data_1SOS
# 
_entry.id   1SOS 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.287 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   1SOS         
WWPDB D_1000176453 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        1SOS 
_pdbx_database_status.recvd_initial_deposition_date   1992-02-11 
_pdbx_database_status.deposit_site                    ? 
_pdbx_database_status.process_site                    BNL 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Parge, H.E.'     1 
'Hallewell, R.A.' 2 
'Tainer, J.A.'    3 
# 
_citation.id                        primary 
_citation.title                     
'Atomic structures of wild-type and thermostable mutant recombinant human Cu,Zn superoxide dismutase.' 
_citation.journal_abbrev            Proc.Natl.Acad.Sci.USA 
_citation.journal_volume            89 
_citation.page_first                6109 
_citation.page_last                 6113 
_citation.year                      1992 
_citation.journal_id_ASTM           PNASA6 
_citation.country                   US 
_citation.journal_id_ISSN           0027-8424 
_citation.journal_id_CSD            0040 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   1463506 
_citation.pdbx_database_id_DOI      10.1073/pnas.89.13.6109 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Parge, H.E.'     1 
primary 'Hallewell, R.A.' 2 
primary 'Tainer, J.A.'    3 
# 
_cell.entry_id           1SOS 
_cell.length_a           205.200 
_cell.length_b           167.000 
_cell.length_c           145.500 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              80 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         1SOS 
_symmetry.space_group_name_H-M             'C 2 2 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
# 
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' 15805.468 10  1.15.1.1 ? ? ? 
2 non-polymer syn 'COPPER (II) ION'      63.546    10  ?        ? ? ? 
3 non-polymer syn 'ZINC ION'             65.409    10  ?        ? ? ? 
4 non-polymer syn 'SULFATE ION'          96.063    2   ?        ? ? ? 
5 water       nat water                  18.015    499 ?        ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;(ACE)ATKAVAVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPK
DEERHVGDLGNVTADKDGVADVSIEDSVISLSGDHSIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;XATKAVAVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEER
HVGDLGNVTADKDGVADVSIEDSVISLSGDHSIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_strand_id                 A,F,B,G,C,H,D,I,E,J 
_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   ACE n 
1 2   ALA n 
1 3   THR n 
1 4   LYS n 
1 5   ALA n 
1 6   VAL n 
1 7   ALA n 
1 8   VAL n 
1 9   LEU n 
1 10  LYS n 
1 11  GLY n 
1 12  ASP n 
1 13  GLY n 
1 14  PRO n 
1 15  VAL n 
1 16  GLN n 
1 17  GLY n 
1 18  ILE n 
1 19  ILE n 
1 20  ASN n 
1 21  PHE n 
1 22  GLU n 
1 23  GLN n 
1 24  LYS n 
1 25  GLU n 
1 26  SER n 
1 27  ASN n 
1 28  GLY n 
1 29  PRO n 
1 30  VAL n 
1 31  LYS n 
1 32  VAL n 
1 33  TRP n 
1 34  GLY n 
1 35  SER n 
1 36  ILE n 
1 37  LYS n 
1 38  GLY n 
1 39  LEU n 
1 40  THR n 
1 41  GLU n 
1 42  GLY n 
1 43  LEU n 
1 44  HIS n 
1 45  GLY n 
1 46  PHE n 
1 47  HIS n 
1 48  VAL n 
1 49  HIS n 
1 50  GLU n 
1 51  PHE n 
1 52  GLY n 
1 53  ASP n 
1 54  ASN n 
1 55  THR n 
1 56  ALA n 
1 57  GLY n 
1 58  CYS n 
1 59  THR n 
1 60  SER n 
1 61  ALA n 
1 62  GLY n 
1 63  PRO n 
1 64  HIS n 
1 65  PHE n 
1 66  ASN n 
1 67  PRO n 
1 68  LEU n 
1 69  SER n 
1 70  ARG n 
1 71  LYS n 
1 72  HIS n 
1 73  GLY n 
1 74  GLY n 
1 75  PRO n 
1 76  LYS n 
1 77  ASP n 
1 78  GLU n 
1 79  GLU n 
1 80  ARG n 
1 81  HIS n 
1 82  VAL n 
1 83  GLY n 
1 84  ASP n 
1 85  LEU n 
1 86  GLY n 
1 87  ASN n 
1 88  VAL n 
1 89  THR n 
1 90  ALA n 
1 91  ASP n 
1 92  LYS n 
1 93  ASP n 
1 94  GLY n 
1 95  VAL n 
1 96  ALA n 
1 97  ASP n 
1 98  VAL n 
1 99  SER n 
1 100 ILE n 
1 101 GLU n 
1 102 ASP n 
1 103 SER n 
1 104 VAL n 
1 105 ILE n 
1 106 SER n 
1 107 LEU n 
1 108 SER n 
1 109 GLY n 
1 110 ASP n 
1 111 HIS n 
1 112 SER n 
1 113 ILE n 
1 114 ILE n 
1 115 GLY n 
1 116 ARG n 
1 117 THR n 
1 118 LEU n 
1 119 VAL n 
1 120 VAL n 
1 121 HIS n 
1 122 GLU n 
1 123 LYS n 
1 124 ALA n 
1 125 ASP n 
1 126 ASP n 
1 127 LEU n 
1 128 GLY n 
1 129 LYS n 
1 130 GLY n 
1 131 GLY n 
1 132 ASN n 
1 133 GLU n 
1 134 GLU n 
1 135 SER n 
1 136 THR n 
1 137 LYS n 
1 138 THR n 
1 139 GLY n 
1 140 ASN n 
1 141 ALA n 
1 142 GLY n 
1 143 SER n 
1 144 ARG n 
1 145 LEU n 
1 146 ALA n 
1 147 CYS n 
1 148 GLY n 
1 149 VAL n 
1 150 ILE n 
1 151 GLY n 
1 152 ILE n 
1 153 ALA n 
1 154 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                     Homo 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      '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      ? 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     ? 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_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_align_begin           1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.pdbx_seq_one_letter_code   ? 
# 
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 1SOS A 2 ? 154 ? P00441 1 ? 153 ? 1 153 
2  1 1SOS F 2 ? 154 ? P00441 1 ? 153 ? 1 153 
3  1 1SOS B 2 ? 154 ? P00441 1 ? 153 ? 1 153 
4  1 1SOS G 2 ? 154 ? P00441 1 ? 153 ? 1 153 
5  1 1SOS C 2 ? 154 ? P00441 1 ? 153 ? 1 153 
6  1 1SOS H 2 ? 154 ? P00441 1 ? 153 ? 1 153 
7  1 1SOS D 2 ? 154 ? P00441 1 ? 153 ? 1 153 
8  1 1SOS I 2 ? 154 ? P00441 1 ? 153 ? 1 153 
9  1 1SOS E 2 ? 154 ? P00441 1 ? 153 ? 1 153 
10 1 1SOS J 2 ? 154 ? P00441 1 ? 153 ? 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 
ACE non-polymer         . 'ACETYL GROUP'    ? 'C2 H4 O'        44.053  
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 
HOH non-polymer         . WATER             ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE        ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE           ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE            ? 'C6 H15 N2 O2 1' 147.195 
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 
SO4 non-polymer         . 'SULFATE ION'     ? 'O4 S -2'        96.063  
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.entry_id          1SOS 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   ? 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      3.94 
_exptl_crystal.density_percent_sol   68.80 
_exptl_crystal.description           ? 
# 
_refine.entry_id                                 1SOS 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             ? 
_refine.ls_d_res_high                            2.5 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.202 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        11120 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         30 
_refine_hist.number_atoms_solvent             499 
_refine_hist.number_atoms_total               11649 
_refine_hist.d_res_high                       2.5 
_refine_hist.d_res_low                        . 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
x_bond_d    0.017 ? ? ? 'X-RAY DIFFRACTION' ? 
x_angle_deg 3.50  ? ? ? 'X-RAY DIFFRACTION' ? 
# 
loop_
_struct_ncs_oper.id 
_struct_ncs_oper.code 
_struct_ncs_oper.details 
_struct_ncs_oper.matrix[1][1] 
_struct_ncs_oper.matrix[1][2] 
_struct_ncs_oper.matrix[1][3] 
_struct_ncs_oper.matrix[2][1] 
_struct_ncs_oper.matrix[2][2] 
_struct_ncs_oper.matrix[2][3] 
_struct_ncs_oper.matrix[3][1] 
_struct_ncs_oper.matrix[3][2] 
_struct_ncs_oper.matrix[3][3] 
_struct_ncs_oper.vector[1] 
_struct_ncs_oper.vector[2] 
_struct_ncs_oper.vector[3] 
1 given ? -0.982700 0.008000  0.185000  0.018200  -0.990100 0.139400  0.184300  0.140300  0.972800 120.63000 56.45800  -15.30400 
2 given ? -0.463700 -0.885800 0.015100  0.886000  -0.463700 0.008200  -0.000200 0.017200  0.999900 106.40600 -66.09600 0.01700   
3 given ? 0.467000  0.867400  0.171900  -0.883700 0.450900  0.125700  0.031500  -0.210600 0.977100 15.10400  123.62500 -4.28600  
4 given ? -0.534900 0.842700  0.060800  -0.844400 -0.535700 -0.003200 0.029900  -0.053000 0.998100 111.29400 61.00000  -3.26200  
5 given ? 0.522700  -0.838500 0.154100  0.832900  0.540800  0.117600  -0.181900 0.066900  0.981000 10.87600  -2.13100  11.15100  
6 given ? -0.981000 -0.026900 -0.192300 0.028200  -0.999600 -0.004000 -0.192200 -0.009400 0.981300 208.83600 28.44200  29.48700  
7 given ? 0.936100  0.007600  0.351500  -0.056900 0.989900  0.130100  -0.347000 -0.141900 0.927100 -79.86000 33.91200  53.15700  
8 given ? 0.476600  0.879000  0.010300  -0.877900 0.476600  -0.046600 -0.045800 0.013200  0.998900 -19.71400 102.41300 9.15900   
9 given ? -0.475300 -0.865900 0.155600  0.876000  -0.449400 0.175200  -0.081800 0.219600  0.972200 142.20700 -44.74400 5.36500   
# 
_struct.entry_id                  1SOS 
_struct.title                     
'ATOMIC STRUCTURES OF WILD-TYPE AND THERMOSTABLE MUTANT RECOMBINANT HUMAN CU, ZN SUPEROXIDE DISMUTASE' 
_struct.pdbx_descriptor           
'SUPEROXIDE DISMUTASE (E.C.1.15.1.1) MUTANT WITH CYS 6 REPLACED BY ALA AND CYS 111 REPLACED BY SER (C6A, C111S)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        1SOS 
_struct_keywords.pdbx_keywords   'OXIDOREDUCTASE (SUPEROXIDE ACCEPTOR)' 
_struct_keywords.text            'OXIDOREDUCTASE (SUPEROXIDE ACCEPTOR)' 
# 
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 1 ? 
H  N N 1 ? 
I  N N 1 ? 
J  N N 1 ? 
K  N N 2 ? 
L  N N 3 ? 
M  N N 2 ? 
N  N N 3 ? 
O  N N 4 ? 
P  N N 2 ? 
Q  N N 3 ? 
R  N N 2 ? 
S  N N 3 ? 
T  N N 2 ? 
U  N N 3 ? 
V  N N 2 ? 
W  N N 3 ? 
X  N N 2 ? 
Y  N N 3 ? 
Z  N N 2 ? 
AA N N 3 ? 
BA N N 4 ? 
CA N N 2 ? 
DA N N 3 ? 
EA N N 2 ? 
FA N N 3 ? 
GA N N 5 ? 
HA N N 5 ? 
IA N N 5 ? 
JA N N 5 ? 
KA N N 5 ? 
LA N N 5 ? 
MA N N 5 ? 
NA N N 5 ? 
OA N N 5 ? 
PA N N 5 ? 
# 
loop_
_struct_biol.id 
1 
2 
3 
4 
5 
# 
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  HA GLU A 134 ? THR A 138 ? GLU A 133 THR A 137 1 'SINGLE-LOOP ALPHA-HELIX' 5 
HELX_P HELX_P2  HF GLU B 134 ? THR B 138 ? GLU F 133 THR F 137 1 'SINGLE-LOOP ALPHA-HELIX' 5 
HELX_P HELX_P3  HB GLU C 134 ? THR C 138 ? GLU B 133 THR B 137 1 'SINGLE-LOOP ALPHA-HELIX' 5 
HELX_P HELX_P4  HG GLU D 134 ? THR D 138 ? GLU G 133 THR G 137 1 'SINGLE-LOOP ALPHA-HELIX' 5 
HELX_P HELX_P5  HC GLU E 134 ? THR E 138 ? GLU C 133 THR C 137 1 'SINGLE-LOOP ALPHA-HELIX' 5 
HELX_P HELX_P6  HH GLU F 134 ? THR F 138 ? GLU H 133 THR H 137 1 'SINGLE-LOOP ALPHA-HELIX' 5 
HELX_P HELX_P7  HD GLU G 134 ? THR G 138 ? GLU D 133 THR D 137 1 'SINGLE-LOOP ALPHA-HELIX' 5 
HELX_P HELX_P8  HI GLU H 134 ? THR H 138 ? GLU I 133 THR I 137 1 'SINGLE-LOOP ALPHA-HELIX' 5 
HELX_P HELX_P9  HE GLU I 134 ? THR I 138 ? GLU E 133 THR E 137 1 'SINGLE-LOOP ALPHA-HELIX' 5 
HELX_P HELX_P10 HJ GLU J 134 ? THR J 138 ? GLU J 133 THR J 137 1 'SINGLE-LOOP ALPHA-HELIX' 5 
# 
_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 58 SG ? ? ? 1_555 A CYS 147 SG  ? ? A CYS 57  A CYS 146 1_555 ? ? ? ? ? ? ? 2.010 ? 
disulf2  disulf ? ? B  CYS 58 SG ? ? ? 1_555 B CYS 147 SG  ? ? F CYS 57  F CYS 146 1_555 ? ? ? ? ? ? ? 2.024 ? 
disulf3  disulf ? ? C  CYS 58 SG ? ? ? 1_555 C CYS 147 SG  ? ? B CYS 57  B CYS 146 1_555 ? ? ? ? ? ? ? 2.025 ? 
disulf4  disulf ? ? D  CYS 58 SG ? ? ? 1_555 D CYS 147 SG  ? ? G CYS 57  G CYS 146 1_555 ? ? ? ? ? ? ? 2.015 ? 
disulf5  disulf ? ? E  CYS 58 SG ? ? ? 1_555 E CYS 147 SG  ? ? C CYS 57  C CYS 146 1_555 ? ? ? ? ? ? ? 1.995 ? 
disulf6  disulf ? ? F  CYS 58 SG ? ? ? 1_555 F CYS 147 SG  ? ? H CYS 57  H CYS 146 1_555 ? ? ? ? ? ? ? 2.002 ? 
disulf7  disulf ? ? G  CYS 58 SG ? ? ? 1_555 G CYS 147 SG  ? ? D CYS 57  D CYS 146 1_555 ? ? ? ? ? ? ? 2.001 ? 
disulf8  disulf ? ? H  CYS 58 SG ? ? ? 1_555 H CYS 147 SG  ? ? I CYS 57  I CYS 146 1_555 ? ? ? ? ? ? ? 2.019 ? 
disulf9  disulf ? ? I  CYS 58 SG ? ? ? 1_555 I CYS 147 SG  ? ? E CYS 57  E CYS 146 1_555 ? ? ? ? ? ? ? 2.032 ? 
disulf10 disulf ? ? J  CYS 58 SG ? ? ? 1_555 J CYS 147 SG  ? ? J CYS 57  J CYS 146 1_555 ? ? ? ? ? ? ? 2.015 ? 
covale1  covale ? ? A  ACE 1  C  ? ? ? 1_555 A ALA 2   N   ? ? A ACE 0   A ALA 1   1_555 ? ? ? ? ? ? ? 1.344 ? 
covale2  covale ? ? B  ACE 1  C  ? ? ? 1_555 B ALA 2   N   ? ? F ACE 0   F ALA 1   1_555 ? ? ? ? ? ? ? 1.357 ? 
covale3  covale ? ? C  ACE 1  C  ? ? ? 1_555 C ALA 2   N   ? ? B ACE 0   B ALA 1   1_555 ? ? ? ? ? ? ? 1.341 ? 
covale4  covale ? ? D  ACE 1  C  ? ? ? 1_555 D ALA 2   N   ? ? G ACE 0   G ALA 1   1_555 ? ? ? ? ? ? ? 1.342 ? 
covale5  covale ? ? E  ACE 1  C  ? ? ? 1_555 E ALA 2   N   ? ? C ACE 0   C ALA 1   1_555 ? ? ? ? ? ? ? 1.345 ? 
covale6  covale ? ? F  ACE 1  C  ? ? ? 1_555 F ALA 2   N   ? ? H ACE 0   H ALA 1   1_555 ? ? ? ? ? ? ? 1.343 ? 
covale7  covale ? ? G  ACE 1  C  ? ? ? 1_555 G ALA 2   N   ? ? D ACE 0   D ALA 1   1_555 ? ? ? ? ? ? ? 1.355 ? 
covale8  covale ? ? H  ACE 1  C  ? ? ? 1_555 H ALA 2   N   ? ? I ACE 0   I ALA 1   1_555 ? ? ? ? ? ? ? 1.345 ? 
covale9  covale ? ? I  ACE 1  C  ? ? ? 1_555 I ALA 2   N   ? ? E ACE 0   E ALA 1   1_555 ? ? ? ? ? ? ? 1.341 ? 
covale10 covale ? ? J  ACE 1  C  ? ? ? 1_555 J ALA 2   N   ? ? J ACE 0   J ALA 1   1_555 ? ? ? ? ? ? ? 1.342 ? 
metalc1  metalc ? ? K  CU  .  CU ? ? ? 1_555 A HIS 49  NE2 ? ? A CU  154 A HIS 48  1_555 ? ? ? ? ? ? ? 2.058 ? 
metalc2  metalc ? ? K  CU  .  CU ? ? ? 1_555 A HIS 64  NE2 ? ? A CU  154 A HIS 63  1_555 ? ? ? ? ? ? ? 2.124 ? 
metalc3  metalc ? ? K  CU  .  CU ? ? ? 1_555 A HIS 121 NE2 ? ? A CU  154 A HIS 120 1_555 ? ? ? ? ? ? ? 2.068 ? 
metalc4  metalc ? ? K  CU  .  CU ? ? ? 1_555 A HIS 47  ND1 ? ? A CU  154 A HIS 46  1_555 ? ? ? ? ? ? ? 2.066 ? 
metalc5  metalc ? ? L  ZN  .  ZN ? ? ? 1_555 A HIS 72  ND1 ? ? A ZN  155 A HIS 71  1_555 ? ? ? ? ? ? ? 2.058 ? 
metalc6  metalc ? ? L  ZN  .  ZN ? ? ? 1_555 A ASP 84  OD1 ? ? A ZN  155 A ASP 83  1_555 ? ? ? ? ? ? ? 1.923 ? 
metalc7  metalc ? ? L  ZN  .  ZN ? ? ? 1_555 A HIS 64  ND1 ? ? A ZN  155 A HIS 63  1_555 ? ? ? ? ? ? ? 2.102 ? 
metalc8  metalc ? ? L  ZN  .  ZN ? ? ? 1_555 A HIS 81  ND1 ? ? A ZN  155 A HIS 80  1_555 ? ? ? ? ? ? ? 2.044 ? 
metalc9  metalc ? ? P  CU  .  CU ? ? ? 1_555 C HIS 64  NE2 ? ? B CU  154 B HIS 63  1_555 ? ? ? ? ? ? ? 2.115 ? 
metalc10 metalc ? ? P  CU  .  CU ? ? ? 1_555 C HIS 121 NE2 ? ? B CU  154 B HIS 120 1_555 ? ? ? ? ? ? ? 2.041 ? 
metalc11 metalc ? ? P  CU  .  CU ? ? ? 1_555 C HIS 49  NE2 ? ? B CU  154 B HIS 48  1_555 ? ? ? ? ? ? ? 2.077 ? 
metalc12 metalc ? ? P  CU  .  CU ? ? ? 1_555 C HIS 47  ND1 ? ? B CU  154 B HIS 46  1_555 ? ? ? ? ? ? ? 2.027 ? 
metalc13 metalc ? ? Q  ZN  .  ZN ? ? ? 1_555 C HIS 81  ND1 ? ? B ZN  155 B HIS 80  1_555 ? ? ? ? ? ? ? 2.055 ? 
metalc14 metalc ? ? Q  ZN  .  ZN ? ? ? 1_555 C ASP 84  OD1 ? ? B ZN  155 B ASP 83  1_555 ? ? ? ? ? ? ? 1.966 ? 
metalc15 metalc ? ? Q  ZN  .  ZN ? ? ? 1_555 C HIS 64  ND1 ? ? B ZN  155 B HIS 63  1_555 ? ? ? ? ? ? ? 2.121 ? 
metalc16 metalc ? ? Q  ZN  .  ZN ? ? ? 1_555 C HIS 72  ND1 ? ? B ZN  155 B HIS 71  1_555 ? ? ? ? ? ? ? 2.076 ? 
metalc17 metalc ? ? T  CU  .  CU ? ? ? 1_555 E HIS 49  NE2 ? ? C CU  154 C HIS 48  1_555 ? ? ? ? ? ? ? 2.085 ? 
metalc18 metalc ? ? T  CU  .  CU ? ? ? 1_555 E HIS 121 NE2 ? ? C CU  154 C HIS 120 1_555 ? ? ? ? ? ? ? 2.035 ? 
metalc19 metalc ? ? T  CU  .  CU ? ? ? 1_555 E HIS 47  ND1 ? ? C CU  154 C HIS 46  1_555 ? ? ? ? ? ? ? 2.066 ? 
metalc20 metalc ? ? T  CU  .  CU ? ? ? 1_555 E HIS 64  NE2 ? ? C CU  154 C HIS 63  1_555 ? ? ? ? ? ? ? 2.080 ? 
metalc21 metalc ? ? U  ZN  .  ZN ? ? ? 1_555 E HIS 72  ND1 ? ? C ZN  155 C HIS 71  1_555 ? ? ? ? ? ? ? 2.062 ? 
metalc22 metalc ? ? U  ZN  .  ZN ? ? ? 1_555 E ASP 84  OD1 ? ? C ZN  155 C ASP 83  1_555 ? ? ? ? ? ? ? 1.943 ? 
metalc23 metalc ? ? U  ZN  .  ZN ? ? ? 1_555 E HIS 81  ND1 ? ? C ZN  155 C HIS 80  1_555 ? ? ? ? ? ? ? 2.046 ? 
metalc24 metalc ? ? U  ZN  .  ZN ? ? ? 1_555 E HIS 64  ND1 ? ? C ZN  155 C HIS 63  1_555 ? ? ? ? ? ? ? 2.079 ? 
metalc25 metalc ? ? X  CU  .  CU ? ? ? 1_555 G HIS 47  ND1 ? ? D CU  154 D HIS 46  1_555 ? ? ? ? ? ? ? 2.044 ? 
metalc26 metalc ? ? X  CU  .  CU ? ? ? 1_555 G HIS 49  NE2 ? ? D CU  154 D HIS 48  1_555 ? ? ? ? ? ? ? 2.092 ? 
metalc27 metalc ? ? X  CU  .  CU ? ? ? 1_555 G HIS 64  NE2 ? ? D CU  154 D HIS 63  1_555 ? ? ? ? ? ? ? 2.108 ? 
metalc28 metalc ? ? X  CU  .  CU ? ? ? 1_555 G HIS 121 NE2 ? ? D CU  154 D HIS 120 1_555 ? ? ? ? ? ? ? 2.049 ? 
metalc29 metalc ? ? Y  ZN  .  ZN ? ? ? 1_555 G HIS 64  ND1 ? ? D ZN  155 D HIS 63  1_555 ? ? ? ? ? ? ? 2.125 ? 
metalc30 metalc ? ? Y  ZN  .  ZN ? ? ? 1_555 G HIS 72  ND1 ? ? D ZN  155 D HIS 71  1_555 ? ? ? ? ? ? ? 2.081 ? 
metalc31 metalc ? ? Y  ZN  .  ZN ? ? ? 1_555 G HIS 81  ND1 ? ? D ZN  155 D HIS 80  1_555 ? ? ? ? ? ? ? 2.093 ? 
metalc32 metalc ? ? Y  ZN  .  ZN ? ? ? 1_555 G ASP 84  OD1 ? ? D ZN  155 D ASP 83  1_555 ? ? ? ? ? ? ? 1.955 ? 
metalc33 metalc ? ? CA CU  .  CU ? ? ? 1_555 I HIS 49  NE2 ? ? E CU  154 E HIS 48  1_555 ? ? ? ? ? ? ? 2.084 ? 
metalc34 metalc ? ? CA CU  .  CU ? ? ? 1_555 I HIS 47  ND1 ? ? E CU  154 E HIS 46  1_555 ? ? ? ? ? ? ? 2.036 ? 
metalc35 metalc ? ? CA CU  .  CU ? ? ? 1_555 I HIS 121 NE2 ? ? E CU  154 E HIS 120 1_555 ? ? ? ? ? ? ? 2.048 ? 
metalc36 metalc ? ? CA CU  .  CU ? ? ? 1_555 I HIS 64  NE2 ? ? E CU  154 E HIS 63  1_555 ? ? ? ? ? ? ? 2.121 ? 
metalc37 metalc ? ? DA ZN  .  ZN ? ? ? 1_555 I HIS 81  ND1 ? ? E ZN  155 E HIS 80  1_555 ? ? ? ? ? ? ? 2.079 ? 
metalc38 metalc ? ? DA ZN  .  ZN ? ? ? 1_555 I HIS 72  ND1 ? ? E ZN  155 E HIS 71  1_555 ? ? ? ? ? ? ? 2.097 ? 
metalc39 metalc ? ? DA ZN  .  ZN ? ? ? 1_555 I ASP 84  OD2 ? ? E ZN  155 E ASP 83  1_555 ? ? ? ? ? ? ? 2.512 ? 
metalc40 metalc ? ? DA ZN  .  ZN ? ? ? 1_555 I HIS 64  ND1 ? ? E ZN  155 E HIS 63  1_555 ? ? ? ? ? ? ? 2.124 ? 
metalc41 metalc ? ? DA ZN  .  ZN ? ? ? 1_555 I ASP 84  OD1 ? ? E ZN  155 E ASP 83  1_555 ? ? ? ? ? ? ? 1.964 ? 
metalc42 metalc ? ? M  CU  .  CU ? ? ? 1_555 B HIS 49  NE2 ? ? F CU  154 F HIS 48  1_555 ? ? ? ? ? ? ? 2.094 ? 
metalc43 metalc ? ? M  CU  .  CU ? ? ? 1_555 B HIS 64  NE2 ? ? F CU  154 F HIS 63  1_555 ? ? ? ? ? ? ? 2.121 ? 
metalc44 metalc ? ? M  CU  .  CU ? ? ? 1_555 B HIS 121 NE2 ? ? F CU  154 F HIS 120 1_555 ? ? ? ? ? ? ? 2.057 ? 
metalc45 metalc ? ? M  CU  .  CU ? ? ? 1_555 B HIS 47  ND1 ? ? F CU  154 F HIS 46  1_555 ? ? ? ? ? ? ? 2.030 ? 
metalc46 metalc ? ? N  ZN  .  ZN ? ? ? 1_555 B ASP 84  OD1 ? ? F ZN  155 F ASP 83  1_555 ? ? ? ? ? ? ? 1.951 ? 
metalc47 metalc ? ? N  ZN  .  ZN ? ? ? 1_555 B HIS 72  ND1 ? ? F ZN  155 F HIS 71  1_555 ? ? ? ? ? ? ? 2.050 ? 
metalc48 metalc ? ? N  ZN  .  ZN ? ? ? 1_555 B HIS 64  ND1 ? ? F ZN  155 F HIS 63  1_555 ? ? ? ? ? ? ? 2.088 ? 
metalc49 metalc ? ? N  ZN  .  ZN ? ? ? 1_555 B HIS 81  ND1 ? ? F ZN  155 F HIS 80  1_555 ? ? ? ? ? ? ? 2.063 ? 
metalc50 metalc ? ? R  CU  .  CU ? ? ? 1_555 D HIS 49  NE2 ? ? G CU  154 G HIS 48  1_555 ? ? ? ? ? ? ? 2.081 ? 
metalc51 metalc ? ? R  CU  .  CU ? ? ? 1_555 D HIS 121 NE2 ? ? G CU  154 G HIS 120 1_555 ? ? ? ? ? ? ? 2.061 ? 
metalc52 metalc ? ? R  CU  .  CU ? ? ? 1_555 D HIS 64  NE2 ? ? G CU  154 G HIS 63  1_555 ? ? ? ? ? ? ? 2.071 ? 
metalc53 metalc ? ? R  CU  .  CU ? ? ? 1_555 D HIS 47  ND1 ? ? G CU  154 G HIS 46  1_555 ? ? ? ? ? ? ? 2.051 ? 
metalc54 metalc ? ? S  ZN  .  ZN ? ? ? 1_555 D ASP 84  OD1 ? ? G ZN  155 G ASP 83  1_555 ? ? ? ? ? ? ? 1.948 ? 
metalc55 metalc ? ? S  ZN  .  ZN ? ? ? 1_555 D HIS 64  ND1 ? ? G ZN  155 G HIS 63  1_555 ? ? ? ? ? ? ? 2.071 ? 
metalc56 metalc ? ? S  ZN  .  ZN ? ? ? 1_555 D ASP 84  OD2 ? ? G ZN  155 G ASP 83  1_555 ? ? ? ? ? ? ? 2.692 ? 
metalc57 metalc ? ? S  ZN  .  ZN ? ? ? 1_555 D HIS 81  ND1 ? ? G ZN  155 G HIS 80  1_555 ? ? ? ? ? ? ? 2.053 ? 
metalc58 metalc ? ? S  ZN  .  ZN ? ? ? 1_555 D HIS 72  ND1 ? ? G ZN  155 G HIS 71  1_555 ? ? ? ? ? ? ? 2.070 ? 
metalc59 metalc ? ? V  CU  .  CU ? ? ? 1_555 F HIS 47  ND1 ? ? H CU  154 H HIS 46  1_555 ? ? ? ? ? ? ? 2.038 ? 
metalc60 metalc ? ? V  CU  .  CU ? ? ? 1_555 F HIS 49  NE2 ? ? H CU  154 H HIS 48  1_555 ? ? ? ? ? ? ? 2.075 ? 
metalc61 metalc ? ? V  CU  .  CU ? ? ? 1_555 F HIS 121 NE2 ? ? H CU  154 H HIS 120 1_555 ? ? ? ? ? ? ? 2.047 ? 
metalc62 metalc ? ? V  CU  .  CU ? ? ? 1_555 F HIS 64  NE2 ? ? H CU  154 H HIS 63  1_555 ? ? ? ? ? ? ? 2.085 ? 
metalc63 metalc ? ? W  ZN  .  ZN ? ? ? 1_555 F HIS 72  ND1 ? ? H ZN  155 H HIS 71  1_555 ? ? ? ? ? ? ? 2.051 ? 
metalc64 metalc ? ? W  ZN  .  ZN ? ? ? 1_555 F HIS 64  ND1 ? ? H ZN  155 H HIS 63  1_555 ? ? ? ? ? ? ? 2.109 ? 
metalc65 metalc ? ? W  ZN  .  ZN ? ? ? 1_555 F HIS 81  ND1 ? ? H ZN  155 H HIS 80  1_555 ? ? ? ? ? ? ? 2.085 ? 
metalc66 metalc ? ? W  ZN  .  ZN ? ? ? 1_555 F ASP 84  OD1 ? ? H ZN  155 H ASP 83  1_555 ? ? ? ? ? ? ? 1.919 ? 
metalc67 metalc ? ? Z  CU  .  CU ? ? ? 1_555 H HIS 121 NE2 ? ? I CU  154 I HIS 120 1_555 ? ? ? ? ? ? ? 2.053 ? 
metalc68 metalc ? ? Z  CU  .  CU ? ? ? 1_555 H HIS 64  NE2 ? ? I CU  154 I HIS 63  1_555 ? ? ? ? ? ? ? 2.119 ? 
metalc69 metalc ? ? Z  CU  .  CU ? ? ? 1_555 H HIS 47  ND1 ? ? I CU  154 I HIS 46  1_555 ? ? ? ? ? ? ? 2.034 ? 
metalc70 metalc ? ? Z  CU  .  CU ? ? ? 1_555 H HIS 49  NE2 ? ? I CU  154 I HIS 48  1_555 ? ? ? ? ? ? ? 2.061 ? 
metalc71 metalc ? ? AA ZN  .  ZN ? ? ? 1_555 H HIS 64  ND1 ? ? I ZN  155 I HIS 63  1_555 ? ? ? ? ? ? ? 2.106 ? 
metalc72 metalc ? ? AA ZN  .  ZN ? ? ? 1_555 H HIS 81  ND1 ? ? I ZN  155 I HIS 80  1_555 ? ? ? ? ? ? ? 2.042 ? 
metalc73 metalc ? ? AA ZN  .  ZN ? ? ? 1_555 H HIS 72  ND1 ? ? I ZN  155 I HIS 71  1_555 ? ? ? ? ? ? ? 2.053 ? 
metalc74 metalc ? ? AA ZN  .  ZN ? ? ? 1_555 H ASP 84  OD1 ? ? I ZN  155 I ASP 83  1_555 ? ? ? ? ? ? ? 1.947 ? 
metalc75 metalc ? ? EA CU  .  CU ? ? ? 1_555 J HIS 47  ND1 ? ? J CU  154 J HIS 46  1_555 ? ? ? ? ? ? ? 2.036 ? 
metalc76 metalc ? ? EA CU  .  CU ? ? ? 1_555 J HIS 64  NE2 ? ? J CU  154 J HIS 63  1_555 ? ? ? ? ? ? ? 2.087 ? 
metalc77 metalc ? ? EA CU  .  CU ? ? ? 1_555 J HIS 121 NE2 ? ? J CU  154 J HIS 120 1_555 ? ? ? ? ? ? ? 2.072 ? 
metalc78 metalc ? ? EA CU  .  CU ? ? ? 1_555 J HIS 49  NE2 ? ? J CU  154 J HIS 48  1_555 ? ? ? ? ? ? ? 2.071 ? 
metalc79 metalc ? ? FA ZN  .  ZN ? ? ? 1_555 J ASP 84  OD1 ? ? J ZN  155 J ASP 83  1_555 ? ? ? ? ? ? ? 1.934 ? 
metalc80 metalc ? ? FA ZN  .  ZN ? ? ? 1_555 J HIS 81  ND1 ? ? J ZN  155 J HIS 80  1_555 ? ? ? ? ? ? ? 2.061 ? 
metalc81 metalc ? ? FA ZN  .  ZN ? ? ? 1_555 J HIS 72  ND1 ? ? J ZN  155 J HIS 71  1_555 ? ? ? ? ? ? ? 2.068 ? 
metalc82 metalc ? ? FA ZN  .  ZN ? ? ? 1_555 J HIS 64  ND1 ? ? J ZN  155 J HIS 63  1_555 ? ? ? ? ? ? ? 2.078 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
metalc ? ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
SA ? 9 ? 
SF ? 9 ? 
SB ? 9 ? 
SG ? 9 ? 
SC ? 9 ? 
SH ? 9 ? 
SD ? 9 ? 
SI ? 9 ? 
SE ? 9 ? 
SJ ? 9 ? 
# 
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 
SA 1 2 ? anti-parallel 
SA 2 3 ? parallel      
SA 3 4 ? anti-parallel 
SA 4 5 ? parallel      
SA 5 6 ? anti-parallel 
SA 6 7 ? parallel      
SA 7 8 ? anti-parallel 
SA 8 9 ? anti-parallel 
SF 1 2 ? anti-parallel 
SF 2 3 ? parallel      
SF 3 4 ? anti-parallel 
SF 4 5 ? parallel      
SF 5 6 ? anti-parallel 
SF 6 7 ? parallel      
SF 7 8 ? anti-parallel 
SF 8 9 ? anti-parallel 
SB 1 2 ? anti-parallel 
SB 2 3 ? parallel      
SB 3 4 ? anti-parallel 
SB 4 5 ? parallel      
SB 5 6 ? anti-parallel 
SB 6 7 ? parallel      
SB 7 8 ? anti-parallel 
SB 8 9 ? anti-parallel 
SG 1 2 ? anti-parallel 
SG 2 3 ? parallel      
SG 3 4 ? anti-parallel 
SG 4 5 ? parallel      
SG 5 6 ? anti-parallel 
SG 6 7 ? parallel      
SG 7 8 ? anti-parallel 
SG 8 9 ? anti-parallel 
SC 1 2 ? anti-parallel 
SC 2 3 ? parallel      
SC 3 4 ? anti-parallel 
SC 4 5 ? parallel      
SC 5 6 ? anti-parallel 
SC 6 7 ? parallel      
SC 7 8 ? anti-parallel 
SC 8 9 ? anti-parallel 
SH 1 2 ? anti-parallel 
SH 2 3 ? parallel      
SH 3 4 ? anti-parallel 
SH 4 5 ? parallel      
SH 5 6 ? anti-parallel 
SH 6 7 ? parallel      
SH 7 8 ? anti-parallel 
SH 8 9 ? anti-parallel 
SD 1 2 ? anti-parallel 
SD 2 3 ? parallel      
SD 3 4 ? anti-parallel 
SD 4 5 ? parallel      
SD 5 6 ? anti-parallel 
SD 6 7 ? parallel      
SD 7 8 ? anti-parallel 
SD 8 9 ? anti-parallel 
SI 1 2 ? anti-parallel 
SI 2 3 ? parallel      
SI 3 4 ? anti-parallel 
SI 4 5 ? parallel      
SI 5 6 ? anti-parallel 
SI 6 7 ? parallel      
SI 7 8 ? anti-parallel 
SI 8 9 ? anti-parallel 
SE 1 2 ? anti-parallel 
SE 2 3 ? parallel      
SE 3 4 ? anti-parallel 
SE 4 5 ? parallel      
SE 5 6 ? anti-parallel 
SE 6 7 ? parallel      
SE 7 8 ? anti-parallel 
SE 8 9 ? anti-parallel 
SJ 1 2 ? anti-parallel 
SJ 2 3 ? parallel      
SJ 3 4 ? anti-parallel 
SJ 4 5 ? parallel      
SJ 5 6 ? anti-parallel 
SJ 6 7 ? parallel      
SJ 7 8 ? anti-parallel 
SJ 8 9 ? 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 
SA 1 ALA A 5   ? LYS A 10  ? ALA A 4   LYS A 9   
SA 2 GLN A 16  ? GLU A 22  ? GLN A 15  GLU A 21  
SA 3 VAL A 30  ? LYS A 31  ? VAL A 29  LYS A 30  
SA 4 VAL A 95  ? ASP A 102 ? VAL A 94  ASP A 101 
SA 5 GLY A 86  ? ALA A 90  ? GLY A 85  ALA A 89  
SA 6 GLY A 42  ? HIS A 49  ? GLY A 41  HIS A 48  
SA 7 ARG A 116 ? HIS A 121 ? ARG A 115 HIS A 120 
SA 8 CYS A 147 ? GLY A 151 ? CYS A 146 GLY A 150 
SA 9 ALA A 5   ? LYS A 10  ? ALA A 4   LYS A 9   
SF 1 ALA B 5   ? LYS B 10  ? ALA F 4   LYS F 9   
SF 2 GLN B 16  ? GLU B 22  ? GLN F 15  GLU F 21  
SF 3 VAL B 30  ? LYS B 31  ? VAL F 29  LYS F 30  
SF 4 VAL B 95  ? ASP B 102 ? VAL F 94  ASP F 101 
SF 5 GLY B 86  ? ALA B 90  ? GLY F 85  ALA F 89  
SF 6 GLY B 42  ? HIS B 49  ? GLY F 41  HIS F 48  
SF 7 ARG B 116 ? HIS B 121 ? ARG F 115 HIS F 120 
SF 8 CYS B 147 ? GLY B 151 ? CYS F 146 GLY F 150 
SF 9 ALA B 5   ? LYS B 10  ? ALA F 4   LYS F 9   
SB 1 ALA C 5   ? LYS C 10  ? ALA B 4   LYS B 9   
SB 2 GLN C 16  ? GLU C 22  ? GLN B 15  GLU B 21  
SB 3 VAL C 30  ? LYS C 31  ? VAL B 29  LYS B 30  
SB 4 VAL C 95  ? ASP C 102 ? VAL B 94  ASP B 101 
SB 5 GLY C 86  ? ALA C 90  ? GLY B 85  ALA B 89  
SB 6 GLY C 42  ? HIS C 49  ? GLY B 41  HIS B 48  
SB 7 ARG C 116 ? HIS C 121 ? ARG B 115 HIS B 120 
SB 8 CYS C 147 ? GLY C 151 ? CYS B 146 GLY B 150 
SB 9 ALA C 5   ? LYS C 10  ? ALA B 4   LYS B 9   
SG 1 ALA D 5   ? LYS D 10  ? ALA G 4   LYS G 9   
SG 2 GLN D 16  ? GLU D 22  ? GLN G 15  GLU G 21  
SG 3 VAL D 30  ? LYS D 31  ? VAL G 29  LYS G 30  
SG 4 VAL D 95  ? ASP D 102 ? VAL G 94  ASP G 101 
SG 5 GLY D 86  ? ALA D 90  ? GLY G 85  ALA G 89  
SG 6 GLY D 42  ? HIS D 49  ? GLY G 41  HIS G 48  
SG 7 ARG D 116 ? HIS D 121 ? ARG G 115 HIS G 120 
SG 8 CYS D 147 ? GLY D 151 ? CYS G 146 GLY G 150 
SG 9 ALA D 5   ? LYS D 10  ? ALA G 4   LYS G 9   
SC 1 ALA E 5   ? LYS E 10  ? ALA C 4   LYS C 9   
SC 2 GLN E 16  ? GLU E 22  ? GLN C 15  GLU C 21  
SC 3 VAL E 30  ? LYS E 31  ? VAL C 29  LYS C 30  
SC 4 VAL E 95  ? ASP E 102 ? VAL C 94  ASP C 101 
SC 5 GLY E 86  ? ALA E 90  ? GLY C 85  ALA C 89  
SC 6 GLY E 42  ? HIS E 49  ? GLY C 41  HIS C 48  
SC 7 ARG E 116 ? HIS E 121 ? ARG C 115 HIS C 120 
SC 8 CYS E 147 ? GLY E 151 ? CYS C 146 GLY C 150 
SC 9 ALA E 5   ? LYS E 10  ? ALA C 4   LYS C 9   
SH 1 ALA F 5   ? LYS F 10  ? ALA H 4   LYS H 9   
SH 2 GLN F 16  ? GLU F 22  ? GLN H 15  GLU H 21  
SH 3 VAL F 30  ? LYS F 31  ? VAL H 29  LYS H 30  
SH 4 VAL F 95  ? ASP F 102 ? VAL H 94  ASP H 101 
SH 5 GLY F 86  ? ALA F 90  ? GLY H 85  ALA H 89  
SH 6 GLY F 42  ? HIS F 49  ? GLY H 41  HIS H 48  
SH 7 ARG F 116 ? HIS F 121 ? ARG H 115 HIS H 120 
SH 8 CYS F 147 ? GLY F 151 ? CYS H 146 GLY H 150 
SH 9 ALA F 5   ? LYS F 10  ? ALA H 4   LYS H 9   
SD 1 ALA G 5   ? LYS G 10  ? ALA D 4   LYS D 9   
SD 2 GLN G 16  ? GLU G 22  ? GLN D 15  GLU D 21  
SD 3 VAL G 30  ? LYS G 31  ? VAL D 29  LYS D 30  
SD 4 VAL G 95  ? ASP G 102 ? VAL D 94  ASP D 101 
SD 5 GLY G 86  ? ALA G 90  ? GLY D 85  ALA D 89  
SD 6 GLY G 42  ? HIS G 49  ? GLY D 41  HIS D 48  
SD 7 ARG G 116 ? HIS G 121 ? ARG D 115 HIS D 120 
SD 8 CYS G 147 ? GLY G 151 ? CYS D 146 GLY D 150 
SD 9 ALA G 5   ? LYS G 10  ? ALA D 4   LYS D 9   
SI 1 ALA H 5   ? LYS H 10  ? ALA I 4   LYS I 9   
SI 2 GLN H 16  ? GLU H 22  ? GLN I 15  GLU I 21  
SI 3 VAL H 30  ? LYS H 31  ? VAL I 29  LYS I 30  
SI 4 VAL H 95  ? ASP H 102 ? VAL I 94  ASP I 101 
SI 5 GLY H 86  ? ALA H 90  ? GLY I 85  ALA I 89  
SI 6 GLY H 42  ? HIS H 49  ? GLY I 41  HIS I 48  
SI 7 ARG H 116 ? HIS H 121 ? ARG I 115 HIS I 120 
SI 8 CYS H 147 ? GLY H 151 ? CYS I 146 GLY I 150 
SI 9 ALA H 5   ? LYS H 10  ? ALA I 4   LYS I 9   
SE 1 ALA I 5   ? LYS I 10  ? ALA E 4   LYS E 9   
SE 2 GLN I 16  ? GLU I 22  ? GLN E 15  GLU E 21  
SE 3 VAL I 30  ? LYS I 31  ? VAL E 29  LYS E 30  
SE 4 VAL I 95  ? ASP I 102 ? VAL E 94  ASP E 101 
SE 5 GLY I 86  ? ALA I 90  ? GLY E 85  ALA E 89  
SE 6 GLY I 42  ? HIS I 49  ? GLY E 41  HIS E 48  
SE 7 ARG I 116 ? HIS I 121 ? ARG E 115 HIS E 120 
SE 8 CYS I 147 ? GLY I 151 ? CYS E 146 GLY E 150 
SE 9 ALA I 5   ? LYS I 10  ? ALA E 4   LYS E 9   
SJ 1 ALA J 5   ? LYS J 10  ? ALA J 4   LYS J 9   
SJ 2 GLN J 16  ? GLU J 22  ? GLN J 15  GLU J 21  
SJ 3 VAL J 30  ? LYS J 31  ? VAL J 29  LYS J 30  
SJ 4 VAL J 95  ? ASP J 102 ? VAL J 94  ASP J 101 
SJ 5 GLY J 86  ? ALA J 90  ? GLY J 85  ALA J 89  
SJ 6 GLY J 42  ? HIS J 49  ? GLY J 41  HIS J 48  
SJ 7 ARG J 116 ? HIS J 121 ? ARG J 115 HIS J 120 
SJ 8 CYS J 147 ? GLY J 151 ? CYS J 146 GLY J 150 
SJ 9 ALA J 5   ? LYS J 10  ? ALA J 4   LYS J 9   
# 
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 
SA 1 2 O ALA A 5   ? O ALA A 4   N PHE A 21  ? N PHE A 20  
SA 2 3 O GLU A 22  ? O GLU A 21  N LYS A 31  ? N LYS A 30  
SA 3 4 O VAL A 32  ? O VAL A 31  N ILE A 100 ? N ILE A 99  
SA 5 6 O VAL A 88  ? O VAL A 87  N HIS A 44  ? N HIS A 43  
SA 6 7 O HIS A 47  ? O HIS A 46  N VAL A 119 ? N VAL A 118 
SA 7 8 O LEU A 118 ? O LEU A 117 N GLY A 148 ? N GLY A 147 
SA 8 9 O VAL A 149 ? O VAL A 148 N VAL A 8   ? N VAL A 7   
SF 1 2 O ALA B 5   ? O ALA F 4   N PHE B 21  ? N PHE F 20  
SF 2 3 O GLU B 22  ? O GLU F 21  N LYS B 31  ? N LYS F 30  
SF 3 4 O VAL B 32  ? O VAL F 31  N ILE B 100 ? N ILE F 99  
SF 5 6 O VAL B 88  ? O VAL F 87  N HIS B 44  ? N HIS F 43  
SF 6 7 O HIS B 47  ? O HIS F 46  N VAL B 119 ? N VAL F 118 
SF 7 8 O LEU B 118 ? O LEU F 117 N GLY B 148 ? N GLY F 147 
SF 8 9 O VAL B 149 ? O VAL F 148 N VAL B 8   ? N VAL F 7   
SB 1 2 O ALA C 5   ? O ALA B 4   N PHE C 21  ? N PHE B 20  
SB 2 3 O GLU C 22  ? O GLU B 21  N LYS C 31  ? N LYS B 30  
SB 3 4 O VAL C 32  ? O VAL B 31  N ILE C 100 ? N ILE B 99  
SB 5 6 O VAL C 88  ? O VAL B 87  N HIS C 44  ? N HIS B 43  
SB 6 7 O HIS C 47  ? O HIS B 46  N VAL C 119 ? N VAL B 118 
SB 7 8 O LEU C 118 ? O LEU B 117 N GLY C 148 ? N GLY B 147 
SB 8 9 O VAL C 149 ? O VAL B 148 N VAL C 8   ? N VAL B 7   
SG 1 2 O ALA D 5   ? O ALA G 4   N PHE D 21  ? N PHE G 20  
SG 2 3 O GLU D 22  ? O GLU G 21  N LYS D 31  ? N LYS G 30  
SG 3 4 O VAL D 32  ? O VAL G 31  N ILE D 100 ? N ILE G 99  
SG 5 6 O VAL D 88  ? O VAL G 87  N HIS D 44  ? N HIS G 43  
SG 6 7 O HIS D 47  ? O HIS G 46  N VAL D 119 ? N VAL G 118 
SG 7 8 O LEU D 118 ? O LEU G 117 N GLY D 148 ? N GLY G 147 
SG 8 9 O VAL D 149 ? O VAL G 148 N VAL D 8   ? N VAL G 7   
SC 1 2 O ALA E 5   ? O ALA C 4   N PHE E 21  ? N PHE C 20  
SC 2 3 O GLU E 22  ? O GLU C 21  N LYS E 31  ? N LYS C 30  
SC 3 4 O VAL E 32  ? O VAL C 31  N ILE E 100 ? N ILE C 99  
SC 5 6 O VAL E 88  ? O VAL C 87  N HIS E 44  ? N HIS C 43  
SC 6 7 O HIS E 47  ? O HIS C 46  N VAL E 119 ? N VAL C 118 
SC 7 8 O LEU E 118 ? O LEU C 117 N GLY E 148 ? N GLY C 147 
SC 8 9 O VAL E 149 ? O VAL C 148 N VAL E 8   ? N VAL C 7   
SH 1 2 O ALA F 5   ? O ALA H 4   N PHE F 21  ? N PHE H 20  
SH 2 3 O GLU F 22  ? O GLU H 21  N LYS F 31  ? N LYS H 30  
SH 3 4 O VAL F 32  ? O VAL H 31  N ILE F 100 ? N ILE H 99  
SH 5 6 O VAL F 88  ? O VAL H 87  N HIS F 44  ? N HIS H 43  
SH 6 7 O HIS F 47  ? O HIS H 46  N VAL F 119 ? N VAL H 118 
SH 7 8 O LEU F 118 ? O LEU H 117 N GLY F 148 ? N GLY H 147 
SH 8 9 O VAL F 149 ? O VAL H 148 N VAL F 8   ? N VAL H 7   
SD 1 2 O ALA G 5   ? O ALA D 4   N PHE G 21  ? N PHE D 20  
SD 2 3 O GLU G 22  ? O GLU D 21  N LYS G 31  ? N LYS D 30  
SD 3 4 O VAL G 32  ? O VAL D 31  N ILE G 100 ? N ILE D 99  
SD 5 6 O VAL G 88  ? O VAL D 87  N HIS G 44  ? N HIS D 43  
SD 6 7 O HIS G 47  ? O HIS D 46  N VAL G 119 ? N VAL D 118 
SD 7 8 O LEU G 118 ? O LEU D 117 N GLY G 148 ? N GLY D 147 
SD 8 9 O VAL G 149 ? O VAL D 148 N VAL G 8   ? N VAL D 7   
SI 1 2 O ALA H 5   ? O ALA I 4   N PHE H 21  ? N PHE I 20  
SI 2 3 O GLU H 22  ? O GLU I 21  N LYS H 31  ? N LYS I 30  
SI 3 4 O VAL H 32  ? O VAL I 31  N ILE H 100 ? N ILE I 99  
SI 5 6 O VAL H 88  ? O VAL I 87  N HIS H 44  ? N HIS I 43  
SI 6 7 O HIS H 47  ? O HIS I 46  N VAL H 119 ? N VAL I 118 
SI 7 8 O LEU H 118 ? O LEU I 117 N GLY H 148 ? N GLY I 147 
SI 8 9 O VAL H 149 ? O VAL I 148 N VAL H 8   ? N VAL I 7   
SE 1 2 O ALA I 5   ? O ALA E 4   N PHE I 21  ? N PHE E 20  
SE 2 3 O GLU I 22  ? O GLU E 21  N LYS I 31  ? N LYS E 30  
SE 3 4 O VAL I 32  ? O VAL E 31  N ILE I 100 ? N ILE E 99  
SE 5 6 O VAL I 88  ? O VAL E 87  N HIS I 44  ? N HIS E 43  
SE 6 7 O HIS I 47  ? O HIS E 46  N VAL I 119 ? N VAL E 118 
SE 7 8 O LEU I 118 ? O LEU E 117 N GLY I 148 ? N GLY E 147 
SE 8 9 O VAL I 149 ? O VAL E 148 N VAL I 8   ? N VAL E 7   
SJ 1 2 O ALA J 5   ? O ALA J 4   N PHE J 21  ? N PHE J 20  
SJ 2 3 O GLU J 22  ? O GLU J 21  N LYS J 31  ? N LYS J 30  
SJ 3 4 O VAL J 32  ? O VAL J 31  N ILE J 100 ? N ILE J 99  
SJ 5 6 O VAL J 88  ? O VAL J 87  N HIS J 44  ? N HIS J 43  
SJ 6 7 O HIS J 47  ? O HIS J 46  N VAL J 119 ? N VAL J 118 
SJ 7 8 O LEU J 118 ? O LEU J 117 N GLY J 148 ? N GLY J 147 
SJ 8 9 O VAL J 149 ? O VAL J 148 N VAL J 8   ? N VAL J 7   
# 
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 
CUA Unknown  ? ? ? ? 4 ?                                    
ZNA Unknown  ? ? ? ? 4 ?                                    
CUF Unknown  ? ? ? ? 4 ?                                    
ZNF Unknown  ? ? ? ? 4 ?                                    
CUB Unknown  ? ? ? ? 4 ?                                    
ZNB Unknown  ? ? ? ? 4 ?                                    
CUG Unknown  ? ? ? ? 4 ?                                    
ZNG Unknown  ? ? ? ? 4 ?                                    
CUC Unknown  ? ? ? ? 4 ?                                    
ZNC Unknown  ? ? ? ? 4 ?                                    
CUH Unknown  ? ? ? ? 4 ?                                    
ZNH Unknown  ? ? ? ? 4 ?                                    
CUD Unknown  ? ? ? ? 4 ?                                    
ZND Unknown  ? ? ? ? 4 ?                                    
CUI Unknown  ? ? ? ? 4 ?                                    
ZNI Unknown  ? ? ? ? 4 ?                                    
CUE Unknown  ? ? ? ? 4 ?                                    
ZNE Unknown  ? ? ? ? 4 ?                                    
CUJ Unknown  ? ? ? ? 4 ?                                    
ZNJ Unknown  ? ? ? ? 4 ?                                    
AC1 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU A 154'  
AC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN A 155'  
AC3 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU F 154'  
AC4 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN F 155'  
AC5 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU B 154'  
AC6 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN B 155'  
AC7 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU G 154'  
AC8 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN G 155'  
AC9 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU C 154'  
BC1 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN C 155'  
BC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU H 154'  
BC3 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN H 155'  
BC4 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU D 154'  
BC5 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN D 155'  
BC6 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU I 154'  
BC7 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN I 155'  
BC8 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU E 154'  
BC9 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE ZN E 155'  
CC1 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU J 154'  
CC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN J 155'  
CC3 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE SO4 F 356' 
CC4 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE SO4 I 357' 
# 
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   CUA 4 HIS A  47  ? HIS A 46  . ? 1_555 ? 
2   CUA 4 HIS A  49  ? HIS A 48  . ? 1_555 ? 
3   CUA 4 HIS A  64  ? HIS A 63  . ? 1_555 ? 
4   CUA 4 HIS A  121 ? HIS A 120 . ? 1_555 ? 
5   ZNA 4 HIS A  64  ? HIS A 63  . ? 1_555 ? 
6   ZNA 4 HIS A  72  ? HIS A 71  . ? 1_555 ? 
7   ZNA 4 HIS A  81  ? HIS A 80  . ? 1_555 ? 
8   ZNA 4 ASP A  84  ? ASP A 83  . ? 1_555 ? 
9   CUF 4 HIS B  47  ? HIS F 46  . ? 1_555 ? 
10  CUF 4 HIS B  49  ? HIS F 48  . ? 1_555 ? 
11  CUF 4 HIS B  64  ? HIS F 63  . ? 1_555 ? 
12  CUF 4 HIS B  121 ? HIS F 120 . ? 1_555 ? 
13  ZNF 4 HIS B  64  ? HIS F 63  . ? 1_555 ? 
14  ZNF 4 HIS B  72  ? HIS F 71  . ? 1_555 ? 
15  ZNF 4 HIS B  81  ? HIS F 80  . ? 1_555 ? 
16  ZNF 4 ASP B  84  ? ASP F 83  . ? 1_555 ? 
17  CUB 4 HIS C  47  ? HIS B 46  . ? 1_555 ? 
18  CUB 4 HIS C  49  ? HIS B 48  . ? 1_555 ? 
19  CUB 4 HIS C  64  ? HIS B 63  . ? 1_555 ? 
20  CUB 4 HIS C  121 ? HIS B 120 . ? 1_555 ? 
21  ZNB 4 HIS C  64  ? HIS B 63  . ? 1_555 ? 
22  ZNB 4 HIS C  72  ? HIS B 71  . ? 1_555 ? 
23  ZNB 4 HIS C  81  ? HIS B 80  . ? 1_555 ? 
24  ZNB 4 ASP C  84  ? ASP B 83  . ? 1_555 ? 
25  CUG 4 HIS D  47  ? HIS G 46  . ? 1_555 ? 
26  CUG 4 HIS D  49  ? HIS G 48  . ? 1_555 ? 
27  CUG 4 HIS D  64  ? HIS G 63  . ? 1_555 ? 
28  CUG 4 HIS D  121 ? HIS G 120 . ? 1_555 ? 
29  ZNG 4 HIS D  64  ? HIS G 63  . ? 1_555 ? 
30  ZNG 4 HIS D  72  ? HIS G 71  . ? 1_555 ? 
31  ZNG 4 HIS D  81  ? HIS G 80  . ? 1_555 ? 
32  ZNG 4 ASP D  84  ? ASP G 83  . ? 1_555 ? 
33  CUC 4 HIS E  47  ? HIS C 46  . ? 1_555 ? 
34  CUC 4 HIS E  49  ? HIS C 48  . ? 1_555 ? 
35  CUC 4 HIS E  64  ? HIS C 63  . ? 1_555 ? 
36  CUC 4 HIS E  121 ? HIS C 120 . ? 1_555 ? 
37  ZNC 4 HIS E  64  ? HIS C 63  . ? 1_555 ? 
38  ZNC 4 HIS E  72  ? HIS C 71  . ? 1_555 ? 
39  ZNC 4 HIS E  81  ? HIS C 80  . ? 1_555 ? 
40  ZNC 4 ASP E  84  ? ASP C 83  . ? 1_555 ? 
41  CUH 4 HIS F  47  ? HIS H 46  . ? 1_555 ? 
42  CUH 4 HIS F  49  ? HIS H 48  . ? 1_555 ? 
43  CUH 4 HIS F  64  ? HIS H 63  . ? 1_555 ? 
44  CUH 4 HIS F  121 ? HIS H 120 . ? 1_555 ? 
45  ZNH 4 HIS F  64  ? HIS H 63  . ? 1_555 ? 
46  ZNH 4 HIS F  72  ? HIS H 71  . ? 1_555 ? 
47  ZNH 4 HIS F  81  ? HIS H 80  . ? 1_555 ? 
48  ZNH 4 ASP F  84  ? ASP H 83  . ? 1_555 ? 
49  CUD 4 HIS G  47  ? HIS D 46  . ? 1_555 ? 
50  CUD 4 HIS G  49  ? HIS D 48  . ? 1_555 ? 
51  CUD 4 HIS G  64  ? HIS D 63  . ? 1_555 ? 
52  CUD 4 HIS G  121 ? HIS D 120 . ? 1_555 ? 
53  ZND 4 HIS G  64  ? HIS D 63  . ? 1_555 ? 
54  ZND 4 HIS G  72  ? HIS D 71  . ? 1_555 ? 
55  ZND 4 HIS G  81  ? HIS D 80  . ? 1_555 ? 
56  ZND 4 ASP G  84  ? ASP D 83  . ? 1_555 ? 
57  CUI 4 HIS H  47  ? HIS I 46  . ? 1_555 ? 
58  CUI 4 HIS H  49  ? HIS I 48  . ? 1_555 ? 
59  CUI 4 HIS H  64  ? HIS I 63  . ? 1_555 ? 
60  CUI 4 HIS H  121 ? HIS I 120 . ? 1_555 ? 
61  ZNI 4 HIS H  64  ? HIS I 63  . ? 1_555 ? 
62  ZNI 4 HIS H  72  ? HIS I 71  . ? 1_555 ? 
63  ZNI 4 HIS H  81  ? HIS I 80  . ? 1_555 ? 
64  ZNI 4 ASP H  84  ? ASP I 83  . ? 1_555 ? 
65  CUE 4 HIS I  47  ? HIS E 46  . ? 1_555 ? 
66  CUE 4 HIS I  49  ? HIS E 48  . ? 1_555 ? 
67  CUE 4 HIS I  64  ? HIS E 63  . ? 1_555 ? 
68  CUE 4 HIS I  121 ? HIS E 120 . ? 1_555 ? 
69  ZNE 4 HIS I  64  ? HIS E 63  . ? 1_555 ? 
70  ZNE 4 HIS I  72  ? HIS E 71  . ? 1_555 ? 
71  ZNE 4 HIS I  81  ? HIS E 80  . ? 1_555 ? 
72  ZNE 4 ASP I  84  ? ASP E 83  . ? 1_555 ? 
73  CUJ 4 HIS J  47  ? HIS J 46  . ? 1_555 ? 
74  CUJ 4 HIS J  49  ? HIS J 48  . ? 1_555 ? 
75  CUJ 4 HIS J  64  ? HIS J 63  . ? 1_555 ? 
76  CUJ 4 HIS J  121 ? HIS J 120 . ? 1_555 ? 
77  ZNJ 4 HIS J  64  ? HIS J 63  . ? 1_555 ? 
78  ZNJ 4 HIS J  72  ? HIS J 71  . ? 1_555 ? 
79  ZNJ 4 HIS J  81  ? HIS J 80  . ? 1_555 ? 
80  ZNJ 4 ASP J  84  ? ASP J 83  . ? 1_555 ? 
81  AC1 4 HIS A  47  ? HIS A 46  . ? 1_555 ? 
82  AC1 4 HIS A  49  ? HIS A 48  . ? 1_555 ? 
83  AC1 4 HIS A  64  ? HIS A 63  . ? 1_555 ? 
84  AC1 4 HIS A  121 ? HIS A 120 . ? 1_555 ? 
85  AC2 4 HIS A  64  ? HIS A 63  . ? 1_555 ? 
86  AC2 4 HIS A  72  ? HIS A 71  . ? 1_555 ? 
87  AC2 4 HIS A  81  ? HIS A 80  . ? 1_555 ? 
88  AC2 4 ASP A  84  ? ASP A 83  . ? 1_555 ? 
89  AC3 4 HIS B  47  ? HIS F 46  . ? 1_555 ? 
90  AC3 4 HIS B  49  ? HIS F 48  . ? 1_555 ? 
91  AC3 4 HIS B  64  ? HIS F 63  . ? 1_555 ? 
92  AC3 4 HIS B  121 ? HIS F 120 . ? 1_555 ? 
93  AC4 4 HIS B  64  ? HIS F 63  . ? 1_555 ? 
94  AC4 4 HIS B  72  ? HIS F 71  . ? 1_555 ? 
95  AC4 4 HIS B  81  ? HIS F 80  . ? 1_555 ? 
96  AC4 4 ASP B  84  ? ASP F 83  . ? 1_555 ? 
97  AC5 4 HIS C  47  ? HIS B 46  . ? 1_555 ? 
98  AC5 4 HIS C  49  ? HIS B 48  . ? 1_555 ? 
99  AC5 4 HIS C  64  ? HIS B 63  . ? 1_555 ? 
100 AC5 4 HIS C  121 ? HIS B 120 . ? 1_555 ? 
101 AC6 4 HIS C  64  ? HIS B 63  . ? 1_555 ? 
102 AC6 4 HIS C  72  ? HIS B 71  . ? 1_555 ? 
103 AC6 4 HIS C  81  ? HIS B 80  . ? 1_555 ? 
104 AC6 4 ASP C  84  ? ASP B 83  . ? 1_555 ? 
105 AC7 4 HIS D  47  ? HIS G 46  . ? 1_555 ? 
106 AC7 4 HIS D  49  ? HIS G 48  . ? 1_555 ? 
107 AC7 4 HIS D  64  ? HIS G 63  . ? 1_555 ? 
108 AC7 4 HIS D  121 ? HIS G 120 . ? 1_555 ? 
109 AC8 4 HIS D  64  ? HIS G 63  . ? 1_555 ? 
110 AC8 4 HIS D  72  ? HIS G 71  . ? 1_555 ? 
111 AC8 4 HIS D  81  ? HIS G 80  . ? 1_555 ? 
112 AC8 4 ASP D  84  ? ASP G 83  . ? 1_555 ? 
113 AC9 4 HIS E  47  ? HIS C 46  . ? 1_555 ? 
114 AC9 4 HIS E  49  ? HIS C 48  . ? 1_555 ? 
115 AC9 4 HIS E  64  ? HIS C 63  . ? 1_555 ? 
116 AC9 4 HIS E  121 ? HIS C 120 . ? 1_555 ? 
117 BC1 4 HIS E  64  ? HIS C 63  . ? 1_555 ? 
118 BC1 4 HIS E  72  ? HIS C 71  . ? 1_555 ? 
119 BC1 4 HIS E  81  ? HIS C 80  . ? 1_555 ? 
120 BC1 4 ASP E  84  ? ASP C 83  . ? 1_555 ? 
121 BC2 4 HIS F  47  ? HIS H 46  . ? 1_555 ? 
122 BC2 4 HIS F  49  ? HIS H 48  . ? 1_555 ? 
123 BC2 4 HIS F  64  ? HIS H 63  . ? 1_555 ? 
124 BC2 4 HIS F  121 ? HIS H 120 . ? 1_555 ? 
125 BC3 4 HIS F  64  ? HIS H 63  . ? 1_555 ? 
126 BC3 4 HIS F  72  ? HIS H 71  . ? 1_555 ? 
127 BC3 4 HIS F  81  ? HIS H 80  . ? 1_555 ? 
128 BC3 4 ASP F  84  ? ASP H 83  . ? 1_555 ? 
129 BC4 4 HIS G  47  ? HIS D 46  . ? 1_555 ? 
130 BC4 4 HIS G  49  ? HIS D 48  . ? 1_555 ? 
131 BC4 4 HIS G  64  ? HIS D 63  . ? 1_555 ? 
132 BC4 4 HIS G  121 ? HIS D 120 . ? 1_555 ? 
133 BC5 4 HIS G  64  ? HIS D 63  . ? 1_555 ? 
134 BC5 4 HIS G  72  ? HIS D 71  . ? 1_555 ? 
135 BC5 4 HIS G  81  ? HIS D 80  . ? 1_555 ? 
136 BC5 4 ASP G  84  ? ASP D 83  . ? 1_555 ? 
137 BC6 4 HIS H  47  ? HIS I 46  . ? 1_555 ? 
138 BC6 4 HIS H  49  ? HIS I 48  . ? 1_555 ? 
139 BC6 4 HIS H  64  ? HIS I 63  . ? 1_555 ? 
140 BC6 4 HIS H  121 ? HIS I 120 . ? 1_555 ? 
141 BC7 4 HIS H  64  ? HIS I 63  . ? 1_555 ? 
142 BC7 4 HIS H  72  ? HIS I 71  . ? 1_555 ? 
143 BC7 4 HIS H  81  ? HIS I 80  . ? 1_555 ? 
144 BC7 4 ASP H  84  ? ASP I 83  . ? 1_555 ? 
145 BC8 4 HIS I  47  ? HIS E 46  . ? 1_555 ? 
146 BC8 4 HIS I  49  ? HIS E 48  . ? 1_555 ? 
147 BC8 4 HIS I  64  ? HIS E 63  . ? 1_555 ? 
148 BC8 4 HIS I  121 ? HIS E 120 . ? 1_555 ? 
149 BC9 5 HIS I  64  ? HIS E 63  . ? 1_555 ? 
150 BC9 5 HIS I  72  ? HIS E 71  . ? 1_555 ? 
151 BC9 5 HIS I  81  ? HIS E 80  . ? 1_555 ? 
152 BC9 5 ASP I  84  ? ASP E 83  . ? 1_555 ? 
153 BC9 5 LYS I  137 ? LYS E 136 . ? 1_555 ? 
154 CC1 4 HIS J  47  ? HIS J 46  . ? 1_555 ? 
155 CC1 4 HIS J  49  ? HIS J 48  . ? 1_555 ? 
156 CC1 4 HIS J  64  ? HIS J 63  . ? 1_555 ? 
157 CC1 4 HIS J  121 ? HIS J 120 . ? 1_555 ? 
158 CC2 4 HIS J  64  ? HIS J 63  . ? 1_555 ? 
159 CC2 4 HIS J  72  ? HIS J 71  . ? 1_555 ? 
160 CC2 4 HIS J  81  ? HIS J 80  . ? 1_555 ? 
161 CC2 4 ASP J  84  ? ASP J 83  . ? 1_555 ? 
162 CC3 3 LYS B  76  ? LYS F 75  . ? 1_555 ? 
163 CC3 3 LYS B  129 ? LYS F 128 . ? 1_555 ? 
164 CC3 3 LYS D  129 ? LYS G 128 . ? 1_555 ? 
165 CC4 5 LYS E  129 ? LYS C 128 . ? 5_555 ? 
166 CC4 5 LYS H  76  ? LYS I 75  . ? 1_555 ? 
167 CC4 5 LYS H  129 ? LYS I 128 . ? 1_555 ? 
168 CC4 5 HOH NA .   ? HOH I 358 . ? 1_555 ? 
169 CC4 5 LYS J  129 ? LYS J 128 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          1SOS 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    1SOS 
_atom_sites.fract_transf_matrix[1][1]   0.004873 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.005988 
_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]   0.006873 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
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 
HETATM 1     C  C   . ACE A  1 1   ? 53.275  28.140  5.578   1.00 34.09 ? 0   ACE A C   1 
HETATM 2     O  O   . ACE A  1 1   ? 52.151  27.619  5.540   1.00 34.04 ? 0   ACE A O   1 
HETATM 3     C  CH3 . ACE A  1 1   ? 54.133  28.277  4.327   1.00 33.82 ? 0   ACE A CH3 1 
ATOM   4     N  N   . ALA A  1 2   ? 53.857  28.615  6.693   1.00 33.66 ? 1   ALA A N   1 
ATOM   5     C  CA  . ALA A  1 2   ? 53.246  28.543  8.017   1.00 29.25 ? 1   ALA A CA  1 
ATOM   6     C  C   . ALA A  1 2   ? 52.077  29.522  8.050   1.00 26.48 ? 1   ALA A C   1 
ATOM   7     O  O   . ALA A  1 2   ? 52.127  30.632  7.518   1.00 27.08 ? 1   ALA A O   1 
ATOM   8     C  CB  . ALA A  1 2   ? 54.259  28.940  9.085   1.00 28.15 ? 1   ALA A CB  1 
ATOM   9     N  N   . THR A  1 3   ? 50.986  29.001  8.571   1.00 22.95 ? 2   THR A N   1 
ATOM   10    C  CA  . THR A  1 3   ? 49.774  29.758  8.755   1.00 19.83 ? 2   THR A CA  1 
ATOM   11    C  C   . THR A  1 3   ? 49.853  30.327  10.166  1.00 16.58 ? 2   THR A C   1 
ATOM   12    O  O   . THR A  1 3   ? 49.296  31.396  10.406  1.00 16.95 ? 2   THR A O   1 
ATOM   13    C  CB  . THR A  1 3   ? 48.547  28.825  8.624   1.00 22.76 ? 2   THR A CB  1 
ATOM   14    O  OG1 . THR A  1 3   ? 48.978  27.752  7.786   1.00 23.35 ? 2   THR A OG1 1 
ATOM   15    C  CG2 . THR A  1 3   ? 47.300  29.483  8.036   1.00 24.48 ? 2   THR A CG2 1 
ATOM   16    N  N   . LYS A  1 4   ? 50.562  29.712  11.122  1.00 11.76 ? 3   LYS A N   1 
ATOM   17    C  CA  . LYS A  1 4   ? 50.535  30.175  12.485  1.00 7.46  ? 3   LYS A CA  1 
ATOM   18    C  C   . LYS A  1 4   ? 51.913  30.194  13.109  1.00 4.48  ? 3   LYS A C   1 
ATOM   19    O  O   . LYS A  1 4   ? 52.773  29.449  12.657  1.00 4.59  ? 3   LYS A O   1 
ATOM   20    C  CB  . LYS A  1 4   ? 49.610  29.276  13.264  1.00 8.42  ? 3   LYS A CB  1 
ATOM   21    C  CG  . LYS A  1 4   ? 48.704  30.152  14.132  1.00 14.33 ? 3   LYS A CG  1 
ATOM   22    C  CD  . LYS A  1 4   ? 47.551  29.397  14.802  1.00 17.78 ? 3   LYS A CD  1 
ATOM   23    C  CE  . LYS A  1 4   ? 46.722  28.721  13.707  1.00 18.30 ? 3   LYS A CE  1 
ATOM   24    N  NZ  . LYS A  1 4   ? 45.285  28.829  13.944  1.00 23.85 ? 3   LYS A NZ  1 
ATOM   25    N  N   . ALA A  1 5   ? 52.168  31.030  14.108  1.00 3.41  ? 4   ALA A N   1 
ATOM   26    C  CA  . ALA A  1 5   ? 53.433  31.083  14.782  1.00 2.00  ? 4   ALA A CA  1 
ATOM   27    C  C   . ALA A  1 5   ? 53.219  31.616  16.191  1.00 2.00  ? 4   ALA A C   1 
ATOM   28    O  O   . ALA A  1 5   ? 52.135  32.139  16.472  1.00 2.00  ? 4   ALA A O   1 
ATOM   29    C  CB  . ALA A  1 5   ? 54.331  31.998  14.023  1.00 3.71  ? 4   ALA A CB  1 
ATOM   30    N  N   . VAL A  1 6   ? 54.147  31.476  17.126  1.00 2.00  ? 5   VAL A N   1 
ATOM   31    C  CA  . VAL A  1 6   ? 54.004  32.019  18.455  1.00 3.06  ? 5   VAL A CA  1 
ATOM   32    C  C   . VAL A  1 6   ? 55.368  32.477  18.987  1.00 4.79  ? 5   VAL A C   1 
ATOM   33    O  O   . VAL A  1 6   ? 56.416  32.022  18.518  1.00 6.96  ? 5   VAL A O   1 
ATOM   34    C  CB  . VAL A  1 6   ? 53.332  30.940  19.398  1.00 4.74  ? 5   VAL A CB  1 
ATOM   35    C  CG1 . VAL A  1 6   ? 54.190  29.727  19.589  1.00 2.98  ? 5   VAL A CG1 1 
ATOM   36    C  CG2 . VAL A  1 6   ? 53.063  31.568  20.772  1.00 2.00  ? 5   VAL A CG2 1 
ATOM   37    N  N   . ALA A  1 7   ? 55.410  33.441  19.894  1.00 3.77  ? 6   ALA A N   1 
ATOM   38    C  CA  . ALA A  1 7   ? 56.637  33.907  20.479  1.00 2.73  ? 6   ALA A CA  1 
ATOM   39    C  C   . ALA A  1 7   ? 56.279  34.066  21.948  1.00 2.62  ? 6   ALA A C   1 
ATOM   40    O  O   . ALA A  1 7   ? 55.242  34.618  22.284  1.00 2.36  ? 6   ALA A O   1 
ATOM   41    C  CB  . ALA A  1 7   ? 57.041  35.238  19.969  1.00 2.00  ? 6   ALA A CB  1 
ATOM   42    N  N   . VAL A  1 8   ? 57.065  33.439  22.820  1.00 3.17  ? 7   VAL A N   1 
ATOM   43    C  CA  . VAL A  1 8   ? 56.914  33.516  24.238  1.00 2.43  ? 7   VAL A CA  1 
ATOM   44    C  C   . VAL A  1 8   ? 57.991  34.506  24.597  1.00 3.65  ? 7   VAL A C   1 
ATOM   45    O  O   . VAL A  1 8   ? 59.175  34.264  24.372  1.00 3.14  ? 7   VAL A O   1 
ATOM   46    C  CB  . VAL A  1 8   ? 57.155  32.156  24.806  1.00 2.00  ? 7   VAL A CB  1 
ATOM   47    C  CG1 . VAL A  1 8   ? 57.053  32.170  26.325  1.00 2.00  ? 7   VAL A CG1 1 
ATOM   48    C  CG2 . VAL A  1 8   ? 56.107  31.254  24.243  1.00 2.00  ? 7   VAL A CG2 1 
ATOM   49    N  N   . LEU A  1 9   ? 57.533  35.656  25.077  1.00 5.41  ? 8   LEU A N   1 
ATOM   50    C  CA  . LEU A  1 9   ? 58.332  36.833  25.326  1.00 4.73  ? 8   LEU A CA  1 
ATOM   51    C  C   . LEU A  1 9   ? 58.850  36.733  26.765  1.00 7.67  ? 8   LEU A C   1 
ATOM   52    O  O   . LEU A  1 9   ? 58.043  36.634  27.681  1.00 8.83  ? 8   LEU A O   1 
ATOM   53    C  CB  . LEU A  1 9   ? 57.346  37.931  25.037  1.00 2.00  ? 8   LEU A CB  1 
ATOM   54    C  CG  . LEU A  1 9   ? 57.737  39.013  24.006  1.00 4.05  ? 8   LEU A CG  1 
ATOM   55    C  CD1 . LEU A  1 9   ? 57.867  38.374  22.664  1.00 2.69  ? 8   LEU A CD1 1 
ATOM   56    C  CD2 . LEU A  1 9   ? 56.677  40.090  23.881  1.00 2.00  ? 8   LEU A CD2 1 
ATOM   57    N  N   . LYS A  1 10  ? 60.136  36.705  27.101  1.00 10.98 ? 9   LYS A N   1 
ATOM   58    C  CA  . LYS A  1 10  ? 60.626  36.520  28.470  1.00 13.72 ? 9   LYS A CA  1 
ATOM   59    C  C   . LYS A  1 10  ? 61.989  37.181  28.536  1.00 15.69 ? 9   LYS A C   1 
ATOM   60    O  O   . LYS A  1 10  ? 62.724  37.174  27.554  1.00 16.98 ? 9   LYS A O   1 
ATOM   61    C  CB  . LYS A  1 10  ? 60.811  35.051  28.834  1.00 13.39 ? 9   LYS A CB  1 
ATOM   62    C  CG  . LYS A  1 10  ? 59.578  34.438  29.532  1.00 20.88 ? 9   LYS A CG  1 
ATOM   63    C  CD  . LYS A  1 10  ? 59.802  32.943  29.874  1.00 25.11 ? 9   LYS A CD  1 
ATOM   64    C  CE  . LYS A  1 10  ? 58.994  32.458  31.098  1.00 29.44 ? 9   LYS A CE  1 
ATOM   65    N  NZ  . LYS A  1 10  ? 57.543  32.445  30.919  1.00 33.04 ? 9   LYS A NZ  1 
ATOM   66    N  N   . GLY A  1 11  ? 62.369  37.776  29.660  1.00 18.06 ? 10  GLY A N   1 
ATOM   67    C  CA  . GLY A  1 11  ? 63.603  38.536  29.757  1.00 18.15 ? 10  GLY A CA  1 
ATOM   68    C  C   . GLY A  1 11  ? 64.112  38.547  31.197  1.00 19.53 ? 10  GLY A C   1 
ATOM   69    O  O   . GLY A  1 11  ? 63.553  37.906  32.075  1.00 18.31 ? 10  GLY A O   1 
ATOM   70    N  N   . ASP A  1 12  ? 65.115  39.373  31.484  1.00 22.81 ? 11  ASP A N   1 
ATOM   71    C  CA  . ASP A  1 12  ? 65.832  39.389  32.754  1.00 25.61 ? 11  ASP A CA  1 
ATOM   72    C  C   . ASP A  1 12  ? 65.101  39.833  34.007  1.00 25.38 ? 11  ASP A C   1 
ATOM   73    O  O   . ASP A  1 12  ? 65.713  39.776  35.088  1.00 27.76 ? 11  ASP A O   1 
ATOM   74    C  CB  . ASP A  1 12  ? 67.082  40.260  32.607  1.00 31.28 ? 11  ASP A CB  1 
ATOM   75    C  CG  . ASP A  1 12  ? 68.293  39.545  31.981  1.00 37.54 ? 11  ASP A CG  1 
ATOM   76    O  OD1 . ASP A  1 12  ? 68.954  38.787  32.699  1.00 40.27 ? 11  ASP A OD1 1 
ATOM   77    O  OD2 . ASP A  1 12  ? 68.601  39.752  30.795  1.00 40.52 ? 11  ASP A OD2 1 
ATOM   78    N  N   . GLY A  1 13  ? 63.819  40.231  33.850  1.00 24.17 ? 12  GLY A N   1 
ATOM   79    C  CA  . GLY A  1 13  ? 62.961  40.810  34.887  1.00 19.54 ? 12  GLY A CA  1 
ATOM   80    C  C   . GLY A  1 13  ? 61.534  40.254  34.849  1.00 16.49 ? 12  GLY A C   1 
ATOM   81    O  O   . GLY A  1 13  ? 61.326  39.147  34.340  1.00 16.37 ? 12  GLY A O   1 
ATOM   82    N  N   . PRO A  1 14  ? 60.502  40.980  35.325  1.00 14.83 ? 13  PRO A N   1 
ATOM   83    C  CA  . PRO A  1 14  ? 59.101  40.513  35.345  1.00 12.87 ? 13  PRO A CA  1 
ATOM   84    C  C   . PRO A  1 14  ? 58.318  40.401  34.011  1.00 11.52 ? 13  PRO A C   1 
ATOM   85    O  O   . PRO A  1 14  ? 57.320  39.672  33.934  1.00 11.35 ? 13  PRO A O   1 
ATOM   86    C  CB  . PRO A  1 14  ? 58.465  41.481  36.302  1.00 13.87 ? 13  PRO A CB  1 
ATOM   87    C  CG  . PRO A  1 14  ? 59.140  42.805  35.986  1.00 9.79  ? 13  PRO A CG  1 
ATOM   88    C  CD  . PRO A  1 14  ? 60.587  42.365  35.817  1.00 11.70 ? 13  PRO A CD  1 
ATOM   89    N  N   . VAL A  1 15  ? 58.814  41.123  32.975  1.00 9.57  ? 14  VAL A N   1 
ATOM   90    C  CA  . VAL A  1 15  ? 58.140  41.430  31.718  1.00 6.29  ? 14  VAL A CA  1 
ATOM   91    C  C   . VAL A  1 15  ? 58.104  40.189  30.884  1.00 5.71  ? 14  VAL A C   1 
ATOM   92    O  O   . VAL A  1 15  ? 59.156  39.743  30.460  1.00 6.78  ? 14  VAL A O   1 
ATOM   93    C  CB  . VAL A  1 15  ? 58.893  42.550  30.984  1.00 4.46  ? 14  VAL A CB  1 
ATOM   94    C  CG1 . VAL A  1 15  ? 58.205  42.835  29.677  1.00 5.43  ? 14  VAL A CG1 1 
ATOM   95    C  CG2 . VAL A  1 15  ? 58.855  43.839  31.737  1.00 2.00  ? 14  VAL A CG2 1 
ATOM   96    N  N   . GLN A  1 16  ? 56.917  39.660  30.649  1.00 6.97  ? 15  GLN A N   1 
ATOM   97    C  CA  . GLN A  1 16  ? 56.726  38.379  29.978  1.00 8.25  ? 15  GLN A CA  1 
ATOM   98    C  C   . GLN A  1 16  ? 55.383  38.332  29.277  1.00 7.00  ? 15  GLN A C   1 
ATOM   99    O  O   . GLN A  1 16  ? 54.474  39.076  29.649  1.00 9.59  ? 15  GLN A O   1 
ATOM   100   C  CB  . GLN A  1 16  ? 56.744  37.229  30.944  1.00 11.58 ? 15  GLN A CB  1 
ATOM   101   C  CG  . GLN A  1 16  ? 55.637  37.166  31.994  1.00 16.45 ? 15  GLN A CG  1 
ATOM   102   C  CD  . GLN A  1 16  ? 55.708  35.873  32.789  1.00 23.32 ? 15  GLN A CD  1 
ATOM   103   O  OE1 . GLN A  1 16  ? 54.778  35.066  32.864  1.00 28.68 ? 15  GLN A OE1 1 
ATOM   104   N  NE2 . GLN A  1 16  ? 56.836  35.564  33.406  1.00 27.52 ? 15  GLN A NE2 1 
ATOM   105   N  N   . GLY A  1 17  ? 55.193  37.464  28.309  1.00 4.68  ? 16  GLY A N   1 
ATOM   106   C  CA  . GLY A  1 17  ? 53.982  37.473  27.540  1.00 3.78  ? 16  GLY A CA  1 
ATOM   107   C  C   . GLY A  1 17  ? 54.059  36.439  26.444  1.00 3.79  ? 16  GLY A C   1 
ATOM   108   O  O   . GLY A  1 17  ? 55.017  35.676  26.392  1.00 6.36  ? 16  GLY A O   1 
ATOM   109   N  N   . ILE A  1 18  ? 53.050  36.339  25.599  1.00 3.43  ? 17  ILE A N   1 
ATOM   110   C  CA  . ILE A  1 18  ? 52.922  35.336  24.561  1.00 3.40  ? 17  ILE A CA  1 
ATOM   111   C  C   . ILE A  1 18  ? 52.092  36.018  23.495  1.00 3.12  ? 17  ILE A C   1 
ATOM   112   O  O   . ILE A  1 18  ? 50.973  36.471  23.768  1.00 2.43  ? 17  ILE A O   1 
ATOM   113   C  CB  . ILE A  1 18  ? 52.144  34.116  25.028  1.00 3.19  ? 17  ILE A CB  1 
ATOM   114   C  CG1 . ILE A  1 18  ? 52.821  33.457  26.197  1.00 2.00  ? 17  ILE A CG1 1 
ATOM   115   C  CG2 . ILE A  1 18  ? 52.006  33.166  23.832  1.00 2.00  ? 17  ILE A CG2 1 
ATOM   116   C  CD1 . ILE A  1 18  ? 52.028  32.242  26.668  1.00 2.00  ? 17  ILE A CD1 1 
ATOM   117   N  N   . ILE A  1 19  ? 52.692  36.087  22.319  1.00 3.94  ? 18  ILE A N   1 
ATOM   118   C  CA  . ILE A  1 19  ? 52.157  36.775  21.160  1.00 2.44  ? 18  ILE A CA  1 
ATOM   119   C  C   . ILE A  1 19  ? 52.030  35.722  20.096  1.00 2.69  ? 18  ILE A C   1 
ATOM   120   O  O   . ILE A  1 19  ? 53.045  35.068  19.836  1.00 2.00  ? 18  ILE A O   1 
ATOM   121   C  CB  . ILE A  1 19  ? 53.104  37.831  20.642  1.00 2.00  ? 18  ILE A CB  1 
ATOM   122   C  CG1 . ILE A  1 19  ? 53.344  38.879  21.681  1.00 2.00  ? 18  ILE A CG1 1 
ATOM   123   C  CG2 . ILE A  1 19  ? 52.515  38.451  19.385  1.00 4.82  ? 18  ILE A CG2 1 
ATOM   124   C  CD1 . ILE A  1 19  ? 52.080  39.518  22.230  1.00 2.41  ? 18  ILE A CD1 1 
ATOM   125   N  N   . ASN A  1 20  ? 50.834  35.612  19.488  1.00 3.58  ? 19  ASN A N   1 
ATOM   126   C  CA  . ASN A  1 20  ? 50.508  34.726  18.381  1.00 3.40  ? 19  ASN A CA  1 
ATOM   127   C  C   . ASN A  1 20  ? 50.462  35.371  17.026  1.00 2.00  ? 19  ASN A C   1 
ATOM   128   O  O   . ASN A  1 20  ? 50.103  36.514  16.935  1.00 2.00  ? 19  ASN A O   1 
ATOM   129   C  CB  . ASN A  1 20  ? 49.179  34.120  18.577  1.00 6.40  ? 19  ASN A CB  1 
ATOM   130   C  CG  . ASN A  1 20  ? 49.176  33.260  19.795  1.00 8.95  ? 19  ASN A CG  1 
ATOM   131   O  OD1 . ASN A  1 20  ? 49.102  33.799  20.892  1.00 10.50 ? 19  ASN A OD1 1 
ATOM   132   N  ND2 . ASN A  1 20  ? 49.271  31.941  19.636  1.00 11.80 ? 19  ASN A ND2 1 
ATOM   133   N  N   . PHE A  1 21  ? 50.781  34.699  15.963  1.00 2.00  ? 20  PHE A N   1 
ATOM   134   C  CA  . PHE A  1 21  ? 50.734  35.214  14.606  1.00 2.95  ? 20  PHE A CA  1 
ATOM   135   C  C   . PHE A  1 21  ? 49.937  34.257  13.756  1.00 4.59  ? 20  PHE A C   1 
ATOM   136   O  O   . PHE A  1 21  ? 50.119  33.034  13.920  1.00 2.99  ? 20  PHE A O   1 
ATOM   137   C  CB  . PHE A  1 21  ? 52.099  35.292  13.949  1.00 2.00  ? 20  PHE A CB  1 
ATOM   138   C  CG  . PHE A  1 21  ? 53.060  36.161  14.749  1.00 3.34  ? 20  PHE A CG  1 
ATOM   139   C  CD1 . PHE A  1 21  ? 53.821  35.587  15.742  1.00 2.36  ? 20  PHE A CD1 1 
ATOM   140   C  CD2 . PHE A  1 21  ? 53.193  37.508  14.446  1.00 2.00  ? 20  PHE A CD2 1 
ATOM   141   C  CE1 . PHE A  1 21  ? 54.728  36.352  16.428  1.00 2.00  ? 20  PHE A CE1 1 
ATOM   142   C  CE2 . PHE A  1 21  ? 54.106  38.261  15.142  1.00 2.65  ? 20  PHE A CE2 1 
ATOM   143   C  CZ  . PHE A  1 21  ? 54.874  37.682  16.130  1.00 2.00  ? 20  PHE A CZ  1 
ATOM   144   N  N   . GLU A  1 22  ? 49.078  34.763  12.865  1.00 6.81  ? 21  GLU A N   1 
ATOM   145   C  CA  . GLU A  1 22  ? 48.326  33.913  11.954  1.00 10.10 ? 21  GLU A CA  1 
ATOM   146   C  C   . GLU A  1 22  ? 48.292  34.589  10.586  1.00 10.21 ? 21  GLU A C   1 
ATOM   147   O  O   . GLU A  1 22  ? 48.055  35.790  10.540  1.00 10.29 ? 21  GLU A O   1 
ATOM   148   C  CB  . GLU A  1 22  ? 46.921  33.721  12.465  1.00 14.50 ? 21  GLU A CB  1 
ATOM   149   C  CG  . GLU A  1 22  ? 45.944  33.045  11.491  1.00 23.00 ? 21  GLU A CG  1 
ATOM   150   C  CD  . GLU A  1 22  ? 44.578  32.702  12.101  1.00 29.37 ? 21  GLU A CD  1 
ATOM   151   O  OE1 . GLU A  1 22  ? 43.860  33.628  12.511  1.00 33.39 ? 21  GLU A OE1 1 
ATOM   152   O  OE2 . GLU A  1 22  ? 44.228  31.513  12.164  1.00 31.33 ? 21  GLU A OE2 1 
ATOM   153   N  N   . GLN A  1 23  ? 48.592  33.898  9.481   1.00 9.11  ? 22  GLN A N   1 
ATOM   154   C  CA  . GLN A  1 23  ? 48.544  34.409  8.106   1.00 7.07  ? 22  GLN A CA  1 
ATOM   155   C  C   . GLN A  1 23  ? 47.772  33.341  7.295   1.00 7.78  ? 22  GLN A C   1 
ATOM   156   O  O   . GLN A  1 23  ? 48.226  32.221  7.092   1.00 5.43  ? 22  GLN A O   1 
ATOM   157   C  CB  . GLN A  1 23  ? 49.946  34.558  7.591   1.00 3.53  ? 22  GLN A CB  1 
ATOM   158   C  CG  . GLN A  1 23  ? 50.029  35.124  6.221   1.00 2.00  ? 22  GLN A CG  1 
ATOM   159   C  CD  . GLN A  1 23  ? 51.447  35.322  5.765   1.00 2.00  ? 22  GLN A CD  1 
ATOM   160   O  OE1 . GLN A  1 23  ? 52.331  34.704  6.314   1.00 2.00  ? 22  GLN A OE1 1 
ATOM   161   N  NE2 . GLN A  1 23  ? 51.799  36.175  4.826   1.00 2.00  ? 22  GLN A NE2 1 
ATOM   162   N  N   . LYS A  1 24  ? 46.540  33.659  6.903   1.00 9.61  ? 23  LYS A N   1 
ATOM   163   C  CA  . LYS A  1 24  ? 45.666  32.750  6.201   1.00 11.61 ? 23  LYS A CA  1 
ATOM   164   C  C   . LYS A  1 24  ? 46.083  32.391  4.804   1.00 12.49 ? 23  LYS A C   1 
ATOM   165   O  O   . LYS A  1 24  ? 45.872  31.234  4.472   1.00 13.61 ? 23  LYS A O   1 
ATOM   166   C  CB  . LYS A  1 24  ? 44.265  33.305  6.140   1.00 15.45 ? 23  LYS A CB  1 
ATOM   167   C  CG  . LYS A  1 24  ? 43.568  33.039  7.458   1.00 22.42 ? 23  LYS A CG  1 
ATOM   168   C  CD  . LYS A  1 24  ? 42.065  33.350  7.436   1.00 26.91 ? 23  LYS A CD  1 
ATOM   169   C  CE  . LYS A  1 24  ? 41.457  32.961  8.798   1.00 31.13 ? 23  LYS A CE  1 
ATOM   170   N  NZ  . LYS A  1 24  ? 42.201  33.575  9.896   1.00 32.81 ? 23  LYS A NZ  1 
ATOM   171   N  N   . GLU A  1 25  ? 46.620  33.295  3.963   1.00 12.62 ? 24  GLU A N   1 
ATOM   172   C  CA  . GLU A  1 25  ? 47.190  32.933  2.668   1.00 12.44 ? 24  GLU A CA  1 
ATOM   173   C  C   . GLU A  1 25  ? 48.581  33.525  2.630   1.00 10.05 ? 24  GLU A C   1 
ATOM   174   O  O   . GLU A  1 25  ? 48.774  34.628  3.168   1.00 10.80 ? 24  GLU A O   1 
ATOM   175   C  CB  . GLU A  1 25  ? 46.486  33.526  1.444   1.00 18.07 ? 24  GLU A CB  1 
ATOM   176   C  CG  . GLU A  1 25  ? 45.083  33.000  1.054   1.00 26.41 ? 24  GLU A CG  1 
ATOM   177   C  CD  . GLU A  1 25  ? 43.869  33.821  1.512   1.00 29.54 ? 24  GLU A CD  1 
ATOM   178   O  OE1 . GLU A  1 25  ? 44.037  34.974  1.931   1.00 34.35 ? 24  GLU A OE1 1 
ATOM   179   O  OE2 . GLU A  1 25  ? 42.744  33.312  1.425   1.00 30.99 ? 24  GLU A OE2 1 
ATOM   180   N  N   . SER A  1 26  ? 49.529  32.927  1.914   1.00 5.49  ? 25  SER A N   1 
ATOM   181   C  CA  . SER A  1 26  ? 50.891  33.422  1.838   1.00 3.29  ? 25  SER A CA  1 
ATOM   182   C  C   . SER A  1 26  ? 51.105  34.890  1.464   1.00 4.13  ? 25  SER A C   1 
ATOM   183   O  O   . SER A  1 26  ? 52.163  35.432  1.797   1.00 5.16  ? 25  SER A O   1 
ATOM   184   C  CB  . SER A  1 26  ? 51.656  32.602  0.833   1.00 2.00  ? 25  SER A CB  1 
ATOM   185   O  OG  . SER A  1 26  ? 51.168  32.804  -0.496  1.00 4.37  ? 25  SER A OG  1 
ATOM   186   N  N   . ASN A  1 27  ? 50.182  35.496  0.704   1.00 4.33  ? 26  ASN A N   1 
ATOM   187   C  CA  . ASN A  1 27  ? 50.320  36.846  0.179   1.00 6.93  ? 26  ASN A CA  1 
ATOM   188   C  C   . ASN A  1 27  ? 49.361  37.807  0.814   1.00 9.16  ? 26  ASN A C   1 
ATOM   189   O  O   . ASN A  1 27  ? 48.985  38.799  0.200   1.00 12.02 ? 26  ASN A O   1 
ATOM   190   C  CB  . ASN A  1 27  ? 50.079  36.908  -1.340  1.00 7.49  ? 26  ASN A CB  1 
ATOM   191   C  CG  . ASN A  1 27  ? 48.680  36.560  -1.819  1.00 10.61 ? 26  ASN A CG  1 
ATOM   192   O  OD1 . ASN A  1 27  ? 48.099  35.514  -1.498  1.00 10.71 ? 26  ASN A OD1 1 
ATOM   193   N  ND2 . ASN A  1 27  ? 48.078  37.402  -2.636  1.00 16.11 ? 26  ASN A ND2 1 
ATOM   194   N  N   . GLY A  1 28  ? 48.932  37.512  2.034   1.00 9.08  ? 27  GLY A N   1 
ATOM   195   C  CA  . GLY A  1 28  ? 48.011  38.343  2.765   1.00 6.78  ? 27  GLY A CA  1 
ATOM   196   C  C   . GLY A  1 28  ? 48.635  38.668  4.121   1.00 8.92  ? 27  GLY A C   1 
ATOM   197   O  O   . GLY A  1 28  ? 49.760  38.276  4.458   1.00 9.21  ? 27  GLY A O   1 
ATOM   198   N  N   . PRO A  1 29  ? 47.913  39.373  4.962   1.00 8.77  ? 28  PRO A N   1 
ATOM   199   C  CA  . PRO A  1 29  ? 48.409  39.861  6.236   1.00 8.10  ? 28  PRO A CA  1 
ATOM   200   C  C   . PRO A  1 29  ? 48.482  38.871  7.379   1.00 6.43  ? 28  PRO A C   1 
ATOM   201   O  O   . PRO A  1 29  ? 47.713  37.922  7.504   1.00 9.11  ? 28  PRO A O   1 
ATOM   202   C  CB  . PRO A  1 29  ? 47.493  41.026  6.488   1.00 9.32  ? 28  PRO A CB  1 
ATOM   203   C  CG  . PRO A  1 29  ? 46.172  40.503  6.010   1.00 10.24 ? 28  PRO A CG  1 
ATOM   204   C  CD  . PRO A  1 29  ? 46.598  39.928  4.661   1.00 10.38 ? 28  PRO A CD  1 
ATOM   205   N  N   . VAL A  1 30  ? 49.405  39.169  8.249   1.00 4.98  ? 29  VAL A N   1 
ATOM   206   C  CA  . VAL A  1 30  ? 49.696  38.398  9.438   1.00 2.74  ? 29  VAL A CA  1 
ATOM   207   C  C   . VAL A  1 30  ? 48.883  39.113  10.534  1.00 4.32  ? 29  VAL A C   1 
ATOM   208   O  O   . VAL A  1 30  ? 48.956  40.350  10.627  1.00 2.00  ? 29  VAL A O   1 
ATOM   209   C  CB  . VAL A  1 30  ? 51.203  38.503  9.706   1.00 2.00  ? 29  VAL A CB  1 
ATOM   210   C  CG1 . VAL A  1 30  ? 51.617  37.708  10.892  1.00 2.76  ? 29  VAL A CG1 1 
ATOM   211   C  CG2 . VAL A  1 30  ? 51.949  38.026  8.503   1.00 2.00  ? 29  VAL A CG2 1 
ATOM   212   N  N   . LYS A  1 31  ? 48.059  38.388  11.289  1.00 4.38  ? 30  LYS A N   1 
ATOM   213   C  CA  . LYS A  1 31  ? 47.374  38.880  12.470  1.00 8.79  ? 30  LYS A CA  1 
ATOM   214   C  C   . LYS A  1 31  ? 48.264  38.636  13.661  1.00 7.91  ? 30  LYS A C   1 
ATOM   215   O  O   . LYS A  1 31  ? 48.656  37.476  13.832  1.00 6.53  ? 30  LYS A O   1 
ATOM   216   C  CB  . LYS A  1 31  ? 46.114  38.140  12.773  1.00 11.85 ? 30  LYS A CB  1 
ATOM   217   C  CG  . LYS A  1 31  ? 45.130  38.258  11.642  1.00 22.58 ? 30  LYS A CG  1 
ATOM   218   C  CD  . LYS A  1 31  ? 43.940  37.318  11.853  1.00 26.91 ? 30  LYS A CD  1 
ATOM   219   C  CE  . LYS A  1 31  ? 43.335  37.090  10.463  1.00 31.85 ? 30  LYS A CE  1 
ATOM   220   N  NZ  . LYS A  1 31  ? 41.907  37.373  10.471  1.00 35.49 ? 30  LYS A NZ  1 
ATOM   221   N  N   . VAL A  1 32  ? 48.642  39.635  14.463  1.00 7.80  ? 31  VAL A N   1 
ATOM   222   C  CA  . VAL A  1 32  ? 49.445  39.358  15.628  1.00 7.86  ? 31  VAL A CA  1 
ATOM   223   C  C   . VAL A  1 32  ? 48.620  39.751  16.841  1.00 10.28 ? 31  VAL A C   1 
ATOM   224   O  O   . VAL A  1 32  ? 47.935  40.780  16.814  1.00 10.76 ? 31  VAL A O   1 
ATOM   225   C  CB  . VAL A  1 32  ? 50.864  40.089  15.500  1.00 6.71  ? 31  VAL A CB  1 
ATOM   226   C  CG1 . VAL A  1 32  ? 50.892  40.969  14.276  1.00 2.00  ? 31  VAL A CG1 1 
ATOM   227   C  CG2 . VAL A  1 32  ? 51.243  40.788  16.815  1.00 7.33  ? 31  VAL A CG2 1 
ATOM   228   N  N   . TRP A  1 33  ? 48.591  38.922  17.895  1.00 10.06 ? 32  TRP A N   1 
ATOM   229   C  CA  . TRP A  1 33  ? 47.796  39.223  19.058  1.00 9.13  ? 32  TRP A CA  1 
ATOM   230   C  C   . TRP A  1 33  ? 48.233  38.528  20.317  1.00 9.82  ? 32  TRP A C   1 
ATOM   231   O  O   . TRP A  1 33  ? 48.777  37.425  20.226  1.00 10.98 ? 32  TRP A O   1 
ATOM   232   C  CB  . TRP A  1 33  ? 46.334  38.876  18.794  1.00 10.18 ? 32  TRP A CB  1 
ATOM   233   C  CG  . TRP A  1 33  ? 45.927  37.410  18.833  1.00 9.63  ? 32  TRP A CG  1 
ATOM   234   C  CD1 . TRP A  1 33  ? 45.414  36.817  19.961  1.00 10.75 ? 32  TRP A CD1 1 
ATOM   235   C  CD2 . TRP A  1 33  ? 46.048  36.535  17.792  1.00 10.39 ? 32  TRP A CD2 1 
ATOM   236   N  NE1 . TRP A  1 33  ? 45.235  35.550  19.635  1.00 10.99 ? 32  TRP A NE1 1 
ATOM   237   C  CE2 . TRP A  1 33  ? 45.615  35.352  18.361  1.00 9.41  ? 32  TRP A CE2 1 
ATOM   238   C  CE3 . TRP A  1 33  ? 46.496  36.599  16.496  1.00 10.55 ? 32  TRP A CE3 1 
ATOM   239   C  CZ2 . TRP A  1 33  ? 45.593  34.201  17.622  1.00 10.17 ? 32  TRP A CZ2 1 
ATOM   240   C  CZ3 . TRP A  1 33  ? 46.473  35.436  15.758  1.00 12.52 ? 32  TRP A CZ3 1 
ATOM   241   C  CH2 . TRP A  1 33  ? 46.042  34.249  16.317  1.00 11.71 ? 32  TRP A CH2 1 
ATOM   242   N  N   . GLY A  1 34  ? 47.980  39.107  21.490  1.00 9.23  ? 33  GLY A N   1 
ATOM   243   C  CA  . GLY A  1 34  ? 48.388  38.484  22.739  1.00 9.57  ? 33  GLY A CA  1 
ATOM   244   C  C   . GLY A  1 34  ? 48.580  39.480  23.872  1.00 9.47  ? 33  GLY A C   1 
ATOM   245   O  O   . GLY A  1 34  ? 48.064  40.590  23.806  1.00 12.85 ? 33  GLY A O   1 
ATOM   246   N  N   . SER A  1 35  ? 49.311  39.182  24.932  1.00 8.53  ? 34  SER A N   1 
ATOM   247   C  CA  . SER A  1 35  ? 49.490  40.114  26.016  1.00 10.05 ? 34  SER A CA  1 
ATOM   248   C  C   . SER A  1 35  ? 50.876  40.037  26.584  1.00 11.72 ? 34  SER A C   1 
ATOM   249   O  O   . SER A  1 35  ? 51.469  38.955  26.684  1.00 14.15 ? 34  SER A O   1 
ATOM   250   C  CB  . SER A  1 35  ? 48.587  39.847  27.175  1.00 11.30 ? 34  SER A CB  1 
ATOM   251   O  OG  . SER A  1 35  ? 47.239  40.138  26.865  1.00 21.13 ? 34  SER A OG  1 
ATOM   252   N  N   . ILE A  1 36  ? 51.410  41.172  26.967  1.00 9.01  ? 35  ILE A N   1 
ATOM   253   C  CA  . ILE A  1 36  ? 52.662  41.165  27.662  1.00 10.00 ? 35  ILE A CA  1 
ATOM   254   C  C   . ILE A  1 36  ? 52.280  41.598  29.090  1.00 11.60 ? 35  ILE A C   1 
ATOM   255   O  O   . ILE A  1 36  ? 51.192  42.142  29.305  1.00 14.06 ? 35  ILE A O   1 
ATOM   256   C  CB  . ILE A  1 36  ? 53.585  42.136  26.918  1.00 6.82  ? 35  ILE A CB  1 
ATOM   257   C  CG1 . ILE A  1 36  ? 53.535  41.866  25.410  1.00 3.95  ? 35  ILE A CG1 1 
ATOM   258   C  CG2 . ILE A  1 36  ? 55.002  41.947  27.451  1.00 2.36  ? 35  ILE A CG2 1 
ATOM   259   C  CD1 . ILE A  1 36  ? 54.130  42.957  24.518  1.00 2.00  ? 35  ILE A CD1 1 
ATOM   260   N  N   . LYS A  1 37  ? 53.076  41.377  30.130  1.00 13.34 ? 36  LYS A N   1 
ATOM   261   C  CA  . LYS A  1 37  ? 52.748  41.753  31.494  1.00 11.57 ? 36  LYS A CA  1 
ATOM   262   C  C   . LYS A  1 37  ? 54.019  42.273  32.149  1.00 10.62 ? 36  LYS A C   1 
ATOM   263   O  O   . LYS A  1 37  ? 55.132  41.961  31.715  1.00 10.79 ? 36  LYS A O   1 
ATOM   264   C  CB  . LYS A  1 37  ? 52.353  40.589  32.300  1.00 15.23 ? 36  LYS A CB  1 
ATOM   265   C  CG  . LYS A  1 37  ? 51.494  39.499  31.755  1.00 18.96 ? 36  LYS A CG  1 
ATOM   266   C  CD  . LYS A  1 37  ? 51.699  38.524  32.920  1.00 25.13 ? 36  LYS A CD  1 
ATOM   267   C  CE  . LYS A  1 37  ? 51.463  37.030  32.567  1.00 28.51 ? 36  LYS A CE  1 
ATOM   268   N  NZ  . LYS A  1 37  ? 52.002  36.179  33.617  1.00 28.90 ? 36  LYS A NZ  1 
ATOM   269   N  N   . GLY A  1 38  ? 53.907  43.055  33.205  1.00 9.53  ? 37  GLY A N   1 
ATOM   270   C  CA  . GLY A  1 38  ? 55.071  43.524  33.925  1.00 9.41  ? 37  GLY A CA  1 
ATOM   271   C  C   . GLY A  1 38  ? 55.669  44.758  33.289  1.00 9.96  ? 37  GLY A C   1 
ATOM   272   O  O   . GLY A  1 38  ? 56.826  45.143  33.541  1.00 10.18 ? 37  GLY A O   1 
ATOM   273   N  N   . LEU A  1 39  ? 54.840  45.401  32.476  1.00 8.04  ? 38  LEU A N   1 
ATOM   274   C  CA  . LEU A  1 39  ? 55.280  46.570  31.751  1.00 5.92  ? 38  LEU A CA  1 
ATOM   275   C  C   . LEU A  1 39  ? 54.949  47.786  32.594  1.00 5.09  ? 38  LEU A C   1 
ATOM   276   O  O   . LEU A  1 39  ? 54.034  47.736  33.399  1.00 6.20  ? 38  LEU A O   1 
ATOM   277   C  CB  . LEU A  1 39  ? 54.561  46.734  30.381  1.00 3.72  ? 38  LEU A CB  1 
ATOM   278   C  CG  . LEU A  1 39  ? 55.221  46.259  29.117  1.00 2.00  ? 38  LEU A CG  1 
ATOM   279   C  CD1 . LEU A  1 39  ? 56.744  46.294  29.148  1.00 2.00  ? 38  LEU A CD1 1 
ATOM   280   C  CD2 . LEU A  1 39  ? 54.817  44.886  28.965  1.00 2.97  ? 38  LEU A CD2 1 
ATOM   281   N  N   . THR A  1 40  ? 55.698  48.868  32.473  1.00 4.63  ? 39  THR A N   1 
ATOM   282   C  CA  . THR A  1 40  ? 55.324  50.141  33.026  1.00 4.96  ? 39  THR A CA  1 
ATOM   283   C  C   . THR A  1 40  ? 54.175  50.628  32.157  1.00 8.72  ? 39  THR A C   1 
ATOM   284   O  O   . THR A  1 40  ? 54.251  50.480  30.933  1.00 9.14  ? 39  THR A O   1 
ATOM   285   C  CB  . THR A  1 40  ? 56.519  51.141  32.949  1.00 3.89  ? 39  THR A CB  1 
ATOM   286   O  OG1 . THR A  1 40  ? 57.203  50.952  31.714  1.00 4.23  ? 39  THR A OG1 1 
ATOM   287   C  CG2 . THR A  1 40  ? 57.511  50.937  34.037  1.00 2.00  ? 39  THR A CG2 1 
ATOM   288   N  N   . GLU A  1 41  ? 53.107  51.192  32.711  1.00 11.58 ? 40  GLU A N   1 
ATOM   289   C  CA  . GLU A  1 41  ? 52.036  51.806  31.958  1.00 13.62 ? 40  GLU A CA  1 
ATOM   290   C  C   . GLU A  1 41  ? 52.438  52.768  30.828  1.00 12.48 ? 40  GLU A C   1 
ATOM   291   O  O   . GLU A  1 41  ? 53.221  53.710  30.989  1.00 11.33 ? 40  GLU A O   1 
ATOM   292   C  CB  . GLU A  1 41  ? 51.152  52.516  32.963  1.00 19.12 ? 40  GLU A CB  1 
ATOM   293   C  CG  . GLU A  1 41  ? 49.858  53.025  32.308  1.00 30.19 ? 40  GLU A CG  1 
ATOM   294   C  CD  . GLU A  1 41  ? 48.861  53.782  33.184  1.00 34.86 ? 40  GLU A CD  1 
ATOM   295   O  OE1 . GLU A  1 41  ? 49.294  54.594  34.011  1.00 39.07 ? 40  GLU A OE1 1 
ATOM   296   O  OE2 . GLU A  1 41  ? 47.652  53.569  33.018  1.00 36.30 ? 40  GLU A OE2 1 
ATOM   297   N  N   . GLY A  1 42  ? 51.911  52.562  29.635  1.00 12.93 ? 41  GLY A N   1 
ATOM   298   C  CA  . GLY A  1 42  ? 52.239  53.441  28.522  1.00 14.62 ? 41  GLY A CA  1 
ATOM   299   C  C   . GLY A  1 42  ? 52.720  52.696  27.309  1.00 12.49 ? 41  GLY A C   1 
ATOM   300   O  O   . GLY A  1 42  ? 52.531  51.493  27.216  1.00 17.23 ? 41  GLY A O   1 
ATOM   301   N  N   . LEU A  1 43  ? 53.428  53.332  26.408  1.00 11.19 ? 42  LEU A N   1 
ATOM   302   C  CA  . LEU A  1 43  ? 53.769  52.726  25.143  1.00 10.16 ? 42  LEU A CA  1 
ATOM   303   C  C   . LEU A  1 43  ? 55.079  51.959  25.070  1.00 12.20 ? 42  LEU A C   1 
ATOM   304   O  O   . LEU A  1 43  ? 56.066  52.423  25.636  1.00 16.21 ? 42  LEU A O   1 
ATOM   305   C  CB  . LEU A  1 43  ? 53.760  53.820  24.137  1.00 7.32  ? 42  LEU A CB  1 
ATOM   306   C  CG  . LEU A  1 43  ? 52.572  53.959  23.180  1.00 9.48  ? 42  LEU A CG  1 
ATOM   307   C  CD1 . LEU A  1 43  ? 51.257  53.566  23.786  1.00 6.12  ? 42  LEU A CD1 1 
ATOM   308   C  CD2 . LEU A  1 43  ? 52.566  55.413  22.724  1.00 7.37  ? 42  LEU A CD2 1 
ATOM   309   N  N   . HIS A  1 44  ? 55.219  50.811  24.397  1.00 9.58  ? 43  HIS A N   1 
ATOM   310   C  CA  . HIS A  1 44  ? 56.482  50.120  24.352  1.00 7.24  ? 43  HIS A CA  1 
ATOM   311   C  C   . HIS A  1 44  ? 56.786  49.640  22.950  1.00 6.81  ? 43  HIS A C   1 
ATOM   312   O  O   . HIS A  1 44  ? 55.934  49.022  22.311  1.00 5.28  ? 43  HIS A O   1 
ATOM   313   C  CB  . HIS A  1 44  ? 56.425  48.944  25.298  1.00 6.37  ? 43  HIS A CB  1 
ATOM   314   C  CG  . HIS A  1 44  ? 56.389  49.406  26.730  1.00 6.65  ? 43  HIS A CG  1 
ATOM   315   N  ND1 . HIS A  1 44  ? 57.406  49.784  27.492  1.00 7.91  ? 43  HIS A ND1 1 
ATOM   316   C  CD2 . HIS A  1 44  ? 55.246  49.533  27.469  1.00 4.75  ? 43  HIS A CD2 1 
ATOM   317   C  CE1 . HIS A  1 44  ? 56.956  50.139  28.659  1.00 4.42  ? 43  HIS A CE1 1 
ATOM   318   N  NE2 . HIS A  1 44  ? 55.658  49.975  28.620  1.00 6.41  ? 43  HIS A NE2 1 
ATOM   319   N  N   . GLY A  1 45  ? 57.990  49.932  22.479  1.00 6.40  ? 44  GLY A N   1 
ATOM   320   C  CA  . GLY A  1 45  ? 58.476  49.522  21.172  1.00 7.62  ? 44  GLY A CA  1 
ATOM   321   C  C   . GLY A  1 45  ? 58.295  48.027  21.000  1.00 8.24  ? 44  GLY A C   1 
ATOM   322   O  O   . GLY A  1 45  ? 58.567  47.230  21.910  1.00 7.86  ? 44  GLY A O   1 
ATOM   323   N  N   . PHE A  1 46  ? 57.769  47.670  19.844  1.00 7.26  ? 45  PHE A N   1 
ATOM   324   C  CA  . PHE A  1 46  ? 57.468  46.294  19.562  1.00 6.69  ? 45  PHE A CA  1 
ATOM   325   C  C   . PHE A  1 46  ? 58.107  45.984  18.227  1.00 6.46  ? 45  PHE A C   1 
ATOM   326   O  O   . PHE A  1 46  ? 57.642  46.469  17.190  1.00 10.06 ? 45  PHE A O   1 
ATOM   327   C  CB  . PHE A  1 46  ? 55.974  46.147  19.529  1.00 2.00  ? 45  PHE A CB  1 
ATOM   328   C  CG  . PHE A  1 46  ? 55.522  44.704  19.679  1.00 3.00  ? 45  PHE A CG  1 
ATOM   329   C  CD1 . PHE A  1 46  ? 56.134  43.854  20.581  1.00 2.70  ? 45  PHE A CD1 1 
ATOM   330   C  CD2 . PHE A  1 46  ? 54.440  44.273  18.930  1.00 2.00  ? 45  PHE A CD2 1 
ATOM   331   C  CE1 . PHE A  1 46  ? 55.642  42.583  20.745  1.00 4.71  ? 45  PHE A CE1 1 
ATOM   332   C  CE2 . PHE A  1 46  ? 53.963  43.016  19.095  1.00 2.00  ? 45  PHE A CE2 1 
ATOM   333   C  CZ  . PHE A  1 46  ? 54.559  42.162  20.003  1.00 6.56  ? 45  PHE A CZ  1 
ATOM   334   N  N   . HIS A  1 47  ? 59.186  45.214  18.152  1.00 5.95  ? 46  HIS A N   1 
ATOM   335   C  CA  . HIS A  1 47  ? 59.863  44.995  16.880  1.00 5.68  ? 46  HIS A CA  1 
ATOM   336   C  C   . HIS A  1 47  ? 60.381  43.598  16.715  1.00 5.37  ? 46  HIS A C   1 
ATOM   337   O  O   . HIS A  1 47  ? 60.726  42.902  17.656  1.00 6.06  ? 46  HIS A O   1 
ATOM   338   C  CB  . HIS A  1 47  ? 61.094  45.866  16.680  1.00 5.93  ? 46  HIS A CB  1 
ATOM   339   C  CG  . HIS A  1 47  ? 61.065  47.306  17.184  1.00 7.33  ? 46  HIS A CG  1 
ATOM   340   N  ND1 . HIS A  1 47  ? 61.917  47.820  18.084  1.00 9.83  ? 46  HIS A ND1 1 
ATOM   341   C  CD2 . HIS A  1 47  ? 60.145  48.273  16.818  1.00 5.49  ? 46  HIS A CD2 1 
ATOM   342   C  CE1 . HIS A  1 47  ? 61.528  49.066  18.274  1.00 8.62  ? 46  HIS A CE1 1 
ATOM   343   N  NE2 . HIS A  1 47  ? 60.466  49.328  17.520  1.00 7.08  ? 46  HIS A NE2 1 
ATOM   344   N  N   . VAL A  1 48  ? 60.500  43.158  15.485  1.00 6.70  ? 47  VAL A N   1 
ATOM   345   C  CA  . VAL A  1 48  ? 61.069  41.868  15.182  1.00 4.37  ? 47  VAL A CA  1 
ATOM   346   C  C   . VAL A  1 48  ? 62.535  42.188  14.882  1.00 5.21  ? 47  VAL A C   1 
ATOM   347   O  O   . VAL A  1 48  ? 62.887  42.962  13.973  1.00 6.08  ? 47  VAL A O   1 
ATOM   348   C  CB  . VAL A  1 48  ? 60.334  41.296  13.974  1.00 2.43  ? 47  VAL A CB  1 
ATOM   349   C  CG1 . VAL A  1 48  ? 60.950  39.979  13.620  1.00 2.00  ? 47  VAL A CG1 1 
ATOM   350   C  CG2 . VAL A  1 48  ? 58.856  41.139  14.263  1.00 2.00  ? 47  VAL A CG2 1 
ATOM   351   N  N   . HIS A  1 49  ? 63.438  41.717  15.717  1.00 3.62  ? 48  HIS A N   1 
ATOM   352   C  CA  . HIS A  1 49  ? 64.855  41.899  15.449  1.00 3.46  ? 48  HIS A CA  1 
ATOM   353   C  C   . HIS A  1 49  ? 65.329  40.745  14.558  1.00 3.52  ? 48  HIS A C   1 
ATOM   354   O  O   . HIS A  1 49  ? 64.710  39.678  14.491  1.00 3.77  ? 48  HIS A O   1 
ATOM   355   C  CB  . HIS A  1 49  ? 65.571  41.943  16.773  1.00 2.00  ? 48  HIS A CB  1 
ATOM   356   C  CG  . HIS A  1 49  ? 65.364  43.271  17.455  1.00 2.00  ? 48  HIS A CG  1 
ATOM   357   N  ND1 . HIS A  1 49  ? 66.307  44.096  17.822  1.00 2.00  ? 48  HIS A ND1 1 
ATOM   358   C  CD2 . HIS A  1 49  ? 64.151  43.832  17.797  1.00 4.77  ? 48  HIS A CD2 1 
ATOM   359   C  CE1 . HIS A  1 49  ? 65.687  45.124  18.364  1.00 4.26  ? 48  HIS A CE1 1 
ATOM   360   N  NE2 . HIS A  1 49  ? 64.372  44.978  18.357  1.00 4.79  ? 48  HIS A NE2 1 
ATOM   361   N  N   . GLU A  1 50  ? 66.467  40.893  13.916  1.00 2.45  ? 49  GLU A N   1 
ATOM   362   C  CA  . GLU A  1 50  ? 66.902  39.989  12.888  1.00 3.61  ? 49  GLU A CA  1 
ATOM   363   C  C   . GLU A  1 50  ? 67.228  38.545  13.185  1.00 5.97  ? 49  GLU A C   1 
ATOM   364   O  O   . GLU A  1 50  ? 66.926  37.655  12.372  1.00 6.67  ? 49  GLU A O   1 
ATOM   365   C  CB  . GLU A  1 50  ? 68.096  40.594  12.248  1.00 4.84  ? 49  GLU A CB  1 
ATOM   366   C  CG  . GLU A  1 50  ? 68.143  40.223  10.797  1.00 7.30  ? 49  GLU A CG  1 
ATOM   367   C  CD  . GLU A  1 50  ? 69.439  40.534  10.077  1.00 8.54  ? 49  GLU A CD  1 
ATOM   368   O  OE1 . GLU A  1 50  ? 70.122  41.501  10.426  1.00 11.40 ? 49  GLU A OE1 1 
ATOM   369   O  OE2 . GLU A  1 50  ? 69.751  39.783  9.144   1.00 11.10 ? 49  GLU A OE2 1 
ATOM   370   N  N   . PHE A  1 51  ? 67.922  38.316  14.308  1.00 3.80  ? 50  PHE A N   1 
ATOM   371   C  CA  . PHE A  1 51  ? 68.419  36.999  14.598  1.00 2.49  ? 50  PHE A CA  1 
ATOM   372   C  C   . PHE A  1 51  ? 67.644  36.397  15.701  1.00 3.43  ? 50  PHE A C   1 
ATOM   373   O  O   . PHE A  1 51  ? 67.240  37.091  16.620  1.00 3.29  ? 50  PHE A O   1 
ATOM   374   C  CB  . PHE A  1 51  ? 69.857  37.004  15.039  1.00 2.00  ? 50  PHE A CB  1 
ATOM   375   C  CG  . PHE A  1 51  ? 70.685  37.675  13.991  1.00 2.00  ? 50  PHE A CG  1 
ATOM   376   C  CD1 . PHE A  1 51  ? 70.817  37.081  12.757  1.00 3.02  ? 50  PHE A CD1 1 
ATOM   377   C  CD2 . PHE A  1 51  ? 71.253  38.883  14.273  1.00 2.00  ? 50  PHE A CD2 1 
ATOM   378   C  CE1 . PHE A  1 51  ? 71.534  37.704  11.782  1.00 2.00  ? 50  PHE A CE1 1 
ATOM   379   C  CE2 . PHE A  1 51  ? 71.971  39.503  13.287  1.00 2.00  ? 50  PHE A CE2 1 
ATOM   380   C  CZ  . PHE A  1 51  ? 72.104  38.912  12.054  1.00 2.00  ? 50  PHE A CZ  1 
ATOM   381   N  N   . GLY A  1 52  ? 67.384  35.102  15.682  1.00 4.74  ? 51  GLY A N   1 
ATOM   382   C  CA  . GLY A  1 52  ? 66.651  34.485  16.763  1.00 2.87  ? 51  GLY A CA  1 
ATOM   383   C  C   . GLY A  1 52  ? 67.705  33.761  17.509  1.00 2.00  ? 51  GLY A C   1 
ATOM   384   O  O   . GLY A  1 52  ? 67.698  32.537  17.568  1.00 3.95  ? 51  GLY A O   1 
ATOM   385   N  N   . ASP A  1 53  ? 68.655  34.553  17.947  1.00 2.00  ? 52  ASP A N   1 
ATOM   386   C  CA  . ASP A  1 53  ? 69.818  34.087  18.648  1.00 3.13  ? 52  ASP A CA  1 
ATOM   387   C  C   . ASP A  1 53  ? 69.650  34.667  20.009  1.00 4.50  ? 52  ASP A C   1 
ATOM   388   O  O   . ASP A  1 53  ? 69.681  35.894  20.158  1.00 6.36  ? 52  ASP A O   1 
ATOM   389   C  CB  . ASP A  1 53  ? 71.066  34.650  18.065  1.00 3.18  ? 52  ASP A CB  1 
ATOM   390   C  CG  . ASP A  1 53  ? 72.382  34.123  18.587  1.00 2.43  ? 52  ASP A CG  1 
ATOM   391   O  OD1 . ASP A  1 53  ? 72.565  33.895  19.791  1.00 2.00  ? 52  ASP A OD1 1 
ATOM   392   O  OD2 . ASP A  1 53  ? 73.228  33.962  17.712  1.00 3.08  ? 52  ASP A OD2 1 
ATOM   393   N  N   . ASN A  1 54  ? 69.497  33.768  20.952  1.00 3.30  ? 53  ASN A N   1 
ATOM   394   C  CA  . ASN A  1 54  ? 69.346  34.190  22.304  1.00 3.90  ? 53  ASN A CA  1 
ATOM   395   C  C   . ASN A  1 54  ? 70.452  33.800  23.251  1.00 2.74  ? 53  ASN A C   1 
ATOM   396   O  O   . ASN A  1 54  ? 70.231  33.652  24.450  1.00 2.00  ? 53  ASN A O   1 
ATOM   397   C  CB  . ASN A  1 54  ? 68.026  33.666  22.764  1.00 11.33 ? 53  ASN A CB  1 
ATOM   398   C  CG  . ASN A  1 54  ? 67.191  34.862  23.146  1.00 20.05 ? 53  ASN A CG  1 
ATOM   399   O  OD1 . ASN A  1 54  ? 67.099  35.143  24.352  1.00 24.65 ? 53  ASN A OD1 1 
ATOM   400   N  ND2 . ASN A  1 54  ? 66.608  35.591  22.166  1.00 18.89 ? 53  ASN A ND2 1 
ATOM   401   N  N   . THR A  1 55  ? 71.700  33.722  22.793  1.00 2.00  ? 54  THR A N   1 
ATOM   402   C  CA  . THR A  1 55  ? 72.732  33.222  23.664  1.00 2.00  ? 54  THR A CA  1 
ATOM   403   C  C   . THR A  1 55  ? 73.126  34.225  24.712  1.00 3.99  ? 54  THR A C   1 
ATOM   404   O  O   . THR A  1 55  ? 73.639  33.913  25.792  1.00 2.31  ? 54  THR A O   1 
ATOM   405   C  CB  . THR A  1 55  ? 73.912  32.831  22.798  1.00 5.96  ? 54  THR A CB  1 
ATOM   406   O  OG1 . THR A  1 55  ? 74.276  33.994  22.115  1.00 6.54  ? 54  THR A OG1 1 
ATOM   407   C  CG2 . THR A  1 55  ? 73.595  31.719  21.783  1.00 7.03  ? 54  THR A CG2 1 
ATOM   408   N  N   . ALA A  1 56  ? 72.941  35.488  24.289  1.00 5.21  ? 55  ALA A N   1 
ATOM   409   C  CA  . ALA A  1 56  ? 73.221  36.635  25.097  1.00 2.20  ? 55  ALA A CA  1 
ATOM   410   C  C   . ALA A  1 56  ? 71.924  37.314  25.527  1.00 3.68  ? 55  ALA A C   1 
ATOM   411   O  O   . ALA A  1 56  ? 71.856  38.536  25.759  1.00 4.10  ? 55  ALA A O   1 
ATOM   412   C  CB  . ALA A  1 56  ? 74.072  37.494  24.250  1.00 2.00  ? 55  ALA A CB  1 
ATOM   413   N  N   . GLY A  1 57  ? 70.861  36.529  25.674  1.00 3.10  ? 56  GLY A N   1 
ATOM   414   C  CA  . GLY A  1 57  ? 69.540  37.039  26.009  1.00 2.95  ? 56  GLY A CA  1 
ATOM   415   C  C   . GLY A  1 57  ? 69.012  37.820  24.822  1.00 5.08  ? 56  GLY A C   1 
ATOM   416   O  O   . GLY A  1 57  ? 69.185  37.419  23.658  1.00 4.91  ? 56  GLY A O   1 
ATOM   417   N  N   . CYS A  1 58  ? 68.450  39.009  25.051  1.00 6.48  ? 57  CYS A N   1 
ATOM   418   C  CA  . CYS A  1 58  ? 67.937  39.772  23.924  1.00 5.73  ? 57  CYS A CA  1 
ATOM   419   C  C   . CYS A  1 58  ? 69.021  40.489  23.163  1.00 4.58  ? 57  CYS A C   1 
ATOM   420   O  O   . CYS A  1 58  ? 68.811  40.890  22.020  1.00 4.09  ? 57  CYS A O   1 
ATOM   421   C  CB  . CYS A  1 58  ? 66.926  40.797  24.379  1.00 5.73  ? 57  CYS A CB  1 
ATOM   422   S  SG  . CYS A  1 58  ? 65.525  40.017  25.181  1.00 5.72  ? 57  CYS A SG  1 
ATOM   423   N  N   . THR A  1 59  ? 70.191  40.643  23.774  1.00 4.67  ? 58  THR A N   1 
ATOM   424   C  CA  . THR A  1 59  ? 71.310  41.357  23.147  1.00 5.50  ? 58  THR A CA  1 
ATOM   425   C  C   . THR A  1 59  ? 71.831  40.706  21.855  1.00 3.37  ? 58  THR A C   1 
ATOM   426   O  O   . THR A  1 59  ? 72.228  41.429  20.942  1.00 2.00  ? 58  THR A O   1 
ATOM   427   C  CB  . THR A  1 59  ? 72.452  41.498  24.218  1.00 5.29  ? 58  THR A CB  1 
ATOM   428   O  OG1 . THR A  1 59  ? 71.834  41.737  25.491  1.00 7.50  ? 58  THR A OG1 1 
ATOM   429   C  CG2 . THR A  1 59  ? 73.366  42.671  23.932  1.00 6.03  ? 58  THR A CG2 1 
ATOM   430   N  N   . SER A  1 60  ? 71.761  39.376  21.721  1.00 2.00  ? 59  SER A N   1 
ATOM   431   C  CA  . SER A  1 60  ? 72.291  38.730  20.552  1.00 2.00  ? 59  SER A CA  1 
ATOM   432   C  C   . SER A  1 60  ? 71.328  38.701  19.371  1.00 3.74  ? 59  SER A C   1 
ATOM   433   O  O   . SER A  1 60  ? 71.683  38.278  18.267  1.00 6.18  ? 59  SER A O   1 
ATOM   434   C  CB  . SER A  1 60  ? 72.713  37.309  20.897  1.00 2.00  ? 59  SER A CB  1 
ATOM   435   O  OG  . SER A  1 60  ? 71.973  36.694  21.923  1.00 2.00  ? 59  SER A OG  1 
ATOM   436   N  N   . ALA A  1 61  ? 70.116  39.203  19.542  1.00 2.16  ? 60  ALA A N   1 
ATOM   437   C  CA  . ALA A  1 61  ? 69.129  39.187  18.488  1.00 2.48  ? 60  ALA A CA  1 
ATOM   438   C  C   . ALA A  1 61  ? 69.489  40.120  17.360  1.00 4.12  ? 60  ALA A C   1 
ATOM   439   O  O   . ALA A  1 61  ? 68.862  40.096  16.303  1.00 5.75  ? 60  ALA A O   1 
ATOM   440   C  CB  . ALA A  1 61  ? 67.764  39.633  18.973  1.00 2.43  ? 60  ALA A CB  1 
ATOM   441   N  N   . GLY A  1 62  ? 70.456  40.994  17.559  1.00 6.25  ? 61  GLY A N   1 
ATOM   442   C  CA  . GLY A  1 62  ? 70.881  41.907  16.509  1.00 7.14  ? 61  GLY A CA  1 
ATOM   443   C  C   . GLY A  1 62  ? 69.873  43.015  16.197  1.00 5.43  ? 61  GLY A C   1 
ATOM   444   O  O   . GLY A  1 62  ? 68.911  43.254  16.930  1.00 5.63  ? 61  GLY A O   1 
ATOM   445   N  N   . PRO A  1 63  ? 70.064  43.764  15.113  1.00 6.51  ? 62  PRO A N   1 
ATOM   446   C  CA  . PRO A  1 63  ? 69.263  44.942  14.758  1.00 4.94  ? 62  PRO A CA  1 
ATOM   447   C  C   . PRO A  1 63  ? 67.875  44.569  14.292  1.00 6.21  ? 62  PRO A C   1 
ATOM   448   O  O   . PRO A  1 63  ? 67.580  43.367  14.176  1.00 6.52  ? 62  PRO A O   1 
ATOM   449   C  CB  . PRO A  1 63  ? 70.063  45.588  13.697  1.00 4.79  ? 62  PRO A CB  1 
ATOM   450   C  CG  . PRO A  1 63  ? 70.606  44.386  12.974  1.00 5.19  ? 62  PRO A CG  1 
ATOM   451   C  CD  . PRO A  1 63  ? 71.113  43.526  14.120  1.00 5.71  ? 62  PRO A CD  1 
ATOM   452   N  N   . HIS A  1 64  ? 67.046  45.580  13.974  1.00 5.95  ? 63  HIS A N   1 
ATOM   453   C  CA  . HIS A  1 64  ? 65.686  45.325  13.502  1.00 7.28  ? 63  HIS A CA  1 
ATOM   454   C  C   . HIS A  1 64  ? 65.792  44.571  12.204  1.00 4.30  ? 63  HIS A C   1 
ATOM   455   O  O   . HIS A  1 64  ? 66.714  44.880  11.451  1.00 2.41  ? 63  HIS A O   1 
ATOM   456   C  CB  . HIS A  1 64  ? 64.883  46.619  13.237  1.00 11.03 ? 63  HIS A CB  1 
ATOM   457   C  CG  . HIS A  1 64  ? 64.462  47.383  14.501  1.00 12.39 ? 63  HIS A CG  1 
ATOM   458   N  ND1 . HIS A  1 64  ? 64.240  48.685  14.655  1.00 11.96 ? 63  HIS A ND1 1 
ATOM   459   C  CD2 . HIS A  1 64  ? 64.268  46.763  15.712  1.00 15.73 ? 63  HIS A CD2 1 
ATOM   460   C  CE1 . HIS A  1 64  ? 63.932  48.806  15.943  1.00 14.04 ? 63  HIS A CE1 1 
ATOM   461   N  NE2 . HIS A  1 64  ? 63.930  47.653  16.628  1.00 21.15 ? 63  HIS A NE2 1 
ATOM   462   N  N   . PHE A  1 65  ? 64.921  43.591  11.969  1.00 2.64  ? 64  PHE A N   1 
ATOM   463   C  CA  . PHE A  1 65  ? 64.956  42.805  10.751  1.00 3.30  ? 64  PHE A CA  1 
ATOM   464   C  C   . PHE A  1 65  ? 64.587  43.812  9.708   1.00 2.81  ? 64  PHE A C   1 
ATOM   465   O  O   . PHE A  1 65  ? 63.529  44.445  9.784   1.00 3.60  ? 64  PHE A O   1 
ATOM   466   C  CB  . PHE A  1 65  ? 63.910  41.655  10.746  1.00 2.65  ? 64  PHE A CB  1 
ATOM   467   C  CG  . PHE A  1 65  ? 63.748  40.862  9.433   1.00 3.93  ? 64  PHE A CG  1 
ATOM   468   C  CD1 . PHE A  1 65  ? 64.854  40.401  8.720   1.00 2.83  ? 64  PHE A CD1 1 
ATOM   469   C  CD2 . PHE A  1 65  ? 62.472  40.612  8.944   1.00 3.69  ? 64  PHE A CD2 1 
ATOM   470   C  CE1 . PHE A  1 65  ? 64.674  39.688  7.546   1.00 3.52  ? 64  PHE A CE1 1 
ATOM   471   C  CE2 . PHE A  1 65  ? 62.304  39.888  7.763   1.00 5.60  ? 64  PHE A CE2 1 
ATOM   472   C  CZ  . PHE A  1 65  ? 63.404  39.433  7.056   1.00 2.79  ? 64  PHE A CZ  1 
ATOM   473   N  N   . ASN A  1 66  ? 65.487  43.946  8.768   1.00 4.58  ? 65  ASN A N   1 
ATOM   474   C  CA  . ASN A  1 66  ? 65.350  44.947  7.738   1.00 8.02  ? 65  ASN A CA  1 
ATOM   475   C  C   . ASN A  1 66  ? 65.820  44.401  6.400   1.00 7.60  ? 65  ASN A C   1 
ATOM   476   O  O   . ASN A  1 66  ? 66.836  44.879  5.901   1.00 9.81  ? 65  ASN A O   1 
ATOM   477   C  CB  . ASN A  1 66  ? 66.182  46.183  8.204   1.00 8.58  ? 65  ASN A CB  1 
ATOM   478   C  CG  . ASN A  1 66  ? 66.144  47.432  7.337   1.00 8.98  ? 65  ASN A CG  1 
ATOM   479   O  OD1 . ASN A  1 66  ? 65.171  47.737  6.641   1.00 6.18  ? 65  ASN A OD1 1 
ATOM   480   N  ND2 . ASN A  1 66  ? 67.196  48.246  7.409   1.00 9.00  ? 65  ASN A ND2 1 
ATOM   481   N  N   . PRO A  1 67  ? 65.205  43.421  5.729   1.00 5.91  ? 66  PRO A N   1 
ATOM   482   C  CA  . PRO A  1 67  ? 65.710  42.848  4.507   1.00 5.20  ? 66  PRO A CA  1 
ATOM   483   C  C   . PRO A  1 67  ? 65.834  43.867  3.385   1.00 8.28  ? 66  PRO A C   1 
ATOM   484   O  O   . PRO A  1 67  ? 66.781  43.723  2.627   1.00 9.11  ? 66  PRO A O   1 
ATOM   485   C  CB  . PRO A  1 67  ? 64.752  41.737  4.196   1.00 2.22  ? 66  PRO A CB  1 
ATOM   486   C  CG  . PRO A  1 67  ? 63.476  42.269  4.650   1.00 2.00  ? 66  PRO A CG  1 
ATOM   487   C  CD  . PRO A  1 67  ? 63.889  42.923  5.983   1.00 5.27  ? 66  PRO A CD  1 
ATOM   488   N  N   . LEU A  1 68  ? 64.996  44.918  3.218   1.00 10.73 ? 67  LEU A N   1 
ATOM   489   C  CA  . LEU A  1 68  ? 65.166  45.832  2.075   1.00 12.43 ? 67  LEU A CA  1 
ATOM   490   C  C   . LEU A  1 68  ? 65.994  47.071  2.434   1.00 14.27 ? 67  LEU A C   1 
ATOM   491   O  O   . LEU A  1 68  ? 65.927  48.065  1.722   1.00 15.16 ? 67  LEU A O   1 
ATOM   492   C  CB  . LEU A  1 68  ? 63.816  46.317  1.515   1.00 9.99  ? 67  LEU A CB  1 
ATOM   493   C  CG  . LEU A  1 68  ? 62.611  45.391  1.553   1.00 13.82 ? 67  LEU A CG  1 
ATOM   494   C  CD1 . LEU A  1 68  ? 61.441  46.096  0.943   1.00 12.85 ? 67  LEU A CD1 1 
ATOM   495   C  CD2 . LEU A  1 68  ? 62.872  44.115  0.781   1.00 17.42 ? 67  LEU A CD2 1 
ATOM   496   N  N   . SER A  1 69  ? 66.790  47.101  3.513   1.00 18.02 ? 68  SER A N   1 
ATOM   497   C  CA  . SER A  1 69  ? 67.567  48.280  3.919   1.00 19.82 ? 68  SER A CA  1 
ATOM   498   C  C   . SER A  1 69  ? 66.864  49.657  3.869   1.00 19.51 ? 68  SER A C   1 
ATOM   499   O  O   . SER A  1 69  ? 67.401  50.670  3.394   1.00 20.99 ? 68  SER A O   1 
ATOM   500   C  CB  . SER A  1 69  ? 68.863  48.324  3.069   1.00 23.74 ? 68  SER A CB  1 
ATOM   501   O  OG  . SER A  1 69  ? 69.657  47.121  3.107   1.00 30.41 ? 68  SER A OG  1 
ATOM   502   N  N   . ARG A  1 70  ? 65.629  49.765  4.353   1.00 17.74 ? 69  ARG A N   1 
ATOM   503   C  CA  . ARG A  1 70  ? 65.007  51.079  4.432   1.00 15.53 ? 69  ARG A CA  1 
ATOM   504   C  C   . ARG A  1 70  ? 65.331  51.567  5.843   1.00 15.10 ? 69  ARG A C   1 
ATOM   505   O  O   . ARG A  1 70  ? 66.094  50.905  6.562   1.00 14.43 ? 69  ARG A O   1 
ATOM   506   C  CB  . ARG A  1 70  ? 63.545  51.005  4.306   1.00 15.21 ? 69  ARG A CB  1 
ATOM   507   C  CG  . ARG A  1 70  ? 63.132  50.457  2.993   1.00 16.87 ? 69  ARG A CG  1 
ATOM   508   C  CD  . ARG A  1 70  ? 61.672  50.642  3.246   1.00 22.62 ? 69  ARG A CD  1 
ATOM   509   N  NE  . ARG A  1 70  ? 60.711  50.243  2.232   1.00 27.31 ? 69  ARG A NE  1 
ATOM   510   C  CZ  . ARG A  1 70  ? 60.748  50.643  0.959   1.00 28.66 ? 69  ARG A CZ  1 
ATOM   511   N  NH1 . ARG A  1 70  ? 61.730  51.411  0.450   1.00 27.59 ? 69  ARG A NH1 1 
ATOM   512   N  NH2 . ARG A  1 70  ? 59.760  50.197  0.184   1.00 30.63 ? 69  ARG A NH2 1 
ATOM   513   N  N   . LYS A  1 71  ? 64.829  52.705  6.300   1.00 12.20 ? 70  LYS A N   1 
ATOM   514   C  CA  . LYS A  1 71  ? 65.189  53.112  7.624   1.00 11.15 ? 70  LYS A CA  1 
ATOM   515   C  C   . LYS A  1 71  ? 63.920  52.936  8.437   1.00 7.80  ? 70  LYS A C   1 
ATOM   516   O  O   . LYS A  1 71  ? 62.833  52.702  7.886   1.00 8.90  ? 70  LYS A O   1 
ATOM   517   C  CB  . LYS A  1 71  ? 65.676  54.560  7.641   1.00 12.78 ? 70  LYS A CB  1 
ATOM   518   C  CG  . LYS A  1 71  ? 64.572  55.538  7.374   1.00 15.65 ? 70  LYS A CG  1 
ATOM   519   C  CD  . LYS A  1 71  ? 65.061  56.983  7.354   1.00 22.61 ? 70  LYS A CD  1 
ATOM   520   C  CE  . LYS A  1 71  ? 66.060  57.296  6.226   1.00 22.31 ? 70  LYS A CE  1 
ATOM   521   N  NZ  . LYS A  1 71  ? 67.420  57.272  6.733   1.00 24.53 ? 70  LYS A NZ  1 
ATOM   522   N  N   . HIS A  1 72  ? 64.134  53.023  9.739   1.00 2.00  ? 71  HIS A N   1 
ATOM   523   C  CA  . HIS A  1 72  ? 63.131  52.785  10.708  1.00 2.00  ? 71  HIS A CA  1 
ATOM   524   C  C   . HIS A  1 72  ? 61.912  53.607  10.462  1.00 2.00  ? 71  HIS A C   1 
ATOM   525   O  O   . HIS A  1 72  ? 62.022  54.781  10.106  1.00 5.28  ? 71  HIS A O   1 
ATOM   526   C  CB  . HIS A  1 72  ? 63.741  53.081  12.064  1.00 3.88  ? 71  HIS A CB  1 
ATOM   527   C  CG  . HIS A  1 72  ? 62.885  52.583  13.203  1.00 5.05  ? 71  HIS A CG  1 
ATOM   528   N  ND1 . HIS A  1 72  ? 62.634  51.339  13.530  1.00 3.85  ? 71  HIS A ND1 1 
ATOM   529   C  CD2 . HIS A  1 72  ? 62.128  53.387  14.016  1.00 6.85  ? 71  HIS A CD2 1 
ATOM   530   C  CE1 . HIS A  1 72  ? 61.756  51.353  14.499  1.00 2.90  ? 71  HIS A CE1 1 
ATOM   531   N  NE2 . HIS A  1 72  ? 61.448  52.584  14.783  1.00 3.54  ? 71  HIS A NE2 1 
ATOM   532   N  N   . GLY A  1 73  ? 60.778  52.995  10.712  1.00 2.00  ? 72  GLY A N   1 
ATOM   533   C  CA  . GLY A  1 73  ? 59.510  53.660  10.582  1.00 3.21  ? 72  GLY A CA  1 
ATOM   534   C  C   . GLY A  1 73  ? 58.545  53.025  11.549  1.00 3.43  ? 72  GLY A C   1 
ATOM   535   O  O   . GLY A  1 73  ? 58.909  52.217  12.405  1.00 7.10  ? 72  GLY A O   1 
ATOM   536   N  N   . GLY A  1 74  ? 57.298  53.401  11.454  1.00 4.19  ? 73  GLY A N   1 
ATOM   537   C  CA  . GLY A  1 74  ? 56.224  52.750  12.189  1.00 5.72  ? 73  GLY A CA  1 
ATOM   538   C  C   . GLY A  1 74  ? 55.492  51.722  11.315  1.00 6.16  ? 73  GLY A C   1 
ATOM   539   O  O   . GLY A  1 74  ? 55.799  51.611  10.129  1.00 6.19  ? 73  GLY A O   1 
ATOM   540   N  N   . PRO A  1 75  ? 54.488  50.974  11.777  1.00 7.84  ? 74  PRO A N   1 
ATOM   541   C  CA  . PRO A  1 75  ? 53.880  49.893  11.016  1.00 10.39 ? 74  PRO A CA  1 
ATOM   542   C  C   . PRO A  1 75  ? 53.271  50.373  9.716   1.00 14.22 ? 74  PRO A C   1 
ATOM   543   O  O   . PRO A  1 75  ? 53.302  49.685  8.693   1.00 17.95 ? 74  PRO A O   1 
ATOM   544   C  CB  . PRO A  1 75  ? 52.828  49.295  11.891  1.00 9.89  ? 74  PRO A CB  1 
ATOM   545   C  CG  . PRO A  1 75  ? 53.103  49.883  13.260  1.00 8.51  ? 74  PRO A CG  1 
ATOM   546   C  CD  . PRO A  1 75  ? 53.735  51.236  12.994  1.00 6.92  ? 74  PRO A CD  1 
ATOM   547   N  N   . LYS A  1 76  ? 52.737  51.591  9.751   1.00 14.85 ? 75  LYS A N   1 
ATOM   548   C  CA  . LYS A  1 76  ? 52.044  52.100  8.599   1.00 18.97 ? 75  LYS A CA  1 
ATOM   549   C  C   . LYS A  1 76  ? 52.857  53.010  7.700   1.00 20.08 ? 75  LYS A C   1 
ATOM   550   O  O   . LYS A  1 76  ? 52.271  53.708  6.879   1.00 22.53 ? 75  LYS A O   1 
ATOM   551   C  CB  . LYS A  1 76  ? 50.792  52.814  9.091   1.00 20.56 ? 75  LYS A CB  1 
ATOM   552   C  CG  . LYS A  1 76  ? 49.886  51.939  9.936   1.00 25.63 ? 75  LYS A CG  1 
ATOM   553   C  CD  . LYS A  1 76  ? 49.385  50.725  9.129   1.00 31.56 ? 75  LYS A CD  1 
ATOM   554   C  CE  . LYS A  1 76  ? 49.038  49.459  9.971   1.00 35.12 ? 75  LYS A CE  1 
ATOM   555   N  NZ  . LYS A  1 76  ? 47.770  49.532  10.696  1.00 35.92 ? 75  LYS A NZ  1 
ATOM   556   N  N   . ASP A  1 77  ? 54.184  53.107  7.806   1.00 21.75 ? 76  ASP A N   1 
ATOM   557   C  CA  . ASP A  1 77  ? 54.966  53.968  6.919   1.00 21.52 ? 76  ASP A CA  1 
ATOM   558   C  C   . ASP A  1 77  ? 55.479  53.156  5.711   1.00 21.21 ? 76  ASP A C   1 
ATOM   559   O  O   . ASP A  1 77  ? 55.397  51.935  5.661   1.00 21.40 ? 76  ASP A O   1 
ATOM   560   C  CB  . ASP A  1 77  ? 56.174  54.573  7.663   1.00 22.69 ? 76  ASP A CB  1 
ATOM   561   C  CG  . ASP A  1 77  ? 55.975  55.623  8.766   1.00 23.99 ? 76  ASP A CG  1 
ATOM   562   O  OD1 . ASP A  1 77  ? 54.865  56.113  8.998   1.00 23.99 ? 76  ASP A OD1 1 
ATOM   563   O  OD2 . ASP A  1 77  ? 56.977  55.965  9.404   1.00 25.00 ? 76  ASP A OD2 1 
ATOM   564   N  N   . GLU A  1 78  ? 56.008  53.812  4.682   1.00 21.49 ? 77  GLU A N   1 
ATOM   565   C  CA  . GLU A  1 78  ? 56.587  53.176  3.509   1.00 21.94 ? 77  GLU A CA  1 
ATOM   566   C  C   . GLU A  1 78  ? 57.968  52.631  3.861   1.00 22.19 ? 77  GLU A C   1 
ATOM   567   O  O   . GLU A  1 78  ? 58.352  51.462  3.650   1.00 21.48 ? 77  GLU A O   1 
ATOM   568   C  CB  . GLU A  1 78  ? 56.755  54.182  2.396   1.00 25.12 ? 77  GLU A CB  1 
ATOM   569   C  CG  . GLU A  1 78  ? 56.317  53.700  1.013   1.00 33.93 ? 77  GLU A CG  1 
ATOM   570   C  CD  . GLU A  1 78  ? 54.813  53.837  0.711   1.00 39.55 ? 77  GLU A CD  1 
ATOM   571   O  OE1 . GLU A  1 78  ? 53.970  53.657  1.612   1.00 41.35 ? 77  GLU A OE1 1 
ATOM   572   O  OE2 . GLU A  1 78  ? 54.488  54.138  -0.450  1.00 42.00 ? 77  GLU A OE2 1 
ATOM   573   N  N   . GLU A  1 79  ? 58.656  53.626  4.428   1.00 19.72 ? 78  GLU A N   1 
ATOM   574   C  CA  . GLU A  1 79  ? 60.020  53.546  4.861   1.00 17.11 ? 78  GLU A CA  1 
ATOM   575   C  C   . GLU A  1 79  ? 59.828  53.110  6.296   1.00 15.88 ? 78  GLU A C   1 
ATOM   576   O  O   . GLU A  1 79  ? 59.468  53.854  7.206   1.00 16.46 ? 78  GLU A O   1 
ATOM   577   C  CB  . GLU A  1 79  ? 60.623  54.920  4.763   1.00 15.98 ? 78  GLU A CB  1 
ATOM   578   C  CG  . GLU A  1 79  ? 62.138  55.018  4.864   1.00 21.70 ? 78  GLU A CG  1 
ATOM   579   C  CD  . GLU A  1 79  ? 63.045  54.527  3.721   1.00 26.10 ? 78  GLU A CD  1 
ATOM   580   O  OE1 . GLU A  1 79  ? 62.588  54.189  2.618   1.00 29.55 ? 78  GLU A OE1 1 
ATOM   581   O  OE2 . GLU A  1 79  ? 64.259  54.503  3.940   1.00 28.70 ? 78  GLU A OE2 1 
ATOM   582   N  N   . ARG A  1 80  ? 59.886  51.813  6.399   1.00 12.90 ? 79  ARG A N   1 
ATOM   583   C  CA  . ARG A  1 80  ? 59.811  51.141  7.659   1.00 11.33 ? 79  ARG A CA  1 
ATOM   584   C  C   . ARG A  1 80  ? 60.756  49.981  7.486   1.00 10.32 ? 79  ARG A C   1 
ATOM   585   O  O   . ARG A  1 80  ? 61.267  49.703  6.395   1.00 12.93 ? 79  ARG A O   1 
ATOM   586   C  CB  . ARG A  1 80  ? 58.365  50.675  7.932   1.00 12.00 ? 79  ARG A CB  1 
ATOM   587   C  CG  . ARG A  1 80  ? 57.750  49.649  7.001   1.00 12.34 ? 79  ARG A CG  1 
ATOM   588   C  CD  . ARG A  1 80  ? 57.572  48.358  7.763   1.00 12.38 ? 79  ARG A CD  1 
ATOM   589   N  NE  . ARG A  1 80  ? 56.241  48.164  8.288   1.00 13.04 ? 79  ARG A NE  1 
ATOM   590   C  CZ  . ARG A  1 80  ? 55.881  46.985  8.802   1.00 13.32 ? 79  ARG A CZ  1 
ATOM   591   N  NH1 . ARG A  1 80  ? 56.684  45.941  8.934   1.00 14.76 ? 79  ARG A NH1 1 
ATOM   592   N  NH2 . ARG A  1 80  ? 54.663  46.838  9.241   1.00 11.36 ? 79  ARG A NH2 1 
ATOM   593   N  N   . HIS A  1 81  ? 61.019  49.289  8.568   1.00 6.48  ? 80  HIS A N   1 
ATOM   594   C  CA  . HIS A  1 81  ? 61.841  48.114  8.472   1.00 5.96  ? 80  HIS A CA  1 
ATOM   595   C  C   . HIS A  1 81  ? 60.812  47.031  8.571   1.00 5.03  ? 80  HIS A C   1 
ATOM   596   O  O   . HIS A  1 81  ? 59.780  47.235  9.209   1.00 7.21  ? 80  HIS A O   1 
ATOM   597   C  CB  . HIS A  1 81  ? 62.725  47.898  9.617   1.00 4.74  ? 80  HIS A CB  1 
ATOM   598   C  CG  . HIS A  1 81  ? 63.768  48.942  9.918   1.00 3.37  ? 80  HIS A CG  1 
ATOM   599   N  ND1 . HIS A  1 81  ? 64.032  49.365  11.129  1.00 2.80  ? 80  HIS A ND1 1 
ATOM   600   C  CD2 . HIS A  1 81  ? 64.741  49.396  9.109   1.00 2.08  ? 80  HIS A CD2 1 
ATOM   601   C  CE1 . HIS A  1 81  ? 65.151  50.013  11.099  1.00 2.00  ? 80  HIS A CE1 1 
ATOM   602   N  NE2 . HIS A  1 81  ? 65.565  50.024  9.883   1.00 2.00  ? 80  HIS A NE2 1 
ATOM   603   N  N   . VAL A  1 82  ? 61.063  45.830  8.099   1.00 6.67  ? 81  VAL A N   1 
ATOM   604   C  CA  . VAL A  1 82  ? 60.048  44.785  8.124   1.00 2.02  ? 81  VAL A CA  1 
ATOM   605   C  C   . VAL A  1 82  ? 59.721  44.453  9.553   1.00 2.00  ? 81  VAL A C   1 
ATOM   606   O  O   . VAL A  1 82  ? 58.565  44.220  9.896   1.00 2.80  ? 81  VAL A O   1 
ATOM   607   C  CB  . VAL A  1 82  ? 60.636  43.646  7.322   1.00 2.00  ? 81  VAL A CB  1 
ATOM   608   C  CG1 . VAL A  1 82  ? 59.794  42.384  7.319   1.00 4.97  ? 81  VAL A CG1 1 
ATOM   609   C  CG2 . VAL A  1 82  ? 60.731  44.182  5.897   1.00 4.27  ? 81  VAL A CG2 1 
ATOM   610   N  N   . GLY A  1 83  ? 60.686  44.512  10.455  1.00 2.00  ? 82  GLY A N   1 
ATOM   611   C  CA  . GLY A  1 83  ? 60.336  44.207  11.818  1.00 3.21  ? 82  GLY A CA  1 
ATOM   612   C  C   . GLY A  1 83  ? 59.665  45.339  12.555  1.00 4.15  ? 82  GLY A C   1 
ATOM   613   O  O   . GLY A  1 83  ? 59.452  45.195  13.764  1.00 7.72  ? 82  GLY A O   1 
ATOM   614   N  N   . ASP A  1 84  ? 59.339  46.489  11.956  1.00 3.75  ? 83  ASP A N   1 
ATOM   615   C  CA  . ASP A  1 84  ? 58.827  47.594  12.739  1.00 2.00  ? 83  ASP A CA  1 
ATOM   616   C  C   . ASP A  1 84  ? 57.370  47.406  12.988  1.00 2.00  ? 83  ASP A C   1 
ATOM   617   O  O   . ASP A  1 84  ? 56.560  47.701  12.125  1.00 3.03  ? 83  ASP A O   1 
ATOM   618   C  CB  . ASP A  1 84  ? 59.056  48.910  12.030  1.00 2.00  ? 83  ASP A CB  1 
ATOM   619   C  CG  . ASP A  1 84  ? 60.500  49.396  12.058  1.00 5.09  ? 83  ASP A CG  1 
ATOM   620   O  OD1 . ASP A  1 84  ? 61.304  49.084  12.926  1.00 2.08  ? 83  ASP A OD1 1 
ATOM   621   O  OD2 . ASP A  1 84  ? 60.857  50.143  11.186  1.00 9.45  ? 83  ASP A OD2 1 
ATOM   622   N  N   . LEU A  1 85  ? 57.014  46.875  14.148  1.00 3.52  ? 84  LEU A N   1 
ATOM   623   C  CA  . LEU A  1 85  ? 55.612  46.730  14.440  1.00 3.99  ? 84  LEU A CA  1 
ATOM   624   C  C   . LEU A  1 85  ? 55.048  47.808  15.360  1.00 5.86  ? 84  LEU A C   1 
ATOM   625   O  O   . LEU A  1 85  ? 53.921  47.682  15.838  1.00 10.87 ? 84  LEU A O   1 
ATOM   626   C  CB  . LEU A  1 85  ? 55.402  45.365  15.009  1.00 3.30  ? 84  LEU A CB  1 
ATOM   627   C  CG  . LEU A  1 85  ? 55.443  44.232  13.999  1.00 3.64  ? 84  LEU A CG  1 
ATOM   628   C  CD1 . LEU A  1 85  ? 55.348  42.953  14.798  1.00 2.76  ? 84  LEU A CD1 1 
ATOM   629   C  CD2 . LEU A  1 85  ? 54.304  44.292  12.987  1.00 2.00  ? 84  LEU A CD2 1 
ATOM   630   N  N   . GLY A  1 86  ? 55.740  48.916  15.636  1.00 3.69  ? 85  GLY A N   1 
ATOM   631   C  CA  . GLY A  1 86  ? 55.146  50.002  16.396  1.00 3.23  ? 85  GLY A CA  1 
ATOM   632   C  C   . GLY A  1 86  ? 55.280  49.864  17.907  1.00 3.53  ? 85  GLY A C   1 
ATOM   633   O  O   . GLY A  1 86  ? 56.344  49.470  18.417  1.00 2.00  ? 85  GLY A O   1 
ATOM   634   N  N   . ASN A  1 87  ? 54.190  50.183  18.620  1.00 2.98  ? 86  ASN A N   1 
ATOM   635   C  CA  . ASN A  1 87  ? 54.192  50.315  20.085  1.00 2.00  ? 86  ASN A CA  1 
ATOM   636   C  C   . ASN A  1 87  ? 53.046  49.570  20.676  1.00 4.03  ? 86  ASN A C   1 
ATOM   637   O  O   . ASN A  1 87  ? 51.974  49.594  20.071  1.00 7.97  ? 86  ASN A O   1 
ATOM   638   C  CB  . ASN A  1 87  ? 53.958  51.695  20.592  1.00 2.00  ? 86  ASN A CB  1 
ATOM   639   C  CG  . ASN A  1 87  ? 55.154  52.572  20.485  1.00 2.00  ? 86  ASN A CG  1 
ATOM   640   O  OD1 . ASN A  1 87  ? 56.256  52.204  20.865  1.00 2.00  ? 86  ASN A OD1 1 
ATOM   641   N  ND2 . ASN A  1 87  ? 54.979  53.779  20.000  1.00 2.00  ? 86  ASN A ND2 1 
ATOM   642   N  N   . VAL A  1 88  ? 53.174  48.889  21.790  1.00 4.50  ? 87  VAL A N   1 
ATOM   643   C  CA  . VAL A  1 88  ? 52.008  48.322  22.429  1.00 4.15  ? 87  VAL A CA  1 
ATOM   644   C  C   . VAL A  1 88  ? 51.737  49.320  23.540  1.00 6.54  ? 87  VAL A C   1 
ATOM   645   O  O   . VAL A  1 88  ? 52.631  50.117  23.872  1.00 5.04  ? 87  VAL A O   1 
ATOM   646   C  CB  . VAL A  1 88  ? 52.317  46.904  22.982  1.00 3.31  ? 87  VAL A CB  1 
ATOM   647   C  CG1 . VAL A  1 88  ? 52.223  46.024  21.790  1.00 2.00  ? 87  VAL A CG1 1 
ATOM   648   C  CG2 . VAL A  1 88  ? 53.722  46.676  23.551  1.00 2.00  ? 87  VAL A CG2 1 
ATOM   649   N  N   . THR A  1 89  ? 50.544  49.269  24.142  1.00 9.68  ? 88  THR A N   1 
ATOM   650   C  CA  . THR A  1 89  ? 50.146  50.147  25.227  1.00 8.54  ? 88  THR A CA  1 
ATOM   651   C  C   . THR A  1 89  ? 49.852  49.302  26.424  1.00 9.78  ? 88  THR A C   1 
ATOM   652   O  O   . THR A  1 89  ? 49.118  48.314  26.321  1.00 13.28 ? 88  THR A O   1 
ATOM   653   C  CB  . THR A  1 89  ? 48.903  50.906  24.874  1.00 9.10  ? 88  THR A CB  1 
ATOM   654   O  OG1 . THR A  1 89  ? 49.119  51.301  23.530  1.00 10.77 ? 88  THR A OG1 1 
ATOM   655   C  CG2 . THR A  1 89  ? 48.634  52.130  25.766  1.00 10.15 ? 88  THR A CG2 1 
ATOM   656   N  N   . ALA A  1 90  ? 50.476  49.713  27.517  1.00 9.18  ? 89  ALA A N   1 
ATOM   657   C  CA  . ALA A  1 90  ? 50.389  49.084  28.812  1.00 9.38  ? 89  ALA A CA  1 
ATOM   658   C  C   . ALA A  1 90  ? 49.386  49.857  29.666  1.00 10.29 ? 89  ALA A C   1 
ATOM   659   O  O   . ALA A  1 90  ? 49.432  51.089  29.736  1.00 10.07 ? 89  ALA A O   1 
ATOM   660   C  CB  . ALA A  1 90  ? 51.750  49.129  29.435  1.00 7.49  ? 89  ALA A CB  1 
ATOM   661   N  N   . ASP A  1 91  ? 48.418  49.181  30.275  1.00 11.74 ? 90  ASP A N   1 
ATOM   662   C  CA  . ASP A  1 91  ? 47.456  49.851  31.118  1.00 13.02 ? 90  ASP A CA  1 
ATOM   663   C  C   . ASP A  1 91  ? 47.979  50.101  32.507  1.00 14.54 ? 90  ASP A C   1 
ATOM   664   O  O   . ASP A  1 91  ? 49.144  49.850  32.769  1.00 14.59 ? 90  ASP A O   1 
ATOM   665   C  CB  . ASP A  1 91  ? 46.182  49.038  31.196  1.00 12.89 ? 90  ASP A CB  1 
ATOM   666   C  CG  . ASP A  1 91  ? 46.177  47.653  31.831  1.00 16.71 ? 90  ASP A CG  1 
ATOM   667   O  OD1 . ASP A  1 91  ? 47.183  47.181  32.382  1.00 16.43 ? 90  ASP A OD1 1 
ATOM   668   O  OD2 . ASP A  1 91  ? 45.102  47.050  31.765  1.00 19.49 ? 90  ASP A OD2 1 
ATOM   669   N  N   . LYS A  1 92  ? 47.185  50.544  33.469  1.00 18.23 ? 91  LYS A N   1 
ATOM   670   C  CA  . LYS A  1 92  ? 47.736  50.813  34.793  1.00 21.22 ? 91  LYS A CA  1 
ATOM   671   C  C   . LYS A  1 92  ? 48.138  49.584  35.583  1.00 19.36 ? 91  LYS A C   1 
ATOM   672   O  O   . LYS A  1 92  ? 48.945  49.695  36.491  1.00 19.01 ? 91  LYS A O   1 
ATOM   673   C  CB  . LYS A  1 92  ? 46.738  51.696  35.573  1.00 24.89 ? 91  LYS A CB  1 
ATOM   674   C  CG  . LYS A  1 92  ? 45.235  51.453  35.431  1.00 33.82 ? 91  LYS A CG  1 
ATOM   675   C  CD  . LYS A  1 92  ? 44.755  50.265  36.255  1.00 38.63 ? 91  LYS A CD  1 
ATOM   676   C  CE  . LYS A  1 92  ? 43.242  50.196  36.153  1.00 43.26 ? 91  LYS A CE  1 
ATOM   677   N  NZ  . LYS A  1 92  ? 42.700  49.393  37.239  1.00 46.65 ? 91  LYS A NZ  1 
ATOM   678   N  N   . ASP A  1 93  ? 47.641  48.400  35.225  1.00 17.85 ? 92  ASP A N   1 
ATOM   679   C  CA  . ASP A  1 93  ? 48.134  47.176  35.838  1.00 17.66 ? 92  ASP A CA  1 
ATOM   680   C  C   . ASP A  1 93  ? 49.405  46.684  35.140  1.00 16.18 ? 92  ASP A C   1 
ATOM   681   O  O   . ASP A  1 93  ? 50.036  45.727  35.580  1.00 15.35 ? 92  ASP A O   1 
ATOM   682   C  CB  . ASP A  1 93  ? 47.075  46.098  35.765  1.00 21.33 ? 92  ASP A CB  1 
ATOM   683   C  CG  . ASP A  1 93  ? 45.811  46.519  36.494  1.00 27.22 ? 92  ASP A CG  1 
ATOM   684   O  OD1 . ASP A  1 93  ? 45.885  46.790  37.698  1.00 32.00 ? 92  ASP A OD1 1 
ATOM   685   O  OD2 . ASP A  1 93  ? 44.760  46.601  35.852  1.00 30.58 ? 92  ASP A OD2 1 
ATOM   686   N  N   . GLY A  1 94  ? 49.783  47.309  34.017  1.00 14.23 ? 93  GLY A N   1 
ATOM   687   C  CA  . GLY A  1 94  ? 50.952  46.941  33.244  1.00 12.68 ? 93  GLY A CA  1 
ATOM   688   C  C   . GLY A  1 94  ? 50.787  45.690  32.373  1.00 12.78 ? 93  GLY A C   1 
ATOM   689   O  O   . GLY A  1 94  ? 51.753  44.930  32.180  1.00 14.71 ? 93  GLY A O   1 
ATOM   690   N  N   . VAL A  1 95  ? 49.566  45.411  31.923  1.00 9.60  ? 94  VAL A N   1 
ATOM   691   C  CA  . VAL A  1 95  ? 49.287  44.356  30.976  1.00 9.82  ? 94  VAL A CA  1 
ATOM   692   C  C   . VAL A  1 95  ? 49.062  45.063  29.635  1.00 9.83  ? 94  VAL A C   1 
ATOM   693   O  O   . VAL A  1 95  ? 48.248  46.001  29.569  1.00 8.81  ? 94  VAL A O   1 
ATOM   694   C  CB  . VAL A  1 95  ? 47.987  43.537  31.337  1.00 9.75  ? 94  VAL A CB  1 
ATOM   695   C  CG1 . VAL A  1 95  ? 47.768  42.405  30.310  1.00 8.52  ? 94  VAL A CG1 1 
ATOM   696   C  CG2 . VAL A  1 95  ? 48.136  42.827  32.679  1.00 7.92  ? 94  VAL A CG2 1 
ATOM   697   N  N   . ALA A  1 96  ? 49.782  44.682  28.572  1.00 10.36 ? 95  ALA A N   1 
ATOM   698   C  CA  . ALA A  1 96  ? 49.508  45.229  27.238  1.00 11.62 ? 95  ALA A CA  1 
ATOM   699   C  C   . ALA A  1 96  ? 48.887  44.133  26.395  1.00 12.82 ? 95  ALA A C   1 
ATOM   700   O  O   . ALA A  1 96  ? 49.497  43.073  26.236  1.00 13.72 ? 95  ALA A O   1 
ATOM   701   C  CB  . ALA A  1 96  ? 50.776  45.686  26.512  1.00 9.28  ? 95  ALA A CB  1 
ATOM   702   N  N   . ASP A  1 97  ? 47.669  44.323  25.887  1.00 14.77 ? 96  ASP A N   1 
ATOM   703   C  CA  . ASP A  1 97  ? 47.026  43.379  24.960  1.00 14.72 ? 96  ASP A CA  1 
ATOM   704   C  C   . ASP A  1 97  ? 47.359  43.771  23.519  1.00 13.12 ? 96  ASP A C   1 
ATOM   705   O  O   . ASP A  1 97  ? 47.316  44.972  23.222  1.00 12.54 ? 96  ASP A O   1 
ATOM   706   C  CB  . ASP A  1 97  ? 45.512  43.397  25.140  1.00 18.99 ? 96  ASP A CB  1 
ATOM   707   C  CG  . ASP A  1 97  ? 45.065  42.335  26.136  1.00 25.65 ? 96  ASP A CG  1 
ATOM   708   O  OD1 . ASP A  1 97  ? 45.043  42.613  27.361  1.00 27.76 ? 96  ASP A OD1 1 
ATOM   709   O  OD2 . ASP A  1 97  ? 44.764  41.225  25.657  1.00 26.31 ? 96  ASP A OD2 1 
ATOM   710   N  N   . VAL A  1 98  ? 47.641  42.865  22.581  1.00 9.46  ? 97  VAL A N   1 
ATOM   711   C  CA  . VAL A  1 98  ? 48.100  43.283  21.266  1.00 9.08  ? 97  VAL A CA  1 
ATOM   712   C  C   . VAL A  1 98  ? 47.093  42.754  20.267  1.00 11.55 ? 97  VAL A C   1 
ATOM   713   O  O   . VAL A  1 98  ? 46.660  41.608  20.440  1.00 11.82 ? 97  VAL A O   1 
ATOM   714   C  CB  . VAL A  1 98  ? 49.483  42.683  20.912  1.00 5.42  ? 97  VAL A CB  1 
ATOM   715   C  CG1 . VAL A  1 98  ? 50.022  43.309  19.683  1.00 2.39  ? 97  VAL A CG1 1 
ATOM   716   C  CG2 . VAL A  1 98  ? 50.507  42.998  21.946  1.00 5.61  ? 97  VAL A CG2 1 
ATOM   717   N  N   . SER A  1 99  ? 46.645  43.599  19.317  1.00 12.91 ? 98  SER A N   1 
ATOM   718   C  CA  . SER A  1 99  ? 45.933  43.215  18.082  1.00 12.60 ? 98  SER A CA  1 
ATOM   719   C  C   . SER A  1 99  ? 46.599  44.036  16.945  1.00 14.64 ? 98  SER A C   1 
ATOM   720   O  O   . SER A  1 99  ? 46.616  45.272  16.973  1.00 15.05 ? 98  SER A O   1 
ATOM   721   C  CB  . SER A  1 99  ? 44.472  43.569  18.101  1.00 9.28  ? 98  SER A CB  1 
ATOM   722   O  OG  . SER A  1 99  ? 43.752  42.549  18.758  1.00 10.08 ? 98  SER A OG  1 
ATOM   723   N  N   . ILE A  1 100 ? 47.263  43.421  15.969  1.00 13.51 ? 99  ILE A N   1 
ATOM   724   C  CA  . ILE A  1 100 ? 47.999  44.113  14.908  1.00 14.11 ? 99  ILE A CA  1 
ATOM   725   C  C   . ILE A  1 100 ? 47.628  43.220  13.736  1.00 13.07 ? 99  ILE A C   1 
ATOM   726   O  O   . ILE A  1 100 ? 47.402  42.026  13.914  1.00 14.22 ? 99  ILE A O   1 
ATOM   727   C  CB  . ILE A  1 100 ? 49.556  44.071  15.145  1.00 15.26 ? 99  ILE A CB  1 
ATOM   728   C  CG1 . ILE A  1 100 ? 49.920  45.021  16.234  1.00 14.78 ? 99  ILE A CG1 1 
ATOM   729   C  CG2 . ILE A  1 100 ? 50.334  44.394  13.878  1.00 14.21 ? 99  ILE A CG2 1 
ATOM   730   C  CD1 . ILE A  1 100 ? 51.454  45.026  16.494  1.00 17.46 ? 99  ILE A CD1 1 
ATOM   731   N  N   . GLU A  1 101 ? 47.465  43.784  12.561  1.00 11.59 ? 100 GLU A N   1 
ATOM   732   C  CA  . GLU A  1 101 ? 47.242  43.072  11.312  1.00 9.69  ? 100 GLU A CA  1 
ATOM   733   C  C   . GLU A  1 101 ? 48.352  43.830  10.609  1.00 6.75  ? 100 GLU A C   1 
ATOM   734   O  O   . GLU A  1 101 ? 48.524  45.047  10.805  1.00 7.26  ? 100 GLU A O   1 
ATOM   735   C  CB  . GLU A  1 101 ? 45.820  43.379  10.732  1.00 11.92 ? 100 GLU A CB  1 
ATOM   736   C  CG  . GLU A  1 101 ? 45.249  42.647  9.480   1.00 16.73 ? 100 GLU A CG  1 
ATOM   737   C  CD  . GLU A  1 101 ? 44.758  43.568  8.343   1.00 21.56 ? 100 GLU A CD  1 
ATOM   738   O  OE1 . GLU A  1 101 ? 43.640  44.086  8.425   1.00 24.98 ? 100 GLU A OE1 1 
ATOM   739   O  OE2 . GLU A  1 101 ? 45.495  43.799  7.369   1.00 23.59 ? 100 GLU A OE2 1 
ATOM   740   N  N   . ASP A  1 102 ? 49.180  43.143  9.858   1.00 6.61  ? 101 ASP A N   1 
ATOM   741   C  CA  . ASP A  1 102 ? 50.292  43.779  9.195   1.00 6.01  ? 101 ASP A CA  1 
ATOM   742   C  C   . ASP A  1 102 ? 50.487  43.160  7.839   1.00 7.88  ? 101 ASP A C   1 
ATOM   743   O  O   . ASP A  1 102 ? 50.264  41.956  7.655   1.00 10.69 ? 101 ASP A O   1 
ATOM   744   C  CB  . ASP A  1 102 ? 51.513  43.588  10.018  1.00 5.17  ? 101 ASP A CB  1 
ATOM   745   C  CG  . ASP A  1 102 ? 52.601  44.500  9.558   1.00 5.09  ? 101 ASP A CG  1 
ATOM   746   O  OD1 . ASP A  1 102 ? 52.433  45.706  9.678   1.00 7.02  ? 101 ASP A OD1 1 
ATOM   747   O  OD2 . ASP A  1 102 ? 53.600  43.996  9.074   1.00 6.44  ? 101 ASP A OD2 1 
ATOM   748   N  N   . SER A  1 103 ? 50.971  43.957  6.902   1.00 8.91  ? 102 SER A N   1 
ATOM   749   C  CA  . SER A  1 103 ? 51.088  43.463  5.555   1.00 9.46  ? 102 SER A CA  1 
ATOM   750   C  C   . SER A  1 103 ? 52.510  43.401  5.045   1.00 8.96  ? 102 SER A C   1 
ATOM   751   O  O   . SER A  1 103 ? 52.753  43.231  3.852   1.00 10.75 ? 102 SER A O   1 
ATOM   752   C  CB  . SER A  1 103 ? 50.235  44.362  4.691   1.00 10.73 ? 102 SER A CB  1 
ATOM   753   O  OG  . SER A  1 103 ? 48.867  44.277  5.079   1.00 17.25 ? 102 SER A OG  1 
ATOM   754   N  N   . VAL A  1 104 ? 53.488  43.597  5.923   1.00 7.40  ? 103 VAL A N   1 
ATOM   755   C  CA  . VAL A  1 104 ? 54.882  43.680  5.493   1.00 4.83  ? 103 VAL A CA  1 
ATOM   756   C  C   . VAL A  1 104 ? 55.654  42.527  6.077   1.00 4.06  ? 103 VAL A C   1 
ATOM   757   O  O   . VAL A  1 104 ? 56.439  41.895  5.376   1.00 10.13 ? 103 VAL A O   1 
ATOM   758   C  CB  . VAL A  1 104 ? 55.430  45.033  5.923   1.00 2.00  ? 103 VAL A CB  1 
ATOM   759   C  CG1 . VAL A  1 104 ? 56.836  45.284  5.573   1.00 2.00  ? 103 VAL A CG1 1 
ATOM   760   C  CG2 . VAL A  1 104 ? 54.726  46.029  5.094   1.00 2.00  ? 103 VAL A CG2 1 
ATOM   761   N  N   . ILE A  1 105 ? 55.418  42.183  7.316   1.00 2.30  ? 104 ILE A N   1 
ATOM   762   C  CA  . ILE A  1 105 ? 56.009  40.992  7.880   1.00 2.63  ? 104 ILE A CA  1 
ATOM   763   C  C   . ILE A  1 105 ? 55.309  39.824  7.215   1.00 2.24  ? 104 ILE A C   1 
ATOM   764   O  O   . ILE A  1 105 ? 54.272  40.000  6.585   1.00 2.00  ? 104 ILE A O   1 
ATOM   765   C  CB  . ILE A  1 105 ? 55.788  40.934  9.424   1.00 2.89  ? 104 ILE A CB  1 
ATOM   766   C  CG1 . ILE A  1 105 ? 54.294  40.945  9.770   1.00 2.63  ? 104 ILE A CG1 1 
ATOM   767   C  CG2 . ILE A  1 105 ? 56.561  42.099  10.036  1.00 2.00  ? 104 ILE A CG2 1 
ATOM   768   C  CD1 . ILE A  1 105 ? 53.872  40.604  11.195  1.00 5.39  ? 104 ILE A CD1 1 
ATOM   769   N  N   . SER A  1 106 ? 55.830  38.619  7.348   1.00 3.72  ? 105 SER A N   1 
ATOM   770   C  CA  . SER A  1 106 ? 55.121  37.481  6.794   1.00 4.69  ? 105 SER A CA  1 
ATOM   771   C  C   . SER A  1 106 ? 55.518  36.240  7.611   1.00 3.61  ? 105 SER A C   1 
ATOM   772   O  O   . SER A  1 106 ? 56.371  36.332  8.510   1.00 2.71  ? 105 SER A O   1 
ATOM   773   C  CB  . SER A  1 106 ? 55.507  37.355  5.302   1.00 2.00  ? 105 SER A CB  1 
ATOM   774   O  OG  . SER A  1 106 ? 54.807  36.300  4.664   1.00 3.06  ? 105 SER A OG  1 
ATOM   775   N  N   . LEU A  1 107 ? 54.896  35.108  7.330   1.00 2.00  ? 106 LEU A N   1 
ATOM   776   C  CA  . LEU A  1 107 ? 55.323  33.864  7.902   1.00 2.38  ? 106 LEU A CA  1 
ATOM   777   C  C   . LEU A  1 107 ? 55.911  32.989  6.793   1.00 3.51  ? 106 LEU A C   1 
ATOM   778   O  O   . LEU A  1 107 ? 56.299  31.846  7.002   1.00 2.76  ? 106 LEU A O   1 
ATOM   779   C  CB  . LEU A  1 107 ? 54.143  33.156  8.597   1.00 2.76  ? 106 LEU A CB  1 
ATOM   780   C  CG  . LEU A  1 107 ? 53.395  33.968  9.652   1.00 2.00  ? 106 LEU A CG  1 
ATOM   781   C  CD1 . LEU A  1 107 ? 52.494  33.073  10.415  1.00 2.00  ? 106 LEU A CD1 1 
ATOM   782   C  CD2 . LEU A  1 107 ? 54.378  34.635  10.597  1.00 2.61  ? 106 LEU A CD2 1 
ATOM   783   N  N   . SER A  1 108 ? 56.064  33.493  5.574   1.00 5.58  ? 107 SER A N   1 
ATOM   784   C  CA  . SER A  1 108 ? 56.700  32.738  4.510   1.00 8.00  ? 107 SER A CA  1 
ATOM   785   C  C   . SER A  1 108 ? 57.512  33.655  3.638   1.00 8.87  ? 107 SER A C   1 
ATOM   786   O  O   . SER A  1 108 ? 57.178  34.848  3.622   1.00 8.89  ? 107 SER A O   1 
ATOM   787   C  CB  . SER A  1 108 ? 55.652  32.037  3.660   1.00 10.84 ? 107 SER A CB  1 
ATOM   788   O  OG  . SER A  1 108 ? 54.413  32.703  3.398   1.00 19.10 ? 107 SER A OG  1 
ATOM   789   N  N   . GLY A  1 109 ? 58.564  33.173  2.969   1.00 9.04  ? 108 GLY A N   1 
ATOM   790   C  CA  . GLY A  1 109 ? 59.344  33.960  2.024   1.00 16.18 ? 108 GLY A CA  1 
ATOM   791   C  C   . GLY A  1 109 ? 60.376  34.916  2.634   1.00 22.13 ? 108 GLY A C   1 
ATOM   792   O  O   . GLY A  1 109 ? 60.637  34.875  3.836   1.00 24.16 ? 108 GLY A O   1 
ATOM   793   N  N   . ASP A  1 110 ? 60.989  35.836  1.859   1.00 26.27 ? 109 ASP A N   1 
ATOM   794   C  CA  . ASP A  1 110 ? 62.058  36.756  2.317   1.00 28.72 ? 109 ASP A CA  1 
ATOM   795   C  C   . ASP A  1 110 ? 61.673  37.558  3.546   1.00 26.97 ? 109 ASP A C   1 
ATOM   796   O  O   . ASP A  1 110 ? 62.487  37.917  4.387   1.00 30.76 ? 109 ASP A O   1 
ATOM   797   C  CB  . ASP A  1 110 ? 62.452  37.756  1.177   1.00 34.85 ? 109 ASP A CB  1 
ATOM   798   C  CG  . ASP A  1 110 ? 63.270  39.023  1.540   1.00 39.60 ? 109 ASP A CG  1 
ATOM   799   O  OD1 . ASP A  1 110 ? 64.445  38.893  1.910   1.00 42.97 ? 109 ASP A OD1 1 
ATOM   800   O  OD2 . ASP A  1 110 ? 62.738  40.142  1.440   1.00 40.98 ? 109 ASP A OD2 1 
ATOM   801   N  N   . HIS A  1 111 ? 60.396  37.847  3.647   1.00 23.26 ? 110 HIS A N   1 
ATOM   802   C  CA  . HIS A  1 111 ? 59.919  38.659  4.720   1.00 18.13 ? 110 HIS A CA  1 
ATOM   803   C  C   . HIS A  1 111 ? 59.566  37.820  5.922   1.00 13.29 ? 110 HIS A C   1 
ATOM   804   O  O   . HIS A  1 111 ? 58.971  38.419  6.829   1.00 14.50 ? 110 HIS A O   1 
ATOM   805   C  CB  . HIS A  1 111 ? 58.696  39.460  4.197   1.00 20.70 ? 110 HIS A CB  1 
ATOM   806   C  CG  . HIS A  1 111 ? 59.059  40.784  3.550   1.00 20.94 ? 110 HIS A CG  1 
ATOM   807   N  ND1 . HIS A  1 111 ? 58.284  41.856  3.463   1.00 23.17 ? 110 HIS A ND1 1 
ATOM   808   C  CD2 . HIS A  1 111 ? 60.288  41.113  3.029   1.00 20.59 ? 110 HIS A CD2 1 
ATOM   809   C  CE1 . HIS A  1 111 ? 58.978  42.823  2.934   1.00 23.78 ? 110 HIS A CE1 1 
ATOM   810   N  NE2 . HIS A  1 111 ? 60.188  42.363  2.673   1.00 23.51 ? 110 HIS A NE2 1 
ATOM   811   N  N   . SER A  1 112 ? 59.893  36.513  5.956   1.00 5.71  ? 111 SER A N   1 
ATOM   812   C  CA  . SER A  1 112 ? 59.428  35.636  7.011   1.00 2.00  ? 111 SER A CA  1 
ATOM   813   C  C   . SER A  1 112 ? 59.942  36.005  8.379   1.00 2.00  ? 111 SER A C   1 
ATOM   814   O  O   . SER A  1 112 ? 61.146  36.133  8.566   1.00 2.00  ? 111 SER A O   1 
ATOM   815   C  CB  . SER A  1 112 ? 59.839  34.229  6.714   1.00 3.26  ? 111 SER A CB  1 
ATOM   816   O  OG  . SER A  1 112 ? 59.477  33.204  7.641   1.00 2.00  ? 111 SER A OG  1 
ATOM   817   N  N   . ILE A  1 113 ? 59.080  36.202  9.378   1.00 2.00  ? 112 ILE A N   1 
ATOM   818   C  CA  . ILE A  1 113 ? 59.628  36.524  10.679  1.00 2.10  ? 112 ILE A CA  1 
ATOM   819   C  C   . ILE A  1 113 ? 59.863  35.258  11.465  1.00 2.92  ? 112 ILE A C   1 
ATOM   820   O  O   . ILE A  1 113 ? 60.281  35.386  12.609  1.00 2.16  ? 112 ILE A O   1 
ATOM   821   C  CB  . ILE A  1 113 ? 58.716  37.448  11.479  1.00 2.00  ? 112 ILE A CB  1 
ATOM   822   C  CG1 . ILE A  1 113 ? 57.344  36.863  11.697  1.00 2.00  ? 112 ILE A CG1 1 
ATOM   823   C  CG2 . ILE A  1 113 ? 58.740  38.773  10.745  1.00 2.00  ? 112 ILE A CG2 1 
ATOM   824   C  CD1 . ILE A  1 113 ? 56.444  37.815  12.487  1.00 2.00  ? 112 ILE A CD1 1 
ATOM   825   N  N   . ILE A  1 114 ? 59.636  34.048  10.896  1.00 2.00  ? 113 ILE A N   1 
ATOM   826   C  CA  . ILE A  1 114 ? 59.826  32.795  11.603  1.00 2.41  ? 113 ILE A CA  1 
ATOM   827   C  C   . ILE A  1 114 ? 61.317  32.582  11.800  1.00 2.31  ? 113 ILE A C   1 
ATOM   828   O  O   . ILE A  1 114 ? 62.110  32.711  10.857  1.00 2.34  ? 113 ILE A O   1 
ATOM   829   C  CB  . ILE A  1 114 ? 59.209  31.590  10.799  1.00 3.40  ? 113 ILE A CB  1 
ATOM   830   C  CG1 . ILE A  1 114 ? 57.711  31.807  10.550  1.00 2.00  ? 113 ILE A CG1 1 
ATOM   831   C  CG2 . ILE A  1 114 ? 59.521  30.304  11.522  1.00 2.00  ? 113 ILE A CG2 1 
ATOM   832   C  CD1 . ILE A  1 114 ? 56.720  31.200  11.502  1.00 2.00  ? 113 ILE A CD1 1 
ATOM   833   N  N   . GLY A  1 115 ? 61.688  32.275  13.055  1.00 2.88  ? 114 GLY A N   1 
ATOM   834   C  CA  . GLY A  1 115 ? 63.069  32.062  13.452  1.00 2.00  ? 114 GLY A CA  1 
ATOM   835   C  C   . GLY A  1 115 ? 63.794  33.313  13.863  1.00 2.00  ? 114 GLY A C   1 
ATOM   836   O  O   . GLY A  1 115 ? 64.962  33.260  14.181  1.00 2.00  ? 114 GLY A O   1 
ATOM   837   N  N   . ARG A  1 116 ? 63.171  34.469  13.842  1.00 2.00  ? 115 ARG A N   1 
ATOM   838   C  CA  . ARG A  1 116 ? 63.738  35.716  14.296  1.00 2.00  ? 115 ARG A CA  1 
ATOM   839   C  C   . ARG A  1 116 ? 63.217  36.075  15.700  1.00 2.00  ? 115 ARG A C   1 
ATOM   840   O  O   . ARG A  1 116 ? 62.410  35.328  16.283  1.00 2.00  ? 115 ARG A O   1 
ATOM   841   C  CB  . ARG A  1 116 ? 63.386  36.736  13.235  1.00 2.00  ? 115 ARG A CB  1 
ATOM   842   C  CG  . ARG A  1 116 ? 63.989  36.300  11.944  1.00 2.00  ? 115 ARG A CG  1 
ATOM   843   C  CD  . ARG A  1 116 ? 63.944  37.405  10.992  1.00 2.27  ? 115 ARG A CD  1 
ATOM   844   N  NE  . ARG A  1 116 ? 64.007  36.822  9.672   1.00 4.16  ? 115 ARG A NE  1 
ATOM   845   C  CZ  . ARG A  1 116 ? 65.138  36.717  8.973   1.00 2.27  ? 115 ARG A CZ  1 
ATOM   846   N  NH1 . ARG A  1 116 ? 66.327  37.121  9.385   1.00 6.10  ? 115 ARG A NH1 1 
ATOM   847   N  NH2 . ARG A  1 116 ? 65.070  36.190  7.791   1.00 2.00  ? 115 ARG A NH2 1 
ATOM   848   N  N   . THR A  1 117 ? 63.631  37.205  16.287  1.00 2.57  ? 116 THR A N   1 
ATOM   849   C  CA  . THR A  1 117 ? 63.317  37.517  17.695  1.00 3.77  ? 116 THR A CA  1 
ATOM   850   C  C   . THR A  1 117 ? 62.310  38.636  17.857  1.00 2.53  ? 116 THR A C   1 
ATOM   851   O  O   . THR A  1 117 ? 62.533  39.688  17.275  1.00 4.00  ? 116 THR A O   1 
ATOM   852   C  CB  . THR A  1 117 ? 64.632  37.882  18.463  1.00 2.00  ? 116 THR A CB  1 
ATOM   853   O  OG1 . THR A  1 117 ? 65.360  36.662  18.607  1.00 2.00  ? 116 THR A OG1 1 
ATOM   854   C  CG2 . THR A  1 117 ? 64.427  38.463  19.829  1.00 2.00  ? 116 THR A CG2 1 
ATOM   855   N  N   . LEU A  1 118 ? 61.211  38.452  18.575  1.00 2.00  ? 117 LEU A N   1 
ATOM   856   C  CA  . LEU A  1 118 ? 60.270  39.514  18.809  1.00 2.65  ? 117 LEU A CA  1 
ATOM   857   C  C   . LEU A  1 118 ? 60.750  40.223  20.059  1.00 3.85  ? 117 LEU A C   1 
ATOM   858   O  O   . LEU A  1 118 ? 61.129  39.500  20.993  1.00 6.45  ? 117 LEU A O   1 
ATOM   859   C  CB  . LEU A  1 118 ? 58.929  38.897  18.998  1.00 3.76  ? 117 LEU A CB  1 
ATOM   860   C  CG  . LEU A  1 118 ? 57.728  39.793  19.134  1.00 4.42  ? 117 LEU A CG  1 
ATOM   861   C  CD1 . LEU A  1 118 ? 57.573  40.765  17.985  1.00 2.00  ? 117 LEU A CD1 1 
ATOM   862   C  CD2 . LEU A  1 118 ? 56.558  38.842  19.252  1.00 3.98  ? 117 LEU A CD2 1 
ATOM   863   N  N   . VAL A  1 119 ? 60.828  41.550  20.123  1.00 2.00  ? 118 VAL A N   1 
ATOM   864   C  CA  . VAL A  1 119 ? 61.369  42.251  21.274  1.00 2.46  ? 118 VAL A CA  1 
ATOM   865   C  C   . VAL A  1 119 ? 60.323  43.271  21.710  1.00 2.90  ? 118 VAL A C   1 
ATOM   866   O  O   . VAL A  1 119 ? 59.676  43.830  20.812  1.00 2.00  ? 118 VAL A O   1 
ATOM   867   C  CB  . VAL A  1 119 ? 62.710  42.965  20.898  1.00 5.09  ? 118 VAL A CB  1 
ATOM   868   C  CG1 . VAL A  1 119 ? 63.211  43.834  22.043  1.00 2.00  ? 118 VAL A CG1 1 
ATOM   869   C  CG2 . VAL A  1 119 ? 63.817  41.907  20.631  1.00 3.45  ? 118 VAL A CG2 1 
ATOM   870   N  N   . VAL A  1 120 ? 60.024  43.333  23.045  1.00 2.49  ? 119 VAL A N   1 
ATOM   871   C  CA  . VAL A  1 120 ? 59.233  44.401  23.615  1.00 3.37  ? 119 VAL A CA  1 
ATOM   872   C  C   . VAL A  1 120 ? 60.261  45.242  24.350  1.00 3.17  ? 119 VAL A C   1 
ATOM   873   O  O   . VAL A  1 120 ? 61.175  44.789  25.058  1.00 2.00  ? 119 VAL A O   1 
ATOM   874   C  CB  . VAL A  1 120 ? 58.106  43.932  24.606  1.00 4.86  ? 119 VAL A CB  1 
ATOM   875   C  CG1 . VAL A  1 120 ? 58.593  43.333  25.904  1.00 5.53  ? 119 VAL A CG1 1 
ATOM   876   C  CG2 . VAL A  1 120 ? 57.331  45.194  25.007  1.00 4.15  ? 119 VAL A CG2 1 
ATOM   877   N  N   . HIS A  1 121 ? 60.144  46.525  24.081  1.00 5.13  ? 120 HIS A N   1 
ATOM   878   C  CA  . HIS A  1 121 ? 61.077  47.528  24.596  1.00 6.15  ? 120 HIS A CA  1 
ATOM   879   C  C   . HIS A  1 121 ? 60.652  48.310  25.826  1.00 6.09  ? 120 HIS A C   1 
ATOM   880   O  O   . HIS A  1 121 ? 59.490  48.423  26.234  1.00 7.31  ? 120 HIS A O   1 
ATOM   881   C  CB  . HIS A  1 121 ? 61.428  48.537  23.485  1.00 4.97  ? 120 HIS A CB  1 
ATOM   882   C  CG  . HIS A  1 121 ? 62.406  47.987  22.447  1.00 5.20  ? 120 HIS A CG  1 
ATOM   883   N  ND1 . HIS A  1 121 ? 63.730  47.912  22.472  1.00 2.85  ? 120 HIS A ND1 1 
ATOM   884   C  CD2 . HIS A  1 121 ? 62.001  47.478  21.235  1.00 6.20  ? 120 HIS A CD2 1 
ATOM   885   C  CE1 . HIS A  1 121 ? 64.095  47.383  21.320  1.00 3.62  ? 120 HIS A CE1 1 
ATOM   886   N  NE2 . HIS A  1 121 ? 63.051  47.119  20.555  1.00 9.52  ? 120 HIS A NE2 1 
ATOM   887   N  N   . GLU A  1 122 ? 61.674  48.846  26.439  1.00 8.58  ? 121 GLU A N   1 
ATOM   888   C  CA  . GLU A  1 122 ? 61.554  49.682  27.595  1.00 12.07 ? 121 GLU A CA  1 
ATOM   889   C  C   . GLU A  1 122 ? 60.760  50.902  27.238  1.00 11.90 ? 121 GLU A C   1 
ATOM   890   O  O   . GLU A  1 122 ? 59.664  51.054  27.753  1.00 14.18 ? 121 GLU A O   1 
ATOM   891   C  CB  . GLU A  1 122 ? 62.923  50.079  28.056  1.00 16.98 ? 121 GLU A CB  1 
ATOM   892   C  CG  . GLU A  1 122 ? 62.938  51.084  29.195  1.00 24.33 ? 121 GLU A CG  1 
ATOM   893   C  CD  . GLU A  1 122 ? 64.345  51.362  29.704  1.00 28.66 ? 121 GLU A CD  1 
ATOM   894   O  OE1 . GLU A  1 122 ? 64.779  50.632  30.613  1.00 32.12 ? 121 GLU A OE1 1 
ATOM   895   O  OE2 . GLU A  1 122 ? 64.985  52.293  29.191  1.00 28.56 ? 121 GLU A OE2 1 
ATOM   896   N  N   . LYS A  1 123 ? 61.209  51.734  26.318  1.00 13.77 ? 122 LYS A N   1 
ATOM   897   C  CA  . LYS A  1 123 ? 60.533  52.995  26.029  1.00 12.17 ? 122 LYS A CA  1 
ATOM   898   C  C   . LYS A  1 123 ? 59.742  52.844  24.736  1.00 11.46 ? 122 LYS A C   1 
ATOM   899   O  O   . LYS A  1 123 ? 59.725  51.783  24.110  1.00 11.09 ? 122 LYS A O   1 
ATOM   900   C  CB  . LYS A  1 123 ? 61.558  54.083  25.870  1.00 14.61 ? 122 LYS A CB  1 
ATOM   901   C  CG  . LYS A  1 123 ? 62.505  54.305  27.017  1.00 18.04 ? 122 LYS A CG  1 
ATOM   902   C  CD  . LYS A  1 123 ? 63.534  55.265  26.489  1.00 23.44 ? 122 LYS A CD  1 
ATOM   903   C  CE  . LYS A  1 123 ? 64.536  55.528  27.593  1.00 28.73 ? 122 LYS A CE  1 
ATOM   904   N  NZ  . LYS A  1 123 ? 65.294  56.736  27.288  1.00 32.85 ? 122 LYS A NZ  1 
ATOM   905   N  N   . ALA A  1 124 ? 59.077  53.911  24.351  1.00 9.07  ? 123 ALA A N   1 
ATOM   906   C  CA  . ALA A  1 124 ? 58.259  53.950  23.180  1.00 9.64  ? 123 ALA A CA  1 
ATOM   907   C  C   . ALA A  1 124 ? 59.064  54.251  21.951  1.00 9.98  ? 123 ALA A C   1 
ATOM   908   O  O   . ALA A  1 124 ? 60.082  54.938  21.991  1.00 11.81 ? 123 ALA A O   1 
ATOM   909   C  CB  . ALA A  1 124 ? 57.236  55.032  23.292  1.00 13.02 ? 123 ALA A CB  1 
ATOM   910   N  N   . ASP A  1 125 ? 58.539  53.835  20.826  1.00 9.27  ? 124 ASP A N   1 
ATOM   911   C  CA  . ASP A  1 125 ? 59.208  54.004  19.570  1.00 9.30  ? 124 ASP A CA  1 
ATOM   912   C  C   . ASP A  1 125 ? 58.736  55.329  19.069  1.00 10.05 ? 124 ASP A C   1 
ATOM   913   O  O   . ASP A  1 125 ? 57.536  55.531  18.879  1.00 10.23 ? 124 ASP A O   1 
ATOM   914   C  CB  . ASP A  1 125 ? 58.786  52.884  18.624  1.00 11.12 ? 124 ASP A CB  1 
ATOM   915   C  CG  . ASP A  1 125 ? 59.422  52.827  17.252  1.00 12.50 ? 124 ASP A CG  1 
ATOM   916   O  OD1 . ASP A  1 125 ? 60.063  53.786  16.861  1.00 13.69 ? 124 ASP A OD1 1 
ATOM   917   O  OD2 . ASP A  1 125 ? 59.251  51.829  16.546  1.00 16.16 ? 124 ASP A OD2 1 
ATOM   918   N  N   . ASP A  1 126 ? 59.651  56.221  18.741  1.00 9.84  ? 125 ASP A N   1 
ATOM   919   C  CA  . ASP A  1 126 ? 59.261  57.469  18.167  1.00 10.93 ? 125 ASP A CA  1 
ATOM   920   C  C   . ASP A  1 126 ? 58.893  57.310  16.689  1.00 11.78 ? 125 ASP A C   1 
ATOM   921   O  O   . ASP A  1 126 ? 58.963  58.268  15.917  1.00 13.37 ? 125 ASP A O   1 
ATOM   922   C  CB  . ASP A  1 126 ? 60.409  58.447  18.385  1.00 11.39 ? 125 ASP A CB  1 
ATOM   923   C  CG  . ASP A  1 126 ? 61.709  58.208  17.626  1.00 17.28 ? 125 ASP A CG  1 
ATOM   924   O  OD1 . ASP A  1 126 ? 61.680  57.958  16.424  1.00 18.19 ? 125 ASP A OD1 1 
ATOM   925   O  OD2 . ASP A  1 126 ? 62.773  58.296  18.231  1.00 15.86 ? 125 ASP A OD2 1 
ATOM   926   N  N   . LEU A  1 127 ? 58.542  56.105  16.221  1.00 10.28 ? 126 LEU A N   1 
ATOM   927   C  CA  . LEU A  1 127 ? 58.221  55.776  14.841  1.00 9.26  ? 126 LEU A CA  1 
ATOM   928   C  C   . LEU A  1 127 ? 59.123  56.350  13.773  1.00 9.88  ? 126 LEU A C   1 
ATOM   929   O  O   . LEU A  1 127 ? 58.728  56.611  12.636  1.00 8.28  ? 126 LEU A O   1 
ATOM   930   C  CB  . LEU A  1 127 ? 56.791  56.179  14.521  1.00 6.11  ? 126 LEU A CB  1 
ATOM   931   C  CG  . LEU A  1 127 ? 55.711  55.712  15.468  1.00 6.02  ? 126 LEU A CG  1 
ATOM   932   C  CD1 . LEU A  1 127 ? 54.393  55.964  14.792  1.00 6.97  ? 126 LEU A CD1 1 
ATOM   933   C  CD2 . LEU A  1 127 ? 55.858  54.229  15.824  1.00 3.37  ? 126 LEU A CD2 1 
ATOM   934   N  N   . GLY A  1 128 ? 60.372  56.590  14.133  1.00 10.91 ? 127 GLY A N   1 
ATOM   935   C  CA  . GLY A  1 128 ? 61.348  56.961  13.127  1.00 15.47 ? 127 GLY A CA  1 
ATOM   936   C  C   . GLY A  1 128 ? 61.283  58.420  12.755  1.00 18.87 ? 127 GLY A C   1 
ATOM   937   O  O   . GLY A  1 128 ? 62.299  58.998  12.345  1.00 19.95 ? 127 GLY A O   1 
ATOM   938   N  N   . LYS A  1 129 ? 60.138  59.049  13.070  1.00 21.57 ? 128 LYS A N   1 
ATOM   939   C  CA  . LYS A  1 129 ? 59.833  60.445  12.814  1.00 21.56 ? 128 LYS A CA  1 
ATOM   940   C  C   . LYS A  1 129 ? 60.336  61.221  14.030  1.00 22.53 ? 128 LYS A C   1 
ATOM   941   O  O   . LYS A  1 129 ? 59.973  62.373  14.246  1.00 23.60 ? 128 LYS A O   1 
ATOM   942   C  CB  . LYS A  1 129 ? 58.317  60.621  12.672  1.00 20.33 ? 128 LYS A CB  1 
ATOM   943   C  CG  . LYS A  1 129 ? 57.466  59.641  11.835  1.00 20.05 ? 128 LYS A CG  1 
ATOM   944   C  CD  . LYS A  1 129 ? 57.767  59.559  10.329  1.00 22.85 ? 128 LYS A CD  1 
ATOM   945   C  CE  . LYS A  1 129 ? 56.439  59.130  9.641   1.00 26.50 ? 128 LYS A CE  1 
ATOM   946   N  NZ  . LYS A  1 129 ? 56.380  59.124  8.170   1.00 22.07 ? 128 LYS A NZ  1 
ATOM   947   N  N   . GLY A  1 130 ? 61.207  60.659  14.864  1.00 25.14 ? 129 GLY A N   1 
ATOM   948   C  CA  . GLY A  1 130 ? 61.655  61.342  16.068  1.00 28.17 ? 129 GLY A CA  1 
ATOM   949   C  C   . GLY A  1 130 ? 62.728  62.372  15.810  1.00 29.25 ? 129 GLY A C   1 
ATOM   950   O  O   . GLY A  1 130 ? 63.119  63.124  16.703  1.00 29.29 ? 129 GLY A O   1 
ATOM   951   N  N   . GLY A  1 131 ? 63.268  62.292  14.599  1.00 31.01 ? 130 GLY A N   1 
ATOM   952   C  CA  . GLY A  1 131 ? 64.234  63.262  14.175  1.00 32.75 ? 130 GLY A CA  1 
ATOM   953   C  C   . GLY A  1 131 ? 65.566  63.234  14.903  1.00 33.77 ? 130 GLY A C   1 
ATOM   954   O  O   . GLY A  1 131 ? 65.886  64.051  15.768  1.00 35.41 ? 130 GLY A O   1 
ATOM   955   N  N   . ASN A  1 132 ? 66.358  62.253  14.502  1.00 32.93 ? 131 ASN A N   1 
ATOM   956   C  CA  . ASN A  1 132 ? 67.758  62.148  14.857  1.00 31.83 ? 131 ASN A CA  1 
ATOM   957   C  C   . ASN A  1 132 ? 68.128  60.777  14.343  1.00 32.61 ? 131 ASN A C   1 
ATOM   958   O  O   . ASN A  1 132 ? 67.268  59.927  14.090  1.00 32.97 ? 131 ASN A O   1 
ATOM   959   C  CB  . ASN A  1 132 ? 68.083  62.209  16.397  1.00 29.13 ? 131 ASN A CB  1 
ATOM   960   C  CG  . ASN A  1 132 ? 67.700  61.071  17.321  1.00 25.44 ? 131 ASN A CG  1 
ATOM   961   O  OD1 . ASN A  1 132 ? 66.649  60.459  17.213  1.00 24.23 ? 131 ASN A OD1 1 
ATOM   962   N  ND2 . ASN A  1 132 ? 68.522  60.693  18.279  1.00 26.86 ? 131 ASN A ND2 1 
ATOM   963   N  N   . GLU A  1 133 ? 69.437  60.626  14.189  1.00 33.03 ? 132 GLU A N   1 
ATOM   964   C  CA  . GLU A  1 133 ? 70.083  59.456  13.643  1.00 32.35 ? 132 GLU A CA  1 
ATOM   965   C  C   . GLU A  1 133 ? 69.680  58.161  14.379  1.00 31.64 ? 132 GLU A C   1 
ATOM   966   O  O   . GLU A  1 133 ? 69.491  57.094  13.786  1.00 31.75 ? 132 GLU A O   1 
ATOM   967   C  CB  . GLU A  1 133 ? 71.552  59.781  13.730  1.00 33.76 ? 132 GLU A CB  1 
ATOM   968   C  CG  . GLU A  1 133 ? 72.358  59.161  12.622  1.00 38.44 ? 132 GLU A CG  1 
ATOM   969   C  CD  . GLU A  1 133 ? 73.830  59.149  12.999  1.00 41.49 ? 132 GLU A CD  1 
ATOM   970   O  OE1 . GLU A  1 133 ? 74.407  60.225  13.148  1.00 44.54 ? 132 GLU A OE1 1 
ATOM   971   O  OE2 . GLU A  1 133 ? 74.394  58.064  13.166  1.00 44.31 ? 132 GLU A OE2 1 
ATOM   972   N  N   . GLU A  1 134 ? 69.527  58.211  15.701  1.00 29.40 ? 133 GLU A N   1 
ATOM   973   C  CA  . GLU A  1 134 ? 69.017  57.063  16.422  1.00 26.86 ? 133 GLU A CA  1 
ATOM   974   C  C   . GLU A  1 134 ? 67.553  56.763  16.105  1.00 24.31 ? 133 GLU A C   1 
ATOM   975   O  O   . GLU A  1 134 ? 67.123  55.605  16.020  1.00 22.49 ? 133 GLU A O   1 
ATOM   976   C  CB  . GLU A  1 134 ? 69.164  57.293  17.911  1.00 30.16 ? 133 GLU A CB  1 
ATOM   977   C  CG  . GLU A  1 134 ? 68.940  56.030  18.723  1.00 35.09 ? 133 GLU A CG  1 
ATOM   978   C  CD  . GLU A  1 134 ? 69.825  54.925  18.195  1.00 39.58 ? 133 GLU A CD  1 
ATOM   979   O  OE1 . GLU A  1 134 ? 71.048  54.996  18.371  1.00 41.96 ? 133 GLU A OE1 1 
ATOM   980   O  OE2 . GLU A  1 134 ? 69.278  54.028  17.554  1.00 41.31 ? 133 GLU A OE2 1 
ATOM   981   N  N   . SER A  1 135 ? 66.762  57.801  15.901  1.00 20.81 ? 134 SER A N   1 
ATOM   982   C  CA  . SER A  1 135 ? 65.379  57.624  15.594  1.00 21.24 ? 134 SER A CA  1 
ATOM   983   C  C   . SER A  1 135 ? 65.271  56.792  14.340  1.00 22.15 ? 134 SER A C   1 
ATOM   984   O  O   . SER A  1 135 ? 64.619  55.744  14.394  1.00 24.40 ? 134 SER A O   1 
ATOM   985   C  CB  . SER A  1 135 ? 64.775  58.974  15.430  1.00 21.33 ? 134 SER A CB  1 
ATOM   986   O  OG  . SER A  1 135 ? 63.472  58.894  14.919  1.00 22.61 ? 134 SER A OG  1 
ATOM   987   N  N   . THR A  1 136 ? 65.982  57.162  13.267  1.00 21.35 ? 135 THR A N   1 
ATOM   988   C  CA  . THR A  1 136 ? 65.992  56.409  12.020  1.00 18.48 ? 135 THR A CA  1 
ATOM   989   C  C   . THR A  1 136 ? 66.609  55.001  12.134  1.00 18.09 ? 135 THR A C   1 
ATOM   990   O  O   . THR A  1 136 ? 66.599  54.260  11.142  1.00 16.92 ? 135 THR A O   1 
ATOM   991   C  CB  . THR A  1 136 ? 66.735  57.270  10.958  1.00 19.14 ? 135 THR A CB  1 
ATOM   992   O  OG1 . THR A  1 136 ? 67.925  57.712  11.596  1.00 23.32 ? 135 THR A OG1 1 
ATOM   993   C  CG2 . THR A  1 136 ? 65.961  58.498  10.472  1.00 16.30 ? 135 THR A CG2 1 
ATOM   994   N  N   . LYS A  1 137 ? 67.185  54.565  13.271  1.00 16.96 ? 136 LYS A N   1 
ATOM   995   C  CA  . LYS A  1 137 ? 67.632  53.188  13.433  1.00 15.02 ? 136 LYS A CA  1 
ATOM   996   C  C   . LYS A  1 137 ? 66.717  52.418  14.366  1.00 13.37 ? 136 LYS A C   1 
ATOM   997   O  O   . LYS A  1 137 ? 66.263  51.362  13.974  1.00 14.67 ? 136 LYS A O   1 
ATOM   998   C  CB  . LYS A  1 137 ? 69.050  53.136  13.978  1.00 16.02 ? 136 LYS A CB  1 
ATOM   999   C  CG  . LYS A  1 137 ? 70.088  53.630  12.979  1.00 20.38 ? 136 LYS A CG  1 
ATOM   1000  C  CD  . LYS A  1 137 ? 71.507  53.614  13.546  1.00 22.84 ? 136 LYS A CD  1 
ATOM   1001  C  CE  . LYS A  1 137 ? 71.830  54.874  14.350  1.00 24.67 ? 136 LYS A CE  1 
ATOM   1002  N  NZ  . LYS A  1 137 ? 73.183  54.843  14.869  1.00 26.46 ? 136 LYS A NZ  1 
ATOM   1003  N  N   . THR A  1 138 ? 66.323  52.899  15.541  1.00 14.66 ? 137 THR A N   1 
ATOM   1004  C  CA  . THR A  1 138 ? 65.550  52.172  16.548  1.00 13.07 ? 137 THR A CA  1 
ATOM   1005  C  C   . THR A  1 138 ? 64.232  52.763  16.942  1.00 12.46 ? 137 THR A C   1 
ATOM   1006  O  O   . THR A  1 138 ? 63.388  52.199  17.657  1.00 12.54 ? 137 THR A O   1 
ATOM   1007  C  CB  . THR A  1 138 ? 66.254  52.072  17.864  1.00 14.99 ? 137 THR A CB  1 
ATOM   1008  O  OG1 . THR A  1 138 ? 66.557  53.411  18.299  1.00 17.35 ? 137 THR A OG1 1 
ATOM   1009  C  CG2 . THR A  1 138 ? 67.523  51.305  17.765  1.00 15.47 ? 137 THR A CG2 1 
ATOM   1010  N  N   . GLY A  1 139 ? 64.181  54.040  16.621  1.00 12.21 ? 138 GLY A N   1 
ATOM   1011  C  CA  . GLY A  1 139 ? 63.052  54.812  17.044  1.00 10.78 ? 138 GLY A CA  1 
ATOM   1012  C  C   . GLY A  1 139 ? 63.202  55.091  18.510  1.00 8.99  ? 138 GLY A C   1 
ATOM   1013  O  O   . GLY A  1 139 ? 62.219  55.306  19.176  1.00 10.12 ? 138 GLY A O   1 
ATOM   1014  N  N   . ASN A  1 140 ? 64.415  55.109  19.038  1.00 11.06 ? 139 ASN A N   1 
ATOM   1015  C  CA  . ASN A  1 140 ? 64.687  55.403  20.429  1.00 9.18  ? 139 ASN A CA  1 
ATOM   1016  C  C   . ASN A  1 140 ? 63.916  54.559  21.438  1.00 8.14  ? 139 ASN A C   1 
ATOM   1017  O  O   . ASN A  1 140 ? 63.624  54.970  22.557  1.00 10.34 ? 139 ASN A O   1 
ATOM   1018  C  CB  . ASN A  1 140 ? 64.423  56.896  20.594  1.00 13.12 ? 139 ASN A CB  1 
ATOM   1019  C  CG  . ASN A  1 140 ? 65.508  57.669  19.897  1.00 14.34 ? 139 ASN A CG  1 
ATOM   1020  O  OD1 . ASN A  1 140 ? 66.664  57.443  20.209  1.00 18.75 ? 139 ASN A OD1 1 
ATOM   1021  N  ND2 . ASN A  1 140 ? 65.293  58.628  19.012  1.00 14.39 ? 139 ASN A ND2 1 
ATOM   1022  N  N   . ALA A  1 141 ? 63.657  53.297  21.149  1.00 8.88  ? 140 ALA A N   1 
ATOM   1023  C  CA  . ALA A  1 141 ? 62.864  52.488  22.042  1.00 7.85  ? 140 ALA A CA  1 
ATOM   1024  C  C   . ALA A  1 141 ? 63.592  51.962  23.275  1.00 7.70  ? 140 ALA A C   1 
ATOM   1025  O  O   . ALA A  1 141 ? 62.998  51.324  24.148  1.00 10.06 ? 140 ALA A O   1 
ATOM   1026  C  CB  . ALA A  1 141 ? 62.312  51.376  21.210  1.00 7.36  ? 140 ALA A CB  1 
ATOM   1027  N  N   . GLY A  1 142 ? 64.883  52.212  23.438  1.00 7.46  ? 141 GLY A N   1 
ATOM   1028  C  CA  . GLY A  1 142 ? 65.585  51.836  24.648  1.00 6.70  ? 141 GLY A CA  1 
ATOM   1029  C  C   . GLY A  1 142 ? 65.833  50.358  24.751  1.00 10.12 ? 141 GLY A C   1 
ATOM   1030  O  O   . GLY A  1 142 ? 65.836  49.622  23.749  1.00 14.16 ? 141 GLY A O   1 
ATOM   1031  N  N   . SER A  1 143 ? 65.962  49.900  25.988  1.00 9.47  ? 142 SER A N   1 
ATOM   1032  C  CA  . SER A  1 143 ? 66.341  48.546  26.296  1.00 8.40  ? 142 SER A CA  1 
ATOM   1033  C  C   . SER A  1 143 ? 65.387  47.536  25.807  1.00 5.86  ? 142 SER A C   1 
ATOM   1034  O  O   . SER A  1 143 ? 64.224  47.882  25.672  1.00 6.01  ? 142 SER A O   1 
ATOM   1035  C  CB  . SER A  1 143 ? 66.457  48.360  27.783  1.00 12.14 ? 142 SER A CB  1 
ATOM   1036  O  OG  . SER A  1 143 ? 67.170  49.479  28.295  1.00 22.19 ? 142 SER A OG  1 
ATOM   1037  N  N   . ARG A  1 144 ? 65.893  46.316  25.590  1.00 6.52  ? 143 ARG A N   1 
ATOM   1038  C  CA  . ARG A  1 144 ? 65.110  45.146  25.215  1.00 4.24  ? 143 ARG A CA  1 
ATOM   1039  C  C   . ARG A  1 144 ? 64.648  44.598  26.553  1.00 5.50  ? 143 ARG A C   1 
ATOM   1040  O  O   . ARG A  1 144 ? 65.468  44.081  27.334  1.00 6.75  ? 143 ARG A O   1 
ATOM   1041  C  CB  . ARG A  1 144 ? 65.994  44.151  24.511  1.00 2.00  ? 143 ARG A CB  1 
ATOM   1042  C  CG  . ARG A  1 144 ? 66.339  44.673  23.149  1.00 5.55  ? 143 ARG A CG  1 
ATOM   1043  C  CD  . ARG A  1 144 ? 67.591  43.984  22.684  1.00 4.95  ? 143 ARG A CD  1 
ATOM   1044  N  NE  . ARG A  1 144 ? 68.157  44.763  21.603  1.00 6.18  ? 143 ARG A NE  1 
ATOM   1045  C  CZ  . ARG A  1 144 ? 68.464  44.229  20.431  1.00 5.41  ? 143 ARG A CZ  1 
ATOM   1046  N  NH1 . ARG A  1 144 ? 68.272  42.930  20.167  1.00 9.90  ? 143 ARG A NH1 1 
ATOM   1047  N  NH2 . ARG A  1 144 ? 68.947  45.016  19.482  1.00 2.00  ? 143 ARG A NH2 1 
ATOM   1048  N  N   . LEU A  1 145 ? 63.356  44.741  26.871  1.00 4.28  ? 144 LEU A N   1 
ATOM   1049  C  CA  . LEU A  1 145 ? 62.933  44.236  28.164  1.00 4.57  ? 144 LEU A CA  1 
ATOM   1050  C  C   . LEU A  1 145 ? 62.695  42.739  28.182  1.00 4.92  ? 144 LEU A C   1 
ATOM   1051  O  O   . LEU A  1 145 ? 62.952  42.071  29.195  1.00 8.21  ? 144 LEU A O   1 
ATOM   1052  C  CB  . LEU A  1 145 ? 61.677  44.916  28.625  1.00 2.12  ? 144 LEU A CB  1 
ATOM   1053  C  CG  . LEU A  1 145 ? 61.788  46.374  29.010  1.00 2.00  ? 144 LEU A CG  1 
ATOM   1054  C  CD1 . LEU A  1 145 ? 60.454  46.800  29.560  1.00 2.00  ? 144 LEU A CD1 1 
ATOM   1055  C  CD2 . LEU A  1 145 ? 62.848  46.591  30.046  1.00 2.00  ? 144 LEU A CD2 1 
ATOM   1056  N  N   . ALA A  1 146 ? 62.193  42.195  27.086  1.00 3.98  ? 145 ALA A N   1 
ATOM   1057  C  CA  . ALA A  1 146 ? 61.867  40.782  26.982  1.00 5.44  ? 145 ALA A CA  1 
ATOM   1058  C  C   . ALA A  1 146 ? 61.781  40.406  25.512  1.00 5.50  ? 145 ALA A C   1 
ATOM   1059  O  O   . ALA A  1 146 ? 61.450  41.283  24.686  1.00 5.11  ? 145 ALA A O   1 
ATOM   1060  C  CB  . ALA A  1 146 ? 60.518  40.466  27.602  1.00 4.54  ? 145 ALA A CB  1 
ATOM   1061  N  N   . CYS A  1 147 ? 62.075  39.138  25.189  1.00 3.75  ? 146 CYS A N   1 
ATOM   1062  C  CA  . CYS A  1 147 ? 62.077  38.722  23.805  1.00 4.80  ? 146 CYS A CA  1 
ATOM   1063  C  C   . CYS A  1 147 ? 61.831  37.257  23.680  1.00 6.21  ? 146 CYS A C   1 
ATOM   1064  O  O   . CYS A  1 147 ? 61.891  36.547  24.691  1.00 5.25  ? 146 CYS A O   1 
ATOM   1065  C  CB  . CYS A  1 147 ? 63.416  39.038  23.135  1.00 5.51  ? 146 CYS A CB  1 
ATOM   1066  S  SG  . CYS A  1 147 ? 64.799  38.459  24.140  1.00 8.05  ? 146 CYS A SG  1 
ATOM   1067  N  N   . GLY A  1 148 ? 61.517  36.844  22.440  1.00 5.97  ? 147 GLY A N   1 
ATOM   1068  C  CA  . GLY A  1 148 ? 61.340  35.449  22.144  1.00 3.94  ? 147 GLY A CA  1 
ATOM   1069  C  C   . GLY A  1 148 ? 61.647  35.106  20.712  1.00 3.83  ? 147 GLY A C   1 
ATOM   1070  O  O   . GLY A  1 148 ? 61.536  35.951  19.838  1.00 7.00  ? 147 GLY A O   1 
ATOM   1071  N  N   . VAL A  1 149 ? 62.062  33.892  20.388  1.00 5.06  ? 148 VAL A N   1 
ATOM   1072  C  CA  . VAL A  1 149 ? 62.284  33.526  18.991  1.00 3.35  ? 148 VAL A CA  1 
ATOM   1073  C  C   . VAL A  1 149 ? 60.905  33.120  18.492  1.00 2.00  ? 148 VAL A C   1 
ATOM   1074  O  O   . VAL A  1 149 ? 60.207  32.420  19.228  1.00 2.10  ? 148 VAL A O   1 
ATOM   1075  C  CB  . VAL A  1 149 ? 63.275  32.370  18.937  1.00 2.00  ? 148 VAL A CB  1 
ATOM   1076  C  CG1 . VAL A  1 149 ? 63.473  31.960  17.508  1.00 2.00  ? 148 VAL A CG1 1 
ATOM   1077  C  CG2 . VAL A  1 149 ? 64.549  32.773  19.629  1.00 2.00  ? 148 VAL A CG2 1 
ATOM   1078  N  N   . ILE A  1 150 ? 60.504  33.526  17.295  1.00 2.00  ? 149 ILE A N   1 
ATOM   1079  C  CA  . ILE A  1 150 ? 59.192  33.247  16.750  1.00 2.00  ? 149 ILE A CA  1 
ATOM   1080  C  C   . ILE A  1 150 ? 59.229  31.851  16.197  1.00 3.17  ? 149 ILE A C   1 
ATOM   1081  O  O   . ILE A  1 150 ? 59.995  31.600  15.241  1.00 4.35  ? 149 ILE A O   1 
ATOM   1082  C  CB  . ILE A  1 150 ? 58.892  34.291  15.658  1.00 2.00  ? 149 ILE A CB  1 
ATOM   1083  C  CG1 . ILE A  1 150 ? 58.836  35.652  16.271  1.00 2.00  ? 149 ILE A CG1 1 
ATOM   1084  C  CG2 . ILE A  1 150 ? 57.576  34.005  14.993  1.00 2.00  ? 149 ILE A CG2 1 
ATOM   1085  C  CD1 . ILE A  1 150 ? 58.933  36.769  15.244  1.00 2.00  ? 149 ILE A CD1 1 
ATOM   1086  N  N   . GLY A  1 151 ? 58.451  30.926  16.760  1.00 2.00  ? 150 GLY A N   1 
ATOM   1087  C  CA  . GLY A  1 151 ? 58.403  29.572  16.253  1.00 2.00  ? 150 GLY A CA  1 
ATOM   1088  C  C   . GLY A  1 151 ? 57.046  29.259  15.629  1.00 2.00  ? 150 GLY A C   1 
ATOM   1089  O  O   . GLY A  1 151 ? 56.035  29.917  15.840  1.00 2.00  ? 150 GLY A O   1 
ATOM   1090  N  N   . ILE A  1 152 ? 57.042  28.227  14.811  1.00 2.00  ? 151 ILE A N   1 
ATOM   1091  C  CA  . ILE A  1 152 ? 55.904  27.660  14.118  1.00 2.89  ? 151 ILE A CA  1 
ATOM   1092  C  C   . ILE A  1 152 ? 54.931  27.039  15.118  1.00 3.35  ? 151 ILE A C   1 
ATOM   1093  O  O   . ILE A  1 152 ? 55.364  26.228  15.927  1.00 4.66  ? 151 ILE A O   1 
ATOM   1094  C  CB  . ILE A  1 152 ? 56.491  26.607  13.163  1.00 5.69  ? 151 ILE A CB  1 
ATOM   1095  C  CG1 . ILE A  1 152 ? 57.287  27.354  12.132  1.00 5.71  ? 151 ILE A CG1 1 
ATOM   1096  C  CG2 . ILE A  1 152 ? 55.440  25.679  12.571  1.00 2.80  ? 151 ILE A CG2 1 
ATOM   1097  C  CD1 . ILE A  1 152 ? 58.080  26.323  11.313  1.00 6.02  ? 151 ILE A CD1 1 
ATOM   1098  N  N   . ALA A  1 153 ? 53.634  27.262  15.072  1.00 3.88  ? 152 ALA A N   1 
ATOM   1099  C  CA  . ALA A  1 153 ? 52.721  26.653  16.005  1.00 7.74  ? 152 ALA A CA  1 
ATOM   1100  C  C   . ALA A  1 153 ? 51.605  25.948  15.245  1.00 13.28 ? 152 ALA A C   1 
ATOM   1101  O  O   . ALA A  1 153 ? 51.416  26.106  14.035  1.00 18.83 ? 152 ALA A O   1 
ATOM   1102  C  CB  . ALA A  1 153 ? 52.078  27.673  16.856  1.00 2.30  ? 152 ALA A CB  1 
ATOM   1103  N  N   . GLN A  1 154 ? 50.961  25.062  15.970  1.00 17.39 ? 153 GLN A N   1 
ATOM   1104  C  CA  . GLN A  1 154 ? 49.755  24.400  15.541  1.00 21.48 ? 153 GLN A CA  1 
ATOM   1105  C  C   . GLN A  1 154 ? 48.668  25.364  16.035  1.00 24.31 ? 153 GLN A C   1 
ATOM   1106  O  O   . GLN A  1 154 ? 48.713  25.795  17.210  1.00 26.09 ? 153 GLN A O   1 
ATOM   1107  C  CB  . GLN A  1 154 ? 49.656  23.058  16.251  1.00 25.39 ? 153 GLN A CB  1 
ATOM   1108  C  CG  . GLN A  1 154 ? 48.631  22.108  15.648  1.00 30.61 ? 153 GLN A CG  1 
ATOM   1109  C  CD  . GLN A  1 154 ? 48.542  20.774  16.376  1.00 33.83 ? 153 GLN A CD  1 
ATOM   1110  O  OE1 . GLN A  1 154 ? 48.984  20.631  17.518  1.00 37.83 ? 153 GLN A OE1 1 
ATOM   1111  N  NE2 . GLN A  1 154 ? 47.975  19.739  15.761  1.00 34.14 ? 153 GLN A NE2 1 
ATOM   1112  O  OXT . GLN A  1 154 ? 47.795  25.688  15.234  1.00 25.91 ? 153 GLN A OXT 1 
HETATM 1113  C  C   . ACE B  1 1   ? 68.092  30.585  4.697   1.00 33.66 ? 0   ACE F C   1 
HETATM 1114  O  O   . ACE B  1 1   ? 67.280  31.070  5.510   1.00 35.99 ? 0   ACE F O   1 
HETATM 1115  C  CH3 . ACE B  1 1   ? 67.673  30.341  3.241   1.00 33.36 ? 0   ACE F CH3 1 
ATOM   1116  N  N   . ALA B  1 2   ? 69.369  30.238  4.998   1.00 30.33 ? 1   ALA F N   1 
ATOM   1117  C  CA  . ALA B  1 2   ? 70.063  30.459  6.282   1.00 23.93 ? 1   ALA F CA  1 
ATOM   1118  C  C   . ALA B  1 2   ? 71.306  29.574  6.249   1.00 19.08 ? 1   ALA F C   1 
ATOM   1119  O  O   . ALA B  1 2   ? 71.175  28.395  5.972   1.00 20.84 ? 1   ALA F O   1 
ATOM   1120  C  CB  . ALA B  1 2   ? 69.245  30.018  7.521   1.00 24.14 ? 1   ALA F CB  1 
ATOM   1121  N  N   . THR B  1 3   ? 72.526  30.088  6.343   1.00 13.72 ? 2   THR F N   1 
ATOM   1122  C  CA  . THR B  1 3   ? 73.686  29.259  6.494   1.00 8.64  ? 2   THR F CA  1 
ATOM   1123  C  C   . THR B  1 3   ? 73.769  28.866  7.958   1.00 5.30  ? 2   THR F C   1 
ATOM   1124  O  O   . THR B  1 3   ? 74.367  27.849  8.254   1.00 3.98  ? 2   THR F O   1 
ATOM   1125  C  CB  . THR B  1 3   ? 75.043  29.963  6.162   1.00 9.54  ? 2   THR F CB  1 
ATOM   1126  O  OG1 . THR B  1 3   ? 74.866  31.342  6.481   1.00 13.27 ? 2   THR F OG1 1 
ATOM   1127  C  CG2 . THR B  1 3   ? 75.515  29.761  4.731   1.00 12.53 ? 2   THR F CG2 1 
ATOM   1128  N  N   . LYS B  1 4   ? 73.254  29.622  8.926   1.00 2.11  ? 3   LYS F N   1 
ATOM   1129  C  CA  . LYS B  1 4   ? 73.449  29.340  10.337  1.00 2.00  ? 3   LYS F CA  1 
ATOM   1130  C  C   . LYS B  1 4   ? 72.254  29.487  11.278  1.00 2.00  ? 3   LYS F C   1 
ATOM   1131  O  O   . LYS B  1 4   ? 71.505  30.446  11.195  1.00 5.42  ? 3   LYS F O   1 
ATOM   1132  C  CB  . LYS B  1 4   ? 74.500  30.218  10.909  1.00 2.95  ? 3   LYS F CB  1 
ATOM   1133  C  CG  . LYS B  1 4   ? 75.865  30.180  10.318  1.00 5.79  ? 3   LYS F CG  1 
ATOM   1134  C  CD  . LYS B  1 4   ? 76.839  29.989  11.467  1.00 8.16  ? 3   LYS F CD  1 
ATOM   1135  C  CE  . LYS B  1 4   ? 78.244  30.343  11.005  1.00 14.54 ? 3   LYS F CE  1 
ATOM   1136  N  NZ  . LYS B  1 4   ? 78.553  29.866  9.649   1.00 17.17 ? 3   LYS F NZ  1 
ATOM   1137  N  N   . ALA B  1 5   ? 72.079  28.618  12.238  1.00 2.00  ? 4   ALA F N   1 
ATOM   1138  C  CA  . ALA B  1 5   ? 70.999  28.686  13.163  1.00 2.00  ? 4   ALA F CA  1 
ATOM   1139  C  C   . ALA B  1 5   ? 71.589  28.409  14.547  1.00 2.00  ? 4   ALA F C   1 
ATOM   1140  O  O   . ALA B  1 5   ? 72.785  28.090  14.644  1.00 2.00  ? 4   ALA F O   1 
ATOM   1141  C  CB  . ALA B  1 5   ? 69.964  27.646  12.796  1.00 2.00  ? 4   ALA F CB  1 
ATOM   1142  N  N   . VAL B  1 6   ? 70.775  28.556  15.614  1.00 2.00  ? 5   VAL F N   1 
ATOM   1143  C  CA  . VAL B  1 6   ? 71.228  28.417  16.998  1.00 3.35  ? 5   VAL F CA  1 
ATOM   1144  C  C   . VAL B  1 6   ? 70.028  28.163  17.869  1.00 3.20  ? 5   VAL F C   1 
ATOM   1145  O  O   . VAL B  1 6   ? 68.933  28.570  17.502  1.00 5.29  ? 5   VAL F O   1 
ATOM   1146  C  CB  . VAL B  1 6   ? 71.959  29.710  17.482  1.00 2.00  ? 5   VAL F CB  1 
ATOM   1147  C  CG1 . VAL B  1 6   ? 71.002  30.813  17.697  1.00 2.00  ? 5   VAL F CG1 1 
ATOM   1148  C  CG2 . VAL B  1 6   ? 72.690  29.430  18.781  1.00 6.02  ? 5   VAL F CG2 1 
ATOM   1149  N  N   . ALA B  1 7   ? 70.171  27.470  18.980  1.00 2.94  ? 6   ALA F N   1 
ATOM   1150  C  CA  . ALA B  1 7   ? 69.075  27.227  19.879  1.00 2.00  ? 6   ALA F CA  1 
ATOM   1151  C  C   . ALA B  1 7   ? 69.641  27.195  21.296  1.00 2.55  ? 6   ALA F C   1 
ATOM   1152  O  O   . ALA B  1 7   ? 70.655  26.552  21.559  1.00 2.66  ? 6   ALA F O   1 
ATOM   1153  C  CB  . ALA B  1 7   ? 68.444  25.885  19.559  1.00 2.00  ? 6   ALA F CB  1 
ATOM   1154  N  N   . VAL B  1 8   ? 68.999  27.888  22.217  1.00 2.40  ? 7   VAL F N   1 
ATOM   1155  C  CA  . VAL B  1 8   ? 69.401  27.896  23.598  1.00 2.44  ? 7   VAL F CA  1 
ATOM   1156  C  C   . VAL B  1 8   ? 68.459  26.901  24.238  1.00 3.79  ? 7   VAL F C   1 
ATOM   1157  O  O   . VAL B  1 8   ? 67.244  27.065  24.148  1.00 5.68  ? 7   VAL F O   1 
ATOM   1158  C  CB  . VAL B  1 8   ? 69.233  29.337  24.113  1.00 4.21  ? 7   VAL F CB  1 
ATOM   1159  C  CG1 . VAL B  1 8   ? 69.578  29.430  25.602  1.00 5.96  ? 7   VAL F CG1 1 
ATOM   1160  C  CG2 . VAL B  1 8   ? 70.199  30.251  23.361  1.00 3.30  ? 7   VAL F CG2 1 
ATOM   1161  N  N   . LEU B  1 9   ? 68.954  25.825  24.822  1.00 3.10  ? 8   LEU F N   1 
ATOM   1162  C  CA  . LEU B  1 9   ? 68.119  24.862  25.485  1.00 2.00  ? 8   LEU F CA  1 
ATOM   1163  C  C   . LEU B  1 9   ? 67.964  25.276  26.930  1.00 3.10  ? 8   LEU F C   1 
ATOM   1164  O  O   . LEU B  1 9   ? 68.952  25.617  27.584  1.00 4.73  ? 8   LEU F O   1 
ATOM   1165  C  CB  . LEU B  1 9   ? 68.795  23.542  25.335  1.00 2.67  ? 8   LEU F CB  1 
ATOM   1166  C  CG  . LEU B  1 9   ? 68.371  22.612  24.183  1.00 3.82  ? 8   LEU F CG  1 
ATOM   1167  C  CD1 . LEU B  1 9   ? 68.313  23.269  22.853  1.00 3.13  ? 8   LEU F CD1 1 
ATOM   1168  C  CD2 . LEU B  1 9   ? 69.425  21.539  24.082  1.00 7.86  ? 8   LEU F CD2 1 
ATOM   1169  N  N   . LYS B  1 10  ? 66.743  25.309  27.453  1.00 6.10  ? 9   LYS F N   1 
ATOM   1170  C  CA  . LYS B  1 10  ? 66.457  25.708  28.824  1.00 10.01 ? 9   LYS F CA  1 
ATOM   1171  C  C   . LYS B  1 10  ? 65.338  24.785  29.259  1.00 10.58 ? 9   LYS F C   1 
ATOM   1172  O  O   . LYS B  1 10  ? 64.546  24.339  28.428  1.00 8.68  ? 9   LYS F O   1 
ATOM   1173  C  CB  . LYS B  1 10  ? 65.949  27.150  28.941  1.00 14.27 ? 9   LYS F CB  1 
ATOM   1174  C  CG  . LYS B  1 10  ? 66.497  27.781  30.244  1.00 26.33 ? 9   LYS F CG  1 
ATOM   1175  C  CD  . LYS B  1 10  ? 66.020  29.215  30.644  1.00 32.16 ? 9   LYS F CD  1 
ATOM   1176  C  CE  . LYS B  1 10  ? 66.341  30.315  29.584  1.00 37.17 ? 9   LYS F CE  1 
ATOM   1177  N  NZ  . LYS B  1 10  ? 65.670  31.597  29.847  1.00 39.32 ? 9   LYS F NZ  1 
