data_1MOL
# 
_entry.id   1MOL 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.279 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   1MOL         
WWPDB D_1000175101 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        1MOL 
_pdbx_database_status.recvd_initial_deposition_date   1993-04-27 
_pdbx_database_status.deposit_site                    ? 
_pdbx_database_status.process_site                    ? 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_cs                  ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Somoza, J.R.' 1 
'Kim, S.-H.'   2 
# 
loop_
_citation.id 
_citation.title 
_citation.journal_abbrev 
_citation.journal_volume 
_citation.page_first 
_citation.page_last 
_citation.year 
_citation.journal_id_ASTM 
_citation.country 
_citation.journal_id_ISSN 
_citation.journal_id_CSD 
_citation.book_publisher 
_citation.pdbx_database_id_PubMed 
_citation.pdbx_database_id_DOI 
primary 
;Two crystal structures of a potently sweet protein. Natural monellin at 2.75 A resolution and single-chain monellin at 1.7 A resolution.
;
J.Mol.Biol.    234 390 404 1993 JMOBAK UK 0022-2836 0070 ? 8230222 10.1006/jmbi.1993.1594 
1       
'1H Resonance Assignments, Secondary Structure and General Topology of Single-Chain Monellin in Solution as Determined by 1H-2D-NMR' 
J.Biomol.NMR   2   557 ?   1992 JBNME9 NE 0925-2738 0800 ? ?       ?                      
2       'Redesigning a Sweet Protein: Increased Stability and Renaturability' 'Protein Eng.' 2   571 ?   1989 PRENE9 UK 0269-2139 
0859 ? ?       ?                      
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Somoza, J.R.' 1  
primary 'Jiang, F.'    2  
primary 'Tong, L.'     3  
primary 'Kang, C.H.'   4  
primary 'Cho, J.M.'    5  
primary 'Kim, S.H.'    6  
1       'Tomic, M.T.'  7  
1       'Somoza, J.R.' 8  
1       'Wemmer, D.E.' 9  
1       'Park, Y.W.'   10 
1       'Cho, J.M.'    11 
1       'Kim, S.-H.'   12 
2       'Kim, S.-H.'   13 
2       'Kang, C.-H.'  14 
2       'Kim, R.'      15 
2       'Cho, J.M.'    16 
2       'Lee, Y.-B.'   17 
2       'Lee, T.-K.'   18 
# 
_cell.entry_id           1MOL 
_cell.length_a           46.360 
_cell.length_b           49.090 
_cell.length_c           40.720 
_cell.angle_alpha        90.00 
_cell.angle_beta         102.86 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         1MOL 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
# 
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 MONELLIN 11083.628 2   ? ? ? ? 
2 water   nat water    18.015    134 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GEWEIIDIGPFTQNLGKFAVDEENKIGQYGRLTFNKVIRPCMKKTIYENEREIKGYEYQLYVYASDKLFRADISEDYKTR
GRKLLRFNGPVPPP
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GEWEIIDIGPFTQNLGKFAVDEENKIGQYGRLTFNKVIRPCMKKTIYENEREIKGYEYQLYVYASDKLFRADISEDYKTR
GRKLLRFNGPVPPP
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1  GLY n 
1 2  GLU n 
1 3  TRP n 
1 4  GLU n 
1 5  ILE n 
1 6  ILE n 
1 7  ASP n 
1 8  ILE n 
1 9  GLY n 
1 10 PRO n 
1 11 PHE n 
1 12 THR n 
1 13 GLN n 
1 14 ASN n 
1 15 LEU n 
1 16 GLY n 
1 17 LYS n 
1 18 PHE n 
1 19 ALA n 
1 20 VAL n 
1 21 ASP n 
1 22 GLU n 
1 23 GLU n 
1 24 ASN n 
1 25 LYS n 
1 26 ILE n 
1 27 GLY n 
1 28 GLN n 
1 29 TYR n 
1 30 GLY n 
1 31 ARG n 
1 32 LEU n 
1 33 THR n 
1 34 PHE n 
1 35 ASN n 
1 36 LYS n 
1 37 VAL n 
1 38 ILE n 
1 39 ARG n 
1 40 PRO n 
1 41 CYS n 
1 42 MET n 
1 43 LYS n 
1 44 LYS n 
1 45 THR n 
1 46 ILE n 
1 47 TYR n 
1 48 GLU n 
1 49 ASN n 
1 50 GLU n 
1 51 ARG n 
1 52 GLU n 
1 53 ILE n 
1 54 LYS n 
1 55 GLY n 
1 56 TYR n 
1 57 GLU n 
1 58 TYR n 
1 59 GLN n 
1 60 LEU n 
1 61 TYR n 
1 62 VAL n 
1 63 TYR n 
1 64 ALA n 
1 65 SER n 
1 66 ASP n 
1 67 LYS n 
1 68 LEU n 
1 69 PHE n 
1 70 ARG n 
1 71 ALA n 
1 72 ASP n 
1 73 ILE n 
1 74 SER n 
1 75 GLU n 
1 76 ASP n 
1 77 TYR n 
1 78 LYS n 
1 79 THR n 
1 80 ARG n 
1 81 GLY n 
1 82 ARG n 
1 83 LYS n 
1 84 LEU n 
1 85 LEU n 
1 86 ARG n 
1 87 PHE n 
1 88 ASN n 
1 89 GLY n 
1 90 PRO n 
1 91 VAL n 
1 92 PRO n 
1 93 PRO n 
1 94 PRO 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               'serendipity berry' 
_entity_src_gen.gene_src_genus                     Dioscoreophyllum 
_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      'Dioscoreophyllum cumminsii' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     3457 
_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                    MONB_DIOCU 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_db_accession          P02882 
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_seq_one_letter_code   
;MGEWEIIDIGPFTQNLGKFAVDEENKIGQYGRLTFNKVIRPCMTIYENEREIKGYEYQLYVYASDKLFRADISEDYKTRG
RKLLRFNGPVPPP
;
_struct_ref.pdbx_db_isoform            ? 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 1MOL A 1 ? 94 ? P02882 2 ? 93 ? 1 94 
2 1 1MOL B 1 ? 94 ? P02882 2 ? 93 ? 1 94 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 1MOL LYS A 43 ? UNP P02882 ? ? INSERTION 43 1 
1 1MOL LYS A 44 ? UNP P02882 ? ? INSERTION 44 2 
2 1MOL LYS B 43 ? UNP P02882 ? ? INSERTION 43 3 
2 1MOL LYS B 44 ? UNP P02882 ? ? INSERTION 44 4 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
_exptl.entry_id          1MOL 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   ? 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.04 
_exptl_crystal.density_percent_sol   39.61 
_exptl_crystal.description           ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           ? 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_diffrn_protocol             ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   . 
