data_3KH4
# 
_entry.id   3KH4 
# 
_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   3KH4         
RCSB  RCSB055985   
WWPDB D_1000055985 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.db_id          3KH3 
_pdbx_database_related.details        'P212121 crystal form' 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_database_status.entry_id                        3KH4 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.recvd_initial_deposition_date   2009-10-30 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_cs                  ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Gazdag, E.M.'     1 
'Blankenfeldt, W.' 2 
# 
_citation.id                        primary 
_citation.title                     
'Purification and crystallization of human Cu/Zn superoxide dismutase recombinantly produced in the protozoan Leishmania tarentolae.' 
_citation.journal_abbrev            'Acta Crystallogr.,Sect.F' 
_citation.journal_volume            66 
_citation.page_first                871 
_citation.page_last                 877 
_citation.year                      2010 
_citation.journal_id_ASTM           ? 
_citation.country                   DK 
_citation.journal_id_ISSN           1744-3091 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   20693657 
_citation.pdbx_database_id_DOI      10.1107/S1744309110019330 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Gazdag, E.M.'     1 
primary 'Cirstea, I.C.'    2 
primary 'Breitling, R.'    3 
primary 'Lukes, J.'        4 
primary 'Blankenfeldt, W.' 5 
primary 'Alexandrov, K.'   6 
# 
_cell.entry_id           3KH4 
_cell.length_a           112.188 
_cell.length_b           112.188 
_cell.length_c           428.268 
_cell.angle_alpha        90.000 
_cell.angle_beta         90.000 
_cell.angle_gamma        120.000 
_cell.pdbx_unique_axis   ? 
_cell.Z_PDB              72 
_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                         3KH4 
_symmetry.Int_Tables_number                179 
_symmetry.space_group_name_H-M             'P 65 2 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_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]' 15827.561 6 1.15.1.1 ? ? ? 
2 non-polymer syn 'COPPER (II) ION'              63.546    6 ?        ? ? ? 
3 non-polymer syn 'ZINC ION'                     65.409    6 ?        ? ? ? 
# 
_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       
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
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   THR 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  ILE n 
1 18  ILE n 
1 19  ASN n 
1 20  PHE n 
1 21  GLU n 
1 22  GLN n 
1 23  LYS n 
1 24  GLU n 
1 25  SER n 
1 26  ASN n 
1 27  GLY n 
1 28  PRO n 
1 29  VAL n 
1 30  LYS n 
1 31  VAL n 
1 32  TRP n 
1 33  GLY n 
1 34  SER n 
1 35  ILE n 
1 36  LYS n 
1 37  GLY n 
1 38  LEU n 
1 39  THR n 
1 40  GLU n 
1 41  GLY n 
1 42  LEU 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  GLU n 
1 50  PHE n 
1 51  GLY n 
1 52  ASP n 
1 53  ASN n 
1 54  THR n 
1 55  ALA 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  LEU n 
1 68  SER n 
1 69  ARG n 
1 70  LYS n 
1 71  HIS n 
1 72  GLY n 
1 73  GLY n 
1 74  PRO n 
1 75  LYS 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 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 SOD1 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Leishmania tarentolae' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     5689 
_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               P10 
_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          'chromosomal integration' 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    SODC_HUMAN 
_struct_ref.pdbx_db_accession          P00441 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_struct_ref.pdbx_align_begin           2 
_struct_ref.pdbx_db_isoform            ? 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 3KH4 A 1 ? 153 ? P00441 2 ? 154 ? 1 153 
2 1 3KH4 B 1 ? 153 ? P00441 2 ? 154 ? 1 153 
3 1 3KH4 C 1 ? 153 ? P00441 2 ? 154 ? 1 153 
4 1 3KH4 D 1 ? 153 ? P00441 2 ? 154 ? 1 153 
5 1 3KH4 E 1 ? 153 ? P00441 2 ? 154 ? 1 153 
6 1 3KH4 F 1 ? 153 ? P00441 2 ? 154 ? 1 153 
# 
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 
CU  non-polymer         . 'COPPER (II) ION' ? 'Cu 2'           63.546  
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 
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 
PHE 'L-peptide linking' y PHENYLALANINE     ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE           ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE            ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE         ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN        ? 'C11 H12 N2 O2'  204.225 
VAL 'L-peptide linking' y VALINE            ? 'C5 H11 N O2'    117.146 
ZN  non-polymer         . 'ZINC ION'        ? 'Zn 2'           65.409  
# 
_exptl.crystals_number   1 
_exptl.entry_id          3KH4 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_percent_sol   69.97 
_exptl_crystal.density_Matthews      4.10 
_exptl_crystal.density_meas          ? 
_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.pH              ? 
_exptl_crystal_grow.temp            292 
_exptl_crystal_grow.pdbx_details    
'21-25% (w/v) PEG4000, 0.1 M NaOAc, pH 4.2-5.2, vapor diffusion, hanging drop, temperature 292K' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   4.2-5.2 
# 
_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                   'MARMOSAIC 225 mm CCD' 
_diffrn_detector.pdbx_collection_date   2009-10-08 
_diffrn_detector.details                'SI(111)' 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.monochromator                    'SI(111) MONOCHROMATOR' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'SLS BEAMLINE X10SA' 
_diffrn_source.pdbx_wavelength_list        1.0 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_site       SLS 
_diffrn_source.pdbx_synchrotron_beamline   X10SA 
# 
_reflns.entry_id                     3KH4 
_reflns.d_resolution_high            3.500 
_reflns.number_obs                   21168 
_reflns.pdbx_Rmerge_I_obs            0.172 
_reflns.pdbx_netI_over_sigmaI        13.130 
_reflns.percent_possible_obs         99.900 
_reflns.B_iso_Wilson_estimate        47.084 
_reflns.observed_criterion_sigma_I   -3.00 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             49.69 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_redundancy              ? 
_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 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.number_unique_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
3.50  3.60  18102 ? 1668 0.586 4.2  ? ? ? ? ? 100.00 ? 1  
3.60  3.70  16033 ? 1476 0.495 4.9  ? ? ? ? ? 100.00 ? 2  
3.70  3.80  14452 ? 1338 0.435 5.5  ? ? ? ? ? 100.00 ? 3  
3.80  3.90  13005 ? 1212 0.382 6.3  ? ? ? ? ? 100.00 ? 4  
3.90  4.00  11863 ? 1100 0.299 7.7  ? ? ? ? ? 100.00 ? 5  
4.00  5.00  72706 ? 6809 0.171 12.7 ? ? ? ? ? 100.00 ? 6  
5.00  6.00  32145 ? 3069 0.150 14.2 ? ? ? ? ? 100.00 ? 7  
6.00  7.00  16475 ? 1607 0.117 16.7 ? ? ? ? ? 100.00 ? 8  
7.00  10.00 18274 ? 1827 0.080 22.5 ? ? ? ? ? 99.90  ? 9  
10.00 15.00 6730  ? 721  0.041 37.9 ? ? ? ? ? 100.00 ? 10 
15.00 20.00 1633  ? 193  0.029 43.7 ? ? ? ? ? 100.00 ? 11 
20.00 ?     1102  ? 148  0.027 43.1 ? ? ? ? ? 91.40  ? 12 
# 
_refine.entry_id                                 3KH4 
_refine.ls_d_res_high                            3.500 
_refine.ls_d_res_low                             49.69 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.ls_percent_reflns_obs                    99.920 
_refine.ls_number_reflns_obs                     21168 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  
;HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
U VALUES: RESIDUAL ONLY
;
_refine.ls_R_factor_obs                          0.201 
_refine.ls_R_factor_R_work                       0.201 
_refine.ls_R_factor_R_free                       0.208 
_refine.ls_percent_reflns_R_free                 5.100 
_refine.ls_number_reflns_R_free                  1088 
_refine.B_iso_mean                               90.385 
_refine.aniso_B[1][1]                            -8.440 
_refine.aniso_B[2][2]                            -8.440 
_refine.aniso_B[3][3]                            12.650 
_refine.aniso_B[1][2]                            -4.220 
_refine.aniso_B[1][3]                            0.000 
_refine.aniso_B[2][3]                            0.000 
_refine.correlation_coeff_Fo_to_Fc               0.934 
_refine.correlation_coeff_Fo_to_Fc_free          0.930 
_refine.pdbx_overall_ESU_R_Free                  0.428 
_refine.overall_SU_ML                            0.310 
_refine.overall_SU_B                             46.112 
_refine.solvent_model_details                    'BABINET MODEL WITH MASK' 
_refine.pdbx_solvent_vdw_probe_radii             1.400 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.B_iso_max                                157.11 
_refine.B_iso_min                                60.37 
_refine.occupancy_max                            1.00 
_refine.occupancy_min                            1.00 
_refine.pdbx_ls_sigma_I                          ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        6660 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         12 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               6672 
_refine_hist.d_res_high                       3.500 
_refine_hist.d_res_low                        49.69 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d       6774  0.017  0.021  ? 'X-RAY DIFFRACTION' ? 
r_bond_other_d         4482  0.000  0.020  ? 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg    9144  1.434  1.945  ? 'X-RAY DIFFRACTION' ? 
r_angle_other_deg      11034 4.332  3.000  ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg 912   7.179  5.000  ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg 288   40.163 25.625 ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg 1110  18.979 15.000 ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg 24    11.035 15.000 ? 'X-RAY DIFFRACTION' ? 
r_chiral_restr         1008  0.080  0.200  ? 'X-RAY DIFFRACTION' ? 
r_gen_planes_refined   7818  0.006  0.020  ? 'X-RAY DIFFRACTION' ? 
r_gen_planes_other     1224  0.004  0.020  ? 'X-RAY DIFFRACTION' ? 
r_mcbond_it            4470  0.447  1.500  ? 'X-RAY DIFFRACTION' ? 
r_mcbond_other         1950  0.000  1.500  ? 'X-RAY DIFFRACTION' ? 
r_mcangle_it           7104  0.933  2.000  ? 'X-RAY DIFFRACTION' ? 
r_scbond_it            2304  1.405  3.000  ? 'X-RAY DIFFRACTION' ? 
r_scangle_it           2040  2.630  4.500  ? 'X-RAY DIFFRACTION' ? 
# 
loop_
_refine_ls_restr_ncs.pdbx_ens_id 
_refine_ls_restr_ncs.dom_id 
_refine_ls_restr_ncs.pdbx_type 
_refine_ls_restr_ncs.pdbx_auth_asym_id 
_refine_ls_restr_ncs.pdbx_number 
_refine_ls_restr_ncs.rms_dev_position 
_refine_ls_restr_ncs.weight_position 
_refine_ls_restr_ncs.pdbx_ordinal 
_refine_ls_restr_ncs.pdbx_refine_id 
_refine_ls_restr_ncs.ncs_model_details 
_refine_ls_restr_ncs.rms_dev_B_iso 
_refine_ls_restr_ncs.weight_B_iso 
1 1 'TIGHT POSITIONAL' A 1857 0.040 0.050 1  'X-RAY DIFFRACTION' ? ? ? 
1 2 'TIGHT POSITIONAL' B 1857 0.040 0.050 2  'X-RAY DIFFRACTION' ? ? ? 
1 3 'TIGHT POSITIONAL' C 1857 0.040 0.050 3  'X-RAY DIFFRACTION' ? ? ? 
1 4 'TIGHT POSITIONAL' D 1857 0.040 0.050 4  'X-RAY DIFFRACTION' ? ? ? 
1 5 'TIGHT POSITIONAL' E 1857 0.040 0.050 5  'X-RAY DIFFRACTION' ? ? ? 
1 6 'TIGHT POSITIONAL' F 1857 0.040 0.050 6  'X-RAY DIFFRACTION' ? ? ? 
1 1 'TIGHT THERMAL'    A 1857 0.070 0.500 7  'X-RAY DIFFRACTION' ? ? ? 
1 2 'TIGHT THERMAL'    B 1857 0.070 0.500 8  'X-RAY DIFFRACTION' ? ? ? 
1 3 'TIGHT THERMAL'    C 1857 0.070 0.500 9  'X-RAY DIFFRACTION' ? ? ? 
1 4 'TIGHT THERMAL'    D 1857 0.060 0.500 10 'X-RAY DIFFRACTION' ? ? ? 
1 5 'TIGHT THERMAL'    E 1857 0.060 0.500 11 'X-RAY DIFFRACTION' ? ? ? 
1 6 'TIGHT THERMAL'    F 1857 0.060 0.500 12 'X-RAY DIFFRACTION' ? ? ? 
# 
_refine_ls_shell.d_res_high                       3.500 
_refine_ls_shell.d_res_low                        3.591 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               100.000 
_refine_ls_shell.number_reflns_R_work             1451 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.257 
_refine_ls_shell.R_factor_R_free                  0.282 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             77 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                1528 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
loop_
_struct_ncs_dom.pdbx_ens_id 
_struct_ncs_dom.id 
_struct_ncs_dom.details 
1 1 A 
1 2 B 
1 3 C 
1 4 D 
1 5 E 
1 6 F 
# 
loop_
_struct_ncs_dom_lim.pdbx_ens_id 
_struct_ncs_dom_lim.dom_id 
_struct_ncs_dom_lim.pdbx_component_id 
_struct_ncs_dom_lim.beg_label_asym_id 
_struct_ncs_dom_lim.beg_label_seq_id 
_struct_ncs_dom_lim.end_label_asym_id 
_struct_ncs_dom_lim.end_label_seq_id 
_struct_ncs_dom_lim.pdbx_refine_code 
_struct_ncs_dom_lim.beg_label_alt_id 
_struct_ncs_dom_lim.end_label_alt_id 
_struct_ncs_dom_lim.beg_label_comp_id 
_struct_ncs_dom_lim.end_label_comp_id 
_struct_ncs_dom_lim.beg_auth_asym_id 
_struct_ncs_dom_lim.beg_auth_seq_id 
_struct_ncs_dom_lim.end_auth_asym_id 
_struct_ncs_dom_lim.end_auth_seq_id 
_struct_ncs_dom_lim.selection_details 
1 1 1 A 1 A 153 1 . . . . A 1 A 153 ? 
1 2 1 B 1 B 153 1 . . . . B 1 B 153 ? 
1 3 1 C 1 C 153 1 . . . . C 1 C 153 ? 
1 4 1 D 1 D 153 1 . . . . D 1 D 153 ? 
1 5 1 E 1 E 153 1 . . . . E 1 E 153 ? 
1 6 1 F 1 F 153 1 . . . . F 1 F 153 ? 
# 
_struct_ncs_ens.id        1 
_struct_ncs_ens.details   ? 
# 
_struct.entry_id                  3KH4 
_struct.title                     
;Crystal structure of human Cu/Zn superoxide dismutase recombinantly produced in Leishmania tarantolae; P6522 crystal form containing 6 chains in the asymmetric unit
;
_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        3KH4 
_struct_keywords.text            
;eukaryotic expression, Leishmania tarantolae, Amyotrophic lateral sclerosis, Antioxidant, Disease mutation, Disulfide bond, Metal-binding, Neurodegeneration, Oxidoreductase, Phosphoprotein
;
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
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 3 ? 
I N N 2 ? 
J N N 3 ? 
K N N 2 ? 
L N N 3 ? 
M N N 2 ? 
N N N 3 ? 
O N N 2 ? 
P N N 3 ? 
Q N N 2 ? 
R N N 3 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
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  ALA A 55  ? GLY A 61  ? ALA 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  GLU A 132 ? LYS A 136 ? GLU A 132 LYS A 136 5 ? 5 
HELX_P HELX_P4  4  ALA B 55  ? GLY B 61  ? ALA 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  GLU B 132 ? LYS B 136 ? GLU B 132 LYS B 136 5 ? 5 
HELX_P HELX_P7  7  ALA C 55  ? GLY C 61  ? ALA 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  GLU C 133 ? GLY C 138 ? GLU C 133 GLY C 138 1 ? 6 
HELX_P HELX_P10 10 ALA D 55  ? GLY D 61  ? ALA D 55  GLY D 61  5 ? 7 
HELX_P HELX_P11 11 SER D 107 ? CYS D 111 ? SER D 107 CYS D 111 5 ? 5 
HELX_P HELX_P12 12 GLU D 133 ? GLY D 138 ? GLU D 133 GLY D 138 1 ? 6 
HELX_P HELX_P13 13 ALA E 55  ? GLY E 61  ? ALA E 55  GLY E 61  5 ? 7 
HELX_P HELX_P14 14 SER E 107 ? CYS E 111 ? SER E 107 CYS E 111 5 ? 5 
HELX_P HELX_P15 15 GLU E 133 ? GLY E 138 ? GLU E 133 GLY E 138 1 ? 6 
HELX_P HELX_P16 16 ALA F 55  ? GLY F 61  ? ALA F 55  GLY F 61  5 ? 7 
HELX_P HELX_P17 17 SER F 107 ? CYS F 111 ? SER F 107 CYS F 111 5 ? 5 
HELX_P HELX_P18 18 GLU F 133 ? GLY F 138 ? GLU F 133 GLY F 138 1 ? 6 
# 
_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 ? ? ? ? ? ? ? 2.081 ? 
disulf2  disulf ? ? B CYS 57  SG  ? ? ? 1_555 B CYS 146 SG ? ? B CYS 57  B CYS 146 1_555 ? ? ? ? ? ? ? 2.070 ? 
disulf3  disulf ? ? C CYS 57  SG  ? ? ? 1_555 C CYS 146 SG ? ? C CYS 57  C CYS 146 1_555 ? ? ? ? ? ? ? 2.081 ? 
disulf4  disulf ? ? D CYS 57  SG  ? ? ? 1_555 D CYS 146 SG ? ? D CYS 57  D CYS 146 1_555 ? ? ? ? ? ? ? 2.098 ? 
disulf5  disulf ? ? E CYS 57  SG  ? ? ? 1_555 E CYS 146 SG ? ? E CYS 57  E CYS 146 1_555 ? ? ? ? ? ? ? 2.103 ? 
disulf6  disulf ? ? F CYS 57  SG  ? ? ? 1_555 F CYS 146 SG ? ? F CYS 57  F CYS 146 1_555 ? ? ? ? ? ? ? 2.086 ? 
metalc1  metalc ? ? A HIS 46  ND1 ? ? ? 1_555 G CU  .   CU ? ? A HIS 46  A CU  154 1_555 ? ? ? ? ? ? ? 2.139 ? 
metalc2  metalc ? ? A HIS 63  ND1 ? ? ? 1_555 H ZN  .   ZN ? ? A HIS 63  A ZN  155 1_555 ? ? ? ? ? ? ? 2.101 ? 
metalc3  metalc ? ? A HIS 71  ND1 ? ? ? 1_555 H ZN  .   ZN ? ? A HIS 71  A ZN  155 1_555 ? ? ? ? ? ? ? 2.109 ? 
metalc4  metalc ? ? A HIS 80  ND1 ? ? ? 1_555 H ZN  .   ZN ? ? A HIS 80  A ZN  155 1_555 ? ? ? ? ? ? ? 2.201 ? 
metalc5  metalc ? ? A ASP 83  OD1 ? ? ? 1_555 H ZN  .   ZN ? ? A ASP 83  A ZN  155 1_555 ? ? ? ? ? ? ? 1.806 ? 
metalc6  metalc ? ? A HIS 120 NE2 ? ? ? 1_555 G CU  .   CU ? ? A HIS 120 A CU  154 1_555 ? ? ? ? ? ? ? 2.134 ? 
metalc7  metalc ? ? B HIS 63  ND1 ? ? ? 1_555 J ZN  .   ZN ? ? B HIS 63  B ZN  155 1_555 ? ? ? ? ? ? ? 2.225 ? 
metalc8  metalc ? ? B HIS 71  ND1 ? ? ? 1_555 J ZN  .   ZN ? ? B HIS 71  B ZN  155 1_555 ? ? ? ? ? ? ? 2.159 ? 
metalc9  metalc ? ? B HIS 80  ND1 ? ? ? 1_555 J ZN  .   ZN ? ? B HIS 80  B ZN  155 1_555 ? ? ? ? ? ? ? 2.080 ? 
metalc10 metalc ? ? B ASP 83  OD1 ? ? ? 1_555 J ZN  .   ZN ? ? B ASP 83  B ZN  155 1_555 ? ? ? ? ? ? ? 1.811 ? 
metalc11 metalc ? ? B HIS 120 NE2 ? ? ? 1_555 I CU  .   CU ? ? B HIS 120 B CU  154 1_555 ? ? ? ? ? ? ? 2.159 ? 
metalc12 metalc ? ? C HIS 46  ND1 ? ? ? 1_555 K CU  .   CU ? ? C HIS 46  C CU  154 1_555 ? ? ? ? ? ? ? 2.399 ? 
metalc13 metalc ? ? C HIS 48  NE2 ? ? ? 1_555 K CU  .   CU ? ? C HIS 48  C CU  154 1_555 ? ? ? ? ? ? ? 2.390 ? 
metalc14 metalc ? ? C HIS 63  ND1 ? ? ? 1_555 L ZN  .   ZN ? ? C HIS 63  C ZN  155 1_555 ? ? ? ? ? ? ? 2.144 ? 
metalc15 metalc ? ? C HIS 71  ND1 ? ? ? 1_555 L ZN  .   ZN ? ? C HIS 71  C ZN  155 1_555 ? ? ? ? ? ? ? 2.047 ? 
metalc16 metalc ? ? C HIS 80  ND1 ? ? ? 1_555 L ZN  .   ZN ? ? C HIS 80  C ZN  155 1_555 ? ? ? ? ? ? ? 2.310 ? 
metalc17 metalc ? ? C ASP 83  OD1 ? ? ? 1_555 L ZN  .   ZN ? ? C ASP 83  C ZN  155 1_555 ? ? ? ? ? ? ? 1.787 ? 
metalc18 metalc ? ? C HIS 120 NE2 ? ? ? 1_555 K CU  .   CU ? ? C HIS 120 C CU  154 1_555 ? ? ? ? ? ? ? 2.169 ? 
metalc19 metalc ? ? D HIS 46  ND1 ? ? ? 1_555 M CU  .   CU ? ? D HIS 46  D CU  154 1_555 ? ? ? ? ? ? ? 2.138 ? 
metalc20 metalc ? ? D HIS 63  ND1 ? ? ? 1_555 N ZN  .   ZN ? ? D HIS 63  D ZN  155 1_555 ? ? ? ? ? ? ? 2.081 ? 
metalc21 metalc ? ? D HIS 71  ND1 ? ? ? 1_555 N ZN  .   ZN ? ? D HIS 71  D ZN  155 1_555 ? ? ? ? ? ? ? 1.981 ? 
metalc22 metalc ? ? D HIS 80  ND1 ? ? ? 1_555 N ZN  .   ZN ? ? D HIS 80  D ZN  155 1_555 ? ? ? ? ? ? ? 2.276 ? 
metalc23 metalc ? ? D ASP 83  OD1 ? ? ? 1_555 N ZN  .   ZN ? ? D ASP 83  D ZN  155 1_555 ? ? ? ? ? ? ? 1.824 ? 
metalc24 metalc ? ? D HIS 120 NE2 ? ? ? 1_555 M CU  .   CU ? ? D HIS 120 D CU  154 1_555 ? ? ? ? ? ? ? 2.054 ? 
metalc25 metalc ? ? E HIS 48  NE2 ? ? ? 1_555 O CU  .   CU ? ? E HIS 48  E CU  154 1_555 ? ? ? ? ? ? ? 2.304 ? 
metalc26 metalc ? ? E HIS 63  ND1 ? ? ? 1_555 P ZN  .   ZN ? ? E HIS 63  E ZN  155 1_555 ? ? ? ? ? ? ? 2.341 ? 
metalc27 metalc ? ? E HIS 71  ND1 ? ? ? 1_555 P ZN  .   ZN ? ? E HIS 71  E ZN  155 1_555 ? ? ? ? ? ? ? 2.103 ? 
metalc28 metalc ? ? E HIS 80  ND1 ? ? ? 1_555 P ZN  .   ZN ? ? E HIS 80  E ZN  155 1_555 ? ? ? ? ? ? ? 2.066 ? 
metalc29 metalc ? ? E ASP 83  OD1 ? ? ? 1_555 P ZN  .   ZN ? ? E ASP 83  E ZN  155 1_555 ? ? ? ? ? ? ? 1.933 ? 
metalc30 metalc ? ? E HIS 120 NE2 ? ? ? 1_555 O CU  .   CU ? ? E HIS 120 E CU  154 1_555 ? ? ? ? ? ? ? 2.180 ? 
metalc31 metalc ? ? F HIS 46  ND1 ? ? ? 1_555 Q CU  .   CU ? ? F HIS 46  F CU  154 1_555 ? ? ? ? ? ? ? 2.228 ? 
metalc32 metalc ? ? F HIS 63  ND1 ? ? ? 1_555 R ZN  .   ZN ? ? F HIS 63  F ZN  155 1_555 ? ? ? ? ? ? ? 2.179 ? 
metalc33 metalc ? ? F HIS 71  ND1 ? ? ? 1_555 R ZN  .   ZN ? ? F HIS 71  F ZN  155 1_555 ? ? ? ? ? ? ? 1.911 ? 
metalc34 metalc ? ? F HIS 80  ND1 ? ? ? 1_555 R ZN  .   ZN ? ? F HIS 80  F ZN  155 1_555 ? ? ? ? ? ? ? 2.304 ? 
metalc35 metalc ? ? F ASP 83  OD1 ? ? ? 1_555 R ZN  .   ZN ? ? F ASP 83  F ZN  155 1_555 ? ? ? ? ? ? ? 1.838 ? 
metalc36 metalc ? ? F HIS 120 NE2 ? ? ? 1_555 Q CU  .   CU ? ? F HIS 120 F CU  154 1_555 ? ? ? ? ? ? ? 2.026 ? 
metalc37 metalc ? ? E HIS 46  ND1 ? ? ? 1_555 O CU  .   CU ? ? E HIS 46  E CU  154 1_555 ? ? ? ? ? ? ? 2.403 ? 
metalc38 metalc ? ? A HIS 48  NE2 ? ? ? 1_555 G CU  .   CU ? ? A HIS 48  A CU  154 1_555 ? ? ? ? ? ? ? 2.423 ? 
metalc39 metalc ? ? B HIS 48  NE2 ? ? ? 1_555 I CU  .   CU ? ? B HIS 48  B CU  154 1_555 ? ? ? ? ? ? ? 2.426 ? 
metalc40 metalc ? ? F HIS 48  NE2 ? ? ? 1_555 Q CU  .   CU ? ? F HIS 48  F CU  154 1_555 ? ? ? ? ? ? ? 2.483 ? 
metalc41 metalc ? ? D HIS 48  NE2 ? ? ? 1_555 M CU  .   CU ? ? D HIS 48  D CU  154 1_555 ? ? ? ? ? ? ? 2.560 ? 
metalc42 metalc ? ? B HIS 46  ND1 ? ? ? 1_555 I CU  .   CU ? ? B HIS 46  B CU  154 1_555 ? ? ? ? ? ? ? 2.617 ? 
metalc43 metalc ? ? C HIS 63  NE2 ? ? ? 1_555 K CU  .   CU ? ? C HIS 63  C CU  154 1_555 ? ? ? ? ? ? ? 2.642 ? 
metalc44 metalc ? ? D HIS 63  NE2 ? ? ? 1_555 M CU  .   CU ? ? D HIS 63  D CU  154 1_555 ? ? ? ? ? ? ? 2.654 ? 
metalc45 metalc ? ? E HIS 63  NE2 ? ? ? 1_555 O CU  .   CU ? ? E HIS 63  E CU  154 1_555 ? ? ? ? ? ? ? 2.659 ? 
metalc46 metalc ? ? B HIS 63  NE2 ? ? ? 1_555 I CU  .   CU ? ? B HIS 63  B CU  154 1_555 ? ? ? ? ? ? ? 2.679 ? 
# 
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 VAL A 94  ? ASP A 101 ? VAL A 94  ASP A 101 
A 2 VAL A 29  ? LYS A 36  ? VAL A 29  LYS A 36  
A 3 GLN A 15  ? GLU A 21  ? GLN A 15  GLU A 21  
A 4 LYS A 3   ? LEU A 8   ? LYS A 3   LEU A 8   
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  ? VAL A 47  ? GLY A 41  VAL A 47  
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  ? LYS B 36  ? VAL B 29  LYS B 36  
C 3 GLN B 15  ? GLU B 21  ? GLN B 15  GLU B 21  
C 4 LYS B 3   ? LEU B 8   ? LYS B 3   LEU B 8   
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  ? VAL B 47  ? GLY B 41  VAL B 47  
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 ALA C 95  ? ASP C 101 ? ALA C 95  ASP C 101 
E 2 VAL C 29  ? LYS C 36  ? VAL C 29  LYS C 36  
E 3 GLN C 15  ? GLU C 21  ? GLN C 15  GLU C 21  
E 4 LYS C 3   ? LEU C 8   ? LYS C 3   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  ? VAL C 47  ? GLY C 41  VAL C 47  
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  ? LYS D 36  ? VAL D 29  LYS D 36  
G 3 GLN D 15  ? GLU D 21  ? GLN D 15  GLU D 21  
G 4 LYS D 3   ? LEU D 8   ? LYS D 3   LEU D 8   
G 5 GLY D 150 ? ILE D 151 ? GLY D 150 ILE D 151 
H 1 ASP D 83  ? ALA D 89  ? ASP D 83  ALA D 89  
H 2 GLY D 41  ? VAL D 47  ? GLY D 41  VAL D 47  
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  ? LYS E 36  ? VAL E 29  LYS E 36  
I 3 GLN E 15  ? GLU E 21  ? GLN E 15  GLU E 21  
I 4 LYS E 3   ? LEU E 8   ? LYS E 3   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  ? VAL E 47  ? GLY E 41  VAL E 47  
J 3 THR E 116 ? VAL E 119 ? THR E 116 VAL E 119 
J 4 ALA E 145 ? VAL E 148 ? ALA E 145 VAL E 148 
K 1 ALA F 95  ? ASP F 101 ? ALA F 95  ASP F 101 
K 2 VAL F 29  ? LYS F 36  ? VAL F 29  LYS F 36  
K 3 GLN F 15  ? GLU F 21  ? GLN F 15  GLU F 21  
K 4 LYS F 3   ? LEU F 8   ? LYS F 3   LEU F 8   
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  ? VAL F 47  ? GLY F 41  VAL F 47  
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 VAL A 31  ? N VAL A 31  
A 2 3 O TRP A 32  ? O TRP A 32  N ASN A 19  ? N ASN A 19  
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 46  ? N HIS A 46  O VAL A 118 ? O VAL A 118 
B 3 4 N LEU A 117 ? N LEU A 117 O GLY A 147 ? O GLY A 147 
C 1 2 O ILE B 99  ? O ILE B 99  N VAL B 31  ? N VAL B 31  
C 2 3 O TRP B 32  ? O TRP B 32  N ASN B 19  ? N ASN B 19  
C 3 4 O PHE B 20  ? O PHE B 20  N ALA B 4   ? N ALA B 4   
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 46  ? N HIS B 46  O VAL B 118 ? O VAL B 118 
D 3 4 N LEU B 117 ? N LEU B 117 O GLY B 147 ? O GLY B 147 
E 1 2 O ALA C 95  ? O ALA C 95  N ILE C 35  ? N ILE C 35  
E 2 3 O TRP C 32  ? O TRP C 32  N ASN C 19  ? N ASN C 19  
E 3 4 O PHE C 20  ? O PHE C 20  N ALA C 4   ? N ALA C 4   
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 TRP D 32  ? O TRP D 32  N ASN D 19  ? N ASN D 19  
G 3 4 O PHE D 20  ? O PHE D 20  N ALA D 4   ? N ALA D 4   
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 46  ? N HIS D 46  O VAL D 118 ? O VAL D 118 
H 3 4 N LEU D 117 ? N LEU D 117 O GLY D 147 ? O GLY D 147 
I 1 2 O ILE E 99  ? O ILE E 99  N VAL E 31  ? N VAL E 31  
I 2 3 O TRP E 32  ? O TRP E 32  N ASN E 19  ? N ASN E 19  
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 ALA F 95  ? O ALA F 95  N ILE F 35  ? N ILE F 35  
K 2 3 O TRP F 32  ? O TRP F 32  N ASN F 19  ? N ASN 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 46  ? N HIS F 46  O VAL F 118 ? O VAL F 118 
L 3 4 N LEU F 117 ? N LEU F 117 O GLY F 147 ? O GLY F 147 
# 
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 CU A 154' 
AC2 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE ZN A 155' 
AC3 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU B 154' 
AC4 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE ZN B 155' 
AC5 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU C 154' 
AC6 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE ZN C 155' 
AC7 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU D 154' 
AC8 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE ZN D 155' 
AC9 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU E 154' 
BC1 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE ZN E 155' 
BC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU F 154' 
BC3 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE ZN F 155' 
# 
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 46  ? HIS A 46  . ? 1_555 ? 
2  AC1 4 HIS A 48  ? HIS A 48  . ? 1_555 ? 
3  AC1 4 HIS A 63  ? HIS A 63  . ? 1_555 ? 
4  AC1 4 HIS A 120 ? HIS A 120 . ? 1_555 ? 
5  AC2 5 HIS A 63  ? HIS A 63  . ? 1_555 ? 
6  AC2 5 HIS A 71  ? HIS A 71  . ? 1_555 ? 
7  AC2 5 HIS A 80  ? HIS A 80  . ? 1_555 ? 
8  AC2 5 ASP A 83  ? ASP A 83  . ? 1_555 ? 
9  AC2 5 LYS A 136 ? LYS A 136 . ? 1_555 ? 
10 AC3 4 HIS B 46  ? HIS B 46  . ? 1_555 ? 
11 AC3 4 HIS B 48  ? HIS B 48  . ? 1_555 ? 
12 AC3 4 HIS B 63  ? HIS B 63  . ? 1_555 ? 
13 AC3 4 HIS B 120 ? HIS B 120 . ? 1_555 ? 
14 AC4 5 HIS B 63  ? HIS B 63  . ? 1_555 ? 
15 AC4 5 HIS B 71  ? HIS B 71  . ? 1_555 ? 
16 AC4 5 HIS B 80  ? HIS B 80  . ? 1_555 ? 
17 AC4 5 ASP B 83  ? ASP B 83  . ? 1_555 ? 
18 AC4 5 LYS B 136 ? LYS B 136 . ? 1_555 ? 
19 AC5 4 HIS C 46  ? HIS C 46  . ? 1_555 ? 
20 AC5 4 HIS C 48  ? HIS C 48  . ? 1_555 ? 
21 AC5 4 HIS C 63  ? HIS C 63  . ? 1_555 ? 
22 AC5 4 HIS C 120 ? HIS C 120 . ? 1_555 ? 
23 AC6 5 HIS C 63  ? HIS C 63  . ? 1_555 ? 
24 AC6 5 HIS C 71  ? HIS C 71  . ? 1_555 ? 
25 AC6 5 HIS C 80  ? HIS C 80  . ? 1_555 ? 
26 AC6 5 ASP C 83  ? ASP C 83  . ? 1_555 ? 
27 AC6 5 LYS C 136 ? LYS C 136 . ? 1_555 ? 
28 AC7 4 HIS D 46  ? HIS D 46  . ? 1_555 ? 
29 AC7 4 HIS D 48  ? HIS D 48  . ? 1_555 ? 
30 AC7 4 HIS D 63  ? HIS D 63  . ? 1_555 ? 
31 AC7 4 HIS D 120 ? HIS D 120 . ? 1_555 ? 
32 AC8 5 HIS D 63  ? HIS D 63  . ? 1_555 ? 
33 AC8 5 HIS D 71  ? HIS D 71  . ? 1_555 ? 
34 AC8 5 HIS D 80  ? HIS D 80  . ? 1_555 ? 
35 AC8 5 ASP D 83  ? ASP D 83  . ? 1_555 ? 
36 AC8 5 LYS D 136 ? LYS D 136 . ? 1_555 ? 
37 AC9 4 HIS E 46  ? HIS E 46  . ? 1_555 ? 
38 AC9 4 HIS E 48  ? HIS E 48  . ? 1_555 ? 
39 AC9 4 HIS E 63  ? HIS E 63  . ? 1_555 ? 
40 AC9 4 HIS E 120 ? HIS E 120 . ? 1_555 ? 
41 BC1 5 HIS E 63  ? HIS E 63  . ? 1_555 ? 
42 BC1 5 HIS E 71  ? HIS E 71  . ? 1_555 ? 
43 BC1 5 HIS E 80  ? HIS E 80  . ? 1_555 ? 
44 BC1 5 ASP E 83  ? ASP E 83  . ? 1_555 ? 
45 BC1 5 LYS E 136 ? LYS E 136 . ? 1_555 ? 
46 BC2 4 HIS F 46  ? HIS F 46  . ? 1_555 ? 
47 BC2 4 HIS F 48  ? HIS F 48  . ? 1_555 ? 
48 BC2 4 HIS F 63  ? HIS F 63  . ? 1_555 ? 
49 BC2 4 HIS F 120 ? HIS F 120 . ? 1_555 ? 
50 BC3 5 HIS F 63  ? HIS F 63  . ? 1_555 ? 
51 BC3 5 HIS F 71  ? HIS F 71  . ? 1_555 ? 
52 BC3 5 HIS F 80  ? HIS F 80  . ? 1_555 ? 
53 BC3 5 ASP F 83  ? ASP F 83  . ? 1_555 ? 
54 BC3 5 LYS F 136 ? LYS F 136 . ? 1_555 ? 
# 
_atom_sites.entry_id                    3KH4 
_atom_sites.fract_transf_matrix[1][1]   0.008914 
_atom_sites.fract_transf_matrix[1][2]   0.005146 
_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]   0.010293 
_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]   0.002335 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
CU 
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   ? -7.232  -21.756 3.416  1.00 98.00  ? 1   ALA A N   1 
ATOM   2    C  CA  . ALA A 1 1   ? -6.849  -22.417 4.695  1.00 94.65  ? 1   ALA A CA  1 
ATOM   3    C  C   . ALA A 1 1   ? -6.018  -23.738 4.485  1.00 94.54  ? 1   ALA A C   1 
ATOM   4    O  O   . ALA A 1 1   ? -6.603  -24.802 4.224  1.00 93.96  ? 1   ALA A O   1 
ATOM   5    C  CB  . ALA A 1 1   ? -8.115  -22.666 5.501  1.00 91.50  ? 1   ALA A CB  1 
ATOM   6    N  N   . THR A 1 2   ? -4.670  -23.637 4.556  1.00 95.25  ? 2   THR A N   1 
ATOM   7    C  CA  . THR A 1 2   ? -3.740  -24.797 4.574  1.00 94.80  ? 2   THR A CA  1 
ATOM   8    C  C   . THR A 1 2   ? -3.704  -25.392 5.960  1.00 90.68  ? 2   THR A C   1 
ATOM   9    O  O   . THR A 1 2   ? -3.695  -26.598 6.082  1.00 89.92  ? 2   THR A O   1 
ATOM   10   C  CB  . THR A 1 2   ? -2.238  -24.446 4.180  1.00 98.45  ? 2   THR A CB  1 
ATOM   11   O  OG1 . THR A 1 2   ? -2.139  -24.165 2.770  1.00 103.06 ? 2   THR A OG1 1 
ATOM   12   C  CG2 . THR A 1 2   ? -1.241  -25.611 4.527  1.00 98.22  ? 2   THR A CG2 1 
ATOM   13   N  N   . LYS A 1 3   ? -3.658  -24.557 6.996  1.00 88.42  ? 3   LYS A N   1 
ATOM   14   C  CA  . LYS A 1 3   ? -3.522  -25.041 8.368  1.00 85.31  ? 3   LYS A CA  1 
ATOM   15   C  C   . LYS A 1 3   ? -4.645  -24.582 9.255  1.00 81.83  ? 3   LYS A C   1 
ATOM   16   O  O   . LYS A 1 3   ? -5.278  -23.574 8.974  1.00 82.27  ? 3   LYS A O   1 
ATOM   17   C  CB  . LYS A 1 3   ? -2.211  -24.560 8.978  1.00 86.93  ? 3   LYS A CB  1 
ATOM   18   C  CG  . LYS A 1 3   ? -0.992  -25.238 8.407  1.00 90.80  ? 3   LYS A CG  1 
ATOM   19   C  CD  . LYS A 1 3   ? 0.260   -24.837 9.175  1.00 94.23  ? 3   LYS A CD  1 
ATOM   20   C  CE  . LYS A 1 3   ? 1.495   -24.894 8.284  1.00 99.47  ? 3   LYS A CE  1 
ATOM   21   N  NZ  . LYS A 1 3   ? 2.572   -23.975 8.783  1.00 102.65 ? 3   LYS A NZ  1 
ATOM   22   N  N   . ALA A 1 4   ? -4.853  -25.335 10.338 1.00 78.48  ? 4   ALA A N   1 
ATOM   23   C  CA  . ALA A 1 4   ? -5.767  -24.968 11.425 1.00 75.64  ? 4   ALA A CA  1 
ATOM   24   C  C   . ALA A 1 4   ? -5.293  -25.496 12.782 1.00 73.65  ? 4   ALA A C   1 
ATOM   25   O  O   . ALA A 1 4   ? -4.314  -26.221 12.880 1.00 73.98  ? 4   ALA A O   1 
ATOM   26   C  CB  . ALA A 1 4   ? -7.152  -25.452 11.131 1.00 74.09  ? 4   ALA A CB  1 
ATOM   27   N  N   . VAL A 1 5   ? -5.990  -25.082 13.828 1.00 71.92  ? 5   VAL A N   1 
ATOM   28   C  CA  . VAL A 1 5   ? -5.655  -25.444 15.203 1.00 70.84  ? 5   VAL A CA  1 
ATOM   29   C  C   . VAL A 1 5   ? -6.897  -25.386 16.098 1.00 69.64  ? 5   VAL A C   1 
ATOM   30   O  O   . VAL A 1 5   ? -7.901  -24.753 15.756 1.00 69.48  ? 5   VAL A O   1 
ATOM   31   C  CB  . VAL A 1 5   ? -4.598  -24.511 15.788 1.00 72.33  ? 5   VAL A CB  1 
ATOM   32   C  CG1 . VAL A 1 5   ? -5.199  -23.165 16.107 1.00 72.64  ? 5   VAL A CG1 1 
ATOM   33   C  CG2 . VAL A 1 5   ? -4.021  -25.098 17.026 1.00 71.17  ? 5   VAL A CG2 1 
ATOM   34   N  N   . CYS A 1 6   ? -6.833  -26.056 17.240 1.00 69.18  ? 6   CYS A N   1 
ATOM   35   C  CA  . CYS A 1 6   ? -7.962  -26.079 18.158 1.00 68.72  ? 6   CYS A CA  1 
ATOM   36   C  C   . CYS A 1 6   ? -7.518  -26.354 19.572 1.00 69.07  ? 6   CYS A C   1 
ATOM   37   O  O   . CYS A 1 6   ? -6.854  -27.329 19.811 1.00 68.92  ? 6   CYS A O   1 
ATOM   38   C  CB  . CYS A 1 6   ? -8.942  -27.170 17.742 1.00 67.29  ? 6   CYS A CB  1 
ATOM   39   S  SG  . CYS A 1 6   ? -10.206 -27.512 18.963 1.00 66.78  ? 6   CYS A SG  1 
ATOM   40   N  N   . VAL A 1 7   ? -7.891  -25.502 20.512 1.00 70.12  ? 7   VAL A N   1 
ATOM   41   C  CA  . VAL A 1 7   ? -7.595  -25.762 21.909 1.00 71.21  ? 7   VAL A CA  1 
ATOM   42   C  C   . VAL A 1 7   ? -8.763  -26.392 22.653 1.00 71.11  ? 7   VAL A C   1 
ATOM   43   O  O   . VAL A 1 7   ? -9.827  -25.792 22.828 1.00 71.52  ? 7   VAL A O   1 
ATOM   44   C  CB  . VAL A 1 7   ? -7.262  -24.504 22.648 1.00 73.29  ? 7   VAL A CB  1 
ATOM   45   C  CG1 . VAL A 1 7   ? -6.866  -24.829 24.054 1.00 74.51  ? 7   VAL A CG1 1 
ATOM   46   C  CG2 . VAL A 1 7   ? -6.163  -23.791 21.959 1.00 74.60  ? 7   VAL A CG2 1 
ATOM   47   N  N   . LEU A 1 8   ? -8.535  -27.602 23.128 1.00 71.16  ? 8   LEU A N   1 
ATOM   48   C  CA  . LEU A 1 8   ? -9.554  -28.358 23.801 1.00 71.20  ? 8   LEU A CA  1 
ATOM   49   C  C   . LEU A 1 8   ? -9.543  -28.000 25.253 1.00 74.24  ? 8   LEU A C   1 
ATOM   50   O  O   . LEU A 1 8   ? -8.501  -28.016 25.870 1.00 75.46  ? 8   LEU A O   1 
ATOM   51   C  CB  . LEU A 1 8   ? -9.269  -29.842 23.635 1.00 69.98  ? 8   LEU A CB  1 
ATOM   52   C  CG  . LEU A 1 8   ? -9.477  -30.324 22.206 1.00 67.56  ? 8   LEU A CG  1 
ATOM   53   C  CD1 . LEU A 1 8   ? -8.939  -31.674 22.016 1.00 65.25  ? 8   LEU A CD1 1 
ATOM   54   C  CD2 . LEU A 1 8   ? -10.953 -30.310 21.875 1.00 67.78  ? 8   LEU A CD2 1 
ATOM   55   N  N   . LYS A 1 9   ? -10.705 -27.670 25.794 1.00 76.46  ? 9   LYS A N   1 
ATOM   56   C  CA  . LYS A 1 9   ? -10.861 -27.375 27.211 1.00 80.54  ? 9   LYS A CA  1 
ATOM   57   C  C   . LYS A 1 9   ? -12.194 -27.918 27.633 1.00 81.10  ? 9   LYS A C   1 
ATOM   58   O  O   . LYS A 1 9   ? -13.058 -28.179 26.797 1.00 79.63  ? 9   LYS A O   1 
ATOM   59   C  CB  . LYS A 1 9   ? -10.905 -25.877 27.464 1.00 83.23  ? 9   LYS A CB  1 
ATOM   60   C  CG  . LYS A 1 9   ? -9.613  -25.109 27.195 1.00 87.30  ? 9   LYS A CG  1 
ATOM   61   C  CD  . LYS A 1 9   ? -8.677  -24.994 28.404 1.00 93.70  ? 9   LYS A CD  1 
ATOM   62   C  CE  . LYS A 1 9   ? -7.717  -23.789 28.253 1.00 96.80  ? 9   LYS A CE  1 
ATOM   63   N  NZ  . LYS A 1 9   ? -6.604  -23.809 29.235 1.00 100.86 ? 9   LYS A NZ  1 
ATOM   64   N  N   . GLY A 1 10  ? -12.382 -28.035 28.937 1.00 84.10  ? 10  GLY A N   1 
ATOM   65   C  CA  . GLY A 1 10  ? -13.650 -28.472 29.471 1.00 85.36  ? 10  GLY A CA  1 
ATOM   66   C  C   . GLY A 1 10  ? -13.706 -28.217 30.955 1.00 89.50  ? 10  GLY A C   1 
ATOM   67   O  O   . GLY A 1 10  ? -12.778 -27.661 31.536 1.00 91.29  ? 10  GLY A O   1 
ATOM   68   N  N   . ASP A 1 11  ? -14.808 -28.640 31.567 1.00 91.67  ? 11  ASP A N   1 
ATOM   69   C  CA  . ASP A 1 11  ? -14.963 -28.630 33.024 1.00 96.05  ? 11  ASP A CA  1 
ATOM   70   C  C   . ASP A 1 11  ? -13.962 -29.544 33.707 1.00 96.40  ? 11  ASP A C   1 
ATOM   71   O  O   . ASP A 1 11  ? -13.501 -29.246 34.796 1.00 99.54  ? 11  ASP A O   1 
ATOM   72   C  CB  . ASP A 1 11  ? -16.385 -29.067 33.392 1.00 97.99  ? 11  ASP A CB  1 
ATOM   73   C  CG  . ASP A 1 11  ? -17.418 -27.995 33.088 1.00 101.18 ? 11  ASP A CG  1 
ATOM   74   O  OD1 . ASP A 1 11  ? -17.048 -26.791 33.102 1.00 105.08 ? 11  ASP A OD1 1 
ATOM   75   O  OD2 . ASP A 1 11  ? -18.589 -28.360 32.834 1.00 104.10 ? 11  ASP A OD2 1 
ATOM   76   N  N   . GLY A 1 12  ? -13.640 -30.658 33.051 1.00 93.43  ? 12  GLY A N   1 
ATOM   77   C  CA  . GLY A 1 12  ? -12.712 -31.638 33.574 1.00 93.49  ? 12  GLY A CA  1 
ATOM   78   C  C   . GLY A 1 12  ? -11.307 -31.092 33.705 1.00 93.67  ? 12  GLY A C   1 
ATOM   79   O  O   . GLY A 1 12  ? -11.079 -29.922 33.518 1.00 93.94  ? 12  GLY A O   1 
ATOM   80   N  N   . PRO A 1 13  ? -10.354 -31.956 34.040 1.00 93.61  ? 13  PRO A N   1 
ATOM   81   C  CA  . PRO A 1 13  ? -8.950  -31.645 33.976 1.00 93.59  ? 13  PRO A CA  1 
ATOM   82   C  C   . PRO A 1 13  ? -8.428  -31.898 32.571 1.00 89.31  ? 13  PRO A C   1 
ATOM   83   O  O   . PRO A 1 13  ? -7.253  -31.703 32.327 1.00 89.30  ? 13  PRO A O   1 
ATOM   84   C  CB  . PRO A 1 13  ? -8.346  -32.667 34.929 1.00 96.22  ? 13  PRO A CB  1 
ATOM   85   C  CG  . PRO A 1 13  ? -9.179  -33.902 34.703 1.00 94.81  ? 13  PRO A CG  1 
ATOM   86   C  CD  . PRO A 1 13  ? -10.573 -33.388 34.336 1.00 93.86  ? 13  PRO A CD  1 
ATOM   87   N  N   . VAL A 1 14  ? -9.300  -32.355 31.668 1.00 85.91  ? 14  VAL A N   1 
ATOM   88   C  CA  . VAL A 1 14  ? -8.918  -32.756 30.324 1.00 82.20  ? 14  VAL A CA  1 
ATOM   89   C  C   . VAL A 1 14  ? -8.636  -31.509 29.551 1.00 81.11  ? 14  VAL A C   1 
ATOM   90   O  O   . VAL A 1 14  ? -9.362  -30.514 29.671 1.00 81.65  ? 14  VAL A O   1 
ATOM   91   C  CB  . VAL A 1 14  ? -10.041 -33.478 29.574 1.00 79.77  ? 14  VAL A CB  1 
ATOM   92   C  CG1 . VAL A 1 14  ? -9.457  -34.214 28.388 1.00 76.24  ? 14  VAL A CG1 1 
ATOM   93   C  CG2 . VAL A 1 14  ? -10.801 -34.446 30.495 1.00 81.91  ? 14  VAL A CG2 1 
ATOM   94   N  N   . GLN A 1 15  ? -7.585  -31.566 28.750 1.00 79.83  ? 15  GLN A N   1 
ATOM   95   C  CA  . GLN A 1 15  ? -7.218  -30.446 27.918 1.00 79.11  ? 15  GLN A CA  1 
ATOM   96   C  C   . GLN A 1 15  ? -6.081  -30.804 26.989 1.00 77.62  ? 15  GLN A C   1 
ATOM   97   O  O   . GLN A 1 15  ? -5.291  -31.688 27.301 1.00 78.57  ? 15  GLN A O   1 
ATOM   98   C  CB  . GLN A 1 15  ? -6.817  -29.249 28.777 1.00 82.24  ? 15  GLN A CB  1 
ATOM   99   C  CG  . GLN A 1 15  ? -5.453  -29.373 29.422 1.00 85.90  ? 15  GLN A CG  1 
ATOM   100  C  CD  . GLN A 1 15  ? -5.133  -28.215 30.342 1.00 91.18  ? 15  GLN A CD  1 
ATOM   101  O  OE1 . GLN A 1 15  ? -4.100  -28.236 31.010 1.00 95.41  ? 15  GLN A OE1 1 
ATOM   102  N  NE2 . GLN A 1 15  ? -6.006  -27.194 30.381 1.00 91.37  ? 15  GLN A NE2 1 
ATOM   103  N  N   . GLY A 1 16  ? -6.000  -30.098 25.862 1.00 75.62  ? 16  GLY A N   1 
ATOM   104  C  CA  . GLY A 1 16  ? -4.920  -30.284 24.899 1.00 74.85  ? 16  GLY A CA  1 
ATOM   105  C  C   . GLY A 1 16  ? -4.990  -29.328 23.732 1.00 73.44  ? 16  GLY A C   1 
ATOM   106  O  O   . GLY A 1 16  ? -5.892  -28.499 23.671 1.00 73.16  ? 16  GLY A O   1 
ATOM   107  N  N   . ILE A 1 17  ? -4.048  -29.471 22.800 1.00 72.92  ? 17  ILE A N   1 
ATOM   108  C  CA  . ILE A 1 17  ? -3.965  -28.655 21.589 1.00 72.10  ? 17  ILE A CA  1 
ATOM   109  C  C   . ILE A 1 17  ? -3.853  -29.571 20.399 1.00 70.66  ? 17  ILE A C   1 
ATOM   110  O  O   . ILE A 1 17  ? -3.061  -30.459 20.407 1.00 71.15  ? 17  ILE A O   1 
ATOM   111  C  CB  . ILE A 1 17  ? -2.681  -27.844 21.583 1.00 74.51  ? 17  ILE A CB  1 
ATOM   112  C  CG1 . ILE A 1 17  ? -2.401  -27.209 22.952 1.00 76.78  ? 17  ILE A CG1 1 
ATOM   113  C  CG2 . ILE A 1 17  ? -2.719  -26.812 20.510 1.00 74.67  ? 17  ILE A CG2 1 
ATOM   114  C  CD1 . ILE A 1 17  ? -2.383  -25.739 22.955 1.00 78.67  ? 17  ILE A CD1 1 
ATOM   115  N  N   . ILE A 1 18  ? -4.620  -29.348 19.360 1.00 69.55  ? 18  ILE A N   1 
ATOM   116  C  CA  . ILE A 1 18  ? -4.581  -30.227 18.206 1.00 69.44  ? 18  ILE A CA  1 
ATOM   117  C  C   . ILE A 1 18  ? -4.455  -29.412 16.953 1.00 70.50  ? 18  ILE A C   1 
ATOM   118  O  O   . ILE A 1 18  ? -5.196  -28.465 16.780 1.00 70.32  ? 18  ILE A O   1 
ATOM   119  C  CB  . ILE A 1 18  ? -5.877  -31.001 18.039 1.00 67.73  ? 18  ILE A CB  1 
ATOM   120  C  CG1 . ILE A 1 18  ? -6.113  -31.934 19.217 1.00 67.72  ? 18  ILE A CG1 1 
ATOM   121  C  CG2 . ILE A 1 18  ? -5.859  -31.780 16.750 1.00 67.20  ? 18  ILE A CG2 1 
ATOM   122  C  CD1 . ILE A 1 18  ? -5.017  -32.868 19.462 1.00 70.21  ? 18  ILE A CD1 1 
ATOM   123  N  N   . ASN A 1 19  ? -3.543  -29.807 16.071 1.00 72.42  ? 19  ASN A N   1 
ATOM   124  C  CA  . ASN A 1 19  ? -3.279  -29.088 14.839 1.00 74.18  ? 19  ASN A CA  1 
ATOM   125  C  C   . ASN A 1 19  ? -3.792  -29.814 13.628 1.00 74.48  ? 19  ASN A C   1 
ATOM   126  O  O   . ASN A 1 19  ? -4.004  -31.003 13.655 1.00 73.87  ? 19  ASN A O   1 
ATOM   127  C  CB  . ASN A 1 19  ? -1.791  -28.894 14.685 1.00 76.76  ? 19  ASN A CB  1 
ATOM   128  C  CG  . ASN A 1 19  ? -1.218  -28.094 15.798 1.00 78.15  ? 19  ASN A CG  1 
ATOM   129  O  OD1 . ASN A 1 19  ? -0.663  -28.638 16.750 1.00 79.26  ? 19  ASN A OD1 1 
ATOM   130  N  ND2 . ASN A 1 19  ? -1.387  -26.780 15.717 1.00 79.20  ? 19  ASN A ND2 1 
ATOM   131  N  N   . PHE A 1 20  ? -3.979  -29.076 12.549 1.00 76.45  ? 20  PHE A N   1 
ATOM   132  C  CA  . PHE A 1 20  ? -4.446  -29.635 11.290 1.00 77.85  ? 20  PHE A CA  1 
ATOM   133  C  C   . PHE A 1 20  ? -3.617  -29.073 10.147 1.00 81.57  ? 20  PHE A C   1 
ATOM   134  O  O   . PHE A 1 20  ? -3.213  -27.920 10.180 1.00 83.00  ? 20  PHE A O   1 
ATOM   135  C  CB  . PHE A 1 20  ? -5.887  -29.226 11.035 1.00 76.59  ? 20  PHE A CB  1 
ATOM   136  C  CG  . PHE A 1 20  ? -6.868  -29.699 12.085 1.00 74.60  ? 20  PHE A CG  1 
ATOM   137  C  CD1 . PHE A 1 20  ? -6.871  -29.160 13.364 1.00 74.84  ? 20  PHE A CD1 1 
ATOM   138  C  CD2 . PHE A 1 20  ? -7.834  -30.639 11.776 1.00 73.18  ? 20  PHE A CD2 1 
ATOM   139  C  CE1 . PHE A 1 20  ? -7.798  -29.585 14.314 1.00 72.87  ? 20  PHE A CE1 1 
ATOM   140  C  CE2 . PHE A 1 20  ? -8.753  -31.057 12.718 1.00 70.40  ? 20  PHE A CE2 1 
ATOM   141  C  CZ  . PHE A 1 20  ? -8.731  -30.532 13.980 1.00 70.40  ? 20  PHE A CZ  1 
ATOM   142  N  N   . GLU A 1 21  ? -3.397  -29.871 9.120  1.00 84.16  ? 21  GLU A N   1 
ATOM   143  C  CA  . GLU A 1 21  ? -2.675  -29.403 7.967  1.00 88.29  ? 21  GLU A CA  1 
ATOM   144  C  C   . GLU A 1 21  ? -3.192  -30.097 6.737  1.00 89.90  ? 21  GLU A C   1 
ATOM   145  O  O   . GLU A 1 21  ? -3.200  -31.302 6.673  1.00 90.31  ? 21  GLU A O   1 
ATOM   146  C  CB  . GLU A 1 21  ? -1.187  -29.664 8.137  1.00 90.98  ? 21  GLU A CB  1 
ATOM   147  C  CG  . GLU A 1 21  ? -0.330  -28.941 7.105  1.00 97.14  ? 21  GLU A CG  1 
ATOM   148  C  CD  . GLU A 1 21  ? 1.171   -29.166 7.291  1.00 103.18 ? 21  GLU A CD  1 
ATOM   149  O  OE1 . GLU A 1 21  ? 1.572   -30.311 7.636  1.00 105.24 ? 21  GLU A OE1 1 
ATOM   150  O  OE2 . GLU A 1 21  ? 1.948   -28.190 7.069  1.00 107.20 ? 21  GLU A OE2 1 
ATOM   151  N  N   . GLN A 1 22  ? -3.627  -29.326 5.755  1.00 91.93  ? 22  GLN A N   1 
ATOM   152  C  CA  . GLN A 1 22  ? -4.096  -29.856 4.480  1.00 94.51  ? 22  GLN A CA  1 
ATOM   153  C  C   . GLN A 1 22  ? -3.231  -29.225 3.382  1.00 99.74  ? 22  GLN A C   1 
ATOM   154  O  O   . GLN A 1 22  ? -3.540  -28.127 2.872  1.00 100.90 ? 22  GLN A O   1 
ATOM   155  C  CB  . GLN A 1 22  ? -5.584  -29.554 4.276  1.00 92.73  ? 22  GLN A CB  1 
ATOM   156  C  CG  . GLN A 1 22  ? -6.157  -30.145 3.005  1.00 94.91  ? 22  GLN A CG  1 
ATOM   157  C  CD  . GLN A 1 22  ? -7.667  -30.063 2.906  1.00 93.24  ? 22  GLN A CD  1 
ATOM   158  O  OE1 . GLN A 1 22  ? -8.272  -29.038 3.215  1.00 91.35  ? 22  GLN A OE1 1 
ATOM   159  N  NE2 . GLN A 1 22  ? -8.280  -31.139 2.428  1.00 94.05  ? 22  GLN A NE2 1 
ATOM   160  N  N   . LYS A 1 23  ? -2.128  -29.910 3.050  1.00 103.53 ? 23  LYS A N   1 
ATOM   161  C  CA  . LYS A 1 23  ? -1.181  -29.396 2.054  1.00 109.03 ? 23  LYS A CA  1 
ATOM   162  C  C   . LYS A 1 23  ? -1.876  -29.232 0.703  1.00 111.95 ? 23  LYS A C   1 
ATOM   163  O  O   . LYS A 1 23  ? -1.684  -28.238 0.021  1.00 114.66 ? 23  LYS A O   1 
ATOM   164  C  CB  . LYS A 1 23  ? 0.102   -30.257 1.956  1.00 112.13 ? 23  LYS A CB  1 
ATOM   165  C  CG  . LYS A 1 23  ? 1.239   -29.778 2.924  1.00 113.65 ? 23  LYS A CG  1 
ATOM   166  C  CD  . LYS A 1 23  ? 2.242   -30.893 3.252  1.00 117.23 ? 23  LYS A CD  1 
ATOM   167  C  CE  . LYS A 1 23  ? 1.604   -31.947 4.202  1.00 115.05 ? 23  LYS A CE  1 
ATOM   168  N  NZ  . LYS A 1 23  ? 2.460   -33.143 4.399  1.00 117.96 ? 23  LYS A NZ  1 
ATOM   169  N  N   . GLU A 1 24  ? -2.722  -30.175 0.338  1.00 111.96 ? 24  GLU A N   1 
ATOM   170  C  CA  . GLU A 1 24  ? -3.392  -30.082 -0.936 1.00 115.60 ? 24  GLU A CA  1 
ATOM   171  C  C   . GLU A 1 24  ? -4.842  -29.781 -0.770 1.00 113.12 ? 24  GLU A C   1 
ATOM   172  O  O   . GLU A 1 24  ? -5.515  -30.458 -0.036 1.00 110.04 ? 24  GLU A O   1 
ATOM   173  C  CB  . GLU A 1 24  ? -3.282  -31.400 -1.690 1.00 118.88 ? 24  GLU A CB  1 
ATOM   174  C  CG  . GLU A 1 24  ? -1.938  -31.617 -2.352 1.00 124.73 ? 24  GLU A CG  1 
ATOM   175  C  CD  . GLU A 1 24  ? -1.945  -32.835 -3.254 1.00 129.60 ? 24  GLU A CD  1 
ATOM   176  O  OE1 . GLU A 1 24  ? -2.737  -33.764 -2.962 1.00 127.90 ? 24  GLU A OE1 1 
ATOM   177  O  OE2 . GLU A 1 24  ? -1.176  -32.844 -4.257 1.00 135.42 ? 24  GLU A OE2 1 
ATOM   178  N  N   . SER A 1 25  ? -5.338  -28.797 -1.502 1.00 115.44 ? 25  SER A N   1 
ATOM   179  C  CA  . SER A 1 25  ? -6.778  -28.570 -1.597 1.00 114.46 ? 25  SER A CA  1 
ATOM   180  C  C   . SER A 1 25  ? -7.509  -29.868 -1.895 1.00 114.54 ? 25  SER A C   1 
ATOM   181  O  O   . SER A 1 25  ? -7.150  -30.611 -2.808 1.00 118.24 ? 25  SER A O   1 
ATOM   182  C  CB  . SER A 1 25  ? -7.103  -27.582 -2.704 1.00 118.59 ? 25  SER A CB  1 
ATOM   183  O  OG  . SER A 1 25  ? -8.509  -27.513 -2.907 1.00 118.99 ? 25  SER A OG  1 
ATOM   184  N  N   . ASN A 1 26  ? -8.537  -30.141 -1.111 1.00 110.92 ? 26  ASN A N   1 
ATOM   185  C  CA  . ASN A 1 26  ? -9.315  -31.394 -1.221 1.00 110.88 ? 26  ASN A CA  1 
ATOM   186  C  C   . ASN A 1 26  ? -8.513  -32.687 -1.078 1.00 110.35 ? 26  ASN A C   1 
ATOM   187  O  O   . ASN A 1 26  ? -9.014  -33.760 -1.390 1.00 111.41 ? 26  ASN A O   1 
ATOM   188  C  CB  . ASN A 1 26  ? -10.103 -31.445 -2.540 1.00 115.53 ? 26  ASN A CB  1 
ATOM   189  C  CG  . ASN A 1 26  ? -11.293 -30.498 -2.556 1.00 116.13 ? 26  ASN A CG  1 
ATOM   190  O  OD1 . ASN A 1 26  ? -11.811 -30.064 -1.524 1.00 113.59 ? 26  ASN A OD1 1 
ATOM   191  N  ND2 . ASN A 1 26  ? -11.736 -30.181 -3.748 1.00 120.70 ? 26  ASN A ND2 1 
ATOM   192  N  N   . GLY A 1 27  ? -7.268  -32.575 -0.619 1.00 108.81 ? 27  GLY A N   1 
ATOM   193  C  CA  . GLY A 1 27  ? -6.427  -33.739 -0.337 1.00 107.99 ? 27  GLY A CA  1 
ATOM   194  C  C   . GLY A 1 27  ? -6.738  -34.258 1.053  1.00 102.29 ? 27  GLY A C   1 
ATOM   195  O  O   . GLY A 1 27  ? -7.795  -33.948 1.602  1.00 99.29  ? 27  GLY A O   1 
ATOM   196  N  N   . PRO A 1 28  ? -5.804  -35.020 1.647  1.00 100.58 ? 28  PRO A N   1 
ATOM   197  C  CA  . PRO A 1 28  ? -5.991  -35.508 2.989  1.00 95.80  ? 28  PRO A CA  1 
ATOM   198  C  C   . PRO A 1 28  ? -5.539  -34.452 3.989  1.00 92.29  ? 28  PRO A C   1 
ATOM   199  O  O   . PRO A 1 28  ? -4.945  -33.458 3.589  1.00 93.69  ? 28  PRO A O   1 
ATOM   200  C  CB  . PRO A 1 28  ? -5.060  -36.706 3.027  1.00 97.43  ? 28  PRO A CB  1 
ATOM   201  C  CG  . PRO A 1 28  ? -3.877  -36.243 2.237  1.00 101.51 ? 28  PRO A CG  1 
ATOM   202  C  CD  . PRO A 1 28  ? -4.418  -35.256 1.201  1.00 103.89 ? 28  PRO A CD  1 
ATOM   203  N  N   . VAL A 1 29  ? -5.797  -34.698 5.269  1.00 87.85  ? 29  VAL A N   1 
ATOM   204  C  CA  . VAL A 1 29  ? -5.586  -33.734 6.349  1.00 84.83  ? 29  VAL A CA  1 
ATOM   205  C  C   . VAL A 1 29  ? -4.838  -34.369 7.530  1.00 83.47  ? 29  VAL A C   1 
ATOM   206  O  O   . VAL A 1 29  ? -5.394  -35.199 8.219  1.00 82.10  ? 29  VAL A O   1 
ATOM   207  C  CB  . VAL A 1 29  ? -6.938  -33.273 6.915  1.00 81.85  ? 29  VAL A CB  1 
ATOM   208  C  CG1 . VAL A 1 29  ? -6.706  -32.333 8.053  1.00 79.08  ? 29  VAL A CG1 1 
ATOM   209  C  CG2 . VAL A 1 29  ? -7.804  -32.637 5.856  1.00 83.38  ? 29  VAL A CG2 1 
ATOM   210  N  N   . LYS A 1 30  ? -3.592  -34.002 7.791  1.00 84.60  ? 30  LYS A N   1 
ATOM   211  C  CA  . LYS A 1 30  ? -2.905  -34.561 8.954  1.00 83.87  ? 30  LYS A CA  1 
ATOM   212  C  C   . LYS A 1 30  ? -3.393  -33.869 10.171 1.00 80.44  ? 30  LYS A C   1 
ATOM   213  O  O   . LYS A 1 30  ? -3.403  -32.659 10.233 1.00 80.39  ? 30  LYS A O   1 
ATOM   214  C  CB  . LYS A 1 30  ? -1.393  -34.409 8.888  1.00 87.13  ? 30  LYS A CB  1 
ATOM   215  C  CG  . LYS A 1 30  ? -0.682  -35.594 8.222  1.00 92.66  ? 30  LYS A CG  1 
ATOM   216  C  CD  . LYS A 1 30  ? 0.662   -35.216 7.519  1.00 99.48  ? 30  LYS A CD  1 
ATOM   217  C  CE  . LYS A 1 30  ? 0.615   -35.449 5.978  1.00 103.61 ? 30  LYS A CE  1 
ATOM   218  N  NZ  . LYS A 1 30  ? 1.832   -36.156 5.514  1.00 108.14 ? 30  LYS A NZ  1 
ATOM   219  N  N   . VAL A 1 31  ? -3.781  -34.654 11.155 1.00 78.30  ? 31  VAL A N   1 
ATOM   220  C  CA  . VAL A 1 31  ? -4.284  -34.131 12.403 1.00 75.70  ? 31  VAL A CA  1 
ATOM   221  C  C   . VAL A 1 31  ? -3.390  -34.603 13.496 1.00 76.40  ? 31  VAL A C   1 
ATOM   222  O  O   . VAL A 1 31  ? -3.273  -35.786 13.673 1.00 76.78  ? 31  VAL A O   1 
ATOM   223  C  CB  . VAL A 1 31  ? -5.650  -34.708 12.701 1.00 73.38  ? 31  VAL A CB  1 
ATOM   224  C  CG1 . VAL A 1 31  ? -6.113  -34.242 14.069 1.00 70.48  ? 31  VAL A CG1 1 
ATOM   225  C  CG2 . VAL A 1 31  ? -6.624  -34.347 11.599 1.00 72.83  ? 31  VAL A CG2 1 
ATOM   226  N  N   . TRP A 1 32  ? -2.746  -33.705 14.224 1.00 77.34  ? 32  TRP A N   1 
ATOM   227  C  CA  . TRP A 1 32  ? -1.912  -34.159 15.310 1.00 78.84  ? 32  TRP A CA  1 
ATOM   228  C  C   . TRP A 1 32  ? -1.746  -33.157 16.422 1.00 77.75  ? 32  TRP A C   1 
ATOM   229  O  O   . TRP A 1 32  ? -1.900  -31.981 16.248 1.00 77.41  ? 32  TRP A O   1 
ATOM   230  C  CB  . TRP A 1 32  ? -0.532  -34.581 14.791 1.00 82.67  ? 32  TRP A CB  1 
ATOM   231  C  CG  . TRP A 1 32  ? 0.414   -33.476 14.835 1.00 88.22  ? 32  TRP A CG  1 
ATOM   232  C  CD1 . TRP A 1 32  ? 1.384   -33.260 15.779 1.00 92.96  ? 32  TRP A CD1 1 
ATOM   233  C  CD2 . TRP A 1 32  ? 0.460   -32.367 13.933 1.00 92.98  ? 32  TRP A CD2 1 
ATOM   234  N  NE1 . TRP A 1 32  ? 2.046   -32.083 15.506 1.00 96.78  ? 32  TRP A NE1 1 
ATOM   235  C  CE2 . TRP A 1 32  ? 1.502   -31.514 14.379 1.00 96.62  ? 32  TRP A CE2 1 
ATOM   236  C  CE3 . TRP A 1 32  ? -0.274  -32.012 12.781 1.00 93.24  ? 32  TRP A CE3 1 
ATOM   237  C  CZ2 . TRP A 1 32  ? 1.835   -30.319 13.714 1.00 98.95  ? 32  TRP A CZ2 1 
ATOM   238  C  CZ3 . TRP A 1 32  ? 0.048   -30.819 12.114 1.00 95.73  ? 32  TRP A CZ3 1 
ATOM   239  C  CH2 . TRP A 1 32  ? 1.097   -29.985 12.586 1.00 98.53  ? 32  TRP A CH2 1 
ATOM   240  N  N   . GLY A 1 33  ? -1.396  -33.672 17.576 1.00 77.76  ? 33  GLY A N   1 
ATOM   241  C  CA  . GLY A 1 33  ? -1.228  -32.875 18.757 1.00 78.03  ? 33  GLY A CA  1 
ATOM   242  C  C   . GLY A 1 33  ? -1.264  -33.791 19.968 1.00 77.97  ? 33  GLY A C   1 
ATOM   243  O  O   . GLY A 1 33  ? -0.930  -34.969 19.869 1.00 79.01  ? 33  GLY A O   1 
ATOM   244  N  N   . SER A 1 34  ? -1.703  -33.272 21.108 1.00 77.19  ? 34  SER A N   1 
ATOM   245  C  CA  . SER A 1 34  ? -1.606  -34.002 22.341 1.00 77.61  ? 34  SER A CA  1 
ATOM   246  C  C   . SER A 1 34  ? -2.627  -33.549 23.333 1.00 76.49  ? 34  SER A C   1 
ATOM   247  O  O   . SER A 1 34  ? -2.820  -32.361 23.498 1.00 76.74  ? 34  SER A O   1 
ATOM   248  C  CB  . SER A 1 34  ? -0.261  -33.742 22.939 1.00 80.67  ? 34  SER A CB  1 
ATOM   249  O  OG  . SER A 1 34  ? -0.122  -34.536 24.079 1.00 82.50  ? 34  SER A OG  1 
ATOM   250  N  N   . ILE A 1 35  ? -3.265  -34.503 24.008 1.00 75.97  ? 35  ILE A N   1 
ATOM   251  C  CA  . ILE A 1 35  ? -4.277  -34.222 25.048 1.00 75.55  ? 35  ILE A CA  1 
ATOM   252  C  C   . ILE A 1 35  ? -3.871  -34.858 26.342 1.00 77.78  ? 35  ILE A C   1 
ATOM   253  O  O   . ILE A 1 35  ? -3.339  -35.944 26.329 1.00 78.79  ? 35  ILE A O   1 
ATOM   254  C  CB  . ILE A 1 35  ? -5.631  -34.824 24.720 1.00 73.16  ? 35  ILE A CB  1 
ATOM   255  C  CG1 . ILE A 1 35  ? -6.004  -34.538 23.268 1.00 71.45  ? 35  ILE A CG1 1 
ATOM   256  C  CG2 . ILE A 1 35  ? -6.658  -34.266 25.652 1.00 73.16  ? 35  ILE A CG2 1 
ATOM   257  C  CD1 . ILE A 1 35  ? -7.332  -35.111 22.845 1.00 69.79  ? 35  ILE A CD1 1 
ATOM   258  N  N   . LYS A 1 36  ? -4.136  -34.205 27.457 1.00 79.35  ? 36  LYS A N   1 
ATOM   259  C  CA  . LYS A 1 36  ? -3.810  -34.788 28.748 1.00 82.45  ? 36  LYS A CA  1 
ATOM   260  C  C   . LYS A 1 36  ? -4.969  -34.744 29.717 1.00 82.54  ? 36  LYS A C   1 
ATOM   261  O  O   . LYS A 1 36  ? -5.899  -33.971 29.535 1.00 81.26  ? 36  LYS A O   1 
ATOM   262  C  CB  . LYS A 1 36  ? -2.596  -34.111 29.364 1.00 86.00  ? 36  LYS A CB  1 
ATOM   263  C  CG  . LYS A 1 36  ? -2.607  -32.600 29.315 1.00 88.45  ? 36  LYS A CG  1 
ATOM   264  C  CD  . LYS A 1 36  ? -1.383  -32.001 30.061 1.00 94.35  ? 36  LYS A CD  1 
ATOM   265  C  CE  . LYS A 1 36  ? -1.633  -30.566 30.594 1.00 96.08  ? 36  LYS A CE  1 
ATOM   266  N  NZ  . LYS A 1 36  ? -0.461  -30.070 31.375 1.00 100.14 ? 36  LYS A NZ  1 
ATOM   267  N  N   . GLY A 1 37  ? -4.908  -35.589 30.745 1.00 84.63  ? 37  GLY A N   1 
ATOM   268  C  CA  . GLY A 1 37  ? -5.987  -35.696 31.744 1.00 85.68  ? 37  GLY A CA  1 
ATOM   269  C  C   . GLY A 1 37  ? -7.082  -36.696 31.410 1.00 83.66  ? 37  GLY A C   1 
ATOM   270  O  O   . GLY A 1 37  ? -8.261  -36.498 31.735 1.00 83.42  ? 37  GLY A O   1 
ATOM   271  N  N   . LEU A 1 38  ? -6.691  -37.774 30.748 1.00 82.54  ? 38  LEU A N   1 
ATOM   272  C  CA  . LEU A 1 38  ? -7.640  -38.768 30.260 1.00 80.86  ? 38  LEU A CA  1 
ATOM   273  C  C   . LEU A 1 38  ? -7.507  -40.054 31.060 1.00 82.83  ? 38  LEU A C   1 
ATOM   274  O  O   . LEU A 1 38  ? -6.470  -40.342 31.633 1.00 85.09  ? 38  LEU A O   1 
ATOM   275  C  CB  . LEU A 1 38  ? -7.386  -39.029 28.769 1.00 78.40  ? 38  LEU A CB  1 
ATOM   276  C  CG  . LEU A 1 38  ? -7.912  -37.910 27.867 1.00 75.97  ? 38  LEU A CG  1 
ATOM   277  C  CD1 . LEU A 1 38  ? -7.105  -37.771 26.609 1.00 74.17  ? 38  LEU A CD1 1 
ATOM   278  C  CD2 . LEU A 1 38  ? -9.360  -38.180 27.578 1.00 75.02  ? 38  LEU A CD2 1 
ATOM   279  N  N   . THR A 1 39  ? -8.566  -40.828 31.117 1.00 82.23  ? 39  THR A N   1 
ATOM   280  C  CA  . THR A 1 39  ? -8.438  -42.145 31.665 1.00 84.10  ? 39  THR A CA  1 
ATOM   281  C  C   . THR A 1 39  ? -7.694  -42.963 30.653 1.00 83.43  ? 39  THR A C   1 
ATOM   282  O  O   . THR A 1 39  ? -7.962  -42.843 29.468 1.00 80.96  ? 39  THR A O   1 
ATOM   283  C  CB  . THR A 1 39  ? -9.785  -42.752 31.880 1.00 84.10  ? 39  THR A CB  1 
ATOM   284  O  OG1 . THR A 1 39  ? -10.735 -42.037 31.087 1.00 81.34  ? 39  THR A OG1 1 
ATOM   285  C  CG2 . THR A 1 39  ? -10.161 -42.635 33.342 1.00 87.21  ? 39  THR A CG2 1 
ATOM   286  N  N   . GLU A 1 40  ? -6.754  -43.786 31.102 1.00 86.32  ? 40  GLU A N   1 
ATOM   287  C  CA  . GLU A 1 40  ? -6.012  -44.678 30.195 1.00 86.53  ? 40  GLU A CA  1 
ATOM   288  C  C   . GLU A 1 40  ? -6.984  -45.333 29.234 1.00 84.32  ? 40  GLU A C   1 
ATOM   289  O  O   . GLU A 1 40  ? -8.119  -45.617 29.613 1.00 84.26  ? 40  GLU A O   1 
ATOM   290  C  CB  . GLU A 1 40  ? -5.248  -45.764 30.977 1.00 90.29  ? 40  GLU A CB  1 
ATOM   291  C  CG  . GLU A 1 40  ? -4.647  -46.917 30.109 1.00 91.79  ? 40  GLU A CG  1 
ATOM   292  C  CD  . GLU A 1 40  ? -3.441  -47.653 30.764 1.00 97.32  ? 40  GLU A CD  1 
ATOM   293  O  OE1 . GLU A 1 40  ? -3.535  -48.078 31.948 1.00 100.85 ? 40  GLU A OE1 1 
ATOM   294  O  OE2 . GLU A 1 40  ? -2.397  -47.829 30.073 1.00 98.69  ? 40  GLU A OE2 1 
ATOM   295  N  N   . GLY A 1 41  ? -6.556  -45.532 27.989 1.00 82.88  ? 41  GLY A N   1 
ATOM   296  C  CA  . GLY A 1 41  ? -7.363  -46.261 27.009 1.00 81.35  ? 41  GLY A CA  1 
ATOM   297  C  C   . GLY A 1 41  ? -7.996  -45.399 25.930 1.00 78.36  ? 41  GLY A C   1 
ATOM   298  O  O   . GLY A 1 41  ? -7.535  -44.289 25.655 1.00 77.53  ? 41  GLY A O   1 
ATOM   299  N  N   . LEU A 1 42  ? -9.063  -45.914 25.322 1.00 76.92  ? 42  LEU A N   1 
ATOM   300  C  CA  . LEU A 1 42  ? -9.629  -45.290 24.141 1.00 74.57  ? 42  LEU A CA  1 
ATOM   301  C  C   . LEU A 1 42  ? -10.579 -44.185 24.493 1.00 72.68  ? 42  LEU A C   1 
ATOM   302  O  O   . LEU A 1 42  ? -11.240 -44.233 25.507 1.00 73.76  ? 42  LEU A O   1 
ATOM   303  C  CB  . LEU A 1 42  ? -10.355 -46.317 23.266 1.00 74.86  ? 42  LEU A CB  1 
ATOM   304  C  CG  . LEU A 1 42  ? -9.494  -47.279 22.438 1.00 76.60  ? 42  LEU A CG  1 
ATOM   305  C  CD1 . LEU A 1 42  ? -9.457  -48.679 23.064 1.00 79.74  ? 42  LEU A CD1 1 
ATOM   306  C  CD2 . LEU A 1 42  ? -9.987  -47.349 20.986 1.00 75.10  ? 42  LEU A CD2 1 
ATOM   307  N  N   . HIS A 1 43  ? -10.656 -43.193 23.629 1.00 70.30  ? 43  HIS A N   1 
ATOM   308  C  CA  . HIS A 1 43  ? -11.626 -42.132 23.778 1.00 68.80  ? 43  HIS A CA  1 
ATOM   309  C  C   . HIS A 1 43  ? -12.101 -41.644 22.436 1.00 66.79  ? 43  HIS A C   1 
ATOM   310  O  O   . HIS A 1 43  ? -11.311 -41.422 21.557 1.00 66.13  ? 43  HIS A O   1 
ATOM   311  C  CB  . HIS A 1 43  ? -11.010 -40.971 24.520 1.00 69.02  ? 43  HIS A CB  1 
ATOM   312  C  CG  . HIS A 1 43  ? -10.757 -41.240 25.962 1.00 71.26  ? 43  HIS A CG  1 
ATOM   313  N  ND1 . HIS A 1 43  ? -11.655 -40.896 26.941 1.00 73.12  ? 43  HIS A ND1 1 
ATOM   314  C  CD2 . HIS A 1 43  ? -9.698  -41.798 26.593 1.00 73.61  ? 43  HIS A CD2 1 
ATOM   315  C  CE1 . HIS A 1 43  ? -11.161 -41.232 28.116 1.00 76.36  ? 43  HIS A CE1 1 
ATOM   316  N  NE2 . HIS A 1 43  ? -9.975  -41.782 27.933 1.00 76.46  ? 43  HIS A NE2 1 
ATOM   317  N  N   . GLY A 1 44  ? -13.401 -41.470 22.297 1.00 66.12  ? 44  GLY A N   1 
ATOM   318  C  CA  . GLY A 1 44  ? -13.994 -40.996 21.070 1.00 65.28  ? 44  GLY A CA  1 
ATOM   319  C  C   . GLY A 1 44  ? -13.534 -39.604 20.738 1.00 64.34  ? 44  GLY A C   1 
ATOM   320  O  O   . GLY A 1 44  ? -13.180 -38.853 21.621 1.00 64.38  ? 44  GLY A O   1 
ATOM   321  N  N   . PHE A 1 45  ? -13.576 -39.251 19.456 1.00 63.99  ? 45  PHE A N   1 
ATOM   322  C  CA  . PHE A 1 45  ? -12.916 -38.051 18.951 1.00 63.44  ? 45  PHE A CA  1 
ATOM   323  C  C   . PHE A 1 45  ? -13.587 -37.618 17.664 1.00 63.37  ? 45  PHE A C   1 
ATOM   324  O  O   . PHE A 1 45  ? -13.429 -38.258 16.647 1.00 63.40  ? 45  PHE A O   1 
ATOM   325  C  CB  . PHE A 1 45  ? -11.478 -38.426 18.699 1.00 63.87  ? 45  PHE A CB  1 
ATOM   326  C  CG  . PHE A 1 45  ? -10.575 -37.293 18.385 1.00 63.98  ? 45  PHE A CG  1 
ATOM   327  C  CD1 . PHE A 1 45  ? -10.307 -36.339 19.301 1.00 64.34  ? 45  PHE A CD1 1 
ATOM   328  C  CD2 . PHE A 1 45  ? -9.907  -37.247 17.189 1.00 64.84  ? 45  PHE A CD2 1 
ATOM   329  C  CE1 . PHE A 1 45  ? -9.445  -35.325 19.009 1.00 65.00  ? 45  PHE A CE1 1 
ATOM   330  C  CE2 . PHE A 1 45  ? -9.044  -36.244 16.906 1.00 64.97  ? 45  PHE A CE2 1 
ATOM   331  C  CZ  . PHE A 1 45  ? -8.820  -35.281 17.814 1.00 65.26  ? 45  PHE A CZ  1 
ATOM   332  N  N   . HIS A 1 46  ? -14.351 -36.534 17.713 1.00 63.47  ? 46  HIS A N   1 
ATOM   333  C  CA  . HIS A 1 46  ? -15.174 -36.146 16.590 1.00 64.31  ? 46  HIS A CA  1 
ATOM   334  C  C   . HIS A 1 46  ? -15.265 -34.674 16.392 1.00 64.07  ? 46  HIS A C   1 
ATOM   335  O  O   . HIS A 1 46  ? -15.151 -33.908 17.351 1.00 63.82  ? 46  HIS A O   1 
ATOM   336  C  CB  . HIS A 1 46  ? -16.588 -36.583 16.831 1.00 65.54  ? 46  HIS A CB  1 
ATOM   337  C  CG  . HIS A 1 46  ? -16.703 -37.951 17.393 1.00 67.63  ? 46  HIS A CG  1 
ATOM   338  N  ND1 . HIS A 1 46  ? -17.263 -38.195 18.621 1.00 70.14  ? 46  HIS A ND1 1 
ATOM   339  C  CD2 . HIS A 1 46  ? -16.323 -39.146 16.899 1.00 70.25  ? 46  HIS A CD2 1 
ATOM   340  C  CE1 . HIS A 1 46  ? -17.224 -39.490 18.858 1.00 72.19  ? 46  HIS A CE1 1 
ATOM   341  N  NE2 . HIS A 1 46  ? -16.658 -40.090 17.827 1.00 71.34  ? 46  HIS A NE2 1 
ATOM   342  N  N   . VAL A 1 47  ? -15.522 -34.290 15.145 1.00 64.61  ? 47  VAL A N   1 
ATOM   343  C  CA  . VAL A 1 47  ? -15.921 -32.945 14.836 1.00 65.11  ? 47  VAL A CA  1 
ATOM   344  C  C   . VAL A 1 47  ? -17.403 -32.912 14.889 1.00 66.43  ? 47  VAL A C   1 
ATOM   345  O  O   . VAL A 1 47  ? -18.050 -33.706 14.227 1.00 67.34  ? 47  VAL A O   1 
ATOM   346  C  CB  . VAL A 1 47  ? -15.542 -32.550 13.454 1.00 65.69  ? 47  VAL A CB  1 
ATOM   347  C  CG1 . VAL A 1 47  ? -16.004 -31.148 13.219 1.00 66.44  ? 47  VAL A CG1 1 
ATOM   348  C  CG2 . VAL A 1 47  ? -14.071 -32.651 13.300 1.00 64.96  ? 47  VAL A CG2 1 
ATOM   349  N  N   . HIS A 1 48  ? -17.942 -32.002 15.685 1.00 67.28  ? 48  HIS A N   1 
ATOM   350  C  CA  . HIS A 1 48  ? -19.381 -31.850 15.796 1.00 69.38  ? 48  HIS A CA  1 
ATOM   351  C  C   . HIS A 1 48  ? -19.775 -30.661 14.971 1.00 70.64  ? 48  HIS A C   1 
ATOM   352  O  O   . HIS A 1 48  ? -18.928 -29.879 14.606 1.00 70.06  ? 48  HIS A O   1 
ATOM   353  C  CB  . HIS A 1 48  ? -19.811 -31.642 17.250 1.00 70.01  ? 48  HIS A CB  1 
ATOM   354  C  CG  . HIS A 1 48  ? -19.655 -32.858 18.119 1.00 70.65  ? 48  HIS A CG  1 
ATOM   355  N  ND1 . HIS A 1 48  ? -20.687 -33.373 18.873 1.00 72.95  ? 48  HIS A ND1 1 
ATOM   356  C  CD2 . HIS A 1 48  ? -18.584 -33.649 18.358 1.00 70.73  ? 48  HIS A CD2 1 
ATOM   357  C  CE1 . HIS A 1 48  ? -20.260 -34.436 19.525 1.00 73.52  ? 48  HIS A CE1 1 
ATOM   358  N  NE2 . HIS A 1 48  ? -18.987 -34.623 19.233 1.00 71.55  ? 48  HIS A NE2 1 
ATOM   359  N  N   . GLU A 1 49  ? -21.070 -30.522 14.714 1.00 72.85  ? 49  GLU A N   1 
ATOM   360  C  CA  . GLU A 1 49  ? -21.584 -29.577 13.717 1.00 74.95  ? 49  GLU A CA  1 
ATOM   361  C  C   . GLU A 1 49  ? -21.281 -28.107 14.005 1.00 74.93  ? 49  GLU A C   1 
ATOM   362  O  O   . GLU A 1 49  ? -20.931 -27.385 13.100 1.00 75.11  ? 49  GLU A O   1 
ATOM   363  C  CB  . GLU A 1 49  ? -23.100 -29.757 13.529 1.00 77.77  ? 49  GLU A CB  1 
ATOM   364  C  CG  . GLU A 1 49  ? -23.644 -29.145 12.238 1.00 81.69  ? 49  GLU A CG  1 
ATOM   365  C  CD  . GLU A 1 49  ? -25.081 -29.573 11.897 1.00 87.10  ? 49  GLU A CD  1 
ATOM   366  O  OE1 . GLU A 1 49  ? -25.538 -30.634 12.368 1.00 88.98  ? 49  GLU A OE1 1 
ATOM   367  O  OE2 . GLU A 1 49  ? -25.762 -28.852 11.133 1.00 91.37  ? 49  GLU A OE2 1 
ATOM   368  N  N   . PHE A 1 50  ? -21.400 -27.665 15.247 1.00 74.97  ? 50  PHE A N   1 
ATOM   369  C  CA  . PHE A 1 50  ? -21.382 -26.231 15.534 1.00 76.40  ? 50  PHE A CA  1 
ATOM   370  C  C   . PHE A 1 50  ? -20.227 -25.733 16.383 1.00 74.89  ? 50  PHE A C   1 
ATOM   371  O  O   . PHE A 1 50  ? -19.786 -26.414 17.292 1.00 73.41  ? 50  PHE A O   1 
ATOM   372  C  CB  . PHE A 1 50  ? -22.673 -25.817 16.236 1.00 79.03  ? 50  PHE A CB  1 
ATOM   373  C  CG  . PHE A 1 50  ? -23.910 -26.182 15.489 1.00 82.37  ? 50  PHE A CG  1 
ATOM   374  C  CD1 . PHE A 1 50  ? -24.014 -25.944 14.134 1.00 84.23  ? 50  PHE A CD1 1 
ATOM   375  C  CD2 . PHE A 1 50  ? -24.984 -26.763 16.153 1.00 85.44  ? 50  PHE A CD2 1 
ATOM   376  C  CE1 . PHE A 1 50  ? -25.163 -26.285 13.445 1.00 87.31  ? 50  PHE A CE1 1 
ATOM   377  C  CE2 . PHE A 1 50  ? -26.129 -27.123 15.466 1.00 88.33  ? 50  PHE A CE2 1 
ATOM   378  C  CZ  . PHE A 1 50  ? -26.220 -26.886 14.108 1.00 89.26  ? 50  PHE A CZ  1 
ATOM   379  N  N   . GLY A 1 51  ? -19.796 -24.506 16.088 1.00 75.72  ? 51  GLY A N   1 
ATOM   380  C  CA  . GLY A 1 51  ? -18.792 -23.786 16.852 1.00 75.54  ? 51  GLY A CA  1 
ATOM   381  C  C   . GLY A 1 51  ? -19.426 -23.035 17.992 1.00 77.64  ? 51  GLY A C   1 
ATOM   382  O  O   . GLY A 1 51  ? -19.062 -21.926 18.303 1.00 78.58  ? 51  GLY A O   1 
ATOM   383  N  N   . ASP A 1 52  ? -20.371 -23.679 18.641 1.00 78.87  ? 52  ASP A N   1 
ATOM   384  C  CA  . ASP A 1 52  ? -21.139 -23.069 19.684 1.00 81.55  ? 52  ASP A CA  1 
ATOM   385  C  C   . ASP A 1 52  ? -20.588 -23.592 20.978 1.00 81.06  ? 52  ASP A C   1 
ATOM   386  O  O   . ASP A 1 52  ? -20.454 -24.786 21.157 1.00 79.71  ? 52  ASP A O   1 
ATOM   387  C  CB  . ASP A 1 52  ? -22.588 -23.497 19.527 1.00 83.45  ? 52  ASP A CB  1 
ATOM   388  C  CG  . ASP A 1 52  ? -23.544 -22.452 19.993 1.00 87.28  ? 52  ASP A CG  1 
ATOM   389  O  OD1 . ASP A 1 52  ? -23.361 -21.993 21.146 1.00 88.35  ? 52  ASP A OD1 1 
ATOM   390  O  OD2 . ASP A 1 52  ? -24.471 -22.111 19.208 1.00 89.99  ? 52  ASP A OD2 1 
ATOM   391  N  N   . ASN A 1 53  ? -20.224 -22.703 21.872 1.00 82.84  ? 53  ASN A N   1 
ATOM   392  C  CA  . ASN A 1 53  ? -19.815 -23.115 23.204 1.00 83.66  ? 53  ASN A CA  1 
ATOM   393  C  C   . ASN A 1 53  ? -20.565 -22.315 24.256 1.00 86.77  ? 53  ASN A C   1 
ATOM   394  O  O   . ASN A 1 53  ? -20.108 -22.168 25.402 1.00 87.94  ? 53  ASN A O   1 
ATOM   395  C  CB  . ASN A 1 53  ? -18.314 -22.940 23.370 1.00 82.71  ? 53  ASN A CB  1 
ATOM   396  C  CG  . ASN A 1 53  ? -17.533 -24.178 22.985 1.00 82.68  ? 53  ASN A CG  1 
ATOM   397  O  OD1 . ASN A 1 53  ? -16.648 -24.572 23.726 1.00 87.58  ? 53  ASN A OD1 1 
ATOM   398  N  ND2 . ASN A 1 53  ? -17.846 -24.797 21.830 1.00 81.94  ? 53  ASN A ND2 1 
ATOM   399  N  N   . THR A 1 54  ? -21.725 -21.813 23.841 1.00 88.33  ? 54  THR A N   1 
ATOM   400  C  CA  . THR A 1 54  ? -22.590 -21.032 24.678 1.00 92.08  ? 54  THR A CA  1 
ATOM   401  C  C   . THR A 1 54  ? -22.797 -21.723 26.002 1.00 93.52  ? 54  THR A C   1 
ATOM   402  O  O   . THR A 1 54  ? -22.561 -21.131 27.041 1.00 95.83  ? 54  THR A O   1 
ATOM   403  C  CB  . THR A 1 54  ? -23.939 -20.871 23.992 1.00 93.99  ? 54  THR A CB  1 
ATOM   404  O  OG1 . THR A 1 54  ? -23.722 -20.256 22.726 1.00 92.63  ? 54  THR A OG1 1 
ATOM   405  C  CG2 . THR A 1 54  ? -24.903 -20.009 24.831 1.00 99.43  ? 54  THR A CG2 1 
ATOM   406  N  N   . ALA A 1 55  ? -23.248 -22.981 25.941 1.00 92.63  ? 55  ALA A N   1 
ATOM   407  C  CA  . ALA A 1 55  ? -23.514 -23.824 27.125 1.00 94.18  ? 55  ALA A CA  1 
ATOM   408  C  C   . ALA A 1 55  ? -22.528 -24.997 27.194 1.00 91.14  ? 55  ALA A C   1 
ATOM   409  O  O   . ALA A 1 55  ? -22.903 -26.162 27.000 1.00 90.02  ? 55  ALA A O   1 
ATOM   410  C  CB  . ALA A 1 55  ? -24.973 -24.354 27.087 1.00 96.21  ? 55  ALA A CB  1 
ATOM   411  N  N   . GLY A 1 56  ? -21.262 -24.686 27.443 1.00 90.48  ? 56  GLY A N   1 
ATOM   412  C  CA  . GLY A 1 56  ? -20.196 -25.707 27.428 1.00 88.07  ? 56  GLY A CA  1 
ATOM   413  C  C   . GLY A 1 56  ? -20.123 -26.503 26.124 1.00 85.13  ? 56  GLY A C   1 
ATOM   414  O  O   . GLY A 1 56  ? -20.337 -25.970 25.019 1.00 84.38  ? 56  GLY A O   1 
ATOM   415  N  N   . CYS A 1 57  ? -19.843 -27.791 26.232 1.00 83.77  ? 57  CYS A N   1 
ATOM   416  C  CA  . CYS A 1 57  ? -19.690 -28.592 25.023 1.00 81.33  ? 57  CYS A CA  1 
ATOM   417  C  C   . CYS A 1 57  ? -21.003 -29.056 24.405 1.00 81.49  ? 57  CYS A C   1 
ATOM   418  O  O   . CYS A 1 57  ? -21.012 -29.392 23.238 1.00 79.70  ? 57  CYS A O   1 
ATOM   419  C  CB  . CYS A 1 57  ? -18.740 -29.754 25.275 1.00 79.58  ? 57  CYS A CB  1 
ATOM   420  S  SG  . CYS A 1 57  ? -16.992 -29.179 25.580 1.00 81.46  ? 57  CYS A SG  1 
ATOM   421  N  N   . THR A 1 58  ? -22.099 -29.058 25.168 1.00 84.03  ? 58  THR A N   1 
ATOM   422  C  CA  . THR A 1 58  ? -23.407 -29.519 24.657 1.00 85.10  ? 58  THR A CA  1 
ATOM   423  C  C   . THR A 1 58  ? -23.953 -28.670 23.511 1.00 85.38  ? 58  THR A C   1 
ATOM   424  O  O   . THR A 1 58  ? -24.728 -29.150 22.696 1.00 85.68  ? 58  THR A O   1 
ATOM   425  C  CB  . THR A 1 58  ? -24.483 -29.523 25.744 1.00 88.55  ? 58  THR A CB  1 
ATOM   426  O  OG1 . THR A 1 58  ? -23.845 -29.441 27.008 1.00 89.09  ? 58  THR A OG1 1 
ATOM   427  C  CG2 . THR A 1 58  ? -25.344 -30.789 25.674 1.00 88.78  ? 58  THR A CG2 1 
ATOM   428  N  N   . SER A 1 59  ? -23.554 -27.405 23.471 1.00 85.64  ? 59  SER A N   1 
ATOM   429  C  CA  . SER A 1 59  ? -23.946 -26.473 22.402 1.00 86.08  ? 59  SER A CA  1 
ATOM   430  C  C   . SER A 1 59  ? -23.461 -26.864 21.002 1.00 83.38  ? 59  SER A C   1 
ATOM   431  O  O   . SER A 1 59  ? -24.053 -26.466 19.998 1.00 84.01  ? 59  SER A O   1 
ATOM   432  C  CB  . SER A 1 59  ? -23.394 -25.090 22.730 1.00 87.00  ? 59  SER A CB  1 
ATOM   433  O  OG  . SER A 1 59  ? -23.704 -24.738 24.057 1.00 90.27  ? 59  SER A OG  1 
ATOM   434  N  N   . ALA A 1 60  ? -22.361 -27.626 20.963 1.00 80.75  ? 60  ALA A N   1 
ATOM   435  C  CA  . ALA A 1 60  ? -21.713 -28.098 19.725 1.00 78.44  ? 60  ALA A CA  1 
ATOM   436  C  C   . ALA A 1 60  ? -22.646 -28.907 18.859 1.00 78.93  ? 60  ALA A C   1 
ATOM   437  O  O   . ALA A 1 60  ? -22.458 -28.986 17.660 1.00 78.18  ? 60  ALA A O   1 
ATOM   438  C  CB  . ALA A 1 60  ? -20.489 -28.938 20.061 1.00 76.10  ? 60  ALA A CB  1 
ATOM   439  N  N   . GLY A 1 61  ? -23.622 -29.543 19.490 1.00 80.57  ? 61  GLY A N   1 
ATOM   440  C  CA  . GLY A 1 61  ? -24.649 -30.286 18.787 1.00 82.01  ? 61  GLY A CA  1 
ATOM   441  C  C   . GLY A 1 61  ? -24.146 -31.651 18.384 1.00 80.34  ? 61  GLY A C   1 
ATOM   442  O  O   . GLY A 1 61  ? -23.138 -32.120 18.911 1.00 78.58  ? 61  GLY A O   1 
ATOM   443  N  N   . PRO A 1 62  ? -24.825 -32.288 17.425 1.00 81.36  ? 62  PRO A N   1 
ATOM   444  C  CA  . PRO A 1 62  ? -24.509 -33.632 17.054 1.00 80.42  ? 62  PRO A CA  1 
ATOM   445  C  C   . PRO A 1 62  ? -23.283 -33.668 16.188 1.00 78.43  ? 62  PRO A C   1 
ATOM   446  O  O   . PRO A 1 62  ? -22.762 -32.632 15.811 1.00 77.66  ? 62  PRO A O   1 
ATOM   447  C  CB  . PRO A 1 62  ? -25.698 -34.021 16.209 1.00 83.07  ? 62  PRO A CB  1 
ATOM   448  C  CG  . PRO A 1 62  ? -26.011 -32.771 15.479 1.00 84.19  ? 62  PRO A CG  1 
ATOM   449  C  CD  . PRO A 1 62  ? -25.729 -31.669 16.448 1.00 83.69  ? 62  PRO A CD  1 
ATOM   450  N  N   . HIS A 1 63  ? -22.863 -34.876 15.847 1.00 77.96  ? 63  HIS A N   1 
ATOM   451  C  CA  . HIS A 1 63  ? -21.721 -35.073 14.988 1.00 76.83  ? 63  HIS A CA  1 
ATOM   452  C  C   . HIS A 1 63  ? -21.928 -34.364 13.679 1.00 77.38  ? 63  HIS A C   1 
ATOM   453  O  O   . HIS A 1 63  ? -23.027 -34.351 13.143 1.00 79.57  ? 63  HIS A O   1 
ATOM   454  C  CB  . HIS A 1 63  ? -21.542 -36.550 14.695 1.00 77.33  ? 63  HIS A CB  1 
ATOM   455  C  CG  . HIS A 1 63  ? -21.050 -37.334 15.860 1.00 78.03  ? 63  HIS A CG  1 
ATOM   456  N  ND1 . HIS A 1 63  ? -20.151 -38.367 15.723 1.00 78.57  ? 63  HIS A ND1 1 
ATOM   457  C  CD2 . HIS A 1 63  ? -21.308 -37.225 17.184 1.00 80.24  ? 63  HIS A CD2 1 
ATOM   458  C  CE1 . HIS A 1 63  ? -19.884 -38.870 16.912 1.00 79.38  ? 63  HIS A CE1 1 
ATOM   459  N  NE2 . HIS A 1 63  ? -20.571 -38.194 17.817 1.00 80.74  ? 63  HIS A NE2 1 
ATOM   460  N  N   . PHE A 1 64  ? -20.852 -33.809 13.149 1.00 75.74  ? 64  PHE A N   1 
ATOM   461  C  CA  . PHE A 1 64  ? -20.910 -33.147 11.871 1.00 76.84  ? 64  PHE A CA  1 
ATOM   462  C  C   . PHE A 1 64  ? -21.273 -34.160 10.820 1.00 77.97  ? 64  PHE A C   1 
ATOM   463  O  O   . PHE A 1 64  ? -20.493 -35.047 10.506 1.00 76.87  ? 64  PHE A O   1 
ATOM   464  C  CB  . PHE A 1 64  ? -19.564 -32.532 11.516 1.00 75.93  ? 64  PHE A CB  1 
ATOM   465  C  CG  . PHE A 1 64  ? -19.557 -31.755 10.203 1.00 78.49  ? 64  PHE A CG  1 
ATOM   466  C  CD1 . PHE A 1 64  ? -20.631 -30.957 9.821  1.00 81.52  ? 64  PHE A CD1 1 
ATOM   467  C  CD2 . PHE A 1 64  ? -18.449 -31.789 9.375  1.00 79.17  ? 64  PHE A CD2 1 
ATOM   468  C  CE1 . PHE A 1 64  ? -20.599 -30.232 8.635  1.00 83.38  ? 64  PHE A CE1 1 
ATOM   469  C  CE2 . PHE A 1 64  ? -18.416 -31.051 8.192  1.00 81.70  ? 64  PHE A CE2 1 
ATOM   470  C  CZ  . PHE A 1 64  ? -19.492 -30.274 7.827  1.00 83.41  ? 64  PHE A CZ  1 
ATOM   471  N  N   . ASN A 1 65  ? -22.455 -34.002 10.256 1.00 80.37  ? 65  ASN A N   1 
ATOM   472  C  CA  . ASN A 1 65  ? -22.966 -34.996 9.355  1.00 82.56  ? 65  ASN A CA  1 
ATOM   473  C  C   . ASN A 1 65  ? -23.781 -34.385 8.239  1.00 85.96  ? 65  ASN A C   1 
ATOM   474  O  O   . ASN A 1 65  ? -25.008 -34.446 8.257  1.00 88.27  ? 65  ASN A O   1 
ATOM   475  C  CB  . ASN A 1 65  ? -23.817 -35.973 10.130 1.00 82.94  ? 65  ASN A CB  1 
ATOM   476  C  CG  . ASN A 1 65  ? -24.293 -37.085 9.271  1.00 84.52  ? 65  ASN A CG  1 
ATOM   477  O  OD1 . ASN A 1 65  ? -23.786 -37.288 8.164  1.00 85.29  ? 65  ASN A OD1 1 
ATOM   478  N  ND2 . ASN A 1 65  ? -25.266 -37.819 9.758  1.00 84.09  ? 65  ASN A ND2 1 
ATOM   479  N  N   . PRO A 1 66  ? -23.099 -33.812 7.241  1.00 86.91  ? 66  PRO A N   1 
ATOM   480  C  CA  . PRO A 1 66  ? -23.743 -33.048 6.177  1.00 90.26  ? 66  PRO A CA  1 
ATOM   481  C  C   . PRO A 1 66  ? -24.376 -33.925 5.087  1.00 94.05  ? 66  PRO A C   1 
ATOM   482  O  O   . PRO A 1 66  ? -25.280 -33.466 4.407  1.00 97.53  ? 66  PRO A O   1 
ATOM   483  C  CB  . PRO A 1 66  ? -22.594 -32.229 5.603  1.00 89.45  ? 66  PRO A CB  1 
ATOM   484  C  CG  . PRO A 1 66  ? -21.421 -33.113 5.747  1.00 87.60  ? 66  PRO A CG  1 
ATOM   485  C  CD  . PRO A 1 66  ? -21.661 -33.985 6.980  1.00 85.37  ? 66  PRO A CD  1 
ATOM   486  N  N   . LEU A 1 67  ? -23.922 -35.169 4.926  1.00 94.03  ? 67  LEU A N   1 
ATOM   487  C  CA  . LEU A 1 67  ? -24.533 -36.092 3.958  1.00 97.92  ? 67  LEU A CA  1 
ATOM   488  C  C   . LEU A 1 67  ? -25.601 -36.988 4.614  1.00 98.87  ? 67  LEU A C   1 
ATOM   489  O  O   . LEU A 1 67  ? -26.025 -37.964 4.002  1.00 101.84 ? 67  LEU A O   1 
ATOM   490  C  CB  . LEU A 1 67  ? -23.471 -37.007 3.317  1.00 98.20  ? 67  LEU A CB  1 
ATOM   491  C  CG  . LEU A 1 67  ? -22.107 -36.468 2.851  1.00 97.59  ? 67  LEU A CG  1 
ATOM   492  C  CD1 . LEU A 1 67  ? -20.945 -37.501 3.157  1.00 95.87  ? 67  LEU A CD1 1 
ATOM   493  C  CD2 . LEU A 1 67  ? -22.135 -36.049 1.357  1.00 100.51 ? 67  LEU A CD2 1 
ATOM   494  N  N   . SER A 1 68  ? -25.991 -36.698 5.862  1.00 96.88  ? 68  SER A N   1 
ATOM   495  C  CA  . SER A 1 68  ? -27.024 -37.470 6.590  1.00 97.93  ? 68  SER A CA  1 
ATOM   496  C  C   . SER A 1 68  ? -26.814 -38.989 6.639  1.00 98.38  ? 68  SER A C   1 
ATOM   497  O  O   . SER A 1 68  ? -27.772 -39.743 6.451  1.00 101.24 ? 68  SER A O   1 
ATOM   498  C  CB  . SER A 1 68  ? -28.412 -37.185 6.018  1.00 102.27 ? 68  SER A CB  1 
ATOM   499  O  OG  . SER A 1 68  ? -28.870 -35.938 6.470  1.00 102.35 ? 68  SER A OG  1 
ATOM   500  N  N   . ARG A 1 69  ? -25.583 -39.427 6.916  1.00 96.02  ? 69  ARG A N   1 
ATOM   501  C  CA  . ARG A 1 69  ? -25.271 -40.851 7.070  1.00 96.60  ? 69  ARG A CA  1 
ATOM   502  C  C   . ARG A 1 69  ? -25.438 -41.329 8.515  1.00 94.35  ? 69  ARG A C   1 
ATOM   503  O  O   . ARG A 1 69  ? -25.680 -40.544 9.424  1.00 92.67  ? 69  ARG A O   1 
ATOM   504  C  CB  . ARG A 1 69  ? -23.839 -41.121 6.641  1.00 95.51  ? 69  ARG A CB  1 
ATOM   505  C  CG  . ARG A 1 69  ? -23.487 -40.614 5.262  1.00 99.52  ? 69  ARG A CG  1 
ATOM   506  C  CD  . ARG A 1 69  ? -24.063 -41.507 4.172  1.00 106.83 ? 69  ARG A CD  1 
ATOM   507  N  NE  . ARG A 1 69  ? -23.656 -41.041 2.846  1.00 111.73 ? 69  ARG A NE  1 
ATOM   508  C  CZ  . ARG A 1 69  ? -22.454 -41.248 2.300  1.00 113.14 ? 69  ARG A CZ  1 
ATOM   509  N  NH1 . ARG A 1 69  ? -21.507 -41.937 2.944  1.00 111.36 ? 69  ARG A NH1 1 
ATOM   510  N  NH2 . ARG A 1 69  ? -22.193 -40.767 1.086  1.00 116.47 ? 69  ARG A NH2 1 
ATOM   511  N  N   . LYS A 1 70  ? -25.303 -42.632 8.718  1.00 94.78  ? 70  LYS A N   1 
ATOM   512  C  CA  . LYS A 1 70  ? -25.276 -43.211 10.063 1.00 92.84  ? 70  LYS A CA  1 
ATOM   513  C  C   . LYS A 1 70  ? -23.845 -43.141 10.603 1.00 88.63  ? 70  LYS A C   1 
ATOM   514  O  O   . LYS A 1 70  ? -22.885 -43.124 9.838  1.00 87.93  ? 70  LYS A O   1 
ATOM   515  C  CB  . LYS A 1 70  ? -25.757 -44.676 10.055 1.00 95.71  ? 70  LYS A CB  1 
ATOM   516  C  CG  . LYS A 1 70  ? -27.013 -45.015 9.164  1.00 101.68 ? 70  LYS A CG  1 
ATOM   517  C  CD  . LYS A 1 70  ? -28.330 -45.296 9.965  1.00 105.67 ? 70  LYS A CD  1 
ATOM   518  C  CE  . LYS A 1 70  ? -29.114 -46.481 9.310  1.00 111.34 ? 70  LYS A CE  1 
ATOM   519  N  NZ  . LYS A 1 70  ? -30.530 -46.700 9.767  1.00 115.28 ? 70  LYS A NZ  1 
ATOM   520  N  N   . HIS A 1 71  ? -23.700 -43.108 11.922 1.00 85.91  ? 71  HIS A N   1 
ATOM   521  C  CA  . HIS A 1 71  ? -22.374 -42.980 12.534 1.00 82.57  ? 71  HIS A CA  1 
ATOM   522  C  C   . HIS A 1 71  ? -21.511 -44.176 12.139 1.00 82.83  ? 71  HIS A C   1 
ATOM   523  O  O   . HIS A 1 71  ? -22.024 -45.258 11.879 1.00 84.93  ? 71  HIS A O   1 
ATOM   524  C  CB  . HIS A 1 71  ? -22.488 -42.839 14.065 1.00 80.83  ? 71  HIS A CB  1 
ATOM   525  C  CG  . HIS A 1 71  ? -21.167 -42.803 14.777 1.00 77.78  ? 71  HIS A CG  1 
ATOM   526  N  ND1 . HIS A 1 71  ? -20.343 -41.701 14.779 1.00 75.73  ? 71  HIS A ND1 1 
ATOM   527  C  CD2 . HIS A 1 71  ? -20.538 -43.739 15.524 1.00 76.64  ? 71  HIS A CD2 1 
ATOM   528  C  CE1 . HIS A 1 71  ? -19.257 -41.967 15.483 1.00 73.91  ? 71  HIS A CE1 1 
ATOM   529  N  NE2 . HIS A 1 71  ? -19.351 -43.197 15.946 1.00 74.23  ? 71  HIS A NE2 1 
ATOM   530  N  N   . GLY A 1 72  ? -20.207 -43.967 12.060 1.00 81.11  ? 72  GLY A N   1 
ATOM   531  C  CA  . GLY A 1 72  ? -19.287 -45.055 11.816 1.00 81.89  ? 72  GLY A CA  1 
ATOM   532  C  C   . GLY A 1 72  ? -17.873 -44.730 12.249 1.00 80.17  ? 72  GLY A C   1 
ATOM   533  O  O   . GLY A 1 72  ? -17.604 -43.694 12.862 1.00 78.54  ? 72  GLY A O   1 
ATOM   534  N  N   . GLY A 1 73  ? -16.973 -45.654 11.960 1.00 81.37  ? 73  GLY A N   1 
ATOM   535  C  CA  . GLY A 1 73  ? -15.561 -45.477 12.233 1.00 80.37  ? 73  GLY A CA  1 
ATOM   536  C  C   . GLY A 1 73  ? -14.961 -44.718 11.090 1.00 81.09  ? 73  GLY A C   1 
ATOM   537  O  O   . GLY A 1 73  ? -15.576 -44.614 10.050 1.00 82.84  ? 73  GLY A O   1 
ATOM   538  N  N   . PRO A 1 74  ? -13.733 -44.212 11.258 1.00 80.48  ? 74  PRO A N   1 
ATOM   539  C  CA  . PRO A 1 74  ? -13.236 -43.275 10.267 1.00 81.02  ? 74  PRO A CA  1 
ATOM   540  C  C   . PRO A 1 74  ? -12.896 -43.948 8.964  1.00 84.19  ? 74  PRO A C   1 
ATOM   541  O  O   . PRO A 1 74  ? -13.071 -43.372 7.925  1.00 85.44  ? 74  PRO A O   1 
ATOM   542  C  CB  . PRO A 1 74  ? -11.988 -42.716 10.924 1.00 79.53  ? 74  PRO A CB  1 
ATOM   543  C  CG  . PRO A 1 74  ? -11.499 -43.812 11.782 1.00 79.96  ? 74  PRO A CG  1 
ATOM   544  C  CD  . PRO A 1 74  ? -12.665 -44.678 12.157 1.00 79.91  ? 74  PRO A CD  1 
ATOM   545  N  N   . LYS A 1 75  ? -12.438 -45.180 9.025  1.00 86.20  ? 75  LYS A N   1 
ATOM   546  C  CA  . LYS A 1 75  ? -12.124 -45.902 7.830  1.00 90.29  ? 75  LYS A CA  1 
ATOM   547  C  C   . LYS A 1 75  ? -13.357 -46.597 7.283  1.00 92.06  ? 75  LYS A C   1 
ATOM   548  O  O   . LYS A 1 75  ? -13.330 -47.079 6.167  1.00 95.32  ? 75  LYS A O   1 
ATOM   549  C  CB  . LYS A 1 75  ? -11.010 -46.886 8.109  1.00 92.03  ? 75  LYS A CB  1 
ATOM   550  C  CG  . LYS A 1 75  ? -9.684  -46.201 8.492  1.00 93.95  ? 75  LYS A CG  1 
ATOM   551  C  CD  . LYS A 1 75  ? -8.467  -47.168 8.442  1.00 100.25 ? 75  LYS A CD  1 
ATOM   552  C  CE  . LYS A 1 75  ? -8.844  -48.620 8.953  1.00 103.30 ? 75  LYS A CE  1 
ATOM   553  N  NZ  . LYS A 1 75  ? -7.760  -49.672 8.981  1.00 106.44 ? 75  LYS A NZ  1 
ATOM   554  N  N   . ASP A 1 76  ? -14.444 -46.647 8.054  1.00 90.50  ? 76  ASP A N   1 
ATOM   555  C  CA  . ASP A 1 76  ? -15.713 -47.190 7.549  1.00 92.67  ? 76  ASP A CA  1 
ATOM   556  C  C   . ASP A 1 76  ? -16.198 -46.339 6.380  1.00 94.26  ? 76  ASP A C   1 
ATOM   557  O  O   . ASP A 1 76  ? -15.778 -45.207 6.176  1.00 92.65  ? 76  ASP A O   1 
ATOM   558  C  CB  . ASP A 1 76  ? -16.783 -47.295 8.658  1.00 90.91  ? 76  ASP A CB  1 
ATOM   559  C  CG  . ASP A 1 76  ? -16.636 -48.576 9.493  1.00 92.09  ? 76  ASP A CG  1 
ATOM   560  O  OD1 . ASP A 1 76  ? -16.591 -49.652 8.866  1.00 96.60  ? 76  ASP A OD1 1 
ATOM   561  O  OD2 . ASP A 1 76  ? -16.560 -48.538 10.756 1.00 90.36  ? 76  ASP A OD2 1 
ATOM   562  N  N   . GLU A 1 77  ? -17.062 -46.914 5.577  1.00 97.87  ? 77  GLU A N   1 
ATOM   563  C  CA  . GLU A 1 77  ? -17.561 -46.203 4.435  1.00 100.48 ? 77  GLU A CA  1 
ATOM   564  C  C   . GLU A 1 77  ? -18.790 -45.405 4.850  1.00 98.48  ? 77  GLU A C   1 
ATOM   565  O  O   . GLU A 1 77  ? -18.832 -44.214 4.618  1.00 97.35  ? 77  GLU A O   1 
ATOM   566  C  CB  . GLU A 1 77  ? -17.893 -47.184 3.318  1.00 106.12 ? 77  GLU A CB  1 
ATOM   567  C  CG  . GLU A 1 77  ? -18.231 -46.481 1.987  1.00 112.25 ? 77  GLU A CG  1 
ATOM   568  C  CD  . GLU A 1 77  ? -19.520 -47.018 1.321  1.00 120.91 ? 77  GLU A CD  1 
ATOM   569  O  OE1 . GLU A 1 77  ? -19.508 -48.194 0.838  1.00 125.84 ? 77  GLU A OE1 1 
ATOM   570  O  OE2 . GLU A 1 77  ? -20.530 -46.250 1.295  1.00 123.71 ? 77  GLU A OE2 1 
ATOM   571  N  N   . GLU A 1 78  ? -19.785 -46.071 5.443  1.00 98.27  ? 78  GLU A N   1 
ATOM   572  C  CA  . GLU A 1 78  ? -20.930 -45.384 6.062  1.00 96.69  ? 78  GLU A CA  1 
ATOM   573  C  C   . GLU A 1 78  ? -20.458 -44.739 7.381  1.00 91.61  ? 78  GLU A C   1 
ATOM   574  O  O   . GLU A 1 78  ? -20.271 -45.422 8.407  1.00 89.90  ? 78  GLU A O   1 
ATOM   575  C  CB  . GLU A 1 78  ? -22.119 -46.347 6.296  1.00 99.09  ? 78  GLU A CB  1 
ATOM   576  C  CG  . GLU A 1 78  ? -23.413 -45.693 6.842  1.00 99.94  ? 78  GLU A CG  1 
ATOM   577  C  CD  . GLU A 1 78  ? -24.262 -44.988 5.773  1.00 105.02 ? 78  GLU A CD  1 
ATOM   578  O  OE1 . GLU A 1 78  ? -23.701 -44.650 4.698  1.00 108.13 ? 78  GLU A OE1 1 
ATOM   579  O  OE2 . GLU A 1 78  ? -25.489 -44.768 6.020  1.00 106.73 ? 78  GLU A OE2 1 
ATOM   580  N  N   . ARG A 1 79  ? -20.249 -43.421 7.321  1.00 89.16  ? 79  ARG A N   1 
ATOM   581  C  CA  . ARG A 1 79  ? -19.800 -42.616 8.461  1.00 84.94  ? 79  ARG A CA  1 
ATOM   582  C  C   . ARG A 1 79  ? -20.196 -41.145 8.383  1.00 83.64  ? 79  ARG A C   1 
ATOM   583  O  O   . ARG A 1 79  ? -20.496 -40.600 7.320  1.00 85.66  ? 79  ARG A O   1 