ATOM   1178  N  N   . GLY B  1 11  ? 65.278  24.428  30.542  1.00 13.65 ? 10  GLY F N   1 
ATOM   1179  C  CA  . GLY B  1 11  ? 64.236  23.548  31.032  1.00 14.48 ? 10  GLY F CA  1 
ATOM   1180  C  C   . GLY B  1 11  ? 63.794  23.844  32.448  1.00 15.54 ? 10  GLY F C   1 
ATOM   1181  O  O   . GLY B  1 11  ? 64.116  24.862  33.070  1.00 15.87 ? 10  GLY F O   1 
ATOM   1182  N  N   . ASP B  1 12  ? 63.020  22.924  33.011  1.00 20.37 ? 11  ASP F N   1 
ATOM   1183  C  CA  . ASP B  1 12  ? 62.542  23.121  34.384  1.00 25.00 ? 11  ASP F CA  1 
ATOM   1184  C  C   . ASP B  1 12  ? 63.558  22.294  35.175  1.00 23.69 ? 11  ASP F C   1 
ATOM   1185  O  O   . ASP B  1 12  ? 63.294  21.170  35.612  1.00 24.97 ? 11  ASP F O   1 
ATOM   1186  C  CB  . ASP B  1 12  ? 61.112  22.541  34.644  1.00 28.98 ? 11  ASP F CB  1 
ATOM   1187  C  CG  . ASP B  1 12  ? 59.956  22.889  33.693  1.00 35.27 ? 11  ASP F CG  1 
ATOM   1188  O  OD1 . ASP B  1 12  ? 59.850  24.032  33.217  1.00 38.15 ? 11  ASP F OD1 1 
ATOM   1189  O  OD2 . ASP B  1 12  ? 59.143  21.982  33.441  1.00 39.39 ? 11  ASP F OD2 1 
ATOM   1190  N  N   . GLY B  1 13  ? 64.785  22.792  35.294  1.00 21.16 ? 12  GLY F N   1 
ATOM   1191  C  CA  . GLY B  1 13  ? 65.812  22.032  35.958  1.00 15.66 ? 12  GLY F CA  1 
ATOM   1192  C  C   . GLY B  1 13  ? 67.189  22.471  35.516  1.00 11.18 ? 12  GLY F C   1 
ATOM   1193  O  O   . GLY B  1 13  ? 67.336  23.532  34.925  1.00 12.73 ? 12  GLY F O   1 
ATOM   1194  N  N   . PRO B  1 14  ? 68.190  21.633  35.786  1.00 7.49  ? 13  PRO F N   1 
ATOM   1195  C  CA  . PRO B  1 14  ? 69.607  21.919  35.624  1.00 4.11  ? 13  PRO F CA  1 
ATOM   1196  C  C   . PRO B  1 14  ? 70.051  22.027  34.187  1.00 4.25  ? 13  PRO F C   1 
ATOM   1197  O  O   . PRO B  1 14  ? 71.057  22.675  33.901  1.00 5.41  ? 13  PRO F O   1 
ATOM   1198  C  CB  . PRO B  1 14  ? 70.334  20.789  36.283  1.00 4.86  ? 13  PRO F CB  1 
ATOM   1199  C  CG  . PRO B  1 14  ? 69.273  19.921  36.966  1.00 5.00  ? 13  PRO F CG  1 
ATOM   1200  C  CD  . PRO B  1 14  ? 67.977  20.257  36.251  1.00 4.85  ? 13  PRO F CD  1 
ATOM   1201  N  N   . VAL B  1 15  ? 69.318  21.353  33.294  1.00 2.75  ? 14  VAL F N   1 
ATOM   1202  C  CA  . VAL B  1 15  ? 69.810  21.217  31.960  1.00 2.03  ? 14  VAL F CA  1 
ATOM   1203  C  C   . VAL B  1 15  ? 69.717  22.478  31.092  1.00 2.12  ? 14  VAL F C   1 
ATOM   1204  O  O   . VAL B  1 15  ? 68.663  23.077  30.907  1.00 2.00  ? 14  VAL F O   1 
ATOM   1205  C  CB  . VAL B  1 15  ? 69.078  20.040  31.387  1.00 2.00  ? 14  VAL F CB  1 
ATOM   1206  C  CG1 . VAL B  1 15  ? 69.560  19.861  29.971  1.00 2.00  ? 14  VAL F CG1 1 
ATOM   1207  C  CG2 . VAL B  1 15  ? 69.379  18.745  32.170  1.00 2.00  ? 14  VAL F CG2 1 
ATOM   1208  N  N   . GLN B  1 16  ? 70.831  22.901  30.543  1.00 2.00  ? 15  GLN F N   1 
ATOM   1209  C  CA  . GLN B  1 16  ? 70.827  24.011  29.656  1.00 7.32  ? 15  GLN F CA  1 
ATOM   1210  C  C   . GLN B  1 16  ? 72.033  23.872  28.797  1.00 7.26  ? 15  GLN F C   1 
ATOM   1211  O  O   . GLN B  1 16  ? 72.987  23.220  29.199  1.00 9.27  ? 15  GLN F O   1 
ATOM   1212  C  CB  . GLN B  1 16  ? 70.893  25.392  30.376  1.00 11.74 ? 15  GLN F CB  1 
ATOM   1213  C  CG  . GLN B  1 16  ? 71.856  25.537  31.545  1.00 15.84 ? 15  GLN F CG  1 
ATOM   1214  C  CD  . GLN B  1 16  ? 72.566  26.875  31.537  1.00 22.16 ? 15  GLN F CD  1 
ATOM   1215  O  OE1 . GLN B  1 16  ? 72.062  27.884  32.036  1.00 23.75 ? 15  GLN F OE1 1 
ATOM   1216  N  NE2 . GLN B  1 16  ? 73.768  26.934  30.944  1.00 23.58 ? 15  GLN F NE2 1 
ATOM   1217  N  N   . GLY B  1 17  ? 72.037  24.509  27.631  1.00 7.99  ? 16  GLY F N   1 
ATOM   1218  C  CA  . GLY B  1 17  ? 73.137  24.410  26.687  1.00 4.00  ? 16  GLY F CA  1 
ATOM   1219  C  C   . GLY B  1 17  ? 72.847  25.247  25.461  1.00 2.00  ? 16  GLY F C   1 
ATOM   1220  O  O   . GLY B  1 17  ? 71.723  25.685  25.277  1.00 2.70  ? 16  GLY F O   1 
ATOM   1221  N  N   . ILE B  1 18  ? 73.792  25.467  24.599  1.00 2.00  ? 17  ILE F N   1 
ATOM   1222  C  CA  . ILE B  1 18  ? 73.601  26.281  23.433  1.00 2.00  ? 17  ILE F CA  1 
ATOM   1223  C  C   . ILE B  1 18  ? 74.052  25.358  22.329  1.00 2.00  ? 17  ILE F C   1 
ATOM   1224  O  O   . ILE B  1 18  ? 75.189  24.892  22.461  1.00 2.00  ? 17  ILE F O   1 
ATOM   1225  C  CB  . ILE B  1 18  ? 74.501  27.539  23.448  1.00 2.00  ? 17  ILE F CB  1 
ATOM   1226  C  CG1 . ILE B  1 18  ? 74.013  28.521  24.498  1.00 2.00  ? 17  ILE F CG1 1 
ATOM   1227  C  CG2 . ILE B  1 18  ? 74.517  28.141  22.048  1.00 2.00  ? 17  ILE F CG2 1 
ATOM   1228  C  CD1 . ILE B  1 18  ? 75.017  29.725  24.662  1.00 2.13  ? 17  ILE F CD1 1 
ATOM   1229  N  N   . ILE B  1 19  ? 73.228  25.146  21.273  1.00 2.00  ? 18  ILE F N   1 
ATOM   1230  C  CA  . ILE B  1 19  ? 73.534  24.260  20.179  1.00 2.00  ? 18  ILE F CA  1 
ATOM   1231  C  C   . ILE B  1 19  ? 73.439  25.086  18.935  1.00 2.00  ? 18  ILE F C   1 
ATOM   1232  O  O   . ILE B  1 19  ? 72.499  25.853  18.778  1.00 3.43  ? 18  ILE F O   1 
ATOM   1233  C  CB  . ILE B  1 19  ? 72.545  23.095  20.156  1.00 2.00  ? 18  ILE F CB  1 
ATOM   1234  C  CG1 . ILE B  1 19  ? 72.688  22.269  21.413  1.00 2.00  ? 18  ILE F CG1 1 
ATOM   1235  C  CG2 . ILE B  1 19  ? 72.798  22.256  18.903  1.00 2.00  ? 18  ILE F CG2 1 
ATOM   1236  C  CD1 . ILE B  1 19  ? 74.015  21.540  21.500  1.00 2.00  ? 18  ILE F CD1 1 
ATOM   1237  N  N   . ASN B  1 20  ? 74.401  24.882  18.057  1.00 2.00  ? 19  ASN F N   1 
ATOM   1238  C  CA  . ASN B  1 20  ? 74.581  25.656  16.860  1.00 2.42  ? 19  ASN F CA  1 
ATOM   1239  C  C   . ASN B  1 20  ? 74.430  24.740  15.671  1.00 3.67  ? 19  ASN F C   1 
ATOM   1240  O  O   . ASN B  1 20  ? 74.891  23.586  15.758  1.00 2.08  ? 19  ASN F O   1 
ATOM   1241  C  CB  . ASN B  1 20  ? 75.946  26.201  16.749  1.00 3.61  ? 19  ASN F CB  1 
ATOM   1242  C  CG  . ASN B  1 20  ? 76.443  26.925  17.970  1.00 6.17  ? 19  ASN F CG  1 
ATOM   1243  O  OD1 . ASN B  1 20  ? 76.275  28.136  18.070  1.00 8.71  ? 19  ASN F OD1 1 
ATOM   1244  N  ND2 . ASN B  1 20  ? 77.066  26.263  18.939  1.00 8.55  ? 19  ASN F ND2 1 
ATOM   1245  N  N   . PHE B  1 21  ? 73.850  25.278  14.580  1.00 2.37  ? 20  PHE F N   1 
ATOM   1246  C  CA  . PHE B  1 21  ? 73.640  24.546  13.333  1.00 2.00  ? 20  PHE F CA  1 
ATOM   1247  C  C   . PHE B  1 21  ? 74.285  25.329  12.234  1.00 2.77  ? 20  PHE F C   1 
ATOM   1248  O  O   . PHE B  1 21  ? 74.036  26.533  12.163  1.00 2.59  ? 20  PHE F O   1 
ATOM   1249  C  CB  . PHE B  1 21  ? 72.210  24.443  12.875  1.00 2.04  ? 20  PHE F CB  1 
ATOM   1250  C  CG  . PHE B  1 21  ? 71.376  23.837  13.951  1.00 2.00  ? 20  PHE F CG  1 
ATOM   1251  C  CD1 . PHE B  1 21  ? 70.923  24.649  14.949  1.00 2.00  ? 20  PHE F CD1 1 
ATOM   1252  C  CD2 . PHE B  1 21  ? 71.198  22.496  13.960  1.00 2.00  ? 20  PHE F CD2 1 
ATOM   1253  C  CE1 . PHE B  1 21  ? 70.242  24.097  15.998  1.00 2.00  ? 20  PHE F CE1 1 
ATOM   1254  C  CE2 . PHE B  1 21  ? 70.513  21.962  15.014  1.00 2.01  ? 20  PHE F CE2 1 
ATOM   1255  C  CZ  . PHE B  1 21  ? 70.058  22.755  16.035  1.00 2.00  ? 20  PHE F CZ  1 
ATOM   1256  N  N   . GLU B  1 22  ? 75.049  24.704  11.346  1.00 3.40  ? 21  GLU F N   1 
ATOM   1257  C  CA  . GLU B  1 22  ? 75.694  25.451  10.274  1.00 4.69  ? 21  GLU F CA  1 
ATOM   1258  C  C   . GLU B  1 22  ? 75.414  24.655  8.987   1.00 5.23  ? 21  GLU F C   1 
ATOM   1259  O  O   . GLU B  1 22  ? 75.558  23.440  9.077   1.00 7.42  ? 21  GLU F O   1 
ATOM   1260  C  CB  . GLU B  1 22  ? 77.135  25.509  10.676  1.00 4.02  ? 21  GLU F CB  1 
ATOM   1261  C  CG  . GLU B  1 22  ? 77.962  26.414  9.783   1.00 12.82 ? 21  GLU F CG  1 
ATOM   1262  C  CD  . GLU B  1 22  ? 79.491  26.541  10.028  1.00 17.37 ? 21  GLU F CD  1 
ATOM   1263  O  OE1 . GLU B  1 22  ? 80.215  25.616  10.449  1.00 20.44 ? 21  GLU F OE1 1 
ATOM   1264  O  OE2 . GLU B  1 22  ? 79.997  27.611  9.704   1.00 22.38 ? 21  GLU F OE2 1 
ATOM   1265  N  N   . GLN B  1 23  ? 74.921  25.192  7.860   1.00 4.17  ? 22  GLN F N   1 
ATOM   1266  C  CA  . GLN B  1 23  ? 74.711  24.540  6.575   1.00 4.03  ? 22  GLN F CA  1 
ATOM   1267  C  C   . GLN B  1 23  ? 75.402  25.464  5.573   1.00 7.77  ? 22  GLN F C   1 
ATOM   1268  O  O   . GLN B  1 23  ? 75.087  26.623  5.331   1.00 7.20  ? 22  GLN F O   1 
ATOM   1269  C  CB  . GLN B  1 23  ? 73.264  24.473  6.245   1.00 2.01  ? 22  GLN F CB  1 
ATOM   1270  C  CG  . GLN B  1 23  ? 73.110  23.386  5.243   1.00 2.00  ? 22  GLN F CG  1 
ATOM   1271  C  CD  . GLN B  1 23  ? 71.668  23.075  4.909   1.00 2.55  ? 22  GLN F CD  1 
ATOM   1272  O  OE1 . GLN B  1 23  ? 70.768  23.884  5.087   1.00 2.13  ? 22  GLN F OE1 1 
ATOM   1273  N  NE2 . GLN B  1 23  ? 71.325  21.897  4.412   1.00 5.46  ? 22  GLN F NE2 1 
ATOM   1274  N  N   . LYS B  1 24  ? 76.419  24.967  4.929   1.00 13.95 ? 23  LYS F N   1 
ATOM   1275  C  CA  . LYS B  1 24  ? 77.278  25.788  4.096   1.00 20.77 ? 23  LYS F CA  1 
ATOM   1276  C  C   . LYS B  1 24  ? 76.668  26.061  2.722   1.00 22.55 ? 23  LYS F C   1 
ATOM   1277  O  O   . LYS B  1 24  ? 76.989  27.067  2.096   1.00 22.63 ? 23  LYS F O   1 
ATOM   1278  C  CB  . LYS B  1 24  ? 78.576  25.020  4.074   1.00 24.18 ? 23  LYS F CB  1 
ATOM   1279  C  CG  . LYS B  1 24  ? 79.864  25.707  3.764   1.00 30.95 ? 23  LYS F CG  1 
ATOM   1280  C  CD  . LYS B  1 24  ? 80.835  24.496  3.874   1.00 36.19 ? 23  LYS F CD  1 
ATOM   1281  C  CE  . LYS B  1 24  ? 82.068  24.674  2.994   1.00 37.40 ? 23  LYS F CE  1 
ATOM   1282  N  NZ  . LYS B  1 24  ? 82.979  23.594  3.290   1.00 39.87 ? 23  LYS F NZ  1 
ATOM   1283  N  N   . GLU B  1 25  ? 75.851  25.129  2.206   1.00 25.65 ? 24  GLU F N   1 
ATOM   1284  C  CA  . GLU B  1 25  ? 75.047  25.291  0.997   1.00 27.83 ? 24  GLU F CA  1 
ATOM   1285  C  C   . GLU B  1 25  ? 73.812  24.461  1.272   1.00 28.13 ? 24  GLU F C   1 
ATOM   1286  O  O   . GLU B  1 25  ? 73.907  23.452  1.981   1.00 27.14 ? 24  GLU F O   1 
ATOM   1287  C  CB  . GLU B  1 25  ? 75.711  24.754  -0.288  1.00 32.85 ? 24  GLU F CB  1 
ATOM   1288  C  CG  . GLU B  1 25  ? 76.172  23.299  -0.387  1.00 36.70 ? 24  GLU F CG  1 
ATOM   1289  C  CD  . GLU B  1 25  ? 77.588  23.016  0.095   1.00 38.01 ? 24  GLU F CD  1 
ATOM   1290  O  OE1 . GLU B  1 25  ? 78.500  23.760  -0.273  1.00 39.11 ? 24  GLU F OE1 1 
ATOM   1291  O  OE2 . GLU B  1 25  ? 77.788  22.025  0.806   1.00 41.22 ? 24  GLU F OE2 1 
ATOM   1292  N  N   . SER B  1 26  ? 72.680  24.852  0.694   1.00 29.68 ? 25  SER F N   1 
ATOM   1293  C  CA  . SER B  1 26  ? 71.321  24.336  0.967   1.00 31.77 ? 25  SER F CA  1 
ATOM   1294  C  C   . SER B  1 26  ? 70.976  22.854  0.768   1.00 30.95 ? 25  SER F C   1 
ATOM   1295  O  O   . SER B  1 26  ? 69.914  22.324  1.108   1.00 32.61 ? 25  SER F O   1 
ATOM   1296  C  CB  . SER B  1 26  ? 70.359  25.215  0.136   1.00 33.47 ? 25  SER F CB  1 
ATOM   1297  O  OG  . SER B  1 26  ? 70.896  25.544  -1.156  1.00 36.91 ? 25  SER F OG  1 
ATOM   1298  N  N   . ASN B  1 27  ? 71.902  22.229  0.090   1.00 28.85 ? 26  ASN F N   1 
ATOM   1299  C  CA  . ASN B  1 27  ? 71.892  20.826  -0.261  1.00 28.71 ? 26  ASN F CA  1 
ATOM   1300  C  C   . ASN B  1 27  ? 72.869  20.029  0.612   1.00 27.27 ? 26  ASN F C   1 
ATOM   1301  O  O   . ASN B  1 27  ? 72.935  18.801  0.603   1.00 27.07 ? 26  ASN F O   1 
ATOM   1302  C  CB  . ASN B  1 27  ? 72.274  20.733  -1.754  1.00 31.54 ? 26  ASN F CB  1 
ATOM   1303  C  CG  . ASN B  1 27  ? 73.433  21.645  -2.189  1.00 31.75 ? 26  ASN F CG  1 
ATOM   1304  O  OD1 . ASN B  1 27  ? 73.271  22.865  -2.116  1.00 33.46 ? 26  ASN F OD1 1 
ATOM   1305  N  ND2 . ASN B  1 27  ? 74.621  21.199  -2.597  1.00 31.68 ? 26  ASN F ND2 1 
ATOM   1306  N  N   . GLY B  1 28  ? 73.681  20.764  1.370   1.00 25.84 ? 27  GLY F N   1 
ATOM   1307  C  CA  . GLY B  1 28  ? 74.727  20.225  2.188   1.00 18.98 ? 27  GLY F CA  1 
ATOM   1308  C  C   . GLY B  1 28  ? 74.182  19.579  3.464   1.00 16.43 ? 27  GLY F C   1 
ATOM   1309  O  O   . GLY B  1 28  ? 73.019  19.716  3.899   1.00 14.51 ? 27  GLY F O   1 
ATOM   1310  N  N   . PRO B  1 29  ? 75.098  18.850  4.090   1.00 11.80 ? 28  PRO F N   1 
ATOM   1311  C  CA  . PRO B  1 29  ? 74.938  18.410  5.453   1.00 9.19  ? 28  PRO F CA  1 
ATOM   1312  C  C   . PRO B  1 29  ? 74.935  19.634  6.363   1.00 6.75  ? 28  PRO F C   1 
ATOM   1313  O  O   . PRO B  1 29  ? 75.490  20.673  5.982   1.00 4.79  ? 28  PRO F O   1 
ATOM   1314  C  CB  . PRO B  1 29  ? 76.102  17.486  5.609   1.00 9.86  ? 28  PRO F CB  1 
ATOM   1315  C  CG  . PRO B  1 29  ? 77.143  18.282  4.865   1.00 11.57 ? 28  PRO F CG  1 
ATOM   1316  C  CD  . PRO B  1 29  ? 76.418  18.550  3.575   1.00 7.83  ? 28  PRO F CD  1 
ATOM   1317  N  N   . VAL B  1 30  ? 74.292  19.563  7.518   1.00 4.85  ? 29  VAL F N   1 
ATOM   1318  C  CA  . VAL B  1 30  ? 74.347  20.681  8.430   1.00 5.46  ? 29  VAL F CA  1 
ATOM   1319  C  C   . VAL B  1 30  ? 75.105  20.109  9.609   1.00 6.58  ? 29  VAL F C   1 
ATOM   1320  O  O   . VAL B  1 30  ? 74.928  18.919  9.891   1.00 6.16  ? 29  VAL F O   1 
ATOM   1321  C  CB  . VAL B  1 30  ? 72.884  21.232  8.807   1.00 2.00  ? 29  VAL F CB  1 
ATOM   1322  C  CG1 . VAL B  1 30  ? 71.828  20.517  8.008   1.00 2.00  ? 29  VAL F CG1 1 
ATOM   1323  C  CG2 . VAL B  1 30  ? 72.605  21.123  10.274  1.00 2.00  ? 29  VAL F CG2 1 
ATOM   1324  N  N   . LYS B  1 31  ? 75.992  20.882  10.259  1.00 7.35  ? 30  LYS F N   1 
ATOM   1325  C  CA  . LYS B  1 31  ? 76.746  20.420  11.417  1.00 7.50  ? 30  LYS F CA  1 
ATOM   1326  C  C   . LYS B  1 31  ? 76.072  20.942  12.665  1.00 5.90  ? 30  LYS F C   1 
ATOM   1327  O  O   . LYS B  1 31  ? 75.728  22.138  12.686  1.00 5.53  ? 30  LYS F O   1 
ATOM   1328  C  CB  . LYS B  1 31  ? 78.138  20.964  11.446  1.00 10.65 ? 30  LYS F CB  1 
ATOM   1329  C  CG  . LYS B  1 31  ? 78.949  20.629  10.241  1.00 18.88 ? 30  LYS F CG  1 
ATOM   1330  C  CD  . LYS B  1 31  ? 80.383  20.994  10.544  1.00 25.91 ? 30  LYS F CD  1 
ATOM   1331  C  CE  . LYS B  1 31  ? 81.219  20.842  9.263   1.00 30.67 ? 30  LYS F CE  1 
ATOM   1332  N  NZ  . LYS B  1 31  ? 82.621  21.219  9.487   1.00 34.60 ? 30  LYS F NZ  1 
ATOM   1333  N  N   . VAL B  1 32  ? 75.873  20.130  13.706  1.00 3.92  ? 31  VAL F N   1 
ATOM   1334  C  CA  . VAL B  1 32  ? 75.268  20.689  14.883  1.00 2.51  ? 31  VAL F CA  1 
ATOM   1335  C  C   . VAL B  1 32  ? 76.279  20.473  15.965  1.00 2.00  ? 31  VAL F C   1 
ATOM   1336  O  O   . VAL B  1 32  ? 76.723  19.360  16.162  1.00 2.05  ? 31  VAL F O   1 
ATOM   1337  C  CB  . VAL B  1 32  ? 73.818  20.049  15.146  1.00 4.02  ? 31  VAL F CB  1 
ATOM   1338  C  CG1 . VAL B  1 32  ? 73.541  19.018  14.085  1.00 4.65  ? 31  VAL F CG1 1 
ATOM   1339  C  CG2 . VAL B  1 32  ? 73.631  19.531  16.547  1.00 2.00  ? 31  VAL F CG2 1 
ATOM   1340  N  N   . TRP B  1 33  ? 76.800  21.546  16.565  1.00 2.24  ? 32  TRP F N   1 
ATOM   1341  C  CA  . TRP B  1 33  ? 77.782  21.439  17.628  1.00 2.00  ? 32  TRP F CA  1 
ATOM   1342  C  C   . TRP B  1 33  ? 77.415  22.312  18.841  1.00 2.00  ? 32  TRP F C   1 
ATOM   1343  O  O   . TRP B  1 33  ? 76.699  23.308  18.681  1.00 2.00  ? 32  TRP F O   1 
ATOM   1344  C  CB  . TRP B  1 33  ? 79.148  21.822  17.077  1.00 2.00  ? 32  TRP F CB  1 
ATOM   1345  C  CG  . TRP B  1 33  ? 79.494  23.298  16.918  1.00 2.91  ? 32  TRP F CG  1 
ATOM   1346  C  CD1 . TRP B  1 33  ? 80.192  23.996  17.887  1.00 7.07  ? 32  TRP F CD1 1 
ATOM   1347  C  CD2 . TRP B  1 33  ? 79.205  24.080  15.846  1.00 3.51  ? 32  TRP F CD2 1 
ATOM   1348  N  NE1 . TRP B  1 33  ? 80.320  25.233  17.428  1.00 9.12  ? 32  TRP F NE1 1 
ATOM   1349  C  CE2 . TRP B  1 33  ? 79.736  25.296  16.218  1.00 7.08  ? 32  TRP F CE2 1 
ATOM   1350  C  CE3 . TRP B  1 33  ? 78.548  23.919  14.659  1.00 4.70  ? 32  TRP F CE3 1 
ATOM   1351  C  CZ2 . TRP B  1 33  ? 79.626  26.370  15.396  1.00 3.87  ? 32  TRP F CZ2 1 
ATOM   1352  C  CZ3 . TRP B  1 33  ? 78.440  24.993  13.828  1.00 2.72  ? 32  TRP F CZ3 1 
ATOM   1353  C  CH2 . TRP B  1 33  ? 78.987  26.197  14.187  1.00 4.04  ? 32  TRP F CH2 1 
ATOM   1354  N  N   . GLY B  1 34  ? 77.827  22.004  20.073  1.00 2.00  ? 33  GLY F N   1 
ATOM   1355  C  CA  . GLY B  1 34  ? 77.529  22.870  21.195  1.00 2.00  ? 33  GLY F CA  1 
ATOM   1356  C  C   . GLY B  1 34  ? 77.697  22.219  22.554  1.00 2.00  ? 33  GLY F C   1 
ATOM   1357  O  O   . GLY B  1 34  ? 78.314  21.183  22.634  1.00 2.83  ? 33  GLY F O   1 
ATOM   1358  N  N   . SER B  1 35  ? 77.172  22.712  23.657  1.00 2.00  ? 34  SER F N   1 
ATOM   1359  C  CA  . SER B  1 35  ? 77.342  22.070  24.927  1.00 3.06  ? 34  SER F CA  1 
ATOM   1360  C  C   . SER B  1 35  ? 76.003  21.966  25.559  1.00 4.75  ? 34  SER F C   1 
ATOM   1361  O  O   . SER B  1 35  ? 75.251  22.916  25.466  1.00 5.93  ? 34  SER F O   1 
ATOM   1362  C  CB  . SER B  1 35  ? 78.154  22.834  25.919  1.00 2.00  ? 34  SER F CB  1 
ATOM   1363  O  OG  . SER B  1 35  ? 79.530  22.727  25.624  1.00 4.15  ? 34  SER F OG  1 
ATOM   1364  N  N   . ILE B  1 36  ? 75.660  20.819  26.132  1.00 7.79  ? 35  ILE F N   1 
ATOM   1365  C  CA  . ILE B  1 36  ? 74.483  20.708  26.969  1.00 6.04  ? 35  ILE F CA  1 
ATOM   1366  C  C   . ILE B  1 36  ? 75.104  20.303  28.306  1.00 5.37  ? 35  ILE F C   1 
ATOM   1367  O  O   . ILE B  1 36  ? 76.096  19.577  28.321  1.00 4.22  ? 35  ILE F O   1 
ATOM   1368  C  CB  . ILE B  1 36  ? 73.562  19.663  26.406  1.00 3.74  ? 35  ILE F CB  1 
ATOM   1369  C  CG1 . ILE B  1 36  ? 73.146  19.897  24.962  1.00 2.00  ? 35  ILE F CG1 1 
ATOM   1370  C  CG2 . ILE B  1 36  ? 72.351  19.761  27.258  1.00 5.55  ? 35  ILE F CG2 1 
ATOM   1371  C  CD1 . ILE B  1 36  ? 72.561  18.593  24.427  1.00 5.22  ? 35  ILE F CD1 1 
ATOM   1372  N  N   . LYS B  1 37  ? 74.558  20.831  29.408  1.00 8.14  ? 36  LYS F N   1 
ATOM   1373  C  CA  . LYS B  1 37  ? 75.010  20.753  30.806  1.00 7.52  ? 36  LYS F CA  1 
ATOM   1374  C  C   . LYS B  1 37  ? 73.911  20.331  31.746  1.00 5.89  ? 36  LYS F C   1 
ATOM   1375  O  O   . LYS B  1 37  ? 72.724  20.589  31.551  1.00 5.60  ? 36  LYS F O   1 
ATOM   1376  C  CB  . LYS B  1 37  ? 75.473  22.108  31.310  1.00 12.40 ? 36  LYS F CB  1 
ATOM   1377  C  CG  . LYS B  1 37  ? 76.813  22.307  30.682  1.00 20.22 ? 36  LYS F CG  1 
ATOM   1378  C  CD  . LYS B  1 37  ? 77.494  23.603  31.032  1.00 26.86 ? 36  LYS F CD  1 
ATOM   1379  C  CE  . LYS B  1 37  ? 78.877  23.558  30.361  1.00 29.90 ? 36  LYS F CE  1 
ATOM   1380  N  NZ  . LYS B  1 37  ? 78.746  23.363  28.919  1.00 32.51 ? 36  LYS F NZ  1 
ATOM   1381  N  N   . GLY B  1 38  ? 74.307  19.731  32.840  1.00 4.66  ? 37  GLY F N   1 
ATOM   1382  C  CA  . GLY B  1 38  ? 73.347  19.296  33.812  1.00 3.83  ? 37  GLY F CA  1 
ATOM   1383  C  C   . GLY B  1 38  ? 72.763  17.961  33.441  1.00 4.05  ? 37  GLY F C   1 
ATOM   1384  O  O   . GLY B  1 38  ? 71.751  17.552  34.024  1.00 6.59  ? 37  GLY F O   1 
ATOM   1385  N  N   . LEU B  1 39  ? 73.341  17.260  32.464  1.00 5.87  ? 38  LEU F N   1 
ATOM   1386  C  CA  . LEU B  1 39  ? 72.742  16.000  32.075  1.00 5.67  ? 38  LEU F CA  1 
ATOM   1387  C  C   . LEU B  1 39  ? 73.274  14.979  33.032  1.00 4.63  ? 38  LEU F C   1 
ATOM   1388  O  O   . LEU B  1 39  ? 74.268  15.224  33.706  1.00 5.92  ? 38  LEU F O   1 
ATOM   1389  C  CB  . LEU B  1 39  ? 73.133  15.516  30.669  1.00 5.24  ? 38  LEU F CB  1 
ATOM   1390  C  CG  . LEU B  1 39  ? 72.536  16.068  29.393  1.00 4.35  ? 38  LEU F CG  1 
ATOM   1391  C  CD1 . LEU B  1 39  ? 71.290  16.894  29.616  1.00 2.00  ? 38  LEU F CD1 1 
ATOM   1392  C  CD2 . LEU B  1 39  ? 73.589  16.931  28.799  1.00 2.00  ? 38  LEU F CD2 1 
ATOM   1393  N  N   . THR B  1 40  ? 72.607  13.849  33.137  1.00 5.15  ? 39  THR F N   1 
ATOM   1394  C  CA  . THR B  1 40  ? 73.224  12.723  33.793  1.00 2.58  ? 39  THR F CA  1 
ATOM   1395  C  C   . THR B  1 40  ? 74.128  12.105  32.744  1.00 2.00  ? 39  THR F C   1 
ATOM   1396  O  O   . THR B  1 40  ? 73.845  12.138  31.554  1.00 2.00  ? 39  THR F O   1 
ATOM   1397  C  CB  . THR B  1 40  ? 72.144  11.762  34.220  1.00 2.39  ? 39  THR F CB  1 
ATOM   1398  O  OG1 . THR B  1 40  ? 71.541  11.259  33.019  1.00 12.97 ? 39  THR F OG1 1 
ATOM   1399  C  CG2 . THR B  1 40  ? 71.090  12.425  35.074  1.00 2.00  ? 39  THR F CG2 1 
ATOM   1400  N  N   . GLU B  1 41  ? 75.217  11.546  33.173  1.00 2.02  ? 40  GLU F N   1 
ATOM   1401  C  CA  . GLU B  1 41  ? 76.113  10.742  32.388  1.00 3.59  ? 40  GLU F CA  1 
ATOM   1402  C  C   . GLU B  1 41  ? 75.380  9.706   31.521  1.00 3.08  ? 40  GLU F C   1 
ATOM   1403  O  O   . GLU B  1 41  ? 74.324  9.194   31.907  1.00 2.95  ? 40  GLU F O   1 
ATOM   1404  C  CB  . GLU B  1 41  ? 77.029  10.059  33.349  1.00 2.55  ? 40  GLU F CB  1 
ATOM   1405  C  CG  . GLU B  1 41  ? 78.209  9.423   32.664  1.00 11.46 ? 40  GLU F CG  1 
ATOM   1406  C  CD  . GLU B  1 41  ? 79.190  8.630   33.500  1.00 14.83 ? 40  GLU F CD  1 
ATOM   1407  O  OE1 . GLU B  1 41  ? 79.074  8.653   34.734  1.00 16.74 ? 40  GLU F OE1 1 
ATOM   1408  O  OE2 . GLU B  1 41  ? 80.056  7.977   32.887  1.00 17.82 ? 40  GLU F OE2 1 
ATOM   1409  N  N   . GLY B  1 42  ? 75.906  9.406   30.337  1.00 2.00  ? 41  GLY F N   1 
ATOM   1410  C  CA  . GLY B  1 42  ? 75.277  8.472   29.449  1.00 2.00  ? 41  GLY F CA  1 
ATOM   1411  C  C   . GLY B  1 42  ? 74.583  9.113   28.278  1.00 2.00  ? 41  GLY F C   1 
ATOM   1412  O  O   . GLY B  1 42  ? 74.618  10.307  27.981  1.00 4.18  ? 41  GLY F O   1 
ATOM   1413  N  N   . LEU B  1 43  ? 73.873  8.233   27.621  1.00 3.59  ? 42  LEU F N   1 
ATOM   1414  C  CA  . LEU B  1 43  ? 73.120  8.513   26.409  1.00 2.64  ? 42  LEU F CA  1 
ATOM   1415  C  C   . LEU B  1 43  ? 71.813  9.263   26.547  1.00 2.00  ? 42  LEU F C   1 
ATOM   1416  O  O   . LEU B  1 43  ? 71.039  8.870   27.397  1.00 2.00  ? 42  LEU F O   1 
ATOM   1417  C  CB  . LEU B  1 43  ? 72.965  7.156   25.805  1.00 2.00  ? 42  LEU F CB  1 
ATOM   1418  C  CG  . LEU B  1 43  ? 73.542  6.918   24.452  1.00 2.00  ? 42  LEU F CG  1 
ATOM   1419  C  CD1 . LEU B  1 43  ? 74.888  7.499   24.273  1.00 5.33  ? 42  LEU F CD1 1 
ATOM   1420  C  CD2 . LEU B  1 43  ? 73.610  5.473   24.295  1.00 2.74  ? 42  LEU F CD2 1 
ATOM   1421  N  N   . HIS B  1 44  ? 71.475  10.324  25.811  1.00 2.80  ? 43  HIS F N   1 
ATOM   1422  C  CA  . HIS B  1 44  ? 70.199  11.094  25.926  1.00 2.59  ? 43  HIS F CA  1 
ATOM   1423  C  C   . HIS B  1 44  ? 69.616  11.386  24.561  1.00 2.24  ? 43  HIS F C   1 
ATOM   1424  O  O   . HIS B  1 44  ? 70.352  11.866  23.719  1.00 2.00  ? 43  HIS F O   1 
ATOM   1425  C  CB  . HIS B  1 44  ? 70.394  12.442  26.603  1.00 2.00  ? 43  HIS F CB  1 
ATOM   1426  C  CG  . HIS B  1 44  ? 70.653  12.353  28.108  1.00 3.93  ? 43  HIS F CG  1 
ATOM   1427  N  ND1 . HIS B  1 44  ? 69.768  12.355  29.092  1.00 2.87  ? 43  HIS F ND1 1 
ATOM   1428  C  CD2 . HIS B  1 44  ? 71.894  12.268  28.706  1.00 2.44  ? 43  HIS F CD2 1 
ATOM   1429  C  CE1 . HIS B  1 44  ? 70.395  12.285  30.243  1.00 2.00  ? 43  HIS F CE1 1 
ATOM   1430  N  NE2 . HIS B  1 44  ? 71.662  12.232  30.000  1.00 2.00  ? 43  HIS F NE2 1 
ATOM   1431  N  N   . GLY B  1 45  ? 68.366  11.076  24.257  1.00 2.00  ? 44  GLY F N   1 
ATOM   1432  C  CA  . GLY B  1 45  ? 67.792  11.341  22.956  1.00 2.00  ? 44  GLY F CA  1 
ATOM   1433  C  C   . GLY B  1 45  ? 67.777  12.819  22.644  1.00 2.32  ? 44  GLY F C   1 
ATOM   1434  O  O   . GLY B  1 45  ? 67.541  13.614  23.545  1.00 3.47  ? 44  GLY F O   1 
ATOM   1435  N  N   . PHE B  1 46  ? 67.964  13.207  21.393  1.00 2.71  ? 45  PHE F N   1 
ATOM   1436  C  CA  . PHE B  1 46  ? 68.153  14.590  20.976  1.00 3.56  ? 45  PHE F CA  1 
ATOM   1437  C  C   . PHE B  1 46  ? 67.389  14.719  19.655  1.00 4.50  ? 45  PHE F C   1 
ATOM   1438  O  O   . PHE B  1 46  ? 67.738  14.020  18.682  1.00 5.89  ? 45  PHE F O   1 
ATOM   1439  C  CB  . PHE B  1 46  ? 69.662  14.752  20.817  1.00 3.40  ? 45  PHE F CB  1 
ATOM   1440  C  CG  . PHE B  1 46  ? 70.285  16.072  20.391  1.00 2.00  ? 45  PHE F CG  1 
ATOM   1441  C  CD1 . PHE B  1 46  ? 70.455  17.090  21.288  1.00 2.00  ? 45  PHE F CD1 1 
ATOM   1442  C  CD2 . PHE B  1 46  ? 70.750  16.205  19.124  1.00 2.00  ? 45  PHE F CD2 1 
ATOM   1443  C  CE1 . PHE B  1 46  ? 71.080  18.235  20.893  1.00 2.00  ? 45  PHE F CE1 1 
ATOM   1444  C  CE2 . PHE B  1 46  ? 71.375  17.362  18.745  1.00 2.00  ? 45  PHE F CE2 1 
ATOM   1445  C  CZ  . PHE B  1 46  ? 71.553  18.384  19.630  1.00 2.00  ? 45  PHE F CZ  1 
ATOM   1446  N  N   . HIS B  1 47  ? 66.323  15.525  19.555  1.00 2.00  ? 46  HIS F N   1 
ATOM   1447  C  CA  . HIS B  1 47  ? 65.502  15.541  18.375  1.00 2.00  ? 46  HIS F CA  1 
ATOM   1448  C  C   . HIS B  1 47  ? 64.984  16.930  18.117  1.00 2.35  ? 46  HIS F C   1 
ATOM   1449  O  O   . HIS B  1 47  ? 64.946  17.791  19.004  1.00 2.00  ? 46  HIS F O   1 
ATOM   1450  C  CB  . HIS B  1 47  ? 64.256  14.709  18.486  1.00 2.00  ? 46  HIS F CB  1 
ATOM   1451  C  CG  . HIS B  1 47  ? 64.442  13.362  19.120  1.00 3.26  ? 46  HIS F CG  1 
ATOM   1452  N  ND1 . HIS B  1 47  ? 63.903  12.898  20.255  1.00 2.90  ? 46  HIS F ND1 1 
ATOM   1453  C  CD2 . HIS B  1 47  ? 65.286  12.406  18.612  1.00 2.27  ? 46  HIS F CD2 1 
ATOM   1454  C  CE1 . HIS B  1 47  ? 64.403  11.696  20.441  1.00 4.50  ? 46  HIS F CE1 1 
ATOM   1455  N  NE2 . HIS B  1 47  ? 65.233  11.416  19.455  1.00 2.00  ? 46  HIS F NE2 1 
ATOM   1456  N  N   . VAL B  1 48  ? 64.535  17.106  16.866  1.00 2.00  ? 47  VAL F N   1 
ATOM   1457  C  CA  . VAL B  1 48  ? 63.885  18.310  16.505  1.00 2.00  ? 47  VAL F CA  1 
ATOM   1458  C  C   . VAL B  1 48  ? 62.428  17.930  16.482  1.00 2.00  ? 47  VAL F C   1 
ATOM   1459  O  O   . VAL B  1 48  ? 61.969  16.921  15.953  1.00 2.00  ? 47  VAL F O   1 
ATOM   1460  C  CB  . VAL B  1 48  ? 64.485  18.768  15.169  1.00 4.37  ? 47  VAL F CB  1 
ATOM   1461  C  CG1 . VAL B  1 48  ? 63.650  19.847  14.556  1.00 2.00  ? 47  VAL F CG1 1 
ATOM   1462  C  CG2 . VAL B  1 48  ? 65.828  19.447  15.415  1.00 2.00  ? 47  VAL F CG2 1 
ATOM   1463  N  N   . HIS B  1 49  ? 61.651  18.696  17.195  1.00 2.00  ? 48  HIS F N   1 
ATOM   1464  C  CA  . HIS B  1 49  ? 60.241  18.403  17.344  1.00 2.73  ? 48  HIS F CA  1 
ATOM   1465  C  C   . HIS B  1 49  ? 59.505  19.378  16.454  1.00 2.54  ? 48  HIS F C   1 
ATOM   1466  O  O   . HIS B  1 49  ? 60.072  20.386  16.072  1.00 3.69  ? 48  HIS F O   1 
ATOM   1467  C  CB  . HIS B  1 49  ? 59.857  18.527  18.818  1.00 2.00  ? 48  HIS F CB  1 
ATOM   1468  C  CG  . HIS B  1 49  ? 60.164  17.268  19.617  1.00 2.00  ? 48  HIS F CG  1 
ATOM   1469  N  ND1 . HIS B  1 49  ? 59.348  16.584  20.349  1.00 2.00  ? 48  HIS F ND1 1 
ATOM   1470  C  CD2 . HIS B  1 49  ? 61.387  16.660  19.737  1.00 2.00  ? 48  HIS F CD2 1 
ATOM   1471  C  CE1 . HIS B  1 49  ? 60.060  15.617  20.885  1.00 2.00  ? 48  HIS F CE1 1 
ATOM   1472  N  NE2 . HIS B  1 49  ? 61.327  15.634  20.529  1.00 2.00  ? 48  HIS F NE2 1 
ATOM   1473  N  N   . GLU B  1 50  ? 58.288  19.092  16.080  1.00 2.00  ? 49  GLU F N   1 
ATOM   1474  C  CA  . GLU B  1 50  ? 57.592  19.822  15.096  1.00 2.00  ? 49  GLU F CA  1 
ATOM   1475  C  C   . GLU B  1 50  ? 57.387  21.296  15.294  1.00 2.45  ? 49  GLU F C   1 
ATOM   1476  O  O   . GLU B  1 50  ? 57.722  22.033  14.393  1.00 2.00  ? 49  GLU F O   1 
ATOM   1477  C  CB  . GLU B  1 50  ? 56.288  19.159  14.936  1.00 2.00  ? 49  GLU F CB  1 
ATOM   1478  C  CG  . GLU B  1 50  ? 55.791  19.553  13.576  1.00 5.30  ? 49  GLU F CG  1 
ATOM   1479  C  CD  . GLU B  1 50  ? 54.667  18.734  12.984  1.00 6.64  ? 49  GLU F CD  1 
ATOM   1480  O  OE1 . GLU B  1 50  ? 54.609  17.499  13.150  1.00 8.48  ? 49  GLU F OE1 1 
ATOM   1481  O  OE2 . GLU B  1 50  ? 53.889  19.381  12.292  1.00 6.00  ? 49  GLU F OE2 1 
ATOM   1482  N  N   . PHE B  1 51  ? 56.861  21.749  16.430  1.00 2.58  ? 50  PHE F N   1 
ATOM   1483  C  CA  . PHE B  1 51  ? 56.470  23.116  16.636  1.00 2.00  ? 50  PHE F CA  1 
ATOM   1484  C  C   . PHE B  1 51  ? 57.471  23.846  17.443  1.00 2.38  ? 50  PHE F C   1 
ATOM   1485  O  O   . PHE B  1 51  ? 58.096  23.271  18.321  1.00 2.00  ? 50  PHE F O   1 
ATOM   1486  C  CB  . PHE B  1 51  ? 55.122  23.209  17.358  1.00 2.00  ? 50  PHE F CB  1 
ATOM   1487  C  CG  . PHE B  1 51  ? 54.121  22.293  16.686  1.00 2.00  ? 50  PHE F CG  1 
ATOM   1488  C  CD1 . PHE B  1 51  ? 53.666  22.590  15.416  1.00 2.00  ? 50  PHE F CD1 1 
ATOM   1489  C  CD2 . PHE B  1 51  ? 53.759  21.106  17.311  1.00 3.73  ? 50  PHE F CD2 1 
ATOM   1490  C  CE1 . PHE B  1 51  ? 52.847  21.689  14.776  1.00 2.00  ? 50  PHE F CE1 1 
ATOM   1491  C  CE2 . PHE B  1 51  ? 52.936  20.198  16.671  1.00 3.95  ? 50  PHE F CE2 1 
ATOM   1492  C  CZ  . PHE B  1 51  ? 52.485  20.488  15.397  1.00 3.91  ? 50  PHE F CZ  1 
ATOM   1493  N  N   . GLY B  1 52  ? 57.592  25.139  17.126  1.00 5.56  ? 51  GLY F N   1 
ATOM   1494  C  CA  . GLY B  1 52  ? 58.443  26.080  17.856  1.00 4.20  ? 51  GLY F CA  1 
ATOM   1495  C  C   . GLY B  1 52  ? 57.609  26.796  18.869  1.00 3.11  ? 51  GLY F C   1 
ATOM   1496  O  O   . GLY B  1 52  ? 57.609  28.014  18.970  1.00 4.07  ? 51  GLY F O   1 
ATOM   1497  N  N   . ASP B  1 53  ? 56.929  26.033  19.675  1.00 2.00  ? 52  ASP F N   1 
ATOM   1498  C  CA  . ASP B  1 53  ? 55.964  26.610  20.539  1.00 2.85  ? 52  ASP F CA  1 
ATOM   1499  C  C   . ASP B  1 53  ? 56.387  26.238  21.911  1.00 4.60  ? 52  ASP F C   1 
ATOM   1500  O  O   . ASP B  1 53  ? 56.289  25.072  22.315  1.00 5.22  ? 52  ASP F O   1 
ATOM   1501  C  CB  . ASP B  1 53  ? 54.638  26.017  20.182  1.00 2.78  ? 52  ASP F CB  1 
ATOM   1502  C  CG  . ASP B  1 53  ? 53.458  26.513  20.974  1.00 3.34  ? 52  ASP F CG  1 
ATOM   1503  O  OD1 . ASP B  1 53  ? 53.600  26.770  22.155  1.00 2.00  ? 52  ASP F OD1 1 
ATOM   1504  O  OD2 . ASP B  1 53  ? 52.382  26.618  20.397  1.00 7.39  ? 52  ASP F OD2 1 
ATOM   1505  N  N   . ASN B  1 54  ? 56.836  27.201  22.658  1.00 6.41  ? 53  ASN F N   1 
ATOM   1506  C  CA  . ASN B  1 54  ? 57.185  26.886  24.015  1.00 10.25 ? 53  ASN F CA  1 
ATOM   1507  C  C   . ASN B  1 54  ? 56.195  27.547  24.953  1.00 10.49 ? 53  ASN F C   1 
ATOM   1508  O  O   . ASN B  1 54  ? 56.565  28.069  25.998  1.00 12.04 ? 53  ASN F O   1 
ATOM   1509  C  CB  . ASN B  1 54  ? 58.616  27.342  24.300  1.00 13.52 ? 53  ASN F CB  1 
ATOM   1510  C  CG  . ASN B  1 54  ? 59.687  26.407  23.756  1.00 20.45 ? 53  ASN F CG  1 
ATOM   1511  O  OD1 . ASN B  1 54  ? 60.864  26.786  23.791  1.00 24.86 ? 53  ASN F OD1 1 
ATOM   1512  N  ND2 . ASN B  1 54  ? 59.458  25.181  23.250  1.00 20.83 ? 53  ASN F ND2 1 
ATOM   1513  N  N   . THR B  1 55  ? 54.905  27.556  24.662  1.00 9.25  ? 54  THR F N   1 
ATOM   1514  C  CA  . THR B  1 55  ? 53.979  28.164  25.604  1.00 11.31 ? 54  THR F CA  1 
ATOM   1515  C  C   . THR B  1 55  ? 53.779  27.222  26.803  1.00 13.37 ? 54  THR F C   1 
ATOM   1516  O  O   . THR B  1 55  ? 53.595  27.673  27.937  1.00 15.31 ? 54  THR F O   1 
ATOM   1517  C  CB  . THR B  1 55  ? 52.636  28.456  24.914  1.00 10.02 ? 54  THR F CB  1 
ATOM   1518  O  OG1 . THR B  1 55  ? 52.214  27.232  24.322  1.00 11.58 ? 54  THR F OG1 1 
ATOM   1519  C  CG2 . THR B  1 55  ? 52.750  29.566  23.878  1.00 10.52 ? 54  THR F CG2 1 
ATOM   1520  N  N   . ALA B  1 56  ? 53.846  25.907  26.620  1.00 10.51 ? 55  ALA F N   1 
ATOM   1521  C  CA  . ALA B  1 56  ? 53.682  25.025  27.731  1.00 7.94  ? 55  ALA F CA  1 
ATOM   1522  C  C   . ALA B  1 56  ? 54.987  24.322  27.944  1.00 11.16 ? 55  ALA F C   1 
ATOM   1523  O  O   . ALA B  1 56  ? 54.981  23.149  28.320  1.00 14.71 ? 55  ALA F O   1 
ATOM   1524  C  CB  . ALA B  1 56  ? 52.611  24.021  27.436  1.00 6.60  ? 55  ALA F CB  1 
ATOM   1525  N  N   . GLY B  1 57  ? 56.121  25.018  27.770  1.00 11.63 ? 56  GLY F N   1 
ATOM   1526  C  CA  . GLY B  1 57  ? 57.424  24.422  27.953  1.00 10.35 ? 56  GLY F CA  1 
ATOM   1527  C  C   . GLY B  1 57  ? 57.748  23.486  26.797  1.00 13.37 ? 56  GLY F C   1 
ATOM   1528  O  O   . GLY B  1 57  ? 57.364  23.739  25.639  1.00 16.06 ? 56  GLY F O   1 
ATOM   1529  N  N   . CYS B  1 58  ? 58.429  22.368  27.091  1.00 12.19 ? 57  CYS F N   1 
ATOM   1530  C  CA  . CYS B  1 58  ? 58.823  21.474  26.034  1.00 8.74  ? 57  CYS F CA  1 
ATOM   1531  C  C   . CYS B  1 58  ? 57.632  20.693  25.546  1.00 9.55  ? 57  CYS F C   1 
ATOM   1532  O  O   . CYS B  1 58  ? 57.669  20.238  24.393  1.00 9.83  ? 57  CYS F O   1 
ATOM   1533  C  CB  . CYS B  1 58  ? 59.886  20.522  26.512  1.00 7.71  ? 57  CYS F CB  1 
ATOM   1534  S  SG  . CYS B  1 58  ? 61.287  21.524  27.058  1.00 6.50  ? 57  CYS F SG  1 
ATOM   1535  N  N   . THR B  1 59  ? 56.547  20.595  26.326  1.00 6.16  ? 58  THR F N   1 
ATOM   1536  C  CA  . THR B  1 59  ? 55.431  19.770  25.899  1.00 6.73  ? 58  THR F CA  1 
ATOM   1537  C  C   . THR B  1 59  ? 54.663  20.309  24.701  1.00 5.74  ? 58  THR F C   1 
ATOM   1538  O  O   . THR B  1 59  ? 54.201  19.541  23.855  1.00 6.30  ? 58  THR F O   1 
ATOM   1539  C  CB  . THR B  1 59  ? 54.459  19.565  27.059  1.00 7.51  ? 58  THR F CB  1 
ATOM   1540  O  OG1 . THR B  1 59  ? 54.814  20.373  28.200  1.00 11.14 ? 58  THR F OG1 1 
ATOM   1541  C  CG2 . THR B  1 59  ? 54.491  18.117  27.401  1.00 7.10  ? 58  THR F CG2 1 
ATOM   1542  N  N   . SER B  1 60  ? 54.528  21.620  24.545  1.00 4.19  ? 59  SER F N   1 
ATOM   1543  C  CA  . SER B  1 60  ? 53.875  22.137  23.368  1.00 3.06  ? 59  SER F CA  1 
ATOM   1544  C  C   . SER B  1 60  ? 54.623  21.981  22.028  1.00 2.93  ? 59  SER F C   1 
ATOM   1545  O  O   . SER B  1 60  ? 54.032  22.284  20.998  1.00 4.86  ? 59  SER F O   1 
ATOM   1546  C  CB  . SER B  1 60  ? 53.545  23.573  23.660  1.00 2.00  ? 59  SER F CB  1 
ATOM   1547  O  OG  . SER B  1 60  ? 54.605  24.205  24.348  1.00 2.39  ? 59  SER F OG  1 
ATOM   1548  N  N   . ALA B  1 61  ? 55.860  21.471  21.939  1.00 2.35  ? 60  ALA F N   1 
ATOM   1549  C  CA  . ALA B  1 61  ? 56.587  21.303  20.689  1.00 2.00  ? 60  ALA F CA  1 
ATOM   1550  C  C   . ALA B  1 61  ? 56.036  20.207  19.791  1.00 2.00  ? 60  ALA F C   1 
ATOM   1551  O  O   . ALA B  1 61  ? 56.372  20.042  18.627  1.00 2.53  ? 60  ALA F O   1 
ATOM   1552  C  CB  . ALA B  1 61  ? 57.991  20.970  21.018  1.00 2.00  ? 60  ALA F CB  1 
ATOM   1553  N  N   . GLY B  1 62  ? 55.237  19.358  20.342  1.00 2.00  ? 61  GLY F N   1 
ATOM   1554  C  CA  . GLY B  1 62  ? 54.638  18.351  19.579  1.00 2.00  ? 61  GLY F CA  1 
ATOM   1555  C  C   . GLY B  1 62  ? 55.571  17.190  19.447  1.00 2.00  ? 61  GLY F C   1 
ATOM   1556  O  O   . GLY B  1 62  ? 56.518  17.051  20.217  1.00 2.03  ? 61  GLY F O   1 
ATOM   1557  N  N   . PRO B  1 63  ? 55.305  16.332  18.451  1.00 3.80  ? 62  PRO F N   1 
ATOM   1558  C  CA  . PRO B  1 63  ? 56.031  15.096  18.188  1.00 2.00  ? 62  PRO F CA  1 
ATOM   1559  C  C   . PRO B  1 63  ? 57.264  15.362  17.324  1.00 2.58  ? 62  PRO F C   1 
ATOM   1560  O  O   . PRO B  1 63  ? 57.469  16.520  16.910  1.00 2.00  ? 62  PRO F O   1 
ATOM   1561  C  CB  . PRO B  1 63  ? 54.954  14.323  17.555  1.00 2.00  ? 62  PRO F CB  1 
ATOM   1562  C  CG  . PRO B  1 63  ? 54.329  15.330  16.596  1.00 2.75  ? 62  PRO F CG  1 
ATOM   1563  C  CD  . PRO B  1 63  ? 54.239  16.547  17.439  1.00 2.00  ? 62  PRO F CD  1 
ATOM   1564  N  N   . HIS B  1 64  ? 58.082  14.358  16.974  1.00 2.00  ? 63  HIS F N   1 
ATOM   1565  C  CA  . HIS B  1 64  ? 59.255  14.618  16.140  1.00 2.85  ? 63  HIS F CA  1 
ATOM   1566  C  C   . HIS B  1 64  ? 58.889  15.249  14.823  1.00 2.08  ? 63  HIS F C   1 
ATOM   1567  O  O   . HIS B  1 64  ? 57.828  14.910  14.300  1.00 2.52  ? 63  HIS F O   1 
ATOM   1568  C  CB  . HIS B  1 64  ? 60.061  13.315  15.895  1.00 2.00  ? 63  HIS F CB  1 
ATOM   1569  C  CG  . HIS B  1 64  ? 60.636  12.801  17.214  1.00 4.63  ? 63  HIS F CG  1 
ATOM   1570  N  ND1 . HIS B  1 64  ? 60.971  11.575  17.547  1.00 3.57  ? 63  HIS F ND1 1 
ATOM   1571  C  CD2 . HIS B  1 64  ? 60.847  13.612  18.326  1.00 6.58  ? 63  HIS F CD2 1 
ATOM   1572  C  CE1 . HIS B  1 64  ? 61.355  11.679  18.816  1.00 7.28  ? 63  HIS F CE1 1 
ATOM   1573  N  NE2 . HIS B  1 64  ? 61.305  12.910  19.335  1.00 10.94 ? 63  HIS F NE2 1 
ATOM   1574  N  N   . PHE B  1 65  ? 59.689  16.207  14.291  1.00 3.69  ? 64  PHE F N   1 
ATOM   1575  C  CA  . PHE B  1 65  ? 59.382  16.835  13.002  1.00 2.00  ? 64  PHE F CA  1 
ATOM   1576  C  C   . PHE B  1 65  ? 59.460  15.696  12.021  1.00 3.05  ? 64  PHE F C   1 
ATOM   1577  O  O   . PHE B  1 65  ? 60.453  14.954  12.040  1.00 3.09  ? 64  PHE F O   1 
ATOM   1578  C  CB  . PHE B  1 65  ? 60.400  17.892  12.636  1.00 2.03  ? 64  PHE F CB  1 
ATOM   1579  C  CG  . PHE B  1 65  ? 60.242  18.567  11.278  1.00 3.04  ? 64  PHE F CG  1 
ATOM   1580  C  CD1 . PHE B  1 65  ? 58.996  18.797  10.708  1.00 2.00  ? 64  PHE F CD1 1 
ATOM   1581  C  CD2 . PHE B  1 65  ? 61.394  18.899  10.599  1.00 2.00  ? 64  PHE F CD2 1 
ATOM   1582  C  CE1 . PHE B  1 65  ? 58.937  19.352  9.463   1.00 2.00  ? 64  PHE F CE1 1 
ATOM   1583  C  CE2 . PHE B  1 65  ? 61.309  19.455  9.355   1.00 2.00  ? 64  PHE F CE2 1 
ATOM   1584  C  CZ  . PHE B  1 65  ? 60.084  19.673  8.792   1.00 2.00  ? 64  PHE F CZ  1 
ATOM   1585  N  N   . ASN B  1 66  ? 58.389  15.523  11.223  1.00 4.11  ? 65  ASN F N   1 
ATOM   1586  C  CA  . ASN B  1 66  ? 58.264  14.373  10.316  1.00 3.30  ? 65  ASN F CA  1 
ATOM   1587  C  C   . ASN B  1 66  ? 57.487  14.621  9.018   1.00 4.54  ? 65  ASN F C   1 
ATOM   1588  O  O   . ASN B  1 66  ? 56.388  14.041  8.818   1.00 3.42  ? 65  ASN F O   1 
ATOM   1589  C  CB  . ASN B  1 66  ? 57.603  13.258  11.100  1.00 4.09  ? 65  ASN F CB  1 
ATOM   1590  C  CG  . ASN B  1 66  ? 57.679  11.908  10.478  1.00 2.00  ? 65  ASN F CG  1 
ATOM   1591  O  OD1 . ASN B  1 66  ? 58.359  11.694  9.481   1.00 3.17  ? 65  ASN F OD1 1 
ATOM   1592  N  ND2 . ASN B  1 66  ? 56.963  10.995  11.076  1.00 2.00  ? 65  ASN F ND2 1 
ATOM   1593  N  N   . PRO B  1 67  ? 57.974  15.488  8.086   1.00 3.10  ? 66  PRO F N   1 
ATOM   1594  C  CA  . PRO B  1 67  ? 57.210  15.867  6.912   1.00 2.00  ? 66  PRO F CA  1 
ATOM   1595  C  C   . PRO B  1 67  ? 56.861  14.699  5.978   1.00 2.01  ? 66  PRO F C   1 
ATOM   1596  O  O   . PRO B  1 67  ? 55.844  14.715  5.290   1.00 2.31  ? 66  PRO F O   1 
ATOM   1597  C  CB  . PRO B  1 67  ? 58.082  16.965  6.321   1.00 2.28  ? 66  PRO F CB  1 
ATOM   1598  C  CG  . PRO B  1 67  ? 59.479  16.815  6.829   1.00 2.00  ? 66  PRO F CG  1 
ATOM   1599  C  CD  . PRO B  1 67  ? 59.205  16.259  8.200   1.00 2.00  ? 66  PRO F CD  1 
ATOM   1600  N  N   . LEU B  1 68  ? 57.645  13.625  6.027   1.00 2.00  ? 67  LEU F N   1 
ATOM   1601  C  CA  . LEU B  1 68  ? 57.500  12.480  5.168   1.00 2.00  ? 67  LEU F CA  1 
ATOM   1602  C  C   . LEU B  1 68  ? 56.722  11.328  5.745   1.00 3.60  ? 67  LEU F C   1 
ATOM   1603  O  O   . LEU B  1 68  ? 56.754  10.239  5.166   1.00 5.14  ? 67  LEU F O   1 
ATOM   1604  C  CB  . LEU B  1 68  ? 58.862  12.006  4.804   1.00 2.00  ? 67  LEU F CB  1 
ATOM   1605  C  CG  . LEU B  1 68  ? 59.692  13.020  4.029   1.00 2.84  ? 67  LEU F CG  1 
ATOM   1606  C  CD1 . LEU B  1 68  ? 60.993  12.380  3.647   1.00 6.85  ? 67  LEU F CD1 1 
ATOM   1607  C  CD2 . LEU B  1 68  ? 58.989  13.428  2.771   1.00 2.79  ? 67  LEU F CD2 1 
ATOM   1608  N  N   . SER B  1 69  ? 56.053  11.534  6.880   1.00 4.26  ? 68  SER F N   1 
ATOM   1609  C  CA  . SER B  1 69  ? 55.354  10.462  7.559   1.00 7.73  ? 68  SER F CA  1 
ATOM   1610  C  C   . SER B  1 69  ? 56.060  9.114   7.701   1.00 6.73  ? 68  SER F C   1 
ATOM   1611  O  O   . SER B  1 69  ? 55.491  8.031   7.584   1.00 8.26  ? 68  SER F O   1 
ATOM   1612  C  CB  . SER B  1 69  ? 54.021  10.282  6.870   1.00 7.95  ? 68  SER F CB  1 
ATOM   1613  O  OG  . SER B  1 69  ? 53.255  11.475  7.123   1.00 18.46 ? 68  SER F OG  1 
ATOM   1614  N  N   . ARG B  1 70  ? 57.317  9.195   8.074   1.00 6.13  ? 69  ARG F N   1 
ATOM   1615  C  CA  . ARG B  1 70  ? 58.157  8.038   8.248   1.00 5.24  ? 69  ARG F CA  1 
ATOM   1616  C  C   . ARG B  1 70  ? 58.021  7.560   9.681   1.00 4.72  ? 69  ARG F C   1 
ATOM   1617  O  O   . ARG B  1 70  ? 57.360  8.227   10.486  1.00 5.25  ? 69  ARG F O   1 
ATOM   1618  C  CB  . ARG B  1 70  ? 59.512  8.525   7.917   1.00 6.17  ? 69  ARG F CB  1 
ATOM   1619  C  CG  . ARG B  1 70  ? 60.171  7.780   6.862   1.00 12.13 ? 69  ARG F CG  1 
ATOM   1620  C  CD  . ARG B  1 70  ? 59.413  7.756   5.563   1.00 18.63 ? 69  ARG F CD  1 
ATOM   1621  N  NE  . ARG B  1 70  ? 60.234  8.454   4.614   1.00 30.27 ? 69  ARG F NE  1 
ATOM   1622  C  CZ  . ARG B  1 70  ? 61.396  7.972   4.147   1.00 35.47 ? 69  ARG F CZ  1 
ATOM   1623  N  NH1 . ARG B  1 70  ? 61.872  6.759   4.502   1.00 38.97 ? 69  ARG F NH1 1 
ATOM   1624  N  NH2 . ARG B  1 70  ? 62.085  8.730   3.284   1.00 36.23 ? 69  ARG F NH2 1 
ATOM   1625  N  N   . LYS B  1 71  ? 58.597  6.417   10.032  1.00 4.23  ? 70  LYS F N   1 
ATOM   1626  C  CA  . LYS B  1 71  ? 58.631  5.925   11.413  1.00 5.32  ? 70  LYS F CA  1 
ATOM   1627  C  C   . LYS B  1 71  ? 59.931  6.421   12.061  1.00 6.41  ? 70  LYS F C   1 
ATOM   1628  O  O   . LYS B  1 71  ? 60.851  6.947   11.401  1.00 8.83  ? 70  LYS F O   1 
ATOM   1629  C  CB  . LYS B  1 71  ? 58.652  4.388   11.526  1.00 5.75  ? 70  LYS F CB  1 
ATOM   1630  C  CG  . LYS B  1 71  ? 57.305  3.670   11.403  1.00 10.94 ? 70  LYS F CG  1 
ATOM   1631  C  CD  . LYS B  1 71  ? 57.531  2.142   11.467  1.00 16.16 ? 70  LYS F CD  1 
ATOM   1632  C  CE  . LYS B  1 71  ? 56.256  1.282   11.327  1.00 17.73 ? 70  LYS F CE  1 
ATOM   1633  N  NZ  . LYS B  1 71  ? 55.695  1.233   9.982   1.00 17.95 ? 70  LYS F NZ  1 
ATOM   1634  N  N   . HIS B  1 72  ? 60.018  6.320   13.379  1.00 3.11  ? 71  HIS F N   1 
ATOM   1635  C  CA  . HIS B  1 72  ? 61.219  6.692   14.076  1.00 2.00  ? 71  HIS F CA  1 
ATOM   1636  C  C   . HIS B  1 72  ? 62.467  5.857   13.798  1.00 3.08  ? 71  HIS F C   1 
ATOM   1637  O  O   . HIS B  1 72  ? 62.395  4.627   13.793  1.00 3.48  ? 71  HIS F O   1 
ATOM   1638  C  CB  . HIS B  1 72  ? 60.947  6.636   15.530  1.00 4.04  ? 71  HIS F CB  1 
ATOM   1639  C  CG  . HIS B  1 72  ? 62.011  7.246   16.430  1.00 4.77  ? 71  HIS F CG  1 
ATOM   1640  N  ND1 . HIS B  1 72  ? 62.195  8.547   16.552  1.00 2.00  ? 71  HIS F ND1 1 
ATOM   1641  C  CD2 . HIS B  1 72  ? 62.861  6.560   17.271  1.00 2.00  ? 71  HIS F CD2 1 
ATOM   1642  C  CE1 . HIS B  1 72  ? 63.124  8.689   17.456  1.00 2.00  ? 71  HIS F CE1 1 
ATOM   1643  N  NE2 . HIS B  1 72  ? 63.511  7.507   17.877  1.00 2.00  ? 71  HIS F NE2 1 
ATOM   1644  N  N   . GLY B  1 73  ? 63.632  6.496   13.637  1.00 2.00  ? 72  GLY F N   1 
ATOM   1645  C  CA  . GLY B  1 73  ? 64.840  5.738   13.556  1.00 2.00  ? 72  GLY F CA  1 
ATOM   1646  C  C   . GLY B  1 73  ? 65.963  6.512   14.184  1.00 2.62  ? 72  GLY F C   1 
ATOM   1647  O  O   . GLY B  1 73  ? 65.716  7.445   14.962  1.00 5.49  ? 72  GLY F O   1 
ATOM   1648  N  N   . GLY B  1 74  ? 67.176  6.140   13.794  1.00 2.00  ? 73  GLY F N   1 
ATOM   1649  C  CA  . GLY B  1 74  ? 68.422  6.753   14.195  1.00 2.00  ? 73  GLY F CA  1 
ATOM   1650  C  C   . GLY B  1 74  ? 68.910  7.531   12.983  1.00 2.00  ? 73  GLY F C   1 
ATOM   1651  O  O   . GLY B  1 74  ? 68.427  7.222   11.896  1.00 2.00  ? 73  GLY F O   1 
ATOM   1652  N  N   . PRO B  1 75  ? 69.801  8.534   13.062  1.00 2.00  ? 74  PRO F N   1 
ATOM   1653  C  CA  . PRO B  1 75  ? 70.185  9.410   11.971  1.00 2.00  ? 74  PRO F CA  1 
ATOM   1654  C  C   . PRO B  1 75  ? 70.654  8.755   10.683  1.00 2.08  ? 74  PRO F C   1 
ATOM   1655  O  O   . PRO B  1 75  ? 70.519  9.272   9.576   1.00 2.00  ? 74  PRO F O   1 
ATOM   1656  C  CB  . PRO B  1 75  ? 71.227  10.300  12.597  1.00 2.00  ? 74  PRO F CB  1 
ATOM   1657  C  CG  . PRO B  1 75  ? 71.601  9.681   13.902  1.00 2.00  ? 74  PRO F CG  1 
ATOM   1658  C  CD  . PRO B  1 75  ? 70.303  9.085   14.306  1.00 2.00  ? 74  PRO F CD  1 
ATOM   1659  N  N   . LYS B  1 76  ? 71.194  7.560   10.818  1.00 2.47  ? 75  LYS F N   1 
ATOM   1660  C  CA  . LYS B  1 76  ? 71.717  6.862   9.681   1.00 2.51  ? 75  LYS F CA  1 
ATOM   1661  C  C   . LYS B  1 76  ? 70.648  5.972   9.139   1.00 3.05  ? 75  LYS F C   1 
ATOM   1662  O  O   . LYS B  1 76  ? 70.960  5.269   8.184   1.00 2.42  ? 75  LYS F O   1 
ATOM   1663  C  CB  . LYS B  1 76  ? 72.888  5.996   10.065  1.00 4.54  ? 75  LYS F CB  1 
ATOM   1664  C  CG  . LYS B  1 76  ? 73.999  6.700   10.808  1.00 8.66  ? 75  LYS F CG  1 
ATOM   1665  C  CD  . LYS B  1 76  ? 74.571  5.849   11.978  1.00 13.47 ? 75  LYS F CD  1 
ATOM   1666  C  CE  . LYS B  1 76  ? 75.717  4.929   11.562  1.00 10.24 ? 75  LYS F CE  1 
ATOM   1667  N  NZ  . LYS B  1 76  ? 75.540  3.642   12.189  1.00 12.16 ? 75  LYS F NZ  1 
ATOM   1668  N  N   . ASP B  1 77  ? 69.419  5.956   9.667   1.00 2.68  ? 76  ASP F N   1 
ATOM   1669  C  CA  . ASP B  1 77  ? 68.447  4.968   9.199   1.00 4.82  ? 76  ASP F CA  1 
ATOM   1670  C  C   . ASP B  1 77  ? 67.713  5.632   8.086   1.00 7.05  ? 76  ASP F C   1 
ATOM   1671  O  O   . ASP B  1 77  ? 67.648  6.857   8.092   1.00 9.56  ? 76  ASP F O   1 
ATOM   1672  C  CB  . ASP B  1 77  ? 67.439  4.549   10.308  1.00 3.17  ? 76  ASP F CB  1 
ATOM   1673  C  CG  . ASP B  1 77  ? 68.010  3.565   11.317  1.00 3.94  ? 76  ASP F CG  1 
ATOM   1674  O  OD1 . ASP B  1 77  ? 68.469  2.522   10.867  1.00 6.39  ? 76  ASP F OD1 1 
ATOM   1675  O  OD2 . ASP B  1 77  ? 68.039  3.803   12.534  1.00 5.62  ? 76  ASP F OD2 1 
ATOM   1676  N  N   . GLU B  1 78  ? 67.190  4.915   7.087   1.00 9.71  ? 77  GLU F N   1 
ATOM   1677  C  CA  . GLU B  1 78  ? 66.447  5.597   6.035   1.00 10.47 ? 77  GLU F CA  1 
ATOM   1678  C  C   . GLU B  1 78  ? 65.078  5.935   6.599   1.00 10.06 ? 77  GLU F C   1 
ATOM   1679  O  O   . GLU B  1 78  ? 64.525  7.031   6.415   1.00 9.17  ? 77  GLU F O   1 
ATOM   1680  C  CB  . GLU B  1 78  ? 66.217  4.736   4.808   1.00 15.26 ? 77  GLU F CB  1 
ATOM   1681  C  CG  . GLU B  1 78  ? 67.267  4.733   3.703   1.00 24.16 ? 77  GLU F CG  1 
ATOM   1682  C  CD  . GLU B  1 78  ? 66.684  4.254   2.352   1.00 29.92 ? 77  GLU F CD  1 
ATOM   1683  O  OE1 . GLU B  1 78  ? 66.668  3.043   2.076   1.00 30.97 ? 77  GLU F OE1 1 
ATOM   1684  O  OE2 . GLU B  1 78  ? 66.250  5.108   1.563   1.00 33.65 ? 77  GLU F OE2 1 
ATOM   1685  N  N   . GLU B  1 79  ? 64.556  4.941   7.326   1.00 7.95  ? 78  GLU F N   1 
ATOM   1686  C  CA  . GLU B  1 79  ? 63.246  5.022   7.948   1.00 6.36  ? 78  GLU F CA  1 
ATOM   1687  C  C   . GLU B  1 79  ? 63.518  5.645   9.288   1.00 5.02  ? 78  GLU F C   1 
ATOM   1688  O  O   . GLU B  1 79  ? 63.904  5.015   10.283  1.00 7.22  ? 78  GLU F O   1 
ATOM   1689  C  CB  . GLU B  1 79  ? 62.652  3.630   8.113   1.00 5.39  ? 78  GLU F CB  1 
ATOM   1690  C  CG  . GLU B  1 79  ? 61.165  3.548   8.508   1.00 11.12 ? 78  GLU F CG  1 
ATOM   1691  C  CD  . GLU B  1 79  ? 60.084  4.147   7.581   1.00 14.35 ? 78  GLU F CD  1 
ATOM   1692  O  OE1 . GLU B  1 79  ? 60.328  4.493   6.411   1.00 18.13 ? 78  GLU F OE1 1 
ATOM   1693  O  OE2 . GLU B  1 79  ? 58.960  4.260   8.057   1.00 12.16 ? 78  GLU F OE2 1 
ATOM   1694  N  N   . ARG B  1 80  ? 63.483  6.940   9.157   1.00 2.45  ? 79  ARG F N   1 
ATOM   1695  C  CA  . ARG B  1 80  ? 63.628  7.799   10.276  1.00 2.39  ? 79  ARG F CA  1 
ATOM   1696  C  C   . ARG B  1 80  ? 62.773  8.993   10.002  1.00 3.04  ? 79  ARG F C   1 
ATOM   1697  O  O   . ARG B  1 80  ? 62.228  9.195   8.914   1.00 5.31  ? 79  ARG F O   1 
ATOM   1698  C  CB  . ARG B  1 80  ? 65.073  8.174   10.444  1.00 2.00  ? 79  ARG F CB  1 
ATOM   1699  C  CG  . ARG B  1 80  ? 65.793  8.829   9.323   1.00 2.00  ? 79  ARG F CG  1 
ATOM   1700  C  CD  . ARG B  1 80  ? 66.123  10.103  9.908   1.00 3.14  ? 79  ARG F CD  1 
ATOM   1701  N  NE  . ARG B  1 80  ? 67.456  10.501  9.592   1.00 4.20  ? 79  ARG F NE  1 
ATOM   1702  C  CZ  . ARG B  1 80  ? 67.861  11.728  9.919   1.00 5.32  ? 79  ARG F CZ  1 
ATOM   1703  N  NH1 . ARG B  1 80  ? 67.081  12.636  10.511  1.00 2.00  ? 79  ARG F NH1 1 
ATOM   1704  N  NH2 . ARG B  1 80  ? 69.115  12.035  9.613   1.00 6.91  ? 79  ARG F NH2 1 
ATOM   1705  N  N   . HIS B  1 81  ? 62.654  9.800   11.029  1.00 2.92  ? 80  HIS F N   1 
ATOM   1706  C  CA  . HIS B  1 81  ? 61.872  11.022  10.942  1.00 2.00  ? 80  HIS F CA  1 
ATOM   1707  C  C   . HIS B  1 81  ? 62.922  12.110  10.673  1.00 2.00  ? 80  HIS F C   1 
ATOM   1708  O  O   . HIS B  1 81  ? 64.056  11.954  11.138  1.00 2.00  ? 80  HIS F O   1 
ATOM   1709  C  CB  . HIS B  1 81  ? 61.202  11.390  12.253  1.00 2.00  ? 80  HIS F CB  1 
ATOM   1710  C  CG  . HIS B  1 81  ? 60.287  10.481  13.039  1.00 2.00  ? 80  HIS F CG  1 
ATOM   1711  N  ND1 . HIS B  1 81  ? 60.311  10.400  14.369  1.00 2.12  ? 80  HIS F ND1 1 
ATOM   1712  C  CD2 . HIS B  1 81  ? 59.240  9.749   12.570  1.00 2.00  ? 80  HIS F CD2 1 
ATOM   1713  C  CE1 . HIS B  1 81  ? 59.289  9.664   14.715  1.00 2.00  ? 80  HIS F CE1 1 
ATOM   1714  N  NE2 . HIS B  1 81  ? 58.653  9.278   13.623  1.00 2.00  ? 80  HIS F NE2 1 
ATOM   1715  N  N   . VAL B  1 82  ? 62.621  13.271  10.077  1.00 4.06  ? 81  VAL F N   1 
ATOM   1716  C  CA  . VAL B  1 82  ? 63.628  14.295  9.784   1.00 2.94  ? 81  VAL F CA  1 
ATOM   1717  C  C   . VAL B  1 82  ? 64.283  14.805  11.076  1.00 2.03  ? 81  VAL F C   1 
ATOM   1718  O  O   . VAL B  1 82  ? 65.493  15.041  11.150  1.00 2.13  ? 81  VAL F O   1 
ATOM   1719  C  CB  . VAL B  1 82  ? 62.915  15.402  8.978   1.00 2.00  ? 81  VAL F CB  1 
ATOM   1720  C  CG1 . VAL B  1 82  ? 63.773  16.625  8.730   1.00 2.00  ? 81  VAL F CG1 1 
ATOM   1721  C  CG2 . VAL B  1 82  ? 62.591  14.807  7.653   1.00 2.00  ? 81  VAL F CG2 1 
ATOM   1722  N  N   . GLY B  1 83  ? 63.529  14.888  12.146  1.00 2.00  ? 82  GLY F N   1 
ATOM   1723  C  CA  . GLY B  1 83  ? 64.112  15.367  13.377  1.00 2.00  ? 82  GLY F CA  1 
ATOM   1724  C  C   . GLY B  1 83  ? 64.828  14.284  14.189  1.00 2.00  ? 82  GLY F C   1 
ATOM   1725  O  O   . GLY B  1 83  ? 65.136  14.477  15.372  1.00 2.00  ? 82  GLY F O   1 
ATOM   1726  N  N   . ASP B  1 84  ? 65.117  13.103  13.679  1.00 2.00  ? 83  ASP F N   1 
ATOM   1727  C  CA  . ASP B  1 84  ? 65.834  12.149  14.496  1.00 2.00  ? 83  ASP F CA  1 
ATOM   1728  C  C   . ASP B  1 84  ? 67.333  12.321  14.413  1.00 2.00  ? 83  ASP F C   1 
ATOM   1729  O  O   . ASP B  1 84  ? 67.984  11.875  13.485  1.00 2.00  ? 83  ASP F O   1 
ATOM   1730  C  CB  . ASP B  1 84  ? 65.449  10.791  14.063  1.00 2.00  ? 83  ASP F CB  1 
ATOM   1731  C  CG  . ASP B  1 84  ? 63.979  10.501  14.261  1.00 2.00  ? 83  ASP F CG  1 
ATOM   1732  O  OD1 . ASP B  1 84  ? 63.264  11.100  15.082  1.00 2.00  ? 83  ASP F OD1 1 
ATOM   1733  O  OD2 . ASP B  1 84  ? 63.564  9.595   13.570  1.00 3.55  ? 83  ASP F OD2 1 
ATOM   1734  N  N   . LEU B  1 85  ? 67.904  13.030  15.372  1.00 3.29  ? 84  LEU F N   1 
ATOM   1735  C  CA  . LEU B  1 85  ? 69.336  13.216  15.400  1.00 2.00  ? 84  LEU F CA  1 
ATOM   1736  C  C   . LEU B  1 85  ? 70.013  12.269  16.343  1.00 2.00  ? 84  LEU F C   1 
ATOM   1737  O  O   . LEU B  1 85  ? 71.216  12.302  16.533  1.00 2.00  ? 84  LEU F O   1 
ATOM   1738  C  CB  . LEU B  1 85  ? 69.597  14.648  15.741  1.00 2.00  ? 84  LEU F CB  1 
ATOM   1739  C  CG  . LEU B  1 85  ? 69.110  15.606  14.676  1.00 2.00  ? 84  LEU F CG  1 
ATOM   1740  C  CD1 . LEU B  1 85  ? 69.512  17.016  15.056  1.00 2.00  ? 84  LEU F CD1 1 
ATOM   1741  C  CD2 . LEU B  1 85  ? 69.691  15.239  13.334  1.00 2.07  ? 84  LEU F CD2 1 
ATOM   1742  N  N   . GLY B  1 86  ? 69.272  11.333  16.894  1.00 2.00  ? 85  GLY F N   1 
ATOM   1743  C  CA  . GLY B  1 86  ? 69.789  10.240  17.684  1.00 2.00  ? 85  GLY F CA  1 
ATOM   1744  C  C   . GLY B  1 86  ? 69.957  10.588  19.147  1.00 2.00  ? 85  GLY F C   1 
ATOM   1745  O  O   . GLY B  1 86  ? 69.096  11.183  19.786  1.00 2.00  ? 85  GLY F O   1 
ATOM   1746  N  N   . ASN B  1 87  ? 71.136  10.207  19.593  1.00 2.51  ? 86  ASN F N   1 
ATOM   1747  C  CA  . ASN B  1 87  ? 71.636  10.352  20.930  1.00 2.00  ? 86  ASN F CA  1 
ATOM   1748  C  C   . ASN B  1 87  ? 72.747  11.382  21.040  1.00 2.00  ? 86  ASN F C   1 
ATOM   1749  O  O   . ASN B  1 87  ? 73.412  11.659  20.047  1.00 2.00  ? 86  ASN F O   1 
ATOM   1750  C  CB  . ASN B  1 87  ? 72.167  9.022   21.367  1.00 2.00  ? 86  ASN F CB  1 
ATOM   1751  C  CG  . ASN B  1 87  ? 71.046  8.092   21.729  1.00 2.62  ? 86  ASN F CG  1 
ATOM   1752  O  OD1 . ASN B  1 87  ? 70.137  8.497   22.449  1.00 2.00  ? 86  ASN F OD1 1 
ATOM   1753  N  ND2 . ASN B  1 87  ? 71.060  6.848   21.279  1.00 2.00  ? 86  ASN F ND2 1 
ATOM   1754  N  N   . VAL B  1 88  ? 73.009  11.989  22.201  1.00 2.00  ? 87  VAL F N   1 
ATOM   1755  C  CA  . VAL B  1 88  ? 74.263  12.704  22.451  1.00 2.00  ? 87  VAL F CA  1 
ATOM   1756  C  C   . VAL B  1 88  ? 74.749  12.129  23.761  1.00 2.00  ? 87  VAL F C   1 
ATOM   1757  O  O   . VAL B  1 88  ? 73.926  11.727  24.570  1.00 2.00  ? 87  VAL F O   1 
ATOM   1758  C  CB  . VAL B  1 88  ? 74.108  14.272  22.612  1.00 2.00  ? 87  VAL F CB  1 
ATOM   1759  C  CG1 . VAL B  1 88  ? 73.669  14.877  21.267  1.00 2.00  ? 87  VAL F CG1 1 
ATOM   1760  C  CG2 . VAL B  1 88  ? 73.115  14.611  23.723  1.00 2.00  ? 87  VAL F CG2 1 
ATOM   1761  N  N   . THR B  1 89  ? 76.039  12.017  23.993  1.00 2.00  ? 88  THR F N   1 
ATOM   1762  C  CA  . THR B  1 89  ? 76.585  11.521  25.242  1.00 2.00  ? 88  THR F CA  1 
ATOM   1763  C  C   . THR B  1 89  ? 77.025  12.606  26.199  1.00 2.00  ? 88  THR F C   1 
ATOM   1764  O  O   . THR B  1 89  ? 77.611  13.608  25.783  1.00 2.14  ? 88  THR F O   1 
ATOM   1765  C  CB  . THR B  1 89  ? 77.737  10.612  24.924  1.00 2.00  ? 88  THR F CB  1 
ATOM   1766  O  OG1 . THR B  1 89  ? 77.149  9.557   24.161  1.00 2.00  ? 88  THR F OG1 1 
ATOM   1767  C  CG2 . THR B  1 89  ? 78.463  10.074  26.131  1.00 2.00  ? 88  THR F CG2 1 
ATOM   1768  N  N   . ALA B  1 90  ? 76.668  12.462  27.471  1.00 2.00  ? 89  ALA F N   1 
ATOM   1769  C  CA  . ALA B  1 90  ? 77.089  13.374  28.500  1.00 2.00  ? 89  ALA F CA  1 
ATOM   1770  C  C   . ALA B  1 90  ? 78.158  12.634  29.268  1.00 3.93  ? 89  ALA F C   1 
ATOM   1771  O  O   . ALA B  1 90  ? 77.973  11.501  29.720  1.00 2.76  ? 89  ALA F O   1 
ATOM   1772  C  CB  . ALA B  1 90  ? 76.034  13.684  29.538  1.00 5.18  ? 89  ALA F CB  1 
ATOM   1773  N  N   . ASP B  1 91  ? 79.289  13.302  29.401  1.00 3.69  ? 90  ASP F N   1 
ATOM   1774  C  CA  . ASP B  1 91  ? 80.367  12.806  30.186  1.00 4.25  ? 90  ASP F CA  1 
ATOM   1775  C  C   . ASP B  1 91  ? 80.035  12.800  31.670  1.00 6.63  ? 90  ASP F C   1 
ATOM   1776  O  O   . ASP B  1 91  ? 78.942  13.143  32.104  1.00 5.64  ? 90  ASP F O   1 
ATOM   1777  C  CB  . ASP B  1 91  ? 81.584  13.653  29.893  1.00 5.98  ? 90  ASP F CB  1 
ATOM   1778  C  CG  . ASP B  1 91  ? 81.780  15.060  30.463  1.00 7.26  ? 90  ASP F CG  1 
ATOM   1779  O  OD1 . ASP B  1 91  ? 81.042  15.537  31.323  1.00 10.23 ? 90  ASP F OD1 1 
ATOM   1780  O  OD2 . ASP B  1 91  ? 82.748  15.682  30.035  1.00 8.42  ? 90  ASP F OD2 1 
ATOM   1781  N  N   . LYS B  1 92  ? 81.045  12.544  32.485  1.00 10.84 ? 91  LYS F N   1 
ATOM   1782  C  CA  . LYS B  1 92  ? 80.890  12.308  33.906  1.00 13.77 ? 91  LYS F CA  1 
ATOM   1783  C  C   . LYS B  1 92  ? 80.521  13.542  34.675  1.00 13.19 ? 91  LYS F C   1 
ATOM   1784  O  O   . LYS B  1 92  ? 79.820  13.434  35.664  1.00 12.51 ? 91  LYS F O   1 
ATOM   1785  C  CB  . LYS B  1 92  ? 82.172  11.708  34.413  1.00 17.54 ? 91  LYS F CB  1 
ATOM   1786  C  CG  . LYS B  1 92  ? 82.299  10.252  33.934  1.00 27.30 ? 91  LYS F CG  1 
ATOM   1787  C  CD  . LYS B  1 92  ? 82.508  9.923   32.420  1.00 31.98 ? 91  LYS F CD  1 
ATOM   1788  C  CE  . LYS B  1 92  ? 83.910  10.243  31.882  1.00 35.85 ? 91  LYS F CE  1 
ATOM   1789  N  NZ  . LYS B  1 92  ? 84.385  9.173   31.008  1.00 39.25 ? 91  LYS F NZ  1 
ATOM   1790  N  N   . ASP B  1 93  ? 80.909  14.715  34.165  1.00 12.96 ? 92  ASP F N   1 
ATOM   1791  C  CA  . ASP B  1 93  ? 80.525  16.021  34.719  1.00 11.86 ? 92  ASP F CA  1 
ATOM   1792  C  C   . ASP B  1 93  ? 79.159  16.483  34.211  1.00 8.65  ? 92  ASP F C   1 
ATOM   1793  O  O   . ASP B  1 93  ? 78.723  17.604  34.447  1.00 9.86  ? 92  ASP F O   1 
ATOM   1794  C  CB  . ASP B  1 93  ? 81.575  17.064  34.346  1.00 15.02 ? 92  ASP F CB  1 
ATOM   1795  C  CG  . ASP B  1 93  ? 83.017  16.618  34.644  1.00 22.29 ? 92  ASP F CG  1 
ATOM   1796  O  OD1 . ASP B  1 93  ? 83.314  16.240  35.793  1.00 25.14 ? 92  ASP F OD1 1 
ATOM   1797  O  OD2 . ASP B  1 93  ? 83.841  16.647  33.713  1.00 23.77 ? 92  ASP F OD2 1 
ATOM   1798  N  N   . GLY B  1 94  ? 78.459  15.617  33.495  1.00 5.61  ? 93  GLY F N   1 
ATOM   1799  C  CA  . GLY B  1 94  ? 77.155  15.888  32.955  1.00 3.91  ? 93  GLY F CA  1 
ATOM   1800  C  C   . GLY B  1 94  ? 77.163  16.757  31.730  1.00 4.20  ? 93  GLY F C   1 
ATOM   1801  O  O   . GLY B  1 94  ? 76.121  17.343  31.418  1.00 5.16  ? 93  GLY F O   1 
ATOM   1802  N  N   . VAL B  1 95  ? 78.284  16.817  31.005  1.00 3.15  ? 94  VAL F N   1 
ATOM   1803  C  CA  . VAL B  1 95  ? 78.402  17.725  29.872  1.00 4.34  ? 94  VAL F CA  1 
ATOM   1804  C  C   . VAL B  1 95  ? 78.390  16.982  28.538  1.00 6.12  ? 94  VAL F C   1 
ATOM   1805  O  O   . VAL B  1 95  ? 79.188  16.053  28.376  1.00 8.69  ? 94  VAL F O   1 
ATOM   1806  C  CB  . VAL B  1 95  ? 79.713  18.548  29.975  1.00 2.00  ? 94  VAL F CB  1 
ATOM   1807  C  CG1 . VAL B  1 95  ? 79.773  19.439  28.733  1.00 2.54  ? 94  VAL F CG1 1 
ATOM   1808  C  CG2 . VAL B  1 95  ? 79.781  19.458  31.213  1.00 2.00  ? 94  VAL F CG2 1 
ATOM   1809  N  N   . ALA B  1 96  ? 77.545  17.370  27.583  1.00 4.96  ? 95  ALA F N   1 
ATOM   1810  C  CA  . ALA B  1 96  ? 77.487  16.822  26.243  1.00 4.23  ? 95  ALA F CA  1 
ATOM   1811  C  C   . ALA B  1 96  ? 78.214  17.759  25.276  1.00 5.22  ? 95  ALA F C   1 
ATOM   1812  O  O   . ALA B  1 96  ? 77.682  18.857  25.021  1.00 7.81  ? 95  ALA F O   1 
ATOM   1813  C  CB  . ALA B  1 96  ? 76.062  16.716  25.753  1.00 2.00  ? 95  ALA F CB  1 
ATOM   1814  N  N   . ASP B  1 97  ? 79.404  17.443  24.748  1.00 2.49  ? 96  ASP F N   1 
ATOM   1815  C  CA  . ASP B  1 97  ? 79.997  18.295  23.728  1.00 3.88  ? 96  ASP F CA  1 
ATOM   1816  C  C   . ASP B  1 97  ? 79.450  17.794  22.419  1.00 3.49  ? 96  ASP F C   1 
ATOM   1817  O  O   . ASP B  1 97  ? 80.002  16.842  21.842  1.00 4.83  ? 96  ASP F O   1 
ATOM   1818  C  CB  . ASP B  1 97  ? 81.494  18.180  23.725  1.00 7.54  ? 96  ASP F CB  1 
ATOM   1819  C  CG  . ASP B  1 97  ? 82.019  18.632  25.068  1.00 15.90 ? 96  ASP F CG  1 
ATOM   1820  O  OD1 . ASP B  1 97  ? 81.782  19.805  25.411  1.00 19.36 ? 96  ASP F OD1 1 
ATOM   1821  O  OD2 . ASP B  1 97  ? 82.622  17.800  25.774  1.00 18.35 ? 96  ASP F OD2 1 
ATOM   1822  N  N   . VAL B  1 98  ? 78.341  18.375  21.975  1.00 2.09  ? 97  VAL F N   1 
ATOM   1823  C  CA  . VAL B  1 98  ? 77.646  17.849  20.824  1.00 2.40  ? 97  VAL F CA  1 
ATOM   1824  C  C   . VAL B  1 98  ? 78.438  18.009  19.528  1.00 3.04  ? 97  VAL F C   1 
ATOM   1825  O  O   . VAL B  1 98  ? 79.116  19.014  19.347  1.00 4.35  ? 97  VAL F O   1 
ATOM   1826  C  CB  . VAL B  1 98  ? 76.277  18.547  20.810  1.00 2.00  ? 97  VAL F CB  1 
ATOM   1827  C  CG1 . VAL B  1 98  ? 75.401  18.093  19.657  1.00 2.00  ? 97  VAL F CG1 1 
ATOM   1828  C  CG2 . VAL B  1 98  ? 75.559  18.149  22.097  1.00 2.00  ? 97  VAL F CG2 1 
ATOM   1829  N  N   . SER B  1 99  ? 78.428  17.018  18.638  1.00 2.10  ? 98  SER F N   1 
ATOM   1830  C  CA  . SER B  1 99  ? 79.061  17.089  17.344  1.00 3.44  ? 98  SER F CA  1 
ATOM   1831  C  C   . SER B  1 99  ? 78.368  16.028  16.526  1.00 4.20  ? 98  SER F C   1 
ATOM   1832  O  O   . SER B  1 99  ? 78.560  14.840  16.758  1.00 8.65  ? 98  SER F O   1 
ATOM   1833  C  CB  . SER B  1 99  ? 80.510  16.767  17.457  1.00 3.73  ? 98  SER F CB  1 
ATOM   1834  O  OG  . SER B  1 99  ? 81.259  17.325  16.389  1.00 9.94  ? 98  SER F OG  1 
ATOM   1835  N  N   . ILE B  1 100 ? 77.467  16.457  15.649  1.00 3.99  ? 99  ILE F N   1 
ATOM   1836  C  CA  . ILE B  1 100 ? 76.623  15.681  14.738  1.00 2.00  ? 99  ILE F CA  1 
ATOM   1837  C  C   . ILE B  1 100 ? 76.740  16.397  13.375  1.00 2.00  ? 99  ILE F C   1 
ATOM   1838  O  O   . ILE B  1 100 ? 76.959  17.618  13.219  1.00 2.57  ? 99  ILE F O   1 
ATOM   1839  C  CB  . ILE B  1 100 ? 75.145  15.706  15.310  1.00 2.00  ? 99  ILE F CB  1 
ATOM   1840  C  CG1 . ILE B  1 100 ? 75.060  14.767  16.507  1.00 2.00  ? 99  ILE F CG1 1 
ATOM   1841  C  CG2 . ILE B  1 100 ? 74.128  15.271  14.284  1.00 2.00  ? 99  ILE F CG2 1 
ATOM   1842  C  CD1 . ILE B  1 100 ? 73.771  14.844  17.359  1.00 2.00  ? 99  ILE F CD1 1 
ATOM   1843  N  N   . GLU B  1 101 ? 76.596  15.647  12.322  1.00 2.00  ? 100 GLU F N   1 
ATOM   1844  C  CA  . GLU B  1 101 ? 76.546  16.177  10.986  1.00 3.11  ? 100 GLU F CA  1 
ATOM   1845  C  C   . GLU B  1 101 ? 75.419  15.392  10.422  1.00 2.00  ? 100 GLU F C   1 
ATOM   1846  O  O   . GLU B  1 101 ? 75.408  14.167  10.567  1.00 5.94  ? 100 GLU F O   1 
ATOM   1847  C  CB  . GLU B  1 101 ? 77.782  15.857  10.296  1.00 6.58  ? 100 GLU F CB  1 
ATOM   1848  C  CG  . GLU B  1 101 ? 77.932  16.595  9.014   1.00 13.74 ? 100 GLU F CG  1 
ATOM   1849  C  CD  . GLU B  1 101 ? 79.245  16.141  8.451   1.00 17.80 ? 100 GLU F CD  1 
ATOM   1850  O  OE1 . GLU B  1 101 ? 80.271  16.392  9.093   1.00 19.26 ? 100 GLU F OE1 1 
ATOM   1851  O  OE2 . GLU B  1 101 ? 79.214  15.510  7.392   1.00 21.81 ? 100 GLU F OE2 1 
ATOM   1852  N  N   . ASP B  1 102 ? 74.451  16.033  9.835   1.00 2.00  ? 101 ASP F N   1 
ATOM   1853  C  CA  . ASP B  1 102 ? 73.272  15.333  9.424   1.00 2.03  ? 101 ASP F CA  1 
ATOM   1854  C  C   . ASP B  1 102 ? 72.848  15.865  8.083   1.00 2.90  ? 101 ASP F C   1 
ATOM   1855  O  O   . ASP B  1 102 ? 72.948  17.058  7.863   1.00 4.48  ? 101 ASP F O   1 
ATOM   1856  C  CB  . ASP B  1 102 ? 72.181  15.541  10.460  1.00 2.00  ? 101 ASP F CB  1 
ATOM   1857  C  CG  . ASP B  1 102 ? 71.096  14.555  10.170  1.00 3.11  ? 101 ASP F CG  1 
ATOM   1858  O  OD1 . ASP B  1 102 ? 71.261  13.344  10.422  1.00 3.29  ? 101 ASP F OD1 1 
ATOM   1859  O  OD2 . ASP B  1 102 ? 70.110  15.016  9.625   1.00 2.00  ? 101 ASP F OD2 1 
ATOM   1860  N  N   . SER B  1 103 ? 72.390  15.044  7.163   1.00 3.68  ? 102 SER F N   1 
ATOM   1861  C  CA  . SER B  1 103 ? 72.011  15.540  5.853   1.00 6.10  ? 102 SER F CA  1 
ATOM   1862  C  C   . SER B  1 103 ? 70.528  15.433  5.541   1.00 6.55  ? 102 SER F C   1 
ATOM   1863  O  O   . SER B  1 103 ? 70.157  15.579  4.374   1.00 8.54  ? 102 SER F O   1 
ATOM   1864  C  CB  . SER B  1 103 ? 72.801  14.768  4.834   1.00 7.25  ? 102 SER F CB  1 
ATOM   1865  O  OG  . SER B  1 103 ? 74.080  14.506  5.424   1.00 18.90 ? 102 SER F OG  1 
ATOM   1866  N  N   . VAL B  1 104 ? 69.664  15.090  6.514   1.00 3.94  ? 103 VAL F N   1 
ATOM   1867  C  CA  . VAL B  1 104 ? 68.249  15.041  6.245   1.00 2.00  ? 103 VAL F CA  1 
ATOM   1868  C  C   . VAL B  1 104 ? 67.636  16.358  6.653   1.00 2.00  ? 103 VAL F C   1 
ATOM   1869  O  O   . VAL B  1 104 ? 66.775  16.891  5.955   1.00 3.57  ? 103 VAL F O   1 
ATOM   1870  C  CB  . VAL B  1 104 ? 67.606  13.855  7.004   1.00 2.00  ? 103 VAL F CB  1 
ATOM   1871  C  CG1 . VAL B  1 104 ? 66.115  13.807  6.874   1.00 2.00  ? 103 VAL F CG1 1 
ATOM   1872  C  CG2 . VAL B  1 104 ? 68.022  12.574  6.328   1.00 4.66  ? 103 VAL F CG2 1 
ATOM   1873  N  N   . ILE B  1 105 ? 67.997  16.833  7.836   1.00 2.63  ? 104 ILE F N   1 
ATOM   1874  C  CA  . ILE B  1 105 ? 67.511  18.093  8.385   1.00 2.79  ? 104 ILE F CA  1 
ATOM   1875  C  C   . ILE B  1 105 ? 68.124  19.151  7.511   1.00 4.30  ? 104 ILE F C   1 
ATOM   1876  O  O   . ILE B  1 105 ? 69.148  18.879  6.874   1.00 7.68  ? 104 ILE F O   1 
ATOM   1877  C  CB  . ILE B  1 105 ? 67.976  18.385  9.839   1.00 2.00  ? 104 ILE F CB  1 
ATOM   1878  C  CG1 . ILE B  1 105 ? 69.481  18.253  10.047  1.00 2.00  ? 104 ILE F CG1 1 
ATOM   1879  C  CG2 . ILE B  1 105 ? 67.150  17.501  10.700  1.00 2.00  ? 104 ILE F CG2 1 
ATOM   1880  C  CD1 . ILE B  1 105 ? 70.045  18.933  11.271  1.00 2.00  ? 104 ILE F CD1 1 
ATOM   1881  N  N   . SER B  1 106 ? 67.585  20.354  7.487   1.00 3.72  ? 105 SER F N   1 
ATOM   1882  C  CA  . SER B  1 106 ? 68.198  21.386  6.694   1.00 2.79  ? 105 SER F CA  1 
ATOM   1883  C  C   . SER B  1 106 ? 67.876  22.680  7.381   1.00 2.00  ? 105 SER F C   1 
ATOM   1884  O  O   . SER B  1 106 ? 67.040  22.658  8.287   1.00 2.00  ? 105 SER F O   1 
ATOM   1885  C  CB  . SER B  1 106 ? 67.588  21.269  5.315   1.00 2.00  ? 105 SER F CB  1 
ATOM   1886  O  OG  . SER B  1 106 ? 67.834  22.359  4.438   1.00 4.77  ? 105 SER F OG  1 
ATOM   1887  N  N   . LEU B  1 107 ? 68.544  23.771  7.025   1.00 2.00  ? 106 LEU F N   1 
ATOM   1888  C  CA  . LEU B  1 107 ? 68.137  25.081  7.486   1.00 2.00  ? 106 LEU F CA  1 
ATOM   1889  C  C   . LEU B  1 107 ? 67.369  25.772  6.369   1.00 2.00  ? 106 LEU F C   1 
ATOM   1890  O  O   . LEU B  1 107 ? 66.940  26.899  6.544   1.00 2.88  ? 106 LEU F O   1 
ATOM   1891  C  CB  . LEU B  1 107 ? 69.324  25.965  7.907   1.00 2.00  ? 106 LEU F CB  1 
ATOM   1892  C  CG  . LEU B  1 107 ? 70.243  25.412  9.005   1.00 3.28  ? 106 LEU F CG  1 
ATOM   1893  C  CD1 . LEU B  1 107 ? 71.166  26.470  9.422   1.00 2.00  ? 106 LEU F CD1 1 
ATOM   1894  C  CD2 . LEU B  1 107 ? 69.416  24.873  10.193  1.00 2.39  ? 106 LEU F CD2 1 
ATOM   1895  N  N   . SER B  1 108 ? 67.117  25.183  5.201   1.00 2.00  ? 107 SER F N   1 
ATOM   1896  C  CA  . SER B  1 108 ? 66.202  25.804  4.239   1.00 3.57  ? 107 SER F CA  1 
ATOM   1897  C  C   . SER B  1 108 ? 65.236  24.845  3.596   1.00 3.48  ? 107 SER F C   1 
ATOM   1898  O  O   . SER B  1 108 ? 65.477  23.631  3.583   1.00 4.99  ? 107 SER F O   1 
ATOM   1899  C  CB  . SER B  1 108 ? 66.937  26.486  3.110   1.00 3.99  ? 107 SER F CB  1 
ATOM   1900  O  OG  . SER B  1 108 ? 68.177  25.908  2.705   1.00 11.03 ? 107 SER F OG  1 
ATOM   1901  N  N   . GLY B  1 109 ? 64.078  25.342  3.141   1.00 6.02  ? 108 GLY F N   1 
ATOM   1902  C  CA  . GLY B  1 109 ? 63.112  24.575  2.346   1.00 7.43  ? 108 GLY F CA  1 
ATOM   1903  C  C   . GLY B  1 109 ? 62.118  23.714  3.121   1.00 10.22 ? 108 GLY F C   1 
ATOM   1904  O  O   . GLY B  1 109 ? 61.786  23.985  4.273   1.00 10.76 ? 108 GLY F O   1 
ATOM   1905  N  N   . ASP B  1 110 ? 61.601  22.640  2.529   1.00 11.08 ? 109 ASP F N   1 
ATOM   1906  C  CA  . ASP B  1 110 ? 60.616  21.813  3.204   1.00 10.10 ? 109 ASP F CA  1 
ATOM   1907  C  C   . ASP B  1 110 ? 61.145  21.158  4.467   1.00 10.06 ? 109 ASP F C   1 
ATOM   1908  O  O   . ASP B  1 110 ? 60.374  20.908  5.385   1.00 12.15 ? 109 ASP F O   1 
ATOM   1909  C  CB  . ASP B  1 110 ? 60.111  20.702  2.268   1.00 13.74 ? 109 ASP F CB  1 
ATOM   1910  C  CG  . ASP B  1 110 ? 59.341  21.115  1.011   1.00 15.39 ? 109 ASP F CG  1 
ATOM   1911  O  OD1 . ASP B  1 110 ? 58.625  22.121  1.025   1.00 18.39 ? 109 ASP F OD1 1 
ATOM   1912  O  OD2 . ASP B  1 110 ? 59.464  20.403  0.017   1.00 14.80 ? 109 ASP F OD2 1 
ATOM   1913  N  N   . HIS B  1 111 ? 62.437  20.836  4.588   1.00 9.76  ? 110 HIS F N   1 
ATOM   1914  C  CA  . HIS B  1 111 ? 62.939  20.135  5.768   1.00 6.69  ? 110 HIS F CA  1 
ATOM   1915  C  C   . HIS B  1 111 ? 63.640  21.085  6.704   1.00 4.45  ? 110 HIS F C   1 
ATOM   1916  O  O   . HIS B  1 111 ? 64.549  20.697  7.442   1.00 4.70  ? 110 HIS F O   1 
ATOM   1917  C  CB  . HIS B  1 111 ? 63.938  19.044  5.382   1.00 9.69  ? 110 HIS F CB  1 
ATOM   1918  C  CG  . HIS B  1 111 ? 63.325  17.846  4.665   1.00 15.30 ? 110 HIS F CG  1 
ATOM   1919  N  ND1 . HIS B  1 111 ? 63.929  16.708  4.326   1.00 16.04 ? 110 HIS F ND1 1 
ATOM   1920  C  CD2 . HIS B  1 111 ? 62.006  17.775  4.251   1.00 15.70 ? 110 HIS F CD2 1 
ATOM   1921  C  CE1 . HIS B  1 111 ? 63.032  15.965  3.730   1.00 17.53 ? 110 HIS F CE1 1 
ATOM   1922  N  NE2 . HIS B  1 111 ? 61.884  16.615  3.687   1.00 19.34 ? 110 HIS F NE2 1 
ATOM   1923  N  N   . SER B  1 112 ? 63.255  22.339  6.632   1.00 2.00  ? 111 SER F N   1 
ATOM   1924  C  CA  . SER B  1 112 ? 63.870  23.304  7.449   1.00 2.00  ? 111 SER F CA  1 
ATOM   1925  C  C   . SER B  1 112 ? 63.481  23.020  8.876   1.00 2.00  ? 111 SER F C   1 
ATOM   1926  O  O   . SER B  1 112 ? 62.306  22.812  9.219   1.00 2.35  ? 111 SER F O   1 
ATOM   1927  C  CB  . SER B  1 112 ? 63.396  24.676  7.011   1.00 2.00  ? 111 SER F CB  1 
ATOM   1928  O  OG  . SER B  1 112 ? 64.027  25.705  7.748   1.00 2.00  ? 111 SER F OG  1 
ATOM   1929  N  N   . ILE B  1 113 ? 64.504  22.998  9.703   1.00 2.00  ? 112 ILE F N   1 
ATOM   1930  C  CA  . ILE B  1 113 ? 64.241  22.958  11.114  1.00 2.00  ? 112 ILE F CA  1 
ATOM   1931  C  C   . ILE B  1 113 ? 64.181  24.367  11.711  1.00 2.00  ? 112 ILE F C   1 
ATOM   1932  O  O   . ILE B  1 113 ? 64.044  24.465  12.926  1.00 4.28  ? 112 ILE F O   1 
ATOM   1933  C  CB  . ILE B  1 113 ? 65.300  22.121  11.781  1.00 2.00  ? 112 ILE F CB  1 
ATOM   1934  C  CG1 . ILE B  1 113 ? 66.660  22.631  11.432  1.00 2.00  ? 112 ILE F CG1 1 
ATOM   1935  C  CG2 . ILE B  1 113 ? 65.073  20.661  11.385  1.00 2.00  ? 112 ILE F CG2 1 
ATOM   1936  C  CD1 . ILE B  1 113 ? 67.760  22.015  12.255  1.00 2.00  ? 112 ILE F CD1 1 
ATOM   1937  N  N   . ILE B  1 114 ? 64.257  25.513  10.999  1.00 2.00  ? 113 ILE F N   1 
ATOM   1938  C  CA  . ILE B  1 114 ? 64.124  26.835  11.611  1.00 2.00  ? 113 ILE F CA  1 
ATOM   1939  C  C   . ILE B  1 114 ? 62.726  27.070  12.173  1.00 2.00  ? 113 ILE F C   1 
ATOM   1940  O  O   . ILE B  1 114 ? 61.717  26.879  11.510  1.00 2.00  ? 113 ILE F O   1 
ATOM   1941  C  CB  . ILE B  1 114 ? 64.398  27.938  10.601  1.00 2.00  ? 113 ILE F CB  1 
ATOM   1942  C  CG1 . ILE B  1 114 ? 65.776  27.782  9.961   1.00 2.51  ? 113 ILE F CG1 1 
ATOM   1943  C  CG2 . ILE B  1 114 ? 64.325  29.278  11.310  1.00 2.00  ? 113 ILE F CG2 1 
ATOM   1944  C  CD1 . ILE B  1 114 ? 66.930  27.854  10.934  1.00 2.00  ? 113 ILE F CD1 1 
ATOM   1945  N  N   . GLY B  1 115 ? 62.615  27.530  13.412  1.00 4.75  ? 114 GLY F N   1 
ATOM   1946  C  CA  . GLY B  1 115 ? 61.335  27.774  14.097  1.00 2.68  ? 114 GLY F CA  1 
ATOM   1947  C  C   . GLY B  1 115 ? 60.743  26.548  14.758  1.00 2.00  ? 114 GLY F C   1 
ATOM   1948  O  O   . GLY B  1 115 ? 59.592  26.561  15.171  1.00 2.00  ? 114 GLY F O   1 
ATOM   1949  N  N   . ARG B  1 116 ? 61.464  25.449  14.806  1.00 2.00  ? 115 ARG F N   1 
ATOM   1950  C  CA  . ARG B  1 116 ? 60.998  24.236  15.458  1.00 3.45  ? 115 ARG F CA  1 
ATOM   1951  C  C   . ARG B  1 116 ? 61.831  24.038  16.701  1.00 2.00  ? 115 ARG F C   1 
ATOM   1952  O  O   . ARG B  1 116 ? 62.673  24.881  16.980  1.00 2.07  ? 115 ARG F O   1 
ATOM   1953  C  CB  . ARG B  1 116 ? 61.123  23.051  14.494  1.00 2.00  ? 115 ARG F CB  1 
ATOM   1954  C  CG  . ARG B  1 116 ? 60.288  23.369  13.264  1.00 2.00  ? 115 ARG F CG  1 
ATOM   1955  C  CD  . ARG B  1 116 ? 60.373  22.176  12.351  1.00 2.78  ? 115 ARG F CD  1 
ATOM   1956  N  NE  . ARG B  1 116 ? 59.859  22.446  11.037  1.00 2.16  ? 115 ARG F NE  1 
ATOM   1957  C  CZ  . ARG B  1 116 ? 58.561  22.588  10.749  1.00 2.00  ? 115 ARG F CZ  1 
ATOM   1958  N  NH1 . ARG B  1 116 ? 57.600  22.529  11.645  1.00 2.00  ? 115 ARG F NH1 1 
ATOM   1959  N  NH2 . ARG B  1 116 ? 58.226  22.802  9.491   1.00 2.00  ? 115 ARG F NH2 1 
ATOM   1960  N  N   . THR B  1 117 ? 61.679  22.969  17.464  1.00 2.66  ? 116 THR F N   1 
ATOM   1961  C  CA  . THR B  1 117 ? 62.248  22.888  18.809  1.00 2.03  ? 116 THR F CA  1 
ATOM   1962  C  C   . THR B  1 117 ? 63.337  21.858  18.922  1.00 2.00  ? 116 THR F C   1 
ATOM   1963  O  O   . THR B  1 117 ? 63.086  20.722  18.531  1.00 3.72  ? 116 THR F O   1 
ATOM   1964  C  CB  . THR B  1 117 ? 61.088  22.557  19.828  1.00 2.00  ? 116 THR F CB  1 
ATOM   1965  O  OG1 . THR B  1 117 ? 60.182  23.652  19.916  1.00 2.00  ? 116 THR F OG1 1 
ATOM   1966  C  CG2 . THR B  1 117 ? 61.610  22.263  21.200  1.00 2.00  ? 116 THR F CG2 1 
ATOM   1967  N  N   . LEU B  1 118 ? 64.524  22.137  19.428  1.00 2.00  ? 117 LEU F N   1 
ATOM   1968  C  CA  . LEU B  1 118 ? 65.457  21.077  19.689  1.00 2.00  ? 117 LEU F CA  1 
ATOM   1969  C  C   . LEU B  1 118 ? 65.115  20.584  21.082  1.00 2.00  ? 117 LEU F C   1 
ATOM   1970  O  O   . LEU B  1 118 ? 64.862  21.419  21.948  1.00 2.76  ? 117 LEU F O   1 
ATOM   1971  C  CB  . LEU B  1 118 ? 66.841  21.608  19.674  1.00 2.35  ? 117 LEU F CB  1 
ATOM   1972  C  CG  . LEU B  1 118 ? 67.916  20.573  19.704  1.00 3.66  ? 117 LEU F CG  1 
ATOM   1973  C  CD1 . LEU B  1 118 ? 67.823  19.646  18.522  1.00 2.20  ? 117 LEU F CD1 1 
ATOM   1974  C  CD2 . LEU B  1 118 ? 69.220  21.290  19.634  1.00 4.57  ? 117 LEU F CD2 1 
ATOM   1975  N  N   . VAL B  1 119 ? 65.070  19.284  21.347  1.00 2.00  ? 118 VAL F N   1 
ATOM   1976  C  CA  . VAL B  1 119 ? 64.731  18.709  22.623  1.00 2.00  ? 118 VAL F CA  1 
ATOM   1977  C  C   . VAL B  1 119 ? 65.821  17.729  23.020  1.00 2.52  ? 118 VAL F C   1 
ATOM   1978  O  O   . VAL B  1 119 ? 66.372  17.008  22.178  1.00 3.07  ? 118 VAL F O   1 
ATOM   1979  C  CB  . VAL B  1 119 ? 63.389  17.966  22.531  1.00 2.00  ? 118 VAL F CB  1 
ATOM   1980  C  CG1 . VAL B  1 119 ? 63.074  17.260  23.835  1.00 2.00  ? 118 VAL F CG1 1 
ATOM   1981  C  CG2 . VAL B  1 119 ? 62.287  18.934  22.202  1.00 2.00  ? 118 VAL F CG2 1 
ATOM   1982  N  N   . VAL B  1 120 ? 66.200  17.711  24.306  1.00 3.76  ? 119 VAL F N   1 
ATOM   1983  C  CA  . VAL B  1 120 ? 67.132  16.735  24.808  1.00 2.00  ? 119 VAL F CA  1 
ATOM   1984  C  C   . VAL B  1 120 ? 66.318  16.063  25.892  1.00 2.00  ? 119 VAL F C   1 
ATOM   1985  O  O   . VAL B  1 120 ? 65.529  16.626  26.647  1.00 2.00  ? 119 VAL F O   1 
ATOM   1986  C  CB  . VAL B  1 120 ? 68.425  17.396  25.314  1.00 2.00  ? 119 VAL F CB  1 
ATOM   1987  C  CG1 . VAL B  1 120 ? 68.179  18.454  26.349  1.00 5.49  ? 119 VAL F CG1 1 
ATOM   1988  C  CG2 . VAL B  1 120 ? 69.299  16.308  25.894  1.00 2.00  ? 119 VAL F CG2 1 
ATOM   1989  N  N   . HIS B  1 121 ? 66.402  14.746  25.758  1.00 3.39  ? 120 HIS F N   1 
ATOM   1990  C  CA  . HIS B  1 121 ? 65.676  13.778  26.525  1.00 2.00  ? 120 HIS F CA  1 
ATOM   1991  C  C   . HIS B  1 121 ? 66.382  13.183  27.733  1.00 2.00  ? 120 HIS F C   1 
ATOM   1992  O  O   . HIS B  1 121 ? 67.607  13.223  27.953  1.00 2.00  ? 120 HIS F O   1 
ATOM   1993  C  CB  . HIS B  1 121 ? 65.247  12.742  25.544  1.00 2.00  ? 120 HIS F CB  1 
ATOM   1994  C  CG  . HIS B  1 121 ? 64.080  13.220  24.675  1.00 2.00  ? 120 HIS F CG  1 
ATOM   1995  N  ND1 . HIS B  1 121 ? 62.796  13.268  24.925  1.00 2.00  ? 120 HIS F ND1 1 
ATOM   1996  C  CD2 . HIS B  1 121 ? 64.224  13.666  23.385  1.00 3.71  ? 120 HIS F CD2 1 
ATOM   1997  C  CE1 . HIS B  1 121 ? 62.191  13.702  23.850  1.00 2.00  ? 120 HIS F CE1 1 
ATOM   1998  N  NE2 . HIS B  1 121 ? 63.059  13.958  22.889  1.00 3.88  ? 120 HIS F NE2 1 
ATOM   1999  N  N   . GLU B  1 122 ? 65.466  12.732  28.557  1.00 2.00  ? 121 GLU F N   1 
ATOM   2000  C  CA  . GLU B  1 122 ? 65.732  12.062  29.796  1.00 2.96  ? 121 GLU F CA  1 
ATOM   2001  C  C   . GLU B  1 122 ? 66.552  10.800  29.574  1.00 2.63  ? 121 GLU F C   1 
ATOM   2002  O  O   . GLU B  1 122 ? 67.593  10.613  30.158  1.00 2.00  ? 121 GLU F O   1 
ATOM   2003  C  CB  . GLU B  1 122 ? 64.421  11.708  30.402  1.00 4.80  ? 121 GLU F CB  1 
ATOM   2004  C  CG  . GLU B  1 122 ? 64.529  11.405  31.874  1.00 8.06  ? 121 GLU F CG  1 
ATOM   2005  C  CD  . GLU B  1 122 ? 63.368  10.636  32.514  1.00 12.17 ? 121 GLU F CD  1 
ATOM   2006  O  OE1 . GLU B  1 122 ? 62.343  10.334  31.845  1.00 12.17 ? 121 GLU F OE1 1 
ATOM   2007  O  OE2 . GLU B  1 122 ? 63.537  10.318  33.706  1.00 12.72 ? 121 GLU F OE2 1 
ATOM   2008  N  N   . LYS B  1 123 ? 66.162  9.930   28.689  1.00 3.09  ? 122 LYS F N   1 
ATOM   2009  C  CA  . LYS B  1 123 ? 66.878  8.691   28.486  1.00 5.14  ? 122 LYS F CA  1 
ATOM   2010  C  C   . LYS B  1 123 ? 67.282  8.641   27.015  1.00 4.54  ? 122 LYS F C   1 
ATOM   2011  O  O   . LYS B  1 123 ? 66.964  9.483   26.163  1.00 3.01  ? 122 LYS F O   1 
ATOM   2012  C  CB  . LYS B  1 123 ? 66.010  7.459   28.736  1.00 8.38  ? 122 LYS F CB  1 
ATOM   2013  C  CG  . LYS B  1 123 ? 64.884  7.458   29.765  1.00 10.05 ? 122 LYS F CG  1 
ATOM   2014  C  CD  . LYS B  1 123 ? 64.070  6.213   29.487  1.00 13.86 ? 122 LYS F CD  1 
ATOM   2015  C  CE  . LYS B  1 123 ? 62.790  6.174   30.314  1.00 21.07 ? 122 LYS F CE  1 
ATOM   2016  N  NZ  . LYS B  1 123 ? 61.773  5.327   29.681  1.00 24.16 ? 122 LYS F NZ  1 
ATOM   2017  N  N   . ALA B  1 124 ? 68.058  7.603   26.802  1.00 2.23  ? 123 ALA F N   1 
ATOM   2018  C  CA  . ALA B  1 124 ? 68.535  7.233   25.496  1.00 2.60  ? 123 ALA F CA  1 
ATOM   2019  C  C   . ALA B  1 124 ? 67.418  6.930   24.539  1.00 2.00  ? 123 ALA F C   1 
ATOM   2020  O  O   . ALA B  1 124 ? 66.375  6.407   24.892  1.00 2.00  ? 123 ALA F O   1 
ATOM   2021  C  CB  . ALA B  1 124 ? 69.414  5.997   25.599  1.00 2.17  ? 123 ALA F CB  1 
ATOM   2022  N  N   . ASP B  1 125 ? 67.673  7.270   23.304  1.00 2.12  ? 124 ASP F N   1 
ATOM   2023  C  CA  . ASP B  1 125 ? 66.767  7.006   22.229  1.00 4.17  ? 124 ASP F CA  1 
ATOM   2024  C  C   . ASP B  1 125 ? 67.156  5.596   21.804  1.00 5.09  ? 124 ASP F C   1 
ATOM   2025  O  O   . ASP B  1 125 ? 68.350  5.408   21.580  1.00 7.43  ? 124 ASP F O   1 
ATOM   2026  C  CB  . ASP B  1 125 ? 67.041  8.025   21.168  1.00 2.61  ? 124 ASP F CB  1 
ATOM   2027  C  CG  . ASP B  1 125 ? 66.175  7.929   19.935  1.00 2.00  ? 124 ASP F CG  1 
ATOM   2028  O  OD1 . ASP B  1 125 ? 65.743  6.860   19.565  1.00 2.00  ? 124 ASP F OD1 1 
ATOM   2029  O  OD2 . ASP B  1 125 ? 65.938  8.939   19.309  1.00 2.00  ? 124 ASP F OD2 1 
ATOM   2030  N  N   . ASP B  1 126 ? 66.252  4.615   21.647  1.00 4.00  ? 125 ASP F N   1 
ATOM   2031  C  CA  . ASP B  1 126 ? 66.624  3.241   21.261  1.00 4.48  ? 125 ASP F CA  1 
ATOM   2032  C  C   . ASP B  1 126 ? 66.777  3.017   19.766  1.00 7.67  ? 125 ASP F C   1 
ATOM   2033  O  O   . ASP B  1 126 ? 66.957  1.899   19.281  1.00 10.62 ? 125 ASP F O   1 
ATOM   2034  C  CB  . ASP B  1 126 ? 65.615  2.212   21.726  1.00 2.00  ? 125 ASP F CB  1 
ATOM   2035  C  CG  . ASP B  1 126 ? 64.166  2.403   21.292  1.00 2.75  ? 125 ASP F CG  1 
ATOM   2036  O  OD1 . ASP B  1 126 ? 63.866  2.983   20.265  1.00 2.00  ? 125 ASP F OD1 1 
ATOM   2037  O  OD2 . ASP B  1 126 ? 63.288  1.949   22.008  1.00 5.87  ? 125 ASP F OD2 1 
ATOM   2038  N  N   . LEU B  1 127 ? 66.581  4.108   19.027  1.00 4.28  ? 126 LEU F N   1 
ATOM   2039  C  CA  . LEU B  1 127 ? 66.783  4.234   17.602  1.00 2.90  ? 126 LEU F CA  1 
ATOM   2040  C  C   . LEU B  1 127 ? 65.816  3.440   16.756  1.00 3.11  ? 126 LEU F C   1 
ATOM   2041  O  O   . LEU B  1 127 ? 65.987  3.223   15.557  1.00 4.38  ? 126 LEU F O   1 
ATOM   2042  C  CB  . LEU B  1 127 ? 68.275  3.876   17.265  1.00 2.00  ? 126 LEU F CB  1 
ATOM   2043  C  CG  . LEU B  1 127 ? 69.376  4.677   18.010  1.00 3.12  ? 126 LEU F CG  1 
ATOM   2044  C  CD1 . LEU B  1 127 ? 70.789  4.244   17.645  1.00 2.00  ? 126 LEU F CD1 1 
ATOM   2045  C  CD2 . LEU B  1 127 ? 69.149  6.175   17.693  1.00 3.04  ? 126 LEU F CD2 1 
ATOM   2046  N  N   . GLY B  1 128 ? 64.685  3.175   17.381  1.00 2.00  ? 127 GLY F N   1 
ATOM   2047  C  CA  . GLY B  1 128 ? 63.597  2.477   16.727  1.00 2.00  ? 127 GLY F CA  1 
ATOM   2048  C  C   . GLY B  1 128 ? 63.740  0.965   16.787  1.00 2.00  ? 127 GLY F C   1 
ATOM   2049  O  O   . GLY B  1 128 ? 62.899  0.206   16.314  1.00 2.00  ? 127 GLY F O   1 
ATOM   2050  N  N   . LYS B  1 129 ? 64.773  0.512   17.474  1.00 2.01  ? 128 LYS F N   1 
ATOM   2051  C  CA  . LYS B  1 129 ? 65.113  -0.875  17.596  1.00 2.00  ? 128 LYS F CA  1 
ATOM   2052  C  C   . LYS B  1 129 ? 64.629  -1.564  18.844  1.00 2.00  ? 128 LYS F C   1 
ATOM   2053  O  O   . LYS B  1 129 ? 65.099  -2.640  19.155  1.00 2.21  ? 128 LYS F O   1 
ATOM   2054  C  CB  . LYS B  1 129 ? 66.616  -0.926  17.461  1.00 2.00  ? 128 LYS F CB  1 
ATOM   2055  C  CG  . LYS B  1 129 ? 66.968  -1.054  15.998  1.00 2.80  ? 128 LYS F CG  1 
ATOM   2056  C  CD  . LYS B  1 129 ? 68.385  -0.696  15.557  1.00 4.49  ? 128 LYS F CD  1 
ATOM   2057  C  CE  . LYS B  1 129 ? 69.437  -1.495  16.256  1.00 4.31  ? 128 LYS F CE  1 
ATOM   2058  N  NZ  . LYS B  1 129 ? 70.693  -1.386  15.554  1.00 11.08 ? 128 LYS F NZ  1 
ATOM   2059  N  N   . GLY B  1 130 ? 63.630  -1.061  19.541  1.00 2.47  ? 129 GLY F N   1 
ATOM   2060  C  CA  . GLY B  1 130 ? 63.260  -1.594  20.825  1.00 2.00  ? 129 GLY F CA  1 
ATOM   2061  C  C   . GLY B  1 130 ? 62.051  -2.464  20.777  1.00 2.00  ? 129 GLY F C   1 
ATOM   2062  O  O   . GLY B  1 130 ? 61.622  -2.937  21.811  1.00 2.00  ? 129 GLY F O   1 
ATOM   2063  N  N   . GLY B  1 131 ? 61.342  -2.610  19.678  1.00 3.06  ? 130 GLY F N   1 
ATOM   2064  C  CA  . GLY B  1 131 ? 60.325  -3.669  19.585  1.00 5.17  ? 130 GLY F CA  1 
ATOM   2065  C  C   . GLY B  1 131 ? 59.015  -3.472  20.301  1.00 6.47  ? 130 GLY F C   1 
ATOM   2066  O  O   . GLY B  1 131 ? 58.471  -4.396  20.920  1.00 9.97  ? 130 GLY F O   1 
ATOM   2067  N  N   . ASN B  1 132 ? 58.492  -2.272  20.189  1.00 2.59  ? 131 ASN F N   1 
ATOM   2068  C  CA  . ASN B  1 132 ? 57.253  -1.949  20.783  1.00 2.00  ? 131 ASN F CA  1 
ATOM   2069  C  C   . ASN B  1 132 ? 56.883  -0.660  20.109  1.00 3.70  ? 131 ASN F C   1 
ATOM   2070  O  O   . ASN B  1 132 ? 57.692  0.031   19.498  1.00 2.85  ? 131 ASN F O   1 
ATOM   2071  C  CB  . ASN B  1 132 ? 57.431  -1.813  22.294  1.00 4.18  ? 131 ASN F CB  1 
ATOM   2072  C  CG  . ASN B  1 132 ? 58.065  -0.598  22.964  1.00 2.76  ? 131 ASN F CG  1 
ATOM   2073  O  OD1 . ASN B  1 132 ? 58.583  0.362   22.418  1.00 2.00  ? 131 ASN F OD1 1 
ATOM   2074  N  ND2 . ASN B  1 132 ? 57.971  -0.642  24.261  1.00 6.67  ? 131 ASN F ND2 1 
ATOM   2075  N  N   . GLU B  1 133 ? 55.626  -0.313  20.211  1.00 6.77  ? 132 GLU F N   1 
ATOM   2076  C  CA  . GLU B  1 133 ? 55.081  0.802   19.480  1.00 9.43  ? 132 GLU F CA  1 
ATOM   2077  C  C   . GLU B  1 133 ? 55.717  2.135   19.796  1.00 10.10 ? 132 GLU F C   1 
ATOM   2078  O  O   . GLU B  1 133 ? 55.905  2.976   18.934  1.00 9.63  ? 132 GLU F O   1 
ATOM   2079  C  CB  . GLU B  1 133 ? 53.592  0.864   19.751  1.00 14.44 ? 132 GLU F CB  1 
ATOM   2080  C  CG  . GLU B  1 133 ? 52.857  1.226   18.448  1.00 23.70 ? 132 GLU F CG  1 
ATOM   2081  C  CD  . GLU B  1 133 ? 51.370  1.522   18.633  1.00 27.10 ? 132 GLU F CD  1 
ATOM   2082  O  OE1 . GLU B  1 133 ? 50.615  0.640   19.065  1.00 28.28 ? 132 GLU F OE1 1 
ATOM   2083  O  OE2 . GLU B  1 133 ? 50.978  2.655   18.342  1.00 30.64 ? 132 GLU F OE2 1 
ATOM   2084  N  N   . GLU B  1 134 ? 56.095  2.332   21.048  1.00 9.52  ? 133 GLU F N   1 
ATOM   2085  C  CA  . GLU B  1 134 ? 56.754  3.537   21.478  1.00 7.49  ? 133 GLU F CA  1 
ATOM   2086  C  C   . GLU B  1 134 ? 58.046  3.714   20.722  1.00 5.93  ? 133 GLU F C   1 
ATOM   2087  O  O   . GLU B  1 134 ? 58.394  4.823   20.342  1.00 11.35 ? 133 GLU F O   1 
ATOM   2088  C  CB  . GLU B  1 134 ? 57.028  3.415   22.945  1.00 8.22  ? 133 GLU F CB  1 
ATOM   2089  C  CG  . GLU B  1 134 ? 57.199  4.732   23.647  1.00 12.27 ? 133 GLU F CG  1 
ATOM   2090  C  CD  . GLU B  1 134 ? 56.015  5.660   23.485  1.00 15.58 ? 133 GLU F CD  1 
ATOM   2091  O  OE1 . GLU B  1 134 ? 54.860  5.229   23.558  1.00 20.12 ? 133 GLU F OE1 1 
ATOM   2092  O  OE2 . GLU B  1 134 ? 56.260  6.836   23.262  1.00 18.24 ? 133 GLU F OE2 1 
ATOM   2093  N  N   . SER B  1 135 ? 58.761  2.639   20.467  1.00 3.91  ? 134 SER F N   1 
ATOM   2094  C  CA  . SER B  1 135 ? 60.029  2.642   19.804  1.00 3.53  ? 134 SER F CA  1 
ATOM   2095  C  C   . SER B  1 135 ? 59.998  3.386   18.500  1.00 2.86  ? 134 SER F C   1 
ATOM   2096  O  O   . SER B  1 135 ? 60.923  4.169   18.268  1.00 6.26  ? 134 SER F O   1 
ATOM   2097  C  CB  . SER B  1 135 ? 60.494  1.236   19.494  1.00 2.89  ? 134 SER F CB  1 
ATOM   2098  O  OG  . SER B  1 135 ? 61.917  1.265   19.368  1.00 5.25  ? 134 SER F OG  1 
ATOM   2099  N  N   . THR B  1 136 ? 58.929  3.187   17.730  1.00 2.81  ? 135 THR F N   1 
ATOM   2100  C  CA  . THR B  1 136 ? 58.765  3.708   16.399  1.00 2.58  ? 135 THR F CA  1 
ATOM   2101  C  C   . THR B  1 136 ? 58.110  5.067   16.445  1.00 4.10  ? 135 THR F C   1 
ATOM   2102  O  O   . THR B  1 136 ? 57.848  5.637   15.369  1.00 5.34  ? 135 THR F O   1 
ATOM   2103  C  CB  . THR B  1 136 ? 57.891  2.781   15.577  1.00 4.93  ? 135 THR F CB  1 
ATOM   2104  O  OG1 . THR B  1 136 ? 56.568  2.927   16.111  1.00 8.11  ? 135 THR F OG1 1 
ATOM   2105  C  CG2 . THR B  1 136 ? 58.310  1.285   15.655  1.00 5.56  ? 135 THR F CG2 1 
ATOM   2106  N  N   . LYS B  1 137 ? 57.699  5.502   17.637  1.00 2.63  ? 136 LYS F N   1 
ATOM   2107  C  CA  . LYS B  1 137 ? 57.041  6.767   17.770  1.00 2.02  ? 136 LYS F CA  1 
ATOM   2108  C  C   . LYS B  1 137 ? 58.078  7.792   18.237  1.00 3.10  ? 136 LYS F C   1 
ATOM   2109  O  O   . LYS B  1 137 ? 58.402  8.746   17.511  1.00 2.65  ? 136 LYS F O   1 
ATOM   2110  C  CB  . LYS B  1 137 ? 55.861  6.641   18.767  1.00 2.00  ? 136 LYS F CB  1 
ATOM   2111  C  CG  . LYS B  1 137 ? 54.561  6.156   18.113  1.00 5.36  ? 136 LYS F CG  1 
ATOM   2112  C  CD  . LYS B  1 137 ? 53.282  6.633   18.790  1.00 13.46 ? 136 LYS F CD  1 
ATOM   2113  C  CE  . LYS B  1 137 ? 52.206  5.632   19.325  1.00 19.70 ? 136 LYS F CE  1 
ATOM   2114  N  NZ  . LYS B  1 137 ? 52.570  4.944   20.584  1.00 24.83 ? 136 LYS F NZ  1 
ATOM   2115  N  N   . THR B  1 138 ? 58.686  7.514   19.388  1.00 2.00  ? 137 THR F N   1 
ATOM   2116  C  CA  . THR B  1 138 ? 59.574  8.399   20.097  1.00 2.07  ? 137 THR F CA  1 
ATOM   2117  C  C   . THR B  1 138 ? 60.991  7.891   20.302  1.00 3.53  ? 137 THR F C   1 
ATOM   2118  O  O   . THR B  1 138 ? 61.934  8.590   20.666  1.00 4.93  ? 137 THR F O   1 
ATOM   2119  C  CB  . THR B  1 138 ? 58.936  8.649   21.442  1.00 7.19  ? 137 THR F CB  1 
ATOM   2120  O  OG1 . THR B  1 138 ? 58.886  7.389   22.164  1.00 5.91  ? 137 THR F OG1 1 
ATOM   2121  C  CG2 . THR B  1 138 ? 57.523  9.214   21.290  1.00 10.46 ? 137 THR F CG2 1 
ATOM   2122  N  N   . GLY B  1 139 ? 61.157  6.584   20.152  1.00 5.48  ? 138 GLY F N   1 
ATOM   2123  C  CA  . GLY B  1 139 ? 62.395  5.911   20.445  1.00 2.00  ? 138 GLY F CA  1 
ATOM   2124  C  C   . GLY B  1 139 ? 62.494  5.656   21.917  1.00 2.00  ? 138 GLY F C   1 
ATOM   2125  O  O   . GLY B  1 139 ? 63.598  5.354   22.325  1.00 3.20  ? 138 GLY F O   1 
ATOM   2126  N  N   . ASN B  1 140 ? 61.427  5.712   22.727  1.00 2.00  ? 139 ASN F N   1 
ATOM   2127  C  CA  . ASN B  1 140 ? 61.479  5.480   24.169  1.00 2.00  ? 139 ASN F CA  1 
ATOM   2128  C  C   . ASN B  1 140 ? 62.385  6.392   24.918  1.00 2.00  ? 139 ASN F C   1 
ATOM   2129  O  O   . ASN B  1 140 ? 62.754  6.086   26.028  1.00 2.00  ? 139 ASN F O   1 
ATOM   2130  C  CB  . ASN B  1 140 ? 61.921  4.044   24.538  1.00 2.40  ? 139 ASN F CB  1 
ATOM   2131  C  CG  . ASN B  1 140 ? 60.756  3.109   24.471  1.00 2.00  ? 139 ASN F CG  1 
ATOM   2132  O  OD1 . ASN B  1 140 ? 59.759  3.313   25.129  1.00 8.28  ? 139 ASN F OD1 1 
ATOM   2133  N  ND2 . ASN B  1 140 ? 60.690  2.103   23.655  1.00 5.19  ? 139 ASN F ND2 1 
ATOM   2134  N  N   . ALA B  1 141 ? 62.598  7.593   24.398  1.00 2.82  ? 140 ALA F N   1 
ATOM   2135  C  CA  . ALA B  1 141 ? 63.534  8.549   24.953  1.00 3.10  ? 140 ALA F CA  1 
ATOM   2136  C  C   . ALA B  1 141 ? 63.116  9.322   26.198  1.00 5.34  ? 140 ALA F C   1 
ATOM   2137  O  O   . ALA B  1 141 ? 63.871  10.173  26.694  1.00 4.84  ? 140 ALA F O   1 
ATOM   2138  C  CB  . ALA B  1 141 ? 63.912  9.546   23.850  1.00 2.06  ? 140 ALA F CB  1 
ATOM   2139  N  N   . GLY B  1 142 ? 61.921  9.050   26.750  1.00 5.23  ? 141 GLY F N   1 
ATOM   2140  C  CA  . GLY B  1 142 ? 61.471  9.651   27.986  1.00 2.57  ? 141 GLY F CA  1 
ATOM   2141  C  C   . GLY B  1 142 ? 61.171  11.117  27.846  1.00 3.74  ? 141 GLY F C   1 
ATOM   2142  O  O   . GLY B  1 142 ? 61.029  11.634  26.742  1.00 3.67  ? 141 GLY F O   1 
ATOM   2143  N  N   . SER B  1 143 ? 61.140  11.782  28.988  1.00 2.96  ? 142 SER F N   1 
ATOM   2144  C  CA  . SER B  1 143 ? 60.786  13.179  29.064  1.00 5.22  ? 142 SER F CA  1 
ATOM   2145  C  C   . SER B  1 143 ? 61.749  14.155  28.409  1.00 3.23  ? 142 SER F C   1 
ATOM   2146  O  O   . SER B  1 143 ? 62.873  13.789  28.103  1.00 2.82  ? 142 SER F O   1 
ATOM   2147  C  CB  . SER B  1 143 ? 60.625  13.593  30.519  1.00 9.19  ? 142 SER F CB  1 
ATOM   2148  O  OG  . SER B  1 143 ? 60.787  12.462  31.379  1.00 17.99 ? 142 SER F OG  1 
ATOM   2149  N  N   . ARG B  1 144 ? 61.328  15.405  28.274  1.00 2.00  ? 143 ARG F N   1 
ATOM   2150  C  CA  . ARG B  1 144 ? 62.020  16.402  27.561  1.00 2.00  ? 143 ARG F CA  1 
ATOM   2151  C  C   . ARG B  1 144 ? 62.596  17.225  28.677  1.00 2.00  ? 143 ARG F C   1 
ATOM   2152  O  O   . ARG B  1 144 ? 61.895  18.010  29.323  1.00 4.95  ? 143 ARG F O   1 
ATOM   2153  C  CB  . ARG B  1 144 ? 60.991  17.153  26.736  1.00 2.00  ? 143 ARG F CB  1 
ATOM   2154  C  CG  . ARG B  1 144 ? 60.134  16.313  25.865  1.00 2.00  ? 143 ARG F CG  1 
ATOM   2155  C  CD  . ARG B  1 144 ? 59.176  17.136  25.071  1.00 2.00  ? 143 ARG F CD  1 
ATOM   2156  N  NE  . ARG B  1 144 ? 58.375  16.221  24.263  1.00 2.00  ? 143 ARG F NE  1 
ATOM   2157  C  CZ  . ARG B  1 144 ? 57.521  16.636  23.326  1.00 2.03  ? 143 ARG F CZ  1 
ATOM   2158  N  NH1 . ARG B  1 144 ? 57.361  17.900  22.959  1.00 7.44  ? 143 ARG F NH1 1 
ATOM   2159  N  NH2 . ARG B  1 144 ? 56.814  15.773  22.644  1.00 4.30  ? 143 ARG F NH2 1 
ATOM   2160  N  N   . LEU B  1 145 ? 63.877  17.077  28.941  1.00 3.06  ? 144 LEU F N   1 
ATOM   2161  C  CA  . LEU B  1 145 ? 64.590  17.823  29.985  1.00 2.09  ? 144 LEU F CA  1 
ATOM   2162  C  C   . LEU B  1 145 ? 64.799  19.314  29.680  1.00 2.00  ? 144 LEU F C   1 
ATOM   2163  O  O   . LEU B  1 145 ? 64.713  20.155  30.581  1.00 2.00  ? 144 LEU F O   1 
ATOM   2164  C  CB  . LEU B  1 145 ? 65.961  17.120  30.227  1.00 2.00  ? 144 LEU F CB  1 
ATOM   2165  C  CG  . LEU B  1 145 ? 65.965  15.631  30.669  1.00 2.00  ? 144 LEU F CG  1 
ATOM   2166  C  CD1 . LEU B  1 145 ? 67.380  15.153  30.919  1.00 2.00  ? 144 LEU F CD1 1 
ATOM   2167  C  CD2 . LEU B  1 145 ? 65.149  15.450  31.914  1.00 2.00  ? 144 LEU F CD2 1 
ATOM   2168  N  N   . ALA B  1 146 ? 65.196  19.661  28.459  1.00 2.00  ? 145 ALA F N   1 
ATOM   2169  C  CA  . ALA B  1 146 ? 65.322  21.037  28.033  1.00 2.00  ? 145 ALA F CA  1 
ATOM   2170  C  C   . ALA B  1 146 ? 65.044  21.059  26.542  1.00 2.00  ? 145 ALA F C   1 
ATOM   2171  O  O   . ALA B  1 146 ? 65.095  20.039  25.838  1.00 2.00  ? 145 ALA F O   1 
ATOM   2172  C  CB  . ALA B  1 146 ? 66.683  21.559  28.230  1.00 2.00  ? 145 ALA F CB  1 
ATOM   2173  N  N   . CYS B  1 147 ? 64.734  22.226  26.040  1.00 2.00  ? 146 CYS F N   1 
ATOM   2174  C  CA  . CYS B  1 147 ? 64.352  22.441  24.676  1.00 2.00  ? 146 CYS F CA  1 
ATOM   2175  C  C   . CYS B  1 147 ? 64.534  23.916  24.423  1.00 2.24  ? 146 CYS F C   1 
ATOM   2176  O  O   . CYS B  1 147 ? 64.742  24.733  25.336  1.00 2.00  ? 146 CYS F O   1 
ATOM   2177  C  CB  . CYS B  1 147 ? 62.907  22.050  24.485  1.00 2.00  ? 146 CYS F CB  1 
ATOM   2178  S  SG  . CYS B  1 147 ? 61.593  22.794  25.512  1.00 5.70  ? 146 CYS F SG  1 
ATOM   2179  N  N   . GLY B  1 148 ? 64.570  24.258  23.145  1.00 3.76  ? 147 GLY F N   1 
ATOM   2180  C  CA  . GLY B  1 148 ? 64.724  25.629  22.744  1.00 2.00  ? 147 GLY F CA  1 
ATOM   2181  C  C   . GLY B  1 148 ? 64.282  25.685  21.336  1.00 2.00  ? 147 GLY F C   1 
ATOM   2182  O  O   . GLY B  1 148 ? 64.352  24.673  20.669  1.00 2.00  ? 147 GLY F O   1 
ATOM   2183  N  N   . VAL B  1 149 ? 63.838  26.843  20.872  1.00 2.73  ? 148 VAL F N   1 
ATOM   2184  C  CA  . VAL B  1 149 ? 63.408  27.042  19.496  1.00 2.88  ? 148 VAL F CA  1 
ATOM   2185  C  C   . VAL B  1 149 ? 64.641  27.369  18.699  1.00 3.04  ? 148 VAL F C   1 
ATOM   2186  O  O   . VAL B  1 149 ? 65.449  28.151  19.214  1.00 3.36  ? 148 VAL F O   1 
ATOM   2187  C  CB  . VAL B  1 149 ? 62.428  28.193  19.415  1.00 2.00  ? 148 VAL F CB  1 
ATOM   2188  C  CG1 . VAL B  1 149 ? 62.223  28.590  17.993  1.00 5.71  ? 148 VAL F CG1 1 
ATOM   2189  C  CG2 . VAL B  1 149 ? 61.077  27.750  19.882  1.00 2.00  ? 148 VAL F CG2 1 
ATOM   2190  N  N   . ILE B  1 150 ? 64.756  26.809  17.491  1.00 2.00  ? 149 ILE F N   1 
ATOM   2191  C  CA  . ILE B  1 150 ? 65.907  26.960  16.614  1.00 2.00  ? 149 ILE F CA  1 
ATOM   2192  C  C   . ILE B  1 150 ? 65.677  28.261  15.924  1.00 2.00  ? 149 ILE F C   1 
ATOM   2193  O  O   . ILE B  1 150 ? 64.624  28.449  15.325  1.00 2.00  ? 149 ILE F O   1 
ATOM   2194  C  CB  . ILE B  1 150 ? 65.934  25.770  15.646  1.00 2.00  ? 149 ILE F CB  1 
ATOM   2195  C  CG1 . ILE B  1 150 ? 66.227  24.501  16.426  1.00 2.00  ? 149 ILE F CG1 1 
ATOM   2196  C  CG2 . ILE B  1 150 ? 66.994  25.971  14.569  1.00 2.00  ? 149 ILE F CG2 1 
ATOM   2197  C  CD1 . ILE B  1 150 ? 65.921  23.271  15.573  1.00 2.00  ? 149 ILE F CD1 1 
ATOM   2198  N  N   . GLY B  1 151 ? 66.631  29.151  15.988  1.00 2.00  ? 150 GLY F N   1 
ATOM   2199  C  CA  . GLY B  1 151 ? 66.436  30.511  15.508  1.00 2.00  ? 150 GLY F CA  1 
ATOM   2200  C  C   . GLY B  1 151 ? 67.494  30.923  14.517  1.00 2.18  ? 150 GLY F C   1 
ATOM   2201  O  O   . GLY B  1 151 ? 68.493  30.232  14.363  1.00 4.80  ? 150 GLY F O   1 
ATOM   2202  N  N   . ILE B  1 152 ? 67.386  32.028  13.819  1.00 2.90  ? 151 ILE F N   1 
ATOM   2203  C  CA  . ILE B  1 152 ? 68.356  32.369  12.802  1.00 4.51  ? 151 ILE F CA  1 
ATOM   2204  C  C   . ILE B  1 152 ? 69.542  33.028  13.467  1.00 7.06  ? 151 ILE F C   1 
ATOM   2205  O  O   . ILE B  1 152 ? 69.362  33.947  14.267  1.00 8.92  ? 151 ILE F O   1 
ATOM   2206  C  CB  . ILE B  1 152 ? 67.684  33.306  11.723  1.00 3.25  ? 151 ILE F CB  1 
ATOM   2207  C  CG1 . ILE B  1 152 ? 66.908  32.426  10.793  1.00 2.00  ? 151 ILE F CG1 1 
ATOM   2208  C  CG2 . ILE B  1 152 ? 68.680  34.056  10.849  1.00 2.08  ? 151 ILE F CG2 1 
ATOM   2209  C  CD1 . ILE B  1 152 ? 65.825  33.199  10.070  1.00 2.00  ? 151 ILE F CD1 1 
ATOM   2210  N  N   . ALA B  1 153 ? 70.747  32.574  13.146  1.00 7.74  ? 152 ALA F N   1 
ATOM   2211  C  CA  . ALA B  1 153 ? 71.953  33.118  13.711  1.00 8.75  ? 152 ALA F CA  1 
ATOM   2212  C  C   . ALA B  1 153 ? 72.831  33.762  12.626  1.00 11.46 ? 152 ALA F C   1 
ATOM   2213  O  O   . ALA B  1 153 ? 72.462  33.874  11.453  1.00 9.77  ? 152 ALA F O   1 
ATOM   2214  C  CB  . ALA B  1 153 ? 72.664  31.966  14.382  1.00 6.70  ? 152 ALA F CB  1 
ATOM   2215  N  N   . GLN B  1 154 ? 74.008  34.200  13.064  1.00 15.10 ? 153 GLN F N   1 
ATOM   2216  C  CA  . GLN B  1 154 ? 75.077  34.776  12.259  1.00 17.98 ? 153 GLN F CA  1 
ATOM   2217  C  C   . GLN B  1 154 ? 76.372  34.257  12.924  1.00 19.52 ? 153 GLN F C   1 
ATOM   2218  O  O   . GLN B  1 154 ? 76.417  34.058  14.163  1.00 24.60 ? 153 GLN F O   1 
ATOM   2219  C  CB  . GLN B  1 154 ? 74.983  36.323  12.291  1.00 19.07 ? 153 GLN F CB  1 
ATOM   2220  C  CG  . GLN B  1 154 ? 75.955  37.183  13.127  1.00 21.92 ? 153 GLN F CG  1 
ATOM   2221  C  CD  . GLN B  1 154 ? 75.618  38.677  13.210  1.00 25.18 ? 153 GLN F CD  1 
ATOM   2222  O  OE1 . GLN B  1 154 ? 75.414  39.236  14.293  1.00 23.31 ? 153 GLN F OE1 1 
ATOM   2223  N  NE2 . GLN B  1 154 ? 75.518  39.424  12.099  1.00 26.21 ? 153 GLN F NE2 1 
ATOM   2224  O  OXT . GLN B  1 154 ? 77.308  33.963  12.189  1.00 17.86 ? 153 GLN F OXT 1 
HETATM 2225  C  C   . ACE C  1 1   ? 107.099 3.864   6.207   1.00 34.85 ? 0   ACE B C   1 
HETATM 2226  O  O   . ACE C  1 1   ? 106.643 4.920   6.697   1.00 35.89 ? 0   ACE B O   1 
HETATM 2227  C  CH3 . ACE C  1 1   ? 106.777 3.425   4.784   1.00 35.26 ? 0   ACE B CH3 1 
ATOM   2228  N  N   . ALA C  1 2   ? 107.859 3.000   6.896   1.00 31.81 ? 1   ALA B N   1 
ATOM   2229  C  CA  . ALA C  1 2   ? 108.278 3.325   8.246   1.00 27.46 ? 1   ALA B CA  1 
ATOM   2230  C  C   . ALA C  1 2   ? 109.706 3.833   8.250   1.00 22.57 ? 1   ALA B C   1 
ATOM   2231  O  O   . ALA C  1 2   ? 110.634 3.107   7.924   1.00 21.55 ? 1   ALA B O   1 
ATOM   2232  C  CB  . ALA C  1 2   ? 108.198 2.107   9.153   1.00 27.30 ? 1   ALA B CB  1 
ATOM   2233  N  N   . THR C  1 3   ? 109.815 5.120   8.528   1.00 18.49 ? 2   THR B N   1 
ATOM   2234  C  CA  . THR C  1 3   ? 111.075 5.765   8.748   1.00 15.50 ? 2   THR B CA  1 
ATOM   2235  C  C   . THR C  1 3   ? 111.531 5.532   10.175  1.00 13.57 ? 2   THR B C   1 
ATOM   2236  O  O   . THR C  1 3   ? 112.739 5.510   10.413  1.00 13.03 ? 2   THR B O   1 
ATOM   2237  C  CB  . THR C  1 3   ? 110.861 7.215   8.457   1.00 17.55 ? 2   THR B CB  1 
ATOM   2238  O  OG1 . THR C  1 3   ? 110.593 7.136   7.069   1.00 23.03 ? 2   THR B OG1 1 
ATOM   2239  C  CG2 . THR C  1 3   ? 112.005 8.207   8.738   1.00 20.96 ? 2   THR B CG2 1 
ATOM   2240  N  N   . LYS C  1 4   ? 110.615 5.411   11.145  1.00 10.43 ? 3   LYS B N   1 
ATOM   2241  C  CA  . LYS C  1 4   ? 110.972 5.180   12.522  1.00 7.98  ? 3   LYS B CA  1 
ATOM   2242  C  C   . LYS C  1 4   ? 110.364 3.888   13.021  1.00 6.37  ? 3   LYS B C   1 
ATOM   2243  O  O   . LYS C  1 4   ? 109.297 3.440   12.582  1.00 6.68  ? 3   LYS B O   1 
ATOM   2244  C  CB  . LYS C  1 4   ? 110.468 6.317   13.387  1.00 10.05 ? 3   LYS B CB  1 
ATOM   2245  C  CG  . LYS C  1 4   ? 111.471 7.358   13.931  1.00 13.85 ? 3   LYS B CG  1 
ATOM   2246  C  CD  . LYS C  1 4   ? 111.895 8.439   12.905  1.00 15.31 ? 3   LYS B CD  1 
ATOM   2247  C  CE  . LYS C  1 4   ? 110.967 9.666   12.796  1.00 20.15 ? 3   LYS B CE  1 
ATOM   2248  N  NZ  . LYS C  1 4   ? 109.648 9.398   12.217  1.00 24.01 ? 3   LYS B NZ  1 
ATOM   2249  N  N   . ALA C  1 5   ? 110.996 3.350   14.039  1.00 4.51  ? 4   ALA B N   1 
ATOM   2250  C  CA  . ALA C  1 5   ? 110.589 2.130   14.692  1.00 2.10  ? 4   ALA B CA  1 
ATOM   2251  C  C   . ALA C  1 5   ? 111.241 2.118   16.065  1.00 2.54  ? 4   ALA B C   1 
ATOM   2252  O  O   . ALA C  1 5   ? 112.240 2.810   16.322  1.00 3.24  ? 4   ALA B O   1 
ATOM   2253  C  CB  . ALA C  1 5   ? 111.077 0.929   13.942  1.00 2.00  ? 4   ALA B CB  1 
ATOM   2254  N  N   . VAL C  1 6   ? 110.661 1.380   17.005  1.00 3.14  ? 5   VAL B N   1 
ATOM   2255  C  CA  . VAL C  1 6   ? 111.193 1.268   18.349  1.00 3.36  ? 5   VAL B CA  1 
ATOM   2256  C  C   . VAL C  1 6   ? 110.966 -0.159  18.915  1.00 3.86  ? 5   VAL B C   1 
ATOM   2257  O  O   . VAL C  1 6   ? 110.089 -0.850  18.388  1.00 2.00  ? 5   VAL B O   1 
ATOM   2258  C  CB  . VAL C  1 6   ? 110.526 2.357   19.198  1.00 2.00  ? 5   VAL B CB  1 
ATOM   2259  C  CG1 . VAL C  1 6   ? 109.070 2.111   19.354  1.00 2.00  ? 5   VAL B CG1 1 
ATOM   2260  C  CG2 . VAL C  1 6   ? 111.188 2.377   20.555  1.00 2.00  ? 5   VAL B CG2 1 
ATOM   2261  N  N   . ALA C  1 7   ? 111.757 -0.669  19.880  1.00 2.00  ? 6   ALA B N   1 
ATOM   2262  C  CA  . ALA C  1 7   ? 111.465 -1.932  20.506  1.00 3.00  ? 6   ALA B CA  1 
ATOM   2263  C  C   . ALA C  1 7   ? 111.712 -1.722  21.979  1.00 4.74  ? 6   ALA B C   1 
ATOM   2264  O  O   . ALA C  1 7   ? 112.766 -1.144  22.292  1.00 7.62  ? 6   ALA B O   1 
ATOM   2265  C  CB  . ALA C  1 7   ? 112.383 -3.051  20.092  1.00 2.00  ? 6   ALA B CB  1 
ATOM   2266  N  N   . VAL C  1 8   ? 110.778 -2.095  22.888  1.00 2.97  ? 7   VAL B N   1 
ATOM   2267  C  CA  . VAL C  1 8   ? 111.042 -2.032  24.314  1.00 2.72  ? 7   VAL B CA  1 
ATOM   2268  C  C   . VAL C  1 8   ? 111.453 -3.460  24.691  1.00 3.86  ? 7   VAL B C   1 
ATOM   2269  O  O   . VAL C  1 8   ? 110.770 -4.452  24.454  1.00 5.84  ? 7   VAL B O   1 
ATOM   2270  C  CB  . VAL C  1 8   ? 109.784 -1.564  25.036  1.00 2.21  ? 7   VAL B CB  1 
ATOM   2271  C  CG1 . VAL C  1 8   ? 110.035 -1.604  26.518  1.00 2.00  ? 7   VAL B CG1 1 
ATOM   2272  C  CG2 . VAL C  1 8   ? 109.459 -0.117  24.661  1.00 2.00  ? 7   VAL B CG2 1 
ATOM   2273  N  N   . LEU C  1 9   ? 112.671 -3.594  25.191  1.00 5.50  ? 8   LEU B N   1 
ATOM   2274  C  CA  . LEU C  1 9   ? 113.320 -4.853  25.521  1.00 3.18  ? 8   LEU B CA  1 
ATOM   2275  C  C   . LEU C  1 9   ? 112.950 -5.141  26.944  1.00 3.24  ? 8   LEU B C   1 
ATOM   2276  O  O   . LEU C  1 9   ? 113.093 -4.252  27.775  1.00 4.25  ? 8   LEU B O   1 
ATOM   2277  C  CB  . LEU C  1 9   ? 114.815 -4.679  25.373  1.00 2.00  ? 8   LEU B CB  1 
ATOM   2278  C  CG  . LEU C  1 9   ? 115.484 -5.283  24.179  1.00 2.00  ? 8   LEU B CG  1 
ATOM   2279  C  CD1 . LEU C  1 9   ? 114.858 -4.813  22.927  1.00 2.63  ? 8   LEU B CD1 1 
ATOM   2280  C  CD2 . LEU C  1 9   ? 116.900 -4.858  24.134  1.00 2.00  ? 8   LEU B CD2 1 
ATOM   2281  N  N   . LYS C  1 10  ? 112.520 -6.351  27.263  1.00 3.12  ? 9   LYS B N   1 
ATOM   2282  C  CA  . LYS C  1 10  ? 112.058 -6.678  28.584  1.00 2.78  ? 9   LYS B CA  1 
ATOM   2283  C  C   . LYS C  1 10  ? 112.188 -8.180  28.806  1.00 4.10  ? 9   LYS B C   1 
ATOM   2284  O  O   . LYS C  1 10  ? 112.158 -8.954  27.847  1.00 4.53  ? 9   LYS B O   1 
ATOM   2285  C  CB  . LYS C  1 10  ? 110.665 -6.236  28.618  1.00 4.98  ? 9   LYS B CB  1 
ATOM   2286  C  CG  . LYS C  1 10  ? 110.385 -5.561  29.902  1.00 17.33 ? 9   LYS B CG  1 
ATOM   2287  C  CD  . LYS C  1 10  ? 108.957 -5.011  29.776  1.00 23.98 ? 9   LYS B CD  1 
ATOM   2288  C  CE  . LYS C  1 10  ? 108.954 -3.498  29.454  1.00 27.52 ? 9   LYS B CE  1 
ATOM   2289  N  NZ  . LYS C  1 10  ? 107.630 -2.923  29.639  1.00 29.18 ? 9   LYS B NZ  1 
ATOM   2290  N  N   . GLY C  1 11  ? 112.359 -8.690  30.012  1.00 5.16  ? 10  GLY B N   1 
ATOM   2291  C  CA  . GLY C  1 11  ? 112.519 -10.115 30.154  1.00 9.02  ? 10  GLY B CA  1 
ATOM   2292  C  C   . GLY C  1 11  ? 112.076 -10.565 31.523  1.00 11.93 ? 10  GLY B C   1 
ATOM   2293  O  O   . GLY C  1 11  ? 111.368 -9.870  32.248  1.00 12.75 ? 10  GLY B O   1 
ATOM   2294  N  N   . ASP C  1 12  ? 112.502 -11.763 31.854  1.00 12.61 ? 11  ASP B N   1 
ATOM   2295  C  CA  . ASP C  1 12  ? 112.216 -12.311 33.149  1.00 15.80 ? 11  ASP B CA  1 
ATOM   2296  C  C   . ASP C  1 12  ? 113.088 -11.755 34.279  1.00 14.03 ? 11  ASP B C   1 
ATOM   2297  O  O   . ASP C  1 12  ? 112.653 -11.689 35.432  1.00 16.17 ? 11  ASP B O   1 
ATOM   2298  C  CB  . ASP C  1 12  ? 112.359 -13.837 33.031  1.00 24.20 ? 11  ASP B CB  1 
ATOM   2299  C  CG  . ASP C  1 12  ? 111.111 -14.511 32.463  1.00 31.96 ? 11  ASP B CG  1 
ATOM   2300  O  OD1 . ASP C  1 12  ? 110.233 -14.833 33.274  1.00 35.92 ? 11  ASP B OD1 1 
ATOM   2301  O  OD2 . ASP C  1 12  ? 111.014 -14.707 31.236  1.00 36.75 ? 11  ASP B OD2 1 
ATOM   2302  N  N   . GLY C  1 13  ? 114.348 -11.456 33.986  1.00 9.88  ? 12  GLY B N   1 
ATOM   2303  C  CA  . GLY C  1 13  ? 115.256 -10.943 34.967  1.00 6.27  ? 12  GLY B CA  1 
ATOM   2304  C  C   . GLY C  1 13  ? 115.366 -9.437  34.881  1.00 5.66  ? 12  GLY B C   1 
ATOM   2305  O  O   . GLY C  1 13  ? 114.429 -8.718  34.559  1.00 7.07  ? 12  GLY B O   1 
ATOM   2306  N  N   . PRO C  1 14  ? 116.552 -8.889  35.123  1.00 6.00  ? 13  PRO B N   1 
ATOM   2307  C  CA  . PRO C  1 14  ? 116.803 -7.476  35.380  1.00 4.85  ? 13  PRO B CA  1 
ATOM   2308  C  C   . PRO C  1 14  ? 116.973 -6.487  34.224  1.00 6.55  ? 13  PRO B C   1 
ATOM   2309  O  O   . PRO C  1 14  ? 116.866 -5.266  34.470  1.00 6.52  ? 13  PRO B O   1 
ATOM   2310  C  CB  . PRO C  1 14  ? 118.009 -7.498  36.221  1.00 2.00  ? 13  PRO B CB  1 
ATOM   2311  C  CG  . PRO C  1 14  ? 118.640 -8.857  36.083  1.00 2.96  ? 13  PRO B CG  1 
ATOM   2312  C  CD  . PRO C  1 14  ? 117.813 -9.615  35.072  1.00 5.79  ? 13  PRO B CD  1 
ATOM   2313  N  N   . VAL C  1 15  ? 117.231 -6.986  32.990  1.00 6.49  ? 14  VAL B N   1 
ATOM   2314  C  CA  . VAL C  1 15  ? 117.642 -6.098  31.903  1.00 8.30  ? 14  VAL B CA  1 
ATOM   2315  C  C   . VAL C  1 15  ? 116.513 -5.552  31.054  1.00 8.68  ? 14  VAL B C   1 
ATOM   2316  O  O   . VAL C  1 15  ? 115.620 -6.257  30.589  1.00 11.60 ? 14  VAL B O   1 
ATOM   2317  C  CB  . VAL C  1 15  ? 118.786 -6.823  30.985  1.00 9.64  ? 14  VAL B CB  1 
ATOM   2318  C  CG1 . VAL C  1 15  ? 118.693 -8.307  31.005  1.00 4.05  ? 14  VAL B CG1 1 
ATOM   2319  C  CG2 . VAL C  1 15  ? 118.606 -6.568  29.496  1.00 8.15  ? 14  VAL B CG2 1 
ATOM   2320  N  N   . GLN C  1 16  ? 116.590 -4.264  30.809  1.00 9.40  ? 15  GLN B N   1 
ATOM   2321  C  CA  . GLN C  1 16  ? 115.580 -3.565  30.043  1.00 8.99  ? 15  GLN B CA  1 
ATOM   2322  C  C   . GLN C  1 16  ? 116.138 -2.381  29.261  1.00 6.12  ? 15  GLN B C   1 
ATOM   2323  O  O   . GLN C  1 16  ? 117.119 -1.747  29.648  1.00 7.48  ? 15  GLN B O   1 
ATOM   2324  C  CB  . GLN C  1 16  ? 114.485 -3.124  31.007  1.00 12.57 ? 15  GLN B CB  1 
ATOM   2325  C  CG  . GLN C  1 16  ? 114.830 -2.255  32.199  1.00 16.71 ? 15  GLN B CG  1 
ATOM   2326  C  CD  . GLN C  1 16  ? 113.969 -2.609  33.411  1.00 18.97 ? 15  GLN B CD  1 
ATOM   2327  O  OE1 . GLN C  1 16  ? 112.799 -2.238  33.569  1.00 19.51 ? 15  GLN B OE1 1 
ATOM   2328  N  NE2 . GLN C  1 16  ? 114.554 -3.382  34.314  1.00 20.97 ? 15  GLN B NE2 1 
ATOM   2329  N  N   . GLY C  1 17  ? 115.544 -2.068  28.128  1.00 6.10  ? 16  GLY B N   1 
ATOM   2330  C  CA  . GLY C  1 17  ? 116.011 -0.989  27.281  1.00 3.62  ? 16  GLY B CA  1 
ATOM   2331  C  C   . GLY C  1 17  ? 114.965 -0.631  26.247  1.00 2.40  ? 16  GLY B C   1 
ATOM   2332  O  O   . GLY C  1 17  ? 113.939 -1.295  26.134  1.00 2.11  ? 16  GLY B O   1 
ATOM   2333  N  N   . ILE C  1 18  ? 115.219 0.456   25.546  1.00 2.00  ? 17  ILE B N   1 
ATOM   2334  C  CA  . ILE C  1 18  ? 114.383 0.996   24.508  1.00 2.72  ? 17  ILE B CA  1 
ATOM   2335  C  C   . ILE C  1 18  ? 115.417 1.195   23.450  1.00 4.97  ? 17  ILE B C   1 
ATOM   2336  O  O   . ILE C  1 18  ? 116.414 1.901   23.706  1.00 6.33  ? 17  ILE B O   1 
ATOM   2337  C  CB  . ILE C  1 18  ? 113.820 2.331   24.882  1.00 2.00  ? 17  ILE B CB  1 
ATOM   2338  C  CG1 . ILE C  1 18  ? 112.963 2.126   26.089  1.00 5.69  ? 17  ILE B CG1 1 
ATOM   2339  C  CG2 . ILE C  1 18  ? 112.969 2.909   23.781  1.00 2.83  ? 17  ILE B CG2 1 
ATOM   2340  C  CD1 . ILE C  1 18  ? 112.339 3.397   26.647  1.00 7.35  ? 17  ILE B CD1 1 
ATOM   2341  N  N   . ILE C  1 19  ? 115.191 0.523   22.319  1.00 5.17  ? 18  ILE B N   1 
ATOM   2342  C  CA  . ILE C  1 19  ? 116.082 0.618   21.155  1.00 4.94  ? 18  ILE B CA  1 
ATOM   2343  C  C   . ILE C  1 19  ? 115.262 1.307   20.065  1.00 4.36  ? 18  ILE B C   1 
ATOM   2344  O  O   . ILE C  1 19  ? 114.105 0.935   19.836  1.00 3.77  ? 18  ILE B O   1 
ATOM   2345  C  CB  . ILE C  1 19  ? 116.525 -0.798  20.640  1.00 5.25  ? 18  ILE B CB  1 
ATOM   2346  C  CG1 . ILE C  1 19  ? 117.283 -1.561  21.770  1.00 4.25  ? 18  ILE B CG1 1 
ATOM   2347  C  CG2 . ILE C  1 19  ? 117.375 -0.653  19.373  1.00 4.08  ? 18  ILE B CG2 1 
ATOM   2348  C  CD1 . ILE C  1 19  ? 118.683 -1.140  22.193  1.00 2.00  ? 18  ILE B CD1 1 
ATOM   2349  N  N   . ASN C  1 20  ? 115.832 2.326   19.432  1.00 4.36  ? 19  ASN B N   1 
ATOM   2350  C  CA  . ASN C  1 20  ? 115.265 3.005   18.261  1.00 3.61  ? 19  ASN B CA  1 
ATOM   2351  C  C   . ASN C  1 20  ? 115.874 2.677   16.940  1.00 2.00  ? 19  ASN B C   1 
ATOM   2352  O  O   . ASN C  1 20  ? 117.066 2.411   16.850  1.00 2.00  ? 19  ASN B O   1 
ATOM   2353  C  CB  . ASN C  1 20  ? 115.392 4.467   18.337  1.00 3.86  ? 19  ASN B CB  1 
ATOM   2354  C  CG  . ASN C  1 20  ? 114.656 4.869   19.548  1.00 5.56  ? 19  ASN B CG  1 
ATOM   2355  O  OD1 . ASN C  1 20  ? 115.179 4.620   20.632  1.00 15.48 ? 19  ASN B OD1 1 
ATOM   2356  N  ND2 . ASN C  1 20  ? 113.439 5.385   19.445  1.00 7.98  ? 19  ASN B ND2 1 
ATOM   2357  N  N   . PHE C  1 21  ? 115.077 2.722   15.893  1.00 2.31  ? 20  PHE B N   1 
ATOM   2358  C  CA  . PHE C  1 21  ? 115.623 2.521   14.558  1.00 2.92  ? 20  PHE B CA  1 
ATOM   2359  C  C   . PHE C  1 21  ? 115.105 3.671   13.750  1.00 2.86  ? 20  PHE B C   1 
ATOM   2360  O  O   . PHE C  1 21  ? 114.051 4.258   14.021  1.00 2.00  ? 20  PHE B O   1 
ATOM   2361  C  CB  . PHE C  1 21  ? 115.146 1.287   13.876  1.00 2.00  ? 20  PHE B CB  1 
ATOM   2362  C  CG  . PHE C  1 21  ? 115.367 0.024   14.688  1.00 2.44  ? 20  PHE B CG  1 
ATOM   2363  C  CD1 . PHE C  1 21  ? 114.544 -0.258  15.767  1.00 2.00  ? 20  PHE B CD1 1 
ATOM   2364  C  CD2 . PHE C  1 21  ? 116.347 -0.862  14.303  1.00 2.00  ? 20  PHE B CD2 1 
ATOM   2365  C  CE1 . PHE C  1 21  ? 114.704 -1.433  16.437  1.00 2.08  ? 20  PHE B CE1 1 
ATOM   2366  C  CE2 . PHE C  1 21  ? 116.499 -2.046  14.980  1.00 2.00  ? 20  PHE B CE2 1 
ATOM   2367  C  CZ  . PHE C  1 21  ? 115.680 -2.330  16.045  1.00 3.58  ? 20  PHE B CZ  1 
ATOM   2368  N  N   . GLU C  1 22  ? 115.906 4.054   12.796  1.00 2.93  ? 21  GLU B N   1 
ATOM   2369  C  CA  . GLU C  1 22  ? 115.477 5.102   11.942  1.00 5.42  ? 21  GLU B CA  1 
ATOM   2370  C  C   . GLU C  1 22  ? 116.096 4.843   10.587  1.00 5.00  ? 21  GLU B C   1 
ATOM   2371  O  O   . GLU C  1 22  ? 117.258 4.464   10.568  1.00 6.80  ? 21  GLU B O   1 
ATOM   2372  C  CB  . GLU C  1 22  ? 115.937 6.378   12.584  1.00 6.73  ? 21  GLU B CB  1 
ATOM   2373  C  CG  . GLU C  1 22  ? 115.386 7.494   11.759  1.00 11.24 ? 21  GLU B CG  1 
ATOM   2374  C  CD  . GLU C  1 22  ? 116.000 8.814   12.096  1.00 11.24 ? 21  GLU B CD  1 
ATOM   2375  O  OE1 . GLU C  1 22  ? 117.225 8.896   12.266  1.00 15.03 ? 21  GLU B OE1 1 
ATOM   2376  O  OE2 . GLU C  1 22  ? 115.227 9.761   12.160  1.00 13.46 ? 21  GLU B OE2 1 
ATOM   2377  N  N   . GLN C  1 23  ? 115.363 4.987   9.483   1.00 6.28  ? 22  GLN B N   1 
ATOM   2378  C  CA  . GLN C  1 23  ? 115.795 4.762   8.097   1.00 6.20  ? 22  GLN B CA  1 
ATOM   2379  C  C   . GLN C  1 23  ? 115.251 5.962   7.360   1.00 8.93  ? 22  GLN B C   1 
ATOM   2380  O  O   . GLN C  1 23  ? 114.044 6.128   7.251   1.00 11.42 ? 22  GLN B O   1 
ATOM   2381  C  CB  . GLN C  1 23  ? 115.150 3.545   7.490   1.00 2.00  ? 22  GLN B CB  1 
ATOM   2382  C  CG  . GLN C  1 23  ? 115.722 3.110   6.189   1.00 3.02  ? 22  GLN B CG  1 
ATOM   2383  C  CD  . GLN C  1 23  ? 115.295 1.740   5.672   1.00 2.00  ? 22  GLN B CD  1 
ATOM   2384  O  OE1 . GLN C  1 23  ? 114.237 1.251   5.994   1.00 3.57  ? 22  GLN B OE1 1 
ATOM   2385  N  NE2 . GLN C  1 23  ? 116.007 0.997   4.871   1.00 2.00  ? 22  GLN B NE2 1 
ATOM   2386  N  N   . LYS C  1 24  ? 116.077 6.879   6.889   1.00 13.09 ? 23  LYS B N   1 
ATOM   2387  C  CA  . LYS C  1 24  ? 115.586 8.018   6.139   1.00 12.88 ? 23  LYS B CA  1 
ATOM   2388  C  C   . LYS C  1 24  ? 115.172 7.625   4.735   1.00 12.97 ? 23  LYS B C   1 
ATOM   2389  O  O   . LYS C  1 24  ? 114.352 8.311   4.131   1.00 13.04 ? 23  LYS B O   1 
ATOM   2390  C  CB  . LYS C  1 24  ? 116.661 9.037   6.087   1.00 16.04 ? 23  LYS B CB  1 
ATOM   2391  C  CG  . LYS C  1 24  ? 116.518 10.026  7.211   1.00 23.99 ? 23  LYS B CG  1 
ATOM   2392  C  CD  . LYS C  1 24  ? 117.905 10.476  7.738   1.00 29.71 ? 23  LYS B CD  1 
ATOM   2393  C  CE  . LYS C  1 24  ? 118.466 9.509   8.814   1.00 29.76 ? 23  LYS B CE  1 
ATOM   2394  N  NZ  . LYS C  1 24  ? 119.786 9.910   9.272   1.00 31.17 ? 23  LYS B NZ  1 
ATOM   2395  N  N   . GLU C  1 25  ? 115.694 6.540   4.153   1.00 12.88 ? 24  GLU B N   1 
ATOM   2396  C  CA  . GLU C  1 25  ? 115.299 6.170   2.796   1.00 14.16 ? 24  GLU B CA  1 
ATOM   2397  C  C   . GLU C  1 25  ? 115.167 4.663   2.636   1.00 14.25 ? 24  GLU B C   1 
ATOM   2398  O  O   . GLU C  1 25  ? 116.004 3.928   3.170   1.00 12.46 ? 24  GLU B O   1 
ATOM   2399  C  CB  . GLU C  1 25  ? 116.297 6.604   1.733   1.00 15.59 ? 24  GLU B CB  1 
ATOM   2400  C  CG  . GLU C  1 25  ? 117.396 7.562   2.151   1.00 20.82 ? 24  GLU B CG  1 
ATOM   2401  C  CD  . GLU C  1 25  ? 117.628 8.737   1.218   1.00 24.22 ? 24  GLU B CD  1 
ATOM   2402  O  OE1 . GLU C  1 25  ? 116.647 9.292   0.693   1.00 26.46 ? 24  GLU B OE1 1 
ATOM   2403  O  OE2 . GLU C  1 25  ? 118.802 9.094   1.047   1.00 24.77 ? 24  GLU B OE2 1 
ATOM   2404  N  N   . SER C  1 26  ? 114.164 4.225   1.856   1.00 13.68 ? 25  SER B N   1 
ATOM   2405  C  CA  . SER C  1 26  ? 113.877 2.829   1.596   1.00 15.33 ? 25  SER B CA  1 
ATOM   2406  C  C   . SER C  1 26  ? 115.118 1.989   1.324   1.00 15.67 ? 25  SER B C   1 
ATOM   2407  O  O   . SER C  1 26  ? 115.213 0.861   1.825   1.00 20.08 ? 25  SER B O   1 
ATOM   2408  C  CB  . SER C  1 26  ? 112.929 2.691   0.390   1.00 17.57 ? 25  SER B CB  1 
ATOM   2409  O  OG  . SER C  1 26  ? 113.090 3.725   -0.605  1.00 23.67 ? 25  SER B OG  1 
ATOM   2410  N  N   . ASN C  1 27  ? 116.094 2.512   0.575   1.00 11.42 ? 26  ASN B N   1 
ATOM   2411  C  CA  . ASN C  1 27  ? 117.249 1.725   0.276   1.00 8.19  ? 26  ASN B CA  1 
ATOM   2412  C  C   . ASN C  1 27  ? 118.531 2.205   0.918   1.00 7.21  ? 26  ASN B C   1 
ATOM   2413  O  O   . ASN C  1 27  ? 119.644 1.817   0.594   1.00 4.14  ? 26  ASN B O   1 
ATOM   2414  C  CB  . ASN C  1 27  ? 117.324 1.618   -1.257  1.00 10.07 ? 26  ASN B CB  1 
ATOM   2415  C  CG  . ASN C  1 27  ? 117.760 2.753   -2.163  1.00 11.14 ? 26  ASN B CG  1 
ATOM   2416  O  OD1 . ASN C  1 27  ? 117.458 3.949   -1.988  1.00 8.70  ? 26  ASN B OD1 1 
ATOM   2417  N  ND2 . ASN C  1 27  ? 118.451 2.268   -3.209  1.00 14.49 ? 26  ASN B ND2 1 
ATOM   2418  N  N   . GLY C  1 28  ? 118.268 2.909   2.011   1.00 7.40  ? 27  GLY B N   1 
ATOM   2419  C  CA  . GLY C  1 28  ? 119.283 3.438   2.871   1.00 7.30  ? 27  GLY B CA  1 
ATOM   2420  C  C   . GLY C  1 28  ? 119.580 2.513   4.062   1.00 11.24 ? 27  GLY B C   1 
ATOM   2421  O  O   . GLY C  1 28  ? 119.085 1.349   4.210   1.00 8.94  ? 27  GLY B O   1 
ATOM   2422  N  N   . PRO C  1 29  ? 120.440 3.099   4.943   1.00 10.85 ? 28  PRO B N   1 
ATOM   2423  C  CA  . PRO C  1 29  ? 120.897 2.465   6.174   1.00 11.45 ? 28  PRO B CA  1 
ATOM   2424  C  C   . PRO C  1 29  ? 119.961 2.767   7.312   1.00 10.93 ? 28  PRO B C   1 
ATOM   2425  O  O   . PRO C  1 29  ? 119.516 3.906   7.504   1.00 12.57 ? 28  PRO B O   1 
ATOM   2426  C  CB  . PRO C  1 29  ? 122.309 3.009   6.438   1.00 8.55  ? 28  PRO B CB  1 
ATOM   2427  C  CG  . PRO C  1 29  ? 122.639 3.740   5.169   1.00 5.59  ? 28  PRO B CG  1 
ATOM   2428  C  CD  . PRO C  1 29  ? 121.303 4.252   4.709   1.00 6.57  ? 28  PRO B CD  1 
ATOM   2429  N  N   . VAL C  1 30  ? 119.691 1.728   8.079   1.00 12.21 ? 29  VAL B N   1 
ATOM   2430  C  CA  . VAL C  1 30  ? 118.919 1.883   9.287   1.00 8.68  ? 29  VAL B CA  1 
ATOM   2431  C  C   . VAL C  1 30  ? 119.945 2.149   10.383  1.00 11.97 ? 29  VAL B C   1 
ATOM   2432  O  O   . VAL C  1 30  ? 120.849 1.304   10.608  1.00 12.92 ? 29  VAL B O   1 
ATOM   2433  C  CB  . VAL C  1 30  ? 118.180 0.603   9.515   1.00 7.32  ? 29  VAL B CB  1 
ATOM   2434  C  CG1 . VAL C  1 30  ? 117.372 0.645   10.790  1.00 6.87  ? 29  VAL B CG1 1 
ATOM   2435  C  CG2 . VAL C  1 30  ? 117.232 0.414   8.369   1.00 5.83  ? 29  VAL B CG2 1 
ATOM   2436  N  N   . LYS C  1 31  ? 119.807 3.358   10.952  1.00 7.29  ? 30  LYS B N   1 
ATOM   2437  C  CA  . LYS C  1 31  ? 120.474 3.834   12.149  1.00 6.21  ? 30  LYS B CA  1 
ATOM   2438  C  C   . LYS C  1 31  ? 119.819 3.219   13.423  1.00 7.04  ? 30  LYS B C   1 
ATOM   2439  O  O   . LYS C  1 31  ? 118.595 3.203   13.606  1.00 7.98  ? 30  LYS B O   1 
ATOM   2440  C  CB  . LYS C  1 31  ? 120.372 5.353   12.133  1.00 8.13  ? 30  LYS B CB  1 
ATOM   2441  C  CG  . LYS C  1 31  ? 120.851 6.065   13.373  1.00 13.37 ? 30  LYS B CG  1 
ATOM   2442  C  CD  . LYS C  1 31  ? 122.323 5.727   13.557  1.00 19.93 ? 30  LYS B CD  1 
ATOM   2443  C  CE  . LYS C  1 31  ? 122.894 6.023   14.958  1.00 23.82 ? 30  LYS B CE  1 
ATOM   2444  N  NZ  . LYS C  1 31  ? 124.251 5.478   15.043  1.00 26.01 ? 30  LYS B NZ  1 
ATOM   2445  N  N   . VAL C  1 32  ? 120.577 2.708   14.375  1.00 4.71  ? 31  VAL B N   1 
ATOM   2446  C  CA  . VAL C  1 32  ? 120.026 1.945   15.474  1.00 3.84  ? 31  VAL B CA  1 
ATOM   2447  C  C   . VAL C  1 32  ? 120.572 2.546   16.747  1.00 3.53  ? 31  VAL B C   1 
ATOM   2448  O  O   . VAL C  1 32  ? 121.791 2.702   16.846  1.00 4.97  ? 31  VAL B O   1 
ATOM   2449  C  CB  . VAL C  1 32  ? 120.473 0.473   15.299  1.00 2.43  ? 31  VAL B CB  1 
ATOM   2450  C  CG1 . VAL C  1 32  ? 119.886 -0.360  16.410  1.00 2.00  ? 31  VAL B CG1 1 
ATOM   2451  C  CG2 . VAL C  1 32  ? 120.028 -0.058  13.920  1.00 2.00  ? 31  VAL B CG2 1 
ATOM   2452  N  N   . TRP C  1 33  ? 119.806 2.934   17.741  1.00 2.00  ? 32  TRP B N   1 
ATOM   2453  C  CA  . TRP C  1 33  ? 120.402 3.488   18.929  1.00 2.90  ? 32  TRP B CA  1 
ATOM   2454  C  C   . TRP C  1 33  ? 119.543 3.368   20.205  1.00 2.88  ? 32  TRP B C   1 
ATOM   2455  O  O   . TRP C  1 33  ? 118.335 3.207   20.108  1.00 4.10  ? 32  TRP B O   1 
ATOM   2456  C  CB  . TRP C  1 33  ? 120.753 4.933   18.586  1.00 2.38  ? 32  TRP B CB  1 
ATOM   2457  C  CG  . TRP C  1 33  ? 119.626 5.938   18.561  1.00 5.53  ? 32  TRP B CG  1 
ATOM   2458  C  CD1 . TRP C  1 33  ? 119.394 6.699   19.679  1.00 7.96  ? 32  TRP B CD1 1 
ATOM   2459  C  CD2 . TRP C  1 33  ? 118.750 6.215   17.531  1.00 7.85  ? 32  TRP B CD2 1 
ATOM   2460  N  NE1 . TRP C  1 33  ? 118.368 7.468   19.372  1.00 12.15 ? 32  TRP B NE1 1 
ATOM   2461  C  CE2 . TRP C  1 33  ? 117.960 7.214   18.098  1.00 9.79  ? 32  TRP B CE2 1 
ATOM   2462  C  CE3 . TRP C  1 33  ? 118.496 5.818   16.241  1.00 10.00 ? 32  TRP B CE3 1 
ATOM   2463  C  CZ2 . TRP C  1 33  ? 116.921 7.798   17.393  1.00 6.84  ? 32  TRP B CZ2 1 
ATOM   2464  C  CZ3 . TRP C  1 33  ? 117.456 6.395   15.549  1.00 10.00 ? 32  TRP B CZ3 1 
ATOM   2465  C  CH2 . TRP C  1 33  ? 116.677 7.388   16.108  1.00 8.64  ? 32  TRP B CH2 1 
ATOM   2466  N  N   . GLY C  1 34  ? 120.083 3.372   21.416  1.00 2.55  ? 33  GLY B N   1 
ATOM   2467  C  CA  . GLY C  1 34  ? 119.320 3.362   22.668  1.00 4.07  ? 33  GLY B CA  1 
ATOM   2468  C  C   . GLY C  1 34  ? 120.199 2.810   23.789  1.00 5.15  ? 33  GLY B C   1 
ATOM   2469  O  O   . GLY C  1 34  ? 121.415 2.770   23.602  1.00 6.29  ? 33  GLY B O   1 
ATOM   2470  N  N   . SER C  1 35  ? 119.671 2.322   24.916  1.00 6.89  ? 34  SER B N   1 
ATOM   2471  C  CA  . SER C  1 35  ? 120.469 1.733   25.993  1.00 6.09  ? 34  SER B CA  1 
ATOM   2472  C  C   . SER C  1 35  ? 119.857 0.432   26.406  1.00 3.52  ? 34  SER B C   1 
ATOM   2473  O  O   . SER C  1 35  ? 118.760 0.096   26.021  1.00 5.11  ? 34  SER B O   1 
ATOM   2474  C  CB  . SER C  1 35  ? 120.502 2.502   27.280  1.00 3.51  ? 34  SER B CB  1 
ATOM   2475  O  OG  . SER C  1 35  ? 120.646 3.886   27.095  1.00 13.61 ? 34  SER B OG  1 
ATOM   2476  N  N   . ILE C  1 36  ? 120.550 -0.337  27.180  1.00 2.98  ? 35  ILE B N   1 
ATOM   2477  C  CA  . ILE C  1 36  ? 119.992 -1.518  27.746  1.00 5.48  ? 35  ILE B CA  1 
ATOM   2478  C  C   . ILE C  1 36  ? 120.635 -1.434  29.140  1.00 5.26  ? 35  ILE B C   1 
ATOM   2479  O  O   . ILE C  1 36  ? 121.878 -1.337  29.221  1.00 3.23  ? 35  ILE B O   1 
ATOM   2480  C  CB  . ILE C  1 36  ? 120.460 -2.782  26.913  1.00 5.88  ? 35  ILE B CB  1 
ATOM   2481  C  CG1 . ILE C  1 36  ? 120.106 -2.705  25.422  1.00 3.05  ? 35  ILE B CG1 1 
ATOM   2482  C  CG2 . ILE C  1 36  ? 119.735 -3.991  27.448  1.00 2.00  ? 35  ILE B CG2 1 
ATOM   2483  C  CD1 . ILE C  1 36  ? 120.705 -3.872  24.586  1.00 6.79  ? 35  ILE B CD1 1 
ATOM   2484  N  N   . LYS C  1 37  ? 119.881 -1.319  30.250  1.00 5.02  ? 36  LYS B N   1 
ATOM   2485  C  CA  . LYS C  1 37  ? 120.542 -1.473  31.540  1.00 4.43  ? 36  LYS B CA  1 
ATOM   2486  C  C   . LYS C  1 37  ? 120.324 -2.875  32.083  1.00 2.46  ? 36  LYS B C   1 
ATOM   2487  O  O   . LYS C  1 37  ? 119.594 -3.626  31.444  1.00 3.08  ? 36  LYS B O   1 
ATOM   2488  C  CB  . LYS C  1 37  ? 120.026 -0.453  32.490  1.00 4.88  ? 36  LYS B CB  1 
ATOM   2489  C  CG  . LYS C  1 37  ? 118.608 -0.580  32.863  1.00 12.40 ? 36  LYS B CG  1 
ATOM   2490  C  CD  . LYS C  1 37  ? 118.208 0.835   33.202  1.00 18.63 ? 36  LYS B CD  1 
ATOM   2491  C  CE  . LYS C  1 37  ? 116.744 0.907   33.684  1.00 25.07 ? 36  LYS B CE  1 
ATOM   2492  N  NZ  . LYS C  1 37  ? 116.258 2.296   33.730  1.00 30.11 ? 36  LYS B NZ  1 
ATOM   2493  N  N   . GLY C  1 38  ? 120.967 -3.326  33.171  1.00 3.12  ? 37  GLY B N   1 
ATOM   2494  C  CA  . GLY C  1 38  ? 120.699 -4.620  33.817  1.00 2.87  ? 37  GLY B CA  1 
ATOM   2495  C  C   . GLY C  1 38  ? 121.540 -5.785  33.320  1.00 5.45  ? 37  GLY B C   1 
ATOM   2496  O  O   . GLY C  1 38  ? 121.354 -6.973  33.621  1.00 4.36  ? 37  GLY B O   1 
ATOM   2497  N  N   . LEU C  1 39  ? 122.584 -5.397  32.603  1.00 9.92  ? 38  LEU B N   1 
ATOM   2498  C  CA  . LEU C  1 39  ? 123.411 -6.315  31.858  1.00 8.43  ? 38  LEU B CA  1 
ATOM   2499  C  C   . LEU C  1 39  ? 124.668 -6.572  32.691  1.00 8.53  ? 38  LEU B C   1 
ATOM   2500  O  O   . LEU C  1 39  ? 125.064 -5.808  33.572  1.00 8.47  ? 38  LEU B O   1 
ATOM   2501  C  CB  . LEU C  1 39  ? 123.569 -5.572  30.534  1.00 6.18  ? 38  LEU B CB  1 
ATOM   2502  C  CG  . LEU C  1 39  ? 123.291 -6.074  29.112  1.00 6.14  ? 38  LEU B CG  1 
ATOM   2503  C  CD1 . LEU C  1 39  ? 122.053 -6.909  28.995  1.00 4.00  ? 38  LEU B CD1 1 
ATOM   2504  C  CD2 . LEU C  1 39  ? 123.223 -4.831  28.249  1.00 4.19  ? 38  LEU B CD2 1 
ATOM   2505  N  N   . THR C  1 40  ? 125.253 -7.749  32.576  1.00 10.55 ? 39  THR B N   1 
ATOM   2506  C  CA  . THR C  1 40  ? 126.509 -8.005  33.248  1.00 12.67 ? 39  THR B CA  1 
ATOM   2507  C  C   . THR C  1 40  ? 127.554 -7.397  32.325  1.00 14.60 ? 39  THR B C   1 
ATOM   2508  O  O   . THR C  1 40  ? 127.392 -7.553  31.106  1.00 17.07 ? 39  THR B O   1 
ATOM   2509  C  CB  . THR C  1 40  ? 126.707 -9.541  33.442  1.00 11.23 ? 39  THR B CB  1 
ATOM   2510  O  OG1 . THR C  1 40  ? 126.174 -10.283 32.346  1.00 15.41 ? 39  THR B OG1 1 
ATOM   2511  C  CG2 . THR C  1 40  ? 125.953 -9.972  34.679  1.00 10.81 ? 39  THR B CG2 1 
ATOM   2512  N  N   . GLU C  1 41  ? 128.476 -6.590  32.877  1.00 15.04 ? 40  GLU B N   1 
ATOM   2513  C  CA  . GLU C  1 41  ? 129.624 -6.005  32.196  1.00 15.28 ? 40  GLU B CA  1 
ATOM   2514  C  C   . GLU C  1 41  ? 130.210 -6.882  31.117  1.00 12.27 ? 40  GLU B C   1 
ATOM   2515  O  O   . GLU C  1 41  ? 130.406 -8.072  31.321  1.00 13.11 ? 40  GLU B O   1 
ATOM   2516  C  CB  . GLU C  1 41  ? 130.695 -5.704  33.231  1.00 20.76 ? 40  GLU B CB  1 
ATOM   2517  C  CG  . GLU C  1 41  ? 131.791 -4.771  32.712  1.00 28.09 ? 40  GLU B CG  1 
ATOM   2518  C  CD  . GLU C  1 41  ? 132.615 -3.991  33.756  1.00 32.13 ? 40  GLU B CD  1 
ATOM   2519  O  OE1 . GLU C  1 41  ? 132.448 -4.205  34.971  1.00 31.78 ? 40  GLU B OE1 1 
ATOM   2520  O  OE2 . GLU C  1 41  ? 133.423 -3.146  33.328  1.00 33.30 ? 40  GLU B OE2 1 
ATOM   2521  N  N   . GLY C  1 42  ? 130.403 -6.310  29.938  1.00 12.17 ? 41  GLY B N   1 
ATOM   2522  C  CA  . GLY C  1 42  ? 130.979 -6.994  28.795  1.00 9.28  ? 41  GLY B CA  1 
ATOM   2523  C  C   . GLY C  1 42  ? 130.061 -7.069  27.589  1.00 9.88  ? 41  GLY B C   1 
ATOM   2524  O  O   . GLY C  1 42  ? 129.043 -6.371  27.464  1.00 8.10  ? 41  GLY B O   1 
ATOM   2525  N  N   . LEU C  1 43  ? 130.422 -8.030  26.734  1.00 9.00  ? 42  LEU B N   1 
ATOM   2526  C  CA  . LEU C  1 43  ? 129.831 -8.214  25.432  1.00 8.29  ? 42  LEU B CA  1 
ATOM   2527  C  C   . LEU C  1 43  ? 128.572 -9.057  25.434  1.00 8.71  ? 42  LEU B C   1 
ATOM   2528  O  O   . LEU C  1 43  ? 128.539 -9.984  26.220  1.00 10.86 ? 42  LEU B O   1 
ATOM   2529  C  CB  . LEU C  1 43  ? 130.885 -8.831  24.552  1.00 6.64  ? 42  LEU B CB  1 
ATOM   2530  C  CG  . LEU C  1 43  ? 131.630 -8.003  23.518  1.00 4.90  ? 42  LEU B CG  1 
ATOM   2531  C  CD1 . LEU C  1 43  ? 132.397 -6.893  24.144  1.00 2.89  ? 42  LEU B CD1 1 
ATOM   2532  C  CD2 . LEU C  1 43  ? 132.564 -8.943  22.778  1.00 2.00  ? 42  LEU B CD2 1 
ATOM   2533  N  N   . HIS C  1 44  ? 127.553 -8.800  24.594  1.00 7.42  ? 43  HIS B N   1 
ATOM   2534  C  CA  . HIS C  1 44  ? 126.274 -9.502  24.558  1.00 5.15  ? 43  HIS B CA  1 
ATOM   2535  C  C   . HIS C  1 44  ? 125.734 -9.473  23.143  1.00 5.93  ? 43  HIS B C   1 
ATOM   2536  O  O   . HIS C  1 44  ? 125.703 -8.372  22.590  1.00 10.01 ? 43  HIS B O   1 
ATOM   2537  C  CB  . HIS C  1 44  ? 125.219 -8.827  25.411  1.00 7.18  ? 43  HIS B CB  1 
ATOM   2538  C  CG  . HIS C  1 44  ? 125.534 -8.793  26.897  1.00 8.87  ? 43  HIS B CG  1 
ATOM   2539  N  ND1 . HIS C  1 44  ? 125.436 -9.752  27.824  1.00 5.37  ? 43  HIS B ND1 1 
ATOM   2540  C  CD2 . HIS C  1 44  ? 126.056 -7.660  27.487  1.00 11.06 ? 43  HIS B CD2 1 
ATOM   2541  C  CE1 . HIS C  1 44  ? 125.889 -9.240  28.933  1.00 9.58  ? 43  HIS B CE1 1 
ATOM   2542  N  NE2 . HIS C  1 44  ? 126.260 -7.986  28.731  1.00 11.59 ? 43  HIS B NE2 1 
ATOM   2543  N  N   . GLY C  1 45  ? 125.324 -10.594 22.552  1.00 2.00  ? 44  GLY B N   1 
ATOM   2544  C  CA  . GLY C  1 45  ? 124.779 -10.696 21.209  1.00 3.05  ? 44  GLY B CA  1 
ATOM   2545  C  C   . GLY C  1 45  ? 123.494 -9.907  21.040  1.00 3.12  ? 44  GLY B C   1 
ATOM   2546  O  O   . GLY C  1 45  ? 122.681 -9.773  21.961  1.00 5.58  ? 44  GLY B O   1 
ATOM   2547  N  N   . PHE C  1 46  ? 123.275 -9.402  19.850  1.00 2.00  ? 45  PHE B N   1 
ATOM   2548  C  CA  . PHE C  1 46  ? 122.167 -8.499  19.583  1.00 3.11  ? 45  PHE B CA  1 
ATOM   2549  C  C   . PHE C  1 46  ? 121.660 -8.922  18.215  1.00 2.73  ? 45  PHE B C   1 
ATOM   2550  O  O   . PHE C  1 46  ? 122.392 -8.845  17.221  1.00 2.00  ? 45  PHE B O   1 
ATOM   2551  C  CB  . PHE C  1 46  ? 122.743 -7.105  19.585  1.00 2.00  ? 45  PHE B CB  1 
ATOM   2552  C  CG  . PHE C  1 46  ? 121.804 -5.925  19.616  1.00 5.17  ? 45  PHE B CG  1 
ATOM   2553  C  CD1 . PHE C  1 46  ? 120.807 -5.854  20.563  1.00 5.84  ? 45  PHE B CD1 1 
ATOM   2554  C  CD2 . PHE C  1 46  ? 121.998 -4.880  18.734  1.00 7.22  ? 45  PHE B CD2 1 
ATOM   2555  C  CE1 . PHE C  1 46  ? 120.023 -4.733  20.620  1.00 4.18  ? 45  PHE B CE1 1 
ATOM   2556  C  CE2 . PHE C  1 46  ? 121.210 -3.753  18.789  1.00 4.80  ? 45  PHE B CE2 1 
ATOM   2557  C  CZ  . PHE C  1 46  ? 120.226 -3.688  19.737  1.00 9.07  ? 45  PHE B CZ  1 
ATOM   2558  N  N   . HIS C  1 47  ? 120.431 -9.395  18.101  1.00 2.00  ? 46  HIS B N   1 
ATOM   2559  C  CA  . HIS C  1 47  ? 119.928 -9.960  16.859  1.00 2.00  ? 46  HIS B CA  1 
ATOM   2560  C  C   . HIS C  1 47  ? 118.486 -9.615  16.683  1.00 3.02  ? 46  HIS B C   1 
ATOM   2561  O  O   . HIS C  1 47  ? 117.829 -9.273  17.676  1.00 2.23  ? 46  HIS B O   1 
ATOM   2562  C  CB  . HIS C  1 47  ? 119.950 -11.473 16.853  1.00 6.33  ? 46  HIS B CB  1 
ATOM   2563  C  CG  . HIS C  1 47  ? 121.230 -12.066 17.397  1.00 7.76  ? 46  HIS B CG  1 
ATOM   2564  N  ND1 . HIS C  1 47  ? 121.358 -12.803 18.460  1.00 8.64  ? 46  HIS B ND1 1 
ATOM   2565  C  CD2 . HIS C  1 47  ? 122.470 -11.893 16.838  1.00 7.60  ? 46  HIS B CD2 1 
ATOM   2566  C  CE1 . HIS C  1 47  ? 122.633 -13.083 18.564  1.00 9.80  ? 46  HIS B CE1 1 
ATOM   2567  N  NE2 . HIS C  1 47  ? 123.301 -12.528 17.587  1.00 7.17  ? 46  HIS B NE2 1 
ATOM   2568  N  N   . VAL C  1 48  ? 117.989 -9.796  15.455  1.00 2.00  ? 47  VAL B N   1 
ATOM   2569  C  CA  . VAL C  1 48  ? 116.579 -9.636  15.203  1.00 2.00  ? 47  VAL B CA  1 
ATOM   2570  C  C   . VAL C  1 48  ? 116.160 -11.069 14.972  1.00 2.34  ? 47  VAL B C   1 
ATOM   2571  O  O   . VAL C  1 48  ? 116.763 -11.749 14.130  1.00 5.14  ? 47  VAL B O   1 
ATOM   2572  C  CB  . VAL C  1 48  ? 116.310 -8.774  13.964  1.00 2.00  ? 47  VAL B CB  1 
ATOM   2573  C  CG1 . VAL C  1 48  ? 114.815 -8.660  13.749  1.00 2.00  ? 47  VAL B CG1 1 
ATOM   2574  C  CG2 . VAL C  1 48  ? 116.898 -7.389  14.171  1.00 3.26  ? 47  VAL B CG2 1 
ATOM   2575  N  N   . HIS C  1 49  ? 115.221 -11.615 15.735  1.00 2.00  ? 48  HIS B N   1 
ATOM   2576  C  CA  . HIS C  1 49  ? 114.844 -12.990 15.545  1.00 2.00  ? 48  HIS B CA  1 
ATOM   2577  C  C   . HIS C  1 49  ? 113.643 -12.932 14.640  1.00 3.52  ? 48  HIS B C   1 
ATOM   2578  O  O   . HIS C  1 49  ? 113.025 -11.872 14.522  1.00 3.92  ? 48  HIS B O   1 
ATOM   2579  C  CB  . HIS C  1 49  ? 114.541 -13.604 16.872  1.00 2.00  ? 48  HIS B CB  1 
ATOM   2580  C  CG  . HIS C  1 49  ? 115.807 -14.035 17.608  1.00 2.00  ? 48  HIS B CG  1 
ATOM   2581  N  ND1 . HIS C  1 49  ? 116.131 -15.234 17.992  1.00 3.46  ? 48  HIS B ND1 1 
ATOM   2582  C  CD2 . HIS C  1 49  ? 116.876 -13.246 17.989  1.00 3.73  ? 48  HIS B CD2 1 
ATOM   2583  C  CE1 . HIS C  1 49  ? 117.321 -15.203 18.565  1.00 2.00  ? 48  HIS B CE1 1 
ATOM   2584  N  NE2 . HIS C  1 49  ? 117.796 -13.981 18.571  1.00 3.58  ? 48  HIS B NE2 1 
ATOM   2585  N  N   . GLU C  1 50  ? 113.269 -14.026 13.987  1.00 3.61  ? 49  GLU B N   1 
ATOM   2586  C  CA  . GLU C  1 50  ? 112.243 -13.980 12.975  1.00 2.25  ? 49  GLU B CA  1 
ATOM   2587  C  C   . GLU C  1 50  ? 110.866 -13.563 13.481  1.00 5.32  ? 49  GLU B C   1 
ATOM   2588  O  O   . GLU C  1 50  ? 110.329 -12.538 13.030  1.00 5.71  ? 49  GLU B O   1 
ATOM   2589  C  CB  . GLU C  1 50  ? 112.175 -15.316 12.354  1.00 2.00  ? 49  GLU B CB  1 
ATOM   2590  C  CG  . GLU C  1 50  ? 111.530 -15.268 11.004  1.00 3.36  ? 49  GLU B CG  1 
ATOM   2591  C  CD  . GLU C  1 50  ? 111.343 -16.632 10.320  1.00 9.94  ? 49  GLU B CD  1 
ATOM   2592  O  OE1 . GLU C  1 50  ? 111.963 -17.591 10.774  1.00 8.99  ? 49  GLU B OE1 1 
ATOM   2593  O  OE2 . GLU C  1 50  ? 110.569 -16.749 9.347   1.00 9.29  ? 49  GLU B OE2 1 
ATOM   2594  N  N   . PHE C  1 51  ? 110.263 -14.268 14.447  1.00 4.06  ? 50  PHE B N   1 
ATOM   2595  C  CA  . PHE C  1 51  ? 108.904 -13.946 14.799  1.00 3.05  ? 50  PHE B CA  1 
ATOM   2596  C  C   . PHE C  1 51  ? 108.775 -12.874 15.834  1.00 3.46  ? 50  PHE B C   1 
ATOM   2597  O  O   . PHE C  1 51  ? 109.595 -12.742 16.733  1.00 2.00  ? 50  PHE B O   1 
ATOM   2598  C  CB  . PHE C  1 51  ? 108.236 -15.169 15.295  1.00 4.76  ? 50  PHE B CB  1 
ATOM   2599  C  CG  . PHE C  1 51  ? 108.453 -16.299 14.322  1.00 2.74  ? 50  PHE B CG  1 
ATOM   2600  C  CD1 . PHE C  1 51  ? 108.043 -16.156 13.011  1.00 3.57  ? 50  PHE B CD1 1 
ATOM   2601  C  CD2 . PHE C  1 51  ? 109.099 -17.420 14.762  1.00 4.03  ? 50  PHE B CD2 1 
ATOM   2602  C  CE1 . PHE C  1 51  ? 108.287 -17.163 12.127  1.00 4.48  ? 50  PHE B CE1 1 
ATOM   2603  C  CE2 . PHE C  1 51  ? 109.344 -18.439 13.869  1.00 4.64  ? 50  PHE B CE2 1 
ATOM   2604  C  CZ  . PHE C  1 51  ? 108.940 -18.298 12.562  1.00 7.68  ? 50  PHE B CZ  1 
ATOM   2605  N  N   . GLY C  1 52  ? 107.727 -12.080 15.723  1.00 4.48  ? 51  GLY B N   1 
ATOM   2606  C  CA  . GLY C  1 52  ? 107.439 -11.113 16.759  1.00 4.80  ? 51  GLY B CA  1 
ATOM   2607  C  C   . GLY C  1 52  ? 106.377 -11.670 17.666  1.00 3.89  ? 51  GLY B C   1 
ATOM   2608  O  O   . GLY C  1 52  ? 105.525 -10.909 18.096  1.00 2.00  ? 51  GLY B O   1 
ATOM   2609  N  N   . ASP C  1 53  ? 106.422 -12.992 17.888  1.00 5.23  ? 52  ASP B N   1 
ATOM   2610  C  CA  . ASP C  1 53  ? 105.520 -13.765 18.725  1.00 7.21  ? 52  ASP B CA  1 
ATOM   2611  C  C   . ASP C  1 53  ? 106.210 -13.830 20.063  1.00 9.05  ? 52  ASP B C   1 
ATOM   2612  O  O   . ASP C  1 53  ? 107.247 -14.489 20.197  1.00 10.05 ? 52  ASP B O   1 
ATOM   2613  C  CB  . ASP C  1 53  ? 105.370 -15.172 18.151  1.00 6.91  ? 52  ASP B CB  1 
ATOM   2614  C  CG  . ASP C  1 53  ? 104.576 -16.233 18.911  1.00 6.38  ? 52  ASP B CG  1 
ATOM   2615  O  OD1 . ASP C  1 53  ? 104.652 -16.313 20.122  1.00 5.77  ? 52  ASP B OD1 1 
ATOM   2616  O  OD2 . ASP C  1 53  ? 103.880 -17.025 18.292  1.00 8.86  ? 52  ASP B OD2 1 
ATOM   2617  N  N   . ASN C  1 54  ? 105.675 -13.214 21.095  1.00 10.70 ? 53  ASN B N   1 
ATOM   2618  C  CA  . ASN C  1 54  ? 106.358 -13.308 22.377  1.00 12.68 ? 53  ASN B CA  1 
ATOM   2619  C  C   . ASN C  1 54  ? 105.408 -13.841 23.428  1.00 11.21 ? 53  ASN B C   1 
ATOM   2620  O  O   . ASN C  1 54  ? 105.415 -13.499 24.601  1.00 11.18 ? 53  ASN B O   1 
ATOM   2621  C  CB  . ASN C  1 54  ? 106.980 -11.882 22.735  1.00 14.13 ? 53  ASN B CB  1 
ATOM   2622  C  CG  . ASN C  1 54  ? 108.274 -11.593 21.902  1.00 17.21 ? 53  ASN B CG  1 
ATOM   2623  O  OD1 . ASN C  1 54  ? 108.623 -10.446 21.595  1.00 20.25 ? 53  ASN B OD1 1 
ATOM   2624  N  ND2 . ASN C  1 54  ? 109.117 -12.533 21.475  1.00 13.95 ? 53  ASN B ND2 1 
ATOM   2625  N  N   . THR C  1 55  ? 104.599 -14.802 22.987  1.00 14.14 ? 54  THR B N   1 
ATOM   2626  C  CA  . THR C  1 55  ? 103.619 -15.455 23.851  1.00 14.18 ? 54  THR B CA  1 
ATOM   2627  C  C   . THR C  1 55  ? 104.308 -16.147 25.018  1.00 15.75 ? 54  THR B C   1 
ATOM   2628  O  O   . THR C  1 55  ? 103.894 -15.894 26.160  1.00 18.19 ? 54  THR B O   1 
ATOM   2629  C  CB  . THR C  1 55  ? 102.806 -16.475 23.062  1.00 11.44 ? 54  THR B CB  1 
ATOM   2630  O  OG1 . THR C  1 55  ? 103.784 -17.171 22.328  1.00 16.06 ? 54  THR B OG1 1 
ATOM   2631  C  CG2 . THR C  1 55  ? 101.786 -15.917 22.100  1.00 8.91  ? 54  THR B CG2 1 
ATOM   2632  N  N   . ALA C  1 56  ? 105.340 -16.986 24.705  1.00 15.40 ? 55  ALA B N   1 
ATOM   2633  C  CA  . ALA C  1 56  ? 106.249 -17.638 25.672  1.00 13.38 ? 55  ALA B CA  1 
ATOM   2634  C  C   . ALA C  1 56  ? 107.432 -16.709 26.009  1.00 11.61 ? 55  ALA B C   1 
ATOM   2635  O  O   . ALA C  1 56  ? 108.552 -17.157 26.264  1.00 13.28 ? 55  ALA B O   1 
ATOM   2636  C  CB  . ALA C  1 56  ? 106.793 -18.940 25.065  1.00 10.00 ? 55  ALA B CB  1 
ATOM   2637  N  N   . GLY C  1 57  ? 107.274 -15.378 26.010  1.00 11.50 ? 56  GLY B N   1 
ATOM   2638  C  CA  . GLY C  1 57  ? 108.399 -14.458 26.172  1.00 7.67  ? 56  GLY B CA  1 
ATOM   2639  C  C   . GLY C  1 57  ? 109.303 -14.523 24.961  1.00 8.08  ? 56  GLY B C   1 
ATOM   2640  O  O   . GLY C  1 57  ? 108.861 -14.768 23.831  1.00 8.15  ? 56  GLY B O   1 
ATOM   2641  N  N   . CYS C  1 58  ? 110.603 -14.428 25.194  1.00 9.56  ? 57  CYS B N   1 
ATOM   2642  C  CA  . CYS C  1 58  ? 111.567 -14.370 24.124  1.00 6.81  ? 57  CYS B CA  1 
ATOM   2643  C  C   . CYS C  1 58  ? 111.765 -15.694 23.442  1.00 7.98  ? 57  CYS B C   1 
ATOM   2644  O  O   . CYS C  1 58  ? 112.335 -15.742 22.347  1.00 9.02  ? 57  CYS B O   1 
ATOM   2645  C  CB  . CYS C  1 58  ? 112.887 -13.937 24.639  1.00 5.37  ? 57  CYS B CB  1 
ATOM   2646  S  SG  . CYS C  1 58  ? 112.729 -12.434 25.603  1.00 12.47 ? 57  CYS B SG  1 
ATOM   2647  N  N   . THR C  1 59  ? 111.315 -16.784 24.036  1.00 6.96  ? 58  THR B N   1 
ATOM   2648  C  CA  . THR C  1 59  ? 111.497 -18.066 23.399  1.00 7.83  ? 58  THR B CA  1 
ATOM   2649  C  C   . THR C  1 59  ? 110.707 -18.184 22.104  1.00 8.02  ? 58  THR B C   1 
ATOM   2650  O  O   . THR C  1 59  ? 111.185 -18.827 21.169  1.00 10.38 ? 58  THR B O   1 
ATOM   2651  C  CB  . THR C  1 59  ? 111.061 -19.163 24.342  1.00 7.07  ? 58  THR B CB  1 
ATOM   2652  O  OG1 . THR C  1 59  ? 111.606 -18.861 25.633  1.00 12.84 ? 58  THR B OG1 1 
ATOM   2653  C  CG2 . THR C  1 59  ? 111.578 -20.520 23.895  1.00 10.92 ? 58  THR B CG2 1 
ATOM   2654  N  N   . SER C  1 60  ? 109.518 -17.611 21.945  1.00 7.50  ? 59  SER B N   1 
ATOM   2655  C  CA  . SER C  1 60  ? 108.813 -17.848 20.707  1.00 6.80  ? 59  SER B CA  1 
ATOM   2656  C  C   . SER C  1 60  ? 109.202 -16.974 19.498  1.00 4.03  ? 59  SER B C   1 
ATOM   2657  O  O   . SER C  1 60  ? 108.879 -17.235 18.348  1.00 3.21  ? 59  SER B O   1 
ATOM   2658  C  CB  . SER C  1 60  ? 107.327 -17.782 21.080  1.00 8.33  ? 59  SER B CB  1 
ATOM   2659  O  OG  . SER C  1 60  ? 106.935 -17.016 22.227  1.00 11.47 ? 59  SER B OG  1 
ATOM   2660  N  N   . ALA C  1 61  ? 110.071 -16.014 19.718  1.00 5.04  ? 60  ALA B N   1 
ATOM   2661  C  CA  . ALA C  1 61  ? 110.653 -15.152 18.717  1.00 2.67  ? 60  ALA B CA  1 
ATOM   2662  C  C   . ALA C  1 61  ? 111.323 -15.920 17.590  1.00 3.19  ? 60  ALA B C   1 
ATOM   2663  O  O   . ALA C  1 61  ? 111.706 -15.331 16.586  1.00 4.65  ? 60  ALA B O   1 
ATOM   2664  C  CB  . ALA C  1 61  ? 111.670 -14.290 19.402  1.00 2.00  ? 60  ALA B CB  1 
ATOM   2665  N  N   . GLY C  1 62  ? 111.550 -17.222 17.686  1.00 2.00  ? 61  GLY B N   1 
ATOM   2666  C  CA  . GLY C  1 62  ? 112.113 -17.995 16.603  1.00 2.00  ? 61  GLY B CA  1 
ATOM   2667  C  C   . GLY C  1 62  ? 113.618 -17.815 16.484  1.00 4.62  ? 61  GLY B C   1 
ATOM   2668  O  O   . GLY C  1 62  ? 114.282 -17.241 17.375  1.00 3.36  ? 61  GLY B O   1 
ATOM   2669  N  N   . PRO C  1 63  ? 114.262 -18.312 15.402  1.00 5.78  ? 62  PRO B N   1 
ATOM   2670  C  CA  . PRO C  1 63  ? 115.705 -18.165 15.179  1.00 4.23  ? 62  PRO B CA  1 
ATOM   2671  C  C   . PRO C  1 63  ? 116.020 -16.772 14.690  1.00 6.80  ? 62  PRO B C   1 
ATOM   2672  O  O   . PRO C  1 63  ? 115.143 -15.890 14.637  1.00 9.44  ? 62  PRO B O   1 
ATOM   2673  C  CB  . PRO C  1 63  ? 116.027 -19.232 14.180  1.00 2.00  ? 62  PRO B CB  1 
ATOM   2674  C  CG  . PRO C  1 63  ? 114.791 -19.202 13.340  1.00 4.77  ? 62  PRO B CG  1 
ATOM   2675  C  CD  . PRO C  1 63  ? 113.660 -19.134 14.353  1.00 4.56  ? 62  PRO B CD  1 
ATOM   2676  N  N   . HIS C  1 64  ? 117.277 -16.567 14.304  1.00 6.62  ? 63  HIS B N   1 
ATOM   2677  C  CA  . HIS C  1 64  ? 117.701 -15.296 13.773  1.00 5.17  ? 63  HIS B CA  1 
ATOM   2678  C  C   . HIS C  1 64  ? 116.958 -15.116 12.465  1.00 4.56  ? 63  HIS B C   1 
ATOM   2679  O  O   . HIS C  1 64  ? 116.815 -16.076 11.710  1.00 7.49  ? 63  HIS B O   1 
ATOM   2680  C  CB  . HIS C  1 64  ? 119.222 -15.303 13.561  1.00 4.22  ? 63  HIS B CB  1 
ATOM   2681  C  CG  . HIS C  1 64  ? 120.079 -15.259 14.822  1.00 2.25  ? 63  HIS B CG  1 
ATOM   2682  N  ND1 . HIS C  1 64  ? 121.396 -15.466 14.958  1.00 6.17  ? 63  HIS B ND1 1 
ATOM   2683  C  CD2 . HIS C  1 64  ? 119.541 -14.959 16.045  1.00 4.62  ? 63  HIS B CD2 1 
ATOM   2684  C  CE1 . HIS C  1 64  ? 121.564 -15.282 16.274  1.00 5.73  ? 63  HIS B CE1 1 
ATOM   2685  N  NE2 . HIS C  1 64  ? 120.458 -14.961 16.967  1.00 9.02  ? 63  HIS B NE2 1 
ATOM   2686  N  N   . PHE C  1 65  ? 116.372 -13.953 12.211  1.00 4.77  ? 64  PHE B N   1 
ATOM   2687  C  CA  . PHE C  1 65  ? 115.713 -13.635 10.951  1.00 4.18  ? 64  PHE B CA  1 
ATOM   2688  C  C   . PHE C  1 65  ? 116.747 -13.710 9.820   1.00 7.53  ? 64  PHE B C   1 
ATOM   2689  O  O   . PHE C  1 65  ? 117.678 -12.866 9.665   1.00 4.20  ? 64  PHE B O   1 
ATOM   2690  C  CB  . PHE C  1 65  ? 115.145 -12.229 11.035  1.00 4.66  ? 64  PHE B CB  1 
ATOM   2691  C  CG  . PHE C  1 65  ? 114.550 -11.657 9.759   1.00 3.16  ? 64  PHE B CG  1 
ATOM   2692  C  CD1 . PHE C  1 65  ? 113.740 -12.440 8.947   1.00 2.00  ? 64  PHE B CD1 1 
ATOM   2693  C  CD2 . PHE C  1 65  ? 114.874 -10.343 9.424   1.00 2.00  ? 64  PHE B CD2 1 
ATOM   2694  C  CE1 . PHE C  1 65  ? 113.242 -11.921 7.784   1.00 2.00  ? 64  PHE B CE1 1 
ATOM   2695  C  CE2 . PHE C  1 65  ? 114.370 -9.842  8.261   1.00 2.00  ? 64  PHE B CE2 1 
ATOM   2696  C  CZ  . PHE C  1 65  ? 113.565 -10.621 7.446   1.00 2.90  ? 64  PHE B CZ  1 
ATOM   2697  N  N   . ASN C  1 66  ? 116.526 -14.789 9.046   1.00 6.47  ? 65  ASN B N   1 
ATOM   2698  C  CA  . ASN C  1 66  ? 117.389 -15.030 7.918   1.00 9.71  ? 65  ASN B CA  1 
ATOM   2699  C  C   . ASN C  1 66  ? 116.671 -15.254 6.588   1.00 9.87  ? 65  ASN B C   1 
ATOM   2700  O  O   . ASN C  1 66  ? 116.514 -16.391 6.191   1.00 14.15 ? 65  ASN B O   1 
ATOM   2701  C  CB  . ASN C  1 66  ? 118.238 -16.202 8.386   1.00 9.84  ? 65  ASN B CB  1 
ATOM   2702  C  CG  . ASN C  1 66  ? 119.289 -16.679 7.423   1.00 10.07 ? 65  ASN B CG  1 
ATOM   2703  O  OD1 . ASN C  1 66  ? 119.744 -15.944 6.549   1.00 9.69  ? 65  ASN B OD1 1 
ATOM   2704  N  ND2 . ASN C  1 66  ? 119.717 -17.926 7.602   1.00 7.52  ? 65  ASN B ND2 1 
ATOM   2705  N  N   . PRO C  1 67  ? 116.150 -14.307 5.810   1.00 12.16 ? 66  PRO B N   1 
ATOM   2706  C  CA  . PRO C  1 67  ? 115.419 -14.558 4.557   1.00 11.68 ? 66  PRO B CA  1 
ATOM   2707  C  C   . PRO C  1 67  ? 116.159 -15.197 3.365   1.00 14.00 ? 66  PRO B C   1 
ATOM   2708  O  O   . PRO C  1 67  ? 115.623 -15.911 2.517   1.00 14.91 ? 66  PRO B O   1 
ATOM   2709  C  CB  . PRO C  1 67  ? 114.865 -13.192 4.219   1.00 8.62  ? 66  PRO B CB  1 
ATOM   2710  C  CG  . PRO C  1 67  ? 115.884 -12.241 4.730   1.00 9.88  ? 66  PRO B CG  1 
ATOM   2711  C  CD  . PRO C  1 67  ? 116.148 -12.881 6.107   1.00 12.79 ? 66  PRO B CD  1 
ATOM   2712  N  N   . LEU C  1 68  ? 117.442 -14.882 3.336   1.00 15.86 ? 67  LEU B N   1 
ATOM   2713  C  CA  . LEU C  1 68  ? 118.370 -15.206 2.280   1.00 14.23 ? 67  LEU B CA  1 
ATOM   2714  C  C   . LEU C  1 68  ? 119.198 -16.378 2.698   1.00 14.12 ? 67  LEU B C   1 
ATOM   2715  O  O   . LEU C  1 68  ? 120.317 -16.408 2.216   1.00 13.92 ? 67  LEU B O   1 
ATOM   2716  C  CB  . LEU C  1 68  ? 119.338 -14.060 2.034   1.00 14.79 ? 67  LEU B CB  1 
ATOM   2717  C  CG  . LEU C  1 68  ? 118.859 -12.708 1.578   1.00 16.51 ? 67  LEU B CG  1 
ATOM   2718  C  CD1 . LEU C  1 68  ? 120.064 -11.819 1.574   1.00 16.95 ? 67  LEU B CD1 1 
ATOM   2719  C  CD2 . LEU C  1 68  ? 118.250 -12.733 0.176   1.00 14.60 ? 67  LEU B CD2 1 
ATOM   2720  N  N   . SER C  1 69  ? 118.772 -17.293 3.572   1.00 16.25 ? 68  SER B N   1 
ATOM   2721  C  CA  . SER C  1 69  ? 119.560 -18.452 4.019   1.00 18.05 ? 68  SER B CA  1 
ATOM   2722  C  C   . SER C  1 69  ? 121.094 -18.332 4.117   1.00 18.32 ? 68  SER B C   1 
ATOM   2723  O  O   . SER C  1 69  ? 121.837 -19.020 3.439   1.00 21.99 ? 68  SER B O   1 
ATOM   2724  C  CB  . SER C  1 69  ? 119.191 -19.612 3.105   1.00 20.00 ? 68  SER B CB  1 
ATOM   2725  O  OG  . SER C  1 69  ? 117.778 -19.721 2.869   1.00 26.11 ? 68  SER B OG  1 
ATOM   2726  N  N   . ARG C  1 70  ? 121.674 -17.466 4.923   1.00 18.43 ? 69  ARG B N   1 
ATOM   2727  C  CA  . ARG C  1 70  ? 123.120 -17.365 5.022   1.00 18.10 ? 69  ARG B CA  1 
ATOM   2728  C  C   . ARG C  1 70  ? 123.478 -18.009 6.340   1.00 17.89 ? 69  ARG B C   1 
ATOM   2729  O  O   . ARG C  1 70  ? 122.636 -18.596 7.028   1.00 19.75 ? 69  ARG B O   1 
ATOM   2730  C  CB  . ARG C  1 70  ? 123.576 -15.908 5.033   1.00 19.09 ? 69  ARG B CB  1 
ATOM   2731  C  CG  . ARG C  1 70  ? 123.117 -15.227 3.755   1.00 24.90 ? 69  ARG B CG  1 
ATOM   2732  C  CD  . ARG C  1 70  ? 123.915 -15.468 2.456   1.00 27.08 ? 69  ARG B CD  1 
ATOM   2733  N  NE  . ARG C  1 70  ? 124.875 -14.375 2.313   1.00 31.01 ? 69  ARG B NE  1 
ATOM   2734  C  CZ  . ARG C  1 70  ? 124.523 -13.192 1.763   1.00 31.51 ? 69  ARG B CZ  1 
ATOM   2735  N  NH1 . ARG C  1 70  ? 123.289 -12.976 1.309   1.00 29.52 ? 69  ARG B NH1 1 
ATOM   2736  N  NH2 . ARG C  1 70  ? 125.403 -12.187 1.727   1.00 31.66 ? 69  ARG B NH2 1 
ATOM   2737  N  N   . LYS C  1 71  ? 124.721 -17.843 6.751   1.00 17.72 ? 70  LYS B N   1 
ATOM   2738  C  CA  . LYS C  1 71  ? 125.185 -18.398 7.993   1.00 15.87 ? 70  LYS B CA  1 
ATOM   2739  C  C   . LYS C  1 71  ? 125.266 -17.284 8.979   1.00 14.55 ? 70  LYS B C   1 
ATOM   2740  O  O   . LYS C  1 71  ? 124.984 -16.125 8.680   1.00 17.21 ? 70  LYS B O   1 
ATOM   2741  C  CB  . LYS C  1 71  ? 126.526 -19.014 7.770   1.00 19.51 ? 70  LYS B CB  1 
ATOM   2742  C  CG  . LYS C  1 71  ? 126.150 -20.451 7.754   1.00 23.20 ? 70  LYS B CG  1 
ATOM   2743  C  CD  . LYS C  1 71  ? 127.091 -21.251 6.890   1.00 28.27 ? 70  LYS B CD  1 
ATOM   2744  C  CE  . LYS C  1 71  ? 126.377 -22.585 6.675   1.00 29.97 ? 70  LYS B CE  1 
ATOM   2745  N  NZ  . LYS C  1 71  ? 125.028 -22.392 6.144   1.00 31.64 ? 70  LYS B NZ  1 
ATOM   2746  N  N   . HIS C  1 72  ? 125.547 -17.605 10.207  1.00 12.56 ? 71  HIS B N   1 
ATOM   2747  C  CA  . HIS C  1 72  ? 125.629 -16.544 11.170  1.00 12.31 ? 71  HIS B CA  1 
ATOM   2748  C  C   . HIS C  1 72  ? 126.954 -15.843 10.854  1.00 11.33 ? 71  HIS B C   1 
ATOM   2749  O  O   . HIS C  1 72  ? 127.831 -16.408 10.195  1.00 16.40 ? 71  HIS B O   1 
ATOM   2750  C  CB  . HIS C  1 72  ? 125.556 -17.160 12.600  1.00 9.08  ? 71  HIS B CB  1 
ATOM   2751  C  CG  . HIS C  1 72  ? 125.533 -16.085 13.685  1.00 8.27  ? 71  HIS B CG  1 
ATOM   2752  N  ND1 . HIS C  1 72  ? 124.490 -15.393 14.135  1.00 6.21  ? 71  HIS B ND1 1 
ATOM   2753  C  CD2 . HIS C  1 72  ? 126.658 -15.629 14.337  1.00 5.34  ? 71  HIS B CD2 1 
ATOM   2754  C  CE1 . HIS C  1 72  ? 124.971 -14.555 15.010  1.00 6.44  ? 71  HIS B CE1 1 
ATOM   2755  N  NE2 . HIS C  1 72  ? 126.267 -14.695 15.123  1.00 2.00  ? 71  HIS B NE2 1 
ATOM   2756  N  N   . GLY C  1 73  ? 127.052 -14.594 11.262  1.00 7.79  ? 72  GLY B N   1 
ATOM   2757  C  CA  . GLY C  1 73  ? 128.224 -13.803 11.086  1.00 5.04  ? 72  GLY B CA  1 
ATOM   2758  C  C   . GLY C  1 73  ? 127.947 -12.578 11.913  1.00 7.93  ? 72  GLY B C   1 
ATOM   2759  O  O   . GLY C  1 73  ? 127.010 -12.446 12.738  1.00 8.20  ? 72  GLY B O   1 
ATOM   2760  N  N   . GLY C  1 74  ? 128.851 -11.669 11.727  1.00 8.76  ? 73  GLY B N   1 
ATOM   2761  C  CA  . GLY C  1 74  ? 128.739 -10.392 12.385  1.00 8.38  ? 73  GLY B CA  1 
ATOM   2762  C  C   . GLY C  1 74  ? 128.208 -9.422  11.360  1.00 7.10  ? 73  GLY B C   1 
ATOM   2763  O  O   . GLY C  1 74  ? 128.165 -9.749  10.167  1.00 3.66  ? 73  GLY B O   1 
ATOM   2764  N  N   . PRO C  1 75  ? 127.886 -8.204  11.796  1.00 6.56  ? 74  PRO B N   1 
ATOM   2765  C  CA  . PRO C  1 75  ? 127.163 -7.282  10.980  1.00 7.85  ? 74  PRO B CA  1 
ATOM   2766  C  C   . PRO C  1 75  ? 128.026 -6.796  9.837   1.00 9.63  ? 74  PRO B C   1 
ATOM   2767  O  O   . PRO C  1 75  ? 127.488 -6.256  8.879   1.00 14.66 ? 74  PRO B O   1 
ATOM   2768  C  CB  . PRO C  1 75  ? 126.705 -6.202  11.962  1.00 7.11  ? 74  PRO B CB  1 
ATOM   2769  C  CG  . PRO C  1 75  ? 127.748 -6.180  13.045  1.00 4.89  ? 74  PRO B CG  1 
ATOM   2770  C  CD  . PRO C  1 75  ? 128.175 -7.655  13.127  1.00 7.09  ? 74  PRO B CD  1 
ATOM   2771  N  N   . LYS C  1 76  ? 129.349 -6.917  9.810   1.00 11.78 ? 75  LYS B N   1 
ATOM   2772  C  CA  . LYS C  1 76  ? 130.092 -6.388  8.658   1.00 12.86 ? 75  LYS B CA  1 
ATOM   2773  C  C   . LYS C  1 76  ? 130.689 -7.494  7.803   1.00 9.77  ? 75  LYS B C   1 
ATOM   2774  O  O   . LYS C  1 76  ? 131.642 -7.356  7.049   1.00 10.41 ? 75  LYS B O   1 
ATOM   2775  C  CB  . LYS C  1 76  ? 131.143 -5.406  9.219   1.00 16.17 ? 75  LYS B CB  1 
ATOM   2776  C  CG  . LYS C  1 76  ? 130.366 -4.209  9.849   1.00 23.71 ? 75  LYS B CG  1 
ATOM   2777  C  CD  . LYS C  1 76  ? 131.075 -2.919  10.291  1.00 27.05 ? 75  LYS B CD  1 
ATOM   2778  C  CE  . LYS C  1 76  ? 131.881 -2.991  11.600  1.00 31.04 ? 75  LYS B CE  1 
ATOM   2779  N  NZ  . LYS C  1 76  ? 132.600 -1.734  11.819  1.00 33.55 ? 75  LYS B NZ  1 
ATOM   2780  N  N   . ASP C  1 77  ? 130.111 -8.660  7.925   1.00 7.43  ? 76  ASP B N   1 
ATOM   2781  C  CA  . ASP C  1 77  ? 130.571 -9.775  7.157   1.00 9.07  ? 76  ASP B CA  1 
ATOM   2782  C  C   . ASP C  1 77  ? 129.581 -9.828  6.016   1.00 11.55 ? 76  ASP B C   1 
ATOM   2783  O  O   . ASP C  1 77  ? 128.538 -9.170  6.050   1.00 13.92 ? 76  ASP B O   1 
ATOM   2784  C  CB  . ASP C  1 77  ? 130.555 -11.066 8.008   1.00 7.13  ? 76  ASP B CB  1 
ATOM   2785  C  CG  . ASP C  1 77  ? 131.626 -11.075 9.101   1.00 6.80  ? 76  ASP B CG  1 
ATOM   2786  O  OD1 . ASP C  1 77  ? 132.677 -10.440 9.002   1.00 5.56  ? 76  ASP B OD1 1 
ATOM   2787  O  OD2 . ASP C  1 77  ? 131.422 -11.742 10.097  1.00 11.56 ? 76  ASP B OD2 1 
ATOM   2788  N  N   . GLU C  1 78  ? 129.902 -10.565 4.962   1.00 12.81 ? 77  GLU B N   1 
ATOM   2789  C  CA  . GLU C  1 78  ? 129.025 -10.595 3.820   1.00 13.15 ? 77  GLU B CA  1 
ATOM   2790  C  C   . GLU C  1 78  ? 127.935 -11.576 4.190   1.00 13.16 ? 77  GLU B C   1 
ATOM   2791  O  O   . GLU C  1 78  ? 126.741 -11.266 4.026   1.00 13.34 ? 77  GLU B O   1 
ATOM   2792  C  CB  . GLU C  1 78  ? 129.729 -11.097 2.526   1.00 15.99 ? 77  GLU B CB  1 
ATOM   2793  C  CG  . GLU C  1 78  ? 130.571 -10.188 1.617   1.00 18.95 ? 77  GLU B CG  1 
ATOM   2794  C  CD  . GLU C  1 78  ? 131.389 -10.938 0.536   1.00 20.75 ? 77  GLU B CD  1 
ATOM   2795  O  OE1 . GLU C  1 78  ? 132.452 -11.470 0.880   1.00 21.27 ? 77  GLU B OE1 1 
ATOM   2796  O  OE2 . GLU C  1 78  ? 130.993 -10.990 -0.643  1.00 19.95 ? 77  GLU B OE2 1 
ATOM   2797  N  N   . GLU C  1 79  ? 128.428 -12.741 4.670   1.00 10.89 ? 78  GLU B N   1 
ATOM   2798  C  CA  . GLU C  1 79  ? 127.660 -13.930 4.968   1.00 8.37  ? 78  GLU B CA  1 
ATOM   2799  C  C   . GLU C  1 79  ? 127.235 -13.698 6.383   1.00 10.23 ? 78  GLU B C   1 
ATOM   2800  O  O   . GLU C  1 79  ? 128.068 -13.625 7.291   1.00 11.27 ? 78  GLU B O   1 
ATOM   2801  C  CB  . GLU C  1 79  ? 128.569 -15.094 4.878   1.00 8.25  ? 78  GLU B CB  1 
ATOM   2802  C  CG  . GLU C  1 79  ? 128.046 -16.505 5.022   1.00 7.09  ? 78  GLU B CG  1 
ATOM   2803  C  CD  . GLU C  1 79  ? 127.102 -16.929 3.934   1.00 9.83  ? 78  GLU B CD  1 
ATOM   2804  O  OE1 . GLU C  1 79  ? 127.144 -16.317 2.857   1.00 15.23 ? 78  GLU B OE1 1 
ATOM   2805  O  OE2 . GLU C  1 79  ? 126.328 -17.863 4.161   1.00 7.36  ? 78  GLU B OE2 1 
ATOM   2806  N  N   . ARG C  1 80  ? 125.944 -13.420 6.480   1.00 8.43  ? 79  ARG B N   1 
ATOM   2807  C  CA  . ARG C  1 80  ? 125.336 -13.127 7.746   1.00 7.79  ? 79  ARG B CA  1 
ATOM   2808  C  C   . ARG C  1 80  ? 123.836 -13.140 7.555   1.00 8.48  ? 79  ARG B C   1 
ATOM   2809  O  O   . ARG C  1 80  ? 123.295 -13.139 6.449   1.00 10.11 ? 79  ARG B O   1 
ATOM   2810  C  CB  . ARG C  1 80  ? 125.805 -11.771 8.276   1.00 5.65  ? 79  ARG B CB  1 
ATOM   2811  C  CG  . ARG C  1 80  ? 125.608 -10.575 7.411   1.00 4.65  ? 79  ARG B CG  1 
ATOM   2812  C  CD  . ARG C  1 80  ? 124.461 -9.737  7.821   1.00 3.32  ? 79  ARG B CD  1 
ATOM   2813  N  NE  . ARG C  1 80  ? 124.911 -8.446  8.317   1.00 3.05  ? 79  ARG B NE  1 
ATOM   2814  C  CZ  . ARG C  1 80  ? 124.030 -7.638  8.949   1.00 3.89  ? 79  ARG B CZ  1 
ATOM   2815  N  NH1 . ARG C  1 80  ? 122.735 -7.920  9.104   1.00 5.15  ? 79  ARG B NH1 1 
ATOM   2816  N  NH2 . ARG C  1 80  ? 124.408 -6.484  9.433   1.00 2.00  ? 79  ARG B NH2 1 
ATOM   2817  N  N   . HIS C  1 81  ? 123.166 -13.219 8.689   1.00 7.89  ? 80  HIS B N   1 
ATOM   2818  C  CA  . HIS C  1 81  ? 121.717 -13.272 8.712   1.00 8.91  ? 80  HIS B CA  1 
ATOM   2819  C  C   . HIS C  1 81  ? 121.310 -11.819 8.715   1.00 8.68  ? 80  HIS B C   1 
ATOM   2820  O  O   . HIS C  1 81  ? 122.009 -10.956 9.288   1.00 8.01  ? 80  HIS B O   1 
ATOM   2821  C  CB  . HIS C  1 81  ? 121.183 -13.891 9.992   1.00 10.56 ? 80  HIS B CB  1 
ATOM   2822  C  CG  . HIS C  1 81  ? 121.577 -15.325 10.342  1.00 8.99  ? 80  HIS B CG  1 
ATOM   2823  N  ND1 . HIS C  1 81  ? 121.735 -15.762 11.573  1.00 5.87  ? 80  HIS B ND1 1 
ATOM   2824  C  CD2 . HIS C  1 81  ? 121.724 -16.389 9.497   1.00 9.55  ? 80  HIS B CD2 1 
ATOM   2825  C  CE1 . HIS C  1 81  ? 121.953 -17.058 11.531  1.00 9.10  ? 80  HIS B CE1 1 
ATOM   2826  N  NE2 . HIS C  1 81  ? 121.945 -17.427 10.274  1.00 11.84 ? 80  HIS B NE2 1 
ATOM   2827  N  N   . VAL C  1 82  ? 120.150 -11.534 8.152   1.00 7.95  ? 81  VAL B N   1 
ATOM   2828  C  CA  . VAL C  1 82  ? 119.747 -10.144 8.111   1.00 5.77  ? 81  VAL B CA  1 
ATOM   2829  C  C   . VAL C  1 82  ? 119.690 -9.624  9.549   1.00 7.68  ? 81  VAL B C   1 
ATOM   2830  O  O   . VAL C  1 82  ? 120.161 -8.507  9.851   1.00 11.79 ? 81  VAL B O   1 
ATOM   2831  C  CB  . VAL C  1 82  ? 118.393 -10.037 7.409   1.00 2.86  ? 81  VAL B CB  1 
ATOM   2832  C  CG1 . VAL C  1 82  ? 117.866 -8.623  7.357   1.00 4.97  ? 81  VAL B CG1 1 
ATOM   2833  C  CG2 . VAL C  1 82  ? 118.603 -10.468 5.986   1.00 2.00  ? 81  VAL B CG2 1 
ATOM   2834  N  N   . GLY C  1 83  ? 119.258 -10.509 10.439  1.00 4.04  ? 82  GLY B N   1 
ATOM   2835  C  CA  . GLY C  1 83  ? 119.120 -10.152 11.824  1.00 4.80  ? 82  GLY B CA  1 
ATOM   2836  C  C   . GLY C  1 83  ? 120.375 -10.026 12.661  1.00 6.30  ? 82  GLY B C   1 
ATOM   2837  O  O   . GLY C  1 83  ? 120.247 -9.751  13.859  1.00 8.88  ? 82  GLY B O   1 
ATOM   2838  N  N   . ASP C  1 84  ? 121.597 -10.198 12.158  1.00 6.40  ? 83  ASP B N   1 
ATOM   2839  C  CA  . ASP C  1 84  ? 122.740 -10.220 13.041  1.00 3.82  ? 83  ASP B CA  1 
ATOM   2840  C  C   . ASP C  1 84  ? 123.290 -8.837  13.257  1.00 5.42  ? 83  ASP B C   1 