_diffrn_radiation_wavelength.wt           1.0 
# 
_refine.entry_id                                 1MOL 
_refine.ls_number_reflns_obs                     15053 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          2.0 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             6.0 
_refine.ls_d_res_high                            1.7 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_R_factor_obs                          0.1740000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1740000 
_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        1566 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.number_atoms_solvent             134 
_refine_hist.number_atoms_total               1700 
_refine_hist.d_res_high                       1.7 
_refine_hist.d_res_low                        6.0 
# 
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                0.015 ? ? ? 'X-RAY DIFFRACTION' ? 
x_bond_d_na             ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_bond_d_prot           ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_angle_d               ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_angle_d_na            ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_angle_d_prot          ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_angle_deg             2.86  ? ? ? 'X-RAY DIFFRACTION' ? 
x_angle_deg_na          ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_angle_deg_prot        ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_dihedral_angle_d      ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_dihedral_angle_d_na   ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_dihedral_angle_d_prot ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_improper_angle_d      ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_improper_angle_d_na   ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_improper_angle_d_prot ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_mcbond_it             ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_mcangle_it            ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_scbond_it             ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_scangle_it            ?     ? ? ? 'X-RAY DIFFRACTION' ? 
# 
_struct.entry_id                  1MOL 
_struct.title                     
;TWO CRYSTAL STRUCTURES OF A POTENTLY SWEET PROTEIN: NATURAL MONELLIN AT 2.75 ANGSTROMS RESOLUTION AND SINGLE-CHAIN MONELLIN AT 1.7 ANGSTROMS RESOLUTION
;
_struct.pdbx_descriptor           'MONELLIN (SINGLE-CHAIN, FUSED)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        1MOL 
_struct_keywords.pdbx_keywords   'SWEET-TASTING PROTEIN' 
_struct_keywords.text            'SWEET-TASTING PROTEIN' 
# 
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 2 ? 
D N N 2 ? 
# 
loop_
_struct_biol.id 
1 
2 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 1 PRO A 10 ? ILE A 26 ? PRO A 10 ILE A 26 1 ? 17 
HELX_P HELX_P2 2 PRO B 10 ? ILE B 26 ? PRO B 10 ILE B 26 1 ? 17 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 ARG 39 A . ? ARG 39 A PRO 40 A ? PRO 40 A 1 -5.58 
2 GLY 89 A . ? GLY 89 A PRO 90 A ? PRO 90 A 1 -5.46 
3 ARG 39 B . ? ARG 39 B PRO 40 B ? PRO 40 B 1 -7.27 
4 GLY 89 B . ? GLY 89 B PRO 90 B ? PRO 90 B 1 -5.88 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
S1 ? 5 ? 
S2 ? 5 ? 
# 
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 
S1 1 2 ? anti-parallel 
S1 2 3 ? anti-parallel 
S1 3 4 ? anti-parallel 
S1 4 5 ? anti-parallel 
S2 1 2 ? anti-parallel 
S2 2 3 ? anti-parallel 
S2 3 4 ? anti-parallel 
S2 4 5 ? 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 
S1 1 GLU A 2  ? ILE A 6  ? GLU A 2  ILE A 6  