ATOM   584  C  CB  . ARG A 1 79  ? -18.280 -42.650 8.559  1.00 83.46  ? 79  ARG A CB  1 
ATOM   585  C  CG  . ARG A 1 79  ? -17.576 -41.972 7.391  1.00 85.11  ? 79  ARG A CG  1 
ATOM   586  C  CD  . ARG A 1 79  ? -16.078 -41.799 7.601  1.00 84.45  ? 79  ARG A CD  1 
ATOM   587  N  NE  . ARG A 1 79  ? -15.739 -40.567 8.323  1.00 82.36  ? 79  ARG A NE  1 
ATOM   588  C  CZ  . ARG A 1 79  ? -14.523 -40.003 8.353  1.00 81.56  ? 79  ARG A CZ  1 
ATOM   589  N  NH1 . ARG A 1 79  ? -13.504 -40.539 7.693  1.00 82.60  ? 79  ARG A NH1 1 
ATOM   590  N  NH2 . ARG A 1 79  ? -14.317 -38.888 9.046  1.00 80.03  ? 79  ARG A NH2 1 
ATOM   591  N  N   . HIS A 1 80  ? -20.153 -40.489 9.529  1.00 80.36  ? 80  HIS A N   1 
ATOM   592  C  CA  . HIS A 1 80  ? -20.318 -39.056 9.561  1.00 78.85  ? 80  HIS A CA  1 
ATOM   593  C  C   . HIS A 1 80  ? -19.013 -38.452 9.112  1.00 77.14  ? 80  HIS A C   1 
ATOM   594  O  O   . HIS A 1 80  ? -17.947 -38.962 9.433  1.00 75.74  ? 80  HIS A O   1 
ATOM   595  C  CB  . HIS A 1 80  ? -20.662 -38.570 10.969 1.00 76.79  ? 80  HIS A CB  1 
ATOM   596  C  CG  . HIS A 1 80  ? -21.952 -39.099 11.495 1.00 77.96  ? 80  HIS A CG  1 
ATOM   597  N  ND1 . HIS A 1 80  ? -22.258 -39.099 12.834 1.00 77.46  ? 80  HIS A ND1 1 
ATOM   598  C  CD2 . HIS A 1 80  ? -23.022 -39.625 10.861 1.00 81.31  ? 80  HIS A CD2 1 
ATOM   599  C  CE1 . HIS A 1 80  ? -23.469 -39.597 13.003 1.00 80.34  ? 80  HIS A CE1 1 
ATOM   600  N  NE2 . HIS A 1 80  ? -23.952 -39.928 11.820 1.00 82.56  ? 80  HIS A NE2 1 
ATOM   601  N  N   . VAL A 1 81  ? -19.095 -37.360 8.372  1.00 77.30  ? 81  VAL A N   1 
ATOM   602  C  CA  . VAL A 1 81  ? -17.890 -36.607 8.022  1.00 75.89  ? 81  VAL A CA  1 
ATOM   603  C  C   . VAL A 1 81  ? -17.044 -36.343 9.245  1.00 72.39  ? 81  VAL A C   1 
ATOM   604  O  O   . VAL A 1 81  ? -15.843 -36.374 9.166  1.00 71.45  ? 81  VAL A O   1 
ATOM   605  C  CB  . VAL A 1 81  ? -18.213 -35.269 7.318  1.00 76.97  ? 81  VAL A CB  1 
ATOM   606  C  CG1 . VAL A 1 81  ? -16.962 -34.498 7.063  1.00 75.27  ? 81  VAL A CG1 1 
ATOM   607  C  CG2 . VAL A 1 81  ? -18.948 -35.545 6.016  1.00 80.87  ? 81  VAL A CG2 1 
ATOM   608  N  N   . GLY A 1 82  ? -17.670 -36.109 10.384 1.00 70.77  ? 82  GLY A N   1 
ATOM   609  C  CA  . GLY A 1 82  ? -16.934 -35.774 11.585 1.00 68.56  ? 82  GLY A CA  1 
ATOM   610  C  C   . GLY A 1 82  ? -16.413 -36.926 12.402 1.00 67.57  ? 82  GLY A C   1 
ATOM   611  O  O   . GLY A 1 82  ? -15.892 -36.673 13.471 1.00 65.93  ? 82  GLY A O   1 
ATOM   612  N  N   . ASP A 1 83  ? -16.551 -38.171 11.937 1.00 68.87  ? 83  ASP A N   1 
ATOM   613  C  CA  . ASP A 1 83  ? -16.210 -39.333 12.763 1.00 68.57  ? 83  ASP A CA  1 
ATOM   614  C  C   . ASP A 1 83  ? -14.760 -39.697 12.603 1.00 68.40  ? 83  ASP A C   1 
ATOM   615  O  O   . ASP A 1 83  ? -14.420 -40.392 11.696 1.00 70.23  ? 83  ASP A O   1 
ATOM   616  C  CB  . ASP A 1 83  ? -17.043 -40.562 12.406 1.00 70.21  ? 83  ASP A CB  1 
ATOM   617  C  CG  . ASP A 1 83  ? -18.510 -40.385 12.679 1.00 71.22  ? 83  ASP A CG  1 
ATOM   618  O  OD1 . ASP A 1 83  ? -18.904 -39.646 13.585 1.00 70.23  ? 83  ASP A OD1 1 
ATOM   619  O  OD2 . ASP A 1 83  ? -19.312 -41.012 11.992 1.00 73.68  ? 83  ASP A OD2 1 
ATOM   620  N  N   . LEU A 1 84  ? -13.899 -39.249 13.500 1.00 67.19  ? 84  LEU A N   1 
ATOM   621  C  CA  . LEU A 1 84  ? -12.484 -39.586 13.430 1.00 67.40  ? 84  LEU A CA  1 
ATOM   622  C  C   . LEU A 1 84  ? -12.141 -40.751 14.334 1.00 67.46  ? 84  LEU A C   1 
ATOM   623  O  O   . LEU A 1 84  ? -10.997 -40.967 14.686 1.00 67.30  ? 84  LEU A O   1 
ATOM   624  C  CB  . LEU A 1 84  ? -11.651 -38.358 13.780 1.00 66.47  ? 84  LEU A CB  1 
ATOM   625  C  CG  . LEU A 1 84  ? -11.913 -37.169 12.850 1.00 66.54  ? 84  LEU A CG  1 
ATOM   626  C  CD1 . LEU A 1 84  ? -11.083 -36.020 13.283 1.00 64.45  ? 84  LEU A CD1 1 
ATOM   627  C  CD2 . LEU A 1 84  ? -11.651 -37.486 11.366 1.00 68.12  ? 84  LEU A CD2 1 
ATOM   628  N  N   . GLY A 1 85  ? -13.148 -41.514 14.718 1.00 68.05  ? 85  GLY A N   1 
ATOM   629  C  CA  . GLY A 1 85  ? -12.927 -42.639 15.603 1.00 68.51  ? 85  GLY A CA  1 
ATOM   630  C  C   . GLY A 1 85  ? -12.305 -42.282 16.942 1.00 67.29  ? 85  GLY A C   1 
ATOM   631  O  O   . GLY A 1 85  ? -12.807 -41.419 17.630 1.00 66.37  ? 85  GLY A O   1 
ATOM   632  N  N   . ASN A 1 86  ? -11.219 -42.950 17.311 1.00 67.80  ? 86  ASN A N   1 
ATOM   633  C  CA  . ASN A 1 86  ? -10.701 -42.864 18.662 1.00 67.58  ? 86  ASN A CA  1 
ATOM   634  C  C   . ASN A 1 86  ? -9.302  -42.375 18.730 1.00 67.62  ? 86  ASN A C   1 
ATOM   635  O  O   . ASN A 1 86  ? -8.592  -42.351 17.731 1.00 68.31  ? 86  ASN A O   1 
ATOM   636  C  CB  . ASN A 1 86  ? -10.729 -44.224 19.322 1.00 69.00  ? 86  ASN A CB  1 
ATOM   637  C  CG  . ASN A 1 86  ? -12.117 -44.691 19.610 1.00 69.78  ? 86  ASN A CG  1 
ATOM   638  O  OD1 . ASN A 1 86  ? -12.771 -44.225 20.537 1.00 71.63  ? 86  ASN A OD1 1 
ATOM   639  N  ND2 . ASN A 1 86  ? -12.581 -45.626 18.826 1.00 72.00  ? 86  ASN A ND2 1 
ATOM   640  N  N   . VAL A 1 87  ? -8.933  -41.973 19.936 1.00 67.28  ? 87  VAL A N   1 
ATOM   641  C  CA  . VAL A 1 87  ? -7.574  -41.631 20.281 1.00 68.18  ? 87  VAL A CA  1 
ATOM   642  C  C   . VAL A 1 87  ? -7.223  -42.382 21.540 1.00 69.86  ? 87  VAL A C   1 
ATOM   643  O  O   . VAL A 1 87  ? -8.105  -42.771 22.278 1.00 69.77  ? 87  VAL A O   1 
ATOM   644  C  CB  . VAL A 1 87  ? -7.414  -40.137 20.528 1.00 67.12  ? 87  VAL A CB  1 
ATOM   645  C  CG1 . VAL A 1 87  ? -7.955  -39.368 19.364 1.00 64.99  ? 87  VAL A CG1 1 
ATOM   646  C  CG2 . VAL A 1 87  ? -8.112  -39.729 21.777 1.00 66.40  ? 87  VAL A CG2 1 
ATOM   647  N  N   . THR A 1 88  ? -5.941  -42.578 21.796 1.00 72.01  ? 88  THR A N   1 
ATOM   648  C  CA  . THR A 1 88  ? -5.523  -43.496 22.834 1.00 74.34  ? 88  THR A CA  1 
ATOM   649  C  C   . THR A 1 88  ? -4.702  -42.804 23.905 1.00 75.76  ? 88  THR A C   1 
ATOM   650  O  O   . THR A 1 88  ? -3.729  -42.134 23.603 1.00 76.52  ? 88  THR A O   1 
ATOM   651  C  CB  . THR A 1 88  ? -4.726  -44.649 22.218 1.00 76.38  ? 88  THR A CB  1 
ATOM   652  O  OG1 . THR A 1 88  ? -5.610  -45.476 21.453 1.00 76.00  ? 88  THR A OG1 1 
ATOM   653  C  CG2 . THR A 1 88  ? -4.050  -45.504 23.284 1.00 79.48  ? 88  THR A CG2 1 
ATOM   654  N  N   . ALA A 1 89  ? -5.088  -43.004 25.159 1.00 76.81  ? 89  ALA A N   1 
ATOM   655  C  CA  . ALA A 1 89  ? -4.422  -42.388 26.279 1.00 78.84  ? 89  ALA A CA  1 
ATOM   656  C  C   . ALA A 1 89  ? -3.425  -43.340 26.893 1.00 82.55  ? 89  ALA A C   1 
ATOM   657  O  O   . ALA A 1 89  ? -3.723  -44.515 27.076 1.00 83.29  ? 89  ALA A O   1 
ATOM   658  C  CB  . ALA A 1 89  ? -5.420  -41.999 27.305 1.00 78.55  ? 89  ALA A CB  1 
ATOM   659  N  N   . ASP A 1 90  ? -2.232  -42.805 27.166 1.00 85.51  ? 90  ASP A N   1 
ATOM   660  C  CA  . ASP A 1 90  ? -1.217  -43.349 28.097 1.00 89.98  ? 90  ASP A CA  1 
ATOM   661  C  C   . ASP A 1 90  ? -1.737  -44.034 29.357 1.00 92.20  ? 90  ASP A C   1 
ATOM   662  O  O   . ASP A 1 90  ? -2.927  -43.928 29.721 1.00 90.58  ? 90  ASP A O   1 
ATOM   663  C  CB  . ASP A 1 90  ? -0.395  -42.182 28.665 1.00 91.82  ? 90  ASP A CB  1 
ATOM   664  C  CG  . ASP A 1 90  ? 0.943   -42.025 28.033 1.00 95.14  ? 90  ASP A CG  1 
ATOM   665  O  OD1 . ASP A 1 90  ? 1.211   -42.727 27.060 1.00 97.41  ? 90  ASP A OD1 1 
ATOM   666  O  OD2 . ASP A 1 90  ? 1.737   -41.186 28.512 1.00 99.05  ? 90  ASP A OD2 1 
ATOM   667  N  N   . LYS A 1 91  ? -0.796  -44.700 30.037 1.00 96.50  ? 91  LYS A N   1 
ATOM   668  C  CA  . LYS A 1 91  ? -0.879  -44.940 31.486 1.00 99.87  ? 91  LYS A CA  1 
ATOM   669  C  C   . LYS A 1 91  ? -1.149  -43.611 32.185 1.00 99.42  ? 91  LYS A C   1 
ATOM   670  O  O   . LYS A 1 91  ? -2.040  -43.509 33.025 1.00 99.58  ? 91  LYS A O   1 
ATOM   671  C  CB  . LYS A 1 91  ? 0.468   -45.477 32.018 1.00 104.80 ? 91  LYS A CB  1 
ATOM   672  C  CG  . LYS A 1 91  ? 0.564   -46.996 32.228 1.00 108.92 ? 91  LYS A CG  1 
ATOM   673  C  CD  . LYS A 1 91  ? 0.010   -47.438 33.629 1.00 113.85 ? 91  LYS A CD  1 
ATOM   674  C  CE  . LYS A 1 91  ? 0.682   -48.732 34.143 1.00 119.11 ? 91  LYS A CE  1 
ATOM   675  N  NZ  . LYS A 1 91  ? -0.290  -49.660 34.810 1.00 120.74 ? 91  LYS A NZ  1 
ATOM   676  N  N   . ASP A 1 92  ? -0.324  -42.624 31.823 1.00 99.35  ? 92  ASP A N   1 
ATOM   677  C  CA  . ASP A 1 92  ? -0.315  -41.268 32.371 1.00 99.77  ? 92  ASP A CA  1 
ATOM   678  C  C   . ASP A 1 92  ? -1.425  -40.376 31.865 1.00 95.79  ? 92  ASP A C   1 
ATOM   679  O  O   . ASP A 1 92  ? -1.437  -39.193 32.155 1.00 96.10  ? 92  ASP A O   1 
ATOM   680  C  CB  . ASP A 1 92  ? 0.999   -40.592 31.993 1.00 101.54 ? 92  ASP A CB  1 
ATOM   681  C  CG  . ASP A 1 92  ? 2.216   -41.349 32.496 1.00 107.15 ? 92  ASP A CG  1 
ATOM   682  O  OD1 . ASP A 1 92  ? 3.302   -40.753 32.532 1.00 111.41 ? 92  ASP A OD1 1 
ATOM   683  O  OD2 . ASP A 1 92  ? 2.112   -42.543 32.854 1.00 110.41 ? 92  ASP A OD2 1 
ATOM   684  N  N   . GLY A 1 93  ? -2.338  -40.913 31.071 1.00 92.48  ? 93  GLY A N   1 
ATOM   685  C  CA  . GLY A 1 93  ? -3.478  -40.131 30.600 1.00 89.27  ? 93  GLY A CA  1 
ATOM   686  C  C   . GLY A 1 93  ? -3.169  -39.055 29.582 1.00 87.08  ? 93  GLY A C   1 
ATOM   687  O  O   . GLY A 1 93  ? -3.963  -38.156 29.382 1.00 85.32  ? 93  GLY A O   1 
ATOM   688  N  N   . VAL A 1 94  ? -1.993  -39.124 28.982 1.00 87.80  ? 94  VAL A N   1 
ATOM   689  C  CA  . VAL A 1 94  ? -1.658  -38.345 27.790 1.00 86.13  ? 94  VAL A CA  1 
ATOM   690  C  C   . VAL A 1 94  ? -1.939  -39.146 26.531 1.00 84.26  ? 94  VAL A C   1 
ATOM   691  O  O   . VAL A 1 94  ? -1.461  -40.264 26.405 1.00 85.75  ? 94  VAL A O   1 
ATOM   692  C  CB  . VAL A 1 94  ? -0.162  -38.003 27.751 1.00 88.75  ? 94  VAL A CB  1 
ATOM   693  C  CG1 . VAL A 1 94  ? 0.199   -37.384 26.435 1.00 86.80  ? 94  VAL A CG1 1 
ATOM   694  C  CG2 . VAL A 1 94  ? 0.216   -37.096 28.925 1.00 91.65  ? 94  VAL A CG2 1 
ATOM   695  N  N   . ALA A 1 95  ? -2.691  -38.569 25.596 1.00 81.80  ? 95  ALA A N   1 
ATOM   696  C  CA  . ALA A 1 95  ? -2.948  -39.198 24.304 1.00 80.41  ? 95  ALA A CA  1 
ATOM   697  C  C   . ALA A 1 95  ? -2.195  -38.446 23.231 1.00 80.83  ? 95  ALA A C   1 
ATOM   698  O  O   . ALA A 1 95  ? -2.429  -37.268 23.051 1.00 79.98  ? 95  ALA A O   1 
ATOM   699  C  CB  . ALA A 1 95  ? -4.415  -39.180 23.999 1.00 77.78  ? 95  ALA A CB  1 
ATOM   700  N  N   . ASP A 1 96  ? -1.292  -39.121 22.521 1.00 82.84  ? 96  ASP A N   1 
ATOM   701  C  CA  . ASP A 1 96  ? -0.505  -38.477 21.469 1.00 84.07  ? 96  ASP A CA  1 
ATOM   702  C  C   . ASP A 1 96  ? -1.198  -38.701 20.166 1.00 81.89  ? 96  ASP A C   1 
ATOM   703  O  O   . ASP A 1 96  ? -1.010  -39.715 19.537 1.00 83.26  ? 96  ASP A O   1 
ATOM   704  C  CB  . ASP A 1 96  ? 0.921   -39.039 21.399 1.00 87.94  ? 96  ASP A CB  1 
ATOM   705  C  CG  . ASP A 1 96  ? 1.872   -38.373 22.420 1.00 92.72  ? 96  ASP A CG  1 
ATOM   706  O  OD1 . ASP A 1 96  ? 1.802   -37.127 22.569 1.00 94.12  ? 96  ASP A OD1 1 
ATOM   707  O  OD2 . ASP A 1 96  ? 2.687   -39.082 23.081 1.00 98.10  ? 96  ASP A OD2 1 
ATOM   708  N  N   . VAL A 1 97  ? -2.003  -37.739 19.761 1.00 79.22  ? 97  VAL A N   1 
ATOM   709  C  CA  . VAL A 1 97  ? -2.830  -37.892 18.585 1.00 77.22  ? 97  VAL A CA  1 
ATOM   710  C  C   . VAL A 1 97  ? -2.028  -37.806 17.306 1.00 78.13  ? 97  VAL A C   1 
ATOM   711  O  O   . VAL A 1 97  ? -1.127  -36.994 17.210 1.00 79.49  ? 97  VAL A O   1 
ATOM   712  C  CB  . VAL A 1 97  ? -3.856  -36.808 18.552 1.00 75.09  ? 97  VAL A CB  1 
ATOM   713  C  CG1 . VAL A 1 97  ? -4.555  -36.815 17.241 1.00 74.83  ? 97  VAL A CG1 1 
ATOM   714  C  CG2 . VAL A 1 97  ? -4.820  -37.023 19.639 1.00 74.38  ? 97  VAL A CG2 1 
ATOM   715  N  N   . SER A 1 98  ? -2.358  -38.643 16.327 1.00 77.69  ? 98  SER A N   1 
ATOM   716  C  CA  . SER A 1 98  ? -1.775  -38.540 14.989 1.00 79.08  ? 98  SER A CA  1 
ATOM   717  C  C   . SER A 1 98  ? -2.577  -39.341 13.949 1.00 78.75  ? 98  SER A C   1 
ATOM   718  O  O   . SER A 1 98  ? -2.627  -40.553 13.996 1.00 79.27  ? 98  SER A O   1 
ATOM   719  C  CB  . SER A 1 98  ? -0.322  -38.988 15.011 1.00 82.05  ? 98  SER A CB  1 
ATOM   720  O  OG  . SER A 1 98  ? 0.285   -38.757 13.772 1.00 84.15  ? 98  SER A OG  1 
ATOM   721  N  N   . ILE A 1 99  ? -3.178  -38.643 12.994 1.00 78.20  ? 99  ILE A N   1 
ATOM   722  C  CA  . ILE A 1 99  ? -4.201  -39.212 12.128 1.00 78.02  ? 99  ILE A CA  1 
ATOM   723  C  C   . ILE A 1 99  ? -4.143  -38.586 10.739 1.00 80.29  ? 99  ILE A C   1 
ATOM   724  O  O   . ILE A 1 99  ? -3.993  -37.371 10.616 1.00 80.53  ? 99  ILE A O   1 
ATOM   725  C  CB  . ILE A 1 99  ? -5.610  -38.859 12.660 1.00 74.85  ? 99  ILE A CB  1 
ATOM   726  C  CG1 . ILE A 1 99  ? -5.834  -39.375 14.063 1.00 72.55  ? 99  ILE A CG1 1 
ATOM   727  C  CG2 . ILE A 1 99  ? -6.671  -39.410 11.751 1.00 74.98  ? 99  ILE A CG2 1 
ATOM   728  C  CD1 . ILE A 1 99  ? -7.270  -39.439 14.443 1.00 69.30  ? 99  ILE A CD1 1 
ATOM   729  N  N   . GLU A 1 100 ? -4.292  -39.391 9.698  1.00 82.83  ? 100 GLU A N   1 
ATOM   730  C  CA  . GLU A 1 100 ? -4.595  -38.845 8.386  1.00 84.96  ? 100 GLU A CA  1 
ATOM   731  C  C   . GLU A 1 100 ? -6.036  -39.120 8.137  1.00 83.50  ? 100 GLU A C   1 
ATOM   732  O  O   . GLU A 1 100 ? -6.546  -40.132 8.562  1.00 83.25  ? 100 GLU A O   1 
ATOM   733  C  CB  . GLU A 1 100 ? -3.776  -39.524 7.289  1.00 89.55  ? 100 GLU A CB  1 
ATOM   734  C  CG  . GLU A 1 100 ? -2.331  -39.012 7.142  1.00 94.16  ? 100 GLU A CG  1 
ATOM   735  C  CD  . GLU A 1 100 ? -1.825  -39.099 5.702  1.00 101.73 ? 100 GLU A CD  1 
ATOM   736  O  OE1 . GLU A 1 100 ? -2.643  -39.392 4.803  1.00 104.41 ? 100 GLU A OE1 1 
ATOM   737  O  OE2 . GLU A 1 100 ? -0.616  -38.862 5.473  1.00 106.83 ? 100 GLU A OE2 1 
ATOM   738  N  N   . ASP A 1 101 ? -6.700  -38.238 7.430  1.00 83.34  ? 101 ASP A N   1 
ATOM   739  C  CA  . ASP A 1 101 ? -8.076  -38.498 7.058  1.00 83.22  ? 101 ASP A CA  1 
ATOM   740  C  C   . ASP A 1 101 ? -8.439  -37.636 5.872  1.00 84.77  ? 101 ASP A C   1 
ATOM   741  O  O   . ASP A 1 101 ? -8.035  -36.469 5.821  1.00 84.66  ? 101 ASP A O   1 
ATOM   742  C  CB  . ASP A 1 101 ? -9.000  -38.140 8.209  1.00 80.21  ? 101 ASP A CB  1 
ATOM   743  C  CG  . ASP A 1 101 ? -10.429 -38.579 7.969  1.00 81.48  ? 101 ASP A CG  1 
ATOM   744  O  OD1 . ASP A 1 101 ? -10.749 -39.707 8.355  1.00 83.30  ? 101 ASP A OD1 1 
ATOM   745  O  OD2 . ASP A 1 101 ? -11.235 -37.805 7.404  1.00 83.60  ? 101 ASP A OD2 1 
ATOM   746  N  N   . SER A 1 102 ? -9.211  -38.181 4.933  1.00 86.43  ? 102 SER A N   1 
ATOM   747  C  CA  . SER A 1 102 ? -9.523  -37.438 3.716  1.00 88.74  ? 102 SER A CA  1 
ATOM   748  C  C   . SER A 1 102 ? -11.003 -37.316 3.461  1.00 88.18  ? 102 SER A C   1 
ATOM   749  O  O   . SER A 1 102 ? -11.413 -36.934 2.375  1.00 90.96  ? 102 SER A O   1 
ATOM   750  C  CB  . SER A 1 102 ? -8.819  -38.092 2.535  1.00 93.13  ? 102 SER A CB  1 
ATOM   751  O  OG  . SER A 1 102 ? -8.587  -39.447 2.858  1.00 94.48  ? 102 SER A OG  1 
ATOM   752  N  N   . VAL A 1 103 ? -11.809 -37.630 4.460  1.00 85.07  ? 103 VAL A N   1 
ATOM   753  C  CA  . VAL A 1 103 ? -13.218 -37.266 4.405  1.00 84.68  ? 103 VAL A CA  1 
ATOM   754  C  C   . VAL A 1 103 ? -13.405 -35.802 4.845  1.00 82.78  ? 103 VAL A C   1 
ATOM   755  O  O   . VAL A 1 103 ? -14.168 -35.050 4.223  1.00 84.37  ? 103 VAL A O   1 
ATOM   756  C  CB  . VAL A 1 103 ? -14.084 -38.166 5.273  1.00 82.93  ? 103 VAL A CB  1 
ATOM   757  C  CG1 . VAL A 1 103 ? -15.444 -37.523 5.498  1.00 82.18  ? 103 VAL A CG1 1 
ATOM   758  C  CG2 . VAL A 1 103 ? -14.258 -39.509 4.610  1.00 85.67  ? 103 VAL A CG2 1 
ATOM   759  N  N   . ILE A 1 104 ? -12.725 -35.402 5.915  1.00 79.64  ? 104 ILE A N   1 
ATOM   760  C  CA  . ILE A 1 104 ? -12.755 -34.015 6.329  1.00 78.17  ? 104 ILE A CA  1 
ATOM   761  C  C   . ILE A 1 104 ? -11.853 -33.196 5.420  1.00 80.64  ? 104 ILE A C   1 
ATOM   762  O  O   . ILE A 1 104 ? -11.010 -33.755 4.690  1.00 82.73  ? 104 ILE A O   1 
ATOM   763  C  CB  . ILE A 1 104 ? -12.310 -33.820 7.778  1.00 75.00  ? 104 ILE A CB  1 
ATOM   764  C  CG1 . ILE A 1 104 ? -10.848 -34.222 7.977  1.00 74.65  ? 104 ILE A CG1 1 
ATOM   765  C  CG2 . ILE A 1 104 ? -13.200 -34.559 8.681  1.00 73.03  ? 104 ILE A CG2 1 
ATOM   766  C  CD1 . ILE A 1 104 ? -10.435 -34.196 9.399  1.00 71.64  ? 104 ILE A CD1 1 
ATOM   767  N  N   . SER A 1 105 ? -12.039 -31.874 5.478  1.00 80.72  ? 105 SER A N   1 
ATOM   768  C  CA  . SER A 1 105 ? -11.326 -30.919 4.630  1.00 83.25  ? 105 SER A CA  1 
ATOM   769  C  C   . SER A 1 105 ? -11.252 -29.610 5.389  1.00 81.84  ? 105 SER A C   1 
ATOM   770  O  O   . SER A 1 105 ? -12.079 -29.355 6.241  1.00 79.64  ? 105 SER A O   1 
ATOM   771  C  CB  . SER A 1 105 ? -12.089 -30.724 3.286  1.00 86.82  ? 105 SER A CB  1 
ATOM   772  O  OG  . SER A 1 105 ? -11.299 -30.158 2.235  1.00 89.82  ? 105 SER A OG  1 
ATOM   773  N  N   . LEU A 1 106 ? -10.263 -28.782 5.072  1.00 83.75  ? 106 LEU A N   1 
ATOM   774  C  CA  . LEU A 1 106 ? -10.192 -27.406 5.594  1.00 83.61  ? 106 LEU A CA  1 
ATOM   775  C  C   . LEU A 1 106 ? -10.789 -26.388 4.622  1.00 87.19  ? 106 LEU A C   1 
ATOM   776  O  O   . LEU A 1 106 ? -10.992 -25.239 4.999  1.00 87.09  ? 106 LEU A O   1 
ATOM   777  C  CB  . LEU A 1 106 ? -8.748  -27.030 5.922  1.00 83.43  ? 106 LEU A CB  1 
ATOM   778  C  CG  . LEU A 1 106 ? -8.051  -27.930 6.941  1.00 80.11  ? 106 LEU A CG  1 
ATOM   779  C  CD1 . LEU A 1 106 ? -6.896  -27.247 7.629  1.00 78.78  ? 106 LEU A CD1 1 
ATOM   780  C  CD2 . LEU A 1 106 ? -9.026  -28.349 7.950  1.00 76.49  ? 106 LEU A CD2 1 
ATOM   781  N  N   . SER A 1 107 ? -11.057 -26.830 3.386  1.00 91.05  ? 107 SER A N   1 
ATOM   782  C  CA  . SER A 1 107 ? -11.769 -26.065 2.366  1.00 94.70  ? 107 SER A CA  1 
ATOM   783  C  C   . SER A 1 107 ? -12.916 -26.919 1.814  1.00 96.58  ? 107 SER A C   1 
ATOM   784  O  O   . SER A 1 107 ? -13.058 -28.089 2.158  1.00 95.46  ? 107 SER A O   1 
ATOM   785  C  CB  . SER A 1 107 ? -10.801 -25.710 1.242  1.00 98.27  ? 107 SER A CB  1 
ATOM   786  O  OG  . SER A 1 107 ? -10.096 -26.868 0.815  1.00 99.19  ? 107 SER A OG  1 
ATOM   787  N  N   . GLY A 1 108 ? -13.729 -26.359 0.934  1.00 100.42 ? 108 GLY A N   1 
ATOM   788  C  CA  . GLY A 1 108 ? -14.854 -27.120 0.379  1.00 102.65 ? 108 GLY A CA  1 
ATOM   789  C  C   . GLY A 1 108 ? -16.015 -27.170 1.353  1.00 100.59 ? 108 GLY A C   1 
ATOM   790  O  O   . GLY A 1 108 ? -16.029 -26.446 2.352  1.00 98.20  ? 108 GLY A O   1 
ATOM   791  N  N   . ASP A 1 109 ? -17.005 -27.999 1.056  1.00 102.14 ? 109 ASP A N   1 
ATOM   792  C  CA  . ASP A 1 109 ? -18.237 -28.022 1.890  1.00 101.29 ? 109 ASP A CA  1 
ATOM   793  C  C   . ASP A 1 109 ? -18.220 -29.158 2.924  1.00 97.57  ? 109 ASP A C   1 
ATOM   794  O  O   . ASP A 1 109 ? -19.233 -29.423 3.619  1.00 96.25  ? 109 ASP A O   1 
ATOM   795  C  CB  . ASP A 1 109 ? -19.540 -28.049 1.042  1.00 105.53 ? 109 ASP A CB  1 
ATOM   796  C  CG  . ASP A 1 109 ? -19.409 -28.910 -0.243 1.00 110.78 ? 109 ASP A CG  1 
ATOM   797  O  OD1 . ASP A 1 109 ? -19.410 -28.308 -1.346 1.00 115.55 ? 109 ASP A OD1 1 
ATOM   798  O  OD2 . ASP A 1 109 ? -19.282 -30.168 -0.152 1.00 112.08 ? 109 ASP A OD2 1 
ATOM   799  N  N   . HIS A 1 110 ? -17.066 -29.828 3.003  1.00 95.69  ? 110 HIS A N   1 
ATOM   800  C  CA  . HIS A 1 110 ? -16.713 -30.622 4.182  1.00 91.84  ? 110 HIS A CA  1 
ATOM   801  C  C   . HIS A 1 110 ? -15.795 -29.796 5.116  1.00 87.86  ? 110 HIS A C   1 
ATOM   802  O  O   . HIS A 1 110 ? -15.167 -30.336 6.012  1.00 85.23  ? 110 HIS A O   1 
ATOM   803  C  CB  . HIS A 1 110 ? -16.040 -31.928 3.745  1.00 92.88  ? 110 HIS A CB  1 
ATOM   804  C  CG  . HIS A 1 110 ? -16.953 -32.865 3.003  1.00 97.75  ? 110 HIS A CG  1 
ATOM   805  N  ND1 . HIS A 1 110 ? -16.635 -34.194 2.799  1.00 100.24 ? 110 HIS A ND1 1 
ATOM   806  C  CD2 . HIS A 1 110 ? -18.172 -32.678 2.434  1.00 101.97 ? 110 HIS A CD2 1 
ATOM   807  C  CE1 . HIS A 1 110 ? -17.610 -34.781 2.126  1.00 103.81 ? 110 HIS A CE1 1 
ATOM   808  N  NE2 . HIS A 1 110 ? -18.557 -33.883 1.894  1.00 105.16 ? 110 HIS A NE2 1 
ATOM   809  N  N   . CYS A 1 111 ? -15.712 -28.485 4.873  1.00 87.26  ? 111 CYS A N   1 
ATOM   810  C  CA  . CYS A 1 111 ? -14.831 -27.593 5.621  1.00 84.02  ? 111 CYS A CA  1 
ATOM   811  C  C   . CYS A 1 111 ? -15.262 -27.726 7.059  1.00 80.27  ? 111 CYS A C   1 
ATOM   812  O  O   . CYS A 1 111 ? -16.443 -27.655 7.321  1.00 80.43  ? 111 CYS A O   1 
ATOM   813  C  CB  . CYS A 1 111 ? -14.963 -26.160 5.073  1.00 85.87  ? 111 CYS A CB  1 
ATOM   814  S  SG  . CYS A 1 111 ? -14.179 -24.871 5.946  1.00 82.96  ? 111 CYS A SG  1 
ATOM   815  N  N   . ILE A 1 112 ? -14.320 -28.000 7.961  1.00 76.77  ? 112 ILE A N   1 
ATOM   816  C  CA  . ILE A 1 112 ? -14.609 -28.163 9.384  1.00 73.40  ? 112 ILE A CA  1 
ATOM   817  C  C   . ILE A 1 112 ? -14.174 -26.966 10.208 1.00 72.51  ? 112 ILE A C   1 
ATOM   818  O  O   . ILE A 1 112 ? -14.283 -26.955 11.422 1.00 71.11  ? 112 ILE A O   1 
ATOM   819  C  CB  . ILE A 1 112 ? -13.935 -29.418 9.967  1.00 71.51  ? 112 ILE A CB  1 
ATOM   820  C  CG1 . ILE A 1 112 ? -12.414 -29.307 9.983  1.00 70.14  ? 112 ILE A CG1 1 
ATOM   821  C  CG2 . ILE A 1 112 ? -14.330 -30.630 9.192  1.00 72.58  ? 112 ILE A CG2 1 
ATOM   822  C  CD1 . ILE A 1 112 ? -11.766 -30.437 10.701 1.00 66.52  ? 112 ILE A CD1 1 
ATOM   823  N  N   . ILE A 1 113 ? -13.674 -25.945 9.550  1.00 73.59  ? 113 ILE A N   1 
ATOM   824  C  CA  . ILE A 1 113 ? -13.235 -24.763 10.245 1.00 73.11  ? 113 ILE A CA  1 
ATOM   825  C  C   . ILE A 1 113 ? -14.440 -24.089 10.819 1.00 72.89  ? 113 ILE A C   1 
ATOM   826  O  O   . ILE A 1 113 ? -15.389 -23.839 10.128 1.00 74.25  ? 113 ILE A O   1 
ATOM   827  C  CB  . ILE A 1 113 ? -12.505 -23.824 9.300  1.00 75.15  ? 113 ILE A CB  1 
ATOM   828  C  CG1 . ILE A 1 113 ? -11.084 -24.330 9.111  1.00 75.05  ? 113 ILE A CG1 1 
ATOM   829  C  CG2 . ILE A 1 113 ? -12.489 -22.433 9.856  1.00 75.87  ? 113 ILE A CG2 1 
ATOM   830  C  CD1 . ILE A 1 113 ? -10.343 -23.609 8.074  1.00 78.94  ? 113 ILE A CD1 1 
ATOM   831  N  N   . GLY A 1 114 ? -14.404 -23.813 12.100 1.00 71.55  ? 114 GLY A N   1 
ATOM   832  C  CA  . GLY A 1 114 ? -15.513 -23.160 12.758 1.00 72.27  ? 114 GLY A CA  1 
ATOM   833  C  C   . GLY A 1 114 ? -16.445 -24.135 13.437 1.00 71.22  ? 114 GLY A C   1 
ATOM   834  O  O   . GLY A 1 114 ? -17.500 -23.758 13.934 1.00 72.16  ? 114 GLY A O   1 
ATOM   835  N  N   . ARG A 1 115 ? -16.051 -25.391 13.485 1.00 69.54  ? 115 ARG A N   1 
ATOM   836  C  CA  . ARG A 1 115 ? -16.868 -26.386 14.110 1.00 68.94  ? 115 ARG A CA  1 
ATOM   837  C  C   . ARG A 1 115 ? -16.140 -26.920 15.324 1.00 67.35  ? 115 ARG A C   1 
ATOM   838  O  O   . ARG A 1 115 ? -14.935 -26.799 15.405 1.00 66.92  ? 115 ARG A O   1 
ATOM   839  C  CB  . ARG A 1 115 ? -17.156 -27.473 13.102 1.00 69.13  ? 115 ARG A CB  1 
ATOM   840  C  CG  . ARG A 1 115 ? -17.764 -26.933 11.830 1.00 71.40  ? 115 ARG A CG  1 
ATOM   841  C  CD  . ARG A 1 115 ? -18.284 -28.046 10.928 1.00 72.76  ? 115 ARG A CD  1 
ATOM   842  N  NE  . ARG A 1 115 ? -18.852 -27.526 9.689  1.00 75.41  ? 115 ARG A NE  1 
ATOM   843  C  CZ  . ARG A 1 115 ? -20.086 -27.060 9.552  1.00 78.25  ? 115 ARG A CZ  1 
ATOM   844  N  NH1 . ARG A 1 115 ? -20.932 -27.063 10.567 1.00 79.23  ? 115 ARG A NH1 1 
ATOM   845  N  NH2 . ARG A 1 115 ? -20.479 -26.597 8.382  1.00 81.13  ? 115 ARG A NH2 1 
ATOM   846  N  N   . THR A 1 116 ? -16.862 -27.488 16.279 1.00 67.00  ? 116 THR A N   1 
ATOM   847  C  CA  . THR A 1 116 ? -16.234 -27.896 17.506 1.00 66.26  ? 116 THR A CA  1 
ATOM   848  C  C   . THR A 1 116 ? -15.664 -29.280 17.343 1.00 64.47  ? 116 THR A C   1 
ATOM   849  O  O   . THR A 1 116 ? -16.278 -30.148 16.750 1.00 64.27  ? 116 THR A O   1 
ATOM   850  C  CB  . THR A 1 116 ? -17.194 -27.884 18.698 1.00 67.46  ? 116 THR A CB  1 
ATOM   851  O  OG1 . THR A 1 116 ? -17.762 -26.585 18.878 1.00 70.47  ? 116 THR A OG1 1 
ATOM   852  C  CG2 . THR A 1 116 ? -16.446 -28.202 19.975 1.00 68.15  ? 116 THR A CG2 1 
ATOM   853  N  N   . LEU A 1 117 ? -14.459 -29.448 17.857 1.00 63.66  ? 117 LEU A N   1 
ATOM   854  C  CA  . LEU A 1 117 ? -13.820 -30.731 17.992 1.00 62.74  ? 117 LEU A CA  1 
ATOM   855  C  C   . LEU A 1 117 ? -14.073 -31.189 19.386 1.00 63.16  ? 117 LEU A C   1 
ATOM   856  O  O   . LEU A 1 117 ? -14.010 -30.392 20.299 1.00 64.43  ? 117 LEU A O   1 
ATOM   857  C  CB  . LEU A 1 117 ? -12.327 -30.564 17.832 1.00 62.51  ? 117 LEU A CB  1 
ATOM   858  C  CG  . LEU A 1 117 ? -11.498 -31.830 17.959 1.00 61.17  ? 117 LEU A CG  1 
ATOM   859  C  CD1 . LEU A 1 117 ? -11.858 -32.757 16.854 1.00 60.84  ? 117 LEU A CD1 1 
ATOM   860  C  CD2 . LEU A 1 117 ? -10.029 -31.518 17.925 1.00 60.37  ? 117 LEU A CD2 1 
ATOM   861  N  N   . VAL A 1 118 ? -14.325 -32.468 19.585 1.00 63.07  ? 118 VAL A N   1 
ATOM   862  C  CA  . VAL A 1 118 ? -14.699 -32.943 20.909 1.00 63.75  ? 118 VAL A CA  1 
ATOM   863  C  C   . VAL A 1 118 ? -14.012 -34.251 21.217 1.00 63.46  ? 118 VAL A C   1 
ATOM   864  O  O   . VAL A 1 118 ? -13.957 -35.114 20.356 1.00 63.06  ? 118 VAL A O   1 
ATOM   865  C  CB  . VAL A 1 118 ? -16.211 -33.191 20.979 1.00 64.44  ? 118 VAL A CB  1 
ATOM   866  C  CG1 . VAL A 1 118 ? -16.594 -33.664 22.341 1.00 65.53  ? 118 VAL A CG1 1 
ATOM   867  C  CG2 . VAL A 1 118 ? -16.968 -31.952 20.667 1.00 65.54  ? 118 VAL A CG2 1 
ATOM   868  N  N   . VAL A 1 119 ? -13.510 -34.399 22.440 1.00 64.26  ? 119 VAL A N   1 
ATOM   869  C  CA  . VAL A 1 119 ? -12.975 -35.674 22.912 1.00 64.70  ? 119 VAL A CA  1 
ATOM   870  C  C   . VAL A 1 119 ? -13.877 -36.165 24.014 1.00 66.59  ? 119 VAL A C   1 
ATOM   871  O  O   . VAL A 1 119 ? -14.347 -35.366 24.802 1.00 67.90  ? 119 VAL A O   1 
ATOM   872  C  CB  . VAL A 1 119 ? -11.567 -35.535 23.441 1.00 64.91  ? 119 VAL A CB  1 
ATOM   873  C  CG1 . VAL A 1 119 ? -11.530 -34.586 24.564 1.00 66.31  ? 119 VAL A CG1 1 
ATOM   874  C  CG2 . VAL A 1 119 ? -11.049 -36.833 23.897 1.00 65.23  ? 119 VAL A CG2 1 
ATOM   875  N  N   . HIS A 1 120 ? -14.120 -37.472 24.069 1.00 67.64  ? 120 HIS A N   1 
ATOM   876  C  CA  . HIS A 1 120 ? -15.231 -38.033 24.837 1.00 69.54  ? 120 HIS A CA  1 
ATOM   877  C  C   . HIS A 1 120 ? -14.827 -38.937 25.977 1.00 71.43  ? 120 HIS A C   1 
ATOM   878  O  O   . HIS A 1 120 ? -13.686 -39.400 26.062 1.00 71.18  ? 120 HIS A O   1 
ATOM   879  C  CB  . HIS A 1 120 ? -16.108 -38.862 23.932 1.00 69.37  ? 120 HIS A CB  1 
ATOM   880  C  CG  . HIS A 1 120 ? -16.982 -38.065 23.029 1.00 70.26  ? 120 HIS A CG  1 
ATOM   881  N  ND1 . HIS A 1 120 ? -18.331 -37.942 23.243 1.00 73.87  ? 120 HIS A ND1 1 
ATOM   882  C  CD2 . HIS A 1 120 ? -16.717 -37.397 21.882 1.00 70.38  ? 120 HIS A CD2 1 
ATOM   883  C  CE1 . HIS A 1 120 ? -18.859 -37.222 22.272 1.00 74.81  ? 120 HIS A CE1 1 
ATOM   884  N  NE2 . HIS A 1 120 ? -17.898 -36.871 21.437 1.00 72.18  ? 120 HIS A NE2 1 
ATOM   885  N  N   . GLU A 1 121 ? -15.819 -39.220 26.823 1.00 73.90  ? 121 GLU A N   1 
ATOM   886  C  CA  . GLU A 1 121 ? -15.654 -40.002 28.054 1.00 76.38  ? 121 GLU A CA  1 
ATOM   887  C  C   . GLU A 1 121 ? -15.143 -41.403 27.811 1.00 76.04  ? 121 GLU A C   1 
ATOM   888  O  O   . GLU A 1 121 ? -14.190 -41.803 28.441 1.00 76.76  ? 121 GLU A O   1 
ATOM   889  C  CB  . GLU A 1 121 ? -16.975 -40.082 28.807 1.00 78.79  ? 121 GLU A CB  1 
ATOM   890  C  CG  . GLU A 1 121 ? -16.841 -40.659 30.220 1.00 83.63  ? 121 GLU A CG  1 
ATOM   891  C  CD  . GLU A 1 121 ? -18.186 -40.853 30.957 1.00 88.92  ? 121 GLU A CD  1 
ATOM   892  O  OE1 . GLU A 1 121 ? -19.257 -40.901 30.302 1.00 89.55  ? 121 GLU A OE1 1 
ATOM   893  O  OE2 . GLU A 1 121 ? -18.150 -40.965 32.206 1.00 93.18  ? 121 GLU A OE2 1 
ATOM   894  N  N   . LYS A 1 122 ? -15.785 -42.139 26.911 1.00 75.53  ? 122 LYS A N   1 
ATOM   895  C  CA  . LYS A 1 122 ? -15.422 -43.537 26.623 1.00 76.41  ? 122 LYS A CA  1 
ATOM   896  C  C   . LYS A 1 122 ? -15.002 -43.754 25.178 1.00 74.39  ? 122 LYS A C   1 
ATOM   897  O  O   . LYS A 1 122 ? -14.919 -42.829 24.405 1.00 73.34  ? 122 LYS A O   1 
ATOM   898  C  CB  . LYS A 1 122 ? -16.606 -44.478 26.853 1.00 78.43  ? 122 LYS A CB  1 
ATOM   899  C  CG  . LYS A 1 122 ? -17.565 -44.122 27.964 1.00 82.35  ? 122 LYS A CG  1 
ATOM   900  C  CD  . LYS A 1 122 ? -18.731 -45.145 28.034 1.00 86.24  ? 122 LYS A CD  1 
ATOM   901  C  CE  . LYS A 1 122 ? -20.045 -44.469 28.418 1.00 88.88  ? 122 LYS A CE  1 
ATOM   902  N  NZ  . LYS A 1 122 ? -21.143 -45.470 28.581 1.00 91.92  ? 122 LYS A NZ  1 
ATOM   903  N  N   . ALA A 1 123 ? -14.787 -45.002 24.806 1.00 74.35  ? 123 ALA A N   1 
ATOM   904  C  CA  . ALA A 1 123 ? -14.458 -45.333 23.445 1.00 72.96  ? 123 ALA A CA  1 
ATOM   905  C  C   . ALA A 1 123 ? -15.622 -45.136 22.525 1.00 72.18  ? 123 ALA A C   1 
ATOM   906  O  O   . ALA A 1 123 ? -16.735 -45.414 22.902 1.00 72.88  ? 123 ALA A O   1 
ATOM   907  C  CB  . ALA A 1 123 ? -14.052 -46.740 23.385 1.00 74.59  ? 123 ALA A CB  1 
ATOM   908  N  N   . ASP A 1 124 ? -15.346 -44.663 21.313 1.00 70.96  ? 124 ASP A N   1 
ATOM   909  C  CA  . ASP A 1 124 ? -16.289 -44.705 20.175 1.00 71.10  ? 124 ASP A CA  1 
ATOM   910  C  C   . ASP A 1 124 ? -16.351 -46.156 19.769 1.00 72.13  ? 124 ASP A C   1 
ATOM   911  O  O   . ASP A 1 124 ? -15.325 -46.780 19.639 1.00 72.22  ? 124 ASP A O   1 
ATOM   912  C  CB  . ASP A 1 124 ? -15.770 -43.828 19.001 1.00 70.24  ? 124 ASP A CB  1 
ATOM   913  C  CG  . ASP A 1 124 ? -16.741 -43.758 17.767 1.00 71.79  ? 124 ASP A CG  1 
ATOM   914  O  OD1 . ASP A 1 124 ? -17.772 -44.451 17.771 1.00 74.16  ? 124 ASP A OD1 1 
ATOM   915  O  OD2 . ASP A 1 124 ? -16.470 -43.008 16.773 1.00 71.63  ? 124 ASP A OD2 1 
ATOM   916  N  N   . ASP A 1 125 ? -17.540 -46.715 19.590 1.00 73.14  ? 125 ASP A N   1 
ATOM   917  C  CA  . ASP A 1 125 ? -17.643 -48.126 19.233 1.00 74.75  ? 125 ASP A CA  1 
ATOM   918  C  C   . ASP A 1 125 ? -17.768 -48.304 17.739 1.00 75.18  ? 125 ASP A C   1 
ATOM   919  O  O   . ASP A 1 125 ? -18.050 -49.377 17.269 1.00 76.73  ? 125 ASP A O   1 
ATOM   920  C  CB  . ASP A 1 125 ? -18.792 -48.807 19.987 1.00 76.61  ? 125 ASP A CB  1 
ATOM   921  C  CG  . ASP A 1 125 ? -20.159 -48.369 19.515 1.00 77.47  ? 125 ASP A CG  1 
ATOM   922  O  OD1 . ASP A 1 125 ? -20.248 -47.849 18.398 1.00 77.50  ? 125 ASP A OD1 1 
ATOM   923  O  OD2 . ASP A 1 125 ? -21.149 -48.559 20.258 1.00 78.66  ? 125 ASP A OD2 1 
ATOM   924  N  N   . LEU A 1 126 ? -17.572 -47.223 17.003 1.00 74.13  ? 126 LEU A N   1 
ATOM   925  C  CA  . LEU A 1 126 ? -17.509 -47.240 15.549 1.00 75.22  ? 126 LEU A CA  1 
ATOM   926  C  C   . LEU A 1 126 ? -18.799 -47.731 14.883 1.00 77.81  ? 126 LEU A C   1 
ATOM   927  O  O   . LEU A 1 126 ? -18.779 -48.204 13.752 1.00 79.52  ? 126 LEU A O   1 
ATOM   928  C  CB  . LEU A 1 126 ? -16.296 -48.048 15.073 1.00 76.04  ? 126 LEU A CB  1 
ATOM   929  C  CG  . LEU A 1 126 ? -14.956 -47.820 15.781 1.00 73.96  ? 126 LEU A CG  1 
ATOM   930  C  CD1 . LEU A 1 126 ? -13.772 -48.339 14.958 1.00 74.57  ? 126 LEU A CD1 1 
ATOM   931  C  CD2 . LEU A 1 126 ? -14.807 -46.367 16.067 1.00 70.73  ? 126 LEU A CD2 1 
ATOM   932  N  N   . GLY A 1 127 ? -19.921 -47.588 15.578 1.00 78.74  ? 127 GLY A N   1 
ATOM   933  C  CA  . GLY A 1 127 ? -21.223 -47.913 15.028 1.00 81.62  ? 127 GLY A CA  1 
ATOM   934  C  C   . GLY A 1 127 ? -21.600 -49.357 15.195 1.00 84.80  ? 127 GLY A C   1 
ATOM   935  O  O   . GLY A 1 127 ? -22.686 -49.728 14.825 1.00 87.25  ? 127 GLY A O   1 
ATOM   936  N  N   . LYS A 1 128 ? -20.737 -50.171 15.790 1.00 85.46  ? 128 LYS A N   1 
ATOM   937  C  CA  . LYS A 1 128 ? -20.965 -51.608 15.853 1.00 88.91  ? 128 LYS A CA  1 
ATOM   938  C  C   . LYS A 1 128 ? -21.461 -52.073 17.202 1.00 89.10  ? 128 LYS A C   1 
ATOM   939  O  O   . LYS A 1 128 ? -21.281 -53.238 17.537 1.00 90.79  ? 128 LYS A O   1 
ATOM   940  C  CB  . LYS A 1 128 ? -19.681 -52.377 15.506 1.00 89.89  ? 128 LYS A CB  1 
ATOM   941  C  CG  . LYS A 1 128 ? -18.813 -51.714 14.453 1.00 91.75  ? 128 LYS A CG  1 
ATOM   942  C  CD  . LYS A 1 128 ? -17.851 -52.688 13.724 1.00 97.17  ? 128 LYS A CD  1 
ATOM   943  C  CE  . LYS A 1 128 ? -16.821 -51.917 12.834 1.00 98.27  ? 128 LYS A CE  1 
ATOM   944  N  NZ  . LYS A 1 128 ? -17.424 -51.223 11.621 1.00 99.93  ? 128 LYS A NZ  1 
ATOM   945  N  N   . GLY A 1 129 ? -22.084 -51.184 17.967 1.00 88.06  ? 129 GLY A N   1 
ATOM   946  C  CA  . GLY A 1 129 ? -22.555 -51.509 19.317 1.00 89.12  ? 129 GLY A CA  1 
ATOM   947  C  C   . GLY A 1 129 ? -23.939 -52.122 19.305 1.00 92.37  ? 129 GLY A C   1 
ATOM   948  O  O   . GLY A 1 129 ? -24.428 -52.614 20.326 1.00 93.74  ? 129 GLY A O   1 
ATOM   949  N  N   . GLY A 1 130 ? -24.579 -52.058 18.146 1.00 93.89  ? 130 GLY A N   1 
ATOM   950  C  CA  . GLY A 1 130 ? -25.870 -52.666 17.951 1.00 97.68  ? 130 GLY A CA  1 
ATOM   951  C  C   . GLY A 1 130 ? -26.989 -52.014 18.713 1.00 98.81  ? 130 GLY A C   1 
ATOM   952  O  O   . GLY A 1 130 ? -28.074 -52.549 18.775 1.00 102.22 ? 130 GLY A O   1 
ATOM   953  N  N   . ASN A 1 131 ? -26.755 -50.864 19.307 1.00 96.71  ? 131 ASN A N   1 
ATOM   954  C  CA  . ASN A 1 131 ? -27.825 -50.213 19.998 1.00 98.47  ? 131 ASN A CA  1 
ATOM   955  C  C   . ASN A 1 131 ? -28.161 -48.956 19.211 1.00 98.10  ? 131 ASN A C   1 
ATOM   956  O  O   . ASN A 1 131 ? -27.475 -48.616 18.255 1.00 96.04  ? 131 ASN A O   1 
ATOM   957  C  CB  . ASN A 1 131 ? -27.520 -50.041 21.516 1.00 97.82  ? 131 ASN A CB  1 
ATOM   958  C  CG  . ASN A 1 131 ? -26.804 -48.760 21.849 1.00 94.25  ? 131 ASN A CG  1 
ATOM   959  O  OD1 . ASN A 1 131 ? -25.851 -48.382 21.189 1.00 91.27  ? 131 ASN A OD1 1 
ATOM   960  N  ND2 . ASN A 1 131 ? -27.253 -48.091 22.907 1.00 94.55  ? 131 ASN A ND2 1 
ATOM   961  N  N   . GLU A 1 132 ? -29.277 -48.333 19.552 1.00 100.95 ? 132 GLU A N   1 
ATOM   962  C  CA  . GLU A 1 132 ? -29.778 -47.190 18.808 1.00 101.86 ? 132 GLU A CA  1 
ATOM   963  C  C   . GLU A 1 132 ? -28.693 -46.127 18.815 1.00 97.57  ? 132 GLU A C   1 
ATOM   964  O  O   . GLU A 1 132 ? -28.270 -45.636 17.769 1.00 95.72  ? 132 GLU A O   1 
ATOM   965  C  CB  . GLU A 1 132 ? -31.101 -46.685 19.452 1.00 105.66 ? 132 GLU A CB  1 
ATOM   966  C  CG  . GLU A 1 132 ? -31.422 -45.146 19.313 1.00 107.92 ? 132 GLU A CG  1 
ATOM   967  C  CD  . GLU A 1 132 ? -32.327 -44.781 18.107 1.00 113.42 ? 132 GLU A CD  1 
ATOM   968  O  OE1 . GLU A 1 132 ? -33.066 -45.677 17.627 1.00 118.23 ? 132 GLU A OE1 1 
ATOM   969  O  OE2 . GLU A 1 132 ? -32.301 -43.596 17.650 1.00 113.71 ? 132 GLU A OE2 1 
ATOM   970  N  N   . GLU A 1 133 ? -28.238 -45.823 20.026 1.00 96.04  ? 133 GLU A N   1 
ATOM   971  C  CA  . GLU A 1 133 ? -27.271 -44.768 20.293 1.00 92.91  ? 133 GLU A CA  1 
ATOM   972  C  C   . GLU A 1 133 ? -25.957 -44.956 19.545 1.00 89.51  ? 133 GLU A C   1 
ATOM   973  O  O   . GLU A 1 133 ? -25.311 -43.985 19.175 1.00 87.36  ? 133 GLU A O   1 
ATOM   974  C  CB  . GLU A 1 133 ? -27.018 -44.678 21.812 1.00 93.16  ? 133 GLU A CB  1 
ATOM   975  C  CG  . GLU A 1 133 ? -26.188 -43.477 22.270 1.00 92.49  ? 133 GLU A CG  1 
ATOM   976  C  CD  . GLU A 1 133 ? -26.832 -42.130 21.875 1.00 95.87  ? 133 GLU A CD  1 
ATOM   977  O  OE1 . GLU A 1 133 ? -28.089 -42.019 21.938 1.00 100.25 ? 133 GLU A OE1 1 
ATOM   978  O  OE2 . GLU A 1 133 ? -26.081 -41.183 21.490 1.00 94.99  ? 133 GLU A OE2 1 
ATOM   979  N  N   . SER A 1 134 ? -25.564 -46.196 19.297 1.00 89.43  ? 134 SER A N   1 
ATOM   980  C  CA  . SER A 1 134 ? -24.291 -46.456 18.621 1.00 86.91  ? 134 SER A CA  1 
ATOM   981  C  C   . SER A 1 134 ? -24.244 -45.914 17.199 1.00 86.50  ? 134 SER A C   1 
ATOM   982  O  O   . SER A 1 134 ? -23.189 -45.556 16.727 1.00 84.88  ? 134 SER A O   1 
ATOM   983  C  CB  . SER A 1 134 ? -23.969 -47.943 18.585 1.00 88.00  ? 134 SER A CB  1 
ATOM   984  O  OG  . SER A 1 134 ? -22.803 -48.174 17.823 1.00 85.88  ? 134 SER A OG  1 
ATOM   985  N  N   . THR A 1 135 ? -25.376 -45.852 16.510 1.00 88.53  ? 135 THR A N   1 
ATOM   986  C  CA  . THR A 1 135 ? -25.388 -45.289 15.154 1.00 88.61  ? 135 THR A CA  1 
ATOM   987  C  C   . THR A 1 135 ? -25.498 -43.766 15.161 1.00 87.26  ? 135 THR A C   1 
ATOM   988  O  O   . THR A 1 135 ? -25.747 -43.157 14.128 1.00 87.86  ? 135 THR A O   1 
ATOM   989  C  CB  . THR A 1 135 ? -26.539 -45.863 14.328 1.00 92.21  ? 135 THR A CB  1 
ATOM   990  O  OG1 . THR A 1 135 ? -27.703 -45.908 15.159 1.00 94.17  ? 135 THR A OG1 1 
ATOM   991  C  CG2 . THR A 1 135 ? -26.185 -47.256 13.801 1.00 92.99  ? 135 THR A CG2 1 
ATOM   992  N  N   . LYS A 1 136 ? -25.296 -43.153 16.321 1.00 85.68  ? 136 LYS A N   1 
ATOM   993  C  CA  . LYS A 1 136 ? -25.373 -41.707 16.444 1.00 85.14  ? 136 LYS A CA  1 
ATOM   994  C  C   . LYS A 1 136 ? -24.118 -41.123 17.082 1.00 81.76  ? 136 LYS A C   1 
ATOM   995  O  O   . LYS A 1 136 ? -23.428 -40.296 16.479 1.00 80.28  ? 136 LYS A O   1 
ATOM   996  C  CB  . LYS A 1 136 ? -26.612 -41.323 17.257 1.00 87.54  ? 136 LYS A CB  1 
ATOM   997  C  CG  . LYS A 1 136 ? -27.908 -41.993 16.759 1.00 93.22  ? 136 LYS A CG  1 
ATOM   998  C  CD  . LYS A 1 136 ? -29.105 -41.756 17.702 1.00 98.40  ? 136 LYS A CD  1 
ATOM   999  C  CE  . LYS A 1 136 ? -29.554 -40.303 17.748 1.00 99.83  ? 136 LYS A CE  1 
ATOM   1000 N  NZ  . LYS A 1 136 ? -30.856 -40.204 18.440 1.00 104.03 ? 136 LYS A NZ  1 
ATOM   1001 N  N   . THR A 1 137 ? -23.823 -41.542 18.302 1.00 80.69  ? 137 THR A N   1 
ATOM   1002 C  CA  . THR A 1 137 ? -22.627 -41.076 18.958 1.00 78.41  ? 137 THR A CA  1 
ATOM   1003 C  C   . THR A 1 137 ? -21.595 -42.162 19.101 1.00 76.89  ? 137 THR A C   1 
ATOM   1004 O  O   . THR A 1 137 ? -20.545 -41.907 19.648 1.00 75.80  ? 137 THR A O   1 
ATOM   1005 C  CB  . THR A 1 137 ? -22.896 -40.516 20.381 1.00 79.05  ? 137 THR A CB  1 
ATOM   1006 O  OG1 . THR A 1 137 ? -23.418 -41.550 21.235 1.00 81.08  ? 137 THR A OG1 1 
ATOM   1007 C  CG2 . THR A 1 137 ? -23.844 -39.315 20.332 1.00 80.77  ? 137 THR A CG2 1 
ATOM   1008 N  N   . GLY A 1 138 ? -21.863 -43.370 18.642 1.00 77.29  ? 138 GLY A N   1 
ATOM   1009 C  CA  . GLY A 1 138 ? -20.943 -44.463 18.916 1.00 76.57  ? 138 GLY A CA  1 
ATOM   1010 C  C   . GLY A 1 138 ? -20.796 -44.786 20.399 1.00 76.45  ? 138 GLY A C   1 
ATOM   1011 O  O   . GLY A 1 138 ? -19.808 -45.385 20.811 1.00 75.73  ? 138 GLY A O   1 
ATOM   1012 N  N   . ASN A 1 139 ? -21.779 -44.396 21.205 1.00 77.51  ? 139 ASN A N   1 
ATOM   1013 C  CA  . ASN A 1 139 ? -21.772 -44.649 22.642 1.00 78.37  ? 139 ASN A CA  1 
ATOM   1014 C  C   . ASN A 1 139 ? -20.566 -44.079 23.331 1.00 76.98  ? 139 ASN A C   1 
ATOM   1015 O  O   . ASN A 1 139 ? -20.114 -44.591 24.336 1.00 77.59  ? 139 ASN A O   1 
ATOM   1016 C  CB  . ASN A 1 139 ? -21.843 -46.152 22.915 1.00 79.98  ? 139 ASN A CB  1 
ATOM   1017 C  CG  . ASN A 1 139 ? -23.243 -46.705 22.771 1.00 82.30  ? 139 ASN A CG  1 
ATOM   1018 O  OD1 . ASN A 1 139 ? -24.231 -45.968 22.771 1.00 81.92  ? 139 ASN A OD1 1 
ATOM   1019 N  ND2 . ASN A 1 139 ? -23.333 -48.020 22.657 1.00 84.12  ? 139 ASN A ND2 1 
ATOM   1020 N  N   . ALA A 1 140 ? -20.064 -42.992 22.789 1.00 75.76  ? 140 ALA A N   1 
ATOM   1021 C  CA  . ALA A 1 140 ? -18.770 -42.473 23.173 1.00 74.73  ? 140 ALA A CA  1 
ATOM   1022 C  C   . ALA A 1 140 ? -18.849 -41.831 24.507 1.00 75.85  ? 140 ALA A C   1 
ATOM   1023 O  O   . ALA A 1 140 ? -17.827 -41.666 25.172 1.00 75.52  ? 140 ALA A O   1 
ATOM   1024 C  CB  . ALA A 1 140 ? -18.315 -41.461 22.174 1.00 73.27  ? 140 ALA A CB  1 
ATOM   1025 N  N   . GLY A 1 141 ? -20.062 -41.434 24.874 1.00 77.67  ? 141 GLY A N   1 
ATOM   1026 C  CA  . GLY A 1 141 ? -20.321 -40.912 26.200 1.00 79.59  ? 141 GLY A CA  1 
ATOM   1027 C  C   . GLY A 1 141 ? -20.241 -39.411 26.233 1.00 79.26  ? 141 GLY A C   1 
ATOM   1028 O  O   . GLY A 1 141 ? -20.219 -38.770 25.187 1.00 77.82  ? 141 GLY A O   1 
ATOM   1029 N  N   . SER A 1 142 ? -20.189 -38.863 27.444 1.00 81.09  ? 142 SER A N   1 
ATOM   1030 C  CA  . SER A 1 142 ? -20.255 -37.423 27.650 1.00 81.75  ? 142 SER A CA  1 
ATOM   1031 C  C   . SER A 1 142 ? -19.023 -36.729 27.070 1.00 79.38  ? 142 SER A C   1 
ATOM   1032 O  O   . SER A 1 142 ? -18.081 -37.389 26.616 1.00 77.69  ? 142 SER A O   1 
ATOM   1033 C  CB  . SER A 1 142 ? -20.410 -37.098 29.139 1.00 84.70  ? 142 SER A CB  1 
ATOM   1034 O  OG  . SER A 1 142 ? -19.357 -37.666 29.894 1.00 85.39  ? 142 SER A OG  1 
ATOM   1035 N  N   . ARG A 1 143 ? -19.045 -35.399 27.093 1.00 79.38  ? 143 ARG A N   1 
ATOM   1036 C  CA  . ARG A 1 143 ? -18.120 -34.606 26.331 1.00 77.54  ? 143 ARG A CA  1 
ATOM   1037 C  C   . ARG A 1 143 ? -17.076 -34.011 27.243 1.00 77.40  ? 143 ARG A C   1 
ATOM   1038 O  O   . ARG A 1 143 ? -17.257 -32.953 27.783 1.00 78.93  ? 143 ARG A O   1 
ATOM   1039 C  CB  . ARG A 1 143 ? -18.911 -33.532 25.577 1.00 78.14  ? 143 ARG A CB  1 
ATOM   1040 C  CG  . ARG A 1 143 ? -20.015 -34.124 24.719 1.00 80.01  ? 143 ARG A CG  1 
ATOM   1041 C  CD  . ARG A 1 143 ? -20.757 -33.094 23.895 1.00 82.93  ? 143 ARG A CD  1 
ATOM   1042 N  NE  . ARG A 1 143 ? -21.541 -33.733 22.833 1.00 84.60  ? 143 ARG A NE  1 
ATOM   1043 C  CZ  . ARG A 1 143 ? -22.332 -33.098 21.973 1.00 86.69  ? 143 ARG A CZ  1 
ATOM   1044 N  NH1 . ARG A 1 143 ? -22.483 -31.789 22.031 1.00 88.01  ? 143 ARG A NH1 1 
ATOM   1045 N  NH2 . ARG A 1 143 ? -22.986 -33.776 21.055 1.00 88.03  ? 143 ARG A NH2 1 
ATOM   1046 N  N   . LEU A 1 144 ? -15.964 -34.697 27.396 1.00 76.00  ? 144 LEU A N   1 
ATOM   1047 C  CA  . LEU A 1 144 ? -14.965 -34.328 28.402 1.00 77.15  ? 144 LEU A CA  1 
ATOM   1048 C  C   . LEU A 1 144 ? -14.264 -32.971 28.206 1.00 76.49  ? 144 LEU A C   1 
ATOM   1049 O  O   . LEU A 1 144 ? -13.997 -32.259 29.173 1.00 78.35  ? 144 LEU A O   1 
ATOM   1050 C  CB  . LEU A 1 144 ? -13.904 -35.436 28.497 1.00 76.93  ? 144 LEU A CB  1 
ATOM   1051 C  CG  . LEU A 1 144 ? -14.235 -36.708 29.278 1.00 78.85  ? 144 LEU A CG  1 
ATOM   1052 C  CD1 . LEU A 1 144 ? -13.018 -37.628 29.345 1.00 79.96  ? 144 LEU A CD1 1 
ATOM   1053 C  CD2 . LEU A 1 144 ? -14.695 -36.369 30.680 1.00 82.96  ? 144 LEU A CD2 1 
ATOM   1054 N  N   . ALA A 1 145 ? -13.917 -32.662 26.959 1.00 74.04  ? 145 ALA A N   1 
ATOM   1055 C  CA  . ALA A 1 145 ? -13.291 -31.391 26.588 1.00 73.80  ? 145 ALA A CA  1 
ATOM   1056 C  C   . ALA A 1 145 ? -13.627 -31.069 25.139 1.00 72.13  ? 145 ALA A C   1 
ATOM   1057 O  O   . ALA A 1 145 ? -13.963 -31.968 24.360 1.00 71.18  ? 145 ALA A O   1 
ATOM   1058 C  CB  . ALA A 1 145 ? -11.809 -31.461 26.779 1.00 73.64  ? 145 ALA A CB  1 
ATOM   1059 N  N   . CYS A 1 146 ? -13.559 -29.794 24.772 1.00 72.59  ? 146 CYS A N   1 
ATOM   1060 C  CA  . CYS A 1 146 ? -13.824 -29.390 23.381 1.00 71.58  ? 146 CYS A CA  1 
ATOM   1061 C  C   . CYS A 1 146 ? -13.336 -27.986 23.058 1.00 71.59  ? 146 CYS A C   1 
ATOM   1062 O  O   . CYS A 1 146 ? -13.022 -27.214 23.952 1.00 73.41  ? 146 CYS A O   1 
ATOM   1063 C  CB  . CYS A 1 146 ? -15.306 -29.467 23.077 1.00 71.97  ? 146 CYS A CB  1 
ATOM   1064 S  SG  . CYS A 1 146 ? -16.260 -28.211 23.889 1.00 76.35  ? 146 CYS A SG  1 
ATOM   1065 N  N   . GLY A 1 147 ? -13.271 -27.656 21.780 1.00 69.95  ? 147 GLY A N   1 
ATOM   1066 C  CA  . GLY A 1 147 ? -12.985 -26.296 21.405 1.00 70.49  ? 147 GLY A CA  1 
ATOM   1067 C  C   . GLY A 1 147 ? -13.285 -26.070 19.960 1.00 69.30  ? 147 GLY A C   1 
ATOM   1068 O  O   . GLY A 1 147 ? -13.312 -27.021 19.197 1.00 68.10  ? 147 GLY A O   1 
ATOM   1069 N  N   . VAL A 1 148 ? -13.510 -24.812 19.583 1.00 69.58  ? 148 VAL A N   1 
ATOM   1070 C  CA  . VAL A 1 148 ? -13.741 -24.478 18.179 1.00 68.69  ? 148 VAL A CA  1 
ATOM   1071 C  C   . VAL A 1 148 ? -12.472 -24.548 17.374 1.00 67.62  ? 148 VAL A C   1 
ATOM   1072 O  O   . VAL A 1 148 ? -11.423 -24.224 17.857 1.00 67.88  ? 148 VAL A O   1 
ATOM   1073 C  CB  . VAL A 1 148 ? -14.328 -23.106 18.019 1.00 70.27  ? 148 VAL A CB  1 
ATOM   1074 C  CG1 . VAL A 1 148 ? -14.448 -22.774 16.574 1.00 69.83  ? 148 VAL A CG1 1 
ATOM   1075 C  CG2 . VAL A 1 148 ? -15.687 -23.072 18.652 1.00 71.44  ? 148 VAL A CG2 1 
ATOM   1076 N  N   . ILE A 1 149 ? -12.589 -24.980 16.139 1.00 66.79  ? 149 ILE A N   1 
ATOM   1077 C  CA  . ILE A 1 149 ? -11.447 -25.196 15.280 1.00 66.73  ? 149 ILE A CA  1 
ATOM   1078 C  C   . ILE A 1 149 ? -11.184 -23.967 14.516 1.00 68.00  ? 149 ILE A C   1 
ATOM   1079 O  O   . ILE A 1 149 ? -12.047 -23.557 13.782 1.00 68.72  ? 149 ILE A O   1 
ATOM   1080 C  CB  . ILE A 1 149 ? -11.792 -26.242 14.211 1.00 66.49  ? 149 ILE A CB  1 
ATOM   1081 C  CG1 . ILE A 1 149 ? -11.663 -27.650 14.761 1.00 65.15  ? 149 ILE A CG1 1 
ATOM   1082 C  CG2 . ILE A 1 149 ? -10.910 -26.099 13.003 1.00 67.82  ? 149 ILE A CG2 1 
ATOM   1083 C  CD1 . ILE A 1 149 ? -12.512 -28.604 14.014 1.00 65.53  ? 149 ILE A CD1 1 
ATOM   1084 N  N   . GLY A 1 150 ? -9.984  -23.420 14.589 1.00 68.88  ? 150 GLY A N   1 
ATOM   1085 C  CA  . GLY A 1 150 ? -9.725  -22.109 13.996 1.00 71.13  ? 150 GLY A CA  1 
ATOM   1086 C  C   . GLY A 1 150 ? -8.558  -22.048 13.062 1.00 72.49  ? 150 GLY A C   1 
ATOM   1087 O  O   . GLY A 1 150 ? -7.756  -22.947 13.027 1.00 72.10  ? 150 GLY A O   1 
ATOM   1088 N  N   . ILE A 1 151 ? -8.466  -20.970 12.298 1.00 75.07  ? 151 ILE A N   1 
ATOM   1089 C  CA  . ILE A 1 151 ? -7.457  -20.868 11.232 1.00 77.39  ? 151 ILE A CA  1 
ATOM   1090 C  C   . ILE A 1 151 ? -6.125  -20.563 11.856 1.00 79.31  ? 151 ILE A C   1 
ATOM   1091 O  O   . ILE A 1 151 ? -6.021  -19.627 12.636 1.00 80.33  ? 151 ILE A O   1 
ATOM   1092 C  CB  . ILE A 1 151 ? -7.773  -19.780 10.196 1.00 79.23  ? 151 ILE A CB  1 
ATOM   1093 C  CG1 . ILE A 1 151 ? -9.148  -20.025 9.583  1.00 78.52  ? 151 ILE A CG1 1 
ATOM   1094 C  CG2 . ILE A 1 151 ? -6.726  -19.786 9.130  1.00 80.72  ? 151 ILE A CG2 1 
ATOM   1095 C  CD1 . ILE A 1 151 ? -9.596  -18.982 8.672  1.00 81.13  ? 151 ILE A CD1 1 
ATOM   1096 N  N   . ALA A 1 152 ? -5.125  -21.366 11.521 1.00 80.90  ? 152 ALA A N   1 
ATOM   1097 C  CA  . ALA A 1 152 ? -3.852  -21.308 12.194 1.00 83.08  ? 152 ALA A CA  1 
ATOM   1098 C  C   . ALA A 1 152 ? -2.848  -20.696 11.275 1.00 87.24  ? 152 ALA A C   1 
ATOM   1099 O  O   . ALA A 1 152 ? -3.032  -20.722 10.057 1.00 87.86  ? 152 ALA A O   1 
ATOM   1100 C  CB  . ALA A 1 152 ? -3.414  -22.669 12.562 1.00 82.12  ? 152 ALA A CB  1 
ATOM   1101 N  N   . GLN A 1 153 ? -1.774  -20.160 11.862 1.00 90.66  ? 153 GLN A N   1 
ATOM   1102 C  CA  . GLN A 1 153 ? -0.746  -19.561 11.044 1.00 95.30  ? 153 GLN A CA  1 
ATOM   1103 C  C   . GLN A 1 153 ? -0.048  -20.671 10.258 1.00 96.78  ? 153 GLN A C   1 
ATOM   1104 O  O   . GLN A 1 153 ? 0.314   -21.724 10.823 1.00 96.04  ? 153 GLN A O   1 
ATOM   1105 C  CB  . GLN A 1 153 ? 0.271   -18.731 11.843 1.00 97.86  ? 153 GLN A CB  1 
ATOM   1106 C  CG  . GLN A 1 153 ? 1.271   -18.002 10.876 1.00 102.21 ? 153 GLN A CG  1 
ATOM   1107 C  CD  . GLN A 1 153 ? 2.060   -16.856 11.514 1.00 105.69 ? 153 GLN A CD  1 
ATOM   1108 O  OE1 . GLN A 1 153 ? 2.648   -16.997 12.588 1.00 106.84 ? 153 GLN A OE1 1 
ATOM   1109 N  NE2 . GLN A 1 153 ? 2.091   -15.716 10.831 1.00 108.23 ? 153 GLN A NE2 1 
ATOM   1110 O  OXT . GLN A 1 153 ? 0.145   -20.504 9.036  1.00 99.62  ? 153 GLN A OXT 1 
ATOM   1111 N  N   . ALA B 1 1   ? -23.028 -20.722 5.614  1.00 96.69  ? 1   ALA B N   1 
ATOM   1112 C  CA  . ALA B 1 1   ? -23.044 -20.103 6.973  1.00 93.73  ? 1   ALA B CA  1 
ATOM   1113 C  C   . ALA B 1 1   ? -23.907 -18.770 7.038  1.00 93.40  ? 1   ALA B C   1 
ATOM   1114 O  O   . ALA B 1 1   ? -23.424 -17.691 6.648  1.00 92.62  ? 1   ALA B O   1 
ATOM   1115 C  CB  . ALA B 1 1   ? -21.584 -19.878 7.419  1.00 90.52  ? 1   ALA B CB  1 
ATOM   1116 N  N   . THR B 1 2   ? -25.173 -18.871 7.498  1.00 94.12  ? 2   THR B N   1 
ATOM   1117 C  CA  . THR B 1 2   ? -26.043 -17.695 7.818  1.00 93.49  ? 2   THR B CA  1 
ATOM   1118 C  C   . THR B 1 2   ? -25.647 -17.110 9.172  1.00 89.47  ? 2   THR B C   1 
ATOM   1119 O  O   . THR B 1 2   ? -25.573 -15.911 9.312  1.00 88.40  ? 2   THR B O   1 
ATOM   1120 C  CB  . THR B 1 2   ? -27.628 -18.034 7.872  1.00 97.16  ? 2   THR B CB  1 
ATOM   1121 O  OG1 . THR B 1 2   ? -28.141 -18.276 6.554  1.00 101.52 ? 2   THR B OG1 1 
ATOM   1122 C  CG2 . THR B 1 2   ? -28.486 -16.901 8.505  1.00 96.57  ? 2   THR B CG2 1 
ATOM   1123 N  N   . LYS B 1 3   ? -25.423 -17.960 10.171 1.00 87.59  ? 3   LYS B N   1 
ATOM   1124 C  CA  . LYS B 1 3   ? -25.185 -17.505 11.535 1.00 84.64  ? 3   LYS B CA  1 
ATOM   1125 C  C   . LYS B 1 3   ? -23.875 -17.984 12.072 1.00 81.36  ? 3   LYS B C   1 
ATOM   1126 O  O   . LYS B 1 3   ? -23.341 -18.992 11.601 1.00 81.88  ? 3   LYS B O   1 
ATOM   1127 C  CB  . LYS B 1 3   ? -26.270 -18.027 12.467 1.00 86.50  ? 3   LYS B CB  1 
ATOM   1128 C  CG  . LYS B 1 3   ? -27.623 -17.377 12.257 1.00 90.60  ? 3   LYS B CG  1 
ATOM   1129 C  CD  . LYS B 1 3   ? -28.662 -17.785 13.339 1.00 94.06  ? 3   LYS B CD  1 
ATOM   1130 C  CE  . LYS B 1 3   ? -30.100 -17.679 12.820 1.00 98.87  ? 3   LYS B CE  1 
ATOM   1131 N  NZ  . LYS B 1 3   ? -30.980 -18.556 13.611 1.00 102.13 ? 3   LYS B NZ  1 
ATOM   1132 N  N   . ALA B 1 4   ? -23.380 -17.257 13.073 1.00 77.97  ? 4   ALA B N   1 
ATOM   1133 C  CA  . ALA B 1 4   ? -22.201 -17.653 13.836 1.00 75.23  ? 4   ALA B CA  1 
ATOM   1134 C  C   . ALA B 1 4   ? -22.273 -17.134 15.251 1.00 73.42  ? 4   ALA B C   1 
ATOM   1135 O  O   . ALA B 1 4   ? -23.185 -16.403 15.592 1.00 73.94  ? 4   ALA B O   1 
ATOM   1136 C  CB  . ALA B 1 4   ? -20.967 -17.169 13.181 1.00 73.75  ? 4   ALA B CB  1 
ATOM   1137 N  N   . VAL B 1 5   ? -21.322 -17.549 16.079 1.00 71.61  ? 5   VAL B N   1 
ATOM   1138 C  CA  . VAL B 1 5   ? -21.285 -17.171 17.488 1.00 70.36  ? 5   VAL B CA  1 
ATOM   1139 C  C   . VAL B 1 5   ? -19.854 -17.245 17.991 1.00 69.08  ? 5   VAL B C   1 
ATOM   1140 O  O   . VAL B 1 5   ? -19.002 -17.864 17.356 1.00 68.85  ? 5   VAL B O   1 
ATOM   1141 C  CB  . VAL B 1 5   ? -22.143 -18.089 18.318 1.00 71.65  ? 5   VAL B CB  1 
ATOM   1142 C  CG1 . VAL B 1 5   ? -21.488 -19.418 18.419 1.00 71.96  ? 5   VAL B CG1 1 
ATOM   1143 C  CG2 . VAL B 1 5   ? -22.347 -17.527 19.668 1.00 70.45  ? 5   VAL B CG2 1 
ATOM   1144 N  N   . CYS B 1 6   ? -19.580 -16.599 19.118 1.00 68.56  ? 6   CYS B N   1 
ATOM   1145 C  CA  . CYS B 1 6   ? -18.242 -16.605 19.676 1.00 67.94  ? 6   CYS B CA  1 
ATOM   1146 C  C   . CYS B 1 6   ? -18.292 -16.334 21.140 1.00 68.08  ? 6   CYS B C   1 
ATOM   1147 O  O   . CYS B 1 6   ? -18.902 -15.364 21.534 1.00 68.08  ? 6   CYS B O   1 
ATOM   1148 C  CB  . CYS B 1 6   ? -17.416 -15.519 19.020 1.00 66.86  ? 6   CYS B CB  1 
ATOM   1149 S  SG  . CYS B 1 6   ? -15.849 -15.239 19.808 1.00 66.60  ? 6   CYS B SG  1 
ATOM   1150 N  N   . VAL B 1 7   ? -17.661 -17.182 21.947 1.00 68.72  ? 7   VAL B N   1 
ATOM   1151 C  CA  . VAL B 1 7   ? -17.576 -16.922 23.375 1.00 69.49  ? 7   VAL B CA  1 
ATOM   1152 C  C   . VAL B 1 7   ? -16.267 -16.282 23.762 1.00 69.31  ? 7   VAL B C   1 
ATOM   1153 O  O   . VAL B 1 7   ? -15.207 -16.860 23.559 1.00 69.60  ? 7   VAL B O   1 
ATOM   1154 C  CB  . VAL B 1 7   ? -17.695 -18.181 24.186 1.00 70.98  ? 7   VAL B CB  1 
ATOM   1155 C  CG1 . VAL B 1 7   ? -17.772 -17.833 25.642 1.00 71.70  ? 7   VAL B CG1 1 
ATOM   1156 C  CG2 . VAL B 1 7   ? -18.905 -18.915 23.799 1.00 72.47  ? 7   VAL B CG2 1 
ATOM   1157 N  N   . LEU B 1 8   ? -16.352 -15.101 24.356 1.00 69.62  ? 8   LEU B N   1 
ATOM   1158 C  CA  . LEU B 1 8   ? -15.183 -14.351 24.750 1.00 69.81  ? 8   LEU B CA  1 
ATOM   1159 C  C   . LEU B 1 8   ? -14.782 -14.672 26.150 1.00 71.95  ? 8   LEU B C   1 
ATOM   1160 O  O   . LEU B 1 8   ? -15.586 -14.576 27.031 1.00 72.64  ? 8   LEU B O   1 
ATOM   1161 C  CB  . LEU B 1 8   ? -15.493 -12.869 24.653 1.00 69.24  ? 8   LEU B CB  1 
ATOM   1162 C  CG  . LEU B 1 8   ? -15.685 -12.365 23.229 1.00 67.33  ? 8   LEU B CG  1 
ATOM   1163 C  CD1 . LEU B 1 8   ? -16.225 -11.007 23.253 1.00 65.45  ? 8   LEU B CD1 1 
ATOM   1164 C  CD2 . LEU B 1 8   ? -14.366 -12.385 22.493 1.00 67.80  ? 8   LEU B CD2 1 
ATOM   1165 N  N   . LYS B 1 9   ? -13.529 -15.045 26.337 1.00 73.90  ? 9   LYS B N   1 
ATOM   1166 C  CA  . LYS B 1 9   ? -12.988 -15.373 27.640 1.00 77.37  ? 9   LYS B CA  1 
ATOM   1167 C  C   . LYS B 1 9   ? -11.589 -14.865 27.699 1.00 78.03  ? 9   LYS B C   1 
ATOM   1168 O  O   . LYS B 1 9   ? -10.993 -14.613 26.670 1.00 77.16  ? 9   LYS B O   1 
ATOM   1169 C  CB  . LYS B 1 9   ? -12.888 -16.875 27.837 1.00 79.31  ? 9   LYS B CB  1 
ATOM   1170 C  CG  . LYS B 1 9   ? -14.209 -17.646 27.931 1.00 83.16  ? 9   LYS B CG  1 
ATOM   1171 C  CD  . LYS B 1 9   ? -14.772 -17.765 29.369 1.00 88.93  ? 9   LYS B CD  1 
ATOM   1172 C  CE  . LYS B 1 9   ? -15.740 -18.965 29.489 1.00 91.74  ? 9   LYS B CE  1 
ATOM   1173 N  NZ  . LYS B 1 9   ? -16.543 -18.944 30.750 1.00 95.10  ? 9   LYS B NZ  1 
ATOM   1174 N  N   . GLY B 1 10  ? -11.040 -14.767 28.900 1.00 80.43  ? 10  GLY B N   1 
ATOM   1175 C  CA  . GLY B 1 10  ? -9.667  -14.324 29.058 1.00 81.76  ? 10  GLY B CA  1 
ATOM   1176 C  C   . GLY B 1 10  ? -9.194  -14.590 30.455 1.00 84.87  ? 10  GLY B C   1 
ATOM   1177 O  O   . GLY B 1 10  ? -9.935  -15.126 31.248 1.00 85.99  ? 10  GLY B O   1 
ATOM   1178 N  N   . ASP B 1 11  ? -7.965  -14.185 30.759 1.00 87.06  ? 11  ASP B N   1 
ATOM   1179 C  CA  . ASP B 1 11  ? -7.420  -14.208 32.140 1.00 90.67  ? 11  ASP B CA  1 
ATOM   1180 C  C   . ASP B 1 11  ? -8.158  -13.307 33.112 1.00 91.26  ? 11  ASP B C   1 
ATOM   1181 O  O   . ASP B 1 11  ? -8.251  -13.610 34.290 1.00 93.29  ? 11  ASP B O   1 
ATOM   1182 C  CB  . ASP B 1 11  ? -5.962  -13.765 32.126 1.00 92.72  ? 11  ASP B CB  1 
ATOM   1183 C  CG  . ASP B 1 11  ? -5.056  -14.824 31.586 1.00 95.61  ? 11  ASP B CG  1 
ATOM   1184 O  OD1 . ASP B 1 11  ? -5.403  -16.020 31.734 1.00 98.77  ? 11  ASP B OD1 1 
ATOM   1185 O  OD2 . ASP B 1 11  ? -4.007  -14.466 31.002 1.00 99.06  ? 11  ASP B OD2 1 
ATOM   1186 N  N   . GLY B 1 12  ? -8.661  -12.185 32.586 1.00 89.62  ? 12  GLY B N   1 
ATOM   1187 C  CA  . GLY B 1 12  ? -9.418  -11.180 33.336 1.00 89.73  ? 12  GLY B CA  1 
ATOM   1188 C  C   . GLY B 1 12  ? -10.768 -11.682 33.784 1.00 88.95  ? 12  GLY B C   1 
ATOM   1189 O  O   . GLY B 1 12  ? -11.075 -12.860 33.660 1.00 88.45  ? 12  GLY B O   1 
ATOM   1190 N  N   . PRO B 1 13  ? -11.584 -10.773 34.306 1.00 88.85  ? 13  PRO B N   1 
ATOM   1191 C  CA  . PRO B 1 13  ? -12.955 -11.081 34.646 1.00 88.60  ? 13  PRO B CA  1 
ATOM   1192 C  C   . PRO B 1 13  ? -13.861 -10.831 33.457 1.00 85.20  ? 13  PRO B C   1 
ATOM   1193 O  O   . PRO B 1 13  ? -15.072 -11.050 33.520 1.00 84.77  ? 13  PRO B O   1 
ATOM   1194 C  CB  . PRO B 1 13  ? -13.252 -10.068 35.741 1.00 91.15  ? 13  PRO B CB  1 
ATOM   1195 C  CG  . PRO B 1 13  ? -12.491 -8.864  35.291 1.00 90.66  ? 13  PRO B CG  1 
ATOM   1196 C  CD  . PRO B 1 13  ? -11.263 -9.367  34.586 1.00 89.85  ? 13  PRO B CD  1 
ATOM   1197 N  N   . VAL B 1 14  ? -13.253 -10.375 32.376 1.00 82.79  ? 14  VAL B N   1 
ATOM   1198 C  CA  . VAL B 1 14  ? -13.987 -9.997  31.198 1.00 80.04  ? 14  VAL B CA  1 
ATOM   1199 C  C   . VAL B 1 14  ? -14.493 -11.245 30.531 1.00 78.56  ? 14  VAL B C   1 
ATOM   1200 O  O   . VAL B 1 14  ? -13.780 -12.245 30.444 1.00 78.66  ? 14  VAL B O   1 
ATOM   1201 C  CB  . VAL B 1 14  ? -13.101 -9.291  30.186 1.00 78.66  ? 14  VAL B CB  1 
ATOM   1202 C  CG1 . VAL B 1 14  ? -13.963 -8.576  29.167 1.00 75.93  ? 14  VAL B CG1 1 
ATOM   1203 C  CG2 . VAL B 1 14  ? -12.141 -8.336  30.891 1.00 81.08  ? 14  VAL B CG2 1 
ATOM   1204 N  N   . GLN B 1 15  ? -15.721 -11.181 30.052 1.00 77.48  ? 15  GLN B N   1 
ATOM   1205 C  CA  . GLN B 1 15  ? -16.311 -12.296 29.345 1.00 76.59  ? 15  GLN B CA  1 
ATOM   1206 C  C   . GLN B 1 15  ? -17.665 -11.936 28.767 1.00 75.48  ? 15  GLN B C   1 
ATOM   1207 O  O   . GLN B 1 15  ? -18.339 -11.030 29.252 1.00 76.31  ? 15  GLN B O   1 
ATOM   1208 C  CB  . GLN B 1 15  ? -16.461 -13.506 30.266 1.00 78.79  ? 15  GLN B CB  1 
ATOM   1209 C  CG  . GLN B 1 15  ? -17.563 -13.395 31.297 1.00 81.91  ? 15  GLN B CG  1 
ATOM   1210 C  CD  . GLN B 1 15  ? -17.577 -14.547 32.292 1.00 86.09  ? 15  GLN B CD  1 
ATOM   1211 O  OE1 . GLN B 1 15  ? -18.304 -14.489 33.277 1.00 89.69  ? 15  GLN B OE1 1 
ATOM   1212 N  NE2 . GLN B 1 15  ? -16.782 -15.601 32.036 1.00 85.98  ? 15  GLN B NE2 1 
ATOM   1213 N  N   . GLY B 1 16  ? -18.051 -12.651 27.719 1.00 73.69  ? 16  GLY B N   1 
ATOM   1214 C  CA  . GLY B 1 16  ? -19.334 -12.433 27.092 1.00 73.11  ? 16  GLY B CA  1 
ATOM   1215 C  C   . GLY B 1 16  ? -19.568 -13.361 25.943 1.00 71.75  ? 16  GLY B C   1 
ATOM   1216 O  O   . GLY B 1 16  ? -18.730 -14.183 25.634 1.00 71.40  ? 16  GLY B O   1 
ATOM   1217 N  N   . ILE B 1 17  ? -20.712 -13.204 25.307 1.00 71.41  ? 17  ILE B N   1 
ATOM   1218 C  CA  . ILE B 1 17  ? -21.107 -14.012 24.163 1.00 70.97  ? 17  ILE B CA  1 
ATOM   1219 C  C   . ILE B 1 17  ? -21.510 -13.073 23.055 1.00 70.07  ? 17  ILE B C   1 
ATOM   1220 O  O   . ILE B 1 17  ? -22.233 -12.138 23.330 1.00 70.61  ? 17  ILE B O   1 
ATOM   1221 C  CB  . ILE B 1 17  ? -22.370 -14.845 24.494 1.00 73.16  ? 17  ILE B CB  1 
ATOM   1222 C  CG1 . ILE B 1 17  ? -22.272 -15.482 25.892 1.00 74.68  ? 17  ILE B CG1 1 
ATOM   1223 C  CG2 . ILE B 1 17  ? -22.668 -15.886 23.382 1.00 73.33  ? 17  ILE B CG2 1 
ATOM   1224 C  CD1 . ILE B 1 17  ? -22.283 -16.967 25.899 1.00 76.36  ? 17  ILE B CD1 1 
ATOM   1225 N  N   . ILE B 1 18  ? -21.089 -13.322 21.816 1.00 69.14  ? 18  ILE B N   1 
ATOM   1226 C  CA  . ILE B 1 18  ? -21.454 -12.442 20.712 1.00 69.40  ? 18  ILE B CA  1 
ATOM   1227 C  C   . ILE B 1 18  ? -21.941 -13.223 19.546 1.00 70.34  ? 18  ILE B C   1 
ATOM   1228 O  O   . ILE B 1 18  ? -21.280 -14.152 19.142 1.00 70.13  ? 18  ILE B O   1 
ATOM   1229 C  CB  . ILE B 1 18  ? -20.262 -11.663 20.186 1.00 68.01  ? 18  ILE B CB  1 
ATOM   1230 C  CG1 . ILE B 1 18  ? -19.700 -10.729 21.248 1.00 68.25  ? 18  ILE B CG1 1 
ATOM   1231 C  CG2 . ILE B 1 18  ? -20.659 -10.858 18.989 1.00 67.82  ? 18  ILE B CG2 1 
ATOM   1232 C  CD1 . ILE B 1 18  ? -20.658 -9.738  21.768 1.00 70.87  ? 18  ILE B CD1 1 
ATOM   1233 N  N   . ASN B 1 19  ? -23.061 -12.808 18.972 1.00 72.23  ? 19  ASN B N   1 
ATOM   1234 C  CA  . ASN B 1 19  ? -23.650 -13.503 17.839 1.00 74.09  ? 19  ASN B CA  1 
ATOM   1235 C  C   . ASN B 1 19  ? -23.503 -12.779 16.532 1.00 74.48  ? 19  ASN B C   1 
ATOM   1236 O  O   . ASN B 1 19  ? -23.318 -11.596 16.501 1.00 74.12  ? 19  ASN B O   1 
ATOM   1237 C  CB  . ASN B 1 19  ? -25.126 -13.709 18.081 1.00 76.53  ? 19  ASN B CB  1 
ATOM   1238 C  CG  . ASN B 1 19  ? -25.379 -14.532 19.287 1.00 77.73  ? 19  ASN B CG  1 
ATOM   1239 O  OD1 . ASN B 1 19  ? -25.645 -13.997 20.362 1.00 78.80  ? 19  ASN B OD1 1 
ATOM   1240 N  ND2 . ASN B 1 19  ? -25.255 -15.857 19.140 1.00 78.69  ? 19  ASN B ND2 1 
ATOM   1241 N  N   . PHE B 1 20  ? -23.610 -13.514 15.445 1.00 76.28  ? 20  PHE B N   1 
ATOM   1242 C  CA  . PHE B 1 20  ? -23.488 -12.955 14.117 1.00 77.69  ? 20  PHE B CA  1 
ATOM   1243 C  C   . PHE B 1 20  ? -24.604 -13.506 13.260 1.00 81.26  ? 20  PHE B C   1 
ATOM   1244 O  O   . PHE B 1 20  ? -25.003 -14.669 13.418 1.00 82.65  ? 20  PHE B O   1 
ATOM   1245 C  CB  . PHE B 1 20  ? -22.181 -13.382 13.467 1.00 76.43  ? 20  PHE B CB  1 
ATOM   1246 C  CG  . PHE B 1 20  ? -20.957 -12.929 14.193 1.00 74.67  ? 20  PHE B CG  1 
ATOM   1247 C  CD1 . PHE B 1 20  ? -20.617 -13.469 15.418 1.00 75.03  ? 20  PHE B CD1 1 
ATOM   1248 C  CD2 . PHE B 1 20  ? -20.112 -11.990 13.639 1.00 73.49  ? 20  PHE B CD2 1 
ATOM   1249 C  CE1 . PHE B 1 20  ? -19.452 -13.046 16.090 1.00 73.38  ? 20  PHE B CE1 1 
ATOM   1250 C  CE2 . PHE B 1 20  ? -18.962 -11.572 14.300 1.00 71.11  ? 20  PHE B CE2 1 
ATOM   1251 C  CZ  . PHE B 1 20  ? -18.630 -12.097 15.517 1.00 71.11  ? 20  PHE B CZ  1 
ATOM   1252 N  N   . GLU B 1 21  ? -25.084 -12.690 12.330 1.00 83.69  ? 21  GLU B N   1 
ATOM   1253 C  CA  . GLU B 1 21  ? -26.105 -13.131 11.403 1.00 87.54  ? 21  GLU B CA  1 
ATOM   1254 C  C   . GLU B 1 21  ? -25.909 -12.419 10.067 1.00 88.81  ? 21  GLU B C   1 
ATOM   1255 O  O   . GLU B 1 21  ? -25.784 -11.208 10.015 1.00 88.87  ? 21  GLU B O   1 
ATOM   1256 C  CB  . GLU B 1 21  ? -27.510 -12.883 11.988 1.00 90.12  ? 21  GLU B CB  1 
ATOM   1257 C  CG  . GLU B 1 21  ? -28.645 -13.612 11.212 1.00 96.04  ? 21  GLU B CG  1 
ATOM   1258 C  CD  . GLU B 1 21  ? -30.060 -13.395 11.791 1.00 101.92 ? 21  GLU B CD  1 
ATOM   1259 O  OE1 . GLU B 1 21  ? -30.325 -12.265 12.302 1.00 103.84 ? 21  GLU B OE1 1 
ATOM   1260 O  OE2 . GLU B 1 21  ? -30.896 -14.356 11.712 1.00 105.82 ? 21  GLU B OE2 1 
ATOM   1261 N  N   . GLN B 1 22  ? -25.840 -13.193 8.995  1.00 90.63  ? 22  GLN B N   1 
ATOM   1262 C  CA  . GLN B 1 22  ? -25.731 -12.661 7.661  1.00 92.72  ? 22  GLN B CA  1 
ATOM   1263 C  C   . GLN B 1 22  ? -26.859 -13.293 6.865  1.00 97.46  ? 22  GLN B C   1 
ATOM   1264 O  O   . GLN B 1 22  ? -26.700 -14.384 6.288  1.00 98.57  ? 22  GLN B O   1 
ATOM   1265 C  CB  . GLN B 1 22  ? -24.357 -12.987 7.054  1.00 91.09  ? 22  GLN B CB  1 
ATOM   1266 C  CG  . GLN B 1 22  ? -24.144 -12.408 5.655  1.00 92.85  ? 22  GLN B CG  1 
ATOM   1267 C  CD  . GLN B 1 22  ? -22.716 -12.498 5.143  1.00 91.10  ? 22  GLN B CD  1 
ATOM   1268 O  OE1 . GLN B 1 22  ? -22.047 -13.512 5.316  1.00 89.26  ? 22  GLN B OE1 1 
ATOM   1269 N  NE2 . GLN B 1 22  ? -22.252 -11.431 4.485  1.00 91.85  ? 22  GLN B NE2 1 
ATOM   1270 N  N   . LYS B 1 23  ? -28.009 -12.610 6.850  1.00 101.03 ? 23  LYS B N   1 
ATOM   1271 C  CA  . LYS B 1 23  ? -29.194 -13.108 6.129  1.00 106.10 ? 23  LYS B CA  1 
ATOM   1272 C  C   . LYS B 1 23  ? -28.984 -13.249 4.630  1.00 108.65 ? 23  LYS B C   1 
ATOM   1273 O  O   . LYS B 1 23  ? -29.500 -14.160 4.033  1.00 111.43 ? 23  LYS B O   1 
ATOM   1274 C  CB  . LYS B 1 23  ? -30.426 -12.240 6.403  1.00 108.87 ? 23  LYS B CB  1 
ATOM   1275 C  CG  . LYS B 1 23  ? -31.242 -12.708 7.644  1.00 110.78 ? 23  LYS B CG  1 
ATOM   1276 C  CD  . LYS B 1 23  ? -32.126 -11.595 8.235  1.00 114.29 ? 23  LYS B CD  1 
ATOM   1277 C  CE  . LYS B 1 23  ? -31.276 -10.542 8.985  1.00 112.42 ? 23  LYS B CE  1 
ATOM   1278 N  NZ  . LYS B 1 23  ? -32.089 -9.351  9.400  1.00 115.18 ? 23  LYS B NZ  1 
ATOM   1279 N  N   . GLU B 1 24  ? -28.225 -12.353 4.027  1.00 108.48 ? 24  GLU B N   1 
ATOM   1280 C  CA  . GLU B 1 24  ? -27.934 -12.465 2.609  1.00 111.45 ? 24  GLU B CA  1 
ATOM   1281 C  C   . GLU B 1 24  ? -26.494 -12.768 2.365  1.00 109.17 ? 24  GLU B C   1 
ATOM   1282 O  O   . GLU B 1 24  ? -25.621 -12.141 2.941  1.00 106.37 ? 24  GLU B O   1 
ATOM   1283 C  CB  . GLU B 1 24  ? -28.227 -11.155 1.921  1.00 114.21 ? 24  GLU B CB  1 
ATOM   1284 C  CG  . GLU B 1 24  ? -29.692 -10.930 1.650  1.00 119.46 ? 24  GLU B CG  1 
ATOM   1285 C  CD  . GLU B 1 24  ? -29.947 -9.681  0.793  1.00 123.69 ? 24  GLU B CD  1 
ATOM   1286 O  OE1 . GLU B 1 24  ? -29.152 -8.683  0.888  1.00 122.20 ? 24  GLU B OE1 1 
ATOM   1287 O  OE2 . GLU B 1 24  ? -30.947 -9.730  0.022  1.00 128.54 ? 24  GLU B OE2 1 
ATOM   1288 N  N   . SER B 1 25  ? -26.240 -13.709 1.477  1.00 111.23 ? 25  SER B N   1 
ATOM   1289 C  CA  . SER B 1 25  ? -24.887 -13.942 1.002  1.00 110.29 ? 25  SER B CA  1 
ATOM   1290 C  C   . SER B 1 25  ? -24.243 -12.634 0.543  1.00 110.04 ? 25  SER B C   1 
ATOM   1291 O  O   . SER B 1 25  ? -24.836 -11.874 -0.238 1.00 112.98 ? 25  SER B O   1 
ATOM   1292 C  CB  . SER B 1 25  ? -24.898 -14.939 -0.153 1.00 113.82 ? 25  SER B CB  1 
ATOM   1293 O  OG  . SER B 1 25  ? -23.612 -15.032 -0.754 1.00 114.16 ? 25  SER B OG  1 
ATOM   1294 N  N   . ASN B 1 26  ? -23.035 -12.376 1.055  1.00 106.80 ? 26  ASN B N   1 
ATOM   1295 C  CA  . ASN B 1 26  ? -22.303 -11.134 0.776  1.00 106.49 ? 26  ASN B CA  1 
ATOM   1296 C  C   . ASN B 1 26  ? -23.043 -9.837  1.127  1.00 106.08 ? 26  ASN B C   1 
ATOM   1297 O  O   . ASN B 1 26  ? -22.657 -8.759  0.700  1.00 107.20 ? 26  ASN B O   1 
ATOM   1298 C  CB  . ASN B 1 26  ? -21.876 -11.131 -0.683 1.00 110.11 ? 26  ASN B CB  1 
ATOM   1299 C  CG  . ASN B 1 26  ? -20.775 -12.174 -0.977 1.00 110.60 ? 26  ASN B CG  1 
ATOM   1300 O  OD1 . ASN B 1 26  ? -19.953 -12.534 -0.097 1.00 108.53 ? 26  ASN B OD1 1 
ATOM   1301 N  ND2 . ASN B 1 26  ? -20.747 -12.648 -2.239 1.00 114.14 ? 26  ASN B ND2 1 
ATOM   1302 N  N   . GLY B 1 27  ? -24.096 -9.953  1.922  1.00 104.60 ? 27  GLY B N   1 
ATOM   1303 C  CA  . GLY B 1 27  ? -24.803 -8.802  2.434  1.00 103.99 ? 27  GLY B CA  1 
ATOM   1304 C  C   . GLY B 1 27  ? -24.110 -8.313  3.681  1.00 99.18  ? 27  GLY B C   1 
ATOM   1305 O  O   . GLY B 1 27  ? -22.934 -8.615  3.892  1.00 96.55  ? 27  GLY B O   1 
ATOM   1306 N  N   . PRO B 1 28  ? -24.835 -7.553  4.514  1.00 97.79  ? 28  PRO B N   1 
ATOM   1307 C  CA  . PRO B 1 28  ? -24.280 -7.052  5.747  1.00 94.00  ? 28  PRO B CA  1 
ATOM   1308 C  C   . PRO B 1 28  ? -24.445 -8.112  6.830  1.00 90.78  ? 28  PRO B C   1 
ATOM   1309 O  O   . PRO B 1 28  ? -25.148 -9.105  6.602  1.00 91.79  ? 28  PRO B O   1 
ATOM   1310 C  CB  . PRO B 1 28  ? -25.158 -5.837  6.044  1.00 95.70  ? 28  PRO B CB  1 
ATOM   1311 C  CG  . PRO B 1 28  ? -26.507 -6.274  5.600  1.00 99.01  ? 28  PRO B CG  1 
ATOM   1312 C  CD  . PRO B 1 28  ? -26.279 -7.281  4.454  1.00 100.70 ? 28  PRO B CD  1 
ATOM   1313 N  N   . VAL B 1 29  ? -23.833 -7.865  7.990  1.00 86.96  ? 29  VAL B N   1 
ATOM   1314 C  CA  . VAL B 1 29  ? -23.733 -8.828  9.066  1.00 84.16  ? 29  VAL B CA  1 
ATOM   1315 C  C   . VAL B 1 29  ? -24.093 -8.196  10.406 1.00 83.17  ? 29  VAL B C   1 
ATOM   1316 O  O   . VAL B 1 29  ? -23.332 -7.389  10.910 1.00 82.02  ? 29  VAL B O   1 
ATOM   1317 C  CB  . VAL B 1 29  ? -22.298 -9.283  9.211  1.00 81.56  ? 29  VAL B CB  1 
ATOM   1318 C  CG1 . VAL B 1 29  ? -22.194 -10.151 10.405 1.00 79.08  ? 29  VAL B CG1 1 
ATOM   1319 C  CG2 . VAL B 1 29  ? -21.807 -9.984  7.951  1.00 82.47  ? 29  VAL B CG2 1 
ATOM   1320 N  N   . LYS B 1 30  ? -25.231 -8.554  10.996 1.00 84.21  ? 30  LYS B N   1 
ATOM   1321 C  CA  . LYS B 1 30  ? -25.588 -8.006  12.313 1.00 83.85  ? 30  LYS B CA  1 
ATOM   1322 C  C   . LYS B 1 30  ? -24.758 -8.711  13.328 1.00 80.59  ? 30  LYS B C   1 
ATOM   1323 O  O   . LYS B 1 30  ? -24.686 -9.926  13.323 1.00 80.38  ? 30  LYS B O   1 
ATOM   1324 C  CB  . LYS B 1 30  ? -27.079 -8.164  12.671 1.00 86.71  ? 30  LYS B CB  1 
ATOM   1325 C  CG  . LYS B 1 30  ? -27.948 -6.968  12.258 1.00 91.95  ? 30  LYS B CG  1 
ATOM   1326 C  CD  . LYS B 1 30  ? -29.429 -7.343  11.960 1.00 98.14  ? 30  LYS B CD  1 
ATOM   1327 C  CE  . LYS B 1 30  ? -29.825 -7.085  10.460 1.00 101.96 ? 30  LYS B CE  1 
ATOM   1328 N  NZ  . LYS B 1 30  ? -31.144 -6.353  10.356 1.00 106.10 ? 30  LYS B NZ  1 
ATOM   1329 N  N   . VAL B 1 31  ? -24.135 -7.942  14.197 1.00 78.69  ? 31  VAL B N   1 
ATOM   1330 C  CA  . VAL B 1 31  ? -23.322 -8.484  15.244 1.00 76.36  ? 31  VAL B CA  1 
ATOM   1331 C  C   . VAL B 1 31  ? -23.862 -8.015  16.554 1.00 77.33  ? 31  VAL B C   1 
ATOM   1332 O  O   . VAL B 1 31  ? -23.876 -6.824  16.787 1.00 78.12  ? 31  VAL B O   1 
ATOM   1333 C  CB  . VAL B 1 31  ? -21.943 -7.935  15.145 1.00 74.51  ? 31  VAL B CB  1 
ATOM   1334 C  CG1 . VAL B 1 31  ? -21.113 -8.420  16.312 1.00 71.79  ? 31  VAL B CG1 1 
ATOM   1335 C  CG2 . VAL B 1 31  ? -21.355 -8.319  13.812 1.00 74.08  ? 31  VAL B CG2 1 
ATOM   1336 N  N   . TRP B 1 32  ? -24.311 -8.910  17.427 1.00 78.12  ? 32  TRP B N   1 
ATOM   1337 C  CA  . TRP B 1 32  ? -24.811 -8.448  18.718 1.00 79.46  ? 32  TRP B CA  1 
ATOM   1338 C  C   . TRP B 1 32  ? -24.619 -9.454  19.827 1.00 78.00  ? 32  TRP B C   1 
ATOM   1339 O  O   . TRP B 1 32  ? -24.415 -10.637 19.604 1.00 77.23  ? 32  TRP B O   1 
ATOM   1340 C  CB  . TRP B 1 32  ? -26.289 -8.022  18.611 1.00 82.94  ? 32  TRP B CB  1 
ATOM   1341 C  CG  . TRP B 1 32  ? -27.202 -9.118  18.895 1.00 88.02  ? 32  TRP B CG  1 
ATOM   1342 C  CD1 . TRP B 1 32  ? -27.887 -9.339  20.072 1.00 92.57  ? 32  TRP B CD1 1 
ATOM   1343 C  CD2 . TRP B 1 32  ? -27.506 -10.214 18.027 1.00 92.56  ? 32  TRP B CD2 1 
ATOM   1344 N  NE1 . TRP B 1 32  ? -28.609 -10.514 19.977 1.00 96.12  ? 32  TRP B NE1 1 
ATOM   1345 C  CE2 . TRP B 1 32  ? -28.395 -11.072 18.735 1.00 96.07  ? 32  TRP B CE2 1 
ATOM   1346 C  CE3 . TRP B 1 32  ? -27.109 -10.567 16.723 1.00 92.90  ? 32  TRP B CE3 1 
ATOM   1347 C  CZ2 . TRP B 1 32  ? -28.898 -12.273 18.172 1.00 98.18  ? 32  TRP B CZ2 1 
ATOM   1348 C  CZ3 . TRP B 1 32  ? -27.614 -11.764 16.155 1.00 95.33  ? 32  TRP B CZ3 1 
ATOM   1349 C  CH2 . TRP B 1 32  ? -28.501 -12.597 16.884 1.00 97.83  ? 32  TRP B CH2 1 
ATOM   1350 N  N   . GLY B 1 33  ? -24.680 -8.943  21.036 1.00 77.97  ? 33  GLY B N   1 
ATOM   1351 C  CA  . GLY B 1 33  ? -24.532 -9.752  22.206 1.00 77.86  ? 33  GLY B CA  1 
ATOM   1352 C  C   . GLY B 1 33  ? -24.171 -8.866  23.367 1.00 77.76  ? 33  GLY B C   1 
ATOM   1353 O  O   . GLY B 1 33  ? -24.530 -7.705  23.398 1.00 79.03  ? 33  GLY B O   1 
ATOM   1354 N  N   . SER B 1 34  ? -23.430 -9.403  24.315 1.00 76.77  ? 34  SER B N   1 
ATOM   1355 C  CA  . SER B 1 34  ? -23.176 -8.687  25.534 1.00 77.33  ? 34  SER B CA  1 
ATOM   1356 C  C   . SER B 1 34  ? -21.888 -9.126  26.200 1.00 75.94  ? 34  SER B C   1 
ATOM   1357 O  O   . SER B 1 34  ? -21.621 -10.306 26.280 1.00 75.95  ? 34  SER B O   1 
ATOM   1358 C  CB  . SER B 1 34  ? -24.323 -8.955  26.473 1.00 79.74  ? 34  SER B CB  1 
ATOM   1359 O  OG  . SER B 1 34  ? -24.149 -8.182  27.621 1.00 81.63  ? 34  SER B OG  1 
ATOM   1360 N  N   . ILE B 1 35  ? -21.105 -8.185  26.692 1.00 75.48  ? 35  ILE B N   1 
ATOM   1361 C  CA  . ILE B 1 35  ? -19.872 -8.509  27.385 1.00 75.07  ? 35  ILE B CA  1 
ATOM   1362 C  C   . ILE B 1 35  ? -19.887 -7.880  28.735 1.00 77.18  ? 35  ILE B C   1 
ATOM   1363 O  O   . ILE B 1 35  ? -20.395 -6.787  28.853 1.00 78.65  ? 35  ILE B O   1 
ATOM   1364 C  CB  . ILE B 1 35  ? -18.676 -7.910  26.694 1.00 73.62  ? 35  ILE B CB  1 
ATOM   1365 C  CG1 . ILE B 1 35  ? -18.730 -8.180  25.199 1.00 72.06  ? 35  ILE B CG1 1 
ATOM   1366 C  CG2 . ILE B 1 35  ? -17.400 -8.454  27.314 1.00 73.40  ? 35  ILE B CG2 1 
ATOM   1367 C  CD1 . ILE B 1 35  ? -17.579 -7.628  24.472 1.00 71.12  ? 35  ILE B CD1 1 
ATOM   1368 N  N   . LYS B 1 36  ? -19.322 -8.526  29.750 1.00 78.12  ? 36  LYS B N   1 
ATOM   1369 C  CA  . LYS B 1 36  ? -19.305 -7.933  31.089 1.00 80.77  ? 36  LYS B CA  1 
ATOM   1370 C  C   . LYS B 1 36  ? -17.921 -7.965  31.654 1.00 80.60  ? 36  LYS B C   1 
ATOM   1371 O  O   . LYS B 1 36  ? -17.070 -8.657  31.144 1.00 79.22  ? 36  LYS B O   1 
ATOM   1372 C  CB  . LYS B 1 36  ? -20.309 -8.614  32.032 1.00 83.31  ? 36  LYS B CB  1 
ATOM   1373 C  CG  . LYS B 1 36  ? -20.331 -10.144 31.970 1.00 85.14  ? 36  LYS B CG  1 
ATOM   1374 C  CD  . LYS B 1 36  ? -21.297 -10.751 33.015 1.00 89.97  ? 36  LYS B CD  1 
ATOM   1375 C  CE  . LYS B 1 36  ? -20.906 -12.173 33.456 1.00 90.88  ? 36  LYS B CE  1 
ATOM   1376 N  NZ  . LYS B 1 36  ? -21.810 -12.635 34.539 1.00 93.98  ? 36  LYS B NZ  1 
ATOM   1377 N  N   . GLY B 1 37  ? -17.699 -7.188  32.702 1.00 82.75  ? 37  GLY B N   1 
ATOM   1378 C  CA  . GLY B 1 37  ? -16.397 -7.107  33.368 1.00 83.73  ? 37  GLY B CA  1 
ATOM   1379 C  C   . GLY B 1 37  ? -15.448 -6.103  32.743 1.00 82.94  ? 37  GLY B C   1 
ATOM   1380 O  O   . GLY B 1 37  ? -14.242 -6.299  32.736 1.00 82.96  ? 37  GLY B O   1 
ATOM   1381 N  N   . LEU B 1 38  ? -15.992 -5.014  32.229 1.00 82.72  ? 38  LEU B N   1 
ATOM   1382 C  CA  . LEU B 1 38  ? -15.205 -4.031  31.531 1.00 82.25  ? 38  LEU B CA  1 
ATOM   1383 C  C   . LEU B 1 38  ? -15.135 -2.779  32.368 1.00 84.92  ? 38  LEU B C   1 
ATOM   1384 O  O   . LEU B 1 38  ? -15.988 -2.547  33.242 1.00 86.69  ? 38  LEU B O   1 
ATOM   1385 C  CB  . LEU B 1 38  ? -15.864 -3.731  30.190 1.00 80.58  ? 38  LEU B CB  1 
ATOM   1386 C  CG  . LEU B 1 38  ? -15.644 -4.818  29.149 1.00 78.00  ? 38  LEU B CG  1 
ATOM   1387 C  CD1 . LEU B 1 38  ? -16.781 -4.896  28.159 1.00 76.20  ? 38  LEU B CD1 1 
ATOM   1388 C  CD2 . LEU B 1 38  ? -14.329 -4.564  28.450 1.00 77.81  ? 38  LEU B CD2 1 
ATOM   1389 N  N   . THR B 1 39  ? -14.108 -1.979  32.108 1.00 85.40  ? 39  THR B N   1 
ATOM   1390 C  CA  . THR B 1 39  ? -14.053 -0.637  32.652 1.00 88.07  ? 39  THR B CA  1 
ATOM   1391 C  C   . THR B 1 39  ? -15.052 0.221   31.895 1.00 88.08  ? 39  THR B C   1 
ATOM   1392 O  O   . THR B 1 39  ? -15.162 0.122   30.685 1.00 85.81  ? 39  THR B O   1 
ATOM   1393 C  CB  . THR B 1 39  ? -12.659 -0.068  32.519 1.00 89.01  ? 39  THR B CB  1 
ATOM   1394 O  OG1 . THR B 1 39  ? -11.953 -0.814  31.516 1.00 86.14  ? 39  THR B OG1 1 
ATOM   1395 C  CG2 . THR B 1 39  ? -11.930 -0.193  33.856 1.00 91.64  ? 39  THR B CG2 1 
ATOM   1396 N  N   . GLU B 1 40  ? -15.804 1.042   32.613 1.00 91.14  ? 40  GLU B N   1 
ATOM   1397 C  CA  . GLU B 1 40  ? -16.759 1.930   31.970 1.00 92.05  ? 40  GLU B CA  1 
ATOM   1398 C  C   . GLU B 1 40  ? -16.094 2.575   30.780 1.00 91.11  ? 40  GLU B C   1 
ATOM   1399 O  O   . GLU B 1 40  ? -14.920 2.871   30.825 1.00 91.87  ? 40  GLU B O   1 
ATOM   1400 C  CB  . GLU B 1 40  ? -17.246 3.012   32.948 1.00 96.07  ? 40  GLU B CB  1 
ATOM   1401 C  CG  . GLU B 1 40  ? -18.045 4.164   32.281 1.00 98.48  ? 40  GLU B CG  1 
ATOM   1402 C  CD  . GLU B 1 40  ? -19.021 4.880   33.231 1.00 103.76 ? 40  GLU B CD  1 
ATOM   1403 O  OE1 . GLU B 1 40  ? -18.592 5.302   34.345 1.00 107.32 ? 40  GLU B OE1 1 
ATOM   1404 O  OE2 . GLU B 1 40  ? -20.223 5.026   32.848 1.00 104.73 ? 40  GLU B OE2 1 
ATOM   1405 N  N   . GLY B 1 41  ? -16.832 2.773   29.701 1.00 89.96  ? 41  GLY B N   1 
ATOM   1406 C  CA  . GLY B 1 41  ? -16.304 3.525   28.562 1.00 89.71  ? 41  GLY B CA  1 
ATOM   1407 C  C   . GLY B 1 41  ? -16.029 2.703   27.328 1.00 86.47  ? 41  GLY B C   1 
ATOM   1408 O  O   . GLY B 1 41  ? -16.631 1.651   27.133 1.00 84.60  ? 41  GLY B O   1 
ATOM   1409 N  N   . LEU B 1 42  ? -15.132 3.199   26.480 1.00 86.10  ? 42  LEU B N   1 
ATOM   1410 C  CA  . LEU B 1 42  ? -14.914 2.586   25.167 1.00 83.64  ? 42  LEU B CA  1 
ATOM   1411 C  C   . LEU B 1 42  ? -13.872 1.500   25.202 1.00 81.33  ? 42  LEU B C   1 
ATOM   1412 O  O   . LEU B 1 42  ? -12.889 1.605   25.945 1.00 82.64  ? 42  LEU B O   1 
ATOM   1413 C  CB  . LEU B 1 42  ? -14.461 3.614   24.133 1.00 85.16  ? 42  LEU B CB  1 
ATOM   1414 C  CG  . LEU B 1 42  ? -15.523 4.570   23.586 1.00 87.25  ? 42  LEU B CG  1 
ATOM   1415 C  CD1 . LEU B 1 42  ? -15.358 6.000   24.193 1.00 91.63  ? 42  LEU B CD1 1 
ATOM   1416 C  CD2 . LEU B 1 42  ? -15.436 4.592   22.065 1.00 85.81  ? 42  LEU B CD2 1 
ATOM   1417 N  N   . HIS B 1 43  ? -14.077 0.479   24.365 1.00 78.14  ? 43  HIS B N   1 
ATOM   1418 C  CA  . HIS B 1 43  ? -13.134 -0.618  24.233 1.00 75.92  ? 43  HIS B CA  1 
ATOM   1419 C  C   . HIS B 1 43  ? -13.069 -1.110  22.817 1.00 73.74  ? 43  HIS B C   1 
ATOM   1420 O  O   . HIS B 1 43  ? -14.087 -1.344  22.195 1.00 72.43  ? 43  HIS B O   1 
ATOM   1421 C  CB  . HIS B 1 43  ? -13.537 -1.777  25.118 1.00 74.89  ? 43  HIS B CB  1 
ATOM   1422 C  CG  . HIS B 1 43  ? -13.372 -1.511  26.578 1.00 77.08  ? 43  HIS B CG  1 
ATOM   1423 N  ND1 . HIS B 1 43  ? -12.227 -1.843  27.268 1.00 79.04  ? 43  HIS B ND1 1 
ATOM   1424 C  CD2 . HIS B 1 43  ? -14.209 -0.953  27.484 1.00 79.39  ? 43  HIS B CD2 1 
ATOM   1425 C  CE1 . HIS B 1 43  ? -12.369 -1.513  28.541 1.00 81.89  ? 43  HIS B CE1 1 
ATOM   1426 N  NE2 . HIS B 1 43  ? -13.559 -0.960  28.696 1.00 82.06  ? 43  HIS B NE2 1 
ATOM   1427 N  N   . GLY B 1 44  ? -11.844 -1.273  22.333 1.00 73.49  ? 44  GLY B N   1 
ATOM   1428 C  CA  . GLY B 1 44  ? -11.579 -1.728  20.980 1.00 72.48  ? 44  GLY B CA  1 
ATOM   1429 C  C   . GLY B 1 44  ? -12.100 -3.117  20.756 1.00 70.29  ? 44  GLY B C   1 
ATOM   1430 O  O   . GLY B 1 44  ? -12.188 -3.874  21.676 1.00 69.83  ? 44  GLY B O   1 
ATOM   1431 N  N   . PHE B 1 45  ? -12.417 -3.454  19.519 1.00 69.64  ? 45  PHE B N   1 
ATOM   1432 C  CA  . PHE B 1 45  ? -13.203 -4.633  19.220 1.00 68.22  ? 45  PHE B CA  1 
ATOM   1433 C  C   . PHE B 1 45  ? -12.929 -5.061  17.787 1.00 67.96  ? 45  PHE B C   1 
ATOM   1434 O  O   . PHE B 1 45  ? -13.363 -4.413  16.848 1.00 68.25  ? 45  PHE B O   1 
ATOM   1435 C  CB  . PHE B 1 45  ? -14.661 -4.246  19.397 1.00 68.64  ? 45  PHE B CB  1 
ATOM   1436 C  CG  . PHE B 1 45  ? -15.631 -5.382  19.327 1.00 67.96  ? 45  PHE B CG  1 
ATOM   1437 C  CD1 . PHE B 1 45  ? -15.639 -6.357  20.275 1.00 67.65  ? 45  PHE B CD1 1 
ATOM   1438 C  CD2 . PHE B 1 45  ? -16.595 -5.430  18.336 1.00 68.47  ? 45  PHE B CD2 1 
ATOM   1439 C  CE1 . PHE B 1 45  ? -16.554 -7.390  20.201 1.00 67.59  ? 45  PHE B CE1 1 
ATOM   1440 C  CE2 . PHE B 1 45  ? -17.513 -6.446  18.286 1.00 67.84  ? 45  PHE B CE2 1 
ATOM   1441 C  CZ  . PHE B 1 45  ? -17.487 -7.425  19.211 1.00 67.56  ? 45  PHE B CZ  1 
ATOM   1442 N  N   . HIS B 1 46  ? -12.188 -6.149  17.622 1.00 67.55  ? 46  HIS B N   1 
ATOM   1443 C  CA  . HIS B 1 46  ? -11.701 -6.540  16.310 1.00 68.21  ? 46  HIS B CA  1 
ATOM   1444 C  C   . HIS B 1 46  ? -11.726 -8.021  16.074 1.00 67.00  ? 46  HIS B C   1 
ATOM   1445 O  O   . HIS B 1 46  ? -11.647 -8.801  16.997 1.00 66.30  ? 46  HIS B O   1 
ATOM   1446 C  CB  . HIS B 1 46  ? -10.260 -6.117  16.158 1.00 69.78  ? 46  HIS B CB  1 
ATOM   1447 C  CG  . HIS B 1 46  ? -9.984  -4.757  16.682 1.00 72.96  ? 46  HIS B CG  1 
ATOM   1448 N  ND1 . HIS B 1 46  ? -9.101  -4.527  17.711 1.00 75.79  ? 46  HIS B ND1 1 
ATOM   1449 C  CD2 . HIS B 1 46  ? -10.492 -3.552  16.336 1.00 76.42  ? 46  HIS B CD2 1 
ATOM   1450 C  CE1 . HIS B 1 46  ? -9.063  -3.229  17.963 1.00 78.83  ? 46  HIS B CE1 1 
ATOM   1451 N  NE2 . HIS B 1 46  ? -9.898  -2.615  17.145 1.00 78.34  ? 46  HIS B NE2 1 
ATOM   1452 N  N   . VAL B 1 47  ? -11.805 -8.391  14.810 1.00 67.24  ? 47  VAL B N   1 
ATOM   1453 C  CA  . VAL B 1 47  ? -11.507 -9.730  14.400 1.00 67.09  ? 47  VAL B CA  1 
ATOM   1454 C  C   . VAL B 1 47  ? -10.051 -9.751  14.059 1.00 68.51  ? 47  VAL B C   1 
ATOM   1455 O  O   . VAL B 1 47  ? -9.625  -8.964  13.226 1.00 69.86  ? 47  VAL B O   1 
ATOM   1456 C  CB  . VAL B 1 47  ? -12.257 -10.114 13.151 1.00 67.36  ? 47  VAL B CB  1 
ATOM   1457 C  CG1 . VAL B 1 47  ? -11.855 -11.492 12.718 1.00 67.51  ? 47  VAL B CG1 1 
ATOM   1458 C  CG2 . VAL B 1 47  ? -13.731 -10.064 13.414 1.00 66.54  ? 47  VAL B CG2 1 
ATOM   1459 N  N   . HIS B 1 48  ? -9.296  -10.644 14.697 1.00 68.96  ? 48  HIS B N   1 
ATOM   1460 C  CA  . HIS B 1 48  ? -7.883  -10.825 14.404 1.00 70.89  ? 48  HIS B CA  1 
ATOM   1461 C  C   . HIS B 1 48  ? -7.724  -12.013 13.488 1.00 71.57  ? 48  HIS B C   1 
ATOM   1462 O  O   . HIS B 1 48  ? -8.646  -12.797 13.341 1.00 70.73  ? 48  HIS B O   1 
ATOM   1463 C  CB  . HIS B 1 48  ? -7.100  -11.060 15.666 1.00 71.21  ? 48  HIS B CB  1 
ATOM   1464 C  CG  . HIS B 1 48  ? -7.015  -9.860  16.531 1.00 72.69  ? 48  HIS B CG  1 
ATOM   1465 N  ND1 . HIS B 1 48  ? -5.819  -9.362  16.983 1.00 75.61  ? 48  HIS B ND1 1 
ATOM   1466 C  CD2 . HIS B 1 48  ? -7.971  -9.035  17.009 1.00 73.43  ? 48  HIS B CD2 1 
ATOM   1467 C  CE1 . HIS B 1 48  ? -6.041  -8.289  17.718 1.00 76.89  ? 48  HIS B CE1 1 
ATOM   1468 N  NE2 . HIS B 1 48  ? -7.342  -8.069  17.751 1.00 74.95  ? 48  HIS B NE2 1 
ATOM   1469 N  N   . GLU B 1 49  ? -6.547  -12.147 12.882 1.00 73.57  ? 49  GLU B N   1 
ATOM   1470 C  CA  . GLU B 1 49  ? -6.339  -13.074 11.764 1.00 74.98  ? 49  GLU B CA  1 
ATOM   1471 C  C   . GLU B 1 49  ? -6.579  -14.522 12.090 1.00 74.31  ? 49  GLU B C   1 
ATOM   1472 O  O   . GLU B 1 49  ? -7.187  -15.203 11.294 1.00 74.04  ? 49  GLU B O   1 
ATOM   1473 C  CB  . GLU B 1 49  ? -4.931  -12.924 11.180 1.00 77.71  ? 49  GLU B CB  1 
ATOM   1474 C  CG  . GLU B 1 49  ? -4.786  -13.538 9.788  1.00 80.93  ? 49  GLU B CG  1 
ATOM   1475 C  CD  . GLU B 1 49  ? -3.482  -13.176 9.131  1.00 86.23  ? 49  GLU B CD  1 
ATOM   1476 O  OE1 . GLU B 1 49  ? -2.828  -12.197 9.585  1.00 88.69  ? 49  GLU B OE1 1 
ATOM   1477 O  OE2 . GLU B 1 49  ? -3.113  -13.896 8.172  1.00 89.78  ? 49  GLU B OE2 1 
ATOM   1478 N  N   . PHE B 1 50  ? -6.115  -14.985 13.248 1.00 74.29  ? 50  PHE B N   1 
ATOM   1479 C  CA  . PHE B 1 50  ? -6.051  -16.431 13.530 1.00 75.13  ? 50  PHE B CA  1 
ATOM   1480 C  C   . PHE B 1 50  ? -6.954  -16.967 14.644 1.00 73.62  ? 50  PHE B C   1 
ATOM   1481 O  O   . PHE B 1 50  ? -7.162  -16.296 15.656 1.00 72.46  ? 50  PHE B O   1 
ATOM   1482 C  CB  . PHE B 1 50  ? -4.613  -16.828 13.867 1.00 77.26  ? 50  PHE B CB  1 
ATOM   1483 C  CG  . PHE B 1 50  ? -3.612  -16.458 12.811 1.00 80.57  ? 50  PHE B CG  1 
ATOM   1484 C  CD1 . PHE B 1 50  ? -3.868  -16.719 11.472 1.00 82.33  ? 50  PHE B CD1 1 
ATOM   1485 C  CD2 . PHE B 1 50  ? -2.411  -15.887 13.156 1.00 83.55  ? 50  PHE B CD2 1 
ATOM   1486 C  CE1 . PHE B 1 50  ? -2.963  -16.399 10.513 1.00 85.06  ? 50  PHE B CE1 1 