ATOM   2841  O  O   . ASP C  1 84  ? 123.866 -8.239  12.356  1.00 9.68  ? 83  ASP B O   1 
ATOM   2842  C  CB  . ASP C  1 84  ? 123.784 -11.092 12.453  1.00 2.00  ? 83  ASP B CB  1 
ATOM   2843  C  CG  . ASP C  1 84  ? 123.417 -12.569 12.337  1.00 3.18  ? 83  ASP B CG  1 
ATOM   2844  O  OD1 . ASP C  1 84  ? 122.504 -13.113 12.985  1.00 2.00  ? 83  ASP B OD1 1 
ATOM   2845  O  OD2 . ASP C  1 84  ? 124.113 -13.198 11.554  1.00 4.70  ? 83  ASP B OD2 1 
ATOM   2846  N  N   . LEU C  1 85  ? 123.116 -8.273  14.437  1.00 4.87  ? 84  LEU B N   1 
ATOM   2847  C  CA  . LEU C  1 85  ? 123.637 -6.951  14.700  1.00 4.09  ? 84  LEU B CA  1 
ATOM   2848  C  C   . LEU C  1 85  ? 124.807 -6.982  15.673  1.00 3.81  ? 84  LEU B C   1 
ATOM   2849  O  O   . LEU C  1 85  ? 125.283 -5.971  16.195  1.00 2.00  ? 84  LEU B O   1 
ATOM   2850  C  CB  . LEU C  1 85  ? 122.426 -6.078  15.147  1.00 4.75  ? 84  LEU B CB  1 
ATOM   2851  C  CG  . LEU C  1 85  ? 121.398 -5.893  14.002  1.00 2.00  ? 84  LEU B CG  1 
ATOM   2852  C  CD1 . LEU C  1 85  ? 120.168 -5.203  14.471  1.00 2.00  ? 84  LEU B CD1 1 
ATOM   2853  C  CD2 . LEU C  1 85  ? 122.029 -5.063  12.916  1.00 2.00  ? 84  LEU B CD2 1 
ATOM   2854  N  N   . GLY C  1 86  ? 125.357 -8.203  15.803  1.00 4.36  ? 85  GLY B N   1 
ATOM   2855  C  CA  . GLY C  1 86  ? 126.651 -8.380  16.424  1.00 3.88  ? 85  GLY B CA  1 
ATOM   2856  C  C   . GLY C  1 86  ? 126.634 -8.332  17.920  1.00 4.20  ? 85  GLY B C   1 
ATOM   2857  O  O   . GLY C  1 86  ? 125.993 -9.207  18.481  1.00 5.88  ? 85  GLY B O   1 
ATOM   2858  N  N   . ASN C  1 87  ? 127.231 -7.327  18.576  1.00 5.30  ? 86  ASN B N   1 
ATOM   2859  C  CA  . ASN C  1 87  ? 127.447 -7.327  20.022  1.00 4.24  ? 86  ASN B CA  1 
ATOM   2860  C  C   . ASN C  1 87  ? 127.411 -5.952  20.635  1.00 6.14  ? 86  ASN B C   1 
ATOM   2861  O  O   . ASN C  1 87  ? 128.015 -5.006  20.106  1.00 6.64  ? 86  ASN B O   1 
ATOM   2862  C  CB  . ASN C  1 87  ? 128.786 -7.824  20.477  1.00 3.23  ? 86  ASN B CB  1 
ATOM   2863  C  CG  . ASN C  1 87  ? 129.042 -9.291  20.406  1.00 2.00  ? 86  ASN B CG  1 
ATOM   2864  O  OD1 . ASN C  1 87  ? 128.236 -10.078 20.854  1.00 5.37  ? 86  ASN B OD1 1 
ATOM   2865  N  ND2 . ASN C  1 87  ? 130.159 -9.741  19.873  1.00 3.01  ? 86  ASN B ND2 1 
ATOM   2866  N  N   . VAL C  1 88  ? 126.705 -5.864  21.771  1.00 7.19  ? 87  VAL B N   1 
ATOM   2867  C  CA  . VAL C  1 88  ? 126.650 -4.622  22.521  1.00 8.89  ? 87  VAL B CA  1 
ATOM   2868  C  C   . VAL C  1 88  ? 127.544 -4.775  23.742  1.00 7.77  ? 87  VAL B C   1 
ATOM   2869  O  O   . VAL C  1 88  ? 127.776 -5.885  24.234  1.00 7.71  ? 87  VAL B O   1 
ATOM   2870  C  CB  . VAL C  1 88  ? 125.176 -4.252  22.947  1.00 8.53  ? 87  VAL B CB  1 
ATOM   2871  C  CG1 . VAL C  1 88  ? 124.459 -3.899  21.650  1.00 4.17  ? 87  VAL B CG1 1 
ATOM   2872  C  CG2 . VAL C  1 88  ? 124.461 -5.353  23.712  1.00 7.55  ? 87  VAL B CG2 1 
ATOM   2873  N  N   . THR C  1 89  ? 128.058 -3.667  24.233  1.00 7.13  ? 88  THR B N   1 
ATOM   2874  C  CA  . THR C  1 89  ? 129.033 -3.730  25.276  1.00 10.04 ? 88  THR B CA  1 
ATOM   2875  C  C   . THR C  1 89  ? 128.511 -2.956  26.447  1.00 11.03 ? 88  THR B C   1 
ATOM   2876  O  O   . THR C  1 89  ? 128.252 -1.744  26.327  1.00 13.88 ? 88  THR B O   1 
ATOM   2877  C  CB  . THR C  1 89  ? 130.360 -3.145  24.756  1.00 10.18 ? 88  THR B CB  1 
ATOM   2878  O  OG1 . THR C  1 89  ? 130.729 -3.927  23.622  1.00 12.80 ? 88  THR B OG1 1 
ATOM   2879  C  CG2 . THR C  1 89  ? 131.484 -3.219  25.776  1.00 10.72 ? 88  THR B CG2 1 
ATOM   2880  N  N   . ALA C  1 90  ? 128.311 -3.717  27.524  1.00 8.49  ? 89  ALA B N   1 
ATOM   2881  C  CA  . ALA C  1 90  ? 127.855 -3.186  28.801  1.00 9.52  ? 89  ALA B CA  1 
ATOM   2882  C  C   . ALA C  1 90  ? 129.032 -2.797  29.682  1.00 10.02 ? 89  ALA B C   1 
ATOM   2883  O  O   . ALA C  1 90  ? 130.016 -3.528  29.823  1.00 6.74  ? 89  ALA B O   1 
ATOM   2884  C  CB  . ALA C  1 90  ? 127.044 -4.214  29.584  1.00 8.36  ? 89  ALA B CB  1 
ATOM   2885  N  N   . ASP C  1 91  ? 128.982 -1.630  30.295  1.00 11.31 ? 90  ASP B N   1 
ATOM   2886  C  CA  . ASP C  1 91  ? 130.062 -1.258  31.159  1.00 14.36 ? 90  ASP B CA  1 
ATOM   2887  C  C   . ASP C  1 91  ? 129.961 -1.748  32.591  1.00 16.22 ? 90  ASP B C   1 
ATOM   2888  O  O   . ASP C  1 91  ? 129.102 -2.553  32.924  1.00 15.10 ? 90  ASP B O   1 
ATOM   2889  C  CB  . ASP C  1 91  ? 130.174 0.228   31.134  1.00 15.25 ? 90  ASP B CB  1 
ATOM   2890  C  CG  . ASP C  1 91  ? 128.908 0.960   31.461  1.00 15.29 ? 90  ASP B CG  1 
ATOM   2891  O  OD1 . ASP C  1 91  ? 128.173 0.554   32.357  1.00 15.91 ? 90  ASP B OD1 1 
ATOM   2892  O  OD2 . ASP C  1 91  ? 128.686 1.960   30.793  1.00 20.08 ? 90  ASP B OD2 1 
ATOM   2893  N  N   . LYS C  1 92  ? 130.821 -1.168  33.444  1.00 21.03 ? 91  LYS B N   1 
ATOM   2894  C  CA  . LYS C  1 92  ? 130.888 -1.400  34.903  1.00 23.90 ? 91  LYS B CA  1 
ATOM   2895  C  C   . LYS C  1 92  ? 129.502 -1.396  35.534  1.00 22.96 ? 91  LYS B C   1 
ATOM   2896  O  O   . LYS C  1 92  ? 129.159 -2.316  36.270  1.00 23.63 ? 91  LYS B O   1 
ATOM   2897  C  CB  . LYS C  1 92  ? 131.763 -0.325  35.563  1.00 26.36 ? 91  LYS B CB  1 
ATOM   2898  C  CG  . LYS C  1 92  ? 133.087 -0.216  34.791  1.00 33.87 ? 91  LYS B CG  1 
ATOM   2899  C  CD  . LYS C  1 92  ? 134.063 0.918   35.153  1.00 40.22 ? 91  LYS B CD  1 
ATOM   2900  C  CE  . LYS C  1 92  ? 133.523 2.361   35.063  1.00 43.53 ? 91  LYS B CE  1 
ATOM   2901  N  NZ  . LYS C  1 92  ? 132.668 2.729   36.188  1.00 44.63 ? 91  LYS B NZ  1 
ATOM   2902  N  N   . ASP C  1 93  ? 128.672 -0.439  35.131  1.00 20.52 ? 92  ASP B N   1 
ATOM   2903  C  CA  . ASP C  1 93  ? 127.308 -0.354  35.596  1.00 21.60 ? 92  ASP B CA  1 
ATOM   2904  C  C   . ASP C  1 93  ? 126.298 -1.141  34.774  1.00 21.08 ? 92  ASP B C   1 
ATOM   2905  O  O   . ASP C  1 93  ? 125.126 -0.776  34.719  1.00 21.47 ? 92  ASP B O   1 
ATOM   2906  C  CB  . ASP C  1 93  ? 126.912 1.082   35.618  1.00 24.96 ? 92  ASP B CB  1 
ATOM   2907  C  CG  . ASP C  1 93  ? 127.855 1.825   36.524  1.00 31.89 ? 92  ASP B CG  1 
ATOM   2908  O  OD1 . ASP C  1 93  ? 128.083 1.341   37.652  1.00 35.93 ? 92  ASP B OD1 1 
ATOM   2909  O  OD2 . ASP C  1 93  ? 128.361 2.865   36.072  1.00 33.34 ? 92  ASP B OD2 1 
ATOM   2910  N  N   . GLY C  1 94  ? 126.728 -2.197  34.084  1.00 18.88 ? 93  GLY B N   1 
ATOM   2911  C  CA  . GLY C  1 94  ? 125.853 -3.019  33.285  1.00 14.34 ? 93  GLY B CA  1 
ATOM   2912  C  C   . GLY C  1 94  ? 125.000 -2.340  32.236  1.00 10.90 ? 93  GLY B C   1 
ATOM   2913  O  O   . GLY C  1 94  ? 124.034 -2.935  31.807  1.00 11.93 ? 93  GLY B O   1 
ATOM   2914  N  N   . VAL C  1 95  ? 125.276 -1.116  31.836  1.00 8.70  ? 94  VAL B N   1 
ATOM   2915  C  CA  . VAL C  1 95  ? 124.553 -0.394  30.814  1.00 8.50  ? 94  VAL B CA  1 
ATOM   2916  C  C   . VAL C  1 95  ? 125.249 -0.511  29.473  1.00 8.86  ? 94  VAL B C   1 
ATOM   2917  O  O   . VAL C  1 95  ? 126.485 -0.440  29.432  1.00 10.59 ? 94  VAL B O   1 
ATOM   2918  C  CB  . VAL C  1 95  ? 124.493 1.045   31.246  1.00 6.89  ? 94  VAL B CB  1 
ATOM   2919  C  CG1 . VAL C  1 95  ? 123.778 1.982   30.313  1.00 2.64  ? 94  VAL B CG1 1 
ATOM   2920  C  CG2 . VAL C  1 95  ? 123.668 0.974   32.513  1.00 10.06 ? 94  VAL B CG2 1 
ATOM   2921  N  N   . ALA C  1 96  ? 124.503 -0.741  28.396  1.00 7.63  ? 95  ALA B N   1 
ATOM   2922  C  CA  . ALA C  1 96  ? 125.075 -0.819  27.059  1.00 8.77  ? 95  ALA B CA  1 
ATOM   2923  C  C   . ALA C  1 96  ? 124.481 0.312   26.258  1.00 10.98 ? 95  ALA B C   1 
ATOM   2924  O  O   . ALA C  1 96  ? 123.251 0.364   26.177  1.00 14.29 ? 95  ALA B O   1 
ATOM   2925  C  CB  . ALA C  1 96  ? 124.703 -2.110  26.350  1.00 4.75  ? 95  ALA B CB  1 
ATOM   2926  N  N   . ASP C  1 97  ? 125.240 1.259   25.696  1.00 11.90 ? 96  ASP B N   1 
ATOM   2927  C  CA  . ASP C  1 97  ? 124.672 2.296   24.843  1.00 12.17 ? 96  ASP B CA  1 
ATOM   2928  C  C   . ASP C  1 97  ? 124.901 1.760   23.456  1.00 10.78 ? 96  ASP B C   1 
ATOM   2929  O  O   . ASP C  1 97  ? 126.021 1.384   23.114  1.00 11.40 ? 96  ASP B O   1 
ATOM   2930  C  CB  . ASP C  1 97  ? 125.391 3.618   24.954  1.00 14.46 ? 96  ASP B CB  1 
ATOM   2931  C  CG  . ASP C  1 97  ? 125.679 3.930   26.417  1.00 23.16 ? 96  ASP B CG  1 
ATOM   2932  O  OD1 . ASP C  1 97  ? 124.744 3.904   27.239  1.00 25.12 ? 96  ASP B OD1 1 
ATOM   2933  O  OD2 . ASP C  1 97  ? 126.861 4.160   26.735  1.00 28.05 ? 96  ASP B OD2 1 
ATOM   2934  N  N   . VAL C  1 98  ? 123.834 1.695   22.680  1.00 8.30  ? 97  VAL B N   1 
ATOM   2935  C  CA  . VAL C  1 98  ? 123.843 1.168   21.335  1.00 6.04  ? 97  VAL B CA  1 
ATOM   2936  C  C   . VAL C  1 98  ? 123.852 2.351   20.366  1.00 5.73  ? 97  VAL B C   1 
ATOM   2937  O  O   . VAL C  1 98  ? 123.168 3.363   20.600  1.00 4.90  ? 97  VAL B O   1 
ATOM   2938  C  CB  . VAL C  1 98  ? 122.576 0.254   21.193  1.00 4.22  ? 97  VAL B CB  1 
ATOM   2939  C  CG1 . VAL C  1 98  ? 122.721 -0.575  19.967  1.00 2.00  ? 97  VAL B CG1 1 
ATOM   2940  C  CG2 . VAL C  1 98  ? 122.421 -0.750  22.364  1.00 2.00  ? 97  VAL B CG2 1 
ATOM   2941  N  N   . SER C  1 99  ? 124.683 2.247   19.324  1.00 5.91  ? 98  SER B N   1 
ATOM   2942  C  CA  . SER C  1 99  ? 124.753 3.188   18.214  1.00 7.70  ? 98  SER B CA  1 
ATOM   2943  C  C   . SER C  1 99  ? 125.348 2.304   17.171  1.00 8.62  ? 98  SER B C   1 
ATOM   2944  O  O   . SER C  1 99  ? 126.464 1.877   17.348  1.00 9.71  ? 98  SER B O   1 
ATOM   2945  C  CB  . SER C  1 99  ? 125.686 4.310   18.487  1.00 6.60  ? 98  SER B CB  1 
ATOM   2946  O  OG  . SER C  1 99  ? 125.369 5.457   17.705  1.00 15.29 ? 98  SER B OG  1 
ATOM   2947  N  N   . ILE C  1 100 ? 124.611 1.912   16.152  1.00 11.35 ? 99  ILE B N   1 
ATOM   2948  C  CA  . ILE C  1 100 ? 124.994 0.944   15.112  1.00 10.99 ? 99  ILE B CA  1 
ATOM   2949  C  C   . ILE C  1 100 ? 124.402 1.580   13.859  1.00 13.22 ? 99  ILE B C   1 
ATOM   2950  O  O   . ILE C  1 100 ? 123.449 2.386   13.920  1.00 12.76 ? 99  ILE B O   1 
ATOM   2951  C  CB  . ILE C  1 100 ? 124.300 -0.426  15.378  1.00 10.92 ? 99  ILE B CB  1 
ATOM   2952  C  CG1 . ILE C  1 100 ? 124.992 -1.092  16.504  1.00 11.04 ? 99  ILE B CG1 1 
ATOM   2953  C  CG2 . ILE C  1 100 ? 124.293 -1.352  14.185  1.00 9.46  ? 99  ILE B CG2 1 
ATOM   2954  C  CD1 . ILE C  1 100 ? 124.014 -2.179  17.040  1.00 12.64 ? 99  ILE B CD1 1 
ATOM   2955  N  N   . GLU C  1 101 ? 124.968 1.238   12.711  1.00 13.97 ? 100 GLU B N   1 
ATOM   2956  C  CA  . GLU C  1 101 ? 124.424 1.650   11.430  1.00 14.14 ? 100 GLU B CA  1 
ATOM   2957  C  C   . GLU C  1 101 ? 124.375 0.372   10.629  1.00 10.52 ? 100 GLU B C   1 
ATOM   2958  O  O   . GLU C  1 101 ? 125.370 -0.344  10.628  1.00 10.70 ? 100 GLU B O   1 
ATOM   2959  C  CB  . GLU C  1 101 ? 125.328 2.646   10.747  1.00 17.95 ? 100 GLU B CB  1 
ATOM   2960  C  CG  . GLU C  1 101 ? 124.886 4.070   10.989  1.00 24.98 ? 100 GLU B CG  1 
ATOM   2961  C  CD  . GLU C  1 101 ? 125.400 5.083   9.935   1.00 33.53 ? 100 GLU B CD  1 
ATOM   2962  O  OE1 . GLU C  1 101 ? 125.210 4.860   8.711   1.00 33.85 ? 100 GLU B OE1 1 
ATOM   2963  O  OE2 . GLU C  1 101 ? 125.989 6.102   10.362  1.00 35.61 ? 100 GLU B OE2 1 
ATOM   2964  N  N   . ASP C  1 102 ? 123.296 -0.022  9.979   1.00 8.82  ? 101 ASP B N   1 
ATOM   2965  C  CA  . ASP C  1 102 ? 123.324 -1.265  9.260   1.00 7.80  ? 101 ASP B CA  1 
ATOM   2966  C  C   . ASP C  1 102 ? 122.670 -1.055  7.930   1.00 10.08 ? 101 ASP B C   1 
ATOM   2967  O  O   . ASP C  1 102 ? 121.715 -0.295  7.801   1.00 13.09 ? 101 ASP B O   1 
ATOM   2968  C  CB  . ASP C  1 102 ? 122.575 -2.327  10.006  1.00 5.98  ? 101 ASP B CB  1 
ATOM   2969  C  CG  . ASP C  1 102 ? 123.110 -3.699  9.680   1.00 4.71  ? 101 ASP B CG  1 
ATOM   2970  O  OD1 . ASP C  1 102 ? 124.241 -3.949  10.067  1.00 6.51  ? 101 ASP B OD1 1 
ATOM   2971  O  OD2 . ASP C  1 102 ? 122.422 -4.506  9.064   1.00 2.11  ? 101 ASP B OD2 1 
ATOM   2972  N  N   . SER C  1 103 ? 123.226 -1.756  6.957   1.00 10.67 ? 102 SER B N   1 
ATOM   2973  C  CA  . SER C  1 103 ? 122.768 -1.734  5.589   1.00 10.60 ? 102 SER B CA  1 
ATOM   2974  C  C   . SER C  1 103 ? 122.139 -3.065  5.194   1.00 11.73 ? 102 SER B C   1 
ATOM   2975  O  O   . SER C  1 103 ? 121.884 -3.268  3.996   1.00 15.49 ? 102 SER B O   1 
ATOM   2976  C  CB  . SER C  1 103 ? 123.925 -1.462  4.656   1.00 11.80 ? 102 SER B CB  1 
ATOM   2977  O  OG  . SER C  1 103 ? 124.588 -0.245  4.988   1.00 21.75 ? 102 SER B OG  1 
ATOM   2978  N  N   . VAL C  1 104 ? 121.920 -4.070  6.070   1.00 9.12  ? 103 VAL B N   1 
ATOM   2979  C  CA  . VAL C  1 104 ? 121.191 -5.211  5.570   1.00 7.12  ? 103 VAL B CA  1 
ATOM   2980  C  C   . VAL C  1 104 ? 119.739 -5.188  6.026   1.00 7.46  ? 103 VAL B C   1 
ATOM   2981  O  O   . VAL C  1 104 ? 118.850 -5.583  5.262   1.00 11.94 ? 103 VAL B O   1 
ATOM   2982  C  CB  . VAL C  1 104 ? 121.897 -6.488  5.997   1.00 6.89  ? 103 VAL B CB  1 
ATOM   2983  C  CG1 . VAL C  1 104 ? 121.223 -7.702  5.350   1.00 2.00  ? 103 VAL B CG1 1 
ATOM   2984  C  CG2 . VAL C  1 104 ? 123.357 -6.369  5.584   1.00 4.64  ? 103 VAL B CG2 1 
ATOM   2985  N  N   . ILE C  1 105 ? 119.479 -4.702  7.235   1.00 5.82  ? 104 ILE B N   1 
ATOM   2986  C  CA  . ILE C  1 105 ? 118.129 -4.609  7.772   1.00 5.25  ? 104 ILE B CA  1 
ATOM   2987  C  C   . ILE C  1 105 ? 117.414 -3.385  7.190   1.00 7.93  ? 104 ILE B C   1 
ATOM   2988  O  O   . ILE C  1 105 ? 118.015 -2.319  6.906   1.00 6.23  ? 104 ILE B O   1 
ATOM   2989  C  CB  . ILE C  1 105 ? 118.161 -4.475  9.316   1.00 2.00  ? 104 ILE B CB  1 
ATOM   2990  C  CG1 . ILE C  1 105 ? 118.910 -3.221  9.756   1.00 2.00  ? 104 ILE B CG1 1 
ATOM   2991  C  CG2 . ILE C  1 105 ? 118.791 -5.733  9.870   1.00 2.61  ? 104 ILE B CG2 1 
ATOM   2992  C  CD1 . ILE C  1 105 ? 118.849 -2.864  11.242  1.00 2.00  ? 104 ILE B CD1 1 
ATOM   2993  N  N   . SER C  1 106 ? 116.099 -3.516  7.076   1.00 7.08  ? 105 SER B N   1 
ATOM   2994  C  CA  . SER C  1 106 ? 115.338 -2.403  6.581   1.00 4.02  ? 105 SER B CA  1 
ATOM   2995  C  C   . SER C  1 106 ? 114.168 -2.299  7.501   1.00 4.47  ? 105 SER B C   1 
ATOM   2996  O  O   . SER C  1 106 ? 113.860 -3.209  8.295   1.00 4.71  ? 105 SER B O   1 
ATOM   2997  C  CB  . SER C  1 106 ? 114.903 -2.717  5.185   1.00 3.69  ? 105 SER B CB  1 
ATOM   2998  O  OG  . SER C  1 106 ? 114.741 -1.484  4.531   1.00 7.62  ? 105 SER B OG  1 
ATOM   2999  N  N   . LEU C  1 107 ? 113.514 -1.171  7.334   1.00 2.00  ? 106 LEU B N   1 
ATOM   3000  C  CA  . LEU C  1 107 ? 112.262 -0.973  7.998   1.00 2.00  ? 106 LEU B CA  1 
ATOM   3001  C  C   . LEU C  1 107 ? 111.159 -1.204  6.971   1.00 2.00  ? 106 LEU B C   1 
ATOM   3002  O  O   . LEU C  1 107 ? 109.979 -1.082  7.276   1.00 2.00  ? 106 LEU B O   1 
ATOM   3003  C  CB  . LEU C  1 107 ? 112.232 0.441   8.570   1.00 3.02  ? 106 LEU B CB  1 
ATOM   3004  C  CG  . LEU C  1 107 ? 113.275 0.746   9.654   1.00 3.49  ? 106 LEU B CG  1 
ATOM   3005  C  CD1 . LEU C  1 107 ? 113.068 2.152   10.103  1.00 6.30  ? 106 LEU B CD1 1 
ATOM   3006  C  CD2 . LEU C  1 107 ? 113.129 -0.114  10.871  1.00 2.00  ? 106 LEU B CD2 1 
ATOM   3007  N  N   . SER C  1 108 ? 111.454 -1.535  5.721   1.00 3.37  ? 107 SER B N   1 
ATOM   3008  C  CA  . SER C  1 108 ? 110.443 -1.802  4.728   1.00 5.36  ? 107 SER B CA  1 
ATOM   3009  C  C   . SER C  1 108 ? 110.978 -2.817  3.747   1.00 7.37  ? 107 SER B C   1 
ATOM   3010  O  O   . SER C  1 108 ? 112.167 -3.134  3.718   1.00 8.09  ? 107 SER B O   1 
ATOM   3011  C  CB  . SER C  1 108 ? 110.060 -0.538  3.959   1.00 2.92  ? 107 SER B CB  1 
ATOM   3012  O  OG  . SER C  1 108 ? 111.185 0.114   3.388   1.00 6.09  ? 107 SER B OG  1 
ATOM   3013  N  N   . GLY C  1 109 ? 110.072 -3.356  2.940   1.00 9.80  ? 108 GLY B N   1 
ATOM   3014  C  CA  . GLY C  1 109 ? 110.412 -4.351  1.942   1.00 13.57 ? 108 GLY B CA  1 
ATOM   3015  C  C   . GLY C  1 109 ? 110.497 -5.706  2.599   1.00 15.43 ? 108 GLY B C   1 
ATOM   3016  O  O   . GLY C  1 109 ? 109.891 -5.883  3.642   1.00 17.88 ? 108 GLY B O   1 
ATOM   3017  N  N   . ASP C  1 110 ? 111.230 -6.702  2.145   1.00 20.22 ? 109 ASP B N   1 
ATOM   3018  C  CA  . ASP C  1 110 ? 111.142 -7.995  2.798   1.00 21.61 ? 109 ASP B CA  1 
ATOM   3019  C  C   . ASP C  1 110 ? 112.381 -8.431  3.528   1.00 20.26 ? 109 ASP B C   1 
ATOM   3020  O  O   . ASP C  1 110 ? 112.692 -9.609  3.701   1.00 21.88 ? 109 ASP B O   1 
ATOM   3021  C  CB  . ASP C  1 110 ? 110.716 -9.014  1.749   1.00 29.21 ? 109 ASP B CB  1 
ATOM   3022  C  CG  . ASP C  1 110 ? 109.343 -8.671  1.164   1.00 33.85 ? 109 ASP B CG  1 
ATOM   3023  O  OD1 . ASP C  1 110 ? 108.388 -8.530  1.945   1.00 37.00 ? 109 ASP B OD1 1 
ATOM   3024  O  OD2 . ASP C  1 110 ? 109.250 -8.522  -0.066  1.00 37.09 ? 109 ASP B OD2 1 
ATOM   3025  N  N   . HIS C  1 111 ? 113.145 -7.402  3.875   1.00 18.11 ? 110 HIS B N   1 
ATOM   3026  C  CA  . HIS C  1 111 ? 114.203 -7.552  4.864   1.00 14.40 ? 110 HIS B CA  1 
ATOM   3027  C  C   . HIS C  1 111 ? 113.712 -6.680  6.016   1.00 11.69 ? 110 HIS B C   1 
ATOM   3028  O  O   . HIS C  1 111 ? 114.542 -6.148  6.762   1.00 11.89 ? 110 HIS B O   1 
ATOM   3029  C  CB  . HIS C  1 111 ? 115.578 -7.004  4.397   1.00 14.95 ? 110 HIS B CB  1 
ATOM   3030  C  CG  . HIS C  1 111 ? 116.472 -7.910  3.538   1.00 15.94 ? 110 HIS B CG  1 
ATOM   3031  N  ND1 . HIS C  1 111 ? 117.773 -7.713  3.338   1.00 13.77 ? 110 HIS B ND1 1 
ATOM   3032  C  CD2 . HIS C  1 111 ? 116.092 -9.074  2.843   1.00 16.52 ? 110 HIS B CD2 1 
ATOM   3033  C  CE1 . HIS C  1 111 ? 118.189 -8.701  2.562   1.00 17.68 ? 110 HIS B CE1 1 
ATOM   3034  N  NE2 . HIS C  1 111 ? 117.180 -9.519  2.264   1.00 14.74 ? 110 HIS B NE2 1 
ATOM   3035  N  N   . SER C  1 112 ? 112.378 -6.503  6.143   1.00 9.32  ? 111 SER B N   1 
ATOM   3036  C  CA  . SER C  1 112 ? 111.776 -5.624  7.135   1.00 7.34  ? 111 SER B CA  1 
ATOM   3037  C  C   . SER C  1 112 ? 111.706 -6.365  8.438   1.00 4.31  ? 111 SER B C   1 
ATOM   3038  O  O   . SER C  1 112 ? 111.097 -7.428  8.504   1.00 4.07  ? 111 SER B O   1 
ATOM   3039  C  CB  . SER C  1 112 ? 110.383 -5.257  6.783   1.00 6.88  ? 111 SER B CB  1 
ATOM   3040  O  OG  . SER C  1 112 ? 109.818 -4.349  7.730   1.00 12.41 ? 111 SER B OG  1 
ATOM   3041  N  N   . ILE C  1 113 ? 112.350 -5.752  9.414   1.00 2.00  ? 112 ILE B N   1 
ATOM   3042  C  CA  . ILE C  1 113 ? 112.388 -6.262  10.749  1.00 2.00  ? 112 ILE B CA  1 
ATOM   3043  C  C   . ILE C  1 113 ? 111.181 -5.830  11.578  1.00 2.26  ? 112 ILE B C   1 
ATOM   3044  O  O   . ILE C  1 113 ? 111.083 -6.129  12.769  1.00 4.65  ? 112 ILE B O   1 
ATOM   3045  C  CB  . ILE C  1 113 ? 113.689 -5.808  11.412  1.00 2.00  ? 112 ILE B CB  1 
ATOM   3046  C  CG1 . ILE C  1 113 ? 113.799 -4.314  11.490  1.00 2.00  ? 112 ILE B CG1 1 
ATOM   3047  C  CG2 . ILE C  1 113 ? 114.826 -6.434  10.614  1.00 2.00  ? 112 ILE B CG2 1 
ATOM   3048  C  CD1 . ILE C  1 113 ? 115.103 -3.806  12.120  1.00 2.12  ? 112 ILE B CD1 1 
ATOM   3049  N  N   . ILE C  1 114 ? 110.233 -5.086  11.046  1.00 2.86  ? 113 ILE B N   1 
ATOM   3050  C  CA  . ILE C  1 114 ? 109.112 -4.600  11.833  1.00 4.33  ? 113 ILE B CA  1 
ATOM   3051  C  C   . ILE C  1 114 ? 108.129 -5.736  12.089  1.00 2.96  ? 113 ILE B C   1 
ATOM   3052  O  O   . ILE C  1 114 ? 107.742 -6.381  11.129  1.00 4.59  ? 113 ILE B O   1 
ATOM   3053  C  CB  . ILE C  1 114 ? 108.485 -3.397  11.049  1.00 2.00  ? 113 ILE B CB  1 
ATOM   3054  C  CG1 . ILE C  1 114 ? 109.415 -2.223  11.267  1.00 2.15  ? 113 ILE B CG1 1 
ATOM   3055  C  CG2 . ILE C  1 114 ? 107.073 -3.082  11.491  1.00 2.00  ? 113 ILE B CG2 1 
ATOM   3056  C  CD1 . ILE C  1 114 ? 108.934 -0.862  10.756  1.00 2.00  ? 113 ILE B CD1 1 
ATOM   3057  N  N   . GLY C  1 115 ? 107.682 -5.957  13.322  1.00 2.87  ? 114 GLY B N   1 
ATOM   3058  C  CA  . GLY C  1 115 ? 106.822 -7.058  13.694  1.00 2.00  ? 114 GLY B CA  1 
ATOM   3059  C  C   . GLY C  1 115 ? 107.669 -8.258  14.122  1.00 3.70  ? 114 GLY B C   1 
ATOM   3060  O  O   . GLY C  1 115 ? 107.130 -9.337  14.417  1.00 4.18  ? 114 GLY B O   1 
ATOM   3061  N  N   . ARG C  1 116 ? 108.997 -8.132  14.144  1.00 2.00  ? 115 ARG B N   1 
ATOM   3062  C  CA  . ARG C  1 116 ? 109.903 -9.206  14.516  1.00 2.59  ? 115 ARG B CA  1 
ATOM   3063  C  C   . ARG C  1 116 ? 110.467 -8.909  15.900  1.00 2.82  ? 115 ARG B C   1 
ATOM   3064  O  O   . ARG C  1 116 ? 110.197 -7.828  16.422  1.00 5.82  ? 115 ARG B O   1 
ATOM   3065  C  CB  . ARG C  1 116 ? 111.012 -9.316  13.420  1.00 2.00  ? 115 ARG B CB  1 
ATOM   3066  C  CG  . ARG C  1 116 ? 110.371 -9.630  12.045  1.00 2.00  ? 115 ARG B CG  1 
ATOM   3067  C  CD  . ARG C  1 116 ? 111.348 -9.942  10.922  1.00 2.00  ? 115 ARG B CD  1 
ATOM   3068  N  NE  . ARG C  1 116 ? 110.689 -10.076 9.626   1.00 2.86  ? 115 ARG B NE  1 
ATOM   3069  C  CZ  . ARG C  1 116 ? 110.071 -11.218 9.258   1.00 5.97  ? 115 ARG B CZ  1 
ATOM   3070  N  NH1 . ARG C  1 116 ? 110.020 -12.308 10.046  1.00 3.12  ? 115 ARG B NH1 1 
ATOM   3071  N  NH2 . ARG C  1 116 ? 109.486 -11.292 8.069   1.00 2.00  ? 115 ARG B NH2 1 
ATOM   3072  N  N   . THR C  1 117 ? 111.236 -9.761  16.561  1.00 3.82  ? 116 THR B N   1 
ATOM   3073  C  CA  . THR C  1 117 ? 111.718 -9.503  17.924  1.00 3.07  ? 116 THR B CA  1 
ATOM   3074  C  C   . THR C  1 117 ? 113.166 -9.045  18.019  1.00 2.24  ? 116 THR B C   1 
ATOM   3075  O  O   . THR C  1 117 ? 114.020 -9.659  17.402  1.00 4.47  ? 116 THR B O   1 
ATOM   3076  C  CB  . THR C  1 117 ? 111.516 -10.793 18.750  1.00 2.00  ? 116 THR B CB  1 
ATOM   3077  O  OG1 . THR C  1 117 ? 110.128 -11.049 18.689  1.00 2.18  ? 116 THR B OG1 1 
ATOM   3078  C  CG2 . THR C  1 117 ? 111.860 -10.705 20.204  1.00 2.00  ? 116 THR B CG2 1 
ATOM   3079  N  N   . LEU C  1 118 ? 113.517 -7.997  18.729  1.00 2.00  ? 117 LEU B N   1 
ATOM   3080  C  CA  . LEU C  1 118 ? 114.904 -7.653  18.975  1.00 2.27  ? 117 LEU B CA  1 
ATOM   3081  C  C   . LEU C  1 118 ? 115.364 -8.356  20.240  1.00 3.50  ? 117 LEU B C   1 
ATOM   3082  O  O   . LEU C  1 118 ? 114.677 -8.268  21.267  1.00 3.58  ? 117 LEU B O   1 
ATOM   3083  C  CB  . LEU C  1 118 ? 115.024 -6.188  19.177  1.00 2.00  ? 117 LEU B CB  1 
ATOM   3084  C  CG  . LEU C  1 118 ? 116.386 -5.665  19.398  1.00 2.00  ? 117 LEU B CG  1 
ATOM   3085  C  CD1 . LEU C  1 118 ? 117.322 -6.003  18.261  1.00 2.00  ? 117 LEU B CD1 1 
ATOM   3086  C  CD2 . LEU C  1 118 ? 116.233 -4.200  19.526  1.00 3.44  ? 117 LEU B CD2 1 
ATOM   3087  N  N   . VAL C  1 119 ? 116.523 -9.017  20.259  1.00 5.40  ? 118 VAL B N   1 
ATOM   3088  C  CA  . VAL C  1 119 ? 116.917 -9.810  21.412  1.00 4.12  ? 118 VAL B CA  1 
ATOM   3089  C  C   . VAL C  1 119 ? 118.309 -9.449  21.855  1.00 4.60  ? 118 VAL B C   1 
ATOM   3090  O  O   . VAL C  1 119 ? 119.180 -9.218  21.022  1.00 5.13  ? 118 VAL B O   1 
ATOM   3091  C  CB  . VAL C  1 119 ? 116.866 -11.303 21.074  1.00 2.00  ? 118 VAL B CB  1 
ATOM   3092  C  CG1 . VAL C  1 119 ? 117.127 -12.142 22.303  1.00 2.00  ? 118 VAL B CG1 1 
ATOM   3093  C  CG2 . VAL C  1 119 ? 115.519 -11.640 20.538  1.00 2.00  ? 118 VAL B CG2 1 
ATOM   3094  N  N   . VAL C  1 120 ? 118.508 -9.341  23.166  1.00 5.49  ? 119 VAL B N   1 
ATOM   3095  C  CA  . VAL C  1 120 ? 119.835 -9.167  23.711  1.00 6.38  ? 119 VAL B CA  1 
ATOM   3096  C  C   . VAL C  1 120 ? 120.081 -10.457 24.478  1.00 6.06  ? 119 VAL B C   1 
ATOM   3097  O  O   . VAL C  1 120 ? 119.245 -10.959 25.239  1.00 6.04  ? 119 VAL B O   1 
ATOM   3098  C  CB  . VAL C  1 120 ? 119.940 -7.925  24.647  1.00 7.13  ? 119 VAL B CB  1 
ATOM   3099  C  CG1 . VAL C  1 120 ? 119.132 -7.996  25.918  1.00 7.68  ? 119 VAL B CG1 1 
ATOM   3100  C  CG2 . VAL C  1 120 ? 121.412 -7.832  25.011  1.00 9.57  ? 119 VAL B CG2 1 
ATOM   3101  N  N   . HIS C  1 121 ? 121.228 -11.029 24.160  1.00 5.14  ? 120 HIS B N   1 
ATOM   3102  C  CA  . HIS C  1 121 ? 121.668 -12.257 24.729  1.00 4.08  ? 120 HIS B CA  1 
ATOM   3103  C  C   . HIS C  1 121 ? 122.593 -12.188 25.966  1.00 5.32  ? 120 HIS B C   1 
ATOM   3104  O  O   . HIS C  1 121 ? 123.159 -11.187 26.435  1.00 2.09  ? 120 HIS B O   1 
ATOM   3105  C  CB  . HIS C  1 121 ? 122.298 -13.018 23.596  1.00 5.03  ? 120 HIS B CB  1 
ATOM   3106  C  CG  . HIS C  1 121 ? 121.350 -13.650 22.591  1.00 4.30  ? 120 HIS B CG  1 
ATOM   3107  N  ND1 . HIS C  1 121 ? 120.832 -14.870 22.554  1.00 2.10  ? 120 HIS B ND1 1 
ATOM   3108  C  CD2 . HIS C  1 121 ? 120.868 -12.980 21.483  1.00 9.88  ? 120 HIS B CD2 1 
ATOM   3109  C  CE1 . HIS C  1 121 ? 120.072 -14.940 21.473  1.00 4.98  ? 120 HIS B CE1 1 
ATOM   3110  N  NE2 . HIS C  1 121 ? 120.084 -13.792 20.812  1.00 8.10  ? 120 HIS B NE2 1 
ATOM   3111  N  N   . GLU C  1 122 ? 122.710 -13.374 26.513  1.00 7.12  ? 121 GLU B N   1 
ATOM   3112  C  CA  . GLU C  1 122 ? 123.477 -13.648 27.696  1.00 11.09 ? 121 GLU B CA  1 
ATOM   3113  C  C   . GLU C  1 122 ? 124.943 -13.355 27.525  1.00 12.82 ? 121 GLU B C   1 
ATOM   3114  O  O   . GLU C  1 122 ? 125.533 -12.577 28.284  1.00 14.63 ? 121 GLU B O   1 
ATOM   3115  C  CB  . GLU C  1 122 ? 123.265 -15.091 28.034  1.00 12.77 ? 121 GLU B CB  1 
ATOM   3116  C  CG  . GLU C  1 122 ? 123.702 -15.548 29.398  1.00 14.97 ? 121 GLU B CG  1 
ATOM   3117  C  CD  . GLU C  1 122 ? 123.697 -17.069 29.544  1.00 18.88 ? 121 GLU B CD  1 
ATOM   3118  O  OE1 . GLU C  1 122 ? 123.412 -17.800 28.591  1.00 18.12 ? 121 GLU B OE1 1 
ATOM   3119  O  OE2 . GLU C  1 122 ? 124.001 -17.539 30.646  1.00 24.82 ? 121 GLU B OE2 1 
ATOM   3120  N  N   . LYS C  1 123 ? 125.464 -13.945 26.459  1.00 14.33 ? 122 LYS B N   1 
ATOM   3121  C  CA  . LYS C  1 123 ? 126.876 -13.938 26.132  1.00 15.84 ? 122 LYS B CA  1 
ATOM   3122  C  C   . LYS C  1 123 ? 127.248 -13.073 24.946  1.00 14.69 ? 122 LYS B C   1 
ATOM   3123  O  O   . LYS C  1 123 ? 126.411 -12.463 24.282  1.00 14.93 ? 122 LYS B O   1 
ATOM   3124  C  CB  . LYS C  1 123 ? 127.331 -15.330 25.812  1.00 15.88 ? 122 LYS B CB  1 
ATOM   3125  C  CG  . LYS C  1 123 ? 127.339 -16.351 26.924  1.00 23.11 ? 122 LYS B CG  1 
ATOM   3126  C  CD  . LYS C  1 123 ? 127.621 -17.661 26.185  1.00 27.87 ? 122 LYS B CD  1 
ATOM   3127  C  CE  . LYS C  1 123 ? 127.626 -18.870 27.103  1.00 29.79 ? 122 LYS B CE  1 
ATOM   3128  N  NZ  . LYS C  1 123 ? 127.257 -20.027 26.305  1.00 30.90 ? 122 LYS B NZ  1 
ATOM   3129  N  N   . ALA C  1 124 ? 128.551 -13.039 24.690  1.00 14.73 ? 123 ALA B N   1 
ATOM   3130  C  CA  . ALA C  1 124 ? 129.104 -12.429 23.503  1.00 13.01 ? 123 ALA B CA  1 
ATOM   3131  C  C   . ALA C  1 124 ? 128.807 -13.415 22.382  1.00 12.08 ? 123 ALA B C   1 
ATOM   3132  O  O   . ALA C  1 124 ? 128.810 -14.648 22.536  1.00 11.52 ? 123 ALA B O   1 
ATOM   3133  C  CB  . ALA C  1 124 ? 130.625 -12.258 23.626  1.00 8.08  ? 123 ALA B CB  1 
ATOM   3134  N  N   . ASP C  1 125 ? 128.445 -12.823 21.267  1.00 11.28 ? 124 ASP B N   1 
ATOM   3135  C  CA  . ASP C  1 125 ? 128.249 -13.575 20.062  1.00 12.51 ? 124 ASP B CA  1 
ATOM   3136  C  C   . ASP C  1 125 ? 129.677 -13.687 19.493  1.00 15.20 ? 124 ASP B C   1 
ATOM   3137  O  O   . ASP C  1 125 ? 130.398 -12.675 19.387  1.00 16.19 ? 124 ASP B O   1 
ATOM   3138  C  CB  . ASP C  1 125 ? 127.311 -12.745 19.189  1.00 12.59 ? 124 ASP B CB  1 
ATOM   3139  C  CG  . ASP C  1 125 ? 127.070 -13.200 17.761  1.00 11.89 ? 124 ASP B CG  1 
ATOM   3140  O  OD1 . ASP C  1 125 ? 127.602 -14.236 17.408  1.00 10.71 ? 124 ASP B OD1 1 
ATOM   3141  O  OD2 . ASP C  1 125 ? 126.351 -12.528 17.005  1.00 12.12 ? 124 ASP B OD2 1 
ATOM   3142  N  N   . ASP C  1 126 ? 130.135 -14.880 19.104  1.00 14.47 ? 125 ASP B N   1 
ATOM   3143  C  CA  . ASP C  1 126 ? 131.452 -15.015 18.487  1.00 14.13 ? 125 ASP B CA  1 
ATOM   3144  C  C   . ASP C  1 126 ? 131.548 -14.620 16.995  1.00 13.16 ? 125 ASP B C   1 
ATOM   3145  O  O   . ASP C  1 126 ? 132.569 -14.690 16.311  1.00 13.06 ? 125 ASP B O   1 
ATOM   3146  C  CB  . ASP C  1 126 ? 131.920 -16.466 18.676  1.00 13.33 ? 125 ASP B CB  1 
ATOM   3147  C  CG  . ASP C  1 126 ? 131.082 -17.522 17.999  1.00 14.17 ? 125 ASP B CG  1 
ATOM   3148  O  OD1 . ASP C  1 126 ? 130.548 -17.298 16.918  1.00 12.14 ? 125 ASP B OD1 1 
ATOM   3149  O  OD2 . ASP C  1 126 ? 130.980 -18.609 18.574  1.00 17.31 ? 125 ASP B OD2 1 
ATOM   3150  N  N   . LEU C  1 127 ? 130.389 -14.397 16.410  1.00 10.88 ? 126 LEU B N   1 
ATOM   3151  C  CA  . LEU C  1 127 ? 130.241 -13.919 15.043  1.00 11.86 ? 126 LEU B CA  1 
ATOM   3152  C  C   . LEU C  1 127 ? 130.515 -14.943 13.965  1.00 12.73 ? 126 LEU B C   1 
ATOM   3153  O  O   . LEU C  1 127 ? 130.804 -14.565 12.827  1.00 14.21 ? 126 LEU B O   1 
ATOM   3154  C  CB  . LEU C  1 127 ? 131.154 -12.674 14.745  1.00 7.15  ? 126 LEU B CB  1 
ATOM   3155  C  CG  . LEU C  1 127 ? 131.309 -11.619 15.799  1.00 3.14  ? 126 LEU B CG  1 
ATOM   3156  C  CD1 . LEU C  1 127 ? 132.307 -10.572 15.396  1.00 2.00  ? 126 LEU B CD1 1 
ATOM   3157  C  CD2 . LEU C  1 127 ? 129.933 -11.058 16.060  1.00 3.95  ? 126 LEU B CD2 1 
ATOM   3158  N  N   . GLY C  1 128 ? 130.316 -16.223 14.249  1.00 14.55 ? 127 GLY B N   1 
ATOM   3159  C  CA  . GLY C  1 128 ? 130.556 -17.262 13.258  1.00 18.47 ? 127 GLY B CA  1 
ATOM   3160  C  C   . GLY C  1 128 ? 131.964 -17.845 13.369  1.00 22.95 ? 127 GLY B C   1 
ATOM   3161  O  O   . GLY C  1 128 ? 132.251 -18.914 12.819  1.00 25.70 ? 127 GLY B O   1 
ATOM   3162  N  N   . LYS C  1 129 ? 132.878 -17.245 14.139  1.00 25.32 ? 128 LYS B N   1 
ATOM   3163  C  CA  . LYS C  1 129 ? 134.244 -17.739 14.263  1.00 27.90 ? 128 LYS B CA  1 
ATOM   3164  C  C   . LYS C  1 129 ? 134.525 -18.641 15.479  1.00 31.18 ? 128 LYS B C   1 
ATOM   3165  O  O   . LYS C  1 129 ? 135.523 -18.496 16.212  1.00 32.60 ? 128 LYS B O   1 
ATOM   3166  C  CB  . LYS C  1 129 ? 135.227 -16.582 14.332  1.00 28.26 ? 128 LYS B CB  1 
ATOM   3167  C  CG  . LYS C  1 129 ? 134.807 -15.152 14.170  1.00 27.19 ? 128 LYS B CG  1 
ATOM   3168  C  CD  . LYS C  1 129 ? 134.787 -14.704 12.730  1.00 28.43 ? 128 LYS B CD  1 
ATOM   3169  C  CE  . LYS C  1 129 ? 134.549 -13.199 12.888  1.00 31.50 ? 128 LYS B CE  1 
ATOM   3170  N  NZ  . LYS C  1 129 ? 134.465 -12.575 11.586  1.00 37.13 ? 128 LYS B NZ  1 
ATOM   3171  N  N   . GLY C  1 130 ? 133.652 -19.602 15.765  1.00 31.52 ? 129 GLY B N   1 
ATOM   3172  C  CA  . GLY C  1 130 ? 133.879 -20.451 16.920  1.00 31.18 ? 129 GLY B CA  1 
ATOM   3173  C  C   . GLY C  1 130 ? 134.259 -21.848 16.500  1.00 33.14 ? 129 GLY B C   1 
ATOM   3174  O  O   . GLY C  1 130 ? 134.484 -22.732 17.333  1.00 31.09 ? 129 GLY B O   1 
ATOM   3175  N  N   . GLY C  1 131 ? 134.231 -22.085 15.183  1.00 34.79 ? 130 GLY B N   1 
ATOM   3176  C  CA  . GLY C  1 131 ? 134.647 -23.351 14.613  1.00 37.09 ? 130 GLY B CA  1 
ATOM   3177  C  C   . GLY C  1 131 ? 133.657 -24.494 14.786  1.00 39.30 ? 130 GLY B C   1 
ATOM   3178  O  O   . GLY C  1 131 ? 133.764 -25.523 14.105  1.00 40.81 ? 130 GLY B O   1 
ATOM   3179  N  N   . ASN C  1 132 ? 132.739 -24.374 15.741  1.00 38.97 ? 131 ASN B N   1 
ATOM   3180  C  CA  . ASN C  1 132 ? 131.706 -25.371 15.901  1.00 37.84 ? 131 ASN B CA  1 
ATOM   3181  C  C   . ASN C  1 132 ? 130.483 -24.925 15.121  1.00 36.14 ? 131 ASN B C   1 
ATOM   3182  O  O   . ASN C  1 132 ? 130.403 -23.814 14.577  1.00 35.08 ? 131 ASN B O   1 
ATOM   3183  C  CB  . ASN C  1 132 ? 131.368 -25.559 17.399  1.00 38.15 ? 131 ASN B CB  1 
ATOM   3184  C  CG  . ASN C  1 132 ? 130.885 -24.309 18.096  1.00 38.08 ? 131 ASN B CG  1 
ATOM   3185  O  OD1 . ASN C  1 132 ? 129.833 -23.763 17.752  1.00 40.04 ? 131 ASN B OD1 1 
ATOM   3186  N  ND2 . ASN C  1 132 ? 131.647 -23.854 19.077  1.00 36.22 ? 131 ASN B ND2 1 
ATOM   3187  N  N   . GLU C  1 133 ? 129.547 -25.868 15.164  1.00 34.89 ? 132 GLU B N   1 
ATOM   3188  C  CA  . GLU C  1 133 ? 128.268 -25.791 14.493  1.00 34.12 ? 132 GLU B CA  1 
ATOM   3189  C  C   . GLU C  1 133 ? 127.412 -24.647 15.012  1.00 31.81 ? 132 GLU B C   1 
ATOM   3190  O  O   . GLU C  1 133 ? 126.928 -23.818 14.244  1.00 32.00 ? 132 GLU B O   1 
ATOM   3191  C  CB  . GLU C  1 133 ? 127.593 -27.119 14.707  1.00 37.38 ? 132 GLU B CB  1 
ATOM   3192  C  CG  . GLU C  1 133 ? 126.432 -27.475 13.790  1.00 42.44 ? 132 GLU B CG  1 
ATOM   3193  C  CD  . GLU C  1 133 ? 125.904 -28.896 14.060  1.00 44.77 ? 132 GLU B CD  1 
ATOM   3194  O  OE1 . GLU C  1 133 ? 126.499 -29.841 13.520  1.00 44.10 ? 132 GLU B OE1 1 
ATOM   3195  O  OE2 . GLU C  1 133 ? 124.913 -29.053 14.801  1.00 45.00 ? 132 GLU B OE2 1 
ATOM   3196  N  N   . GLU C  1 134 ? 127.264 -24.535 16.333  1.00 29.11 ? 133 GLU B N   1 
ATOM   3197  C  CA  . GLU C  1 134 ? 126.445 -23.501 16.902  1.00 25.09 ? 133 GLU B CA  1 
ATOM   3198  C  C   . GLU C  1 134 ? 126.941 -22.110 16.550  1.00 24.70 ? 133 GLU B C   1 
ATOM   3199  O  O   . GLU C  1 134 ? 126.111 -21.195 16.376  1.00 24.69 ? 133 GLU B O   1 
ATOM   3200  C  CB  . GLU C  1 134 ? 126.409 -23.731 18.365  1.00 25.30 ? 133 GLU B CB  1 
ATOM   3201  C  CG  . GLU C  1 134 ? 125.111 -24.484 18.670  1.00 27.18 ? 133 GLU B CG  1 
ATOM   3202  C  CD  . GLU C  1 134 ? 123.900 -23.556 18.807  1.00 29.09 ? 133 GLU B CD  1 
ATOM   3203  O  OE1 . GLU C  1 134 ? 124.038 -22.512 19.461  1.00 28.88 ? 133 GLU B OE1 1 
ATOM   3204  O  OE2 . GLU C  1 134 ? 122.825 -23.918 18.313  1.00 28.06 ? 133 GLU B OE2 1 
ATOM   3205  N  N   . SER C  1 135 ? 128.249 -21.903 16.373  1.00 23.29 ? 134 SER B N   1 
ATOM   3206  C  CA  . SER C  1 135 ? 128.778 -20.631 15.891  1.00 21.48 ? 134 SER B CA  1 
ATOM   3207  C  C   . SER C  1 135 ? 128.017 -20.237 14.628  1.00 22.05 ? 134 SER B C   1 
ATOM   3208  O  O   . SER C  1 135 ? 127.431 -19.162 14.623  1.00 24.01 ? 134 SER B O   1 
ATOM   3209  C  CB  . SER C  1 135 ? 130.225 -20.764 15.534  1.00 19.58 ? 134 SER B CB  1 
ATOM   3210  O  OG  . SER C  1 135 ? 130.969 -19.672 15.996  1.00 10.21 ? 134 SER B OG  1 
ATOM   3211  N  N   . THR C  1 136 ? 127.865 -21.069 13.599  1.00 22.12 ? 135 THR B N   1 
ATOM   3212  C  CA  . THR C  1 136 ? 127.210 -20.689 12.350  1.00 21.53 ? 135 THR B CA  1 
ATOM   3213  C  C   . THR C  1 136 ? 125.691 -20.650 12.381  1.00 22.60 ? 135 THR B C   1 
ATOM   3214  O  O   . THR C  1 136 ? 125.023 -20.317 11.390  1.00 21.30 ? 135 THR B O   1 
ATOM   3215  C  CB  . THR C  1 136 ? 127.676 -21.644 11.265  1.00 21.31 ? 135 THR B CB  1 
ATOM   3216  O  OG1 . THR C  1 136 ? 127.781 -22.944 11.847  1.00 22.93 ? 135 THR B OG1 1 
ATOM   3217  C  CG2 . THR C  1 136 ? 128.971 -21.181 10.663  1.00 20.60 ? 135 THR B CG2 1 
ATOM   3218  N  N   . LYS C  1 137 ? 125.106 -20.972 13.531  1.00 23.52 ? 136 LYS B N   1 
ATOM   3219  C  CA  . LYS C  1 137 ? 123.672 -20.912 13.660  1.00 22.57 ? 136 LYS B CA  1 
ATOM   3220  C  C   . LYS C  1 137 ? 123.283 -19.772 14.569  1.00 20.91 ? 136 LYS B C   1 
ATOM   3221  O  O   . LYS C  1 137 ? 122.380 -19.018 14.213  1.00 23.50 ? 136 LYS B O   1 
ATOM   3222  C  CB  . LYS C  1 137 ? 123.151 -22.244 14.193  1.00 24.13 ? 136 LYS B CB  1 
ATOM   3223  C  CG  . LYS C  1 137 ? 123.227 -23.439 13.199  1.00 28.84 ? 136 LYS B CG  1 
ATOM   3224  C  CD  . LYS C  1 137 ? 122.721 -24.729 13.870  1.00 35.43 ? 136 LYS B CD  1 
ATOM   3225  C  CE  . LYS C  1 137 ? 123.731 -25.245 14.944  1.00 38.96 ? 136 LYS B CE  1 
ATOM   3226  N  NZ  . LYS C  1 137 ? 123.146 -26.160 15.930  1.00 42.14 ? 136 LYS B NZ  1 
ATOM   3227  N  N   . THR C  1 138 ? 123.948 -19.546 15.687  1.00 18.01 ? 137 THR B N   1 
ATOM   3228  C  CA  . THR C  1 138 ? 123.517 -18.532 16.621  1.00 16.37 ? 137 THR B CA  1 
ATOM   3229  C  C   . THR C  1 138 ? 124.662 -17.761 17.183  1.00 14.36 ? 137 THR B C   1 
ATOM   3230  O  O   . THR C  1 138 ? 124.487 -16.949 18.093  1.00 18.02 ? 137 THR B O   1 
ATOM   3231  C  CB  . THR C  1 138 ? 122.766 -19.134 17.814  1.00 19.45 ? 137 THR B CB  1 
ATOM   3232  O  OG1 . THR C  1 138 ? 123.674 -19.982 18.517  1.00 23.37 ? 137 THR B OG1 1 
ATOM   3233  C  CG2 . THR C  1 138 ? 121.641 -20.078 17.403  1.00 20.62 ? 137 THR B CG2 1 
ATOM   3234  N  N   . GLY C  1 139 ? 125.868 -18.036 16.716  1.00 12.75 ? 138 GLY B N   1 
ATOM   3235  C  CA  . GLY C  1 139 ? 127.061 -17.377 17.202  1.00 10.92 ? 138 GLY B CA  1 
ATOM   3236  C  C   . GLY C  1 139 ? 127.337 -17.578 18.679  1.00 10.74 ? 138 GLY B C   1 
ATOM   3237  O  O   . GLY C  1 139 ? 128.055 -16.758 19.252  1.00 9.18  ? 138 GLY B O   1 
ATOM   3238  N  N   . ASN C  1 140 ? 126.792 -18.662 19.263  1.00 12.34 ? 139 ASN B N   1 
ATOM   3239  C  CA  . ASN C  1 140 ? 126.934 -19.062 20.678  1.00 13.99 ? 139 ASN B CA  1 
ATOM   3240  C  C   . ASN C  1 140 ? 126.672 -17.927 21.648  1.00 13.25 ? 139 ASN B C   1 
ATOM   3241  O  O   . ASN C  1 140 ? 127.470 -17.641 22.539  1.00 15.69 ? 139 ASN B O   1 
ATOM   3242  C  CB  . ASN C  1 140 ? 128.340 -19.598 21.000  1.00 15.31 ? 139 ASN B CB  1 
ATOM   3243  C  CG  . ASN C  1 140 ? 128.665 -20.923 20.355  1.00 19.32 ? 139 ASN B CG  1 
ATOM   3244  O  OD1 . ASN C  1 140 ? 129.577 -21.001 19.538  1.00 24.18 ? 139 ASN B OD1 1 
ATOM   3245  N  ND2 . ASN C  1 140 ? 127.988 -22.029 20.628  1.00 19.01 ? 139 ASN B ND2 1 
ATOM   3246  N  N   . ALA C  1 141 ? 125.557 -17.238 21.508  1.00 12.40 ? 140 ALA B N   1 
ATOM   3247  C  CA  . ALA C  1 141 ? 125.355 -16.081 22.358  1.00 12.17 ? 140 ALA B CA  1 
ATOM   3248  C  C   . ALA C  1 141 ? 124.613 -16.405 23.635  1.00 12.52 ? 140 ALA B C   1 
ATOM   3249  O  O   . ALA C  1 141 ? 124.427 -15.511 24.462  1.00 15.91 ? 140 ALA B O   1 
ATOM   3250  C  CB  . ALA C  1 141 ? 124.591 -14.994 21.590  1.00 9.61  ? 140 ALA B CB  1 
ATOM   3251  N  N   . GLY C  1 142 ? 124.143 -17.631 23.864  1.00 10.41 ? 141 GLY B N   1 
ATOM   3252  C  CA  . GLY C  1 142 ? 123.455 -17.950 25.093  1.00 6.44  ? 141 GLY B CA  1 
ATOM   3253  C  C   . GLY C  1 142 ? 121.988 -17.588 25.039  1.00 7.53  ? 141 GLY B C   1 
ATOM   3254  O  O   . GLY C  1 142 ? 121.365 -17.431 23.976  1.00 7.96  ? 141 GLY B O   1 
ATOM   3255  N  N   . SER C  1 143 ? 121.437 -17.487 26.237  1.00 8.54  ? 142 SER B N   1 
ATOM   3256  C  CA  . SER C  1 143 ? 120.056 -17.109 26.436  1.00 7.78  ? 142 SER B CA  1 
ATOM   3257  C  C   . SER C  1 143 ? 119.704 -15.737 25.938  1.00 7.34  ? 142 SER B C   1 
ATOM   3258  O  O   . SER C  1 143 ? 120.528 -14.837 25.751  1.00 5.36  ? 142 SER B O   1 
ATOM   3259  C  CB  . SER C  1 143 ? 119.730 -17.187 27.915  1.00 9.87  ? 142 SER B CB  1 
ATOM   3260  O  OG  . SER C  1 143 ? 119.604 -18.589 28.089  1.00 19.01 ? 142 SER B OG  1 
ATOM   3261  N  N   . ARG C  1 144 ? 118.420 -15.721 25.652  1.00 7.51  ? 143 ARG B N   1 
ATOM   3262  C  CA  . ARG C  1 144 ? 117.703 -14.527 25.316  1.00 6.16  ? 143 ARG B CA  1 
ATOM   3263  C  C   . ARG C  1 144 ? 117.427 -13.861 26.660  1.00 4.52  ? 143 ARG B C   1 
ATOM   3264  O  O   . ARG C  1 144 ? 116.590 -14.333 27.430  1.00 6.11  ? 143 ARG B O   1 
ATOM   3265  C  CB  . ARG C  1 144 ? 116.420 -14.962 24.575  1.00 5.74  ? 143 ARG B CB  1 
ATOM   3266  C  CG  . ARG C  1 144 ? 116.712 -15.682 23.278  1.00 9.07  ? 143 ARG B CG  1 
ATOM   3267  C  CD  . ARG C  1 144 ? 115.560 -16.502 22.730  1.00 11.46 ? 143 ARG B CD  1 
ATOM   3268  N  NE  . ARG C  1 144 ? 116.056 -17.225 21.562  1.00 12.66 ? 143 ARG B NE  1 
ATOM   3269  C  CZ  . ARG C  1 144 ? 115.275 -17.649 20.551  1.00 12.30 ? 143 ARG B CZ  1 
ATOM   3270  N  NH1 . ARG C  1 144 ? 113.961 -17.467 20.510  1.00 12.49 ? 143 ARG B NH1 1 
ATOM   3271  N  NH2 . ARG C  1 144 ? 115.826 -18.207 19.486  1.00 11.88 ? 143 ARG B NH2 1 
ATOM   3272  N  N   . LEU C  1 145 ? 118.071 -12.788 27.058  1.00 4.41  ? 144 LEU B N   1 
ATOM   3273  C  CA  . LEU C  1 145 ? 117.739 -12.180 28.341  1.00 3.77  ? 144 LEU B CA  1 
ATOM   3274  C  C   . LEU C  1 145 ? 116.570 -11.203 28.339  1.00 3.76  ? 144 LEU B C   1 
ATOM   3275  O  O   . LEU C  1 145 ? 115.808 -11.099 29.308  1.00 6.81  ? 144 LEU B O   1 
ATOM   3276  C  CB  . LEU C  1 145 ? 118.946 -11.450 28.907  1.00 2.00  ? 144 LEU B CB  1 
ATOM   3277  C  CG  . LEU C  1 145 ? 120.229 -12.230 29.163  1.00 2.00  ? 144 LEU B CG  1 
ATOM   3278  C  CD1 . LEU C  1 145 ? 121.152 -11.325 29.881  1.00 2.00  ? 144 LEU B CD1 1 
ATOM   3279  C  CD2 . LEU C  1 145 ? 120.011 -13.480 30.017  1.00 2.00  ? 144 LEU B CD2 1 
ATOM   3280  N  N   . ALA C  1 146 ? 116.438 -10.447 27.261  1.00 4.54  ? 145 ALA B N   1 
ATOM   3281  C  CA  . ALA C  1 146 ? 115.456 -9.388  27.080  1.00 3.35  ? 145 ALA B CA  1 
ATOM   3282  C  C   . ALA C  1 146 ? 115.045 -9.436  25.630  1.00 3.92  ? 145 ALA B C   1 
ATOM   3283  O  O   . ALA C  1 146 ? 115.854 -9.822  24.785  1.00 3.55  ? 145 ALA B O   1 
ATOM   3284  C  CB  . ALA C  1 146 ? 116.041 -8.025  27.246  1.00 2.00  ? 145 ALA B CB  1 
ATOM   3285  N  N   . CYS C  1 147 ? 113.837 -9.046  25.286  1.00 4.85  ? 146 CYS B N   1 
ATOM   3286  C  CA  . CYS C  1 147 ? 113.417 -9.018  23.904  1.00 4.93  ? 146 CYS B CA  1 
ATOM   3287  C  C   . CYS C  1 147 ? 112.174 -8.157  23.842  1.00 3.55  ? 146 CYS B C   1 
ATOM   3288  O  O   . CYS C  1 147 ? 111.664 -7.785  24.907  1.00 2.00  ? 146 CYS B O   1 
ATOM   3289  C  CB  . CYS C  1 147 ? 113.121 -10.435 23.403  1.00 5.17  ? 146 CYS B CB  1 
ATOM   3290  S  SG  . CYS C  1 147 ? 111.796 -11.120 24.377  1.00 6.18  ? 146 CYS B SG  1 
ATOM   3291  N  N   . GLY C  1 148 ? 111.763 -7.744  22.634  1.00 3.01  ? 147 GLY B N   1 
ATOM   3292  C  CA  . GLY C  1 148 ? 110.590 -6.899  22.419  1.00 2.00  ? 147 GLY B CA  1 
ATOM   3293  C  C   . GLY C  1 148 ? 110.321 -6.855  20.922  1.00 2.00  ? 147 GLY B C   1 
ATOM   3294  O  O   . GLY C  1 148 ? 111.274 -7.049  20.161  1.00 2.00  ? 147 GLY B O   1 
ATOM   3295  N  N   . VAL C  1 149 ? 109.095 -6.575  20.477  1.00 2.00  ? 148 VAL B N   1 
ATOM   3296  C  CA  . VAL C  1 149 ? 108.701 -6.556  19.074  1.00 2.00  ? 148 VAL B CA  1 
ATOM   3297  C  C   . VAL C  1 149 ? 109.020 -5.185  18.492  1.00 2.17  ? 148 VAL B C   1 
ATOM   3298  O  O   . VAL C  1 149 ? 108.696 -4.150  19.096  1.00 2.00  ? 148 VAL B O   1 
ATOM   3299  C  CB  . VAL C  1 149 ? 107.195 -6.845  18.969  1.00 2.00  ? 148 VAL B CB  1 
ATOM   3300  C  CG1 . VAL C  1 149 ? 106.771 -7.050  17.573  1.00 2.00  ? 148 VAL B CG1 1 
ATOM   3301  C  CG2 . VAL C  1 149 ? 106.869 -8.141  19.589  1.00 2.00  ? 148 VAL B CG2 1 
ATOM   3302  N  N   . ILE C  1 150 ? 109.676 -5.093  17.315  1.00 4.88  ? 149 ILE B N   1 
ATOM   3303  C  CA  . ILE C  1 150 ? 109.911 -3.786  16.676  1.00 2.48  ? 149 ILE B CA  1 
ATOM   3304  C  C   . ILE C  1 150 ? 108.582 -3.269  16.143  1.00 2.00  ? 149 ILE B C   1 
ATOM   3305  O  O   . ILE C  1 150 ? 107.914 -3.839  15.286  1.00 2.00  ? 149 ILE B O   1 
ATOM   3306  C  CB  . ILE C  1 150 ? 110.920 -3.892  15.519  1.00 2.00  ? 149 ILE B CB  1 
ATOM   3307  C  CG1 . ILE C  1 150 ? 112.250 -4.386  16.006  1.00 2.00  ? 149 ILE B CG1 1 
ATOM   3308  C  CG2 . ILE C  1 150 ? 111.193 -2.503  14.940  1.00 2.00  ? 149 ILE B CG2 1 
ATOM   3309  C  CD1 . ILE C  1 150 ? 112.569 -5.872  15.760  1.00 2.00  ? 149 ILE B CD1 1 
ATOM   3310  N  N   . GLY C  1 151 ? 108.125 -2.222  16.769  1.00 2.54  ? 150 GLY B N   1 
ATOM   3311  C  CA  . GLY C  1 151 ? 106.916 -1.538  16.377  1.00 3.95  ? 150 GLY B CA  1 
ATOM   3312  C  C   . GLY C  1 151 ? 107.224 -0.301  15.561  1.00 3.06  ? 150 GLY B C   1 
ATOM   3313  O  O   . GLY C  1 151 ? 108.340 0.201   15.596  1.00 6.32  ? 150 GLY B O   1 
ATOM   3314  N  N   . ILE C  1 152 ? 106.274 0.189   14.777  1.00 2.31  ? 151 ILE B N   1 
ATOM   3315  C  CA  . ILE C  1 152 ? 106.385 1.417   14.004  1.00 2.00  ? 151 ILE B CA  1 
ATOM   3316  C  C   . ILE C  1 152 ? 106.299 2.526   15.018  1.00 2.00  ? 151 ILE B C   1 
ATOM   3317  O  O   . ILE C  1 152 ? 105.483 2.488   15.931  1.00 2.00  ? 151 ILE B O   1 
ATOM   3318  C  CB  . ILE C  1 152 ? 105.211 1.567   12.989  1.00 2.00  ? 151 ILE B CB  1 
ATOM   3319  C  CG1 . ILE C  1 152 ? 105.342 0.445   11.988  1.00 2.85  ? 151 ILE B CG1 1 
ATOM   3320  C  CG2 . ILE C  1 152 ? 105.217 2.918   12.306  1.00 2.00  ? 151 ILE B CG2 1 
ATOM   3321  C  CD1 . ILE C  1 152 ? 104.091 0.258   11.117  1.00 2.00  ? 151 ILE B CD1 1 
ATOM   3322  N  N   . ALA C  1 153 ? 107.124 3.541   14.887  1.00 3.83  ? 152 ALA B N   1 
ATOM   3323  C  CA  . ALA C  1 153 ? 106.997 4.696   15.748  1.00 5.68  ? 152 ALA B CA  1 
ATOM   3324  C  C   . ALA C  1 153 ? 107.008 5.970   14.916  1.00 9.75  ? 152 ALA B C   1 
ATOM   3325  O  O   . ALA C  1 153 ? 106.832 5.966   13.683  1.00 10.04 ? 152 ALA B O   1 
ATOM   3326  C  CB  . ALA C  1 153 ? 108.141 4.663   16.731  1.00 3.85  ? 152 ALA B CB  1 
ATOM   3327  N  N   . GLN C  1 154 ? 107.203 7.064   15.645  1.00 16.98 ? 153 GLN B N   1 
ATOM   3328  C  CA  . GLN C  1 154 ? 107.319 8.443   15.183  1.00 23.88 ? 153 GLN B CA  1 
ATOM   3329  C  C   . GLN C  1 154 ? 108.222 9.147   16.267  1.00 26.43 ? 153 GLN B C   1 
ATOM   3330  O  O   . GLN C  1 154 ? 109.279 9.688   15.932  1.00 27.31 ? 153 GLN B O   1 
ATOM   3331  C  CB  . GLN C  1 154 ? 105.842 8.874   15.068  1.00 25.67 ? 153 GLN B CB  1 
ATOM   3332  C  CG  . GLN C  1 154 ? 105.352 10.283  15.258  1.00 31.10 ? 153 GLN B CG  1 
ATOM   3333  C  CD  . GLN C  1 154 ? 104.510 10.398  16.524  1.00 33.41 ? 153 GLN B CD  1 
ATOM   3334  O  OE1 . GLN C  1 154 ? 103.411 10.957  16.535  1.00 35.58 ? 153 GLN B OE1 1 
ATOM   3335  N  NE2 . GLN C  1 154 ? 104.974 9.913   17.670  1.00 37.17 ? 153 GLN B NE2 1 
ATOM   3336  O  OXT . GLN C  1 154 ? 107.949 9.039   17.479  1.00 30.16 ? 153 GLN B OXT 1 
HETATM 3337  C  C   . ACE D  1 1   ? 103.241 -11.351 4.533   1.00 34.46 ? 0   ACE G C   1 
HETATM 3338  O  O   . ACE D  1 1   ? 103.446 -12.527 4.192   1.00 34.75 ? 0   ACE G O   1 
HETATM 3339  C  CH3 . ACE D  1 1   ? 103.693 -10.192 3.658   1.00 35.36 ? 0   ACE G CH3 1 
ATOM   3340  N  N   . ALA D  1 2   ? 102.616 -10.990 5.664   1.00 32.25 ? 1   ALA G N   1 
ATOM   3341  C  CA  . ALA D  1 2   ? 102.219 -11.967 6.671   1.00 29.83 ? 1   ALA G CA  1 
ATOM   3342  C  C   . ALA D  1 2   ? 100.933 -12.771 6.428   1.00 26.46 ? 1   ALA G C   1 
ATOM   3343  O  O   . ALA D  1 2   ? 100.073 -12.427 5.609   1.00 28.24 ? 1   ALA G O   1 
ATOM   3344  C  CB  . ALA D  1 2   ? 102.113 -11.223 8.013   1.00 30.36 ? 1   ALA G CB  1 
ATOM   3345  N  N   . THR D  1 3   ? 100.841 -13.873 7.159   1.00 22.69 ? 2   THR G N   1 
ATOM   3346  C  CA  . THR D  1 3   ? 99.668  -14.718 7.177   1.00 19.28 ? 2   THR G CA  1 
ATOM   3347  C  C   . THR D  1 3   ? 99.106  -14.775 8.573   1.00 16.64 ? 2   THR G C   1 
ATOM   3348  O  O   . THR D  1 3   ? 97.899  -14.889 8.722   1.00 15.61 ? 2   THR G O   1 
ATOM   3349  C  CB  . THR D  1 3   ? 100.039 -16.112 6.747   1.00 19.77 ? 2   THR G CB  1 
ATOM   3350  O  OG1 . THR D  1 3   ? 100.386 -15.908 5.399   1.00 26.67 ? 2   THR G OG1 1 
ATOM   3351  C  CG2 . THR D  1 3   ? 98.960  -17.187 6.831   1.00 25.48 ? 2   THR G CG2 1 
ATOM   3352  N  N   . LYS D  1 4   ? 99.953  -14.711 9.607   1.00 12.67 ? 3   LYS G N   1 
ATOM   3353  C  CA  . LYS D  1 4   ? 99.549  -14.881 10.975  1.00 6.68  ? 3   LYS G CA  1 
ATOM   3354  C  C   . LYS D  1 4   ? 100.272 -13.841 11.808  1.00 5.13  ? 3   LYS G C   1 
ATOM   3355  O  O   . LYS D  1 4   ? 101.452 -13.583 11.573  1.00 3.24  ? 3   LYS G O   1 
ATOM   3356  C  CB  . LYS D  1 4   ? 99.947  -16.260 11.442  1.00 5.55  ? 3   LYS G CB  1 
ATOM   3357  C  CG  . LYS D  1 4   ? 99.219  -17.375 10.730  1.00 11.04 ? 3   LYS G CG  1 
ATOM   3358  C  CD  . LYS D  1 4   ? 99.467  -18.769 11.285  1.00 14.26 ? 3   LYS G CD  1 
ATOM   3359  C  CE  . LYS D  1 4   ? 99.217  -18.880 12.792  1.00 19.48 ? 3   LYS G CE  1 
ATOM   3360  N  NZ  . LYS D  1 4   ? 97.841  -18.614 13.205  1.00 22.86 ? 3   LYS G NZ  1 
ATOM   3361  N  N   . ALA D  1 5   ? 99.609  -13.287 12.815  1.00 2.67  ? 4   ALA G N   1 
ATOM   3362  C  CA  . ALA D  1 5   ? 100.233 -12.386 13.734  1.00 2.00  ? 4   ALA G CA  1 
ATOM   3363  C  C   . ALA D  1 5   ? 99.732  -12.753 15.125  1.00 2.31  ? 4   ALA G C   1 
ATOM   3364  O  O   . ALA D  1 5   ? 98.857  -13.594 15.318  1.00 2.00  ? 4   ALA G O   1 
ATOM   3365  C  CB  . ALA D  1 5   ? 99.851  -10.934 13.437  1.00 2.00  ? 4   ALA G CB  1 
ATOM   3366  N  N   . VAL D  1 6   ? 100.343 -12.152 16.119  1.00 2.00  ? 5   VAL G N   1 
ATOM   3367  C  CA  . VAL D  1 6   ? 99.920  -12.311 17.458  1.00 2.80  ? 5   VAL G CA  1 
ATOM   3368  C  C   . VAL D  1 6   ? 100.295 -11.043 18.206  1.00 2.00  ? 5   VAL G C   1 
ATOM   3369  O  O   . VAL D  1 6   ? 101.127 -10.262 17.776  1.00 2.00  ? 5   VAL G O   1 
ATOM   3370  C  CB  . VAL D  1 6   ? 100.562 -13.598 18.045  1.00 2.00  ? 5   VAL G CB  1 
ATOM   3371  C  CG1 . VAL D  1 6   ? 102.044 -13.537 18.071  1.00 2.00  ? 5   VAL G CG1 1 
ATOM   3372  C  CG2 . VAL D  1 6   ? 99.976  -13.813 19.419  1.00 2.00  ? 5   VAL G CG2 1 
ATOM   3373  N  N   . ALA D  1 7   ? 99.540  -10.784 19.254  1.00 2.00  ? 6   ALA G N   1 
ATOM   3374  C  CA  . ALA D  1 7   ? 99.806  -9.683  20.089  1.00 2.24  ? 6   ALA G CA  1 
ATOM   3375  C  C   . ALA D  1 7   ? 99.483  -10.198 21.453  1.00 3.66  ? 6   ALA G C   1 
ATOM   3376  O  O   . ALA D  1 7   ? 98.358  -10.679 21.656  1.00 4.14  ? 6   ALA G O   1 
ATOM   3377  C  CB  . ALA D  1 7   ? 98.880  -8.550  19.777  1.00 2.00  ? 6   ALA G CB  1 
ATOM   3378  N  N   . VAL D  1 8   ? 100.450 -10.147 22.374  1.00 3.69  ? 7   VAL G N   1 
ATOM   3379  C  CA  . VAL D  1 8   ? 100.131 -10.402 23.782  1.00 3.89  ? 7   VAL G CA  1 
ATOM   3380  C  C   . VAL D  1 8   ? 99.844  -9.057  24.498  1.00 5.39  ? 7   VAL G C   1 
ATOM   3381  O  O   . VAL D  1 8   ? 100.694 -8.165  24.476  1.00 6.22  ? 7   VAL G O   1 
ATOM   3382  C  CB  . VAL D  1 8   ? 101.302 -11.193 24.432  1.00 2.00  ? 7   VAL G CB  1 
ATOM   3383  C  CG1 . VAL D  1 8   ? 102.565 -10.686 23.969  1.00 2.84  ? 7   VAL G CG1 1 
ATOM   3384  C  CG2 . VAL D  1 8   ? 101.321 -11.042 25.935  1.00 2.00  ? 7   VAL G CG2 1 
ATOM   3385  N  N   . LEU D  1 9   ? 98.665  -8.842  25.102  1.00 4.80  ? 8   LEU G N   1 
ATOM   3386  C  CA  . LEU D  1 9   ? 98.281  -7.582  25.741  1.00 2.83  ? 8   LEU G CA  1 
ATOM   3387  C  C   . LEU D  1 9   ? 98.649  -7.647  27.195  1.00 2.00  ? 8   LEU G C   1 
ATOM   3388  O  O   . LEU D  1 9   ? 98.448  -8.648  27.856  1.00 2.00  ? 8   LEU G O   1 
ATOM   3389  C  CB  . LEU D  1 9   ? 96.773  -7.322  25.668  1.00 2.00  ? 8   LEU G CB  1 
ATOM   3390  C  CG  . LEU D  1 9   ? 96.093  -7.641  24.332  1.00 2.00  ? 8   LEU G CG  1 
ATOM   3391  C  CD1 . LEU D  1 9   ? 94.629  -7.273  24.338  1.00 2.00  ? 8   LEU G CD1 1 
ATOM   3392  C  CD2 . LEU D  1 9   ? 96.824  -6.904  23.264  1.00 2.00  ? 8   LEU G CD2 1 
ATOM   3393  N  N   . LYS D  1 10  ? 99.207  -6.600  27.721  1.00 3.52  ? 9   LYS G N   1 
ATOM   3394  C  CA  . LYS D  1 10  ? 99.596  -6.510  29.113  1.00 6.77  ? 9   LYS G CA  1 
ATOM   3395  C  C   . LYS D  1 10  ? 99.283  -5.067  29.535  1.00 6.20  ? 9   LYS G C   1 
ATOM   3396  O  O   . LYS D  1 10  ? 99.132  -4.223  28.653  1.00 5.60  ? 9   LYS G O   1 
ATOM   3397  C  CB  . LYS D  1 10  ? 101.101 -6.772  29.274  1.00 10.47 ? 9   LYS G CB  1 
ATOM   3398  C  CG  . LYS D  1 10  ? 101.780 -8.098  28.888  1.00 17.18 ? 9   LYS G CG  1 
ATOM   3399  C  CD  . LYS D  1 10  ? 101.388 -9.338  29.730  1.00 22.96 ? 9   LYS G CD  1 
ATOM   3400  C  CE  . LYS D  1 10  ? 102.433 -10.467 29.538  1.00 26.12 ? 9   LYS G CE  1 
ATOM   3401  N  NZ  . LYS D  1 10  ? 101.918 -11.791 29.908  1.00 28.83 ? 9   LYS G NZ  1 
ATOM   3402  N  N   . GLY D  1 11  ? 99.110  -4.696  30.800  1.00 5.90  ? 10  GLY G N   1 
ATOM   3403  C  CA  . GLY D  1 11  ? 98.859  -3.303  31.187  1.00 9.59  ? 10  GLY G CA  1 
ATOM   3404  C  C   . GLY D  1 11  ? 99.435  -3.128  32.577  1.00 11.75 ? 10  GLY G C   1 
ATOM   3405  O  O   . GLY D  1 11  ? 100.347 -3.867  32.936  1.00 13.74 ? 10  GLY G O   1 
ATOM   3406  N  N   . ASP D  1 12  ? 99.013  -2.219  33.431  1.00 14.54 ? 11  ASP G N   1 
ATOM   3407  C  CA  . ASP D  1 12  ? 99.488  -2.191  34.847  1.00 16.28 ? 11  ASP G CA  1 
ATOM   3408  C  C   . ASP D  1 12  ? 98.326  -2.597  35.734  1.00 14.60 ? 11  ASP G C   1 
ATOM   3409  O  O   . ASP D  1 12  ? 98.161  -2.084  36.842  1.00 16.21 ? 11  ASP G O   1 
ATOM   3410  C  CB  . ASP D  1 12  ? 99.879  -0.813  35.379  1.00 19.28 ? 11  ASP G CB  1 
ATOM   3411  C  CG  . ASP D  1 12  ? 100.737 -0.034  34.425  1.00 22.96 ? 11  ASP G CG  1 
ATOM   3412  O  OD1 . ASP D  1 12  ? 101.814 -0.547  34.049  1.00 23.87 ? 11  ASP G OD1 1 
ATOM   3413  O  OD2 . ASP D  1 12  ? 100.282 1.070   34.086  1.00 24.90 ? 11  ASP G OD2 1 
ATOM   3414  N  N   . GLY D  1 13  ? 97.465  -3.471  35.225  1.00 10.35 ? 12  GLY G N   1 
ATOM   3415  C  CA  . GLY D  1 13  ? 96.260  -3.810  35.932  1.00 5.33  ? 12  GLY G CA  1 
ATOM   3416  C  C   . GLY D  1 13  ? 96.125  -5.288  35.766  1.00 3.45  ? 12  GLY G C   1 
ATOM   3417  O  O   . GLY D  1 13  ? 97.095  -5.923  35.348  1.00 2.45  ? 12  GLY G O   1 
ATOM   3418  N  N   . PRO D  1 14  ? 94.950  -5.866  35.980  1.00 2.69  ? 13  PRO G N   1 
ATOM   3419  C  CA  . PRO D  1 14  ? 94.750  -7.290  35.826  1.00 3.82  ? 13  PRO G CA  1 
ATOM   3420  C  C   . PRO D  1 14  ? 94.512  -7.774  34.389  1.00 2.44  ? 13  PRO G C   1 
ATOM   3421  O  O   . PRO D  1 14  ? 94.488  -8.971  34.148  1.00 2.00  ? 13  PRO G O   1 
ATOM   3422  C  CB  . PRO D  1 14  ? 93.597  -7.539  36.795  1.00 3.74  ? 13  PRO G CB  1 
ATOM   3423  C  CG  . PRO D  1 14  ? 92.730  -6.287  36.698  1.00 2.00  ? 13  PRO G CG  1 
ATOM   3424  C  CD  . PRO D  1 14  ? 93.734  -5.189  36.401  1.00 2.00  ? 13  PRO G CD  1 
ATOM   3425  N  N   . VAL D  1 15  ? 94.382  -6.903  33.395  1.00 2.00  ? 14  VAL G N   1 
ATOM   3426  C  CA  . VAL D  1 15  ? 93.923  -7.342  32.100  1.00 2.00  ? 14  VAL G CA  1 
ATOM   3427  C  C   . VAL D  1 15  ? 95.068  -7.944  31.336  1.00 2.00  ? 14  VAL G C   1 
ATOM   3428  O  O   . VAL D  1 15  ? 96.148  -7.358  31.293  1.00 3.28  ? 14  VAL G O   1 
ATOM   3429  C  CB  . VAL D  1 15  ? 93.317  -6.131  31.377  1.00 2.00  ? 14  VAL G CB  1 
ATOM   3430  C  CG1 . VAL D  1 15  ? 92.763  -6.487  30.000  1.00 2.00  ? 14  VAL G CG1 1 
ATOM   3431  C  CG2 . VAL D  1 15  ? 92.160  -5.642  32.169  1.00 2.00  ? 14  VAL G CG2 1 
ATOM   3432  N  N   . GLN D  1 16  ? 94.875  -9.120  30.775  1.00 2.00  ? 15  GLN G N   1 
ATOM   3433  C  CA  . GLN D  1 16  ? 95.886  -9.685  29.934  1.00 2.64  ? 15  GLN G CA  1 
ATOM   3434  C  C   . GLN D  1 16  ? 95.355  -10.819 29.084  1.00 3.62  ? 15  GLN G C   1 
ATOM   3435  O  O   . GLN D  1 16  ? 94.408  -11.508 29.480  1.00 2.97  ? 15  GLN G O   1 
ATOM   3436  C  CB  . GLN D  1 16  ? 97.043  -10.177 30.757  1.00 6.43  ? 15  GLN G CB  1 
ATOM   3437  C  CG  . GLN D  1 16  ? 96.791  -11.300 31.727  1.00 16.81 ? 15  GLN G CG  1 
ATOM   3438  C  CD  . GLN D  1 16  ? 98.016  -11.481 32.610  1.00 21.60 ? 15  GLN G CD  1 
ATOM   3439  O  OE1 . GLN D  1 16  ? 99.098  -11.874 32.161  1.00 24.63 ? 15  GLN G OE1 1 
ATOM   3440  N  NE2 . GLN D  1 16  ? 97.904  -11.169 33.897  1.00 23.15 ? 15  GLN G NE2 1 
ATOM   3441  N  N   . GLY D  1 17  ? 95.907  -11.012 27.880  1.00 2.00  ? 16  GLY G N   1 
ATOM   3442  C  CA  . GLY D  1 17  ? 95.425  -12.050 27.001  1.00 2.08  ? 16  GLY G CA  1 
ATOM   3443  C  C   . GLY D  1 17  ? 96.299  -12.096 25.789  1.00 3.03  ? 16  GLY G C   1 
ATOM   3444  O  O   . GLY D  1 17  ? 97.184  -11.249 25.626  1.00 6.65  ? 16  GLY G O   1 
ATOM   3445  N  N   . ILE D  1 18  ? 96.046  -13.072 24.946  1.00 2.00  ? 17  ILE G N   1 
ATOM   3446  C  CA  . ILE D  1 18  ? 96.806  -13.295 23.720  1.00 2.75  ? 17  ILE G CA  1 
ATOM   3447  C  C   . ILE D  1 18  ? 95.807  -13.282 22.576  1.00 2.00  ? 17  ILE G C   1 
ATOM   3448  O  O   . ILE D  1 18  ? 94.736  -13.892 22.726  1.00 2.00  ? 17  ILE G O   1 
ATOM   3449  C  CB  . ILE D  1 18  ? 97.513  -14.620 23.889  1.00 3.71  ? 17  ILE G CB  1 
ATOM   3450  C  CG1 . ILE D  1 18  ? 98.790  -14.308 24.627  1.00 5.64  ? 17  ILE G CG1 1 
ATOM   3451  C  CG2 . ILE D  1 18  ? 97.762  -15.318 22.581  1.00 4.24  ? 17  ILE G CG2 1 
ATOM   3452  C  CD1 . ILE D  1 18  ? 99.336  -15.566 25.307  1.00 7.50  ? 17  ILE G CD1 1 
ATOM   3453  N  N   . ILE D  1 19  ? 96.087  -12.534 21.508  1.00 2.00  ? 18  ILE G N   1 
ATOM   3454  C  CA  . ILE D  1 19  ? 95.170  -12.403 20.382  1.00 2.41  ? 18  ILE G CA  1 
ATOM   3455  C  C   . ILE D  1 19  ? 95.920  -12.819 19.117  1.00 2.00  ? 18  ILE G C   1 
ATOM   3456  O  O   . ILE D  1 19  ? 97.070  -12.439 18.893  1.00 2.86  ? 18  ILE G O   1 
ATOM   3457  C  CB  . ILE D  1 19  ? 94.660  -10.916 20.343  1.00 2.00  ? 18  ILE G CB  1 
ATOM   3458  C  CG1 . ILE D  1 19  ? 93.652  -10.678 21.438  1.00 2.00  ? 18  ILE G CG1 1 
ATOM   3459  C  CG2 . ILE D  1 19  ? 94.003  -10.605 19.005  1.00 2.00  ? 18  ILE G CG2 1 
ATOM   3460  C  CD1 . ILE D  1 19  ? 92.346  -11.441 21.228  1.00 2.00  ? 18  ILE G CD1 1 
ATOM   3461  N  N   . ASN D  1 20  ? 95.271  -13.553 18.251  1.00 2.00  ? 19  ASN G N   1 
ATOM   3462  C  CA  . ASN D  1 20  ? 95.894  -14.099 17.081  1.00 2.00  ? 19  ASN G CA  1 
ATOM   3463  C  C   . ASN D  1 20  ? 95.179  -13.478 15.925  1.00 2.00  ? 19  ASN G C   1 
ATOM   3464  O  O   . ASN D  1 20  ? 93.998  -13.162 16.029  1.00 2.00  ? 19  ASN G O   1 
ATOM   3465  C  CB  . ASN D  1 20  ? 95.716  -15.613 17.048  1.00 2.00  ? 19  ASN G CB  1 
ATOM   3466  C  CG  . ASN D  1 20  ? 96.326  -16.343 18.243  1.00 2.00  ? 19  ASN G CG  1 
ATOM   3467  O  OD1 . ASN D  1 20  ? 95.670  -16.662 19.238  1.00 2.00  ? 19  ASN G OD1 1 
ATOM   3468  N  ND2 . ASN D  1 20  ? 97.605  -16.639 18.229  1.00 2.00  ? 19  ASN G ND2 1 
ATOM   3469  N  N   . PHE D  1 21  ? 95.877  -13.271 14.828  1.00 2.00  ? 20  PHE G N   1 
ATOM   3470  C  CA  . PHE D  1 21  ? 95.299  -12.739 13.613  1.00 2.47  ? 20  PHE G CA  1 
ATOM   3471  C  C   . PHE D  1 21  ? 95.687  -13.663 12.485  1.00 2.66  ? 20  PHE G C   1 
ATOM   3472  O  O   . PHE D  1 21  ? 96.838  -14.115 12.443  1.00 4.84  ? 20  PHE G O   1 
ATOM   3473  C  CB  . PHE D  1 21  ? 95.841  -11.384 13.262  1.00 2.00  ? 20  PHE G CB  1 
ATOM   3474  C  CG  . PHE D  1 21  ? 95.488  -10.335 14.277  1.00 2.00  ? 20  PHE G CG  1 
ATOM   3475  C  CD1 . PHE D  1 21  ? 96.307  -10.109 15.366  1.00 2.03  ? 20  PHE G CD1 1 
ATOM   3476  C  CD2 . PHE D  1 21  ? 94.378  -9.562  14.081  1.00 2.00  ? 20  PHE G CD2 1 
ATOM   3477  C  CE1 . PHE D  1 21  ? 96.029  -9.097  16.277  1.00 2.00  ? 20  PHE G CE1 1 
ATOM   3478  C  CE2 . PHE D  1 21  ? 94.106  -8.554  14.990  1.00 4.28  ? 20  PHE G CE2 1 
ATOM   3479  C  CZ  . PHE D  1 21  ? 94.924  -8.316  16.085  1.00 2.00  ? 20  PHE G CZ  1 
ATOM   3480  N  N   . GLU D  1 22  ? 94.808  -13.929 11.534  1.00 2.69  ? 21  GLU G N   1 
ATOM   3481  C  CA  . GLU D  1 22  ? 95.130  -14.841 10.474  1.00 2.42  ? 21  GLU G CA  1 
ATOM   3482  C  C   . GLU D  1 22  ? 94.377  -14.482 9.207   1.00 2.00  ? 21  GLU G C   1 
ATOM   3483  O  O   . GLU D  1 22  ? 93.166  -14.303 9.186   1.00 2.00  ? 21  GLU G O   1 
ATOM   3484  C  CB  . GLU D  1 22  ? 94.807  -16.234 10.959  1.00 2.00  ? 21  GLU G CB  1 
ATOM   3485  C  CG  . GLU D  1 22  ? 95.095  -17.229 9.853   1.00 10.72 ? 21  GLU G CG  1 
ATOM   3486  C  CD  . GLU D  1 22  ? 94.742  -18.683 10.137  1.00 13.45 ? 21  GLU G CD  1 
ATOM   3487  O  OE1 . GLU D  1 22  ? 93.744  -18.946 10.812  1.00 14.59 ? 21  GLU G OE1 1 
ATOM   3488  O  OE2 . GLU D  1 22  ? 95.472  -19.553 9.654   1.00 18.20 ? 21  GLU G OE2 1 
ATOM   3489  N  N   . GLN D  1 23  ? 95.160  -14.388 8.143   1.00 4.40  ? 22  GLN G N   1 
ATOM   3490  C  CA  . GLN D  1 23  ? 94.786  -13.946 6.831   1.00 6.51  ? 22  GLN G CA  1 
ATOM   3491  C  C   . GLN D  1 23  ? 95.361  -14.897 5.796   1.00 10.16 ? 22  GLN G C   1 
ATOM   3492  O  O   . GLN D  1 23  ? 96.570  -14.947 5.568   1.00 10.26 ? 22  GLN G O   1 
ATOM   3493  C  CB  . GLN D  1 23  ? 95.344  -12.552 6.643   1.00 5.94  ? 22  GLN G CB  1 
ATOM   3494  C  CG  . GLN D  1 23  ? 94.956  -12.008 5.306   1.00 3.05  ? 22  GLN G CG  1 
ATOM   3495  C  CD  . GLN D  1 23  ? 95.251  -10.553 5.165   1.00 4.72  ? 22  GLN G CD  1 
ATOM   3496  O  OE1 . GLN D  1 23  ? 96.332  -10.046 5.477   1.00 7.67  ? 22  GLN G OE1 1 
ATOM   3497  N  NE2 . GLN D  1 23  ? 94.263  -9.823  4.705   1.00 3.08  ? 22  GLN G NE2 1 
ATOM   3498  N  N   . LYS D  1 24  ? 94.518  -15.633 5.099   1.00 14.56 ? 23  LYS G N   1 
ATOM   3499  C  CA  . LYS D  1 24  ? 95.073  -16.605 4.193   1.00 19.04 ? 23  LYS G CA  1 
ATOM   3500  C  C   . LYS D  1 24  ? 95.197  -16.092 2.775   1.00 21.36 ? 23  LYS G C   1 
ATOM   3501  O  O   . LYS D  1 24  ? 95.970  -16.644 1.989   1.00 23.40 ? 23  LYS G O   1 
ATOM   3502  C  CB  . LYS D  1 24  ? 94.245  -17.871 4.153   1.00 23.90 ? 23  LYS G CB  1 
ATOM   3503  C  CG  . LYS D  1 24  ? 93.038  -18.054 5.071   1.00 28.14 ? 23  LYS G CG  1 
ATOM   3504  C  CD  . LYS D  1 24  ? 93.431  -18.517 6.462   1.00 33.01 ? 23  LYS G CD  1 
ATOM   3505  C  CE  . LYS D  1 24  ? 92.160  -18.893 7.242   1.00 38.31 ? 23  LYS G CE  1 
ATOM   3506  N  NZ  . LYS D  1 24  ? 91.465  -20.019 6.613   1.00 40.81 ? 23  LYS G NZ  1 
ATOM   3507  N  N   . GLU D  1 25  ? 94.498  -15.040 2.379   1.00 22.14 ? 24  GLU G N   1 
ATOM   3508  C  CA  . GLU D  1 25  ? 94.622  -14.557 1.016   1.00 23.29 ? 24  GLU G CA  1 
ATOM   3509  C  C   . GLU D  1 25  ? 95.053  -13.117 1.268   1.00 24.48 ? 24  GLU G C   1 
ATOM   3510  O  O   . GLU D  1 25  ? 94.507  -12.496 2.173   1.00 24.54 ? 24  GLU G O   1 
ATOM   3511  C  CB  . GLU D  1 25  ? 93.251  -14.703 0.385   1.00 24.90 ? 24  GLU G CB  1 
ATOM   3512  C  CG  . GLU D  1 25  ? 93.209  -15.358 -0.987  1.00 32.72 ? 24  GLU G CG  1 
ATOM   3513  C  CD  . GLU D  1 25  ? 93.236  -14.396 -2.189  1.00 38.61 ? 24  GLU G CD  1 
ATOM   3514  O  OE1 . GLU D  1 25  ? 94.341  -13.988 -2.615  1.00 39.77 ? 24  GLU G OE1 1 
ATOM   3515  O  OE2 . GLU D  1 25  ? 92.142  -14.073 -2.694  1.00 38.07 ? 24  GLU G OE2 1 
ATOM   3516  N  N   . SER D  1 26  ? 95.984  -12.488 0.567   1.00 26.37 ? 25  SER G N   1 
ATOM   3517  C  CA  . SER D  1 26  ? 96.462  -11.145 0.873   1.00 27.54 ? 25  SER G CA  1 
ATOM   3518  C  C   . SER D  1 26  ? 95.425  -10.027 0.700   1.00 28.70 ? 25  SER G C   1 
ATOM   3519  O  O   . SER D  1 26  ? 95.646  -8.854  1.023   1.00 30.05 ? 25  SER G O   1 
ATOM   3520  C  CB  . SER D  1 26  ? 97.690  -10.862 -0.014  1.00 28.28 ? 25  SER G CB  1 
ATOM   3521  O  OG  . SER D  1 26  ? 97.416  -11.102 -1.405  1.00 27.40 ? 25  SER G OG  1 
ATOM   3522  N  N   . ASN D  1 27  ? 94.283  -10.337 0.120   1.00 28.05 ? 26  ASN G N   1 
ATOM   3523  C  CA  . ASN D  1 27  ? 93.218  -9.368  -0.073  1.00 29.62 ? 26  ASN G CA  1 
ATOM   3524  C  C   . ASN D  1 27  ? 91.988  -10.198 0.285   1.00 29.73 ? 26  ASN G C   1 
ATOM   3525  O  O   . ASN D  1 27  ? 91.095  -10.558 -0.498  1.00 30.85 ? 26  ASN G O   1 
ATOM   3526  C  CB  . ASN D  1 27  ? 93.226  -8.904  -1.541  1.00 32.26 ? 26  ASN G CB  1 
ATOM   3527  C  CG  . ASN D  1 27  ? 93.393  -10.051 -2.541  1.00 35.30 ? 26  ASN G CG  1 
ATOM   3528  O  OD1 . ASN D  1 27  ? 92.839  -11.145 -2.382  1.00 36.66 ? 26  ASN G OD1 1 
ATOM   3529  N  ND2 . ASN D  1 27  ? 94.220  -9.881  -3.572  1.00 33.77 ? 26  ASN G ND2 1 
ATOM   3530  N  N   . GLY D  1 28  ? 92.014  -10.538 1.575   1.00 26.91 ? 27  GLY G N   1 
ATOM   3531  C  CA  . GLY D  1 28  ? 91.020  -11.410 2.170   1.00 21.76 ? 27  GLY G CA  1 
ATOM   3532  C  C   . GLY D  1 28  ? 90.823  -10.957 3.606   1.00 19.28 ? 27  GLY G C   1 
ATOM   3533  O  O   . GLY D  1 28  ? 91.566  -10.082 4.080   1.00 19.60 ? 27  GLY G O   1 
ATOM   3534  N  N   . PRO D  1 29  ? 89.817  -11.493 4.303   1.00 15.88 ? 28  PRO G N   1 
ATOM   3535  C  CA  . PRO D  1 29  ? 89.490  -11.078 5.652   1.00 10.56 ? 28  PRO G CA  1 
ATOM   3536  C  C   . PRO D  1 29  ? 90.449  -11.718 6.629   1.00 9.69  ? 28  PRO G C   1 
ATOM   3537  O  O   . PRO D  1 29  ? 91.021  -12.784 6.364   1.00 11.66 ? 28  PRO G O   1 
ATOM   3538  C  CB  . PRO D  1 29  ? 88.046  -11.497 5.763   1.00 10.73 ? 28  PRO G CB  1 
ATOM   3539  C  CG  . PRO D  1 29  ? 87.920  -12.750 4.929   1.00 10.52 ? 28  PRO G CG  1 
ATOM   3540  C  CD  . PRO D  1 29  ? 88.812  -12.408 3.739   1.00 12.45 ? 28  PRO G CD  1 
ATOM   3541  N  N   . VAL D  1 30  ? 90.604  -11.064 7.761   1.00 7.77  ? 29  VAL G N   1 
ATOM   3542  C  CA  . VAL D  1 30  ? 91.526  -11.415 8.824   1.00 5.17  ? 29  VAL G CA  1 
ATOM   3543  C  C   . VAL D  1 30  ? 90.699  -11.951 9.961   1.00 5.56  ? 29  VAL G C   1 
ATOM   3544  O  O   . VAL D  1 30  ? 89.844  -11.216 10.460  1.00 7.26  ? 29  VAL G O   1 
ATOM   3545  C  CB  . VAL D  1 30  ? 92.272  -10.127 9.223   1.00 3.36  ? 29  VAL G CB  1 
ATOM   3546  C  CG1 . VAL D  1 30  ? 93.115  -10.328 10.438  1.00 2.01  ? 29  VAL G CG1 1 
ATOM   3547  C  CG2 . VAL D  1 30  ? 93.121  -9.679  8.042   1.00 2.00  ? 29  VAL G CG2 1 
ATOM   3548  N  N   . LYS D  1 31  ? 90.845  -13.210 10.328  1.00 5.80  ? 30  LYS G N   1 
ATOM   3549  C  CA  . LYS D  1 31  ? 90.264  -13.767 11.550  1.00 5.28  ? 30  LYS G CA  1 
ATOM   3550  C  C   . LYS D  1 31  ? 91.049  -13.226 12.741  1.00 3.95  ? 30  LYS G C   1 
ATOM   3551  O  O   . LYS D  1 31  ? 92.261  -13.485 12.771  1.00 2.00  ? 30  LYS G O   1 
ATOM   3552  C  CB  . LYS D  1 31  ? 90.424  -15.263 11.637  1.00 9.65  ? 30  LYS G CB  1 
ATOM   3553  C  CG  . LYS D  1 31  ? 89.857  -16.072 10.498  1.00 16.44 ? 30  LYS G CG  1 
ATOM   3554  C  CD  . LYS D  1 31  ? 88.338  -16.011 10.604  1.00 23.92 ? 30  LYS G CD  1 
ATOM   3555  C  CE  . LYS D  1 31  ? 87.637  -17.096 9.783   1.00 26.73 ? 30  LYS G CE  1 
ATOM   3556  N  NZ  . LYS D  1 31  ? 86.222  -17.138 10.137  1.00 28.39 ? 30  LYS G NZ  1 
ATOM   3557  N  N   . VAL D  1 32  ? 90.502  -12.459 13.689  1.00 2.00  ? 31  VAL G N   1 
ATOM   3558  C  CA  . VAL D  1 32  ? 91.241  -12.127 14.901  1.00 2.00  ? 31  VAL G CA  1 
ATOM   3559  C  C   . VAL D  1 32  ? 90.557  -12.940 15.987  1.00 2.00  ? 31  VAL G C   1 
ATOM   3560  O  O   . VAL D  1 32  ? 89.336  -12.932 16.083  1.00 2.00  ? 31  VAL G O   1 
ATOM   3561  C  CB  . VAL D  1 32  ? 91.287  -10.503 15.241  1.00 2.26  ? 31  VAL G CB  1 
ATOM   3562  C  CG1 . VAL D  1 32  ? 90.404  -9.692  14.296  1.00 2.00  ? 31  VAL G CG1 1 
ATOM   3563  C  CG2 . VAL D  1 32  ? 90.921  -10.224 16.702  1.00 2.00  ? 31  VAL G CG2 1 
ATOM   3564  N  N   . TRP D  1 33  ? 91.236  -13.771 16.763  1.00 2.76  ? 32  TRP G N   1 
ATOM   3565  C  CA  . TRP D  1 33  ? 90.606  -14.469 17.877  1.00 2.00  ? 32  TRP G CA  1 
ATOM   3566  C  C   . TRP D  1 33  ? 91.577  -14.593 19.033  1.00 2.00  ? 32  TRP G C   1 
ATOM   3567  O  O   . TRP D  1 33  ? 92.777  -14.415 18.882  1.00 2.00  ? 32  TRP G O   1 
ATOM   3568  C  CB  . TRP D  1 33  ? 90.158  -15.857 17.442  1.00 5.37  ? 32  TRP G CB  1 
ATOM   3569  C  CG  . TRP D  1 33  ? 91.270  -16.850 17.192  1.00 7.15  ? 32  TRP G CG  1 
ATOM   3570  C  CD1 . TRP D  1 33  ? 91.617  -17.730 18.176  1.00 10.86 ? 32  TRP G CD1 1 
ATOM   3571  C  CD2 . TRP D  1 33  ? 92.058  -16.966 16.073  1.00 9.72  ? 32  TRP G CD2 1 
ATOM   3572  N  NE1 . TRP D  1 33  ? 92.638  -18.408 17.696  1.00 11.86 ? 32  TRP G NE1 1 
ATOM   3573  C  CE2 . TRP D  1 33  ? 92.923  -17.996 16.453  1.00 9.96  ? 32  TRP G CE2 1 
ATOM   3574  C  CE3 . TRP D  1 33  ? 92.168  -16.393 14.834  1.00 9.02  ? 32  TRP G CE3 1 
ATOM   3575  C  CZ2 . TRP D  1 33  ? 93.929  -18.480 15.643  1.00 10.27 ? 32  TRP G CZ2 1 
ATOM   3576  C  CZ3 . TRP D  1 33  ? 93.172  -16.877 14.027  1.00 12.35 ? 32  TRP G CZ3 1 
ATOM   3577  C  CH2 . TRP D  1 33  ? 94.040  -17.903 14.400  1.00 12.15 ? 32  TRP G CH2 1 
ATOM   3578  N  N   . GLY D  1 34  ? 91.152  -14.877 20.235  1.00 2.26  ? 33  GLY G N   1 
ATOM   3579  C  CA  . GLY D  1 34  ? 92.049  -15.061 21.366  1.00 2.00  ? 33  GLY G CA  1 
ATOM   3580  C  C   . GLY D  1 34  ? 91.233  -14.948 22.640  1.00 3.15  ? 33  GLY G C   1 
ATOM   3581  O  O   . GLY D  1 34  ? 89.996  -14.869 22.559  1.00 4.01  ? 33  GLY G O   1 
ATOM   3582  N  N   . SER D  1 35  ? 91.858  -14.880 23.808  1.00 4.07  ? 34  SER G N   1 
ATOM   3583  C  CA  . SER D  1 35  ? 91.156  -14.731 25.077  1.00 3.74  ? 34  SER G CA  1 
ATOM   3584  C  C   . SER D  1 35  ? 91.727  -13.488 25.679  1.00 3.79  ? 34  SER G C   1 
ATOM   3585  O  O   . SER D  1 35  ? 92.912  -13.225 25.426  1.00 5.24  ? 34  SER G O   1 
ATOM   3586  C  CB  . SER D  1 35  ? 91.467  -15.835 26.056  1.00 6.02  ? 34  SER G CB  1 
ATOM   3587  O  OG  . SER D  1 35  ? 90.249  -16.445 26.506  1.00 13.20 ? 34  SER G OG  1 
ATOM   3588  N  N   . ILE D  1 36  ? 90.973  -12.721 26.456  1.00 2.79  ? 35  ILE G N   1 
ATOM   3589  C  CA  . ILE D  1 36  ? 91.520  -11.589 27.184  1.00 2.00  ? 35  ILE G CA  1 
ATOM   3590  C  C   . ILE D  1 36  ? 90.962  -11.873 28.551  1.00 2.00  ? 35  ILE G C   1 
ATOM   3591  O  O   . ILE D  1 36  ? 89.835  -12.346 28.619  1.00 2.90  ? 35  ILE G O   1 
ATOM   3592  C  CB  . ILE D  1 36  ? 90.984  -10.266 26.684  1.00 2.00  ? 35  ILE G CB  1 
ATOM   3593  C  CG1 . ILE D  1 36  ? 91.228  -10.204 25.220  1.00 2.64  ? 35  ILE G CG1 1 
ATOM   3594  C  CG2 . ILE D  1 36  ? 91.710  -9.079  27.304  1.00 2.00  ? 35  ILE G CG2 1 
ATOM   3595  C  CD1 . ILE D  1 36  ? 90.628  -8.927  24.582  1.00 8.01  ? 35  ILE G CD1 1 
ATOM   3596  N  N   . LYS D  1 37  ? 91.639  -11.657 29.661  1.00 2.98  ? 36  LYS G N   1 
ATOM   3597  C  CA  . LYS D  1 37  ? 91.104  -11.971 30.970  1.00 3.25  ? 36  LYS G CA  1 
ATOM   3598  C  C   . LYS D  1 37  ? 91.256  -10.714 31.785  1.00 4.62  ? 36  LYS G C   1 
ATOM   3599  O  O   . LYS D  1 37  ? 92.002  -9.804  31.360  1.00 4.56  ? 36  LYS G O   1 
ATOM   3600  C  CB  . LYS D  1 37  ? 91.871  -13.125 31.646  1.00 2.00  ? 36  LYS G CB  1 
ATOM   3601  C  CG  . LYS D  1 37  ? 93.144  -12.682 32.371  1.00 12.31 ? 36  LYS G CG  1 
ATOM   3602  C  CD  . LYS D  1 37  ? 93.658  -13.634 33.465  1.00 16.65 ? 36  LYS G CD  1 
ATOM   3603  C  CE  . LYS D  1 37  ? 94.825  -13.040 34.287  1.00 20.17 ? 36  LYS G CE  1 
ATOM   3604  N  NZ  . LYS D  1 37  ? 94.452  -11.831 35.009  1.00 20.71 ? 36  LYS G NZ  1 
ATOM   3605  N  N   . GLY D  1 38  ? 90.529  -10.736 32.934  1.00 5.96  ? 37  GLY G N   1 
ATOM   3606  C  CA  . GLY D  1 38  ? 90.476  -9.678  33.927  1.00 2.00  ? 37  GLY G CA  1 
ATOM   3607  C  C   . GLY D  1 38  ? 89.660  -8.486  33.522  1.00 2.00  ? 37  GLY G C   1 
ATOM   3608  O  O   . GLY D  1 38  ? 89.939  -7.390  34.003  1.00 2.00  ? 37  GLY G O   1 
ATOM   3609  N  N   . LEU D  1 39  ? 88.643  -8.577  32.657  1.00 4.16  ? 38  LEU G N   1 
ATOM   3610  C  CA  . LEU D  1 39  ? 87.875  -7.396  32.254  1.00 2.00  ? 38  LEU G CA  1 
ATOM   3611  C  C   . LEU D  1 39  ? 86.605  -7.371  33.047  1.00 2.00  ? 38  LEU G C   1 
ATOM   3612  O  O   . LEU D  1 39  ? 86.023  -8.403  33.380  1.00 2.00  ? 38  LEU G O   1 
ATOM   3613  C  CB  . LEU D  1 39  ? 87.381  -7.393  30.844  1.00 2.00  ? 38  LEU G CB  1 
ATOM   3614  C  CG  . LEU D  1 39  ? 88.195  -7.262  29.587  1.00 2.90  ? 38  LEU G CG  1 
ATOM   3615  C  CD1 . LEU D  1 39  ? 89.101  -6.049  29.544  1.00 2.00  ? 38  LEU G CD1 1 
ATOM   3616  C  CD2 . LEU D  1 39  ? 88.962  -8.502  29.506  1.00 8.03  ? 38  LEU G CD2 1 
ATOM   3617  N  N   . THR D  1 40  ? 86.071  -6.203  33.291  1.00 2.34  ? 39  THR G N   1 
ATOM   3618  C  CA  . THR D  1 40  ? 84.787  -6.128  33.934  1.00 2.95  ? 39  THR G CA  1 
ATOM   3619  C  C   . THR D  1 40  ? 83.793  -6.614  32.866  1.00 5.55  ? 39  THR G C   1 
ATOM   3620  O  O   . THR D  1 40  ? 84.053  -6.443  31.665  1.00 5.48  ? 39  THR G O   1 
ATOM   3621  C  CB  . THR D  1 40  ? 84.522  -4.656  34.371  1.00 2.99  ? 39  THR G CB  1 
ATOM   3622  O  OG1 . THR D  1 40  ? 84.542  -3.817  33.218  1.00 2.46  ? 39  THR G OG1 1 
ATOM   3623  C  CG2 . THR D  1 40  ? 85.578  -4.167  35.336  1.00 2.00  ? 39  THR G CG2 1 
ATOM   3624  N  N   . GLU D  1 41  ? 82.679  -7.232  33.272  1.00 7.90  ? 40  GLU G N   1 
ATOM   3625  C  CA  . GLU D  1 41  ? 81.663  -7.799  32.408  1.00 6.98  ? 40  GLU G CA  1 
ATOM   3626  C  C   . GLU D  1 41  ? 81.043  -6.751  31.518  1.00 5.62  ? 40  GLU G C   1 
ATOM   3627  O  O   . GLU D  1 41  ? 80.703  -5.646  31.931  1.00 4.32  ? 40  GLU G O   1 
ATOM   3628  C  CB  . GLU D  1 41  ? 80.637  -8.434  33.303  1.00 10.76 ? 40  GLU G CB  1 
ATOM   3629  C  CG  . GLU D  1 41  ? 79.425  -9.043  32.642  1.00 15.81 ? 40  GLU G CG  1 
ATOM   3630  C  CD  . GLU D  1 41  ? 78.443  -9.692  33.618  1.00 19.65 ? 40  GLU G CD  1 
ATOM   3631  O  OE1 . GLU D  1 41  ? 78.213  -9.143  34.709  1.00 21.33 ? 40  GLU G OE1 1 
ATOM   3632  O  OE2 . GLU D  1 41  ? 77.905  -10.747 33.263  1.00 19.12 ? 40  GLU G OE2 1 
ATOM   3633  N  N   . GLY D  1 42  ? 80.947  -7.128  30.250  1.00 6.40  ? 41  GLY G N   1 
ATOM   3634  C  CA  . GLY D  1 42  ? 80.323  -6.314  29.245  1.00 3.68  ? 41  GLY G CA  1 
ATOM   3635  C  C   . GLY D  1 42  ? 81.280  -5.986  28.144  1.00 4.28  ? 41  GLY G C   1 
ATOM   3636  O  O   . GLY D  1 42  ? 82.304  -6.630  27.909  1.00 7.55  ? 41  GLY G O   1 
ATOM   3637  N  N   . LEU D  1 43  ? 80.925  -4.866  27.543  1.00 4.62  ? 42  LEU G N   1 
ATOM   3638  C  CA  . LEU D  1 43  ? 81.525  -4.351  26.335  1.00 2.42  ? 42  LEU G CA  1 
ATOM   3639  C  C   . LEU D  1 43  ? 82.721  -3.558  26.667  1.00 2.00  ? 42  LEU G C   1 
ATOM   3640  O  O   . LEU D  1 43  ? 82.672  -2.856  27.675  1.00 3.62  ? 42  LEU G O   1 
ATOM   3641  C  CB  . LEU D  1 43  ? 80.529  -3.492  25.610  1.00 2.00  ? 42  LEU G CB  1 
ATOM   3642  C  CG  . LEU D  1 43  ? 79.617  -4.102  24.556  1.00 2.00  ? 42  LEU G CG  1 
ATOM   3643  C  CD1 . LEU D  1 43  ? 79.517  -5.597  24.609  1.00 2.00  ? 42  LEU G CD1 1 
ATOM   3644  C  CD2 . LEU D  1 43  ? 78.280  -3.515  24.787  1.00 2.02  ? 42  LEU G CD2 1 
ATOM   3645  N  N   . HIS D  1 44  ? 83.724  -3.739  25.801  1.00 2.11  ? 43  HIS G N   1 
ATOM   3646  C  CA  . HIS D  1 44  ? 85.041  -3.121  25.822  1.00 2.00  ? 43  HIS G CA  1 
ATOM   3647  C  C   . HIS D  1 44  ? 85.548  -2.936  24.413  1.00 2.00  ? 43  HIS G C   1 
ATOM   3648  O  O   . HIS D  1 44  ? 85.721  -3.930  23.688  1.00 3.82  ? 43  HIS G O   1 
ATOM   3649  C  CB  . HIS D  1 44  ? 86.088  -3.980  26.538  1.00 2.00  ? 43  HIS G CB  1 
ATOM   3650  C  CG  . HIS D  1 44  ? 85.816  -4.097  28.038  1.00 4.68  ? 43  HIS G CG  1 
ATOM   3651  N  ND1 . HIS D  1 44  ? 86.171  -3.259  29.009  1.00 2.09  ? 43  HIS G ND1 1 
ATOM   3652  C  CD2 . HIS D  1 44  ? 85.059  -5.102  28.593  1.00 2.00  ? 43  HIS G CD2 1 
ATOM   3653  C  CE1 . HIS D  1 44  ? 85.658  -3.692  30.116  1.00 2.00  ? 43  HIS G CE1 1 
ATOM   3654  N  NE2 . HIS D  1 44  ? 85.004  -4.784  29.837  1.00 3.67  ? 43  HIS G NE2 1 
ATOM   3655  N  N   . GLY D  1 45  ? 85.783  -1.679  24.039  1.00 2.00  ? 44  GLY G N   1 
ATOM   3656  C  CA  . GLY D  1 45  ? 86.364  -1.265  22.765  1.00 2.00  ? 44  GLY G CA  1 
ATOM   3657  C  C   . GLY D  1 45  ? 87.648  -2.006  22.430  1.00 2.00  ? 44  GLY G C   1 
ATOM   3658  O  O   . GLY D  1 45  ? 88.579  -2.017  23.230  1.00 4.71  ? 44  GLY G O   1 
ATOM   3659  N  N   . PHE D  1 46  ? 87.696  -2.680  21.303  1.00 2.00  ? 45  PHE G N   1 
ATOM   3660  C  CA  . PHE D  1 46  ? 88.840  -3.422  20.849  1.00 2.00  ? 45  PHE G CA  1 
ATOM   3661  C  C   . PHE D  1 46  ? 89.391  -2.658  19.630  1.00 2.77  ? 45  PHE G C   1 
ATOM   3662  O  O   . PHE D  1 46  ? 88.666  -2.543  18.646  1.00 4.77  ? 45  PHE G O   1 
ATOM   3663  C  CB  . PHE D  1 46  ? 88.286  -4.781  20.536  1.00 2.00  ? 45  PHE G CB  1 
ATOM   3664  C  CG  . PHE D  1 46  ? 89.322  -5.867  20.426  1.00 2.00  ? 45  PHE G CG  1 
ATOM   3665  C  CD1 . PHE D  1 46  ? 90.195  -6.103  21.460  1.00 2.00  ? 45  PHE G CD1 1 
ATOM   3666  C  CD2 . PHE D  1 46  ? 89.369  -6.613  19.290  1.00 2.14  ? 45  PHE G CD2 1 
ATOM   3667  C  CE1 . PHE D  1 46  ? 91.130  -7.089  21.376  1.00 2.00  ? 45  PHE G CE1 1 
ATOM   3668  C  CE2 . PHE D  1 46  ? 90.312  -7.609  19.208  1.00 4.86  ? 45  PHE G CE2 1 
ATOM   3669  C  CZ  . PHE D  1 46  ? 91.184  -7.842  20.245  1.00 2.64  ? 45  PHE G CZ  1 
ATOM   3670  N  N   . HIS D  1 47  ? 90.575  -2.045  19.535  1.00 2.00  ? 46  HIS G N   1 
ATOM   3671  C  CA  . HIS D  1 47  ? 90.953  -1.226  18.392  1.00 2.00  ? 46  HIS G CA  1 
ATOM   3672  C  C   . HIS D  1 47  ? 92.388  -1.447  18.070  1.00 2.00  ? 46  HIS G C   1 
ATOM   3673  O  O   . HIS D  1 47  ? 93.130  -1.958  18.897  1.00 2.00  ? 46  HIS G O   1 
ATOM   3674  C  CB  . HIS D  1 47  ? 90.864  0.259   18.639  1.00 2.22  ? 46  HIS G CB  1 
ATOM   3675  C  CG  . HIS D  1 47  ? 89.570  0.776   19.220  1.00 2.00  ? 46  HIS G CG  1 
ATOM   3676  N  ND1 . HIS D  1 47  ? 89.443  1.662   20.214  1.00 2.00  ? 46  HIS G ND1 1 
ATOM   3677  C  CD2 . HIS D  1 47  ? 88.334  0.334   18.819  1.00 2.00  ? 46  HIS G CD2 1 
ATOM   3678  C  CE1 . HIS D  1 47  ? 88.133  1.733   20.410  1.00 3.53  ? 46  HIS G CE1 1 
ATOM   3679  N  NE2 . HIS D  1 47  ? 87.475  0.937   19.585  1.00 2.00  ? 46  HIS G NE2 1 
ATOM   3680  N  N   . VAL D  1 48  ? 92.844  -1.045  16.892  1.00 3.43  ? 47  VAL G N   1 
ATOM   3681  C  CA  . VAL D  1 48  ? 94.254  -1.127  16.505  1.00 2.31  ? 47  VAL G CA  1 
ATOM   3682  C  C   . VAL D  1 48  ? 94.597  0.355   16.487  1.00 2.00  ? 47  VAL G C   1 
ATOM   3683  O  O   . VAL D  1 48  ? 93.833  1.204   16.038  1.00 2.00  ? 47  VAL G O   1 
ATOM   3684  C  CB  . VAL D  1 48  ? 94.451  -1.716  15.134  1.00 2.00  ? 47  VAL G CB  1 
ATOM   3685  C  CG1 . VAL D  1 48  ? 95.883  -1.881  14.883  1.00 2.00  ? 47  VAL G CG1 1 
ATOM   3686  C  CG2 . VAL D  1 48  ? 93.919  -3.073  15.046  1.00 2.00  ? 47  VAL G CG2 1 
ATOM   3687  N  N   . HIS D  1 49  ? 95.684  0.710   17.120  1.00 2.00  ? 48  HIS G N   1 
ATOM   3688  C  CA  . HIS D  1 49  ? 96.112  2.083   17.284  1.00 2.00  ? 48  HIS G CA  1 
ATOM   3689  C  C   . HIS D  1 49  ? 97.392  2.173   16.475  1.00 2.00  ? 48  HIS G C   1 
ATOM   3690  O  O   . HIS D  1 49  ? 98.116  1.216   16.237  1.00 2.00  ? 48  HIS G O   1 
ATOM   3691  C  CB  . HIS D  1 49  ? 96.363  2.388   18.762  1.00 2.70  ? 48  HIS G CB  1 
ATOM   3692  C  CG  . HIS D  1 49  ? 95.136  2.616   19.644  1.00 2.00  ? 48  HIS G CG  1 
ATOM   3693  N  ND1 . HIS D  1 49  ? 94.957  3.643   20.405  1.00 2.00  ? 48  HIS G ND1 1 
ATOM   3694  C  CD2 . HIS D  1 49  ? 93.986  1.879   19.737  1.00 2.00  ? 48  HIS G CD2 1 
ATOM   3695  C  CE1 . HIS D  1 49  ? 93.740  3.555   20.913  1.00 2.00  ? 48  HIS G CE1 1 
ATOM   3696  N  NE2 . HIS D  1 49  ? 93.124  2.488   20.526  1.00 2.00  ? 48  HIS G NE2 1 
ATOM   3697  N  N   . GLU D  1 50  ? 97.712  3.356   16.071  1.00 2.00  ? 49  GLU G N   1 
ATOM   3698  C  CA  . GLU D  1 50  ? 98.718  3.586   15.089  1.00 2.00  ? 49  GLU G CA  1 
ATOM   3699  C  C   . GLU D  1 50  ? 100.099 3.091   15.354  1.00 2.62  ? 49  GLU G C   1 
ATOM   3700  O  O   . GLU D  1 50  ? 100.700 2.661   14.378  1.00 2.41  ? 49  GLU G O   1 
ATOM   3701  C  CB  . GLU D  1 50  ? 98.815  5.092   14.784  1.00 2.00  ? 49  GLU G CB  1 
ATOM   3702  C  CG  . GLU D  1 50  ? 99.005  5.199   13.292  1.00 5.81  ? 49  GLU G CG  1 
ATOM   3703  C  CD  . GLU D  1 50  ? 99.504  6.510   12.729  1.00 14.06 ? 49  GLU G CD  1 
ATOM   3704  O  OE1 . GLU D  1 50  ? 98.919  7.561   13.052  1.00 13.47 ? 49  GLU G OE1 1 
ATOM   3705  O  OE2 . GLU D  1 50  ? 100.476 6.457   11.941  1.00 16.34 ? 49  GLU G OE2 1 
ATOM   3706  N  N   . PHE D  1 51  ? 100.653 3.102   16.561  1.00 2.00  ? 50  PHE G N   1 
ATOM   3707  C  CA  . PHE D  1 51  ? 102.063 2.833   16.684  1.00 2.00  ? 50  PHE G CA  1 
ATOM   3708  C  C   . PHE D  1 51  ? 102.359 1.672   17.558  1.00 2.00  ? 50  PHE G C   1 
ATOM   3709  O  O   . PHE D  1 51  ? 101.665 1.448   18.535  1.00 2.00  ? 50  PHE G O   1 
ATOM   3710  C  CB  . PHE D  1 51  ? 102.804 3.981   17.281  1.00 2.52  ? 50  PHE G CB  1 
ATOM   3711  C  CG  . PHE D  1 51  ? 102.585 5.277   16.555  1.00 2.00  ? 50  PHE G CG  1 
ATOM   3712  C  CD1 . PHE D  1 51  ? 102.931 5.403   15.222  1.00 2.77  ? 50  PHE G CD1 1 
ATOM   3713  C  CD2 . PHE D  1 51  ? 102.055 6.324   17.249  1.00 2.00  ? 50  PHE G CD2 1 
ATOM   3714  C  CE1 . PHE D  1 51  ? 102.747 6.611   14.575  1.00 2.00  ? 50  PHE G CE1 1 
ATOM   3715  C  CE2 . PHE D  1 51  ? 101.875 7.525   16.598  1.00 2.93  ? 50  PHE G CE2 1 
ATOM   3716  C  CZ  . PHE D  1 51  ? 102.218 7.678   15.262  1.00 2.00  ? 50  PHE G CZ  1 
ATOM   3717  N  N   . GLY D  1 52  ? 103.416 0.944   17.233  1.00 2.00  ? 51  GLY G N   1 
ATOM   3718  C  CA  . GLY D  1 52  ? 103.899 -0.124  18.064  1.00 2.00  ? 51  GLY G CA  1 
ATOM   3719  C  C   . GLY D  1 52  ? 104.906 0.409   19.058  1.00 2.18  ? 51  GLY G C   1 
ATOM   3720  O  O   . GLY D  1 52  ? 105.885 -0.256  19.369  1.00 4.26  ? 51  GLY G O   1 
ATOM   3721  N  N   . ASP D  1 53  ? 104.686 1.599   19.576  1.00 2.91  ? 52  ASP G N   1 
ATOM   3722  C  CA  . ASP D  1 53  ? 105.557 2.291   20.504  1.00 4.21  ? 52  ASP G CA  1 
ATOM   3723  C  C   . ASP D  1 53  ? 104.920 2.083   21.859  1.00 4.18  ? 52  ASP G C   1 
ATOM   3724  O  O   . ASP D  1 53  ? 103.871 2.672   22.168  1.00 2.89  ? 52  ASP G O   1 
ATOM   3725  C  CB  . ASP D  1 53  ? 105.590 3.785   20.182  1.00 8.42  ? 52  ASP G CB  1 
ATOM   3726  C  CG  . ASP D  1 53  ? 106.507 4.685   21.013  1.00 11.74 ? 52  ASP G CG  1 
ATOM   3727  O  OD1 . ASP D  1 53  ? 106.773 4.412   22.181  1.00 11.99 ? 52  ASP G OD1 1 
ATOM   3728  O  OD2 . ASP D  1 53  ? 106.942 5.703   20.483  1.00 15.99 ? 52  ASP G OD2 1 
ATOM   3729  N  N   . ASN D  1 54  ? 105.540 1.228   22.662  1.00 3.43  ? 53  ASN G N   1 
ATOM   3730  C  CA  . ASN D  1 54  ? 104.987 1.005   23.958  1.00 4.04  ? 53  ASN G CA  1 
ATOM   3731  C  C   . ASN D  1 54  ? 105.918 1.516   25.044  1.00 4.91  ? 53  ASN G C   1 
ATOM   3732  O  O   . ASN D  1 54  ? 105.923 1.015   26.167  1.00 6.07  ? 53  ASN G O   1 
ATOM   3733  C  CB  . ASN D  1 54  ? 104.665 -0.510  24.029  1.00 8.11  ? 53  ASN G CB  1 
ATOM   3734  C  CG  . ASN D  1 54  ? 103.269 -0.859  23.388  1.00 12.51 ? 53  ASN G CG  1 
ATOM   3735  O  OD1 . ASN D  1 54  ? 102.915 -2.033  23.183  1.00 14.43 ? 53  ASN G OD1 1 
ATOM   3736  N  ND2 . ASN D  1 54  ? 102.353 0.031   22.988  1.00 9.81  ? 53  ASN G ND2 1 
ATOM   3737  N  N   . THR D  1 55  ? 106.660 2.594   24.803  1.00 4.72  ? 54  THR G N   1 
ATOM   3738  C  CA  . THR D  1 55  ? 107.663 2.994   25.767  1.00 5.85  ? 54  THR G CA  1 
ATOM   3739  C  C   . THR D  1 55  ? 107.016 3.632   26.965  1.00 6.89  ? 54  THR G C   1 
ATOM   3740  O  O   . THR D  1 55  ? 107.429 3.424   28.091  1.00 11.05 ? 54  THR G O   1 
ATOM   3741  C  CB  . THR D  1 55  ? 108.594 3.958   25.131  1.00 5.72  ? 54  THR G CB  1 
ATOM   3742  O  OG1 . THR D  1 55  ? 107.761 4.989   24.649  1.00 7.26  ? 54  THR G OG1 1 
ATOM   3743  C  CG2 . THR D  1 55  ? 109.430 3.338   24.042  1.00 7.09  ? 54  THR G CG2 1 
ATOM   3744  N  N   . ALA D  1 56  ? 106.012 4.469   26.725  1.00 7.24  ? 55  ALA G N   1 
ATOM   3745  C  CA  . ALA D  1 56  ? 105.186 5.063   27.775  1.00 3.79  ? 55  ALA G CA  1 
ATOM   3746  C  C   . ALA D  1 56  ? 103.983 4.163   28.031  1.00 5.20  ? 55  ALA G C   1 
ATOM   3747  O  O   . ALA D  1 56  ? 102.875 4.661   28.285  1.00 5.39  ? 55  ALA G O   1 
ATOM   3748  C  CB  . ALA D  1 56  ? 104.676 6.436   27.339  1.00 2.87  ? 55  ALA G CB  1 
ATOM   3749  N  N   . GLY D  1 57  ? 104.111 2.816   27.977  1.00 5.34  ? 56  GLY G N   1 
ATOM   3750  C  CA  . GLY D  1 57  ? 102.968 1.928   28.133  1.00 4.67  ? 56  GLY G CA  1 
ATOM   3751  C  C   . GLY D  1 57  ? 102.021 2.074   26.956  1.00 7.22  ? 56  GLY G C   1 
ATOM   3752  O  O   . GLY D  1 57  ? 102.422 2.532   25.873  1.00 8.70  ? 56  GLY G O   1 
ATOM   3753  N  N   . CYS D  1 58  ? 100.722 1.833   27.178  1.00 8.07  ? 57  CYS G N   1 
ATOM   3754  C  CA  . CYS D  1 58  ? 99.760  1.865   26.073  1.00 5.92  ? 57  CYS G CA  1 
ATOM   3755  C  C   . CYS D  1 58  ? 99.494  3.192   25.416  1.00 5.40  ? 57  CYS G C   1 
ATOM   3756  O  O   . CYS D  1 58  ? 99.063  3.264   24.269  1.00 4.62  ? 57  CYS G O   1 
ATOM   3757  C  CB  . CYS D  1 58  ? 98.425  1.329   26.504  1.00 2.80  ? 57  CYS G CB  1 
ATOM   3758  S  SG  . CYS D  1 58  ? 98.634  -0.426  26.847  1.00 4.76  ? 57  CYS G SG  1 
ATOM   3759  N  N   . THR D  1 59  ? 99.801  4.238   26.146  1.00 6.21  ? 58  THR G N   1 
ATOM   3760  C  CA  . THR D  1 59  ? 99.608  5.606   25.728  1.00 8.65  ? 58  THR G CA  1 
ATOM   3761  C  C   . THR D  1 59  ? 100.431 5.894   24.488  1.00 8.77  ? 58  THR G C   1 
ATOM   3762  O  O   . THR D  1 59  ? 99.911  6.570   23.598  1.00 13.95 ? 58  THR G O   1 
ATOM   3763  C  CB  . THR D  1 59  ? 100.041 6.560   26.870  1.00 10.24 ? 58  THR G CB  1 
ATOM   3764  O  OG1 . THR D  1 59  ? 99.603  6.019   28.140  1.00 14.24 ? 58  THR G OG1 1 
ATOM   3765  C  CG2 . THR D  1 59  ? 99.468  7.924   26.636  1.00 10.52 ? 58  THR G CG2 1 
ATOM   3766  N  N   . SER D  1 60  ? 101.659 5.384   24.308  1.00 5.85  ? 59  SER G N   1 
ATOM   3767  C  CA  . SER D  1 60  ? 102.401 5.776   23.136  1.00 2.00  ? 59  SER G CA  1 
ATOM   3768  C  C   . SER D  1 60  ? 101.951 5.060   21.875  1.00 2.00  ? 59  SER G C   1 
ATOM   3769  O  O   . SER D  1 60  ? 102.415 5.377   20.780  1.00 2.91  ? 59  SER G O   1 
ATOM   3770  C  CB  . SER D  1 60  ? 103.882 5.576   23.424  1.00 2.00  ? 59  SER G CB  1 
ATOM   3771  O  OG  . SER D  1 60  ? 104.242 4.575   24.375  1.00 5.75  ? 59  SER G OG  1 
ATOM   3772  N  N   . ALA D  1 61  ? 100.962 4.164   21.984  1.00 3.66  ? 60  ALA G N   1 
ATOM   3773  C  CA  . ALA D  1 61  ? 100.335 3.504   20.852  1.00 3.61  ? 60  ALA G CA  1 
ATOM   3774  C  C   . ALA D  1 61  ? 99.753  4.554   19.923  1.00 4.73  ? 60  ALA G C   1 
ATOM   3775  O  O   . ALA D  1 61  ? 99.473  4.266   18.765  1.00 8.15  ? 60  ALA G O   1 
ATOM   3776  C  CB  . ALA D  1 61  ? 99.177  2.635   21.270  1.00 2.00  ? 60  ALA G CB  1 
ATOM   3777  N  N   . GLY D  1 62  ? 99.446  5.763   20.384  1.00 3.71  ? 61  GLY G N   1 
ATOM   3778  C  CA  . GLY D  1 62  ? 98.965  6.794   19.493  1.00 2.12  ? 61  GLY G CA  1 
ATOM   3779  C  C   . GLY D  1 62  ? 97.460  6.762   19.396  1.00 2.78  ? 61  GLY G C   1 
ATOM   3780  O  O   . GLY D  1 62  ? 96.811  6.139   20.233  1.00 6.50  ? 61  GLY G O   1 
ATOM   3781  N  N   . PRO D  1 63  ? 96.829  7.423   18.429  1.00 2.76  ? 62  PRO G N   1 
ATOM   3782  C  CA  . PRO D  1 63  ? 95.410  7.304   18.094  1.00 2.00  ? 62  PRO G CA  1 
ATOM   3783  C  C   . PRO D  1 63  ? 95.024  6.019   17.342  1.00 2.00  ? 62  PRO G C   1 
ATOM   3784  O  O   . PRO D  1 63  ? 95.877  5.163   17.147  1.00 2.00  ? 62  PRO G O   1 
ATOM   3785  C  CB  . PRO D  1 63  ? 95.208  8.576   17.318  1.00 2.00  ? 62  PRO G CB  1 
ATOM   3786  C  CG  . PRO D  1 63  ? 96.454  8.564   16.461  1.00 2.00  ? 62  PRO G CG  1 
ATOM   3787  C  CD  . PRO D  1 63  ? 97.464  8.409   17.555  1.00 2.00  ? 62  PRO G CD  1 
ATOM   3788  N  N   . HIS D  1 64  ? 93.790  5.836   16.834  1.00 2.99  ? 63  HIS G N   1 
ATOM   3789  C  CA  . HIS D  1 64  ? 93.430  4.646   16.054  1.00 2.26  ? 63  HIS G CA  1 
ATOM   3790  C  C   . HIS D  1 64  ? 94.074  4.736   14.682  1.00 2.00  ? 63  HIS G C   1 
ATOM   3791  O  O   . HIS D  1 64  ? 94.124  5.799   14.084  1.00 2.00  ? 63  HIS G O   1 
ATOM   3792  C  CB  . HIS D  1 64  ? 91.906  4.508   15.853  1.00 2.00  ? 63  HIS G CB  1 
ATOM   3793  C  CG  . HIS D  1 64  ? 91.073  4.233   17.117  1.00 2.33  ? 63  HIS G CG  1 
ATOM   3794  N  ND1 . HIS D  1 64  ? 89.777  4.453   17.341  1.00 2.00  ? 63  HIS G ND1 1 
ATOM   3795  C  CD2 . HIS D  1 64  ? 91.600  3.755   18.285  1.00 2.00  ? 63  HIS G CD2 1 
ATOM   3796  C  CE1 . HIS D  1 64  ? 89.571  4.126   18.589  1.00 2.00  ? 63  HIS G CE1 1 
ATOM   3797  N  NE2 . HIS D  1 64  ? 90.664  3.691   19.178  1.00 2.48  ? 63  HIS G NE2 1 
ATOM   3798  N  N   . PHE D  1 65  ? 94.619  3.643   14.163  1.00 2.00  ? 64  PHE G N   1 
ATOM   3799  C  CA  . PHE D  1 65  ? 95.229  3.615   12.852  1.00 2.00  ? 64  PHE G CA  1 
ATOM   3800  C  C   . PHE D  1 65  ? 94.140  4.017   11.866  1.00 2.00  ? 64  PHE G C   1 
ATOM   3801  O  O   . PHE D  1 65  ? 93.068  3.405   11.771  1.00 2.25  ? 64  PHE G O   1 
ATOM   3802  C  CB  . PHE D  1 65  ? 95.726  2.224   12.654  1.00 2.00  ? 64  PHE G CB  1 
ATOM   3803  C  CG  . PHE D  1 65  ? 96.333  1.922   11.306  1.00 2.81  ? 64  PHE G CG  1 
ATOM   3804  C  CD1 . PHE D  1 65  ? 97.236  2.787   10.703  1.00 2.00  ? 64  PHE G CD1 1 
ATOM   3805  C  CD2 . PHE D  1 65  ? 95.941  0.757   10.671  1.00 2.00  ? 64  PHE G CD2 1 
ATOM   3806  C  CE1 . PHE D  1 65  ? 97.720  2.476   9.455   1.00 2.00  ? 64  PHE G CE1 1 
ATOM   3807  C  CE2 . PHE D  1 65  ? 96.430  0.458   9.419   1.00 2.00  ? 64  PHE G CE2 1 
ATOM   3808  C  CZ  . PHE D  1 65  ? 97.317  1.309   8.820   1.00 2.55  ? 64  PHE G CZ  1 
ATOM   3809  N  N   . ASN D  1 66  ? 94.387  5.108   11.174  1.00 2.00  ? 65  ASN G N   1 
ATOM   3810  C  CA  . ASN D  1 66  ? 93.396  5.721   10.309  1.00 2.00  ? 65  ASN G CA  1 
ATOM   3811  C  C   . ASN D  1 66  ? 94.004  6.125   8.985   1.00 3.04  ? 65  ASN G C   1 
ATOM   3812  O  O   . ASN D  1 66  ? 93.986  7.308   8.665   1.00 7.37  ? 65  ASN G O   1 
ATOM   3813  C  CB  . ASN D  1 66  ? 92.836  6.926   11.039  1.00 2.00  ? 65  ASN G CB  1 
ATOM   3814  C  CG  . ASN D  1 66  ? 91.631  7.555   10.404  1.00 2.00  ? 65  ASN G CG  1 
ATOM   3815  O  OD1 . ASN D  1 66  ? 90.939  7.007   9.546   1.00 4.23  ? 65  ASN G OD1 1 
ATOM   3816  N  ND2 . ASN D  1 66  ? 91.323  8.777   10.781  1.00 2.70  ? 65  ASN G ND2 1 
ATOM   3817  N  N   . PRO D  1 67  ? 94.575  5.284   8.125   1.00 4.06  ? 66  PRO G N   1 
ATOM   3818  C  CA  . PRO D  1 67  ? 95.257  5.714   6.930   1.00 3.79  ? 66  PRO G CA  1 
ATOM   3819  C  C   . PRO D  1 67  ? 94.332  6.425   5.957   1.00 6.47  ? 66  PRO G C   1 
ATOM   3820  O  O   . PRO D  1 67  ? 94.836  7.051   5.021   1.00 11.92 ? 66  PRO G O   1 
ATOM   3821  C  CB  . PRO D  1 67  ? 95.845  4.462   6.357   1.00 2.00  ? 66  PRO G CB  1 
ATOM   3822  C  CG  . PRO D  1 67  ? 94.832  3.449   6.736   1.00 3.72  ? 66  PRO G CG  1 
ATOM   3823  C  CD  . PRO D  1 67  ? 94.493  3.827   8.173   1.00 3.76  ? 66  PRO G CD  1 
ATOM   3824  N  N   . LEU D  1 68  ? 93.008  6.411   6.061   1.00 4.13  ? 67  LEU G N   1 
ATOM   3825  C  CA  . LEU D  1 68  ? 92.170  7.115   5.105   1.00 2.13  ? 67  LEU G CA  1 
ATOM   3826  C  C   . LEU D  1 68  ? 91.515  8.318   5.766   1.00 4.62  ? 67  LEU G C   1 
ATOM   3827  O  O   . LEU D  1 68  ? 90.528  8.799   5.242   1.00 2.57  ? 67  LEU G O   1 
ATOM   3828  C  CB  . LEU D  1 68  ? 91.101  6.194   4.589   1.00 2.00  ? 67  LEU G CB  1 
ATOM   3829  C  CG  . LEU D  1 68  ? 91.544  4.812   4.130   1.00 2.78  ? 67  LEU G CG  1 
ATOM   3830  C  CD1 . LEU D  1 68  ? 90.371  4.002   3.672   1.00 2.00  ? 67  LEU G CD1 1 
ATOM   3831  C  CD2 . LEU D  1 68  ? 92.531  4.964   3.010   1.00 2.46  ? 67  LEU G CD2 1 
ATOM   3832  N  N   . SER D  1 69  ? 91.975  8.815   6.930   1.00 6.81  ? 68  SER G N   1 
ATOM   3833  C  CA  . SER D  1 69  ? 91.392  9.967   7.616   1.00 9.57  ? 68  SER G CA  1 
ATOM   3834  C  C   . SER D  1 69  ? 89.871  10.062  7.606   1.00 10.35 ? 68  SER G C   1 
ATOM   3835  O  O   . SER D  1 69  ? 89.257  11.016  7.118   1.00 13.70 ? 68  SER G O   1 
ATOM   3836  C  CB  . SER D  1 69  ? 92.008  11.234  7.036   1.00 8.78  ? 68  SER G CB  1 
ATOM   3837  O  OG  . SER D  1 69  ? 93.367  11.153  7.481   1.00 14.91 ? 68  SER G OG  1 
ATOM   3838  N  N   . ARG D  1 70  ? 89.285  9.007   8.161   1.00 8.84  ? 69  ARG G N   1 
ATOM   3839  C  CA  . ARG D  1 70  ? 87.856  8.927   8.273   1.00 7.81  ? 69  ARG G CA  1 
ATOM   3840  C  C   . ARG D  1 70  ? 87.504  9.164   9.712   1.00 8.66  ? 69  ARG G C   1 
ATOM   3841  O  O   . ARG D  1 70  ? 88.334  9.666   10.485  1.00 10.38 ? 69  ARG G O   1 
ATOM   3842  C  CB  . ARG D  1 70  ? 87.412  7.568   7.806   1.00 8.32  ? 69  ARG G CB  1 
ATOM   3843  C  CG  . ARG D  1 70  ? 87.706  7.578   6.314   1.00 7.37  ? 69  ARG G CG  1 
ATOM   3844  C  CD  . ARG D  1 70  ? 86.500  7.689   5.444   1.00 10.15 ? 69  ARG G CD  1 
ATOM   3845  N  NE  . ARG D  1 70  ? 86.060  6.345   5.112   1.00 17.48 ? 69  ARG G NE  1 
ATOM   3846  C  CZ  . ARG D  1 70  ? 86.544  5.665   4.053   1.00 19.23 ? 69  ARG G CZ  1 
ATOM   3847  N  NH1 . ARG D  1 70  ? 87.436  6.188   3.183   1.00 18.85 ? 69  ARG G NH1 1 
ATOM   3848  N  NH2 . ARG D  1 70  ? 86.074  4.436   3.845   1.00 21.05 ? 69  ARG G NH2 1 
ATOM   3849  N  N   . LYS D  1 71  ? 86.275  8.899   10.102  1.00 7.96  ? 70  LYS G N   1 
ATOM   3850  C  CA  . LYS D  1 71  ? 85.905  9.035   11.490  1.00 6.31  ? 70  LYS G CA  1 
ATOM   3851  C  C   . LYS D  1 71  ? 85.578  7.661   12.029  1.00 3.75  ? 70  LYS G C   1 
ATOM   3852  O  O   . LYS D  1 71  ? 85.406  6.706   11.281  1.00 3.17  ? 70  LYS G O   1 
ATOM   3853  C  CB  . LYS D  1 71  ? 84.710  9.879   11.637  1.00 8.25  ? 70  LYS G CB  1 
ATOM   3854  C  CG  . LYS D  1 71  ? 85.037  11.294  11.254  1.00 17.77 ? 70  LYS G CG  1 
ATOM   3855  C  CD  . LYS D  1 71  ? 83.688  12.042  11.157  1.00 25.59 ? 70  LYS G CD  1 
ATOM   3856  C  CE  . LYS D  1 71  ? 83.927  13.333  10.371  1.00 30.62 ? 70  LYS G CE  1 
ATOM   3857  N  NZ  . LYS D  1 71  ? 82.696  13.858  9.767   1.00 38.46 ? 70  LYS G NZ  1 
ATOM   3858  N  N   . HIS D  1 72  ? 85.586  7.596   13.349  1.00 2.00  ? 71  HIS G N   1 
ATOM   3859  C  CA  . HIS D  1 72  ? 85.267  6.434   14.101  1.00 2.00  ? 71  HIS G CA  1 
ATOM   3860  C  C   . HIS D  1 72  ? 83.925  5.885   13.715  1.00 2.08  ? 71  HIS G C   1 
ATOM   3861  O  O   . HIS D  1 72  ? 82.966  6.621   13.472  1.00 4.46  ? 71  HIS G O   1 
ATOM   3862  C  CB  . HIS D  1 72  ? 85.236  6.748   15.561  1.00 2.56  ? 71  HIS G CB  1 
ATOM   3863  C  CG  . HIS D  1 72  ? 85.354  5.479   16.369  1.00 2.00  ? 71  HIS G CG  1 
ATOM   3864  N  ND1 . HIS D  1 72  ? 86.463  4.794   16.482  1.00 2.00  ? 71  HIS G ND1 1 
ATOM   3865  C  CD2 . HIS D  1 72  ? 84.376  4.849   17.054  1.00 2.00  ? 71  HIS G CD2 1 
ATOM   3866  C  CE1 . HIS D  1 72  ? 86.182  3.761   17.220  1.00 3.15  ? 71  HIS G CE1 1 
ATOM   3867  N  NE2 . HIS D  1 72  ? 84.928  3.790   17.553  1.00 2.00  ? 71  HIS G NE2 1 
ATOM   3868  N  N   . GLY D  1 73  ? 83.928  4.582   13.700  1.00 2.00  ? 72  GLY G N   1 
ATOM   3869  C  CA  . GLY D  1 73  ? 82.740  3.902   13.400  1.00 2.00  ? 72  GLY G CA  1 
ATOM   3870  C  C   . GLY D  1 73  ? 82.920  2.535   14.005  1.00 2.00  ? 72  GLY G C   1 
ATOM   3871  O  O   . GLY D  1 73  ? 83.850  2.235   14.779  1.00 2.17  ? 72  GLY G O   1 
ATOM   3872  N  N   . GLY D  1 74  ? 81.959  1.705   13.712  1.00 2.00  ? 73  GLY G N   1 
ATOM   3873  C  CA  . GLY D  1 74  ? 82.063  0.326   14.078  1.00 2.47  ? 73  GLY G CA  1 
ATOM   3874  C  C   . GLY D  1 74  ? 82.648  -0.420  12.920  1.00 2.00  ? 73  GLY G C   1 
ATOM   3875  O  O   . GLY D  1 74  ? 82.831  0.156   11.861  1.00 2.00  ? 73  GLY G O   1 
ATOM   3876  N  N   . PRO D  1 75  ? 82.906  -1.700  13.055  1.00 2.00  ? 74  PRO G N   1 
ATOM   3877  C  CA  . PRO D  1 75  ? 83.501  -2.508  12.019  1.00 3.98  ? 74  PRO G CA  1 
ATOM   3878  C  C   . PRO D  1 75  ? 82.643  -2.724  10.786  1.00 6.55  ? 74  PRO G C   1 
ATOM   3879  O  O   . PRO D  1 75  ? 83.153  -3.028  9.703   1.00 10.72 ? 74  PRO G O   1 
ATOM   3880  C  CB  . PRO D  1 75  ? 83.872  -3.792  12.733  1.00 3.66  ? 74  PRO G CB  1 
ATOM   3881  C  CG  . PRO D  1 75  ? 83.036  -3.873  13.981  1.00 2.00  ? 74  PRO G CG  1 
ATOM   3882  C  CD  . PRO D  1 75  ? 82.929  -2.401  14.328  1.00 2.88  ? 74  PRO G CD  1 
ATOM   3883  N  N   . LYS D  1 76  ? 81.333  -2.561  10.874  1.00 7.15  ? 75  LYS G N   1 
ATOM   3884  C  CA  . LYS D  1 76  ? 80.498  -2.780  9.718   1.00 7.80  ? 75  LYS G CA  1 
ATOM   3885  C  C   . LYS D  1 76  ? 80.289  -1.483  8.971   1.00 9.31  ? 75  LYS G C   1 
ATOM   3886  O  O   . LYS D  1 76  ? 79.478  -1.404  8.053   1.00 12.21 ? 75  LYS G O   1 
ATOM   3887  C  CB  . LYS D  1 76  ? 79.143  -3.340  10.145  1.00 9.64  ? 75  LYS G CB  1 
ATOM   3888  C  CG  . LYS D  1 76  ? 79.076  -4.662  10.943  1.00 14.55 ? 75  LYS G CG  1 
ATOM   3889  C  CD  . LYS D  1 76  ? 77.604  -5.121  11.168  1.00 17.64 ? 75  LYS G CD  1 
ATOM   3890  C  CE  . LYS D  1 76  ? 76.754  -4.122  11.989  1.00 20.77 ? 75  LYS G CE  1 
ATOM   3891  N  NZ  . LYS D  1 76  ? 75.355  -4.059  11.575  1.00 18.43 ? 75  LYS G NZ  1 
ATOM   3892  N  N   . ASP D  1 77  ? 80.993  -0.415  9.278   1.00 11.05 ? 76  ASP G N   1 
ATOM   3893  C  CA  . ASP D  1 77  ? 80.681  0.862   8.672   1.00 10.86 ? 76  ASP G CA  1 
ATOM   3894  C  C   . ASP D  1 77  ? 81.685  1.162   7.572   1.00 12.35 ? 76  ASP G C   1 
ATOM   3895  O  O   . ASP D  1 77  ? 82.817  0.654   7.498   1.00 12.10 ? 76  ASP G O   1 
ATOM   3896  C  CB  . ASP D  1 77  ? 80.716  2.001   9.739   1.00 13.02 ? 76  ASP G CB  1 
ATOM   3897  C  CG  . ASP D  1 77  ? 79.762  2.016   10.946  1.00 14.40 ? 76  ASP G CG  1 
ATOM   3898  O  OD1 . ASP D  1 77  ? 78.949  1.117   11.136  1.00 18.76 ? 76  ASP G OD1 1 
ATOM   3899  O  OD2 . ASP D  1 77  ? 79.835  2.940   11.739  1.00 14.80 ? 76  ASP G OD2 1 
ATOM   3900  N  N   . GLU D  1 78  ? 81.240  2.003   6.640   1.00 15.28 ? 77  GLU G N   1 
ATOM   3901  C  CA  . GLU D  1 78  ? 82.163  2.500   5.636   1.00 15.55 ? 77  GLU G CA  1 
ATOM   3902  C  C   . GLU D  1 78  ? 83.031  3.549   6.343   1.00 11.70 ? 77  GLU G C   1 
ATOM   3903  O  O   . GLU D  1 78  ? 84.234  3.667   6.123   1.00 13.04 ? 77  GLU G O   1 
ATOM   3904  C  CB  . GLU D  1 78  ? 81.475  3.217   4.485   1.00 22.27 ? 77  GLU G CB  1 
ATOM   3905  C  CG  . GLU D  1 78  ? 80.644  2.552   3.381   1.00 31.34 ? 77  GLU G CG  1 
ATOM   3906  C  CD  . GLU D  1 78  ? 80.634  3.447   2.112   1.00 36.42 ? 77  GLU G CD  1 
ATOM   3907  O  OE1 . GLU D  1 78  ? 81.638  3.403   1.385   1.00 38.68 ? 77  GLU G OE1 1 
ATOM   3908  O  OE2 . GLU D  1 78  ? 79.667  4.196   1.858   1.00 37.73 ? 77  GLU G OE2 1 
ATOM   3909  N  N   . GLU D  1 79  ? 82.409  4.334   7.215   1.00 6.71  ? 78  GLU G N   1 
ATOM   3910  C  CA  . GLU D  1 79  ? 83.074  5.428   7.851   1.00 4.96  ? 78  GLU G CA  1 
ATOM   3911  C  C   . GLU D  1 79  ? 83.457  4.832   9.178   1.00 3.23  ? 78  GLU G C   1 
ATOM   3912  O  O   . GLU D  1 79  ? 82.649  4.596   10.071  1.00 2.00  ? 78  GLU G O   1 
ATOM   3913  C  CB  . GLU D  1 79  ? 82.121  6.602   8.026   1.00 3.12  ? 78  GLU G CB  1 
ATOM   3914  C  CG  . GLU D  1 79  ? 82.765  7.933   8.391   1.00 2.96  ? 78  GLU G CG  1 
ATOM   3915  C  CD  . GLU D  1 79  ? 83.511  8.687   7.298   1.00 10.19 ? 78  GLU G CD  1 
ATOM   3916  O  OE1 . GLU D  1 79  ? 83.241  8.480   6.109   1.00 14.46 ? 78  GLU G OE1 1 
ATOM   3917  O  OE2 . GLU D  1 79  ? 84.362  9.519   7.636   1.00 13.79 ? 78  GLU G OE2 1 
ATOM   3918  N  N   . ARG D  1 80  ? 84.722  4.456   9.113   1.00 3.29  ? 79  ARG G N   1 
ATOM   3919  C  CA  . ARG D  1 80  ? 85.389  3.855   10.231  1.00 3.56  ? 79  ARG G CA  1 
ATOM   3920  C  C   . ARG D  1 80  ? 86.847  3.989   9.912   1.00 2.00  ? 79  ARG G C   1 
ATOM   3921  O  O   . ARG D  1 80  ? 87.211  4.136   8.748   1.00 2.00  ? 79  ARG G O   1 
ATOM   3922  C  CB  . ARG D  1 80  ? 84.994  2.385   10.358  1.00 2.92  ? 79  ARG G CB  1 
ATOM   3923  C  CG  . ARG D  1 80  ? 85.267  1.574   9.130   1.00 2.00  ? 79  ARG G CG  1 
ATOM   3924  C  CD  . ARG D  1 80  ? 86.218  0.680   9.741   1.00 2.00  ? 79  ARG G CD  1 
ATOM   3925  N  NE  . ARG D  1 80  ? 85.867  -0.687  9.630   1.00 2.00  ? 79  ARG G NE  1 
ATOM   3926  C  CZ  . ARG D  1 80  ? 86.787  -1.581  9.932   1.00 2.00  ? 79  ARG G CZ  1 
ATOM   3927  N  NH1 . ARG D  1 80  ? 88.001  -1.212  10.324  1.00 2.00  ? 79  ARG G NH1 1 
ATOM   3928  N  NH2 . ARG D  1 80  ? 86.474  -2.865  9.828   1.00 2.00  ? 79  ARG G NH2 1 
ATOM   3929  N  N   . HIS D  1 81  ? 87.643  4.002   10.975  1.00 2.00  ? 80  HIS G N   1 
ATOM   3930  C  CA  . HIS D  1 81  ? 89.095  3.947   10.871  1.00 3.03  ? 80  HIS G CA  1 
ATOM   3931  C  C   . HIS D  1 81  ? 89.483  2.477   10.562  1.00 2.00  ? 80  HIS G C   1 
ATOM   3932  O  O   . HIS D  1 81  ? 88.733  1.600   10.950  1.00 2.00  ? 80  HIS G O   1 
ATOM   3933  C  CB  . HIS D  1 81  ? 89.781  4.303   12.187  1.00 2.00  ? 80  HIS G CB  1 
ATOM   3934  C  CG  . HIS D  1 81  ? 89.379  5.560   12.935  1.00 4.81  ? 80  HIS G CG  1 
ATOM   3935  N  ND1 . HIS D  1 81  ? 89.149  5.613   14.245  1.00 4.56  ? 80  HIS G ND1 1 
ATOM   3936  C  CD2 . HIS D  1 81  ? 89.288  6.852   12.444  1.00 2.00  ? 80  HIS G CD2 1 
ATOM   3937  C  CE1 . HIS D  1 81  ? 88.939  6.893   14.562  1.00 2.00  ? 80  HIS G CE1 1 
ATOM   3938  N  NE2 . HIS D  1 81  ? 89.028  7.607   13.471  1.00 2.00  ? 80  HIS G NE2 1 
ATOM   3939  N  N   . VAL D  1 82  ? 90.620  2.110   9.944   1.00 3.05  ? 81  VAL G N   1 
ATOM   3940  C  CA  . VAL D  1 82  ? 91.042  0.731   9.676   1.00 2.00  ? 81  VAL G CA  1 
ATOM   3941  C  C   . VAL D  1 82  ? 91.149  -0.088  10.960  1.00 2.32  ? 81  VAL G C   1 
ATOM   3942  O  O   . VAL D  1 82  ? 90.776  -1.268  10.977  1.00 2.00  ? 81  VAL G O   1 
ATOM   3943  C  CB  . VAL D  1 82  ? 92.400  0.754   8.940   1.00 2.00  ? 81  VAL G CB  1 
ATOM   3944  C  CG1 . VAL D  1 82  ? 93.057  -0.608  8.837   1.00 2.00  ? 81  VAL G CG1 1 
ATOM   3945  C  CG2 . VAL D  1 82  ? 92.151  1.080   7.508   1.00 2.00  ? 81  VAL G CG2 1 
ATOM   3946  N  N   . GLY D  1 83  ? 91.609  0.551   12.059  1.00 2.73  ? 82  GLY G N   1 
ATOM   3947  C  CA  . GLY D  1 83  ? 91.768  -0.117  13.341  1.00 2.00  ? 82  GLY G CA  1 
ATOM   3948  C  C   . GLY D  1 83  ? 90.503  -0.222  14.150  1.00 2.00  ? 82  GLY G C   1 
ATOM   3949  O  O   . GLY D  1 83  ? 90.580  -0.584  15.309  1.00 2.00  ? 82  GLY G O   1 
ATOM   3950  N  N   . ASP D  1 84  ? 89.304  0.063   13.664  1.00 2.36  ? 83  ASP G N   1 
ATOM   3951  C  CA  . ASP D  1 84  ? 88.078  0.019   14.440  1.00 2.00  ? 83  ASP G CA  1 
ATOM   3952  C  C   . ASP D  1 84  ? 87.433  -1.326  14.368  1.00 2.00  ? 83  ASP G C   1 
ATOM   3953  O  O   . ASP D  1 84  ? 86.708  -1.620  13.429  1.00 2.00  ? 83  ASP G O   1 
ATOM   3954  C  CB  . ASP D  1 84  ? 87.078  1.068   13.957  1.00 2.00  ? 83  ASP G CB  1 
ATOM   3955  C  CG  . ASP D  1 84  ? 87.472  2.477   14.348  1.00 3.12  ? 83  ASP G CG  1 
ATOM   3956  O  OD1 . ASP D  1 84  ? 88.339  2.647   15.211  1.00 5.14  ? 83  ASP G OD1 1 
ATOM   3957  O  OD2 . ASP D  1 84  ? 86.933  3.451   13.798  1.00 7.24  ? 83  ASP G OD2 1 
ATOM   3958  N  N   . LEU D  1 85  ? 87.704  -2.128  15.390  1.00 2.00  ? 84  LEU G N   1 
ATOM   3959  C  CA  . LEU D  1 85  ? 87.253  -3.514  15.487  1.00 2.00  ? 84  LEU G CA  1 
ATOM   3960  C  C   . LEU D  1 85  ? 86.032  -3.661  16.394  1.00 2.00  ? 84  LEU G C   1 
ATOM   3961  O  O   . LEU D  1 85  ? 85.607  -4.774  16.669  1.00 2.56  ? 84  LEU G O   1 
ATOM   3962  C  CB  . LEU D  1 85  ? 88.414  -4.360  15.995  1.00 2.00  ? 84  LEU G CB  1 
ATOM   3963  C  CG  . LEU D  1 85  ? 89.639  -4.610  15.057  1.00 2.89  ? 84  LEU G CG  1 
ATOM   3964  C  CD1 . LEU D  1 85  ? 90.784  -5.229  15.790  1.00 2.00  ? 84  LEU G CD1 1 
ATOM   3965  C  CD2 . LEU D  1 85  ? 89.263  -5.618  13.982  1.00 2.83  ? 84  LEU G CD2 1 
ATOM   3966  N  N   . GLY D  1 86  ? 85.373  -2.580  16.841  1.00 2.00  ? 85  GLY G N   1 
ATOM   3967  C  CA  . GLY D  1 86  ? 84.171  -2.681  17.648  1.00 2.00  ? 85  GLY G CA  1 
ATOM   3968  C  C   . GLY D  1 86  ? 84.447  -3.075  19.075  1.00 2.00  ? 85  GLY G C   1 
ATOM   3969  O  O   . GLY D  1 86  ? 85.445  -2.621  19.627  1.00 2.41  ? 85  GLY G O   1 
ATOM   3970  N  N   . ASN D  1 87  ? 83.675  -3.978  19.678  1.00 2.29  ? 86  ASN G N   1 
ATOM   3971  C  CA  . ASN D  1 87  ? 83.801  -4.289  21.093  1.00 2.00  ? 86  ASN G CA  1 
ATOM   3972  C  C   . ASN D  1 87  ? 83.961  -5.790  21.225  1.00 3.82  ? 86  ASN G C   1 
ATOM   3973  O  O   . ASN D  1 87  ? 83.617  -6.548  20.312  1.00 2.00  ? 86  ASN G O   1 
ATOM   3974  C  CB  . ASN D  1 87  ? 82.584  -3.970  21.902  1.00 2.00  ? 86  ASN G CB  1 
ATOM   3975  C  CG  . ASN D  1 87  ? 82.162  -2.532  21.944  1.00 3.12  ? 86  ASN G CG  1 
ATOM   3976  O  OD1 . ASN D  1 87  ? 82.911  -1.744  22.475  1.00 6.04  ? 86  ASN G OD1 1 
ATOM   3977  N  ND2 . ASN D  1 87  ? 81.018  -2.052  21.488  1.00 2.00  ? 86  ASN G ND2 1 
ATOM   3978  N  N   . VAL D  1 88  ? 84.542  -6.204  22.349  1.00 2.71  ? 87  VAL G N   1 
ATOM   3979  C  CA  . VAL D  1 88  ? 84.588  -7.595  22.694  1.00 2.88  ? 87  VAL G CA  1 
ATOM   3980  C  C   . VAL D  1 88  ? 83.710  -7.651  23.929  1.00 3.41  ? 87  VAL G C   1 
ATOM   3981  O  O   . VAL D  1 88  ? 83.457  -6.593  24.536  1.00 2.00  ? 87  VAL G O   1 
ATOM   3982  C  CB  . VAL D  1 88  ? 86.030  -8.060  23.018  1.00 3.36  ? 87  VAL G CB  1 
ATOM   3983  C  CG1 . VAL D  1 88  ? 86.831  -8.025  21.757  1.00 2.00  ? 87  VAL G CG1 1 
ATOM   3984  C  CG2 . VAL D  1 88  ? 86.686  -7.175  24.068  1.00 3.65  ? 87  VAL G CG2 1 
ATOM   3985  N  N   . THR D  1 89  ? 83.235  -8.855  24.294  1.00 2.04  ? 88  THR G N   1 
ATOM   3986  C  CA  . THR D  1 89  ? 82.385  -9.081  25.457  1.00 2.00  ? 88  THR G CA  1 
ATOM   3987  C  C   . THR D  1 89  ? 82.972  -9.996  26.523  1.00 2.00  ? 88  THR G C   1 
ATOM   3988  O  O   . THR D  1 89  ? 83.175  -11.206 26.333  1.00 2.00  ? 88  THR G O   1 
ATOM   3989  C  CB  . THR D  1 89  ? 81.022  -9.667  24.968  1.00 2.49  ? 88  THR G CB  1 
ATOM   3990  O  OG1 . THR D  1 89  ? 80.512  -8.761  24.025  1.00 2.00  ? 88  THR G OG1 1 
ATOM   3991  C  CG2 . THR D  1 89  ? 80.011  -9.877  26.079  1.00 2.00  ? 88  THR G CG2 1 
ATOM   3992  N  N   . ALA D  1 90  ? 83.234  -9.423  27.675  1.00 2.00  ? 89  ALA G N   1 
ATOM   3993  C  CA  . ALA D  1 90  ? 83.713  -10.183 28.808  1.00 2.00  ? 89  ALA G CA  1 
ATOM   3994  C  C   . ALA D  1 90  ? 82.527  -10.736 29.603  1.00 2.58  ? 89  ALA G C   1 
ATOM   3995  O  O   . ALA D  1 90  ? 81.551  -10.036 29.918  1.00 2.00  ? 89  ALA G O   1 
ATOM   3996  C  CB  . ALA D  1 90  ? 84.536  -9.294  29.720  1.00 2.00  ? 89  ALA G CB  1 
ATOM   3997  N  N   . ASP D  1 91  ? 82.558  -12.025 29.888  1.00 2.00  ? 90  ASP G N   1 
ATOM   3998  C  CA  . ASP D  1 91  ? 81.544  -12.608 30.737  1.00 3.90  ? 90  ASP G CA  1 
ATOM   3999  C  C   . ASP D  1 91  ? 81.661  -12.209 32.206  1.00 4.37  ? 90  ASP G C   1 
ATOM   4000  O  O   . ASP D  1 91  ? 82.557  -11.461 32.571  1.00 4.47  ? 90  ASP G O   1 
ATOM   4001  C  CB  . ASP D  1 91  ? 81.584  -14.118 30.655  1.00 5.03  ? 90  ASP G CB  1 
ATOM   4002  C  CG  . ASP D  1 91  ? 82.869  -14.846 30.972  1.00 6.27  ? 90  ASP G CG  1 
ATOM   4003  O  OD1 . ASP D  1 91  ? 83.674  -14.406 31.784  1.00 8.20  ? 90  ASP G OD1 1 
ATOM   4004  O  OD2 . ASP D  1 91  ? 83.057  -15.911 30.398  1.00 10.85 ? 90  ASP G OD2 1 
ATOM   4005  N  N   . LYS D  1 92  ? 80.811  -12.718 33.099  1.00 7.38  ? 91  LYS G N   1 
ATOM   4006  C  CA  . LYS D  1 92  ? 80.816  -12.412 34.541  1.00 9.78  ? 91  LYS G CA  1 
ATOM   4007  C  C   . LYS D  1 92  ? 82.090  -12.733 35.282  1.00 9.24  ? 91  LYS G C   1 
ATOM   4008  O  O   . LYS D  1 92  ? 82.412  -12.037 36.236  1.00 10.74 ? 91  LYS G O   1 
ATOM   4009  C  CB  . LYS D  1 92  ? 79.696  -13.133 35.261  1.00 11.17 ? 91  LYS G CB  1 
ATOM   4010  C  CG  . LYS D  1 92  ? 79.642  -14.620 34.883  1.00 18.02 ? 91  LYS G CG  1 
ATOM   4011  C  CD  . LYS D  1 92  ? 78.582  -15.395 35.660  1.00 25.49 ? 91  LYS G CD  1 
ATOM   4012  C  CE  . LYS D  1 92  ? 77.157  -14.799 35.491  1.00 29.05 ? 91  LYS G CE  1 
ATOM   4013  N  NZ  . LYS D  1 92  ? 76.194  -15.427 36.393  1.00 33.97 ? 91  LYS G NZ  1 
ATOM   4014  N  N   . ASP D  1 93  ? 82.807  -13.766 34.844  1.00 9.97  ? 92  ASP G N   1 
ATOM   4015  C  CA  . ASP D  1 93  ? 84.153  -14.033 35.330  1.00 10.27 ? 92  ASP G CA  1 
ATOM   4016  C  C   . ASP D  1 93  ? 85.206  -13.104 34.735  1.00 9.68  ? 92  ASP G C   1 
ATOM   4017  O  O   . ASP D  1 93  ? 86.403  -13.325 34.954  1.00 12.33 ? 92  ASP G O   1 
ATOM   4018  C  CB  . ASP D  1 93  ? 84.586  -15.464 35.011  1.00 12.10 ? 92  ASP G CB  1 
ATOM   4019  C  CG  . ASP D  1 93  ? 83.714  -16.514 35.658  1.00 13.50 ? 92  ASP G CG  1 
ATOM   4020  O  OD1 . ASP D  1 93  ? 83.477  -16.431 36.876  1.00 13.58 ? 92  ASP G OD1 1 
ATOM   4021  O  OD2 . ASP D  1 93  ? 83.269  -17.394 34.911  1.00 16.54 ? 92  ASP G OD2 1 
ATOM   4022  N  N   . GLY D  1 94  ? 84.824  -12.088 33.954  1.00 7.22  ? 93  GLY G N   1 
ATOM   4023  C  CA  . GLY D  1 94  ? 85.749  -11.159 33.374  1.00 3.16  ? 93  GLY G CA  1 
ATOM   4024  C  C   . GLY D  1 94  ? 86.558  -11.664 32.209  1.00 2.00  ? 93  GLY G C   1 
ATOM   4025  O  O   . GLY D  1 94  ? 87.552  -11.067 31.839  1.00 3.54  ? 93  GLY G O   1 
ATOM   4026  N  N   . VAL D  1 95  ? 86.185  -12.715 31.543  1.00 2.17  ? 94  VAL G N   1 
ATOM   4027  C  CA  . VAL D  1 95  ? 86.933  -13.218 30.398  1.00 4.59  ? 94  VAL G CA  1 
ATOM   4028  C  C   . VAL D  1 95  ? 86.263  -12.881 29.057  1.00 4.08  ? 94  VAL G C   1 
ATOM   4029  O  O   . VAL D  1 95  ? 85.061  -13.140 28.924  1.00 4.34  ? 94  VAL G O   1 
ATOM   4030  C  CB  . VAL D  1 95  ? 87.070  -14.744 30.570  1.00 2.81  ? 94  VAL G CB  1 
ATOM   4031  C  CG1 . VAL D  1 95  ? 87.627  -15.436 29.351  1.00 2.00  ? 94  VAL G CG1 1 
ATOM   4032  C  CG2 . VAL D  1 95  ? 87.985  -14.948 31.731  1.00 2.54  ? 94  VAL G CG2 1 
ATOM   4033  N  N   . ALA D  1 96  ? 86.983  -12.378 28.047  1.00 4.39  ? 95  ALA G N   1 
ATOM   4034  C  CA  . ALA D  1 96  ? 86.459  -12.092 26.720  1.00 2.00  ? 95  ALA G CA  1 
ATOM   4035  C  C   . ALA D  1 96  ? 87.035  -13.118 25.751  1.00 2.22  ? 95  ALA G C   1 
ATOM   4036  O  O   . ALA D  1 96  ? 88.237  -13.093 25.461  1.00 2.16  ? 95  ALA G O   1 
ATOM   4037  C  CB  . ALA D  1 96  ? 86.893  -10.739 26.278  1.00 2.00  ? 95  ALA G CB  1 
ATOM   4038  N  N   . ASP D  1 97  ? 86.289  -14.114 25.270  1.00 2.00  ? 96  ASP G N   1 
ATOM   4039  C  CA  . ASP D  1 97  ? 86.819  -15.001 24.258  1.00 2.00  ? 96  ASP G CA  1 
ATOM   4040  C  C   . ASP D  1 97  ? 86.541  -14.233 23.011  1.00 3.31  ? 96  ASP G C   1 
ATOM   4041  O  O   . ASP D  1 97  ? 85.354  -13.963 22.829  1.00 4.14  ? 96  ASP G O   1 
ATOM   4042  C  CB  . ASP D  1 97  ? 86.089  -16.328 24.169  1.00 4.89  ? 96  ASP G CB  1 
ATOM   4043  C  CG  . ASP D  1 97  ? 86.202  -17.115 25.474  1.00 10.83 ? 96  ASP G CG  1 
ATOM   4044  O  OD1 . ASP D  1 97  ? 87.312  -17.348 25.983  1.00 15.52 ? 96  ASP G OD1 1 
ATOM   4045  O  OD2 . ASP D  1 97  ? 85.157  -17.480 26.016  1.00 16.83 ? 96  ASP G OD2 1 
ATOM   4046  N  N   . VAL D  1 98  ? 87.495  -13.820 22.163  1.00 2.56  ? 97  VAL G N   1 
ATOM   4047  C  CA  . VAL D  1 98  ? 87.049  -13.059 21.024  1.00 2.72  ? 97  VAL G CA  1 
ATOM   4048  C  C   . VAL D  1 98  ? 87.061  -13.858 19.720  1.00 2.00  ? 97  VAL G C   1 
ATOM   4049  O  O   . VAL D  1 98  ? 87.876  -14.751 19.522  1.00 2.00  ? 97  VAL G O   1 
ATOM   4050  C  CB  . VAL D  1 98  ? 87.876  -11.681 20.921  1.00 2.00  ? 97  VAL G CB  1 
ATOM   4051  C  CG1 . VAL D  1 98  ? 88.540  -11.410 22.243  1.00 2.00  ? 97  VAL G CG1 1 
ATOM   4052  C  CG2 . VAL D  1 98  ? 88.799  -11.650 19.754  1.00 2.00  ? 97  VAL G CG2 1 
ATOM   4053  N  N   . SER D  1 99  ? 86.119  -13.593 18.829  1.00 2.00  ? 98  SER G N   1 
ATOM   4054  C  CA  . SER D  1 99  ? 86.169  -14.103 17.481  1.00 2.00  ? 98  SER G CA  1 
ATOM   4055  C  C   . SER D  1 99  ? 85.820  -12.934 16.567  1.00 2.00  ? 98  SER G C   1 
ATOM   4056  O  O   . SER D  1 99  ? 84.763  -12.358 16.739  1.00 3.57  ? 98  SER G O   1 
ATOM   4057  C  CB  . SER D  1 99  ? 85.175  -15.198 17.296  1.00 2.00  ? 98  SER G CB  1 
ATOM   4058  O  OG  . SER D  1 99  ? 85.843  -16.446 17.177  1.00 7.08  ? 98  SER G OG  1 
ATOM   4059  N  N   . ILE D  1 100 ? 86.597  -12.422 15.634  1.00 2.00  ? 99  ILE G N   1 
ATOM   4060  C  CA  . ILE D  1 100 ? 86.130  -11.346 14.782  1.00 2.22  ? 99  ILE G CA  1 
ATOM   4061  C  C   . ILE D  1 100 ? 86.575  -11.703 13.390  1.00 2.00  ? 99  ILE G C   1 
ATOM   4062  O  O   . ILE D  1 100 ? 87.626  -12.304 13.249  1.00 2.44  ? 99  ILE G O   1 
ATOM   4063  C  CB  . ILE D  1 100 ? 86.742  -9.960  15.261  1.00 5.11  ? 99  ILE G CB  1 
ATOM   4064  C  CG1 . ILE D  1 100 ? 86.070  -9.575  16.613  1.00 3.76  ? 99  ILE G CG1 1 
ATOM   4065  C  CG2 . ILE D  1 100 ? 86.592  -8.878  14.163  1.00 2.42  ? 99  ILE G CG2 1 
ATOM   4066  C  CD1 . ILE D  1 100 ? 86.734  -8.434  17.427  1.00 7.81  ? 99  ILE G CD1 1 
ATOM   4067  N  N   . GLU D  1 101 ? 85.829  -11.466 12.344  1.00 2.00  ? 100 GLU G N   1 
ATOM   4068  C  CA  . GLU D  1 101 ? 86.400  -11.599 11.036  1.00 3.32  ? 100 GLU G CA  1 
ATOM   4069  C  C   . GLU D  1 101 ? 86.324  -10.181 10.465  1.00 3.13  ? 100 GLU G C   1 
ATOM   4070  O  O   . GLU D  1 101 ? 85.285  -9.529  10.563  1.00 2.00  ? 100 GLU G O   1 
ATOM   4071  C  CB  . GLU D  1 101 ? 85.583  -12.562 10.264  1.00 8.62  ? 100 GLU G CB  1 
ATOM   4072  C  CG  . GLU D  1 101 ? 85.885  -12.531 8.762   1.00 16.02 ? 100 GLU G CG  1 
ATOM   4073  C  CD  . GLU D  1 101 ? 85.365  -13.776 8.053   1.00 23.58 ? 100 GLU G CD  1 
ATOM   4074  O  OE1 . GLU D  1 101 ? 85.660  -14.867 8.556   1.00 25.16 ? 100 GLU G OE1 1 
ATOM   4075  O  OE2 . GLU D  1 101 ? 84.687  -13.665 7.013   1.00 27.03 ? 100 GLU G OE2 1 
ATOM   4076  N  N   . ASP D  1 102 ? 87.415  -9.633  9.950   1.00 2.00  ? 101 ASP G N   1 
ATOM   4077  C  CA  . ASP D  1 102 ? 87.334  -8.297  9.442   1.00 2.37  ? 101 ASP G CA  1 
ATOM   4078  C  C   . ASP D  1 102 ? 87.939  -8.143  8.053   1.00 3.09  ? 101 ASP G C   1 
ATOM   4079  O  O   . ASP D  1 102 ? 88.894  -8.798  7.694   1.00 3.00  ? 101 ASP G O   1 
ATOM   4080  C  CB  . ASP D  1 102 ? 88.015  -7.345  10.408  1.00 2.00  ? 101 ASP G CB  1 
ATOM   4081  C  CG  . ASP D  1 102 ? 87.645  -5.918  10.069  1.00 2.68  ? 101 ASP G CG  1 
ATOM   4082  O  OD1 . ASP D  1 102 ? 86.446  -5.617  10.103  1.00 6.35  ? 101 ASP G OD1 1 
ATOM   4083  O  OD2 . ASP D  1 102 ? 88.533  -5.134  9.739   1.00 3.22  ? 101 ASP G OD2 1 
ATOM   4084  N  N   . SER D  1 103 ? 87.393  -7.277  7.224   1.00 4.45  ? 102 SER G N   1 
ATOM   4085  C  CA  . SER D  1 103 ? 87.919  -7.095  5.893   1.00 5.07  ? 102 SER G CA  1 
ATOM   4086  C  C   . SER D  1 103 ? 88.710  -5.858  5.635   1.00 2.84  ? 102 SER G C   1 
ATOM   4087  O  O   . SER D  1 103 ? 89.273  -5.758  4.558   1.00 2.18  ? 102 SER G O   1 
ATOM   4088  C  CB  . SER D  1 103 ? 86.794  -7.130  4.880   1.00 7.90  ? 102 SER G CB  1 
ATOM   4089  O  OG  . SER D  1 103 ? 86.510  -8.497  4.544   1.00 16.79 ? 102 SER G OG  1 
ATOM   4090  N  N   . VAL D  1 104 ? 88.719  -4.913  6.574   1.00 3.60  ? 103 VAL G N   1 
ATOM   4091  C  CA  . VAL D  1 104 ? 89.402  -3.659  6.344   1.00 2.00  ? 103 VAL G CA  1 
ATOM   4092  C  C   . VAL D  1 104 ? 90.819  -3.728  6.875   1.00 2.00  ? 103 VAL G C   1 
ATOM   4093  O  O   . VAL D  1 104 ? 91.710  -3.106  6.302   1.00 3.21  ? 103 VAL G O   1 
ATOM   4094  C  CB  . VAL D  1 104 ? 88.541  -2.534  6.991   1.00 2.00  ? 103 VAL G CB  1 
ATOM   4095  C  CG1 . VAL D  1 104 ? 89.131  -1.169  6.788   1.00 2.00  ? 103 VAL G CG1 1 
ATOM   4096  C  CG2 . VAL D  1 104 ? 87.161  -2.551  6.334   1.00 2.00  ? 103 VAL G CG2 1 
ATOM   4097  N  N   . ILE D  1 105 ? 91.078  -4.426  7.979   1.00 3.18  ? 104 ILE G N   1 
ATOM   4098  C  CA  . ILE D  1 105 ? 92.452  -4.589  8.443   1.00 3.19  ? 104 ILE G CA  1 
ATOM   4099  C  C   . ILE D  1 105 ? 93.100  -5.610  7.514   1.00 3.56  ? 104 ILE G C   1 
ATOM   4100  O  O   . ILE D  1 105 ? 92.425  -6.416  6.866   1.00 2.00  ? 104 ILE G O   1 
ATOM   4101  C  CB  . ILE D  1 105 ? 92.551  -5.131  9.909   1.00 2.61  ? 104 ILE G CB  1 
ATOM   4102  C  CG1 . ILE D  1 105 ? 91.872  -6.495  10.095  1.00 2.00  ? 104 ILE G CG1 1 
ATOM   4103  C  CG2 . ILE D  1 105 ? 91.920  -4.080  10.819  1.00 2.99  ? 104 ILE G CG2 1 
ATOM   4104  C  CD1 . ILE D  1 105 ? 92.077  -6.987  11.517  1.00 2.00  ? 104 ILE G CD1 1 
ATOM   4105  N  N   . SER D  1 106 ? 94.428  -5.579  7.465   1.00 4.99  ? 105 SER G N   1 
ATOM   4106  C  CA  . SER D  1 106 ? 95.165  -6.550  6.689   1.00 3.27  ? 105 SER G CA  1 
ATOM   4107  C  C   . SER D  1 106 ? 96.468  -6.745  7.405   1.00 2.59  ? 105 SER G C   1 
ATOM   4108  O  O   . SER D  1 106 ? 96.854  -5.955  8.247   1.00 2.00  ? 105 SER G O   1 
ATOM   4109  C  CB  . SER D  1 106 ? 95.420  -6.031  5.294   1.00 2.85  ? 105 SER G CB  1 
ATOM   4110  O  OG  . SER D  1 106 ? 96.167  -6.930  4.470   1.00 2.93  ? 105 SER G OG  1 
ATOM   4111  N  N   . LEU D  1 107 ? 97.135  -7.839  7.095   1.00 3.51  ? 106 LEU G N   1 
ATOM   4112  C  CA  . LEU D  1 107 ? 98.455  -8.117  7.611   1.00 4.12  ? 106 LEU G CA  1 
ATOM   4113  C  C   . LEU D  1 107 ? 99.553  -7.730  6.596   1.00 2.00  ? 106 LEU G C   1 
ATOM   4114  O  O   . LEU D  1 107 ? 100.749 -7.956  6.780   1.00 2.00  ? 106 LEU G O   1 
ATOM   4115  C  CB  . LEU D  1 107 ? 98.490  -9.612  7.964   1.00 4.29  ? 106 LEU G CB  1 
ATOM   4116  C  CG  . LEU D  1 107 ? 97.489  -10.020 8.990   1.00 2.35  ? 106 LEU G CG  1 
ATOM   4117  C  CD1 . LEU D  1 107 ? 97.835  -11.412 9.337   1.00 2.00  ? 106 LEU G CD1 1 
ATOM   4118  C  CD2 . LEU D  1 107 ? 97.480  -9.066  10.205  1.00 2.44  ? 106 LEU G CD2 1 
ATOM   4119  N  N   . SER D  1 108 ? 99.162  -7.188  5.463   1.00 2.00  ? 107 SER G N   1 
ATOM   4120  C  CA  . SER D  1 108 ? 100.109 -6.793  4.444   1.00 3.54  ? 107 SER G CA  1 
ATOM   4121  C  C   . SER D  1 108 ? 99.489  -5.655  3.732   1.00 3.23  ? 107 SER G C   1 
ATOM   4122  O  O   . SER D  1 108 ? 98.292  -5.446  3.899   1.00 5.68  ? 107 SER G O   1 
ATOM   4123  C  CB  . SER D  1 108 ? 100.448 -7.919  3.420   1.00 2.00  ? 107 SER G CB  1 
ATOM   4124  O  OG  . SER D  1 108 ? 99.572  -9.008  3.084   1.00 7.81  ? 107 SER G OG  1 
ATOM   4125  N  N   . GLY D  1 109 ? 100.294 -4.838  3.061   1.00 4.73  ? 108 GLY G N   1 
ATOM   4126  C  CA  . GLY D  1 109 ? 99.827  -3.712  2.251   1.00 7.42  ? 108 GLY G CA  1 
ATOM   4127  C  C   . GLY D  1 109 ? 99.670  -2.448  3.059   1.00 9.96  ? 108 GLY G C   1 
ATOM   4128  O  O   . GLY D  1 109 ? 99.949  -2.466  4.246   1.00 13.34 ? 108 GLY G O   1 
ATOM   4129  N  N   . ASP D  1 110 ? 99.182  -1.330  2.535   1.00 11.57 ? 109 ASP G N   1 
ATOM   4130  C  CA  . ASP D  1 110 ? 99.040  -0.085  3.320   1.00 10.97 ? 109 ASP G CA  1 
ATOM   4131  C  C   . ASP D  1 110 ? 98.264  -0.213  4.622   1.00 10.13 ? 109 ASP G C   1 
ATOM   4132  O  O   . ASP D  1 110 ? 98.504  0.508   5.588   1.00 14.20 ? 109 ASP G O   1 
ATOM   4133  C  CB  . ASP D  1 110 ? 98.305  1.032   2.549   1.00 11.23 ? 109 ASP G CB  1 
ATOM   4134  C  CG  . ASP D  1 110 ? 98.885  1.544   1.248   1.00 10.23 ? 109 ASP G CG  1 
ATOM   4135  O  OD1 . ASP D  1 110 ? 100.100 1.536   1.066   1.00 11.05 ? 109 ASP G OD1 1 
ATOM   4136  O  OD2 . ASP D  1 110 ? 98.085  1.973   0.426   1.00 11.58 ? 109 ASP G OD2 1 
ATOM   4137  N  N   . HIS D  1 111 ? 97.256  -1.074  4.586   1.00 6.40  ? 110 HIS G N   1 
ATOM   4138  C  CA  . HIS D  1 111 ? 96.419  -1.347  5.725   1.00 5.99  ? 110 HIS G CA  1 
ATOM   4139  C  C   . HIS D  1 111 ? 96.950  -2.417  6.676   1.00 5.86  ? 110 HIS G C   1 
ATOM   4140  O  O   . HIS D  1 111 ? 96.140  -2.963  7.442   1.00 6.56  ? 110 HIS G O   1 
ATOM   4141  C  CB  . HIS D  1 111 ? 95.067  -1.787  5.237   1.00 7.78  ? 110 HIS G CB  1 
ATOM   4142  C  CG  . HIS D  1 111 ? 94.256  -0.682  4.609   1.00 10.24 ? 110 HIS G CG  1 
ATOM   4143  N  ND1 . HIS D  1 111 ? 92.971  -0.774  4.290   1.00 9.69  ? 110 HIS G ND1 1 
ATOM   4144  C  CD2 . HIS D  1 111 ? 94.735  0.595   4.327   1.00 10.39 ? 110 HIS G CD2 1 
ATOM   4145  C  CE1 . HIS D  1 111 ? 92.655  0.423   3.818   1.00 15.09 ? 110 HIS G CE1 1 
ATOM   4146  N  NE2 . HIS D  1 111 ? 93.716  1.231   3.845   1.00 12.36 ? 110 HIS G NE2 1 
ATOM   4147  N  N   . SER D  1 112 ? 98.244  -2.767  6.627   1.00 3.08  ? 111 SER G N   1 
ATOM   4148  C  CA  . SER D  1 112 ? 98.783  -3.841  7.436   1.00 3.00  ? 111 SER G CA  1 
ATOM   4149  C  C   . SER D  1 112 ? 98.771  -3.443  8.896   1.00 2.83  ? 111 SER G C   1 
ATOM   4150  O  O   . SER D  1 112 ? 99.044  -2.288  9.168   1.00 3.04  ? 111 SER G O   1 
ATOM   4151  C  CB  . SER D  1 112 ? 100.179 -4.128  6.989   1.00 3.53  ? 111 SER G CB  1 
ATOM   4152  O  OG  . SER D  1 112 ? 100.867 -5.091  7.753   1.00 2.00  ? 111 SER G OG  1 
ATOM   4153  N  N   . ILE D  1 113 ? 98.479  -4.310  9.857   1.00 2.00  ? 112 ILE G N   1 
ATOM   4154  C  CA  . ILE D  1 113 ? 98.485  -3.853  11.243  1.00 3.66  ? 112 ILE G CA  1 
ATOM   4155  C  C   . ILE D  1 113 ? 99.721  -4.435  11.934  1.00 5.27  ? 112 ILE G C   1 
ATOM   4156  O  O   . ILE D  1 113 ? 99.873  -4.455  13.163  1.00 4.14  ? 112 ILE G O   1 
ATOM   4157  C  CB  . ILE D  1 113 ? 97.139  -4.269  11.966  1.00 2.00  ? 112 ILE G CB  1 
ATOM   4158  C  CG1 . ILE D  1 113 ? 96.908  -5.759  11.795  1.00 2.23  ? 112 ILE G CG1 1 
ATOM   4159  C  CG2 . ILE D  1 113 ? 95.984  -3.387  11.444  1.00 2.00  ? 112 ILE G CG2 1 
ATOM   4160  C  CD1 . ILE D  1 113 ? 95.834  -6.434  12.634  1.00 2.00  ? 112 ILE G CD1 1 
ATOM   4161  N  N   . ILE D  1 114 ? 100.676 -4.933  11.127  1.00 3.63  ? 113 ILE G N   1 
ATOM   4162  C  CA  . ILE D  1 114 ? 101.909 -5.445  11.677  1.00 3.04  ? 113 ILE G CA  1 
ATOM   4163  C  C   . ILE D  1 114 ? 102.755 -4.273  12.172  1.00 4.26  ? 113 ILE G C   1 
ATOM   4164  O  O   . ILE D  1 114 ? 102.899 -3.239  11.498  1.00 2.00  ? 113 ILE G O   1 
ATOM   4165  C  CB  . ILE D  1 114 ? 102.655 -6.237  10.614  1.00 2.62  ? 113 ILE G CB  1 
ATOM   4166  C  CG1 . ILE D  1 114 ? 101.863 -7.455  10.109  1.00 2.00  ? 113 ILE G CG1 1 
ATOM   4167  C  CG2 . ILE D  1 114 ? 103.955 -6.656  11.218  1.00 2.00  ? 113 ILE G CG2 1 
ATOM   4168  C  CD1 . ILE D  1 114 ? 101.585 -8.549  11.083  1.00 2.00  ? 113 ILE G CD1 1 
ATOM   4169  N  N   . GLY D  1 115 ? 103.260 -4.459  13.397  1.00 2.90  ? 114 GLY G N   1 
ATOM   4170  C  CA  . GLY D  1 115 ? 104.110 -3.480  14.014  1.00 2.00  ? 114 GLY G CA  1 
ATOM   4171  C  C   . GLY D  1 115 ? 103.330 -2.359  14.641  1.00 2.00  ? 114 GLY G C   1 
ATOM   4172  O  O   . GLY D  1 115 ? 103.937 -1.350  14.993  1.00 3.84  ? 114 GLY G O   1 
ATOM   4173  N  N   . ARG D  1 116 ? 102.020 -2.475  14.817  1.00 2.00  ? 115 ARG G N   1 
ATOM   4174  C  CA  . ARG D  1 116 ? 101.191 -1.468  15.437  1.00 2.00  ? 115 ARG G CA  1 
ATOM   4175  C  C   . ARG D  1 116 ? 100.622 -2.023  16.709  1.00 2.00  ? 115 ARG G C   1 
ATOM   4176  O  O   . ARG D  1 116 ? 100.920 -3.156  17.054  1.00 2.00  ? 115 ARG G O   1 
ATOM   4177  C  CB  . ARG D  1 116 ? 100.068 -1.075  14.509  1.00 2.00  ? 115 ARG G CB  1 
ATOM   4178  C  CG  . ARG D  1 116 ? 100.599 -0.370  13.264  1.00 2.00  ? 115 ARG G CG  1 
ATOM   4179  C  CD  . ARG D  1 116 ? 99.510  0.230   12.359  1.00 2.39  ? 115 ARG G CD  1 
ATOM   4180  N  NE  . ARG D  1 116 ? 100.082 0.627   11.081  1.00 2.00  ? 115 ARG G NE  1 
ATOM   4181  C  CZ  . ARG D  1 116 ? 100.692 1.816   10.924  1.00 4.50  ? 115 ARG G CZ  1 
ATOM   4182  N  NH1 . ARG D  1 116 ? 100.711 2.791   11.844  1.00 2.00  ? 115 ARG G NH1 1 
ATOM   4183  N  NH2 . ARG D  1 116 ? 101.216 2.113   9.751   1.00 6.57  ? 115 ARG G NH2 1 
ATOM   4184  N  N   . THR D  1 117 ? 99.762  -1.340  17.439  1.00 2.35  ? 116 THR G N   1 
ATOM   4185  C  CA  . THR D  1 117 ? 99.311  -1.818  18.746  1.00 2.34  ? 116 THR G CA  1 
ATOM   4186  C  C   . THR D  1 117 ? 97.836  -2.130  18.887  1.00 2.00  ? 116 THR G C   1 
ATOM   4187  O  O   . THR D  1 117 ? 97.002  -1.305  18.545  1.00 4.79  ? 116 THR G O   1 
ATOM   4188  C  CB  . THR D  1 117 ? 99.755  -0.752  19.769  1.00 3.57  ? 116 THR G CB  1 
ATOM   4189  O  OG1 . THR D  1 117 ? 101.164 -0.751  19.655  1.00 3.37  ? 116 THR G OG1 1 
ATOM   4190  C  CG2 . THR D  1 117 ? 99.397  -1.016  21.202  1.00 3.09  ? 116 THR G CG2 1 
ATOM   4191  N  N   . LEU D  1 118 ? 97.457  -3.295  19.362  1.00 2.41  ? 117 LEU G N   1 
ATOM   4192  C  CA  . LEU D  1 118 ? 96.071  -3.610  19.648  1.00 2.69  ? 117 LEU G CA  1 
ATOM   4193  C  C   . LEU D  1 118 ? 95.793  -3.089  21.058  1.00 2.90  ? 117 LEU G C   1 
ATOM   4194  O  O   . LEU D  1 118 ? 96.612  -3.331  21.947  1.00 2.00  ? 117 LEU G O   1 
ATOM   4195  C  CB  . LEU D  1 118 ? 95.848  -5.106  19.628  1.00 2.00  ? 117 LEU G CB  1 
ATOM   4196  C  CG  . LEU D  1 118 ? 94.419  -5.618  19.671  1.00 2.00  ? 117 LEU G CG  1 
ATOM   4197  C  CD1 . LEU D  1 118 ? 93.611  -5.112  18.487  1.00 2.00  ? 117 LEU G CD1 1 
ATOM   4198  C  CD2 . LEU D  1 118 ? 94.467  -7.115  19.569  1.00 2.00  ? 117 LEU G CD2 1 
ATOM   4199  N  N   . VAL D  1 119 ? 94.703  -2.371  21.321  1.00 2.00  ? 118 VAL G N   1 
ATOM   4200  C  CA  . VAL D  1 119 ? 94.401  -1.871  22.637  1.00 2.00  ? 118 VAL G CA  1 
ATOM   4201  C  C   . VAL D  1 119 ? 93.055  -2.417  23.031  1.00 2.00  ? 118 VAL G C   1 
ATOM   4202  O  O   . VAL D  1 119 ? 92.188  -2.527  22.144  1.00 2.00  ? 118 VAL G O   1 
ATOM   4203  C  CB  . VAL D  1 119 ? 94.380  -0.342  22.595  1.00 2.00  ? 118 VAL G CB  1 
ATOM   4204  C  CG1 . VAL D  1 119 ? 93.875  0.272   23.875  1.00 2.00  ? 118 VAL G CG1 1 
ATOM   4205  C  CG2 . VAL D  1 119 ? 95.791  0.120   22.308  1.00 2.00  ? 118 VAL G CG2 1 
ATOM   4206  N  N   . VAL D  1 120 ? 92.872  -2.845  24.297  1.00 2.00  ? 119 VAL G N   1 
ATOM   4207  C  CA  . VAL D  1 120 ? 91.549  -3.168  24.785  1.00 2.00  ? 119 VAL G CA  1 
ATOM   4208  C  C   . VAL D  1 120 ? 91.293  -2.189  25.892  1.00 2.00  ? 119 VAL G C   1 
ATOM   4209  O  O   . VAL D  1 120 ? 92.137  -1.876  26.741  1.00 2.10  ? 119 VAL G O   1 
ATOM   4210  C  CB  . VAL D  1 120 ? 91.466  -4.610  25.244  1.00 2.00  ? 119 VAL G CB  1 
ATOM   4211  C  CG1 . VAL D  1 120 ? 92.336  -4.920  26.399  1.00 5.95  ? 119 VAL G CG1 1 
ATOM   4212  C  CG2 . VAL D  1 120 ? 90.035  -4.865  25.585  1.00 2.00  ? 119 VAL G CG2 1 
ATOM   4213  N  N   . HIS D  1 121 ? 90.133  -1.605  25.672  1.00 2.00  ? 120 HIS G N   1 
ATOM   4214  C  CA  . HIS D  1 121 ? 89.662  -0.502  26.419  1.00 2.00  ? 120 HIS G CA  1 
ATOM   4215  C  C   . HIS D  1 121 ? 88.712  -0.809  27.562  1.00 3.16  ? 120 HIS G C   1 
ATOM   4216  O  O   . HIS D  1 121 ? 88.115  -1.871  27.767  1.00 2.00  ? 120 HIS G O   1 
ATOM   4217  C  CB  . HIS D  1 121 ? 89.001  0.461   25.476  1.00 2.00  ? 120 HIS G CB  1 
ATOM   4218  C  CG  . HIS D  1 121 ? 89.906  1.280   24.575  1.00 2.00  ? 120 HIS G CG  1 
ATOM   4219  N  ND1 . HIS D  1 121 ? 90.415  2.468   24.792  1.00 2.00  ? 120 HIS G ND1 1 
ATOM   4220  C  CD2 . HIS D  1 121 ? 90.315  0.887   23.317  1.00 4.61  ? 120 HIS G CD2 1 
ATOM   4221  C  CE1 . HIS D  1 121 ? 91.096  2.795   23.727  1.00 2.34  ? 120 HIS G CE1 1 
ATOM   4222  N  NE2 . HIS D  1 121 ? 91.044  1.840   22.813  1.00 5.70  ? 120 HIS G NE2 1 
ATOM   4223  N  N   . GLU D  1 122 ? 88.576  0.259   28.331  1.00 7.04  ? 121 GLU G N   1 
ATOM   4224  C  CA  . GLU D  1 122 ? 87.866  0.288   29.586  1.00 8.00  ? 121 GLU G CA  1 
ATOM   4225  C  C   . GLU D  1 122 ? 86.390  0.152   29.450  1.00 6.99  ? 121 GLU G C   1 
ATOM   4226  O  O   . GLU D  1 122 ? 85.745  -0.631  30.145  1.00 7.40  ? 121 GLU G O   1 
ATOM   4227  C  CB  . GLU D  1 122 ? 88.187  1.562   30.265  1.00 9.82  ? 121 GLU G CB  1 
ATOM   4228  C  CG  . GLU D  1 122 ? 87.469  1.707   31.581  1.00 15.09 ? 121 GLU G CG  1 
ATOM   4229  C  CD  . GLU D  1 122 ? 87.884  2.941   32.353  1.00 18.70 ? 121 GLU G CD  1 
ATOM   4230  O  OE1 . GLU D  1 122 ? 87.885  4.076   31.795  1.00 16.63 ? 121 GLU G OE1 1 
ATOM   4231  O  OE2 . GLU D  1 122 ? 88.211  2.704   33.527  1.00 19.03 ? 121 GLU G OE2 1 
ATOM   4232  N  N   . LYS D  1 123 ? 85.923  0.945   28.509  1.00 6.87  ? 122 LYS G N   1 
ATOM   4233  C  CA  . LYS D  1 123 ? 84.523  0.953   28.169  1.00 5.50  ? 122 LYS G CA  1 
ATOM   4234  C  C   . LYS D  1 123 ? 84.196  0.413   26.785  1.00 2.86  ? 122 LYS G C   1 
ATOM   4235  O  O   . LYS D  1 123 ? 85.047  0.055   25.972  1.00 2.00  ? 122 LYS G O   1 
ATOM   4236  C  CB  . LYS D  1 123 ? 84.048  2.360   28.309  1.00 5.36  ? 122 LYS G CB  1 
ATOM   4237  C  CG  . LYS D  1 123 ? 84.083  2.724   29.792  1.00 8.21  ? 122 LYS G CG  1 
ATOM   4238  C  CD  . LYS D  1 123 ? 83.542  4.125   29.899  1.00 11.51 ? 122 LYS G CD  1 
ATOM   4239  C  CE  . LYS D  1 123 ? 84.516  5.120   29.301  1.00 11.38 ? 122 LYS G CE  1 
ATOM   4240  N  NZ  . LYS D  1 123 ? 83.819  6.344   28.935  1.00 16.18 ? 122 LYS G NZ  1 
ATOM   4241  N  N   . ALA D  1 124 ? 82.895  0.324   26.602  1.00 2.00  ? 123 ALA G N   1 
ATOM   4242  C  CA  . ALA D  1 124 ? 82.252  -0.024  25.372  1.00 2.00  ? 123 ALA G CA  1 
ATOM   4243  C  C   . ALA D  1 124 ? 82.475  1.117   24.403  1.00 2.78  ? 123 ALA G C   1 
ATOM   4244  O  O   . ALA D  1 124 ? 82.484  2.308   24.759  1.00 5.42  ? 123 ALA G O   1 
ATOM   4245  C  CB  . ALA D  1 124 ? 80.781  -0.163  25.585  1.00 2.00  ? 123 ALA G CB  1 
ATOM   4246  N  N   . ASP D  1 125 ? 82.636  0.772   23.165  1.00 2.00  ? 124 ASP G N   1 
ATOM   4247  C  CA  . ASP D  1 125 ? 82.829  1.776   22.171  1.00 2.00  ? 124 ASP G CA  1 
ATOM   4248  C  C   . ASP D  1 125 ? 81.405  1.954   21.644  1.00 2.69  ? 124 ASP G C   1 
ATOM   4249  O  O   . ASP D  1 125 ? 80.683  0.984   21.376  1.00 2.34  ? 124 ASP G O   1 
ATOM   4250  C  CB  . ASP D  1 125 ? 83.818  1.144   21.257  1.00 2.85  ? 124 ASP G CB  1 
ATOM   4251  C  CG  . ASP D  1 125 ? 83.992  1.625   19.843  1.00 2.98  ? 124 ASP G CG  1 
ATOM   4252  O  OD1 . ASP D  1 125 ? 83.514  2.692   19.495  1.00 4.60  ? 124 ASP G OD1 1 
ATOM   4253  O  OD2 . ASP D  1 125 ? 84.639  0.919   19.082  1.00 3.56  ? 124 ASP G OD2 1 
ATOM   4254  N  N   . ASP D  1 126 ? 80.945  3.184   21.471  1.00 2.00  ? 125 ASP G N   1 
ATOM   4255  C  CA  . ASP D  1 126 ? 79.624  3.370   20.967  1.00 2.00  ? 125 ASP G CA  1 
ATOM   4256  C  C   . ASP D  1 126 ? 79.483  3.384   19.455  1.00 2.00  ? 125 ASP G C   1 
ATOM   4257  O  O   . ASP D  1 126 ? 78.461  3.722   18.865  1.00 2.01  ? 125 ASP G O   1 
ATOM   4258  C  CB  . ASP D  1 126 ? 79.090  4.635   21.633  1.00 2.62  ? 125 ASP G CB  1 
ATOM   4259  C  CG  . ASP D  1 126 ? 79.744  5.973   21.386  1.00 2.98  ? 125 ASP G CG  1 
ATOM   4260  O  OD1 . ASP D  1 126 ? 80.377  6.157   20.358  1.00 5.95  ? 125 ASP G OD1 1 
ATOM   4261  O  OD2 . ASP D  1 126 ? 79.570  6.849   22.219  1.00 2.00  ? 125 ASP G OD2 1 
ATOM   4262  N  N   . LEU D  1 127 ? 80.576  3.020   18.806  1.00 2.17  ? 126 LEU G N   1 
ATOM   4263  C  CA  . LEU D  1 127 ? 80.728  2.854   17.370  1.00 2.23  ? 126 LEU G CA  1 
ATOM   4264  C  C   . LEU D  1 127 ? 80.407  4.129   16.631  1.00 2.00  ? 126 LEU G C   1 
ATOM   4265  O  O   . LEU D  1 127 ? 79.957  4.105   15.489  1.00 3.16  ? 126 LEU G O   1 
ATOM   4266  C  CB  . LEU D  1 127 ? 79.828  1.673   16.850  1.00 2.37  ? 126 LEU G CB  1 
ATOM   4267  C  CG  . LEU D  1 127 ? 79.757  0.311   17.581  1.00 2.00  ? 126 LEU G CG  1 
ATOM   4268  C  CD1 . LEU D  1 127 ? 78.428  -0.301  17.288  1.00 2.00  ? 126 LEU G CD1 1 
ATOM   4269  C  CD2 . LEU D  1 127 ? 80.909  -0.570  17.209  1.00 2.00  ? 126 LEU G CD2 1 
ATOM   4270  N  N   . GLY D  1 128 ? 80.670  5.250   17.297  1.00 2.00  ? 127 GLY G N   1 
ATOM   4271  C  CA  . GLY D  1 128 ? 80.545  6.509   16.617  1.00 2.00  ? 127 GLY G CA  1 
ATOM   4272  C  C   . GLY D  1 128 ? 79.136  7.044   16.596  1.00 2.62  ? 127 GLY G C   1 
ATOM   4273  O  O   . GLY D  1 128 ? 78.852  8.088   16.016  1.00 2.41  ? 127 GLY G O   1 
ATOM   4274  N  N   . LYS D  1 129 ? 78.273  6.396   17.358  1.00 2.55  ? 128 LYS G N   1 
ATOM   4275  C  CA  . LYS D  1 129 ? 76.891  6.780   17.399  1.00 3.37  ? 128 LYS G CA  1 
ATOM   4276  C  C   . LYS D  1 129 ? 76.537  7.519   18.682  1.00 2.70  ? 128 LYS G C   1 
ATOM   4277  O  O   . LYS D  1 129 ? 75.363  7.580   19.043  1.00 2.00  ? 128 LYS G O   1 
ATOM   4278  C  CB  . LYS D  1 129 ? 76.080  5.491   17.225  1.00 4.53  ? 128 LYS G CB  1 
ATOM   4279  C  CG  . LYS D  1 129 ? 76.124  4.803   15.849  1.00 6.15  ? 128 LYS G CG  1 
ATOM   4280  C  CD  . LYS D  1 129 ? 75.401  3.428   15.886  1.00 12.49 ? 128 LYS G CD  1 
ATOM   4281  C  CE  . LYS D  1 129 ? 73.860  3.533   16.043  1.00 13.45 ? 128 LYS G CE  1 
ATOM   4282  N  NZ  . LYS D  1 129 ? 73.169  2.263   16.212  1.00 10.68 ? 128 LYS G NZ  1 
ATOM   4283  N  N   . GLY D  1 130 ? 77.515  8.120   19.369  1.00 2.00  ? 129 GLY G N   1 
ATOM   4284  C  CA  . GLY D  1 130 ? 77.237  8.755   20.649  1.00 2.00  ? 129 GLY G CA  1 
ATOM   4285  C  C   . GLY D  1 130 ? 77.050  10.259  20.535  1.00 2.00  ? 129 GLY G C   1 
ATOM   4286  O  O   . GLY D  1 130 ? 77.011  10.946  21.545  1.00 3.06  ? 129 GLY G O   1 
ATOM   4287  N  N   . GLY D  1 131 ? 77.051  10.850  19.353  1.00 2.00  ? 130 GLY G N   1 
ATOM   4288  C  CA  . GLY D  1 131 ? 76.706  12.241  19.150  1.00 2.00  ? 130 GLY G CA  1 
ATOM   4289  C  C   . GLY D  1 131 ? 77.516  13.313  19.812  1.00 2.00  ? 130 GLY G C   1 
ATOM   4290  O  O   . GLY D  1 131 ? 77.033  14.403  20.058  1.00 2.64  ? 130 GLY G O   1 
ATOM   4291  N  N   . ASN D  1 132 ? 78.763  13.111  20.076  1.00 2.00  ? 131 ASN G N   1 
ATOM   4292  C  CA  . ASN D  1 132 ? 79.579  14.092  20.775  1.00 2.27  ? 131 ASN G CA  1 
ATOM   4293  C  C   . ASN D  1 132 ? 80.949  14.026  20.154  1.00 2.01  ? 131 ASN G C   1 
ATOM   4294  O  O   . ASN D  1 132 ? 81.208  13.103  19.392  1.00 5.91  ? 131 ASN G O   1 
ATOM   4295  C  CB  . ASN D  1 132 ? 79.630  13.770  22.280  1.00 3.10  ? 131 ASN G CB  1 
ATOM   4296  C  CG  . ASN D  1 132 ? 80.495  12.613  22.749  1.00 2.00  ? 131 ASN G CG  1 
ATOM   4297  O  OD1 . ASN D  1 132 ? 80.863  11.746  21.970  1.00 2.38  ? 131 ASN G OD1 1 
ATOM   4298  N  ND2 . ASN D  1 132 ? 80.912  12.551  24.002  1.00 2.00  ? 131 ASN G ND2 1 
ATOM   4299  N  N   . GLU D  1 133 ? 81.857  14.962  20.358  1.00 5.31  ? 132 GLU G N   1 
ATOM   4300  C  CA  . GLU D  1 133 ? 83.146  14.939  19.672  1.00 5.96  ? 132 GLU G CA  1 
ATOM   4301  C  C   . GLU D  1 133 ? 83.860  13.618  19.840  1.00 6.53  ? 132 GLU G C   1 
ATOM   4302  O  O   . GLU D  1 133 ? 84.293  13.002  18.876  1.00 8.48  ? 132 GLU G O   1 
ATOM   4303  C  CB  . GLU D  1 133 ? 84.084  15.973  20.192  1.00 9.46  ? 132 GLU G CB  1 
ATOM   4304  C  CG  . GLU D  1 133 ? 84.194  17.234  19.331  1.00 22.31 ? 132 GLU G CG  1 
ATOM   4305  C  CD  . GLU D  1 133 ? 84.795  18.418  20.098  1.00 27.10 ? 132 GLU G CD  1 
ATOM   4306  O  OE1 . GLU D  1 133 ? 84.032  19.119  20.791  1.00 25.88 ? 132 GLU G OE1 1 
ATOM   4307  O  OE2 . GLU D  1 133 ? 86.023  18.611  19.984  1.00 32.03 ? 132 GLU G OE2 1 
ATOM   4308  N  N   . GLU D  1 134 ? 83.922  13.107  21.055  1.00 4.29  ? 133 GLU G N   1 
ATOM   4309  C  CA  . GLU D  1 134 ? 84.737  11.968  21.342  1.00 4.71  ? 133 GLU G CA  1 
ATOM   4310  C  C   . GLU D  1 134 ? 84.316  10.658  20.665  1.00 3.70  ? 133 GLU G C   1 
ATOM   4311  O  O   . GLU D  1 134 ? 85.107  9.773   20.334  1.00 2.59  ? 133 GLU G O   1 
ATOM   4312  C  CB  . GLU D  1 134 ? 84.685  12.002  22.809  1.00 7.95  ? 133 GLU G CB  1 
ATOM   4313  C  CG  . GLU D  1 134 ? 85.665  11.121  23.569  1.00 15.33 ? 133 GLU G CG  1 
ATOM   4314  C  CD  . GLU D  1 134 ? 87.128  11.378  23.256  1.00 19.67 ? 133 GLU G CD  1 
ATOM   4315  O  OE1 . GLU D  1 134 ? 87.546  12.535  23.055  1.00 23.39 ? 133 GLU G OE1 1 
ATOM   4316  O  OE2 . GLU D  1 134 ? 87.829  10.373  23.208  1.00 18.40 ? 133 GLU G OE2 1 
ATOM   4317  N  N   . SER D  1 135 ? 83.041  10.562  20.382  1.00 2.02  ? 134 SER G N   1 
ATOM   4318  C  CA  . SER D  1 135 ? 82.489  9.422   19.763  1.00 2.00  ? 134 SER G CA  1 
ATOM   4319  C  C   . SER D  1 135 ? 83.130  9.061   18.426  1.00 3.42  ? 134 SER G C   1 
ATOM   4320  O  O   . SER D  1 135 ? 83.362  7.864   18.159  1.00 5.53  ? 134 SER G O   1 
ATOM   4321  C  CB  . SER D  1 135 ? 81.049  9.737   19.668  1.00 2.00  ? 134 SER G CB  1 
ATOM   4322  O  OG  . SER D  1 135 ? 80.307  8.614   19.266  1.00 2.00  ? 134 SER G OG  1 
ATOM   4323  N  N   . THR D  1 136 ? 83.446  10.071  17.627  1.00 4.26  ? 135 THR G N   1 
ATOM   4324  C  CA  . THR D  1 136 ? 83.981  9.956   16.270  1.00 2.68  ? 135 THR G CA  1 
ATOM   4325  C  C   . THR D  1 136 ? 85.488  9.965   16.164  1.00 2.00  ? 135 THR G C   1 
ATOM   4326  O  O   . THR D  1 136 ? 86.036  9.935   15.056  1.00 2.00  ? 135 THR G O   1 
ATOM   4327  C  CB  . THR D  1 136 ? 83.363  11.102  15.451  1.00 6.94  ? 135 THR G CB  1 
ATOM   4328  O  OG1 . THR D  1 136 ? 83.385  12.289  16.264  1.00 3.44  ? 135 THR G OG1 1 
ATOM   4329  C  CG2 . THR D  1 136 ? 81.956  10.711  14.967  1.00 6.15  ? 135 THR G CG2 1 
ATOM   4330  N  N   . LYS D  1 137 ? 86.130  9.975   17.345  1.00 2.00  ? 136 LYS G N   1 
ATOM   4331  C  CA  . LYS D  1 137 ? 87.556  9.911   17.451  1.00 2.00  ? 136 LYS G CA  1 
ATOM   4332  C  C   . LYS D  1 137 ? 87.832  8.614   18.165  1.00 2.00  ? 136 LYS G C   1 
ATOM   4333  O  O   . LYS D  1 137 ? 88.566  7.808   17.617  1.00 2.58  ? 136 LYS G O   1 
ATOM   4334  C  CB  . LYS D  1 137 ? 88.119  11.010  18.281  1.00 2.00  ? 136 LYS G CB  1 
ATOM   4335  C  CG  . LYS D  1 137 ? 87.854  12.481  17.956  1.00 5.06  ? 136 LYS G CG  1 
ATOM   4336  C  CD  . LYS D  1 137 ? 88.901  13.176  18.809  1.00 10.96 ? 136 LYS G CD  1 
ATOM   4337  C  CE  . LYS D  1 137 ? 88.840  14.691  18.939  1.00 16.12 ? 136 LYS G CE  1 
ATOM   4338  N  NZ  . LYS D  1 137 ? 88.493  15.035  20.320  1.00 21.63 ? 136 LYS G NZ  1 
ATOM   4339  N  N   . THR D  1 138 ? 87.303  8.316   19.346  1.00 2.00  ? 137 THR G N   1 
ATOM   4340  C  CA  . THR D  1 138 ? 87.586  7.068   20.014  1.00 2.00  ? 137 THR G CA  1 
ATOM   4341  C  C   . THR D  1 138 ? 86.409  6.188   20.329  1.00 2.00  ? 137 THR G C   1 
ATOM   4342  O  O   . THR D  1 138 ? 86.554  5.152   21.000  1.00 2.00  ? 137 THR G O   1 
ATOM   4343  C  CB  . THR D  1 138 ? 88.274  7.307   21.335  1.00 2.00  ? 137 THR G CB  1 
ATOM   4344  O  OG1 . THR D  1 138 ? 87.343  7.852   22.246  1.00 2.00  ? 137 THR G OG1 1 
ATOM   4345  C  CG2 . THR D  1 138 ? 89.387  8.261   21.199  1.00 2.00  ? 137 THR G CG2 1 
ATOM   4346  N  N   . GLY D  1 139 ? 85.205  6.650   20.000  1.00 2.41  ? 138 GLY G N   1 
ATOM   4347  C  CA  . GLY D  1 139 ? 84.011  5.908   20.316  1.00 2.00  ? 138 GLY G CA  1 
ATOM   4348  C  C   . GLY D  1 139 ? 83.697  6.042   21.795  1.00 2.00  ? 138 GLY G C   1 
ATOM   4349  O  O   . GLY D  1 139 ? 82.848  5.308   22.279  1.00 2.00  ? 138 GLY G O   1 
ATOM   4350  N  N   . ASN D  1 140 ? 84.304  6.942   22.562  1.00 2.00  ? 139 ASN G N   1 
ATOM   4351  C  CA  . ASN D  1 140 ? 84.037  7.045   23.998  1.00 2.52  ? 139 ASN G CA  1 
ATOM   4352  C  C   . ASN D  1 140 ? 84.380  5.747   24.752  1.00 3.36  ? 139 ASN G C   1 
ATOM   4353  O  O   . ASN D  1 140 ? 83.776  5.399   25.770  1.00 2.00  ? 139 ASN G O   1 
ATOM   4354  C  CB  . ASN D  1 140 ? 82.565  7.402   24.301  1.00 2.00  ? 139 ASN G CB  1 
ATOM   4355  C  CG  . ASN D  1 140 ? 82.175  8.788   23.867  1.00 2.00  ? 139 ASN G CG  1 
ATOM   4356  O  OD1 . ASN D  1 140 ? 82.611  9.766   24.436  1.00 7.68  ? 139 ASN G OD1 1 
ATOM   4357  N  ND2 . ASN D  1 140 ? 81.361  9.068   22.882  1.00 2.00  ? 139 ASN G ND2 1 
ATOM   4358  N  N   . ALA D  1 141 ? 85.402  5.022   24.267  1.00 2.00  ? 140 ALA G N   1 
ATOM   4359  C  CA  . ALA D  1 141 ? 85.815  3.791   24.927  1.00 3.21  ? 140 ALA G CA  1 
ATOM   4360  C  C   . ALA D  1 141 ? 86.728  3.945   26.152  1.00 4.20  ? 140 ALA G C   1 
ATOM   4361  O  O   . ALA D  1 141 ? 87.028  2.982   26.891  1.00 5.37  ? 140 ALA G O   1 
ATOM   4362  C  CB  . ALA D  1 141 ? 86.483  2.874   23.900  1.00 2.00  ? 140 ALA G CB  1 
ATOM   4363  N  N   . GLY D  1 142 ? 87.117  5.185   26.467  1.00 4.32  ? 141 GLY G N   1 
ATOM   4364  C  CA  . GLY D  1 142 ? 87.924  5.475   27.628  1.00 2.00  ? 141 GLY G CA  1 
ATOM   4365  C  C   . GLY D  1 142 ? 89.331  4.950   27.494  1.00 5.85  ? 141 GLY G C   1 
ATOM   4366  O  O   . GLY D  1 142 ? 89.921  4.887   26.404  1.00 8.73  ? 141 GLY G O   1 
ATOM   4367  N  N   . SER D  1 143 ? 89.766  4.486   28.658  1.00 7.78  ? 142 SER G N   1 
ATOM   4368  C  CA  . SER D  1 143 ? 91.124  4.025   28.924  1.00 7.78  ? 142 SER G CA  1 
ATOM   4369  C  C   . SER D  1 143 ? 91.514  2.743   28.241  1.00 6.46  ? 142 SER G C   1 
ATOM   4370  O  O   . SER D  1 143 ? 90.654  1.912   27.956  1.00 6.91  ? 142 SER G O   1 
ATOM   4371  C  CB  . SER D  1 143 ? 91.315  3.823   30.408  1.00 6.98  ? 142 SER G CB  1 
ATOM   4372  O  OG  . SER D  1 143 ? 91.411  5.127   30.927  1.00 15.32 ? 142 SER G OG  1 
ATOM   4373  N  N   . ARG D  1 144 ? 92.832  2.625   28.099  1.00 5.45  ? 143 ARG G N   1 
ATOM   4374  C  CA  . ARG D  1 144 ? 93.582  1.577   27.464  1.00 2.00  ? 143 ARG G CA  1 
ATOM   4375  C  C   . ARG D  1 144 ? 93.922  0.647   28.596  1.00 2.00  ? 143 ARG G C   1 
ATOM   4376  O  O   . ARG D  1 144 ? 94.876  0.856   29.331  1.00 3.38  ? 143 ARG G O   1 
ATOM   4377  C  CB  . ARG D  1 144 ? 94.804  2.219   26.874  1.00 2.00  ? 143 ARG G CB  1 
ATOM   4378  C  CG  . ARG D  1 144 ? 94.463  3.318   25.922  1.00 2.00  ? 143 ARG G CG  1 
ATOM   4379  C  CD  . ARG D  1 144 ? 95.650  3.971   25.276  1.00 3.62  ? 143 ARG G CD  1 
ATOM   4380  N  NE  . ARG D  1 144 ? 95.054  4.860   24.305  1.00 7.52  ? 143 ARG G NE  1 
ATOM   4381  C  CZ  . ARG D  1 144 ? 95.702  5.405   23.281  1.00 5.49  ? 143 ARG G CZ  1 
ATOM   4382  N  NH1 . ARG D  1 144 ? 97.009  5.265   23.041  1.00 7.57  ? 143 ARG G NH1 1 
ATOM   4383  N  NH2 . ARG D  1 144 ? 94.982  6.165   22.491  1.00 5.69  ? 143 ARG G NH2 1 
ATOM   4384  N  N   . LEU D  1 145 ? 93.207  -0.398  28.875  1.00 3.16  ? 144 LEU G N   1 
ATOM   4385  C  CA  . LEU D  1 145 ? 93.552  -1.169  30.035  1.00 2.00  ? 144 LEU G CA  1 
ATOM   4386  C  C   . LEU D  1 145 ? 94.752  -2.037  29.748  1.00 2.91  ? 144 LEU G C   1 
ATOM   4387  O  O   . LEU D  1 145 ? 95.566  -2.297  30.643  1.00 5.51  ? 144 LEU G O   1 
ATOM   4388  C  CB  . LEU D  1 145 ? 92.386  -1.968  30.376  1.00 2.00  ? 144 LEU G CB  1 
ATOM   4389  C  CG  . LEU D  1 145 ? 91.182  -1.147  30.684  1.00 2.00  ? 144 LEU G CG  1 
ATOM   4390  C  CD1 . LEU D  1 145 ? 90.072  -2.149  30.851  1.00 2.19  ? 144 LEU G CD1 1 
ATOM   4391  C  CD2 . LEU D  1 145 ? 91.398  -0.227  31.868  1.00 2.00  ? 144 LEU G CD2 1 
ATOM   4392  N  N   . ALA D  1 146 ? 94.888  -2.470  28.505  1.00 2.02  ? 145 ALA G N   1 
ATOM   4393  C  CA  . ALA D  1 146 ? 95.985  -3.329  28.127  1.00 2.00  ? 145 ALA G CA  1 
ATOM   4394  C  C   . ALA D  1 146 ? 96.256  -3.239  26.628  1.00 2.04  ? 145 ALA G C   1 
ATOM   4395  O  O   . ALA D  1 146 ? 95.329  -3.045  25.838  1.00 2.00  ? 145 ALA G O   1 
ATOM   4396  C  CB  . ALA D  1 146 ? 95.630  -4.755  28.499  1.00 2.00  ? 145 ALA G CB  1 
ATOM   4397  N  N   . CYS D  1 147 ? 97.507  -3.337  26.199  1.00 2.40  ? 146 CYS G N   1 
ATOM   4398  C  CA  . CYS D  1 147 ? 97.830  -3.326  24.793  1.00 2.00  ? 146 CYS G CA  1 
ATOM   4399  C  C   . CYS D  1 147 ? 99.064  -4.158  24.495  1.00 2.00  ? 146 CYS G C   1 
ATOM   4400  O  O   . CYS D  1 147 ? 99.691  -4.660  25.416  1.00 2.00  ? 146 CYS G O   1 
ATOM   4401  C  CB  . CYS D  1 147 ? 98.064  -1.939  24.395  1.00 2.94  ? 146 CYS G CB  1 
ATOM   4402  S  SG  . CYS D  1 147 ? 99.497  -1.382  25.297  1.00 2.03  ? 146 CYS G SG  1 
ATOM   4403  N  N   . GLY D  1 148 ? 99.421  -4.430  23.247  1.00 2.66  ? 147 GLY G N   1 
ATOM   4404  C  CA  . GLY D  1 148 ? 100.637 -5.143  22.897  1.00 2.00  ? 147 GLY G CA  1 
ATOM   4405  C  C   . GLY D  1 148 ? 100.887 -4.912  21.413  1.00 2.54  ? 147 GLY G C   1 
ATOM   4406  O  O   . GLY D  1 148 ? 99.920  -4.689  20.686  1.00 2.00  ? 147 GLY G O   1 
ATOM   4407  N  N   . VAL D  1 149 ? 102.147 -4.941  20.941  1.00 3.10  ? 148 VAL G N   1 
ATOM   4408  C  CA  . VAL D  1 149 ? 102.486 -4.714  19.546  1.00 2.00  ? 148 VAL G CA  1 
ATOM   4409  C  C   . VAL D  1 149 ? 102.145 -5.944  18.735  1.00 2.00  ? 148 VAL G C   1 
ATOM   4410  O  O   . VAL D  1 149 ? 102.337 -7.088  19.158  1.00 2.00  ? 148 VAL G O   1 
ATOM   4411  C  CB  . VAL D  1 149 ? 103.993 -4.371  19.429  1.00 2.00  ? 148 VAL G CB  1 
ATOM   4412  C  CG1 . VAL D  1 149 ? 104.324 -3.952  18.009  1.00 2.00  ? 148 VAL G CG1 1 
ATOM   4413  C  CG2 . VAL D  1 149 ? 104.348 -3.203  20.346  1.00 2.47  ? 148 VAL G CG2 1 
ATOM   4414  N  N   . ILE D  1 150 ? 101.635 -5.763  17.539  1.00 2.17  ? 149 ILE G N   1 
ATOM   4415  C  CA  . ILE D  1 150 ? 101.272 -6.897  16.685  1.00 2.00  ? 149 ILE G CA  1 
ATOM   4416  C  C   . ILE D  1 150 ? 102.493 -7.343  15.929  1.00 2.00  ? 149 ILE G C   1 
ATOM   4417  O  O   . ILE D  1 150 ? 103.038 -6.591  15.137  1.00 2.00  ? 149 ILE G O   1 
ATOM   4418  C  CB  . ILE D  1 150 ? 100.141 -6.446  15.742  1.00 2.00  ? 149 ILE G CB  1 
ATOM   4419  C  CG1 . ILE D  1 150 ? 99.011  -5.844  16.557  1.00 2.00  ? 149 ILE G CG1 1 
ATOM   4420  C  CG2 . ILE D  1 150 ? 99.614  -7.630  14.960  1.00 2.00  ? 149 ILE G CG2 1 
ATOM   4421  C  CD1 . ILE D  1 150 ? 97.798  -5.279  15.840  1.00 2.00  ? 149 ILE G CD1 1 
ATOM   4422  N  N   . GLY D  1 151 ? 102.964 -8.540  16.142  1.00 2.00  ? 150 GLY G N   1 
ATOM   4423  C  CA  . GLY D  1 151 ? 104.116 -9.061  15.464  1.00 2.00  ? 150 GLY G CA  1 
ATOM   4424  C  C   . GLY D  1 151 ? 103.775 -10.263 14.629  1.00 2.00  ? 150 GLY G C   1 
ATOM   4425  O  O   . GLY D  1 151 ? 102.715 -10.848 14.746  1.00 2.00  ? 150 GLY G O   1 
ATOM   4426  N  N   . ILE D  1 152 ? 104.695 -10.625 13.743  1.00 2.89  ? 151 ILE G N   1 
ATOM   4427  C  CA  . ILE D  1 152 ? 104.569 -11.712 12.802  1.00 2.00  ? 151 ILE G CA  1 
ATOM   4428  C  C   . ILE D  1 152 ? 104.656 -13.002 13.570  1.00 2.00  ? 151 ILE G C   1 
ATOM   4429  O  O   . ILE D  1 152 ? 105.522 -13.146 14.428  1.00 3.44  ? 151 ILE G O   1 
ATOM   4430  C  CB  . ILE D  1 152 ? 105.709 -11.607 11.754  1.00 2.00  ? 151 ILE G CB  1 
ATOM   4431  C  CG1 . ILE D  1 152 ? 105.612 -10.258 11.100  1.00 2.00  ? 151 ILE G CG1 1 
ATOM   4432  C  CG2 . ILE D  1 152 ? 105.591 -12.646 10.648  1.00 2.00  ? 151 ILE G CG2 1 
ATOM   4433  C  CD1 . ILE D  1 152 ? 106.834 -9.858  10.262  1.00 2.00  ? 151 ILE G CD1 1 
ATOM   4434  N  N   . ALA D  1 153 ? 103.816 -13.968 13.317  1.00 5.13  ? 152 ALA G N   1 
ATOM   4435  C  CA  . ALA D  1 153 ? 103.967 -15.236 14.005  1.00 9.29  ? 152 ALA G CA  1 
ATOM   4436  C  C   . ALA D  1 153 ? 104.090 -16.301 12.941  1.00 12.55 ? 152 ALA G C   1 
ATOM   4437  O  O   . ALA D  1 153 ? 104.016 -16.034 11.735  1.00 13.33 ? 152 ALA G O   1 
ATOM   4438  C  CB  . ALA D  1 153 ? 102.748 -15.513 14.867  1.00 7.71  ? 152 ALA G CB  1 
ATOM   4439  N  N   . GLN D  1 154 ? 104.365 -17.487 13.455  1.00 19.17 ? 153 GLN G N   1 
ATOM   4440  C  CA  . GLN D  1 154 ? 104.444 -18.743 12.718  1.00 24.82 ? 153 GLN G CA  1 
ATOM   4441  C  C   . GLN D  1 154 ? 103.032 -19.320 12.766  1.00 28.15 ? 153 GLN G C   1 
ATOM   4442  O  O   . GLN D  1 154 ? 102.633 -19.889 11.747  1.00 33.09 ? 153 GLN G O   1 
ATOM   4443  C  CB  . GLN D  1 154 ? 105.413 -19.712 13.408  1.00 27.06 ? 153 GLN G CB  1 
ATOM   4444  C  CG  . GLN D  1 154 ? 105.650 -21.116 12.844  1.00 33.09 ? 153 GLN G CG  1 
ATOM   4445  C  CD  . GLN D  1 154 ? 106.691 -21.158 11.727  1.00 38.22 ? 153 GLN G CD  1 
ATOM   4446  O  OE1 . GLN D  1 154 ? 107.786 -21.720 11.876  1.00 38.79 ? 153 GLN G OE1 1 
ATOM   4447  N  NE2 . GLN D  1 154 ? 106.420 -20.549 10.569  1.00 40.11 ? 153 GLN G NE2 1 
ATOM   4448  O  OXT . GLN D  1 154 ? 102.358 -19.200 13.813  1.00 29.47 ? 153 GLN G OXT 1 
HETATM 4449  C  C   . ACE E  1 1   ? 58.787  -31.490 5.526   1.00 31.49 ? 0   ACE C C   1 
HETATM 4450  O  O   . ACE E  1 1   ? 59.972  -31.120 5.629   1.00 32.48 ? 0   ACE C O   1 
HETATM 4451  C  CH3 . ACE E  1 1   ? 58.124  -31.499 4.150   1.00 31.88 ? 0   ACE C CH3 1 
ATOM   4452  N  N   . ALA E  1 2   ? 58.035  -31.785 6.602   1.00 28.66 ? 1   ALA C N   1 
ATOM   4453  C  CA  . ALA E  1 2   ? 58.657  -31.990 7.911   1.00 24.99 ? 1   ALA C CA  1 
ATOM   4454  C  C   . ALA E  1 2   ? 58.680  -33.511 8.003   1.00 19.72 ? 1   ALA C C   1 
ATOM   4455  O  O   . ALA E  1 2   ? 57.735  -34.156 7.599   1.00 20.49 ? 1   ALA C O   1 
ATOM   4456  C  CB  . ALA E  1 2   ? 57.808  -31.447 9.068   1.00 25.81 ? 1   ALA C CB  1 
ATOM   4457  N  N   . THR E  1 3   ? 59.736  -34.157 8.410   1.00 16.50 ? 2   THR C N   1 
ATOM   4458  C  CA  . THR E  1 3   ? 59.698  -35.576 8.557   1.00 14.02 ? 2   THR C CA  1 
ATOM   4459  C  C   . THR E  1 3   ? 59.250  -35.859 9.966   1.00 12.08 ? 2   THR C C   1 
ATOM   4460  O  O   . THR E  1 3   ? 58.717  -36.934 10.195  1.00 11.09 ? 2   THR C O   1 
ATOM   4461  C  CB  . THR E  1 3   ? 61.089  -36.136 8.263   1.00 16.07 ? 2   THR C CB  1 
ATOM   4462  O  OG1 . THR E  1 3   ? 62.114  -35.285 8.807   1.00 19.12 ? 2   THR C OG1 1 
ATOM   4463  C  CG2 . THR E  1 3   ? 61.270  -36.204 6.753   1.00 19.55 ? 2   THR C CG2 1 
ATOM   4464  N  N   . LYS E  1 4   ? 59.464  -34.976 10.954  1.00 10.28 ? 3   LYS C N   1 
ATOM   4465  C  CA  . LYS E  1 4   ? 59.042  -35.245 12.312  1.00 8.19  ? 3   LYS C CA  1 
ATOM   4466  C  C   . LYS E  1 4   ? 58.346  -34.092 12.961  1.00 5.98  ? 3   LYS C C   1 
ATOM   4467  O  O   . LYS E  1 4   ? 58.597  -32.925 12.641  1.00 5.14  ? 3   LYS C O   1 
ATOM   4468  C  CB  . LYS E  1 4   ? 60.181  -35.582 13.234  1.00 12.80 ? 3   LYS C CB  1 
ATOM   4469  C  CG  . LYS E  1 4   ? 60.938  -36.835 12.872  1.00 16.01 ? 3   LYS C CG  1 
ATOM   4470  C  CD  . LYS E  1 4   ? 61.324  -37.748 14.021  1.00 22.84 ? 3   LYS C CD  1 
ATOM   4471  C  CE  . LYS E  1 4   ? 62.109  -38.838 13.218  1.00 29.79 ? 3   LYS C CE  1 
ATOM   4472  N  NZ  . LYS E  1 4   ? 62.470  -40.119 13.855  1.00 29.42 ? 3   LYS C NZ  1 
ATOM   4473  N  N   . ALA E  1 5   ? 57.489  -34.462 13.911  1.00 4.07  ? 4   ALA C N   1 
ATOM   4474  C  CA  . ALA E  1 5   ? 56.736  -33.510 14.697  1.00 2.28  ? 4   ALA C CA  1 
ATOM   4475  C  C   . ALA E  1 5   ? 56.487  -34.117 16.074  1.00 2.00  ? 4   ALA C C   1 
ATOM   4476  O  O   . ALA E  1 5   ? 56.817  -35.283 16.319  1.00 2.00  ? 4   ALA C O   1 
ATOM   4477  C  CB  . ALA E  1 5   ? 55.400  -33.167 14.006  1.00 2.07  ? 4   ALA C CB  1 
ATOM   4478  N  N   . VAL E  1 6   ? 55.998  -33.336 17.024  1.00 2.00  ? 5   VAL C N   1 
ATOM   4479  C  CA  . VAL E  1 6   ? 55.782  -33.776 18.390  1.00 2.12  ? 5   VAL C CA  1 
ATOM   4480  C  C   . VAL E  1 6   ? 54.644  -32.937 18.912  1.00 2.00  ? 5   VAL C C   1 
ATOM   4481  O  O   . VAL E  1 6   ? 54.236  -32.012 18.204  1.00 3.66  ? 5   VAL C O   1 
ATOM   4482  C  CB  . VAL E  1 6   ? 57.104  -33.559 19.168  1.00 3.15  ? 5   VAL C CB  1 
ATOM   4483  C  CG1 . VAL E  1 6   ? 57.219  -32.162 19.694  1.00 4.03  ? 5   VAL C CG1 1 
ATOM   4484  C  CG2 . VAL E  1 6   ? 57.169  -34.533 20.317  1.00 2.04  ? 5   VAL C CG2 1 
ATOM   4485  N  N   . ALA E  1 7   ? 54.059  -33.247 20.047  1.00 2.34  ? 6   ALA C N   1 
ATOM   4486  C  CA  . ALA E  1 7   ? 53.040  -32.428 20.678  1.00 2.00  ? 6   ALA C CA  1 
ATOM   4487  C  C   . ALA E  1 7   ? 53.004  -32.937 22.085  1.00 2.00  ? 6   ALA C C   1 
ATOM   4488  O  O   . ALA E  1 7   ? 52.998  -34.142 22.310  1.00 2.00  ? 6   ALA C O   1 
ATOM   4489  C  CB  . ALA E  1 7   ? 51.651  -32.641 20.156  1.00 2.00  ? 6   ALA C CB  1 
ATOM   4490  N  N   . VAL E  1 8   ? 53.175  -31.992 22.997  1.00 2.59  ? 7   VAL C N   1 
ATOM   4491  C  CA  . VAL E  1 8   ? 53.115  -32.236 24.420  1.00 2.07  ? 7   VAL C CA  1 
ATOM   4492  C  C   . VAL E  1 8   ? 51.689  -31.886 24.831  1.00 2.00  ? 7   VAL C C   1 
ATOM   4493  O  O   . VAL E  1 8   ? 51.174  -30.786 24.642  1.00 2.00  ? 7   VAL C O   1 
ATOM   4494  C  CB  . VAL E  1 8   ? 54.171  -31.348 25.118  1.00 2.00  ? 7   VAL C CB  1 
ATOM   4495  C  CG1 . VAL E  1 8   ? 54.133  -31.643 26.603  1.00 2.00  ? 7   VAL C CG1 1 
ATOM   4496  C  CG2 . VAL E  1 8   ? 55.566  -31.634 24.612  1.00 2.00  ? 7   VAL C CG2 1 
ATOM   4497  N  N   . LEU E  1 9   ? 50.993  -32.963 25.137  1.00 2.53  ? 8   LEU C N   1 
ATOM   4498  C  CA  . LEU E  1 9   ? 49.637  -32.896 25.632  1.00 2.27  ? 8   LEU C CA  1 
ATOM   4499  C  C   . LEU E  1 9   ? 49.702  -32.581 27.095  1.00 2.42  ? 8   LEU C C   1 
ATOM   4500  O  O   . LEU E  1 9   ? 50.331  -33.281 27.904  1.00 2.00  ? 8   LEU C O   1 
ATOM   4501  C  CB  . LEU E  1 9   ? 48.898  -34.206 25.509  1.00 2.29  ? 8   LEU C CB  1 
ATOM   4502  C  CG  . LEU E  1 9   ? 48.096  -34.469 24.242  1.00 4.62  ? 8   LEU C CG  1 
ATOM   4503  C  CD1 . LEU E  1 9   ? 48.752  -33.817 23.067  1.00 2.08  ? 8   LEU C CD1 1 