S1 2 PHE A 34 ? GLU A 48 ? PHE A 34 GLU A 48 
S1 3 GLU A 52 ? ALA A 64 ? GLU A 52 ALA A 64 
S1 4 LYS A 67 ? ASP A 76 ? LYS A 67 ASP A 76 
S1 5 ARG A 82 ? ASN A 88 ? ARG A 82 ASN A 88 
S2 1 GLU B 2  ? ILE B 6  ? GLU B 2  ILE B 6  
S2 2 PHE B 34 ? GLU B 48 ? PHE B 34 GLU B 48 
S2 3 GLU B 52 ? ALA B 64 ? GLU B 52 ALA B 64 
S2 4 LYS B 67 ? ASP B 76 ? LYS B 67 ASP B 76 
S2 5 ARG B 82 ? ASN B 88 ? ARG B 82 ASN B 88 
# 
_database_PDB_matrix.entry_id          1MOL 
_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                    1MOL 
_atom_sites.fract_transf_matrix[1][1]   0.021570 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.004924 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.020371 
_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]   0.025190 
_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_sites_footnote.id 
_atom_sites_footnote.text 
1 'CIS PROLINE - PRO A    40' 
2 'CIS PROLINE - PRO A    90' 
3 'CIS PROLINE - PRO B    40' 
4 'CIS PROLINE - PRO B    90' 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . GLY A 1 1  ? 3.780   61.802 -46.579 1.00 30.39 ? 1   GLY A N   1 
ATOM   2    C CA  . GLY A 1 1  ? 4.499   62.177 -47.774 1.00 23.64 ? 1   GLY A CA  1 
ATOM   3    C C   . GLY A 1 1  ? 3.485   62.378 -48.884 1.00 23.28 ? 1   GLY A C   1 
ATOM   4    O O   . GLY A 1 1  ? 2.281   62.491 -48.646 1.00 23.51 ? 1   GLY A O   1 
ATOM   5    N N   . GLU A 1 2  ? 3.963   62.400 -50.103 1.00 20.96 ? 2   GLU A N   1 
ATOM   6    C CA  . GLU A 1 2  ? 3.188   62.567 -51.311 1.00 19.49 ? 2   GLU A CA  1 
ATOM   7    C C   . GLU A 1 2  ? 3.337   61.226 -51.970 1.00 15.95 ? 2   GLU A C   1 
ATOM   8    O O   . GLU A 1 2  ? 4.430   60.653 -51.909 1.00 15.58 ? 2   GLU A O   1 
ATOM   9    C CB  . GLU A 1 2  ? 3.836   63.651 -52.111 1.00 20.12 ? 2   GLU A CB  1 
ATOM   10   C CG  . GLU A 1 2  ? 3.537   63.743 -53.577 1.00 31.19 ? 2   GLU A CG  1 
ATOM   11   C CD  . GLU A 1 2  ? 4.546   64.682 -54.200 1.00 37.64 ? 2   GLU A CD  1 
ATOM   12   O OE1 . GLU A 1 2  ? 4.702   65.793 -53.676 1.00 40.00 ? 2   GLU A OE1 1 
ATOM   13   O OE2 . GLU A 1 2  ? 5.186   64.276 -55.178 1.00 43.30 ? 2   GLU A OE2 1 
ATOM   14   N N   . TRP A 1 3  ? 2.314   60.742 -52.650 1.00 15.91 ? 3   TRP A N   1 
ATOM   15   C CA  . TRP A 1 3  ? 2.343   59.382 -53.137 1.00 15.04 ? 3   TRP A CA  1 
ATOM   16   C C   . TRP A 1 3  ? 2.008   59.416 -54.604 1.00 14.61 ? 3   TRP A C   1 
ATOM   17   O O   . TRP A 1 3  ? 1.206   60.264 -55.031 1.00 15.24 ? 3   TRP A O   1 
ATOM   18   C CB  . TRP A 1 3  ? 1.311   58.561 -52.348 1.00 11.81 ? 3   TRP A CB  1 
ATOM   19   C CG  . TRP A 1 3  ? 1.725   58.292 -50.913 1.00 15.22 ? 3   TRP A CG  1 
ATOM   20   C CD1 . TRP A 1 3  ? 1.434   59.118 -49.833 1.00 16.88 ? 3   TRP A CD1 1 
ATOM   21   C CD2 . TRP A 1 3  ? 2.366   57.154 -50.535 1.00 16.32 ? 3   TRP A CD2 1 
ATOM   22   N NE1 . TRP A 1 3  ? 1.863   58.479 -48.772 1.00 18.42 ? 3   TRP A NE1 1 
ATOM   23   C CE2 . TRP A 1 3  ? 2.423   57.303 -49.152 1.00 19.95 ? 3   TRP A CE2 1 
ATOM   24   C CE3 . TRP A 1 3  ? 2.832   56.036 -51.208 1.00 20.53 ? 3   TRP A CE3 1 
ATOM   25   C CZ2 . TRP A 1 3  ? 2.980   56.288 -48.404 1.00 22.10 ? 3   TRP A CZ2 1 
ATOM   26   C CZ3 . TRP A 1 3  ? 3.402   55.030 -50.445 1.00 23.28 ? 3   TRP A CZ3 1 
ATOM   27   C CH2 . TRP A 1 3  ? 3.468   55.165 -49.060 1.00 25.02 ? 3   TRP A CH2 1 
ATOM   28   N N   . GLU A 1 4  ? 2.629   58.534 -55.381 1.00 13.47 ? 4   GLU A N   1 
ATOM   29   C CA  . GLU A 1 4  ? 2.329   58.383 -56.800 1.00 13.75 ? 4   GLU A CA  1 
ATOM   30   C C   . GLU A 1 4  ? 2.629   56.949 -57.259 1.00 14.94 ? 4   GLU A C   1 
ATOM   31   O O   . GLU A 1 4  ? 3.367   56.186 -56.608 1.00 13.18 ? 4   GLU A O   1 