ATOM   1487 C  CE2 . PHE B 1 50  ? -1.512  -15.557 12.196 1.00 86.40  ? 50  PHE B CE2 1 
ATOM   1488 C  CZ  . PHE B 1 50  ? -1.789  -15.815 10.870 1.00 87.17  ? 50  PHE B CZ  1 
ATOM   1489 N  N   . GLY B 1 51  ? -7.448  -18.196 14.451 1.00 73.96  ? 51  GLY B N   1 
ATOM   1490 C  CA  . GLY B 1 51  ? -8.205  -18.916 15.468 1.00 73.71  ? 51  GLY B CA  1 
ATOM   1491 C  C   . GLY B 1 51  ? -7.297  -19.672 16.421 1.00 75.28  ? 51  GLY B C   1 
ATOM   1492 O  O   . GLY B 1 51  ? -7.554  -20.805 16.807 1.00 75.91  ? 51  GLY B O   1 
ATOM   1493 N  N   . ASP B 1 52  ? -6.222  -19.017 16.812 1.00 76.37  ? 52  ASP B N   1 
ATOM   1494 C  CA  . ASP B 1 52  ? -5.190  -19.637 17.593 1.00 78.46  ? 52  ASP B CA  1 
ATOM   1495 C  C   . ASP B 1 52  ? -5.376  -19.117 18.971 1.00 77.92  ? 52  ASP B C   1 
ATOM   1496 O  O   . ASP B 1 52  ? -5.487  -17.924 19.171 1.00 76.99  ? 52  ASP B O   1 
ATOM   1497 C  CB  . ASP B 1 52  ? -3.832  -19.205 17.056 1.00 80.30  ? 52  ASP B CB  1 
ATOM   1498 C  CG  . ASP B 1 52  ? -2.798  -20.237 17.244 1.00 83.21  ? 52  ASP B CG  1 
ATOM   1499 O  OD1 . ASP B 1 52  ? -2.607  -20.637 18.412 1.00 83.75  ? 52  ASP B OD1 1 
ATOM   1500 O  OD2 . ASP B 1 52  ? -2.194  -20.625 16.209 1.00 85.77  ? 52  ASP B OD2 1 
ATOM   1501 N  N   . ASN B 1 53  ? -5.462  -20.013 19.923 1.00 79.17  ? 53  ASN B N   1 
ATOM   1502 C  CA  . ASN B 1 53  ? -5.488  -19.610 21.303 1.00 79.76  ? 53  ASN B CA  1 
ATOM   1503 C  C   . ASN B 1 53  ? -4.482  -20.393 22.079 1.00 82.00  ? 53  ASN B C   1 
ATOM   1504 O  O   . ASN B 1 53  ? -4.615  -20.535 23.292 1.00 82.84  ? 53  ASN B O   1 
ATOM   1505 C  CB  . ASN B 1 53  ? -6.876  -19.814 21.877 1.00 78.94  ? 53  ASN B CB  1 
ATOM   1506 C  CG  . ASN B 1 53  ? -7.746  -18.593 21.722 1.00 79.81  ? 53  ASN B CG  1 
ATOM   1507 O  OD1 . ASN B 1 53  ? -8.423  -18.206 22.669 1.00 84.72  ? 53  ASN B OD1 1 
ATOM   1508 N  ND2 . ASN B 1 53  ? -7.731  -17.963 20.531 1.00 79.71  ? 53  ASN B ND2 1 
ATOM   1509 N  N   . THR B 1 54  ? -3.475  -20.891 21.362 1.00 83.32  ? 54  THR B N   1 
ATOM   1510 C  CA  . THR B 1 54  ? -2.400  -21.676 21.926 1.00 86.15  ? 54  THR B CA  1 
ATOM   1511 C  C   . THR B 1 54  ? -1.852  -20.992 23.143 1.00 87.26  ? 54  THR B C   1 
ATOM   1512 O  O   . THR B 1 54  ? -1.861  -21.574 24.217 1.00 88.81  ? 54  THR B O   1 
ATOM   1513 C  CB  . THR B 1 54  ? -1.288  -21.837 20.909 1.00 87.90  ? 54  THR B CB  1 
ATOM   1514 O  OG1 . THR B 1 54  ? -1.840  -22.468 19.759 1.00 86.86  ? 54  THR B OG1 1 
ATOM   1515 C  CG2 . THR B 1 54  ? -0.103  -22.667 21.456 1.00 92.30  ? 54  THR B CG2 1 
ATOM   1516 N  N   . ALA B 1 55  ? -1.413  -19.746 22.977 1.00 86.94  ? 55  ALA B N   1 
ATOM   1517 C  CA  . ALA B 1 55  ? -0.840  -18.941 24.065 1.00 88.46  ? 55  ALA B CA  1 
ATOM   1518 C  C   . ALA B 1 55  ? -1.750  -17.785 24.402 1.00 86.31  ? 55  ALA B C   1 
ATOM   1519 O  O   . ALA B 1 55  ? -1.424  -16.639 24.135 1.00 85.99  ? 55  ALA B O   1 
ATOM   1520 C  CB  . ALA B 1 55  ? 0.519   -18.421 23.665 1.00 90.60  ? 55  ALA B CB  1 
ATOM   1521 N  N   . GLY B 1 56  ? -2.904  -18.096 24.971 1.00 85.53  ? 56  GLY B N   1 
ATOM   1522 C  CA  . GLY B 1 56  ? -3.927  -17.089 25.242 1.00 83.89  ? 56  GLY B CA  1 
ATOM   1523 C  C   . GLY B 1 56  ? -4.363  -16.304 24.003 1.00 81.89  ? 56  GLY B C   1 
ATOM   1524 O  O   . GLY B 1 56  ? -4.452  -16.844 22.891 1.00 81.05  ? 56  GLY B O   1 
ATOM   1525 N  N   . CYS B 1 57  ? -4.623  -15.017 24.197 1.00 81.28  ? 57  CYS B N   1 
ATOM   1526 C  CA  . CYS B 1 57  ? -5.109  -14.204 23.103 1.00 79.79  ? 57  CYS B CA  1 
ATOM   1527 C  C   . CYS B 1 57  ? -4.006  -13.748 22.142 1.00 80.50  ? 57  CYS B C   1 
ATOM   1528 O  O   . CYS B 1 57  ? -4.297  -13.467 20.977 1.00 79.23  ? 57  CYS B O   1 
ATOM   1529 C  CB  . CYS B 1 57  ? -5.924  -13.031 23.642 1.00 78.81  ? 57  CYS B CB  1 
ATOM   1530 S  SG  . CYS B 1 57  ? -7.499  -13.565 24.418 1.00 80.03  ? 57  CYS B SG  1 
ATOM   1531 N  N   . THR B 1 58  ? -2.751  -13.705 22.608 1.00 82.80  ? 58  THR B N   1 
ATOM   1532 C  CA  . THR B 1 58  ? -1.623  -13.242 21.774 1.00 84.21  ? 58  THR B CA  1 
ATOM   1533 C  C   . THR B 1 58  ? -1.450  -14.095 20.526 1.00 84.02  ? 58  THR B C   1 
ATOM   1534 O  O   . THR B 1 58  ? -0.966  -13.620 19.509 1.00 84.74  ? 58  THR B O   1 
ATOM   1535 C  CB  . THR B 1 58  ? -0.263  -13.257 22.520 1.00 87.33  ? 58  THR B CB  1 
ATOM   1536 O  OG1 . THR B 1 58  ? -0.478  -13.421 23.915 1.00 87.67  ? 58  THR B OG1 1 
ATOM   1537 C  CG2 . THR B 1 58  ? 0.518   -11.959 22.262 1.00 88.44  ? 58  THR B CG2 1 
ATOM   1538 N  N   . SER B 1 59  ? -1.831  -15.357 20.611 1.00 83.47  ? 59  SER B N   1 
ATOM   1539 C  CA  . SER B 1 59  ? -1.749  -16.270 19.470 1.00 83.68  ? 59  SER B CA  1 
ATOM   1540 C  C   . SER B 1 59  ? -2.621  -15.858 18.277 1.00 81.56  ? 59  SER B C   1 
ATOM   1541 O  O   . SER B 1 59  ? -2.337  -16.257 17.129 1.00 82.28  ? 59  SER B O   1 
ATOM   1542 C  CB  . SER B 1 59  ? -2.158  -17.665 19.909 1.00 83.89  ? 59  SER B CB  1 
ATOM   1543 O  OG  . SER B 1 59  ? -1.499  -17.999 21.115 1.00 86.61  ? 59  SER B OG  1 
ATOM   1544 N  N   . ALA B 1 60  ? -3.672  -15.078 18.552 1.00 79.33  ? 60  ALA B N   1 
ATOM   1545 C  CA  . ALA B 1 60  ? -4.603  -14.590 17.530 1.00 77.68  ? 60  ALA B CA  1 
ATOM   1546 C  C   . ALA B 1 60  ? -3.913  -13.811 16.412 1.00 78.76  ? 60  ALA B C   1 
ATOM   1547 O  O   . ALA B 1 60  ? -4.378  -13.818 15.270 1.00 78.31  ? 60  ALA B O   1 
ATOM   1548 C  CB  . ALA B 1 60  ? -5.649  -13.726 18.174 1.00 75.97  ? 60  ALA B CB  1 
ATOM   1549 N  N   . GLY B 1 61  ? -2.810  -13.148 16.753 1.00 80.55  ? 61  GLY B N   1 
ATOM   1550 C  CA  . GLY B 1 61  ? -2.001  -12.411 15.794 1.00 82.39  ? 61  GLY B CA  1 
ATOM   1551 C  C   . GLY B 1 61  ? -2.574  -11.031 15.556 1.00 81.71  ? 61  GLY B C   1 
ATOM   1552 O  O   . GLY B 1 61  ? -3.412  -10.571 16.318 1.00 80.25  ? 61  GLY B O   1 
ATOM   1553 N  N   . PRO B 1 62  ? -2.163  -10.378 14.469 1.00 83.20  ? 62  PRO B N   1 
ATOM   1554 C  CA  . PRO B 1 62  ? -2.579  -9.031  14.205 1.00 83.12  ? 62  PRO B CA  1 
ATOM   1555 C  C   . PRO B 1 62  ? -3.999  -8.979  13.701 1.00 81.15  ? 62  PRO B C   1 
ATOM   1556 O  O   . PRO B 1 62  ? -4.620  -10.008 13.494 1.00 79.73  ? 62  PRO B O   1 
ATOM   1557 C  CB  . PRO B 1 62  ? -1.673  -8.642  13.067 1.00 85.94  ? 62  PRO B CB  1 
ATOM   1558 C  CG  . PRO B 1 62  ? -1.582  -9.913  12.252 1.00 86.08  ? 62  PRO B CG  1 
ATOM   1559 C  CD  . PRO B 1 62  ? -1.595  -11.012 13.263 1.00 85.00  ? 62  PRO B CD  1 
ATOM   1560 N  N   . HIS B 1 63  ? -4.485  -7.774  13.462 1.00 81.43  ? 63  HIS B N   1 
ATOM   1561 C  CA  . HIS B 1 63  ? -5.819  -7.586  12.946 1.00 80.30  ? 63  HIS B CA  1 
ATOM   1562 C  C   . HIS B 1 63  ? -5.989  -8.269  11.619 1.00 80.09  ? 63  HIS B C   1 
ATOM   1563 O  O   . HIS B 1 63  ? -5.074  -8.281  10.816 1.00 82.00  ? 63  HIS B O   1 
ATOM   1564 C  CB  . HIS B 1 63  ? -6.074  -6.120  12.728 1.00 81.76  ? 63  HIS B CB  1 
ATOM   1565 C  CG  . HIS B 1 63  ? -6.207  -5.341  13.986 1.00 83.30  ? 63  HIS B CG  1 
ATOM   1566 N  ND1 . HIS B 1 63  ? -7.106  -4.304  14.110 1.00 84.61  ? 63  HIS B ND1 1 
ATOM   1567 C  CD2 . HIS B 1 63  ? -5.580  -5.450  15.182 1.00 85.69  ? 63  HIS B CD2 1 
ATOM   1568 C  CE1 . HIS B 1 63  ? -7.022  -3.800  15.329 1.00 86.01  ? 63  HIS B CE1 1 
ATOM   1569 N  NE2 . HIS B 1 63  ? -6.109  -4.482  16.002 1.00 87.05  ? 63  HIS B NE2 1 
ATOM   1570 N  N   . PHE B 1 64  ? -7.179  -8.808  11.394 1.00 78.01  ? 64  PHE B N   1 
ATOM   1571 C  CA  . PHE B 1 64  ? -7.485  -9.496  10.163 1.00 78.38  ? 64  PHE B CA  1 
ATOM   1572 C  C   . PHE B 1 64  ? -7.434  -8.505  9.061  1.00 79.80  ? 64  PHE B C   1 
ATOM   1573 O  O   . PHE B 1 64  ? -8.261  -7.608  8.987  1.00 79.19  ? 64  PHE B O   1 
ATOM   1574 C  CB  . PHE B 1 64  ? -8.877  -10.112 10.205 1.00 77.12  ? 64  PHE B CB  1 
ATOM   1575 C  CG  . PHE B 1 64  ? -9.260  -10.874 8.947  1.00 78.86  ? 64  PHE B CG  1 
ATOM   1576 C  CD1 . PHE B 1 64  ? -8.350  -11.656 8.281  1.00 81.38  ? 64  PHE B CD1 1 
ATOM   1577 C  CD2 . PHE B 1 64  ? -10.557 -10.840 8.467  1.00 79.38  ? 64  PHE B CD2 1 
ATOM   1578 C  CE1 . PHE B 1 64  ? -8.717  -12.365 7.151  1.00 82.61  ? 64  PHE B CE1 1 
ATOM   1579 C  CE2 . PHE B 1 64  ? -10.922 -11.557 7.333  1.00 81.27  ? 64  PHE B CE2 1 
ATOM   1580 C  CZ  . PHE B 1 64  ? -10.001 -12.317 6.681  1.00 82.47  ? 64  PHE B CZ  1 
ATOM   1581 N  N   . ASN B 1 65  ? -6.459  -8.666  8.189  1.00 81.95  ? 65  ASN B N   1 
ATOM   1582 C  CA  . ASN B 1 65  ? -6.186  -7.641  7.198  1.00 84.49  ? 65  ASN B CA  1 
ATOM   1583 C  C   . ASN B 1 65  ? -5.726  -8.232  5.878  1.00 86.88  ? 65  ASN B C   1 
ATOM   1584 O  O   . ASN B 1 65  ? -4.557  -8.180  5.536  1.00 89.10  ? 65  ASN B O   1 
ATOM   1585 C  CB  . ASN B 1 65  ? -5.138  -6.670  7.764  1.00 85.71  ? 65  ASN B CB  1 
ATOM   1586 C  CG  . ASN B 1 65  ? -4.896  -5.526  6.875  1.00 87.49  ? 65  ASN B CG  1 
ATOM   1587 O  OD1 . ASN B 1 65  ? -5.675  -5.277  5.944  1.00 88.21  ? 65  ASN B OD1 1 
ATOM   1588 N  ND2 . ASN B 1 65  ? -3.817  -4.811  7.133  1.00 87.44  ? 65  ASN B ND2 1 
ATOM   1589 N  N   . PRO B 1 66  ? -6.659  -8.783  5.122  1.00 86.98  ? 66  PRO B N   1 
ATOM   1590 C  CA  . PRO B 1 66  ? -6.335  -9.539  3.931  1.00 89.47  ? 66  PRO B CA  1 
ATOM   1591 C  C   . PRO B 1 66  ? -6.012  -8.665  2.738  1.00 93.18  ? 66  PRO B C   1 
ATOM   1592 O  O   . PRO B 1 66  ? -5.347  -9.136  1.816  1.00 95.96  ? 66  PRO B O   1 
ATOM   1593 C  CB  . PRO B 1 66  ? -7.599  -10.340 3.669  1.00 88.16  ? 66  PRO B CB  1 
ATOM   1594 C  CG  . PRO B 1 66  ? -8.661  -9.467  4.141  1.00 86.95  ? 66  PRO B CG  1 
ATOM   1595 C  CD  . PRO B 1 66  ? -8.102  -8.622  5.282  1.00 85.52  ? 66  PRO B CD  1 
ATOM   1596 N  N   . LEU B 1 67  ? -6.469  -7.410  2.743  1.00 93.85  ? 67  LEU B N   1 
ATOM   1597 C  CA  . LEU B 1 67  ? -6.149  -6.467  1.658  1.00 97.62  ? 67  LEU B CA  1 
ATOM   1598 C  C   . LEU B 1 67  ? -4.936  -5.573  1.989  1.00 99.41  ? 67  LEU B C   1 
ATOM   1599 O  O   . LEU B 1 67  ? -4.669  -4.606  1.276  1.00 102.68 ? 67  LEU B O   1 
ATOM   1600 C  CB  . LEU B 1 67  ? -7.351  -5.574  1.344  1.00 97.89  ? 67  LEU B CB  1 
ATOM   1601 C  CG  . LEU B 1 67  ? -8.757  -6.169  1.289  1.00 96.47  ? 67  LEU B CG  1 
ATOM   1602 C  CD1 . LEU B 1 67  ? -9.732  -5.151  1.978  1.00 95.58  ? 67  LEU B CD1 1 
ATOM   1603 C  CD2 . LEU B 1 67  ? -9.170  -6.600  -0.148 1.00 98.17  ? 67  LEU B CD2 1 
ATOM   1604 N  N   . SER B 1 68  ? -4.226  -5.883  3.071  1.00 97.89  ? 68  SER B N   1 
ATOM   1605 C  CA  . SER B 1 68  ? -3.033  -5.135  3.485  1.00 99.80  ? 68  SER B CA  1 
ATOM   1606 C  C   . SER B 1 68  ? -3.217  -3.627  3.610  1.00 101.27 ? 68  SER B C   1 
ATOM   1607 O  O   . SER B 1 68  ? -2.371  -2.873  3.197  1.00 104.50 ? 68  SER B O   1 
ATOM   1608 C  CB  . SER B 1 68  ? -1.875  -5.427  2.544  1.00 103.49 ? 68  SER B CB  1 
ATOM   1609 O  OG  . SER B 1 68  ? -1.347  -6.680  2.845  1.00 102.73 ? 68  SER B OG  1 
ATOM   1610 N  N   . ARG B 1 69  ? -4.315  -3.193  4.205  1.00 99.53  ? 69  ARG B N   1 
ATOM   1611 C  CA  . ARG B 1 69  ? -4.558  -1.771  4.451  1.00 101.33 ? 69  ARG B CA  1 
ATOM   1612 C  C   . ARG B 1 69  ? -4.008  -1.322  5.793  1.00 100.17 ? 69  ARG B C   1 
ATOM   1613 O  O   . ARG B 1 69  ? -3.475  -2.109  6.551  1.00 98.50  ? 69  ARG B O   1 
ATOM   1614 C  CB  . ARG B 1 69  ? -6.054  -1.475  4.428  1.00 100.21 ? 69  ARG B CB  1 
ATOM   1615 C  CG  . ARG B 1 69  ? -6.783  -1.972  3.176  1.00 103.08 ? 69  ARG B CG  1 
ATOM   1616 C  CD  . ARG B 1 69  ? -6.541  -1.093  1.972  1.00 109.99 ? 69  ARG B CD  1 
ATOM   1617 N  NE  . ARG B 1 69  ? -7.294  -1.578  0.810  1.00 113.48 ? 69  ARG B NE  1 
ATOM   1618 C  CZ  . ARG B 1 69  ? -8.600  -1.387  0.618  1.00 114.51 ? 69  ARG B CZ  1 
ATOM   1619 N  NH1 . ARG B 1 69  ? -9.333  -0.706  1.502  1.00 113.64 ? 69  ARG B NH1 1 
ATOM   1620 N  NH2 . ARG B 1 69  ? -9.176  -1.851  -0.484 1.00 116.58 ? 69  ARG B NH2 1 
ATOM   1621 N  N   . LYS B 1 70  ? -4.118  -0.027  6.053  1.00 101.76 ? 70  LYS B N   1 
ATOM   1622 C  CA  . LYS B 1 70  ? -3.755  0.554   7.345  1.00 101.15 ? 70  LYS B CA  1 
ATOM   1623 C  C   . LYS B 1 70  ? -4.989  0.486   8.241  1.00 96.95  ? 70  LYS B C   1 
ATOM   1624 O  O   . LYS B 1 70  ? -6.121  0.485   7.750  1.00 95.60  ? 70  LYS B O   1 
ATOM   1625 C  CB  . LYS B 1 70  ? -3.278  2.033   7.217  1.00 105.45 ? 70  LYS B CB  1 
ATOM   1626 C  CG  . LYS B 1 70  ? -2.309  2.388   6.033  1.00 111.40 ? 70  LYS B CG  1 
ATOM   1627 C  CD  . LYS B 1 70  ? -0.827  2.660   6.451  1.00 116.26 ? 70  LYS B CD  1 
ATOM   1628 C  CE  . LYS B 1 70  ? -0.243  3.844   5.609  1.00 122.87 ? 70  LYS B CE  1 
ATOM   1629 N  NZ  . LYS B 1 70  ? 1.232   4.057   5.673  1.00 127.41 ? 70  LYS B NZ  1 
ATOM   1630 N  N   . HIS B 1 71  ? -4.756  0.458   9.552  1.00 94.79  ? 71  HIS B N   1 
ATOM   1631 C  CA  . HIS B 1 71  ? -5.840  0.339   10.512 1.00 91.43  ? 71  HIS B CA  1 
ATOM   1632 C  C   . HIS B 1 71  ? -6.756  1.539   10.389 1.00 92.41  ? 71  HIS B C   1 
ATOM   1633 O  O   . HIS B 1 71  ? -6.311  2.618   10.058 1.00 95.42  ? 71  HIS B O   1 
ATOM   1634 C  CB  . HIS B 1 71  ? -5.293  0.202   11.950 1.00 90.30  ? 71  HIS B CB  1 
ATOM   1635 C  CG  . HIS B 1 71  ? -6.357  0.169   13.015 1.00 87.27  ? 71  HIS B CG  1 
ATOM   1636 N  ND1 . HIS B 1 71  ? -7.156  -0.930  13.241 1.00 84.13  ? 71  HIS B ND1 1 
ATOM   1637 C  CD2 . HIS B 1 71  ? -6.751  1.106   13.908 1.00 86.90  ? 71  HIS B CD2 1 
ATOM   1638 C  CE1 . HIS B 1 71  ? -8.006  -0.661  14.214 1.00 82.48  ? 71  HIS B CE1 1 
ATOM   1639 N  NE2 . HIS B 1 71  ? -7.776  0.566   14.640 1.00 83.99  ? 71  HIS B NE2 1 
ATOM   1640 N  N   . GLY B 1 72  ? -8.038  1.332   10.645 1.00 90.32  ? 72  GLY B N   1 
ATOM   1641 C  CA  . GLY B 1 72  ? -8.990  2.429   10.707 1.00 91.74  ? 72  GLY B CA  1 
ATOM   1642 C  C   . GLY B 1 72  ? -10.225 2.122   11.552 1.00 89.64  ? 72  GLY B C   1 
ATOM   1643 O  O   . GLY B 1 72  ? -10.311 1.085   12.243 1.00 87.37  ? 72  GLY B O   1 
ATOM   1644 N  N   . GLY B 1 73  ? -11.183 3.044   11.513 1.00 91.15  ? 73  GLY B N   1 
ATOM   1645 C  CA  . GLY B 1 73  ? -12.487 2.837   12.130 1.00 89.54  ? 73  GLY B CA  1 
ATOM   1646 C  C   . GLY B 1 73  ? -13.350 2.040   11.184 1.00 88.89  ? 73  GLY B C   1 
ATOM   1647 O  O   . GLY B 1 73  ? -13.016 1.875   10.029 1.00 90.25  ? 73  GLY B O   1 
ATOM   1648 N  N   . PRO B 1 74  ? -14.485 1.561   11.653 1.00 87.64  ? 74  PRO B N   1 
ATOM   1649 C  CA  . PRO B 1 74  ? -15.229 0.643   10.817 1.00 87.14  ? 74  PRO B CA  1 
ATOM   1650 C  C   . PRO B 1 74  ? -15.891 1.332   9.646  1.00 90.11  ? 74  PRO B C   1 
ATOM   1651 O  O   . PRO B 1 74  ? -16.015 0.743   8.584  1.00 90.41  ? 74  PRO B O   1 
ATOM   1652 C  CB  . PRO B 1 74  ? -16.276 0.080   11.776 1.00 85.36  ? 74  PRO B CB  1 
ATOM   1653 C  CG  . PRO B 1 74  ? -16.514 1.181   12.770 1.00 86.63  ? 74  PRO B CG  1 
ATOM   1654 C  CD  . PRO B 1 74  ? -15.272 2.047   12.797 1.00 87.67  ? 74  PRO B CD  1 
ATOM   1655 N  N   . LYS B 1 75  ? -16.311 2.574   9.842  1.00 92.79  ? 75  LYS B N   1 
ATOM   1656 C  CA  . LYS B 1 75  ? -16.961 3.318   8.789  1.00 96.69  ? 75  LYS B CA  1 
ATOM   1657 C  C   . LYS B 1 75  ? -15.918 4.042   7.931  1.00 99.03  ? 75  LYS B C   1 
ATOM   1658 O  O   . LYS B 1 75  ? -16.244 4.543   6.860  1.00 101.93 ? 75  LYS B O   1 
ATOM   1659 C  CB  . LYS B 1 75  ? -17.984 4.291   9.378  1.00 98.86  ? 75  LYS B CB  1 
ATOM   1660 C  CG  . LYS B 1 75  ? -19.186 3.605   10.111 1.00 99.98  ? 75  LYS B CG  1 
ATOM   1661 C  CD  . LYS B 1 75  ? -20.362 4.582   10.413 1.00 106.29 ? 75  LYS B CD  1 
ATOM   1662 C  CE  . LYS B 1 75  ? -19.844 6.036   10.809 1.00 110.81 ? 75  LYS B CE  1 
ATOM   1663 N  NZ  . LYS B 1 75  ? -20.870 7.128   11.106 1.00 114.39 ? 75  LYS B NZ  1 
ATOM   1664 N  N   . ASP B 1 76  ? -14.666 4.085   8.387  1.00 98.16  ? 76  ASP B N   1 
ATOM   1665 C  CA  . ASP B 1 76  ? -13.584 4.621   7.572  1.00 100.74 ? 76  ASP B CA  1 
ATOM   1666 C  C   . ASP B 1 76  ? -13.451 3.785   6.330  1.00 101.10 ? 76  ASP B C   1 
ATOM   1667 O  O   . ASP B 1 76  ? -13.940 2.661   6.266  1.00 98.47  ? 76  ASP B O   1 
ATOM   1668 C  CB  . ASP B 1 76  ? -12.245 4.674   8.325  1.00 100.02 ? 76  ASP B CB  1 
ATOM   1669 C  CG  . ASP B 1 76  ? -12.086 5.948   9.153  1.00 102.75 ? 76  ASP B CG  1 
ATOM   1670 O  OD1 . ASP B 1 76  ? -12.266 7.041   8.587  1.00 107.80 ? 76  ASP B OD1 1 
ATOM   1671 O  OD2 . ASP B 1 76  ? -11.771 5.885   10.365 1.00 101.77 ? 76  ASP B OD2 1 
ATOM   1672 N  N   . GLU B 1 77  ? -12.826 4.363   5.319  1.00 104.84 ? 77  GLU B N   1 
ATOM   1673 C  CA  . GLU B 1 77  ? -12.663 3.676   4.062  1.00 106.40 ? 77  GLU B CA  1 
ATOM   1674 C  C   . GLU B 1 77  ? -11.357 2.879   4.066  1.00 104.58 ? 77  GLU B C   1 
ATOM   1675 O  O   . GLU B 1 77  ? -11.353 1.699   3.737  1.00 102.80 ? 77  GLU B O   1 
ATOM   1676 C  CB  . GLU B 1 77  ? -12.688 4.664   2.915  1.00 111.80 ? 77  GLU B CB  1 
ATOM   1677 C  CG  . GLU B 1 77  ? -12.758 3.965   1.555  1.00 116.54 ? 77  GLU B CG  1 
ATOM   1678 C  CD  . GLU B 1 77  ? -11.741 4.539   0.550  1.00 125.66 ? 77  GLU B CD  1 
ATOM   1679 O  OE1 . GLU B 1 77  ? -11.919 5.756   0.150  1.00 130.84 ? 77  GLU B OE1 1 
ATOM   1680 O  OE2 . GLU B 1 77  ? -10.775 3.753   0.193  1.00 128.35 ? 77  GLU B OE2 1 
ATOM   1681 N  N   . GLU B 1 78  ? -10.252 3.528   4.424  1.00 105.32 ? 78  GLU B N   1 
ATOM   1682 C  CA  . GLU B 1 78  ? -8.995  2.815   4.704  1.00 103.83 ? 78  GLU B CA  1 
ATOM   1683 C  C   . GLU B 1 78  ? -9.080  2.148   6.097  1.00 99.01  ? 78  GLU B C   1 
ATOM   1684 O  O   . GLU B 1 78  ? -8.913  2.807   7.146  1.00 98.36  ? 78  GLU B O   1 
ATOM   1685 C  CB  . GLU B 1 78  ? -7.776  3.757   4.603  1.00 107.42 ? 78  GLU B CB  1 
ATOM   1686 C  CG  . GLU B 1 78  ? -6.387  3.069   4.740  1.00 108.28 ? 78  GLU B CG  1 
ATOM   1687 C  CD  . GLU B 1 78  ? -5.879  2.401   3.418  1.00 112.30 ? 78  GLU B CD  1 
ATOM   1688 O  OE1 . GLU B 1 78  ? -6.680  2.180   2.486  1.00 114.63 ? 78  GLU B OE1 1 
ATOM   1689 O  OE2 . GLU B 1 78  ? -4.669  2.095   3.296  1.00 113.88 ? 78  GLU B OE2 1 
ATOM   1690 N  N   . ARG B 1 79  ? -9.347  0.833   6.076  1.00 95.50  ? 79  ARG B N   1 
ATOM   1691 C  CA  . ARG B 1 79  ? -9.466  0.017   7.287  1.00 91.25  ? 79  ARG B CA  1 
ATOM   1692 C  C   . ARG B 1 79  ? -9.143  -1.469  7.067  1.00 88.91  ? 79  ARG B C   1 
ATOM   1693 O  O   . ARG B 1 79  ? -9.206  -2.001  5.935  1.00 89.81  ? 79  ARG B O   1 
ATOM   1694 C  CB  . ARG B 1 79  ? -10.885 0.076   7.812  1.00 89.55  ? 79  ARG B CB  1 
ATOM   1695 C  CG  . ARG B 1 79  ? -11.887 -0.601  6.858  1.00 90.15  ? 79  ARG B CG  1 
ATOM   1696 C  CD  . ARG B 1 79  ? -13.289 -0.773  7.486  1.00 89.24  ? 79  ARG B CD  1 
ATOM   1697 N  NE  . ARG B 1 79  ? -13.426 -2.011  8.280  1.00 86.66  ? 79  ARG B NE  1 
ATOM   1698 C  CZ  . ARG B 1 79  ? -14.589 -2.578  8.626  1.00 85.25  ? 79  ARG B CZ  1 
ATOM   1699 N  NH1 . ARG B 1 79  ? -15.753 -2.037  8.273  1.00 86.01  ? 79  ARG B NH1 1 
ATOM   1700 N  NH2 . ARG B 1 79  ? -14.590 -3.700  9.335  1.00 83.46  ? 79  ARG B NH2 1 
ATOM   1701 N  N   . HIS B 1 80  ? -8.843  -2.136  8.186  1.00 85.71  ? 80  HIS B N   1 
ATOM   1702 C  CA  . HIS B 1 80  ? -8.669  -3.577  8.189  1.00 83.19  ? 80  HIS B CA  1 
ATOM   1703 C  C   . HIS B 1 80  ? -10.060 -4.192  8.138  1.00 80.79  ? 80  HIS B C   1 
ATOM   1704 O  O   . HIS B 1 80  ? -10.991 -3.699  8.781  1.00 79.49  ? 80  HIS B O   1 
ATOM   1705 C  CB  . HIS B 1 80  ? -7.937  -4.077  9.439  1.00 81.29  ? 80  HIS B CB  1 
ATOM   1706 C  CG  . HIS B 1 80  ? -6.543  -3.557  9.595  1.00 83.28  ? 80  HIS B CG  1 
ATOM   1707 N  ND1 . HIS B 1 80  ? -5.891  -3.532  10.809 1.00 83.30  ? 80  HIS B ND1 1 
ATOM   1708 C  CD2 . HIS B 1 80  ? -5.672  -3.050  8.698  1.00 87.02  ? 80  HIS B CD2 1 
ATOM   1709 C  CE1 . HIS B 1 80  ? -4.676  -3.043  10.651 1.00 86.49  ? 80  HIS B CE1 1 
ATOM   1710 N  NE2 . HIS B 1 80  ? -4.519  -2.737  9.380  1.00 88.82  ? 80  HIS B NE2 1 
ATOM   1711 N  N   . VAL B 1 81  ? -10.197 -5.269  7.373  1.00 79.98  ? 81  VAL B N   1 
ATOM   1712 C  CA  . VAL B 1 81  ? -11.442 -6.010  7.346  1.00 77.86  ? 81  VAL B CA  1 
ATOM   1713 C  C   . VAL B 1 81  ? -11.914 -6.282  8.744  1.00 74.62  ? 81  VAL B C   1 
ATOM   1714 O  O   . VAL B 1 81  ? -13.084 -6.272  8.999  1.00 73.62  ? 81  VAL B O   1 
ATOM   1715 C  CB  . VAL B 1 81  ? -11.320 -7.338  6.564  1.00 78.06  ? 81  VAL B CB  1 
ATOM   1716 C  CG1 . VAL B 1 81  ? -12.595 -8.120  6.624  1.00 76.05  ? 81  VAL B CG1 1 
ATOM   1717 C  CG2 . VAL B 1 81  ? -10.998 -7.061  5.117  1.00 81.53  ? 81  VAL B CG2 1 
ATOM   1718 N  N   . GLY B 1 82  ? -11.001 -6.507  9.661  1.00 73.35  ? 82  GLY B N   1 
ATOM   1719 C  CA  . GLY B 1 82  ? -11.382 -6.844  11.025 1.00 71.43  ? 82  GLY B CA  1 
ATOM   1720 C  C   . GLY B 1 82  ? -11.648 -5.701  11.986 1.00 71.33  ? 82  GLY B C   1 
ATOM   1721 O  O   . GLY B 1 82  ? -11.818 -5.944  13.177 1.00 69.67  ? 82  GLY B O   1 
ATOM   1722 N  N   . ASP B 1 83  ? -11.660 -4.458  11.505 1.00 73.33  ? 83  ASP B N   1 
ATOM   1723 C  CA  . ASP B 1 83  ? -11.737 -3.302  12.412 1.00 73.88  ? 83  ASP B CA  1 
ATOM   1724 C  C   . ASP B 1 83  ? -13.171 -2.961  12.625 1.00 73.59  ? 83  ASP B C   1 
ATOM   1725 O  O   . ASP B 1 83  ? -13.759 -2.297  11.807 1.00 75.48  ? 83  ASP B O   1 
ATOM   1726 C  CB  . ASP B 1 83  ? -11.027 -2.064  11.847 1.00 76.42  ? 83  ASP B CB  1 
ATOM   1727 C  CG  . ASP B 1 83  ? -9.529  -2.238  11.719 1.00 77.56  ? 83  ASP B CG  1 
ATOM   1728 O  OD1 . ASP B 1 83  ? -8.911  -2.944  12.528 1.00 76.20  ? 83  ASP B OD1 1 
ATOM   1729 O  OD2 . ASP B 1 83  ? -8.947  -1.655  10.790 1.00 80.34  ? 83  ASP B OD2 1 
ATOM   1730 N  N   . LEU B 1 84  ? -13.741 -3.408  13.727 1.00 72.19  ? 84  LEU B N   1 
ATOM   1731 C  CA  . LEU B 1 84  ? -15.124 -3.063  14.054 1.00 72.38  ? 84  LEU B CA  1 
ATOM   1732 C  C   . LEU B 1 84  ? -15.197 -1.889  15.039 1.00 73.26  ? 84  LEU B C   1 
ATOM   1733 O  O   . LEU B 1 84  ? -16.221 -1.644  15.683 1.00 73.12  ? 84  LEU B O   1 
ATOM   1734 C  CB  . LEU B 1 84  ? -15.850 -4.292  14.602 1.00 70.65  ? 84  LEU B CB  1 
ATOM   1735 C  CG  . LEU B 1 84  ? -15.839 -5.470  13.627 1.00 69.86  ? 84  LEU B CG  1 
ATOM   1736 C  CD1 . LEU B 1 84  ? -16.541 -6.629  14.264 1.00 67.18  ? 84  LEU B CD1 1 
ATOM   1737 C  CD2 . LEU B 1 84  ? -16.465 -5.119  12.281 1.00 71.19  ? 84  LEU B CD2 1 
ATOM   1738 N  N   . GLY B 1 85  ? -14.111 -1.142  15.142 1.00 74.51  ? 85  GLY B N   1 
ATOM   1739 C  CA  . GLY B 1 85  ? -14.099 -0.013  16.037 1.00 75.92  ? 85  GLY B CA  1 
ATOM   1740 C  C   . GLY B 1 85  ? -14.340 -0.386  17.482 1.00 74.51  ? 85  GLY B C   1 
ATOM   1741 O  O   . GLY B 1 85  ? -13.687 -1.265  17.993 1.00 73.26  ? 85  GLY B O   1 
ATOM   1742 N  N   . ASN B 1 86  ? -15.270 0.287   18.140 1.00 75.18  ? 86  ASN B N   1 
ATOM   1743 C  CA  . ASN B 1 86  ? -15.379 0.188   19.582 1.00 74.97  ? 86  ASN B CA  1 
ATOM   1744 C  C   . ASN B 1 86  ? -16.711 -0.307  20.032 1.00 74.23  ? 86  ASN B C   1 
ATOM   1745 O  O   . ASN B 1 86  ? -17.659 -0.329  19.267 1.00 74.51  ? 86  ASN B O   1 
ATOM   1746 C  CB  . ASN B 1 86  ? -15.165 1.545   20.227 1.00 77.51  ? 86  ASN B CB  1 
ATOM   1747 C  CG  . ASN B 1 86  ? -13.746 2.020   20.125 1.00 79.17  ? 86  ASN B CG  1 
ATOM   1748 O  OD1 . ASN B 1 86  ? -12.856 1.540   20.815 1.00 80.74  ? 86  ASN B OD1 1 
ATOM   1749 N  ND2 . ASN B 1 86  ? -13.528 2.992   19.277 1.00 82.35  ? 86  ASN B ND2 1 
ATOM   1750 N  N   . VAL B 1 87  ? -16.748 -0.713  21.295 1.00 73.69  ? 87  VAL B N   1 
ATOM   1751 C  CA  . VAL B 1 87  ? -17.974 -1.053  21.994 1.00 73.75  ? 87  VAL B CA  1 
ATOM   1752 C  C   . VAL B 1 87  ? -17.961 -0.326  23.325 1.00 75.74  ? 87  VAL B C   1 
ATOM   1753 O  O   . VAL B 1 87  ? -16.900 0.041   23.822 1.00 76.15  ? 87  VAL B O   1 
ATOM   1754 C  CB  . VAL B 1 87  ? -18.064 -2.549  22.249 1.00 71.77  ? 87  VAL B CB  1 
ATOM   1755 C  CG1 . VAL B 1 87  ? -17.895 -3.330  20.949 1.00 69.27  ? 87  VAL B CG1 1 
ATOM   1756 C  CG2 . VAL B 1 87  ? -17.016 -2.958  23.243 1.00 70.95  ? 87  VAL B CG2 1 
ATOM   1757 N  N   . THR B 1 88  ? -19.133 -0.130  23.908 1.00 77.44  ? 88  THR B N   1 
ATOM   1758 C  CA  . THR B 1 88  ? -19.259 0.787   25.016 1.00 80.20  ? 88  THR B CA  1 
ATOM   1759 C  C   . THR B 1 88  ? -19.752 0.109   26.264 1.00 80.62  ? 88  THR B C   1 
ATOM   1760 O  O   . THR B 1 88  ? -20.774 -0.537  26.237 1.00 80.51  ? 88  THR B O   1 
ATOM   1761 C  CB  . THR B 1 88  ? -20.214 1.939   24.637 1.00 82.78  ? 88  THR B CB  1 
ATOM   1762 O  OG1 . THR B 1 88  ? -19.571 2.792   23.671 1.00 83.49  ? 88  THR B OG1 1 
ATOM   1763 C  CG2 . THR B 1 88  ? -20.614 2.776   25.868 1.00 86.20  ? 88  THR B CG2 1 
ATOM   1764 N  N   . ALA B 1 89  ? -19.028 0.303   27.361 1.00 81.86  ? 89  ALA B N   1 
ATOM   1765 C  CA  . ALA B 1 89  ? -19.352 -0.299  28.630 1.00 82.99  ? 89  ALA B CA  1 
ATOM   1766 C  C   . ALA B 1 89  ? -20.158 0.660   29.501 1.00 86.79  ? 89  ALA B C   1 
ATOM   1767 O  O   . ALA B 1 89  ? -19.828 1.833   29.618 1.00 88.55  ? 89  ALA B O   1 
ATOM   1768 C  CB  . ALA B 1 89  ? -18.086 -0.683  29.348 1.00 82.53  ? 89  ALA B CB  1 
ATOM   1769 N  N   . ASP B 1 90  ? -21.231 0.128   30.081 1.00 88.67  ? 90  ASP B N   1 
ATOM   1770 C  CA  . ASP B 1 90  ? -21.921 0.656   31.259 1.00 92.64  ? 90  ASP B CA  1 
ATOM   1771 C  C   . ASP B 1 90  ? -21.070 1.279   32.336 1.00 95.07  ? 90  ASP B C   1 
ATOM   1772 O  O   . ASP B 1 90  ? -19.854 1.137   32.380 1.00 93.84  ? 90  ASP B O   1 
ATOM   1773 C  CB  . ASP B 1 90  ? -22.561 -0.512  32.009 1.00 93.20  ? 90  ASP B CB  1 
ATOM   1774 C  CG  . ASP B 1 90  ? -24.022 -0.672  31.733 1.00 96.00  ? 90  ASP B CG  1 
ATOM   1775 O  OD1 . ASP B 1 90  ? -24.575 0.007   30.847 1.00 98.63  ? 90  ASP B OD1 1 
ATOM   1776 O  OD2 . ASP B 1 90  ? -24.621 -1.532  32.414 1.00 98.93  ? 90  ASP B OD2 1 
ATOM   1777 N  N   . LYS B 1 91  ? -21.776 1.927   33.252 1.00 99.26  ? 91  LYS B N   1 
ATOM   1778 C  CA  . LYS B 1 91  ? -21.298 2.152   34.630 1.00 102.37 ? 91  LYS B CA  1 
ATOM   1779 C  C   . LYS B 1 91  ? -20.866 0.817   35.220 1.00 100.63 ? 91  LYS B C   1 
ATOM   1780 O  O   . LYS B 1 91  ? -19.812 0.684   35.804 1.00 100.76 ? 91  LYS B O   1 
ATOM   1781 C  CB  . LYS B 1 91  ? -22.452 2.715   35.514 1.00 106.79 ? 91  LYS B CB  1 
ATOM   1782 C  CG  . LYS B 1 91  ? -22.504 4.250   35.750 1.00 111.83 ? 91  LYS B CG  1 
ATOM   1783 C  CD  . LYS B 1 91  ? -21.616 4.670   36.951 1.00 116.94 ? 91  LYS B CD  1 
ATOM   1784 C  CE  . LYS B 1 91  ? -22.152 5.942   37.653 1.00 122.71 ? 91  LYS B CE  1 
ATOM   1785 N  NZ  . LYS B 1 91  ? -21.053 6.870   38.083 1.00 125.85 ? 91  LYS B NZ  1 
ATOM   1786 N  N   . ASP B 1 92  ? -21.764 -0.143  35.083 1.00 99.60  ? 92  ASP B N   1 
ATOM   1787 C  CA  . ASP B 1 92  ? -21.627 -1.489  35.616 1.00 99.02  ? 92  ASP B CA  1 
ATOM   1788 C  C   . ASP B 1 92  ? -20.684 -2.389  34.826 1.00 95.30  ? 92  ASP B C   1 
ATOM   1789 O  O   . ASP B 1 92  ? -20.585 -3.584  35.117 1.00 94.65  ? 92  ASP B O   1 
ATOM   1790 C  CB  . ASP B 1 92  ? -23.005 -2.165  35.615 1.00 99.94  ? 92  ASP B CB  1 
ATOM   1791 C  CG  . ASP B 1 92  ? -24.028 -1.425  36.483 1.00 105.14 ? 92  ASP B CG  1 
ATOM   1792 O  OD1 . ASP B 1 92  ? -25.050 -2.034  36.876 1.00 108.49 ? 92  ASP B OD1 1 
ATOM   1793 O  OD2 . ASP B 1 92  ? -23.811 -0.233  36.782 1.00 108.94 ? 92  ASP B OD2 1 
ATOM   1794 N  N   . GLY B 1 93  ? -20.022 -1.850  33.808 1.00 93.05  ? 93  GLY B N   1 
ATOM   1795 C  CA  . GLY B 1 93  ? -19.059 -2.635  33.046 1.00 89.89  ? 93  GLY B CA  1 
ATOM   1796 C  C   . GLY B 1 93  ? -19.662 -3.656  32.099 1.00 87.34  ? 93  GLY B C   1 
ATOM   1797 O  O   . GLY B 1 93  ? -18.951 -4.501  31.578 1.00 85.41  ? 93  GLY B O   1 
ATOM   1798 N  N   . VAL B 1 94  ? -20.967 -3.596  31.879 1.00 87.76  ? 94  VAL B N   1 
ATOM   1799 C  CA  . VAL B 1 94  ? -21.600 -4.362  30.817 1.00 86.05  ? 94  VAL B CA  1 
ATOM   1800 C  C   . VAL B 1 94  ? -21.667 -3.564  29.522 1.00 85.16  ? 94  VAL B C   1 
ATOM   1801 O  O   . VAL B 1 94  ? -22.163 -2.455  29.525 1.00 87.17  ? 94  VAL B O   1 
ATOM   1802 C  CB  . VAL B 1 94  ? -23.042 -4.720  31.189 1.00 87.95  ? 94  VAL B CB  1 
ATOM   1803 C  CG1 . VAL B 1 94  ? -23.780 -5.305  29.978 1.00 86.04  ? 94  VAL B CG1 1 
ATOM   1804 C  CG2 . VAL B 1 94  ? -23.058 -5.666  32.396 1.00 89.64  ? 94  VAL B CG2 1 
ATOM   1805 N  N   . ALA B 1 95  ? -21.214 -4.131  28.411 1.00 82.90  ? 95  ALA B N   1 
ATOM   1806 C  CA  . ALA B 1 95  ? -21.350 -3.481  27.122 1.00 82.29  ? 95  ALA B CA  1 
ATOM   1807 C  C   . ALA B 1 95  ? -22.381 -4.202  26.309 1.00 82.28  ? 95  ALA B C   1 
ATOM   1808 O  O   . ALA B 1 95  ? -22.238 -5.374  26.095 1.00 81.13  ? 95  ALA B O   1 
ATOM   1809 C  CB  . ALA B 1 95  ? -20.058 -3.500  26.416 1.00 80.38  ? 95  ALA B CB  1 
ATOM   1810 N  N   . ASP B 1 96  ? -23.420 -3.510  25.857 1.00 84.44  ? 96  ASP B N   1 
ATOM   1811 C  CA  . ASP B 1 96  ? -24.466 -4.137  25.032 1.00 85.36  ? 96  ASP B CA  1 
ATOM   1812 C  C   . ASP B 1 96  ? -24.178 -3.919  23.575 1.00 83.59  ? 96  ASP B C   1 
ATOM   1813 O  O   . ASP B 1 96  ? -24.585 -2.934  22.993 1.00 85.27  ? 96  ASP B O   1 
ATOM   1814 C  CB  . ASP B 1 96  ? -25.872 -3.596  25.350 1.00 88.84  ? 96  ASP B CB  1 
ATOM   1815 C  CG  . ASP B 1 96  ? -26.531 -4.305  26.568 1.00 92.82  ? 96  ASP B CG  1 
ATOM   1816 O  OD1 . ASP B 1 96  ? -26.451 -5.564  26.677 1.00 93.66  ? 96  ASP B OD1 1 
ATOM   1817 O  OD2 . ASP B 1 96  ? -27.134 -3.595  27.422 1.00 98.03  ? 96  ASP B OD2 1 
ATOM   1818 N  N   . VAL B 1 97  ? -23.499 -4.879  22.987 1.00 80.79  ? 97  VAL B N   1 
ATOM   1819 C  CA  . VAL B 1 97  ? -23.046 -4.744  21.640 1.00 79.28  ? 97  VAL B CA  1 
ATOM   1820 C  C   . VAL B 1 97  ? -24.173 -4.844  20.613 1.00 79.89  ? 97  VAL B C   1 
ATOM   1821 O  O   . VAL B 1 97  ? -25.090 -5.639  20.754 1.00 80.72  ? 97  VAL B O   1 
ATOM   1822 C  CB  . VAL B 1 97  ? -22.045 -5.814  21.339 1.00 77.11  ? 97  VAL B CB  1 
ATOM   1823 C  CG1 . VAL B 1 97  ? -21.765 -5.832  19.855 1.00 77.05  ? 97  VAL B CG1 1 
ATOM   1824 C  CG2 . VAL B 1 97  ? -20.793 -5.569  22.146 1.00 76.51  ? 97  VAL B CG2 1 
ATOM   1825 N  N   . SER B 1 98  ? -24.088 -4.023  19.578 1.00 79.78  ? 98  SER B N   1 
ATOM   1826 C  CA  . SER B 1 98  ? -24.995 -4.108  18.446 1.00 80.79  ? 98  SER B CA  1 
ATOM   1827 C  C   . SER B 1 98  ? -24.437 -3.269  17.277 1.00 80.72  ? 98  SER B C   1 
ATOM   1828 O  O   . SER B 1 98  ? -24.209 -2.070  17.391 1.00 81.44  ? 98  SER B O   1 
ATOM   1829 C  CB  . SER B 1 98  ? -26.409 -3.658  18.842 1.00 83.56  ? 98  SER B CB  1 
ATOM   1830 O  OG  . SER B 1 98  ? -27.324 -3.860  17.778 1.00 85.02  ? 98  SER B OG  1 
ATOM   1831 N  N   . ILE B 1 99  ? -24.200 -3.932  16.161 1.00 80.01  ? 99  ILE B N   1 
ATOM   1832 C  CA  . ILE B 1 99  ? -23.453 -3.361  15.059 1.00 80.18  ? 99  ILE B CA  1 
ATOM   1833 C  C   . ILE B 1 99  ? -23.883 -3.986  13.749 1.00 81.88  ? 99  ILE B C   1 
ATOM   1834 O  O   . ILE B 1 99  ? -24.085 -5.198  13.689 1.00 81.80  ? 99  ILE B O   1 
ATOM   1835 C  CB  . ILE B 1 99  ? -21.971 -3.720  15.177 1.00 77.50  ? 99  ILE B CB  1 
ATOM   1836 C  CG1 . ILE B 1 99  ? -21.370 -3.183  16.477 1.00 75.94  ? 99  ILE B CG1 1 
ATOM   1837 C  CG2 . ILE B 1 99  ? -21.214 -3.234  13.964 1.00 77.81  ? 99  ILE B CG2 1 
ATOM   1838 C  CD1 . ILE B 1 99  ? -19.856 -3.066  16.449 1.00 73.19  ? 99  ILE B CD1 1 
ATOM   1839 N  N   . GLU B 1 100 ? -24.023 -3.183  12.702 1.00 84.45  ? 100 GLU B N   1 
ATOM   1840 C  CA  . GLU B 1 100 ? -24.112 -3.717  11.353 1.00 86.04  ? 100 GLU B CA  1 
ATOM   1841 C  C   . GLU B 1 100 ? -22.773 -3.463  10.744 1.00 84.91  ? 100 GLU B C   1 
ATOM   1842 O  O   . GLU B 1 100 ? -22.129 -2.490  11.083 1.00 85.13  ? 100 GLU B O   1 
ATOM   1843 C  CB  . GLU B 1 100 ? -25.195 -3.013  10.528 1.00 90.10  ? 100 GLU B CB  1 
ATOM   1844 C  CG  . GLU B 1 100 ? -26.617 -3.542  10.772 1.00 94.13  ? 100 GLU B CG  1 
ATOM   1845 C  CD  . GLU B 1 100 ? -27.507 -3.464  9.524  1.00 100.97 ? 100 GLU B CD  1 
ATOM   1846 O  OE1 . GLU B 1 100 ? -26.972 -3.212  8.410  1.00 103.40 ? 100 GLU B OE1 1 
ATOM   1847 O  OE2 . GLU B 1 100 ? -28.742 -3.672  9.675  1.00 105.45 ? 100 GLU B OE2 1 
ATOM   1848 N  N   . ASP B 1 101 ? -22.339 -4.328  9.848  1.00 84.37  ? 101 ASP B N   1 
ATOM   1849 C  CA  . ASP B 1 101 ? -21.133 -4.046  9.102  1.00 84.39  ? 101 ASP B CA  1 
ATOM   1850 C  C   . ASP B 1 101 ? -21.153 -4.878  7.864  1.00 85.20  ? 101 ASP B C   1 
ATOM   1851 O  O   . ASP B 1 101 ? -21.647 -5.993  7.916  1.00 84.92  ? 101 ASP B O   1 
ATOM   1852 C  CB  . ASP B 1 101 ? -19.920 -4.411  9.919  1.00 82.00  ? 101 ASP B CB  1 
ATOM   1853 C  CG  . ASP B 1 101 ? -18.639 -3.946  9.266  1.00 83.80  ? 101 ASP B CG  1 
ATOM   1854 O  OD1 . ASP B 1 101 ? -18.251 -2.787  9.511  1.00 86.44  ? 101 ASP B OD1 1 
ATOM   1855 O  OD2 . ASP B 1 101 ? -18.023 -4.728  8.499  1.00 85.51  ? 101 ASP B OD2 1 
ATOM   1856 N  N   . SER B 1 102 ? -20.634 -4.360  6.755  1.00 86.67  ? 102 SER B N   1 
ATOM   1857 C  CA  . SER B 1 102 ? -20.673 -5.108  5.493  1.00 88.15  ? 102 SER B CA  1 
ATOM   1858 C  C   . SER B 1 102 ? -19.323 -5.257  4.833  1.00 87.69  ? 102 SER B C   1 
ATOM   1859 O  O   . SER B 1 102 ? -19.246 -5.697  3.682  1.00 89.59  ? 102 SER B O   1 
ATOM   1860 C  CB  . SER B 1 102 ? -21.664 -4.464  4.544  1.00 91.82  ? 102 SER B CB  1 
ATOM   1861 O  OG  . SER B 1 102 ? -21.807 -3.116  4.903  1.00 93.86  ? 102 SER B OG  1 
ATOM   1862 N  N   . VAL B 1 103 ? -18.262 -4.919  5.566  1.00 85.46  ? 103 VAL B N   1 
ATOM   1863 C  CA  . VAL B 1 103 ? -16.902 -5.266  5.146  1.00 84.91  ? 103 VAL B CA  1 
ATOM   1864 C  C   . VAL B 1 103 ? -16.588 -6.728  5.489  1.00 82.80  ? 103 VAL B C   1 
ATOM   1865 O  O   . VAL B 1 103 ? -16.000 -7.448  4.664  1.00 83.76  ? 103 VAL B O   1 
ATOM   1866 C  CB  . VAL B 1 103 ? -15.855 -4.374  5.791  1.00 83.90  ? 103 VAL B CB  1 
ATOM   1867 C  CG1 . VAL B 1 103 ? -14.512 -4.999  5.666  1.00 83.14  ? 103 VAL B CG1 1 
ATOM   1868 C  CG2 . VAL B 1 103 ? -15.866 -3.045  5.134  1.00 86.84  ? 103 VAL B CG2 1 
ATOM   1869 N  N   . ILE B 1 104 ? -16.973 -7.154  6.698  1.00 80.09  ? 104 ILE B N   1 
ATOM   1870 C  CA  . ILE B 1 104 ? -16.843 -8.553  7.095  1.00 78.26  ? 104 ILE B CA  1 
ATOM   1871 C  C   . ILE B 1 104 ? -17.958 -9.387  6.477  1.00 79.91  ? 104 ILE B C   1 
ATOM   1872 O  O   . ILE B 1 104 ? -18.983 -8.849  6.055  1.00 81.70  ? 104 ILE B O   1 
ATOM   1873 C  CB  . ILE B 1 104 ? -16.871 -8.723  8.615  1.00 75.55  ? 104 ILE B CB  1 
ATOM   1874 C  CG1 . ILE B 1 104 ? -18.237 -8.345  9.184  1.00 75.38  ? 104 ILE B CG1 1 
ATOM   1875 C  CG2 . ILE B 1 104 ? -15.784 -7.910  9.253  1.00 74.06  ? 104 ILE B CG2 1 
ATOM   1876 C  CD1 . ILE B 1 104 ? -18.301 -8.363  10.658 1.00 72.89  ? 104 ILE B CD1 1 
ATOM   1877 N  N   . SER B 1 105 ? -17.753 -10.699 6.444  1.00 79.76  ? 105 SER B N   1 
ATOM   1878 C  CA  . SER B 1 105 ? -18.686 -11.634 5.812  1.00 81.82  ? 105 SER B CA  1 
ATOM   1879 C  C   . SER B 1 105 ? -18.559 -12.966 6.543  1.00 80.59  ? 105 SER B C   1 
ATOM   1880 O  O   . SER B 1 105 ? -17.524 -13.247 7.132  1.00 78.68  ? 105 SER B O   1 
ATOM   1881 C  CB  . SER B 1 105 ? -18.337 -11.794 4.310  1.00 84.66  ? 105 SER B CB  1 
ATOM   1882 O  OG  . SER B 1 105 ? -19.403 -12.300 3.497  1.00 87.17  ? 105 SER B OG  1 
ATOM   1883 N  N   . LEU B 1 106 ? -19.614 -13.773 6.511  1.00 82.19  ? 106 LEU B N   1 
ATOM   1884 C  CA  . LEU B 1 106 ? -19.556 -15.149 7.007  1.00 82.21  ? 106 LEU B CA  1 
ATOM   1885 C  C   . LEU B 1 106 ? -19.250 -16.162 5.899  1.00 85.32  ? 106 LEU B C   1 
ATOM   1886 O  O   . LEU B 1 106 ? -19.003 -17.325 6.169  1.00 85.51  ? 106 LEU B O   1 
ATOM   1887 C  CB  . LEU B 1 106 ? -20.867 -15.514 7.714  1.00 82.22  ? 106 LEU B CB  1 
ATOM   1888 C  CG  . LEU B 1 106 ? -21.243 -14.622 8.895  1.00 79.25  ? 106 LEU B CG  1 
ATOM   1889 C  CD1 . LEU B 1 106 ? -22.198 -15.318 9.830  1.00 78.20  ? 106 LEU B CD1 1 
ATOM   1890 C  CD2 . LEU B 1 106 ? -20.013 -14.222 9.639  1.00 75.81  ? 106 LEU B CD2 1 
ATOM   1891 N  N   . SER B 1 107 ? -19.294 -15.704 4.653  1.00 88.72  ? 107 SER B N   1 
ATOM   1892 C  CA  . SER B 1 107 ? -18.906 -16.484 3.475  1.00 91.91  ? 107 SER B CA  1 
ATOM   1893 C  C   . SER B 1 107 ? -17.923 -15.642 2.683  1.00 93.30  ? 107 SER B C   1 
ATOM   1894 O  O   . SER B 1 107 ? -17.576 -14.532 3.091  1.00 92.06  ? 107 SER B O   1 
ATOM   1895 C  CB  . SER B 1 107 ? -20.139 -16.803 2.613  1.00 95.22  ? 107 SER B CB  1 
ATOM   1896 O  OG  . SER B 1 107 ? -20.875 -15.611 2.259  1.00 96.15  ? 107 SER B OG  1 
ATOM   1897 N  N   . GLY B 1 108 ? -17.460 -16.162 1.553  1.00 96.79  ? 108 GLY B N   1 
ATOM   1898 C  CA  . GLY B 1 108 ? -16.532 -15.402 0.693  1.00 98.63  ? 108 GLY B CA  1 
ATOM   1899 C  C   . GLY B 1 108 ? -15.151 -15.365 1.326  1.00 96.96  ? 108 GLY B C   1 
ATOM   1900 O  O   . GLY B 1 108 ? -14.897 -16.079 2.318  1.00 94.98  ? 108 GLY B O   1 
ATOM   1901 N  N   . ASP B 1 109 ? -14.256 -14.546 0.766  1.00 98.30  ? 109 ASP B N   1 
ATOM   1902 C  CA  . ASP B 1 109 ? -12.836 -14.492 1.251  1.00 97.54  ? 109 ASP B CA  1 
ATOM   1903 C  C   . ASP B 1 109 ? -12.593 -13.344 2.274  1.00 94.45  ? 109 ASP B C   1 
ATOM   1904 O  O   . ASP B 1 109 ? -11.454 -13.063 2.676  1.00 93.44  ? 109 ASP B O   1 
ATOM   1905 C  CB  . ASP B 1 109 ? -11.777 -14.511 0.100  1.00 100.91 ? 109 ASP B CB  1 
ATOM   1906 C  CG  . ASP B 1 109 ? -12.194 -13.700 -1.132 1.00 105.80 ? 109 ASP B CG  1 
ATOM   1907 O  OD1 . ASP B 1 109 ? -12.443 -14.355 -2.184 1.00 109.74 ? 109 ASP B OD1 1 
ATOM   1908 O  OD2 . ASP B 1 109 ? -12.262 -12.431 -1.051 1.00 107.64 ? 109 ASP B OD2 1 
ATOM   1909 N  N   . HIS B 1 110 ? -13.679 -12.705 2.694  1.00 92.74  ? 110 HIS B N   1 
ATOM   1910 C  CA  . HIS B 1 110 ? -13.657 -11.936 3.914  1.00 89.85  ? 110 HIS B CA  1 
ATOM   1911 C  C   . HIS B 1 110 ? -14.262 -12.774 5.065  1.00 86.27  ? 110 HIS B C   1 
ATOM   1912 O  O   . HIS B 1 110 ? -14.568 -12.246 6.144  1.00 84.16  ? 110 HIS B O   1 
ATOM   1913 C  CB  . HIS B 1 110 ? -14.428 -10.629 3.699  1.00 91.16  ? 110 HIS B CB  1 
ATOM   1914 C  CG  . HIS B 1 110 ? -13.753 -9.663  2.767  1.00 95.86  ? 110 HIS B CG  1 
ATOM   1915 N  ND1 . HIS B 1 110 ? -14.107 -8.327  2.694  1.00 98.60  ? 110 HIS B ND1 1 
ATOM   1916 C  CD2 . HIS B 1 110 ? -12.729 -9.827  1.891  1.00 99.75  ? 110 HIS B CD2 1 
ATOM   1917 C  CE1 . HIS B 1 110 ? -13.347 -7.718  1.798  1.00 101.88 ? 110 HIS B CE1 1 
ATOM   1918 N  NE2 . HIS B 1 110 ? -12.501 -8.604  1.298  1.00 102.99 ? 110 HIS B NE2 1 
ATOM   1919 N  N   . CYS B 1 111 ? -14.453 -14.076 4.824  1.00 85.30  ? 111 CYS B N   1 
ATOM   1920 C  CA  . CYS B 1 111 ? -15.090 -14.966 5.799  1.00 82.25  ? 111 CYS B CA  1 
ATOM   1921 C  C   . CYS B 1 111 ? -14.255 -14.841 7.064  1.00 78.95  ? 111 CYS B C   1 
ATOM   1922 O  O   . CYS B 1 111 ? -13.027 -14.929 6.995  1.00 78.86  ? 111 CYS B O   1 
ATOM   1923 C  CB  . CYS B 1 111 ? -15.159 -16.413 5.268  1.00 83.65  ? 111 CYS B CB  1 
ATOM   1924 S  SG  . CYS B 1 111 ? -15.702 -17.686 6.438  1.00 80.49  ? 111 CYS B SG  1 
ATOM   1925 N  N   . ILE B 1 112 ? -14.919 -14.567 8.189  1.00 75.86  ? 112 ILE B N   1 
ATOM   1926 C  CA  . ILE B 1 112 ? -14.254 -14.424 9.487  1.00 72.86  ? 112 ILE B CA  1 
ATOM   1927 C  C   . ILE B 1 112 ? -14.464 -15.624 10.396 1.00 71.93  ? 112 ILE B C   1 
ATOM   1928 O  O   . ILE B 1 112 ? -14.050 -15.621 11.564 1.00 70.59  ? 112 ILE B O   1 
ATOM   1929 C  CB  . ILE B 1 112 ? -14.728 -13.186 10.234 1.00 71.37  ? 112 ILE B CB  1 
ATOM   1930 C  CG1 . ILE B 1 112 ? -16.190 -13.300 10.665 1.00 70.09  ? 112 ILE B CG1 1 
ATOM   1931 C  CG2 . ILE B 1 112 ? -14.562 -12.019 9.362  1.00 72.71  ? 112 ILE B CG2 1 
ATOM   1932 C  CD1 . ILE B 1 112 ? -16.612 -12.215 11.562 1.00 66.89  ? 112 ILE B CD1 1 
ATOM   1933 N  N   . ILE B 1 113 ? -15.115 -16.651 9.869  1.00 72.72  ? 113 ILE B N   1 
ATOM   1934 C  CA  . ILE B 1 113 ? -15.341 -17.848 10.637 1.00 72.22  ? 113 ILE B CA  1 
ATOM   1935 C  C   . ILE B 1 113 ? -14.011 -18.534 10.830 1.00 71.86  ? 113 ILE B C   1 
ATOM   1936 O  O   . ILE B 1 113 ? -13.284 -18.786 9.875  1.00 72.93  ? 113 ILE B O   1 
ATOM   1937 C  CB  . ILE B 1 113 ? -16.338 -18.774 9.943  1.00 74.19  ? 113 ILE B CB  1 
ATOM   1938 C  CG1 . ILE B 1 113 ? -17.755 -18.262 10.182 1.00 74.27  ? 113 ILE B CG1 1 
ATOM   1939 C  CG2 . ILE B 1 113 ? -16.243 -20.185 10.484 1.00 74.84  ? 113 ILE B CG2 1 
ATOM   1940 C  CD1 . ILE B 1 113 ? -18.796 -19.019 9.417  1.00 78.09  ? 113 ILE B CD1 1 
ATOM   1941 N  N   . GLY B 1 114 ? -13.696 -18.810 12.078 1.00 70.50  ? 114 GLY B N   1 
ATOM   1942 C  CA  . GLY B 1 114 ? -12.461 -19.458 12.407 1.00 70.86  ? 114 GLY B CA  1 
ATOM   1943 C  C   . GLY B 1 114 ? -11.387 -18.481 12.822 1.00 69.83  ? 114 GLY B C   1 
ATOM   1944 O  O   . GLY B 1 114 ? -10.233 -18.850 13.016 1.00 70.45  ? 114 GLY B O   1 
ATOM   1945 N  N   . ARG B 1 115 ? -11.763 -17.234 13.004 1.00 68.54  ? 115 ARG B N   1 
ATOM   1946 C  CA  . ARG B 1 115 ? -10.804 -16.245 13.400 1.00 68.18  ? 115 ARG B CA  1 
ATOM   1947 C  C   . ARG B 1 115 ? -11.154 -15.735 14.782 1.00 66.86  ? 115 ARG B C   1 
ATOM   1948 O  O   . ARG B 1 115 ? -12.291 -15.818 15.195 1.00 66.59  ? 115 ARG B O   1 
ATOM   1949 C  CB  . ARG B 1 115 ? -10.812 -15.144 12.363 1.00 68.57  ? 115 ARG B CB  1 
ATOM   1950 C  CG  . ARG B 1 115 ? -10.601 -15.679 10.958 1.00 70.56  ? 115 ARG B CG  1 
ATOM   1951 C  CD  . ARG B 1 115 ? -10.348 -14.586 9.947  1.00 72.06  ? 115 ARG B CD  1 
ATOM   1952 N  NE  . ARG B 1 115 ? -10.148 -15.120 8.609  1.00 74.07  ? 115 ARG B NE  1 
ATOM   1953 C  CZ  . ARG B 1 115 ? -8.985  -15.552 8.140  1.00 76.61  ? 115 ARG B CZ  1 
ATOM   1954 N  NH1 . ARG B 1 115 ? -7.883  -15.507 8.880  1.00 77.66  ? 115 ARG B NH1 1 
ATOM   1955 N  NH2 . ARG B 1 115 ? -8.914  -16.033 6.910  1.00 79.02  ? 115 ARG B NH2 1 
ATOM   1956 N  N   . THR B 1 116 ? -10.189 -15.208 15.508 1.00 66.58  ? 116 THR B N   1 
ATOM   1957 C  CA  . THR B 1 116 ? -10.467 -14.802 16.853 1.00 66.03  ? 116 THR B CA  1 
ATOM   1958 C  C   . THR B 1 116 ? -11.050 -13.431 16.908 1.00 64.88  ? 116 THR B C   1 
ATOM   1959 O  O   . THR B 1 116 ? -10.581 -12.545 16.248 1.00 65.31  ? 116 THR B O   1 
ATOM   1960 C  CB  . THR B 1 116 ? -9.228  -14.769 17.683 1.00 67.01  ? 116 THR B CB  1 
ATOM   1961 O  OG1 . THR B 1 116 ? -8.604  -16.054 17.654 1.00 69.54  ? 116 THR B OG1 1 
ATOM   1962 C  CG2 . THR B 1 116 ? -9.592  -14.427 19.115 1.00 67.68  ? 116 THR B CG2 1 
ATOM   1963 N  N   . LEU B 1 117 ? -12.080 -13.268 17.708 1.00 64.08  ? 117 LEU B N   1 
ATOM   1964 C  CA  . LEU B 1 117 ? -12.645 -11.977 18.017 1.00 63.75  ? 117 LEU B CA  1 
ATOM   1965 C  C   . LEU B 1 117 ? -11.982 -11.527 19.285 1.00 64.20  ? 117 LEU B C   1 
ATOM   1966 O  O   . LEU B 1 117 ? -11.739 -12.334 20.140 1.00 64.95  ? 117 LEU B O   1 
ATOM   1967 C  CB  . LEU B 1 117 ? -14.138 -12.132 18.267 1.00 63.39  ? 117 LEU B CB  1 
ATOM   1968 C  CG  . LEU B 1 117 ? -14.902 -10.881 18.648 1.00 62.47  ? 117 LEU B CG  1 
ATOM   1969 C  CD1 . LEU B 1 117 ? -14.813 -9.934  17.515 1.00 62.86  ? 117 LEU B CD1 1 
ATOM   1970 C  CD2 . LEU B 1 117 ? -16.318 -11.203 18.941 1.00 61.32  ? 117 LEU B CD2 1 
ATOM   1971 N  N   . VAL B 1 118 ? -11.698 -10.245 19.432 1.00 64.72  ? 118 VAL B N   1 
ATOM   1972 C  CA  . VAL B 1 118 ? -10.976 -9.770  20.604 1.00 65.50  ? 118 VAL B CA  1 
ATOM   1973 C  C   . VAL B 1 118 ? -11.548 -8.475  21.077 1.00 65.92  ? 118 VAL B C   1 
ATOM   1974 O  O   . VAL B 1 118 ? -11.832 -7.617  20.277 1.00 66.25  ? 118 VAL B O   1 
ATOM   1975 C  CB  . VAL B 1 118 ? -9.519  -9.488  20.277 1.00 66.43  ? 118 VAL B CB  1 
ATOM   1976 C  CG1 . VAL B 1 118 ? -8.810  -8.985  21.468 1.00 67.60  ? 118 VAL B CG1 1 
ATOM   1977 C  CG2 . VAL B 1 118 ? -8.847  -10.709 19.808 1.00 67.17  ? 118 VAL B CG2 1 
ATOM   1978 N  N   . VAL B 1 119 ? -11.706 -8.327  22.380 1.00 66.63  ? 119 VAL B N   1 
ATOM   1979 C  CA  . VAL B 1 119 ? -12.076 -7.052  22.982 1.00 67.74  ? 119 VAL B CA  1 
ATOM   1980 C  C   . VAL B 1 119 ? -10.874 -6.560  23.778 1.00 69.97  ? 119 VAL B C   1 
ATOM   1981 O  O   . VAL B 1 119 ? -10.158 -7.365  24.361 1.00 70.70  ? 119 VAL B O   1 
ATOM   1982 C  CB  . VAL B 1 119 ? -13.277 -7.179  23.888 1.00 67.49  ? 119 VAL B CB  1 
ATOM   1983 C  CG1 . VAL B 1 119 ? -13.008 -8.158  24.973 1.00 68.13  ? 119 VAL B CG1 1 
ATOM   1984 C  CG2 . VAL B 1 119 ? -13.603 -5.873  24.511 1.00 68.45  ? 119 VAL B CG2 1 
ATOM   1985 N  N   . HIS B 1 120 ? -10.646 -5.249  23.797 1.00 71.94  ? 120 HIS B N   1 
ATOM   1986 C  CA  . HIS B 1 120 ? -9.370  -4.694  24.230 1.00 74.34  ? 120 HIS B CA  1 
ATOM   1987 C  C   . HIS B 1 120 ? -9.440  -3.810  25.456 1.00 76.59  ? 120 HIS B C   1 
ATOM   1988 O  O   . HIS B 1 120 ? -10.502 -3.360  25.863 1.00 76.43  ? 120 HIS B O   1 
ATOM   1989 C  CB  . HIS B 1 120 ? -8.786  -3.851  23.125 1.00 75.18  ? 120 HIS B CB  1 
ATOM   1990 C  CG  . HIS B 1 120 ? -8.185  -4.630  22.011 1.00 75.72  ? 120 HIS B CG  1 
ATOM   1991 N  ND1 . HIS B 1 120 ? -6.823  -4.729  21.837 1.00 79.49  ? 120 HIS B ND1 1 
ATOM   1992 C  CD2 . HIS B 1 120 ? -8.749  -5.295  20.979 1.00 75.42  ? 120 HIS B CD2 1 
ATOM   1993 C  CE1 . HIS B 1 120 ? -6.574  -5.443  20.757 1.00 79.98  ? 120 HIS B CE1 1 
ATOM   1994 N  NE2 . HIS B 1 120 ? -7.727  -5.801  20.217 1.00 77.22  ? 120 HIS B NE2 1 
ATOM   1995 N  N   . GLU B 1 121 ? -8.259  -3.535  26.001 1.00 79.31  ? 121 GLU B N   1 
ATOM   1996 C  CA  . GLU B 1 121 ? -8.087  -2.771  27.238 1.00 82.19  ? 121 GLU B CA  1 
ATOM   1997 C  C   . GLU B 1 121 ? -8.651  -1.371  27.153 1.00 82.99  ? 121 GLU B C   1 
ATOM   1998 O  O   . GLU B 1 121 ? -9.386  -0.973  28.020 1.00 83.59  ? 121 GLU B O   1 
ATOM   1999 C  CB  . GLU B 1 121 ? -6.600  -2.700  27.605 1.00 84.86  ? 121 GLU B CB  1 
ATOM   2000 C  CG  . GLU B 1 121 ? -6.322  -2.133  28.987 1.00 89.68  ? 121 GLU B CG  1 
ATOM   2001 C  CD  . GLU B 1 121 ? -4.819  -1.918  29.264 1.00 95.31  ? 121 GLU B CD  1 
ATOM   2002 O  OE1 . GLU B 1 121 ? -4.009  -1.926  28.292 1.00 96.05  ? 121 GLU B OE1 1 
ATOM   2003 O  OE2 . GLU B 1 121 ? -4.461  -1.732  30.470 1.00 99.55  ? 121 GLU B OE2 1 
ATOM   2004 N  N   . LYS B 1 122 ? -8.281  -0.630  26.117 1.00 83.61  ? 122 LYS B N   1 
ATOM   2005 C  CA  . LYS B 1 122 ? -8.692  0.775   25.955 1.00 85.77  ? 122 LYS B CA  1 
ATOM   2006 C  C   . LYS B 1 122 ? -9.508  1.006   24.695 1.00 83.95  ? 122 LYS B C   1 
ATOM   2007 O  O   . LYS B 1 122 ? -9.824  0.074   23.974 1.00 81.95  ? 122 LYS B O   1 
ATOM   2008 C  CB  . LYS B 1 122 ? -7.472  1.710   25.850 1.00 89.14  ? 122 LYS B CB  1 
ATOM   2009 C  CG  . LYS B 1 122 ? -6.246  1.342   26.670 1.00 92.75  ? 122 LYS B CG  1 
ATOM   2010 C  CD  . LYS B 1 122 ? -5.115  2.348   26.414 1.00 98.02  ? 122 LYS B CD  1 
ATOM   2011 C  CE  . LYS B 1 122 ? -3.768  1.643   26.416 1.00 100.38 ? 122 LYS B CE  1 
ATOM   2012 N  NZ  . LYS B 1 122 ? -2.633  2.586   26.264 1.00 104.97 ? 122 LYS B NZ  1 
ATOM   2013 N  N   . ALA B 1 123 ? -9.803  2.270   24.416 1.00 85.10  ? 123 ALA B N   1 
ATOM   2014 C  CA  . ALA B 1 123 ? -10.479 2.634   23.196 1.00 84.06  ? 123 ALA B CA  1 
ATOM   2015 C  C   . ALA B 1 123 ? -9.593  2.487   21.951 1.00 83.62  ? 123 ALA B C   1 
ATOM   2016 O  O   . ALA B 1 123 ? -8.408  2.823   21.969 1.00 84.99  ? 123 ALA B O   1 
ATOM   2017 C  CB  . ALA B 1 123 ? -10.946 4.017   23.307 1.00 86.67  ? 123 ALA B CB  1 
ATOM   2018 N  N   . ASP B 1 124 ? -10.192 1.977   20.876 1.00 81.68  ? 124 ASP B N   1 
ATOM   2019 C  CA  . ASP B 1 124 ? -9.603  2.006   19.527 1.00 82.06  ? 124 ASP B CA  1 
ATOM   2020 C  C   . ASP B 1 124 ? -9.661  3.466   19.150 1.00 84.40  ? 124 ASP B C   1 
ATOM   2021 O  O   . ASP B 1 124 ? -10.693 4.087   19.324 1.00 84.70  ? 124 ASP B O   1 
ATOM   2022 C  CB  . ASP B 1 124 ? -10.439 1.137   18.535 1.00 80.07  ? 124 ASP B CB  1 
ATOM   2023 C  CG  . ASP B 1 124 ? -9.844  1.056   17.099 1.00 81.46  ? 124 ASP B CG  1 
ATOM   2024 O  OD1 . ASP B 1 124 ? -8.821  1.692   16.818 1.00 84.73  ? 124 ASP B OD1 1 
ATOM   2025 O  OD2 . ASP B 1 124 ? -10.410 0.350   16.232 1.00 80.46  ? 124 ASP B OD2 1 
ATOM   2026 N  N   . ASP B 1 125 ? -8.565  4.030   18.655 1.00 86.36  ? 125 ASP B N   1 
ATOM   2027 C  CA  . ASP B 1 125 ? -8.549  5.453   18.263 1.00 89.29  ? 125 ASP B CA  1 
ATOM   2028 C  C   . ASP B 1 125 ? -8.846  5.636   16.770 1.00 89.53  ? 125 ASP B C   1 
ATOM   2029 O  O   . ASP B 1 125 ? -8.712  6.712   16.223 1.00 92.05  ? 125 ASP B O   1 
ATOM   2030 C  CB  . ASP B 1 125 ? -7.228  6.132   18.686 1.00 92.41  ? 125 ASP B CB  1 
ATOM   2031 C  CG  . ASP B 1 125 ? -6.020  5.715   17.828 1.00 93.38  ? 125 ASP B CG  1 
ATOM   2032 O  OD1 . ASP B 1 125 ? -6.219  5.210   16.702 1.00 92.39  ? 125 ASP B OD1 1 
ATOM   2033 O  OD2 . ASP B 1 125 ? -4.861  5.898   18.301 1.00 95.35  ? 125 ASP B OD2 1 
ATOM   2034 N  N   . LEU B 1 126 ? -9.238  4.551   16.122 1.00 87.18  ? 126 LEU B N   1 
ATOM   2035 C  CA  . LEU B 1 126 ? -9.710  4.558   14.734 1.00 87.82  ? 126 LEU B CA  1 
ATOM   2036 C  C   . LEU B 1 126 ? -8.669  4.999   13.719 1.00 90.90  ? 126 LEU B C   1 
ATOM   2037 O  O   . LEU B 1 126 ? -8.998  5.432   12.614 1.00 92.39  ? 126 LEU B O   1 
ATOM   2038 C  CB  . LEU B 1 126 ? -10.981 5.394   14.624 1.00 88.86  ? 126 LEU B CB  1 
ATOM   2039 C  CG  . LEU B 1 126 ? -12.046 5.115   15.700 1.00 86.29  ? 126 LEU B CG  1 
ATOM   2040 C  CD1 . LEU B 1 126 ? -13.419 5.612   15.254 1.00 86.63  ? 126 LEU B CD1 1 
ATOM   2041 C  CD2 . LEU B 1 126 ? -12.101 3.626   16.011 1.00 81.60  ? 126 LEU B CD2 1 
ATOM   2042 N  N   . GLY B 1 127 ? -7.405  4.861   14.110 1.00 92.40  ? 127 GLY B N   1 
ATOM   2043 C  CA  . GLY B 1 127 ? -6.269  5.213   13.262 1.00 95.98  ? 127 GLY B CA  1 
ATOM   2044 C  C   . GLY B 1 127 ? -5.750  6.637   13.406 1.00 100.86 ? 127 GLY B C   1 
ATOM   2045 O  O   . GLY B 1 127 ? -4.645  6.926   12.897 1.00 103.75 ? 127 GLY B O   1 
ATOM   2046 N  N   . LYS B 1 128 ? -6.494  7.491   14.144 1.00 102.46 ? 128 LYS B N   1 
ATOM   2047 C  CA  . LYS B 1 128 ? -6.273  8.961   14.195 1.00 107.49 ? 128 LYS B CA  1 
ATOM   2048 C  C   . LYS B 1 128 ? -5.409  9.438   15.360 1.00 109.10 ? 128 LYS B C   1 
ATOM   2049 O  O   . LYS B 1 128 ? -5.492  10.613  15.742 1.00 112.34 ? 128 LYS B O   1 
ATOM   2050 C  CB  . LYS B 1 128 ? -7.621  9.711   14.214 1.00 108.40 ? 128 LYS B CB  1 
ATOM   2051 C  CG  . LYS B 1 128 ? -8.736  9.028   13.405 1.00 108.62 ? 128 LYS B CG  1 
ATOM   2052 C  CD  . LYS B 1 128 ? -9.843  10.015  12.943 1.00 114.44 ? 128 LYS B CD  1 
ATOM   2053 C  CE  . LYS B 1 128 ? -11.066 9.259   12.374 1.00 113.79 ? 128 LYS B CE  1 
ATOM   2054 N  NZ  . LYS B 1 128 ? -10.760 8.602   11.051 1.00 114.58 ? 128 LYS B NZ  1 
ATOM   2055 N  N   . GLY B 1 129 ? -4.596  8.530   15.914 1.00 107.51 ? 129 GLY B N   1 
ATOM   2056 C  CA  . GLY B 1 129 ? -3.787  8.810   17.112 1.00 109.32 ? 129 GLY B CA  1 
ATOM   2057 C  C   . GLY B 1 129 ? -2.437  9.388   16.733 1.00 113.98 ? 129 GLY B C   1 
ATOM   2058 O  O   . GLY B 1 129 ? -1.623  9.785   17.649 1.00 116.27 ? 129 GLY B O   1 
ATOM   2059 N  N   . GLY B 1 130 ? -2.192  9.387   15.396 1.00 115.24 ? 130 GLY B N   1 
ATOM   2060 C  CA  . GLY B 1 130 ? -1.002  9.986   14.801 1.00 120.14 ? 130 GLY B CA  1 
ATOM   2061 C  C   . GLY B 1 130 ? 0.297   9.314   15.205 1.00 121.13 ? 130 GLY B C   1 
ATOM   2062 O  O   . GLY B 1 130 ? 1.351   9.848   14.913 1.00 125.60 ? 130 GLY B O   1 
ATOM   2063 N  N   . ASN B 1 131 ? 0.250   8.163   15.872 1.00 117.67 ? 131 ASN B N   1 
ATOM   2064 C  CA  . ASN B 1 131 ? 1.472   7.514   16.258 1.00 119.11 ? 131 ASN B CA  1 
ATOM   2065 C  C   . ASN B 1 131 ? 1.605   6.268   15.376 1.00 117.01 ? 131 ASN B C   1 
ATOM   2066 O  O   . ASN B 1 131 ? 0.670   5.908   14.662 1.00 113.96 ? 131 ASN B O   1 
ATOM   2067 C  CB  . ASN B 1 131 ? 1.576   7.364   17.825 1.00 118.54 ? 131 ASN B CB  1 
ATOM   2068 C  CG  . ASN B 1 131 ? 0.930   6.128   18.354 1.00 113.24 ? 131 ASN B CG  1 
ATOM   2069 O  OD1 . ASN B 1 131 ? -0.199  5.793   17.967 1.00 109.30 ? 131 ASN B OD1 1 
ATOM   2070 N  ND2 . ASN B 1 131 ? 1.642   5.429   19.260 1.00 112.81 ? 131 ASN B ND2 1 
ATOM   2071 N  N   . GLU B 1 132 ? 2.786   5.669   15.358 1.00 119.53 ? 132 GLU B N   1 
ATOM   2072 C  CA  . GLU B 1 132 ? 3.032   4.511   14.499 1.00 118.90 ? 132 GLU B CA  1 
ATOM   2073 C  C   . GLU B 1 132 ? 1.968   3.419   14.795 1.00 113.08 ? 132 GLU B C   1 
ATOM   2074 O  O   . GLU B 1 132 ? 1.269   2.915   13.878 1.00 110.02 ? 132 GLU B O   1 
ATOM   2075 C  CB  . GLU B 1 132 ? 4.476   3.984   14.747 1.00 122.50 ? 132 GLU B CB  1 
ATOM   2076 C  CG  . GLU B 1 132 ? 4.730   2.408   14.527 1.00 122.77 ? 132 GLU B CG  1 
ATOM   2077 C  CD  . GLU B 1 132 ? 5.286   2.027   13.115 1.00 127.61 ? 132 GLU B CD  1 
ATOM   2078 O  OE1 . GLU B 1 132 ? 5.920   2.904   12.465 1.00 133.57 ? 132 GLU B OE1 1 
ATOM   2079 O  OE2 . GLU B 1 132 ? 5.093   0.852   12.668 1.00 126.22 ? 132 GLU B OE2 1 
ATOM   2080 N  N   . GLU B 1 133 ? 1.877   3.105   16.106 1.00 111.48 ? 133 GLU B N   1 
ATOM   2081 C  CA  . GLU B 1 133 ? 1.018   2.050   16.663 1.00 106.91 ? 133 GLU B CA  1 
ATOM   2082 C  C   . GLU B 1 133 ? -0.466  2.251   16.327 1.00 103.22 ? 133 GLU B C   1 
ATOM   2083 O  O   . GLU B 1 133 ? -1.192  1.261   16.203 1.00 99.74  ? 133 GLU B O   1 
ATOM   2084 C  CB  . GLU B 1 133 ? 1.216   1.946   18.200 1.00 107.08 ? 133 GLU B CB  1 
ATOM   2085 C  CG  . GLU B 1 133 ? 0.529   0.741   18.841 1.00 104.93 ? 133 GLU B CG  1 
ATOM   2086 C  CD  . GLU B 1 133 ? 1.016   -0.589  18.242 1.00 106.77 ? 133 GLU B CD  1 
ATOM   2087 O  OE1 . GLU B 1 133 ? 2.234   -0.699  17.988 1.00 111.23 ? 133 GLU B OE1 1 
ATOM   2088 O  OE2 . GLU B 1 133 ? 0.185   -1.509  18.005 1.00 104.78 ? 133 GLU B OE2 1 
ATOM   2089 N  N   . SER B 1 134 ? -0.905  3.506   16.167 1.00 104.26 ? 134 SER B N   1 
ATOM   2090 C  CA  . SER B 1 134 ? -2.306  3.789   15.852 1.00 101.71 ? 134 SER B CA  1 
ATOM   2091 C  C   . SER B 1 134 ? -2.744  3.285   14.456 1.00 100.53 ? 134 SER B C   1 
ATOM   2092 O  O   . SER B 1 134 ? -3.921  2.963   14.256 1.00 98.36  ? 134 SER B O   1 
ATOM   2093 C  CB  . SER B 1 134 ? -2.625  5.276   15.950 1.00 104.32 ? 134 SER B CB  1 
ATOM   2094 O  OG  . SER B 1 134 ? -3.964  5.523   15.547 1.00 101.77 ? 134 SER B OG  1 
ATOM   2095 N  N   . THR B 1 135 ? -1.833  3.188   13.495 1.00 102.33 ? 135 THR B N   1 
ATOM   2096 C  CA  . THR B 1 135 ? -2.211  2.626   12.184 1.00 101.34 ? 135 THR B CA  1 
ATOM   2097 C  C   . THR B 1 135 ? -2.111  1.086   12.117 1.00 98.44  ? 135 THR B C   1 
ATOM   2098 O  O   . THR B 1 135 ? -2.171  0.489   11.033 1.00 98.09  ? 135 THR B O   1 
ATOM   2099 C  CB  . THR B 1 135 ? -1.333  3.242   11.102 1.00 105.64 ? 135 THR B CB  1 
ATOM   2100 O  OG1 . THR B 1 135 ? 0.017   3.300   11.612 1.00 108.10 ? 135 THR B OG1 1 
ATOM   2101 C  CG2 . THR B 1 135 ? -1.862  4.681   10.709 1.00 107.49 ? 135 THR B CG2 1 
ATOM   2102 N  N   . LYS B 1 136 ? -1.982  0.458   13.286 1.00 96.63  ? 136 LYS B N   1 
ATOM   2103 C  CA  . LYS B 1 136 ? -1.896  -1.000  13.409 1.00 94.69  ? 136 LYS B CA  1 
ATOM   2104 C  C   . LYS B 1 136 ? -2.961  -1.593  14.372 1.00 90.72  ? 136 LYS B C   1 
ATOM   2105 O  O   . LYS B 1 136 ? -3.816  -2.417  13.967 1.00 88.23  ? 136 LYS B O   1 
ATOM   2106 C  CB  . LYS B 1 136 ? -0.484  -1.382  13.865 1.00 96.97  ? 136 LYS B CB  1 
ATOM   2107 C  CG  . LYS B 1 136 ? 0.625   -0.692  13.033 1.00 103.41 ? 136 LYS B CG  1 
ATOM   2108 C  CD  . LYS B 1 136 ? 2.051   -0.931  13.611 1.00 108.79 ? 136 LYS B CD  1 
ATOM   2109 C  CE  . LYS B 1 136 ? 2.502   -2.422  13.501 1.00 108.79 ? 136 LYS B CE  1 
ATOM   2110 N  NZ  . LYS B 1 136 ? 3.956   -2.638  13.777 1.00 112.83 ? 136 LYS B NZ  1 
ATOM   2111 N  N   . THR B 1 137 ? -2.906  -1.179  15.635 1.00 90.21  ? 137 THR B N   1 
ATOM   2112 C  CA  . THR B 1 137 ? -3.881  -1.636  16.598 1.00 87.36  ? 137 THR B CA  1 
ATOM   2113 C  C   . THR B 1 137 ? -4.854  -0.543  16.991 1.00 86.65  ? 137 THR B C   1 
ATOM   2114 O  O   . THR B 1 137 ? -5.736  -0.795  17.785 1.00 85.29  ? 137 THR B O   1 
ATOM   2115 C  CB  . THR B 1 137 ? -3.235  -2.219  17.914 1.00 87.52  ? 137 THR B CB  1 
ATOM   2116 O  OG1 . THR B 1 137 ? -2.516  -1.195  18.612 1.00 90.62  ? 137 THR B OG1 1 
ATOM   2117 C  CG2 . THR B 1 137 ? -2.330  -3.425  17.618 1.00 88.19  ? 137 THR B CG2 1 
ATOM   2118 N  N   . GLY B 1 138 ? -4.717  0.665   16.482 1.00 88.08  ? 138 GLY B N   1 
ATOM   2119 C  CA  . GLY B 1 138 ? -5.510  1.759   17.022 1.00 88.25  ? 138 GLY B CA  1 
ATOM   2120 C  C   . GLY B 1 138 ? -5.255  2.038   18.505 1.00 88.60  ? 138 GLY B C   1 
ATOM   2121 O  O   . GLY B 1 138 ? -6.124  2.565   19.208 1.00 88.00  ? 138 GLY B O   1 
ATOM   2122 N  N   . ASN B 1 139 ? -4.069  1.671   18.997 1.00 89.79  ? 139 ASN B N   1 
ATOM   2123 C  CA  . ASN B 1 139 ? -3.663  1.921   20.401 1.00 91.11  ? 139 ASN B CA  1 
ATOM   2124 C  C   . ASN B 1 139 ? -4.599  1.326   21.424 1.00 88.86  ? 139 ASN B C   1 
ATOM   2125 O  O   . ASN B 1 139 ? -4.683  1.798   22.569 1.00 89.81  ? 139 ASN B O   1 
ATOM   2126 C  CB  . ASN B 1 139 ? -3.528  3.431   20.662 1.00 94.28  ? 139 ASN B CB  1 
ATOM   2127 C  CG  . ASN B 1 139 ? -2.193  3.993   20.201 1.00 97.82  ? 139 ASN B CG  1 
ATOM   2128 O  OD1 . ASN B 1 139 ? -1.174  3.267   20.070 1.00 97.12  ? 139 ASN B OD1 1 
ATOM   2129 N  ND2 . ASN B 1 139 ? -2.180  5.306   19.976 1.00 100.99 ? 139 ASN B ND2 1 
ATOM   2130 N  N   . ALA B 1 140 ? -5.271  0.261   21.000 1.00 86.36  ? 140 ALA B N   1 
ATOM   2131 C  CA  . ALA B 1 140 ? -6.425  -0.270  21.713 1.00 84.44  ? 140 ALA B CA  1 
ATOM   2132 C  C   . ALA B 1 140 ? -5.980  -0.920  22.989 1.00 84.92  ? 140 ALA B C   1 
ATOM   2133 O  O   . ALA B 1 140 ? -6.765  -1.057  23.928 1.00 84.13  ? 140 ALA B O   1 
ATOM   2134 C  CB  . ALA B 1 140 ? -7.145  -1.273  20.861 1.00 81.83  ? 140 ALA B CB  1 
ATOM   2135 N  N   . GLY B 1 141 ? -4.716  -1.329  23.002 1.00 86.63  ? 141 GLY B N   1 
ATOM   2136 C  CA  . GLY B 1 141 ? -4.097  -1.864  24.194 1.00 87.83  ? 141 GLY B CA  1 
ATOM   2137 C  C   . GLY B 1 141 ? -4.165  -3.366  24.207 1.00 86.01  ? 141 GLY B C   1 
ATOM   2138 O  O   . GLY B 1 141 ? -4.458  -3.997  23.195 1.00 84.12  ? 141 GLY B O   1 
ATOM   2139 N  N   . SER B 1 142 ? -3.902  -3.927  25.378 1.00 87.14  ? 142 SER B N   1 
ATOM   2140 C  CA  . SER B 1 142 ? -3.789  -5.370  25.543 1.00 86.30  ? 142 SER B CA  1 
ATOM   2141 C  C   . SER B 1 142 ? -5.122  -6.036  25.306 1.00 83.20  ? 142 SER B C   1 
ATOM   2142 O  O   . SER B 1 142 ? -6.144  -5.366  25.127 1.00 81.97  ? 142 SER B O   1 
ATOM   2143 C  CB  . SER B 1 142 ? -3.279  -5.707  26.950 1.00 88.53  ? 142 SER B CB  1 
ATOM   2144 O  OG  . SER B 1 142 ? -4.137  -5.159  27.940 1.00 89.09  ? 142 SER B OG  1 
ATOM   2145 N  N   . ARG B 1 143 ? -5.095  -7.360  25.328 1.00 82.18  ? 143 ARG B N   1 
ATOM   2146 C  CA  . ARG B 1 143 ? -6.202  -8.158  24.857 1.00 79.91  ? 143 ARG B CA  1 
ATOM   2147 C  C   . ARG B 1 143 ? -6.991  -8.782  26.019 1.00 78.93  ? 143 ARG B C   1 
ATOM   2148 O  O   . ARG B 1 143 ? -6.697  -9.878  26.473 1.00 79.42  ? 143 ARG B O   1 
ATOM   2149 C  CB  . ARG B 1 143 ? -5.642  -9.211  23.903 1.00 79.92  ? 143 ARG B CB  1 
ATOM   2150 C  CG  . ARG B 1 143 ? -4.809  -8.596  22.797 1.00 82.45  ? 143 ARG B CG  1 
ATOM   2151 C  CD  . ARG B 1 143 ? -4.321  -9.617  21.809 1.00 84.97  ? 143 ARG B CD  1 
ATOM   2152 N  NE  . ARG B 1 143 ? -3.854  -8.978  20.579 1.00 87.35  ? 143 ARG B NE  1 
ATOM   2153 C  CZ  . ARG B 1 143 ? -3.342  -9.619  19.527 1.00 89.12  ? 143 ARG B CZ  1 
ATOM   2154 N  NH1 . ARG B 1 143 ? -3.208  -10.945 19.530 1.00 89.33  ? 143 ARG B NH1 1 
ATOM   2155 N  NH2 . ARG B 1 143 ? -2.957  -8.929  18.458 1.00 91.05  ? 143 ARG B NH2 1 
ATOM   2156 N  N   . LEU B 1 144 ? -8.014  -8.080  26.479 1.00 77.78  ? 144 LEU B N   1 
ATOM   2157 C  CA  . LEU B 1 144 ? -8.699  -8.445  27.709 1.00 78.03  ? 144 LEU B CA  1 
ATOM   2158 C  C   . LEU B 1 144 ? -9.421  -9.805  27.683 1.00 76.36  ? 144 LEU B C   1 
ATOM   2159 O  O   . LEU B 1 144 ? -9.399  -10.556 28.664 1.00 77.29  ? 144 LEU B O   1 
ATOM   2160 C  CB  . LEU B 1 144 ? -9.683  -7.335  28.079 1.00 78.31  ? 144 LEU B CB  1 
ATOM   2161 C  CG  . LEU B 1 144 ? -9.119  -6.087  28.746 1.00 81.09  ? 144 LEU B CG  1 
ATOM   2162 C  CD1 . LEU B 1 144 ? -10.278 -5.143  29.091 1.00 82.51  ? 144 LEU B CD1 1 
ATOM   2163 C  CD2 . LEU B 1 144 ? -8.285  -6.442  29.992 1.00 84.41  ? 144 LEU B CD2 1 
ATOM   2164 N  N   . ALA B 1 145 ? -10.086 -10.092 26.577 1.00 73.98  ? 145 ALA B N   1 
ATOM   2165 C  CA  . ALA B 1 145 ? -10.791 -11.343 26.405 1.00 73.16  ? 145 ALA B CA  1 
ATOM   2166 C  C   . ALA B 1 145 ? -10.900 -11.675 24.927 1.00 71.92  ? 145 ALA B C   1 
ATOM   2167 O  O   . ALA B 1 145 ? -10.827 -10.789 24.105 1.00 71.91  ? 145 ALA B O   1 
ATOM   2168 C  CB  . ALA B 1 145 ? -12.140 -11.227 26.993 1.00 72.88  ? 145 ALA B CB  1 
ATOM   2169 N  N   . CYS B 1 146 ? -11.075 -12.942 24.573 1.00 71.83  ? 146 CYS B N   1 
ATOM   2170 C  CA  . CYS B 1 146 ? -11.185 -13.337 23.155 1.00 70.95  ? 146 CYS B CA  1 
ATOM   2171 C  C   . CYS B 1 146 ? -11.719 -14.742 22.952 1.00 70.39  ? 146 CYS B C   1 
ATOM   2172 O  O   . CYS B 1 146 ? -11.755 -15.537 23.879 1.00 71.66  ? 146 CYS B O   1 
ATOM   2173 C  CB  . CYS B 1 146 ? -9.826  -13.269 22.481 1.00 71.65  ? 146 CYS B CB  1 
ATOM   2174 S  SG  . CYS B 1 146 ? -8.649  -14.544 23.002 1.00 75.27  ? 146 CYS B SG  1 
ATOM   2175 N  N   . GLY B 1 147 ? -12.124 -15.055 21.737 1.00 68.92  ? 147 GLY B N   1 
ATOM   2176 C  CA  . GLY B 1 147 ? -12.506 -16.404 21.440 1.00 69.06  ? 147 GLY B CA  1 
ATOM   2177 C  C   . GLY B 1 147 ? -12.630 -16.634 19.973 1.00 68.07  ? 147 GLY B C   1 
ATOM   2178 O  O   . GLY B 1 147 ? -12.830 -15.705 19.233 1.00 67.41  ? 147 GLY B O   1 
ATOM   2179 N  N   . VAL B 1 148 ? -12.525 -17.879 19.545 1.00 67.99  ? 148 VAL B N   1 
ATOM   2180 C  CA  . VAL B 1 148 ? -12.698 -18.186 18.139 1.00 67.32  ? 148 VAL B CA  1 
ATOM   2181 C  C   . VAL B 1 148 ? -14.139 -18.085 17.716 1.00 66.55  ? 148 VAL B C   1 
ATOM   2182 O  O   . VAL B 1 148 ? -15.023 -18.403 18.458 1.00 66.72  ? 148 VAL B O   1 
ATOM   2183 C  CB  . VAL B 1 148 ? -12.200 -19.561 17.815 1.00 68.54  ? 148 VAL B CB  1 
ATOM   2184 C  CG1 . VAL B 1 148 ? -12.505 -19.889 16.416 1.00 68.17  ? 148 VAL B CG1 1 
ATOM   2185 C  CG2 . VAL B 1 148 ? -10.732 -19.611 18.020 1.00 69.40  ? 148 VAL B CG2 1 
ATOM   2186 N  N   . ILE B 1 149 ? -14.358 -17.646 16.498 1.00 66.02  ? 149 ILE B N   1 
ATOM   2187 C  CA  . ILE B 1 149 ? -15.685 -17.436 15.968 1.00 66.14  ? 149 ILE B CA  1 
ATOM   2188 C  C   . ILE B 1 149 ? -16.129 -18.686 15.300 1.00 67.36  ? 149 ILE B C   1 
ATOM   2189 O  O   . ILE B 1 149 ? -15.446 -19.171 14.424 1.00 67.87  ? 149 ILE B O   1 
ATOM   2190 C  CB  . ILE B 1 149 ? -15.648 -16.386 14.864 1.00 66.02  ? 149 ILE B CB  1 
ATOM   2191 C  CG1 . ILE B 1 149 ? -15.607 -14.993 15.445 1.00 65.14  ? 149 ILE B CG1 1 
ATOM   2192 C  CG2 . ILE B 1 149 ? -16.848 -16.490 13.987 1.00 67.35  ? 149 ILE B CG2 1 
ATOM   2193 C  CD1 . ILE B 1 149 ? -14.982 -14.016 14.515 1.00 65.79  ? 149 ILE B CD1 1 
ATOM   2194 N  N   . GLY B 1 150 ? -17.293 -19.195 15.656 1.00 68.30  ? 150 GLY B N   1 
ATOM   2195 C  CA  . GLY B 1 150 ? -17.710 -20.501 15.142 1.00 70.53  ? 150 GLY B CA  1 
ATOM   2196 C  C   . GLY B 1 150 ? -19.101 -20.536 14.567 1.00 72.05  ? 150 GLY B C   1 
ATOM   2197 O  O   . GLY B 1 150 ? -19.882 -19.621 14.789 1.00 71.66  ? 150 GLY B O   1 
ATOM   2198 N  N   . ILE B 1 151 ? -19.412 -21.614 13.852 1.00 74.51  ? 151 ILE B N   1 
ATOM   2199 C  CA  . ILE B 1 151 ? -20.669 -21.709 13.126 1.00 76.94  ? 151 ILE B CA  1 
ATOM   2200 C  C   . ILE B 1 151 ? -21.765 -22.002 14.106 1.00 79.17  ? 151 ILE B C   1 
ATOM   2201 O  O   . ILE B 1 151 ? -21.661 -22.939 14.877 1.00 80.49  ? 151 ILE B O   1 
ATOM   2202 C  CB  . ILE B 1 151 ? -20.660 -22.800 12.082 1.00 78.90  ? 151 ILE B CB  1 
ATOM   2203 C  CG1 . ILE B 1 151 ? -19.511 -22.589 11.126 1.00 78.17  ? 151 ILE B CG1 1 
ATOM   2204 C  CG2 . ILE B 1 151 ? -21.938 -22.770 11.304 1.00 80.61  ? 151 ILE B CG2 1 
ATOM   2205 C  CD1 . ILE B 1 151 ? -19.403 -23.648 10.122 1.00 80.84  ? 151 ILE B CD1 1 
ATOM   2206 N  N   . ALA B 1 152 ? -22.818 -21.200 14.090 1.00 80.90  ? 152 ALA B N   1 
ATOM   2207 C  CA  . ALA B 1 152 ? -23.873 -21.293 15.099 1.00 83.10  ? 152 ALA B CA  1 
ATOM   2208 C  C   . ALA B 1 152 ? -25.069 -21.940 14.488 1.00 87.55  ? 152 ALA B C   1 
ATOM   2209 O  O   . ALA B 1 152 ? -25.198 -21.991 13.252 1.00 88.34  ? 152 ALA B O   1 
ATOM   2210 C  CB  . ALA B 1 152 ? -24.254 -19.941 15.580 1.00 82.08  ? 152 ALA B CB  1 
ATOM   2211 N  N   . GLN B 1 153 ? -25.963 -22.430 15.345 1.00 91.10  ? 153 GLN B N   1 
ATOM   2212 C  CA  . GLN B 1 153 ? -27.191 -23.023 14.817 1.00 96.08  ? 153 GLN B CA  1 
ATOM   2213 C  C   . GLN B 1 153 ? -28.079 -21.917 14.237 1.00 97.39  ? 153 GLN B C   1 
ATOM   2214 O  O   . GLN B 1 153 ? -28.290 -20.892 14.911 1.00 96.62  ? 153 GLN B O   1 
ATOM   2215 C  CB  . GLN B 1 153 ? -27.958 -23.866 15.850 1.00 98.83  ? 153 GLN B CB  1 
ATOM   2216 C  CG  . GLN B 1 153 ? -29.160 -24.597 15.176 1.00 103.53 ? 153 GLN B CG  1 
ATOM   2217 C  CD  . GLN B 1 153 ? -29.711 -25.769 15.979 1.00 107.43 ? 153 GLN B CD  1 
ATOM   2218 O  OE1 . GLN B 1 153 ? -29.876 -25.689 17.204 1.00 108.35 ? 153 GLN B OE1 1 
ATOM   2219 N  NE2 . GLN B 1 153 ? -30.014 -26.861 15.287 1.00 110.54 ? 153 GLN B NE2 1 
ATOM   2220 O  OXT . GLN B 1 153 ? -28.562 -22.029 13.090 1.00 100.04 ? 153 GLN B OXT 1 
ATOM   2221 N  N   . ALA C 1 1   ? 10.834  -76.629 4.550  1.00 116.09 ? 1   ALA C N   1 
ATOM   2222 C  CA  . ALA C 1 1   ? 10.158  -76.463 5.888  1.00 112.07 ? 1   ALA C CA  1 
ATOM   2223 C  C   . ALA C 1 1   ? 8.576   -76.522 5.816  1.00 112.03 ? 1   ALA C C   1 
ATOM   2224 O  O   . ALA C 1 1   ? 7.913   -75.521 5.456  1.00 111.28 ? 1   ALA C O   1 
ATOM   2225 C  CB  . ALA C 1 1   ? 10.650  -75.162 6.536  1.00 108.11 ? 1   ALA C CB  1 
ATOM   2226 N  N   . THR C 1 2   ? 8.003   -77.710 6.101  1.00 113.04 ? 2   THR C N   1 
ATOM   2227 C  CA  . THR C 1 2   ? 6.538   -77.909 6.250  1.00 112.72 ? 2   THR C CA  1 
ATOM   2228 C  C   . THR C 1 2   ? 6.124   -77.411 7.605  1.00 107.93 ? 2   THR C C   1 
ATOM   2229 O  O   . THR C 1 2   ? 5.119   -76.722 7.707  1.00 106.78 ? 2   THR C O   1 
ATOM   2230 C  CB  . THR C 1 2   ? 6.048   -79.437 6.130  1.00 117.01 ? 2   THR C CB  1 
ATOM   2231 O  OG1 . THR C 1 2   ? 6.065   -79.870 4.756  1.00 122.57 ? 2   THR C OG1 1 
ATOM   2232 C  CG2 . THR C 1 2   ? 4.601   -79.650 6.650  1.00 116.68 ? 2   THR C CG2 1 
ATOM   2233 N  N   . LYS C 1 3   ? 6.888   -77.766 8.644  1.00 105.63 ? 3   LYS C N   1 
ATOM   2234 C  CA  . LYS C 1 3   ? 6.529   -77.437 10.039 1.00 102.02 ? 3   LYS C CA  1 
ATOM   2235 C  C   . LYS C 1 3   ? 7.571   -76.577 10.715 1.00 98.01  ? 3   LYS C C   1 
ATOM   2236 O  O   . LYS C 1 3   ? 8.733   -76.515 10.274 1.00 98.26  ? 3   LYS C O   1 
ATOM   2237 C  CB  . LYS C 1 3   ? 6.331   -78.694 10.877 1.00 103.82 ? 3   LYS C CB  1 
ATOM   2238 C  CG  . LYS C 1 3   ? 5.108   -79.459 10.493 1.00 108.38 ? 3   LYS C CG  1 
ATOM   2239 C  CD  . LYS C 1 3   ? 4.865   -80.639 11.433 1.00 112.38 ? 3   LYS C CD  1 
ATOM   2240 C  CE  . LYS C 1 3   ? 4.109   -81.794 10.708 1.00 118.18 ? 3   LYS C CE  1 
ATOM   2241 N  NZ  . LYS C 1 3   ? 4.364   -83.126 11.338 1.00 121.95 ? 3   LYS C NZ  1 
ATOM   2242 N  N   . ALA C 1 4   ? 7.107   -75.895 11.767 1.00 94.32  ? 4   ALA C N   1 
ATOM   2243 C  CA  . ALA C 1 4   ? 7.956   -75.137 12.685 1.00 91.03  ? 4   ALA C CA  1 
ATOM   2244 C  C   . ALA C 1 4   ? 7.358   -75.070 14.091 1.00 89.04  ? 4   ALA C C   1 
ATOM   2245 O  O   . ALA C 1 4   ? 6.243   -75.539 14.345 1.00 89.67  ? 4   ALA C O   1 
ATOM   2246 C  CB  . ALA C 1 4   ? 8.216   -73.730 12.147 1.00 89.08  ? 4   ALA C CB  1 
ATOM   2247 N  N   . VAL C 1 5   ? 8.142   -74.509 15.001 1.00 86.92  ? 5   VAL C N   1 
ATOM   2248 C  CA  . VAL C 1 5   ? 7.764   -74.409 16.396 1.00 85.96  ? 5   VAL C CA  1 
ATOM   2249 C  C   . VAL C 1 5   ? 8.500   -73.254 17.047 1.00 84.32  ? 5   VAL C C   1 
ATOM   2250 O  O   . VAL C 1 5   ? 9.499   -72.770 16.510 1.00 83.79  ? 5   VAL C O   1 
ATOM   2251 C  CB  . VAL C 1 5   ? 8.107   -75.694 17.156 1.00 87.98  ? 5   VAL C CB  1 
ATOM   2252 C  CG1 . VAL C 1 5   ? 9.613   -75.815 17.359 1.00 87.97  ? 5   VAL C CG1 1 
ATOM   2253 C  CG2 . VAL C 1 5   ? 7.420   -75.715 18.481 1.00 87.27  ? 5   VAL C CG2 1 
ATOM   2254 N  N   . CYS C 1 6   ? 8.009   -72.812 18.197 1.00 83.94  ? 6   CYS C N   1 
ATOM   2255 C  CA  . CYS C 1 6   ? 8.647   -71.726 18.906 1.00 83.23  ? 6   CYS C CA  1 
ATOM   2256 C  C   . CYS C 1 6   ? 8.277   -71.757 20.357 1.00 84.13  ? 6   CYS C C   1 
ATOM   2257 O  O   . CYS C 1 6   ? 7.098   -71.750 20.668 1.00 84.40  ? 6   CYS C O   1 
ATOM   2258 C  CB  . CYS C 1 6   ? 8.185   -70.389 18.337 1.00 81.44  ? 6   CYS C CB  1 
ATOM   2259 S  SG  . CYS C 1 6   ? 8.689   -68.970 19.355 1.00 81.13  ? 6   CYS C SG  1 
ATOM   2260 N  N   . VAL C 1 7   ? 9.267   -71.749 21.243 1.00 85.17  ? 7   VAL C N   1 
ATOM   2261 C  CA  . VAL C 1 7   ? 8.980   -71.643 22.662 1.00 86.76  ? 7   VAL C CA  1 
ATOM   2262 C  C   . VAL C 1 7   ? 9.078   -70.215 23.155 1.00 86.30  ? 7   VAL C C   1 
ATOM   2263 O  O   . VAL C 1 7   ? 10.124  -69.571 23.071 1.00 86.06  ? 7   VAL C O   1 
ATOM   2264 C  CB  . VAL C 1 7   ? 9.922   -72.475 23.482 1.00 89.24  ? 7   VAL C CB  1 
ATOM   2265 C  CG1 . VAL C 1 7   ? 9.489   -72.453 24.950 1.00 91.14  ? 7   VAL C CG1 1 
ATOM   2266 C  CG2 . VAL C 1 7   ? 9.943   -73.872 22.956 1.00 90.66  ? 7   VAL C CG2 1 
ATOM   2267 N  N   . LEU C 1 8   ? 7.973   -69.743 23.706 1.00 86.95  ? 8   LEU C N   1 
ATOM   2268 C  CA  . LEU C 1 8   ? 7.878   -68.389 24.235 1.00 87.05  ? 8   LEU C CA  1 
ATOM   2269 C  C   . LEU C 1 8   ? 8.224   -68.340 25.697 1.00 90.62  ? 8   LEU C C   1 
ATOM   2270 O  O   . LEU C 1 8   ? 7.643   -69.067 26.492 1.00 92.51  ? 8   LEU C O   1 
ATOM   2271 C  CB  . LEU C 1 8   ? 6.459   -67.888 24.085 1.00 85.98  ? 8   LEU C CB  1 
ATOM   2272 C  CG  . LEU C 1 8   ? 6.078   -67.698 22.619 1.00 82.96  ? 8   LEU C CG  1 
ATOM   2273 C  CD1 . LEU C 1 8   ? 4.614   -67.493 22.464 1.00 80.91  ? 8   LEU C CD1 1 
ATOM   2274 C  CD2 . LEU C 1 8   ? 6.846   -66.517 22.057 1.00 82.52  ? 8   LEU C CD2 1 
ATOM   2275 N  N   . LYS C 1 9   ? 9.171   -67.477 26.035 1.00 92.53  ? 9   LYS C N   1 
ATOM   2276 C  CA  . LYS C 1 9   ? 9.649   -67.306 27.405 1.00 97.27  ? 9   LYS C CA  1 
ATOM   2277 C  C   . LYS C 1 9   ? 9.897   -65.842 27.607 1.00 97.55  ? 9   LYS C C   1 
ATOM   2278 O  O   . LYS C 1 9   ? 10.018  -65.078 26.653 1.00 95.38  ? 9   LYS C O   1 
ATOM   2279 C  CB  . LYS C 1 9   ? 10.997  -68.007 27.642 1.00 99.79  ? 9   LYS C CB  1 
ATOM   2280 C  CG  . LYS C 1 9   ? 10.993  -69.556 27.581 1.00 104.09 ? 9   LYS C CG  1 
ATOM   2281 C  CD  . LYS C 1 9   ? 10.703  -70.231 28.955 1.00 111.77 ? 9   LYS C CD  1 
ATOM   2282 C  CE  . LYS C 1 9   ? 11.240  -71.690 28.996 1.00 115.16 ? 9   LYS C CE  1 
ATOM   2283 N  NZ  . LYS C 1 9   ? 10.733  -72.471 30.178 1.00 120.40 ? 9   LYS C NZ  1 
ATOM   2284 N  N   . GLY C 1 10  ? 10.022  -65.459 28.861 1.00 101.30 ? 10  GLY C N   1 
ATOM   2285 C  CA  . GLY C 1 10  ? 10.315  -64.074 29.189 1.00 102.56 ? 10  GLY C CA  1 
ATOM   2286 C  C   . GLY C 1 10  ? 10.665  -63.927 30.662 1.00 107.56 ? 10  GLY C C   1 
ATOM   2287 O  O   . GLY C 1 10  ? 10.679  -64.915 31.415 1.00 110.04 ? 10  GLY C O   1 
ATOM   2288 N  N   . ASP C 1 11  ? 10.928  -62.687 31.070 1.00 109.61 ? 11  ASP C N   1 
ATOM   2289 C  CA  . ASP C 1 11  ? 11.123  -62.353 32.484 1.00 115.11 ? 11  ASP C CA  1 
ATOM   2290 C  C   . ASP C 1 11  ? 9.877   -62.582 33.343 1.00 117.00 ? 11  ASP C C   1 
ATOM   2291 O  O   . ASP C 1 11  ? 9.972   -62.876 34.548 1.00 121.33 ? 11  ASP C O   1 
ATOM   2292 C  CB  . ASP C 1 11  ? 11.506  -60.887 32.610 1.00 116.84 ? 11  ASP C CB  1 
ATOM   2293 C  CG  . ASP C 1 11  ? 12.920  -60.624 32.144 1.00 119.13 ? 11  ASP C CG  1 
ATOM   2294 O  OD1 . ASP C 1 11  ? 13.737  -61.589 32.182 1.00 122.49 ? 11  ASP C OD1 1 
ATOM   2295 O  OD2 . ASP C 1 11  ? 13.203  -59.461 31.730 1.00 121.84 ? 11  ASP C OD2 1 
ATOM   2296 N  N   . GLY C 1 12  ? 8.709   -62.409 32.715 1.00 113.91 ? 12  GLY C N   1 
ATOM   2297 C  CA  . GLY C 1 12  ? 7.424   -62.612 33.372 1.00 115.01 ? 12  GLY C CA  1 
ATOM   2298 C  C   . GLY C 1 12  ? 7.178   -64.066 33.701 1.00 115.71 ? 12  GLY C C   1 
ATOM   2299 O  O   . GLY C 1 12  ? 8.045   -64.937 33.531 1.00 115.47 ? 12  GLY C O   1 
ATOM   2300 N  N   . PRO C 1 13  ? 5.970   -64.344 34.161 1.00 116.56 ? 13  PRO C N   1 
ATOM   2301 C  CA  . PRO C 1 13  ? 5.518   -65.713 34.322 1.00 117.15 ? 13  PRO C CA  1 
ATOM   2302 C  C   . PRO C 1 13  ? 4.920   -66.275 33.009 1.00 111.91 ? 13  PRO C C   1 
ATOM   2303 O  O   . PRO C 1 13  ? 4.521   -67.449 32.937 1.00 112.12 ? 13  PRO C O   1 
ATOM   2304 C  CB  . PRO C 1 13  ? 4.429   -65.543 35.358 1.00 121.34 ? 13  PRO C CB  1 
ATOM   2305 C  CG  . PRO C 1 13  ? 3.773   -64.228 34.992 1.00 119.41 ? 13  PRO C CG  1 
ATOM   2306 C  CD  . PRO C 1 13  ? 4.885   -63.372 34.411 1.00 117.14 ? 13  PRO C CD  1 
ATOM   2307 N  N   . VAL C 1 14  ? 4.885   -65.425 31.983 1.00 107.39 ? 14  VAL C N   1 
ATOM   2308 C  CA  . VAL C 1 14  ? 4.278   -65.762 30.705 1.00 102.84 ? 14  VAL C CA  1 
ATOM   2309 C  C   . VAL C 1 14  ? 5.134   -66.785 30.025 1.00 101.05 ? 14  VAL C C   1 
ATOM   2310 O  O   . VAL C 1 14  ? 6.362   -66.701 30.055 1.00 101.26 ? 14  VAL C O   1 
ATOM   2311 C  CB  . VAL C 1 14  ? 4.205   -64.549 29.761 1.00 99.39  ? 14  VAL C CB  1 
ATOM   2312 C  CG1 . VAL C 1 14  ? 3.238   -64.855 28.617 1.00 95.14  ? 14  VAL C CG1 1 
ATOM   2313 C  CG2 . VAL C 1 14  ? 3.834   -63.255 30.550 1.00 102.02 ? 14  VAL C CG2 1 
ATOM   2314 N  N   . GLN C 1 15  ? 4.488   -67.748 29.405 1.00 99.64  ? 15  GLN C N   1 
ATOM   2315 C  CA  . GLN C 1 15  ? 5.219   -68.744 28.644 1.00 98.48  ? 15  GLN C CA  1 
ATOM   2316 C  C   . GLN C 1 15  ? 4.285   -69.674 27.882 1.00 96.97  ? 15  GLN C C   1 
ATOM   2317 O  O   . GLN C 1 15  ? 3.140   -69.903 28.289 1.00 98.63  ? 15  GLN C O   1 
ATOM   2318 C  CB  . GLN C 1 15  ? 6.126   -69.571 29.564 1.00 102.23 ? 15  GLN C CB  1 
ATOM   2319 C  CG  . GLN C 1 15  ? 5.377   -70.584 30.445 1.00 107.31 ? 15  GLN C CG  1 
ATOM   2320 C  CD  . GLN C 1 15  ? 6.280   -71.326 31.448 1.00 113.35 ? 15  GLN C CD  1 
ATOM   2321 O  OE1 . GLN C 1 15  ? 5.777   -72.106 32.282 1.00 118.53 ? 15  GLN C OE1 1 
ATOM   2322 N  NE2 . GLN C 1 15  ? 7.613   -71.094 31.367 1.00 112.86 ? 15  GLN C NE2 1 
ATOM   2323 N  N   . GLY C 1 16  ? 4.781   -70.230 26.790 1.00 94.04  ? 16  GLY C N   1 
ATOM   2324 C  CA  . GLY C 1 16  ? 3.979   -71.151 26.024 1.00 93.33  ? 16  GLY C CA  1 
ATOM   2325 C  C   . GLY C 1 16  ? 4.753   -71.753 24.887 1.00 91.25  ? 16  GLY C C   1 
ATOM   2326 O  O   . GLY C 1 16  ? 5.942   -71.471 24.732 1.00 90.55  ? 16  GLY C O   1 
ATOM   2327 N  N   . ILE C 1 17  ? 4.076   -72.602 24.117 1.00 90.65  ? 17  ILE C N   1 
ATOM   2328 C  CA  . ILE C 1 17  ? 4.647   -73.258 22.952 1.00 89.41  ? 17  ILE C CA  1 
ATOM   2329 C  C   . ILE C 1 17  ? 3.703   -73.024 21.810 1.00 87.72  ? 17  ILE C C   1 
ATOM   2330 O  O   . ILE C 1 17  ? 2.509   -73.134 21.994 1.00 88.51  ? 17  ILE C O   1 
ATOM   2331 C  CB  . ILE C 1 17  ? 4.697   -74.774 23.135 1.00 92.47  ? 17  ILE C CB  1 
ATOM   2332 C  CG1 . ILE C 1 17  ? 5.186   -75.150 24.552 1.00 95.58  ? 17  ILE C CG1 1 
ATOM   2333 C  CG2 . ILE C 1 17  ? 5.523   -75.429 22.011 1.00 91.92  ? 17  ILE C CG2 1 
ATOM   2334 C  CD1 . ILE C 1 17  ? 6.503   -75.925 24.585 1.00 97.53  ? 17  ILE C CD1 1 
ATOM   2335 N  N   . ILE C 1 18  ? 4.216   -72.699 20.633 1.00 85.99  ? 18  ILE C N   1 
ATOM   2336 C  CA  . ILE C 1 18  ? 3.351   -72.446 19.484 1.00 85.54  ? 18  ILE C CA  1 
ATOM   2337 C  C   . ILE C 1 18  ? 3.877   -73.169 18.294 1.00 86.34  ? 18  ILE C C   1 
ATOM   2338 O  O   . ILE C 1 18  ? 5.059   -73.082 18.016 1.00 85.94  ? 18  ILE C O   1 
ATOM   2339 C  CB  . ILE C 1 18  ? 3.324   -70.952 19.088 1.00 83.24  ? 18  ILE C CB  1 
ATOM   2340 C  CG1 . ILE C 1 18  ? 2.758   -70.084 20.217 1.00 83.52  ? 18  ILE C CG1 1 
ATOM   2341 C  CG2 . ILE C 1 18  ? 2.513   -70.751 17.803 1.00 82.28  ? 18  ILE C CG2 1 
ATOM   2342 C  CD1 . ILE C 1 18  ? 1.361   -70.449 20.647 1.00 86.55  ? 18  ILE C CD1 1 
ATOM   2343 N  N   . ASN C 1 19  ? 2.999   -73.851 17.574 1.00 88.43  ? 19  ASN C N   1 
ATOM   2344 C  CA  . ASN C 1 19  ? 3.393   -74.622 16.395 1.00 90.28  ? 19  ASN C CA  1 
ATOM   2345 C  C   . ASN C 1 19  ? 2.941   -73.995 15.118 1.00 90.18  ? 19  ASN C C   1 
ATOM   2346 O  O   . ASN C 1 19  ? 2.026   -73.199 15.113 1.00 89.33  ? 19  ASN C O   1 
ATOM   2347 C  CB  . ASN C 1 19  ? 2.803   -76.021 16.466 1.00 93.51  ? 19  ASN C CB  1 
ATOM   2348 C  CG  . ASN C 1 19  ? 3.274   -76.770 17.685 1.00 95.40  ? 19  ASN C CG  1 
ATOM   2349 O  OD1 . ASN C 1 19  ? 2.619   -76.749 18.736 1.00 96.68  ? 19  ASN C OD1 1 
ATOM   2350 N  ND2 . ASN C 1 19  ? 4.455   -77.394 17.576 1.00 96.56  ? 19  ASN C ND2 1 
ATOM   2351 N  N   . PHE C 1 20  ? 3.597   -74.378 14.033 1.00 92.07  ? 20  PHE C N   1 
ATOM   2352 C  CA  . PHE C 1 20  ? 3.280   -73.867 12.710 1.00 93.31  ? 20  PHE C CA  1 
ATOM   2353 C  C   . PHE C 1 20  ? 3.252   -75.006 11.752 1.00 97.42  ? 20  PHE C C   1 
ATOM   2354 O  O   . PHE C 1 20  ? 4.029   -75.940 11.889 1.00 99.14  ? 20  PHE C O   1 
ATOM   2355 C  CB  . PHE C 1 20  ? 4.349   -72.905 12.215 1.00 91.65  ? 20  PHE C CB  1 
ATOM   2356 C  CG  . PHE C 1 20  ? 4.521   -71.677 13.075 1.00 89.30  ? 20  PHE C CG  1 
ATOM   2357 C  CD1 . PHE C 1 20  ? 5.071   -71.770 14.344 1.00 89.48  ? 20  PHE C CD1 1 
ATOM   2358 C  CD2 . PHE C 1 20  ? 4.170   -70.419 12.601 1.00 87.56  ? 20  PHE C CD2 1 
ATOM   2359 C  CE1 . PHE C 1 20  ? 5.245   -70.635 15.122 1.00 87.41  ? 20  PHE C CE1 1 
ATOM   2360 C  CE2 . PHE C 1 20  ? 4.345   -69.293 13.374 1.00 84.58  ? 20  PHE C CE2 1 
ATOM   2361 C  CZ  . PHE C 1 20  ? 4.878   -69.398 14.633 1.00 84.68  ? 20  PHE C CZ  1 
ATOM   2362 N  N   . GLU C 1 21  ? 2.382   -74.918 10.759 1.00 100.20 ? 21  GLU C N   1 
ATOM   2363 C  CA  . GLU C 1 21  ? 2.314   -75.934 9.721  1.00 104.89 ? 21  GLU C CA  1 
ATOM   2364 C  C   . GLU C 1 21  ? 1.905   -75.286 8.398  1.00 106.39 ? 21  GLU C C   1 
ATOM   2365 O  O   . GLU C 1 21  ? 0.919   -74.564 8.330  1.00 106.25 ? 21  GLU C O   1 
ATOM   2366 C  CB  . GLU C 1 21  ? 1.348   -77.067 10.135 1.00 108.02 ? 21  GLU C CB  1 
ATOM   2367 C  CG  . GLU C 1 21  ? 1.456   -78.341 9.235  1.00 114.82 ? 21  GLU C CG  1 
ATOM   2368 C  CD  . GLU C 1 21  ? 0.517   -79.513 9.645  1.00 121.37 ? 21  GLU C CD  1 
ATOM   2369 O  OE1 . GLU C 1 21  ? -0.650  -79.247 10.080 1.00 123.47 ? 21  GLU C OE1 1 
ATOM   2370 O  OE2 . GLU C 1 21  ? 0.956   -80.702 9.508  1.00 125.75 ? 21  GLU C OE2 1 
ATOM   2371 N  N   . GLN C 1 22  ? 2.697   -75.516 7.364  1.00 108.74 ? 22  GLN C N   1 
ATOM   2372 C  CA  . GLN C 1 22  ? 2.384   -75.042 6.028  1.00 111.66 ? 22  GLN C CA  1 
ATOM   2373 C  C   . GLN C 1 22  ? 2.410   -76.270 5.116  1.00 117.59 ? 22  GLN C C   1 
ATOM   2374 O  O   . GLN C 1 22  ? 3.461   -76.648 4.569  1.00 119.18 ? 22  GLN C O   1 
ATOM   2375 C  CB  . GLN C 1 22  ? 3.377   -73.965 5.578  1.00 109.80 ? 22  GLN C CB  1 
ATOM   2376 C  CG  . GLN C 1 22  ? 3.081   -73.366 4.207  1.00 112.33 ? 22  GLN C CG  1 
ATOM   2377 C  CD  . GLN C 1 22  ? 3.928   -72.119 3.875  1.00 110.67 ? 22  GLN C CD  1 
ATOM   2378 O  OE1 . GLN C 1 22  ? 5.154   -72.072 4.104  1.00 108.59 ? 22  GLN C OE1 1 
ATOM   2379 N  NE2 . GLN C 1 22  ? 3.265   -71.101 3.317  1.00 111.39 ? 22  GLN C NE2 1 
ATOM   2380 N  N   . LYS C 1 23  ? 1.246   -76.907 4.974  1.00 121.58 ? 23  LYS C N   1 
ATOM   2381 C  CA  . LYS C 1 23  ? 1.135   -78.103 4.133  1.00 127.87 ? 23  LYS C CA  1 
ATOM   2382 C  C   . LYS C 1 23  ? 1.481   -77.824 2.664  1.00 131.64 ? 23  LYS C C   1 
ATOM   2383 O  O   . LYS C 1 23  ? 2.089   -78.661 2.011  1.00 135.35 ? 23  LYS C O   1 
ATOM   2384 C  CB  . LYS C 1 23  ? -0.262  -78.748 4.231  1.00 131.15 ? 23  LYS C CB  1 
ATOM   2385 C  CG  . LYS C 1 23  ? -0.371  -79.812 5.369  1.00 132.79 ? 23  LYS C CG  1 
ATOM   2386 C  CD  . LYS C 1 23  ? -1.835  -80.041 5.850  1.00 136.25 ? 23  LYS C CD  1 
ATOM   2387 C  CE  . LYS C 1 23  ? -2.351  -78.831 6.702  1.00 133.18 ? 23  LYS C CE  1 
ATOM   2388 N  NZ  . LYS C 1 23  ? -3.791  -78.918 7.072  1.00 135.76 ? 23  LYS C NZ  1 