ATOM   4504  C  CD2 . LEU E  1 9   ? 48.017  -35.968 23.983  1.00 2.00  ? 8   LEU C CD2 1 
ATOM   4505  N  N   . LYS E  1 10  ? 49.052  -31.473 27.392  1.00 2.18  ? 9   LYS C N   1 
ATOM   4506  C  CA  . LYS E  1 10  ? 48.870  -31.027 28.748  1.00 4.72  ? 9   LYS C CA  1 
ATOM   4507  C  C   . LYS E  1 10  ? 47.475  -30.477 28.828  1.00 5.49  ? 9   LYS C C   1 
ATOM   4508  O  O   . LYS E  1 10  ? 46.873  -30.171 27.810  1.00 7.73  ? 9   LYS C O   1 
ATOM   4509  C  CB  . LYS E  1 10  ? 49.885  -29.981 29.111  1.00 4.79  ? 9   LYS C CB  1 
ATOM   4510  C  CG  . LYS E  1 10  ? 51.036  -30.780 29.668  1.00 11.46 ? 9   LYS C CG  1 
ATOM   4511  C  CD  . LYS E  1 10  ? 52.230  -29.990 30.200  1.00 21.99 ? 9   LYS C CD  1 
ATOM   4512  C  CE  . LYS E  1 10  ? 53.398  -30.920 30.655  1.00 25.86 ? 9   LYS C CE  1 
ATOM   4513  N  NZ  . LYS E  1 10  ? 54.656  -30.198 30.852  1.00 29.32 ? 9   LYS C NZ  1 
ATOM   4514  N  N   . GLY E  1 11  ? 46.855  -30.431 29.993  1.00 7.70  ? 10  GLY C N   1 
ATOM   4515  C  CA  . GLY E  1 11  ? 45.470  -30.002 30.118  1.00 8.16  ? 10  GLY C CA  1 
ATOM   4516  C  C   . GLY E  1 11  ? 45.203  -29.679 31.581  1.00 9.50  ? 10  GLY C C   1 
ATOM   4517  O  O   . GLY E  1 11  ? 46.152  -29.662 32.367  1.00 7.81  ? 10  GLY C O   1 
ATOM   4518  N  N   . ASP E  1 12  ? 43.954  -29.472 32.006  1.00 12.28 ? 11  ASP C N   1 
ATOM   4519  C  CA  . ASP E  1 12  ? 43.798  -29.037 33.373  1.00 14.87 ? 11  ASP C CA  1 
ATOM   4520  C  C   . ASP E  1 12  ? 43.682  -30.054 34.459  1.00 14.87 ? 11  ASP C C   1 
ATOM   4521  O  O   . ASP E  1 12  ? 43.702  -29.698 35.640  1.00 14.88 ? 11  ASP C O   1 
ATOM   4522  C  CB  . ASP E  1 12  ? 42.629  -28.071 33.463  1.00 20.57 ? 11  ASP C CB  1 
ATOM   4523  C  CG  . ASP E  1 12  ? 43.200  -26.637 33.370  1.00 28.20 ? 11  ASP C CG  1 
ATOM   4524  O  OD1 . ASP E  1 12  ? 44.017  -26.262 34.243  1.00 29.15 ? 11  ASP C OD1 1 
ATOM   4525  O  OD2 . ASP E  1 12  ? 42.854  -25.911 32.411  1.00 30.05 ? 11  ASP C OD2 1 
ATOM   4526  N  N   . GLY E  1 13  ? 43.634  -31.317 34.056  1.00 15.26 ? 12  GLY C N   1 
ATOM   4527  C  CA  . GLY E  1 13  ? 43.547  -32.398 35.020  1.00 11.18 ? 12  GLY C CA  1 
ATOM   4528  C  C   . GLY E  1 13  ? 44.868  -33.100 35.123  1.00 8.90  ? 12  GLY C C   1 
ATOM   4529  O  O   . GLY E  1 13  ? 45.904  -32.483 34.908  1.00 8.59  ? 12  GLY C O   1 
ATOM   4530  N  N   . PRO E  1 14  ? 44.866  -34.404 35.448  1.00 8.31  ? 13  PRO C N   1 
ATOM   4531  C  CA  . PRO E  1 14  ? 46.008  -35.331 35.317  1.00 6.19  ? 13  PRO C CA  1 
ATOM   4532  C  C   . PRO E  1 14  ? 46.496  -35.833 33.929  1.00 4.22  ? 13  PRO C C   1 
ATOM   4533  O  O   . PRO E  1 14  ? 47.594  -36.389 33.802  1.00 2.00  ? 13  PRO C O   1 
ATOM   4534  C  CB  . PRO E  1 14  ? 45.579  -36.444 36.218  1.00 4.32  ? 13  PRO C CB  1 
ATOM   4535  C  CG  . PRO E  1 14  ? 44.116  -36.497 35.905  1.00 2.15  ? 13  PRO C CG  1 
ATOM   4536  C  CD  . PRO E  1 14  ? 43.771  -35.061 36.137  1.00 4.26  ? 13  PRO C CD  1 
ATOM   4537  N  N   . VAL E  1 15  ? 45.681  -35.669 32.878  1.00 3.51  ? 14  VAL C N   1 
ATOM   4538  C  CA  . VAL E  1 15  ? 45.991  -36.161 31.549  1.00 2.45  ? 14  VAL C CA  1 
ATOM   4539  C  C   . VAL E  1 15  ? 47.142  -35.354 31.007  1.00 3.31  ? 14  VAL C C   1 
ATOM   4540  O  O   . VAL E  1 15  ? 47.122  -34.115 30.933  1.00 8.98  ? 14  VAL C O   1 
ATOM   4541  C  CB  . VAL E  1 15  ? 44.778  -36.040 30.637  1.00 2.00  ? 14  VAL C CB  1 
ATOM   4542  C  CG1 . VAL E  1 15  ? 45.123  -36.745 29.360  1.00 2.00  ? 14  VAL C CG1 1 
ATOM   4543  C  CG2 . VAL E  1 15  ? 43.533  -36.669 31.247  1.00 2.00  ? 14  VAL C CG2 1 
ATOM   4544  N  N   . GLN E  1 16  ? 48.126  -36.108 30.578  1.00 2.00  ? 15  GLN C N   1 
ATOM   4545  C  CA  . GLN E  1 16  ? 49.425  -35.596 30.295  1.00 2.00  ? 15  GLN C CA  1 
ATOM   4546  C  C   . GLN E  1 16  ? 50.001  -36.486 29.255  1.00 2.00  ? 15  GLN C C   1 
ATOM   4547  O  O   . GLN E  1 16  ? 49.667  -37.669 29.290  1.00 5.12  ? 15  GLN C O   1 
ATOM   4548  C  CB  . GLN E  1 16  ? 50.140  -35.712 31.575  1.00 4.47  ? 15  GLN C CB  1 
ATOM   4549  C  CG  . GLN E  1 16  ? 51.518  -35.180 31.792  1.00 9.64  ? 15  GLN C CG  1 
ATOM   4550  C  CD  . GLN E  1 16  ? 51.914  -35.450 33.226  1.00 11.14 ? 15  GLN C CD  1 
ATOM   4551  O  OE1 . GLN E  1 16  ? 53.086  -35.680 33.482  1.00 17.32 ? 15  GLN C OE1 1 
ATOM   4552  N  NE2 . GLN E  1 16  ? 51.054  -35.533 34.234  1.00 13.81 ? 15  GLN C NE2 1 
ATOM   4553  N  N   . GLY E  1 17  ? 50.862  -36.059 28.347  1.00 2.00  ? 16  GLY C N   1 
ATOM   4554  C  CA  . GLY E  1 17  ? 51.444  -37.000 27.406  1.00 2.03  ? 16  GLY C CA  1 
ATOM   4555  C  C   . GLY E  1 17  ? 52.211  -36.375 26.271  1.00 2.00  ? 16  GLY C C   1 
ATOM   4556  O  O   . GLY E  1 17  ? 52.062  -35.170 26.042  1.00 2.91  ? 16  GLY C O   1 
ATOM   4557  N  N   . ILE E  1 18  ? 52.977  -37.195 25.544  1.00 2.00  ? 17  ILE C N   1 
ATOM   4558  C  CA  . ILE E  1 18  ? 53.851  -36.761 24.454  1.00 2.17  ? 17  ILE C CA  1 
ATOM   4559  C  C   . ILE E  1 18  ? 53.607  -37.616 23.214  1.00 3.46  ? 17  ILE C C   1 
ATOM   4560  O  O   . ILE E  1 18  ? 53.750  -38.842 23.297  1.00 5.80  ? 17  ILE C O   1 
ATOM   4561  C  CB  . ILE E  1 18  ? 55.301  -36.891 24.906  1.00 2.00  ? 17  ILE C CB  1 
ATOM   4562  C  CG1 . ILE E  1 18  ? 55.529  -35.845 25.946  1.00 2.00  ? 17  ILE C CG1 1 
ATOM   4563  C  CG2 . ILE E  1 18  ? 56.283  -36.713 23.778  1.00 2.00  ? 17  ILE C CG2 1 
ATOM   4564  C  CD1 . ILE E  1 18  ? 56.870  -36.122 26.591  1.00 2.53  ? 17  ILE C CD1 1 
ATOM   4565  N  N   . ILE E  1 19  ? 53.245  -37.041 22.077  1.00 2.14  ? 18  ILE C N   1 
ATOM   4566  C  CA  . ILE E  1 19  ? 52.959  -37.820 20.886  1.00 2.00  ? 18  ILE C CA  1 
ATOM   4567  C  C   . ILE E  1 19  ? 53.920  -37.374 19.804  1.00 2.69  ? 18  ILE C C   1 
ATOM   4568  O  O   . ILE E  1 19  ? 54.108  -36.166 19.578  1.00 5.38  ? 18  ILE C O   1 
ATOM   4569  C  CB  . ILE E  1 19  ? 51.498  -37.566 20.495  1.00 2.00  ? 18  ILE C CB  1 
ATOM   4570  C  CG1 . ILE E  1 19  ? 50.597  -38.098 21.633  1.00 2.00  ? 18  ILE C CG1 1 
ATOM   4571  C  CG2 . ILE E  1 19  ? 51.188  -38.157 19.105  1.00 2.00  ? 18  ILE C CG2 1 
ATOM   4572  C  CD1 . ILE E  1 19  ? 50.601  -39.624 21.772  1.00 2.00  ? 18  ILE C CD1 1 
ATOM   4573  N  N   . ASN E  1 20  ? 54.566  -38.330 19.176  1.00 2.00  ? 19  ASN C N   1 
ATOM   4574  C  CA  . ASN E  1 20  ? 55.471  -38.083 18.091  1.00 2.50  ? 19  ASN C CA  1 
ATOM   4575  C  C   . ASN E  1 20  ? 54.829  -38.442 16.788  1.00 2.28  ? 19  ASN C C   1 
ATOM   4576  O  O   . ASN E  1 20  ? 53.998  -39.354 16.699  1.00 2.00  ? 19  ASN C O   1 
ATOM   4577  C  CB  . ASN E  1 20  ? 56.708  -38.919 18.148  1.00 2.88  ? 19  ASN C CB  1 
ATOM   4578  C  CG  . ASN E  1 20  ? 57.426  -38.693 19.431  1.00 2.00  ? 19  ASN C CG  1 
ATOM   4579  O  OD1 . ASN E  1 20  ? 57.123  -39.330 20.424  1.00 2.00  ? 19  ASN C OD1 1 
ATOM   4580  N  ND2 . ASN E  1 20  ? 58.401  -37.801 19.447  1.00 3.39  ? 19  ASN C ND2 1 
ATOM   4581  N  N   . PHE E  1 21  ? 55.288  -37.707 15.794  1.00 2.00  ? 20  PHE C N   1 
ATOM   4582  C  CA  . PHE E  1 21  ? 54.849  -37.940 14.448  1.00 2.83  ? 20  PHE C CA  1 
ATOM   4583  C  C   . PHE E  1 21  ? 56.070  -38.079 13.536  1.00 3.32  ? 20  PHE C C   1 
ATOM   4584  O  O   . PHE E  1 21  ? 57.121  -37.428 13.691  1.00 2.00  ? 20  PHE C O   1 
ATOM   4585  C  CB  . PHE E  1 21  ? 53.997  -36.790 13.975  1.00 2.00  ? 20  PHE C CB  1 
ATOM   4586  C  CG  . PHE E  1 21  ? 52.676  -36.525 14.707  1.00 2.41  ? 20  PHE C CG  1 
ATOM   4587  C  CD1 . PHE E  1 21  ? 52.638  -35.690 15.815  1.00 2.92  ? 20  PHE C CD1 1 
ATOM   4588  C  CD2 . PHE E  1 21  ? 51.498  -37.074 14.238  1.00 2.00  ? 20  PHE C CD2 1 
ATOM   4589  C  CE1 . PHE E  1 21  ? 51.431  -35.404 16.434  1.00 2.62  ? 20  PHE C CE1 1 
ATOM   4590  C  CE2 . PHE E  1 21  ? 50.303  -36.789 14.856  1.00 2.00  ? 20  PHE C CE2 1 
ATOM   4591  C  CZ  . PHE E  1 21  ? 50.268  -35.963 15.947  1.00 3.75  ? 20  PHE C CZ  1 
ATOM   4592  N  N   . GLU E  1 22  ? 55.937  -38.999 12.601  1.00 4.61  ? 21  GLU C N   1 
ATOM   4593  C  CA  . GLU E  1 22  ? 56.985  -39.194 11.612  1.00 7.34  ? 21  GLU C CA  1 
ATOM   4594  C  C   . GLU E  1 22  ? 56.425  -39.488 10.219  1.00 5.49  ? 21  GLU C C   1 
ATOM   4595  O  O   . GLU E  1 22  ? 55.427  -40.187 10.071  1.00 5.94  ? 21  GLU C O   1 
ATOM   4596  C  CB  . GLU E  1 22  ? 57.865  -40.298 12.108  1.00 6.10  ? 21  GLU C CB  1 
ATOM   4597  C  CG  . GLU E  1 22  ? 59.077  -40.448 11.258  1.00 12.03 ? 21  GLU C CG  1 
ATOM   4598  C  CD  . GLU E  1 22  ? 59.713  -41.796 11.576  1.00 20.23 ? 21  GLU C CD  1 
ATOM   4599  O  OE1 . GLU E  1 22  ? 59.094  -42.847 11.306  1.00 24.18 ? 21  GLU C OE1 1 
ATOM   4600  O  OE2 . GLU E  1 22  ? 60.829  -41.792 12.096  1.00 21.63 ? 21  GLU C OE2 1 
ATOM   4601  N  N   . GLN E  1 23  ? 56.943  -38.892 9.169   1.00 6.24  ? 22  GLN C N   1 
ATOM   4602  C  CA  . GLN E  1 23  ? 56.436  -39.131 7.835   1.00 6.18  ? 22  GLN C CA  1 
ATOM   4603  C  C   . GLN E  1 23  ? 57.724  -39.191 7.064   1.00 7.77  ? 22  GLN C C   1 
ATOM   4604  O  O   . GLN E  1 23  ? 58.434  -38.203 6.865   1.00 8.12  ? 22  GLN C O   1 
ATOM   4605  C  CB  . GLN E  1 23  ? 55.604  -37.979 7.318   1.00 2.00  ? 22  GLN C CB  1 
ATOM   4606  C  CG  . GLN E  1 23  ? 54.913  -38.337 6.033   1.00 2.00  ? 22  GLN C CG  1 
ATOM   4607  C  CD  . GLN E  1 23  ? 54.020  -37.257 5.484   1.00 2.00  ? 22  GLN C CD  1 
ATOM   4608  O  OE1 . GLN E  1 23  ? 54.219  -36.099 5.818   1.00 6.80  ? 22  GLN C OE1 1 
ATOM   4609  N  NE2 . GLN E  1 23  ? 52.975  -37.472 4.704   1.00 2.00  ? 22  GLN C NE2 1 
ATOM   4610  N  N   . LYS E  1 24  ? 58.029  -40.411 6.687   1.00 8.26  ? 23  LYS C N   1 
ATOM   4611  C  CA  . LYS E  1 24  ? 59.246  -40.610 5.968   1.00 11.11 ? 23  LYS C CA  1 
ATOM   4612  C  C   . LYS E  1 24  ? 59.304  -40.092 4.527   1.00 11.34 ? 23  LYS C C   1 
ATOM   4613  O  O   . LYS E  1 24  ? 60.378  -39.679 4.092   1.00 11.79 ? 23  LYS C O   1 
ATOM   4614  C  CB  . LYS E  1 24  ? 59.554  -42.089 6.050   1.00 15.10 ? 23  LYS C CB  1 
ATOM   4615  C  CG  . LYS E  1 24  ? 60.072  -42.462 7.434   1.00 21.75 ? 23  LYS C CG  1 
ATOM   4616  C  CD  . LYS E  1 24  ? 61.238  -41.539 7.847   1.00 28.67 ? 23  LYS C CD  1 
ATOM   4617  C  CE  . LYS E  1 24  ? 62.117  -42.144 8.939   1.00 33.44 ? 23  LYS C CE  1 
ATOM   4618  N  NZ  . LYS E  1 24  ? 63.323  -41.345 9.133   1.00 36.87 ? 23  LYS C NZ  1 
ATOM   4619  N  N   . GLU E  1 25  ? 58.242  -40.083 3.715   1.00 11.52 ? 24  GLU C N   1 
ATOM   4620  C  CA  . GLU E  1 25  ? 58.312  -39.477 2.394   1.00 12.57 ? 24  GLU C CA  1 
ATOM   4621  C  C   . GLU E  1 25  ? 57.153  -38.502 2.395   1.00 12.71 ? 24  GLU C C   1 
ATOM   4622  O  O   . GLU E  1 25  ? 56.134  -38.851 2.991   1.00 13.03 ? 24  GLU C O   1 
ATOM   4623  C  CB  . GLU E  1 25  ? 58.054  -40.425 1.222   1.00 14.73 ? 24  GLU C CB  1 
ATOM   4624  C  CG  . GLU E  1 25  ? 59.188  -41.341 0.810   1.00 20.85 ? 24  GLU C CG  1 
ATOM   4625  C  CD  . GLU E  1 25  ? 59.238  -42.675 1.571   1.00 27.28 ? 24  GLU C CD  1 
ATOM   4626  O  OE1 . GLU E  1 25  ? 58.182  -43.291 1.825   1.00 29.26 ? 24  GLU C OE1 1 
ATOM   4627  O  OE2 . GLU E  1 25  ? 60.355  -43.098 1.906   1.00 30.00 ? 24  GLU C OE2 1 
ATOM   4628  N  N   . SER E  1 26  ? 57.179  -37.362 1.695   1.00 10.77 ? 25  SER C N   1 
ATOM   4629  C  CA  . SER E  1 26  ? 56.049  -36.443 1.680   1.00 8.73  ? 25  SER C CA  1 
ATOM   4630  C  C   . SER E  1 26  ? 54.701  -37.022 1.248   1.00 7.38  ? 25  SER C C   1 
ATOM   4631  O  O   . SER E  1 26  ? 53.622  -36.486 1.530   1.00 10.63 ? 25  SER C O   1 
ATOM   4632  C  CB  . SER E  1 26  ? 56.396  -35.242 0.757   1.00 8.68  ? 25  SER C CB  1 
ATOM   4633  O  OG  . SER E  1 26  ? 56.669  -35.608 -0.591  1.00 5.65  ? 25  SER C OG  1 
ATOM   4634  N  N   . ASN E  1 27  ? 54.732  -38.063 0.440   1.00 6.93  ? 26  ASN C N   1 
ATOM   4635  C  CA  . ASN E  1 27  ? 53.517  -38.694 -0.033  1.00 6.55  ? 26  ASN C CA  1 
ATOM   4636  C  C   . ASN E  1 27  ? 53.234  -39.987 0.743   1.00 7.03  ? 26  ASN C C   1 
ATOM   4637  O  O   . ASN E  1 27  ? 52.370  -40.790 0.399   1.00 11.06 ? 26  ASN C O   1 
ATOM   4638  C  CB  . ASN E  1 27  ? 53.634  -38.942 -1.586  1.00 4.69  ? 26  ASN C CB  1 
ATOM   4639  C  CG  . ASN E  1 27  ? 54.702  -39.857 -2.119  1.00 2.00  ? 26  ASN C CG  1 
ATOM   4640  O  OD1 . ASN E  1 27  ? 55.650  -40.219 -1.432  1.00 7.33  ? 26  ASN C OD1 1 
ATOM   4641  N  ND2 . ASN E  1 27  ? 54.662  -40.310 -3.349  1.00 4.24  ? 26  ASN C ND2 1 
ATOM   4642  N  N   . GLY E  1 28  ? 53.871  -40.211 1.881   1.00 5.53  ? 27  GLY C N   1 
ATOM   4643  C  CA  . GLY E  1 28  ? 53.631  -41.419 2.652   1.00 6.87  ? 27  GLY C CA  1 
ATOM   4644  C  C   . GLY E  1 28  ? 52.672  -41.281 3.845   1.00 4.72  ? 27  GLY C C   1 
ATOM   4645  O  O   . GLY E  1 28  ? 52.287  -40.176 4.228   1.00 3.88  ? 27  GLY C O   1 
ATOM   4646  N  N   . PRO E  1 29  ? 52.266  -42.400 4.470   1.00 4.14  ? 28  PRO C N   1 
ATOM   4647  C  CA  . PRO E  1 29  ? 51.642  -42.425 5.783   1.00 4.66  ? 28  PRO C CA  1 
ATOM   4648  C  C   . PRO E  1 29  ? 52.519  -41.749 6.816   1.00 3.54  ? 28  PRO C C   1 
ATOM   4649  O  O   . PRO E  1 29  ? 53.739  -41.599 6.692   1.00 5.49  ? 28  PRO C O   1 
ATOM   4650  C  CB  . PRO E  1 29  ? 51.410  -43.907 6.089   1.00 2.00  ? 28  PRO C CB  1 
ATOM   4651  C  CG  . PRO E  1 29  ? 52.522  -44.548 5.333   1.00 2.00  ? 28  PRO C CG  1 
ATOM   4652  C  CD  . PRO E  1 29  ? 52.483  -43.774 4.029   1.00 2.00  ? 28  PRO C CD  1 
ATOM   4653  N  N   . VAL E  1 30  ? 51.816  -41.398 7.856   1.00 3.74  ? 29  VAL C N   1 
ATOM   4654  C  CA  . VAL E  1 30  ? 52.404  -40.771 9.015   1.00 6.04  ? 29  VAL C CA  1 
ATOM   4655  C  C   . VAL E  1 30  ? 52.297  -41.817 10.128  1.00 4.39  ? 29  VAL C C   1 
ATOM   4656  O  O   . VAL E  1 30  ? 51.259  -42.425 10.353  1.00 2.00  ? 29  VAL C O   1 
ATOM   4657  C  CB  . VAL E  1 30  ? 51.610  -39.472 9.340   1.00 2.00  ? 29  VAL C CB  1 
ATOM   4658  C  CG1 . VAL E  1 30  ? 52.186  -38.917 10.587  1.00 3.50  ? 29  VAL C CG1 1 
ATOM   4659  C  CG2 . VAL E  1 30  ? 51.674  -38.453 8.259   1.00 2.00  ? 29  VAL C CG2 1 
ATOM   4660  N  N   . LYS E  1 31  ? 53.392  -42.038 10.800  1.00 5.67  ? 30  LYS C N   1 
ATOM   4661  C  CA  . LYS E  1 31  ? 53.414  -42.911 11.922  1.00 9.08  ? 30  LYS C CA  1 
ATOM   4662  C  C   . LYS E  1 31  ? 53.190  -42.022 13.160  1.00 8.58  ? 30  LYS C C   1 
ATOM   4663  O  O   . LYS E  1 31  ? 53.945  -41.029 13.285  1.00 7.70  ? 30  LYS C O   1 
ATOM   4664  C  CB  . LYS E  1 31  ? 54.773  -43.605 11.922  1.00 14.08 ? 30  LYS C CB  1 
ATOM   4665  C  CG  . LYS E  1 31  ? 54.783  -45.012 12.581  1.00 20.89 ? 30  LYS C CG  1 
ATOM   4666  C  CD  . LYS E  1 31  ? 56.201  -45.658 12.599  1.00 25.63 ? 30  LYS C CD  1 
ATOM   4667  C  CE  . LYS E  1 31  ? 56.807  -45.642 14.026  1.00 26.61 ? 30  LYS C CE  1 
ATOM   4668  N  NZ  . LYS E  1 31  ? 58.262  -45.572 13.998  1.00 28.78 ? 30  LYS C NZ  1 
ATOM   4669  N  N   . VAL E  1 32  ? 52.188  -42.302 14.033  1.00 3.13  ? 31  VAL C N   1 
ATOM   4670  C  CA  . VAL E  1 32  ? 52.010  -41.516 15.233  1.00 3.19  ? 31  VAL C CA  1 
ATOM   4671  C  C   . VAL E  1 32  ? 52.058  -42.416 16.466  1.00 5.03  ? 31  VAL C C   1 
ATOM   4672  O  O   . VAL E  1 32  ? 51.413  -43.466 16.506  1.00 8.53  ? 31  VAL C O   1 
ATOM   4673  C  CB  . VAL E  1 32  ? 50.677  -40.621 15.083  1.00 4.82  ? 31  VAL C CB  1 
ATOM   4674  C  CG1 . VAL E  1 32  ? 49.776  -41.206 14.046  1.00 4.03  ? 31  VAL C CG1 1 
ATOM   4675  C  CG2 . VAL E  1 32  ? 49.960  -40.434 16.420  1.00 2.00  ? 31  VAL C CG2 1 
ATOM   4676  N  N   . TRP E  1 33  ? 52.856  -42.074 17.492  1.00 3.23  ? 32  TRP C N   1 
ATOM   4677  C  CA  . TRP E  1 33  ? 53.108  -42.928 18.603  1.00 2.00  ? 32  TRP C CA  1 
ATOM   4678  C  C   . TRP E  1 33  ? 53.467  -42.219 19.898  1.00 3.00  ? 32  TRP C C   1 
ATOM   4679  O  O   . TRP E  1 33  ? 54.000  -41.120 19.850  1.00 4.97  ? 32  TRP C O   1 
ATOM   4680  C  CB  . TRP E  1 33  ? 54.243  -43.874 18.221  1.00 2.84  ? 32  TRP C CB  1 
ATOM   4681  C  CG  . TRP E  1 33  ? 55.698  -43.354 18.225  1.00 3.92  ? 32  TRP C CG  1 
ATOM   4682  C  CD1 . TRP E  1 33  ? 56.464  -43.397 19.363  1.00 2.00  ? 32  TRP C CD1 1 
ATOM   4683  C  CD2 . TRP E  1 33  ? 56.384  -42.798 17.165  1.00 4.78  ? 32  TRP C CD2 1 
ATOM   4684  N  NE1 . TRP E  1 33  ? 57.600  -42.853 19.040  1.00 3.50  ? 32  TRP C NE1 1 
ATOM   4685  C  CE2 . TRP E  1 33  ? 57.591  -42.479 17.753  1.00 6.69  ? 32  TRP C CE2 1 
ATOM   4686  C  CE3 . TRP E  1 33  ? 56.146  -42.502 15.840  1.00 4.97  ? 32  TRP C CE3 1 
ATOM   4687  C  CZ2 . TRP E  1 33  ? 58.601  -41.882 17.022  1.00 12.52 ? 32  TRP C CZ2 1 
ATOM   4688  C  CZ3 . TRP E  1 33  ? 57.143  -41.912 15.109  1.00 12.35 ? 32  TRP C CZ3 1 
ATOM   4689  C  CH2 . TRP E  1 33  ? 58.363  -41.585 15.687  1.00 13.93 ? 32  TRP C CH2 1 
ATOM   4690  N  N   . GLY E  1 34  ? 53.284  -42.797 21.076  1.00 2.00  ? 33  GLY C N   1 
ATOM   4691  C  CA  . GLY E  1 34  ? 53.773  -42.217 22.295  1.00 2.00  ? 33  GLY C CA  1 
ATOM   4692  C  C   . GLY E  1 34  ? 52.807  -42.544 23.366  1.00 2.45  ? 33  GLY C C   1 
ATOM   4693  O  O   . GLY E  1 34  ? 51.837  -43.218 23.103  1.00 5.32  ? 33  GLY C O   1 
ATOM   4694  N  N   . SER E  1 35  ? 52.953  -42.085 24.580  1.00 5.82  ? 34  SER C N   1 
ATOM   4695  C  CA  . SER E  1 35  ? 51.997  -42.361 25.635  1.00 7.34  ? 34  SER C CA  1 
ATOM   4696  C  C   . SER E  1 35  ? 51.328  -41.088 26.072  1.00 7.51  ? 34  SER C C   1 
ATOM   4697  O  O   . SER E  1 35  ? 51.923  -40.012 26.021  1.00 8.02  ? 34  SER C O   1 
ATOM   4698  C  CB  . SER E  1 35  ? 52.659  -42.908 26.861  1.00 10.35 ? 34  SER C CB  1 
ATOM   4699  O  OG  . SER E  1 35  ? 53.470  -44.038 26.603  1.00 16.56 ? 34  SER C OG  1 
ATOM   4700  N  N   . ILE E  1 36  ? 50.109  -41.277 26.542  1.00 6.51  ? 35  ILE C N   1 
ATOM   4701  C  CA  . ILE E  1 36  ? 49.308  -40.282 27.198  1.00 5.57  ? 35  ILE C CA  1 
ATOM   4702  C  C   . ILE E  1 36  ? 48.990  -40.994 28.517  1.00 8.32  ? 35  ILE C C   1 
ATOM   4703  O  O   . ILE E  1 36  ? 48.748  -42.202 28.564  1.00 10.29 ? 35  ILE C O   1 
ATOM   4704  C  CB  . ILE E  1 36  ? 48.024  -40.008 26.445  1.00 4.24  ? 35  ILE C CB  1 
ATOM   4705  C  CG1 . ILE E  1 36  ? 48.308  -39.540 25.052  1.00 2.00  ? 35  ILE C CG1 1 
ATOM   4706  C  CG2 . ILE E  1 36  ? 47.266  -38.953 27.222  1.00 2.00  ? 35  ILE C CG2 1 
ATOM   4707  C  CD1 . ILE E  1 36  ? 46.966  -39.631 24.300  1.00 2.00  ? 35  ILE C CD1 1 
ATOM   4708  N  N   . LYS E  1 37  ? 48.986  -40.364 29.661  1.00 9.09  ? 36  LYS C N   1 
ATOM   4709  C  CA  . LYS E  1 37  ? 48.622  -41.053 30.871  1.00 9.00  ? 36  LYS C CA  1 
ATOM   4710  C  C   . LYS E  1 37  ? 47.706  -40.136 31.664  1.00 7.78  ? 36  LYS C C   1 
ATOM   4711  O  O   . LYS E  1 37  ? 47.492  -38.959 31.336  1.00 5.44  ? 36  LYS C O   1 
ATOM   4712  C  CB  . LYS E  1 37  ? 49.900  -41.388 31.598  1.00 12.53 ? 36  LYS C CB  1 
ATOM   4713  C  CG  . LYS E  1 37  ? 50.725  -40.185 31.966  1.00 18.15 ? 36  LYS C CG  1 
ATOM   4714  C  CD  . LYS E  1 37  ? 52.062  -40.628 32.544  1.00 22.43 ? 36  LYS C CD  1 
ATOM   4715  C  CE  . LYS E  1 37  ? 52.724  -39.419 33.237  1.00 26.59 ? 36  LYS C CE  1 
ATOM   4716  N  NZ  . LYS E  1 37  ? 51.851  -38.814 34.241  1.00 28.13 ? 36  LYS C NZ  1 
ATOM   4717  N  N   . GLY E  1 38  ? 47.140  -40.720 32.702  1.00 8.01  ? 37  GLY C N   1 
ATOM   4718  C  CA  . GLY E  1 38  ? 46.204  -40.035 33.569  1.00 6.64  ? 37  GLY C CA  1 
ATOM   4719  C  C   . GLY E  1 38  ? 44.805  -40.236 33.035  1.00 5.23  ? 37  GLY C C   1 
ATOM   4720  O  O   . GLY E  1 38  ? 43.854  -39.603 33.478  1.00 7.03  ? 37  GLY C O   1 
ATOM   4721  N  N   . LEU E  1 39  ? 44.626  -41.086 32.033  1.00 6.84  ? 38  LEU C N   1 
ATOM   4722  C  CA  . LEU E  1 39  ? 43.294  -41.297 31.502  1.00 7.75  ? 38  LEU C CA  1 
ATOM   4723  C  C   . LEU E  1 39  ? 42.516  -42.261 32.388  1.00 8.31  ? 38  LEU C C   1 
ATOM   4724  O  O   . LEU E  1 39  ? 43.112  -42.984 33.178  1.00 9.29  ? 38  LEU C O   1 
ATOM   4725  C  CB  . LEU E  1 39  ? 43.319  -41.911 30.104  1.00 5.47  ? 38  LEU C CB  1 
ATOM   4726  C  CG  . LEU E  1 39  ? 43.515  -41.149 28.805  1.00 2.00  ? 38  LEU C CG  1 
ATOM   4727  C  CD1 . LEU E  1 39  ? 43.213  -39.696 28.995  1.00 4.77  ? 38  LEU C CD1 1 
ATOM   4728  C  CD2 . LEU E  1 39  ? 44.891  -41.300 28.349  1.00 2.00  ? 38  LEU C CD2 1 
ATOM   4729  N  N   . THR E  1 40  ? 41.188  -42.229 32.325  1.00 7.07  ? 39  THR C N   1 
ATOM   4730  C  CA  . THR E  1 40  ? 40.365  -43.262 32.889  1.00 5.25  ? 39  THR C CA  1 
ATOM   4731  C  C   . THR E  1 40  ? 40.490  -44.408 31.878  1.00 4.55  ? 39  THR C C   1 
ATOM   4732  O  O   . THR E  1 40  ? 40.650  -44.211 30.664  1.00 6.48  ? 39  THR C O   1 
ATOM   4733  C  CB  . THR E  1 40  ? 38.874  -42.714 33.065  1.00 5.42  ? 39  THR C CB  1 
ATOM   4734  O  OG1 . THR E  1 40  ? 38.353  -42.087 31.894  1.00 5.62  ? 39  THR C OG1 1 
ATOM   4735  C  CG2 . THR E  1 40  ? 38.861  -41.613 34.124  1.00 4.60  ? 39  THR C CG2 1 
ATOM   4736  N  N   . GLU E  1 41  ? 40.593  -45.619 32.358  1.00 5.16  ? 40  GLU C N   1 
ATOM   4737  C  CA  . GLU E  1 41  ? 40.621  -46.809 31.534  1.00 4.25  ? 40  GLU C CA  1 
ATOM   4738  C  C   . GLU E  1 41  ? 39.534  -46.811 30.485  1.00 2.92  ? 40  GLU C C   1 
ATOM   4739  O  O   . GLU E  1 41  ? 38.402  -46.427 30.759  1.00 2.93  ? 40  GLU C O   1 
ATOM   4740  C  CB  . GLU E  1 41  ? 40.464  -47.998 32.437  1.00 6.67  ? 40  GLU C CB  1 
ATOM   4741  C  CG  . GLU E  1 41  ? 40.545  -49.289 31.682  1.00 14.04 ? 40  GLU C CG  1 
ATOM   4742  C  CD  . GLU E  1 41  ? 39.971  -50.513 32.370  1.00 17.74 ? 40  GLU C CD  1 
ATOM   4743  O  OE1 . GLU E  1 41  ? 39.295  -50.371 33.400  1.00 19.09 ? 40  GLU C OE1 1 
ATOM   4744  O  OE2 . GLU E  1 41  ? 40.217  -51.613 31.839  1.00 21.37 ? 40  GLU C OE2 1 
ATOM   4745  N  N   . GLY E  1 42  ? 39.851  -47.218 29.266  1.00 4.52  ? 41  GLY C N   1 
ATOM   4746  C  CA  . GLY E  1 42  ? 38.860  -47.248 28.198  1.00 3.38  ? 41  GLY C CA  1 
ATOM   4747  C  C   . GLY E  1 42  ? 39.238  -46.368 27.024  1.00 5.07  ? 41  GLY C C   1 
ATOM   4748  O  O   . GLY E  1 42  ? 40.130  -45.510 27.039  1.00 8.52  ? 41  GLY C O   1 
ATOM   4749  N  N   . LEU E  1 43  ? 38.494  -46.625 25.967  1.00 5.82  ? 42  LEU C N   1 
ATOM   4750  C  CA  . LEU E  1 43  ? 38.521  -45.937 24.684  1.00 3.88  ? 42  LEU C CA  1 
ATOM   4751  C  C   . LEU E  1 43  ? 38.508  -44.432 24.843  1.00 3.88  ? 42  LEU C C   1 
ATOM   4752  O  O   . LEU E  1 43  ? 37.838  -43.980 25.765  1.00 4.36  ? 42  LEU C O   1 
ATOM   4753  C  CB  . LEU E  1 43  ? 37.315  -46.405 23.966  1.00 2.65  ? 42  LEU C CB  1 
ATOM   4754  C  CG  . LEU E  1 43  ? 37.385  -47.159 22.666  1.00 5.38  ? 42  LEU C CG  1 
ATOM   4755  C  CD1 . LEU E  1 43  ? 38.535  -48.133 22.648  1.00 2.00  ? 42  LEU C CD1 1 
ATOM   4756  C  CD2 . LEU E  1 43  ? 36.000  -47.776 22.449  1.00 2.51  ? 42  LEU C CD2 1 
ATOM   4757  N  N   . HIS E  1 44  ? 39.192  -43.598 24.058  1.00 5.92  ? 43  HIS C N   1 
ATOM   4758  C  CA  . HIS E  1 44  ? 39.163  -42.127 24.205  1.00 3.53  ? 43  HIS C CA  1 
ATOM   4759  C  C   . HIS E  1 44  ? 39.404  -41.518 22.850  1.00 2.20  ? 43  HIS C C   1 
ATOM   4760  O  O   . HIS E  1 44  ? 40.385  -41.873 22.209  1.00 2.00  ? 43  HIS C O   1 
ATOM   4761  C  CB  . HIS E  1 44  ? 40.276  -41.577 25.141  1.00 3.64  ? 43  HIS C CB  1 
ATOM   4762  C  CG  . HIS E  1 44  ? 39.984  -41.700 26.642  1.00 6.03  ? 43  HIS C CG  1 
ATOM   4763  N  ND1 . HIS E  1 44  ? 40.067  -42.720 27.492  1.00 6.92  ? 43  HIS C ND1 1 
ATOM   4764  C  CD2 . HIS E  1 44  ? 39.474  -40.666 27.386  1.00 8.31  ? 43  HIS C CD2 1 
ATOM   4765  C  CE1 . HIS E  1 44  ? 39.629  -42.341 28.667  1.00 6.84  ? 43  HIS C CE1 1 
ATOM   4766  N  NE2 . HIS E  1 44  ? 39.269  -41.091 28.592  1.00 8.72  ? 43  HIS C NE2 1 
ATOM   4767  N  N   . GLY E  1 45  ? 38.524  -40.614 22.404  1.00 2.63  ? 44  GLY C N   1 
ATOM   4768  C  CA  . GLY E  1 45  ? 38.667  -39.880 21.153  1.00 2.00  ? 44  GLY C CA  1 
ATOM   4769  C  C   . GLY E  1 45  ? 40.078  -39.298 21.002  1.00 2.06  ? 44  GLY C C   1 
ATOM   4770  O  O   . GLY E  1 45  ? 40.672  -38.963 22.030  1.00 3.00  ? 44  GLY C O   1 
ATOM   4771  N  N   . PHE E  1 46  ? 40.641  -39.201 19.787  1.00 2.00  ? 45  PHE C N   1 
ATOM   4772  C  CA  . PHE E  1 46  ? 41.995  -38.725 19.538  1.00 2.00  ? 45  PHE C CA  1 
ATOM   4773  C  C   . PHE E  1 46  ? 41.950  -37.966 18.233  1.00 2.94  ? 45  PHE C C   1 
ATOM   4774  O  O   . PHE E  1 46  ? 41.756  -38.573 17.167  1.00 3.15  ? 45  PHE C O   1 
ATOM   4775  C  CB  . PHE E  1 46  ? 42.857  -39.899 19.407  1.00 2.00  ? 45  PHE C CB  1 
ATOM   4776  C  CG  . PHE E  1 46  ? 44.323  -39.622 19.361  1.00 2.00  ? 45  PHE C CG  1 
ATOM   4777  C  CD1 . PHE E  1 46  ? 44.953  -39.243 20.510  1.00 2.10  ? 45  PHE C CD1 1 
ATOM   4778  C  CD2 . PHE E  1 46  ? 45.008  -39.844 18.201  1.00 2.00  ? 45  PHE C CD2 1 
ATOM   4779  C  CE1 . PHE E  1 46  ? 46.306  -39.104 20.522  1.00 2.00  ? 45  PHE C CE1 1 
ATOM   4780  C  CE2 . PHE E  1 46  ? 46.360  -39.703 18.208  1.00 2.00  ? 45  PHE C CE2 1 
ATOM   4781  C  CZ  . PHE E  1 46  ? 47.007  -39.336 19.362  1.00 4.58  ? 45  PHE C CZ  1 
ATOM   4782  N  N   . HIS E  1 47  ? 42.088  -36.641 18.249  1.00 2.00  ? 46  HIS C N   1 
ATOM   4783  C  CA  . HIS E  1 47  ? 41.788  -35.843 17.060  1.00 3.11  ? 46  HIS C CA  1 
ATOM   4784  C  C   . HIS E  1 47  ? 42.707  -34.649 16.872  1.00 2.02  ? 46  HIS C C   1 
ATOM   4785  O  O   . HIS E  1 47  ? 43.301  -34.187 17.837  1.00 2.00  ? 46  HIS C O   1 
ATOM   4786  C  CB  . HIS E  1 47  ? 40.392  -35.248 17.097  1.00 2.00  ? 46  HIS C CB  1 
ATOM   4787  C  CG  . HIS E  1 47  ? 39.219  -36.146 17.438  1.00 2.00  ? 46  HIS C CG  1 
ATOM   4788  N  ND1 . HIS E  1 47  ? 38.196  -35.809 18.228  1.00 3.93  ? 46  HIS C ND1 1 
ATOM   4789  C  CD2 . HIS E  1 47  ? 39.061  -37.446 17.018  1.00 2.00  ? 46  HIS C CD2 1 
ATOM   4790  C  CE1 . HIS E  1 47  ? 37.439  -36.877 18.302  1.00 2.00  ? 46  HIS C CE1 1 
ATOM   4791  N  NE2 . HIS E  1 47  ? 37.957  -37.846 17.581  1.00 2.96  ? 46  HIS C NE2 1 
ATOM   4792  N  N   . VAL E  1 48  ? 42.795  -34.137 15.646  1.00 2.00  ? 47  VAL C N   1 
ATOM   4793  C  CA  . VAL E  1 48  ? 43.614  -32.992 15.325  1.00 3.48  ? 47  VAL C CA  1 
ATOM   4794  C  C   . VAL E  1 48  ? 42.576  -31.895 15.087  1.00 3.27  ? 47  VAL C C   1 
ATOM   4795  O  O   . VAL E  1 48  ? 41.765  -31.970 14.158  1.00 7.24  ? 47  VAL C O   1 
ATOM   4796  C  CB  . VAL E  1 48  ? 44.459  -33.229 14.047  1.00 2.00  ? 47  VAL C CB  1 
ATOM   4797  C  CG1 . VAL E  1 48  ? 45.196  -31.917 13.851  1.00 2.00  ? 47  VAL C CG1 1 
ATOM   4798  C  CG2 . VAL E  1 48  ? 45.464  -34.359 14.133  1.00 2.00  ? 47  VAL C CG2 1 
ATOM   4799  N  N   . HIS E  1 49  ? 42.473  -30.947 15.984  1.00 2.00  ? 48  HIS C N   1 
ATOM   4800  C  CA  . HIS E  1 49  ? 41.574  -29.831 15.847  1.00 2.63  ? 48  HIS C CA  1 
ATOM   4801  C  C   . HIS E  1 49  ? 42.208  -28.741 14.971  1.00 2.00  ? 48  HIS C C   1 
ATOM   4802  O  O   . HIS E  1 49  ? 43.417  -28.630 14.863  1.00 2.00  ? 48  HIS C O   1 
ATOM   4803  C  CB  . HIS E  1 49  ? 41.200  -29.302 17.263  1.00 2.10  ? 48  HIS C CB  1 
ATOM   4804  C  CG  . HIS E  1 49  ? 40.143  -30.192 17.895  1.00 2.00  ? 48  HIS C CG  1 
ATOM   4805  N  ND1 . HIS E  1 49  ? 38.979  -29.857 18.364  1.00 2.00  ? 48  HIS C ND1 1 
ATOM   4806  C  CD2 . HIS E  1 49  ? 40.245  -31.559 18.071  1.00 2.00  ? 48  HIS C CD2 1 
ATOM   4807  C  CE1 . HIS E  1 49  ? 38.402  -30.961 18.808  1.00 2.00  ? 48  HIS C CE1 1 
ATOM   4808  N  NE2 . HIS E  1 49  ? 39.154  -32.018 18.639  1.00 2.00  ? 48  HIS C NE2 1 
ATOM   4809  N  N   . GLU E  1 50  ? 41.414  -27.941 14.317  1.00 2.00  ? 49  GLU C N   1 
ATOM   4810  C  CA  . GLU E  1 50  ? 41.908  -26.995 13.352  1.00 4.00  ? 49  GLU C CA  1 
ATOM   4811  C  C   . GLU E  1 50  ? 42.915  -25.927 13.804  1.00 3.31  ? 49  GLU C C   1 
ATOM   4812  O  O   . GLU E  1 50  ? 43.890  -25.721 13.101  1.00 2.00  ? 49  GLU C O   1 
ATOM   4813  C  CB  . GLU E  1 50  ? 40.734  -26.309 12.738  1.00 2.51  ? 49  GLU C CB  1 
ATOM   4814  C  CG  . GLU E  1 50  ? 41.172  -25.544 11.545  1.00 7.45  ? 49  GLU C CG  1 
ATOM   4815  C  CD  . GLU E  1 50  ? 40.062  -24.955 10.684  1.00 11.80 ? 49  GLU C CD  1 
ATOM   4816  O  OE1 . GLU E  1 50  ? 38.884  -25.259 10.910  1.00 16.00 ? 49  GLU C OE1 1 
ATOM   4817  O  OE2 . GLU E  1 50  ? 40.400  -24.196 9.765   1.00 10.63 ? 49  GLU C OE2 1 
ATOM   4818  N  N   . PHE E  1 51  ? 42.788  -25.282 14.940  1.00 2.00  ? 50  PHE C N   1 
ATOM   4819  C  CA  . PHE E  1 51  ? 43.680  -24.198 15.271  1.00 3.15  ? 50  PHE C CA  1 
ATOM   4820  C  C   . PHE E  1 51  ? 44.709  -24.665 16.245  1.00 3.18  ? 50  PHE C C   1 
ATOM   4821  O  O   . PHE E  1 51  ? 44.455  -25.561 17.067  1.00 2.00  ? 50  PHE C O   1 
ATOM   4822  C  CB  . PHE E  1 51  ? 42.911  -23.023 15.881  1.00 2.00  ? 50  PHE C CB  1 
ATOM   4823  C  CG  . PHE E  1 51  ? 41.882  -22.607 14.863  1.00 2.00  ? 50  PHE C CG  1 
ATOM   4824  C  CD1 . PHE E  1 51  ? 42.275  -22.300 13.558  1.00 2.20  ? 50  PHE C CD1 1 
ATOM   4825  C  CD2 . PHE E  1 51  ? 40.547  -22.652 15.199  1.00 2.00  ? 50  PHE C CD2 1 
ATOM   4826  C  CE1 . PHE E  1 51  ? 41.315  -22.044 12.601  1.00 2.00  ? 50  PHE C CE1 1 
ATOM   4827  C  CE2 . PHE E  1 51  ? 39.599  -22.387 14.221  1.00 2.00  ? 50  PHE C CE2 1 
ATOM   4828  C  CZ  . PHE E  1 51  ? 39.980  -22.098 12.931  1.00 2.00  ? 50  PHE C CZ  1 
ATOM   4829  N  N   . GLY E  1 52  ? 45.859  -24.021 16.160  1.00 2.00  ? 51  GLY C N   1 
ATOM   4830  C  CA  . GLY E  1 52  ? 46.946  -24.336 17.068  1.00 3.43  ? 51  GLY C CA  1 
ATOM   4831  C  C   . GLY E  1 52  ? 46.966  -23.196 18.025  1.00 3.43  ? 51  GLY C C   1 
ATOM   4832  O  O   . GLY E  1 52  ? 47.918  -22.446 18.113  1.00 4.12  ? 51  GLY C O   1 
ATOM   4833  N  N   . ASP E  1 53  ? 45.866  -23.080 18.734  1.00 5.30  ? 52  ASP C N   1 
ATOM   4834  C  CA  . ASP E  1 53  ? 45.610  -21.938 19.558  1.00 6.56  ? 52  ASP C CA  1 
ATOM   4835  C  C   . ASP E  1 53  ? 45.188  -22.450 20.927  1.00 6.88  ? 52  ASP C C   1 
ATOM   4836  O  O   . ASP E  1 53  ? 44.052  -22.830 21.180  1.00 6.31  ? 52  ASP C O   1 
ATOM   4837  C  CB  . ASP E  1 53  ? 44.517  -21.098 18.835  1.00 3.78  ? 52  ASP C CB  1 
ATOM   4838  C  CG  . ASP E  1 53  ? 44.119  -19.809 19.526  1.00 6.03  ? 52  ASP C CG  1 
ATOM   4839  O  OD1 . ASP E  1 53  ? 44.110  -19.753 20.745  1.00 3.89  ? 52  ASP C OD1 1 
ATOM   4840  O  OD2 . ASP E  1 53  ? 43.820  -18.837 18.846  1.00 10.84 ? 52  ASP C OD2 1 
ATOM   4841  N  N   . ASN E  1 54  ? 46.104  -22.343 21.859  1.00 10.22 ? 53  ASN C N   1 
ATOM   4842  C  CA  . ASN E  1 54  ? 45.856  -22.753 23.232  1.00 12.19 ? 53  ASN C CA  1 
ATOM   4843  C  C   . ASN E  1 54  ? 45.717  -21.462 24.068  1.00 11.25 ? 53  ASN C C   1 
ATOM   4844  O  O   . ASN E  1 54  ? 46.001  -21.428 25.265  1.00 11.89 ? 53  ASN C O   1 
ATOM   4845  C  CB  . ASN E  1 54  ? 47.036  -23.636 23.733  1.00 16.69 ? 53  ASN C CB  1 
ATOM   4846  C  CG  . ASN E  1 54  ? 47.032  -25.156 23.385  1.00 24.41 ? 53  ASN C CG  1 
ATOM   4847  O  OD1 . ASN E  1 54  ? 46.553  -25.696 22.360  1.00 23.75 ? 53  ASN C OD1 1 
ATOM   4848  N  ND2 . ASN E  1 54  ? 47.649  -25.913 24.299  1.00 26.96 ? 53  ASN C ND2 1 
ATOM   4849  N  N   . THR E  1 55  ? 45.217  -20.345 23.530  1.00 7.71  ? 54  THR C N   1 
ATOM   4850  C  CA  . THR E  1 55  ? 45.117  -19.180 24.362  1.00 7.44  ? 54  THR C CA  1 
ATOM   4851  C  C   . THR E  1 55  ? 43.975  -19.282 25.386  1.00 11.86 ? 54  THR C C   1 
ATOM   4852  O  O   . THR E  1 55  ? 43.902  -18.470 26.315  1.00 16.95 ? 54  THR C O   1 
ATOM   4853  C  CB  . THR E  1 55  ? 44.982  -17.937 23.463  1.00 3.89  ? 54  THR C CB  1 
ATOM   4854  O  OG1 . THR E  1 55  ? 43.752  -18.007 22.795  1.00 2.75  ? 54  THR C OG1 1 
ATOM   4855  C  CG2 . THR E  1 55  ? 46.124  -17.841 22.442  1.00 4.23  ? 54  THR C CG2 1 
ATOM   4856  N  N   . ALA E  1 56  ? 43.076  -20.276 25.266  1.00 10.47 ? 55  ALA C N   1 
ATOM   4857  C  CA  . ALA E  1 56  ? 41.936  -20.547 26.152  1.00 7.01  ? 55  ALA C CA  1 
ATOM   4858  C  C   . ALA E  1 56  ? 41.954  -22.087 26.338  1.00 9.64  ? 55  ALA C C   1 
ATOM   4859  O  O   . ALA E  1 56  ? 40.949  -22.812 26.240  1.00 9.88  ? 55  ALA C O   1 
ATOM   4860  C  CB  . ALA E  1 56  ? 40.643  -20.119 25.456  1.00 2.00  ? 55  ALA C CB  1 
ATOM   4861  N  N   . GLY E  1 57  ? 43.142  -22.666 26.523  1.00 9.18  ? 56  GLY C N   1 
ATOM   4862  C  CA  . GLY E  1 57  ? 43.296  -24.089 26.657  1.00 8.60  ? 56  GLY C CA  1 
ATOM   4863  C  C   . GLY E  1 57  ? 42.851  -24.742 25.384  1.00 9.73  ? 56  GLY C C   1 
ATOM   4864  O  O   . GLY E  1 57  ? 42.846  -24.112 24.313  1.00 11.74 ? 56  GLY C O   1 
ATOM   4865  N  N   . CYS E  1 58  ? 42.383  -25.977 25.538  1.00 9.86  ? 57  CYS C N   1 
ATOM   4866  C  CA  . CYS E  1 58  ? 41.924  -26.711 24.384  1.00 7.86  ? 57  CYS C CA  1 
ATOM   4867  C  C   . CYS E  1 58  ? 40.684  -26.097 23.748  1.00 8.14  ? 57  CYS C C   1 
ATOM   4868  O  O   . CYS E  1 58  ? 40.399  -26.413 22.588  1.00 7.39  ? 57  CYS C O   1 
ATOM   4869  C  CB  . CYS E  1 58  ? 41.616  -28.135 24.766  1.00 4.82  ? 57  CYS C CB  1 
ATOM   4870  S  SG  . CYS E  1 58  ? 42.977  -28.902 25.658  1.00 7.43  ? 57  CYS C SG  1 
ATOM   4871  N  N   . THR E  1 59  ? 39.939  -25.194 24.409  1.00 8.44  ? 58  THR C N   1 
ATOM   4872  C  CA  . THR E  1 59  ? 38.726  -24.669 23.814  1.00 8.79  ? 58  THR C CA  1 
ATOM   4873  C  C   . THR E  1 59  ? 39.034  -23.906 22.551  1.00 7.64  ? 58  THR C C   1 
ATOM   4874  O  O   . THR E  1 59  ? 38.299  -24.058 21.580  1.00 10.22 ? 58  THR C O   1 
ATOM   4875  C  CB  . THR E  1 59  ? 38.023  -23.785 24.826  1.00 10.28 ? 58  THR C CB  1 
ATOM   4876  O  OG1 . THR E  1 59  ? 37.783  -24.659 25.922  1.00 11.92 ? 58  THR C OG1 1 
ATOM   4877  C  CG2 . THR E  1 59  ? 36.716  -23.170 24.341  1.00 10.70 ? 58  THR C CG2 1 
ATOM   4878  N  N   . SER E  1 60  ? 40.183  -23.232 22.462  1.00 7.07  ? 59  SER C N   1 
ATOM   4879  C  CA  . SER E  1 60  ? 40.486  -22.436 21.272  1.00 5.64  ? 59  SER C CA  1 
ATOM   4880  C  C   . SER E  1 60  ? 41.051  -23.165 20.062  1.00 4.28  ? 59  SER C C   1 
ATOM   4881  O  O   . SER E  1 60  ? 41.200  -22.614 18.981  1.00 3.83  ? 59  SER C O   1 
ATOM   4882  C  CB  . SER E  1 60  ? 41.405  -21.326 21.719  1.00 9.65  ? 59  SER C CB  1 
ATOM   4883  O  OG  . SER E  1 60  ? 42.225  -21.655 22.855  1.00 10.26 ? 59  SER C OG  1 
ATOM   4884  N  N   . ALA E  1 61  ? 41.269  -24.470 20.232  1.00 4.77  ? 60  ALA C N   1 
ATOM   4885  C  CA  . ALA E  1 61  ? 41.737  -25.355 19.213  1.00 2.00  ? 60  ALA C CA  1 
ATOM   4886  C  C   . ALA E  1 61  ? 40.686  -25.494 18.102  1.00 2.72  ? 60  ALA C C   1 
ATOM   4887  O  O   . ALA E  1 61  ? 40.976  -25.992 17.014  1.00 6.53  ? 60  ALA C O   1 
ATOM   4888  C  CB  . ALA E  1 61  ? 42.017  -26.657 19.911  1.00 2.75  ? 60  ALA C CB  1 
ATOM   4889  N  N   . GLY E  1 62  ? 39.427  -25.125 18.251  1.00 2.36  ? 61  GLY C N   1 
ATOM   4890  C  CA  . GLY E  1 62  ? 38.476  -25.145 17.155  1.00 2.00  ? 61  GLY C CA  1 
ATOM   4891  C  C   . GLY E  1 62  ? 37.902  -26.525 16.891  1.00 4.73  ? 61  GLY C C   1 
ATOM   4892  O  O   . GLY E  1 62  ? 38.066  -27.473 17.670  1.00 8.16  ? 61  GLY C O   1 
ATOM   4893  N  N   . PRO E  1 63  ? 37.201  -26.733 15.788  1.00 4.25  ? 62  PRO C N   1 
ATOM   4894  C  CA  . PRO E  1 63  ? 36.546  -27.981 15.473  1.00 2.95  ? 62  PRO C CA  1 
ATOM   4895  C  C   . PRO E  1 63  ? 37.535  -28.961 14.881  1.00 3.94  ? 62  PRO C C   1 
ATOM   4896  O  O   . PRO E  1 63  ? 38.702  -28.570 14.761  1.00 6.64  ? 62  PRO C O   1 
ATOM   4897  C  CB  . PRO E  1 63  ? 35.467  -27.497 14.573  1.00 2.00  ? 62  PRO C CB  1 
ATOM   4898  C  CG  . PRO E  1 63  ? 36.075  -26.409 13.760  1.00 2.00  ? 62  PRO C CG  1 
ATOM   4899  C  CD  . PRO E  1 63  ? 37.006  -25.737 14.739  1.00 5.82  ? 62  PRO C CD  1 
ATOM   4900  N  N   . HIS E  1 64  ? 37.184  -30.169 14.466  1.00 2.00  ? 63  HIS C N   1 
ATOM   4901  C  CA  . HIS E  1 64  ? 38.226  -31.020 13.954  1.00 2.00  ? 63  HIS C CA  1 
ATOM   4902  C  C   . HIS E  1 64  ? 38.716  -30.442 12.616  1.00 2.84  ? 63  HIS C C   1 
ATOM   4903  O  O   . HIS E  1 64  ? 37.959  -29.841 11.842  1.00 2.00  ? 63  HIS C O   1 
ATOM   4904  C  CB  . HIS E  1 64  ? 37.713  -32.457 13.740  1.00 4.93  ? 63  HIS C CB  1 
ATOM   4905  C  CG  . HIS E  1 64  ? 37.251  -33.222 14.979  1.00 7.68  ? 63  HIS C CG  1 
ATOM   4906  N  ND1 . HIS E  1 64  ? 36.319  -34.161 15.063  1.00 10.04 ? 63  HIS C ND1 1 
ATOM   4907  C  CD2 . HIS E  1 64  ? 37.759  -33.038 16.242  1.00 11.21 ? 63  HIS C CD2 1 
ATOM   4908  C  CE1 . HIS E  1 64  ? 36.302  -34.498 16.354  1.00 12.74 ? 63  HIS C CE1 1 
ATOM   4909  N  NE2 . HIS E  1 64  ? 37.161  -33.842 17.097  1.00 12.67 ? 63  HIS C NE2 1 
ATOM   4910  N  N   . PHE E  1 65  ? 40.007  -30.609 12.329  1.00 2.76  ? 64  PHE C N   1 
ATOM   4911  C  CA  . PHE E  1 65  ? 40.611  -30.156 11.098  1.00 2.57  ? 64  PHE C CA  1 
ATOM   4912  C  C   . PHE E  1 65  ? 39.949  -30.863 9.930   1.00 2.90  ? 64  PHE C C   1 
ATOM   4913  O  O   . PHE E  1 65  ? 40.035  -32.075 9.729   1.00 3.16  ? 64  PHE C O   1 
ATOM   4914  C  CB  . PHE E  1 65  ? 42.090  -30.449 11.167  1.00 2.00  ? 64  PHE C CB  1 
ATOM   4915  C  CG  . PHE E  1 65  ? 42.892  -30.168 9.917   1.00 2.00  ? 64  PHE C CG  1 
ATOM   4916  C  CD1 . PHE E  1 65  ? 42.669  -29.075 9.141   1.00 2.00  ? 64  PHE C CD1 1 
ATOM   4917  C  CD2 . PHE E  1 65  ? 43.856  -31.052 9.561   1.00 2.00  ? 64  PHE C CD2 1 
ATOM   4918  C  CE1 . PHE E  1 65  ? 43.403  -28.882 8.013   1.00 2.00  ? 64  PHE C CE1 1 
ATOM   4919  C  CE2 . PHE E  1 65  ? 44.589  -30.853 8.427   1.00 2.00  ? 64  PHE C CE2 1 
ATOM   4920  C  CZ  . PHE E  1 65  ? 44.367  -29.766 7.646   1.00 2.00  ? 64  PHE C CZ  1 
ATOM   4921  N  N   . ASN E  1 66  ? 39.318  -30.051 9.113   1.00 4.24  ? 65  ASN C N   1 
ATOM   4922  C  CA  . ASN E  1 66  ? 38.512  -30.598 8.063   1.00 6.23  ? 65  ASN C CA  1 
ATOM   4923  C  C   . ASN E  1 66  ? 38.602  -29.743 6.825   1.00 8.85  ? 65  ASN C C   1 
ATOM   4924  O  O   . ASN E  1 66  ? 37.663  -28.973 6.583   1.00 11.51 ? 65  ASN C O   1 
ATOM   4925  C  CB  . ASN E  1 66  ? 37.136  -30.648 8.638   1.00 5.27  ? 65  ASN C CB  1 
ATOM   4926  C  CG  . ASN E  1 66  ? 36.019  -31.136 7.768   1.00 3.98  ? 65  ASN C CG  1 
ATOM   4927  O  OD1 . ASN E  1 66  ? 36.200  -31.882 6.807   1.00 7.29  ? 65  ASN C OD1 1 
ATOM   4928  N  ND2 . ASN E  1 66  ? 34.809  -30.790 8.168   1.00 2.00  ? 65  ASN C ND2 1 
ATOM   4929  N  N   . PRO E  1 67  ? 39.670  -29.815 5.998   1.00 7.95  ? 66  PRO C N   1 
ATOM   4930  C  CA  . PRO E  1 67  ? 39.815  -28.999 4.816   1.00 5.61  ? 66  PRO C CA  1 
ATOM   4931  C  C   . PRO E  1 67  ? 38.858  -29.410 3.698   1.00 9.25  ? 66  PRO C C   1 
ATOM   4932  O  O   . PRO E  1 67  ? 38.512  -28.582 2.853   1.00 10.06 ? 66  PRO C O   1 
ATOM   4933  C  CB  . PRO E  1 67  ? 41.317  -29.138 4.527   1.00 2.00  ? 66  PRO C CB  1 
ATOM   4934  C  CG  . PRO E  1 67  ? 41.705  -30.506 4.928   1.00 2.00  ? 66  PRO C CG  1 
ATOM   4935  C  CD  . PRO E  1 67  ? 40.796  -30.747 6.120   1.00 6.92  ? 66  PRO C CD  1 
ATOM   4936  N  N   . LEU E  1 68  ? 38.399  -30.688 3.627   1.00 13.00 ? 67  LEU C N   1 
ATOM   4937  C  CA  . LEU E  1 68  ? 37.465  -31.124 2.569   1.00 11.86 ? 67  LEU C CA  1 
ATOM   4938  C  C   . LEU E  1 68  ? 35.967  -31.090 2.924   1.00 12.88 ? 67  LEU C C   1 
ATOM   4939  O  O   . LEU E  1 68  ? 35.129  -31.609 2.196   1.00 14.11 ? 67  LEU C O   1 
ATOM   4940  C  CB  . LEU E  1 68  ? 37.840  -32.516 2.154   1.00 7.76  ? 67  LEU C CB  1 
ATOM   4941  C  CG  . LEU E  1 68  ? 39.303  -32.765 1.853   1.00 9.52  ? 67  LEU C CG  1 
ATOM   4942  C  CD1 . LEU E  1 68  ? 39.483  -34.181 1.295   1.00 7.66  ? 67  LEU C CD1 1 
ATOM   4943  C  CD2 . LEU E  1 68  ? 39.789  -31.749 0.850   1.00 9.24  ? 67  LEU C CD2 1 
ATOM   4944  N  N   . SER E  1 69  ? 35.567  -30.473 4.033   1.00 15.05 ? 68  SER C N   1 
ATOM   4945  C  CA  . SER E  1 69  ? 34.193  -30.425 4.497   1.00 15.26 ? 68  SER C CA  1 
ATOM   4946  C  C   . SER E  1 69  ? 33.398  -31.700 4.359   1.00 13.00 ? 68  SER C C   1 
ATOM   4947  O  O   . SER E  1 69  ? 32.328  -31.748 3.763   1.00 14.24 ? 68  SER C O   1 
ATOM   4948  C  CB  . SER E  1 69  ? 33.488  -29.309 3.786   1.00 16.97 ? 68  SER C CB  1 
ATOM   4949  O  OG  . SER E  1 69  ? 34.215  -28.149 4.157   1.00 25.60 ? 68  SER C OG  1 
ATOM   4950  N  N   . ARG E  1 70  ? 33.960  -32.743 4.944   1.00 12.48 ? 69  ARG C N   1 
ATOM   4951  C  CA  . ARG E  1 70  ? 33.289  -34.032 5.004   1.00 12.59 ? 69  ARG C CA  1 
ATOM   4952  C  C   . ARG E  1 70  ? 32.634  -34.144 6.373   1.00 10.68 ? 69  ARG C C   1 
ATOM   4953  O  O   . ARG E  1 70  ? 32.688  -33.166 7.123   1.00 12.07 ? 69  ARG C O   1 
ATOM   4954  C  CB  . ARG E  1 70  ? 34.290  -35.149 4.804   1.00 12.96 ? 69  ARG C CB  1 
ATOM   4955  C  CG  . ARG E  1 70  ? 34.828  -35.156 3.396   1.00 13.18 ? 69  ARG C CG  1 
ATOM   4956  C  CD  . ARG E  1 70  ? 35.470  -36.518 3.264   1.00 20.36 ? 69  ARG C CD  1 
ATOM   4957  N  NE  . ARG E  1 70  ? 36.500  -36.562 2.236   1.00 23.65 ? 69  ARG C NE  1 
ATOM   4958  C  CZ  . ARG E  1 70  ? 36.218  -36.893 0.976   1.00 26.20 ? 69  ARG C CZ  1 
ATOM   4959  N  NH1 . ARG E  1 70  ? 34.960  -37.219 0.610   1.00 26.63 ? 69  ARG C NH1 1 
ATOM   4960  N  NH2 . ARG E  1 70  ? 37.214  -36.912 0.084   1.00 23.53 ? 69  ARG C NH2 1 
ATOM   4961  N  N   . LYS E  1 71  ? 31.980  -35.234 6.762   1.00 9.84  ? 70  LYS C N   1 
ATOM   4962  C  CA  . LYS E  1 71  ? 31.399  -35.285 8.098   1.00 10.34 ? 70  LYS C CA  1 
ATOM   4963  C  C   . LYS E  1 71  ? 32.327  -36.162 8.921   1.00 7.67  ? 70  LYS C C   1 
ATOM   4964  O  O   . LYS E  1 71  ? 33.310  -36.708 8.406   1.00 9.88  ? 70  LYS C O   1 
ATOM   4965  C  CB  . LYS E  1 71  ? 30.023  -35.933 8.133   1.00 16.38 ? 70  LYS C CB  1 
ATOM   4966  C  CG  . LYS E  1 71  ? 29.086  -35.830 6.918   1.00 22.04 ? 70  LYS C CG  1 
ATOM   4967  C  CD  . LYS E  1 71  ? 28.294  -34.520 6.767   1.00 25.82 ? 70  LYS C CD  1 
ATOM   4968  C  CE  . LYS E  1 71  ? 27.244  -34.658 5.645   1.00 27.89 ? 70  LYS C CE  1 
ATOM   4969  N  NZ  . LYS E  1 71  ? 26.323  -35.776 5.829   1.00 31.37 ? 70  LYS C NZ  1 
ATOM   4970  N  N   . HIS E  1 72  ? 32.076  -36.278 10.200  1.00 3.62  ? 71  HIS C N   1 
ATOM   4971  C  CA  . HIS E  1 72  ? 32.901  -37.093 11.078  1.00 4.16  ? 71  HIS C CA  1 
ATOM   4972  C  C   . HIS E  1 72  ? 32.910  -38.557 10.727  1.00 2.04  ? 71  HIS C C   1 
ATOM   4973  O  O   . HIS E  1 72  ? 31.921  -39.093 10.246  1.00 5.66  ? 71  HIS C O   1 
ATOM   4974  C  CB  . HIS E  1 72  ? 32.444  -36.983 12.545  1.00 4.73  ? 71  HIS C CB  1 
ATOM   4975  C  CG  . HIS E  1 72  ? 33.537  -37.359 13.549  1.00 5.37  ? 71  HIS C CG  1 
ATOM   4976  N  ND1 . HIS E  1 72  ? 34.668  -36.701 13.695  1.00 3.97  ? 71  HIS C ND1 1 
ATOM   4977  C  CD2 . HIS E  1 72  ? 33.522  -38.400 14.443  1.00 2.00  ? 71  HIS C CD2 1 
ATOM   4978  C  CE1 . HIS E  1 72  ? 35.315  -37.316 14.659  1.00 3.26  ? 71  HIS C CE1 1 
ATOM   4979  N  NE2 . HIS E  1 72  ? 34.620  -38.326 15.099  1.00 2.00  ? 71  HIS C NE2 1 
ATOM   4980  N  N   . GLY E  1 73  ? 34.008  -39.201 11.018  1.00 2.00  ? 72  GLY C N   1 
ATOM   4981  C  CA  . GLY E  1 73  ? 34.115  -40.596 10.752  1.00 2.00  ? 72  GLY C CA  1 
ATOM   4982  C  C   . GLY E  1 73  ? 35.283  -41.185 11.525  1.00 2.89  ? 72  GLY C C   1 
ATOM   4983  O  O   . GLY E  1 73  ? 35.988  -40.526 12.312  1.00 3.78  ? 72  GLY C O   1 
ATOM   4984  N  N   . GLY E  1 74  ? 35.412  -42.494 11.378  1.00 2.00  ? 73  GLY C N   1 
ATOM   4985  C  CA  . GLY E  1 74  ? 36.542  -43.206 11.915  1.00 2.00  ? 73  GLY C CA  1 
ATOM   4986  C  C   . GLY E  1 74  ? 37.647  -43.032 10.897  1.00 2.00  ? 73  GLY C C   1 
ATOM   4987  O  O   . GLY E  1 74  ? 37.347  -42.700 9.760   1.00 2.00  ? 73  GLY C O   1 
ATOM   4988  N  N   . PRO E  1 75  ? 38.915  -43.263 11.176  1.00 2.00  ? 74  PRO C N   1 
ATOM   4989  C  CA  . PRO E  1 75  ? 39.964  -43.033 10.221  1.00 4.32  ? 74  PRO C CA  1 
ATOM   4990  C  C   . PRO E  1 75  ? 39.955  -44.037 9.074   1.00 6.61  ? 74  PRO C C   1 
ATOM   4991  O  O   . PRO E  1 75  ? 40.608  -43.844 8.046   1.00 9.10  ? 74  PRO C O   1 
ATOM   4992  C  CB  . PRO E  1 75  ? 41.231  -43.059 11.055  1.00 2.00  ? 74  PRO C CB  1 
ATOM   4993  C  CG  . PRO E  1 75  ? 40.881  -43.980 12.164  1.00 2.00  ? 74  PRO C CG  1 
ATOM   4994  C  CD  . PRO E  1 75  ? 39.450  -43.577 12.499  1.00 3.98  ? 74  PRO C CD  1 
ATOM   4995  N  N   . LYS E  1 76  ? 39.260  -45.153 9.246   1.00 7.68  ? 75  LYS C N   1 
ATOM   4996  C  CA  . LYS E  1 76  ? 39.249  -46.194 8.257   1.00 9.59  ? 75  LYS C CA  1 
ATOM   4997  C  C   . LYS E  1 76  ? 38.296  -45.800 7.133   1.00 10.38 ? 75  LYS C C   1 
ATOM   4998  O  O   . LYS E  1 76  ? 38.312  -46.424 6.073   1.00 11.78 ? 75  LYS C O   1 
ATOM   4999  C  CB  . LYS E  1 76  ? 38.792  -47.480 8.906   1.00 12.21 ? 75  LYS C CB  1 
ATOM   5000  C  CG  . LYS E  1 76  ? 39.717  -48.334 9.769   1.00 16.75 ? 75  LYS C CG  1 
ATOM   5001  C  CD  . LYS E  1 76  ? 38.962  -49.657 10.158  1.00 24.27 ? 75  LYS C CD  1 
ATOM   5002  C  CE  . LYS E  1 76  ? 39.706  -50.741 11.005  1.00 28.09 ? 75  LYS C CE  1 
ATOM   5003  N  NZ  . LYS E  1 76  ? 38.825  -51.819 11.474  1.00 31.12 ? 75  LYS C NZ  1 
ATOM   5004  N  N   . ASP E  1 77  ? 37.480  -44.762 7.345   1.00 10.48 ? 76  ASP C N   1 
ATOM   5005  C  CA  . ASP E  1 77  ? 36.452  -44.327 6.425   1.00 10.54 ? 76  ASP C CA  1 
ATOM   5006  C  C   . ASP E  1 77  ? 36.874  -43.317 5.410   1.00 12.02 ? 76  ASP C C   1 
ATOM   5007  O  O   . ASP E  1 77  ? 37.920  -42.694 5.533   1.00 13.78 ? 76  ASP C O   1 
ATOM   5008  C  CB  . ASP E  1 77  ? 35.287  -43.677 7.122   1.00 11.54 ? 76  ASP C CB  1 
ATOM   5009  C  CG  . ASP E  1 77  ? 34.579  -44.589 8.076   1.00 12.90 ? 76  ASP C CG  1 
ATOM   5010  O  OD1 . ASP E  1 77  ? 34.507  -45.798 7.822   1.00 15.99 ? 76  ASP C OD1 1 
ATOM   5011  O  OD2 . ASP E  1 77  ? 34.116  -44.071 9.086   1.00 13.84 ? 76  ASP C OD2 1 
ATOM   5012  N  N   . GLU E  1 78  ? 35.982  -43.144 4.430   1.00 12.71 ? 77  GLU C N   1 
ATOM   5013  C  CA  . GLU E  1 78  ? 36.145  -42.177 3.382   1.00 14.80 ? 77  GLU C CA  1 
ATOM   5014  C  C   . GLU E  1 78  ? 35.534  -40.828 3.726   1.00 14.76 ? 77  GLU C C   1 
ATOM   5015  O  O   . GLU E  1 78  ? 35.973  -39.758 3.272   1.00 13.16 ? 77  GLU C O   1 
ATOM   5016  C  CB  . GLU E  1 78  ? 35.511  -42.678 2.146   1.00 20.32 ? 77  GLU C CB  1 
ATOM   5017  C  CG  . GLU E  1 78  ? 36.479  -43.600 1.447   1.00 32.88 ? 77  GLU C CG  1 
ATOM   5018  C  CD  . GLU E  1 78  ? 36.092  -43.778 -0.019  1.00 39.82 ? 77  GLU C CD  1 
ATOM   5019  O  OE1 . GLU E  1 78  ? 36.421  -42.869 -0.792  1.00 42.82 ? 77  GLU C OE1 1 
ATOM   5020  O  OE2 . GLU E  1 78  ? 35.468  -44.799 -0.370  1.00 42.64 ? 77  GLU C OE2 1 
ATOM   5021  N  N   . GLU E  1 79  ? 34.480  -40.936 4.537   1.00 11.49 ? 78  GLU C N   1 
ATOM   5022  C  CA  . GLU E  1 79  ? 33.803  -39.785 5.038   1.00 7.18  ? 78  GLU C CA  1 
ATOM   5023  C  C   . GLU E  1 79  ? 34.276  -39.666 6.448   1.00 4.52  ? 78  GLU C C   1 
ATOM   5024  O  O   . GLU E  1 79  ? 33.801  -40.247 7.413   1.00 5.12  ? 78  GLU C O   1 
ATOM   5025  C  CB  . GLU E  1 79  ? 32.305  -39.972 5.018   1.00 9.54  ? 78  GLU C CB  1 
ATOM   5026  C  CG  . GLU E  1 79  ? 31.495  -38.685 5.165   1.00 12.49 ? 78  GLU C CG  1 
ATOM   5027  C  CD  . GLU E  1 79  ? 31.603  -37.651 4.035   1.00 14.83 ? 78  GLU C CD  1 
ATOM   5028  O  OE1 . GLU E  1 79  ? 32.318  -37.875 3.047   1.00 19.15 ? 78  GLU C OE1 1 
ATOM   5029  O  OE2 . GLU E  1 79  ? 30.964  -36.594 4.137   1.00 16.97 ? 78  GLU C OE2 1 
ATOM   5030  N  N   . ARG E  1 80  ? 35.364  -38.975 6.453   1.00 3.87  ? 79  ARG C N   1 
ATOM   5031  C  CA  . ARG E  1 80  ? 35.978  -38.581 7.682   1.00 4.41  ? 79  ARG C CA  1 
ATOM   5032  C  C   . ARG E  1 80  ? 36.552  -37.166 7.490   1.00 5.93  ? 79  ARG C C   1 
ATOM   5033  O  O   . ARG E  1 80  ? 36.748  -36.661 6.355   1.00 8.10  ? 79  ARG C O   1 
ATOM   5034  C  CB  . ARG E  1 80  ? 37.035  -39.629 7.983   1.00 2.01  ? 79  ARG C CB  1 
ATOM   5035  C  CG  . ARG E  1 80  ? 38.128  -39.787 6.965   1.00 2.00  ? 79  ARG C CG  1 
ATOM   5036  C  CD  . ARG E  1 80  ? 39.248  -39.453 7.873   1.00 2.00  ? 79  ARG C CD  1 
ATOM   5037  N  NE  . ARG E  1 80  ? 40.341  -40.374 7.851   1.00 2.00  ? 79  ARG C NE  1 
ATOM   5038  C  CZ  . ARG E  1 80  ? 41.512  -40.047 8.382   1.00 2.01  ? 79  ARG C CZ  1 
ATOM   5039  N  NH1 . ARG E  1 80  ? 41.852  -38.899 8.945   1.00 2.00  ? 79  ARG C NH1 1 
ATOM   5040  N  NH2 . ARG E  1 80  ? 42.438  -40.940 8.317   1.00 7.17  ? 79  ARG C NH2 1 
ATOM   5041  N  N   . HIS E  1 81  ? 36.784  -36.497 8.615   1.00 3.66  ? 80  HIS C N   1 
ATOM   5042  C  CA  . HIS E  1 81  ? 37.574  -35.267 8.650   1.00 3.36  ? 80  HIS C CA  1 
ATOM   5043  C  C   . HIS E  1 81  ? 39.063  -35.637 8.567   1.00 3.58  ? 80  HIS C C   1 
ATOM   5044  O  O   . HIS E  1 81  ? 39.422  -36.743 8.976   1.00 2.53  ? 80  HIS C O   1 
ATOM   5045  C  CB  . HIS E  1 81  ? 37.456  -34.529 9.924   1.00 2.00  ? 80  HIS C CB  1 
ATOM   5046  C  CG  . HIS E  1 81  ? 36.063  -34.205 10.388  1.00 2.77  ? 80  HIS C CG  1 
ATOM   5047  N  ND1 . HIS E  1 81  ? 35.677  -34.208 11.640  1.00 2.04  ? 80  HIS C ND1 1 
ATOM   5048  C  CD2 . HIS E  1 81  ? 35.025  -33.798 9.615   1.00 2.14  ? 80  HIS C CD2 1 
ATOM   5049  C  CE1 . HIS E  1 81  ? 34.442  -33.798 11.660  1.00 2.10  ? 80  HIS C CE1 1 
ATOM   5050  N  NE2 . HIS E  1 81  ? 34.064  -33.558 10.439  1.00 2.06  ? 80  HIS C NE2 1 
ATOM   5051  N  N   . VAL E  1 82  ? 39.980  -34.778 8.142   1.00 2.49  ? 81  VAL C N   1 
ATOM   5052  C  CA  . VAL E  1 82  ? 41.389  -35.170 8.077   1.00 3.45  ? 81  VAL C CA  1 
ATOM   5053  C  C   . VAL E  1 82  ? 41.965  -35.400 9.465   1.00 2.56  ? 81  VAL C C   1 
ATOM   5054  O  O   . VAL E  1 82  ? 42.824  -36.251 9.616   1.00 2.00  ? 81  VAL C O   1 
ATOM   5055  C  CB  . VAL E  1 82  ? 42.190  -34.086 7.324   1.00 2.00  ? 81  VAL C CB  1 
ATOM   5056  C  CG1 . VAL E  1 82  ? 43.678  -34.330 7.361   1.00 2.00  ? 81  VAL C CG1 1 
ATOM   5057  C  CG2 . VAL E  1 82  ? 41.735  -34.104 5.876   1.00 2.00  ? 81  VAL C CG2 1 
ATOM   5058  N  N   . GLY E  1 83  ? 41.464  -34.712 10.496  1.00 3.34  ? 82  GLY C N   1 
ATOM   5059  C  CA  . GLY E  1 83  ? 41.945  -34.816 11.875  1.00 3.26  ? 82  GLY C CA  1 
ATOM   5060  C  C   . GLY E  1 83  ? 41.311  -35.956 12.680  1.00 3.95  ? 82  GLY C C   1 
ATOM   5061  O  O   . GLY E  1 83  ? 41.307  -36.002 13.924  1.00 5.22  ? 82  GLY C O   1 
ATOM   5062  N  N   . ASP E  1 84  ? 40.693  -36.907 12.024  1.00 2.34  ? 83  ASP C N   1 
ATOM   5063  C  CA  . ASP E  1 84  ? 40.022  -37.965 12.717  1.00 2.00  ? 83  ASP C CA  1 
ATOM   5064  C  C   . ASP E  1 84  ? 40.958  -39.145 12.855  1.00 2.00  ? 83  ASP C C   1 
ATOM   5065  O  O   . ASP E  1 84  ? 40.980  -40.043 12.028  1.00 2.00  ? 83  ASP C O   1 
ATOM   5066  C  CB  . ASP E  1 84  ? 38.805  -38.455 11.987  1.00 2.00  ? 83  ASP C CB  1 
ATOM   5067  C  CG  . ASP E  1 84  ? 37.543  -37.643 11.825  1.00 2.20  ? 83  ASP C CG  1 
ATOM   5068  O  OD1 . ASP E  1 84  ? 37.226  -36.652 12.504  1.00 2.68  ? 83  ASP C OD1 1 
ATOM   5069  O  OD2 . ASP E  1 84  ? 36.824  -38.092 10.955  1.00 4.71  ? 83  ASP C OD2 1 
ATOM   5070  N  N   . LEU E  1 85  ? 41.734  -39.145 13.927  1.00 2.65  ? 84  LEU C N   1 
ATOM   5071  C  CA  . LEU E  1 85  ? 42.561  -40.289 14.178  1.00 2.82  ? 84  LEU C CA  1 
ATOM   5072  C  C   . LEU E  1 85  ? 41.851  -41.347 15.009  1.00 2.00  ? 84  LEU C C   1 
ATOM   5073  O  O   . LEU E  1 85  ? 42.370  -42.450 15.181  1.00 2.00  ? 84  LEU C O   1 
ATOM   5074  C  CB  . LEU E  1 85  ? 43.850  -39.811 14.804  1.00 2.00  ? 84  LEU C CB  1 
ATOM   5075  C  CG  . LEU E  1 85  ? 44.600  -38.943 13.838  1.00 2.01  ? 84  LEU C CG  1 
ATOM   5076  C  CD1 . LEU E  1 85  ? 45.787  -38.300 14.539  1.00 2.00  ? 84  LEU C CD1 1 
ATOM   5077  C  CD2 . LEU E  1 85  ? 44.958  -39.782 12.629  1.00 2.48  ? 84  LEU C CD2 1 
ATOM   5078  N  N   . GLY E  1 86  ? 40.636  -41.066 15.449  1.00 2.00  ? 85  GLY C N   1 
ATOM   5079  C  CA  . GLY E  1 86  ? 39.769  -42.103 15.979  1.00 2.77  ? 85  GLY C CA  1 
ATOM   5080  C  C   . GLY E  1 86  ? 39.803  -42.297 17.476  1.00 2.00  ? 85  GLY C C   1 
ATOM   5081  O  O   . GLY E  1 86  ? 39.383  -41.388 18.159  1.00 2.00  ? 85  GLY C O   1 
ATOM   5082  N  N   . ASN E  1 87  ? 40.292  -43.414 18.015  1.00 3.64  ? 86  ASN C N   1 
ATOM   5083  C  CA  . ASN E  1 87  ? 40.301  -43.683 19.443  1.00 2.83  ? 86  ASN C CA  1 
ATOM   5084  C  C   . ASN E  1 87  ? 41.639  -44.246 19.834  1.00 2.00  ? 86  ASN C C   1 
ATOM   5085  O  O   . ASN E  1 87  ? 42.312  -44.789 18.967  1.00 2.00  ? 86  ASN C O   1 
ATOM   5086  C  CB  . ASN E  1 87  ? 39.278  -44.700 19.829  1.00 2.00  ? 86  ASN C CB  1 
ATOM   5087  C  CG  . ASN E  1 87  ? 37.902  -44.134 19.910  1.00 2.00  ? 86  ASN C CG  1 
ATOM   5088  O  OD1 . ASN E  1 87  ? 37.616  -43.165 20.609  1.00 6.93  ? 86  ASN C OD1 1 
ATOM   5089  N  ND2 . ASN E  1 87  ? 36.982  -44.701 19.191  1.00 2.00  ? 86  ASN C ND2 1 
ATOM   5090  N  N   . VAL E  1 88  ? 42.051  -44.042 21.086  1.00 2.00  ? 87  VAL C N   1 
ATOM   5091  C  CA  . VAL E  1 88  ? 43.258  -44.592 21.689  1.00 2.00  ? 87  VAL C CA  1 
ATOM   5092  C  C   . VAL E  1 88  ? 42.712  -45.273 22.940  1.00 2.27  ? 87  VAL C C   1 
ATOM   5093  O  O   . VAL E  1 88  ? 41.663  -44.866 23.489  1.00 2.00  ? 87  VAL C O   1 
ATOM   5094  C  CB  . VAL E  1 88  ? 44.306  -43.525 22.107  1.00 2.00  ? 87  VAL C CB  1 
ATOM   5095  C  CG1 . VAL E  1 88  ? 44.777  -42.966 20.814  1.00 2.00  ? 87  VAL C CG1 1 
ATOM   5096  C  CG2 . VAL E  1 88  ? 43.807  -42.380 22.986  1.00 2.00  ? 87  VAL C CG2 1 
ATOM   5097  N  N   . THR E  1 89  ? 43.361  -46.334 23.397  1.00 2.00  ? 88  THR C N   1 
ATOM   5098  C  CA  . THR E  1 89  ? 42.819  -47.112 24.487  1.00 2.19  ? 88  THR C CA  1 
ATOM   5099  C  C   . THR E  1 89  ? 43.779  -47.042 25.607  1.00 2.20  ? 88  THR C C   1 
ATOM   5100  O  O   . THR E  1 89  ? 44.986  -47.251 25.407  1.00 5.78  ? 88  THR C O   1 
ATOM   5101  C  CB  . THR E  1 89  ? 42.647  -48.524 24.018  1.00 5.98  ? 88  THR C CB  1 
ATOM   5102  O  OG1 . THR E  1 89  ? 41.619  -48.308 23.052  1.00 8.69  ? 88  THR C OG1 1 
ATOM   5103  C  CG2 . THR E  1 89  ? 42.333  -49.615 25.080  1.00 2.47  ? 88  THR C CG2 1 
ATOM   5104  N  N   . ALA E  1 90  ? 43.213  -46.699 26.758  1.00 2.00  ? 89  ALA C N   1 
ATOM   5105  C  CA  . ALA E  1 90  ? 43.999  -46.497 27.951  1.00 2.35  ? 89  ALA C CA  1 
ATOM   5106  C  C   . ALA E  1 90  ? 43.765  -47.670 28.863  1.00 3.55  ? 89  ALA C C   1 
ATOM   5107  O  O   . ALA E  1 90  ? 42.623  -48.032 29.182  1.00 2.00  ? 89  ALA C O   1 
ATOM   5108  C  CB  . ALA E  1 90  ? 43.545  -45.218 28.589  1.00 4.63  ? 89  ALA C CB  1 
ATOM   5109  N  N   . ASP E  1 91  ? 44.875  -48.318 29.177  1.00 5.91  ? 90  ASP C N   1 
ATOM   5110  C  CA  . ASP E  1 91  ? 44.825  -49.469 30.034  1.00 9.71  ? 90  ASP C CA  1 
ATOM   5111  C  C   . ASP E  1 91  ? 44.357  -49.204 31.472  1.00 13.09 ? 90  ASP C C   1 
ATOM   5112  O  O   . ASP E  1 91  ? 43.990  -48.109 31.908  1.00 11.92 ? 90  ASP C O   1 
ATOM   5113  C  CB  . ASP E  1 91  ? 46.216  -50.133 30.013  1.00 10.07 ? 90  ASP C CB  1 
ATOM   5114  C  CG  . ASP E  1 91  ? 47.448  -49.495 30.651  1.00 12.43 ? 90  ASP C CG  1 
ATOM   5115  O  OD1 . ASP E  1 91  ? 47.319  -48.779 31.651  1.00 14.82 ? 90  ASP C OD1 1 
ATOM   5116  O  OD2 . ASP E  1 91  ? 48.558  -49.748 30.153  1.00 12.81 ? 90  ASP C OD2 1 
ATOM   5117  N  N   . LYS E  1 92  ? 44.464  -50.251 32.265  1.00 18.35 ? 91  LYS C N   1 
ATOM   5118  C  CA  . LYS E  1 92  ? 44.004  -50.246 33.633  1.00 23.30 ? 91  LYS C CA  1 
ATOM   5119  C  C   . LYS E  1 92  ? 44.687  -49.194 34.476  1.00 23.03 ? 91  LYS C C   1 
ATOM   5120  O  O   . LYS E  1 92  ? 43.975  -48.580 35.279  1.00 24.51 ? 91  LYS C O   1 
ATOM   5121  C  CB  . LYS E  1 92  ? 44.222  -51.636 34.234  1.00 27.93 ? 91  LYS C CB  1 
ATOM   5122  C  CG  . LYS E  1 92  ? 43.408  -52.747 33.530  1.00 36.12 ? 91  LYS C CG  1 
ATOM   5123  C  CD  . LYS E  1 92  ? 44.159  -54.095 33.615  1.00 43.16 ? 91  LYS C CD  1 
ATOM   5124  C  CE  . LYS E  1 92  ? 43.541  -55.384 32.985  1.00 45.50 ? 91  LYS C CE  1 
ATOM   5125  N  NZ  . LYS E  1 92  ? 44.162  -56.587 33.579  1.00 45.22 ? 91  LYS C NZ  1 
ATOM   5126  N  N   . ASP E  1 93  ? 46.006  -48.917 34.357  1.00 22.53 ? 92  ASP C N   1 
ATOM   5127  C  CA  . ASP E  1 93  ? 46.610  -47.845 35.179  1.00 22.20 ? 92  ASP C CA  1 
ATOM   5128  C  C   . ASP E  1 93  ? 46.287  -46.446 34.662  1.00 21.06 ? 92  ASP C C   1 
ATOM   5129  O  O   . ASP E  1 93  ? 46.642  -45.478 35.323  1.00 23.26 ? 92  ASP C O   1 
ATOM   5130  C  CB  . ASP E  1 93  ? 48.120  -47.902 35.238  1.00 25.23 ? 92  ASP C CB  1 
ATOM   5131  C  CG  . ASP E  1 93  ? 48.703  -49.290 35.469  1.00 29.90 ? 92  ASP C CG  1 
ATOM   5132  O  OD1 . ASP E  1 93  ? 48.436  -49.915 36.504  1.00 32.19 ? 92  ASP C OD1 1 
ATOM   5133  O  OD2 . ASP E  1 93  ? 49.437  -49.746 34.586  1.00 34.65 ? 92  ASP C OD2 1 
ATOM   5134  N  N   . GLY E  1 94  ? 45.611  -46.329 33.505  1.00 18.12 ? 93  GLY C N   1 
ATOM   5135  C  CA  . GLY E  1 94  ? 45.244  -45.065 32.927  1.00 14.18 ? 93  GLY C CA  1 
ATOM   5136  C  C   . GLY E  1 94  ? 46.236  -44.628 31.879  1.00 11.96 ? 93  GLY C C   1 
ATOM   5137  O  O   . GLY E  1 94  ? 46.371  -43.430 31.616  1.00 12.79 ? 93  GLY C O   1 
ATOM   5138  N  N   . VAL E  1 95  ? 46.935  -45.574 31.251  1.00 9.24  ? 94  VAL C N   1 
ATOM   5139  C  CA  . VAL E  1 95  ? 48.001  -45.238 30.303  1.00 7.66  ? 94  VAL C CA  1 
ATOM   5140  C  C   . VAL E  1 95  ? 47.639  -45.693 28.925  1.00 5.70  ? 94  VAL C C   1 
ATOM   5141  O  O   . VAL E  1 95  ? 47.284  -46.864 28.777  1.00 2.77  ? 94  VAL C O   1 
ATOM   5142  C  CB  . VAL E  1 95  ? 49.315  -45.918 30.652  1.00 7.06  ? 94  VAL C CB  1 
ATOM   5143  C  CG1 . VAL E  1 95  ? 50.426  -45.554 29.688  1.00 2.00  ? 94  VAL C CG1 1 
ATOM   5144  C  CG2 . VAL E  1 95  ? 49.618  -45.536 32.088  1.00 5.66  ? 94  VAL C CG2 1 
ATOM   5145  N  N   . ALA E  1 96  ? 47.743  -44.780 27.965  1.00 4.24  ? 95  ALA C N   1 
ATOM   5146  C  CA  . ALA E  1 96  ? 47.376  -45.085 26.598  1.00 6.67  ? 95  ALA C CA  1 
ATOM   5147  C  C   . ALA E  1 96  ? 48.626  -45.034 25.768  1.00 6.66  ? 95  ALA C C   1 
ATOM   5148  O  O   . ALA E  1 96  ? 49.253  -43.975 25.680  1.00 4.91  ? 95  ALA C O   1 
ATOM   5149  C  CB  . ALA E  1 96  ? 46.393  -44.061 26.057  1.00 5.89  ? 95  ALA C CB  1 
ATOM   5150  N  N   . ASP E  1 97  ? 48.983  -46.184 25.211  1.00 6.92  ? 96  ASP C N   1 
ATOM   5151  C  CA  . ASP E  1 97  ? 50.198  -46.300 24.445  1.00 9.52  ? 96  ASP C CA  1 
ATOM   5152  C  C   . ASP E  1 97  ? 49.807  -46.283 22.985  1.00 9.77  ? 96  ASP C C   1 
ATOM   5153  O  O   . ASP E  1 97  ? 49.589  -47.341 22.380  1.00 10.61 ? 96  ASP C O   1 
ATOM   5154  C  CB  . ASP E  1 97  ? 50.906  -47.599 24.712  1.00 15.93 ? 96  ASP C CB  1 
ATOM   5155  C  CG  . ASP E  1 97  ? 51.396  -47.804 26.131  1.00 23.11 ? 96  ASP C CG  1 
ATOM   5156  O  OD1 . ASP E  1 97  ? 52.119  -46.947 26.654  1.00 25.80 ? 96  ASP C OD1 1 
ATOM   5157  O  OD2 . ASP E  1 97  ? 51.071  -48.860 26.698  1.00 29.94 ? 96  ASP C OD2 1 
ATOM   5158  N  N   . VAL E  1 98  ? 49.802  -45.082 22.418  1.00 7.50  ? 97  VAL C N   1 
ATOM   5159  C  CA  . VAL E  1 98  ? 49.328  -44.820 21.078  1.00 3.32  ? 97  VAL C CA  1 
ATOM   5160  C  C   . VAL E  1 98  ? 50.214  -45.453 20.010  1.00 2.67  ? 97  VAL C C   1 
ATOM   5161  O  O   . VAL E  1 98  ? 51.431  -45.510 20.164  1.00 2.54  ? 97  VAL C O   1 
ATOM   5162  C  CB  . VAL E  1 98  ? 49.240  -43.288 20.945  1.00 2.92  ? 97  VAL C CB  1 
ATOM   5163  C  CG1 . VAL E  1 98  ? 48.493  -42.998 19.679  1.00 2.00  ? 97  VAL C CG1 1 
ATOM   5164  C  CG2 . VAL E  1 98  ? 48.475  -42.612 22.085  1.00 2.00  ? 97  VAL C CG2 1 
ATOM   5165  N  N   . SER E  1 99  ? 49.623  -45.987 18.941  1.00 2.82  ? 98  SER C N   1 
ATOM   5166  C  CA  . SER E  1 99  ? 50.343  -46.457 17.768  1.00 5.78  ? 98  SER C CA  1 
ATOM   5167  C  C   . SER E  1 99  ? 49.408  -46.493 16.553  1.00 7.35  ? 98  SER C C   1 
ATOM   5168  O  O   . SER E  1 99  ? 48.767  -47.504 16.214  1.00 10.55 ? 98  SER C O   1 
ATOM   5169  C  CB  . SER E  1 99  ? 50.882  -47.835 17.995  1.00 4.58  ? 98  SER C CB  1 
ATOM   5170  O  OG  . SER E  1 99  ? 51.795  -48.175 16.969  1.00 10.84 ? 98  SER C OG  1 
ATOM   5171  N  N   . ILE E  1 100 ? 49.353  -45.374 15.844  1.00 5.06  ? 99  ILE C N   1 
ATOM   5172  C  CA  . ILE E  1 100 ? 48.412  -45.209 14.756  1.00 6.05  ? 99  ILE C CA  1 
ATOM   5173  C  C   . ILE E  1 100 ? 49.281  -45.019 13.536  1.00 5.59  ? 99  ILE C C   1 
ATOM   5174  O  O   . ILE E  1 100 ? 50.399  -44.545 13.660  1.00 8.02  ? 99  ILE C O   1 
ATOM   5175  C  CB  . ILE E  1 100 ? 47.538  -43.961 15.036  1.00 6.14  ? 99  ILE C CB  1 
ATOM   5176  C  CG1 . ILE E  1 100 ? 46.711  -44.242 16.277  1.00 5.40  ? 99  ILE C CG1 1 
ATOM   5177  C  CG2 . ILE E  1 100 ? 46.628  -43.624 13.874  1.00 3.21  ? 99  ILE C CG2 1 
ATOM   5178  C  CD1 . ILE E  1 100 ? 46.098  -42.945 16.814  1.00 8.37  ? 99  ILE C CD1 1 
ATOM   5179  N  N   . GLU E  1 101 ? 48.857  -45.388 12.348  1.00 6.86  ? 100 GLU C N   1 
ATOM   5180  C  CA  . GLU E  1 101 ? 49.603  -45.081 11.161  1.00 7.09  ? 100 GLU C CA  1 
ATOM   5181  C  C   . GLU E  1 101 ? 48.506  -44.554 10.267  1.00 3.61  ? 100 GLU C C   1 
ATOM   5182  O  O   . GLU E  1 101 ? 47.614  -45.301 9.922   1.00 2.68  ? 100 GLU C O   1 
ATOM   5183  C  CB  . GLU E  1 101 ? 50.209  -46.334 10.619  1.00 13.78 ? 100 GLU C CB  1 
ATOM   5184  C  CG  . GLU E  1 101 ? 51.059  -45.995 9.411   1.00 20.00 ? 100 GLU C CG  1 
ATOM   5185  C  CD  . GLU E  1 101 ? 51.408  -47.225 8.606   1.00 24.19 ? 100 GLU C CD  1 
ATOM   5186  O  OE1 . GLU E  1 101 ? 50.619  -47.573 7.718   1.00 26.67 ? 100 GLU C OE1 1 
ATOM   5187  O  OE2 . GLU E  1 101 ? 52.460  -47.811 8.882   1.00 25.27 ? 100 GLU C OE2 1 
ATOM   5188  N  N   . ASP E  1 102 ? 48.491  -43.288 9.928   1.00 2.00  ? 101 ASP C N   1 
ATOM   5189  C  CA  . ASP E  1 102 ? 47.429  -42.729 9.147   1.00 2.00  ? 101 ASP C CA  1 
ATOM   5190  C  C   . ASP E  1 102 ? 47.991  -42.163 7.874   1.00 3.38  ? 101 ASP C C   1 
ATOM   5191  O  O   . ASP E  1 102 ? 49.066  -41.570 7.884   1.00 6.55  ? 101 ASP C O   1 
ATOM   5192  C  CB  . ASP E  1 102 ? 46.764  -41.605 9.871   1.00 4.89  ? 101 ASP C CB  1 
ATOM   5193  C  CG  . ASP E  1 102 ? 45.416  -41.278 9.290   1.00 4.84  ? 101 ASP C CG  1 
ATOM   5194  O  OD1 . ASP E  1 102 ? 44.455  -41.939 9.674   1.00 9.62  ? 101 ASP C OD1 1 
ATOM   5195  O  OD2 . ASP E  1 102 ? 45.331  -40.403 8.462   1.00 2.00  ? 101 ASP C OD2 1 
ATOM   5196  N  N   . SER E  1 103 ? 47.285  -42.295 6.773   1.00 3.97  ? 102 SER C N   1 
ATOM   5197  C  CA  . SER E  1 103 ? 47.704  -41.693 5.513   1.00 5.62  ? 102 SER C CA  1 
ATOM   5198  C  C   . SER E  1 103 ? 46.909  -40.461 5.050   1.00 4.40  ? 102 SER C C   1 
ATOM   5199  O  O   . SER E  1 103 ? 47.215  -39.838 4.020   1.00 7.62  ? 102 SER C O   1 
ATOM   5200  C  CB  . SER E  1 103 ? 47.640  -42.775 4.447   1.00 4.60  ? 102 SER C CB  1 
ATOM   5201  O  OG  . SER E  1 103 ? 46.581  -43.662 4.790   1.00 13.75 ? 102 SER C OG  1 
ATOM   5202  N  N   . VAL E  1 104 ? 45.793  -40.115 5.692   1.00 2.00  ? 103 VAL C N   1 
ATOM   5203  C  CA  . VAL E  1 104 ? 45.153  -38.872 5.298   1.00 3.91  ? 103 VAL C CA  1 
ATOM   5204  C  C   . VAL E  1 104 ? 45.888  -37.638 5.827   1.00 3.20  ? 103 VAL C C   1 
ATOM   5205  O  O   . VAL E  1 104 ? 46.041  -36.668 5.066   1.00 8.24  ? 103 VAL C O   1 
ATOM   5206  C  CB  . VAL E  1 104 ? 43.714  -38.837 5.822   1.00 2.00  ? 103 VAL C CB  1 
ATOM   5207  C  CG1 . VAL E  1 104 ? 43.097  -37.477 5.507   1.00 2.00  ? 103 VAL C CG1 1 
ATOM   5208  C  CG2 . VAL E  1 104 ? 42.948  -39.944 5.189   1.00 2.00  ? 103 VAL C CG2 1 
ATOM   5209  N  N   . ILE E  1 105 ? 46.338  -37.625 7.065   1.00 2.99  ? 104 ILE C N   1 
ATOM   5210  C  CA  . ILE E  1 105 ? 47.099  -36.515 7.603   1.00 2.96  ? 104 ILE C CA  1 
ATOM   5211  C  C   . ILE E  1 105 ? 48.459  -36.502 6.891   1.00 3.84  ? 104 ILE C C   1 
ATOM   5212  O  O   . ILE E  1 105 ? 48.860  -37.479 6.253   1.00 3.28  ? 104 ILE C O   1 
ATOM   5213  C  CB  . ILE E  1 105 ? 47.242  -36.675 9.161   1.00 2.00  ? 104 ILE C CB  1 
ATOM   5214  C  CG1 . ILE E  1 105 ? 47.732  -38.037 9.602   1.00 2.00  ? 104 ILE C CG1 1 
ATOM   5215  C  CG2 . ILE E  1 105 ? 45.861  -36.421 9.768   1.00 2.00  ? 104 ILE C CG2 1 
ATOM   5216  C  CD1 . ILE E  1 105 ? 48.118  -38.122 11.086  1.00 2.00  ? 104 ILE C CD1 1 
ATOM   5217  N  N   . SER E  1 106 ? 49.116  -35.343 6.861   1.00 5.23  ? 105 SER C N   1 
ATOM   5218  C  CA  . SER E  1 106 ? 50.462  -35.252 6.342   1.00 4.42  ? 105 SER C CA  1 
ATOM   5219  C  C   . SER E  1 106 ? 51.166  -34.280 7.282   1.00 3.48  ? 105 SER C C   1 
ATOM   5220  O  O   . SER E  1 106 ? 50.546  -33.604 8.123   1.00 4.03  ? 105 SER C O   1 
ATOM   5221  C  CB  . SER E  1 106 ? 50.477  -34.718 4.906   1.00 2.00  ? 105 SER C CB  1 
ATOM   5222  O  OG  . SER E  1 106 ? 51.746  -35.050 4.313   1.00 2.00  ? 105 SER C OG  1 
ATOM   5223  N  N   . LEU E  1 107 ? 52.489  -34.258 7.195   1.00 2.00  ? 106 LEU C N   1 
ATOM   5224  C  CA  . LEU E  1 107 ? 53.253  -33.271 7.917   1.00 2.67  ? 106 LEU C CA  1 
ATOM   5225  C  C   . LEU E  1 107 ? 53.701  -32.189 6.961   1.00 3.59  ? 106 LEU C C   1 
ATOM   5226  O  O   . LEU E  1 107 ? 54.469  -31.321 7.378   1.00 5.46  ? 106 LEU C O   1 
ATOM   5227  C  CB  . LEU E  1 107 ? 54.480  -33.883 8.594   1.00 2.00  ? 106 LEU C CB  1 
ATOM   5228  C  CG  . LEU E  1 107 ? 54.190  -34.856 9.756   1.00 2.00  ? 106 LEU C CG  1 
ATOM   5229  C  CD1 . LEU E  1 107 ? 55.474  -35.064 10.476  1.00 2.00  ? 106 LEU C CD1 1 
ATOM   5230  C  CD2 . LEU E  1 107 ? 53.095  -34.349 10.685  1.00 2.00  ? 106 LEU C CD2 1 
ATOM   5231  N  N   . SER E  1 108 ? 53.127  -32.174 5.745   1.00 2.00  ? 107 SER C N   1 
ATOM   5232  C  CA  . SER E  1 108 ? 53.458  -31.285 4.659   1.00 3.49  ? 107 SER C CA  1 
ATOM   5233  C  C   . SER E  1 108 ? 52.212  -31.173 3.781   1.00 6.02  ? 107 SER C C   1 
ATOM   5234  O  O   . SER E  1 108 ? 51.367  -32.090 3.628   1.00 4.68  ? 107 SER C O   1 
ATOM   5235  C  CB  . SER E  1 108 ? 54.555  -31.820 3.730   1.00 3.81  ? 107 SER C CB  1 
ATOM   5236  O  OG  . SER E  1 108 ? 55.404  -32.765 4.361   1.00 7.77  ? 107 SER C OG  1 
ATOM   5237  N  N   . GLY E  1 109 ? 52.148  -29.967 3.206   1.00 5.23  ? 108 GLY C N   1 
ATOM   5238  C  CA  . GLY E  1 109 ? 51.143  -29.627 2.214   1.00 5.50  ? 108 GLY C CA  1 
ATOM   5239  C  C   . GLY E  1 109 ? 49.791  -29.372 2.847   1.00 9.06  ? 108 GLY C C   1 
ATOM   5240  O  O   . GLY E  1 109 ? 49.649  -29.263 4.059   1.00 12.85 ? 108 GLY C O   1 
ATOM   5241  N  N   . ASP E  1 110 ? 48.778  -29.463 2.021   1.00 10.42 ? 109 ASP C N   1 
ATOM   5242  C  CA  . ASP E  1 110 ? 47.414  -29.114 2.321   1.00 13.20 ? 109 ASP C CA  1 
ATOM   5243  C  C   . ASP E  1 110 ? 46.848  -29.767 3.538   1.00 12.47 ? 109 ASP C C   1 
ATOM   5244  O  O   . ASP E  1 110 ? 46.072  -29.157 4.253   1.00 16.88 ? 109 ASP C O   1 
ATOM   5245  C  CB  . ASP E  1 110 ? 46.524  -29.446 1.102   1.00 17.47 ? 109 ASP C CB  1 
ATOM   5246  C  CG  . ASP E  1 110 ? 47.171  -28.937 -0.200  1.00 23.44 ? 109 ASP C CG  1 
ATOM   5247  O  OD1 . ASP E  1 110 ? 47.178  -27.695 -0.416  1.00 22.97 ? 109 ASP C OD1 1 
ATOM   5248  O  OD2 . ASP E  1 110 ? 47.715  -29.796 -0.932  1.00 19.10 ? 109 ASP C OD2 1 
ATOM   5249  N  N   . HIS E  1 111 ? 47.178  -31.014 3.776   1.00 11.09 ? 110 HIS C N   1 
ATOM   5250  C  CA  . HIS E  1 111 ? 46.661  -31.720 4.936   1.00 9.00  ? 110 HIS C CA  1 
ATOM   5251  C  C   . HIS E  1 111 ? 47.648  -31.601 6.106   1.00 6.26  ? 110 HIS C C   1 
ATOM   5252  O  O   . HIS E  1 111 ? 47.708  -32.491 6.949   1.00 5.20  ? 110 HIS C O   1 
ATOM   5253  C  CB  . HIS E  1 111 ? 46.448  -33.189 4.521   1.00 7.66  ? 110 HIS C CB  1 
ATOM   5254  C  CG  . HIS E  1 111 ? 45.288  -33.463 3.572   1.00 9.08  ? 110 HIS C CG  1 
ATOM   5255  N  ND1 . HIS E  1 111 ? 44.791  -34.667 3.336   1.00 9.19  ? 110 HIS C ND1 1 
ATOM   5256  C  CD2 . HIS E  1 111 ? 44.598  -32.549 2.788   1.00 9.14  ? 110 HIS C CD2 1 
ATOM   5257  C  CE1 . HIS E  1 111 ? 43.842  -34.523 2.437   1.00 10.79 ? 110 HIS C CE1 1 
ATOM   5258  N  NE2 . HIS E  1 111 ? 43.731  -33.258 2.111   1.00 9.86  ? 110 HIS C NE2 1 
ATOM   5259  N  N   . SER E  1 112 ? 48.483  -30.573 6.203   1.00 5.91  ? 111 SER C N   1 
ATOM   5260  C  CA  . SER E  1 112 ? 49.529  -30.634 7.194   1.00 6.43  ? 111 SER C CA  1 
ATOM   5261  C  C   . SER E  1 112 ? 48.936  -30.275 8.525   1.00 5.14  ? 111 SER C C   1 
ATOM   5262  O  O   . SER E  1 112 ? 48.160  -29.331 8.666   1.00 2.51  ? 111 SER C O   1 
ATOM   5263  C  CB  . SER E  1 112 ? 50.602  -29.677 6.895   1.00 8.47  ? 111 SER C CB  1 
ATOM   5264  O  OG  . SER E  1 112 ? 51.650  -29.816 7.833   1.00 12.54 ? 111 SER C OG  1 
ATOM   5265  N  N   . ILE E  1 113 ? 49.301  -31.098 9.486   1.00 3.25  ? 112 ILE C N   1 
ATOM   5266  C  CA  . ILE E  1 113 ? 48.800  -30.871 10.808  1.00 2.76  ? 112 ILE C CA  1 
ATOM   5267  C  C   . ILE E  1 113 ? 49.795  -30.093 11.641  1.00 4.65  ? 112 ILE C C   1 
ATOM   5268  O  O   . ILE E  1 113 ? 49.544  -29.890 12.826  1.00 7.56  ? 112 ILE C O   1 
ATOM   5269  C  CB  . ILE E  1 113 ? 48.489  -32.210 11.405  1.00 2.59  ? 112 ILE C CB  1 
ATOM   5270  C  CG1 . ILE E  1 113 ? 49.681  -33.128 11.372  1.00 2.00  ? 112 ILE C CG1 1 
ATOM   5271  C  CG2 . ILE E  1 113 ? 47.281  -32.757 10.623  1.00 2.87  ? 112 ILE C CG2 1 
ATOM   5272  C  CD1 . ILE E  1 113 ? 49.494  -34.247 12.346  1.00 2.00  ? 112 ILE C CD1 1 
ATOM   5273  N  N   . ILE E  1 114 ? 50.942  -29.631 11.122  1.00 4.35  ? 113 ILE C N   1 
ATOM   5274  C  CA  . ILE E  1 114 ? 51.934  -28.841 11.866  1.00 4.21  ? 113 ILE C CA  1 
ATOM   5275  C  C   . ILE E  1 114 ? 51.265  -27.552 12.318  1.00 2.00  ? 113 ILE C C   1 
ATOM   5276  O  O   . ILE E  1 114 ? 50.537  -26.946 11.550  1.00 3.66  ? 113 ILE C O   1 
ATOM   5277  C  CB  . ILE E  1 114 ? 53.183  -28.503 10.931  1.00 6.49  ? 113 ILE C CB  1 
ATOM   5278  C  CG1 . ILE E  1 114 ? 53.902  -29.807 10.546  1.00 3.61  ? 113 ILE C CG1 1 
ATOM   5279  C  CG2 . ILE E  1 114 ? 54.136  -27.487 11.579  1.00 3.70  ? 113 ILE C CG2 1 
ATOM   5280  C  CD1 . ILE E  1 114 ? 54.156  -30.801 11.636  1.00 6.19  ? 113 ILE C CD1 1 
ATOM   5281  N  N   . GLY E  1 115 ? 51.482  -27.096 13.519  1.00 2.00  ? 114 GLY C N   1 
ATOM   5282  C  CA  . GLY E  1 115 ? 50.826  -25.914 13.986  1.00 2.00  ? 114 GLY C CA  1 
ATOM   5283  C  C   . GLY E  1 115 ? 49.369  -26.139 14.333  1.00 2.08  ? 114 GLY C C   1 
ATOM   5284  O  O   . GLY E  1 115 ? 48.727  -25.142 14.639  1.00 2.44  ? 114 GLY C O   1 
ATOM   5285  N  N   . ARG E  1 116 ? 48.791  -27.345 14.275  1.00 2.00  ? 115 ARG C N   1 
ATOM   5286  C  CA  . ARG E  1 116 ? 47.434  -27.569 14.740  1.00 2.00  ? 115 ARG C CA  1 
ATOM   5287  C  C   . ARG E  1 116 ? 47.413  -28.246 16.103  1.00 2.00  ? 115 ARG C C   1 
ATOM   5288  O  O   . ARG E  1 116 ? 48.497  -28.473 16.654  1.00 2.00  ? 115 ARG C O   1 
ATOM   5289  C  CB  . ARG E  1 116 ? 46.670  -28.409 13.727  1.00 3.16  ? 115 ARG C CB  1 
ATOM   5290  C  CG  . ARG E  1 116 ? 46.603  -27.593 12.464  1.00 4.53  ? 115 ARG C CG  1 
ATOM   5291  C  CD  . ARG E  1 116 ? 45.690  -28.186 11.427  1.00 4.29  ? 115 ARG C CD  1 
ATOM   5292  N  NE  . ARG E  1 116 ? 45.940  -27.560 10.122  1.00 7.46  ? 115 ARG C NE  1 
ATOM   5293  C  CZ  . ARG E  1 116 ? 45.376  -26.438 9.661   1.00 2.00  ? 115 ARG C CZ  1 
ATOM   5294  N  NH1 . ARG E  1 116 ? 44.490  -25.740 10.351  1.00 2.00  ? 115 ARG C NH1 1 
ATOM   5295  N  NH2 . ARG E  1 116 ? 45.701  -26.033 8.457   1.00 2.00  ? 115 ARG C NH2 1 
ATOM   5296  N  N   . THR E  1 117 ? 46.262  -28.571 16.699  1.00 2.00  ? 116 THR C N   1 
ATOM   5297  C  CA  . THR E  1 117 ? 46.189  -29.130 18.049  1.00 2.00  ? 116 THR C CA  1 
ATOM   5298  C  C   . THR E  1 117 ? 45.808  -30.604 18.144  1.00 2.00  ? 116 THR C C   1 
ATOM   5299  O  O   . THR E  1 117 ? 44.753  -30.980 17.621  1.00 2.00  ? 116 THR C O   1 
ATOM   5300  C  CB  . THR E  1 117 ? 45.184  -28.286 18.841  1.00 2.00  ? 116 THR C CB  1 
ATOM   5301  O  OG1 . THR E  1 117 ? 45.712  -26.966 18.877  1.00 2.83  ? 116 THR C OG1 1 
ATOM   5302  C  CG2 . THR E  1 117 ? 45.006  -28.698 20.269  1.00 2.00  ? 116 THR C CG2 1 
ATOM   5303  N  N   . LEU E  1 118 ? 46.571  -31.483 18.811  1.00 2.00  ? 117 LEU C N   1 
ATOM   5304  C  CA  . LEU E  1 118 ? 46.139  -32.842 19.057  1.00 2.00  ? 117 LEU C CA  1 
ATOM   5305  C  C   . LEU E  1 118 ? 45.311  -32.763 20.346  1.00 2.47  ? 117 LEU C C   1 
ATOM   5306  O  O   . LEU E  1 118 ? 45.658  -32.051 21.283  1.00 2.00  ? 117 LEU C O   1 
ATOM   5307  C  CB  . LEU E  1 118 ? 47.338  -33.715 19.228  1.00 2.00  ? 117 LEU C CB  1 
ATOM   5308  C  CG  . LEU E  1 118 ? 47.116  -35.210 19.360  1.00 3.70  ? 117 LEU C CG  1 
ATOM   5309  C  CD1 . LEU E  1 118 ? 46.491  -35.795 18.102  1.00 2.11  ? 117 LEU C CD1 1 
ATOM   5310  C  CD2 . LEU E  1 118 ? 48.441  -35.856 19.584  1.00 2.00  ? 117 LEU C CD2 1 
ATOM   5311  N  N   . VAL E  1 119 ? 44.154  -33.418 20.419  1.00 3.70  ? 118 VAL C N   1 
ATOM   5312  C  CA  . VAL E  1 119 ? 43.275  -33.372 21.560  1.00 3.75  ? 118 VAL C CA  1 
ATOM   5313  C  C   . VAL E  1 119 ? 42.987  -34.820 21.905  1.00 5.71  ? 118 VAL C C   1 
ATOM   5314  O  O   . VAL E  1 119 ? 42.794  -35.638 20.976  1.00 7.65  ? 118 VAL C O   1 
ATOM   5315  C  CB  . VAL E  1 119 ? 41.942  -32.643 21.220  1.00 2.08  ? 118 VAL C CB  1 
ATOM   5316  C  CG1 . VAL E  1 119 ? 41.013  -32.766 22.388  1.00 2.98  ? 118 VAL C CG1 1 
ATOM   5317  C  CG2 . VAL E  1 119 ? 42.086  -31.150 21.134  1.00 2.00  ? 118 VAL C CG2 1 
ATOM   5318  N  N   . VAL E  1 120 ? 43.013  -35.167 23.206  1.00 3.80  ? 119 VAL C N   1 
ATOM   5319  C  CA  . VAL E  1 120 ? 42.591  -36.493 23.579  1.00 3.91  ? 119 VAL C CA  1 
ATOM   5320  C  C   . VAL E  1 120 ? 41.330  -36.198 24.391  1.00 5.03  ? 119 VAL C C   1 
ATOM   5321  O  O   . VAL E  1 120 ? 41.303  -35.261 25.229  1.00 5.07  ? 119 VAL C O   1 
ATOM   5322  C  CB  . VAL E  1 120 ? 43.734  -37.215 24.348  1.00 3.54  ? 119 VAL C CB  1 
ATOM   5323  C  CG1 . VAL E  1 120 ? 44.090  -36.637 25.672  1.00 2.00  ? 119 VAL C CG1 1 
ATOM   5324  C  CG2 . VAL E  1 120 ? 43.227  -38.621 24.564  1.00 2.00  ? 119 VAL C CG2 1 
ATOM   5325  N  N   . HIS E  1 121 ? 40.249  -36.912 24.025  1.00 2.00  ? 120 HIS C N   1 
ATOM   5326  C  CA  . HIS E  1 121 ? 38.953  -36.548 24.541  1.00 2.74  ? 120 HIS C CA  1 
ATOM   5327  C  C   . HIS E  1 121 ? 38.544  -37.313 25.764  1.00 6.21  ? 120 HIS C C   1 
ATOM   5328  O  O   . HIS E  1 121 ? 39.144  -38.334 26.101  1.00 8.29  ? 120 HIS C O   1 
ATOM   5329  C  CB  . HIS E  1 121 ? 37.863  -36.742 23.532  1.00 2.00  ? 120 HIS C CB  1 
ATOM   5330  C  CG  . HIS E  1 121 ? 37.778  -35.566 22.622  1.00 2.03  ? 120 HIS C CG  1 
ATOM   5331  N  ND1 . HIS E  1 121 ? 37.131  -34.447 22.779  1.00 2.88  ? 120 HIS C ND1 1 
ATOM   5332  C  CD2 . HIS E  1 121 ? 38.412  -35.498 21.413  1.00 5.53  ? 120 HIS C CD2 1 
ATOM   5333  C  CE1 . HIS E  1 121 ? 37.340  -33.716 21.707  1.00 3.30  ? 120 HIS C CE1 1 
ATOM   5334  N  NE2 . HIS E  1 121 ? 38.115  -34.355 20.869  1.00 6.07  ? 120 HIS C NE2 1 
ATOM   5335  N  N   . GLU E  1 122 ? 37.464  -36.878 26.401  1.00 4.88  ? 121 GLU C N   1 
ATOM   5336  C  CA  . GLU E  1 122 ? 37.002  -37.506 27.608  1.00 6.90  ? 121 GLU C CA  1 
ATOM   5337  C  C   . GLU E  1 122 ? 36.406  -38.915 27.541  1.00 4.58  ? 121 GLU C C   1 
ATOM   5338  O  O   . GLU E  1 122 ? 36.649  -39.694 28.452  1.00 3.58  ? 121 GLU C O   1 
ATOM   5339  C  CB  . GLU E  1 122 ? 36.040  -36.566 28.147  1.00 11.65 ? 121 GLU C CB  1 
ATOM   5340  C  CG  . GLU E  1 122 ? 35.879  -36.741 29.639  1.00 17.85 ? 121 GLU C CG  1 
ATOM   5341  C  CD  . GLU E  1 122 ? 34.478  -36.438 30.122  1.00 21.54 ? 121 GLU C CD  1 
ATOM   5342  O  OE1 . GLU E  1 122 ? 33.652  -35.935 29.346  1.00 23.32 ? 121 GLU C OE1 1 
ATOM   5343  O  OE2 . GLU E  1 122 ? 34.220  -36.736 31.290  1.00 25.04 ? 121 GLU C OE2 1 
ATOM   5344  N  N   . LYS E  1 123 ? 35.728  -39.176 26.416  1.00 3.75  ? 122 LYS C N   1 
ATOM   5345  C  CA  . LYS E  1 123 ? 34.884  -40.314 26.107  1.00 4.83  ? 122 LYS C CA  1 
ATOM   5346  C  C   . LYS E  1 123 ? 35.292  -40.955 24.794  1.00 4.40  ? 122 LYS C C   1 
ATOM   5347  O  O   . LYS E  1 123 ? 36.206  -40.473 24.135  1.00 7.39  ? 122 LYS C O   1 
ATOM   5348  C  CB  . LYS E  1 123 ? 33.424  -39.866 25.976  1.00 6.11  ? 122 LYS C CB  1 
ATOM   5349  C  CG  . LYS E  1 123 ? 32.727  -39.563 27.307  1.00 7.82  ? 122 LYS C CG  1 
ATOM   5350  C  CD  . LYS E  1 123 ? 31.654  -38.509 27.142  1.00 8.71  ? 122 LYS C CD  1 
ATOM   5351  C  CE  . LYS E  1 123 ? 30.576  -38.835 26.098  1.00 15.02 ? 122 LYS C CE  1 
ATOM   5352  N  NZ  . LYS E  1 123 ? 29.621  -37.729 25.960  1.00 16.86 ? 122 LYS C NZ  1 
ATOM   5353  N  N   . ALA E  1 124 ? 34.634  -42.025 24.382  1.00 2.00  ? 123 ALA C N   1 
ATOM   5354  C  CA  . ALA E  1 124 ? 34.959  -42.702 23.153  1.00 3.29  ? 123 ALA C CA  1 
ATOM   5355  C  C   . ALA E  1 124 ? 34.371  -41.959 21.973  1.00 4.98  ? 123 ALA C C   1 
ATOM   5356  O  O   . ALA E  1 124 ? 33.377  -41.232 22.107  1.00 7.73  ? 123 ALA C O   1 
ATOM   5357  C  CB  . ALA E  1 124 ? 34.405  -44.108 23.130  1.00 2.00  ? 123 ALA C CB  1 
ATOM   5358  N  N   . ASP E  1 125 ? 35.018  -42.071 20.820  1.00 3.90  ? 124 ASP C N   1 
ATOM   5359  C  CA  . ASP E  1 125 ? 34.516  -41.432 19.623  1.00 5.82  ? 124 ASP C CA  1 
ATOM   5360  C  C   . ASP E  1 125 ? 33.628  -42.539 19.036  1.00 6.14  ? 124 ASP C C   1 
ATOM   5361  O  O   . ASP E  1 125 ? 34.100  -43.651 18.828  1.00 4.51  ? 124 ASP C O   1 
ATOM   5362  C  CB  . ASP E  1 125 ? 35.742  -41.061 18.743  1.00 4.53  ? 124 ASP C CB  1 
ATOM   5363  C  CG  . ASP E  1 125 ? 35.549  -40.517 17.328  1.00 2.00  ? 124 ASP C CG  1 
ATOM   5364  O  OD1 . ASP E  1 125 ? 34.451  -40.523 16.828  1.00 2.00  ? 124 ASP C OD1 1 
ATOM   5365  O  OD2 . ASP E  1 125 ? 36.506  -40.093 16.689  1.00 2.00  ? 124 ASP C OD2 1 
ATOM   5366  N  N   . ASP E  1 126 ? 32.332  -42.305 18.815  1.00 7.02  ? 125 ASP C N   1 
ATOM   5367  C  CA  . ASP E  1 126 ? 31.457  -43.268 18.181  1.00 8.12  ? 125 ASP C CA  1 
ATOM   5368  C  C   . ASP E  1 126 ? 31.589  -43.402 16.663  1.00 8.52  ? 125 ASP C C   1 
ATOM   5369  O  O   . ASP E  1 126 ? 30.841  -44.138 16.009  1.00 11.05 ? 125 ASP C O   1 
ATOM   5370  C  CB  . ASP E  1 126 ? 30.006  -42.946 18.509  1.00 12.37 ? 125 ASP C CB  1 
ATOM   5371  C  CG  . ASP E  1 126 ? 29.374  -41.678 17.945  1.00 15.11 ? 125 ASP C CG  1 
ATOM   5372  O  OD1 . ASP E  1 126 ? 29.787  -41.188 16.895  1.00 16.45 ? 125 ASP C OD1 1 
ATOM   5373  O  OD2 . ASP E  1 126 ? 28.442  -41.194 18.587  1.00 17.22 ? 125 ASP C OD2 1 
ATOM   5374  N  N   . LEU E  1 127 ? 32.438  -42.576 16.056  1.00 6.68  ? 126 LEU C N   1 
ATOM   5375  C  CA  . LEU E  1 127 ? 32.870  -42.662 14.659  1.00 3.88  ? 126 LEU C CA  1 
ATOM   5376  C  C   . LEU E  1 127 ? 31.779  -42.401 13.648  1.00 4.72  ? 126 LEU C C   1 
ATOM   5377  O  O   . LEU E  1 127 ? 31.765  -42.947 12.546  1.00 2.14  ? 126 LEU C O   1 
ATOM   5378  C  CB  . LEU E  1 127 ? 33.498  -44.038 14.369  1.00 2.00  ? 126 LEU C CB  1 
ATOM   5379  C  CG  . LEU E  1 127 ? 34.575  -44.610 15.321  1.00 3.83  ? 126 LEU C CG  1 
ATOM   5380  C  CD1 . LEU E  1 127 ? 34.907  -46.037 14.932  1.00 2.00  ? 126 LEU C CD1 1 
ATOM   5381  C  CD2 . LEU E  1 127 ? 35.836  -43.773 15.269  1.00 2.00  ? 126 LEU C CD2 1 
ATOM   5382  N  N   . GLY E  1 128 ? 30.873  -41.496 14.024  1.00 6.40  ? 127 GLY C N   1 
ATOM   5383  C  CA  . GLY E  1 128 ? 29.838  -41.072 13.099  1.00 9.20  ? 127 GLY C CA  1 
ATOM   5384  C  C   . GLY E  1 128 ? 28.612  -41.971 13.111  1.00 10.04 ? 127 GLY C C   1 
ATOM   5385  O  O   . GLY E  1 128 ? 27.577  -41.663 12.520  1.00 8.20  ? 127 GLY C O   1 
ATOM   5386  N  N   . LYS E  1 129 ? 28.671  -43.022 13.912  1.00 11.26 ? 128 LYS C N   1 
ATOM   5387  C  CA  . LYS E  1 129 ? 27.602  -43.990 13.995  1.00 11.23 ? 128 LYS C CA  1 
ATOM   5388  C  C   . LYS E  1 129 ? 26.650  -43.824 15.179  1.00 11.16 ? 128 LYS C C   1 
ATOM   5389  O  O   . LYS E  1 129 ? 25.880  -44.745 15.445  1.00 13.04 ? 128 LYS C O   1 
ATOM   5390  C  CB  . LYS E  1 129 ? 28.202  -45.343 14.066  1.00 13.18 ? 128 LYS C CB  1 
ATOM   5391  C  CG  . LYS E  1 129 ? 29.038  -45.817 12.919  1.00 16.16 ? 128 LYS C CG  1 
ATOM   5392  C  CD  . LYS E  1 129 ? 29.498  -47.183 13.456  1.00 20.16 ? 128 LYS C CD  1 
ATOM   5393  C  CE  . LYS E  1 129 ? 29.478  -48.282 12.411  1.00 23.28 ? 128 LYS C CE  1 
ATOM   5394  N  NZ  . LYS E  1 129 ? 30.195  -47.891 11.203  1.00 28.06 ? 128 LYS C NZ  1 
ATOM   5395  N  N   . GLY E  1 130 ? 26.631  -42.717 15.915  1.00 9.62  ? 129 GLY C N   1 
ATOM   5396  C  CA  . GLY E  1 130 ? 25.748  -42.595 17.052  1.00 7.20  ? 129 GLY C CA  1 
ATOM   5397  C  C   . GLY E  1 130 ? 24.329  -42.212 16.681  1.00 7.59  ? 129 GLY C C   1 
ATOM   5398  O  O   . GLY E  1 130 ? 23.509  -42.113 17.585  1.00 9.93  ? 129 GLY C O   1 
ATOM   5399  N  N   . GLY E  1 131 ? 23.963  -41.901 15.442  1.00 5.41  ? 130 GLY C N   1 
ATOM   5400  C  CA  . GLY E  1 131 ? 22.577  -41.638 15.133  1.00 3.32  ? 130 GLY C CA  1 
ATOM   5401  C  C   . GLY E  1 131 ? 22.108  -40.253 15.508  1.00 5.42  ? 130 GLY C C   1 
ATOM   5402  O  O   . GLY E  1 131 ? 20.888  -39.987 15.555  1.00 5.97  ? 130 GLY C O   1 
ATOM   5403  N  N   . ASN E  1 132 ? 23.010  -39.303 15.714  1.00 7.40  ? 131 ASN C N   1 
ATOM   5404  C  CA  . ASN E  1 132 ? 22.560  -37.968 16.097  1.00 7.23  ? 131 ASN C CA  1 
ATOM   5405  C  C   . ASN E  1 132 ? 23.414  -36.940 15.435  1.00 9.63  ? 131 ASN C C   1 
ATOM   5406  O  O   . ASN E  1 132 ? 24.327  -37.245 14.679  1.00 11.14 ? 131 ASN C O   1 
ATOM   5407  C  CB  . ASN E  1 132 ? 22.626  -37.732 17.622  1.00 5.55  ? 131 ASN C CB  1 
ATOM   5408  C  CG  . ASN E  1 132 ? 23.948  -37.582 18.330  1.00 6.04  ? 131 ASN C CG  1 
ATOM   5409  O  OD1 . ASN E  1 132 ? 25.045  -37.511 17.742  1.00 10.19 ? 131 ASN C OD1 1 
ATOM   5410  N  ND2 . ASN E  1 132 ? 23.909  -37.502 19.646  1.00 5.58  ? 131 ASN C ND2 1 
ATOM   5411  N  N   . GLU E  1 133 ? 23.051  -35.696 15.709  1.00 14.71 ? 132 GLU C N   1 
ATOM   5412  C  CA  . GLU E  1 133 ? 23.755  -34.526 15.252  1.00 16.83 ? 132 GLU C CA  1 
ATOM   5413  C  C   . GLU E  1 133 ? 25.236  -34.554 15.623  1.00 16.41 ? 132 GLU C C   1 
ATOM   5414  O  O   . GLU E  1 133 ? 26.074  -34.728 14.744  1.00 17.14 ? 132 GLU C O   1 
ATOM   5415  C  CB  . GLU E  1 133 ? 23.098  -33.266 15.850  1.00 22.88 ? 132 GLU C CB  1 
ATOM   5416  C  CG  . GLU E  1 133 ? 22.406  -32.409 14.814  1.00 29.83 ? 132 GLU C CG  1 
ATOM   5417  C  CD  . GLU E  1 133 ? 23.398  -31.920 13.761  1.00 34.91 ? 132 GLU C CD  1 
ATOM   5418  O  OE1 . GLU E  1 133 ? 23.602  -32.610 12.732  1.00 36.20 ? 132 GLU C OE1 1 
ATOM   5419  O  OE2 . GLU E  1 133 ? 23.924  -30.820 13.990  1.00 37.67 ? 132 GLU C OE2 1 
ATOM   5420  N  N   . GLU E  1 134 ? 25.593  -34.426 16.913  1.00 13.07 ? 133 GLU C N   1 
ATOM   5421  C  CA  . GLU E  1 134 ? 26.964  -34.413 17.327  1.00 13.89 ? 133 GLU C CA  1 
ATOM   5422  C  C   . GLU E  1 134 ? 27.847  -35.522 16.777  1.00 14.04 ? 133 GLU C C   1 
ATOM   5423  O  O   . GLU E  1 134 ? 29.055  -35.327 16.591  1.00 15.71 ? 133 GLU C O   1 
ATOM   5424  C  CB  . GLU E  1 134 ? 26.973  -34.441 18.842  1.00 16.45 ? 133 GLU C CB  1 
ATOM   5425  C  CG  . GLU E  1 134 ? 27.800  -33.309 19.487  1.00 22.83 ? 133 GLU C CG  1 
ATOM   5426  C  CD  . GLU E  1 134 ? 27.490  -31.910 18.927  1.00 25.95 ? 133 GLU C CD  1 
ATOM   5427  O  OE1 . GLU E  1 134 ? 26.317  -31.520 18.802  1.00 28.31 ? 133 GLU C OE1 1 
ATOM   5428  O  OE2 . GLU E  1 134 ? 28.449  -31.203 18.616  1.00 28.97 ? 133 GLU C OE2 1 
ATOM   5429  N  N   . SER E  1 135 ? 27.298  -36.678 16.458  1.00 11.25 ? 134 SER C N   1 
ATOM   5430  C  CA  . SER E  1 135 ? 28.073  -37.761 15.953  1.00 10.44 ? 134 SER C CA  1 
ATOM   5431  C  C   . SER E  1 135 ? 28.741  -37.381 14.646  1.00 11.21 ? 134 SER C C   1 
ATOM   5432  O  O   . SER E  1 135 ? 29.814  -37.907 14.364  1.00 11.56 ? 134 SER C O   1 
ATOM   5433  C  CB  . SER E  1 135 ? 27.160  -38.935 15.785  1.00 10.46 ? 134 SER C CB  1 
ATOM   5434  O  OG  . SER E  1 135 ? 27.859  -40.133 15.452  1.00 9.83  ? 134 SER C OG  1 
ATOM   5435  N  N   . THR E  1 136 ? 28.227  -36.477 13.829  1.00 11.62 ? 135 THR C N   1 
ATOM   5436  C  CA  . THR E  1 136 ? 28.844  -36.178 12.542  1.00 12.94 ? 135 THR C CA  1 
ATOM   5437  C  C   . THR E  1 136 ? 29.757  -34.954 12.611  1.00 12.84 ? 135 THR C C   1 
ATOM   5438  O  O   . THR E  1 136 ? 30.411  -34.468 11.656  1.00 12.97 ? 135 THR C O   1 
ATOM   5439  C  CB  . THR E  1 136 ? 27.670  -36.003 11.503  1.00 16.86 ? 135 THR C CB  1 
ATOM   5440  O  OG1 . THR E  1 136 ? 26.849  -34.866 11.870  1.00 19.07 ? 135 THR C OG1 1 
ATOM   5441  C  CG2 . THR E  1 136 ? 26.828  -37.297 11.438  1.00 15.63 ? 135 THR C CG2 1 
ATOM   5442  N  N   . LYS E  1 137 ? 29.776  -34.450 13.832  1.00 12.47 ? 136 LYS C N   1 
ATOM   5443  C  CA  . LYS E  1 137 ? 30.585  -33.311 14.103  1.00 11.92 ? 136 LYS C CA  1 
ATOM   5444  C  C   . LYS E  1 137 ? 31.797  -33.766 14.860  1.00 10.02 ? 136 LYS C C   1 
ATOM   5445  O  O   . LYS E  1 137 ? 32.905  -33.699 14.326  1.00 13.07 ? 136 LYS C O   1 
ATOM   5446  C  CB  . LYS E  1 137 ? 29.766  -32.298 14.883  1.00 14.39 ? 136 LYS C CB  1 
ATOM   5447  C  CG  . LYS E  1 137 ? 28.879  -31.599 13.862  1.00 20.99 ? 136 LYS C CG  1 
ATOM   5448  C  CD  . LYS E  1 137 ? 27.984  -30.499 14.436  1.00 29.15 ? 136 LYS C CD  1 
ATOM   5449  C  CE  . LYS E  1 137 ? 26.853  -31.177 15.219  1.00 34.34 ? 136 LYS C CE  1 
ATOM   5450  N  NZ  . LYS E  1 137 ? 26.058  -30.224 15.988  1.00 39.74 ? 136 LYS C NZ  1 
ATOM   5451  N  N   . THR E  1 138 ? 31.572  -34.335 16.031  1.00 5.02  ? 137 THR C N   1 
ATOM   5452  C  CA  . THR E  1 138 ? 32.607  -34.643 16.960  1.00 3.41  ? 137 THR C CA  1 
ATOM   5453  C  C   . THR E  1 138 ? 32.646  -36.090 17.301  1.00 5.93  ? 137 THR C C   1 
ATOM   5454  O  O   . THR E  1 138 ? 33.454  -36.575 18.108  1.00 10.56 ? 137 THR C O   1 
ATOM   5455  C  CB  . THR E  1 138 ? 32.317  -33.850 18.151  1.00 5.31  ? 137 THR C CB  1 
ATOM   5456  O  OG1 . THR E  1 138 ? 31.026  -34.267 18.584  1.00 5.40  ? 137 THR C OG1 1 
ATOM   5457  C  CG2 . THR E  1 138 ? 32.141  -32.366 17.867  1.00 10.70 ? 137 THR C CG2 1 
ATOM   5458  N  N   . GLY E  1 139 ? 31.697  -36.859 16.814  1.00 4.63  ? 138 GLY C N   1 
ATOM   5459  C  CA  . GLY E  1 139 ? 31.707  -38.251 17.194  1.00 4.57  ? 138 GLY C CA  1 
ATOM   5460  C  C   . GLY E  1 139 ? 31.295  -38.465 18.635  1.00 4.53  ? 138 GLY C C   1 
ATOM   5461  O  O   . GLY E  1 139 ? 31.332  -39.626 19.037  1.00 5.16  ? 138 GLY C O   1 
ATOM   5462  N  N   . ASN E  1 140 ? 30.853  -37.404 19.360  1.00 4.57  ? 139 ASN C N   1 
ATOM   5463  C  CA  . ASN E  1 140 ? 30.354  -37.419 20.735  1.00 4.33  ? 139 ASN C CA  1 
ATOM   5464  C  C   . ASN E  1 140 ? 31.415  -37.799 21.749  1.00 5.12  ? 139 ASN C C   1 
ATOM   5465  O  O   . ASN E  1 140 ? 31.126  -38.086 22.901  1.00 6.85  ? 139 ASN C O   1 
ATOM   5466  C  CB  . ASN E  1 140 ? 29.181  -38.383 20.946  1.00 5.60  ? 139 ASN C CB  1 
ATOM   5467  C  CG  . ASN E  1 140 ? 27.879  -37.947 20.307  1.00 6.07  ? 139 ASN C CG  1 
ATOM   5468  O  OD1 . ASN E  1 140 ? 27.130  -37.242 20.944  1.00 10.01 ? 139 ASN C OD1 1 
ATOM   5469  N  ND2 . ASN E  1 140 ? 27.437  -38.303 19.100  1.00 5.73  ? 139 ASN C ND2 1 
ATOM   5470  N  N   . ALA E  1 141 ? 32.664  -37.625 21.337  1.00 4.00  ? 140 ALA C N   1 
ATOM   5471  C  CA  . ALA E  1 141 ? 33.875  -37.839 22.099  1.00 2.97  ? 140 ALA C CA  1 
ATOM   5472  C  C   . ALA E  1 141 ? 33.950  -37.046 23.405  1.00 2.00  ? 140 ALA C C   1 
ATOM   5473  O  O   . ALA E  1 141 ? 34.721  -37.353 24.323  1.00 2.00  ? 140 ALA C O   1 
ATOM   5474  C  CB  . ALA E  1 141 ? 35.035  -37.476 21.166  1.00 2.00  ? 140 ALA C CB  1 
ATOM   5475  N  N   . GLY E  1 142 ? 33.213  -35.954 23.476  1.00 2.00  ? 141 GLY C N   1 
ATOM   5476  C  CA  . GLY E  1 142 ? 33.121  -35.209 24.706  1.00 3.71  ? 141 GLY C CA  1 
ATOM   5477  C  C   . GLY E  1 142 ? 34.212  -34.205 24.969  1.00 3.74  ? 141 GLY C C   1 
ATOM   5478  O  O   . GLY E  1 142 ? 34.872  -33.711 24.072  1.00 6.46  ? 141 GLY C O   1 
ATOM   5479  N  N   . SER E  1 143 ? 34.447  -33.951 26.234  1.00 4.71  ? 142 SER C N   1 
ATOM   5480  C  CA  . SER E  1 143 ? 35.373  -32.948 26.694  1.00 8.04  ? 142 SER C CA  1 
ATOM   5481  C  C   . SER E  1 143 ? 36.770  -33.130 26.168  1.00 7.75  ? 142 SER C C   1 
ATOM   5482  O  O   . SER E  1 143 ? 37.156  -34.243 25.829  1.00 7.48  ? 142 SER C O   1 
ATOM   5483  C  CB  . SER E  1 143 ? 35.425  -32.971 28.200  1.00 10.10 ? 142 SER C CB  1 
ATOM   5484  O  OG  . SER E  1 143 ? 34.158  -33.348 28.707  1.00 15.82 ? 142 SER C OG  1 
ATOM   5485  N  N   . ARG E  1 144 ? 37.520  -32.033 26.095  1.00 8.68  ? 143 ARG C N   1 
ATOM   5486  C  CA  . ARG E  1 144 ? 38.902  -32.095 25.624  1.00 9.87  ? 143 ARG C CA  1 
ATOM   5487  C  C   . ARG E  1 144 ? 39.784  -32.213 26.862  1.00 9.67  ? 143 ARG C C   1 
ATOM   5488  O  O   . ARG E  1 144 ? 40.008  -31.189 27.515  1.00 10.79 ? 143 ARG C O   1 
ATOM   5489  C  CB  . ARG E  1 144 ? 39.201  -30.810 24.806  1.00 6.82  ? 143 ARG C CB  1 
ATOM   5490  C  CG  . ARG E  1 144 ? 38.265  -30.635 23.625  1.00 3.20  ? 143 ARG C CG  1 
ATOM   5491  C  CD  . ARG E  1 144 ? 38.425  -29.283 22.984  1.00 4.57  ? 143 ARG C CD  1 
ATOM   5492  N  NE  . ARG E  1 144 ? 37.438  -29.217 21.918  1.00 6.05  ? 143 ARG C NE  1 
ATOM   5493  C  CZ  . ARG E  1 144 ? 37.463  -28.321 20.925  1.00 2.89  ? 143 ARG C CZ  1 
ATOM   5494  N  NH1 . ARG E  1 144 ? 38.401  -27.403 20.820  1.00 9.83  ? 143 ARG C NH1 1 
ATOM   5495  N  NH2 . ARG E  1 144 ? 36.525  -28.341 20.008  1.00 2.00  ? 143 ARG C NH2 1 
ATOM   5496  N  N   . LEU E  1 145 ? 40.279  -33.412 27.210  1.00 9.39  ? 144 LEU C N   1 
ATOM   5497  C  CA  . LEU E  1 145 ? 41.047  -33.585 28.450  1.00 8.64  ? 144 LEU C CA  1 
ATOM   5498  C  C   . LEU E  1 145 ? 42.419  -32.998 28.455  1.00 7.00  ? 144 LEU C C   1 
ATOM   5499  O  O   . LEU E  1 145 ? 42.843  -32.393 29.434  1.00 10.05 ? 144 LEU C O   1 
ATOM   5500  C  CB  . LEU E  1 145 ? 41.256  -35.042 28.834  1.00 7.70  ? 144 LEU C CB  1 
ATOM   5501  C  CG  . LEU E  1 145 ? 40.023  -35.810 29.189  1.00 7.73  ? 144 LEU C CG  1 
ATOM   5502  C  CD1 . LEU E  1 145 ? 40.451  -37.137 29.753  1.00 7.05  ? 144 LEU C CD1 1 
ATOM   5503  C  CD2 . LEU E  1 145 ? 39.180  -35.010 30.175  1.00 5.56  ? 144 LEU C CD2 1 
ATOM   5504  N  N   . ALA E  1 146 ? 43.171  -33.270 27.407  1.00 7.05  ? 145 ALA C N   1 
ATOM   5505  C  CA  . ALA E  1 146 ? 44.479  -32.659 27.293  1.00 4.98  ? 145 ALA C CA  1 
ATOM   5506  C  C   . ALA E  1 146 ? 44.615  -32.360 25.805  1.00 3.85  ? 145 ALA C C   1 
ATOM   5507  O  O   . ALA E  1 146 ? 43.875  -32.937 24.995  1.00 2.00  ? 145 ALA C O   1 
ATOM   5508  C  CB  . ALA E  1 146 ? 45.548  -33.642 27.766  1.00 5.19  ? 145 ALA C CB  1 
ATOM   5509  N  N   . CYS E  1 147 ? 45.492  -31.427 25.456  1.00 2.93  ? 146 CYS C N   1 
ATOM   5510  C  CA  . CYS E  1 147 ? 45.762  -31.055 24.082  1.00 3.23  ? 146 CYS C CA  1 
ATOM   5511  C  C   . CYS E  1 147 ? 47.155  -30.478 23.919  1.00 3.91  ? 146 CYS C C   1 
ATOM   5512  O  O   . CYS E  1 147 ? 47.904  -30.379 24.895  1.00 4.84  ? 146 CYS C O   1 
ATOM   5513  C  CB  . CYS E  1 147 ? 44.766  -30.041 23.592  1.00 3.72  ? 146 CYS C CB  1 
ATOM   5514  S  SG  . CYS E  1 147 ? 44.668  -28.583 24.648  1.00 9.16  ? 146 CYS C SG  1 
ATOM   5515  N  N   . GLY E  1 148 ? 47.617  -30.168 22.705  1.00 4.95  ? 147 GLY C N   1 
ATOM   5516  C  CA  . GLY E  1 148 ? 48.949  -29.615 22.505  1.00 4.50  ? 147 GLY C CA  1 
ATOM   5517  C  C   . GLY E  1 148 ? 49.154  -29.255 21.062  1.00 2.00  ? 147 GLY C C   1 
ATOM   5518  O  O   . GLY E  1 148 ? 48.647  -29.969 20.217  1.00 6.38  ? 147 GLY C O   1 
ATOM   5519  N  N   . VAL E  1 149 ? 49.871  -28.196 20.723  1.00 3.11  ? 148 VAL C N   1 
ATOM   5520  C  CA  . VAL E  1 149 ? 50.060  -27.766 19.338  1.00 2.49  ? 148 VAL C CA  1 
ATOM   5521  C  C   . VAL E  1 149 ? 51.079  -28.694 18.720  1.00 2.00  ? 148 VAL C C   1 
ATOM   5522  O  O   . VAL E  1 149 ? 52.017  -29.030 19.436  1.00 2.00  ? 148 VAL C O   1 
ATOM   5523  C  CB  . VAL E  1 149 ? 50.529  -26.309 19.384  1.00 2.00  ? 148 VAL C CB  1 
ATOM   5524  C  CG1 . VAL E  1 149 ? 50.963  -25.803 18.060  1.00 2.00  ? 148 VAL C CG1 1 
ATOM   5525  C  CG2 . VAL E  1 149 ? 49.367  -25.470 19.702  1.00 2.00  ? 148 VAL C CG2 1 
ATOM   5526  N  N   . ILE E  1 150 ? 50.999  -29.097 17.483  1.00 2.00  ? 149 ILE C N   1 
ATOM   5527  C  CA  . ILE E  1 150 ? 51.927  -30.065 16.920  1.00 2.00  ? 149 ILE C CA  1 
ATOM   5528  C  C   . ILE E  1 150 ? 53.088  -29.273 16.432  1.00 2.00  ? 149 ILE C C   1 
ATOM   5529  O  O   . ILE E  1 150 ? 52.834  -28.432 15.582  1.00 2.00  ? 149 ILE C O   1 
ATOM   5530  C  CB  . ILE E  1 150 ? 51.285  -30.836 15.729  1.00 2.19  ? 149 ILE C CB  1 
ATOM   5531  C  CG1 . ILE E  1 150 ? 50.136  -31.638 16.309  1.00 2.00  ? 149 ILE C CG1 1 
ATOM   5532  C  CG2 . ILE E  1 150 ? 52.289  -31.725 14.979  1.00 2.00  ? 149 ILE C CG2 1 
ATOM   5533  C  CD1 . ILE E  1 150 ? 48.972  -31.777 15.350  1.00 2.00  ? 149 ILE C CD1 1 
ATOM   5534  N  N   . GLY E  1 151 ? 54.331  -29.463 16.828  1.00 2.00  ? 150 GLY C N   1 
ATOM   5535  C  CA  . GLY E  1 151 ? 55.404  -28.636 16.284  1.00 3.98  ? 150 GLY C CA  1 
ATOM   5536  C  C   . GLY E  1 151 ? 56.435  -29.429 15.515  1.00 2.00  ? 150 GLY C C   1 
ATOM   5537  O  O   . GLY E  1 151 ? 56.333  -30.628 15.587  1.00 3.39  ? 150 GLY C O   1 
ATOM   5538  N  N   . ILE E  1 152 ? 57.398  -28.885 14.785  1.00 2.00  ? 151 ILE C N   1 
ATOM   5539  C  CA  . ILE E  1 152 ? 58.424  -29.592 14.048  1.00 2.00  ? 151 ILE C CA  1 
ATOM   5540  C  C   . ILE E  1 152 ? 59.388  -30.059 15.108  1.00 2.00  ? 151 ILE C C   1 
ATOM   5541  O  O   . ILE E  1 152 ? 59.688  -29.342 16.072  1.00 2.00  ? 151 ILE C O   1 
ATOM   5542  C  CB  . ILE E  1 152 ? 59.144  -28.650 13.096  1.00 2.00  ? 151 ILE C CB  1 
ATOM   5543  C  CG1 . ILE E  1 152 ? 58.267  -28.379 11.939  1.00 3.38  ? 151 ILE C CG1 1 
ATOM   5544  C  CG2 . ILE E  1 152 ? 60.421  -29.213 12.556  1.00 2.00  ? 151 ILE C CG2 1 
ATOM   5545  C  CD1 . ILE E  1 152 ? 58.409  -26.879 11.599  1.00 2.00  ? 151 ILE C CD1 1 
ATOM   5546  N  N   . ALA E  1 153 ? 59.860  -31.279 14.897  1.00 2.00  ? 152 ALA C N   1 
ATOM   5547  C  CA  . ALA E  1 153 ? 60.755  -31.971 15.783  1.00 2.20  ? 152 ALA C CA  1 
ATOM   5548  C  C   . ALA E  1 153 ? 61.962  -32.253 14.944  1.00 5.14  ? 152 ALA C C   1 
ATOM   5549  O  O   . ALA E  1 153 ? 61.872  -32.261 13.716  1.00 5.99  ? 152 ALA C O   1 
ATOM   5550  C  CB  . ALA E  1 153 ? 60.169  -33.289 16.211  1.00 2.00  ? 152 ALA C CB  1 
ATOM   5551  N  N   . GLN E  1 154 ? 63.086  -32.404 15.592  1.00 9.56  ? 153 GLN C N   1 
ATOM   5552  C  CA  . GLN E  1 154 ? 64.333  -32.758 14.944  1.00 15.72 ? 153 GLN C CA  1 
ATOM   5553  C  C   . GLN E  1 154 ? 64.323  -34.273 14.803  1.00 19.29 ? 153 GLN C C   1 
ATOM   5554  O  O   . GLN E  1 154 ? 64.643  -34.742 13.704  1.00 22.84 ? 153 GLN C O   1 
ATOM   5555  C  CB  . GLN E  1 154 ? 65.489  -32.343 15.827  1.00 18.05 ? 153 GLN C CB  1 
ATOM   5556  C  CG  . GLN E  1 154 ? 66.892  -32.461 15.261  1.00 22.50 ? 153 GLN C CG  1 
ATOM   5557  C  CD  . GLN E  1 154 ? 67.950  -32.372 16.362  1.00 26.40 ? 153 GLN C CD  1 
ATOM   5558  O  OE1 . GLN E  1 154 ? 68.982  -31.701 16.257  1.00 29.89 ? 153 GLN C OE1 1 
ATOM   5559  N  NE2 . GLN E  1 154 ? 67.779  -33.096 17.461  1.00 26.54 ? 153 GLN C NE2 1 
ATOM   5560  O  OXT . GLN E  1 154 ? 63.992  -34.947 15.803  1.00 22.44 ? 153 GLN C OXT 1 
HETATM 5561  C  C   . ACE F  1 1   ? 49.415  -21.362 6.956   1.00 35.03 ? 0   ACE H C   1 
HETATM 5562  O  O   . ACE F  1 1   ? 48.358  -22.024 7.022   1.00 36.12 ? 0   ACE H O   1 
HETATM 5563  C  CH3 . ACE F  1 1   ? 50.736  -22.061 6.647   1.00 35.73 ? 0   ACE H CH3 1 
ATOM   5564  N  N   . ALA F  1 2   ? 49.430  -20.026 7.088   1.00 31.79 ? 1   ALA H N   1 
ATOM   5565  C  CA  . ALA F  1 2   ? 48.238  -19.320 7.516   1.00 26.83 ? 1   ALA H CA  1 
ATOM   5566  C  C   . ALA F  1 2   ? 48.263  -17.853 7.141   1.00 23.07 ? 1   ALA H C   1 
ATOM   5567  O  O   . ALA F  1 2   ? 49.091  -17.415 6.362   1.00 23.62 ? 1   ALA H O   1 
ATOM   5568  C  CB  . ALA F  1 2   ? 48.133  -19.438 9.017   1.00 26.29 ? 1   ALA H CB  1 
ATOM   5569  N  N   . THR F  1 3   ? 47.260  -17.124 7.604   1.00 19.39 ? 2   THR H N   1 
ATOM   5570  C  CA  . THR F  1 3   ? 47.208  -15.686 7.515   1.00 15.26 ? 2   THR H CA  1 
ATOM   5571  C  C   . THR F  1 3   ? 47.359  -15.213 8.939   1.00 11.78 ? 2   THR H C   1 
ATOM   5572  O  O   . THR F  1 3   ? 47.655  -14.042 9.138   1.00 13.96 ? 2   THR H O   1 
ATOM   5573  C  CB  . THR F  1 3   ? 45.850  -15.290 6.913   1.00 17.18 ? 2   THR H CB  1 
ATOM   5574  O  OG1 . THR F  1 3   ? 46.050  -15.812 5.604   1.00 20.50 ? 2   THR H OG1 1 
ATOM   5575  C  CG2 . THR F  1 3   ? 45.403  -13.809 6.891   1.00 15.64 ? 2   THR H CG2 1 
ATOM   5576  N  N   . LYS F  1 4   ? 47.161  -16.060 9.946   1.00 6.90  ? 3   LYS H N   1 
ATOM   5577  C  CA  . LYS F  1 4   ? 47.274  -15.676 11.317  1.00 3.25  ? 3   LYS H CA  1 
ATOM   5578  C  C   . LYS F  1 4   ? 47.826  -16.823 12.107  1.00 2.33  ? 3   LYS H C   1 
ATOM   5579  O  O   . LYS F  1 4   ? 47.611  -17.986 11.788  1.00 2.00  ? 3   LYS H O   1 
ATOM   5580  C  CB  . LYS F  1 4   ? 45.927  -15.307 11.867  1.00 6.80  ? 3   LYS H CB  1 
ATOM   5581  C  CG  . LYS F  1 4   ? 45.437  -13.962 11.370  1.00 13.63 ? 3   LYS H CG  1 
ATOM   5582  C  CD  . LYS F  1 4   ? 44.086  -13.678 11.975  1.00 20.82 ? 3   LYS H CD  1 
ATOM   5583  C  CE  . LYS F  1 4   ? 43.356  -12.630 11.127  1.00 26.41 ? 3   LYS H CE  1 
ATOM   5584  N  NZ  . LYS F  1 4   ? 43.148  -13.068 9.745   1.00 30.43 ? 3   LYS H NZ  1 
ATOM   5585  N  N   . ALA F  1 5   ? 48.613  -16.496 13.107  1.00 2.99  ? 4   ALA H N   1 
ATOM   5586  C  CA  . ALA F  1 5   ? 49.183  -17.476 14.005  1.00 2.00  ? 4   ALA H CA  1 
ATOM   5587  C  C   . ALA F  1 5   ? 49.258  -16.833 15.382  1.00 2.00  ? 4   ALA H C   1 
ATOM   5588  O  O   . ALA F  1 5   ? 49.131  -15.596 15.582  1.00 2.00  ? 4   ALA H O   1 
ATOM   5589  C  CB  . ALA F  1 5   ? 50.560  -17.863 13.546  1.00 2.00  ? 4   ALA H CB  1 
ATOM   5590  N  N   . VAL F  1 6   ? 49.412  -17.691 16.370  1.00 2.00  ? 5   VAL H N   1 
ATOM   5591  C  CA  . VAL F  1 6   ? 49.530  -17.205 17.730  1.00 3.17  ? 5   VAL H CA  1 
ATOM   5592  C  C   . VAL F  1 6   ? 50.612  -17.984 18.424  1.00 2.00  ? 5   VAL H C   1 
ATOM   5593  O  O   . VAL F  1 6   ? 50.916  -19.072 17.949  1.00 2.74  ? 5   VAL H O   1 
ATOM   5594  C  CB  . VAL F  1 6   ? 48.113  -17.360 18.395  1.00 4.86  ? 5   VAL H CB  1 
ATOM   5595  C  CG1 . VAL F  1 6   ? 47.769  -18.804 18.637  1.00 6.93  ? 5   VAL H CG1 1 
ATOM   5596  C  CG2 . VAL F  1 6   ? 48.069  -16.592 19.675  1.00 4.18  ? 5   VAL H CG2 1 
ATOM   5597  N  N   . ALA F  1 7   ? 51.214  -17.480 19.488  1.00 2.00  ? 6   ALA H N   1 
ATOM   5598  C  CA  . ALA F  1 7   ? 52.116  -18.239 20.334  1.00 2.00  ? 6   ALA H CA  1 
ATOM   5599  C  C   . ALA F  1 7   ? 51.803  -17.908 21.799  1.00 2.00  ? 6   ALA H C   1 
ATOM   5600  O  O   . ALA F  1 7   ? 51.642  -16.743 22.168  1.00 2.00  ? 6   ALA H O   1 
ATOM   5601  C  CB  . ALA F  1 7   ? 53.561  -17.864 20.046  1.00 2.00  ? 6   ALA H CB  1 
ATOM   5602  N  N   . VAL F  1 8   ? 51.604  -18.913 22.640  1.00 2.11  ? 7   VAL H N   1 
ATOM   5603  C  CA  . VAL F  1 8   ? 51.332  -18.668 24.053  1.00 4.25  ? 7   VAL H CA  1 
ATOM   5604  C  C   . VAL F  1 8   ? 52.623  -18.957 24.812  1.00 5.21  ? 7   VAL H C   1 
ATOM   5605  O  O   . VAL F  1 8   ? 53.047  -20.114 24.856  1.00 6.78  ? 7   VAL H O   1 
ATOM   5606  C  CB  . VAL F  1 8   ? 50.202  -19.585 24.559  1.00 2.61  ? 7   VAL H CB  1 
ATOM   5607  C  CG1 . VAL F  1 8   ? 49.919  -19.363 26.038  1.00 2.64  ? 7   VAL H CG1 1 
ATOM   5608  C  CG2 . VAL F  1 8   ? 48.941  -19.224 23.824  1.00 2.00  ? 7   VAL H CG2 1 
ATOM   5609  N  N   . LEU F  1 9   ? 53.274  -17.920 25.351  1.00 3.70  ? 8   LEU H N   1 
ATOM   5610  C  CA  . LEU F  1 9   ? 54.564  -18.082 25.982  1.00 2.66  ? 8   LEU H CA  1 
ATOM   5611  C  C   . LEU F  1 9   ? 54.467  -18.526 27.416  1.00 2.87  ? 8   LEU H C   1 
ATOM   5612  O  O   . LEU F  1 9   ? 53.795  -17.850 28.188  1.00 4.81  ? 8   LEU H O   1 
ATOM   5613  C  CB  . LEU F  1 9   ? 55.307  -16.795 25.934  1.00 2.00  ? 8   LEU H CB  1 
ATOM   5614  C  CG  . LEU F  1 9   ? 56.198  -16.466 24.765  1.00 2.00  ? 8   LEU H CG  1 
ATOM   5615  C  CD1 . LEU F  1 9   ? 55.454  -16.345 23.482  1.00 2.00  ? 8   LEU H CD1 1 
ATOM   5616  C  CD2 . LEU F  1 9   ? 56.830  -15.150 25.083  1.00 2.00  ? 8   LEU H CD2 1 
ATOM   5617  N  N   . LYS F  1 10  ? 55.076  -19.606 27.840  1.00 3.66  ? 9   LYS H N   1 
ATOM   5618  C  CA  . LYS F  1 10  ? 55.006  -20.012 29.233  1.00 7.93  ? 9   LYS H CA  1 
ATOM   5619  C  C   . LYS F  1 10  ? 56.383  -20.472 29.616  1.00 7.87  ? 9   LYS H C   1 
ATOM   5620  O  O   . LYS F  1 10  ? 57.214  -20.744 28.752  1.00 8.48  ? 9   LYS H O   1 
ATOM   5621  C  CB  . LYS F  1 10  ? 54.073  -21.173 29.476  1.00 9.41  ? 9   LYS H CB  1 
ATOM   5622  C  CG  . LYS F  1 10  ? 52.896  -20.830 30.363  1.00 17.40 ? 9   LYS H CG  1 
ATOM   5623  C  CD  . LYS F  1 10  ? 51.759  -20.025 29.711  1.00 21.87 ? 9   LYS H CD  1 
ATOM   5624  C  CE  . LYS F  1 10  ? 50.663  -19.864 30.777  1.00 26.22 ? 9   LYS H CE  1 
ATOM   5625  N  NZ  . LYS F  1 10  ? 49.445  -19.283 30.246  1.00 29.39 ? 9   LYS H NZ  1 
ATOM   5626  N  N   . GLY F  1 11  ? 56.678  -20.533 30.891  1.00 8.96  ? 10  GLY H N   1 
ATOM   5627  C  CA  . GLY F  1 11  ? 58.002  -20.946 31.291  1.00 10.56 ? 10  GLY H CA  1 
ATOM   5628  C  C   . GLY F  1 11  ? 57.885  -21.403 32.724  1.00 13.38 ? 10  GLY H C   1 
ATOM   5629  O  O   . GLY F  1 11  ? 56.781  -21.517 33.278  1.00 15.95 ? 10  GLY H O   1 
ATOM   5630  N  N   . ASP F  1 12  ? 59.023  -21.646 33.348  1.00 14.25 ? 11  ASP H N   1 
ATOM   5631  C  CA  . ASP F  1 12  ? 58.979  -22.069 34.720  1.00 17.09 ? 11  ASP H CA  1 
ATOM   5632  C  C   . ASP F  1 12  ? 58.949  -20.910 35.730  1.00 17.15 ? 11  ASP H C   1 
ATOM   5633  O  O   . ASP F  1 12  ? 58.797  -21.124 36.943  1.00 21.52 ? 11  ASP H O   1 
ATOM   5634  C  CB  . ASP F  1 12  ? 60.157  -23.027 34.938  1.00 18.50 ? 11  ASP H CB  1 
ATOM   5635  C  CG  . ASP F  1 12  ? 60.008  -24.399 34.224  1.00 26.21 ? 11  ASP H CG  1 
ATOM   5636  O  OD1 . ASP F  1 12  ? 58.889  -24.837 33.873  1.00 25.95 ? 11  ASP H OD1 1 
ATOM   5637  O  OD2 . ASP F  1 12  ? 61.050  -25.042 34.008  1.00 29.90 ? 11  ASP H OD2 1 
ATOM   5638  N  N   . GLY F  1 13  ? 59.012  -19.658 35.291  1.00 12.84 ? 12  GLY H N   1 
ATOM   5639  C  CA  . GLY F  1 13  ? 58.963  -18.567 36.226  1.00 5.73  ? 12  GLY H CA  1 
ATOM   5640  C  C   . GLY F  1 13  ? 57.744  -17.757 35.895  1.00 4.02  ? 12  GLY H C   1 
ATOM   5641  O  O   . GLY F  1 13  ? 56.811  -18.270 35.296  1.00 3.62  ? 12  GLY H O   1 
ATOM   5642  N  N   . PRO F  1 14  ? 57.689  -16.463 36.228  1.00 4.66  ? 13  PRO H N   1 
ATOM   5643  C  CA  . PRO F  1 14  ? 56.512  -15.635 36.068  1.00 2.50  ? 13  PRO H CA  1 
ATOM   5644  C  C   . PRO F  1 14  ? 56.286  -15.094 34.689  1.00 2.00  ? 13  PRO H C   1 
ATOM   5645  O  O   . PRO F  1 14  ? 55.326  -14.345 34.529  1.00 2.10  ? 13  PRO H O   1 
ATOM   5646  C  CB  . PRO F  1 14  ? 56.728  -14.584 37.102  1.00 2.00  ? 13  PRO H CB  1 
ATOM   5647  C  CG  . PRO F  1 14  ? 58.173  -14.328 36.901  1.00 2.00  ? 13  PRO H CG  1 
ATOM   5648  C  CD  . PRO F  1 14  ? 58.681  -15.736 37.009  1.00 2.00  ? 13  PRO H CD  1 
ATOM   5649  N  N   . VAL F  1 15  ? 57.086  -15.434 33.680  1.00 3.03  ? 14  VAL H N   1 
ATOM   5650  C  CA  . VAL F  1 15  ? 56.906  -14.781 32.382  1.00 5.52  ? 14  VAL H CA  1 
ATOM   5651  C  C   . VAL F  1 15  ? 56.155  -15.767 31.529  1.00 6.30  ? 14  VAL H C   1 
ATOM   5652  O  O   . VAL F  1 15  ? 56.358  -16.991 31.466  1.00 7.31  ? 14  VAL H O   1 
ATOM   5653  C  CB  . VAL F  1 15  ? 58.296  -14.302 31.705  1.00 3.27  ? 14  VAL H CB  1 
ATOM   5654  C  CG1 . VAL F  1 15  ? 59.401  -15.206 32.086  1.00 6.06  ? 14  VAL H CG1 1 
ATOM   5655  C  CG2 . VAL F  1 15  ? 58.226  -14.284 30.174  1.00 2.00  ? 14  VAL H CG2 1 
ATOM   5656  N  N   . GLN F  1 16  ? 55.129  -15.081 31.059  1.00 6.11  ? 15  GLN H N   1 
ATOM   5657  C  CA  . GLN F  1 16  ? 54.064  -15.668 30.278  1.00 6.47  ? 15  GLN H CA  1 
ATOM   5658  C  C   . GLN F  1 16  ? 53.554  -14.571 29.368  1.00 2.48  ? 15  GLN H C   1 
ATOM   5659  O  O   . GLN F  1 16  ? 53.669  -13.414 29.720  1.00 2.00  ? 15  GLN H O   1 
ATOM   5660  C  CB  . GLN F  1 16  ? 52.950  -16.161 31.214  1.00 10.69 ? 15  GLN H CB  1 
ATOM   5661  C  CG  . GLN F  1 16  ? 52.595  -15.050 32.182  1.00 18.05 ? 15  GLN H CG  1 
ATOM   5662  C  CD  . GLN F  1 16  ? 51.303  -15.177 32.945  1.00 22.88 ? 15  GLN H CD  1 
ATOM   5663  O  OE1 . GLN F  1 16  ? 50.488  -14.241 32.981  1.00 25.08 ? 15  GLN H OE1 1 
ATOM   5664  N  NE2 . GLN F  1 16  ? 51.111  -16.329 33.570  1.00 21.18 ? 15  GLN H NE2 1 
ATOM   5665  N  N   . GLY F  1 17  ? 53.021  -14.838 28.194  1.00 2.99  ? 16  GLY H N   1 
ATOM   5666  C  CA  . GLY F  1 17  ? 52.509  -13.795 27.309  1.00 2.00  ? 16  GLY H CA  1 
ATOM   5667  C  C   . GLY F  1 17  ? 51.742  -14.419 26.155  1.00 2.00  ? 16  GLY H C   1 
ATOM   5668  O  O   . GLY F  1 17  ? 51.664  -15.663 26.063  1.00 4.08  ? 16  GLY H O   1 
ATOM   5669  N  N   . ILE F  1 18  ? 51.134  -13.603 25.304  1.00 2.00  ? 17  ILE H N   1 
ATOM   5670  C  CA  . ILE F  1 18  ? 50.458  -14.109 24.131  1.00 2.00  ? 17  ILE H CA  1 
ATOM   5671  C  C   . ILE F  1 18  ? 50.934  -13.227 22.984  1.00 2.89  ? 17  ILE H C   1 
ATOM   5672  O  O   . ILE F  1 18  ? 50.809  -11.994 23.046  1.00 3.24  ? 17  ILE H O   1 
ATOM   5673  C  CB  . ILE F  1 18  ? 48.927  -14.025 24.284  1.00 2.00  ? 17  ILE H CB  1 
ATOM   5674  C  CG1 . ILE F  1 18  ? 48.458  -14.849 25.470  1.00 2.00  ? 17  ILE H CG1 1 
ATOM   5675  C  CG2 . ILE F  1 18  ? 48.275  -14.565 22.996  1.00 2.00  ? 17  ILE H CG2 1 
ATOM   5676  C  CD1 . ILE F  1 18  ? 46.953  -14.837 25.815  1.00 2.00  ? 17  ILE H CD1 1 
ATOM   5677  N  N   . ILE F  1 19  ? 51.525  -13.814 21.939  1.00 2.31  ? 18  ILE H N   1 
ATOM   5678  C  CA  . ILE F  1 19  ? 52.061  -13.063 20.824  1.00 2.00  ? 18  ILE H CA  1 
ATOM   5679  C  C   . ILE F  1 19  ? 51.318  -13.505 19.569  1.00 2.00  ? 18  ILE H C   1 
ATOM   5680  O  O   . ILE F  1 19  ? 51.058  -14.701 19.409  1.00 2.00  ? 18  ILE H O   1 
ATOM   5681  C  CB  . ILE F  1 19  ? 53.587  -13.334 20.766  1.00 2.00  ? 18  ILE H CB  1 
ATOM   5682  C  CG1 . ILE F  1 19  ? 54.294  -12.745 21.983  1.00 2.00  ? 18  ILE H CG1 1 
ATOM   5683  C  CG2 . ILE F  1 19  ? 54.142  -12.770 19.462  1.00 2.00  ? 18  ILE H CG2 1 
ATOM   5684  C  CD1 . ILE F  1 19  ? 53.991  -11.276 22.280  1.00 2.00  ? 18  ILE H CD1 1 
ATOM   5685  N  N   . ASN F  1 20  ? 50.990  -12.594 18.666  1.00 2.00  ? 19  ASN H N   1 
ATOM   5686  C  CA  . ASN F  1 20  ? 50.136  -12.889 17.537  1.00 2.90  ? 19  ASN H CA  1 
ATOM   5687  C  C   . ASN F  1 20  ? 50.927  -12.592 16.290  1.00 4.64  ? 19  ASN H C   1 
ATOM   5688  O  O   . ASN F  1 20  ? 51.775  -11.685 16.338  1.00 5.46  ? 19  ASN H O   1 
ATOM   5689  C  CB  . ASN F  1 20  ? 48.894  -12.005 17.481  1.00 2.00  ? 19  ASN H CB  1 
ATOM   5690  C  CG  . ASN F  1 20  ? 47.899  -12.178 18.607  1.00 2.59  ? 19  ASN H CG  1 
ATOM   5691  O  OD1 . ASN F  1 20  ? 46.929  -12.915 18.512  1.00 4.23  ? 19  ASN H OD1 1 
ATOM   5692  N  ND2 . ASN F  1 20  ? 47.986  -11.490 19.729  1.00 4.82  ? 19  ASN H ND2 1 
ATOM   5693  N  N   . PHE F  1 21  ? 50.658  -13.286 15.186  1.00 2.99  ? 20  PHE H N   1 
ATOM   5694  C  CA  . PHE F  1 21  ? 51.371  -13.016 13.957  1.00 5.49  ? 20  PHE H CA  1 
ATOM   5695  C  C   . PHE F  1 21  ? 50.348  -12.905 12.846  1.00 8.49  ? 20  PHE H C   1 
ATOM   5696  O  O   . PHE F  1 21  ? 49.396  -13.690 12.833  1.00 9.85  ? 20  PHE H O   1 
ATOM   5697  C  CB  . PHE F  1 21  ? 52.314  -14.127 13.587  1.00 5.42  ? 20  PHE H CB  1 
ATOM   5698  C  CG  . PHE F  1 21  ? 53.432  -14.390 14.609  1.00 3.92  ? 20  PHE H CG  1 
ATOM   5699  C  CD1 . PHE F  1 21  ? 54.611  -13.682 14.520  1.00 3.76  ? 20  PHE H CD1 1 
ATOM   5700  C  CD2 . PHE F  1 21  ? 53.278  -15.384 15.551  1.00 2.00  ? 20  PHE H CD2 1 
ATOM   5701  C  CE1 . PHE F  1 21  ? 55.628  -13.961 15.389  1.00 3.87  ? 20  PHE H CE1 1 
ATOM   5702  C  CE2 . PHE F  1 21  ? 54.296  -15.663 16.422  1.00 2.00  ? 20  PHE H CE2 1 
ATOM   5703  C  CZ  . PHE F  1 21  ? 55.475  -14.961 16.326  1.00 4.46  ? 20  PHE H CZ  1 
ATOM   5704  N  N   . GLU F  1 22  ? 50.483  -11.952 11.919  1.00 11.09 ? 21  GLU H N   1 
ATOM   5705  C  CA  . GLU F  1 22  ? 49.551  -11.820 10.805  1.00 12.58 ? 21  GLU H CA  1 
ATOM   5706  C  C   . GLU F  1 22  ? 50.273  -11.542 9.508   1.00 11.79 ? 21  GLU H C   1 
ATOM   5707  O  O   . GLU F  1 22  ? 51.028  -10.567 9.455   1.00 10.94 ? 21  GLU H O   1 
ATOM   5708  C  CB  . GLU F  1 22  ? 48.609  -10.685 11.021  1.00 13.81 ? 21  GLU H CB  1 
ATOM   5709  C  CG  . GLU F  1 22  ? 47.492  -10.629 10.011  1.00 17.31 ? 21  GLU H CG  1 
ATOM   5710  C  CD  . GLU F  1 22  ? 46.514  -9.589  10.493  1.00 22.18 ? 21  GLU H CD  1 
ATOM   5711  O  OE1 . GLU F  1 22  ? 46.726  -8.416  10.178  1.00 27.21 ? 21  GLU H OE1 1 
ATOM   5712  O  OE2 . GLU F  1 22  ? 45.570  -9.938  11.209  1.00 22.97 ? 21  GLU H OE2 1 
ATOM   5713  N  N   . GLN F  1 23  ? 50.089  -12.362 8.478   1.00 11.22 ? 22  GLN H N   1 
ATOM   5714  C  CA  . GLN F  1 23  ? 50.695  -12.077 7.190   1.00 11.29 ? 22  GLN H CA  1 
ATOM   5715  C  C   . GLN F  1 23  ? 49.520  -11.850 6.250   1.00 12.80 ? 22  GLN H C   1 
ATOM   5716  O  O   . GLN F  1 23  ? 48.775  -12.785 5.980   1.00 11.10 ? 22  GLN H O   1 
ATOM   5717  C  CB  . GLN F  1 23  ? 51.516  -13.254 6.768   1.00 6.36  ? 22  GLN H CB  1 
ATOM   5718  C  CG  . GLN F  1 23  ? 52.381  -12.972 5.617   1.00 2.00  ? 22  GLN H CG  1 
ATOM   5719  C  CD  . GLN F  1 23  ? 53.417  -14.047 5.380   1.00 2.42  ? 22  GLN H CD  1 
ATOM   5720  O  OE1 . GLN F  1 23  ? 53.327  -15.235 5.690   1.00 2.00  ? 22  GLN H OE1 1 
ATOM   5721  N  NE2 . GLN F  1 23  ? 54.528  -13.603 4.828   1.00 4.73  ? 22  GLN H NE2 1 
ATOM   5722  N  N   . LYS F  1 24  ? 49.256  -10.620 5.795   1.00 17.93 ? 23  LYS H N   1 
ATOM   5723  C  CA  . LYS F  1 24  ? 48.135  -10.358 4.884   1.00 23.48 ? 23  LYS H CA  1 
ATOM   5724  C  C   . LYS F  1 24  ? 48.338  -11.038 3.551   1.00 25.90 ? 23  LYS H C   1 
ATOM   5725  O  O   . LYS F  1 24  ? 47.363  -11.388 2.904   1.00 28.14 ? 23  LYS H O   1 
ATOM   5726  C  CB  . LYS F  1 24  ? 47.920  -8.909  4.464   1.00 28.86 ? 23  LYS H CB  1 
ATOM   5727  C  CG  . LYS F  1 24  ? 47.631  -7.819  5.473   1.00 33.65 ? 23  LYS H CG  1 
ATOM   5728  C  CD  . LYS F  1 24  ? 46.332  -8.094  6.208   1.00 38.33 ? 23  LYS H CD  1 
ATOM   5729  C  CE  . LYS F  1 24  ? 46.272  -7.075  7.339   1.00 41.05 ? 23  LYS H CE  1 
ATOM   5730  N  NZ  . LYS F  1 24  ? 44.914  -6.806  7.774   1.00 42.96 ? 23  LYS H NZ  1 
ATOM   5731  N  N   . GLU F  1 25  ? 49.557  -11.205 3.051   1.00 28.44 ? 24  GLU H N   1 
ATOM   5732  C  CA  . GLU F  1 25  ? 49.731  -11.891 1.784   1.00 30.16 ? 24  GLU H CA  1 
ATOM   5733  C  C   . GLU F  1 25  ? 51.030  -12.671 1.834   1.00 29.72 ? 24  GLU H C   1 
ATOM   5734  O  O   . GLU F  1 25  ? 51.985  -12.272 2.494   1.00 31.08 ? 24  GLU H O   1 
ATOM   5735  C  CB  . GLU F  1 25  ? 49.755  -10.869 0.659   1.00 32.24 ? 24  GLU H CB  1 
ATOM   5736  C  CG  . GLU F  1 25  ? 50.939  -9.949  0.814   1.00 38.98 ? 24  GLU H CG  1 
ATOM   5737  C  CD  . GLU F  1 25  ? 50.858  -8.680  0.000   1.00 44.30 ? 24  GLU H CD  1 
ATOM   5738  O  OE1 . GLU F  1 25  ? 51.254  -8.708  -1.178  1.00 47.88 ? 24  GLU H OE1 1 
ATOM   5739  O  OE2 . GLU F  1 25  ? 50.415  -7.673  0.574   1.00 46.78 ? 24  GLU H OE2 1 
ATOM   5740  N  N   . SER F  1 26  ? 51.055  -13.756 1.101   1.00 30.14 ? 25  SER H N   1 
ATOM   5741  C  CA  . SER F  1 26  ? 52.138  -14.717 0.957   1.00 31.56 ? 25  SER H CA  1 
ATOM   5742  C  C   . SER F  1 26  ? 53.576  -14.214 0.917   1.00 31.21 ? 25  SER H C   1 
ATOM   5743  O  O   . SER F  1 26  ? 54.516  -14.811 1.474   1.00 33.05 ? 25  SER H O   1 
ATOM   5744  C  CB  . SER F  1 26  ? 51.833  -15.524 -0.311  1.00 31.79 ? 25  SER H CB  1 
ATOM   5745  O  OG  . SER F  1 26  ? 50.855  -14.844 -1.134  1.00 38.15 ? 25  SER H OG  1 
ATOM   5746  N  N   . ASN F  1 27  ? 53.752  -13.114 0.205   1.00 29.05 ? 26  ASN H N   1 
ATOM   5747  C  CA  . ASN F  1 27  ? 55.086  -12.566 0.030   1.00 27.61 ? 26  ASN H CA  1 
ATOM   5748  C  C   . ASN F  1 27  ? 55.278  -11.282 0.860   1.00 23.52 ? 26  ASN H C   1 
ATOM   5749  O  O   . ASN F  1 27  ? 56.330  -10.648 0.785   1.00 24.96 ? 26  ASN H O   1 
ATOM   5750  C  CB  . ASN F  1 27  ? 55.290  -12.330 -1.500  1.00 30.45 ? 26  ASN H CB  1 
ATOM   5751  C  CG  . ASN F  1 27  ? 54.399  -11.224 -2.085  1.00 33.06 ? 26  ASN H CG  1 
ATOM   5752  O  OD1 . ASN F  1 27  ? 53.205  -11.083 -1.770  1.00 34.05 ? 26  ASN H OD1 1 
ATOM   5753  N  ND2 . ASN F  1 27  ? 54.951  -10.369 -2.927  1.00 35.07 ? 26  ASN H ND2 1 
ATOM   5754  N  N   . GLY F  1 28  ? 54.312  -10.858 1.678   1.00 17.73 ? 27  GLY H N   1 
ATOM   5755  C  CA  . GLY F  1 28  ? 54.428  -9.647  2.468   1.00 12.19 ? 27  GLY H CA  1 
ATOM   5756  C  C   . GLY F  1 28  ? 54.985  -9.861  3.882   1.00 8.40  ? 27  GLY H C   1 
ATOM   5757  O  O   . GLY F  1 28  ? 55.355  -10.957 4.301   1.00 6.40  ? 27  GLY H O   1 
ATOM   5758  N  N   . PRO F  1 29  ? 55.113  -8.789  4.646   1.00 5.66  ? 28  PRO H N   1 
ATOM   5759  C  CA  . PRO F  1 29  ? 55.559  -8.839  6.013   1.00 4.59  ? 28  PRO H CA  1 
ATOM   5760  C  C   . PRO F  1 29  ? 54.541  -9.447  6.953   1.00 4.64  ? 28  PRO H C   1 
ATOM   5761  O  O   . PRO F  1 29  ? 53.332  -9.427  6.667   1.00 4.73  ? 28  PRO H O   1 
ATOM   5762  C  CB  . PRO F  1 29  ? 55.887  -7.410  6.314   1.00 5.05  ? 28  PRO H CB  1 
ATOM   5763  C  CG  . PRO F  1 29  ? 54.919  -6.606  5.478   1.00 2.42  ? 28  PRO H CG  1 
ATOM   5764  C  CD  . PRO F  1 29  ? 54.941  -7.415  4.189   1.00 4.09  ? 28  PRO H CD  1 
ATOM   5765  N  N   . VAL F  1 30  ? 55.057  -9.981  8.066   1.00 3.69  ? 29  VAL H N   1 
ATOM   5766  C  CA  . VAL F  1 30  ? 54.188  -10.554 9.076   1.00 5.57  ? 29  VAL H CA  1 
ATOM   5767  C  C   . VAL F  1 30  ? 54.305  -9.658  10.286  1.00 5.12  ? 29  VAL H C   1 
ATOM   5768  O  O   . VAL F  1 30  ? 55.395  -9.271  10.684  1.00 9.46  ? 29  VAL H O   1 
ATOM   5769  C  CB  . VAL F  1 30  ? 54.546  -12.109 9.356   1.00 2.00  ? 29  VAL H CB  1 
ATOM   5770  C  CG1 . VAL F  1 30  ? 55.853  -12.451 8.750   1.00 2.00  ? 29  VAL H CG1 1 
ATOM   5771  C  CG2 . VAL F  1 30  ? 54.498  -12.441 10.807  1.00 2.00  ? 29  VAL H CG2 1 
ATOM   5772  N  N   . LYS F  1 31  ? 53.150  -9.153  10.696  1.00 5.65  ? 30  LYS H N   1 
ATOM   5773  C  CA  . LYS F  1 31  ? 53.017  -8.254  11.834  1.00 7.46  ? 30  LYS H CA  1 
ATOM   5774  C  C   . LYS F  1 31  ? 53.085  -9.086  13.087  1.00 6.06  ? 30  LYS H C   1 
ATOM   5775  O  O   . LYS F  1 31  ? 52.424  -10.126 13.104  1.00 5.74  ? 30  LYS H O   1 
ATOM   5776  C  CB  . LYS F  1 31  ? 51.676  -7.572  11.883  1.00 10.18 ? 30  LYS H CB  1 
ATOM   5777  C  CG  . LYS F  1 31  ? 51.604  -6.111  11.513  1.00 15.20 ? 30  LYS H CG  1 
ATOM   5778  C  CD  . LYS F  1 31  ? 50.371  -5.566  12.236  1.00 21.47 ? 30  LYS H CD  1 
ATOM   5779  C  CE  . LYS F  1 31  ? 50.606  -5.495  13.765  1.00 26.53 ? 30  LYS H CE  1 
ATOM   5780  N  NZ  . LYS F  1 31  ? 49.408  -5.114  14.513  1.00 27.57 ? 30  LYS H NZ  1 
ATOM   5781  N  N   . VAL F  1 32  ? 53.818  -8.721  14.123  1.00 4.89  ? 31  VAL H N   1 
ATOM   5782  C  CA  . VAL F  1 32  ? 53.744  -9.523  15.322  1.00 4.85  ? 31  VAL H CA  1 
ATOM   5783  C  C   . VAL F  1 32  ? 53.483  -8.537  16.431  1.00 2.44  ? 31  VAL H C   1 
ATOM   5784  O  O   . VAL F  1 32  ? 54.166  -7.545  16.537  1.00 3.00  ? 31  VAL H O   1 
ATOM   5785  C  CB  . VAL F  1 32  ? 55.064  -10.411 15.477  1.00 3.02  ? 31  VAL H CB  1 
ATOM   5786  C  CG1 . VAL F  1 32  ? 56.111  -10.063 14.433  1.00 2.00  ? 31  VAL H CG1 1 
ATOM   5787  C  CG2 . VAL F  1 32  ? 55.545  -10.339 16.904  1.00 2.00  ? 31  VAL H CG2 1 
ATOM   5788  N  N   . TRP F  1 33  ? 52.440  -8.713  17.202  1.00 2.00  ? 32  TRP H N   1 
ATOM   5789  C  CA  . TRP F  1 33  ? 52.111  -7.830  18.287  1.00 2.00  ? 32  TRP H CA  1 
ATOM   5790  C  C   . TRP F  1 33  ? 51.629  -8.639  19.460  1.00 2.00  ? 32  TRP H C   1 
ATOM   5791  O  O   . TRP F  1 33  ? 51.212  -9.778  19.269  1.00 2.00  ? 32  TRP H O   1 
ATOM   5792  C  CB  . TRP F  1 33  ? 51.035  -6.886  17.851  1.00 2.00  ? 32  TRP H CB  1 
ATOM   5793  C  CG  . TRP F  1 33  ? 49.695  -7.505  17.532  1.00 2.38  ? 32  TRP H CG  1 
ATOM   5794  C  CD1 . TRP F  1 33  ? 48.713  -7.396  18.447  1.00 2.00  ? 32  TRP H CD1 1 
ATOM   5795  C  CD2 . TRP F  1 33  ? 49.299  -8.180  16.386  1.00 8.26  ? 32  TRP H CD2 1 
ATOM   5796  N  NE1 . TRP F  1 33  ? 47.699  -8.008  17.906  1.00 7.06  ? 32  TRP H NE1 1 
ATOM   5797  C  CE2 . TRP F  1 33  ? 47.999  -8.495  16.693  1.00 7.40  ? 32  TRP H CE2 1 
ATOM   5798  C  CE3 . TRP F  1 33  ? 49.806  -8.608  15.166  1.00 12.97 ? 32  TRP H CE3 1 
ATOM   5799  C  CZ2 . TRP F  1 33  ? 47.193  -9.198  15.811  1.00 11.91 ? 32  TRP H CZ2 1 
ATOM   5800  C  CZ3 . TRP F  1 33  ? 49.001  -9.304  14.278  1.00 13.51 ? 32  TRP H CZ3 1 
ATOM   5801  C  CH2 . TRP F  1 33  ? 47.696  -9.613  14.590  1.00 10.87 ? 32  TRP H CH2 1 
ATOM   5802  N  N   . GLY F  1 34  ? 51.623  -8.174  20.684  1.00 2.00  ? 33  GLY H N   1 
ATOM   5803  C  CA  . GLY F  1 34  ? 51.083  -8.942  21.798  1.00 2.00  ? 33  GLY H CA  1 
ATOM   5804  C  C   . GLY F  1 34  ? 51.651  -8.411  23.102  1.00 2.97  ? 33  GLY H C   1 
ATOM   5805  O  O   . GLY F  1 34  ? 52.069  -7.256  23.119  1.00 3.38  ? 33  GLY H O   1 
ATOM   5806  N  N   . SER F  1 35  ? 51.700  -9.173  24.202  1.00 4.04  ? 34  SER H N   1 
ATOM   5807  C  CA  . SER F  1 35  ? 52.404  -8.740  25.388  1.00 4.72  ? 34  SER H CA  1 
ATOM   5808  C  C   . SER F  1 35  ? 52.983  -9.897  26.166  1.00 4.52  ? 34  SER H C   1 
ATOM   5809  O  O   . SER F  1 35  ? 52.526  -11.031 26.030  1.00 4.84  ? 34  SER H O   1 
ATOM   5810  C  CB  . SER F  1 35  ? 51.508  -7.935  26.307  1.00 6.21  ? 34  SER H CB  1 
ATOM   5811  O  OG  . SER F  1 35  ? 50.448  -8.635  26.927  1.00 12.73 ? 34  SER H OG  1 
ATOM   5812  N  N   . ILE F  1 36  ? 54.031  -9.615  26.928  1.00 2.27  ? 35  ILE H N   1 
ATOM   5813  C  CA  . ILE F  1 36  ? 54.668  -10.565 27.780  1.00 3.39  ? 35  ILE H CA  1 
ATOM   5814  C  C   . ILE F  1 36  ? 54.732  -9.860  29.144  1.00 6.47  ? 35  ILE H C   1 
ATOM   5815  O  O   . ILE F  1 36  ? 55.004  -8.651  29.238  1.00 6.04  ? 35  ILE H O   1 
ATOM   5816  C  CB  . ILE F  1 36  ? 56.032  -10.855 27.189  1.00 3.69  ? 35  ILE H CB  1 
ATOM   5817  C  CG1 . ILE F  1 36  ? 55.891  -11.595 25.881  1.00 4.61  ? 35  ILE H CG1 1 
ATOM   5818  C  CG2 . ILE F  1 36  ? 56.817  -11.704 28.138  1.00 2.00  ? 35  ILE H CG2 1 
ATOM   5819  C  CD1 . ILE F  1 36  ? 57.101  -11.262 24.982  1.00 7.81  ? 35  ILE H CD1 1 
ATOM   5820  N  N   . LYS F  1 37  ? 54.466  -10.591 30.227  1.00 6.86  ? 36  LYS H N   1 
ATOM   5821  C  CA  . LYS F  1 37  ? 54.460  -10.054 31.574  1.00 7.24  ? 36  LYS H CA  1 
ATOM   5822  C  C   . LYS F  1 37  ? 55.549  -10.789 32.320  1.00 6.62  ? 36  LYS H C   1 
ATOM   5823  O  O   . LYS F  1 37  ? 55.950  -11.873 31.876  1.00 6.51  ? 36  LYS H O   1 
ATOM   5824  C  CB  . LYS F  1 37  ? 53.197  -10.369 32.325  1.00 8.20  ? 36  LYS H CB  1 
ATOM   5825  C  CG  . LYS F  1 37  ? 51.835  -10.293 31.674  1.00 15.12 ? 36  LYS H CG  1 
ATOM   5826  C  CD  . LYS F  1 37  ? 50.890  -11.119 32.574  1.00 20.93 ? 36  LYS H CD  1 
ATOM   5827  C  CE  . LYS F  1 37  ? 49.412  -11.148 32.117  1.00 26.63 ? 36  LYS H CE  1 
ATOM   5828  N  NZ  . LYS F  1 37  ? 48.570  -11.938 33.022  1.00 28.41 ? 36  LYS H NZ  1 
ATOM   5829  N  N   . GLY F  1 38  ? 55.996  -10.236 33.455  1.00 5.44  ? 37  GLY H N   1 
ATOM   5830  C  CA  . GLY F  1 38  ? 56.909  -10.911 34.385  1.00 3.59  ? 37  GLY H CA  1 
ATOM   5831  C  C   . GLY F  1 38  ? 58.363  -10.767 34.004  1.00 5.28  ? 37  GLY H C   1 
ATOM   5832  O  O   . GLY F  1 38  ? 59.253  -11.567 34.330  1.00 7.52  ? 37  GLY H O   1 
ATOM   5833  N  N   . LEU F  1 39  ? 58.618  -9.680  33.301  1.00 6.02  ? 38  LEU H N   1 
ATOM   5834  C  CA  . LEU F  1 39  ? 59.922  -9.431  32.746  1.00 5.09  ? 38  LEU H CA  1 
ATOM   5835  C  C   . LEU F  1 39  ? 60.695  -8.503  33.643  1.00 5.15  ? 38  LEU H C   1 
ATOM   5836  O  O   . LEU F  1 39  ? 60.066  -7.787  34.418  1.00 8.07  ? 38  LEU H O   1 
ATOM   5837  C  CB  . LEU F  1 39  ? 59.652  -8.848  31.366  1.00 4.69  ? 38  LEU H CB  1 
ATOM   5838  C  CG  . LEU F  1 39  ? 59.958  -9.623  30.125  1.00 2.00  ? 38  LEU H CG  1 
ATOM   5839  C  CD1 . LEU F  1 39  ? 59.851  -11.077 30.328  1.00 2.00  ? 38  LEU H CD1 1 
ATOM   5840  C  CD2 . LEU F  1 39  ? 59.025  -9.139  29.091  1.00 2.00  ? 38  LEU H CD2 1 
ATOM   5841  N  N   . THR F  1 40  ? 62.020  -8.495  33.665  1.00 4.85  ? 39  THR H N   1 
ATOM   5842  C  CA  . THR F  1 40  ? 62.761  -7.438  34.337  1.00 5.05  ? 39  THR H CA  1 
ATOM   5843  C  C   . THR F  1 40  ? 62.777  -6.309  33.311  1.00 4.81  ? 39  THR H C   1 
ATOM   5844  O  O   . THR F  1 40  ? 62.611  -6.554  32.120  1.00 5.54  ? 39  THR H O   1 
ATOM   5845  C  CB  . THR F  1 40  ? 64.156  -7.947  34.655  1.00 3.14  ? 39  THR H CB  1 
ATOM   5846  O  OG1 . THR F  1 40  ? 64.696  -8.473  33.449  1.00 10.23 ? 39  THR H OG1 1 
ATOM   5847  C  CG2 . THR F  1 40  ? 64.157  -9.035  35.683  1.00 4.37  ? 39  THR H CG2 1 
ATOM   5848  N  N   . GLU F  1 41  ? 63.044  -5.083  33.686  1.00 7.50  ? 40  GLU H N   1 
ATOM   5849  C  CA  . GLU F  1 41  ? 62.949  -3.924  32.797  1.00 7.75  ? 40  GLU H CA  1 
ATOM   5850  C  C   . GLU F  1 41  ? 63.996  -3.976  31.740  1.00 8.33  ? 40  GLU H C   1 
ATOM   5851  O  O   . GLU F  1 41  ? 65.111  -4.383  32.062  1.00 11.56 ? 40  GLU H O   1 
ATOM   5852  C  CB  . GLU F  1 41  ? 63.202  -2.638  33.503  1.00 5.74  ? 40  GLU H CB  1 
ATOM   5853  C  CG  . GLU F  1 41  ? 62.078  -1.676  33.643  1.00 12.48 ? 40  GLU H CG  1 
ATOM   5854  C  CD  . GLU F  1 41  ? 62.563  -0.251  33.983  1.00 16.56 ? 40  GLU H CD  1 
ATOM   5855  O  OE1 . GLU F  1 41  ? 63.100  -0.062  35.079  1.00 19.97 ? 40  GLU H OE1 1 
ATOM   5856  O  OE2 . GLU F  1 41  ? 62.416  0.670   33.159  1.00 18.00 ? 40  GLU H OE2 1 
ATOM   5857  N  N   . GLY F  1 42  ? 63.677  -3.531  30.541  1.00 8.02  ? 41  GLY H N   1 
ATOM   5858  C  CA  . GLY F  1 42  ? 64.698  -3.369  29.547  1.00 7.30  ? 41  GLY H CA  1 
ATOM   5859  C  C   . GLY F  1 42  ? 64.583  -4.364  28.466  1.00 6.14  ? 41  GLY H C   1 
ATOM   5860  O  O   . GLY F  1 42  ? 63.536  -4.996  28.341  1.00 7.91  ? 41  GLY H O   1 
ATOM   5861  N  N   . LEU F  1 43  ? 65.690  -4.512  27.740  1.00 5.82  ? 42  LEU H N   1 
ATOM   5862  C  CA  . LEU F  1 43  ? 65.726  -5.379  26.553  1.00 5.11  ? 42  LEU H CA  1 
ATOM   5863  C  C   . LEU F  1 43  ? 65.800  -6.853  26.832  1.00 4.01  ? 42  LEU H C   1 
ATOM   5864  O  O   . LEU F  1 43  ? 66.458  -7.267  27.777  1.00 7.39  ? 42  LEU H O   1 
ATOM   5865  C  CB  . LEU F  1 43  ? 66.915  -5.028  25.673  1.00 5.85  ? 42  LEU H CB  1 
ATOM   5866  C  CG  . LEU F  1 43  ? 67.018  -3.843  24.747  1.00 2.00  ? 42  LEU H CG  1 
ATOM   5867  C  CD1 . LEU F  1 43  ? 66.005  -2.822  25.078  1.00 2.00  ? 42  LEU H CD1 1 
ATOM   5868  C  CD2 . LEU F  1 43  ? 68.448  -3.434  24.742  1.00 2.00  ? 42  LEU H CD2 1 
ATOM   5869  N  N   . HIS F  1 44  ? 65.125  -7.679  26.057  1.00 4.25  ? 43  HIS H N   1 
ATOM   5870  C  CA  . HIS F  1 44  ? 65.110  -9.105  26.212  1.00 2.00  ? 43  HIS H CA  1 
ATOM   5871  C  C   . HIS F  1 44  ? 65.111  -9.578  24.779  1.00 2.47  ? 43  HIS H C   1 
ATOM   5872  O  O   . HIS F  1 44  ? 64.312  -9.082  23.979  1.00 2.00  ? 43  HIS H O   1 
ATOM   5873  C  CB  . HIS F  1 44  ? 63.837  -9.547  26.879  1.00 2.00  ? 43  HIS H CB  1 
ATOM   5874  C  CG  . HIS F  1 44  ? 63.866  -9.352  28.384  1.00 2.00  ? 43  HIS H CG  1 
ATOM   5875  N  ND1 . HIS F  1 44  ? 64.451  -10.103 29.314  1.00 2.00  ? 43  HIS H ND1 1 
ATOM   5876  C  CD2 . HIS F  1 44  ? 63.335  -8.264  29.027  1.00 2.00  ? 43  HIS H CD2 1 
ATOM   5877  C  CE1 . HIS F  1 44  ? 64.305  -9.504  30.467  1.00 2.00  ? 43  HIS H CE1 1 
ATOM   5878  N  NE2 . HIS F  1 44  ? 63.630  -8.403  30.291  1.00 2.00  ? 43  HIS H NE2 1 
ATOM   5879  N  N   . GLY F  1 45  ? 65.988  -10.524 24.434  1.00 2.55  ? 44  GLY H N   1 
ATOM   5880  C  CA  . GLY F  1 45  ? 66.066  -11.134 23.123  1.00 2.00  ? 44  GLY H CA  1 
ATOM   5881  C  C   . GLY F  1 45  ? 64.776  -11.769 22.737  1.00 2.00  ? 44  GLY H C   1 
ATOM   5882  O  O   . GLY F  1 45  ? 64.184  -12.289 23.646  1.00 2.00  ? 44  GLY H O   1 
ATOM   5883  N  N   . PHE F  1 46  ? 64.313  -11.762 21.504  1.00 2.00  ? 45  PHE H N   1 
ATOM   5884  C  CA  . PHE F  1 46  ? 63.038  -12.336 21.121  1.00 2.11  ? 45  PHE H CA  1 
ATOM   5885  C  C   . PHE F  1 46  ? 63.317  -13.127 19.853  1.00 2.00  ? 45  PHE H C   1 
ATOM   5886  O  O   . PHE F  1 46  ? 63.721  -12.517 18.860  1.00 2.05  ? 45  PHE H O   1 
ATOM   5887  C  CB  . PHE F  1 46  ? 62.096  -11.214 20.863  1.00 2.00  ? 45  PHE H CB  1 
ATOM   5888  C  CG  . PHE F  1 46  ? 60.628  -11.497 20.705  1.00 2.00  ? 45  PHE H CG  1 
ATOM   5889  C  CD1 . PHE F  1 46  ? 59.873  -11.980 21.767  1.00 3.57  ? 45  PHE H CD1 1 
ATOM   5890  C  CD2 . PHE F  1 46  ? 60.008  -11.150 19.511  1.00 2.00  ? 45  PHE H CD2 1 
ATOM   5891  C  CE1 . PHE F  1 46  ? 58.506  -12.111 21.607  1.00 2.83  ? 45  PHE H CE1 1 
ATOM   5892  C  CE2 . PHE F  1 46  ? 58.643  -11.285 19.363  1.00 2.00  ? 45  PHE H CE2 1 
ATOM   5893  C  CZ  . PHE F  1 46  ? 57.890  -11.754 20.408  1.00 2.65  ? 45  PHE H CZ  1 
ATOM   5894  N  N   . HIS F  1 47  ? 63.152  -14.437 19.765  1.00 2.00  ? 46  HIS H N   1 
ATOM   5895  C  CA  . HIS F  1 47  ? 63.624  -15.133 18.600  1.00 2.00  ? 46  HIS H CA  1 
ATOM   5896  C  C   . HIS F  1 47  ? 62.808  -16.324 18.339  1.00 2.00  ? 46  HIS H C   1 
ATOM   5897  O  O   . HIS F  1 47  ? 62.150  -16.793 19.228  1.00 4.97  ? 46  HIS H O   1 
ATOM   5898  C  CB  . HIS F  1 47  ? 65.015  -15.693 18.725  1.00 2.32  ? 46  HIS H CB  1 
ATOM   5899  C  CG  . HIS F  1 47  ? 66.078  -14.846 19.389  1.00 2.72  ? 46  HIS H CG  1 
ATOM   5900  N  ND1 . HIS F  1 47  ? 66.772  -15.158 20.482  1.00 2.00  ? 46  HIS H ND1 1 
ATOM   5901  C  CD2 . HIS F  1 47  ? 66.474  -13.604 18.954  1.00 2.91  ? 46  HIS H CD2 1 
ATOM   5902  C  CE1 . HIS F  1 47  ? 67.561  -14.147 20.724  1.00 2.00  ? 46  HIS H CE1 1 
ATOM   5903  N  NE2 . HIS F  1 47  ? 67.376  -13.209 19.810  1.00 2.00  ? 46  HIS H NE2 1 
ATOM   5904  N  N   . VAL F  1 48  ? 62.861  -16.870 17.157  1.00 2.00  ? 47  VAL H N   1 
ATOM   5905  C  CA  . VAL F  1 48  ? 62.094  -18.020 16.777  1.00 2.00  ? 47  VAL H CA  1 
ATOM   5906  C  C   . VAL F  1 48  ? 63.163  -19.073 16.671  1.00 2.00  ? 47  VAL H C   1 
ATOM   5907  O  O   . VAL F  1 48  ? 64.172  -18.896 15.971  1.00 2.00  ? 47  VAL H O   1 
ATOM   5908  C  CB  . VAL F  1 48  ? 61.391  -17.772 15.425  1.00 2.04  ? 47  VAL H CB  1 
ATOM   5909  C  CG1 . VAL F  1 48  ? 60.627  -19.035 15.038  1.00 2.00  ? 47  VAL H CG1 1 
ATOM   5910  C  CG2 . VAL F  1 48  ? 60.474  -16.555 15.504  1.00 2.00  ? 47  VAL H CG2 1 
ATOM   5911  N  N   . HIS F  1 49  ? 63.016  -20.127 17.452  1.00 2.00  ? 48  HIS H N   1 
ATOM   5912  C  CA  . HIS F  1 49  ? 63.966  -21.226 17.483  1.00 2.00  ? 48  HIS H CA  1 
ATOM   5913  C  C   . HIS F  1 49  ? 63.341  -22.350 16.651  1.00 2.00  ? 48  HIS H C   1 
ATOM   5914  O  O   . HIS F  1 49  ? 62.137  -22.480 16.460  1.00 2.00  ? 48  HIS H O   1 
ATOM   5915  C  CB  . HIS F  1 49  ? 64.277  -21.655 18.996  1.00 2.00  ? 48  HIS H CB  1 
ATOM   5916  C  CG  . HIS F  1 49  ? 65.201  -20.721 19.831  1.00 2.00  ? 48  HIS H CG  1 
ATOM   5917  N  ND1 . HIS F  1 49  ? 66.287  -20.986 20.533  1.00 2.00  ? 48  HIS H ND1 1 
ATOM   5918  C  CD2 . HIS F  1 49  ? 65.089  -19.379 19.946  1.00 2.00  ? 48  HIS H CD2 1 
ATOM   5919  C  CE1 . HIS F  1 49  ? 66.820  -19.923 21.027  1.00 2.00  ? 48  HIS H CE1 1 
ATOM   5920  N  NE2 . HIS F  1 49  ? 66.082  -18.923 20.668  1.00 2.00  ? 48  HIS H NE2 1 
ATOM   5921  N  N   . GLU F  1 50  ? 64.213  -23.177 16.111  1.00 3.15  ? 49  GLU H N   1 
ATOM   5922  C  CA  . GLU F  1 50  ? 63.938  -24.157 15.104  1.00 2.00  ? 49  GLU H CA  1 
ATOM   5923  C  C   . GLU F  1 50  ? 62.918  -25.245 15.352  1.00 2.68  ? 49  GLU H C   1 
ATOM   5924  O  O   . GLU F  1 50  ? 62.288  -25.687 14.395  1.00 2.00  ? 49  GLU H O   1 
ATOM   5925  C  CB  . GLU F  1 50  ? 65.265  -24.746 14.782  1.00 2.22  ? 49  GLU H CB  1 
ATOM   5926  C  CG  . GLU F  1 50  ? 65.247  -25.512 13.461  1.00 8.17  ? 49  GLU H CG  1 
ATOM   5927  C  CD  . GLU F  1 50  ? 66.567  -26.135 13.015  1.00 9.14  ? 49  GLU H CD  1 
ATOM   5928  O  OE1 . GLU F  1 50  ? 67.625  -25.812 13.563  1.00 13.06 ? 49  GLU H OE1 1 
ATOM   5929  O  OE2 . GLU F  1 50  ? 66.524  -26.964 12.106  1.00 12.38 ? 49  GLU H OE2 1 
ATOM   5930  N  N   . PHE F  1 51  ? 62.730  -25.787 16.553  1.00 3.05  ? 50  PHE H N   1 
ATOM   5931  C  CA  . PHE F  1 51  ? 61.819  -26.910 16.694  1.00 2.81  ? 50  PHE H CA  1 
ATOM   5932  C  C   . PHE F  1 51  ? 60.731  -26.463 17.608  1.00 2.98  ? 50  PHE H C   1 
ATOM   5933  O  O   . PHE F  1 51  ? 60.994  -25.797 18.594  1.00 3.15  ? 50  PHE H O   1 
ATOM   5934  C  CB  . PHE F  1 51  ? 62.473  -28.150 17.335  1.00 2.00  ? 50  PHE H CB  1 
ATOM   5935  C  CG  . PHE F  1 51  ? 63.738  -28.508 16.619  1.00 2.00  ? 50  PHE H CG  1 
ATOM   5936  C  CD1 . PHE F  1 51  ? 63.679  -28.894 15.306  1.00 2.00  ? 50  PHE H CD1 1 
ATOM   5937  C  CD2 . PHE F  1 51  ? 64.935  -28.334 17.268  1.00 2.00  ? 50  PHE H CD2 1 
ATOM   5938  C  CE1 . PHE F  1 51  ? 64.843  -29.093 14.616  1.00 2.00  ? 50  PHE H CE1 1 
ATOM   5939  C  CE2 . PHE F  1 51  ? 66.105  -28.533 16.580  1.00 2.00  ? 50  PHE H CE2 1 
ATOM   5940  C  CZ  . PHE F  1 51  ? 66.054  -28.909 15.249  1.00 2.00  ? 50  PHE H CZ  1 
ATOM   5941  N  N   . GLY F  1 52  ? 59.497  -26.815 17.356  1.00 3.74  ? 51  GLY H N   1 
ATOM   5942  C  CA  . GLY F  1 52  ? 58.470  -26.503 18.300  1.00 3.17  ? 51  GLY H CA  1 
ATOM   5943  C  C   . GLY F  1 52  ? 58.353  -27.723 19.128  1.00 3.06  ? 51  GLY H C   1 
ATOM   5944  O  O   . GLY F  1 52  ? 57.303  -28.359 19.121  1.00 2.98  ? 51  GLY H O   1 
ATOM   5945  N  N   . ASP F  1 53  ? 59.457  -28.059 19.797  1.00 5.79  ? 52  ASP H N   1 
ATOM   5946  C  CA  . ASP F  1 53  ? 59.562  -29.253 20.635  1.00 7.38  ? 52  ASP H CA  1 
ATOM   5947  C  C   . ASP F  1 53  ? 59.653  -28.761 22.076  1.00 9.96  ? 52  ASP H C   1 
ATOM   5948  O  O   . ASP F  1 53  ? 60.598  -28.121 22.565  1.00 11.61 ? 52  ASP H O   1 
ATOM   5949  C  CB  . ASP F  1 53  ? 60.804  -29.995 20.184  1.00 10.46 ? 52  ASP H CB  1 
ATOM   5950  C  CG  . ASP F  1 53  ? 61.048  -31.385 20.766  1.00 13.80 ? 52  ASP H CG  1 
ATOM   5951  O  OD1 . ASP F  1 53  ? 60.585  -31.634 21.863  1.00 13.13 ? 52  ASP H OD1 1 
ATOM   5952  O  OD2 . ASP F  1 53  ? 61.719  -32.224 20.153  1.00 12.98 ? 52  ASP H OD2 1 
ATOM   5953  N  N   . ASN F  1 54  ? 58.568  -28.981 22.771  1.00 11.33 ? 53  ASN H N   1 
ATOM   5954  C  CA  . ASN F  1 54  ? 58.487  -28.478 24.113  1.00 12.80 ? 53  ASN H CA  1 
ATOM   5955  C  C   . ASN F  1 54  ? 58.624  -29.510 25.164  1.00 12.29 ? 53  ASN H C   1 
ATOM   5956  O  O   . ASN F  1 54  ? 58.395  -29.298 26.350  1.00 12.13 ? 53  ASN H O   1 
ATOM   5957  C  CB  . ASN F  1 54  ? 57.194  -27.761 24.312  1.00 17.81 ? 53  ASN H CB  1 
ATOM   5958  C  CG  . ASN F  1 54  ? 57.589  -26.347 24.698  1.00 27.08 ? 53  ASN H CG  1 
ATOM   5959  O  OD1 . ASN F  1 54  ? 56.974  -25.734 25.584  1.00 30.34 ? 53  ASN H OD1 1 
ATOM   5960  N  ND2 . ASN F  1 54  ? 58.621  -25.748 24.068  1.00 29.90 ? 53  ASN H ND2 1 
ATOM   5961  N  N   . THR F  1 55  ? 59.078  -30.660 24.711  1.00 10.96 ? 54  THR H N   1 
ATOM   5962  C  CA  . THR F  1 55  ? 59.266  -31.752 25.623  1.00 10.53 ? 54  THR H CA  1 
ATOM   5963  C  C   . THR F  1 55  ? 60.177  -31.454 26.816  1.00 8.80  ? 54  THR H C   1 
ATOM   5964  O  O   . THR F  1 55  ? 60.106  -32.121 27.841  1.00 11.09 ? 54  THR H O   1 
ATOM   5965  C  CB  . THR F  1 55  ? 59.783  -32.911 24.786  1.00 8.83  ? 54  THR H CB  1 
ATOM   5966  O  OG1 . THR F  1 55  ? 60.976  -32.405 24.189  1.00 12.25 ? 54  THR H OG1 1 
ATOM   5967  C  CG2 . THR F  1 55  ? 58.803  -33.408 23.747  1.00 3.83  ? 54  THR H CG2 1 
ATOM   5968  N  N   . ALA F  1 56  ? 61.071  -30.489 26.714  1.00 7.03  ? 55  ALA H N   1 
ATOM   5969  C  CA  . ALA F  1 56  ? 61.993  -30.201 27.790  1.00 6.45  ? 55  ALA H CA  1 
ATOM   5970  C  C   . ALA F  1 56  ? 61.975  -28.687 27.995  1.00 8.03  ? 55  ALA H C   1 
ATOM   5971  O  O   . ALA F  1 56  ? 63.009  -28.005 28.056  1.00 10.47 ? 55  ALA H O   1 
ATOM   5972  C  CB  . ALA F  1 56  ? 63.373  -30.698 27.360  1.00 2.05  ? 55  ALA H CB  1 
ATOM   5973  N  N   . GLY F  1 57  ? 60.767  -28.132 28.034  1.00 7.32  ? 56  GLY H N   1 
ATOM   5974  C  CA  . GLY F  1 57  ? 60.575  -26.715 28.166  1.00 5.43  ? 56  GLY H CA  1 
ATOM   5975  C  C   . GLY F  1 57  ? 61.175  -26.047 26.957  1.00 7.49  ? 56  GLY H C   1 
ATOM   5976  O  O   . GLY F  1 57  ? 61.251  -26.600 25.842  1.00 11.80 ? 56  GLY H O   1 
ATOM   5977  N  N   . CYS F  1 58  ? 61.671  -24.850 27.192  1.00 6.39  ? 57  CYS H N   1 
ATOM   5978  C  CA  . CYS F  1 58  ? 62.332  -24.111 26.138  1.00 3.66  ? 57  CYS H CA  1 
ATOM   5979  C  C   . CYS F  1 58  ? 63.616  -24.696 25.604  1.00 3.54  ? 57  CYS H C   1 
ATOM   5980  O  O   . CYS F  1 58  ? 64.003  -24.331 24.510  1.00 5.45  ? 57  CYS H O   1 
ATOM   5981  C  CB  . CYS F  1 58  ? 62.605  -22.744 26.647  1.00 2.01  ? 57  CYS H CB  1 
ATOM   5982  S  SG  . CYS F  1 58  ? 61.024  -22.068 27.174  1.00 2.68  ? 57  CYS H SG  1 
ATOM   5983  N  N   . THR F  1 59  ? 64.273  -25.610 26.292  1.00 3.53  ? 58  THR H N   1 
ATOM   5984  C  CA  . THR F  1 59  ? 65.560  -26.162 25.929  1.00 4.97  ? 58  THR H CA  1 
ATOM   5985  C  C   . THR F  1 59  ? 65.576  -26.925 24.626  1.00 4.84  ? 58  THR H C   1 
ATOM   5986  O  O   . THR F  1 59  ? 66.503  -26.815 23.810  1.00 7.92  ? 58  THR H O   1 
ATOM   5987  C  CB  . THR F  1 59  ? 66.016  -27.060 27.094  1.00 6.86  ? 58  THR H CB  1 
ATOM   5988  O  OG1 . THR F  1 59  ? 65.741  -26.369 28.325  1.00 11.87 ? 58  THR H OG1 1 
ATOM   5989  C  CG2 . THR F  1 59  ? 67.492  -27.339 27.037  1.00 6.71  ? 58  THR H CG2 1 
ATOM   5990  N  N   . SER F  1 60  ? 64.524  -27.700 24.439  1.00 5.23  ? 59  SER H N   1 
ATOM   5991  C  CA  . SER F  1 60  ? 64.316  -28.491 23.216  1.00 6.14  ? 59  SER H CA  1 
ATOM   5992  C  C   . SER F  1 60  ? 63.908  -27.766 21.908  1.00 6.31  ? 59  SER H C   1 
ATOM   5993  O  O   . SER F  1 60  ? 63.830  -28.394 20.837  1.00 4.77  ? 59  SER H O   1 
ATOM   5994  C  CB  . SER F  1 60  ? 63.320  -29.537 23.569  1.00 4.02  ? 59  SER H CB  1 
ATOM   5995  O  OG  . SER F  1 60  ? 62.497  -29.071 24.643  1.00 7.84  ? 59  SER H OG  1 
ATOM   5996  N  N   . ALA F  1 61  ? 63.764  -26.427 22.030  1.00 3.03  ? 60  ALA H N   1 
ATOM   5997  C  CA  . ALA F  1 61  ? 63.453  -25.519 20.961  1.00 2.00  ? 60  ALA H CA  1 
ATOM   5998  C  C   . ALA F  1 61  ? 64.597  -25.389 19.948  1.00 4.17  ? 60  ALA H C   1 
ATOM   5999  O  O   . ALA F  1 61  ? 64.426  -24.989 18.777  1.00 3.23  ? 60  ALA H O   1 
ATOM   6000  C  CB  . ALA F  1 61  ? 63.150  -24.182 21.586  1.00 2.00  ? 60  ALA H CB  1 
ATOM   6001  N  N   . GLY F  1 62  ? 65.817  -25.652 20.451  1.00 3.56  ? 61  GLY H N   1 
ATOM   6002  C  CA  . GLY F  1 62  ? 67.015  -25.721 19.640  1.00 2.00  ? 61  GLY H CA  1 
ATOM   6003  C  C   . GLY F  1 62  ? 67.558  -24.365 19.262  1.00 3.15  ? 61  GLY H C   1 
ATOM   6004  O  O   . GLY F  1 62  ? 67.106  -23.360 19.821  1.00 3.04  ? 61  GLY H O   1 
ATOM   6005  N  N   . PRO F  1 63  ? 68.491  -24.247 18.312  1.00 2.85  ? 62  PRO H N   1 
ATOM   6006  C  CA  . PRO F  1 63  ? 69.110  -22.994 17.936  1.00 3.00  ? 62  PRO H CA  1 
ATOM   6007  C  C   . PRO F  1 63  ? 68.123  -22.066 17.208  1.00 2.71  ? 62  PRO H C   1 
ATOM   6008  O  O   . PRO F  1 63  ? 66.995  -22.459 16.887  1.00 2.87  ? 62  PRO H O   1 
ATOM   6009  C  CB  . PRO F  1 63  ? 70.289  -23.416 17.090  1.00 2.00  ? 62  PRO H CB  1 
ATOM   6010  C  CG  . PRO F  1 63  ? 69.699  -24.519 16.286  1.00 3.97  ? 62  PRO H CG  1 
ATOM   6011  C  CD  . PRO F  1 63  ? 68.801  -25.259 17.293  1.00 6.05  ? 62  PRO H CD  1 
ATOM   6012  N  N   . HIS F  1 64  ? 68.536  -20.846 16.882  1.00 2.00  ? 63  HIS H N   1 
ATOM   6013  C  CA  . HIS F  1 64  ? 67.660  -19.968 16.183  1.00 2.00  ? 63  HIS H CA  1 
ATOM   6014  C  C   . HIS F  1 64  ? 67.424  -20.562 14.808  1.00 2.00  ? 63  HIS H C   1 
ATOM   6015  O  O   . HIS F  1 64  ? 68.347  -21.022 14.151  1.00 2.00  ? 63  HIS H O   1 
ATOM   6016  C  CB  . HIS F  1 64  ? 68.268  -18.573 16.029  1.00 2.00  ? 63  HIS H CB  1 
ATOM   6017  C  CG  . HIS F  1 64  ? 68.422  -17.739 17.263  1.00 2.00  ? 63  HIS H CG  1 
ATOM   6018  N  ND1 . HIS F  1 64  ? 69.375  -16.855 17.503  1.00 4.61  ? 63  HIS H ND1 1 
ATOM   6019  C  CD2 . HIS F  1 64  ? 67.594  -17.808 18.342  1.00 3.09  ? 63  HIS H CD2 1 
ATOM   6020  C  CE1 . HIS F  1 64  ? 69.078  -16.440 18.735  1.00 5.80  ? 63  HIS H CE1 1 
ATOM   6021  N  NE2 . HIS F  1 64  ? 68.005  -16.988 19.277  1.00 4.35  ? 63  HIS H NE2 1 
ATOM   6022  N  N   . PHE F  1 65  ? 66.181  -20.519 14.358  1.00 2.00  ? 64  PHE H N   1 
ATOM   6023  C  CA  . PHE F  1 65  ? 65.770  -20.940 13.052  1.00 2.00  ? 64  PHE H CA  1 
ATOM   6024  C  C   . PHE F  1 65  ? 66.619  -20.204 12.026  1.00 2.30  ? 64  PHE H C   1 
ATOM   6025  O  O   . PHE F  1 65  ? 66.537  -18.988 11.828  1.00 3.73  ? 64  PHE H O   1 
ATOM   6026  C  CB  . PHE F  1 65  ? 64.314  -20.599 12.918  1.00 2.00  ? 64  PHE H CB  1 
ATOM   6027  C  CG  . PHE F  1 65  ? 63.688  -21.004 11.606  1.00 2.00  ? 64  PHE H CG  1 
ATOM   6028  C  CD1 . PHE F  1 65  ? 64.063  -22.163 10.970  1.00 2.00  ? 64  PHE H CD1 1 
ATOM   6029  C  CD2 . PHE F  1 65  ? 62.747  -20.144 11.069  1.00 2.00  ? 64  PHE H CD2 1 
ATOM   6030  C  CE1 . PHE F  1 65  ? 63.488  -22.435 9.768   1.00 2.00  ? 64  PHE H CE1 1 
ATOM   6031  C  CE2 . PHE F  1 65  ? 62.181  -20.435 9.859   1.00 2.00  ? 64  PHE H CE2 1 
ATOM   6032  C  CZ  . PHE F  1 65  ? 62.557  -21.585 9.220   1.00 2.00  ? 64  PHE H CZ  1 
ATOM   6033  N  N   . ASN F  1 66  ? 67.415  -20.997 11.343  1.00 2.00  ? 65  ASN H N   1 
ATOM   6034  C  CA  . ASN F  1 66  ? 68.393  -20.491 10.431  1.00 4.00  ? 65  ASN H CA  1 
ATOM   6035  C  C   . ASN F  1 66  ? 68.371  -21.281 9.140   1.00 6.73  ? 65  ASN H C   1 
ATOM   6036  O  O   . ASN F  1 66  ? 69.324  -21.984 8.816   1.00 10.49 ? 65  ASN H O   1 
ATOM   6037  C  CB  . ASN F  1 66  ? 69.745  -20.584 11.130  1.00 2.00  ? 65  ASN H CB  1 
ATOM   6038  C  CG  . ASN F  1 66  ? 70.867  -19.973 10.353  1.00 2.00  ? 65  ASN H CG  1 
ATOM   6039  O  OD1 . ASN F  1 66  ? 70.634  -19.285 9.357   1.00 5.68  ? 65  ASN H OD1 1 
ATOM   6040  N  ND2 . ASN F  1 66  ? 72.121  -20.205 10.718  1.00 2.00  ? 65  ASN H ND2 1 
ATOM   6041  N  N   . PRO F  1 67  ? 67.320  -21.254 8.333   1.00 7.75  ? 66  PRO H N   1 
ATOM   6042  C  CA  . PRO F  1 67  ? 67.288  -21.968 7.069   1.00 6.62  ? 66  PRO H CA  1 
ATOM   6043  C  C   . PRO F  1 67  ? 68.510  -21.776 6.179   1.00 7.85  ? 66  PRO H C   1 
ATOM   6044  O  O   . PRO F  1 67  ? 69.015  -22.721 5.610   1.00 9.41  ? 66  PRO H O   1 
ATOM   6045  C  CB  . PRO F  1 67  ? 66.057  -21.481 6.363   1.00 7.12  ? 66  PRO H CB  1 
ATOM   6046  C  CG  . PRO F  1 67  ? 65.279  -20.698 7.371   1.00 9.36  ? 66  PRO H CG  1 
ATOM   6047  C  CD  . PRO F  1 67  ? 66.307  -20.211 8.362   1.00 9.46  ? 66  PRO H CD  1 
ATOM   6048  N  N   . LEU F  1 68  ? 69.026  -20.558 6.065   1.00 9.42  ? 67  LEU H N   1 
ATOM   6049  C  CA  . LEU F  1 68  ? 70.064  -20.221 5.104   1.00 8.84  ? 67  LEU H CA  1 
ATOM   6050  C  C   . LEU F  1 68  ? 71.451  -20.191 5.701   1.00 9.80  ? 67  LEU H C   1 
ATOM   6051  O  O   . LEU F  1 68  ? 72.371  -19.678 5.065   1.00 12.59 ? 67  LEU H O   1 
ATOM   6052  C  CB  . LEU F  1 68  ? 69.762  -18.877 4.538   1.00 9.60  ? 67  LEU H CB  1 
ATOM   6053  C  CG  . LEU F  1 68  ? 68.361  -18.644 3.966   1.00 11.54 ? 67  LEU H CG  1 
ATOM   6054  C  CD1 . LEU F  1 68  ? 67.840  -17.304 4.414   1.00 13.62 ? 67  LEU H CD1 1 
ATOM   6055  C  CD2 . LEU F  1 68  ? 68.404  -18.660 2.465   1.00 12.95 ? 67  LEU H CD2 1 
ATOM   6056  N  N   . SER F  1 69  ? 71.648  -20.645 6.930   1.00 9.18  ? 68  SER H N   1 
ATOM   6057  C  CA  . SER F  1 69  ? 72.962  -20.723 7.554   1.00 7.77  ? 68  SER H CA  1 
ATOM   6058  C  C   . SER F  1 69  ? 73.759  -19.422 7.564   1.00 7.99  ? 68  SER H C   1 
ATOM   6059  O  O   . SER F  1 69  ? 74.980  -19.398 7.333   1.00 4.34  ? 68  SER H O   1 
ATOM   6060  C  CB  . SER F  1 69  ? 73.766  -21.816 6.866   1.00 6.06  ? 68  SER H CB  1 
ATOM   6061  O  OG  . SER F  1 69  ? 72.997  -22.922 6.411   1.00 9.66  ? 68  SER H OG  1 
ATOM   6062  N  N   . ARG F  1 70  ? 73.060  -18.326 7.898   1.00 9.85  ? 69  ARG H N   1 
ATOM   6063  C  CA  . ARG F  1 70  ? 73.733  -17.034 7.989   1.00 9.96  ? 69  ARG H CA  1 
ATOM   6064  C  C   . ARG F  1 70  ? 74.093  -16.911 9.453   1.00 9.08  ? 69  ARG H C   1 
ATOM   6065  O  O   . ARG F  1 70  ? 73.678  -17.737 10.266  1.00 12.63 ? 69  ARG H O   1 
ATOM   6066  C  CB  . ARG F  1 70  ? 72.842  -15.879 7.660   1.00 14.83 ? 69  ARG H CB  1 
ATOM   6067  C  CG  . ARG F  1 70  ? 71.858  -15.985 6.525   1.00 19.01 ? 69  ARG H CG  1 
ATOM   6068  C  CD  . ARG F  1 70  ? 72.177  -14.999 5.450   1.00 23.74 ? 69  ARG H CD  1 
ATOM   6069  N  NE  . ARG F  1 70  ? 72.906  -15.766 4.474   1.00 31.72 ? 69  ARG H NE  1 
ATOM   6070  C  CZ  . ARG F  1 70  ? 72.326  -16.208 3.347   1.00 36.19 ? 69  ARG H CZ  1 
ATOM   6071  N  NH1 . ARG F  1 70  ? 71.044  -15.919 3.090   1.00 37.33 ? 69  ARG H NH1 1 
ATOM   6072  N  NH2 . ARG F  1 70  ? 73.037  -16.974 2.492   1.00 37.90 ? 69  ARG H NH2 1 
ATOM   6073  N  N   . LYS F  1 71  ? 74.812  -15.903 9.896   1.00 9.05  ? 70  LYS H N   1 
ATOM   6074  C  CA  . LYS F  1 71  ? 75.206  -15.788 11.296  1.00 6.94  ? 70  LYS H CA  1 
ATOM   6075  C  C   . LYS F  1 71  ? 74.138  -14.903 11.925  1.00 5.84  ? 70  LYS H C   1 
ATOM   6076  O  O   . LYS F  1 71  ? 73.243  -14.414 11.211  1.00 5.72  ? 70  LYS H O   1 
ATOM   6077  C  CB  . LYS F  1 71  ? 76.594  -15.135 11.434  1.00 10.68 ? 70  LYS H CB  1 
ATOM   6078  C  CG  . LYS F  1 71  ? 77.860  -16.024 11.368  1.00 14.99 ? 70  LYS H CG  1 
ATOM   6079  C  CD  . LYS F  1 71  ? 78.113  -16.760 10.022  1.00 22.46 ? 70  LYS H CD  1 
ATOM   6080  C  CE  . LYS F  1 71  ? 79.012  -16.001 9.017   1.00 25.04 ? 70  LYS H CE  1 
ATOM   6081  N  NZ  . LYS F  1 71  ? 78.834  -16.449 7.635   1.00 24.94 ? 70  LYS H NZ  1 
ATOM   6082  N  N   . HIS F  1 72  ? 74.185  -14.734 13.252  1.00 2.71  ? 71  HIS H N   1 
ATOM   6083  C  CA  . HIS F  1 72  ? 73.198  -14.053 14.021  1.00 2.00  ? 71  HIS H CA  1 
ATOM   6084  C  C   . HIS F  1 72  ? 73.283  -12.576 13.787  1.00 2.00  ? 71  HIS H C   1 
ATOM   6085  O  O   . HIS F  1 72  ? 74.384  -12.051 13.715  1.00 3.76  ? 71  HIS H O   1 
ATOM   6086  C  CB  . HIS F  1 72  ? 73.460  -14.425 15.454  1.00 3.06  ? 71  HIS H CB  1 
ATOM   6087  C  CG  . HIS F  1 72  ? 72.445  -13.848 16.439  1.00 2.79  ? 71  HIS H CG  1 
ATOM   6088  N  ND1 . HIS F  1 72  ? 71.238  -14.275 16.670  1.00 2.00  ? 71  HIS H ND1 1 
ATOM   6089  C  CD2 . HIS F  1 72  ? 72.604  -12.697 17.154  1.00 3.34  ? 71  HIS H CD2 1 
ATOM   6090  C  CE1 . HIS F  1 72  ? 70.648  -13.449 17.462  1.00 2.00  ? 71  HIS H CE1 1 
ATOM   6091  N  NE2 . HIS F  1 72  ? 71.474  -12.491 17.751  1.00 2.00  ? 71  HIS H NE2 1 
ATOM   6092  N  N   . GLY F  1 73  ? 72.196  -11.835 13.648  1.00 2.92  ? 72  GLY H N   1 
ATOM   6093  C  CA  . GLY F  1 73  ? 72.268  -10.385 13.440  1.00 4.02  ? 72  GLY H CA  1 
ATOM   6094  C  C   . GLY F  1 73  ? 71.054  -9.701  14.012  1.00 2.07  ? 72  GLY H C   1 
ATOM   6095  O  O   . GLY F  1 73  ? 70.229  -10.316 14.684  1.00 3.70  ? 72  GLY H O   1 
ATOM   6096  N  N   . GLY F  1 74  ? 70.981  -8.404  13.898  1.00 2.00  ? 73  GLY H N   1 
ATOM   6097  C  CA  . GLY F  1 74  ? 69.773  -7.678  14.235  1.00 2.00  ? 73  GLY H CA  1 
ATOM   6098  C  C   . GLY F  1 74  ? 68.677  -7.979  13.213  1.00 2.63  ? 73  GLY H C   1 
ATOM   6099  O  O   . GLY F  1 74  ? 68.999  -8.476  12.131  1.00 2.00  ? 73  GLY H O   1 
ATOM   6100  N  N   . PRO F  1 75  ? 67.378  -7.700  13.452  1.00 3.72  ? 74  PRO H N   1 
ATOM   6101  C  CA  . PRO F  1 75  ? 66.314  -7.956  12.502  1.00 5.44  ? 74  PRO H CA  1 
ATOM   6102  C  C   . PRO F  1 75  ? 66.459  -7.200  11.212  1.00 6.89  ? 74  PRO H C   1 
ATOM   6103  O  O   . PRO F  1 75  ? 65.936  -7.621  10.180  1.00 8.80  ? 74  PRO H O   1 
ATOM   6104  C  CB  . PRO F  1 75  ? 65.032  -7.618  13.216  1.00 2.99  ? 74  PRO H CB  1 
ATOM   6105  C  CG  . PRO F  1 75  ? 65.481  -6.784  14.362  1.00 2.83  ? 74  PRO H CG  1 
ATOM   6106  C  CD  . PRO F  1 75  ? 66.778  -7.440  14.749  1.00 2.01  ? 74  PRO H CD  1 
ATOM   6107  N  N   . LYS F  1 76  ? 67.196  -6.084  11.298  1.00 8.90  ? 75  LYS H N   1 
ATOM   6108  C  CA  . LYS F  1 76  ? 67.449  -5.236  10.142  1.00 10.61 ? 75  LYS H CA  1 
ATOM   6109  C  C   . LYS F  1 76  ? 68.695  -5.678  9.351   1.00 8.69  ? 75  LYS H C   1 
ATOM   6110  O  O   . LYS F  1 76  ? 68.958  -5.153  8.276   1.00 11.67 ? 75  LYS H O   1 
ATOM   6111  C  CB  . LYS F  1 76  ? 67.614  -3.742  10.599  1.00 12.91 ? 75  LYS H CB  1 
ATOM   6112  C  CG  . LYS F  1 76  ? 66.444  -2.878  11.176  1.00 20.79 ? 75  LYS H CG  1 
ATOM   6113  C  CD  . LYS F  1 76  ? 66.833  -1.389  11.612  1.00 27.24 ? 75  LYS H CD  1 
ATOM   6114  C  CE  . LYS F  1 76  ? 65.639  -0.526  12.205  1.00 31.73 ? 75  LYS H CE  1 
ATOM   6115  N  NZ  . LYS F  1 76  ? 65.984  0.831   12.646  1.00 29.25 ? 75  LYS H NZ  1 
ATOM   6116  N  N   . ASP F  1 77  ? 69.537  -6.604  9.786   1.00 6.20  ? 76  ASP H N   1 
ATOM   6117  C  CA  . ASP F  1 77  ? 70.762  -6.947  9.079   1.00 4.22  ? 76  ASP H CA  1 
ATOM   6118  C  C   . ASP F  1 77  ? 70.541  -7.891  7.923   1.00 2.00  ? 76  ASP H C   1 
ATOM   6119  O  O   . ASP F  1 77  ? 69.541  -8.575  7.971   1.00 2.00  ? 76  ASP H O   1 
ATOM   6120  C  CB  . ASP F  1 77  ? 71.736  -7.584  10.073  1.00 7.41  ? 76  ASP H CB  1 
ATOM   6121  C  CG  . ASP F  1 77  ? 72.247  -6.539  11.018  1.00 6.73  ? 76  ASP H CG  1 
ATOM   6122  O  OD1 . ASP F  1 77  ? 72.778  -5.545  10.561  1.00 11.00 ? 76  ASP H OD1 1 
ATOM   6123  O  OD2 . ASP F  1 77  ? 72.108  -6.687  12.213  1.00 11.70 ? 76  ASP H OD2 1 
ATOM   6124  N  N   . GLU F  1 78  ? 71.369  -7.988  6.870   1.00 2.51  ? 77  GLU H N   1 
ATOM   6125  C  CA  . GLU F  1 78  ? 71.129  -8.970  5.831   1.00 4.55  ? 77  GLU H CA  1 
ATOM   6126  C  C   . GLU F  1 78  ? 71.656  -10.275 6.404   1.00 4.13  ? 77  GLU H C   1 
ATOM   6127  O  O   . GLU F  1 78  ? 71.081  -11.341 6.174   1.00 2.00  ? 77  GLU H O   1 
ATOM   6128  C  CB  . GLU F  1 78  ? 71.878  -8.644  4.553   1.00 10.22 ? 77  GLU H CB  1 
ATOM   6129  C  CG  . GLU F  1 78  ? 71.477  -9.548  3.355   1.00 25.82 ? 77  GLU H CG  1 
ATOM   6130  C  CD  . GLU F  1 78  ? 72.498  -10.594 2.797   1.00 34.67 ? 77  GLU H CD  1 
ATOM   6131  O  OE1 . GLU F  1 78  ? 73.059  -11.388 3.568   1.00 39.92 ? 77  GLU H OE1 1 
ATOM   6132  O  OE2 . GLU F  1 78  ? 72.724  -10.643 1.569   1.00 39.57 ? 77  GLU H OE2 1 
ATOM   6133  N  N   . GLU F  1 79  ? 72.750  -10.212 7.183   1.00 3.61  ? 78  GLU H N   1 
ATOM   6134  C  CA  . GLU F  1 79  ? 73.312  -11.409 7.767   1.00 4.12  ? 78  GLU H CA  1 
ATOM   6135  C  C   . GLU F  1 79  ? 72.615  -11.505 9.110   1.00 2.75  ? 78  GLU H C   1 
ATOM   6136  O  O   . GLU F  1 79  ? 72.906  -10.810 10.083  1.00 3.76  ? 78  GLU H O   1 
ATOM   6137  C  CB  . GLU F  1 79  ? 74.821  -11.287 7.942   1.00 3.41  ? 78  GLU H CB  1 
ATOM   6138  C  CG  . GLU F  1 79  ? 75.562  -12.551 8.389   1.00 10.96 ? 78  GLU H CG  1 
ATOM   6139  C  CD  . GLU F  1 79  ? 75.676  -13.755 7.432   1.00 16.78 ? 78  GLU H CD  1 
ATOM   6140  O  OE1 . GLU F  1 79  ? 75.272  -13.675 6.267   1.00 22.79 ? 78  GLU H OE1 1 
ATOM   6141  O  OE2 . GLU F  1 79  ? 76.201  -14.801 7.836   1.00 17.50 ? 78  GLU H OE2 1 
ATOM   6142  N  N   . ARG F  1 80  ? 71.520  -12.233 9.034   1.00 2.00  ? 79  ARG H N   1 
ATOM   6143  C  CA  . ARG F  1 80  ? 70.822  -12.610 10.218  1.00 2.00  ? 79  ARG H CA  1 
ATOM   6144  C  C   . ARG F  1 80  ? 70.239  -13.995 9.998   1.00 2.04  ? 79  ARG H C   1 
ATOM   6145  O  O   . ARG F  1 80  ? 70.327  -14.577 8.908   1.00 2.00  ? 79  ARG H O   1 
ATOM   6146  C  CB  . ARG F  1 80  ? 69.772  -11.557 10.503  1.00 2.00  ? 79  ARG H CB  1 
ATOM   6147  C  CG  . ARG F  1 80  ? 68.792  -11.165 9.465   1.00 2.00  ? 79  ARG H CG  1 
ATOM   6148  C  CD  . ARG F  1 80  ? 67.486  -11.703 9.938   1.00 2.00  ? 79  ARG H CD  1 
ATOM   6149  N  NE  . ARG F  1 80  ? 66.469  -10.724 9.802   1.00 2.00  ? 79  ARG H NE  1 
ATOM   6150  C  CZ  . ARG F  1 80  ? 65.208  -10.990 10.092  1.00 2.00  ? 79  ARG H CZ  1 
ATOM   6151  N  NH1 . ARG F  1 80  ? 64.718  -12.141 10.529  1.00 2.00  ? 79  ARG H NH1 1 
ATOM   6152  N  NH2 . ARG F  1 80  ? 64.377  -10.010 9.923   1.00 2.00  ? 79  ARG H NH2 1 
ATOM   6153  N  N   . HIS F  1 81  ? 69.660  -14.536 11.053  1.00 2.00  ? 80  HIS H N   1 
ATOM   6154  C  CA  . HIS F  1 81  ? 69.000  -15.812 10.975  1.00 4.69  ? 80  HIS H CA  1 
ATOM   6155  C  C   . HIS F  1 81  ? 67.538  -15.466 10.742  1.00 2.95  ? 80  HIS H C   1 
ATOM   6156  O  O   . HIS F  1 81  ? 67.103  -14.433 11.230  1.00 2.00  ? 80  HIS H O   1 
ATOM   6157  C  CB  . HIS F  1 81  ? 69.011  -16.591 12.262  1.00 5.42  ? 80  HIS H CB  1 
ATOM   6158  C  CG  . HIS F  1 81  ? 70.303  -16.910 12.976  1.00 5.42  ? 80  HIS H CG  1 
ATOM   6159  N  ND1 . HIS F  1 81  ? 70.452  -16.849 14.310  1.00 5.09  ? 80  HIS H ND1 1 
ATOM   6160  C  CD2 . HIS F  1 81  ? 71.432  -17.404 12.395  1.00 2.00  ? 80  HIS H CD2 1 
ATOM   6161  C  CE1 . HIS F  1 81  ? 71.653  -17.337 14.535  1.00 2.52  ? 80  HIS H CE1 1 
ATOM   6162  N  NE2 . HIS F  1 81  ? 72.223  -17.660 13.391  1.00 2.00  ? 80  HIS H NE2 1 
ATOM   6163  N  N   . VAL F  1 82  ? 66.707  -16.297 10.121  1.00 4.32  ? 81  VAL H N   1 
ATOM   6164  C  CA  . VAL F  1 82  ? 65.298  -15.942 9.926   1.00 3.67  ? 81  VAL H CA  1 
ATOM   6165  C  C   . VAL F  1 82  ? 64.578  -15.696 11.256  1.00 3.34  ? 81  VAL H C   1 
ATOM   6166  O  O   . VAL F  1 82  ? 63.749  -14.794 11.417  1.00 2.00  ? 81  VAL H O   1 