ATOM   32   C CB  . GLU A 1 4  ? 3.142   59.334 -57.661 1.00 11.74 ? 4   GLU A CB  1 
ATOM   33   C CG  . GLU A 1 4  ? 4.622   59.006 -57.738 1.00 16.04 ? 4   GLU A CG  1 
ATOM   34   C CD  . GLU A 1 4  ? 5.426   60.158 -58.311 1.00 18.88 ? 4   GLU A CD  1 
ATOM   35   O OE1 . GLU A 1 4  ? 5.379   60.397 -59.506 1.00 22.07 ? 4   GLU A OE1 1 
ATOM   36   O OE2 . GLU A 1 4  ? 6.103   60.821 -57.548 1.00 21.00 ? 4   GLU A OE2 1 
ATOM   37   N N   . ILE A 1 5  ? 1.980   56.516 -58.336 1.00 16.06 ? 5   ILE A N   1 
ATOM   38   C CA  . ILE A 1 5  ? 2.294   55.208 -58.883 1.00 17.48 ? 5   ILE A CA  1 
ATOM   39   C C   . ILE A 1 5  ? 3.313   55.447 -59.977 1.00 16.72 ? 5   ILE A C   1 
ATOM   40   O O   . ILE A 1 5  ? 3.254   56.454 -60.697 1.00 16.80 ? 5   ILE A O   1 
ATOM   41   C CB  . ILE A 1 5  ? 0.995   54.537 -59.426 1.00 17.96 ? 5   ILE A CB  1 
ATOM   42   C CG1 . ILE A 1 5  ? 0.097   54.208 -58.241 1.00 19.88 ? 5   ILE A CG1 1 
ATOM   43   C CG2 . ILE A 1 5  ? 1.293   53.219 -60.155 1.00 13.83 ? 5   ILE A CG2 1 
ATOM   44   C CD1 . ILE A 1 5  ? -1.373  54.255 -58.665 1.00 24.08 ? 5   ILE A CD1 1 
ATOM   45   N N   . ILE A 1 6  ? 4.266   54.553 -60.089 1.00 15.35 ? 6   ILE A N   1 
ATOM   46   C CA  . ILE A 1 6  ? 5.301   54.661 -61.117 1.00 18.06 ? 6   ILE A CA  1 
ATOM   47   C C   . ILE A 1 6  ? 5.268   53.388 -61.983 1.00 18.17 ? 6   ILE A C   1 
ATOM   48   O O   . ILE A 1 6  ? 4.594   52.474 -61.491 1.00 18.74 ? 6   ILE A O   1 
ATOM   49   C CB  . ILE A 1 6  ? 6.710   54.873 -60.411 1.00 16.63 ? 6   ILE A CB  1 
ATOM   50   C CG1 . ILE A 1 6  ? 7.089   53.774 -59.384 1.00 16.16 ? 6   ILE A CG1 1 
ATOM   51   C CG2 . ILE A 1 6  ? 6.632   56.270 -59.744 1.00 15.06 ? 6   ILE A CG2 1 
ATOM   52   C CD1 . ILE A 1 6  ? 8.586   53.743 -58.959 1.00 12.29 ? 6   ILE A CD1 1 
ATOM   53   N N   . ASP A 1 7  ? 5.836   53.171 -63.197 1.00 20.39 ? 7   ASP A N   1 
ATOM   54   C CA  . ASP A 1 7  ? 5.583   51.845 -63.775 1.00 25.98 ? 7   ASP A CA  1 
ATOM   55   C C   . ASP A 1 7  ? 6.740   50.911 -63.425 1.00 23.52 ? 7   ASP A C   1 
ATOM   56   O O   . ASP A 1 7  ? 7.625   51.222 -62.630 1.00 23.33 ? 7   ASP A O   1 
ATOM   57   C CB  . ASP A 1 7  ? 5.339   51.833 -65.346 1.00 34.55 ? 7   ASP A CB  1 
ATOM   58   C CG  . ASP A 1 7  ? 4.573   50.584 -65.986 1.00 39.53 ? 7   ASP A CG  1 
ATOM   59   O OD1 . ASP A 1 7  ? 3.345   50.430 -65.835 1.00 39.06 ? 7   ASP A OD1 1 
ATOM   60   O OD2 . ASP A 1 7  ? 5.226   49.751 -66.645 1.00 40.75 ? 7   ASP A OD2 1 
ATOM   61   N N   . ILE A 1 8  ? 6.650   49.688 -63.916 1.00 23.73 ? 8   ILE A N   1 
ATOM   62   C CA  . ILE A 1 8  ? 7.508   48.608 -63.529 1.00 22.45 ? 8   ILE A CA  1 
ATOM   63   C C   . ILE A 1 8  ? 8.582   48.272 -64.551 1.00 21.61 ? 8   ILE A C   1 
ATOM   64   O O   . ILE A 1 8  ? 8.965   47.106 -64.748 1.00 21.36 ? 8   ILE A O   1 
ATOM   65   C CB  . ILE A 1 8  ? 6.577   47.407 -63.217 1.00 24.34 ? 8   ILE A CB  1 
ATOM   66   C CG1 . ILE A 1 8  ? 5.772   47.051 -64.452 1.00 24.98 ? 8   ILE A CG1 1 
ATOM   67   C CG2 . ILE A 1 8  ? 5.700   47.757 -61.987 1.00 22.75 ? 8   ILE A CG2 1 
ATOM   68   C CD1 . ILE A 1 8  ? 5.077   45.657 -64.361 1.00 29.22 ? 8   ILE A CD1 1 
ATOM   69   N N   . GLY A 1 9  ? 9.107   49.330 -65.165 1.00 16.55 ? 9   GLY A N   1 
ATOM   70   C CA  . GLY A 1 9  ? 10.207  49.151 -66.101 1.00 13.40 ? 9   GLY A CA  1 
ATOM   71   C C   . GLY A 1 9  ? 11.561  48.922 -65.403 1.00 13.85 ? 9   GLY A C   1 
ATOM   72   O O   . GLY A 1 9  ? 11.629  48.610 -64.191 1.00 11.81 ? 9   GLY A O   1 
ATOM   73   N N   . PRO A 1 10 ? 12.672  49.098 -66.121 1.00 13.31 ? 10  PRO A N   1 
ATOM   74   C CA  . PRO A 1 10 ? 14.033  48.782 -65.649 1.00 12.46 ? 10  PRO A CA  1 