ATOM   2389 N  N   . GLU C 1 24  ? 1.107   -76.659 2.146  1.00 131.52 ? 24  GLU C N   1 
ATOM   2390 C  CA  . GLU C 1 24  ? 1.440   -76.326 0.772  1.00 135.69 ? 24  GLU C CA  1 
ATOM   2391 C  C   . GLU C 1 24  ? 2.451   -75.231 0.719  1.00 132.94 ? 24  GLU C C   1 
ATOM   2392 O  O   . GLU C 1 24  ? 2.310   -74.216 1.402  1.00 128.80 ? 24  GLU C O   1 
ATOM   2393 C  CB  . GLU C 1 24  ? 0.205   -75.860 0.040  1.00 139.12 ? 24  GLU C CB  1 
ATOM   2394 C  CG  . GLU C 1 24  ? -0.691  -77.011 -0.390 1.00 145.40 ? 24  GLU C CG  1 
ATOM   2395 C  CD  . GLU C 1 24  ? -1.828  -76.554 -1.290 1.00 150.78 ? 24  GLU C CD  1 
ATOM   2396 O  OE1 . GLU C 1 24  ? -2.259  -75.365 -1.141 1.00 148.71 ? 24  GLU C OE1 1 
ATOM   2397 O  OE2 . GLU C 1 24  ? -2.269  -77.391 -2.137 1.00 157.11 ? 24  GLU C OE2 1 
ATOM   2398 N  N   . SER C 1 25  ? 3.465   -75.432 -0.111 1.00 136.05 ? 25  SER C N   1 
ATOM   2399 C  CA  . SER C 1 25  ? 4.398   -74.358 -0.433 1.00 135.15 ? 25  SER C CA  1 
ATOM   2400 C  C   . SER C 1 25  ? 3.629   -73.096 -0.844 1.00 135.02 ? 25  SER C C   1 
ATOM   2401 O  O   . SER C 1 25  ? 2.718   -73.156 -1.694 1.00 139.12 ? 25  SER C O   1 
ATOM   2402 C  CB  . SER C 1 25  ? 5.318   -74.786 -1.577 1.00 140.31 ? 25  SER C CB  1 
ATOM   2403 O  OG  . SER C 1 25  ? 6.054   -73.665 -2.040 1.00 141.08 ? 25  SER C OG  1 
ATOM   2404 N  N   . ASN C 1 26  ? 3.986   -71.968 -0.223 1.00 130.61 ? 26  ASN C N   1 
ATOM   2405 C  CA  . ASN C 1 26  ? 3.295   -70.677 -0.461 1.00 130.32 ? 26  ASN C CA  1 
ATOM   2406 C  C   . ASN C 1 26  ? 1.767   -70.698 -0.214 1.00 129.55 ? 26  ASN C C   1 
ATOM   2407 O  O   . ASN C 1 26  ? 1.051   -69.775 -0.626 1.00 130.81 ? 26  ASN C O   1 
ATOM   2408 C  CB  . ASN C 1 26  ? 3.576   -70.152 -1.888 1.00 135.85 ? 26  ASN C CB  1 
ATOM   2409 C  CG  . ASN C 1 26  ? 5.028   -69.665 -2.080 1.00 136.79 ? 26  ASN C CG  1 
ATOM   2410 O  OD1 . ASN C 1 26  ? 5.739   -69.268 -1.118 1.00 133.43 ? 26  ASN C OD1 1 
ATOM   2411 N  ND2 . ASN C 1 26  ? 5.470   -69.687 -3.340 1.00 142.35 ? 26  ASN C ND2 1 
ATOM   2412 N  N   . GLY C 1 27  ? 1.275   -71.740 0.456  1.00 127.60 ? 27  GLY C N   1 
ATOM   2413 C  CA  . GLY C 1 27  ? -0.116  -71.796 0.872  1.00 126.32 ? 27  GLY C CA  1 
ATOM   2414 C  C   . GLY C 1 27  ? -0.294  -71.058 2.187  1.00 119.72 ? 27  GLY C C   1 
ATOM   2415 O  O   . GLY C 1 27  ? 0.540   -70.223 2.574  1.00 116.24 ? 27  GLY C O   1 
ATOM   2416 N  N   . PRO C 1 28  ? -1.375  -71.384 2.905  1.00 117.76 ? 28  PRO C N   1 
ATOM   2417 C  CA  . PRO C 1 28  ? -1.591  -70.772 4.201  1.00 112.34 ? 28  PRO C CA  1 
ATOM   2418 C  C   . PRO C 1 28  ? -0.826  -71.564 5.282  1.00 108.69 ? 28  PRO C C   1 
ATOM   2419 O  O   . PRO C 1 28  ? -0.281  -72.653 4.991  1.00 110.42 ? 28  PRO C O   1 
ATOM   2420 C  CB  . PRO C 1 28  ? -3.111  -70.923 4.389  1.00 113.81 ? 28  PRO C CB  1 
ATOM   2421 C  CG  . PRO C 1 28  ? -3.389  -72.299 3.788  1.00 118.38 ? 28  PRO C CG  1 
ATOM   2422 C  CD  . PRO C 1 28  ? -2.314  -72.506 2.689  1.00 121.29 ? 28  PRO C CD  1 
ATOM   2423 N  N   . VAL C 1 29  ? -0.838  -71.025 6.505  1.00 103.71 ? 29  VAL C N   1 
ATOM   2424 C  CA  . VAL C 1 29  ? -0.039  -71.516 7.603  1.00 100.45 ? 29  VAL C CA  1 
ATOM   2425 C  C   . VAL C 1 29  ? -0.866  -71.629 8.859  1.00 98.75  ? 29  VAL C C   1 
ATOM   2426 O  O   . VAL C 1 29  ? -1.219  -70.622 9.434  1.00 96.87  ? 29  VAL C O   1 
ATOM   2427 C  CB  . VAL C 1 29  ? 1.077   -70.498 7.930  1.00 97.27  ? 29  VAL C CB  1 
ATOM   2428 C  CG1 . VAL C 1 29  ? 1.844   -70.973 9.132  1.00 94.36  ? 29  VAL C CG1 1 
ATOM   2429 C  CG2 . VAL C 1 29  ? 2.009   -70.236 6.720  1.00 98.91  ? 29  VAL C CG2 1 
ATOM   2430 N  N   . LYS C 1 30  ? -1.168  -72.830 9.314  1.00 100.23 ? 30  LYS C N   1 
ATOM   2431 C  CA  . LYS C 1 30  ? -1.902  -72.965 10.587 1.00 99.55  ? 30  LYS C CA  1 
ATOM   2432 C  C   . LYS C 1 30  ? -0.959  -72.716 11.713 1.00 95.84  ? 30  LYS C C   1 
ATOM   2433 O  O   . LYS C 1 30  ? 0.108   -73.290 11.764 1.00 95.94  ? 30  LYS C O   1 
ATOM   2434 C  CB  . LYS C 1 30  ? -2.551  -74.354 10.787 1.00 103.26 ? 30  LYS C CB  1 
ATOM   2435 C  CG  . LYS C 1 30  ? -3.997  -74.464 10.238 1.00 108.82 ? 30  LYS C CG  1 
ATOM   2436 C  CD  . LYS C 1 30  ? -4.400  -75.898 9.782  1.00 115.99 ? 30  LYS C CD  1 
ATOM   2437 C  CE  . LYS C 1 30  ? -4.682  -75.956 8.237  1.00 120.45 ? 30  LYS C CE  1 
ATOM   2438 N  NZ  . LYS C 1 30  ? -5.928  -76.730 7.934  1.00 125.50 ? 30  LYS C NZ  1 
ATOM   2439 N  N   . VAL C 1 31  ? -1.368  -71.869 12.627 1.00 93.36  ? 31  VAL C N   1 
ATOM   2440 C  CA  . VAL C 1 31  ? -0.562  -71.551 13.772 1.00 90.83  ? 31  VAL C CA  1 
ATOM   2441 C  C   . VAL C 1 31  ? -1.344  -71.923 15.000 1.00 92.08  ? 31  VAL C C   1 
ATOM   2442 O  O   . VAL C 1 31  ? -2.406  -71.354 15.227 1.00 92.54  ? 31  VAL C O   1 
ATOM   2443 C  CB  . VAL C 1 31  ? -0.303  -70.058 13.826 1.00 88.04  ? 31  VAL C CB  1 
ATOM   2444 C  CG1 . VAL C 1 31  ? 0.467   -69.697 15.089 1.00 85.15  ? 31  VAL C CG1 1 
ATOM   2445 C  CG2 . VAL C 1 31  ? 0.427   -69.633 12.587 1.00 87.35  ? 31  VAL C CG2 1 
ATOM   2446 N  N   . TRP C 1 32  ? -0.856  -72.841 15.822 1.00 93.44  ? 32  TRP C N   1 
ATOM   2447 C  CA  . TRP C 1 32  ? -1.595  -73.114 17.047 1.00 95.26  ? 32  TRP C CA  1 
ATOM   2448 C  C   . TRP C 1 32  ? -0.728  -73.571 18.203 1.00 94.50  ? 32  TRP C C   1 
ATOM   2449 O  O   . TRP C 1 32  ? 0.379   -74.052 18.037 1.00 94.09  ? 32  TRP C O   1 
ATOM   2450 C  CB  . TRP C 1 32  ? -2.696  -74.135 16.765 1.00 99.32  ? 32  TRP C CB  1 
ATOM   2451 C  CG  . TRP C 1 32  ? -2.228  -75.484 16.965 1.00 105.26 ? 32  TRP C CG  1 
ATOM   2452 C  CD1 . TRP C 1 32  ? -2.466  -76.284 18.060 1.00 110.63 ? 32  TRP C CD1 1 
ATOM   2453 C  CD2 . TRP C 1 32  ? -1.378  -76.223 16.083 1.00 110.01 ? 32  TRP C CD2 1 
ATOM   2454 N  NE1 . TRP C 1 32  ? -1.825  -77.491 17.895 1.00 114.96 ? 32  TRP C NE1 1 
ATOM   2455 C  CE2 . TRP C 1 32  ? -1.153  -77.489 16.692 1.00 114.42 ? 32  TRP C CE2 1 
ATOM   2456 C  CE3 . TRP C 1 32  ? -0.785  -75.946 14.833 1.00 110.00 ? 32  TRP C CE3 1 
ATOM   2457 C  CZ2 . TRP C 1 32  ? -0.353  -78.500 16.081 1.00 116.92 ? 32  TRP C CZ2 1 
ATOM   2458 C  CZ3 . TRP C 1 32  ? 0.027   -76.956 14.215 1.00 112.85 ? 32  TRP C CZ3 1 
ATOM   2459 C  CH2 . TRP C 1 32  ? 0.225   -78.213 14.849 1.00 116.10 ? 32  TRP C CH2 1 
ATOM   2460 N  N   . GLY C 1 33  ? -1.272  -73.428 19.386 1.00 94.79  ? 33  GLY C N   1 
ATOM   2461 C  CA  . GLY C 1 33  ? -0.581  -73.826 20.566 1.00 95.49  ? 33  GLY C CA  1 
ATOM   2462 C  C   . GLY C 1 33  ? -1.241  -73.163 21.737 1.00 95.76  ? 33  GLY C C   1 
ATOM   2463 O  O   . GLY C 1 33  ? -2.422  -72.857 21.703 1.00 96.87  ? 33  GLY C O   1 
ATOM   2464 N  N   . SER C 1 34  ? -0.477  -72.913 22.778 1.00 95.32  ? 34  SER C N   1 
ATOM   2465 C  CA  . SER C 1 34  ? -1.063  -72.440 24.004 1.00 96.68  ? 34  SER C CA  1 
ATOM   2466 C  C   . SER C 1 34  ? -0.082  -71.627 24.822 1.00 95.62  ? 34  SER C C   1 
ATOM   2467 O  O   . SER C 1 34  ? 1.090   -71.994 24.935 1.00 95.78  ? 34  SER C O   1 
ATOM   2468 C  CB  . SER C 1 34  ? -1.501  -73.624 24.842 1.00 100.81 ? 34  SER C CB  1 
ATOM   2469 O  OG  . SER C 1 34  ? -2.171  -73.149 26.010 1.00 103.57 ? 34  SER C OG  1 
ATOM   2470 N  N   . ILE C 1 35  ? -0.562  -70.532 25.402 1.00 95.13  ? 35  ILE C N   1 
ATOM   2471 C  CA  . ILE C 1 35  ? 0.271   -69.682 26.243 1.00 94.87  ? 35  ILE C CA  1 
ATOM   2472 C  C   . ILE C 1 35  ? -0.415  -69.540 27.564 1.00 98.30  ? 35  ILE C C   1 
ATOM   2473 O  O   . ILE C 1 35  ? -1.636  -69.447 27.606 1.00 99.47  ? 35  ILE C O   1 
ATOM   2474 C  CB  . ILE C 1 35  ? 0.420   -68.253 25.663 1.00 91.76  ? 35  ILE C CB  1 
ATOM   2475 C  CG1 . ILE C 1 35  ? 0.758   -68.316 24.172 1.00 88.86  ? 35  ILE C CG1 1 
ATOM   2476 C  CG2 . ILE C 1 35  ? 1.468   -67.442 26.443 1.00 91.76  ? 35  ILE C CG2 1 
ATOM   2477 C  CD1 . ILE C 1 35  ? 0.919   -66.974 23.560 1.00 86.53  ? 35  ILE C CD1 1 
ATOM   2478 N  N   . LYS C 1 36  ? 0.369   -69.480 28.637 1.00 100.57 ? 36  LYS C N   1 
ATOM   2479 C  CA  . LYS C 1 36  ? -0.184  -69.253 29.969 1.00 104.72 ? 36  LYS C CA  1 
ATOM   2480 C  C   . LYS C 1 36  ? 0.530   -68.121 30.699 1.00 104.75 ? 36  LYS C C   1 
ATOM   2481 O  O   . LYS C 1 36  ? 1.625   -67.704 30.306 1.00 102.46 ? 36  LYS C O   1 
ATOM   2482 C  CB  . LYS C 1 36  ? -0.159  -70.549 30.797 1.00 109.40 ? 36  LYS C CB  1 
ATOM   2483 C  CG  . LYS C 1 36  ? 1.163   -71.340 30.753 1.00 111.60 ? 36  LYS C CG  1 
ATOM   2484 C  CD  . LYS C 1 36  ? 1.115   -72.578 31.701 1.00 118.82 ? 36  LYS C CD  1 
ATOM   2485 C  CE  . LYS C 1 36  ? 2.526   -73.006 32.216 1.00 120.65 ? 36  LYS C CE  1 
ATOM   2486 N  NZ  . LYS C 1 36  ? 2.428   -74.087 33.256 1.00 126.32 ? 36  LYS C NZ  1 
ATOM   2487 N  N   . GLY C 1 37  ? -0.118  -67.629 31.755 1.00 108.02 ? 37  GLY C N   1 
ATOM   2488 C  CA  . GLY C 1 37  ? 0.414   -66.542 32.582 1.00 109.49 ? 37  GLY C CA  1 
ATOM   2489 C  C   . GLY C 1 37  ? 0.085   -65.161 32.054 1.00 106.79 ? 37  GLY C C   1 
ATOM   2490 O  O   . GLY C 1 37  ? 0.872   -64.232 32.211 1.00 106.43 ? 37  GLY C O   1 
ATOM   2491 N  N   . LEU C 1 38  ? -1.084  -65.027 31.434 1.00 105.34 ? 38  LEU C N   1 
ATOM   2492 C  CA  . LEU C 1 38  ? -1.487  -63.777 30.792 1.00 102.94 ? 38  LEU C CA  1 
ATOM   2493 C  C   . LEU C 1 38  ? -2.593  -63.137 31.591 1.00 106.01 ? 38  LEU C C   1 
ATOM   2494 O  O   . LEU C 1 38  ? -3.345  -63.825 32.289 1.00 109.32 ? 38  LEU C O   1 
ATOM   2495 C  CB  . LEU C 1 38  ? -1.991  -64.057 29.372 1.00 99.44  ? 38  LEU C CB  1 
ATOM   2496 C  CG  . LEU C 1 38  ? -0.851  -64.303 28.386 1.00 96.11  ? 38  LEU C CG  1 
ATOM   2497 C  CD1 . LEU C 1 38  ? -1.246  -65.246 27.234 1.00 93.52  ? 38  LEU C CD1 1 
ATOM   2498 C  CD2 . LEU C 1 38  ? -0.328  -62.955 27.900 1.00 94.32  ? 38  LEU C CD2 1 
ATOM   2499 N  N   . THR C 1 39  ? -2.708  -61.819 31.482 1.00 105.28 ? 39  THR C N   1 
ATOM   2500 C  CA  . THR C 1 39  ? -3.877  -61.137 32.020 1.00 107.83 ? 39  THR C CA  1 
ATOM   2501 C  C   . THR C 1 39  ? -5.047  -61.528 31.129 1.00 106.55 ? 39  THR C C   1 
ATOM   2502 O  O   . THR C 1 39  ? -4.895  -61.606 29.904 1.00 102.67 ? 39  THR C O   1 
ATOM   2503 C  CB  . THR C 1 39  ? -3.682  -59.611 32.045 1.00 107.58 ? 39  THR C CB  1 
ATOM   2504 O  OG1 . THR C 1 39  ? -2.635  -59.249 31.143 1.00 103.52 ? 39  THR C OG1 1 
ATOM   2505 C  CG2 . THR C 1 39  ? -3.274  -59.152 33.435 1.00 111.97 ? 39  THR C CG2 1 
ATOM   2506 N  N   . GLU C 1 40  ? -6.197  -61.818 31.739 1.00 110.50 ? 40  GLU C N   1 
ATOM   2507 C  CA  . GLU C 1 40  ? -7.428  -62.101 30.971 1.00 110.36 ? 40  GLU C CA  1 
ATOM   2508 C  C   . GLU C 1 40  ? -7.597  -61.052 29.849 1.00 106.95 ? 40  GLU C C   1 
ATOM   2509 O  O   . GLU C 1 40  ? -7.303  -59.847 30.042 1.00 106.92 ? 40  GLU C O   1 
ATOM   2510 C  CB  . GLU C 1 40  ? -8.692  -62.094 31.879 1.00 115.35 ? 40  GLU C CB  1 
ATOM   2511 C  CG  . GLU C 1 40  ? -10.046 -62.165 31.094 1.00 116.21 ? 40  GLU C CG  1 
ATOM   2512 C  CD  . GLU C 1 40  ? -11.188 -62.767 31.921 1.00 122.83 ? 40  GLU C CD  1 
ATOM   2513 O  OE1 . GLU C 1 40  ? -11.388 -62.287 33.064 1.00 127.66 ? 40  GLU C OE1 1 
ATOM   2514 O  OE2 . GLU C 1 40  ? -11.868 -63.711 31.425 1.00 123.77 ? 40  GLU C OE2 1 
ATOM   2515 N  N   . GLY C 1 41  ? -8.053  -61.515 28.685 1.00 104.47 ? 41  GLY C N   1 
ATOM   2516 C  CA  . GLY C 1 41  ? -8.349  -60.607 27.584 1.00 101.87 ? 41  GLY C CA  1 
ATOM   2517 C  C   . GLY C 1 41  ? -7.413  -60.697 26.397 1.00 97.77  ? 41  GLY C C   1 
ATOM   2518 O  O   . GLY C 1 41  ? -6.788  -61.748 26.153 1.00 96.74  ? 41  GLY C O   1 
ATOM   2519 N  N   . LEU C 1 42  ? -7.332  -59.595 25.649 1.00 95.67  ? 42  LEU C N   1 
ATOM   2520 C  CA  . LEU C 1 42  ? -6.592  -59.601 24.387 1.00 92.41  ? 42  LEU C CA  1 
ATOM   2521 C  C   . LEU C 1 42  ? -5.123  -59.288 24.575 1.00 90.45  ? 42  LEU C C   1 
ATOM   2522 O  O   . LEU C 1 42  ? -4.756  -58.472 25.442 1.00 91.94  ? 42  LEU C O   1 
ATOM   2523 C  CB  . LEU C 1 42  ? -7.175  -58.599 23.398 1.00 91.98  ? 42  LEU C CB  1 
ATOM   2524 C  CG  . LEU C 1 42  ? -8.499  -58.997 22.740 1.00 93.36  ? 42  LEU C CG  1 
ATOM   2525 C  CD1 . LEU C 1 42  ? -9.673  -58.180 23.332 1.00 96.82  ? 42  LEU C CD1 1 
ATOM   2526 C  CD2 . LEU C 1 42  ? -8.393  -58.810 21.232 1.00 90.94  ? 42  LEU C CD2 1 
ATOM   2527 N  N   . HIS C 1 43  ? -4.293  -59.918 23.746 1.00 87.35  ? 43  HIS C N   1 
ATOM   2528 C  CA  . HIS C 1 43  ? -2.871  -59.632 23.747 1.00 85.56  ? 43  HIS C CA  1 
ATOM   2529 C  C   . HIS C 1 43  ? -2.309  -59.676 22.342 1.00 82.80  ? 43  HIS C C   1 
ATOM   2530 O  O   . HIS C 1 43  ? -2.622  -60.573 21.557 1.00 81.68  ? 43  HIS C O   1 
ATOM   2531 C  CB  . HIS C 1 43  ? -2.141  -60.622 24.605 1.00 86.12  ? 43  HIS C CB  1 
ATOM   2532 C  CG  . HIS C 1 43  ? -2.399  -60.458 26.069 1.00 89.55  ? 43  HIS C CG  1 
ATOM   2533 N  ND1 . HIS C 1 43  ? -1.589  -59.698 26.891 1.00 91.98  ? 43  HIS C ND1 1 
ATOM   2534 C  CD2 . HIS C 1 43  ? -3.360  -60.981 26.866 1.00 92.70  ? 43  HIS C CD2 1 
ATOM   2535 C  CE1 . HIS C 1 43  ? -2.032  -59.774 28.134 1.00 95.95  ? 43  HIS C CE1 1 
ATOM   2536 N  NE2 . HIS C 1 43  ? -3.113  -60.536 28.145 1.00 96.43  ? 43  HIS C NE2 1 
ATOM   2537 N  N   . GLY C 1 44  ? -1.487  -58.681 22.032 1.00 81.83  ? 44  GLY C N   1 
ATOM   2538 C  CA  . GLY C 1 44  ? -0.868  -58.582 20.727 1.00 80.25  ? 44  GLY C CA  1 
ATOM   2539 C  C   . GLY C 1 44  ? 0.088   -59.717 20.473 1.00 78.97  ? 44  GLY C C   1 
ATOM   2540 O  O   . GLY C 1 44  ? 0.685   -60.251 21.392 1.00 79.18  ? 44  GLY C O   1 
ATOM   2541 N  N   . PHE C 1 45  ? 0.264   -60.042 19.199 1.00 78.20  ? 45  PHE C N   1 
ATOM   2542 C  CA  . PHE C 1 45  ? 0.907   -61.285 18.792 1.00 77.67  ? 45  PHE C CA  1 
ATOM   2543 C  C   . PHE C 1 45  ? 1.521   -61.167 17.409 1.00 77.09  ? 45  PHE C C   1 
ATOM   2544 O  O   . PHE C 1 45  ? 0.798   -61.142 16.404 1.00 76.89  ? 45  PHE C O   1 
ATOM   2545 C  CB  . PHE C 1 45  ? -0.172  -62.344 18.768 1.00 78.43  ? 45  PHE C CB  1 
ATOM   2546 C  CG  . PHE C 1 45  ? 0.329   -63.747 18.619 1.00 78.65  ? 45  PHE C CG  1 
ATOM   2547 C  CD1 . PHE C 1 45  ? 1.111   -64.332 19.609 1.00 79.17  ? 45  PHE C CD1 1 
ATOM   2548 C  CD2 . PHE C 1 45  ? -0.053  -64.507 17.525 1.00 79.05  ? 45  PHE C CD2 1 
ATOM   2549 C  CE1 . PHE C 1 45  ? 1.534   -65.636 19.480 1.00 79.98  ? 45  PHE C CE1 1 
ATOM   2550 C  CE2 . PHE C 1 45  ? 0.359   -65.801 17.391 1.00 79.41  ? 45  PHE C CE2 1 
ATOM   2551 C  CZ  . PHE C 1 45  ? 1.157   -66.376 18.366 1.00 80.08  ? 45  PHE C CZ  1 
ATOM   2552 N  N   . HIS C 1 46  ? 2.848   -61.074 17.368 1.00 76.94  ? 46  HIS C N   1 
ATOM   2553 C  CA  . HIS C 1 46  ? 3.532   -60.722 16.143 1.00 77.57  ? 46  HIS C CA  1 
ATOM   2554 C  C   . HIS C 1 46  ? 4.820   -61.465 15.943 1.00 77.17  ? 46  HIS C C   1 
ATOM   2555 O  O   . HIS C 1 46  ? 5.492   -61.813 16.911 1.00 77.02  ? 46  HIS C O   1 
ATOM   2556 C  CB  . HIS C 1 46  ? 3.910   -59.247 16.159 1.00 78.66  ? 46  HIS C CB  1 
ATOM   2557 C  CG  . HIS C 1 46  ? 2.839   -58.357 16.669 1.00 80.93  ? 46  HIS C CG  1 
ATOM   2558 N  ND1 . HIS C 1 46  ? 3.010   -57.572 17.782 1.00 83.47  ? 46  HIS C ND1 1 
ATOM   2559 C  CD2 . HIS C 1 46  ? 1.577   -58.140 16.231 1.00 83.71  ? 46  HIS C CD2 1 
ATOM   2560 C  CE1 . HIS C 1 46  ? 1.892   -56.905 18.010 1.00 85.81  ? 46  HIS C CE1 1 
ATOM   2561 N  NE2 . HIS C 1 46  ? 1.008   -57.230 17.081 1.00 84.94  ? 46  HIS C NE2 1 
ATOM   2562 N  N   . VAL C 1 47  ? 5.188   -61.637 14.678 1.00 77.50  ? 47  VAL C N   1 
ATOM   2563 C  CA  . VAL C 1 47  ? 6.527   -62.019 14.333 1.00 77.86  ? 47  VAL C CA  1 
ATOM   2564 C  C   . VAL C 1 47  ? 7.322   -60.752 14.159 1.00 79.10  ? 47  VAL C C   1 
ATOM   2565 O  O   . VAL C 1 47  ? 6.944   -59.899 13.367 1.00 80.29  ? 47  VAL C O   1 
ATOM   2566 C  CB  . VAL C 1 47  ? 6.572   -62.739 13.025 1.00 78.61  ? 47  VAL C CB  1 
ATOM   2567 C  CG1 . VAL C 1 47  ? 7.992   -63.124 12.738 1.00 79.30  ? 47  VAL C CG1 1 
ATOM   2568 C  CG2 . VAL C 1 47  ? 5.714   -63.941 13.081 1.00 78.06  ? 47  VAL C CG2 1 
ATOM   2569 N  N   . HIS C 1 48  ? 8.417   -60.617 14.890 1.00 79.74  ? 48  HIS C N   1 
ATOM   2570 C  CA  . HIS C 1 48  ? 9.297   -59.463 14.734 1.00 81.71  ? 48  HIS C CA  1 
ATOM   2571 C  C   . HIS C 1 48  ? 10.441  -59.835 13.806 1.00 82.95  ? 48  HIS C C   1 
ATOM   2572 O  O   . HIS C 1 48  ? 10.620  -61.005 13.492 1.00 82.51  ? 48  HIS C O   1 
ATOM   2573 C  CB  . HIS C 1 48  ? 9.810   -59.006 16.088 1.00 82.06  ? 48  HIS C CB  1 
ATOM   2574 C  CG  . HIS C 1 48  ? 8.751   -58.395 16.940 1.00 83.00  ? 48  HIS C CG  1 
ATOM   2575 N  ND1 . HIS C 1 48  ? 8.898   -57.160 17.531 1.00 85.57  ? 48  HIS C ND1 1 
ATOM   2576 C  CD2 . HIS C 1 48  ? 7.520   -58.840 17.290 1.00 83.38  ? 48  HIS C CD2 1 
ATOM   2577 C  CE1 . HIS C 1 48  ? 7.807   -56.874 18.220 1.00 86.43  ? 48  HIS C CE1 1 
ATOM   2578 N  NE2 . HIS C 1 48  ? 6.955   -57.879 18.091 1.00 84.53  ? 48  HIS C NE2 1 
ATOM   2579 N  N   . GLU C 1 49  ? 11.214  -58.842 13.378 1.00 85.01  ? 49  GLU C N   1 
ATOM   2580 C  CA  . GLU C 1 49  ? 12.211  -59.041 12.324 1.00 87.16  ? 49  GLU C CA  1 
ATOM   2581 C  C   . GLU C 1 49  ? 13.336  -60.028 12.657 1.00 86.95  ? 49  GLU C C   1 
ATOM   2582 O  O   . GLU C 1 49  ? 13.702  -60.846 11.821 1.00 87.12  ? 49  GLU C O   1 
ATOM   2583 C  CB  . GLU C 1 49  ? 12.828  -57.700 11.914 1.00 90.06  ? 49  GLU C CB  1 
ATOM   2584 C  CG  . GLU C 1 49  ? 13.540  -57.749 10.549 1.00 94.22  ? 49  GLU C CG  1 
ATOM   2585 C  CD  . GLU C 1 49  ? 13.898  -56.363 9.982  1.00 99.91  ? 49  GLU C CD  1 
ATOM   2586 O  OE1 . GLU C 1 49  ? 13.325  -55.315 10.423 1.00 101.83 ? 49  GLU C OE1 1 
ATOM   2587 O  OE2 . GLU C 1 49  ? 14.767  -56.340 9.078  1.00 104.26 ? 49  GLU C OE2 1 
ATOM   2588 N  N   . PHE C 1 50  ? 13.873  -59.957 13.871 1.00 86.75  ? 50  PHE C N   1 
ATOM   2589 C  CA  . PHE C 1 50  ? 15.118  -60.665 14.182 1.00 87.89  ? 50  PHE C CA  1 
ATOM   2590 C  C   . PHE C 1 50  ? 15.030  -61.794 15.195 1.00 86.41  ? 50  PHE C C   1 
ATOM   2591 O  O   . PHE C 1 50  ? 14.276  -61.720 16.170 1.00 85.03  ? 50  PHE C O   1 
ATOM   2592 C  CB  . PHE C 1 50  ? 16.162  -59.674 14.697 1.00 90.18  ? 50  PHE C CB  1 
ATOM   2593 C  CG  . PHE C 1 50  ? 16.437  -58.533 13.757 1.00 93.81  ? 50  PHE C CG  1 
ATOM   2594 C  CD1 . PHE C 1 50  ? 16.630  -58.770 12.383 1.00 95.97  ? 50  PHE C CD1 1 
ATOM   2595 C  CD2 . PHE C 1 50  ? 16.532  -57.229 14.242 1.00 96.62  ? 50  PHE C CD2 1 
ATOM   2596 C  CE1 . PHE C 1 50  ? 16.892  -57.735 11.516 1.00 99.11  ? 50  PHE C CE1 1 
ATOM   2597 C  CE2 . PHE C 1 50  ? 16.792  -56.182 13.378 1.00 99.75  ? 50  PHE C CE2 1 
ATOM   2598 C  CZ  . PHE C 1 50  ? 16.971  -56.433 12.008 1.00 101.05 ? 50  PHE C CZ  1 
ATOM   2599 N  N   . GLY C 1 51  ? 15.862  -62.816 14.975 1.00 87.17  ? 51  GLY C N   1 
ATOM   2600 C  CA  . GLY C 1 51  ? 16.032  -63.917 15.919 1.00 86.95  ? 51  GLY C CA  1 
ATOM   2601 C  C   . GLY C 1 51  ? 17.097  -63.574 16.941 1.00 88.68  ? 51  GLY C C   1 
ATOM   2602 O  O   . GLY C 1 51  ? 17.956  -64.365 17.281 1.00 89.71  ? 51  GLY C O   1 
ATOM   2603 N  N   . ASP C 1 52  ? 17.029  -62.368 17.450 1.00 89.65  ? 52  ASP C N   1 
ATOM   2604 C  CA  . ASP C 1 52  ? 18.027  -61.882 18.360 1.00 92.15  ? 52  ASP C CA  1 
ATOM   2605 C  C   . ASP C 1 52  ? 17.365  -61.932 19.708 1.00 91.85  ? 52  ASP C C   1 
ATOM   2606 O  O   . ASP C 1 52  ? 16.242  -61.435 19.879 1.00 90.70  ? 52  ASP C O   1 
ATOM   2607 C  CB  . ASP C 1 52  ? 18.386  -60.440 17.970 1.00 93.98  ? 52  ASP C CB  1 
ATOM   2608 C  CG  . ASP C 1 52  ? 19.822  -60.069 18.284 1.00 97.30  ? 52  ASP C CG  1 
ATOM   2609 O  OD1 . ASP C 1 52  ? 20.207  -60.261 19.466 1.00 98.10  ? 52  ASP C OD1 1 
ATOM   2610 O  OD2 . ASP C 1 52  ? 20.520  -59.566 17.343 1.00 99.70  ? 52  ASP C OD2 1 
ATOM   2611 N  N   . ASN C 1 53  ? 18.021  -62.569 20.659 1.00 93.56  ? 53  ASN C N   1 
ATOM   2612 C  CA  . ASN C 1 53  ? 17.550  -62.505 22.037 1.00 94.76  ? 53  ASN C CA  1 
ATOM   2613 C  C   . ASN C 1 53  ? 18.670  -62.099 22.973 1.00 97.71  ? 53  ASN C C   1 
ATOM   2614 O  O   . ASN C 1 53  ? 18.598  -62.347 24.185 1.00 99.15  ? 53  ASN C O   1 
ATOM   2615 C  CB  . ASN C 1 53  ? 16.944  -63.829 22.446 1.00 94.18  ? 53  ASN C CB  1 
ATOM   2616 C  CG  . ASN C 1 53  ? 15.435  -63.884 22.192 1.00 94.65  ? 53  ASN C CG  1 
ATOM   2617 O  OD1 . ASN C 1 53  ? 14.697  -64.290 23.077 1.00 100.13 ? 53  ASN C OD1 1 
ATOM   2618 N  ND2 . ASN C 1 53  ? 14.972  -63.467 21.001 1.00 93.69  ? 53  ASN C ND2 1 
ATOM   2619 N  N   . THR C 1 54  ? 19.680  -61.444 22.378 1.00 98.91  ? 54  THR C N   1 
ATOM   2620 C  CA  . THR C 1 54  ? 20.868  -60.962 23.071 1.00 102.30 ? 54  THR C CA  1 
ATOM   2621 C  C   . THR C 1 54  ? 20.488  -60.214 24.323 1.00 104.06 ? 54  THR C C   1 
ATOM   2622 O  O   . THR C 1 54  ? 20.958  -60.548 25.393 1.00 106.71 ? 54  THR C O   1 
ATOM   2623 C  CB  . THR C 1 54  ? 21.662  -60.025 22.166 1.00 103.69 ? 54  THR C CB  1 
ATOM   2624 O  OG1 . THR C 1 54  ? 21.984  -60.737 20.967 1.00 102.09 ? 54  THR C OG1 1 
ATOM   2625 C  CG2 . THR C 1 54  ? 22.956  -59.519 22.864 1.00 108.63 ? 54  THR C CG2 1 
ATOM   2626 N  N   . ALA C 1 55  ? 19.626  -59.213 24.171 1.00 103.30 ? 55  ALA C N   1 
ATOM   2627 C  CA  . ALA C 1 55  ? 19.136  -58.408 25.291 1.00 105.52 ? 55  ALA C CA  1 
ATOM   2628 C  C   . ALA C 1 55  ? 17.643  -58.644 25.489 1.00 103.16 ? 55  ALA C C   1 
ATOM   2629 O  O   . ALA C 1 55  ? 16.829  -57.745 25.234 1.00 102.25 ? 55  ALA C O   1 
ATOM   2630 C  CB  . ALA C 1 55  ? 19.412  -56.911 25.042 1.00 107.36 ? 55  ALA C CB  1 
ATOM   2631 N  N   . GLY C 1 56  ? 17.291  -59.848 25.943 1.00 102.82 ? 56  GLY C N   1 
ATOM   2632 C  CA  . GLY C 1 56  ? 15.885  -60.233 26.111 1.00 101.04 ? 56  GLY C CA  1 
ATOM   2633 C  C   . GLY C 1 56  ? 15.087  -60.069 24.813 1.00 97.91  ? 56  GLY C C   1 
ATOM   2634 O  O   . GLY C 1 56  ? 15.608  -60.316 23.690 1.00 96.46  ? 56  GLY C O   1 
ATOM   2635 N  N   . CYS C 1 57  ? 13.827  -59.641 24.958 1.00 96.96  ? 57  CYS C N   1 
ATOM   2636 C  CA  . CYS C 1 57  ? 12.947  -59.541 23.804 1.00 94.27  ? 57  CYS C CA  1 
ATOM   2637 C  C   . CYS C 1 57  ? 13.150  -58.281 22.979 1.00 94.09  ? 57  CYS C C   1 
ATOM   2638 O  O   . CYS C 1 57  ? 12.815  -58.278 21.802 1.00 92.20  ? 57  CYS C O   1 
ATOM   2639 C  CB  . CYS C 1 57  ? 11.495  -59.711 24.221 1.00 93.18  ? 57  CYS C CB  1 
ATOM   2640 S  SG  . CYS C 1 57  ? 11.146  -61.411 24.846 1.00 95.52  ? 57  CYS C SG  1 
ATOM   2641 N  N   . THR C 1 58  ? 13.732  -57.234 23.564 1.00 96.68  ? 58  THR C N   1 
ATOM   2642 C  CA  . THR C 1 58  ? 13.973  -55.957 22.839 1.00 97.47  ? 58  THR C CA  1 
ATOM   2643 C  C   . THR C 1 58  ? 14.883  -56.113 21.623 1.00 97.09  ? 58  THR C C   1 
ATOM   2644 O  O   . THR C 1 58  ? 14.761  -55.361 20.665 1.00 97.09  ? 58  THR C O   1 
ATOM   2645 C  CB  . THR C 1 58  ? 14.619  -54.861 23.734 1.00 101.22 ? 58  THR C CB  1 
ATOM   2646 O  OG1 . THR C 1 58  ? 14.503  -55.228 25.115 1.00 102.72 ? 58  THR C OG1 1 
ATOM   2647 C  CG2 . THR C 1 58  ? 13.967  -53.490 23.492 1.00 101.49 ? 58  THR C CG2 1 
ATOM   2648 N  N   . SER C 1 59  ? 15.791  -57.086 21.679 1.00 97.14  ? 59  SER C N   1 
ATOM   2649 C  CA  . SER C 1 59  ? 16.706  -57.390 20.571 1.00 97.15  ? 59  SER C CA  1 
ATOM   2650 C  C   . SER C 1 59  ? 15.997  -57.806 19.261 1.00 94.40  ? 59  SER C C   1 
ATOM   2651 O  O   . SER C 1 59  ? 16.540  -57.616 18.161 1.00 94.99  ? 59  SER C O   1 
ATOM   2652 C  CB  . SER C 1 59  ? 17.666  -58.495 21.012 1.00 97.93  ? 59  SER C CB  1 
ATOM   2653 O  OG  . SER C 1 59  ? 18.203  -58.181 22.287 1.00 101.24 ? 59  SER C OG  1 
ATOM   2654 N  N   . ALA C 1 60  ? 14.796  -58.369 19.394 1.00 91.90  ? 60  ALA C N   1 
ATOM   2655 C  CA  . ALA C 1 60  ? 13.991  -58.839 18.263 1.00 89.85  ? 60  ALA C CA  1 
ATOM   2656 C  C   . ALA C 1 60  ? 13.749  -57.763 17.225 1.00 90.55  ? 60  ALA C C   1 
ATOM   2657 O  O   . ALA C 1 60  ? 13.557  -58.055 16.036 1.00 89.87  ? 60  ALA C O   1 
ATOM   2658 C  CB  . ALA C 1 60  ? 12.664  -59.336 18.760 1.00 88.04  ? 60  ALA C CB  1 
ATOM   2659 N  N   . GLY C 1 61  ? 13.717  -56.517 17.699 1.00 92.24  ? 61  GLY C N   1 
ATOM   2660 C  CA  . GLY C 1 61  ? 13.540  -55.349 16.843 1.00 93.71  ? 61  GLY C CA  1 
ATOM   2661 C  C   . GLY C 1 61  ? 12.078  -55.102 16.532 1.00 92.36  ? 61  GLY C C   1 
ATOM   2662 O  O   . GLY C 1 61  ? 11.197  -55.605 17.226 1.00 90.76  ? 61  GLY C O   1 
ATOM   2663 N  N   . PRO C 1 62  ? 11.805  -54.353 15.460 1.00 93.60  ? 62  PRO C N   1 
ATOM   2664 C  CA  . PRO C 1 62  ? 10.434  -53.986 15.137 1.00 92.80  ? 62  PRO C CA  1 
ATOM   2665 C  C   . PRO C 1 62  ? 9.704   -55.129 14.486 1.00 90.80  ? 62  PRO C C   1 
ATOM   2666 O  O   . PRO C 1 62  ? 10.283  -56.163 14.188 1.00 90.02  ? 62  PRO C O   1 
ATOM   2667 C  CB  . PRO C 1 62  ? 10.629  -52.901 14.098 1.00 95.61  ? 62  PRO C CB  1 
ATOM   2668 C  CG  . PRO C 1 62  ? 11.858  -53.400 13.310 1.00 96.69  ? 62  PRO C CG  1 
ATOM   2669 C  CD  . PRO C 1 62  ? 12.732  -54.071 14.340 1.00 95.86  ? 62  PRO C CD  1 
ATOM   2670 N  N   . HIS C 1 63  ? 8.442   -54.913 14.204 1.00 90.41  ? 63  HIS C N   1 
ATOM   2671 C  CA  . HIS C 1 63  ? 7.668   -55.921 13.540 1.00 89.44  ? 63  HIS C CA  1 
ATOM   2672 C  C   . HIS C 1 63  ? 8.285   -56.303 12.214 1.00 90.10  ? 63  HIS C C   1 
ATOM   2673 O  O   . HIS C 1 63  ? 8.817   -55.464 11.500 1.00 92.43  ? 63  HIS C O   1 
ATOM   2674 C  CB  . HIS C 1 63  ? 6.289   -55.381 13.262 1.00 90.25  ? 63  HIS C CB  1 
ATOM   2675 C  CG  . HIS C 1 63  ? 5.452   -55.220 14.483 1.00 90.94  ? 63  HIS C CG  1 
ATOM   2676 N  ND1 . HIS C 1 63  ? 4.103   -55.495 14.489 1.00 91.53  ? 63  HIS C ND1 1 
ATOM   2677 C  CD2 . HIS C 1 63  ? 5.767   -54.822 15.736 1.00 93.17  ? 63  HIS C CD2 1 
ATOM   2678 C  CE1 . HIS C 1 63  ? 3.620   -55.259 15.692 1.00 92.48  ? 63  HIS C CE1 1 
ATOM   2679 N  NE2 . HIS C 1 63  ? 4.609   -54.854 16.469 1.00 93.82  ? 63  HIS C NE2 1 
ATOM   2680 N  N   . PHE C 1 64  ? 8.158   -57.572 11.869 1.00 88.48  ? 64  PHE C N   1 
ATOM   2681 C  CA  . PHE C 1 64  ? 8.653   -58.057 10.603 1.00 89.83  ? 64  PHE C CA  1 
ATOM   2682 C  C   . PHE C 1 64  ? 7.894   -57.382 9.495  1.00 91.27  ? 64  PHE C C   1 
ATOM   2683 O  O   . PHE C 1 64  ? 6.717   -57.664 9.290  1.00 90.19  ? 64  PHE C O   1 
ATOM   2684 C  CB  . PHE C 1 64  ? 8.478   -59.578 10.482 1.00 88.91  ? 64  PHE C CB  1 
ATOM   2685 C  CG  . PHE C 1 64  ? 9.048   -60.178 9.198  1.00 91.70  ? 64  PHE C CG  1 
ATOM   2686 C  CD1 . PHE C 1 64  ? 10.249  -59.729 8.659  1.00 94.76  ? 64  PHE C CD1 1 
ATOM   2687 C  CD2 . PHE C 1 64  ? 8.398   -61.232 8.571  1.00 92.61  ? 64  PHE C CD2 1 
ATOM   2688 C  CE1 . PHE C 1 64  ? 10.759  -60.292 7.517  1.00 97.06  ? 64  PHE C CE1 1 
ATOM   2689 C  CE2 . PHE C 1 64  ? 8.917   -61.820 7.421  1.00 95.55  ? 64  PHE C CE2 1 
ATOM   2690 C  CZ  . PHE C 1 64  ? 10.095  -61.344 6.892  1.00 97.56  ? 64  PHE C CZ  1 
ATOM   2691 N  N   . ASN C 1 65  ? 8.603   -56.524 8.766  1.00 93.88  ? 65  ASN C N   1 
ATOM   2692 C  CA  . ASN C 1 65  ? 7.977   -55.681 7.773  1.00 96.65  ? 65  ASN C CA  1 
ATOM   2693 C  C   . ASN C 1 65  ? 8.828   -55.485 6.513  1.00 100.46 ? 65  ASN C C   1 
ATOM   2694 O  O   . ASN C 1 65  ? 9.397   -54.417 6.289  1.00 102.83 ? 65  ASN C O   1 
ATOM   2695 C  CB  . ASN C 1 65  ? 7.615   -54.335 8.403  1.00 96.90  ? 65  ASN C CB  1 
ATOM   2696 C  CG  . ASN C 1 65  ? 6.809   -53.446 7.455  1.00 99.04  ? 65  ASN C CG  1 
ATOM   2697 O  OD1 . ASN C 1 65  ? 6.217   -53.935 6.467  1.00 100.18 ? 65  ASN C OD1 1 
ATOM   2698 N  ND2 . ASN C 1 65  ? 6.762   -52.150 7.756  1.00 98.49  ? 65  ASN C ND2 1 
ATOM   2699 N  N   . PRO C 1 66  ? 8.860   -56.514 5.658  1.00 101.68 ? 66  PRO C N   1 
ATOM   2700 C  CA  . PRO C 1 66  ? 9.752   -56.506 4.513  1.00 105.64 ? 66  PRO C CA  1 
ATOM   2701 C  C   . PRO C 1 66  ? 9.237   -55.646 3.362  1.00 110.14 ? 66  PRO C C   1 
ATOM   2702 O  O   . PRO C 1 66  ? 10.044  -55.172 2.576  1.00 114.22 ? 66  PRO C O   1 
ATOM   2703 C  CB  . PRO C 1 66  ? 9.816   -57.994 4.109  1.00 105.12 ? 66  PRO C CB  1 
ATOM   2704 C  CG  . PRO C 1 66  ? 8.467   -58.529 4.438  1.00 102.91 ? 66  PRO C CG  1 
ATOM   2705 C  CD  . PRO C 1 66  ? 7.954   -57.685 5.634  1.00 100.05 ? 66  PRO C CD  1 
ATOM   2706 N  N   . LEU C 1 67  ? 7.922   -55.439 3.259  1.00 110.14 ? 67  LEU C N   1 
ATOM   2707 C  CA  . LEU C 1 67  ? 7.356   -54.601 2.193  1.00 114.73 ? 67  LEU C CA  1 
ATOM   2708 C  C   . LEU C 1 67  ? 7.183   -53.130 2.628  1.00 115.63 ? 67  LEU C C   1 
ATOM   2709 O  O   . LEU C 1 67  ? 6.546   -52.346 1.924  1.00 119.04 ? 67  LEU C O   1 
ATOM   2710 C  CB  . LEU C 1 67  ? 5.994   -55.151 1.736  1.00 115.12 ? 67  LEU C CB  1 
ATOM   2711 C  CG  . LEU C 1 67  ? 5.752   -56.668 1.519  1.00 114.38 ? 67  LEU C CG  1 
ATOM   2712 C  CD1 . LEU C 1 67  ? 4.251   -57.029 1.961  1.00 112.37 ? 67  LEU C CD1 1 
ATOM   2713 C  CD2 . LEU C 1 67  ? 6.084   -57.182 0.099  1.00 117.91 ? 67  LEU C CD2 1 
ATOM   2714 N  N   . SER C 1 68  ? 7.728   -52.772 3.798  1.00 113.15 ? 68  SER C N   1 
ATOM   2715 C  CA  . SER C 1 68  ? 7.676   -51.383 4.357  1.00 114.11 ? 68  SER C CA  1 
ATOM   2716 C  C   . SER C 1 68  ? 6.274   -50.733 4.483  1.00 114.42 ? 68  SER C C   1 
ATOM   2717 O  O   . SER C 1 68  ? 6.124   -49.521 4.251  1.00 117.28 ? 68  SER C O   1 
ATOM   2718 C  CB  . SER C 1 68  ? 8.607   -50.449 3.567  1.00 119.10 ? 68  SER C CB  1 
ATOM   2719 O  OG  . SER C 1 68  ? 9.961   -50.645 3.941  1.00 118.85 ? 68  SER C OG  1 
ATOM   2720 N  N   . ARG C 1 69  ? 5.277   -51.536 4.886  1.00 111.88 ? 69  ARG C N   1 
ATOM   2721 C  CA  . ARG C 1 69  ? 3.894   -51.064 5.076  1.00 112.31 ? 69  ARG C CA  1 
ATOM   2722 C  C   . ARG C 1 69  ? 3.710   -50.462 6.488  1.00 109.59 ? 69  ARG C C   1 
ATOM   2723 O  O   . ARG C 1 69  ? 4.629   -50.501 7.345  1.00 107.66 ? 69  ARG C O   1 
ATOM   2724 C  CB  . ARG C 1 69  ? 2.890   -52.206 4.876  1.00 110.96 ? 69  ARG C CB  1 
ATOM   2725 C  CG  . ARG C 1 69  ? 3.039   -52.950 3.580  1.00 115.43 ? 69  ARG C CG  1 
ATOM   2726 C  CD  . ARG C 1 69  ? 2.480   -52.170 2.432  1.00 123.14 ? 69  ARG C CD  1 
ATOM   2727 N  NE  . ARG C 1 69  ? 2.589   -52.950 1.198  1.00 129.02 ? 69  ARG C NE  1 
ATOM   2728 C  CZ  . ARG C 1 69  ? 1.771   -53.954 0.843  1.00 130.44 ? 69  ARG C CZ  1 
ATOM   2729 N  NH1 . ARG C 1 69  ? 0.743   -54.306 1.621  1.00 127.97 ? 69  ARG C NH1 1 
ATOM   2730 N  NH2 . ARG C 1 69  ? 1.975   -54.610 -0.312 1.00 134.30 ? 69  ARG C NH2 1 
ATOM   2731 N  N   . LYS C 1 70  ? 2.521   -49.893 6.711  1.00 109.87 ? 70  LYS C N   1 
ATOM   2732 C  CA  . LYS C 1 70  ? 2.108   -49.424 8.042  1.00 107.46 ? 70  LYS C CA  1 
ATOM   2733 C  C   . LYS C 1 70  ? 1.486   -50.618 8.783  1.00 102.85 ? 70  LYS C C   1 
ATOM   2734 O  O   . LYS C 1 70  ? 0.973   -51.571 8.148  1.00 102.05 ? 70  LYS C O   1 
ATOM   2735 C  CB  . LYS C 1 70  ? 1.090   -48.266 7.958  1.00 110.43 ? 70  LYS C CB  1 
ATOM   2736 C  CG  . LYS C 1 70  ? 1.366   -47.169 6.891  1.00 117.04 ? 70  LYS C CG  1 
ATOM   2737 C  CD  . LYS C 1 70  ? 1.854   -45.814 7.462  1.00 121.03 ? 70  LYS C CD  1 
ATOM   2738 C  CE  . LYS C 1 70  ? 1.192   -44.659 6.651  1.00 127.27 ? 70  LYS C CE  1 
ATOM   2739 N  NZ  . LYS C 1 70  ? 1.799   -43.314 6.865  1.00 131.61 ? 70  LYS C NZ  1 
ATOM   2740 N  N   . HIS C 1 71  ? 1.531   -50.559 10.117 1.00 99.81  ? 71  HIS C N   1 
ATOM   2741 C  CA  . HIS C 1 71  ? 1.013   -51.645 10.955 1.00 96.16  ? 71  HIS C CA  1 
ATOM   2742 C  C   . HIS C 1 71  ? -0.477  -51.815 10.735 1.00 96.36  ? 71  HIS C C   1 
ATOM   2743 O  O   . HIS C 1 71  ? -1.178  -50.847 10.480 1.00 98.59  ? 71  HIS C O   1 
ATOM   2744 C  CB  . HIS C 1 71  ? 1.309   -51.377 12.440 1.00 94.40  ? 71  HIS C CB  1 
ATOM   2745 C  CG  . HIS C 1 71  ? 0.729   -52.400 13.375 1.00 91.32  ? 71  HIS C CG  1 
ATOM   2746 N  ND1 . HIS C 1 71  ? 1.257   -53.663 13.526 1.00 89.16  ? 71  HIS C ND1 1 
ATOM   2747 C  CD2 . HIS C 1 71  ? -0.337  -52.341 14.206 1.00 90.13  ? 71  HIS C CD2 1 
ATOM   2748 C  CE1 . HIS C 1 71  ? 0.531   -54.342 14.396 1.00 87.28  ? 71  HIS C CE1 1 
ATOM   2749 N  NE2 . HIS C 1 71  ? -0.439  -53.559 14.827 1.00 87.74  ? 71  HIS C NE2 1 
ATOM   2750 N  N   . GLY C 1 72  ? -0.957  -53.047 10.821 1.00 94.58  ? 72  GLY C N   1 
ATOM   2751 C  CA  . GLY C 1 72  ? -2.387  -53.305 10.743 1.00 95.33  ? 72  GLY C CA  1 
ATOM   2752 C  C   . GLY C 1 72  ? -2.816  -54.587 11.445 1.00 93.43  ? 72  GLY C C   1 
ATOM   2753 O  O   . GLY C 1 72  ? -2.037  -55.246 12.151 1.00 91.71  ? 72  GLY C O   1 
ATOM   2754 N  N   . GLY C 1 73  ? -4.082  -54.933 11.258 1.00 94.60  ? 73  GLY C N   1 
ATOM   2755 C  CA  . GLY C 1 73  ? -4.619  -56.206 11.723 1.00 93.49  ? 73  GLY C CA  1 
ATOM   2756 C  C   . GLY C 1 73  ? -4.328  -57.274 10.685 1.00 94.26  ? 73  GLY C C   1 
ATOM   2757 O  O   . GLY C 1 73  ? -3.986  -56.962 9.545  1.00 96.13  ? 73  GLY C O   1 
ATOM   2758 N  N   . PRO C 1 74  ? -4.485  -58.549 11.057 1.00 93.63  ? 74  PRO C N   1 
ATOM   2759 C  CA  . PRO C 1 74  ? -4.001  -59.599 10.160 1.00 94.23  ? 74  PRO C CA  1 
ATOM   2760 C  C   . PRO C 1 74  ? -4.862  -59.701 8.921  1.00 97.58  ? 74  PRO C C   1 
ATOM   2761 O  O   . PRO C 1 74  ? -4.350  -59.998 7.863  1.00 99.10  ? 74  PRO C O   1 
ATOM   2762 C  CB  . PRO C 1 74  ? -4.103  -60.867 11.002 1.00 92.70  ? 74  PRO C CB  1 
ATOM   2763 C  CG  . PRO C 1 74  ? -5.261  -60.595 11.926 1.00 93.31  ? 74  PRO C CG  1 
ATOM   2764 C  CD  . PRO C 1 74  ? -5.385  -59.076 12.099 1.00 93.20  ? 74  PRO C CD  1 
ATOM   2765 N  N   . LYS C 1 75  ? -6.155  -59.432 9.044  1.00 99.48  ? 75  LYS C N   1 
ATOM   2766 C  CA  . LYS C 1 75  ? -7.048  -59.501 7.897  1.00 103.71 ? 75  LYS C CA  1 
ATOM   2767 C  C   . LYS C 1 75  ? -7.100  -58.161 7.128  1.00 105.63 ? 75  LYS C C   1 
ATOM   2768 O  O   . LYS C 1 75  ? -7.619  -58.087 6.004  1.00 109.00 ? 75  LYS C O   1 
ATOM   2769 C  CB  . LYS C 1 75  ? -8.430  -59.929 8.370  1.00 105.27 ? 75  LYS C CB  1 
ATOM   2770 C  CG  . LYS C 1 75  ? -8.483  -61.365 8.994  1.00 107.03 ? 75  LYS C CG  1 
ATOM   2771 C  CD  . LYS C 1 75  ? -9.949  -61.893 9.154  1.00 113.07 ? 75  LYS C CD  1 
ATOM   2772 C  CE  . LYS C 1 75  ? -10.958 -60.736 9.582  1.00 115.81 ? 75  LYS C CE  1 
ATOM   2773 N  NZ  . LYS C 1 75  ? -12.416 -61.083 9.757  1.00 118.93 ? 75  LYS C NZ  1 
ATOM   2774 N  N   . ASP C 1 76  ? -6.535  -57.112 7.727  1.00 103.91 ? 76  ASP C N   1 
ATOM   2775 C  CA  . ASP C 1 76  ? -6.386  -55.832 7.033  1.00 106.20 ? 76  ASP C CA  1 
ATOM   2776 C  C   . ASP C 1 76  ? -5.505  -56.035 5.818  1.00 108.15 ? 76  ASP C C   1 
ATOM   2777 O  O   . ASP C 1 76  ? -4.771  -57.016 5.718  1.00 106.68 ? 76  ASP C O   1 
ATOM   2778 C  CB  . ASP C 1 76  ? -5.816  -54.720 7.956  1.00 104.36 ? 76  ASP C CB  1 
ATOM   2779 C  CG  . ASP C 1 76  ? -6.913  -54.036 8.794  1.00 105.29 ? 76  ASP C CG  1 
ATOM   2780 O  OD1 . ASP C 1 76  ? -7.960  -53.671 8.211  1.00 109.64 ? 76  ASP C OD1 1 
ATOM   2781 O  OD2 . ASP C 1 76  ? -6.753  -53.861 10.026 1.00 103.58 ? 76  ASP C OD2 1 
ATOM   2782 N  N   . GLU C 1 77  ? -5.604  -55.113 4.881  1.00 112.00 ? 77  GLU C N   1 
ATOM   2783 C  CA  . GLU C 1 77  ? -4.818  -55.210 3.675  1.00 115.24 ? 77  GLU C CA  1 
ATOM   2784 C  C   . GLU C 1 77  ? -3.493  -54.505 3.872  1.00 113.47 ? 77  GLU C C   1 
ATOM   2785 O  O   . GLU C 1 77  ? -2.458  -55.106 3.617  1.00 112.71 ? 77  GLU C O   1 
ATOM   2786 C  CB  . GLU C 1 77  ? -5.566  -54.621 2.492  1.00 121.28 ? 77  GLU C CB  1 
ATOM   2787 C  CG  . GLU C 1 77  ? -4.880  -54.934 1.138  1.00 127.96 ? 77  GLU C CG  1 
ATOM   2788 C  CD  . GLU C 1 77  ? -4.750  -53.707 0.238  1.00 137.42 ? 77  GLU C CD  1 
ATOM   2789 O  OE1 . GLU C 1 77  ? -5.806  -53.262 -0.303 1.00 142.75 ? 77  GLU C OE1 1 
ATOM   2790 O  OE2 . GLU C 1 77  ? -3.596  -53.198 0.087  1.00 140.65 ? 77  GLU C OE2 1 
ATOM   2791 N  N   . GLU C 1 78  ? -3.529  -53.239 4.304  1.00 113.11 ? 78  GLU C N   1 
ATOM   2792 C  CA  . GLU C 1 78  ? -2.313  -52.546 4.758  1.00 111.64 ? 78  GLU C CA  1 
ATOM   2793 C  C   . GLU C 1 78  ? -1.878  -53.097 6.170  1.00 106.10 ? 78  GLU C C   1 
ATOM   2794 O  O   . GLU C 1 78  ? -2.475  -52.744 7.231  1.00 103.99 ? 78  GLU C O   1 
ATOM   2795 C  CB  . GLU C 1 78  ? -2.504  -51.009 4.767  1.00 114.19 ? 78  GLU C CB  1 
ATOM   2796 C  CG  . GLU C 1 78  ? -1.214  -50.175 5.126  1.00 115.19 ? 78  GLU C CG  1 
ATOM   2797 C  CD  . GLU C 1 78  ? -0.183  -50.002 3.954  1.00 120.92 ? 78  GLU C CD  1 
ATOM   2798 O  OE1 . GLU C 1 78  ? -0.214  -50.829 2.981  1.00 124.43 ? 78  GLU C OE1 1 
ATOM   2799 O  OE2 . GLU C 1 78  ? 0.676   -49.055 4.027  1.00 122.43 ? 78  GLU C OE2 1 
ATOM   2800 N  N   . ARG C 1 79  ? -0.852  -53.971 6.150  1.00 103.60 ? 79  ARG C N   1 
ATOM   2801 C  CA  . ARG C 1 79  ? -0.300  -54.606 7.349  1.00 98.91  ? 79  ARG C CA  1 
ATOM   2802 C  C   . ARG C 1 79  ? 1.177   -55.016 7.204  1.00 97.83  ? 79  ARG C C   1 
ATOM   2803 O  O   . ARG C 1 79  ? 1.714   -55.196 6.099  1.00 100.33 ? 79  ARG C O   1 
ATOM   2804 C  CB  . ARG C 1 79  ? -1.099  -55.862 7.673  1.00 97.13  ? 79  ARG C CB  1 
ATOM   2805 C  CG  . ARG C 1 79  ? -0.947  -56.966 6.617  1.00 99.16  ? 79  ARG C CG  1 
ATOM   2806 C  CD  . ARG C 1 79  ? -1.528  -58.305 7.062  1.00 98.42  ? 79  ARG C CD  1 
ATOM   2807 N  NE  . ARG C 1 79  ? -0.586  -59.129 7.845  1.00 96.22  ? 79  ARG C NE  1 
ATOM   2808 C  CZ  . ARG C 1 79  ? -0.718  -60.444 8.078  1.00 95.35  ? 79  ARG C CZ  1 
ATOM   2809 N  NH1 . ARG C 1 79  ? -1.741  -61.133 7.576  1.00 96.47  ? 79  ARG C NH1 1 
ATOM   2810 N  NH2 . ARG C 1 79  ? 0.187   -61.088 8.816  1.00 93.70  ? 79  ARG C NH2 1 
ATOM   2811 N  N   . HIS C 1 80  ? 1.820   -55.215 8.344  1.00 94.17  ? 80  HIS C N   1 
ATOM   2812 C  CA  . HIS C 1 80  ? 3.130   -55.816 8.351  1.00 92.59  ? 80  HIS C CA  1 
ATOM   2813 C  C   . HIS C 1 80  ? 2.935   -57.306 8.140  1.00 90.91  ? 80  HIS C C   1 
ATOM   2814 O  O   . HIS C 1 80  ? 1.970   -57.893 8.642  1.00 89.22  ? 80  HIS C O   1 
ATOM   2815 C  CB  . HIS C 1 80  ? 3.839   -55.585 9.682  1.00 90.21  ? 80  HIS C CB  1 
ATOM   2816 C  CG  . HIS C 1 80  ? 4.091   -54.150 9.996  1.00 91.54  ? 80  HIS C CG  1 
ATOM   2817 N  ND1 . HIS C 1 80  ? 4.355   -53.701 11.271 1.00 90.85  ? 80  HIS C ND1 1 
ATOM   2818 C  CD2 . HIS C 1 80  ? 4.124   -53.058 9.199  1.00 95.33  ? 80  HIS C CD2 1 
ATOM   2819 C  CE1 . HIS C 1 80  ? 4.551   -52.394 11.248 1.00 93.77  ? 80  HIS C CE1 1 
ATOM   2820 N  NE2 . HIS C 1 80  ? 4.415   -51.977 10.001 1.00 96.45  ? 80  HIS C NE2 1 
ATOM   2821 N  N   . VAL C 1 81  ? 3.858   -57.921 7.408  1.00 91.36  ? 81  VAL C N   1 
ATOM   2822 C  CA  . VAL C 1 81  ? 3.872   -59.395 7.278  1.00 89.95  ? 81  VAL C CA  1 
ATOM   2823 C  C   . VAL C 1 81  ? 3.782   -60.087 8.641  1.00 85.95  ? 81  VAL C C   1 
ATOM   2824 O  O   . VAL C 1 81  ? 3.152   -61.121 8.777  1.00 84.95  ? 81  VAL C O   1 
ATOM   2825 C  CB  . VAL C 1 81  ? 5.115   -59.933 6.491  1.00 91.50  ? 81  VAL C CB  1 
ATOM   2826 C  CG1 . VAL C 1 81  ? 5.069   -61.477 6.371  1.00 89.91  ? 81  VAL C CG1 1 
ATOM   2827 C  CG2 . VAL C 1 81  ? 5.177   -59.320 5.094  1.00 95.98  ? 81  VAL C CG2 1 
ATOM   2828 N  N   . GLY C 1 82  ? 4.393   -59.499 9.652  1.00 84.02  ? 82  GLY C N   1 
ATOM   2829 C  CA  . GLY C 1 82  ? 4.380   -60.104 10.970 1.00 81.69  ? 82  GLY C CA  1 
ATOM   2830 C  C   . GLY C 1 82  ? 3.179   -59.825 11.869 1.00 80.67  ? 82  GLY C C   1 
ATOM   2831 O  O   . GLY C 1 82  ? 3.177   -60.227 13.033 1.00 78.75  ? 82  GLY C O   1 
ATOM   2832 N  N   . ASP C 1 83  ? 2.154   -59.150 11.352 1.00 82.17  ? 83  ASP C N   1 
ATOM   2833 C  CA  . ASP C 1 83  ? 1.032   -58.719 12.201 1.00 81.85  ? 83  ASP C CA  1 
ATOM   2834 C  C   . ASP C 1 83  ? -0.001  -59.813 12.247 1.00 81.80  ? 83  ASP C C   1 
ATOM   2835 O  O   . ASP C 1 83  ? -0.822  -59.922 11.331 1.00 83.75  ? 83  ASP C O   1 
ATOM   2836 C  CB  . ASP C 1 83  ? 0.357   -57.431 11.682 1.00 83.52  ? 83  ASP C CB  1 
ATOM   2837 C  CG  . ASP C 1 83  ? 1.272   -56.215 11.717 1.00 84.56  ? 83  ASP C CG  1 
ATOM   2838 O  OD1 . ASP C 1 83  ? 2.174   -56.136 12.583 1.00 83.36  ? 83  ASP C OD1 1 
ATOM   2839 O  OD2 . ASP C 1 83  ? 1.089   -55.315 10.871 1.00 87.04  ? 83  ASP C OD2 1 
ATOM   2840 N  N   . LEU C 1 84  ? 0.013   -60.621 13.303 1.00 80.48  ? 84  LEU C N   1 
ATOM   2841 C  CA  . LEU C 1 84  ? -1.023  -61.655 13.451 1.00 80.89  ? 84  LEU C CA  1 
ATOM   2842 C  C   . LEU C 1 84  ? -2.193  -61.219 14.366 1.00 81.03  ? 84  LEU C C   1 
ATOM   2843 O  O   . LEU C 1 84  ? -3.015  -62.025 14.814 1.00 81.10  ? 84  LEU C O   1 
ATOM   2844 C  CB  . LEU C 1 84  ? -0.362  -62.950 13.907 1.00 80.13  ? 84  LEU C CB  1 
ATOM   2845 C  CG  . LEU C 1 84  ? 0.719   -63.467 12.933 1.00 80.05  ? 84  LEU C CG  1 
ATOM   2846 C  CD1 . LEU C 1 84  ? 1.293   -64.749 13.468 1.00 78.18  ? 84  LEU C CD1 1 
ATOM   2847 C  CD2 . LEU C 1 84  ? 0.231   -63.683 11.506 1.00 81.56  ? 84  LEU C CD2 1 
ATOM   2848 N  N   . GLY C 1 85  ? -2.278  -59.919 14.599 1.00 81.42  ? 85  GLY C N   1 
ATOM   2849 C  CA  . GLY C 1 85  ? -3.287  -59.389 15.466 1.00 81.98  ? 85  GLY C CA  1 
ATOM   2850 C  C   . GLY C 1 85  ? -3.175  -59.928 16.876 1.00 81.21  ? 85  GLY C C   1 
ATOM   2851 O  O   . GLY C 1 85  ? -2.103  -59.904 17.489 1.00 80.27  ? 85  GLY C O   1 
ATOM   2852 N  N   . ASN C 1 86  ? -4.286  -60.426 17.395 1.00 82.03  ? 86  ASN C N   1 
ATOM   2853 C  CA  . ASN C 1 86  ? -4.364  -60.736 18.807 1.00 82.37  ? 86  ASN C CA  1 
ATOM   2854 C  C   . ASN C 1 86  ? -4.638  -62.200 19.095 1.00 82.73  ? 86  ASN C C   1 
ATOM   2855 O  O   . ASN C 1 86  ? -5.106  -62.972 18.227 1.00 83.06  ? 86  ASN C O   1 
ATOM   2856 C  CB  . ASN C 1 86  ? -5.469  -59.916 19.467 1.00 84.06  ? 86  ASN C CB  1 
ATOM   2857 C  CG  . ASN C 1 86  ? -5.136  -58.472 19.546 1.00 84.63  ? 86  ASN C CG  1 
ATOM   2858 O  OD1 . ASN C 1 86  ? -4.310  -58.050 20.360 1.00 86.33  ? 86  ASN C OD1 1 
ATOM   2859 N  ND2 . ASN C 1 86  ? -5.793  -57.685 18.708 1.00 86.54  ? 86  ASN C ND2 1 
ATOM   2860 N  N   . VAL C 1 87  ? -4.349  -62.536 20.355 1.00 82.95  ? 87  VAL C N   1 
ATOM   2861 C  CA  . VAL C 1 87  ? -4.738  -63.796 20.964 1.00 84.22  ? 87  VAL C CA  1 
ATOM   2862 C  C   . VAL C 1 87  ? -5.478  -63.492 22.286 1.00 86.68  ? 87  VAL C C   1 
ATOM   2863 O  O   . VAL C 1 87  ? -5.305  -62.408 22.904 1.00 86.57  ? 87  VAL C O   1 
ATOM   2864 C  CB  . VAL C 1 87  ? -3.518  -64.671 21.231 1.00 83.22  ? 87  VAL C CB  1 
ATOM   2865 C  CG1 . VAL C 1 87  ? -2.673  -64.771 19.971 1.00 80.42  ? 87  VAL C CG1 1 
ATOM   2866 C  CG2 . VAL C 1 87  ? -2.706  -64.105 22.344 1.00 82.75  ? 87  VAL C CG2 1 
ATOM   2867 N  N   . THR C 1 88  ? -6.295  -64.450 22.714 1.00 89.30  ? 88  THR C N   1 
ATOM   2868 C  CA  . THR C 1 88  ? -7.230  -64.201 23.789 1.00 92.34  ? 88  THR C CA  1 
ATOM   2869 C  C   . THR C 1 88  ? -6.971  -65.102 25.000 1.00 94.69  ? 88  THR C C   1 
ATOM   2870 O  O   . THR C 1 88  ? -6.915  -66.332 24.877 1.00 95.54  ? 88  THR C O   1 
ATOM   2871 C  CB  . THR C 1 88  ? -8.666  -64.383 23.262 1.00 94.27  ? 88  THR C CB  1 
ATOM   2872 O  OG1 . THR C 1 88  ? -8.946  -63.378 22.263 1.00 93.00  ? 88  THR C OG1 1 
ATOM   2873 C  CG2 . THR C 1 88  ? -9.699  -64.321 24.441 1.00 98.34  ? 88  THR C CG2 1 
ATOM   2874 N  N   . ALA C 1 89  ? -6.836  -64.473 26.166 1.00 96.41  ? 89  ALA C N   1 
ATOM   2875 C  CA  . ALA C 1 89  ? -6.557  -65.185 27.398 1.00 99.61  ? 89  ALA C CA  1 
ATOM   2876 C  C   . ALA C 1 89  ? -7.856  -65.456 28.149 1.00 104.33 ? 89  ALA C C   1 
ATOM   2877 O  O   . ALA C 1 89  ? -8.709  -64.565 28.283 1.00 105.27 ? 89  ALA C O   1 
ATOM   2878 C  CB  . ALA C 1 89  ? -5.616  -64.389 28.277 1.00 99.56  ? 89  ALA C CB  1 
ATOM   2879 N  N   . ASP C 1 90  ? -7.995  -66.709 28.594 1.00 107.93 ? 90  ASP C N   1 
ATOM   2880 C  CA  . ASP C 1 90  ? -8.904  -67.149 29.679 1.00 113.68 ? 90  ASP C CA  1 
ATOM   2881 C  C   . ASP C 1 90  ? -9.143  -66.156 30.811 1.00 116.70 ? 90  ASP C C   1 
ATOM   2882 O  O   . ASP C 1 90  ? -8.432  -65.143 30.956 1.00 114.82 ? 90  ASP C O   1 
ATOM   2883 C  CB  . ASP C 1 90  ? -8.257  -68.360 30.393 1.00 116.48 ? 90  ASP C CB  1 
ATOM   2884 C  CG  . ASP C 1 90  ? -8.842  -69.704 29.980 1.00 120.10 ? 90  ASP C CG  1 
ATOM   2885 O  OD1 . ASP C 1 90  ? -9.639  -69.733 28.993 1.00 121.32 ? 90  ASP C OD1 1 
ATOM   2886 O  OD2 . ASP C 1 90  ? -8.491  -70.727 30.662 1.00 124.91 ? 90  ASP C OD2 1 
ATOM   2887 N  N   . LYS C 1 91  ? -10.123 -66.513 31.643 1.00 122.19 ? 91  LYS C N   1 
ATOM   2888 C  CA  . LYS C 1 91  ? -10.148 -66.112 33.078 1.00 127.26 ? 91  LYS C CA  1 
ATOM   2889 C  C   . LYS C 1 91  ? -8.799  -66.451 33.786 1.00 127.48 ? 91  LYS C C   1 
ATOM   2890 O  O   . LYS C 1 91  ? -8.174  -65.635 34.520 1.00 128.02 ? 91  LYS C O   1 
ATOM   2891 C  CB  . LYS C 1 91  ? -11.265 -66.909 33.810 1.00 133.57 ? 91  LYS C CB  1 
ATOM   2892 C  CG  . LYS C 1 91  ? -12.602 -66.195 34.016 1.00 137.92 ? 91  LYS C CG  1 
ATOM   2893 C  CD  . LYS C 1 91  ? -12.574 -65.327 35.305 1.00 144.27 ? 91  LYS C CD  1 
ATOM   2894 C  CE  . LYS C 1 91  ? -13.987 -65.179 35.905 1.00 150.77 ? 91  LYS C CE  1 
ATOM   2895 N  NZ  . LYS C 1 91  ? -14.210 -63.780 36.392 1.00 152.78 ? 91  LYS C NZ  1 
ATOM   2896 N  N   . ASP C 1 92  ? -8.415  -67.710 33.556 1.00 127.31 ? 92  ASP C N   1 
ATOM   2897 C  CA  . ASP C 1 92  ? -7.228  -68.346 34.110 1.00 128.31 ? 92  ASP C CA  1 
ATOM   2898 C  C   . ASP C 1 92  ? -5.907  -67.890 33.491 1.00 123.19 ? 92  ASP C C   1 
ATOM   2899 O  O   . ASP C 1 92  ? -4.845  -68.396 33.880 1.00 123.84 ? 92  ASP C O   1 
ATOM   2900 C  CB  . ASP C 1 92  ? -7.357  -69.875 33.912 1.00 130.31 ? 92  ASP C CB  1 
ATOM   2901 C  CG  . ASP C 1 92  ? -8.613  -70.473 34.606 1.00 137.39 ? 92  ASP C CG  1 
ATOM   2902 O  OD1 . ASP C 1 92  ? -8.617  -71.721 34.797 1.00 142.23 ? 92  ASP C OD1 1 
ATOM   2903 O  OD2 . ASP C 1 92  ? -9.576  -69.720 34.974 1.00 141.07 ? 92  ASP C OD2 1 
ATOM   2904 N  N   . GLY C 1 93  ? -5.967  -66.980 32.512 1.00 118.43 ? 93  GLY C N   1 
ATOM   2905 C  CA  . GLY C 1 93  ? -4.760  -66.488 31.835 1.00 113.89 ? 93  GLY C CA  1 
ATOM   2906 C  C   . GLY C 1 93  ? -4.103  -67.431 30.824 1.00 110.74 ? 93  GLY C C   1 
ATOM   2907 O  O   . GLY C 1 93  ? -2.960  -67.193 30.396 1.00 107.94 ? 93  GLY C O   1 
ATOM   2908 N  N   . VAL C 1 94  ? -4.795  -68.518 30.470 1.00 111.59 ? 94  VAL C N   1 
ATOM   2909 C  CA  . VAL C 1 94  ? -4.376  -69.375 29.361 1.00 109.10 ? 94  VAL C CA  1 
ATOM   2910 C  C   . VAL C 1 94  ? -5.014  -68.900 28.050 1.00 106.12 ? 94  VAL C C   1 
ATOM   2911 O  O   . VAL C 1 94  ? -6.242  -68.751 27.986 1.00 107.75 ? 94  VAL C O   1 
ATOM   2912 C  CB  . VAL C 1 94  ? -4.806  -70.851 29.579 1.00 112.58 ? 94  VAL C CB  1 
ATOM   2913 C  CG1 . VAL C 1 94  ? -4.549  -71.708 28.285 1.00 109.51 ? 94  VAL C CG1 1 
ATOM   2914 C  CG2 . VAL C 1 94  ? -4.108  -71.442 30.835 1.00 116.44 ? 94  VAL C CG2 1 
ATOM   2915 N  N   . ALA C 1 95  ? -4.200  -68.693 27.008 1.00 102.49 ? 95  ALA C N   1 
ATOM   2916 C  CA  . ALA C 1 95  ? -4.726  -68.363 25.687 1.00 100.09 ? 95  ALA C CA  1 
ATOM   2917 C  C   . ALA C 1 95  ? -4.547  -69.556 24.773 1.00 100.13 ? 95  ALA C C   1 
ATOM   2918 O  O   . ALA C 1 95  ? -3.428  -70.035 24.609 1.00 99.12  ? 95  ALA C O   1 
ATOM   2919 C  CB  . ALA C 1 95  ? -4.021  -67.165 25.132 1.00 96.66  ? 95  ALA C CB  1 
ATOM   2920 N  N   . ASP C 1 96  ? -5.643  -70.046 24.197 1.00 101.98 ? 96  ASP C N   1 
ATOM   2921 C  CA  . ASP C 1 96  ? -5.573  -71.188 23.279 1.00 103.05 ? 96  ASP C CA  1 
ATOM   2922 C  C   . ASP C 1 96  ? -5.491  -70.697 21.864 1.00 99.84  ? 96  ASP C C   1 
ATOM   2923 O  O   . ASP C 1 96  ? -6.482  -70.445 21.223 1.00 100.89 ? 96  ASP C O   1 
ATOM   2924 C  CB  . ASP C 1 96  ? -6.786  -72.115 23.422 1.00 107.41 ? 96  ASP C CB  1 
ATOM   2925 C  CG  . ASP C 1 96  ? -6.624  -73.138 24.546 1.00 113.35 ? 96  ASP C CG  1 
ATOM   2926 O  OD1 . ASP C 1 96  ? -5.505  -73.734 24.659 1.00 114.81 ? 96  ASP C OD1 1 
ATOM   2927 O  OD2 . ASP C 1 96  ? -7.634  -73.355 25.295 1.00 119.52 ? 96  ASP C OD2 1 
ATOM   2928 N  N   . VAL C 1 97  ? -4.289  -70.568 21.369 1.00 96.68  ? 97  VAL C N   1 
ATOM   2929 C  CA  . VAL C 1 97  ? -4.101  -69.972 20.074 1.00 94.01  ? 97  VAL C CA  1 
ATOM   2930 C  C   . VAL C 1 97  ? -4.522  -70.893 18.934 1.00 94.77  ? 97  VAL C C   1 
ATOM   2931 O  O   . VAL C 1 97  ? -4.276  -72.089 18.966 1.00 96.41  ? 97  VAL C O   1 
ATOM   2932 C  CB  . VAL C 1 97  ? -2.637  -69.653 19.881 1.00 91.66  ? 97  VAL C CB  1 
ATOM   2933 C  CG1 . VAL C 1 97  ? -2.359  -69.314 18.443 1.00 90.65  ? 97  VAL C CG1 1 
ATOM   2934 C  CG2 . VAL C 1 97  ? -2.244  -68.525 20.795 1.00 90.86  ? 97  VAL C CG2 1 
ATOM   2935 N  N   . SER C 1 98  ? -5.129  -70.314 17.911 1.00 93.80  ? 98  SER C N   1 
ATOM   2936 C  CA  . SER C 1 98  ? -5.404  -71.036 16.682 1.00 94.84  ? 98  SER C CA  1 
ATOM   2937 C  C   . SER C 1 98  ? -5.784  -70.092 15.532 1.00 93.97  ? 98  SER C C   1 
ATOM   2938 O  O   . SER C 1 98  ? -6.773  -69.395 15.589 1.00 94.27  ? 98  SER C O   1 
ATOM   2939 C  CB  . SER C 1 98  ? -6.505  -72.036 16.900 1.00 98.29  ? 98  SER C CB  1 
ATOM   2940 O  OG  . SER C 1 98  ? -6.668  -72.776 15.713 1.00 100.13 ? 98  SER C OG  1 
ATOM   2941 N  N   . ILE C 1 99  ? -4.984  -70.086 14.481 1.00 93.23  ? 99  ILE C N   1 
ATOM   2942 C  CA  . ILE C 1 99  ? -5.020  -69.036 13.465 1.00 92.65  ? 99  ILE C CA  1 
ATOM   2943 C  C   . ILE C 1 99  ? -4.632  -69.612 12.136 1.00 94.95  ? 99  ILE C C   1 
ATOM   2944 O  O   . ILE C 1 99  ? -3.702  -70.403 12.069 1.00 95.40  ? 99  ILE C O   1 
ATOM   2945 C  CB  . ILE C 1 99  ? -3.940  -67.953 13.738 1.00 89.24  ? 99  ILE C CB  1 
ATOM   2946 C  CG1 . ILE C 1 99  ? -4.165  -67.276 15.083 1.00 87.26  ? 99  ILE C CG1 1 
ATOM   2947 C  CG2 . ILE C 1 99  ? -3.894  -66.940 12.629 1.00 88.80  ? 99  ILE C CG2 1 
ATOM   2948 C  CD1 . ILE C 1 99  ? -3.492  -65.915 15.207 1.00 83.70  ? 99  ILE C CD1 1 
ATOM   2949 N  N   . GLU C 1 100 ? -5.314  -69.214 11.073 1.00 97.42  ? 100 GLU C N   1 
ATOM   2950 C  CA  . GLU C 1 100 ? -4.787  -69.422 9.726  1.00 99.64  ? 100 GLU C CA  1 
ATOM   2951 C  C   . GLU C 1 100 ? -4.302  -68.089 9.238  1.00 98.00  ? 100 GLU C C   1 
ATOM   2952 O  O   . GLU C 1 100 ? -4.867  -67.062 9.572  1.00 97.40  ? 100 GLU C O   1 
ATOM   2953 C  CB  . GLU C 1 100 ? -5.852  -69.929 8.763  1.00 104.23 ? 100 GLU C CB  1 
ATOM   2954 C  CG  . GLU C 1 100 ? -6.125  -71.421 8.852  1.00 109.25 ? 100 GLU C CG  1 
ATOM   2955 C  CD  . GLU C 1 100 ? -6.518  -72.027 7.506  1.00 117.13 ? 100 GLU C CD  1 
ATOM   2956 O  OE1 . GLU C 1 100 ? -6.341  -71.329 6.464  1.00 119.69 ? 100 GLU C OE1 1 
ATOM   2957 O  OE2 . GLU C 1 100 ? -6.980  -73.205 7.508  1.00 122.45 ? 100 GLU C OE2 1 
ATOM   2958 N  N   . ASP C 1 101 ? -3.260  -68.094 8.434  1.00 98.03  ? 101 ASP C N   1 
ATOM   2959 C  CA  . ASP C 1 101 ? -2.805  -66.859 7.838  1.00 97.68  ? 101 ASP C CA  1 
ATOM   2960 C  C   . ASP C 1 101 ? -1.996  -67.191 6.607  1.00 99.58  ? 101 ASP C C   1 
ATOM   2961 O  O   . ASP C 1 101 ? -1.251  -68.163 6.609  1.00 99.78  ? 101 ASP C O   1 
ATOM   2962 C  CB  . ASP C 1 101 ? -1.936  -66.088 8.825  1.00 94.35  ? 101 ASP C CB  1 
ATOM   2963 C  CG  . ASP C 1 101 ? -1.620  -64.675 8.343  1.00 95.59  ? 101 ASP C CG  1 
ATOM   2964 O  OD1 . ASP C 1 101 ? -2.447  -63.775 8.636  1.00 97.33  ? 101 ASP C OD1 1 
ATOM   2965 O  OD2 . ASP C 1 101 ? -0.564  -64.464 7.680  1.00 97.60  ? 101 ASP C OD2 1 
ATOM   2966 N  N   . SER C 1 102 ? -2.124  -66.387 5.563  1.00 101.32 ? 102 SER C N   1 
ATOM   2967 C  CA  . SER C 1 102 ? -1.416  -66.669 4.330  1.00 104.15 ? 102 SER C CA  1 
ATOM   2968 C  C   . SER C 1 102 ? -0.546  -65.518 3.851  1.00 103.72 ? 102 SER C C   1 
ATOM   2969 O  O   . SER C 1 102 ? -0.038  -65.546 2.733  1.00 106.87 ? 102 SER C O   1 
ATOM   2970 C  CB  . SER C 1 102 ? -2.423  -67.076 3.269  1.00 108.87 ? 102 SER C CB  1 
ATOM   2971 O  OG  . SER C 1 102 ? -3.676  -66.509 3.586  1.00 109.88 ? 102 SER C OG  1 
ATOM   2972 N  N   . VAL C 1 103 ? -0.353  -64.515 4.697  1.00 100.27 ? 103 VAL C N   1 
ATOM   2973 C  CA  . VAL C 1 103 ? 0.656   -63.493 4.419  1.00 99.93  ? 103 VAL C CA  1 
ATOM   2974 C  C   . VAL C 1 103 ? 2.036   -64.012 4.814  1.00 98.04  ? 103 VAL C C   1 
ATOM   2975 O  O   . VAL C 1 103 ? 3.003   -63.846 4.064  1.00 100.03 ? 103 VAL C O   1 
ATOM   2976 C  CB  . VAL C 1 103 ? 0.392   -62.183 5.159  1.00 97.63  ? 103 VAL C CB  1 
ATOM   2977 C  CG1 . VAL C 1 103 ? 1.657   -61.345 5.181  1.00 96.82  ? 103 VAL C CG1 1 
ATOM   2978 C  CG2 . VAL C 1 103 ? -0.725  -61.438 4.482  1.00 100.41 ? 103 VAL C CG2 1 
ATOM   2979 N  N   . ILE C 1 104 ? 2.123   -64.634 5.992  1.00 94.65  ? 104 ILE C N   1 
ATOM   2980 C  CA  . ILE C 1 104 ? 3.375   -65.286 6.424  1.00 93.10  ? 104 ILE C CA  1 
ATOM   2981 C  C   . ILE C 1 104 ? 3.561   -66.618 5.695  1.00 95.90  ? 104 ILE C C   1 
ATOM   2982 O  O   . ILE C 1 104 ? 2.588   -67.192 5.152  1.00 98.23  ? 104 ILE C O   1 
ATOM   2983 C  CB  . ILE C 1 104 ? 3.422   -65.559 7.941  1.00 89.36  ? 104 ILE C CB  1 
ATOM   2984 C  CG1 . ILE C 1 104 ? 2.359   -66.583 8.344  1.00 89.06  ? 104 ILE C CG1 1 
ATOM   2985 C  CG2 . ILE C 1 104 ? 3.258   -64.268 8.709  1.00 87.00  ? 104 ILE C CG2 1 
ATOM   2986 C  CD1 . ILE C 1 104 ? 2.249   -66.736 9.791  1.00 86.00  ? 104 ILE C CD1 1 
ATOM   2987 N  N   . SER C 1 105 ? 4.805   -67.105 5.710  1.00 96.10  ? 105 SER C N   1 
ATOM   2988 C  CA  . SER C 1 105 ? 5.194   -68.332 4.993  1.00 99.16  ? 105 SER C CA  1 
ATOM   2989 C  C   . SER C 1 105 ? 6.335   -68.979 5.757  1.00 97.64  ? 105 SER C C   1 
ATOM   2990 O  O   . SER C 1 105 ? 7.075   -68.293 6.487  1.00 94.99  ? 105 SER C O   1 
ATOM   2991 C  CB  . SER C 1 105 ? 5.635   -67.991 3.538  1.00 103.40 ? 105 SER C CB  1 
ATOM   2992 O  OG  . SER C 1 105 ? 5.597   -69.114 2.623  1.00 107.09 ? 105 SER C OG  1 
ATOM   2993 N  N   . LEU C 1 106 ? 6.478   -70.293 5.604  1.00 99.72  ? 106 LEU C N   1 
ATOM   2994 C  CA  . LEU C 1 106 ? 7.663   -70.991 6.139  1.00 99.65  ? 106 LEU C CA  1 
ATOM   2995 C  C   . LEU C 1 106 ? 8.791   -71.155 5.088  1.00 103.78 ? 106 LEU C C   1 
ATOM   2996 O  O   . LEU C 1 106 ? 9.936   -71.521 5.433  1.00 103.66 ? 106 LEU C O   1 
ATOM   2997 C  CB  . LEU C 1 106 ? 7.273   -72.346 6.723  1.00 99.49  ? 106 LEU C CB  1 
ATOM   2998 C  CG  . LEU C 1 106 ? 6.244   -72.296 7.854  1.00 95.79  ? 106 LEU C CG  1 
ATOM   2999 C  CD1 . LEU C 1 106 ? 6.282   -73.536 8.724  1.00 94.52  ? 106 LEU C CD1 1 
ATOM   3000 C  CD2 . LEU C 1 106 ? 6.496   -71.086 8.699  1.00 91.48  ? 106 LEU C CD2 1 
ATOM   3001 N  N   . SER C 1 107 ? 8.453   -70.862 3.827  1.00 108.12 ? 107 SER C N   1 
ATOM   3002 C  CA  . SER C 1 107 ? 9.405   -70.801 2.720  1.00 112.35 ? 107 SER C CA  1 
ATOM   3003 C  C   . SER C 1 107 ? 9.242   -69.443 2.029  1.00 114.34 ? 107 SER C C   1 
ATOM   3004 O  O   . SER C 1 107 ? 8.434   -68.609 2.471  1.00 112.43 ? 107 SER C O   1 
ATOM   3005 C  CB  . SER C 1 107 ? 9.131   -71.956 1.750  1.00 116.79 ? 107 SER C CB  1 
ATOM   3006 O  OG  . SER C 1 107 ? 7.743   -72.044 1.395  1.00 118.03 ? 107 SER C OG  1 
ATOM   3007 N  N   . GLY C 1 108 ? 10.011  -69.190 0.967  1.00 119.06 ? 108 GLY C N   1 
ATOM   3008 C  CA  . GLY C 1 108 ? 9.888   -67.917 0.221  1.00 121.53 ? 108 GLY C CA  1 
ATOM   3009 C  C   . GLY C 1 108 ? 10.505  -66.763 1.007  1.00 118.84 ? 108 GLY C C   1 
ATOM   3010 O  O   . GLY C 1 108 ? 11.194  -66.988 2.021  1.00 115.85 ? 108 GLY C O   1 
ATOM   3011 N  N   . ASP C 1 109 ? 10.282  -65.528 0.560  1.00 120.47 ? 109 ASP C N   1 
ATOM   3012 C  CA  . ASP C 1 109 ? 10.962  -64.363 1.203  1.00 118.86 ? 109 ASP C CA  1 
ATOM   3013 C  C   . ASP C 1 109 ? 10.052  -63.693 2.227  1.00 114.23 ? 109 ASP C C   1 
ATOM   3014 O  O   . ASP C 1 109 ? 10.390  -62.645 2.790  1.00 112.49 ? 109 ASP C O   1 
ATOM   3015 C  CB  . ASP C 1 109 ? 11.577  -63.352 0.185  1.00 123.68 ? 109 ASP C CB  1 
ATOM   3016 C  CG  . ASP C 1 109 ? 10.732  -63.171 -1.090 1.00 130.15 ? 109 ASP C CG  1 
ATOM   3017 O  OD1 . ASP C 1 109 ? 11.223  -63.609 -2.178 1.00 135.84 ? 109 ASP C OD1 1 
ATOM   3018 O  OD2 . ASP C 1 109 ? 9.597   -62.598 -0.992 1.00 131.28 ? 109 ASP C OD2 1 
ATOM   3019 N  N   . HIS C 1 110 ? 8.899   -64.317 2.468  1.00 112.28 ? 110 HIS C N   1 
ATOM   3020 C  CA  . HIS C 1 110 ? 8.111   -64.028 3.665  1.00 107.91 ? 110 HIS C CA  1 
ATOM   3021 C  C   . HIS C 1 110 ? 8.400   -65.081 4.754  1.00 103.58 ? 110 HIS C C   1 
ATOM   3022 O  O   . HIS C 1 110 ? 7.681   -65.133 5.775  1.00 100.50 ? 110 HIS C O   1 
ATOM   3023 C  CB  . HIS C 1 110 ? 6.603   -64.005 3.325  1.00 109.20 ? 110 HIS C CB  1 
ATOM   3024 C  CG  . HIS C 1 110 ? 6.186   -62.853 2.440  1.00 114.56 ? 110 HIS C CG  1 
ATOM   3025 N  ND1 . HIS C 1 110 ? 4.862   -62.475 2.282  1.00 117.01 ? 110 HIS C ND1 1 
ATOM   3026 C  CD2 . HIS C 1 110 ? 6.917   -61.973 1.700  1.00 119.31 ? 110 HIS C CD2 1 
ATOM   3027 C  CE1 . HIS C 1 110 ? 4.798   -61.425 1.475  1.00 120.93 ? 110 HIS C CE1 1 
ATOM   3028 N  NE2 . HIS C 1 110 ? 6.030   -61.101 1.106  1.00 122.76 ? 110 HIS C NE2 1 
ATOM   3029 N  N   . CYS C 1 111 ? 9.449   -65.901 4.530  1.00 103.15 ? 111 CYS C N   1 
ATOM   3030 C  CA  . CYS C 1 111 ? 9.862   -66.976 5.456  1.00 99.39  ? 111 CYS C CA  1 
ATOM   3031 C  C   . CYS C 1 111 ? 10.126  -66.322 6.831  1.00 94.96  ? 111 CYS C C   1 
ATOM   3032 O  O   . CYS C 1 111 ? 10.867  -65.325 6.937  1.00 94.74  ? 111 CYS C O   1 
ATOM   3033 C  CB  . CYS C 1 111 ? 11.099  -67.714 4.919  1.00 101.48 ? 111 CYS C CB  1 
ATOM   3034 S  SG  . CYS C 1 111 ? 11.803  -68.968 5.983  1.00 97.98  ? 111 CYS C SG  1 
ATOM   3035 N  N   . ILE C 1 112 ? 9.455   -66.840 7.859  1.00 91.17  ? 112 ILE C N   1 
ATOM   3036 C  CA  . ILE C 1 112 ? 9.564   -66.283 9.212  1.00 87.30  ? 112 ILE C CA  1 
ATOM   3037 C  C   . ILE C 1 112 ? 10.442  -67.145 10.122 1.00 86.21  ? 112 ILE C C   1 
ATOM   3038 O  O   . ILE C 1 112 ? 10.573  -66.886 11.333 1.00 84.30  ? 112 ILE C O   1 
ATOM   3039 C  CB  . ILE C 1 112 ? 8.175   -66.125 9.866  1.00 85.32  ? 112 ILE C CB  1 
ATOM   3040 C  CG1 . ILE C 1 112 ? 7.504   -67.483 10.123 1.00 84.12  ? 112 ILE C CG1 1 
ATOM   3041 C  CG2 . ILE C 1 112 ? 7.295   -65.257 8.996  1.00 86.58  ? 112 ILE C CG2 1 
ATOM   3042 C  CD1 . ILE C 1 112 ? 6.288   -67.365 10.961 1.00 80.41  ? 112 ILE C CD1 1 
ATOM   3043 N  N   . ILE C 1 113 ? 11.017  -68.194 9.543  1.00 87.57  ? 113 ILE C N   1 
ATOM   3044 C  CA  . ILE C 1 113 ? 11.863  -69.090 10.294 1.00 86.84  ? 113 ILE C CA  1 
ATOM   3045 C  C   . ILE C 1 113 ? 13.096  -68.323 10.653 1.00 86.32  ? 113 ILE C C   1 
ATOM   3046 O  O   . ILE C 1 113 ? 13.746  -67.725 9.797  1.00 87.75  ? 113 ILE C O   1 
ATOM   3047 C  CB  . ILE C 1 113 ? 12.228  -70.314 9.483  1.00 89.30  ? 113 ILE C CB  1 
ATOM   3048 C  CG1 . ILE C 1 113 ? 11.071  -71.293 9.519  1.00 89.71  ? 113 ILE C CG1 1 
ATOM   3049 C  CG2 . ILE C 1 113 ? 13.430  -70.967 10.049 1.00 89.78  ? 113 ILE C CG2 1 
ATOM   3050 C  CD1 . ILE C 1 113 ? 11.262  -72.443 8.585  1.00 94.15  ? 113 ILE C CD1 1 
ATOM   3051 N  N   . GLY C 1 114 ? 13.393  -68.309 11.938 1.00 84.59  ? 114 GLY C N   1 
ATOM   3052 C  CA  . GLY C 1 114 ? 14.568  -67.620 12.418 1.00 84.82  ? 114 GLY C CA  1 
ATOM   3053 C  C   . GLY C 1 114 ? 14.275  -66.237 12.920 1.00 83.49  ? 114 GLY C C   1 
ATOM   3054 O  O   . GLY C 1 114 ? 15.203  -65.473 13.206 1.00 84.11  ? 114 GLY C O   1 
ATOM   3055 N  N   . ARG C 1 115 ? 12.991  -65.922 13.042 1.00 82.04  ? 115 ARG C N   1 
ATOM   3056 C  CA  . ARG C 1 115 ? 12.570  -64.615 13.518 1.00 81.27  ? 115 ARG C CA  1 
ATOM   3057 C  C   . ARG C 1 115 ? 11.836  -64.777 14.828 1.00 79.68  ? 115 ARG C C   1 
ATOM   3058 O  O   . ARG C 1 115 ? 11.310  -65.843 15.110 1.00 79.59  ? 115 ARG C O   1 
ATOM   3059 C  CB  . ARG C 1 115 ? 11.699  -63.961 12.462 1.00 81.58  ? 115 ARG C CB  1 
ATOM   3060 C  CG  . ARG C 1 115 ? 12.385  -63.936 11.097 1.00 84.10  ? 115 ARG C CG  1 
ATOM   3061 C  CD  . ARG C 1 115 ? 11.638  -63.078 10.119 1.00 85.80  ? 115 ARG C CD  1 
ATOM   3062 N  NE  . ARG C 1 115 ? 12.293  -63.056 8.825  1.00 88.77  ? 115 ARG C NE  1 
ATOM   3063 C  CZ  . ARG C 1 115 ? 13.284  -62.236 8.503  1.00 91.52  ? 115 ARG C CZ  1 
ATOM   3064 N  NH1 . ARG C 1 115 ? 13.756  -61.351 9.376  1.00 92.02  ? 115 ARG C NH1 1 
ATOM   3065 N  NH2 . ARG C 1 115 ? 13.807  -62.300 7.289  1.00 94.84  ? 115 ARG C NH2 1 
ATOM   3066 N  N   . THR C 1 116 ? 11.815  -63.740 15.646 1.00 79.16  ? 116 THR C N   1 
ATOM   3067 C  CA  . THR C 1 116 ? 11.216  -63.881 16.952 1.00 78.65  ? 116 THR C CA  1 
ATOM   3068 C  C   . THR C 1 116 ? 9.701   -63.730 16.860 1.00 77.15  ? 116 THR C C   1 
ATOM   3069 O  O   . THR C 1 116 ? 9.187   -62.879 16.165 1.00 77.08  ? 116 THR C O   1 
ATOM   3070 C  CB  . THR C 1 116 ? 11.786  -62.875 17.963 1.00 79.57  ? 116 THR C CB  1 
ATOM   3071 O  OG1 . THR C 1 116 ? 13.210  -63.015 18.039 1.00 82.30  ? 116 THR C OG1 1 
ATOM   3072 C  CG2 . THR C 1 116 ? 11.207  -63.125 19.349 1.00 80.47  ? 116 THR C CG2 1 
ATOM   3073 N  N   . LEU C 1 117 ? 8.997   -64.597 17.552 1.00 76.56  ? 117 LEU C N   1 
ATOM   3074 C  CA  . LEU C 1 117 ? 7.594   -64.442 17.780 1.00 75.89  ? 117 LEU C CA  1 
ATOM   3075 C  C   . LEU C 1 117 ? 7.447   -63.776 19.127 1.00 76.44  ? 117 LEU C C   1 
ATOM   3076 O  O   . LEU C 1 117 ? 8.177   -64.092 20.045 1.00 77.80  ? 117 LEU C O   1 
ATOM   3077 C  CB  . LEU C 1 117 ? 6.967   -65.811 17.849 1.00 76.01  ? 117 LEU C CB  1 
ATOM   3078 C  CG  . LEU C 1 117 ? 5.468   -65.859 18.103 1.00 75.09  ? 117 LEU C CG  1 
ATOM   3079 C  CD1 . LEU C 1 117 ? 4.791   -65.207 16.959 1.00 74.69  ? 117 LEU C CD1 1 
ATOM   3080 C  CD2 . LEU C 1 117 ? 4.955   -67.277 18.244 1.00 74.61  ? 117 LEU C CD2 1 
ATOM   3081 N  N   . VAL C 1 118 ? 6.493   -62.873 19.270 1.00 76.45  ? 118 VAL C N   1 
ATOM   3082 C  CA  . VAL C 1 118 ? 6.347   -62.123 20.512 1.00 77.44  ? 118 VAL C CA  1 
ATOM   3083 C  C   . VAL C 1 118 ? 4.899   -61.982 20.910 1.00 77.66  ? 118 VAL C C   1 
ATOM   3084 O  O   . VAL C 1 118 ? 4.040   -61.729 20.073 1.00 77.20  ? 118 VAL C O   1 
ATOM   3085 C  CB  . VAL C 1 118 ? 6.903   -60.722 20.366 1.00 77.82  ? 118 VAL C CB  1 
ATOM   3086 C  CG1 . VAL C 1 118 ? 6.764   -59.953 21.661 1.00 79.33  ? 118 VAL C CG1 1 
ATOM   3087 C  CG2 . VAL C 1 118 ? 8.338   -60.797 19.997 1.00 78.79  ? 118 VAL C CG2 1 
ATOM   3088 N  N   . VAL C 1 119 ? 4.629   -62.148 22.193 1.00 79.02  ? 119 VAL C N   1 
ATOM   3089 C  CA  . VAL C 1 119 ? 3.312   -61.881 22.726 1.00 80.02  ? 119 VAL C CA  1 
ATOM   3090 C  C   . VAL C 1 119 ? 3.455   -60.674 23.644 1.00 82.22  ? 119 VAL C C   1 
ATOM   3091 O  O   . VAL C 1 119 ? 4.466   -60.524 24.327 1.00 83.64  ? 119 VAL C O   1 
ATOM   3092 C  CB  . VAL C 1 119 ? 2.750   -63.098 23.487 1.00 80.95  ? 119 VAL C CB  1 
ATOM   3093 C  CG1 . VAL C 1 119 ? 3.682   -63.497 24.592 1.00 82.69  ? 119 VAL C CG1 1 
ATOM   3094 C  CG2 . VAL C 1 119 ? 1.370   -62.802 24.064 1.00 81.81  ? 119 VAL C CG2 1 
ATOM   3095 N  N   . HIS C 1 120 ? 2.439   -59.818 23.666 1.00 83.48  ? 120 HIS C N   1 
ATOM   3096 C  CA  . HIS C 1 120 ? 2.567   -58.483 24.247 1.00 85.56  ? 120 HIS C CA  1 
ATOM   3097 C  C   . HIS C 1 120 ? 1.696   -58.236 25.475 1.00 88.32  ? 120 HIS C C   1 
ATOM   3098 O  O   . HIS C 1 120 ? 0.765   -58.994 25.777 1.00 88.55  ? 120 HIS C O   1 
ATOM   3099 C  CB  . HIS C 1 120 ? 2.202   -57.436 23.198 1.00 84.86  ? 120 HIS C CB  1 
ATOM   3100 C  CG  . HIS C 1 120 ? 3.259   -57.208 22.175 1.00 85.03  ? 120 HIS C CG  1 
ATOM   3101 N  ND1 . HIS C 1 120 ? 4.062   -56.089 22.175 1.00 88.57  ? 120 HIS C ND1 1 
ATOM   3102 C  CD2 . HIS C 1 120 ? 3.633   -57.939 21.103 1.00 84.80  ? 120 HIS C CD2 1 
ATOM   3103 C  CE1 . HIS C 1 120 ? 4.894   -56.144 21.151 1.00 88.86  ? 120 HIS C CE1 1 
ATOM   3104 N  NE2 . HIS C 1 120 ? 4.654   -57.257 20.483 1.00 86.31  ? 120 HIS C NE2 1 
ATOM   3105 N  N   . GLU C 1 121 ? 2.006   -57.121 26.141 1.00 91.00  ? 121 GLU C N   1 
ATOM   3106 C  CA  . GLU C 1 121 ? 1.346   -56.694 27.372 1.00 94.47  ? 121 GLU C CA  1 
ATOM   3107 C  C   . GLU C 1 121 ? -0.143  -56.458 27.200 1.00 94.40  ? 121 GLU C C   1 
ATOM   3108 O  O   . GLU C 1 121 ? -0.925  -57.014 27.960 1.00 95.77  ? 121 GLU C O   1 
ATOM   3109 C  CB  . GLU C 1 121 ? 2.004   -55.421 27.889 1.00 97.10  ? 121 GLU C CB  1 
ATOM   3110 C  CG  . GLU C 1 121 ? 1.573   -55.025 29.295 1.00 103.09 ? 121 GLU C CG  1 
ATOM   3111 C  CD  . GLU C 1 121 ? 2.196   -53.688 29.766 1.00 108.57 ? 121 GLU C CD  1 
ATOM   3112 O  OE1 . GLU C 1 121 ? 2.626   -52.853 28.918 1.00 108.33 ? 121 GLU C OE1 1 
ATOM   3113 O  OE2 . GLU C 1 121 ? 2.246   -53.475 31.001 1.00 114.05 ? 121 GLU C OE2 1 
ATOM   3114 N  N   . LYS C 1 122 ? -0.518  -55.642 26.211 1.00 93.33  ? 122 LYS C N   1 
ATOM   3115 C  CA  . LYS C 1 122 ? -1.928  -55.278 25.967 1.00 94.24  ? 122 LYS C CA  1 
ATOM   3116 C  C   . LYS C 1 122 ? -2.442  -55.776 24.620 1.00 91.40  ? 122 LYS C C   1 
ATOM   3117 O  O   . LYS C 1 122 ? -1.754  -56.509 23.905 1.00 89.61  ? 122 LYS C O   1 
ATOM   3118 C  CB  . LYS C 1 122 ? -2.113  -53.751 25.982 1.00 96.32  ? 122 LYS C CB  1 
ATOM   3119 C  CG  . LYS C 1 122 ? -1.228  -52.972 26.936 1.00 100.67 ? 122 LYS C CG  1 
ATOM   3120 C  CD  . LYS C 1 122 ? -1.497  -51.464 26.815 1.00 104.72 ? 122 LYS C CD  1 
ATOM   3121 C  CE  . LYS C 1 122 ? -0.210  -50.660 27.011 1.00 107.39 ? 122 LYS C CE  1 
ATOM   3122 N  NZ  . LYS C 1 122 ? -0.455  -49.195 27.113 1.00 111.04 ? 122 LYS C NZ  1 
ATOM   3123 N  N   . ALA C 1 123 ? -3.647  -55.333 24.273 1.00 91.39  ? 123 ALA C N   1 
ATOM   3124 C  CA  . ALA C 1 123 ? -4.217  -55.602 22.971 1.00 89.45  ? 123 ALA C CA  1 
ATOM   3125 C  C   . ALA C 1 123 ? -3.517  -54.820 21.862 1.00 88.05  ? 123 ALA C C   1 
ATOM   3126 O  O   . ALA C 1 123 ? -3.152  -53.661 22.057 1.00 88.74  ? 123 ALA C O   1 
ATOM   3127 C  CB  . ALA C 1 123 ? -5.676  -55.253 22.984 1.00 91.18  ? 123 ALA C CB  1 
ATOM   3128 N  N   . ASP C 1 124 ? -3.329  -55.479 20.711 1.00 86.20  ? 124 ASP C N   1 
ATOM   3129 C  CA  . ASP C 1 124 ? -2.973  -54.830 19.427 1.00 85.75  ? 124 ASP C CA  1 
ATOM   3130 C  C   . ASP C 1 124 ? -4.226  -54.107 18.985 1.00 86.70  ? 124 ASP C C   1 
ATOM   3131 O  O   . ASP C 1 124 ? -5.300  -54.688 18.998 1.00 86.84  ? 124 ASP C O   1 
ATOM   3132 C  CB  . ASP C 1 124 ? -2.575  -55.894 18.369 1.00 84.46  ? 124 ASP C CB  1 
ATOM   3133 C  CG  . ASP C 1 124 ? -2.131  -55.289 17.002 1.00 85.66  ? 124 ASP C CG  1 
ATOM   3134 O  OD1 . ASP C 1 124 ? -2.234  -54.047 16.851 1.00 88.10  ? 124 ASP C OD1 1 
ATOM   3135 O  OD2 . ASP C 1 124 ? -1.687  -56.065 16.079 1.00 85.27  ? 124 ASP C OD2 1 
ATOM   3136 N  N   . ASP C 1 125 ? -4.107  -52.834 18.625 1.00 87.64  ? 125 ASP C N   1 
ATOM   3137 C  CA  . ASP C 1 125 ? -5.289  -52.060 18.258 1.00 89.26  ? 125 ASP C CA  1 
ATOM   3138 C  C   . ASP C 1 125 ? -5.486  -52.077 16.754 1.00 89.28  ? 125 ASP C C   1 
ATOM   3139 O  O   . ASP C 1 125 ? -6.294  -51.332 16.227 1.00 90.80  ? 125 ASP C O   1 
ATOM   3140 C  CB  . ASP C 1 125 ? -5.244  -50.630 18.839 1.00 91.40  ? 125 ASP C CB  1 
ATOM   3141 C  CG  . ASP C 1 125 ? -4.218  -49.723 18.153 1.00 92.44  ? 125 ASP C CG  1 
ATOM   3142 O  OD1 . ASP C 1 125 ? -3.778  -50.051 17.015 1.00 92.05  ? 125 ASP C OD1 1 
ATOM   3143 O  OD2 . ASP C 1 125 ? -3.874  -48.660 18.756 1.00 93.97  ? 125 ASP C OD2 1 
ATOM   3144 N  N   . LEU C 1 126 ? -4.724  -52.927 16.072 1.00 87.92  ? 126 LEU C N   1 
ATOM   3145 C  CA  . LEU C 1 126 ? -4.890  -53.181 14.635 1.00 88.79  ? 126 LEU C CA  1 
ATOM   3146 C  C   . LEU C 1 126 ? -4.712  -51.936 13.767 1.00 91.35  ? 126 LEU C C   1 
ATOM   3147 O  O   . LEU C 1 126 ? -5.232  -51.871 12.645 1.00 92.84  ? 126 LEU C O   1 
ATOM   3148 C  CB  . LEU C 1 126 ? -6.250  -53.832 14.353 1.00 89.46  ? 126 LEU C CB  1 
ATOM   3149 C  CG  . LEU C 1 126 ? -6.650  -54.972 15.282 1.00 87.52  ? 126 LEU C CG  1 
ATOM   3150 C  CD1 . LEU C 1 126 ? -7.728  -55.829 14.610 1.00 88.14  ? 126 LEU C CD1 1 
ATOM   3151 C  CD2 . LEU C 1 126 ? -5.427  -55.789 15.633 1.00 84.25  ? 126 LEU C CD2 1 
ATOM   3152 N  N   . GLY C 1 127 ? -3.968  -50.962 14.300 1.00 92.43  ? 127 GLY C N   1 
ATOM   3153 C  CA  . GLY C 1 127 ? -3.640  -49.727 13.591 1.00 95.56  ? 127 GLY C CA  1 
ATOM   3154 C  C   . GLY C 1 127 ? -4.641  -48.593 13.758 1.00 98.82  ? 127 GLY C C   1 
ATOM   3155 O  O   . GLY C 1 127 ? -4.391  -47.469 13.332 1.00 101.34 ? 127 GLY C O   1 
ATOM   3156 N  N   . LYS C 1 128 ? -5.768  -48.868 14.408 1.00 99.55  ? 128 LYS C N   1 
ATOM   3157 C  CA  . LYS C 1 128 ? -6.903  -47.939 14.415 1.00 103.10 ? 128 LYS C CA  1 
ATOM   3158 C  C   . LYS C 1 128 ? -6.956  -47.125 15.715 1.00 103.64 ? 128 LYS C C   1 
ATOM   3159 O  O   . LYS C 1 128 ? -8.027  -46.658 16.100 1.00 105.38 ? 128 LYS C O   1 
ATOM   3160 C  CB  . LYS C 1 128 ? -8.243  -48.685 14.226 1.00 103.72 ? 128 LYS C CB  1 
ATOM   3161 C  CG  . LYS C 1 128 ? -8.186  -49.915 13.336 1.00 105.36 ? 128 LYS C CG  1 
ATOM   3162 C  CD  . LYS C 1 128 ? -9.557  -50.332 12.773 1.00 110.42 ? 128 LYS C CD  1 
ATOM   3163 C  CE  . LYS C 1 128 ? -9.469  -51.716 12.072 1.00 111.38 ? 128 LYS C CE  1 
ATOM   3164 N  NZ  . LYS C 1 128 ? -8.642  -51.693 10.792 1.00 113.21 ? 128 LYS C NZ  1 
ATOM   3165 N  N   . GLY C 1 129 ? -5.811  -46.948 16.383 1.00 102.82 ? 129 GLY C N   1 
ATOM   3166 C  CA  . GLY C 1 129 ? -5.733  -46.191 17.655 1.00 104.08 ? 129 GLY C CA  1 
ATOM   3167 C  C   . GLY C 1 129 ? -5.541  -44.695 17.446 1.00 107.74 ? 129 GLY C C   1 
ATOM   3168 O  O   . GLY C 1 129 ? -5.568  -43.905 18.403 1.00 109.22 ? 129 GLY C O   1 
ATOM   3169 N  N   . GLY C 1 130 ? -5.302  -44.322 16.175 1.00 109.35 ? 130 GLY C N   1 
ATOM   3170 C  CA  . GLY C 1 130 ? -5.149  -42.926 15.762 1.00 113.37 ? 130 GLY C CA  1 
ATOM   3171 C  C   . GLY C 1 130 ? -4.015  -42.174 16.480 1.00 114.84 ? 130 GLY C C   1 
ATOM   3172 O  O   . GLY C 1 130 ? -4.016  -40.948 16.583 1.00 118.50 ? 130 GLY C O   1 
ATOM   3173 N  N   . ASN C 1 131 ? -3.029  -42.894 16.974 1.00 112.60 ? 131 ASN C N   1 
ATOM   3174 C  CA  . ASN C 1 131 ? -1.860  -42.230 17.447 1.00 114.52 ? 131 ASN C CA  1 
ATOM   3175 C  C   . ASN C 1 131 ? -0.658  -42.743 16.652 1.00 113.68 ? 131 ASN C C   1 
ATOM   3176 O  O   . ASN C 1 131 ? -0.780  -43.694 15.868 1.00 111.08 ? 131 ASN C O   1 
ATOM   3177 C  CB  . ASN C 1 131 ? -1.773  -42.353 18.968 1.00 114.29 ? 131 ASN C CB  1 
ATOM   3178 C  CG  . ASN C 1 131 ? -1.057  -43.596 19.432 1.00 110.55 ? 131 ASN C CG  1 
ATOM   3179 O  OD1 . ASN C 1 131 ? -1.245  -44.675 18.864 1.00 107.21 ? 131 ASN C OD1 1 
ATOM   3180 N  ND2 . ASN C 1 131 ? -0.250  -43.461 20.502 1.00 110.90 ? 131 ASN C ND2 1 
ATOM   3181 N  N   . GLU C 1 132 ? 0.468   -42.050 16.776 1.00 116.71 ? 132 GLU C N   1 
ATOM   3182 C  CA  . GLU C 1 132 ? 1.636   -42.328 15.937 1.00 117.43 ? 132 GLU C CA  1 
ATOM   3183 C  C   . GLU C 1 132 ? 2.017   -43.796 16.104 1.00 112.76 ? 132 GLU C C   1 
ATOM   3184 O  O   . GLU C 1 132 ? 2.165   -44.558 15.120 1.00 110.58 ? 132 GLU C O   1 
ATOM   3185 C  CB  . GLU C 1 132 ? 2.791   -41.372 16.322 1.00 121.56 ? 132 GLU C CB  1 
ATOM   3186 C  CG  . GLU C 1 132 ? 4.279   -41.926 16.140 1.00 123.61 ? 132 GLU C CG  1 
ATOM   3187 C  CD  . GLU C 1 132 ? 4.994   -41.516 14.813 1.00 129.14 ? 132 GLU C CD  1 
ATOM   3188 O  OE1 . GLU C 1 132 ? 4.627   -40.438 14.259 1.00 134.59 ? 132 GLU C OE1 1 
ATOM   3189 O  OE2 . GLU C 1 132 ? 5.929   -42.262 14.353 1.00 128.79 ? 132 GLU C OE2 1 
ATOM   3190 N  N   . GLU C 1 133 ? 2.129   -44.165 17.381 1.00 111.27 ? 133 GLU C N   1 
ATOM   3191 C  CA  . GLU C 1 133 ? 2.545   -45.494 17.814 1.00 107.82 ? 133 GLU C CA  1 
ATOM   3192 C  C   . GLU C 1 133 ? 1.654   -46.642 17.293 1.00 104.02 ? 133 GLU C C   1 
ATOM   3193 O  O   . GLU C 1 133 ? 2.116   -47.759 17.092 1.00 101.34 ? 133 GLU C O   1 
ATOM   3194 C  CB  . GLU C 1 133 ? 2.614   -45.515 19.351 1.00 108.33 ? 133 GLU C CB  1 
ATOM   3195 C  CG  . GLU C 1 133 ? 3.250   -46.770 19.944 1.00 107.60 ? 133 GLU C CG  1 
ATOM   3196 C  CD  . GLU C 1 133 ? 4.698   -46.999 19.464 1.00 110.57 ? 133 GLU C CD  1 
ATOM   3197 O  OE1 . GLU C 1 133 ? 5.456   -45.988 19.337 1.00 115.10 ? 133 GLU C OE1 1 
ATOM   3198 O  OE2 . GLU C 1 133 ? 5.063   -48.192 19.199 1.00 109.19 ? 133 GLU C OE2 1 
ATOM   3199 N  N   . SER C 1 134 ? 0.380   -46.361 17.067 1.00 104.09 ? 134 SER C N   1 
ATOM   3200 C  CA  . SER C 1 134 ? -0.538  -47.390 16.622 1.00 101.32 ? 134 SER C CA  1 
ATOM   3201 C  C   . SER C 1 134 ? -0.195  -47.901 15.239 1.00 100.73 ? 134 SER C C   1 
ATOM   3202 O  O   . SER C 1 134 ? -0.427  -49.060 14.970 1.00 99.01  ? 134 SER C O   1 
ATOM   3203 C  CB  . SER C 1 134 ? -1.982  -46.911 16.635 1.00 102.53 ? 134 SER C CB  1 
ATOM   3204 O  OG  . SER C 1 134 ? -2.819  -47.912 16.092 1.00 100.02 ? 134 SER C OG  1 
ATOM   3205 N  N   . THR C 1 135 ? 0.357   -47.073 14.358 1.00 102.84 ? 135 THR C N   1 
ATOM   3206 C  CA  . THR C 1 135 ? 0.712   -47.549 13.009 1.00 102.80 ? 135 THR C CA  1 
ATOM   3207 C  C   . THR C 1 135 ? 2.090   -48.242 12.973 1.00 101.38 ? 135 THR C C   1 
ATOM   3208 O  O   . THR C 1 135 ? 2.625   -48.525 11.893 1.00 101.98 ? 135 THR C O   1 
ATOM   3209 C  CB  . THR C 1 135 ? 0.685   -46.384 12.040 1.00 106.77 ? 135 THR C CB  1 
ATOM   3210 O  OG1 . THR C 1 135 ? 1.190   -45.234 12.739 1.00 108.88 ? 135 THR C OG1 1 
ATOM   3211 C  CG2 . THR C 1 135 ? -0.750  -46.109 11.555 1.00 107.34 ? 135 THR C CG2 1 
ATOM   3212 N  N   . LYS C 1 136 ? 2.635   -48.544 14.156 1.00 99.84  ? 136 LYS C N   1 
ATOM   3213 C  CA  . LYS C 1 136 ? 3.933   -49.228 14.299 1.00 98.96  ? 136 LYS C CA  1 
ATOM   3214 C  C   . LYS C 1 136 ? 3.830   -50.527 15.131 1.00 95.32  ? 136 LYS C C   1 
ATOM   3215 O  O   . LYS C 1 136 ? 4.117   -51.629 14.632 1.00 93.51  ? 136 LYS C O   1 
ATOM   3216 C  CB  . LYS C 1 136 ? 4.950   -48.260 14.928 1.00 101.36 ? 136 LYS C CB  1 
ATOM   3217 C  CG  . LYS C 1 136 ? 4.974   -46.879 14.233 1.00 107.37 ? 136 LYS C CG  1 
ATOM   3218 C  CD  . LYS C 1 136 ? 5.864   -45.843 14.986 1.00 112.81 ? 136 LYS C CD  1 
ATOM   3219 C  CE  . LYS C 1 136 ? 7.370   -46.201 14.976 1.00 114.08 ? 136 LYS C CE  1 
ATOM   3220 N  NZ  . LYS C 1 136 ? 8.195   -45.068 15.475 1.00 118.26 ? 136 LYS C NZ  1 
ATOM   3221 N  N   . THR C 1 137 ? 3.422   -50.389 16.390 1.00 94.42  ? 137 THR C N   1 
ATOM   3222 C  CA  . THR C 1 137 ? 3.271   -51.543 17.241 1.00 92.04  ? 137 THR C CA  1 
ATOM   3223 C  C   . THR C 1 137 ? 1.817   -51.851 17.526 1.00 90.65  ? 137 THR C C   1 
ATOM   3224 O  O   . THR C 1 137 ? 1.537   -52.791 18.250 1.00 89.57  ? 137 THR C O   1 
ATOM   3225 C  CB  . THR C 1 137 ? 4.004   -51.382 18.610 1.00 92.83  ? 137 THR C CB  1 
ATOM   3226 O  OG1 . THR C 1 137 ? 3.460   -50.270 19.329 1.00 95.32  ? 137 THR C OG1 1 
ATOM   3227 C  CG2 . THR C 1 137 ? 5.514   -51.211 18.426 1.00 94.18  ? 137 THR C CG2 1 
ATOM   3228 N  N   . GLY C 1 138 ? 0.883   -51.070 17.007 1.00 91.19  ? 138 GLY C N   1 
ATOM   3229 C  CA  . GLY C 1 138 ? -0.514  -51.234 17.424 1.00 90.64  ? 138 GLY C CA  1 
ATOM   3230 C  C   . GLY C 1 138 ? -0.772  -50.974 18.911 1.00 90.92  ? 138 GLY C C   1 
ATOM   3231 O  O   . GLY C 1 138 ? -1.757  -51.453 19.463 1.00 90.27  ? 138 GLY C O   1 
ATOM   3232 N  N   . ASN C 1 139 ? 0.117   -50.211 19.553 1.00 92.27  ? 139 ASN C N   1 
ATOM   3233 C  CA  . ASN C 1 139 ? 0.020   -49.870 20.984 1.00 93.72  ? 139 ASN C CA  1 
ATOM   3234 C  C   . ASN C 1 139 ? -0.007  -51.078 21.895 1.00 92.66  ? 139 ASN C C   1 
ATOM   3235 O  O   . ASN C 1 139 ? -0.538  -51.012 23.011 1.00 93.88  ? 139 ASN C O   1 
ATOM   3236 C  CB  . ASN C 1 139 ? -1.219  -49.006 21.252 1.00 95.62  ? 139 ASN C CB  1 
ATOM   3237 C  CG  . ASN C 1 139 ? -0.987  -47.533 20.965 1.00 98.22  ? 139 ASN C CG  1 
ATOM   3238 O  OD1 . ASN C 1 139 ? 0.153   -47.053 20.836 1.00 97.85  ? 139 ASN C OD1 1 
ATOM   3239 N  ND2 . ASN C 1 139 ? -2.082  -46.799 20.869 1.00 100.31 ? 139 ASN C ND2 1 
ATOM   3240 N  N   . ALA C 1 140 ? 0.603   -52.164 21.421 1.00 90.99  ? 140 ALA C N   1 
ATOM   3241 C  CA  . ALA C 1 140 ? 0.428   -53.493 22.019 1.00 90.07  ? 140 ALA C CA  1 
ATOM   3242 C  C   . ALA C 1 140 ? 1.140   -53.573 23.356 1.00 91.75  ? 140 ALA C C   1 
ATOM   3243 O  O   . ALA C 1 140 ? 0.840   -54.439 24.199 1.00 91.79  ? 140 ALA C O   1 
ATOM   3244 C  CB  . ALA C 1 140 ? 0.968   -54.552 21.099 1.00 87.96  ? 140 ALA C CB  1 
ATOM   3245 N  N   . GLY C 1 141 ? 2.106   -52.672 23.526 1.00 93.59  ? 141 GLY C N   1 
ATOM   3246 C  CA  . GLY C 1 141 ? 2.797   -52.516 24.790 1.00 95.92  ? 141 GLY C CA  1 
ATOM   3247 C  C   . GLY C 1 141 ? 4.070   -53.322 24.825 1.00 95.21  ? 141 GLY C C   1 
ATOM   3248 O  O   . GLY C 1 141 ? 4.555   -53.807 23.809 1.00 93.10  ? 141 GLY C O   1 
ATOM   3249 N  N   . SER C 1 142 ? 4.599   -53.476 26.022 1.00 97.64  ? 142 SER C N   1 
ATOM   3250 C  CA  . SER C 1 142 ? 5.875   -54.150 26.221 1.00 97.97  ? 142 SER C CA  1 
ATOM   3251 C  C   . SER C 1 142 ? 5.789   -55.623 25.827 1.00 95.25  ? 142 SER C C   1 
ATOM   3252 O  O   . SER C 1 142 ? 4.717   -56.142 25.499 1.00 93.64  ? 142 SER C O   1 
ATOM   3253 C  CB  . SER C 1 142 ? 6.339   -54.002 27.684 1.00 101.73 ? 142 SER C CB  1 
ATOM   3254 O  OG  . SER C 1 142 ? 5.382   -54.541 28.609 1.00 103.40 ? 142 SER C OG  1 
ATOM   3255 N  N   . ARG C 1 143 ? 6.929   -56.293 25.877 1.00 95.06  ? 143 ARG C N   1 
ATOM   3256 C  CA  . ARG C 1 143 ? 7.073   -57.611 25.278 1.00 92.89  ? 143 ARG C CA  1 
ATOM   3257 C  C   . ARG C 1 143 ? 7.130   -58.687 26.356 1.00 93.42  ? 143 ARG C C   1 
ATOM   3258 O  O   . ARG C 1 143 ? 8.191   -59.012 26.878 1.00 95.00  ? 143 ARG C O   1 
ATOM   3259 C  CB  . ARG C 1 143 ? 8.327   -57.600 24.407 1.00 92.66  ? 143 ARG C CB  1 
ATOM   3260 C  CG  . ARG C 1 143 ? 8.303   -56.463 23.389 1.00 94.10  ? 143 ARG C CG  1 
ATOM   3261 C  CD  . ARG C 1 143 ? 9.502   -56.472 22.476 1.00 96.55  ? 143 ARG C CD  1 
ATOM   3262 N  NE  . ARG C 1 143 ? 9.288   -55.636 21.296 1.00 97.88  ? 143 ARG C NE  1 
ATOM   3263 C  CZ  . ARG C 1 143 ? 10.184  -55.435 20.327 1.00 99.54  ? 143 ARG C CZ  1 
ATOM   3264 N  NH1 . ARG C 1 143 ? 11.385  -56.002 20.367 1.00 100.39 ? 143 ARG C NH1 1 
ATOM   3265 N  NH2 . ARG C 1 143 ? 9.877   -54.651 19.304 1.00 100.86 ? 143 ARG C NH2 1 
ATOM   3266 N  N   . LEU C 1 144 ? 5.975   -59.237 26.691 1.00 92.56  ? 144 LEU C N   1 
ATOM   3267 C  CA  . LEU C 1 144 ? 5.854   -60.125 27.850 1.00 94.43  ? 144 LEU C CA  1 
ATOM   3268 C  C   . LEU C 1 144 ? 6.677   -61.427 27.752 1.00 93.63  ? 144 LEU C C   1 
ATOM   3269 O  O   . LEU C 1 144 ? 7.298   -61.855 28.740 1.00 96.17  ? 144 LEU C O   1 
ATOM   3270 C  CB  . LEU C 1 144 ? 4.374   -60.459 28.097 1.00 94.80  ? 144 LEU C CB  1 
ATOM   3271 C  CG  . LEU C 1 144 ? 3.513   -59.409 28.817 1.00 97.64  ? 144 LEU C CG  1 
ATOM   3272 C  CD1 . LEU C 1 144 ? 2.069   -59.955 29.026 1.00 99.18  ? 144 LEU C CD1 1 
ATOM   3273 C  CD2 . LEU C 1 144 ? 4.138   -58.967 30.154 1.00 102.41 ? 144 LEU C CD2 1 
ATOM   3274 N  N   . ALA C 1 145 ? 6.658   -62.058 26.577 1.00 90.35  ? 145 ALA C N   1 
ATOM   3275 C  CA  . ALA C 1 145 ? 7.404   -63.287 26.337 1.00 89.93  ? 145 ALA C CA  1 
ATOM   3276 C  C   . ALA C 1 145 ? 7.715   -63.401 24.859 1.00 87.38  ? 145 ALA C C   1 
ATOM   3277 O  O   . ALA C 1 145 ? 7.044   -62.780 24.044 1.00 86.10  ? 145 ALA C O   1 
ATOM   3278 C  CB  . ALA C 1 145 ? 6.607   -64.476 26.790 1.00 90.58  ? 145 ALA C CB  1 
ATOM   3279 N  N   . CYS C 1 146 ? 8.730   -64.186 24.509 1.00 87.47  ? 146 CYS C N   1 
ATOM   3280 C  CA  . CYS C 1 146 ? 9.116   -64.352 23.111 1.00 85.66  ? 146 CYS C CA  1 
ATOM   3281 C  C   . CYS C 1 146 ? 10.045  -65.514 22.898 1.00 85.47  ? 146 CYS C C   1 
ATOM   3282 O  O   . CYS C 1 146 ? 10.606  -66.046 23.835 1.00 87.46  ? 146 CYS C O   1 
ATOM   3283 C  CB  . CYS C 1 146 ? 9.806   -63.090 22.600 1.00 85.69  ? 146 CYS C CB  1 
ATOM   3284 S  SG  . CYS C 1 146 ? 11.451  -62.775 23.304 1.00 90.27  ? 146 CYS C SG  1 
ATOM   3285 N  N   . GLY C 1 147 ? 10.217  -65.897 21.648 1.00 83.59  ? 147 GLY C N   1 
ATOM   3286 C  CA  . GLY C 1 147 ? 11.227  -66.881 21.313 1.00 83.98  ? 147 GLY C CA  1 
ATOM   3287 C  C   . GLY C 1 147 ? 11.471  -66.969 19.830 1.00 82.25  ? 147 GLY C C   1 
ATOM   3288 O  O   . GLY C 1 147 ? 10.614  -66.617 19.041 1.00 80.96  ? 147 GLY C O   1 
ATOM   3289 N  N   . VAL C 1 148 ? 12.641  -67.458 19.449 1.00 82.24  ? 148 VAL C N   1 
ATOM   3290 C  CA  . VAL C 1 148 ? 12.934  -67.632 18.037 1.00 81.18  ? 148 VAL C CA  1 
ATOM   3291 C  C   . VAL C 1 148 ? 12.138  -68.771 17.471 1.00 80.48  ? 148 VAL C C   1 