ATOM   6167  C  CB  . VAL F  1 82  ? 64.647  -17.067 9.125   1.00 2.00  ? 81  VAL H CB  1 
ATOM   6168  C  CG1 . VAL F  1 82  ? 63.166  -16.861 9.045   1.00 2.86  ? 81  VAL H CG1 1 
ATOM   6169  C  CG2 . VAL F  1 82  ? 65.180  -17.042 7.703   1.00 2.00  ? 81  VAL H CG2 1 
ATOM   6170  N  N   . GLY F  1 83  ? 64.976  -16.500 12.231  1.00 4.01  ? 82  GLY H N   1 
ATOM   6171  C  CA  . GLY F  1 83  ? 64.446  -16.411 13.580  1.00 3.05  ? 82  GLY H CA  1 
ATOM   6172  C  C   . GLY F  1 83  ? 64.907  -15.214 14.379  1.00 2.00  ? 82  GLY H C   1 
ATOM   6173  O  O   . GLY F  1 83  ? 64.587  -15.114 15.549  1.00 2.00  ? 82  GLY H O   1 
ATOM   6174  N  N   . ASP F  1 84  ? 65.610  -14.227 13.877  1.00 2.11  ? 83  ASP H N   1 
ATOM   6175  C  CA  . ASP F  1 84  ? 66.105  -13.127 14.701  1.00 2.00  ? 83  ASP H CA  1 
ATOM   6176  C  C   . ASP F  1 84  ? 65.169  -11.976 14.754  1.00 2.00  ? 83  ASP H C   1 
ATOM   6177  O  O   . ASP F  1 84  ? 65.258  -11.115 13.889  1.00 2.00  ? 83  ASP H O   1 
ATOM   6178  C  CB  . ASP F  1 84  ? 67.430  -12.604 14.195  1.00 2.00  ? 83  ASP H CB  1 
ATOM   6179  C  CG  . ASP F  1 84  ? 68.625  -13.531 14.351  1.00 2.73  ? 83  ASP H CG  1 
ATOM   6180  O  OD1 . ASP F  1 84  ? 68.559  -14.606 14.925  1.00 2.00  ? 83  ASP H OD1 1 
ATOM   6181  O  OD2 . ASP F  1 84  ? 69.661  -13.155 13.851  1.00 7.37  ? 83  ASP H OD2 1 
ATOM   6182  N  N   . LEU F  1 85  ? 64.304  -11.899 15.761  1.00 2.00  ? 84  LEU H N   1 
ATOM   6183  C  CA  . LEU F  1 85  ? 63.431  -10.748 15.817  1.00 2.22  ? 84  LEU H CA  1 
ATOM   6184  C  C   . LEU F  1 85  ? 63.890  -9.603  16.724  1.00 2.00  ? 84  LEU H C   1 
ATOM   6185  O  O   . LEU F  1 85  ? 63.194  -8.628  16.990  1.00 2.00  ? 84  LEU H O   1 
ATOM   6186  C  CB  . LEU F  1 85  ? 62.041  -11.248 16.176  1.00 2.00  ? 84  LEU H CB  1 
ATOM   6187  C  CG  . LEU F  1 85  ? 61.385  -12.201 15.167  1.00 2.00  ? 84  LEU H CG  1 
ATOM   6188  C  CD1 . LEU F  1 85  ? 60.105  -12.732 15.756  1.00 2.39  ? 84  LEU H CD1 1 
ATOM   6189  C  CD2 . LEU F  1 85  ? 61.094  -11.503 13.856  1.00 2.00  ? 84  LEU H CD2 1 
ATOM   6190  N  N   . GLY F  1 86  ? 65.160  -9.664  17.087  1.00 2.00  ? 85  GLY H N   1 
ATOM   6191  C  CA  . GLY F  1 86  ? 65.795  -8.626  17.861  1.00 2.04  ? 85  GLY H CA  1 
ATOM   6192  C  C   . GLY F  1 86  ? 65.371  -8.562  19.312  1.00 2.00  ? 85  GLY H C   1 
ATOM   6193  O  O   . GLY F  1 86  ? 65.415  -9.590  19.989  1.00 2.00  ? 85  GLY H O   1 
ATOM   6194  N  N   . ASN F  1 87  ? 64.992  -7.388  19.805  1.00 2.41  ? 86  ASN H N   1 
ATOM   6195  C  CA  . ASN F  1 87  ? 64.719  -7.214  21.228  1.00 2.11  ? 86  ASN H CA  1 
ATOM   6196  C  C   . ASN F  1 87  ? 63.355  -6.668  21.479  1.00 2.00  ? 86  ASN H C   1 
ATOM   6197  O  O   . ASN F  1 87  ? 62.913  -5.871  20.669  1.00 4.44  ? 86  ASN H O   1 
ATOM   6198  C  CB  . ASN F  1 87  ? 65.694  -6.241  21.885  1.00 2.00  ? 86  ASN H CB  1 
ATOM   6199  C  CG  . ASN F  1 87  ? 67.069  -6.790  22.171  1.00 2.00  ? 86  ASN H CG  1 
ATOM   6200  O  OD1 . ASN F  1 87  ? 67.201  -7.736  22.929  1.00 2.84  ? 86  ASN H OD1 1 
ATOM   6201  N  ND2 . ASN F  1 87  ? 68.174  -6.327  21.635  1.00 2.00  ? 86  ASN H ND2 1 
ATOM   6202  N  N   . VAL F  1 88  ? 62.674  -7.077  22.537  1.00 2.00  ? 87  VAL H N   1 
ATOM   6203  C  CA  . VAL F  1 88  ? 61.456  -6.466  23.019  1.00 2.00  ? 87  VAL H CA  1 
ATOM   6204  C  C   . VAL F  1 88  ? 61.871  -5.686  24.244  1.00 2.00  ? 87  VAL H C   1 
ATOM   6205  O  O   . VAL F  1 88  ? 62.944  -5.927  24.805  1.00 2.00  ? 87  VAL H O   1 
ATOM   6206  C  CB  . VAL F  1 88  ? 60.376  -7.486  23.453  1.00 2.54  ? 87  VAL H CB  1 
ATOM   6207  C  CG1 . VAL F  1 88  ? 59.736  -7.888  22.181  1.00 3.18  ? 87  VAL H CG1 1 
ATOM   6208  C  CG2 . VAL F  1 88  ? 60.881  -8.708  24.230  1.00 2.00  ? 87  VAL H CG2 1 
ATOM   6209  N  N   . THR F  1 89  ? 61.037  -4.794  24.737  1.00 2.00  ? 88  THR H N   1 
ATOM   6210  C  CA  . THR F  1 89  ? 61.386  -3.950  25.863  1.00 2.00  ? 88  THR H CA  1 
ATOM   6211  C  C   . THR F  1 89  ? 60.321  -4.124  26.938  1.00 4.71  ? 88  THR H C   1 
ATOM   6212  O  O   . THR F  1 89  ? 59.130  -3.948  26.622  1.00 5.81  ? 88  THR H O   1 
ATOM   6213  C  CB  . THR F  1 89  ? 61.418  -2.518  25.369  1.00 2.00  ? 88  THR H CB  1 
ATOM   6214  O  OG1 . THR F  1 89  ? 62.323  -2.557  24.286  1.00 2.00  ? 88  THR H OG1 1 
ATOM   6215  C  CG2 . THR F  1 89  ? 61.781  -1.486  26.417  1.00 2.00  ? 88  THR H CG2 1 
ATOM   6216  N  N   . ALA F  1 90  ? 60.676  -4.524  28.164  1.00 3.05  ? 89  ALA H N   1 
ATOM   6217  C  CA  . ALA F  1 90  ? 59.739  -4.593  29.247  1.00 2.00  ? 89  ALA H CA  1 
ATOM   6218  C  C   . ALA F  1 90  ? 59.841  -3.273  29.976  1.00 2.00  ? 89  ALA H C   1 
ATOM   6219  O  O   . ALA F  1 90  ? 60.942  -2.817  30.210  1.00 2.00  ? 89  ALA H O   1 
ATOM   6220  C  CB  . ALA F  1 90  ? 60.120  -5.665  30.172  1.00 2.00  ? 89  ALA H CB  1 
ATOM   6221  N  N   . ASP F  1 91  ? 58.760  -2.585  30.283  1.00 3.96  ? 90  ASP H N   1 
ATOM   6222  C  CA  . ASP F  1 91  ? 58.754  -1.324  31.024  1.00 7.63  ? 90  ASP H CA  1 
ATOM   6223  C  C   . ASP F  1 91  ? 58.874  -1.542  32.538  1.00 9.56  ? 90  ASP H C   1 
ATOM   6224  O  O   . ASP F  1 91  ? 58.865  -2.694  32.971  1.00 7.13  ? 90  ASP H O   1 
ATOM   6225  C  CB  . ASP F  1 91  ? 57.432  -0.562  30.726  1.00 9.13  ? 90  ASP H CB  1 
ATOM   6226  C  CG  . ASP F  1 91  ? 56.095  -1.148  31.229  1.00 12.73 ? 90  ASP H CG  1 
ATOM   6227  O  OD1 . ASP F  1 91  ? 56.043  -1.803  32.268  1.00 11.89 ? 90  ASP H OD1 1 
ATOM   6228  O  OD2 . ASP F  1 91  ? 55.064  -0.938  30.574  1.00 15.88 ? 90  ASP H OD2 1 
ATOM   6229  N  N   . LYS F  1 92  ? 58.818  -0.480  33.354  1.00 11.94 ? 91  LYS H N   1 
ATOM   6230  C  CA  . LYS F  1 92  ? 58.862  -0.525  34.819  1.00 16.33 ? 91  LYS H CA  1 
ATOM   6231  C  C   . LYS F  1 92  ? 58.048  -1.634  35.466  1.00 14.81 ? 91  LYS H C   1 
ATOM   6232  O  O   . LYS F  1 92  ? 58.543  -2.333  36.342  1.00 15.25 ? 91  LYS H O   1 
ATOM   6233  C  CB  . LYS F  1 92  ? 58.366  0.798   35.426  1.00 22.34 ? 91  LYS H CB  1 
ATOM   6234  C  CG  . LYS F  1 92  ? 59.246  2.033   35.185  1.00 29.63 ? 91  LYS H CG  1 
ATOM   6235  C  CD  . LYS F  1 92  ? 58.642  3.268   35.857  1.00 33.76 ? 91  LYS H CD  1 
ATOM   6236  C  CE  . LYS F  1 92  ? 59.458  4.534   35.571  1.00 37.63 ? 91  LYS H CE  1 
ATOM   6237  N  NZ  . LYS F  1 92  ? 58.757  5.711   36.075  1.00 40.61 ? 91  LYS H NZ  1 
ATOM   6238  N  N   . ASP F  1 93  ? 56.793  -1.786  35.050  1.00 14.37 ? 92  ASP H N   1 
ATOM   6239  C  CA  . ASP F  1 93  ? 55.908  -2.887  35.450  1.00 15.97 ? 92  ASP H CA  1 
ATOM   6240  C  C   . ASP F  1 93  ? 56.285  -4.321  34.988  1.00 14.04 ? 92  ASP H C   1 
ATOM   6241  O  O   . ASP F  1 93  ? 55.527  -5.261  35.233  1.00 14.25 ? 92  ASP H O   1 
ATOM   6242  C  CB  . ASP F  1 93  ? 54.473  -2.636  34.943  1.00 18.26 ? 92  ASP H CB  1 
ATOM   6243  C  CG  . ASP F  1 93  ? 53.671  -1.502  35.555  1.00 21.43 ? 92  ASP H CG  1 
ATOM   6244  O  OD1 . ASP F  1 93  ? 53.712  -1.324  36.774  1.00 22.52 ? 92  ASP H OD1 1 
ATOM   6245  O  OD2 . ASP F  1 93  ? 52.975  -0.818  34.798  1.00 25.24 ? 92  ASP H OD2 1 
ATOM   6246  N  N   . GLY F  1 94  ? 57.422  -4.555  34.323  1.00 13.73 ? 93  GLY H N   1 
ATOM   6247  C  CA  . GLY F  1 94  ? 57.810  -5.845  33.787  1.00 9.90  ? 93  GLY H CA  1 
ATOM   6248  C  C   . GLY F  1 94  ? 56.914  -6.237  32.628  1.00 9.54  ? 93  GLY H C   1 
ATOM   6249  O  O   . GLY F  1 94  ? 56.669  -7.426  32.455  1.00 11.31 ? 93  GLY H O   1 
ATOM   6250  N  N   . VAL F  1 95  ? 56.389  -5.303  31.835  1.00 7.71  ? 94  VAL H N   1 
ATOM   6251  C  CA  . VAL F  1 95  ? 55.504  -5.638  30.729  1.00 8.05  ? 94  VAL H CA  1 
ATOM   6252  C  C   . VAL F  1 95  ? 56.073  -5.244  29.366  1.00 10.09 ? 94  VAL H C   1 
ATOM   6253  O  O   . VAL F  1 95  ? 56.501  -4.083  29.161  1.00 12.93 ? 94  VAL H O   1 
ATOM   6254  C  CB  . VAL F  1 95  ? 54.134  -4.941  30.888  1.00 8.23  ? 94  VAL H CB  1 
ATOM   6255  C  CG1 . VAL F  1 95  ? 53.270  -5.204  29.676  1.00 2.00  ? 94  VAL H CG1 1 
ATOM   6256  C  CG2 . VAL F  1 95  ? 53.410  -5.507  32.124  1.00 6.80  ? 94  VAL H CG2 1 
ATOM   6257  N  N   . ALA F  1 96  ? 56.063  -6.156  28.399  1.00 6.98  ? 95  ALA H N   1 
ATOM   6258  C  CA  . ALA F  1 96  ? 56.563  -5.800  27.095  1.00 6.13  ? 95  ALA H CA  1 
ATOM   6259  C  C   . ALA F  1 96  ? 55.386  -5.713  26.140  1.00 4.12  ? 95  ALA H C   1 
ATOM   6260  O  O   . ALA F  1 96  ? 54.696  -6.707  25.984  1.00 2.07  ? 95  ALA H O   1 
ATOM   6261  C  CB  . ALA F  1 96  ? 57.563  -6.864  26.598  1.00 5.49  ? 95  ALA H CB  1 
ATOM   6262  N  N   . ASP F  1 97  ? 55.024  -4.591  25.538  1.00 4.57  ? 96  ASP H N   1 
ATOM   6263  C  CA  . ASP F  1 97  ? 53.988  -4.614  24.531  1.00 6.79  ? 96  ASP H CA  1 
ATOM   6264  C  C   . ASP F  1 97  ? 54.686  -4.774  23.201  1.00 6.71  ? 96  ASP H C   1 
ATOM   6265  O  O   . ASP F  1 97  ? 55.206  -3.807  22.652  1.00 10.66 ? 96  ASP H O   1 
ATOM   6266  C  CB  . ASP F  1 97  ? 53.201  -3.330  24.574  1.00 9.92  ? 96  ASP H CB  1 
ATOM   6267  C  CG  . ASP F  1 97  ? 52.117  -3.508  25.612  1.00 15.83 ? 96  ASP H CG  1 
ATOM   6268  O  OD1 . ASP F  1 97  ? 51.104  -4.146  25.265  1.00 18.64 ? 96  ASP H OD1 1 
ATOM   6269  O  OD2 . ASP F  1 97  ? 52.310  -3.037  26.749  1.00 17.35 ? 96  ASP H OD2 1 
ATOM   6270  N  N   . VAL F  1 98  ? 54.678  -5.960  22.641  1.00 4.41  ? 97  VAL H N   1 
ATOM   6271  C  CA  . VAL F  1 98  ? 55.451  -6.226  21.461  1.00 2.58  ? 97  VAL H CA  1 
ATOM   6272  C  C   . VAL F  1 98  ? 54.741  -5.631  20.263  1.00 3.20  ? 97  VAL H C   1 
ATOM   6273  O  O   . VAL F  1 98  ? 53.515  -5.682  20.241  1.00 6.45  ? 97  VAL H O   1 
ATOM   6274  C  CB  . VAL F  1 98  ? 55.576  -7.738  21.356  1.00 2.00  ? 97  VAL H CB  1 
ATOM   6275  C  CG1 . VAL F  1 98  ? 56.346  -8.130  20.111  1.00 2.00  ? 97  VAL H CG1 1 
ATOM   6276  C  CG2 . VAL F  1 98  ? 56.205  -8.232  22.641  1.00 2.00  ? 97  VAL H CG2 1 
ATOM   6277  N  N   . SER F  1 99  ? 55.433  -5.096  19.275  1.00 2.00  ? 98  SER H N   1 
ATOM   6278  C  CA  . SER F  1 99  ? 54.867  -4.655  18.006  1.00 3.97  ? 98  SER H CA  1 
ATOM   6279  C  C   . SER F  1 99  ? 56.110  -4.714  17.121  1.00 4.14  ? 98  SER H C   1 
ATOM   6280  O  O   . SER F  1 99  ? 57.096  -4.036  17.357  1.00 7.84  ? 98  SER H O   1 
ATOM   6281  C  CB  . SER F  1 99  ? 54.349  -3.204  18.029  1.00 6.67  ? 98  SER H CB  1 
ATOM   6282  O  OG  . SER F  1 99  ? 53.909  -2.660  16.759  1.00 12.56 ? 98  SER H OG  1 
ATOM   6283  N  N   . ILE F  1 100 ? 56.176  -5.563  16.125  1.00 5.07  ? 99  ILE H N   1 
ATOM   6284  C  CA  . ILE F  1 100 ? 57.332  -5.788  15.281  1.00 5.88  ? 99  ILE H CA  1 
ATOM   6285  C  C   . ILE F  1 100 ? 56.639  -6.061  13.961  1.00 5.83  ? 99  ILE H C   1 
ATOM   6286  O  O   . ILE F  1 100 ? 55.509  -6.546  13.916  1.00 7.22  ? 99  ILE H O   1 
ATOM   6287  C  CB  . ILE F  1 100 ? 58.149  -7.071  15.736  1.00 4.01  ? 99  ILE H CB  1 
ATOM   6288  C  CG1 . ILE F  1 100 ? 58.826  -6.861  17.064  1.00 2.00  ? 99  ILE H CG1 1 
ATOM   6289  C  CG2 . ILE F  1 100 ? 59.199  -7.399  14.710  1.00 2.10  ? 99  ILE H CG2 1 
ATOM   6290  C  CD1 . ILE F  1 100 ? 59.400  -8.146  17.609  1.00 2.65  ? 99  ILE H CD1 1 
ATOM   6291  N  N   . GLU F  1 101 ? 57.327  -5.732  12.891  1.00 7.73  ? 100 GLU H N   1 
ATOM   6292  C  CA  . GLU F  1 101 ? 56.915  -6.052  11.554  1.00 8.42  ? 100 GLU H CA  1 
ATOM   6293  C  C   . GLU F  1 101 ? 58.203  -6.586  10.931  1.00 6.96  ? 100 GLU H C   1 
ATOM   6294  O  O   . GLU F  1 101 ? 59.278  -6.017  11.129  1.00 6.70  ? 100 GLU H O   1 
ATOM   6295  C  CB  . GLU F  1 101 ? 56.473  -4.815  10.884  1.00 9.35  ? 100 GLU H CB  1 
ATOM   6296  C  CG  . GLU F  1 101 ? 55.823  -5.176  9.558   1.00 16.52 ? 100 GLU H CG  1 
ATOM   6297  C  CD  . GLU F  1 101 ? 55.699  -3.988  8.627   1.00 19.94 ? 100 GLU H CD  1 
ATOM   6298  O  OE1 . GLU F  1 101 ? 55.047  -3.007  9.028   1.00 21.35 ? 100 GLU H OE1 1 
ATOM   6299  O  OE2 . GLU F  1 101 ? 56.275  -4.061  7.525   1.00 22.08 ? 100 GLU H OE2 1 
ATOM   6300  N  N   . ASP F  1 102 ? 58.129  -7.681  10.207  1.00 5.59  ? 101 ASP H N   1 
ATOM   6301  C  CA  . ASP F  1 102 ? 59.307  -8.298  9.687   1.00 3.79  ? 101 ASP H CA  1 
ATOM   6302  C  C   . ASP F  1 102 ? 58.985  -9.003  8.409   1.00 4.42  ? 101 ASP H C   1 
ATOM   6303  O  O   . ASP F  1 102 ? 58.019  -9.750  8.350   1.00 3.96  ? 101 ASP H O   1 
ATOM   6304  C  CB  . ASP F  1 102 ? 59.818  -9.315  10.648  1.00 2.00  ? 101 ASP H CB  1 
ATOM   6305  C  CG  . ASP F  1 102 ? 61.228  -9.693  10.276  1.00 2.72  ? 101 ASP H CG  1 
ATOM   6306  O  OD1 . ASP F  1 102 ? 62.103  -8.872  10.490  1.00 7.67  ? 101 ASP H OD1 1 
ATOM   6307  O  OD2 . ASP F  1 102 ? 61.486  -10.781 9.773   1.00 6.15  ? 101 ASP H OD2 1 
ATOM   6308  N  N   . SER F  1 103 ? 59.797  -8.830  7.386   1.00 5.94  ? 102 SER H N   1 
ATOM   6309  C  CA  . SER F  1 103 ? 59.561  -9.539  6.144   1.00 4.84  ? 102 SER H CA  1 
ATOM   6310  C  C   . SER F  1 103 ? 60.547  -10.622 5.777   1.00 4.37  ? 102 SER H C   1 
ATOM   6311  O  O   . SER F  1 103 ? 60.674  -10.979 4.606   1.00 6.88  ? 102 SER H O   1 
ATOM   6312  C  CB  . SER F  1 103 ? 59.489  -8.520  5.061   1.00 2.00  ? 102 SER H CB  1 
ATOM   6313  O  OG  . SER F  1 103 ? 60.554  -7.646  5.316   1.00 6.24  ? 102 SER H OG  1 
ATOM   6314  N  N   . VAL F  1 104 ? 61.342  -11.081 6.727   1.00 3.29  ? 103 VAL H N   1 
ATOM   6315  C  CA  . VAL F  1 104 ? 62.171  -12.253 6.512   1.00 4.59  ? 103 VAL H CA  1 
ATOM   6316  C  C   . VAL F  1 104 ? 61.451  -13.482 7.060   1.00 5.74  ? 103 VAL H C   1 
ATOM   6317  O  O   . VAL F  1 104 ? 61.566  -14.546 6.473   1.00 9.51  ? 103 VAL H O   1 
ATOM   6318  C  CB  . VAL F  1 104 ? 63.516  -12.031 7.195   1.00 2.93  ? 103 VAL H CB  1 
ATOM   6319  C  CG1 . VAL F  1 104 ? 64.398  -13.269 7.172   1.00 2.00  ? 103 VAL H CG1 1 
ATOM   6320  C  CG2 . VAL F  1 104 ? 64.194  -10.894 6.455   1.00 2.00  ? 103 VAL H CG2 1 
ATOM   6321  N  N   . ILE F  1 105 ? 60.753  -13.430 8.194   1.00 6.79  ? 104 ILE H N   1 
ATOM   6322  C  CA  . ILE F  1 105 ? 59.955  -14.537 8.682   1.00 4.75  ? 104 ILE H CA  1 
ATOM   6323  C  C   . ILE F  1 105 ? 58.685  -14.565 7.860   1.00 4.97  ? 104 ILE H C   1 
ATOM   6324  O  O   . ILE F  1 105 ? 58.384  -13.597 7.150   1.00 7.45  ? 104 ILE H O   1 
ATOM   6325  C  CB  . ILE F  1 105 ? 59.524  -14.389 10.146  1.00 4.35  ? 104 ILE H CB  1 
ATOM   6326  C  CG1 . ILE F  1 105 ? 58.921  -13.046 10.422  1.00 2.00  ? 104 ILE H CG1 1 
ATOM   6327  C  CG2 . ILE F  1 105 ? 60.726  -14.753 10.985  1.00 2.57  ? 104 ILE H CG2 1 
ATOM   6328  C  CD1 . ILE F  1 105 ? 57.988  -13.123 11.641  1.00 2.00  ? 104 ILE H CD1 1 
ATOM   6329  N  N   . SER F  1 106 ? 57.909  -15.634 7.989   1.00 3.94  ? 105 SER H N   1 
ATOM   6330  C  CA  . SER F  1 106 ? 56.699  -15.790 7.226   1.00 3.54  ? 105 SER H CA  1 
ATOM   6331  C  C   . SER F  1 106 ? 55.886  -16.891 7.873   1.00 2.32  ? 105 SER H C   1 
ATOM   6332  O  O   . SER F  1 106 ? 56.367  -17.741 8.637   1.00 2.00  ? 105 SER H O   1 
ATOM   6333  C  CB  . SER F  1 106 ? 57.093  -16.148 5.753   1.00 2.85  ? 105 SER H CB  1 
ATOM   6334  O  OG  . SER F  1 106 ? 55.985  -16.395 4.864   1.00 2.00  ? 105 SER H OG  1 
ATOM   6335  N  N   . LEU F  1 107 ? 54.622  -16.900 7.504   1.00 2.75  ? 106 LEU H N   1 
ATOM   6336  C  CA  . LEU F  1 107 ? 53.732  -17.957 7.961   1.00 2.51  ? 106 LEU H CA  1 
ATOM   6337  C  C   . LEU F  1 107 ? 53.582  -18.994 6.867   1.00 2.35  ? 106 LEU H C   1 
ATOM   6338  O  O   . LEU F  1 107 ? 52.802  -19.932 7.000   1.00 2.00  ? 106 LEU H O   1 
ATOM   6339  C  CB  . LEU F  1 107 ? 52.400  -17.348 8.320   1.00 2.00  ? 106 LEU H CB  1 
ATOM   6340  C  CG  . LEU F  1 107 ? 52.377  -16.252 9.377   1.00 2.00  ? 106 LEU H CG  1 
ATOM   6341  C  CD1 . LEU F  1 107 ? 51.014  -15.656 9.505   1.00 2.00  ? 106 LEU H CD1 1 
ATOM   6342  C  CD2 . LEU F  1 107 ? 52.624  -16.837 10.712  1.00 2.00  ? 106 LEU H CD2 1 
ATOM   6343  N  N   . SER F  1 108 ? 54.372  -18.852 5.790   1.00 4.32  ? 107 SER H N   1 
ATOM   6344  C  CA  . SER F  1 108 ? 54.338  -19.747 4.645   1.00 6.02  ? 107 SER H CA  1 
ATOM   6345  C  C   . SER F  1 108 ? 55.658  -19.999 3.942   1.00 4.00  ? 107 SER H C   1 
ATOM   6346  O  O   . SER F  1 108 ? 56.542  -19.147 3.892   1.00 4.72  ? 107 SER H O   1 
ATOM   6347  C  CB  . SER F  1 108 ? 53.378  -19.220 3.591   1.00 6.39  ? 107 SER H CB  1 
ATOM   6348  O  OG  . SER F  1 108 ? 52.183  -19.990 3.555   1.00 12.76 ? 107 SER H OG  1 
ATOM   6349  N  N   . GLY F  1 109 ? 55.807  -21.205 3.409   1.00 2.00  ? 108 GLY H N   1 
ATOM   6350  C  CA  . GLY F  1 109 ? 56.951  -21.530 2.590   1.00 3.76  ? 108 GLY H CA  1 
ATOM   6351  C  C   . GLY F  1 109 ? 58.192  -21.898 3.359   1.00 5.82  ? 108 GLY H C   1 
ATOM   6352  O  O   . GLY F  1 109 ? 58.096  -22.409 4.456   1.00 10.31 ? 108 GLY H O   1 
ATOM   6353  N  N   . ASP F  1 110 ? 59.389  -21.649 2.841   1.00 7.77  ? 109 ASP H N   1 
ATOM   6354  C  CA  . ASP F  1 110 ? 60.652  -22.018 3.459   1.00 7.25  ? 109 ASP H CA  1 
ATOM   6355  C  C   . ASP F  1 110 ? 60.943  -21.393 4.792   1.00 7.10  ? 109 ASP H C   1 
ATOM   6356  O  O   . ASP F  1 110 ? 61.727  -21.901 5.583   1.00 9.57  ? 109 ASP H O   1 
ATOM   6357  C  CB  . ASP F  1 110 ? 61.842  -21.639 2.586   1.00 10.73 ? 109 ASP H CB  1 
ATOM   6358  C  CG  . ASP F  1 110 ? 62.204  -22.470 1.370   1.00 13.48 ? 109 ASP H CG  1 
ATOM   6359  O  OD1 . ASP F  1 110 ? 61.816  -23.643 1.318   1.00 11.96 ? 109 ASP H OD1 1 
ATOM   6360  O  OD2 . ASP F  1 110 ? 62.911  -21.917 0.506   1.00 17.22 ? 109 ASP H OD2 1 
ATOM   6361  N  N   . HIS F  1 111 ? 60.387  -20.207 4.971   1.00 7.32  ? 110 HIS H N   1 
ATOM   6362  C  CA  . HIS F  1 111 ? 60.685  -19.360 6.099   1.00 5.01  ? 110 HIS H CA  1 
ATOM   6363  C  C   . HIS F  1 111 ? 59.514  -19.441 7.012   1.00 4.67  ? 110 HIS H C   1 
ATOM   6364  O  O   . HIS F  1 111 ? 59.177  -18.422 7.626   1.00 5.72  ? 110 HIS H O   1 
ATOM   6365  C  CB  . HIS F  1 111 ? 60.809  -17.944 5.666   1.00 5.43  ? 110 HIS H CB  1 
ATOM   6366  C  CG  . HIS F  1 111 ? 62.062  -17.640 4.904   1.00 10.08 ? 110 HIS H CG  1 
ATOM   6367  N  ND1 . HIS F  1 111 ? 62.495  -16.402 4.667   1.00 11.58 ? 110 HIS H ND1 1 
ATOM   6368  C  CD2 . HIS F  1 111 ? 62.916  -18.561 4.329   1.00 8.75  ? 110 HIS H CD2 1 
ATOM   6369  C  CE1 . HIS F  1 111 ? 63.581  -16.531 3.958   1.00 13.13 ? 110 HIS H CE1 1 
ATOM   6370  N  NE2 . HIS F  1 111 ? 63.818  -17.828 3.761   1.00 11.81 ? 110 HIS H NE2 1 
ATOM   6371  N  N   . SER F  1 112 ? 58.824  -20.570 7.029   1.00 2.05  ? 111 SER H N   1 
ATOM   6372  C  CA  . SER F  1 112 ? 57.658  -20.553 7.840   1.00 3.25  ? 111 SER H CA  1 
ATOM   6373  C  C   . SER F  1 112 ? 58.078  -20.756 9.294   1.00 2.00  ? 111 SER H C   1 
ATOM   6374  O  O   . SER F  1 112 ? 59.095  -21.325 9.656   1.00 2.00  ? 111 SER H O   1 
ATOM   6375  C  CB  . SER F  1 112 ? 56.714  -21.600 7.357   1.00 2.00  ? 111 SER H CB  1 
ATOM   6376  O  OG  . SER F  1 112 ? 55.469  -21.282 7.962   1.00 2.00  ? 111 SER H OG  1 
ATOM   6377  N  N   . ILE F  1 113 ? 57.363  -20.073 10.134  1.00 2.06  ? 112 ILE H N   1 
ATOM   6378  C  CA  . ILE F  1 113 ? 57.668  -20.144 11.543  1.00 3.84  ? 112 ILE H CA  1 
ATOM   6379  C  C   . ILE F  1 113 ? 56.600  -20.960 12.266  1.00 2.58  ? 112 ILE H C   1 
ATOM   6380  O  O   . ILE F  1 113 ? 56.683  -21.164 13.486  1.00 2.66  ? 112 ILE H O   1 
ATOM   6381  C  CB  . ILE F  1 113 ? 57.745  -18.723 12.138  1.00 2.00  ? 112 ILE H CB  1 
ATOM   6382  C  CG1 . ILE F  1 113 ? 56.384  -18.036 12.049  1.00 2.00  ? 112 ILE H CG1 1 
ATOM   6383  C  CG2 . ILE F  1 113 ? 58.957  -18.047 11.488  1.00 2.00  ? 112 ILE H CG2 1 
ATOM   6384  C  CD1 . ILE F  1 113 ? 56.359  -16.724 12.828  1.00 4.18  ? 112 ILE H CD1 1 
ATOM   6385  N  N   . ILE F  1 114 ? 55.569  -21.369 11.523  1.00 2.00  ? 113 ILE H N   1 
ATOM   6386  C  CA  . ILE F  1 114 ? 54.487  -22.169 12.100  1.00 4.10  ? 113 ILE H CA  1 
ATOM   6387  C  C   . ILE F  1 114 ? 55.024  -23.526 12.595  1.00 2.00  ? 113 ILE H C   1 
ATOM   6388  O  O   . ILE F  1 114 ? 55.631  -24.256 11.817  1.00 2.00  ? 113 ILE H O   1 
ATOM   6389  C  CB  . ILE F  1 114 ? 53.399  -22.331 10.999  1.00 2.00  ? 113 ILE H CB  1 
ATOM   6390  C  CG1 . ILE F  1 114 ? 52.932  -20.962 10.639  1.00 2.00  ? 113 ILE H CG1 1 
ATOM   6391  C  CG2 . ILE F  1 114 ? 52.326  -23.296 11.432  1.00 2.00  ? 113 ILE H CG2 1 
ATOM   6392  C  CD1 . ILE F  1 114 ? 51.462  -20.800 10.351  1.00 2.62  ? 113 ILE H CD1 1 
ATOM   6393  N  N   . GLY F  1 115 ? 54.881  -23.874 13.853  1.00 2.00  ? 114 GLY H N   1 
ATOM   6394  C  CA  . GLY F  1 115 ? 55.359  -25.156 14.332  1.00 2.00  ? 114 GLY H CA  1 
ATOM   6395  C  C   . GLY F  1 115 ? 56.748  -25.071 14.950  1.00 2.82  ? 114 GLY H C   1 
ATOM   6396  O  O   . GLY F  1 115 ? 57.316  -26.081 15.369  1.00 2.00  ? 114 GLY H O   1 
ATOM   6397  N  N   . ARG F  1 116 ? 57.289  -23.857 15.040  1.00 2.02  ? 115 ARG H N   1 
ATOM   6398  C  CA  . ARG F  1 116 ? 58.583  -23.561 15.631  1.00 2.00  ? 115 ARG H CA  1 
ATOM   6399  C  C   . ARG F  1 116 ? 58.350  -22.799 16.921  1.00 2.00  ? 115 ARG H C   1 
ATOM   6400  O  O   . ARG F  1 116 ? 57.227  -22.425 17.234  1.00 3.76  ? 115 ARG H O   1 
ATOM   6401  C  CB  . ARG F  1 116 ? 59.396  -22.738 14.638  1.00 2.00  ? 115 ARG H CB  1 
ATOM   6402  C  CG  . ARG F  1 116 ? 59.462  -23.537 13.345  1.00 2.25  ? 115 ARG H CG  1 
ATOM   6403  C  CD  . ARG F  1 116 ? 60.654  -23.167 12.544  1.00 2.00  ? 115 ARG H CD  1 
ATOM   6404  N  NE  . ARG F  1 116 ? 60.550  -23.624 11.187  1.00 2.00  ? 115 ARG H NE  1 
ATOM   6405  C  CZ  . ARG F  1 116 ? 61.203  -24.690 10.797  1.00 6.22  ? 115 ARG H CZ  1 
ATOM   6406  N  NH1 . ARG F  1 116 ? 61.929  -25.409 11.657  1.00 10.38 ? 115 ARG H NH1 1 
ATOM   6407  N  NH2 . ARG F  1 116 ? 61.106  -25.088 9.525   1.00 11.14 ? 115 ARG H NH2 1 
ATOM   6408  N  N   . THR F  1 117 ? 59.337  -22.522 17.732  1.00 2.86  ? 116 THR H N   1 
ATOM   6409  C  CA  . THR F  1 117 ? 59.138  -21.919 19.027  1.00 2.55  ? 116 THR H CA  1 
ATOM   6410  C  C   . THR F  1 117 ? 59.433  -20.437 19.098  1.00 3.61  ? 116 THR H C   1 
ATOM   6411  O  O   . THR F  1 117 ? 60.505  -20.046 18.630  1.00 4.51  ? 116 THR H O   1 
ATOM   6412  C  CB  . THR F  1 117 ? 60.023  -22.716 19.952  1.00 3.40  ? 116 THR H CB  1 
ATOM   6413  O  OG1 . THR F  1 117 ? 59.611  -24.076 19.907  1.00 2.00  ? 116 THR H OG1 1 
ATOM   6414  C  CG2 . THR F  1 117 ? 59.935  -22.181 21.349  1.00 4.19  ? 116 THR H CG2 1 
ATOM   6415  N  N   . LEU F  1 118 ? 58.600  -19.555 19.679  1.00 4.91  ? 117 LEU H N   1 
ATOM   6416  C  CA  . LEU F  1 118 ? 58.959  -18.154 19.905  1.00 2.00  ? 117 LEU H CA  1 
ATOM   6417  C  C   . LEU F  1 118 ? 59.555  -18.123 21.286  1.00 2.31  ? 117 LEU H C   1 
ATOM   6418  O  O   . LEU F  1 118 ? 59.003  -18.710 22.224  1.00 3.12  ? 117 LEU H O   1 
ATOM   6419  C  CB  . LEU F  1 118 ? 57.771  -17.321 19.911  1.00 2.00  ? 117 LEU H CB  1 
ATOM   6420  C  CG  . LEU F  1 118 ? 58.089  -15.880 19.967  1.00 2.00  ? 117 LEU H CG  1 
ATOM   6421  C  CD1 . LEU F  1 118 ? 58.980  -15.417 18.822  1.00 2.00  ? 117 LEU H CD1 1 
ATOM   6422  C  CD2 . LEU F  1 118 ? 56.746  -15.220 20.043  1.00 2.00  ? 117 LEU H CD2 1 
ATOM   6423  N  N   . VAL F  1 119 ? 60.694  -17.515 21.465  1.00 2.85  ? 118 VAL H N   1 
ATOM   6424  C  CA  . VAL F  1 119 ? 61.366  -17.571 22.742  1.00 3.06  ? 118 VAL H CA  1 
ATOM   6425  C  C   . VAL F  1 119 ? 61.667  -16.153 23.183  1.00 2.85  ? 118 VAL H C   1 
ATOM   6426  O  O   . VAL F  1 119 ? 62.188  -15.394 22.355  1.00 2.00  ? 118 VAL H O   1 
ATOM   6427  C  CB  . VAL F  1 119 ? 62.696  -18.356 22.648  1.00 2.00  ? 118 VAL H CB  1 
ATOM   6428  C  CG1 . VAL F  1 119 ? 63.331  -18.302 24.012  1.00 2.00  ? 118 VAL H CG1 1 
ATOM   6429  C  CG2 . VAL F  1 119 ? 62.530  -19.838 22.416  1.00 2.00  ? 118 VAL H CG2 1 
ATOM   6430  N  N   . VAL F  1 120 ? 61.368  -15.790 24.439  1.00 2.40  ? 119 VAL H N   1 
ATOM   6431  C  CA  . VAL F  1 120 ? 61.812  -14.515 24.958  1.00 4.17  ? 119 VAL H CA  1 
ATOM   6432  C  C   . VAL F  1 120 ? 62.912  -14.828 25.956  1.00 3.91  ? 119 VAL H C   1 
ATOM   6433  O  O   . VAL F  1 120 ? 62.729  -15.688 26.829  1.00 3.65  ? 119 VAL H O   1 
ATOM   6434  C  CB  . VAL F  1 120 ? 60.646  -13.739 25.612  1.00 6.71  ? 119 VAL H CB  1 
ATOM   6435  C  CG1 . VAL F  1 120 ? 59.997  -14.443 26.778  1.00 10.01 ? 119 VAL H CG1 1 
ATOM   6436  C  CG2 . VAL F  1 120 ? 61.245  -12.442 26.118  1.00 9.78  ? 119 VAL H CG2 1 
ATOM   6437  N  N   . HIS F  1 121 ? 64.075  -14.167 25.816  1.00 3.14  ? 120 HIS H N   1 
ATOM   6438  C  CA  . HIS F  1 121 ? 65.266  -14.446 26.582  1.00 2.00  ? 120 HIS H CA  1 
ATOM   6439  C  C   . HIS F  1 121 ? 65.482  -13.531 27.777  1.00 4.18  ? 120 HIS H C   1 
ATOM   6440  O  O   . HIS F  1 121 ? 64.945  -12.412 27.927  1.00 2.92  ? 120 HIS H O   1 
ATOM   6441  C  CB  . HIS F  1 121 ? 66.462  -14.323 25.728  1.00 2.00  ? 120 HIS H CB  1 
ATOM   6442  C  CG  . HIS F  1 121 ? 66.654  -15.480 24.807  1.00 2.00  ? 120 HIS H CG  1 
ATOM   6443  N  ND1 . HIS F  1 121 ? 67.317  -16.611 25.017  1.00 2.00  ? 120 HIS H ND1 1 
ATOM   6444  C  CD2 . HIS F  1 121 ? 66.127  -15.508 23.548  1.00 2.00  ? 120 HIS H CD2 1 
ATOM   6445  C  CE1 . HIS F  1 121 ? 67.193  -17.320 23.914  1.00 2.00  ? 120 HIS H CE1 1 
ATOM   6446  N  NE2 . HIS F  1 121 ? 66.473  -16.660 23.021  1.00 4.97  ? 120 HIS H NE2 1 
ATOM   6447  N  N   . GLU F  1 122 ? 66.356  -14.047 28.631  1.00 2.36  ? 121 GLU H N   1 
ATOM   6448  C  CA  . GLU F  1 122 ? 66.748  -13.409 29.863  1.00 2.00  ? 121 GLU H CA  1 
ATOM   6449  C  C   . GLU F  1 122 ? 67.388  -12.058 29.711  1.00 2.00  ? 121 GLU H C   1 
ATOM   6450  O  O   . GLU F  1 122 ? 67.007  -11.143 30.420  1.00 3.14  ? 121 GLU H O   1 
ATOM   6451  C  CB  . GLU F  1 122 ? 67.675  -14.287 30.526  1.00 2.00  ? 121 GLU H CB  1 
ATOM   6452  C  CG  . GLU F  1 122 ? 68.009  -13.778 31.874  1.00 6.96  ? 121 GLU H CG  1 
ATOM   6453  C  CD  . GLU F  1 122 ? 69.219  -14.474 32.469  1.00 10.85 ? 121 GLU H CD  1 
ATOM   6454  O  OE1 . GLU F  1 122 ? 70.100  -14.963 31.728  1.00 11.29 ? 121 GLU H OE1 1 
ATOM   6455  O  OE2 . GLU F  1 122 ? 69.244  -14.512 33.702  1.00 13.55 ? 121 GLU H OE2 1 
ATOM   6456  N  N   . LYS F  1 123 ? 68.313  -11.940 28.780  1.00 2.00  ? 122 LYS H N   1 
ATOM   6457  C  CA  . LYS F  1 123 ? 69.108  -10.764 28.544  1.00 3.35  ? 122 LYS H CA  1 
ATOM   6458  C  C   . LYS F  1 123 ? 68.841  -10.094 27.221  1.00 2.65  ? 122 LYS H C   1 
ATOM   6459  O  O   . LYS F  1 123 ? 68.120  -10.638 26.397  1.00 5.70  ? 122 LYS H O   1 
ATOM   6460  C  CB  . LYS F  1 123 ? 70.555  -11.128 28.561  1.00 6.42  ? 122 LYS H CB  1 
ATOM   6461  C  CG  . LYS F  1 123 ? 70.963  -11.632 29.892  1.00 7.72  ? 122 LYS H CG  1 
ATOM   6462  C  CD  . LYS F  1 123 ? 72.446  -11.806 29.920  1.00 13.97 ? 122 LYS H CD  1 
ATOM   6463  C  CE  . LYS F  1 123 ? 72.849  -11.409 31.341  1.00 21.91 ? 122 LYS H CE  1 
ATOM   6464  N  NZ  . LYS F  1 123 ? 72.238  -10.151 31.791  1.00 24.45 ? 122 LYS H NZ  1 
ATOM   6465  N  N   . ALA F  1 124 ? 69.538  -9.000  26.958  1.00 2.00  ? 123 ALA H N   1 
ATOM   6466  C  CA  . ALA F  1 124 ? 69.448  -8.267  25.709  1.00 2.00  ? 123 ALA H CA  1 
ATOM   6467  C  C   . ALA F  1 124 ? 70.247  -8.916  24.627  1.00 2.00  ? 123 ALA H C   1 
ATOM   6468  O  O   . ALA F  1 124 ? 71.383  -9.314  24.823  1.00 2.00  ? 123 ALA H O   1 
ATOM   6469  C  CB  . ALA F  1 124 ? 70.021  -6.873  25.759  1.00 2.00  ? 123 ALA H CB  1 
ATOM   6470  N  N   . ASP F  1 125 ? 69.683  -8.975  23.447  1.00 2.00  ? 124 ASP H N   1 
ATOM   6471  C  CA  . ASP F  1 125 ? 70.371  -9.489  22.285  1.00 3.05  ? 124 ASP H CA  1 
ATOM   6472  C  C   . ASP F  1 125 ? 71.411  -8.458  21.899  1.00 3.32  ? 124 ASP H C   1 
ATOM   6473  O  O   . ASP F  1 125 ? 71.044  -7.294  21.704  1.00 5.98  ? 124 ASP H O   1 
ATOM   6474  C  CB  . ASP F  1 125 ? 69.333  -9.668  21.189  1.00 3.64  ? 124 ASP H CB  1 
ATOM   6475  C  CG  . ASP F  1 125 ? 69.714  -10.499 19.982  1.00 4.98  ? 124 ASP H CG  1 
ATOM   6476  O  OD1 . ASP F  1 125 ? 70.887  -10.628 19.711  1.00 7.71  ? 124 ASP H OD1 1 
ATOM   6477  O  OD2 . ASP F  1 125 ? 68.840  -11.035 19.307  1.00 4.21  ? 124 ASP H OD2 1 
ATOM   6478  N  N   . ASP F  1 126 ? 72.690  -8.743  21.779  1.00 2.78  ? 125 ASP H N   1 
ATOM   6479  C  CA  . ASP F  1 126 ? 73.568  -7.711  21.273  1.00 3.69  ? 125 ASP H CA  1 
ATOM   6480  C  C   . ASP F  1 126 ? 73.584  -7.790  19.756  1.00 5.59  ? 125 ASP H C   1 
ATOM   6481  O  O   . ASP F  1 126 ? 74.642  -7.610  19.165  1.00 8.11  ? 125 ASP H O   1 
ATOM   6482  C  CB  . ASP F  1 126 ? 74.999  -7.873  21.816  1.00 4.25  ? 125 ASP H CB  1 
ATOM   6483  C  CG  . ASP F  1 126 ? 75.807  -9.145  21.519  1.00 9.41  ? 125 ASP H CG  1 
ATOM   6484  O  OD1 . ASP F  1 126 ? 75.500  -9.826  20.526  1.00 2.00  ? 125 ASP H OD1 1 
ATOM   6485  O  OD2 . ASP F  1 126 ? 76.743  -9.419  22.317  1.00 12.16 ? 125 ASP H OD2 1 
ATOM   6486  N  N   . LEU F  1 127 ? 72.515  -8.186  19.065  1.00 3.01  ? 126 LEU H N   1 
ATOM   6487  C  CA  . LEU F  1 127 ? 72.439  -8.232  17.623  1.00 2.00  ? 126 LEU H CA  1 
ATOM   6488  C  C   . LEU F  1 127 ? 73.670  -8.672  16.794  1.00 2.00  ? 126 LEU H C   1 
ATOM   6489  O  O   . LEU F  1 127 ? 73.729  -8.434  15.596  1.00 3.25  ? 126 LEU H O   1 
ATOM   6490  C  CB  . LEU F  1 127 ? 71.908  -6.837  17.223  1.00 2.00  ? 126 LEU H CB  1 
ATOM   6491  C  CG  . LEU F  1 127 ? 70.688  -6.217  18.007  1.00 2.00  ? 126 LEU H CG  1 
ATOM   6492  C  CD1 . LEU F  1 127 ? 70.532  -4.789  17.644  1.00 2.00  ? 126 LEU H CD1 1 
ATOM   6493  C  CD2 . LEU F  1 127 ? 69.432  -7.011  17.772  1.00 2.00  ? 126 LEU H CD2 1 
ATOM   6494  N  N   . GLY F  1 128 ? 74.649  -9.374  17.349  1.00 2.00  ? 127 GLY H N   1 
ATOM   6495  C  CA  . GLY F  1 128 ? 75.755  -9.937  16.612  1.00 2.00  ? 127 GLY H CA  1 
ATOM   6496  C  C   . GLY F  1 128 ? 76.992  -9.090  16.700  1.00 2.00  ? 127 GLY H C   1 
ATOM   6497  O  O   . GLY F  1 128 ? 78.014  -9.339  16.078  1.00 2.00  ? 127 GLY H O   1 
ATOM   6498  N  N   . LYS F  1 129 ? 76.989  -8.104  17.569  1.00 2.08  ? 128 LYS H N   1 
ATOM   6499  C  CA  . LYS F  1 129 ? 78.024  -7.123  17.579  1.00 2.00  ? 128 LYS H CA  1 
ATOM   6500  C  C   . LYS F  1 129 ? 78.859  -7.199  18.816  1.00 3.28  ? 128 LYS H C   1 
ATOM   6501  O  O   . LYS F  1 129 ? 79.461  -6.167  19.125  1.00 2.90  ? 128 LYS H O   1 
ATOM   6502  C  CB  . LYS F  1 129 ? 77.374  -5.749  17.455  1.00 3.95  ? 128 LYS H CB  1 
ATOM   6503  C  CG  . LYS F  1 129 ? 76.553  -5.573  16.162  1.00 11.43 ? 128 LYS H CG  1 
ATOM   6504  C  CD  . LYS F  1 129 ? 76.252  -4.127  15.757  1.00 16.31 ? 128 LYS H CD  1 
ATOM   6505  C  CE  . LYS F  1 129 ? 75.447  -3.357  16.792  1.00 20.72 ? 128 LYS H CE  1 
ATOM   6506  N  NZ  . LYS F  1 129 ? 75.390  -1.933  16.473  1.00 25.11 ? 128 LYS H NZ  1 
ATOM   6507  N  N   . GLY F  1 130 ? 78.924  -8.361  19.498  1.00 3.31  ? 129 GLY H N   1 
ATOM   6508  C  CA  . GLY F  1 130 ? 79.601  -8.478  20.768  1.00 2.00  ? 129 GLY H CA  1 
ATOM   6509  C  C   . GLY F  1 130 ? 81.044  -8.905  20.667  1.00 4.02  ? 129 GLY H C   1 
ATOM   6510  O  O   . GLY F  1 130 ? 81.747  -9.056  21.676  1.00 7.94  ? 129 GLY H O   1 
ATOM   6511  N  N   . GLY F  1 131 ? 81.575  -9.204  19.496  1.00 3.53  ? 130 GLY H N   1 
ATOM   6512  C  CA  . GLY F  1 131 ? 82.993  -9.505  19.403  1.00 2.00  ? 130 GLY H CA  1 
ATOM   6513  C  C   . GLY F  1 131 ? 83.313  -10.893 19.897  1.00 2.07  ? 130 GLY H C   1 
ATOM   6514  O  O   . GLY F  1 131 ? 84.485  -11.247 20.068  1.00 2.00  ? 130 GLY H O   1 
ATOM   6515  N  N   . ASN F  1 132 ? 82.309  -11.749 20.113  1.00 4.06  ? 131 ASN H N   1 
ATOM   6516  C  CA  . ASN F  1 132 ? 82.614  -13.126 20.461  1.00 5.11  ? 131 ASN H CA  1 
ATOM   6517  C  C   . ASN F  1 132 ? 81.827  -14.116 19.624  1.00 5.77  ? 131 ASN H C   1 
ATOM   6518  O  O   . ASN F  1 132 ? 80.931  -13.743 18.876  1.00 6.16  ? 131 ASN H O   1 
ATOM   6519  C  CB  . ASN F  1 132 ? 82.397  -13.325 21.974  1.00 2.00  ? 131 ASN H CB  1 
ATOM   6520  C  CG  . ASN F  1 132 ? 81.036  -13.183 22.581  1.00 2.01  ? 131 ASN H CG  1 
ATOM   6521  O  OD1 . ASN F  1 132 ? 80.017  -13.214 21.903  1.00 5.94  ? 131 ASN H OD1 1 
ATOM   6522  N  ND2 . ASN F  1 132 ? 80.912  -13.067 23.890  1.00 6.52  ? 131 ASN H ND2 1 
ATOM   6523  N  N   . GLU F  1 133 ? 82.150  -15.400 19.657  1.00 9.08  ? 132 GLU H N   1 
ATOM   6524  C  CA  . GLU F  1 133 ? 81.463  -16.392 18.841  1.00 11.24 ? 132 GLU H CA  1 
ATOM   6525  C  C   . GLU F  1 133 ? 79.986  -16.550 19.192  1.00 10.54 ? 132 GLU H C   1 
ATOM   6526  O  O   . GLU F  1 133 ? 79.084  -16.666 18.363  1.00 10.75 ? 132 GLU H O   1 
ATOM   6527  C  CB  . GLU F  1 133 ? 82.233  -17.624 19.060  1.00 16.55 ? 132 GLU H CB  1 
ATOM   6528  C  CG  . GLU F  1 133 ? 81.926  -18.830 18.191  1.00 24.71 ? 132 GLU H CG  1 
ATOM   6529  C  CD  . GLU F  1 133 ? 82.649  -19.983 18.877  1.00 29.70 ? 132 GLU H CD  1 
ATOM   6530  O  OE1 . GLU F  1 133 ? 83.847  -20.170 18.617  1.00 34.32 ? 132 GLU H OE1 1 
ATOM   6531  O  OE2 . GLU F  1 133 ? 82.036  -20.645 19.726  1.00 31.64 ? 132 GLU H OE2 1 
ATOM   6532  N  N   . GLU F  1 134 ? 79.771  -16.565 20.505  1.00 8.78  ? 133 GLU H N   1 
ATOM   6533  C  CA  . GLU F  1 134 ? 78.463  -16.580 21.070  1.00 6.11  ? 133 GLU H CA  1 
ATOM   6534  C  C   . GLU F  1 134 ? 77.579  -15.521 20.483  1.00 4.76  ? 133 GLU H C   1 
ATOM   6535  O  O   . GLU F  1 134 ? 76.456  -15.845 20.129  1.00 5.39  ? 133 GLU H O   1 
ATOM   6536  C  CB  . GLU F  1 134 ? 78.591  -16.375 22.524  1.00 8.18  ? 133 GLU H CB  1 
ATOM   6537  C  CG  . GLU F  1 134 ? 77.303  -16.654 23.261  1.00 14.10 ? 133 GLU H CG  1 
ATOM   6538  C  CD  . GLU F  1 134 ? 76.744  -18.063 23.088  1.00 18.61 ? 133 GLU H CD  1 
ATOM   6539  O  OE1 . GLU F  1 134 ? 77.508  -19.040 23.003  1.00 19.82 ? 133 GLU H OE1 1 
ATOM   6540  O  OE2 . GLU F  1 134 ? 75.515  -18.168 23.042  1.00 22.83 ? 133 GLU H OE2 1 
ATOM   6541  N  N   . SER F  1 135 ? 78.092  -14.297 20.329  1.00 4.11  ? 134 SER H N   1 
ATOM   6542  C  CA  . SER F  1 135 ? 77.416  -13.174 19.743  1.00 2.00  ? 134 SER H CA  1 
ATOM   6543  C  C   . SER F  1 135 ? 76.900  -13.568 18.409  1.00 2.34  ? 134 SER H C   1 
ATOM   6544  O  O   . SER F  1 135 ? 75.686  -13.479 18.254  1.00 2.55  ? 134 SER H O   1 
ATOM   6545  C  CB  . SER F  1 135 ? 78.329  -12.036 19.519  1.00 3.21  ? 134 SER H CB  1 
ATOM   6546  O  OG  . SER F  1 135 ? 77.616  -10.832 19.289  1.00 2.70  ? 134 SER H OG  1 
ATOM   6547  N  N   . THR F  1 136 ? 77.723  -14.040 17.484  1.00 5.36  ? 135 THR H N   1 
ATOM   6548  C  CA  . THR F  1 136 ? 77.202  -14.475 16.190  1.00 7.17  ? 135 THR H CA  1 
ATOM   6549  C  C   . THR F  1 136 ? 76.428  -15.782 16.234  1.00 9.55  ? 135 THR H C   1 
ATOM   6550  O  O   . THR F  1 136 ? 76.040  -16.242 15.155  1.00 10.43 ? 135 THR H O   1 
ATOM   6551  C  CB  . THR F  1 136 ? 78.350  -14.566 15.162  1.00 7.17  ? 135 THR H CB  1 
ATOM   6552  O  OG1 . THR F  1 136 ? 79.490  -15.213 15.696  1.00 9.94  ? 135 THR H OG1 1 
ATOM   6553  C  CG2 . THR F  1 136 ? 78.740  -13.144 14.774  1.00 9.16  ? 135 THR H CG2 1 
ATOM   6554  N  N   . LYS F  1 137 ? 76.156  -16.415 17.401  1.00 7.85  ? 136 LYS H N   1 
ATOM   6555  C  CA  . LYS F  1 137 ? 75.205  -17.502 17.409  1.00 6.75  ? 136 LYS H CA  1 
ATOM   6556  C  C   . LYS F  1 137 ? 73.908  -17.072 18.052  1.00 4.40  ? 136 LYS H C   1 
ATOM   6557  O  O   . LYS F  1 137 ? 72.869  -17.256 17.411  1.00 5.65  ? 136 LYS H O   1 
ATOM   6558  C  CB  . LYS F  1 137 ? 75.635  -18.719 18.204  1.00 10.59 ? 136 LYS H CB  1 
ATOM   6559  C  CG  . LYS F  1 137 ? 76.859  -19.493 17.813  1.00 14.90 ? 136 LYS H CG  1 
ATOM   6560  C  CD  . LYS F  1 137 ? 77.133  -20.242 19.116  1.00 18.20 ? 136 LYS H CD  1 
ATOM   6561  C  CE  . LYS F  1 137 ? 78.586  -20.722 19.219  1.00 21.01 ? 136 LYS H CE  1 
ATOM   6562  N  NZ  . LYS F  1 137 ? 78.972  -20.934 20.615  1.00 22.12 ? 136 LYS H NZ  1 
ATOM   6563  N  N   . THR F  1 138 ? 73.888  -16.560 19.289  1.00 2.00  ? 137 THR H N   1 
ATOM   6564  C  CA  . THR F  1 138 ? 72.638  -16.265 19.970  1.00 2.00  ? 137 THR H CA  1 
ATOM   6565  C  C   . THR F  1 138 ? 72.468  -14.813 20.363  1.00 2.00  ? 137 THR H C   1 
ATOM   6566  O  O   . THR F  1 138 ? 71.484  -14.417 20.990  1.00 2.60  ? 137 THR H O   1 
ATOM   6567  C  CB  . THR F  1 138 ? 72.549  -17.098 21.214  1.00 2.00  ? 137 THR H CB  1 
ATOM   6568  O  OG1 . THR F  1 138 ? 73.550  -16.571 22.099  1.00 2.79  ? 137 THR H OG1 1 
ATOM   6569  C  CG2 . THR F  1 138 ? 72.837  -18.584 20.981  1.00 2.00  ? 137 THR H CG2 1 
ATOM   6570  N  N   . GLY F  1 139 ? 73.426  -13.957 20.084  1.00 2.00  ? 138 GLY H N   1 
ATOM   6571  C  CA  . GLY F  1 139 ? 73.300  -12.618 20.536  1.00 2.00  ? 138 GLY H CA  1 
ATOM   6572  C  C   . GLY F  1 139 ? 73.654  -12.492 21.982  1.00 2.00  ? 138 GLY H C   1 
ATOM   6573  O  O   . GLY F  1 139 ? 73.636  -11.378 22.488  1.00 2.00  ? 138 GLY H O   1 
ATOM   6574  N  N   . ASN F  1 140 ? 74.117  -13.556 22.632  1.00 2.00  ? 139 ASN H N   1 
ATOM   6575  C  CA  . ASN F  1 140 ? 74.436  -13.557 24.068  1.00 2.00  ? 139 ASN H CA  1 
ATOM   6576  C  C   . ASN F  1 140 ? 73.199  -13.175 24.898  1.00 2.00  ? 139 ASN H C   1 
ATOM   6577  O  O   . ASN F  1 140 ? 73.255  -12.497 25.925  1.00 2.00  ? 139 ASN H O   1 
ATOM   6578  C  CB  . ASN F  1 140 ? 75.587  -12.570 24.395  1.00 2.54  ? 139 ASN H CB  1 
ATOM   6579  C  CG  . ASN F  1 140 ? 77.021  -12.993 24.132  1.00 3.00  ? 139 ASN H CG  1 
ATOM   6580  O  OD1 . ASN F  1 140 ? 77.760  -13.500 24.973  1.00 3.90  ? 139 ASN H OD1 1 
ATOM   6581  N  ND2 . ASN F  1 140 ? 77.502  -12.698 22.931  1.00 6.60  ? 139 ASN H ND2 1 
ATOM   6582  N  N   . ALA F  1 141 ? 72.042  -13.634 24.418  1.00 2.00  ? 140 ALA H N   1 
ATOM   6583  C  CA  . ALA F  1 141 ? 70.733  -13.365 24.982  1.00 3.32  ? 140 ALA H CA  1 
ATOM   6584  C  C   . ALA F  1 141 ? 70.358  -14.069 26.287  1.00 2.00  ? 140 ALA H C   1 
ATOM   6585  O  O   . ALA F  1 141 ? 69.293  -13.804 26.843  1.00 2.09  ? 140 ALA H O   1 
ATOM   6586  C  CB  . ALA F  1 141 ? 69.682  -13.692 23.929  1.00 2.00  ? 140 ALA H CB  1 
ATOM   6587  N  N   . GLY F  1 142 ? 71.192  -14.959 26.806  1.00 2.00  ? 141 GLY H N   1 
ATOM   6588  C  CA  . GLY F  1 142 ? 70.997  -15.642 28.063  1.00 2.00  ? 141 GLY H CA  1 
ATOM   6589  C  C   . GLY F  1 142 ? 69.980  -16.752 27.964  1.00 2.00  ? 141 GLY H C   1 
ATOM   6590  O  O   . GLY F  1 142 ? 69.605  -17.174 26.877  1.00 3.37  ? 141 GLY H O   1 
ATOM   6591  N  N   . SER F  1 143 ? 69.433  -17.173 29.084  1.00 2.00  ? 142 SER H N   1 
ATOM   6592  C  CA  . SER F  1 143 ? 68.441  -18.215 29.152  1.00 2.00  ? 142 SER H CA  1 
ATOM   6593  C  C   . SER F  1 143 ? 67.086  -17.882 28.551  1.00 2.00  ? 142 SER H C   1 
ATOM   6594  O  O   . SER F  1 143 ? 66.750  -16.744 28.206  1.00 2.00  ? 142 SER H O   1 
ATOM   6595  C  CB  . SER F  1 143 ? 68.319  -18.595 30.597  1.00 3.43  ? 142 SER H CB  1 
ATOM   6596  O  OG  . SER F  1 143 ? 68.154  -17.391 31.344  1.00 6.24  ? 142 SER H OG  1 
ATOM   6597  N  N   . ARG F  1 144 ? 66.312  -18.940 28.363  1.00 2.00  ? 143 ARG H N   1 
ATOM   6598  C  CA  . ARG F  1 144 ? 65.062  -18.825 27.692  1.00 2.00  ? 143 ARG H CA  1 
ATOM   6599  C  C   . ARG F  1 144 ? 64.056  -18.664 28.786  1.00 2.86  ? 143 ARG H C   1 
ATOM   6600  O  O   . ARG F  1 144 ? 63.841  -19.591 29.546  1.00 5.74  ? 143 ARG H O   1 
ATOM   6601  C  CB  . ARG F  1 144 ? 64.906  -20.086 26.876  1.00 2.00  ? 143 ARG H CB  1 
ATOM   6602  C  CG  . ARG F  1 144 ? 66.016  -20.158 25.872  1.00 2.00  ? 143 ARG H CG  1 
ATOM   6603  C  CD  . ARG F  1 144 ? 65.869  -21.393 25.101  1.00 5.45  ? 143 ARG H CD  1 
ATOM   6604  N  NE  . ARG F  1 144 ? 67.094  -21.581 24.339  1.00 5.54  ? 143 ARG H NE  1 
ATOM   6605  C  CZ  . ARG F  1 144 ? 67.182  -22.561 23.431  1.00 2.00  ? 143 ARG H CZ  1 
ATOM   6606  N  NH1 . ARG F  1 144 ? 66.160  -23.333 23.177  1.00 2.00  ? 143 ARG H NH1 1 
ATOM   6607  N  NH2 . ARG F  1 144 ? 68.289  -22.756 22.729  1.00 2.00  ? 143 ARG H NH2 1 
ATOM   6608  N  N   . LEU F  1 145 ? 63.448  -17.517 28.929  1.00 3.36  ? 144 LEU H N   1 
ATOM   6609  C  CA  . LEU F  1 145 ? 62.503  -17.350 30.008  1.00 4.83  ? 144 LEU H CA  1 
ATOM   6610  C  C   . LEU F  1 145 ? 61.146  -17.968 29.684  1.00 5.68  ? 144 LEU H C   1 
ATOM   6611  O  O   . LEU F  1 145 ? 60.469  -18.504 30.552  1.00 9.34  ? 144 LEU H O   1 
ATOM   6612  C  CB  . LEU F  1 145 ? 62.333  -15.875 30.306  1.00 5.52  ? 144 LEU H CB  1 
ATOM   6613  C  CG  . LEU F  1 145 ? 63.520  -15.033 30.766  1.00 4.63  ? 144 LEU H CG  1 
ATOM   6614  C  CD1 . LEU F  1 145 ? 63.032  -13.724 31.317  1.00 2.00  ? 144 LEU H CD1 1 
ATOM   6615  C  CD2 . LEU F  1 145 ? 64.258  -15.740 31.873  1.00 4.68  ? 144 LEU H CD2 1 
ATOM   6616  N  N   . ALA F  1 146 ? 60.685  -17.931 28.455  1.00 5.85  ? 145 ALA H N   1 
ATOM   6617  C  CA  . ALA F  1 146 ? 59.393  -18.478 28.100  1.00 4.29  ? 145 ALA H CA  1 
ATOM   6618  C  C   . ALA F  1 146 ? 59.361  -18.786 26.596  1.00 4.57  ? 145 ALA H C   1 
ATOM   6619  O  O   . ALA F  1 146 ? 59.900  -18.057 25.741  1.00 2.00  ? 145 ALA H O   1 
ATOM   6620  C  CB  . ALA F  1 146 ? 58.301  -17.469 28.423  1.00 3.25  ? 145 ALA H CB  1 
ATOM   6621  N  N   . CYS F  1 147 ? 58.741  -19.909 26.265  1.00 4.49  ? 146 CYS H N   1 
ATOM   6622  C  CA  . CYS F  1 147 ? 58.571  -20.290 24.899  1.00 2.61  ? 146 CYS H CA  1 
ATOM   6623  C  C   . CYS F  1 147 ? 57.144  -20.693 24.613  1.00 2.00  ? 146 CYS H C   1 
ATOM   6624  O  O   . CYS F  1 147 ? 56.301  -20.723 25.488  1.00 2.00  ? 146 CYS H O   1 
ATOM   6625  C  CB  . CYS F  1 147 ? 59.564  -21.379 24.661  1.00 2.00  ? 146 CYS H CB  1 
ATOM   6626  S  SG  . CYS F  1 147 ? 59.589  -22.665 25.912  1.00 8.66  ? 146 CYS H SG  1 
ATOM   6627  N  N   . GLY F  1 148 ? 56.789  -20.867 23.363  1.00 2.00  ? 147 GLY H N   1 
ATOM   6628  C  CA  . GLY F  1 148 ? 55.493  -21.326 22.930  1.00 2.00  ? 147 GLY H CA  1 
ATOM   6629  C  C   . GLY F  1 148 ? 55.573  -21.705 21.443  1.00 2.00  ? 147 GLY H C   1 
ATOM   6630  O  O   . GLY F  1 148 ? 56.258  -21.071 20.642  1.00 2.00  ? 147 GLY H O   1 
ATOM   6631  N  N   . VAL F  1 149 ? 54.965  -22.836 21.077  1.00 3.27  ? 148 VAL H N   1 
ATOM   6632  C  CA  . VAL F  1 149 ? 54.946  -23.298 19.710  1.00 2.00  ? 148 VAL H CA  1 
ATOM   6633  C  C   . VAL F  1 149 ? 53.996  -22.371 18.980  1.00 2.00  ? 148 VAL H C   1 
ATOM   6634  O  O   . VAL F  1 149 ? 52.929  -22.007 19.479  1.00 2.00  ? 148 VAL H O   1 
ATOM   6635  C  CB  . VAL F  1 149 ? 54.473  -24.755 19.691  1.00 2.00  ? 148 VAL H CB  1 
ATOM   6636  C  CG1 . VAL F  1 149 ? 54.448  -25.330 18.314  1.00 2.00  ? 148 VAL H CG1 1 
ATOM   6637  C  CG2 . VAL F  1 149 ? 55.470  -25.575 20.456  1.00 2.00  ? 148 VAL H CG2 1 
ATOM   6638  N  N   . ILE F  1 150 ? 54.439  -21.926 17.829  1.00 2.00  ? 149 ILE H N   1 
ATOM   6639  C  CA  . ILE F  1 150 ? 53.676  -21.041 17.011  1.00 2.00  ? 149 ILE H CA  1 
ATOM   6640  C  C   . ILE F  1 150 ? 52.626  -21.829 16.253  1.00 2.00  ? 149 ILE H C   1 
ATOM   6641  O  O   . ILE F  1 150 ? 52.936  -22.584 15.323  1.00 3.52  ? 149 ILE H O   1 
ATOM   6642  C  CB  . ILE F  1 150 ? 54.675  -20.315 16.092  1.00 3.24  ? 149 ILE H CB  1 
ATOM   6643  C  CG1 . ILE F  1 150 ? 55.684  -19.537 16.927  1.00 2.00  ? 149 ILE H CG1 1 
ATOM   6644  C  CG2 . ILE F  1 150 ? 53.924  -19.312 15.219  1.00 2.64  ? 149 ILE H CG2 1 
ATOM   6645  C  CD1 . ILE F  1 150 ? 56.926  -19.030 16.200  1.00 2.00  ? 149 ILE H CD1 1 
ATOM   6646  N  N   . GLY F  1 151 ? 51.370  -21.710 16.639  1.00 2.00  ? 150 GLY H N   1 
ATOM   6647  C  CA  . GLY F  1 151 ? 50.320  -22.429 15.947  1.00 2.28  ? 150 GLY H CA  1 
ATOM   6648  C  C   . GLY F  1 151 ? 49.481  -21.486 15.078  1.00 2.65  ? 150 GLY H C   1 
ATOM   6649  O  O   . GLY F  1 151 ? 49.597  -20.256 15.092  1.00 2.00  ? 150 GLY H O   1 
ATOM   6650  N  N   . ILE F  1 152 ? 48.653  -22.114 14.269  1.00 2.34  ? 151 ILE H N   1 
ATOM   6651  C  CA  . ILE F  1 152 ? 47.788  -21.412 13.352  1.00 5.97  ? 151 ILE H CA  1 
ATOM   6652  C  C   . ILE F  1 152 ? 46.570  -20.847 14.052  1.00 8.29  ? 151 ILE H C   1 
ATOM   6653  O  O   . ILE F  1 152 ? 45.868  -21.581 14.732  1.00 12.80 ? 151 ILE H O   1 
ATOM   6654  C  CB  . ILE F  1 152 ? 47.307  -22.361 12.209  1.00 6.67  ? 151 ILE H CB  1 
ATOM   6655  C  CG1 . ILE F  1 152 ? 48.547  -22.936 11.525  1.00 6.59  ? 151 ILE H CG1 1 
ATOM   6656  C  CG2 . ILE F  1 152 ? 46.400  -21.628 11.208  1.00 2.00  ? 151 ILE H CG2 1 
ATOM   6657  C  CD1 . ILE F  1 152 ? 48.299  -23.754 10.265  1.00 2.00  ? 151 ILE H CD1 1 
ATOM   6658  N  N   . ALA F  1 153 ? 46.211  -19.609 13.824  1.00 9.91  ? 152 ALA H N   1 
ATOM   6659  C  CA  . ALA F  1 153 ? 45.044  -19.037 14.416  1.00 12.36 ? 152 ALA H CA  1 
ATOM   6660  C  C   . ALA F  1 153 ? 44.102  -18.738 13.269  1.00 17.73 ? 152 ALA H C   1 
ATOM   6661  O  O   . ALA F  1 153 ? 44.490  -18.685 12.077  1.00 19.90 ? 152 ALA H O   1 
ATOM   6662  C  CB  . ALA F  1 153 ? 45.411  -17.752 15.094  1.00 13.09 ? 152 ALA H CB  1 
ATOM   6663  N  N   . GLN F  1 154 ? 42.836  -18.637 13.643  1.00 21.19 ? 153 GLN H N   1 
ATOM   6664  C  CA  . GLN F  1 154 ? 41.871  -18.127 12.697  1.00 25.64 ? 153 GLN H CA  1 
ATOM   6665  C  C   . GLN F  1 154 ? 41.643  -16.655 13.059  1.00 28.31 ? 153 GLN H C   1 
ATOM   6666  O  O   . GLN F  1 154 ? 41.819  -16.282 14.243  1.00 30.74 ? 153 GLN H O   1 
ATOM   6667  C  CB  . GLN F  1 154 ? 40.509  -18.822 12.767  1.00 26.85 ? 153 GLN H CB  1 
ATOM   6668  C  CG  . GLN F  1 154 ? 39.610  -18.707 14.011  1.00 27.19 ? 153 GLN H CG  1 
ATOM   6669  C  CD  . GLN F  1 154 ? 38.172  -19.173 13.757  1.00 30.46 ? 153 GLN H CD  1 
ATOM   6670  O  OE1 . GLN F  1 154 ? 37.433  -19.404 14.708  1.00 29.82 ? 153 GLN H OE1 1 
ATOM   6671  N  NE2 . GLN F  1 154 ? 37.645  -19.348 12.536  1.00 31.55 ? 153 GLN H NE2 1 
ATOM   6672  O  OXT . GLN F  1 154 ? 41.228  -15.924 12.153  1.00 28.73 ? 153 GLN H OXT 1 
HETATM 6673  C  C   . ACE G  1 1   ? 154.440 4.198   7.379   1.00 37.51 ? 0   ACE D C   1 
HETATM 6674  O  O   . ACE G  1 1   ? 154.287 5.410   7.581   1.00 40.52 ? 0   ACE D O   1 
HETATM 6675  C  CH3 . ACE G  1 1   ? 153.380 3.513   6.523   1.00 36.16 ? 0   ACE D CH3 1 
ATOM   6676  N  N   . ALA G  1 2   ? 155.536 3.573   7.873   1.00 36.13 ? 1   ALA D N   1 
ATOM   6677  C  CA  . ALA G  1 2   ? 156.467 4.230   8.810   1.00 33.10 ? 1   ALA D CA  1 
ATOM   6678  C  C   . ALA G  1 2   ? 157.776 3.476   9.053   1.00 30.66 ? 1   ALA D C   1 
ATOM   6679  O  O   . ALA G  1 2   ? 158.046 2.441   8.459   1.00 31.00 ? 1   ALA D O   1 
ATOM   6680  C  CB  . ALA G  1 2   ? 155.798 4.415   10.195  1.00 32.26 ? 1   ALA D CB  1 
ATOM   6681  N  N   . THR G  1 3   ? 158.618 4.052   9.908   1.00 29.35 ? 2   THR D N   1 
ATOM   6682  C  CA  . THR G  1 3   ? 159.857 3.452   10.370  1.00 27.32 ? 2   THR D CA  1 
ATOM   6683  C  C   . THR G  1 3   ? 159.499 2.638   11.608  1.00 25.68 ? 2   THR D C   1 
ATOM   6684  O  O   . THR G  1 3   ? 159.816 1.443   11.661  1.00 27.48 ? 2   THR D O   1 
ATOM   6685  C  CB  . THR G  1 3   ? 160.894 4.533   10.790  1.00 30.04 ? 2   THR D CB  1 
ATOM   6686  O  OG1 . THR G  1 3   ? 161.021 5.407   9.668   1.00 32.62 ? 2   THR D OG1 1 
ATOM   6687  C  CG2 . THR G  1 3   ? 162.253 3.968   11.218  1.00 30.03 ? 2   THR D CG2 1 
ATOM   6688  N  N   . LYS G  1 4   ? 158.838 3.274   12.596  1.00 19.65 ? 3   LYS D N   1 
ATOM   6689  C  CA  . LYS G  1 4   ? 158.577 2.678   13.883  1.00 14.29 ? 3   LYS D CA  1 
ATOM   6690  C  C   . LYS G  1 4   ? 157.125 2.734   14.240  1.00 11.75 ? 3   LYS D C   1 
ATOM   6691  O  O   . LYS G  1 4   ? 156.426 3.684   13.905  1.00 10.07 ? 3   LYS D O   1 
ATOM   6692  C  CB  . LYS G  1 4   ? 159.262 3.394   14.977  1.00 15.36 ? 3   LYS D CB  1 
ATOM   6693  C  CG  . LYS G  1 4   ? 160.743 3.595   14.863  1.00 17.77 ? 3   LYS D CG  1 
ATOM   6694  C  CD  . LYS G  1 4   ? 161.275 3.682   16.287  1.00 21.91 ? 3   LYS D CD  1 
ATOM   6695  C  CE  . LYS G  1 4   ? 160.920 2.376   17.037  1.00 26.73 ? 3   LYS D CE  1 
ATOM   6696  N  NZ  . LYS G  1 4   ? 161.925 1.991   18.034  1.00 32.12 ? 3   LYS D NZ  1 
ATOM   6697  N  N   . ALA G  1 5   ? 156.660 1.747   14.976  1.00 10.04 ? 4   ALA D N   1 
ATOM   6698  C  CA  . ALA G  1 5   ? 155.274 1.715   15.386  1.00 6.82  ? 4   ALA D CA  1 
ATOM   6699  C  C   . ALA G  1 5   ? 155.160 1.160   16.798  1.00 3.64  ? 4   ALA D C   1 
ATOM   6700  O  O   . ALA G  1 5   ? 156.092 0.458   17.186  1.00 5.12  ? 4   ALA D O   1 
ATOM   6701  C  CB  . ALA G  1 5   ? 154.525 0.849   14.394  1.00 4.82  ? 4   ALA D CB  1 
ATOM   6702  N  N   . VAL G  1 6   ? 154.139 1.381   17.616  1.00 3.18  ? 5   VAL D N   1 
ATOM   6703  C  CA  . VAL G  1 6   ? 154.088 0.764   18.926  1.00 4.95  ? 5   VAL D CA  1 
ATOM   6704  C  C   . VAL G  1 6   ? 152.714 0.181   19.095  1.00 5.28  ? 5   VAL D C   1 
ATOM   6705  O  O   . VAL G  1 6   ? 151.827 0.533   18.328  1.00 8.39  ? 5   VAL D O   1 
ATOM   6706  C  CB  . VAL G  1 6   ? 154.411 1.856   19.971  1.00 6.09  ? 5   VAL D CB  1 
ATOM   6707  C  CG1 . VAL G  1 6   ? 153.208 2.721   20.282  1.00 5.04  ? 5   VAL D CG1 1 
ATOM   6708  C  CG2 . VAL G  1 6   ? 155.006 1.177   21.156  1.00 3.66  ? 5   VAL D CG2 1 
ATOM   6709  N  N   . ALA G  1 7   ? 152.499 -0.669  20.075  1.00 6.13  ? 6   ALA D N   1 
ATOM   6710  C  CA  . ALA G  1 7   ? 151.215 -1.304  20.309  1.00 5.30  ? 6   ALA D CA  1 
ATOM   6711  C  C   . ALA G  1 7   ? 151.166 -1.367  21.816  1.00 6.01  ? 6   ALA D C   1 
ATOM   6712  O  O   . ALA G  1 7   ? 152.145 -1.813  22.414  1.00 11.67 ? 6   ALA D O   1 
ATOM   6713  C  CB  . ALA G  1 7   ? 151.252 -2.669  19.765  1.00 2.00  ? 6   ALA D CB  1 
ATOM   6714  N  N   . VAL G  1 8   ? 150.156 -0.902  22.518  1.00 6.25  ? 7   VAL D N   1 
ATOM   6715  C  CA  . VAL G  1 8   ? 150.155 -0.894  23.984  1.00 6.27  ? 7   VAL D CA  1 
ATOM   6716  C  C   . VAL G  1 8   ? 149.038 -1.868  24.346  1.00 8.06  ? 7   VAL D C   1 
ATOM   6717  O  O   . VAL G  1 8   ? 147.857 -1.572  24.087  1.00 8.10  ? 7   VAL D O   1 
ATOM   6718  C  CB  . VAL G  1 8   ? 149.884 0.568   24.386  1.00 4.11  ? 7   VAL D CB  1 
ATOM   6719  C  CG1 . VAL G  1 8   ? 149.459 0.670   25.809  1.00 5.79  ? 7   VAL D CG1 1 
ATOM   6720  C  CG2 . VAL G  1 8   ? 151.147 1.378   24.191  1.00 2.54  ? 7   VAL D CG2 1 
ATOM   6721  N  N   . LEU G  1 9   ? 149.414 -3.053  24.842  1.00 7.07  ? 8   LEU D N   1 
ATOM   6722  C  CA  . LEU G  1 9   ? 148.497 -4.135  25.185  1.00 6.34  ? 8   LEU D CA  1 
ATOM   6723  C  C   . LEU G  1 9   ? 147.814 -3.996  26.548  1.00 7.95  ? 8   LEU D C   1 
ATOM   6724  O  O   . LEU G  1 9   ? 148.452 -3.815  27.585  1.00 9.27  ? 8   LEU D O   1 
ATOM   6725  C  CB  . LEU G  1 9   ? 149.298 -5.424  25.121  1.00 7.46  ? 8   LEU D CB  1 
ATOM   6726  C  CG  . LEU G  1 9   ? 149.517 -6.246  23.855  1.00 6.62  ? 8   LEU D CG  1 
ATOM   6727  C  CD1 . LEU G  1 9   ? 149.981 -5.447  22.688  1.00 7.15  ? 8   LEU D CD1 1 
ATOM   6728  C  CD2 . LEU G  1 9   ? 150.568 -7.248  24.183  1.00 7.91  ? 8   LEU D CD2 1 
ATOM   6729  N  N   . LYS G  1 10  ? 146.509 -4.076  26.630  1.00 10.24 ? 9   LYS D N   1 
ATOM   6730  C  CA  . LYS G  1 10  ? 145.755 -3.885  27.867  1.00 14.41 ? 9   LYS D CA  1 
ATOM   6731  C  C   . LYS G  1 10  ? 144.612 -4.825  27.675  1.00 17.08 ? 9   LYS D C   1 
ATOM   6732  O  O   . LYS G  1 10  ? 144.290 -5.123  26.515  1.00 19.15 ? 9   LYS D O   1 
ATOM   6733  C  CB  . LYS G  1 10  ? 145.089 -2.536  28.017  1.00 16.08 ? 9   LYS D CB  1 
ATOM   6734  C  CG  . LYS G  1 10  ? 145.980 -1.331  27.978  1.00 21.57 ? 9   LYS D CG  1 
ATOM   6735  C  CD  . LYS G  1 10  ? 146.086 -0.746  29.375  1.00 30.28 ? 9   LYS D CD  1 
ATOM   6736  C  CE  . LYS G  1 10  ? 146.999 0.476   29.251  1.00 35.79 ? 9   LYS D CE  1 
ATOM   6737  N  NZ  . LYS G  1 10  ? 147.056 1.239   30.495  1.00 40.78 ? 9   LYS D NZ  1 
ATOM   6738  N  N   . GLY G  1 11  ? 143.957 -5.302  28.724  1.00 20.79 ? 10  GLY D N   1 
ATOM   6739  C  CA  . GLY G  1 11  ? 142.838 -6.223  28.516  1.00 21.99 ? 10  GLY D CA  1 
ATOM   6740  C  C   . GLY G  1 11  ? 141.874 -6.174  29.686  1.00 23.14 ? 10  GLY D C   1 
ATOM   6741  O  O   . GLY G  1 11  ? 141.809 -5.162  30.394  1.00 19.73 ? 10  GLY D O   1 
ATOM   6742  N  N   . ASP G  1 12  ? 141.127 -7.271  29.900  1.00 26.25 ? 11  ASP D N   1 
ATOM   6743  C  CA  . ASP G  1 12  ? 140.166 -7.333  30.998  1.00 29.79 ? 11  ASP D CA  1 
ATOM   6744  C  C   . ASP G  1 12  ? 141.026 -7.788  32.160  1.00 31.26 ? 11  ASP D C   1 
ATOM   6745  O  O   . ASP G  1 12  ? 141.253 -8.982  32.418  1.00 33.99 ? 11  ASP D O   1 
ATOM   6746  C  CB  . ASP G  1 12  ? 139.082 -8.361  30.741  1.00 33.35 ? 11  ASP D CB  1 
ATOM   6747  C  CG  . ASP G  1 12  ? 137.885 -7.843  29.954  1.00 37.09 ? 11  ASP D CG  1 
ATOM   6748  O  OD1 . ASP G  1 12  ? 137.973 -7.812  28.722  1.00 39.99 ? 11  ASP D OD1 1 
ATOM   6749  O  OD2 . ASP G  1 12  ? 136.868 -7.489  30.574  1.00 41.07 ? 11  ASP D OD2 1 
ATOM   6750  N  N   . GLY G  1 13  ? 141.635 -6.778  32.768  1.00 29.91 ? 12  GLY D N   1 
ATOM   6751  C  CA  . GLY G  1 13  ? 142.546 -7.006  33.861  1.00 26.57 ? 12  GLY D CA  1 
ATOM   6752  C  C   . GLY G  1 13  ? 143.925 -7.303  33.318  1.00 22.31 ? 12  GLY D C   1 
ATOM   6753  O  O   . GLY G  1 13  ? 144.436 -6.507  32.527  1.00 24.09 ? 12  GLY D O   1 
ATOM   6754  N  N   . PRO G  1 14  ? 144.551 -8.424  33.726  1.00 19.57 ? 13  PRO D N   1 
ATOM   6755  C  CA  . PRO G  1 14  ? 145.925 -8.418  34.231  1.00 16.02 ? 13  PRO D CA  1 
ATOM   6756  C  C   . PRO G  1 14  ? 147.054 -8.170  33.235  1.00 14.81 ? 13  PRO D C   1 
ATOM   6757  O  O   . PRO G  1 14  ? 148.058 -7.527  33.548  1.00 11.42 ? 13  PRO D O   1 
ATOM   6758  C  CB  . PRO G  1 14  ? 146.016 -9.763  34.954  1.00 15.67 ? 13  PRO D CB  1 
ATOM   6759  C  CG  . PRO G  1 14  ? 145.101 -10.693 34.149  1.00 15.23 ? 13  PRO D CG  1 
ATOM   6760  C  CD  . PRO G  1 14  ? 143.930 -9.752  33.888  1.00 18.38 ? 13  PRO D CD  1 
ATOM   6761  N  N   . VAL G  1 15  ? 146.885 -8.688  32.013  1.00 14.08 ? 14  VAL D N   1 
ATOM   6762  C  CA  . VAL G  1 15  ? 147.937 -8.640  31.004  1.00 13.95 ? 14  VAL D CA  1 
ATOM   6763  C  C   . VAL G  1 15  ? 148.059 -7.232  30.423  1.00 15.39 ? 14  VAL D C   1 
ATOM   6764  O  O   . VAL G  1 15  ? 147.104 -6.580  29.970  1.00 17.86 ? 14  VAL D O   1 
ATOM   6765  C  CB  . VAL G  1 15  ? 147.626 -9.678  29.885  1.00 11.00 ? 14  VAL D CB  1 
ATOM   6766  C  CG1 . VAL G  1 15  ? 148.728 -9.653  28.840  1.00 11.08 ? 14  VAL D CG1 1 
ATOM   6767  C  CG2 . VAL G  1 15  ? 147.593 -11.090 30.445  1.00 8.80  ? 14  VAL D CG2 1 
ATOM   6768  N  N   . GLN G  1 16  ? 149.282 -6.742  30.477  1.00 14.77 ? 15  GLN D N   1 
ATOM   6769  C  CA  . GLN G  1 16  ? 149.584 -5.452  29.920  1.00 15.61 ? 15  GLN D CA  1 
ATOM   6770  C  C   . GLN G  1 16  ? 150.834 -5.589  29.095  1.00 12.76 ? 15  GLN D C   1 
ATOM   6771  O  O   . GLN G  1 16  ? 151.626 -6.481  29.373  1.00 13.87 ? 15  GLN D O   1 
ATOM   6772  C  CB  . GLN G  1 16  ? 149.862 -4.447  30.997  1.00 19.91 ? 15  GLN D CB  1 
ATOM   6773  C  CG  . GLN G  1 16  ? 148.715 -4.253  31.942  1.00 26.25 ? 15  GLN D CG  1 
ATOM   6774  C  CD  . GLN G  1 16  ? 149.268 -3.967  33.325  1.00 30.97 ? 15  GLN D CD  1 
ATOM   6775  O  OE1 . GLN G  1 16  ? 149.921 -2.940  33.546  1.00 35.24 ? 15  GLN D OE1 1 
ATOM   6776  N  NE2 . GLN G  1 16  ? 149.065 -4.870  34.283  1.00 33.97 ? 15  GLN D NE2 1 
ATOM   6777  N  N   . GLY G  1 17  ? 151.122 -4.760  28.113  1.00 12.35 ? 16  GLY D N   1 
ATOM   6778  C  CA  . GLY G  1 17  ? 152.409 -4.863  27.454  1.00 11.10 ? 16  GLY D CA  1 
ATOM   6779  C  C   . GLY G  1 17  ? 152.668 -3.690  26.550  1.00 8.94  ? 16  GLY D C   1 
ATOM   6780  O  O   . GLY G  1 17  ? 151.768 -2.933  26.213  1.00 11.57 ? 16  GLY D O   1 
ATOM   6781  N  N   . ILE G  1 18  ? 153.897 -3.523  26.145  1.00 6.61  ? 17  ILE D N   1 
ATOM   6782  C  CA  . ILE G  1 18  ? 154.260 -2.543  25.156  1.00 6.54  ? 17  ILE D CA  1 
ATOM   6783  C  C   . ILE G  1 18  ? 155.183 -3.282  24.221  1.00 7.53  ? 17  ILE D C   1 
ATOM   6784  O  O   . ILE G  1 18  ? 156.199 -3.811  24.663  1.00 7.47  ? 17  ILE D O   1 
ATOM   6785  C  CB  . ILE G  1 18  ? 155.040 -1.368  25.693  1.00 5.14  ? 17  ILE D CB  1 
ATOM   6786  C  CG1 . ILE G  1 18  ? 154.212 -0.642  26.731  1.00 6.36  ? 17  ILE D CG1 1 
ATOM   6787  C  CG2 . ILE G  1 18  ? 155.376 -0.444  24.530  1.00 2.85  ? 17  ILE D CG2 1 
ATOM   6788  C  CD1 . ILE G  1 18  ? 154.852 0.658   27.234  1.00 8.15  ? 17  ILE D CD1 1 
ATOM   6789  N  N   . ILE G  1 19  ? 154.801 -3.325  22.951  1.00 8.53  ? 18  ILE D N   1 
ATOM   6790  C  CA  . ILE G  1 19  ? 155.581 -3.963  21.926  1.00 8.93  ? 18  ILE D CA  1 
ATOM   6791  C  C   . ILE G  1 19  ? 155.860 -2.847  20.926  1.00 9.90  ? 18  ILE D C   1 
ATOM   6792  O  O   . ILE G  1 19  ? 154.973 -2.026  20.632  1.00 9.35  ? 18  ILE D O   1 
ATOM   6793  C  CB  . ILE G  1 19  ? 154.758 -5.106  21.318  1.00 8.88  ? 18  ILE D CB  1 
ATOM   6794  C  CG1 . ILE G  1 19  ? 154.381 -6.112  22.389  1.00 7.88  ? 18  ILE D CG1 1 
ATOM   6795  C  CG2 . ILE G  1 19  ? 155.574 -5.784  20.217  1.00 10.10 ? 18  ILE D CG2 1 
ATOM   6796  C  CD1 . ILE G  1 19  ? 155.579 -6.786  23.077  1.00 8.66  ? 18  ILE D CD1 1 
ATOM   6797  N  N   . ASN G  1 20  ? 157.140 -2.814  20.516  1.00 10.34 ? 19  ASN D N   1 
ATOM   6798  C  CA  . ASN G  1 20  ? 157.736 -1.890  19.560  1.00 9.27  ? 19  ASN D CA  1 
ATOM   6799  C  C   . ASN G  1 20  ? 158.039 -2.619  18.291  1.00 11.46 ? 19  ASN D C   1 
ATOM   6800  O  O   . ASN G  1 20  ? 158.417 -3.803  18.351  1.00 14.11 ? 19  ASN D O   1 
ATOM   6801  C  CB  . ASN G  1 20  ? 159.043 -1.378  19.956  1.00 9.43  ? 19  ASN D CB  1 
ATOM   6802  C  CG  . ASN G  1 20  ? 158.921 -0.726  21.285  1.00 12.98 ? 19  ASN D CG  1 
ATOM   6803  O  OD1 . ASN G  1 20  ? 159.093 -1.369  22.321  1.00 14.86 ? 19  ASN D OD1 1 
ATOM   6804  N  ND2 . ASN G  1 20  ? 158.570 0.556   21.279  1.00 13.75 ? 19  ASN D ND2 1 
ATOM   6805  N  N   . PHE G  1 21  ? 157.848 -1.922  17.167  1.00 11.76 ? 20  PHE D N   1 
ATOM   6806  C  CA  . PHE G  1 21  ? 158.130 -2.439  15.833  1.00 12.07 ? 20  PHE D CA  1 
ATOM   6807  C  C   . PHE G  1 21  ? 159.109 -1.464  15.202  1.00 13.76 ? 20  PHE D C   1 
ATOM   6808  O  O   . PHE G  1 21  ? 159.081 -0.273  15.528  1.00 15.40 ? 20  PHE D O   1 
ATOM   6809  C  CB  . PHE G  1 21  ? 156.863 -2.505  14.971  1.00 9.76  ? 20  PHE D CB  1 
ATOM   6810  C  CG  . PHE G  1 21  ? 155.855 -3.606  15.365  1.00 8.71  ? 20  PHE D CG  1 
ATOM   6811  C  CD1 . PHE G  1 21  ? 156.008 -4.897  14.896  1.00 9.76  ? 20  PHE D CD1 1 
ATOM   6812  C  CD2 . PHE G  1 21  ? 154.785 -3.331  16.193  1.00 7.24  ? 20  PHE D CD2 1 
ATOM   6813  C  CE1 . PHE G  1 21  ? 155.116 -5.890  15.245  1.00 6.96  ? 20  PHE D CE1 1 
ATOM   6814  C  CE2 . PHE G  1 21  ? 153.896 -4.328  16.541  1.00 4.82  ? 20  PHE D CE2 1 
ATOM   6815  C  CZ  . PHE G  1 21  ? 154.061 -5.601  16.067  1.00 5.96  ? 20  PHE D CZ  1 
ATOM   6816  N  N   . GLU G  1 22  ? 160.022 -1.913  14.355  1.00 15.16 ? 21  GLU D N   1 
ATOM   6817  C  CA  . GLU G  1 22  ? 160.933 -1.020  13.682  1.00 16.69 ? 21  GLU D CA  1 
ATOM   6818  C  C   . GLU G  1 22  ? 161.273 -1.676  12.338  1.00 16.59 ? 21  GLU D C   1 
ATOM   6819  O  O   . GLU G  1 22  ? 161.723 -2.819  12.315  1.00 15.37 ? 21  GLU D O   1 
ATOM   6820  C  CB  . GLU G  1 22  ? 162.164 -0.846  14.544  1.00 17.79 ? 21  GLU D CB  1 
ATOM   6821  C  CG  . GLU G  1 22  ? 163.101 0.210   13.970  1.00 23.23 ? 21  GLU D CG  1 
ATOM   6822  C  CD  . GLU G  1 22  ? 164.464 0.253   14.636  1.00 26.49 ? 21  GLU D CD  1 
ATOM   6823  O  OE1 . GLU G  1 22  ? 165.193 -0.748  14.596  1.00 28.96 ? 21  GLU D OE1 1 
ATOM   6824  O  OE2 . GLU G  1 22  ? 164.798 1.310   15.180  1.00 31.60 ? 21  GLU D OE2 1 
ATOM   6825  N  N   . GLN G  1 23  ? 160.997 -1.039  11.215  1.00 16.82 ? 22  GLN D N   1 
ATOM   6826  C  CA  . GLN G  1 23  ? 161.282 -1.572  9.911   1.00 19.81 ? 22  GLN D CA  1 
ATOM   6827  C  C   . GLN G  1 23  ? 162.278 -0.579  9.374   1.00 25.30 ? 22  GLN D C   1 
ATOM   6828  O  O   . GLN G  1 23  ? 161.945 0.487   8.874   1.00 28.45 ? 22  GLN D O   1 
ATOM   6829  C  CB  . GLN G  1 23  ? 160.036 -1.579  9.077   1.00 15.89 ? 22  GLN D CB  1 
ATOM   6830  C  CG  . GLN G  1 23  ? 160.267 -1.776  7.622   1.00 10.97 ? 22  GLN D CG  1 
ATOM   6831  C  CD  . GLN G  1 23  ? 158.992 -2.164  6.945   1.00 9.93  ? 22  GLN D CD  1 
ATOM   6832  O  OE1 . GLN G  1 23  ? 158.031 -1.416  6.955   1.00 9.85  ? 22  GLN D OE1 1 
ATOM   6833  N  NE2 . GLN G  1 23  ? 158.926 -3.357  6.366   1.00 11.17 ? 22  GLN D NE2 1 
ATOM   6834  N  N   . LYS G  1 24  ? 163.527 -0.945  9.511   1.00 31.18 ? 23  LYS D N   1 
ATOM   6835  C  CA  . LYS G  1 24  ? 164.659 -0.119  9.118   1.00 36.22 ? 23  LYS D CA  1 
ATOM   6836  C  C   . LYS G  1 24  ? 164.827 0.129   7.611   1.00 38.15 ? 23  LYS D C   1 
ATOM   6837  O  O   . LYS G  1 24  ? 165.720 0.868   7.175   1.00 38.18 ? 23  LYS D O   1 
ATOM   6838  C  CB  . LYS G  1 24  ? 165.937 -0.777  9.654   1.00 39.35 ? 23  LYS D CB  1 
ATOM   6839  C  CG  . LYS G  1 24  ? 166.240 -2.163  9.003   1.00 41.93 ? 23  LYS D CG  1 
ATOM   6840  C  CD  . LYS G  1 24  ? 167.446 -2.861  9.645   1.00 44.97 ? 23  LYS D CD  1 
ATOM   6841  C  CE  . LYS G  1 24  ? 168.756 -2.068  9.580   1.00 45.90 ? 23  LYS D CE  1 
ATOM   6842  N  NZ  . LYS G  1 24  ? 169.789 -2.732  10.363  1.00 48.27 ? 23  LYS D NZ  1 
ATOM   6843  N  N   . GLU G  1 25  ? 163.980 -0.479  6.782   1.00 39.44 ? 24  GLU D N   1 
ATOM   6844  C  CA  . GLU G  1 25  ? 164.245 -0.495  5.365   1.00 41.15 ? 24  GLU D CA  1 
ATOM   6845  C  C   . GLU G  1 25  ? 162.953 -0.834  4.682   1.00 39.06 ? 24  GLU D C   1 
ATOM   6846  O  O   . GLU G  1 25  ? 162.409 -1.899  4.935   1.00 36.36 ? 24  GLU D O   1 
ATOM   6847  C  CB  . GLU G  1 25  ? 165.312 -1.572  5.065   1.00 44.50 ? 24  GLU D CB  1 
ATOM   6848  C  CG  . GLU G  1 25  ? 165.744 -1.852  3.621   1.00 48.80 ? 24  GLU D CG  1 
ATOM   6849  C  CD  . GLU G  1 25  ? 166.582 -0.745  2.991   1.00 52.92 ? 24  GLU D CD  1 
ATOM   6850  O  OE1 . GLU G  1 25  ? 167.635 -0.419  3.562   1.00 54.73 ? 24  GLU D OE1 1 
ATOM   6851  O  OE2 . GLU G  1 25  ? 166.185 -0.232  1.930   1.00 54.30 ? 24  GLU D OE2 1 
ATOM   6852  N  N   . SER G  1 26  ? 162.534 0.063   3.812   1.00 38.52 ? 25  SER D N   1 
ATOM   6853  C  CA  . SER G  1 26  ? 161.382 -0.053  2.932   1.00 39.10 ? 25  SER D CA  1 
ATOM   6854  C  C   . SER G  1 26  ? 160.609 -1.365  2.684   1.00 39.71 ? 25  SER D C   1 
ATOM   6855  O  O   . SER G  1 26  ? 159.397 -1.365  2.463   1.00 40.34 ? 25  SER D O   1 
ATOM   6856  C  CB  . SER G  1 26  ? 161.875 0.509   1.634   1.00 39.10 ? 25  SER D CB  1 
ATOM   6857  O  OG  . SER G  1 26  ? 163.206 0.039   1.352   1.00 38.64 ? 25  SER D OG  1 
ATOM   6858  N  N   . ASN G  1 27  ? 161.281 -2.510  2.634   1.00 39.80 ? 26  ASN D N   1 
ATOM   6859  C  CA  . ASN G  1 27  ? 160.677 -3.826  2.388   1.00 39.44 ? 26  ASN D CA  1 
ATOM   6860  C  C   . ASN G  1 27  ? 161.577 -4.876  3.035   1.00 35.89 ? 26  ASN D C   1 
ATOM   6861  O  O   . ASN G  1 27  ? 161.679 -6.018  2.592   1.00 36.13 ? 26  ASN D O   1 
ATOM   6862  C  CB  . ASN G  1 27  ? 160.576 -4.101  0.868   1.00 44.17 ? 26  ASN D CB  1 
ATOM   6863  C  CG  . ASN G  1 27  ? 161.934 -4.111  0.132   1.00 48.29 ? 26  ASN D CG  1 
ATOM   6864  O  OD1 . ASN G  1 27  ? 162.830 -3.267  0.349   1.00 47.79 ? 26  ASN D OD1 1 
ATOM   6865  N  ND2 . ASN G  1 27  ? 162.126 -5.076  -0.772  1.00 48.84 ? 26  ASN D ND2 1 
ATOM   6866  N  N   . GLY G  1 28  ? 162.272 -4.454  4.087   1.00 33.59 ? 27  GLY D N   1 
ATOM   6867  C  CA  . GLY G  1 28  ? 163.188 -5.268  4.853   1.00 28.55 ? 27  GLY D CA  1 
ATOM   6868  C  C   . GLY G  1 28  ? 162.419 -5.678  6.084   1.00 25.97 ? 27  GLY D C   1 
ATOM   6869  O  O   . GLY G  1 28  ? 161.265 -5.252  6.256   1.00 25.05 ? 27  GLY D O   1 
ATOM   6870  N  N   . PRO G  1 29  ? 162.978 -6.497  6.952   1.00 24.80 ? 28  PRO D N   1 
ATOM   6871  C  CA  . PRO G  1 29  ? 162.275 -7.059  8.080   1.00 24.15 ? 28  PRO D CA  1 
ATOM   6872  C  C   . PRO G  1 29  ? 161.940 -6.019  9.132   1.00 23.10 ? 28  PRO D C   1 
ATOM   6873  O  O   . PRO G  1 29  ? 162.584 -4.976  9.229   1.00 23.42 ? 28  PRO D O   1 
ATOM   6874  C  CB  . PRO G  1 29  ? 163.184 -8.148  8.600   1.00 22.64 ? 28  PRO D CB  1 
ATOM   6875  C  CG  . PRO G  1 29  ? 164.541 -7.587  8.305   1.00 26.25 ? 28  PRO D CG  1 
ATOM   6876  C  CD  . PRO G  1 29  ? 164.336 -7.009  6.893   1.00 26.78 ? 28  PRO D CD  1 
ATOM   6877  N  N   . VAL G  1 30  ? 160.893 -6.338  9.882   1.00 21.58 ? 29  VAL D N   1 
ATOM   6878  C  CA  . VAL G  1 30  ? 160.414 -5.594  11.016  1.00 18.68 ? 29  VAL D CA  1 
ATOM   6879  C  C   . VAL G  1 30  ? 160.985 -6.307  12.244  1.00 18.88 ? 29  VAL D C   1 
ATOM   6880  O  O   . VAL G  1 30  ? 160.862 -7.533  12.382  1.00 17.74 ? 29  VAL D O   1 
ATOM   6881  C  CB  . VAL G  1 30  ? 158.892 -5.650  10.982  1.00 18.63 ? 29  VAL D CB  1 
ATOM   6882  C  CG1 . VAL G  1 30  ? 158.316 -4.912  12.160  1.00 16.45 ? 29  VAL D CG1 1 
ATOM   6883  C  CG2 . VAL G  1 30  ? 158.405 -5.081  9.668   1.00 14.55 ? 29  VAL D CG2 1 
ATOM   6884  N  N   . LYS G  1 31  ? 161.709 -5.567  13.075  1.00 16.87 ? 30  LYS D N   1 
ATOM   6885  C  CA  . LYS G  1 31  ? 162.164 -6.024  14.374  1.00 15.63 ? 30  LYS D CA  1 
ATOM   6886  C  C   . LYS G  1 31  ? 160.938 -5.874  15.264  1.00 15.19 ? 30  LYS D C   1 
ATOM   6887  O  O   . LYS G  1 31  ? 160.278 -4.832  15.162  1.00 14.14 ? 30  LYS D O   1 
ATOM   6888  C  CB  . LYS G  1 31  ? 163.205 -5.114  14.940  1.00 17.59 ? 30  LYS D CB  1 
ATOM   6889  C  CG  . LYS G  1 31  ? 164.366 -5.749  15.627  1.00 21.13 ? 30  LYS D CG  1 
ATOM   6890  C  CD  . LYS G  1 31  ? 165.502 -5.493  14.641  1.00 26.96 ? 30  LYS D CD  1 
ATOM   6891  C  CE  . LYS G  1 31  ? 166.793 -5.251  15.429  1.00 31.47 ? 30  LYS D CE  1 
ATOM   6892  N  NZ  . LYS G  1 31  ? 167.902 -4.721  14.632  1.00 33.36 ? 30  LYS D NZ  1 
ATOM   6893  N  N   . VAL G  1 32  ? 160.513 -6.813  16.093  1.00 14.21 ? 31  VAL D N   1 
ATOM   6894  C  CA  . VAL G  1 32  ? 159.408 -6.508  16.989  1.00 14.05 ? 31  VAL D CA  1 
ATOM   6895  C  C   . VAL G  1 32  ? 159.939 -6.927  18.330  1.00 12.29 ? 31  VAL D C   1 
ATOM   6896  O  O   . VAL G  1 32  ? 160.561 -7.969  18.456  1.00 15.48 ? 31  VAL D O   1 
ATOM   6897  C  CB  . VAL G  1 32  ? 158.047 -7.240  16.529  1.00 15.08 ? 31  VAL D CB  1 
ATOM   6898  C  CG1 . VAL G  1 32  ? 158.350 -8.252  15.466  1.00 17.16 ? 31  VAL D CG1 1 
ATOM   6899  C  CG2 . VAL G  1 32  ? 157.294 -7.877  17.689  1.00 12.56 ? 31  VAL D CG2 1 
ATOM   6900  N  N   . TRP G  1 33  ? 159.874 -6.115  19.348  1.00 12.96 ? 32  TRP D N   1 
ATOM   6901  C  CA  . TRP G  1 33  ? 160.458 -6.495  20.618  1.00 14.48 ? 32  TRP D CA  1 
ATOM   6902  C  C   . TRP G  1 33  ? 159.644 -5.894  21.760  1.00 13.53 ? 32  TRP D C   1 
ATOM   6903  O  O   . TRP G  1 33  ? 158.915 -4.935  21.508  1.00 14.87 ? 32  TRP D O   1 
ATOM   6904  C  CB  . TRP G  1 33  ? 161.929 -6.022  20.641  1.00 15.45 ? 32  TRP D CB  1 
ATOM   6905  C  CG  . TRP G  1 33  ? 162.187 -4.516  20.712  1.00 18.48 ? 32  TRP D CG  1 
ATOM   6906  C  CD1 . TRP G  1 33  ? 162.377 -3.888  21.923  1.00 18.82 ? 32  TRP D CD1 1 
ATOM   6907  C  CD2 . TRP G  1 33  ? 162.245 -3.622  19.664  1.00 17.44 ? 32  TRP D CD2 1 
ATOM   6908  N  NE1 . TRP G  1 33  ? 162.539 -2.607  21.642  1.00 17.73 ? 32  TRP D NE1 1 
ATOM   6909  C  CE2 . TRP G  1 33  ? 162.461 -2.412  20.320  1.00 16.57 ? 32  TRP D CE2 1 
ATOM   6910  C  CE3 . TRP G  1 33  ? 162.138 -3.655  18.298  1.00 15.13 ? 32  TRP D CE3 1 
ATOM   6911  C  CZ2 . TRP G  1 33  ? 162.575 -1.224  19.636  1.00 17.30 ? 32  TRP D CZ2 1 
ATOM   6912  C  CZ3 . TRP G  1 33  ? 162.257 -2.461  17.614  1.00 17.25 ? 32  TRP D CZ3 1 
ATOM   6913  C  CH2 . TRP G  1 33  ? 162.467 -1.254  18.261  1.00 17.24 ? 32  TRP D CH2 1 
ATOM   6914  N  N   . GLY G  1 34  ? 159.603 -6.413  22.977  1.00 12.95 ? 33  GLY D N   1 
ATOM   6915  C  CA  . GLY G  1 34  ? 158.905 -5.719  24.055  1.00 13.25 ? 33  GLY D CA  1 
ATOM   6916  C  C   . GLY G  1 34  ? 158.678 -6.611  25.261  1.00 12.98 ? 33  GLY D C   1 
ATOM   6917  O  O   . GLY G  1 34  ? 159.389 -7.595  25.430  1.00 11.55 ? 33  GLY D O   1 
ATOM   6918  N  N   . SER G  1 35  ? 157.741 -6.320  26.141  1.00 13.08 ? 34  SER D N   1 
ATOM   6919  C  CA  . SER G  1 35  ? 157.420 -7.218  27.231  1.00 14.16 ? 34  SER D CA  1 
ATOM   6920  C  C   . SER G  1 35  ? 155.936 -7.220  27.352  1.00 14.13 ? 34  SER D C   1 
ATOM   6921  O  O   . SER G  1 35  ? 155.283 -6.200  27.106  1.00 16.82 ? 34  SER D O   1 
ATOM   6922  C  CB  . SER G  1 35  ? 157.912 -6.778  28.578  1.00 15.44 ? 34  SER D CB  1 
ATOM   6923  O  OG  . SER G  1 35  ? 159.320 -6.885  28.624  1.00 21.31 ? 34  SER D OG  1 
ATOM   6924  N  N   . ILE G  1 36  ? 155.408 -8.380  27.667  1.00 12.85 ? 35  ILE D N   1 
ATOM   6925  C  CA  . ILE G  1 36  ? 154.011 -8.511  27.974  1.00 11.57 ? 35  ILE D CA  1 
ATOM   6926  C  C   . ILE G  1 36  ? 154.099 -9.061  29.411  1.00 11.36 ? 35  ILE D C   1 
ATOM   6927  O  O   . ILE G  1 36  ? 155.021 -9.821  29.730  1.00 12.54 ? 35  ILE D O   1 
ATOM   6928  C  CB  . ILE G  1 36  ? 153.378 -9.485  26.953  1.00 10.64 ? 35  ILE D CB  1 
ATOM   6929  C  CG1 . ILE G  1 36  ? 153.741 -9.098  25.516  1.00 9.82  ? 35  ILE D CG1 1 
ATOM   6930  C  CG2 . ILE G  1 36  ? 151.858 -9.436  27.128  1.00 10.46 ? 35  ILE D CG2 1 
ATOM   6931  C  CD1 . ILE G  1 36  ? 153.333 -10.099 24.418  1.00 4.33  ? 35  ILE D CD1 1 
ATOM   6932  N  N   . LYS G  1 37  ? 153.255 -8.697  30.362  1.00 10.85 ? 36  LYS D N   1 
ATOM   6933  C  CA  . LYS G  1 37  ? 153.336 -9.253  31.693  1.00 9.73  ? 36  LYS D CA  1 
ATOM   6934  C  C   . LYS G  1 37  ? 151.941 -9.543  32.132  1.00 6.87  ? 36  LYS D C   1 
ATOM   6935  O  O   . LYS G  1 37  ? 150.952 -9.176  31.503  1.00 7.64  ? 36  LYS D O   1 
ATOM   6936  C  CB  . LYS G  1 37  ? 153.963 -8.317  32.728  1.00 12.97 ? 36  LYS D CB  1 
ATOM   6937  C  CG  . LYS G  1 37  ? 153.213 -7.078  33.208  1.00 20.78 ? 36  LYS D CG  1 
ATOM   6938  C  CD  . LYS G  1 37  ? 154.164 -6.249  34.095  1.00 25.65 ? 36  LYS D CD  1 
ATOM   6939  C  CE  . LYS G  1 37  ? 153.775 -4.757  34.353  1.00 27.52 ? 36  LYS D CE  1 
ATOM   6940  N  NZ  . LYS G  1 37  ? 152.536 -4.572  35.096  1.00 29.20 ? 36  LYS D NZ  1 
ATOM   6941  N  N   . GLY G  1 38  ? 151.907 -10.284 33.211  1.00 6.73  ? 37  GLY D N   1 
ATOM   6942  C  CA  . GLY G  1 38  ? 150.680 -10.725 33.812  1.00 6.10  ? 37  GLY D CA  1 
ATOM   6943  C  C   . GLY G  1 38  ? 150.292 -11.995 33.125  1.00 4.80  ? 37  GLY D C   1 
ATOM   6944  O  O   . GLY G  1 38  ? 149.147 -12.390 33.234  1.00 4.99  ? 37  GLY D O   1 
ATOM   6945  N  N   . LEU G  1 39  ? 151.178 -12.630 32.385  1.00 6.88  ? 38  LEU D N   1 
ATOM   6946  C  CA  . LEU G  1 39  ? 150.823 -13.859 31.676  1.00 11.76 ? 38  LEU D CA  1 
ATOM   6947  C  C   . LEU G  1 39  ? 150.938 -15.077 32.553  1.00 14.79 ? 38  LEU D C   1 
ATOM   6948  O  O   . LEU G  1 39  ? 151.520 -15.066 33.648  1.00 19.25 ? 38  LEU D O   1 
ATOM   6949  C  CB  . LEU G  1 39  ? 151.730 -14.176 30.478  1.00 10.16 ? 38  LEU D CB  1 
ATOM   6950  C  CG  . LEU G  1 39  ? 151.704 -13.488 29.107  1.00 8.63  ? 38  LEU D CG  1 
ATOM   6951  C  CD1 . LEU G  1 39  ? 150.321 -12.991 28.813  1.00 6.22  ? 38  LEU D CD1 1 
ATOM   6952  C  CD2 . LEU G  1 39  ? 152.661 -12.335 29.094  1.00 9.51  ? 38  LEU D CD2 1 
ATOM   6953  N  N   . THR G  1 40  ? 150.337 -16.169 32.137  1.00 16.14 ? 39  THR D N   1 
ATOM   6954  C  CA  . THR G  1 40  ? 150.742 -17.402 32.778  1.00 17.77 ? 39  THR D CA  1 
ATOM   6955  C  C   . THR G  1 40  ? 152.094 -17.750 32.144  1.00 17.75 ? 39  THR D C   1 
ATOM   6956  O  O   . THR G  1 40  ? 152.348 -17.306 31.011  1.00 16.01 ? 39  THR D O   1 
ATOM   6957  C  CB  . THR G  1 40  ? 149.677 -18.479 32.504  1.00 18.89 ? 39  THR D CB  1 
ATOM   6958  O  OG1 . THR G  1 40  ? 149.209 -18.267 31.176  1.00 22.60 ? 39  THR D OG1 1 
ATOM   6959  C  CG2 . THR G  1 40  ? 148.518 -18.409 33.450  1.00 18.58 ? 39  THR D CG2 1 
ATOM   6960  N  N   . GLU G  1 41  ? 152.934 -18.501 32.861  1.00 19.90 ? 40  GLU D N   1 
ATOM   6961  C  CA  . GLU G  1 41  ? 154.188 -19.085 32.375  1.00 20.58 ? 40  GLU D CA  1 
ATOM   6962  C  C   . GLU G  1 41  ? 153.896 -20.056 31.216  1.00 19.20 ? 40  GLU D C   1 
ATOM   6963  O  O   . GLU G  1 41  ? 152.925 -20.827 31.244  1.00 19.13 ? 40  GLU D O   1 
ATOM   6964  C  CB  . GLU G  1 41  ? 154.885 -19.845 33.521  1.00 25.16 ? 40  GLU D CB  1 
ATOM   6965  C  CG  . GLU G  1 41  ? 156.328 -20.284 33.212  1.00 31.23 ? 40  GLU D CG  1 
ATOM   6966  C  CD  . GLU G  1 41  ? 156.986 -21.391 34.059  1.00 33.37 ? 40  GLU D CD  1 
ATOM   6967  O  OE1 . GLU G  1 41  ? 156.884 -21.373 35.289  1.00 33.74 ? 40  GLU D OE1 1 
ATOM   6968  O  OE2 . GLU G  1 41  ? 157.622 -22.274 33.463  1.00 34.00 ? 40  GLU D OE2 1 
ATOM   6969  N  N   . GLY G  1 42  ? 154.687 -20.036 30.145  1.00 17.78 ? 41  GLY D N   1 
ATOM   6970  C  CA  . GLY G  1 42  ? 154.374 -20.874 29.015  1.00 16.66 ? 41  GLY D CA  1 
ATOM   6971  C  C   . GLY G  1 42  ? 154.241 -20.076 27.729  1.00 16.38 ? 41  GLY D C   1 
ATOM   6972  O  O   . GLY G  1 42  ? 154.631 -18.913 27.650  1.00 16.96 ? 41  GLY D O   1 
ATOM   6973  N  N   . LEU G  1 43  ? 153.641 -20.738 26.742  1.00 15.46 ? 42  LEU D N   1 
ATOM   6974  C  CA  . LEU G  1 43  ? 153.487 -20.281 25.377  1.00 13.39 ? 42  LEU D CA  1 
ATOM   6975  C  C   . LEU G  1 43  ? 152.191 -19.539 25.221  1.00 12.22 ? 42  LEU D C   1 
ATOM   6976  O  O   . LEU G  1 43  ? 151.171 -19.942 25.773  1.00 12.62 ? 42  LEU D O   1 
ATOM   6977  C  CB  . LEU G  1 43  ? 153.527 -21.511 24.458  1.00 12.42 ? 42  LEU D CB  1 
ATOM   6978  C  CG  . LEU G  1 43  ? 154.745 -21.680 23.542  1.00 11.17 ? 42  LEU D CG  1 
ATOM   6979  C  CD1 . LEU G  1 43  ? 155.992 -21.157 24.219  1.00 13.61 ? 42  LEU D CD1 1 
ATOM   6980  C  CD2 . LEU G  1 43  ? 154.926 -23.128 23.196  1.00 10.68 ? 42  LEU D CD2 1 
ATOM   6981  N  N   . HIS G  1 44  ? 152.237 -18.429 24.495  1.00 12.63 ? 43  HIS D N   1 
ATOM   6982  C  CA  . HIS G  1 44  ? 151.096 -17.569 24.239  1.00 8.64  ? 43  HIS D CA  1 
ATOM   6983  C  C   . HIS G  1 44  ? 151.020 -17.208 22.765  1.00 7.38  ? 43  HIS D C   1 
ATOM   6984  O  O   . HIS G  1 44  ? 152.000 -16.687 22.226  1.00 5.10  ? 43  HIS D O   1 
ATOM   6985  C  CB  . HIS G  1 44  ? 151.269 -16.356 25.097  1.00 9.36  ? 43  HIS D CB  1 
ATOM   6986  C  CG  . HIS G  1 44  ? 150.956 -16.726 26.525  1.00 12.24 ? 43  HIS D CG  1 
ATOM   6987  N  ND1 . HIS G  1 44  ? 151.736 -16.748 27.610  1.00 13.29 ? 43  HIS D ND1 1 
ATOM   6988  C  CD2 . HIS G  1 44  ? 149.719 -17.218 26.881  1.00 12.12 ? 43  HIS D CD2 1 
ATOM   6989  C  CE1 . HIS G  1 44  ? 151.000 -17.244 28.578  1.00 11.58 ? 43  HIS D CE1 1 
ATOM   6990  N  NE2 . HIS G  1 44  ? 149.798 -17.523 28.140  1.00 12.43 ? 43  HIS D NE2 1 
ATOM   6991  N  N   . GLY G  1 45  ? 149.936 -17.569 22.079  1.00 5.72  ? 44  GLY D N   1 
ATOM   6992  C  CA  . GLY G  1 45  ? 149.762 -17.171 20.698  1.00 8.32  ? 44  GLY D CA  1 
ATOM   6993  C  C   . GLY G  1 45  ? 149.890 -15.649 20.577  1.00 11.61 ? 44  GLY D C   1 
ATOM   6994  O  O   . GLY G  1 45  ? 149.396 -14.920 21.448  1.00 11.07 ? 44  GLY D O   1 
ATOM   6995  N  N   . PHE G  1 46  ? 150.584 -15.183 19.535  1.00 10.32 ? 45  PHE D N   1 
ATOM   6996  C  CA  . PHE G  1 46  ? 150.841 -13.778 19.298  1.00 8.51  ? 45  PHE D CA  1 
ATOM   6997  C  C   . PHE G  1 46  ? 150.517 -13.487 17.826  1.00 10.49 ? 45  PHE D C   1 
ATOM   6998  O  O   . PHE G  1 46  ? 151.206 -13.993 16.924  1.00 10.82 ? 45  PHE D O   1 
ATOM   6999  C  CB  . PHE G  1 46  ? 152.295 -13.577 19.637  1.00 7.55  ? 45  PHE D CB  1 
ATOM   7000  C  CG  . PHE G  1 46  ? 152.825 -12.157 19.724  1.00 6.05  ? 45  PHE D CG  1 
ATOM   7001  C  CD1 . PHE G  1 46  ? 152.248 -11.222 20.541  1.00 4.01  ? 45  PHE D CD1 1 
ATOM   7002  C  CD2 . PHE G  1 46  ? 153.960 -11.836 19.031  1.00 6.81  ? 45  PHE D CD2 1 
ATOM   7003  C  CE1 . PHE G  1 46  ? 152.798 -9.963  20.642  1.00 3.85  ? 45  PHE D CE1 1 
ATOM   7004  C  CE2 . PHE G  1 46  ? 154.494 -10.577 19.142  1.00 4.35  ? 45  PHE D CE2 1 
ATOM   7005  C  CZ  . PHE G  1 46  ? 153.927 -9.641  19.960  1.00 2.58  ? 45  PHE D CZ  1 
ATOM   7006  N  N   . HIS G  1 47  ? 149.469 -12.710 17.478  1.00 10.42 ? 46  HIS D N   1 
ATOM   7007  C  CA  . HIS G  1 47  ? 149.074 -12.484 16.097  1.00 7.99  ? 46  HIS D CA  1 
ATOM   7008  C  C   . HIS G  1 47  ? 148.759 -11.029 15.830  1.00 8.79  ? 46  HIS D C   1 
ATOM   7009  O  O   . HIS G  1 47  ? 148.672 -10.252 16.777  1.00 10.12 ? 46  HIS D O   1 
ATOM   7010  C  CB  . HIS G  1 47  ? 147.837 -13.287 15.748  1.00 9.98  ? 46  HIS D CB  1 
ATOM   7011  C  CG  . HIS G  1 47  ? 147.885 -14.729 16.198  1.00 10.66 ? 46  HIS D CG  1 
ATOM   7012  N  ND1 . HIS G  1 47  ? 147.054 -15.332 17.028  1.00 16.02 ? 46  HIS D ND1 1 
ATOM   7013  C  CD2 . HIS G  1 47  ? 148.890 -15.602 15.906  1.00 12.69 ? 46  HIS D CD2 1 
ATOM   7014  C  CE1 . HIS G  1 47  ? 147.535 -16.525 17.268  1.00 15.63 ? 46  HIS D CE1 1 
ATOM   7015  N  NE2 . HIS G  1 47  ? 148.647 -16.679 16.594  1.00 15.15 ? 46  HIS D NE2 1 
ATOM   7016  N  N   . VAL G  1 48  ? 148.622 -10.603 14.569  1.00 7.51  ? 47  VAL D N   1 
ATOM   7017  C  CA  . VAL G  1 48  ? 148.152 -9.283  14.211  1.00 6.95  ? 47  VAL D CA  1 
ATOM   7018  C  C   . VAL G  1 48  ? 146.839 -9.669  13.608  1.00 7.81  ? 47  VAL D C   1 
ATOM   7019  O  O   . VAL G  1 48  ? 146.765 -10.504 12.706  1.00 12.77 ? 47  VAL D O   1 
ATOM   7020  C  CB  . VAL G  1 48  ? 148.888 -8.560  13.097  1.00 7.53  ? 47  VAL D CB  1 
ATOM   7021  C  CG1 . VAL G  1 48  ? 148.167 -7.263  12.771  1.00 7.88  ? 47  VAL D CG1 1 
ATOM   7022  C  CG2 . VAL G  1 48  ? 150.281 -8.229  13.532  1.00 10.71 ? 47  VAL D CG2 1 
ATOM   7023  N  N   . HIS G  1 49  ? 145.790 -9.138  14.162  1.00 7.54  ? 48  HIS D N   1 
ATOM   7024  C  CA  . HIS G  1 49  ? 144.459 -9.366  13.696  1.00 5.30  ? 48  HIS D CA  1 
ATOM   7025  C  C   . HIS G  1 49  ? 144.189 -8.161  12.824  1.00 7.09  ? 48  HIS D C   1 
ATOM   7026  O  O   . HIS G  1 49  ? 144.890 -7.132  12.892  1.00 10.27 ? 48  HIS D O   1 
ATOM   7027  C  CB  . HIS G  1 49  ? 143.538 -9.443  14.885  1.00 3.49  ? 48  HIS D CB  1 
ATOM   7028  C  CG  . HIS G  1 49  ? 143.581 -10.786 15.594  1.00 2.00  ? 48  HIS D CG  1 
ATOM   7029  N  ND1 . HIS G  1 49  ? 142.571 -11.613 15.773  1.00 2.00  ? 48  HIS D ND1 1 
ATOM   7030  C  CD2 . HIS G  1 49  ? 144.699 -11.356 16.163  1.00 2.00  ? 48  HIS D CD2 1 
ATOM   7031  C  CE1 . HIS G  1 49  ? 143.060 -12.646 16.426  1.00 3.05  ? 48  HIS D CE1 1 
ATOM   7032  N  NE2 . HIS G  1 49  ? 144.361 -12.510 16.671  1.00 5.42  ? 48  HIS D NE2 1 
ATOM   7033  N  N   . GLU G  1 50  ? 143.129 -8.278  12.048  1.00 5.07  ? 49  GLU D N   1 
ATOM   7034  C  CA  . GLU G  1 50  ? 142.845 -7.376  10.986  1.00 4.22  ? 49  GLU D CA  1 
ATOM   7035  C  C   . GLU G  1 50  ? 142.370 -5.982  11.273  1.00 5.76  ? 49  GLU D C   1 
ATOM   7036  O  O   . GLU G  1 50  ? 142.843 -5.069  10.614  1.00 10.54 ? 49  GLU D O   1 
ATOM   7037  C  CB  . GLU G  1 50  ? 141.850 -8.068  10.076  1.00 5.05  ? 49  GLU D CB  1 
ATOM   7038  C  CG  . GLU G  1 50  ? 141.958 -7.525  8.639   1.00 3.59  ? 49  GLU D CG  1 
ATOM   7039  C  CD  . GLU G  1 50  ? 140.784 -7.749  7.714   1.00 2.00  ? 49  GLU D CD  1 
ATOM   7040  O  OE1 . GLU G  1 50  ? 139.857 -8.463  8.016   1.00 2.00  ? 49  GLU D OE1 1 
ATOM   7041  O  OE2 . GLU G  1 50  ? 140.773 -7.159  6.655   1.00 9.57  ? 49  GLU D OE2 1 
ATOM   7042  N  N   . PHE G  1 51  ? 141.417 -5.708  12.143  1.00 6.59  ? 50  PHE D N   1 
ATOM   7043  C  CA  . PHE G  1 51  ? 140.878 -4.366  12.318  1.00 6.16  ? 50  PHE D CA  1 
ATOM   7044  C  C   . PHE G  1 51  ? 141.427 -3.747  13.559  1.00 7.86  ? 50  PHE D C   1 
ATOM   7045  O  O   . PHE G  1 51  ? 141.497 -4.392  14.604  1.00 7.80  ? 50  PHE D O   1 
ATOM   7046  C  CB  . PHE G  1 51  ? 139.378 -4.366  12.470  1.00 4.55  ? 50  PHE D CB  1 
ATOM   7047  C  CG  . PHE G  1 51  ? 138.808 -5.100  11.296  1.00 6.84  ? 50  PHE D CG  1 
ATOM   7048  C  CD1 . PHE G  1 51  ? 138.974 -4.582  10.025  1.00 8.88  ? 50  PHE D CD1 1 
ATOM   7049  C  CD2 . PHE G  1 51  ? 138.156 -6.289  11.506  1.00 5.83  ? 50  PHE D CD2 1 
ATOM   7050  C  CE1 . PHE G  1 51  ? 138.481 -5.289  8.949   1.00 9.98  ? 50  PHE D CE1 1 
ATOM   7051  C  CE2 . PHE G  1 51  ? 137.662 -6.988  10.437  1.00 5.12  ? 50  PHE D CE2 1 
ATOM   7052  C  CZ  . PHE G  1 51  ? 137.820 -6.494  9.164   1.00 8.08  ? 50  PHE D CZ  1 
ATOM   7053  N  N   . GLY G  1 52  ? 141.744 -2.471  13.501  1.00 8.51  ? 51  GLY D N   1 
ATOM   7054  C  CA  . GLY G  1 52  ? 142.210 -1.792  14.661  1.00 7.61  ? 51  GLY D CA  1 
ATOM   7055  C  C   . GLY G  1 52  ? 140.977 -1.229  15.260  1.00 8.22  ? 51  GLY D C   1 
ATOM   7056  O  O   . GLY G  1 52  ? 140.894 -0.029  15.471  1.00 11.94 ? 51  GLY D O   1 
ATOM   7057  N  N   . ASP G  1 53  ? 140.031 -2.088  15.566  1.00 8.84  ? 52  ASP D N   1 
ATOM   7058  C  CA  . ASP G  1 53  ? 138.747 -1.697  16.096  1.00 10.62 ? 52  ASP D CA  1 
ATOM   7059  C  C   . ASP G  1 53  ? 138.607 -2.422  17.419  1.00 11.20 ? 52  ASP D C   1 
ATOM   7060  O  O   . ASP G  1 53  ? 138.486 -3.646  17.516  1.00 11.08 ? 52  ASP D O   1 
ATOM   7061  C  CB  . ASP G  1 53  ? 137.679 -2.095  15.065  1.00 11.59 ? 52  ASP D CB  1 
ATOM   7062  C  CG  . ASP G  1 53  ? 136.204 -2.048  15.453  1.00 14.97 ? 52  ASP D CG  1 
ATOM   7063  O  OD1 . ASP G  1 53  ? 135.865 -1.681  16.575  1.00 9.64  ? 52  ASP D OD1 1 
ATOM   7064  O  OD2 . ASP G  1 53  ? 135.374 -2.436  14.620  1.00 21.89 ? 52  ASP D OD2 1 
ATOM   7065  N  N   . ASN G  1 54  ? 138.571 -1.533  18.395  1.00 10.62 ? 53  ASN D N   1 
ATOM   7066  C  CA  . ASN G  1 54  ? 138.549 -1.837  19.806  1.00 10.61 ? 53  ASN D CA  1 
ATOM   7067  C  C   . ASN G  1 54  ? 137.238 -1.489  20.510  1.00 10.78 ? 53  ASN D C   1 
ATOM   7068  O  O   . ASN G  1 54  ? 137.160 -1.342  21.741  1.00 9.75  ? 53  ASN D O   1 
ATOM   7069  C  CB  . ASN G  1 54  ? 139.702 -1.069  20.363  1.00 16.15 ? 53  ASN D CB  1 
ATOM   7070  C  CG  . ASN G  1 54  ? 140.551 -1.876  21.310  1.00 23.95 ? 53  ASN D CG  1 
ATOM   7071  O  OD1 . ASN G  1 54  ? 140.549 -1.627  22.524  1.00 24.83 ? 53  ASN D OD1 1 
ATOM   7072  N  ND2 . ASN G  1 54  ? 141.307 -2.830  20.730  1.00 24.84 ? 53  ASN D ND2 1 
ATOM   7073  N  N   . THR G  1 55  ? 136.161 -1.314  19.733  1.00 8.67  ? 54  THR D N   1 
ATOM   7074  C  CA  . THR G  1 55  ? 134.907 -0.944  20.334  1.00 7.85  ? 54  THR D CA  1 
ATOM   7075  C  C   . THR G  1 55  ? 134.391 -2.110  21.147  1.00 10.58 ? 54  THR D C   1 
ATOM   7076  O  O   . THR G  1 55  ? 134.028 -1.869  22.296  1.00 12.89 ? 54  THR D O   1 
ATOM   7077  C  CB  . THR G  1 55  ? 133.945 -0.492  19.216  1.00 6.86  ? 54  THR D CB  1 
ATOM   7078  O  OG1 . THR G  1 55  ? 133.766 -1.506  18.237  1.00 7.52  ? 54  THR D OG1 1 
ATOM   7079  C  CG2 . THR G  1 55  ? 134.549 0.743   18.524  1.00 4.19  ? 54  THR D CG2 1 
ATOM   7080  N  N   . ALA G  1 56  ? 134.384 -3.372  20.670  1.00 10.36 ? 55  ALA D N   1 
ATOM   7081  C  CA  . ALA G  1 56  ? 134.006 -4.510  21.511  1.00 8.13  ? 55  ALA D CA  1 
ATOM   7082  C  C   . ALA G  1 56  ? 135.222 -5.187  22.161  1.00 8.97  ? 55  ALA D C   1 
ATOM   7083  O  O   . ALA G  1 56  ? 135.376 -6.423  22.159  1.00 10.12 ? 55  ALA D O   1 
ATOM   7084  C  CB  . ALA G  1 56  ? 133.253 -5.544  20.681  1.00 7.26  ? 55  ALA D CB  1 
ATOM   7085  N  N   . GLY G  1 57  ? 136.146 -4.449  22.768  1.00 10.13 ? 56  GLY D N   1 
ATOM   7086  C  CA  . GLY G  1 57  ? 137.284 -5.068  23.450  1.00 11.68 ? 56  GLY D CA  1 
ATOM   7087  C  C   . GLY G  1 57  ? 138.222 -5.722  22.449  1.00 12.44 ? 56  GLY D C   1 
ATOM   7088  O  O   . GLY G  1 57  ? 138.614 -5.063  21.476  1.00 16.10 ? 56  GLY D O   1 
ATOM   7089  N  N   . CYS G  1 58  ? 138.586 -6.992  22.567  1.00 11.07 ? 57  CYS D N   1 
ATOM   7090  C  CA  . CYS G  1 58  ? 139.466 -7.544  21.528  1.00 10.77 ? 57  CYS D CA  1 
ATOM   7091  C  C   . CYS G  1 58  ? 138.765 -8.288  20.423  1.00 9.21  ? 57  CYS D C   1 
ATOM   7092  O  O   . CYS G  1 58  ? 139.340 -8.565  19.365  1.00 9.60  ? 57  CYS D O   1 
ATOM   7093  C  CB  . CYS G  1 58  ? 140.499 -8.516  22.072  1.00 7.90  ? 57  CYS D CB  1 
ATOM   7094  S  SG  . CYS G  1 58  ? 141.577 -7.665  23.212  1.00 7.32  ? 57  CYS D SG  1 
ATOM   7095  N  N   . THR G  1 59  ? 137.488 -8.562  20.650  1.00 8.26  ? 58  THR D N   1 
ATOM   7096  C  CA  . THR G  1 59  ? 136.745 -9.379  19.734  1.00 9.10  ? 58  THR D CA  1 
ATOM   7097  C  C   . THR G  1 59  ? 136.536 -8.716  18.373  1.00 7.92  ? 58  THR D C   1 
ATOM   7098  O  O   . THR G  1 59  ? 136.596 -9.364  17.327  1.00 8.03  ? 58  THR D O   1 
ATOM   7099  C  CB  . THR G  1 59  ? 135.424 -9.693  20.462  1.00 9.20  ? 58  THR D CB  1 
ATOM   7100  O  OG1 . THR G  1 59  ? 135.749 -10.315 21.709  1.00 11.73 ? 58  THR D OG1 1 
ATOM   7101  C  CG2 . THR G  1 59  ? 134.576 -10.676 19.667  1.00 13.19 ? 58  THR D CG2 1 
ATOM   7102  N  N   . SER G  1 60  ? 136.373 -7.399  18.364  1.00 9.64  ? 59  SER D N   1 
ATOM   7103  C  CA  . SER G  1 60  ? 136.082 -6.675  17.147  1.00 9.07  ? 59  SER D CA  1 
ATOM   7104  C  C   . SER G  1 60  ? 137.295 -6.477  16.246  1.00 9.06  ? 59  SER D C   1 
ATOM   7105  O  O   . SER G  1 60  ? 137.171 -5.856  15.191  1.00 12.39 ? 59  SER D O   1 
ATOM   7106  C  CB  . SER G  1 60  ? 135.443 -5.378  17.586  1.00 9.72  ? 59  SER D CB  1 
ATOM   7107  O  OG  . SER G  1 60  ? 136.210 -4.684  18.572  1.00 10.09 ? 59  SER D OG  1 
ATOM   7108  N  N   . ALA G  1 61  ? 138.473 -6.976  16.635  1.00 7.95  ? 60  ALA D N   1 
ATOM   7109  C  CA  . ALA G  1 61  ? 139.654 -6.913  15.790  1.00 7.28  ? 60  ALA D CA  1 
ATOM   7110  C  C   . ALA G  1 61  ? 139.556 -7.878  14.602  1.00 5.03  ? 60  ALA D C   1 
ATOM   7111  O  O   . ALA G  1 61  ? 140.407 -7.850  13.737  1.00 4.07  ? 60  ALA D O   1 
ATOM   7112  C  CB  . ALA G  1 61  ? 140.892 -7.247  16.640  1.00 6.42  ? 60  ALA D CB  1 
ATOM   7113  N  N   . GLY G  1 62  ? 138.616 -8.819  14.507  1.00 6.34  ? 61  GLY D N   1 
ATOM   7114  C  CA  . GLY G  1 62  ? 138.460 -9.653  13.340  1.00 3.97  ? 61  GLY D CA  1 
ATOM   7115  C  C   . GLY G  1 62  ? 139.352 -10.879 13.377  1.00 6.70  ? 61  GLY D C   1 
ATOM   7116  O  O   . GLY G  1 62  ? 139.933 -11.294 14.391  1.00 7.41  ? 61  GLY D O   1 
ATOM   7117  N  N   . PRO G  1 63  ? 139.536 -11.510 12.232  1.00 8.43  ? 62  PRO D N   1 
ATOM   7118  C  CA  . PRO G  1 63  ? 140.347 -12.696 12.111  1.00 7.85  ? 62  PRO D CA  1 
ATOM   7119  C  C   . PRO G  1 63  ? 141.815 -12.327 12.097  1.00 9.09  ? 62  PRO D C   1 
ATOM   7120  O  O   . PRO G  1 63  ? 142.167 -11.141 12.123  1.00 7.00  ? 62  PRO D O   1 
ATOM   7121  C  CB  . PRO G  1 63  ? 139.815 -13.270 10.834  1.00 9.53  ? 62  PRO D CB  1 
ATOM   7122  C  CG  . PRO G  1 63  ? 139.658 -12.034 9.973   1.00 9.14  ? 62  PRO D CG  1 
ATOM   7123  C  CD  . PRO G  1 63  ? 138.952 -11.115 10.942  1.00 9.56  ? 62  PRO D CD  1 
ATOM   7124  N  N   . HIS G  1 64  ? 142.696 -13.335 12.001  1.00 10.43 ? 63  HIS D N   1 
ATOM   7125  C  CA  . HIS G  1 64  ? 144.096 -13.026 11.785  1.00 9.97  ? 63  HIS D CA  1 
ATOM   7126  C  C   . HIS G  1 64  ? 144.236 -12.264 10.459  1.00 7.60  ? 63  HIS D C   1 
ATOM   7127  O  O   . HIS G  1 64  ? 143.424 -12.367 9.545   1.00 4.34  ? 63  HIS D O   1 
ATOM   7128  C  CB  . HIS G  1 64  ? 144.887 -14.320 11.759  1.00 13.26 ? 63  HIS D CB  1 
ATOM   7129  C  CG  . HIS G  1 64  ? 145.079 -15.020 13.103  1.00 18.34 ? 63  HIS D CG  1 
ATOM   7130  N  ND1 . HIS G  1 64  ? 145.433 -16.286 13.307  1.00 19.65 ? 63  HIS D ND1 1 
ATOM   7131  C  CD2 . HIS G  1 64  ? 144.933 -14.401 14.330  1.00 20.73 ? 63  HIS D CD2 1 
ATOM   7132  C  CE1 . HIS G  1 64  ? 145.484 -16.366 14.648  1.00 21.01 ? 63  HIS D CE1 1 
ATOM   7133  N  NE2 . HIS G  1 64  ? 145.192 -15.240 15.307  1.00 23.02 ? 63  HIS D NE2 1 
ATOM   7134  N  N   . PHE G  1 65  ? 145.247 -11.429 10.334  1.00 9.50  ? 64  PHE D N   1 
ATOM   7135  C  CA  . PHE G  1 65  ? 145.474 -10.600 9.165   1.00 9.46  ? 64  PHE D CA  1 
ATOM   7136  C  C   . PHE G  1 65  ? 145.963 -11.511 8.061   1.00 10.60 ? 64  PHE D C   1 
ATOM   7137  O  O   . PHE G  1 65  ? 147.058 -12.079 8.191   1.00 10.36 ? 64  PHE D O   1 
ATOM   7138  C  CB  . PHE G  1 65  ? 146.518 -9.545  9.514   1.00 5.72  ? 64  PHE D CB  1 
ATOM   7139  C  CG  . PHE G  1 65  ? 146.789 -8.600  8.378   1.00 5.14  ? 64  PHE D CG  1 
ATOM   7140  C  CD1 . PHE G  1 65  ? 145.756 -8.183  7.569   1.00 6.28  ? 64  PHE D CD1 1 
ATOM   7141  C  CD2 . PHE G  1 65  ? 148.080 -8.177  8.162   1.00 5.57  ? 64  PHE D CD2 1 
ATOM   7142  C  CE1 . PHE G  1 65  ? 146.033 -7.317  6.539   1.00 7.89  ? 64  PHE D CE1 1 
ATOM   7143  C  CE2 . PHE G  1 65  ? 148.359 -7.311  7.138   1.00 6.89  ? 64  PHE D CE2 1 
ATOM   7144  C  CZ  . PHE G  1 65  ? 147.331 -6.889  6.324   1.00 9.50  ? 64  PHE D CZ  1 
ATOM   7145  N  N   . ASN G  1 66  ? 145.173 -11.589 6.980   1.00 10.72 ? 65  ASN D N   1 
ATOM   7146  C  CA  . ASN G  1 66  ? 145.416 -12.537 5.906   1.00 12.40 ? 65  ASN D CA  1 
ATOM   7147  C  C   . ASN G  1 66  ? 145.178 -11.984 4.487   1.00 15.69 ? 65  ASN D C   1 
ATOM   7148  O  O   . ASN G  1 66  ? 144.194 -12.415 3.866   1.00 16.93 ? 65  ASN D O   1 
ATOM   7149  C  CB  . ASN G  1 66  ? 144.499 -13.734 6.188   1.00 12.63 ? 65  ASN D CB  1 
ATOM   7150  C  CG  . ASN G  1 66  ? 144.806 -15.013 5.426   1.00 14.06 ? 65  ASN D CG  1 
ATOM   7151  O  OD1 . ASN G  1 66  ? 145.805 -15.125 4.712   1.00 15.64 ? 65  ASN D OD1 1 
ATOM   7152  N  ND2 . ASN G  1 66  ? 144.009 -16.058 5.594   1.00 12.14 ? 65  ASN D ND2 1 
ATOM   7153  N  N   . PRO G  1 67  ? 145.918 -11.046 3.849   1.00 14.92 ? 66  PRO D N   1 
ATOM   7154  C  CA  . PRO G  1 67  ? 145.603 -10.549 2.511   1.00 15.66 ? 66  PRO D CA  1 
ATOM   7155  C  C   . PRO G  1 67  ? 145.781 -11.539 1.368   1.00 17.30 ? 66  PRO D C   1 
ATOM   7156  O  O   . PRO G  1 67  ? 145.283 -11.388 0.244   1.00 15.84 ? 66  PRO D O   1 
ATOM   7157  C  CB  . PRO G  1 67  ? 146.472 -9.294  2.380   1.00 13.90 ? 66  PRO D CB  1 
ATOM   7158  C  CG  . PRO G  1 67  ? 147.632 -9.544  3.299   1.00 11.47 ? 66  PRO D CG  1 
ATOM   7159  C  CD  . PRO G  1 67  ? 146.906 -10.181 4.464   1.00 15.01 ? 66  PRO D CD  1 
ATOM   7160  N  N   . LEU G  1 68  ? 146.579 -12.531 1.742   1.00 19.27 ? 67  LEU D N   1 
ATOM   7161  C  CA  . LEU G  1 68  ? 146.909 -13.515 0.756   1.00 22.27 ? 67  LEU D CA  1 
ATOM   7162  C  C   . LEU G  1 68  ? 146.117 -14.779 0.935   1.00 23.03 ? 67  LEU D C   1 
ATOM   7163  O  O   . LEU G  1 68  ? 146.588 -15.778 0.406   1.00 26.92 ? 67  LEU D O   1 
ATOM   7164  C  CB  . LEU G  1 68  ? 148.367 -13.906 0.816   1.00 20.24 ? 67  LEU D CB  1 
ATOM   7165  C  CG  . LEU G  1 68  ? 149.488 -12.905 0.679   1.00 18.59 ? 67  LEU D CG  1 
ATOM   7166  C  CD1 . LEU G  1 68  ? 150.714 -13.763 0.443   1.00 19.70 ? 67  LEU D CD1 1 
ATOM   7167  C  CD2 . LEU G  1 68  ? 149.324 -11.926 -0.462  1.00 18.72 ? 67  LEU D CD2 1 
ATOM   7168  N  N   . SER G  1 69  ? 144.949 -14.753 1.577   1.00 24.72 ? 68  SER D N   1 
ATOM   7169  C  CA  . SER G  1 69  ? 144.074 -15.913 1.788   1.00 27.28 ? 68  SER D CA  1 
ATOM   7170  C  C   . SER G  1 69  ? 144.768 -17.271 1.895   1.00 27.36 ? 68  SER D C   1 
ATOM   7171  O  O   . SER G  1 69  ? 144.737 -18.113 0.996   1.00 27.72 ? 68  SER D O   1 
ATOM   7172  C  CB  . SER G  1 69  ? 143.036 -15.916 0.655   1.00 28.85 ? 68  SER D CB  1 
ATOM   7173  O  OG  . SER G  1 69  ? 142.239 -14.731 0.725   1.00 30.51 ? 68  SER D OG  1 
ATOM   7174  N  N   . ARG G  1 70  ? 145.455 -17.402 3.032   1.00 26.70 ? 69  ARG D N   1 
ATOM   7175  C  CA  . ARG G  1 70  ? 146.267 -18.567 3.312   1.00 24.23 ? 69  ARG D CA  1 
ATOM   7176  C  C   . ARG G  1 70  ? 145.928 -19.198 4.642   1.00 22.19 ? 69  ARG D C   1 
ATOM   7177  O  O   . ARG G  1 70  ? 145.141 -18.643 5.404   1.00 23.97 ? 69  ARG D O   1 
ATOM   7178  C  CB  . ARG G  1 70  ? 147.742 -18.158 3.282   1.00 25.27 ? 69  ARG D CB  1 
ATOM   7179  C  CG  . ARG G  1 70  ? 148.235 -18.221 1.850   1.00 26.86 ? 69  ARG D CG  1 
ATOM   7180  C  CD  . ARG G  1 70  ? 149.684 -17.800 1.713   1.00 26.93 ? 69  ARG D CD  1 
ATOM   7181  N  NE  . ARG G  1 70  ? 150.481 -18.853 1.177   1.00 27.34 ? 69  ARG D NE  1 
ATOM   7182  C  CZ  . ARG G  1 70  ? 151.806 -18.818 1.086   1.00 28.91 ? 69  ARG D CZ  1 
ATOM   7183  N  NH1 . ARG G  1 70  ? 152.602 -17.813 1.462   1.00 29.45 ? 69  ARG D NH1 1 
ATOM   7184  N  NH2 . ARG G  1 70  ? 152.377 -20.021 0.858   1.00 31.28 ? 69  ARG D NH2 1 
ATOM   7185  N  N   . LYS G  1 71  ? 146.457 -20.356 4.982   1.00 18.93 ? 70  LYS D N   1 
ATOM   7186  C  CA  . LYS G  1 71  ? 146.130 -20.956 6.251   1.00 18.30 ? 70  LYS D CA  1 
ATOM   7187  C  C   . LYS G  1 71  ? 146.997 -20.339 7.308   1.00 17.09 ? 70  LYS D C   1 
ATOM   7188  O  O   . LYS G  1 71  ? 147.923 -19.563 7.068   1.00 17.78 ? 70  LYS D O   1 
ATOM   7189  C  CB  . LYS G  1 71  ? 146.358 -22.473 6.234   1.00 19.07 ? 70  LYS D CB  1 
ATOM   7190  C  CG  . LYS G  1 71  ? 145.311 -23.136 5.356   1.00 20.15 ? 70  LYS D CG  1 
ATOM   7191  C  CD  . LYS G  1 71  ? 145.345 -24.649 5.416   1.00 22.39 ? 70  LYS D CD  1 
ATOM   7192  C  CE  . LYS G  1 71  ? 144.224 -25.232 4.541   1.00 25.79 ? 70  LYS D CE  1 
ATOM   7193  N  NZ  . LYS G  1 71  ? 142.889 -24.870 5.004   1.00 29.29 ? 70  LYS D NZ  1 
ATOM   7194  N  N   . HIS G  1 72  ? 146.643 -20.677 8.514   1.00 15.33 ? 71  HIS D N   1 
ATOM   7195  C  CA  . HIS G  1 72  ? 147.389 -20.225 9.627   1.00 12.52 ? 71  HIS D CA  1 
ATOM   7196  C  C   . HIS G  1 72  ? 148.630 -21.055 9.785   1.00 12.32 ? 71  HIS D C   1 
ATOM   7197  O  O   . HIS G  1 72  ? 148.568 -22.282 9.831   1.00 15.71 ? 71  HIS D O   1 
ATOM   7198  C  CB  . HIS G  1 72  ? 146.491 -20.329 10.798  1.00 10.92 ? 71  HIS D CB  1 
ATOM   7199  C  CG  . HIS G  1 72  ? 147.222 -19.953 12.043  1.00 7.90  ? 71  HIS D CG  1 
ATOM   7200  N  ND1 . HIS G  1 72  ? 147.584 -18.747 12.365  1.00 7.73  ? 71  HIS D ND1 1 
ATOM   7201  C  CD2 . HIS G  1 72  ? 147.657 -20.852 12.971  1.00 7.64  ? 71  HIS D CD2 1 
ATOM   7202  C  CE1 . HIS G  1 72  ? 148.237 -18.887 13.479  1.00 8.57  ? 71  HIS D CE1 1 
ATOM   7203  N  NE2 . HIS G  1 72  ? 148.283 -20.145 13.832  1.00 6.54  ? 71  HIS D NE2 1 
ATOM   7204  N  N   . GLY G  1 73  ? 149.747 -20.392 9.922   1.00 11.57 ? 72  GLY D N   1 
ATOM   7205  C  CA  . GLY G  1 73  ? 150.973 -21.108 10.146  1.00 11.82 ? 72  GLY D CA  1 
ATOM   7206  C  C   . GLY G  1 73  ? 151.704 -20.397 11.243  1.00 12.45 ? 72  GLY D C   1 
ATOM   7207  O  O   . GLY G  1 73  ? 151.144 -19.656 12.074  1.00 14.07 ? 72  GLY D O   1 
ATOM   7208  N  N   . GLY G  1 74  ? 152.995 -20.638 11.227  1.00 13.87 ? 73  GLY D N   1 
ATOM   7209  C  CA  . GLY G  1 74  ? 153.903 -20.012 12.170  1.00 15.45 ? 73  GLY D CA  1 
ATOM   7210  C  C   . GLY G  1 74  ? 154.730 -19.019 11.376  1.00 17.11 ? 73  GLY D C   1 
ATOM   7211  O  O   . GLY G  1 74  ? 154.777 -19.172 10.152  1.00 17.92 ? 73  GLY D O   1 
ATOM   7212  N  N   . PRO G  1 75  ? 155.459 -18.055 11.932  1.00 17.37 ? 74  PRO D N   1 
ATOM   7213  C  CA  . PRO G  1 75  ? 156.122 -16.994 11.163  1.00 20.49 ? 74  PRO D CA  1 
ATOM   7214  C  C   . PRO G  1 75  ? 157.138 -17.429 10.087  1.00 24.30 ? 74  PRO D C   1 
ATOM   7215  O  O   . PRO G  1 75  ? 157.539 -16.648 9.204   1.00 25.83 ? 74  PRO D O   1 
ATOM   7216  C  CB  . PRO G  1 75  ? 156.747 -16.125 12.223  1.00 18.19 ? 74  PRO D CB  1 
ATOM   7217  C  CG  . PRO G  1 75  ? 157.019 -17.094 13.350  1.00 17.30 ? 74  PRO D CG  1 
ATOM   7218  C  CD  . PRO G  1 75  ? 155.816 -18.015 13.334  1.00 16.41 ? 74  PRO D CD  1 
ATOM   7219  N  N   . LYS G  1 76  ? 157.583 -18.697 10.211  1.00 24.48 ? 75  LYS D N   1 
ATOM   7220  C  CA  . LYS G  1 76  ? 158.617 -19.282 9.365   1.00 24.99 ? 75  LYS D CA  1 
ATOM   7221  C  C   . LYS G  1 76  ? 158.087 -20.345 8.441   1.00 25.46 ? 75  LYS D C   1 
ATOM   7222  O  O   . LYS G  1 76  ? 158.826 -20.944 7.667   1.00 26.16 ? 75  LYS D O   1 
ATOM   7223  C  CB  . LYS G  1 76  ? 159.724 -19.883 10.225  1.00 26.27 ? 75  LYS D CB  1 
ATOM   7224  C  CG  . LYS G  1 76  ? 160.247 -18.751 11.080  1.00 26.71 ? 75  LYS D CG  1 
ATOM   7225  C  CD  . LYS G  1 76  ? 161.585 -18.865 11.755  1.00 28.60 ? 75  LYS D CD  1 
ATOM   7226  C  CE  . LYS G  1 76  ? 161.869 -17.463 12.293  1.00 30.11 ? 75  LYS D CE  1 
ATOM   7227  N  NZ  . LYS G  1 76  ? 161.784 -16.461 11.234  1.00 29.95 ? 75  LYS D NZ  1 
ATOM   7228  N  N   . ASP G  1 77  ? 156.788 -20.578 8.515   1.00 26.23 ? 76  ASP D N   1 
ATOM   7229  C  CA  . ASP G  1 77  ? 156.174 -21.502 7.613   1.00 27.33 ? 76  ASP D CA  1 
ATOM   7230  C  C   . ASP G  1 77  ? 155.891 -20.661 6.392   1.00 27.85 ? 76  ASP D C   1 
ATOM   7231  O  O   . ASP G  1 77  ? 155.839 -19.437 6.440   1.00 29.12 ? 76  ASP D O   1 
ATOM   7232  C  CB  . ASP G  1 77  ? 154.905 -22.079 8.250   1.00 30.09 ? 76  ASP D CB  1 
ATOM   7233  C  CG  . ASP G  1 77  ? 155.234 -23.076 9.381   1.00 33.15 ? 76  ASP D CG  1 
ATOM   7234  O  OD1 . ASP G  1 77  ? 155.858 -24.108 9.114   1.00 33.02 ? 76  ASP D OD1 1 
ATOM   7235  O  OD2 . ASP G  1 77  ? 154.884 -22.830 10.536  1.00 34.11 ? 76  ASP D OD2 1 
ATOM   7236  N  N   . GLU G  1 78  ? 155.812 -21.341 5.255   1.00 30.15 ? 77  GLU D N   1 
ATOM   7237  C  CA  . GLU G  1 78  ? 155.613 -20.737 3.932   1.00 30.70 ? 77  GLU D CA  1 
ATOM   7238  C  C   . GLU G  1 78  ? 154.240 -20.086 3.915   1.00 27.47 ? 77  GLU D C   1 
ATOM   7239  O  O   . GLU G  1 78  ? 154.020 -18.898 3.656   1.00 27.48 ? 77  GLU D O   1 
ATOM   7240  C  CB  . GLU G  1 78  ? 155.713 -21.847 2.818   1.00 37.72 ? 77  GLU D CB  1 
ATOM   7241  C  CG  . GLU G  1 78  ? 157.022 -22.726 2.826   1.00 45.90 ? 77  GLU D CG  1 
ATOM   7242  C  CD  . GLU G  1 78  ? 157.073 -24.000 1.956   1.00 48.93 ? 77  GLU D CD  1 
ATOM   7243  O  OE1 . GLU G  1 78  ? 157.271 -23.879 0.734   1.00 49.99 ? 77  GLU D OE1 1 
ATOM   7244  O  OE2 . GLU G  1 78  ? 156.933 -25.108 2.513   1.00 52.10 ? 77  GLU D OE2 1 
ATOM   7245  N  N   . GLU G  1 79  ? 153.344 -21.006 4.241   1.00 23.85 ? 78  GLU D N   1 
ATOM   7246  C  CA  . GLU G  1 79  ? 151.951 -20.723 4.365   1.00 22.25 ? 78  GLU D CA  1 
ATOM   7247  C  C   . GLU G  1 79  ? 151.656 -20.357 5.802   1.00 19.13 ? 78  GLU D C   1 
ATOM   7248  O  O   . GLU G  1 79  ? 151.868 -21.108 6.775   1.00 15.22 ? 78  GLU D O   1 
ATOM   7249  C  CB  . GLU G  1 79  ? 151.188 -21.934 3.970   1.00 26.16 ? 78  GLU D CB  1 
ATOM   7250  C  CG  . GLU G  1 79  ? 149.722 -21.712 3.733   1.00 32.37 ? 78  GLU D CG  1 
ATOM   7251  C  CD  . GLU G  1 79  ? 149.337 -22.654 2.606   1.00 40.18 ? 78  GLU D CD  1 
ATOM   7252  O  OE1 . GLU G  1 79  ? 148.981 -23.808 2.919   1.00 42.03 ? 78  GLU D OE1 1 
ATOM   7253  O  OE2 . GLU G  1 79  ? 149.416 -22.220 1.432   1.00 43.63 ? 78  GLU D OE2 1 
ATOM   7254  N  N   . ARG G  1 80  ? 151.246 -19.102 5.810   1.00 16.41 ? 79  ARG D N   1 
ATOM   7255  C  CA  . ARG G  1 80  ? 150.759 -18.516 7.004   1.00 14.59 ? 79  ARG D CA  1 
ATOM   7256  C  C   . ARG G  1 80  ? 150.062 -17.266 6.555   1.00 15.23 ? 79  ARG D C   1 
ATOM   7257  O  O   . ARG G  1 80  ? 150.094 -16.826 5.388   1.00 15.83 ? 79  ARG D O   1 
ATOM   7258  C  CB  . ARG G  1 80  ? 151.908 -18.189 7.948   1.00 16.00 ? 79  ARG D CB  1 
ATOM   7259  C  CG  . ARG G  1 80  ? 153.203 -17.624 7.394   1.00 13.61 ? 79  ARG D CG  1 
ATOM   7260  C  CD  . ARG G  1 80  ? 153.219 -16.275 7.981   1.00 11.98 ? 79  ARG D CD  1 
ATOM   7261  N  NE  . ARG G  1 80  ? 154.531 -15.785 8.271   1.00 13.37 ? 79  ARG D NE  1 
ATOM   7262  C  CZ  . ARG G  1 80  ? 154.632 -14.546 8.756   1.00 16.65 ? 79  ARG D CZ  1 
ATOM   7263  N  NH1 . ARG G  1 80  ? 153.573 -13.754 8.937   1.00 15.76 ? 79  ARG D NH1 1 
ATOM   7264  N  NH2 . ARG G  1 80  ? 155.831 -14.056 9.038   1.00 18.00 ? 79  ARG D NH2 1 
ATOM   7265  N  N   . HIS G  1 81  ? 149.345 -16.771 7.555   1.00 14.40 ? 80  HIS D N   1 
ATOM   7266  C  CA  . HIS G  1 81  ? 148.637 -15.496 7.435   1.00 11.56 ? 80  HIS D CA  1 
ATOM   7267  C  C   . HIS G  1 81  ? 149.688 -14.442 7.670   1.00 9.01  ? 80  HIS D C   1 
ATOM   7268  O  O   . HIS G  1 81  ? 150.646 -14.740 8.394   1.00 8.82  ? 80  HIS D O   1 
ATOM   7269  C  CB  . HIS G  1 81  ? 147.633 -15.259 8.511   1.00 11.49 ? 80  HIS D CB  1 
ATOM   7270  C  CG  . HIS G  1 81  ? 146.574 -16.291 8.716   1.00 10.69 ? 80  HIS D CG  1 
ATOM   7271  N  ND1 . HIS G  1 81  ? 146.122 -16.667 9.890   1.00 12.92 ? 80  HIS D ND1 1 
ATOM   7272  C  CD2 . HIS G  1 81  ? 145.883 -16.899 7.730   1.00 11.94 ? 80  HIS D CD2 1 
ATOM   7273  C  CE1 . HIS G  1 81  ? 145.130 -17.492 9.611   1.00 13.89 ? 80  HIS D CE1 1 
ATOM   7274  N  NE2 . HIS G  1 81  ? 144.994 -17.627 8.317   1.00 15.10 ? 80  HIS D NE2 1 
ATOM   7275  N  N   . VAL G  1 82  ? 149.524 -13.220 7.185   1.00 7.69  ? 81  VAL D N   1 
ATOM   7276  C  CA  . VAL G  1 82  ? 150.533 -12.197 7.435   1.00 7.55  ? 81  VAL D CA  1 
ATOM   7277  C  C   . VAL G  1 82  ? 150.666 -11.946 8.922   1.00 6.87  ? 81  VAL D C   1 
ATOM   7278  O  O   . VAL G  1 82  ? 151.789 -11.800 9.388   1.00 8.12  ? 81  VAL D O   1 
ATOM   7279  C  CB  . VAL G  1 82  ? 150.156 -10.909 6.733   1.00 7.71  ? 81  VAL D CB  1 
ATOM   7280  C  CG1 . VAL G  1 82  ? 151.069 -9.728  7.056   1.00 8.86  ? 81  VAL D CG1 1 
ATOM   7281  C  CG2 . VAL G  1 82  ? 150.304 -11.216 5.245   1.00 11.20 ? 81  VAL D CG2 1 
ATOM   7282  N  N   . GLY G  1 83  ? 149.590 -11.949 9.694   1.00 3.99  ? 82  GLY D N   1 
ATOM   7283  C  CA  . GLY G  1 83  ? 149.715 -11.688 11.108  1.00 5.14  ? 82  GLY D CA  1 
ATOM   7284  C  C   . GLY G  1 83  ? 150.114 -12.871 11.973  1.00 6.46  ? 82  GLY D C   1 
ATOM   7285  O  O   . GLY G  1 83  ? 149.679 -12.939 13.128  1.00 6.13  ? 82  GLY D O   1 
ATOM   7286  N  N   . ASP G  1 84  ? 150.865 -13.871 11.517  1.00 8.37  ? 83  ASP D N   1 
ATOM   7287  C  CA  . ASP G  1 84  ? 151.218 -14.997 12.364  1.00 7.00  ? 83  ASP D CA  1 
ATOM   7288  C  C   . ASP G  1 84  ? 152.644 -14.905 12.852  1.00 9.28  ? 83  ASP D C   1 
ATOM   7289  O  O   . ASP G  1 84  ? 153.655 -15.304 12.245  1.00 9.24  ? 83  ASP D O   1 
ATOM   7290  C  CB  . ASP G  1 84  ? 151.017 -16.282 11.625  1.00 5.71  ? 83  ASP D CB  1 
ATOM   7291  C  CG  . ASP G  1 84  ? 149.550 -16.564 11.307  1.00 7.93  ? 83  ASP D CG  1 
ATOM   7292  O  OD1 . ASP G  1 84  ? 148.646 -16.095 11.973  1.00 6.21  ? 83  ASP D OD1 1 
ATOM   7293  O  OD2 . ASP G  1 84  ? 149.309 -17.301 10.374  1.00 12.43 ? 83  ASP D OD2 1 
ATOM   7294  N  N   . LEU G  1 85  ? 152.669 -14.313 14.045  1.00 10.56 ? 84  LEU D N   1 
ATOM   7295  C  CA  . LEU G  1 85  ? 153.932 -14.088 14.693  1.00 6.14  ? 84  LEU D CA  1 
ATOM   7296  C  C   . LEU G  1 85  ? 154.281 -15.199 15.647  1.00 4.18  ? 84  LEU D C   1 
ATOM   7297  O  O   . LEU G  1 85  ? 155.286 -15.123 16.332  1.00 7.16  ? 84  LEU D O   1 
ATOM   7298  C  CB  . LEU G  1 85  ? 153.846 -12.724 15.341  1.00 4.37  ? 84  LEU D CB  1 
ATOM   7299  C  CG  . LEU G  1 85  ? 153.843 -11.593 14.305  1.00 2.00  ? 84  LEU D CG  1 
ATOM   7300  C  CD1 . LEU G  1 85  ? 153.797 -10.280 15.020  1.00 2.41  ? 84  LEU D CD1 1 
ATOM   7301  C  CD2 . LEU G  1 85  ? 155.096 -11.601 13.477  1.00 2.00  ? 84  LEU D CD2 1 
ATOM   7302  N  N   . GLY G  1 86  ? 153.552 -16.309 15.689  1.00 3.99  ? 85  GLY D N   1 
ATOM   7303  C  CA  . GLY G  1 86  ? 153.981 -17.429 16.514  1.00 2.89  ? 85  GLY D CA  1 
ATOM   7304  C  C   . GLY G  1 86  ? 153.600 -17.304 17.977  1.00 2.08  ? 85  GLY D C   1 
ATOM   7305  O  O   . GLY G  1 86  ? 152.463 -16.987 18.318  1.00 2.00  ? 85  GLY D O   1 
ATOM   7306  N  N   . ASN G  1 87  ? 154.556 -17.502 18.848  1.00 4.08  ? 86  ASN D N   1 
ATOM   7307  C  CA  . ASN G  1 87  ? 154.266 -17.647 20.270  1.00 6.83  ? 86  ASN D CA  1 
ATOM   7308  C  C   . ASN G  1 87  ? 155.280 -16.873 21.030  1.00 5.91  ? 86  ASN D C   1 
ATOM   7309  O  O   . ASN G  1 87  ? 156.435 -16.730 20.618  1.00 6.47  ? 86  ASN D O   1 
ATOM   7310  C  CB  . ASN G  1 87  ? 154.397 -19.084 20.826  1.00 9.25  ? 86  ASN D CB  1 
ATOM   7311  C  CG  . ASN G  1 87  ? 153.302 -20.044 20.401  1.00 13.86 ? 86  ASN D CG  1 
ATOM   7312  O  OD1 . ASN G  1 87  ? 152.123 -19.720 20.509  1.00 15.73 ? 86  ASN D OD1 1 
ATOM   7313  N  ND2 . ASN G  1 87  ? 153.573 -21.255 19.928  1.00 15.46 ? 86  ASN D ND2 1 
ATOM   7314  N  N   . VAL G  1 88  ? 154.872 -16.347 22.150  1.00 6.12  ? 87  VAL D N   1 
ATOM   7315  C  CA  . VAL G  1 88  ? 155.849 -15.714 22.996  1.00 9.07  ? 87  VAL D CA  1 
ATOM   7316  C  C   . VAL G  1 88  ? 155.797 -16.478 24.312  1.00 10.27 ? 87  VAL D C   1 
ATOM   7317  O  O   . VAL G  1 88  ? 154.741 -17.028 24.668  1.00 10.92 ? 87  VAL D O   1 
ATOM   7318  C  CB  . VAL G  1 88  ? 155.510 -14.235 23.156  1.00 7.66  ? 87  VAL D CB  1 
ATOM   7319  C  CG1 . VAL G  1 88  ? 155.865 -13.624 21.828  1.00 9.89  ? 87  VAL D CG1 1 
ATOM   7320  C  CG2 . VAL G  1 88  ? 154.051 -13.960 23.514  1.00 4.54  ? 87  VAL D CG2 1 
ATOM   7321  N  N   . THR G  1 89  ? 156.909 -16.492 25.032  1.00 11.73 ? 88  THR D N   1 
ATOM   7322  C  CA  . THR G  1 89  ? 157.011 -17.348 26.175  1.00 15.83 ? 88  THR D CA  1 
ATOM   7323  C  C   . THR G  1 89  ? 157.149 -16.550 27.447  1.00 17.06 ? 88  THR D C   1 
ATOM   7324  O  O   . THR G  1 89  ? 158.158 -15.877 27.661  1.00 17.96 ? 88  THR D O   1 
ATOM   7325  C  CB  . THR G  1 89  ? 158.242 -18.318 25.991  1.00 18.95 ? 88  THR D CB  1 
ATOM   7326  O  OG1 . THR G  1 89  ? 158.137 -18.972 24.719  1.00 21.53 ? 88  THR D OG1 1 
ATOM   7327  C  CG2 . THR G  1 89  ? 158.288 -19.393 27.079  1.00 19.96 ? 88  THR D CG2 1 
ATOM   7328  N  N   . ALA G  1 90  ? 156.160 -16.638 28.315  1.00 18.53 ? 89  ALA D N   1 
ATOM   7329  C  CA  . ALA G  1 90  ? 156.267 -15.975 29.590  1.00 19.10 ? 89  ALA D CA  1 
ATOM   7330  C  C   . ALA G  1 90  ? 157.078 -16.842 30.564  1.00 19.57 ? 89  ALA D C   1 
ATOM   7331  O  O   . ALA G  1 90  ? 156.942 -18.073 30.593  1.00 19.60 ? 89  ALA D O   1 
ATOM   7332  C  CB  . ALA G  1 90  ? 154.874 -15.753 30.112  1.00 19.77 ? 89  ALA D CB  1 
ATOM   7333  N  N   . ASP G  1 91  ? 157.987 -16.282 31.356  1.00 20.11 ? 90  ASP D N   1 
ATOM   7334  C  CA  . ASP G  1 91  ? 158.683 -17.052 32.369  1.00 22.00 ? 90  ASP D CA  1 
ATOM   7335  C  C   . ASP G  1 91  ? 157.790 -17.271 33.586  1.00 24.16 ? 90  ASP D C   1 
ATOM   7336  O  O   . ASP G  1 91  ? 156.655 -16.786 33.631  1.00 25.52 ? 90  ASP D O   1 
ATOM   7337  C  CB  . ASP G  1 91  ? 159.974 -16.350 32.825  1.00 20.21 ? 90  ASP D CB  1 
ATOM   7338  C  CG  . ASP G  1 91  ? 159.870 -14.958 33.431  1.00 21.97 ? 90  ASP D CG  1 
ATOM   7339  O  OD1 . ASP G  1 91  ? 158.783 -14.539 33.795  1.00 23.80 ? 90  ASP D OD1 1 
ATOM   7340  O  OD2 . ASP G  1 91  ? 160.885 -14.264 33.541  1.00 24.83 ? 90  ASP D OD2 1 
ATOM   7341  N  N   . LYS G  1 92  ? 158.304 -17.918 34.638  1.00 25.45 ? 91  LYS D N   1 
ATOM   7342  C  CA  . LYS G  1 92  ? 157.574 -18.155 35.880  1.00 25.07 ? 91  LYS D CA  1 
ATOM   7343  C  C   . LYS G  1 92  ? 157.092 -16.910 36.594  1.00 22.47 ? 91  LYS D C   1 
ATOM   7344  O  O   . LYS G  1 92  ? 156.392 -17.035 37.585  1.00 23.23 ? 91  LYS D O   1 
ATOM   7345  C  CB  . LYS G  1 92  ? 158.443 -18.986 36.832  1.00 27.14 ? 91  LYS D CB  1 
ATOM   7346  C  CG  . LYS G  1 92  ? 159.930 -18.595 36.944  1.00 32.50 ? 91  LYS D CG  1 
ATOM   7347  C  CD  . LYS G  1 92  ? 160.405 -18.591 38.400  1.00 35.94 ? 91  LYS D CD  1 
ATOM   7348  C  CE  . LYS G  1 92  ? 160.157 -19.913 39.154  1.00 37.78 ? 91  LYS D CE  1 
ATOM   7349  N  NZ  . LYS G  1 92  ? 160.209 -19.675 40.593  1.00 40.84 ? 91  LYS D NZ  1 
ATOM   7350  N  N   . ASP G  1 93  ? 157.443 -15.712 36.134  1.00 20.23 ? 92  ASP D N   1 
ATOM   7351  C  CA  . ASP G  1 93  ? 156.897 -14.462 36.661  1.00 19.60 ? 92  ASP D CA  1 
ATOM   7352  C  C   . ASP G  1 93  ? 155.756 -13.895 35.842  1.00 17.66 ? 92  ASP D C   1 
ATOM   7353  O  O   . ASP G  1 93  ? 155.268 -12.800 36.118  1.00 19.44 ? 92  ASP D O   1 
ATOM   7354  C  CB  . ASP G  1 93  ? 157.931 -13.365 36.721  1.00 20.66 ? 92  ASP D CB  1 
ATOM   7355  C  CG  . ASP G  1 93  ? 159.187 -13.714 37.484  1.00 25.54 ? 92  ASP D CG  1 
ATOM   7356  O  OD1 . ASP G  1 93  ? 159.165 -14.633 38.323  1.00 27.85 ? 92  ASP D OD1 1 
ATOM   7357  O  OD2 . ASP G  1 93  ? 160.191 -13.049 37.214  1.00 27.73 ? 92  ASP D OD2 1 
ATOM   7358  N  N   . GLY G  1 94  ? 155.345 -14.597 34.793  1.00 16.20 ? 93  GLY D N   1 
ATOM   7359  C  CA  . GLY G  1 94  ? 154.303 -14.121 33.905  1.00 14.49 ? 93  GLY D CA  1 
ATOM   7360  C  C   . GLY G  1 94  ? 154.783 -13.026 32.956  1.00 13.61 ? 93  GLY D C   1 
ATOM   7361  O  O   . GLY G  1 94  ? 153.975 -12.313 32.365  1.00 13.79 ? 93  GLY D O   1 
ATOM   7362  N  N   . VAL G  1 95  ? 156.093 -12.878 32.791  1.00 11.92 ? 94  VAL D N   1 
ATOM   7363  C  CA  . VAL G  1 95  ? 156.680 -11.851 31.960  1.00 11.96 ? 94  VAL D CA  1 
ATOM   7364  C  C   . VAL G  1 95  ? 157.168 -12.497 30.673  1.00 13.51 ? 94  VAL D C   1 
ATOM   7365  O  O   . VAL G  1 95  ? 157.719 -13.600 30.703  1.00 12.89 ? 94  VAL D O   1 
ATOM   7366  C  CB  . VAL G  1 95  ? 157.816 -11.181 32.760  1.00 10.24 ? 94  VAL D CB  1 
ATOM   7367  C  CG1 . VAL G  1 95  ? 158.448 -10.046 31.988  1.00 11.17 ? 94  VAL D CG1 1 
ATOM   7368  C  CG2 . VAL G  1 95  ? 157.216 -10.500 33.991  1.00 10.35 ? 94  VAL D CG2 1 
ATOM   7369  N  N   . ALA G  1 96  ? 156.942 -11.888 29.517  1.00 15.00 ? 95  ALA D N   1 
ATOM   7370  C  CA  . ALA G  1 96  ? 157.355 -12.472 28.255  1.00 14.65 ? 95  ALA D CA  1 
ATOM   7371  C  C   . ALA G  1 96  ? 158.157 -11.359 27.642  1.00 16.44 ? 95  ALA D C   1 
ATOM   7372  O  O   . ALA G  1 96  ? 157.623 -10.262 27.481  1.00 16.66 ? 95  ALA D O   1 
ATOM   7373  C  CB  . ALA G  1 96  ? 156.174 -12.764 27.348  1.00 12.83 ? 95  ALA D CB  1 
ATOM   7374  N  N   . ASP G  1 97  ? 159.450 -11.569 27.426  1.00 18.06 ? 96  ASP D N   1 
ATOM   7375  C  CA  . ASP G  1 97  ? 160.250 -10.588 26.720  1.00 20.63 ? 96  ASP D CA  1 
ATOM   7376  C  C   . ASP G  1 97  ? 160.180 -11.104 25.285  1.00 20.93 ? 96  ASP D C   1 
ATOM   7377  O  O   . ASP G  1 97  ? 160.226 -12.319 25.029  1.00 22.39 ? 96  ASP D O   1 
ATOM   7378  C  CB  . ASP G  1 97  ? 161.643 -10.575 27.331  1.00 23.73 ? 96  ASP D CB  1 
ATOM   7379  C  CG  . ASP G  1 97  ? 161.551 -10.056 28.793  1.00 30.19 ? 96  ASP D CG  1 
ATOM   7380  O  OD1 . ASP G  1 97  ? 161.357 -8.849  28.977  1.00 32.27 ? 96  ASP D OD1 1 
ATOM   7381  O  OD2 . ASP G  1 97  ? 161.660 -10.836 29.757  1.00 31.61 ? 96  ASP D OD2 1 
ATOM   7382  N  N   . VAL G  1 98  ? 159.857 -10.181 24.378  1.00 18.32 ? 97  VAL D N   1 
ATOM   7383  C  CA  . VAL G  1 98  ? 159.563 -10.473 22.995  1.00 15.82 ? 97  VAL D CA  1 
ATOM   7384  C  C   . VAL G  1 98  ? 160.691 -9.887  22.169  1.00 18.84 ? 97  VAL D C   1 
ATOM   7385  O  O   . VAL G  1 98  ? 161.179 -8.800  22.480  1.00 18.82 ? 97  VAL D O   1 
ATOM   7386  C  CB  . VAL G  1 98  ? 158.220 -9.826  22.600  1.00 13.75 ? 97  VAL D CB  1 
ATOM   7387  C  CG1 . VAL G  1 98  ? 157.897 -10.071 21.127  1.00 10.39 ? 97  VAL D CG1 1 
ATOM   7388  C  CG2 . VAL G  1 98  ? 157.122 -10.422 23.439  1.00 8.05  ? 97  VAL D CG2 1 
ATOM   7389  N  N   . SER G  1 99  ? 161.085 -10.628 21.129  1.00 21.54 ? 98  SER D N   1 
ATOM   7390  C  CA  . SER G  1 99  ? 162.077 -10.277 20.107  1.00 23.63 ? 98  SER D CA  1 
ATOM   7391  C  C   . SER G  1 99  ? 161.920 -11.260 18.940  1.00 23.97 ? 98  SER D C   1 
ATOM   7392  O  O   . SER G  1 99  ? 162.181 -12.468 19.011  1.00 24.09 ? 98  SER D O   1 
ATOM   7393  C  CB  . SER G  1 99  ? 163.529 -10.364 20.611  1.00 24.14 ? 98  SER D CB  1 
ATOM   7394  O  OG  . SER G  1 99  ? 163.946 -9.164  21.278  1.00 30.14 ? 98  SER D OG  1 
ATOM   7395  N  N   . ILE G  1 100 ? 161.369 -10.700 17.878  1.00 22.65 ? 99  ILE D N   1 
ATOM   7396  C  CA  . ILE G  1 100 ? 161.066 -11.368 16.641  1.00 23.10 ? 99  ILE D CA  1 
ATOM   7397  C  C   . ILE G  1 100 ? 161.745 -10.435 15.640  1.00 24.72 ? 99  ILE D C   1 
ATOM   7398  O  O   . ILE G  1 100 ? 161.996 -9.246  15.893  1.00 25.36 ? 99  ILE D O   1 
ATOM   7399  C  CB  . ILE G  1 100 ? 159.527 -11.396 16.451  1.00 23.75 ? 99  ILE D CB  1 
ATOM   7400  C  CG1 . ILE G  1 100 ? 158.942 -12.364 17.430  1.00 26.26 ? 99  ILE D CG1 1 
ATOM   7401  C  CG2 . ILE G  1 100 ? 159.119 -11.776 15.030  1.00 23.28 ? 99  ILE D CG2 1 
ATOM   7402  C  CD1 . ILE G  1 100 ? 157.397 -12.289 17.405  1.00 28.67 ? 99  ILE D CD1 1 
ATOM   7403  N  N   . GLU G  1 101 ? 162.023 -10.999 14.477  1.00 24.81 ? 100 GLU D N   1 
ATOM   7404  C  CA  . GLU G  1 101 ? 162.588 -10.340 13.318  1.00 22.48 ? 100 GLU D CA  1 
ATOM   7405  C  C   . GLU G  1 101 ? 161.629 -10.987 12.298  1.00 20.55 ? 100 GLU D C   1 
ATOM   7406  O  O   . GLU G  1 101 ? 161.447 -12.219 12.282  1.00 20.79 ? 100 GLU D O   1 
ATOM   7407  C  CB  . GLU G  1 101 ? 164.042 -10.814 13.263  1.00 26.39 ? 100 GLU D CB  1 
ATOM   7408  C  CG  . GLU G  1 101 ? 165.244 -9.852  13.069  1.00 31.80 ? 100 GLU D CG  1 
ATOM   7409  C  CD  . GLU G  1 101 ? 165.558 -9.414  11.628  1.00 36.94 ? 100 GLU D CD  1 
ATOM   7410  O  OE1 . GLU G  1 101 ? 165.347 -10.196 10.673  1.00 36.31 ? 100 GLU D OE1 1 
ATOM   7411  O  OE2 . GLU G  1 101 ? 166.029 -8.276  11.475  1.00 38.60 ? 100 GLU D OE2 1 
ATOM   7412  N  N   . ASP G  1 102 ? 160.904 -10.258 11.473  1.00 16.78 ? 101 ASP D N   1 
ATOM   7413  C  CA  . ASP G  1 102 ? 159.961 -10.900 10.598  1.00 14.07 ? 101 ASP D CA  1 
ATOM   7414  C  C   . ASP G  1 102 ? 159.930 -10.136 9.343   1.00 14.86 ? 101 ASP D C   1 
ATOM   7415  O  O   . ASP G  1 102 ? 160.058 -8.926  9.398   1.00 17.71 ? 101 ASP D O   1 
ATOM   7416  C  CB  . ASP G  1 102 ? 158.592 -10.859 11.166  1.00 14.34 ? 101 ASP D CB  1 
ATOM   7417  C  CG  . ASP G  1 102 ? 157.639 -11.848 10.552  1.00 12.33 ? 101 ASP D CG  1 
ATOM   7418  O  OD1 . ASP G  1 102 ? 157.902 -13.035 10.652  1.00 12.41 ? 101 ASP D OD1 1 
ATOM   7419  O  OD2 . ASP G  1 102 ? 156.630 -11.434 9.999   1.00 15.51 ? 101 ASP D OD2 1 
ATOM   7420  N  N   . SER G  1 103 ? 159.630 -10.812 8.248   1.00 15.19 ? 102 SER D N   1 
ATOM   7421  C  CA  . SER G  1 103 ? 159.626 -10.144 6.979   1.00 16.21 ? 102 SER D CA  1 
ATOM   7422  C  C   . SER G  1 103 ? 158.373 -10.368 6.175   1.00 17.33 ? 102 SER D C   1 
ATOM   7423  O  O   . SER G  1 103 ? 158.415 -10.302 4.958   1.00 20.22 ? 102 SER D O   1 
ATOM   7424  C  CB  . SER G  1 103 ? 160.840 -10.606 6.203   1.00 18.96 ? 102 SER D CB  1 
ATOM   7425  O  OG  . SER G  1 103 ? 161.991 -10.670 7.072   1.00 28.23 ? 102 SER D OG  1 
ATOM   7426  N  N   . VAL G  1 104 ? 157.209 -10.696 6.745   1.00 17.05 ? 103 VAL D N   1 
ATOM   7427  C  CA  . VAL G  1 104 ? 155.989 -10.743 5.922   1.00 17.14 ? 103 VAL D CA  1 
ATOM   7428  C  C   . VAL G  1 104 ? 155.094 -9.566  6.295   1.00 16.64 ? 103 VAL D C   1 
ATOM   7429  O  O   . VAL G  1 104 ? 154.422 -8.963  5.427   1.00 18.01 ? 103 VAL D O   1 
ATOM   7430  C  CB  . VAL G  1 104 ? 155.239 -12.054 6.158   1.00 18.37 ? 103 VAL D CB  1 
ATOM   7431  C  CG1 . VAL G  1 104 ? 153.967 -12.123 5.301   1.00 20.09 ? 103 VAL D CG1 1 
ATOM   7432  C  CG2 . VAL G  1 104 ? 156.210 -13.188 5.861   1.00 16.16 ? 103 VAL D CG2 1 
ATOM   7433  N  N   . ILE G  1 105 ? 155.085 -9.301  7.627   1.00 14.80 ? 104 ILE D N   1 
ATOM   7434  C  CA  . ILE G  1 105 ? 154.411 -8.129  8.163   1.00 11.88 ? 104 ILE D CA  1 
ATOM   7435  C  C   . ILE G  1 105 ? 155.305 -6.982  7.683   1.00 13.78 ? 104 ILE D C   1 
ATOM   7436  O  O   . ILE G  1 105 ? 156.495 -7.177  7.397   1.00 13.46 ? 104 ILE D O   1 
ATOM   7437  C  CB  . ILE G  1 105 ? 154.312 -8.093  9.763   1.00 6.79  ? 104 ILE D CB  1 
ATOM   7438  C  CG1 . ILE G  1 105 ? 155.644 -8.119  10.490  1.00 6.05  ? 104 ILE D CG1 1 
ATOM   7439  C  CG2 . ILE G  1 105 ? 153.487 -9.282  10.168  1.00 5.60  ? 104 ILE D CG2 1 
ATOM   7440  C  CD1 . ILE G  1 105 ? 155.749 -7.761  11.985  1.00 2.00  ? 104 ILE D CD1 1 
ATOM   7441  N  N   . SER G  1 106 ? 154.761 -5.779  7.554   1.00 15.06 ? 105 SER D N   1 
ATOM   7442  C  CA  . SER G  1 106 ? 155.528 -4.621  7.184   1.00 15.04 ? 105 SER D CA  1 
ATOM   7443  C  C   . SER G  1 106 ? 154.855 -3.446  7.875   1.00 16.24 ? 105 SER D C   1 
ATOM   7444  O  O   . SER G  1 106 ? 153.711 -3.546  8.364   1.00 19.90 ? 105 SER D O   1 
ATOM   7445  C  CB  . SER G  1 106 ? 155.520 -4.407  5.659   1.00 14.85 ? 105 SER D CB  1 
ATOM   7446  O  OG  . SER G  1 106 ? 156.315 -3.239  5.393   1.00 19.73 ? 105 SER D OG  1 
ATOM   7447  N  N   . LEU G  1 107 ? 155.556 -2.319  7.924   1.00 13.78 ? 106 LEU D N   1 
ATOM   7448  C  CA  . LEU G  1 107 ? 154.998 -1.119  8.483   1.00 13.33 ? 106 LEU D CA  1 
ATOM   7449  C  C   . LEU G  1 107 ? 154.677 -0.246  7.284   1.00 14.36 ? 106 LEU D C   1 
ATOM   7450  O  O   . LEU G  1 107 ? 154.411 0.937   7.451   1.00 15.44 ? 106 LEU D O   1 
ATOM   7451  C  CB  . LEU G  1 107 ? 155.990 -0.364  9.357   1.00 10.65 ? 106 LEU D CB  1 
ATOM   7452  C  CG  . LEU G  1 107 ? 156.766 -1.017  10.492  1.00 9.90  ? 106 LEU D CG  1 
ATOM   7453  C  CD1 . LEU G  1 107 ? 157.190 0.115   11.359  1.00 2.00  ? 106 LEU D CD1 1 
ATOM   7454  C  CD2 . LEU G  1 107 ? 155.962 -2.011  11.308  1.00 4.24  ? 106 LEU D CD2 1 
ATOM   7455  N  N   . SER G  1 108 ? 154.720 -0.735  6.053   1.00 15.85 ? 107 SER D N   1 
ATOM   7456  C  CA  . SER G  1 108 ? 154.457 0.072   4.882   1.00 14.94 ? 107 SER D CA  1 
ATOM   7457  C  C   . SER G  1 108 ? 153.794 -0.833  3.852   1.00 15.68 ? 107 SER D C   1 
ATOM   7458  O  O   . SER G  1 108 ? 153.913 -2.065  3.836   1.00 15.77 ? 107 SER D O   1 
ATOM   7459  C  CB  . SER G  1 108 ? 155.759 0.590   4.311   1.00 13.66 ? 107 SER D CB  1 
ATOM   7460  O  OG  . SER G  1 108 ? 156.840 0.850   5.220   1.00 21.71 ? 107 SER D OG  1 
ATOM   7461  N  N   . GLY G  1 109 ? 152.965 -0.257  3.005   1.00 17.13 ? 108 GLY D N   1 
ATOM   7462  C  CA  . GLY G  1 109 ? 152.481 -1.005  1.873   1.00 17.78 ? 108 GLY D CA  1 
ATOM   7463  C  C   . GLY G  1 109 ? 151.188 -1.680  2.182   1.00 19.88 ? 108 GLY D C   1 
ATOM   7464  O  O   . GLY G  1 109 ? 150.518 -1.347  3.153   1.00 20.67 ? 108 GLY D O   1 
ATOM   7465  N  N   . ASP G  1 110 ? 150.835 -2.655  1.346   1.00 22.70 ? 109 ASP D N   1 
ATOM   7466  C  CA  . ASP G  1 110 ? 149.558 -3.344  1.513   1.00 22.38 ? 109 ASP D CA  1 
ATOM   7467  C  C   . ASP G  1 110 ? 149.599 -4.351  2.621   1.00 19.90 ? 109 ASP D C   1 
ATOM   7468  O  O   . ASP G  1 110 ? 148.538 -4.798  3.031   1.00 21.40 ? 109 ASP D O   1 
ATOM   7469  C  CB  . ASP G  1 110 ? 149.117 -4.063  0.208   1.00 23.65 ? 109 ASP D CB  1 
ATOM   7470  C  CG  . ASP G  1 110 ? 147.983 -3.364  -0.571  1.00 28.57 ? 109 ASP D CG  1 
ATOM   7471  O  OD1 . ASP G  1 110 ? 147.794 -2.117  -0.500  1.00 26.02 ? 109 ASP D OD1 1 
ATOM   7472  O  OD2 . ASP G  1 110 ? 147.285 -4.110  -1.271  1.00 27.09 ? 109 ASP D OD2 1 
ATOM   7473  N  N   . HIS G  1 111 ? 150.791 -4.754  3.061   1.00 17.44 ? 110 HIS D N   1 
ATOM   7474  C  CA  . HIS G  1 111 ? 150.889 -5.683  4.162   1.00 15.98 ? 110 HIS D CA  1 
ATOM   7475  C  C   . HIS G  1 111 ? 151.040 -4.927  5.492   1.00 14.72 ? 110 HIS D C   1 
ATOM   7476  O  O   . HIS G  1 111 ? 151.249 -5.553  6.516   1.00 13.72 ? 110 HIS D O   1 
ATOM   7477  C  CB  . HIS G  1 111 ? 152.069 -6.602  3.907   1.00 16.32 ? 110 HIS D CB  1 
ATOM   7478  C  CG  . HIS G  1 111 ? 151.822 -7.797  2.974   1.00 19.59 ? 110 HIS D CG  1 
ATOM   7479  N  ND1 . HIS G  1 111 ? 152.543 -8.926  2.957   1.00 17.81 ? 110 HIS D ND1 1 
ATOM   7480  C  CD2 . HIS G  1 111 ? 150.804 -7.932  2.030   1.00 16.39 ? 110 HIS D CD2 1 
ATOM   7481  C  CE1 . HIS G  1 111 ? 151.997 -9.721  2.062   1.00 16.33 ? 110 HIS D CE1 1 
ATOM   7482  N  NE2 . HIS G  1 111 ? 150.951 -9.122  1.509   1.00 12.69 ? 110 HIS D NE2 1 
ATOM   7483  N  N   . SER G  1 112 ? 150.896 -3.596  5.506   1.00 14.42 ? 111 SER D N   1 
ATOM   7484  C  CA  . SER G  1 112 ? 150.966 -2.740  6.684   1.00 13.69 ? 111 SER D CA  1 
ATOM   7485  C  C   . SER G  1 112 ? 150.194 -3.285  7.880   1.00 12.94 ? 111 SER D C   1 
ATOM   7486  O  O   . SER G  1 112 ? 149.033 -3.696  7.734   1.00 13.60 ? 111 SER D O   1 
ATOM   7487  C  CB  . SER G  1 112 ? 150.392 -1.383  6.350   1.00 11.75 ? 111 SER D CB  1 
ATOM   7488  O  OG  . SER G  1 112 ? 150.987 -0.336  7.101   1.00 19.41 ? 111 SER D OG  1 
ATOM   7489  N  N   . ILE G  1 113 ? 150.857 -3.330  9.044   1.00 11.11 ? 112 ILE D N   1 
ATOM   7490  C  CA  . ILE G  1 113 ? 150.154 -3.691  10.279  1.00 9.26  ? 112 ILE D CA  1 
ATOM   7491  C  C   . ILE G  1 113 ? 149.747 -2.449  11.076  1.00 7.03  ? 112 ILE D C   1 
ATOM   7492  O  O   . ILE G  1 113 ? 149.167 -2.521  12.154  1.00 10.14 ? 112 ILE D O   1 
ATOM   7493  C  CB  . ILE G  1 113 ? 151.040 -4.633  11.155  1.00 9.24  ? 112 ILE D CB  1 
ATOM   7494  C  CG1 . ILE G  1 113 ? 152.481 -4.119  11.361  1.00 9.00  ? 112 ILE D CG1 1 
ATOM   7495  C  CG2 . ILE G  1 113 ? 150.957 -5.998  10.477  1.00 10.10 ? 112 ILE D CG2 1 
ATOM   7496  C  CD1 . ILE G  1 113 ? 153.232 -4.606  12.603  1.00 2.00  ? 112 ILE D CD1 1 
ATOM   7497  N  N   . ILE G  1 114 ? 150.037 -1.259  10.571  1.00 5.09  ? 113 ILE D N   1 
ATOM   7498  C  CA  . ILE G  1 114 ? 149.708 0.024   11.163  1.00 2.24  ? 113 ILE D CA  1 
ATOM   7499  C  C   . ILE G  1 114 ? 148.194 0.159   11.156  1.00 2.00  ? 113 ILE D C   1 
ATOM   7500  O  O   . ILE G  1 114 ? 147.552 -0.032  10.134  1.00 6.26  ? 113 ILE D O   1 
ATOM   7501  C  CB  . ILE G  1 114 ? 150.362 1.125   10.309  1.00 2.00  ? 113 ILE D CB  1 
ATOM   7502  C  CG1 . ILE G  1 114 ? 151.876 0.988   10.271  1.00 2.00  ? 113 ILE D CG1 1 
ATOM   7503  C  CG2 . ILE G  1 114 ? 149.954 2.480   10.834  1.00 2.00  ? 113 ILE D CG2 1 
ATOM   7504  C  CD1 . ILE G  1 114 ? 152.716 1.072   11.533  1.00 2.00  ? 113 ILE D CD1 1 
ATOM   7505  N  N   . GLY G  1 115 ? 147.583 0.478   12.269  1.00 2.64  ? 114 GLY D N   1 
ATOM   7506  C  CA  . GLY G  1 115 ? 146.154 0.659   12.373  1.00 2.00  ? 114 GLY D CA  1 
ATOM   7507  C  C   . GLY G  1 115 ? 145.471 -0.665  12.569  1.00 2.76  ? 114 GLY D C   1 
ATOM   7508  O  O   . GLY G  1 115 ? 144.248 -0.755  12.468  1.00 4.88  ? 114 GLY D O   1 
ATOM   7509  N  N   . ARG G  1 116 ? 146.220 -1.728  12.837  1.00 4.35  ? 115 ARG D N   1 
ATOM   7510  C  CA  . ARG G  1 116 ? 145.641 -3.035  13.029  1.00 3.36  ? 115 ARG D CA  1 
ATOM   7511  C  C   . ARG G  1 116 ? 145.787 -3.399  14.503  1.00 2.00  ? 115 ARG D C   1 
ATOM   7512  O  O   . ARG G  1 116 ? 146.147 -2.515  15.278  1.00 3.46  ? 115 ARG D O   1 
ATOM   7513  C  CB  . ARG G  1 116 ? 146.362 -3.988  12.046  1.00 6.10  ? 115 ARG D CB  1 
ATOM   7514  C  CG  . ARG G  1 116 ? 146.055 -3.574  10.583  1.00 4.32  ? 115 ARG D CG  1 
ATOM   7515  C  CD  . ARG G  1 116 ? 146.271 -4.689  9.599   1.00 7.39  ? 115 ARG D CD  1 
ATOM   7516  N  NE  . ARG G  1 116 ? 146.300 -4.210  8.229   1.00 8.52  ? 115 ARG D NE  1 
ATOM   7517  C  CZ  . ARG G  1 116 ? 145.234 -3.986  7.444   1.00 7.45  ? 115 ARG D CZ  1 
ATOM   7518  N  NH1 . ARG G  1 116 ? 143.981 -4.177  7.829   1.00 7.00  ? 115 ARG D NH1 1 
ATOM   7519  N  NH2 . ARG G  1 116 ? 145.459 -3.550  6.217   1.00 6.75  ? 115 ARG D NH2 1 
ATOM   7520  N  N   . THR G  1 117 ? 145.520 -4.603  14.970  1.00 2.00  ? 116 THR D N   1 
ATOM   7521  C  CA  . THR G  1 117 ? 145.522 -4.916  16.379  1.00 2.25  ? 116 THR D CA  1 
ATOM   7522  C  C   . THR G  1 117 ? 146.489 -6.055  16.640  1.00 3.46  ? 116 THR D C   1 
ATOM   7523  O  O   . THR G  1 117 ? 146.414 -7.077  15.959  1.00 2.00  ? 116 THR D O   1 
ATOM   7524  C  CB  . THR G  1 117 ? 144.113 -5.347  16.850  1.00 2.00  ? 116 THR D CB  1 
ATOM   7525  O  OG1 . THR G  1 117 ? 143.246 -4.272  16.551  1.00 2.00  ? 116 THR D OG1 1 
ATOM   7526  C  CG2 . THR G  1 117 ? 144.057 -5.728  18.340  1.00 2.00  ? 116 THR D CG2 1 
ATOM   7527  N  N   . LEU G  1 118 ? 147.397 -5.881  17.602  1.00 2.26  ? 117 LEU D N   1 
ATOM   7528  C  CA  . LEU G  1 118 ? 148.287 -6.933  18.046  1.00 2.31  ? 117 LEU D CA  1 
ATOM   7529  C  C   . LEU G  1 118 ? 147.520 -7.625  19.148  1.00 2.83  ? 117 LEU D C   1 
ATOM   7530  O  O   . LEU G  1 118 ? 146.917 -6.899  19.935  1.00 2.00  ? 117 LEU D O   1 
ATOM   7531  C  CB  . LEU G  1 118 ? 149.546 -6.335  18.606  1.00 2.00  ? 117 LEU D CB  1 
ATOM   7532  C  CG  . LEU G  1 118 ? 150.670 -7.273  18.928  1.00 2.00  ? 117 LEU D CG  1 
ATOM   7533  C  CD1 . LEU G  1 118 ? 151.000 -8.151  17.734  1.00 2.00  ? 117 LEU D CD1 1 
ATOM   7534  C  CD2 . LEU G  1 118 ? 151.851 -6.439  19.372  1.00 2.00  ? 117 LEU D CD2 1 
ATOM   7535  N  N   . VAL G  1 119 ? 147.510 -8.957  19.269  1.00 2.28  ? 118 VAL D N   1 
ATOM   7536  C  CA  . VAL G  1 119 ? 146.742 -9.694  20.263  1.00 2.35  ? 118 VAL D CA  1 
ATOM   7537  C  C   . VAL G  1 119 ? 147.574 -10.802 20.926  1.00 5.09  ? 118 VAL D C   1 
ATOM   7538  O  O   . VAL G  1 119 ? 148.181 -11.643 20.242  1.00 2.79  ? 118 VAL D O   1 
ATOM   7539  C  CB  . VAL G  1 119 ? 145.499 -10.290 19.572  1.00 3.01  ? 118 VAL D CB  1 
ATOM   7540  C  CG1 . VAL G  1 119 ? 144.701 -11.106 20.546  1.00 4.48  ? 118 VAL D CG1 1 
ATOM   7541  C  CG2 . VAL G  1 119 ? 144.553 -9.190  19.082  1.00 2.00  ? 118 VAL D CG2 1 
ATOM   7542  N  N   . VAL G  1 120 ? 147.694 -10.808 22.272  1.00 6.17  ? 119 VAL D N   1 
ATOM   7543  C  CA  . VAL G  1 120 ? 148.393 -11.886 22.925  1.00 3.86  ? 119 VAL D CA  1 
ATOM   7544  C  C   . VAL G  1 120 ? 147.242 -12.752 23.359  1.00 6.65  ? 119 VAL D C   1 
ATOM   7545  O  O   . VAL G  1 120 ? 146.200 -12.261 23.834  1.00 8.05  ? 119 VAL D O   1 
ATOM   7546  C  CB  . VAL G  1 120 ? 149.249 -11.386 24.101  1.00 4.95  ? 119 VAL D CB  1 
ATOM   7547  C  CG1 . VAL G  1 120 ? 148.494 -10.732 25.258  1.00 7.33  ? 119 VAL D CG1 1 
ATOM   7548  C  CG2 . VAL G  1 120 ? 149.991 -12.623 24.593  1.00 6.16  ? 119 VAL D CG2 1 
ATOM   7549  N  N   . HIS G  1 121 ? 147.388 -14.053 23.077  1.00 8.50  ? 120 HIS D N   1 
ATOM   7550  C  CA  . HIS G  1 121 ? 146.362 -15.019 23.360  1.00 9.08  ? 120 HIS D CA  1 
ATOM   7551  C  C   . HIS G  1 121 ? 146.589 -15.782 24.647  1.00 13.35 ? 120 HIS D C   1 
ATOM   7552  O  O   . HIS G  1 121 ? 147.679 -15.778 25.225  1.00 14.37 ? 120 HIS D O   1 
ATOM   7553  C  CB  . HIS G  1 121 ? 146.276 -15.981 22.259  1.00 6.55  ? 120 HIS D CB  1 
ATOM   7554  C  CG  . HIS G  1 121 ? 145.514 -15.410 21.106  1.00 6.95  ? 120 HIS D CG  1 
ATOM   7555  N  ND1 . HIS G  1 121 ? 144.231 -15.508 20.821  1.00 3.66  ? 120 HIS D ND1 1 
ATOM   7556  C  CD2 . HIS G  1 121 ? 146.138 -14.693 20.107  1.00 10.22 ? 120 HIS D CD2 1 
ATOM   7557  C  CE1 . HIS G  1 121 ? 144.069 -14.881 19.678  1.00 7.24  ? 120 HIS D CE1 1 
ATOM   7558  N  NE2 . HIS G  1 121 ? 145.218 -14.384 19.241  1.00 11.81 ? 120 HIS D NE2 1 
ATOM   7559  N  N   . GLU G  1 122 ? 145.532 -16.468 25.046  1.00 16.21 ? 121 GLU D N   1 
ATOM   7560  C  CA  . GLU G  1 122 ? 145.446 -17.240 26.254  1.00 20.31 ? 121 GLU D CA  1 
ATOM   7561  C  C   . GLU G  1 122 ? 146.397 -18.403 26.331  1.00 20.98 ? 121 GLU D C   1 
ATOM   7562  O  O   . GLU G  1 122 ? 147.103 -18.592 27.338  1.00 20.41 ? 121 GLU D O   1 
ATOM   7563  C  CB  . GLU G  1 122 ? 144.040 -17.784 26.408  1.00 23.56 ? 121 GLU D CB  1 
ATOM   7564  C  CG  . GLU G  1 122 ? 143.825 -18.579 27.700  1.00 27.10 ? 121 GLU D CG  1 
ATOM   7565  C  CD  . GLU G  1 122 ? 142.416 -19.135 27.849  1.00 30.89 ? 121 GLU D CD  1 
ATOM   7566  O  OE1 . GLU G  1 122 ? 141.890 -19.749 26.919  1.00 34.48 ? 121 GLU D OE1 1 
ATOM   7567  O  OE2 . GLU G  1 122 ? 141.832 -18.962 28.917  1.00 35.53 ? 121 GLU D OE2 1 
ATOM   7568  N  N   . LYS G  1 123 ? 146.283 -19.165 25.239  1.00 21.18 ? 122 LYS D N   1 
ATOM   7569  C  CA  . LYS G  1 123 ? 146.965 -20.427 25.077  1.00 19.91 ? 122 LYS D CA  1 
ATOM   7570  C  C   . LYS G  1 123 ? 147.880 -20.332 23.892  1.00 20.08 ? 122 LYS D C   1 
ATOM   7571  O  O   . LYS G  1 123 ? 147.874 -19.396 23.084  1.00 21.99 ? 122 LYS D O   1 
ATOM   7572  C  CB  . LYS G  1 123 ? 145.973 -21.555 24.823  1.00 20.50 ? 122 LYS D CB  1 
ATOM   7573  C  CG  . LYS G  1 123 ? 145.029 -21.683 25.995  1.00 25.00 ? 122 LYS D CG  1 
ATOM   7574  C  CD  . LYS G  1 123 ? 144.165 -22.925 26.063  1.00 28.21 ? 122 LYS D CD  1 
ATOM   7575  C  CE  . LYS G  1 123 ? 143.234 -23.068 24.876  1.00 32.93 ? 122 LYS D CE  1 
ATOM   7576  N  NZ  . LYS G  1 123 ? 142.123 -23.942 25.255  1.00 36.61 ? 122 LYS D NZ  1 
ATOM   7577  N  N   . ALA G  1 124 ? 148.726 -21.331 23.873  1.00 19.94 ? 123 ALA D N   1 
ATOM   7578  C  CA  . ALA G  1 124 ? 149.641 -21.547 22.786  1.00 21.45 ? 123 ALA D CA  1 
ATOM   7579  C  C   . ALA G  1 124 ? 149.048 -21.704 21.376  1.00 21.65 ? 123 ALA D C   1 
ATOM   7580  O  O   . ALA G  1 124 ? 148.056 -22.388 21.115  1.00 22.41 ? 123 ALA D O   1 
ATOM   7581  C  CB  . ALA G  1 124 ? 150.470 -22.798 23.086  1.00 18.79 ? 123 ALA D CB  1 
ATOM   7582  N  N   . ASP G  1 125 ? 149.695 -21.045 20.434  1.00 20.98 ? 124 ASP D N   1 
ATOM   7583  C  CA  . ASP G  1 125 ? 149.379 -21.232 19.046  1.00 19.37 ? 124 ASP D CA  1 
ATOM   7584  C  C   . ASP G  1 125 ? 150.066 -22.552 18.698  1.00 19.13 ? 124 ASP D C   1 
ATOM   7585  O  O   . ASP G  1 125 ? 151.241 -22.774 19.045  1.00 19.14 ? 124 ASP D O   1 
ATOM   7586  C  CB  . ASP G  1 125 ? 149.968 -20.079 18.218  1.00 18.45 ? 124 ASP D CB  1 
ATOM   7587  C  CG  . ASP G  1 125 ? 149.516 -20.017 16.764  1.00 15.67 ? 124 ASP D CG  1 
ATOM   7588  O  OD1 . ASP G  1 125 ? 148.789 -20.898 16.343  1.00 16.24 ? 124 ASP D OD1 1 
ATOM   7589  O  OD2 . ASP G  1 125 ? 149.870 -19.079 16.057  1.00 14.27 ? 124 ASP D OD2 1 
ATOM   7590  N  N   . ASP G  1 126 ? 149.330 -23.393 17.969  1.00 18.32 ? 125 ASP D N   1 
ATOM   7591  C  CA  . ASP G  1 126 ? 149.795 -24.686 17.504  1.00 18.14 ? 125 ASP D CA  1 
ATOM   7592  C  C   . ASP G  1 126 ? 150.425 -24.574 16.114  1.00 19.26 ? 125 ASP D C   1 
ATOM   7593  O  O   . ASP G  1 126 ? 150.526 -25.539 15.355  1.00 21.12 ? 125 ASP D O   1 
ATOM   7594  C  CB  . ASP G  1 126 ? 148.597 -25.668 17.489  1.00 17.89 ? 125 ASP D CB  1 
ATOM   7595  C  CG  . ASP G  1 126 ? 147.495 -25.565 16.414  1.00 19.81 ? 125 ASP D CG  1 
ATOM   7596  O  OD1 . ASP G  1 126 ? 147.671 -24.945 15.367  1.00 18.66 ? 125 ASP D OD1 1 
ATOM   7597  O  OD2 . ASP G  1 126 ? 146.429 -26.156 16.604  1.00 20.59 ? 125 ASP D OD2 1 
ATOM   7598  N  N   . LEU G  1 127 ? 150.754 -23.374 15.663  1.00 19.57 ? 126 LEU D N   1 
ATOM   7599  C  CA  . LEU G  1 127 ? 151.337 -23.116 14.361  1.00 19.34 ? 126 LEU D CA  1 
ATOM   7600  C  C   . LEU G  1 127 ? 150.684 -23.742 13.120  1.00 21.06 ? 126 LEU D C   1 
ATOM   7601  O  O   . LEU G  1 127 ? 151.275 -23.807 12.057  1.00 21.35 ? 126 LEU D O   1 
ATOM   7602  C  CB  . LEU G  1 127 ? 152.833 -23.471 14.555  1.00 15.43 ? 126 LEU D CB  1 
ATOM   7603  C  CG  . LEU G  1 127 ? 153.476 -22.656 15.727  1.00 15.05 ? 126 LEU D CG  1 
ATOM   7604  C  CD1 . LEU G  1 127 ? 154.966 -22.878 15.806  1.00 11.34 ? 126 LEU D CD1 1 
ATOM   7605  C  CD2 . LEU G  1 127 ? 153.169 -21.158 15.523  1.00 12.70 ? 126 LEU D CD2 1 
ATOM   7606  N  N   . GLY G  1 128 ? 149.424 -24.162 13.180  1.00 24.32 ? 127 GLY D N   1 
ATOM   7607  C  CA  . GLY G  1 128 ? 148.718 -24.689 12.022  1.00 28.88 ? 127 GLY D CA  1 
ATOM   7608  C  C   . GLY G  1 128 ? 148.837 -26.198 11.878  1.00 32.86 ? 127 GLY D C   1 
ATOM   7609  O  O   . GLY G  1 128 ? 148.065 -26.869 11.174  1.00 34.05 ? 127 GLY D O   1 
ATOM   7610  N  N   . LYS G  1 129 ? 149.727 -26.813 12.630  1.00 35.65 ? 128 LYS D N   1 
ATOM   7611  C  CA  . LYS G  1 129 ? 149.891 -28.248 12.560  1.00 37.55 ? 128 LYS D CA  1 
ATOM   7612  C  C   . LYS G  1 129 ? 149.145 -29.034 13.637  1.00 38.79 ? 128 LYS D C   1 
ATOM   7613  O  O   . LYS G  1 129 ? 149.378 -30.228 13.827  1.00 39.92 ? 128 LYS D O   1 
ATOM   7614  C  CB  . LYS G  1 129 ? 151.391 -28.454 12.575  1.00 38.04 ? 128 LYS D CB  1 
ATOM   7615  C  CG  . LYS G  1 129 ? 151.923 -28.036 11.200  1.00 36.76 ? 128 LYS D CG  1 
ATOM   7616  C  CD  . LYS G  1 129 ? 153.357 -27.601 11.293  1.00 38.31 ? 128 LYS D CD  1 
ATOM   7617  C  CE  . LYS G  1 129 ? 153.333 -26.108 11.559  1.00 37.24 ? 128 LYS D CE  1 
ATOM   7618  N  NZ  . LYS G  1 129 ? 154.676 -25.598 11.730  1.00 40.77 ? 128 LYS D NZ  1 
ATOM   7619  N  N   . GLY G  1 130 ? 148.194 -28.385 14.311  1.00 40.91 ? 129 GLY D N   1 
ATOM   7620  C  CA  . GLY G  1 130 ? 147.451 -28.989 15.404  1.00 42.24 ? 129 GLY D CA  1 
ATOM   7621  C  C   . GLY G  1 130 ? 146.381 -29.949 14.941  1.00 43.47 ? 129 GLY D C   1 
ATOM   7622  O  O   . GLY G  1 130 ? 145.837 -30.675 15.778  1.00 46.52 ? 129 GLY D O   1 
ATOM   7623  N  N   . GLY G  1 131 ? 146.021 -29.903 13.656  1.00 42.73 ? 130 GLY D N   1 
ATOM   7624  C  CA  . GLY G  1 131 ? 145.086 -30.868 13.086  1.00 42.75 ? 130 GLY D CA  1 
ATOM   7625  C  C   . GLY G  1 131 ? 143.609 -30.764 13.467  1.00 42.87 ? 130 GLY D C   1 
ATOM   7626  O  O   . GLY G  1 131 ? 143.059 -31.515 14.276  1.00 43.64 ? 130 GLY D O   1 
ATOM   7627  N  N   . ASN G  1 132 ? 142.948 -29.814 12.815  1.00 41.99 ? 131 ASN D N   1 
ATOM   7628  C  CA  . ASN G  1 132 ? 141.507 -29.563 12.871  1.00 39.90 ? 131 ASN D CA  1 
ATOM   7629  C  C   . ASN G  1 132 ? 141.312 -28.310 12.040  1.00 39.50 ? 131 ASN D C   1 
ATOM   7630  O  O   . ASN G  1 132 ? 142.306 -27.624 11.743  1.00 40.14 ? 131 ASN D O   1 
ATOM   7631  C  CB  . ASN G  1 132 ? 140.950 -29.317 14.318  1.00 38.47 ? 131 ASN D CB  1 
ATOM   7632  C  CG  . ASN G  1 132 ? 141.756 -28.523 15.353  1.00 38.96 ? 131 ASN D CG  1 
ATOM   7633  O  OD1 . ASN G  1 132 ? 142.502 -27.605 15.035  1.00 39.11 ? 131 ASN D OD1 1 
ATOM   7634  N  ND2 . ASN G  1 132 ? 141.642 -28.775 16.650  1.00 38.79 ? 131 ASN D ND2 1 
ATOM   7635  N  N   . GLU G  1 133 ? 140.075 -28.024 11.601  1.00 38.45 ? 132 GLU D N   1 
ATOM   7636  C  CA  . GLU G  1 133 ? 139.712 -26.800 10.866  1.00 36.42 ? 132 GLU D CA  1 
ATOM   7637  C  C   . GLU G  1 133 ? 140.279 -25.603 11.624  1.00 34.44 ? 132 GLU D C   1 
ATOM   7638  O  O   . GLU G  1 133 ? 140.951 -24.744 11.067  1.00 32.51 ? 132 GLU D O   1 
ATOM   7639  C  CB  . GLU G  1 133 ? 138.179 -26.714 10.779  1.00 38.49 ? 132 GLU D CB  1 
ATOM   7640  C  CG  . GLU G  1 133 ? 137.556 -25.464 10.136  1.00 42.45 ? 132 GLU D CG  1 
ATOM   7641  C  CD  . GLU G  1 133 ? 136.155 -25.107 10.673  1.00 44.94 ? 132 GLU D CD  1 
ATOM   7642  O  OE1 . GLU G  1 133 ? 135.192 -25.823 10.370  1.00 46.10 ? 132 GLU D OE1 1 
ATOM   7643  O  OE2 . GLU G  1 133 ? 136.026 -24.105 11.394  1.00 43.97 ? 132 GLU D OE2 1 
ATOM   7644  N  N   . GLU G  1 134 ? 140.095 -25.604 12.948  1.00 33.71 ? 133 GLU D N   1 
ATOM   7645  C  CA  . GLU G  1 134 ? 140.617 -24.558 13.804  1.00 33.45 ? 133 GLU D CA  1 
ATOM   7646  C  C   . GLU G  1 134 ? 142.081 -24.248 13.705  1.00 32.35 ? 133 GLU D C   1 
ATOM   7647  O  O   . GLU G  1 134 ? 142.445 -23.092 13.523  1.00 33.76 ? 133 GLU D O   1 
ATOM   7648  C  CB  . GLU G  1 134 ? 140.362 -24.857 15.251  1.00 34.38 ? 133 GLU D CB  1 
ATOM   7649  C  CG  . GLU G  1 134 ? 138.975 -24.428 15.655  1.00 37.23 ? 133 GLU D CG  1 
ATOM   7650  C  CD  . GLU G  1 134 ? 138.704 -22.955 15.375  1.00 38.29 ? 133 GLU D CD  1 
ATOM   7651  O  OE1 . GLU G  1 134 ? 139.061 -22.109 16.208  1.00 37.27 ? 133 GLU D OE1 1 
ATOM   7652  O  OE2 . GLU G  1 134 ? 138.133 -22.682 14.310  1.00 40.60 ? 133 GLU D OE2 1 
ATOM   7653  N  N   . SER G  1 135 ? 142.932 -25.252 13.782  1.00 30.81 ? 134 SER D N   1 
ATOM   7654  C  CA  . SER G  1 135 ? 144.364 -25.102 13.699  1.00 29.30 ? 134 SER D CA  1 
ATOM   7655  C  C   . SER G  1 135 ? 144.759 -24.282 12.481  1.00 28.13 ? 134 SER D C   1 
ATOM   7656  O  O   . SER G  1 135 ? 145.672 -23.454 12.551  1.00 27.07 ? 134 SER D O   1 
ATOM   7657  C  CB  . SER G  1 135 ? 144.953 -26.487 13.628  1.00 29.85 ? 134 SER D CB  1 
ATOM   7658  O  OG  . SER G  1 135 ? 146.363 -26.525 13.541  1.00 29.21 ? 134 SER D OG  1 
ATOM   7659  N  N   . THR G  1 136 ? 144.039 -24.441 11.378  1.00 27.09 ? 135 THR D N   1 
ATOM   7660  C  CA  . THR G  1 136 ? 144.422 -23.746 10.171  1.00 28.52 ? 135 THR D CA  1 
ATOM   7661  C  C   . THR G  1 136 ? 143.781 -22.386 10.027  1.00 27.23 ? 135 THR D C   1 
ATOM   7662  O  O   . THR G  1 136 ? 144.137 -21.607 9.141   1.00 27.19 ? 135 THR D O   1 
ATOM   7663  C  CB  . THR G  1 136 ? 144.094 -24.655 8.993   1.00 29.87 ? 135 THR D CB  1 
ATOM   7664  O  OG1 . THR G  1 136 ? 142.712 -25.010 9.071   1.00 32.35 ? 135 THR D OG1 1 
ATOM   7665  C  CG2 . THR G  1 136 ? 145.007 -25.884 8.989   1.00 30.63 ? 135 THR D CG2 1 
ATOM   7666  N  N   . LYS G  1 137 ? 142.801 -22.127 10.890  1.00 28.28 ? 136 LYS D N   1 
ATOM   7667  C  CA  . LYS G  1 137 ? 142.171 -20.825 11.005  1.00 28.60 ? 136 LYS D CA  1 
ATOM   7668  C  C   . LYS G  1 137 ? 142.891 -19.934 12.015  1.00 26.97 ? 136 LYS D C   1 
ATOM   7669  O  O   . LYS G  1 137 ? 143.536 -18.968 11.629  1.00 27.26 ? 136 LYS D O   1 
ATOM   7670  C  CB  . LYS G  1 137 ? 140.714 -21.018 11.408  1.00 30.23 ? 136 LYS D CB  1 
ATOM   7671  C  CG  . LYS G  1 137 ? 139.791 -21.378 10.234  1.00 35.48 ? 136 LYS D CG  1 
ATOM   7672  C  CD  . LYS G  1 137 ? 138.407 -21.798 10.747  1.00 39.67 ? 136 LYS D CD  1 
ATOM   7673  C  CE  . LYS G  1 137 ? 137.738 -20.736 11.650  1.00 42.63 ? 136 LYS D CE  1 
ATOM   7674  N  NZ  . LYS G  1 137 ? 136.497 -21.192 12.272  1.00 43.57 ? 136 LYS D NZ  1 
ATOM   7675  N  N   . THR G  1 138 ? 142.931 -20.290 13.296  1.00 25.59 ? 137 THR D N   1 
ATOM   7676  C  CA  . THR G  1 138 ? 143.433 -19.451 14.383  1.00 24.44 ? 137 THR D CA  1 
ATOM   7677  C  C   . THR G  1 138 ? 144.594 -20.018 15.202  1.00 22.75 ? 137 THR D C   1 
ATOM   7678  O  O   . THR G  1 138 ? 145.065 -19.447 16.208  1.00 21.32 ? 137 THR D O   1 
ATOM   7679  C  CB  . THR G  1 138 ? 142.219 -19.155 15.303  1.00 27.23 ? 137 THR D CB  1 
ATOM   7680  O  OG1 . THR G  1 138 ? 141.669 -20.435 15.707  1.00 33.56 ? 137 THR D OG1 1 
ATOM   7681  C  CG2 . THR G  1 138 ? 141.107 -18.368 14.597  1.00 28.26 ? 137 THR D CG2 1 
ATOM   7682  N  N   . GLY G  1 139 ? 144.954 -21.256 14.799  1.00 22.10 ? 138 GLY D N   1 
ATOM   7683  C  CA  . GLY G  1 139 ? 145.962 -22.081 15.449  1.00 17.01 ? 138 GLY D CA  1 
ATOM   7684  C  C   . GLY G  1 139 ? 145.646 -22.434 16.879  1.00 15.34 ? 138 GLY D C   1 
ATOM   7685  O  O   . GLY G  1 139 ? 146.592 -22.622 17.618  1.00 15.06 ? 138 GLY D O   1 
ATOM   7686  N  N   . ASN G  1 140 ? 144.381 -22.497 17.315  1.00 15.44 ? 139 ASN D N   1 
ATOM   7687  C  CA  . ASN G  1 140 ? 143.977 -22.826 18.699  1.00 14.91 ? 139 ASN D CA  1 
ATOM   7688  C  C   . ASN G  1 140 ? 144.567 -22.001 19.860  1.00 13.78 ? 139 ASN D C   1 
ATOM   7689  O  O   . ASN G  1 140 ? 144.746 -22.496 20.978  1.00 16.31 ? 139 ASN D O   1 
ATOM   7690  C  CB  . ASN G  1 140 ? 144.240 -24.329 18.943  1.00 13.80 ? 139 ASN D CB  1 
ATOM   7691  C  CG  . ASN G  1 140 ? 143.265 -25.192 18.165  1.00 14.64 ? 139 ASN D CG  1 
ATOM   7692  O  OD1 . ASN G  1 140 ? 142.074 -24.914 18.108  1.00 16.16 ? 139 ASN D OD1 1 
ATOM   7693  N  ND2 . ASN G  1 140 ? 143.680 -26.266 17.504  1.00 16.69 ? 139 ASN D ND2 1 
ATOM   7694  N  N   . ALA G  1 141 ? 144.776 -20.699 19.656  1.00 10.04 ? 140 ALA D N   1 
ATOM   7695  C  CA  . ALA G  1 141 ? 145.368 -19.886 20.675  1.00 9.61  ? 140 ALA D CA  1 
ATOM   7696  C  C   . ALA G  1 141 ? 144.398 -19.408 21.780  1.00 10.55 ? 140 ALA D C   1 
ATOM   7697  O  O   . ALA G  1 141 ? 144.783 -18.783 22.808  1.00 8.79  ? 140 ALA D O   1 
ATOM   7698  C  CB  . ALA G  1 141 ? 146.023 -18.748 19.922  1.00 11.12 ? 140 ALA D CB  1 
ATOM   7699  N  N   . GLY G  1 142 ? 143.097 -19.657 21.579  1.00 8.06  ? 141 GLY D N   1 
ATOM   7700  C  CA  . GLY G  1 142 ? 142.142 -19.390 22.640  1.00 9.47  ? 141 GLY D CA  1 
ATOM   7701  C  C   . GLY G  1 142 ? 141.847 -17.924 22.837  1.00 13.00 ? 141 GLY D C   1 
ATOM   7702  O  O   . GLY G  1 142 ? 141.982 -17.121 21.907  1.00 16.84 ? 141 GLY D O   1 
ATOM   7703  N  N   . SER G  1 143 ? 141.527 -17.490 24.054  1.00 13.29 ? 142 SER D N   1 
ATOM   7704  C  CA  . SER G  1 143 ? 141.020 -16.129 24.257  1.00 10.38 ? 142 SER D CA  1 
ATOM   7705  C  C   . SER G  1 143 ? 142.051 -15.105 23.934  1.00 7.53  ? 142 SER D C   1 
ATOM   7706  O  O   . SER G  1 143 ? 143.222 -15.377 24.165  1.00 5.54  ? 142 SER D O   1 
ATOM   7707  C  CB  . SER G  1 143 ? 140.596 -15.892 25.701  1.00 12.24 ? 142 SER D CB  1 
ATOM   7708  O  OG  . SER G  1 143 ? 139.707 -16.927 26.085  1.00 19.82 ? 142 SER D OG  1 
ATOM   7709  N  N   . ARG G  1 144 ? 141.618 -13.943 23.451  1.00 8.24  ? 143 ARG D N   1 
ATOM   7710  C  CA  . ARG G  1 144 ? 142.502 -12.809 23.148  1.00 6.98  ? 143 ARG D CA  1 
ATOM   7711  C  C   . ARG G  1 144 ? 142.658 -12.273 24.549  1.00 6.14  ? 143 ARG D C   1 
ATOM   7712  O  O   . ARG G  1 144 ? 141.629 -11.908 25.086  1.00 8.59  ? 143 ARG D O   1 
ATOM   7713  C  CB  . ARG G  1 144 ? 141.771 -11.836 22.220  1.00 6.45  ? 143 ARG D CB  1 
ATOM   7714  C  CG  . ARG G  1 144 ? 141.133 -12.543 21.025  1.00 5.94  ? 143 ARG D CG  1 
ATOM   7715  C  CD  . ARG G  1 144 ? 140.610 -11.674 19.925  1.00 8.10  ? 143 ARG D CD  1 
ATOM   7716  N  NE  . ARG G  1 144 ? 140.146 -12.503 18.815  1.00 14.96 ? 143 ARG D NE  1 
ATOM   7717  C  CZ  . ARG G  1 144 ? 139.651 -12.011 17.665  1.00 16.31 ? 143 ARG D CZ  1 
ATOM   7718  N  NH1 . ARG G  1 144 ? 139.536 -10.698 17.422  1.00 20.43 ? 143 ARG D NH1 1 
ATOM   7719  N  NH2 . ARG G  1 144 ? 139.215 -12.850 16.735  1.00 16.72 ? 143 ARG D NH2 1 
ATOM   7720  N  N   . LEU G  1 145 ? 143.800 -12.285 25.220  1.00 5.79  ? 144 LEU D N   1 
ATOM   7721  C  CA  . LEU G  1 145 ? 143.815 -11.885 26.621  1.00 5.40  ? 144 LEU D CA  1 
ATOM   7722  C  C   . LEU G  1 145 ? 143.973 -10.427 26.793  1.00 4.48  ? 144 LEU D C   1 
ATOM   7723  O  O   . LEU G  1 145 ? 143.472 -9.887  27.755  1.00 5.90  ? 144 LEU D O   1 
ATOM   7724  C  CB  . LEU G  1 145 ? 144.945 -12.427 27.436  1.00 6.25  ? 144 LEU D CB  1 
ATOM   7725  C  CG  . LEU G  1 145 ? 144.959 -13.887 27.688  1.00 8.90  ? 144 LEU D CG  1 
ATOM   7726  C  CD1 . LEU G  1 145 ? 146.297 -14.240 28.302  1.00 10.67 ? 144 LEU D CD1 1 
ATOM   7727  C  CD2 . LEU G  1 145 ? 143.777 -14.272 28.530  1.00 8.66  ? 144 LEU D CD2 1 
ATOM   7728  N  N   . ALA G  1 146 ? 144.820 -9.846  25.975  1.00 4.06  ? 145 ALA D N   1 
ATOM   7729  C  CA  . ALA G  1 146 ? 145.048 -8.421  25.923  1.00 5.21  ? 145 ALA D CA  1 
ATOM   7730  C  C   . ALA G  1 146 ? 145.271 -8.110  24.431  1.00 6.57  ? 145 ALA D C   1 
ATOM   7731  O  O   . ALA G  1 146 ? 145.617 -8.987  23.611  1.00 7.69  ? 145 ALA D O   1 
ATOM   7732  C  CB  . ALA G  1 146 ? 146.294 -8.061  26.692  1.00 3.74  ? 145 ALA D CB  1 
ATOM   7733  N  N   . CYS G  1 147 ? 145.076 -6.893  23.988  1.00 5.79  ? 146 CYS D N   1 
ATOM   7734  C  CA  . CYS G  1 147 ? 145.286 -6.560  22.599  1.00 4.66  ? 146 CYS D CA  1 
ATOM   7735  C  C   . CYS G  1 147 ? 145.430 -5.053  22.505  1.00 5.10  ? 146 CYS D C   1 
ATOM   7736  O  O   . CYS G  1 147 ? 145.064 -4.375  23.477  1.00 2.41  ? 146 CYS D O   1 
ATOM   7737  C  CB  . CYS G  1 147 ? 144.098 -7.031  21.769  1.00 5.81  ? 146 CYS D CB  1 
ATOM   7738  S  SG  . CYS G  1 147 ? 142.498 -6.280  22.099  1.00 9.52  ? 146 CYS D SG  1 
ATOM   7739  N  N   . GLY G  1 148 ? 146.023 -4.556  21.403  1.00 3.42  ? 147 GLY D N   1 
ATOM   7740  C  CA  . GLY G  1 148 ? 146.206 -3.145  21.203  1.00 3.36  ? 147 GLY D CA  1 
ATOM   7741  C  C   . GLY G  1 148 ? 146.423 -2.769  19.766  1.00 4.68  ? 147 GLY D C   1 
ATOM   7742  O  O   . GLY G  1 148 ? 147.022 -3.524  19.017  1.00 5.46  ? 147 GLY D O   1 
ATOM   7743  N  N   . VAL G  1 149 ? 145.978 -1.567  19.391  1.00 7.38  ? 148 VAL D N   1 
ATOM   7744  C  CA  . VAL G  1 149 ? 146.050 -1.046  18.021  1.00 4.45  ? 148 VAL D CA  1 
ATOM   7745  C  C   . VAL G  1 149 ? 147.465 -0.608  17.747  1.00 5.58  ? 148 VAL D C   1 
ATOM   7746  O  O   . VAL G  1 149 ? 148.003 0.052   18.636  1.00 7.29  ? 148 VAL D O   1 
ATOM   7747  C  CB  . VAL G  1 149 ? 145.082 0.112   17.924  1.00 2.57  ? 148 VAL D CB  1 
ATOM   7748  C  CG1 . VAL G  1 149 ? 145.243 0.860   16.620  1.00 3.67  ? 148 VAL D CG1 1 
ATOM   7749  C  CG2 . VAL G  1 149 ? 143.672 -0.451  18.028  1.00 2.00  ? 148 VAL D CG2 1 
ATOM   7750  N  N   . ILE G  1 150 ? 148.079 -0.913  16.593  1.00 5.72  ? 149 ILE D N   1 
ATOM   7751  C  CA  . ILE G  1 150 ? 149.485 -0.583  16.271  1.00 3.40  ? 149 ILE D CA  1 
ATOM   7752  C  C   . ILE G  1 150 ? 149.480 0.814   15.725  1.00 4.52  ? 149 ILE D C   1 
ATOM   7753  O  O   . ILE G  1 150 ? 148.729 1.091   14.784  1.00 4.25  ? 149 ILE D O   1 
ATOM   7754  C  CB  . ILE G  1 150 ? 150.075 -1.552  15.210  1.00 2.00  ? 149 ILE D CB  1 
ATOM   7755  C  CG1 . ILE G  1 150 ? 150.109 -2.917  15.859  1.00 2.00  ? 149 ILE D CG1 1 
ATOM   7756  C  CG2 . ILE G  1 150 ? 151.511 -1.211  14.801  1.00 2.00  ? 149 ILE D CG2 1 
ATOM   7757  C  CD1 . ILE G  1 150 ? 150.335 -4.117  14.977  1.00 2.00  ? 149 ILE D CD1 1 
ATOM   7758  N  N   . GLY G  1 151 ? 150.256 1.725   16.286  1.00 5.19  ? 150 GLY D N   1 
ATOM   7759  C  CA  . GLY G  1 151 ? 150.229 3.097   15.816  1.00 6.66  ? 150 GLY D CA  1 
ATOM   7760  C  C   . GLY G  1 151 ? 151.617 3.586   15.500  1.00 6.44  ? 150 GLY D C   1 
ATOM   7761  O  O   . GLY G  1 151 ? 152.622 3.033   15.932  1.00 5.27  ? 150 GLY D O   1 
ATOM   7762  N  N   . ILE G  1 152 ? 151.683 4.655   14.747  1.00 6.52  ? 151 ILE D N   1 
ATOM   7763  C  CA  . ILE G  1 152 ? 152.965 5.174   14.314  1.00 8.06  ? 151 ILE D CA  1 
ATOM   7764  C  C   . ILE G  1 152 ? 153.729 5.711   15.489  1.00 8.54  ? 151 ILE D C   1 
ATOM   7765  O  O   . ILE G  1 152 ? 153.072 6.207   16.396  1.00 11.96 ? 151 ILE D O   1 
ATOM   7766  C  CB  . ILE G  1 152 ? 152.738 6.275   13.245  1.00 4.71  ? 151 ILE D CB  1 
ATOM   7767  C  CG1 . ILE G  1 152 ? 151.946 5.641   12.103  1.00 4.97  ? 151 ILE D CG1 1 
ATOM   7768  C  CG2 . ILE G  1 152 ? 154.044 6.805   12.712  1.00 2.00  ? 151 ILE D CG2 1 
ATOM   7769  C  CD1 . ILE G  1 152 ? 151.770 6.399   10.784  1.00 8.45  ? 151 ILE D CD1 1 
ATOM   7770  N  N   . ALA G  1 153 ? 155.046 5.620   15.517  1.00 10.94 ? 152 ALA D N   1 
ATOM   7771  C  CA  . ALA G  1 153 ? 155.860 6.163   16.574  1.00 14.49 ? 152 ALA D CA  1 
ATOM   7772  C  C   . ALA G  1 153 ? 157.105 6.739   15.926  1.00 19.13 ? 152 ALA D C   1 
ATOM   7773  O  O   . ALA G  1 153 ? 157.382 6.426   14.746  1.00 21.71 ? 152 ALA D O   1 
ATOM   7774  C  CB  . ALA G  1 153 ? 156.248 5.069   17.538  1.00 12.66 ? 152 ALA D CB  1 
ATOM   7775  N  N   . GLN G  1 154 ? 157.851 7.567   16.662  1.00 23.99 ? 153 GLN D N   1 
ATOM   7776  C  CA  . GLN G  1 154 ? 159.028 8.209   16.086  1.00 30.48 ? 153 GLN D CA  1 
ATOM   7777  C  C   . GLN G  1 154 ? 160.339 7.610   16.579  1.00 34.00 ? 153 GLN D C   1 
ATOM   7778  O  O   . GLN G  1 154 ? 161.343 7.809   15.871  1.00 37.27 ? 153 GLN D O   1 
ATOM   7779  C  CB  . GLN G  1 154 ? 159.020 9.714   16.400  1.00 31.86 ? 153 GLN D CB  1 
ATOM   7780  C  CG  . GLN G  1 154 ? 159.912 10.291  17.516  1.00 33.50 ? 153 GLN D CG  1 
ATOM   7781  C  CD  . GLN G  1 154 ? 159.138 11.130  18.508  1.00 33.69 ? 153 GLN D CD  1 
ATOM   7782  O  OE1 . GLN G  1 154 ? 158.493 10.632  19.439  1.00 36.42 ? 153 GLN D OE1 1 
ATOM   7783  N  NE2 . GLN G  1 154 ? 159.149 12.445  18.301  1.00 33.33 ? 153 GLN D NE2 1 
ATOM   7784  O  OXT . GLN G  1 154 ? 160.322 6.997   17.671  1.00 38.06 ? 153 GLN D OXT 1 
HETATM 7785  C  C   . ACE H  1 1   ? 143.052 2.076   4.461   1.00 41.92 ? 0   ACE I C   1 
HETATM 7786  O  O   . ACE H  1 1   ? 142.975 0.833   4.621   1.00 45.20 ? 0   ACE I O   1 
HETATM 7787  C  CH3 . ACE H  1 1   ? 144.428 2.732   4.277   1.00 41.83 ? 0   ACE I CH3 1 
ATOM   7788  N  N   . ALA H  1 2   ? 141.944 2.837   4.430   1.00 37.87 ? 1   ALA I N   1 
ATOM   7789  C  CA  . ALA H  1 2   ? 140.628 2.243   4.640   1.00 34.89 ? 1   ALA I CA  1 
ATOM   7790  C  C   . ALA H  1 2   ? 139.524 3.133   4.094   1.00 30.82 ? 1   ALA I C   1 
ATOM   7791  O  O   . ALA H  1 2   ? 139.780 4.001   3.268   1.00 31.83 ? 1   ALA I O   1 
ATOM   7792  C  CB  . ALA H  1 2   ? 140.384 2.003   6.151   1.00 34.07 ? 1   ALA I CB  1 
ATOM   7793  N  N   . THR H  1 3   ? 138.275 2.813   4.405   1.00 27.21 ? 2   THR I N   1 
ATOM   7794  C  CA  . THR H  1 3   ? 137.169 3.670   4.080   1.00 23.15 ? 2   THR I CA  1 
ATOM   7795  C  C   . THR H  1 3   ? 136.511 3.865   5.422   1.00 19.98 ? 2   THR I C   1 
ATOM   7796  O  O   . THR H  1 3   ? 135.906 4.899   5.646   1.00 21.69 ? 2   THR I O   1 
ATOM   7797  C  CB  . THR H  1 3   ? 136.185 3.017   3.053   1.00 23.98 ? 2   THR I CB  1 
ATOM   7798  O  OG1 . THR H  1 3   ? 135.806 1.721   3.522   1.00 26.33 ? 2   THR I OG1 1 
ATOM   7799  C  CG2 . THR H  1 3   ? 136.829 2.943   1.663   1.00 23.84 ? 2   THR I CG2 1 
ATOM   7800  N  N   . LYS H  1 4   ? 136.546 2.906   6.335   1.00 17.28 ? 3   LYS I N   1 
ATOM   7801  C  CA  . LYS H  1 4   ? 136.060 3.131   7.658   1.00 15.61 ? 3   LYS I CA  1 
ATOM   7802  C  C   . LYS H  1 4   ? 137.240 3.013   8.633   1.00 13.07 ? 3   LYS I C   1 
ATOM   7803  O  O   . LYS H  1 4   ? 138.130 2.190   8.415   1.00 11.70 ? 3   LYS I O   1 
ATOM   7804  C  CB  . LYS H  1 4   ? 135.000 2.103   7.927   1.00 18.09 ? 3   LYS I CB  1 
ATOM   7805  C  CG  . LYS H  1 4   ? 133.671 2.408   7.241   1.00 24.46 ? 3   LYS I CG  1 
ATOM   7806  C  CD  . LYS H  1 4   ? 132.496 1.510   7.684   1.00 27.40 ? 3   LYS I CD  1 
ATOM   7807  C  CE  . LYS H  1 4   ? 132.218 1.575   9.201   1.00 29.50 ? 3   LYS I CE  1 
ATOM   7808  N  NZ  . LYS H  1 4   ? 131.107 0.694   9.547   1.00 31.87 ? 3   LYS I NZ  1 
ATOM   7809  N  N   . ALA H  1 5   ? 137.314 3.849   9.663   1.00 9.63  ? 4   ALA I N   1 
ATOM   7810  C  CA  . ALA H  1 5   ? 138.266 3.747   10.757  1.00 4.84  ? 4   ALA I CA  1 
ATOM   7811  C  C   . ALA H  1 5   ? 137.507 4.069   12.065  1.00 3.94  ? 4   ALA I C   1 
ATOM   7812  O  O   . ALA H  1 5   ? 136.268 4.295   12.050  1.00 2.84  ? 4   ALA I O   1 
ATOM   7813  C  CB  . ALA H  1 5   ? 139.394 4.725   10.572  1.00 5.13  ? 4   ALA I CB  1 
ATOM   7814  N  N   . VAL H  1 6   ? 138.145 3.981   13.234  1.00 2.00  ? 5   VAL I N   1 
ATOM   7815  C  CA  . VAL H  1 6   ? 137.505 4.195   14.510  1.00 2.00  ? 5   VAL I CA  1 
ATOM   7816  C  C   . VAL H  1 6   ? 138.623 4.442   15.466  1.00 2.00  ? 5   VAL I C   1 
ATOM   7817  O  O   . VAL H  1 6   ? 139.734 4.054   15.141  1.00 2.00  ? 5   VAL I O   1 
ATOM   7818  C  CB  . VAL H  1 6   ? 136.666 2.943   14.918  1.00 2.24  ? 5   VAL I CB  1 
ATOM   7819  C  CG1 . VAL H  1 6   ? 137.552 1.763   15.233  1.00 2.00  ? 5   VAL I CG1 1 
ATOM   7820  C  CG2 . VAL H  1 6   ? 135.773 3.297   16.091  1.00 2.00  ? 5   VAL I CG2 1 
ATOM   7821  N  N   . ALA H  1 7   ? 138.340 5.117   16.585  1.00 4.30  ? 6   ALA I N   1 
ATOM   7822  C  CA  . ALA H  1 7   ? 139.257 5.515   17.643  1.00 2.00  ? 6   ALA I CA  1 
ATOM   7823  C  C   . ALA H  1 7   ? 138.475 5.476   18.937  1.00 2.00  ? 6   ALA I C   1 
ATOM   7824  O  O   . ALA H  1 7   ? 137.458 6.163   19.069  1.00 2.18  ? 6   ALA I O   1 
ATOM   7825  C  CB  . ALA H  1 7   ? 139.723 6.941   17.516  1.00 2.00  ? 6   ALA I CB  1 
ATOM   7826  N  N   . VAL H  1 8   ? 138.907 4.677   19.888  1.00 2.00  ? 7   VAL I N   1 
ATOM   7827  C  CA  . VAL H  1 8   ? 138.244 4.591   21.172  1.00 2.62  ? 7   VAL I CA  1 
ATOM   7828  C  C   . VAL H  1 8   ? 138.957 5.563   22.068  1.00 2.98  ? 7   VAL I C   1 
ATOM   7829  O  O   . VAL H  1 8   ? 140.114 5.365   22.399  1.00 5.00  ? 7   VAL I O   1 
ATOM   7830  C  CB  . VAL H  1 8   ? 138.365 3.189   21.737  1.00 2.00  ? 7   VAL I CB  1 