ATOM   75   C C   . PRO A 1 10 ? 14.380  49.364 -64.272 1.00 12.23 ? 10  PRO A C   1 
ATOM   76   O O   . PRO A 1 10 ? 14.909  48.634 -63.429 1.00 10.49 ? 10  PRO A O   1 
ATOM   77   C CB  . PRO A 1 10 ? 14.942  49.295 -66.736 1.00 12.06 ? 10  PRO A CB  1 
ATOM   78   C CG  . PRO A 1 10 ? 14.059  49.172 -67.957 1.00 15.24 ? 10  PRO A CG  1 
ATOM   79   C CD  . PRO A 1 10 ? 12.696  49.653 -67.477 1.00 13.12 ? 10  PRO A CD  1 
ATOM   80   N N   . PHE A 1 11 ? 14.044  50.644 -63.963 1.00 10.95 ? 11  PHE A N   1 
ATOM   81   C CA  . PHE A 1 11 ? 14.336  51.230 -62.666 1.00 12.99 ? 11  PHE A CA  1 
ATOM   82   C C   . PHE A 1 11 ? 13.695  50.399 -61.556 1.00 13.05 ? 11  PHE A C   1 
ATOM   83   O O   . PHE A 1 11 ? 14.348  50.021 -60.576 1.00 10.78 ? 11  PHE A O   1 
ATOM   84   C CB  . PHE A 1 11 ? 13.804  52.686 -62.614 1.00 13.50 ? 11  PHE A CB  1 
ATOM   85   C CG  . PHE A 1 11 ? 14.026  53.367 -61.260 1.00 14.91 ? 11  PHE A CG  1 
ATOM   86   C CD1 . PHE A 1 11 ? 15.305  53.797 -60.904 1.00 16.06 ? 11  PHE A CD1 1 
ATOM   87   C CD2 . PHE A 1 11 ? 12.967  53.562 -60.375 1.00 16.77 ? 11  PHE A CD2 1 
ATOM   88   C CE1 . PHE A 1 11 ? 15.513  54.410 -59.665 1.00 14.72 ? 11  PHE A CE1 1 
ATOM   89   C CE2 . PHE A 1 11 ? 13.184  54.182 -59.135 1.00 18.20 ? 11  PHE A CE2 1 
ATOM   90   C CZ  . PHE A 1 11 ? 14.460  54.604 -58.770 1.00 14.61 ? 11  PHE A CZ  1 
ATOM   91   N N   . THR A 1 12 ? 12.450  49.995 -61.752 1.00 9.19  ? 12  THR A N   1 
ATOM   92   C CA  . THR A 1 12 ? 11.726  49.340 -60.679 1.00 10.93 ? 12  THR A CA  1 
ATOM   93   C C   . THR A 1 12 ? 12.191  47.885 -60.580 1.00 10.19 ? 12  THR A C   1 
ATOM   94   O O   . THR A 1 12 ? 12.229  47.310 -59.477 1.00 10.62 ? 12  THR A O   1 
ATOM   95   C CB  . THR A 1 12 ? 10.194  49.477 -60.976 1.00 14.06 ? 12  THR A CB  1 
ATOM   96   O OG1 . THR A 1 12 ? 9.873   50.877 -60.896 1.00 16.17 ? 12  THR A OG1 1 
ATOM   97   C CG2 . THR A 1 12 ? 9.321   48.747 -60.004 1.00 16.28 ? 12  THR A CG2 1 
ATOM   98   N N   . GLN A 1 13 ? 12.563  47.307 -61.726 1.00 10.79 ? 13  GLN A N   1 
ATOM   99   C CA  . GLN A 1 13 ? 13.098  45.932 -61.774 1.00 11.60 ? 13  GLN A CA  1 
ATOM   100  C C   . GLN A 1 13 ? 14.371  45.872 -60.936 1.00 10.09 ? 13  GLN A C   1 
ATOM   101  O O   . GLN A 1 13 ? 14.532  44.960 -60.136 1.00 10.87 ? 13  GLN A O   1 
ATOM   102  C CB  . GLN A 1 13 ? 13.468  45.519 -63.188 1.00 13.11 ? 13  GLN A CB  1 
ATOM   103  C CG  . GLN A 1 13 ? 12.170  45.285 -63.933 1.00 16.77 ? 13  GLN A CG  1 
ATOM   104  C CD  . GLN A 1 13 ? 12.247  45.151 -65.448 1.00 19.21 ? 13  GLN A CD  1 
ATOM   105  O OE1 . GLN A 1 13 ? 13.295  44.868 -66.057 1.00 16.34 ? 13  GLN A OE1 1 
ATOM   106  N NE2 . GLN A 1 13 ? 11.060  45.392 -66.036 1.00 18.88 ? 13  GLN A NE2 1 
ATOM   107  N N   . ASN A 1 14 ? 15.233  46.896 -61.043 1.00 9.97  ? 14  ASN A N   1 
ATOM   108  C CA  . ASN A 1 14 ? 16.477  46.946 -60.264 1.00 10.90 ? 14  ASN A CA  1 
ATOM   109  C C   . ASN A 1 14 ? 16.235  47.199 -58.815 1.00 10.08 ? 14  ASN A C   1 
ATOM   110  O O   . ASN A 1 14 ? 16.995  46.699 -57.994 1.00 9.71  ? 14  ASN A O   1 
ATOM   111  C CB  . ASN A 1 14 ? 17.400  48.000 -60.818 1.00 10.43 ? 14  ASN A CB  1 
ATOM   112  C CG  . ASN A 1 14 ? 17.944  47.501 -62.158 1.00 14.30 ? 14  ASN A CG  1 
ATOM   113  O OD1 . ASN A 1 14 ? 18.175  46.301 -62.358 1.00 14.55 ? 14  ASN A OD1 1 
ATOM   114  N ND2 . ASN A 1 14 ? 18.218  48.324 -63.144 1.00 15.54 ? 14  ASN A ND2 1 
ATOM   115  N N   . LEU A 1 15 ? 15.148  47.898 -58.436 1.00 8.89  ? 15  LEU A N   1 
ATOM   116  C CA  . LEU A 1 15 ? 14.754  48.019 -57.045 1.00 8.92  ? 15  LEU A CA  1 
ATOM   117  C C   . LEU A 1 15 ? 14.278  46.662 -56.529 1.00 7.39  ? 15  LEU A C   1 
ATOM   118  O O   . LEU A 1 15 ? 14.580  46.334 -55.383 1.00 7.81  ? 15  LEU A O   1 