ATOM   3292 O  O   . VAL C 1 148 ? 11.875  -69.740 18.155 1.00 80.96  ? 148 VAL C O   1 
ATOM   3293 C  CB  . VAL C 1 148 ? 14.405  -67.901 17.796 1.00 82.47  ? 148 VAL C CB  1 
ATOM   3294 C  CG1 . VAL C 1 148 ? 14.651  -68.176 16.354 1.00 81.91  ? 148 VAL C CG1 1 
ATOM   3295 C  CG2 . VAL C 1 148 ? 15.185  -66.717 18.216 1.00 83.28  ? 148 VAL C CG2 1 
ATOM   3296 N  N   . ILE C 1 149 ? 11.762  -68.635 16.210 1.00 79.72  ? 149 ILE C N   1 
ATOM   3297 C  CA  . ILE C 1 149 ? 10.948  -69.620 15.514 1.00 80.04  ? 149 ILE C CA  1 
ATOM   3298 C  C   . ILE C 1 149 ? 11.854  -70.573 14.815 1.00 81.38  ? 149 ILE C C   1 
ATOM   3299 O  O   . ILE C 1 149 ? 12.649  -70.147 13.986 1.00 81.79  ? 149 ILE C O   1 
ATOM   3300 C  CB  . ILE C 1 149 ? 10.118  -68.952 14.402 1.00 79.72  ? 149 ILE C CB  1 
ATOM   3301 C  CG1 . ILE C 1 149 ? 8.906   -68.250 14.971 1.00 78.46  ? 149 ILE C CG1 1 
ATOM   3302 C  CG2 . ILE C 1 149 ? 9.649   -69.956 13.387 1.00 81.36  ? 149 ILE C CG2 1 
ATOM   3303 C  CD1 . ILE C 1 149 ? 8.504   -67.095 14.101 1.00 78.71  ? 149 ILE C CD1 1 
ATOM   3304 N  N   . GLY C 1 150 ? 11.698  -71.862 15.083 1.00 82.53  ? 150 GLY C N   1 
ATOM   3305 C  CA  . GLY C 1 150 ? 12.644  -72.849 14.567 1.00 84.96  ? 150 GLY C CA  1 
ATOM   3306 C  C   . GLY C 1 150 ? 12.030  -74.046 13.877 1.00 86.99  ? 150 GLY C C   1 
ATOM   3307 O  O   . GLY C 1 150 ? 10.848  -74.340 14.087 1.00 86.95  ? 150 GLY C O   1 
ATOM   3308 N  N   . ILE C 1 151 ? 12.845  -74.760 13.092 1.00 89.47  ? 151 ILE C N   1 
ATOM   3309 C  CA  . ILE C 1 151 ? 12.340  -75.832 12.240 1.00 92.23  ? 151 ILE C CA  1 
ATOM   3310 C  C   . ILE C 1 151 ? 11.954  -76.998 13.122 1.00 94.49  ? 151 ILE C C   1 
ATOM   3311 O  O   . ILE C 1 151 ? 12.756  -77.433 13.929 1.00 95.53  ? 151 ILE C O   1 
ATOM   3312 C  CB  . ILE C 1 151 ? 13.373  -76.281 11.206 1.00 94.40  ? 151 ILE C CB  1 
ATOM   3313 C  CG1 . ILE C 1 151 ? 13.818  -75.084 10.374 1.00 93.53  ? 151 ILE C CG1 1 
ATOM   3314 C  CG2 . ILE C 1 151 ? 12.801  -77.378 10.310 1.00 96.76  ? 151 ILE C CG2 1 
ATOM   3315 C  CD1 . ILE C 1 151 ? 14.873  -75.426 9.406  1.00 96.40  ? 151 ILE C CD1 1 
ATOM   3316 N  N   . ALA C 1 152 ? 10.721  -77.480 12.986 1.00 96.59  ? 152 ALA C N   1 
ATOM   3317 C  CA  . ALA C 1 152 ? 10.180  -78.529 13.872 1.00 99.17  ? 152 ALA C CA  1 
ATOM   3318 C  C   . ALA C 1 152 ? 10.166  -79.825 13.121 1.00 104.01 ? 152 ALA C C   1 
ATOM   3319 O  O   . ALA C 1 152 ? 10.258  -79.848 11.853 1.00 105.08 ? 152 ALA C O   1 
ATOM   3320 C  CB  . ALA C 1 152 ? 8.790   -78.215 14.319 1.00 98.26  ? 152 ALA C CB  1 
ATOM   3321 N  N   . GLN C 1 153 ? 10.055  -80.916 13.877 1.00 107.74 ? 153 GLN C N   1 
ATOM   3322 C  CA  . GLN C 1 153 ? 9.971   -82.222 13.207 1.00 113.15 ? 153 GLN C CA  1 
ATOM   3323 C  C   . GLN C 1 153 ? 8.619   -82.402 12.501 1.00 115.08 ? 153 GLN C C   1 
ATOM   3324 O  O   . GLN C 1 153 ? 7.579   -82.109 13.122 1.00 114.53 ? 153 GLN C O   1 
ATOM   3325 C  CB  . GLN C 1 153 ? 10.231  -83.396 14.154 1.00 116.13 ? 153 GLN C CB  1 
ATOM   3326 C  CG  . GLN C 1 153 ? 10.301  -84.739 13.373 1.00 121.18 ? 153 GLN C CG  1 
ATOM   3327 C  CD  . GLN C 1 153 ? 10.948  -85.884 14.177 1.00 125.04 ? 153 GLN C CD  1 
ATOM   3328 O  OE1 . GLN C 1 153 ? 10.688  -86.071 15.375 1.00 125.95 ? 153 GLN C OE1 1 
ATOM   3329 N  NE2 . GLN C 1 153 ? 11.804  -86.648 13.505 1.00 127.99 ? 153 GLN C NE2 1 
ATOM   3330 O  OXT . GLN C 1 153 ? 8.565   -82.829 11.323 1.00 118.13 ? 153 GLN C OXT 1 
ATOM   3331 N  N   . ALA D 1 1   ? 20.389  -64.136 4.045  1.00 110.41 ? 1   ALA D N   1 
ATOM   3332 C  CA  . ALA D 1 1   ? 21.013  -64.228 5.415  1.00 105.87 ? 1   ALA D CA  1 
ATOM   3333 C  C   . ALA D 1 1   ? 22.594  -64.205 5.370  1.00 104.94 ? 1   ALA D C   1 
ATOM   3334 O  O   . ALA D 1 1   ? 23.246  -65.237 5.145  1.00 103.52 ? 1   ALA D O   1 
ATOM   3335 C  CB  . ALA D 1 1   ? 20.473  -65.481 6.143  1.00 101.83 ? 1   ALA D CB  1 
ATOM   3336 N  N   . THR D 1 2   ? 23.177  -63.008 5.525  1.00 106.12 ? 2   THR D N   1 
ATOM   3337 C  CA  . THR D 1 2   ? 24.625  -62.825 5.692  1.00 105.15 ? 2   THR D CA  1 
ATOM   3338 C  C   . THR D 1 2   ? 24.966  -63.208 7.122  1.00 100.03 ? 2   THR D C   1 
ATOM   3339 O  O   . THR D 1 2   ? 25.939  -63.901 7.351  1.00 98.20  ? 2   THR D O   1 
ATOM   3340 C  CB  . THR D 1 2   ? 25.130  -61.312 5.437  1.00 109.58 ? 2   THR D CB  1 
ATOM   3341 O  OG1 . THR D 1 2   ? 25.098  -60.994 4.043  1.00 114.95 ? 2   THR D OG1 1 
ATOM   3342 C  CG2 . THR D 1 2   ? 26.574  -61.074 5.934  1.00 108.80 ? 2   THR D CG2 1 
ATOM   3343 N  N   . LYS D 1 3   ? 24.181  -62.735 8.088  1.00 98.16  ? 3   LYS D N   1 
ATOM   3344 C  CA  . LYS D 1 3   ? 24.516  -62.914 9.503  1.00 94.57  ? 3   LYS D CA  1 
ATOM   3345 C  C   . LYS D 1 3   ? 23.460  -63.688 10.267 1.00 90.85  ? 3   LYS D C   1 
ATOM   3346 O  O   . LYS D 1 3   ? 22.301  -63.742 9.862  1.00 91.81  ? 3   LYS D O   1 
ATOM   3347 C  CB  . LYS D 1 3   ? 24.720  -61.558 10.194 1.00 96.77  ? 3   LYS D CB  1 
ATOM   3348 C  CG  . LYS D 1 3   ? 25.987  -60.846 9.775  1.00 100.96 ? 3   LYS D CG  1 
ATOM   3349 C  CD  . LYS D 1 3   ? 26.244  -59.601 10.622 1.00 104.89 ? 3   LYS D CD  1 
ATOM   3350 C  CE  . LYS D 1 3   ? 27.046  -58.561 9.858  1.00 110.59 ? 3   LYS D CE  1 
ATOM   3351 N  NZ  . LYS D 1 3   ? 26.852  -57.225 10.476 1.00 114.46 ? 3   LYS D NZ  1 
ATOM   3352 N  N   . ALA D 1 4   ? 23.888  -64.283 11.377 1.00 86.79  ? 4   ALA D N   1 
ATOM   3353 C  CA  . ALA D 1 4   ? 22.989  -64.899 12.332 1.00 83.82  ? 4   ALA D CA  1 
ATOM   3354 C  C   . ALA D 1 4   ? 23.566  -64.842 13.759 1.00 81.78  ? 4   ALA D C   1 
ATOM   3355 O  O   . ALA D 1 4   ? 24.721  -64.426 13.975 1.00 82.02  ? 4   ALA D O   1 
ATOM   3356 C  CB  . ALA D 1 4   ? 22.700  -66.313 11.921 1.00 81.81  ? 4   ALA D CB  1 
ATOM   3357 N  N   . VAL D 1 5   ? 22.734  -65.244 14.722 1.00 79.98  ? 5   VAL D N   1 
ATOM   3358 C  CA  . VAL D 1 5   ? 23.081  -65.204 16.135 1.00 78.81  ? 5   VAL D CA  1 
ATOM   3359 C  C   . VAL D 1 5   ? 22.295  -66.257 16.895 1.00 77.39  ? 5   VAL D C   1 
ATOM   3360 O  O   . VAL D 1 5   ? 21.271  -66.722 16.417 1.00 77.27  ? 5   VAL D O   1 
ATOM   3361 C  CB  . VAL D 1 5   ? 22.755  -63.847 16.733 1.00 81.02  ? 5   VAL D CB  1 
ATOM   3362 C  CG1 . VAL D 1 5   ? 21.277  -63.695 16.889 1.00 81.64  ? 5   VAL D CG1 1 
ATOM   3363 C  CG2 . VAL D 1 5   ? 23.406  -63.695 18.059 1.00 80.20  ? 5   VAL D CG2 1 
ATOM   3364 N  N   . CYS D 1 6   ? 22.776  -66.630 18.075 1.00 76.82  ? 6   CYS D N   1 
ATOM   3365 C  CA  . CYS D 1 6   ? 22.109  -67.633 18.886 1.00 76.19  ? 6   CYS D CA  1 
ATOM   3366 C  C   . CYS D 1 6   ? 22.448  -67.449 20.337 1.00 76.94  ? 6   CYS D C   1 
ATOM   3367 O  O   . CYS D 1 6   ? 23.616  -67.410 20.686 1.00 76.84  ? 6   CYS D O   1 
ATOM   3368 C  CB  . CYS D 1 6   ? 22.561  -69.026 18.455 1.00 74.07  ? 6   CYS D CB  1 
ATOM   3369 S  SG  . CYS D 1 6   ? 21.993  -70.352 19.530 1.00 73.71  ? 6   CYS D SG  1 
ATOM   3370 N  N   . VAL D 1 7   ? 21.444  -67.347 21.192 1.00 78.41  ? 7   VAL D N   1 
ATOM   3371 C  CA  . VAL D 1 7   ? 21.703  -67.291 22.628 1.00 80.00  ? 7   VAL D CA  1 
ATOM   3372 C  C   . VAL D 1 7   ? 21.573  -68.664 23.262 1.00 79.62  ? 7   VAL D C   1 
ATOM   3373 O  O   . VAL D 1 7   ? 20.511  -69.297 23.212 1.00 79.82  ? 7   VAL D O   1 
ATOM   3374 C  CB  . VAL D 1 7   ? 20.748  -66.358 23.353 1.00 82.79  ? 7   VAL D CB  1 
ATOM   3375 C  CG1 . VAL D 1 7   ? 21.107  -66.261 24.812 1.00 84.52  ? 7   VAL D CG1 1 
ATOM   3376 C  CG2 . VAL D 1 7   ? 20.800  -65.005 22.728 1.00 84.52  ? 7   VAL D CG2 1 
ATOM   3377 N  N   . LEU D 1 8   ? 22.658  -69.106 23.880 1.00 79.80  ? 8   LEU D N   1 
ATOM   3378 C  CA  . LEU D 1 8   ? 22.694  -70.389 24.541 1.00 79.88  ? 8   LEU D CA  1 
ATOM   3379 C  C   . LEU D 1 8   ? 22.282  -70.247 25.984 1.00 83.65  ? 8   LEU D C   1 
ATOM   3380 O  O   . LEU D 1 8   ? 22.805  -69.397 26.700 1.00 85.29  ? 8   LEU D O   1 
ATOM   3381 C  CB  . LEU D 1 8   ? 24.101  -70.942 24.479 1.00 78.49  ? 8   LEU D CB  1 
ATOM   3382 C  CG  . LEU D 1 8   ? 24.533  -71.317 23.077 1.00 75.21  ? 8   LEU D CG  1 
ATOM   3383 C  CD1 . LEU D 1 8   ? 25.972  -71.584 23.055 1.00 72.91  ? 8   LEU D CD1 1 
ATOM   3384 C  CD2 . LEU D 1 8   ? 23.785  -72.536 22.646 1.00 75.05  ? 8   LEU D CD2 1 
ATOM   3385 N  N   . LYS D 1 9   ? 21.332  -71.079 26.391 1.00 85.87  ? 9   LYS D N   1 
ATOM   3386 C  CA  . LYS D 1 9   ? 20.840  -71.114 27.758 1.00 90.79  ? 9   LYS D CA  1 
ATOM   3387 C  C   . LYS D 1 9   ? 20.583  -72.556 28.089 1.00 91.26  ? 9   LYS D C   1 
ATOM   3388 O  O   . LYS D 1 9   ? 20.491  -73.395 27.202 1.00 89.09  ? 9   LYS D O   1 
ATOM   3389 C  CB  . LYS D 1 9   ? 19.507  -70.367 27.911 1.00 93.72  ? 9   LYS D CB  1 
ATOM   3390 C  CG  . LYS D 1 9   ? 19.558  -68.832 27.710 1.00 98.05  ? 9   LYS D CG  1 
ATOM   3391 C  CD  . LYS D 1 9   ? 19.838  -68.025 29.001 1.00 105.48 ? 9   LYS D CD  1 
ATOM   3392 C  CE  . LYS D 1 9   ? 19.354  -66.563 28.874 1.00 108.97 ? 9   LYS D CE  1 
ATOM   3393 N  NZ  . LYS D 1 9   ? 19.882  -65.696 29.974 1.00 113.83 ? 9   LYS D NZ  1 
ATOM   3394 N  N   . GLY D 1 10  ? 20.426  -72.834 29.373 1.00 95.16  ? 10  GLY D N   1 
ATOM   3395 C  CA  . GLY D 1 10  ? 20.090  -74.177 29.821 1.00 96.52  ? 10  GLY D CA  1 
ATOM   3396 C  C   . GLY D 1 10  ? 19.699  -74.164 31.274 1.00 101.65 ? 10  GLY D C   1 
ATOM   3397 O  O   . GLY D 1 10  ? 19.648  -73.106 31.914 1.00 104.15 ? 10  GLY D O   1 
ATOM   3398 N  N   . ASP D 1 11  ? 19.412  -75.346 31.798 1.00 104.05 ? 11  ASP D N   1 
ATOM   3399 C  CA  . ASP D 1 11  ? 19.167  -75.505 33.233 1.00 109.73 ? 11  ASP D CA  1 
ATOM   3400 C  C   . ASP D 1 11  ? 20.393  -75.107 34.062 1.00 111.11 ? 11  ASP D C   1 
ATOM   3401 O  O   . ASP D 1 11  ? 20.256  -74.490 35.133 1.00 115.12 ? 11  ASP D O   1 
ATOM   3402 C  CB  . ASP D 1 11  ? 18.767  -76.953 33.526 1.00 111.83 ? 11  ASP D CB  1 
ATOM   3403 C  CG  . ASP D 1 11  ? 17.331  -77.256 33.125 1.00 114.85 ? 11  ASP D CG  1 
ATOM   3404 O  OD1 . ASP D 1 11  ? 16.482  -76.312 33.084 1.00 118.62 ? 11  ASP D OD1 1 
ATOM   3405 O  OD2 . ASP D 1 11  ? 17.051  -78.453 32.861 1.00 117.98 ? 11  ASP D OD2 1 
ATOM   3406 N  N   . GLY D 1 12  ? 21.578  -75.428 33.529 1.00 107.86 ? 12  GLY D N   1 
ATOM   3407 C  CA  . GLY D 1 12  ? 22.835  -75.176 34.206 1.00 108.77 ? 12  GLY D CA  1 
ATOM   3408 C  C   . GLY D 1 12  ? 23.093  -73.696 34.417 1.00 109.23 ? 12  GLY D C   1 
ATOM   3409 O  O   . GLY D 1 12  ? 22.237  -72.847 34.166 1.00 109.07 ? 12  GLY D O   1 
ATOM   3410 N  N   . PRO D 1 13  ? 24.293  -73.376 34.892 1.00 109.95 ? 13  PRO D N   1 
ATOM   3411 C  CA  . PRO D 1 13  ? 24.791  -72.003 34.913 1.00 110.07 ? 13  PRO D CA  1 
ATOM   3412 C  C   . PRO D 1 13  ? 25.430  -71.634 33.566 1.00 104.56 ? 13  PRO D C   1 
ATOM   3413 O  O   . PRO D 1 13  ? 25.900  -70.512 33.397 1.00 104.43 ? 13  PRO D O   1 
ATOM   3414 C  CB  . PRO D 1 13  ? 25.869  -72.069 35.991 1.00 114.16 ? 13  PRO D CB  1 
ATOM   3415 C  CG  . PRO D 1 13  ? 26.486  -73.453 35.777 1.00 112.68 ? 13  PRO D CG  1 
ATOM   3416 C  CD  . PRO D 1 13  ? 25.350  -74.347 35.258 1.00 110.69 ? 13  PRO D CD  1 
ATOM   3417 N  N   . VAL D 1 14  ? 25.446  -72.599 32.637 1.00 100.20 ? 14  VAL D N   1 
ATOM   3418 C  CA  . VAL D 1 14  ? 26.082  -72.451 31.346 1.00 95.44  ? 14  VAL D CA  1 
ATOM   3419 C  C   . VAL D 1 14  ? 25.247  -71.501 30.532 1.00 93.70  ? 14  VAL D C   1 
ATOM   3420 O  O   . VAL D 1 14  ? 24.011  -71.562 30.560 1.00 94.25  ? 14  VAL D O   1 
ATOM   3421 C  CB  . VAL D 1 14  ? 26.132  -73.764 30.568 1.00 92.25  ? 14  VAL D CB  1 
ATOM   3422 C  CG1 . VAL D 1 14  ? 27.169  -73.668 29.488 1.00 88.03  ? 14  VAL D CG1 1 
ATOM   3423 C  CG2 . VAL D 1 14  ? 26.418  -74.937 31.500 1.00 95.36  ? 14  VAL D CG2 1 
ATOM   3424 N  N   . GLN D 1 15  ? 25.927  -70.610 29.822 1.00 92.05  ? 15  GLN D N   1 
ATOM   3425 C  CA  . GLN D 1 15  ? 25.260  -69.652 28.963 1.00 90.77  ? 15  GLN D CA  1 
ATOM   3426 C  C   . GLN D 1 15  ? 26.259  -68.814 28.149 1.00 89.01  ? 15  GLN D C   1 
ATOM   3427 O  O   . GLN D 1 15  ? 27.406  -68.596 28.561 1.00 90.28  ? 15  GLN D O   1 
ATOM   3428 C  CB  . GLN D 1 15  ? 24.354  -68.728 29.787 1.00 94.59  ? 15  GLN D CB  1 
ATOM   3429 C  CG  . GLN D 1 15  ? 25.103  -67.675 30.579 1.00 99.29  ? 15  GLN D CG  1 
ATOM   3430 C  CD  . GLN D 1 15  ? 24.205  -66.860 31.486 1.00 105.41 ? 15  GLN D CD  1 
ATOM   3431 O  OE1 . GLN D 1 15  ? 24.701  -66.080 32.305 1.00 110.62 ? 15  GLN D OE1 1 
ATOM   3432 N  NE2 . GLN D 1 15  ? 22.878  -67.018 31.339 1.00 105.25 ? 15  GLN D NE2 1 
ATOM   3433 N  N   . GLY D 1 16  ? 25.799  -68.340 26.998 1.00 86.26  ? 16  GLY D N   1 
ATOM   3434 C  CA  . GLY D 1 16  ? 26.619  -67.513 26.151 1.00 85.18  ? 16  GLY D CA  1 
ATOM   3435 C  C   . GLY D 1 16  ? 25.858  -67.018 24.951 1.00 83.24  ? 16  GLY D C   1 
ATOM   3436 O  O   . GLY D 1 16  ? 24.672  -67.292 24.808 1.00 82.85  ? 16  GLY D O   1 
ATOM   3437 N  N   . ILE D 1 17  ? 26.566  -66.290 24.094 1.00 82.49  ? 17  ILE D N   1 
ATOM   3438 C  CA  . ILE D 1 17  ? 26.045  -65.752 22.838 1.00 81.30  ? 17  ILE D CA  1 
ATOM   3439 C  C   . ILE D 1 17  ? 26.994  -66.119 21.717 1.00 79.26  ? 17  ILE D C   1 
ATOM   3440 O  O   . ILE D 1 17  ? 28.196  -65.975 21.876 1.00 79.91  ? 17  ILE D O   1 
ATOM   3441 C  CB  . ILE D 1 17  ? 26.049  -64.220 22.884 1.00 84.38  ? 17  ILE D CB  1 
ATOM   3442 C  CG1 . ILE D 1 17  ? 25.543  -63.708 24.245 1.00 87.42  ? 17  ILE D CG1 1 
ATOM   3443 C  CG2 . ILE D 1 17  ? 25.285  -63.635 21.684 1.00 84.29  ? 17  ILE D CG2 1 
ATOM   3444 C  CD1 . ILE D 1 17  ? 24.269  -62.942 24.171 1.00 89.84  ? 17  ILE D CD1 1 
ATOM   3445 N  N   . ILE D 1 18  ? 26.493  -66.582 20.587 1.00 77.42  ? 18  ILE D N   1 
ATOM   3446 C  CA  . ILE D 1 18  ? 27.384  -66.963 19.500 1.00 76.79  ? 18  ILE D CA  1 
ATOM   3447 C  C   . ILE D 1 18  ? 26.900  -66.356 18.227 1.00 77.73  ? 18  ILE D C   1 
ATOM   3448 O  O   . ILE D 1 18  ? 25.726  -66.468 17.917 1.00 77.59  ? 18  ILE D O   1 
ATOM   3449 C  CB  . ILE D 1 18  ? 27.402  -68.478 19.267 1.00 74.45  ? 18  ILE D CB  1 
ATOM   3450 C  CG1 . ILE D 1 18  ? 27.931  -69.217 20.477 1.00 74.71  ? 18  ILE D CG1 1 
ATOM   3451 C  CG2 . ILE D 1 18  ? 28.267  -68.827 18.079 1.00 73.28  ? 18  ILE D CG2 1 
ATOM   3452 C  CD1 . ILE D 1 18  ? 29.302  -68.797 20.869 1.00 77.66  ? 18  ILE D CD1 1 
ATOM   3453 N  N   . ASN D 1 19  ? 27.808  -65.761 17.465 1.00 79.57  ? 19  ASN D N   1 
ATOM   3454 C  CA  . ASN D 1 19  ? 27.458  -65.113 16.205 1.00 81.48  ? 19  ASN D CA  1 
ATOM   3455 C  C   . ASN D 1 19  ? 27.913  -65.863 14.988 1.00 81.17  ? 19  ASN D C   1 
ATOM   3456 O  O   . ASN D 1 19  ? 28.843  -66.630 15.041 1.00 80.23  ? 19  ASN D O   1 
ATOM   3457 C  CB  . ASN D 1 19  ? 28.087  -63.739 16.162 1.00 84.67  ? 19  ASN D CB  1 
ATOM   3458 C  CG  . ASN D 1 19  ? 27.625  -62.870 17.296 1.00 86.75  ? 19  ASN D CG  1 
ATOM   3459 O  OD1 . ASN D 1 19  ? 28.291  -62.769 18.322 1.00 88.06  ? 19  ASN D OD1 1 
ATOM   3460 N  ND2 . ASN D 1 19  ? 26.454  -62.268 17.139 1.00 88.24  ? 19  ASN D ND2 1 
ATOM   3461 N  N   . PHE D 1 20  ? 27.266  -65.606 13.871 1.00 83.15  ? 20  PHE D N   1 
ATOM   3462 C  CA  . PHE D 1 20  ? 27.623  -66.254 12.624 1.00 84.19  ? 20  PHE D CA  1 
ATOM   3463 C  C   . PHE D 1 20  ? 27.743  -65.197 11.546 1.00 88.47  ? 20  PHE D C   1 
ATOM   3464 O  O   . PHE D 1 20  ? 27.041  -64.186 11.582 1.00 90.61  ? 20  PHE D O   1 
ATOM   3465 C  CB  . PHE D 1 20  ? 26.546  -67.236 12.210 1.00 82.66  ? 20  PHE D CB  1 
ATOM   3466 C  CG  . PHE D 1 20  ? 26.318  -68.346 13.186 1.00 80.32  ? 20  PHE D CG  1 
ATOM   3467 C  CD1 . PHE D 1 20  ? 25.751  -68.106 14.429 1.00 80.80  ? 20  PHE D CD1 1 
ATOM   3468 C  CD2 . PHE D 1 20  ? 26.627  -69.658 12.847 1.00 78.50  ? 20  PHE D CD2 1 
ATOM   3469 C  CE1 . PHE D 1 20  ? 25.531  -69.162 15.327 1.00 78.77  ? 20  PHE D CE1 1 
ATOM   3470 C  CE2 . PHE D 1 20  ? 26.401  -70.710 13.736 1.00 75.53  ? 20  PHE D CE2 1 
ATOM   3471 C  CZ  . PHE D 1 20  ? 25.865  -70.463 14.971 1.00 75.80  ? 20  PHE D CZ  1 
ATOM   3472 N  N   . GLU D 1 21  ? 28.625  -65.425 10.584 1.00 90.74  ? 21  GLU D N   1 
ATOM   3473 C  CA  . GLU D 1 21  ? 28.733  -64.521 9.459  1.00 95.45  ? 21  GLU D CA  1 
ATOM   3474 C  C   . GLU D 1 21  ? 29.193  -65.283 8.213  1.00 96.74  ? 21  GLU D C   1 
ATOM   3475 O  O   . GLU D 1 21  ? 30.213  -65.960 8.235  1.00 96.43  ? 21  GLU D O   1 
ATOM   3476 C  CB  . GLU D 1 21  ? 29.695  -63.372 9.797  1.00 98.48  ? 21  GLU D CB  1 
ATOM   3477 C  CG  . GLU D 1 21  ? 29.644  -62.186 8.788  1.00 105.48 ? 21  GLU D CG  1 
ATOM   3478 C  CD  . GLU D 1 21  ? 30.601  -61.009 9.144  1.00 111.72 ? 21  GLU D CD  1 
ATOM   3479 O  OE1 . GLU D 1 21  ? 31.743  -61.261 9.598  1.00 113.47 ? 21  GLU D OE1 1 
ATOM   3480 O  OE2 . GLU D 1 21  ? 30.219  -59.828 8.950  1.00 116.45 ? 21  GLU D OE2 1 
ATOM   3481 N  N   . GLN D 1 22  ? 28.423  -65.175 7.138  1.00 99.21  ? 22  GLN D N   1 
ATOM   3482 C  CA  . GLN D 1 22  ? 28.745  -65.809 5.867  1.00 101.63 ? 22  GLN D CA  1 
ATOM   3483 C  C   . GLN D 1 22  ? 28.753  -64.693 4.833  1.00 107.68 ? 22  GLN D C   1 
ATOM   3484 O  O   . GLN D 1 22  ? 27.709  -64.363 4.233  1.00 109.67 ? 22  GLN D O   1 
ATOM   3485 C  CB  . GLN D 1 22  ? 27.712  -66.895 5.513  1.00 99.91  ? 22  GLN D CB  1 
ATOM   3486 C  CG  . GLN D 1 22  ? 28.003  -67.646 4.211  1.00 102.05 ? 22  GLN D CG  1 
ATOM   3487 C  CD  . GLN D 1 22  ? 27.113  -68.890 3.966  1.00 100.29 ? 22  GLN D CD  1 
ATOM   3488 O  OE1 . GLN D 1 22  ? 25.898  -68.879 4.224  1.00 98.53  ? 22  GLN D OE1 1 
ATOM   3489 N  NE2 . GLN D 1 22  ? 27.727  -69.958 3.440  1.00 100.70 ? 22  GLN D NE2 1 
ATOM   3490 N  N   . LYS D 1 23  ? 29.927  -64.089 4.647  1.00 111.45 ? 23  LYS D N   1 
ATOM   3491 C  CA  . LYS D 1 23  ? 30.084  -62.977 3.693  1.00 117.81 ? 23  LYS D CA  1 
ATOM   3492 C  C   . LYS D 1 23  ? 29.790  -63.376 2.254  1.00 121.47 ? 23  LYS D C   1 
ATOM   3493 O  O   . LYS D 1 23  ? 29.274  -62.581 1.501  1.00 125.67 ? 23  LYS D O   1 
ATOM   3494 C  CB  . LYS D 1 23  ? 31.477  -62.353 3.764  1.00 120.73 ? 23  LYS D CB  1 
ATOM   3495 C  CG  . LYS D 1 23  ? 31.579  -61.203 4.792  1.00 122.67 ? 23  LYS D CG  1 
ATOM   3496 C  CD  . LYS D 1 23  ? 33.025  -60.954 5.285  1.00 125.85 ? 23  LYS D CD  1 
ATOM   3497 C  CE  . LYS D 1 23  ? 33.499  -62.067 6.254  1.00 122.61 ? 23  LYS D CE  1 
ATOM   3498 N  NZ  . LYS D 1 23  ? 34.945  -61.940 6.599  1.00 125.28 ? 23  LYS D NZ  1 
ATOM   3499 N  N   . GLU D 1 24  ? 30.105  -64.598 1.866  1.00 120.83 ? 24  GLU D N   1 
ATOM   3500 C  CA  . GLU D 1 24  ? 29.772  -65.050 0.523  1.00 124.91 ? 24  GLU D CA  1 
ATOM   3501 C  C   . GLU D 1 24  ? 28.728  -66.123 0.561  1.00 122.29 ? 24  GLU D C   1 
ATOM   3502 O  O   . GLU D 1 24  ? 28.859  -67.080 1.325  1.00 118.26 ? 24  GLU D O   1 
ATOM   3503 C  CB  . GLU D 1 24  ? 30.999  -65.637 -0.135 1.00 127.69 ? 24  GLU D CB  1 
ATOM   3504 C  CG  . GLU D 1 24  ? 31.953  -64.605 -0.636 1.00 133.67 ? 24  GLU D CG  1 
ATOM   3505 C  CD  . GLU D 1 24  ? 33.124  -65.233 -1.389 1.00 138.15 ? 24  GLU D CD  1 
ATOM   3506 O  OE1 . GLU D 1 24  ? 33.517  -66.415 -1.101 1.00 135.53 ? 24  GLU D OE1 1 
ATOM   3507 O  OE2 . GLU D 1 24  ? 33.648  -64.519 -2.284 1.00 144.61 ? 24  GLU D OE2 1 
ATOM   3508 N  N   . SER D 1 25  ? 27.721  -65.995 -0.291 1.00 125.49 ? 25  SER D N   1 
ATOM   3509 C  CA  . SER D 1 25  ? 26.797  -67.098 -0.532 1.00 124.69 ? 25  SER D CA  1 
ATOM   3510 C  C   . SER D 1 25  ? 27.541  -68.439 -0.801 1.00 123.94 ? 25  SER D C   1 
ATOM   3511 O  O   . SER D 1 25  ? 28.473  -68.501 -1.629 1.00 127.60 ? 25  SER D O   1 
ATOM   3512 C  CB  . SER D 1 25  ? 25.911  -66.781 -1.726 1.00 130.09 ? 25  SER D CB  1 
ATOM   3513 O  OG  . SER D 1 25  ? 25.178  -67.946 -2.085 1.00 130.74 ? 25  SER D OG  1 
ATOM   3514 N  N   . ASN D 1 26  ? 27.144  -69.496 -0.081 1.00 119.53 ? 26  ASN D N   1 
ATOM   3515 C  CA  . ASN D 1 26  ? 27.816  -70.808 -0.170 1.00 118.66 ? 26  ASN D CA  1 
ATOM   3516 C  C   . ASN D 1 26  ? 29.325  -70.789 0.099  1.00 117.54 ? 26  ASN D C   1 
ATOM   3517 O  O   . ASN D 1 26  ? 30.015  -71.761 -0.238 1.00 118.48 ? 26  ASN D O   1 
ATOM   3518 C  CB  . ASN D 1 26  ? 27.575  -71.458 -1.541 1.00 123.84 ? 26  ASN D CB  1 
ATOM   3519 C  CG  . ASN D 1 26  ? 26.136  -71.916 -1.732 1.00 125.33 ? 26  ASN D CG  1 
ATOM   3520 O  OD1 . ASN D 1 26  ? 25.384  -72.165 -0.757 1.00 122.47 ? 26  ASN D OD1 1 
ATOM   3521 N  ND2 . ASN D 1 26  ? 25.736  -72.030 -3.002 1.00 130.76 ? 26  ASN D ND2 1 
ATOM   3522 N  N   . GLY D 1 27  ? 29.824  -69.693 0.690  1.00 115.65 ? 27  GLY D N   1 
ATOM   3523 C  CA  . GLY D 1 27  ? 31.206  -69.592 1.137  1.00 114.13 ? 27  GLY D CA  1 
ATOM   3524 C  C   . GLY D 1 27  ? 31.309  -70.154 2.538  1.00 107.69 ? 27  GLY D C   1 
ATOM   3525 O  O   . GLY D 1 27  ? 30.411  -70.875 2.981  1.00 104.53 ? 27  GLY D O   1 
ATOM   3526 N  N   . PRO D 1 28  ? 32.397  -69.821 3.253  1.00 105.61 ? 28  PRO D N   1 
ATOM   3527 C  CA  . PRO D 1 28  ? 32.596  -70.318 4.599  1.00 100.32 ? 28  PRO D CA  1 
ATOM   3528 C  C   . PRO D 1 28  ? 31.863  -69.404 5.569  1.00 97.06  ? 28  PRO D C   1 
ATOM   3529 O  O   . PRO D 1 28  ? 31.392  -68.334 5.169  1.00 99.00  ? 28  PRO D O   1 
ATOM   3530 C  CB  . PRO D 1 28  ? 34.110  -70.196 4.782  1.00 101.68 ? 28  PRO D CB  1 
ATOM   3531 C  CG  . PRO D 1 28  ? 34.434  -68.914 4.071  1.00 106.19 ? 28  PRO D CG  1 
ATOM   3532 C  CD  . PRO D 1 28  ? 33.395  -68.787 2.931  1.00 109.08 ? 28  PRO D CD  1 
ATOM   3533 N  N   . VAL D 1 29  ? 31.815  -69.825 6.828  1.00 92.31  ? 29  VAL D N   1 
ATOM   3534 C  CA  . VAL D 1 29  ? 31.009  -69.198 7.856  1.00 89.57  ? 29  VAL D CA  1 
ATOM   3535 C  C   . VAL D 1 29  ? 31.810  -68.957 9.127  1.00 88.06  ? 29  VAL D C   1 
ATOM   3536 O  O   . VAL D 1 29  ? 32.128  -69.909 9.824  1.00 86.13  ? 29  VAL D O   1 
ATOM   3537 C  CB  . VAL D 1 29  ? 29.864  -70.137 8.280  1.00 86.53  ? 29  VAL D CB  1 
ATOM   3538 C  CG1 . VAL D 1 29  ? 29.104  -69.533 9.436  1.00 83.93  ? 29  VAL D CG1 1 
ATOM   3539 C  CG2 . VAL D 1 29  ? 28.950  -70.458 7.114  1.00 88.20  ? 29  VAL D CG2 1 
ATOM   3540 N  N   . LYS D 1 30  ? 32.125  -67.707 9.459  1.00 89.62  ? 30  LYS D N   1 
ATOM   3541 C  CA  . LYS D 1 30  ? 32.822  -67.442 10.720 1.00 88.94  ? 30  LYS D CA  1 
ATOM   3542 C  C   . LYS D 1 30  ? 31.846  -67.541 11.840 1.00 85.61  ? 30  LYS D C   1 
ATOM   3543 O  O   . LYS D 1 30  ? 30.801  -66.930 11.795 1.00 85.94  ? 30  LYS D O   1 
ATOM   3544 C  CB  . LYS D 1 30  ? 33.501  -66.067 10.777 1.00 92.59  ? 30  LYS D CB  1 
ATOM   3545 C  CG  . LYS D 1 30  ? 34.952  -66.077 10.251 1.00 97.95  ? 30  LYS D CG  1 
ATOM   3546 C  CD  . LYS D 1 30  ? 35.426  -64.717 9.644  1.00 105.23 ? 30  LYS D CD  1 
ATOM   3547 C  CE  . LYS D 1 30  ? 35.770  -64.843 8.104  1.00 109.35 ? 30  LYS D CE  1 
ATOM   3548 N  NZ  . LYS D 1 30  ? 37.071  -64.197 7.721  1.00 114.04 ? 30  LYS D NZ  1 
ATOM   3549 N  N   . VAL D 1 31  ? 32.212  -68.313 12.847 1.00 83.20  ? 31  VAL D N   1 
ATOM   3550 C  CA  . VAL D 1 31  ? 31.402  -68.521 14.015 1.00 80.76  ? 31  VAL D CA  1 
ATOM   3551 C  C   . VAL D 1 31  ? 32.196  -68.043 15.194 1.00 81.94  ? 31  VAL D C   1 
ATOM   3552 O  O   . VAL D 1 31  ? 33.250  -68.576 15.467 1.00 82.33  ? 31  VAL D O   1 
ATOM   3553 C  CB  . VAL D 1 31  ? 31.135  -70.013 14.207 1.00 78.06  ? 31  VAL D CB  1 
ATOM   3554 C  CG1 . VAL D 1 31  ? 30.339  -70.263 15.470 1.00 75.37  ? 31  VAL D CG1 1 
ATOM   3555 C  CG2 . VAL D 1 31  ? 30.453  -70.555 12.998 1.00 77.34  ? 31  VAL D CG2 1 
ATOM   3556 N  N   . TRP D 1 32  ? 31.718  -67.056 15.917 1.00 83.43  ? 32  TRP D N   1 
ATOM   3557 C  CA  . TRP D 1 32  ? 32.439  -66.669 17.113 1.00 85.34  ? 32  TRP D CA  1 
ATOM   3558 C  C   . TRP D 1 32  ? 31.554  -66.079 18.193 1.00 84.85  ? 32  TRP D C   1 
ATOM   3559 O  O   . TRP D 1 32  ? 30.460  -65.591 17.962 1.00 84.60  ? 32  TRP D O   1 
ATOM   3560 C  CB  . TRP D 1 32  ? 33.568  -65.694 16.760 1.00 89.33  ? 32  TRP D CB  1 
ATOM   3561 C  CG  . TRP D 1 32  ? 33.128  -64.299 16.812 1.00 95.42  ? 32  TRP D CG  1 
ATOM   3562 C  CD1 . TRP D 1 32  ? 33.360  -63.399 17.813 1.00 100.86 ? 32  TRP D CD1 1 
ATOM   3563 C  CD2 . TRP D 1 32  ? 32.312  -63.632 15.839 1.00 100.40 ? 32  TRP D CD2 1 
ATOM   3564 N  NE1 . TRP D 1 32  ? 32.744  -62.198 17.523 1.00 105.23 ? 32  TRP D NE1 1 
ATOM   3565 C  CE2 . TRP D 1 32  ? 32.093  -62.308 16.318 1.00 104.82 ? 32  TRP D CE2 1 
ATOM   3566 C  CE3 . TRP D 1 32  ? 31.740  -64.023 14.601 1.00 100.34 ? 32  TRP D CE3 1 
ATOM   3567 C  CZ2 . TRP D 1 32  ? 31.323  -61.357 15.599 1.00 107.57 ? 32  TRP D CZ2 1 
ATOM   3568 C  CZ3 . TRP D 1 32  ? 30.968  -63.081 13.878 1.00 103.26 ? 32  TRP D CZ3 1 
ATOM   3569 C  CH2 . TRP D 1 32  ? 30.772  -61.759 14.386 1.00 106.82 ? 32  TRP D CH2 1 
ATOM   3570 N  N   . GLY D 1 33  ? 32.068  -66.117 19.397 1.00 85.26  ? 33  GLY D N   1 
ATOM   3571 C  CA  . GLY D 1 33  ? 31.359  -65.577 20.521 1.00 86.15  ? 33  GLY D CA  1 
ATOM   3572 C  C   . GLY D 1 33  ? 31.991  -66.096 21.776 1.00 86.47  ? 33  GLY D C   1 
ATOM   3573 O  O   . GLY D 1 33  ? 33.179  -66.404 21.807 1.00 87.45  ? 33  GLY D O   1 
ATOM   3574 N  N   . SER D 1 34  ? 31.191  -66.221 22.814 1.00 86.18  ? 34  SER D N   1 
ATOM   3575 C  CA  . SER D 1 34  ? 31.737  -66.571 24.093 1.00 87.57  ? 34  SER D CA  1 
ATOM   3576 C  C   . SER D 1 34  ? 30.741  -67.280 24.971 1.00 86.60  ? 34  SER D C   1 
ATOM   3577 O  O   . SER D 1 34  ? 29.600  -66.848 25.048 1.00 86.93  ? 34  SER D O   1 
ATOM   3578 C  CB  . SER D 1 34  ? 32.153  -65.310 24.795 1.00 91.41  ? 34  SER D CB  1 
ATOM   3579 O  OG  . SER D 1 34  ? 32.742  -65.678 26.015 1.00 94.15  ? 34  SER D OG  1 
ATOM   3580 N  N   . ILE D 1 35  ? 31.171  -68.345 25.644 1.00 86.07  ? 35  ILE D N   1 
ATOM   3581 C  CA  . ILE D 1 35  ? 30.295  -69.072 26.559 1.00 86.15  ? 35  ILE D CA  1 
ATOM   3582 C  C   . ILE D 1 35  ? 30.933  -69.101 27.916 1.00 89.59  ? 35  ILE D C   1 
ATOM   3583 O  O   . ILE D 1 35  ? 32.144  -69.186 27.990 1.00 90.86  ? 35  ILE D O   1 
ATOM   3584 C  CB  . ILE D 1 35  ? 30.097  -70.517 26.133 1.00 83.26  ? 35  ILE D CB  1 
ATOM   3585 C  CG1 . ILE D 1 35  ? 29.802  -70.603 24.645 1.00 80.37  ? 35  ILE D CG1 1 
ATOM   3586 C  CG2 . ILE D 1 35  ? 28.951  -71.144 26.906 1.00 83.46  ? 35  ILE D CG2 1 
ATOM   3587 C  CD1 . ILE D 1 35  ? 29.574  -71.990 24.191 1.00 78.30  ? 35  ILE D CD1 1 
ATOM   3588 N  N   . LYS D 1 36  ? 30.137  -69.047 28.983 1.00 91.90  ? 36  LYS D N   1 
ATOM   3589 C  CA  . LYS D 1 36  ? 30.693  -69.127 30.333 1.00 96.17  ? 36  LYS D CA  1 
ATOM   3590 C  C   . LYS D 1 36  ? 29.962  -70.142 31.176 1.00 96.63  ? 36  LYS D C   1 
ATOM   3591 O  O   . LYS D 1 36  ? 28.864  -70.553 30.826 1.00 94.66  ? 36  LYS D O   1 
ATOM   3592 C  CB  . LYS D 1 36  ? 30.678  -67.754 31.012 1.00 100.65 ? 36  LYS D CB  1 
ATOM   3593 C  CG  . LYS D 1 36  ? 29.368  -66.943 30.860 1.00 102.84 ? 36  LYS D CG  1 
ATOM   3594 C  CD  . LYS D 1 36  ? 29.434  -65.620 31.687 1.00 109.85 ? 36  LYS D CD  1 
ATOM   3595 C  CE  . LYS D 1 36  ? 28.048  -65.096 32.135 1.00 111.95 ? 36  LYS D CE  1 
ATOM   3596 N  NZ  . LYS D 1 36  ? 28.215  -63.876 33.015 1.00 117.22 ? 36  LYS D NZ  1 
ATOM   3597 N  N   . GLY D 1 37  ? 30.580  -70.544 32.285 1.00 99.99  ? 37  GLY D N   1 
ATOM   3598 C  CA  . GLY D 1 37  ? 29.989  -71.549 33.196 1.00 101.82 ? 37  GLY D CA  1 
ATOM   3599 C  C   . GLY D 1 37  ? 30.302  -73.011 32.841 1.00 99.54  ? 37  GLY D C   1 
ATOM   3600 O  O   . GLY D 1 37  ? 29.512  -73.947 33.104 1.00 99.45  ? 37  GLY D O   1 
ATOM   3601 N  N   . LEU D 1 38  ? 31.469  -73.217 32.249 1.00 98.01  ? 38  LEU D N   1 
ATOM   3602 C  CA  . LEU D 1 38  ? 31.839  -74.528 31.738 1.00 95.92  ? 38  LEU D CA  1 
ATOM   3603 C  C   . LEU D 1 38  ? 32.909  -75.102 32.607 1.00 99.19  ? 38  LEU D C   1 
ATOM   3604 O  O   . LEU D 1 38  ? 33.670  -74.351 33.219 1.00 102.33 ? 38  LEU D O   1 
ATOM   3605 C  CB  . LEU D 1 38  ? 32.373  -74.395 30.304 1.00 92.23  ? 38  LEU D CB  1 
ATOM   3606 C  CG  . LEU D 1 38  ? 31.257  -74.220 29.278 1.00 88.56  ? 38  LEU D CG  1 
ATOM   3607 C  CD1 . LEU D 1 38  ? 31.729  -73.441 28.080 1.00 85.77  ? 38  LEU D CD1 1 
ATOM   3608 C  CD2 . LEU D 1 38  ? 30.734  -75.573 28.883 1.00 87.10  ? 38  LEU D CD2 1 
ATOM   3609 N  N   . THR D 1 39  ? 32.992  -76.425 32.648 1.00 98.87  ? 39  THR D N   1 
ATOM   3610 C  CA  . THR D 1 39  ? 34.139  -77.066 33.281 1.00 102.02 ? 39  THR D CA  1 
ATOM   3611 C  C   . THR D 1 39  ? 35.350  -76.831 32.402 1.00 100.71 ? 39  THR D C   1 
ATOM   3612 O  O   . THR D 1 39  ? 35.245  -76.925 31.198 1.00 96.82  ? 39  THR D O   1 
ATOM   3613 C  CB  . THR D 1 39  ? 33.903  -78.555 33.454 1.00 102.46 ? 39  THR D CB  1 
ATOM   3614 O  OG1 . THR D 1 39  ? 32.857  -78.953 32.553 1.00 98.37  ? 39  THR D OG1 1 
ATOM   3615 C  CG2 . THR D 1 39  ? 33.489  -78.876 34.920 1.00 107.21 ? 39  THR D CG2 1 
ATOM   3616 N  N   . GLU D 1 40  ? 36.488  -76.485 32.995 1.00 104.82 ? 40  GLU D N   1 
ATOM   3617 C  CA  . GLU D 1 40  ? 37.723  -76.303 32.224 1.00 104.71 ? 40  GLU D CA  1 
ATOM   3618 C  C   . GLU D 1 40  ? 37.879  -77.470 31.241 1.00 101.74 ? 40  GLU D C   1 
ATOM   3619 O  O   . GLU D 1 40  ? 37.527  -78.629 31.563 1.00 102.20 ? 40  GLU D O   1 
ATOM   3620 C  CB  . GLU D 1 40  ? 38.964  -76.245 33.143 1.00 110.15 ? 40  GLU D CB  1 
ATOM   3621 C  CG  . GLU D 1 40  ? 40.348  -76.306 32.378 1.00 111.30 ? 40  GLU D CG  1 
ATOM   3622 C  CD  . GLU D 1 40  ? 41.535  -75.659 33.155 1.00 118.29 ? 40  GLU D CD  1 
ATOM   3623 O  OE1 . GLU D 1 40  ? 41.713  -75.991 34.355 1.00 123.68 ? 40  GLU D OE1 1 
ATOM   3624 O  OE2 . GLU D 1 40  ? 42.289  -74.823 32.573 1.00 118.99 ? 40  GLU D OE2 1 
ATOM   3625 N  N   . GLY D 1 41  ? 38.388  -77.158 30.045 1.00 99.09  ? 41  GLY D N   1 
ATOM   3626 C  CA  . GLY D 1 41  ? 38.676  -78.191 29.045 1.00 96.68  ? 41  GLY D CA  1 
ATOM   3627 C  C   . GLY D 1 41  ? 37.727  -78.215 27.860 1.00 92.12  ? 41  GLY D C   1 
ATOM   3628 O  O   . GLY D 1 41  ? 37.086  -77.195 27.520 1.00 90.61  ? 41  GLY D O   1 
ATOM   3629 N  N   . LEU D 1 42  ? 37.645  -79.375 27.211 1.00 90.28  ? 42  LEU D N   1 
ATOM   3630 C  CA  . LEU D 1 42  ? 36.930  -79.473 25.936 1.00 86.54  ? 42  LEU D CA  1 
ATOM   3631 C  C   . LEU D 1 42  ? 35.448  -79.715 26.141 1.00 84.51  ? 42  LEU D C   1 
ATOM   3632 O  O   . LEU D 1 42  ? 35.042  -80.364 27.115 1.00 86.37  ? 42  LEU D O   1 
ATOM   3633 C  CB  . LEU D 1 42  ? 37.496  -80.577 25.053 1.00 86.25  ? 42  LEU D CB  1 
ATOM   3634 C  CG  . LEU D 1 42  ? 38.829  -80.277 24.391 1.00 87.69  ? 42  LEU D CG  1 
ATOM   3635 C  CD1 . LEU D 1 42  ? 39.972  -81.067 25.081 1.00 92.10  ? 42  LEU D CD1 1 
ATOM   3636 C  CD2 . LEU D 1 42  ? 38.733  -80.603 22.908 1.00 85.06  ? 42  LEU D CD2 1 
ATOM   3637 N  N   . HIS D 1 43  ? 34.652  -79.191 25.212 1.00 80.90  ? 43  HIS D N   1 
ATOM   3638 C  CA  . HIS D 1 43  ? 33.230  -79.443 25.200 1.00 78.92  ? 43  HIS D CA  1 
ATOM   3639 C  C   . HIS D 1 43  ? 32.696  -79.524 23.794 1.00 75.80  ? 43  HIS D C   1 
ATOM   3640 O  O   . HIS D 1 43  ? 33.020  -78.712 22.946 1.00 74.34  ? 43  HIS D O   1 
ATOM   3641 C  CB  . HIS D 1 43  ? 32.516  -78.336 25.913 1.00 79.31  ? 43  HIS D CB  1 
ATOM   3642 C  CG  . HIS D 1 43  ? 32.742  -78.329 27.382 1.00 82.96  ? 43  HIS D CG  1 
ATOM   3643 N  ND1 . HIS D 1 43  ? 31.901  -78.978 28.261 1.00 85.84  ? 43  HIS D ND1 1 
ATOM   3644 C  CD2 . HIS D 1 43  ? 33.699  -77.738 28.134 1.00 86.15  ? 43  HIS D CD2 1 
ATOM   3645 C  CE1 . HIS D 1 43  ? 32.325  -78.781 29.497 1.00 90.06  ? 43  HIS D CE1 1 
ATOM   3646 N  NE2 . HIS D 1 43  ? 33.418  -78.037 29.447 1.00 90.44  ? 43  HIS D NE2 1 
ATOM   3647 N  N   . GLY D 1 44  ? 31.862  -80.519 23.560 1.00 75.06  ? 44  GLY D N   1 
ATOM   3648 C  CA  . GLY D 1 44  ? 31.262  -80.732 22.257 1.00 73.25  ? 44  GLY D CA  1 
ATOM   3649 C  C   . GLY D 1 44  ? 30.337  -79.614 21.871 1.00 71.63  ? 44  GLY D C   1 
ATOM   3650 O  O   . GLY D 1 44  ? 29.759  -78.971 22.719 1.00 71.99  ? 44  GLY D O   1 
ATOM   3651 N  N   . PHE D 1 45  ? 30.175  -79.419 20.574 1.00 70.48  ? 45  PHE D N   1 
ATOM   3652 C  CA  . PHE D 1 45  ? 29.576  -78.214 20.051 1.00 69.58  ? 45  PHE D CA  1 
ATOM   3653 C  C   . PHE D 1 45  ? 28.995  -78.523 18.686 1.00 68.89  ? 45  PHE D C   1 
ATOM   3654 O  O   . PHE D 1 45  ? 29.745  -78.715 17.717 1.00 68.47  ? 45  PHE D O   1 
ATOM   3655 C  CB  . PHE D 1 45  ? 30.685  -77.176 19.936 1.00 70.05  ? 45  PHE D CB  1 
ATOM   3656 C  CG  . PHE D 1 45  ? 30.224  -75.774 19.615 1.00 70.00  ? 45  PHE D CG  1 
ATOM   3657 C  CD1 . PHE D 1 45  ? 29.456  -75.067 20.506 1.00 70.58  ? 45  PHE D CD1 1 
ATOM   3658 C  CD2 . PHE D 1 45  ? 30.640  -75.141 18.447 1.00 70.11  ? 45  PHE D CD2 1 
ATOM   3659 C  CE1 . PHE D 1 45  ? 29.083  -73.790 20.222 1.00 71.14  ? 45  PHE D CE1 1 
ATOM   3660 C  CE2 . PHE D 1 45  ? 30.266  -73.871 18.169 1.00 70.17  ? 45  PHE D CE2 1 
ATOM   3661 C  CZ  . PHE D 1 45  ? 29.488  -73.196 19.054 1.00 71.00  ? 45  PHE D CZ  1 
ATOM   3662 N  N   . HIS D 1 46  ? 27.661  -78.569 18.616 1.00 68.89  ? 46  HIS D N   1 
ATOM   3663 C  CA  . HIS D 1 46  ? 26.981  -79.001 17.410 1.00 69.37  ? 46  HIS D CA  1 
ATOM   3664 C  C   . HIS D 1 46  ? 25.728  -78.242 17.115 1.00 68.96  ? 46  HIS D C   1 
ATOM   3665 O  O   . HIS D 1 46  ? 25.072  -77.748 18.022 1.00 68.88  ? 46  HIS D O   1 
ATOM   3666 C  CB  . HIS D 1 46  ? 26.567  -80.452 17.553 1.00 70.76  ? 46  HIS D CB  1 
ATOM   3667 C  CG  . HIS D 1 46  ? 27.605  -81.299 18.195 1.00 73.36  ? 46  HIS D CG  1 
ATOM   3668 N  ND1 . HIS D 1 46  ? 27.402  -81.935 19.400 1.00 76.33  ? 46  HIS D ND1 1 
ATOM   3669 C  CD2 . HIS D 1 46  ? 28.880  -81.575 17.820 1.00 76.00  ? 46  HIS D CD2 1 
ATOM   3670 C  CE1 . HIS D 1 46  ? 28.507  -82.584 19.730 1.00 78.83  ? 46  HIS D CE1 1 
ATOM   3671 N  NE2 . HIS D 1 46  ? 29.418  -82.383 18.789 1.00 77.73  ? 46  HIS D NE2 1 
ATOM   3672 N  N   . VAL D 1 47  ? 25.393  -78.201 15.828 1.00 69.30  ? 47  VAL D N   1 
ATOM   3673 C  CA  . VAL D 1 47  ? 24.070  -77.828 15.385 1.00 69.80  ? 47  VAL D CA  1 
ATOM   3674 C  C   . VAL D 1 47  ? 23.276  -79.101 15.342 1.00 71.16  ? 47  VAL D C   1 
ATOM   3675 O  O   . VAL D 1 47  ? 23.675  -80.049 14.686 1.00 72.13  ? 47  VAL D O   1 
ATOM   3676 C  CB  . VAL D 1 47  ? 24.076  -77.252 13.978 1.00 70.19  ? 47  VAL D CB  1 
ATOM   3677 C  CG1 . VAL D 1 47  ? 22.706  -76.890 13.592 1.00 71.22  ? 47  VAL D CG1 1 
ATOM   3678 C  CG2 . VAL D 1 47  ? 24.904  -76.050 13.927 1.00 69.47  ? 47  VAL D CG2 1 
ATOM   3679 N  N   . HIS D 1 48  ? 22.159  -79.130 16.039 1.00 72.19  ? 48  HIS D N   1 
ATOM   3680 C  CA  . HIS D 1 48  ? 21.269  -80.269 15.975 1.00 74.53  ? 48  HIS D CA  1 
ATOM   3681 C  C   . HIS D 1 48  ? 20.118  -79.942 15.034 1.00 76.02  ? 48  HIS D C   1 
ATOM   3682 O  O   . HIS D 1 48  ? 19.904  -78.778 14.696 1.00 75.63  ? 48  HIS D O   1 
ATOM   3683 C  CB  . HIS D 1 48  ? 20.725  -80.578 17.353 1.00 75.52  ? 48  HIS D CB  1 
ATOM   3684 C  CG  . HIS D 1 48  ? 21.749  -81.122 18.294 1.00 76.39  ? 48  HIS D CG  1 
ATOM   3685 N  ND1 . HIS D 1 48  ? 21.561  -82.293 19.000 1.00 79.21  ? 48  HIS D ND1 1 
ATOM   3686 C  CD2 . HIS D 1 48  ? 22.966  -80.651 18.654 1.00 76.47  ? 48  HIS D CD2 1 
ATOM   3687 C  CE1 . HIS D 1 48  ? 22.618  -82.514 19.758 1.00 80.04  ? 48  HIS D CE1 1 
ATOM   3688 N  NE2 . HIS D 1 48  ? 23.485  -81.532 19.569 1.00 77.81  ? 48  HIS D NE2 1 
ATOM   3689 N  N   . GLU D 1 49  ? 19.348  -80.959 14.657 1.00 78.32  ? 49  GLU D N   1 
ATOM   3690 C  CA  . GLU D 1 49  ? 18.377  -80.843 13.569 1.00 80.55  ? 49  GLU D CA  1 
ATOM   3691 C  C   . GLU D 1 49  ? 17.271  -79.812 13.793 1.00 80.78  ? 49  GLU D C   1 
ATOM   3692 O  O   . GLU D 1 49  ? 16.927  -79.098 12.873 1.00 81.06  ? 49  GLU D O   1 
ATOM   3693 C  CB  . GLU D 1 49  ? 17.736  -82.204 13.281 1.00 83.65  ? 49  GLU D CB  1 
ATOM   3694 C  CG  . GLU D 1 49  ? 17.055  -82.289 11.921 1.00 87.78  ? 49  GLU D CG  1 
ATOM   3695 C  CD  . GLU D 1 49  ? 16.664  -83.712 11.528 1.00 93.37  ? 49  GLU D CD  1 
ATOM   3696 O  OE1 . GLU D 1 49  ? 17.233  -84.698 12.065 1.00 95.08  ? 49  GLU D OE1 1 
ATOM   3697 O  OE2 . GLU D 1 49  ? 15.775  -83.831 10.658 1.00 98.09  ? 49  GLU D OE2 1 
ATOM   3698 N  N   . PHE D 1 50  ? 16.717  -79.731 14.998 1.00 80.98  ? 50  PHE D N   1 
ATOM   3699 C  CA  . PHE D 1 50  ? 15.477  -78.965 15.205 1.00 82.78  ? 50  PHE D CA  1 
ATOM   3700 C  C   . PHE D 1 50  ? 15.554  -77.749 16.105 1.00 81.37  ? 50  PHE D C   1 
ATOM   3701 O  O   . PHE D 1 50  ? 16.266  -77.740 17.100 1.00 79.83  ? 50  PHE D O   1 
ATOM   3702 C  CB  . PHE D 1 50  ? 14.393  -79.871 15.773 1.00 85.57  ? 50  PHE D CB  1 
ATOM   3703 C  CG  . PHE D 1 50  ? 14.138  -81.085 14.943 1.00 89.04  ? 50  PHE D CG  1 
ATOM   3704 C  CD1 . PHE D 1 50  ? 13.993  -80.990 13.554 1.00 91.10  ? 50  PHE D CD1 1 
ATOM   3705 C  CD2 . PHE D 1 50  ? 14.033  -82.325 15.541 1.00 92.11  ? 50  PHE D CD2 1 
ATOM   3706 C  CE1 . PHE D 1 50  ? 13.747  -82.114 12.776 1.00 94.20  ? 50  PHE D CE1 1 
ATOM   3707 C  CE2 . PHE D 1 50  ? 13.795  -83.454 14.776 1.00 95.26  ? 50  PHE D CE2 1 
ATOM   3708 C  CZ  . PHE D 1 50  ? 13.652  -83.344 13.380 1.00 96.27  ? 50  PHE D CZ  1 
ATOM   3709 N  N   . GLY D 1 51  ? 14.763  -76.742 15.754 1.00 82.46  ? 51  GLY D N   1 
ATOM   3710 C  CA  . GLY D 1 51  ? 14.617  -75.550 16.556 1.00 82.58  ? 51  GLY D CA  1 
ATOM   3711 C  C   . GLY D 1 51  ? 13.520  -75.768 17.573 1.00 85.06  ? 51  GLY D C   1 
ATOM   3712 O  O   . GLY D 1 51  ? 12.655  -74.926 17.790 1.00 86.68  ? 51  GLY D O   1 
ATOM   3713 N  N   . ASP D 1 52  ? 13.560  -76.915 18.215 1.00 85.95  ? 52  ASP D N   1 
ATOM   3714 C  CA  . ASP D 1 52  ? 12.541  -77.275 19.158 1.00 88.96  ? 52  ASP D CA  1 
ATOM   3715 C  C   . ASP D 1 52  ? 13.153  -77.132 20.523 1.00 88.46  ? 52  ASP D C   1 
ATOM   3716 O  O   . ASP D 1 52  ? 14.229  -77.653 20.780 1.00 86.83  ? 52  ASP D O   1 
ATOM   3717 C  CB  . ASP D 1 52  ? 12.161  -78.720 18.900 1.00 90.84  ? 52  ASP D CB  1 
ATOM   3718 C  CG  . ASP D 1 52  ? 10.747  -79.011 19.238 1.00 94.97  ? 52  ASP D CG  1 
ATOM   3719 O  OD1 . ASP D 1 52  ? 10.351  -78.647 20.379 1.00 96.08  ? 52  ASP D OD1 1 
ATOM   3720 O  OD2 . ASP D 1 52  ? 10.077  -79.621 18.345 1.00 97.86  ? 52  ASP D OD2 1 
ATOM   3721 N  N   . ASN D 1 53  ? 12.499  -76.393 21.392 1.00 90.61  ? 53  ASN D N   1 
ATOM   3722 C  CA  . ASN D 1 53  ? 12.942  -76.316 22.782 1.00 91.64  ? 53  ASN D CA  1 
ATOM   3723 C  C   . ASN D 1 53  ? 11.791  -76.582 23.708 1.00 95.20  ? 53  ASN D C   1 
ATOM   3724 O  O   . ASN D 1 53  ? 11.802  -76.124 24.864 1.00 96.71  ? 53  ASN D O   1 
ATOM   3725 C  CB  . ASN D 1 53  ? 13.541  -74.946 23.096 1.00 90.93  ? 53  ASN D CB  1 
ATOM   3726 C  CG  . ASN D 1 53  ? 15.050  -74.905 22.906 1.00 90.73  ? 53  ASN D CG  1 
ATOM   3727 O  OD1 . ASN D 1 53  ? 15.760  -74.366 23.768 1.00 95.66  ? 53  ASN D OD1 1 
ATOM   3728 N  ND2 . ASN D 1 53  ? 15.556  -75.456 21.758 1.00 89.55  ? 53  ASN D ND2 1 
ATOM   3729 N  N   . THR D 1 54  ? 10.794  -77.298 23.165 1.00 96.91  ? 54  THR D N   1 
ATOM   3730 C  CA  . THR D 1 54  ? 9.564   -77.671 23.869 1.00 101.12 ? 54  THR D CA  1 
ATOM   3731 C  C   . THR D 1 54  ? 9.875   -78.269 25.216 1.00 102.87 ? 54  THR D C   1 
ATOM   3732 O  O   . THR D 1 54  ? 9.381   -77.807 26.239 1.00 105.70 ? 54  THR D O   1 
ATOM   3733 C  CB  . THR D 1 54  ? 8.780   -78.718 23.056 1.00 102.84 ? 54  THR D CB  1 
ATOM   3734 O  OG1 . THR D 1 54  ? 8.463   -78.161 21.787 1.00 101.53 ? 54  THR D OG1 1 
ATOM   3735 C  CG2 . THR D 1 54  ? 7.497   -79.138 23.758 1.00 108.54 ? 54  THR D CG2 1 
ATOM   3736 N  N   . ALA D 1 55  ? 10.714  -79.299 25.188 1.00 101.70 ? 55  ALA D N   1 
ATOM   3737 C  CA  . ALA D 1 55  ? 11.170  -79.987 26.390 1.00 103.72 ? 55  ALA D CA  1 
ATOM   3738 C  C   . ALA D 1 55  ? 12.681  -79.757 26.597 1.00 100.60 ? 55  ALA D C   1 
ATOM   3739 O  O   . ALA D 1 55  ? 13.489  -80.678 26.429 1.00 99.32  ? 55  ALA D O   1 
ATOM   3740 C  CB  . ALA D 1 55  ? 10.855  -81.482 26.279 1.00 105.84 ? 55  ALA D CB  1 
ATOM   3741 N  N   . GLY D 1 56  ? 13.056  -78.523 26.944 1.00 100.01 ? 56  GLY D N   1 
ATOM   3742 C  CA  . GLY D 1 56  ? 14.467  -78.153 27.094 1.00 97.52  ? 56  GLY D CA  1 
ATOM   3743 C  C   . GLY D 1 56  ? 15.284  -78.468 25.839 1.00 93.99  ? 56  GLY D C   1 
ATOM   3744 O  O   . GLY D 1 56  ? 14.803  -78.335 24.696 1.00 92.81  ? 56  GLY D O   1 
ATOM   3745 N  N   . CYS D 1 57  ? 16.522  -78.903 26.044 1.00 92.64  ? 57  CYS D N   1 
ATOM   3746 C  CA  . CYS D 1 57  ? 17.415  -79.137 24.923 1.00 89.63  ? 57  CYS D CA  1 
ATOM   3747 C  C   . CYS D 1 57  ? 17.198  -80.462 24.223 1.00 89.59  ? 57  CYS D C   1 
ATOM   3748 O  O   . CYS D 1 57  ? 17.592  -80.595 23.076 1.00 87.41  ? 57  CYS D O   1 
ATOM   3749 C  CB  . CYS D 1 57  ? 18.870  -78.969 25.357 1.00 88.11  ? 57  CYS D CB  1 
ATOM   3750 S  SG  . CYS D 1 57  ? 19.244  -77.218 25.818 1.00 90.28  ? 57  CYS D SG  1 
ATOM   3751 N  N   . THR D 1 58  ? 16.560  -81.427 24.887 1.00 92.63  ? 58  THR D N   1 
ATOM   3752 C  CA  . THR D 1 58  ? 16.319  -82.769 24.288 1.00 93.64  ? 58  THR D CA  1 
ATOM   3753 C  C   . THR D 1 58  ? 15.448  -82.715 23.024 1.00 93.33  ? 58  THR D C   1 
ATOM   3754 O  O   . THR D 1 58  ? 15.582  -83.560 22.131 1.00 93.18  ? 58  THR D O   1 
ATOM   3755 C  CB  . THR D 1 58  ? 15.633  -83.755 25.280 1.00 97.86  ? 58  THR D CB  1 
ATOM   3756 O  OG1 . THR D 1 58  ? 15.733  -83.248 26.611 1.00 99.28  ? 58  THR D OG1 1 
ATOM   3757 C  CG2 . THR D 1 58  ? 16.266  -85.149 25.201 1.00 98.23  ? 58  THR D CG2 1 
ATOM   3758 N  N   . SER D 1 59  ? 14.564  -81.719 22.972 1.00 93.55  ? 59  SER D N   1 
ATOM   3759 C  CA  . SER D 1 59  ? 13.675  -81.513 21.841 1.00 93.76  ? 59  SER D CA  1 
ATOM   3760 C  C   . SER D 1 59  ? 14.415  -81.235 20.533 1.00 90.53  ? 59  SER D C   1 
ATOM   3761 O  O   . SER D 1 59  ? 13.880  -81.491 19.464 1.00 91.26  ? 59  SER D O   1 
ATOM   3762 C  CB  . SER D 1 59  ? 12.735  -80.353 22.146 1.00 95.00  ? 59  SER D CB  1 
ATOM   3763 O  OG  . SER D 1 59  ? 12.126  -80.535 23.413 1.00 98.83  ? 59  SER D OG  1 
ATOM   3764 N  N   . ALA D 1 60  ? 15.632  -80.698 20.626 1.00 87.55  ? 60  ALA D N   1 
ATOM   3765 C  CA  . ALA D 1 60  ? 16.482  -80.372 19.459 1.00 84.94  ? 60  ALA D CA  1 
ATOM   3766 C  C   . ALA D 1 60  ? 16.762  -81.565 18.556 1.00 85.35  ? 60  ALA D C   1 
ATOM   3767 O  O   . ALA D 1 60  ? 16.994  -81.413 17.351 1.00 84.36  ? 60  ALA D O   1 
ATOM   3768 C  CB  . ALA D 1 60  ? 17.800  -79.796 19.926 1.00 82.56  ? 60  ALA D CB  1 
ATOM   3769 N  N   . GLY D 1 61  ? 16.756  -82.750 19.158 1.00 87.21  ? 61  GLY D N   1 
ATOM   3770 C  CA  . GLY D 1 61  ? 16.909  -83.991 18.423 1.00 88.66  ? 61  GLY D CA  1 
ATOM   3771 C  C   . GLY D 1 61  ? 18.364  -84.296 18.169 1.00 86.77  ? 61  GLY D C   1 
ATOM   3772 O  O   . GLY D 1 61  ? 19.237  -83.746 18.827 1.00 84.89  ? 61  GLY D O   1 
ATOM   3773 N  N   . PRO D 1 62  ? 18.634  -85.163 17.190 1.00 87.85  ? 62  PRO D N   1 
ATOM   3774 C  CA  . PRO D 1 62  ? 19.988  -85.609 16.930 1.00 86.74  ? 62  PRO D CA  1 
ATOM   3775 C  C   . PRO D 1 62  ? 20.756  -84.554 16.194 1.00 84.25  ? 62  PRO D C   1 
ATOM   3776 O  O   . PRO D 1 62  ? 20.219  -83.521 15.847 1.00 83.32  ? 62  PRO D O   1 
ATOM   3777 C  CB  . PRO D 1 62  ? 19.779  -86.790 16.000 1.00 89.48  ? 62  PRO D CB  1 
ATOM   3778 C  CG  . PRO D 1 62  ? 18.600  -86.357 15.163 1.00 90.74  ? 62  PRO D CG  1 
ATOM   3779 C  CD  . PRO D 1 62  ? 17.716  -85.551 16.099 1.00 90.25  ? 62  PRO D CD  1 
ATOM   3780 N  N   . HIS D 1 63  ? 22.009  -84.837 15.921 1.00 83.70  ? 63  HIS D N   1 
ATOM   3781 C  CA  . HIS D 1 63  ? 22.832  -83.920 15.159 1.00 82.15  ? 63  HIS D CA  1 
ATOM   3782 C  C   . HIS D 1 63  ? 22.242  -83.672 13.791 1.00 82.57  ? 63  HIS D C   1 
ATOM   3783 O  O   . HIS D 1 63  ? 21.702  -84.578 13.160 1.00 84.97  ? 63  HIS D O   1 
ATOM   3784 C  CB  . HIS D 1 63  ? 24.213  -84.505 14.969 1.00 82.56  ? 63  HIS D CB  1 
ATOM   3785 C  CG  . HIS D 1 63  ? 25.024  -84.529 16.216 1.00 83.55  ? 63  HIS D CG  1 
ATOM   3786 N  ND1 . HIS D 1 63  ? 26.379  -84.281 16.220 1.00 83.88  ? 63  HIS D ND1 1 
ATOM   3787 C  CD2 . HIS D 1 63  ? 24.671  -84.758 17.503 1.00 86.21  ? 63  HIS D CD2 1 
ATOM   3788 C  CE1 . HIS D 1 63  ? 26.829  -84.378 17.455 1.00 85.14  ? 63  HIS D CE1 1 
ATOM   3789 N  NE2 . HIS D 1 63  ? 25.814  -84.656 18.253 1.00 86.87  ? 63  HIS D NE2 1 
ATOM   3790 N  N   . PHE D 1 64  ? 22.384  -82.445 13.323 1.00 80.65  ? 64  PHE D N   1 
ATOM   3791 C  CA  . PHE D 1 64  ? 21.901  -82.076 12.022 1.00 81.65  ? 64  PHE D CA  1 
ATOM   3792 C  C   . PHE D 1 64  ? 22.666  -82.868 11.015 1.00 82.73  ? 64  PHE D C   1 
ATOM   3793 O  O   . PHE D 1 64  ? 23.853  -82.652 10.827 1.00 81.35  ? 64  PHE D O   1 
ATOM   3794 C  CB  . PHE D 1 64  ? 22.135  -80.592 11.765 1.00 80.57  ? 64  PHE D CB  1 
ATOM   3795 C  CG  . PHE D 1 64  ? 21.623  -80.104 10.428 1.00 83.31  ? 64  PHE D CG  1 
ATOM   3796 C  CD1 . PHE D 1 64  ? 20.415  -80.574 9.908  1.00 86.86  ? 64  PHE D CD1 1 
ATOM   3797 C  CD2 . PHE D 1 64  ? 22.328  -79.146 9.701  1.00 83.75  ? 64  PHE D CD2 1 
ATOM   3798 C  CE1 . PHE D 1 64  ? 19.935  -80.117 8.674  1.00 89.07  ? 64  PHE D CE1 1 
ATOM   3799 C  CE2 . PHE D 1 64  ? 21.843  -78.678 8.474  1.00 86.67  ? 64  PHE D CE2 1 
ATOM   3800 C  CZ  . PHE D 1 64  ? 20.647  -79.163 7.961  1.00 88.99  ? 64  PHE D CZ  1 
ATOM   3801 N  N   . ASN D 1 65  ? 21.975  -83.776 10.351 1.00 85.41  ? 65  ASN D N   1 
ATOM   3802 C  CA  . ASN D 1 65  ? 22.643  -84.713 9.480  1.00 87.73  ? 65  ASN D CA  1 
ATOM   3803 C  C   . ASN D 1 65  ? 21.809  -85.011 8.246  1.00 91.48  ? 65  ASN D C   1 
ATOM   3804 O  O   . ASN D 1 65  ? 21.177  -86.065 8.146  1.00 94.15  ? 65  ASN D O   1 
ATOM   3805 C  CB  . ASN D 1 65  ? 22.939  -85.995 10.255 1.00 88.26  ? 65  ASN D CB  1 
ATOM   3806 C  CG  . ASN D 1 65  ? 23.728  -86.972 9.450  1.00 89.97  ? 65  ASN D CG  1 
ATOM   3807 O  OD1 . ASN D 1 65  ? 24.298  -86.611 8.413  1.00 90.76  ? 65  ASN D OD1 1 
ATOM   3808 N  ND2 . ASN D 1 65  ? 23.777  -88.215 9.907  1.00 89.74  ? 65  ASN D ND2 1 
ATOM   3809 N  N   . PRO D 1 66  ? 21.822  -84.089 7.281  1.00 92.34  ? 66  PRO D N   1 
ATOM   3810 C  CA  . PRO D 1 66  ? 20.956  -84.204 6.118  1.00 96.32  ? 66  PRO D CA  1 
ATOM   3811 C  C   . PRO D 1 66  ? 21.455  -85.193 5.044  1.00 100.35 ? 66  PRO D C   1 
ATOM   3812 O  O   . PRO D 1 66  ? 20.649  -85.713 4.278  1.00 104.36 ? 66  PRO D O   1 
ATOM   3813 C  CB  . PRO D 1 66  ? 20.926  -82.768 5.584  1.00 95.63  ? 66  PRO D CB  1 
ATOM   3814 C  CG  . PRO D 1 66  ? 22.256  -82.234 5.894  1.00 92.94  ? 66  PRO D CG  1 
ATOM   3815 C  CD  . PRO D 1 66  ? 22.732  -82.943 7.159  1.00 90.34  ? 66  PRO D CD  1 
ATOM   3816 N  N   . LEU D 1 67  ? 22.758  -85.457 4.998  1.00 99.99  ? 67  LEU D N   1 
ATOM   3817 C  CA  . LEU D 1 67  ? 23.313  -86.428 4.047  1.00 104.19 ? 67  LEU D CA  1 
ATOM   3818 C  C   . LEU D 1 67  ? 23.447  -87.839 4.672  1.00 105.22 ? 67  LEU D C   1 
ATOM   3819 O  O   . LEU D 1 67  ? 24.079  -88.712 4.090  1.00 108.40 ? 67  LEU D O   1 
ATOM   3820 C  CB  . LEU D 1 67  ? 24.693  -85.975 3.551  1.00 104.04 ? 67  LEU D CB  1 
ATOM   3821 C  CG  . LEU D 1 67  ? 24.970  -84.509 3.189  1.00 103.12 ? 67  LEU D CG  1 
ATOM   3822 C  CD1 . LEU D 1 67  ? 26.418  -84.111 3.658  1.00 100.86 ? 67  LEU D CD1 1 
ATOM   3823 C  CD2 . LEU D 1 67  ? 24.733  -84.213 1.689  1.00 106.62 ? 67  LEU D CD2 1 
ATOM   3824 N  N   . SER D 1 68  ? 22.883  -88.047 5.861  1.00 103.14 ? 68  SER D N   1 
ATOM   3825 C  CA  . SER D 1 68  ? 22.893  -89.347 6.542  1.00 104.46 ? 68  SER D CA  1 
ATOM   3826 C  C   . SER D 1 68  ? 24.272  -89.970 6.722  1.00 104.68 ? 68  SER D C   1 
ATOM   3827 O  O   . SER D 1 68  ? 24.431  -91.163 6.543  1.00 107.96 ? 68  SER D O   1 
ATOM   3828 C  CB  . SER D 1 68  ? 21.972  -90.338 5.816  1.00 109.58 ? 68  SER D CB  1 
ATOM   3829 O  OG  . SER D 1 68  ? 20.619  -90.073 6.115  1.00 109.88 ? 68  SER D OG  1 
ATOM   3830 N  N   . ARG D 1 69  ? 25.258  -89.177 7.103  1.00 101.89 ? 69  ARG D N   1 
ATOM   3831 C  CA  . ARG D 1 69  ? 26.609  -89.699 7.359  1.00 102.63 ? 69  ARG D CA  1 
ATOM   3832 C  C   . ARG D 1 69  ? 26.773  -90.147 8.810  1.00 100.51 ? 69  ARG D C   1 
ATOM   3833 O  O   . ARG D 1 69  ? 25.867  -89.979 9.630  1.00 98.96  ? 69  ARG D O   1 
ATOM   3834 C  CB  . ARG D 1 69  ? 27.660  -88.629 7.067  1.00 101.11 ? 69  ARG D CB  1 
ATOM   3835 C  CG  . ARG D 1 69  ? 27.564  -88.012 5.683  1.00 105.11 ? 69  ARG D CG  1 
ATOM   3836 C  CD  . ARG D 1 69  ? 28.129  -88.933 4.595  1.00 112.52 ? 69  ARG D CD  1 
ATOM   3837 N  NE  . ARG D 1 69  ? 28.079  -88.285 3.276  1.00 117.52 ? 69  ARG D NE  1 
ATOM   3838 C  CZ  . ARG D 1 69  ? 28.927  -87.340 2.847  1.00 118.51 ? 69  ARG D CZ  1 
ATOM   3839 N  NH1 . ARG D 1 69  ? 29.930  -86.914 3.606  1.00 116.24 ? 69  ARG D NH1 1 
ATOM   3840 N  NH2 . ARG D 1 69  ? 28.779  -86.820 1.639  1.00 122.02 ? 69  ARG D NH2 1 
ATOM   3841 N  N   . LYS D 1 70  ? 27.938  -90.713 9.115  1.00 100.96 ? 70  LYS D N   1 
ATOM   3842 C  CA  . LYS D 1 70  ? 28.298  -91.043 10.492 1.00 99.31  ? 70  LYS D CA  1 
ATOM   3843 C  C   . LYS D 1 70  ? 28.928  -89.790 11.122 1.00 94.62  ? 70  LYS D C   1 
ATOM   3844 O  O   . LYS D 1 70  ? 29.491  -88.945 10.405 1.00 93.36  ? 70  LYS D O   1 
ATOM   3845 C  CB  . LYS D 1 70  ? 29.281  -92.236 10.556 1.00 102.72 ? 70  LYS D CB  1 
ATOM   3846 C  CG  . LYS D 1 70  ? 28.988  -93.446 9.603  1.00 109.25 ? 70  LYS D CG  1 
ATOM   3847 C  CD  . LYS D 1 70  ? 28.452  -94.735 10.308 1.00 113.93 ? 70  LYS D CD  1 
ATOM   3848 C  CE  . LYS D 1 70  ? 29.110  -96.005 9.650  1.00 120.33 ? 70  LYS D CE  1 
ATOM   3849 N  NZ  . LYS D 1 70  ? 28.480  -97.314 10.023 1.00 125.05 ? 70  LYS D NZ  1 
ATOM   3850 N  N   . HIS D 1 71  ? 28.849  -89.698 12.456 1.00 92.05  ? 71  HIS D N   1 
ATOM   3851 C  CA  . HIS D 1 71  ? 29.377  -88.548 13.190 1.00 88.36  ? 71  HIS D CA  1 
ATOM   3852 C  C   . HIS D 1 71  ? 30.884  -88.444 13.020 1.00 88.55  ? 71  HIS D C   1 
ATOM   3853 O  O   . HIS D 1 71  ? 31.568  -89.452 12.934 1.00 90.98  ? 71  HIS D O   1 
ATOM   3854 C  CB  . HIS D 1 71  ? 29.044  -88.652 14.678 1.00 87.17  ? 71  HIS D CB  1 
ATOM   3855 C  CG  . HIS D 1 71  ? 29.633  -87.554 15.508 1.00 84.11  ? 71  HIS D CG  1 
ATOM   3856 N  ND1 . HIS D 1 71  ? 29.131  -86.272 15.519 1.00 81.56  ? 71  HIS D ND1 1 
ATOM   3857 C  CD2 . HIS D 1 71  ? 30.691  -87.549 16.352 1.00 83.34  ? 71  HIS D CD2 1 
ATOM   3858 C  CE1 . HIS D 1 71  ? 29.858  -85.525 16.330 1.00 79.76  ? 71  HIS D CE1 1 
ATOM   3859 N  NE2 . HIS D 1 71  ? 30.808  -86.277 16.848 1.00 80.74  ? 71  HIS D NE2 1 
ATOM   3860 N  N   . GLY D 1 72  ? 31.401  -87.225 12.982 1.00 86.49  ? 72  GLY D N   1 
ATOM   3861 C  CA  . GLY D 1 72  ? 32.838  -87.016 12.894 1.00 87.26  ? 72  GLY D CA  1 
ATOM   3862 C  C   . GLY D 1 72  ? 33.276  -85.662 13.424 1.00 85.21  ? 72  GLY D C   1 
ATOM   3863 O  O   . GLY D 1 72  ? 32.489  -84.904 14.000 1.00 83.32  ? 72  GLY D O   1 
ATOM   3864 N  N   . GLY D 1 73  ? 34.561  -85.381 13.251 1.00 86.34  ? 73  GLY D N   1 
ATOM   3865 C  CA  . GLY D 1 73  ? 35.131  -84.100 13.619 1.00 85.08  ? 73  GLY D CA  1 
ATOM   3866 C  C   . GLY D 1 73  ? 34.909  -83.153 12.488 1.00 85.11  ? 73  GLY D C   1 
ATOM   3867 O  O   . GLY D 1 73  ? 34.587  -83.572 11.401 1.00 86.68  ? 73  GLY D O   1 
ATOM   3868 N  N   . PRO D 1 74  ? 35.114  -81.867 12.721 1.00 84.31  ? 74  PRO D N   1 
ATOM   3869 C  CA  . PRO D 1 74  ? 34.664  -80.914 11.712 1.00 84.54  ? 74  PRO D CA  1 
ATOM   3870 C  C   . PRO D 1 74  ? 35.529  -80.940 10.495 1.00 87.42  ? 74  PRO D C   1 
ATOM   3871 O  O   . PRO D 1 74  ? 35.038  -80.728 9.416  1.00 88.45  ? 74  PRO D O   1 
ATOM   3872 C  CB  . PRO D 1 74  ? 34.785  -79.567 12.417 1.00 83.19  ? 74  PRO D CB  1 
ATOM   3873 C  CG  . PRO D 1 74  ? 35.906  -79.772 13.402 1.00 83.95  ? 74  PRO D CG  1 
ATOM   3874 C  CD  . PRO D 1 74  ? 35.986  -81.250 13.729 1.00 84.10  ? 74  PRO D CD  1 
ATOM   3875 N  N   . LYS D 1 75  ? 36.810  -81.215 10.673 1.00 89.59  ? 75  LYS D N   1 
ATOM   3876 C  CA  . LYS D 1 75  ? 37.732  -81.293 9.560  1.00 93.50  ? 75  LYS D CA  1 
ATOM   3877 C  C   . LYS D 1 75  ? 37.770  -82.696 8.973  1.00 95.38  ? 75  LYS D C   1 
ATOM   3878 O  O   . LYS D 1 75  ? 38.357  -82.899 7.927  1.00 98.55  ? 75  LYS D O   1 
ATOM   3879 C  CB  . LYS D 1 75  ? 39.121  -80.863 10.000 1.00 95.29  ? 75  LYS D CB  1 
ATOM   3880 C  CG  . LYS D 1 75  ? 39.193  -79.362 10.451 1.00 97.18  ? 75  LYS D CG  1 
ATOM   3881 C  CD  . LYS D 1 75  ? 40.652  -78.832 10.577 1.00 103.42 ? 75  LYS D CD  1 
ATOM   3882 C  CE  . LYS D 1 75  ? 41.618  -79.963 11.153 1.00 106.87 ? 75  LYS D CE  1 
ATOM   3883 N  NZ  . LYS D 1 75  ? 43.075  -79.619 11.374 1.00 110.22 ? 75  LYS D NZ  1 
ATOM   3884 N  N   . ASP D 1 76  ? 37.133  -83.660 9.635  1.00 94.08  ? 76  ASP D N   1 
ATOM   3885 C  CA  . ASP D 1 76  ? 36.976  -84.999 9.071  1.00 96.45  ? 76  ASP D CA  1 
ATOM   3886 C  C   . ASP D 1 76  ? 36.097  -84.932 7.852  1.00 97.71  ? 76  ASP D C   1 
ATOM   3887 O  O   . ASP D 1 76  ? 35.344  -83.981 7.663  1.00 95.83  ? 76  ASP D O   1 
ATOM   3888 C  CB  . ASP D 1 76  ? 36.369  -85.986 10.079 1.00 95.28  ? 76  ASP D CB  1 
ATOM   3889 C  CG  . ASP D 1 76  ? 37.423  -86.633 10.989 1.00 96.94  ? 76  ASP D CG  1 
ATOM   3890 O  OD1 . ASP D 1 76  ? 38.456  -87.113 10.473 1.00 101.35 ? 76  ASP D OD1 1 
ATOM   3891 O  OD2 . ASP D 1 76  ? 37.211  -86.690 12.217 1.00 95.72  ? 76  ASP D OD2 1 
ATOM   3892 N  N   . GLU D 1 77  ? 36.218  -85.941 7.009  1.00 101.51 ? 77  GLU D N   1 
ATOM   3893 C  CA  . GLU D 1 77  ? 35.473  -85.966 5.776  1.00 104.25 ? 77  GLU D CA  1 
ATOM   3894 C  C   . GLU D 1 77  ? 34.108  -86.606 6.010  1.00 102.59 ? 77  GLU D C   1 
ATOM   3895 O  O   . GLU D 1 77  ? 33.092  -86.019 5.678  1.00 101.61 ? 77  GLU D O   1 
ATOM   3896 C  CB  . GLU D 1 77  ? 36.260  -86.705 4.709  1.00 109.85 ? 77  GLU D CB  1 
ATOM   3897 C  CG  . GLU D 1 77  ? 35.614  -86.630 3.354  1.00 116.13 ? 77  GLU D CG  1 
ATOM   3898 C  CD  . GLU D 1 77  ? 35.493  -88.043 2.660  1.00 125.50 ? 77  GLU D CD  1 
ATOM   3899 O  OE1 . GLU D 1 77  ? 36.562  -88.588 2.198  1.00 130.64 ? 77  GLU D OE1 1 
ATOM   3900 O  OE2 . GLU D 1 77  ? 34.319  -88.581 2.573  1.00 128.69 ? 77  GLU D OE2 1 
ATOM   3901 N  N   . GLU D 1 78  ? 34.084  -87.808 6.569  1.00 102.65 ? 78  GLU D N   1 
ATOM   3902 C  CA  . GLU D 1 78  ? 32.827  -88.410 7.029  1.00 101.45 ? 78  GLU D CA  1 
ATOM   3903 C  C   . GLU D 1 78  ? 32.361  -87.737 8.342  1.00 96.34  ? 78  GLU D C   1 
ATOM   3904 O  O   . GLU D 1 78  ? 32.869  -88.039 9.441  1.00 94.88  ? 78  GLU D O   1 
ATOM   3905 C  CB  . GLU D 1 78  ? 32.983  -89.926 7.219  1.00 104.49 ? 78  GLU D CB  1 
ATOM   3906 C  CG  . GLU D 1 78  ? 31.681  -90.684 7.631  1.00 105.74 ? 78  GLU D CG  1 
ATOM   3907 C  CD  . GLU D 1 78  ? 30.718  -91.006 6.455  1.00 110.99 ? 78  GLU D CD  1 
ATOM   3908 O  OE1 . GLU D 1 78  ? 30.802  -90.319 5.400  1.00 113.99 ? 78  GLU D OE1 1 
ATOM   3909 O  OE2 . GLU D 1 78  ? 29.880  -91.946 6.588  1.00 112.94 ? 78  GLU D OE2 1 
ATOM   3910 N  N   . ARG D 1 79  ? 31.395  -86.826 8.209  1.00 93.60  ? 79  ARG D N   1 
ATOM   3911 C  CA  . ARG D 1 79  ? 30.855  -86.056 9.335  1.00 89.29  ? 79  ARG D CA  1 
ATOM   3912 C  C   . ARG D 1 79  ? 29.395  -85.613 9.117  1.00 88.07  ? 79  ARG D C   1 
ATOM   3913 O  O   . ARG D 1 79  ? 28.883  -85.543 7.979  1.00 90.07  ? 79  ARG D O   1 
ATOM   3914 C  CB  . ARG D 1 79  ? 31.688  -84.791 9.568  1.00 87.38  ? 79  ARG D CB  1 
ATOM   3915 C  CG  . ARG D 1 79  ? 31.598  -83.768 8.398  1.00 88.84  ? 79  ARG D CG  1 
ATOM   3916 C  CD  . ARG D 1 79  ? 32.226  -82.407 8.719  1.00 87.80  ? 79  ARG D CD  1 
ATOM   3917 N  NE  . ARG D 1 79  ? 31.299  -81.505 9.409  1.00 85.71  ? 79  ARG D NE  1 
ATOM   3918 C  CZ  . ARG D 1 79  ? 31.449  -80.180 9.509  1.00 84.77  ? 79  ARG D CZ  1 
ATOM   3919 N  NH1 . ARG D 1 79  ? 32.484  -79.579 8.959  1.00 85.63  ? 79  ARG D NH1 1 
ATOM   3920 N  NH2 . ARG D 1 79  ? 30.548  -79.437 10.157 1.00 83.42  ? 79  ARG D NH2 1 
ATOM   3921 N  N   . HIS D 1 80  ? 28.741  -85.269 10.222 1.00 84.76  ? 80  HIS D N   1 
ATOM   3922 C  CA  . HIS D 1 80  ? 27.448  -84.642 10.151 1.00 83.12  ? 80  HIS D CA  1 
ATOM   3923 C  C   . HIS D 1 80  ? 27.684  -83.193 9.802  1.00 81.10  ? 80  HIS D C   1 
ATOM   3924 O  O   . HIS D 1 80  ? 28.635  -82.590 10.295 1.00 79.36  ? 80  HIS D O   1 
ATOM   3925 C  CB  . HIS D 1 80  ? 26.736  -84.727 11.485 1.00 81.28  ? 80  HIS D CB  1 
ATOM   3926 C  CG  . HIS D 1 80  ? 26.473  -86.119 11.945 1.00 82.98  ? 80  HIS D CG  1 
ATOM   3927 N  ND1 . HIS D 1 80  ? 26.184  -86.426 13.259 1.00 82.72  ? 80  HIS D ND1 1 
ATOM   3928 C  CD2 . HIS D 1 80  ? 26.423  -87.282 11.262 1.00 86.59  ? 80  HIS D CD2 1 
ATOM   3929 C  CE1 . HIS D 1 80  ? 25.957  -87.721 13.362 1.00 86.00  ? 80  HIS D CE1 1 
ATOM   3930 N  NE2 . HIS D 1 80  ? 26.102  -88.264 12.166 1.00 88.39  ? 80  HIS D NE2 1 
ATOM   3931 N  N   . VAL D 1 81  ? 26.816  -82.634 8.966  1.00 81.35  ? 81  VAL D N   1 
ATOM   3932 C  CA  . VAL D 1 81  ? 26.840  -81.190 8.680  1.00 79.68  ? 81  VAL D CA  1 
ATOM   3933 C  C   . VAL D 1 81  ? 26.917  -80.360 9.963  1.00 76.04  ? 81  VAL D C   1 
ATOM   3934 O  O   . VAL D 1 81  ? 27.576  -79.346 10.013 1.00 74.75  ? 81  VAL D O   1 
ATOM   3935 C  CB  . VAL D 1 81  ? 25.607  -80.741 7.852  1.00 81.17  ? 81  VAL D CB  1 
ATOM   3936 C  CG1 . VAL D 1 81  ? 25.613  -79.264 7.625  1.00 79.63  ? 81  VAL D CG1 1 
ATOM   3937 C  CG2 . VAL D 1 81  ? 25.596  -81.439 6.519  1.00 85.35  ? 81  VAL D CG2 1 
ATOM   3938 N  N   . GLY D 1 82  ? 26.261  -80.812 11.016 1.00 74.68  ? 82  GLY D N   1 
ATOM   3939 C  CA  . GLY D 1 82  ? 26.246  -80.075 12.271 1.00 72.51  ? 82  GLY D CA  1 
ATOM   3940 C  C   . GLY D 1 82  ? 27.412  -80.290 13.222 1.00 71.56  ? 82  GLY D C   1 
ATOM   3941 O  O   . GLY D 1 82  ? 27.378  -79.777 14.333 1.00 69.82  ? 82  GLY D O   1 
ATOM   3942 N  N   . ASP D 1 83  ? 28.439  -81.040 12.808 1.00 72.91  ? 83  ASP D N   1 
ATOM   3943 C  CA  . ASP D 1 83  ? 29.532  -81.399 13.708 1.00 72.71  ? 83  ASP D CA  1 
ATOM   3944 C  C   . ASP D 1 83  ? 30.597  -80.339 13.653 1.00 72.33  ? 83  ASP D C   1 
ATOM   3945 O  O   . ASP D 1 83  ? 31.399  -80.318 12.754 1.00 73.88  ? 83  ASP D O   1 
ATOM   3946 C  CB  . ASP D 1 83  ? 30.152  -82.750 13.341 1.00 74.57  ? 83  ASP D CB  1 
ATOM   3947 C  CG  . ASP D 1 83  ? 29.187  -83.917 13.503 1.00 75.88  ? 83  ASP D CG  1 
ATOM   3948 O  OD1 . ASP D 1 83  ? 28.295  -83.892 14.390 1.00 74.92  ? 83  ASP D OD1 1 
ATOM   3949 O  OD2 . ASP D 1 83  ? 29.337  -84.897 12.747 1.00 78.50  ? 83  ASP D OD2 1 
ATOM   3950 N  N   . LEU D 1 84  ? 30.604  -79.439 14.614 1.00 71.27  ? 84  LEU D N   1 
ATOM   3951 C  CA  . LEU D 1 84  ? 31.646  -78.421 14.666 1.00 71.52  ? 84  LEU D CA  1 
ATOM   3952 C  C   . LEU D 1 84  ? 32.749  -78.778 15.667 1.00 71.99  ? 84  LEU D C   1 
ATOM   3953 O  O   . LEU D 1 84  ? 33.542  -77.941 16.088 1.00 71.96  ? 84  LEU D O   1 
ATOM   3954 C  CB  . LEU D 1 84  ? 31.011  -77.077 14.997 1.00 70.76  ? 84  LEU D CB  1 
ATOM   3955 C  CG  . LEU D 1 84  ? 29.972  -76.618 13.966 1.00 70.49  ? 84  LEU D CG  1 
ATOM   3956 C  CD1 . LEU D 1 84  ? 29.380  -75.314 14.386 1.00 68.57  ? 84  LEU D CD1 1 
ATOM   3957 C  CD2 . LEU D 1 84  ? 30.570  -76.507 12.573 1.00 71.62  ? 84  LEU D CD2 1 
ATOM   3958 N  N   . GLY D 1 85  ? 32.809  -80.047 16.036 1.00 72.83  ? 85  GLY D N   1 
ATOM   3959 C  CA  . GLY D 1 85  ? 33.799  -80.496 16.998 1.00 73.81  ? 85  GLY D CA  1 
ATOM   3960 C  C   . GLY D 1 85  ? 33.693  -79.832 18.362 1.00 73.17  ? 85  GLY D C   1 
ATOM   3961 O  O   . GLY D 1 85  ? 32.619  -79.804 18.965 1.00 72.46  ? 85  GLY D O   1 
ATOM   3962 N  N   . ASN D 1 86  ? 34.803  -79.303 18.856 1.00 73.96  ? 86  ASN D N   1 
ATOM   3963 C  CA  . ASN D 1 86  ? 34.864  -78.867 20.241 1.00 74.58  ? 86  ASN D CA  1 
ATOM   3964 C  C   . ASN D 1 86  ? 35.186  -77.398 20.410 1.00 74.69  ? 86  ASN D C   1 
ATOM   3965 O  O   . ASN D 1 86  ? 35.685  -76.736 19.498 1.00 74.95  ? 86  ASN D O   1 
ATOM   3966 C  CB  . ASN D 1 86  ? 35.938  -79.641 20.990 1.00 76.89  ? 86  ASN D CB  1 
ATOM   3967 C  CG  . ASN D 1 86  ? 35.587  -81.090 21.192 1.00 77.91  ? 86  ASN D CG  1 
ATOM   3968 O  OD1 . ASN D 1 86  ? 34.777  -81.439 22.047 1.00 80.03  ? 86  ASN D OD1 1 
ATOM   3969 N  ND2 . ASN D 1 86  ? 36.230  -81.948 20.434 1.00 79.90  ? 86  ASN D ND2 1 
ATOM   3970 N  N   . VAL D 1 87  ? 34.896  -76.909 21.606 1.00 75.02  ? 87  VAL D N   1 
ATOM   3971 C  CA  . VAL D 1 87  ? 35.305  -75.588 22.034 1.00 76.05  ? 87  VAL D CA  1 
ATOM   3972 C  C   . VAL D 1 87  ? 36.008  -75.779 23.375 1.00 78.87  ? 87  VAL D C   1 
ATOM   3973 O  O   . VAL D 1 87  ? 35.814  -76.792 24.059 1.00 79.16  ? 87  VAL D O   1 
ATOM   3974 C  CB  . VAL D 1 87  ? 34.109  -74.636 22.171 1.00 74.83  ? 87  VAL D CB  1 
ATOM   3975 C  CG1 . VAL D 1 87  ? 33.322  -74.617 20.907 1.00 71.74  ? 87  VAL D CG1 1 
ATOM   3976 C  CG2 . VAL D 1 87  ? 33.243  -75.046 23.301 1.00 74.67  ? 87  VAL D CG2 1 
ATOM   3977 N  N   . THR D 1 88  ? 36.818  -74.805 23.753 1.00 81.46  ? 88  THR D N   1 
ATOM   3978 C  CA  . THR D 1 88  ? 37.713  -74.982 24.873 1.00 84.84  ? 88  THR D CA  1 
ATOM   3979 C  C   . THR D 1 88  ? 37.465  -73.984 25.968 1.00 87.06  ? 88  THR D C   1 
ATOM   3980 O  O   . THR D 1 88  ? 37.462  -72.785 25.723 1.00 87.81  ? 88  THR D O   1 
ATOM   3981 C  CB  . THR D 1 88  ? 39.151  -74.839 24.396 1.00 86.90  ? 88  THR D CB  1 
ATOM   3982 O  OG1 . THR D 1 88  ? 39.493  -75.957 23.572 1.00 86.12  ? 88  THR D OG1 1 
ATOM   3983 C  CG2 . THR D 1 88  ? 40.099  -74.775 25.582 1.00 91.37  ? 88  THR D CG2 1 
ATOM   3984 N  N   . ALA D 1 89  ? 37.298  -74.478 27.184 1.00 89.13  ? 89  ALA D N   1 
ATOM   3985 C  CA  . ALA D 1 89  ? 37.032  -73.621 28.333 1.00 92.37  ? 89  ALA D CA  1 
ATOM   3986 C  C   . ALA D 1 89  ? 38.313  -73.283 29.097 1.00 97.29  ? 89  ALA D C   1 
ATOM   3987 O  O   . ALA D 1 89  ? 39.141  -74.164 29.373 1.00 98.74  ? 89  ALA D O   1 
ATOM   3988 C  CB  . ALA D 1 89  ? 36.035  -74.284 29.280 1.00 92.59  ? 89  ALA D CB  1 
ATOM   3989 N  N   . ASP D 1 90  ? 38.453  -71.989 29.407 1.00 100.50 ? 90  ASP D N   1 
ATOM   3990 C  CA  . ASP D 1 90  ? 39.344  -71.448 30.445 1.00 106.34 ? 90  ASP D CA  1 
ATOM   3991 C  C   . ASP D 1 90  ? 39.535  -72.335 31.655 1.00 109.89 ? 90  ASP D C   1 
ATOM   3992 O  O   . ASP D 1 90  ? 38.801  -73.322 31.868 1.00 108.17 ? 90  ASP D O   1 
ATOM   3993 C  CB  . ASP D 1 90  ? 38.704  -70.169 31.031 1.00 108.66 ? 90  ASP D CB  1 
ATOM   3994 C  CG  . ASP D 1 90  ? 39.334  -68.908 30.546 1.00 111.99 ? 90  ASP D CG  1 
ATOM   3995 O  OD1 . ASP D 1 90  ? 40.149  -68.996 29.598 1.00 113.39 ? 90  ASP D OD1 1 
ATOM   3996 O  OD2 . ASP D 1 90  ? 38.994  -67.829 31.116 1.00 116.47 ? 90  ASP D OD2 1 
ATOM   3997 N  N   . LYS D 1 91  ? 40.500  -71.911 32.476 1.00 115.66 ? 91  LYS D N   1 
ATOM   3998 C  CA  . LYS D 1 91  ? 40.483  -72.159 33.951 1.00 120.98 ? 91  LYS D CA  1 
ATOM   3999 C  C   . LYS D 1 91  ? 39.131  -71.717 34.571 1.00 120.60 ? 91  LYS D C   1 
ATOM   4000 O  O   . LYS D 1 91  ? 38.468  -72.452 35.317 1.00 121.11 ? 91  LYS D O   1 
ATOM   4001 C  CB  . LYS D 1 91  ? 41.602  -71.321 34.636 1.00 127.44 ? 91  LYS D CB  1 
ATOM   4002 C  CG  . LYS D 1 91  ? 42.918  -72.045 34.952 1.00 132.55 ? 91  LYS D CG  1 
ATOM   4003 C  CD  . LYS D 1 91  ? 42.847  -72.761 36.326 1.00 139.41 ? 91  LYS D CD  1 
ATOM   4004 C  CE  . LYS D 1 91  ? 44.243  -72.860 36.980 1.00 146.71 ? 91  LYS D CE  1 
ATOM   4005 N  NZ  . LYS D 1 91  ? 44.423  -74.207 37.606 1.00 149.59 ? 91  LYS D NZ  1 
ATOM   4006 N  N   . ASP D 1 92  ? 38.787  -70.473 34.229 1.00 120.05 ? 92  ASP D N   1 
ATOM   4007 C  CA  . ASP D 1 92  ? 37.593  -69.754 34.684 1.00 120.63 ? 92  ASP D CA  1 
ATOM   4008 C  C   . ASP D 1 92  ? 36.283  -70.208 34.056 1.00 115.35 ? 92  ASP D C   1 
ATOM   4009 O  O   . ASP D 1 92  ? 35.238  -69.575 34.288 1.00 115.59 ? 92  ASP D O   1 
ATOM   4010 C  CB  . ASP D 1 92  ? 37.753  -68.251 34.356 1.00 122.25 ? 92  ASP D CB  1 
ATOM   4011 C  CG  . ASP D 1 92  ? 38.984  -67.617 35.045 1.00 129.37 ? 92  ASP D CG  1 
ATOM   4012 O  OD1 . ASP D 1 92  ? 38.975  -66.372 35.221 1.00 134.03 ? 92  ASP D OD1 1 
ATOM   4013 O  OD2 . ASP D 1 92  ? 39.941  -68.359 35.415 1.00 133.24 ? 92  ASP D OD2 1 
ATOM   4014 N  N   . GLY D 1 93  ? 36.336  -71.250 33.224 1.00 110.98 ? 93  GLY D N   1 
ATOM   4015 C  CA  . GLY D 1 93  ? 35.127  -71.774 32.574 1.00 106.46 ? 93  GLY D CA  1 
ATOM   4016 C  C   . GLY D 1 93  ? 34.500  -70.891 31.479 1.00 102.97 ? 93  GLY D C   1 
ATOM   4017 O  O   . GLY D 1 93  ? 33.331  -71.094 31.099 1.00 100.28 ? 93  GLY D O   1 
ATOM   4018 N  N   . VAL D 1 94  ? 35.249  -69.891 31.005 1.00 103.39 ? 94  VAL D N   1 
ATOM   4019 C  CA  . VAL D 1 94  ? 34.884  -69.169 29.791 1.00 100.48 ? 94  VAL D CA  1 
ATOM   4020 C  C   . VAL D 1 94  ? 35.525  -69.809 28.555 1.00 97.45  ? 94  VAL D C   1 
ATOM   4021 O  O   . VAL D 1 94  ? 36.720  -70.053 28.544 1.00 99.17  ? 94  VAL D O   1 
ATOM   4022 C  CB  . VAL D 1 94  ? 35.348  -67.705 29.858 1.00 103.62 ? 94  VAL D CB  1 
ATOM   4023 C  CG1 . VAL D 1 94  ? 35.147  -67.000 28.490 1.00 100.26 ? 94  VAL D CG1 1 
ATOM   4024 C  CG2 . VAL D 1 94  ? 34.631  -66.975 31.016 1.00 107.48 ? 94  VAL D CG2 1 
ATOM   4025 N  N   . ALA D 1 95  ? 34.739  -70.075 27.517 1.00 93.86  ? 95  ALA D N   1 
ATOM   4026 C  CA  . ALA D 1 95  ? 35.282  -70.568 26.245 1.00 91.50  ? 95  ALA D CA  1 
ATOM   4027 C  C   . ALA D 1 95  ? 35.149  -69.505 25.187 1.00 91.14  ? 95  ALA D C   1 
ATOM   4028 O  O   . ALA D 1 95  ? 34.045  -69.061 24.895 1.00 89.91  ? 95  ALA D O   1 
ATOM   4029 C  CB  . ALA D 1 95  ? 34.558  -71.807 25.802 1.00 88.24  ? 95  ALA D CB  1 
ATOM   4030 N  N   . ASP D 1 96  ? 36.268  -69.087 24.619 1.00 92.99  ? 96  ASP D N   1 
ATOM   4031 C  CA  . ASP D 1 96  ? 36.236  -68.035 23.612 1.00 93.85  ? 96  ASP D CA  1 
ATOM   4032 C  C   . ASP D 1 96  ? 36.175  -68.690 22.269 1.00 90.68  ? 96  ASP D C   1 
ATOM   4033 O  O   . ASP D 1 96  ? 37.206  -69.034 21.696 1.00 91.86  ? 96  ASP D O   1 
ATOM   4034 C  CB  . ASP D 1 96  ? 37.464  -67.117 23.685 1.00 98.04  ? 96  ASP D CB  1 
ATOM   4035 C  CG  . ASP D 1 96  ? 37.298  -66.002 24.703 1.00 103.86 ? 96  ASP D CG  1 
ATOM   4036 O  OD1 . ASP D 1 96  ? 36.214  -65.348 24.710 1.00 105.32 ? 96  ASP D OD1 1 
ATOM   4037 O  OD2 . ASP D 1 96  ? 38.254  -65.780 25.496 1.00 110.05 ? 96  ASP D OD2 1 
ATOM   4038 N  N   . VAL D 1 97  ? 34.966  -68.830 21.748 1.00 87.42  ? 97  VAL D N   1 
ATOM   4039 C  CA  . VAL D 1 97  ? 34.766  -69.540 20.502 1.00 84.49  ? 97  VAL D CA  1 
ATOM   4040 C  C   . VAL D 1 97  ? 35.219  -68.756 19.282 1.00 84.89  ? 97  VAL D C   1 
ATOM   4041 O  O   . VAL D 1 97  ? 35.002  -67.561 19.199 1.00 86.46  ? 97  VAL D O   1 
ATOM   4042 C  CB  . VAL D 1 97  ? 33.306  -69.844 20.318 1.00 82.17  ? 97  VAL D CB  1 
ATOM   4043 C  CG1 . VAL D 1 97  ? 33.066  -70.350 18.933 1.00 81.04  ? 97  VAL D CG1 1 
ATOM   4044 C  CG2 . VAL D 1 97  ? 32.851  -70.854 21.349 1.00 81.68  ? 97  VAL D CG2 1 
ATOM   4045 N  N   . SER D 1 98  ? 35.847  -69.444 18.340 1.00 83.89  ? 98  SER D N   1 
ATOM   4046 C  CA  . SER D 1 98  ? 36.184  -68.857 17.053 1.00 84.84  ? 98  SER D CA  1 
ATOM   4047 C  C   . SER D 1 98  ? 36.544  -69.950 16.053 1.00 83.84  ? 98  SER D C   1 
ATOM   4048 O  O   . SER D 1 98  ? 37.510  -70.686 16.243 1.00 84.22  ? 98  SER D O   1 
ATOM   4049 C  CB  . SER D 1 98  ? 37.333  -67.862 17.186 1.00 88.34  ? 98  SER D CB  1 
ATOM   4050 O  OG  . SER D 1 98  ? 37.581  -67.219 15.948 1.00 89.80  ? 98  SER D OG  1 
ATOM   4051 N  N   . ILE D 1 99  ? 35.759  -70.038 14.985 1.00 82.91  ? 99  ILE D N   1 
ATOM   4052 C  CA  . ILE D 1 99  ? 35.790  -71.169 14.059 1.00 82.28  ? 99  ILE D CA  1 
ATOM   4053 C  C   . ILE D 1 99  ? 35.449  -70.730 12.656 1.00 84.22  ? 99  ILE D C   1 
ATOM   4054 O  O   . ILE D 1 99  ? 34.542  -69.961 12.479 1.00 84.63  ? 99  ILE D O   1 
ATOM   4055 C  CB  . ILE D 1 99  ? 34.706  -72.200 14.421 1.00 79.01  ? 99  ILE D CB  1 
ATOM   4056 C  CG1 . ILE D 1 99  ? 34.905  -72.726 15.827 1.00 77.31  ? 99  ILE D CG1 1 
ATOM   4057 C  CG2 . ILE D 1 99  ? 34.693  -73.342 13.440 1.00 78.54  ? 99  ILE D CG2 1 
ATOM   4058 C  CD1 . ILE D 1 99  ? 34.222  -74.024 16.076 1.00 74.01  ? 99  ILE D CD1 1 
ATOM   4059 N  N   . GLU D 1 100 ? 36.149  -71.232 11.654 1.00 86.58  ? 100 GLU D N   1 
ATOM   4060 C  CA  . GLU D 1 100 ? 35.662  -71.144 10.278 1.00 88.57  ? 100 GLU D CA  1 
ATOM   4061 C  C   . GLU D 1 100 ? 35.187  -72.506 9.902  1.00 87.01  ? 100 GLU D C   1 
ATOM   4062 O  O   . GLU D 1 100 ? 35.767  -73.499 10.343 1.00 86.66  ? 100 GLU D O   1 
ATOM   4063 C  CB  . GLU D 1 100 ? 36.768  -70.769 9.306  1.00 92.98  ? 100 GLU D CB  1 
ATOM   4064 C  CG  . GLU D 1 100 ? 37.088  -69.279 9.255  1.00 97.92  ? 100 GLU D CG  1 
ATOM   4065 C  CD  . GLU D 1 100 ? 37.593  -68.820 7.893  1.00 105.58 ? 100 GLU D CD  1 
ATOM   4066 O  OE1 . GLU D 1 100 ? 37.509  -69.608 6.905  1.00 108.18 ? 100 GLU D OE1 1 
ATOM   4067 O  OE2 . GLU D 1 100 ? 38.058  -67.653 7.825  1.00 110.82 ? 100 GLU D OE2 1 
ATOM   4068 N  N   . ASP D 1 101 ? 34.148  -72.573 9.083  1.00 86.82  ? 101 ASP D N   1 
ATOM   4069 C  CA  . ASP D 1 101 ? 33.659  -73.860 8.612  1.00 86.41  ? 101 ASP D CA  1 
ATOM   4070 C  C   . ASP D 1 101 ? 32.872  -73.657 7.357  1.00 88.05  ? 101 ASP D C   1 
ATOM   4071 O  O   . ASP D 1 101 ? 32.130  -72.698 7.260  1.00 88.34  ? 101 ASP D O   1 
ATOM   4072 C  CB  . ASP D 1 101 ? 32.736  -74.497 9.641  1.00 83.47  ? 101 ASP D CB  1 
ATOM   4073 C  CG  . ASP D 1 101 ? 32.386  -75.927 9.290  1.00 84.69  ? 101 ASP D CG  1 
ATOM   4074 O  OD1 . ASP D 1 101 ? 33.166  -76.821 9.680  1.00 86.65  ? 101 ASP D OD1 1 
ATOM   4075 O  OD2 . ASP D 1 101 ? 31.344  -76.164 8.636  1.00 86.73  ? 101 ASP D OD2 1 
ATOM   4076 N  N   . SER D 1 102 ? 33.001  -74.561 6.401  1.00 89.65  ? 102 SER D N   1 
ATOM   4077 C  CA  . SER D 1 102 ? 32.319  -74.384 5.122  1.00 92.20  ? 102 SER D CA  1 
ATOM   4078 C  C   . SER D 1 102 ? 31.441  -75.560 4.729  1.00 91.77  ? 102 SER D C   1 
ATOM   4079 O  O   . SER D 1 102 ? 30.989  -75.654 3.600  1.00 94.68  ? 102 SER D O   1 
ATOM   4080 C  CB  . SER D 1 102 ? 33.358  -74.099 4.057  1.00 96.50  ? 102 SER D CB  1 
ATOM   4081 O  OG  . SER D 1 102 ? 34.587  -74.622 4.499  1.00 97.36  ? 102 SER D OG  1 
ATOM   4082 N  N   . VAL D 1 103 ? 31.192  -76.456 5.671  1.00 88.65  ? 103 VAL D N   1 
ATOM   4083 C  CA  . VAL D 1 103 ? 30.166  -77.470 5.486  1.00 88.25  ? 103 VAL D CA  1 
ATOM   4084 C  C   . VAL D 1 103 ? 28.806  -76.867 5.805  1.00 86.59  ? 103 VAL D C   1 
ATOM   4085 O  O   . VAL D 1 103 ? 27.847  -77.076 5.070  1.00 88.55  ? 103 VAL D O   1 
ATOM   4086 C  CB  . VAL D 1 103 ? 30.401  -78.698 6.367  1.00 86.18  ? 103 VAL D CB  1 
ATOM   4087 C  CG1 . VAL D 1 103 ? 29.145  -79.535 6.428  1.00 85.78  ? 103 VAL D CG1 1 
ATOM   4088 C  CG2 . VAL D 1 103 ? 31.535  -79.516 5.809  1.00 88.76  ? 103 VAL D CG2 1 
ATOM   4089 N  N   . ILE D 1 104 ? 28.724  -76.129 6.907  1.00 83.47  ? 104 ILE D N   1 
ATOM   4090 C  CA  . ILE D 1 104 ? 27.493  -75.439 7.251  1.00 82.31  ? 104 ILE D CA  1 
ATOM   4091 C  C   . ILE D 1 104 ? 27.379  -74.207 6.389  1.00 85.08  ? 104 ILE D C   1 
ATOM   4092 O  O   . ILE D 1 104 ? 28.374  -73.775 5.820  1.00 87.07  ? 104 ILE D O   1 
ATOM   4093 C  CB  . ILE D 1 104 ? 27.431  -75.008 8.722  1.00 79.00  ? 104 ILE D CB  1 
ATOM   4094 C  CG1 . ILE D 1 104 ? 28.510  -73.976 9.040  1.00 78.63  ? 104 ILE D CG1 1 
ATOM   4095 C  CG2 . ILE D 1 104 ? 27.547  -76.198 9.623  1.00 76.80  ? 104 ILE D CG2 1 
ATOM   4096 C  CD1 . ILE D 1 104 ? 28.581  -73.656 10.463 1.00 75.79  ? 104 ILE D CD1 1 
ATOM   4097 N  N   . SER D 1 105 ? 26.163  -73.653 6.320  1.00 85.86  ? 105 SER D N   1 
ATOM   4098 C  CA  . SER D 1 105 ? 25.801  -72.505 5.462  1.00 88.93  ? 105 SER D CA  1 
ATOM   4099 C  C   . SER D 1 105 ? 24.652  -71.747 6.132  1.00 88.02  ? 105 SER D C   1 
ATOM   4100 O  O   . SER D 1 105 ? 23.889  -72.322 6.917  1.00 85.72  ? 105 SER D O   1 
ATOM   4101 C  CB  . SER D 1 105 ? 25.367  -73.007 4.056  1.00 92.81  ? 105 SER D CB  1 
ATOM   4102 O  OG  . SER D 1 105 ? 25.442  -72.000 3.044  1.00 96.57  ? 105 SER D OG  1 
ATOM   4103 N  N   . LEU D 1 106 ? 24.528  -70.460 5.831  1.00 90.39  ? 106 LEU D N   1 
ATOM   4104 C  CA  . LEU D 1 106 ? 23.356  -69.692 6.265  1.00 90.96  ? 106 LEU D CA  1 
ATOM   4105 C  C   . LEU D 1 106 ? 22.264  -69.590 5.186  1.00 95.42  ? 106 LEU D C   1 
ATOM   4106 O  O   . LEU D 1 106 ? 21.159  -69.096 5.452  1.00 96.09  ? 106 LEU D O   1 
ATOM   4107 C  CB  . LEU D 1 106 ? 23.774  -68.306 6.728  1.00 90.93  ? 106 LEU D CB  1 
ATOM   4108 C  CG  . LEU D 1 106 ? 24.790  -68.286 7.880  1.00 86.79  ? 106 LEU D CG  1 
ATOM   4109 C  CD1 . LEU D 1 106 ? 24.765  -66.967 8.620  1.00 86.00  ? 106 LEU D CD1 1 
ATOM   4110 C  CD2 . LEU D 1 106 ? 24.520  -69.388 8.848  1.00 82.43  ? 106 LEU D CD2 1 
ATOM   4111 N  N   . SER D 1 107 ? 22.592  -70.062 3.982  1.00 99.36  ? 107 SER D N   1 
ATOM   4112 C  CA  . SER D 1 107 ? 21.647  -70.209 2.875  1.00 103.82 ? 107 SER D CA  1 
ATOM   4113 C  C   . SER D 1 107 ? 21.794  -71.630 2.342  1.00 105.15 ? 107 SER D C   1 
ATOM   4114 O  O   . SER D 1 107 ? 22.582  -72.417 2.863  1.00 102.83 ? 107 SER D O   1 
ATOM   4115 C  CB  . SER D 1 107 ? 21.953  -69.157 1.794  1.00 108.24 ? 107 SER D CB  1 
ATOM   4116 O  OG  . SER D 1 107 ? 23.332  -69.149 1.429  1.00 108.87 ? 107 SER D OG  1 
ATOM   4117 N  N   . GLY D 1 108 ? 21.038  -71.976 1.312  1.00 109.95 ? 108 GLY D N   1 
ATOM   4118 C  CA  . GLY D 1 108 ? 21.149  -73.312 0.701  1.00 112.04 ? 108 GLY D CA  1 
ATOM   4119 C  C   . GLY D 1 108 ? 20.470  -74.356 1.576  1.00 109.62 ? 108 GLY D C   1 
ATOM   4120 O  O   . GLY D 1 108 ? 19.757  -74.016 2.534  1.00 107.20 ? 108 GLY D O   1 
ATOM   4121 N  N   . ASP D 1 109 ? 20.673  -75.628 1.251  1.00 110.90 ? 109 ASP D N   1 
ATOM   4122 C  CA  . ASP D 1 109 ? 19.984  -76.723 1.987  1.00 109.64 ? 109 ASP D CA  1 
ATOM   4123 C  C   . ASP D 1 109 ? 20.887  -77.344 3.088  1.00 104.83 ? 109 ASP D C   1 
ATOM   4124 O  O   . ASP D 1 109 ? 20.556  -78.375 3.718  1.00 103.32 ? 109 ASP D O   1 
ATOM   4125 C  CB  . ASP D 1 109 ? 19.391  -77.804 1.034  1.00 114.49 ? 109 ASP D CB  1 
ATOM   4126 C  CG  . ASP D 1 109 ? 20.294  -78.101 -0.202 1.00 120.08 ? 109 ASP D CG  1 
ATOM   4127 O  OD1 . ASP D 1 109 ? 19.879  -77.713 -1.339 1.00 125.81 ? 109 ASP D OD1 1 
ATOM   4128 O  OD2 . ASP D 1 109 ? 21.406  -78.700 -0.029 1.00 120.69 ? 109 ASP D OD2 1 
ATOM   4129 N  N   . HIS D 1 110 ? 22.035  -76.706 3.307  1.00 102.46 ? 110 HIS D N   1 
ATOM   4130 C  CA  . HIS D 1 110 ? 22.772  -76.882 4.550  1.00 97.90  ? 110 HIS D CA  1 
ATOM   4131 C  C   . HIS D 1 110 ? 22.453  -75.708 5.506  1.00 93.99  ? 110 HIS D C   1 
ATOM   4132 O  O   . HIS D 1 110 ? 23.125  -75.548 6.525  1.00 90.90  ? 110 HIS D O   1 
ATOM   4133 C  CB  . HIS D 1 110 ? 24.283  -76.974 4.261  1.00 98.50  ? 110 HIS D CB  1 
ATOM   4134 C  CG  . HIS D 1 110 ? 24.689  -78.211 3.509  1.00 103.36 ? 110 HIS D CG  1 
ATOM   4135 N  ND1 . HIS D 1 110 ? 26.005  -78.629 3.420  1.00 105.26 ? 110 HIS D ND1 1 
ATOM   4136 C  CD2 . HIS D 1 110 ? 23.953  -79.138 2.841  1.00 108.14 ? 110 HIS D CD2 1 
ATOM   4137 C  CE1 . HIS D 1 110 ? 26.061  -79.750 2.722  1.00 108.97 ? 110 HIS D CE1 1 
ATOM   4138 N  NE2 . HIS D 1 110 ? 24.832  -80.081 2.359  1.00 111.17 ? 110 HIS D NE2 1 
ATOM   4139 N  N   . CYS D 1 111 ? 21.432  -74.900 5.175  1.00 94.06  ? 111 CYS D N   1 
ATOM   4140 C  CA  . CYS D 1 111 ? 21.059  -73.712 5.954  1.00 90.86  ? 111 CYS D CA  1 
ATOM   4141 C  C   . CYS D 1 111 ? 20.757  -74.213 7.361  1.00 86.73  ? 111 CYS D C   1 
ATOM   4142 O  O   . CYS D 1 111 ? 19.982  -75.170 7.526  1.00 86.88  ? 111 CYS D O   1 
ATOM   4143 C  CB  . CYS D 1 111 ? 19.853  -73.017 5.316  1.00 93.61  ? 111 CYS D CB  1 
ATOM   4144 S  SG  . CYS D 1 111 ? 19.170  -71.675 6.209  1.00 90.94  ? 111 CYS D SG  1 
ATOM   4145 N  N   . ILE D 1 112 ? 21.424  -73.619 8.355  1.00 82.87  ? 112 ILE D N   1 
ATOM   4146 C  CA  . ILE D 1 112 ? 21.268  -74.019 9.767  1.00 79.21  ? 112 ILE D CA  1 
ATOM   4147 C  C   . ILE D 1 112 ? 20.381  -73.050 10.549 1.00 78.74  ? 112 ILE D C   1 
ATOM   4148 O  O   . ILE D 1 112 ? 20.205  -73.175 11.769 1.00 77.13  ? 112 ILE D O   1 
ATOM   4149 C  CB  . ILE D 1 112 ? 22.626  -74.139 10.491 1.00 76.65  ? 112 ILE D CB  1 
ATOM   4150 C  CG1 . ILE D 1 112 ? 23.317  -72.783 10.622 1.00 75.51  ? 112 ILE D CG1 1 
ATOM   4151 C  CG2 . ILE D 1 112 ? 23.521  -75.092 9.757  1.00 77.46  ? 112 ILE D CG2 1 
ATOM   4152 C  CD1 . ILE D 1 112 ? 24.516  -72.810 11.514 1.00 71.63  ? 112 ILE D CD1 1 
ATOM   4153 N  N   . ILE D 1 113 ? 19.837  -72.062 9.849  1.00 80.39  ? 113 ILE D N   1 
ATOM   4154 C  CA  . ILE D 1 113 ? 19.005  -71.081 10.491 1.00 80.36  ? 113 ILE D CA  1 
ATOM   4155 C  C   . ILE D 1 113 ? 17.748  -71.772 10.920 1.00 80.32  ? 113 ILE D C   1 
ATOM   4156 O  O   . ILE D 1 113 ? 17.094  -72.422 10.112 1.00 81.86  ? 113 ILE D O   1 
ATOM   4157 C  CB  . ILE D 1 113 ? 18.713  -69.923 9.553  1.00 83.12  ? 113 ILE D CB  1 
ATOM   4158 C  CG1 . ILE D 1 113 ? 19.921  -68.991 9.553  1.00 82.83  ? 113 ILE D CG1 1 
ATOM   4159 C  CG2 . ILE D 1 113 ? 17.475  -69.173 9.999  1.00 84.59  ? 113 ILE D CG2 1 
ATOM   4160 C  CD1 . ILE D 1 113 ? 19.837  -67.919 8.570  1.00 87.53  ? 113 ILE D CD1 1 
ATOM   4161 N  N   . GLY D 1 114 ? 17.436  -71.649 12.203 1.00 78.80  ? 114 GLY D N   1 
ATOM   4162 C  CA  . GLY D 1 114 ? 16.241  -72.258 12.734 1.00 79.65  ? 114 GLY D CA  1 
ATOM   4163 C  C   . GLY D 1 114 ? 16.499  -73.600 13.363 1.00 78.06  ? 114 GLY D C   1 
ATOM   4164 O  O   . GLY D 1 114 ? 15.566  -74.336 13.675 1.00 79.04  ? 114 GLY D O   1 
ATOM   4165 N  N   . ARG D 1 115 ? 17.769  -73.917 13.554 1.00 75.96  ? 115 ARG D N   1 
ATOM   4166 C  CA  . ARG D 1 115 ? 18.138  -75.174 14.159 1.00 74.94  ? 115 ARG D CA  1 
ATOM   4167 C  C   . ARG D 1 115 ? 18.844  -74.864 15.454 1.00 73.21  ? 115 ARG D C   1 
ATOM   4168 O  O   . ARG D 1 115 ? 19.331  -73.756 15.630 1.00 72.82  ? 115 ARG D O   1 
ATOM   4169 C  CB  . ARG D 1 115 ? 19.009  -75.962 13.204 1.00 74.63  ? 115 ARG D CB  1 
ATOM   4170 C  CG  . ARG D 1 115 ? 18.373  -76.114 11.844 1.00 77.25  ? 115 ARG D CG  1 
ATOM   4171 C  CD  . ARG D 1 115 ? 19.124  -77.093 10.962 1.00 78.38  ? 115 ARG D CD  1 
ATOM   4172 N  NE  . ARG D 1 115 ? 18.490  -77.249 9.649  1.00 81.52  ? 115 ARG D NE  1 
ATOM   4173 C  CZ  . ARG D 1 115 ? 17.470  -78.072 9.381  1.00 84.72  ? 115 ARG D CZ  1 
ATOM   4174 N  NH1 . ARG D 1 115 ? 16.941  -78.859 10.318 1.00 85.60  ? 115 ARG D NH1 1 
ATOM   4175 N  NH2 . ARG D 1 115 ? 16.975  -78.122 8.159  1.00 87.99  ? 115 ARG D NH2 1 
ATOM   4176 N  N   . THR D 1 116 ? 18.850  -75.818 16.377 1.00 72.85  ? 116 THR D N   1 
ATOM   4177 C  CA  . THR D 1 116 ? 19.385  -75.556 17.692 1.00 72.24  ? 116 THR D CA  1 
ATOM   4178 C  C   . THR D 1 116 ? 20.870  -75.781 17.671 1.00 70.15  ? 116 THR D C   1 
ATOM   4179 O  O   . THR D 1 116 ? 21.348  -76.728 17.085 1.00 69.81  ? 116 THR D O   1 
ATOM   4180 C  CB  . THR D 1 116 ? 18.747  -76.434 18.790 1.00 73.61  ? 116 THR D CB  1 
ATOM   4181 O  OG1 . THR D 1 116 ? 17.327  -76.222 18.849 1.00 76.84  ? 116 THR D OG1 1 
ATOM   4182 C  CG2 . THR D 1 116 ? 19.304  -76.060 20.137 1.00 74.48  ? 116 THR D CG2 1 
ATOM   4183 N  N   . LEU D 1 117 ? 21.587  -74.863 18.288 1.00 69.44  ? 117 LEU D N   1 
ATOM   4184 C  CA  . LEU D 1 117 ? 22.993  -75.011 18.547 1.00 68.44  ? 117 LEU D CA  1 
ATOM   4185 C  C   . LEU D 1 117 ? 23.099  -75.556 19.940 1.00 69.14  ? 117 LEU D C   1 
ATOM   4186 O  O   . LEU D 1 117 ? 22.346  -75.154 20.784 1.00 70.78  ? 117 LEU D O   1 
ATOM   4187 C  CB  . LEU D 1 117 ? 23.646  -73.646 18.502 1.00 68.27  ? 117 LEU D CB  1 
ATOM   4188 C  CG  . LEU D 1 117 ? 25.139  -73.602 18.746 1.00 66.95  ? 117 LEU D CG  1 
ATOM   4189 C  CD1 . LEU D 1 117 ? 25.801  -74.376 17.634 1.00 66.20  ? 117 LEU D CD1 1 
ATOM   4190 C  CD2 . LEU D 1 117 ? 25.655  -72.181 18.789 1.00 66.23  ? 117 LEU D CD2 1 
ATOM   4191 N  N   . VAL D 1 118 ? 24.036  -76.449 20.202 1.00 68.99  ? 118 VAL D N   1 
ATOM   4192 C  CA  . VAL D 1 118 ? 24.133  -77.056 21.515 1.00 70.17  ? 118 VAL D CA  1 
ATOM   4193 C  C   . VAL D 1 118 ? 25.573  -77.169 21.945 1.00 70.21  ? 118 VAL D C   1 
ATOM   4194 O  O   . VAL D 1 118 ? 26.431  -77.508 21.141 1.00 69.51  ? 118 VAL D O   1 