ATOM   7831  C  CG1 . VAL H  1 8   ? 137.861 3.067   23.176  1.00 2.36  ? 7   VAL I CG1 1 
ATOM   7832  C  CG2 . VAL H  1 8   ? 137.549 2.319   20.814  1.00 2.00  ? 7   VAL I CG2 1 
ATOM   7833  N  N   . LEU H  1 9   ? 138.317 6.631   22.462  1.00 3.93  ? 8   LEU I N   1 
ATOM   7834  C  CA  . LEU H  1 9   ? 138.953 7.585   23.325  1.00 5.31  ? 8   LEU I CA  1 
ATOM   7835  C  C   . LEU H  1 9   ? 138.813 7.197   24.792  1.00 8.48  ? 8   LEU I C   1 
ATOM   7836  O  O   . LEU H  1 9   ? 137.719 6.984   25.316  1.00 7.95  ? 8   LEU I O   1 
ATOM   7837  C  CB  . LEU H  1 9   ? 138.320 8.901   23.012  1.00 4.43  ? 8   LEU I CB  1 
ATOM   7838  C  CG  . LEU H  1 9   ? 138.911 9.667   21.861  1.00 2.00  ? 8   LEU I CG  1 
ATOM   7839  C  CD1 . LEU H  1 9   ? 138.991 8.940   20.564  1.00 4.30  ? 8   LEU I CD1 1 
ATOM   7840  C  CD2 . LEU H  1 9   ? 137.962 10.770  21.643  1.00 3.98  ? 8   LEU I CD2 1 
ATOM   7841  N  N   . LYS H  1 10  ? 139.936 7.057   25.477  1.00 12.36 ? 9   LYS I N   1 
ATOM   7842  C  CA  . LYS H  1 10  ? 140.002 6.793   26.910  1.00 15.74 ? 9   LYS I CA  1 
ATOM   7843  C  C   . LYS H  1 10  ? 141.012 7.823   27.368  1.00 18.75 ? 9   LYS I C   1 
ATOM   7844  O  O   . LYS H  1 10  ? 141.843 8.294   26.580  1.00 18.93 ? 9   LYS I O   1 
ATOM   7845  C  CB  . LYS H  1 10  ? 140.584 5.419   27.282  1.00 15.85 ? 9   LYS I CB  1 
ATOM   7846  C  CG  . LYS H  1 10  ? 139.801 4.119   26.947  1.00 19.54 ? 9   LYS I CG  1 
ATOM   7847  C  CD  . LYS H  1 10  ? 138.625 3.833   27.893  1.00 23.40 ? 9   LYS I CD  1 
ATOM   7848  C  CE  . LYS H  1 10  ? 137.380 3.273   27.166  1.00 28.03 ? 9   LYS I CE  1 
ATOM   7849  N  NZ  . LYS H  1 10  ? 136.695 4.183   26.226  1.00 27.85 ? 9   LYS I NZ  1 
ATOM   7850  N  N   . GLY H  1 11  ? 140.994 8.223   28.629  1.00 22.37 ? 10  GLY I N   1 
ATOM   7851  C  CA  . GLY H  1 11  ? 142.003 9.145   29.128  1.00 25.37 ? 10  GLY I CA  1 
ATOM   7852  C  C   . GLY H  1 11  ? 142.324 8.912   30.604  1.00 27.56 ? 10  GLY I C   1 
ATOM   7853  O  O   . GLY H  1 11  ? 142.162 7.820   31.162  1.00 28.09 ? 10  GLY I O   1 
ATOM   7854  N  N   . ASP H  1 12  ? 142.777 9.984   31.252  1.00 29.50 ? 11  ASP I N   1 
ATOM   7855  C  CA  . ASP H  1 12  ? 143.078 9.941   32.680  1.00 30.25 ? 11  ASP I CA  1 
ATOM   7856  C  C   . ASP H  1 12  ? 141.893 10.180  33.652  1.00 28.06 ? 11  ASP I C   1 
ATOM   7857  O  O   . ASP H  1 12  ? 142.033 9.981   34.866  1.00 30.93 ? 11  ASP I O   1 
ATOM   7858  C  CB  . ASP H  1 12  ? 144.147 10.975  32.964  1.00 33.43 ? 11  ASP I CB  1 
ATOM   7859  C  CG  . ASP H  1 12  ? 145.364 10.443  33.703  1.00 36.71 ? 11  ASP I CG  1 
ATOM   7860  O  OD1 . ASP H  1 12  ? 145.225 9.790   34.745  1.00 40.67 ? 11  ASP I OD1 1 
ATOM   7861  O  OD2 . ASP H  1 12  ? 146.470 10.709  33.226  1.00 40.10 ? 11  ASP I OD2 1 
ATOM   7862  N  N   . GLY H  1 13  ? 140.703 10.572  33.196  1.00 22.25 ? 12  GLY I N   1 
ATOM   7863  C  CA  . GLY H  1 13  ? 139.663 10.976  34.105  1.00 15.92 ? 12  GLY I CA  1 
ATOM   7864  C  C   . GLY H  1 13  ? 138.365 10.412  33.604  1.00 12.50 ? 12  GLY I C   1 
ATOM   7865  O  O   . GLY H  1 13  ? 138.379 9.300   33.112  1.00 14.87 ? 12  GLY I O   1 
ATOM   7866  N  N   . PRO H  1 14  ? 137.240 11.114  33.654  1.00 8.33  ? 13  PRO I N   1 
ATOM   7867  C  CA  . PRO H  1 14  ? 135.938 10.650  33.241  1.00 6.28  ? 13  PRO I CA  1 
ATOM   7868  C  C   . PRO H  1 14  ? 135.613 10.480  31.791  1.00 5.01  ? 13  PRO I C   1 
ATOM   7869  O  O   . PRO H  1 14  ? 134.691 9.705   31.464  1.00 5.64  ? 13  PRO I O   1 
ATOM   7870  C  CB  . PRO H  1 14  ? 134.983 11.599  33.886  1.00 7.85  ? 13  PRO I CB  1 
ATOM   7871  C  CG  . PRO H  1 14  ? 135.736 12.878  33.829  1.00 9.17  ? 13  PRO I CG  1 
ATOM   7872  C  CD  . PRO H  1 14  ? 137.114 12.399  34.308  1.00 10.70 ? 13  PRO I CD  1 
ATOM   7873  N  N   . VAL H  1 15  ? 136.395 11.125  30.927  1.00 4.07  ? 14  VAL I N   1 
ATOM   7874  C  CA  . VAL H  1 15  ? 136.017 11.091  29.529  1.00 5.88  ? 14  VAL I CA  1 
ATOM   7875  C  C   . VAL H  1 15  ? 136.509 9.888   28.754  1.00 6.28  ? 14  VAL I C   1 
ATOM   7876  O  O   . VAL H  1 15  ? 137.636 9.414   28.900  1.00 7.20  ? 14  VAL I O   1 
ATOM   7877  C  CB  . VAL H  1 15  ? 136.408 12.415  28.779  1.00 3.74  ? 14  VAL I CB  1 
ATOM   7878  C  CG1 . VAL H  1 15  ? 137.100 13.386  29.714  1.00 5.22  ? 14  VAL I CG1 1 
ATOM   7879  C  CG2 . VAL H  1 15  ? 137.236 12.125  27.574  1.00 2.00  ? 14  VAL I CG2 1 
ATOM   7880  N  N   . GLN H  1 16  ? 135.507 9.367   28.046  1.00 5.88  ? 15  GLN I N   1 
ATOM   7881  C  CA  . GLN H  1 16  ? 135.687 8.311   27.106  1.00 7.14  ? 15  GLN I CA  1 
ATOM   7882  C  C   . GLN H  1 16  ? 134.644 8.504   26.024  1.00 7.84  ? 15  GLN I C   1 
ATOM   7883  O  O   . GLN H  1 16  ? 133.601 9.129   26.239  1.00 9.04  ? 15  GLN I O   1 
ATOM   7884  C  CB  . GLN H  1 16  ? 135.431 6.966   27.659  1.00 11.90 ? 15  GLN I CB  1 
ATOM   7885  C  CG  . GLN H  1 16  ? 135.505 6.736   29.173  1.00 20.37 ? 15  GLN I CG  1 
ATOM   7886  C  CD  . GLN H  1 16  ? 134.106 6.577   29.728  1.00 22.78 ? 15  GLN I CD  1 
ATOM   7887  O  OE1 . GLN H  1 16  ? 133.247 6.104   28.969  1.00 23.32 ? 15  GLN I OE1 1 
ATOM   7888  N  NE2 . GLN H  1 16  ? 133.801 6.981   30.976  1.00 22.33 ? 15  GLN I NE2 1 
ATOM   7889  N  N   . GLY H  1 17  ? 134.923 7.984   24.833  1.00 6.81  ? 16  GLY I N   1 
ATOM   7890  C  CA  . GLY H  1 17  ? 134.029 8.047   23.709  1.00 3.60  ? 16  GLY I CA  1 
ATOM   7891  C  C   . GLY H  1 17  ? 134.518 7.087   22.636  1.00 2.00  ? 16  GLY I C   1 
ATOM   7892  O  O   . GLY H  1 17  ? 135.618 6.556   22.719  1.00 2.00  ? 16  GLY I O   1 
ATOM   7893  N  N   . ILE H  1 18  ? 133.727 6.839   21.627  1.00 2.00  ? 17  ILE I N   1 
ATOM   7894  C  CA  . ILE H  1 18  ? 134.125 6.059   20.463  1.00 2.98  ? 17  ILE I CA  1 
ATOM   7895  C  C   . ILE H  1 18  ? 133.931 7.039   19.310  1.00 3.03  ? 17  ILE I C   1 
ATOM   7896  O  O   . ILE H  1 18  ? 132.817 7.558   19.180  1.00 2.00  ? 17  ILE I O   1 
ATOM   7897  C  CB  . ILE H  1 18  ? 133.190 4.831   20.216  1.00 3.43  ? 17  ILE I CB  1 
ATOM   7898  C  CG1 . ILE H  1 18  ? 133.423 3.882   21.338  1.00 2.00  ? 17  ILE I CG1 1 
ATOM   7899  C  CG2 . ILE H  1 18  ? 133.409 4.193   18.836  1.00 2.00  ? 17  ILE I CG2 1 
ATOM   7900  C  CD1 . ILE H  1 18  ? 132.286 2.921   21.449  1.00 2.00  ? 17  ILE I CD1 1 
ATOM   7901  N  N   . ILE H  1 19  ? 134.909 7.357   18.472  1.00 2.94  ? 18  ILE I N   1 
ATOM   7902  C  CA  . ILE H  1 19  ? 134.670 8.236   17.323  1.00 3.85  ? 18  ILE I CA  1 
ATOM   7903  C  C   . ILE H  1 19  ? 134.814 7.392   16.064  1.00 3.39  ? 18  ILE I C   1 
ATOM   7904  O  O   . ILE H  1 19  ? 135.779 6.624   15.964  1.00 4.30  ? 18  ILE I O   1 
ATOM   7905  C  CB  . ILE H  1 19  ? 135.705 9.378   17.351  1.00 4.79  ? 18  ILE I CB  1 
ATOM   7906  C  CG1 . ILE H  1 19  ? 135.510 10.186  18.613  1.00 4.62  ? 18  ILE I CG1 1 
ATOM   7907  C  CG2 . ILE H  1 19  ? 135.570 10.258  16.124  1.00 3.55  ? 18  ILE I CG2 1 
ATOM   7908  C  CD1 . ILE H  1 19  ? 134.084 10.758  18.598  1.00 11.49 ? 18  ILE I CD1 1 
ATOM   7909  N  N   . ASN H  1 20  ? 133.908 7.479   15.102  1.00 3.60  ? 19  ASN I N   1 
ATOM   7910  C  CA  . ASN H  1 20  ? 133.996 6.731   13.846  1.00 2.26  ? 19  ASN I CA  1 
ATOM   7911  C  C   . ASN H  1 20  ? 134.349 7.621   12.709  1.00 2.00  ? 19  ASN I C   1 
ATOM   7912  O  O   . ASN H  1 20  ? 133.869 8.738   12.685  1.00 2.00  ? 19  ASN I O   1 
ATOM   7913  C  CB  . ASN H  1 20  ? 132.716 6.100   13.408  1.00 2.00  ? 19  ASN I CB  1 
ATOM   7914  C  CG  . ASN H  1 20  ? 132.223 5.127   14.429  1.00 2.77  ? 19  ASN I CG  1 
ATOM   7915  O  OD1 . ASN H  1 20  ? 131.480 5.576   15.273  1.00 2.00  ? 19  ASN I OD1 1 
ATOM   7916  N  ND2 . ASN H  1 20  ? 132.541 3.826   14.464  1.00 4.60  ? 19  ASN I ND2 1 
ATOM   7917  N  N   . PHE H  1 21  ? 135.071 7.098   11.733  1.00 2.00  ? 20  PHE I N   1 
ATOM   7918  C  CA  . PHE H  1 21  ? 135.529 7.805   10.556  1.00 4.46  ? 20  PHE I CA  1 
ATOM   7919  C  C   . PHE H  1 21  ? 135.068 7.160   9.248   1.00 7.95  ? 20  PHE I C   1 
ATOM   7920  O  O   . PHE H  1 21  ? 135.254 5.939   9.096   1.00 11.04 ? 20  PHE I O   1 
ATOM   7921  C  CB  . PHE H  1 21  ? 137.044 7.821   10.511  1.00 4.96  ? 20  PHE I CB  1 
ATOM   7922  C  CG  . PHE H  1 21  ? 137.701 8.709   11.539  1.00 2.59  ? 20  PHE I CG  1 
ATOM   7923  C  CD1 . PHE H  1 21  ? 137.950 8.205   12.790  1.00 2.00  ? 20  PHE I CD1 1 
ATOM   7924  C  CD2 . PHE H  1 21  ? 138.037 9.996   11.189  1.00 3.74  ? 20  PHE I CD2 1 
ATOM   7925  C  CE1 . PHE H  1 21  ? 138.550 9.001   13.718  1.00 2.00  ? 20  PHE I CE1 1 
ATOM   7926  C  CE2 . PHE H  1 21  ? 138.640 10.791  12.132  1.00 9.00  ? 20  PHE I CE2 1 
ATOM   7927  C  CZ  . PHE H  1 21  ? 138.880 10.300  13.403  1.00 8.74  ? 20  PHE I CZ  1 
ATOM   7928  N  N   . GLU H  1 22  ? 134.545 7.846   8.229   1.00 10.13 ? 21  GLU I N   1 
ATOM   7929  C  CA  . GLU H  1 22  ? 134.152 7.129   7.030   1.00 11.30 ? 21  GLU I CA  1 
ATOM   7930  C  C   . GLU H  1 22  ? 134.493 7.952   5.816   1.00 10.98 ? 21  GLU I C   1 
ATOM   7931  O  O   . GLU H  1 22  ? 134.155 9.124   5.780   1.00 12.16 ? 21  GLU I O   1 
ATOM   7932  C  CB  . GLU H  1 22  ? 132.674 6.856   7.098   1.00 15.37 ? 21  GLU I CB  1 
ATOM   7933  C  CG  . GLU H  1 22  ? 132.231 5.947   5.955   1.00 22.60 ? 21  GLU I CG  1 
ATOM   7934  C  CD  . GLU H  1 22  ? 130.813 5.397   6.046   1.00 26.60 ? 21  GLU I CD  1 
ATOM   7935  O  OE1 . GLU H  1 22  ? 129.896 5.943   6.681   1.00 27.28 ? 21  GLU I OE1 1 
ATOM   7936  O  OE2 . GLU H  1 22  ? 130.638 4.355   5.430   1.00 32.99 ? 21  GLU I OE2 1 
ATOM   7937  N  N   . GLN H  1 23  ? 135.123 7.380   4.803   1.00 8.30  ? 22  GLN I N   1 
ATOM   7938  C  CA  . GLN H  1 23  ? 135.636 8.074   3.668   1.00 6.81  ? 22  GLN I CA  1 
ATOM   7939  C  C   . GLN H  1 23  ? 135.088 7.280   2.528   1.00 10.40 ? 22  GLN I C   1 
ATOM   7940  O  O   . GLN H  1 23  ? 135.368 6.082   2.372   1.00 10.43 ? 22  GLN I O   1 
ATOM   7941  C  CB  . GLN H  1 23  ? 137.130 8.016   3.699   1.00 4.01  ? 22  GLN I CB  1 
ATOM   7942  C  CG  . GLN H  1 23  ? 137.780 8.322   2.374   1.00 2.00  ? 22  GLN I CG  1 
ATOM   7943  C  CD  . GLN H  1 23  ? 139.134 8.971   2.490   1.00 2.51  ? 22  GLN I CD  1 
ATOM   7944  O  OE1 . GLN H  1 23  ? 140.088 8.361   2.967   1.00 7.18  ? 22  GLN I OE1 1 
ATOM   7945  N  NE2 . GLN H  1 23  ? 139.299 10.235  2.138   1.00 2.00  ? 22  GLN I NE2 1 
ATOM   7946  N  N   . LYS H  1 24  ? 134.293 7.931   1.694   1.00 14.19 ? 23  LYS I N   1 
ATOM   7947  C  CA  . LYS H  1 24  ? 133.714 7.147   0.617   1.00 17.12 ? 23  LYS I CA  1 
ATOM   7948  C  C   . LYS H  1 24  ? 134.540 7.136   -0.634  1.00 17.50 ? 23  LYS I C   1 
ATOM   7949  O  O   . LYS H  1 24  ? 134.369 6.218   -1.427  1.00 19.83 ? 23  LYS I O   1 
ATOM   7950  C  CB  . LYS H  1 24  ? 132.328 7.617   0.245   1.00 19.46 ? 23  LYS I CB  1 
ATOM   7951  C  CG  . LYS H  1 24  ? 131.501 7.568   1.510   1.00 24.19 ? 23  LYS I CG  1 
ATOM   7952  C  CD  . LYS H  1 24  ? 130.186 6.913   1.267   1.00 28.48 ? 23  LYS I CD  1 
ATOM   7953  C  CE  . LYS H  1 24  ? 129.137 7.402   2.275   1.00 31.61 ? 23  LYS I CE  1 
ATOM   7954  N  NZ  . LYS H  1 24  ? 127.878 6.738   1.958   1.00 36.64 ? 23  LYS I NZ  1 
ATOM   7955  N  N   . GLU H  1 25  ? 135.485 8.060   -0.803  1.00 17.88 ? 24  GLU I N   1 
ATOM   7956  C  CA  . GLU H  1 25  ? 136.309 8.154   -1.998  1.00 19.51 ? 24  GLU I CA  1 
ATOM   7957  C  C   . GLU H  1 25  ? 137.699 8.593   -1.519  1.00 21.47 ? 24  GLU I C   1 
ATOM   7958  O  O   . GLU H  1 25  ? 137.773 9.349   -0.542  1.00 22.95 ? 24  GLU I O   1 
ATOM   7959  C  CB  . GLU H  1 25  ? 135.693 9.193   -2.967  1.00 20.15 ? 24  GLU I CB  1 
ATOM   7960  C  CG  . GLU H  1 25  ? 134.338 8.879   -3.637  1.00 19.51 ? 24  GLU I CG  1 
ATOM   7961  C  CD  . GLU H  1 25  ? 133.778 10.136  -4.260  1.00 22.22 ? 24  GLU I CD  1 
ATOM   7962  O  OE1 . GLU H  1 25  ? 133.127 10.882  -3.540  1.00 20.71 ? 24  GLU I OE1 1 
ATOM   7963  O  OE2 . GLU H  1 25  ? 134.019 10.398  -5.447  1.00 26.53 ? 24  GLU I OE2 1 
ATOM   7964  N  N   . SER H  1 26  ? 138.810 8.206   -2.153  1.00 21.57 ? 25  SER I N   1 
ATOM   7965  C  CA  . SER H  1 26  ? 140.149 8.514   -1.660  1.00 22.83 ? 25  SER I CA  1 
ATOM   7966  C  C   . SER H  1 26  ? 140.407 10.002  -1.524  1.00 26.82 ? 25  SER I C   1 
ATOM   7967  O  O   . SER H  1 26  ? 140.737 10.541  -0.460  1.00 30.14 ? 25  SER I O   1 
ATOM   7968  C  CB  . SER H  1 26  ? 141.174 7.913   -2.601  1.00 22.23 ? 25  SER I CB  1 
ATOM   7969  O  OG  . SER H  1 26  ? 140.858 8.184   -3.976  1.00 21.80 ? 25  SER I OG  1 
ATOM   7970  N  N   . ASN H  1 27  ? 140.153 10.705  -2.618  1.00 26.16 ? 26  ASN I N   1 
ATOM   7971  C  CA  . ASN H  1 27  ? 140.350 12.134  -2.612  1.00 26.45 ? 26  ASN I CA  1 
ATOM   7972  C  C   . ASN H  1 27  ? 139.034 12.769  -2.110  1.00 24.96 ? 26  ASN I C   1 
ATOM   7973  O  O   . ASN H  1 27  ? 138.718 13.921  -2.423  1.00 24.91 ? 26  ASN I O   1 
ATOM   7974  C  CB  . ASN H  1 27  ? 140.748 12.559  -4.065  1.00 29.13 ? 26  ASN I CB  1 
ATOM   7975  C  CG  . ASN H  1 27  ? 139.664 12.457  -5.159  1.00 32.87 ? 26  ASN I CG  1 
ATOM   7976  O  OD1 . ASN H  1 27  ? 139.044 11.399  -5.361  1.00 37.60 ? 26  ASN I OD1 1 
ATOM   7977  N  ND2 . ASN H  1 27  ? 139.405 13.490  -5.958  1.00 32.24 ? 26  ASN I ND2 1 
ATOM   7978  N  N   . GLY H  1 28  ? 138.252 12.051  -1.287  1.00 22.35 ? 27  GLY I N   1 
ATOM   7979  C  CA  . GLY H  1 28  ? 136.950 12.516  -0.848  1.00 18.40 ? 27  GLY I CA  1 
ATOM   7980  C  C   . GLY H  1 28  ? 136.935 13.014  0.596   1.00 15.47 ? 27  GLY I C   1 
ATOM   7981  O  O   . GLY H  1 28  ? 137.891 12.904  1.372   1.00 15.08 ? 27  GLY I O   1 
ATOM   7982  N  N   . PRO H  1 29  ? 135.808 13.599  0.982   1.00 14.44 ? 28  PRO I N   1 
ATOM   7983  C  CA  . PRO H  1 29  ? 135.480 13.877  2.366   1.00 12.97 ? 28  PRO I CA  1 
ATOM   7984  C  C   . PRO H  1 29  ? 135.297 12.591  3.142   1.00 14.36 ? 28  PRO I C   1 
ATOM   7985  O  O   . PRO H  1 29  ? 134.887 11.526  2.598   1.00 15.18 ? 28  PRO I O   1 
ATOM   7986  C  CB  . PRO H  1 29  ? 134.225 14.676  2.304   1.00 12.94 ? 28  PRO I CB  1 
ATOM   7987  C  CG  . PRO H  1 29  ? 134.260 15.241  0.894   1.00 13.46 ? 28  PRO I CG  1 
ATOM   7988  C  CD  . PRO H  1 29  ? 134.765 14.086  0.090   1.00 11.87 ? 28  PRO I CD  1 
ATOM   7989  N  N   . VAL H  1 30  ? 135.683 12.793  4.414   1.00 12.39 ? 29  VAL I N   1 
ATOM   7990  C  CA  . VAL H  1 30  ? 135.480 11.783  5.453   1.00 9.70  ? 29  VAL I CA  1 
ATOM   7991  C  C   . VAL H  1 30  ? 134.575 12.393  6.526   1.00 8.62  ? 29  VAL I C   1 
ATOM   7992  O  O   . VAL H  1 30  ? 134.737 13.539  6.939   1.00 8.35  ? 29  VAL I O   1 
ATOM   7993  C  CB  . VAL H  1 30  ? 136.903 11.258  6.026   1.00 7.79  ? 29  VAL I CB  1 
ATOM   7994  C  CG1 . VAL H  1 30  ? 138.076 12.031  5.471   1.00 4.29  ? 29  VAL I CG1 1 
ATOM   7995  C  CG2 . VAL H  1 30  ? 136.966 11.377  7.507   1.00 2.00  ? 29  VAL I CG2 1 
ATOM   7996  N  N   . LYS H  1 31  ? 133.489 11.686  6.799   1.00 9.70  ? 30  LYS I N   1 
ATOM   7997  C  CA  . LYS H  1 31  ? 132.512 12.008  7.820   1.00 10.11 ? 30  LYS I CA  1 
ATOM   7998  C  C   . LYS H  1 31  ? 133.088 11.529  9.142   1.00 9.62  ? 30  LYS I C   1 
ATOM   7999  O  O   . LYS H  1 31  ? 133.541 10.376  9.183   1.00 11.14 ? 30  LYS I O   1 
ATOM   8000  C  CB  . LYS H  1 31  ? 131.224 11.243  7.662   1.00 13.93 ? 30  LYS I CB  1 
ATOM   8001  C  CG  . LYS H  1 31  ? 129.936 11.676  6.933   1.00 23.73 ? 30  LYS I CG  1 
ATOM   8002  C  CD  . LYS H  1 31  ? 129.952 11.363  5.405   1.00 29.99 ? 30  LYS I CD  1 
ATOM   8003  C  CE  . LYS H  1 31  ? 128.629 11.742  4.701   1.00 32.35 ? 30  LYS I CE  1 
ATOM   8004  N  NZ  . LYS H  1 31  ? 128.807 11.753  3.244   1.00 38.22 ? 30  LYS I NZ  1 
ATOM   8005  N  N   . VAL H  1 32  ? 133.098 12.263  10.244  1.00 7.73  ? 31  VAL I N   1 
ATOM   8006  C  CA  . VAL H  1 32  ? 133.577 11.741  11.513  1.00 6.25  ? 31  VAL I CA  1 
ATOM   8007  C  C   . VAL H  1 32  ? 132.432 12.055  12.460  1.00 7.68  ? 31  VAL I C   1 
ATOM   8008  O  O   . VAL H  1 32  ? 131.979 13.202  12.582  1.00 10.56 ? 31  VAL I O   1 
ATOM   8009  C  CB  . VAL H  1 32  ? 134.961 12.409  11.929  1.00 4.02  ? 31  VAL I CB  1 
ATOM   8010  C  CG1 . VAL H  1 32  ? 135.069 13.792  11.434  1.00 5.11  ? 31  VAL I CG1 1 
ATOM   8011  C  CG2 . VAL H  1 32  ? 135.093 12.494  13.442  1.00 2.00  ? 31  VAL I CG2 1 
ATOM   8012  N  N   . TRP H  1 33  ? 131.891 11.025  13.081  1.00 5.91  ? 32  TRP I N   1 
ATOM   8013  C  CA  . TRP H  1 33  ? 130.737 11.134  13.933  1.00 5.35  ? 32  TRP I CA  1 
ATOM   8014  C  C   . TRP H  1 33  ? 131.018 10.236  15.119  1.00 7.98  ? 32  TRP I C   1 
ATOM   8015  O  O   . TRP H  1 33  ? 131.777 9.272   14.973  1.00 6.26  ? 32  TRP I O   1 
ATOM   8016  C  CB  . TRP H  1 33  ? 129.499 10.660  13.165  1.00 8.34  ? 32  TRP I CB  1 
ATOM   8017  C  CG  . TRP H  1 33  ? 129.252 9.149   12.900  1.00 8.62  ? 32  TRP I CG  1 
ATOM   8018  C  CD1 . TRP H  1 33  ? 128.316 8.502   13.653  1.00 9.13  ? 32  TRP I CD1 1 
ATOM   8019  C  CD2 . TRP H  1 33  ? 129.849 8.307   11.983  1.00 9.74  ? 32  TRP I CD2 1 
ATOM   8020  N  NE1 . TRP H  1 33  ? 128.318 7.268   13.224  1.00 14.09 ? 32  TRP I NE1 1 
ATOM   8021  C  CE2 . TRP H  1 33  ? 129.212 7.117   12.236  1.00 11.80 ? 32  TRP I CE2 1 
ATOM   8022  C  CE3 . TRP H  1 33  ? 130.805 8.320   10.989  1.00 15.40 ? 32  TRP I CE3 1 
ATOM   8023  C  CZ2 . TRP H  1 33  ? 129.499 5.957   11.530  1.00 15.00 ? 32  TRP I CZ2 1 
ATOM   8024  C  CZ3 . TRP H  1 33  ? 131.104 7.159   10.275  1.00 15.67 ? 32  TRP I CZ3 1 
ATOM   8025  C  CH2 . TRP H  1 33  ? 130.458 5.977   10.538  1.00 12.40 ? 32  TRP I CH2 1 
ATOM   8026  N  N   . GLY H  1 34  ? 130.460 10.475  16.303  1.00 9.56  ? 33  GLY I N   1 
ATOM   8027  C  CA  . GLY H  1 34  ? 130.713 9.576   17.431  1.00 11.80 ? 33  GLY I CA  1 
ATOM   8028  C  C   . GLY H  1 34  ? 130.211 10.194  18.718  1.00 12.50 ? 33  GLY I C   1 
ATOM   8029  O  O   . GLY H  1 34  ? 129.583 11.258  18.615  1.00 15.37 ? 33  GLY I O   1 
ATOM   8030  N  N   . SER H  1 35  ? 130.460 9.647   19.910  1.00 12.23 ? 34  SER I N   1 
ATOM   8031  C  CA  . SER H  1 35  ? 129.942 10.237  21.144  1.00 13.11 ? 34  SER I CA  1 
ATOM   8032  C  C   . SER H  1 35  ? 131.056 10.262  22.153  1.00 12.26 ? 34  SER I C   1 
ATOM   8033  O  O   . SER H  1 35  ? 131.797 9.282   22.272  1.00 13.15 ? 34  SER I O   1 
ATOM   8034  C  CB  . SER H  1 35  ? 128.804 9.399   21.675  1.00 17.57 ? 34  SER I CB  1 
ATOM   8035  O  OG  . SER H  1 35  ? 127.890 10.017  22.585  1.00 22.50 ? 34  SER I OG  1 
ATOM   8036  N  N   . ILE H  1 36  ? 131.263 11.397  22.824  1.00 12.21 ? 35  ILE I N   1 
ATOM   8037  C  CA  . ILE H  1 36  ? 132.298 11.514  23.850  1.00 8.39  ? 35  ILE I CA  1 
ATOM   8038  C  C   . ILE H  1 36  ? 131.510 12.024  25.038  1.00 9.19  ? 35  ILE I C   1 
ATOM   8039  O  O   . ILE H  1 36  ? 130.635 12.884  24.894  1.00 9.42  ? 35  ILE I O   1 
ATOM   8040  C  CB  . ILE H  1 36  ? 133.392 12.541  23.477  1.00 4.92  ? 35  ILE I CB  1 
ATOM   8041  C  CG1 . ILE H  1 36  ? 133.929 12.338  22.057  1.00 2.00  ? 35  ILE I CG1 1 
ATOM   8042  C  CG2 . ILE H  1 36  ? 134.473 12.413  24.542  1.00 2.00  ? 35  ILE I CG2 1 
ATOM   8043  C  CD1 . ILE H  1 36  ? 134.917 13.394  21.601  1.00 2.00  ? 35  ILE I CD1 1 
ATOM   8044  N  N   . LYS H  1 37  ? 131.759 11.463  26.200  1.00 10.59 ? 36  LYS I N   1 
ATOM   8045  C  CA  . LYS H  1 37  ? 131.062 11.876  27.400  1.00 11.45 ? 36  LYS I CA  1 
ATOM   8046  C  C   . LYS H  1 37  ? 132.041 12.078  28.528  1.00 8.11  ? 36  LYS I C   1 
ATOM   8047  O  O   . LYS H  1 37  ? 133.239 11.826  28.461  1.00 8.20  ? 36  LYS I O   1 
ATOM   8048  C  CB  . LYS H  1 37  ? 129.983 10.841  27.822  1.00 14.76 ? 36  LYS I CB  1 
ATOM   8049  C  CG  . LYS H  1 37  ? 130.255 9.371   27.529  1.00 18.76 ? 36  LYS I CG  1 
ATOM   8050  C  CD  . LYS H  1 37  ? 130.277 8.542   28.815  1.00 22.66 ? 36  LYS I CD  1 
ATOM   8051  C  CE  . LYS H  1 37  ? 130.345 7.058   28.380  1.00 25.81 ? 36  LYS I CE  1 
ATOM   8052  N  NZ  . LYS H  1 37  ? 130.250 6.104   29.475  1.00 24.99 ? 36  LYS I NZ  1 
ATOM   8053  N  N   . GLY H  1 38  ? 131.510 12.662  29.554  1.00 6.51  ? 37  GLY I N   1 
ATOM   8054  C  CA  . GLY H  1 38  ? 132.321 13.006  30.665  1.00 6.86  ? 37  GLY I CA  1 
ATOM   8055  C  C   . GLY H  1 38  ? 132.782 14.410  30.413  1.00 6.75  ? 37  GLY I C   1 
ATOM   8056  O  O   . GLY H  1 38  ? 133.435 14.896  31.317  1.00 6.70  ? 37  GLY I O   1 
ATOM   8057  N  N   . LEU H  1 39  ? 132.492 15.116  29.292  1.00 6.33  ? 38  LEU I N   1 
ATOM   8058  C  CA  . LEU H  1 39  ? 133.140 16.410  29.092  1.00 6.60  ? 38  LEU I CA  1 
ATOM   8059  C  C   . LEU H  1 39  ? 132.401 17.456  29.905  1.00 9.18  ? 38  LEU I C   1 
ATOM   8060  O  O   . LEU H  1 39  ? 131.261 17.238  30.327  1.00 11.78 ? 38  LEU I O   1 
ATOM   8061  C  CB  . LEU H  1 39  ? 133.079 16.944  27.690  1.00 5.95  ? 38  LEU I CB  1 
ATOM   8062  C  CG  . LEU H  1 39  ? 133.851 16.478  26.486  1.00 6.41  ? 38  LEU I CG  1 
ATOM   8063  C  CD1 . LEU H  1 39  ? 135.314 16.342  26.849  1.00 8.73  ? 38  LEU I CD1 1 
ATOM   8064  C  CD2 . LEU H  1 39  ? 133.295 15.183  25.995  1.00 5.19  ? 38  LEU I CD2 1 
ATOM   8065  N  N   . THR H  1 40  ? 133.016 18.607  30.148  1.00 8.20  ? 39  THR I N   1 
ATOM   8066  C  CA  . THR H  1 40  ? 132.339 19.745  30.725  1.00 5.22  ? 39  THR I CA  1 
ATOM   8067  C  C   . THR H  1 40  ? 131.651 20.428  29.568  1.00 4.25  ? 39  THR I C   1 
ATOM   8068  O  O   . THR H  1 40  ? 132.158 20.323  28.450  1.00 4.30  ? 39  THR I O   1 
ATOM   8069  C  CB  . THR H  1 40  ? 133.382 20.642  31.369  1.00 7.64  ? 39  THR I CB  1 
ATOM   8070  O  OG1 . THR H  1 40  ? 134.436 20.745  30.434  1.00 9.76  ? 39  THR I OG1 1 
ATOM   8071  C  CG2 . THR H  1 40  ? 134.012 20.052  32.631  1.00 6.01  ? 39  THR I CG2 1 
ATOM   8072  N  N   . GLU H  1 41  ? 130.479 21.023  29.805  1.00 6.14  ? 40  GLU I N   1 
ATOM   8073  C  CA  . GLU H  1 41  ? 129.710 21.799  28.836  1.00 6.16  ? 40  GLU I CA  1 
ATOM   8074  C  C   . GLU H  1 41  ? 130.562 22.778  28.022  1.00 4.80  ? 40  GLU I C   1 
ATOM   8075  O  O   . GLU H  1 41  ? 131.548 23.310  28.517  1.00 2.00  ? 40  GLU I O   1 
ATOM   8076  C  CB  . GLU H  1 41  ? 128.585 22.580  29.574  1.00 6.86  ? 40  GLU I CB  1 
ATOM   8077  C  CG  . GLU H  1 41  ? 127.477 23.104  28.649  1.00 11.67 ? 40  GLU I CG  1 
ATOM   8078  C  CD  . GLU H  1 41  ? 126.329 23.832  29.345  1.00 18.82 ? 40  GLU I CD  1 
ATOM   8079  O  OE1 . GLU H  1 41  ? 125.878 23.326  30.366  1.00 22.78 ? 40  GLU I OE1 1 
ATOM   8080  O  OE2 . GLU H  1 41  ? 125.868 24.893  28.884  1.00 22.63 ? 40  GLU I OE2 1 
ATOM   8081  N  N   . GLY H  1 42  ? 130.234 22.999  26.743  1.00 6.22  ? 41  GLY I N   1 
ATOM   8082  C  CA  . GLY H  1 42  ? 130.999 23.881  25.894  1.00 6.51  ? 41  GLY I CA  1 
ATOM   8083  C  C   . GLY H  1 42  ? 131.999 23.145  25.025  1.00 7.68  ? 41  GLY I C   1 
ATOM   8084  O  O   . GLY H  1 42  ? 132.065 21.927  24.982  1.00 11.79 ? 41  GLY I O   1 
ATOM   8085  N  N   . LEU H  1 43  ? 132.751 23.955  24.295  1.00 8.95  ? 42  LEU I N   1 
ATOM   8086  C  CA  . LEU H  1 43  ? 133.790 23.653  23.331  1.00 5.23  ? 42  LEU I CA  1 
ATOM   8087  C  C   . LEU H  1 43  ? 135.016 22.922  23.852  1.00 5.15  ? 42  LEU I C   1 
ATOM   8088  O  O   . LEU H  1 43  ? 135.505 23.257  24.923  1.00 5.16  ? 42  LEU I O   1 
ATOM   8089  C  CB  . LEU H  1 43  ? 134.197 25.001  22.702  1.00 5.58  ? 42  LEU I CB  1 
ATOM   8090  C  CG  . LEU H  1 43  ? 133.637 25.645  21.405  1.00 3.62  ? 42  LEU I CG  1 
ATOM   8091  C  CD1 . LEU H  1 43  ? 132.314 25.132  20.966  1.00 2.00  ? 42  LEU I CD1 1 
ATOM   8092  C  CD2 . LEU H  1 43  ? 133.538 27.095  21.672  1.00 2.00  ? 42  LEU I CD2 1 
ATOM   8093  N  N   . HIS H  1 44  ? 135.521 21.915  23.119  1.00 6.29  ? 43  HIS I N   1 
ATOM   8094  C  CA  . HIS H  1 44  ? 136.740 21.158  23.402  1.00 4.84  ? 43  HIS I CA  1 
ATOM   8095  C  C   . HIS H  1 44  ? 137.501 20.986  22.066  1.00 5.17  ? 43  HIS I C   1 
ATOM   8096  O  O   . HIS H  1 44  ? 136.885 20.594  21.078  1.00 4.85  ? 43  HIS I O   1 
ATOM   8097  C  CB  . HIS H  1 44  ? 136.382 19.807  23.966  1.00 2.00  ? 43  HIS I CB  1 
ATOM   8098  C  CG  . HIS H  1 44  ? 135.837 19.941  25.369  1.00 2.00  ? 43  HIS I CG  1 
ATOM   8099  N  ND1 . HIS H  1 44  ? 136.509 20.011  26.515  1.00 2.00  ? 43  HIS I ND1 1 
ATOM   8100  C  CD2 . HIS H  1 44  ? 134.497 20.100  25.663  1.00 2.00  ? 43  HIS I CD2 1 
ATOM   8101  C  CE1 . HIS H  1 44  ? 135.634 20.216  27.475  1.00 2.00  ? 43  HIS I CE1 1 
ATOM   8102  N  NE2 . HIS H  1 44  ? 134.432 20.268  26.953  1.00 2.00  ? 43  HIS I NE2 1 
ATOM   8103  N  N   . GLY H  1 45  ? 138.785 21.374  21.976  1.00 3.05  ? 44  GLY I N   1 
ATOM   8104  C  CA  . GLY H  1 45  ? 139.576 21.236  20.787  1.00 2.00  ? 44  GLY I CA  1 
ATOM   8105  C  C   . GLY H  1 45  ? 139.652 19.768  20.418  1.00 3.20  ? 44  GLY I C   1 
ATOM   8106  O  O   . GLY H  1 45  ? 139.892 18.979  21.317  1.00 5.33  ? 44  GLY I O   1 
ATOM   8107  N  N   . PHE H  1 46  ? 139.513 19.370  19.160  1.00 2.50  ? 45  PHE I N   1 
ATOM   8108  C  CA  . PHE H  1 46  ? 139.494 17.997  18.710  1.00 2.00  ? 45  PHE I CA  1 
ATOM   8109  C  C   . PHE H  1 46  ? 140.576 17.796  17.649  1.00 2.40  ? 45  PHE I C   1 
ATOM   8110  O  O   . PHE H  1 46  ? 140.410 18.302  16.534  1.00 2.95  ? 45  PHE I O   1 
ATOM   8111  C  CB  . PHE H  1 46  ? 138.132 17.819  18.181  1.00 2.00  ? 45  PHE I CB  1 
ATOM   8112  C  CG  . PHE H  1 46  ? 137.664 16.418  17.906  1.00 2.64  ? 45  PHE I CG  1 
ATOM   8113  C  CD1 . PHE H  1 46  ? 137.548 15.507  18.948  1.00 2.00  ? 45  PHE I CD1 1 
ATOM   8114  C  CD2 . PHE H  1 46  ? 137.207 16.119  16.628  1.00 3.15  ? 45  PHE I CD2 1 
ATOM   8115  C  CE1 . PHE H  1 46  ? 136.970 14.291  18.712  1.00 2.00  ? 45  PHE I CE1 1 
ATOM   8116  C  CE2 . PHE H  1 46  ? 136.623 14.884  16.405  1.00 2.00  ? 45  PHE I CE2 1 
ATOM   8117  C  CZ  . PHE H  1 46  ? 136.501 13.994  17.454  1.00 2.41  ? 45  PHE I CZ  1 
ATOM   8118  N  N   . HIS H  1 47  ? 141.697 17.104  17.843  1.00 2.00  ? 46  HIS I N   1 
ATOM   8119  C  CA  . HIS H  1 47  ? 142.720 17.075  16.839  1.00 2.00  ? 46  HIS I CA  1 
ATOM   8120  C  C   . HIS H  1 47  ? 143.300 15.705  16.620  1.00 4.09  ? 46  HIS I C   1 
ATOM   8121  O  O   . HIS H  1 47  ? 143.290 14.836  17.524  1.00 6.19  ? 46  HIS I O   1 
ATOM   8122  C  CB  . HIS H  1 47  ? 143.888 17.945  17.210  1.00 3.69  ? 46  HIS I CB  1 
ATOM   8123  C  CG  . HIS H  1 47  ? 143.567 19.263  17.893  1.00 6.46  ? 46  HIS I CG  1 
ATOM   8124  N  ND1 . HIS H  1 47  ? 143.950 19.663  19.109  1.00 4.57  ? 46  HIS I ND1 1 
ATOM   8125  C  CD2 . HIS H  1 47  ? 142.823 20.252  17.304  1.00 3.08  ? 46  HIS I CD2 1 
ATOM   8126  C  CE1 . HIS H  1 47  ? 143.464 20.862  19.244  1.00 8.37  ? 46  HIS I CE1 1 
ATOM   8127  N  NE2 . HIS H  1 47  ? 142.788 21.209  18.169  1.00 5.52  ? 46  HIS I NE2 1 
ATOM   8128  N  N   . VAL H  1 48  ? 143.879 15.553  15.426  1.00 2.07  ? 47  VAL I N   1 
ATOM   8129  C  CA  . VAL H  1 48  ? 144.643 14.380  15.117  1.00 2.00  ? 47  VAL I CA  1 
ATOM   8130  C  C   . VAL H  1 48  ? 146.077 14.814  15.341  1.00 3.13  ? 47  VAL I C   1 
ATOM   8131  O  O   . VAL H  1 48  ? 146.499 15.894  14.899  1.00 2.00  ? 47  VAL I O   1 
ATOM   8132  C  CB  . VAL H  1 48  ? 144.454 13.914  13.678  1.00 2.00  ? 47  VAL I CB  1 
ATOM   8133  C  CG1 . VAL H  1 48  ? 145.277 12.650  13.455  1.00 2.00  ? 47  VAL I CG1 1 
ATOM   8134  C  CG2 . VAL H  1 48  ? 143.015 13.540  13.447  1.00 2.00  ? 47  VAL I CG2 1 
ATOM   8135  N  N   . HIS H  1 49  ? 146.786 13.997  16.136  1.00 5.15  ? 48  HIS I N   1 
ATOM   8136  C  CA  . HIS H  1 49  ? 148.162 14.225  16.570  1.00 4.41  ? 48  HIS I CA  1 
ATOM   8137  C  C   . HIS H  1 49  ? 148.968 13.159  15.858  1.00 5.51  ? 48  HIS I C   1 
ATOM   8138  O  O   . HIS H  1 49  ? 148.468 12.105  15.429  1.00 8.77  ? 48  HIS I O   1 
ATOM   8139  C  CB  . HIS H  1 49  ? 148.281 14.090  18.107  1.00 3.79  ? 48  HIS I CB  1 
ATOM   8140  C  CG  . HIS H  1 49  ? 147.726 15.283  18.911  1.00 2.13  ? 48  HIS I CG  1 
ATOM   8141  N  ND1 . HIS H  1 49  ? 148.351 16.105  19.735  1.00 2.00  ? 48  HIS I ND1 1 
ATOM   8142  C  CD2 . HIS H  1 49  ? 146.416 15.716  18.867  1.00 2.00  ? 48  HIS I CD2 1 
ATOM   8143  C  CE1 . HIS H  1 49  ? 147.462 16.996  20.154  1.00 2.00  ? 48  HIS I CE1 1 
ATOM   8144  N  NE2 . HIS H  1 49  ? 146.285 16.766  19.629  1.00 2.00  ? 48  HIS I NE2 1 
ATOM   8145  N  N   . GLU H  1 50  ? 150.237 13.436  15.767  1.00 3.44  ? 49  GLU I N   1 
ATOM   8146  C  CA  . GLU H  1 50  ? 151.141 12.704  14.937  1.00 4.40  ? 49  GLU I CA  1 
ATOM   8147  C  C   . GLU H  1 50  ? 151.445 11.232  15.189  1.00 4.73  ? 49  GLU I C   1 
ATOM   8148  O  O   . GLU H  1 50  ? 151.668 10.481  14.239  1.00 4.66  ? 49  GLU I O   1 
ATOM   8149  C  CB  . GLU H  1 50  ? 152.387 13.539  14.952  1.00 6.15  ? 49  GLU I CB  1 
ATOM   8150  C  CG  . GLU H  1 50  ? 153.151 13.199  13.716  1.00 12.31 ? 49  GLU I CG  1 
ATOM   8151  C  CD  . GLU H  1 50  ? 154.562 13.714  13.611  1.00 17.03 ? 49  GLU I CD  1 
ATOM   8152  O  OE1 . GLU H  1 50  ? 155.109 14.277  14.581  1.00 22.21 ? 49  GLU I OE1 1 
ATOM   8153  O  OE2 . GLU H  1 50  ? 155.106 13.515  12.522  1.00 18.12 ? 49  GLU I OE2 1 
ATOM   8154  N  N   . PHE H  1 51  ? 151.524 10.766  16.433  1.00 4.42  ? 50  PHE I N   1 
ATOM   8155  C  CA  . PHE H  1 51  ? 151.876 9.384   16.700  1.00 5.09  ? 50  PHE I CA  1 
ATOM   8156  C  C   . PHE H  1 51  ? 150.749 8.627   17.368  1.00 5.21  ? 50  PHE I C   1 
ATOM   8157  O  O   . PHE H  1 51  ? 150.086 9.117   18.286  1.00 4.75  ? 50  PHE I O   1 
ATOM   8158  C  CB  . PHE H  1 51  ? 153.116 9.286   17.617  1.00 4.01  ? 50  PHE I CB  1 
ATOM   8159  C  CG  . PHE H  1 51  ? 154.239 10.139  17.069  1.00 2.00  ? 50  PHE I CG  1 
ATOM   8160  C  CD1 . PHE H  1 51  ? 154.819 9.823   15.870  1.00 3.29  ? 50  PHE I CD1 1 
ATOM   8161  C  CD2 . PHE H  1 51  ? 154.617 11.264  17.747  1.00 2.00  ? 50  PHE I CD2 1 
ATOM   8162  C  CE1 . PHE H  1 51  ? 155.750 10.671  15.337  1.00 3.10  ? 50  PHE I CE1 1 
ATOM   8163  C  CE2 . PHE H  1 51  ? 155.551 12.114  17.215  1.00 2.00  ? 50  PHE I CE2 1 
ATOM   8164  C  CZ  . PHE H  1 51  ? 156.119 11.804  16.014  1.00 2.91  ? 50  PHE I CZ  1 
ATOM   8165  N  N   . GLY H  1 52  ? 150.553 7.379   16.968  1.00 6.23  ? 51  GLY I N   1 
ATOM   8166  C  CA  . GLY H  1 52  ? 149.661 6.487   17.678  1.00 7.26  ? 51  GLY I CA  1 
ATOM   8167  C  C   . GLY H  1 52  ? 150.484 5.869   18.787  1.00 7.40  ? 51  GLY I C   1 
ATOM   8168  O  O   . GLY H  1 52  ? 150.407 4.668   19.008  1.00 7.90  ? 51  GLY I O   1 
ATOM   8169  N  N   . ASP H  1 53  ? 151.270 6.677   19.500  1.00 8.09  ? 52  ASP I N   1 
ATOM   8170  C  CA  . ASP H  1 53  ? 152.085 6.221   20.576  1.00 9.60  ? 52  ASP I CA  1 
ATOM   8171  C  C   . ASP H  1 53  ? 151.309 6.610   21.811  1.00 11.69 ? 52  ASP I C   1 
ATOM   8172  O  O   . ASP H  1 53  ? 151.131 7.798   22.124  1.00 13.07 ? 52  ASP I O   1 
ATOM   8173  C  CB  . ASP H  1 53  ? 153.470 6.916   20.597  1.00 9.52  ? 52  ASP I CB  1 
ATOM   8174  C  CG  . ASP H  1 53  ? 154.492 6.310   21.579  1.00 10.96 ? 52  ASP I CG  1 
ATOM   8175  O  OD1 . ASP H  1 53  ? 154.046 5.683   22.519  1.00 7.99  ? 52  ASP I OD1 1 
ATOM   8176  O  OD2 . ASP H  1 53  ? 155.709 6.425   21.417  1.00 11.13 ? 52  ASP I OD2 1 
ATOM   8177  N  N   . ASN H  1 54  ? 150.856 5.591   22.519  1.00 11.15 ? 53  ASN I N   1 
ATOM   8178  C  CA  . ASN H  1 54  ? 150.209 5.863   23.775  1.00 13.99 ? 53  ASN I CA  1 
ATOM   8179  C  C   . ASN H  1 54  ? 150.954 5.308   24.955  1.00 13.88 ? 53  ASN I C   1 
ATOM   8180  O  O   . ASN H  1 54  ? 150.338 5.133   26.000  1.00 14.34 ? 53  ASN I O   1 
ATOM   8181  C  CB  . ASN H  1 54  ? 148.787 5.314   23.800  1.00 18.54 ? 53  ASN I CB  1 
ATOM   8182  C  CG  . ASN H  1 54  ? 147.784 6.295   23.199  1.00 24.11 ? 53  ASN I CG  1 
ATOM   8183  O  OD1 . ASN H  1 54  ? 146.581 6.030   23.259  1.00 28.48 ? 53  ASN I OD1 1 
ATOM   8184  N  ND2 . ASN H  1 54  ? 148.122 7.427   22.565  1.00 22.60 ? 53  ASN I ND2 1 
ATOM   8185  N  N   . THR H  1 55  ? 152.264 5.026   24.830  1.00 13.21 ? 54  THR I N   1 
ATOM   8186  C  CA  . THR H  1 55  ? 153.062 4.523   25.941  1.00 12.73 ? 54  THR I CA  1 
ATOM   8187  C  C   . THR H  1 55  ? 152.783 5.324   27.228  1.00 13.13 ? 54  THR I C   1 
ATOM   8188  O  O   . THR H  1 55  ? 152.389 4.778   28.268  1.00 14.44 ? 54  THR I O   1 
ATOM   8189  C  CB  . THR H  1 55  ? 154.611 4.577   25.572  1.00 13.51 ? 54  THR I CB  1 
ATOM   8190  O  OG1 . THR H  1 55  ? 154.889 5.761   24.852  1.00 16.82 ? 54  THR I OG1 1 
ATOM   8191  C  CG2 . THR H  1 55  ? 155.056 3.458   24.658  1.00 12.80 ? 54  THR I CG2 1 
ATOM   8192  N  N   . ALA H  1 56  ? 152.821 6.657   27.070  1.00 12.78 ? 55  ALA I N   1 
ATOM   8193  C  CA  . ALA H  1 56  ? 152.673 7.626   28.152  1.00 11.20 ? 55  ALA I CA  1 
ATOM   8194  C  C   . ALA H  1 56  ? 151.423 8.479   28.155  1.00 9.84  ? 55  ALA I C   1 
ATOM   8195  O  O   . ALA H  1 56  ? 151.443 9.720   28.259  1.00 8.55  ? 55  ALA I O   1 
ATOM   8196  C  CB  . ALA H  1 56  ? 153.851 8.550   28.124  1.00 13.06 ? 55  ALA I CB  1 
ATOM   8197  N  N   . GLY H  1 57  ? 150.330 7.747   28.024  1.00 8.18  ? 56  GLY I N   1 
ATOM   8198  C  CA  . GLY H  1 57  ? 149.028 8.365   27.920  1.00 8.63  ? 56  GLY I CA  1 
ATOM   8199  C  C   . GLY H  1 57  ? 148.954 9.201   26.649  1.00 9.80  ? 56  GLY I C   1 
ATOM   8200  O  O   . GLY H  1 57  ? 149.574 8.886   25.626  1.00 12.00 ? 56  GLY I O   1 
ATOM   8201  N  N   . CYS H  1 58  ? 148.294 10.347  26.727  1.00 9.76  ? 57  CYS I N   1 
ATOM   8202  C  CA  . CYS H  1 58  ? 148.167 11.153  25.545  1.00 8.43  ? 57  CYS I CA  1 
ATOM   8203  C  C   . CYS H  1 58  ? 149.427 11.933  25.296  1.00 8.30  ? 57  CYS I C   1 
ATOM   8204  O  O   . CYS H  1 58  ? 149.668 12.413  24.188  1.00 9.23  ? 57  CYS I O   1 
ATOM   8205  C  CB  . CYS H  1 58  ? 147.008 12.091  25.693  1.00 7.81  ? 57  CYS I CB  1 
ATOM   8206  S  SG  . CYS H  1 58  ? 145.459 11.181  25.887  1.00 8.62  ? 57  CYS I SG  1 
ATOM   8207  N  N   . THR H  1 59  ? 150.302 12.018  26.280  1.00 9.10  ? 58  THR I N   1 
ATOM   8208  C  CA  . THR H  1 59  ? 151.510 12.806  26.142  1.00 9.87  ? 58  THR I CA  1 
ATOM   8209  C  C   . THR H  1 59  ? 152.369 12.314  24.979  1.00 10.30 ? 58  THR I C   1 
ATOM   8210  O  O   . THR H  1 59  ? 152.836 13.097  24.154  1.00 11.77 ? 58  THR I O   1 
ATOM   8211  C  CB  . THR H  1 59  ? 152.207 12.709  27.487  1.00 8.16  ? 58  THR I CB  1 
ATOM   8212  O  OG1 . THR H  1 59  ? 151.282 13.173  28.474  1.00 14.12 ? 58  THR I OG1 1 
ATOM   8213  C  CG2 . THR H  1 59  ? 153.486 13.491  27.494  1.00 9.99  ? 58  THR I CG2 1 
ATOM   8214  N  N   . SER H  1 60  ? 152.537 11.003  24.829  1.00 11.85 ? 59  SER I N   1 
ATOM   8215  C  CA  . SER H  1 60  ? 153.396 10.495  23.794  1.00 11.54 ? 59  SER I CA  1 
ATOM   8216  C  C   . SER H  1 60  ? 152.843 10.659  22.369  1.00 12.08 ? 59  SER I C   1 
ATOM   8217  O  O   . SER H  1 60  ? 153.604 10.425  21.433  1.00 14.78 ? 59  SER I O   1 
ATOM   8218  C  CB  . SER H  1 60  ? 153.689 9.040   24.194  1.00 9.65  ? 59  SER I CB  1 
ATOM   8219  O  OG  . SER H  1 60  ? 152.629 8.410   24.917  1.00 9.16  ? 59  SER I OG  1 
ATOM   8220  N  N   . ALA H  1 61  ? 151.619 11.158  22.129  1.00 12.44 ? 60  ALA I N   1 
ATOM   8221  C  CA  . ALA H  1 61  ? 151.038 11.296  20.796  1.00 11.45 ? 60  ALA I CA  1 
ATOM   8222  C  C   . ALA H  1 61  ? 151.717 12.368  19.965  1.00 11.19 ? 60  ALA I C   1 
ATOM   8223  O  O   . ALA H  1 61  ? 151.480 12.457  18.758  1.00 10.09 ? 60  ALA I O   1 
ATOM   8224  C  CB  . ALA H  1 61  ? 149.575 11.679  20.851  1.00 11.89 ? 60  ALA I CB  1 
ATOM   8225  N  N   . GLY H  1 62  ? 152.540 13.202  20.613  1.00 9.71  ? 61  GLY I N   1 
ATOM   8226  C  CA  . GLY H  1 62  ? 153.330 14.213  19.948  1.00 6.68  ? 61  GLY I CA  1 
ATOM   8227  C  C   . GLY H  1 62  ? 152.452 15.380  19.537  1.00 5.84  ? 61  GLY I C   1 
ATOM   8228  O  O   . GLY H  1 62  ? 151.379 15.562  20.107  1.00 8.69  ? 61  GLY I O   1 
ATOM   8229  N  N   . PRO H  1 63  ? 152.803 16.230  18.579  1.00 6.02  ? 62  PRO I N   1 
ATOM   8230  C  CA  . PRO H  1 63  ? 152.008 17.393  18.194  1.00 5.86  ? 62  PRO I CA  1 
ATOM   8231  C  C   . PRO H  1 63  ? 150.919 17.079  17.179  1.00 5.69  ? 62  PRO I C   1 
ATOM   8232  O  O   . PRO H  1 63  ? 150.745 15.932  16.773  1.00 8.14  ? 62  PRO I O   1 
ATOM   8233  C  CB  . PRO H  1 63  ? 153.080 18.322  17.726  1.00 3.01  ? 62  PRO I CB  1 
ATOM   8234  C  CG  . PRO H  1 63  ? 154.031 17.414  16.977  1.00 2.00  ? 62  PRO I CG  1 
ATOM   8235  C  CD  . PRO H  1 63  ? 154.071 16.195  17.850  1.00 5.24  ? 62  PRO I CD  1 
ATOM   8236  N  N   . HIS H  1 64  ? 150.139 18.071  16.777  1.00 7.35  ? 63  HIS I N   1 
ATOM   8237  C  CA  . HIS H  1 64  ? 149.086 17.894  15.795  1.00 7.44  ? 63  HIS I CA  1 
ATOM   8238  C  C   . HIS H  1 64  ? 149.658 17.277  14.549  1.00 7.84  ? 63  HIS I C   1 
ATOM   8239  O  O   . HIS H  1 64  ? 150.833 17.446  14.241  1.00 10.02 ? 63  HIS I O   1 
ATOM   8240  C  CB  . HIS H  1 64  ? 148.438 19.238  15.449  1.00 6.90  ? 63  HIS I CB  1 
ATOM   8241  C  CG  . HIS H  1 64  ? 147.656 19.872  16.585  1.00 6.21  ? 63  HIS I CG  1 
ATOM   8242  N  ND1 . HIS H  1 64  ? 147.217 21.106  16.703  1.00 8.13  ? 63  HIS I ND1 1 
ATOM   8243  C  CD2 . HIS H  1 64  ? 147.213 19.165  17.678  1.00 12.15 ? 63  HIS I CD2 1 
ATOM   8244  C  CE1 . HIS H  1 64  ? 146.519 21.084  17.853  1.00 9.86  ? 63  HIS I CE1 1 
ATOM   8245  N  NE2 . HIS H  1 64  ? 146.489 19.906  18.479  1.00 13.39 ? 63  HIS I NE2 1 
ATOM   8246  N  N   . PHE H  1 65  ? 148.887 16.548  13.762  1.00 8.91  ? 64  PHE I N   1 
ATOM   8247  C  CA  . PHE H  1 65  ? 149.455 15.875  12.602  1.00 6.25  ? 64  PHE I CA  1 
ATOM   8248  C  C   . PHE H  1 65  ? 149.576 16.989  11.594  1.00 3.46  ? 64  PHE I C   1 
ATOM   8249  O  O   . PHE H  1 65  ? 148.602 17.672  11.329  1.00 2.00  ? 64  PHE I O   1 
ATOM   8250  C  CB  . PHE H  1 65  ? 148.484 14.761  12.200  1.00 5.78  ? 64  PHE I CB  1 
ATOM   8251  C  CG  . PHE H  1 65  ? 148.812 14.064  10.905  1.00 6.39  ? 64  PHE I CG  1 
ATOM   8252  C  CD1 . PHE H  1 65  ? 150.107 13.710  10.596  1.00 6.47  ? 64  PHE I CD1 1 
ATOM   8253  C  CD2 . PHE H  1 65  ? 147.793 13.796  10.027  1.00 6.68  ? 64  PHE I CD2 1 
ATOM   8254  C  CE1 . PHE H  1 65  ? 150.370 13.087  9.383   1.00 7.55  ? 64  PHE I CE1 1 
ATOM   8255  C  CE2 . PHE H  1 65  ? 148.080 13.176  8.824   1.00 6.43  ? 64  PHE I CE2 1 
ATOM   8256  C  CZ  . PHE H  1 65  ? 149.366 12.817  8.498   1.00 4.35  ? 64  PHE I CZ  1 
ATOM   8257  N  N   . ASN H  1 66  ? 150.753 17.233  11.060  1.00 4.20  ? 65  ASN I N   1 
ATOM   8258  C  CA  . ASN H  1 66  ? 150.954 18.339  10.149  1.00 3.47  ? 65  ASN I CA  1 
ATOM   8259  C  C   . ASN H  1 66  ? 152.061 18.024  9.170   1.00 4.09  ? 65  ASN I C   1 
ATOM   8260  O  O   . ASN H  1 66  ? 153.108 18.665  9.211   1.00 7.58  ? 65  ASN I O   1 
ATOM   8261  C  CB  . ASN H  1 66  ? 151.267 19.572  10.980  1.00 2.05  ? 65  ASN I CB  1 
ATOM   8262  C  CG  . ASN H  1 66  ? 151.844 20.828  10.346  1.00 2.08  ? 65  ASN I CG  1 
ATOM   8263  O  OD1 . ASN H  1 66  ? 151.589 21.274  9.223   1.00 2.00  ? 65  ASN I OD1 1 
ATOM   8264  N  ND2 . ASN H  1 66  ? 152.653 21.476  11.136  1.00 2.00  ? 65  ASN I ND2 1 
ATOM   8265  N  N   . PRO H  1 67  ? 151.891 17.091  8.233   1.00 3.95  ? 66  PRO I N   1 
ATOM   8266  C  CA  . PRO H  1 67  ? 152.886 16.780  7.224   1.00 3.92  ? 66  PRO I CA  1 
ATOM   8267  C  C   . PRO H  1 67  ? 153.213 18.015  6.384   1.00 6.96  ? 66  PRO I C   1 
ATOM   8268  O  O   . PRO H  1 67  ? 154.377 18.223  6.065   1.00 11.49 ? 66  PRO I O   1 
ATOM   8269  C  CB  . PRO H  1 67  ? 152.250 15.662  6.464   1.00 2.00  ? 66  PRO I CB  1 
ATOM   8270  C  CG  . PRO H  1 67  ? 150.808 16.091  6.451   1.00 3.10  ? 66  PRO I CG  1 
ATOM   8271  C  CD  . PRO H  1 67  ? 150.614 16.478  7.887   1.00 5.13  ? 66  PRO I CD  1 
ATOM   8272  N  N   . LEU H  1 68  ? 152.305 18.923  6.055   1.00 5.85  ? 67  LEU I N   1 
ATOM   8273  C  CA  . LEU H  1 68  ? 152.658 20.000  5.130   1.00 5.88  ? 67  LEU I CA  1 
ATOM   8274  C  C   . LEU H  1 68  ? 153.376 21.173  5.757   1.00 7.37  ? 67  LEU I C   1 
ATOM   8275  O  O   . LEU H  1 68  ? 153.712 22.107  5.042   1.00 8.56  ? 67  LEU I O   1 
ATOM   8276  C  CB  . LEU H  1 68  ? 151.426 20.531  4.424   1.00 5.14  ? 67  LEU I CB  1 
ATOM   8277  C  CG  . LEU H  1 68  ? 150.744 19.492  3.560   1.00 5.38  ? 67  LEU I CG  1 
ATOM   8278  C  CD1 . LEU H  1 68  ? 149.475 20.047  3.055   1.00 6.39  ? 67  LEU I CD1 1 
ATOM   8279  C  CD2 . LEU H  1 68  ? 151.641 19.078  2.434   1.00 5.91  ? 67  LEU I CD2 1 
ATOM   8280  N  N   . SER H  1 69  ? 153.632 21.177  7.071   1.00 9.08  ? 68  SER I N   1 
ATOM   8281  C  CA  . SER H  1 69  ? 154.321 22.257  7.741   1.00 9.13  ? 68  SER I CA  1 
ATOM   8282  C  C   . SER H  1 69  ? 153.764 23.630  7.533   1.00 10.69 ? 68  SER I C   1 
ATOM   8283  O  O   . SER H  1 69  ? 154.424 24.579  7.094   1.00 12.35 ? 68  SER I O   1 
ATOM   8284  C  CB  . SER H  1 69  ? 155.761 22.232  7.337   1.00 7.44  ? 68  SER I CB  1 
ATOM   8285  O  OG  . SER H  1 69  ? 156.365 21.303  8.232   1.00 14.21 ? 68  SER I OG  1 
ATOM   8286  N  N   . ARG H  1 70  ? 152.496 23.614  7.940   1.00 10.42 ? 69  ARG I N   1 
ATOM   8287  C  CA  . ARG H  1 70  ? 151.629 24.770  8.024   1.00 8.57  ? 69  ARG I CA  1 
ATOM   8288  C  C   . ARG H  1 70  ? 151.403 25.128  9.486   1.00 5.38  ? 69  ARG I C   1 
ATOM   8289  O  O   . ARG H  1 70  ? 151.888 24.455  10.386  1.00 2.00  ? 69  ARG I O   1 
ATOM   8290  C  CB  . ARG H  1 70  ? 150.304 24.470  7.334   1.00 11.15 ? 69  ARG I CB  1 
ATOM   8291  C  CG  . ARG H  1 70  ? 150.565 24.446  5.851   1.00 18.31 ? 69  ARG I CG  1 
ATOM   8292  C  CD  . ARG H  1 70  ? 149.319 24.340  4.994   1.00 26.27 ? 69  ARG I CD  1 
ATOM   8293  N  NE  . ARG H  1 70  ? 149.739 23.998  3.642   1.00 33.67 ? 69  ARG I NE  1 
ATOM   8294  C  CZ  . ARG H  1 70  ? 148.893 23.749  2.630   1.00 37.63 ? 69  ARG I CZ  1 
ATOM   8295  N  NH1 . ARG H  1 70  ? 147.548 23.826  2.785   1.00 38.63 ? 69  ARG I NH1 1 
ATOM   8296  N  NH2 . ARG H  1 70  ? 149.442 23.433  1.432   1.00 38.37 ? 69  ARG I NH2 1 
ATOM   8297  N  N   . LYS H  1 71  ? 150.695 26.215  9.717   1.00 5.59  ? 70  LYS I N   1 
ATOM   8298  C  CA  . LYS H  1 71  ? 150.347 26.654  11.043  1.00 8.39  ? 70  LYS I CA  1 
ATOM   8299  C  C   . LYS H  1 71  ? 148.945 26.209  11.379  1.00 8.21  ? 70  LYS I C   1 
ATOM   8300  O  O   . LYS H  1 71  ? 148.121 25.882  10.524  1.00 11.35 ? 70  LYS I O   1 
ATOM   8301  C  CB  . LYS H  1 71  ? 150.409 28.149  11.154  1.00 10.59 ? 70  LYS I CB  1 
ATOM   8302  C  CG  . LYS H  1 71  ? 151.849 28.570  11.352  1.00 14.92 ? 70  LYS I CG  1 
ATOM   8303  C  CD  . LYS H  1 71  ? 151.944 30.082  11.434  1.00 17.51 ? 70  LYS I CD  1 
ATOM   8304  C  CE  . LYS H  1 71  ? 153.280 30.528  12.067  1.00 19.48 ? 70  LYS I CE  1 
ATOM   8305  N  NZ  . LYS H  1 71  ? 154.416 30.112  11.267  1.00 24.03 ? 70  LYS I NZ  1 
ATOM   8306  N  N   . HIS H  1 72  ? 148.704 26.122  12.670  1.00 7.19  ? 71  HIS I N   1 
ATOM   8307  C  CA  . HIS H  1 72  ? 147.431 25.683  13.185  1.00 4.42  ? 71  HIS I CA  1 
ATOM   8308  C  C   . HIS H  1 72  ? 146.320 26.636  12.786  1.00 3.23  ? 71  HIS I C   1 
ATOM   8309  O  O   . HIS H  1 72  ? 146.543 27.836  12.774  1.00 4.47  ? 71  HIS I O   1 
ATOM   8310  C  CB  . HIS H  1 72  ? 147.579 25.581  14.706  1.00 3.34  ? 71  HIS I CB  1 
ATOM   8311  C  CG  . HIS H  1 72  ? 146.311 25.144  15.414  1.00 4.06  ? 71  HIS I CG  1 
ATOM   8312  N  ND1 . HIS H  1 72  ? 145.927 23.906  15.628  1.00 2.00  ? 71  HIS I ND1 1 
ATOM   8313  C  CD2 . HIS H  1 72  ? 145.321 25.988  15.854  1.00 2.00  ? 71  HIS I CD2 1 
ATOM   8314  C  CE1 . HIS H  1 72  ? 144.757 23.940  16.161  1.00 2.00  ? 71  HIS I CE1 1 
ATOM   8315  N  NE2 . HIS H  1 72  ? 144.400 25.188  16.287  1.00 2.00  ? 71  HIS I NE2 1 
ATOM   8316  N  N   . GLY H  1 73  ? 145.141 26.134  12.481  1.00 2.00  ? 72  GLY I N   1 
ATOM   8317  C  CA  . GLY H  1 73  ? 143.988 26.977  12.292  1.00 2.00  ? 72  GLY I CA  1 
ATOM   8318  C  C   . GLY H  1 73  ? 142.761 26.116  12.535  1.00 2.00  ? 72  GLY I C   1 
ATOM   8319  O  O   . GLY H  1 73  ? 142.847 25.008  13.064  1.00 2.00  ? 72  GLY I O   1 
ATOM   8320  N  N   . GLY H  1 74  ? 141.588 26.623  12.252  1.00 3.66  ? 73  GLY I N   1 
ATOM   8321  C  CA  . GLY H  1 74  ? 140.382 25.848  12.321  1.00 3.37  ? 73  GLY I CA  1 
ATOM   8322  C  C   . GLY H  1 74  ? 140.255 25.117  11.004  1.00 5.66  ? 73  GLY I C   1 
ATOM   8323  O  O   . GLY H  1 74  ? 140.875 25.562  10.038  1.00 5.44  ? 73  GLY I O   1 
ATOM   8324  N  N   . PRO H  1 75  ? 139.436 24.050  10.889  1.00 6.53  ? 74  PRO I N   1 
ATOM   8325  C  CA  . PRO H  1 75  ? 139.262 23.218  9.694   1.00 6.88  ? 74  PRO I CA  1 
ATOM   8326  C  C   . PRO H  1 75  ? 138.882 23.832  8.347   1.00 9.52  ? 74  PRO I C   1 
ATOM   8327  O  O   . PRO H  1 75  ? 139.104 23.274  7.276   1.00 11.17 ? 74  PRO I O   1 
ATOM   8328  C  CB  . PRO H  1 75  ? 138.265 22.228  10.145  1.00 7.53  ? 74  PRO I CB  1 
ATOM   8329  C  CG  . PRO H  1 75  ? 137.402 23.017  11.090  1.00 3.97  ? 74  PRO I CG  1 
ATOM   8330  C  CD  . PRO H  1 75  ? 138.452 23.683  11.906  1.00 4.50  ? 74  PRO I CD  1 
ATOM   8331  N  N   . LYS H  1 76  ? 138.255 24.995  8.362   1.00 13.61 ? 75  LYS I N   1 
ATOM   8332  C  CA  . LYS H  1 76  ? 137.853 25.666  7.147   1.00 15.42 ? 75  LYS I CA  1 
ATOM   8333  C  C   . LYS H  1 76  ? 138.973 26.537  6.685   1.00 14.09 ? 75  LYS I C   1 
ATOM   8334  O  O   . LYS H  1 76  ? 138.837 27.119  5.617   1.00 14.28 ? 75  LYS I O   1 
ATOM   8335  C  CB  . LYS H  1 76  ? 136.670 26.600  7.330   1.00 21.06 ? 75  LYS I CB  1 
ATOM   8336  C  CG  . LYS H  1 76  ? 135.282 25.999  7.581   1.00 27.82 ? 75  LYS I CG  1 
ATOM   8337  C  CD  . LYS H  1 76  ? 134.215 27.113  7.849   1.00 33.96 ? 75  LYS I CD  1 
ATOM   8338  C  CE  . LYS H  1 76  ? 134.398 27.965  9.131   1.00 34.52 ? 75  LYS I CE  1 
ATOM   8339  N  NZ  . LYS H  1 76  ? 133.368 28.993  9.200   1.00 36.60 ? 75  LYS I NZ  1 
ATOM   8340  N  N   . ASP H  1 77  ? 140.038 26.720  7.439   1.00 12.25 ? 76  ASP I N   1 
ATOM   8341  C  CA  . ASP H  1 77  ? 141.058 27.597  6.951   1.00 13.31 ? 76  ASP I CA  1 
ATOM   8342  C  C   . ASP H  1 77  ? 141.935 26.819  5.995   1.00 14.93 ? 76  ASP I C   1 
ATOM   8343  O  O   . ASP H  1 77  ? 141.811 25.608  5.797   1.00 19.20 ? 76  ASP I O   1 
ATOM   8344  C  CB  . ASP H  1 77  ? 141.811 28.160  8.158   1.00 14.70 ? 76  ASP I CB  1 
ATOM   8345  C  CG  . ASP H  1 77  ? 140.918 28.983  9.090   1.00 16.63 ? 76  ASP I CG  1 
ATOM   8346  O  OD1 . ASP H  1 77  ? 140.159 29.807  8.578   1.00 18.31 ? 76  ASP I OD1 1 
ATOM   8347  O  OD2 . ASP H  1 77  ? 140.956 28.783  10.317  1.00 16.08 ? 76  ASP I OD2 1 
ATOM   8348  N  N   . GLU H  1 78  ? 142.760 27.545  5.274   1.00 17.33 ? 77  GLU I N   1 
ATOM   8349  C  CA  . GLU H  1 78  ? 143.667 26.990  4.263   1.00 19.56 ? 77  GLU I CA  1 
ATOM   8350  C  C   . GLU H  1 78  ? 144.984 26.574  4.917   1.00 18.12 ? 77  GLU I C   1 
ATOM   8351  O  O   . GLU H  1 78  ? 145.618 25.577  4.572   1.00 17.91 ? 77  GLU I O   1 
ATOM   8352  C  CB  . GLU H  1 78  ? 143.891 28.076  3.210   1.00 24.58 ? 77  GLU I CB  1 
ATOM   8353  C  CG  . GLU H  1 78  ? 144.557 27.716  1.891   1.00 31.00 ? 77  GLU I CG  1 
ATOM   8354  C  CD  . GLU H  1 78  ? 143.581 27.211  0.831   1.00 34.98 ? 77  GLU I CD  1 
ATOM   8355  O  OE1 . GLU H  1 78  ? 142.613 27.924  0.524   1.00 38.67 ? 77  GLU I OE1 1 
ATOM   8356  O  OE2 . GLU H  1 78  ? 143.807 26.116  0.299   1.00 36.28 ? 77  GLU I OE2 1 
ATOM   8357  N  N   . GLU H  1 79  ? 145.391 27.423  5.868   1.00 18.07 ? 78  GLU I N   1 
ATOM   8358  C  CA  . GLU H  1 79  ? 146.567 27.246  6.713   1.00 14.69 ? 78  GLU I CA  1 
ATOM   8359  C  C   . GLU H  1 79  ? 145.994 26.594  7.966   1.00 12.57 ? 78  GLU I C   1 
ATOM   8360  O  O   . GLU H  1 79  ? 145.224 27.163  8.752   1.00 10.78 ? 78  GLU I O   1 
ATOM   8361  C  CB  . GLU H  1 79  ? 147.192 28.614  7.052   1.00 16.98 ? 78  GLU I CB  1 
ATOM   8362  C  CG  . GLU H  1 79  ? 148.592 28.749  7.710   1.00 16.37 ? 78  GLU I CG  1 
ATOM   8363  C  CD  . GLU H  1 79  ? 149.855 28.235  7.001   1.00 16.58 ? 78  GLU I CD  1 
ATOM   8364  O  OE1 . GLU H  1 79  ? 149.813 27.829  5.830   1.00 19.11 ? 78  GLU I OE1 1 
ATOM   8365  O  OE2 . GLU H  1 79  ? 150.907 28.237  7.652   1.00 16.91 ? 78  GLU I OE2 1 
ATOM   8366  N  N   . ARG H  1 80  ? 146.183 25.291  7.937   1.00 8.35  ? 79  ARG I N   1 
ATOM   8367  C  CA  . ARG H  1 80  ? 145.869 24.480  9.066   1.00 4.98  ? 79  ARG I CA  1 
ATOM   8368  C  C   . ARG H  1 80  ? 146.717 23.303  8.845   1.00 5.26  ? 79  ARG I C   1 
ATOM   8369  O  O   . ARG H  1 80  ? 147.293 23.100  7.768   1.00 6.95  ? 79  ARG I O   1 
ATOM   8370  C  CB  . ARG H  1 80  ? 144.406 24.051  9.140   1.00 5.42  ? 79  ARG I CB  1 
ATOM   8371  C  CG  . ARG H  1 80  ? 143.559 23.642  7.945   1.00 4.14  ? 79  ARG I CG  1 
ATOM   8372  C  CD  . ARG H  1 80  ? 143.547 22.164  7.947   1.00 6.42  ? 79  ARG I CD  1 
ATOM   8373  N  NE  . ARG H  1 80  ? 142.185 21.691  7.921   1.00 6.27  ? 79  ARG I NE  1 
ATOM   8374  C  CZ  . ARG H  1 80  ? 141.874 20.445  8.276   1.00 5.00  ? 79  ARG I CZ  1 
ATOM   8375  N  NH1 . ARG H  1 80  ? 142.734 19.538  8.703   1.00 3.74  ? 79  ARG I NH1 1 
ATOM   8376  N  NH2 . ARG H  1 80  ? 140.623 20.099  8.204   1.00 7.37  ? 79  ARG I NH2 1 
ATOM   8377  N  N   . HIS H  1 81  ? 146.835 22.610  9.956   1.00 3.44  ? 80  HIS I N   1 
ATOM   8378  C  CA  . HIS H  1 81  ? 147.580 21.389  9.955   1.00 2.00  ? 80  HIS I CA  1 
ATOM   8379  C  C   . HIS H  1 81  ? 146.584 20.338  9.517   1.00 2.00  ? 80  HIS I C   1 
ATOM   8380  O  O   . HIS H  1 81  ? 145.395 20.501  9.750   1.00 2.16  ? 80  HIS I O   1 
ATOM   8381  C  CB  . HIS H  1 81  ? 148.012 20.952  11.293  1.00 2.51  ? 80  HIS I CB  1 
ATOM   8382  C  CG  . HIS H  1 81  ? 148.698 21.877  12.251  1.00 2.60  ? 80  HIS I CG  1 
ATOM   8383  N  ND1 . HIS H  1 81  ? 148.253 22.004  13.468  1.00 2.00  ? 80  HIS I ND1 1 
ATOM   8384  C  CD2 . HIS H  1 81  ? 149.882 22.551  12.137  1.00 3.47  ? 80  HIS I CD2 1 
ATOM   8385  C  CE1 . HIS H  1 81  ? 149.122 22.706  14.136  1.00 2.00  ? 80  HIS I CE1 1 
ATOM   8386  N  NE2 . HIS H  1 81  ? 150.100 23.031  13.327  1.00 2.00  ? 80  HIS I NE2 1 
ATOM   8387  N  N   . VAL H  1 82  ? 146.989 19.229  8.951   1.00 2.00  ? 81  VAL I N   1 
ATOM   8388  C  CA  . VAL H  1 82  ? 146.064 18.206  8.551   1.00 2.00  ? 81  VAL I CA  1 
ATOM   8389  C  C   . VAL H  1 82  ? 145.264 17.729  9.740   1.00 2.33  ? 81  VAL I C   1 
ATOM   8390  O  O   . VAL H  1 82  ? 144.064 17.491  9.657   1.00 2.97  ? 81  VAL I O   1 
ATOM   8391  C  CB  . VAL H  1 82  ? 146.863 17.069  7.904   1.00 2.48  ? 81  VAL I CB  1 
ATOM   8392  C  CG1 . VAL H  1 82  ? 145.968 15.902  7.534   1.00 2.00  ? 81  VAL I CG1 1 
ATOM   8393  C  CG2 . VAL H  1 82  ? 147.498 17.599  6.618   1.00 2.00  ? 81  VAL I CG2 1 
ATOM   8394  N  N   . GLY H  1 83  ? 145.855 17.673  10.917  1.00 2.86  ? 82  GLY I N   1 
ATOM   8395  C  CA  . GLY H  1 83  ? 145.160 17.189  12.083  1.00 2.00  ? 82  GLY I CA  1 
ATOM   8396  C  C   . GLY H  1 83  ? 144.174 18.161  12.662  1.00 2.00  ? 82  GLY I C   1 
ATOM   8397  O  O   . GLY H  1 83  ? 143.592 17.824  13.659  1.00 3.19  ? 82  GLY I O   1 
ATOM   8398  N  N   . ASP H  1 84  ? 143.888 19.360  12.191  1.00 3.52  ? 83  ASP I N   1 
ATOM   8399  C  CA  . ASP H  1 84  ? 143.004 20.312  12.838  1.00 2.00  ? 83  ASP I CA  1 
ATOM   8400  C  C   . ASP H  1 84  ? 141.523 20.222  12.498  1.00 2.06  ? 83  ASP I C   1 
ATOM   8401  O  O   . ASP H  1 84  ? 140.990 20.787  11.526  1.00 2.00  ? 83  ASP I O   1 
ATOM   8402  C  CB  . ASP H  1 84  ? 143.507 21.705  12.523  1.00 2.00  ? 83  ASP I CB  1 
ATOM   8403  C  CG  . ASP H  1 84  ? 144.856 22.050  13.130  1.00 2.00  ? 83  ASP I CG  1 
ATOM   8404  O  OD1 . ASP H  1 84  ? 145.375 21.361  14.011  1.00 2.00  ? 83  ASP I OD1 1 
ATOM   8405  O  OD2 . ASP H  1 84  ? 145.381 23.056  12.701  1.00 4.61  ? 83  ASP I OD2 1 
ATOM   8406  N  N   . LEU H  1 85  ? 140.841 19.530  13.413  1.00 2.55  ? 84  LEU I N   1 
ATOM   8407  C  CA  . LEU H  1 85  ? 139.412 19.323  13.262  1.00 2.00  ? 84  LEU I CA  1 
ATOM   8408  C  C   . LEU H  1 85  ? 138.622 20.264  14.118  1.00 2.00  ? 84  LEU I C   1 
ATOM   8409  O  O   . LEU H  1 85  ? 137.410 20.187  14.217  1.00 2.00  ? 84  LEU I O   1 
ATOM   8410  C  CB  . LEU H  1 85  ? 139.092 17.802  13.543  1.00 2.00  ? 84  LEU I CB  1 
ATOM   8411  C  CG  . LEU H  1 85  ? 139.728 16.847  12.510  1.00 2.00  ? 84  LEU I CG  1 
ATOM   8412  C  CD1 . LEU H  1 85  ? 139.523 15.355  12.795  1.00 2.00  ? 84  LEU I CD1 1 
ATOM   8413  C  CD2 . LEU H  1 85  ? 139.093 17.227  11.201  1.00 2.00  ? 84  LEU I CD2 1 
ATOM   8414  N  N   . GLY H  1 86  ? 139.285 21.245  14.702  1.00 2.73  ? 85  GLY I N   1 
ATOM   8415  C  CA  . GLY H  1 86  ? 138.595 22.355  15.352  1.00 2.89  ? 85  GLY I CA  1 
ATOM   8416  C  C   . GLY H  1 86  ? 138.001 22.008  16.684  1.00 2.00  ? 85  GLY I C   1 
ATOM   8417  O  O   . GLY H  1 86  ? 138.719 21.448  17.501  1.00 2.00  ? 85  GLY I O   1 
ATOM   8418  N  N   . ASN H  1 87  ? 136.701 22.212  16.847  1.00 2.21  ? 86  ASN I N   1 
ATOM   8419  C  CA  . ASN H  1 87  ? 136.039 21.994  18.125  1.00 2.51  ? 86  ASN I CA  1 
ATOM   8420  C  C   . ASN H  1 87  ? 134.879 21.037  18.125  1.00 2.00  ? 86  ASN I C   1 
ATOM   8421  O  O   . ASN H  1 87  ? 134.275 20.837  17.089  1.00 2.00  ? 86  ASN I O   1 
ATOM   8422  C  CB  . ASN H  1 87  ? 135.502 23.319  18.733  1.00 2.39  ? 86  ASN I CB  1 
ATOM   8423  C  CG  . ASN H  1 87  ? 136.618 24.164  19.284  1.00 2.00  ? 86  ASN I CG  1 
ATOM   8424  O  OD1 . ASN H  1 87  ? 137.467 23.701  20.055  1.00 2.00  ? 86  ASN I OD1 1 
ATOM   8425  N  ND2 . ASN H  1 87  ? 136.653 25.406  18.842  1.00 2.00  ? 86  ASN I ND2 1 
ATOM   8426  N  N   . VAL H  1 88  ? 134.592 20.407  19.271  1.00 2.31  ? 87  VAL I N   1 
ATOM   8427  C  CA  . VAL H  1 88  ? 133.379 19.637  19.464  1.00 3.29  ? 87  VAL I CA  1 
ATOM   8428  C  C   . VAL H  1 88  ? 132.782 20.176  20.740  1.00 2.00  ? 87  VAL I C   1 
ATOM   8429  O  O   . VAL H  1 88  ? 133.522 20.638  21.601  1.00 2.00  ? 87  VAL I O   1 
ATOM   8430  C  CB  . VAL H  1 88  ? 133.558 18.085  19.648  1.00 2.00  ? 87  VAL I CB  1 
ATOM   8431  C  CG1 . VAL H  1 88  ? 134.067 17.544  18.356  1.00 2.00  ? 87  VAL I CG1 1 
ATOM   8432  C  CG2 . VAL H  1 88  ? 134.475 17.711  20.738  1.00 3.49  ? 87  VAL I CG2 1 
ATOM   8433  N  N   . THR H  1 89  ? 131.460 20.103  20.818  1.00 2.00  ? 88  THR I N   1 
ATOM   8434  C  CA  . THR H  1 89  ? 130.690 20.685  21.886  1.00 2.60  ? 88  THR I CA  1 
ATOM   8435  C  C   . THR H  1 89  ? 129.979 19.720  22.832  1.00 3.19  ? 88  THR I C   1 
ATOM   8436  O  O   . THR H  1 89  ? 129.095 19.010  22.354  1.00 5.81  ? 88  THR I O   1 
ATOM   8437  C  CB  . THR H  1 89  ? 129.691 21.646  21.221  1.00 2.00  ? 88  THR I CB  1 
ATOM   8438  O  OG1 . THR H  1 89  ? 130.474 22.557  20.463  1.00 2.00  ? 88  THR I OG1 1 
ATOM   8439  C  CG2 . THR H  1 89  ? 128.860 22.441  22.188  1.00 2.00  ? 88  THR I CG2 1 
ATOM   8440  N  N   . ALA H  1 90  ? 130.289 19.679  24.139  1.00 2.00  ? 89  ALA I N   1 
ATOM   8441  C  CA  . ALA H  1 90  ? 129.567 18.869  25.122  1.00 2.00  ? 89  ALA I CA  1 
ATOM   8442  C  C   . ALA H  1 90  ? 128.320 19.585  25.546  1.00 3.13  ? 89  ALA I C   1 
ATOM   8443  O  O   . ALA H  1 90  ? 128.379 20.777  25.777  1.00 7.86  ? 89  ALA I O   1 
ATOM   8444  C  CB  . ALA H  1 90  ? 130.383 18.647  26.369  1.00 2.00  ? 89  ALA I CB  1 
ATOM   8445  N  N   . ASP H  1 91  ? 127.148 18.979  25.613  1.00 6.19  ? 90  ASP I N   1 
ATOM   8446  C  CA  . ASP H  1 91  ? 125.949 19.621  26.143  1.00 6.93  ? 90  ASP I CA  1 
ATOM   8447  C  C   . ASP H  1 91  ? 125.985 19.753  27.672  1.00 8.86  ? 90  ASP I C   1 
ATOM   8448  O  O   . ASP H  1 91  ? 126.984 19.377  28.285  1.00 8.10  ? 90  ASP I O   1 
ATOM   8449  C  CB  . ASP H  1 91  ? 124.757 18.799  25.762  1.00 8.61  ? 90  ASP I CB  1 
ATOM   8450  C  CG  . ASP H  1 91  ? 124.836 17.326  26.190  1.00 12.21 ? 90  ASP I CG  1 
ATOM   8451  O  OD1 . ASP H  1 91  ? 125.494 16.980  27.175  1.00 9.24  ? 90  ASP I OD1 1 
ATOM   8452  O  OD2 . ASP H  1 91  ? 124.222 16.501  25.513  1.00 15.26 ? 90  ASP I OD2 1 
ATOM   8453  N  N   . LYS H  1 92  ? 124.867 20.084  28.341  1.00 12.23 ? 91  LYS I N   1 
ATOM   8454  C  CA  . LYS H  1 92  ? 124.828 20.196  29.807  1.00 16.41 ? 91  LYS I CA  1 
ATOM   8455  C  C   . LYS H  1 92  ? 125.097 18.954  30.623  1.00 16.98 ? 91  LYS I C   1 
ATOM   8456  O  O   . LYS H  1 92  ? 125.280 19.053  31.839  1.00 17.16 ? 91  LYS I O   1 
ATOM   8457  C  CB  . LYS H  1 92  ? 123.487 20.754  30.296  1.00 19.31 ? 91  LYS I CB  1 
ATOM   8458  C  CG  . LYS H  1 92  ? 122.219 20.217  29.638  1.00 25.45 ? 91  LYS I CG  1 
ATOM   8459  C  CD  . LYS H  1 92  ? 120.974 21.083  29.941  1.00 30.89 ? 91  LYS I CD  1 
ATOM   8460  C  CE  . LYS H  1 92  ? 121.044 22.521  29.349  1.00 35.28 ? 91  LYS I CE  1 
ATOM   8461  N  NZ  . LYS H  1 92  ? 119.825 23.301  29.535  1.00 36.32 ? 91  LYS I NZ  1 
ATOM   8462  N  N   . ASP H  1 93  ? 125.083 17.809  29.922  1.00 17.21 ? 92  ASP I N   1 
ATOM   8463  C  CA  . ASP H  1 93  ? 125.398 16.497  30.480  1.00 17.90 ? 92  ASP I CA  1 
ATOM   8464  C  C   . ASP H  1 93  ? 126.798 15.997  30.106  1.00 17.81 ? 92  ASP I C   1 
ATOM   8465  O  O   . ASP H  1 93  ? 127.206 14.880  30.443  1.00 20.02 ? 92  ASP I O   1 
ATOM   8466  C  CB  . ASP H  1 93  ? 124.368 15.474  30.002  1.00 18.85 ? 92  ASP I CB  1 
ATOM   8467  C  CG  . ASP H  1 93  ? 122.959 15.711  30.531  1.00 24.04 ? 92  ASP I CG  1 
ATOM   8468  O  OD1 . ASP H  1 93  ? 122.778 16.383  31.563  1.00 22.40 ? 92  ASP I OD1 1 
ATOM   8469  O  OD2 . ASP H  1 93  ? 122.025 15.214  29.887  1.00 28.56 ? 92  ASP I OD2 1 
ATOM   8470  N  N   . GLY H  1 94  ? 127.557 16.802  29.361  1.00 14.33 ? 93  GLY I N   1 
ATOM   8471  C  CA  . GLY H  1 94  ? 128.881 16.403  29.003  1.00 9.22  ? 93  GLY I CA  1 
ATOM   8472  C  C   . GLY H  1 94  ? 128.969 15.408  27.897  1.00 7.07  ? 93  GLY I C   1 
ATOM   8473  O  O   . GLY H  1 94  ? 129.937 14.665  27.839  1.00 8.25  ? 93  GLY I O   1 
ATOM   8474  N  N   . VAL H  1 95  ? 128.033 15.440  26.976  1.00 4.75  ? 94  VAL I N   1 
ATOM   8475  C  CA  . VAL H  1 95  ? 128.034 14.542  25.836  1.00 4.40  ? 94  VAL I CA  1 
ATOM   8476  C  C   . VAL H  1 95  ? 128.201 15.400  24.617  1.00 4.29  ? 94  VAL I C   1 
ATOM   8477  O  O   . VAL H  1 95  ? 127.391 16.305  24.376  1.00 5.50  ? 94  VAL I O   1 
ATOM   8478  C  CB  . VAL H  1 95  ? 126.708 13.775  25.709  1.00 2.01  ? 94  VAL I CB  1 
ATOM   8479  C  CG1 . VAL H  1 95  ? 126.651 12.952  24.448  1.00 2.00  ? 94  VAL I CG1 1 
ATOM   8480  C  CG2 . VAL H  1 95  ? 126.594 12.848  26.903  1.00 2.00  ? 94  VAL I CG2 1 
ATOM   8481  N  N   . ALA H  1 96  ? 129.262 15.152  23.872  1.00 5.10  ? 95  ALA I N   1 
ATOM   8482  C  CA  . ALA H  1 96  ? 129.538 15.809  22.600  1.00 2.95  ? 95  ALA I CA  1 
ATOM   8483  C  C   . ALA H  1 96  ? 129.159 14.766  21.538  1.00 2.17  ? 95  ALA I C   1 
ATOM   8484  O  O   . ALA H  1 96  ? 129.867 13.782  21.370  1.00 3.00  ? 95  ALA I O   1 
ATOM   8485  C  CB  . ALA H  1 96  ? 131.018 16.115  22.535  1.00 2.00  ? 95  ALA I CB  1 
ATOM   8486  N  N   . ASP H  1 97  ? 128.002 14.863  20.917  1.00 2.00  ? 96  ASP I N   1 
ATOM   8487  C  CA  . ASP H  1 97  ? 127.578 14.018  19.832  1.00 2.51  ? 96  ASP I CA  1 
ATOM   8488  C  C   . ASP H  1 97  ? 128.185 14.612  18.580  1.00 3.50  ? 96  ASP I C   1 
ATOM   8489  O  O   . ASP H  1 97  ? 127.577 15.467  17.933  1.00 4.36  ? 96  ASP I O   1 
ATOM   8490  C  CB  . ASP H  1 97  ? 126.064 14.035  19.671  1.00 9.21  ? 96  ASP I CB  1 
ATOM   8491  C  CG  . ASP H  1 97  ? 125.263 13.469  20.851  1.00 15.22 ? 96  ASP I CG  1 
ATOM   8492  O  OD1 . ASP H  1 97  ? 125.652 12.390  21.332  1.00 12.65 ? 96  ASP I OD1 1 
ATOM   8493  O  OD2 . ASP H  1 97  ? 124.257 14.101  21.256  1.00 17.22 ? 96  ASP I OD2 1 
ATOM   8494  N  N   . VAL H  1 98  ? 129.359 14.135  18.219  1.00 3.26  ? 97  VAL I N   1 
ATOM   8495  C  CA  . VAL H  1 98  ? 130.187 14.686  17.179  1.00 3.37  ? 97  VAL I CA  1 
ATOM   8496  C  C   . VAL H  1 98  ? 129.629 14.411  15.822  1.00 5.03  ? 97  VAL I C   1 
ATOM   8497  O  O   . VAL H  1 98  ? 129.210 13.290  15.517  1.00 8.86  ? 97  VAL I O   1 
ATOM   8498  C  CB  . VAL H  1 98  ? 131.584 14.091  17.210  1.00 2.00  ? 97  VAL I CB  1 
ATOM   8499  C  CG1 . VAL H  1 98  ? 132.424 14.719  16.087  1.00 2.00  ? 97  VAL I CG1 1 
ATOM   8500  C  CG2 . VAL H  1 98  ? 132.166 14.262  18.601  1.00 2.00  ? 97  VAL I CG2 1 
ATOM   8501  N  N   . SER H  1 99  ? 129.751 15.417  14.988  1.00 5.32  ? 98  SER I N   1 
ATOM   8502  C  CA  . SER H  1 99  ? 129.348 15.265  13.619  1.00 7.14  ? 98  SER I CA  1 
ATOM   8503  C  C   . SER H  1 99  ? 130.199 16.241  12.823  1.00 6.37  ? 98  SER I C   1 
ATOM   8504  O  O   . SER H  1 99  ? 129.846 17.412  12.763  1.00 8.15  ? 98  SER I O   1 
ATOM   8505  C  CB  . SER H  1 99  ? 127.867 15.559  13.616  1.00 8.50  ? 98  SER I CB  1 
ATOM   8506  O  OG  . SER H  1 99  ? 127.257 15.822  12.356  1.00 14.63 ? 98  SER I OG  1 
ATOM   8507  N  N   . ILE H  1 100 ? 131.336 15.857  12.262  1.00 4.36  ? 99  ILE I N   1 
ATOM   8508  C  CA  . ILE H  1 100 ? 132.198 16.728  11.478  1.00 3.54  ? 99  ILE I CA  1 
ATOM   8509  C  C   . ILE H  1 100 ? 132.301 16.054  10.101  1.00 6.00  ? 99  ILE I C   1 
ATOM   8510  O  O   . ILE H  1 100 ? 132.073 14.845  9.971   1.00 8.70  ? 99  ILE I O   1 
ATOM   8511  C  CB  . ILE H  1 100 ? 133.578 16.815  12.154  1.00 2.00  ? 99  ILE I CB  1 
ATOM   8512  C  CG1 . ILE H  1 100 ? 133.396 17.654  13.350  1.00 2.00  ? 99  ILE I CG1 1 
ATOM   8513  C  CG2 . ILE H  1 100 ? 134.662 17.461  11.299  1.00 2.00  ? 99  ILE I CG2 1 
ATOM   8514  C  CD1 . ILE H  1 100 ? 134.594 17.679  14.325  1.00 2.00  ? 99  ILE I CD1 1 
ATOM   8515  N  N   . GLU H  1 101 ? 132.594 16.772  9.041   1.00 4.60  ? 100 GLU I N   1 
ATOM   8516  C  CA  . GLU H  1 101 ? 132.849 16.173  7.778   1.00 7.97  ? 100 GLU I CA  1 
ATOM   8517  C  C   . GLU H  1 101 ? 134.111 16.898  7.415   1.00 5.57  ? 100 GLU I C   1 
ATOM   8518  O  O   . GLU H  1 101 ? 134.148 18.128  7.562   1.00 8.04  ? 100 GLU I O   1 
ATOM   8519  C  CB  . GLU H  1 101 ? 131.764 16.497  6.797   1.00 14.95 ? 100 GLU I CB  1 
ATOM   8520  C  CG  . GLU H  1 101 ? 131.881 15.574  5.566   1.00 26.50 ? 100 GLU I CG  1 
ATOM   8521  C  CD  . GLU H  1 101 ? 131.110 16.043  4.323   1.00 33.71 ? 100 GLU I CD  1 
ATOM   8522  O  OE1 . GLU H  1 101 ? 131.088 17.266  4.067   1.00 34.54 ? 100 GLU I OE1 1 
ATOM   8523  O  OE2 . GLU H  1 101 ? 130.557 15.177  3.613   1.00 37.80 ? 100 GLU I OE2 1 
ATOM   8524  N  N   . ASP H  1 102 ? 135.198 16.274  7.000   1.00 4.36  ? 101 ASP I N   1 
ATOM   8525  C  CA  . ASP H  1 102 ? 136.359 17.088  6.710   1.00 6.15  ? 101 ASP I CA  1 
ATOM   8526  C  C   . ASP H  1 102 ? 136.939 16.566  5.428   1.00 7.69  ? 101 ASP I C   1 
ATOM   8527  O  O   . ASP H  1 102 ? 136.973 15.355  5.228   1.00 12.90 ? 101 ASP I O   1 
ATOM   8528  C  CB  . ASP H  1 102 ? 137.381 16.976  7.832   1.00 4.70  ? 101 ASP I CB  1 
ATOM   8529  C  CG  . ASP H  1 102 ? 138.499 17.984  7.685   1.00 4.10  ? 101 ASP I CG  1 
ATOM   8530  O  OD1 . ASP H  1 102 ? 138.217 19.179  7.817   1.00 9.85  ? 101 ASP I OD1 1 
ATOM   8531  O  OD2 . ASP H  1 102 ? 139.631 17.590  7.419   1.00 2.00  ? 101 ASP I OD2 1 
ATOM   8532  N  N   . SER H  1 103 ? 137.377 17.454  4.573   1.00 7.86  ? 102 SER I N   1 
ATOM   8533  C  CA  . SER H  1 103 ? 137.947 17.134  3.284   1.00 10.92 ? 102 SER I CA  1 
ATOM   8534  C  C   . SER H  1 103 ? 139.453 17.332  3.172   1.00 12.54 ? 102 SER I C   1 
ATOM   8535  O  O   . SER H  1 103 ? 139.933 17.616  2.074   1.00 14.57 ? 102 SER I O   1 
ATOM   8536  C  CB  . SER H  1 103 ? 137.207 17.993  2.236   1.00 15.64 ? 102 SER I CB  1 
ATOM   8537  O  OG  . SER H  1 103 ? 136.661 19.200  2.797   1.00 23.40 ? 102 SER I OG  1 
ATOM   8538  N  N   . VAL H  1 104 ? 140.221 17.300  4.286   1.00 10.45 ? 103 VAL I N   1 
ATOM   8539  C  CA  . VAL H  1 104 ? 141.682 17.448  4.273   1.00 5.89  ? 103 VAL I CA  1 
ATOM   8540  C  C   . VAL H  1 104 ? 142.355 16.226  4.910   1.00 7.48  ? 103 VAL I C   1 
ATOM   8541  O  O   . VAL H  1 104 ? 143.394 15.736  4.452   1.00 9.90  ? 103 VAL I O   1 
ATOM   8542  C  CB  . VAL H  1 104 ? 142.029 18.758  5.025   1.00 4.08  ? 103 VAL I CB  1 
ATOM   8543  C  CG1 . VAL H  1 104 ? 143.535 18.936  5.302   1.00 2.00  ? 103 VAL I CG1 1 
ATOM   8544  C  CG2 . VAL H  1 104 ? 141.540 19.899  4.158   1.00 2.00  ? 103 VAL I CG2 1 
ATOM   8545  N  N   . ILE H  1 105 ? 141.790 15.743  6.022   1.00 7.80  ? 104 ILE I N   1 
ATOM   8546  C  CA  . ILE H  1 105 ? 142.270 14.526  6.686   1.00 7.31  ? 104 ILE I CA  1 
ATOM   8547  C  C   . ILE H  1 105 ? 141.971 13.369  5.752   1.00 8.27  ? 104 ILE I C   1 
ATOM   8548  O  O   . ILE H  1 105 ? 141.071 13.480  4.922   1.00 7.98  ? 104 ILE I O   1 
ATOM   8549  C  CB  . ILE H  1 105 ? 141.553 14.254  8.036   1.00 2.50  ? 104 ILE I CB  1 
ATOM   8550  C  CG1 . ILE H  1 105 ? 140.046 14.326  7.958   1.00 2.00  ? 104 ILE I CG1 1 
ATOM   8551  C  CG2 . ILE H  1 105 ? 142.055 15.299  8.979   1.00 2.00  ? 104 ILE I CG2 1 
ATOM   8552  C  CD1 . ILE H  1 105 ? 139.251 13.707  9.112   1.00 2.00  ? 104 ILE I CD1 1 
ATOM   8553  N  N   . SER H  1 106 ? 142.663 12.252  5.838   1.00 8.85  ? 105 SER I N   1 
ATOM   8554  C  CA  . SER H  1 106 ? 142.330 11.157  4.976   1.00 6.76  ? 105 SER I CA  1 
ATOM   8555  C  C   . SER H  1 106 ? 142.634 9.864   5.680   1.00 6.62  ? 105 SER I C   1 
ATOM   8556  O  O   . SER H  1 106 ? 143.410 9.826   6.644   1.00 6.97  ? 105 SER I O   1 
ATOM   8557  C  CB  . SER H  1 106 ? 143.144 11.224  3.744   1.00 6.27  ? 105 SER I CB  1 
ATOM   8558  O  OG  . SER H  1 106 ? 142.238 10.625  2.860   1.00 13.80 ? 105 SER I OG  1 
ATOM   8559  N  N   . LEU H  1 107 ? 142.010 8.820   5.130   1.00 5.39  ? 106 LEU I N   1 
ATOM   8560  C  CA  . LEU H  1 107 ? 142.226 7.458   5.545   1.00 4.28  ? 106 LEU I CA  1 
ATOM   8561  C  C   . LEU H  1 107 ? 143.089 6.791   4.495   1.00 4.74  ? 106 LEU I C   1 
ATOM   8562  O  O   . LEU H  1 107 ? 143.225 5.576   4.592   1.00 5.61  ? 106 LEU I O   1 
ATOM   8563  C  CB  . LEU H  1 107 ? 140.916 6.676   5.666   1.00 2.00  ? 106 LEU I CB  1 
ATOM   8564  C  CG  . LEU H  1 107 ? 139.817 7.335   6.481   1.00 3.73  ? 106 LEU I CG  1 
ATOM   8565  C  CD1 . LEU H  1 107 ? 138.795 6.307   6.863   1.00 4.25  ? 106 LEU I CD1 1 
ATOM   8566  C  CD2 . LEU H  1 107 ? 140.366 7.907   7.765   1.00 4.35  ? 106 LEU I CD2 1 
ATOM   8567  N  N   . SER H  1 108 ? 143.712 7.459   3.503   1.00 5.09  ? 107 SER I N   1 
ATOM   8568  C  CA  . SER H  1 108 ? 144.546 6.792   2.506   1.00 6.97  ? 107 SER I CA  1 
ATOM   8569  C  C   . SER H  1 108 ? 145.813 7.554   2.181   1.00 7.35  ? 107 SER I C   1 
ATOM   8570  O  O   . SER H  1 108 ? 145.850 8.758   2.371   1.00 11.63 ? 107 SER I O   1 
ATOM   8571  C  CB  . SER H  1 108 ? 143.770 6.615   1.183   1.00 10.13 ? 107 SER I CB  1 
ATOM   8572  O  OG  . SER H  1 108 ? 142.530 5.924   1.308   1.00 11.57 ? 107 SER I OG  1 
ATOM   8573  N  N   . GLY H  1 109 ? 146.899 6.947   1.714   1.00 7.91  ? 108 GLY I N   1 
ATOM   8574  C  CA  . GLY H  1 109 ? 148.059 7.662   1.233   1.00 11.71 ? 108 GLY I CA  1 
ATOM   8575  C  C   . GLY H  1 109 ? 148.810 8.276   2.408   1.00 16.76 ? 108 GLY I C   1 
ATOM   8576  O  O   . GLY H  1 109 ? 148.417 8.046   3.548   1.00 18.16 ? 108 GLY I O   1 
ATOM   8577  N  N   . ASP H  1 110 ? 149.866 9.082   2.195   1.00 18.85 ? 109 ASP I N   1 
ATOM   8578  C  CA  . ASP H  1 110 ? 150.676 9.710   3.251   1.00 20.17 ? 109 ASP I CA  1 
ATOM   8579  C  C   . ASP H  1 110 ? 150.004 10.846  4.028   1.00 17.84 ? 109 ASP I C   1 
ATOM   8580  O  O   . ASP H  1 110 ? 150.659 11.637  4.691   1.00 17.96 ? 109 ASP I O   1 
ATOM   8581  C  CB  . ASP H  1 110 ? 151.970 10.286  2.665   1.00 24.53 ? 109 ASP I CB  1 
ATOM   8582  C  CG  . ASP H  1 110 ? 152.739 9.439   1.650   1.00 29.34 ? 109 ASP I CG  1 
ATOM   8583  O  OD1 . ASP H  1 110 ? 152.673 8.196   1.667   1.00 30.85 ? 109 ASP I OD1 1 
ATOM   8584  O  OD2 . ASP H  1 110 ? 153.420 10.067  0.831   1.00 32.51 ? 109 ASP I OD2 1 
ATOM   8585  N  N   . HIS H  1 111 ? 148.717 11.077  3.905   1.00 15.50 ? 110 HIS I N   1 
ATOM   8586  C  CA  . HIS H  1 111 ? 148.052 12.081  4.714   1.00 13.52 ? 110 HIS I CA  1 
ATOM   8587  C  C   . HIS H  1 111 ? 147.048 11.409  5.645   1.00 9.71  ? 110 HIS I C   1 
ATOM   8588  O  O   . HIS H  1 111 ? 146.045 12.008  6.067   1.00 9.51  ? 110 HIS I O   1 
ATOM   8589  C  CB  . HIS H  1 111 ? 147.333 13.059  3.795   1.00 16.60 ? 110 HIS I CB  1 
ATOM   8590  C  CG  . HIS H  1 111 ? 148.219 14.202  3.363   1.00 20.35 ? 110 HIS I CG  1 
ATOM   8591  N  ND1 . HIS H  1 111 ? 147.808 15.321  2.768   1.00 22.35 ? 110 HIS I ND1 1 
ATOM   8592  C  CD2 . HIS H  1 111 ? 149.591 14.252  3.545   1.00 20.93 ? 110 HIS I CD2 1 
ATOM   8593  C  CE1 . HIS H  1 111 ? 148.893 16.048  2.587   1.00 26.32 ? 110 HIS I CE1 1 
ATOM   8594  N  NE2 . HIS H  1 111 ? 149.958 15.400  3.054   1.00 25.39 ? 110 HIS I NE2 1 
ATOM   8595  N  N   . SER H  1 112 ? 147.373 10.144  5.871   1.00 4.25  ? 111 SER I N   1 
ATOM   8596  C  CA  . SER H  1 112 ? 146.539 9.224   6.549   1.00 3.73  ? 111 SER I CA  1 
ATOM   8597  C  C   . SER H  1 112 ? 146.657 9.501   8.022   1.00 5.36  ? 111 SER I C   1 
ATOM   8598  O  O   . SER H  1 112 ? 147.702 9.892   8.562   1.00 3.97  ? 111 SER I O   1 
ATOM   8599  C  CB  . SER H  1 112 ? 146.987 7.826   6.291   1.00 2.00  ? 111 SER I CB  1 
ATOM   8600  O  OG  . SER H  1 112 ? 145.800 7.109   6.151   1.00 3.64  ? 111 SER I OG  1 
ATOM   8601  N  N   . ILE H  1 113 ? 145.490 9.347   8.626   1.00 5.81  ? 112 ILE I N   1 
ATOM   8602  C  CA  . ILE H  1 113 ? 145.403 9.518   10.057  1.00 4.49  ? 112 ILE I CA  1 
ATOM   8603  C  C   . ILE H  1 113 ? 145.305 8.116   10.661  1.00 3.71  ? 112 ILE I C   1 
ATOM   8604  O  O   . ILE H  1 113 ? 145.190 7.954   11.880  1.00 3.45  ? 112 ILE I O   1 
ATOM   8605  C  CB  . ILE H  1 113 ? 144.181 10.413  10.377  1.00 2.00  ? 112 ILE I CB  1 
ATOM   8606  C  CG1 . ILE H  1 113 ? 142.875 9.820   9.950   1.00 2.00  ? 112 ILE I CG1 1 
ATOM   8607  C  CG2 . ILE H  1 113 ? 144.430 11.734  9.674   1.00 2.00  ? 112 ILE I CG2 1 
ATOM   8608  C  CD1 . ILE H  1 113 ? 141.714 10.658  10.466  1.00 2.44  ? 112 ILE I CD1 1 
ATOM   8609  N  N   . ILE H  1 114 ? 145.403 7.050   9.867   1.00 2.37  ? 113 ILE I N   1 
ATOM   8610  C  CA  . ILE H  1 114 ? 145.296 5.732   10.469  1.00 3.08  ? 113 ILE I CA  1 
ATOM   8611  C  C   . ILE H  1 114 ? 146.603 5.432   11.179  1.00 3.03  ? 113 ILE I C   1 
ATOM   8612  O  O   . ILE H  1 114 ? 147.690 5.648   10.645  1.00 3.34  ? 113 ILE I O   1 
ATOM   8613  C  CB  . ILE H  1 114 ? 144.922 4.759   9.333   1.00 2.00  ? 113 ILE I CB  1 
ATOM   8614  C  CG1 . ILE H  1 114 ? 143.443 5.014   9.157   1.00 2.00  ? 113 ILE I CG1 1 
ATOM   8615  C  CG2 . ILE H  1 114 ? 145.194 3.319   9.597   1.00 2.00  ? 113 ILE I CG2 1 
ATOM   8616  C  CD1 . ILE H  1 114 ? 142.731 4.236   8.098   1.00 2.00  ? 113 ILE I CD1 1 
ATOM   8617  N  N   . GLY H  1 115 ? 146.458 5.024   12.435  1.00 2.93  ? 114 GLY I N   1 
ATOM   8618  C  CA  . GLY H  1 115 ? 147.572 4.702   13.292  1.00 2.00  ? 114 GLY I CA  1 
ATOM   8619  C  C   . GLY H  1 115 ? 148.070 5.976   13.946  1.00 2.00  ? 114 GLY I C   1 
ATOM   8620  O  O   . GLY H  1 115 ? 149.215 6.044   14.390  1.00 4.68  ? 114 GLY I O   1 
ATOM   8621  N  N   . ARG H  1 116 ? 147.298 7.039   14.044  1.00 2.07  ? 115 ARG I N   1 
ATOM   8622  C  CA  . ARG H  1 116 ? 147.699 8.266   14.712  1.00 2.00  ? 115 ARG I CA  1 
ATOM   8623  C  C   . ARG H  1 116 ? 146.700 8.523   15.786  1.00 2.00  ? 115 ARG I C   1 
ATOM   8624  O  O   . ARG H  1 116 ? 145.738 7.767   15.892  1.00 2.00  ? 115 ARG I O   1 
ATOM   8625  C  CB  . ARG H  1 116 ? 147.705 9.428   13.751  1.00 2.79  ? 115 ARG I CB  1 
ATOM   8626  C  CG  . ARG H  1 116 ? 148.712 9.156   12.637  1.00 3.85  ? 115 ARG I CG  1 
ATOM   8627  C  CD  . ARG H  1 116 ? 149.112 10.450  12.003  1.00 2.00  ? 115 ARG I CD  1 
ATOM   8628  N  NE  . ARG H  1 116 ? 149.745 10.211  10.736  1.00 2.00  ? 115 ARG I NE  1 
ATOM   8629  C  CZ  . ARG H  1 116 ? 151.031 9.960   10.594  1.00 3.34  ? 115 ARG I CZ  1 
ATOM   8630  N  NH1 . ARG H  1 116 ? 151.913 9.892   11.586  1.00 9.36  ? 115 ARG I NH1 1 
ATOM   8631  N  NH2 . ARG H  1 116 ? 151.470 9.763   9.381   1.00 7.02  ? 115 ARG I NH2 1 
ATOM   8632  N  N   . THR H  1 117 ? 146.821 9.566   16.582  1.00 2.00  ? 116 THR I N   1 
ATOM   8633  C  CA  . THR H  1 117 ? 145.934 9.728   17.720  1.00 2.00  ? 116 THR I CA  1 
ATOM   8634  C  C   . THR H  1 117 ? 144.895 10.824  17.620  1.00 2.00  ? 116 THR I C   1 
ATOM   8635  O  O   . THR H  1 117 ? 145.211 11.911  17.170  1.00 2.00  ? 116 THR I O   1 
ATOM   8636  C  CB  . THR H  1 117 ? 146.813 9.920   19.013  1.00 2.54  ? 116 THR I CB  1 
ATOM   8637  O  OG1 . THR H  1 117 ? 147.537 8.724   19.220  1.00 2.00  ? 116 THR I OG1 1 
ATOM   8638  C  CG2 . THR H  1 117 ? 146.019 10.073  20.284  1.00 2.00  ? 116 THR I CG2 1 
ATOM   8639  N  N   . LEU H  1 118 ? 143.644 10.559  17.975  1.00 2.48  ? 117 LEU I N   1 
ATOM   8640  C  CA  . LEU H  1 118 ? 142.632 11.586  18.059  1.00 3.05  ? 117 LEU I CA  1 
ATOM   8641  C  C   . LEU H  1 118 ? 142.653 11.930  19.547  1.00 5.20  ? 117 LEU I C   1 
ATOM   8642  O  O   . LEU H  1 118 ? 142.694 11.043  20.395  1.00 6.35  ? 117 LEU I O   1 
ATOM   8643  C  CB  . LEU H  1 118 ? 141.282 11.071  17.687  1.00 2.00  ? 117 LEU I CB  1 
ATOM   8644  C  CG  . LEU H  1 118 ? 140.193 12.108  17.638  1.00 2.00  ? 117 LEU I CG  1 
ATOM   8645  C  CD1 . LEU H  1 118 ? 140.432 13.129  16.545  1.00 4.68  ? 117 LEU I CD1 1 
ATOM   8646  C  CD2 . LEU H  1 118 ? 138.913 11.418  17.386  1.00 2.00  ? 117 LEU I CD2 1 
ATOM   8647  N  N   . VAL H  1 119 ? 142.730 13.213  19.866  1.00 4.87  ? 118 VAL I N   1 
ATOM   8648  C  CA  . VAL H  1 119 ? 142.860 13.743  21.209  1.00 3.47  ? 118 VAL I CA  1 
ATOM   8649  C  C   . VAL H  1 119 ? 141.665 14.692  21.351  1.00 3.96  ? 118 VAL I C   1 
ATOM   8650  O  O   . VAL H  1 119 ? 141.318 15.371  20.371  1.00 2.93  ? 118 VAL I O   1 
ATOM   8651  C  CB  . VAL H  1 119 ? 144.217 14.511  21.325  1.00 2.00  ? 118 VAL I CB  1 
ATOM   8652  C  CG1 . VAL H  1 119 ? 144.317 15.308  22.601  1.00 2.00  ? 118 VAL I CG1 1 
ATOM   8653  C  CG2 . VAL H  1 119 ? 145.340 13.509  21.249  1.00 2.00  ? 118 VAL I CG2 1 
ATOM   8654  N  N   . VAL H  1 120 ? 140.927 14.664  22.486  1.00 5.46  ? 119 VAL I N   1 
ATOM   8655  C  CA  . VAL H  1 120 ? 139.937 15.684  22.781  1.00 2.49  ? 119 VAL I CA  1 
ATOM   8656  C  C   . VAL H  1 120 ? 140.601 16.351  23.973  1.00 2.00  ? 119 VAL I C   1 
ATOM   8657  O  O   . VAL H  1 120 ? 141.184 15.702  24.858  1.00 2.00  ? 119 VAL I O   1 
ATOM   8658  C  CB  . VAL H  1 120 ? 138.539 15.087  23.136  1.00 2.04  ? 119 VAL I CB  1 
ATOM   8659  C  CG1 . VAL H  1 120 ? 138.488 14.405  24.471  1.00 2.00  ? 119 VAL I CG1 1 
ATOM   8660  C  CG2 . VAL H  1 120 ? 137.549 16.246  23.091  1.00 2.00  ? 119 VAL I CG2 1 
ATOM   8661  N  N   . HIS H  1 121 ? 140.596 17.676  23.814  1.00 3.82  ? 120 HIS I N   1 
ATOM   8662  C  CA  . HIS H  1 121 ? 141.129 18.699  24.700  1.00 2.06  ? 120 HIS I CA  1 
ATOM   8663  C  C   . HIS H  1 121 ? 140.210 19.365  25.722  1.00 2.00  ? 120 HIS I C   1 
ATOM   8664  O  O   . HIS H  1 121 ? 138.987 19.467  25.619  1.00 2.00  ? 120 HIS I O   1 
ATOM   8665  C  CB  . HIS H  1 121 ? 141.750 19.774  23.842  1.00 2.00  ? 120 HIS I CB  1 
ATOM   8666  C  CG  . HIS H  1 121 ? 143.071 19.399  23.176  1.00 2.00  ? 120 HIS I CG  1 
ATOM   8667  N  ND1 . HIS H  1 121 ? 144.329 19.510  23.565  1.00 2.00  ? 120 HIS I ND1 1 
ATOM   8668  C  CD2 . HIS H  1 121 ? 143.106 18.873  21.920  1.00 2.94  ? 120 HIS I CD2 1 
ATOM   8669  C  CE1 . HIS H  1 121 ? 145.075 19.073  22.576  1.00 2.00  ? 120 HIS I CE1 1 
ATOM   8670  N  NE2 . HIS H  1 121 ? 144.333 18.689  21.571  1.00 2.00  ? 120 HIS I NE2 1 
ATOM   8671  N  N   . GLU H  1 122 ? 140.865 19.814  26.760  1.00 2.00  ? 121 GLU I N   1 
ATOM   8672  C  CA  . GLU H  1 122 ? 140.307 20.522  27.889  1.00 4.52  ? 121 GLU I CA  1 
ATOM   8673  C  C   . GLU H  1 122 ? 139.694 21.863  27.528  1.00 4.96  ? 121 GLU I C   1 
ATOM   8674  O  O   . GLU H  1 122 ? 138.573 22.180  27.946  1.00 5.81  ? 121 GLU I O   1 
ATOM   8675  C  CB  . GLU H  1 122 ? 141.414 20.725  28.881  1.00 9.62  ? 121 GLU I CB  1 
ATOM   8676  C  CG  . GLU H  1 122 ? 141.254 21.750  29.997  1.00 14.95 ? 121 GLU I CG  1 
ATOM   8677  C  CD  . GLU H  1 122 ? 142.554 22.050  30.755  1.00 20.24 ? 121 GLU I CD  1 
ATOM   8678  O  OE1 . GLU H  1 122 ? 143.623 22.245  30.157  1.00 22.54 ? 121 GLU I OE1 1 
ATOM   8679  O  OE2 . GLU H  1 122 ? 142.490 22.113  31.979  1.00 27.98 ? 121 GLU I OE2 1 
ATOM   8680  N  N   . LYS H  1 123 ? 140.408 22.668  26.779  1.00 2.87  ? 122 LYS I N   1 
ATOM   8681  C  CA  . LYS H  1 123 ? 139.859 23.947  26.438  1.00 3.82  ? 122 LYS I CA  1 
ATOM   8682  C  C   . LYS H  1 123 ? 139.404 23.925  24.996  1.00 4.99  ? 122 LYS I C   1 
ATOM   8683  O  O   . LYS H  1 123 ? 139.588 22.938  24.239  1.00 4.31  ? 122 LYS I O   1 
ATOM   8684  C  CB  . LYS H  1 123 ? 140.916 25.005  26.641  1.00 5.15  ? 122 LYS I CB  1 
ATOM   8685  C  CG  . LYS H  1 123 ? 141.292 25.144  28.094  1.00 8.45  ? 122 LYS I CG  1 
ATOM   8686  C  CD  . LYS H  1 123 ? 142.492 26.067  28.274  1.00 17.11 ? 122 LYS I CD  1 
ATOM   8687  C  CE  . LYS H  1 123 ? 142.688 26.217  29.791  1.00 23.77 ? 122 LYS I CE  1 
ATOM   8688  N  NZ  . LYS H  1 123 ? 143.813 27.072  30.182  1.00 28.08 ? 122 LYS I NZ  1 
ATOM   8689  N  N   . ALA H  1 124 ? 138.848 25.079  24.638  1.00 2.00  ? 123 ALA I N   1 
ATOM   8690  C  CA  . ALA H  1 124 ? 138.421 25.283  23.272  1.00 3.40  ? 123 ALA I CA  1 
ATOM   8691  C  C   . ALA H  1 124 ? 139.597 25.572  22.375  1.00 3.22  ? 123 ALA I C   1 
ATOM   8692  O  O   . ALA H  1 124 ? 140.462 26.347  22.754  1.00 5.60  ? 123 ALA I O   1 
ATOM   8693  C  CB  . ALA H  1 124 ? 137.476 26.458  23.168  1.00 2.89  ? 123 ALA I CB  1 
ATOM   8694  N  N   . ASP H  1 125 ? 139.719 24.972  21.198  1.00 5.51  ? 124 ASP I N   1 
ATOM   8695  C  CA  . ASP H  1 125 ? 140.770 25.315  20.248  1.00 2.83  ? 124 ASP I CA  1 
ATOM   8696  C  C   . ASP H  1 125 ? 140.398 26.739  19.813  1.00 3.79  ? 124 ASP I C   1 
ATOM   8697  O  O   . ASP H  1 125 ? 139.299 26.916  19.288  1.00 5.52  ? 124 ASP I O   1 
ATOM   8698  C  CB  . ASP H  1 125 ? 140.686 24.301  19.124  1.00 2.00  ? 124 ASP I CB  1 
ATOM   8699  C  CG  . ASP H  1 125 ? 141.557 24.454  17.899  1.00 4.72  ? 124 ASP I CG  1 
ATOM   8700  O  OD1 . ASP H  1 125 ? 142.156 25.488  17.768  1.00 7.49  ? 124 ASP I OD1 1 
ATOM   8701  O  OD2 . ASP H  1 125 ? 141.652 23.566  17.043  1.00 8.82  ? 124 ASP I OD2 1 
ATOM   8702  N  N   . ASP H  1 126 ? 141.202 27.793  20.015  1.00 3.46  ? 125 ASP I N   1 
ATOM   8703  C  CA  . ASP H  1 126 ? 140.903 29.152  19.525  1.00 5.24  ? 125 ASP I CA  1 
ATOM   8704  C  C   . ASP H  1 126 ? 141.071 29.326  17.995  1.00 4.47  ? 125 ASP I C   1 
ATOM   8705  O  O   . ASP H  1 126 ? 141.087 30.424  17.422  1.00 5.73  ? 125 ASP I O   1 
ATOM   8706  C  CB  . ASP H  1 126 ? 141.780 30.247  20.278  1.00 2.00  ? 125 ASP I CB  1 
ATOM   8707  C  CG  . ASP H  1 126 ? 143.289 30.386  20.026  1.00 2.00  ? 125 ASP I CG  1 
ATOM   8708  O  OD1 . ASP H  1 126 ? 143.742 30.288  18.896  1.00 2.00  ? 125 ASP I OD1 1 
ATOM   8709  O  OD2 . ASP H  1 126 ? 144.031 30.628  20.966  1.00 2.00  ? 125 ASP I OD2 1 
ATOM   8710  N  N   . LEU H  1 127 ? 141.330 28.209  17.330  1.00 2.00  ? 126 LEU I N   1 
ATOM   8711  C  CA  . LEU H  1 127 ? 141.327 28.072  15.890  1.00 2.57  ? 126 LEU I CA  1 
ATOM   8712  C  C   . LEU H  1 127 ? 142.354 28.905  15.199  1.00 3.74  ? 126 LEU I C   1 
ATOM   8713  O  O   . LEU H  1 127 ? 142.225 29.153  13.998  1.00 4.10  ? 126 LEU I O   1 
ATOM   8714  C  CB  . LEU H  1 127 ? 139.963 28.431  15.254  1.00 2.00  ? 126 LEU I CB  1 
ATOM   8715  C  CG  . LEU H  1 127 ? 138.669 27.699  15.579  1.00 2.00  ? 126 LEU I CG  1 
ATOM   8716  C  CD1 . LEU H  1 127 ? 137.565 28.380  14.827  1.00 2.00  ? 126 LEU I CD1 1 
ATOM   8717  C  CD2 . LEU H  1 127 ? 138.733 26.223  15.182  1.00 2.00  ? 126 LEU I CD2 1 
ATOM   8718  N  N   . GLY H  1 128 ? 143.391 29.258  15.972  1.00 5.47  ? 127 GLY I N   1 
ATOM   8719  C  CA  . GLY H  1 128 ? 144.538 29.972  15.432  1.00 4.77  ? 127 GLY I CA  1 
ATOM   8720  C  C   . GLY H  1 128 ? 144.368 31.470  15.482  1.00 6.45  ? 127 GLY I C   1 
ATOM   8721  O  O   . GLY H  1 128 ? 145.212 32.197  14.968  1.00 8.52  ? 127 GLY I O   1 
ATOM   8722  N  N   . LYS H  1 129 ? 143.371 31.999  16.201  1.00 6.29  ? 128 LYS I N   1 
ATOM   8723  C  CA  . LYS H  1 129 ? 143.098 33.425  16.210  1.00 3.28  ? 128 LYS I CA  1 
ATOM   8724  C  C   . LYS H  1 129 ? 143.396 34.152  17.510  1.00 5.42  ? 128 LYS I C   1 
ATOM   8725  O  O   . LYS H  1 129 ? 142.919 35.271  17.755  1.00 4.68  ? 128 LYS I O   1 
ATOM   8726  C  CB  . LYS H  1 129 ? 141.669 33.637  15.892  1.00 2.42  ? 128 LYS I CB  1 
ATOM   8727  C  CG  . LYS H  1 129 ? 141.252 33.081  14.565  1.00 6.75  ? 128 LYS I CG  1 
ATOM   8728  C  CD  . LYS H  1 129 ? 139.950 33.785  14.404  1.00 11.88 ? 128 LYS I CD  1 
ATOM   8729  C  CE  . LYS H  1 129 ? 138.982 33.045  13.544  1.00 15.20 ? 128 LYS I CE  1 
ATOM   8730  N  NZ  . LYS H  1 129 ? 137.764 33.798  13.753  1.00 18.56 ? 128 LYS I NZ  1 
ATOM   8731  N  N   . GLY H  1 130 ? 144.183 33.522  18.383  1.00 5.56  ? 129 GLY I N   1 
ATOM   8732  C  CA  . GLY H  1 130 ? 144.462 34.081  19.684  1.00 5.30  ? 129 GLY I CA  1 
ATOM   8733  C  C   . GLY H  1 130 ? 145.530 35.157  19.666  1.00 3.80  ? 129 GLY I C   1 
ATOM   8734  O  O   . GLY H  1 130 ? 145.747 35.794  20.692  1.00 4.60  ? 129 GLY I O   1 
ATOM   8735  N  N   . GLY H  1 131 ? 146.271 35.335  18.595  1.00 2.75  ? 130 GLY I N   1 
ATOM   8736  C  CA  . GLY H  1 131 ? 147.317 36.336  18.572  1.00 2.45  ? 130 GLY I CA  1 
ATOM   8737  C  C   . GLY H  1 131 ? 148.571 36.070  19.368  1.00 2.63  ? 130 GLY I C   1 
ATOM   8738  O  O   . GLY H  1 131 ? 149.427 36.937  19.493  1.00 5.48  ? 130 GLY I O   1 
ATOM   8739  N  N   . ASN H  1 132 ? 148.766 34.917  19.964  1.00 4.59  ? 131 ASN I N   1 
ATOM   8740  C  CA  . ASN H  1 132 ? 149.991 34.631  20.673  1.00 5.60  ? 131 ASN I CA  1 
ATOM   8741  C  C   . ASN H  1 132 ? 150.678 33.485  20.019  1.00 8.08  ? 131 ASN I C   1 
ATOM   8742  O  O   . ASN H  1 132 ? 150.005 32.782  19.272  1.00 11.59 ? 131 ASN I O   1 
ATOM   8743  C  CB  . ASN H  1 132 ? 149.745 34.262  22.108  1.00 8.31  ? 131 ASN I CB  1 
ATOM   8744  C  CG  . ASN H  1 132 ? 148.955 33.022  22.452  1.00 8.03  ? 131 ASN I CG  1 
ATOM   8745  O  OD1 . ASN H  1 132 ? 148.914 32.630  23.609  1.00 13.75 ? 131 ASN I OD1 1 
ATOM   8746  N  ND2 . ASN H  1 132 ? 148.253 32.339  21.575  1.00 8.10  ? 131 ASN I ND2 1 
ATOM   8747  N  N   . GLU H  1 133 ? 151.934 33.173  20.301  1.00 11.68 ? 132 GLU I N   1 
ATOM   8748  C  CA  . GLU H  1 133 ? 152.594 32.122  19.568  1.00 13.75 ? 132 GLU I CA  1 
ATOM   8749  C  C   . GLU H  1 133 ? 151.935 30.761  19.740  1.00 12.50 ? 132 GLU I C   1 
ATOM   8750  O  O   . GLU H  1 133 ? 151.819 30.047  18.750  1.00 12.71 ? 132 GLU I O   1 
ATOM   8751  C  CB  . GLU H  1 133 ? 154.052 32.068  19.986  1.00 19.60 ? 132 GLU I CB  1 
ATOM   8752  C  CG  . GLU H  1 133 ? 154.749 31.456  18.758  1.00 27.65 ? 132 GLU I CG  1 
ATOM   8753  C  CD  . GLU H  1 133 ? 156.240 31.163  18.907  1.00 32.43 ? 132 GLU I CD  1 
ATOM   8754  O  OE1 . GLU H  1 133 ? 156.603 30.379  19.803  1.00 34.17 ? 132 GLU I OE1 1 
ATOM   8755  O  OE2 . GLU H  1 133 ? 157.021 31.719  18.116  1.00 33.38 ? 132 GLU I OE2 1 
ATOM   8756  N  N   . GLU H  1 134 ? 151.427 30.385  20.918  1.00 11.21 ? 133 GLU I N   1 
ATOM   8757  C  CA  . GLU H  1 134 ? 150.696 29.125  21.091  1.00 10.65 ? 133 GLU I CA  1 
ATOM   8758  C  C   . GLU H  1 134 ? 149.461 28.989  20.232  1.00 10.14 ? 133 GLU I C   1 
ATOM   8759  O  O   . GLU H  1 134 ? 149.091 27.853  19.890  1.00 13.03 ? 133 GLU I O   1 
ATOM   8760  C  CB  . GLU H  1 134 ? 150.159 28.890  22.485  1.00 11.64 ? 133 GLU I CB  1 
ATOM   8761  C  CG  . GLU H  1 134 ? 151.071 28.062  23.364  1.00 16.66 ? 133 GLU I CG  1 
ATOM   8762  C  CD  . GLU H  1 134 ? 151.193 26.599  22.973  1.00 17.89 ? 133 GLU I CD  1 
ATOM   8763  O  OE1 . GLU H  1 134 ? 150.257 25.850  23.249  1.00 17.13 ? 133 GLU I OE1 1 
ATOM   8764  O  OE2 . GLU H  1 134 ? 152.231 26.200  22.428  1.00 22.97 ? 133 GLU I OE2 1 
ATOM   8765  N  N   . SER H  1 135 ? 148.791 30.076  19.850  1.00 7.49  ? 134 SER I N   1 
ATOM   8766  C  CA  . SER H  1 135 ? 147.608 29.953  19.042  1.00 6.39  ? 134 SER I CA  1 
ATOM   8767  C  C   . SER H  1 135 ? 147.959 29.286  17.728  1.00 7.98  ? 134 SER I C   1 
ATOM   8768  O  O   . SER H  1 135 ? 147.183 28.434  17.276  1.00 8.39  ? 134 SER I O   1 
ATOM   8769  C  CB  . SER H  1 135 ? 147.049 31.270  18.777  1.00 5.44  ? 134 SER I CB  1 
ATOM   8770  O  OG  . SER H  1 135 ? 145.919 31.079  17.984  1.00 2.00  ? 134 SER I OG  1 
ATOM   8771  N  N   . THR H  1 136 ? 149.122 29.579  17.144  1.00 7.13  ? 135 THR I N   1 
ATOM   8772  C  CA  . THR H  1 136 ? 149.465 28.935  15.908  1.00 5.30  ? 135 THR I CA  1 
ATOM   8773  C  C   . THR H  1 136 ? 150.104 27.598  16.087  1.00 6.52  ? 135 THR I C   1 
ATOM   8774  O  O   . THR H  1 136 ? 150.544 27.044  15.084  1.00 6.34  ? 135 THR I O   1 
ATOM   8775  C  CB  . THR H  1 136 ? 150.394 29.790  15.135  1.00 6.74  ? 135 THR I CB  1 
ATOM   8776  O  OG1 . THR H  1 136 ? 151.509 30.078  16.000  1.00 10.05 ? 135 THR I OG1 1 
ATOM   8777  C  CG2 . THR H  1 136 ? 149.640 30.968  14.544  1.00 2.89  ? 135 THR I CG2 1 
ATOM   8778  N  N   . LYS H  1 137 ? 150.243 27.078  17.302  1.00 8.16  ? 136 LYS I N   1 
ATOM   8779  C  CA  . LYS H  1 137 ? 150.812 25.758  17.512  1.00 7.40  ? 136 LYS I CA  1 
ATOM   8780  C  C   . LYS H  1 137 ? 149.701 24.827  17.915  1.00 7.06  ? 136 LYS I C   1 
ATOM   8781  O  O   . LYS H  1 137 ? 149.435 23.884  17.170  1.00 7.66  ? 136 LYS I O   1 
ATOM   8782  C  CB  . LYS H  1 137 ? 151.849 25.756  18.606  1.00 10.15 ? 136 LYS I CB  1 
ATOM   8783  C  CG  . LYS H  1 137 ? 153.152 26.332  18.086  1.00 18.77 ? 136 LYS I CG  1 
ATOM   8784  C  CD  . LYS H  1 137 ? 154.212 26.389  19.170  1.00 27.24 ? 136 LYS I CD  1 
ATOM   8785  C  CE  . LYS H  1 137 ? 154.002 27.684  19.988  1.00 34.56 ? 136 LYS I CE  1 
ATOM   8786  N  NZ  . LYS H  1 137 ? 154.653 27.701  21.297  1.00 37.51 ? 136 LYS I NZ  1 
ATOM   8787  N  N   . THR H  1 138 ? 148.997 25.074  19.020  1.00 4.98  ? 137 THR I N   1 
ATOM   8788  C  CA  . THR H  1 138 ? 147.937 24.181  19.463  1.00 4.28  ? 137 THR I CA  1 
ATOM   8789  C  C   . THR H  1 138 ? 146.563 24.817  19.462  1.00 2.00  ? 137 THR I C   1 
ATOM   8790  O  O   . THR H  1 138 ? 145.539 24.201  19.670  1.00 2.00  ? 137 THR I O   1 
ATOM   8791  C  CB  . THR H  1 138 ? 148.293 23.724  20.855  1.00 8.02  ? 137 THR I CB  1 
ATOM   8792  O  OG1 . THR H  1 138 ? 148.177 24.918  21.643  1.00 14.19 ? 137 THR I OG1 1 
ATOM   8793  C  CG2 . THR H  1 138 ? 149.708 23.156  21.012  1.00 5.65  ? 137 THR I CG2 1 
ATOM   8794  N  N   . GLY H  1 139 ? 146.496 26.112  19.278  1.00 2.57  ? 138 GLY I N   1 
ATOM   8795  C  CA  . GLY H  1 139 ? 145.245 26.817  19.303  1.00 2.00  ? 138 GLY I CA  1 
ATOM   8796  C  C   . GLY H  1 139 ? 144.886 27.084  20.741  1.00 3.69  ? 138 GLY I C   1 
ATOM   8797  O  O   . GLY H  1 139 ? 143.730 27.393  20.993  1.00 2.00  ? 138 GLY I O   1 
ATOM   8798  N  N   . ASN H  1 140 ? 145.847 26.979  21.696  1.00 5.81  ? 139 ASN I N   1 
ATOM   8799  C  CA  . ASN H  1 140 ? 145.615 27.194  23.128  1.00 5.05  ? 139 ASN I CA  1 
ATOM   8800  C  C   . ASN H  1 140 ? 144.462 26.315  23.634  1.00 4.81  ? 139 ASN I C   1 
ATOM   8801  O  O   . ASN H  1 140 ? 143.663 26.704  24.491  1.00 5.37  ? 139 ASN I O   1 
ATOM   8802  C  CB  . ASN H  1 140 ? 145.271 28.675  23.462  1.00 6.93  ? 139 ASN I CB  1 
ATOM   8803  C  CG  . ASN H  1 140 ? 146.345 29.746  23.248  1.00 11.50 ? 139 ASN I CG  1 
ATOM   8804  O  OD1 . ASN H  1 140 ? 146.447 30.329  22.167  1.00 15.14 ? 139 ASN I OD1 1 
ATOM   8805  N  ND2 . ASN H  1 140 ? 147.230 30.093  24.177  1.00 13.12 ? 139 ASN I ND2 1 
ATOM   8806  N  N   . ALA H  1 141 ? 144.446 25.080  23.126  1.00 3.21  ? 140 ALA I N   1 
ATOM   8807  C  CA  . ALA H  1 141 ? 143.444 24.071  23.390  1.00 4.56  ? 140 ALA I CA  1 
ATOM   8808  C  C   . ALA H  1 141 ? 143.560 23.392  24.748  1.00 5.09  ? 140 ALA I C   1 
ATOM   8809  O  O   . ALA H  1 141 ? 142.756 22.526  25.096  1.00 4.73  ? 140 ALA I O   1 
ATOM   8810  C  CB  . ALA H  1 141 ? 143.530 22.993  22.291  1.00 2.00  ? 140 ALA I CB  1 
ATOM   8811  N  N   . GLY H  1 142 ? 144.547 23.724  25.558  1.00 6.04  ? 141 GLY I N   1 
ATOM   8812  C  CA  . GLY H  1 142 ? 144.727 23.132  26.863  1.00 8.06  ? 141 GLY I CA  1 
ATOM   8813  C  C   . GLY H  1 142 ? 145.229 21.718  26.749  1.00 10.73 ? 141 GLY I C   1 
ATOM   8814  O  O   . GLY H  1 142 ? 145.708 21.303  25.675  1.00 13.48 ? 141 GLY I O   1 
ATOM   8815  N  N   . SER H  1 143 ? 145.089 20.960  27.839  1.00 9.68  ? 142 SER I N   1 
ATOM   8816  C  CA  . SER H  1 143 ? 145.574 19.603  27.904  1.00 7.96  ? 142 SER I CA  1 
ATOM   8817  C  C   . SER H  1 143 ? 144.685 18.605  27.198  1.00 8.44  ? 142 SER I C   1 
ATOM   8818  O  O   . SER H  1 143 ? 143.530 18.894  26.880  1.00 6.69  ? 142 SER I O   1 
ATOM   8819  C  CB  . SER H  1 143 ? 145.737 19.256  29.373  1.00 9.14  ? 142 SER I CB  1 
ATOM   8820  O  OG  . SER H  1 143 ? 144.596 19.679  30.107  1.00 16.45 ? 142 SER I OG  1 
ATOM   8821  N  N   . ARG H  1 144 ? 145.231 17.390  27.102  1.00 7.15  ? 143 ARG I N   1 
ATOM   8822  C  CA  . ARG H  1 144 ? 144.679 16.277  26.400  1.00 5.36  ? 143 ARG I CA  1 
ATOM   8823  C  C   . ARG H  1 144 ? 143.939 15.463  27.402  1.00 5.92  ? 143 ARG I C   1 
ATOM   8824  O  O   . ARG H  1 144 ? 144.610 14.879  28.245  1.00 10.08 ? 143 ARG I O   1 
ATOM   8825  C  CB  . ARG H  1 144 ? 145.822 15.466  25.796  1.00 4.75  ? 143 ARG I CB  1 
ATOM   8826  C  CG  . ARG H  1 144 ? 146.702 16.384  24.979  1.00 5.63  ? 143 ARG I CG  1 
ATOM   8827  C  CD  . ARG H  1 144 ? 147.851 15.650  24.366  1.00 6.33  ? 143 ARG I CD  1 
ATOM   8828  N  NE  . ARG H  1 144 ? 148.629 16.668  23.706  1.00 9.42  ? 143 ARG I NE  1 
ATOM   8829  C  CZ  . ARG H  1 144 ? 149.736 16.388  23.009  1.00 10.15 ? 143 ARG I CZ  1 
ATOM   8830  N  NH1 . ARG H  1 144 ? 150.163 15.124  22.925  1.00 9.22  ? 143 ARG I NH1 1 
ATOM   8831  N  NH2 . ARG H  1 144 ? 150.405 17.381  22.395  1.00 6.37  ? 143 ARG I NH2 1 
ATOM   8832  N  N   . LEU H  1 145 ? 142.632 15.323  27.334  1.00 5.38  ? 144 LEU I N   1 
ATOM   8833  C  CA  . LEU H  1 145 ? 141.897 14.575  28.321  1.00 4.58  ? 144 LEU I CA  1 
ATOM   8834  C  C   . LEU H  1 145 ? 141.768 13.098  28.013  1.00 7.05  ? 144 LEU I C   1 
ATOM   8835  O  O   . LEU H  1 145 ? 141.851 12.240  28.898  1.00 11.97 ? 144 LEU I O   1 
ATOM   8836  C  CB  . LEU H  1 145 ? 140.527 15.170  28.432  1.00 2.78  ? 144 LEU I CB  1 
ATOM   8837  C  CG  . LEU H  1 145 ? 140.318 16.587  28.843  1.00 2.00  ? 144 LEU I CG  1 
ATOM   8838  C  CD1 . LEU H  1 145 ? 138.859 16.885  28.704  1.00 2.01  ? 144 LEU I CD1 1 
ATOM   8839  C  CD2 . LEU H  1 145 ? 140.759 16.812  30.255  1.00 2.00  ? 144 LEU I CD2 1 
ATOM   8840  N  N   . ALA H  1 146 ? 141.459 12.793  26.763  1.00 6.98  ? 145 ALA I N   1 
ATOM   8841  C  CA  . ALA H  1 146 ? 141.299 11.435  26.293  1.00 3.98  ? 145 ALA I CA  1 
ATOM   8842  C  C   . ALA H  1 146 ? 141.842 11.372  24.878  1.00 4.88  ? 145 ALA I C   1 
ATOM   8843  O  O   . ALA H  1 146 ? 141.761 12.305  24.089  1.00 5.77  ? 145 ALA I O   1 
ATOM   8844  C  CB  . ALA H  1 146 ? 139.892 11.011  26.162  1.00 2.00  ? 145 ALA I CB  1 
ATOM   8845  N  N   . CYS H  1 147 ? 142.405 10.261  24.504  1.00 6.33  ? 146 CYS I N   1 
ATOM   8846  C  CA  . CYS H  1 147 ? 142.930 10.084  23.194  1.00 6.39  ? 146 CYS I CA  1 
ATOM   8847  C  C   . CYS H  1 147 ? 142.826 8.616   22.835  1.00 6.47  ? 146 CYS I C   1 
ATOM   8848  O  O   . CYS H  1 147 ? 142.388 7.781   23.635  1.00 5.80  ? 146 CYS I O   1 
ATOM   8849  C  CB  . CYS H  1 147 ? 144.341 10.587  23.210  1.00 7.63  ? 146 CYS I CB  1 
ATOM   8850  S  SG  . CYS H  1 147 ? 145.378 9.785   24.431  1.00 8.28  ? 146 CYS I SG  1 
ATOM   8851  N  N   . GLY H  1 148 ? 143.074 8.296   21.581  1.00 6.82  ? 147 GLY I N   1 
ATOM   8852  C  CA  . GLY H  1 148 ? 143.024 6.902   21.164  1.00 6.73  ? 147 GLY I CA  1 
ATOM   8853  C  C   . GLY H  1 148 ? 143.607 6.839   19.765  1.00 4.62  ? 147 GLY I C   1 
ATOM   8854  O  O   . GLY H  1 148 ? 143.604 7.854   19.064  1.00 3.72  ? 147 GLY I O   1 
ATOM   8855  N  N   . VAL H  1 149 ? 144.112 5.663   19.407  1.00 4.65  ? 148 VAL I N   1 
ATOM   8856  C  CA  . VAL H  1 149 ? 144.748 5.447   18.126  1.00 2.70  ? 148 VAL I CA  1 
ATOM   8857  C  C   . VAL H  1 149 ? 143.612 5.099   17.222  1.00 2.00  ? 148 VAL I C   1 
ATOM   8858  O  O   . VAL H  1 149 ? 142.646 4.475   17.638  1.00 2.00  ? 148 VAL I O   1 
ATOM   8859  C  CB  . VAL H  1 149 ? 145.735 4.286   18.139  1.00 2.00  ? 148 VAL I CB  1 
ATOM   8860  C  CG1 . VAL H  1 149 ? 146.613 4.454   16.946  1.00 2.00  ? 148 VAL I CG1 1 
ATOM   8861  C  CG2 . VAL H  1 149 ? 146.679 4.313   19.299  1.00 2.00  ? 148 VAL I CG2 1 
ATOM   8862  N  N   . ILE H  1 150 ? 143.731 5.554   15.996  1.00 3.38  ? 149 ILE I N   1 
ATOM   8863  C  CA  . ILE H  1 150 ? 142.710 5.377   14.974  1.00 2.71  ? 149 ILE I CA  1 
ATOM   8864  C  C   . ILE H  1 150 ? 143.143 4.155   14.253  1.00 2.00  ? 149 ILE I C   1 
ATOM   8865  O  O   . ILE H  1 150 ? 144.262 4.133   13.737  1.00 2.00  ? 149 ILE I O   1 
ATOM   8866  C  CB  . ILE H  1 150 ? 142.703 6.596   14.031  1.00 4.56  ? 149 ILE I CB  1 
ATOM   8867  C  CG1 . ILE H  1 150 ? 142.377 7.847   14.860  1.00 2.00  ? 149 ILE I CG1 1 
ATOM   8868  C  CG2 . ILE H  1 150 ? 141.776 6.319   12.851  1.00 5.21  ? 149 ILE I CG2 1 
ATOM   8869  C  CD1 . ILE H  1 150 ? 142.476 9.117   14.107  1.00 2.00  ? 149 ILE I CD1 1 
ATOM   8870  N  N   . GLY H  1 151 ? 142.274 3.164   14.254  1.00 3.50  ? 150 GLY I N   1 
ATOM   8871  C  CA  . GLY H  1 151 ? 142.548 1.878   13.654  1.00 3.40  ? 150 GLY I CA  1 
ATOM   8872  C  C   . GLY H  1 151 ? 141.507 1.569   12.606  1.00 3.71  ? 150 GLY I C   1 
ATOM   8873  O  O   . GLY H  1 151 ? 140.420 2.154   12.591  1.00 4.04  ? 150 GLY I O   1 
ATOM   8874  N  N   . ILE H  1 152 ? 141.831 0.604   11.745  1.00 3.98  ? 151 ILE I N   1 
ATOM   8875  C  CA  . ILE H  1 152 ? 141.015 0.279   10.594  1.00 3.61  ? 151 ILE I CA  1 
ATOM   8876  C  C   . ILE H  1 152 ? 139.775 -0.411  11.071  1.00 4.32  ? 151 ILE I C   1 
ATOM   8877  O  O   . ILE H  1 152 ? 139.845 -1.229  11.981  1.00 7.84  ? 151 ILE I O   1 
ATOM   8878  C  CB  . ILE H  1 152 ? 141.886 -0.596  9.652   1.00 2.79  ? 151 ILE I CB  1 
ATOM   8879  C  CG1 . ILE H  1 152 ? 142.951 0.282   9.070   1.00 2.00  ? 151 ILE I CG1 1 
ATOM   8880  C  CG2 . ILE H  1 152 ? 141.092 -1.196  8.492   1.00 2.00  ? 151 ILE I CG2 1 
ATOM   8881  C  CD1 . ILE H  1 152 ? 144.077 -0.439  8.266   1.00 8.92  ? 151 ILE I CD1 1 
ATOM   8882  N  N   . ALA H  1 153 ? 138.645 -0.098  10.485  1.00 7.41  ? 152 ALA I N   1 
ATOM   8883  C  CA  . ALA H  1 153 ? 137.386 -0.754  10.789  1.00 10.34 ? 152 ALA I CA  1 
ATOM   8884  C  C   . ALA H  1 153 ? 136.893 -1.460  9.503   1.00 15.17 ? 152 ALA I C   1 
ATOM   8885  O  O   . ALA H  1 153 ? 137.478 -1.259  8.423   1.00 15.86 ? 152 ALA I O   1 
ATOM   8886  C  CB  . ALA H  1 153 ? 136.388 0.280   11.217  1.00 8.70  ? 152 ALA I CB  1 
ATOM   8887  N  N   . GLN H  1 154 ? 135.793 -2.229  9.581   1.00 17.79 ? 153 GLN I N   1 
ATOM   8888  C  CA  . GLN H  1 154 ? 135.356 -3.037  8.472   1.00 20.87 ? 153 GLN I CA  1 
ATOM   8889  C  C   . GLN H  1 154 ? 134.351 -2.435  7.470   1.00 22.96 ? 153 GLN I C   1 
ATOM   8890  O  O   . GLN H  1 154 ? 134.629 -2.431  6.262   1.00 22.66 ? 153 GLN I O   1 
ATOM   8891  C  CB  . GLN H  1 154 ? 134.843 -4.310  9.109   1.00 20.89 ? 153 GLN I CB  1 
ATOM   8892  C  CG  . GLN H  1 154 ? 134.572 -5.450  8.126   1.00 24.10 ? 153 GLN I CG  1 
ATOM   8893  C  CD  . GLN H  1 154 ? 134.583 -6.821  8.784   1.00 26.41 ? 153 GLN I CD  1 
ATOM   8894  O  OE1 . GLN H  1 154 ? 134.522 -6.960  10.011  1.00 27.66 ? 153 GLN I OE1 1 
ATOM   8895  N  NE2 . GLN H  1 154 ? 134.698 -7.889  7.987   1.00 27.48 ? 153 GLN I NE2 1 
ATOM   8896  O  OXT . GLN H  1 154 ? 133.275 -2.012  7.892   1.00 25.38 ? 153 GLN I OXT 1 
HETATM 8897  C  C   . ACE I  1 1   ? 101.339 30.046  1.949   1.00 49.68 ? 0   ACE E C   1 
HETATM 8898  O  O   . ACE I  1 1   ? 102.263 29.498  2.562   1.00 50.76 ? 0   ACE E O   1 
HETATM 8899  C  CH3 . ACE I  1 1   ? 101.618 30.873  0.700   1.00 50.41 ? 0   ACE E CH3 1 
ATOM   8900  N  N   . ALA I  1 2   ? 100.065 29.957  2.359   1.00 48.55 ? 1   ALA E N   1 
ATOM   8901  C  CA  . ALA I  1 2   ? 99.675  29.152  3.511   1.00 44.61 ? 1   ALA E CA  1 
ATOM   8902  C  C   . ALA I  1 2   ? 98.325  28.506  3.218   1.00 41.46 ? 1   ALA E C   1 
ATOM   8903  O  O   . ALA I  1 2   ? 97.507  28.979  2.422   1.00 39.97 ? 1   ALA E O   1 
ATOM   8904  C  CB  . ALA I  1 2   ? 99.538  30.020  4.770   1.00 42.40 ? 1   ALA E CB  1 
ATOM   8905  N  N   . THR I  1 3   ? 98.193  27.331  3.798   1.00 38.85 ? 2   THR E N   1 
ATOM   8906  C  CA  . THR I  1 3   ? 96.918  26.653  3.811   1.00 37.77 ? 2   THR E CA  1 
ATOM   8907  C  C   . THR I  1 3   ? 96.339  26.899  5.194   1.00 34.72 ? 2   THR E C   1 
ATOM   8908  O  O   . THR I  1 3   ? 95.124  27.016  5.345   1.00 35.25 ? 2   THR E O   1 
ATOM   8909  C  CB  . THR I  1 3   ? 97.077  25.153  3.596   1.00 39.11 ? 2   THR E CB  1 
ATOM   8910  O  OG1 . THR I  1 3   ? 98.293  24.801  4.284   1.00 42.41 ? 2   THR E OG1 1 
ATOM   8911  C  CG2 . THR I  1 3   ? 97.031  24.765  2.122   1.00 40.00 ? 2   THR E CG2 1 
ATOM   8912  N  N   . LYS I  1 4   ? 97.183  26.948  6.229   1.00 29.37 ? 3   LYS E N   1 
ATOM   8913  C  CA  . LYS I  1 4   ? 96.707  27.237  7.544   1.00 22.60 ? 3   LYS E CA  1 
ATOM   8914  C  C   . LYS I  1 4   ? 97.424  28.483  8.004   1.00 18.64 ? 3   LYS E C   1 
ATOM   8915  O  O   . LYS I  1 4   ? 98.524  28.772  7.549   1.00 19.70 ? 3   LYS E O   1 
ATOM   8916  C  CB  . LYS I  1 4   ? 97.015  26.091  8.471   1.00 24.23 ? 3   LYS E CB  1 
ATOM   8917  C  CG  . LYS I  1 4   ? 96.208  24.798  8.344   1.00 25.99 ? 3   LYS E CG  1 
ATOM   8918  C  CD  . LYS I  1 4   ? 96.293  24.101  9.715   1.00 28.83 ? 3   LYS E CD  1 
ATOM   8919  C  CE  . LYS I  1 4   ? 95.442  22.816  9.933   1.00 33.30 ? 3   LYS E CE  1 
ATOM   8920  N  NZ  . LYS I  1 4   ? 95.492  22.330  11.317  1.00 30.58 ? 3   LYS E NZ  1 
ATOM   8921  N  N   . ALA I  1 5   ? 96.776  29.268  8.842   1.00 14.56 ? 4   ALA E N   1 
ATOM   8922  C  CA  . ALA I  1 5   ? 97.370  30.383  9.549   1.00 10.41 ? 4   ALA E CA  1 
ATOM   8923  C  C   . ALA I  1 5   ? 96.707  30.413  10.936  1.00 9.71  ? 4   ALA E C   1 
ATOM   8924  O  O   . ALA I  1 5   ? 95.663  29.774  11.119  1.00 10.91 ? 4   ALA E O   1 
ATOM   8925  C  CB  . ALA I  1 5   ? 97.084  31.686  8.832   1.00 7.56  ? 4   ALA E CB  1 
ATOM   8926  N  N   . VAL I  1 6   ? 97.246  31.073  11.960  1.00 8.68  ? 5   VAL E N   1 
ATOM   8927  C  CA  . VAL I  1 6   ? 96.626  31.167  13.288  1.00 6.06  ? 5   VAL E CA  1 
ATOM   8928  C  C   . VAL I  1 6   ? 96.888  32.599  13.692  1.00 7.67  ? 5   VAL E C   1 
ATOM   8929  O  O   . VAL I  1 6   ? 97.805  33.195  13.124  1.00 6.58  ? 5   VAL E O   1 
ATOM   8930  C  CB  . VAL I  1 6   ? 97.289  30.201  14.366  1.00 4.34  ? 5   VAL E CB  1 
ATOM   8931  C  CG1 . VAL I  1 6   ? 98.654  30.644  14.800  1.00 2.00  ? 5   VAL E CG1 1 
ATOM   8932  C  CG2 . VAL I  1 6   ? 96.465  30.188  15.635  1.00 2.87  ? 5   VAL E CG2 1 
ATOM   8933  N  N   . ALA I  1 7   ? 96.128  33.165  14.632  1.00 8.00  ? 6   ALA E N   1 
ATOM   8934  C  CA  . ALA I  1 7   ? 96.386  34.491  15.168  1.00 8.06  ? 6   ALA E CA  1 
ATOM   8935  C  C   . ALA I  1 7   ? 96.012  34.336  16.626  1.00 9.21  ? 6   ALA E C   1 
ATOM   8936  O  O   . ALA I  1 7   ? 94.909  33.852  16.916  1.00 9.28  ? 6   ALA E O   1 
ATOM   8937  C  CB  . ALA I  1 7   ? 95.469  35.557  14.598  1.00 5.18  ? 6   ALA E CB  1 
ATOM   8938  N  N   . VAL I  1 8   ? 96.946  34.582  17.552  1.00 10.64 ? 7   VAL E N   1 
ATOM   8939  C  CA  . VAL I  1 8   ? 96.613  34.614  18.965  1.00 9.14  ? 7   VAL E CA  1 
ATOM   8940  C  C   . VAL I  1 8   ? 96.109  36.029  19.190  1.00 11.80 ? 7   VAL E C   1 
ATOM   8941  O  O   . VAL I  1 8   ? 96.713  37.006  18.741  1.00 14.19 ? 7   VAL E O   1 
ATOM   8942  C  CB  . VAL I  1 8   ? 97.838  34.358  19.839  1.00 6.95  ? 7   VAL E CB  1 
ATOM   8943  C  CG1 . VAL I  1 8   ? 97.556  34.833  21.256  1.00 4.65  ? 7   VAL E CG1 1 
ATOM   8944  C  CG2 . VAL I  1 8   ? 98.098  32.871  19.993  1.00 2.00  ? 7   VAL E CG2 1 
ATOM   8945  N  N   . LEU I  1 9   ? 94.989  36.138  19.885  1.00 13.56 ? 8   LEU E N   1 
ATOM   8946  C  CA  . LEU I  1 9   ? 94.297  37.389  20.161  1.00 13.62 ? 8   LEU E CA  1 
ATOM   8947  C  C   . LEU I  1 9   ? 94.568  37.713  21.608  1.00 16.31 ? 8   LEU E C   1 
ATOM   8948  O  O   . LEU I  1 9   ? 94.429  36.857  22.506  1.00 19.30 ? 8   LEU E O   1 
ATOM   8949  C  CB  . LEU I  1 9   ? 92.796  37.219  19.945  1.00 10.51 ? 8   LEU E CB  1 
ATOM   8950  C  CG  . LEU I  1 9   ? 92.137  37.739  18.678  1.00 8.73  ? 8   LEU E CG  1 
ATOM   8951  C  CD1 . LEU I  1 9   ? 92.698  37.136  17.413  1.00 6.89  ? 8   LEU E CD1 1 
ATOM   8952  C  CD2 . LEU I  1 9   ? 90.675  37.395  18.809  1.00 6.32  ? 8   LEU E CD2 1 
ATOM   8953  N  N   . LYS I  1 10  ? 95.012  38.930  21.817  1.00 19.79 ? 9   LYS E N   1 
ATOM   8954  C  CA  . LYS I  1 10  ? 95.266  39.373  23.160  1.00 25.11 ? 9   LYS E CA  1 
ATOM   8955  C  C   . LYS I  1 10  ? 95.160  40.876  23.166  1.00 25.46 ? 9   LYS E C   1 
ATOM   8956  O  O   . LYS I  1 10  ? 95.397  41.557  22.172  1.00 23.88 ? 9   LYS E O   1 
ATOM   8957  C  CB  . LYS I  1 10  ? 96.661  38.957  23.612  1.00 29.08 ? 9   LYS E CB  1 
ATOM   8958  C  CG  . LYS I  1 10  ? 96.842  39.072  25.142  1.00 36.66 ? 9   LYS E CG  1 
ATOM   8959  C  CD  . LYS I  1 10  ? 98.355  39.224  25.389  1.00 40.49 ? 9   LYS E CD  1 
ATOM   8960  C  CE  . LYS I  1 10  ? 98.788  39.728  26.776  1.00 41.72 ? 9   LYS E CE  1 
ATOM   8961  N  NZ  . LYS I  1 10  ? 100.252 39.760  26.804  1.00 44.71 ? 9   LYS E NZ  1 
ATOM   8962  N  N   . GLY I  1 11  ? 94.696  41.363  24.293  1.00 28.70 ? 10  GLY E N   1 
ATOM   8963  C  CA  . GLY I  1 11  ? 94.614  42.787  24.507  1.00 33.21 ? 10  GLY E CA  1 
ATOM   8964  C  C   . GLY I  1 11  ? 95.052  43.104  25.934  1.00 35.79 ? 10  GLY E C   1 
ATOM   8965  O  O   . GLY I  1 11  ? 95.529  42.287  26.739  1.00 35.75 ? 10  GLY E O   1 
ATOM   8966  N  N   . ASP I  1 12  ? 94.851  44.378  26.198  1.00 39.13 ? 11  ASP E N   1 
ATOM   8967  C  CA  . ASP I  1 12  ? 95.119  44.957  27.495  1.00 41.98 ? 11  ASP E CA  1 
ATOM   8968  C  C   . ASP I  1 12  ? 93.942  44.463  28.351  1.00 42.21 ? 11  ASP E C   1 
ATOM   8969  O  O   . ASP I  1 12  ? 92.819  44.984  28.315  1.00 43.20 ? 11  ASP E O   1 
ATOM   8970  C  CB  . ASP I  1 12  ? 95.121  46.458  27.296  1.00 46.81 ? 11  ASP E CB  1 
ATOM   8971  C  CG  . ASP I  1 12  ? 95.763  47.318  28.377  1.00 52.41 ? 11  ASP E CG  1 
ATOM   8972  O  OD1 . ASP I  1 12  ? 95.405  47.184  29.561  1.00 56.17 ? 11  ASP E OD1 1 
ATOM   8973  O  OD2 . ASP I  1 12  ? 96.612  48.145  28.001  1.00 56.25 ? 11  ASP E OD2 1 
ATOM   8974  N  N   . GLY I  1 13  ? 94.129  43.367  29.080  1.00 41.05 ? 12  GLY E N   1 
ATOM   8975  C  CA  . GLY I  1 13  ? 93.016  42.876  29.883  1.00 37.93 ? 12  GLY E CA  1 
ATOM   8976  C  C   . GLY I  1 13  ? 92.353  41.619  29.300  1.00 34.45 ? 12  GLY E C   1 
ATOM   8977  O  O   . GLY I  1 13  ? 93.020  40.778  28.686  1.00 37.07 ? 12  GLY E O   1 
ATOM   8978  N  N   . PRO I  1 14  ? 91.049  41.469  29.523  1.00 30.49 ? 13  PRO E N   1 
ATOM   8979  C  CA  . PRO I  1 14  ? 90.357  40.188  29.617  1.00 26.39 ? 13  PRO E CA  1 
ATOM   8980  C  C   . PRO I  1 14  ? 90.334  39.321  28.359  1.00 23.90 ? 13  PRO E C   1 
ATOM   8981  O  O   . PRO I  1 14  ? 90.586  38.115  28.373  1.00 21.73 ? 13  PRO E O   1 
ATOM   8982  C  CB  . PRO I  1 14  ? 88.971  40.574  30.083  1.00 26.36 ? 13  PRO E CB  1 
ATOM   8983  C  CG  . PRO I  1 14  ? 89.063  42.023  30.563  1.00 27.35 ? 13  PRO E CG  1 
ATOM   8984  C  CD  . PRO I  1 14  ? 90.105  42.585  29.602  1.00 30.10 ? 13  PRO E CD  1 
ATOM   8985  N  N   . VAL I  1 15  ? 90.045  39.999  27.256  1.00 22.49 ? 14  VAL E N   1 
ATOM   8986  C  CA  . VAL I  1 15  ? 89.862  39.393  25.955  1.00 21.23 ? 14  VAL E CA  1 
ATOM   8987  C  C   . VAL I  1 15  ? 91.106  38.725  25.404  1.00 20.61 ? 14  VAL E C   1 
ATOM   8988  O  O   . VAL I  1 15  ? 92.168  39.330  25.168  1.00 19.35 ? 14  VAL E O   1 
ATOM   8989  C  CB  . VAL I  1 15  ? 89.386  40.469  24.986  1.00 21.29 ? 14  VAL E CB  1 
ATOM   8990  C  CG1 . VAL I  1 15  ? 88.912  39.813  23.727  1.00 20.41 ? 14  VAL E CG1 1 
ATOM   8991  C  CG2 . VAL I  1 15  ? 88.230  41.267  25.589  1.00 23.74 ? 14  VAL E CG2 1 
ATOM   8992  N  N   . GLN I  1 16  ? 90.896  37.431  25.200  1.00 19.92 ? 15  GLN E N   1 
ATOM   8993  C  CA  . GLN I  1 16  ? 91.935  36.603  24.644  1.00 22.61 ? 15  GLN E CA  1 
ATOM   8994  C  C   . GLN I  1 16  ? 91.317  35.440  23.872  1.00 22.05 ? 15  GLN E C   1 
ATOM   8995  O  O   . GLN I  1 16  ? 90.182  35.051  24.176  1.00 24.13 ? 15  GLN E O   1 
ATOM   8996  C  CB  . GLN I  1 16  ? 92.831  36.074  25.755  1.00 26.24 ? 15  GLN E CB  1 
ATOM   8997  C  CG  . GLN I  1 16  ? 92.112  35.321  26.885  1.00 34.81 ? 15  GLN E CG  1 
ATOM   8998  C  CD  . GLN I  1 16  ? 92.943  34.169  27.471  1.00 38.96 ? 15  GLN E CD  1 
ATOM   8999  O  OE1 . GLN I  1 16  ? 92.544  32.992  27.606  1.00 38.86 ? 15  GLN E OE1 1 
ATOM   9000  N  NE2 . GLN I  1 16  ? 94.182  34.530  27.808  1.00 41.07 ? 15  GLN E NE2 1 
ATOM   9001  N  N   . GLY I  1 17  ? 91.998  34.892  22.861  1.00 19.84 ? 16  GLY E N   1 
ATOM   9002  C  CA  . GLY I  1 17  ? 91.483  33.764  22.107  1.00 18.99 ? 16  GLY E CA  1 
ATOM   9003  C  C   . GLY I  1 17  ? 92.430  33.364  20.978  1.00 19.24 ? 16  GLY E C   1 
ATOM   9004  O  O   . GLY I  1 17  ? 93.368  34.109  20.669  1.00 19.91 ? 16  GLY E O   1 
ATOM   9005  N  N   . ILE I  1 18  ? 92.261  32.203  20.339  1.00 17.34 ? 17  ILE E N   1 
ATOM   9006  C  CA  . ILE I  1 18  ? 93.125  31.791  19.237  1.00 14.41 ? 17  ILE E CA  1 
ATOM   9007  C  C   . ILE I  1 18  ? 92.164  31.664  18.075  1.00 13.61 ? 17  ILE E C   1 
ATOM   9008  O  O   . ILE I  1 18  ? 91.153  30.976  18.222  1.00 16.95 ? 17  ILE E O   1 
ATOM   9009  C  CB  . ILE I  1 18  ? 93.757  30.475  19.646  1.00 12.69 ? 17  ILE E CB  1 
ATOM   9010  C  CG1 . ILE I  1 18  ? 94.768  30.758  20.773  1.00 13.76 ? 17  ILE E CG1 1 
ATOM   9011  C  CG2 . ILE I  1 18  ? 94.368  29.791  18.449  1.00 10.75 ? 17  ILE E CG2 1 
ATOM   9012  C  CD1 . ILE I  1 18  ? 95.190  29.490  21.550  1.00 13.39 ? 17  ILE E CD1 1 
ATOM   9013  N  N   . ILE I  1 19  ? 92.336  32.356  16.974  1.00 11.98 ? 18  ILE E N   1 
ATOM   9014  C  CA  . ILE I  1 19  ? 91.458  32.175  15.840  1.00 12.19 ? 18  ILE E CA  1 
ATOM   9015  C  C   . ILE I  1 19  ? 92.330  31.373  14.918  1.00 12.60 ? 18  ILE E C   1 
ATOM   9016  O  O   . ILE I  1 19  ? 93.554  31.559  14.874  1.00 16.53 ? 18  ILE E O   1 
ATOM   9017  C  CB  . ILE I  1 19  ? 91.114  33.527  15.225  1.00 13.36 ? 18  ILE E CB  1 
ATOM   9018  C  CG1 . ILE I  1 19  ? 90.372  34.338  16.272  1.00 13.02 ? 18  ILE E CG1 1 
ATOM   9019  C  CG2 . ILE I  1 19  ? 90.311  33.364  13.926  1.00 14.14 ? 18  ILE E CG2 1 
ATOM   9020  C  CD1 . ILE I  1 19  ? 89.133  33.670  16.873  1.00 14.06 ? 18  ILE E CD1 1 
ATOM   9021  N  N   . ASN I  1 20  ? 91.726  30.476  14.187  1.00 12.50 ? 19  ASN E N   1 
ATOM   9022  C  CA  . ASN I  1 20  ? 92.420  29.667  13.204  1.00 13.47 ? 19  ASN E CA  1 
ATOM   9023  C  C   . ASN I  1 20  ? 91.931  30.000  11.805  1.00 11.82 ? 19  ASN E C   1 
ATOM   9024  O  O   . ASN I  1 20  ? 90.813  30.526  11.664  1.00 12.89 ? 19  ASN E O   1 
ATOM   9025  C  CB  . ASN I  1 20  ? 92.166  28.240  13.515  1.00 15.77 ? 19  ASN E CB  1 
ATOM   9026  C  CG  . ASN I  1 20  ? 92.714  27.895  14.880  1.00 19.64 ? 19  ASN E CG  1 
ATOM   9027  O  OD1 . ASN I  1 20  ? 92.120  28.140  15.936  1.00 23.40 ? 19  ASN E OD1 1 
ATOM   9028  N  ND2 . ASN I  1 20  ? 93.905  27.326  14.907  1.00 23.01 ? 19  ASN E ND2 1 
ATOM   9029  N  N   . PHE I  1 21  ? 92.722  29.771  10.749  1.00 12.41 ? 20  PHE E N   1 
ATOM   9030  C  CA  . PHE I  1 21  ? 92.323  30.089  9.361   1.00 13.29 ? 20  PHE E CA  1 
ATOM   9031  C  C   . PHE I  1 21  ? 92.738  28.966  8.444   1.00 13.63 ? 20  PHE E C   1 
ATOM   9032  O  O   . PHE I  1 21  ? 93.835  28.454  8.637   1.00 14.43 ? 20  PHE E O   1 
ATOM   9033  C  CB  . PHE I  1 21  ? 92.999  31.323  8.811   1.00 10.46 ? 20  PHE E CB  1 
ATOM   9034  C  CG  . PHE I  1 21  ? 92.745  32.618  9.581   1.00 13.60 ? 20  PHE E CG  1 
ATOM   9035  C  CD1 . PHE I  1 21  ? 93.412  32.890  10.762  1.00 12.21 ? 20  PHE E CD1 1 
ATOM   9036  C  CD2 . PHE I  1 21  ? 91.853  33.559  9.084   1.00 13.71 ? 20  PHE E CD2 1 
ATOM   9037  C  CE1 . PHE I  1 21  ? 93.200  34.096  11.413  1.00 12.09 ? 20  PHE E CE1 1 
ATOM   9038  C  CE2 . PHE I  1 21  ? 91.648  34.761  9.739   1.00 11.49 ? 20  PHE E CE2 1 
ATOM   9039  C  CZ  . PHE I  1 21  ? 92.316  35.030  10.908  1.00 13.54 ? 20  PHE E CZ  1 
ATOM   9040  N  N   . GLU I  1 22  ? 91.960  28.522  7.467   1.00 16.50 ? 21  GLU E N   1 
ATOM   9041  C  CA  . GLU I  1 22  ? 92.416  27.487  6.564   1.00 19.62 ? 21  GLU E CA  1 
ATOM   9042  C  C   . GLU I  1 22  ? 91.928  27.680  5.146   1.00 22.00 ? 21  GLU E C   1 
ATOM   9043  O  O   . GLU I  1 22  ? 90.732  27.825  4.927   1.00 24.33 ? 21  GLU E O   1 
ATOM   9044  C  CB  . GLU I  1 22  ? 91.949  26.208  7.089   1.00 19.72 ? 21  GLU E CB  1 
ATOM   9045  C  CG  . GLU I  1 22  ? 92.373  25.002  6.311   1.00 22.69 ? 21  GLU E CG  1 
ATOM   9046  C  CD  . GLU I  1 22  ? 92.096  23.808  7.203   1.00 24.62 ? 21  GLU E CD  1 
ATOM   9047  O  OE1 . GLU I  1 22  ? 90.934  23.461  7.414   1.00 26.79 ? 21  GLU E OE1 1 
ATOM   9048  O  OE2 . GLU I  1 22  ? 93.046  23.245  7.731   1.00 27.38 ? 21  GLU E OE2 1 
ATOM   9049  N  N   . GLN I  1 23  ? 92.806  27.762  4.170   1.00 24.32 ? 22  GLN E N   1 
ATOM   9050  C  CA  . GLN I  1 23  ? 92.453  27.930  2.783   1.00 28.56 ? 22  GLN E CA  1 
ATOM   9051  C  C   . GLN I  1 23  ? 92.860  26.714  1.949   1.00 31.86 ? 22  GLN E C   1 
ATOM   9052  O  O   . GLN I  1 23  ? 93.921  26.610  1.339   1.00 33.22 ? 22  GLN E O   1 
ATOM   9053  C  CB  . GLN I  1 23  ? 93.129  29.154  2.289   1.00 29.17 ? 22  GLN E CB  1 
ATOM   9054  C  CG  . GLN I  1 23  ? 92.759  29.441  0.861   1.00 30.89 ? 22  GLN E CG  1 
ATOM   9055  C  CD  . GLN I  1 23  ? 93.193  30.833  0.470   1.00 32.87 ? 22  GLN E CD  1 
ATOM   9056  O  OE1 . GLN I  1 23  ? 94.292  31.288  0.818   1.00 35.65 ? 22  GLN E OE1 1 
ATOM   9057  N  NE2 . GLN I  1 23  ? 92.292  31.546  -0.191  1.00 33.06 ? 22  GLN E NE2 1 
ATOM   9058  N  N   . LYS I  1 24  ? 91.925  25.781  1.884   1.00 34.89 ? 23  LYS E N   1 
ATOM   9059  C  CA  . LYS I  1 24  ? 92.042  24.510  1.186   1.00 36.53 ? 23  LYS E CA  1 
ATOM   9060  C  C   . LYS I  1 24  ? 92.687  24.459  -0.204  1.00 38.08 ? 23  LYS E C   1 
ATOM   9061  O  O   . LYS I  1 24  ? 93.322  23.464  -0.577  1.00 38.74 ? 23  LYS E O   1 
ATOM   9062  C  CB  . LYS I  1 24  ? 90.627  23.918  1.150   1.00 37.22 ? 23  LYS E CB  1 
ATOM   9063  C  CG  . LYS I  1 24  ? 90.121  23.613  2.571   1.00 38.97 ? 23  LYS E CG  1 
ATOM   9064  C  CD  . LYS I  1 24  ? 90.348  22.163  3.041   1.00 40.05 ? 23  LYS E CD  1 
ATOM   9065  C  CE  . LYS I  1 24  ? 91.753  21.532  2.889   1.00 41.32 ? 23  LYS E CE  1 
ATOM   9066  N  NZ  . LYS I  1 24  ? 92.768  22.179  3.707   1.00 44.58 ? 23  LYS E NZ  1 
ATOM   9067  N  N   . GLU I  1 25  ? 92.511  25.512  -0.993  1.00 38.47 ? 24  GLU E N   1 
ATOM   9068  C  CA  . GLU I  1 25  ? 93.086  25.616  -2.316  1.00 40.08 ? 24  GLU E CA  1 
ATOM   9069  C  C   . GLU I  1 25  ? 93.113  27.081  -2.575  1.00 40.59 ? 24  GLU E C   1 
ATOM   9070  O  O   . GLU I  1 25  ? 92.130  27.747  -2.272  1.00 40.65 ? 24  GLU E O   1 
ATOM   9071  C  CB  . GLU I  1 25  ? 92.231  24.951  -3.375  1.00 42.99 ? 24  GLU E CB  1 
ATOM   9072  C  CG  . GLU I  1 25  ? 90.715  25.198  -3.403  1.00 46.51 ? 24  GLU E CG  1 
ATOM   9073  C  CD  . GLU I  1 25  ? 90.034  24.161  -4.301  1.00 49.74 ? 24  GLU E CD  1 
ATOM   9074  O  OE1 . GLU I  1 25  ? 90.017  24.346  -5.531  1.00 50.73 ? 24  GLU E OE1 1 
ATOM   9075  O  OE2 . GLU I  1 25  ? 89.542  23.158  -3.757  1.00 49.92 ? 24  GLU E OE2 1 
ATOM   9076  N  N   . SER I  1 26  ? 94.199  27.569  -3.157  1.00 42.58 ? 25  SER E N   1 
ATOM   9077  C  CA  . SER I  1 26  ? 94.519  28.983  -3.423  1.00 43.70 ? 25  SER E CA  1 
ATOM   9078  C  C   . SER I  1 26  ? 93.447  30.040  -3.696  1.00 43.69 ? 25  SER E C   1 
ATOM   9079  O  O   . SER I  1 26  ? 93.558  31.237  -3.460  1.00 43.45 ? 25  SER E O   1 
ATOM   9080  C  CB  . SER I  1 26  ? 95.487  28.985  -4.590  1.00 45.27 ? 25  SER E CB  1 
ATOM   9081  O  OG  . SER I  1 26  ? 94.935  28.250  -5.700  1.00 47.09 ? 25  SER E OG  1 
ATOM   9082  N  N   . ASN I  1 27  ? 92.463  29.475  -4.368  1.00 44.89 ? 26  ASN E N   1 
ATOM   9083  C  CA  . ASN I  1 27  ? 91.317  30.126  -4.974  1.00 46.38 ? 26  ASN E CA  1 
ATOM   9084  C  C   . ASN I  1 27  ? 89.982  29.987  -4.234  1.00 45.02 ? 26  ASN E C   1 
ATOM   9085  O  O   . ASN I  1 27  ? 88.969  30.601  -4.590  1.00 44.07 ? 26  ASN E O   1 
ATOM   9086  C  CB  . ASN I  1 27  ? 91.208  29.542  -6.399  1.00 49.89 ? 26  ASN E CB  1 
ATOM   9087  C  CG  . ASN I  1 27  ? 91.059  28.006  -6.449  1.00 51.41 ? 26  ASN E CG  1 
ATOM   9088  O  OD1 . ASN I  1 27  ? 89.985  27.441  -6.244  1.00 52.91 ? 26  ASN E OD1 1 
ATOM   9089  N  ND2 . ASN I  1 27  ? 92.113  27.224  -6.682  1.00 51.83 ? 26  ASN E ND2 1 
ATOM   9090  N  N   . GLY I  1 28  ? 90.018  29.179  -3.175  1.00 43.64 ? 27  GLY E N   1 
ATOM   9091  C  CA  . GLY I  1 28  ? 88.829  28.744  -2.479  1.00 40.00 ? 27  GLY E CA  1 
ATOM   9092  C  C   . GLY I  1 28  ? 88.580  29.483  -1.182  1.00 36.59 ? 27  GLY E C   1 
ATOM   9093  O  O   . GLY I  1 28  ? 89.343  30.367  -0.776  1.00 37.49 ? 27  GLY E O   1 
ATOM   9094  N  N   . PRO I  1 29  ? 87.483  29.135  -0.507  1.00 34.66 ? 28  PRO E N   1 
ATOM   9095  C  CA  . PRO I  1 29  ? 87.173  29.608  0.844   1.00 32.45 ? 28  PRO E CA  1 
ATOM   9096  C  C   . PRO I  1 29  ? 88.192  29.403  1.954   1.00 25.70 ? 28  PRO E C   1 
ATOM   9097  O  O   . PRO I  1 29  ? 88.813  28.333  2.050   1.00 25.77 ? 28  PRO E O   1 
ATOM   9098  C  CB  . PRO I  1 29  ? 85.810  28.940  1.132   1.00 34.38 ? 28  PRO E CB  1 
ATOM   9099  C  CG  . PRO I  1 29  ? 85.704  27.754  0.187   1.00 32.15 ? 28  PRO E CG  1 
ATOM   9100  C  CD  . PRO I  1 29  ? 86.348  28.378  -1.055  1.00 34.65 ? 28  PRO E CD  1 
ATOM   9101  N  N   . VAL I  1 30  ? 88.334  30.489  2.720   1.00 20.64 ? 29  VAL E N   1 
ATOM   9102  C  CA  . VAL I  1 30  ? 89.125  30.491  3.938   1.00 18.45 ? 29  VAL E CA  1 
ATOM   9103  C  C   . VAL I  1 30  ? 88.097  30.218  5.041   1.00 17.48 ? 29  VAL E C   1 
ATOM   9104  O  O   . VAL I  1 30  ? 87.065  30.911  5.152   1.00 16.51 ? 29  VAL E O   1 
ATOM   9105  C  CB  . VAL I  1 30  ? 89.795  31.853  4.279   1.00 17.81 ? 29  VAL E CB  1 
ATOM   9106  C  CG1 . VAL I  1 30  ? 90.686  31.664  5.511   1.00 14.55 ? 29  VAL E CG1 1 
ATOM   9107  C  CG2 . VAL I  1 30  ? 90.599  32.380  3.115   1.00 16.23 ? 29  VAL E CG2 1 
ATOM   9108  N  N   . LYS I  1 31  ? 88.362  29.171  5.819   1.00 14.48 ? 30  LYS E N   1 
ATOM   9109  C  CA  . LYS I  1 31  ? 87.577  28.792  6.974   1.00 13.90 ? 30  LYS E CA  1 
ATOM   9110  C  C   . LYS I  1 31  ? 88.084  29.552  8.200   1.00 13.18 ? 30  LYS E C   1 
ATOM   9111  O  O   . LYS I  1 31  ? 89.214  29.259  8.630   1.00 14.26 ? 30  LYS E O   1 
ATOM   9112  C  CB  . LYS I  1 31  ? 87.749  27.324  7.249   1.00 15.19 ? 30  LYS E CB  1 
ATOM   9113  C  CG  . LYS I  1 31  ? 86.677  26.348  6.863   1.00 18.74 ? 30  LYS E CG  1 
ATOM   9114  C  CD  . LYS I  1 31  ? 86.991  24.945  7.473   1.00 24.45 ? 30  LYS E CD  1 
ATOM   9115  C  CE  . LYS I  1 31  ? 87.129  24.814  9.020   1.00 23.83 ? 30  LYS E CE  1 
ATOM   9116  N  NZ  . LYS I  1 31  ? 86.156  25.602  9.775   1.00 23.22 ? 30  LYS E NZ  1 
ATOM   9117  N  N   . VAL I  1 32  ? 87.421  30.514  8.805   1.00 10.41 ? 31  VAL E N   1 
ATOM   9118  C  CA  . VAL I  1 32  ? 88.007  31.045  10.009  1.00 11.89 ? 31  VAL E CA  1 
ATOM   9119  C  C   . VAL I  1 32  ? 87.154  30.551  11.154  1.00 13.65 ? 31  VAL E C   1 
ATOM   9120  O  O   . VAL I  1 32  ? 85.951  30.873  11.244  1.00 15.24 ? 31  VAL E O   1 
ATOM   9121  C  CB  . VAL I  1 32  ? 88.152  32.659  9.998   1.00 11.73 ? 31  VAL E CB  1 
ATOM   9122  C  CG1 . VAL I  1 32  ? 87.580  33.223  8.732   1.00 11.46 ? 31  VAL E CG1 1 
ATOM   9123  C  CG2 . VAL I  1 32  ? 87.509  33.325  11.197  1.00 6.80  ? 31  VAL E CG2 1 
ATOM   9124  N  N   . TRP I  1 33  ? 87.775  29.738  12.024  1.00 12.27 ? 32  TRP E N   1 
ATOM   9125  C  CA  . TRP I  1 33  ? 87.083  29.257  13.215  1.00 11.88 ? 32  TRP E CA  1 
ATOM   9126  C  C   . TRP I  1 33  ? 87.854  29.539  14.528  1.00 11.58 ? 32  TRP E C   1 
ATOM   9127  O  O   . TRP I  1 33  ? 88.914  30.156  14.466  1.00 13.98 ? 32  TRP E O   1 
ATOM   9128  C  CB  . TRP I  1 33  ? 86.803  27.761  13.024  1.00 13.00 ? 32  TRP E CB  1 
ATOM   9129  C  CG  . TRP I  1 33  ? 87.975  26.812  13.153  1.00 11.03 ? 32  TRP E CG  1 
ATOM   9130  C  CD1 . TRP I  1 33  ? 88.241  26.236  14.364  1.00 12.83 ? 32  TRP E CD1 1 
ATOM   9131  C  CD2 . TRP I  1 33  ? 88.903  26.506  12.181  1.00 10.67 ? 32  TRP E CD2 1 
ATOM   9132  N  NE1 . TRP I  1 33  ? 89.358  25.553  14.150  1.00 16.06 ? 32  TRP E NE1 1 
ATOM   9133  C  CE2 . TRP I  1 33  ? 89.781  25.685  12.871  1.00 13.68 ? 32  TRP E CE2 1 
ATOM   9134  C  CE3 . TRP I  1 33  ? 89.138  26.773  10.844  1.00 11.30 ? 32  TRP E CE3 1 
ATOM   9135  C  CZ2 . TRP I  1 33  ? 90.885  25.128  12.244  1.00 13.56 ? 32  TRP E CZ2 1 
ATOM   9136  C  CZ3 . TRP I  1 33  ? 90.266  26.232  10.229  1.00 11.05 ? 32  TRP E CZ3 1 
ATOM   9137  C  CH2 . TRP I  1 33  ? 91.132  25.415  10.912  1.00 10.99 ? 32  TRP E CH2 1 
ATOM   9138  N  N   . GLY I  1 34  ? 87.449  29.200  15.757  1.00 10.48 ? 33  GLY E N   1 
ATOM   9139  C  CA  . GLY I  1 34  ? 88.224  29.523  16.958  1.00 9.52  ? 33  GLY E CA  1 
ATOM   9140  C  C   . GLY I  1 34  ? 87.294  29.945  18.077  1.00 10.89 ? 33  GLY E C   1 
ATOM   9141  O  O   . GLY I  1 34  ? 86.084  29.730  18.017  1.00 9.13  ? 33  GLY E O   1 
ATOM   9142  N  N   . SER I  1 35  ? 87.814  30.627  19.087  1.00 13.34 ? 34  SER E N   1 
ATOM   9143  C  CA  . SER I  1 35  ? 87.076  31.054  20.278  1.00 15.70 ? 34  SER E CA  1 
ATOM   9144  C  C   . SER I  1 35  ? 87.723  32.296  20.821  1.00 15.65 ? 34  SER E C   1 
ATOM   9145  O  O   . SER I  1 35  ? 88.951  32.395  20.680  1.00 17.88 ? 34  SER E O   1 
ATOM   9146  C  CB  . SER I  1 35  ? 87.147  30.052  21.415  1.00 16.88 ? 34  SER E CB  1 
ATOM   9147  O  OG  . SER I  1 35  ? 85.818  29.759  21.848  1.00 21.87 ? 34  SER E OG  1 
ATOM   9148  N  N   . ILE I  1 36  ? 86.945  33.185  21.434  1.00 14.19 ? 35  ILE E N   1 
ATOM   9149  C  CA  . ILE I  1 36  ? 87.439  34.399  22.042  1.00 11.45 ? 35  ILE E CA  1 
ATOM   9150  C  C   . ILE I  1 36  ? 86.679  34.335  23.341  1.00 12.38 ? 35  ILE E C   1 
ATOM   9151  O  O   . ILE I  1 36  ? 85.500  33.998  23.351  1.00 12.87 ? 35  ILE E O   1 
ATOM   9152  C  CB  . ILE I  1 36  ? 87.039  35.673  21.263  1.00 10.77 ? 35  ILE E CB  1 
ATOM   9153  C  CG1 . ILE I  1 36  ? 87.571  35.640  19.837  1.00 9.93  ? 35  ILE E CG1 1 
ATOM   9154  C  CG2 . ILE I  1 36  ? 87.642  36.885  21.962  1.00 10.52 ? 35  ILE E CG2 1 
ATOM   9155  C  CD1 . ILE I  1 36  ? 87.021  36.767  18.942  1.00 6.80  ? 35  ILE E CD1 1 
ATOM   9156  N  N   . LYS I  1 37  ? 87.264  34.596  24.482  1.00 13.36 ? 36  LYS E N   1 
ATOM   9157  C  CA  . LYS I  1 37  ? 86.499  34.601  25.701  1.00 13.92 ? 36  LYS E CA  1 
ATOM   9158  C  C   . LYS I  1 37  ? 86.855  35.900  26.378  1.00 12.73 ? 36  LYS E C   1 
ATOM   9159  O  O   . LYS I  1 37  ? 87.757  36.602  25.943  1.00 12.10 ? 36  LYS E O   1 
ATOM   9160  C  CB  . LYS I  1 37  ? 86.874  33.417  26.569  1.00 16.01 ? 36  LYS E CB  1 
ATOM   9161  C  CG  . LYS I  1 37  ? 88.233  33.483  27.197  1.00 25.08 ? 36  LYS E CG  1 
ATOM   9162  C  CD  . LYS I  1 37  ? 88.076  33.150  28.697  1.00 33.18 ? 36  LYS E CD  1 
ATOM   9163  C  CE  . LYS I  1 37  ? 89.426  33.219  29.435  1.00 37.08 ? 36  LYS E CE  1 
ATOM   9164  N  NZ  . LYS I  1 37  ? 89.386  32.632  30.770  1.00 44.61 ? 36  LYS E NZ  1 
ATOM   9165  N  N   . GLY I  1 38  ? 86.141  36.196  27.459  1.00 15.58 ? 37  GLY E N   1 
ATOM   9166  C  CA  . GLY I  1 38  ? 86.302  37.407  28.236  1.00 12.98 ? 37  GLY E CA  1 
ATOM   9167  C  C   . GLY I  1 38  ? 85.573  38.562  27.562  1.00 14.54 ? 37  GLY E C   1 
ATOM   9168  O  O   . GLY I  1 38  ? 85.930  39.717  27.798  1.00 14.08 ? 37  GLY E O   1 
ATOM   9169  N  N   . LEU I  1 39  ? 84.599  38.327  26.671  1.00 14.99 ? 38  LEU E N   1 
ATOM   9170  C  CA  . LEU I  1 39  ? 83.851  39.418  26.069  1.00 14.09 ? 38  LEU E CA  1 
ATOM   9171  C  C   . LEU I  1 39  ? 82.602  39.765  26.877  1.00 16.00 ? 38  LEU E C   1 
ATOM   9172  O  O   . LEU I  1 39  ? 82.145  39.070  27.795  1.00 16.81 ? 38  LEU E O   1 
ATOM   9173  C  CB  . LEU I  1 39  ? 83.406  39.051  24.661  1.00 9.84  ? 38  LEU E CB  1 
ATOM   9174  C  CG  . LEU I  1 39  ? 84.181  39.272  23.351  1.00 8.43  ? 38  LEU E CG  1 
ATOM   9175  C  CD1 . LEU I  1 39  ? 85.401  40.102  23.539  1.00 2.00  ? 38  LEU E CD1 1 
ATOM   9176  C  CD2 . LEU I  1 39  ? 84.440  37.895  22.756  1.00 6.03  ? 38  LEU E CD2 1 
ATOM   9177  N  N   . THR I  1 40  ? 82.016  40.898  26.523  1.00 17.31 ? 39  THR E N   1 
ATOM   9178  C  CA  . THR I  1 40  ? 80.730  41.294  27.060  1.00 17.57 ? 39  THR E CA  1 
ATOM   9179  C  C   . THR I  1 40  ? 79.705  40.641  26.122  1.00 18.46 ? 39  THR E C   1 
ATOM   9180  O  O   . THR I  1 40  ? 79.930  40.609  24.899  1.00 17.07 ? 39  THR E O   1 
ATOM   9181  C  CB  . THR I  1 40  ? 80.654  42.841  27.060  1.00 15.71 ? 39  THR E CB  1 
ATOM   9182  O  OG1 . THR I  1 40  ? 81.060  43.303  25.780  1.00 17.67 ? 39  THR E OG1 1 
ATOM   9183  C  CG2 . THR I  1 40  ? 81.559  43.451  28.122  1.00 16.20 ? 39  THR E CG2 1 
ATOM   9184  N  N   . GLU I  1 41  ? 78.636  40.075  26.690  1.00 18.21 ? 40  GLU E N   1 
ATOM   9185  C  CA  . GLU I  1 41  ? 77.603  39.445  25.910  1.00 18.47 ? 40  GLU E CA  1 
ATOM   9186  C  C   . GLU I  1 41  ? 77.077  40.358  24.802  1.00 17.47 ? 40  GLU E C   1 
ATOM   9187  O  O   . GLU I  1 41  ? 76.915  41.572  24.953  1.00 17.18 ? 40  GLU E O   1 
ATOM   9188  C  CB  . GLU I  1 41  ? 76.464  39.013  26.844  1.00 22.62 ? 40  GLU E CB  1 
ATOM   9189  C  CG  . GLU I  1 41  ? 75.896  40.083  27.790  1.00 30.28 ? 40  GLU E CG  1 
ATOM   9190  C  CD  . GLU I  1 41  ? 74.549  39.772  28.476  1.00 34.05 ? 40  GLU E CD  1 
ATOM   9191  O  OE1 . GLU I  1 41  ? 74.352  38.688  29.035  1.00 35.63 ? 40  GLU E OE1 1 
ATOM   9192  O  OE2 . GLU I  1 41  ? 73.680  40.650  28.461  1.00 37.99 ? 40  GLU E OE2 1 
ATOM   9193  N  N   . GLY I  1 42  ? 76.867  39.782  23.629  1.00 16.58 ? 41  GLY E N   1 
ATOM   9194  C  CA  . GLY I  1 42  ? 76.346  40.538  22.516  1.00 14.29 ? 41  GLY E CA  1 
ATOM   9195  C  C   . GLY I  1 42  ? 77.298  40.483  21.339  1.00 12.35 ? 41  GLY E C   1 
ATOM   9196  O  O   . GLY I  1 42  ? 78.276  39.728  21.329  1.00 8.58  ? 41  GLY E O   1 
ATOM   9197  N  N   . LEU I  1 43  ? 76.934  41.298  20.353  1.00 10.88 ? 42  LEU E N   1 
ATOM   9198  C  CA  . LEU I  1 43  ? 77.615  41.364  19.075  1.00 12.35 ? 42  LEU E CA  1 
ATOM   9199  C  C   . LEU I  1 43  ? 78.929  42.123  19.142  1.00 11.23 ? 42  LEU E C   1 
ATOM   9200  O  O   . LEU I  1 43  ? 78.979  43.123  19.850  1.00 12.71 ? 42  LEU E O   1 
ATOM   9201  C  CB  . LEU I  1 43  ? 76.634  42.017  18.099  1.00 14.95 ? 42  LEU E CB  1 
ATOM   9202  C  CG  . LEU I  1 43  ? 75.818  41.189  17.105  1.00 15.91 ? 42  LEU E CG  1 
ATOM   9203  C  CD1 . LEU I  1 43  ? 74.844  40.267  17.792  1.00 18.45 ? 42  LEU E CD1 1 
ATOM   9204  C  CD2 . LEU I  1 43  ? 75.011  42.127  16.247  1.00 17.45 ? 42  LEU E CD2 1 
ATOM   9205  N  N   . HIS I  1 44  ? 79.997  41.717  18.484  1.00 11.24 ? 43  HIS E N   1 
ATOM   9206  C  CA  . HIS I  1 44  ? 81.294  42.391  18.488  1.00 11.58 ? 43  HIS E CA  1 
ATOM   9207  C  C   . HIS I  1 44  ? 81.929  42.253  17.099  1.00 12.70 ? 43  HIS E C   1 
ATOM   9208  O  O   . HIS I  1 44  ? 81.955  41.151  16.513  1.00 15.02 ? 43  HIS E O   1 
ATOM   9209  C  CB  . HIS I  1 44  ? 82.261  41.780  19.507  1.00 11.58 ? 43  HIS E CB  1 
ATOM   9210  C  CG  . HIS I  1 44  ? 81.962  42.124  20.968  1.00 12.79 ? 43  HIS E CG  1 
ATOM   9211  N  ND1 . HIS I  1 44  ? 82.372  43.160  21.701  1.00 12.31 ? 43  HIS E ND1 1 
ATOM   9212  C  CD2 . HIS I  1 44  ? 81.150  41.379  21.791  1.00 14.57 ? 43  HIS E CD2 1 
ATOM   9213  C  CE1 . HIS I  1 44  ? 81.853  43.088  22.895  1.00 10.73 ? 43  HIS E CE1 1 
ATOM   9214  N  NE2 . HIS I  1 44  ? 81.115  42.012  22.945  1.00 12.88 ? 43  HIS E NE2 1 
ATOM   9215  N  N   . GLY I  1 45  ? 82.338  43.390  16.517  1.00 10.25 ? 44  GLY E N   1 
ATOM   9216  C  CA  . GLY I  1 45  ? 82.998  43.448  15.227  1.00 8.39  ? 44  GLY E CA  1 
ATOM   9217  C  C   . GLY I  1 45  ? 84.273  42.615  15.208  1.00 8.96  ? 44  GLY E C   1 
ATOM   9218  O  O   . GLY I  1 45  ? 84.887  42.373  16.265  1.00 9.50  ? 44  GLY E O   1 
ATOM   9219  N  N   . PHE I  1 46  ? 84.701  42.180  14.023  1.00 7.57  ? 45  PHE E N   1 
ATOM   9220  C  CA  . PHE I  1 46  ? 85.855  41.309  13.944  1.00 8.77  ? 45  PHE E CA  1 
ATOM   9221  C  C   . PHE I  1 46  ? 86.412  41.720  12.609  1.00 9.67  ? 45  PHE E C   1 
ATOM   9222  O  O   . PHE I  1 46  ? 85.676  41.593  11.614  1.00 10.31 ? 45  PHE E O   1 
ATOM   9223  C  CB  . PHE I  1 46  ? 85.277  39.903  14.000  1.00 8.61  ? 45  PHE E CB  1 
ATOM   9224  C  CG  . PHE I  1 46  ? 86.133  38.639  13.958  1.00 10.08 ? 45  PHE E CG  1 
ATOM   9225  C  CD1 . PHE I  1 46  ? 86.979  38.313  14.996  1.00 10.99 ? 45  PHE E CD1 1 
ATOM   9226  C  CD2 . PHE I  1 46  ? 85.998  37.766  12.883  1.00 10.52 ? 45  PHE E CD2 1 
ATOM   9227  C  CE1 . PHE I  1 46  ? 87.664  37.118  14.973  1.00 10.37 ? 45  PHE E CE1 1 
ATOM   9228  C  CE2 . PHE I  1 46  ? 86.686  36.574  12.861  1.00 8.41  ? 45  PHE E CE2 1 
ATOM   9229  C  CZ  . PHE I  1 46  ? 87.524  36.253  13.904  1.00 11.75 ? 45  PHE E CZ  1 
ATOM   9230  N  N   . HIS I  1 47  ? 87.641  42.255  12.495  1.00 9.53  ? 46  HIS E N   1 
ATOM   9231  C  CA  . HIS I  1 47  ? 88.093  42.697  11.175  1.00 11.46 ? 46  HIS E CA  1 
ATOM   9232  C  C   . HIS I  1 47  ? 89.530  42.339  10.966  1.00 12.54 ? 46  HIS E C   1 
ATOM   9233  O  O   . HIS I  1 47  ? 90.288  42.205  11.936  1.00 11.36 ? 46  HIS E O   1 
ATOM   9234  C  CB  . HIS I  1 47  ? 87.964  44.251  10.978  1.00 12.17 ? 46  HIS E CB  1 
ATOM   9235  C  CG  . HIS I  1 47  ? 86.632  44.874  11.440  1.00 13.11 ? 46  HIS E CG  1 
ATOM   9236  N  ND1 . HIS I  1 47  ? 86.363  45.684  12.475  1.00 16.11 ? 46  HIS E ND1 1 
ATOM   9237  C  CD2 . HIS I  1 47  ? 85.418  44.620  10.828  1.00 12.97 ? 46  HIS E CD2 1 
ATOM   9238  C  CE1 . HIS I  1 47  ? 85.064  45.911  12.508  1.00 14.10 ? 46  HIS E CE1 1 
ATOM   9239  N  NE2 . HIS I  1 47  ? 84.500  45.262  11.511  1.00 13.95 ? 46  HIS E NE2 1 
ATOM   9240  N  N   . VAL I  1 48  ? 89.922  42.163  9.708   1.00 15.11 ? 47  VAL E N   1 
ATOM   9241  C  CA  . VAL I  1 48  ? 91.335  42.042  9.412   1.00 17.89 ? 47  VAL E CA  1 
ATOM   9242  C  C   . VAL I  1 48  ? 91.776  43.493  9.170   1.00 20.38 ? 47  VAL E C   1 
ATOM   9243  O  O   . VAL I  1 48  ? 91.204  44.190  8.326   1.00 22.65 ? 47  VAL E O   1 
ATOM   9244  C  CB  . VAL I  1 48  ? 91.542  41.209  8.175   1.00 17.68 ? 47  VAL E CB  1 
ATOM   9245  C  CG1 . VAL I  1 48  ? 93.021  41.276  7.820   1.00 19.11 ? 47  VAL E CG1 1 
ATOM   9246  C  CG2 . VAL I  1 48  ? 91.138  39.746  8.426   1.00 19.77 ? 47  VAL E CG2 1 
ATOM   9247  N  N   . HIS I  1 49  ? 92.696  44.053  9.933   1.00 21.36 ? 48  HIS E N   1 
ATOM   9248  C  CA  . HIS I  1 49  ? 93.170  45.405  9.737   1.00 22.78 ? 48  HIS E CA  1 
ATOM   9249  C  C   . HIS I  1 49  ? 94.491  45.255  9.016   1.00 23.95 ? 48  HIS E C   1 
ATOM   9250  O  O   . HIS I  1 49  ? 95.219  44.268  9.167   1.00 24.86 ? 48  HIS E O   1 
ATOM   9251  C  CB  . HIS I  1 49  ? 93.384  46.121  11.066  1.00 25.23 ? 48  HIS E CB  1 
ATOM   9252  C  CG  . HIS I  1 49  ? 92.106  46.564  11.803  1.00 27.48 ? 48  HIS E CG  1 
ATOM   9253  N  ND1 . HIS I  1 49  ? 91.917  47.702  12.440  1.00 25.99 ? 48  HIS E ND1 1 
ATOM   9254  C  CD2 . HIS I  1 49  ? 90.932  45.838  11.927  1.00 28.42 ? 48  HIS E CD2 1 
ATOM   9255  C  CE1 . HIS I  1 49  ? 90.697  47.674  12.927  1.00 28.54 ? 48  HIS E CE1 1 
ATOM   9256  N  NE2 . HIS I  1 49  ? 90.069  46.546  12.625  1.00 29.08 ? 48  HIS E NE2 1 
ATOM   9257  N  N   . GLU I  1 50  ? 94.817  46.244  8.205   1.00 23.77 ? 49  GLU E N   1 
ATOM   9258  C  CA  . GLU I  1 50  ? 95.951  46.164  7.321   1.00 22.96 ? 49  GLU E CA  1 
ATOM   9259  C  C   . GLU I  1 50  ? 97.374  45.999  7.842   1.00 22.31 ? 49  GLU E C   1 
ATOM   9260  O  O   . GLU I  1 50  ? 98.145  45.304  7.175   1.00 24.19 ? 49  GLU E O   1 
ATOM   9261  C  CB  . GLU I  1 50  ? 95.872  47.387  6.440   1.00 25.24 ? 49  GLU E CB  1 
ATOM   9262  C  CG  . GLU I  1 50  ? 96.897  47.388  5.311   1.00 25.32 ? 49  GLU E CG  1 
ATOM   9263  C  CD  . GLU I  1 50  ? 96.960  48.639  4.465   1.00 26.46 ? 49  GLU E CD  1 
ATOM   9264  O  OE1 . GLU I  1 50  ? 96.282  49.640  4.762   1.00 23.03 ? 49  GLU E OE1 1 
ATOM   9265  O  OE2 . GLU I  1 50  ? 97.730  48.570  3.503   1.00 26.65 ? 49  GLU E OE2 1 
ATOM   9266  N  N   . PHE I  1 51  ? 97.827  46.620  8.923   1.00 20.12 ? 50  PHE E N   1 
ATOM   9267  C  CA  . PHE I  1 51  ? 99.216  46.453  9.282   1.00 19.42 ? 50  PHE E CA  1 
ATOM   9268  C  C   . PHE I  1 51  ? 99.223  45.403  10.334  1.00 19.71 ? 50  PHE E C   1 
ATOM   9269  O  O   . PHE I  1 51  ? 98.251  45.254  11.075  1.00 21.47 ? 50  PHE E O   1 
ATOM   9270  C  CB  . PHE I  1 51  ? 99.837  47.738  9.841   1.00 20.13 ? 50  PHE E CB  1 
ATOM   9271  C  CG  . PHE I  1 51  ? 99.728  48.812  8.788   1.00 19.62 ? 50  PHE E CG  1 
ATOM   9272  C  CD1 . PHE I  1 51  ? 100.069 48.506  7.480   1.00 19.39 ? 50  PHE E CD1 1 
ATOM   9273  C  CD2 . PHE I  1 51  ? 99.174  50.022  9.121   1.00 21.85 ? 50  PHE E CD2 1 
ATOM   9274  C  CE1 . PHE I  1 51  ? 99.853  49.409  6.490   1.00 20.68 ? 50  PHE E CE1 1 
ATOM   9275  C  CE2 . PHE I  1 51  ? 98.953  50.942  8.118   1.00 24.72 ? 50  PHE E CE2 1 
ATOM   9276  C  CZ  . PHE I  1 51  ? 99.285  50.629  6.810   1.00 25.19 ? 50  PHE E CZ  1 
ATOM   9277  N  N   . GLY I  1 52  ? 100.323 44.665  10.302  1.00 18.06 ? 51  GLY E N   1 
ATOM   9278  C  CA  . GLY I  1 52  ? 100.612 43.658  11.275  1.00 15.72 ? 51  GLY E CA  1 
ATOM   9279  C  C   . GLY I  1 52  ? 101.588 44.255  12.242  1.00 15.69 ? 51  GLY E C   1 
ATOM   9280  O  O   . GLY I  1 52  ? 102.549 43.599  12.633  1.00 15.56 ? 51  GLY E O   1 
ATOM   9281  N  N   . ASP I  1 53  ? 101.314 45.483  12.666  1.00 16.07 ? 52  ASP E N   1 
ATOM   9282  C  CA  . ASP I  1 53  ? 102.183 46.257  13.523  1.00 17.13 ? 52  ASP E CA  1 
ATOM   9283  C  C   . ASP I  1 53  ? 101.517 46.310  14.878  1.00 17.76 ? 52  ASP E C   1 
ATOM   9284  O  O   . ASP I  1 53  ? 100.407 46.825  15.026  1.00 17.92 ? 52  ASP E O   1 
ATOM   9285  C  CB  . ASP I  1 53  ? 102.324 47.645  12.911  1.00 19.59 ? 52  ASP E CB  1 
ATOM   9286  C  CG  . ASP I  1 53  ? 103.322 48.639  13.512  1.00 22.66 ? 52  ASP E CG  1 
ATOM   9287  O  OD1 . ASP I  1 53  ? 103.634 48.582  14.708  1.00 18.72 ? 52  ASP E OD1 1 
ATOM   9288  O  OD2 . ASP I  1 53  ? 103.770 49.495  12.741  1.00 25.91 ? 52  ASP E OD2 1 
ATOM   9289  N  N   . ASN I  1 54  ? 102.138 45.791  15.915  1.00 18.71 ? 53  ASN E N   1 
ATOM   9290  C  CA  . ASN I  1 54  ? 101.479 45.819  17.203  1.00 18.92 ? 53  ASN E CA  1 
ATOM   9291  C  C   . ASN I  1 54  ? 102.304 46.586  18.199  1.00 21.27 ? 53  ASN E C   1 
ATOM   9292  O  O   . ASN I  1 54  ? 102.210 46.341  19.396  1.00 22.55 ? 53  ASN E O   1 
ATOM   9293  C  CB  . ASN I  1 54  ? 101.246 44.385  17.633  1.00 16.81 ? 53  ASN E CB  1 
ATOM   9294  C  CG  . ASN I  1 54  ? 99.829  43.912  17.266  1.00 19.34 ? 53  ASN E CG  1 
ATOM   9295  O  OD1 . ASN I  1 54  ? 99.265  43.220  18.099  1.00 23.53 ? 53  ASN E OD1 1 
ATOM   9296  N  ND2 . ASN I  1 54  ? 99.063  44.116  16.186  1.00 11.12 ? 53  ASN E ND2 1 
ATOM   9297  N  N   . THR I  1 55  ? 103.098 47.566  17.743  1.00 23.16 ? 54  THR E N   1 
ATOM   9298  C  CA  . THR I  1 55  ? 103.950 48.334  18.630  1.00 24.64 ? 54  THR E CA  1 
ATOM   9299  C  C   . THR I  1 55  ? 103.235 49.129  19.700  1.00 26.87 ? 54  THR E C   1 
ATOM   9300  O  O   . THR I  1 55  ? 103.692 49.245  20.844  1.00 30.37 ? 54  THR E O   1 
ATOM   9301  C  CB  . THR I  1 55  ? 104.780 49.295  17.836  1.00 23.58 ? 54  THR E CB  1 
ATOM   9302  O  OG1 . THR I  1 55  ? 103.891 50.019  16.997  1.00 25.32 ? 54  THR E OG1 1 
ATOM   9303  C  CG2 . THR I  1 55  ? 105.833 48.579  17.041  1.00 26.24 ? 54  THR E CG2 1 
ATOM   9304  N  N   . ALA I  1 56  ? 102.128 49.717  19.266  1.00 26.76 ? 55  ALA E N   1 
ATOM   9305  C  CA  . ALA I  1 56  ? 101.302 50.561  20.103  1.00 26.84 ? 55  ALA E CA  1 
ATOM   9306  C  C   . ALA I  1 56  ? 100.043 49.789  20.425  1.00 26.84 ? 55  ALA E C   1 
ATOM   9307  O  O   . ALA I  1 56  ? 98.974  50.363  20.614  1.00 29.16 ? 55  ALA E O   1 
ATOM   9308  C  CB  . ALA I  1 56  ? 100.965 51.825  19.324  1.00 25.26 ? 55  ALA E CB  1 
ATOM   9309  N  N   . GLY I  1 57  ? 100.128 48.469  20.503  1.00 26.77 ? 56  GLY E N   1 
ATOM   9310  C  CA  . GLY I  1 57  ? 98.961  47.638  20.681  1.00 25.04 ? 56  GLY E CA  1 
ATOM   9311  C  C   . GLY I  1 57  ? 98.221  47.570  19.350  1.00 25.76 ? 56  GLY E C   1 
ATOM   9312  O  O   . GLY I  1 57  ? 98.779  47.786  18.258  1.00 27.11 ? 56  GLY E O   1 
ATOM   9313  N  N   . CYS I  1 58  ? 96.916  47.368  19.487  1.00 24.39 ? 57  CYS E N   1 
ATOM   9314  C  CA  . CYS I  1 58  ? 96.035  47.185  18.360  1.00 23.11 ? 57  CYS E CA  1 
ATOM   9315  C  C   . CYS I  1 58  ? 95.915  48.412  17.488  1.00 23.38 ? 57  CYS E C   1 
ATOM   9316  O  O   . CYS I  1 58  ? 95.463  48.305  16.351  1.00 20.93 ? 57  CYS E O   1 
ATOM   9317  C  CB  . CYS I  1 58  ? 94.658  46.780  18.868  1.00 23.07 ? 57  CYS E CB  1 
ATOM   9318  S  SG  . CYS I  1 58  ? 94.676  45.225  19.801  1.00 24.85 ? 57  CYS E SG  1 
ATOM   9319  N  N   . THR I  1 59  ? 96.371  49.575  17.950  1.00 25.24 ? 58  THR E N   1 
ATOM   9320  C  CA  . THR I  1 59  ? 96.235  50.827  17.211  1.00 27.02 ? 58  THR E CA  1 
ATOM   9321  C  C   . THR I  1 59  ? 97.128  50.919  15.996  1.00 27.89 ? 58  THR E C   1 
ATOM   9322  O  O   . THR I  1 59  ? 96.742  51.466  14.954  1.00 30.02 ? 58  THR E O   1 
ATOM   9323  C  CB  . THR I  1 59  ? 96.557  52.000  18.101  1.00 27.95 ? 58  THR E CB  1 
ATOM   9324  O  OG1 . THR I  1 59  ? 96.428  51.594  19.477  1.00 30.66 ? 58  THR E OG1 1 
ATOM   9325  C  CG2 . THR I  1 59  ? 95.626  53.153  17.755  1.00 30.02 ? 58  THR E CG2 1 
ATOM   9326  N  N   . SER I  1 60  ? 98.320  50.343  16.102  1.00 27.22 ? 59  SER E N   1 
ATOM   9327  C  CA  . SER I  1 60  ? 99.222  50.358  14.977  1.00 26.05 ? 59  SER E CA  1 
ATOM   9328  C  C   . SER I  1 60  ? 98.772  49.440  13.836  1.00 26.00 ? 59  SER E C   1 
ATOM   9329  O  O   . SER I  1 60  ? 99.395  49.447  12.781  1.00 28.41 ? 59  SER E O   1 
ATOM   9330  C  CB  . SER I  1 60  ? 100.606 49.997  15.510  1.00 25.58 ? 59  SER E CB  1 
ATOM   9331  O  OG  . SER I  1 60  ? 100.668 49.664  16.900  1.00 22.21 ? 59  SER E OG  1 
ATOM   9332  N  N   . ALA I  1 61  ? 97.693  48.653  13.982  1.00 26.98 ? 60  ALA E N   1 
ATOM   9333  C  CA  . ALA I  1 61  ? 97.115  47.806  12.925  1.00 24.84 ? 60  ALA E CA  1 
ATOM   9334  C  C   . ALA I  1 61  ? 96.484  48.682  11.853  1.00 24.16 ? 60  ALA E C   1 
ATOM   9335  O  O   . ALA I  1 61  ? 96.190  48.248  10.732  1.00 24.56 ? 60  ALA E O   1 
ATOM   9336  C  CB  . ALA I  1 61  ? 96.018  46.945  13.470  1.00 24.82 ? 60  ALA E CB  1 
ATOM   9337  N  N   . GLY I  1 62  ? 96.204  49.924  12.245  1.00 21.56 ? 61  GLY E N   1 
ATOM   9338  C  CA  . GLY I  1 62  ? 95.687  50.920  11.349  1.00 21.76 ? 61  GLY E CA  1 
ATOM   9339  C  C   . GLY I  1 62  ? 94.269  50.584  10.903  1.00 22.52 ? 61  GLY E C   1 
ATOM   9340  O  O   . GLY I  1 62  ? 93.428  50.137  11.691  1.00 20.59 ? 61  GLY E O   1 
ATOM   9341  N  N   . PRO I  1 63  ? 93.950  50.781  9.629   1.00 23.22 ? 62  PRO E N   1 
ATOM   9342  C  CA  . PRO I  1 63  ? 92.606  50.637  9.078   1.00 22.48 ? 62  PRO E CA  1 
ATOM   9343  C  C   . PRO I  1 63  ? 92.223  49.212  8.717   1.00 21.90 ? 62  PRO E C   1 
ATOM   9344  O  O   . PRO I  1 63  ? 93.049  48.301  8.792   1.00 22.31 ? 62  PRO E O   1 
ATOM   9345  C  CB  . PRO I  1 63  ? 92.653  51.565  7.911   1.00 22.49 ? 62  PRO E CB  1 
ATOM   9346  C  CG  . PRO I  1 63  ? 94.016  51.251  7.344   1.00 23.52 ? 62  PRO E CG  1 
ATOM   9347  C  CD  . PRO I  1 63  ? 94.876  51.272  8.612   1.00 24.25 ? 62  PRO E CD  1 
ATOM   9348  N  N   . HIS I  1 64  ? 90.980  48.990  8.292   1.00 21.79 ? 63  HIS E N   1 
ATOM   9349  C  CA  . HIS I  1 64  ? 90.561  47.680  7.819   1.00 19.74 ? 63  HIS E CA  1 
ATOM   9350  C  C   . HIS I  1 64  ? 91.260  47.444  6.495   1.00 18.81 ? 63  HIS E C   1 
ATOM   9351  O  O   . HIS I  1 64  ? 91.386  48.353  5.676   1.00 18.88 ? 63  HIS E O   1 
ATOM   9352  C  CB  . HIS I  1 64  ? 89.058  47.613  7.606   1.00 17.92 ? 63  HIS E CB  1 
ATOM   9353  C  CG  . HIS I  1 64  ? 88.183  47.730  8.865   1.00 20.53 ? 63  HIS E CG  1 
ATOM   9354  N  ND1 . HIS I  1 64  ? 86.866  47.983  8.917   1.00 21.23 ? 63  HIS E ND1 1 
ATOM   9355  C  CD2 . HIS I  1 64  ? 88.669  47.587  10.154  1.00 22.27 ? 63  HIS E CD2 1 
ATOM   9356  C  CE1 . HIS I  1 64  ? 86.622  47.984  10.235  1.00 22.94 ? 63  HIS E CE1 1 
ATOM   9357  N  NE2 . HIS I  1 64  ? 87.683  47.738  11.017  1.00 25.71 ? 63  HIS E NE2 1 
ATOM   9358  N  N   . PHE I  1 65  ? 91.797  46.244  6.301   1.00 19.63 ? 64  PHE E N   1 
ATOM   9359  C  CA  . PHE I  1 65  ? 92.492  45.876  5.080   1.00 19.91 ? 64  PHE E CA  1 
ATOM   9360  C  C   . PHE I  1 65  ? 91.532  46.084  3.927   1.00 21.70 ? 64  PHE E C   1 
ATOM   9361  O  O   . PHE I  1 65  ? 90.537  45.373  3.750   1.00 22.64 ? 64  PHE E O   1 
ATOM   9362  C  CB  . PHE I  1 65  ? 92.943  44.400  5.158   1.00 17.06 ? 64  PHE E CB  1 
ATOM   9363  C  CG  . PHE I  1 65  ? 93.659  43.796  3.943   1.00 12.38 ? 64  PHE E CG  1 
ATOM   9364  C  CD1 . PHE I  1 65  ? 94.565  44.506  3.179   1.00 12.68 ? 64  PHE E CD1 1 
ATOM   9365  C  CD2 . PHE I  1 65  ? 93.369  42.492  3.598   1.00 12.81 ? 64  PHE E CD2 1 
ATOM   9366  C  CE1 . PHE I  1 65  ? 95.164  43.928  2.086   1.00 11.84 ? 64  PHE E CE1 1 
ATOM   9367  C  CE2 . PHE I  1 65  ? 93.971  41.910  2.500   1.00 13.06 ? 64  PHE E CE2 1 
ATOM   9368  C  CZ  . PHE I  1 65  ? 94.865  42.626  1.747   1.00 14.11 ? 64  PHE E CZ  1 
ATOM   9369  N  N   . ASN I  1 66  ? 91.850  47.107  3.147   1.00 23.77 ? 65  ASN E N   1 
ATOM   9370  C  CA  . ASN I  1 66  ? 91.002  47.418  2.015   1.00 25.66 ? 65  ASN E CA  1 
ATOM   9371  C  C   . ASN I  1 66  ? 91.797  47.503  0.699   1.00 27.13 ? 65  ASN E C   1 
ATOM   9372  O  O   . ASN I  1 66  ? 91.936  48.586  0.115   1.00 28.20 ? 65  ASN E O   1 
ATOM   9373  C  CB  . ASN I  1 66  ? 90.292  48.730  2.382   1.00 25.05 ? 65  ASN E CB  1 
ATOM   9374  C  CG  . ASN I  1 66  ? 89.184  49.127  1.421   1.00 22.29 ? 65  ASN E CG  1 
ATOM   9375  O  OD1 . ASN I  1 66  ? 88.586  48.245  0.807   1.00 20.79 ? 65  ASN E OD1 1 
ATOM   9376  N  ND2 . ASN I  1 66  ? 88.870  50.415  1.251   1.00 17.65 ? 65  ASN E ND2 1 
ATOM   9377  N  N   . PRO I  1 67  ? 92.374  46.429  0.139   1.00 28.12 ? 66  PRO E N   1 
ATOM   9378  C  CA  . PRO I  1 67  ? 93.224  46.493  -1.054  1.00 30.26 ? 66  PRO E CA  1 
ATOM   9379  C  C   . PRO I  1 67  ? 92.523  47.008  -2.298  1.00 31.75 ? 66  PRO E C   1 
ATOM   9380  O  O   . PRO I  1 67  ? 93.186  47.337  -3.267  1.00 34.89 ? 66  PRO E O   1 
ATOM   9381  C  CB  . PRO I  1 67  ? 93.745  45.070  -1.258  1.00 28.71 ? 66  PRO E CB  1 
ATOM   9382  C  CG  . PRO I  1 67  ? 92.592  44.243  -0.737  1.00 28.53 ? 66  PRO E CG  1 
ATOM   9383  C  CD  . PRO I  1 67  ? 92.119  45.045  0.495   1.00 28.99 ? 66  PRO E CD  1 
ATOM   9384  N  N   . LEU I  1 68  ? 91.191  46.995  -2.278  1.00 33.47 ? 67  LEU E N   1 
ATOM   9385  C  CA  . LEU I  1 68  ? 90.405  47.344  -3.441  1.00 33.26 ? 67  LEU E CA  1 
ATOM   9386  C  C   . LEU I  1 68  ? 89.732  48.715  -3.333  1.00 34.04 ? 67  LEU E C   1 
ATOM   9387  O  O   . LEU I  1 68  ? 89.078  49.111  -4.296  1.00 37.62 ? 67  LEU E O   1 
ATOM   9388  C  CB  . LEU I  1 68  ? 89.352  46.266  -3.626  1.00 31.80 ? 67  LEU E CB  1 
ATOM   9389  C  CG  . LEU I  1 68  ? 89.752  44.766  -3.631  1.00 32.15 ? 67  LEU E CG  1 
ATOM   9390  C  CD1 . LEU I  1 68  ? 88.477  43.923  -3.647  1.00 33.41 ? 67  LEU E CD1 1 
ATOM   9391  C  CD2 . LEU I  1 68  ? 90.635  44.423  -4.824  1.00 29.64 ? 67  LEU E CD2 1 
ATOM   9392  N  N   . SER I  1 69  ? 89.913  49.493  -2.260  1.00 32.83 ? 68  SER E N   1 
ATOM   9393  C  CA  . SER I  1 69  ? 89.185  50.742  -2.073  1.00 33.56 ? 68  SER E CA  1 
ATOM   9394  C  C   . SER I  1 69  ? 87.716  50.771  -2.457  1.00 34.03 ? 68  SER E C   1 
ATOM   9395  O  O   . SER I  1 69  ? 87.215  51.256  -3.473  1.00 35.27 ? 68  SER E O   1 
ATOM   9396  C  CB  . SER I  1 69  ? 89.914  51.839  -2.784  1.00 34.03 ? 68  SER E CB  1 
ATOM   9397  O  OG  . SER I  1 69  ? 90.887  52.283  -1.843  1.00 37.75 ? 68  SER E OG  1 
ATOM   9398  N  N   . ARG I  1 70  ? 87.065  50.085  -1.528  1.00 33.42 ? 69  ARG E N   1 
ATOM   9399  C  CA  . ARG I  1 70  ? 85.632  49.926  -1.514  1.00 30.82 ? 69  ARG E CA  1 
ATOM   9400  C  C   . ARG I  1 70  ? 85.305  50.376  -0.103  1.00 30.51 ? 69  ARG E C   1 
ATOM   9401  O  O   . ARG I  1 70  ? 86.165  50.662  0.737   1.00 29.51 ? 69  ARG E O   1 
ATOM   9402  C  CB  . ARG I  1 70  ? 85.276  48.463  -1.719  1.00 30.29 ? 69  ARG E CB  1 
ATOM   9403  C  CG  . ARG I  1 70  ? 86.086  47.898  -2.866  1.00 29.45 ? 69  ARG E CG  1 
ATOM   9404  C  CD  . ARG I  1 70  ? 85.516  48.217  -4.250  1.00 28.43 ? 69  ARG E CD  1 
ATOM   9405  N  NE  . ARG I  1 70  ? 84.449  47.263  -4.310  1.00 30.42 ? 69  ARG E NE  1 
ATOM   9406  C  CZ  . ARG I  1 70  ? 84.631  46.003  -4.729  1.00 31.23 ? 69  ARG E CZ  1 
ATOM   9407  N  NH1 . ARG I  1 70  ? 85.801  45.500  -5.140  1.00 33.32 ? 69  ARG E NH1 1 
ATOM   9408  N  NH2 . ARG I  1 70  ? 83.707  45.107  -4.402  1.00 33.30 ? 69  ARG E NH2 1 
ATOM   9409  N  N   . LYS I  1 71  ? 84.034  50.510  0.173   1.00 32.25 ? 70  LYS E N   1 
ATOM   9410  C  CA  . LYS I  1 71  ? 83.592  50.961  1.475   1.00 33.41 ? 70  LYS E CA  1 
ATOM   9411  C  C   . LYS I  1 71  ? 83.351  49.750  2.386   1.00 34.33 ? 70  LYS E C   1 
ATOM   9412  O  O   . LYS I  1 71  ? 83.543  48.565  2.023   1.00 35.02 ? 70  LYS E O   1 
ATOM   9413  C  CB  . LYS I  1 71  ? 82.305  51.761  1.293   1.00 35.84 ? 70  LYS E CB  1 
ATOM   9414  C  CG  . LYS I  1 71  ? 82.387  53.164  0.686   1.00 39.82 ? 70  LYS E CG  1 
ATOM   9415  C  CD  . LYS I  1 71  ? 82.514  54.232  1.782   1.00 42.96 ? 70  LYS E CD  1 
ATOM   9416  C  CE  . LYS I  1 71  ? 81.871  55.592  1.376   1.00 45.09 ? 70  LYS E CE  1 
ATOM   9417  N  NZ  . LYS I  1 71  ? 81.934  56.590  2.445   1.00 43.16 ? 70  LYS E NZ  1 
ATOM   9418  N  N   . HIS I  1 72  ? 82.950  50.067  3.615   1.00 31.34 ? 71  HIS E N   1 
ATOM   9419  C  CA  . HIS I  1 72  ? 82.547  49.050  4.551   1.00 28.94 ? 71  HIS E CA  1 
ATOM   9420  C  C   . HIS I  1 72  ? 81.129  48.640  4.228   1.00 29.36 ? 71  HIS E C   1 
ATOM   9421  O  O   . HIS I  1 72  ? 80.228  49.428  3.865   1.00 30.00 ? 71  HIS E O   1 
ATOM   9422  C  CB  . HIS I  1 72  ? 82.592  49.605  5.937   1.00 27.56 ? 71  HIS E CB  1 
ATOM   9423  C  CG  . HIS I  1 72  ? 82.667  48.630  7.092   1.00 26.67 ? 71  HIS E CG  1 
ATOM   9424  N  ND1 . HIS I  1 72  ? 83.598  47.720  7.369   1.00 25.15 ? 71  HIS E ND1 1 
ATOM   9425  C  CD2 . HIS I  1 72  ? 81.813  48.705  8.155   1.00 26.21 ? 71  HIS E CD2 1 
ATOM   9426  C  CE1 . HIS I  1 72  ? 83.331  47.289  8.577   1.00 27.04 ? 71  HIS E CE1 1 
ATOM   9427  N  NE2 . HIS I  1 72  ? 82.266  47.883  9.049   1.00 25.18 ? 71  HIS E NE2 1 
ATOM   9428  N  N   . GLY I  1 73  ? 81.081  47.330  4.359   1.00 28.32 ? 72  GLY E N   1 
ATOM   9429  C  CA  . GLY I  1 73  ? 79.854  46.568  4.273   1.00 26.80 ? 72  GLY E CA  1 
ATOM   9430  C  C   . GLY I  1 73  ? 80.039  45.487  5.319   1.00 24.93 ? 72  GLY E C   1 
ATOM   9431  O  O   . GLY I  1 73  ? 80.817  45.649  6.274   1.00 26.82 ? 72  GLY E O   1 
ATOM   9432  N  N   . GLY I  1 74  ? 79.409  44.350  5.138   1.00 23.61 ? 73  GLY E N   1 
ATOM   9433  C  CA  . GLY I  1 74  ? 79.588  43.235  6.033   1.00 24.07 ? 73  GLY E CA  1 
ATOM   9434  C  C   . GLY I  1 74  ? 79.826  42.038  5.122   1.00 25.23 ? 73  GLY E C   1 
ATOM   9435  O  O   . GLY I  1 74  ? 79.530  42.148  3.940   1.00 26.76 ? 73  GLY E O   1 
ATOM   9436  N  N   . PRO I  1 75  ? 80.244  40.837  5.511   1.00 25.23 ? 74  PRO E N   1 
ATOM   9437  C  CA  . PRO I  1 75  ? 80.872  39.852  4.635   1.00 26.33 ? 74  PRO E CA  1 
ATOM   9438  C  C   . PRO I  1 75  ? 80.133  39.423  3.372   1.00 27.86 ? 74  PRO E C   1 
ATOM   9439  O  O   . PRO I  1 75  ? 80.713  38.760  2.502   1.00 30.34 ? 74  PRO E O   1 
ATOM   9440  C  CB  . PRO I  1 75  ? 81.173  38.672  5.559   1.00 26.19 ? 74  PRO E CB  1 
ATOM   9441  C  CG  . PRO I  1 75  ? 80.120  38.778  6.636   1.00 24.50 ? 74  PRO E CG  1 
ATOM   9442  C  CD  . PRO I  1 75  ? 79.972  40.275  6.829   1.00 24.02 ? 74  PRO E CD  1 
ATOM   9443  N  N   . LYS I  1 76  ? 78.834  39.675  3.258   1.00 28.67 ? 75  LYS E N   1 
ATOM   9444  C  CA  . LYS I  1 76  ? 78.161  39.211  2.059   1.00 30.62 ? 75  LYS E CA  1 
ATOM   9445  C  C   . LYS I  1 76  ? 77.546  40.427  1.445   1.00 30.45 ? 75  LYS E C   1 
ATOM   9446  O  O   . LYS I  1 76  ? 76.327  40.552  1.295   1.00 33.87 ? 75  LYS E O   1 
ATOM   9447  C  CB  . LYS I  1 76  ? 77.041  38.188  2.353   1.00 31.06 ? 75  LYS E CB  1 
ATOM   9448  C  CG  . LYS I  1 76  ? 77.293  36.960  3.225   1.00 34.62 ? 75  LYS E CG  1 
ATOM   9449  C  CD  . LYS I  1 76  ? 76.595  37.068  4.588   1.00 35.23 ? 75  LYS E CD  1 
ATOM   9450  C  CE  . LYS I  1 76  ? 75.065  37.000  4.546   1.00 36.61 ? 75  LYS E CE  1 
ATOM   9451  N  NZ  . LYS I  1 76  ? 74.604  35.675  4.149   1.00 39.77 ? 75  LYS E NZ  1 
ATOM   9452  N  N   . ASP I  1 77  ? 78.350  41.457  1.310   1.00 30.97 ? 76  ASP E N   1 
ATOM   9453  C  CA  . ASP I  1 77  ? 77.948  42.658  0.624   1.00 29.41 ? 76  ASP E CA  1 
ATOM   9454  C  C   . ASP I  1 77  ? 78.979  42.638  -0.511  1.00 30.42 ? 76  ASP E C   1 
ATOM   9455  O  O   . ASP I  1 77  ? 80.045  42.017  -0.415  1.00 28.58 ? 76  ASP E O   1 
ATOM   9456  C  CB  . ASP I  1 77  ? 78.154  43.886  1.516   1.00 30.81 ? 76  ASP E CB  1 
ATOM   9457  C  CG  . ASP I  1 77  ? 77.018  44.364  2.403   1.00 32.84 ? 76  ASP E CG  1 
ATOM   9458  O  OD1 . ASP I  1 77  ? 76.251  43.583  2.973   1.00 32.19 ? 76  ASP E OD1 1 
ATOM   9459  O  OD2 . ASP I  1 77  ? 76.929  45.581  2.529   1.00 36.05 ? 76  ASP E OD2 1 
ATOM   9460  N  N   . GLU I  1 78  ? 78.753  43.234  -1.704  1.00 32.97 ? 77  GLU E N   1 
ATOM   9461  C  CA  . GLU I  1 78  ? 79.831  43.258  -2.698  1.00 34.95 ? 77  GLU E CA  1 
ATOM   9462  C  C   . GLU I  1 78  ? 80.658  44.464  -2.237  1.00 33.72 ? 77  GLU E C   1 
ATOM   9463  O  O   . GLU I  1 78  ? 81.900  44.477  -2.379  1.00 35.27 ? 77  GLU E O   1 
ATOM   9464  C  CB  . GLU I  1 78  ? 79.402  43.548  -4.134  1.00 38.96 ? 77  GLU E CB  1 
ATOM   9465  C  CG  . GLU I  1 78  ? 79.956  42.476  -5.149  1.00 46.19 ? 77  GLU E CG  1 
ATOM   9466  C  CD  . GLU I  1 78  ? 81.463  42.592  -5.557  1.00 52.76 ? 77  GLU E CD  1 
ATOM   9467  O  OE1 . GLU I  1 78  ? 82.322  42.274  -4.731  1.00 56.40 ? 77  GLU E OE1 1 
ATOM   9468  O  OE2 . GLU I  1 78  ? 81.778  42.933  -6.703  1.00 54.36 ? 77  GLU E OE2 1 
ATOM   9469  N  N   . GLU I  1 79  ? 80.018  45.556  -1.826  1.00 29.41 ? 78  GLU E N   1 
ATOM   9470  C  CA  . GLU I  1 79  ? 80.812  46.653  -1.358  1.00 27.38 ? 78  GLU E CA  1 
ATOM   9471  C  C   . GLU I  1 79  ? 81.250  46.244  0.032   1.00 24.88 ? 78  GLU E C   1 
ATOM   9472  O  O   . GLU I  1 79  ? 80.485  46.140  0.987   1.00 23.40 ? 78  GLU E O   1 
ATOM   9473  C  CB  . GLU I  1 79  ? 79.962  47.919  -1.348  1.00 29.53 ? 78  GLU E CB  1 
ATOM   9474  C  CG  . GLU I  1 79  ? 80.809  49.156  -1.036  1.00 33.33 ? 78  GLU E CG  1 
ATOM   9475  C  CD  . GLU I  1 79  ? 81.560  49.743  -2.231  1.00 36.50 ? 78  GLU E CD  1 
ATOM   9476  O  OE1 . GLU I  1 79  ? 81.954  49.009  -3.146  1.00 37.77 ? 78  GLU E OE1 1 
ATOM   9477  O  OE2 . GLU I  1 79  ? 81.764  50.959  -2.233  1.00 36.85 ? 78  GLU E OE2 1 
ATOM   9478  N  N   . ARG I  1 80  ? 82.525  45.967  0.130   1.00 25.38 ? 79  ARG E N   1 
ATOM   9479  C  CA  . ARG I  1 80  ? 83.188  45.693  1.406   1.00 24.61 ? 79  ARG E CA  1 
ATOM   9480  C  C   . ARG I  1 80  ? 84.709  45.758  1.229   1.00 23.93 ? 79  ARG E C   1 
ATOM   9481  O  O   . ARG I  1 80  ? 85.302  45.569  0.144   1.00 23.08 ? 79  ARG E O   1 
ATOM   9482  C  CB  . ARG I  1 80  ? 82.838  44.301  1.943   1.00 23.83 ? 79  ARG E CB  1 
ATOM   9483  C  CG  . ARG I  1 80  ? 83.135  43.153  0.988   1.00 24.14 ? 79  ARG E CG  1 
ATOM   9484  C  CD  . ARG I  1 80  ? 82.854  41.831  1.652   1.00 25.22 ? 79  ARG E CD  1 
ATOM   9485  N  NE  . ARG I  1 80  ? 83.748  41.614  2.784   1.00 27.36 ? 79  ARG E NE  1 
ATOM   9486  C  CZ  . ARG I  1 80  ? 84.288  40.423  3.032   1.00 25.06 ? 79  ARG E CZ  1 
ATOM   9487  N  NH1 . ARG I  1 80  ? 84.046  39.372  2.267   1.00 23.56 ? 79  ARG E NH1 1 
ATOM   9488  N  NH2 . ARG I  1 80  ? 85.034  40.271  4.109   1.00 25.33 ? 79  ARG E NH2 1 
ATOM   9489  N  N   . HIS I  1 81  ? 85.293  46.076  2.376   1.00 21.47 ? 80  HIS E N   1 
ATOM   9490  C  CA  . HIS I  1 81  ? 86.752  46.056  2.495   1.00 20.16 ? 80  HIS E CA  1 
ATOM   9491  C  C   . HIS I  1 81  ? 87.081  44.572  2.659   1.00 20.08 ? 80  HIS E C   1 
ATOM   9492  O  O   . HIS I  1 81  ? 86.347  43.855  3.364   1.00 22.55 ? 80  HIS E O   1 
ATOM   9493  C  CB  . HIS I  1 81  ? 87.247  46.719  3.736   1.00 18.18 ? 80  HIS E CB  1 