ATOM   119  C CB  . LEU A 1 15 ? 13.589  49.036 -56.868 1.00 12.41 ? 15  LEU A CB  1 
ATOM   120  C CG  . LEU A 1 15 ? 13.980  50.517 -56.960 1.00 12.04 ? 15  LEU A CG  1 
ATOM   121  C CD1 . LEU A 1 15 ? 12.705  51.354 -57.085 1.00 12.25 ? 15  LEU A CD1 1 
ATOM   122  C CD2 . LEU A 1 15 ? 14.792  50.909 -55.741 1.00 10.68 ? 15  LEU A CD2 1 
ATOM   123  N N   . GLY A 1 16 ? 13.500  45.890 -57.300 1.00 9.17  ? 16  GLY A N   1 
ATOM   124  C CA  . GLY A 1 16 ? 13.069  44.536 -56.927 1.00 7.27  ? 16  GLY A CA  1 
ATOM   125  C C   . GLY A 1 16 ? 14.303  43.642 -56.683 1.00 10.10 ? 16  GLY A C   1 
ATOM   126  O O   . GLY A 1 16 ? 14.406  42.938 -55.655 1.00 8.55  ? 16  GLY A O   1 
ATOM   127  N N   . LYS A 1 17 ? 15.276  43.687 -57.607 1.00 8.25  ? 17  LYS A N   1 
ATOM   128  C CA  . LYS A 1 17 ? 16.501  42.913 -57.431 1.00 11.62 ? 17  LYS A CA  1 
ATOM   129  C C   . LYS A 1 17 ? 17.278  43.283 -56.173 1.00 12.26 ? 17  LYS A C   1 
ATOM   130  O O   . LYS A 1 17 ? 17.760  42.394 -55.437 1.00 13.75 ? 17  LYS A O   1 
ATOM   131  C CB  . LYS A 1 17 ? 17.411  43.085 -58.609 1.00 10.15 ? 17  LYS A CB  1 
ATOM   132  C CG  . LYS A 1 17 ? 16.948  42.418 -59.873 1.00 15.11 ? 17  LYS A CG  1 
ATOM   133  C CD  . LYS A 1 17 ? 18.027  42.638 -60.902 1.00 18.31 ? 17  LYS A CD  1 
ATOM   134  C CE  . LYS A 1 17 ? 17.561  41.995 -62.167 1.00 23.23 ? 17  LYS A CE  1 
ATOM   135  N NZ  . LYS A 1 17 ? 18.669  41.917 -63.096 1.00 22.83 ? 17  LYS A NZ  1 
ATOM   136  N N   . PHE A 1 18 ? 17.411  44.592 -55.876 1.00 11.64 ? 18  PHE A N   1 
ATOM   137  C CA  . PHE A 1 18 ? 18.018  45.119 -54.651 1.00 10.87 ? 18  PHE A CA  1 
ATOM   138  C C   . PHE A 1 18 ? 17.324  44.533 -53.409 1.00 11.48 ? 18  PHE A C   1 
ATOM   139  O O   . PHE A 1 18 ? 17.970  44.041 -52.475 1.00 10.63 ? 18  PHE A O   1 
ATOM   140  C CB  . PHE A 1 18 ? 17.913  46.708 -54.646 1.00 11.37 ? 18  PHE A CB  1 
ATOM   141  C CG  . PHE A 1 18 ? 18.337  47.304 -53.306 1.00 12.05 ? 18  PHE A CG  1 
ATOM   142  C CD1 . PHE A 1 18 ? 19.673  47.568 -53.050 1.00 11.12 ? 18  PHE A CD1 1 
ATOM   143  C CD2 . PHE A 1 18 ? 17.390  47.573 -52.324 1.00 10.56 ? 18  PHE A CD2 1 
ATOM   144  C CE1 . PHE A 1 18 ? 20.050  48.089 -51.803 1.00 9.94  ? 18  PHE A CE1 1 
ATOM   145  C CE2 . PHE A 1 18 ? 17.769  48.066 -51.071 1.00 13.40 ? 18  PHE A CE2 1 
ATOM   146  C CZ  . PHE A 1 18 ? 19.116  48.329 -50.800 1.00 12.31 ? 18  PHE A CZ  1 
ATOM   147  N N   . ALA A 1 19 ? 15.984  44.550 -53.358 1.00 9.65  ? 19  ALA A N   1 
ATOM   148  C CA  . ALA A 1 19 ? 15.233  43.987 -52.269 1.00 8.94  ? 19  ALA A CA  1 
ATOM   149  C C   . ALA A 1 19 ? 15.529  42.499 -52.069 1.00 9.15  ? 19  ALA A C   1 
ATOM   150  O O   . ALA A 1 19 ? 15.696  42.068 -50.912 1.00 11.14 ? 19  ALA A O   1 
ATOM   151  C CB  . ALA A 1 19 ? 13.705  44.178 -52.524 1.00 6.94  ? 19  ALA A CB  1 
ATOM   152  N N   . VAL A 1 20 ? 15.587  41.701 -53.126 1.00 9.52  ? 20  VAL A N   1 
ATOM   153  C CA  . VAL A 1 20 ? 15.858  40.268 -52.993 1.00 11.22 ? 20  VAL A CA  1 
ATOM   154  C C   . VAL A 1 20 ? 17.306  40.109 -52.510 1.00 12.22 ? 20  VAL A C   1 
ATOM   155  O O   . VAL A 1 20 ? 17.545  39.380 -51.546 1.00 11.28 ? 20  VAL A O   1 
ATOM   156  C CB  . VAL A 1 20 ? 15.618  39.559 -54.362 1.00 11.72 ? 20  VAL A CB  1 
ATOM   157  C CG1 . VAL A 1 20 ? 16.119  38.075 -54.359 1.00 11.60 ? 20  VAL A CG1 1 
ATOM   158  C CG2 . VAL A 1 20 ? 14.107  39.611 -54.628 1.00 8.83  ? 20  VAL A CG2 1 
ATOM   159  N N   . ASP A 1 21 ? 18.267  40.859 -53.065 1.00 10.70 ? 21  ASP A N   1 
ATOM   160  C CA  . ASP A 1 21 ? 19.628  40.772 -52.551 1.00 11.85 ? 21  ASP A CA  1 
ATOM   161  C C   . ASP A 1 21 ? 19.779  41.145 -51.087 1.00 10.03 ? 21  ASP A C   1 