ATOM   4195 C  CB  . VAL D 1 118 ? 23.567  -78.450 21.486 1.00 70.88  ? 118 VAL D CB  1 
ATOM   4196 C  CG1 . VAL D 1 118 ? 23.682  -79.090 22.841 1.00 72.66  ? 118 VAL D CG1 1 
ATOM   4197 C  CG2 . VAL D 1 118 ? 22.149  -78.397 21.051 1.00 72.05  ? 118 VAL D CG2 1 
ATOM   4198 N  N   . VAL D 1 119 ? 25.835  -76.885 23.214 1.00 71.73  ? 119 VAL D N   1 
ATOM   4199 C  CA  . VAL D 1 119 ? 27.143  -77.122 23.809 1.00 72.66  ? 119 VAL D CA  1 
ATOM   4200 C  C   . VAL D 1 119 ? 26.967  -78.206 24.861 1.00 75.29  ? 119 VAL D C   1 
ATOM   4201 O  O   . VAL D 1 119 ? 25.951  -78.228 25.555 1.00 77.00  ? 119 VAL D O   1 
ATOM   4202 C  CB  . VAL D 1 119 ? 27.703  -75.871 24.455 1.00 73.25  ? 119 VAL D CB  1 
ATOM   4203 C  CG1 . VAL D 1 119 ? 26.775  -75.380 25.512 1.00 75.21  ? 119 VAL D CG1 1 
ATOM   4204 C  CG2 . VAL D 1 119 ? 29.031  -76.158 25.063 1.00 74.13  ? 119 VAL D CG2 1 
ATOM   4205 N  N   . HIS D 1 120 ? 27.950  -79.095 24.986 1.00 76.62  ? 120 HIS D N   1 
ATOM   4206 C  CA  . HIS D 1 120 ? 27.757  -80.359 25.694 1.00 79.21  ? 120 HIS D CA  1 
ATOM   4207 C  C   . HIS D 1 120 ? 28.583  -80.496 26.968 1.00 82.23  ? 120 HIS D C   1 
ATOM   4208 O  O   . HIS D 1 120 ? 29.513  -79.729 27.219 1.00 82.20  ? 120 HIS D O   1 
ATOM   4209 C  CB  . HIS D 1 120 ? 28.100  -81.521 24.764 1.00 78.69  ? 120 HIS D CB  1 
ATOM   4210 C  CG  . HIS D 1 120 ? 27.051  -81.821 23.740 1.00 78.87  ? 120 HIS D CG  1 
ATOM   4211 N  ND1 . HIS D 1 120 ? 26.202  -82.906 23.843 1.00 82.86  ? 120 HIS D ND1 1 
ATOM   4212 C  CD2 . HIS D 1 120 ? 26.740  -81.210 22.572 1.00 78.07  ? 120 HIS D CD2 1 
ATOM   4213 C  CE1 . HIS D 1 120 ? 25.403  -82.941 22.790 1.00 82.87  ? 120 HIS D CE1 1 
ATOM   4214 N  NE2 . HIS D 1 120 ? 25.706  -81.919 22.005 1.00 79.76  ? 120 HIS D NE2 1 
ATOM   4215 N  N   . GLU D 1 121 ? 28.235  -81.525 27.738 1.00 85.44  ? 121 GLU D N   1 
ATOM   4216 C  CA  . GLU D 1 121 ? 28.874  -81.837 29.007 1.00 89.22  ? 121 GLU D CA  1 
ATOM   4217 C  C   . GLU D 1 121 ? 30.359  -82.128 28.864 1.00 89.17  ? 121 GLU D C   1 
ATOM   4218 O  O   . GLU D 1 121 ? 31.138  -81.512 29.556 1.00 90.48  ? 121 GLU D O   1 
ATOM   4219 C  CB  . GLU D 1 121 ? 28.180  -83.033 29.657 1.00 92.53  ? 121 GLU D CB  1 
ATOM   4220 C  CG  . GLU D 1 121 ? 28.604  -83.293 31.112 1.00 98.85  ? 121 GLU D CG  1 
ATOM   4221 C  CD  . GLU D 1 121 ? 28.005  -84.588 31.706 1.00 105.05 ? 121 GLU D CD  1 
ATOM   4222 O  OE1 . GLU D 1 121 ? 27.514  -85.471 30.930 1.00 104.98 ? 121 GLU D OE1 1 
ATOM   4223 O  OE2 . GLU D 1 121 ? 28.040  -84.717 32.962 1.00 110.87 ? 121 GLU D OE2 1 
ATOM   4224 N  N   . LYS D 1 122 ? 30.732  -83.064 27.985 1.00 88.33  ? 122 LYS D N   1 
ATOM   4225 C  CA  . LYS D 1 122 ? 32.139  -83.500 27.813 1.00 89.61  ? 122 LYS D CA  1 
ATOM   4226 C  C   . LYS D 1 122 ? 32.675  -83.185 26.422 1.00 86.40  ? 122 LYS D C   1 
ATOM   4227 O  O   . LYS D 1 122 ? 32.008  -82.549 25.615 1.00 84.08  ? 122 LYS D O   1 
ATOM   4228 C  CB  . LYS D 1 122 ? 32.310  -85.018 28.006 1.00 92.40  ? 122 LYS D CB  1 
ATOM   4229 C  CG  . LYS D 1 122 ? 31.401  -85.673 29.023 1.00 97.29  ? 122 LYS D CG  1 
ATOM   4230 C  CD  . LYS D 1 122 ? 31.628  -87.196 29.069 1.00 102.05 ? 122 LYS D CD  1 
ATOM   4231 C  CE  . LYS D 1 122 ? 30.304  -87.938 29.301 1.00 104.80 ? 122 LYS D CE  1 
ATOM   4232 N  NZ  . LYS D 1 122 ? 30.485  -89.390 29.509 1.00 109.08 ? 122 LYS D NZ  1 
ATOM   4233 N  N   . ALA D 1 123 ? 33.884  -83.668 26.151 1.00 86.75  ? 123 ALA D N   1 
ATOM   4234 C  CA  . ALA D 1 123 ? 34.496  -83.523 24.848 1.00 84.36  ? 123 ALA D CA  1 
ATOM   4235 C  C   . ALA D 1 123 ? 33.801  -84.401 23.837 1.00 82.87  ? 123 ALA D C   1 
ATOM   4236 O  O   . ALA D 1 123 ? 33.332  -85.479 24.175 1.00 83.96  ? 123 ALA D O   1 
ATOM   4237 C  CB  . ALA D 1 123 ? 35.931  -83.896 24.925 1.00 86.53  ? 123 ALA D CB  1 
ATOM   4238 N  N   . ASP D 1 124 ? 33.690  -83.880 22.615 1.00 80.54  ? 124 ASP D N   1 
ATOM   4239 C  CA  . ASP D 1 124 ? 33.317  -84.638 21.402 1.00 79.96  ? 124 ASP D CA  1 
ATOM   4240 C  C   . ASP D 1 124 ? 34.556  -85.444 21.110 1.00 81.25  ? 124 ASP D C   1 
ATOM   4241 O  O   . ASP D 1 124 ? 35.638  -84.914 21.167 1.00 81.54  ? 124 ASP D O   1 
ATOM   4242 C  CB  . ASP D 1 124 ? 32.963  -83.655 20.232 1.00 77.91  ? 124 ASP D CB  1 
ATOM   4243 C  CG  . ASP D 1 124 ? 32.501  -84.351 18.930 1.00 78.78  ? 124 ASP D CG  1 
ATOM   4244 O  OD1 . ASP D 1 124 ? 32.540  -85.603 18.895 1.00 81.78  ? 124 ASP D OD1 1 
ATOM   4245 O  OD2 . ASP D 1 124 ? 32.114  -83.640 17.941 1.00 77.64  ? 124 ASP D OD2 1 
ATOM   4246 N  N   . ASP D 1 125 ? 34.414  -86.729 20.847 1.00 82.47  ? 125 ASP D N   1 
ATOM   4247 C  CA  . ASP D 1 125 ? 35.574  -87.551 20.570 1.00 84.59  ? 125 ASP D CA  1 
ATOM   4248 C  C   . ASP D 1 125 ? 35.779  -87.711 19.082 1.00 84.13  ? 125 ASP D C   1 
ATOM   4249 O  O   . ASP D 1 125 ? 36.554  -88.546 18.661 1.00 86.02  ? 125 ASP D O   1 
ATOM   4250 C  CB  . ASP D 1 125 ? 35.478  -88.919 21.277 1.00 87.65  ? 125 ASP D CB  1 
ATOM   4251 C  CG  . ASP D 1 125 ? 34.429  -89.861 20.658 1.00 88.52  ? 125 ASP D CG  1 
ATOM   4252 O  OD1 . ASP D 1 125 ? 34.044  -89.640 19.483 1.00 87.67  ? 125 ASP D OD1 1 
ATOM   4253 O  OD2 . ASP D 1 125 ? 34.002  -90.829 21.348 1.00 90.45  ? 125 ASP D OD2 1 
ATOM   4254 N  N   . LEU D 1 126 ? 35.047  -86.930 18.301 1.00 82.01  ? 126 LEU D N   1 
ATOM   4255 C  CA  . LEU D 1 126 ? 35.230  -86.828 16.858 1.00 82.39  ? 126 LEU D CA  1 
ATOM   4256 C  C   . LEU D 1 126 ? 35.007  -88.135 16.102 1.00 85.02  ? 126 LEU D C   1 
ATOM   4257 O  O   . LEU D 1 126 ? 35.511  -88.328 14.982 1.00 86.39  ? 126 LEU D O   1 
ATOM   4258 C  CB  . LEU D 1 126 ? 36.604  -86.221 16.536 1.00 83.02  ? 126 LEU D CB  1 
ATOM   4259 C  CG  . LEU D 1 126 ? 37.006  -84.992 17.344 1.00 80.95  ? 126 LEU D CG  1 
ATOM   4260 C  CD1 . LEU D 1 126 ? 38.136  -84.225 16.609 1.00 81.38  ? 126 LEU D CD1 1 
ATOM   4261 C  CD2 . LEU D 1 126 ? 35.794  -84.130 17.595 1.00 77.17  ? 126 LEU D CD2 1 
ATOM   4262 N  N   . GLY D 1 127 ? 34.234  -89.021 16.710 1.00 86.46  ? 127 GLY D N   1 
ATOM   4263 C  CA  . GLY D 1 127 ? 33.899  -90.295 16.089 1.00 89.87  ? 127 GLY D CA  1 
ATOM   4264 C  C   . GLY D 1 127 ? 34.886  -91.421 16.326 1.00 93.98  ? 127 GLY D C   1 
ATOM   4265 O  O   . GLY D 1 127 ? 34.635  -92.531 15.904 1.00 96.65  ? 127 GLY D O   1 
ATOM   4266 N  N   . LYS D 1 128 ? 35.992  -91.146 17.023 1.00 95.23  ? 128 LYS D N   1 
ATOM   4267 C  CA  . LYS D 1 128 ? 37.107  -92.102 17.144 1.00 99.52  ? 128 LYS D CA  1 
ATOM   4268 C  C   . LYS D 1 128 ? 37.139  -92.803 18.486 1.00 101.03 ? 128 LYS D C   1 
ATOM   4269 O  O   . LYS D 1 128 ? 38.205  -93.250 18.903 1.00 103.58 ? 128 LYS D O   1 
ATOM   4270 C  CB  . LYS D 1 128 ? 38.458  -91.392 16.935 1.00 100.26 ? 128 LYS D CB  1 
ATOM   4271 C  CG  . LYS D 1 128 ? 38.425  -90.245 15.883 1.00 100.68 ? 128 LYS D CG  1 
ATOM   4272 C  CD  . LYS D 1 128 ? 39.809  -89.908 15.304 1.00 105.89 ? 128 LYS D CD  1 
ATOM   4273 C  CE  . LYS D 1 128 ? 39.779  -88.599 14.504 1.00 105.61 ? 128 LYS D CE  1 
ATOM   4274 N  NZ  . LYS D 1 128 ? 38.926  -88.752 13.275 1.00 106.59 ? 128 LYS D NZ  1 
ATOM   4275 N  N   . GLY D 1 129 ? 35.988  -92.891 19.155 1.00 100.27 ? 129 GLY D N   1 
ATOM   4276 C  CA  . GLY D 1 129 ? 35.880  -93.524 20.495 1.00 102.56 ? 129 GLY D CA  1 
ATOM   4277 C  C   . GLY D 1 129 ? 35.655  -95.033 20.411 1.00 106.75 ? 129 GLY D C   1 
ATOM   4278 O  O   . GLY D 1 129 ? 35.683  -95.756 21.427 1.00 109.40 ? 129 GLY D O   1 
ATOM   4279 N  N   . GLY D 1 130 ? 35.386  -95.491 19.188 1.00 107.61 ? 130 GLY D N   1 
ATOM   4280 C  CA  . GLY D 1 130 ? 35.223  -96.899 18.915 1.00 112.25 ? 130 GLY D CA  1 
ATOM   4281 C  C   . GLY D 1 130 ? 34.051  -97.556 19.602 1.00 114.04 ? 130 GLY D C   1 
ATOM   4282 O  O   . GLY D 1 130 ? 33.981  -98.767 19.687 1.00 118.40 ? 130 GLY D O   1 
ATOM   4283 N  N   . ASN D 1 131 ? 33.122  -96.774 20.106 1.00 111.51 ? 131 ASN D N   1 
ATOM   4284 C  CA  . ASN D 1 131 ? 31.934  -97.368 20.662 1.00 113.86 ? 131 ASN D CA  1 
ATOM   4285 C  C   . ASN D 1 131 ? 30.753  -96.923 19.804 1.00 112.14 ? 131 ASN D C   1 
ATOM   4286 O  O   . ASN D 1 131 ? 30.913  -96.090 18.913 1.00 108.92 ? 131 ASN D O   1 
ATOM   4287 C  CB  . ASN D 1 131 ? 31.815  -97.073 22.163 1.00 113.99 ? 131 ASN D CB  1 
ATOM   4288 C  CG  . ASN D 1 131 ? 31.108  -95.807 22.448 1.00 109.49 ? 131 ASN D CG  1 
ATOM   4289 O  OD1 . ASN D 1 131 ? 31.393  -94.786 21.841 1.00 105.38 ? 131 ASN D OD1 1 
ATOM   4290 N  ND2 . ASN D 1 131 ? 30.174  -95.853 23.392 1.00 110.38 ? 131 ASN D ND2 1 
ATOM   4291 N  N   . GLU D 1 132 ? 29.602  -97.544 20.001 1.00 115.24 ? 132 GLU D N   1 
ATOM   4292 C  CA  . GLU D 1 132 ? 28.451  -97.309 19.115 1.00 115.25 ? 132 GLU D CA  1 
ATOM   4293 C  C   . GLU D 1 132 ? 28.087  -95.834 19.135 1.00 109.90 ? 132 GLU D C   1 
ATOM   4294 O  O   . GLU D 1 132 ? 27.971  -95.180 18.085 1.00 107.12 ? 132 GLU D O   1 
ATOM   4295 C  CB  . GLU D 1 132 ? 27.259  -98.184 19.564 1.00 119.85 ? 132 GLU D CB  1 
ATOM   4296 C  CG  . GLU D 1 132 ? 25.811  -97.624 19.288 1.00 121.15 ? 132 GLU D CG  1 
ATOM   4297 C  CD  . GLU D 1 132 ? 25.138  -98.169 18.004 1.00 126.38 ? 132 GLU D CD  1 
ATOM   4298 O  OE1 . GLU D 1 132 ? 25.466  -99.299 17.563 1.00 132.02 ? 132 GLU D OE1 1 
ATOM   4299 O  OE2 . GLU D 1 132 ? 24.257  -97.459 17.449 1.00 125.72 ? 132 GLU D OE2 1 
ATOM   4300 N  N   . GLU D 1 133 ? 27.954  -95.334 20.357 1.00 108.61 ? 133 GLU D N   1 
ATOM   4301 C  CA  . GLU D 1 133 ? 27.565  -93.968 20.623 1.00 104.67 ? 133 GLU D CA  1 
ATOM   4302 C  C   . GLU D 1 133 ? 28.510  -92.928 20.003 1.00 100.43 ? 133 GLU D C   1 
ATOM   4303 O  O   . GLU D 1 133 ? 28.089  -91.837 19.660 1.00 97.36  ? 133 GLU D O   1 
ATOM   4304 C  CB  . GLU D 1 133 ? 27.482  -93.768 22.143 1.00 105.77 ? 133 GLU D CB  1 
ATOM   4305 C  CG  . GLU D 1 133 ? 26.879  -92.434 22.603 1.00 104.44 ? 133 GLU D CG  1 
ATOM   4306 C  CD  . GLU D 1 133 ? 25.456  -92.223 22.093 1.00 107.09 ? 133 GLU D CD  1 
ATOM   4307 O  OE1 . GLU D 1 133 ? 24.691  -93.221 21.988 1.00 112.02 ? 133 GLU D OE1 1 
ATOM   4308 O  OE2 . GLU D 1 133 ? 25.107  -91.055 21.772 1.00 105.37 ? 133 GLU D OE2 1 
ATOM   4309 N  N   . SER D 1 134 ? 29.785  -93.250 19.845 1.00 100.63 ? 134 SER D N   1 
ATOM   4310 C  CA  . SER D 1 134 ? 30.725  -92.277 19.311 1.00 97.33  ? 134 SER D CA  1 
ATOM   4311 C  C   . SER D 1 134 ? 30.367  -91.901 17.888 1.00 95.92  ? 134 SER D C   1 
ATOM   4312 O  O   . SER D 1 134 ? 30.560  -90.767 17.517 1.00 93.64  ? 134 SER D O   1 
ATOM   4313 C  CB  . SER D 1 134 ? 32.164  -92.781 19.377 1.00 99.04  ? 134 SER D CB  1 
ATOM   4314 O  OG  . SER D 1 134 ? 33.044  -91.897 18.718 1.00 96.10  ? 134 SER D OG  1 
ATOM   4315 N  N   . THR D 1 135 ? 29.825  -92.815 17.091 1.00 98.00  ? 135 THR D N   1 
ATOM   4316 C  CA  . THR D 1 135 ? 29.482  -92.480 15.697 1.00 97.32  ? 135 THR D CA  1 
ATOM   4317 C  C   . THR D 1 135 ? 28.126  -91.777 15.574 1.00 95.50  ? 135 THR D C   1 
ATOM   4318 O  O   . THR D 1 135 ? 27.581  -91.631 14.475 1.00 95.61  ? 135 THR D O   1 
ATOM   4319 C  CB  . THR D 1 135 ? 29.464  -93.726 14.832 1.00 101.32 ? 135 THR D CB  1 
ATOM   4320 O  OG1 . THR D 1 135 ? 28.840  -94.765 15.592 1.00 103.87 ? 135 THR D OG1 1 
ATOM   4321 C  CG2 . THR D 1 135 ? 30.893  -94.126 14.396 1.00 102.24 ? 135 THR D CG2 1 
ATOM   4322 N  N   . LYS D 1 136 ? 27.609  -91.307 16.700 1.00 94.06  ? 136 LYS D N   1 
ATOM   4323 C  CA  . LYS D 1 136 ? 26.341  -90.593 16.727 1.00 93.09  ? 136 LYS D CA  1 
ATOM   4324 C  C   . LYS D 1 136 ? 26.457  -89.228 17.434 1.00 89.41  ? 136 LYS D C   1 
ATOM   4325 O  O   . LYS D 1 136 ? 26.167  -88.184 16.838 1.00 87.36  ? 136 LYS D O   1 
ATOM   4326 C  CB  . LYS D 1 136 ? 25.282  -91.458 17.404 1.00 95.99  ? 136 LYS D CB  1 
ATOM   4327 C  CG  . LYS D 1 136 ? 25.243  -92.879 16.860 1.00 102.18 ? 136 LYS D CG  1 
ATOM   4328 C  CD  . LYS D 1 136 ? 24.339  -93.808 17.695 1.00 108.27 ? 136 LYS D CD  1 
ATOM   4329 C  CE  . LYS D 1 136 ? 22.871  -93.427 17.620 1.00 109.47 ? 136 LYS D CE  1 
ATOM   4330 N  NZ  . LYS D 1 136 ? 22.031  -94.484 18.220 1.00 114.36 ? 136 LYS D NZ  1 
ATOM   4331 N  N   . THR D 1 137 ? 26.864  -89.230 18.697 1.00 88.87  ? 137 THR D N   1 
ATOM   4332 C  CA  . THR D 1 137 ? 27.022  -87.990 19.427 1.00 86.31  ? 137 THR D CA  1 
ATOM   4333 C  C   . THR D 1 137 ? 28.464  -87.692 19.737 1.00 85.03  ? 137 THR D C   1 
ATOM   4334 O  O   . THR D 1 137 ? 28.744  -86.700 20.399 1.00 83.88  ? 137 THR D O   1 
ATOM   4335 C  CB  . THR D 1 137 ? 26.266  -87.987 20.779 1.00 87.52  ? 137 THR D CB  1 
ATOM   4336 O  OG1 . THR D 1 137 ? 26.832  -88.965 21.662 1.00 90.45  ? 137 THR D OG1 1 
ATOM   4337 C  CG2 . THR D 1 137 ? 24.758  -88.226 20.560 1.00 89.12  ? 137 THR D CG2 1 
ATOM   4338 N  N   . GLY D 1 138 ? 29.386  -88.544 19.306 1.00 85.78  ? 138 GLY D N   1 
ATOM   4339 C  CA  . GLY D 1 138 ? 30.779  -88.386 19.730 1.00 85.39  ? 138 GLY D CA  1 
ATOM   4340 C  C   . GLY D 1 138 ? 30.985  -88.502 21.228 1.00 86.13  ? 138 GLY D C   1 
ATOM   4341 O  O   . GLY D 1 138 ? 31.963  -88.007 21.733 1.00 85.71  ? 138 GLY D O   1 
ATOM   4342 N  N   . ASN D 1 139 ? 30.063  -89.151 21.930 1.00 87.76  ? 139 ASN D N   1 
ATOM   4343 C  CA  . ASN D 1 139 ? 30.145  -89.314 23.383 1.00 89.86  ? 139 ASN D CA  1 
ATOM   4344 C  C   . ASN D 1 139 ? 30.239  -88.001 24.140 1.00 88.48  ? 139 ASN D C   1 
ATOM   4345 O  O   . ASN D 1 139 ? 30.832  -87.922 25.231 1.00 89.93  ? 139 ASN D O   1 
ATOM   4346 C  CB  . ASN D 1 139 ? 31.349  -90.183 23.766 1.00 92.52  ? 139 ASN D CB  1 
ATOM   4347 C  CG  . ASN D 1 139 ? 31.062  -91.653 23.661 1.00 95.66  ? 139 ASN D CG  1 
ATOM   4348 O  OD1 . ASN D 1 139 ? 29.892  -92.085 23.634 1.00 95.11  ? 139 ASN D OD1 1 
ATOM   4349 N  ND2 . ASN D 1 139 ? 32.139  -92.453 23.626 1.00 98.43  ? 139 ASN D ND2 1 
ATOM   4350 N  N   . ALA D 1 140 ? 29.639  -86.973 23.561 1.00 86.18  ? 140 ALA D N   1 
ATOM   4351 C  CA  . ALA D 1 140 ? 29.849  -85.606 24.035 1.00 84.95  ? 140 ALA D CA  1 
ATOM   4352 C  C   . ALA D 1 140 ? 29.097  -85.366 25.314 1.00 86.75  ? 140 ALA D C   1 
ATOM   4353 O  O   . ALA D 1 140 ? 29.374  -84.417 26.038 1.00 86.56  ? 140 ALA D O   1 
ATOM   4354 C  CB  . ALA D 1 140 ? 29.387  -84.637 23.006 1.00 82.32  ? 140 ALA D CB  1 
ATOM   4355 N  N   . GLY D 1 141 ? 28.112  -86.221 25.558 1.00 88.96  ? 141 GLY D N   1 
ATOM   4356 C  CA  . GLY D 1 141 ? 27.402  -86.223 26.810 1.00 91.68  ? 141 GLY D CA  1 
ATOM   4357 C  C   . GLY D 1 141 ? 26.150  -85.387 26.725 1.00 90.73  ? 141 GLY D C   1 
ATOM   4358 O  O   . GLY D 1 141 ? 25.683  -85.023 25.633 1.00 88.21  ? 141 GLY D O   1 
ATOM   4359 N  N   . SER D 1 142 ? 25.607  -85.096 27.900 1.00 93.32  ? 142 SER D N   1 
ATOM   4360 C  CA  . SER D 1 142 ? 24.344  -84.394 28.012 1.00 93.49  ? 142 SER D CA  1 
ATOM   4361 C  C   . SER D 1 142 ? 24.462  -82.966 27.472 1.00 90.20  ? 142 SER D C   1 
ATOM   4362 O  O   . SER D 1 142 ? 25.549  -82.494 27.118 1.00 88.21  ? 142 SER D O   1 
ATOM   4363 C  CB  . SER D 1 142 ? 23.875  -84.395 29.474 1.00 97.55  ? 142 SER D CB  1 
ATOM   4364 O  OG  . SER D 1 142 ? 24.858  -83.800 30.317 1.00 98.85  ? 142 SER D OG  1 
ATOM   4365 N  N   . ARG D 1 143 ? 23.329  -82.286 27.427 1.00 89.89  ? 143 ARG D N   1 
ATOM   4366 C  CA  . ARG D 1 143 ? 23.219  -81.045 26.703 1.00 87.34  ? 143 ARG D CA  1 
ATOM   4367 C  C   . ARG D 1 143 ? 23.172  -79.865 27.659 1.00 87.74  ? 143 ARG D C   1 
ATOM   4368 O  O   . ARG D 1 143 ? 22.113  -79.459 28.100 1.00 89.46  ? 143 ARG D O   1 
ATOM   4369 C  CB  . ARG D 1 143 ? 21.971  -81.117 25.828 1.00 87.21  ? 143 ARG D CB  1 
ATOM   4370 C  CG  . ARG D 1 143 ? 21.995  -82.348 24.926 1.00 88.86  ? 143 ARG D CG  1 
ATOM   4371 C  CD  . ARG D 1 143 ? 20.814  -82.409 23.982 1.00 91.29  ? 143 ARG D CD  1 
ATOM   4372 N  NE  . ARG D 1 143 ? 21.050  -83.367 22.899 1.00 92.56  ? 143 ARG D NE  1 
ATOM   4373 C  CZ  . ARG D 1 143 ? 20.169  -83.661 21.941 1.00 94.40  ? 143 ARG D CZ  1 
ATOM   4374 N  NH1 . ARG D 1 143 ? 18.964  -83.081 21.911 1.00 95.46  ? 143 ARG D NH1 1 
ATOM   4375 N  NH2 . ARG D 1 143 ? 20.490  -84.542 20.999 1.00 95.50  ? 143 ARG D NH2 1 
ATOM   4376 N  N   . LEU D 1 144 ? 24.332  -79.304 27.962 1.00 86.61  ? 144 LEU D N   1 
ATOM   4377 C  CA  . LEU D 1 144 ? 24.454  -78.301 29.021 1.00 88.34  ? 144 LEU D CA  1 
ATOM   4378 C  C   . LEU D 1 144 ? 23.684  -77.001 28.791 1.00 87.31  ? 144 LEU D C   1 
ATOM   4379 O  O   . LEU D 1 144 ? 23.067  -76.463 29.726 1.00 89.99  ? 144 LEU D O   1 
ATOM   4380 C  CB  . LEU D 1 144 ? 25.938  -77.977 29.264 1.00 88.56  ? 144 LEU D CB  1 
ATOM   4381 C  CG  . LEU D 1 144 ? 26.763  -78.974 30.105 1.00 91.71  ? 144 LEU D CG  1 
ATOM   4382 C  CD1 . LEU D 1 144 ? 28.192  -78.449 30.288 1.00 93.03  ? 144 LEU D CD1 1 
ATOM   4383 C  CD2 . LEU D 1 144 ? 26.134  -79.239 31.485 1.00 96.93  ? 144 LEU D CD2 1 
ATOM   4384 N  N   . ALA D 1 145 ? 23.754  -76.486 27.566 1.00 83.88  ? 145 ALA D N   1 
ATOM   4385 C  CA  . ALA D 1 145 ? 23.031  -75.262 27.176 1.00 83.45  ? 145 ALA D CA  1 
ATOM   4386 C  C   . ALA D 1 145 ? 22.724  -75.297 25.680 1.00 80.88  ? 145 ALA D C   1 
ATOM   4387 O  O   . ALA D 1 145 ? 23.387  -76.024 24.927 1.00 79.57  ? 145 ALA D O   1 
ATOM   4388 C  CB  . ALA D 1 145 ? 23.844  -74.028 27.510 1.00 83.65  ? 145 ALA D CB  1 
ATOM   4389 N  N   . CYS D 1 146 ? 21.719  -74.540 25.242 1.00 81.06  ? 146 CYS D N   1 
ATOM   4390 C  CA  . CYS D 1 146 ? 21.350  -74.517 23.824 1.00 79.22  ? 146 CYS D CA  1 
ATOM   4391 C  C   . CYS D 1 146 ? 20.447  -73.345 23.471 1.00 79.28  ? 146 CYS D C   1 
ATOM   4392 O  O   . CYS D 1 146 ? 19.875  -72.698 24.343 1.00 81.58  ? 146 CYS D O   1 
ATOM   4393 C  CB  . CYS D 1 146 ? 20.657  -75.822 23.426 1.00 79.43  ? 146 CYS D CB  1 
ATOM   4394 S  SG  . CYS D 1 146 ? 18.980  -76.041 24.102 1.00 84.55  ? 146 CYS D SG  1 
ATOM   4395 N  N   . GLY D 1 147 ? 20.319  -73.074 22.182 1.00 77.32  ? 147 GLY D N   1 
ATOM   4396 C  CA  . GLY D 1 147 ? 19.351  -72.103 21.735 1.00 77.93  ? 147 GLY D CA  1 
ATOM   4397 C  C   . GLY D 1 147 ? 19.159  -72.189 20.259 1.00 76.22  ? 147 GLY D C   1 
ATOM   4398 O  O   . GLY D 1 147 ? 20.038  -72.669 19.555 1.00 74.52  ? 147 GLY D O   1 
ATOM   4399 N  N   . VAL D 1 148 ? 18.010  -71.720 19.794 1.00 76.71  ? 148 VAL D N   1 
ATOM   4400 C  CA  . VAL D 1 148 ? 17.744  -71.684 18.362 1.00 75.76  ? 148 VAL D CA  1 
ATOM   4401 C  C   . VAL D 1 148 ? 18.554  -70.604 17.656 1.00 74.78  ? 148 VAL D C   1 
ATOM   4402 O  O   . VAL D 1 148 ? 18.785  -69.537 18.199 1.00 75.31  ? 148 VAL D O   1 
ATOM   4403 C  CB  . VAL D 1 148 ? 16.280  -71.456 18.077 1.00 77.70  ? 148 VAL D CB  1 
ATOM   4404 C  CG1 . VAL D 1 148 ? 16.067  -71.348 16.601 1.00 77.31  ? 148 VAL D CG1 1 
ATOM   4405 C  CG2 . VAL D 1 148 ? 15.498  -72.594 18.625 1.00 78.64  ? 148 VAL D CG2 1 
ATOM   4406 N  N   . ILE D 1 149 ? 18.971  -70.905 16.436 1.00 73.66  ? 149 ILE D N   1 
ATOM   4407 C  CA  . ILE D 1 149 ? 19.808  -70.019 15.658 1.00 73.63  ? 149 ILE D CA  1 
ATOM   4408 C  C   . ILE D 1 149 ? 18.941  -69.132 14.829 1.00 75.52  ? 149 ILE D C   1 
ATOM   4409 O  O   . ILE D 1 149 ? 18.170  -69.629 14.011 1.00 76.17  ? 149 ILE D O   1 
ATOM   4410 C  CB  . ILE D 1 149 ? 20.632  -70.808 14.646 1.00 72.82  ? 149 ILE D CB  1 
ATOM   4411 C  CG1 . ILE D 1 149 ? 21.826  -71.459 15.321 1.00 71.15  ? 149 ILE D CG1 1 
ATOM   4412 C  CG2 . ILE D 1 149 ? 21.117  -69.907 13.530 1.00 74.24  ? 149 ILE D CG2 1 
ATOM   4413 C  CD1 . ILE D 1 149 ? 22.269  -72.689 14.600 1.00 71.09  ? 149 ILE D CD1 1 
ATOM   4414 N  N   . GLY D 1 150 ? 19.117  -67.826 14.971 1.00 76.82  ? 150 GLY D N   1 
ATOM   4415 C  CA  . GLY D 1 150 ? 18.199  -66.878 14.345 1.00 79.77  ? 150 GLY D CA  1 
ATOM   4416 C  C   . GLY D 1 150 ? 18.863  -65.786 13.560 1.00 81.61  ? 150 GLY D C   1 
ATOM   4417 O  O   . GLY D 1 150 ? 20.069  -65.547 13.722 1.00 80.95  ? 150 GLY D O   1 
ATOM   4418 N  N   . ILE D 1 151 ? 18.072  -65.101 12.730 1.00 84.82  ? 151 ILE D N   1 
ATOM   4419 C  CA  . ILE D 1 151 ? 18.628  -64.129 11.762 1.00 87.63  ? 151 ILE D CA  1 
ATOM   4420 C  C   . ILE D 1 151 ? 19.012  -62.863 12.493 1.00 90.01  ? 151 ILE D C   1 
ATOM   4421 O  O   . ILE D 1 151 ? 18.202  -62.297 13.223 1.00 91.53  ? 151 ILE D O   1 
ATOM   4422 C  CB  . ILE D 1 151 ? 17.662  -63.781 10.620 1.00 90.39  ? 151 ILE D CB  1 
ATOM   4423 C  CG1 . ILE D 1 151 ? 17.201  -65.056 9.913  1.00 89.44  ? 151 ILE D CG1 1 
ATOM   4424 C  CG2 . ILE D 1 151 ? 18.343  -62.861 9.636  1.00 92.36  ? 151 ILE D CG2 1 
ATOM   4425 C  CD1 . ILE D 1 151 ? 16.148  -64.839 8.907  1.00 92.95  ? 151 ILE D CD1 1 
ATOM   4426 N  N   . ALA D 1 152 ? 20.261  -62.447 12.311 1.00 91.49  ? 152 ALA D N   1 
ATOM   4427 C  CA  . ALA D 1 152 ? 20.825  -61.350 13.078 1.00 94.04  ? 152 ALA D CA  1 
ATOM   4428 C  C   . ALA D 1 152 ? 20.828  -60.128 12.217 1.00 99.19  ? 152 ALA D C   1 
ATOM   4429 O  O   . ALA D 1 152 ? 20.716  -60.228 10.971 1.00 100.20 ? 152 ALA D O   1 
ATOM   4430 C  CB  . ALA D 1 152 ? 22.236  -61.673 13.496 1.00 92.35  ? 152 ALA D CB  1 
ATOM   4431 N  N   . GLN D 1 153 ? 20.968  -58.970 12.865 1.00 103.14 ? 153 GLN D N   1 
ATOM   4432 C  CA  . GLN D 1 153 ? 21.110  -57.745 12.080 1.00 108.90 ? 153 GLN D CA  1 
ATOM   4433 C  C   . GLN D 1 153 ? 22.495  -57.632 11.380 1.00 110.30 ? 153 GLN D C   1 
ATOM   4434 O  O   . GLN D 1 153 ? 23.545  -57.876 12.017 1.00 109.16 ? 153 GLN D O   1 
ATOM   4435 C  CB  . GLN D 1 153 ? 20.847  -56.490 12.907 1.00 112.29 ? 153 GLN D CB  1 
ATOM   4436 C  CG  . GLN D 1 153 ? 20.831  -55.247 11.995 1.00 117.87 ? 153 GLN D CG  1 
ATOM   4437 C  CD  . GLN D 1 153 ? 20.172  -54.039 12.640 1.00 122.43 ? 153 GLN D CD  1 
ATOM   4438 O  OE1 . GLN D 1 153 ? 20.451  -53.690 13.796 1.00 123.46 ? 153 GLN D OE1 1 
ATOM   4439 N  NE2 . GLN D 1 153 ? 19.301  -53.381 11.882 1.00 126.13 ? 153 GLN D NE2 1 
ATOM   4440 O  OXT . GLN D 1 153 ? 22.578  -57.278 10.172 1.00 113.54 ? 153 GLN D OXT 1 
ATOM   4441 N  N   . ALA E 1 1   ? -44.366 -63.429 4.842  1.00 106.30 ? 1   ALA E N   1 
ATOM   4442 C  CA  . ALA E 1 1   ? -43.878 -62.850 6.144  1.00 101.85 ? 1   ALA E CA  1 
ATOM   4443 C  C   . ALA E 1 1   ? -43.128 -61.450 5.996  1.00 101.68 ? 1   ALA E C   1 
ATOM   4444 O  O   . ALA E 1 1   ? -41.912 -61.405 5.655  1.00 101.09 ? 1   ALA E O   1 
ATOM   4445 C  CB  . ALA E 1 1   ? -43.009 -63.900 6.865  1.00 97.94  ? 1   ALA E CB  1 
ATOM   4446 N  N   . THR E 1 2   ? -43.872 -60.336 6.213  1.00 102.39 ? 2   THR E N   1 
ATOM   4447 C  CA  . THR E 1 2   ? -43.310 -58.949 6.311  1.00 101.74 ? 2   THR E CA  1 
ATOM   4448 C  C   . THR E 1 2   ? -42.669 -58.771 7.673  1.00 96.44  ? 2   THR E C   1 
ATOM   4449 O  O   . THR E 1 2   ? -41.586 -58.221 7.760  1.00 95.10  ? 2   THR E O   1 
ATOM   4450 C  CB  . THR E 1 2   ? -44.392 -57.752 6.139  1.00 105.91 ? 2   THR E CB  1 
ATOM   4451 O  OG1 . THR E 1 2   ? -44.830 -57.635 4.780  1.00 111.82 ? 2   THR E OG1 1 
ATOM   4452 C  CG2 . THR E 1 2   ? -43.832 -56.347 6.569  1.00 105.11 ? 2   THR E CG2 1 
ATOM   4453 N  N   . LYS E 1 3   ? -43.353 -59.221 8.730  1.00 93.90  ? 3   LYS E N   1 
ATOM   4454 C  CA  . LYS E 1 3   ? -42.906 -58.995 10.114 1.00 89.92  ? 3   LYS E CA  1 
ATOM   4455 C  C   . LYS E 1 3   ? -42.697 -60.279 10.882 1.00 86.05  ? 3   LYS E C   1 
ATOM   4456 O  O   . LYS E 1 3   ? -43.253 -61.314 10.521 1.00 86.82  ? 3   LYS E O   1 
ATOM   4457 C  CB  . LYS E 1 3   ? -43.923 -58.155 10.879 1.00 91.60  ? 3   LYS E CB  1 
ATOM   4458 C  CG  . LYS E 1 3   ? -43.983 -56.716 10.426 1.00 95.86  ? 3   LYS E CG  1 
ATOM   4459 C  CD  . LYS E 1 3   ? -44.890 -55.885 11.341 1.00 99.47  ? 3   LYS E CD  1 
ATOM   4460 C  CE  . LYS E 1 3   ? -45.501 -54.701 10.583 1.00 105.32 ? 3   LYS E CE  1 
ATOM   4461 N  NZ  . LYS E 1 3   ? -46.757 -54.246 11.247 1.00 109.05 ? 3   LYS E NZ  1 
ATOM   4462 N  N   . ALA E 1 4   ? -41.883 -60.186 11.935 1.00 82.02  ? 4   ALA E N   1 
ATOM   4463 C  CA  . ALA E 1 4   ? -41.680 -61.268 12.891 1.00 78.89  ? 4   ALA E CA  1 
ATOM   4464 C  C   . ALA E 1 4   ? -41.361 -60.708 14.260 1.00 76.64  ? 4   ALA E C   1 
ATOM   4465 O  O   . ALA E 1 4   ? -41.218 -59.502 14.427 1.00 76.85  ? 4   ALA E O   1 
ATOM   4466 C  CB  . ALA E 1 4   ? -40.578 -62.212 12.431 1.00 77.32  ? 4   ALA E CB  1 
ATOM   4467 N  N   . VAL E 1 5   ? -41.285 -61.613 15.235 1.00 74.83  ? 5   VAL E N   1 
ATOM   4468 C  CA  . VAL E 1 5   ? -41.012 -61.276 16.628 1.00 73.44  ? 5   VAL E CA  1 
ATOM   4469 C  C   . VAL E 1 5   ? -40.400 -62.462 17.349 1.00 72.15  ? 5   VAL E C   1 
ATOM   4470 O  O   . VAL E 1 5   ? -40.507 -63.601 16.897 1.00 72.04  ? 5   VAL E O   1 
ATOM   4471 C  CB  . VAL E 1 5   ? -42.285 -60.891 17.351 1.00 75.18  ? 5   VAL E CB  1 
ATOM   4472 C  CG1 . VAL E 1 5   ? -43.123 -62.101 17.575 1.00 75.61  ? 5   VAL E CG1 1 
ATOM   4473 C  CG2 . VAL E 1 5   ? -41.961 -60.237 18.655 1.00 74.00  ? 5   VAL E CG2 1 
ATOM   4474 N  N   . CYS E 1 6   ? -39.753 -62.189 18.471 1.00 71.70  ? 6   CYS E N   1 
ATOM   4475 C  CA  . CYS E 1 6   ? -39.126 -63.242 19.258 1.00 71.42  ? 6   CYS E CA  1 
ATOM   4476 C  C   . CYS E 1 6   ? -38.981 -62.840 20.706 1.00 72.01  ? 6   CYS E C   1 
ATOM   4477 O  O   . CYS E 1 6   ? -38.405 -61.812 20.983 1.00 71.74  ? 6   CYS E O   1 
ATOM   4478 C  CB  . CYS E 1 6   ? -37.736 -63.527 18.721 1.00 70.00  ? 6   CYS E CB  1 
ATOM   4479 S  SG  . CYS E 1 6   ? -36.752 -64.569 19.806 1.00 69.94  ? 6   CYS E SG  1 
ATOM   4480 N  N   . VAL E 1 7   ? -39.488 -63.651 21.627 1.00 73.50  ? 7   VAL E N   1 
ATOM   4481 C  CA  . VAL E 1 7   ? -39.292 -63.389 23.049 1.00 74.99  ? 7   VAL E CA  1 
ATOM   4482 C  C   . VAL E 1 7   ? -38.099 -64.149 23.614 1.00 75.15  ? 7   VAL E C   1 
ATOM   4483 O  O   . VAL E 1 7   ? -38.049 -65.390 23.611 1.00 75.59  ? 7   VAL E O   1 
ATOM   4484 C  CB  . VAL E 1 7   ? -40.483 -63.790 23.863 1.00 77.40  ? 7   VAL E CB  1 
ATOM   4485 C  CG1 . VAL E 1 7   ? -40.292 -63.346 25.270 1.00 79.22  ? 7   VAL E CG1 1 
ATOM   4486 C  CG2 . VAL E 1 7   ? -41.694 -63.183 23.310 1.00 78.67  ? 7   VAL E CG2 1 
ATOM   4487 N  N   . LEU E 1 8   ? -37.146 -63.386 24.123 1.00 75.41  ? 8   LEU E N   1 
ATOM   4488 C  CA  . LEU E 1 8   ? -35.938 -63.946 24.672 1.00 75.95  ? 8   LEU E CA  1 
ATOM   4489 C  C   . LEU E 1 8   ? -36.097 -64.212 26.139 1.00 79.72  ? 8   LEU E C   1 
ATOM   4490 O  O   . LEU E 1 8   ? -36.478 -63.332 26.887 1.00 81.02  ? 8   LEU E O   1 
ATOM   4491 C  CB  . LEU E 1 8   ? -34.804 -62.966 24.477 1.00 74.54  ? 8   LEU E CB  1 
ATOM   4492 C  CG  . LEU E 1 8   ? -34.390 -62.779 23.021 1.00 71.43  ? 8   LEU E CG  1 
ATOM   4493 C  CD1 . LEU E 1 8   ? -33.445 -61.648 22.876 1.00 68.80  ? 8   LEU E CD1 1 
ATOM   4494 C  CD2 . LEU E 1 8   ? -33.742 -64.028 22.510 1.00 72.05  ? 8   LEU E CD2 1 
ATOM   4495 N  N   . LYS E 1 9   ? -35.804 -65.439 26.533 1.00 82.43  ? 9   LYS E N   1 
ATOM   4496 C  CA  . LYS E 1 9   ? -35.892 -65.876 27.913 1.00 87.52  ? 9   LYS E CA  1 
ATOM   4497 C  C   . LYS E 1 9   ? -34.748 -66.829 28.174 1.00 88.77  ? 9   LYS E C   1 
ATOM   4498 O  O   . LYS E 1 9   ? -34.145 -67.360 27.244 1.00 87.00  ? 9   LYS E O   1 
ATOM   4499 C  CB  . LYS E 1 9   ? -37.170 -66.675 28.170 1.00 90.28  ? 9   LYS E CB  1 
ATOM   4500 C  CG  . LYS E 1 9   ? -38.491 -65.910 28.071 1.00 94.02  ? 9   LYS E CG  1 
ATOM   4501 C  CD  . LYS E 1 9   ? -38.953 -65.265 29.413 1.00 101.50 ? 9   LYS E CD  1 
ATOM   4502 C  CE  . LYS E 1 9   ? -40.485 -65.012 29.427 1.00 104.70 ? 9   LYS E CE  1 
ATOM   4503 N  NZ  . LYS E 1 9   ? -40.910 -64.147 30.577 1.00 109.77 ? 9   LYS E NZ  1 
ATOM   4504 N  N   . GLY E 1 10  ? -34.474 -67.080 29.445 1.00 92.88  ? 10  GLY E N   1 
ATOM   4505 C  CA  . GLY E 1 10  ? -33.414 -67.996 29.812 1.00 94.91  ? 10  GLY E CA  1 
ATOM   4506 C  C   . GLY E 1 10  ? -33.460 -68.281 31.283 1.00 100.32 ? 10  GLY E C   1 
ATOM   4507 O  O   . GLY E 1 10  ? -34.337 -67.777 31.986 1.00 102.40 ? 10  GLY E O   1 
ATOM   4508 N  N   . ASP E 1 11  ? -32.506 -69.081 31.750 1.00 103.45 ? 11  ASP E N   1 
ATOM   4509 C  CA  . ASP E 1 11  ? -32.335 -69.349 33.187 1.00 109.51 ? 11  ASP E CA  1 
ATOM   4510 C  C   . ASP E 1 11  ? -31.949 -68.111 33.984 1.00 110.69 ? 11  ASP E C   1 
ATOM   4511 O  O   . ASP E 1 11  ? -32.308 -67.977 35.160 1.00 115.14 ? 11  ASP E O   1 
ATOM   4512 C  CB  . ASP E 1 11  ? -31.250 -70.395 33.392 1.00 112.52 ? 11  ASP E CB  1 
ATOM   4513 C  CG  . ASP E 1 11  ? -31.707 -71.791 32.996 1.00 115.74 ? 11  ASP E CG  1 
ATOM   4514 O  OD1 . ASP E 1 11  ? -32.936 -72.055 33.052 1.00 119.13 ? 11  ASP E OD1 1 
ATOM   4515 O  OD2 . ASP E 1 11  ? -30.847 -72.628 32.636 1.00 119.32 ? 11  ASP E OD2 1 
ATOM   4516 N  N   . GLY E 1 12  ? -31.211 -67.208 33.336 1.00 107.05 ? 12  GLY E N   1 
ATOM   4517 C  CA  . GLY E 1 12  ? -30.785 -65.956 33.948 1.00 107.43 ? 12  GLY E CA  1 
ATOM   4518 C  C   . GLY E 1 12  ? -31.942 -65.015 34.245 1.00 107.23 ? 12  GLY E C   1 
ATOM   4519 O  O   . GLY E 1 12  ? -33.119 -65.378 34.124 1.00 107.21 ? 12  GLY E O   1 
ATOM   4520 N  N   . PRO E 1 13  ? -31.614 -63.786 34.659 1.00 107.32 ? 13  PRO E N   1 
ATOM   4521 C  CA  . PRO E 1 13  ? -32.587 -62.699 34.770 1.00 106.93 ? 13  PRO E CA  1 
ATOM   4522 C  C   . PRO E 1 13  ? -32.742 -61.970 33.415 1.00 100.98 ? 13  PRO E C   1 
ATOM   4523 O  O   . PRO E 1 13  ? -33.513 -61.004 33.304 1.00 100.37 ? 13  PRO E O   1 
ATOM   4524 C  CB  . PRO E 1 13  ? -31.927 -61.780 35.781 1.00 110.64 ? 13  PRO E CB  1 
ATOM   4525 C  CG  . PRO E 1 13  ? -30.447 -61.895 35.428 1.00 109.07 ? 13  PRO E CG  1 
ATOM   4526 C  CD  . PRO E 1 13  ? -30.239 -63.308 34.911 1.00 107.99 ? 13  PRO E CD  1 
ATOM   4527 N  N   . VAL E 1 14  ? -31.996 -62.446 32.404 1.00 96.84  ? 14  VAL E N   1 
ATOM   4528 C  CA  . VAL E 1 14  ? -31.932 -61.826 31.088 1.00 91.52  ? 14  VAL E CA  1 
ATOM   4529 C  C   . VAL E 1 14  ? -33.226 -62.114 30.397 1.00 89.68  ? 14  VAL E C   1 
ATOM   4530 O  O   . VAL E 1 14  ? -33.750 -63.232 30.494 1.00 90.64  ? 14  VAL E O   1 
ATOM   4531 C  CB  . VAL E 1 14  ? -30.838 -62.426 30.212 1.00 88.72  ? 14  VAL E CB  1 
ATOM   4532 C  CG1 . VAL E 1 14  ? -30.577 -61.490 29.086 1.00 84.14  ? 14  VAL E CG1 1 
ATOM   4533 C  CG2 . VAL E 1 14  ? -29.553 -62.715 31.020 1.00 92.12  ? 14  VAL E CG2 1 
ATOM   4534 N  N   . GLN E 1 15  ? -33.744 -61.106 29.715 1.00 87.42  ? 15  GLN E N   1 
ATOM   4535 C  CA  . GLN E 1 15  ? -34.958 -61.276 28.957 1.00 86.05  ? 15  GLN E CA  1 
ATOM   4536 C  C   . GLN E 1 15  ? -35.291 -60.043 28.165 1.00 83.72  ? 15  GLN E C   1 
ATOM   4537 O  O   . GLN E 1 15  ? -34.914 -58.942 28.557 1.00 84.76  ? 15  GLN E O   1 
ATOM   4538 C  CB  . GLN E 1 15  ? -36.128 -61.600 29.888 1.00 90.08  ? 15  GLN E CB  1 
ATOM   4539 C  CG  . GLN E 1 15  ? -36.635 -60.428 30.709 1.00 94.36  ? 15  GLN E CG  1 
ATOM   4540 C  CD  . GLN E 1 15  ? -37.725 -60.818 31.718 1.00 100.78 ? 15  GLN E CD  1 
ATOM   4541 O  OE1 . GLN E 1 15  ? -38.142 -59.964 32.508 1.00 105.75 ? 15  GLN E OE1 1 
ATOM   4542 N  NE2 . GLN E 1 15  ? -38.197 -62.090 31.692 1.00 101.02 ? 15  GLN E NE2 1 
ATOM   4543 N  N   . GLY E 1 16  ? -36.025 -60.236 27.071 1.00 80.97  ? 16  GLY E N   1 
ATOM   4544 C  CA  . GLY E 1 16  ? -36.461 -59.128 26.242 1.00 79.51  ? 16  GLY E CA  1 
ATOM   4545 C  C   . GLY E 1 16  ? -37.357 -59.577 25.121 1.00 77.55  ? 16  GLY E C   1 
ATOM   4546 O  O   . GLY E 1 16  ? -37.663 -60.757 25.006 1.00 77.30  ? 16  GLY E O   1 
ATOM   4547 N  N   . ILE E 1 17  ? -37.748 -58.613 24.292 1.00 76.54  ? 17  ILE E N   1 
ATOM   4548 C  CA  . ILE E 1 17  ? -38.571 -58.826 23.107 1.00 75.40  ? 17  ILE E CA  1 
ATOM   4549 C  C   . ILE E 1 17  ? -37.884 -58.170 21.920 1.00 73.38  ? 17  ILE E C   1 
ATOM   4550 O  O   . ILE E 1 17  ? -37.449 -57.047 22.032 1.00 73.71  ? 17  ILE E O   1 
ATOM   4551 C  CB  . ILE E 1 17  ? -39.901 -58.097 23.245 1.00 78.11  ? 17  ILE E CB  1 
ATOM   4552 C  CG1 . ILE E 1 17  ? -40.494 -58.254 24.647 1.00 81.24  ? 17  ILE E CG1 1 
ATOM   4553 C  CG2 . ILE E 1 17  ? -40.867 -58.562 22.187 1.00 78.06  ? 17  ILE E CG2 1 
ATOM   4554 C  CD1 . ILE E 1 17  ? -41.820 -58.934 24.671 1.00 83.66  ? 17  ILE E CD1 1 
ATOM   4555 N  N   . ILE E 1 18  ? -37.799 -58.846 20.786 1.00 71.93  ? 18  ILE E N   1 
ATOM   4556 C  CA  . ILE E 1 18  ? -37.138 -58.279 19.630 1.00 71.36  ? 18  ILE E CA  1 
ATOM   4557 C  C   . ILE E 1 18  ? -38.014 -58.425 18.445 1.00 72.39  ? 18  ILE E C   1 
ATOM   4558 O  O   . ILE E 1 18  ? -38.521 -59.508 18.220 1.00 72.41  ? 18  ILE E O   1 
ATOM   4559 C  CB  . ILE E 1 18  ? -35.869 -59.023 19.295 1.00 69.48  ? 18  ILE E CB  1 
ATOM   4560 C  CG1 . ILE E 1 18  ? -34.846 -58.861 20.398 1.00 69.76  ? 18  ILE E CG1 1 
ATOM   4561 C  CG2 . ILE E 1 18  ? -35.299 -58.508 18.037 1.00 68.82  ? 18  ILE E CG2 1 
ATOM   4562 C  CD1 . ILE E 1 18  ? -34.515 -57.464 20.722 1.00 72.12  ? 18  ILE E CD1 1 
ATOM   4563 N  N   . ASN E 1 19  ? -38.160 -57.349 17.673 1.00 74.11  ? 19  ASN E N   1 
ATOM   4564 C  CA  . ASN E 1 19  ? -38.994 -57.357 16.475 1.00 76.19  ? 19  ASN E CA  1 
ATOM   4565 C  C   . ASN E 1 19  ? -38.218 -57.358 15.187 1.00 76.29  ? 19  ASN E C   1 
ATOM   4566 O  O   . ASN E 1 19  ? -37.083 -56.971 15.158 1.00 75.41  ? 19  ASN E O   1 
ATOM   4567 C  CB  . ASN E 1 19  ? -39.907 -56.151 16.484 1.00 78.96  ? 19  ASN E CB  1 
ATOM   4568 C  CG  . ASN E 1 19  ? -40.809 -56.147 17.670 1.00 80.67  ? 19  ASN E CG  1 
ATOM   4569 O  OD1 . ASN E 1 19  ? -40.509 -55.527 18.688 1.00 81.68  ? 19  ASN E OD1 1 
ATOM   4570 N  ND2 . ASN E 1 19  ? -41.905 -56.891 17.574 1.00 82.06  ? 19  ASN E ND2 1 
ATOM   4571 N  N   . PHE E 1 20  ? -38.861 -57.793 14.117 1.00 78.53  ? 20  PHE E N   1 
ATOM   4572 C  CA  . PHE E 1 20  ? -38.253 -57.807 12.805 1.00 80.17  ? 20  PHE E CA  1 
ATOM   4573 C  C   . PHE E 1 20  ? -39.221 -57.221 11.792 1.00 84.32  ? 20  PHE E C   1 
ATOM   4574 O  O   . PHE E 1 20  ? -40.423 -57.378 11.926 1.00 86.06  ? 20  PHE E O   1 
ATOM   4575 C  CB  . PHE E 1 20  ? -37.930 -59.233 12.393 1.00 79.21  ? 20  PHE E CB  1 
ATOM   4576 C  CG  . PHE E 1 20  ? -36.964 -59.939 13.308 1.00 76.95  ? 20  PHE E CG  1 
ATOM   4577 C  CD1 . PHE E 1 20  ? -37.330 -60.307 14.583 1.00 77.03  ? 20  PHE E CD1 1 
ATOM   4578 C  CD2 . PHE E 1 20  ? -35.705 -60.287 12.868 1.00 75.78  ? 20  PHE E CD2 1 
ATOM   4579 C  CE1 . PHE E 1 20  ? -36.442 -60.984 15.411 1.00 75.22  ? 20  PHE E CE1 1 
ATOM   4580 C  CE2 . PHE E 1 20  ? -34.824 -60.955 13.686 1.00 73.16  ? 20  PHE E CE2 1 
ATOM   4581 C  CZ  . PHE E 1 20  ? -35.191 -61.303 14.955 1.00 73.04  ? 20  PHE E CZ  1 
ATOM   4582 N  N   . GLU E 1 21  ? -38.698 -56.557 10.774 1.00 87.09  ? 21  GLU E N   1 
ATOM   4583 C  CA  . GLU E 1 21  ? -39.536 -56.038 9.709  1.00 91.97  ? 21  GLU E CA  1 
ATOM   4584 C  C   . GLU E 1 21  ? -38.791 -56.012 8.383  1.00 94.11  ? 21  GLU E C   1 
ATOM   4585 O  O   . GLU E 1 21  ? -37.727 -55.438 8.292  1.00 94.13  ? 21  GLU E O   1 
ATOM   4586 C  CB  . GLU E 1 21  ? -40.030 -54.647 10.061 1.00 94.44  ? 21  GLU E CB  1 
ATOM   4587 C  CG  . GLU E 1 21  ? -41.162 -54.157 9.148  1.00 101.56 ? 21  GLU E CG  1 
ATOM   4588 C  CD  . GLU E 1 21  ? -41.694 -52.748 9.541  1.00 107.44 ? 21  GLU E CD  1 
ATOM   4589 O  OE1 . GLU E 1 21  ? -40.875 -51.879 9.922  1.00 108.76 ? 21  GLU E OE1 1 
ATOM   4590 O  OE2 . GLU E 1 21  ? -42.934 -52.510 9.459  1.00 112.09 ? 21  GLU E OE2 1 
ATOM   4591 N  N   . GLN E 1 22  ? -39.343 -56.675 7.372  1.00 96.94  ? 22  GLN E N   1 
ATOM   4592 C  CA  . GLN E 1 22  ? -38.732 -56.748 6.045  1.00 100.24 ? 22  GLN E CA  1 
ATOM   4593 C  C   . GLN E 1 22  ? -39.795 -56.227 5.086  1.00 106.32 ? 22  GLN E C   1 
ATOM   4594 O  O   . GLN E 1 22  ? -40.642 -56.989 4.587  1.00 108.27 ? 22  GLN E O   1 
ATOM   4595 C  CB  . GLN E 1 22  ? -38.286 -58.187 5.684  1.00 98.87  ? 22  GLN E CB  1 
ATOM   4596 C  CG  . GLN E 1 22  ? -37.604 -58.312 4.336  1.00 101.95 ? 22  GLN E CG  1 
ATOM   4597 C  CD  . GLN E 1 22  ? -36.978 -59.685 4.090  1.00 100.79 ? 22  GLN E CD  1 
ATOM   4598 O  OE1 . GLN E 1 22  ? -37.563 -60.722 4.412  1.00 98.65  ? 22  GLN E OE1 1 
ATOM   4599 N  NE2 . GLN E 1 22  ? -35.780 -59.692 3.494  1.00 102.20 ? 22  GLN E NE2 1 
ATOM   4600 N  N   . LYS E 1 23  ? -39.766 -54.914 4.856  1.00 110.17 ? 23  LYS E N   1 
ATOM   4601 C  CA  . LYS E 1 23  ? -40.749 -54.264 3.983  1.00 116.56 ? 23  LYS E CA  1 
ATOM   4602 C  C   . LYS E 1 23  ? -40.662 -54.760 2.553  1.00 120.95 ? 23  LYS E C   1 
ATOM   4603 O  O   . LYS E 1 23  ? -41.679 -54.898 1.889  1.00 125.08 ? 23  LYS E O   1 
ATOM   4604 C  CB  . LYS E 1 23  ? -40.621 -52.737 4.023  1.00 119.43 ? 23  LYS E CB  1 
ATOM   4605 C  CG  . LYS E 1 23  ? -41.509 -52.074 5.136  1.00 120.48 ? 23  LYS E CG  1 
ATOM   4606 C  CD  . LYS E 1 23  ? -41.001 -50.683 5.559  1.00 123.36 ? 23  LYS E CD  1 
ATOM   4607 C  CE  . LYS E 1 23  ? -39.712 -50.793 6.402  1.00 119.92 ? 23  LYS E CE  1 
ATOM   4608 N  NZ  . LYS E 1 23  ? -39.100 -49.467 6.655  1.00 122.39 ? 23  LYS E NZ  1 
ATOM   4609 N  N   . GLU E 1 24  ? -39.465 -55.051 2.077  1.00 121.00 ? 24  GLU E N   1 
ATOM   4610 C  CA  . GLU E 1 24  ? -39.341 -55.572 0.726  1.00 126.09 ? 24  GLU E CA  1 
ATOM   4611 C  C   . GLU E 1 24  ? -38.873 -56.984 0.713  1.00 123.83 ? 24  GLU E C   1 
ATOM   4612 O  O   . GLU E 1 24  ? -37.880 -57.307 1.359  1.00 119.92 ? 24  GLU E O   1 
ATOM   4613 C  CB  . GLU E 1 24  ? -38.314 -54.765 -0.035 1.00 129.90 ? 24  GLU E CB  1 
ATOM   4614 C  CG  . GLU E 1 24  ? -38.853 -53.431 -0.538 1.00 136.05 ? 24  GLU E CG  1 
ATOM   4615 C  CD  . GLU E 1 24  ? -37.856 -52.719 -1.440 1.00 141.56 ? 24  GLU E CD  1 
ATOM   4616 O  OE1 . GLU E 1 24  ? -36.626 -52.950 -1.257 1.00 139.53 ? 24  GLU E OE1 1 
ATOM   4617 O  OE2 . GLU E 1 24  ? -38.309 -51.951 -2.330 1.00 148.25 ? 24  GLU E OE2 1 
ATOM   4618 N  N   . SER E 1 25  ? -39.545 -57.817 -0.066 1.00 127.22 ? 25  SER E N   1 
ATOM   4619 C  CA  . SER E 1 25  ? -39.052 -59.166 -0.320 1.00 126.79 ? 25  SER E CA  1 
ATOM   4620 C  C   . SER E 1 25  ? -37.561 -59.119 -0.704 1.00 127.11 ? 25  SER E C   1 
ATOM   4621 O  O   . SER E 1 25  ? -37.131 -58.295 -1.534 1.00 131.32 ? 25  SER E O   1 
ATOM   4622 C  CB  . SER E 1 25  ? -39.860 -59.825 -1.438 1.00 132.42 ? 25  SER E CB  1 
ATOM   4623 O  OG  . SER E 1 25  ? -39.254 -61.046 -1.832 1.00 133.66 ? 25  SER E OG  1 
ATOM   4624 N  N   . ASN E 1 26  ? -36.775 -59.978 -0.061 1.00 122.91 ? 26  ASN E N   1 
ATOM   4625 C  CA  . ASN E 1 26  ? -35.325 -60.028 -0.283 1.00 123.12 ? 26  ASN E CA  1 
ATOM   4626 C  C   . ASN E 1 26  ? -34.606 -58.685 -0.109 1.00 122.15 ? 26  ASN E C   1 
ATOM   4627 O  O   . ASN E 1 26  ? -33.461 -58.537 -0.545 1.00 124.02 ? 26  ASN E O   1 
ATOM   4628 C  CB  . ASN E 1 26  ? -35.002 -60.595 -1.670 1.00 129.53 ? 26  ASN E CB  1 
ATOM   4629 C  CG  . ASN E 1 26  ? -35.324 -62.096 -1.799 1.00 130.94 ? 26  ASN E CG  1 
ATOM   4630 O  OD1 . ASN E 1 26  ? -35.351 -62.885 -0.817 1.00 127.39 ? 26  ASN E OD1 1 
ATOM   4631 N  ND2 . ASN E 1 26  ? -35.554 -62.499 -3.038 1.00 137.18 ? 26  ASN E ND2 1 
ATOM   4632 N  N   . GLY E 1 27  ? -35.268 -57.722 0.536  1.00 119.28 ? 27  GLY E N   1 
ATOM   4633 C  CA  . GLY E 1 27  ? -34.622 -56.478 0.943  1.00 117.47 ? 27  GLY E CA  1 
ATOM   4634 C  C   . GLY E 1 27  ? -33.863 -56.624 2.268  1.00 110.46 ? 27  GLY E C   1 
ATOM   4635 O  O   . GLY E 1 27  ? -33.496 -57.741 2.685  1.00 107.24 ? 27  GLY E O   1 
ATOM   4636 N  N   . PRO E 1 28  ? -33.626 -55.488 2.944  1.00 107.81 ? 28  PRO E N   1 
ATOM   4637 C  CA  . PRO E 1 28  ? -33.007 -55.521 4.246  1.00 101.96 ? 28  PRO E CA  1 
ATOM   4638 C  C   . PRO E 1 28  ? -34.099 -55.706 5.316  1.00 97.85  ? 28  PRO E C   1 
ATOM   4639 O  O   . PRO E 1 28  ? -35.316 -55.588 5.003  1.00 99.50  ? 28  PRO E O   1 
ATOM   4640 C  CB  . PRO E 1 28  ? -32.403 -54.128 4.363  1.00 102.90 ? 28  PRO E CB  1 
ATOM   4641 C  CG  . PRO E 1 28  ? -33.452 -53.258 3.727  1.00 107.27 ? 28  PRO E CG  1 
ATOM   4642 C  CD  . PRO E 1 28  ? -34.144 -54.136 2.655  1.00 110.93 ? 28  PRO E CD  1 
ATOM   4643 N  N   . VAL E 1 29  ? -33.648 -55.950 6.556  1.00 92.49  ? 29  VAL E N   1 
ATOM   4644 C  CA  . VAL E 1 29  ? -34.501 -56.350 7.668  1.00 88.72  ? 29  VAL E CA  1 
ATOM   4645 C  C   . VAL E 1 29  ? -34.202 -55.486 8.878  1.00 86.40  ? 29  VAL E C   1 
ATOM   4646 O  O   . VAL E 1 29  ? -33.144 -55.600 9.445  1.00 84.75  ? 29  VAL E O   1 
ATOM   4647 C  CB  . VAL E 1 29  ? -34.188 -57.791 8.083  1.00 85.95  ? 29  VAL E CB  1 
ATOM   4648 C  CG1 . VAL E 1 29  ? -34.980 -58.140 9.288  1.00 82.56  ? 29  VAL E CG1 1 
ATOM   4649 C  CG2 . VAL E 1 29  ? -34.443 -58.779 6.953  1.00 88.40  ? 29  VAL E CG2 1 
ATOM   4650 N  N   . LYS E 1 30  ? -35.104 -54.618 9.289  1.00 87.22  ? 30  LYS E N   1 
ATOM   4651 C  CA  . LYS E 1 30  ? -34.868 -53.851 10.517 1.00 85.81  ? 30  LYS E CA  1 
ATOM   4652 C  C   . LYS E 1 30  ? -35.153 -54.715 11.706 1.00 82.14  ? 30  LYS E C   1 
ATOM   4653 O  O   . LYS E 1 30  ? -36.224 -55.285 11.798 1.00 82.44  ? 30  LYS E O   1 
ATOM   4654 C  CB  . LYS E 1 30  ? -35.751 -52.600 10.622 1.00 88.99  ? 30  LYS E CB  1 
ATOM   4655 C  CG  . LYS E 1 30  ? -35.120 -51.334 10.020 1.00 94.24  ? 30  LYS E CG  1 
ATOM   4656 C  CD  . LYS E 1 30  ? -36.157 -50.302 9.499  1.00 101.14 ? 30  LYS E CD  1 
ATOM   4657 C  CE  . LYS E 1 30  ? -36.030 -50.106 7.963  1.00 106.03 ? 30  LYS E CE  1 
ATOM   4658 N  NZ  . LYS E 1 30  ? -36.024 -48.660 7.605  1.00 110.66 ? 30  LYS E NZ  1 
ATOM   4659 N  N   . VAL E 1 31  ? -34.210 -54.767 12.633 1.00 79.51  ? 31  VAL E N   1 
ATOM   4660 C  CA  . VAL E 1 31  ? -34.330 -55.572 13.830 1.00 76.81  ? 31  VAL E CA  1 
ATOM   4661 C  C   . VAL E 1 31  ? -34.260 -54.657 15.004 1.00 77.14  ? 31  VAL E C   1 
ATOM   4662 O  O   . VAL E 1 31  ? -33.269 -53.994 15.177 1.00 77.25  ? 31  VAL E O   1 
ATOM   4663 C  CB  . VAL E 1 31  ? -33.160 -56.519 13.955 1.00 74.66  ? 31  VAL E CB  1 
ATOM   4664 C  CG1 . VAL E 1 31  ? -33.259 -57.290 15.228 1.00 71.78  ? 31  VAL E CG1 1 
ATOM   4665 C  CG2 . VAL E 1 31  ? -33.115 -57.440 12.781 1.00 74.79  ? 31  VAL E CG2 1 
ATOM   4666 N  N   . TRP E 1 32  ? -35.297 -54.594 15.814 1.00 78.23  ? 32  TRP E N   1 
ATOM   4667 C  CA  . TRP E 1 32  ? -35.216 -53.748 16.980 1.00 79.47  ? 32  TRP E CA  1 
ATOM   4668 C  C   . TRP E 1 32  ? -36.078 -54.220 18.107 1.00 78.71  ? 32  TRP E C   1 
ATOM   4669 O  O   . TRP E 1 32  ? -37.016 -54.988 17.926 1.00 78.49  ? 32  TRP E O   1 
ATOM   4670 C  CB  . TRP E 1 32  ? -35.585 -52.305 16.631 1.00 83.03  ? 32  TRP E CB  1 
ATOM   4671 C  CG  . TRP E 1 32  ? -37.022 -52.032 16.809 1.00 88.87  ? 32  TRP E CG  1 
ATOM   4672 C  CD1 . TRP E 1 32  ? -37.610 -51.375 17.849 1.00 93.81  ? 32  TRP E CD1 1 
ATOM   4673 C  CD2 . TRP E 1 32  ? -38.074 -52.443 15.935 1.00 94.08  ? 32  TRP E CD2 1 
ATOM   4674 N  NE1 . TRP E 1 32  ? -38.975 -51.337 17.671 1.00 98.14  ? 32  TRP E NE1 1 
ATOM   4675 C  CE2 . TRP E 1 32  ? -39.290 -51.990 16.505 1.00 98.21  ? 32  TRP E CE2 1 
ATOM   4676 C  CE3 . TRP E 1 32  ? -38.110 -53.147 14.716 1.00 94.62  ? 32  TRP E CE3 1 
ATOM   4677 C  CZ2 . TRP E 1 32  ? -40.545 -52.220 15.898 1.00 101.18 ? 32  TRP E CZ2 1 
ATOM   4678 C  CZ3 . TRP E 1 32  ? -39.360 -53.379 14.106 1.00 97.79  ? 32  TRP E CZ3 1 
ATOM   4679 C  CH2 . TRP E 1 32  ? -40.561 -52.912 14.702 1.00 100.83 ? 32  TRP E CH2 1 
ATOM   4680 N  N   . GLY E 1 33  ? -35.734 -53.725 19.282 1.00 78.79  ? 33  GLY E N   1 
ATOM   4681 C  CA  . GLY E 1 33  ? -36.429 -54.073 20.499 1.00 79.53  ? 33  GLY E CA  1 
ATOM   4682 C  C   . GLY E 1 33  ? -35.543 -53.785 21.679 1.00 79.40  ? 33  GLY E C   1 
ATOM   4683 O  O   . GLY E 1 33  ? -34.674 -52.934 21.592 1.00 80.06  ? 33  GLY E O   1 
ATOM   4684 N  N   . SER E 1 34  ? -35.721 -54.522 22.763 1.00 79.13  ? 34  SER E N   1 
ATOM   4685 C  CA  . SER E 1 34  ? -35.050 -54.188 23.985 1.00 80.14  ? 34  SER E CA  1 
ATOM   4686 C  C   . SER E 1 34  ? -34.820 -55.423 24.826 1.00 79.52  ? 34  SER E C   1 
ATOM   4687 O  O   . SER E 1 34  ? -35.701 -56.241 24.948 1.00 80.02  ? 34  SER E O   1 
ATOM   4688 C  CB  . SER E 1 34  ? -35.926 -53.205 24.740 1.00 83.53  ? 34  SER E CB  1 
ATOM   4689 O  OG  . SER E 1 34  ? -35.303 -52.754 25.903 1.00 86.13  ? 34  SER E OG  1 
ATOM   4690 N  N   . ILE E 1 35  ? -33.636 -55.552 25.411 1.00 79.11  ? 35  ILE E N   1 
ATOM   4691 C  CA  . ILE E 1 35  ? -33.337 -56.638 26.338 1.00 79.56  ? 35  ILE E CA  1 
ATOM   4692 C  C   . ILE E 1 35  ? -32.934 -56.045 27.669 1.00 82.80  ? 35  ILE E C   1 
ATOM   4693 O  O   . ILE E 1 35  ? -32.339 -54.970 27.694 1.00 83.80  ? 35  ILE E O   1 
ATOM   4694 C  CB  . ILE E 1 35  ? -32.173 -57.468 25.850 1.00 77.22  ? 35  ILE E CB  1 
ATOM   4695 C  CG1 . ILE E 1 35  ? -32.362 -57.809 24.385 1.00 74.82  ? 35  ILE E CG1 1 
ATOM   4696 C  CG2 . ILE E 1 35  ? -32.045 -58.723 26.668 1.00 78.15  ? 35  ILE E CG2 1 
ATOM   4697 C  CD1 . ILE E 1 35  ? -31.272 -58.683 23.828 1.00 73.40  ? 35  ILE E CD1 1 
ATOM   4698 N  N   . LYS E 1 36  ? -33.238 -56.721 28.770 1.00 85.25  ? 36  LYS E N   1 
ATOM   4699 C  CA  . LYS E 1 36  ? -32.774 -56.261 30.069 1.00 89.20  ? 36  LYS E CA  1 
ATOM   4700 C  C   . LYS E 1 36  ? -32.160 -57.374 30.874 1.00 90.22  ? 36  LYS E C   1 
ATOM   4701 O  O   . LYS E 1 36  ? -32.349 -58.536 30.564 1.00 88.90  ? 36  LYS E O   1 
ATOM   4702 C  CB  . LYS E 1 36  ? -33.900 -55.587 30.845 1.00 93.41  ? 36  LYS E CB  1 
ATOM   4703 C  CG  . LYS E 1 36  ? -35.234 -56.334 30.831 1.00 96.28  ? 36  LYS E CG  1 
ATOM   4704 C  CD  . LYS E 1 36  ? -36.319 -55.637 31.747 1.00 103.13 ? 36  LYS E CD  1 
ATOM   4705 C  CE  . LYS E 1 36  ? -37.389 -56.632 32.278 1.00 105.42 ? 36  LYS E CE  1 
ATOM   4706 N  NZ  . LYS E 1 36  ? -38.300 -55.959 33.193 1.00 110.56 ? 36  LYS E NZ  1 
ATOM   4707 N  N   . GLY E 1 37  ? -31.405 -57.000 31.903 1.00 93.35  ? 37  GLY E N   1 
ATOM   4708 C  CA  . GLY E 1 37  ? -30.711 -57.963 32.770 1.00 95.68  ? 37  GLY E CA  1 
ATOM   4709 C  C   . GLY E 1 37  ? -29.333 -58.377 32.281 1.00 93.50  ? 37  GLY E C   1 
ATOM   4710 O  O   . GLY E 1 37  ? -28.904 -59.523 32.471 1.00 94.02  ? 37  GLY E O   1 
ATOM   4711 N  N   . LEU E 1 38  ? -28.637 -57.443 31.649 1.00 91.50  ? 38  LEU E N   1 
ATOM   4712 C  CA  . LEU E 1 38  ? -27.350 -57.737 31.035 1.00 89.76  ? 38  LEU E CA  1 
ATOM   4713 C  C   . LEU E 1 38  ? -26.245 -57.064 31.801 1.00 92.41  ? 38  LEU E C   1 
ATOM   4714 O  O   . LEU E 1 38  ? -26.460 -56.026 32.408 1.00 94.62  ? 38  LEU E O   1 
ATOM   4715 C  CB  . LEU E 1 38  ? -27.343 -57.238 29.582 1.00 85.83  ? 38  LEU E CB  1 
ATOM   4716 C  CG  . LEU E 1 38  ? -28.118 -58.157 28.635 1.00 82.88  ? 38  LEU E CG  1 
ATOM   4717 C  CD1 . LEU E 1 38  ? -28.722 -57.427 27.490 1.00 79.85  ? 38  LEU E CD1 1 
ATOM   4718 C  CD2 . LEU E 1 38  ? -27.213 -59.241 28.131 1.00 82.18  ? 38  LEU E CD2 1 
ATOM   4719 N  N   . THR E 1 39  ? -25.053 -57.635 31.759 1.00 92.54  ? 39  THR E N   1 
ATOM   4720 C  CA  . THR E 1 39  ? -23.909 -56.919 32.274 1.00 94.99  ? 39  THR E CA  1 
ATOM   4721 C  C   . THR E 1 39  ? -23.667 -55.748 31.330 1.00 92.88  ? 39  THR E C   1 
ATOM   4722 O  O   . THR E 1 39  ? -23.771 -55.908 30.103 1.00 89.25  ? 39  THR E O   1 
ATOM   4723 C  CB  . THR E 1 39  ? -22.673 -57.810 32.334 1.00 96.05  ? 39  THR E CB  1 
ATOM   4724 O  OG1 . THR E 1 39  ? -22.846 -58.922 31.454 1.00 92.92  ? 39  THR E OG1 1 
ATOM   4725 C  CG2 . THR E 1 39  ? -22.472 -58.308 33.748 1.00 101.11 ? 39  THR E CG2 1 
ATOM   4726 N  N   . GLU E 1 40  ? -23.365 -54.572 31.883 1.00 95.74  ? 40  GLU E N   1 
ATOM   4727 C  CA  . GLU E 1 40  ? -22.993 -53.415 31.059 1.00 94.62  ? 40  GLU E CA  1 
ATOM   4728 C  C   . GLU E 1 40  ? -22.016 -53.852 29.964 1.00 92.04  ? 40  GLU E C   1 
ATOM   4729 O  O   . GLU E 1 40  ? -21.165 -54.706 30.189 1.00 93.19  ? 40  GLU E O   1 
ATOM   4730 C  CB  . GLU E 1 40  ? -22.354 -52.303 31.913 1.00 98.73  ? 40  GLU E CB  1 
ATOM   4731 C  CG  . GLU E 1 40  ? -21.718 -51.149 31.085 1.00 98.94  ? 40  GLU E CG  1 
ATOM   4732 C  CD  . GLU E 1 40  ? -21.666 -49.805 31.825 1.00 104.29 ? 40  GLU E CD  1 
ATOM   4733 O  OE1 . GLU E 1 40  ? -21.157 -49.766 32.975 1.00 109.30 ? 40  GLU E OE1 1 
ATOM   4734 O  OE2 . GLU E 1 40  ? -22.119 -48.784 31.237 1.00 104.17 ? 40  GLU E OE2 1 
ATOM   4735 N  N   . GLY E 1 41  ? -22.147 -53.291 28.773 1.00 89.19  ? 41  GLY E N   1 
ATOM   4736 C  CA  . GLY E 1 41  ? -21.177 -53.562 27.713 1.00 87.46  ? 41  GLY E CA  1 
ATOM   4737 C  C   . GLY E 1 41  ? -21.685 -54.424 26.572 1.00 84.03  ? 41  GLY E C   1 
ATOM   4738 O  O   . GLY E 1 41  ? -22.886 -54.518 26.332 1.00 82.60  ? 41  GLY E O   1 
ATOM   4739 N  N   . LEU E 1 42  ? -20.760 -55.039 25.848 1.00 83.03  ? 42  LEU E N   1 
ATOM   4740 C  CA  . LEU E 1 42  ? -21.118 -55.731 24.621 1.00 80.43  ? 42  LEU E CA  1 
ATOM   4741 C  C   . LEU E 1 42  ? -21.568 -57.153 24.869 1.00 79.46  ? 42  LEU E C   1 
ATOM   4742 O  O   . LEU E 1 42  ? -21.064 -57.832 25.757 1.00 81.68  ? 42  LEU E O   1 
ATOM   4743 C  CB  . LEU E 1 42  ? -19.945 -55.768 23.639 1.00 80.92  ? 42  LEU E CB  1 
ATOM   4744 C  CG  . LEU E 1 42  ? -19.615 -54.474 22.900 1.00 81.48  ? 42  LEU E CG  1 
ATOM   4745 C  CD1 . LEU E 1 42  ? -18.351 -53.799 23.509 1.00 85.04  ? 42  LEU E CD1 1 
ATOM   4746 C  CD2 . LEU E 1 42  ? -19.464 -54.775 21.406 1.00 79.57  ? 42  LEU E CD2 1 
ATOM   4747 N  N   . HIS E 1 43  ? -22.497 -57.614 24.045 1.00 76.51  ? 43  HIS E N   1 
ATOM   4748 C  CA  . HIS E 1 43  ? -22.949 -58.988 24.101 1.00 75.57  ? 43  HIS E CA  1 
ATOM   4749 C  C   . HIS E 1 43  ? -23.228 -59.517 22.718 1.00 73.19  ? 43  HIS E C   1 
ATOM   4750 O  O   . HIS E 1 43  ? -23.861 -58.856 21.912 1.00 71.50  ? 43  HIS E O   1 
ATOM   4751 C  CB  . HIS E 1 43  ? -24.209 -59.077 24.935 1.00 75.49  ? 43  HIS E CB  1 
ATOM   4752 C  CG  . HIS E 1 43  ? -23.981 -58.838 26.390 1.00 78.58  ? 43  HIS E CG  1 
ATOM   4753 N  ND1 . HIS E 1 43  ? -23.713 -59.861 27.267 1.00 82.01  ? 43  HIS E ND1 1 
ATOM   4754 C  CD2 . HIS E 1 43  ? -23.983 -57.699 27.124 1.00 80.69  ? 43  HIS E CD2 1 
ATOM   4755 C  CE1 . HIS E 1 43  ? -23.580 -59.365 28.486 1.00 85.72  ? 43  HIS E CE1 1 
ATOM   4756 N  NE2 . HIS E 1 43  ? -23.734 -58.053 28.425 1.00 84.74  ? 43  HIS E NE2 1 
ATOM   4757 N  N   . GLY E 1 44  ? -22.765 -60.723 22.454 1.00 73.46  ? 44  GLY E N   1 
ATOM   4758 C  CA  . GLY E 1 44  ? -23.000 -61.375 21.177 1.00 72.60  ? 44  GLY E CA  1 
ATOM   4759 C  C   . GLY E 1 44  ? -24.470 -61.630 20.896 1.00 70.81  ? 44  GLY E C   1 
ATOM   4760 O  O   . GLY E 1 44  ? -25.265 -61.733 21.813 1.00 70.82  ? 44  GLY E O   1 
ATOM   4761 N  N   . PHE E 1 45  ? -24.836 -61.749 19.629 1.00 69.91  ? 45  PHE E N   1 
ATOM   4762 C  CA  . PHE E 1 45  ? -26.223 -61.712 19.259 1.00 68.63  ? 45  PHE E CA  1 
ATOM   4763 C  C   . PHE E 1 45  ? -26.369 -62.381 17.940 1.00 68.77  ? 45  PHE E C   1 
ATOM   4764 O  O   . PHE E 1 45  ? -25.970 -61.829 16.962 1.00 68.83  ? 45  PHE E O   1 
ATOM   4765 C  CB  . PHE E 1 45  ? -26.613 -60.254 19.141 1.00 68.17  ? 45  PHE E CB  1 
ATOM   4766 C  CG  . PHE E 1 45  ? -28.077 -60.004 18.932 1.00 67.66  ? 45  PHE E CG  1 
ATOM   4767 C  CD1 . PHE E 1 45  ? -28.983 -60.322 19.903 1.00 68.01  ? 45  PHE E CD1 1 
ATOM   4768 C  CD2 . PHE E 1 45  ? -28.537 -59.360 17.803 1.00 67.68  ? 45  PHE E CD2 1 
ATOM   4769 C  CE1 . PHE E 1 45  ? -30.316 -60.043 19.728 1.00 68.06  ? 45  PHE E CE1 1 
ATOM   4770 C  CE2 . PHE E 1 45  ? -29.858 -59.083 17.639 1.00 67.26  ? 45  PHE E CE2 1 
ATOM   4771 C  CZ  . PHE E 1 45  ? -30.744 -59.429 18.595 1.00 67.66  ? 45  PHE E CZ  1 
ATOM   4772 N  N   . HIS E 1 46  ? -26.947 -63.572 17.905 1.00 69.32  ? 46  HIS E N   1 
ATOM   4773 C  CA  . HIS E 1 46  ? -26.991 -64.377 16.685 1.00 70.61  ? 46  HIS E CA  1 
ATOM   4774 C  C   . HIS E 1 46  ? -28.285 -65.115 16.474 1.00 69.93  ? 46  HIS E C   1 
ATOM   4775 O  O   . HIS E 1 46  ? -28.984 -65.435 17.416 1.00 69.46  ? 46  HIS E O   1 
ATOM   4776 C  CB  . HIS E 1 46  ? -25.898 -65.429 16.746 1.00 73.04  ? 46  HIS E CB  1 
ATOM   4777 C  CG  . HIS E 1 46  ? -24.614 -64.912 17.277 1.00 75.81  ? 46  HIS E CG  1 
ATOM   4778 N  ND1 . HIS E 1 46  ? -24.055 -65.376 18.447 1.00 79.07  ? 46  HIS E ND1 1 
ATOM   4779 C  CD2 . HIS E 1 46  ? -23.798 -63.933 16.823 1.00 78.54  ? 46  HIS E CD2 1 
ATOM   4780 C  CE1 . HIS E 1 46  ? -22.930 -64.716 18.678 1.00 81.48  ? 46  HIS E CE1 1 
ATOM   4781 N  NE2 . HIS E 1 46  ? -22.755 -63.832 17.710 1.00 80.34  ? 46  HIS E NE2 1 
ATOM   4782 N  N   . VAL E 1 47  ? -28.570 -65.417 15.222 1.00 70.60  ? 47  VAL E N   1 
ATOM   4783 C  CA  . VAL E 1 47  ? -29.549 -66.417 14.904 1.00 71.20  ? 47  VAL E CA  1 
ATOM   4784 C  C   . VAL E 1 47  ? -28.827 -67.742 14.838 1.00 73.64  ? 47  VAL E C   1 
ATOM   4785 O  O   . VAL E 1 47  ? -27.872 -67.876 14.108 1.00 75.60  ? 47  VAL E O   1 
ATOM   4786 C  CB  . VAL E 1 47  ? -30.167 -66.171 13.550 1.00 71.66  ? 47  VAL E CB  1 
ATOM   4787 C  CG1 . VAL E 1 47  ? -31.175 -67.212 13.265 1.00 72.49  ? 47  VAL E CG1 1 
ATOM   4788 C  CG2 . VAL E 1 47  ? -30.813 -64.856 13.523 1.00 70.19  ? 47  VAL E CG2 1 
ATOM   4789 N  N   . HIS E 1 48  ? -29.273 -68.727 15.596 1.00 74.56  ? 48  HIS E N   1 
ATOM   4790 C  CA  . HIS E 1 48  ? -28.703 -70.058 15.516 1.00 77.66  ? 48  HIS E CA  1 
ATOM   4791 C  C   . HIS E 1 48  ? -29.610 -70.914 14.672 1.00 78.98  ? 48  HIS E C   1 
ATOM   4792 O  O   . HIS E 1 48  ? -30.732 -70.527 14.378 1.00 77.60  ? 48  HIS E O   1 
ATOM   4793 C  CB  . HIS E 1 48  ? -28.575 -70.663 16.891 1.00 78.51  ? 48  HIS E CB  1 
ATOM   4794 C  CG  . HIS E 1 48  ? -27.537 -70.008 17.730 1.00 79.57  ? 48  HIS E CG  1 
ATOM   4795 N  ND1 . HIS E 1 48  ? -26.530 -70.717 18.340 1.00 83.17  ? 48  HIS E ND1 1 
ATOM   4796 C  CD2 . HIS E 1 48  ? -27.349 -68.710 18.063 1.00 79.19  ? 48  HIS E CD2 1 
ATOM   4797 C  CE1 . HIS E 1 48  ? -25.763 -69.879 19.014 1.00 83.99  ? 48  HIS E CE1 1 
ATOM   4798 N  NE2 . HIS E 1 48  ? -26.240 -68.656 18.865 1.00 80.84  ? 48  HIS E NE2 1 
ATOM   4799 N  N   . GLU E 1 49  ? -29.126 -72.092 14.303 1.00 82.20  ? 49  GLU E N   1 
ATOM   4800 C  CA  . GLU E 1 49  ? -29.771 -72.905 13.267 1.00 84.64  ? 49  GLU E CA  1 
ATOM   4801 C  C   . GLU E 1 49  ? -31.178 -73.384 13.587 1.00 83.85  ? 49  GLU E C   1 
ATOM   4802 O  O   . GLU E 1 49  ? -32.042 -73.356 12.704 1.00 83.63  ? 49  GLU E O   1 
ATOM   4803 C  CB  . GLU E 1 49  ? -28.909 -74.130 12.920 1.00 88.98  ? 49  GLU E CB  1 
ATOM   4804 C  CG  . GLU E 1 49  ? -29.297 -74.808 11.578 1.00 93.45  ? 49  GLU E CG  1 
ATOM   4805 C  CD  . GLU E 1 49  ? -28.264 -75.841 11.081 1.00 100.60 ? 49  GLU E CD  1 
ATOM   4806 O  OE1 . GLU E 1 49  ? -27.111 -75.855 11.593 1.00 103.42 ? 49  GLU E OE1 1 
ATOM   4807 O  OE2 . GLU E 1 49  ? -28.603 -76.643 10.174 1.00 105.41 ? 49  GLU E OE2 1 
ATOM   4808 N  N   . PHE E 1 50  ? -31.406 -73.832 14.831 1.00 83.72  ? 50  PHE E N   1 
ATOM   4809 C  CA  . PHE E 1 50  ? -32.647 -74.559 15.169 1.00 84.46  ? 50  PHE E CA  1 
ATOM   4810 C  C   . PHE E 1 50  ? -33.589 -73.888 16.129 1.00 81.93  ? 50  PHE E C   1 
ATOM   4811 O  O   . PHE E 1 50  ? -33.141 -73.246 17.078 1.00 80.35  ? 50  PHE E O   1 
ATOM   4812 C  CB  . PHE E 1 50  ? -32.309 -75.918 15.743 1.00 87.59  ? 50  PHE E CB  1 
ATOM   4813 C  CG  . PHE E 1 50  ? -31.447 -76.741 14.844 1.00 92.28  ? 50  PHE E CG  1 
ATOM   4814 C  CD1 . PHE E 1 50  ? -31.726 -76.840 13.477 1.00 94.27  ? 50  PHE E CD1 1 
ATOM   4815 C  CD2 . PHE E 1 50  ? -30.352 -77.423 15.361 1.00 96.40  ? 50  PHE E CD2 1 
ATOM   4816 C  CE1 . PHE E 1 50  ? -30.941 -77.596 12.665 1.00 98.50  ? 50  PHE E CE1 1 
ATOM   4817 C  CE2 . PHE E 1 50  ? -29.552 -78.188 14.545 1.00 100.50 ? 50  PHE E CE2 1 
ATOM   4818 C  CZ  . PHE E 1 50  ? -29.847 -78.279 13.198 1.00 101.69 ? 50  PHE E CZ  1 
ATOM   4819 N  N   . GLY E 1 51  ? -34.891 -74.082 15.886 1.00 82.02  ? 51  GLY E N   1 
ATOM   4820 C  CA  . GLY E 1 51  ? -35.939 -73.632 16.801 1.00 81.16  ? 51  GLY E CA  1 
ATOM   4821 C  C   . GLY E 1 51  ? -36.189 -74.633 17.917 1.00 83.33  ? 51  GLY E C   1 
ATOM   4822 O  O   . GLY E 1 51  ? -37.309 -74.925 18.288 1.00 84.00  ? 51  GLY E O   1 
ATOM   4823 N  N   . ASP E 1 52  ? -35.118 -75.170 18.454 1.00 85.18  ? 52  ASP E N   1 
ATOM   4824 C  CA  . ASP E 1 52  ? -35.201 -76.246 19.400 1.00 88.22  ? 52  ASP E CA  1 
ATOM   4825 C  C   . ASP E 1 52  ? -34.930 -75.595 20.717 1.00 87.78  ? 52  ASP E C   1 
ATOM   4826 O  O   . ASP E 1 52  ? -33.964 -74.859 20.871 1.00 86.67  ? 52  ASP E O   1 
ATOM   4827 C  CB  . ASP E 1 52  ? -34.132 -77.292 19.070 1.00 91.17  ? 52  ASP E CB  1 
ATOM   4828 C  CG  . ASP E 1 52  ? -34.537 -78.695 19.464 1.00 95.22  ? 52  ASP E CG  1 
ATOM   4829 O  OD1 . ASP E 1 52  ? -34.890 -78.878 20.659 1.00 96.08  ? 52  ASP E OD1 1 
ATOM   4830 O  OD2 . ASP E 1 52  ? -34.474 -79.596 18.569 1.00 98.23  ? 52  ASP E OD2 1 
ATOM   4831 N  N   . ASN E 1 53  ? -35.815 -75.816 21.664 1.00 89.42  ? 53  ASN E N   1 
ATOM   4832 C  CA  . ASN E 1 53  ? -35.560 -75.380 23.023 1.00 90.55  ? 53  ASN E CA  1 
ATOM   4833 C  C   . ASN E 1 53  ? -35.811 -76.503 23.980 1.00 94.06  ? 53  ASN E C   1 
ATOM   4834 O  O   . ASN E 1 53  ? -36.072 -76.267 25.152 1.00 95.50  ? 53  ASN E O   1 
ATOM   4835 C  CB  . ASN E 1 53  ? -36.412 -74.172 23.360 1.00 88.91  ? 53  ASN E CB  1 
ATOM   4836 C  CG  . ASN E 1 53  ? -35.691 -72.840 23.047 1.00 88.86  ? 53  ASN E CG  1 
ATOM   4837 O  OD1 . ASN E 1 53  ? -35.719 -71.937 23.879 1.00 93.81  ? 53  ASN E OD1 1 
ATOM   4838 N  ND2 . ASN E 1 53  ? -35.042 -72.719 21.859 1.00 87.92  ? 53  ASN E ND2 1 
ATOM   4839 N  N   . THR E 1 54  ? -35.701 -77.721 23.450 1.00 95.94  ? 54  THR E N   1 
ATOM   4840 C  CA  . THR E 1 54  ? -35.873 -78.945 24.191 1.00 100.22 ? 54  THR E CA  1 
ATOM   4841 C  C   . THR E 1 54  ? -35.056 -78.907 25.462 1.00 102.68 ? 54  THR E C   1 
ATOM   4842 O  O   . THR E 1 54  ? -35.594 -79.080 26.536 1.00 105.31 ? 54  THR E O   1 
ATOM   4843 C  CB  . THR E 1 54  ? -35.391 -80.132 23.344 1.00 102.45 ? 54  THR E CB  1 
ATOM   4844 O  OG1 . THR E 1 54  ? -36.117 -80.127 22.112 1.00 100.12 ? 54  THR E OG1 1 
ATOM   4845 C  CG2 . THR E 1 54  ? -35.553 -81.487 24.093 1.00 108.34 ? 54  THR E CG2 1 
ATOM   4846 N  N   . ALA E 1 55  ? -33.756 -78.681 25.325 1.00 102.47 ? 55  ALA E N   1 
ATOM   4847 C  CA  . ALA E 1 55  ? -32.844 -78.606 26.457 1.00 105.34 ? 55  ALA E CA  1 
ATOM   4848 C  C   . ALA E 1 55  ? -32.309 -77.166 26.592 1.00 102.31 ? 55  ALA E C   1 
ATOM   4849 O  O   . ALA E 1 55  ? -31.122 -76.905 26.332 1.00 101.85 ? 55  ALA E O   1 
ATOM   4850 C  CB  . ALA E 1 55  ? -31.687 -79.614 26.277 1.00 108.71 ? 55  ALA E CB  1 
ATOM   4851 N  N   . GLY E 1 56  ? -33.184 -76.240 26.997 1.00 100.88 ? 56  GLY E N   1 
ATOM   4852 C  CA  . GLY E 1 56  ? -32.826 -74.817 27.107 1.00 98.24  ? 56  GLY E CA  1 
ATOM   4853 C  C   . GLY E 1 56  ? -32.264 -74.272 25.796 1.00 94.82  ? 56  GLY E C   1 
ATOM   4854 O  O   . GLY E 1 56  ? -32.695 -74.669 24.692 1.00 93.48  ? 56  GLY E O   1 
ATOM   4855 N  N   . CYS E 1 57  ? -31.275 -73.387 25.899 1.00 93.81  ? 57  CYS E N   1 
ATOM   4856 C  CA  . CYS E 1 57  ? -30.725 -72.738 24.700 1.00 90.83  ? 57  CYS E CA  1 
ATOM   4857 C  C   . CYS E 1 57  ? -29.720 -73.582 23.918 1.00 91.76  ? 57  CYS E C   1 
ATOM   4858 O  O   . CYS E 1 57  ? -29.533 -73.339 22.731 1.00 89.65  ? 57  CYS E O   1 
ATOM   4859 C  CB  . CYS E 1 57  ? -30.154 -71.363 25.043 1.00 88.99  ? 57  CYS E CB  1 
ATOM   4860 S  SG  . CYS E 1 57  ? -31.465 -70.155 25.529 1.00 89.70  ? 57  CYS E SG  1 
ATOM   4861 N  N   . THR E 1 58  ? -29.109 -74.582 24.560 1.00 95.58  ? 58  THR E N   1 
ATOM   4862 C  CA  . THR E 1 58  ? -28.106 -75.461 23.892 1.00 97.75  ? 58  THR E CA  1 
ATOM   4863 C  C   . THR E 1 58  ? -28.694 -76.258 22.706 1.00 97.54  ? 58  THR E C   1 
ATOM   4864 O  O   . THR E 1 58  ? -27.980 -76.614 21.762 1.00 98.36  ? 58  THR E O   1 
ATOM   4865 C  CB  . THR E 1 58  ? -27.447 -76.499 24.857 1.00 102.83 ? 58  THR E CB  1 
ATOM   4866 O  OG1 . THR E 1 58  ? -27.707 -76.135 26.215 1.00 103.90 ? 58  THR E OG1 1 
ATOM   4867 C  CG2 . THR E 1 58  ? -25.919 -76.610 24.613 1.00 104.16 ? 58  THR E CG2 1 
ATOM   4868 N  N   . SER E 1 59  ? -29.993 -76.539 22.770 1.00 96.82  ? 59  SER E N   1 
ATOM   4869 C  CA  . SER E 1 59  ? -30.695 -77.240 21.698 1.00 96.77  ? 59  SER E CA  1 
ATOM   4870 C  C   . SER E 1 59  ? -30.670 -76.492 20.362 1.00 93.48  ? 59  SER E C   1 
ATOM   4871 O  O   . SER E 1 59  ? -30.769 -77.118 19.298 1.00 94.39  ? 59  SER E O   1 
ATOM   4872 C  CB  . SER E 1 59  ? -32.148 -77.473 22.110 1.00 96.72  ? 59  SER E CB  1 
ATOM   4873 O  OG  . SER E 1 59  ? -32.213 -78.039 23.399 1.00 100.63 ? 59  SER E OG  1 
ATOM   4874 N  N   . ALA E 1 60  ? -30.549 -75.161 20.435 1.00 90.18  ? 60  ALA E N   1 
ATOM   4875 C  CA  . ALA E 1 60  ? -30.533 -74.269 19.265 1.00 87.47  ? 60  ALA E CA  1 
ATOM   4876 C  C   . ALA E 1 60  ? -29.468 -74.648 18.244 1.00 89.07  ? 60  ALA E C   1 
ATOM   4877 O  O   . ALA E 1 60  ? -29.628 -74.439 17.033 1.00 88.18  ? 60  ALA E O   1 
ATOM   4878 C  CB  . ALA E 1 60  ? -30.317 -72.838 19.728 1.00 84.72  ? 60  ALA E CB  1 
ATOM   4879 N  N   . GLY E 1 61  ? -28.379 -75.203 18.758 1.00 91.81  ? 61  GLY E N   1 
ATOM   4880 C  CA  . GLY E 1 61  ? -27.301 -75.678 17.933 1.00 94.50  ? 61  GLY E CA  1 
ATOM   4881 C  C   . GLY E 1 61  ? -26.369 -74.542 17.588 1.00 93.09  ? 61  GLY E C   1 
ATOM   4882 O  O   . GLY E 1 61  ? -26.406 -73.485 18.233 1.00 90.47  ? 61  GLY E O   1 
ATOM   4883 N  N   . PRO E 1 62  ? -25.541 -74.743 16.546 1.00 95.30  ? 62  PRO E N   1 
ATOM   4884 C  CA  . PRO E 1 62  ? -24.548 -73.752 16.172 1.00 94.70  ? 62  PRO E CA  1 
ATOM   4885 C  C   . PRO E 1 62  ? -25.188 -72.567 15.431 1.00 91.43  ? 62  PRO E C   1 
ATOM   4886 O  O   . PRO E 1 62  ? -26.393 -72.589 15.111 1.00 89.72  ? 62  PRO E O   1 
ATOM   4887 C  CB  . PRO E 1 62  ? -23.683 -74.523 15.189 1.00 98.90  ? 62  PRO E CB  1 
ATOM   4888 C  CG  . PRO E 1 62  ? -24.709 -75.361 14.427 1.00 99.66  ? 62  PRO E CG  1 
ATOM   4889 C  CD  . PRO E 1 62  ? -25.741 -75.734 15.463 1.00 98.15  ? 62  PRO E CD  1 
ATOM   4890 N  N   . HIS E 1 63  ? -24.368 -71.571 15.116 1.00 90.90  ? 63  HIS E N   1 
ATOM   4891 C  CA  . HIS E 1 63  ? -24.835 -70.415 14.388 1.00 88.66  ? 63  HIS E CA  1 
ATOM   4892 C  C   . HIS E 1 63  ? -25.430 -70.817 13.064 1.00 89.39  ? 63  HIS E C   1 
ATOM   4893 O  O   . HIS E 1 63  ? -24.928 -71.722 12.397 1.00 92.84  ? 63  HIS E O   1 
ATOM   4894 C  CB  . HIS E 1 63  ? -23.679 -69.504 14.093 1.00 89.67  ? 63  HIS E CB  1 
ATOM   4895 C  CG  . HIS E 1 63  ? -23.145 -68.804 15.295 1.00 90.17  ? 63  HIS E CG  1 
ATOM   4896 N  ND1 . HIS E 1 63  ? -22.719 -67.496 15.252 1.00 90.12  ? 63  HIS E ND1 1 
ATOM   4897 C  CD2 . HIS E 1 63  ? -22.973 -69.218 16.572 1.00 92.70  ? 63  HIS E CD2 1 
ATOM   4898 C  CE1 . HIS E 1 63  ? -22.286 -67.138 16.445 1.00 90.80  ? 63  HIS E CE1 1 
ATOM   4899 N  NE2 . HIS E 1 63  ? -22.438 -68.161 17.267 1.00 92.78  ? 63  HIS E NE2 1 
ATOM   4900 N  N   . PHE E 1 64  ? -26.476 -70.106 12.669 1.00 86.57  ? 64  PHE E N   1 
ATOM   4901 C  CA  . PHE E 1 64  ? -27.148 -70.378 11.416 1.00 87.74  ? 64  PHE E CA  1 
ATOM   4902 C  C   . PHE E 1 64  ? -26.196 -70.117 10.308 1.00 90.03  ? 64  PHE E C   1 
ATOM   4903 O  O   . PHE E 1 64  ? -25.864 -68.982 10.043 1.00 88.76  ? 64  PHE E O   1 
ATOM   4904 C  CB  . PHE E 1 64  ? -28.361 -69.478 11.238 1.00 85.39  ? 64  PHE E CB  1 
ATOM   4905 C  CG  . PHE E 1 64  ? -29.139 -69.734 9.969  1.00 88.20  ? 64  PHE E CG  1 
ATOM   4906 C  CD1 . PHE E 1 64  ? -29.346 -71.033 9.494  1.00 92.12  ? 64  PHE E CD1 1 
ATOM   4907 C  CD2 . PHE E 1 64  ? -29.721 -68.671 9.270  1.00 88.38  ? 64  PHE E CD2 1 
ATOM   4908 C  CE1 . PHE E 1 64  ? -30.092 -71.262 8.331  1.00 94.35  ? 64  PHE E CE1 1 
ATOM   4909 C  CE2 . PHE E 1 64  ? -30.477 -68.888 8.094  1.00 91.25  ? 64  PHE E CE2 1 
ATOM   4910 C  CZ  . PHE E 1 64  ? -30.656 -70.181 7.627  1.00 93.96  ? 64  PHE E CZ  1 
ATOM   4911 N  N   . ASN E 1 65  ? -25.773 -71.177 9.645  1.00 93.86  ? 65  ASN E N   1 
ATOM   4912 C  CA  . ASN E 1 65  ? -24.698 -71.077 8.680  1.00 97.62  ? 65  ASN E CA  1 
ATOM   4913 C  C   . ASN E 1 65  ? -24.941 -71.981 7.461  1.00 102.24 ? 65  ASN E C   1 
ATOM   4914 O  O   . ASN E 1 65  ? -24.304 -73.043 7.302  1.00 105.97 ? 65  ASN E O   1 
ATOM   4915 C  CB  . ASN E 1 65  ? -23.372 -71.412 9.367  1.00 98.94  ? 65  ASN E CB  1 
ATOM   4916 C  CG  . ASN E 1 65  ? -22.210 -71.197 8.469  1.00 102.08 ? 65  ASN E CG  1 
ATOM   4917 O  OD1 . ASN E 1 65  ? -22.337 -70.537 7.422  1.00 103.07 ? 65  ASN E OD1 1 
ATOM   4918 N  ND2 . ASN E 1 65  ? -21.064 -71.734 8.851  1.00 102.82 ? 65  ASN E ND2 1 
ATOM   4919 N  N   . PRO E 1 66  ? -25.862 -71.545 6.585  1.00 102.52 ? 66  PRO E N   1 
ATOM   4920 C  CA  . PRO E 1 66  ? -26.279 -72.390 5.463  1.00 107.05 ? 66  PRO E CA  1 
ATOM   4921 C  C   . PRO E 1 66  ? -25.238 -72.443 4.327  1.00 112.91 ? 66  PRO E C   1 
ATOM   4922 O  O   . PRO E 1 66  ? -25.188 -73.449 3.612  1.00 117.89 ? 66  PRO E O   1 
ATOM   4923 C  CB  . PRO E 1 66  ? -27.596 -71.741 4.999  1.00 105.15 ? 66  PRO E CB  1 
ATOM   4924 C  CG  . PRO E 1 66  ? -27.399 -70.286 5.279  1.00 102.20 ? 66  PRO E CG  1 
ATOM   4925 C  CD  . PRO E 1 66  ? -26.431 -70.185 6.488  1.00 99.52  ? 66  PRO E CD  1 
ATOM   4926 N  N   . LEU E 1 67  ? -24.410 -71.397 4.174  1.00 113.06 ? 67  LEU E N   1 
ATOM   4927 C  CA  . LEU E 1 67  ? -23.380 -71.358 3.119  1.00 118.92 ? 67  LEU E CA  1 
ATOM   4928 C  C   . LEU E 1 67  ? -22.016 -71.923 3.619  1.00 121.39 ? 67  LEU E C   1 
ATOM   4929 O  O   . LEU E 1 67  ? -20.985 -71.790 2.920  1.00 126.20 ? 67  LEU E O   1 
ATOM   4930 C  CB  . LEU E 1 67  ? -23.179 -69.926 2.588  1.00 118.64 ? 67  LEU E CB  1 
ATOM   4931 C  CG  . LEU E 1 67  ? -24.381 -68.994 2.311  1.00 116.41 ? 67  LEU E CG  1 
ATOM   4932 C  CD1 . LEU E 1 67  ? -24.049 -67.522 2.737  1.00 113.49 ? 67  LEU E CD1 1 
ATOM   4933 C  CD2 . LEU E 1 67  ? -24.864 -69.053 0.859  1.00 120.48 ? 67  LEU E CD2 1 
ATOM   4934 N  N   . SER E 1 68  ? -22.004 -72.531 4.818  1.00 118.76 ? 68  SER E N   1 
ATOM   4935 C  CA  . SER E 1 68  ? -20.781 -73.125 5.416  1.00 121.10 ? 68  SER E CA  1 
ATOM   4936 C  C   . SER E 1 68  ? -19.553 -72.204 5.475  1.00 122.03 ? 68  SER E C   1 
ATOM   4937 O  O   . SER E 1 68  ? -18.450 -72.640 5.205  1.00 126.81 ? 68  SER E O   1 
ATOM   4938 C  CB  . SER E 1 68  ? -20.411 -74.411 4.687  1.00 127.60 ? 68  SER E CB  1 
ATOM   4939 O  OG  . SER E 1 68  ? -21.256 -75.448 5.108  1.00 127.07 ? 68  SER E OG  1 
ATOM   4940 N  N   . ARG E 1 69  ? -19.755 -70.941 5.841  1.00 118.17 ? 69  ARG E N   1 
ATOM   4941 C  CA  . ARG E 1 69  ? -18.657 -69.976 5.994  1.00 119.06 ? 69  ARG E CA  1 
ATOM   4942 C  C   . ARG E 1 69  ? -18.070 -70.041 7.414  1.00 116.45 ? 69  ARG E C   1 
ATOM   4943 O  O   . ARG E 1 69  ? -18.588 -70.743 8.309  1.00 114.06 ? 69  ARG E O   1 
ATOM   4944 C  CB  . ARG E 1 69  ? -19.141 -68.540 5.723  1.00 116.25 ? 69  ARG E CB  1 
ATOM   4945 C  CG  . ARG E 1 69  ? -19.844 -68.357 4.400  1.00 120.47 ? 69  ARG E CG  1 
ATOM   4946 C  CD  . ARG E 1 69  ? -18.853 -68.323 3.242  1.00 129.75 ? 69  ARG E CD  1 
ATOM   4947 N  NE  . ARG E 1 69  ? -19.551 -68.079 1.983  1.00 135.08 ? 69  ARG E NE  1 
ATOM   4948 C  CZ  . ARG E 1 69  ? -20.014 -66.888 1.577  1.00 135.42 ? 69  ARG E CZ  1 
ATOM   4949 N  NH1 . ARG E 1 69  ? -19.833 -65.778 2.308  1.00 132.03 ? 69  ARG E NH1 1 
ATOM   4950 N  NH2 . ARG E 1 69  ? -20.668 -66.800 0.411  1.00 139.31 ? 69  ARG E NH2 1 
ATOM   4951 N  N   . LYS E 1 70  ? -16.984 -69.291 7.602  1.00 117.36 ? 70  LYS E N   1 
ATOM   4952 C  CA  . LYS E 1 70  ? -16.392 -69.078 8.937  1.00 115.00 ? 70  LYS E CA  1 
ATOM   4953 C  C   . LYS E 1 70  ? -17.116 -67.897 9.627  1.00 108.30 ? 70  LYS E C   1 
ATOM   4954 O  O   . LYS E 1 70  ? -17.674 -66.981 8.955  1.00 106.23 ? 70  LYS E O   1 
ATOM   4955 C  CB  . LYS E 1 70  ? -14.862 -68.783 8.862  1.00 119.53 ? 70  LYS E CB  1 
ATOM   4956 C  CG  . LYS E 1 70  ? -14.023 -69.611 7.825  1.00 128.12 ? 70  LYS E CG  1 
ATOM   4957 C  CD  . LYS E 1 70  ? -13.087 -70.680 8.476  1.00 134.05 ? 70  LYS E CD  1 
ATOM   4958 C  CE  . LYS E 1 70  ? -11.735 -70.739 7.685  1.00 142.43 ? 70  LYS E CE  1 
ATOM   4959 N  NZ  . LYS E 1 70  ? -10.826 -71.905 7.961  1.00 148.89 ? 70  LYS E NZ  1 
ATOM   4960 N  N   . HIS E 1 71  ? -17.084 -67.920 10.962 1.00 104.89 ? 71  HIS E N   1 
ATOM   4961 C  CA  . HIS E 1 71  ? -17.772 -66.896 11.744 1.00 99.56  ? 71  HIS E CA  1 
ATOM   4962 C  C   . HIS E 1 71  ? -17.161 -65.524 11.473 1.00 99.33  ? 71  HIS E C   1 
ATOM   4963 O  O   . HIS E 1 71  ? -15.952 -65.415 11.275 1.00 102.62 ? 71  HIS E O   1 
ATOM   4964 C  CB  . HIS E 1 71  ? -17.731 -67.218 13.250 1.00 97.60  ? 71  HIS E CB  1 
ATOM   4965 C  CG  . HIS E 1 71  ? -18.357 -66.163 14.125 1.00 92.73  ? 71  HIS E CG  1 
ATOM   4966 N  ND1 . HIS E 1 71  ? -19.720 -66.000 14.253 1.00 89.11  ? 71  HIS E ND1 1 
ATOM   4967 C  CD2 . HIS E 1 71  ? -17.796 -65.221 14.919 1.00 91.10  ? 71  HIS E CD2 1 
ATOM   4968 C  CE1 . HIS E 1 71  ? -19.969 -64.995 15.076 1.00 86.01  ? 71  HIS E CE1 1 
ATOM   4969 N  NE2 . HIS E 1 71  ? -18.818 -64.508 15.497 1.00 87.00  ? 71  HIS E NE2 1 
ATOM   4970 N  N   . GLY E 1 72  ? -18.000 -64.491 11.472 1.00 95.89  ? 72  GLY E N   1 
ATOM   4971 C  CA  . GLY E 1 72  ? -17.525 -63.127 11.326 1.00 95.91  ? 72  GLY E CA  1 
ATOM   4972 C  C   . GLY E 1 72  ? -18.438 -62.090 11.951 1.00 92.17  ? 72  GLY E C   1 
ATOM   4973 O  O   . GLY E 1 72  ? -19.389 -62.408 12.683 1.00 89.76  ? 72  GLY E O   1 
ATOM   4974 N  N   . GLY E 1 73  ? -18.120 -60.830 11.692 1.00 92.65  ? 73  GLY E N   1 
ATOM   4975 C  CA  . GLY E 1 73  ? -18.971 -59.719 12.097 1.00 89.85  ? 73  GLY E CA  1 
ATOM   4976 C  C   . GLY E 1 73  ? -20.035 -59.485 11.042 1.00 89.88  ? 73  GLY E C   1 
ATOM   4977 O  O   . GLY E 1 73  ? -19.934 -59.983 9.931  1.00 92.54  ? 73  GLY E O   1 
ATOM   4978 N  N   . PRO E 1 74  ? -21.053 -58.701 11.376 1.00 87.70  ? 74  PRO E N   1 
ATOM   4979 C  CA  . PRO E 1 74  ? -22.176 -58.658 10.485 1.00 87.93  ? 74  PRO E CA  1 
ATOM   4980 C  C   . PRO E 1 74  ? -21.838 -57.940 9.224  1.00 91.56  ? 74  PRO E C   1 
ATOM   4981 O  O   . PRO E 1 74  ? -22.334 -58.314 8.181  1.00 93.42  ? 74  PRO E O   1 
ATOM   4982 C  CB  . PRO E 1 74  ? -23.219 -57.879 11.269 1.00 85.13  ? 74  PRO E CB  1 
ATOM   4983 C  CG  . PRO E 1 74  ? -22.438 -56.984 12.155 1.00 85.03  ? 74  PRO E CG  1 
ATOM   4984 C  CD  . PRO E 1 74  ? -21.086 -57.617 12.370 1.00 86.09  ? 74  PRO E CD  1 
ATOM   4985 N  N   . LYS E 1 75  ? -20.985 -56.920 9.310  1.00 93.37  ? 75  LYS E N   1 
ATOM   4986 C  CA  . LYS E 1 75  ? -20.580 -56.155 8.131  1.00 97.75  ? 75  LYS E CA  1 
ATOM   4987 C  C   . LYS E 1 75  ? -19.396 -56.826 7.426  1.00 101.23 ? 75  LYS E C   1 
ATOM   4988 O  O   . LYS E 1 75  ? -19.080 -56.474 6.300  1.00 105.16 ? 75  LYS E O   1 
ATOM   4989 C  CB  . LYS E 1 75  ? -20.261 -54.718 8.517  1.00 98.21  ? 75  LYS E CB  1 
ATOM   4990 C  CG  . LYS E 1 75  ? -21.484 -53.942 9.068  1.00 98.57  ? 75  LYS E CG  1 
ATOM   4991 C  CD  . LYS E 1 75  ? -21.230 -52.418 9.143  1.00 103.72 ? 75  LYS E CD  1 
ATOM   4992 C  CE  . LYS E 1 75  ? -19.740 -52.106 9.565  1.00 106.89 ? 75  LYS E CE  1 
ATOM   4993 N  NZ  . LYS E 1 75  ? -19.330 -50.676 9.688  1.00 109.10 ? 75  LYS E NZ  1 
ATOM   4994 N  N   . ASP E 1 76  ? -18.773 -57.817 8.072  1.00 100.43 ? 76  ASP E N   1 
ATOM   4995 C  CA  . ASP E 1 76  ? -17.736 -58.620 7.425  1.00 104.44 ? 76  ASP E CA  1 
ATOM   4996 C  C   . ASP E 1 76  ? -18.349 -59.373 6.258  1.00 106.97 ? 76  ASP E C   1 
ATOM   4997 O  O   . ASP E 1 76  ? -19.563 -59.558 6.176  1.00 104.50 ? 76  ASP E O   1 
ATOM   4998 C  CB  . ASP E 1 76  ? -17.056 -59.611 8.393  1.00 103.56 ? 76  ASP E CB  1 
ATOM   4999 C  CG  . ASP E 1 76  ? -15.903 -58.971 9.178  1.00 104.85 ? 76  ASP E CG  1 
ATOM   5000 O  OD1 . ASP E 1 76  ? -15.076 -58.276 8.540  1.00 109.59 ? 76  ASP E OD1 1 
ATOM   5001 O  OD2 . ASP E 1 76  ? -15.811 -59.159 10.427 1.00 102.94 ? 76  ASP E OD2 1 
ATOM   5002 N  N   . GLU E 1 77  ? -17.491 -59.775 5.332  1.00 112.46 ? 77  GLU E N   1 
ATOM   5003 C  CA  . GLU E 1 77  ? -17.939 -60.460 4.137  1.00 116.39 ? 77  GLU E CA  1 
ATOM   5004 C  C   . GLU E 1 77  ? -17.979 -61.961 4.382  1.00 115.64 ? 77  GLU E C   1 
ATOM   5005 O  O   . GLU E 1 77  ? -18.988 -62.600 4.096  1.00 114.77 ? 77  GLU E O   1 
ATOM   5006 C  CB  . GLU E 1 77  ? -17.021 -60.142 2.963  1.00 123.58 ? 77  GLU E CB  1 
ATOM   5007 C  CG  . GLU E 1 77  ? -17.596 -60.655 1.611  1.00 131.01 ? 77  GLU E CG  1 
ATOM   5008 C  CD  . GLU E 1 77  ? -16.569 -61.447 0.781  1.00 142.35 ? 77  GLU E CD  1 
ATOM   5009 O  OE1 . GLU E 1 77  ? -15.618 -60.808 0.225  1.00 148.42 ? 77  GLU E OE1 1 
ATOM   5010 O  OE2 . GLU E 1 77  ? -16.727 -62.709 0.706  1.00 146.28 ? 77  GLU E OE2 1 
ATOM   5011 N  N   . GLU E 1 78  ? -16.872 -62.517 4.875  1.00 116.37 ? 78  GLU E N   1 
ATOM   5012 C  CA  . GLU E 1 78  ? -16.872 -63.888 5.388  1.00 115.77 ? 78  GLU E CA  1 
ATOM   5013 C  C   . GLU E 1 78  ? -17.567 -63.957 6.788  1.00 109.03 ? 78  GLU E C   1 
ATOM   5014 O  O   . GLU E 1 78  ? -16.959 -63.655 7.839  1.00 106.86 ? 78  GLU E O   1 
ATOM   5015 C  CB  . GLU E 1 78  ? -15.444 -64.466 5.458  1.00 120.22 ? 78  GLU E CB  1 
ATOM   5016 C  CG  . GLU E 1 78  ? -15.356 -65.975 5.891  1.00 122.39 ? 78  GLU E CG  1 
ATOM   5017 C  CD  . GLU E 1 78  ? -15.655 -67.013 4.747  1.00 129.21 ? 78  GLU E CD  1 
ATOM   5018 O  OE1 . GLU E 1 78  ? -16.288 -66.603 3.715  1.00 132.27 ? 78  GLU E OE1 1 
ATOM   5019 O  OE2 . GLU E 1 78  ? -15.265 -68.231 4.905  1.00 132.03 ? 78  GLU E OE2 1 
ATOM   5020 N  N   . ARG E 1 79  ? -18.840 -64.377 6.773  1.00 105.76 ? 79  ARG E N   1 
ATOM   5021 C  CA  . ARG E 1 79  ? -19.673 -64.481 7.978  1.00 99.91  ? 79  ARG E CA  1 
ATOM   5022 C  C   . ARG E 1 79  ? -20.754 -65.579 7.866  1.00 98.75  ? 79  ARG E C   1 
ATOM   5023 O  O   . ARG E 1 79  ? -21.128 -66.021 6.763  1.00 101.70 ? 79  ARG E O   1 
ATOM   5024 C  CB  . ARG E 1 79  ? -20.377 -63.147 8.235  1.00 96.41  ? 79  ARG E CB  1 
ATOM   5025 C  CG  . ARG E 1 79  ? -21.402 -62.784 7.145  1.00 97.75  ? 79  ARG E CG  1 
ATOM   5026 C  CD  . ARG E 1 79  ? -22.276 -61.590 7.519  1.00 95.36  ? 79  ARG E CD  1 
ATOM   5027 N  NE  . ARG E 1 79  ? -23.465 -61.966 8.302  1.00 92.33  ? 79  ARG E NE  1 
ATOM   5028 C  CZ  . ARG E 1 79  ? -24.550 -61.191 8.487  1.00 90.17  ? 79  ARG E CZ  1 
ATOM   5029 N  NH1 . ARG E 1 79  ? -24.624 -59.985 7.931  1.00 90.71  ? 79  ARG E NH1 1 
ATOM   5030 N  NH2 . ARG E 1 79  ? -25.583 -61.620 9.228  1.00 87.79  ? 79  ARG E NH2 1 
ATOM   5031 N  N   . HIS E 1 80  ? -21.281 -65.978 9.021  1.00 94.45  ? 80  HIS E N   1 
ATOM   5032 C  CA  . HIS E 1 80  ? -22.452 -66.824 9.064  1.00 92.39  ? 80  HIS E CA  1 
ATOM   5033 C  C   . HIS E 1 80  ? -23.646 -65.946 8.793  1.00 89.23  ? 80  HIS E C   1 
ATOM   5034 O  O   . HIS E 1 80  ? -23.693 -64.811 9.250  1.00 86.66  ? 80  HIS E O   1 
ATOM   5035 C  CB  . HIS E 1 80  ? -22.606 -67.471 10.428 1.00 89.92  ? 80  HIS E CB  1 
ATOM   5036 C  CG  . HIS E 1 80  ? -21.483 -68.388 10.793 1.00 92.98  ? 80  HIS E CG  1 
ATOM   5037 N  ND1 . HIS E 1 80  ? -21.228 -68.776 12.093 1.00 92.52  ? 80  HIS E ND1 1 
ATOM   5038 C  CD2 . HIS E 1 80  ? -20.548 -69.004 10.028 1.00 98.26  ? 80  HIS E CD2 1 
ATOM   5039 C  CE1 . HIS E 1 80  ? -20.190 -69.600 12.113 1.00 96.98  ? 80  HIS E CE1 1 
ATOM   5040 N  NE2 . HIS E 1 80  ? -19.758 -69.756 10.872 1.00 100.44 ? 80  HIS E NE2 1 
ATOM   5041 N  N   . VAL E 1 81  ? -24.615 -66.466 8.053  1.00 89.51  ? 81  VAL E N   1 
ATOM   5042 C  CA  . VAL E 1 81  ? -25.883 -65.746 7.859  1.00 86.82  ? 81  VAL E CA  1 
ATOM   5043 C  C   . VAL E 1 81  ? -26.467 -65.232 9.179  1.00 81.79  ? 81  VAL E C   1 
ATOM   5044 O  O   . VAL E 1 81  ? -27.074 -64.174 9.216  1.00 79.75  ? 81  VAL E O   1 
ATOM   5045 C  CB  . VAL E 1 81  ? -26.935 -66.615 7.119  1.00 88.41  ? 81  VAL E CB  1 
ATOM   5046 C  CG1 . VAL E 1 81  ? -28.257 -65.866 6.964  1.00 85.67  ? 81  VAL E CG1 1 
ATOM   5047 C  CG2 . VAL E 1 81  ? -26.411 -67.020 5.755  1.00 93.88  ? 81  VAL E CG2 1 
ATOM   5048 N  N   . GLY E 1 82  ? -26.265 -65.978 10.259 1.00 80.20  ? 82  GLY E N   1 
ATOM   5049 C  CA  . GLY E 1 82  ? -26.818 -65.623 11.559 1.00 76.83  ? 82  GLY E CA  1 
ATOM   5050 C  C   . GLY E 1 82  ? -26.013 -64.679 12.428 1.00 75.42  ? 82  GLY E C   1 
ATOM   5051 O  O   . GLY E 1 82  ? -26.408 -64.419 13.554 1.00 72.90  ? 82  GLY E O   1 
ATOM   5052 N  N   . ASP E 1 83  ? -24.895 -64.159 11.920 1.00 77.42  ? 83  ASP E N   1 
ATOM   5053 C  CA  . ASP E 1 83  ? -23.969 -63.362 12.746 1.00 76.94  ? 83  ASP E CA  1 
ATOM   5054 C  C   . ASP E 1 83  ? -24.364 -61.916 12.724 1.00 75.57  ? 83  ASP E C   1 
ATOM   5055 O  O   . ASP E 1 83  ? -23.963 -61.207 11.842 1.00 77.56  ? 83  ASP E O   1 
ATOM   5056 C  CB  . ASP E 1 83  ? -22.515 -63.447 12.239 1.00 79.90  ? 83  ASP E CB  1 
ATOM   5057 C  CG  . ASP E 1 83  ? -21.922 -64.851 12.333 1.00 82.45  ? 83  ASP E CG  1 
ATOM   5058 O  OD1 . ASP E 1 83  ? -22.314 -65.645 13.218 1.00 81.45  ? 83  ASP E OD1 1 
ATOM   5059 O  OD2 . ASP E 1 83  ? -21.042 -65.178 11.514 1.00 86.06  ? 83  ASP E OD2 1 
ATOM   5060 N  N   . LEU E 1 84  ? -25.126 -61.462 13.697 1.00 73.25  ? 84  LEU E N   1 
ATOM   5061 C  CA  . LEU E 1 84  ? -25.517 -60.066 13.747 1.00 72.39  ? 84  LEU E CA  1 
ATOM   5062 C  C   . LEU E 1 84  ? -24.577 -59.253 14.636 1.00 72.34  ? 84  LEU E C   1 
ATOM   5063 O  O   . LEU E 1 84  ? -24.900 -58.133 15.045 1.00 71.43  ? 84  LEU E O   1 
ATOM   5064 C  CB  . LEU E 1 84  ? -26.959 -59.980 14.216 1.00 70.70  ? 84  LEU E CB  1 
ATOM   5065 C  CG  . LEU E 1 84  ? -27.933 -60.732 13.305 1.00 70.92  ? 84  LEU E CG  1 
ATOM   5066 C  CD1 . LEU E 1 84  ? -29.336 -60.590 13.804 1.00 68.23  ? 84  LEU E CD1 1 
ATOM   5067 C  CD2 . LEU E 1 84  ? -27.851 -60.252 11.885 1.00 72.76  ? 84  LEU E CD2 1 
ATOM   5068 N  N   . GLY E 1 85  ? -23.405 -59.809 14.932 1.00 73.70  ? 85  GLY E N   1 
ATOM   5069 C  CA  . GLY E 1 85  ? -22.462 -59.140 15.812 1.00 74.13  ? 85  GLY E CA  1 
ATOM   5070 C  C   . GLY E 1 85  ? -22.938 -58.895 17.230 1.00 72.43  ? 85  GLY E C   1 
ATOM   5071 O  O   . GLY E 1 85  ? -23.344 -59.818 17.899 1.00 72.03  ? 85  GLY E O   1 
ATOM   5072 N  N   . ASN E 1 86  ? -22.883 -57.661 17.699 1.00 72.08  ? 86  ASN E N   1 
ATOM   5073 C  CA  . ASN E 1 86  ? -23.137 -57.394 19.100 1.00 71.73  ? 86  ASN E CA  1 
ATOM   5074 C  C   . ASN E 1 86  ? -24.286 -56.455 19.358 1.00 70.75  ? 86  ASN E C   1 
ATOM   5075 O  O   . ASN E 1 86  ? -24.765 -55.776 18.462 1.00 70.80  ? 86  ASN E O   1 
ATOM   5076 C  CB  . ASN E 1 86  ? -21.890 -56.810 19.735 1.00 73.53  ? 86  ASN E CB  1 
ATOM   5077 C  CG  . ASN E 1 86  ? -20.804 -57.821 19.873 1.00 75.62  ? 86  ASN E CG  1 
ATOM   5078 O  OD1 . ASN E 1 86  ? -20.850 -58.683 20.737 1.00 78.08  ? 86  ASN E OD1 1 
ATOM   5079 N  ND2 . ASN E 1 86  ? -19.815 -57.732 19.022 1.00 78.35  ? 86  ASN E ND2 1 
ATOM   5080 N  N   . VAL E 1 87  ? -24.719 -56.440 20.609 1.00 70.48  ? 87  VAL E N   1 
ATOM   5081 C  CA  . VAL E 1 87  ? -25.622 -55.439 21.119 1.00 70.51  ? 87  VAL E CA  1 
ATOM   5082 C  C   . VAL E 1 87  ? -25.041 -54.888 22.429 1.00 72.52  ? 87  VAL E C   1 
ATOM   5083 O  O   . VAL E 1 87  ? -24.245 -55.536 23.105 1.00 73.07  ? 87  VAL E O   1 
ATOM   5084 C  CB  . VAL E 1 87  ? -26.976 -56.023 21.370 1.00 69.41  ? 87  VAL E CB  1 
ATOM   5085 C  CG1 . VAL E 1 87  ? -27.428 -56.756 20.178 1.00 67.21  ? 87  VAL E CG1 1 
ATOM   5086 C  CG2 . VAL E 1 87  ? -26.896 -56.946 22.493 1.00 69.74  ? 87  VAL E CG2 1 
ATOM   5087 N  N   . THR E 1 88  ? -25.456 -53.685 22.788 1.00 74.12  ? 88  THR E N   1 
ATOM   5088 C  CA  . THR E 1 88  ? -24.786 -52.940 23.834 1.00 76.69  ? 88  THR E CA  1 
ATOM   5089 C  C   . THR E 1 88  ? -25.730 -52.650 24.997 1.00 78.33  ? 88  THR E C   1 
ATOM   5090 O  O   . THR E 1 88  ? -26.830 -52.117 24.809 1.00 78.47  ? 88  THR E O   1 
ATOM   5091 C  CB  . THR E 1 88  ? -24.196 -51.613 23.277 1.00 77.89  ? 88  THR E CB  1 
ATOM   5092 O  OG1 . THR E 1 88  ? -23.078 -51.893 22.420 1.00 77.53  ? 88  THR E OG1 1 
ATOM   5093 C  CG2 . THR E 1 88  ? -23.710 -50.697 24.412 1.00 81.19  ? 88  THR E CG2 1 
ATOM   5094 N  N   . ALA E 1 89  ? -25.270 -52.990 26.198 1.00 80.36  ? 89  ALA E N   1 
ATOM   5095 C  CA  . ALA E 1 89  ? -26.047 -52.822 27.411 1.00 82.97  ? 89  ALA E CA  1 
ATOM   5096 C  C   . ALA E 1 89  ? -25.664 -51.536 28.130 1.00 86.57  ? 89  ALA E C   1 
ATOM   5097 O  O   . ALA E 1 89  ? -24.492 -51.230 28.278 1.00 87.62  ? 89  ALA E O   1 