ATOM   9494  C  CG  . HIS I  1 81  ? 86.699  48.068  4.152   1.00 15.11 ? 80  HIS E CG  1 
ATOM   9495  N  ND1 . HIS I  1 81  ? 86.360  48.382  5.391   1.00 14.88 ? 80  HIS E ND1 1 
ATOM   9496  C  CD2 . HIS I  1 81  ? 86.638  49.196  3.385   1.00 13.44 ? 80  HIS E CD2 1 
ATOM   9497  C  CE1 . HIS I  1 81  ? 86.129  49.683  5.403   1.00 12.21 ? 80  HIS E CE1 1 
ATOM   9498  N  NE2 . HIS I  1 81  ? 86.297  50.153  4.195   1.00 12.69 ? 80  HIS E NE2 1 
ATOM   9499  N  N   . VAL I  1 82  ? 88.162  44.054  2.107   1.00 18.82 ? 81  VAL E N   1 
ATOM   9500  C  CA  . VAL I  1 82  ? 88.447  42.623  2.214   1.00 17.17 ? 81  VAL E CA  1 
ATOM   9501  C  C   . VAL I  1 82  ? 88.518  42.104  3.656   1.00 15.46 ? 81  VAL E C   1 
ATOM   9502  O  O   . VAL I  1 82  ? 88.133  40.983  3.952   1.00 13.54 ? 81  VAL E O   1 
ATOM   9503  C  CB  . VAL I  1 82  ? 89.766  42.386  1.420   1.00 18.44 ? 81  VAL E CB  1 
ATOM   9504  C  CG1 . VAL I  1 82  ? 90.256  40.941  1.472   1.00 17.35 ? 81  VAL E CG1 1 
ATOM   9505  C  CG2 . VAL I  1 82  ? 89.474  42.718  -0.047  1.00 18.22 ? 81  VAL E CG2 1 
ATOM   9506  N  N   . GLY I  1 83  ? 88.947  42.891  4.632   1.00 15.54 ? 82  GLY E N   1 
ATOM   9507  C  CA  . GLY I  1 83  ? 89.012  42.410  6.004   1.00 15.31 ? 82  GLY E CA  1 
ATOM   9508  C  C   . GLY I  1 83  ? 87.700  42.487  6.777   1.00 15.50 ? 82  GLY E C   1 
ATOM   9509  O  O   . GLY I  1 83  ? 87.691  42.408  8.035   1.00 12.65 ? 82  GLY E O   1 
ATOM   9510  N  N   . ASP I  1 84  ? 86.574  42.674  6.080   1.00 15.46 ? 83  ASP E N   1 
ATOM   9511  C  CA  . ASP I  1 84  ? 85.348  42.891  6.811   1.00 18.76 ? 83  ASP E CA  1 
ATOM   9512  C  C   . ASP I  1 84  ? 84.541  41.664  7.099   1.00 20.07 ? 83  ASP E C   1 
ATOM   9513  O  O   . ASP I  1 84  ? 83.580  41.336  6.426   1.00 23.84 ? 83  ASP E O   1 
ATOM   9514  C  CB  . ASP I  1 84  ? 84.516  43.918  6.064   1.00 18.63 ? 83  ASP E CB  1 
ATOM   9515  C  CG  . ASP I  1 84  ? 85.061  45.351  6.178   1.00 20.31 ? 83  ASP E CG  1 
ATOM   9516  O  OD1 . ASP I  1 84  ? 85.989  45.679  6.917   1.00 18.02 ? 83  ASP E OD1 1 
ATOM   9517  O  OD2 . ASP I  1 84  ? 84.537  46.183  5.465   1.00 24.25 ? 83  ASP E OD2 1 
ATOM   9518  N  N   . LEU I  1 85  ? 84.877  41.000  8.188   1.00 21.19 ? 84  LEU E N   1 
ATOM   9519  C  CA  . LEU I  1 85  ? 84.246  39.732  8.500   1.00 19.77 ? 84  LEU E CA  1 
ATOM   9520  C  C   . LEU I  1 85  ? 83.050  39.850  9.436   1.00 21.03 ? 84  LEU E C   1 
ATOM   9521  O  O   . LEU I  1 85  ? 82.637  38.896  10.104  1.00 22.63 ? 84  LEU E O   1 
ATOM   9522  C  CB  . LEU I  1 85  ? 85.304  38.826  9.090   1.00 18.64 ? 84  LEU E CB  1 
ATOM   9523  C  CG  . LEU I  1 85  ? 86.468  38.431  8.245   1.00 14.29 ? 84  LEU E CG  1 
ATOM   9524  C  CD1 . LEU I  1 85  ? 87.372  37.599  9.118   1.00 17.93 ? 84  LEU E CD1 1 
ATOM   9525  C  CD2 . LEU I  1 85  ? 86.032  37.619  7.042   1.00 16.28 ? 84  LEU E CD2 1 
ATOM   9526  N  N   . GLY I  1 86  ? 82.443  41.040  9.456   1.00 21.51 ? 85  GLY E N   1 
ATOM   9527  C  CA  . GLY I  1 86  ? 81.197  41.273  10.172  1.00 19.21 ? 85  GLY E CA  1 
ATOM   9528  C  C   . GLY I  1 86  ? 81.295  41.041  11.651  1.00 16.40 ? 85  GLY E C   1 
ATOM   9529  O  O   . GLY I  1 86  ? 82.336  41.377  12.194  1.00 18.98 ? 85  GLY E O   1 
ATOM   9530  N  N   . ASN I  1 87  ? 80.256  40.492  12.276  1.00 14.67 ? 86  ASN E N   1 
ATOM   9531  C  CA  . ASN I  1 87  ? 80.202  40.318  13.719  1.00 11.68 ? 86  ASN E CA  1 
ATOM   9532  C  C   . ASN I  1 87  ? 80.390  38.889  14.144  1.00 11.79 ? 86  ASN E C   1 
ATOM   9533  O  O   . ASN I  1 87  ? 80.046  37.964  13.393  1.00 7.67  ? 86  ASN E O   1 
ATOM   9534  C  CB  . ASN I  1 87  ? 78.865  40.766  14.266  1.00 11.85 ? 86  ASN E CB  1 
ATOM   9535  C  CG  . ASN I  1 87  ? 78.751  42.282  14.294  1.00 13.09 ? 86  ASN E CG  1 
ATOM   9536  O  OD1 . ASN I  1 87  ? 79.460  42.966  15.015  1.00 13.30 ? 86  ASN E OD1 1 
ATOM   9537  N  ND2 . ASN I  1 87  ? 77.903  42.930  13.527  1.00 12.62 ? 86  ASN E ND2 1 
ATOM   9538  N  N   . VAL I  1 88  ? 80.981  38.748  15.338  1.00 13.55 ? 87  VAL E N   1 
ATOM   9539  C  CA  . VAL I  1 88  ? 80.969  37.475  16.090  1.00 12.86 ? 87  VAL E CA  1 
ATOM   9540  C  C   . VAL I  1 88  ? 80.102  37.837  17.292  1.00 12.06 ? 87  VAL E C   1 
ATOM   9541  O  O   . VAL I  1 88  ? 79.927  39.035  17.569  1.00 11.80 ? 87  VAL E O   1 
ATOM   9542  C  CB  . VAL I  1 88  ? 82.350  36.991  16.636  1.00 12.04 ? 87  VAL E CB  1 
ATOM   9543  C  CG1 . VAL I  1 88  ? 83.262  36.893  15.444  1.00 12.62 ? 87  VAL E CG1 1 
ATOM   9544  C  CG2 . VAL I  1 88  ? 82.977  37.910  17.696  1.00 12.41 ? 87  VAL E CG2 1 
ATOM   9545  N  N   . THR I  1 89  ? 79.581  36.870  18.034  1.00 12.29 ? 88  THR E N   1 
ATOM   9546  C  CA  . THR I  1 89  ? 78.621  37.130  19.140  1.00 12.51 ? 88  THR E CA  1 
ATOM   9547  C  C   . THR I  1 89  ? 79.050  36.474  20.454  1.00 12.16 ? 88  THR E C   1 
ATOM   9548  O  O   . THR I  1 89  ? 79.547  35.326  20.429  1.00 15.69 ? 88  THR E O   1 
ATOM   9549  C  CB  . THR I  1 89  ? 77.234  36.589  18.678  1.00 10.69 ? 88  THR E CB  1 
ATOM   9550  O  OG1 . THR I  1 89  ? 77.007  37.230  17.416  1.00 10.45 ? 88  THR E OG1 1 
ATOM   9551  C  CG2 . THR I  1 89  ? 76.097  36.846  19.639  1.00 6.92  ? 88  THR E CG2 1 
ATOM   9552  N  N   . ALA I  1 90  ? 78.922  37.109  21.609  1.00 9.62  ? 89  ALA E N   1 
ATOM   9553  C  CA  . ALA I  1 90  ? 79.407  36.456  22.808  1.00 8.01  ? 89  ALA E CA  1 
ATOM   9554  C  C   . ALA I  1 90  ? 78.202  36.068  23.579  1.00 7.56  ? 89  ALA E C   1 
ATOM   9555  O  O   . ALA I  1 90  ? 77.300  36.880  23.748  1.00 5.96  ? 89  ALA E O   1 
ATOM   9556  C  CB  . ALA I  1 90  ? 80.228  37.353  23.714  1.00 2.07  ? 89  ALA E CB  1 
ATOM   9557  N  N   . ASP I  1 91  ? 78.139  34.812  23.996  1.00 10.47 ? 90  ASP E N   1 
ATOM   9558  C  CA  . ASP I  1 91  ? 77.079  34.429  24.893  1.00 13.32 ? 90  ASP E CA  1 
ATOM   9559  C  C   . ASP I  1 91  ? 77.118  35.221  26.194  1.00 16.36 ? 90  ASP E C   1 
ATOM   9560  O  O   . ASP I  1 91  ? 77.997  36.031  26.506  1.00 16.15 ? 90  ASP E O   1 
ATOM   9561  C  CB  . ASP I  1 91  ? 77.145  32.950  25.238  1.00 12.64 ? 90  ASP E CB  1 
ATOM   9562  C  CG  . ASP I  1 91  ? 78.485  32.343  25.607  1.00 13.63 ? 90  ASP E CG  1 
ATOM   9563  O  OD1 . ASP I  1 91  ? 79.279  32.998  26.260  1.00 17.12 ? 90  ASP E OD1 1 
ATOM   9564  O  OD2 . ASP I  1 91  ? 78.747  31.205  25.217  1.00 13.97 ? 90  ASP E OD2 1 
ATOM   9565  N  N   . LYS I  1 92  ? 76.139  34.961  27.022  1.00 20.20 ? 91  LYS E N   1 
ATOM   9566  C  CA  . LYS I  1 92  ? 76.093  35.556  28.338  1.00 23.01 ? 91  LYS E CA  1 
ATOM   9567  C  C   . LYS I  1 92  ? 77.386  35.322  29.136  1.00 22.19 ? 91  LYS E C   1 
ATOM   9568  O  O   . LYS I  1 92  ? 77.725  36.117  30.003  1.00 25.81 ? 91  LYS E O   1 
ATOM   9569  C  CB  . LYS I  1 92  ? 74.820  34.972  28.980  1.00 26.64 ? 91  LYS E CB  1 
ATOM   9570  C  CG  . LYS I  1 92  ? 74.790  33.455  28.826  1.00 30.18 ? 91  LYS E CG  1 
ATOM   9571  C  CD  . LYS I  1 92  ? 73.507  32.848  29.297  1.00 38.19 ? 91  LYS E CD  1 
ATOM   9572  C  CE  . LYS I  1 92  ? 73.793  31.354  29.423  1.00 43.45 ? 91  LYS E CE  1 
ATOM   9573  N  NZ  . LYS I  1 92  ? 72.708  30.672  30.127  1.00 50.88 ? 91  LYS E NZ  1 
ATOM   9574  N  N   . ASP I  1 93  ? 78.193  34.295  28.879  1.00 20.02 ? 92  ASP E N   1 
ATOM   9575  C  CA  . ASP I  1 93  ? 79.456  34.083  29.587  1.00 18.03 ? 92  ASP E CA  1 
ATOM   9576  C  C   . ASP I  1 93  ? 80.654  34.750  28.932  1.00 16.10 ? 92  ASP E C   1 
ATOM   9577  O  O   . ASP I  1 93  ? 81.806  34.511  29.290  1.00 15.55 ? 92  ASP E O   1 
ATOM   9578  C  CB  . ASP I  1 93  ? 79.765  32.581  29.718  1.00 20.89 ? 92  ASP E CB  1 
ATOM   9579  C  CG  . ASP I  1 93  ? 78.854  31.810  30.672  1.00 24.97 ? 92  ASP E CG  1 
ATOM   9580  O  OD1 . ASP I  1 93  ? 78.297  32.420  31.597  1.00 31.83 ? 92  ASP E OD1 1 
ATOM   9581  O  OD2 . ASP I  1 93  ? 78.717  30.594  30.518  1.00 23.63 ? 92  ASP E OD2 1 
ATOM   9582  N  N   . GLY I  1 94  ? 80.460  35.551  27.916  1.00 13.43 ? 93  GLY E N   1 
ATOM   9583  C  CA  . GLY I  1 94  ? 81.575  36.228  27.320  1.00 13.56 ? 93  GLY E CA  1 
ATOM   9584  C  C   . GLY I  1 94  ? 82.242  35.444  26.208  1.00 14.24 ? 93  GLY E C   1 
ATOM   9585  O  O   . GLY I  1 94  ? 83.102  35.995  25.511  1.00 17.38 ? 93  GLY E O   1 
ATOM   9586  N  N   . VAL I  1 95  ? 81.929  34.181  25.996  1.00 10.78 ? 94  VAL E N   1 
ATOM   9587  C  CA  . VAL I  1 95  ? 82.591  33.445  24.939  1.00 11.32 ? 94  VAL E CA  1 
ATOM   9588  C  C   . VAL I  1 95  ? 81.957  33.659  23.565  1.00 11.58 ? 94  VAL E C   1 
ATOM   9589  O  O   . VAL I  1 95  ? 80.737  33.592  23.358  1.00 11.76 ? 94  VAL E O   1 
ATOM   9590  C  CB  . VAL I  1 95  ? 82.587  31.965  25.292  1.00 9.09  ? 94  VAL E CB  1 
ATOM   9591  C  CG1 . VAL I  1 95  ? 83.479  31.172  24.396  1.00 7.73  ? 94  VAL E CG1 1 
ATOM   9592  C  CG2 . VAL I  1 95  ? 83.145  31.818  26.669  1.00 8.28  ? 94  VAL E CG2 1 
ATOM   9593  N  N   . ALA I  1 96  ? 82.811  34.084  22.662  1.00 11.40 ? 95  ALA E N   1 
ATOM   9594  C  CA  . ALA I  1 96  ? 82.436  34.143  21.273  1.00 13.58 ? 95  ALA E CA  1 
ATOM   9595  C  C   . ALA I  1 96  ? 83.004  32.888  20.609  1.00 13.58 ? 95  ALA E C   1 
ATOM   9596  O  O   . ALA I  1 96  ? 84.217  32.647  20.532  1.00 14.79 ? 95  ALA E O   1 
ATOM   9597  C  CB  . ALA I  1 96  ? 83.040  35.345  20.593  1.00 14.24 ? 95  ALA E CB  1 
ATOM   9598  N  N   . ASP I  1 97  ? 82.104  32.052  20.159  1.00 13.81 ? 96  ASP E N   1 
ATOM   9599  C  CA  . ASP I  1 97  ? 82.415  30.837  19.459  1.00 16.04 ? 96  ASP E CA  1 
ATOM   9600  C  C   . ASP I  1 97  ? 82.507  31.185  17.989  1.00 15.46 ? 96  ASP E C   1 
ATOM   9601  O  O   . ASP I  1 97  ? 81.450  31.398  17.389  1.00 14.37 ? 96  ASP E O   1 
ATOM   9602  C  CB  . ASP I  1 97  ? 81.300  29.932  19.721  1.00 22.76 ? 96  ASP E CB  1 
ATOM   9603  C  CG  . ASP I  1 97  ? 81.692  28.511  19.525  1.00 28.81 ? 96  ASP E CG  1 
ATOM   9604  O  OD1 . ASP I  1 97  ? 81.553  28.016  18.389  1.00 32.99 ? 96  ASP E OD1 1 
ATOM   9605  O  OD2 . ASP I  1 97  ? 82.128  27.949  20.538  1.00 31.78 ? 96  ASP E OD2 1 
ATOM   9606  N  N   . VAL I  1 98  ? 83.693  31.228  17.363  1.00 16.04 ? 97  VAL E N   1 
ATOM   9607  C  CA  . VAL I  1 98  ? 83.788  31.732  15.999  1.00 13.86 ? 97  VAL E CA  1 
ATOM   9608  C  C   . VAL I  1 98  ? 83.718  30.603  14.967  1.00 14.56 ? 97  VAL E C   1 
ATOM   9609  O  O   . VAL I  1 98  ? 84.300  29.519  15.128  1.00 16.40 ? 97  VAL E O   1 
ATOM   9610  C  CB  . VAL I  1 98  ? 85.120  32.592  15.883  1.00 11.30 ? 97  VAL E CB  1 
ATOM   9611  C  CG1 . VAL I  1 98  ? 85.184  33.254  14.509  1.00 12.08 ? 97  VAL E CG1 1 
ATOM   9612  C  CG2 . VAL I  1 98  ? 85.119  33.827  16.771  1.00 5.59  ? 97  VAL E CG2 1 
ATOM   9613  N  N   . SER I  1 99  ? 82.928  30.788  13.919  1.00 13.40 ? 98  SER E N   1 
ATOM   9614  C  CA  . SER I  1 99  ? 82.880  29.840  12.804  1.00 14.34 ? 98  SER E CA  1 
ATOM   9615  C  C   . SER I  1 99  ? 82.416  30.692  11.631  1.00 13.10 ? 98  SER E C   1 
ATOM   9616  O  O   . SER I  1 99  ? 81.322  31.258  11.691  1.00 13.93 ? 98  SER E O   1 
ATOM   9617  C  CB  . SER I  1 99  ? 81.889  28.726  13.103  1.00 11.52 ? 98  SER E CB  1 
ATOM   9618  O  OG  . SER I  1 99  ? 82.109  27.691  12.147  1.00 19.40 ? 98  SER E OG  1 
ATOM   9619  N  N   . ILE I  1 100 ? 83.258  30.886  10.622  1.00 12.38 ? 99  ILE E N   1 
ATOM   9620  C  CA  . ILE I  1 100 ? 83.033  31.820  9.532   1.00 14.48 ? 99  ILE E CA  1 
ATOM   9621  C  C   . ILE I  1 100 ? 83.695  31.160  8.339   1.00 15.04 ? 99  ILE E C   1 
ATOM   9622  O  O   . ILE I  1 100 ? 84.687  30.439  8.473   1.00 16.85 ? 99  ILE E O   1 
ATOM   9623  C  CB  . ILE I  1 100 ? 83.732  33.205  9.803   1.00 16.73 ? 99  ILE E CB  1 
ATOM   9624  C  CG1 . ILE I  1 100 ? 82.969  33.950  10.882  1.00 17.16 ? 99  ILE E CG1 1 
ATOM   9625  C  CG2 . ILE I  1 100 ? 83.828  34.072  8.512   1.00 14.02 ? 99  ILE E CG2 1 
ATOM   9626  C  CD1 . ILE I  1 100 ? 83.679  35.304  11.180  1.00 21.51 ? 99  ILE E CD1 1 
ATOM   9627  N  N   . GLU I  1 101 ? 83.193  31.445  7.148   1.00 15.96 ? 100 GLU E N   1 
ATOM   9628  C  CA  . GLU I  1 101 ? 83.798  30.960  5.940   1.00 17.11 ? 100 GLU E CA  1 
ATOM   9629  C  C   . GLU I  1 101 ? 83.663  32.124  4.980   1.00 17.87 ? 100 GLU E C   1 
ATOM   9630  O  O   . GLU I  1 101 ? 82.538  32.568  4.759   1.00 17.50 ? 100 GLU E O   1 
ATOM   9631  C  CB  . GLU I  1 101 ? 83.043  29.774  5.431   1.00 19.29 ? 100 GLU E CB  1 
ATOM   9632  C  CG  . GLU I  1 101 ? 83.954  29.328  4.306   1.00 23.50 ? 100 GLU E CG  1 
ATOM   9633  C  CD  . GLU I  1 101 ? 83.445  28.222  3.473   1.00 26.54 ? 100 GLU E CD  1 
ATOM   9634  O  OE1 . GLU I  1 101 ? 82.620  28.522  2.609   1.00 27.52 ? 100 GLU E OE1 1 
ATOM   9635  O  OE2 . GLU I  1 101 ? 83.962  27.121  3.684   1.00 29.18 ? 100 GLU E OE2 1 
ATOM   9636  N  N   . ASP I  1 102 ? 84.774  32.646  4.443   1.00 21.22 ? 101 ASP E N   1 
ATOM   9637  C  CA  . ASP I  1 102 ? 84.782  33.836  3.612   1.00 21.09 ? 101 ASP E CA  1 
ATOM   9638  C  C   . ASP I  1 102 ? 85.670  33.577  2.436   1.00 21.53 ? 101 ASP E C   1 
ATOM   9639  O  O   . ASP I  1 102 ? 86.692  32.909  2.531   1.00 24.23 ? 101 ASP E O   1 
ATOM   9640  C  CB  . ASP I  1 102 ? 85.311  35.017  4.402   1.00 21.50 ? 101 ASP E CB  1 
ATOM   9641  C  CG  . ASP I  1 102 ? 85.161  36.350  3.677   1.00 24.49 ? 101 ASP E CG  1 
ATOM   9642  O  OD1 . ASP I  1 102 ? 84.070  36.673  3.207   1.00 27.77 ? 101 ASP E OD1 1 
ATOM   9643  O  OD2 . ASP I  1 102 ? 86.134  37.084  3.579   1.00 24.16 ? 101 ASP E OD2 1 
ATOM   9644  N  N   . SER I  1 103 ? 85.302  34.082  1.287   1.00 25.22 ? 102 SER E N   1 
ATOM   9645  C  CA  . SER I  1 103 ? 86.072  33.885  0.067   1.00 27.71 ? 102 SER E CA  1 
ATOM   9646  C  C   . SER I  1 103 ? 86.270  35.264  -0.532  1.00 27.39 ? 102 SER E C   1 
ATOM   9647  O  O   . SER I  1 103 ? 85.720  35.643  -1.567  1.00 30.10 ? 102 SER E O   1 
ATOM   9648  C  CB  . SER I  1 103 ? 85.287  32.965  -0.873  1.00 30.38 ? 102 SER E CB  1 
ATOM   9649  O  OG  . SER I  1 103 ? 83.872  33.100  -0.631  1.00 36.25 ? 102 SER E OG  1 
ATOM   9650  N  N   . VAL I  1 104 ? 86.990  36.065  0.239   1.00 26.09 ? 103 VAL E N   1 
ATOM   9651  C  CA  . VAL I  1 104 ? 87.400  37.387  -0.163  1.00 24.85 ? 103 VAL E CA  1 
ATOM   9652  C  C   . VAL I  1 104 ? 88.727  37.557  0.560   1.00 24.62 ? 103 VAL E C   1 
ATOM   9653  O  O   . VAL I  1 104 ? 89.683  38.036  -0.052  1.00 28.07 ? 103 VAL E O   1 
ATOM   9654  C  CB  . VAL I  1 104 ? 86.371  38.431  0.257   1.00 23.83 ? 103 VAL E CB  1 
ATOM   9655  C  CG1 . VAL I  1 104 ? 86.976  39.817  0.309   1.00 28.61 ? 103 VAL E CG1 1 
ATOM   9656  C  CG2 . VAL I  1 104 ? 85.392  38.664  -0.861  1.00 24.02 ? 103 VAL E CG2 1 
ATOM   9657  N  N   . ILE I  1 105 ? 88.831  37.206  1.836   1.00 22.95 ? 104 ILE E N   1 
ATOM   9658  C  CA  . ILE I  1 105 ? 90.118  37.179  2.510   1.00 22.41 ? 104 ILE E CA  1 
ATOM   9659  C  C   . ILE I  1 105 ? 90.892  36.015  1.888   1.00 24.09 ? 104 ILE E C   1 
ATOM   9660  O  O   . ILE I  1 105 ? 90.261  35.058  1.400   1.00 23.33 ? 104 ILE E O   1 
ATOM   9661  C  CB  . ILE I  1 105 ? 89.989  36.914  4.034   1.00 19.65 ? 104 ILE E CB  1 
ATOM   9662  C  CG1 . ILE I  1 105 ? 89.174  35.663  4.338   1.00 16.76 ? 104 ILE E CG1 1 
ATOM   9663  C  CG2 . ILE I  1 105 ? 89.396  38.169  4.651   1.00 20.30 ? 104 ILE E CG2 1 
ATOM   9664  C  CD1 . ILE I  1 105 ? 89.108  35.276  5.822   1.00 15.70 ? 104 ILE E CD1 1 
ATOM   9665  N  N   . SER I  1 106 ? 92.235  36.092  1.856   1.00 24.58 ? 105 SER E N   1 
ATOM   9666  C  CA  . SER I  1 106 ? 93.028  34.965  1.398   1.00 22.02 ? 105 SER E CA  1 
ATOM   9667  C  C   . SER I  1 106 ? 94.208  34.810  2.334   1.00 20.04 ? 105 SER E C   1 
ATOM   9668  O  O   . SER I  1 106 ? 94.677  35.715  3.032   1.00 19.37 ? 105 SER E O   1 
ATOM   9669  C  CB  . SER I  1 106 ? 93.529  35.192  -0.033  1.00 21.64 ? 105 SER E CB  1 
ATOM   9670  O  OG  . SER I  1 106 ? 93.918  33.957  -0.627  1.00 21.44 ? 105 SER E OG  1 
ATOM   9671  N  N   . LEU I  1 107 ? 94.653  33.586  2.351   1.00 18.88 ? 106 LEU E N   1 
ATOM   9672  C  CA  . LEU I  1 107 ? 95.839  33.241  3.080   1.00 20.30 ? 106 LEU E CA  1 
ATOM   9673  C  C   . LEU I  1 107 ? 96.977  33.329  2.089   1.00 22.35 ? 106 LEU E C   1 
ATOM   9674  O  O   . LEU I  1 107 ? 98.149  33.476  2.452   1.00 23.65 ? 106 LEU E O   1 
ATOM   9675  C  CB  . LEU I  1 107 ? 95.711  31.819  3.662   1.00 17.76 ? 106 LEU E CB  1 
ATOM   9676  C  CG  . LEU I  1 107 ? 94.764  31.629  4.868   1.00 15.38 ? 106 LEU E CG  1 
ATOM   9677  C  CD1 . LEU I  1 107 ? 95.072  30.345  5.571   1.00 11.96 ? 106 LEU E CD1 1 
ATOM   9678  C  CD2 . LEU I  1 107 ? 94.983  32.740  5.882   1.00 14.94 ? 106 LEU E CD2 1 
ATOM   9679  N  N   . SER I  1 108 ? 96.659  33.317  0.806   1.00 24.73 ? 107 SER E N   1 
ATOM   9680  C  CA  . SER I  1 108 ? 97.672  33.326  -0.215  1.00 27.72 ? 107 SER E CA  1 
ATOM   9681  C  C   . SER I  1 108 ? 97.341  34.248  -1.379  1.00 30.72 ? 107 SER E C   1 
ATOM   9682  O  O   . SER I  1 108 ? 96.266  34.173  -1.997  1.00 31.05 ? 107 SER E O   1 
ATOM   9683  C  CB  . SER I  1 108 ? 97.860  31.848  -0.632  1.00 29.49 ? 107 SER E CB  1 
ATOM   9684  O  OG  . SER I  1 108 ? 96.779  30.893  -0.597  1.00 29.09 ? 107 SER E OG  1 
ATOM   9685  N  N   . GLY I  1 109 ? 98.200  35.234  -1.646  1.00 32.15 ? 108 GLY E N   1 
ATOM   9686  C  CA  . GLY I  1 109 ? 97.924  36.126  -2.755  1.00 34.92 ? 108 GLY E CA  1 
ATOM   9687  C  C   . GLY I  1 109 ? 97.935  37.621  -2.429  1.00 38.34 ? 108 GLY E C   1 
ATOM   9688  O  O   . GLY I  1 109 ? 98.583  38.118  -1.495  1.00 41.85 ? 108 GLY E O   1 
ATOM   9689  N  N   . ASP I  1 110 ? 97.228  38.405  -3.240  1.00 37.86 ? 109 ASP E N   1 
ATOM   9690  C  CA  . ASP I  1 110 ? 97.133  39.851  -3.105  1.00 35.76 ? 109 ASP E CA  1 
ATOM   9691  C  C   . ASP I  1 110 ? 96.397  40.221  -1.835  1.00 34.21 ? 109 ASP E C   1 
ATOM   9692  O  O   . ASP I  1 110 ? 96.754  41.040  -0.997  1.00 34.52 ? 109 ASP E O   1 
ATOM   9693  C  CB  . ASP I  1 110 ? 96.382  40.364  -4.314  1.00 40.77 ? 109 ASP E CB  1 
ATOM   9694  C  CG  . ASP I  1 110 ? 97.087  41.479  -5.055  1.00 43.45 ? 109 ASP E CG  1 
ATOM   9695  O  OD1 . ASP I  1 110 ? 98.050  41.185  -5.778  1.00 45.53 ? 109 ASP E OD1 1 
ATOM   9696  O  OD2 . ASP I  1 110 ? 96.666  42.633  -4.886  1.00 48.54 ? 109 ASP E OD2 1 
ATOM   9697  N  N   . HIS I  1 111 ? 95.303  39.496  -1.734  1.00 31.68 ? 110 HIS E N   1 
ATOM   9698  C  CA  . HIS I  1 111 ? 94.368  39.699  -0.659  1.00 29.96 ? 110 HIS E CA  1 
ATOM   9699  C  C   . HIS I  1 111 ? 94.855  38.937  0.552   1.00 27.70 ? 110 HIS E C   1 
ATOM   9700  O  O   . HIS I  1 111 ? 94.012  38.505  1.339   1.00 27.15 ? 110 HIS E O   1 
ATOM   9701  C  CB  . HIS I  1 111 ? 92.996  39.180  -1.134  1.00 30.11 ? 110 HIS E CB  1 
ATOM   9702  C  CG  . HIS I  1 111 ? 92.262  40.041  -2.162  1.00 32.19 ? 110 HIS E CG  1 
ATOM   9703  N  ND1 . HIS I  1 111 ? 90.942  40.070  -2.336  1.00 31.31 ? 110 HIS E ND1 1 
ATOM   9704  C  CD2 . HIS I  1 111 ? 92.839  40.948  -3.044  1.00 31.91 ? 110 HIS E CD2 1 
ATOM   9705  C  CE1 . HIS I  1 111 ? 90.699  40.956  -3.277  1.00 32.88 ? 110 HIS E CE1 1 
ATOM   9706  N  NE2 . HIS I  1 111 ? 91.846  41.479  -3.698  1.00 32.28 ? 110 HIS E NE2 1 
ATOM   9707  N  N   . SER I  1 112 ? 96.157  38.723  0.725   1.00 25.44 ? 111 SER E N   1 
ATOM   9708  C  CA  . SER I  1 112 ? 96.517  37.799  1.751   1.00 23.40 ? 111 SER E CA  1 
ATOM   9709  C  C   . SER I  1 112 ? 96.476  38.603  2.992   1.00 21.98 ? 111 SER E C   1 
ATOM   9710  O  O   . SER I  1 112 ? 96.679  39.817  2.990   1.00 24.19 ? 111 SER E O   1 
ATOM   9711  C  CB  . SER I  1 112 ? 97.882  37.262  1.621   1.00 24.24 ? 111 SER E CB  1 
ATOM   9712  O  OG  . SER I  1 112 ? 97.929  36.163  2.528   1.00 31.04 ? 111 SER E OG  1 
ATOM   9713  N  N   . ILE I  1 113 ? 96.131  37.848  4.017   1.00 18.66 ? 112 ILE E N   1 
ATOM   9714  C  CA  . ILE I  1 113 ? 96.039  38.437  5.321   1.00 17.18 ? 112 ILE E CA  1 
ATOM   9715  C  C   . ILE I  1 113 ? 97.185  37.961  6.207   1.00 16.00 ? 112 ILE E C   1 
ATOM   9716  O  O   . ILE I  1 113 ? 97.344  38.439  7.339   1.00 15.17 ? 112 ILE E O   1 
ATOM   9717  C  CB  . ILE I  1 113 ? 94.651  38.098  5.901   1.00 17.93 ? 112 ILE E CB  1 
ATOM   9718  C  CG1 . ILE I  1 113 ? 94.445  36.585  6.066   1.00 16.83 ? 112 ILE E CG1 1 
ATOM   9719  C  CG2 . ILE I  1 113 ? 93.622  38.754  4.979   1.00 15.43 ? 112 ILE E CG2 1 
ATOM   9720  C  CD1 . ILE I  1 113 ? 93.051  36.159  6.500   1.00 14.36 ? 112 ILE E CD1 1 
ATOM   9721  N  N   . ILE I  1 114 ? 98.032  37.025  5.736   1.00 15.41 ? 113 ILE E N   1 
ATOM   9722  C  CA  . ILE I  1 114 ? 99.189  36.600  6.533   1.00 13.26 ? 113 ILE E CA  1 
ATOM   9723  C  C   . ILE I  1 114 ? 100.040 37.848  6.829   1.00 13.16 ? 113 ILE E C   1 
ATOM   9724  O  O   . ILE I  1 114 ? 100.319 38.670  5.943   1.00 16.65 ? 113 ILE E O   1 
ATOM   9725  C  CB  . ILE I  1 114 ? 100.073 35.584  5.782   1.00 9.15  ? 113 ILE E CB  1 
ATOM   9726  C  CG1 . ILE I  1 114 ? 99.307  34.362  5.317   1.00 5.77  ? 113 ILE E CG1 1 
ATOM   9727  C  CG2 . ILE I  1 114 ? 101.207 35.212  6.723   1.00 4.30  ? 113 ILE E CG2 1 
ATOM   9728  C  CD1 . ILE I  1 114 ? 98.739  33.428  6.388   1.00 4.39  ? 113 ILE E CD1 1 
ATOM   9729  N  N   . GLY I  1 115 ? 100.434 38.022  8.067   1.00 10.12 ? 114 GLY E N   1 
ATOM   9730  C  CA  . GLY I  1 115 ? 101.222 39.171  8.406   1.00 9.25  ? 114 GLY E CA  1 
ATOM   9731  C  C   . GLY I  1 115 ? 100.351 40.362  8.783   1.00 8.67  ? 114 GLY E C   1 
ATOM   9732  O  O   . GLY I  1 115 ? 100.896 41.385  9.121   1.00 9.28  ? 114 GLY E O   1 
ATOM   9733  N  N   . ARG I  1 116 ? 99.029  40.348  8.813   1.00 10.59 ? 115 ARG E N   1 
ATOM   9734  C  CA  . ARG I  1 116 ? 98.203  41.483  9.172   1.00 10.51 ? 115 ARG E CA  1 
ATOM   9735  C  C   . ARG I  1 116 ? 97.479  41.237  10.502  1.00 11.96 ? 115 ARG E C   1 
ATOM   9736  O  O   . ARG I  1 116 ? 97.520  40.131  11.066  1.00 13.23 ? 115 ARG E O   1 
ATOM   9737  C  CB  . ARG I  1 116 ? 97.192  41.730  8.063   1.00 8.79  ? 115 ARG E CB  1 
ATOM   9738  C  CG  . ARG I  1 116 ? 97.755  41.532  6.665   1.00 10.71 ? 115 ARG E CG  1 
ATOM   9739  C  CD  . ARG I  1 116 ? 97.535  42.700  5.759   1.00 13.08 ? 115 ARG E CD  1 
ATOM   9740  N  NE  . ARG I  1 116 ? 97.696  42.233  4.394   1.00 17.38 ? 115 ARG E NE  1 
ATOM   9741  C  CZ  . ARG I  1 116 ? 98.172  43.012  3.396   1.00 16.92 ? 115 ARG E CZ  1 
ATOM   9742  N  NH1 . ARG I  1 116 ? 98.547  44.265  3.615   1.00 13.63 ? 115 ARG E NH1 1 
ATOM   9743  N  NH2 . ARG I  1 116 ? 98.280  42.511  2.160   1.00 15.20 ? 115 ARG E NH2 1 
ATOM   9744  N  N   . THR I  1 117 ? 96.827  42.249  11.064  1.00 12.80 ? 116 THR E N   1 
ATOM   9745  C  CA  . THR I  1 117 ? 96.192  42.094  12.346  1.00 13.28 ? 116 THR E CA  1 
ATOM   9746  C  C   . THR I  1 117 ? 94.745  41.688  12.337  1.00 14.42 ? 116 THR E C   1 
ATOM   9747  O  O   . THR I  1 117 ? 93.979  42.174  11.514  1.00 17.68 ? 116 THR E O   1 
ATOM   9748  C  CB  . THR I  1 117 ? 96.380  43.407  13.089  1.00 14.32 ? 116 THR E CB  1 
ATOM   9749  O  OG1 . THR I  1 117 ? 97.798  43.649  13.122  1.00 13.39 ? 116 THR E OG1 1 
ATOM   9750  C  CG2 . THR I  1 117 ? 95.818  43.366  14.521  1.00 14.43 ? 116 THR E CG2 1 
ATOM   9751  N  N   . LEU I  1 118 ? 94.298  40.792  13.209  1.00 15.33 ? 117 LEU E N   1 
ATOM   9752  C  CA  . LEU I  1 118 ? 92.864  40.497  13.345  1.00 13.84 ? 117 LEU E CA  1 
ATOM   9753  C  C   . LEU I  1 118 ? 92.356  41.256  14.561  1.00 14.23 ? 117 LEU E C   1 
ATOM   9754  O  O   . LEU I  1 118 ? 93.005  41.127  15.605  1.00 15.72 ? 117 LEU E O   1 
ATOM   9755  C  CB  . LEU I  1 118 ? 92.600  39.039  13.608  1.00 11.01 ? 117 LEU E CB  1 
ATOM   9756  C  CG  . LEU I  1 118 ? 91.160  38.594  13.636  1.00 9.91  ? 117 LEU E CG  1 
ATOM   9757  C  CD1 . LEU I  1 118 ? 90.502  38.840  12.284  1.00 6.67  ? 117 LEU E CD1 1 
ATOM   9758  C  CD2 . LEU I  1 118 ? 91.147  37.144  14.062  1.00 7.30  ? 117 LEU E CD2 1 
ATOM   9759  N  N   . VAL I  1 119 ? 91.273  42.024  14.546  1.00 11.24 ? 118 VAL E N   1 
ATOM   9760  C  CA  . VAL I  1 119 ? 90.861  42.725  15.746  1.00 9.93  ? 118 VAL E CA  1 
ATOM   9761  C  C   . VAL I  1 119 ? 89.447  42.269  16.147  1.00 10.91 ? 118 VAL E C   1 
ATOM   9762  O  O   . VAL I  1 119 ? 88.605  42.000  15.271  1.00 10.31 ? 118 VAL E O   1 
ATOM   9763  C  CB  . VAL I  1 119 ? 90.927  44.257  15.458  1.00 9.67  ? 118 VAL E CB  1 
ATOM   9764  C  CG1 . VAL I  1 119 ? 90.506  45.074  16.634  1.00 8.87  ? 118 VAL E CG1 1 
ATOM   9765  C  CG2 . VAL I  1 119 ? 92.330  44.687  15.227  1.00 9.32  ? 118 VAL E CG2 1 
ATOM   9766  N  N   . VAL I  1 120 ? 89.212  42.083  17.458  1.00 10.36 ? 119 VAL E N   1 
ATOM   9767  C  CA  . VAL I  1 120 ? 87.883  41.850  17.987  1.00 10.75 ? 119 VAL E CA  1 
ATOM   9768  C  C   . VAL I  1 120 ? 87.605  43.194  18.652  1.00 13.28 ? 119 VAL E C   1 
ATOM   9769  O  O   . VAL I  1 120 ? 88.432  43.743  19.404  1.00 14.88 ? 119 VAL E O   1 
ATOM   9770  C  CB  . VAL I  1 120 ? 87.805  40.692  19.049  1.00 10.03 ? 119 VAL E CB  1 
ATOM   9771  C  CG1 . VAL I  1 120 ? 88.630  40.869  20.310  1.00 4.16  ? 119 VAL E CG1 1 
ATOM   9772  C  CG2 . VAL I  1 120 ? 86.366  40.699  19.537  1.00 11.27 ? 119 VAL E CG2 1 
ATOM   9773  N  N   . HIS I  1 121 ? 86.459  43.767  18.310  1.00 14.91 ? 120 HIS E N   1 
ATOM   9774  C  CA  . HIS I  1 121 ? 86.065  45.107  18.746  1.00 15.06 ? 120 HIS E CA  1 
ATOM   9775  C  C   . HIS I  1 121 ? 85.092  45.186  19.914  1.00 17.41 ? 120 HIS E C   1 
ATOM   9776  O  O   . HIS I  1 121 ? 84.456  44.222  20.349  1.00 18.39 ? 120 HIS E O   1 
ATOM   9777  C  CB  . HIS I  1 121 ? 85.436  45.860  17.606  1.00 11.28 ? 120 HIS E CB  1 
ATOM   9778  C  CG  . HIS I  1 121 ? 86.413  46.466  16.638  1.00 11.72 ? 120 HIS E CG  1 
ATOM   9779  N  ND1 . HIS I  1 121 ? 86.843  47.698  16.616  1.00 9.68  ? 120 HIS E ND1 1 
ATOM   9780  C  CD2 . HIS I  1 121 ? 86.957  45.809  15.562  1.00 13.19 ? 120 HIS E CD2 1 
ATOM   9781  C  CE1 . HIS I  1 121 ? 87.624  47.808  15.556  1.00 11.49 ? 120 HIS E CE1 1 
ATOM   9782  N  NE2 . HIS I  1 121 ? 87.700  46.663  14.907  1.00 14.29 ? 120 HIS E NE2 1 
ATOM   9783  N  N   . GLU I  1 122 ? 84.936  46.407  20.376  1.00 19.61 ? 121 GLU E N   1 
ATOM   9784  C  CA  . GLU I  1 122 ? 84.089  46.773  21.490  1.00 21.51 ? 121 GLU E CA  1 
ATOM   9785  C  C   . GLU I  1 122 ? 82.612  46.612  21.164  1.00 21.05 ? 121 GLU E C   1 
ATOM   9786  O  O   . GLU I  1 122 ? 81.842  46.025  21.924  1.00 22.35 ? 121 GLU E O   1 
ATOM   9787  C  CB  . GLU I  1 122 ? 84.437  48.203  21.810  1.00 22.80 ? 121 GLU E CB  1 
ATOM   9788  C  CG  . GLU I  1 122 ? 83.890  48.814  23.095  1.00 24.89 ? 121 GLU E CG  1 
ATOM   9789  C  CD  . GLU I  1 122 ? 83.841  50.350  23.081  1.00 25.51 ? 121 GLU E CD  1 
ATOM   9790  O  OE1 . GLU I  1 122 ? 84.144  51.026  22.087  1.00 22.71 ? 121 GLU E OE1 1 
ATOM   9791  O  OE2 . GLU I  1 122 ? 83.463  50.886  24.114  1.00 28.66 ? 121 GLU E OE2 1 
ATOM   9792  N  N   . LYS I  1 123 ? 82.211  47.068  20.007  1.00 19.59 ? 122 LYS E N   1 
ATOM   9793  C  CA  . LYS I  1 123 ? 80.810  47.099  19.663  1.00 21.14 ? 122 LYS E CA  1 
ATOM   9794  C  C   . LYS I  1 123 ? 80.450  46.309  18.402  1.00 18.74 ? 122 LYS E C   1 
ATOM   9795  O  O   . LYS I  1 123 ? 81.278  45.776  17.650  1.00 20.39 ? 122 LYS E O   1 
ATOM   9796  C  CB  . LYS I  1 123 ? 80.360  48.561  19.468  1.00 24.70 ? 122 LYS E CB  1 
ATOM   9797  C  CG  . LYS I  1 123 ? 80.618  49.564  20.592  1.00 27.32 ? 122 LYS E CG  1 
ATOM   9798  C  CD  . LYS I  1 123 ? 80.166  50.933  20.120  1.00 28.84 ? 122 LYS E CD  1 
ATOM   9799  C  CE  . LYS I  1 123 ? 80.766  51.998  21.020  1.00 33.81 ? 122 LYS E CE  1 
ATOM   9800  N  NZ  . LYS I  1 123 ? 80.672  53.328  20.413  1.00 35.68 ? 122 LYS E NZ  1 
ATOM   9801  N  N   . ALA I  1 124 ? 79.169  46.273  18.129  1.00 15.37 ? 123 ALA E N   1 
ATOM   9802  C  CA  . ALA I  1 124 ? 78.690  45.565  16.999  1.00 14.66 ? 123 ALA E CA  1 
ATOM   9803  C  C   . ALA I  1 124 ? 78.953  46.452  15.803  1.00 15.32 ? 123 ALA E C   1 
ATOM   9804  O  O   . ALA I  1 124 ? 78.761  47.684  15.791  1.00 17.74 ? 123 ALA E O   1 
ATOM   9805  C  CB  . ALA I  1 124 ? 77.222  45.325  17.211  1.00 13.53 ? 123 ALA E CB  1 
ATOM   9806  N  N   . ASP I  1 125 ? 79.508  45.805  14.803  1.00 15.73 ? 124 ASP E N   1 
ATOM   9807  C  CA  . ASP I  1 125 ? 79.728  46.442  13.529  1.00 16.00 ? 124 ASP E CA  1 
ATOM   9808  C  C   . ASP I  1 125 ? 78.319  46.653  12.974  1.00 18.37 ? 124 ASP E C   1 
ATOM   9809  O  O   . ASP I  1 125 ? 77.464  45.748  12.990  1.00 17.01 ? 124 ASP E O   1 
ATOM   9810  C  CB  . ASP I  1 125 ? 80.571  45.489  12.671  1.00 14.69 ? 124 ASP E CB  1 
ATOM   9811  C  CG  . ASP I  1 125 ? 80.874  45.880  11.231  1.00 16.13 ? 124 ASP E CG  1 
ATOM   9812  O  OD1 . ASP I  1 125 ? 80.549  46.998  10.868  1.00 16.20 ? 124 ASP E OD1 1 
ATOM   9813  O  OD2 . ASP I  1 125 ? 81.429  45.074  10.461  1.00 18.36 ? 124 ASP E OD2 1 
ATOM   9814  N  N   . ASP I  1 126 ? 78.031  47.884  12.543  1.00 20.27 ? 125 ASP E N   1 
ATOM   9815  C  CA  . ASP I  1 126 ? 76.759  48.156  11.871  1.00 21.63 ? 125 ASP E CA  1 
ATOM   9816  C  C   . ASP I  1 126 ? 76.769  47.780  10.390  1.00 21.05 ? 125 ASP E C   1 
ATOM   9817  O  O   . ASP I  1 126 ? 75.874  48.148  9.628   1.00 23.32 ? 125 ASP E O   1 
ATOM   9818  C  CB  . ASP I  1 126 ? 76.361  49.645  11.989  1.00 24.05 ? 125 ASP E CB  1 
ATOM   9819  C  CG  . ASP I  1 126 ? 77.212  50.706  11.280  1.00 28.16 ? 125 ASP E CG  1 
ATOM   9820  O  OD1 . ASP I  1 126 ? 77.544  50.607  10.095  1.00 29.17 ? 125 ASP E OD1 1 
ATOM   9821  O  OD2 . ASP I  1 126 ? 77.539  51.676  11.944  1.00 29.64 ? 125 ASP E OD2 1 
ATOM   9822  N  N   . LEU I  1 127 ? 77.839  47.145  9.934   1.00 20.13 ? 126 LEU E N   1 
ATOM   9823  C  CA  . LEU I  1 127 ? 78.010  46.656  8.583   1.00 19.49 ? 126 LEU E CA  1 
ATOM   9824  C  C   . LEU I  1 127 ? 77.851  47.635  7.446   1.00 21.00 ? 126 LEU E C   1 
ATOM   9825  O  O   . LEU I  1 127 ? 77.668  47.229  6.302   1.00 22.83 ? 126 LEU E O   1 
ATOM   9826  C  CB  . LEU I  1 127 ? 77.052  45.473  8.358   1.00 16.06 ? 126 LEU E CB  1 
ATOM   9827  C  CG  . LEU I  1 127 ? 77.058  44.303  9.342   1.00 11.56 ? 126 LEU E CG  1 
ATOM   9828  C  CD1 . LEU I  1 127 ? 76.376  43.165  8.651   1.00 9.17  ? 126 LEU E CD1 1 
ATOM   9829  C  CD2 . LEU I  1 127 ? 78.452  43.880  9.736   1.00 7.17  ? 126 LEU E CD2 1 
ATOM   9830  N  N   . GLY I  1 128 ? 78.001  48.914  7.721   1.00 24.18 ? 127 GLY E N   1 
ATOM   9831  C  CA  . GLY I  1 128 ? 77.789  49.908  6.684   1.00 29.06 ? 127 GLY E CA  1 
ATOM   9832  C  C   . GLY I  1 128 ? 76.517  50.683  6.988   1.00 31.92 ? 127 GLY E C   1 
ATOM   9833  O  O   . GLY I  1 128 ? 76.553  51.905  7.133   1.00 34.32 ? 127 GLY E O   1 
ATOM   9834  N  N   . LYS I  1 129 ? 75.391  50.009  7.236   1.00 33.20 ? 128 LYS E N   1 
ATOM   9835  C  CA  . LYS I  1 129 ? 74.053  50.589  7.419   1.00 33.32 ? 128 LYS E CA  1 
ATOM   9836  C  C   . LYS I  1 129 ? 73.728  51.362  8.712   1.00 34.27 ? 128 LYS E C   1 
ATOM   9837  O  O   . LYS I  1 129 ? 72.619  51.319  9.264   1.00 33.48 ? 128 LYS E O   1 
ATOM   9838  C  CB  . LYS I  1 129 ? 73.007  49.472  7.257   1.00 33.65 ? 128 LYS E CB  1 
ATOM   9839  C  CG  . LYS I  1 129 ? 73.321  48.189  6.470   1.00 34.75 ? 128 LYS E CG  1 
ATOM   9840  C  CD  . LYS I  1 129 ? 73.598  48.323  4.968   1.00 38.41 ? 128 LYS E CD  1 
ATOM   9841  C  CE  . LYS I  1 129 ? 74.106  46.951  4.485   1.00 41.62 ? 128 LYS E CE  1 
ATOM   9842  N  NZ  . LYS I  1 129 ? 74.407  46.920  3.060   1.00 41.19 ? 128 LYS E NZ  1 
ATOM   9843  N  N   . GLY I  1 130 ? 74.688  52.114  9.246   1.00 35.68 ? 129 GLY E N   1 
ATOM   9844  C  CA  . GLY I  1 130 ? 74.461  52.876  10.475  1.00 37.12 ? 129 GLY E CA  1 
ATOM   9845  C  C   . GLY I  1 130 ? 74.042  54.289  10.120  1.00 38.02 ? 129 GLY E C   1 
ATOM   9846  O  O   . GLY I  1 130 ? 73.652  55.068  10.996  1.00 37.22 ? 129 GLY E O   1 
ATOM   9847  N  N   . GLY I  1 131 ? 74.254  54.663  8.848   1.00 38.39 ? 130 GLY E N   1 
ATOM   9848  C  CA  . GLY I  1 131 ? 73.841  55.970  8.357   1.00 40.35 ? 130 GLY E CA  1 
ATOM   9849  C  C   . GLY I  1 131 ? 74.856  57.111  8.464   1.00 41.50 ? 130 GLY E C   1 
ATOM   9850  O  O   . GLY I  1 131 ? 74.808  58.048  7.662   1.00 43.30 ? 130 GLY E O   1 
ATOM   9851  N  N   . ASN I  1 132 ? 75.747  57.125  9.453   1.00 42.48 ? 131 ASN E N   1 
ATOM   9852  C  CA  . ASN I  1 132 ? 76.763  58.168  9.565   1.00 43.60 ? 131 ASN E CA  1 
ATOM   9853  C  C   . ASN I  1 132 ? 77.954  57.736  8.725   1.00 45.12 ? 131 ASN E C   1 
ATOM   9854  O  O   . ASN I  1 132 ? 78.006  56.547  8.366   1.00 45.85 ? 131 ASN E O   1 
ATOM   9855  C  CB  . ASN I  1 132 ? 77.167  58.344  11.036  1.00 43.25 ? 131 ASN E CB  1 
ATOM   9856  C  CG  . ASN I  1 132 ? 77.656  57.064  11.713  1.00 43.97 ? 131 ASN E CG  1 
ATOM   9857  O  OD1 . ASN I  1 132 ? 78.695  56.551  11.304  1.00 44.30 ? 131 ASN E OD1 1 
ATOM   9858  N  ND2 . ASN I  1 132 ? 76.987  56.445  12.690  1.00 42.12 ? 131 ASN E ND2 1 
ATOM   9859  N  N   . GLU I  1 133 ? 78.954  58.563  8.397   1.00 46.61 ? 132 GLU E N   1 
ATOM   9860  C  CA  . GLU I  1 133 ? 80.027  58.059  7.546   1.00 47.43 ? 132 GLU E CA  1 
ATOM   9861  C  C   . GLU I  1 133 ? 81.007  57.126  8.285   1.00 46.33 ? 132 GLU E C   1 
ATOM   9862  O  O   . GLU I  1 133 ? 81.696  56.307  7.660   1.00 46.90 ? 132 GLU E O   1 
ATOM   9863  C  CB  . GLU I  1 133 ? 80.804  59.200  6.924   1.00 50.72 ? 132 GLU E CB  1 
ATOM   9864  C  CG  . GLU I  1 133 ? 81.491  60.086  7.960   1.00 56.88 ? 132 GLU E CG  1 
ATOM   9865  C  CD  . GLU I  1 133 ? 82.689  60.871  7.411   1.00 58.91 ? 132 GLU E CD  1 
ATOM   9866  O  OE1 . GLU I  1 133 ? 82.552  61.536  6.367   1.00 61.37 ? 132 GLU E OE1 1 
ATOM   9867  O  OE2 . GLU I  1 133 ? 83.760  60.815  8.039   1.00 60.97 ? 132 GLU E OE2 1 
ATOM   9868  N  N   . GLU I  1 134 ? 81.070  57.137  9.624   1.00 43.52 ? 133 GLU E N   1 
ATOM   9869  C  CA  . GLU I  1 134 ? 81.891  56.180  10.339  1.00 41.25 ? 133 GLU E CA  1 
ATOM   9870  C  C   . GLU I  1 134 ? 81.438  54.756  9.972   1.00 39.01 ? 133 GLU E C   1 
ATOM   9871  O  O   . GLU I  1 134 ? 82.231  53.816  9.845   1.00 37.27 ? 133 GLU E O   1 
ATOM   9872  C  CB  . GLU I  1 134 ? 81.717  56.448  11.814  1.00 43.83 ? 133 GLU E CB  1 
ATOM   9873  C  CG  . GLU I  1 134 ? 82.544  55.601  12.771  1.00 49.17 ? 133 GLU E CG  1 
ATOM   9874  C  CD  . GLU I  1 134 ? 84.016  56.006  12.868  1.00 53.37 ? 133 GLU E CD  1 
ATOM   9875  O  OE1 . GLU I  1 134 ? 84.716  56.091  11.841  1.00 54.24 ? 133 GLU E OE1 1 
ATOM   9876  O  OE2 . GLU I  1 134 ? 84.472  56.208  14.002  1.00 56.19 ? 133 GLU E OE2 1 
ATOM   9877  N  N   . SER I  1 135 ? 80.144  54.606  9.722   1.00 35.59 ? 134 SER E N   1 
ATOM   9878  C  CA  . SER I  1 135 ? 79.539  53.366  9.323   1.00 34.35 ? 134 SER E CA  1 
ATOM   9879  C  C   . SER I  1 135 ? 80.058  52.791  8.056   1.00 34.62 ? 134 SER E C   1 
ATOM   9880  O  O   . SER I  1 135 ? 80.080  51.566  7.921   1.00 34.58 ? 134 SER E O   1 
ATOM   9881  C  CB  . SER I  1 135 ? 78.082  53.582  9.204   1.00 33.08 ? 134 SER E CB  1 
ATOM   9882  O  OG  . SER I  1 135 ? 77.721  53.868  10.541  1.00 32.58 ? 134 SER E OG  1 
ATOM   9883  N  N   . THR I  1 136 ? 80.553  53.653  7.198   1.00 33.86 ? 135 THR E N   1 
ATOM   9884  C  CA  . THR I  1 136 ? 81.092  53.160  5.957   1.00 34.33 ? 135 THR E CA  1 
ATOM   9885  C  C   . THR I  1 136 ? 82.608  53.020  6.051   1.00 35.46 ? 135 THR E C   1 
ATOM   9886  O  O   . THR I  1 136 ? 83.251  52.533  5.116   1.00 36.93 ? 135 THR E O   1 
ATOM   9887  C  CB  . THR I  1 136 ? 80.647  54.111  4.851   1.00 33.00 ? 135 THR E CB  1 
ATOM   9888  O  OG1 . THR I  1 136 ? 80.892  55.459  5.246   1.00 33.05 ? 135 THR E OG1 1 
ATOM   9889  C  CG2 . THR I  1 136 ? 79.194  53.858  4.531   1.00 30.49 ? 135 THR E CG2 1 
ATOM   9890  N  N   . LYS I  1 137 ? 83.211  53.453  7.157   1.00 35.98 ? 136 LYS E N   1 
ATOM   9891  C  CA  . LYS I  1 137 ? 84.638  53.275  7.345   1.00 36.68 ? 136 LYS E CA  1 
ATOM   9892  C  C   . LYS I  1 137 ? 84.896  52.107  8.314   1.00 36.07 ? 136 LYS E C   1 
ATOM   9893  O  O   . LYS I  1 137 ? 85.206  50.975  7.890   1.00 34.78 ? 136 LYS E O   1 
ATOM   9894  C  CB  . LYS I  1 137 ? 85.239  54.602  7.882   1.00 39.19 ? 136 LYS E CB  1 
ATOM   9895  C  CG  . LYS I  1 137 ? 85.287  55.819  6.936   1.00 40.38 ? 136 LYS E CG  1 
ATOM   9896  C  CD  . LYS I  1 137 ? 86.060  56.982  7.584   1.00 42.66 ? 136 LYS E CD  1 
ATOM   9897  C  CE  . LYS I  1 137 ? 85.328  57.567  8.809   1.00 45.42 ? 136 LYS E CE  1 
ATOM   9898  N  NZ  . LYS I  1 137 ? 86.064  58.650  9.462   1.00 45.80 ? 136 LYS E NZ  1 
ATOM   9899  N  N   . THR I  1 138 ? 84.693  52.369  9.613   1.00 35.52 ? 137 THR E N   1 
ATOM   9900  C  CA  . THR I  1 138 ? 84.930  51.416  10.684  1.00 34.26 ? 137 THR E CA  1 
ATOM   9901  C  C   . THR I  1 138 ? 83.680  50.553  10.858  1.00 33.58 ? 137 THR E C   1 
ATOM   9902  O  O   . THR I  1 138 ? 83.726  49.371  11.197  1.00 36.40 ? 137 THR E O   1 
ATOM   9903  C  CB  . THR I  1 138 ? 85.276  52.184  12.005  1.00 33.10 ? 137 THR E CB  1 
ATOM   9904  O  OG1 . THR I  1 138 ? 84.118  52.846  12.510  1.00 30.91 ? 137 THR E OG1 1 
ATOM   9905  C  CG2 . THR I  1 138 ? 86.323  53.257  11.745  1.00 31.09 ? 137 THR E CG2 1 
ATOM   9906  N  N   . GLY I  1 139 ? 82.511  51.100  10.560  1.00 33.59 ? 138 GLY E N   1 
ATOM   9907  C  CA  . GLY I  1 139 ? 81.235  50.426  10.771  1.00 31.60 ? 138 GLY E CA  1 
ATOM   9908  C  C   . GLY I  1 139 ? 80.823  50.495  12.216  1.00 30.88 ? 138 GLY E C   1 
ATOM   9909  O  O   . GLY I  1 139 ? 80.032  49.676  12.661  1.00 29.64 ? 138 GLY E O   1 
ATOM   9910  N  N   . ASN I  1 140 ? 81.410  51.460  12.941  1.00 31.27 ? 139 ASN E N   1 
ATOM   9911  C  CA  . ASN I  1 140 ? 81.124  51.762  14.344  1.00 30.82 ? 139 ASN E CA  1 
ATOM   9912  C  C   . ASN I  1 140 ? 81.345  50.610  15.324  1.00 30.06 ? 139 ASN E C   1 
ATOM   9913  O  O   . ASN I  1 140 ? 80.769  50.520  16.412  1.00 29.44 ? 139 ASN E O   1 
ATOM   9914  C  CB  . ASN I  1 140 ? 79.680  52.243  14.504  1.00 32.05 ? 139 ASN E CB  1 
ATOM   9915  C  CG  . ASN I  1 140 ? 79.275  53.442  13.675  1.00 33.04 ? 139 ASN E CG  1 
ATOM   9916  O  OD1 . ASN I  1 140 ? 78.481  54.251  14.131  1.00 36.50 ? 139 ASN E OD1 1 
ATOM   9917  N  ND2 . ASN I  1 140 ? 79.666  53.614  12.424  1.00 29.66 ? 139 ASN E ND2 1 
ATOM   9918  N  N   . ALA I  1 141 ? 82.269  49.714  15.007  1.00 30.08 ? 140 ALA E N   1 
ATOM   9919  C  CA  . ALA I  1 141 ? 82.544  48.611  15.901  1.00 28.91 ? 140 ALA E CA  1 
ATOM   9920  C  C   . ALA I  1 141 ? 83.309  49.099  17.130  1.00 28.57 ? 140 ALA E C   1 
ATOM   9921  O  O   . ALA I  1 141 ? 83.622  48.301  18.018  1.00 30.81 ? 140 ALA E O   1 
ATOM   9922  C  CB  . ALA I  1 141 ? 83.336  47.571  15.133  1.00 28.98 ? 140 ALA E CB  1 
ATOM   9923  N  N   . GLY I  1 142 ? 83.671  50.383  17.236  1.00 25.59 ? 141 GLY E N   1 
ATOM   9924  C  CA  . GLY I  1 142 ? 84.275  50.942  18.443  1.00 23.15 ? 141 GLY E CA  1 
ATOM   9925  C  C   . GLY I  1 142 ? 85.756  50.657  18.642  1.00 22.04 ? 141 GLY E C   1 
ATOM   9926  O  O   . GLY I  1 142 ? 86.496  50.415  17.668  1.00 22.14 ? 141 GLY E O   1 
ATOM   9927  N  N   . SER I  1 143 ? 86.186  50.670  19.912  1.00 19.22 ? 142 SER E N   1 
ATOM   9928  C  CA  . SER I  1 143 ? 87.586  50.442  20.203  1.00 19.76 ? 142 SER E CA  1 
ATOM   9929  C  C   . SER I  1 143 ? 87.945  48.974  19.883  1.00 19.65 ? 142 SER E C   1 
ATOM   9930  O  O   . SER I  1 143 ? 87.062  48.182  19.503  1.00 19.19 ? 142 SER E O   1 
ATOM   9931  C  CB  . SER I  1 143 ? 87.890  50.837  21.700  1.00 18.04 ? 142 SER E CB  1 
ATOM   9932  O  OG  . SER I  1 143 ? 87.142  50.223  22.746  1.00 18.86 ? 142 SER E OG  1 
ATOM   9933  N  N   . ARG I  1 144 ? 89.258  48.671  19.972  1.00 19.85 ? 143 ARG E N   1 
ATOM   9934  C  CA  . ARG I  1 144 ? 89.905  47.423  19.605  1.00 17.29 ? 143 ARG E CA  1 
ATOM   9935  C  C   . ARG I  1 144 ? 90.267  46.790  20.926  1.00 17.42 ? 143 ARG E C   1 
ATOM   9936  O  O   . ARG I  1 144 ? 91.128  47.305  21.634  1.00 17.20 ? 143 ARG E O   1 
ATOM   9937  C  CB  . ARG I  1 144 ? 91.158  47.727  18.778  1.00 15.00 ? 143 ARG E CB  1 
ATOM   9938  C  CG  . ARG I  1 144 ? 90.862  48.455  17.491  1.00 11.89 ? 143 ARG E CG  1 
ATOM   9939  C  CD  . ARG I  1 144 ? 92.113  48.740  16.715  1.00 10.86 ? 143 ARG E CD  1 
ATOM   9940  N  NE  . ARG I  1 144 ? 91.709  49.629  15.634  1.00 13.44 ? 143 ARG E NE  1 
ATOM   9941  C  CZ  . ARG I  1 144 ? 92.521  50.096  14.679  1.00 11.32 ? 143 ARG E CZ  1 
ATOM   9942  N  NH1 . ARG I  1 144 ? 93.814  49.777  14.548  1.00 12.17 ? 143 ARG E NH1 1 
ATOM   9943  N  NH2 . ARG I  1 144 ? 91.998  50.888  13.768  1.00 12.27 ? 143 ARG E NH2 1 
ATOM   9944  N  N   . LEU I  1 145 ? 89.519  45.725  21.232  1.00 18.41 ? 144 LEU E N   1 
ATOM   9945  C  CA  . LEU I  1 145 ? 89.633  44.951  22.458  1.00 15.96 ? 144 LEU E CA  1 
ATOM   9946  C  C   . LEU I  1 145 ? 90.792  43.974  22.472  1.00 15.75 ? 144 LEU E C   1 
ATOM   9947  O  O   . LEU I  1 145 ? 91.341  43.611  23.528  1.00 18.42 ? 144 LEU E O   1 
ATOM   9948  C  CB  . LEU I  1 145 ? 88.360  44.157  22.701  1.00 14.58 ? 144 LEU E CB  1 
ATOM   9949  C  CG  . LEU I  1 145 ? 87.087  44.875  23.201  1.00 17.99 ? 144 LEU E CG  1 
ATOM   9950  C  CD1 . LEU I  1 145 ? 85.952  43.837  23.264  1.00 16.67 ? 144 LEU E CD1 1 
ATOM   9951  C  CD2 . LEU I  1 145 ? 87.306  45.524  24.582  1.00 14.77 ? 144 LEU E CD2 1 
ATOM   9952  N  N   . ALA I  1 146 ? 91.115  43.451  21.308  1.00 13.43 ? 145 ALA E N   1 
ATOM   9953  C  CA  . ALA I  1 146 ? 92.182  42.490  21.236  1.00 10.36 ? 145 ALA E CA  1 
ATOM   9954  C  C   . ALA I  1 146 ? 92.472  42.404  19.776  1.00 10.07 ? 145 ALA E C   1 
ATOM   9955  O  O   . ALA I  1 146 ? 91.659  42.774  18.909  1.00 5.49  ? 145 ALA E O   1 
ATOM   9956  C  CB  . ALA I  1 146 ? 91.759  41.106  21.704  1.00 8.21  ? 145 ALA E CB  1 
ATOM   9957  N  N   . CYS I  1 147 ? 93.700  41.956  19.583  1.00 10.75 ? 146 CYS E N   1 
ATOM   9958  C  CA  . CYS I  1 147 ? 94.169  41.678  18.261  1.00 12.90 ? 146 CYS E CA  1 
ATOM   9959  C  C   . CYS I  1 147 ? 95.430  40.821  18.270  1.00 13.68 ? 146 CYS E C   1 
ATOM   9960  O  O   . CYS I  1 147 ? 96.039  40.576  19.315  1.00 13.62 ? 146 CYS E O   1 
ATOM   9961  C  CB  . CYS I  1 147 ? 94.379  43.002  17.568  1.00 14.24 ? 146 CYS E CB  1 
ATOM   9962  S  SG  . CYS I  1 147 ? 95.563  44.015  18.430  1.00 18.45 ? 146 CYS E SG  1 
ATOM   9963  N  N   . GLY I  1 148 ? 95.761  40.277  17.106  1.00 11.60 ? 147 GLY E N   1 
ATOM   9964  C  CA  . GLY I  1 148 ? 96.901  39.418  16.940  1.00 10.80 ? 147 GLY E CA  1 
ATOM   9965  C  C   . GLY I  1 148 ? 97.402  39.540  15.519  1.00 13.22 ? 147 GLY E C   1 
ATOM   9966  O  O   . GLY I  1 148 ? 96.708  40.119  14.678  1.00 14.81 ? 147 GLY E O   1 
ATOM   9967  N  N   . VAL I  1 149 ? 98.612  39.058  15.210  1.00 12.96 ? 148 VAL E N   1 
ATOM   9968  C  CA  . VAL I  1 149 ? 99.131  39.131  13.857  1.00 11.11 ? 148 VAL E CA  1 
ATOM   9969  C  C   . VAL I  1 149 ? 98.845  37.710  13.437  1.00 13.57 ? 148 VAL E C   1 
ATOM   9970  O  O   . VAL I  1 149 ? 99.029  36.754  14.231  1.00 13.91 ? 148 VAL E O   1 
ATOM   9971  C  CB  . VAL I  1 149 ? 100.668 39.390  13.824  1.00 9.63  ? 148 VAL E CB  1 
ATOM   9972  C  CG1 . VAL I  1 149 ? 101.234 39.408  12.413  1.00 9.07  ? 148 VAL E CG1 1 
ATOM   9973  C  CG2 . VAL I  1 149 ? 100.937 40.737  14.374  1.00 5.62  ? 148 VAL E CG2 1 
ATOM   9974  N  N   . ILE I  1 150 ? 98.381  37.630  12.178  1.00 13.56 ? 149 ILE E N   1 
ATOM   9975  C  CA  . ILE I  1 150 ? 98.043  36.357  11.560  1.00 10.82 ? 149 ILE E CA  1 
ATOM   9976  C  C   . ILE I  1 150 ? 99.348  35.759  11.091  1.00 13.04 ? 149 ILE E C   1 
ATOM   9977  O  O   . ILE I  1 150 ? 99.985  36.265  10.166  1.00 16.49 ? 149 ILE E O   1 
ATOM   9978  C  CB  . ILE I  1 150 ? 97.069  36.665  10.420  1.00 10.99 ? 149 ILE E CB  1 
ATOM   9979  C  CG1 . ILE I  1 150 ? 95.788  37.059  11.062  1.00 9.85  ? 149 ILE E CG1 1 
ATOM   9980  C  CG2 . ILE I  1 150 ? 96.879  35.487  9.457   1.00 4.24  ? 149 ILE E CG2 1 
ATOM   9981  C  CD1 . ILE I  1 150 ? 95.116  38.179  10.269  1.00 13.32 ? 149 ILE E CD1 1 
ATOM   9982  N  N   . GLY I  1 151 ? 99.828  34.745  11.775  1.00 14.10 ? 150 GLY E N   1 
ATOM   9983  C  CA  . GLY I  1 151 ? 101.043 34.043  11.401  1.00 12.71 ? 150 GLY E CA  1 
ATOM   9984  C  C   . GLY I  1 151 ? 100.718 32.799  10.588  1.00 10.97 ? 150 GLY E C   1 
ATOM   9985  O  O   . GLY I  1 151 ? 99.588  32.320  10.549  1.00 10.81 ? 150 GLY E O   1 
ATOM   9986  N  N   . ILE I  1 152 ? 101.707 32.278  9.884   1.00 10.51 ? 151 ILE E N   1 
ATOM   9987  C  CA  . ILE I  1 152 ? 101.574 31.115  9.027   1.00 9.43  ? 151 ILE E CA  1 
ATOM   9988  C  C   . ILE I  1 152 ? 101.640 29.987  10.016  1.00 9.46  ? 151 ILE E C   1 
ATOM   9989  O  O   . ILE I  1 152 ? 102.615 29.903  10.766  1.00 7.43  ? 151 ILE E O   1 
ATOM   9990  C  CB  . ILE I  1 152 ? 102.765 31.100  8.033   1.00 7.08  ? 151 ILE E CB  1 
ATOM   9991  C  CG1 . ILE I  1 152 ? 102.469 32.090  6.932   1.00 5.58  ? 151 ILE E CG1 1 
ATOM   9992  C  CG2 . ILE I  1 152 ? 102.988 29.759  7.426   1.00 2.01  ? 151 ILE E CG2 1 
ATOM   9993  C  CD1 . ILE I  1 152 ? 103.755 32.537  6.203   1.00 2.69  ? 151 ILE E CD1 1 
ATOM   9994  N  N   . ALA I  1 153 ? 100.619 29.166  10.133  1.00 13.43 ? 152 ALA E N   1 
ATOM   9995  C  CA  . ALA I  1 153 ? 100.764 28.034  11.043  1.00 16.89 ? 152 ALA E CA  1 
ATOM   9996  C  C   . ALA I  1 153 ? 101.086 26.820  10.188  1.00 19.99 ? 152 ALA E C   1 
ATOM   9997  O  O   . ALA I  1 153 ? 101.041 26.877  8.948   1.00 21.05 ? 152 ALA E O   1 
ATOM   9998  C  CB  . ALA I  1 153 ? 99.488  27.784  11.811  1.00 14.50 ? 152 ALA E CB  1 
ATOM   9999  N  N   . GLN I  1 154 ? 101.494 25.810  10.940  1.00 24.86 ? 153 GLN E N   1 
ATOM   10000 C  CA  . GLN I  1 154 ? 101.927 24.515  10.455  1.00 29.39 ? 153 GLN E CA  1 
ATOM   10001 C  C   . GLN I  1 154 ? 100.749 23.679  10.010  1.00 30.81 ? 153 GLN E C   1 
ATOM   10002 O  O   . GLN I  1 154 ? 99.861  23.400  10.819  1.00 32.04 ? 153 GLN E O   1 
ATOM   10003 C  CB  . GLN I  1 154 ? 102.699 23.833  11.598  1.00 32.56 ? 153 GLN E CB  1 
ATOM   10004 C  CG  . GLN I  1 154 ? 103.313 22.443  11.419  1.00 34.41 ? 153 GLN E CG  1 
ATOM   10005 C  CD  . GLN I  1 154 ? 104.115 21.996  12.647  1.00 35.82 ? 153 GLN E CD  1 
ATOM   10006 O  OE1 . GLN I  1 154 ? 103.728 22.141  13.809  1.00 37.10 ? 153 GLN E OE1 1 
ATOM   10007 N  NE2 . GLN I  1 154 ? 105.293 21.419  12.475  1.00 37.30 ? 153 GLN E NE2 1 
ATOM   10008 O  OXT . GLN I  1 154 ? 100.741 23.308  8.843   1.00 35.93 ? 153 GLN E OXT 1 
HETATM 10009 C  C   . ACE J  1 1   ? 105.536 42.453  0.232   1.00 48.82 ? 0   ACE J C   1 
HETATM 10010 O  O   . ACE J  1 1   ? 104.844 43.176  -0.500  1.00 51.78 ? 0   ACE J O   1 
HETATM 10011 C  CH3 . ACE J  1 1   ? 105.387 40.943  0.120   1.00 48.03 ? 0   ACE J CH3 1 
ATOM   10012 N  N   . ALA J  1 2   ? 106.430 42.999  1.071   1.00 46.95 ? 1   ALA J N   1 
ATOM   10013 C  CA  . ALA J  1 2   ? 106.462 44.447  1.247   1.00 44.87 ? 1   ALA J CA  1 
ATOM   10014 C  C   . ALA J  1 2   ? 107.822 45.130  1.447   1.00 43.12 ? 1   ALA J C   1 
ATOM   10015 O  O   . ALA J  1 2   ? 108.888 44.516  1.356   1.00 43.18 ? 1   ALA J O   1 
ATOM   10016 C  CB  . ALA J  1 2   ? 105.529 44.789  2.435   1.00 45.24 ? 1   ALA J CB  1 
ATOM   10017 N  N   . THR J  1 3   ? 107.737 46.439  1.691   1.00 39.95 ? 2   THR J N   1 
ATOM   10018 C  CA  . THR J  1 3   ? 108.870 47.294  1.943   1.00 36.75 ? 2   THR J CA  1 
ATOM   10019 C  C   . THR J  1 3   ? 109.240 47.218  3.420   1.00 35.30 ? 2   THR J C   1 
ATOM   10020 O  O   . THR J  1 3   ? 110.407 47.450  3.748   1.00 36.91 ? 2   THR J O   1 
ATOM   10021 C  CB  . THR J  1 3   ? 108.508 48.784  1.561   1.00 37.15 ? 2   THR J CB  1 
ATOM   10022 O  OG1 . THR J  1 3   ? 107.770 48.731  0.339   1.00 40.95 ? 2   THR J OG1 1 
ATOM   10023 C  CG2 . THR J  1 3   ? 109.701 49.688  1.347   1.00 34.80 ? 2   THR J CG2 1 
ATOM   10024 N  N   . LYS J  1 4   ? 108.331 46.965  4.369   1.00 31.24 ? 3   LYS J N   1 
ATOM   10025 C  CA  . LYS J  1 4   ? 108.692 47.032  5.779   1.00 27.05 ? 3   LYS J CA  1 
ATOM   10026 C  C   . LYS J  1 4   ? 107.967 45.972  6.555   1.00 24.49 ? 3   LYS J C   1 
ATOM   10027 O  O   . LYS J  1 4   ? 106.890 45.557  6.126   1.00 25.45 ? 3   LYS J O   1 
ATOM   10028 C  CB  . LYS J  1 4   ? 108.311 48.357  6.427   1.00 26.45 ? 3   LYS J CB  1 
ATOM   10029 C  CG  . LYS J  1 4   ? 109.063 49.581  5.979   1.00 29.25 ? 3   LYS J CG  1 
ATOM   10030 C  CD  . LYS J  1 4   ? 108.636 50.794  6.819   1.00 33.81 ? 3   LYS J CD  1 
ATOM   10031 C  CE  . LYS J  1 4   ? 109.296 50.899  8.213   1.00 36.75 ? 3   LYS J CE  1 
ATOM   10032 N  NZ  . LYS J  1 4   ? 109.313 52.276  8.699   1.00 36.11 ? 3   LYS J NZ  1 
ATOM   10033 N  N   . ALA J  1 5   ? 108.505 45.548  7.690   1.00 20.58 ? 4   ALA J N   1 
ATOM   10034 C  CA  . ALA J  1 5   ? 107.846 44.605  8.561   1.00 15.21 ? 4   ALA J CA  1 
ATOM   10035 C  C   . ALA J  1 5   ? 108.337 44.946  9.948   1.00 12.57 ? 4   ALA J C   1 
ATOM   10036 O  O   . ALA J  1 5   ? 109.356 45.631  10.086  1.00 10.40 ? 4   ALA J O   1 
ATOM   10037 C  CB  . ALA J  1 5   ? 108.248 43.185  8.199   1.00 16.49 ? 4   ALA J CB  1 
ATOM   10038 N  N   . VAL J  1 6   ? 107.626 44.518  10.984  1.00 9.05  ? 5   VAL J N   1 
ATOM   10039 C  CA  . VAL J  1 6   ? 107.972 44.798  12.368  1.00 8.24  ? 5   VAL J CA  1 
ATOM   10040 C  C   . VAL J  1 6   ? 107.636 43.546  13.173  1.00 9.08  ? 5   VAL J C   1 
ATOM   10041 O  O   . VAL J  1 6   ? 106.766 42.780  12.778  1.00 9.23  ? 5   VAL J O   1 
ATOM   10042 C  CB  . VAL J  1 6   ? 107.180 46.055  12.864  1.00 6.86  ? 5   VAL J CB  1 
ATOM   10043 C  CG1 . VAL J  1 6   ? 105.717 45.827  12.565  1.00 10.62 ? 5   VAL J CG1 1 
ATOM   10044 C  CG2 . VAL J  1 6   ? 107.350 46.322  14.373  1.00 5.51  ? 5   VAL J CG2 1 
ATOM   10045 N  N   . ALA J  1 7   ? 108.368 43.256  14.249  1.00 10.79 ? 6   ALA J N   1 
ATOM   10046 C  CA  . ALA J  1 7   ? 108.116 42.128  15.121  1.00 11.78 ? 6   ALA J CA  1 
ATOM   10047 C  C   . ALA J  1 7   ? 108.288 42.650  16.537  1.00 13.17 ? 6   ALA J C   1 
ATOM   10048 O  O   . ALA J  1 7   ? 109.159 43.473  16.838  1.00 15.60 ? 6   ALA J O   1 
ATOM   10049 C  CB  . ALA J  1 7   ? 109.111 41.002  14.922  1.00 11.08 ? 6   ALA J CB  1 
ATOM   10050 N  N   . VAL J  1 8   ? 107.387 42.213  17.402  1.00 13.51 ? 7   VAL J N   1 
ATOM   10051 C  CA  . VAL J  1 8   ? 107.330 42.672  18.774  1.00 13.14 ? 7   VAL J CA  1 
ATOM   10052 C  C   . VAL J  1 8   ? 107.580 41.375  19.543  1.00 15.03 ? 7   VAL J C   1 
ATOM   10053 O  O   . VAL J  1 8   ? 106.831 40.395  19.473  1.00 17.96 ? 7   VAL J O   1 
ATOM   10054 C  CB  . VAL J  1 8   ? 105.929 43.285  19.050  1.00 10.37 ? 7   VAL J CB  1 
ATOM   10055 C  CG1 . VAL J  1 8   ? 105.902 43.934  20.423  1.00 4.71  ? 7   VAL J CG1 1 
ATOM   10056 C  CG2 . VAL J  1 8   ? 105.600 44.308  17.962  1.00 10.54 ? 7   VAL J CG2 1 
ATOM   10057 N  N   . LEU J  1 9   ? 108.710 41.387  20.212  1.00 13.45 ? 8   LEU J N   1 
ATOM   10058 C  CA  . LEU J  1 9   ? 109.258 40.240  20.868  1.00 12.18 ? 8   LEU J CA  1 
ATOM   10059 C  C   . LEU J  1 9   ? 108.884 40.212  22.308  1.00 14.35 ? 8   LEU J C   1 
ATOM   10060 O  O   . LEU J  1 9   ? 109.292 41.095  23.052  1.00 15.11 ? 8   LEU J O   1 
ATOM   10061 C  CB  . LEU J  1 9   ? 110.774 40.292  20.733  1.00 11.62 ? 8   LEU J CB  1 
ATOM   10062 C  CG  . LEU J  1 9   ? 111.488 39.701  19.544  1.00 5.23  ? 8   LEU J CG  1 
ATOM   10063 C  CD1 . LEU J  1 9   ? 110.879 40.156  18.281  1.00 7.29  ? 8   LEU J CD1 1 
ATOM   10064 C  CD2 . LEU J  1 9   ? 112.916 40.124  19.601  1.00 3.05  ? 8   LEU J CD2 1 
ATOM   10065 N  N   . LYS J  1 10  ? 108.144 39.236  22.766  1.00 18.60 ? 9   LYS J N   1 
ATOM   10066 C  CA  . LYS J  1 10  ? 107.829 39.143  24.182  1.00 22.18 ? 9   LYS J CA  1 
ATOM   10067 C  C   . LYS J  1 10  ? 108.010 37.676  24.576  1.00 23.82 ? 9   LYS J C   1 
ATOM   10068 O  O   . LYS J  1 10  ? 108.016 36.798  23.705  1.00 22.74 ? 9   LYS J O   1 
ATOM   10069 C  CB  . LYS J  1 10  ? 106.389 39.608  24.421  1.00 24.52 ? 9   LYS J CB  1 
ATOM   10070 C  CG  . LYS J  1 10  ? 106.099 41.121  24.285  1.00 31.68 ? 9   LYS J CG  1 
ATOM   10071 C  CD  . LYS J  1 10  ? 104.643 41.446  24.685  1.00 36.66 ? 9   LYS J CD  1 
ATOM   10072 C  CE  . LYS J  1 10  ? 103.671 41.629  23.494  1.00 40.78 ? 9   LYS J CE  1 
ATOM   10073 N  NZ  . LYS J  1 10  ? 102.255 41.773  23.894  1.00 43.43 ? 9   LYS J NZ  1 
ATOM   10074 N  N   . GLY J  1 11  ? 108.213 37.370  25.850  1.00 25.65 ? 10  GLY J N   1 
ATOM   10075 C  CA  . GLY J  1 11  ? 108.364 36.010  26.312  1.00 29.31 ? 10  GLY J CA  1 
ATOM   10076 C  C   . GLY J  1 11  ? 107.949 35.897  27.777  1.00 33.02 ? 10  GLY J C   1 
ATOM   10077 O  O   . GLY J  1 11  ? 107.580 36.877  28.436  1.00 34.99 ? 10  GLY J O   1 
ATOM   10078 N  N   . ASP J  1 12  ? 108.010 34.694  28.352  1.00 34.40 ? 11  ASP J N   1 
ATOM   10079 C  CA  . ASP J  1 12  ? 107.636 34.446  29.742  1.00 35.97 ? 11  ASP J CA  1 
ATOM   10080 C  C   . ASP J  1 12  ? 108.819 34.839  30.617  1.00 35.36 ? 11  ASP J C   1 
ATOM   10081 O  O   . ASP J  1 12  ? 109.360 34.019  31.370  1.00 36.70 ? 11  ASP J O   1 
ATOM   10082 C  CB  . ASP J  1 12  ? 107.318 32.961  29.951  1.00 40.67 ? 11  ASP J CB  1 
ATOM   10083 C  CG  . ASP J  1 12  ? 106.342 32.370  28.930  1.00 45.53 ? 11  ASP J CG  1 
ATOM   10084 O  OD1 . ASP J  1 12  ? 105.130 32.430  29.162  1.00 48.12 ? 11  ASP J OD1 1 
ATOM   10085 O  OD2 . ASP J  1 12  ? 106.800 31.857  27.897  1.00 48.92 ? 11  ASP J OD2 1 
ATOM   10086 N  N   . GLY J  1 13  ? 109.244 36.099  30.519  1.00 32.81 ? 12  GLY J N   1 
ATOM   10087 C  CA  . GLY J  1 13  ? 110.404 36.573  31.225  1.00 29.34 ? 12  GLY J CA  1 
ATOM   10088 C  C   . GLY J  1 13  ? 110.744 37.941  30.681  1.00 28.17 ? 12  GLY J C   1 
ATOM   10089 O  O   . GLY J  1 13  ? 110.176 38.351  29.662  1.00 28.94 ? 12  GLY J O   1 
ATOM   10090 N  N   . PRO J  1 14  ? 111.723 38.622  31.313  1.00 25.90 ? 13  PRO J N   1 
ATOM   10091 C  CA  . PRO J  1 14  ? 112.069 40.030  31.154  1.00 23.64 ? 13  PRO J CA  1 
ATOM   10092 C  C   . PRO J  1 14  ? 112.391 40.543  29.778  1.00 21.50 ? 13  PRO J C   1 
ATOM   10093 O  O   . PRO J  1 14  ? 112.420 41.767  29.623  1.00 22.06 ? 13  PRO J O   1 
ATOM   10094 C  CB  . PRO J  1 14  ? 113.243 40.256  32.068  1.00 23.07 ? 13  PRO J CB  1 
ATOM   10095 C  CG  . PRO J  1 14  ? 113.944 38.947  31.925  1.00 24.03 ? 13  PRO J CG  1 
ATOM   10096 C  CD  . PRO J  1 14  ? 112.769 38.005  32.124  1.00 24.82 ? 13  PRO J CD  1 
ATOM   10097 N  N   . VAL J  1 15  ? 112.588 39.625  28.825  1.00 18.65 ? 14  VAL J N   1 
ATOM   10098 C  CA  . VAL J  1 15  ? 113.098 39.969  27.525  1.00 15.25 ? 14  VAL J CA  1 
ATOM   10099 C  C   . VAL J  1 15  ? 111.940 40.425  26.688  1.00 16.39 ? 14  VAL J C   1 
ATOM   10100 O  O   . VAL J  1 15  ? 110.894 39.780  26.597  1.00 17.91 ? 14  VAL J O   1 
ATOM   10101 C  CB  . VAL J  1 15  ? 113.767 38.754  26.893  1.00 12.46 ? 14  VAL J CB  1 
ATOM   10102 C  CG1 . VAL J  1 15  ? 114.448 39.167  25.635  1.00 11.59 ? 14  VAL J CG1 1 
ATOM   10103 C  CG2 . VAL J  1 15  ? 114.834 38.206  27.775  1.00 10.87 ? 14  VAL J CG2 1 
ATOM   10104 N  N   . GLN J  1 16  ? 112.148 41.574  26.085  1.00 17.26 ? 15  GLN J N   1 
ATOM   10105 C  CA  . GLN J  1 16  ? 111.185 42.144  25.169  1.00 17.93 ? 15  GLN J CA  1 
ATOM   10106 C  C   . GLN J  1 16  ? 111.916 43.087  24.228  1.00 17.33 ? 15  GLN J C   1 
ATOM   10107 O  O   . GLN J  1 16  ? 113.036 43.520  24.536  1.00 16.72 ? 15  GLN J O   1 
ATOM   10108 C  CB  . GLN J  1 16  ? 110.135 42.913  25.930  1.00 22.40 ? 15  GLN J CB  1 
ATOM   10109 C  CG  . GLN J  1 16  ? 110.723 44.047  26.745  1.00 28.82 ? 15  GLN J CG  1 
ATOM   10110 C  CD  . GLN J  1 16  ? 109.624 44.880  27.339  1.00 33.07 ? 15  GLN J CD  1 
ATOM   10111 O  OE1 . GLN J  1 16  ? 109.162 45.865  26.754  1.00 36.50 ? 15  GLN J OE1 1 
ATOM   10112 N  NE2 . GLN J  1 16  ? 109.168 44.471  28.518  1.00 33.94 ? 15  GLN J NE2 1 
ATOM   10113 N  N   . GLY J  1 17  ? 111.326 43.439  23.090  1.00 16.67 ? 16  GLY J N   1 
ATOM   10114 C  CA  . GLY J  1 17  ? 111.967 44.322  22.142  1.00 16.07 ? 16  GLY J CA  1 
ATOM   10115 C  C   . GLY J  1 17  ? 111.090 44.486  20.927  1.00 17.19 ? 16  GLY J C   1 
ATOM   10116 O  O   . GLY J  1 17  ? 110.000 43.898  20.848  1.00 17.97 ? 16  GLY J O   1 
ATOM   10117 N  N   . ILE J  1 18  ? 111.535 45.302  19.974  1.00 16.32 ? 17  ILE J N   1 
ATOM   10118 C  CA  . ILE J  1 18  ? 110.806 45.581  18.733  1.00 15.21 ? 17  ILE J CA  1 
ATOM   10119 C  C   . ILE J  1 18  ? 111.933 45.512  17.699  1.00 15.04 ? 17  ILE J C   1 
ATOM   10120 O  O   . ILE J  1 18  ? 113.032 46.012  17.996  1.00 16.51 ? 17  ILE J O   1 
ATOM   10121 C  CB  . ILE J  1 18  ? 110.193 47.006  18.729  1.00 14.38 ? 17  ILE J CB  1 
ATOM   10122 C  CG1 . ILE J  1 18  ? 109.470 47.376  20.040  1.00 17.42 ? 17  ILE J CG1 1 
ATOM   10123 C  CG2 . ILE J  1 18  ? 109.184 47.049  17.618  1.00 15.16 ? 17  ILE J CG2 1 
ATOM   10124 C  CD1 . ILE J  1 18  ? 108.261 46.552  20.544  1.00 15.78 ? 17  ILE J CD1 1 
ATOM   10125 N  N   . ILE J  1 19  ? 111.771 44.888  16.534  1.00 12.43 ? 18  ILE J N   1 
ATOM   10126 C  CA  . ILE J  1 19  ? 112.833 44.800  15.521  1.00 10.09 ? 18  ILE J CA  1 
ATOM   10127 C  C   . ILE J  1 19  ? 112.115 45.217  14.268  1.00 9.40  ? 18  ILE J C   1 
ATOM   10128 O  O   . ILE J  1 19  ? 110.961 44.839  14.041  1.00 12.89 ? 18  ILE J O   1 
ATOM   10129 C  CB  . ILE J  1 19  ? 113.381 43.334  15.353  1.00 7.02  ? 18  ILE J CB  1 
ATOM   10130 C  CG1 . ILE J  1 19  ? 114.074 42.902  16.625  1.00 4.06  ? 18  ILE J CG1 1 
ATOM   10131 C  CG2 . ILE J  1 19  ? 114.362 43.225  14.201  1.00 3.28  ? 18  ILE J CG2 1 
ATOM   10132 C  CD1 . ILE J  1 19  ? 115.284 43.729  17.050  1.00 4.66  ? 18  ILE J CD1 1 
ATOM   10133 N  N   . ASN J  1 20  ? 112.729 46.035  13.485  1.00 8.37  ? 19  ASN J N   1 
ATOM   10134 C  CA  . ASN J  1 20  ? 112.163 46.491  12.240  1.00 12.45 ? 19  ASN J CA  1 
ATOM   10135 C  C   . ASN J  1 20  ? 112.858 45.858  11.040  1.00 12.42 ? 19  ASN J C   1 
ATOM   10136 O  O   . ASN J  1 20  ? 114.068 45.687  11.097  1.00 11.71 ? 19  ASN J O   1 
ATOM   10137 C  CB  . ASN J  1 20  ? 112.305 47.999  12.163  1.00 15.54 ? 19  ASN J CB  1 
ATOM   10138 C  CG  . ASN J  1 20  ? 111.675 48.777  13.310  1.00 19.87 ? 19  ASN J CG  1 
ATOM   10139 O  OD1 . ASN J  1 20  ? 112.162 48.825  14.448  1.00 24.57 ? 19  ASN J OD1 1 
ATOM   10140 N  ND2 . ASN J  1 20  ? 110.545 49.420  13.049  1.00 20.54 ? 19  ASN J ND2 1 
ATOM   10141 N  N   . PHE J  1 21  ? 112.174 45.495  9.959   1.00 12.15 ? 20  PHE J N   1 
ATOM   10142 C  CA  . PHE J  1 21  ? 112.806 44.988  8.746   1.00 15.57 ? 20  PHE J CA  1 
ATOM   10143 C  C   . PHE J  1 21  ? 112.401 45.983  7.702   1.00 18.39 ? 20  PHE J C   1 
ATOM   10144 O  O   . PHE J  1 21  ? 111.260 46.459  7.750   1.00 22.45 ? 20  PHE J O   1 
ATOM   10145 C  CB  . PHE J  1 21  ? 112.280 43.625  8.244   1.00 14.39 ? 20  PHE J CB  1 
ATOM   10146 C  CG  . PHE J  1 21  ? 112.503 42.554  9.286   1.00 12.22 ? 20  PHE J CG  1 
ATOM   10147 C  CD1 . PHE J  1 21  ? 111.601 42.427  10.334  1.00 11.70 ? 20  PHE J CD1 1 
ATOM   10148 C  CD2 . PHE J  1 21  ? 113.647 41.792  9.242   1.00 11.38 ? 20  PHE J CD2 1 
ATOM   10149 C  CE1 . PHE J  1 21  ? 111.845 41.541  11.354  1.00 10.87 ? 20  PHE J CE1 1 
ATOM   10150 C  CE2 . PHE J  1 21  ? 113.889 40.898  10.272  1.00 13.18 ? 20  PHE J CE2 1 
ATOM   10151 C  CZ  . PHE J  1 21  ? 112.996 40.777  11.323  1.00 13.73 ? 20  PHE J CZ  1 
ATOM   10152 N  N   . GLU J  1 22  ? 113.255 46.312  6.754   1.00 19.26 ? 21  GLU J N   1 
ATOM   10153 C  CA  . GLU J  1 22  ? 112.869 47.225  5.703   1.00 20.71 ? 21  GLU J CA  1 
ATOM   10154 C  C   . GLU J  1 22  ? 113.645 46.712  4.517   1.00 21.12 ? 21  GLU J C   1 
ATOM   10155 O  O   . GLU J  1 22  ? 114.841 46.457  4.664   1.00 20.95 ? 21  GLU J O   1 
ATOM   10156 C  CB  . GLU J  1 22  ? 113.284 48.625  6.099   1.00 24.65 ? 21  GLU J CB  1 
ATOM   10157 C  CG  . GLU J  1 22  ? 112.906 49.714  5.105   1.00 32.82 ? 21  GLU J CG  1 
ATOM   10158 C  CD  . GLU J  1 22  ? 113.174 51.147  5.599   1.00 38.32 ? 21  GLU J CD  1 
ATOM   10159 O  OE1 . GLU J  1 22  ? 112.555 51.591  6.581   1.00 41.22 ? 21  GLU J OE1 1 
ATOM   10160 O  OE2 . GLU J  1 22  ? 114.002 51.832  4.985   1.00 41.25 ? 21  GLU J OE2 1 
ATOM   10161 N  N   . GLN J  1 23  ? 113.026 46.506  3.360   1.00 21.63 ? 22  GLN J N   1 
ATOM   10162 C  CA  . GLN J  1 23  ? 113.668 45.978  2.172   1.00 23.56 ? 22  GLN J CA  1 
ATOM   10163 C  C   . GLN J  1 23  ? 113.268 46.925  1.057   1.00 27.83 ? 22  GLN J C   1 
ATOM   10164 O  O   . GLN J  1 23  ? 112.401 46.650  0.220   1.00 27.75 ? 22  GLN J O   1 
ATOM   10165 C  CB  . GLN J  1 23  ? 113.152 44.579  1.925   1.00 19.24 ? 22  GLN J CB  1 
ATOM   10166 C  CG  . GLN J  1 23  ? 113.669 43.972  0.656   1.00 19.00 ? 22  GLN J CG  1 
ATOM   10167 C  CD  . GLN J  1 23  ? 113.160 42.568  0.458   1.00 21.97 ? 22  GLN J CD  1 
ATOM   10168 O  OE1 . GLN J  1 23  ? 112.048 42.203  0.854   1.00 25.11 ? 22  GLN J OE1 1 
ATOM   10169 N  NE2 . GLN J  1 23  ? 113.967 41.681  -0.100  1.00 23.15 ? 22  GLN J NE2 1 
ATOM   10170 N  N   . LYS J  1 24  ? 113.885 48.102  0.994   1.00 33.66 ? 23  LYS J N   1 
ATOM   10171 C  CA  . LYS J  1 24  ? 113.474 49.082  -0.017  1.00 38.95 ? 23  LYS J CA  1 
ATOM   10172 C  C   . LYS J  1 24  ? 114.060 48.832  -1.413  1.00 40.62 ? 23  LYS J C   1 
ATOM   10173 O  O   . LYS J  1 24  ? 114.931 49.565  -1.869  1.00 41.81 ? 23  LYS J O   1 
ATOM   10174 C  CB  . LYS J  1 24  ? 113.821 50.531  0.496   1.00 40.78 ? 23  LYS J CB  1 
ATOM   10175 C  CG  . LYS J  1 24  ? 112.979 50.920  1.743   1.00 43.06 ? 23  LYS J CG  1 
ATOM   10176 C  CD  . LYS J  1 24  ? 112.244 52.284  1.816   1.00 44.19 ? 23  LYS J CD  1 
ATOM   10177 C  CE  . LYS J  1 24  ? 113.086 53.509  2.232   1.00 44.96 ? 23  LYS J CE  1 
ATOM   10178 N  NZ  . LYS J  1 24  ? 112.249 54.662  2.549   1.00 44.17 ? 23  LYS J NZ  1 
ATOM   10179 N  N   . GLU J  1 25  ? 113.613 47.747  -2.059  1.00 42.70 ? 24  GLU J N   1 
ATOM   10180 C  CA  . GLU J  1 25  ? 113.893 47.342  -3.437  1.00 45.88 ? 24  GLU J CA  1 
ATOM   10181 C  C   . GLU J  1 25  ? 113.634 45.842  -3.499  1.00 46.77 ? 24  GLU J C   1 
ATOM   10182 O  O   . GLU J  1 25  ? 114.210 45.025  -2.788  1.00 47.20 ? 24  GLU J O   1 
ATOM   10183 C  CB  . GLU J  1 25  ? 115.356 47.542  -3.950  1.00 46.89 ? 24  GLU J CB  1 
ATOM   10184 C  CG  . GLU J  1 25  ? 115.451 47.255  -5.472  1.00 50.18 ? 24  GLU J CG  1 
ATOM   10185 C  CD  . GLU J  1 25  ? 116.722 47.659  -6.242  1.00 51.93 ? 24  GLU J CD  1 
ATOM   10186 O  OE1 . GLU J  1 25  ? 117.836 47.259  -5.871  1.00 51.44 ? 24  GLU J OE1 1 
ATOM   10187 O  OE2 . GLU J  1 25  ? 116.569 48.367  -7.246  1.00 50.43 ? 24  GLU J OE2 1 
ATOM   10188 N  N   . SER J  1 26  ? 112.746 45.497  -4.411  1.00 49.37 ? 25  SER J N   1 
ATOM   10189 C  CA  . SER J  1 26  ? 112.210 44.171  -4.730  1.00 50.85 ? 25  SER J CA  1 
ATOM   10190 C  C   . SER J  1 26  ? 112.989 42.864  -4.438  1.00 50.97 ? 25  SER J C   1 
ATOM   10191 O  O   . SER J  1 26  ? 112.404 41.797  -4.244  1.00 51.39 ? 25  SER J O   1 
ATOM   10192 C  CB  . SER J  1 26  ? 111.815 44.279  -6.244  1.00 52.38 ? 25  SER J CB  1 
ATOM   10193 O  OG  . SER J  1 26  ? 111.614 45.638  -6.724  1.00 52.68 ? 25  SER J OG  1 
ATOM   10194 N  N   . ASN J  1 27  ? 114.316 42.909  -4.379  1.00 50.48 ? 26  ASN J N   1 
ATOM   10195 C  CA  . ASN J  1 27  ? 115.193 41.746  -4.239  1.00 49.73 ? 26  ASN J CA  1 
ATOM   10196 C  C   . ASN J  1 27  ? 116.513 42.323  -3.688  1.00 48.25 ? 26  ASN J C   1 
ATOM   10197 O  O   . ASN J  1 27  ? 117.652 42.112  -4.146  1.00 49.00 ? 26  ASN J O   1 
ATOM   10198 C  CB  . ASN J  1 27  ? 115.350 41.128  -5.641  1.00 52.77 ? 26  ASN J CB  1 
ATOM   10199 C  CG  . ASN J  1 27  ? 116.251 39.901  -5.759  1.00 54.73 ? 26  ASN J CG  1 
ATOM   10200 O  OD1 . ASN J  1 27  ? 115.793 38.756  -5.722  1.00 58.18 ? 26  ASN J OD1 1 
ATOM   10201 N  ND2 . ASN J  1 27  ? 117.558 40.058  -5.917  1.00 55.80 ? 26  ASN J ND2 1 
ATOM   10202 N  N   . GLY J  1 28  ? 116.315 43.197  -2.706  1.00 44.70 ? 27  GLY J N   1 
ATOM   10203 C  CA  . GLY J  1 28  ? 117.402 43.913  -2.098  1.00 39.15 ? 27  GLY J CA  1 
ATOM   10204 C  C   . GLY J  1 28  ? 117.673 43.345  -0.734  1.00 36.20 ? 27  GLY J C   1 
ATOM   10205 O  O   . GLY J  1 28  ? 116.865 42.599  -0.171  1.00 36.96 ? 27  GLY J O   1 
ATOM   10206 N  N   . PRO J  1 29  ? 118.833 43.680  -0.197  1.00 33.41 ? 28  PRO J N   1 
ATOM   10207 C  CA  . PRO J  1 29  ? 119.073 43.740  1.236   1.00 31.10 ? 28  PRO J CA  1 
ATOM   10208 C  C   . PRO J  1 29  ? 118.005 44.441  2.049   1.00 28.01 ? 28  PRO J C   1 
ATOM   10209 O  O   . PRO J  1 29  ? 117.476 45.520  1.722   1.00 28.42 ? 28  PRO J O   1 
ATOM   10210 C  CB  . PRO J  1 29  ? 120.431 44.411  1.355   1.00 31.84 ? 28  PRO J CB  1 
ATOM   10211 C  CG  . PRO J  1 29  ? 120.586 45.129  0.014   1.00 32.70 ? 28  PRO J CG  1 
ATOM   10212 C  CD  . PRO J  1 29  ? 120.001 44.105  -0.951  1.00 31.48 ? 28  PRO J CD  1 
ATOM   10213 N  N   . VAL J  1 30  ? 117.777 43.717  3.123   1.00 25.53 ? 29  VAL J N   1 
ATOM   10214 C  CA  . VAL J  1 30  ? 116.848 44.135  4.130   1.00 23.26 ? 29  VAL J CA  1 
ATOM   10215 C  C   . VAL J  1 30  ? 117.682 44.370  5.384   1.00 22.01 ? 29  VAL J C   1 
ATOM   10216 O  O   . VAL J  1 30  ? 118.505 43.549  5.804   1.00 21.09 ? 29  VAL J O   1 
ATOM   10217 C  CB  . VAL J  1 30  ? 115.656 43.018  4.331   1.00 23.21 ? 29  VAL J CB  1 
ATOM   10218 C  CG1 . VAL J  1 30  ? 115.921 41.787  3.471   1.00 22.64 ? 29  VAL J CG1 1 
ATOM   10219 C  CG2 . VAL J  1 30  ? 115.482 42.601  5.790   1.00 20.85 ? 29  VAL J CG2 1 
ATOM   10220 N  N   . LYS J  1 31  ? 117.486 45.577  5.906   1.00 20.35 ? 30  LYS J N   1 
ATOM   10221 C  CA  . LYS J  1 31  ? 118.107 46.005  7.140   1.00 20.23 ? 30  LYS J CA  1 
ATOM   10222 C  C   . LYS J  1 31  ? 117.237 45.525  8.283   1.00 18.30 ? 30  LYS J C   1 
ATOM   10223 O  O   . LYS J  1 31  ? 116.021 45.720  8.217   1.00 19.74 ? 30  LYS J O   1 
ATOM   10224 C  CB  . LYS J  1 31  ? 118.163 47.505  7.303   1.00 23.12 ? 30  LYS J CB  1 
ATOM   10225 C  CG  . LYS J  1 31  ? 118.683 48.342  6.146   1.00 29.90 ? 30  LYS J CG  1 
ATOM   10226 C  CD  . LYS J  1 31  ? 119.069 49.737  6.669   1.00 32.92 ? 30  LYS J CD  1 
ATOM   10227 C  CE  . LYS J  1 31  ? 120.609 49.917  6.773   1.00 36.42 ? 30  LYS J CE  1 
ATOM   10228 N  NZ  . LYS J  1 31  ? 120.948 51.252  7.282   1.00 40.97 ? 30  LYS J NZ  1 
ATOM   10229 N  N   . VAL J  1 32  ? 117.771 44.920  9.333   1.00 14.10 ? 31  VAL J N   1 
ATOM   10230 C  CA  . VAL J  1 32  ? 116.934 44.562  10.439  1.00 10.84 ? 31  VAL J CA  1 
ATOM   10231 C  C   . VAL J  1 32  ? 117.640 45.289  11.568  1.00 11.83 ? 31  VAL J C   1 
ATOM   10232 O  O   . VAL J  1 32  ? 118.844 45.143  11.863  1.00 12.39 ? 31  VAL J O   1 
ATOM   10233 C  CB  . VAL J  1 32  ? 116.804 42.949  10.639  1.00 8.29  ? 31  VAL J CB  1 
ATOM   10234 C  CG1 . VAL J  1 32  ? 117.473 42.205  9.513   1.00 6.11  ? 31  VAL J CG1 1 
ATOM   10235 C  CG2 . VAL J  1 32  ? 117.352 42.493  11.937  1.00 5.82  ? 31  VAL J CG2 1 
ATOM   10236 N  N   . TRP J  1 33  ? 116.887 46.186  12.174  1.00 12.31 ? 32  TRP J N   1 
ATOM   10237 C  CA  . TRP J  1 33  ? 117.422 46.968  13.262  1.00 13.92 ? 32  TRP J CA  1 
ATOM   10238 C  C   . TRP J  1 33  ? 116.408 46.985  14.398  1.00 14.63 ? 32  TRP J C   1 
ATOM   10239 O  O   . TRP J  1 33  ? 115.267 46.602  14.176  1.00 15.60 ? 32  TRP J O   1 
ATOM   10240 C  CB  . TRP J  1 33  ? 117.743 48.411  12.747  1.00 14.55 ? 32  TRP J CB  1 
ATOM   10241 C  CG  . TRP J  1 33  ? 116.582 49.358  12.502  1.00 13.83 ? 32  TRP J CG  1 
ATOM   10242 C  CD1 . TRP J  1 33  ? 116.135 50.168  13.514  1.00 14.44 ? 32  TRP J CD1 1 
ATOM   10243 C  CD2 . TRP J  1 33  ? 115.844 49.495  11.337  1.00 14.84 ? 32  TRP J CD2 1 
ATOM   10244 N  NE1 . TRP J  1 33  ? 115.102 50.816  13.006  1.00 17.22 ? 32  TRP J NE1 1 
ATOM   10245 C  CE2 . TRP J  1 33  ? 114.894 50.451  11.718  1.00 14.75 ? 32  TRP J CE2 1 
ATOM   10246 C  CE3 . TRP J  1 33  ? 115.821 48.979  10.057  1.00 14.02 ? 32  TRP J CE3 1 
ATOM   10247 C  CZ2 . TRP J  1 33  ? 113.914 50.889  10.842  1.00 13.26 ? 32  TRP J CZ2 1 
ATOM   10248 C  CZ3 . TRP J  1 33  ? 114.838 49.426  9.189   1.00 15.30 ? 32  TRP J CZ3 1 
ATOM   10249 C  CH2 . TRP J  1 33  ? 113.897 50.367  9.567   1.00 13.48 ? 32  TRP J CH2 1 
ATOM   10250 N  N   . GLY J  1 34  ? 116.714 47.410  15.617  1.00 14.51 ? 33  GLY J N   1 
ATOM   10251 C  CA  . GLY J  1 34  ? 115.736 47.480  16.696  1.00 12.74 ? 33  GLY J CA  1 
ATOM   10252 C  C   . GLY J  1 34  ? 116.500 47.353  17.998  1.00 12.42 ? 33  GLY J C   1 
ATOM   10253 O  O   . GLY J  1 34  ? 117.734 47.312  17.971  1.00 11.49 ? 33  GLY J O   1 
ATOM   10254 N  N   . SER J  1 35  ? 115.821 47.225  19.118  1.00 12.50 ? 34  SER J N   1 
ATOM   10255 C  CA  . SER J  1 35  ? 116.460 47.175  20.422  1.00 15.20 ? 34  SER J CA  1 
ATOM   10256 C  C   . SER J  1 35  ? 115.794 46.054  21.161  1.00 14.82 ? 34  SER J C   1 
ATOM   10257 O  O   . SER J  1 35  ? 114.585 45.882  20.966  1.00 18.57 ? 34  SER J O   1 
ATOM   10258 C  CB  . SER J  1 35  ? 116.238 48.501  21.153  1.00 16.94 ? 34  SER J CB  1 
ATOM   10259 O  OG  . SER J  1 35  ? 116.316 48.504  22.582  1.00 17.55 ? 34  SER J OG  1 
ATOM   10260 N  N   . ILE J  1 36  ? 116.495 45.310  21.991  1.00 12.44 ? 35  ILE J N   1 
ATOM   10261 C  CA  . ILE J  1 36  ? 115.877 44.231  22.735  1.00 13.06 ? 35  ILE J CA  1 
ATOM   10262 C  C   . ILE J  1 36  ? 116.375 44.457  24.151  1.00 14.02 ? 35  ILE J C   1 
ATOM   10263 O  O   . ILE J  1 36  ? 117.531 44.826  24.295  1.00 15.16 ? 35  ILE J O   1 
ATOM   10264 C  CB  . ILE J  1 36  ? 116.343 42.878  22.206  1.00 12.34 ? 35  ILE J CB  1 
ATOM   10265 C  CG1 . ILE J  1 36  ? 115.895 42.666  20.763  1.00 12.88 ? 35  ILE J CG1 1 
ATOM   10266 C  CG2 . ILE J  1 36  ? 115.764 41.797  23.086  1.00 11.59 ? 35  ILE J CG2 1 
ATOM   10267 C  CD1 . ILE J  1 36  ? 116.545 41.406  20.114  1.00 11.66 ? 35  ILE J CD1 1 
ATOM   10268 N  N   . LYS J  1 37  ? 115.609 44.313  25.226  1.00 15.94 ? 36  LYS J N   1 
ATOM   10269 C  CA  . LYS J  1 37  ? 116.128 44.544  26.563  1.00 15.71 ? 36  LYS J CA  1 
ATOM   10270 C  C   . LYS J  1 37  ? 115.753 43.368  27.382  1.00 13.18 ? 36  LYS J C   1 
ATOM   10271 O  O   . LYS J  1 37  ? 114.861 42.607  27.020  1.00 13.86 ? 36  LYS J O   1 
ATOM   10272 C  CB  . LYS J  1 37  ? 115.549 45.764  27.286  1.00 17.69 ? 36  LYS J CB  1 
ATOM   10273 C  CG  . LYS J  1 37  ? 114.281 46.385  26.745  1.00 20.92 ? 36  LYS J CG  1 
ATOM   10274 C  CD  . LYS J  1 37  ? 114.559 47.399  25.627  1.00 24.26 ? 36  LYS J CD  1 
ATOM   10275 C  CE  . LYS J  1 37  ? 115.055 48.777  26.119  1.00 25.97 ? 36  LYS J CE  1 
ATOM   10276 N  NZ  . LYS J  1 37  ? 116.466 48.786  26.474  1.00 25.08 ? 36  LYS J NZ  1 
ATOM   10277 N  N   . GLY J  1 38  ? 116.554 43.248  28.416  1.00 12.42 ? 37  GLY J N   1 
ATOM   10278 C  CA  . GLY J  1 38  ? 116.369 42.237  29.435  1.00 15.20 ? 37  GLY J CA  1 
ATOM   10279 C  C   . GLY J  1 38  ? 117.084 40.912  29.176  1.00 16.14 ? 37  GLY J C   1 
ATOM   10280 O  O   . GLY J  1 38  ? 116.708 39.875  29.719  1.00 17.10 ? 37  GLY J O   1 
ATOM   10281 N  N   . LEU J  1 39  ? 118.141 40.957  28.359  1.00 19.42 ? 38  LEU J N   1 
ATOM   10282 C  CA  . LEU J  1 39  ? 118.990 39.825  27.936  1.00 16.71 ? 38  LEU J CA  1 
ATOM   10283 C  C   . LEU J  1 39  ? 120.235 39.759  28.822  1.00 17.46 ? 38  LEU J C   1 
ATOM   10284 O  O   . LEU J  1 39  ? 120.552 40.750  29.491  1.00 16.90 ? 38  LEU J O   1 
ATOM   10285 C  CB  . LEU J  1 39  ? 119.434 40.059  26.503  1.00 14.43 ? 38  LEU J CB  1 
ATOM   10286 C  CG  . LEU J  1 39  ? 118.448 40.059  25.338  1.00 12.44 ? 38  LEU J CG  1 
ATOM   10287 C  CD1 . LEU J  1 39  ? 119.070 40.842  24.186  1.00 10.77 ? 38  LEU J CD1 1 
ATOM   10288 C  CD2 . LEU J  1 39  ? 118.107 38.630  24.933  1.00 11.26 ? 38  LEU J CD2 1 
ATOM   10289 N  N   . THR J  1 40  ? 121.004 38.673  28.933  1.00 17.58 ? 39  THR J N   1 
ATOM   10290 C  CA  . THR J  1 40  ? 122.276 38.831  29.606  1.00 17.36 ? 39  THR J CA  1 
ATOM   10291 C  C   . THR J  1 40  ? 123.240 39.401  28.582  1.00 18.08 ? 39  THR J C   1 
ATOM   10292 O  O   . THR J  1 40  ? 123.048 39.299  27.364  1.00 18.95 ? 39  THR J O   1 
ATOM   10293 C  CB  . THR J  1 40  ? 122.800 37.521  30.096  1.00 18.26 ? 39  THR J CB  1 
ATOM   10294 O  OG1 . THR J  1 40  ? 121.689 36.913  30.726  1.00 17.40 ? 39  THR J OG1 1 
ATOM   10295 C  CG2 . THR J  1 40  ? 123.953 37.660  31.112  1.00 19.91 ? 39  THR J CG2 1 
ATOM   10296 N  N   . GLU J  1 41  ? 124.252 40.061  29.106  1.00 19.49 ? 40  GLU J N   1 
ATOM   10297 C  CA  . GLU J  1 41  ? 125.323 40.659  28.347  1.00 19.81 ? 40  GLU J CA  1 
ATOM   10298 C  C   . GLU J  1 41  ? 126.044 39.545  27.602  1.00 17.83 ? 40  GLU J C   1 
ATOM   10299 O  O   . GLU J  1 41  ? 126.224 38.442  28.133  1.00 20.10 ? 40  GLU J O   1 
ATOM   10300 C  CB  . GLU J  1 41  ? 126.171 41.358  29.381  1.00 23.01 ? 40  GLU J CB  1 
ATOM   10301 C  CG  . GLU J  1 41  ? 127.381 42.135  28.907  1.00 24.91 ? 40  GLU J CG  1 
ATOM   10302 C  CD  . GLU J  1 41  ? 128.669 41.759  29.628  1.00 27.18 ? 40  GLU J CD  1 
ATOM   10303 O  OE1 . GLU J  1 41  ? 128.617 41.371  30.808  1.00 26.60 ? 40  GLU J OE1 1 
ATOM   10304 O  OE2 . GLU J  1 41  ? 129.723 41.856  28.978  1.00 29.28 ? 40  GLU J OE2 1 
ATOM   10305 N  N   . GLY J  1 42  ? 126.400 39.801  26.352  1.00 15.00 ? 41  GLY J N   1 
ATOM   10306 C  CA  . GLY J  1 42  ? 127.040 38.812  25.510  1.00 11.93 ? 41  GLY J CA  1 
ATOM   10307 C  C   . GLY J  1 42  ? 126.254 38.483  24.241  1.00 10.87 ? 41  GLY J C   1 
ATOM   10308 O  O   . GLY J  1 42  ? 125.396 39.247  23.767  1.00 9.98  ? 41  GLY J O   1 
ATOM   10309 N  N   . LEU J  1 43  ? 126.491 37.284  23.707  1.00 10.34 ? 42  LEU J N   1 
ATOM   10310 C  CA  . LEU J  1 43  ? 125.953 36.955  22.395  1.00 8.40  ? 42  LEU J CA  1 
ATOM   10311 C  C   . LEU J  1 43  ? 124.723 36.127  22.515  1.00 8.05  ? 42  LEU J C   1 
ATOM   10312 O  O   . LEU J  1 43  ? 124.629 35.330  23.462  1.00 10.75 ? 42  LEU J O   1 
ATOM   10313 C  CB  . LEU J  1 43  ? 126.954 36.207  21.589  1.00 3.92  ? 42  LEU J CB  1 
ATOM   10314 C  CG  . LEU J  1 43  ? 128.190 36.950  21.152  1.00 4.56  ? 42  LEU J CG  1 
ATOM   10315 C  CD1 . LEU J  1 43  ? 129.029 35.950  20.424  1.00 2.03  ? 42  LEU J CD1 1 
ATOM   10316 C  CD2 . LEU J  1 43  ? 127.875 38.183  20.281  1.00 3.71  ? 42  LEU J CD2 1 
ATOM   10317 N  N   . HIS J  1 44  ? 123.766 36.366  21.620  1.00 6.13  ? 43  HIS J N   1 
ATOM   10318 C  CA  . HIS J  1 44  ? 122.512 35.639  21.675  1.00 6.64  ? 43  HIS J CA  1 
ATOM   10319 C  C   . HIS J  1 44  ? 122.101 35.308  20.273  1.00 7.63  ? 43  HIS J C   1 
ATOM   10320 O  O   . HIS J  1 44  ? 122.111 36.199  19.421  1.00 10.67 ? 43  HIS J O   1 
ATOM   10321 C  CB  . HIS J  1 44  ? 121.364 36.451  22.271  1.00 6.24  ? 43  HIS J CB  1 
ATOM   10322 C  CG  . HIS J  1 44  ? 121.512 36.693  23.743  1.00 8.67  ? 43  HIS J CG  1 
ATOM   10323 N  ND1 . HIS J  1 44  ? 120.922 36.022  24.714  1.00 12.02 ? 43  HIS J ND1 1 
ATOM   10324 C  CD2 . HIS J  1 44  ? 122.422 37.554  24.312  1.00 9.56  ? 43  HIS J CD2 1 
ATOM   10325 C  CE1 . HIS J  1 44  ? 121.456 36.411  25.849  1.00 10.77 ? 43  HIS J CE1 1 
ATOM   10326 N  NE2 . HIS J  1 44  ? 122.344 37.321  25.592  1.00 10.57 ? 43  HIS J NE2 1 
ATOM   10327 N  N   . GLY J  1 45  ? 121.710 34.075  20.001  1.00 6.05  ? 44  GLY J N   1 
ATOM   10328 C  CA  . GLY J  1 45  ? 121.250 33.736  18.673  1.00 4.78  ? 44  GLY J CA  1 
ATOM   10329 C  C   . GLY J  1 45  ? 120.029 34.528  18.279  1.00 3.65  ? 44  GLY J C   1 
ATOM   10330 O  O   . GLY J  1 45  ? 119.143 34.754  19.087  1.00 6.40  ? 44  GLY J O   1 
ATOM   10331 N  N   . PHE J  1 46  ? 119.944 34.915  17.033  1.00 3.62  ? 45  PHE J N   1 
ATOM   10332 C  CA  . PHE J  1 46  ? 118.874 35.734  16.517  1.00 2.57  ? 45  PHE J CA  1 
ATOM   10333 C  C   . PHE J  1 46  ? 118.543 34.937  15.265  1.00 3.14  ? 45  PHE J C   1 
ATOM   10334 O  O   . PHE J  1 46  ? 119.435 34.662  14.457  1.00 2.01  ? 45  PHE J O   1 
ATOM   10335 C  CB  . PHE J  1 46  ? 119.461 37.146  16.215  1.00 2.00  ? 45  PHE J CB  1 
ATOM   10336 C  CG  . PHE J  1 46  ? 118.487 38.280  15.936  1.00 2.00  ? 45  PHE J CG  1 
ATOM   10337 C  CD1 . PHE J  1 46  ? 117.480 38.608  16.837  1.00 2.45  ? 45  PHE J CD1 1 
ATOM   10338 C  CD2 . PHE J  1 46  ? 118.601 38.994  14.754  1.00 6.89  ? 45  PHE J CD2 1 
ATOM   10339 C  CE1 . PHE J  1 46  ? 116.597 39.630  16.568  1.00 2.00  ? 45  PHE J CE1 1 
ATOM   10340 C  CE2 . PHE J  1 46  ? 117.708 40.027  14.476  1.00 5.41  ? 45  PHE J CE2 1 
ATOM   10341 C  CZ  . PHE J  1 46  ? 116.716 40.335  15.382  1.00 6.79  ? 45  PHE J CZ  1 
ATOM   10342 N  N   . HIS J  1 47  ? 117.313 34.478  15.054  1.00 3.04  ? 46  HIS J N   1 
ATOM   10343 C  CA  . HIS J  1 47  ? 116.976 33.658  13.904  1.00 2.90  ? 46  HIS J CA  1 
ATOM   10344 C  C   . HIS J  1 47  ? 115.491 33.862  13.648  1.00 2.94  ? 46  HIS J C   1 
ATOM   10345 O  O   . HIS J  1 47  ? 114.760 34.209  14.587  1.00 2.00  ? 46  HIS J O   1 
ATOM   10346 C  CB  . HIS J  1 47  ? 117.132 32.129  14.133  1.00 4.41  ? 46  HIS J CB  1 
ATOM   10347 C  CG  . HIS J  1 47  ? 118.311 31.554  14.911  1.00 3.46  ? 46  HIS J CG  1 
ATOM   10348 N  ND1 . HIS J  1 47  ? 118.283 30.727  15.956  1.00 5.52  ? 46  HIS J ND1 1 
ATOM   10349 C  CD2 . HIS J  1 47  ? 119.625 31.817  14.643  1.00 2.04  ? 46  HIS J CD2 1 
ATOM   10350 C  CE1 . HIS J  1 47  ? 119.522 30.502  16.321  1.00 5.51  ? 46  HIS J CE1 1 
ATOM   10351 N  NE2 . HIS J  1 47  ? 120.333 31.165  15.529  1.00 3.64  ? 46  HIS J NE2 1 
ATOM   10352 N  N   . VAL J  1 48  ? 115.061 33.615  12.399  1.00 4.47  ? 47  VAL J N   1 
ATOM   10353 C  CA  . VAL J  1 48  ? 113.660 33.569  11.953  1.00 6.21  ? 47  VAL J CA  1 
ATOM   10354 C  C   . VAL J  1 48  ? 113.291 32.084  11.978  1.00 6.54  ? 47  VAL J C   1 
ATOM   10355 O  O   . VAL J  1 48  ? 113.942 31.260  11.297  1.00 6.30  ? 47  VAL J O   1 
ATOM   10356 C  CB  . VAL J  1 48  ? 113.429 34.036  10.478  1.00 7.36  ? 47  VAL J CB  1 
ATOM   10357 C  CG1 . VAL J  1 48  ? 111.930 34.024  10.148  1.00 8.16  ? 47  VAL J CG1 1 
ATOM   10358 C  CG2 . VAL J  1 48  ? 113.884 35.474  10.289  1.00 6.24  ? 47  VAL J CG2 1 
ATOM   10359 N  N   . HIS J  1 49  ? 112.319 31.708  12.812  1.00 5.29  ? 48  HIS J N   1 
ATOM   10360 C  CA  . HIS J  1 49  ? 111.811 30.346  12.851  1.00 5.21  ? 48  HIS J CA  1 
ATOM   10361 C  C   . HIS J  1 49  ? 110.592 30.260  11.918  1.00 5.58  ? 48  HIS J C   1 
ATOM   10362 O  O   . HIS J  1 49  ? 110.012 31.286  11.538  1.00 5.26  ? 48  HIS J O   1 
ATOM   10363 C  CB  . HIS J  1 49  ? 111.431 29.990  14.262  1.00 6.92  ? 48  HIS J CB  1 
ATOM   10364 C  CG  . HIS J  1 49  ? 112.592 29.680  15.194  1.00 6.37  ? 48  HIS J CG  1 
ATOM   10365 N  ND1 . HIS J  1 49  ? 112.732 28.623  15.963  1.00 6.02  ? 48  HIS J ND1 1 
ATOM   10366 C  CD2 . HIS J  1 49  ? 113.687 30.489  15.399  1.00 7.23  ? 48  HIS J CD2 1 
ATOM   10367 C  CE1 . HIS J  1 49  ? 113.862 28.776  16.604  1.00 7.82  ? 48  HIS J CE1 1 
ATOM   10368 N  NE2 . HIS J  1 49  ? 114.461 29.909  16.273  1.00 8.32  ? 48  HIS J NE2 1 
ATOM   10369 N  N   . GLU J  1 50  ? 110.138 29.071  11.552  1.00 4.05  ? 49  GLU J N   1 
ATOM   10370 C  CA  . GLU J  1 50  ? 109.182 28.867  10.468  1.00 6.85  ? 49  GLU J CA  1 
ATOM   10371 C  C   . GLU J  1 50  ? 107.736 29.377  10.479  1.00 8.26  ? 49  GLU J C   1 
ATOM   10372 O  O   . GLU J  1 50  ? 107.156 29.786  9.467   1.00 6.92  ? 49  GLU J O   1 
ATOM   10373 C  CB  . GLU J  1 50  ? 109.176 27.368  10.210  1.00 8.55  ? 49  GLU J CB  1 
ATOM   10374 C  CG  . GLU J  1 50  ? 108.611 26.941  8.869   1.00 12.92 ? 49  GLU J CG  1 
ATOM   10375 C  CD  . GLU J  1 50  ? 108.825 25.465  8.509   1.00 14.23 ? 49  GLU J CD  1 
ATOM   10376 O  OE1 . GLU J  1 50  ? 109.697 24.807  9.080   1.00 16.05 ? 49  GLU J OE1 1 
ATOM   10377 O  OE2 . GLU J  1 50  ? 108.119 24.978  7.629   1.00 12.24 ? 49  GLU J OE2 1 
ATOM   10378 N  N   . PHE J  1 51  ? 107.098 29.294  11.624  1.00 8.11  ? 50  PHE J N   1 
ATOM   10379 C  CA  . PHE J  1 51  ? 105.703 29.566  11.709  1.00 7.28  ? 50  PHE J CA  1 
ATOM   10380 C  C   . PHE J  1 51  ? 105.588 30.709  12.642  1.00 7.45  ? 50  PHE J C   1 
ATOM   10381 O  O   . PHE J  1 51  ? 106.344 30.846  13.609  1.00 5.62  ? 50  PHE J O   1 
ATOM   10382 C  CB  . PHE J  1 51  ? 104.950 28.383  12.295  1.00 8.41  ? 50  PHE J CB  1 
ATOM   10383 C  CG  . PHE J  1 51  ? 105.271 27.079  11.627  1.00 8.66  ? 50  PHE J CG  1 
ATOM   10384 C  CD1 . PHE J  1 51  ? 104.940 26.867  10.300  1.00 10.57 ? 50  PHE J CD1 1 
ATOM   10385 C  CD2 . PHE J  1 51  ? 105.905 26.109  12.358  1.00 12.20 ? 50  PHE J CD2 1 
ATOM   10386 C  CE1 . PHE J  1 51  ? 105.239 25.673  9.678   1.00 10.88 ? 50  PHE J CE1 1 
ATOM   10387 C  CE2 . PHE J  1 51  ? 106.202 24.908  11.729  1.00 14.65 ? 50  PHE J CE2 1 
ATOM   10388 C  CZ  . PHE J  1 51  ? 105.874 24.691  10.398  1.00 12.08 ? 50  PHE J CZ  1 
ATOM   10389 N  N   . GLY J  1 52  ? 104.510 31.407  12.333  1.00 8.69  ? 51  GLY J N   1 
ATOM   10390 C  CA  . GLY J  1 52  ? 104.019 32.512  13.139  1.00 10.72 ? 51  GLY J CA  1 
ATOM   10391 C  C   . GLY J  1 52  ? 102.919 32.010  14.077  1.00 12.48 ? 51  GLY J C   1 
ATOM   10392 O  O   . GLY J  1 52  ? 101.942 32.707  14.366  1.00 9.97  ? 51  GLY J O   1 
ATOM   10393 N  N   . ASP J  1 53  ? 103.075 30.748  14.478  1.00 12.61 ? 52  ASP J N   1 
ATOM   10394 C  CA  . ASP J  1 53  ? 102.190 30.028  15.354  1.00 15.60 ? 52  ASP J CA  1 
ATOM   10395 C  C   . ASP J  1 53  ? 102.671 30.401  16.756  1.00 19.70 ? 52  ASP J C   1 
ATOM   10396 O  O   . ASP J  1 53  ? 103.417 29.642  17.401  1.00 19.07 ? 52  ASP J O   1 
ATOM   10397 C  CB  . ASP J  1 53  ? 102.382 28.542  15.086  1.00 16.05 ? 52  ASP J CB  1 
ATOM   10398 C  CG  . ASP J  1 53  ? 101.335 27.513  15.517  1.00 16.61 ? 52  ASP J CG  1 
ATOM   10399 O  OD1 . ASP J  1 53  ? 100.777 27.549  16.635  1.00 11.23 ? 52  ASP J OD1 1 
ATOM   10400 O  OD2 . ASP J  1 53  ? 101.121 26.644  14.665  1.00 16.15 ? 52  ASP J OD2 1 
ATOM   10401 N  N   . ASN J  1 54  ? 102.340 31.542  17.341  1.00 22.16 ? 53  ASN J N   1 
ATOM   10402 C  CA  . ASN J  1 54  ? 102.856 31.728  18.675  1.00 24.64 ? 53  ASN J CA  1 
ATOM   10403 C  C   . ASN J  1 54  ? 101.717 31.541  19.625  1.00 24.33 ? 53  ASN J C   1 
ATOM   10404 O  O   . ASN J  1 54  ? 101.349 32.362  20.458  1.00 25.33 ? 53  ASN J O   1 
ATOM   10405 C  CB  . ASN J  1 54  ? 103.546 33.098  18.792  1.00 28.24 ? 53  ASN J CB  1 
ATOM   10406 C  CG  . ASN J  1 54  ? 104.912 33.027  18.080  1.00 32.58 ? 53  ASN J CG  1 
ATOM   10407 O  OD1 . ASN J  1 54  ? 105.325 33.973  17.387  1.00 34.64 ? 53  ASN J OD1 1 
ATOM   10408 N  ND2 . ASN J  1 54  ? 105.714 31.951  18.171  1.00 35.62 ? 53  ASN J ND2 1 
ATOM   10409 N  N   . THR J  1 55  ? 101.274 30.299  19.490  1.00 22.84 ? 54  THR J N   1 
ATOM   10410 C  CA  . THR J  1 55  ? 100.139 29.771  20.219  1.00 23.51 ? 54  THR J CA  1 
ATOM   10411 C  C   . THR J  1 55  ? 100.579 29.168  21.546  1.00 24.14 ? 54  THR J C   1 
ATOM   10412 O  O   . THR J  1 55  ? 100.001 29.507  22.574  1.00 26.89 ? 54  THR J O   1 
ATOM   10413 C  CB  . THR J  1 55  ? 99.517  28.827  19.182  1.00 22.71 ? 54  THR J CB  1 
ATOM   10414 O  OG1 . THR J  1 55  ? 98.559  29.684  18.558  1.00 21.55 ? 54  THR J OG1 1 
ATOM   10415 C  CG2 . THR J  1 55  ? 98.962  27.511  19.685  1.00 21.55 ? 54  THR J CG2 1 
ATOM   10416 N  N   . ALA J  1 56  ? 101.603 28.306  21.561  1.00 24.26 ? 55  ALA J N   1 
ATOM   10417 C  CA  . ALA J  1 56  ? 102.219 27.765  22.764  1.00 22.93 ? 55  ALA J CA  1 
ATOM   10418 C  C   . ALA J  1 56  ? 103.531 28.548  22.941  1.00 24.10 ? 55  ALA J C   1 
ATOM   10419 O  O   . ALA J  1 56  ? 104.656 28.020  23.084  1.00 24.31 ? 55  ALA J O   1 
ATOM   10420 C  CB  . ALA J  1 56  ? 102.539 26.290  22.570  1.00 22.68 ? 55  ALA J CB  1 
ATOM   10421 N  N   . GLY J  1 57  ? 103.409 29.874  22.859  1.00 22.59 ? 56  GLY J N   1 
ATOM   10422 C  CA  . GLY J  1 57  ? 104.569 30.730  23.019  1.00 21.93 ? 56  GLY J CA  1 
ATOM   10423 C  C   . GLY J  1 57  ? 105.536 30.560  21.864  1.00 20.81 ? 56  GLY J C   1 
ATOM   10424 O  O   . GLY J  1 57  ? 105.146 30.309  20.707  1.00 22.16 ? 56  GLY J O   1 
ATOM   10425 N  N   . CYS J  1 58  ? 106.814 30.607  22.232  1.00 18.52 ? 57  CYS J N   1 
ATOM   10426 C  CA  . CYS J  1 58  ? 107.848 30.565  21.229  1.00 15.43 ? 57  CYS J CA  1 
ATOM   10427 C  C   . CYS J  1 58  ? 108.044 29.227  20.600  1.00 14.51 ? 57  CYS J C   1 
ATOM   10428 O  O   . CYS J  1 58  ? 108.360 29.144  19.419  1.00 15.12 ? 57  CYS J O   1 
ATOM   10429 C  CB  . CYS J  1 58  ? 109.135 31.021  21.842  1.00 15.06 ? 57  CYS J CB  1 
ATOM   10430 S  SG  . CYS J  1 58  ? 109.001 32.784  22.213  1.00 12.78 ? 57  CYS J SG  1 
ATOM   10431 N  N   . THR J  1 59  ? 107.796 28.187  21.379  1.00 15.56 ? 58  THR J N   1 
ATOM   10432 C  CA  . THR J  1 59  ? 107.981 26.805  20.971  1.00 15.31 ? 58  THR J CA  1 
ATOM   10433 C  C   . THR J  1 59  ? 107.218 26.444  19.715  1.00 15.26 ? 58  THR J C   1 
ATOM   10434 O  O   . THR J  1 59  ? 107.768 25.850  18.785  1.00 17.43 ? 58  THR J O   1 
ATOM   10435 C  CB  . THR J  1 59  ? 107.569 25.917  22.130  1.00 16.81 ? 58  THR J CB  1 
ATOM   10436 O  OG1 . THR J  1 59  ? 108.057 26.439  23.384  1.00 20.99 ? 58  THR J OG1 1 
ATOM   10437 C  CG2 . THR J  1 59  ? 108.184 24.573  21.911  1.00 19.71 ? 58  THR J CG2 1 
ATOM   10438 N  N   . SER J  1 60  ? 105.980 26.887  19.601  1.00 14.60 ? 59  SER J N   1 
ATOM   10439 C  CA  . SER J  1 60  ? 105.230 26.662  18.379  1.00 12.86 ? 59  SER J CA  1 
ATOM   10440 C  C   . SER J  1 60  ? 105.711 27.404  17.127  1.00 11.03 ? 59  SER J C   1 
ATOM   10441 O  O   . SER J  1 60  ? 105.070 27.323  16.073  1.00 9.38  ? 59  SER J O   1 
ATOM   10442 C  CB  . SER J  1 60  ? 103.766 26.982  18.678  1.00 13.60 ? 59  SER J CB  1 
ATOM   10443 O  OG  . SER J  1 60  ? 103.684 27.932  19.734  1.00 18.41 ? 59  SER J OG  1 
ATOM   10444 N  N   . ALA J  1 61  ? 106.855 28.099  17.192  1.00 10.45 ? 60  ALA J N   1 
ATOM   10445 C  CA  . ALA J  1 61  ? 107.372 28.805  16.021  1.00 12.28 ? 60  ALA J CA  1 
ATOM   10446 C  C   . ALA J  1 61  ? 108.003 27.827  15.056  1.00 12.91 ? 60  ALA J C   1 
ATOM   10447 O  O   . ALA J  1 61  ? 108.281 28.133  13.897  1.00 15.65 ? 60  ALA J O   1 
ATOM   10448 C  CB  . ALA J  1 61  ? 108.444 29.802  16.375  1.00 9.93  ? 60  ALA J CB  1 
ATOM   10449 N  N   . GLY J  1 62  ? 108.293 26.615  15.514  1.00 14.20 ? 61  GLY J N   1 
ATOM   10450 C  CA  . GLY J  1 62  ? 108.883 25.607  14.657  1.00 12.58 ? 61  GLY J CA  1 
ATOM   10451 C  C   . GLY J  1 62  ? 110.395 25.773  14.590  1.00 12.78 ? 61  GLY J C   1 
ATOM   10452 O  O   . GLY J  1 62  ? 110.978 26.479  15.427  1.00 15.23 ? 61  GLY J O   1 
ATOM   10453 N  N   . PRO J  1 63  ? 111.102 25.151  13.630  1.00 11.46 ? 62  PRO J N   1 
ATOM   10454 C  CA  . PRO J  1 63  ? 112.552 25.182  13.553  1.00 8.54  ? 62  PRO J CA  1 
ATOM   10455 C  C   . PRO J  1 63  ? 112.958 26.439  12.798  1.00 8.06  ? 62  PRO J C   1 
ATOM   10456 O  O   . PRO J  1 63  ? 112.101 27.280  12.492  1.00 9.88  ? 62  PRO J O   1 
ATOM   10457 C  CB  . PRO J  1 63  ? 112.822 23.852  12.873  1.00 6.16  ? 62  PRO J CB  1 
ATOM   10458 C  CG  . PRO J  1 63  ? 111.756 23.837  11.809  1.00 5.55  ? 62  PRO J CG  1 
ATOM   10459 C  CD  . PRO J  1 63  ? 110.541 24.324  12.552  1.00 8.26  ? 62  PRO J CD  1 
ATOM   10460 N  N   . HIS J  1 64  ? 114.231 26.609  12.432  1.00 6.77  ? 63  HIS J N   1 
ATOM   10461 C  CA  . HIS J  1 64  ? 114.620 27.765  11.667  1.00 4.30  ? 63  HIS J CA  1 
ATOM   10462 C  C   . HIS J  1 64  ? 114.010 27.595  10.268  1.00 5.75  ? 63  HIS J C   1 
ATOM   10463 O  O   . HIS J  1 64  ? 113.837 26.482  9.737   1.00 4.87  ? 63  HIS J O   1 
ATOM   10464 C  CB  . HIS J  1 64  ? 116.124 27.843  11.576  1.00 4.12  ? 63  HIS J CB  1 
ATOM   10465 C  CG  . HIS J  1 64  ? 116.895 28.065  12.868  1.00 4.43  ? 63  HIS J CG  1 
ATOM   10466 N  ND1 . HIS J  1 64  ? 118.171 27.765  13.079  1.00 6.04  ? 63  HIS J ND1 1 
ATOM   10467 C  CD2 . HIS J  1 64  ? 116.378 28.618  14.018  1.00 8.19  ? 63  HIS J CD2 1 
ATOM   10468 C  CE1 . HIS J  1 64  ? 118.408 28.136  14.328  1.00 8.72  ? 63  HIS J CE1 1 
ATOM   10469 N  NE2 . HIS J  1 64  ? 117.328 28.660  14.918  1.00 12.79 ? 63  HIS J NE2 1 
ATOM   10470 N  N   . PHE J  1 65  ? 113.624 28.753  9.723   1.00 5.64  ? 64  PHE J N   1 
ATOM   10471 C  CA  . PHE J  1 65  ? 113.051 28.902  8.412   1.00 3.42  ? 64  PHE J CA  1 
ATOM   10472 C  C   . PHE J  1 65  ? 114.189 28.528  7.494   1.00 6.95  ? 64  PHE J C   1 
ATOM   10473 O  O   . PHE J  1 65  ? 115.306 29.082  7.532   1.00 8.43  ? 64  PHE J O   1 
ATOM   10474 C  CB  . PHE J  1 65  ? 112.625 30.323  8.269   1.00 2.30  ? 64  PHE J CB  1 
ATOM   10475 C  CG  . PHE J  1 65  ? 112.048 30.628  6.918   1.00 5.04  ? 64  PHE J CG  1 
ATOM   10476 C  CD1 . PHE J  1 65  ? 111.134 29.780  6.339   1.00 4.65  ? 64  PHE J CD1 1 
ATOM   10477 C  CD2 . PHE J  1 65  ? 112.464 31.769  6.264   1.00 6.96  ? 64  PHE J CD2 1 
ATOM   10478 C  CE1 . PHE J  1 65  ? 110.675 30.051  5.081   1.00 4.75  ? 64  PHE J CE1 1 
ATOM   10479 C  CE2 . PHE J  1 65  ? 112.002 32.039  4.997   1.00 7.80  ? 64  PHE J CE2 1 
ATOM   10480 C  CZ  . PHE J  1 65  ? 111.096 31.190  4.419   1.00 7.72  ? 64  PHE J CZ  1 
ATOM   10481 N  N   . ASN J  1 66  ? 113.820 27.460  6.771   1.00 11.67 ? 65  ASN J N   1 
ATOM   10482 C  CA  . ASN J  1 66  ? 114.689 26.676  5.895   1.00 12.33 ? 65  ASN J CA  1 
ATOM   10483 C  C   . ASN J  1 66  ? 114.037 26.245  4.583   1.00 13.70 ? 65  ASN J C   1 
ATOM   10484 O  O   . ASN J  1 66  ? 113.882 25.037  4.403   1.00 15.15 ? 65  ASN J O   1 
ATOM   10485 C  CB  . ASN J  1 66  ? 115.153 25.428  6.672   1.00 11.01 ? 65  ASN J CB  1 
ATOM   10486 C  CG  . ASN J  1 66  ? 116.431 24.798  6.149   1.00 13.91 ? 65  ASN J CG  1 
ATOM   10487 O  OD1 . ASN J  1 66  ? 117.143 25.306  5.271   1.00 15.42 ? 65  ASN J OD1 1 
ATOM   10488 N  ND2 . ASN J  1 66  ? 116.808 23.646  6.686   1.00 16.55 ? 65  ASN J ND2 1 
ATOM   10489 N  N   . PRO J  1 67  ? 113.652 27.074  3.596   1.00 13.53 ? 66  PRO J N   1 
ATOM   10490 C  CA  . PRO J  1 67  ? 113.098 26.642  2.336   1.00 14.77 ? 66  PRO J CA  1 
ATOM   10491 C  C   . PRO J  1 67  ? 113.913 25.616  1.574   1.00 16.87 ? 66  PRO J C   1 
ATOM   10492 O  O   . PRO J  1 67  ? 113.318 24.782  0.880   1.00 17.52 ? 66  PRO J O   1 
ATOM   10493 C  CB  . PRO J  1 67  ? 112.937 27.886  1.509   1.00 11.88 ? 66  PRO J CB  1 
ATOM   10494 C  CG  . PRO J  1 67  ? 112.789 28.992  2.475   1.00 12.68 ? 66  PRO J CG  1 
ATOM   10495 C  CD  . PRO J  1 67  ? 113.758 28.530  3.561   1.00 16.49 ? 66  PRO J CD  1 
ATOM   10496 N  N   . LEU J  1 68  ? 115.260 25.708  1.706   1.00 18.84 ? 67  LEU J N   1 
ATOM   10497 C  CA  . LEU J  1 68  ? 116.227 24.976  0.875   1.00 18.64 ? 67  LEU J CA  1 
ATOM   10498 C  C   . LEU J  1 68  ? 116.893 23.768  1.520   1.00 19.99 ? 67  LEU J C   1 
ATOM   10499 O  O   . LEU J  1 68  ? 117.874 23.269  0.974   1.00 21.29 ? 67  LEU J O   1 
ATOM   10500 C  CB  . LEU J  1 68  ? 117.358 25.899  0.420   1.00 16.03 ? 67  LEU J CB  1 
ATOM   10501 C  CG  . LEU J  1 68  ? 117.138 27.337  -0.044  1.00 17.84 ? 67  LEU J CG  1 
ATOM   10502 C  CD1 . LEU J  1 68  ? 118.491 27.915  -0.437  1.00 17.87 ? 67  LEU J CD1 1 
ATOM   10503 C  CD2 . LEU J  1 68  ? 116.193 27.401  -1.240  1.00 17.84 ? 67  LEU J CD2 1 
ATOM   10504 N  N   . SER J  1 69  ? 116.440 23.288  2.685   1.00 21.07 ? 68  SER J N   1 
ATOM   10505 C  CA  . SER J  1 69  ? 117.046 22.158  3.387   1.00 21.67 ? 68  SER J CA  1 
ATOM   10506 C  C   . SER J  1 69  ? 118.573 22.169  3.563   1.00 21.43 ? 68  SER J C   1 
ATOM   10507 O  O   . SER J  1 69  ? 119.274 21.143  3.556   1.00 22.27 ? 68  SER J O   1 
ATOM   10508 C  CB  . SER J  1 69  ? 116.609 20.872  2.680   1.00 24.10 ? 68  SER J CB  1 
ATOM   10509 O  OG  . SER J  1 69  ? 115.183 20.785  2.618   1.00 28.14 ? 68  SER J OG  1 
ATOM   10510 N  N   . ARG J  1 70  ? 119.074 23.379  3.781   1.00 19.21 ? 69  ARG J N   1 
ATOM   10511 C  CA  . ARG J  1 70  ? 120.481 23.575  4.036   1.00 18.48 ? 69  ARG J CA  1 
ATOM   10512 C  C   . ARG J  1 70  ? 120.702 23.275  5.525   1.00 17.46 ? 69  ARG J C   1 
ATOM   10513 O  O   . ARG J  1 70  ? 119.752 23.066  6.295   1.00 17.39 ? 69  ARG J O   1 
ATOM   10514 C  CB  . ARG J  1 70  ? 120.881 25.022  3.731   1.00 19.16 ? 69  ARG J CB  1 
ATOM   10515 C  CG  . ARG J  1 70  ? 120.437 25.481  2.364   1.00 20.44 ? 69  ARG J CG  1 
ATOM   10516 C  CD  . ARG J  1 70  ? 121.343 25.026  1.264   1.00 22.36 ? 69  ARG J CD  1 
ATOM   10517 N  NE  . ARG J  1 70  ? 122.245 26.129  0.958   1.00 31.11 ? 69  ARG J NE  1 
ATOM   10518 C  CZ  . ARG J  1 70  ? 122.290 26.759  -0.244  1.00 33.50 ? 69  ARG J CZ  1 
ATOM   10519 N  NH1 . ARG J  1 70  ? 121.524 26.383  -1.292  1.00 32.70 ? 69  ARG J NH1 1 
ATOM   10520 N  NH2 . ARG J  1 70  ? 123.145 27.782  -0.410  1.00 33.29 ? 69  ARG J NH2 1 
ATOM   10521 N  N   . LYS J  1 71  ? 121.981 23.257  5.917   1.00 16.61 ? 70  LYS J N   1 
ATOM   10522 C  CA  . LYS J  1 71  ? 122.405 23.035  7.285   1.00 12.61 ? 70  LYS J CA  1 
ATOM   10523 C  C   . LYS J  1 71  ? 122.673 24.396  7.856   1.00 9.71  ? 70  LYS J C   1 
ATOM   10524 O  O   . LYS J  1 71  ? 122.693 25.382  7.132   1.00 12.79 ? 70  LYS J O   1 
ATOM   10525 C  CB  . LYS J  1 71  ? 123.662 22.204  7.349   1.00 15.11 ? 70  LYS J CB  1 
ATOM   10526 C  CG  . LYS J  1 71  ? 123.360 20.709  7.099   1.00 20.09 ? 70  LYS J CG  1 
ATOM   10527 C  CD  . LYS J  1 71  ? 124.565 19.776  7.205   1.00 22.15 ? 70  LYS J CD  1 
ATOM   10528 C  CE  . LYS J  1 71  ? 125.568 20.182  6.128   1.00 26.92 ? 70  LYS J CE  1 
ATOM   10529 N  NZ  . LYS J  1 71  ? 126.831 19.489  6.263   1.00 29.38 ? 70  LYS J NZ  1 
ATOM   10530 N  N   . HIS J  1 72  ? 122.809 24.495  9.152   1.00 7.96  ? 71  HIS J N   1 
ATOM   10531 C  CA  . HIS J  1 72  ? 122.903 25.762  9.837   1.00 5.59  ? 71  HIS J CA  1 
ATOM   10532 C  C   . HIS J  1 72  ? 124.242 26.402  9.620   1.00 4.85  ? 71  HIS J C   1 
ATOM   10533 O  O   . HIS J  1 72  ? 125.227 25.682  9.443   1.00 9.46  ? 71  HIS J O   1 
ATOM   10534 C  CB  . HIS J  1 72  ? 122.657 25.520  11.313  1.00 5.72  ? 71  HIS J CB  1 
ATOM   10535 C  CG  . HIS J  1 72  ? 122.597 26.768  12.172  1.00 5.48  ? 71  HIS J CG  1 
ATOM   10536 N  ND1 . HIS J  1 72  ? 121.525 27.542  12.222  1.00 3.94  ? 71  HIS J ND1 1 
ATOM   10537 C  CD2 . HIS J  1 72  ? 123.581 27.281  12.987  1.00 2.18  ? 71  HIS J CD2 1 
ATOM   10538 C  CE1 . HIS J  1 72  ? 121.810 28.515  13.042  1.00 3.98  ? 71  HIS J CE1 1 
ATOM   10539 N  NE2 . HIS J  1 72  ? 123.040 28.353  13.489  1.00 2.56  ? 71  HIS J NE2 1 
ATOM   10540 N  N   . GLY J  1 73  ? 124.296 27.718  9.622   1.00 3.75  ? 72  GLY J N   1 
ATOM   10541 C  CA  . GLY J  1 73  ? 125.557 28.414  9.463   1.00 3.09  ? 72  GLY J CA  1 
ATOM   10542 C  C   . GLY J  1 73  ? 125.411 29.829  9.991   1.00 2.81  ? 72  GLY J C   1 
ATOM   10543 O  O   . GLY J  1 73  ? 124.387 30.167  10.587  1.00 4.24  ? 72  GLY J O   1 
ATOM   10544 N  N   . GLY J  1 74  ? 126.408 30.685  9.972   1.00 3.88  ? 73  GLY J N   1 
ATOM   10545 C  CA  . GLY J  1 74  ? 126.143 32.083  10.284  1.00 4.99  ? 73  GLY J CA  1 
ATOM   10546 C  C   . GLY J  1 74  ? 125.665 32.809  9.024   1.00 6.40  ? 73  GLY J C   1 
ATOM   10547 O  O   . GLY J  1 74  ? 125.661 32.232  7.941   1.00 5.60  ? 73  GLY J O   1 
ATOM   10548 N  N   . PRO J  1 75  ? 125.329 34.096  9.049   1.00 7.73  ? 74  PRO J N   1 
ATOM   10549 C  CA  . PRO J  1 75  ? 124.566 34.701  7.991   1.00 8.84  ? 74  PRO J CA  1 
ATOM   10550 C  C   . PRO J  1 75  ? 125.473 34.987  6.799   1.00 13.73 ? 74  PRO J C   1 
ATOM   10551 O  O   . PRO J  1 75  ? 125.058 35.094  5.635   1.00 17.21 ? 74  PRO J O   1 
ATOM   10552 C  CB  . PRO J  1 75  ? 123.962 35.869  8.721   1.00 10.86 ? 74  PRO J CB  1 
ATOM   10553 C  CG  . PRO J  1 75  ? 124.950 36.284  9.810   1.00 10.33 ? 74  PRO J CG  1 
ATOM   10554 C  CD  . PRO J  1 75  ? 125.599 34.995  10.169  1.00 8.14  ? 74  PRO J CD  1 
ATOM   10555 N  N   . LYS J  1 76  ? 126.776 35.104  7.079   1.00 15.99 ? 75  LYS J N   1 
ATOM   10556 C  CA  . LYS J  1 76  ? 127.778 35.251  6.036   1.00 15.11 ? 75  LYS J CA  1 
ATOM   10557 C  C   . LYS J  1 76  ? 128.130 33.917  5.348   1.00 15.01 ? 75  LYS J C   1 
ATOM   10558 O  O   . LYS J  1 76  ? 128.964 33.915  4.451   1.00 17.74 ? 75  LYS J O   1 
ATOM   10559 C  CB  . LYS J  1 76  ? 129.001 35.903  6.690   1.00 13.13 ? 75  LYS J CB  1 
ATOM   10560 C  CG  . LYS J  1 76  ? 128.994 37.445  6.610   1.00 18.27 ? 75  LYS J CG  1 
ATOM   10561 C  CD  . LYS J  1 76  ? 128.028 38.239  7.526   1.00 21.33 ? 75  LYS J CD  1 
ATOM   10562 C  CE  . LYS J  1 76  ? 128.554 38.300  8.990   1.00 21.73 ? 75  LYS J CE  1 
ATOM   10563 N  NZ  . LYS J  1 76  ? 127.610 38.950  9.893   1.00 19.89 ? 75  LYS J NZ  1 
ATOM   10564 N  N   . ASP J  1 77  ? 127.545 32.754  5.647   1.00 15.58 ? 76  ASP J N   1 
ATOM   10565 C  CA  . ASP J  1 77  ? 127.970 31.498  5.045   1.00 16.25 ? 76  ASP J CA  1 
ATOM   10566 C  C   . ASP J  1 77  ? 127.164 31.166  3.813   1.00 18.24 ? 76  ASP J C   1 
ATOM   10567 O  O   . ASP J  1 77  ? 126.117 31.730  3.532   1.00 19.38 ? 76  ASP J O   1 
ATOM   10568 C  CB  . ASP J  1 77  ? 127.818 30.357  6.028   1.00 14.69 ? 76  ASP J CB  1 
ATOM   10569 C  CG  . ASP J  1 77  ? 128.643 30.453  7.303   1.00 18.23 ? 76  ASP J CG  1 
ATOM   10570 O  OD1 . ASP J  1 77  ? 129.414 31.392  7.508   1.00 21.35 ? 76  ASP J OD1 1 
ATOM   10571 O  OD2 . ASP J  1 77  ? 128.519 29.559  8.129   1.00 23.09 ? 76  ASP J OD2 1 
ATOM   10572 N  N   . GLU J  1 78  ? 127.679 30.235  3.036   1.00 21.57 ? 77  GLU J N   1 
ATOM   10573 C  CA  . GLU J  1 78  ? 127.028 29.735  1.826   1.00 23.85 ? 77  GLU J CA  1 
ATOM   10574 C  C   . GLU J  1 78  ? 125.864 28.858  2.231   1.00 21.56 ? 77  GLU J C   1 
ATOM   10575 O  O   . GLU J  1 78  ? 124.778 28.903  1.659   1.00 22.61 ? 77  GLU J O   1 
ATOM   10576 C  CB  . GLU J  1 78  ? 128.041 28.894  0.986   1.00 30.40 ? 77  GLU J CB  1 
ATOM   10577 C  CG  . GLU J  1 78  ? 127.617 28.276  -0.391  1.00 38.67 ? 77  GLU J CG  1 
ATOM   10578 C  CD  . GLU J  1 78  ? 128.416 27.049  -0.921  1.00 42.76 ? 77  GLU J CD  1 
ATOM   10579 O  OE1 . GLU J  1 78  ? 129.606 27.182  -1.284  1.00 42.91 ? 77  GLU J OE1 1 
ATOM   10580 O  OE2 . GLU J  1 78  ? 127.820 25.955  -0.979  1.00 44.01 ? 77  GLU J OE2 1 
ATOM   10581 N  N   . GLU J  1 79  ? 126.198 28.004  3.202   1.00 18.76 ? 78  GLU J N   1 
ATOM   10582 C  CA  . GLU J  1 79  ? 125.359 26.964  3.751   1.00 14.40 ? 78  GLU J CA  1 
ATOM   10583 C  C   . GLU J  1 79  ? 124.847 27.504  5.054   1.00 12.23 ? 78  GLU J C   1 
ATOM   10584 O  O   . GLU J  1 79  ? 125.601 27.662  6.013   1.00 11.63 ? 78  GLU J O   1 
ATOM   10585 C  CB  . GLU J  1 79  ? 126.196 25.747  4.008   1.00 16.78 ? 78  GLU J CB  1 
ATOM   10586 C  CG  . GLU J  1 79  ? 125.508 24.530  4.582   1.00 18.16 ? 78  GLU J CG  1 
ATOM   10587 C  CD  . GLU J  1 79  ? 124.656 23.756  3.591   1.00 24.84 ? 78  GLU J CD  1 
ATOM   10588 O  OE1 . GLU J  1 79  ? 124.323 24.304  2.527   1.00 25.65 ? 78  GLU J OE1 1 
ATOM   10589 O  OE2 . GLU J  1 79  ? 124.336 22.591  3.885   1.00 25.45 ? 78  GLU J OE2 1 
ATOM   10590 N  N   . ARG J  1 80  ? 123.578 27.831  5.028   1.00 9.79  ? 79  ARG J N   1 
ATOM   10591 C  CA  . ARG J  1 80  ? 122.886 28.333  6.179   1.00 8.52  ? 79  ARG J CA  1 
ATOM   10592 C  C   . ARG J  1 80  ? 121.411 28.243  5.861   1.00 9.65  ? 79  ARG J C   1 
ATOM   10593 O  O   . ARG J  1 80  ? 120.959 28.055  4.720   1.00 13.27 ? 79  ARG J O   1 
ATOM   10594 C  CB  . ARG J  1 80  ? 123.298 29.786  6.461   1.00 7.67  ? 79  ARG J CB  1 
ATOM   10595 C  CG  . ARG J  1 80  ? 123.345 30.722  5.259   1.00 2.07  ? 79  ARG J CG  1 
ATOM   10596 C  CD  . ARG J  1 80  ? 122.134 31.577  5.103   1.00 2.00  ? 79  ARG J CD  1 
ATOM   10597 N  NE  . ARG J  1 80  ? 122.401 32.972  5.390   1.00 2.00  ? 79  ARG J NE  1 
ATOM   10598 C  CZ  . ARG J  1 80  ? 121.413 33.812  5.773   1.00 3.00  ? 79  ARG J CZ  1 
ATOM   10599 N  NH1 . ARG J  1 80  ? 120.111 33.525  5.945   1.00 2.00  ? 79  ARG J NH1 1 
ATOM   10600 N  NH2 . ARG J  1 80  ? 121.730 35.055  5.985   1.00 2.59  ? 79  ARG J NH2 1 
ATOM   10601 N  N   . HIS J  1 81  ? 120.654 28.340  6.923   1.00 8.13  ? 80  HIS J N   1 
ATOM   10602 C  CA  . HIS J  1 81  ? 119.225 28.381  6.828   1.00 9.53  ? 80  HIS J CA  1 
ATOM   10603 C  C   . HIS J  1 81  ? 118.887 29.838  6.511   1.00 13.94 ? 80  HIS J C   1 
ATOM   10604 O  O   . HIS J  1 81  ? 119.517 30.734  7.085   1.00 13.75 ? 80  HIS J O   1 
ATOM   10605 C  CB  . HIS J  1 81  ? 118.575 28.075  8.123   1.00 6.59  ? 80  HIS J CB  1 
ATOM   10606 C  CG  . HIS J  1 81  ? 118.906 26.762  8.803   1.00 7.14  ? 80  HIS J CG  1 
ATOM   10607 N  ND1 . HIS J  1 81  ? 119.279 26.664  10.062  1.00 5.67  ? 80  HIS J ND1 1 
ATOM   10608 C  CD2 . HIS J  1 81  ? 118.784 25.496  8.281   1.00 3.38  ? 80  HIS J CD2 1 
ATOM   10609 C  CE1 . HIS J  1 81  ? 119.363 25.385  10.321  1.00 2.73  ? 80  HIS J CE1 1 
ATOM   10610 N  NE2 . HIS J  1 81  ? 119.072 24.699  9.252   1.00 2.00  ? 80  HIS J NE2 1 
ATOM   10611 N  N   . VAL J  1 82  ? 117.858 30.115  5.691   1.00 16.15 ? 81  VAL J N   1 
ATOM   10612 C  CA  . VAL J  1 82  ? 117.408 31.454  5.341   1.00 13.75 ? 81  VAL J CA  1 
ATOM   10613 C  C   . VAL J  1 82  ? 117.128 32.261  6.582   1.00 13.56 ? 81  VAL J C   1 
ATOM   10614 O  O   . VAL J  1 82  ? 117.281 33.481  6.549   1.00 13.19 ? 81  VAL J O   1 
ATOM   10615 C  CB  . VAL J  1 82  ? 116.119 31.378  4.433   1.00 13.19 ? 81  VAL J CB  1 
ATOM   10616 C  CG1 . VAL J  1 82  ? 115.502 32.759  4.180   1.00 10.33 ? 81  VAL J CG1 1 
ATOM   10617 C  CG2 . VAL J  1 82  ? 116.520 30.831  3.058   1.00 10.05 ? 81  VAL J CG2 1 
ATOM   10618 N  N   . GLY J  1 83  ? 116.746 31.623  7.683   1.00 14.16 ? 82  GLY J N   1 
ATOM   10619 C  CA  . GLY J  1 83  ? 116.479 32.400  8.888   1.00 14.95 ? 82  GLY J CA  1 
ATOM   10620 C  C   . GLY J  1 83  ? 117.680 32.564  9.788   1.00 13.40 ? 82  GLY J C   1 
ATOM   10621 O  O   . GLY J  1 83  ? 117.508 32.810  10.974  1.00 16.70 ? 82  GLY J O   1 
ATOM   10622 N  N   . ASP J  1 84  ? 118.922 32.416  9.366   1.00 14.21 ? 83  ASP J N   1 
ATOM   10623 C  CA  . ASP J  1 84  ? 120.069 32.458  10.268  1.00 12.42 ? 83  ASP J CA  1 
ATOM   10624 C  C   . ASP J  1 84  ? 120.652 33.834  10.241  1.00 12.22 ? 83  ASP J C   1 
ATOM   10625 O  O   . ASP J  1 84  ? 121.334 34.199  9.286   1.00 13.53 ? 83  ASP J O   1 
ATOM   10626 C  CB  . ASP J  1 84  ? 121.145 31.474  9.847   1.00 10.65 ? 83  ASP J CB  1 
ATOM   10627 C  CG  . ASP J  1 84  ? 120.797 30.033  10.096  1.00 10.25 ? 83  ASP J CG  1 
ATOM   10628 O  OD1 . ASP J  1 84  ? 119.856 29.752  10.814  1.00 10.62 ? 83  ASP J OD1 1 
ATOM   10629 O  OD2 . ASP J  1 84  ? 121.483 29.176  9.571   1.00 14.62 ? 83  ASP J OD2 1 
ATOM   10630 N  N   . LEU J  1 85  ? 120.350 34.611  11.269  1.00 10.88 ? 84  LEU J N   1 
ATOM   10631 C  CA  . LEU J  1 85  ? 120.818 35.967  11.262  1.00 9.05  ? 84  LEU J CA  1 
ATOM   10632 C  C   . LEU J  1 85  ? 121.972 36.118  12.214  1.00 8.59  ? 84  LEU J C   1 
ATOM   10633 O  O   . LEU J  1 85  ? 122.330 37.241  12.527  1.00 9.35  ? 84  LEU J O   1 
ATOM   10634 C  CB  . LEU J  1 85  ? 119.646 36.868  11.617  1.00 11.50 ? 84  LEU J CB  1 
ATOM   10635 C  CG  . LEU J  1 85  ? 118.694 37.352  10.511  1.00 11.75 ? 84  LEU J CG  1 
ATOM   10636 C  CD1 . LEU J  1 85  ? 118.419 36.284  9.490   1.00 10.80 ? 84  LEU J CD1 1 
ATOM   10637 C  CD2 . LEU J  1 85  ? 117.385 37.747  11.173  1.00 9.17  ? 84  LEU J CD2 1 
ATOM   10638 N  N   . GLY J  1 86  ? 122.574 35.009  12.657  1.00 7.46  ? 85  GLY J N   1 
ATOM   10639 C  CA  . GLY J  1 86  ? 123.750 35.067  13.488  1.00 5.03  ? 85  GLY J CA  1 
ATOM   10640 C  C   . GLY J  1 86  ? 123.402 35.416  14.908  1.00 5.36  ? 85  GLY J C   1 
ATOM   10641 O  O   . GLY J  1 86  ? 122.456 34.851  15.457  1.00 6.04  ? 85  GLY J O   1 
ATOM   10642 N  N   . ASN J  1 87  ? 124.128 36.364  15.475  1.00 5.46  ? 86  ASN J N   1 
ATOM   10643 C  CA  . ASN J  1 87  ? 124.052 36.702  16.883  1.00 7.53  ? 86  ASN J CA  1 
ATOM   10644 C  C   . ASN J  1 87  ? 123.831 38.175  17.080  1.00 8.90  ? 86  ASN J C   1 
ATOM   10645 O  O   . ASN J  1 87  ? 124.398 38.944  16.314  1.00 11.33 ? 86  ASN J O   1 
ATOM   10646 C  CB  . ASN J  1 87  ? 125.328 36.434  17.674  1.00 7.25  ? 86  ASN J CB  1 
ATOM   10647 C  CG  . ASN J  1 87  ? 125.568 34.999  18.107  1.00 9.32  ? 86  ASN J CG  1 
ATOM   10648 O  OD1 . ASN J  1 87  ? 124.794 34.387  18.846  1.00 10.42 ? 86  ASN J OD1 1 
ATOM   10649 N  ND2 . ASN J  1 87  ? 126.648 34.380  17.672  1.00 7.46  ? 86  ASN J ND2 1 
ATOM   10650 N  N   . VAL J  1 88  ? 123.051 38.648  18.051  1.00 9.37  ? 87  VAL J N   1 
ATOM   10651 C  CA  . VAL J  1 88  ? 123.045 40.070  18.385  1.00 9.24  ? 87  VAL J CA  1 
ATOM   10652 C  C   . VAL J  1 88  ? 123.736 40.129  19.769  1.00 11.59 ? 87  VAL J C   1 
ATOM   10653 O  O   . VAL J  1 88  ? 123.685 39.173  20.560  1.00 12.85 ? 87  VAL J O   1 
ATOM   10654 C  CB  . VAL J  1 88  ? 121.593 40.704  18.476  1.00 7.21  ? 87  VAL J CB  1 
ATOM   10655 C  CG1 . VAL J  1 88  ? 120.933 40.437  17.186  1.00 7.99  ? 87  VAL J CG1 1 
ATOM   10656 C  CG2 . VAL J  1 88  ? 120.684 40.135  19.545  1.00 7.47  ? 87  VAL J CG2 1 
ATOM   10657 N  N   . THR J  1 89  ? 124.496 41.187  20.066  1.00 12.24 ? 88  THR J N   1 
ATOM   10658 C  CA  . THR J  1 89  ? 125.180 41.382  21.348  1.00 10.68 ? 88  THR J CA  1 
ATOM   10659 C  C   . THR J  1 89  ? 124.369 42.188  22.341  1.00 10.40 ? 88  THR J C   1 
ATOM   10660 O  O   . THR J  1 89  ? 123.684 43.103  21.906  1.00 11.19 ? 88  THR J O   1 
ATOM   10661 C  CB  . THR J  1 89  ? 126.525 42.070  21.032  1.00 7.75  ? 88  THR J CB  1 
ATOM   10662 O  OG1 . THR J  1 89  ? 127.194 41.247  20.064  1.00 8.35  ? 88  THR J OG1 1 
ATOM   10663 C  CG2 . THR J  1 89  ? 127.408 42.231  22.251  1.00 6.24  ? 88  THR J CG2 1 
ATOM   10664 N  N   . ALA J  1 90  ? 124.391 41.921  23.638  1.00 13.22 ? 89  ALA J N   1 
ATOM   10665 C  CA  . ALA J  1 90  ? 123.688 42.729  24.644  1.00 16.05 ? 89  ALA J CA  1 
ATOM   10666 C  C   . ALA J  1 90  ? 124.726 43.339  25.563  1.00 17.53 ? 89  ALA J C   1 
ATOM   10667 O  O   . ALA J  1 90  ? 125.675 42.652  25.959  1.00 16.71 ? 89  ALA J O   1 
ATOM   10668 C  CB  . ALA J  1 90  ? 122.783 41.923  25.548  1.00 16.16 ? 89  ALA J CB  1 
ATOM   10669 N  N   . ASP J  1 91  ? 124.617 44.627  25.872  1.00 19.12 ? 90  ASP J N   1 
ATOM   10670 C  CA  . ASP J  1 91  ? 125.583 45.274  26.729  1.00 21.22 ? 90  ASP J CA  1 
ATOM   10671 C  C   . ASP J  1 91  ? 125.390 44.923  28.184  1.00 23.36 ? 90  ASP J C   1 
ATOM   10672 O  O   . ASP J  1 91  ? 124.395 44.312  28.552  1.00 23.61 ? 90  ASP J O   1 
ATOM   10673 C  CB  . ASP J  1 91  ? 125.512 46.796  26.581  1.00 22.89 ? 90  ASP J CB  1 
ATOM   10674 C  CG  . ASP J  1 91  ? 124.220 47.517  26.944  1.00 23.93 ? 90  ASP J CG  1 
ATOM   10675 O  OD1 . ASP J  1 91  ? 123.542 47.137  27.904  1.00 22.90 ? 90  ASP J OD1 1 
ATOM   10676 O  OD2 . ASP J  1 91  ? 123.898 48.470  26.236  1.00 24.07 ? 90  ASP J OD2 1 
ATOM   10677 N  N   . LYS J  1 92  ? 126.324 45.426  28.993  1.00 28.90 ? 91  LYS J N   1 
ATOM   10678 C  CA  . LYS J  1 92  ? 126.398 45.327  30.459  1.00 32.82 ? 91  LYS J CA  1 
ATOM   10679 C  C   . LYS J  1 92  ? 125.055 45.309  31.165  1.00 33.58 ? 91  LYS J C   1 
ATOM   10680 O  O   . LYS J  1 92  ? 124.780 44.528  32.073  1.00 33.91 ? 91  LYS J O   1 
ATOM   10681 C  CB  . LYS J  1 92  ? 127.222 46.507  30.938  1.00 35.40 ? 91  LYS J CB  1 
ATOM   10682 C  CG  . LYS J  1 92  ? 127.357 46.704  32.443  1.00 41.19 ? 91  LYS J CG  1 
ATOM   10683 C  CD  . LYS J  1 92  ? 127.912 48.112  32.610  1.00 44.23 ? 91  LYS J CD  1 
ATOM   10684 C  CE  . LYS J  1 92  ? 127.763 48.670  34.027  1.00 46.15 ? 91  LYS J CE  1 
ATOM   10685 N  NZ  . LYS J  1 92  ? 128.447 49.956  34.094  1.00 46.27 ? 91  LYS J NZ  1 
ATOM   10686 N  N   . ASP J  1 93  ? 124.228 46.238  30.710  1.00 34.43 ? 92  ASP J N   1 
ATOM   10687 C  CA  . ASP J  1 93  ? 122.875 46.347  31.184  1.00 34.66 ? 92  ASP J CA  1 
ATOM   10688 C  C   . ASP J  1 93  ? 121.887 45.778  30.135  1.00 31.43 ? 92  ASP J C   1 
ATOM   10689 O  O   . ASP J  1 93  ? 121.157 46.496  29.450  1.00 31.58 ? 92  ASP J O   1 
ATOM   10690 C  CB  . ASP J  1 93  ? 122.678 47.853  31.535  1.00 39.38 ? 92  ASP J CB  1 
ATOM   10691 C  CG  . ASP J  1 93  ? 123.116 48.957  30.554  1.00 42.31 ? 92  ASP J CG  1 
ATOM   10692 O  OD1 . ASP J  1 93  ? 124.279 49.374  30.610  1.00 46.70 ? 92  ASP J OD1 1 
ATOM   10693 O  OD2 . ASP J  1 93  ? 122.292 49.415  29.752  1.00 43.67 ? 92  ASP J OD2 1 
ATOM   10694 N  N   . GLY J  1 94  ? 121.994 44.469  29.892  1.00 26.33 ? 93  GLY J N   1 
ATOM   10695 C  CA  . GLY J  1 94  ? 121.143 43.672  29.018  1.00 18.47 ? 93  GLY J CA  1 
ATOM   10696 C  C   . GLY J  1 94  ? 120.398 44.228  27.814  1.00 14.70 ? 93  GLY J C   1 
ATOM   10697 O  O   . GLY J  1 94  ? 119.372 43.616  27.490  1.00 14.26 ? 93  GLY J O   1 
ATOM   10698 N  N   . VAL J  1 95  ? 120.802 45.314  27.147  1.00 12.30 ? 94  VAL J N   1 
ATOM   10699 C  CA  . VAL J  1 95  ? 120.155 45.880  25.949  1.00 10.13 ? 94  VAL J CA  1 
ATOM   10700 C  C   . VAL J  1 95  ? 120.873 45.503  24.647  1.00 10.82 ? 94  VAL J C   1 
ATOM   10701 O  O   . VAL J  1 95  ? 122.094 45.589  24.541  1.00 12.76 ? 94  VAL J O   1 
ATOM   10702 C  CB  . VAL J  1 95  ? 120.092 47.443  26.057  1.00 9.34  ? 94  VAL J CB  1 
ATOM   10703 C  CG1 . VAL J  1 95  ? 119.399 48.089  24.850  1.00 6.51  ? 94  VAL J CG1 1 
ATOM   10704 C  CG2 . VAL J  1 95  ? 119.301 47.800  27.306  1.00 7.14  ? 94  VAL J CG2 1 
ATOM   10705 N  N   . ALA J  1 96  ? 120.205 45.109  23.589  1.00 11.67 ? 95  ALA J N   1 
ATOM   10706 C  CA  . ALA J  1 96  ? 120.854 44.666  22.377  1.00 13.44 ? 95  ALA J CA  1 
ATOM   10707 C  C   . ALA J  1 96  ? 120.350 45.621  21.340  1.00 16.56 ? 95  ALA J C   1 
ATOM   10708 O  O   . ALA J  1 96  ? 119.126 45.745  21.170  1.00 20.38 ? 95  ALA J O   1 
ATOM   10709 C  CB  . ALA J  1 96  ? 120.412 43.259  21.993  1.00 10.27 ? 95  ALA J CB  1 
ATOM   10710 N  N   . ASP J  1 97  ? 121.224 46.355  20.673  1.00 17.25 ? 96  ASP J N   1 
ATOM   10711 C  CA  . ASP J  1 97  ? 120.752 47.231  19.625  1.00 17.85 ? 96  ASP J CA  1 
ATOM   10712 C  C   . ASP J  1 97  ? 121.191 46.595  18.337  1.00 14.87 ? 96  ASP J C   1 
ATOM   10713 O  O   . ASP J  1 97  ? 122.371 46.596  17.986  1.00 14.16 ? 96  ASP J O   1 
ATOM   10714 C  CB  . ASP J  1 97  ? 121.350 48.642  19.754  1.00 23.90 ? 96  ASP J CB  1 
ATOM   10715 C  CG  . ASP J  1 97  ? 120.391 49.631  20.421  1.00 28.52 ? 96  ASP J CG  1 
ATOM   10716 O  OD1 . ASP J  1 97  ? 120.338 49.660  21.667  1.00 29.00 ? 96  ASP J OD1 1 
ATOM   10717 O  OD2 . ASP J  1 97  ? 119.705 50.356  19.670  1.00 31.37 ? 96  ASP J OD2 1 
ATOM   10718 N  N   . VAL J  1 98  ? 120.196 46.030  17.692  1.00 9.20  ? 97  VAL J N   1 
ATOM   10719 C  CA  . VAL J  1 98  ? 120.396 45.258  16.497  1.00 6.60  ? 97  VAL J CA  1 
ATOM   10720 C  C   . VAL J  1 98  ? 120.661 46.122  15.268  1.00 8.17  ? 97  VAL J C   1 
ATOM   10721 O  O   . VAL J  1 98  ? 119.991 47.138  15.050  1.00 10.89 ? 97  VAL J O   1 
ATOM   10722 C  CB  . VAL J  1 98  ? 119.136 44.375  16.319  1.00 3.94  ? 97  VAL J CB  1 
ATOM   10723 C  CG1 . VAL J  1 98  ? 119.230 43.562  15.050  1.00 2.00  ? 97  VAL J CG1 1 
ATOM   10724 C  CG2 . VAL J  1 98  ? 118.967 43.495  17.564  1.00 3.78  ? 97  VAL J CG2 1 
ATOM   10725 N  N   . SER J  1 99  ? 121.660 45.778  14.463  1.00 8.83  ? 98  SER J N   1 
ATOM   10726 C  CA  . SER J  1 99  ? 121.847 46.310  13.116  1.00 6.99  ? 98  SER J CA  1 
ATOM   10727 C  C   . SER J  1 99  ? 122.549 45.200  12.396  1.00 7.22  ? 98  SER J C   1 
ATOM   10728 O  O   . SER J  1 99  ? 123.716 44.864  12.615  1.00 9.49  ? 98  SER J O   1 
ATOM   10729 C  CB  . SER J  1 99  ? 122.746 47.524  12.997  1.00 7.94  ? 98  SER J CB  1 
ATOM   10730 O  OG  . SER J  1 99  ? 122.067 48.690  13.460  1.00 16.40 ? 98  SER J OG  1 
ATOM   10731 N  N   . ILE J  1 100 ? 121.740 44.553  11.597  1.00 5.77  ? 99  ILE J N   1 
ATOM   10732 C  CA  . ILE J  1 100 ? 122.160 43.440  10.776  1.00 7.57  ? 99  ILE J CA  1 
ATOM   10733 C  C   . ILE J  1 100 ? 121.705 43.889  9.358   1.00 8.67  ? 99  ILE J C   1 
ATOM   10734 O  O   . ILE J  1 100 ? 120.824 44.745  9.198   1.00 8.55  ? 99  ILE J O   1 
ATOM   10735 C  CB  . ILE J  1 100 ? 121.405 42.171  11.352  1.00 6.67  ? 99  ILE J CB  1 
ATOM   10736 C  CG1 . ILE J  1 100 ? 121.999 41.845  12.729  1.00 9.60  ? 99  ILE J CG1 1 
ATOM   10737 C  CG2 . ILE J  1 100 ? 121.431 41.013  10.376  1.00 2.00  ? 99  ILE J CG2 1 
ATOM   10738 C  CD1 . ILE J  1 100 ? 121.234 40.793  13.573  1.00 9.90  ? 99  ILE J CD1 1 
ATOM   10739 N  N   . GLU J  1 101 ? 122.289 43.376  8.294   1.00 10.15 ? 100 GLU J N   1 
ATOM   10740 C  CA  . GLU J  1 101 ? 121.784 43.643  6.973   1.00 14.83 ? 100 GLU J CA  1 
ATOM   10741 C  C   . GLU J  1 101 ? 121.902 42.303  6.301   1.00 13.86 ? 100 GLU J C   1 
ATOM   10742 O  O   . GLU J  1 101 ? 123.009 41.781  6.193   1.00 14.60 ? 100 GLU J O   1 
ATOM   10743 C  CB  . GLU J  1 101 ? 122.646 44.674  6.287   1.00 20.05 ? 100 GLU J CB  1 
ATOM   10744 C  CG  . GLU J  1 101 ? 122.070 45.122  4.952   1.00 25.75 ? 100 GLU J CG  1 
ATOM   10745 C  CD  . GLU J  1 101 ? 122.825 46.321  4.425   1.00 29.81 ? 100 GLU J CD  1 
ATOM   10746 O  OE1 . GLU J  1 101 ? 123.937 46.133  3.915   1.00 33.58 ? 100 GLU J OE1 1 
ATOM   10747 O  OE2 . GLU J  1 101 ? 122.299 47.430  4.555   1.00 31.39 ? 100 GLU J OE2 1 
ATOM   10748 N  N   . ASP J  1 102 ? 120.790 41.682  5.929   1.00 13.98 ? 101 ASP J N   1 
ATOM   10749 C  CA  . ASP J  1 102 ? 120.877 40.370  5.330   1.00 11.58 ? 101 ASP J CA  1 
ATOM   10750 C  C   . ASP J  1 102 ? 120.298 40.487  3.939   1.00 10.73 ? 101 ASP J C   1 
ATOM   10751 O  O   . ASP J  1 102 ? 119.510 41.376  3.611   1.00 7.75  ? 101 ASP J O   1 
ATOM   10752 C  CB  . ASP J  1 102 ? 120.084 39.375  6.186   1.00 12.24 ? 101 ASP J CB  1 
ATOM   10753 C  CG  . ASP J  1 102 ? 120.465 37.931  5.896   1.00 14.60 ? 101 ASP J CG  1 
ATOM   10754 O  OD1 . ASP J  1 102 ? 121.610 37.610  6.160   1.00 17.84 ? 101 ASP J OD1 1 
ATOM   10755 O  OD2 . ASP J  1 102 ? 119.666 37.128  5.417   1.00 14.91 ? 101 ASP J OD2 1 
ATOM   10756 N  N   . SER J  1 103 ? 120.722 39.589  3.090   1.00 12.45 ? 102 SER J N   1 
ATOM   10757 C  CA  . SER J  1 103 ? 120.136 39.514  1.769   1.00 15.24 ? 102 SER J CA  1 
ATOM   10758 C  C   . SER J  1 103 ? 119.868 38.068  1.374   1.00 15.02 ? 102 SER J C   1 
ATOM   10759 O  O   . SER J  1 103 ? 120.389 37.502  0.423   1.00 16.87 ? 102 SER J O   1 
ATOM   10760 C  CB  . SER J  1 103 ? 121.077 40.184  0.798   1.00 16.89 ? 102 SER J CB  1 
ATOM   10761 O  OG  . SER J  1 103 ? 122.424 39.947  1.207   1.00 24.98 ? 102 SER J OG  1 
ATOM   10762 N  N   . VAL J  1 104 ? 119.141 37.358  2.204   1.00 14.87 ? 103 VAL J N   1 
ATOM   10763 C  CA  . VAL J  1 104 ? 118.693 36.018  1.836   1.00 15.78 ? 103 VAL J CA  1 
ATOM   10764 C  C   . VAL J  1 104 ? 117.370 35.918  2.573   1.00 16.03 ? 103 VAL J C   1 
ATOM   10765 O  O   . VAL J  1 104 ? 116.436 35.338  2.022   1.00 18.81 ? 103 VAL J O   1 
ATOM   10766 C  CB  . VAL J  1 104 ? 119.758 34.821  2.155   1.00 13.36 ? 103 VAL J CB  1 
ATOM   10767 C  CG1 . VAL J  1 104 ? 120.870 35.354  2.983   1.00 15.34 ? 103 VAL J CG1 1 
ATOM   10768 C  CG2 . VAL J  1 104 ? 119.111 33.615  2.777   1.00 8.72  ? 103 VAL J CG2 1 
ATOM   10769 N  N   . ILE J  1 105 ? 117.202 36.533  3.743   1.00 15.69 ? 104 ILE J N   1 
ATOM   10770 C  CA  . ILE J  1 105 ? 115.837 36.778  4.187   1.00 15.85 ? 104 ILE J CA  1 
ATOM   10771 C  C   . ILE J  1 105 ? 115.265 37.836  3.209   1.00 17.61 ? 104 ILE J C   1 
ATOM   10772 O  O   . ILE J  1 105 ? 116.016 38.612  2.602   1.00 16.28 ? 104 ILE J O   1 
ATOM   10773 C  CB  . ILE J  1 105 ? 115.740 37.337  5.665   1.00 13.57 ? 104 ILE J CB  1 
ATOM   10774 C  CG1 . ILE J  1 105 ? 116.311 38.755  5.820   1.00 12.64 ? 104 ILE J CG1 1 
ATOM   10775 C  CG2 . ILE J  1 105 ? 116.428 36.337  6.550   1.00 8.45  ? 104 ILE J CG2 1 
ATOM   10776 C  CD1 . ILE J  1 105 ? 116.150 39.374  7.220   1.00 11.22 ? 104 ILE J CD1 1 
ATOM   10777 N  N   . SER J  1 106 ? 113.946 37.837  3.026   1.00 20.37 ? 105 SER J N   1 
ATOM   10778 C  CA  . SER J  1 106 ? 113.245 38.799  2.199   1.00 20.50 ? 105 SER J CA  1 
ATOM   10779 C  C   . SER J  1 106 ? 111.914 39.028  2.890   1.00 22.50 ? 105 SER J C   1 
ATOM   10780 O  O   . SER J  1 106 ? 111.526 38.310  3.823   1.00 22.68 ? 105 SER J O   1 
ATOM   10781 C  CB  . SER J  1 106 ? 112.999 38.237  0.805   1.00 19.59 ? 105 SER J CB  1 
ATOM   10782 O  OG  . SER J  1 106 ? 112.418 39.200  -0.083  1.00 18.39 ? 105 SER J OG  1 
ATOM   10783 N  N   . LEU J  1 107 ? 111.224 40.079  2.462   1.00 23.04 ? 106 LEU J N   1 
ATOM   10784 C  CA  . LEU J  1 107 ? 109.879 40.389  2.941   1.00 21.78 ? 106 LEU J CA  1 
ATOM   10785 C  C   . LEU J  1 107 ? 108.896 40.184  1.790   1.00 22.37 ? 106 LEU J C   1 
ATOM   10786 O  O   . LEU J  1 107 ? 107.690 40.048  1.980   1.00 20.51 ? 106 LEU J O   1 
ATOM   10787 C  CB  . LEU J  1 107 ? 109.811 41.829  3.419   1.00 19.93 ? 106 LEU J CB  1 
ATOM   10788 C  CG  . LEU J  1 107 ? 110.827 42.329  4.442   1.00 19.51 ? 106 LEU J CG  1 
ATOM   10789 C  CD1 . LEU J  1 107 ? 110.439 43.744  4.788   1.00 16.82 ? 106 LEU J CD1 1 
ATOM   10790 C  CD2 . LEU J  1 107 ? 110.881 41.432  5.686   1.00 18.21 ? 106 LEU J CD2 1 
ATOM   10791 N  N   . SER J  1 108 ? 109.434 40.202  0.570   1.00 25.11 ? 107 SER J N   1 
ATOM   10792 C  CA  . SER J  1 108 ? 108.746 39.976  -0.697  1.00 27.35 ? 107 SER J CA  1 
ATOM   10793 C  C   . SER J  1 108 ? 109.162 38.561  -1.121  1.00 28.43 ? 107 SER J C   1 
ATOM   10794 O  O   . SER J  1 108 ? 110.049 38.003  -0.472  1.00 30.80 ? 107 SER J O   1 
ATOM   10795 C  CB  . SER J  1 108 ? 109.248 41.017  -1.718  1.00 29.45 ? 107 SER J CB  1 
ATOM   10796 O  OG  . SER J  1 108 ? 109.445 42.371  -1.247  1.00 31.85 ? 107 SER J OG  1 
ATOM   10797 N  N   . GLY J  1 109 ? 108.610 37.870  -2.120  1.00 29.32 ? 108 GLY J N   1 
ATOM   10798 C  CA  . GLY J  1 109 ? 109.164 36.598  -2.620  1.00 29.35 ? 108 GLY J CA  1 
ATOM   10799 C  C   . GLY J  1 109 ? 108.803 35.338  -1.864  1.00 30.13 ? 108 GLY J C   1 
ATOM   10800 O  O   . GLY J  1 109 ? 107.971 35.391  -0.972  1.00 31.60 ? 108 GLY J O   1 
ATOM   10801 N  N   . ASP J  1 110 ? 109.414 34.183  -2.180  1.00 32.14 ? 109 ASP J N   1 
ATOM   10802 C  CA  . ASP J  1 110 ? 109.167 32.890  -1.494  1.00 30.57 ? 109 ASP J CA  1 
ATOM   10803 C  C   . ASP J  1 110 ? 110.040 32.704  -0.244  1.00 28.41 ? 109 ASP J C   1 
ATOM   10804 O  O   . ASP J  1 110 ? 110.057 31.664  0.415   1.00 26.98 ? 109 ASP J O   1 
ATOM   10805 C  CB  . ASP J  1 110 ? 109.454 31.673  -2.422  1.00 35.44 ? 109 ASP J CB  1 
ATOM   10806 C  CG  . ASP J  1 110 ? 108.551 31.476  -3.658  1.00 39.88 ? 109 ASP J CG  1 
ATOM   10807 O  OD1 . ASP J  1 110 ? 108.522 32.389  -4.493  1.00 42.52 ? 109 ASP J OD1 1 
ATOM   10808 O  OD2 . ASP J  1 110 ? 107.898 30.422  -3.801  1.00 39.19 ? 109 ASP J OD2 1 
ATOM   10809 N  N   . HIS J  1 111 ? 110.911 33.667  0.025   1.00 25.81 ? 110 HIS J N   1 
ATOM   10810 C  CA  . HIS J  1 111 ? 111.728 33.658  1.228   1.00 24.64 ? 110 HIS J CA  1 
ATOM   10811 C  C   . HIS J  1 111 ? 111.245 34.767  2.144   1.00 22.74 ? 110 HIS J C   1 
ATOM   10812 O  O   . HIS J  1 111 ? 112.034 35.356  2.900   1.00 22.29 ? 110 HIS J O   1 
ATOM   10813 C  CB  . HIS J  1 111 ? 113.176 33.964  0.964   1.00 25.24 ? 110 HIS J CB  1 
ATOM   10814 C  CG  . HIS J  1 111 ? 113.978 32.931  0.229   1.00 25.10 ? 110 HIS J CG  1 
ATOM   10815 N  ND1 . HIS J  1 111 ? 115.279 33.053  -0.007  1.00 24.12 ? 110 HIS J ND1 1 
ATOM   10816 C  CD2 . HIS J  1 111 ? 113.517 31.744  -0.286  1.00 25.40 ? 110 HIS J CD2 1 
ATOM   10817 C  CE1 . HIS J  1 111 ? 115.640 31.986  -0.653  1.00 25.43 ? 110 HIS J CE1 1 
ATOM   10818 N  NE2 . HIS J  1 111 ? 114.584 31.211  -0.817  1.00 25.79 ? 110 HIS J NE2 1 
ATOM   10819 N  N   . SER J  1 112 ? 109.971 35.129  2.012   1.00 20.89 ? 111 SER J N   1 
ATOM   10820 C  CA  . SER J  1 112 ? 109.452 36.193  2.827   1.00 20.26 ? 111 SER J CA  1 
ATOM   10821 C  C   . SER J  1 112 ? 109.398 35.637  4.237   1.00 20.15 ? 111 SER J C   1 
ATOM   10822 O  O   . SER J  1 112 ? 109.078 34.464  4.437   1.00 23.15 ? 111 SER J O   1 
ATOM   10823 C  CB  . SER J  1 112 ? 108.075 36.590  2.367   1.00 19.17 ? 111 SER J CB  1 
ATOM   10824 O  OG  . SER J  1 112 ? 107.470 37.422  3.355   1.00 21.25 ? 111 SER J OG  1 
ATOM   10825 N  N   . ILE J  1 113 ? 109.840 36.463  5.177   1.00 18.10 ? 112 ILE J N   1 
ATOM   10826 C  CA  . ILE J  1 113 ? 109.788 36.120  6.576   1.00 15.48 ? 112 ILE J CA  1 
ATOM   10827 C  C   . ILE J  1 113 ? 108.530 36.695  7.258   1.00 16.33 ? 112 ILE J C   1 
ATOM   10828 O  O   . ILE J  1 113 ? 108.326 36.573  8.475   1.00 15.81 ? 112 ILE J O   1 
ATOM   10829 C  CB  . ILE J  1 113 ? 111.059 36.626  7.272   1.00 13.69 ? 112 ILE J CB  1 
ATOM   10830 C  CG1 . ILE J  1 113 ? 111.170 38.144  7.229   1.00 13.46 ? 112 ILE J CG1 1 
ATOM   10831 C  CG2 . ILE J  1 113 ? 112.238 35.923  6.620   1.00 13.44 ? 112 ILE J CG2 1 
ATOM   10832 C  CD1 . ILE J  1 113 ? 112.277 38.667  8.184   1.00 11.01 ? 112 ILE J CD1 1 
ATOM   10833 N  N   . ILE J  1 114 ? 107.653 37.360  6.503   1.00 15.69 ? 113 ILE J N   1 
ATOM   10834 C  CA  . ILE J  1 114 ? 106.424 37.890  7.068   1.00 16.62 ? 113 ILE J CA  1 
ATOM   10835 C  C   . ILE J  1 114 ? 105.533 36.691  7.343   1.00 14.97 ? 113 ILE J C   1 
ATOM   10836 O  O   . ILE J  1 114 ? 105.462 35.743  6.544   1.00 16.83 ? 113 ILE J O   1 
ATOM   10837 C  CB  . ILE J  1 114 ? 105.738 38.878  6.070   1.00 19.21 ? 113 ILE J CB  1 
ATOM   10838 C  CG1 . ILE J  1 114 ? 106.643 40.082  5.760   1.00 19.31 ? 113 ILE J CG1 1 
ATOM   10839 C  CG2 . ILE J  1 114 ? 104.475 39.445  6.715   1.00 20.24 ? 113 ILE J CG2 1 
ATOM   10840 C  CD1 . ILE J  1 114 ? 106.042 40.943  4.626   1.00 23.18 ? 113 ILE J CD1 1 
ATOM   10841 N  N   . GLY J  1 115 ? 104.884 36.753  8.494   1.00 10.22 ? 114 GLY J N   1 
ATOM   10842 C  CA  . GLY J  1 115 ? 104.062 35.678  8.944   1.00 8.33  ? 114 GLY J CA  1 
ATOM   10843 C  C   . GLY J  1 115 ? 104.867 34.619  9.693   1.00 9.23  ? 114 GLY J C   1 
ATOM   10844 O  O   . GLY J  1 115 ? 104.320 33.539  10.016  1.00 9.33  ? 114 GLY J O   1 
ATOM   10845 N  N   . ARG J  1 116 ? 106.152 34.842  9.994   1.00 6.20  ? 115 ARG J N   1 
ATOM   10846 C  CA  . ARG J  1 116 ? 106.926 33.815  10.675  1.00 4.28  ? 115 ARG J CA  1 
ATOM   10847 C  C   . ARG J  1 116 ? 107.319 34.413  12.013  1.00 4.94  ? 115 ARG J C   1 
ATOM   10848 O  O   . ARG J  1 116 ? 106.844 35.530  12.303  1.00 5.58  ? 115 ARG J O   1 
ATOM   10849 C  CB  . ARG J  1 116 ? 108.110 33.464  9.799   1.00 2.13  ? 115 ARG J CB  1 
ATOM   10850 C  CG  . ARG J  1 116 ? 107.537 32.798  8.566   1.00 4.13  ? 115 ARG J CG  1 
ATOM   10851 C  CD  . ARG J  1 116 ? 108.554 32.680  7.458   1.00 10.08 ? 115 ARG J CD  1 
ATOM   10852 N  NE  . ARG J  1 116 ? 107.991 32.141  6.236   1.00 14.66 ? 115 ARG J NE  1 
ATOM   10853 C  CZ  . ARG J  1 116 ? 107.610 30.850  6.127   1.00 17.08 ? 115 ARG J CZ  1 
ATOM   10854 N  NH1 . ARG J  1 116 ? 107.794 29.967  7.104   1.00 12.07 ? 115 ARG J NH1 1 
ATOM   10855 N  NH2 . ARG J  1 116 ? 107.086 30.417  4.985   1.00 14.11 ? 115 ARG J NH2 1 
ATOM   10856 N  N   . THR J  1 117 ? 108.123 33.731  12.831  1.00 2.41  ? 116 THR J N   1 
ATOM   10857 C  CA  . THR J  1 117 ? 108.507 34.233  14.135  1.00 2.49  ? 116 THR J CA  1 
ATOM   10858 C  C   . THR J  1 117 ? 109.943 34.640  14.179  1.00 2.66  ? 116 THR J C   1 
ATOM   10859 O  O   . THR J  1 117 ? 110.830 34.024  13.603  1.00 5.00  ? 116 THR J O   1 
ATOM   10860 C  CB  . THR J  1 117 ? 108.247 33.164  15.191  1.00 2.80  ? 116 THR J CB  1 
ATOM   10861 O  OG1 . THR J  1 117 ? 106.840 33.001  15.154  1.00 5.71  ? 116 THR J OG1 1 
ATOM   10862 C  CG2 . THR J  1 117 ? 108.620 33.507  16.600  1.00 2.00  ? 116 THR J CG2 1 
ATOM   10863 N  N   . LEU J  1 118 ? 110.206 35.737  14.829  1.00 4.76  ? 117 LEU J N   1 
ATOM   10864 C  CA  . LEU J  1 118 ? 111.578 36.158  15.007  1.00 4.49  ? 117 LEU J CA  1 
ATOM   10865 C  C   . LEU J  1 118 ? 111.867 35.668  16.400  1.00 4.56  ? 117 LEU J C   1 
ATOM   10866 O  O   . LEU J  1 118 ? 110.957 35.790  17.237  1.00 5.89  ? 117 LEU J O   1 
ATOM   10867 C  CB  . LEU J  1 118 ? 111.654 37.647  14.946  1.00 4.69  ? 117 LEU J CB  1 
ATOM   10868 C  CG  . LEU J  1 118 ? 113.028 38.211  15.034  1.00 4.98  ? 117 LEU J CG  1 
ATOM   10869 C  CD1 . LEU J  1 118 ? 113.979 37.489  14.079  1.00 2.01  ? 117 LEU J CD1 1 
ATOM   10870 C  CD2 . LEU J  1 118 ? 112.900 39.687  14.741  1.00 2.37  ? 117 LEU J CD2 1 
ATOM   10871 N  N   . VAL J  1 119 ? 113.027 35.092  16.688  1.00 2.95  ? 118 VAL J N   1 
ATOM   10872 C  CA  . VAL J  1 119 ? 113.267 34.569  18.024  1.00 2.53  ? 118 VAL J CA  1 
ATOM   10873 C  C   . VAL J  1 119 ? 114.580 35.109  18.526  1.00 2.00  ? 118 VAL J C   1 
ATOM   10874 O  O   . VAL J  1 119 ? 115.435 35.352  17.674  1.00 2.00  ? 118 VAL J O   1 
ATOM   10875 C  CB  . VAL J  1 119 ? 113.317 33.009  17.997  1.00 2.00  ? 118 VAL J CB  1 
ATOM   10876 C  CG1 . VAL J  1 119 ? 113.472 32.408  19.367  1.00 2.00  ? 118 VAL J CG1 1 
ATOM   10877 C  CG2 . VAL J  1 119 ? 112.011 32.474  17.528  1.00 2.07  ? 118 VAL J CG2 1 
ATOM   10878 N  N   . VAL J  1 120 ? 114.756 35.411  19.817  1.00 2.00  ? 119 VAL J N   1 
ATOM   10879 C  CA  . VAL J  1 120 ? 116.089 35.667  20.327  1.00 3.57  ? 119 VAL J CA  1 
ATOM   10880 C  C   . VAL J  1 120 ? 116.323 34.560  21.347  1.00 6.03  ? 119 VAL J C   1 
ATOM   10881 O  O   . VAL J  1 120 ? 115.423 34.162  22.129  1.00 6.82  ? 119 VAL J O   1 
ATOM   10882 C  CB  . VAL J  1 120 ? 116.186 37.072  20.954  1.00 4.12  ? 119 VAL J CB  1 
ATOM   10883 C  CG1 . VAL J  1 120 ? 115.765 37.205  22.413  1.00 4.37  ? 119 VAL J CG1 1 
ATOM   10884 C  CG2 . VAL J  1 120 ? 117.666 37.418  20.843  1.00 2.64  ? 119 VAL J CG2 1 
ATOM   10885 N  N   . HIS J  1 121 ? 117.527 33.994  21.327  1.00 5.89  ? 120 HIS J N   1 
ATOM   10886 C  CA  . HIS J  1 121 ? 117.789 32.845  22.164  1.00 5.66  ? 120 HIS J CA  1 
ATOM   10887 C  C   . HIS J  1 121 ? 118.616 33.163  23.374  1.00 5.25  ? 120 HIS J C   1 
ATOM   10888 O  O   . HIS J  1 121 ? 119.279 34.189  23.459  1.00 7.70  ? 120 HIS J O   1 
ATOM   10889 C  CB  . HIS J  1 121 ? 118.511 31.742  21.387  1.00 6.10  ? 120 HIS J CB  1 
ATOM   10890 C  CG  . HIS J  1 121 ? 117.683 31.020  20.348  1.00 5.92  ? 120 HIS J CG  1 
ATOM   10891 N  ND1 . HIS J  1 121 ? 117.070 29.885  20.474  1.00 6.80  ? 120 HIS J ND1 1 
ATOM   10892 C  CD2 . HIS J  1 121 ? 117.535 31.404  19.029  1.00 8.02  ? 120 HIS J CD2 1 
ATOM   10893 C  CE1 . HIS J  1 121 ? 116.580 29.565  19.286  1.00 7.31  ? 120 HIS J CE1 1 
ATOM   10894 N  NE2 . HIS J  1 121 ? 116.854 30.482  18.386  1.00 9.84  ? 120 HIS J NE2 1 
ATOM   10895 N  N   . GLU J  1 122 ? 118.639 32.185  24.250  1.00 7.57  ? 121 GLU J N   1 
ATOM   10896 C  CA  . GLU J  1 122 ? 119.306 32.198  25.536  1.00 11.93 ? 121 GLU J CA  1 
ATOM   10897 C  C   . GLU J  1 122 ? 120.791 32.452  25.481  1.00 12.12 ? 121 GLU J C   1 
ATOM   10898 O  O   . GLU J  1 122 ? 121.264 33.377  26.154  1.00 11.43 ? 121 GLU J O   1 
ATOM   10899 C  CB  . GLU J  1 122 ? 119.011 30.870  26.150  1.00 15.06 ? 121 GLU J CB  1 
ATOM   10900 C  CG  . GLU J  1 122 ? 119.654 30.454  27.447  1.00 21.02 ? 121 GLU J CG  1 
ATOM   10901 C  CD  . GLU J  1 122 ? 119.225 29.011  27.740  1.00 25.77 ? 121 GLU J CD  1 
ATOM   10902 O  OE1 . GLU J  1 122 ? 118.134 28.802  28.278  1.00 27.20 ? 121 GLU J OE1 1 
ATOM   10903 O  OE2 . GLU J  1 122 ? 119.978 28.086  27.419  1.00 29.61 ? 121 GLU J OE2 1 
ATOM   10904 N  N   . LYS J  1 123 ? 121.441 31.613  24.652  1.00 13.12 ? 122 LYS J N   1 
ATOM   10905 C  CA  . LYS J  1 123 ? 122.883 31.524  24.459  1.00 10.44 ? 122 LYS J CA  1 
ATOM   10906 C  C   . LYS J  1 123 ? 123.286 31.861  23.017  1.00 8.17  ? 122 LYS J C   1 
ATOM   10907 O  O   . LYS J  1 123 ? 122.478 32.205  22.143  1.00 4.47  ? 122 LYS J O   1 
ATOM   10908 C  CB  . LYS J  1 123 ? 123.382 30.126  24.759  1.00 14.92 ? 122 LYS J CB  1 
ATOM   10909 C  CG  . LYS J  1 123 ? 123.136 29.461  26.126  1.00 18.14 ? 122 LYS J CG  1 
ATOM   10910 C  CD  . LYS J  1 123 ? 123.976 28.184  26.218  1.00 19.78 ? 122 LYS J CD  1 
ATOM   10911 C  CE  . LYS J  1 123 ? 123.509 27.186  25.161  1.00 24.63 ? 122 LYS J CE  1 
ATOM   10912 N  NZ  . LYS J  1 123 ? 124.274 25.941  25.158  1.00 26.28 ? 122 LYS J NZ  1 
ATOM   10913 N  N   . ALA J  1 124 ? 124.581 31.779  22.779  1.00 6.21  ? 123 ALA J N   1 
ATOM   10914 C  CA  . ALA J  1 124 ? 125.143 32.196  21.526  1.00 6.15  ? 123 ALA J CA  1 
ATOM   10915 C  C   . ALA J  1 124 ? 125.080 31.087  20.503  1.00 6.82  ? 123 ALA J C   1 
ATOM   10916 O  O   . ALA J  1 124 ? 125.317 29.898  20.776  1.00 7.13  ? 123 ALA J O   1 
ATOM   10917 C  CB  . ALA J  1 124 ? 126.564 32.583  21.741  1.00 2.00  ? 123 ALA J CB  1 
ATOM   10918 N  N   . ASP J  1 125 ? 124.742 31.526  19.299  1.00 5.27  ? 124 ASP J N   1 
ATOM   10919 C  CA  . ASP J  1 125 ? 124.659 30.623  18.187  1.00 5.43  ? 124 ASP J CA  1 
ATOM   10920 C  C   . ASP J  1 125 ? 126.123 30.430  17.838  1.00 7.48  ? 124 ASP J C   1 
ATOM   10921 O  O   . ASP J  1 125 ? 126.834 31.434  17.713  1.00 12.29 ? 124 ASP J O   1 
ATOM   10922 C  CB  . ASP J  1 125 ? 123.893 31.318  17.084  1.00 4.33  ? 124 ASP J CB  1 
ATOM   10923 C  CG  . ASP J  1 125 ? 123.834 30.633  15.729  1.00 4.80  ? 124 ASP J CG  1 
ATOM   10924 O  OD1 . ASP J  1 125 ? 124.577 29.691  15.477  1.00 3.74  ? 124 ASP J OD1 1 
ATOM   10925 O  OD2 . ASP J  1 125 ? 123.031 31.036  14.898  1.00 3.90  ? 124 ASP J OD2 1 
ATOM   10926 N  N   . ASP J  1 126 ? 126.631 29.225  17.596  1.00 6.31  ? 125 ASP J N   1 
ATOM   10927 C  CA  . ASP J  1 126 ? 128.057 29.024  17.238  1.00 6.11  ? 125 ASP J CA  1 
ATOM   10928 C  C   . ASP J  1 126 ? 128.383 29.054  15.742  1.00 4.48  ? 125 ASP J C   1 
ATOM   10929 O  O   . ASP J  1 126 ? 129.427 28.647  15.245  1.00 4.22  ? 125 ASP J O   1 
ATOM   10930 C  CB  . ASP J  1 126 ? 128.535 27.677  17.818  1.00 4.07  ? 125 ASP J CB  1 
ATOM   10931 C  CG  . ASP J  1 126 ? 127.784 26.442  17.329  1.00 5.02  ? 125 ASP J CG  1 
ATOM   10932 O  OD1 . ASP J  1 126 ? 127.052 26.459  16.329  1.00 2.72  ? 125 ASP J OD1 1 
ATOM   10933 O  OD2 . ASP J  1 126 ? 127.920 25.434  17.999  1.00 5.93  ? 125 ASP J OD2 1 
ATOM   10934 N  N   . LEU J  1 127 ? 127.367 29.443  15.001  1.00 5.38  ? 126 LEU J N   1 
ATOM   10935 C  CA  . LEU J  1 127 ? 127.336 29.508  13.552  1.00 5.91  ? 126 LEU J CA  1 
ATOM   10936 C  C   . LEU J  1 127 ? 127.703 28.190  12.833  1.00 7.81  ? 126 LEU J C   1 
ATOM   10937 O  O   . LEU J  1 127 ? 128.274 28.174  11.756  1.00 11.12 ? 126 LEU J O   1 
ATOM   10938 C  CB  . LEU J  1 127 ? 128.229 30.697  13.119  1.00 2.00  ? 126 LEU J CB  1 
ATOM   10939 C  CG  . LEU J  1 127 ? 128.167 32.009  13.991  1.00 3.76  ? 126 LEU J CG  1 
ATOM   10940 C  CD1 . LEU J  1 127 ? 129.280 32.931  13.574  1.00 2.00  ? 126 LEU J CD1 1 
ATOM   10941 C  CD2 . LEU J  1 127 ? 126.812 32.631  13.934  1.00 2.00  ? 126 LEU J CD2 1 
ATOM   10942 N  N   . GLY J  1 128 ? 127.327 27.027  13.349  1.00 7.77  ? 127 GLY J N   1 
ATOM   10943 C  CA  . GLY J  1 128 ? 127.553 25.753  12.662  1.00 7.11  ? 127 GLY J CA  1 
ATOM   10944 C  C   . GLY J  1 128 ? 128.950 25.179  12.903  1.00 7.52  ? 127 GLY J C   1 
ATOM   10945 O  O   . GLY J  1 128 ? 129.284 24.101  12.426  1.00 5.32  ? 127 GLY J O   1 
ATOM   10946 N  N   . LYS J  1 129 ? 129.730 25.884  13.729  1.00 7.51  ? 128 LYS J N   1 
ATOM   10947 C  CA  . LYS J  1 129 ? 131.126 25.600  13.991  1.00 6.28  ? 128 LYS J CA  1 
ATOM   10948 C  C   . LYS J  1 129 ? 131.343 24.860  15.268  1.00 6.44  ? 128 LYS J C   1 
ATOM   10949 O  O   . LYS J  1 129 ? 132.465 24.829  15.707  1.00 6.21  ? 128 LYS J O   1 
ATOM   10950 C  CB  . LYS J  1 129 ? 131.855 26.921  14.025  1.00 7.69  ? 128 LYS J CB  1 
ATOM   10951 C  CG  . LYS J  1 129 ? 132.068 27.701  12.742  1.00 7.62  ? 128 LYS J CG  1 
ATOM   10952 C  CD  . LYS J  1 129 ? 132.663 29.075  13.098  1.00 14.37 ? 128 LYS J CD  1 
ATOM   10953 C  CE  . LYS J  1 129 ? 134.159 29.138  13.496  1.00 15.80 ? 128 LYS J CE  1 
ATOM   10954 N  NZ  . LYS J  1 129 ? 135.048 29.098  12.336  1.00 16.83 ? 128 LYS J NZ  1 
ATOM   10955 N  N   . GLY J  1 130 ? 130.333 24.268  15.894  1.00 8.61  ? 129 GLY J N   1 
ATOM   10956 C  CA  . GLY J  1 130 ? 130.485 23.624  17.189  1.00 5.61  ? 129 GLY J CA  1 
ATOM   10957 C  C   . GLY J  1 130 ? 130.817 22.162  17.104  1.00 3.30  ? 129 GLY J C   1 
ATOM   10958 O  O   . GLY J  1 130 ? 131.105 21.558  18.127  1.00 3.68  ? 129 GLY J O   1 
ATOM   10959 N  N   . GLY J  1 131 ? 130.741 21.494  15.972  1.00 3.50  ? 130 GLY J N   1 
ATOM   10960 C  CA  . GLY J  1 131 ? 131.232 20.116  15.850  1.00 2.00  ? 130 GLY J CA  1 
ATOM   10961 C  C   . GLY J  1 131 ? 130.325 19.040  16.385  1.00 2.00  ? 130 GLY J C   1 
ATOM   10962 O  O   . GLY J  1 131 ? 130.672 17.863  16.433  1.00 2.00  ? 130 GLY J O   1 
ATOM   10963 N  N   . ASN J  1 132 ? 129.146 19.401  16.810  1.00 2.00  ? 131 ASN J N   1 
ATOM   10964 C  CA  . ASN J  1 132 ? 128.205 18.411  17.241  1.00 2.00  ? 131 ASN J CA  1 
ATOM   10965 C  C   . ASN J  1 132 ? 127.000 18.520  16.321  1.00 2.60  ? 131 ASN J C   1 
ATOM   10966 O  O   . ASN J  1 132 ? 126.847 19.460  15.534  1.00 2.62  ? 131 ASN J O   1 
ATOM   10967 C  CB  . ASN J  1 132 ? 127.833 18.636  18.733  1.00 2.00  ? 131 ASN J CB  1 
ATOM   10968 C  CG  . ASN J  1 132 ? 126.954 19.829  19.087  1.00 4.49  ? 131 ASN J CG  1 
ATOM   10969 O  OD1 . ASN J  1 132 ? 126.860 20.864  18.398  1.00 3.46  ? 131 ASN J OD1 1 
ATOM   10970 N  ND2 . ASN J  1 132 ? 126.260 19.691  20.210  1.00 4.30  ? 131 ASN J ND2 1 
ATOM   10971 N  N   . GLU J  1 133 ? 126.140 17.511  16.344  1.00 4.41  ? 132 GLU J N   1 
ATOM   10972 C  CA  . GLU J  1 133 ? 124.914 17.545  15.566  1.00 7.50  ? 132 GLU J CA  1 
ATOM   10973 C  C   . GLU J  1 133 ? 124.081 18.816  15.681  1.00 5.33  ? 132 GLU J C   1 
ATOM   10974 O  O   . GLU J  1 133 ? 123.700 19.440  14.709  1.00 5.73  ? 132 GLU J O   1 
ATOM   10975 C  CB  . GLU J  1 133 ? 124.031 16.423  15.963  1.00 8.75  ? 132 GLU J CB  1 
ATOM   10976 C  CG  . GLU J  1 133 ? 124.635 15.112  15.622  1.00 17.17 ? 132 GLU J CG  1 
ATOM   10977 C  CD  . GLU J  1 133 ? 123.736 13.933  15.965  1.00 24.66 ? 132 GLU J CD  1 
ATOM   10978 O  OE1 . GLU J  1 133 ? 122.535 14.100  16.205  1.00 28.06 ? 132 GLU J OE1 1 
ATOM   10979 O  OE2 . GLU J  1 133 ? 124.253 12.813  15.986  1.00 31.38 ? 132 GLU J OE2 1 
ATOM   10980 N  N   . GLU J  1 134 ? 123.834 19.250  16.898  1.00 6.68  ? 133 GLU J N   1 
ATOM   10981 C  CA  . GLU J  1 134 ? 123.021 20.412  17.184  1.00 8.51  ? 133 GLU J CA  1 
ATOM   10982 C  C   . GLU J  1 134 ? 123.520 21.694  16.535  1.00 9.16  ? 133 GLU J C   1 
ATOM   10983 O  O   . GLU J  1 134 ? 122.726 22.572  16.157  1.00 8.91  ? 133 GLU J O   1 
ATOM   10984 C  CB  . GLU J  1 134 ? 122.974 20.570  18.677  1.00 10.31 ? 133 GLU J CB  1 
ATOM   10985 C  CG  . GLU J  1 134 ? 121.903 21.538  19.113  1.00 15.20 ? 133 GLU J CG  1 
ATOM   10986 C  CD  . GLU J  1 134 ? 120.465 21.055  18.980  1.00 19.84 ? 133 GLU J CD  1 
ATOM   10987 O  OE1 . GLU J  1 134 ? 120.219 19.882  18.677  1.00 20.01 ? 133 GLU J OE1 1 
ATOM   10988 O  OE2 . GLU J  1 134 ? 119.583 21.884  19.223  1.00 22.00 ? 133 GLU J OE2 1 
ATOM   10989 N  N   . SER J  1 135 ? 124.843 21.748  16.326  1.00 7.13  ? 134 SER J N   1 
ATOM   10990 C  CA  . SER J  1 135 ? 125.457 22.869  15.728  1.00 3.77  ? 134 SER J CA  1 
ATOM   10991 C  C   . SER J  1 135 ? 124.870 23.165  14.391  1.00 5.28  ? 134 SER J C   1 
ATOM   10992 O  O   . SER J  1 135 ? 124.671 24.353  14.090  1.00 7.93  ? 134 SER J O   1 
ATOM   10993 C  CB  . SER J  1 135 ? 126.874 22.628  15.554  1.00 2.00  ? 134 SER J CB  1 
ATOM   10994 O  OG  . SER J  1 135 ? 127.420 23.929  15.447  1.00 2.37  ? 134 SER J OG  1 
ATOM   10995 N  N   . THR J  1 136 ? 124.552 22.131  13.625  1.00 4.69  ? 135 THR J N   1 
ATOM   10996 C  CA  . THR J  1 136 ? 124.090 22.331  12.267  1.00 5.07  ? 135 THR J CA  1 
ATOM   10997 C  C   . THR J  1 136 ? 122.596 22.311  12.060  1.00 4.71  ? 135 THR J C   1 
ATOM   10998 O  O   . THR J  1 136 ? 122.121 22.285  10.933  1.00 3.49  ? 135 THR J O   1 
ATOM   10999 C  CB  . THR J  1 136 ? 124.799 21.287  11.403  1.00 8.19  ? 135 THR J CB  1 
ATOM   11000 O  OG1 . THR J  1 136 ? 124.791 20.033  12.120  1.00 9.46  ? 135 THR J OG1 1 
ATOM   11001 C  CG2 . THR J  1 136 ? 126.208 21.793  11.025  1.00 2.00  ? 135 THR J CG2 1 
ATOM   11002 N  N   . LYS J  1 137 ? 121.893 22.409  13.190  1.00 6.25  ? 136 LYS J N   1 
ATOM   11003 C  CA  . LYS J  1 137 ? 120.444 22.445  13.282  1.00 6.12  ? 136 LYS J CA  1 
ATOM   11004 C  C   . LYS J  1 137 ? 120.003 23.785  13.870  1.00 6.93  ? 136 LYS J C   1 
ATOM   11005 O  O   . LYS J  1 137 ? 119.380 24.621  13.194  1.00 8.28  ? 136 LYS J O   1 
ATOM   11006 C  CB  . LYS J  1 137 ? 119.998 21.281  14.171  1.00 9.54  ? 136 LYS J CB  1 
ATOM   11007 C  CG  . LYS J  1 137 ? 119.801 19.907  13.479  1.00 11.54 ? 136 LYS J CG  1 
ATOM   11008 C  CD  . LYS J  1 137 ? 119.838 18.751  14.459  1.00 16.36 ? 136 LYS J CD  1 
ATOM   11009 C  CE  . LYS J  1 137 ? 119.006 18.967  15.737  1.00 19.04 ? 136 LYS J CE  1 
ATOM   11010 N  NZ  . LYS J  1 137 ? 119.264 17.883  16.686  1.00 24.47 ? 136 LYS J NZ  1 
ATOM   11011 N  N   . THR J  1 138 ? 120.413 24.024  15.119  1.00 6.22  ? 137 THR J N   1 
ATOM   11012 C  CA  . THR J  1 138 ? 120.054 25.218  15.851  1.00 7.02  ? 137 THR J CA  1 
ATOM   11013 C  C   . THR J  1 138 ? 121.205 26.126  16.161  1.00 8.15  ? 137 THR J C   1 
ATOM   11014 O  O   . THR J  1 138 ? 121.063 27.209  16.747  1.00 12.27 ? 137 THR J O   1 
ATOM   11015 C  CB  . THR J  1 138 ? 119.426 24.899  17.220  1.00 9.40  ? 137 THR J CB  1 
ATOM   11016 O  OG1 . THR J  1 138 ? 120.412 24.166  17.960  1.00 9.37  ? 137 THR J OG1 1 
ATOM   11017 C  CG2 . THR J  1 138 ? 118.108 24.151  17.100  1.00 6.37  ? 137 THR J CG2 1 
ATOM   11018 N  N   . GLY J  1 139 ? 122.403 25.614  15.947  1.00 9.39  ? 138 GLY J N   1 
ATOM   11019 C  CA  . GLY J  1 139 ? 123.582 26.366  16.309  1.00 8.53  ? 138 GLY J CA  1 
ATOM   11020 C  C   . GLY J  1 139 ? 123.842 26.338  17.795  1.00 7.21  ? 138 GLY J C   1 
ATOM   11021 O  O   . GLY J  1 139 ? 124.683 27.123  18.196  1.00 9.10  ? 138 GLY J O   1 
ATOM   11022 N  N   . ASN J  1 140 ? 123.233 25.503  18.633  1.00 6.35  ? 139 ASN J N   1 
ATOM   11023 C  CA  . ASN J  1 140 ? 123.468 25.474  20.087  1.00 7.57  ? 139 ASN J CA  1 
ATOM   11024 C  C   . ASN J  1 140 ? 123.101 26.784  20.780  1.00 10.26 ? 139 ASN J C   1 
ATOM   11025 O  O   . ASN J  1 140 ? 123.675 27.167  21.803  1.00 11.09 ? 139 ASN J O   1 
ATOM   11026 C  CB  . ASN J  1 140 ? 124.904 25.201  20.434  1.00 4.70  ? 139 ASN J CB  1 
ATOM   11027 C  CG  . ASN J  1 140 ? 125.219 23.792  20.095  1.00 7.48  ? 139 ASN J CG  1 
ATOM   11028 O  OD1 . ASN J  1 140 ? 124.623 22.892  20.641  1.00 12.89 ? 139 ASN J OD1 1 
ATOM   11029 N  ND2 . ASN J  1 140 ? 126.059 23.443  19.144  1.00 10.62 ? 139 ASN J ND2 1 
ATOM   11030 N  N   . ALA J  1 141 ? 122.100 27.493  20.244  1.00 8.24  ? 140 ALA J N   1 
ATOM   11031 C  CA  . ALA J  1 141 ? 121.684 28.742  20.826  1.00 8.15  ? 140 ALA J CA  1 
ATOM   11032 C  C   . ALA J  1 141 ? 120.835 28.624  22.100  1.00 9.09  ? 140 ALA J C   1 
ATOM   11033 O  O   . ALA J  1 141 ? 120.628 29.614  22.808  1.00 11.39 ? 140 ALA J O   1 
ATOM   11034 C  CB  . ALA J  1 141 ? 120.932 29.524  19.747  1.00 6.57  ? 140 ALA J CB  1 
ATOM   11035 N  N   . GLY J  1 142 ? 120.251 27.476  22.427  1.00 8.01  ? 141 GLY J N   1 
ATOM   11036 C  CA  . GLY J  1 142 ? 119.499 27.322  23.657  1.00 9.68  ? 141 GLY J CA  1 
ATOM   11037 C  C   . GLY J  1 142 ? 118.057 27.786  23.555  1.00 13.11 ? 141 GLY J C   1 
ATOM   11038 O  O   . GLY J  1 142 ? 117.507 27.987  22.454  1.00 13.03 ? 141 GLY J O   1 
ATOM   11039 N  N   . SER J  1 143 ? 117.452 27.964  24.740  1.00 15.06 ? 142 SER J N   1 
ATOM   11040 C  CA  . SER J  1 143 ? 116.064 28.387  24.857  1.00 14.67 ? 142 SER J CA  1 
ATOM   11041 C  C   . SER J  1 143 ? 115.659 29.600  24.076  1.00 13.36 ? 142 SER J C   1 
ATOM   11042 O  O   . SER J  1 143 ? 116.517 30.407  23.756  1.00 13.94 ? 142 SER J O   1 
ATOM   11043 C  CB  . SER J  1 143 ? 115.734 28.627  26.300  1.00 14.38 ? 142 SER J CB  1 
ATOM   11044 O  OG  . SER J  1 143 ? 115.789 27.342  26.919  1.00 18.96 ? 142 SER J OG  1 
ATOM   11045 N  N   . ARG J  1 144 ? 114.372 29.652  23.717  1.00 13.14 ? 143 ARG J N   1 
ATOM   11046 C  CA  . ARG J  1 144 ? 113.781 30.744  22.974  1.00 10.48 ? 143 ARG J CA  1 
ATOM   11047 C  C   . ARG J  1 144 ? 113.279 31.597  24.127  1.00 11.11 ? 143 ARG J C   1 
ATOM   11048 O  O   . ARG J  1 144 ? 112.539 31.076  24.973  1.00 11.93 ? 143 ARG J O   1 
ATOM   11049 C  CB  . ARG J  1 144 ? 112.615 30.238  22.102  1.00 8.70  ? 143 ARG J CB  1 
ATOM   11050 C  CG  . ARG J  1 144 ? 112.944 29.033  21.210  1.00 10.36 ? 143 ARG J CG  1 
ATOM   11051 C  CD  . ARG J  1 144 ? 111.839 28.571  20.254  1.00 8.96  ? 143 ARG J CD  1 
ATOM   11052 N  NE  . ARG J  1 144 ? 112.310 27.432  19.482  1.00 8.10  ? 143 ARG J NE  1 
ATOM   11053 C  CZ  . ARG J  1 144 ? 111.614 26.843  18.509  1.00 7.95  ? 143 ARG J CZ  1 
ATOM   11054 N  NH1 . ARG J  1 144 ? 110.405 27.263  18.166  1.00 9.23  ? 143 ARG J NH1 1 
ATOM   11055 N  NH2 . ARG J  1 144 ? 112.142 25.806  17.864  1.00 5.89  ? 143 ARG J NH2 1 
ATOM   11056 N  N   . LEU J  1 145 ? 113.705 32.862  24.173  1.00 10.79 ? 144 LEU J N   1 
ATOM   11057 C  CA  . LEU J  1 145 ? 113.463 33.802  25.271  1.00 10.55 ? 144 LEU J CA  1 
ATOM   11058 C  C   . LEU J  1 145 ? 112.314 34.785  25.154  1.00 10.99 ? 144 LEU J C   1 
ATOM   11059 O  O   . LEU J  1 145 ? 111.695 35.243  26.120  1.00 13.33 ? 144 LEU J O   1 
ATOM   11060 C  CB  . LEU J  1 145 ? 114.689 34.661  25.504  1.00 9.57  ? 144 LEU J CB  1 
ATOM   11061 C  CG  . LEU J  1 145 ? 116.039 34.088  25.831  1.00 8.06  ? 144 LEU J CG  1 
ATOM   11062 C  CD1 . LEU J  1 145 ? 117.045 35.221  25.943  1.00 5.04  ? 144 LEU J CD1 1 
ATOM   11063 C  CD2 . LEU J  1 145 ? 115.944 33.285  27.107  1.00 6.46  ? 144 LEU J CD2 1 
ATOM   11064 N  N   . ALA J  1 146 ? 112.212 35.234  23.926  1.00 10.57 ? 145 ALA J N   1 
ATOM   11065 C  CA  . ALA J  1 146 ? 111.258 36.216  23.506  1.00 11.61 ? 145 ALA J CA  1 
ATOM   11066 C  C   . ALA J  1 146 ? 111.044 35.917  22.038  1.00 11.54 ? 145 ALA J C   1 
ATOM   11067 O  O   . ALA J  1 146 ? 111.963 35.419  21.383  1.00 13.45 ? 145 ALA J O   1 
ATOM   11068 C  CB  . ALA J  1 146 ? 111.842 37.605  23.643  1.00 14.56 ? 145 ALA J CB  1 
ATOM   11069 N  N   . CYS J  1 147 ? 109.884 36.156  21.466  1.00 11.15 ? 146 CYS J N   1 
ATOM   11070 C  CA  . CYS J  1 147 ? 109.679 35.908  20.058  1.00 10.49 ? 146 CYS J CA  1 
ATOM   11071 C  C   . CYS J  1 147 ? 108.461 36.674  19.661  1.00 10.01 ? 146 CYS J C   1 
ATOM   11072 O  O   . CYS J  1 147 ? 107.782 37.188  20.540  1.00 11.35 ? 146 CYS J O   1 
ATOM   11073 C  CB  . CYS J  1 147 ? 109.459 34.430  19.781  1.00 12.07 ? 146 CYS J CB  1 
ATOM   11074 S  SG  . CYS J  1 147 ? 108.079 33.653  20.646  1.00 10.70 ? 146 CYS J SG  1 
ATOM   11075 N  N   . GLY J  1 148 ? 108.169 36.823  18.376  1.00 10.98 ? 147 GLY J N   1 
ATOM   11076 C  CA  . GLY J  1 148 ? 107.037 37.621  17.936  1.00 7.74  ? 147 GLY J CA  1 
ATOM   11077 C  C   . GLY J  1 148 ? 106.819 37.362  16.473  1.00 6.91  ? 147 GLY J C   1 
ATOM   11078 O  O   . GLY J  1 148 ? 107.787 36.953  15.827  1.00 7.35  ? 147 GLY J O   1 
ATOM   11079 N  N   . VAL J  1 149 ? 105.621 37.629  15.930  1.00 8.07  ? 148 VAL J N   1 
ATOM   11080 C  CA  . VAL J  1 149 ? 105.303 37.295  14.543  1.00 7.30  ? 148 VAL J CA  1 
ATOM   11081 C  C   . VAL J  1 149 ? 105.656 38.536  13.711  1.00 8.83  ? 148 VAL J C   1 
ATOM   11082 O  O   . VAL J  1 149 ? 105.373 39.695  14.085  1.00 11.51 ? 148 VAL J O   1 
ATOM   11083 C  CB  . VAL J  1 149 ? 103.760 36.872  14.418  1.00 5.84  ? 148 VAL J CB  1 
ATOM   11084 C  CG1 . VAL J  1 149 ? 103.429 36.388  13.012  1.00 3.26  ? 148 VAL J CG1 1 
ATOM   11085 C  CG2 . VAL J  1 149 ? 103.446 35.631  15.254  1.00 2.00  ? 148 VAL J CG2 1 
ATOM   11086 N  N   . ILE J  1 150 ? 106.339 38.304  12.593  1.00 7.07  ? 149 ILE J N   1 
ATOM   11087 C  CA  . ILE J  1 150 ? 106.800 39.380  11.747  1.00 6.16  ? 149 ILE J CA  1 
ATOM   11088 C  C   . ILE J  1 150 ? 105.610 39.817  10.918  1.00 6.44  ? 149 ILE J C   1 
ATOM   11089 O  O   . ILE J  1 150 ? 105.172 39.066  10.037  1.00 7.29  ? 149 ILE J O   1 
ATOM   11090 C  CB  . ILE J  1 150 ? 107.958 38.868  10.859  1.00 5.18  ? 149 ILE J CB  1 
ATOM   11091 C  CG1 . ILE J  1 150 ? 109.125 38.386  11.716  1.00 5.38  ? 149 ILE J CG1 1 
ATOM   11092 C  CG2 . ILE J  1 150 ? 108.458 39.997  9.981   1.00 6.21  ? 149 ILE J CG2 1 
ATOM   11093 C  CD1 . ILE J  1 150 ? 110.088 37.374  11.057  1.00 2.89  ? 149 ILE J CD1 1 
ATOM   11094 N  N   . GLY J  1 151 ? 105.030 40.973  11.194  1.00 4.13  ? 150 GLY J N   1 
ATOM   11095 C  CA  . GLY J  1 151 ? 103.973 41.475  10.350  1.00 5.12  ? 150 GLY J CA  1 
ATOM   11096 C  C   . GLY J  1 151 ? 104.359 42.736  9.575   1.00 8.66  ? 150 GLY J C   1 
ATOM   11097 O  O   . GLY J  1 151 ? 105.287 43.504  9.868   1.00 10.30 ? 150 GLY J O   1 
ATOM   11098 N  N   . ILE J  1 152 ? 103.545 42.996  8.568   1.00 9.51  ? 151 ILE J N   1 
ATOM   11099 C  CA  . ILE J  1 152 ? 103.690 44.098  7.650   1.00 9.32  ? 151 ILE J CA  1 
ATOM   11100 C  C   . ILE J  1 152 ? 103.570 45.402  8.362   1.00 13.70 ? 151 ILE J C   1 
ATOM   11101 O  O   . ILE J  1 152 ? 102.698 45.545  9.219   1.00 14.69 ? 151 ILE J O   1 
ATOM   11102 C  CB  . ILE J  1 152 ? 102.628 43.961  6.627   1.00 6.86  ? 151 ILE J CB  1 
ATOM   11103 C  CG1 . ILE J  1 152 ? 103.109 42.844  5.769   1.00 2.09  ? 151 ILE J CG1 1 
ATOM   11104 C  CG2 . ILE J  1 152 ? 102.321 45.275  5.886   1.00 6.02  ? 151 ILE J CG2 1 
ATOM   11105 C  CD1 . ILE J  1 152 ? 101.932 42.314  4.985   1.00 5.92  ? 151 ILE J CD1 1 
ATOM   11106 N  N   . ALA J  1 153 ? 104.420 46.345  7.968   1.00 18.07 ? 152 ALA J N   1 
ATOM   11107 C  CA  . ALA J  1 153 ? 104.397 47.651  8.585   1.00 21.53 ? 152 ALA J CA  1 
ATOM   11108 C  C   . ALA J  1 153 ? 104.105 48.762  7.587   1.00 24.54 ? 152 ALA J C   1 
ATOM   11109 O  O   . ALA J  1 153 ? 104.077 48.580  6.364   1.00 24.49 ? 152 ALA J O   1 
ATOM   11110 C  CB  . ALA J  1 153 ? 105.734 47.879  9.284   1.00 20.26 ? 152 ALA J CB  1 
ATOM   11111 N  N   . GLN J  1 154 ? 103.807 49.870  8.263   1.00 30.55 ? 153 GLN J N   1 
ATOM   11112 C  CA  . GLN J  1 154 ? 103.409 51.154  7.698   1.00 34.98 ? 153 GLN J CA  1 
ATOM   11113 C  C   . GLN J  1 154 ? 104.656 51.999  7.373   1.00 36.68 ? 153 GLN J C   1 
ATOM   11114 O  O   . GLN J  1 154 ? 104.865 52.297  6.188   1.00 37.71 ? 153 GLN J O   1 
ATOM   11115 C  CB  . GLN J  1 154 ? 102.462 51.795  8.764   1.00 37.38 ? 153 GLN J CB  1 
ATOM   11116 C  CG  . GLN J  1 154 ? 102.078 53.294  8.769   1.00 41.63 ? 153 GLN J CG  1 
ATOM   11117 C  CD  . GLN J  1 154 ? 101.542 53.946  7.481   1.00 44.24 ? 153 GLN J CD  1 
ATOM   11118 O  OE1 . GLN J  1 154 ? 100.378 54.376  7.405   1.00 46.14 ? 153 GLN J OE1 1 
ATOM   11119 N  NE2 . GLN J  1 154 ? 102.337 54.087  6.420   1.00 43.55 ? 153 GLN J NE2 1 
ATOM   11120 O  OXT . GLN J  1 154 ? 105.390 52.369  8.302   1.00 37.74 ? 153 GLN J OXT 1 
HETATM 11121 CU CU  . CU  K  2 .   ? 63.696  46.906  18.602  1.00 15.93 ? 154 CU  A CU  1 
HETATM 11122 ZN ZN  . ZN  L  3 .   ? 63.194  49.433  12.992  1.00 6.87  ? 155 ZN  A ZN  1 
HETATM 11123 CU CU  . CU  M  2 .   ? 62.254  13.817  21.001  1.00 13.18 ? 154 CU  F CU  1 
HETATM 11124 ZN ZN  . ZN  N  3 .   ? 61.647  10.425  15.941  1.00 2.00  ? 155 ZN  F ZN  1 
HETATM 11125 S  S   . SO4 O  4 .   ? 73.089  0.059   13.050  1.00 63.24 ? 356 SO4 F S   1 
HETATM 11126 O  O1  . SO4 O  4 .   ? 72.292  0.591   14.129  1.00 62.54 ? 356 SO4 F O1  1 
HETATM 11127 O  O2  . SO4 O  4 .   ? 73.431  -1.315  13.295  1.00 60.63 ? 356 SO4 F O2  1 
HETATM 11128 O  O3  . SO4 O  4 .   ? 74.300  0.825   12.907  1.00 61.16 ? 356 SO4 F O3  1 
HETATM 11129 O  O4  . SO4 O  4 .   ? 72.303  0.175   11.857  1.00 61.85 ? 356 SO4 F O4  1 
HETATM 11130 CU CU  . CU  P  2 .   ? 119.855 -14.117 18.810  1.00 20.06 ? 154 CU  B CU  1 
HETATM 11131 ZN ZN  . ZN  Q  3 .   ? 122.628 -15.052 13.282  1.00 7.57  ? 155 ZN  B ZN  1 
HETATM 11132 CU CU  . CU  R  2 .   ? 91.088  2.660   20.923  1.00 8.75  ? 154 CU  G CU  1 
HETATM 11133 ZN ZN  . ZN  S  3 .   ? 88.395  4.503   15.799  1.00 2.00  ? 155 ZN  G ZN  1 
HETATM 11134 CU CU  . CU  T  2 .   ? 38.202  -33.855 18.898  1.00 12.01 ? 154 CU  C CU  1 
HETATM 11135 ZN ZN  . ZN  U  3 .   ? 36.118  -35.283 13.324  1.00 10.36 ? 155 ZN  C ZN  1 
HETATM 11136 CU CU  . CU  V  2 .   ? 66.971  -17.095 21.084  1.00 12.91 ? 154 CU  H CU  1 
HETATM 11137 ZN ZN  . ZN  W  3 .   ? 69.888  -15.604 15.884  1.00 4.83  ? 155 ZN  H ZN  1 
HETATM 11138 CU CU  . CU  X  2 .   ? 145.293 -14.308 17.195  1.00 21.05 ? 154 CU  D CU  1 
HETATM 11139 ZN ZN  . ZN  Y  3 .   ? 146.856 -16.869 11.840  1.00 15.23 ? 155 ZN  D ZN  1 
HETATM 11140 CU CU  . CU  Z  2 .   ? 145.533 18.665  19.906  1.00 10.16 ? 154 CU  I CU  1 
HETATM 11141 ZN ZN  . ZN  AA 3 .   ? 146.858 22.209  14.945  1.00 3.76  ? 155 ZN  I ZN  1 
HETATM 11142 S  S   . SO4 BA 4 .   ? 135.161 32.231  10.604  1.00 74.56 ? 357 SO4 I S   1 
HETATM 11143 O  O1  . SO4 BA 4 .   ? 135.651 30.997  10.051  1.00 74.18 ? 357 SO4 I O1  1 
HETATM 11144 O  O2  . SO4 BA 4 .   ? 135.485 33.313  9.727   1.00 72.98 ? 357 SO4 I O2  1 
HETATM 11145 O  O3  . SO4 BA 4 .   ? 135.797 32.415  11.878  1.00 73.69 ? 357 SO4 I O3  1 
HETATM 11146 O  O4  . SO4 BA 4 .   ? 133.734 32.179  10.790  1.00 73.78 ? 357 SO4 I O4  1 
HETATM 11147 CU CU  . CU  CA 2 .   ? 88.017  46.797  12.888  1.00 28.35 ? 154 CU  E CU  1 
HETATM 11148 ZN ZN  . ZN  DA 3 .   ? 85.684  47.599  7.194   1.00 15.62 ? 155 ZN  E ZN  1 
HETATM 11149 CU CU  . CU  EA 2 .   ? 116.523 29.830  16.447  1.00 11.66 ? 154 CU  J CU  1 
HETATM 11150 ZN ZN  . ZN  FA 3 .   ? 119.608 28.001  11.596  1.00 8.34  ? 155 ZN  J ZN  1 
HETATM 11151 O  O   . HOH GA 5 .   ? 49.261  27.326  19.624  1.00 25.08 ? 156 HOH A O   1 
HETATM 11152 O  O   . HOH GA 5 .   ? 61.911  56.823  23.818  1.00 33.86 ? 157 HOH A O   1 
HETATM 11153 O  O   . HOH GA 5 .   ? 55.663  30.927  32.803  1.00 40.12 ? 158 HOH A O   1 
HETATM 11154 O  O   . HOH GA 5 .   ? 59.632  31.454  21.669  1.00 2.27  ? 159 HOH A O   1 
HETATM 11155 O  O   . HOH GA 5 .   ? 67.852  41.381  36.971  1.00 30.33 ? 160 HOH A O   1 
HETATM 11156 O  O   . HOH GA 5 .   ? 69.881  35.913  39.882  1.00 43.91 ? 161 HOH A O   1 
