71 ? A HIS 71 ? 1_555 102.1 ? 
33 ND1 ? A HIS 80 ? A HIS 80 ? 1_555 ZN ? G ZN . ? A ZN 1001 ? 1_555 ND1 ? A HIS 71 ? A HIS 71 ? 1_555 121.2 ? 
34 ND1 ? A HIS 63 ? A HIS 63 ? 1_555 ZN ? G ZN . ? A ZN 1001 ? 1_555 ND1 ? A HIS 71 ? A HIS 71 ? 1_555 110.2 ? 
35 ND1 ? C HIS 80 ? C HIS 80 ? 1_555 ZN ? I ZN . ? C ZN 1001 ? 1_555 ND1 ? C HIS 71 ? C HIS 71 ? 1_555 116.6 ? 
36 ND1 ? C HIS 80 ? C HIS 80 ? 1_555 ZN ? I ZN . ? C ZN 1001 ? 1_555 OD1 ? C ASP 83 ? C ASP 83 ? 1_555 138.0 ? 
37 ND1 ? C HIS 71 ? C HIS 71 ? 1_555 ZN ? I ZN . ? C ZN 1001 ? 1_555 OD1 ? C ASP 83 ? C ASP 83 ? 1_555 77.5  ? 
# 
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 2010-09-08 
2 'Structure model' 1 1 2011-07-13 
3 'Structure model' 1 2 2017-06-07 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' 'Database references'       
3 3 'Structure model' 'Structure summary'         
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
PHASER   phasing          .                        ? 1 
PHENIX   refinement       '(phenix.refine: 1.5_2)' ? 2 
HKL-2000 'data reduction' .                        ? 3 
HKL-2000 'data scaling'   .                        ? 4 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASN A 65  ? ? -143.65 54.50   
2  1 ALA B 145 ? ? -178.13 148.69  
3  1 HIS C 63  ? ? -39.54  139.02  
4  1 ASN C 65  ? ? -159.78 63.90   
5  1 LYS C 69  ? ? -61.42  -157.06 
6  1 ASP C 76  ? ? -39.29  137.40  
7  1 ASP C 90  ? ? -66.09  -153.96 
8  1 ASP C 92  ? ? -95.64  34.73   
9  1 CYS C 111 ? ? -47.06  108.59  
10 1 PRO D 28  ? ? -40.35  152.09  
11 1 SER E 25  ? ? -35.94  -108.30 
12 1 GLN E 34  ? ? -171.93 128.14  
13 1 GLN E 55  ? ? -112.99 63.78   
14 1 ASN E 65  ? ? -164.66 77.13   
15 1 SER E 68  ? ? 28.51   55.45   
16 1 ASP E 76  ? ? -46.10  165.52  
17 1 SER E 107 ? ? 176.37  163.31  
18 1 SER F 25  ? ? -19.87  -88.09  
19 1 GLN F 55  ? ? -106.94 51.53   
20 1 ASN F 65  ? ? -154.96 59.56   
# 
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 C LYS 128 ? C LYS 128 
2 1 Y 1 C GLY 129 ? C GLY 129 
3 1 Y 1 C GLY 130 ? C GLY 130 
4 1 Y 1 D GLN 153 ? D GLN 153 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION' ZN  
3 water      HOH 
# 