ATOM   5098 C  CB  . ALA E 1 89  ? -25.839 -54.014 28.328 1.00 83.84  ? 89  ALA E CB  1 
ATOM   5099 N  N   . ASP E 1 90  ? -26.682 -50.785 28.527 1.00 89.22  ? 90  ASP E N   1 
ATOM   5100 C  CA  . ASP E 1 90  ? -26.618 -49.724 29.533 1.00 94.07  ? 90  ASP E CA  1 
ATOM   5101 C  C   . ASP E 1 90  ? -25.654 -49.934 30.675 1.00 97.43  ? 90  ASP E C   1 
ATOM   5102 O  O   . ASP E 1 90  ? -25.095 -51.018 30.852 1.00 96.64  ? 90  ASP E O   1 
ATOM   5103 C  CB  . ASP E 1 90  ? -27.984 -49.656 30.233 1.00 96.65  ? 90  ASP E CB  1 
ATOM   5104 C  CG  . ASP E 1 90  ? -28.840 -48.503 29.781 1.00 99.37  ? 90  ASP E CG  1 
ATOM   5105 O  OD1 . ASP E 1 90  ? -28.411 -47.791 28.851 1.00 100.50 ? 90  ASP E OD1 1 
ATOM   5106 O  OD2 . ASP E 1 90  ? -29.946 -48.318 30.368 1.00 103.71 ? 90  ASP E OD2 1 
ATOM   5107 N  N   . LYS E 1 91  ? -25.503 -48.871 31.472 1.00 102.07 ? 91  LYS E N   1 
ATOM   5108 C  CA  . LYS E 1 91  ? -25.156 -48.970 32.905 1.00 107.01 ? 91  LYS E CA  1 
ATOM   5109 C  C   . LYS E 1 91  ? -26.133 -49.938 33.603 1.00 107.66 ? 91  LYS E C   1 
ATOM   5110 O  O   . LYS E 1 91  ? -25.746 -50.876 34.324 1.00 108.83 ? 91  LYS E O   1 
ATOM   5111 C  CB  . LYS E 1 91  ? -25.298 -47.583 33.570 1.00 112.05 ? 91  LYS E CB  1 
ATOM   5112 C  CG  . LYS E 1 91  ? -23.998 -46.764 33.755 1.00 115.99 ? 91  LYS E CG  1 
ATOM   5113 C  CD  . LYS E 1 91  ? -23.248 -47.143 35.068 1.00 122.65 ? 91  LYS E CD  1 
ATOM   5114 C  CE  . LYS E 1 91  ? -22.440 -45.958 35.612 1.00 128.04 ? 91  LYS E CE  1 
ATOM   5115 N  NZ  . LYS E 1 91  ? -21.107 -46.412 36.095 1.00 130.80 ? 91  LYS E NZ  1 
ATOM   5116 N  N   . ASP E 1 92  ? -27.409 -49.646 33.353 1.00 107.18 ? 92  ASP E N   1 
ATOM   5117 C  CA  . ASP E 1 92  ? -28.560 -50.346 33.901 1.00 108.55 ? 92  ASP E CA  1 
ATOM   5118 C  C   . ASP E 1 92  ? -28.812 -51.704 33.318 1.00 104.50 ? 92  ASP E C   1 
ATOM   5119 O  O   . ASP E 1 92  ? -29.830 -52.308 33.635 1.00 105.60 ? 92  ASP E O   1 
ATOM   5120 C  CB  . ASP E 1 92  ? -29.848 -49.549 33.631 1.00 109.60 ? 92  ASP E CB  1 
ATOM   5121 C  CG  . ASP E 1 92  ? -29.776 -48.133 34.104 1.00 115.05 ? 92  ASP E CG  1 
ATOM   5122 O  OD1 . ASP E 1 92  ? -30.867 -47.559 34.297 1.00 119.39 ? 92  ASP E OD1 1 
ATOM   5123 O  OD2 . ASP E 1 92  ? -28.644 -47.590 34.264 1.00 117.95 ? 92  ASP E OD2 1 
ATOM   5124 N  N   . GLY E 1 93  ? -27.943 -52.180 32.440 1.00 100.40 ? 93  GLY E N   1 
ATOM   5125 C  CA  . GLY E 1 93  ? -28.115 -53.512 31.856 1.00 97.10  ? 93  GLY E CA  1 
ATOM   5126 C  C   . GLY E 1 93  ? -29.246 -53.670 30.839 1.00 93.87  ? 93  GLY E C   1 
ATOM   5127 O  O   . GLY E 1 93  ? -29.554 -54.802 30.436 1.00 91.82  ? 93  GLY E O   1 
ATOM   5128 N  N   . VAL E 1 94  ? -29.870 -52.562 30.439 1.00 93.76  ? 94  VAL E N   1 
ATOM   5129 C  CA  . VAL E 1 94  ? -30.789 -52.571 29.305 1.00 91.15  ? 94  VAL E CA  1 
ATOM   5130 C  C   . VAL E 1 94  ? -30.066 -52.318 27.988 1.00 88.18  ? 94  VAL E C   1 
ATOM   5131 O  O   . VAL E 1 94  ? -29.324 -51.345 27.872 1.00 89.31  ? 94  VAL E O   1 
ATOM   5132 C  CB  . VAL E 1 94  ? -31.812 -51.479 29.439 1.00 93.68  ? 94  VAL E CB  1 
ATOM   5133 C  CG1 . VAL E 1 94  ? -32.644 -51.392 28.163 1.00 90.59  ? 94  VAL E CG1 1 
ATOM   5134 C  CG2 . VAL E 1 94  ? -32.649 -51.734 30.681 1.00 97.83  ? 94  VAL E CG2 1 
ATOM   5135 N  N   . ALA E 1 95  ? -30.278 -53.173 26.990 1.00 85.27  ? 95  ALA E N   1 
ATOM   5136 C  CA  . ALA E 1 95  ? -29.688 -52.973 25.655 1.00 83.02  ? 95  ALA E CA  1 
ATOM   5137 C  C   . ALA E 1 95  ? -30.769 -52.603 24.663 1.00 82.68  ? 95  ALA E C   1 
ATOM   5138 O  O   . ALA E 1 95  ? -31.690 -53.378 24.453 1.00 81.84  ? 95  ALA E O   1 
ATOM   5139 C  CB  . ALA E 1 95  ? -28.991 -54.220 25.193 1.00 80.56  ? 95  ALA E CB  1 
ATOM   5140 N  N   . ASP E 1 96  ? -30.665 -51.420 24.062 1.00 83.97  ? 96  ASP E N   1 
ATOM   5141 C  CA  . ASP E 1 96  ? -31.708 -50.943 23.148 1.00 84.86  ? 96  ASP E CA  1 
ATOM   5142 C  C   . ASP E 1 96  ? -31.344 -51.313 21.747 1.00 82.24  ? 96  ASP E C   1 
ATOM   5143 O  O   . ASP E 1 96  ? -30.708 -50.559 21.059 1.00 83.30  ? 96  ASP E O   1 
ATOM   5144 C  CB  . ASP E 1 96  ? -31.914 -49.414 23.237 1.00 88.33  ? 96  ASP E CB  1 
ATOM   5145 C  CG  . ASP E 1 96  ? -32.899 -48.998 24.368 1.00 93.75  ? 96  ASP E CG  1 
ATOM   5146 O  OD1 . ASP E 1 96  ? -33.958 -49.645 24.522 1.00 95.74  ? 96  ASP E OD1 1 
ATOM   5147 O  OD2 . ASP E 1 96  ? -32.630 -48.017 25.106 1.00 99.10  ? 96  ASP E OD2 1 
ATOM   5148 N  N   . VAL E 1 97  ? -31.783 -52.467 21.303 1.00 79.73  ? 97  VAL E N   1 
ATOM   5149 C  CA  . VAL E 1 97  ? -31.330 -52.982 20.042 1.00 77.54  ? 97  VAL E CA  1 
ATOM   5150 C  C   . VAL E 1 97  ? -31.864 -52.183 18.887 1.00 77.98  ? 97  VAL E C   1 
ATOM   5151 O  O   . VAL E 1 97  ? -32.996 -51.753 18.924 1.00 79.42  ? 97  VAL E O   1 
ATOM   5152 C  CB  . VAL E 1 97  ? -31.779 -54.406 19.902 1.00 75.95  ? 97  VAL E CB  1 
ATOM   5153 C  CG1 . VAL E 1 97  ? -31.554 -54.864 18.512 1.00 75.67  ? 97  VAL E CG1 1 
ATOM   5154 C  CG2 . VAL E 1 97  ? -31.027 -55.272 20.861 1.00 75.66  ? 97  VAL E CG2 1 
ATOM   5155 N  N   . SER E 1 98  ? -31.039 -51.990 17.866 1.00 77.30  ? 98  SER E N   1 
ATOM   5156 C  CA  . SER E 1 98  ? -31.504 -51.444 16.600 1.00 78.54  ? 98  SER E CA  1 
ATOM   5157 C  C   . SER E 1 98  ? -30.475 -51.711 15.489 1.00 78.09  ? 98  SER E C   1 
ATOM   5158 O  O   . SER E 1 98  ? -29.347 -51.256 15.579 1.00 78.19  ? 98  SER E O   1 
ATOM   5159 C  CB  . SER E 1 98  ? -31.806 -49.956 16.751 1.00 81.09  ? 98  SER E CB  1 
ATOM   5160 O  OG  . SER E 1 98  ? -32.410 -49.441 15.593 1.00 83.09  ? 98  SER E OG  1 
ATOM   5161 N  N   . ILE E 1 99  ? -30.882 -52.453 14.459 1.00 77.90  ? 99  ILE E N   1 
ATOM   5162 C  CA  . ILE E 1 99  ? -29.977 -52.984 13.464 1.00 78.15  ? 99  ILE E CA  1 
ATOM   5163 C  C   . ILE E 1 99  ? -30.660 -53.112 12.119 1.00 80.91  ? 99  ILE E C   1 
ATOM   5164 O  O   . ILE E 1 99  ? -31.806 -53.535 12.056 1.00 81.31  ? 99  ILE E O   1 
ATOM   5165 C  CB  . ILE E 1 99  ? -29.573 -54.409 13.820 1.00 75.58  ? 99  ILE E CB  1 
ATOM   5166 C  CG1 . ILE E 1 99  ? -28.882 -54.455 15.172 1.00 73.47  ? 99  ILE E CG1 1 
ATOM   5167 C  CG2 . ILE E 1 99  ? -28.669 -54.984 12.769 1.00 76.32  ? 99  ILE E CG2 1 
ATOM   5168 C  CD1 . ILE E 1 99  ? -28.014 -55.688 15.379 1.00 70.93  ? 99  ILE E CD1 1 
ATOM   5169 N  N   . GLU E 1 100 ? -29.963 -52.757 11.041 1.00 83.85  ? 100 GLU E N   1 
ATOM   5170 C  CA  . GLU E 1 100 ? -30.373 -53.161 9.698  1.00 86.66  ? 100 GLU E CA  1 
ATOM   5171 C  C   . GLU E 1 100 ? -29.447 -54.275 9.295  1.00 85.86  ? 100 GLU E C   1 
ATOM   5172 O  O   . GLU E 1 100 ? -28.295 -54.284 9.692  1.00 85.37  ? 100 GLU E O   1 
ATOM   5173 C  CB  . GLU E 1 100 ? -30.262 -52.009 8.691  1.00 91.15  ? 100 GLU E CB  1 
ATOM   5174 C  CG  . GLU E 1 100 ? -31.432 -51.010 8.744  1.00 95.35  ? 100 GLU E CG  1 
ATOM   5175 C  CD  . GLU E 1 100 ? -31.778 -50.412 7.383  1.00 103.64 ? 100 GLU E CD  1 
ATOM   5176 O  OE1 . GLU E 1 100 ? -31.248 -50.918 6.348  1.00 107.32 ? 100 GLU E OE1 1 
ATOM   5177 O  OE2 . GLU E 1 100 ? -32.599 -49.452 7.363  1.00 108.30 ? 100 GLU E OE2 1 
ATOM   5178 N  N   . ASP E 1 101 ? -29.940 -55.216 8.519  1.00 86.44  ? 101 ASP E N   1 
ATOM   5179 C  CA  . ASP E 1 101 ? -29.086 -56.233 7.982  1.00 87.17  ? 101 ASP E CA  1 
ATOM   5180 C  C   . ASP E 1 101 ? -29.768 -56.819 6.779  1.00 89.77  ? 101 ASP E C   1 
ATOM   5181 O  O   . ASP E 1 101 ? -30.993 -56.977 6.787  1.00 89.56  ? 101 ASP E O   1 
ATOM   5182 C  CB  . ASP E 1 101 ? -28.878 -57.318 9.007  1.00 84.15  ? 101 ASP E CB  1 
ATOM   5183 C  CG  . ASP E 1 101 ? -27.813 -58.323 8.595  1.00 86.60  ? 101 ASP E CG  1 
ATOM   5184 O  OD1 . ASP E 1 101 ? -26.635 -58.067 8.908  1.00 88.60  ? 101 ASP E OD1 1 
ATOM   5185 O  OD2 . ASP E 1 101 ? -28.139 -59.381 7.995  1.00 89.37  ? 101 ASP E OD2 1 
ATOM   5186 N  N   . SER E 1 102 ? -28.989 -57.157 5.749  1.00 92.53  ? 102 SER E N   1 
ATOM   5187 C  CA  . SER E 1 102 ? -29.566 -57.706 4.516  1.00 95.94  ? 102 SER E CA  1 
ATOM   5188 C  C   . SER E 1 102 ? -28.965 -59.037 4.086  1.00 96.62  ? 102 SER E C   1 
ATOM   5189 O  O   . SER E 1 102 ? -29.197 -59.492 2.966  1.00 100.49 ? 102 SER E O   1 
ATOM   5190 C  CB  . SER E 1 102 ? -29.418 -56.677 3.421  1.00 100.70 ? 102 SER E CB  1 
ATOM   5191 O  OG  . SER E 1 102 ? -28.329 -55.854 3.780  1.00 101.40 ? 102 SER E OG  1 
ATOM   5192 N  N   . VAL E 1 103 ? -28.211 -59.665 4.978  1.00 93.40  ? 103 VAL E N   1 
ATOM   5193 C  CA  . VAL E 1 103 ? -27.824 -61.053 4.779  1.00 94.03  ? 103 VAL E CA  1 
ATOM   5194 C  C   . VAL E 1 103 ? -28.967 -61.957 5.214  1.00 91.76  ? 103 VAL E C   1 
ATOM   5195 O  O   . VAL E 1 103 ? -29.279 -62.935 4.530  1.00 94.28  ? 103 VAL E O   1 
ATOM   5196 C  CB  . VAL E 1 103 ? -26.562 -61.437 5.559  1.00 92.36  ? 103 VAL E CB  1 
ATOM   5197 C  CG1 . VAL E 1 103 ? -26.470 -62.931 5.669  1.00 92.46  ? 103 VAL E CG1 1 
ATOM   5198 C  CG2 . VAL E 1 103 ? -25.327 -60.903 4.874  1.00 95.78  ? 103 VAL E CG2 1 
ATOM   5199 N  N   . ILE E 1 104 ? -29.574 -61.646 6.359  1.00 87.48  ? 104 ILE E N   1 
ATOM   5200 C  CA  . ILE E 1 104 ? -30.752 -62.390 6.815  1.00 85.64  ? 104 ILE E CA  1 
ATOM   5201 C  C   . ILE E 1 104 ? -31.984 -61.931 6.051  1.00 87.89  ? 104 ILE E C   1 
ATOM   5202 O  O   . ILE E 1 104 ? -31.985 -60.838 5.458  1.00 89.83  ? 104 ILE E O   1 
ATOM   5203 C  CB  . ILE E 1 104 ? -31.012 -62.238 8.329  1.00 81.21  ? 104 ILE E CB  1 
ATOM   5204 C  CG1 . ILE E 1 104 ? -31.371 -60.793 8.667  1.00 80.05  ? 104 ILE E CG1 1 
ATOM   5205 C  CG2 . ILE E 1 104 ? -29.812 -62.700 9.128  1.00 79.29  ? 104 ILE E CG2 1 
ATOM   5206 C  CD1 . ILE E 1 104 ? -31.448 -60.524 10.124 1.00 76.19  ? 104 ILE E CD1 1 
ATOM   5207 N  N   . SER E 1 105 ? -33.025 -62.769 6.094  1.00 88.08  ? 105 SER E N   1 
ATOM   5208 C  CA  . SER E 1 105 ? -34.269 -62.539 5.353  1.00 90.85  ? 105 SER E CA  1 
ATOM   5209 C  C   . SER E 1 105 ? -35.407 -63.172 6.136  1.00 88.86  ? 105 SER E C   1 
ATOM   5210 O  O   . SER E 1 105 ? -35.183 -64.115 6.893  1.00 86.54  ? 105 SER E O   1 
ATOM   5211 C  CB  . SER E 1 105 ? -34.162 -63.167 3.932  1.00 95.81  ? 105 SER E CB  1 
ATOM   5212 O  OG  . SER E 1 105 ? -35.078 -62.596 2.979  1.00 99.30  ? 105 SER E OG  1 
ATOM   5213 N  N   . LEU E 1 106 ? -36.617 -62.667 5.947  1.00 90.38  ? 106 LEU E N   1 
ATOM   5214 C  CA  . LEU E 1 106 ? -37.801 -63.333 6.486  1.00 90.17  ? 106 LEU E CA  1 
ATOM   5215 C  C   . LEU E 1 106 ? -38.467 -64.302 5.483  1.00 94.65  ? 106 LEU E C   1 
ATOM   5216 O  O   . LEU E 1 106 ? -39.365 -65.081 5.849  1.00 94.56  ? 106 LEU E O   1 
ATOM   5217 C  CB  . LEU E 1 106 ? -38.813 -62.299 6.996  1.00 89.46  ? 106 LEU E CB  1 
ATOM   5218 C  CG  . LEU E 1 106 ? -38.300 -61.349 8.079  1.00 85.22  ? 106 LEU E CG  1 
ATOM   5219 C  CD1 . LEU E 1 106 ? -39.448 -60.734 8.864  1.00 83.34  ? 106 LEU E CD1 1 
ATOM   5220 C  CD2 . LEU E 1 106 ? -37.364 -62.077 9.004  1.00 81.07  ? 106 LEU E CD2 1 
ATOM   5221 N  N   . SER E 1 107 ? -38.023 -64.238 4.228  1.00 99.52  ? 107 SER E N   1 
ATOM   5222 C  CA  . SER E 1 107 ? -38.446 -65.159 3.156  1.00 104.34 ? 107 SER E CA  1 
ATOM   5223 C  C   . SER E 1 107 ? -37.189 -65.725 2.496  1.00 107.03 ? 107 SER E C   1 
ATOM   5224 O  O   . SER E 1 107 ? -36.066 -65.409 2.894  1.00 105.38 ? 107 SER E O   1 
ATOM   5225 C  CB  . SER E 1 107 ? -39.327 -64.410 2.123  1.00 108.80 ? 107 SER E CB  1 
ATOM   5226 O  OG  . SER E 1 107 ? -38.703 -63.205 1.657  1.00 110.34 ? 107 SER E OG  1 
ATOM   5227 N  N   . GLY E 1 108 ? -37.358 -66.565 1.488  1.00 112.24 ? 108 GLY E N   1 
ATOM   5228 C  CA  . GLY E 1 108 ? -36.192 -67.103 0.782  1.00 115.67 ? 108 GLY E CA  1 
ATOM   5229 C  C   . GLY E 1 108 ? -35.513 -68.157 1.632  1.00 113.26 ? 108 GLY E C   1 
ATOM   5230 O  O   . GLY E 1 108 ? -36.050 -68.572 2.656  1.00 109.82 ? 108 GLY E O   1 
ATOM   5231 N  N   . ASP E 1 109 ? -34.333 -68.597 1.218  1.00 115.83 ? 109 ASP E N   1 
ATOM   5232 C  CA  . ASP E 1 109 ? -33.645 -69.720 1.929  1.00 114.85 ? 109 ASP E CA  1 
ATOM   5233 C  C   . ASP E 1 109 ? -32.596 -69.208 2.940  1.00 110.28 ? 109 ASP E C   1 
ATOM   5234 O  O   . ASP E 1 109 ? -31.802 -69.977 3.516  1.00 109.21 ? 109 ASP E O   1 
ATOM   5235 C  CB  . ASP E 1 109 ? -33.053 -70.791 0.952  1.00 120.83 ? 109 ASP E CB  1 
ATOM   5236 C  CG  . ASP E 1 109 ? -32.475 -70.182 -0.341 1.00 127.79 ? 109 ASP E CG  1 
ATOM   5237 O  OD1 . ASP E 1 109 ? -33.055 -70.447 -1.426 1.00 133.83 ? 109 ASP E OD1 1 
ATOM   5238 O  OD2 . ASP E 1 109 ? -31.462 -69.429 -0.274 1.00 129.34 ? 109 ASP E OD2 1 
ATOM   5239 N  N   . HIS E 1 110 ? -32.592 -67.889 3.126  1.00 107.71 ? 110 HIS E N   1 
ATOM   5240 C  CA  . HIS E 1 110 ? -31.967 -67.287 4.310  1.00 103.01 ? 110 HIS E CA  1 
ATOM   5241 C  C   . HIS E 1 110 ? -33.068 -66.964 5.361  1.00 97.63  ? 110 HIS E C   1 
ATOM   5242 O  O   . HIS E 1 110 ? -32.816 -66.225 6.340  1.00 94.01  ? 110 HIS E O   1 
ATOM   5243 C  CB  . HIS E 1 110 ? -31.181 -66.010 3.925  1.00 104.11 ? 110 HIS E CB  1 
ATOM   5244 C  CG  . HIS E 1 110 ? -29.950 -66.269 3.097  1.00 110.45 ? 110 HIS E CG  1 
ATOM   5245 N  ND1 . HIS E 1 110 ? -28.961 -65.318 2.916  1.00 113.10 ? 110 HIS E ND1 1 
ATOM   5246 C  CD2 . HIS E 1 110 ? -29.530 -67.378 2.432  1.00 116.25 ? 110 HIS E CD2 1 
ATOM   5247 C  CE1 . HIS E 1 110 ? -27.998 -65.821 2.157  1.00 118.13 ? 110 HIS E CE1 1 
ATOM   5248 N  NE2 . HIS E 1 110 ? -28.314 -67.071 1.855  1.00 120.58 ? 110 HIS E NE2 1 
ATOM   5249 N  N   . CYS E 1 111 ? -34.280 -67.510 5.144  1.00 96.86  ? 111 CYS E N   1 
ATOM   5250 C  CA  . CYS E 1 111 ? -35.431 -67.267 6.026  1.00 92.30  ? 111 CYS E CA  1 
ATOM   5251 C  C   . CYS E 1 111 ? -35.042 -67.737 7.421  1.00 87.84  ? 111 CYS E C   1 
ATOM   5252 O  O   . CYS E 1 111 ? -34.596 -68.874 7.587  1.00 88.40  ? 111 CYS E O   1 
ATOM   5253 C  CB  . CYS E 1 111 ? -36.663 -68.008 5.503  1.00 94.41  ? 111 CYS E CB  1 
ATOM   5254 S  SG  . CYS E 1 111 ? -38.093 -67.956 6.523  1.00 90.06  ? 111 CYS E SG  1 
ATOM   5255 N  N   . ILE E 1 112 ? -35.151 -66.846 8.404  1.00 83.41  ? 112 ILE E N   1 
ATOM   5256 C  CA  . ILE E 1 112 ? -34.749 -67.150 9.786  1.00 79.55  ? 112 ILE E CA  1 
ATOM   5257 C  C   . ILE E 1 112 ? -35.947 -67.417 10.687 1.00 77.88  ? 112 ILE E C   1 
ATOM   5258 O  O   . ILE E 1 112 ? -35.815 -67.588 11.900 1.00 75.92  ? 112 ILE E O   1 
ATOM   5259 C  CB  . ILE E 1 112 ? -33.926 -66.013 10.411 1.00 77.16  ? 112 ILE E CB  1 
ATOM   5260 C  CG1 . ILE E 1 112 ? -34.763 -64.755 10.599 1.00 75.05  ? 112 ILE E CG1 1 
ATOM   5261 C  CG2 . ILE E 1 112 ? -32.746 -65.702 9.549  1.00 79.04  ? 112 ILE E CG2 1 
ATOM   5262 C  CD1 . ILE E 1 112 ? -34.048 -63.720 11.371 1.00 70.99  ? 112 ILE E CD1 1 
ATOM   5263 N  N   . ILE E 1 113 ? -37.125 -67.446 10.093 1.00 78.87  ? 113 ILE E N   1 
ATOM   5264 C  CA  . ILE E 1 113 ? -38.308 -67.722 10.851 1.00 77.83  ? 113 ILE E CA  1 
ATOM   5265 C  C   . ILE E 1 113 ? -38.280 -69.156 11.297 1.00 77.81  ? 113 ILE E C   1 
ATOM   5266 O  O   . ILE E 1 113 ? -38.129 -70.048 10.492 1.00 79.86  ? 113 ILE E O   1 
ATOM   5267 C  CB  . ILE E 1 113 ? -39.528 -67.467 10.030 1.00 79.98  ? 113 ILE E CB  1 
ATOM   5268 C  CG1 . ILE E 1 113 ? -39.799 -65.978 10.000 1.00 79.75  ? 113 ILE E CG1 1 
ATOM   5269 C  CG2 . ILE E 1 113 ? -40.689 -68.127 10.635 1.00 80.36  ? 113 ILE E CG2 1 
ATOM   5270 C  CD1 . ILE E 1 113 ? -40.882 -65.604 9.054  1.00 84.15  ? 113 ILE E CD1 1 
ATOM   5271 N  N   . GLY E 1 114 ? -38.411 -69.370 12.593 1.00 75.94  ? 114 GLY E N   1 
ATOM   5272 C  CA  . GLY E 1 114 ? -38.383 -70.702 13.147 1.00 76.70  ? 114 GLY E CA  1 
ATOM   5273 C  C   . GLY E 1 114 ? -37.031 -71.083 13.700 1.00 75.99  ? 114 GLY E C   1 
ATOM   5274 O  O   . GLY E 1 114 ? -36.775 -72.243 14.036 1.00 77.23  ? 114 GLY E O   1 
ATOM   5275 N  N   . ARG E 1 115 ? -36.144 -70.116 13.780 1.00 74.38  ? 115 ARG E N   1 
ATOM   5276 C  CA  . ARG E 1 115 ? -34.818 -70.397 14.255 1.00 74.31  ? 115 ARG E CA  1 
ATOM   5277 C  C   . ARG E 1 115 ? -34.620 -69.605 15.499 1.00 72.30  ? 115 ARG E C   1 
ATOM   5278 O  O   . ARG E 1 115 ? -35.336 -68.648 15.707 1.00 71.33  ? 115 ARG E O   1 
ATOM   5279 C  CB  . ARG E 1 115 ? -33.809 -70.026 13.196 1.00 75.08  ? 115 ARG E CB  1 
ATOM   5280 C  CG  . ARG E 1 115 ? -34.105 -70.700 11.864 1.00 77.98  ? 115 ARG E CG  1 
ATOM   5281 C  CD  . ARG E 1 115 ? -32.970 -70.525 10.882 1.00 80.31  ? 115 ARG E CD  1 
ATOM   5282 N  NE  . ARG E 1 115 ? -33.245 -71.175 9.607  1.00 83.67  ? 115 ARG E NE  1 
ATOM   5283 C  CZ  . ARG E 1 115 ? -33.007 -72.456 9.344  1.00 87.26  ? 115 ARG E CZ  1 
ATOM   5284 N  NH1 . ARG E 1 115 ? -32.489 -73.267 10.257 1.00 88.40  ? 115 ARG E NH1 1 
ATOM   5285 N  NH2 . ARG E 1 115 ? -33.301 -72.934 8.153  1.00 90.84  ? 115 ARG E NH2 1 
ATOM   5286 N  N   . THR E 1 116 ? -33.689 -70.031 16.347 1.00 72.43  ? 116 THR E N   1 
ATOM   5287 C  CA  . THR E 1 116 ? -33.542 -69.415 17.650 1.00 71.56  ? 116 THR E CA  1 
ATOM   5288 C  C   . THR E 1 116 ? -32.657 -68.214 17.531 1.00 69.72  ? 116 THR E C   1 
ATOM   5289 O  O   . THR E 1 116 ? -31.673 -68.247 16.842 1.00 70.16  ? 116 THR E O   1 
ATOM   5290 C  CB  . THR E 1 116 ? -32.956 -70.367 18.717 1.00 73.29  ? 116 THR E CB  1 
ATOM   5291 O  OG1 . THR E 1 116 ? -33.798 -71.520 18.874 1.00 76.45  ? 116 THR E OG1 1 
ATOM   5292 C  CG2 . THR E 1 116 ? -32.888 -69.663 20.071 1.00 73.82  ? 116 THR E CG2 1 
ATOM   5293 N  N   . LEU E 1 117 ? -33.060 -67.140 18.182 1.00 68.33  ? 117 LEU E N   1 
ATOM   5294 C  CA  . LEU E 1 117 ? -32.246 -65.973 18.360 1.00 67.28  ? 117 LEU E CA  1 
ATOM   5295 C  C   . LEU E 1 117 ? -31.615 -66.116 19.711 1.00 68.07  ? 117 LEU E C   1 
ATOM   5296 O  O   . LEU E 1 117 ? -32.260 -66.578 20.623 1.00 69.34  ? 117 LEU E O   1 
ATOM   5297 C  CB  . LEU E 1 117 ? -33.136 -64.752 18.371 1.00 66.32  ? 117 LEU E CB  1 
ATOM   5298 C  CG  . LEU E 1 117 ? -32.430 -63.429 18.571 1.00 64.73  ? 117 LEU E CG  1 
ATOM   5299 C  CD1 . LEU E 1 117 ? -31.509 -63.238 17.439 1.00 64.73  ? 117 LEU E CD1 1 
ATOM   5300 C  CD2 . LEU E 1 117 ? -33.408 -62.302 18.623 1.00 63.30  ? 117 LEU E CD2 1 
ATOM   5301 N  N   . VAL E 1 118 ? -30.369 -65.710 19.862 1.00 68.31  ? 118 VAL E N   1 
ATOM   5302 C  CA  . VAL E 1 118 ? -29.670 -65.917 21.113 1.00 69.61  ? 118 VAL E CA  1 
ATOM   5303 C  C   . VAL E 1 118 ? -28.857 -64.724 21.481 1.00 69.34  ? 118 VAL E C   1 
ATOM   5304 O  O   . VAL E 1 118 ? -28.196 -64.177 20.646 1.00 69.02  ? 118 VAL E O   1 
ATOM   5305 C  CB  . VAL E 1 118 ? -28.695 -67.067 20.984 1.00 71.25  ? 118 VAL E CB  1 
ATOM   5306 C  CG1 . VAL E 1 118 ? -28.001 -67.289 22.283 1.00 73.33  ? 118 VAL E CG1 1 
ATOM   5307 C  CG2 . VAL E 1 118 ? -29.410 -68.296 20.585 1.00 72.65  ? 118 VAL E CG2 1 
ATOM   5308 N  N   . VAL E 1 119 ? -28.881 -64.323 22.733 1.00 70.34  ? 119 VAL E N   1 
ATOM   5309 C  CA  . VAL E 1 119 ? -27.982 -63.278 23.204 1.00 70.94  ? 119 VAL E CA  1 
ATOM   5310 C  C   . VAL E 1 119 ? -27.005 -63.946 24.151 1.00 74.00  ? 119 VAL E C   1 
ATOM   5311 O  O   . VAL E 1 119 ? -27.373 -64.877 24.833 1.00 75.90  ? 119 VAL E O   1 
ATOM   5312 C  CB  . VAL E 1 119 ? -28.735 -62.150 23.900 1.00 70.66  ? 119 VAL E CB  1 
ATOM   5313 C  CG1 . VAL E 1 119 ? -29.560 -62.669 25.031 1.00 72.43  ? 119 VAL E CG1 1 
ATOM   5314 C  CG2 . VAL E 1 119 ? -27.771 -61.108 24.411 1.00 71.08  ? 119 VAL E CG2 1 
ATOM   5315 N  N   . HIS E 1 120 ? -25.764 -63.485 24.193 1.00 75.51  ? 120 HIS E N   1 
ATOM   5316 C  CA  . HIS E 1 120 ? -24.683 -64.236 24.828 1.00 78.82  ? 120 HIS E CA  1 
ATOM   5317 C  C   . HIS E 1 120 ? -24.035 -63.539 26.014 1.00 81.37  ? 120 HIS E C   1 
ATOM   5318 O  O   . HIS E 1 120 ? -24.197 -62.336 26.228 1.00 80.41  ? 120 HIS E O   1 
ATOM   5319 C  CB  . HIS E 1 120 ? -23.582 -64.505 23.821 1.00 79.14  ? 120 HIS E CB  1 
ATOM   5320 C  CG  . HIS E 1 120 ? -23.900 -65.575 22.840 1.00 80.09  ? 120 HIS E CG  1 
ATOM   5321 N  ND1 . HIS E 1 120 ? -23.311 -66.817 22.891 1.00 85.00  ? 120 HIS E ND1 1 
ATOM   5322 C  CD2 . HIS E 1 120 ? -24.699 -65.576 21.747 1.00 79.33  ? 120 HIS E CD2 1 
ATOM   5323 C  CE1 . HIS E 1 120 ? -23.749 -67.545 21.882 1.00 85.74  ? 120 HIS E CE1 1 
ATOM   5324 N  NE2 . HIS E 1 120 ? -24.593 -66.815 21.172 1.00 81.97  ? 120 HIS E NE2 1 
ATOM   5325 N  N   . GLU E 1 121 ? -23.243 -64.327 26.740 1.00 85.26  ? 121 GLU E N   1 
ATOM   5326 C  CA  . GLU E 1 121 ? -22.560 -63.904 27.956 1.00 88.72  ? 121 GLU E CA  1 
ATOM   5327 C  C   . GLU E 1 121 ? -21.617 -62.739 27.729 1.00 88.13  ? 121 GLU E C   1 
ATOM   5328 O  O   . GLU E 1 121 ? -21.721 -61.752 28.438 1.00 88.51  ? 121 GLU E O   1 
ATOM   5329 C  CB  . GLU E 1 121 ? -21.778 -65.083 28.541 1.00 92.98  ? 121 GLU E CB  1 
ATOM   5330 C  CG  . GLU E 1 121 ? -21.223 -64.828 29.956 1.00 99.17  ? 121 GLU E CG  1 
ATOM   5331 C  CD  . GLU E 1 121 ? -20.351 -65.991 30.510 1.00 106.43 ? 121 GLU E CD  1 
ATOM   5332 O  OE1 . GLU E 1 121 ? -19.871 -66.864 29.721 1.00 107.43 ? 121 GLU E OE1 1 
ATOM   5333 O  OE2 . GLU E 1 121 ? -20.156 -66.013 31.756 1.00 112.06 ? 121 GLU E OE2 1 
ATOM   5334 N  N   . LYS E 1 122 ? -20.703 -62.868 26.759 1.00 87.83  ? 122 LYS E N   1 
ATOM   5335 C  CA  . LYS E 1 122 ? -19.676 -61.840 26.484 1.00 88.54  ? 122 LYS E CA  1 
ATOM   5336 C  C   . LYS E 1 122 ? -19.823 -61.222 25.098 1.00 85.26  ? 122 LYS E C   1 
ATOM   5337 O  O   . LYS E 1 122 ? -20.773 -61.513 24.376 1.00 83.31  ? 122 LYS E O   1 
ATOM   5338 C  CB  . LYS E 1 122 ? -18.257 -62.428 26.547 1.00 92.19  ? 122 LYS E CB  1 
ATOM   5339 C  CG  . LYS E 1 122 ? -18.017 -63.525 27.560 1.00 97.86  ? 122 LYS E CG  1 
ATOM   5340 C  CD  . LYS E 1 122 ? -16.566 -64.030 27.490 1.00 103.54 ? 122 LYS E CD  1 
ATOM   5341 C  CE  . LYS E 1 122 ? -16.506 -65.546 27.729 1.00 107.78 ? 122 LYS E CE  1 
ATOM   5342 N  NZ  . LYS E 1 122 ? -15.107 -66.094 27.766 1.00 112.97 ? 122 LYS E NZ  1 
ATOM   5343 N  N   . ALA E 1 123 ? -18.846 -60.395 24.722 1.00 85.23  ? 123 ALA E N   1 
ATOM   5344 C  CA  . ALA E 1 123 ? -18.774 -59.822 23.389 1.00 82.86  ? 123 ALA E CA  1 
ATOM   5345 C  C   . ALA E 1 123 ? -18.390 -60.846 22.305 1.00 82.80  ? 123 ALA E C   1 
ATOM   5346 O  O   . ALA E 1 123 ? -17.535 -61.700 22.514 1.00 84.80  ? 123 ALA E O   1 
ATOM   5347 C  CB  . ALA E 1 123 ? -17.790 -58.703 23.395 1.00 84.19  ? 123 ALA E CB  1 
ATOM   5348 N  N   . ASP E 1 124 ? -19.066 -60.750 21.159 1.00 80.59  ? 124 ASP E N   1 
ATOM   5349 C  CA  . ASP E 1 124 ? -18.698 -61.455 19.935 1.00 81.24  ? 124 ASP E CA  1 
ATOM   5350 C  C   . ASP E 1 124 ? -17.465 -60.745 19.502 1.00 82.65  ? 124 ASP E C   1 
ATOM   5351 O  O   . ASP E 1 124 ? -17.469 -59.543 19.470 1.00 81.65  ? 124 ASP E O   1 
ATOM   5352 C  CB  . ASP E 1 124 ? -19.797 -61.323 18.864 1.00 79.23  ? 124 ASP E CB  1 
ATOM   5353 C  CG  . ASP E 1 124 ? -19.484 -62.105 17.550 1.00 81.74  ? 124 ASP E CG  1 
ATOM   5354 O  OD1 . ASP E 1 124 ? -18.367 -62.651 17.451 1.00 85.46  ? 124 ASP E OD1 1 
ATOM   5355 O  OD2 . ASP E 1 124 ? -20.345 -62.170 16.601 1.00 81.07  ? 124 ASP E OD2 1 
ATOM   5356 N  N   . ASP E 1 125 ? -16.398 -61.476 19.196 1.00 85.37  ? 125 ASP E N   1 
ATOM   5357 C  CA  . ASP E 1 125 ? -15.122 -60.854 18.795 1.00 87.59  ? 125 ASP E CA  1 
ATOM   5358 C  C   . ASP E 1 125 ? -14.988 -60.794 17.279 1.00 88.06  ? 125 ASP E C   1 
ATOM   5359 O  O   . ASP E 1 125 ? -13.919 -60.543 16.757 1.00 90.39  ? 125 ASP E O   1 
ATOM   5360 C  CB  . ASP E 1 125 ? -13.919 -61.576 19.426 1.00 91.36  ? 125 ASP E CB  1 
ATOM   5361 C  CG  . ASP E 1 125 ? -13.625 -62.941 18.782 1.00 94.21  ? 125 ASP E CG  1 
ATOM   5362 O  OD1 . ASP E 1 125 ? -14.111 -63.195 17.641 1.00 93.84  ? 125 ASP E OD1 1 
ATOM   5363 O  OD2 . ASP E 1 125 ? -12.888 -63.751 19.420 1.00 97.06  ? 125 ASP E OD2 1 
ATOM   5364 N  N   . LEU E 1 126 ? -16.092 -61.063 16.590 1.00 86.26  ? 126 LEU E N   1 
ATOM   5365 C  CA  . LEU E 1 126 ? -16.230 -60.852 15.143 1.00 87.27  ? 126 LEU E CA  1 
ATOM   5366 C  C   . LEU E 1 126 ? -15.232 -61.662 14.336 1.00 91.73  ? 126 LEU E C   1 
ATOM   5367 O  O   . LEU E 1 126 ? -14.898 -61.293 13.199 1.00 93.76  ? 126 LEU E O   1 
ATOM   5368 C  CB  . LEU E 1 126 ? -16.134 -59.361 14.769 1.00 86.79  ? 126 LEU E CB  1 
ATOM   5369 C  CG  . LEU E 1 126 ? -16.972 -58.401 15.609 1.00 83.09  ? 126 LEU E CG  1 
ATOM   5370 C  CD1 . LEU E 1 126 ? -17.169 -57.060 14.907 1.00 82.61  ? 126 LEU E CD1 1 
ATOM   5371 C  CD2 . LEU E 1 126 ? -18.303 -59.047 15.899 1.00 79.20  ? 126 LEU E CD2 1 
ATOM   5372 N  N   . GLY E 1 127 ? -14.781 -62.771 14.918 1.00 93.95  ? 127 GLY E N   1 
ATOM   5373 C  CA  . GLY E 1 127 ? -13.889 -63.699 14.234 1.00 99.10  ? 127 GLY E CA  1 
ATOM   5374 C  C   . GLY E 1 127 ? -12.405 -63.359 14.346 1.00 103.67 ? 127 GLY E C   1 
ATOM   5375 O  O   . GLY E 1 127 ? -11.551 -64.118 13.858 1.00 107.98 ? 127 GLY E O   1 
ATOM   5376 N  N   . LYS E 1 128 ? -12.093 -62.239 15.009 1.00 103.33 ? 128 LYS E N   1 
ATOM   5377 C  CA  . LYS E 1 128 ? -10.722 -61.707 15.045 1.00 107.78 ? 128 LYS E CA  1 
ATOM   5378 C  C   . LYS E 1 128 ? -9.996  -62.016 16.379 1.00 108.97 ? 128 LYS E C   1 
ATOM   5379 O  O   . LYS E 1 128 ? -9.060  -61.308 16.762 1.00 111.04 ? 128 LYS E O   1 
ATOM   5380 C  CB  . LYS E 1 128 ? -10.709 -60.178 14.784 1.00 107.00 ? 128 LYS E CB  1 
ATOM   5381 C  CG  . LYS E 1 128 ? -11.795 -59.670 13.833 1.00 107.34 ? 128 LYS E CG  1 
ATOM   5382 C  CD  . LYS E 1 128 ? -11.467 -58.299 13.189 1.00 111.74 ? 128 LYS E CD  1 
ATOM   5383 C  CE  . LYS E 1 128 ? -12.711 -57.711 12.439 1.00 111.15 ? 128 LYS E CE  1 
ATOM   5384 N  NZ  . LYS E 1 128 ? -13.088 -58.441 11.164 1.00 113.85 ? 128 LYS E NZ  1 
ATOM   5385 N  N   . GLY E 1 129 ? -10.405 -63.072 17.076 1.00 108.56 ? 129 GLY E N   1 
ATOM   5386 C  CA  . GLY E 1 129 ? -9.797  -63.429 18.373 1.00 110.58 ? 129 GLY E CA  1 
ATOM   5387 C  C   . GLY E 1 129 ? -8.583  -64.326 18.225 1.00 116.66 ? 129 GLY E C   1 
ATOM   5388 O  O   . GLY E 1 129 ? -7.859  -64.612 19.228 1.00 119.11 ? 129 GLY E O   1 
ATOM   5389 N  N   . GLY E 1 130 ? -8.399  -64.798 16.973 1.00 119.15 ? 130 GLY E N   1 
ATOM   5390 C  CA  . GLY E 1 130 ? -7.255  -65.630 16.590 1.00 125.77 ? 130 GLY E CA  1 
ATOM   5391 C  C   . GLY E 1 130 ? -7.145  -66.941 17.377 1.00 128.69 ? 130 GLY E C   1 
ATOM   5392 O  O   . GLY E 1 130 ? -6.050  -67.514 17.563 1.00 134.43 ? 130 GLY E O   1 
ATOM   5393 N  N   . ASN E 1 131 ? -8.271  -67.417 17.877 1.00 125.44 ? 131 ASN E N   1 
ATOM   5394 C  CA  . ASN E 1 131 ? -8.288  -68.738 18.450 1.00 128.69 ? 131 ASN E CA  1 
ATOM   5395 C  C   . ASN E 1 131 ? -9.330  -69.561 17.690 1.00 127.58 ? 131 ASN E C   1 
ATOM   5396 O  O   . ASN E 1 131 ? -10.101 -69.012 16.862 1.00 123.50 ? 131 ASN E O   1 
ATOM   5397 C  CB  . ASN E 1 131 ? -8.466  -68.679 19.977 1.00 127.71 ? 131 ASN E CB  1 
ATOM   5398 C  CG  . ASN E 1 131 ? -9.909  -68.697 20.415 1.00 121.94 ? 131 ASN E CG  1 
ATOM   5399 O  OD1 . ASN E 1 131 ? -10.753 -68.053 19.814 1.00 117.04 ? 131 ASN E OD1 1 
ATOM   5400 N  ND2 . ASN E 1 131 ? -10.194 -69.427 21.474 1.00 122.68 ? 131 ASN E ND2 1 
ATOM   5401 N  N   . GLU E 1 132 ? -9.284  -70.877 17.897 1.00 132.05 ? 132 GLU E N   1 
ATOM   5402 C  CA  . GLU E 1 132 ? -10.088 -71.818 17.090 1.00 132.96 ? 132 GLU E CA  1 
ATOM   5403 C  C   . GLU E 1 132 ? -11.552 -71.413 17.211 1.00 125.98 ? 132 GLU E C   1 
ATOM   5404 O  O   . GLU E 1 132 ? -12.278 -71.241 16.189 1.00 123.06 ? 132 GLU E O   1 
ATOM   5405 C  CB  . GLU E 1 132 ? -9.837  -73.286 17.553 1.00 138.85 ? 132 GLU E CB  1 
ATOM   5406 C  CG  . GLU E 1 132 ? -11.038 -74.311 17.405 1.00 140.27 ? 132 GLU E CG  1 
ATOM   5407 C  CD  . GLU E 1 132 ? -11.026 -75.168 16.116 1.00 146.97 ? 132 GLU E CD  1 
ATOM   5408 O  OE1 . GLU E 1 132 ? -9.928  -75.424 15.545 1.00 154.33 ? 132 GLU E OE1 1 
ATOM   5409 O  OE2 . GLU E 1 132 ? -12.133 -75.593 15.681 1.00 145.60 ? 132 GLU E OE2 1 
ATOM   5410 N  N   . GLU E 1 133 ? -11.933 -71.233 18.481 1.00 123.47 ? 133 GLU E N   1 
ATOM   5411 C  CA  . GLU E 1 133 ? -13.299 -70.916 18.877 1.00 118.02 ? 133 GLU E CA  1 
ATOM   5412 C  C   . GLU E 1 133 ? -13.849 -69.596 18.307 1.00 112.34 ? 133 GLU E C   1 
ATOM   5413 O  O   . GLU E 1 133 ? -15.059 -69.447 18.109 1.00 108.22 ? 133 GLU E O   1 
ATOM   5414 C  CB  . GLU E 1 133 ? -13.382 -70.903 20.408 1.00 118.29 ? 133 GLU E CB  1 
ATOM   5415 C  CG  . GLU E 1 133 ? -14.827 -70.796 20.976 1.00 115.56 ? 133 GLU E CG  1 
ATOM   5416 C  CD  . GLU E 1 133 ? -15.748 -71.972 20.547 1.00 118.66 ? 133 GLU E CD  1 
ATOM   5417 O  OE1 . GLU E 1 133 ? -15.241 -73.127 20.417 1.00 124.95 ? 133 GLU E OE1 1 
ATOM   5418 O  OE2 . GLU E 1 133 ? -16.972 -71.737 20.332 1.00 115.75 ? 133 GLU E OE2 1 
ATOM   5419 N  N   . SER E 1 134 ? -12.964 -68.650 18.028 1.00 112.49 ? 134 SER E N   1 
ATOM   5420 C  CA  . SER E 1 134 ? -13.398 -67.374 17.480 1.00 108.17 ? 134 SER E CA  1 
ATOM   5421 C  C   . SER E 1 134 ? -13.988 -67.491 16.069 1.00 107.33 ? 134 SER E C   1 
ATOM   5422 O  O   . SER E 1 134 ? -14.894 -66.747 15.736 1.00 103.96 ? 134 SER E O   1 
ATOM   5423 C  CB  . SER E 1 134 ? -12.265 -66.357 17.462 1.00 109.61 ? 134 SER E CB  1 
ATOM   5424 O  OG  . SER E 1 134 ? -12.712 -65.152 16.876 1.00 105.53 ? 134 SER E OG  1 
ATOM   5425 N  N   . THR E 1 135 ? -13.518 -68.418 15.248 1.00 110.96 ? 135 THR E N   1 
ATOM   5426 C  CA  . THR E 1 135 ? -14.118 -68.579 13.921 1.00 110.82 ? 135 THR E CA  1 
ATOM   5427 C  C   . THR E 1 135 ? -15.403 -69.433 13.919 1.00 108.76 ? 135 THR E C   1 
ATOM   5428 O  O   . THR E 1 135 ? -15.901 -69.807 12.848 1.00 109.44 ? 135 THR E O   1 
ATOM   5429 C  CB  . THR E 1 135 ? -13.114 -69.203 12.995 1.00 116.81 ? 135 THR E CB  1 
ATOM   5430 O  OG1 . THR E 1 135 ? -12.438 -70.238 13.729 1.00 120.47 ? 135 THR E OG1 1 
ATOM   5431 C  CG2 . THR E 1 135 ? -12.117 -68.131 12.509 1.00 117.82 ? 135 THR E CG2 1 
ATOM   5432 N  N   . LYS E 1 136 ? -15.951 -69.702 15.108 1.00 106.53 ? 136 LYS E N   1 
ATOM   5433 C  CA  . LYS E 1 136 ? -17.179 -70.497 15.261 1.00 105.11 ? 136 LYS E CA  1 
ATOM   5434 C  C   . LYS E 1 136 ? -18.281 -69.766 16.042 1.00 99.66  ? 136 LYS E C   1 
ATOM   5435 O  O   . LYS E 1 136 ? -19.410 -69.590 15.529 1.00 96.84  ? 136 LYS E O   1 
ATOM   5436 C  CB  . LYS E 1 136 ? -16.847 -71.810 15.958 1.00 108.91 ? 136 LYS E CB  1 
ATOM   5437 C  CG  . LYS E 1 136 ? -15.664 -72.528 15.312 1.00 116.99 ? 136 LYS E CG  1 
ATOM   5438 C  CD  . LYS E 1 136 ? -15.218 -73.766 16.136 1.00 124.04 ? 136 LYS E CD  1 
ATOM   5439 C  CE  . LYS E 1 136 ? -16.283 -74.904 16.157 1.00 125.10 ? 136 LYS E CE  1 
ATOM   5440 N  NZ  . LYS E 1 136 ? -15.751 -76.188 16.696 1.00 131.05 ? 136 LYS E NZ  1 
ATOM   5441 N  N   . THR E 1 137 ? -17.962 -69.364 17.276 1.00 98.46  ? 137 THR E N   1 
ATOM   5442 C  CA  . THR E 1 137 ? -18.901 -68.600 18.091 1.00 94.30  ? 137 THR E CA  1 
ATOM   5443 C  C   . THR E 1 137 ? -18.443 -67.177 18.323 1.00 91.97  ? 137 THR E C   1 
ATOM   5444 O  O   . THR E 1 137 ? -19.130 -66.439 18.996 1.00 89.50  ? 137 THR E O   1 
ATOM   5445 C  CB  . THR E 1 137 ? -19.158 -69.247 19.499 1.00 95.25  ? 137 THR E CB  1 
ATOM   5446 O  OG1 . THR E 1 137 ? -17.933 -69.276 20.263 1.00 98.91  ? 137 THR E OG1 1 
ATOM   5447 C  CG2 . THR E 1 137 ? -19.794 -70.668 19.371 1.00 97.25  ? 137 THR E CG2 1 
ATOM   5448 N  N   . GLY E 1 138 ? -17.290 -66.786 17.808 1.00 93.25  ? 138 GLY E N   1 
ATOM   5449 C  CA  . GLY E 1 138 ? -16.752 -65.486 18.159 1.00 91.96  ? 138 GLY E CA  1 
ATOM   5450 C  C   . GLY E 1 138 ? -16.429 -65.339 19.640 1.00 92.17  ? 138 GLY E C   1 
ATOM   5451 O  O   . GLY E 1 138 ? -16.363 -64.220 20.155 1.00 90.58  ? 138 GLY E O   1 
ATOM   5452 N  N   . ASN E 1 139 ? -16.220 -66.458 20.336 1.00 94.64  ? 139 ASN E N   1 
ATOM   5453 C  CA  . ASN E 1 139 ? -15.904 -66.452 21.782 1.00 96.14  ? 139 ASN E CA  1 
ATOM   5454 C  C   . ASN E 1 139 ? -16.944 -65.757 22.632 1.00 93.28  ? 139 ASN E C   1 
ATOM   5455 O  O   . ASN E 1 139 ? -16.624 -65.252 23.713 1.00 94.12  ? 139 ASN E O   1 
ATOM   5456 C  CB  . ASN E 1 139 ? -14.538 -65.799 22.048 1.00 98.73  ? 139 ASN E CB  1 
ATOM   5457 C  CG  . ASN E 1 139 ? -13.377 -66.761 21.838 1.00 103.57 ? 139 ASN E CG  1 
ATOM   5458 O  OD1 . ASN E 1 139 ? -13.565 -67.985 21.761 1.00 104.17 ? 139 ASN E OD1 1 
ATOM   5459 N  ND2 . ASN E 1 139 ? -12.159 -66.207 21.749 1.00 106.50 ? 139 ASN E ND2 1 
ATOM   5460 N  N   . ALA E 1 140 ? -18.190 -65.773 22.152 1.00 90.55  ? 140 ALA E N   1 
ATOM   5461 C  CA  . ALA E 1 140 ? -19.260 -64.929 22.697 1.00 87.84  ? 140 ALA E CA  1 
ATOM   5462 C  C   . ALA E 1 140 ? -19.693 -65.428 24.042 1.00 89.55  ? 140 ALA E C   1 
ATOM   5463 O  O   . ALA E 1 140 ? -20.295 -64.685 24.828 1.00 88.28  ? 140 ALA E O   1 
ATOM   5464 C  CB  . ALA E 1 140 ? -20.424 -64.933 21.788 1.00 85.00  ? 140 ALA E CB  1 
ATOM   5465 N  N   . GLY E 1 141 ? -19.399 -66.710 24.279 1.00 92.88  ? 141 GLY E N   1 
ATOM   5466 C  CA  . GLY E 1 141 ? -19.622 -67.338 25.563 1.00 95.51  ? 141 GLY E CA  1 
ATOM   5467 C  C   . GLY E 1 141 ? -20.948 -68.064 25.594 1.00 94.45  ? 141 GLY E C   1 
ATOM   5468 O  O   . GLY E 1 141 ? -21.565 -68.346 24.552 1.00 92.05  ? 141 GLY E O   1 
ATOM   5469 N  N   . SER E 1 142 ? -21.370 -68.362 26.816 1.00 96.80  ? 142 SER E N   1 
ATOM   5470 C  CA  . SER E 1 142 ? -22.573 -69.152 27.066 1.00 97.05  ? 142 SER E CA  1 
ATOM   5471 C  C   . SER E 1 142 ? -23.811 -68.387 26.626 1.00 92.84  ? 142 SER E C   1 
ATOM   5472 O  O   . SER E 1 142 ? -23.718 -67.204 26.267 1.00 90.40  ? 142 SER E O   1 
ATOM   5473 C  CB  . SER E 1 142 ? -22.672 -69.542 28.559 1.00 101.14 ? 142 SER E CB  1 
ATOM   5474 O  OG  . SER E 1 142 ? -22.658 -68.400 29.410 1.00 101.50 ? 142 SER E OG  1 
ATOM   5475 N  N   . ARG E 1 143 ? -24.963 -69.056 26.679 1.00 92.32  ? 143 ARG E N   1 
ATOM   5476 C  CA  . ARG E 1 143 ? -26.179 -68.559 26.063 1.00 88.93  ? 143 ARG E CA  1 
ATOM   5477 C  C   . ARG E 1 143 ? -27.154 -68.019 27.104 1.00 88.42  ? 143 ARG E C   1 
ATOM   5478 O  O   . ARG E 1 143 ? -27.981 -68.732 27.624 1.00 89.95  ? 143 ARG E O   1 
ATOM   5479 C  CB  . ARG E 1 143 ? -26.783 -69.677 25.232 1.00 89.14  ? 143 ARG E CB  1 
ATOM   5480 C  CG  . ARG E 1 143 ? -25.782 -70.242 24.245 1.00 91.71  ? 143 ARG E CG  1 
ATOM   5481 C  CD  . ARG E 1 143 ? -26.364 -71.328 23.365 1.00 94.59  ? 143 ARG E CD  1 
ATOM   5482 N  NE  . ARG E 1 143 ? -25.504 -71.623 22.219 1.00 96.70  ? 143 ARG E NE  1 
ATOM   5483 C  CZ  . ARG E 1 143 ? -25.745 -72.556 21.297 1.00 99.06  ? 143 ARG E CZ  1 
ATOM   5484 N  NH1 . ARG E 1 143 ? -26.835 -73.312 21.358 1.00 99.71  ? 143 ARG E NH1 1 
ATOM   5485 N  NH2 . ARG E 1 143 ? -24.892 -72.728 20.293 1.00 101.26 ? 143 ARG E NH2 1 
ATOM   5486 N  N   . LEU E 1 144 ? -27.050 -66.731 27.383 1.00 86.64  ? 144 LEU E N   1 
ATOM   5487 C  CA  . LEU E 1 144 ? -27.775 -66.112 28.490 1.00 87.71  ? 144 LEU E CA  1 
ATOM   5488 C  C   . LEU E 1 144 ? -29.310 -66.168 28.395 1.00 86.23  ? 144 LEU E C   1 
ATOM   5489 O  O   . LEU E 1 144 ? -29.985 -66.358 29.409 1.00 88.76  ? 144 LEU E O   1 
ATOM   5490 C  CB  . LEU E 1 144 ? -27.321 -64.645 28.663 1.00 87.07  ? 144 LEU E CB  1 
ATOM   5491 C  CG  . LEU E 1 144 ? -25.986 -64.375 29.370 1.00 90.26  ? 144 LEU E CG  1 
ATOM   5492 C  CD1 . LEU E 1 144 ? -25.733 -62.876 29.522 1.00 90.66  ? 144 LEU E CD1 1 
ATOM   5493 C  CD2 . LEU E 1 144 ? -25.941 -65.044 30.754 1.00 95.97  ? 144 LEU E CD2 1 
ATOM   5494 N  N   . ALA E 1 145 ? -29.846 -65.937 27.198 1.00 82.55  ? 145 ALA E N   1 
ATOM   5495 C  CA  . ALA E 1 145 ? -31.289 -65.986 26.939 1.00 81.57  ? 145 ALA E CA  1 
ATOM   5496 C  C   . ALA E 1 145 ? -31.523 -66.271 25.469 1.00 79.09  ? 145 ALA E C   1 
ATOM   5497 O  O   . ALA E 1 145 ? -30.638 -66.035 24.650 1.00 78.07  ? 145 ALA E O   1 
ATOM   5498 C  CB  . ALA E 1 145 ? -31.948 -64.690 27.324 1.00 81.05  ? 145 ALA E CB  1 
ATOM   5499 N  N   . CYS E 1 146 ? -32.702 -66.785 25.127 1.00 79.09  ? 146 CYS E N   1 
ATOM   5500 C  CA  . CYS E 1 146 ? -33.029 -67.100 23.724 1.00 77.32  ? 146 CYS E CA  1 
ATOM   5501 C  C   . CYS E 1 146 ? -34.500 -67.313 23.494 1.00 76.75  ? 146 CYS E C   1 
ATOM   5502 O  O   . CYS E 1 146 ? -35.270 -67.418 24.422 1.00 78.68  ? 146 CYS E O   1 
ATOM   5503 C  CB  . CYS E 1 146 ? -32.277 -68.337 23.242 1.00 78.34  ? 146 CYS E CB  1 
ATOM   5504 S  SG  . CYS E 1 146 ? -32.797 -69.907 23.921 1.00 83.47  ? 146 CYS E SG  1 
ATOM   5505 N  N   . GLY E 1 147 ? -34.894 -67.360 22.240 1.00 74.74  ? 147 GLY E N   1 
ATOM   5506 C  CA  . GLY E 1 147 ? -36.246 -67.756 21.912 1.00 74.90  ? 147 GLY E CA  1 
ATOM   5507 C  C   . GLY E 1 147 ? -36.402 -68.018 20.436 1.00 73.28  ? 147 GLY E C   1 
ATOM   5508 O  O   . GLY E 1 147 ? -35.640 -67.521 19.632 1.00 71.96  ? 147 GLY E O   1 
ATOM   5509 N  N   . VAL E 1 148 ? -37.404 -68.794 20.076 1.00 73.37  ? 148 VAL E N   1 
ATOM   5510 C  CA  . VAL E 1 148 ? -37.688 -69.013 18.671 1.00 72.36  ? 148 VAL E CA  1 
ATOM   5511 C  C   . VAL E 1 148 ? -38.291 -67.782 18.041 1.00 70.94  ? 148 VAL E C   1 
ATOM   5512 O  O   . VAL E 1 148 ? -39.020 -67.045 18.669 1.00 70.82  ? 148 VAL E O   1 
ATOM   5513 C  CB  . VAL E 1 148 ? -38.638 -70.181 18.468 1.00 73.98  ? 148 VAL E CB  1 
ATOM   5514 C  CG1 . VAL E 1 148 ? -38.995 -70.322 17.039 1.00 73.36  ? 148 VAL E CG1 1 
ATOM   5515 C  CG2 . VAL E 1 148 ? -37.969 -71.429 18.933 1.00 75.57  ? 148 VAL E CG2 1 
ATOM   5516 N  N   . ILE E 1 149 ? -37.968 -67.577 16.779 1.00 70.25  ? 149 ILE E N   1 
ATOM   5517 C  CA  . ILE E 1 149 ? -38.407 -66.411 16.037 1.00 69.88  ? 149 ILE E CA  1 
ATOM   5518 C  C   . ILE E 1 149 ? -39.671 -66.742 15.339 1.00 71.10  ? 149 ILE E C   1 
ATOM   5519 O  O   . ILE E 1 149 ? -39.701 -67.682 14.577 1.00 71.99  ? 149 ILE E O   1 
ATOM   5520 C  CB  . ILE E 1 149 ? -37.408 -66.087 14.930 1.00 69.77  ? 149 ILE E CB  1 
ATOM   5521 C  CG1 . ILE E 1 149 ? -36.205 -65.351 15.475 1.00 68.40  ? 149 ILE E CG1 1 
ATOM   5522 C  CG2 . ILE E 1 149 ? -38.039 -65.227 13.893 1.00 71.10  ? 149 ILE E CG2 1 
ATOM   5523 C  CD1 . ILE E 1 149 ? -35.012 -65.592 14.655 1.00 69.30  ? 149 ILE E CD1 1 
ATOM   5524 N  N   . GLY E 1 150 ? -40.704 -65.951 15.536 1.00 71.78  ? 150 GLY E N   1 
ATOM   5525 C  CA  . GLY E 1 150 ? -42.011 -66.320 15.020 1.00 74.23  ? 150 GLY E CA  1 
ATOM   5526 C  C   . GLY E 1 150 ? -42.730 -65.227 14.284 1.00 75.84  ? 150 GLY E C   1 
ATOM   5527 O  O   . GLY E 1 150 ? -42.407 -64.067 14.443 1.00 75.36  ? 150 GLY E O   1 
ATOM   5528 N  N   . ILE E 1 151 ? -43.742 -65.611 13.509 1.00 78.66  ? 151 ILE E N   1 
ATOM   5529 C  CA  . ILE E 1 151 ? -44.412 -64.702 12.578 1.00 81.23  ? 151 ILE E CA  1 
ATOM   5530 C  C   . ILE E 1 151 ? -45.282 -63.769 13.362 1.00 83.26  ? 151 ILE E C   1 
ATOM   5531 O  O   . ILE E 1 151 ? -46.126 -64.217 14.111 1.00 84.53  ? 151 ILE E O   1 
ATOM   5532 C  CB  . ILE E 1 151 ? -45.295 -65.437 11.568 1.00 83.62  ? 151 ILE E CB  1 
ATOM   5533 C  CG1 . ILE E 1 151 ? -44.457 -66.460 10.803 1.00 83.13  ? 151 ILE E CG1 1 
ATOM   5534 C  CG2 . ILE E 1 151 ? -45.938 -64.463 10.640 1.00 85.75  ? 151 ILE E CG2 1 
ATOM   5535 C  CD1 . ILE E 1 151 ? -45.245 -67.323 9.913  1.00 86.31  ? 151 ILE E CD1 1 
ATOM   5536 N  N   . ALA E 1 152 ? -45.076 -62.474 13.174 1.00 85.01  ? 152 ALA E N   1 
ATOM   5537 C  CA  . ALA E 1 152 ? -45.715 -61.451 13.985 1.00 87.28  ? 152 ALA E CA  1 
ATOM   5538 C  C   . ALA E 1 152 ? -46.839 -60.838 13.186 1.00 92.22  ? 152 ALA E C   1 
ATOM   5539 O  O   . ALA E 1 152 ? -46.871 -60.923 11.946 1.00 93.34  ? 152 ALA E O   1 
ATOM   5540 C  CB  . ALA E 1 152 ? -44.716 -60.383 14.376 1.00 85.83  ? 152 ALA E CB  1 
ATOM   5541 N  N   . GLN E 1 153 ? -47.767 -60.201 13.896 1.00 96.09  ? 153 GLN E N   1 
ATOM   5542 C  CA  . GLN E 1 153 ? -48.850 -59.504 13.205 1.00 101.61 ? 153 GLN E CA  1 
ATOM   5543 C  C   . GLN E 1 153 ? -48.333 -58.279 12.473 1.00 103.29 ? 153 GLN E C   1 
ATOM   5544 O  O   . GLN E 1 153 ? -47.628 -57.435 13.044 1.00 102.60 ? 153 GLN E O   1 
ATOM   5545 C  CB  . GLN E 1 153 ? -49.991 -59.079 14.135 1.00 104.73 ? 153 GLN E CB  1 
ATOM   5546 C  CG  . GLN E 1 153 ? -51.170 -58.509 13.317 1.00 110.24 ? 153 GLN E CG  1 
ATOM   5547 C  CD  . GLN E 1 153 ? -52.492 -58.498 14.078 1.00 114.50 ? 153 GLN E CD  1 
ATOM   5548 O  OE1 . GLN E 1 153 ? -52.551 -58.118 15.258 1.00 115.41 ? 153 GLN E OE1 1 
ATOM   5549 N  NE2 . GLN E 1 153 ? -53.569 -58.921 13.397 1.00 117.90 ? 153 GLN E NE2 1 
ATOM   5550 O  OXT . GLN E 1 153 ? -48.638 -58.129 11.290 1.00 106.57 ? 153 GLN E OXT 1 
ATOM   5551 N  N   . ALA F 1 1   ? -37.616 -77.500 5.158  1.00 107.91 ? 1   ALA F N   1 
ATOM   5552 C  CA  . ALA F 1 1   ? -38.042 -78.042 6.501  1.00 104.16 ? 1   ALA F CA  1 
ATOM   5553 C  C   . ALA F 1 1   ? -38.783 -79.450 6.445  1.00 103.90 ? 1   ALA F C   1 
ATOM   5554 O  O   . ALA F 1 1   ? -39.999 -79.522 6.153  1.00 102.87 ? 1   ALA F O   1 
ATOM   5555 C  CB  . ALA F 1 1   ? -38.895 -76.981 7.211  1.00 100.07 ? 1   ALA F CB  1 
ATOM   5556 N  N   . THR F 1 2   ? -38.035 -80.549 6.676  1.00 105.02 ? 2   THR F N   1 
ATOM   5557 C  CA  . THR F 1 2   ? -38.612 -81.908 6.855  1.00 104.40 ? 2   THR F CA  1 
ATOM   5558 C  C   . THR F 1 2   ? -39.175 -82.028 8.267  1.00 99.68  ? 2   THR F C   1 
ATOM   5559 O  O   . THR F 1 2   ? -40.253 -82.575 8.445  1.00 98.24  ? 2   THR F O   1 
ATOM   5560 C  CB  . THR F 1 2   ? -37.564 -83.093 6.662  1.00 108.73 ? 2   THR F CB  1 
ATOM   5561 O  OG1 . THR F 1 2   ? -37.231 -83.237 5.277  1.00 113.92 ? 2   THR F OG1 1 
ATOM   5562 C  CG2 . THR F 1 2   ? -38.107 -84.483 7.171  1.00 108.22 ? 2   THR F CG2 1 
ATOM   5563 N  N   . LYS F 1 3   ? -38.436 -81.537 9.267  1.00 97.59  ? 3   LYS F N   1 
ATOM   5564 C  CA  . LYS F 1 3   ? -38.823 -81.692 10.676 1.00 93.91  ? 3   LYS F CA  1 
ATOM   5565 C  C   . LYS F 1 3   ? -38.994 -80.357 11.387 1.00 90.07  ? 3   LYS F C   1 
ATOM   5566 O  O   . LYS F 1 3   ? -38.405 -79.330 10.976 1.00 90.75  ? 3   LYS F O   1 
ATOM   5567 C  CB  . LYS F 1 3   ? -37.780 -82.505 11.443 1.00 95.82  ? 3   LYS F CB  1 
ATOM   5568 C  CG  . LYS F 1 3   ? -37.750 -83.962 11.062 1.00 100.15 ? 3   LYS F CG  1 
ATOM   5569 C  CD  . LYS F 1 3   ? -36.810 -84.771 11.972 1.00 103.90 ? 3   LYS F CD  1 
ATOM   5570 C  CE  . LYS F 1 3   ? -36.227 -85.994 11.228 1.00 109.56 ? 3   LYS F CE  1 
ATOM   5571 N  NZ  . LYS F 1 3   ? -34.908 -86.391 11.827 1.00 113.18 ? 3   LYS F NZ  1 
ATOM   5572 N  N   . ALA F 1 4   ? -39.795 -80.399 12.459 1.00 86.01  ? 4   ALA F N   1 
ATOM   5573 C  CA  . ALA F 1 4   ? -39.951 -79.276 13.392 1.00 82.66  ? 4   ALA F CA  1 
ATOM   5574 C  C   . ALA F 1 4   ? -40.222 -79.776 14.793 1.00 80.41  ? 4   ALA F C   1 
ATOM   5575 O  O   . ALA F 1 4   ? -40.386 -80.978 15.018 1.00 80.93  ? 4   ALA F O   1 
ATOM   5576 C  CB  . ALA F 1 4   ? -41.059 -78.337 12.954 1.00 80.56  ? 4   ALA F CB  1 
ATOM   5577 N  N   . VAL F 1 5   ? -40.249 -78.832 15.726 1.00 78.16  ? 5   VAL F N   1 
ATOM   5578 C  CA  . VAL F 1 5   ? -40.443 -79.119 17.140 1.00 76.76  ? 5   VAL F CA  1 
ATOM   5579 C  C   . VAL F 1 5   ? -41.026 -77.912 17.869 1.00 74.89  ? 5   VAL F C   1 
ATOM   5580 O  O   . VAL F 1 5   ? -40.923 -76.806 17.396 1.00 74.83  ? 5   VAL F O   1 
ATOM   5581 C  CB  . VAL F 1 5   ? -39.117 -79.475 17.812 1.00 78.64  ? 5   VAL F CB  1 
ATOM   5582 C  CG1 . VAL F 1 5   ? -38.281 -78.226 17.982 1.00 78.73  ? 5   VAL F CG1 1 
ATOM   5583 C  CG2 . VAL F 1 5   ? -39.342 -80.143 19.158 1.00 77.38  ? 5   VAL F CG2 1 
ATOM   5584 N  N   . CYS F 1 6   ? -41.634 -78.127 19.022 1.00 73.93  ? 6   CYS F N   1 
ATOM   5585 C  CA  . CYS F 1 6   ? -42.218 -77.047 19.767 1.00 72.93  ? 6   CYS F CA  1 
ATOM   5586 C  C   . CYS F 1 6   ? -42.281 -77.407 21.222 1.00 73.12  ? 6   CYS F C   1 
ATOM   5587 O  O   . CYS F 1 6   ? -42.810 -78.443 21.556 1.00 73.13  ? 6   CYS F O   1 
ATOM   5588 C  CB  . CYS F 1 6   ? -43.638 -76.792 19.284 1.00 71.22  ? 6   CYS F CB  1 
ATOM   5589 S  SG  . CYS F 1 6   ? -44.591 -75.715 20.410 1.00 70.41  ? 6   CYS F SG  1 
ATOM   5590 N  N   . VAL F 1 7   ? -41.761 -76.557 22.093 1.00 73.86  ? 7   VAL F N   1 
ATOM   5591 C  CA  . VAL F 1 7   ? -41.911 -76.776 23.519 1.00 74.48  ? 7   VAL F CA  1 
ATOM   5592 C  C   . VAL F 1 7   ? -43.070 -75.978 24.069 1.00 73.75  ? 7   VAL F C   1 
ATOM   5593 O  O   . VAL F 1 7   ? -43.102 -74.754 23.974 1.00 73.82  ? 7   VAL F O   1 
ATOM   5594 C  CB  . VAL F 1 7   ? -40.694 -76.352 24.268 1.00 76.44  ? 7   VAL F CB  1 
ATOM   5595 C  CG1 . VAL F 1 7   ? -40.851 -76.688 25.710 1.00 77.24  ? 7   VAL F CG1 1 
ATOM   5596 C  CG2 . VAL F 1 7   ? -39.506 -77.039 23.704 1.00 78.55  ? 7   VAL F CG2 1 
ATOM   5597 N  N   . LEU F 1 8   ? -44.013 -76.680 24.673 1.00 73.78  ? 8   LEU F N   1 
ATOM   5598 C  CA  . LEU F 1 8   ? -45.182 -76.063 25.245 1.00 73.31  ? 8   LEU F CA  1 
ATOM   5599 C  C   . LEU F 1 8   ? -44.912 -75.710 26.671 1.00 75.79  ? 8   LEU F C   1 
ATOM   5600 O  O   . LEU F 1 8   ? -44.413 -76.535 27.394 1.00 77.03  ? 8   LEU F O   1 
ATOM   5601 C  CB  . LEU F 1 8   ? -46.338 -77.037 25.156 1.00 72.24  ? 8   LEU F CB  1 
ATOM   5602 C  CG  . LEU F 1 8   ? -46.814 -77.265 23.718 1.00 70.10  ? 8   LEU F CG  1 
ATOM   5603 C  CD1 . LEU F 1 8   ? -47.776 -78.361 23.672 1.00 67.90  ? 8   LEU F CD1 1 
ATOM   5604 C  CD2 . LEU F 1 8   ? -47.484 -76.044 23.146 1.00 70.01  ? 8   LEU F CD2 1 
ATOM   5605 N  N   . LYS F 1 9   ? -45.216 -74.473 27.049 1.00 77.47  ? 9   LYS F N   1 
ATOM   5606 C  CA  . LYS F 1 9   ? -45.077 -73.983 28.423 1.00 81.16  ? 9   LYS F CA  1 
ATOM   5607 C  C   . LYS F 1 9   ? -46.193 -73.028 28.715 1.00 81.26  ? 9   LYS F C   1 
ATOM   5608 O  O   . LYS F 1 9   ? -46.816 -72.509 27.808 1.00 79.90  ? 9   LYS F O   1 
ATOM   5609 C  CB  . LYS F 1 9   ? -43.797 -73.184 28.609 1.00 83.62  ? 9   LYS F CB  1 
ATOM   5610 C  CG  . LYS F 1 9   ? -42.485 -73.967 28.487 1.00 88.16  ? 9   LYS F CG  1 
ATOM   5611 C  CD  . LYS F 1 9   ? -41.967 -74.556 29.831 1.00 94.55  ? 9   LYS F CD  1 
ATOM   5612 C  CE  . LYS F 1 9   ? -40.444 -74.819 29.795 1.00 97.99  ? 9   LYS F CE  1 
ATOM   5613 N  NZ  . LYS F 1 9   ? -39.995 -75.630 30.966 1.00 101.96 ? 9   LYS F NZ  1 
ATOM   5614 N  N   . GLY F 1 10  ? -46.424 -72.760 29.984 1.00 83.79  ? 10  GLY F N   1 
ATOM   5615 C  CA  . GLY F 1 10  ? -47.474 -71.833 30.353 1.00 84.59  ? 10  GLY F CA  1 
ATOM   5616 C  C   . GLY F 1 10  ? -47.368 -71.479 31.804 1.00 88.07  ? 10  GLY F C   1 
ATOM   5617 O  O   . GLY F 1 10  ? -46.490 -71.958 32.492 1.00 89.88  ? 10  GLY F O   1 
ATOM   5618 N  N   . ASP F 1 11  ? -48.266 -70.630 32.265 1.00 89.73  ? 11  ASP F N   1 
ATOM   5619 C  CA  . ASP F 1 11  ? -48.353 -70.288 33.684 1.00 93.85  ? 11  ASP F CA  1 
ATOM   5620 C  C   . ASP F 1 11  ? -48.700 -71.499 34.545 1.00 94.74  ? 11  ASP F C   1 
ATOM   5621 O  O   . ASP F 1 11  ? -48.281 -71.593 35.703 1.00 97.60  ? 11  ASP F O   1 
ATOM   5622 C  CB  . ASP F 1 11  ? -49.435 -69.222 33.903 1.00 95.45  ? 11  ASP F CB  1 
ATOM   5623 C  CG  . ASP F 1 11  ? -48.984 -67.837 33.482 1.00 98.28  ? 11  ASP F CG  1 
ATOM   5624 O  OD1 . ASP F 1 11  ? -47.752 -67.616 33.469 1.00 101.81 ? 11  ASP F OD1 1 
ATOM   5625 O  OD2 . ASP F 1 11  ? -49.854 -66.977 33.164 1.00 101.30 ? 11  ASP F OD2 1 
ATOM   5626 N  N   . GLY F 1 12  ? -49.497 -72.406 33.973 1.00 92.37  ? 12  GLY F N   1 
ATOM   5627 C  CA  . GLY F 1 12  ? -49.928 -73.617 34.654 1.00 92.67  ? 12  GLY F CA  1 
ATOM   5628 C  C   . GLY F 1 12  ? -48.776 -74.559 34.927 1.00 92.89  ? 12  GLY F C   1 
ATOM   5629 O  O   . GLY F 1 12  ? -47.618 -74.229 34.726 1.00 92.86  ? 12  GLY F O   1 
ATOM   5630 N  N   . PRO F 1 13  ? -49.102 -75.752 35.394 1.00 93.10  ? 13  PRO F N   1 
ATOM   5631 C  CA  . PRO F 1 13  ? -48.153 -76.835 35.500 1.00 93.42  ? 13  PRO F CA  1 
ATOM   5632 C  C   . PRO F 1 13  ? -48.108 -77.626 34.206 1.00 89.68  ? 13  PRO F C   1 
ATOM   5633 O  O   . PRO F 1 13  ? -47.414 -78.629 34.130 1.00 89.88  ? 13  PRO F O   1 
ATOM   5634 C  CB  . PRO F 1 13  ? -48.774 -77.702 36.572 1.00 96.27  ? 13  PRO F CB  1 
ATOM   5635 C  CG  . PRO F 1 13  ? -50.248 -77.586 36.289 1.00 94.95  ? 13  PRO F CG  1 
ATOM   5636 C  CD  . PRO F 1 13  ? -50.464 -76.193 35.737 1.00 93.55  ? 13  PRO F CD  1 
ATOM   5637 N  N   . VAL F 1 14  ? -48.869 -77.176 33.206 1.00 86.42  ? 14  VAL F N   1 
ATOM   5638 C  CA  . VAL F 1 14  ? -48.954 -77.847 31.913 1.00 83.18  ? 14  VAL F CA  1 
ATOM   5639 C  C   . VAL F 1 14  ? -47.669 -77.610 31.160 1.00 82.14  ? 14  VAL F C   1 
ATOM   5640 O  O   . VAL F 1 14  ? -47.121 -76.510 31.171 1.00 82.32  ? 14  VAL F O   1 
ATOM   5641 C  CB  . VAL F 1 14  ? -50.079 -77.295 31.036 1.00 80.65  ? 14  VAL F CB  1 
ATOM   5642 C  CG1 . VAL F 1 14  ? -50.410 -78.287 29.945 1.00 77.46  ? 14  VAL F CG1 1 
ATOM   5643 C  CG2 . VAL F 1 14  ? -51.290 -76.962 31.881 1.00 82.64  ? 14  VAL F CG2 1 
ATOM   5644 N  N   . GLN F 1 15  ? -47.191 -78.659 30.518 1.00 81.27  ? 15  GLN F N   1 
ATOM   5645 C  CA  . GLN F 1 15  ? -46.001 -78.568 29.719 1.00 80.82  ? 15  GLN F CA  1 
ATOM   5646 C  C   . GLN F 1 15  ? -45.727 -79.860 28.941 1.00 79.84  ? 15  GLN F C   1 
ATOM   5647 O  O   . GLN F 1 15  ? -46.153 -80.936 29.326 1.00 80.69  ? 15  GLN F O   1 
ATOM   5648 C  CB  . GLN F 1 15  ? -44.800 -78.205 30.586 1.00 83.69  ? 15  GLN F CB  1 
ATOM   5649 C  CG  . GLN F 1 15  ? -44.267 -79.350 31.424 1.00 87.66  ? 15  GLN F CG  1 
ATOM   5650 C  CD  . GLN F 1 15  ? -43.140 -78.939 32.370 1.00 92.70  ? 15  GLN F CD  1 
ATOM   5651 O  OE1 . GLN F 1 15  ? -42.713 -79.735 33.221 1.00 96.86  ? 15  GLN F OE1 1 
ATOM   5652 N  NE2 . GLN F 1 15  ? -42.651 -77.698 32.225 1.00 92.64  ? 15  GLN F NE2 1 
ATOM   5653 N  N   . GLY F 1 16  ? -45.019 -79.729 27.827 1.00 78.18  ? 16  GLY F N   1 
ATOM   5654 C  CA  . GLY F 1 16  ? -44.645 -80.876 27.025 1.00 77.85  ? 16  GLY F CA  1 
ATOM   5655 C  C   . GLY F 1 16  ? -43.801 -80.486 25.838 1.00 76.76  ? 16  GLY F C   1 
ATOM   5656 O  O   . GLY F 1 16  ? -43.469 -79.323 25.663 1.00 76.44  ? 16  GLY F O   1 
ATOM   5657 N  N   . ILE F 1 17  ? -43.464 -81.470 25.022 1.00 76.61  ? 17  ILE F N   1 
ATOM   5658 C  CA  . ILE F 1 17  ? -42.671 -81.278 23.814 1.00 76.26  ? 17  ILE F CA  1 
ATOM   5659 C  C   . ILE F 1 17  ? -43.361 -81.982 22.689 1.00 75.15  ? 17  ILE F C   1 
ATOM   5660 O  O   . ILE F 1 17  ? -43.728 -83.108 22.853 1.00 75.86  ? 17  ILE F O   1 
ATOM   5661 C  CB  . ILE F 1 17  ? -41.346 -82.007 23.932 1.00 79.08  ? 17  ILE F CB  1 
ATOM   5662 C  CG1 . ILE F 1 17  ? -40.699 -81.758 25.306 1.00 81.12  ? 17  ILE F CG1 1 
ATOM   5663 C  CG2 . ILE F 1 17  ? -40.454 -81.642 22.780 1.00 79.55  ? 17  ILE F CG2 1 
ATOM   5664 C  CD1 . ILE F 1 17  ? -39.407 -80.991 25.261 1.00 83.12  ? 17  ILE F CD1 1 
ATOM   5665 N  N   . ILE F 1 18  ? -43.507 -81.362 21.537 1.00 74.09  ? 18  ILE F N   1 
ATOM   5666 C  CA  . ILE F 1 18  ? -44.216 -82.004 20.433 1.00 74.16  ? 18  ILE F CA  1 
ATOM   5667 C  C   . ILE F 1 18  ? -43.397 -81.922 19.196 1.00 75.64  ? 18  ILE F C   1 
ATOM   5668 O  O   . ILE F 1 18  ? -42.925 -80.860 18.886 1.00 75.65  ? 18  ILE F O   1 
ATOM   5669 C  CB  . ILE F 1 18  ? -45.520 -81.284 20.102 1.00 72.01  ? 18  ILE F CB  1 
ATOM   5670 C  CG1 . ILE F 1 18  ? -46.493 -81.346 21.256 1.00 71.71  ? 18  ILE F CG1 1 
ATOM   5671 C  CG2 . ILE F 1 18  ? -46.191 -81.920 18.912 1.00 71.64  ? 18  ILE F CG2 1 
ATOM   5672 C  CD1 . ILE F 1 18  ? -46.883 -82.719 21.635 1.00 74.42  ? 18  ILE F CD1 1 
ATOM   5673 N  N   . ASN F 1 19  ? -43.272 -83.011 18.458 1.00 77.81  ? 19  ASN F N   1 
ATOM   5674 C  CA  . ASN F 1 19  ? -42.463 -83.018 17.244 1.00 80.14  ? 19  ASN F CA  1 
ATOM   5675 C  C   . ASN F 1 19  ? -43.275 -83.059 15.994 1.00 80.36  ? 19  ASN F C   1 
ATOM   5676 O  O   . ASN F 1 19  ? -44.409 -83.449 16.016 1.00 79.58  ? 19  ASN F O   1 
ATOM   5677 C  CB  . ASN F 1 19  ? -41.559 -84.230 17.257 1.00 83.30  ? 19  ASN F CB  1 
ATOM   5678 C  CG  . ASN F 1 19  ? -40.603 -84.219 18.425 1.00 84.80  ? 19  ASN F CG  1 
ATOM   5679 O  OD1 . ASN F 1 19  ? -40.839 -84.886 19.436 1.00 85.85  ? 19  ASN F OD1 1 
ATOM   5680 N  ND2 . ASN F 1 19  ? -39.526 -83.440 18.310 1.00 85.87  ? 19  ASN F ND2 1 
ATOM   5681 N  N   . PHE F 1 20  ? -42.677 -82.680 14.885 1.00 82.63  ? 20  PHE F N   1 
ATOM   5682 C  CA  . PHE F 1 20  ? -43.364 -82.720 13.597 1.00 84.16  ? 20  PHE F CA  1 
ATOM   5683 C  C   . PHE F 1 20  ? -42.439 -83.312 12.575 1.00 88.49  ? 20  PHE F C   1 
ATOM   5684 O  O   . PHE F 1 20  ? -41.223 -83.129 12.671 1.00 90.33  ? 20  PHE F O   1 
ATOM   5685 C  CB  . PHE F 1 20  ? -43.717 -81.329 13.118 1.00 82.69  ? 20  PHE F CB  1 
ATOM   5686 C  CG  . PHE F 1 20  ? -44.638 -80.577 14.039 1.00 80.18  ? 20  PHE F CG  1 
ATOM   5687 C  CD1 . PHE F 1 20  ? -44.217 -80.164 15.297 1.00 80.15  ? 20  PHE F CD1 1 
ATOM   5688 C  CD2 . PHE F 1 20  ? -45.913 -80.235 13.631 1.00 78.41  ? 20  PHE F CD2 1 
ATOM   5689 C  CE1 . PHE F 1 20  ? -45.067 -79.449 16.125 1.00 77.78  ? 20  PHE F CE1 1 
ATOM   5690 C  CE2 . PHE F 1 20  ? -46.759 -79.532 14.467 1.00 75.23  ? 20  PHE F CE2 1 
ATOM   5691 C  CZ  . PHE F 1 20  ? -46.338 -79.142 15.706 1.00 75.07  ? 20  PHE F CZ  1 
ATOM   5692 N  N   . GLU F 1 21  ? -43.009 -84.012 11.599 1.00 91.11  ? 21  GLU F N   1 
ATOM   5693 C  CA  . GLU F 1 21  ? -42.222 -84.589 10.523 1.00 95.81  ? 21  GLU F CA  1 
ATOM   5694 C  C   . GLU F 1 21  ? -43.060 -84.616 9.245  1.00 97.22  ? 21  GLU F C   1 
ATOM   5695 O  O   . GLU F 1 21  ? -44.192 -85.088 9.250  1.00 96.89  ? 21  GLU F O   1 
ATOM   5696 C  CB  . GLU F 1 21  ? -41.715 -85.990 10.917 1.00 98.70  ? 21  GLU F CB  1 
ATOM   5697 C  CG  . GLU F 1 21  ? -40.614 -86.545 9.982  1.00 105.67 ? 21  GLU F CG  1 
ATOM   5698 C  CD  . GLU F 1 21  ? -40.054 -87.942 10.392 1.00 111.82 ? 21  GLU F CD  1 
ATOM   5699 O  OE1 . GLU F 1 21  ? -40.842 -88.816 10.846 1.00 113.55 ? 21  GLU F OE1 1 
ATOM   5700 O  OE2 . GLU F 1 21  ? -38.820 -88.163 10.223 1.00 116.31 ? 21  GLU F OE2 1 
ATOM   5701 N  N   . GLN F 1 22  ? -42.520 -84.049 8.173  1.00 99.68  ? 22  GLN F N   1 
ATOM   5702 C  CA  . GLN F 1 22  ? -43.163 -84.058 6.863  1.00 102.20 ? 22  GLN F CA  1 
ATOM   5703 C  C   . GLN F 1 22  ? -42.139 -84.628 5.888  1.00 108.03 ? 22  GLN F C   1 
ATOM   5704 O  O   . GLN F 1 22  ? -41.298 -83.895 5.322  1.00 109.62 ? 22  GLN F O   1 
ATOM   5705 C  CB  . GLN F 1 22  ? -43.614 -82.649 6.447  1.00 100.30 ? 22  GLN F CB  1 
ATOM   5706 C  CG  . GLN F 1 22  ? -44.362 -82.598 5.102  1.00 102.37 ? 22  GLN F CG  1 
ATOM   5707 C  CD  . GLN F 1 22  ? -45.015 -81.237 4.778  1.00 100.44 ? 22  GLN F CD  1 
ATOM   5708 O  OE1 . GLN F 1 22  ? -44.425 -80.175 4.985  1.00 98.70  ? 22  GLN F OE1 1 
ATOM   5709 N  NE2 . GLN F 1 22  ? -46.235 -81.279 4.251  1.00 100.73 ? 22  GLN F NE2 1 
ATOM   5710 N  N   . LYS F 1 23  ? -42.193 -85.954 5.729  1.00 111.91 ? 23  LYS F N   1 
ATOM   5711 C  CA  . LYS F 1 23  ? -41.257 -86.664 4.850  1.00 117.97 ? 23  LYS F CA  1 
ATOM   5712 C  C   . LYS F 1 23  ? -41.411 -86.216 3.404  1.00 121.09 ? 23  LYS F C   1 
ATOM   5713 O  O   . LYS F 1 23  ? -40.431 -86.081 2.697  1.00 124.66 ? 23  LYS F O   1 
ATOM   5714 C  CB  . LYS F 1 23  ? -41.401 -88.199 4.966  1.00 120.92 ? 23  LYS F CB  1 
ATOM   5715 C  CG  . LYS F 1 23  ? -40.478 -88.824 6.062  1.00 122.65 ? 23  LYS F CG  1 
ATOM   5716 C  CD  . LYS F 1 23  ? -40.984 -90.196 6.541  1.00 125.95 ? 23  LYS F CD  1 
ATOM   5717 C  CE  . LYS F 1 23  ? -42.251 -90.034 7.447  1.00 123.01 ? 23  LYS F CE  1 
ATOM   5718 N  NZ  . LYS F 1 23  ? -42.928 -91.326 7.807  1.00 125.36 ? 23  LYS F NZ  1 
ATOM   5719 N  N   . GLU F 1 24  ? -42.628 -85.962 2.970  1.00 120.48 ? 24  GLU F N   1 
ATOM   5720 C  CA  . GLU F 1 24  ? -42.807 -85.491 1.622  1.00 124.23 ? 24  GLU F CA  1 
ATOM   5721 C  C   . GLU F 1 24  ? -43.265 -84.070 1.578  1.00 121.52 ? 24  GLU F C   1 
ATOM   5722 O  O   . GLU F 1 24  ? -44.221 -83.712 2.264  1.00 117.74 ? 24  GLU F O   1 
ATOM   5723 C  CB  . GLU F 1 24  ? -43.857 -86.324 0.927  1.00 127.21 ? 24  GLU F CB  1 
ATOM   5724 C  CG  . GLU F 1 24  ? -43.339 -87.677 0.447  1.00 133.22 ? 24  GLU F CG  1 
ATOM   5725 C  CD  . GLU F 1 24  ? -44.360 -88.383 -0.439 1.00 137.83 ? 24  GLU F CD  1 
ATOM   5726 O  OE1 . GLU F 1 24  ? -45.612 -88.151 -0.255 1.00 135.70 ? 24  GLU F OE1 1 
ATOM   5727 O  OE2 . GLU F 1 24  ? -43.879 -89.147 -1.325 1.00 143.73 ? 24  GLU F OE2 1 
ATOM   5728 N  N   . SER F 1 25  ? -42.616 -83.281 0.728  1.00 124.29 ? 25  SER F N   1 
ATOM   5729 C  CA  . SER F 1 25  ? -43.099 -81.952 0.416  1.00 123.26 ? 25  SER F CA  1 
ATOM   5730 C  C   . SER F 1 25  ? -44.597 -82.000 0.079  1.00 122.59 ? 25  SER F C   1 
ATOM   5731 O  O   . SER F 1 25  ? -45.056 -82.840 -0.717 1.00 125.92 ? 25  SER F O   1 
ATOM   5732 C  CB  . SER F 1 25  ? -42.331 -81.366 -0.768 1.00 128.01 ? 25  SER F CB  1 
ATOM   5733 O  OG  . SER F 1 25  ? -42.965 -80.163 -1.198 1.00 128.37 ? 25  SER F OG  1 
ATOM   5734 N  N   . ASN F 1 26  ? -45.353 -81.114 0.718  1.00 118.47 ? 26  ASN F N   1 
ATOM   5735 C  CA  . ASN F 1 26  ? -46.821 -81.075 0.559  1.00 117.72 ? 26  ASN F CA  1 
ATOM   5736 C  C   . ASN F 1 26  ? -47.561 -82.399 0.857  1.00 116.86 ? 26  ASN F C   1 
ATOM   5737 O  O   . ASN F 1 26  ? -48.753 -82.535 0.556  1.00 117.32 ? 26  ASN F O   1 
ATOM   5738 C  CB  . ASN F 1 26  ? -47.199 -80.572 -0.843 1.00 122.21 ? 26  ASN F CB  1 
ATOM   5739 C  CG  . ASN F 1 26  ? -46.877 -79.090 -1.051 1.00 123.07 ? 26  ASN F CG  1 
ATOM   5740 O  OD1 . ASN F 1 26  ? -46.741 -78.281 -0.091 1.00 120.39 ? 26  ASN F OD1 1 
ATOM   5741 N  ND2 . ASN F 1 26  ? -46.757 -78.722 -2.326 1.00 127.74 ? 26  ASN F ND2 1 
ATOM   5742 N  N   . GLY F 1 27  ? -46.861 -83.352 1.474  1.00 115.50 ? 27  GLY F N   1 
ATOM   5743 C  CA  . GLY F 1 27  ? -47.478 -84.576 1.938  1.00 114.22 ? 27  GLY F CA  1 
ATOM   5744 C  C   . GLY F 1 27  ? -48.141 -84.347 3.282  1.00 108.14 ? 27  GLY F C   1 
ATOM   5745 O  O   . GLY F 1 27  ? -48.440 -83.215 3.649  1.00 105.02 ? 27  GLY F O   1 
ATOM   5746 N  N   . PRO F 1 28  ? -48.373 -85.428 4.033  1.00 106.28 ? 28  PRO F N   1 
ATOM   5747 C  CA  . PRO F 1 28  ? -48.956 -85.327 5.353  1.00 101.23 ? 28  PRO F CA  1 
ATOM   5748 C  C   . PRO F 1 28  ? -47.840 -85.087 6.362  1.00 98.14  ? 28  PRO F C   1 
ATOM   5749 O  O   . PRO F 1 28  ? -46.654 -85.173 6.003  1.00 100.05 ? 28  PRO F O   1 
ATOM   5750 C  CB  . PRO F 1 28  ? -49.573 -86.712 5.557  1.00 102.63 ? 28  PRO F CB  1 
ATOM   5751 C  CG  . PRO F 1 28  ? -48.577 -87.628 4.909  1.00 107.13 ? 28  PRO F CG  1 
ATOM   5752 C  CD  . PRO F 1 28  ? -47.912 -86.803 3.774  1.00 109.81 ? 28  PRO F CD  1 
ATOM   5753 N  N   . VAL F 1 29  ? -48.228 -84.830 7.606  1.00 93.45  ? 29  VAL F N   1 
ATOM   5754 C  CA  . VAL F 1 29  ? -47.319 -84.400 8.644  1.00 90.64  ? 29  VAL F CA  1 
ATOM   5755 C  C   . VAL F 1 29  ? -47.574 -85.198 9.897  1.00 89.24  ? 29  VAL F C   1 
ATOM   5756 O  O   . VAL F 1 29  ? -48.623 -85.022 10.505 1.00 87.51  ? 29  VAL F O   1 
ATOM   5757 C  CB  . VAL F 1 29  ? -47.604 -82.948 9.009  1.00 87.51  ? 29  VAL F CB  1 
ATOM   5758 C  CG1 . VAL F 1 29  ? -46.729 -82.527 10.144 1.00 84.92  ? 29  VAL F CG1 1 
ATOM   5759 C  CG2 . VAL F 1 29  ? -47.410 -82.054 7.822  1.00 89.16  ? 29  VAL F CG2 1 
ATOM   5760 N  N   . LYS F 1 30  ? -46.649 -86.056 10.317 1.00 90.66  ? 30  LYS F N   1 
ATOM   5761 C  CA  . LYS F 1 30  ? -46.821 -86.756 11.611 1.00 89.82  ? 30  LYS F CA  1 
ATOM   5762 C  C   . LYS F 1 30  ? -46.497 -85.820 12.746 1.00 86.25  ? 30  LYS F C   1 
ATOM   5763 O  O   . LYS F 1 30  ? -45.451 -85.201 12.752 1.00 86.41  ? 30  LYS F O   1 
ATOM   5764 C  CB  . LYS F 1 30  ? -45.955 -88.015 11.752 1.00 93.26  ? 30  LYS F CB  1 
ATOM   5765 C  CG  . LYS F 1 30  ? -46.637 -89.291 11.238 1.00 98.64  ? 30  LYS F CG  1 
ATOM   5766 C  CD  . LYS F 1 30  ? -45.646 -90.362 10.713 1.00 105.72 ? 30  LYS F CD  1 
ATOM   5767 C  CE  . LYS F 1 30  ? -45.846 -90.643 9.185  1.00 109.90 ? 30  LYS F CE  1 
ATOM   5768 N  NZ  . LYS F 1 30  ? -45.893 -92.108 8.921  1.00 114.30 ? 30  LYS F NZ  1 
ATOM   5769 N  N   . VAL F 1 31  ? -47.402 -85.733 13.706 1.00 83.63  ? 31  VAL F N   1 
ATOM   5770 C  CA  . VAL F 1 31  ? -47.225 -84.890 14.856 1.00 80.81  ? 31  VAL F CA  1 
ATOM   5771 C  C   . VAL F 1 31  ? -47.252 -85.786 16.060 1.00 81.61  ? 31  VAL F C   1 
ATOM   5772 O  O   . VAL F 1 31  ? -48.231 -86.469 16.293 1.00 82.02  ? 31  VAL F O   1 
ATOM   5773 C  CB  . VAL F 1 31  ? -48.369 -83.925 14.963 1.00 78.13  ? 31  VAL F CB  1 
ATOM   5774 C  CG1 . VAL F 1 31  ? -48.213 -83.071 16.214 1.00 75.08  ? 31  VAL F CG1 1 
ATOM   5775 C  CG2 . VAL F 1 31  ? -48.444 -83.100 13.713 1.00 77.64  ? 31  VAL F CG2 1 
ATOM   5776 N  N   . TRP F 1 32  ? -46.192 -85.821 16.835 1.00 82.77  ? 32  TRP F N   1 
ATOM   5777 C  CA  . TRP F 1 32  ? -46.255 -86.613 18.047 1.00 84.14  ? 32  TRP F CA  1 
ATOM   5778 C  C   . TRP F 1 32  ? -45.341 -86.120 19.149 1.00 83.12  ? 32  TRP F C   1 
ATOM   5779 O  O   . TRP F 1 32  ? -44.365 -85.408 18.920 1.00 82.85  ? 32  TRP F O   1 
ATOM   5780 C  CB  . TRP F 1 32  ? -45.949 -88.081 17.748 1.00 88.04  ? 32  TRP F CB  1 
ATOM   5781 C  CG  . TRP F 1 32  ? -44.531 -88.364 17.885 1.00 93.92  ? 32  TRP F CG  1 
ATOM   5782 C  CD1 . TRP F 1 32  ? -43.909 -88.972 18.944 1.00 98.67  ? 32  TRP F CD1 1 
ATOM   5783 C  CD2 . TRP F 1 32  ? -43.503 -87.997 16.952 1.00 99.25  ? 32  TRP F CD2 1 
ATOM   5784 N  NE1 . TRP F 1 32  ? -42.548 -89.017 18.717 1.00 103.11 ? 32  TRP F NE1 1 
ATOM   5785 C  CE2 . TRP F 1 32  ? -42.268 -88.430 17.503 1.00 103.27 ? 32  TRP F CE2 1 
ATOM   5786 C  CE3 . TRP F 1 32  ? -43.504 -87.347 15.696 1.00 99.74  ? 32  TRP F CE3 1 
ATOM   5787 C  CZ2 . TRP F 1 32  ? -41.023 -88.232 16.835 1.00 106.02 ? 32  TRP F CZ2 1 
ATOM   5788 C  CZ3 . TRP F 1 32  ? -42.263 -87.150 15.023 1.00 102.81 ? 32  TRP F CZ3 1 
ATOM   5789 C  CH2 . TRP F 1 32  ? -41.046 -87.594 15.601 1.00 105.83 ? 32  TRP F CH2 1 
ATOM   5790 N  N   . GLY F 1 33  ? -45.688 -86.526 20.356 1.00 82.82  ? 33  GLY F N   1 
ATOM   5791 C  CA  . GLY F 1 33  ? -44.959 -86.134 21.522 1.00 82.95  ? 33  GLY F CA  1 
ATOM   5792 C  C   . GLY F 1 33  ? -45.804 -86.383 22.739 1.00 82.39  ? 33  GLY F C   1 
ATOM   5793 O  O   . GLY F 1 33  ? -46.637 -87.258 22.738 1.00 83.34  ? 33  GLY F O   1 
ATOM   5794 N  N   . SER F 1 34  ? -45.602 -85.591 23.774 1.00 81.45  ? 34  SER F N   1 
ATOM   5795 C  CA  . SER F 1 34  ? -46.221 -85.858 25.042 1.00 81.83  ? 34  SER F CA  1 
ATOM   5796 C  C   . SER F 1 34  ? -46.375 -84.609 25.868 1.00 80.32  ? 34  SER F C   1 
ATOM   5797 O  O   . SER F 1 34  ? -45.435 -83.839 25.992 1.00 80.67  ? 34  SER F O   1 
ATOM   5798 C  CB  . SER F 1 34  ? -45.341 -86.808 25.818 1.00 84.98  ? 34  SER F CB  1 
ATOM   5799 O  OG  . SER F 1 34  ? -45.962 -87.111 27.040 1.00 86.68  ? 34  SER F OG  1 
ATOM   5800 N  N   . ILE F 1 35  ? -47.541 -84.436 26.470 1.00 79.33  ? 35  ILE F N   1 
ATOM   5801 C  CA  . ILE F 1 35  ? -47.792 -83.306 27.355 1.00 78.65  ? 35  ILE F CA  1 
ATOM   5802 C  C   . ILE F 1 35  ? -48.192 -83.816 28.714 1.00 80.86  ? 35  ILE F C   1 
ATOM   5803 O  O   . ILE F 1 35  ? -48.852 -84.840 28.809 1.00 82.03  ? 35  ILE F O   1 
ATOM   5804 C  CB  . ILE F 1 35  ? -48.944 -82.465 26.871 1.00 76.16  ? 35  ILE F CB  1 
ATOM   5805 C  CG1 . ILE F 1 35  ? -48.832 -82.222 25.380 1.00 74.50  ? 35  ILE F CG1 1 
ATOM   5806 C  CG2 . ILE F 1 35  ? -48.982 -81.165 27.639 1.00 75.78  ? 35  ILE F CG2 1 
ATOM   5807 C  CD1 . ILE F 1 35  ? -49.960 -81.412 24.847 1.00 72.87  ? 35  ILE F CD1 1 
ATOM   5808 N  N   . LYS F 1 36  ? -47.821 -83.099 29.766 1.00 82.13  ? 36  LYS F N   1 
ATOM   5809 C  CA  . LYS F 1 36  ? -48.218 -83.491 31.116 1.00 84.98  ? 36  LYS F CA  1 
ATOM   5810 C  C   . LYS F 1 36  ? -48.816 -82.351 31.880 1.00 84.49  ? 36  LYS F C   1 
ATOM   5811 O  O   . LYS F 1 36  ? -48.677 -81.215 31.488 1.00 82.96  ? 36  LYS F O   1 
ATOM   5812 C  CB  . LYS F 1 36  ? -47.041 -84.110 31.893 1.00 88.63  ? 36  LYS F CB  1 
ATOM   5813 C  CG  . LYS F 1 36  ? -45.694 -83.386 31.790 1.00 90.96  ? 36  LYS F CG  1 
ATOM   5814 C  CD  . LYS F 1 36  ? -44.609 -84.078 32.648 1.00 96.71  ? 36  LYS F CD  1 
ATOM   5815 C  CE  . LYS F 1 36  ? -43.518 -83.110 33.097 1.00 98.30  ? 36  LYS F CE  1 
ATOM   5816 N  NZ  . LYS F 1 36  ? -42.592 -83.813 34.049 1.00 102.54 ? 36  LYS F NZ  1 
ATOM   5817 N  N   . GLY F 1 37  ? -49.505 -82.664 32.965 1.00 86.56  ? 37  GLY F N   1 
ATOM   5818 C  CA  . GLY F 1 37  ? -50.135 -81.641 33.804 1.00 87.33  ? 37  GLY F CA  1 
ATOM   5819 C  C   . GLY F 1 37  ? -51.509 -81.211 33.329 1.00 85.28  ? 37  GLY F C   1 
ATOM   5820 O  O   . GLY F 1 37  ? -51.904 -80.040 33.458 1.00 84.61  ? 37  GLY F O   1 
ATOM   5821 N  N   . LEU F 1 38  ? -52.245 -82.175 32.785 1.00 84.67  ? 38  LEU F N   1 
ATOM   5822 C  CA  . LEU F 1 38  ? -53.578 -81.930 32.207 1.00 83.16  ? 38  LEU F CA  1 
ATOM   5823 C  C   . LEU F 1 38  ? -54.679 -82.594 33.022 1.00 85.31  ? 38  LEU F C   1 
ATOM   5824 O  O   . LEU F 1 38  ? -54.446 -83.621 33.690 1.00 87.70  ? 38  LEU F O   1 
ATOM   5825 C  CB  . LEU F 1 38  ? -53.640 -82.486 30.781 1.00 80.84  ? 38  LEU F CB  1 
ATOM   5826 C  CG  . LEU F 1 38  ? -52.904 -81.611 29.779 1.00 78.42  ? 38  LEU F CG  1 
ATOM   5827 C  CD1 . LEU F 1 38  ? -52.355 -82.442 28.685 1.00 76.98  ? 38  LEU F CD1 1 
ATOM   5828 C  CD2 . LEU F 1 38  ? -53.815 -80.508 29.258 1.00 77.12  ? 38  LEU F CD2 1 
ATOM   5829 N  N   . THR F 1 39  ? -55.873 -82.009 32.984 1.00 84.77  ? 39  THR F N   1 
ATOM   5830 C  CA  . THR F 1 39  ? -57.016 -82.654 33.587 1.00 86.76  ? 39  THR F CA  1 
ATOM   5831 C  C   . THR F 1 39  ? -57.350 -83.827 32.719 1.00 86.33  ? 39  THR F C   1 
ATOM   5832 O  O   . THR F 1 39  ? -57.344 -83.704 31.505 1.00 83.70  ? 39  THR F O   1 
ATOM   5833 C  CB  . THR F 1 39  ? -58.217 -81.730 33.677 1.00 86.76  ? 39  THR F CB  1 
ATOM   5834 O  OG1 . THR F 1 39  ? -58.086 -80.664 32.732 1.00 83.70  ? 39  THR F OG1 1 
ATOM   5835 C  CG2 . THR F 1 39  ? -58.314 -81.147 35.078 1.00 89.64  ? 39  THR F CG2 1 
ATOM   5836 N  N   . GLU F 1 40  ? -57.606 -84.973 33.340 1.00 89.52  ? 40  GLU F N   1 
ATOM   5837 C  CA  . GLU F 1 40  ? -57.986 -86.169 32.596 1.00 90.11  ? 40  GLU F CA  1 
ATOM   5838 C  C   . GLU F 1 40  ? -58.997 -85.780 31.523 1.00 87.94  ? 40  GLU F C   1 
ATOM   5839 O  O   . GLU F 1 40  ? -59.806 -84.881 31.729 1.00 87.81  ? 40  GLU F O   1 
ATOM   5840 C  CB  . GLU F 1 40  ? -58.570 -87.250 33.528 1.00 94.08  ? 40  GLU F CB  1 
ATOM   5841 C  CG  . GLU F 1 40  ? -59.230 -88.449 32.772 1.00 95.87  ? 40  GLU F CG  1 
ATOM   5842 C  CD  . GLU F 1 40  ? -59.293 -89.757 33.598 1.00 101.52 ? 40  GLU F CD  1 
ATOM   5843 O  OE1 . GLU F 1 40  ? -59.787 -89.705 34.769 1.00 105.16 ? 40  GLU F OE1 1 
ATOM   5844 O  OE2 . GLU F 1 40  ? -58.862 -90.827 33.050 1.00 102.67 ? 40  GLU F OE2 1 
ATOM   5845 N  N   . GLY F 1 41  ? -58.919 -86.423 30.368 1.00 86.58  ? 41  GLY F N   1 
ATOM   5846 C  CA  . GLY F 1 41  ? -59.917 -86.211 29.336 1.00 85.21  ? 41  GLY F CA  1 
ATOM   5847 C  C   . GLY F 1 41  ? -59.444 -85.424 28.135 1.00 82.10  ? 41  GLY F C   1 
ATOM   5848 O  O   . GLY F 1 41  ? -58.251 -85.399 27.839 1.00 81.22  ? 41  GLY F O   1 
ATOM   5849 N  N   . LEU F 1 42  ? -60.386 -84.796 27.431 1.00 80.71  ? 42  LEU F N   1 
ATOM   5850 C  CA  . LEU F 1 42  ? -60.069 -84.143 26.159 1.00 78.29  ? 42  LEU F CA  1 
ATOM   5851 C  C   . LEU F 1 42  ? -59.599 -82.710 26.333 1.00 76.26  ? 42  LEU F C   1 
ATOM   5852 O  O   . LEU F 1 42  ? -60.048 -82.002 27.245 1.00 77.15  ? 42  LEU F O   1 
ATOM   5853 C  CB  . LEU F 1 42  ? -61.270 -84.128 25.220 1.00 78.54  ? 42  LEU F CB  1 
ATOM   5854 C  CG  . LEU F 1 42  ? -61.606 -85.464 24.566 1.00 80.37  ? 42  LEU F CG  1 
ATOM   5855 C  CD1 . LEU F 1 42  ? -62.850 -86.106 25.239 1.00 83.75  ? 42  LEU F CD1 1 
ATOM   5856 C  CD2 . LEU F 1 42  ? -61.792 -85.249 23.070 1.00 78.59  ? 42  LEU F CD2 1 
ATOM   5857 N  N   . HIS F 1 43  ? -58.704 -82.294 25.439 1.00 73.66  ? 43  HIS F N   1 
ATOM   5858 C  CA  . HIS F 1 43  ? -58.229 -80.931 25.409 1.00 71.72  ? 43  HIS F CA  1 
ATOM   5859 C  C   . HIS F 1 43  ? -57.984 -80.475 23.990 1.00 69.68  ? 43  HIS F C   1 
ATOM   5860 O  O   . HIS F 1 43  ? -57.349 -81.165 23.198 1.00 68.98  ? 43  HIS F O   1 
ATOM   5861 C  CB  . HIS F 1 43  ? -56.947 -80.814 26.194 1.00 71.70  ? 43  HIS F CB  1 
ATOM   5862 C  CG  . HIS F 1 43  ? -57.134 -80.964 27.659 1.00 73.88  ? 43  HIS F CG  1 
ATOM   5863 N  ND1 . HIS F 1 43  ? -57.338 -79.891 28.492 1.00 75.80  ? 43  HIS F ND1 1 
ATOM   5864 C  CD2 . HIS F 1 43  ? -57.146 -82.062 28.446 1.00 76.59  ? 43  HIS F CD2 1 
ATOM   5865 C  CE1 . HIS F 1 43  ? -57.442 -80.320 29.738 1.00 78.97  ? 43  HIS F CE1 1 
ATOM   5866 N  NE2 . HIS F 1 43  ? -57.337 -81.636 29.736 1.00 79.42  ? 43  HIS F NE2 1 
ATOM   5867 N  N   . GLY F 1 44  ? -58.469 -79.285 23.689 1.00 68.82  ? 44  GLY F N   1 
ATOM   5868 C  CA  . GLY F 1 44  ? -58.295 -78.713 22.378 1.00 67.92  ? 44  GLY F CA  1 
ATOM   5869 C  C   . GLY F 1 44  ? -56.846 -78.477 22.050 1.00 66.81  ? 44  GLY F C   1 
ATOM   5870 O  O   . GLY F 1 44  ? -56.065 -78.228 22.931 1.00 66.87  ? 44  GLY F O   1 
ATOM   5871 N  N   . PHE F 1 45  ? -56.514 -78.465 20.770 1.00 66.41  ? 45  PHE F N   1 
ATOM   5872 C  CA  . PHE F 1 45  ? -55.145 -78.490 20.336 1.00 66.00  ? 45  PHE F CA  1 
ATOM   5873 C  C   . PHE F 1 45  ? -55.043 -77.877 18.964 1.00 65.91  ? 45  PHE F C   1 
ATOM   5874 O  O   . PHE F 1 45  ? -55.477 -78.467 18.005 1.00 66.08  ? 45  PHE F O   1 
ATOM   5875 C  CB  . PHE F 1 45  ? -54.756 -79.936 20.282 1.00 66.78  ? 45  PHE F CB  1 
ATOM   5876 C  CG  . PHE F 1 45  ? -53.302 -80.190 20.046 1.00 67.15  ? 45  PHE F CG  1 
ATOM   5877 C  CD1 . PHE F 1 45  ? -52.358 -79.837 20.981 1.00 67.33  ? 45  PHE F CD1 1 
ATOM   5878 C  CD2 . PHE F 1 45  ? -52.888 -80.890 18.922 1.00 68.06  ? 45  PHE F CD2 1 
ATOM   5879 C  CE1 . PHE F 1 45  ? -51.042 -80.134 20.773 1.00 68.14  ? 45  PHE F CE1 1 
ATOM   5880 C  CE2 . PHE F 1 45  ? -51.579 -81.183 18.716 1.00 68.37  ? 45  PHE F CE2 1 
ATOM   5881 C  CZ  . PHE F 1 45  ? -50.656 -80.804 19.637 1.00 68.70  ? 45  PHE F CZ  1 
ATOM   5882 N  N   . HIS F 1 46  ? -54.460 -76.690 18.871 1.00 65.86  ? 46  HIS F N   1 
ATOM   5883 C  CA  . HIS F 1 46  ? -54.453 -75.936 17.637 1.00 66.64  ? 46  HIS F CA  1 
ATOM   5884 C  C   . HIS F 1 46  ? -53.172 -75.205 17.365 1.00 66.30  ? 46  HIS F C   1 
ATOM   5885 O  O   . HIS F 1 46  ? -52.457 -74.854 18.284 1.00 65.88  ? 46  HIS F O   1 
ATOM   5886 C  CB  . HIS F 1 46  ? -55.518 -74.874 17.716 1.00 67.52  ? 46  HIS F CB  1 
ATOM   5887 C  CG  . HIS F 1 46  ? -56.790 -75.352 18.310 1.00 69.64  ? 46  HIS F CG  1 
ATOM   5888 N  ND1 . HIS F 1 46  ? -57.323 -74.809 19.456 1.00 71.86  ? 46  HIS F ND1 1 
ATOM   5889 C  CD2 . HIS F 1 46  ? -57.642 -76.322 17.914 1.00 72.60  ? 46  HIS F CD2 1 
ATOM   5890 C  CE1 . HIS F 1 46  ? -58.457 -75.426 19.738 1.00 74.12  ? 46  HIS F CE1 1 
ATOM   5891 N  NE2 . HIS F 1 46  ? -58.672 -76.351 18.821 1.00 73.69  ? 46  HIS F NE2 1 
ATOM   5892 N  N   . VAL F 1 47  ? -52.920 -74.939 16.090 1.00 66.97  ? 47  VAL F N   1 
ATOM   5893 C  CA  . VAL F 1 47  ? -51.934 -73.958 15.692 1.00 67.46  ? 47  VAL F CA  1 
ATOM   5894 C  C   . VAL F 1 47  ? -52.643 -72.640 15.566 1.00 68.40  ? 47  VAL F C   1 
ATOM   5895 O  O   . VAL F 1 47  ? -53.647 -72.558 14.885 1.00 69.29  ? 47  VAL F O   1 
ATOM   5896 C  CB  . VAL F 1 47  ? -51.346 -74.259 14.344 1.00 68.42  ? 47  VAL F CB  1 
ATOM   5897 C  CG1 . VAL F 1 47  ? -50.376 -73.191 13.985 1.00 69.09  ? 47  VAL F CG1 1 
ATOM   5898 C  CG2 . VAL F 1 47  ? -50.662 -75.585 14.375 1.00 68.16  ? 47  VAL F CG2 1 
ATOM   5899 N  N   . HIS F 1 48  ? -52.142 -71.616 16.240 1.00 68.95  ? 48  HIS F N   1 
ATOM   5900 C  CA  . HIS F 1 48  ? -52.724 -70.288 16.152 1.00 70.48  ? 48  HIS F CA  1 
ATOM   5901 C  C   . HIS F 1 48  ? -51.857 -69.490 15.231 1.00 71.73  ? 48  HIS F C   1 
ATOM   5902 O  O   . HIS F 1 48  ? -50.772 -69.913 14.903 1.00 71.55  ? 48  HIS F O   1 
ATOM   5903 C  CB  . HIS F 1 48  ? -52.792 -69.625 17.523 1.00 70.62  ? 48  HIS F CB  1 
ATOM   5904 C  CG  . HIS F 1 48  ? -53.810 -70.229 18.439 1.00 71.27  ? 48  HIS F CG  1 
ATOM   5905 N  ND1 . HIS F 1 48  ? -54.771 -69.484 19.082 1.00 73.34  ? 48  HIS F ND1 1 
ATOM   5906 C  CD2 . HIS F 1 48  ? -54.020 -71.510 18.816 1.00 71.87  ? 48  HIS F CD2 1 
ATOM   5907 C  CE1 . HIS F 1 48  ? -55.526 -70.279 19.817 1.00 73.98  ? 48  HIS F CE1 1 
ATOM   5908 N  NE2 . HIS F 1 48  ? -55.090 -71.514 19.676 1.00 72.43  ? 48  HIS F NE2 1 
ATOM   5909 N  N   . GLU F 1 49  ? -52.338 -68.324 14.833 1.00 73.55  ? 49  GLU F N   1 
ATOM   5910 C  CA  . GLU F 1 49  ? -51.724 -67.563 13.736 1.00 75.74  ? 49  GLU F CA  1 
ATOM   5911 C  C   . GLU F 1 49  ? -50.303 -67.105 13.985 1.00 75.72  ? 49  GLU F C   1 
ATOM   5912 O  O   . GLU F 1 49  ? -49.485 -67.192 13.096 1.00 76.14  ? 49  GLU F O   1 
ATOM   5913 C  CB  . GLU F 1 49  ? -52.592 -66.347 13.357 1.00 78.11  ? 49  GLU F CB  1 
ATOM   5914 C  CG  . GLU F 1 49  ? -52.264 -65.757 11.980 1.00 81.95  ? 49  GLU F CG  1 
ATOM   5915 C  CD  . GLU F 1 49  ? -53.296 -64.760 11.483 1.00 86.91  ? 49  GLU F CD  1 
ATOM   5916 O  OE1 . GLU F 1 49  ? -54.449 -64.761 11.982 1.00 88.51  ? 49  GLU F OE1 1 
ATOM   5917 O  OE2 . GLU F 1 49  ? -52.941 -63.969 10.577 1.00 91.13  ? 49  GLU F OE2 1 
ATOM   5918 N  N   . PHE F 1 50  ? -50.016 -66.617 15.185 1.00 75.53  ? 50  PHE F N   1 
ATOM   5919 C  CA  . PHE F 1 50  ? -48.766 -65.891 15.430 1.00 76.84  ? 50  PHE F CA  1 
ATOM   5920 C  C   . PHE F 1 50  ? -47.798 -66.535 16.400 1.00 75.53  ? 50  PHE F C   1 
ATOM   5921 O  O   . PHE F 1 50  ? -48.199 -67.130 17.403 1.00 73.89  ? 50  PHE F O   1 
ATOM   5922 C  CB  . PHE F 1 50  ? -49.064 -64.479 15.950 1.00 78.72  ? 50  PHE F CB  1 
ATOM   5923 C  CG  . PHE F 1 50  ? -49.961 -63.672 15.051 1.00 81.79  ? 50  PHE F CG  1 
ATOM   5924 C  CD1 . PHE F 1 50  ? -49.752 -63.634 13.684 1.00 84.00  ? 50  PHE F CD1 1 
ATOM   5925 C  CD2 . PHE F 1 50  ? -51.014 -62.947 15.580 1.00 84.19  ? 50  PHE F CD2 1 
ATOM   5926 C  CE1 . PHE F 1 50  ? -50.581 -62.898 12.861 1.00 86.68  ? 50  PHE F CE1 1 
ATOM   5927 C  CE2 . PHE F 1 50  ? -51.852 -62.213 14.762 1.00 86.80  ? 50  PHE F CE2 1 
ATOM   5928 C  CZ  . PHE F 1 50  ? -51.635 -62.191 13.397 1.00 88.05  ? 50  PHE F CZ  1 
ATOM   5929 N  N   . GLY F 1 51  ? -46.514 -66.343 16.101 1.00 76.57  ? 51  GLY F N   1 
ATOM   5930 C  CA  . GLY F 1 51  ? -45.427 -66.734 16.978 1.00 76.68  ? 51  GLY F CA  1 
ATOM   5931 C  C   . GLY F 1 51  ? -45.134 -65.647 17.995 1.00 78.13  ? 51  GLY F C   1 
ATOM   5932 O  O   . GLY F 1 51  ? -43.993 -65.329 18.293 1.00 79.30  ? 51  GLY F O   1 
ATOM   5933 N  N   . ASP F 1 52  ? -46.185 -65.088 18.556 1.00 78.57  ? 52  ASP F N   1 
ATOM   5934 C  CA  . ASP F 1 52  ? -46.056 -63.998 19.479 1.00 80.58  ? 52  ASP F CA  1 
ATOM   5935 C  C   . ASP F 1 52  ? -46.276 -64.572 20.859 1.00 79.98  ? 52  ASP F C   1 
ATOM   5936 O  O   . ASP F 1 52  ? -47.269 -65.252 21.111 1.00 78.71  ? 52  ASP F O   1 
ATOM   5937 C  CB  . ASP F 1 52  ? -47.132 -62.983 19.152 1.00 81.90  ? 52  ASP F CB  1 
ATOM   5938 C  CG  . ASP F 1 52  ? -46.731 -61.599 19.469 1.00 85.02  ? 52  ASP F CG  1 
ATOM   5939 O  OD1 . ASP F 1 52  ? -46.337 -61.371 20.646 1.00 85.54  ? 52  ASP F OD1 1 
ATOM   5940 O  OD2 . ASP F 1 52  ? -46.838 -60.763 18.520 1.00 87.58  ? 52  ASP F OD2 1 
ATOM   5941 N  N   . ASN F 1 53  ? -45.337 -64.349 21.752 1.00 81.48  ? 53  ASN F N   1 
ATOM   5942 C  CA  . ASN F 1 53  ? -45.547 -64.734 23.127 1.00 81.93  ? 53  ASN F CA  1 
ATOM   5943 C  C   . ASN F 1 53  ? -45.270 -63.553 24.015 1.00 84.24  ? 53  ASN F C   1 
ATOM   5944 O  O   . ASN F 1 53  ? -44.952 -63.729 25.183 1.00 85.23  ? 53  ASN F O   1 
ATOM   5945 C  CB  . ASN F 1 53  ? -44.662 -65.911 23.494 1.00 81.47  ? 53  ASN F CB  1 
ATOM   5946 C  CG  . ASN F 1 53  ? -45.332 -67.239 23.270 1.00 82.00  ? 53  ASN F CG  1 
ATOM   5947 O  OD1 . ASN F 1 53  ? -45.235 -68.105 24.118 1.00 87.02  ? 53  ASN F OD1 1 
ATOM   5948 N  ND2 . ASN F 1 53  ? -46.008 -67.417 22.134 1.00 81.70  ? 53  ASN F ND2 1 
ATOM   5949 N  N   . THR F 1 54  ? -45.402 -62.355 23.439 1.00 85.44  ? 54  THR F N   1 
ATOM   5950 C  CA  . THR F 1 54  ? -45.182 -61.097 24.131 1.00 88.40  ? 54  THR F CA  1 
ATOM   5951 C  C   . THR F 1 54  ? -45.957 -61.043 25.432 1.00 89.39  ? 54  THR F C   1 
ATOM   5952 O  O   . THR F 1 54  ? -45.387 -60.791 26.487 1.00 91.50  ? 54  THR F O   1 
ATOM   5953 C  CB  . THR F 1 54  ? -45.658 -59.934 23.262 1.00 89.91  ? 54  THR F CB  1 
ATOM   5954 O  OG1 . THR F 1 54  ? -44.973 -59.991 22.016 1.00 89.00  ? 54  THR F OG1 1 
ATOM   5955 C  CG2 . THR F 1 54  ? -45.413 -58.557 23.936 1.00 94.34  ? 54  THR F CG2 1 
ATOM   5956 N  N   . ALA F 1 55  ? -47.259 -61.285 25.345 1.00 88.36  ? 55  ALA F N   1 
ATOM   5957 C  CA  . ALA F 1 55  ? -48.128 -61.309 26.504 1.00 89.58  ? 55  ALA F CA  1 
ATOM   5958 C  C   . ALA F 1 55  ? -48.664 -62.723 26.740 1.00 87.24  ? 55  ALA F C   1 
ATOM   5959 O  O   . ALA F 1 55  ? -49.853 -62.974 26.569 1.00 86.34  ? 55  ALA F O   1 
ATOM   5960 C  CB  . ALA F 1 55  ? -49.263 -60.339 26.288 1.00 91.10  ? 55  ALA F CB  1 
ATOM   5961 N  N   . GLY F 1 56  ? -47.781 -63.639 27.138 1.00 86.92  ? 56  GLY F N   1 
ATOM   5962 C  CA  . GLY F 1 56  ? -48.145 -65.045 27.326 1.00 85.21  ? 56  GLY F CA  1 
ATOM   5963 C  C   . GLY F 1 56  ? -48.757 -65.666 26.081 1.00 82.87  ? 56  GLY F C   1 
ATOM   5964 O  O   . GLY F 1 56  ? -48.350 -65.356 24.957 1.00 82.37  ? 56  GLY F O   1 
ATOM   5965 N  N   . CYS F 1 57  ? -49.745 -66.533 26.268 1.00 81.80  ? 57  CYS F N   1 
ATOM   5966 C  CA  . CYS F 1 57  ? -50.313 -67.235 25.129 1.00 79.94  ? 57  CYS F CA  1 
ATOM   5967 C  C   . CYS F 1 57  ? -51.339 -66.420 24.340 1.00 79.96  ? 57  CYS F C   1 
ATOM   5968 O  O   . CYS F 1 57  ? -51.555 -66.713 23.157 1.00 78.48  ? 57  CYS F O   1 
ATOM   5969 C  CB  . CYS F 1 57  ? -50.869 -68.584 25.570 1.00 78.71  ? 57  CYS F CB  1 
ATOM   5970 S  SG  . CYS F 1 57  ? -49.524 -69.730 26.114 1.00 80.79  ? 57  CYS F SG  1 
ATOM   5971 N  N   . THR F 1 58  ? -51.938 -65.393 24.968 1.00 82.01  ? 58  THR F N   1 
ATOM   5972 C  CA  . THR F 1 58  ? -52.973 -64.533 24.296 1.00 82.80  ? 58  THR F CA  1 
ATOM   5973 C  C   . THR F 1 58  ? -52.441 -63.798 23.074 1.00 82.93  ? 58  THR F C   1 
ATOM   5974 O  O   . THR F 1 58  ? -53.201 -63.477 22.175 1.00 83.25  ? 58  THR F O   1 
ATOM   5975 C  CB  . THR F 1 58  ? -53.568 -63.447 25.212 1.00 85.53  ? 58  THR F CB  1 
ATOM   5976 O  OG1 . THR F 1 58  ? -53.242 -63.757 26.564 1.00 86.31  ? 58  THR F OG1 1 
ATOM   5977 C  CG2 . THR F 1 58  ? -55.094 -63.346 25.022 1.00 85.46  ? 58  THR F CG2 1 
ATOM   5978 N  N   . SER F 1 59  ? -51.139 -63.531 23.062 1.00 83.06  ? 59  SER F N   1 
ATOM   5979 C  CA  . SER F 1 59  ? -50.470 -62.889 21.937 1.00 83.56  ? 59  SER F CA  1 
ATOM   5980 C  C   . SER F 1 59  ? -50.552 -63.689 20.642 1.00 81.48  ? 59  SER F C   1 
ATOM   5981 O  O   . SER F 1 59  ? -50.513 -63.109 19.563 1.00 82.23  ? 59  SER F O   1 
ATOM   5982 C  CB  . SER F 1 59  ? -48.994 -62.649 22.292 1.00 84.47  ? 59  SER F CB  1 
ATOM   5983 O  OG  . SER F 1 59  ? -48.875 -62.051 23.584 1.00 87.20  ? 59  SER F OG  1 
ATOM   5984 N  N   . ALA F 1 60  ? -50.652 -65.015 20.764 1.00 79.29  ? 60  ALA F N   1 
ATOM   5985 C  CA  . ALA F 1 60  ? -50.704 -65.944 19.618 1.00 77.70  ? 60  ALA F CA  1 
ATOM   5986 C  C   . ALA F 1 60  ? -51.802 -65.617 18.638 1.00 78.17  ? 60  ALA F C   1 
ATOM   5987 O  O   . ALA F 1 60  ? -51.687 -65.910 17.459 1.00 77.82  ? 60  ALA F O   1 
ATOM   5988 C  CB  . ALA F 1 60  ? -50.898 -67.356 20.119 1.00 75.97  ? 60  ALA F CB  1 
ATOM   5989 N  N   . GLY F 1 61  ? -52.880 -65.040 19.159 1.00 79.41  ? 61  GLY F N   1 
ATOM   5990 C  CA  . GLY F 1 61  ? -54.017 -64.599 18.359 1.00 80.70  ? 61  GLY F CA  1 
ATOM   5991 C  C   . GLY F 1 61  ? -54.980 -65.723 18.094 1.00 79.45  ? 61  GLY F C   1 
ATOM   5992 O  O   . GLY F 1 61  ? -54.926 -66.741 18.745 1.00 78.07  ? 61  GLY F O   1 
ATOM   5993 N  N   . PRO F 1 62  ? -55.841 -65.563 17.108 1.00 80.57  ? 62  PRO F N   1 
ATOM   5994 C  CA  . PRO F 1 62  ? -56.842 -66.565 16.820 1.00 79.98  ? 62  PRO F CA  1 
ATOM   5995 C  C   . PRO F 1 62  ? -56.241 -67.761 16.124 1.00 78.51  ? 62  PRO F C   1 
ATOM   5996 O  O   . PRO F 1 62  ? -55.052 -67.759 15.794 1.00 77.89  ? 62  PRO F O   1 
ATOM   5997 C  CB  . PRO F 1 62  ? -57.733 -65.853 15.825 1.00 82.47  ? 62  PRO F CB  1 
ATOM   5998 C  CG  . PRO F 1 62  ? -56.738 -65.057 14.998 1.00 83.53  ? 62  PRO F CG  1 
ATOM   5999 C  CD  . PRO F 1 62  ? -55.666 -64.631 15.984 1.00 82.73  ? 62  PRO F CD  1 
ATOM   6000 N  N   . HIS F 1 63  ? -57.081 -68.749 15.857 1.00 78.23  ? 63  HIS F N   1 