ATOM   162  O O   . ASP A 1 21 ? 20.496  40.479 -50.331 1.00 11.90 ? 21  ASP A O   1 
ATOM   163  C CB  . ASP A 1 21 ? 20.494  41.667 -53.413 1.00 14.00 ? 21  ASP A CB  1 
ATOM   164  C CG  . ASP A 1 21 ? 20.794  41.126 -54.801 1.00 17.86 ? 21  ASP A CG  1 
ATOM   165  O OD1 . ASP A 1 21 ? 20.516  39.967 -55.127 1.00 19.16 ? 21  ASP A OD1 1 
ATOM   166  O OD2 . ASP A 1 21 ? 21.336  41.898 -55.576 1.00 19.63 ? 21  ASP A OD2 1 
ATOM   167  N N   . GLU A 1 22 ? 19.098  42.180 -50.628 1.00 10.95 ? 22  GLU A N   1 
ATOM   168  C CA  . GLU A 1 22 ? 19.121  42.567 -49.256 1.00 11.39 ? 22  GLU A CA  1 
ATOM   169  C C   . GLU A 1 22 ? 18.454  41.529 -48.370 1.00 13.81 ? 22  GLU A C   1 
ATOM   170  O O   . GLU A 1 22 ? 18.993  41.185 -47.311 1.00 13.57 ? 22  GLU A O   1 
ATOM   171  C CB  . GLU A 1 22 ? 18.448  43.922 -49.102 1.00 14.32 ? 22  GLU A CB  1 
ATOM   172  C CG  . GLU A 1 22 ? 19.312  45.101 -49.576 1.00 13.41 ? 22  GLU A CG  1 
ATOM   173  C CD  . GLU A 1 22 ? 20.665  45.166 -48.883 1.00 16.66 ? 22  GLU A CD  1 
ATOM   174  O OE1 . GLU A 1 22 ? 20.721  45.293 -47.671 1.00 17.39 ? 22  GLU A OE1 1 
ATOM   175  O OE2 . GLU A 1 22 ? 21.678  45.094 -49.561 1.00 19.44 ? 22  GLU A OE2 1 
ATOM   176  N N   . GLU A 1 23 ? 17.339  40.964 -48.799 1.00 11.76 ? 23  GLU A N   1 
ATOM   177  C CA  . GLU A 1 23 ? 16.651  39.958 -48.013 1.00 11.15 ? 23  GLU A CA  1 
ATOM   178  C C   . GLU A 1 23 ? 17.529  38.714 -47.964 1.00 10.92 ? 23  GLU A C   1 
ATOM   179  O O   . GLU A 1 23 ? 17.602  38.069 -46.923 1.00 13.44 ? 23  GLU A O   1 
ATOM   180  C CB  . GLU A 1 23 ? 15.282  39.618 -48.648 1.00 9.97  ? 23  GLU A CB  1 
ATOM   181  C CG  . GLU A 1 23 ? 14.486  38.592 -47.861 1.00 13.55 ? 23  GLU A CG  1 
ATOM   182  C CD  . GLU A 1 23 ? 14.259  38.931 -46.375 1.00 19.60 ? 23  GLU A CD  1 
ATOM   183  O OE1 . GLU A 1 23 ? 14.002  40.083 -45.986 1.00 18.08 ? 23  GLU A OE1 1 
ATOM   184  O OE2 . GLU A 1 23 ? 14.396  38.008 -45.572 1.00 26.73 ? 23  GLU A OE2 1 
ATOM   185  N N   . ASN A 1 24 ? 18.262  38.369 -49.001 1.00 12.81 ? 24  ASN A N   1 
ATOM   186  C CA  . ASN A 1 24 ? 19.130  37.198 -48.922 1.00 15.97 ? 24  ASN A CA  1 
ATOM   187  C C   . ASN A 1 24 ? 20.203  37.372 -47.870 1.00 18.19 ? 24  ASN A C   1 
ATOM   188  O O   . ASN A 1 24 ? 20.639  36.413 -47.250 1.00 19.15 ? 24  ASN A O   1 
ATOM   189  C CB  . ASN A 1 24 ? 19.826  36.925 -50.234 1.00 15.13 ? 24  ASN A CB  1 
ATOM   190  C CG  . ASN A 1 24 ? 18.912  36.124 -51.128 1.00 14.51 ? 24  ASN A CG  1 
ATOM   191  O OD1 . ASN A 1 24 ? 17.935  35.488 -50.708 1.00 15.85 ? 24  ASN A OD1 1 
ATOM   192  N ND2 . ASN A 1 24 ? 19.188  36.148 -52.405 1.00 13.57 ? 24  ASN A ND2 1 
ATOM   193  N N   . LYS A 1 25 ? 20.597  38.630 -47.598 1.00 18.30 ? 25  LYS A N   1 
ATOM   194  C CA  . LYS A 1 25 ? 21.584  38.853 -46.542 1.00 20.58 ? 25  LYS A CA  1 
ATOM   195  C C   . LYS A 1 25 ? 20.959  38.599 -45.183 1.00 20.81 ? 25  LYS A C   1 
ATOM   196  O O   . LYS A 1 25 ? 21.634  38.184 -44.243 1.00 22.04 ? 25  LYS A O   1 
ATOM   197  C CB  . LYS A 1 25 ? 22.114  40.289 -46.578 1.00 18.72 ? 25  LYS A CB  1 
ATOM   198  C CG  . LYS A 1 25 ? 22.875  40.687 -47.810 1.00 18.83 ? 25  LYS A CG  1 
ATOM   199  C CD  . LYS A 1 25 ? 23.254  42.076 -47.432 1.00 19.68 ? 25  LYS A CD  1 
ATOM   200  C CE  . LYS A 1 25 ? 23.882  42.781 -48.586 1.00 21.22 ? 25  LYS A CE  1 
ATOM   201  N NZ  . LYS A 1 25 ? 24.074  44.158 -48.164 1.00 22.86 ? 25  LYS A NZ  1 
ATOM   202  N N   . ILE A 1 26 ? 19.671  38.825 -45.058 1.00 20.30 ? 26  ILE A N   1 
ATOM   203  C CA  . ILE A 1 26 ? 18.969  38.617 -43.818 1.00 20.98 ? 26  ILE A CA  1 
ATOM   204  C C   . ILE A 1 26 ? 18.742  37.131 -43.586 1.00 23.35 ? 26  ILE A C   1 