HETATM 11157 O  O   . HOH GA 5 .   ? 60.508  37.207  37.381  1.00 23.82 ? 162 HOH A O   1 
HETATM 11158 O  O   . HOH GA 5 .   ? 49.292  29.285  3.872   1.00 31.18 ? 163 HOH A O   1 
HETATM 11159 O  O   . HOH GA 5 .   ? 56.722  31.435  -0.728  1.00 33.18 ? 164 HOH A O   1 
HETATM 11160 O  O   . HOH GA 5 .   ? 48.846  32.745  -2.170  1.00 2.00  ? 165 HOH A O   1 
HETATM 11161 O  O   . HOH GA 5 .   ? 49.310  40.907  -1.475  1.00 8.48  ? 166 HOH A O   1 
HETATM 11162 O  O   . HOH GA 5 .   ? 44.935  44.439  32.920  1.00 18.42 ? 167 HOH A O   1 
HETATM 11163 O  O   . HOH GA 5 .   ? 58.313  47.472  32.562  1.00 11.17 ? 168 HOH A O   1 
HETATM 11164 O  O   . HOH GA 5 .   ? 45.491  58.789  24.758  1.00 34.82 ? 169 HOH A O   1 
HETATM 11165 O  O   . HOH GA 5 .   ? 68.412  31.335  20.215  1.00 2.00  ? 170 HOH A O   1 
HETATM 11166 O  O   . HOH GA 5 .   ? 63.303  46.191  5.493   1.00 9.42  ? 171 HOH A O   1 
HETATM 11167 O  O   . HOH GA 5 .   ? 57.347  45.771  1.563   1.00 18.43 ? 172 HOH A O   1 
HETATM 11168 O  O   . HOH GA 5 .   ? 61.428  47.673  4.595   1.00 2.00  ? 173 HOH A O   1 
HETATM 11169 O  O   . HOH GA 5 .   ? 67.848  51.584  9.725   1.00 23.80 ? 174 HOH A O   1 
HETATM 11170 O  O   . HOH GA 5 .   ? 68.178  43.505  9.342   1.00 8.98  ? 175 HOH A O   1 
HETATM 11171 O  O   . HOH GA 5 .   ? 60.032  56.420  8.716   1.00 12.30 ? 176 HOH A O   1 
HETATM 11172 O  O   . HOH GA 5 .   ? 69.126  51.324  6.670   1.00 39.59 ? 177 HOH A O   1 
HETATM 11173 O  O   . HOH GA 5 .   ? 47.191  50.431  6.003   1.00 48.74 ? 178 HOH A O   1 
HETATM 11174 O  O   . HOH GA 5 .   ? 48.491  48.436  13.272  1.00 30.33 ? 179 HOH A O   1 
HETATM 11175 O  O   . HOH GA 5 .   ? 44.502  39.979  22.364  1.00 20.74 ? 180 HOH A O   1 
HETATM 11176 O  O   . HOH GA 5 .   ? 41.417  41.207  18.379  1.00 51.51 ? 181 HOH A O   1 
HETATM 11177 O  O   . HOH GA 5 .   ? 66.711  52.846  21.225  1.00 36.31 ? 182 HOH A O   1 
HETATM 11178 O  O   . HOH GA 5 .   ? 72.786  44.439  27.226  1.00 24.35 ? 183 HOH A O   1 
HETATM 11179 O  O   . HOH GA 5 .   ? 69.304  45.835  26.061  1.00 23.91 ? 184 HOH A O   1 
HETATM 11180 O  O   . HOH GA 5 .   ? 72.586  47.625  28.326  1.00 30.64 ? 185 HOH A O   1 
HETATM 11181 O  O   . HOH GA 5 .   ? 70.702  45.139  23.904  1.00 32.56 ? 186 HOH A O   1 
HETATM 11182 O  O   . HOH GA 5 .   ? 56.398  42.929  0.788   1.00 13.69 ? 187 HOH A O   1 
HETATM 11183 O  O   . HOH GA 5 .   ? 68.988  41.371  6.329   1.00 27.34 ? 188 HOH A O   1 
HETATM 11184 O  O   . HOH GA 5 .   ? 68.186  54.170  26.977  1.00 40.85 ? 189 HOH A O   1 
HETATM 11185 O  O   . HOH GA 5 .   ? 67.156  48.600  19.742  1.00 17.99 ? 190 HOH A O   1 
HETATM 11186 O  O   . HOH GA 5 .   ? 69.405  42.257  26.678  1.00 36.75 ? 191 HOH A O   1 
HETATM 11187 O  O   . HOH GA 5 .   ? 68.676  56.343  23.006  1.00 42.38 ? 192 HOH A O   1 
HETATM 11188 O  O   . HOH GA 5 .   ? 71.290  60.010  17.072  1.00 27.09 ? 193 HOH A O   1 
HETATM 11189 O  O   . HOH GA 5 .   ? 63.415  65.525  11.967  1.00 35.84 ? 194 HOH A O   1 
HETATM 11190 O  O   . HOH GA 5 .   ? 71.209  61.672  10.307  1.00 38.87 ? 195 HOH A O   1 
HETATM 11191 O  O   . HOH GA 5 .   ? 67.321  41.153  40.749  1.00 33.02 ? 196 HOH A O   1 
HETATM 11192 O  O   . HOH GA 5 .   ? 68.885  47.496  10.173  1.00 26.73 ? 197 HOH A O   1 
HETATM 11193 O  O   . HOH GA 5 .   ? 59.062  47.566  3.065   1.00 17.07 ? 198 HOH A O   1 
HETATM 11194 O  O   . HOH GA 5 .   ? 44.408  41.365  32.530  1.00 47.81 ? 199 HOH A O   1 
HETATM 11195 O  O   . HOH GA 5 .   ? 58.672  29.798  3.206   1.00 12.10 ? 200 HOH A O   1 
HETATM 11196 O  O   . HOH GA 5 .   ? 75.938  33.159  17.271  1.00 32.76 ? 201 HOH A O   1 
HETATM 11197 O  O   . HOH GA 5 .   ? 51.170  24.422  18.690  1.00 2.00  ? 202 HOH A O   1 
HETATM 11198 O  O   . HOH GA 5 .   ? 69.700  32.403  27.914  1.00 23.54 ? 203 HOH A O   1 
HETATM 11199 O  O   . HOH GA 5 .   ? 63.884  32.544  23.405  1.00 37.38 ? 204 HOH A O   1 
HETATM 11200 O  O   . HOH GA 5 .   ? 68.811  36.472  8.149   1.00 33.35 ? 205 HOH A O   1 
HETATM 11201 O  O   . HOH GA 5 .   ? 61.102  31.832  25.946  1.00 25.49 ? 206 HOH A O   1 
HETATM 11202 O  O   . HOH GA 5 .   ? 52.219  24.722  6.231   1.00 30.65 ? 207 HOH A O   1 
HETATM 11203 O  O   . HOH GA 5 .   ? 49.230  29.606  21.706  1.00 33.20 ? 208 HOH A O   1 
HETATM 11204 O  O   . HOH GA 5 .   ? 58.012  27.913  7.408   1.00 37.67 ? 209 HOH A O   1 
HETATM 11205 O  O   . HOH GA 5 .   ? 71.047  51.691  3.880   1.00 45.16 ? 210 HOH A O   1 
HETATM 11206 O  O   . HOH GA 5 .   ? 72.575  63.489  15.045  1.00 45.14 ? 211 HOH A O   1 
HETATM 11207 O  O   . HOH HA 5 .   ? 57.510  29.564  21.369  1.00 2.00  ? 357 HOH F O   1 
HETATM 11208 O  O   . HOH HA 5 .   ? 74.348  42.458  12.644  1.00 29.10 ? 358 HOH F O   1 
HETATM 11209 O  O   . HOH HA 5 .   ? 66.683  29.428  21.286  1.00 5.28  ? 359 HOH F O   1 
HETATM 11210 O  O   . HOH HA 5 .   ? 64.423  27.935  25.360  1.00 14.37 ? 360 HOH F O   1 
HETATM 11211 O  O   . HOH HA 5 .   ? 71.027  2.309   26.839  1.00 27.90 ? 361 HOH F O   1 
HETATM 11212 O  O   . HOH HA 5 .   ? 66.275  1.952   7.454   1.00 27.13 ? 362 HOH F O   1 
HETATM 11213 O  O   . HOH HA 5 .   ? 64.234  -3.201  13.909  1.00 29.70 ? 363 HOH F O   1 
HETATM 11214 O  O   . HOH HA 5 .   ? 62.621  0.316   10.614  1.00 36.48 ? 364 HOH F O   1 
HETATM 11215 O  O   . HOH HA 5 .   ? 78.275  28.150  20.747  1.00 20.65 ? 365 HOH F O   1 
HETATM 11216 O  O   . HOH HA 5 .   ? 65.003  10.700  5.034   1.00 46.36 ? 366 HOH F O   1 
HETATM 11217 O  O   . HOH HA 5 .   ? 71.233  4.245   13.642  1.00 25.03 ? 367 HOH F O   1 
HETATM 11218 O  O   . HOH HA 5 .   ? 67.840  4.722   29.169  1.00 19.63 ? 368 HOH F O   1 
HETATM 11219 O  O   . HOH HA 5 .   ? 66.249  16.280  35.399  1.00 21.54 ? 369 HOH F O   1 
HETATM 11220 O  O   . HOH HA 5 .   ? 58.097  20.773  29.615  1.00 21.04 ? 370 HOH F O   1 
HETATM 11221 O  O   . HOH HA 5 .   ? 67.215  21.600  0.310   1.00 29.61 ? 371 HOH F O   1 
HETATM 11222 O  O   . HOH HA 5 .   ? 74.282  25.289  -5.519  1.00 29.11 ? 372 HOH F O   1 
HETATM 11223 O  O   . HOH HA 5 .   ? 85.300  18.328  30.064  1.00 25.40 ? 373 HOH F O   1 
HETATM 11224 O  O   . HOH HA 5 .   ? 75.763  11.278  36.067  1.00 15.55 ? 374 HOH F O   1 
HETATM 11225 O  O   . HOH HA 5 .   ? 69.484  15.326  33.658  1.00 11.06 ? 375 HOH F O   1 
HETATM 11226 O  O   . HOH HA 5 .   ? 55.441  25.226  34.544  1.00 34.68 ? 376 HOH F O   1 
HETATM 11227 O  O   . HOH HA 5 .   ? 54.606  21.943  11.211  1.00 18.83 ? 377 HOH F O   1 
HETATM 11228 O  O   . HOH HA 5 .   ? 61.280  11.631  7.421   1.00 4.30  ? 378 HOH F O   1 
HETATM 11229 O  O   . HOH HA 5 .   ? 56.209  7.704   13.726  1.00 23.18 ? 379 HOH F O   1 
HETATM 11230 O  O   . HOH HA 5 .   ? 53.576  13.688  9.062   1.00 21.32 ? 380 HOH F O   1 
HETATM 11231 O  O   . HOH HA 5 .   ? 62.923  2.748   11.792  1.00 16.20 ? 381 HOH F O   1 
HETATM 11232 O  O   . HOH HA 5 .   ? 53.593  8.233   10.325  1.00 43.52 ? 382 HOH F O   1 
HETATM 11233 O  O   . HOH HA 5 .   ? 72.789  6.474   -1.726  1.00 38.00 ? 383 HOH F O   1 
HETATM 11234 O  O   . HOH HA 5 .   ? 81.416  20.442  20.502  1.00 28.47 ? 384 HOH F O   1 
HETATM 11235 O  O   . HOH HA 5 .   ? 77.013  12.720  12.602  1.00 13.14 ? 385 HOH F O   1 
HETATM 11236 O  O   . HOH HA 5 .   ? 68.137  2.007   24.788  1.00 18.84 ? 386 HOH F O   1 
HETATM 11237 O  O   . HOH HA 5 .   ? 57.507  15.726  29.376  1.00 2.00  ? 387 HOH F O   1 
HETATM 11238 O  O   . HOH HA 5 .   ? 59.168  5.364   31.361  1.00 44.49 ? 388 HOH F O   1 
HETATM 11239 O  O   . HOH HA 5 .   ? 53.782  15.776  25.646  1.00 9.99  ? 389 HOH F O   1 
HETATM 11240 O  O   . HOH HA 5 .   ? 57.370  20.867  5.661   1.00 10.96 ? 390 HOH F O   1 
HETATM 11241 O  O   . HOH HA 5 .   ? 59.511  10.840  24.048  1.00 32.90 ? 391 HOH F O   1 
HETATM 11242 O  O   . HOH HA 5 .   ? 53.415  15.790  21.555  1.00 36.71 ? 392 HOH F O   1 
HETATM 11243 O  O   . HOH HA 5 .   ? 58.525  13.098  22.594  1.00 23.59 ? 393 HOH F O   1 
HETATM 11244 O  O   . HOH HA 5 .   ? 54.873  9.295   15.574  1.00 33.11 ? 394 HOH F O   1 
HETATM 11245 O  O   . HOH HA 5 .   ? 58.951  7.743   25.494  1.00 36.62 ? 395 HOH F O   1 
HETATM 11246 O  O   . HOH HA 5 .   ? 78.560  25.895  22.888  1.00 23.69 ? 396 HOH F O   1 
HETATM 11247 O  O   . HOH HA 5 .   ? 82.919  21.032  17.833  1.00 43.10 ? 397 HOH F O   1 
HETATM 11248 O  O   . HOH HA 5 .   ? 67.195  31.825  32.673  1.00 34.55 ? 398 HOH F O   1 
HETATM 11249 O  O   . HOH HA 5 .   ? 51.641  21.043  8.222   1.00 39.64 ? 399 HOH F O   1 
HETATM 11250 O  O   . HOH HA 5 .   ? 59.789  16.983  1.934   1.00 29.89 ? 400 HOH F O   1 
HETATM 11251 O  O   . HOH HA 5 .   ? 77.069  22.057  -5.588  1.00 27.66 ? 401 HOH F O   1 
HETATM 11252 O  O   . HOH HA 5 .   ? 57.294  11.751  18.027  1.00 23.46 ? 402 HOH F O   1 
HETATM 11253 O  O   . HOH HA 5 .   ? 50.614  24.842  22.257  1.00 32.08 ? 403 HOH F O   1 
HETATM 11254 O  O   . HOH HA 5 .   ? 79.770  9.101   29.205  1.00 13.40 ? 404 HOH F O   1 
HETATM 11255 O  O   . HOH HA 5 .   ? 63.918  -0.212  23.760  1.00 2.00  ? 405 HOH F O   1 
HETATM 11256 O  O   . HOH HA 5 .   ? 65.709  -4.988  17.847  1.00 13.96 ? 406 HOH F O   1 
HETATM 11257 O  O   . HOH HA 5 .   ? 60.970  -1.642  16.999  1.00 13.22 ? 407 HOH F O   1 
HETATM 11258 O  O   . HOH HA 5 .   ? 73.735  37.765  8.432   1.00 32.88 ? 408 HOH F O   1 
HETATM 11259 O  O   . HOH IA 5 .   ? 116.455 -10.200 31.851  1.00 8.83  ? 156 HOH B O   1 
HETATM 11260 O  O   . HOH IA 5 .   ? 119.722 -27.932 11.802  1.00 40.84 ? 157 HOH B O   1 
HETATM 11261 O  O   . HOH IA 5 .   ? 126.668 -27.526 19.217  1.00 36.97 ? 158 HOH B O   1 
HETATM 11262 O  O   . HOH IA 5 .   ? 107.632 5.811   10.832  1.00 27.18 ? 159 HOH B O   1 
HETATM 11263 O  O   . HOH IA 5 .   ? 127.883 -8.526  0.867   1.00 23.62 ? 160 HOH B O   1 
HETATM 11264 O  O   . HOH IA 5 .   ? 122.661 -13.897 33.653  1.00 35.66 ? 161 HOH B O   1 
HETATM 11265 O  O   . HOH IA 5 .   ? 130.311 -15.446 0.257   1.00 31.29 ? 162 HOH B O   1 
HETATM 11266 O  O   . HOH IA 5 .   ? 112.447 10.191  15.940  1.00 38.40 ? 163 HOH B O   1 
HETATM 11267 O  O   . HOH IA 5 .   ? 110.123 7.945   19.568  1.00 45.39 ? 164 HOH B O   1 
HETATM 11268 O  O   . HOH IA 5 .   ? 107.422 -4.836  24.428  1.00 25.72 ? 165 HOH B O   1 
HETATM 11269 O  O   . HOH IA 5 .   ? 115.986 -12.482 37.920  1.00 34.56 ? 166 HOH B O   1 
HETATM 11270 O  O   . HOH IA 5 .   ? 112.143 -16.336 27.494  1.00 33.92 ? 167 HOH B O   1 
HETATM 11271 O  O   . HOH IA 5 .   ? 119.795 2.459   30.817  1.00 32.66 ? 168 HOH B O   1 
HETATM 11272 O  O   . HOH IA 5 .   ? 124.158 -4.708  36.749  1.00 11.79 ? 169 HOH B O   1 
HETATM 11273 O  O   . HOH IA 5 .   ? 129.986 1.498   24.154  1.00 11.47 ? 170 HOH B O   1 
HETATM 11274 O  O   . HOH IA 5 .   ? 104.020 -10.846 20.356  1.00 2.00  ? 171 HOH B O   1 
HETATM 11275 O  O   . HOH IA 5 .   ? 111.662 -20.614 10.223  1.00 26.28 ? 172 HOH B O   1 
HETATM 11276 O  O   . HOH IA 5 .   ? 119.408 -13.647 5.538   1.00 3.84  ? 173 HOH B O   1 
HETATM 11277 O  O   . HOH IA 5 .   ? 127.524 -1.825  0.976   1.00 48.92 ? 174 HOH B O   1 
HETATM 11278 O  O   . HOH IA 5 .   ? 121.606 -10.688 3.836   1.00 8.85  ? 175 HOH B O   1 
HETATM 11279 O  O   . HOH IA 5 .   ? 116.740 -26.280 12.155  1.00 12.63 ? 176 HOH B O   1 
HETATM 11280 O  O   . HOH IA 5 .   ? 119.604 -21.166 12.972  1.00 42.22 ? 177 HOH B O   1 
HETATM 11281 O  O   . HOH IA 5 .   ? 131.920 -13.196 5.370   1.00 24.50 ? 178 HOH B O   1 
HETATM 11282 O  O   . HOH IA 5 .   ? 129.592 -1.408  22.130  1.00 35.84 ? 179 HOH B O   1 
HETATM 11283 O  O   . HOH IA 5 .   ? 123.509 6.459   21.610  1.00 20.06 ? 180 HOH B O   1 
HETATM 11284 O  O   . HOH IA 5 .   ? 121.767 -20.685 21.587  1.00 47.68 ? 181 HOH B O   1 
HETATM 11285 O  O   . HOH IA 5 .   ? 116.604 -18.416 26.060  1.00 24.78 ? 182 HOH B O   1 
HETATM 11286 O  O   . HOH IA 5 .   ? 119.379 -18.383 19.687  1.00 25.30 ? 183 HOH B O   1 
HETATM 11287 O  O   . HOH IA 5 .   ? 130.493 -17.319 23.331  1.00 35.29 ? 184 HOH B O   1 
HETATM 11288 O  O   . HOH IA 5 .   ? 105.226 -17.928 16.100  1.00 10.31 ? 185 HOH B O   1 
HETATM 11289 O  O   . HOH IA 5 .   ? 108.697 -21.505 22.933  1.00 53.76 ? 186 HOH B O   1 
HETATM 11290 O  O   . HOH IA 5 .   ? 124.327 -10.049 3.337   1.00 37.95 ? 187 HOH B O   1 
HETATM 11291 O  O   . HOH IA 5 .   ? 110.726 -14.062 5.314   1.00 18.62 ? 188 HOH B O   1 
HETATM 11292 O  O   . HOH IA 5 .   ? 131.249 -27.856 21.317  1.00 35.78 ? 189 HOH B O   1 
HETATM 11293 O  O   . HOH IA 5 .   ? 117.144 -21.155 17.434  1.00 24.57 ? 190 HOH B O   1 
HETATM 11294 O  O   . HOH IA 5 .   ? 132.640 -21.944 20.795  1.00 26.88 ? 191 HOH B O   1 
HETATM 11295 O  O   . HOH IA 5 .   ? 116.669 -13.689 32.201  1.00 33.01 ? 192 HOH B O   1 
HETATM 11296 O  O   . HOH IA 5 .   ? 106.585 -0.653  5.816   1.00 30.56 ? 193 HOH B O   1 
HETATM 11297 O  O   . HOH IA 5 .   ? 118.753 -24.550 10.410  1.00 22.30 ? 194 HOH B O   1 
HETATM 11298 O  O   . HOH IA 5 .   ? 118.406 -21.357 8.249   1.00 20.69 ? 195 HOH B O   1 
HETATM 11299 O  O   . HOH IA 5 .   ? 131.257 -4.714  18.294  1.00 33.68 ? 196 HOH B O   1 
HETATM 11300 O  O   . HOH IA 5 .   ? 130.865 -14.297 27.110  1.00 29.56 ? 197 HOH B O   1 
HETATM 11301 O  O   . HOH IA 5 .   ? 132.442 -31.024 22.094  1.00 27.85 ? 198 HOH B O   1 
HETATM 11302 O  O   . HOH IA 5 .   ? 108.385 -14.644 7.559   1.00 44.85 ? 199 HOH B O   1 
HETATM 11303 O  O   . HOH IA 5 .   ? 104.556 -6.776  3.261   1.00 27.06 ? 200 HOH B O   1 
HETATM 11304 O  O   . HOH IA 5 .   ? 108.340 -3.229  21.666  1.00 2.00  ? 201 HOH B O   1 
HETATM 11305 O  O   . HOH IA 5 .   ? 135.731 0.983   42.613  1.00 37.00 ? 202 HOH B O   1 
HETATM 11306 O  O   . HOH IA 5 .   ? 127.612 -14.833 31.352  1.00 35.77 ? 203 HOH B O   1 
HETATM 11307 O  O   . HOH IA 5 .   ? 135.539 -13.528 17.853  1.00 51.10 ? 204 HOH B O   1 
HETATM 11308 O  O   . HOH IA 5 .   ? 135.842 -17.504 19.042  1.00 22.59 ? 205 HOH B O   1 
HETATM 11309 O  O   . HOH IA 5 .   ? 135.698 -11.152 9.526   1.00 34.76 ? 206 HOH B O   1 
HETATM 11310 O  O   . HOH IA 5 .   ? 124.699 10.102  8.044   1.00 53.89 ? 207 HOH B O   1 
HETATM 11311 O  O   . HOH IA 5 .   ? 118.157 14.761  10.687  1.00 43.85 ? 208 HOH B O   1 
HETATM 11312 O  O   . HOH IA 5 .   ? 117.964 12.700  22.581  1.00 31.71 ? 209 HOH B O   1 
HETATM 11313 O  O   . HOH JA 5 .   ? 86.975  -13.610 -0.001  1.00 36.42 ? 156 HOH G O   1 
HETATM 11314 O  O   . HOH JA 5 .   ? 84.167  -17.270 40.853  1.00 26.83 ? 157 HOH G O   1 
HETATM 11315 O  O   . HOH JA 5 .   ? 96.208  4.337   1.875   1.00 13.65 ? 158 HOH G O   1 
HETATM 11316 O  O   . HOH JA 5 .   ? 78.078  7.921   12.569  1.00 15.36 ? 159 HOH G O   1 
HETATM 11317 O  O   . HOH JA 5 .   ? 73.330  5.962   19.622  1.00 2.00  ? 160 HOH G O   1 
HETATM 11318 O  O   . HOH JA 5 .   ? 78.390  7.127   24.443  1.00 2.00  ? 161 HOH G O   1 
HETATM 11319 O  O   . HOH JA 5 .   ? 75.858  7.855   -0.633  1.00 48.20 ? 162 HOH G O   1 
HETATM 11320 O  O   . HOH JA 5 .   ? 75.460  9.784   14.511  1.00 30.65 ? 163 HOH G O   1 
HETATM 11321 O  O   . HOH JA 5 .   ? 96.872  -15.593 -3.825  1.00 33.42 ? 164 HOH G O   1 
HETATM 11322 O  O   . HOH JA 5 .   ? 85.680  -2.895  2.722   1.00 28.14 ? 165 HOH G O   1 
HETATM 11323 O  O   . HOH JA 5 .   ? 98.375  -18.128 20.902  1.00 33.05 ? 166 HOH G O   1 
HETATM 11324 O  O   . HOH JA 5 .   ? 103.668 -3.055  8.753   1.00 2.00  ? 167 HOH G O   1 
HETATM 11325 O  O   . HOH JA 5 .   ? 105.336 -12.690 32.116  1.00 41.28 ? 168 HOH G O   1 
HETATM 11326 O  O   . HOH JA 5 .   ? 103.091 -8.382  21.336  1.00 6.68  ? 169 HOH G O   1 
HETATM 11327 O  O   . HOH JA 5 .   ? 102.777 -6.058  26.118  1.00 20.58 ? 170 HOH G O   1 
HETATM 11328 O  O   . HOH JA 5 .   ? 89.384  -17.923 13.232  1.00 28.03 ? 171 HOH G O   1 
HETATM 11329 O  O   . HOH JA 5 .   ? 87.288  -21.191 23.243  1.00 22.55 ? 172 HOH G O   1 
HETATM 11330 O  O   . HOH JA 5 .   ? 83.659  14.201  24.827  1.00 27.53 ? 173 HOH G O   1 
HETATM 11331 O  O   . HOH JA 5 .   ? 77.703  0.951   23.961  1.00 29.78 ? 174 HOH G O   1 
HETATM 11332 O  O   . HOH JA 5 .   ? 99.659  10.883  19.745  1.00 23.90 ? 175 HOH G O   1 
HETATM 11333 O  O   . HOH JA 5 .   ? 73.144  8.394   17.449  1.00 19.77 ? 176 HOH G O   1 
HETATM 11334 O  O   . HOH JA 5 .   ? 72.984  6.647   15.216  1.00 17.47 ? 177 HOH G O   1 
HETATM 11335 O  O   . HOH JA 5 .   ? 99.077  -16.567 15.675  1.00 23.35 ? 178 HOH G O   1 
HETATM 11336 O  O   . HOH JA 5 .   ? 99.740  -20.433 4.368   1.00 55.04 ? 179 HOH G O   1 
HETATM 11337 O  O   . HOH JA 5 .   ? 76.217  3.286   27.096  1.00 8.61  ? 180 HOH G O   1 
HETATM 11338 O  O   . HOH JA 5 .   ? 99.183  -12.315 28.741  1.00 33.73 ? 181 HOH G O   1 
HETATM 11339 O  O   . HOH JA 5 .   ? 102.049 4.284   32.283  1.00 36.92 ? 182 HOH G O   1 
HETATM 11340 O  O   . HOH JA 5 .   ? 95.120  -19.497 20.291  1.00 32.05 ? 183 HOH G O   1 
HETATM 11341 O  O   . HOH JA 5 .   ? 82.626  -7.524  36.192  1.00 5.67  ? 184 HOH G O   1 
HETATM 11342 O  O   . HOH JA 5 .   ? 87.685  -3.743  32.745  1.00 2.00  ? 185 HOH G O   1 
HETATM 11343 O  O   . HOH JA 5 .   ? 77.717  -13.816 28.615  1.00 35.71 ? 186 HOH G O   1 
HETATM 11344 O  O   . HOH JA 5 .   ? 107.352 -0.737  21.426  1.00 2.00  ? 187 HOH G O   1 
HETATM 11345 O  O   . HOH JA 5 .   ? 97.792  13.427  22.740  1.00 41.51 ? 188 HOH G O   1 
HETATM 11346 O  O   . HOH JA 5 .   ? 91.385  4.868   7.842   1.00 16.98 ? 189 HOH G O   1 
HETATM 11347 O  O   . HOH JA 5 .   ? 88.641  0.770   4.059   1.00 44.56 ? 190 HOH G O   1 
HETATM 11348 O  O   . HOH JA 5 .   ? 89.319  3.521   6.986   1.00 2.00  ? 191 HOH G O   1 
HETATM 11349 O  O   . HOH JA 5 .   ? 88.935  10.366  13.640  1.00 2.00  ? 192 HOH G O   1 
HETATM 11350 O  O   . HOH JA 5 .   ? 95.542  11.788  14.177  1.00 18.93 ? 193 HOH G O   1 
HETATM 11351 O  O   . HOH JA 5 .   ? 80.468  6.154   11.626  1.00 14.83 ? 194 HOH G O   1 
HETATM 11352 O  O   . HOH JA 5 .   ? 88.147  15.530  11.141  1.00 28.46 ? 195 HOH G O   1 
HETATM 11353 O  O   . HOH JA 5 .   ? 79.712  -4.252  14.767  1.00 4.12  ? 196 HOH G O   1 
HETATM 11354 O  O   . HOH JA 5 .   ? 78.545  4.520   7.156   1.00 12.32 ? 197 HOH G O   1 
HETATM 11355 O  O   . HOH JA 5 .   ? 83.385  -6.638  17.514  1.00 4.70  ? 198 HOH G O   1 
HETATM 11356 O  O   . HOH JA 5 .   ? 88.146  -17.471 20.617  1.00 28.50 ? 199 HOH G O   1 
HETATM 11357 O  O   . HOH JA 5 .   ? 87.027  -15.619 14.143  1.00 3.49  ? 200 HOH G O   1 
HETATM 11358 O  O   . HOH JA 5 .   ? 80.971  4.206   25.853  1.00 7.82  ? 201 HOH G O   1 
HETATM 11359 O  O   . HOH JA 5 .   ? 103.179 9.491   29.457  1.00 38.58 ? 202 HOH G O   1 
HETATM 11360 O  O   . HOH JA 5 .   ? 94.638  5.497   29.095  1.00 12.77 ? 203 HOH G O   1 
HETATM 11361 O  O   . HOH JA 5 .   ? 110.386 1.554   29.419  1.00 29.74 ? 204 HOH G O   1 
HETATM 11362 O  O   . HOH JA 5 .   ? 105.859 8.543   22.782  1.00 42.26 ? 205 HOH G O   1 
HETATM 11363 O  O   . HOH JA 5 .   ? 90.802  -1.567  -0.134  1.00 20.03 ? 206 HOH G O   1 
HETATM 11364 O  O   . HOH JA 5 .   ? 97.539  6.314   9.718   1.00 10.58 ? 207 HOH G O   1 
HETATM 11365 O  O   . HOH JA 5 .   ? 92.132  10.049  30.524  1.00 35.83 ? 208 HOH G O   1 
HETATM 11366 O  O   . HOH JA 5 .   ? 96.349  10.211  20.797  1.00 32.07 ? 209 HOH G O   1 
HETATM 11367 O  O   . HOH JA 5 .   ? 92.823  8.594   24.360  1.00 10.65 ? 210 HOH G O   1 
HETATM 11368 O  O   . HOH JA 5 .   ? 92.535  7.585   20.801  1.00 16.91 ? 211 HOH G O   1 
HETATM 11369 O  O   . HOH JA 5 .   ? 84.660  22.111  22.225  1.00 39.35 ? 212 HOH G O   1 
HETATM 11370 O  O   . HOH JA 5 .   ? 78.601  -10.670 29.477  1.00 16.88 ? 213 HOH G O   1 
HETATM 11371 O  O   . HOH JA 5 .   ? 82.122  -7.702  15.314  1.00 19.05 ? 214 HOH G O   1 
HETATM 11372 O  O   . HOH JA 5 .   ? 89.366  -4.705  34.794  1.00 6.73  ? 215 HOH G O   1 
HETATM 11373 O  O   . HOH JA 5 .   ? 92.596  -2.108  34.528  1.00 20.99 ? 216 HOH G O   1 
HETATM 11374 O  O   . HOH JA 5 .   ? 83.339  -14.695 26.742  1.00 16.07 ? 217 HOH G O   1 
HETATM 11375 O  O   . HOH JA 5 .   ? 89.941  0.001   35.288  1.00 23.58 ? 218 HOH G O   1 
HETATM 11376 O  O   . HOH KA 5 .   ? 50.474  -49.632 14.771  1.00 32.25 ? 156 HOH C O   1 
HETATM 11377 O  O   . HOH KA 5 .   ? 39.807  -46.454 15.833  1.00 2.00  ? 157 HOH C O   1 
HETATM 11378 O  O   . HOH KA 5 .   ? 47.569  -48.336 8.656   1.00 17.39 ? 158 HOH C O   1 
HETATM 11379 O  O   . HOH KA 5 .   ? 33.230  -25.056 26.414  1.00 35.96 ? 159 HOH C O   1 
HETATM 11380 O  O   . HOH KA 5 .   ? 37.366  -36.897 33.074  1.00 29.77 ? 160 HOH C O   1 
HETATM 11381 O  O   . HOH KA 5 .   ? 41.646  -39.932 1.165   1.00 24.62 ? 161 HOH C O   1 
HETATM 11382 O  O   . HOH KA 5 .   ? 47.057  -21.300 42.629  1.00 24.02 ? 162 HOH C O   1 
HETATM 11383 O  O   . HOH KA 5 .   ? 48.062  -46.204 2.973   1.00 26.65 ? 163 HOH C O   1 
HETATM 11384 O  O   . HOH KA 5 .   ? 45.457  -48.922 4.103   1.00 29.40 ? 164 HOH C O   1 
HETATM 11385 O  O   . HOH KA 5 .   ? 43.694  -52.905 30.553  1.00 25.65 ? 165 HOH C O   1 
HETATM 11386 O  O   . HOH KA 5 .   ? 31.069  -42.079 29.917  1.00 20.21 ? 166 HOH C O   1 
HETATM 11387 O  O   . HOH KA 5 .   ? 53.997  -34.016 29.594  1.00 29.77 ? 167 HOH C O   1 
HETATM 11388 O  O   . HOH KA 5 .   ? 40.831  -35.187 33.054  1.00 36.56 ? 168 HOH C O   1 
HETATM 11389 O  O   . HOH KA 5 .   ? 36.192  -23.356 28.145  1.00 15.77 ? 169 HOH C O   1 
HETATM 11390 O  O   . HOH KA 5 .   ? 40.790  -25.624 40.544  1.00 54.14 ? 170 HOH C O   1 
HETATM 11391 O  O   . HOH KA 5 .   ? 46.126  -26.330 37.503  1.00 38.86 ? 171 HOH C O   1 
HETATM 11392 O  O   . HOH KA 5 .   ? 61.282  -32.249 10.978  1.00 2.92  ? 172 HOH C O   1 
HETATM 11393 O  O   . HOH KA 5 .   ? 50.206  -41.135 -1.290  1.00 32.32 ? 173 HOH C O   1 
HETATM 11394 O  O   . HOH KA 5 .   ? 57.600  -44.287 30.842  1.00 53.39 ? 174 HOH C O   1 
HETATM 11395 O  O   . HOH KA 5 .   ? 40.217  -39.724 31.786  1.00 5.85  ? 175 HOH C O   1 
HETATM 11396 O  O   . HOH KA 5 .   ? 48.674  -21.273 20.768  1.00 2.00  ? 176 HOH C O   1 
HETATM 11397 O  O   . HOH KA 5 .   ? 38.473  -33.267 5.737   1.00 14.08 ? 177 HOH C O   1 
HETATM 11398 O  O   . HOH KA 5 .   ? 41.589  -36.751 1.857   1.00 34.57 ? 178 HOH C O   1 
HETATM 11399 O  O   . HOH KA 5 .   ? 38.975  -35.678 4.619   1.00 28.67 ? 179 HOH C O   1 
HETATM 11400 O  O   . HOH KA 5 .   ? 29.819  -44.940 9.743   1.00 27.17 ? 180 HOH C O   1 
HETATM 11401 O  O   . HOH KA 5 .   ? 42.394  -45.222 16.209  1.00 4.20  ? 181 HOH C O   1 
HETATM 11402 O  O   . HOH KA 5 .   ? 53.862  -46.545 21.369  1.00 27.12 ? 182 HOH C O   1 
HETATM 11403 O  O   . HOH KA 5 .   ? 30.632  -41.419 23.019  1.00 20.75 ? 183 HOH C O   1 
HETATM 11404 O  O   . HOH KA 5 .   ? 36.426  -28.339 30.638  1.00 43.25 ? 184 HOH C O   1 
HETATM 11405 O  O   . HOH KA 5 .   ? 35.987  -28.999 26.489  1.00 15.90 ? 185 HOH C O   1 
HETATM 11406 O  O   . HOH KA 5 .   ? 32.045  -28.409 31.292  1.00 18.22 ? 186 HOH C O   1 
HETATM 11407 O  O   . HOH KA 5 .   ? 35.314  -29.681 11.095  1.00 11.33 ? 187 HOH C O   1 
HETATM 11408 O  O   . HOH KA 5 .   ? 39.225  -38.498 3.237   1.00 33.29 ? 188 HOH C O   1 
HETATM 11409 O  O   . HOH KA 5 .   ? 33.609  -23.591 16.854  1.00 41.00 ? 189 HOH C O   1 
HETATM 11410 O  O   . HOH KA 5 .   ? 29.738  -32.957 26.300  1.00 2.61  ? 190 HOH C O   1 
HETATM 11411 O  O   . HOH KA 5 .   ? 21.739  -27.971 17.193  1.00 38.84 ? 191 HOH C O   1 
HETATM 11412 O  O   . HOH KA 5 .   ? 26.314  -38.951 25.090  1.00 32.88 ? 192 HOH C O   1 
HETATM 11413 O  O   . HOH KA 5 .   ? 34.011  -30.927 14.556  1.00 4.95  ? 193 HOH C O   1 
HETATM 11414 O  O   . HOH KA 5 .   ? 31.084  -34.064 21.369  1.00 22.40 ? 194 HOH C O   1 
HETATM 11415 O  O   . HOH KA 5 .   ? 24.946  -40.645 12.612  1.00 33.65 ? 195 HOH C O   1 
HETATM 11416 O  O   . HOH KA 5 .   ? 24.649  -47.208 12.471  1.00 31.85 ? 196 HOH C O   1 
HETATM 11417 O  O   . HOH KA 5 .   ? 70.516  -28.763 16.650  1.00 29.64 ? 197 HOH C O   1 
HETATM 11418 O  O   . HOH KA 5 .   ? 53.342  -29.348 21.827  1.00 27.37 ? 198 HOH C O   1 
HETATM 11419 O  O   . HOH LA 5 .   ? 67.691  -0.152  26.543  1.00 33.78 ? 156 HOH H O   1 
HETATM 11420 O  O   . HOH LA 5 .   ? 79.077  -3.463  19.944  1.00 2.00  ? 157 HOH H O   1 
HETATM 11421 O  O   . HOH LA 5 .   ? 59.129  -2.053  13.245  1.00 19.85 ? 158 HOH H O   1 
HETATM 11422 O  O   . HOH LA 5 .   ? 74.434  -7.749  32.858  1.00 27.21 ? 159 HOH H O   1 
HETATM 11423 O  O   . HOH LA 5 .   ? 52.790  -2.815  12.648  1.00 31.78 ? 160 HOH H O   1 
HETATM 11424 O  O   . HOH LA 5 .   ? 73.632  -0.800  18.800  1.00 34.89 ? 161 HOH H O   1 
HETATM 11425 O  O   . HOH LA 5 .   ? 50.926  -4.985  21.718  1.00 20.93 ? 162 HOH H O   1 
HETATM 11426 O  O   . HOH LA 5 .   ? 56.839  -2.574  26.250  1.00 16.09 ? 163 HOH H O   1 
HETATM 11427 O  O   . HOH LA 5 .   ? 52.975  -22.956 3.560   1.00 29.42 ? 164 HOH H O   1 
HETATM 11428 O  O   . HOH LA 5 .   ? 46.398  -4.125  24.232  1.00 30.68 ? 165 HOH H O   1 
HETATM 11429 O  O   . HOH LA 5 .   ? 48.758  -3.629  27.179  1.00 33.29 ? 166 HOH H O   1 
HETATM 11430 O  O   . HOH LA 5 .   ? 66.871  -23.440 32.368  1.00 39.49 ? 167 HOH H O   1 
HETATM 11431 O  O   . HOH LA 5 .   ? 61.550  -28.445 31.643  1.00 36.58 ? 168 HOH H O   1 
HETATM 11432 O  O   . HOH LA 5 .   ? 61.064  -4.984  3.246   1.00 42.03 ? 169 HOH H O   1 
HETATM 11433 O  O   . HOH LA 5 .   ? 61.934  -6.787  1.030   1.00 34.77 ? 170 HOH H O   1 
HETATM 11434 O  O   . HOH LA 5 .   ? 43.951  -12.019 16.349  1.00 34.85 ? 171 HOH H O   1 
HETATM 11435 O  O   . HOH LA 5 .   ? 63.673  -14.150 35.598  1.00 33.20 ? 172 HOH H O   1 
HETATM 11436 O  O   . HOH LA 5 .   ? 43.246  -14.667 23.779  1.00 22.77 ? 173 HOH H O   1 
HETATM 11437 O  O   . HOH LA 5 .   ? 44.662  -12.260 24.141  1.00 26.42 ? 174 HOH H O   1 
HETATM 11438 O  O   . HOH LA 5 .   ? 45.351  -14.119 29.763  1.00 26.50 ? 175 HOH H O   1 
HETATM 11439 O  O   . HOH LA 5 .   ? 45.089  -6.916  20.676  1.00 29.89 ? 176 HOH H O   1 
HETATM 11440 O  O   . HOH LA 5 .   ? 57.388  -25.045 41.025  1.00 34.53 ? 177 HOH H O   1 
HETATM 11441 O  O   . HOH LA 5 .   ? 68.195  -15.151 7.112   1.00 17.43 ? 178 HOH H O   1 
HETATM 11442 O  O   . HOH LA 5 .   ? 72.074  -3.702  25.512  1.00 29.84 ? 179 HOH H O   1 
HETATM 11443 O  O   . HOH LA 5 .   ? 75.364  -4.489  21.997  1.00 26.57 ? 180 HOH H O   1 
HETATM 11444 O  O   . HOH LA 5 .   ? 64.410  2.207   31.075  1.00 33.96 ? 181 HOH H O   1 
HETATM 11445 O  O   . HOH LA 5 .   ? 65.333  -11.559 33.378  1.00 16.24 ? 182 HOH H O   1 
HETATM 11446 O  O   . HOH LA 5 .   ? 60.870  -35.040 20.423  1.00 16.27 ? 183 HOH H O   1 
HETATM 11447 O  O   . HOH LA 5 .   ? 41.823  -19.100 16.503  1.00 22.18 ? 184 HOH H O   1 
HETATM 11448 O  O   . HOH LA 5 .   ? 51.459  -21.666 21.462  1.00 3.01  ? 185 HOH H O   1 
HETATM 11449 O  O   . HOH LA 5 .   ? 53.057  -23.950 23.146  1.00 14.82 ? 186 HOH H O   1 
HETATM 11450 O  O   . HOH LA 5 .   ? 51.443  -16.545 4.507   1.00 7.18  ? 187 HOH H O   1 
HETATM 11451 O  O   . HOH LA 5 .   ? 44.540  -14.998 18.453  1.00 2.87  ? 188 HOH H O   1 
HETATM 11452 O  O   . HOH LA 5 .   ? 68.312  -3.742  28.927  1.00 15.23 ? 189 HOH H O   1 
HETATM 11453 O  O   . HOH LA 5 .   ? 50.169  -17.065 28.579  1.00 9.27  ? 190 HOH H O   1 
HETATM 11454 O  O   . HOH LA 5 .   ? 55.056  -20.968 43.291  1.00 29.52 ? 191 HOH H O   1 
HETATM 11455 O  O   . HOH LA 5 .   ? 59.909  -24.384 30.261  1.00 15.28 ? 192 HOH H O   1 
HETATM 11456 O  O   . HOH LA 5 .   ? 41.666  -13.270 1.753   1.00 37.45 ? 193 HOH H O   1 
HETATM 11457 O  O   . HOH LA 5 .   ? 44.804  -14.771 21.548  1.00 20.55 ? 194 HOH H O   1 
HETATM 11458 O  O   . HOH LA 5 .   ? 55.780  1.369   37.505  1.00 39.45 ? 195 HOH H O   1 
HETATM 11459 O  O   . HOH LA 5 .   ? 62.500  -11.222 33.411  1.00 11.73 ? 196 HOH H O   1 
HETATM 11460 O  O   . HOH LA 5 .   ? 56.119  -29.700 21.382  1.00 2.00  ? 197 HOH H O   1 
HETATM 11461 O  O   . HOH LA 5 .   ? 70.421  -20.194 24.860  1.00 13.15 ? 198 HOH H O   1 
HETATM 11462 O  O   . HOH LA 5 .   ? 68.688  -17.677 8.161   1.00 7.07  ? 199 HOH H O   1 
HETATM 11463 O  O   . HOH LA 5 .   ? 65.076  -12.468 3.182   1.00 8.77  ? 200 HOH H O   1 
HETATM 11464 O  O   . HOH LA 5 .   ? 67.442  -9.284  6.178   1.00 24.49 ? 201 HOH H O   1 
HETATM 11465 O  O   . HOH LA 5 .   ? 73.899  -19.758 14.494  1.00 31.02 ? 202 HOH H O   1 
HETATM 11466 O  O   . HOH LA 5 .   ? 71.166  -23.280 9.768   1.00 27.11 ? 203 HOH H O   1 
HETATM 11467 O  O   . HOH LA 5 .   ? 75.479  -10.434 11.618  1.00 3.99  ? 204 HOH H O   1 
HETATM 11468 O  O   . HOH LA 5 .   ? 78.524  -24.669 18.717  1.00 49.45 ? 205 HOH H O   1 
HETATM 11469 O  O   . HOH LA 5 .   ? 58.696  1.977   31.876  1.00 18.47 ? 206 HOH H O   1 
HETATM 11470 O  O   . HOH LA 5 .   ? 50.758  -1.706  16.607  1.00 49.35 ? 207 HOH H O   1 
HETATM 11471 O  O   . HOH LA 5 .   ? 73.398  -9.571  26.730  1.00 7.72  ? 208 HOH H O   1 
HETATM 11472 O  O   . HOH LA 5 .   ? 67.569  -21.713 29.332  1.00 28.10 ? 209 HOH H O   1 
HETATM 11473 O  O   . HOH LA 5 .   ? 66.197  -18.434 34.128  1.00 37.93 ? 210 HOH H O   1 
HETATM 11474 O  O   . HOH LA 5 .   ? 63.430  -31.663 18.306  1.00 26.22 ? 211 HOH H O   1 
HETATM 11475 O  O   . HOH LA 5 .   ? 70.024  -16.229 -1.494  1.00 36.20 ? 212 HOH H O   1 
HETATM 11476 O  O   . HOH LA 5 .   ? 64.422  -25.493 7.604   1.00 17.35 ? 213 HOH H O   1 
HETATM 11477 O  O   . HOH LA 5 .   ? 71.030  -24.949 20.804  1.00 20.08 ? 214 HOH H O   1 
HETATM 11478 O  O   . HOH LA 5 .   ? 70.633  -17.436 24.086  1.00 2.00  ? 215 HOH H O   1 
HETATM 11479 O  O   . HOH LA 5 .   ? 71.737  -20.305 17.865  1.00 11.46 ? 216 HOH H O   1 
HETATM 11480 O  O   . HOH LA 5 .   ? 73.612  -16.376 25.074  1.00 22.15 ? 217 HOH H O   1 
HETATM 11481 O  O   . HOH LA 5 .   ? 81.524  -16.797 23.802  1.00 9.78  ? 218 HOH H O   1 
HETATM 11482 O  O   . HOH MA 5 .   ? 160.223 -21.570 -6.998  1.00 54.32 ? 156 HOH D O   1 
HETATM 11483 O  O   . HOH MA 5 .   ? 156.424 -22.236 19.881  1.00 26.68 ? 157 HOH D O   1 
HETATM 11484 O  O   . HOH MA 5 .   ? 147.378 -14.756 31.387  1.00 25.61 ? 158 HOH D O   1 
HETATM 11485 O  O   . HOH MA 5 .   ? 135.872 -25.599 -12.199 1.00 27.84 ? 159 HOH D O   1 
HETATM 11486 O  O   . HOH MA 5 .   ? 134.828 -9.044  13.966  1.00 25.48 ? 160 HOH D O   1 
HETATM 11487 O  O   . HOH MA 5 .   ? 142.223 -12.463 31.970  1.00 31.10 ? 161 HOH D O   1 
HETATM 11488 O  O   . HOH MA 5 .   ? 162.433 2.668   21.501  1.00 40.68 ? 162 HOH D O   1 
HETATM 11489 O  O   . HOH MA 5 .   ? 159.752 5.251   19.762  1.00 44.71 ? 163 HOH D O   1 
HETATM 11490 O  O   . HOH MA 5 .   ? 148.353 1.379   20.961  1.00 7.39  ? 164 HOH D O   1 
HETATM 11491 O  O   . HOH MA 5 .   ? 139.656 0.219   26.790  1.00 40.68 ? 165 HOH D O   1 
HETATM 11492 O  O   . HOH MA 5 .   ? 137.679 -9.659  24.098  1.00 33.37 ? 166 HOH D O   1 
HETATM 11493 O  O   . HOH MA 5 .   ? 138.813 -7.191  25.707  1.00 4.27  ? 167 HOH D O   1 
HETATM 11494 O  O   . HOH MA 5 .   ? 139.061 -5.905  34.445  1.00 19.95 ? 168 HOH D O   1 
HETATM 11495 O  O   . HOH MA 5 .   ? 170.224 0.749   5.933   1.00 31.18 ? 169 HOH D O   1 
HETATM 11496 O  O   . HOH MA 5 .   ? 169.527 -6.744  5.349   1.00 40.78 ? 170 HOH D O   1 
HETATM 11497 O  O   . HOH MA 5 .   ? 152.329 -17.984 35.903  1.00 14.44 ? 171 HOH D O   1 
HETATM 11498 O  O   . HOH MA 5 .   ? 140.629 -14.983 34.122  1.00 46.46 ? 172 HOH D O   1 
HETATM 11499 O  O   . HOH MA 5 .   ? 157.627 -25.377 25.694  1.00 20.08 ? 173 HOH D O   1 
HETATM 11500 O  O   . HOH MA 5 .   ? 140.343 -15.749 18.474  1.00 8.79  ? 174 HOH D O   1 
HETATM 11501 O  O   . HOH MA 5 .   ? 148.378 -13.896 4.579   1.00 33.93 ? 175 HOH D O   1 
HETATM 11502 O  O   . HOH MA 5 .   ? 154.497 -11.196 2.379   1.00 37.44 ? 176 HOH D O   1 
HETATM 11503 O  O   . HOH MA 5 .   ? 142.336 -19.506 7.805   1.00 30.89 ? 177 HOH D O   1 
HETATM 11504 O  O   . HOH MA 5 .   ? 139.655 -3.495  5.560   1.00 39.31 ? 178 HOH D O   1 
HETATM 11505 O  O   . HOH MA 5 .   ? 140.651 -15.622 7.352   1.00 32.16 ? 179 HOH D O   1 
HETATM 11506 O  O   . HOH MA 5 .   ? 158.778 -24.513 22.797  1.00 22.47 ? 180 HOH D O   1 
HETATM 11507 O  O   . HOH MA 5 .   ? 162.875 -15.920 8.112   1.00 41.84 ? 181 HOH D O   1 
HETATM 11508 O  O   . HOH MA 5 .   ? 159.243 -15.898 15.042  1.00 18.39 ? 182 HOH D O   1 
HETATM 11509 O  O   . HOH MA 5 .   ? 168.923 -13.044 17.771  1.00 36.40 ? 183 HOH D O   1 
HETATM 11510 O  O   . HOH MA 5 .   ? 146.742 -17.634 30.296  1.00 41.45 ? 184 HOH D O   1 
HETATM 11511 O  O   . HOH MA 5 .   ? 135.711 -8.234  26.360  1.00 23.50 ? 185 HOH D O   1 
HETATM 11512 O  O   . HOH MA 5 .   ? 137.943 -14.756 22.712  1.00 29.65 ? 186 HOH D O   1 
HETATM 11513 O  O   . HOH MA 5 .   ? 134.916 -6.213  13.224  1.00 8.11  ? 187 HOH D O   1 
HETATM 11514 O  O   . HOH MA 5 .   ? 141.963 0.440   25.109  1.00 26.99 ? 188 HOH D O   1 
HETATM 11515 O  O   . HOH MA 5 .   ? 161.411 -8.760  2.818   1.00 34.30 ? 189 HOH D O   1 
HETATM 11516 O  O   . HOH MA 5 .   ? 146.136 -4.378  2.279   1.00 20.39 ? 190 HOH D O   1 
HETATM 11517 O  O   . HOH MA 5 .   ? 139.058 -15.308 14.506  1.00 30.26 ? 191 HOH D O   1 
HETATM 11518 O  O   . HOH MA 5 .   ? 139.989 -20.515 19.199  1.00 36.59 ? 192 HOH D O   1 
HETATM 11519 O  O   . HOH MA 5 .   ? 132.604 -24.269 10.768  1.00 28.81 ? 193 HOH D O   1 
HETATM 11520 O  O   . HOH MA 5 .   ? 140.922 -28.202 7.639   1.00 19.57 ? 194 HOH D O   1 
HETATM 11521 O  O   . HOH MA 5 .   ? 154.274 -31.001 14.998  1.00 23.61 ? 195 HOH D O   1 
HETATM 11522 O  O   . HOH MA 5 .   ? 137.660 -6.148  4.857   1.00 31.70 ? 196 HOH D O   1 
HETATM 11523 O  O   . HOH MA 5 .   ? 132.933 -0.909  14.698  1.00 19.43 ? 197 HOH D O   1 
HETATM 11524 O  O   . HOH MA 5 .   ? 145.639 -0.005  23.796  1.00 16.21 ? 198 HOH D O   1 
HETATM 11525 O  O   . HOH NA 5 .   ? 137.713 28.766  10.634  1.00 21.18 ? 358 HOH I O   1 
HETATM 11526 O  O   . HOH NA 5 .   ? 133.837 32.186  15.663  1.00 40.51 ? 359 HOH I O   1 
HETATM 11527 O  O   . HOH NA 5 .   ? 139.424 30.449  23.003  1.00 32.91 ? 360 HOH I O   1 
HETATM 11528 O  O   . HOH NA 5 .   ? 147.533 30.893  27.535  1.00 18.67 ? 361 HOH I O   1 
HETATM 11529 O  O   . HOH NA 5 .   ? 125.229 19.180  35.681  1.00 38.22 ? 362 HOH I O   1 
HETATM 11530 O  O   . HOH NA 5 .   ? 124.043 5.037   1.004   1.00 38.02 ? 363 HOH I O   1 
HETATM 11531 O  O   . HOH NA 5 .   ? 135.641 0.690   28.061  1.00 39.15 ? 364 HOH I O   1 
HETATM 11532 O  O   . HOH NA 5 .   ? 122.406 13.979  26.913  1.00 20.31 ? 365 HOH I O   1 
HETATM 11533 O  O   . HOH NA 5 .   ? 141.227 3.072   19.626  1.00 2.00  ? 366 HOH I O   1 
HETATM 11534 O  O   . HOH NA 5 .   ? 129.340 1.569   13.126  1.00 50.29 ? 367 HOH I O   1 
HETATM 11535 O  O   . HOH NA 5 .   ? 133.985 28.210  25.907  1.00 13.58 ? 368 HOH I O   1 
HETATM 11536 O  O   . HOH NA 5 .   ? 124.767 9.451   22.437  1.00 36.79 ? 369 HOH I O   1 
HETATM 11537 O  O   . HOH NA 5 .   ? 138.163 12.725  37.640  1.00 17.55 ? 370 HOH I O   1 
HETATM 11538 O  O   . HOH NA 5 .   ? 149.448 10.572  30.901  1.00 43.07 ? 371 HOH I O   1 
HETATM 11539 O  O   . HOH NA 5 .   ? 157.288 16.216  26.027  1.00 47.64 ? 372 HOH I O   1 
HETATM 11540 O  O   . HOH NA 5 .   ? 132.954 5.315   -4.358  1.00 22.36 ? 373 HOH I O   1 
HETATM 11541 O  O   . HOH NA 5 .   ? 137.669 10.120  -7.436  1.00 19.49 ? 374 HOH I O   1 
HETATM 11542 O  O   . HOH NA 5 .   ? 138.488 19.019  -4.956  1.00 33.59 ? 375 HOH I O   1 
HETATM 11543 O  O   . HOH NA 5 .   ? 129.597 19.892  32.647  1.00 22.54 ? 376 HOH I O   1 
HETATM 11544 O  O   . HOH NA 5 .   ? 145.123 20.885  33.452  1.00 35.10 ? 377 HOH I O   1 
HETATM 11545 O  O   . HOH NA 5 .   ? 150.015 19.648  7.759   1.00 9.28  ? 378 HOH I O   1 
HETATM 11546 O  O   . HOH NA 5 .   ? 146.247 21.068  4.470   1.00 23.98 ? 379 HOH I O   1 
HETATM 11547 O  O   . HOH NA 5 .   ? 148.261 21.028  6.442   1.00 12.74 ? 380 HOH I O   1 
HETATM 11548 O  O   . HOH NA 5 .   ? 151.938 25.034  13.581  1.00 23.84 ? 381 HOH I O   1 
HETATM 11549 O  O   . HOH NA 5 .   ? 153.568 20.192  13.619  1.00 44.96 ? 382 HOH I O   1 
HETATM 11550 O  O   . HOH NA 5 .   ? 154.880 26.251  9.527   1.00 48.60 ? 383 HOH I O   1 
HETATM 11551 O  O   . HOH NA 5 .   ? 140.073 27.209  2.354   1.00 24.30 ? 384 HOH I O   1 
HETATM 11552 O  O   . HOH NA 5 .   ? 124.677 16.927  11.786  1.00 27.89 ? 385 HOH I O   1 
HETATM 11553 O  O   . HOH NA 5 .   ? 141.045 28.364  24.471  1.00 6.93  ? 386 HOH I O   1 
HETATM 11554 O  O   . HOH NA 5 .   ? 148.474 16.494  28.433  1.00 16.24 ? 387 HOH I O   1 
HETATM 11555 O  O   . HOH NA 5 .   ? 149.007 19.751  24.083  1.00 20.46 ? 388 HOH I O   1 
HETATM 11556 O  O   . HOH NA 5 .   ? 156.753 8.144   19.438  1.00 27.58 ? 389 HOH I O   1 
HETATM 11557 O  O   . HOH NA 5 .   ? 144.335 6.542   26.315  1.00 30.02 ? 390 HOH I O   1 
HETATM 11558 O  O   . HOH NA 5 .   ? 143.584 3.640   21.581  1.00 29.71 ? 391 HOH I O   1 
HETATM 11559 O  O   . HOH NA 5 .   ? 151.850 19.665  21.247  1.00 30.43 ? 392 HOH I O   1 
HETATM 11560 O  O   . HOH NA 5 .   ? 147.223 13.188  29.103  1.00 27.58 ? 393 HOH I O   1 
HETATM 11561 O  O   . HOH NA 5 .   ? 148.299 19.645  21.043  1.00 20.92 ? 394 HOH I O   1 
HETATM 11562 O  O   . HOH NA 5 .   ? 150.553 20.606  18.134  1.00 22.24 ? 395 HOH I O   1 
HETATM 11563 O  O   . HOH NA 5 .   ? 147.900 24.066  24.926  1.00 30.46 ? 396 HOH I O   1 
HETATM 11564 O  O   . HOH NA 5 .   ? 154.072 30.569  23.927  1.00 31.25 ? 397 HOH I O   1 
HETATM 11565 O  O   . HOH NA 5 .   ? 151.756 31.820  23.339  1.00 24.20 ? 398 HOH I O   1 
HETATM 11566 O  O   . HOH NA 5 .   ? 140.531 36.408  17.956  1.00 4.25  ? 399 HOH I O   1 
HETATM 11567 O  O   . HOH NA 5 .   ? 126.512 29.797  28.782  1.00 28.30 ? 400 HOH I O   1 
HETATM 11568 O  O   . HOH NA 5 .   ? 126.562 17.164  21.876  1.00 21.25 ? 401 HOH I O   1 
HETATM 11569 O  O   . HOH NA 5 .   ? 122.658 11.143  25.125  1.00 50.26 ? 402 HOH I O   1 
HETATM 11570 O  O   . HOH NA 5 .   ? 134.785 21.021  14.455  1.00 9.17  ? 403 HOH I O   1 
HETATM 11571 O  O   . HOH OA 5 .   ? 70.861  39.700  28.550  1.00 23.48 ? 156 HOH E O   1 
HETATM 11572 O  O   . HOH OA 5 .   ? 95.479  38.267  28.245  1.00 25.24 ? 157 HOH E O   1 
HETATM 11573 O  O   . HOH OA 5 .   ? 80.202  33.761  16.593  1.00 13.25 ? 158 HOH E O   1 
HETATM 11574 O  O   . HOH OA 5 .   ? 80.392  27.725  0.654   1.00 43.10 ? 159 HOH E O   1 
HETATM 11575 O  O   . HOH OA 5 .   ? 89.382  28.101  28.047  1.00 35.25 ? 160 HOH E O   1 
HETATM 11576 O  O   . HOH OA 5 .   ? 79.115  32.364  19.682  1.00 31.50 ? 161 HOH E O   1 
HETATM 11577 O  O   . HOH OA 5 .   ? 90.846  28.547  19.443  1.00 32.11 ? 162 HOH E O   1 
HETATM 11578 O  O   . HOH OA 5 .   ? 93.397  55.917  13.118  1.00 31.81 ? 163 HOH E O   1 
HETATM 11579 O  O   . HOH OA 5 .   ? 79.352  30.341  16.024  1.00 19.87 ? 164 HOH E O   1 
HETATM 11580 O  O   . HOH OA 5 .   ? 97.620  20.885  8.133   1.00 47.19 ? 165 HOH E O   1 
HETATM 11581 O  O   . HOH OA 5 .   ? 75.673  44.365  21.416  1.00 20.09 ? 166 HOH E O   1 
HETATM 11582 O  O   . HOH OA 5 .   ? 98.565  37.991  30.497  1.00 46.55 ? 167 HOH E O   1 
HETATM 11583 O  O   . HOH OA 5 .   ? 84.650  46.379  28.107  1.00 24.16 ? 168 HOH E O   1 
HETATM 11584 O  O   . HOH OA 5 .   ? 94.769  47.454  22.807  1.00 47.23 ? 169 HOH E O   1 
HETATM 11585 O  O   . HOH OA 5 .   ? 93.063  41.309  32.660  1.00 29.66 ? 170 HOH E O   1 
HETATM 11586 O  O   . HOH OA 5 .   ? 100.962 32.823  -3.993  1.00 44.67 ? 171 HOH E O   1 
HETATM 11587 O  O   . HOH OA 5 .   ? 80.608  39.724  30.721  1.00 50.41 ? 172 HOH E O   1 
HETATM 11588 O  O   . HOH OA 5 .   ? 82.206  45.728  24.879  1.00 11.46 ? 173 HOH E O   1 
HETATM 11589 O  O   . HOH OA 5 .   ? 103.543 43.476  15.101  1.00 8.10  ? 174 HOH E O   1 
HETATM 11590 O  O   . HOH OA 5 .   ? 88.233  50.827  14.534  1.00 19.20 ? 175 HOH E O   1 
HETATM 11591 O  O   . HOH OA 5 .   ? 88.341  45.971  -0.594  1.00 11.78 ? 176 HOH E O   1 
HETATM 11592 O  O   . HOH OA 5 .   ? 88.083  38.410  -4.936  1.00 54.00 ? 177 HOH E O   1 
HETATM 11593 O  O   . HOH OA 5 .   ? 86.385  52.961  3.091   1.00 28.25 ? 178 HOH E O   1 
HETATM 11594 O  O   . HOH OA 5 .   ? 91.223  55.465  6.715   1.00 47.80 ? 179 HOH E O   1 
HETATM 11595 O  O   . HOH OA 5 .   ? 74.929  43.582  -1.618  1.00 30.14 ? 180 HOH E O   1 
HETATM 11596 O  O   . HOH OA 5 .   ? 80.642  32.641  14.053  1.00 26.23 ? 181 HOH E O   1 
HETATM 11597 O  O   . HOH OA 5 .   ? 77.592  49.794  17.854  1.00 33.68 ? 182 HOH E O   1 
HETATM 11598 O  O   . HOH OA 5 .   ? 82.734  55.864  16.085  1.00 50.38 ? 183 HOH E O   1 
HETATM 11599 O  O   . HOH OA 5 .   ? 100.240 54.263  16.294  1.00 50.84 ? 184 HOH E O   1 
HETATM 11600 O  O   . HOH OA 5 .   ? 93.373  55.175  9.953   1.00 37.00 ? 185 HOH E O   1 
HETATM 11601 O  O   . HOH OA 5 .   ? 89.007  50.973  11.983  1.00 21.78 ? 186 HOH E O   1 
HETATM 11602 O  O   . HOH OA 5 .   ? 84.732  53.380  15.761  1.00 38.99 ? 187 HOH E O   1 
HETATM 11603 O  O   . HOH OA 5 .   ? 95.651  52.992  4.323   1.00 39.31 ? 188 HOH E O   1 
HETATM 11604 O  O   . HOH OA 5 .   ? 101.419 47.549  3.356   1.00 40.70 ? 189 HOH E O   1 
HETATM 11605 O  O   . HOH OA 5 .   ? 106.317 54.836  14.828  1.00 51.96 ? 190 HOH E O   1 
HETATM 11606 O  O   . HOH OA 5 .   ? 96.197  26.360  -8.391  1.00 49.02 ? 191 HOH E O   1 
HETATM 11607 O  O   . HOH OA 5 .   ? 104.329 22.871  6.980   1.00 36.05 ? 192 HOH E O   1 
HETATM 11608 O  O   . HOH OA 5 .   ? 99.781  35.850  16.930  1.00 2.00  ? 193 HOH E O   1 
HETATM 11609 O  O   . HOH OA 5 .   ? 100.508 38.422  17.958  1.00 6.33  ? 194 HOH E O   1 
HETATM 11610 O  O   . HOH PA 5 .   ? 118.428 25.634  27.717  1.00 24.03 ? 156 HOH J O   1 
HETATM 11611 O  O   . HOH PA 5 .   ? 134.552 26.059  16.914  1.00 17.35 ? 157 HOH J O   1 
HETATM 11612 O  O   . HOH PA 5 .   ? 121.460 24.334  24.158  1.00 22.45 ? 158 HOH J O   1 
HETATM 11613 O  O   . HOH PA 5 .   ? 120.167 24.675  21.092  1.00 10.89 ? 159 HOH J O   1 
HETATM 11614 O  O   . HOH PA 5 .   ? 106.113 40.413  -4.174  1.00 37.27 ? 160 HOH J O   1 
HETATM 11615 O  O   . HOH PA 5 .   ? 114.705 36.768  -8.648  1.00 41.78 ? 161 HOH J O   1 
HETATM 11616 O  O   . HOH PA 5 .   ? 116.980 26.121  -5.330  1.00 34.30 ? 162 HOH J O   1 
HETATM 11617 O  O   . HOH PA 5 .   ? 122.289 22.241  -0.239  1.00 37.26 ? 163 HOH J O   1 
HETATM 11618 O  O   . HOH PA 5 .   ? 129.962 21.859  13.374  1.00 9.77  ? 164 HOH J O   1 
HETATM 11619 O  O   . HOH PA 5 .   ? 133.480 24.320  11.484  1.00 25.92 ? 165 HOH J O   1 
HETATM 11620 O  O   . HOH PA 5 .   ? 129.323 25.058  20.313  1.00 2.00  ? 166 HOH J O   1 
HETATM 11621 O  O   . HOH PA 5 .   ? 129.116 19.783  7.986   1.00 25.54 ? 167 HOH J O   1 
HETATM 11622 O  O   . HOH PA 5 .   ? 121.286 20.002  22.955  1.00 59.83 ? 168 HOH J O   1 
HETATM 11623 O  O   . HOH PA 5 .   ? 100.088 24.433  13.499  1.00 38.84 ? 169 HOH J O   1 
HETATM 11624 O  O   . HOH PA 5 .   ? 109.150 48.611  24.069  1.00 58.60 ? 170 HOH J O   1 
HETATM 11625 O  O   . HOH PA 5 .   ? 104.405 40.499  16.420  1.00 10.30 ? 171 HOH J O   1 
HETATM 11626 O  O   . HOH PA 5 .   ? 110.155 53.367  5.657   1.00 34.04 ? 172 HOH J O   1 
HETATM 11627 O  O   . HOH PA 5 .   ? 111.583 27.469  27.490  1.00 57.18 ? 173 HOH J O   1 
HETATM 11628 O  O   . HOH PA 5 .   ? 130.059 36.848  27.145  1.00 34.37 ? 174 HOH J O   1 
HETATM 11629 O  O   . HOH PA 5 .   ? 120.430 35.421  28.311  1.00 30.09 ? 175 HOH J O   1 
HETATM 11630 O  O   . HOH PA 5 .   ? 130.834 38.977  24.051  1.00 27.28 ? 176 HOH J O   1 
HETATM 11631 O  O   . HOH PA 5 .   ? 100.306 33.184  16.330  1.00 2.82  ? 177 HOH J O   1 
HETATM 11632 O  O   . HOH PA 5 .   ? 116.384 25.916  20.104  1.00 30.90 ? 178 HOH J O   1 
HETATM 11633 O  O   . HOH PA 5 .   ? 117.057 34.898  -0.626  1.00 34.08 ? 179 HOH J O   1 
HETATM 11634 O  O   . HOH PA 5 .   ? 117.614 27.607  3.906   1.00 13.06 ? 180 HOH J O   1 
HETATM 11635 O  O   . HOH PA 5 .   ? 111.508 25.859  6.379   1.00 31.28 ? 181 HOH J O   1 
HETATM 11636 O  O   . HOH PA 5 .   ? 131.113 30.460  3.201   1.00 34.32 ? 182 HOH J O   1 
HETATM 11637 O  O   . HOH PA 5 .   ? 120.797 18.933  9.418   1.00 23.08 ? 183 HOH J O   1 
HETATM 11638 O  O   . HOH PA 5 .   ? 124.969 38.526  13.695  1.00 30.76 ? 184 HOH J O   1 
HETATM 11639 O  O   . HOH PA 5 .   ? 121.480 51.233  15.360  1.00 32.50 ? 185 HOH J O   1 
HETATM 11640 O  O   . HOH PA 5 .   ? 127.224 30.900  24.895  1.00 8.57  ? 186 HOH J O   1 
HETATM 11641 O  O   . HOH PA 5 .   ? 111.612 24.934  21.989  1.00 25.35 ? 187 HOH J O   1 
HETATM 11642 O  O   . HOH PA 5 .   ? 112.482 26.088  24.348  1.00 25.38 ? 188 HOH J O   1 
HETATM 11643 O  O   . HOH PA 5 .   ? 114.434 26.553  29.712  1.00 38.17 ? 189 HOH J O   1 
HETATM 11644 O  O   . HOH PA 5 .   ? 103.226 24.779  14.830  1.00 35.22 ? 190 HOH J O   1 
HETATM 11645 O  O   . HOH PA 5 .   ? 115.000 25.334  15.617  1.00 19.09 ? 191 HOH J O   1 
HETATM 11646 O  O   . HOH PA 5 .   ? 112.431 35.416  -2.612  1.00 29.85 ? 192 HOH J O   1 
HETATM 11647 O  O   . HOH PA 5 .   ? 111.166 22.817  16.021  1.00 39.37 ? 193 HOH J O   1 
HETATM 11648 O  O   . HOH PA 5 .   ? 116.563 24.649  13.315  1.00 9.81  ? 194 HOH J O   1 
HETATM 11649 O  O   . HOH PA 5 .   ? 110.409 21.921  21.285  1.00 32.14 ? 195 HOH J O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ACE 1   0   0   ACE ACE A . n 
A 1 2   ALA 2   1   1   ALA ALA A . n 
A 1 3   THR 3   2   2   THR THR A . n 
A 1 4   LYS 4   3   3   LYS LYS A . n 
A 1 5   ALA 5   4   4   ALA ALA A . n 
A 1 6   VAL 6   5   5   VAL VAL A . n 
A 1 7   ALA 7   6   6   ALA ALA A . n 
A 1 8   VAL 8   7   7   VAL VAL A . n 
A 1 9   LEU 9   8   8   LEU LEU A . n 
A 1 10  LYS 10  9   9   LYS LYS A . n 
A 1 11  GLY 11  10  10  GLY GLY A . n 
A 1 12  ASP 12  11  11  ASP ASP A . n 
A 1 13  GLY 13  12  12  GLY GLY A . n 
A 1 14  PRO 14  13  13  PRO PRO A . n 
A 1 15  VAL 15  14  14  VAL VAL A . n 
A 1 16  GLN 16  15  15  GLN GLN A . n 
A 1 17  GLY 17  16  16  GLY GLY A . n 
A 1 18  ILE 18  17  17  ILE ILE A . n 
A 1 19  ILE 19  18  18  ILE ILE A . n 
A 1 20  ASN 20  19  19  ASN ASN A . n 
A 1 21  PHE 21  20  20  PHE PHE A . n 
A 1 22  GLU 22  21  21  GLU GLU A . n 
A 1 23  GLN 23  22  22  GLN GLN A . n 
A 1 24  LYS 24  23  23  LYS LYS A . n 
A 1 25  GLU 25  24  24  GLU GLU A . n 
A 1 26  SER 26  25  25  SER SER A . n 
A 1 27  ASN 27  26  26  ASN ASN A . n 
A 1 28  GLY 28  27  27  GLY GLY A . n 
A 1 29  PRO 29  28  28  PRO PRO A . n 
A 1 30  VAL 30  29  29  VAL VAL A . n 
A 1 31  LYS 31  30  30  LYS LYS A . n 
A 1 32  VAL 32  31  31  VAL VAL A . n 
A 1 33  TRP 33  32  32  TRP TRP A . n 
A 1 34  GLY 34  33  33  GLY GLY A . n 
A 1 35  SER 35  34  34  SER SER A . n 
A 1 36  ILE 36  35  35  ILE ILE A . n 
A 1 37  LYS 37  36  36  LYS LYS A . n 
A 1 38  GLY 38  37  37  GLY GLY A . n 
A 1 39  LEU 39  38  38  LEU LEU A . n 
A 1 40  THR 40  39  39  THR THR A . n 
A 1 41  GLU 41  40  40  GLU GLU A . n 
A 1 42  GLY 42  41  41  GLY GLY A . n 
A 1 43  LEU 43  42  42  LEU LEU A . n 
A 1 44  HIS 44  43  43  HIS HIS A . n 
A 1 45  GLY 45  44  44  GLY GLY A . n 
A 1 46  PHE 46  45  45  PHE PHE A . n 
A 1 47  HIS 47  46  46  HIS HIS A . n 
A 1 48  VAL 48  47  47  VAL VAL A . n 
A 1 49  HIS 49  48  48  HIS HIS A . n 
A 1 50  GLU 50  49  49  GLU GLU A . n 
A 1 51  PHE 51  50  50  PHE PHE A . n 
A 1 52  GLY 52  51  51  GLY GLY A . n 
A 1 53  ASP 53  52  52  ASP ASP A . n 
A 1 54  ASN 54  53  53  ASN ASN A . n 
A 1 55  THR 55  54  54  THR THR A . n 
A 1 56  ALA 56  55  55  ALA ALA A . n 
A 1 57  GLY 57  56  56  GLY GLY A . n 
A 1 58  CYS 58  57  57  CYS CYS A . n 
A 1 59  THR 59  58  58  THR THR A . n 
A 1 60  SER 60  59  59  SER SER A . n 
A 1 61  ALA 61  60  60  ALA ALA A . n 
A 1 62  GLY 62  61  61  GLY GLY A . n 
A 1 63  PRO 63  62  62  PRO PRO A . n 
A 1 64  HIS 64  63  63  HIS HIS A . n 
A 1 65  PHE 65  64  64  PHE PHE A . n 
A 1 66  ASN 66  65  65  ASN ASN A . n 
A 1 67  PRO 67  66  66  PRO PRO A . n 
A 1 68  LEU 68  67  67  LEU LEU A . n 
A 1 69  SER 69  68  68  SER SER A . n 
A 1 70  ARG 70  69  69  ARG ARG A . n 
A 1 71  LYS 71  70  70  LYS LYS A . n 
A 1 72  HIS 72  71  71  HIS HIS A . n 
A 1 73  GLY 73  72  72  GLY GLY A . n 
A 1 74  GLY 74  73  73  GLY GLY A . n 
A 1 75  PRO 75  74  74  PRO PRO A . n 
A 1 76  LYS 76  75  75  LYS LYS A . n 
A 1 77  ASP 77  76  76  ASP ASP A . n 
A 1 78  GLU 78  77  77  GLU GLU A . n 
A 1 79  GLU 79  78  78  GLU GLU A . n 
A 1 80  ARG 80  79  79  ARG ARG A . n 
A 1 81  HIS 81  80  80  HIS HIS A . n 
A 1 82  VAL 82  81  81  VAL VAL A . n 
A 1 83  GLY 83  82  82  GLY GLY A . n 
A 1 84  ASP 84  83  83  ASP ASP A . n 
A 1 85  LEU 85  84  84  LEU LEU A . n 
A 1 86  GLY 86  85  85  GLY GLY A . n 
A 1 87  ASN 87  86  86  ASN ASN A . n 
A 1 88  VAL 88  87  87  VAL VAL A . n 
A 1 89  THR 89  88  88  THR THR A . n 
A 1 90  ALA 90  89  89  ALA ALA A . n 
A 1 91  ASP 91  90  90  ASP ASP A . n 
A 1 92  LYS 92  91  91  LYS LYS A . n 
A 1 93  ASP 93  92  92  ASP ASP A . n 
A 1 94  GLY 94  93  93  GLY GLY A . n 
A 1 95  VAL 95  94  94  VAL VAL A . n 
A 1 96  ALA 96  95  95  ALA ALA A . n 
A 1 97  ASP 97  96  96  ASP ASP A . n 
A 1 98  VAL 98  97  97  VAL VAL A . n 
A 1 99  SER 99  98  98  SER SER A . n 
A 1 100 ILE 100 99  99  ILE ILE A . n 
A 1 101 GLU 101 100 100 GLU GLU A . n 
A 1 102 ASP 102 101 101 ASP ASP A . n 
A 1 103 SER 103 102 102 SER SER A . n 
A 1 104 VAL 104 103 103 VAL VAL A . n 
A 1 105 ILE 105 104 104 ILE ILE A . n 
A 1 106 SER 106 105 105 SER SER A . n 
A 1 107 LEU 107 106 106 LEU LEU A . n 
A 1 108 SER 108 107 107 SER SER A . n 
A 1 109 GLY 109 108 108 GLY GLY A . n 
A 1 110 ASP 110 109 109 ASP ASP A . n 
A 1 111 HIS 111 110 110 HIS HIS A . n 
A 1 112 SER 112 111 111 SER SER A . n 
A 1 113 ILE 113 112 112 ILE ILE A . n 
A 1 114 ILE 114 113 113 ILE ILE A . n 
A 1 115 GLY 115 114 114 GLY GLY A . n 
A 1 116 ARG 116 115 115 ARG ARG A . n 
A 1 117 THR 117 116 116 THR THR A . n 
A 1 118 LEU 118 117 117 LEU LEU A . n 
A 1 119 VAL 119 118 118 VAL VAL A . n 
A 1 120 VAL 120 119 119 VAL VAL A . n 
A 1 121 HIS 121 120 120 HIS HIS A . n 
A 1 122 GLU 122 121 121 GLU GLU A . n 
A 1 123 LYS 123 122 122 LYS LYS A . n 
A 1 124 ALA 124 123 123 ALA ALA A . n 
A 1 125 ASP 125 124 124 ASP ASP A . n 
A 1 126 ASP 126 125 125 ASP ASP A . n 
A 1 127 LEU 127 126 126 LEU LEU A . n 
A 1 128 GLY 128 127 127 GLY GLY A . n 
A 1 129 LYS 129 128 128 LYS LYS A . n 
A 1 130 GLY 130 129 129 GLY GLY A . n 
A 1 131 GLY 131 130 130 GLY GLY A . n 
A 1 132 ASN 132 131 131 ASN ASN A . n 
A 1 133 GLU 133 132 132 GLU GLU A . n 
A 1 134 GLU 134 133 133 GLU GLU A . n 
A 1 135 SER 135 134 134 SER SER A . n 
A 1 136 THR 136 135 135 THR THR A . n 
A 1 137 LYS 137 136 136 LYS LYS A . n 
A 1 138 THR 138 137 137 THR THR A . n 
A 1 139 GLY 139 138 138 GLY GLY A . n 
A 1 140 ASN 140 139 139 ASN ASN A . n 
A 1 141 ALA 141 140 140 ALA ALA A . n 
A 1 142 GLY 142 141 141 GLY GLY A . n 
A 1 143 SER 143 142 142 SER SER A . n 
A 1 144 ARG 144 143 143 ARG ARG A . n 
A 1 145 LEU 145 144 144 LEU LEU A . n 
A 1 146 ALA 146 145 145 ALA ALA A . n 
A 1 147 CYS 147 146 146 CYS CYS A . n 
A 1 148 GLY 148 147 147 GLY GLY A . n 
A 1 149 VAL 149 148 148 VAL VAL A . n 
A 1 150 ILE 150 149 149 ILE ILE A . n 
A 1 151 GLY 151 150 150 GLY GLY A . n 
A 1 152 ILE 152 151 151 ILE ILE A . n 
A 1 153 ALA 153 152 152 ALA ALA A . n 
A 1 154 GLN 154 153 153 GLN GLN A . n 
B 1 1   ACE 1   0   0   ACE ACE F . n 
B 1 2   ALA 2   1   1   ALA ALA F . n 
B 1 3   THR 3   2   2   THR THR F . n 
B 1 4   LYS 4   3   3   LYS LYS F . n 
B 1 5   ALA 5   4   4   ALA ALA F . n 
B 1 6   VAL 6   5   5   VAL VAL F . n 
B 1 7   ALA 7   6   6   ALA ALA F . n 
B 1 8   VAL 8   7   7   VAL VAL F . n 
B 1 9   LEU 9   8   8   LEU LEU F . n 
B 1 10  LYS 10  9   9   LYS LYS F . n 
B 1 11  GLY 11  10  10  GLY GLY F . n 
B 1 12  ASP 12  11  11  ASP ASP F . n 
B 1 13  GLY 13  12  12  GLY GLY F . n 
B 1 14  PRO 14  13  13  PRO PRO F . n 
B 1 15  VAL 15  14  14  VAL VAL F . n 
B 1 16  GLN 16  15  15  GLN GLN F . n 
B 1 17  GLY 17  16  16  GLY GLY F . n 
B 1 18  ILE 18  17  17  ILE ILE F . n 
B 1 19  ILE 19  18  18  ILE ILE F . n 
B 1 20  ASN 20  19  19  ASN ASN F . n 
B 1 21  PHE 21  20  20  PHE PHE F . n 
B 1 22  GLU 22  21  21  GLU GLU F . n 
B 1 23  GLN 23  22  22  GLN GLN F . n 
B 1 24  LYS 24  23  23  LYS LYS F . n 
B 1 25  GLU 25  24  24  GLU GLU F . n 
B 1 26  SER 26  25  25  SER SER F . n 
B 1 27  ASN 27  26  26  ASN ASN F . n 
B 1 28  GLY 28  27  27  GLY GLY F . n 
B 1 29  PRO 29  28  28  PRO PRO F . n 
B 1 30  VAL 30  29  29  VAL VAL F . n 
B 1 31  LYS 31  30  30  LYS LYS F . n 
B 1 32  VAL 32  31  31  VAL VAL F . n 
B 1 33  TRP 33  32  32  TRP TRP F . n 
B 1 34  GLY 34  33  33  GLY GLY F . n 
B 1 35  SER 35  34  34  SER SER F . n 
B 1 36  ILE 36  35  35  ILE ILE F . n 
B 1 37  LYS 37  36  36  LYS LYS F . n 
B 1 38  GLY 38  37  37  GLY GLY F . n 
B 1 39  LEU 39  38  38  LEU LEU F . n 
B 1 40  THR 40  39  39  THR THR F . n 
B 1 41  GLU 41  40  40  GLU GLU F . n 
B 1 42  GLY 42  41  41  GLY GLY F . n 
B 1 43  LEU 43  42  42  LEU LEU F . n 
B 1 44  HIS 44  43  43  HIS HIS F . n 
B 1 45  GLY 45  44  44  GLY GLY F . n 
B 1 46  PHE 46  45  45  PHE PHE F . n 
B 1 47  HIS 47  46  46  HIS HIS F . n 
B 1 48  VAL 48  47  47  VAL VAL F . n 
B 1 49  HIS 49  48  48  HIS HIS F . n 
B 1 50  GLU 50  49  49  GLU GLU F . n 
B 1 51  PHE 51  50  50  PHE PHE F . n 
B 1 52  GLY 52  51  51  GLY GLY F . n 
B 1 53  ASP 53  52  52  ASP ASP F . n 
B 1 54  ASN 54  53  53  ASN ASN F . n 
B 1 55  THR 55  54  54  THR THR F . n 
B 1 56  ALA 56  55  55  ALA ALA F . n 
B 1 57  GLY 57  56  56  GLY GLY F . n 
B 1 58  CYS 58  57  57  CYS CYS F . n 
B 1 59  THR 59  58  58  THR THR F . n 
B 1 60  SER 60  59  59  SER SER F . n 
B 1 61  ALA 61  60  60  ALA ALA F . n 
B 1 62  GLY 62  61  61  GLY GLY F . n 
B 1 63  PRO 63  62  62  PRO PRO F . n 
B 1 64  HIS 64  63  63  HIS HIS F . n 
B 1 65  PHE 65  64  64  PHE PHE F . n 
B 1 66  ASN 66  65  65  ASN ASN F . n 
B 1 67  PRO 67  66  66  PRO PRO F . n 
B 1 68  LEU 68  67  67  LEU LEU F . n 
B 1 69  SER 69  68  68  SER SER F . n 
B 1 70  ARG 70  69  69  ARG ARG F . n 
B 1 71  LYS 71  70  70  LYS LYS F . n 
B 1 72  HIS 72  71  71  HIS HIS F . n 
B 1 73  GLY 73  72  72  GLY GLY F . n 
B 1 74  GLY 74  73  73  GLY GLY F . n 
B 1 75  PRO 75  74  74  PRO PRO F . n 
B 1 76  LYS 76  75  75  LYS LYS F . n 
B 1 77  ASP 77  76  76  ASP ASP F . n 
B 1 78  GLU 78  77  77  GLU GLU F . n 
B 1 79  GLU 79  78  78  GLU GLU F . n 
B 1 80  ARG 80  79  79  ARG ARG F . n 
B 1 81  HIS 81  80  80  HIS HIS F . n 
B 1 82  VAL 82  81  81  VAL VAL F . n 
B 1 83  GLY 83  82  82  GLY GLY F . n 
B 1 84  ASP 84  83  83  ASP ASP F . n 
B 1 85  LEU 85  84  84  LEU LEU F . n 
B 1 86  GLY 86  85  85  GLY GLY F . n 
B 1 87  ASN 87  86  86  ASN ASN F . n 
B 1 88  VAL 88  87  87  VAL VAL F . n 
B 1 89  THR 89  88  88  THR THR F . n 
B 1 90  ALA 90  89  89  ALA ALA F . n 
B 1 91  ASP 91  90  90  ASP ASP F . n 
B 1 92  LYS 92  91  91  LYS LYS F . n 
B 1 93  ASP 93  92  92  ASP ASP F . n 
B 1 94  GLY 94  93  93  GLY GLY F . n 
B 1 95  VAL 95  94  94  VAL VAL F . n 
B 1 96  ALA 96  95  95  ALA ALA F . n 
B 1 97  ASP 97  96  96  ASP ASP F . n 
B 1 98  VAL 98  97  97  VAL VAL F . n 
B 1 99  SER 99  98  98  SER SER F . n 
B 1 100 ILE 100 99  99  ILE ILE F . n 
B 1 101 GLU 101 100 100 GLU GLU F . n 
B 1 102 ASP 102 101 101 ASP ASP F . n 
B 1 103 SER 103 102 102 SER SER F . n 
B 1 104 VAL 104 103 103 VAL VAL F . n 
B 1 105 ILE 105 104 104 ILE ILE F . n 
B 1 106 SER 106 105 105 SER SER F . n 
B 1 107 LEU 107 106 106 LEU LEU F . n 
B 1 108 SER 108 107 107 SER SER F . n 
B 1 109 GLY 109 108 108 GLY GLY F . n 
B 1 110 ASP 110 109 109 ASP ASP F . n 
B 1 111 HIS 111 110 110 HIS HIS F . n 
B 1 112 SER 112 111 111 SER SER F . n 
B 1 113 ILE 113 112 112 ILE ILE F . n 
B 1 114 ILE 114 113 113 ILE ILE F . n 
B 1 115 GLY 115 114 114 GLY GLY F . n 
B 1 116 ARG 116 115 115 ARG ARG F . n 
B 1 117 THR 117 116 116 THR THR F . n 
B 1 118 LEU 118 117 117 LEU LEU F . n 
B 1 119 VAL 119 118 118 VAL VAL F . n 
B 1 120 VAL 120 119 119 VAL VAL F . n 
B 1 121 HIS 121 120 120 HIS HIS F . n 
B 1 122 GLU 122 121 121 GLU GLU F . n 
B 1 123 LYS 123 122 122 LYS LYS F . n 
B 1 124 ALA 124 123 123 ALA ALA F . n 
B 1 125 ASP 125 124 124 ASP ASP F . n 
B 1 126 ASP 126 125 125 ASP ASP F . n 
B 1 127 LEU 127 126 126 LEU LEU F . n 
B 1 128 GLY 128 127 127 GLY GLY F . n 
B 1 129 LYS 129 128 128 LYS LYS F . n 
B 1 130 GLY 130 129 129 GLY GLY F . n 
B 1 131 GLY 131 130 130 GLY GLY F . n 
B 1 132 ASN 132 131 131 ASN ASN F . n 
B 1 133 GLU 133 132 132 GLU GLU F . n 
B 1 134 GLU 134 133 133 GLU GLU F . n 
B 1 135 SER 135 134 134 SER SER F . n 
B 1 136 THR 136 135 135 THR THR F . n 
B 1 137 LYS 137 136 136 LYS LYS F . n 
B 1 138 THR 138 137 137 THR THR F . n 
B 1 139 GLY 139 138 138 GLY GLY F . n 
B 1 140 ASN 140 139 139 ASN ASN F . n 
B 1 141 ALA 141 140 140 ALA ALA F . n 
B 1 142 GLY 142 141 141 GLY GLY F . n 
B 1 143 SER 143 142 142 SER SER F . n 
B 1 144 ARG 144 143 143 ARG ARG F . n 
B 1 145 LEU 145 144 144 LEU LEU F . n 
B 1 146 ALA 146 145 145 ALA ALA F . n 
B 1 147 CYS 147 146 146 CYS CYS F . n 
B 1 148 GLY 148 147 147 GLY GLY F . n 
B 1 149 VAL 149 148 148 VAL VAL F . n 
B 1 150 ILE 150 149 149 ILE ILE F . n 
B 1 151 GLY 151 150 150 GLY GLY F . n 
B 1 152 ILE 152 151 151 ILE ILE F . n 
B 1 153 ALA 153 152 152 ALA ALA F . n 
B 1 154 GLN 154 153 153 GLN GLN F . n 
C 1 1   ACE 1   0   0   ACE ACE B . n 
C 1 2   ALA 2   1   1   ALA ALA B . n 
C 1 3   THR 3   2   2   THR THR B . n 
C 1 4   LYS 4   3   3   LYS LYS B . n 
C 1 5   ALA 5   4   4   ALA ALA B . n 
C 1 6   VAL 6   5   5   VAL VAL B . n 
C 1 7   ALA 7   6   6   ALA ALA B . n 
C 1 8   VAL 8   7   7   VAL VAL B . n 
C 1 9   LEU 9   8   8   LEU LEU B . n 
C 1 10  LYS 10  9   9   LYS LYS B . n 
C 1 11  GLY 11  10  10  GLY GLY B . n 
C 1 12  ASP 12  11  11  ASP ASP B . n 
C 1 13  GLY 13  12  12  GLY GLY B . n 
C 1 14  PRO 14  13  13  PRO PRO B . n 
C 1 15  VAL 15  14  14  VAL VAL B . n 
C 1 16  GLN 16  15  15  GLN GLN B . n 
C 1 17  GLY 17  16  16  GLY GLY B . n 
C 1 18  ILE 18  17  17  ILE ILE B . n 
C 1 19  ILE 19  18  18  ILE ILE B . n 
C 1 20  ASN 20  19  19  ASN ASN B . n 
C 1 21  PHE 21  20  20  PHE PHE B . n 
C 1 22  GLU 22  21  21  GLU GLU B . n 
C 1 23  GLN 23  22  22  GLN GLN B . n 
C 1 24  LYS 24  23  23  LYS LYS B . n 
C 1 25  GLU 25  24  24  GLU GLU B . n 
C 1 26  SER 26  25  25  SER SER B . n 
C 1 27  ASN 27  26  26  ASN ASN B . n 
C 1 28  GLY 28  27  27  GLY GLY B . n 
C 1 29  PRO 29  28  28  PRO PRO B . n 
C 1 30  VAL 30  29  29  VAL VAL B . n 
C 1 31  LYS 31  30  30  LYS LYS B . n 
C 1 32  VAL 32  31  31  VAL VAL B . n 
C 1 33  TRP 33  32  32  TRP TRP B . n 
C 1 34  GLY 34  33  33  GLY GLY B . n 
C 1 35  SER 35  34  34  SER SER B . n 
C 1 36  ILE 36  35  35  ILE ILE B . n 
C 1 37  LYS 37  36  36  LYS LYS B . n 
C 1 38  GLY 38  37  37  GLY GLY B . n 
C 1 39  LEU 39  38  38  LEU LEU B . n 
C 1 40  THR 40  39  39  THR THR B . n 
C 1 41  GLU 41  40  40  GLU GLU B . n 
C 1 42  GLY 42  41  41  GLY GLY B . n 
C 1 43  LEU 43  42  42  LEU LEU B . n 
C 1 44  HIS 44  43  43  HIS HIS B . n 
C 1 45  GLY 45  44  44  GLY GLY B . n 
C 1 46  PHE 46  45  45  PHE PHE B . n 
C 1 47  HIS 47  46  46  HIS HIS B . n 
C 1 48  VAL 48  47  47  VAL VAL B . n 
C 1 49  HIS 49  48  48  HIS HIS B . n 
C 1 50  GLU 50  49  49  GLU GLU B . n 
C 1 51  PHE 51  50  50  PHE PHE B . n 
C 1 52  GLY 52  51  51  GLY GLY B . n 
C 1 53  ASP 53  52  52  ASP ASP B . n 
C 1 54  ASN 54  53  53  ASN ASN B . n 
C 1 55  THR 55  54  54  THR THR B . n 
C 1 56  ALA 56  55  55  ALA ALA B . n 
C 1 57  GLY 57  56  56  GLY GLY B . n 
C 1 58  CYS 58  57  57  CYS CYS B . n 
C 1 59  THR 59  58  58  THR THR B . n 
C 1 60  SER 60  59  59  SER SER B . n 
C 1 61  ALA 61  60  60  ALA ALA B . n 
C 1 62  GLY 62  61  61  GLY GLY B . n 
C 1 63  PRO 63  62  62  PRO PRO B . n 
C 1 64  HIS 64  63  63  HIS HIS B . n 
C 1 65  PHE 65  64  64  PHE PHE B . n 
C 1 66  ASN 66  65  65  ASN ASN B . n 
C 1 67  PRO 67  66  66  PRO PRO B . n 
C 1 68  LEU 68  67  67  LEU LEU B . n 
C 1 69  SER 69  68  68  SER SER B . n 
C 1 70  ARG 70  69  69  ARG ARG B . n 
C 1 71  LYS 71  70  70  LYS LYS B . n 
C 1 72  HIS 72  71  71  HIS HIS B . n 
C 1 73  GLY 73  72  72  GLY GLY B . n 
C 1 74  GLY 74  73  73  GLY GLY B . n 
C 1 75  PRO 75  74  74  PRO PRO B . n 
C 1 76  LYS 76  75  75  LYS LYS B . n 
C 1 77  ASP 77  76  76  ASP ASP B . n 
C 1 78  GLU 78  77  77  GLU GLU B . n 
C 1 79  GLU 79  78  78  GLU GLU B . n 
C 1 80  ARG 80  79  79  ARG ARG B . n 
C 1 81  HIS 81  80  80  HIS HIS B . n 
C 1 82  VAL 82  81  81  VAL VAL B . n 
C 1 83  GLY 83  82  82  GLY GLY B . n 
C 1 84  ASP 84  83  83  ASP ASP B . n 
C 1 85  LEU 85  84  84  LEU LEU B . n 
C 1 86  GLY 86  85  85  GLY GLY B . n 
C 1 87  ASN 87  86  86  ASN ASN B . n 
C 1 88  VAL 88  87  87  VAL VAL B . n 
C 1 89  THR 89  88  88  THR THR B . n 
C 1 90  ALA 90  89  89  ALA ALA B . n 
C 1 91  ASP 91  90  90  ASP ASP B . n 
C 1 92  LYS 92  91  91  LYS LYS B . n 
C 1 93  ASP 93  92  92  ASP ASP B . n 
C 1 94  GLY 94  93  93  GLY GLY B . n 
C 1 95  VAL 95  94  94  VAL VAL B . n 
C 1 96  ALA 96  95  95  ALA ALA B . n 
C 1 97  ASP 97  96  96  ASP ASP B . n 
C 1 98  VAL 98  97  97  VAL VAL B . n 
C 1 99  SER 99  98  98  SER SER B . n 
C 1 100 ILE 100 99  99  ILE ILE B . n 
C 1 101 GLU 101 100 100 GLU GLU B . n 
C 1 102 ASP 102 101 101 ASP ASP B . n 
C 1 103 SER 103 102 102 SER SER B . n 
C 1 104 VAL 104 103 103 VAL VAL B . n 
C 1 105 ILE 105 104 104 ILE ILE B . n 
C 1 106 SER 106 105 105 SER SER B . n 
C 1 107 LEU 107 106 106 LEU LEU B . n 
C 1 108 SER 108 107 107 SER SER B . n 
C 1 109 GLY 109 108 108 GLY GLY B . n 
C 1 110 ASP 110 109 109 ASP ASP B . n 
C 1 111 HIS 111 110 110 HIS HIS B . n 
C 1 112 SER 112 111 111 SER SER B . n 
C 1 113 ILE 113 112 112 ILE ILE B . n 
C 1 114 ILE 114 113 113 ILE ILE B . n 
C 1 115 GLY 115 114 114 GLY GLY B . n 
C 1 116 ARG 116 115 115 ARG ARG B . n 
C 1 117 THR 117 116 116 THR THR B . n 
C 1 118 LEU 118 117 117 LEU LEU B . n 
C 1 119 VAL 119 118 118 VAL VAL B . n 
C 1 120 VAL 120 119 119 VAL VAL B . n 
C 1 121 HIS 121 120 120 HIS HIS B . n 
C 1 122 GLU 122 121 121 GLU GLU B . n 
C 1 123 LYS 123 122 122 LYS LYS B . n 
C 1 124 ALA 124 123 123 ALA ALA B . n 
C 1 125 ASP 125 124 124 ASP ASP B . n 
C 1 126 ASP 126 125 125 ASP ASP B . n 
C 1 127 LEU 127 126 126 LEU LEU B . n 
C 1 128 GLY 128 127 127 GLY GLY B . n 
C 1 129 LYS 129 128 128 LYS LYS B . n 
C 1 130 GLY 130 129 129 GLY GLY B . n 
C 1 131 GLY 131 130 130 GLY GLY B . n 
C 1 132 ASN 132 131 131 ASN ASN B . n 
C 1 133 GLU 133 132 132 GLU GLU B . n 
C 1 134 GLU 134 133 133 GLU GLU B . n 
C 1 135 SER 135 134 134 SER SER B . n 
C 1 136 THR 136 135 135 THR THR B . n 
C 1 137 LYS 137 136 136 LYS LYS B . n 
C 1 138 THR 138 137 137 THR THR B . n 
C 1 139 GLY 139 138 138 GLY GLY B . n 
C 1 140 ASN 140 139 139 ASN ASN B . n 
C 1 141 ALA 141 140 140 ALA ALA B . n 
C 1 142 GLY 142 141 141 GLY GLY B . n 
C 1 143 SER 143 142 142 SER SER B . n 
C 1 144 ARG 144 143 143 ARG ARG B . n 
C 1 145 LEU 145 144 144 LEU LEU B . n 
C 1 146 ALA 146 145 145 ALA ALA B . n 
C 1 147 CYS 147 146 146 CYS CYS B . n 
C 1 148 GLY 148 147 147 GLY GLY B . n 
C 1 149 VAL 149 148 148 VAL VAL B . n 
C 1 150 ILE 150 149 149 ILE ILE B . n 
C 1 151 GLY 151 150 150 GLY GLY B . n 
C 1 152 ILE 152 151 151 ILE ILE B . n 
C 1 153 ALA 153 152 152 ALA ALA B . n 
C 1 154 GLN 154 153 153 GLN GLN B . n 
D 1 1   ACE 1   0   0   ACE ACE G . n 
D 1 2   ALA 2   1   1   ALA ALA G . n 
D 1 3   THR 3   2   2   THR THR G . n 
D 1 4   LYS 4   3   3   LYS LYS G . n 
D 1 5   ALA 5   4   4   ALA ALA G . n 
D 1 6   VAL 6   5   5   VAL VAL G . n 
D 1 7   ALA 7   6   6   ALA ALA G . n 
D 1 8   VAL 8   7   7   VAL VAL G . n 
D 1 9   LEU 9   8   8   LEU LEU G . n 
D 1 10  LYS 10  9   9   LYS LYS G . n 
D 1 11  GLY 11  10  10  GLY GLY G . n 
D 1 12  ASP 12  11  11  ASP ASP G . n 
D 1 13  GLY 13  12  12  GLY GLY G . n 
D 1 14  PRO 14  13  13  PRO PRO G . n 
D 1 15  VAL 15  14  14  VAL VAL G . n 
D 1 16  GLN 16  15  15  GLN GLN G . n 
D 1 17  GLY 17  16  16  GLY GLY G . n 
D 1 18  ILE 18  17  17  ILE ILE G . n 
D 1 19  ILE 19  18  18  ILE ILE G . n 
D 1 20  ASN 20  19  19  ASN ASN G . n 
D 1 21  PHE 21  20  20  PHE PHE G . n 
D 1 22  GLU 22  21  21  GLU GLU G . n 
D 1 23  GLN 23  22  22  GLN GLN G . n 
D 1 24  LYS 24  23  23  LYS LYS G . n 
D 1 25  GLU 25  24  24  GLU GLU G . n 
D 1 26  SER 26  25  25  SER SER G . n 
D 1 27  ASN 27  26  26  ASN ASN G . n 
D 1 28  GLY 28  27  27  GLY GLY G . n 
D 1 29  PRO 29  28  28  PRO PRO G . n 
D 1 30  VAL 30  29  29  VAL VAL G . n 
D 1 31  LYS 31  30  30  LYS LYS G . n 
D 1 32  VAL 32  31  31  VAL VAL G . n 
D 1 33  TRP 33  32  32  TRP TRP G . n 
D 1 34  GLY 34  33  33  GLY GLY G . n 
D 1 35  SER 35  34  34  SER SER G . n 
D 1 36  ILE 36  35  35  ILE ILE G . n 
D 1 37  LYS 37  36  36  LYS LYS G . n 
D 1 38  GLY 38  37  37  GLY GLY G . n 
D 1 39  LEU 39  38  38  LEU LEU G . n 
D 1 40  THR 40  39  39  THR THR G . n 
D 1 41  GLU 41  40  40  GLU GLU G . n 
D 1 42  GLY 42  41  41  GLY GLY G . n 
D 1 43  LEU 43  42  42  LEU LEU G . n 
D 1 44  HIS 44  43  43  HIS HIS G . n 
D 1 45  GLY 45  44  44  GLY GLY G . n 
D 1 46  PHE 46  45  45  PHE PHE G . n 
D 1 47  HIS 47  46  46  HIS HIS G . n 
D 1 48  VAL 48  47  47  VAL VAL G . n 
D 1 49  HIS 49  48  48  HIS HIS G . n 
D 1 50  GLU 50  49  49  GLU GLU G . n 
D 1 51  PHE 51  50  50  PHE PHE G . n 
D 1 52  GLY 52  51  51  GLY GLY G . n 
D 1 53  ASP 53  52  52  ASP ASP G . n 
D 1 54  ASN 54  53  53  ASN ASN G . n 
D 1 55  THR 55  54  54  THR THR G . n 
D 1 56  ALA 56  55  55  ALA ALA G . n 
D 1 57  GLY 57  56  56  GLY GLY G . n 
D 1 58  CYS 58  57  57  CYS CYS G . n 
D 1 59  THR 59  58  58  THR THR G . n 
D 1 60  SER 60  59  59  SER SER G . n 
D 1 61  ALA 61  60  60  ALA ALA G . n 
D 1 62  GLY 62  61  61  GLY GLY G . n 
D 1 63  PRO 63  62  62  PRO PRO G . n 
D 1 64  HIS 64  63  63  HIS HIS G . n 
D 1 65  PHE 65  64  64  PHE PHE G . n 
D 1 66  ASN 66  65  65  ASN ASN G . n 
D 1 67  PRO 67  66  66  PRO PRO G . n 
D 1 68  LEU 68  67  67  LEU LEU G . n 
D 1 69  SER 69  68  68  SER SER G . n 
D 1 70  ARG 70  69  69  ARG ARG G . n 
D 1 71  LYS 71  70  70  LYS LYS G . n 
D 1 72  HIS 72  71  71  HIS HIS G . n 
D 1 73  GLY 73  72  72  GLY GLY G . n 
D 1 74  GLY 74  73  73  GLY GLY G . n 
D 1 75  PRO 75  74  74  PRO PRO G . n 
D 1 76  LYS 76  75  75  LYS LYS G . n 
D 1 77  ASP 77  76  76  ASP ASP G . n 
D 1 78  GLU 78  77  77  GLU GLU G . n 
D 1 79  GLU 79  78  78  GLU GLU G . n 
D 1 80  ARG 80  79  79  ARG ARG G . n 
D 1 81  HIS 81  80  80  HIS HIS G . n 
D 1 82  VAL 82  81  81  VAL VAL G . n 
D 1 83  GLY 83  82  82  GLY GLY G . n 
D 1 84  ASP 84  83  83  ASP ASP G . n 
D 1 85  LEU 85  84  84  LEU LEU G . n 
D 1 86  GLY 86  85  85  GLY GLY G . n 
D 1 87  ASN 87  86  86  ASN ASN G . n 
D 1 88  VAL 88  87  87  VAL VAL G . n 
D 1 89  THR 89  88  88  THR THR G . n 
D 1 90  ALA 90  89  89  ALA ALA G . n 
D 1 91  ASP 91  90  90  ASP ASP G . n 
D 1 92  LYS 92  91  91  LYS LYS G . n 
D 1 93  ASP 93  92  92  ASP ASP G . n 
D 1 94  GLY 94  93  93  GLY GLY G . n 
D 1 95  VAL 95  94  94  VAL VAL G . n 
D 1 96  ALA 96  95  95  ALA ALA G . n 
D 1 97  ASP 97  96  96  ASP ASP G . n 
D 1 98  VAL 98  97  97  VAL VAL G . n 
D 1 99  SER 99  98  98  SER SER G . n 
D 1 100 ILE 100 99  99  ILE ILE G . n 
D 1 101 GLU 101 100 100 GLU GLU G . n 
D 1 102 ASP 102 101 101 ASP ASP G . n 
D 1 103 SER 103 102 102 SER SER G . n 
D 1 104 VAL 104 103 103 VAL VAL G . n 
D 1 105 ILE 105 104 104 ILE ILE G . n 
D 1 106 SER 106 105 105 SER SER G . n 
D 1 107 LEU 107 106 106 LEU LEU G . n 
D 1 108 SER 108 107 107 SER SER G . n 
D 1 109 GLY 109 108 108 GLY GLY G . n 
D 1 110 ASP 110 109 109 ASP ASP G . n 
D 1 111 HIS 111 110 110 HIS HIS G . n 
D 1 112 SER 112 111 111 SER SER G . n 
D 1 113 ILE 113 112 112 ILE ILE G . n 
D 1 114 ILE 114 113 113 ILE ILE G . n 
D 1 115 GLY 115 114 114 GLY GLY G . n 
D 1 116 ARG 116 115 115 ARG ARG G . n 
D 1 117 THR 117 116 116 THR THR G . n 
D 1 118 LEU 118 117 117 LEU LEU G . n 
D 1 119 VAL 119 118 118 VAL VAL G . n 
D 1 120 VAL 120 119 119 VAL VAL G . n 
D 1 121 HIS 121 120 120 HIS HIS G . n 
D 1 122 GLU 122 121 121 GLU GLU G . n 
D 1 123 LYS 123 122 122 LYS LYS G . n 
D 1 124 ALA 124 123 123 ALA ALA G . n 
D 1 125 ASP 125 124 124 ASP ASP G . n 
D 1 126 ASP 126 125 125 ASP ASP G . n 
D 1 127 LEU 127 126 126 LEU LEU G . n 
D 1 128 GLY 128 127 127 GLY GLY G . n 
D 1 129 LYS 129 128 128 LYS LYS G . n 
D 1 130 GLY 130 129 129 GLY GLY G . n 
D 1 131 GLY 131 130 130 GLY GLY G . n 
D 1 132 ASN 132 131 131 ASN ASN G . n 
D 1 133 GLU 133 132 132 GLU GLU G . n 
D 1 134 GLU 134 133 133 GLU GLU G . n 
D 1 135 SER 135 134 134 SER SER G . n 
D 1 136 THR 136 135 135 THR THR G . n 
D 1 137 LYS 137 136 136 LYS LYS G . n 
D 1 138 THR 138 137 137 THR THR G . n 
D 1 139 GLY 139 138 138 GLY GLY G . n 
D 1 140 ASN 140 139 139 ASN ASN G . n 
D 1 141 ALA 141 140 140 ALA ALA G . n 
D 1 142 GLY 142 141 141 GLY GLY G . n 
D 1 143 SER 143 142 142 SER SER G . n 
D 1 144 ARG 144 143 143 ARG ARG G . n 
D 1 145 LEU 145 144 144 LEU LEU G . n 
D 1 146 ALA 146 145 145 ALA ALA G . n 
D 1 147 CYS 147 146 146 CYS CYS G . n 
D 1 148 GLY 148 147 147 GLY GLY G . n 
D 1 149 VAL 149 148 148 VAL VAL G . n 
D 1 150 ILE 150 149 149 ILE ILE G . n 
D 1 151 GLY 151 150 150 GLY GLY G . n 
D 1 152 ILE 152 151 151 ILE ILE G . n 
D 1 153 ALA 153 152 152 ALA ALA G . n 
D 1 154 GLN 154 153 153 GLN GLN G . n 
E 1 1   ACE 1   0   0   ACE ACE C . n 
E 1 2   ALA 2   1   1   ALA ALA C . n 
E 1 3   THR 3   2   2   THR THR C . n 
E 1 4   LYS 4   3   3   LYS LYS C . n 
E 1 5   ALA 5   4   4   ALA ALA C . n 
E 1 6   VAL 6   5   5   VAL VAL C . n 
E 1 7   ALA 7   6   6   ALA ALA C . n 
E 1 8   VAL 8   7   7   VAL VAL C . n 
E 1 9   LEU 9   8   8   LEU LEU C . n 
E 1 10  LYS 10  9   9   LYS LYS C . n 
E 1 11  GLY 11  10  10  GLY GLY C . n 
E 1 12  ASP 12  11  11  ASP ASP C . n 
E 1 13  GLY 13  12  12  GLY GLY C . n 
E 1 14  PRO 14  13  13  PRO PRO C . n 
E 1 15  VAL 15  14  14  VAL VAL C . n 
E 1 16  GLN 16  15  15  GLN GLN C . n 
E 1 17  GLY 17  16  16  GLY GLY C . n 
E 1 18  ILE 18  17  17  ILE ILE C . n 
E 1 19  ILE 19  18  18  ILE ILE C . n 
E 1 20  ASN 20  19  19  ASN ASN C . n 
E 1 21  PHE 21  20  20  PHE PHE C . n 
E 1 22  GLU 22  21  21  GLU GLU C . n 
E 1 23  GLN 23  22  22  GLN GLN C . n 
E 1 24  LYS 24  23  23  LYS LYS C . n 
E 1 25  GLU 25  24  24  GLU GLU C . n 
E 1 26  SER 26  25  25  SER SER C . n 
E 1 27  ASN 27  26  26  ASN ASN C . n 
E 1 28  GLY 28  27  27  GLY GLY C . n 
E 1 29  PRO 29  28  28  PRO PRO C . n 
E 1 30  VAL 30  29  29  VAL VAL C . n 
E 1 31  LYS 31  30  30  LYS LYS C . n 
E 1 32  VAL 32  31  31  VAL VAL C . n 
E 1 33  TRP 33  32  32  TRP TRP C . n 
E 1 34  GLY 34  33  33  GLY GLY C . n 
E 1 35  SER 35  34  34  SER SER C . n 
E 1 36  ILE 36  35  35  ILE ILE C . n 
E 1 37  LYS 37  36  36  LYS LYS C . n 
E 1 38  GLY 38  37  37  GLY GLY C . n 
E 1 39  LEU 39  38  38  LEU LEU C . n 
E 1 40  THR 40  39  39  THR THR C . n 
E 1 41  GLU 41  40  40  GLU GLU C . n 
E 1 42  GLY 42  41  41  GLY GLY C . n 
E 1 43  LEU 43  42  42  LEU LEU C . n 
E 1 44  HIS 44  43  43  HIS HIS C . n 
E 1 45  GLY 45  44  44  GLY GLY C . n 
E 1 46  PHE 46  45  45  PHE PHE C . n 
E 1 47  HIS 47  46  46  HIS HIS C . n 
E 1 48  VAL 48  47  47  VAL VAL C . n 
E 1 49  HIS 49  48  48  HIS HIS C . n 
E 1 50  GLU 50  49  49  GLU GLU C . n 
E 1 51  PHE 51  50  50  PHE PHE C . n 
E 1 52  GLY 52  51  51  GLY GLY C . n 
E 1 53  ASP 53  52  52  ASP ASP C . n 
E 1 54  ASN 54  53  53  ASN ASN C . n 
E 1 55  THR 55  54  54  THR THR C . n 
E 1 56  ALA 56  55  55  ALA ALA C . n 
E 1 57  GLY 57  56  56  GLY GLY C . n 
E 1 58  CYS 58  57  57  CYS CYS C . n 
E 1 59  THR 59  58  58  THR THR C . n 
E 1 60  SER 60  59  59  SER SER C . n 
E 1 61  ALA 61  60  60  ALA ALA C . n 
E 1 62  GLY 62  61  61  GLY GLY C . n 
E 1 63  PRO 63  62  62  PRO PRO C . n 
E 1 64  HIS 64  63  63  HIS HIS C . n 
E 1 65  PHE 65  64  64  PHE PHE C . n 
E 1 66  ASN 66  65  65  ASN ASN C . n 
E 1 67  PRO 67  66  66  PRO PRO C . n 
E 1 68  LEU 68  67  67  LEU LEU C . n 
E 1 69  SER 69  68  68  SER SER C . n 
E 1 70  ARG 70  69  69  ARG ARG C . n 
E 1 71  LYS 71  70  70  LYS LYS C . n 
E 1 72  HIS 72  71  71  HIS HIS C . n 
E 1 73  GLY 73  72  72  GLY GLY C . n 
E 1 74  GLY 74  73  73  GLY GLY C . n 
E 1 75  PRO 75  74  74  PRO PRO C . n 
E 1 76  LYS 76  75  75  LYS LYS C . n 
E 1 77  ASP 77  76  76  ASP ASP C . n 
E 1 78  GLU 78  77  77  GLU GLU C . n 
E 1 79  GLU 79  78  78  GLU GLU C . n 
E 1 80  ARG 80  79  79  ARG ARG C . n 
E 1 81  HIS 81  80  80  HIS HIS C . n 
E 1 82  VAL 82  81  81  VAL VAL C . n 
E 1 83  GLY 83  82  82  GLY GLY C . n 
E 1 84  ASP 84  83  83  ASP ASP C . n 
E 1 85  LEU 85  84  84  LEU LEU C . n 
E 1 86  GLY 86  85  85  GLY GLY C . n 
E 1 87  ASN 87  86  86  ASN ASN C . n 
E 1 88  VAL 88  87  87  VAL VAL C . n 
E 1 89  THR 89  88  88  THR THR C . n 
E 1 90  ALA 90  89  89  ALA ALA C . n 
E 1 91  ASP 91  90  90  ASP ASP C . n 
E 1 92  LYS 92  91  91  LYS LYS C . n 
E 1 93  ASP 93  92  92  ASP ASP C . n 
E 1 94  GLY 94  93  93  GLY GLY C . n 
E 1 95  VAL 95  94  94  VAL VAL C . n 
E 1 96  ALA 96  95  95  ALA ALA C . n 
E 1 97  ASP 97  96  96  ASP ASP C . n 
E 1 98  VAL 98  97  97  VAL VAL C . n 
E 1 99  SER 99  98  98  SER SER C . n 
E 1 100 ILE 100 99  99  ILE ILE C . n 
E 1 101 GLU 101 100 100 GLU GLU C . n 
E 1 102 ASP 102 101 101 ASP ASP C . n 
E 1 103 SER 103 102 102 SER SER C . n 
E 1 104 VAL 104 103 103 VAL VAL C . n 
E 1 105 ILE 105 104 104 ILE ILE C . n 
E 1 106 SER 106 105 105 SER SER C . n 
E 1 107 LEU 107 106 106 LEU LEU C . n 
E 1 108 SER 108 107 107 SER SER C . n 
E 1 109 GLY 109 108 108 GLY GLY C . n 
E 1 110 ASP 110 109 109 ASP ASP C . n 
E 1 111 HIS 111 110 110 HIS HIS C . n 
E 1 112 SER 112 111 111 SER SER C . n 
E 1 113 ILE 113 112 112 ILE ILE C . n 
E 1 114 ILE 114 113 113 ILE ILE C . n 
E 1 115 GLY 115 114 114 GLY GLY C . n 
E 1 116 ARG 116 115 115 ARG ARG C . n 
E 1 117 THR 117 116 116 THR THR C . n 
E 1 118 LEU 118 117 117 LEU LEU C . n 
E 1 119 VAL 119 118 118 VAL VAL C . n 
E 1 120 VAL 120 119 119 VAL VAL C . n 
E 1 121 HIS 121 120 120 HIS HIS C . n 
E 1 122 GLU 122 121 121 GLU GLU C . n 
E 1 123 LYS 123 122 122 LYS LYS C . n 
E 1 124 ALA 124 123 123 ALA ALA C . n 
E 1 125 ASP 125 124 124 ASP ASP C . n 
E 1 126 ASP 126 125 125 ASP ASP C . n 
E 1 127 LEU 127 126 126 LEU LEU C . n 
E 1 128 GLY 128 127 127 GLY GLY C . n 
E 1 129 LYS 129 128 128 LYS LYS C . n 
E 1 130 GLY 130 129 129 GLY GLY C . n 
E 1 131 GLY 131 130 130 GLY GLY C . n 
E 1 132 ASN 132 131 131 ASN ASN C . n 
E 1 133 GLU 133 132 132 GLU GLU C . n 
E 1 134 GLU 134 133 133 GLU GLU C . n 
E 1 135 SER 135 134 134 SER SER C . n 
E 1 136 THR 136 135 135 THR THR C . n 
E 1 137 LYS 137 136 136 LYS LYS C . n 
E 1 138 THR 138 137 137 THR THR C . n 
E 1 139 GLY 139 138 138 GLY GLY C . n 
E 1 140 ASN 140 139 139 ASN ASN C . n 
E 1 141 ALA 141 140 140 ALA ALA C . n 
E 1 142 GLY 142 141 141 GLY GLY C . n 
E 1 143 SER 143 142 142 SER SER C . n 
E 1 144 ARG 144 143 143 ARG ARG C . n 
E 1 145 LEU 145 144 144 LEU LEU C . n 
E 1 146 ALA 146 145 145 ALA ALA C . n 
E 1 147 CYS 147 146 146 CYS CYS C . n 
E 1 148 GLY 148 147 147 GLY GLY C . n 
E 1 149 VAL 149 148 148 VAL VAL C . n 
E 1 150 ILE 150 149 149 ILE ILE C . n 
E 1 151 GLY 151 150 150 GLY GLY C . n 
E 1 152 ILE 152 151 151 ILE ILE C . n 
E 1 153 ALA 153 152 152 ALA ALA C . n 
E 1 154 GLN 154 153 153 GLN GLN C . n 
F 1 1   ACE 1   0   0   ACE ACE H . n 
F 1 2   ALA 2   1   1   ALA ALA H . n 
F 1 3   THR 3   2   2   THR THR H . n 
F 1 4   LYS 4   3   3   LYS LYS H . n 
F 1 5   ALA 5   4   4   ALA ALA H . n 
F 1 6   VAL 6   5   5   VAL VAL H . n 
F 1 7   ALA 7   6   6   ALA ALA H . n 
F 1 8   VAL 8   7   7   VAL VAL H . n 
F 1 9   LEU 9   8   8   LEU LEU H . n 
F 1 10  LYS 10  9   9   LYS LYS H . n 
F 1 11  GLY 11  10  10  GLY GLY H . n 
F 1 12  ASP 12  11  11  ASP ASP H . n 
F 1 13  GLY 13  12  12  GLY GLY H . n 
F 1 14  PRO 14  13  13  PRO PRO H . n 
F 1 15  VAL 15  14  14  VAL VAL H . n 
F 1 16  GLN 16  15  15  GLN GLN H . n 
F 1 17  GLY 17  16  16  GLY GLY H . n 
F 1 18  ILE 18  17  17  ILE ILE H . n 
F 1 19  ILE 19  18  18  ILE ILE H . n 
F 1 20  ASN 20  19  19  ASN ASN H . n 
F 1 21  PHE 21  20  20  PHE PHE H . n 
F 1 22  GLU 22  21  21  GLU GLU H . n 
F 1 23  GLN 23  22  22  GLN GLN H . n 
F 1 24  LYS 24  23  23  LYS LYS H . n 
F 1 25  GLU 25  24  24  GLU GLU H . n 
F 1 26  SER 26  25  25  SER SER H . n 
F 1 27  ASN 27  26  26  ASN ASN H . n 
F 1 28  GLY 28  27  27  GLY GLY H . n 
F 1 29  PRO 29  28  28  PRO PRO H . n 
F 1 30  VAL 30  29  29  VAL VAL H . n 
F 1 31  LYS 31  30  30  LYS LYS H . n 
F 1 32  VAL 32  31  31  VAL VAL H . n 
F 1 33  TRP 33  32  32  TRP TRP H . n 
F 1 34  GLY 34  33  33  GLY GLY H . n 
F 1 35  SER 35  34  34  SER SER H . n 
F 1 36  ILE 36  35  35  ILE ILE H . n 
F 1 37  LYS 37  36  36  LYS LYS H . n 
F 1 38  GLY 38  37  37  GLY GLY H . n 
F 1 39  LEU 39  38  38  LEU LEU H . n 
F 1 40  THR 40  39  39  THR THR H . n 
F 1 41  GLU 41  40  40  GLU GLU H . n 
F 1 42  GLY 42  41  41  GLY GLY H . n 
F 1 43  LEU 43  42  42  LEU LEU H . n 
F 1 44  HIS 44  43  43  HIS HIS H . n 
F 1 45  GLY 45  44  44  GLY GLY H . n 
F 1 46  PHE 46  45  45  PHE PHE H . n 
F 1 47  HIS 47  46  46  HIS HIS H . n 
F 1 48  VAL 48  47  47  VAL VAL H . n 
F 1 49  HIS 49  48  48  HIS HIS H . n 
F 1 50  GLU 50  49  49  GLU GLU H . n 
F 1 51  PHE 51  50  50  PHE PHE H . n 
F 1 52  GLY 52  51  51  GLY GLY H . n 
F 1 53  ASP 53  52  52  ASP ASP H . n 
F 1 54  ASN 54  53  53  ASN ASN H . n 
F 1 55  THR 55  54  54  THR THR H . n 
F 1 56  ALA 56  55  55  ALA ALA H . n 
F 1 57  GLY 57  56  56  GLY GLY H . n 
F 1 58  CYS 58  57  57  CYS CYS H . n 
F 1 59  THR 59  58  58  THR THR H . n 
F 1 60  SER 60  59  59  SER SER H . n 
F 1 61  ALA 61  60  60  ALA ALA H . n 
F 1 62  GLY 62  61  61  GLY GLY H . n 
F 1 63  PRO 63  62  62  PRO PRO H . n 
F 1 64  HIS 64  63  63  HIS HIS H . n 
F 1 65  PHE 65  64  64  PHE PHE H . n 
F 1 66  ASN 66  65  65  ASN ASN H . n 
F 1 67  PRO 67  66  66  PRO PRO H . n 
F 1 68  LEU 68  67  67  LEU LEU H . n 
F 1 69  SER 69  68  68  SER SER H . n 
F 1 70  ARG 70  69  69  ARG ARG H . n 
F 1 71  LYS 71  70  70  LYS LYS H . n 
F 1 72  HIS 72  71  71  HIS HIS H . n 
F 1 73  GLY 73  72  72  GLY GLY H . n 
F 1 74  GLY 74  73  73  GLY GLY H . n 
F 1 75  PRO 75  74  74  PRO PRO H . n 
F 1 76  LYS 76  75  75  LYS LYS H . n 
F 1 77  ASP 77  76  76  ASP ASP H . n 
F 1 78  GLU 78  77  77  GLU GLU H . n 
F 1 79  GLU 79  78  78  GLU GLU H . n 
F 1 80  ARG 80  79  79  ARG ARG H . n 
F 1 81  HIS 81  80  80  HIS HIS H . n 
F 1 82  VAL 82  81  81  VAL VAL H . n 
F 1 83  GLY 83  82  82  GLY GLY H . n 
F 1 84  ASP 84  83  83  ASP ASP H . n 
F 1 85  LEU 85  84  84  LEU LEU H . n 
F 1 86  GLY 86  85  85  GLY GLY H . n 
F 1 87  ASN 87  86  86  ASN ASN H . n 
F 1 88  VAL 88  87  87  VAL VAL H . n 
F 1 89  THR 89  88  88  THR THR H . n 
F 1 90  ALA 90  89  89  ALA ALA H . n 
F 1 91  ASP 91  90  90  ASP ASP H . n 
F 1 92  LYS 92  91  91  LYS LYS H . n 
F 1 93  ASP 93  92  92  ASP ASP H . n 
F 1 94  GLY 94  93  93  GLY GLY H . n 
F 1 95  VAL 95  94  94  VAL VAL H . n 
F 1 96  ALA 96  95  95  ALA ALA H . n 
F 1 97  ASP 97  96  96  ASP ASP H . n 
F 1 98  VAL 98  97  97  VAL VAL H . n 
F 1 99  SER 99  98  98  SER SER H . n 
F 1 100 ILE 100 99  99  ILE ILE H . n 
F 1 101 GLU 101 100 100 GLU GLU H . n 
F 1 102 ASP 102 101 101 ASP ASP H . n 
F 1 103 SER 103 102 102 SER SER H . n 
F 1 104 VAL 104 103 103 VAL VAL H . n 
F 1 105 ILE 105 104 104 ILE ILE H . n 
F 1 106 SER 106 105 105 SER SER H . n 
F 1 107 LEU 107 106 106 LEU LEU H . n 
F 1 108 SER 108 107 107 SER SER H . n 
F 1 109 GLY 109 108 108 GLY GLY H . n 
F 1 110 ASP 110 109 109 ASP ASP H . n 
F 1 111 HIS 111 110 110 HIS HIS H . n 
F 1 112 SER 112 111 111 SER SER H . n 
F 1 113 ILE 113 112 112 ILE ILE H . n 
F 1 114 ILE 114 113 113 ILE ILE H . n 
F 1 115 GLY 115 114 114 GLY GLY H . n 
F 1 116 ARG 116 115 115 ARG ARG H . n 
F 1 117 THR 117 116 116 THR THR H . n 
F 1 118 LEU 118 117 117 LEU LEU H . n 
F 1 119 VAL 119 118 118 VAL VAL H . n 
F 1 120 VAL 120 119 119 VAL VAL H . n 
F 1 121 HIS 121 120 120 HIS HIS H . n 
F 1 122 GLU 122 121 121 GLU GLU H . n 
F 1 123 LYS 123 122 122 LYS LYS H . n 
F 1 124 ALA 124 123 123 ALA ALA H . n 
F 1 125 ASP 125 124 124 ASP ASP H . n 
F 1 126 ASP 126 125 125 ASP ASP H . n 
F 1 127 LEU 127 126 126 LEU LEU H . n 
F 1 128 GLY 128 127 127 GLY GLY H . n 
F 1 129 LYS 129 128 128 LYS LYS H . n 
F 1 130 GLY 130 129 129 GLY GLY H . n 
F 1 131 GLY 131 130 130 GLY GLY H . n 
F 1 132 ASN 132 131 131 ASN ASN H . n 
F 1 133 GLU 133 132 132 GLU GLU H . n 
F 1 134 GLU 134 133 133 GLU GLU H . n 
F 1 135 SER 135 134 134 SER SER H . n 
F 1 136 THR 136 135 135 THR THR H . n 
F 1 137 LYS 137 136 136 LYS LYS H . n 
F 1 138 THR 138 137 137 THR THR H . n 
F 1 139 GLY 139 138 138 GLY GLY H . n 
F 1 140 ASN 140 139 139 ASN ASN H . n 
F 1 141 ALA 141 140 140 ALA ALA H . n 
F 1 142 GLY 142 141 141 GLY GLY H . n 
F 1 143 SER 143 142 142 SER SER H . n 
F 1 144 ARG 144 143 143 ARG ARG H . n 
F 1 145 LEU 145 144 144 LEU LEU H . n 
F 1 146 ALA 146 145 145 ALA ALA H . n 
F 1 147 CYS 147 146 146 CYS CYS H . n 
F 1 148 GLY 148 147 147 GLY GLY H . n 
F 1 149 VAL 149 148 148 VAL VAL H . n 
F 1 150 ILE 150 149 149 ILE ILE H . n 
F 1 151 GLY 151 150 150 GLY GLY H . n 
F 1 152 ILE 152 151 151 ILE ILE H . n 
F 1 153 ALA 153 152 152 ALA ALA H . n 
F 1 154 GLN 154 153 153 GLN GLN H . n 
G 1 1   ACE 1   0   0   ACE ACE D . n 
G 1 2   ALA 2   1   1   ALA ALA D . n 
G 1 3   THR 3   2   2   THR THR D . n 
G 1 4   LYS 4   3   3   LYS LYS D . n 
G 1 5   ALA 5   4   4   ALA ALA D . n 
G 1 6   VAL 6   5   5   VAL VAL D . n 
G 1 7   ALA 7   6   6   ALA ALA D . n 
G 1 8   VAL 8   7   7   VAL VAL D . n 
G 1 9   LEU 9   8   8   LEU LEU D . n 
G 1 10  LYS 10  9   9   LYS LYS D . n 
G 1 11  GLY 11  10  10  GLY GLY D . n 
G 1 12  ASP 12  11  11  ASP ASP D . n 
G 1 13  GLY 13  12  12  GLY GLY D . n 
G 1 14  PRO 14  13  13  PRO PRO D . n 
G 1 15  VAL 15  14  14  VAL VAL D . n 
G 1 16  GLN 16  15  15  GLN GLN D . n 
G 1 17  GLY 17  16  16  GLY GLY D . n 
G 1 18  ILE 18  17  17  ILE ILE D . n 
G 1 19  ILE 19  18  18  ILE ILE D . n 
G 1 20  ASN 20  19  19  ASN ASN D . n 
G 1 21  PHE 21  20  20  PHE PHE D . n 
G 1 22  GLU 22  21  21  GLU GLU D . n 
G 1 23  GLN 23  22  22  GLN GLN D . n 
G 1 24  LYS 24  23  23  LYS LYS D . n 
G 1 25  GLU 25  24  24  GLU GLU D . n 
G 1 26  SER 26  25  25  SER SER D . n 
G 1 27  ASN 27  26  26  ASN ASN D . n 
G 1 28  GLY 28  27  27  GLY GLY D . n 
G 1 29  PRO 29  28  28  PRO PRO D . n 
G 1 30  VAL 30  29  29  VAL VAL D . n 
G 1 31  LYS 31  30  30  LYS LYS D . n 
G 1 32  VAL 32  31  31  VAL VAL D . n 
G 1 33  TRP 33  32  32  TRP TRP D . n 
G 1 34  GLY 34  33  33  GLY GLY D . n 
G 1 35  SER 35  34  34  SER SER D . n 
G 1 36  ILE 36  35  35  ILE ILE D . n 
G 1 37  LYS 37  36  36  LYS LYS D . n 
G 1 38  GLY 38  37  37  GLY GLY D . n 
G 1 39  LEU 39  38  38  LEU LEU D . n 
G 1 40  THR 40  39  39  THR THR D . n 
G 1 41  GLU 41  40  40  GLU GLU D . n 
G 1 42  GLY 42  41  41  GLY GLY D . n 
G 1 43  LEU 43  42  42  LEU LEU D . n 
G 1 44  HIS 44  43  43  HIS HIS D . n 
G 1 45  GLY 45  44  44  GLY GLY D . n 
G 1 46  PHE 46  45  45  PHE PHE D . n 
G 1 47  HIS 47  46  46  HIS HIS D . n 
G 1 48  VAL 48  47  47  VAL VAL D . n 
G 1 49  HIS 49  48  48  HIS HIS D . n 
G 1 50  GLU 50  49  49  GLU GLU D . n 
G 1 51  PHE 51  50  50  PHE PHE D . n 
G 1 52  GLY 52  51  51  GLY GLY D . n 
G 1 53  ASP 53  52  52  ASP ASP D . n 
G 1 54  ASN 54  53  53  ASN ASN D . n 
G 1 55  THR 55  54  54  THR THR D . n 
G 1 56  ALA 56  55  55  ALA ALA D . n 
G 1 57  GLY 57  56  56  GLY GLY D . n 
G 1 58  CYS 58  57  57  CYS CYS D . n 
G 1 59  THR 59  58  58  THR THR D . n 
G 1 60  SER 60  59  59  SER SER D . n 
G 1 61  ALA 61  60  60  ALA ALA D . n 
G 1 62  GLY 62  61  61  GLY GLY D . n 
G 1 63  PRO 63  62  62  PRO PRO D . n 
G 1 64  HIS 64  63  63  HIS HIS D . n 
G 1 65  PHE 65  64  64  PHE PHE D . n 
G 1 66  ASN 66  65  65  ASN ASN D . n 
G 1 67  PRO 67  66  66  PRO PRO D . n 
G 1 68  LEU 68  67  67  LEU LEU D . n 
G 1 69  SER 69  68  68  SER SER D . n 
G 1 70  ARG 70  69  69  ARG ARG D . n 
G 1 71  LYS 71  70  70  LYS LYS D . n 
G 1 72  HIS 72  71  71  HIS HIS D . n 
G 1 73  GLY 73  72  72  GLY GLY D . n 
G 1 74  GLY 74  73  73  GLY GLY D . n 
G 1 75  PRO 75  74  74  PRO PRO D . n 
G 1 76  LYS 76  75  75  LYS LYS D . n 
G 1 77  ASP 77  76  76  ASP ASP D . n 
G 1 78  GLU 78  77  77  GLU GLU D . n 
G 1 79  GLU 79  78  78  GLU GLU D . n 
G 1 80  ARG 80  79  79  ARG ARG D . n 
G 1 81  HIS 81  80  80  HIS HIS D . n 
G 1 82  VAL 82  81  81  VAL VAL D . n 
G 1 83  GLY 83  82  82  GLY GLY D . n 
G 1 84  ASP 84  83  83  ASP ASP D . n 
G 1 85  LEU 85  84  84  LEU LEU D . n 
G 1 86  GLY 86  85  85  GLY GLY D . n 
G 1 87  ASN 87  86  86  ASN ASN D . n 
G 1 88  VAL 88  87  87  VAL VAL D . n 
G 1 89  THR 89  88  88  THR THR D . n 
G 1 90  ALA 90  89  89  ALA ALA D . n 
G 1 91  ASP 91  90  90  ASP ASP D . n 
G 1 92  LYS 92  91  91  LYS LYS D . n 
G 1 93  ASP 93  92  92  ASP ASP D . n 
G 1 94  GLY 94  93  93  GLY GLY D . n 
G 1 95  VAL 95  94  94  VAL VAL D . n 
G 1 96  ALA 96  95  95  ALA ALA D . n 
G 1 97  ASP 97  96  96  ASP ASP D . n 
G 1 98  VAL 98  97  97  VAL VAL D . n 
G 1 99  SER 99  98  98  SER SER D . n 
G 1 100 ILE 100 99  99  ILE ILE D . n 
G 1 101 GLU 101 100 100 GLU GLU D . n 
G 1 102 ASP 102 101 101 ASP ASP D . n 
G 1 103 SER 103 102 102 SER SER D . n 
G 1 104 VAL 104 103 103 VAL VAL D . n 
G 1 105 ILE 105 104 104 ILE ILE D . n 
G 1 106 SER 106 105 105 SER SER D . n 
G 1 107 LEU 107 106 106 LEU LEU D . n 
G 1 108 SER 108 107 107 SER SER D . n 
G 1 109 GLY 109 108 108 GLY GLY D . n 
G 1 110 ASP 110 109 109 ASP ASP D . n 
G 1 111 HIS 111 110 110 HIS HIS D . n 
G 1 112 SER 112 111 111 SER SER D . n 
G 1 113 ILE 113 112 112 ILE ILE D . n 
G 1 114 ILE 114 113 113 ILE ILE D . n 
G 1 115 GLY 115 114 114 GLY GLY D . n 
G 1 116 ARG 116 115 115 ARG ARG D . n 
G 1 117 THR 117 116 116 THR THR D . n 
G 1 118 LEU 118 117 117 LEU LEU D . n 
G 1 119 VAL 119 118 118 VAL VAL D . n 
G 1 120 VAL 120 119 119 VAL VAL D . n 
G 1 121 HIS 121 120 120 HIS HIS D . n 
G 1 122 GLU 122 121 121 GLU GLU D . n 
G 1 123 LYS 123 122 122 LYS LYS D . n 
G 1 124 ALA 124 123 123 ALA ALA D . n 
G 1 125 ASP 125 124 124 ASP ASP D . n 
G 1 126 ASP 126 125 125 ASP ASP D . n 
G 1 127 LEU 127 126 126 LEU LEU D . n 
G 1 128 GLY 128 127 127 GLY GLY D . n 
G 1 129 LYS 129 128 128 LYS LYS D . n 
G 1 130 GLY 130 129 129 GLY GLY D . n 
G 1 131 GLY 131 130 130 GLY GLY D . n 
G 1 132 ASN 132 131 131 ASN ASN D . n 
G 1 133 GLU 133 132 132 GLU GLU D . n 
G 1 134 GLU 134 133 133 GLU GLU D . n 
G 1 135 SER 135 134 134 SER SER D . n 
G 1 136 THR 136 135 135 THR THR D . n 
G 1 137 LYS 137 136 136 LYS LYS D . n 
G 1 138 THR 138 137 137 THR THR D . n 
G 1 139 GLY 139 138 138 GLY GLY D . n 
G 1 140 ASN 140 139 139 ASN ASN D . n 
G 1 141 ALA 141 140 140 ALA ALA D . n 
G 1 142 GLY 142 141 141 GLY GLY D . n 
G 1 143 SER 143 142 142 SER SER D . n 
G 1 144 ARG 144 143 143 ARG ARG D . n 
G 1 145 LEU 145 144 144 LEU LEU D . n 
G 1 146 ALA 146 145 145 ALA ALA D . n 
G 1 147 CYS 147 146 146 CYS CYS D . n 
G 1 148 GLY 148 147 147 GLY GLY D . n 
G 1 149 VAL 149 148 148 VAL VAL D . n 
G 1 150 ILE 150 149 149 ILE ILE D . n 
G 1 151 GLY 151 150 150 GLY GLY D . n 
G 1 152 ILE 152 151 151 ILE ILE D . n 
G 1 153 ALA 153 152 152 ALA ALA D . n 
G 1 154 GLN 154 153 153 GLN GLN D . n 
H 1 1   ACE 1   0   0   ACE ACE I . n 
H 1 2   ALA 2   1   1   ALA ALA I . n 
H 1 3   THR 3   2   2   THR THR I . n 
H 1 4   LYS 4   3   3   LYS LYS I . n 
H 1 5   ALA 5   4   4   ALA ALA I . n 
H 1 6   VAL 6   5   5   VAL VAL I . n 
H 1 7   ALA 7   6   6   ALA ALA I . n 
H 1 8   VAL 8   7   7   VAL VAL I . n 
H 1 9   LEU 9   8   8   LEU LEU I . n 
H 1 10  LYS 10  9   9   LYS LYS I . n 
H 1 11  GLY 11  10  10  GLY GLY I . n 
H 1 12  ASP 12  11  11  ASP ASP I . n 
H 1 13  GLY 13  12  12  GLY GLY I . n 
H 1 14  PRO 14  13  13  PRO PRO I . n 
H 1 15  VAL 15  14  14  VAL VAL I . n 
H 1 16  GLN 16  15  15  GLN GLN I . n 
H 1 17  GLY 17  16  16  GLY GLY I . n 
H 1 18  ILE 18  17  17  ILE ILE I . n 
H 1 19  ILE 19  18  18  ILE ILE I . n 
H 1 20  ASN 20  19  19  ASN ASN I . n 
H 1 21  PHE 21  20  20  PHE PHE I . n 
H 1 22  GLU 22  21  21  GLU GLU I . n 
H 1 23  GLN 23  22  22  GLN GLN I . n 
H 1 24  LYS 24  23  23  LYS LYS I . n 
H 1 25  GLU 25  24  24  GLU GLU I . n 
H 1 26  SER 26  25  25  SER SER I . n 
H 1 27  ASN 27  26  26  ASN ASN I . n 
H 1 28  GLY 28  27  27  GLY GLY I . n 
H 1 29  PRO 29  28  28  PRO PRO I . n 
H 1 30  VAL 30  29  29  VAL VAL I . n 
H 1 31  LYS 31  30  30  LYS LYS I . n 
H 1 32  VAL 32  31  31  VAL VAL I . n 
H 1 33  TRP 33  32  32  TRP TRP I . n 
H 1 34  GLY 34  33  33  GLY GLY I . n 
H 1 35  SER 35  34  34  SER SER I . n 
H 1 36  ILE 36  35  35  ILE ILE I . n 
H 1 37  LYS 37  36  36  LYS LYS I . n 
H 1 38  GLY 38  37  37  GLY GLY I . n 
H 1 39  LEU 39  38  38  LEU LEU I . n 
H 1 40  THR 40  39  39  THR THR I . n 
H 1 41  GLU 41  40  40  GLU GLU I . n 
H 1 42  GLY 42  41  41  GLY GLY I . n 
H 1 43  LEU 43  42  42  LEU LEU I . n 
H 1 44  HIS 44  43  43  HIS HIS I . n 
H 1 45  GLY 45  44  44  GLY GLY I . n 
H 1 46  PHE 46  45  45  PHE PHE I . n 
H 1 47  HIS 47  46  46  HIS HIS I . n 
H 1 48  VAL 48  47  47  VAL VAL I . n 
H 1 49  HIS 49  48  48  HIS HIS I . n 
H 1 50  GLU 50  49  49  GLU GLU I . n 
H 1 51  PHE 51  50  50  PHE PHE I . n 
H 1 52  GLY 52  51  51  GLY GLY I . n 
H 1 53  ASP 53  52  52  ASP ASP I . n 
H 1 54  ASN 54  53  53  ASN ASN I . n 
H 1 55  THR 55  54  54  THR THR I . n 
H 1 56  ALA 56  55  55  ALA ALA I . n 
H 1 57  GLY 57  56  56  GLY GLY I . n 
H 1 58  CYS 58  57  57  CYS CYS I . n 
H 1 59  THR 59  58  58  THR THR I . n 
H 1 60  SER 60  59  59  SER SER I . n 
H 1 61  ALA 61  60  60  ALA ALA I . n 
H 1 62  GLY 62  61  61  GLY GLY I . n 
H 1 63  PRO 63  62  62  PRO PRO I . n 
H 1 64  HIS 64  63  63  HIS HIS I . n 
H 1 65  PHE 65  64  64  PHE PHE I . n 
H 1 66  ASN 66  65  65  ASN ASN I . n 
H 1 67  PRO 67  66  66  PRO PRO I . n 
H 1 68  LEU 68  67  67  LEU LEU I . n 
H 1 69  SER 69  68  68  SER SER I . n 
H 1 70  ARG 70  69  69  ARG ARG I . n 
H 1 71  LYS 71  70  70  LYS LYS I . n 
H 1 72  HIS 72  71  71  HIS HIS I . n 
H 1 73  GLY 73  72  72  GLY GLY I . n 
H 1 74  GLY 74  73  73  GLY GLY I . n 
H 1 75  PRO 75  74  74  PRO PRO I . n 
H 1 76  LYS 76  75  75  LYS LYS I . n 
H 1 77  ASP 77  76  76  ASP ASP I . n 
H 1 78  GLU 78  77  77  GLU GLU I . n 
H 1 79  GLU 79  78  78  GLU GLU I . n 
H 1 80  ARG 80  79  79  ARG ARG I . n 
H 1 81  HIS 81  80  80  HIS HIS I . n 
H 1 82  VAL 82  81  81  VAL VAL I . n 
H 1 83  GLY 83  82  82  GLY GLY I . n 
H 1 84  ASP 84  83  83  ASP ASP I . n 
H 1 85  LEU 85  84  84  LEU LEU I . n 
H 1 86  GLY 86  85  85  GLY GLY I . n 
H 1 87  ASN 87  86  86  ASN ASN I . n 
H 1 88  VAL 88  87  87  VAL VAL I . n 
H 1 89  THR 89  88  88  THR THR I . n 
H 1 90  ALA 90  89  89  ALA ALA I . n 
H 1 91  ASP 91  90  90  ASP ASP I . n 
H 1 92  LYS 92  91  91  LYS LYS I . n 
H 1 93  ASP 93  92  92  ASP ASP I . n 
H 1 94  GLY 94  93  93  GLY GLY I . n 
H 1 95  VAL 95  94  94  VAL VAL I . n 
H 1 96  ALA 96  95  95  ALA ALA I . n 
H 1 97  ASP 97  96  96  ASP ASP I . n 
H 1 98  VAL 98  97  97  VAL VAL I . n 
H 1 99  SER 99  98  98  SER SER I . n 
H 1 100 ILE 100 99  99  ILE ILE I . n 
H 1 101 GLU 101 100 100 GLU GLU I . n 
H 1 102 ASP 102 101 101 ASP ASP I . n 
H 1 103 SER 103 102 102 SER SER I . n 
H 1 104 VAL 104 103 103 VAL VAL I . n 
H 1 105 ILE 105 104 104 ILE ILE I . n 
H 1 106 SER 106 105 105 SER SER I . n 
H 1 107 LEU 107 106 106 LEU LEU I . n 
H 1 108 SER 108 107 107 SER SER I . n 
H 1 109 GLY 109 108 108 GLY GLY I . n 
H 1 110 ASP 110 109 109 ASP ASP I . n 
H 1 111 HIS 111 110 110 HIS HIS I . n 
H 1 112 SER 112 111 111 SER SER I . n 
H 1 113 ILE 113 112 112 ILE ILE I . n 
H 1 114 ILE 114 113 113 ILE ILE I . n 
H 1 115 GLY 115 114 114 GLY GLY I . n 
H 1 116 ARG 116 115 115 ARG ARG I . n 
H 1 117 THR 117 116 116 THR THR I . n 
H 1 118 LEU 118 117 117 LEU LEU I . n 
H 1 119 VAL 119 118 118 VAL VAL I . n 
H 1 120 VAL 120 119 119 VAL VAL I . n 
H 1 121 HIS 121 120 120 HIS HIS I . n 
H 1 122 GLU 122 121 121 GLU GLU I . n 
H 1 123 LYS 123 122 122 LYS LYS I . n 
H 1 124 ALA 124 123 123 ALA ALA I . n 
H 1 125 ASP 125 124 124 ASP ASP I . n 
H 1 126 ASP 126 125 125 ASP ASP I . n 
H 1 127 LEU 127 126 126 LEU LEU I . n 
H 1 128 GLY 128 127 127 GLY GLY I . n 
H 1 129 LYS 129 128 128 LYS LYS I . n 
H 1 130 GLY 130 129 129 GLY GLY I . n 
H 1 131 GLY 131 130 130 GLY GLY I . n 
H 1 132 ASN 132 131 131 ASN ASN I . n 
H 1 133 GLU 133 132 132 GLU GLU I . n 
H 1 134 GLU 134 133 133 GLU GLU I . n 
H 1 135 SER 135 134 134 SER SER I . n 
H 1 136 THR 136 135 135 THR THR I . n 
H 1 137 LYS 137 136 136 LYS LYS I . n 
H 1 138 THR 138 137 137 THR THR I . n 
H 1 139 GLY 139 138 138 GLY GLY I . n 
H 1 140 ASN 140 139 139 ASN ASN I . n 
H 1 141 ALA 141 140 140 ALA ALA I . n 
H 1 142 GLY 142 141 141 GLY GLY I . n 
H 1 143 SER 143 142 142 SER SER I . n 
H 1 144 ARG 144 143 143 ARG ARG I . n 
H 1 145 LEU 145 144 144 LEU LEU I . n 
H 1 146 ALA 146 145 145 ALA ALA I . n 
H 1 147 CYS 147 146 146 CYS CYS I . n 
H 1 148 GLY 148 147 147 GLY GLY I . n 
H 1 149 VAL 149 148 148 VAL VAL I . n 
H 1 150 ILE 150 149 149 ILE ILE I . n 
H 1 151 GLY 151 150 150 GLY GLY I . n 
H 1 152 ILE 152 151 151 ILE ILE I . n 
H 1 153 ALA 153 152 152 ALA ALA I . n 
H 1 154 GLN 154 153 153 GLN GLN I . n 
I 1 1   ACE 1   0   0   ACE ACE E . n 
I 1 2   ALA 2   1   1   ALA ALA E . n 
I 1 3   THR 3   2   2   THR THR E . n 
I 1 4   LYS 4   3   3   LYS LYS E . n 
I 1 5   ALA 5   4   4   ALA ALA E . n 
I 1 6   VAL 6   5   5   VAL VAL E . n 
I 1 7   ALA 7   6   6   ALA ALA E . n 
I 1 8   VAL 8   7   7   VAL VAL E . n 
I 1 9   LEU 9   8   8   LEU LEU E . n 
I 1 10  LYS 10  9   9   LYS LYS E . n 
I 1 11  GLY 11  10  10  GLY GLY E . n 
I 1 12  ASP 12  11  11  ASP ASP E . n 
I 1 13  GLY 13  12  12  GLY GLY E . n 
I 1 14  PRO 14  13  13  PRO PRO E . n 
I 1 15  VAL 15  14  14  VAL VAL E . n 
I 1 16  GLN 16  15  15  GLN GLN E . n 
I 1 17  GLY 17  16  16  GLY GLY E . n 
I 1 18  ILE 18  17  17  ILE ILE E . n 
I 1 19  ILE 19  18  18  ILE ILE E . n 
I 1 20  ASN 20  19  19  ASN ASN E . n 
I 1 21  PHE 21  20  20  PHE PHE E . n 
I 1 22  GLU 22  21  21  GLU GLU E . n 
I 1 23  GLN 23  22  22  GLN GLN E . n 
I 1 24  LYS 24  23  23  LYS LYS E . n 
I 1 25  GLU 25  24  24  GLU GLU E . n 
I 1 26  SER 26  25  25  SER SER E . n 
I 1 27  ASN 27  26  26  ASN ASN E . n 
I 1 28  GLY 28  27  27  GLY GLY E . n 
I 1 29  PRO 29  28  28  PRO PRO E . n 
I 1 30  VAL 30  29  29  VAL VAL E . n 
I 1 31  LYS 31  30  30  LYS LYS E . n 
I 1 32  VAL 32  31  31  VAL VAL E . n 
I 1 33  TRP 33  32  32  TRP TRP E . n 
I 1 34  GLY 34  33  33  GLY GLY E . n 
I 1 35  SER 35  34  34  SER SER E . n 
I 1 36  ILE 36  35  35  ILE ILE E . n 
I 1 37  LYS 37  36  36  LYS LYS E . n 
I 1 38  GLY 38  37  37  GLY GLY E . n 
I 1 39  LEU 39  38  38  LEU LEU E . n 
I 1 40  THR 40  39  39  THR THR E . n 
I 1 41  GLU 41  40  40  GLU GLU E . n 
I 1 42  GLY 42  41  41  GLY GLY E . n 
I 1 43  LEU 43  42  42  LEU LEU E . n 
I 1 44  HIS 44  43  43  HIS HIS E . n 
I 1 45  GLY 45  44  44  GLY GLY E . n 
I 1 46  PHE 46  45  45  PHE PHE E . n 
I 1 47  HIS 47  46  46  HIS HIS E . n 
I 1 48  VAL 48  47  47  VAL VAL E . n 
I 1 49  HIS 49  48  48  HIS HIS E . n 
I 1 50  GLU 50  49  49  GLU GLU E . n 
I 1 51  PHE 51  50  50  PHE PHE E . n 
I 1 52  GLY 52  51  51  GLY GLY E . n 
I 1 53  ASP 53  52  52  ASP ASP E . n 
I 1 54  ASN 54  53  53  ASN ASN E . n 
I 1 55  THR 55  54  54  THR THR E . n 
I 1 56  ALA 56  55  55  ALA ALA E . n 
I 1 57  GLY 57  56  56  GLY GLY E . n 
I 1 58  CYS 58  57  57  CYS CYS E . n 
I 1 59  THR 59  58  58  THR THR E . n 
I 1 60  SER 60  59  59  SER SER E . n 
I 1 61  ALA 61  60  60  ALA ALA E . n 
I 1 62  GLY 62  61  61  GLY GLY E . n 
I 1 63  PRO 63  62  62  PRO PRO E . n 
I 1 64  HIS 64  63  63  HIS HIS E . n 
I 1 65  PHE 65  64  64  PHE PHE E . n 
I 1 66  ASN 66  65  65  ASN ASN E . n 
I 1 67  PRO 67  66  66  PRO PRO E . n 
I 1 68  LEU 68  67  67  LEU LEU E . n 
I 1 69  SER 69  68  68  SER SER E . n 
I 1 70  ARG 70  69  69  ARG ARG E . n 
I 1 71  LYS 71  70  70  LYS LYS E . n 
I 1 72  HIS 72  71  71  HIS HIS E . n 
I 1 73  GLY 73  72  72  GLY GLY E . n 
I 1 74  GLY 74  73  73  GLY GLY E . n 
I 1 75  PRO 75  74  74  PRO PRO E . n 
I 1 76  LYS 76  75  75  LYS LYS E . n 
I 1 77  ASP 77  76  76  ASP ASP E . n 
I 1 78  GLU 78  77  77  GLU GLU E . n 
I 1 79  GLU 79  78  78  GLU GLU E . n 
I 1 80  ARG 80  79  79  ARG ARG E . n 
I 1 81  HIS 81  80  80  HIS HIS E . n 
I 1 82  VAL 82  81  81  VAL VAL E . n 
I 1 83  GLY 83  82  82  GLY GLY E . n 
I 1 84  ASP 84  83  83  ASP ASP E . n 
I 1 85  LEU 85  84  84  LEU LEU E . n 
I 1 86  GLY 86  85  85  GLY GLY E . n 
I 1 87  ASN 87  86  86  ASN ASN E . n 
I 1 88  VAL 88  87  87  VAL VAL E . n 
I 1 89  THR 89  88  88  THR THR E . n 
I 1 90  ALA 90  89  89  ALA ALA E . n 
I 1 91  ASP 91  90  90  ASP ASP E . n 
I 1 92  LYS 92  91  91  LYS LYS E . n 
I 1 93  ASP 93  92  92  ASP ASP E . n 
I 1 94  GLY 94  93  93  GLY GLY E . n 
I 1 95  VAL 95  94  94  VAL VAL E . n 
I 1 96  ALA 96  95  95  ALA ALA E . n 
I 1 97  ASP 97  96  96  ASP ASP E . n 
I 1 98  VAL 98  97  97  VAL VAL E . n 
I 1 99  SER 99  98  98  SER SER E . n 
I 1 100 ILE 100 99  99  ILE ILE E . n 
I 1 101 GLU 101 100 100 GLU GLU E . n 
I 1 102 ASP 102 101 101 ASP ASP E . n 
I 1 103 SER 103 102 102 SER SER E . n 
I 1 104 VAL 104 103 103 VAL VAL E . n 
I 1 105 ILE 105 104 104 ILE ILE E . n 
I 1 106 SER 106 105 105 SER SER E . n 
I 1 107 LEU 107 106 106 LEU LEU E . n 
I 1 108 SER 108 107 107 SER SER E . n 
I 1 109 GLY 109 108 108 GLY GLY E . n 
I 1 110 ASP 110 109 109 ASP ASP E . n 
I 1 111 HIS 111 110 110 HIS HIS E . n 
I 1 112 SER 112 111 111 SER SER E . n 
I 1 113 ILE 113 112 112 ILE ILE E . n 
I 1 114 ILE 114 113 113 ILE ILE E . n 
I 1 115 GLY 115 114 114 GLY GLY E . n 
I 1 116 ARG 116 115 115 ARG ARG E . n 
I 1 117 THR 117 116 116 THR THR E . n 
I 1 118 LEU 118 117 117 LEU LEU E . n 
I 1 119 VAL 119 118 118 VAL VAL E . n 
I 1 120 VAL 120 119 119 VAL VAL E . n 
I 1 121 HIS 121 120 120 HIS HIS E . n 
I 1 122 GLU 122 121 121 GLU GLU E . n 
I 1 123 LYS 123 122 122 LYS LYS E . n 
I 1 124 ALA 124 123 123 ALA ALA E . n 
I 1 125 ASP 125 124 124 ASP ASP E . n 
I 1 126 ASP 126 125 125 ASP ASP E . n 
I 1 127 LEU 127 126 126 LEU LEU E . n 
I 1 128 GLY 128 127 127 GLY GLY E . n 
I 1 129 LYS 129 128 128 LYS LYS E . n 
I 1 130 GLY 130 129 129 GLY GLY E . n 
I 1 131 GLY 131 130 130 GLY GLY E . n 
I 1 132 ASN 132 131 131 ASN ASN E . n 
I 1 133 GLU 133 132 132 GLU GLU E . n 
I 1 134 GLU 134 133 133 GLU GLU E . n 
I 1 135 SER 135 134 134 SER SER E . n 
I 1 136 THR 136 135 135 THR THR E . n 
I 1 137 LYS 137 136 136 LYS LYS E . n 
I 1 138 THR 138 137 137 THR THR E . n 
I 1 139 GLY 139 138 138 GLY GLY E . n 
I 1 140 ASN 140 139 139 ASN ASN E . n 
I 1 141 ALA 141 140 140 ALA ALA E . n 
I 1 142 GLY 142 141 141 GLY GLY E . n 
I 1 143 SER 143 142 142 SER SER E . n 
I 1 144 ARG 144 143 143 ARG ARG E . n 
I 1 145 LEU 145 144 144 LEU LEU E . n 
I 1 146 ALA 146 145 145 ALA ALA E . n 
I 1 147 CYS 147 146 146 CYS CYS E . n 
I 1 148 GLY 148 147 147 GLY GLY E . n 
I 1 149 VAL 149 148 148 VAL VAL E . n 
I 1 150 ILE 150 149 149 ILE ILE E . n 
I 1 151 GLY 151 150 150 GLY GLY E . n 
I 1 152 ILE 152 151 151 ILE ILE E . n 
I 1 153 ALA 153 152 152 ALA ALA E . n 
I 1 154 GLN 154 153 153 GLN GLN E . n 
J 1 1   ACE 1   0   0   ACE ACE J . n 
J 1 2   ALA 2   1   1   ALA ALA J . n 
J 1 3   THR 3   2   2   THR THR J . n 
J 1 4   LYS 4   3   3   LYS LYS J . n 
J 1 5   ALA 5   4   4   ALA ALA J . n 
J 1 6   VAL 6   5   5   VAL VAL J . n 
J 1 7   ALA 7   6   6   ALA ALA J . n 
J 1 8   VAL 8   7   7   VAL VAL J . n 
J 1 9   LEU 9   8   8   LEU LEU J . n 
J 1 10  LYS 10  9   9   LYS LYS J . n 
J 1 11  GLY 11  10  10  GLY GLY J . n 
J 1 12  ASP 12  11  11  ASP ASP J . n 
J 1 13  GLY 13  12  12  GLY GLY J . n 
J 1 14  PRO 14  13  13  PRO PRO J . n 
J 1 15  VAL 15  14  14  VAL VAL J . n 
J 1 16  GLN 16  15  15  GLN GLN J . n 
J 1 17  GLY 17  16  16  GLY GLY J . n 
J 1 18  ILE 18  17  17  ILE ILE J . n 
J 1 19  ILE 19  18  18  ILE ILE J . n 
J 1 20  ASN 20  19  19  ASN ASN J . n 
J 1 21  PHE 21  20  20  PHE PHE J . n 
J 1 22  GLU 22  21  21  GLU GLU J . n 
J 1 23  GLN 23  22  22  GLN GLN J . n 
J 1 24  LYS 24  23  23  LYS LYS J . n 
J 1 25  GLU 25  24  24  GLU GLU J . n 
J 1 26  SER 26  25  25  SER SER J . n 
J 1 27  ASN 27  26  26  ASN ASN J . n 
J 1 28  GLY 28  27  27  GLY GLY J . n 
J 1 29  PRO 29  28  28  PRO PRO J . n 
J 1 30  VAL 30  29  29  VAL VAL J . n 
J 1 31  LYS 31  30  30  LYS LYS J . n 
J 1 32  VAL 32  31  31  VAL VAL J . n 
J 1 33  TRP 33  32  32  TRP TRP J . n 
J 1 34  GLY 34  33  33  GLY GLY J . n 
J 1 35  SER 35  34  34  SER SER J . n 
J 1 36  ILE 36  35  35  ILE ILE J . n 
J 1 37  LYS 37  36  36  LYS LYS J . n 
J 1 38  GLY 38  37  37  GLY GLY J . n 
J 1 39  LEU 39  38  38  LEU LEU J . n 
J 1 40  THR 40  39  39  THR THR J . n 
J 1 41  GLU 41  40  40  GLU GLU J . n 
J 1 42  GLY 42  41  41  GLY GLY J . n 
J 1 43  LEU 43  42  42  LEU LEU J . n 
J 1 44  HIS 44  43  43  HIS HIS J . n 
J 1 45  GLY 45  44  44  GLY GLY J . n 
J 1 46  PHE 46  45  45  PHE PHE J . n 
J 1 47  HIS 47  46  46  HIS HIS J . n 
J 1 48  VAL 48  47  47  VAL VAL J . n 
J 1 49  HIS 49  48  48  HIS HIS J . n 
J 1 50  GLU 50  49  49  GLU GLU J . n 
J 1 51  PHE 51  50  50  PHE PHE J . n 
J 1 52  GLY 52  51  51  GLY GLY J . n 
J 1 53  ASP 53  52  52  ASP ASP J . n 
J 1 54  ASN 54  53  53  ASN ASN J . n 
J 1 55  THR 55  54  54  THR THR J . n 
J 1 56  ALA 56  55  55  ALA ALA J . n 
J 1 57  GLY 57  56  56  GLY GLY J . n 
J 1 58  CYS 58  57  57  CYS CYS J . n 
J 1 59  THR 59  58  58  THR THR J . n 
J 1 60  SER 60  59  59  SER SER J . n 
J 1 61  ALA 61  60  60  ALA ALA J . n 
J 1 62  GLY 62  61  61  GLY GLY J . n 
J 1 63  PRO 63  62  62  PRO PRO J . n 
J 1 64  HIS 64  63  63  HIS HIS J . n 
J 1 65  PHE 65  64  64  PHE PHE J . n 
J 1 66  ASN 66  65  65  ASN ASN J . n 
J 1 67  PRO 67  66  66  PRO PRO J . n 
J 1 68  LEU 68  67  67  LEU LEU J . n 
J 1 69  SER 69  68  68  SER SER J . n 
J 1 70  ARG 70  69  69  ARG ARG J . n 
J 1 71  LYS 71  70  70  LYS LYS J . n 
J 1 72  HIS 72  71  71  HIS HIS J . n 
J 1 73  GLY 73  72  72  GLY GLY J . n 
J 1 74  GLY 74  73  73  GLY GLY J . n 
J 1 75  PRO 75  74  74  PRO PRO J . n 
J 1 76  LYS 76  75  75  LYS LYS J . n 
J 1 77  ASP 77  76  76  ASP ASP J . n 
J 1 78  GLU 78  77  77  GLU GLU J . n 
J 1 79  GLU 79  78  78  GLU GLU J . n 
J 1 80  ARG 80  79  79  ARG ARG J . n 
J 1 81  HIS 81  80  80  HIS HIS J . n 
J 1 82  VAL 82  81  81  VAL VAL J . n 
J 1 83  GLY 83  82  82  GLY GLY J . n 
J 1 84  ASP 84  83  83  ASP ASP J . n 
J 1 85  LEU 85  84  84  LEU LEU J . n 
J 1 86  GLY 86  85  85  GLY GLY J . n 
J 1 87  ASN 87  86  86  ASN ASN J . n 
J 1 88  VAL 88  87  87  VAL VAL J . n 
J 1 89  THR 89  88  88  THR THR J . n 
J 1 90  ALA 90  89  89  ALA ALA J . n 
J 1 91  ASP 91  90  90  ASP ASP J . n 
J 1 92  LYS 92  91  91  LYS LYS J . n 
J 1 93  ASP 93  92  92  ASP ASP J . n 
J 1 94  GLY 94  93  93  GLY GLY J . n 
J 1 95  VAL 95  94  94  VAL VAL J . n 
J 1 96  ALA 96  95  95  ALA ALA J . n 
J 1 97  ASP 97  96  96  ASP ASP J . n 
J 1 98  VAL 98  97  97  VAL VAL J . n 
J 1 99  SER 99  98  98  SER SER J . n 
J 1 100 ILE 100 99  99  ILE ILE J . n 
J 1 101 GLU 101 100 100 GLU GLU J . n 
J 1 102 ASP 102 101 101 ASP ASP J . n 
J 1 103 SER 103 102 102 SER SER J . n 
J 1 104 VAL 104 103 103 VAL VAL J . n 
J 1 105 ILE 105 104 104 ILE ILE J . n 
J 1 106 SER 106 105 105 SER SER J . n 
J 1 107 LEU 107 106 106 LEU LEU J . n 
J 1 108 SER 108 107 107 SER SER J . n 
J 1 109 GLY 109 108 108 GLY GLY J . n 
J 1 110 ASP 110 109 109 ASP ASP J . n 
J 1 111 HIS 111 110 110 HIS HIS J . n 
J 1 112 SER 112 111 111 SER SER J . n 
J 1 113 ILE 113 112 112 ILE ILE J . n 
J 1 114 ILE 114 113 113 ILE ILE J . n 
J 1 115 GLY 115 114 114 GLY GLY J . n 
J 1 116 ARG 116 115 115 ARG ARG J . n 
J 1 117 THR 117 116 116 THR THR J . n 
J 1 118 LEU 118 117 117 LEU LEU J . n 
J 1 119 VAL 119 118 118 VAL VAL J . n 
J 1 120 VAL 120 119 119 VAL VAL J . n 
J 1 121 HIS 121 120 120 HIS HIS J . n 
J 1 122 GLU 122 121 121 GLU GLU J . n 
J 1 123 LYS 123 122 122 LYS LYS J . n 
J 1 124 ALA 124 123 123 ALA ALA J . n 
J 1 125 ASP 125 124 124 ASP ASP J . n 
J 1 126 ASP 126 125 125 ASP ASP J . n 
J 1 127 LEU 127 126 126 LEU LEU J . n 
J 1 128 GLY 128 127 127 GLY GLY J . n 
J 1 129 LYS 129 128 128 LYS LYS J . n 
J 1 130 GLY 130 129 129 GLY GLY J . n 
J 1 131 GLY 131 130 130 GLY GLY J . n 
J 1 132 ASN 132 131 131 ASN ASN J . n 
J 1 133 GLU 133 132 132 GLU GLU J . n 
J 1 134 GLU 134 133 133 GLU GLU J . n 
J 1 135 SER 135 134 134 SER SER J . n 
J 1 136 THR 136 135 135 THR THR J . n 
J 1 137 LYS 137 136 136 LYS LYS J . n 
J 1 138 THR 138 137 137 THR THR J . n 
J 1 139 GLY 139 138 138 GLY GLY J . n 
J 1 140 ASN 140 139 139 ASN ASN J . n 
J 1 141 ALA 141 140 140 ALA ALA J . n 
J 1 142 GLY 142 141 141 GLY GLY J . n 
J 1 143 SER 143 142 142 SER SER J . n 
J 1 144 ARG 144 143 143 ARG ARG J . n 
J 1 145 LEU 145 144 144 LEU LEU J . n 
J 1 146 ALA 146 145 145 ALA ALA J . n 
J 1 147 CYS 147 146 146 CYS CYS J . n 
J 1 148 GLY 148 147 147 GLY GLY J . n 
J 1 149 VAL 149 148 148 VAL VAL J . n 
J 1 150 ILE 150 149 149 ILE ILE J . n 
J 1 151 GLY 151 150 150 GLY GLY J . n 
J 1 152 ILE 152 151 151 ILE ILE J . n 
J 1 153 ALA 153 152 152 ALA ALA J . n 
J 1 154 GLN 154 153 153 GLN GLN J . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
K  2 CU  1  154 154 CU  CU  A . 
L  3 ZN  1  155 155 ZN  ZN  A . 
M  2 CU  1  154 154 CU  CU  F . 
N  3 ZN  1  155 155 ZN  ZN  F . 
O  4 SO4 1  356 356 SO4 SO4 F . 
P  2 CU  1  154 154 CU  CU  B . 
Q  3 ZN  1  155 155 ZN  ZN  B . 
R  2 CU  1  154 154 CU  CU  G . 
S  3 ZN  1  155 155 ZN  ZN  G . 
T  2 CU  1  154 154 CU  CU  C . 
U  3 ZN  1  155 155 ZN  ZN  C . 
V  2 CU  1  154 154 CU  CU  H . 
W  3 ZN  1  155 155 ZN  ZN  H . 
X  2 CU  1  154 154 CU  CU  D . 
Y  3 ZN  1  155 155 ZN  ZN  D . 
Z  2 CU  1  154 154 CU  CU  I . 
AA 3 ZN  1  155 155 ZN  ZN  I . 
BA 4 SO4 1  357 357 SO4 SO4 I . 
CA 2 CU  1  154 154 CU  CU  E . 
DA 3 ZN  1  155 155 ZN  ZN  E . 
EA 2 CU  1  154 154 CU  CU  J . 
FA 3 ZN  1  155 155 ZN  ZN  J . 
GA 5 HOH 1  156 3   HOH HOH A . 
GA 5 HOH 2  157 4   HOH HOH A . 
GA 5 HOH 3  158 5   HOH HOH A . 
GA 5 HOH 4  159 6   HOH HOH A . 
GA 5 HOH 5  160 8   HOH HOH A . 
GA 5 HOH 6  161 10  HOH HOH A . 
GA 5 HOH 7  162 11  HOH HOH A . 
GA 5 HOH 8  163 12  HOH HOH A . 
GA 5 HOH 9  164 13  HOH HOH A . 
GA 5 HOH 10 165 14  HOH HOH A . 
GA 5 HOH 11 166 15  HOH HOH A . 
GA 5 HOH 12 167 16  HOH HOH A . 
GA 5 HOH 13 168 18  HOH HOH A . 
GA 5 HOH 14 169 19  HOH HOH A . 
GA 5 HOH 15 170 20  HOH HOH A . 
GA 5 HOH 16 171 23  HOH HOH A . 
GA 5 HOH 17 172 24  HOH HOH A . 
GA 5 HOH 18 173 25  HOH HOH A . 
GA 5 HOH 19 174 26  HOH HOH A . 
GA 5 HOH 20 175 27  HOH HOH A . 
GA 5 HOH 21 176 28  HOH HOH A . 
GA 5 HOH 22 177 29  HOH HOH A . 
GA 5 HOH 23 178 31  HOH HOH A . 
GA 5 HOH 24 179 32  HOH HOH A . 
GA 5 HOH 25 180 33  HOH HOH A . 
GA 5 HOH 26 181 34  HOH HOH A . 
GA 5 HOH 27 182 35  HOH HOH A . 
GA 5 HOH 28 183 36  HOH HOH A . 
GA 5 HOH 29 184 37  HOH HOH A . 
GA 5 HOH 30 185 38  HOH HOH A . 
GA 5 HOH 31 186 43  HOH HOH A . 
GA 5 HOH 32 187 44  HOH HOH A . 
GA 5 HOH 33 188 45  HOH HOH A . 
GA 5 HOH 34 189 46  HOH HOH A . 
GA 5 HOH 35 190 48  HOH HOH A . 
GA 5 HOH 36 191 49  HOH HOH A . 
GA 5 HOH 37 192 50  HOH HOH A . 
GA 5 HOH 38 193 51  HOH HOH A . 
GA 5 HOH 39 194 52  HOH HOH A . 
GA 5 HOH 40 195 53  HOH HOH A . 
GA 5 HOH 41 196 57  HOH HOH A . 
GA 5 HOH 42 197 66  HOH HOH A . 
GA 5 HOH 43 198 72  HOH HOH A . 
GA 5 HOH 44 199 82  HOH HOH A . 
GA 5 HOH 45 200 84  HOH HOH A . 
GA 5 HOH 46 201 103 HOH HOH A . 
GA 5 HOH 47 202 139 HOH HOH A . 
GA 5 HOH 48 203 185 HOH HOH A . 
GA 5 HOH 49 204 186 HOH HOH A . 
GA 5 HOH 50 205 191 HOH HOH A . 
GA 5 HOH 51 206 198 HOH HOH A . 
GA 5 HOH 52 207 263 HOH HOH A . 
GA 5 HOH 53 208 290 HOH HOH A . 
GA 5 HOH 54 209 359 HOH HOH A . 
GA 5 HOH 55 210 828 HOH HOH A . 
GA 5 HOH 56 211 853 HOH HOH A . 
HA 5 HOH 1  357 7   HOH HOH F . 
HA 5 HOH 2  358 21  HOH HOH F . 
HA 5 HOH 3  359 40  HOH HOH F . 
HA 5 HOH 4  360 41  HOH HOH F . 
HA 5 HOH 5  361 68  HOH HOH F . 
HA 5 HOH 6  362 73  HOH HOH F . 
HA 5 HOH 7  363 77  HOH HOH F . 
HA 5 HOH 8  364 78  HOH HOH F . 
HA 5 HOH 9  365 83  HOH HOH F . 
HA 5 HOH 10 366 87  HOH HOH F . 
HA 5 HOH 11 367 92  HOH HOH F . 
HA 5 HOH 12 368 104 HOH HOH F . 
HA 5 HOH 13 369 108 HOH HOH F . 
HA 5 HOH 14 370 109 HOH HOH F . 
HA 5 HOH 15 371 113 HOH HOH F . 
HA 5 HOH 16 372 114 HOH HOH F . 
HA 5 HOH 17 373 116 HOH HOH F . 
HA 5 HOH 18 374 117 HOH HOH F . 
HA 5 HOH 19 375 118 HOH HOH F . 
HA 5 HOH 20 376 120 HOH HOH F . 
HA 5 HOH 21 377 121 HOH HOH F . 
HA 5 HOH 22 378 123 HOH HOH F . 
HA 5 HOH 23 379 126 HOH HOH F . 
HA 5 HOH 24 380 127 HOH HOH F . 
HA 5 HOH 25 381 128 HOH HOH F . 
HA 5 HOH 26 382 129 HOH HOH F . 
HA 5 HOH 27 383 131 HOH HOH F . 
HA 5 HOH 28 384 133 HOH HOH F . 
HA 5 HOH 29 385 134 HOH HOH F . 
HA 5 HOH 30 386 135 HOH HOH F . 
HA 5 HOH 31 387 137 HOH HOH F . 
HA 5 HOH 32 388 138 HOH HOH F . 
HA 5 HOH 33 389 143 HOH HOH F . 
HA 5 HOH 34 390 145 HOH HOH F . 
HA 5 HOH 35 391 146 HOH HOH F . 
HA 5 HOH 36 392 147 HOH HOH F . 
HA 5 HOH 37 393 148 HOH HOH F . 
HA 5 HOH 38 394 149 HOH HOH F . 
HA 5 HOH 39 395 150 HOH HOH F . 
HA 5 HOH 40 396 184 HOH HOH F . 
HA 5 HOH 41 397 187 HOH HOH F . 
HA 5 HOH 42 398 197 HOH HOH F . 
HA 5 HOH 43 399 261 HOH HOH F . 
HA 5 HOH 44 400 262 HOH HOH F . 
HA 5 HOH 45 401 272 HOH HOH F . 
HA 5 HOH 46 402 280 HOH HOH F . 
HA 5 HOH 47 403 289 HOH HOH F . 
HA 5 HOH 48 404 350 HOH HOH F . 
HA 5 HOH 49 405 519 HOH HOH F . 
HA 5 HOH 50 406 530 HOH HOH F . 
HA 5 HOH 51 407 532 HOH HOH F . 
HA 5 HOH 52 408 832 HOH HOH F . 
IA 5 HOH 1  156 56  HOH HOH B . 
IA 5 HOH 2  157 160 HOH HOH B . 
IA 5 HOH 3  158 161 HOH HOH B . 
IA 5 HOH 4  159 162 HOH HOH B . 
IA 5 HOH 5  160 165 HOH HOH B . 
IA 5 HOH 6  161 190 HOH HOH B . 
IA 5 HOH 7  162 192 HOH HOH B . 
IA 5 HOH 8  163 202 HOH HOH B . 
IA 5 HOH 9  164 203 HOH HOH B . 
IA 5 HOH 10 165 205 HOH HOH B . 
IA 5 HOH 11 166 208 HOH HOH B . 
IA 5 HOH 12 167 209 HOH HOH B . 
IA 5 HOH 13 168 216 HOH HOH B . 
IA 5 HOH 14 169 217 HOH HOH B . 
IA 5 HOH 15 170 219 HOH HOH B . 
IA 5 HOH 16 171 220 HOH HOH B . 
IA 5 HOH 17 172 221 HOH HOH B . 
IA 5 HOH 18 173 223 HOH HOH B . 
IA 5 HOH 19 174 224 HOH HOH B . 
IA 5 HOH 20 175 225 HOH HOH B . 
IA 5 HOH 21 176 226 HOH HOH B . 
IA 5 HOH 22 177 227 HOH HOH B . 
IA 5 HOH 23 178 228 HOH HOH B . 
IA 5 HOH 24 179 232 HOH HOH B . 
IA 5 HOH 25 180 233 HOH HOH B . 
IA 5 HOH 26 181 235 HOH HOH B . 
IA 5 HOH 27 182 236 HOH HOH B . 
IA 5 HOH 28 183 237 HOH HOH B . 
IA 5 HOH 29 184 238 HOH HOH B . 
IA 5 HOH 30 185 239 HOH HOH B . 
IA 5 HOH 31 186 243 HOH HOH B . 
IA 5 HOH 32 187 244 HOH HOH B . 
IA 5 HOH 33 188 245 HOH HOH B . 
IA 5 HOH 34 189 246 HOH HOH B . 
IA 5 HOH 35 190 247 HOH HOH B . 
IA 5 HOH 36 191 253 HOH HOH B . 
IA 5 HOH 37 192 256 HOH HOH B . 
IA 5 HOH 38 193 264 HOH HOH B . 
IA 5 HOH 39 194 270 HOH HOH B . 
IA 5 HOH 40 195 271 HOH HOH B . 
IA 5 HOH 41 196 274 HOH HOH B . 
IA 5 HOH 42 197 277 HOH HOH B . 
IA 5 HOH 43 198 283 HOH HOH B . 
IA 5 HOH 44 199 301 HOH HOH B . 
IA 5 HOH 45 200 313 HOH HOH B . 
IA 5 HOH 46 201 340 HOH HOH B . 
IA 5 HOH 47 202 610 HOH HOH B . 
IA 5 HOH 48 203 638 HOH HOH B . 
IA 5 HOH 49 204 643 HOH HOH B . 
IA 5 HOH 50 205 646 HOH HOH B . 
IA 5 HOH 51 206 647 HOH HOH B . 
IA 5 HOH 52 207 745 HOH HOH B . 
IA 5 HOH 53 208 945 HOH HOH B . 
IA 5 HOH 54 209 951 HOH HOH B . 
JA 5 HOH 1  156 61  HOH HOH G . 
JA 5 HOH 2  157 79  HOH HOH G . 
JA 5 HOH 3  158 88  HOH HOH G . 
JA 5 HOH 4  159 90  HOH HOH G . 
JA 5 HOH 5  160 91  HOH HOH G . 
JA 5 HOH 6  161 119 HOH HOH G . 
JA 5 HOH 7  162 125 HOH HOH G . 
JA 5 HOH 8  163 130 HOH HOH G . 
JA 5 HOH 9  164 166 HOH HOH G . 
JA 5 HOH 10 165 170 HOH HOH G . 
JA 5 HOH 11 166 188 HOH HOH G . 
JA 5 HOH 12 167 201 HOH HOH G . 
JA 5 HOH 13 168 211 HOH HOH G . 
JA 5 HOH 14 169 240 HOH HOH G . 
JA 5 HOH 15 170 241 HOH HOH G . 
JA 5 HOH 16 171 255 HOH HOH G . 
JA 5 HOH 17 172 267 HOH HOH G . 
JA 5 HOH 18 173 275 HOH HOH G . 
JA 5 HOH 19 174 286 HOH HOH G . 
JA 5 HOH 20 175 287 HOH HOH G . 
JA 5 HOH 21 176 292 HOH HOH G . 
JA 5 HOH 22 177 293 HOH HOH G . 
JA 5 HOH 23 178 302 HOH HOH G . 
JA 5 HOH 24 179 303 HOH HOH G . 
JA 5 HOH 25 180 304 HOH HOH G . 
JA 5 HOH 26 181 305 HOH HOH G . 
JA 5 HOH 27 182 309 HOH HOH G . 
JA 5 HOH 28 183 316 HOH HOH G . 
JA 5 HOH 29 184 317 HOH HOH G . 
JA 5 HOH 30 185 318 HOH HOH G . 
JA 5 HOH 31 186 319 HOH HOH G . 
JA 5 HOH 32 187 320 HOH HOH G . 
JA 5 HOH 33 188 321 HOH HOH G . 
JA 5 HOH 34 189 323 HOH HOH G . 
JA 5 HOH 35 190 324 HOH HOH G . 
JA 5 HOH 36 191 325 HOH HOH G . 
JA 5 HOH 37 192 326 HOH HOH G . 
JA 5 HOH 38 193 327 HOH HOH G . 
JA 5 HOH 39 194 328 HOH HOH G . 
JA 5 HOH 40 195 329 HOH HOH G . 
JA 5 HOH 41 196 330 HOH HOH G . 
JA 5 HOH 42 197 331 HOH HOH G . 
JA 5 HOH 43 198 332 HOH HOH G . 
JA 5 HOH 44 199 333 HOH HOH G . 
JA 5 HOH 45 200 334 HOH HOH G . 
JA 5 HOH 46 201 335 HOH HOH G . 
JA 5 HOH 47 202 336 HOH HOH G . 
JA 5 HOH 48 203 337 HOH HOH G . 
JA 5 HOH 49 204 338 HOH HOH G . 
JA 5 HOH 50 205 339 HOH HOH G . 
JA 5 HOH 51 206 344 HOH HOH G . 
JA 5 HOH 52 207 345 HOH HOH G . 
JA 5 HOH 53 208 346 HOH HOH G . 
JA 5 HOH 54 209 347 HOH HOH G . 
JA 5 HOH 55 210 348 HOH HOH G . 
JA 5 HOH 56 211 349 HOH HOH G . 
JA 5 HOH 57 212 351 HOH HOH G . 
JA 5 HOH 58 213 358 HOH HOH G . 
JA 5 HOH 59 214 362 HOH HOH G . 
JA 5 HOH 60 215 363 HOH HOH G . 
JA 5 HOH 61 216 364 HOH HOH G . 
JA 5 HOH 62 217 366 HOH HOH G . 
JA 5 HOH 63 218 367 HOH HOH G . 
KA 5 HOH 1  156 62  HOH HOH C . 
KA 5 HOH 2  157 65  HOH HOH C . 
KA 5 HOH 3  158 85  HOH HOH C . 
KA 5 HOH 4  159 268 HOH HOH C . 
KA 5 HOH 5  160 276 HOH HOH C . 
KA 5 HOH 6  161 282 HOH HOH C . 
KA 5 HOH 7  162 284 HOH HOH C . 
KA 5 HOH 8  163 297 HOH HOH C . 
KA 5 HOH 9  164 298 HOH HOH C . 
KA 5 HOH 10 165 360 HOH HOH C . 
KA 5 HOH 11 166 404 HOH HOH C . 
KA 5 HOH 12 167 405 HOH HOH C . 
KA 5 HOH 13 168 408 HOH HOH C . 
KA 5 HOH 14 169 409 HOH HOH C . 
KA 5 HOH 15 170 410 HOH HOH C . 
KA 5 HOH 16 171 411 HOH HOH C . 
KA 5 HOH 17 172 412 HOH HOH C . 
KA 5 HOH 18 173 415 HOH HOH C . 
KA 5 HOH 19 174 416 HOH HOH C . 
KA 5 HOH 20 175 418 HOH HOH C . 
KA 5 HOH 21 176 420 HOH HOH C . 
KA 5 HOH 22 177 423 HOH HOH C . 
KA 5 HOH 23 178 424 HOH HOH C . 
KA 5 HOH 24 179 425 HOH HOH C . 
KA 5 HOH 25 180 428 HOH HOH C . 
KA 5 HOH 26 181 432 HOH HOH C . 
KA 5 HOH 27 182 433 HOH HOH C . 
KA 5 HOH 28 183 435 HOH HOH C . 
KA 5 HOH 29 184 436 HOH HOH C . 
KA 5 HOH 30 185 437 HOH HOH C . 
KA 5 HOH 31 186 438 HOH HOH C . 
KA 5 HOH 32 187 443 HOH HOH C . 
KA 5 HOH 33 188 444 HOH HOH C . 
KA 5 HOH 34 189 445 HOH HOH C . 
KA 5 HOH 35 190 446 HOH HOH C . 
KA 5 HOH 36 191 447 HOH HOH C . 
KA 5 HOH 37 192 448 HOH HOH C . 
KA 5 HOH 38 193 449 HOH HOH C . 
KA 5 HOH 39 194 450 HOH HOH C . 
KA 5 HOH 40 195 452 HOH HOH C . 
KA 5 HOH 41 196 454 HOH HOH C . 
KA 5 HOH 42 197 521 HOH HOH C . 
KA 5 HOH 43 198 540 HOH HOH C . 
LA 5 HOH 1  156 69  HOH HOH H . 
LA 5 HOH 2  157 71  HOH HOH H . 
LA 5 HOH 3  158 76  HOH HOH H . 
LA 5 HOH 4  159 80  HOH HOH H . 
LA 5 HOH 5  160 86  HOH HOH H . 
LA 5 HOH 6  161 89  HOH HOH H . 
LA 5 HOH 7  162 152 HOH HOH H . 
LA 5 HOH 8  163 153 HOH HOH H . 
LA 5 HOH 9  164 164 HOH HOH H . 
LA 5 HOH 10 165 168 HOH HOH H . 
LA 5 HOH 11 166 169 HOH HOH H . 
LA 5 HOH 12 167 171 HOH HOH H . 
LA 5 HOH 13 168 172 HOH HOH H . 
LA 5 HOH 14 169 180 HOH HOH H . 
LA 5 HOH 15 170 181 HOH HOH H . 
LA 5 HOH 16 171 193 HOH HOH H . 
LA 5 HOH 17 172 194 HOH HOH H . 
LA 5 HOH 18 173 257 HOH HOH H . 
LA 5 HOH 19 174 258 HOH HOH H . 
LA 5 HOH 20 175 259 HOH HOH H . 
LA 5 HOH 21 176 260 HOH HOH H . 
LA 5 HOH 22 177 285 HOH HOH H . 
LA 5 HOH 23 178 294 HOH HOH H . 
LA 5 HOH 24 179 299 HOH HOH H . 
LA 5 HOH 25 180 352 HOH HOH H . 
LA 5 HOH 26 181 353 HOH HOH H . 
LA 5 HOH 27 182 365 HOH HOH H . 
LA 5 HOH 28 183 403 HOH HOH H . 
LA 5 HOH 29 184 421 HOH HOH H . 
LA 5 HOH 30 185 440 HOH HOH H . 
LA 5 HOH 31 186 441 HOH HOH H . 
LA 5 HOH 32 187 501 HOH HOH H . 
LA 5 HOH 33 188 503 HOH HOH H . 
LA 5 HOH 34 189 504 HOH HOH H . 
LA 5 HOH 35 190 505 HOH HOH H . 
LA 5 HOH 36 191 508 HOH HOH H . 
LA 5 HOH 37 192 509 HOH HOH H . 
LA 5 HOH 38 193 512 HOH HOH H . 
LA 5 HOH 39 194 516 HOH HOH H . 
LA 5 HOH 40 195 517 HOH HOH H . 
LA 5 HOH 41 196 518 HOH HOH H . 
LA 5 HOH 42 197 520 HOH HOH H . 
LA 5 HOH 43 198 522 HOH HOH H . 
LA 5 HOH 44 199 523 HOH HOH H . 
LA 5 HOH 45 200 524 HOH HOH H . 
LA 5 HOH 46 201 525 HOH HOH H . 
LA 5 HOH 47 202 526 HOH HOH H . 
LA 5 HOH 48 203 527 HOH HOH H . 
LA 5 HOH 49 204 528 HOH HOH H . 
LA 5 HOH 50 205 529 HOH HOH H . 
LA 5 HOH 51 206 533 HOH HOH H . 
LA 5 HOH 52 207 534 HOH HOH H . 
LA 5 HOH 53 208 535 HOH HOH H . 
LA 5 HOH 54 209 537 HOH HOH H . 
LA 5 HOH 55 210 538 HOH HOH H . 
LA 5 HOH 56 211 539 HOH HOH H . 
LA 5 HOH 57 212 544 HOH HOH H . 
LA 5 HOH 58 213 545 HOH HOH H . 
LA 5 HOH 59 214 547 HOH HOH H . 
LA 5 HOH 60 215 548 HOH HOH H . 
LA 5 HOH 61 216 549 HOH HOH H . 
LA 5 HOH 62 217 550 HOH HOH H . 
LA 5 HOH 63 218 551 HOH HOH H . 
MA 5 HOH 1  156 74  HOH HOH D . 
MA 5 HOH 2  157 173 HOH HOH D . 
MA 5 HOH 3  158 183 HOH HOH D . 
MA 5 HOH 4  159 229 HOH HOH D . 
MA 5 HOH 5  160 230 HOH HOH D . 
MA 5 HOH 6  161 265 HOH HOH D . 
MA 5 HOH 7  162 602 HOH HOH D . 
MA 5 HOH 8  163 603 HOH HOH D . 
MA 5 HOH 9  164 606 HOH HOH D . 
MA 5 HOH 10 165 607 HOH HOH D . 
MA 5 HOH 11 166 608 HOH HOH D . 
MA 5 HOH 12 167 609 HOH HOH D . 
MA 5 HOH 13 168 611 HOH HOH D . 
MA 5 HOH 14 169 612 HOH HOH D . 
MA 5 HOH 15 170 615 HOH HOH D . 
MA 5 HOH 16 171 617 HOH HOH D . 
MA 5 HOH 17 172 618 HOH HOH D . 
MA 5 HOH 18 173 619 HOH HOH D . 
MA 5 HOH 19 174 622 HOH HOH D . 
MA 5 HOH 20 175 623 HOH HOH D . 
MA 5 HOH 21 176 624 HOH HOH D . 
MA 5 HOH 22 177 626 HOH HOH D . 
MA 5 HOH 23 178 627 HOH HOH D . 
MA 5 HOH 24 179 629 HOH HOH D . 
MA 5 HOH 25 180 630 HOH HOH D . 
MA 5 HOH 26 181 631 HOH HOH D . 
MA 5 HOH 27 182 632 HOH HOH D . 
MA 5 HOH 28 183 634 HOH HOH D . 
MA 5 HOH 29 184 635 HOH HOH D . 
MA 5 HOH 30 185 636 HOH HOH D . 
MA 5 HOH 31 186 637 HOH HOH D . 
MA 5 HOH 32 187 639 HOH HOH D . 
MA 5 HOH 33 188 641 HOH HOH D . 
MA 5 HOH 34 189 644 HOH HOH D . 
MA 5 HOH 35 190 645 HOH HOH D . 
MA 5 HOH 36 191 648 HOH HOH D . 
MA 5 HOH 37 192 650 HOH HOH D . 
MA 5 HOH 38 193 651 HOH HOH D . 
MA 5 HOH 39 194 653 HOH HOH D . 
MA 5 HOH 40 195 654 HOH HOH D . 
MA 5 HOH 41 196 701 HOH HOH D . 
MA 5 HOH 42 197 703 HOH HOH D . 
MA 5 HOH 43 198 707 HOH HOH D . 
NA 5 HOH 1  358 93  HOH HOH I . 
NA 5 HOH 2  359 94  HOH HOH I . 
NA 5 HOH 3  360 95  HOH HOH I . 
NA 5 HOH 4  361 99  HOH HOH I . 
NA 5 HOH 5  362 175 HOH HOH I . 
NA 5 HOH 6  363 215 HOH HOH I . 
NA 5 HOH 7  364 278 HOH HOH I . 
NA 5 HOH 8  365 295 HOH HOH I . 
NA 5 HOH 9  366 640 HOH HOH I . 
NA 5 HOH 10 367 702 HOH HOH I . 
NA 5 HOH 11 368 704 HOH HOH I . 
NA 5 HOH 12 369 705 HOH HOH I . 
NA 5 HOH 13 370 708 HOH HOH I . 
NA 5 HOH 14 371 709 HOH HOH I . 
NA 5 HOH 15 372 710 HOH HOH I . 
NA 5 HOH 16 373 712 HOH HOH I . 
NA 5 HOH 17 374 713 HOH HOH I . 
NA 5 HOH 18 375 715 HOH HOH I . 
NA 5 HOH 19 376 717 HOH HOH I . 
NA 5 HOH 20 377 718 HOH HOH I . 
NA 5 HOH 21 378 723 HOH HOH I . 
NA 5 HOH 22 379 724 HOH HOH I . 
NA 5 HOH 23 380 725 HOH HOH I . 
NA 5 HOH 24 381 726 HOH HOH I . 
NA 5 HOH 25 382 727 HOH HOH I . 
NA 5 HOH 26 383 729 HOH HOH I . 
NA 5 HOH 27 384 731 HOH HOH I . 
NA 5 HOH 28 385 734 HOH HOH I . 
NA 5 HOH 29 386 735 HOH HOH I . 
NA 5 HOH 30 387 737 HOH HOH I . 
NA 5 HOH 31 388 738 HOH HOH I . 
NA 5 HOH 32 389 739 HOH HOH I . 
NA 5 HOH 33 390 740 HOH HOH I . 
NA 5 HOH 34 391 741 HOH HOH I . 
NA 5 HOH 35 392 743 HOH HOH I . 
NA 5 HOH 36 393 746 HOH HOH I . 
NA 5 HOH 37 394 747 HOH HOH I . 
NA 5 HOH 38 395 749 HOH HOH I . 
NA 5 HOH 39 396 750 HOH HOH I . 
NA 5 HOH 40 397 751 HOH HOH I . 
NA 5 HOH 41 398 752 HOH HOH I . 
NA 5 HOH 42 399 755 HOH HOH I . 
NA 5 HOH 43 400 904 HOH HOH I . 
NA 5 HOH 44 401 946 HOH HOH I . 
NA 5 HOH 45 402 952 HOH HOH I . 
NA 5 HOH 46 403 954 HOH HOH I . 
OA 5 HOH 1  156 9   HOH HOH E . 
OA 5 HOH 2  157 59  HOH HOH E . 
OA 5 HOH 3  158 102 HOH HOH E . 
OA 5 HOH 4  159 112 HOH HOH E . 
OA 5 HOH 5  160 179 HOH HOH E . 
OA 5 HOH 6  161 196 HOH HOH E . 
OA 5 HOH 7  162 199 HOH HOH E . 
OA 5 HOH 8  163 269 HOH HOH E . 
OA 5 HOH 9  164 291 HOH HOH E . 
OA 5 HOH 10 165 802 HOH HOH E . 
OA 5 HOH 11 166 804 HOH HOH E . 
OA 5 HOH 12 167 805 HOH HOH E . 
OA 5 HOH 13 168 808 HOH HOH E . 
OA 5 HOH 14 169 809 HOH HOH E . 
OA 5 HOH 15 170 811 HOH HOH E . 
OA 5 HOH 16 171 813 HOH HOH E . 
OA 5 HOH 17 172 817 HOH HOH E . 
OA 5 HOH 18 173 818 HOH HOH E . 
OA 5 HOH 19 174 820 HOH HOH E . 
OA 5 HOH 20 175 822 HOH HOH E . 
OA 5 HOH 21 176 823 HOH HOH E . 
OA 5 HOH 22 177 825 HOH HOH E . 
OA 5 HOH 23 178 826 HOH HOH E . 
OA 5 HOH 24 179 829 HOH HOH E . 
OA 5 HOH 25 180 831 HOH HOH E . 
OA 5 HOH 26 181 833 HOH HOH E . 
OA 5 HOH 27 182 835 HOH HOH E . 
OA 5 HOH 28 183 837 HOH HOH E . 
OA 5 HOH 29 184 839 HOH HOH E . 
OA 5 HOH 30 185 847 HOH HOH E . 
OA 5 HOH 31 186 849 HOH HOH E . 
OA 5 HOH 32 187 850 HOH HOH E . 
OA 5 HOH 33 188 851 HOH HOH E . 
OA 5 HOH 34 189 901 HOH HOH E . 
OA 5 HOH 35 190 902 HOH HOH E . 
OA 5 HOH 36 191 913 HOH HOH E . 
OA 5 HOH 37 192 921 HOH HOH E . 
OA 5 HOH 38 193 940 HOH HOH E . 
OA 5 HOH 39 194 941 HOH HOH E . 
PA 5 HOH 1  156 81  HOH HOH J . 
PA 5 HOH 2  157 96  HOH HOH J . 
PA 5 HOH 3  158 97  HOH HOH J . 
PA 5 HOH 4  159 98  HOH HOH J . 
PA 5 HOH 5  160 167 HOH HOH J . 
PA 5 HOH 6  161 177 HOH HOH J . 
PA 5 HOH 7  162 178 HOH HOH J . 
PA 5 HOH 8  163 212 HOH HOH J . 
PA 5 HOH 9  164 354 HOH HOH J . 
PA 5 HOH 10 165 355 HOH HOH J . 
PA 5 HOH 11 166 719 HOH HOH J . 
PA 5 HOH 12 167 732 HOH HOH J . 
PA 5 HOH 13 168 733 HOH HOH J . 
PA 5 HOH 14 169 803 HOH HOH J . 
PA 5 HOH 15 170 810 HOH HOH J . 
PA 5 HOH 16 171 840 HOH HOH J . 
PA 5 HOH 17 172 903 HOH HOH J . 
PA 5 HOH 18 173 909 HOH HOH J . 
PA 5 HOH 19 174 917 HOH HOH J . 
PA 5 HOH 20 175 918 HOH HOH J . 
PA 5 HOH 21 176 919 HOH HOH J . 
PA 5 HOH 22 177 920 HOH HOH J . 
PA 5 HOH 23 178 922 HOH HOH J . 
PA 5 HOH 24 179 924 HOH HOH J . 
PA 5 HOH 25 180 925 HOH HOH J . 
PA 5 HOH 26 181 927 HOH HOH J . 
PA 5 HOH 27 182 928 HOH HOH J . 
PA 5 HOH 28 183 929 HOH HOH J . 
PA 5 HOH 29 184 932 HOH HOH J . 
PA 5 HOH 30 185 933 HOH HOH J . 
PA 5 HOH 31 186 935 HOH HOH J . 
PA 5 HOH 32 187 936 HOH HOH J . 
PA 5 HOH 33 188 937 HOH HOH J . 
PA 5 HOH 34 189 938 HOH HOH J . 
PA 5 HOH 35 190 939 HOH HOH J . 
PA 5 HOH 36 191 943 HOH HOH J . 
PA 5 HOH 37 192 944 HOH HOH J . 
PA 5 HOH 38 193 947 HOH HOH J . 
PA 5 HOH 39 194 949 HOH HOH J . 
PA 5 HOH 40 195 950 HOH HOH J . 
# 
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 
4 author_and_software_defined_assembly PISA dimeric 2 
5 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,K,L,M,N,O,GA,HA   
2 1 C,D,P,Q,R,S,IA,JA     
3 1 E,F,T,U,V,W,KA,LA     
4 1 G,H,X,Y,Z,AA,BA,MA,NA 
5 1 I,J,CA,DA,EA,FA,OA,PA 
# 
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)' 1900  ? 
1 MORE         -37   ? 
1 'SSA (A^2)'  13630 ? 
2 'ABSA (A^2)' 1990  ? 
2 MORE         -44   ? 
2 'SSA (A^2)'  13750 ? 
3 'ABSA (A^2)' 1890  ? 
3 MORE         -39   ? 
3 'SSA (A^2)'  13830 ? 
4 'ABSA (A^2)' 2100  ? 
4 MORE         -47   ? 
4 'SSA (A^2)'  13680 ? 
5 'ABSA (A^2)' 1910  ? 
5 MORE         -37   ? 
5 'SSA (A^2)'  13620 ? 
# 
_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   NE2 ? A HIS 49  ? A HIS 48  ? 1_555 CU ? K  CU . ? A CU 154 ? 1_555 NE2 ? A HIS 64  ? A HIS 63  ? 1_555 100.5 ? 
2   NE2 ? A HIS 49  ? A HIS 48  ? 1_555 CU ? K  CU . ? A CU 154 ? 1_555 NE2 ? A HIS 121 ? A HIS 120 ? 1_555 108.1 ? 
3   NE2 ? A HIS 64  ? A HIS 63  ? 1_555 CU ? K  CU . ? A CU 154 ? 1_555 NE2 ? A HIS 121 ? A HIS 120 ? 1_555 151.2 ? 
4   NE2 ? A HIS 49  ? A HIS 48  ? 1_555 CU ? K  CU . ? A CU 154 ? 1_555 ND1 ? A HIS 47  ? A HIS 46  ? 1_555 131.9 ? 
5   NE2 ? A HIS 64  ? A HIS 63  ? 1_555 CU ? K  CU . ? A CU 154 ? 1_555 ND1 ? A HIS 47  ? A HIS 46  ? 1_555 72.9  ? 
6   NE2 ? A HIS 121 ? A HIS 120 ? 1_555 CU ? K  CU . ? A CU 154 ? 1_555 ND1 ? A HIS 47  ? A HIS 46  ? 1_555 85.6  ? 
7   ND1 ? A HIS 72  ? A HIS 71  ? 1_555 ZN ? L  ZN . ? A ZN 155 ? 1_555 OD1 ? A ASP 84  ? A ASP 83  ? 1_555 84.8  ? 
8   ND1 ? A HIS 72  ? A HIS 71  ? 1_555 ZN ? L  ZN . ? A ZN 155 ? 1_555 ND1 ? A HIS 64  ? A HIS 63  ? 1_555 105.0 ? 
9   OD1 ? A ASP 84  ? A ASP 83  ? 1_555 ZN ? L  ZN . ? A ZN 155 ? 1_555 ND1 ? A HIS 64  ? A HIS 63  ? 1_555 116.8 ? 
10  ND1 ? A HIS 72  ? A HIS 71  ? 1_555 ZN ? L  ZN . ? A ZN 155 ? 1_555 ND1 ? A HIS 81  ? A HIS 80  ? 1_555 112.4 ? 
11  OD1 ? A ASP 84  ? A ASP 83  ? 1_555 ZN ? L  ZN . ? A ZN 155 ? 1_555 ND1 ? A HIS 81  ? A HIS 80  ? 1_555 111.4 ? 
12  ND1 ? A HIS 64  ? A HIS 63  ? 1_555 ZN ? L  ZN . ? A ZN 155 ? 1_555 ND1 ? A HIS 81  ? A HIS 80  ? 1_555 120.3 ? 
13  NE2 ? C HIS 64  ? B HIS 63  ? 1_555 CU ? P  CU . ? B CU 154 ? 1_555 NE2 ? C HIS 121 ? B HIS 120 ? 1_555 152.4 ? 
14  NE2 ? C HIS 64  ? B HIS 63  ? 1_555 CU ? P  CU . ? B CU 154 ? 1_555 NE2 ? C HIS 49  ? B HIS 48  ? 1_555 102.0 ? 
15  NE2 ? C HIS 121 ? B HIS 120 ? 1_555 CU ? P  CU . ? B CU 154 ? 1_555 NE2 ? C HIS 49  ? B HIS 48  ? 1_555 102.3 ? 
16  NE2 ? C HIS 64  ? B HIS 63  ? 1_555 CU ? P  CU . ? B CU 154 ? 1_555 ND1 ? C HIS 47  ? B HIS 46  ? 1_555 84.1  ? 
17  NE2 ? C HIS 121 ? B HIS 120 ? 1_555 CU ? P  CU . ? B CU 154 ? 1_555 ND1 ? C HIS 47  ? B HIS 46  ? 1_555 89.0  ? 
18  NE2 ? C HIS 49  ? B HIS 48  ? 1_555 CU ? P  CU . ? B CU 154 ? 1_555 ND1 ? C HIS 47  ? B HIS 46  ? 1_555 132.3 ? 
19  ND1 ? C HIS 81  ? B HIS 80  ? 1_555 ZN ? Q  ZN . ? B ZN 155 ? 1_555 OD1 ? C ASP 84  ? B ASP 83  ? 1_555 100.8 ? 
20  ND1 ? C HIS 81  ? B HIS 80  ? 1_555 ZN ? Q  ZN . ? B ZN 155 ? 1_555 ND1 ? C HIS 64  ? B HIS 63  ? 1_555 109.7 ? 
21  OD1 ? C ASP 84  ? B ASP 83  ? 1_555 ZN ? Q  ZN . ? B ZN 155 ? 1_555 ND1 ? C HIS 64  ? B HIS 63  ? 1_555 106.0 ? 
22  ND1 ? C HIS 81  ? B HIS 80  ? 1_555 ZN ? Q  ZN . ? B ZN 155 ? 1_555 ND1 ? C HIS 72  ? B HIS 71  ? 1_555 132.4 ? 
23  OD1 ? C ASP 84  ? B ASP 83  ? 1_555 ZN ? Q  ZN . ? B ZN 155 ? 1_555 ND1 ? C HIS 72  ? B HIS 71  ? 1_555 106.3 ? 
24  ND1 ? C HIS 64  ? B HIS 63  ? 1_555 ZN ? Q  ZN . ? B ZN 155 ? 1_555 ND1 ? C HIS 72  ? B HIS 71  ? 1_555 99.5  ? 
25  NE2 ? E HIS 49  ? C HIS 48  ? 1_555 CU ? T  CU . ? C CU 154 ? 1_555 NE2 ? E HIS 121 ? C HIS 120 ? 1_555 110.9 ? 
26  NE2 ? E HIS 49  ? C HIS 48  ? 1_555 CU ? T  CU . ? C CU 154 ? 1_555 ND1 ? E HIS 47  ? C HIS 46  ? 1_555 142.6 ? 
27  NE2 ? E HIS 121 ? C HIS 120 ? 1_555 CU ? T  CU . ? C CU 154 ? 1_555 ND1 ? E HIS 47  ? C HIS 46  ? 1_555 94.7  ? 
28  NE2 ? E HIS 49  ? C HIS 48  ? 1_555 CU ? T  CU . ? C CU 154 ? 1_555 NE2 ? E HIS 64  ? C HIS 63  ? 1_555 96.6  ? 
29  NE2 ? E HIS 121 ? C HIS 120 ? 1_555 CU ? T  CU . ? C CU 154 ? 1_555 NE2 ? E HIS 64  ? C HIS 63  ? 1_555 144.9 ? 
30  ND1 ? E HIS 47  ? C HIS 46  ? 1_555 CU ? T  CU . ? C CU 154 ? 1_555 NE2 ? E HIS 64  ? C HIS 63  ? 1_555 74.0  ? 
31  ND1 ? E HIS 72  ? C HIS 71  ? 1_555 ZN ? U  ZN . ? C ZN 155 ? 1_555 OD1 ? E ASP 84  ? C ASP 83  ? 1_555 89.6  ? 
32  ND1 ? E HIS 72  ? C HIS 71  ? 1_555 ZN ? U  ZN . ? C ZN 155 ? 1_555 ND1 ? E HIS 81  ? C HIS 80  ? 1_555 111.0 ? 
33  OD1 ? E ASP 84  ? C ASP 83  ? 1_555 ZN ? U  ZN . ? C ZN 155 ? 1_555 ND1 ? E HIS 81  ? C HIS 80  ? 1_555 98.4  ? 
34  ND1 ? E HIS 72  ? C HIS 71  ? 1_555 ZN ? U  ZN . ? C ZN 155 ? 1_555 ND1 ? E HIS 64  ? C HIS 63  ? 1_555 106.8 ? 
35  OD1 ? E ASP 84  ? C ASP 83  ? 1_555 ZN ? U  ZN . ? C ZN 155 ? 1_555 ND1 ? E HIS 64  ? C HIS 63  ? 1_555 132.7 ? 
36  ND1 ? E HIS 81  ? C HIS 80  ? 1_555 ZN ? U  ZN . ? C ZN 155 ? 1_555 ND1 ? E HIS 64  ? C HIS 63  ? 1_555 115.2 ? 
37  ND1 ? G HIS 47  ? D HIS 46  ? 1_555 CU ? X  CU . ? D CU 154 ? 1_555 NE2 ? G HIS 49  ? D HIS 48  ? 1_555 142.6 ? 
38  ND1 ? G HIS 47  ? D HIS 46  ? 1_555 CU ? X  CU . ? D CU 154 ? 1_555 NE2 ? G HIS 64  ? D HIS 63  ? 1_555 75.3  ? 
39  NE2 ? G HIS 49  ? D HIS 48  ? 1_555 CU ? X  CU . ? D CU 154 ? 1_555 NE2 ? G HIS 64  ? D HIS 63  ? 1_555 97.7  ? 
40  ND1 ? G HIS 47  ? D HIS 46  ? 1_555 CU ? X  CU . ? D CU 154 ? 1_555 NE2 ? G HIS 121 ? D HIS 120 ? 1_555 95.4  ? 
41  NE2 ? G HIS 49  ? D HIS 48  ? 1_555 CU ? X  CU . ? D CU 154 ? 1_555 NE2 ? G HIS 121 ? D HIS 120 ? 1_555 105.4 ? 
42  NE2 ? G HIS 64  ? D HIS 63  ? 1_555 CU ? X  CU . ? D CU 154 ? 1_555 NE2 ? G HIS 121 ? D HIS 120 ? 1_555 151.2 ? 
43  ND1 ? G HIS 64  ? D HIS 63  ? 1_555 ZN ? Y  ZN . ? D ZN 155 ? 1_555 ND1 ? G HIS 72  ? D HIS 71  ? 1_555 107.9 ? 
44  ND1 ? G HIS 64  ? D HIS 63  ? 1_555 ZN ? Y  ZN . ? D ZN 155 ? 1_555 ND1 ? G HIS 81  ? D HIS 80  ? 1_555 112.4 ? 
45  ND1 ? G HIS 72  ? D HIS 71  ? 1_555 ZN ? Y  ZN . ? D ZN 155 ? 1_555 ND1 ? G HIS 81  ? D HIS 80  ? 1_555 116.4 ? 
46  ND1 ? G HIS 64  ? D HIS 63  ? 1_555 ZN ? Y  ZN . ? D ZN 155 ? 1_555 OD1 ? G ASP 84  ? D ASP 83  ? 1_555 117.2 ? 
47  ND1 ? G HIS 72  ? D HIS 71  ? 1_555 ZN ? Y  ZN . ? D ZN 155 ? 1_555 OD1 ? G ASP 84  ? D ASP 83  ? 1_555 91.1  ? 
48  ND1 ? G HIS 81  ? D HIS 80  ? 1_555 ZN ? Y  ZN . ? D ZN 155 ? 1_555 OD1 ? G ASP 84  ? D ASP 83  ? 1_555 110.3 ? 
49  NE2 ? I HIS 49  ? E HIS 48  ? 1_555 CU ? CA CU . ? E CU 154 ? 1_555 ND1 ? I HIS 47  ? E HIS 46  ? 1_555 135.1 ? 
50  NE2 ? I HIS 49  ? E HIS 48  ? 1_555 CU ? CA CU . ? E CU 154 ? 1_555 NE2 ? I HIS 121 ? E HIS 120 ? 1_555 105.6 ? 
51  ND1 ? I HIS 47  ? E HIS 46  ? 1_555 CU ? CA CU . ? E CU 154 ? 1_555 NE2 ? I HIS 121 ? E HIS 120 ? 1_555 92.2  ? 
52  NE2 ? I HIS 49  ? E HIS 48  ? 1_555 CU ? CA CU . ? E CU 154 ? 1_555 NE2 ? I HIS 64  ? E HIS 63  ? 1_555 95.6  ? 
53  ND1 ? I HIS 47  ? E HIS 46  ? 1_555 CU ? CA CU . ? E CU 154 ? 1_555 NE2 ? I HIS 64  ? E HIS 63  ? 1_555 86.3  ? 
54  NE2 ? I HIS 121 ? E HIS 120 ? 1_555 CU ? CA CU . ? E CU 154 ? 1_555 NE2 ? I HIS 64  ? E HIS 63  ? 1_555 151.0 ? 
55  ND1 ? I HIS 81  ? E HIS 80  ? 1_555 ZN ? DA ZN . ? E ZN 155 ? 1_555 ND1 ? I HIS 72  ? E HIS 71  ? 1_555 112.0 ? 
56  ND1 ? I HIS 81  ? E HIS 80  ? 1_555 ZN ? DA ZN . ? E ZN 155 ? 1_555 OD2 ? I ASP 84  ? E ASP 83  ? 1_555 76.3  ? 
57  ND1 ? I HIS 72  ? E HIS 71  ? 1_555 ZN ? DA ZN . ? E ZN 155 ? 1_555 OD2 ? I ASP 84  ? E ASP 83  ? 1_555 68.6  ? 
58  ND1 ? I HIS 81  ? E HIS 80  ? 1_555 ZN ? DA ZN . ? E ZN 155 ? 1_555 ND1 ? I HIS 64  ? E HIS 63  ? 1_555 117.0 ? 
59  ND1 ? I HIS 72  ? E HIS 71  ? 1_555 ZN ? DA ZN . ? E ZN 155 ? 1_555 ND1 ? I HIS 64  ? E HIS 63  ? 1_555 118.4 ? 
60  OD2 ? I ASP 84  ? E ASP 83  ? 1_555 ZN ? DA ZN . ? E ZN 155 ? 1_555 ND1 ? I HIS 64  ? E HIS 63  ? 1_555 156.1 ? 
61  ND1 ? I HIS 81  ? E HIS 80  ? 1_555 ZN ? DA ZN . ? E ZN 155 ? 1_555 OD1 ? I ASP 84  ? E ASP 83  ? 1_555 101.3 ? 
62  ND1 ? I HIS 72  ? E HIS 71  ? 1_555 ZN ? DA ZN . ? E ZN 155 ? 1_555 OD1 ? I ASP 84  ? E ASP 83  ? 1_555 102.9 ? 
63  OD2 ? I ASP 84  ? E ASP 83  ? 1_555 ZN ? DA ZN . ? E ZN 155 ? 1_555 OD1 ? I ASP 84  ? E ASP 83  ? 1_555 54.7  ? 
64  ND1 ? I HIS 64  ? E HIS 63  ? 1_555 ZN ? DA ZN . ? E ZN 155 ? 1_555 OD1 ? I ASP 84  ? E ASP 83  ? 1_555 101.8 ? 
65  NE2 ? B HIS 49  ? F HIS 48  ? 1_555 CU ? M  CU . ? F CU 154 ? 1_555 NE2 ? B HIS 64  ? F HIS 63  ? 1_555 89.8  ? 
66  NE2 ? B HIS 49  ? F HIS 48  ? 1_555 CU ? M  CU . ? F CU 154 ? 1_555 NE2 ? B HIS 121 ? F HIS 120 ? 1_555 108.7 ? 
67  NE2 ? B HIS 64  ? F HIS 63  ? 1_555 CU ? M  CU . ? F CU 154 ? 1_555 NE2 ? B HIS 121 ? F HIS 120 ? 1_555 157.7 ? 
68  NE2 ? B HIS 49  ? F HIS 48  ? 1_555 CU ? M  CU . ? F CU 154 ? 1_555 ND1 ? B HIS 47  ? F HIS 46  ? 1_555 132.0 ? 
69  NE2 ? B HIS 64  ? F HIS 63  ? 1_555 CU ? M  CU . ? F CU 154 ? 1_555 ND1 ? B HIS 47  ? F HIS 46  ? 1_555 83.2  ? 
70  NE2 ? B HIS 121 ? F HIS 120 ? 1_555 CU ? M  CU . ? F CU 154 ? 1_555 ND1 ? B HIS 47  ? F HIS 46  ? 1_555 92.9  ? 
71  OD1 ? B ASP 84  ? F ASP 83  ? 1_555 ZN ? N  ZN . ? F ZN 155 ? 1_555 ND1 ? B HIS 72  ? F HIS 71  ? 1_555 103.1 ? 
72  OD1 ? B ASP 84  ? F ASP 83  ? 1_555 ZN ? N  ZN . ? F ZN 155 ? 1_555 ND1 ? B HIS 64  ? F HIS 63  ? 1_555 114.6 ? 
73  ND1 ? B HIS 72  ? F HIS 71  ? 1_555 ZN ? N  ZN . ? F ZN 155 ? 1_555 ND1 ? B HIS 64  ? F HIS 63  ? 1_555 111.2 ? 
74  OD1 ? B ASP 84  ? F ASP 83  ? 1_555 ZN ? N  ZN . ? F ZN 155 ? 1_555 ND1 ? B HIS 81  ? F HIS 80  ? 1_555 101.9 ? 
75  ND1 ? B HIS 72  ? F HIS 71  ? 1_555 ZN ? N  ZN . ? F ZN 155 ? 1_555 ND1 ? B HIS 81  ? F HIS 80  ? 1_555 112.9 ? 
76  ND1 ? B HIS 64  ? F HIS 63  ? 1_555 ZN ? N  ZN . ? F ZN 155 ? 1_555 ND1 ? B HIS 81  ? F HIS 80  ? 1_555 112.5 ? 
77  NE2 ? D HIS 49  ? G HIS 48  ? 1_555 CU ? R  CU . ? G CU 154 ? 1_555 NE2 ? D HIS 121 ? G HIS 120 ? 1_555 99.4  ? 
78  NE2 ? D HIS 49  ? G HIS 48  ? 1_555 CU ? R  CU . ? G CU 154 ? 1_555 NE2 ? D HIS 64  ? G HIS 63  ? 1_555 94.6  ? 
79  NE2 ? D HIS 121 ? G HIS 120 ? 1_555 CU ? R  CU . ? G CU 154 ? 1_555 NE2 ? D HIS 64  ? G HIS 63  ? 1_555 165.2 ? 
80  NE2 ? D HIS 49  ? G HIS 48  ? 1_555 CU ? R  CU . ? G CU 154 ? 1_555 ND1 ? D HIS 47  ? G HIS 46  ? 1_555 132.7 ? 
81  NE2 ? D HIS 121 ? G HIS 120 ? 1_555 CU ? R  CU . ? G CU 154 ? 1_555 ND1 ? D HIS 47  ? G HIS 46  ? 1_555 96.1  ? 
82  NE2 ? D HIS 64  ? G HIS 63  ? 1_555 CU ? R  CU . ? G CU 154 ? 1_555 ND1 ? D HIS 47  ? G HIS 46  ? 1_555 77.7  ? 
83  OD1 ? D ASP 84  ? G ASP 83  ? 1_555 ZN ? S  ZN . ? G ZN 155 ? 1_555 ND1 ? D HIS 64  ? G HIS 63  ? 1_555 102.8 ? 
84  OD1 ? D ASP 84  ? G ASP 83  ? 1_555 ZN ? S  ZN . ? G ZN 155 ? 1_555 OD2 ? D ASP 84  ? G ASP 83  ? 1_555 52.2  ? 
85  ND1 ? D HIS 64  ? G HIS 63  ? 1_555 ZN ? S  ZN . ? G ZN 155 ? 1_555 OD2 ? D ASP 84  ? G ASP 83  ? 1_555 155.0 ? 
86  OD1 ? D ASP 84  ? G ASP 83  ? 1_555 ZN ? S  ZN . ? G ZN 155 ? 1_555 ND1 ? D HIS 81  ? G HIS 80  ? 1_555 107.3 ? 
87  ND1 ? D HIS 64  ? G HIS 63  ? 1_555 ZN ? S  ZN . ? G ZN 155 ? 1_555 ND1 ? D HIS 81  ? G HIS 80  ? 1_555 109.4 ? 
88  OD2 ? D ASP 84  ? G ASP 83  ? 1_555 ZN ? S  ZN . ? G ZN 155 ? 1_555 ND1 ? D HIS 81  ? G HIS 80  ? 1_555 81.3  ? 
89  OD1 ? D ASP 84  ? G ASP 83  ? 1_555 ZN ? S  ZN . ? G ZN 155 ? 1_555 ND1 ? D HIS 72  ? G HIS 71  ? 1_555 101.9 ? 
90  ND1 ? D HIS 64  ? G HIS 63  ? 1_555 ZN ? S  ZN . ? G ZN 155 ? 1_555 ND1 ? D HIS 72  ? G HIS 71  ? 1_555 112.4 ? 
91  OD2 ? D ASP 84  ? G ASP 83  ? 1_555 ZN ? S  ZN . ? G ZN 155 ? 1_555 ND1 ? D HIS 72  ? G HIS 71  ? 1_555 78.1  ? 
92  ND1 ? D HIS 81  ? G HIS 80  ? 1_555 ZN ? S  ZN . ? G ZN 155 ? 1_555 ND1 ? D HIS 72  ? G HIS 71  ? 1_555 121.1 ? 
93  ND1 ? F HIS 47  ? H HIS 46  ? 1_555 CU ? V  CU . ? H CU 154 ? 1_555 NE2 ? F HIS 49  ? H HIS 48  ? 1_555 137.4 ? 
94  ND1 ? F HIS 47  ? H HIS 46  ? 1_555 CU ? V  CU . ? H CU 154 ? 1_555 NE2 ? F HIS 121 ? H HIS 120 ? 1_555 93.1  ? 
95  NE2 ? F HIS 49  ? H HIS 48  ? 1_555 CU ? V  CU . ? H CU 154 ? 1_555 NE2 ? F HIS 121 ? H HIS 120 ? 1_555 105.8 ? 
96  ND1 ? F HIS 47  ? H HIS 46  ? 1_555 CU ? V  CU . ? H CU 154 ? 1_555 NE2 ? F HIS 64  ? H HIS 63  ? 1_555 75.1  ? 
97  NE2 ? F HIS 49  ? H HIS 48  ? 1_555 CU ? V  CU . ? H CU 154 ? 1_555 NE2 ? F HIS 64  ? H HIS 63  ? 1_555 94.8  ? 
98  NE2 ? F HIS 121 ? H HIS 120 ? 1_555 CU ? V  CU . ? H CU 154 ? 1_555 NE2 ? F HIS 64  ? H HIS 63  ? 1_555 158.4 ? 
99  ND1 ? F HIS 72  ? H HIS 71  ? 1_555 ZN ? W  ZN . ? H ZN 155 ? 1_555 ND1 ? F HIS 64  ? H HIS 63  ? 1_555 104.5 ? 
100 ND1 ? F HIS 72  ? H HIS 71  ? 1_555 ZN ? W  ZN . ? H ZN 155 ? 1_555 ND1 ? F HIS 81  ? H HIS 80  ? 1_555 119.9 ? 
101 ND1 ? F HIS 64  ? H HIS 63  ? 1_555 ZN ? W  ZN . ? H ZN 155 ? 1_555 ND1 ? F HIS 81  ? H HIS 80  ? 1_555 106.9 ? 
102 ND1 ? F HIS 72  ? H HIS 71  ? 1_555 ZN ? W  ZN . ? H ZN 155 ? 1_555 OD1 ? F ASP 84  ? H ASP 83  ? 1_555 108.1 ? 
103 ND1 ? F HIS 64  ? H HIS 63  ? 1_555 ZN ? W  ZN . ? H ZN 155 ? 1_555 OD1 ? F ASP 84  ? H ASP 83  ? 1_555 121.6 ? 
104 ND1 ? F HIS 81  ? H HIS 80  ? 1_555 ZN ? W  ZN . ? H ZN 155 ? 1_555 OD1 ? F ASP 84  ? H ASP 83  ? 1_555 96.9  ? 
105 NE2 ? H HIS 121 ? I HIS 120 ? 1_555 CU ? Z  CU . ? I CU 154 ? 1_555 NE2 ? H HIS 64  ? I HIS 63  ? 1_555 143.4 ? 
106 NE2 ? H HIS 121 ? I HIS 120 ? 1_555 CU ? Z  CU . ? I CU 154 ? 1_555 ND1 ? H HIS 47  ? I HIS 46  ? 1_555 81.8  ? 
107 NE2 ? H HIS 64  ? I HIS 63  ? 1_555 CU ? Z  CU . ? I CU 154 ? 1_555 ND1 ? H HIS 47  ? I HIS 46  ? 1_555 78.5  ? 
108 NE2 ? H HIS 121 ? I HIS 120 ? 1_555 CU ? Z  CU . ? I CU 154 ? 1_555 NE2 ? H HIS 49  ? I HIS 48  ? 1_555 109.5 ? 
109 NE2 ? H HIS 64  ? I HIS 63  ? 1_555 CU ? Z  CU . ? I CU 154 ? 1_555 NE2 ? H HIS 49  ? I HIS 48  ? 1_555 106.5 ? 
110 ND1 ? H HIS 47  ? I HIS 46  ? 1_555 CU ? Z  CU . ? I CU 154 ? 1_555 NE2 ? H HIS 49  ? I HIS 48  ? 1_555 133.1 ? 
111 ND1 ? H HIS 64  ? I HIS 63  ? 1_555 ZN ? AA ZN . ? I ZN 155 ? 1_555 ND1 ? H HIS 81  ? I HIS 80  ? 1_555 115.8 ? 
112 ND1 ? H HIS 64  ? I HIS 63  ? 1_555 ZN ? AA ZN . ? I ZN 155 ? 1_555 ND1 ? H HIS 72  ? I HIS 71  ? 1_555 103.4 ? 
113 ND1 ? H HIS 81  ? I HIS 80  ? 1_555 ZN ? AA ZN . ? I ZN 155 ? 1_555 ND1 ? H HIS 72  ? I HIS 71  ? 1_555 129.3 ? 
114 ND1 ? H HIS 64  ? I HIS 63  ? 1_555 ZN ? AA ZN . ? I ZN 155 ? 1_555 OD1 ? H ASP 84  ? I ASP 83  ? 1_555 107.6 ? 
115 ND1 ? H HIS 81  ? I HIS 80  ? 1_555 ZN ? AA ZN . ? I ZN 155 ? 1_555 OD1 ? H ASP 84  ? I ASP 83  ? 1_555 97.4  ? 
116 ND1 ? H HIS 72  ? I HIS 71  ? 1_555 ZN ? AA ZN . ? I ZN 155 ? 1_555 OD1 ? H ASP 84  ? I ASP 83  ? 1_555 100.0 ? 
117 ND1 ? J HIS 47  ? J HIS 46  ? 1_555 CU ? EA CU . ? J CU 154 ? 1_555 NE2 ? J HIS 64  ? J HIS 63  ? 1_555 74.7  ? 
118 ND1 ? J HIS 47  ? J HIS 46  ? 1_555 CU ? EA CU . ? J CU 154 ? 1_555 NE2 ? J HIS 121 ? J HIS 120 ? 1_555 87.1  ? 
119 NE2 ? J HIS 64  ? J HIS 63  ? 1_555 CU ? EA CU . ? J CU 154 ? 1_555 NE2 ? J HIS 121 ? J HIS 120 ? 1_555 143.2 ? 
120 ND1 ? J HIS 47  ? J HIS 46  ? 1_555 CU ? EA CU . ? J CU 154 ? 1_555 NE2 ? J HIS 49  ? J HIS 48  ? 1_555 145.5 ? 
121 NE2 ? J HIS 64  ? J HIS 63  ? 1_555 CU ? EA CU . ? J CU 154 ? 1_555 NE2 ? J HIS 49  ? J HIS 48  ? 1_555 110.1 ? 
122 NE2 ? J HIS 121 ? J HIS 120 ? 1_555 CU ? EA CU . ? J CU 154 ? 1_555 NE2 ? J HIS 49  ? J HIS 48  ? 1_555 103.0 ? 
123 OD1 ? J ASP 84  ? J ASP 83  ? 1_555 ZN ? FA ZN . ? J ZN 155 ? 1_555 ND1 ? J HIS 81  ? J HIS 80  ? 1_555 107.9 ? 
124 OD1 ? J ASP 84  ? J ASP 83  ? 1_555 ZN ? FA ZN . ? J ZN 155 ? 1_555 ND1 ? J HIS 72  ? J HIS 71  ? 1_555 101.8 ? 
125 ND1 ? J HIS 81  ? J HIS 80  ? 1_555 ZN ? FA ZN . ? J ZN 155 ? 1_555 ND1 ? J HIS 72  ? J HIS 71  ? 1_555 103.3 ? 
126 OD1 ? J ASP 84  ? J ASP 83  ? 1_555 ZN ? FA ZN . ? J ZN 155 ? 1_555 ND1 ? J HIS 64  ? J HIS 63  ? 1_555 118.7 ? 
127 ND1 ? J HIS 81  ? J HIS 80  ? 1_555 ZN ? FA ZN . ? J ZN 155 ? 1_555 ND1 ? J HIS 64  ? J HIS 63  ? 1_555 110.3 ? 
128 ND1 ? J HIS 72  ? J HIS 71  ? 1_555 ZN ? FA ZN . ? J ZN 155 ? 1_555 ND1 ? J HIS 64  ? J HIS 63  ? 1_555 113.6 ? 
# 
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 1993-04-15 
2 'Structure model' 1 1 2008-03-03 
3 'Structure model' 1 2 2011-07-13 
4 'Structure model' 1 3 2017-11-29 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' 'Version format compliance' 
3 4 'Structure model' 'Derived calculations'      
4 4 'Structure model' Other                       
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 4 'Structure model' pdbx_database_status 
2 4 'Structure model' struct_conf          
3 4 'Structure model' struct_conf_type     
# 
_pdbx_audit_revision_item.ordinal             1 
_pdbx_audit_revision_item.revision_ordinal    4 
_pdbx_audit_revision_item.data_content_type   'Structure model' 
_pdbx_audit_revision_item.item                '_pdbx_database_status.process_site' 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
X-PLOR 'model building' . ? 1 
X-PLOR refinement       . ? 2 
X-PLOR phasing          . ? 3 
# 
_pdbx_database_remark.id     700 
_pdbx_database_remark.text   
;SHEET
THE SHEETS PRESENTED ON SHEET RECORDS BELOW ARE ACTUALLY
EIGHT-STRANDED BETA-BARRELS.  EACH ONE IS REPRESENTED BY A
NINE-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE
IDENTICAL.
;
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1  1 NE2 A HIS 43  ? ? CD2 A HIS 43  ? ? 1.300 1.373 -0.073 0.011 N 
2  1 NE2 A HIS 48  ? ? CD2 A HIS 48  ? ? 1.295 1.373 -0.078 0.011 N 
3  1 NE2 A HIS 71  ? ? CD2 A HIS 71  ? ? 1.302 1.373 -0.071 0.011 N 
4  1 NE2 A HIS 80  ? ? CD2 A HIS 80  ? ? 1.293 1.373 -0.080 0.011 N 
5  1 NE2 A HIS 110 ? ? CD2 A HIS 110 ? ? 1.304 1.373 -0.069 0.011 N 
6  1 NE2 A HIS 120 ? ? CD2 A HIS 120 ? ? 1.301 1.373 -0.072 0.011 N 
7  1 NE2 F HIS 46  ? ? CD2 F HIS 46  ? ? 1.301 1.373 -0.072 0.011 N 
8  1 NE2 F HIS 48  ? ? CD2 F HIS 48  ? ? 1.298 1.373 -0.075 0.011 N 
9  1 NE2 F HIS 71  ? ? CD2 F HIS 71  ? ? 1.299 1.373 -0.074 0.011 N 
10 1 NE2 F HIS 80  ? ? CD2 F HIS 80  ? ? 1.294 1.373 -0.079 0.011 N 
11 1 NE2 F HIS 110 ? ? CD2 F HIS 110 ? ? 1.296 1.373 -0.077 0.011 N 
12 1 NE2 F HIS 120 ? ? CD2 F HIS 120 ? ? 1.299 1.373 -0.074 0.011 N 
13 1 NE2 B HIS 43  ? ? CD2 B HIS 43  ? ? 1.302 1.373 -0.071 0.011 N 
14 1 NE2 B HIS 46  ? ? CD2 B HIS 46  ? ? 1.286 1.373 -0.087 0.011 N 
15 1 NE2 B HIS 63  ? ? CD2 B HIS 63  ? ? 1.300 1.373 -0.073 0.011 N 
16 1 NE2 B HIS 71  ? ? CD2 B HIS 71  ? ? 1.282 1.373 -0.091 0.011 N 
17 1 NE2 G HIS 43  ? ? CD2 G HIS 43  ? ? 1.285 1.373 -0.088 0.011 N 
18 1 NE2 G HIS 46  ? ? CD2 G HIS 46  ? ? 1.299 1.373 -0.074 0.011 N 
19 1 NE2 G HIS 63  ? ? CD2 G HIS 63  ? ? 1.295 1.373 -0.078 0.011 N 
20 1 NE2 G HIS 71  ? ? CD2 G HIS 71  ? ? 1.294 1.373 -0.079 0.011 N 
21 1 NE2 G HIS 80  ? ? CD2 G HIS 80  ? ? 1.301 1.373 -0.072 0.011 N 
22 1 NE2 G HIS 110 ? ? CD2 G HIS 110 ? ? 1.294 1.373 -0.079 0.011 N 
23 1 NE2 G HIS 120 ? ? CD2 G HIS 120 ? ? 1.301 1.373 -0.072 0.011 N 
24 1 NE2 C HIS 43  ? ? CD2 C HIS 43  ? ? 1.295 1.373 -0.078 0.011 N 
25 1 NE2 C HIS 46  ? ? CD2 C HIS 46  ? ? 1.302 1.373 -0.071 0.011 N 
26 1 NE2 C HIS 71  ? ? CD2 C HIS 71  ? ? 1.281 1.373 -0.092 0.011 N 
27 1 NE2 C HIS 80  ? ? CD2 C HIS 80  ? ? 1.288 1.373 -0.085 0.011 N 
28 1 NE2 C HIS 120 ? ? CD2 C HIS 120 ? ? 1.300 1.373 -0.073 0.011 N 
29 1 NE2 H HIS 43  ? ? CD2 H HIS 43  ? ? 1.305 1.373 -0.068 0.011 N 
30 1 NE2 H HIS 46  ? ? CD2 H HIS 46  ? ? 1.305 1.373 -0.068 0.011 N 
31 1 NE2 H HIS 71  ? ? CD2 H HIS 71  ? ? 1.295 1.373 -0.078 0.011 N 
32 1 NE2 H HIS 80  ? ? CD2 H HIS 80  ? ? 1.297 1.373 -0.076 0.011 N 
33 1 NE2 H HIS 110 ? ? CD2 H HIS 110 ? ? 1.294 1.373 -0.079 0.011 N 
34 1 NE2 D HIS 43  ? ? CD2 D HIS 43  ? ? 1.298 1.373 -0.075 0.011 N 
35 1 NE2 D HIS 46  ? ? CD2 D HIS 46  ? ? 1.301 1.373 -0.072 0.011 N 
36 1 NE2 D HIS 48  ? ? CD2 D HIS 48  ? ? 1.305 1.373 -0.068 0.011 N 
37 1 NE2 D HIS 71  ? ? CD2 D HIS 71  ? ? 1.278 1.373 -0.095 0.011 N 
38 1 NE2 D HIS 80  ? ? CD2 D HIS 80  ? ? 1.290 1.373 -0.083 0.011 N 
39 1 NE2 D HIS 120 ? ? CD2 D HIS 120 ? ? 1.301 1.373 -0.072 0.011 N 
40 1 NE2 I HIS 43  ? ? CD2 I HIS 43  ? ? 1.303 1.373 -0.070 0.011 N 
41 1 NE2 I HIS 46  ? ? CD2 I HIS 46  ? ? 1.290 1.373 -0.083 0.011 N 
42 1 NE2 I HIS 48  ? ? CD2 I HIS 48  ? ? 1.304 1.373 -0.069 0.011 N 
43 1 NE2 I HIS 71  ? ? CD2 I HIS 71  ? ? 1.294 1.373 -0.079 0.011 N 
44 1 NE2 I HIS 80  ? ? CD2 I HIS 80  ? ? 1.302 1.373 -0.071 0.011 N 
45 1 NE2 I HIS 110 ? ? CD2 I HIS 110 ? ? 1.301 1.373 -0.072 0.011 N 
46 1 NE2 I HIS 120 ? ? CD2 I HIS 120 ? ? 1.289 1.373 -0.084 0.011 N 
47 1 NE2 E HIS 71  ? ? CD2 E HIS 71  ? ? 1.296 1.373 -0.077 0.011 N 
48 1 NE2 E HIS 80  ? ? CD2 E HIS 80  ? ? 1.299 1.373 -0.074 0.011 N 
49 1 NE2 E HIS 110 ? ? CD2 E HIS 110 ? ? 1.302 1.373 -0.071 0.011 N 
50 1 NE2 J HIS 43  ? ? CD2 J HIS 43  ? ? 1.303 1.373 -0.070 0.011 N 
51 1 NE2 J HIS 48  ? ? CD2 J HIS 48  ? ? 1.304 1.373 -0.069 0.011 N 
52 1 NE2 J HIS 71  ? ? CD2 J HIS 71  ? ? 1.301 1.373 -0.072 0.011 N 
53 1 NE2 J HIS 80  ? ? CD2 J HIS 80  ? ? 1.289 1.373 -0.084 0.011 N 
54 1 NE2 J HIS 110 ? ? CD2 J HIS 110 ? ? 1.306 1.373 -0.067 0.011 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1  1 CD1 A TRP 32  ? ? CG  A TRP 32  ? ? CD2 A TRP 32  ? ? 112.49 106.30 6.19   0.80 N 
2  1 CE2 A TRP 32  ? ? CD2 A TRP 32  ? ? CG  A TRP 32  ? ? 101.94 107.30 -5.36  0.80 N 
3  1 CB  A ARG 69  ? ? CG  A ARG 69  ? ? CD  A ARG 69  ? ? 94.39  111.60 -17.21 2.60 N 
4  1 NE  A ARG 69  ? ? CZ  A ARG 69  ? ? NH1 A ARG 69  ? ? 123.48 120.30 3.18   0.50 N 
5  1 NE  A ARG 69  ? ? CZ  A ARG 69  ? ? NH2 A ARG 69  ? ? 115.71 120.30 -4.59  0.50 N 
6  1 NE  A ARG 79  ? ? CZ  A ARG 79  ? ? NH1 A ARG 79  ? ? 124.83 120.30 4.53   0.50 N 
7  1 N   A GLU 100 ? ? CA  A GLU 100 ? ? C   A GLU 100 ? ? 92.36  111.00 -18.64 2.70 N 
8  1 NE  A ARG 115 ? ? CZ  A ARG 115 ? ? NH1 A ARG 115 ? ? 125.13 120.30 4.83   0.50 N 
9  1 CD1 F TRP 32  ? ? CG  F TRP 32  ? ? CD2 F TRP 32  ? ? 111.70 106.30 5.40   0.80 N 
10 1 CE2 F TRP 32  ? ? CD2 F TRP 32  ? ? CG  F TRP 32  ? ? 102.30 107.30 -5.00  0.80 N 
11 1 NE  F ARG 79  ? ? CZ  F ARG 79  ? ? NH1 F ARG 79  ? ? 123.86 120.30 3.56   0.50 N 
12 1 NE  F ARG 79  ? ? CZ  F ARG 79  ? ? NH2 F ARG 79  ? ? 116.33 120.30 -3.97  0.50 N 
13 1 CA  F HIS 80  ? ? CB  F HIS 80  ? ? CG  F HIS 80  ? ? 124.83 113.60 11.23  1.70 N 
14 1 NE  F ARG 115 ? ? CZ  F ARG 115 ? ? NH1 F ARG 115 ? ? 123.90 120.30 3.60   0.50 N 
15 1 NE  F ARG 143 ? ? CZ  F ARG 143 ? ? NH1 F ARG 143 ? ? 124.63 120.30 4.33   0.50 N 
16 1 CA  F CYS 146 ? ? CB  F CYS 146 ? ? SG  F CYS 146 ? ? 120.81 114.20 6.61   1.10 N 
17 1 CG1 B VAL 14  ? ? CB  B VAL 14  ? ? CG2 B VAL 14  ? ? 99.96  110.90 -10.94 1.60 N 
18 1 CD1 B TRP 32  ? ? CG  B TRP 32  ? ? CD2 B TRP 32  ? ? 112.92 106.30 6.62   0.80 N 
19 1 CB  B TRP 32  ? ? CG  B TRP 32  ? ? CD1 B TRP 32  ? ? 118.80 127.00 -8.20  1.30 N 
20 1 CE2 B TRP 32  ? ? CD2 B TRP 32  ? ? CG  B TRP 32  ? ? 101.53 107.30 -5.77  0.80 N 
21 1 CG  B TRP 32  ? ? CD2 B TRP 32  ? ? CE3 B TRP 32  ? ? 139.49 133.90 5.59   0.90 N 
22 1 CA  B LYS 70  ? ? CB  B LYS 70  ? ? CG  B LYS 70  ? ? 99.99  113.40 -13.41 2.20 N 
23 1 NE  B ARG 79  ? ? CZ  B ARG 79  ? ? NH1 B ARG 79  ? ? 124.08 120.30 3.78   0.50 N 
24 1 CB  B ASP 83  ? ? CG  B ASP 83  ? ? OD1 B ASP 83  ? ? 124.04 118.30 5.74   0.90 N 
25 1 NE  B ARG 143 ? ? CZ  B ARG 143 ? ? NH1 B ARG 143 ? ? 123.67 120.30 3.37   0.50 N 
26 1 CD1 G TRP 32  ? ? CG  G TRP 32  ? ? CD2 G TRP 32  ? ? 112.77 106.30 6.47   0.80 N 
27 1 CE2 G TRP 32  ? ? CD2 G TRP 32  ? ? CG  G TRP 32  ? ? 101.29 107.30 -6.01  0.80 N 
28 1 NE  G ARG 115 ? ? CZ  G ARG 115 ? ? NH1 G ARG 115 ? ? 124.68 120.30 4.38   0.50 N 
29 1 N   G GLU 133 ? ? CA  G GLU 133 ? ? CB  G GLU 133 ? ? 99.32  110.60 -11.28 1.80 N 
30 1 NE  G ARG 143 ? ? CZ  G ARG 143 ? ? NH1 G ARG 143 ? ? 124.92 120.30 4.62   0.50 N 
31 1 NE  G ARG 143 ? ? CZ  G ARG 143 ? ? NH2 G ARG 143 ? ? 115.73 120.30 -4.57  0.50 N 
32 1 CD1 C TRP 32  ? ? CG  C TRP 32  ? ? CD2 C TRP 32  ? ? 111.85 106.30 5.55   0.80 N 
33 1 CE2 C TRP 32  ? ? CD2 C TRP 32  ? ? CG  C TRP 32  ? ? 101.58 107.30 -5.72  0.80 N 
34 1 NE  C ARG 79  ? ? CZ  C ARG 79  ? ? NH1 C ARG 79  ? ? 127.66 120.30 7.36   0.50 N 
35 1 NE  C ARG 79  ? ? CZ  C ARG 79  ? ? NH2 C ARG 79  ? ? 116.32 120.30 -3.98  0.50 N 
36 1 CB  C ASP 83  ? ? CG  C ASP 83  ? ? OD1 C ASP 83  ? ? 125.72 118.30 7.42   0.90 N 
37 1 CB  C ASP 83  ? ? CG  C ASP 83  ? ? OD2 C ASP 83  ? ? 111.90 118.30 -6.40  0.90 N 
38 1 CG1 C VAL 118 ? ? CB  C VAL 118 ? ? CG2 C VAL 118 ? ? 100.70 110.90 -10.20 1.60 N 
39 1 CD1 H TRP 32  ? ? CG  H TRP 32  ? ? CD2 H TRP 32  ? ? 113.10 106.30 6.80   0.80 N 
40 1 CB  H TRP 32  ? ? CG  H TRP 32  ? ? CD1 H TRP 32  ? ? 118.06 127.00 -8.94  1.30 N 
41 1 CE2 H TRP 32  ? ? CD2 H TRP 32  ? ? CG  H TRP 32  ? ? 101.37 107.30 -5.93  0.80 N 
42 1 CG  H TRP 32  ? ? CD2 H TRP 32  ? ? CE3 H TRP 32  ? ? 140.46 133.90 6.56   0.90 N 
43 1 NE  H ARG 79  ? ? CZ  H ARG 79  ? ? NH1 H ARG 79  ? ? 126.89 120.30 6.59   0.50 N 
44 1 NE  H ARG 79  ? ? CZ  H ARG 79  ? ? NH2 H ARG 79  ? ? 115.54 120.30 -4.76  0.50 N 
45 1 CD1 D TRP 32  ? ? CG  D TRP 32  ? ? CD2 D TRP 32  ? ? 111.52 106.30 5.22   0.80 N 
46 1 CE2 D TRP 32  ? ? CD2 D TRP 32  ? ? CG  D TRP 32  ? ? 102.23 107.30 -5.07  0.80 N 
47 1 NE  D ARG 69  ? ? CZ  D ARG 69  ? ? NH1 D ARG 69  ? ? 126.49 120.30 6.19   0.50 N 
48 1 NE  D ARG 69  ? ? CZ  D ARG 69  ? ? NH2 D ARG 69  ? ? 114.18 120.30 -6.12  0.50 N 
49 1 NE  D ARG 115 ? ? CZ  D ARG 115 ? ? NH1 D ARG 115 ? ? 123.85 120.30 3.55   0.50 N 
50 1 CA  I LYS 30  ? ? CB  I LYS 30  ? ? CG  I LYS 30  ? ? 128.40 113.40 15.00  2.20 N 
51 1 CD1 I TRP 32  ? ? CG  I TRP 32  ? ? CD2 I TRP 32  ? ? 111.96 106.30 5.66   0.80 N 
52 1 CB  I TRP 32  ? ? CG  I TRP 32  ? ? CD1 I TRP 32  ? ? 118.43 127.00 -8.57  1.30 N 
53 1 CE2 I TRP 32  ? ? CD2 I TRP 32  ? ? CG  I TRP 32  ? ? 101.86 107.30 -5.44  0.80 N 
54 1 CG  I TRP 32  ? ? CD2 I TRP 32  ? ? CE3 I TRP 32  ? ? 140.59 133.90 6.69   0.90 N 
55 1 NE  I ARG 69  ? ? CZ  I ARG 69  ? ? NH2 I ARG 69  ? ? 117.03 120.30 -3.27  0.50 N 
56 1 NE  I ARG 79  ? ? CZ  I ARG 79  ? ? NH1 I ARG 79  ? ? 125.19 120.30 4.89   0.50 N 
57 1 NE  I ARG 115 ? ? CZ  I ARG 115 ? ? NH1 I ARG 115 ? ? 125.23 120.30 4.93   0.50 N 
58 1 NE  I ARG 115 ? ? CZ  I ARG 115 ? ? NH2 I ARG 115 ? ? 117.20 120.30 -3.10  0.50 N 
59 1 CD1 E TRP 32  ? ? CG  E TRP 32  ? ? CD2 E TRP 32  ? ? 113.59 106.30 7.29   0.80 N 
60 1 CG  E TRP 32  ? ? CD1 E TRP 32  ? ? NE1 E TRP 32  ? ? 103.76 110.10 -6.34  1.00 N 
61 1 CE2 E TRP 32  ? ? CD2 E TRP 32  ? ? CG  E TRP 32  ? ? 101.94 107.30 -5.36  0.80 N 
62 1 CB  E ASN 53  ? ? CG  E ASN 53  ? ? ND2 E ASN 53  ? ? 132.24 116.70 15.54  2.40 N 
63 1 NE  E ARG 69  ? ? CZ  E ARG 69  ? ? NH1 E ARG 69  ? ? 124.62 120.30 4.32   0.50 N 
64 1 CB  E ASP 83  ? ? CG  E ASP 83  ? ? OD1 E ASP 83  ? ? 124.07 118.30 5.77   0.90 N 
65 1 CG1 E VAL 97  ? ? CB  E VAL 97  ? ? CG2 E VAL 97  ? ? 99.98  110.90 -10.92 1.60 N 
66 1 CG1 E VAL 103 ? ? CB  E VAL 103 ? ? CG2 E VAL 103 ? ? 98.27  110.90 -12.63 1.60 N 
67 1 NE  E ARG 143 ? ? CZ  E ARG 143 ? ? NH1 E ARG 143 ? ? 124.97 120.30 4.67   0.50 N 
68 1 CD1 J TRP 32  ? ? CG  J TRP 32  ? ? CD2 J TRP 32  ? ? 112.86 106.30 6.56   0.80 N 
69 1 CE2 J TRP 32  ? ? CD2 J TRP 32  ? ? CG  J TRP 32  ? ? 101.54 107.30 -5.76  0.80 N 
70 1 NE  J ARG 79  ? ? CZ  J ARG 79  ? ? NH1 J ARG 79  ? ? 127.68 120.30 7.38   0.50 N 
# 
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 ASP A 125 ? ? -77.18  21.64   
2  1 LEU A 126 ? ? 43.64   27.89   
3  1 ASN A 131 ? ? 171.47  160.58  
4  1 ASP F 90  ? ? -68.51  -170.32 
5  1 GLU B 40  ? ? -33.39  129.77  
6  1 ALA B 55  ? ? -86.62  31.63   
7  1 SER B 68  ? ? 32.01   61.29   
8  1 ARG B 69  ? ? -105.44 -169.34 
9  1 LYS B 128 ? ? -96.20  45.16   
10 1 ALA G 55  ? ? -90.98  36.94   
11 1 SER G 68  ? ? 39.56   58.93   
12 1 ARG G 69  ? ? -105.92 -167.82 
13 1 ASP C 90  ? ? -64.46  -172.95 
14 1 SER C 98  ? ? -158.02 89.33   
15 1 LYS C 136 ? ? -104.64 -61.23  
16 1 ASP H 92  ? ? -66.09  4.24    
17 1 ASP H 125 ? ? -87.51  31.97   
18 1 LEU H 126 ? ? 37.92   20.09   
19 1 SER D 25  ? ? -12.10  -36.41  
20 1 ASN D 26  ? ? -153.77 28.15   
21 1 ALA D 55  ? ? -94.26  47.76   
22 1 SER D 68  ? ? 29.96   70.67   
23 1 LYS D 91  ? ? -59.09  -5.56   
24 1 SER D 98  ? ? -165.27 107.33  
25 1 LEU D 126 ? ? 48.97   19.65   
26 1 ASN D 131 ? ? 175.47  162.38  
27 1 ALA I 55  ? ? -112.08 50.27   
28 1 ASN I 65  ? ? -150.75 69.08   
29 1 ASP I 90  ? ? -73.74  -167.40 
30 1 LYS I 136 ? ? -107.68 -60.14  
31 1 SER E 25  ? ? -30.57  -34.85  
32 1 PHE E 64  ? ? -57.16  109.59  
33 1 SER E 68  ? ? 40.12   73.34   
34 1 ASP E 90  ? ? -59.97  176.85  
35 1 VAL E 103 ? ? -148.87 -45.27  
36 1 LYS E 128 ? ? -72.40  36.83   
37 1 LYS E 136 ? ? -102.71 -76.64  
38 1 GLU J 24  ? ? 158.05  123.31  
39 1 SER J 25  ? ? -25.33  -25.78  
40 1 ASN J 26  ? ? -159.01 44.64   
41 1 ASN J 53  ? ? -105.81 61.99   
42 1 ALA J 55  ? ? -102.67 49.21   
43 1 SER J 59  ? ? -67.96  6.62    
44 1 ASP J 92  ? ? -103.74 64.75   
45 1 VAL J 103 ? ? -148.82 -32.72  
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   GLY 
_pdbx_validate_peptide_omega.auth_asym_id_1   D 
_pdbx_validate_peptide_omega.auth_seq_id_1    12 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   PRO 
_pdbx_validate_peptide_omega.auth_asym_id_2   D 
_pdbx_validate_peptide_omega.auth_seq_id_2    13 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            -129.84 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'COPPER (II) ION' CU  
3 'ZINC ION'        ZN  
4 'SULFATE ION'     SO4 
5 water             HOH 
# 