ATOM   6001 C  CA  . HIS F 1 63  ? -56.646 -69.939 15.164 1.00 77.55  ? 63  HIS F CA  1 
ATOM   6002 C  C   . HIS F 1 63  ? -56.104 -69.592 13.804 1.00 78.20  ? 63  HIS F C   1 
ATOM   6003 O  O   . HIS F 1 63  ? -56.640 -68.714 13.137 1.00 80.11  ? 63  HIS F O   1 
ATOM   6004 C  CB  . HIS F 1 63  ? -57.816 -70.849 14.938 1.00 78.28  ? 63  HIS F CB  1 
ATOM   6005 C  CG  . HIS F 1 63  ? -58.318 -71.496 16.168 1.00 78.93  ? 63  HIS F CG  1 
ATOM   6006 N  ND1 . HIS F 1 63  ? -58.775 -72.789 16.178 1.00 79.82  ? 63  HIS F ND1 1 
ATOM   6007 C  CD2 . HIS F 1 63  ? -58.440 -71.035 17.428 1.00 81.15  ? 63  HIS F CD2 1 
ATOM   6008 C  CE1 . HIS F 1 63  ? -59.160 -73.101 17.397 1.00 80.81  ? 63  HIS F CE1 1 
ATOM   6009 N  NE2 . HIS F 1 63  ? -58.965 -72.056 18.177 1.00 81.91  ? 63  HIS F NE2 1 
ATOM   6010 N  N   . PHE F 1 64  ? -55.077 -70.325 13.385 1.00 76.95  ? 64  PHE F N   1 
ATOM   6011 C  CA  . PHE F 1 64  ? -54.451 -70.125 12.092 1.00 78.13  ? 64  PHE F CA  1 
ATOM   6012 C  C   . PHE F 1 64  ? -55.440 -70.445 11.032 1.00 79.27  ? 64  PHE F C   1 
ATOM   6013 O  O   . PHE F 1 64  ? -55.809 -71.594 10.860 1.00 78.40  ? 64  PHE F O   1 
ATOM   6014 C  CB  . PHE F 1 64  ? -53.241 -71.037 11.922 1.00 77.62  ? 64  PHE F CB  1 
ATOM   6015 C  CG  . PHE F 1 64  ? -52.505 -70.850 10.619 1.00 80.43  ? 64  PHE F CG  1 
ATOM   6016 C  CD1 . PHE F 1 64  ? -52.313 -69.581 10.076 1.00 83.25  ? 64  PHE F CD1 1 
ATOM   6017 C  CD2 . PHE F 1 64  ? -51.962 -71.949 9.949  1.00 81.62  ? 64  PHE F CD2 1 
ATOM   6018 C  CE1 . PHE F 1 64  ? -51.620 -69.414 8.887  1.00 85.38  ? 64  PHE F CE1 1 
ATOM   6019 C  CE2 . PHE F 1 64  ? -51.252 -71.789 8.755  1.00 84.35  ? 64  PHE F CE2 1 
ATOM   6020 C  CZ  . PHE F 1 64  ? -51.085 -70.520 8.229  1.00 86.00  ? 64  PHE F CZ  1 
ATOM   6021 N  N   . ASN F 1 65  ? -55.860 -69.421 10.306 1.00 81.49  ? 65  ASN F N   1 
ATOM   6022 C  CA  . ASN F 1 65  ? -56.975 -69.570 9.393  1.00 83.61  ? 65  ASN F CA  1 
ATOM   6023 C  C   . ASN F 1 65  ? -56.790 -68.741 8.150  1.00 86.73  ? 65  ASN F C   1 
ATOM   6024 O  O   . ASN F 1 65  ? -57.427 -67.711 7.974  1.00 88.69  ? 65  ASN F O   1 
ATOM   6025 C  CB  . ASN F 1 65  ? -58.273 -69.200 10.107 1.00 83.61  ? 65  ASN F CB  1 
ATOM   6026 C  CG  . ASN F 1 65  ? -59.449 -69.453 9.265  1.00 85.05  ? 65  ASN F CG  1 
ATOM   6027 O  OD1 . ASN F 1 65  ? -59.339 -70.108 8.228  1.00 86.17  ? 65  ASN F OD1 1 
ATOM   6028 N  ND2 . ASN F 1 65  ? -60.591 -68.943 9.680  1.00 84.26  ? 65  ASN F ND2 1 
ATOM   6029 N  N   . PRO F 1 66  ? -55.914 -69.201 7.266  1.00 87.97  ? 66  PRO F N   1 
ATOM   6030 C  CA  . PRO F 1 66  ? -55.528 -68.415 6.099  1.00 91.39  ? 66  PRO F CA  1 
ATOM   6031 C  C   . PRO F 1 66  ? -56.563 -68.429 4.983  1.00 94.96  ? 66  PRO F C   1 
ATOM   6032 O  O   . PRO F 1 66  ? -56.553 -67.510 4.183  1.00 98.06  ? 66  PRO F O   1 
ATOM   6033 C  CB  . PRO F 1 66  ? -54.231 -69.087 5.635  1.00 91.06  ? 66  PRO F CB  1 
ATOM   6034 C  CG  . PRO F 1 66  ? -54.430 -70.494 5.975  1.00 89.40  ? 66  PRO F CG  1 
ATOM   6035 C  CD  . PRO F 1 66  ? -55.347 -70.552 7.206  1.00 86.80  ? 66  PRO F CD  1 
ATOM   6036 N  N   . LEU F 1 67  ? -57.428 -69.450 4.936  1.00 94.96  ? 67  LEU F N   1 
ATOM   6037 C  CA  . LEU F 1 67  ? -58.499 -69.504 3.961  1.00 98.51  ? 67  LEU F CA  1 
ATOM   6038 C  C   . LEU F 1 67  ? -59.817 -68.935 4.535  1.00 98.93  ? 67  LEU F C   1 
ATOM   6039 O  O   . LEU F 1 67  ? -60.846 -69.114 3.936  1.00 101.64 ? 67  LEU F O   1 
ATOM   6040 C  CB  . LEU F 1 67  ? -58.732 -70.939 3.481  1.00 99.02  ? 67  LEU F CB  1 
ATOM   6041 C  CG  . LEU F 1 67  ? -57.566 -71.884 3.174  1.00 98.71  ? 67  LEU F CG  1 
ATOM   6042 C  CD1 . LEU F 1 67  ? -57.949 -73.287 3.636  1.00 97.61  ? 67  LEU F CD1 1 
ATOM   6043 C  CD2 . LEU F 1 67  ? -57.155 -71.933 1.696  1.00 101.86 ? 67  LEU F CD2 1 
ATOM   6044 N  N   . SER F 1 68  ? -59.791 -68.264 5.686  1.00 96.87  ? 68  SER F N   1 
ATOM   6045 C  CA  . SER F 1 68  ? -60.990 -67.627 6.284  1.00 97.69  ? 68  SER F CA  1 
ATOM   6046 C  C   . SER F 1 68  ? -62.225 -68.511 6.442  1.00 98.08  ? 68  SER F C   1 
ATOM   6047 O  O   . SER F 1 68  ? -63.340 -68.054 6.241  1.00 100.62 ? 68  SER F O   1 
ATOM   6048 C  CB  . SER F 1 68  ? -61.368 -66.351 5.514  1.00 101.83 ? 68  SER F CB  1 
ATOM   6049 O  OG  . SER F 1 68  ? -60.476 -65.300 5.837  1.00 101.54 ? 68  SER F OG  1 
ATOM   6050 N  N   . ARG F 1 69  ? -62.025 -69.761 6.829  1.00 96.25  ? 69  ARG F N   1 
ATOM   6051 C  CA  . ARG F 1 69  ? -63.131 -70.700 7.039  1.00 97.17  ? 69  ARG F CA  1 
ATOM   6052 C  C   . ARG F 1 69  ? -63.673 -70.580 8.458  1.00 94.97  ? 69  ARG F C   1 
ATOM   6053 O  O   . ARG F 1 69  ? -63.135 -69.825 9.266  1.00 93.24  ? 69  ARG F O   1 
ATOM   6054 C  CB  . ARG F 1 69  ? -62.679 -72.143 6.807  1.00 96.41  ? 69  ARG F CB  1 
ATOM   6055 C  CG  . ARG F 1 69  ? -62.016 -72.408 5.470  1.00 100.42 ? 69  ARG F CG  1 
ATOM   6056 C  CD  . ARG F 1 69  ? -63.026 -72.510 4.338  1.00 107.51 ? 69  ARG F CD  1 
ATOM   6057 N  NE  . ARG F 1 69  ? -62.363 -72.803 3.058  1.00 112.39 ? 69  ARG F NE  1 
ATOM   6058 C  CZ  . ARG F 1 69  ? -61.934 -74.004 2.680  1.00 114.03 ? 69  ARG F CZ  1 
ATOM   6059 N  NH1 . ARG F 1 69  ? -62.103 -75.075 3.441  1.00 112.59 ? 69  ARG F NH1 1 
ATOM   6060 N  NH2 . ARG F 1 69  ? -61.333 -74.137 1.521  1.00 117.41 ? 69  ARG F NH2 1 
ATOM   6061 N  N   . LYS F 1 70  ? -64.751 -71.324 8.736  1.00 95.49  ? 70  LYS F N   1 
ATOM   6062 C  CA  . LYS F 1 70  ? -65.300 -71.456 10.090 1.00 93.59  ? 70  LYS F CA  1 
ATOM   6063 C  C   . LYS F 1 70  ? -64.582 -72.609 10.795 1.00 89.73  ? 70  LYS F C   1 
ATOM   6064 O  O   . LYS F 1 70  ? -64.098 -73.552 10.149 1.00 89.05  ? 70  LYS F O   1 
ATOM   6065 C  CB  . LYS F 1 70  ? -66.814 -71.736 10.084 1.00 96.41  ? 70  LYS F CB  1 
ATOM   6066 C  CG  . LYS F 1 70  ? -67.674 -70.930 9.090  1.00 102.10 ? 70  LYS F CG  1 
ATOM   6067 C  CD  . LYS F 1 70  ? -68.581 -69.830 9.724  1.00 105.84 ? 70  LYS F CD  1 
ATOM   6068 C  CE  . LYS F 1 70  ? -69.991 -69.810 8.983  1.00 111.80 ? 70  LYS F CE  1 
ATOM   6069 N  NZ  . LYS F 1 70  ? -70.915 -68.633 9.218  1.00 115.58 ? 70  LYS F NZ  1 
ATOM   6070 N  N   . HIS F 1 71  ? -64.530 -72.528 12.125 1.00 87.10  ? 71  HIS F N   1 
ATOM   6071 C  CA  . HIS F 1 71  ? -63.819 -73.523 12.925 1.00 84.05  ? 71  HIS F CA  1 
ATOM   6072 C  C   . HIS F 1 71  ? -64.446 -74.899 12.740 1.00 84.54  ? 71  HIS F C   1 
ATOM   6073 O  O   . HIS F 1 71  ? -65.639 -75.010 12.510 1.00 86.59  ? 71  HIS F O   1 
ATOM   6074 C  CB  . HIS F 1 71  ? -63.812 -73.135 14.406 1.00 82.31  ? 71  HIS F CB  1 
ATOM   6075 C  CG  . HIS F 1 71  ? -63.163 -74.147 15.294 1.00 79.55  ? 71  HIS F CG  1 
ATOM   6076 N  ND1 . HIS F 1 71  ? -61.801 -74.330 15.352 1.00 77.56  ? 71  HIS F ND1 1 
ATOM   6077 C  CD2 . HIS F 1 71  ? -63.697 -75.036 16.159 1.00 78.69  ? 71  HIS F CD2 1 
ATOM   6078 C  CE1 . HIS F 1 71  ? -61.526 -75.298 16.209 1.00 76.00  ? 71  HIS F CE1 1 
ATOM   6079 N  NE2 . HIS F 1 71  ? -62.660 -75.738 16.718 1.00 76.49  ? 71  HIS F NE2 1 
ATOM   6080 N  N   . GLY F 1 72  ? -63.626 -75.939 12.813 1.00 83.02  ? 72  GLY F N   1 
ATOM   6081 C  CA  . GLY F 1 72  ? -64.116 -77.298 12.724 1.00 83.96  ? 72  GLY F CA  1 
ATOM   6082 C  C   . GLY F 1 72  ? -63.163 -78.306 13.331 1.00 82.43  ? 72  GLY F C   1 
ATOM   6083 O  O   . GLY F 1 72  ? -62.140 -77.944 13.941 1.00 80.66  ? 72  GLY F O   1 
ATOM   6084 N  N   . GLY F 1 73  ? -63.517 -79.578 13.166 1.00 83.74  ? 73  GLY F N   1 
ATOM   6085 C  CA  . GLY F 1 73  ? -62.671 -80.689 13.584 1.00 82.95  ? 73  GLY F CA  1 
ATOM   6086 C  C   . GLY F 1 73  ? -61.666 -80.999 12.504 1.00 83.67  ? 73  GLY F C   1 
ATOM   6087 O  O   . GLY F 1 73  ? -61.818 -80.568 11.359 1.00 85.39  ? 73  GLY F O   1 
ATOM   6088 N  N   . PRO F 1 74  ? -60.644 -81.781 12.838 1.00 83.12  ? 74  PRO F N   1 
ATOM   6089 C  CA  . PRO F 1 74  ? -59.551 -81.872 11.883 1.00 83.82  ? 74  PRO F CA  1 
ATOM   6090 C  C   . PRO F 1 74  ? -59.959 -82.649 10.654 1.00 87.00  ? 74  PRO F C   1 
ATOM   6091 O  O   . PRO F 1 74  ? -59.505 -82.347 9.557  1.00 88.35  ? 74  PRO F O   1 
ATOM   6092 C  CB  . PRO F 1 74  ? -58.463 -82.602 12.662 1.00 82.62  ? 74  PRO F CB  1 
ATOM   6093 C  CG  . PRO F 1 74  ? -59.221 -83.459 13.642 1.00 83.03  ? 74  PRO F CG  1 
ATOM   6094 C  CD  . PRO F 1 74  ? -60.569 -82.813 13.880 1.00 82.72  ? 74  PRO F CD  1 
ATOM   6095 N  N   . LYS F 1 75  ? -60.823 -83.635 10.831 1.00 88.86  ? 75  LYS F N   1 
ATOM   6096 C  CA  . LYS F 1 75  ? -61.256 -84.431 9.705  1.00 92.90  ? 75  LYS F CA  1 
ATOM   6097 C  C   . LYS F 1 75  ? -62.459 -83.799 9.023  1.00 94.49  ? 75  LYS F C   1 
ATOM   6098 O  O   . LYS F 1 75  ? -62.865 -84.262 7.958  1.00 97.70  ? 75  LYS F O   1 
ATOM   6099 C  CB  . LYS F 1 75  ? -61.561 -85.847 10.147 1.00 94.58  ? 75  LYS F CB  1 
ATOM   6100 C  CG  . LYS F 1 75  ? -60.318 -86.608 10.663 1.00 96.70  ? 75  LYS F CG  1 
ATOM   6101 C  CD  . LYS F 1 75  ? -60.569 -88.133 10.777 1.00 102.98 ? 75  LYS F CD  1 
ATOM   6102 C  CE  . LYS F 1 75  ? -62.065 -88.444 11.216 1.00 106.03 ? 75  LYS F CE  1 
ATOM   6103 N  NZ  . LYS F 1 75  ? -62.528 -89.886 11.340 1.00 109.27 ? 75  LYS F NZ  1 
ATOM   6104 N  N   . ASP F 1 76  ? -63.019 -82.747 9.624  1.00 92.75  ? 76  ASP F N   1 
ATOM   6105 C  CA  . ASP F 1 76  ? -64.088 -81.979 8.994  1.00 94.65  ? 76  ASP F CA  1 
ATOM   6106 C  C   . ASP F 1 76  ? -63.518 -81.290 7.785  1.00 96.00  ? 76  ASP F C   1 
ATOM   6107 O  O   . ASP F 1 76  ? -62.312 -81.115 7.673  1.00 94.32  ? 76  ASP F O   1 
ATOM   6108 C  CB  . ASP F 1 76  ? -64.715 -80.942 9.947  1.00 92.99  ? 76  ASP F CB  1 
ATOM   6109 C  CG  . ASP F 1 76  ? -65.833 -81.540 10.831 1.00 94.35  ? 76  ASP F CG  1 
ATOM   6110 O  OD1 . ASP F 1 76  ? -66.700 -82.243 10.257 1.00 98.59  ? 76  ASP F OD1 1 
ATOM   6111 O  OD2 . ASP F 1 76  ? -65.859 -81.306 12.085 1.00 92.78  ? 76  ASP F OD2 1 
ATOM   6112 N  N   . GLU F 1 77  ? -64.403 -80.932 6.866  1.00 99.49  ? 77  GLU F N   1 
ATOM   6113 C  CA  . GLU F 1 77  ? -64.002 -80.298 5.620  1.00 102.08 ? 77  GLU F CA  1 
ATOM   6114 C  C   . GLU F 1 77  ? -63.944 -78.780 5.794  1.00 100.17 ? 77  GLU F C   1 
ATOM   6115 O  O   . GLU F 1 77  ? -62.939 -78.178 5.462  1.00 99.34  ? 77  GLU F O   1 
ATOM   6116 C  CB  . GLU F 1 77  ? -64.963 -80.666 4.490  1.00 107.47 ? 77  GLU F CB  1 
ATOM   6117 C  CG  . GLU F 1 77  ? -64.446 -80.209 3.088  1.00 113.40 ? 77  GLU F CG  1 
ATOM   6118 C  CD  . GLU F 1 77  ? -65.527 -79.423 2.270  1.00 121.98 ? 77  GLU F CD  1 
ATOM   6119 O  OE1 . GLU F 1 77  ? -66.505 -80.083 1.760  1.00 126.98 ? 77  GLU F OE1 1 
ATOM   6120 O  OE2 . GLU F 1 77  ? -65.394 -78.148 2.165  1.00 124.54 ? 77  GLU F OE2 1 
ATOM   6121 N  N   . GLU F 1 78  ? -65.023 -78.176 6.293  1.00 99.71  ? 78  GLU F N   1 
ATOM   6122 C  CA  . GLU F 1 78  ? -64.979 -76.785 6.756  1.00 98.04  ? 78  GLU F CA  1 
ATOM   6123 C  C   . GLU F 1 78  ? -64.220 -76.693 8.121  1.00 93.14  ? 78  GLU F C   1 
ATOM   6124 O  O   . GLU F 1 78  ? -64.772 -76.981 9.207  1.00 91.51  ? 78  GLU F O   1 
ATOM   6125 C  CB  . GLU F 1 78  ? -66.398 -76.185 6.858  1.00 100.32 ? 78  GLU F CB  1 
ATOM   6126 C  CG  . GLU F 1 78  ? -66.462 -74.670 7.236  1.00 100.89 ? 78  GLU F CG  1 
ATOM   6127 C  CD  . GLU F 1 78  ? -66.193 -73.716 6.067  1.00 105.55 ? 78  GLU F CD  1 
ATOM   6128 O  OE1 . GLU F 1 78  ? -65.620 -74.180 5.061  1.00 108.97 ? 78  GLU F OE1 1 
ATOM   6129 O  OE2 . GLU F 1 78  ? -66.547 -72.510 6.145  1.00 106.77 ? 78  GLU F OE2 1 
ATOM   6130 N  N   . ARG F 1 79  ? -62.952 -76.282 8.043  1.00 90.65  ? 79  ARG F N   1 
ATOM   6131 C  CA  . ARG F 1 79  ? -62.090 -76.131 9.212  1.00 86.57  ? 79  ARG F CA  1 
ATOM   6132 C  C   . ARG F 1 79  ? -61.011 -75.073 9.036  1.00 85.26  ? 79  ARG F C   1 
ATOM   6133 O  O   . ARG F 1 79  ? -60.662 -74.695 7.921  1.00 87.34  ? 79  ARG F O   1 
ATOM   6134 C  CB  . ARG F 1 79  ? -61.386 -77.448 9.504  1.00 85.33  ? 79  ARG F CB  1 
ATOM   6135 C  CG  . ARG F 1 79  ? -60.406 -77.875 8.413  1.00 87.26  ? 79  ARG F CG  1 
ATOM   6136 C  CD  . ARG F 1 79  ? -59.527 -79.071 8.796  1.00 86.84  ? 79  ARG F CD  1 
ATOM   6137 N  NE  . ARG F 1 79  ? -58.314 -78.685 9.520  1.00 84.89  ? 79  ARG F NE  1 
ATOM   6138 C  CZ  . ARG F 1 79  ? -57.236 -79.459 9.686  1.00 84.35  ? 79  ARG F CZ  1 
ATOM   6139 N  NH1 . ARG F 1 79  ? -57.184 -80.666 9.158  1.00 85.53  ? 79  ARG F NH1 1 
ATOM   6140 N  NH2 . ARG F 1 79  ? -56.189 -79.018 10.387 1.00 82.98  ? 79  ARG F NH2 1 
ATOM   6141 N  N   . HIS F 1 80  ? -60.446 -74.630 10.149 1.00 81.98  ? 80  HIS F N   1 
ATOM   6142 C  CA  . HIS F 1 80  ? -59.257 -73.791 10.113 1.00 80.42  ? 80  HIS F CA  1 
ATOM   6143 C  C   . HIS F 1 80  ? -58.050 -74.678 9.846  1.00 78.99  ? 80  HIS F C   1 
ATOM   6144 O  O   . HIS F 1 80  ? -57.965 -75.771 10.371 1.00 77.68  ? 80  HIS F O   1 
ATOM   6145 C  CB  . HIS F 1 80  ? -59.055 -73.067 11.435 1.00 78.17  ? 80  HIS F CB  1 
ATOM   6146 C  CG  . HIS F 1 80  ? -60.170 -72.141 11.806 1.00 79.28  ? 80  HIS F CG  1 
ATOM   6147 N  ND1 . HIS F 1 80  ? -60.383 -71.710 13.096 1.00 78.67  ? 80  HIS F ND1 1 
ATOM   6148 C  CD2 . HIS F 1 80  ? -61.125 -71.546 11.055 1.00 82.60  ? 80  HIS F CD2 1 
ATOM   6149 C  CE1 . HIS F 1 80  ? -61.405 -70.874 13.124 1.00 81.10  ? 80  HIS F CE1 1 
ATOM   6150 N  NE2 . HIS F 1 80  ? -61.880 -70.762 11.900 1.00 83.45  ? 80  HIS F NE2 1 
ATOM   6151 N  N   . VAL F 1 81  ? -57.117 -74.208 9.032  1.00 79.26  ? 81  VAL F N   1 
ATOM   6152 C  CA  . VAL F 1 81  ? -55.879 -74.942 8.808  1.00 78.18  ? 81  VAL F CA  1 
ATOM   6153 C  C   . VAL F 1 81  ? -55.266 -75.371 10.114 1.00 74.81  ? 81  VAL F C   1 
ATOM   6154 O  O   . VAL F 1 81  ? -54.676 -76.415 10.206 1.00 74.11  ? 81  VAL F O   1 
ATOM   6155 C  CB  . VAL F 1 81  ? -54.857 -74.119 8.012  1.00 79.52  ? 81  VAL F CB  1 
ATOM   6156 C  CG1 . VAL F 1 81  ? -53.539 -74.855 7.878  1.00 78.37  ? 81  VAL F CG1 1 
ATOM   6157 C  CG2 . VAL F 1 81  ? -55.417 -73.839 6.647  1.00 83.30  ? 81  VAL F CG2 1 
ATOM   6158 N  N   . GLY F 1 82  ? -55.420 -74.572 11.144 1.00 73.05  ? 82  GLY F N   1 
ATOM   6159 C  CA  . GLY F 1 82  ? -54.820 -74.904 12.441 1.00 71.03  ? 82  GLY F CA  1 
ATOM   6160 C  C   . GLY F 1 82  ? -55.615 -75.782 13.399 1.00 69.99  ? 82  GLY F C   1 
ATOM   6161 O  O   . GLY F 1 82  ? -55.218 -75.950 14.540 1.00 68.26  ? 82  GLY F O   1 
ATOM   6162 N  N   . ASP F 1 83  ? -56.743 -76.324 12.959 1.00 71.33  ? 83  ASP F N   1 
ATOM   6163 C  CA  . ASP F 1 83  ? -57.616 -77.070 13.856 1.00 71.01  ? 83  ASP F CA  1 
ATOM   6164 C  C   . ASP F 1 83  ? -57.195 -78.518 13.859 1.00 71.12  ? 83  ASP F C   1 
ATOM   6165 O  O   . ASP F 1 83  ? -57.538 -79.270 12.963 1.00 72.98  ? 83  ASP F O   1 
ATOM   6166 C  CB  . ASP F 1 83  ? -59.085 -76.984 13.419 1.00 72.61  ? 83  ASP F CB  1 
ATOM   6167 C  CG  . ASP F 1 83  ? -59.654 -75.586 13.521 1.00 73.24  ? 83  ASP F CG  1 
ATOM   6168 O  OD1 . ASP F 1 83  ? -59.204 -74.785 14.354 1.00 71.97  ? 83  ASP F OD1 1 
ATOM   6169 O  OD2 . ASP F 1 83  ? -60.578 -75.266 12.766 1.00 75.62  ? 83  ASP F OD2 1 
ATOM   6170 N  N   . LEU F 1 84  ? -56.447 -78.922 14.864 1.00 69.92  ? 84  LEU F N   1 
ATOM   6171 C  CA  . LEU F 1 84  ? -56.060 -80.312 14.968 1.00 70.45  ? 84  LEU F CA  1 
ATOM   6172 C  C   . LEU F 1 84  ? -56.951 -81.074 15.923 1.00 70.58  ? 84  LEU F C   1 
ATOM   6173 O  O   . LEU F 1 84  ? -56.623 -82.187 16.317 1.00 70.88  ? 84  LEU F O   1 
ATOM   6174 C  CB  . LEU F 1 84  ? -54.596 -80.406 15.370 1.00 69.79  ? 84  LEU F CB  1 
ATOM   6175 C  CG  . LEU F 1 84  ? -53.650 -79.717 14.370 1.00 69.93  ? 84  LEU F CG  1 
ATOM   6176 C  CD1 . LEU F 1 84  ? -52.249 -79.825 14.873 1.00 68.03  ? 84  LEU F CD1 1 
ATOM   6177 C  CD2 . LEU F 1 84  ? -53.754 -80.267 12.936 1.00 71.59  ? 84  LEU F CD2 1 
ATOM   6178 N  N   . GLY F 1 85  ? -58.104 -80.495 16.254 1.00 70.90  ? 85  GLY F N   1 
ATOM   6179 C  CA  . GLY F 1 85  ? -59.035 -81.101 17.203 1.00 71.37  ? 85  GLY F CA  1 
ATOM   6180 C  C   . GLY F 1 85  ? -58.533 -81.270 18.634 1.00 70.23  ? 85  GLY F C   1 
ATOM   6181 O  O   . GLY F 1 85  ? -58.102 -80.318 19.273 1.00 69.04  ? 85  GLY F O   1 
ATOM   6182 N  N   . ASN F 1 86  ? -58.583 -82.499 19.132 1.00 70.94  ? 86  ASN F N   1 
ATOM   6183 C  CA  . ASN F 1 86  ? -58.268 -82.757 20.515 1.00 70.83  ? 86  ASN F CA  1 
ATOM   6184 C  C   . ASN F 1 86  ? -57.147 -83.746 20.746 1.00 71.05  ? 86  ASN F C   1 
ATOM   6185 O  O   . ASN F 1 86  ? -56.750 -84.521 19.873 1.00 71.87  ? 86  ASN F O   1 
ATOM   6186 C  CB  . ASN F 1 86  ? -59.488 -83.303 21.219 1.00 72.33  ? 86  ASN F CB  1 
ATOM   6187 C  CG  . ASN F 1 86  ? -60.567 -82.300 21.342 1.00 72.89  ? 86  ASN F CG  1 
ATOM   6188 O  OD1 . ASN F 1 86  ? -60.513 -81.414 22.179 1.00 74.61  ? 86  ASN F OD1 1 
ATOM   6189 N  ND2 . ASN F 1 86  ? -61.574 -82.435 20.520 1.00 75.03  ? 86  ASN F ND2 1 
ATOM   6190 N  N   . VAL F 1 87  ? -56.658 -83.698 21.967 1.00 70.75  ? 87  VAL F N   1 
ATOM   6191 C  CA  . VAL F 1 87  ? -55.736 -84.674 22.467 1.00 71.69  ? 87  VAL F CA  1 
ATOM   6192 C  C   . VAL F 1 87  ? -56.296 -85.189 23.781 1.00 73.43  ? 87  VAL F C   1 
ATOM   6193 O  O   . VAL F 1 87  ? -57.127 -84.533 24.421 1.00 73.11  ? 87  VAL F O   1 
ATOM   6194 C  CB  . VAL F 1 87  ? -54.361 -84.039 22.669 1.00 70.65  ? 87  VAL F CB  1 
ATOM   6195 C  CG1 . VAL F 1 87  ? -53.931 -83.394 21.392 1.00 68.45  ? 87  VAL F CG1 1 
ATOM   6196 C  CG2 . VAL F 1 87  ? -54.392 -83.007 23.785 1.00 69.58  ? 87  VAL F CG2 1 
ATOM   6197 N  N   . THR F 1 88  ? -55.820 -86.349 24.201 1.00 75.59  ? 88  THR F N   1 
ATOM   6198 C  CA  . THR F 1 88  ? -56.430 -87.024 25.321 1.00 78.05  ? 88  THR F CA  1 
ATOM   6199 C  C   . THR F 1 88  ? -55.483 -87.273 26.484 1.00 79.44  ? 88  THR F C   1 
ATOM   6200 O  O   . THR F 1 88  ? -54.412 -87.835 26.305 1.00 80.22  ? 88  THR F O   1 
ATOM   6201 C  CB  . THR F 1 88  ? -56.992 -88.348 24.847 1.00 80.15  ? 88  THR F CB  1 
ATOM   6202 O  OG1 . THR F 1 88  ? -58.053 -88.079 23.928 1.00 79.74  ? 88  THR F OG1 1 
ATOM   6203 C  CG2 . THR F 1 88  ? -57.481 -89.195 26.048 1.00 83.35  ? 88  THR F CG2 1 
ATOM   6204 N  N   . ALA F 1 89  ? -55.913 -86.876 27.677 1.00 80.43  ? 89  ALA F N   1 
ATOM   6205 C  CA  . ALA F 1 89  ? -55.108 -86.986 28.864 1.00 82.42  ? 89  ALA F CA  1 
ATOM   6206 C  C   . ALA F 1 89  ? -55.464 -88.230 29.651 1.00 86.19  ? 89  ALA F C   1 
ATOM   6207 O  O   . ALA F 1 89  ? -56.641 -88.502 29.870 1.00 87.04  ? 89  ALA F O   1 
ATOM   6208 C  CB  . ALA F 1 89  ? -55.318 -85.769 29.727 1.00 81.84  ? 89  ALA F CB  1 
ATOM   6209 N  N   . ASP F 1 90  ? -54.417 -88.965 30.044 1.00 89.10  ? 90  ASP F N   1 
ATOM   6210 C  CA  . ASP F 1 90  ? -54.405 -89.976 31.119 1.00 93.57  ? 90  ASP F CA  1 
ATOM   6211 C  C   . ASP F 1 90  ? -55.302 -89.679 32.296 1.00 95.69  ? 90  ASP F C   1 
ATOM   6212 O  O   . ASP F 1 90  ? -55.803 -88.563 32.462 1.00 94.01  ? 90  ASP F O   1 
ATOM   6213 C  CB  . ASP F 1 90  ? -52.999 -90.025 31.757 1.00 95.32  ? 90  ASP F CB  1 
ATOM   6214 C  CG  . ASP F 1 90  ? -52.174 -91.224 31.345 1.00 98.91  ? 90  ASP F CG  1 
ATOM   6215 O  OD1 . ASP F 1 90  ? -52.591 -91.949 30.420 1.00 101.23 ? 90  ASP F OD1 1 
ATOM   6216 O  OD2 . ASP F 1 90  ? -51.090 -91.434 31.961 1.00 102.63 ? 90  ASP F OD2 1 
ATOM   6217 N  N   . LYS F 1 91  ? -55.450 -90.710 33.135 1.00 100.14 ? 91  LYS F N   1 
ATOM   6218 C  CA  . LYS F 1 91  ? -55.747 -90.552 34.578 1.00 103.51 ? 91  LYS F CA  1 
ATOM   6219 C  C   . LYS F 1 91  ? -54.743 -89.559 35.154 1.00 102.59 ? 91  LYS F C   1 
ATOM   6220 O  O   . LYS F 1 91  ? -55.099 -88.581 35.785 1.00 102.26 ? 91  LYS F O   1 
ATOM   6221 C  CB  . LYS F 1 91  ? -55.587 -91.906 35.317 1.00 108.50 ? 91  LYS F CB  1 
ATOM   6222 C  CG  . LYS F 1 91  ? -56.872 -92.702 35.589 1.00 112.81 ? 91  LYS F CG  1 
ATOM   6223 C  CD  . LYS F 1 91  ? -57.557 -92.276 36.898 1.00 117.79 ? 91  LYS F CD  1 
ATOM   6224 C  CE  . LYS F 1 91  ? -58.349 -93.438 37.533 1.00 123.42 ? 91  LYS F CE  1 
ATOM   6225 N  NZ  . LYS F 1 91  ? -59.625 -92.963 38.122 1.00 125.54 ? 91  LYS F NZ  1 
ATOM   6226 N  N   . ASP F 1 92  ? -53.479 -89.869 34.900 1.00 102.53 ? 92  ASP F N   1 
ATOM   6227 C  CA  . ASP F 1 92  ? -52.324 -89.158 35.408 1.00 102.84 ? 92  ASP F CA  1 
ATOM   6228 C  C   . ASP F 1 92  ? -52.094 -87.805 34.751 1.00 98.84  ? 92  ASP F C   1 
ATOM   6229 O  O   . ASP F 1 92  ? -51.088 -87.148 35.022 1.00 99.02  ? 92  ASP F O   1 
ATOM   6230 C  CB  . ASP F 1 92  ? -51.069 -90.013 35.175 1.00 104.69 ? 92  ASP F CB  1 
ATOM   6231 C  CG  . ASP F 1 92  ? -51.122 -91.355 35.882 1.00 110.36 ? 92  ASP F CG  1 
ATOM   6232 O  OD1 . ASP F 1 92  ? -50.059 -91.997 36.008 1.00 114.43 ? 92  ASP F OD1 1 
ATOM   6233 O  OD2 . ASP F 1 92  ? -52.216 -91.780 36.311 1.00 113.92 ? 92  ASP F OD2 1 
ATOM   6234 N  N   . GLY F 1 93  ? -52.980 -87.384 33.862 1.00 95.51  ? 93  GLY F N   1 
ATOM   6235 C  CA  . GLY F 1 93  ? -52.800 -86.098 33.215 1.00 92.11  ? 93  GLY F CA  1 
ATOM   6236 C  C   . GLY F 1 93  ? -51.683 -86.014 32.173 1.00 90.04  ? 93  GLY F C   1 
ATOM   6237 O  O   . GLY F 1 93  ? -51.331 -84.921 31.740 1.00 88.08  ? 93  GLY F O   1 
ATOM   6238 N  N   . VAL F 1 94  ? -51.118 -87.140 31.769 1.00 90.79  ? 94  VAL F N   1 
ATOM   6239 C  CA  . VAL F 1 94  ? -50.249 -87.166 30.610 1.00 89.24  ? 94  VAL F CA  1 
ATOM   6240 C  C   . VAL F 1 94  ? -51.055 -87.428 29.353 1.00 87.45  ? 94  VAL F C   1 
ATOM   6241 O  O   . VAL F 1 94  ? -51.842 -88.343 29.323 1.00 89.00  ? 94  VAL F O   1 
ATOM   6242 C  CB  . VAL F 1 94  ? -49.214 -88.284 30.749 1.00 92.11  ? 94  VAL F CB  1 
ATOM   6243 C  CG1 . VAL F 1 94  ? -48.402 -88.450 29.445 1.00 90.30  ? 94  VAL F CG1 1 
ATOM   6244 C  CG2 . VAL F 1 94  ? -48.321 -88.024 31.956 1.00 94.78  ? 94  VAL F CG2 1 
ATOM   6245 N  N   . ALA F 1 95  ? -50.851 -86.652 28.304 1.00 85.02  ? 95  ALA F N   1 
ATOM   6246 C  CA  . ALA F 1 95  ? -51.466 -86.957 27.014 1.00 83.95  ? 95  ALA F CA  1 
ATOM   6247 C  C   . ALA F 1 95  ? -50.415 -87.393 26.006 1.00 84.53  ? 95  ALA F C   1 
ATOM   6248 O  O   . ALA F 1 95  ? -49.478 -86.657 25.749 1.00 83.69  ? 95  ALA F O   1 
ATOM   6249 C  CB  . ALA F 1 95  ? -52.189 -85.765 26.503 1.00 81.28  ? 95  ALA F CB  1 
ATOM   6250 N  N   . ASP F 1 96  ? -50.567 -88.583 25.436 1.00 86.64  ? 96  ASP F N   1 
ATOM   6251 C  CA  . ASP F 1 96  ? -49.599 -89.087 24.458 1.00 88.15  ? 96  ASP F CA  1 
ATOM   6252 C  C   . ASP F 1 96  ? -50.099 -88.754 23.087 1.00 85.93  ? 96  ASP F C   1 
ATOM   6253 O  O   . ASP F 1 96  ? -50.885 -89.482 22.505 1.00 87.22  ? 96  ASP F O   1 
ATOM   6254 C  CB  . ASP F 1 96  ? -49.390 -90.609 24.562 1.00 92.07  ? 96  ASP F CB  1 
ATOM   6255 C  CG  . ASP F 1 96  ? -48.368 -90.994 25.603 1.00 96.87  ? 96  ASP F CG  1 
ATOM   6256 O  OD1 . ASP F 1 96  ? -47.302 -90.307 25.646 1.00 98.29  ? 96  ASP F OD1 1 
ATOM   6257 O  OD2 . ASP F 1 96  ? -48.643 -91.979 26.364 1.00 102.18 ? 96  ASP F OD2 1 
ATOM   6258 N  N   . VAL F 1 97  ? -49.616 -87.653 22.558 1.00 83.32  ? 97  VAL F N   1 
ATOM   6259 C  CA  . VAL F 1 97  ? -50.080 -87.173 21.284 1.00 81.38  ? 97  VAL F CA  1 
ATOM   6260 C  C   . VAL F 1 97  ? -49.550 -87.993 20.117 1.00 82.59  ? 97  VAL F C   1 
ATOM   6261 O  O   . VAL F 1 97  ? -48.379 -88.356 20.105 1.00 84.10  ? 97  VAL F O   1 
ATOM   6262 C  CB  . VAL F 1 97  ? -49.619 -85.761 21.085 1.00 79.25  ? 97  VAL F CB  1 
ATOM   6263 C  CG1 . VAL F 1 97  ? -49.835 -85.349 19.668 1.00 79.08  ? 97  VAL F CG1 1 
ATOM   6264 C  CG2 . VAL F 1 97  ? -50.360 -84.861 22.028 1.00 78.13  ? 97  VAL F CG2 1 
ATOM   6265 N  N   . SER F 1 98  ? -50.406 -88.266 19.129 1.00 82.16  ? 98  SER F N   1 
ATOM   6266 C  CA  . SER F 1 98  ? -49.950 -88.883 17.878 1.00 83.61  ? 98  SER F CA  1 
ATOM   6267 C  C   . SER F 1 98  ? -50.975 -88.699 16.795 1.00 83.06  ? 98  SER F C   1 
ATOM   6268 O  O   . SER F 1 98  ? -52.035 -89.218 16.915 1.00 83.54  ? 98  SER F O   1 
ATOM   6269 C  CB  . SER F 1 98  ? -49.681 -90.368 18.084 1.00 86.70  ? 98  SER F CB  1 
ATOM   6270 O  OG  . SER F 1 98  ? -49.210 -90.967 16.900 1.00 88.80  ? 98  SER F OG  1 
ATOM   6271 N  N   . ILE F 1 99  ? -50.635 -87.982 15.733 1.00 82.61  ? 99  ILE F N   1 
ATOM   6272 C  CA  . ILE F 1 99  ? -51.604 -87.473 14.753 1.00 82.32  ? 99  ILE F CA  1 
ATOM   6273 C  C   . ILE F 1 99  ? -51.006 -87.420 13.353 1.00 84.79  ? 99  ILE F C   1 
ATOM   6274 O  O   . ILE F 1 99  ? -49.877 -87.002 13.199 1.00 85.24  ? 99  ILE F O   1 
ATOM   6275 C  CB  . ILE F 1 99  ? -52.001 -85.989 15.083 1.00 78.95  ? 99  ILE F CB  1 
ATOM   6276 C  CG1 . ILE F 1 99  ? -52.620 -85.868 16.480 1.00 76.74  ? 99  ILE F CG1 1 
ATOM   6277 C  CG2 . ILE F 1 99  ? -52.955 -85.406 14.021 1.00 78.76  ? 99  ILE F CG2 1 
ATOM   6278 C  CD1 . ILE F 1 99  ? -53.456 -84.608 16.687 1.00 73.28  ? 99  ILE F CD1 1 
ATOM   6279 N  N   . GLU F 1 100 ? -51.757 -87.823 12.333 1.00 87.26  ? 100 GLU F N   1 
ATOM   6280 C  CA  . GLU F 1 100 ? -51.399 -87.482 10.965 1.00 89.45  ? 100 GLU F CA  1 
ATOM   6281 C  C   . GLU F 1 100 ? -52.346 -86.444 10.487 1.00 88.02  ? 100 GLU F C   1 
ATOM   6282 O  O   . GLU F 1 100 ? -53.516 -86.505 10.810 1.00 87.78  ? 100 GLU F O   1 
ATOM   6283 C  CB  . GLU F 1 100 ? -51.564 -88.658 10.041 1.00 93.85  ? 100 GLU F CB  1 
ATOM   6284 C  CG  . GLU F 1 100 ? -50.407 -89.627 10.077 1.00 98.75  ? 100 GLU F CG  1 
ATOM   6285 C  CD  . GLU F 1 100 ? -50.089 -90.227 8.709  1.00 106.40 ? 100 GLU F CD  1 
ATOM   6286 O  OE1 . GLU F 1 100 ? -50.659 -89.767 7.665  1.00 108.98 ? 100 GLU F OE1 1 
ATOM   6287 O  OE2 . GLU F 1 100 ? -49.233 -91.148 8.703  1.00 111.41 ? 100 GLU F OE2 1 
ATOM   6288 N  N   . ASP F 1 101 ? -51.876 -85.500 9.698  1.00 87.84  ? 101 ASP F N   1 
ATOM   6289 C  CA  . ASP F 1 101 ? -52.769 -84.485 9.172  1.00 87.31  ? 101 ASP F CA  1 
ATOM   6290 C  C   . ASP F 1 101 ? -52.151 -83.933 7.940  1.00 89.02  ? 101 ASP F C   1 
ATOM   6291 O  O   . ASP F 1 101 ? -50.926 -83.781 7.901  1.00 89.43  ? 101 ASP F O   1 
ATOM   6292 C  CB  . ASP F 1 101 ? -52.928 -83.348 10.167 1.00 84.25  ? 101 ASP F CB  1 
ATOM   6293 C  CG  . ASP F 1 101 ? -54.018 -82.380 9.761  1.00 85.38  ? 101 ASP F CG  1 
ATOM   6294 O  OD1 . ASP F 1 101 ? -55.189 -82.648 10.110 1.00 87.21  ? 101 ASP F OD1 1 
ATOM   6295 O  OD2 . ASP F 1 101 ? -53.719 -81.354 9.097  1.00 87.52  ? 101 ASP F OD2 1 
ATOM   6296 N  N   . SER F 1 102 ? -52.966 -83.614 6.937  1.00 90.38  ? 102 SER F N   1 
ATOM   6297 C  CA  . SER F 1 102 ? -52.416 -83.128 5.660  1.00 92.91  ? 102 SER F CA  1 
ATOM   6298 C  C   . SER F 1 102 ? -53.008 -81.817 5.197  1.00 92.22  ? 102 SER F C   1 
ATOM   6299 O  O   . SER F 1 102 ? -52.819 -81.422 4.044  1.00 94.99  ? 102 SER F O   1 
ATOM   6300 C  CB  . SER F 1 102 ? -52.604 -84.190 4.595  1.00 97.22  ? 102 SER F CB  1 
ATOM   6301 O  OG  . SER F 1 102 ? -53.715 -84.976 4.964  1.00 98.37  ? 102 SER F OG  1 
ATOM   6302 N  N   . VAL F 1 103 ? -53.719 -81.142 6.096  1.00 88.92  ? 103 VAL F N   1 
ATOM   6303 C  CA  . VAL F 1 103 ? -54.107 -79.753 5.869  1.00 88.17  ? 103 VAL F CA  1 
ATOM   6304 C  C   . VAL F 1 103 ? -52.930 -78.826 6.213  1.00 86.51  ? 103 VAL F C   1 
ATOM   6305 O  O   . VAL F 1 103 ? -52.631 -77.879 5.465  1.00 88.15  ? 103 VAL F O   1 
ATOM   6306 C  CB  . VAL F 1 103 ? -55.340 -79.345 6.691  1.00 85.86  ? 103 VAL F CB  1 
ATOM   6307 C  CG1 . VAL F 1 103 ? -55.467 -77.837 6.712  1.00 85.13  ? 103 VAL F CG1 1 
ATOM   6308 C  CG2 . VAL F 1 103 ? -56.581 -79.943 6.115  1.00 88.11  ? 103 VAL F CG2 1 
ATOM   6309 N  N   . ILE F 1 104 ? -52.273 -79.094 7.337  1.00 83.58  ? 104 ILE F N   1 
ATOM   6310 C  CA  . ILE F 1 104 ? -51.073 -78.351 7.701  1.00 82.42  ? 104 ILE F CA  1 
ATOM   6311 C  C   . ILE F 1 104 ? -49.885 -78.854 6.898  1.00 85.24  ? 104 ILE F C   1 
ATOM   6312 O  O   . ILE F 1 104 ? -49.928 -79.964 6.337  1.00 87.33  ? 104 ILE F O   1 
ATOM   6313 C  CB  . ILE F 1 104 ? -50.743 -78.449 9.201  1.00 79.19  ? 104 ILE F CB  1 
ATOM   6314 C  CG1 . ILE F 1 104 ? -50.368 -79.881 9.582  1.00 79.13  ? 104 ILE F CG1 1 
ATOM   6315 C  CG2 . ILE F 1 104 ? -51.910 -77.955 10.027 1.00 76.78  ? 104 ILE F CG2 1 
ATOM   6316 C  CD1 . ILE F 1 104 ? -50.173 -80.081 11.017 1.00 76.19  ? 104 ILE F CD1 1 
ATOM   6317 N  N   . SER F 1 105 ? -48.831 -78.032 6.868  1.00 85.64  ? 105 SER F N   1 
ATOM   6318 C  CA  . SER F 1 105 ? -47.621 -78.304 6.088  1.00 88.76  ? 105 SER F CA  1 
ATOM   6319 C  C   . SER F 1 105 ? -46.456 -77.640 6.798  1.00 87.65  ? 105 SER F C   1 
ATOM   6320 O  O   . SER F 1 105 ? -46.655 -76.691 7.547  1.00 85.15  ? 105 SER F O   1 
ATOM   6321 C  CB  . SER F 1 105 ? -47.774 -77.748 4.647  1.00 92.38  ? 105 SER F CB  1 
ATOM   6322 O  OG  . SER F 1 105 ? -46.889 -78.372 3.695  1.00 95.92  ? 105 SER F OG  1 
ATOM   6323 N  N   . LEU F 1 106 ? -45.249 -78.147 6.576  1.00 89.96  ? 106 LEU F N   1 
ATOM   6324 C  CA  . LEU F 1 106 ? -44.036 -77.471 7.048  1.00 90.30  ? 106 LEU F CA  1 
ATOM   6325 C  C   . LEU F 1 106 ? -43.405 -76.574 5.972  1.00 94.14  ? 106 LEU F C   1 
ATOM   6326 O  O   . LEU F 1 106 ? -42.491 -75.787 6.247  1.00 94.40  ? 106 LEU F O   1 
ATOM   6327 C  CB  . LEU F 1 106 ? -43.018 -78.495 7.563  1.00 90.61  ? 106 LEU F CB  1 
ATOM   6328 C  CG  . LEU F 1 106 ? -43.502 -79.388 8.705  1.00 87.07  ? 106 LEU F CG  1 
ATOM   6329 C  CD1 . LEU F 1 106 ? -42.307 -79.963 9.473  1.00 86.22  ? 106 LEU F CD1 1 
ATOM   6330 C  CD2 . LEU F 1 106 ? -44.426 -78.621 9.641  1.00 82.65  ? 106 LEU F CD2 1 
ATOM   6331 N  N   . SER F 1 107 ? -43.902 -76.713 4.747  1.00 97.99  ? 107 SER F N   1 
ATOM   6332 C  CA  . SER F 1 107 ? -43.533 -75.859 3.619  1.00 101.97 ? 107 SER F CA  1 
ATOM   6333 C  C   . SER F 1 107 ? -44.819 -75.336 2.974  1.00 103.20 ? 107 SER F C   1 
ATOM   6334 O  O   . SER F 1 107 ? -45.927 -75.673 3.379  1.00 101.54 ? 107 SER F O   1 
ATOM   6335 C  CB  . SER F 1 107 ? -42.707 -76.666 2.600  1.00 106.30 ? 107 SER F CB  1 
ATOM   6336 O  OG  . SER F 1 107 ? -43.384 -77.874 2.220  1.00 107.36 ? 107 SER F OG  1 
ATOM   6337 N  N   . GLY F 1 108 ? -44.688 -74.504 1.962  1.00 107.16 ? 108 GLY F N   1 
ATOM   6338 C  CA  . GLY F 1 108 ? -45.873 -73.980 1.285  1.00 108.87 ? 108 GLY F CA  1 
ATOM   6339 C  C   . GLY F 1 108 ? -46.488 -72.874 2.113  1.00 106.24 ? 108 GLY F C   1 
ATOM   6340 O  O   . GLY F 1 108 ? -45.888 -72.429 3.102  1.00 103.74 ? 108 GLY F O   1 
ATOM   6341 N  N   . ASP F 1 109 ? -47.677 -72.422 1.712  1.00 107.33 ? 109 ASP F N   1 
ATOM   6342 C  CA  . ASP F 1 109 ? -48.337 -71.260 2.394  1.00 105.72 ? 109 ASP F CA  1 
ATOM   6343 C  C   . ASP F 1 109 ? -49.366 -71.704 3.454  1.00 101.46 ? 109 ASP F C   1 
ATOM   6344 O  O   . ASP F 1 109 ? -50.126 -70.893 3.992  1.00 99.62  ? 109 ASP F O   1 
ATOM   6345 C  CB  . ASP F 1 109 ? -48.947 -70.242 1.395  1.00 109.53 ? 109 ASP F CB  1 
ATOM   6346 C  CG  . ASP F 1 109 ? -49.569 -70.914 0.163  1.00 115.01 ? 109 ASP F CG  1 
ATOM   6347 O  OD1 . ASP F 1 109 ? -48.986 -70.723 -0.947 1.00 120.19 ? 109 ASP F OD1 1 
ATOM   6348 O  OD2 . ASP F 1 109 ? -50.610 -71.637 0.308  1.00 116.09 ? 109 ASP F OD2 1 
ATOM   6349 N  N   . HIS F 1 110 ? -49.380 -73.013 3.716  1.00 99.85  ? 110 HIS F N   1 
ATOM   6350 C  CA  . HIS F 1 110 ? -49.949 -73.552 4.942  1.00 95.88  ? 110 HIS F CA  1 
ATOM   6351 C  C   . HIS F 1 110 ? -48.806 -73.845 5.929  1.00 92.38  ? 110 HIS F C   1 
ATOM   6352 O  O   . HIS F 1 110 ? -49.019 -74.538 6.920  1.00 89.89  ? 110 HIS F O   1 
ATOM   6353 C  CB  . HIS F 1 110 ? -50.759 -74.840 4.663  1.00 96.91  ? 110 HIS F CB  1 
ATOM   6354 C  CG  . HIS F 1 110 ? -52.018 -74.621 3.860  1.00 101.40 ? 110 HIS F CG  1 
ATOM   6355 N  ND1 . HIS F 1 110 ? -53.025 -75.569 3.774  1.00 103.49 ? 110 HIS F ND1 1 
ATOM   6356 C  CD2 . HIS F 1 110 ? -52.430 -73.564 3.108  1.00 105.53 ? 110 HIS F CD2 1 
ATOM   6357 C  CE1 . HIS F 1 110 ? -53.991 -75.110 2.994  1.00 106.75 ? 110 HIS F CE1 1 
ATOM   6358 N  NE2 . HIS F 1 110 ? -53.656 -73.897 2.577  1.00 108.29 ? 110 HIS F NE2 1 
ATOM   6359 N  N   . CYS F 1 111 ? -47.602 -73.331 5.652  1.00 92.03  ? 111 CYS F N   1 
ATOM   6360 C  CA  . CYS F 1 111 ? -46.442 -73.544 6.519  1.00 89.02  ? 111 CYS F CA  1 
ATOM   6361 C  C   . CYS F 1 111 ? -46.784 -73.007 7.920  1.00 84.81  ? 111 CYS F C   1 
ATOM   6362 O  O   . CYS F 1 111 ? -47.281 -71.885 8.059  1.00 84.34  ? 111 CYS F O   1 
ATOM   6363 C  CB  . CYS F 1 111 ? -45.208 -72.852 5.940  1.00 91.28  ? 111 CYS F CB  1 
ATOM   6364 S  SG  . CYS F 1 111 ? -43.792 -72.866 7.019  1.00 88.33  ? 111 CYS F SG  1 
ATOM   6365 N  N   . ILE F 1 112 ? -46.587 -73.841 8.940  1.00 81.45  ? 112 ILE F N   1 
ATOM   6366 C  CA  . ILE F 1 112 ? -46.944 -73.484 10.320 1.00 77.66  ? 112 ILE F CA  1 
ATOM   6367 C  C   . ILE F 1 112 ? -45.724 -73.176 11.162 1.00 76.86  ? 112 ILE F C   1 
ATOM   6368 O  O   . ILE F 1 112 ? -45.814 -72.940 12.363 1.00 74.87  ? 112 ILE F O   1 
ATOM   6369 C  CB  . ILE F 1 112 ? -47.741 -74.609 11.022 1.00 75.62  ? 112 ILE F CB  1 
ATOM   6370 C  CG1 . ILE F 1 112 ? -46.903 -75.859 11.221 1.00 74.71  ? 112 ILE F CG1 1 
ATOM   6371 C  CG2 . ILE F 1 112 ? -48.979 -74.975 10.234 1.00 76.55  ? 112 ILE F CG2 1 
ATOM   6372 C  CD1 . ILE F 1 112 ? -47.590 -76.839 12.086 1.00 71.05  ? 112 ILE F CD1 1 
ATOM   6373 N  N   . ILE F 1 113 ? -44.567 -73.204 10.527 1.00 78.49  ? 113 ILE F N   1 
ATOM   6374 C  CA  . ILE F 1 113 ? -43.338 -72.919 11.229 1.00 78.17  ? 113 ILE F CA  1 
ATOM   6375 C  C   . ILE F 1 113 ? -43.395 -71.477 11.620 1.00 77.48  ? 113 ILE F C   1 
ATOM   6376 O  O   . ILE F 1 113 ? -43.716 -70.614 10.797 1.00 78.67  ? 113 ILE F O   1 
ATOM   6377 C  CB  . ILE F 1 113 ? -42.119 -73.221 10.352 1.00 80.95  ? 113 ILE F CB  1 
ATOM   6378 C  CG1 . ILE F 1 113 ? -41.871 -74.725 10.377 1.00 81.32  ? 113 ILE F CG1 1 
ATOM   6379 C  CG2 . ILE F 1 113 ? -40.887 -72.502 10.850 1.00 81.78  ? 113 ILE F CG2 1 
ATOM   6380 C  CD1 . ILE F 1 113 ? -40.793 -75.175 9.467  1.00 85.97  ? 113 ILE F CD1 1 
ATOM   6381 N  N   . GLY F 1 114 ? -43.143 -71.216 12.888 1.00 75.70  ? 114 GLY F N   1 
ATOM   6382 C  CA  . GLY F 1 114 ? -43.137 -69.846 13.370 1.00 75.87  ? 114 GLY F CA  1 
ATOM   6383 C  C   . GLY F 1 114 ? -44.458 -69.409 13.959 1.00 74.18  ? 114 GLY F C   1 
ATOM   6384 O  O   . GLY F 1 114 ? -44.647 -68.248 14.305 1.00 74.51  ? 114 GLY F O   1 
ATOM   6385 N  N   . ARG F 1 115 ? -45.375 -70.348 14.099 1.00 72.68  ? 115 ARG F N   1 
ATOM   6386 C  CA  . ARG F 1 115 ? -46.681 -70.048 14.635 1.00 71.42  ? 115 ARG F CA  1 
ATOM   6387 C  C   . ARG F 1 115 ? -46.847 -70.771 15.946 1.00 69.70  ? 115 ARG F C   1 
ATOM   6388 O  O   . ARG F 1 115 ? -46.173 -71.748 16.193 1.00 69.70  ? 115 ARG F O   1 
ATOM   6389 C  CB  . ARG F 1 115 ? -47.725 -70.478 13.626 1.00 71.68  ? 115 ARG F CB  1 
ATOM   6390 C  CG  . ARG F 1 115 ? -47.476 -69.882 12.241 1.00 74.15  ? 115 ARG F CG  1 
ATOM   6391 C  CD  . ARG F 1 115 ? -48.655 -70.085 11.321 1.00 75.45  ? 115 ARG F CD  1 
ATOM   6392 N  NE  . ARG F 1 115 ? -48.425 -69.498 10.014 1.00 78.17  ? 115 ARG F NE  1 
ATOM   6393 C  CZ  . ARG F 1 115 ? -48.651 -68.225 9.709  1.00 80.56  ? 115 ARG F CZ  1 
ATOM   6394 N  NH1 . ARG F 1 115 ? -49.121 -67.369 10.607 1.00 80.93  ? 115 ARG F NH1 1 
ATOM   6395 N  NH2 . ARG F 1 115 ? -48.404 -67.803 8.485  1.00 83.53  ? 115 ARG F NH2 1 
ATOM   6396 N  N   . THR F 1 116 ? -47.721 -70.282 16.805 1.00 68.90  ? 116 THR F N   1 
ATOM   6397 C  CA  . THR F 1 116 ? -47.824 -70.857 18.121 1.00 68.09  ? 116 THR F CA  1 
ATOM   6398 C  C   . THR F 1 116 ? -48.720 -72.064 18.072 1.00 66.50  ? 116 THR F C   1 
ATOM   6399 O  O   . THR F 1 116 ? -49.732 -72.055 17.410 1.00 66.32  ? 116 THR F O   1 
ATOM   6400 C  CB  . THR F 1 116 ? -48.355 -69.863 19.149 1.00 68.49  ? 116 THR F CB  1 
ATOM   6401 O  OG1 . THR F 1 116 ? -47.522 -68.704 19.186 1.00 71.10  ? 116 THR F OG1 1 
ATOM   6402 C  CG2 . THR F 1 116 ? -48.341 -70.476 20.518 1.00 69.12  ? 116 THR F CG2 1 
ATOM   6403 N  N   . LEU F 1 117 ? -48.287 -73.117 18.746 1.00 65.93  ? 117 LEU F N   1 
ATOM   6404 C  CA  . LEU F 1 117 ? -49.097 -74.283 19.020 1.00 65.22  ? 117 LEU F CA  1 
ATOM   6405 C  C   . LEU F 1 117 ? -49.695 -74.108 20.393 1.00 65.24  ? 117 LEU F C   1 
ATOM   6406 O  O   . LEU F 1 117 ? -49.011 -73.672 21.294 1.00 66.38  ? 117 LEU F O   1 
ATOM   6407 C  CB  . LEU F 1 117 ? -48.209 -75.508 19.045 1.00 65.36  ? 117 LEU F CB  1 
ATOM   6408 C  CG  . LEU F 1 117 ? -48.903 -76.816 19.301 1.00 64.09  ? 117 LEU F CG  1 
ATOM   6409 C  CD1 . LEU F 1 117 ? -49.838 -77.077 18.188 1.00 63.98  ? 117 LEU F CD1 1 
ATOM   6410 C  CD2 . LEU F 1 117 ? -47.885 -77.872 19.357 1.00 63.72  ? 117 LEU F CD2 1 
ATOM   6411 N  N   . VAL F 1 118 ? -50.951 -74.469 20.590 1.00 64.95  ? 118 VAL F N   1 
ATOM   6412 C  CA  . VAL F 1 118 ? -51.592 -74.210 21.870 1.00 65.31  ? 118 VAL F CA  1 
ATOM   6413 C  C   . VAL F 1 118 ? -52.425 -75.388 22.303 1.00 65.38  ? 118 VAL F C   1 
ATOM   6414 O  O   . VAL F 1 118 ? -53.112 -75.982 21.489 1.00 65.22  ? 118 VAL F O   1 
ATOM   6415 C  CB  . VAL F 1 118 ? -52.511 -73.024 21.772 1.00 65.58  ? 118 VAL F CB  1 
ATOM   6416 C  CG1 . VAL F 1 118 ? -53.179 -72.755 23.091 1.00 66.32  ? 118 VAL F CG1 1 
ATOM   6417 C  CG2 . VAL F 1 118 ? -51.734 -71.831 21.348 1.00 66.61  ? 118 VAL F CG2 1 
ATOM   6418 N  N   . VAL F 1 119 ? -52.358 -75.726 23.590 1.00 66.26  ? 119 VAL F N   1 
ATOM   6419 C  CA  . VAL F 1 119 ? -53.220 -76.750 24.184 1.00 66.79  ? 119 VAL F CA  1 
ATOM   6420 C  C   . VAL F 1 119 ? -54.134 -76.068 25.185 1.00 68.32  ? 119 VAL F C   1 
ATOM   6421 O  O   . VAL F 1 119 ? -53.699 -75.165 25.900 1.00 69.26  ? 119 VAL F O   1 
ATOM   6422 C  CB  . VAL F 1 119 ? -52.417 -77.826 24.887 1.00 67.18  ? 119 VAL F CB  1 
ATOM   6423 C  CG1 . VAL F 1 119 ? -51.582 -77.213 25.961 1.00 68.24  ? 119 VAL F CG1 1 
ATOM   6424 C  CG2 . VAL F 1 119 ? -53.332 -78.855 25.484 1.00 67.67  ? 119 VAL F CG2 1 
ATOM   6425 N  N   . HIS F 1 120 ? -55.389 -76.500 25.237 1.00 69.35  ? 120 HIS F N   1 
ATOM   6426 C  CA  . HIS F 1 120 ? -56.426 -75.708 25.853 1.00 71.11  ? 120 HIS F CA  1 
ATOM   6427 C  C   . HIS F 1 120 ? -57.021 -76.333 27.077 1.00 73.10  ? 120 HIS F C   1 
ATOM   6428 O  O   . HIS F 1 120 ? -56.838 -77.509 27.335 1.00 73.19  ? 120 HIS F O   1 
ATOM   6429 C  CB  . HIS F 1 120 ? -57.554 -75.484 24.869 1.00 71.09  ? 120 HIS F CB  1 
ATOM   6430 C  CG  . HIS F 1 120 ? -57.274 -74.434 23.849 1.00 71.84  ? 120 HIS F CG  1 
ATOM   6431 N  ND1 . HIS F 1 120 ? -57.838 -73.175 23.899 1.00 75.08  ? 120 HIS F ND1 1 
ATOM   6432 C  CD2 . HIS F 1 120 ? -56.519 -74.467 22.726 1.00 72.06  ? 120 HIS F CD2 1 
ATOM   6433 C  CE1 . HIS F 1 120 ? -57.433 -72.477 22.853 1.00 75.86  ? 120 HIS F CE1 1 
ATOM   6434 N  NE2 . HIS F 1 120 ? -56.630 -73.237 22.127 1.00 73.72  ? 120 HIS F NE2 1 
ATOM   6435 N  N   . GLU F 1 121 ? -57.789 -75.515 27.795 1.00 75.35  ? 121 GLU F N   1 
ATOM   6436 C  CA  . GLU F 1 121 ? -58.431 -75.890 29.055 1.00 77.94  ? 121 GLU F CA  1 
ATOM   6437 C  C   . GLU F 1 121 ? -59.384 -77.038 28.906 1.00 77.97  ? 121 GLU F C   1 
ATOM   6438 O  O   . GLU F 1 121 ? -59.253 -77.990 29.625 1.00 78.80  ? 121 GLU F O   1 
ATOM   6439 C  CB  . GLU F 1 121 ? -59.181 -74.695 29.649 1.00 80.22  ? 121 GLU F CB  1 
ATOM   6440 C  CG  . GLU F 1 121 ? -59.643 -74.914 31.097 1.00 84.86  ? 121 GLU F CG  1 
ATOM   6441 C  CD  . GLU F 1 121 ? -60.466 -73.772 31.655 1.00 89.94  ? 121 GLU F CD  1 
ATOM   6442 O  OE1 . GLU F 1 121 ? -61.059 -72.971 30.879 1.00 90.72  ? 121 GLU F OE1 1 
ATOM   6443 O  OE2 . GLU F 1 121 ? -60.518 -73.685 32.896 1.00 94.10  ? 121 GLU F OE2 1 
ATOM   6444 N  N   . LYS F 1 122 ? -60.335 -76.934 27.983 1.00 77.67  ? 122 LYS F N   1 
ATOM   6445 C  CA  . LYS F 1 122 ? -61.371 -77.952 27.792 1.00 78.97  ? 122 LYS F CA  1 
ATOM   6446 C  C   . LYS F 1 122 ? -61.293 -78.606 26.427 1.00 77.12  ? 122 LYS F C   1 
ATOM   6447 O  O   . LYS F 1 122 ? -60.380 -78.361 25.650 1.00 75.76  ? 122 LYS F O   1 
ATOM   6448 C  CB  . LYS F 1 122 ? -62.775 -77.358 27.901 1.00 81.10  ? 122 LYS F CB  1 
ATOM   6449 C  CG  . LYS F 1 122 ? -62.953 -76.219 28.875 1.00 84.68  ? 122 LYS F CG  1 
ATOM   6450 C  CD  . LYS F 1 122 ? -64.398 -75.695 28.820 1.00 88.79  ? 122 LYS F CD  1 
ATOM   6451 C  CE  . LYS F 1 122 ? -64.447 -74.189 29.006 1.00 91.04  ? 122 LYS F CE  1 
ATOM   6452 N  NZ  . LYS F 1 122 ? -65.839 -73.665 29.133 1.00 94.53  ? 122 LYS F NZ  1 
ATOM   6453 N  N   . ALA F 1 123 ? -62.288 -79.431 26.135 1.00 77.52  ? 123 ALA F N   1 
ATOM   6454 C  CA  . ALA F 1 123 ? -62.384 -80.074 24.842 1.00 76.32  ? 123 ALA F CA  1 
ATOM   6455 C  C   . ALA F 1 123 ? -62.800 -79.091 23.751 1.00 75.35  ? 123 ALA F C   1 
ATOM   6456 O  O   . ALA F 1 123 ? -63.642 -78.227 23.983 1.00 75.82  ? 123 ALA F O   1 
ATOM   6457 C  CB  . ALA F 1 123 ? -63.376 -81.189 24.919 1.00 78.18  ? 123 ALA F CB  1 
ATOM   6458 N  N   . ASP F 1 124 ? -62.179 -79.239 22.579 1.00 73.91  ? 124 ASP F N   1 
ATOM   6459 C  CA  . ASP F 1 124 ? -62.605 -78.589 21.348 1.00 73.84  ? 124 ASP F CA  1 
ATOM   6460 C  C   . ASP F 1 124 ? -63.882 -79.321 21.013 1.00 75.10  ? 124 ASP F C   1 
ATOM   6461 O  O   . ASP F 1 124 ? -63.915 -80.533 21.087 1.00 75.32  ? 124 ASP F O   1 
ATOM   6462 C  CB  . ASP F 1 124 ? -61.535 -78.776 20.240 1.00 72.95  ? 124 ASP F CB  1 
ATOM   6463 C  CG  . ASP F 1 124 ? -61.884 -78.071 18.887 1.00 74.40  ? 124 ASP F CG  1 
ATOM   6464 O  OD1 . ASP F 1 124 ? -63.000 -77.499 18.767 1.00 76.74  ? 124 ASP F OD1 1 
ATOM   6465 O  OD2 . ASP F 1 124 ? -61.041 -78.123 17.928 1.00 74.04  ? 124 ASP F OD2 1 
ATOM   6466 N  N   . ASP F 1 125 ? -64.942 -78.594 20.673 1.00 76.17  ? 125 ASP F N   1 
ATOM   6467 C  CA  . ASP F 1 125 ? -66.223 -79.227 20.342 1.00 77.96  ? 125 ASP F CA  1 
ATOM   6468 C  C   . ASP F 1 125 ? -66.404 -79.350 18.842 1.00 78.26  ? 125 ASP F C   1 
ATOM   6469 O  O   . ASP F 1 125 ? -67.490 -79.621 18.376 1.00 79.87  ? 125 ASP F O   1 
ATOM   6470 C  CB  . ASP F 1 125 ? -67.389 -78.466 20.978 1.00 79.83  ? 125 ASP F CB  1 
ATOM   6471 C  CG  . ASP F 1 125 ? -67.630 -77.132 20.343 1.00 80.49  ? 125 ASP F CG  1 
ATOM   6472 O  OD1 . ASP F 1 125 ? -67.194 -76.965 19.191 1.00 80.36  ? 125 ASP F OD1 1 
ATOM   6473 O  OD2 . ASP F 1 125 ? -68.257 -76.262 20.998 1.00 81.62  ? 125 ASP F OD2 1 
ATOM   6474 N  N   . LEU F 1 126 ? -65.327 -79.114 18.104 1.00 76.88  ? 126 LEU F N   1 
ATOM   6475 C  CA  . LEU F 1 126 ? -65.259 -79.380 16.681 1.00 77.93  ? 126 LEU F CA  1 
ATOM   6476 C  C   . LEU F 1 126 ? -66.286 -78.598 15.874 1.00 80.37  ? 126 LEU F C   1 
ATOM   6477 O  O   . LEU F 1 126 ? -66.660 -79.001 14.779 1.00 82.10  ? 126 LEU F O   1 
ATOM   6478 C  CB  . LEU F 1 126 ? -65.383 -80.887 16.401 1.00 78.92  ? 126 LEU F CB  1 
ATOM   6479 C  CG  . LEU F 1 126 ? -64.552 -81.832 17.266 1.00 77.02  ? 126 LEU F CG  1 
ATOM   6480 C  CD1 . LEU F 1 126 ? -64.382 -83.212 16.584 1.00 77.83  ? 126 LEU F CD1 1 
ATOM   6481 C  CD2 . LEU F 1 126 ? -63.225 -81.192 17.547 1.00 73.64  ? 126 LEU F CD2 1 
ATOM   6482 N  N   . GLY F 1 127 ? -66.724 -77.474 16.411 1.00 81.19  ? 127 GLY F N   1 
ATOM   6483 C  CA  . GLY F 1 127 ? -67.641 -76.583 15.715 1.00 84.06  ? 127 GLY F CA  1 
ATOM   6484 C  C   . GLY F 1 127 ? -69.109 -76.870 15.948 1.00 87.42  ? 127 GLY F C   1 
ATOM   6485 O  O   . GLY F 1 127 ? -69.957 -76.076 15.570 1.00 89.53  ? 127 GLY F O   1 
ATOM   6486 N  N   . LYS F 1 128 ? -69.415 -77.975 16.619 1.00 88.48  ? 128 LYS F N   1 
ATOM   6487 C  CA  . LYS F 1 128 ? -70.787 -78.480 16.682 1.00 92.22  ? 128 LYS F CA  1 
ATOM   6488 C  C   . LYS F 1 128 ? -71.506 -78.089 17.970 1.00 92.83  ? 128 LYS F C   1 
ATOM   6489 O  O   . LYS F 1 128 ? -72.483 -78.745 18.361 1.00 95.00  ? 128 LYS F O   1 
ATOM   6490 C  CB  . LYS F 1 128 ? -70.810 -80.016 16.519 1.00 93.23  ? 128 LYS F CB  1 
ATOM   6491 C  CG  . LYS F 1 128 ? -69.765 -80.580 15.556 1.00 94.86  ? 128 LYS F CG  1 
ATOM   6492 C  CD  . LYS F 1 128 ? -70.121 -81.989 14.991 1.00 100.35 ? 128 LYS F CD  1 
ATOM   6493 C  CE  . LYS F 1 128 ? -68.908 -82.644 14.242 1.00 101.13 ? 128 LYS F CE  1 
ATOM   6494 N  NZ  . LYS F 1 128 ? -68.535 -81.964 12.953 1.00 102.56 ? 128 LYS F NZ  1 
ATOM   6495 N  N   . GLY F 1 129 ? -71.035 -77.030 18.628 1.00 91.59  ? 129 GLY F N   1 
ATOM   6496 C  CA  . GLY F 1 129 ? -71.579 -76.614 19.941 1.00 92.71  ? 129 GLY F CA  1 
ATOM   6497 C  C   . GLY F 1 129 ? -72.786 -75.708 19.803 1.00 96.13  ? 129 GLY F C   1 
ATOM   6498 O  O   . GLY F 1 129 ? -73.455 -75.344 20.796 1.00 97.62  ? 129 GLY F O   1 
ATOM   6499 N  N   . GLY F 1 130 ? -73.031 -75.307 18.556 1.00 97.52  ? 130 GLY F N   1 
ATOM   6500 C  CA  . GLY F 1 130 ? -74.180 -74.492 18.215 1.00 101.30 ? 130 GLY F CA  1 
ATOM   6501 C  C   . GLY F 1 130 ? -74.210 -73.140 18.900 1.00 102.20 ? 130 GLY F C   1 
ATOM   6502 O  O   . GLY F 1 130 ? -75.248 -72.538 19.044 1.00 105.61 ? 130 GLY F O   1 
ATOM   6503 N  N   . ASN F 1 131 ? -73.078 -72.654 19.354 1.00 99.93  ? 131 ASN F N   1 
ATOM   6504 C  CA  . ASN F 1 131 ? -73.050 -71.312 19.872 1.00 101.45 ? 131 ASN F CA  1 
ATOM   6505 C  C   . ASN F 1 131 ? -72.059 -70.515 19.030 1.00 100.38 ? 131 ASN F C   1 
ATOM   6506 O  O   . ASN F 1 131 ? -71.367 -71.082 18.173 1.00 98.06  ? 131 ASN F O   1 
ATOM   6507 C  CB  . ASN F 1 131 ? -72.802 -71.313 21.395 1.00 100.88 ? 131 ASN F CB  1 
ATOM   6508 C  CG  . ASN F 1 131 ? -71.341 -71.317 21.756 1.00 96.95  ? 131 ASN F CG  1 
ATOM   6509 O  OD1 . ASN F 1 131 ? -70.551 -72.071 21.203 1.00 93.92  ? 131 ASN F OD1 1 
ATOM   6510 N  ND2 . ASN F 1 131 ? -70.974 -70.476 22.703 1.00 97.01  ? 131 ASN F ND2 1 
ATOM   6511 N  N   . GLU F 1 132 ? -72.066 -69.200 19.203 1.00 102.75 ? 132 GLU F N   1 
ATOM   6512 C  CA  . GLU F 1 132 ? -71.278 -68.326 18.334 1.00 103.21 ? 132 GLU F CA  1 
ATOM   6513 C  C   . GLU F 1 132 ? -69.819 -68.724 18.416 1.00 98.86  ? 132 GLU F C   1 
ATOM   6514 O  O   . GLU F 1 132 ? -69.152 -68.981 17.395 1.00 96.87  ? 132 GLU F O   1 
ATOM   6515 C  CB  . GLU F 1 132 ? -71.489 -66.855 18.747 1.00 106.65 ? 132 GLU F CB  1 
ATOM   6516 C  CG  . GLU F 1 132 ? -70.288 -65.862 18.506 1.00 108.22 ? 132 GLU F CG  1 
ATOM   6517 C  CD  . GLU F 1 132 ? -70.370 -65.060 17.200 1.00 113.34 ? 132 GLU F CD  1 
ATOM   6518 O  OE1 . GLU F 1 132 ? -71.499 -64.832 16.700 1.00 118.41 ? 132 GLU F OE1 1 
ATOM   6519 O  OE2 . GLU F 1 132 ? -69.298 -64.638 16.688 1.00 113.15 ? 132 GLU F OE2 1 
ATOM   6520 N  N   . GLU F 1 133 ? -69.370 -68.809 19.668 1.00 97.35  ? 133 GLU F N   1 
ATOM   6521 C  CA  . GLU F 1 133 ? -67.994 -69.112 20.013 1.00 94.06  ? 133 GLU F CA  1 
ATOM   6522 C  C   . GLU F 1 133 ? -67.484 -70.449 19.433 1.00 90.92  ? 133 GLU F C   1 
ATOM   6523 O  O   . GLU F 1 133 ? -66.307 -70.586 19.112 1.00 88.46  ? 133 GLU F O   1 
ATOM   6524 C  CB  . GLU F 1 133 ? -67.855 -69.088 21.541 1.00 94.34  ? 133 GLU F CB  1 
ATOM   6525 C  CG  . GLU F 1 133 ? -66.407 -69.154 22.056 1.00 93.60  ? 133 GLU F CG  1 
ATOM   6526 C  CD  . GLU F 1 133 ? -65.523 -67.973 21.538 1.00 96.29  ? 133 GLU F CD  1 
ATOM   6527 O  OE1 . GLU F 1 133 ? -66.048 -66.838 21.391 1.00 100.25 ? 133 GLU F OE1 1 
ATOM   6528 O  OE2 . GLU F 1 133 ? -64.306 -68.182 21.260 1.00 95.30  ? 133 GLU F OE2 1 
ATOM   6529 N  N   . SER F 1 134 ? -68.372 -71.428 19.279 1.00 91.29  ? 134 SER F N   1 
ATOM   6530 C  CA  . SER F 1 134 ? -67.971 -72.744 18.805 1.00 88.91  ? 134 SER F CA  1 
ATOM   6531 C  C   . SER F 1 134 ? -67.415 -72.666 17.392 1.00 88.38  ? 134 SER F C   1 
ATOM   6532 O  O   . SER F 1 134 ? -66.521 -73.421 17.063 1.00 86.89  ? 134 SER F O   1 
ATOM   6533 C  CB  . SER F 1 134 ? -69.125 -73.744 18.869 1.00 90.40  ? 134 SER F CB  1 
ATOM   6534 O  OG  . SER F 1 134 ? -68.764 -74.972 18.279 1.00 88.54  ? 134 SER F OG  1 
ATOM   6535 N  N   . THR F 1 135 ? -67.903 -71.757 16.553 1.00 90.14  ? 135 THR F N   1 
ATOM   6536 C  CA  . THR F 1 135 ? -67.380 -71.677 15.184 1.00 90.01  ? 135 THR F CA  1 
ATOM   6537 C  C   . THR F 1 135 ? -66.112 -70.834 15.108 1.00 88.44  ? 135 THR F C   1 
ATOM   6538 O  O   . THR F 1 135 ? -65.673 -70.468 14.015 1.00 88.88  ? 135 THR F O   1 
ATOM   6539 C  CB  . THR F 1 135 ? -68.421 -71.099 14.268 1.00 93.40  ? 135 THR F CB  1 
ATOM   6540 O  OG1 . THR F 1 135 ? -69.088 -70.068 14.992 1.00 95.05  ? 135 THR F OG1 1 
ATOM   6541 C  CG2 . THR F 1 135 ? -69.425 -72.171 13.842 1.00 94.43  ? 135 THR F CG2 1 
ATOM   6542 N  N   . LYS F 1 136 ? -65.509 -70.556 16.266 1.00 86.81  ? 136 LYS F N   1 
ATOM   6543 C  CA  . LYS F 1 136 ? -64.263 -69.793 16.339 1.00 85.85  ? 136 LYS F CA  1 
ATOM   6544 C  C   . LYS F 1 136 ? -63.164 -70.529 17.118 1.00 82.58  ? 136 LYS F C   1 
ATOM   6545 O  O   . LYS F 1 136 ? -62.097 -70.821 16.582 1.00 81.20  ? 136 LYS F O   1 
ATOM   6546 C  CB  . LYS F 1 136 ? -64.537 -68.428 16.955 1.00 87.80  ? 136 LYS F CB  1 
ATOM   6547 C  CG  . LYS F 1 136 ? -65.730 -67.710 16.313 1.00 93.31  ? 136 LYS F CG  1 
ATOM   6548 C  CD  . LYS F 1 136 ? -66.136 -66.428 17.074 1.00 98.21  ? 136 LYS F CD  1 
ATOM   6549 C  CE  . LYS F 1 136 ? -65.074 -65.329 17.007 1.00 99.08  ? 136 LYS F CE  1 
ATOM   6550 N  NZ  . LYS F 1 136 ? -65.581 -64.021 17.472 1.00 102.87 ? 136 LYS F NZ  1 
ATOM   6551 N  N   . THR F 1 137 ? -63.413 -70.835 18.377 1.00 81.64  ? 137 THR F N   1 
ATOM   6552 C  CA  . THR F 1 137 ? -62.428 -71.564 19.153 1.00 79.46  ? 137 THR F CA  1 
ATOM   6553 C  C   . THR F 1 137 ? -62.891 -72.961 19.500 1.00 78.40  ? 137 THR F C   1 
ATOM   6554 O  O   . THR F 1 137 ? -62.209 -73.658 20.229 1.00 77.46  ? 137 THR F O   1 
ATOM   6555 C  CB  . THR F 1 137 ? -62.111 -70.882 20.488 1.00 79.76  ? 137 THR F CB  1 
ATOM   6556 O  OG1 . THR F 1 137 ? -63.301 -70.857 21.279 1.00 82.08  ? 137 THR F OG1 1 
ATOM   6557 C  CG2 . THR F 1 137 ? -61.548 -69.472 20.282 1.00 80.96  ? 137 THR F CG2 1 
ATOM   6558 N  N   . GLY F 1 138 ? -64.051 -73.378 19.029 1.00 79.06  ? 138 GLY F N   1 
ATOM   6559 C  CA  . GLY F 1 138 ? -64.588 -74.662 19.463 1.00 78.67  ? 138 GLY F CA  1 
ATOM   6560 C  C   . GLY F 1 138 ? -64.864 -74.738 20.957 1.00 78.63  ? 138 GLY F C   1 
ATOM   6561 O  O   . GLY F 1 138 ? -64.940 -75.828 21.506 1.00 78.25  ? 138 GLY F O   1 
ATOM   6562 N  N   . ASN F 1 139 ? -65.026 -73.588 21.609 1.00 79.40  ? 139 ASN F N   1 
ATOM   6563 C  CA  . ASN F 1 139 ? -65.302 -73.516 23.046 1.00 80.44  ? 139 ASN F CA  1 
ATOM   6564 C  C   . ASN F 1 139 ? -64.232 -74.148 23.894 1.00 79.19  ? 139 ASN F C   1 
ATOM   6565 O  O   . ASN F 1 139 ? -64.493 -74.575 25.016 1.00 79.99  ? 139 ASN F O   1 
ATOM   6566 C  CB  . ASN F 1 139 ? -66.653 -74.167 23.370 1.00 82.45  ? 139 ASN F CB  1 
ATOM   6567 C  CG  . ASN F 1 139 ? -67.815 -73.243 23.120 1.00 84.83  ? 139 ASN F CG  1 
ATOM   6568 O  OD1 . ASN F 1 139 ? -67.647 -72.022 23.025 1.00 84.14  ? 139 ASN F OD1 1 
ATOM   6569 N  ND2 . ASN F 1 139 ? -69.013 -73.817 23.023 1.00 87.00  ? 139 ASN F ND2 1 
ATOM   6570 N  N   . ALA F 1 140 ? -63.017 -74.172 23.358 1.00 77.76  ? 140 ALA F N   1 
ATOM   6571 C  CA  . ALA F 1 140 ? -61.934 -75.001 23.894 1.00 76.73  ? 140 ALA F CA  1 
ATOM   6572 C  C   . ALA F 1 140 ? -61.454 -74.447 25.186 1.00 77.58  ? 140 ALA F C   1 
ATOM   6573 O  O   . ALA F 1 140 ? -60.835 -75.157 25.969 1.00 77.34  ? 140 ALA F O   1 
ATOM   6574 C  CB  . ALA F 1 140 ? -60.789 -75.067 22.926 1.00 75.07  ? 140 ALA F CB  1 
ATOM   6575 N  N   . GLY F 1 141 ? -61.730 -73.167 25.387 1.00 79.10  ? 141 GLY F N   1 
ATOM   6576 C  CA  . GLY F 1 141 ? -61.454 -72.518 26.643 1.00 80.73  ? 141 GLY F CA  1 
ATOM   6577 C  C   . GLY F 1 141 ? -60.108 -71.851 26.607 1.00 80.03  ? 141 GLY F C   1 
ATOM   6578 O  O   . GLY F 1 141 ? -59.510 -71.678 25.525 1.00 78.53  ? 141 GLY F O   1 
ATOM   6579 N  N   . SER F 1 142 ? -59.638 -71.480 27.797 1.00 81.58  ? 142 SER F N   1 
ATOM   6580 C  CA  . SER F 1 142 ? -58.411 -70.696 27.945 1.00 81.75  ? 142 SER F CA  1 
ATOM   6581 C  C   . SER F 1 142 ? -57.189 -71.505 27.505 1.00 79.45  ? 142 SER F C   1 
ATOM   6582 O  O   . SER F 1 142 ? -57.293 -72.694 27.174 1.00 78.02  ? 142 SER F O   1 
ATOM   6583 C  CB  . SER F 1 142 ? -58.241 -70.192 29.381 1.00 84.29  ? 142 SER F CB  1 
ATOM   6584 O  OG  . SER F 1 142 ? -58.144 -71.280 30.274 1.00 85.36  ? 142 SER F OG  1 
ATOM   6585 N  N   . ARG F 1 143 ? -56.044 -70.833 27.499 1.00 79.15  ? 143 ARG F N   1 
ATOM   6586 C  CA  . ARG F 1 143 ? -54.871 -71.345 26.846 1.00 77.62  ? 143 ARG F CA  1 
ATOM   6587 C  C   . ARG F 1 143 ? -53.849 -71.840 27.862 1.00 77.50  ? 143 ARG F C   1 
ATOM   6588 O  O   . ARG F 1 143 ? -53.018 -71.086 28.344 1.00 78.62  ? 143 ARG F O   1 
ATOM   6589 C  CB  . ARG F 1 143 ? -54.309 -70.246 25.950 1.00 77.92  ? 143 ARG F CB  1 
ATOM   6590 C  CG  . ARG F 1 143 ? -55.354 -69.702 24.969 1.00 79.75  ? 143 ARG F CG  1 
ATOM   6591 C  CD  . ARG F 1 143 ? -54.770 -68.672 24.021 1.00 82.45  ? 143 ARG F CD  1 
ATOM   6592 N  NE  . ARG F 1 143 ? -55.653 -68.432 22.893 1.00 84.14  ? 143 ARG F NE  1 
ATOM   6593 C  CZ  . ARG F 1 143 ? -55.430 -67.546 21.928 1.00 86.07  ? 143 ARG F CZ  1 
ATOM   6594 N  NH1 . ARG F 1 143 ? -54.342 -66.784 21.928 1.00 86.82  ? 143 ARG F NH1 1 
ATOM   6595 N  NH2 . ARG F 1 143 ? -56.319 -67.420 20.948 1.00 87.65  ? 143 ARG F NH2 1 
ATOM   6596 N  N   . LEU F 1 144 ? -53.916 -73.124 28.170 1.00 76.41  ? 144 LEU F N   1 
ATOM   6597 C  CA  . LEU F 1 144 ? -53.171 -73.681 29.281 1.00 77.41  ? 144 LEU F CA  1 
ATOM   6598 C  C   . LEU F 1 144 ? -51.657 -73.640 29.116 1.00 76.68  ? 144 LEU F C   1 
ATOM   6599 O  O   . LEU F 1 144 ? -50.924 -73.355 30.067 1.00 78.36  ? 144 LEU F O   1 
ATOM   6600 C  CB  . LEU F 1 144 ? -53.632 -75.123 29.540 1.00 77.65  ? 144 LEU F CB  1 
ATOM   6601 C  CG  . LEU F 1 144 ? -54.941 -75.350 30.324 1.00 79.80  ? 144 LEU F CG  1 
ATOM   6602 C  CD1 . LEU F 1 144 ? -55.199 -76.860 30.546 1.00 81.18  ? 144 LEU F CD1 1 
ATOM   6603 C  CD2 . LEU F 1 144 ? -54.966 -74.595 31.674 1.00 83.49  ? 144 LEU F CD2 1 
ATOM   6604 N  N   . ALA F 1 145 ? -51.194 -73.960 27.920 1.00 74.49  ? 145 ALA F N   1 
ATOM   6605 C  CA  . ALA F 1 145 ? -49.766 -73.942 27.607 1.00 74.43  ? 145 ALA F CA  1 
ATOM   6606 C  C   . ALA F 1 145 ? -49.561 -73.716 26.106 1.00 73.04  ? 145 ALA F C   1 
ATOM   6607 O  O   . ALA F 1 145 ? -50.456 -74.004 25.311 1.00 72.29  ? 145 ALA F O   1 
ATOM   6608 C  CB  . ALA F 1 145 ? -49.134 -75.236 28.027 1.00 74.70  ? 145 ALA F CB  1 
ATOM   6609 N  N   . CYS F 1 146 ? -48.400 -73.198 25.709 1.00 73.45  ? 146 CYS F N   1 
ATOM   6610 C  CA  . CYS F 1 146 ? -48.131 -72.933 24.292 1.00 72.49  ? 146 CYS F CA  1 
ATOM   6611 C  C   . CYS F 1 146 ? -46.670 -72.693 24.006 1.00 72.63  ? 146 CYS F C   1 
ATOM   6612 O  O   . CYS F 1 146 ? -45.887 -72.441 24.897 1.00 74.18  ? 146 CYS F O   1 
ATOM   6613 C  CB  . CYS F 1 146 ? -48.898 -71.711 23.825 1.00 72.65  ? 146 CYS F CB  1 
ATOM   6614 S  SG  . CYS F 1 146 ? -48.281 -70.131 24.487 1.00 76.62  ? 146 CYS F SG  1 
ATOM   6615 N  N   . GLY F 1 147 ? -46.308 -72.762 22.743 1.00 71.51  ? 147 GLY F N   1 
ATOM   6616 C  CA  . GLY F 1 147 ? -44.967 -72.404 22.345 1.00 72.27  ? 147 GLY F CA  1 
ATOM   6617 C  C   . GLY F 1 147 ? -44.846 -72.240 20.857 1.00 71.35  ? 147 GLY F C   1 
ATOM   6618 O  O   . GLY F 1 147 ? -45.623 -72.815 20.106 1.00 70.34  ? 147 GLY F O   1 
ATOM   6619 N  N   . VAL F 1 148 ? -43.861 -71.465 20.426 1.00 71.67  ? 148 VAL F N   1 
ATOM   6620 C  CA  . VAL F 1 148 ? -43.627 -71.300 18.997 1.00 71.24  ? 148 VAL F CA  1 
ATOM   6621 C  C   . VAL F 1 148 ? -43.066 -72.568 18.372 1.00 70.81  ? 148 VAL F C   1 
ATOM   6622 O  O   . VAL F 1 148 ? -42.297 -73.279 18.974 1.00 71.24  ? 148 VAL F O   1 
ATOM   6623 C  CB  . VAL F 1 148 ? -42.689 -70.134 18.726 1.00 72.73  ? 148 VAL F CB  1 
ATOM   6624 C  CG1 . VAL F 1 148 ? -42.377 -70.053 17.283 1.00 72.70  ? 148 VAL F CG1 1 
ATOM   6625 C  CG2 . VAL F 1 148 ? -43.340 -68.875 19.187 1.00 72.95  ? 148 VAL F CG2 1 
ATOM   6626 N  N   . ILE F 1 149 ? -43.466 -72.827 17.150 1.00 70.23  ? 149 ILE F N   1 
ATOM   6627 C  CA  . ILE F 1 149 ? -43.047 -74.002 16.433 1.00 70.86  ? 149 ILE F CA  1 
ATOM   6628 C  C   . ILE F 1 149 ? -41.823 -73.701 15.633 1.00 72.68  ? 149 ILE F C   1 
ATOM   6629 O  O   . ILE F 1 149 ? -41.875 -72.865 14.740 1.00 73.27  ? 149 ILE F O   1 
ATOM   6630 C  CB  . ILE F 1 149 ? -44.076 -74.375 15.384 1.00 70.64  ? 149 ILE F CB  1 
ATOM   6631 C  CG1 . ILE F 1 149 ? -45.252 -75.079 16.017 1.00 69.08  ? 149 ILE F CG1 1 
ATOM   6632 C  CG2 . ILE F 1 149 ? -43.477 -75.272 14.333 1.00 72.55  ? 149 ILE F CG2 1 
ATOM   6633 C  CD1 . ILE F 1 149 ? -46.481 -74.906 15.202 1.00 69.43  ? 149 ILE F CD1 1 
ATOM   6634 N  N   . GLY F 1 150 ? -40.758 -74.449 15.859 1.00 74.04  ? 150 GLY F N   1 
ATOM   6635 C  CA  . GLY F 1 150 ? -39.466 -74.126 15.263 1.00 76.80  ? 150 GLY F CA  1 
ATOM   6636 C  C   . GLY F 1 150 ? -38.810 -75.238 14.489 1.00 78.99  ? 150 GLY F C   1 
ATOM   6637 O  O   . GLY F 1 150 ? -39.193 -76.391 14.621 1.00 78.83  ? 150 GLY F O   1 
ATOM   6638 N  N   . ILE F 1 151 ? -37.799 -74.899 13.700 1.00 82.00  ? 151 ILE F N   1 
ATOM   6639 C  CA  . ILE F 1 151 ? -37.185 -75.880 12.803 1.00 85.05  ? 151 ILE F CA  1 
ATOM   6640 C  C   . ILE F 1 151 ? -36.293 -76.787 13.607 1.00 87.39  ? 151 ILE F C   1 
ATOM   6641 O  O   . ILE F 1 151 ? -35.453 -76.301 14.378 1.00 88.43  ? 151 ILE F O   1 
ATOM   6642 C  CB  . ILE F 1 151 ? -36.350 -75.236 11.716 1.00 87.58  ? 151 ILE F CB  1 
ATOM   6643 C  CG1 . ILE F 1 151 ? -37.212 -74.249 10.938 1.00 86.48  ? 151 ILE F CG1 1 
ATOM   6644 C  CG2 . ILE F 1 151 ? -35.790 -76.307 10.800 1.00 89.80  ? 151 ILE F CG2 1 
ATOM   6645 C  CD1 . ILE F 1 151 ? -36.466 -73.524 9.900  1.00 89.68  ? 151 ILE F CD1 1 
ATOM   6646 N  N   . ALA F 1 152 ? -36.493 -78.095 13.444 1.00 89.31  ? 152 ALA F N   1 
ATOM   6647 C  CA  . ALA F 1 152 ? -35.820 -79.104 14.282 1.00 91.76  ? 152 ALA F CA  1 
ATOM   6648 C  C   . ALA F 1 152 ? -34.722 -79.742 13.495 1.00 96.75  ? 152 ALA F C   1 
ATOM   6649 O  O   . ALA F 1 152 ? -34.724 -79.689 12.246 1.00 98.01  ? 152 ALA F O   1 
ATOM   6650 C  CB  . ALA F 1 152 ? -36.794 -80.183 14.734 1.00 90.40  ? 152 ALA F CB  1 
ATOM   6651 N  N   . GLN F 1 153 ? -33.797 -80.374 14.207 1.00 100.31 ? 153 GLN F N   1 
ATOM   6652 C  CA  . GLN F 1 153 ? -32.760 -81.104 13.493 1.00 105.92 ? 153 GLN F CA  1 
ATOM   6653 C  C   . GLN F 1 153 ? -33.319 -82.370 12.796 1.00 107.79 ? 153 GLN F C   1 
ATOM   6654 O  O   . GLN F 1 153 ? -34.063 -83.163 13.411 1.00 107.00 ? 153 GLN F O   1 
ATOM   6655 C  CB  . GLN F 1 153 ? -31.580 -81.479 14.387 1.00 108.76 ? 153 GLN F CB  1 
ATOM   6656 C  CG  . GLN F 1 153 ? -30.444 -82.097 13.538 1.00 114.07 ? 153 GLN F CG  1 
ATOM   6657 C  CD  . GLN F 1 153 ? -29.093 -82.101 14.230 1.00 118.05 ? 153 GLN F CD  1 
ATOM   6658 O  OE1 . GLN F 1 153 ? -28.956 -82.492 15.415 1.00 118.88 ? 153 GLN F OE1 1 
ATOM   6659 N  NE2 . GLN F 1 153 ? -28.075 -81.670 13.491 1.00 121.16 ? 153 GLN F NE2 1 
ATOM   6660 O  OXT . GLN F 1 153 ? -33.040 -82.636 11.605 1.00 111.04 ? 153 GLN F OXT 1 
HETATM 6661 CU CU  . CU  G 2 .   ? -18.813 -37.023 19.515 1.00 122.96 ? 154 CU  A CU  1 
HETATM 6662 ZN ZN  . ZN  H 3 .   ? -20.613 -39.701 14.167 1.00 72.76  ? 155 ZN  A ZN  1 
HETATM 6663 CU CU  . CU  I 2 .   ? -6.848  -5.746  18.246 1.00 119.37 ? 154 CU  B CU  1 
HETATM 6664 ZN ZN  . ZN  J 3 .   ? -7.107  -2.908  12.377 1.00 78.13  ? 155 ZN  B ZN  1 
HETATM 6665 CU CU  . CU  K 2 .   ? 5.040   -56.505 18.486 1.00 136.66 ? 154 CU  C CU  1 
HETATM 6666 ZN ZN  . ZN  L 3 .   ? 2.982   -54.576 12.909 1.00 95.31  ? 155 ZN  C ZN  1 
HETATM 6667 CU CU  . CU  M 2 .   ? 25.614  -82.824 20.163 1.00 148.52 ? 154 CU  D CU  1 
HETATM 6668 ZN ZN  . ZN  N 3 .   ? 27.456  -85.439 14.868 1.00 68.78  ? 155 ZN  D ZN  1 
HETATM 6669 CU CU  . CU  O 2 .   ? -24.192 -67.654 19.200 1.00 138.29 ? 154 CU  E CU  1 
HETATM 6670 ZN ZN  . ZN  P 3 .   ? -21.233 -67.229 13.463 1.00 93.03  ? 155 ZN  E ZN  1 
HETATM 6671 CU CU  . CU  Q 2 .   ? -57.179 -72.730 20.244 1.00 111.58 ? 154 CU  F CU  1 
HETATM 6672 ZN ZN  . ZN  R 3 .   ? -60.291 -73.347 14.715 1.00 74.68  ? 155 ZN  F ZN  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   THR 2   2   2   THR THR 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  ILE 17  17  17  ILE ILE A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  ASN 19  19  19  ASN ASN 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  GLU 24  24  24  GLU GLU A . n 
A 1 25  SER 25  25  25  SER SER A . n 
A 1 26  ASN 26  26  26  ASN ASN A . n 
A 1 27  GLY 27  27  27  GLY GLY 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  LYS 30  30  30  LYS LYS A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  TRP 32  32  32  TRP TRP A . n 
A 1 33  GLY 33  33  33  GLY GLY A . n 
A 1 34  SER 34  34  34  SER SER A . n 
A 1 35  ILE 35  35  35  ILE ILE A . n 
A 1 36  LYS 36  36  36  LYS LYS 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  LEU 42  42  42  LEU LEU 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  GLU 49  49  49  GLU GLU A . n 
A 1 50  PHE 50  50  50  PHE PHE 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  ALA 55  55  55  ALA ALA 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  LEU 67  67  67  LEU LEU A . n 
A 1 68  SER 68  68  68  SER SER A . n 
A 1 69  ARG 69  69  69  ARG ARG 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  LYS 75  75  75  LYS LYS 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   THR 2   2   2   THR THR 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  ILE 17  17  17  ILE ILE B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  ASN 19  19  19  ASN ASN 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  GLU 24  24  24  GLU GLU B . n 
B 1 25  SER 25  25  25  SER SER B . n 
B 1 26  ASN 26  26  26  ASN ASN B . n 
B 1 27  GLY 27  27  27  GLY GLY 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  LYS 30  30  30  LYS LYS B . n 
B 1 31  VAL 31  31  31  VAL VAL B . n 
B 1 32  TRP 32  32  32  TRP TRP B . n 
B 1 33  GLY 33  33  33  GLY GLY B . n 
B 1 34  SER 34  34  34  SER SER B . n 
B 1 35  ILE 35  35  35  ILE ILE B . n 
B 1 36  LYS 36  36  36  LYS LYS 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  LEU 42  42  42  LEU LEU 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  GLU 49  49  49  GLU GLU B . n 
B 1 50  PHE 50  50  50  PHE PHE 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  ALA 55  55  55  ALA ALA 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  LEU 67  67  67  LEU LEU B . n 
B 1 68  SER 68  68  68  SER SER B . n 
B 1 69  ARG 69  69  69  ARG ARG 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  LYS 75  75  75  LYS LYS 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   THR 2   2   2   THR THR 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  ILE 17  17  17  ILE ILE C . n 
C 1 18  ILE 18  18  18  ILE ILE C . n 
C 1 19  ASN 19  19  19  ASN ASN 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  GLU 24  24  24  GLU GLU C . n 
C 1 25  SER 25  25  25  SER SER C . n 
C 1 26  ASN 26  26  26  ASN ASN C . n 
C 1 27  GLY 27  27  27  GLY GLY 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  LYS 30  30  30  LYS LYS C . n 
C 1 31  VAL 31  31  31  VAL VAL C . n 
C 1 32  TRP 32  32  32  TRP TRP C . n 
C 1 33  GLY 33  33  33  GLY GLY C . n 
C 1 34  SER 34  34  34  SER SER C . n 
C 1 35  ILE 35  35  35  ILE ILE C . n 
C 1 36  LYS 36  36  36  LYS LYS 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  LEU 42  42  42  LEU LEU 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  GLU 49  49  49  GLU GLU C . n 
C 1 50  PHE 50  50  50  PHE PHE 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  ALA 55  55  55  ALA ALA 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  LEU 67  67  67  LEU LEU C . n 
C 1 68  SER 68  68  68  SER SER C . n 
C 1 69  ARG 69  69  69  ARG ARG 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  LYS 75  75  75  LYS LYS 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 128 128 128 LYS LYS C . n 
C 1 129 GLY 129 129 129 GLY GLY C . n 
C 1 130 GLY 130 130 130 GLY GLY 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   THR 2   2   2   THR THR 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  ILE 17  17  17  ILE ILE D . n 
D 1 18  ILE 18  18  18  ILE ILE D . n 
D 1 19  ASN 19  19  19  ASN ASN 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  GLU 24  24  24  GLU GLU D . n 
D 1 25  SER 25  25  25  SER SER D . n 
D 1 26  ASN 26  26  26  ASN ASN D . n 
D 1 27  GLY 27  27  27  GLY GLY 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  LYS 30  30  30  LYS LYS D . n 
D 1 31  VAL 31  31  31  VAL VAL D . n 
D 1 32  TRP 32  32  32  TRP TRP D . n 
D 1 33  GLY 33  33  33  GLY GLY D . n 
D 1 34  SER 34  34  34  SER SER D . n 
D 1 35  ILE 35  35  35  ILE ILE D . n 
D 1 36  LYS 36  36  36  LYS LYS 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  LEU 42  42  42  LEU LEU 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  GLU 49  49  49  GLU GLU D . n 
D 1 50  PHE 50  50  50  PHE PHE 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  ALA 55  55  55  ALA ALA 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  LEU 67  67  67  LEU LEU D . n 
D 1 68  SER 68  68  68  SER SER D . n 
D 1 69  ARG 69  69  69  ARG ARG 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  LYS 75  75  75  LYS LYS 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 153 153 153 GLN GLN D . n 
E 1 1   ALA 1   1   1   ALA ALA E . n 
E 1 2   THR 2   2   2   THR THR 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  ILE 17  17  17  ILE ILE E . n 
E 1 18  ILE 18  18  18  ILE ILE E . n 
E 1 19  ASN 19  19  19  ASN ASN 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  GLU 24  24  24  GLU GLU E . n 
E 1 25  SER 25  25  25  SER SER E . n 
E 1 26  ASN 26  26  26  ASN ASN E . n 
E 1 27  GLY 27  27  27  GLY GLY 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  LYS 30  30  30  LYS LYS E . n 
E 1 31  VAL 31  31  31  VAL VAL E . n 
E 1 32  TRP 32  32  32  TRP TRP E . n 
E 1 33  GLY 33  33  33  GLY GLY E . n 
E 1 34  SER 34  34  34  SER SER E . n 
E 1 35  ILE 35  35  35  ILE ILE E . n 
E 1 36  LYS 36  36  36  LYS LYS 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  LEU 42  42  42  LEU LEU 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  GLU 49  49  49  GLU GLU E . n 
E 1 50  PHE 50  50  50  PHE PHE 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  ALA 55  55  55  ALA ALA 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  LEU 67  67  67  LEU LEU E . n 
E 1 68  SER 68  68  68  SER SER E . n 
E 1 69  ARG 69  69  69  ARG ARG 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  LYS 75  75  75  LYS LYS 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   THR 2   2   2   THR THR 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  ILE 17  17  17  ILE ILE F . n 
F 1 18  ILE 18  18  18  ILE ILE F . n 
F 1 19  ASN 19  19  19  ASN ASN 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  GLU 24  24  24  GLU GLU F . n 
F 1 25  SER 25  25  25  SER SER F . n 
F 1 26  ASN 26  26  26  ASN ASN F . n 
F 1 27  GLY 27  27  27  GLY GLY 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  LYS 30  30  30  LYS LYS F . n 
F 1 31  VAL 31  31  31  VAL VAL F . n 
F 1 32  TRP 32  32  32  TRP TRP F . n 
F 1 33  GLY 33  33  33  GLY GLY F . n 
F 1 34  SER 34  34  34  SER SER F . n 
F 1 35  ILE 35  35  35  ILE ILE F . n 
F 1 36  LYS 36  36  36  LYS LYS 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  LEU 42  42  42  LEU LEU 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  GLU 49  49  49  GLU GLU F . n 
F 1 50  PHE 50  50  50  PHE PHE 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  ALA 55  55  55  ALA ALA 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  LEU 67  67  67  LEU LEU F . n 
F 1 68  SER 68  68  68  SER SER F . n 
F 1 69  ARG 69  69  69  ARG ARG 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  LYS 75  75  75  LYS LYS 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_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,I,J 
2 1 C,D,K,L,M,N 
3 1 E,F,O,P,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)' 1460  ? 
1 MORE         -22   ? 
1 'SSA (A^2)'  13710 ? 
2 'ABSA (A^2)' 1480  ? 
2 MORE         -22   ? 
2 'SSA (A^2)'  13730 ? 
3 'ABSA (A^2)' 1340  ? 
3 MORE         -10   ? 
3 'SSA (A^2)'  13700 ? 
# 
_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 ? A HIS 46  ? A HIS 46  ? 1_555 CU ? G CU . ? A CU 154 ? 1_555 NE2 ? A HIS 120 ? A HIS 120 ? 1_555 96.0  ? 
2  ND1 ? A HIS 46  ? A HIS 46  ? 1_555 CU ? G CU . ? A CU 154 ? 1_555 NE2 ? A HIS 48  ? A HIS 48  ? 1_555 123.1 ? 
3  NE2 ? A HIS 120 ? A HIS 120 ? 1_555 CU ? G CU . ? A CU 154 ? 1_555 NE2 ? A HIS 48  ? A HIS 48  ? 1_555 93.7  ? 
4  ND1 ? A HIS 63  ? A HIS 63  ? 1_555 ZN ? H ZN . ? A ZN 155 ? 1_555 ND1 ? A HIS 71  ? A HIS 71  ? 1_555 111.0 ? 
5  ND1 ? A HIS 63  ? A HIS 63  ? 1_555 ZN ? H ZN . ? A ZN 155 ? 1_555 ND1 ? A HIS 80  ? A HIS 80  ? 1_555 116.1 ? 
6  ND1 ? A HIS 71  ? A HIS 71  ? 1_555 ZN ? H ZN . ? A ZN 155 ? 1_555 ND1 ? A HIS 80  ? A HIS 80  ? 1_555 122.1 ? 
7  ND1 ? A HIS 63  ? A HIS 63  ? 1_555 ZN ? H ZN . ? A ZN 155 ? 1_555 OD1 ? A ASP 83  ? A ASP 83  ? 1_555 90.6  ? 
8  ND1 ? A HIS 71  ? A HIS 71  ? 1_555 ZN ? H ZN . ? A ZN 155 ? 1_555 OD1 ? A ASP 83  ? A ASP 83  ? 1_555 90.1  ? 
9  ND1 ? A HIS 80  ? A HIS 80  ? 1_555 ZN ? H ZN . ? A ZN 155 ? 1_555 OD1 ? A ASP 83  ? A ASP 83  ? 1_555 120.2 ? 
10 ND1 ? B HIS 63  ? B HIS 63  ? 1_555 ZN ? J ZN . ? B ZN 155 ? 1_555 ND1 ? B HIS 71  ? B HIS 71  ? 1_555 105.3 ? 
11 ND1 ? B HIS 63  ? B HIS 63  ? 1_555 ZN ? J ZN . ? B ZN 155 ? 1_555 ND1 ? B HIS 80  ? B HIS 80  ? 1_555 113.5 ? 
12 ND1 ? B HIS 71  ? B HIS 71  ? 1_555 ZN ? J ZN . ? B ZN 155 ? 1_555 ND1 ? B HIS 80  ? B HIS 80  ? 1_555 126.1 ? 
13 ND1 ? B HIS 63  ? B HIS 63  ? 1_555 ZN ? J ZN . ? B ZN 155 ? 1_555 OD1 ? B ASP 83  ? B ASP 83  ? 1_555 85.6  ? 
14 ND1 ? B HIS 71  ? B HIS 71  ? 1_555 ZN ? J ZN . ? B ZN 155 ? 1_555 OD1 ? B ASP 83  ? B ASP 83  ? 1_555 87.8  ? 
15 ND1 ? B HIS 80  ? B HIS 80  ? 1_555 ZN ? J ZN . ? B ZN 155 ? 1_555 OD1 ? B ASP 83  ? B ASP 83  ? 1_555 129.7 ? 
16 NE2 ? B HIS 120 ? B HIS 120 ? 1_555 CU ? I CU . ? B CU 154 ? 1_555 NE2 ? B HIS 48  ? B HIS 48  ? 1_555 94.5  ? 
17 NE2 ? B HIS 120 ? B HIS 120 ? 1_555 CU ? I CU . ? B CU 154 ? 1_555 ND1 ? B HIS 46  ? B HIS 46  ? 1_555 81.3  ? 
18 NE2 ? B HIS 48  ? B HIS 48  ? 1_555 CU ? I CU . ? B CU 154 ? 1_555 ND1 ? B HIS 46  ? B HIS 46  ? 1_555 103.2 ? 
19 NE2 ? B HIS 120 ? B HIS 120 ? 1_555 CU ? I CU . ? B CU 154 ? 1_555 NE2 ? B HIS 63  ? B HIS 63  ? 1_555 152.7 ? 
20 NE2 ? B HIS 48  ? B HIS 48  ? 1_555 CU ? I CU . ? B CU 154 ? 1_555 NE2 ? B HIS 63  ? B HIS 63  ? 1_555 109.7 ? 
21 ND1 ? B HIS 46  ? B HIS 46  ? 1_555 CU ? I CU . ? B CU 154 ? 1_555 NE2 ? B HIS 63  ? B HIS 63  ? 1_555 81.2  ? 
22 ND1 ? C HIS 46  ? C HIS 46  ? 1_555 CU ? K CU . ? C CU 154 ? 1_555 NE2 ? C HIS 48  ? C HIS 48  ? 1_555 112.0 ? 
23 ND1 ? C HIS 46  ? C HIS 46  ? 1_555 CU ? K CU . ? C CU 154 ? 1_555 NE2 ? C HIS 120 ? C HIS 120 ? 1_555 88.0  ? 
24 NE2 ? C HIS 48  ? C HIS 48  ? 1_555 CU ? K CU . ? C CU 154 ? 1_555 NE2 ? C HIS 120 ? C HIS 120 ? 1_555 95.5  ? 
25 ND1 ? C HIS 46  ? C HIS 46  ? 1_555 CU ? K CU . ? C CU 154 ? 1_555 NE2 ? C HIS 63  ? C HIS 63  ? 1_555 85.2  ? 
26 NE2 ? C HIS 48  ? C HIS 48  ? 1_555 CU ? K CU . ? C CU 154 ? 1_555 NE2 ? C HIS 63  ? C HIS 63  ? 1_555 111.3 ? 
27 NE2 ? C HIS 120 ? C HIS 120 ? 1_555 CU ? K CU . ? C CU 154 ? 1_555 NE2 ? C HIS 63  ? C HIS 63  ? 1_555 153.0 ? 
28 ND1 ? C HIS 63  ? C HIS 63  ? 1_555 ZN ? L ZN . ? C ZN 155 ? 1_555 ND1 ? C HIS 71  ? C HIS 71  ? 1_555 114.2 ? 
29 ND1 ? C HIS 63  ? C HIS 63  ? 1_555 ZN ? L ZN . ? C ZN 155 ? 1_555 ND1 ? C HIS 80  ? C HIS 80  ? 1_555 112.0 ? 
30 ND1 ? C HIS 71  ? C HIS 71  ? 1_555 ZN ? L ZN . ? C ZN 155 ? 1_555 ND1 ? C HIS 80  ? C HIS 80  ? 1_555 123.1 ? 
31 ND1 ? C HIS 63  ? C HIS 63  ? 1_555 ZN ? L ZN . ? C ZN 155 ? 1_555 OD1 ? C ASP 83  ? C ASP 83  ? 1_555 89.8  ? 
32 ND1 ? C HIS 71  ? C HIS 71  ? 1_555 ZN ? L ZN . ? C ZN 155 ? 1_555 OD1 ? C ASP 83  ? C ASP 83  ? 1_555 93.6  ? 
33 ND1 ? C HIS 80  ? C HIS 80  ? 1_555 ZN ? L ZN . ? C ZN 155 ? 1_555 OD1 ? C ASP 83  ? C ASP 83  ? 1_555 118.0 ? 
34 ND1 ? D HIS 46  ? D HIS 46  ? 1_555 CU ? M CU . ? D CU 154 ? 1_555 NE2 ? D HIS 120 ? D HIS 120 ? 1_555 95.7  ? 
35 ND1 ? D HIS 46  ? D HIS 46  ? 1_555 CU ? M CU . ? D CU 154 ? 1_555 NE2 ? D HIS 48  ? D HIS 48  ? 1_555 113.8 ? 
36 NE2 ? D HIS 120 ? D HIS 120 ? 1_555 CU ? M CU . ? D CU 154 ? 1_555 NE2 ? D HIS 48  ? D HIS 48  ? 1_555 91.3  ? 
37 ND1 ? D HIS 46  ? D HIS 46  ? 1_555 CU ? M CU . ? D CU 154 ? 1_555 NE2 ? D HIS 63  ? D HIS 63  ? 1_555 88.1  ? 
38 NE2 ? D HIS 120 ? D HIS 120 ? 1_555 CU ? M CU . ? D CU 154 ? 1_555 NE2 ? D HIS 63  ? D HIS 63  ? 1_555 161.1 ? 
39 NE2 ? D HIS 48  ? D HIS 48  ? 1_555 CU ? M CU . ? D CU 154 ? 1_555 NE2 ? D HIS 63  ? D HIS 63  ? 1_555 104.1 ? 
40 ND1 ? D HIS 63  ? D HIS 63  ? 1_555 ZN ? N ZN . ? D ZN 155 ? 1_555 ND1 ? D HIS 71  ? D HIS 71  ? 1_555 117.3 ? 
41 ND1 ? D HIS 63  ? D HIS 63  ? 1_555 ZN ? N ZN . ? D ZN 155 ? 1_555 ND1 ? D HIS 80  ? D HIS 80  ? 1_555 114.3 ? 
42 ND1 ? D HIS 71  ? D HIS 71  ? 1_555 ZN ? N ZN . ? D ZN 155 ? 1_555 ND1 ? D HIS 80  ? D HIS 80  ? 1_555 121.5 ? 
43 ND1 ? D HIS 63  ? D HIS 63  ? 1_555 ZN ? N ZN . ? D ZN 155 ? 1_555 OD1 ? D ASP 83  ? D ASP 83  ? 1_555 86.3  ? 
44 ND1 ? D HIS 71  ? D HIS 71  ? 1_555 ZN ? N ZN . ? D ZN 155 ? 1_555 OD1 ? D ASP 83  ? D ASP 83  ? 1_555 93.1  ? 
45 ND1 ? D HIS 80  ? D HIS 80  ? 1_555 ZN ? N ZN . ? D ZN 155 ? 1_555 OD1 ? D ASP 83  ? D ASP 83  ? 1_555 116.1 ? 
46 NE2 ? E HIS 48  ? E HIS 48  ? 1_555 CU ? O CU . ? E CU 154 ? 1_555 NE2 ? E HIS 120 ? E HIS 120 ? 1_555 97.8  ? 
47 NE2 ? E HIS 48  ? E HIS 48  ? 1_555 CU ? O CU . ? E CU 154 ? 1_555 ND1 ? E HIS 46  ? E HIS 46  ? 1_555 114.7 ? 
48 NE2 ? E HIS 120 ? E HIS 120 ? 1_555 CU ? O CU . ? E CU 154 ? 1_555 ND1 ? E HIS 46  ? E HIS 46  ? 1_555 85.9  ? 
49 NE2 ? E HIS 48  ? E HIS 48  ? 1_555 CU ? O CU . ? E CU 154 ? 1_555 NE2 ? E HIS 63  ? E HIS 63  ? 1_555 113.4 ? 
50 NE2 ? E HIS 120 ? E HIS 120 ? 1_555 CU ? O CU . ? E CU 154 ? 1_555 NE2 ? E HIS 63  ? E HIS 63  ? 1_555 148.5 ? 
51 ND1 ? E HIS 46  ? E HIS 46  ? 1_555 CU ? O CU . ? E CU 154 ? 1_555 NE2 ? E HIS 63  ? E HIS 63  ? 1_555 85.1  ? 
52 ND1 ? E HIS 63  ? E HIS 63  ? 1_555 ZN ? P ZN . ? E ZN 155 ? 1_555 ND1 ? E HIS 71  ? E HIS 71  ? 1_555 103.7 ? 
53 ND1 ? E HIS 63  ? E HIS 63  ? 1_555 ZN ? P ZN . ? E ZN 155 ? 1_555 ND1 ? E HIS 80  ? E HIS 80  ? 1_555 115.0 ? 
54 ND1 ? E HIS 71  ? E HIS 71  ? 1_555 ZN ? P ZN . ? E ZN 155 ? 1_555 ND1 ? E HIS 80  ? E HIS 80  ? 1_555 133.2 ? 
55 ND1 ? E HIS 63  ? E HIS 63  ? 1_555 ZN ? P ZN . ? E ZN 155 ? 1_555 OD1 ? E ASP 83  ? E ASP 83  ? 1_555 80.5  ? 
56 ND1 ? E HIS 71  ? E HIS 71  ? 1_555 ZN ? P ZN . ? E ZN 155 ? 1_555 OD1 ? E ASP 83  ? E ASP 83  ? 1_555 88.3  ? 
57 ND1 ? E HIS 80  ? E HIS 80  ? 1_555 ZN ? P ZN . ? E ZN 155 ? 1_555 OD1 ? E ASP 83  ? E ASP 83  ? 1_555 122.1 ? 
58 ND1 ? F HIS 46  ? F HIS 46  ? 1_555 CU ? Q CU . ? F CU 154 ? 1_555 NE2 ? F HIS 120 ? F HIS 120 ? 1_555 96.5  ? 
59 ND1 ? F HIS 46  ? F HIS 46  ? 1_555 CU ? Q CU . ? F CU 154 ? 1_555 NE2 ? F HIS 48  ? F HIS 48  ? 1_555 115.5 ? 
60 NE2 ? F HIS 120 ? F HIS 120 ? 1_555 CU ? Q CU . ? F CU 154 ? 1_555 NE2 ? F HIS 48  ? F HIS 48  ? 1_555 96.2  ? 
61 ND1 ? F HIS 63  ? F HIS 63  ? 1_555 ZN ? R ZN . ? F ZN 155 ? 1_555 ND1 ? F HIS 71  ? F HIS 71  ? 1_555 117.2 ? 
62 ND1 ? F HIS 63  ? F HIS 63  ? 1_555 ZN ? R ZN . ? F ZN 155 ? 1_555 ND1 ? F HIS 80  ? F HIS 80  ? 1_555 108.5 ? 
63 ND1 ? F HIS 71  ? F HIS 71  ? 1_555 ZN ? R ZN . ? F ZN 155 ? 1_555 ND1 ? F HIS 80  ? F HIS 80  ? 1_555 124.6 ? 
64 ND1 ? F HIS 63  ? F HIS 63  ? 1_555 ZN ? R ZN . ? F ZN 155 ? 1_555 OD1 ? F ASP 83  ? F ASP 83  ? 1_555 85.5  ? 
65 ND1 ? F HIS 71  ? F HIS 71  ? 1_555 ZN ? R ZN . ? F ZN 155 ? 1_555 OD1 ? F ASP 83  ? F ASP 83  ? 1_555 97.5  ? 
66 ND1 ? F HIS 80  ? F HIS 80  ? 1_555 ZN ? R ZN . ? F ZN 155 ? 1_555 OD1 ? F ASP 83  ? F ASP 83  ? 1_555 116.2 ? 
# 
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 2010-08-11 
2 'Structure model' 1 1 2011-07-13 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Version format compliance' 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.pdbx_refine_id 
1 ? refined -13.1880 -35.3838 16.2062 0.2460 0.2065 0.0411 -0.0111 0.0874  0.0655 3.8655 7.3103 2.6896 0.6540  0.2053  -1.4116 
-0.1068 0.0404  0.0664  0.1620 0.0159  -0.0846 -0.2823 0.1157  -0.1577 'X-RAY DIFFRACTION' 
2 ? refined -13.7200 -7.2764  16.4854 0.2797 0.1406 0.1920 -0.0360 0.0747  0.1288 3.6428 4.9351 4.5987 -0.5283 -0.3909 0.5378  
0.0060  0.0494  -0.0554 0.2531 0.4279  0.0679  -0.1449 -0.2402 0.1853  'X-RAY DIFFRACTION' 
3 ? refined 3.1534   -62.8182 16.0965 0.3244 0.3779 0.2983 0.0321  0.0217  0.1339 8.0936 6.1090 1.5459 -2.1316 -0.3708 0.4391  
0.2539  -0.1000 -0.1538 0.1976 -0.2738 0.2018  -0.1149 -0.2134 -0.0046 'X-RAY DIFFRACTION' 
4 ? refined 27.4514  -76.9018 17.1263 0.2501 0.2607 0.1647 0.0332  -0.0712 0.0643 7.4505 6.2711 3.2117 -1.3879 0.2650  -0.1527 
-0.0083 -0.0107 0.0190  0.0554 0.0809  -0.0999 -0.0526 0.1699  -0.0504 'X-RAY DIFFRACTION' 
5 ? refined -28.6236 -62.9948 16.5580 0.2930 0.2862 0.0931 -0.0548 0.0743  0.1109 7.9923 7.2983 2.2062 3.3145  1.0280  0.6191  
-0.1012 -0.0246 0.1258  0.2566 -0.3693 -0.3401 -0.2615 0.1414  0.2307  'X-RAY DIFFRACTION' 
6 ? refined -52.8178 -77.3172 17.4908 0.2474 0.2393 0.1123 -0.0572 -0.0032 0.0878 6.0208 4.7563 2.9501 1.1792  -0.2283 -0.5861 
-0.0264 -0.0103 0.0367  0.1958 -0.4040 -0.1362 -0.3508 -0.1429 -0.1137 'X-RAY DIFFRACTION' 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.selection_details 
1 1 A 1 A 153 ? . . . . 'X-RAY DIFFRACTION' ? 
2 2 B 1 B 153 ? . . . . 'X-RAY DIFFRACTION' ? 
3 3 C 1 C 153 ? . . . . 'X-RAY DIFFRACTION' ? 
4 4 D 1 D 153 ? . . . . 'X-RAY DIFFRACTION' ? 
5 5 E 1 E 153 ? . . . . 'X-RAY DIFFRACTION' ? 
6 6 F 1 F 153 ? . . . . 'X-RAY DIFFRACTION' ? 
# 
loop_
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
_software.pdbx_ordinal 
XSCALE      .        ?               package 'Wolfgang Kabsch'    ?                     'data scaling'    
http://www.mpimf-heidelberg.mpg.de/~kabsch/xds/html_doc/xscale_program.html ?          ? 1 
REFMAC      5.5.0102 ?               program 'Garib N. Murshudov' garib@ysbl.york.ac.uk refinement        
http://www.ccp4.ac.uk/dist/html/refmac5.html                                Fortran_77 ? 2 
PDB_EXTRACT 3.006    'June 11, 2008' package PDB                  help@deposit.rcsb.org 'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/                                   C++        ? 3 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    OD2 
_pdbx_validate_symm_contact.auth_asym_id_1    B 
_pdbx_validate_symm_contact.auth_comp_id_1    ASP 
_pdbx_validate_symm_contact.auth_seq_id_1     90 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    NZ 
_pdbx_validate_symm_contact.auth_asym_id_2    D 
_pdbx_validate_symm_contact.auth_comp_id_2    LYS 
_pdbx_validate_symm_contact.auth_seq_id_2     91 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   10_455 
_pdbx_validate_symm_contact.dist              1.75 
# 
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 26  ? ? 57.06   12.54  
2  1 ALA A 55  ? ? -112.85 68.08  
3  1 ASP A 90  ? ? -35.77  169.17 
4  1 SER A 98  ? ? -164.21 114.75 
5  1 LYS A 136 ? ? -126.72 -59.89 
6  1 ASN B 26  ? ? 56.56   15.69  
7  1 ALA B 55  ? ? -112.38 68.74  
8  1 ASP B 90  ? ? -36.63  169.33 
9  1 LYS B 136 ? ? -125.09 -61.00 
10 1 ASN C 26  ? ? 56.07   14.54  
11 1 ALA C 55  ? ? -113.74 69.22  
12 1 ASP C 90  ? ? -33.01  169.95 
13 1 SER C 98  ? ? -165.71 117.95 
14 1 LYS C 136 ? ? -123.69 -61.44 
15 1 ASN D 26  ? ? 55.34   15.57  
16 1 ALA D 55  ? ? -113.31 69.83  
17 1 ASP D 90  ? ? -33.08  170.36 
18 1 SER D 98  ? ? -164.64 118.06 
19 1 LYS D 136 ? ? -127.16 -59.06 
20 1 ASN E 26  ? ? 53.71   16.50  
21 1 ALA E 55  ? ? -112.97 70.06  
22 1 ASP E 90  ? ? -33.88  171.83 
23 1 SER E 98  ? ? -163.21 118.84 
24 1 LYS E 136 ? ? -124.45 -57.74 
25 1 ASN F 26  ? ? 55.21   12.93  
26 1 ALA F 55  ? ? -113.44 68.74  
27 1 ASP F 90  ? ? -34.23  168.90 
28 1 SER F 98  ? ? -162.44 116.62 
29 1 LYS F 136 ? ? -125.95 -59.86 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'COPPER (II) ION' CU 
3 'ZINC ION'        ZN 
# 
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 CU 1 154 154 CU CU A . 
H 3 ZN 1 155 155 ZN ZN A . 
I 2 CU 1 154 154 CU CU B . 
J 3 ZN 1 155 155 ZN ZN B . 
K 2 CU 1 154 154 CU CU C . 
L 3 ZN 1 155 155 ZN ZN C . 
M 2 CU 1 154 154 CU CU D . 
N 3 ZN 1 155 155 ZN ZN D . 
O 2 CU 1 154 154 CU CU E . 
P 3 ZN 1 155 155 ZN ZN E . 
Q 2 CU 1 154 154 CU CU F . 
R 3 ZN 1 155 155 ZN ZN F . 
# 