ATOM   205  O O   . ILE A 1 26 ? 18.986  36.647 -42.483 1.00 26.53 ? 26  ILE A O   1 
ATOM   206  C CB  . ILE A 1 26 ? 17.712  39.443 -43.962 1.00 20.04 ? 26  ILE A CB  1 
ATOM   207  C CG1 . ILE A 1 26 ? 18.148  40.877 -43.777 1.00 19.95 ? 26  ILE A CG1 1 
ATOM   208  C CG2 . ILE A 1 26 ? 16.625  39.010 -43.007 1.00 24.09 ? 26  ILE A CG2 1 
ATOM   209  C CD1 . ILE A 1 26 ? 17.029  41.875 -44.024 1.00 21.90 ? 26  ILE A CD1 1 
ATOM   210  N N   . GLY A 1 27 ? 18.237  36.396 -44.566 1.00 22.80 ? 27  GLY A N   1 
ATOM   211  C CA  . GLY A 1 27 ? 18.100  34.971 -44.457 1.00 22.10 ? 27  GLY A CA  1 
ATOM   212  C C   . GLY A 1 27 ? 16.779  34.499 -43.943 1.00 22.96 ? 27  GLY A C   1 
ATOM   213  O O   . GLY A 1 27 ? 16.558  33.291 -43.970 1.00 23.70 ? 27  GLY A O   1 
ATOM   214  N N   . GLN A 1 28 ? 15.827  35.345 -43.550 1.00 23.02 ? 28  GLN A N   1 
ATOM   215  C CA  . GLN A 1 28 ? 14.595  34.793 -43.012 1.00 26.13 ? 28  GLN A CA  1 
ATOM   216  C C   . GLN A 1 28 ? 13.759  33.883 -43.900 1.00 27.07 ? 28  GLN A C   1 
ATOM   217  O O   . GLN A 1 28 ? 13.020  33.030 -43.392 1.00 28.46 ? 28  GLN A O   1 
ATOM   218  C CB  . GLN A 1 28 ? 13.749  35.937 -42.539 1.00 31.82 ? 28  GLN A CB  1 
ATOM   219  C CG  . GLN A 1 28 ? 13.332  35.647 -41.086 1.00 42.89 ? 28  GLN A CG  1 
ATOM   220  C CD  . GLN A 1 28 ? 14.414  35.217 -40.061 1.00 47.60 ? 28  GLN A CD  1 
ATOM   221  O OE1 . GLN A 1 28 ? 15.545  35.733 -40.010 1.00 49.60 ? 28  GLN A OE1 1 
ATOM   222  N NE2 . GLN A 1 28 ? 14.132  34.214 -39.221 1.00 48.68 ? 28  GLN A NE2 1 
ATOM   223  N N   . TYR A 1 29 ? 13.923  33.994 -45.222 1.00 26.30 ? 29  TYR A N   1 
ATOM   224  C CA  . TYR A 1 29 ? 13.174  33.209 -46.188 1.00 24.42 ? 29  TYR A CA  1 
ATOM   225  C C   . TYR A 1 29 ? 14.118  32.302 -46.970 1.00 25.65 ? 29  TYR A C   1 
ATOM   226  O O   . TYR A 1 29 ? 13.788  31.875 -48.077 1.00 29.18 ? 29  TYR A O   1 
ATOM   227  C CB  . TYR A 1 29 ? 12.452  34.160 -47.136 1.00 21.50 ? 29  TYR A CB  1 
ATOM   228  C CG  . TYR A 1 29 ? 11.430  35.065 -46.463 1.00 22.84 ? 29  TYR A CG  1 
ATOM   229  C CD1 . TYR A 1 29 ? 10.170  34.576 -46.175 1.00 26.85 ? 29  TYR A CD1 1 
ATOM   230  C CD2 . TYR A 1 29 ? 11.742  36.368 -46.161 1.00 22.95 ? 29  TYR A CD2 1 
ATOM   231  C CE1 . TYR A 1 29 ? 9.213   35.387 -45.590 1.00 27.64 ? 29  TYR A CE1 1 
ATOM   232  C CE2 . TYR A 1 29 ? 10.799  37.189 -45.574 1.00 25.54 ? 29  TYR A CE2 1 
ATOM   233  C CZ  . TYR A 1 29 ? 9.537   36.700 -45.291 1.00 28.19 ? 29  TYR A CZ  1 
ATOM   234  O OH  . TYR A 1 29 ? 8.591   37.557 -44.734 1.00 30.37 ? 29  TYR A OH  1 
ATOM   235  N N   . GLY A 1 30 ? 15.310  31.985 -46.455 1.00 25.97 ? 30  GLY A N   1 
ATOM   236  C CA  . GLY A 1 30 ? 16.251  31.159 -47.179 1.00 23.85 ? 30  GLY A CA  1 
ATOM   237  C C   . GLY A 1 30 ? 16.779  31.926 -48.380 1.00 25.20 ? 30  GLY A C   1 
ATOM   238  O O   . GLY A 1 30 ? 16.667  33.152 -48.459 1.00 24.44 ? 30  GLY A O   1 
ATOM   239  N N   . ARG A 1 31 ? 17.304  31.234 -49.383 1.00 22.68 ? 31  ARG A N   1 
ATOM   240  C CA  . ARG A 1 31 ? 17.950  31.894 -50.486 1.00 24.48 ? 31  ARG A CA  1 
ATOM   241  C C   . ARG A 1 31 ? 16.915  32.095 -51.582 1.00 21.68 ? 31  ARG A C   1 
ATOM   242  O O   . ARG A 1 31 ? 16.234  31.162 -51.989 1.00 22.04 ? 31  ARG A O   1 
ATOM   243  C CB  . ARG A 1 31 ? 19.092  30.988 -50.886 1.00 29.22 ? 31  ARG A CB  1 
ATOM   244  C CG  . ARG A 1 31 ? 20.424  31.635 -50.582 1.00 37.51 ? 31  ARG A CG  1 
ATOM   245  C CD  . ARG A 1 31 ? 21.218  31.705 -51.888 1.00 47.20 ? 31  ARG A CD  1 
ATOM   246  N NE  . ARG A 1 31 ? 20.432  32.183 -53.035 1.00 51.97 ? 31  ARG A NE  1 
ATOM   247  C CZ  . ARG A 1 31 ? 20.723  31.833 -54.299 1.00 52.50 ? 31  ARG A CZ  1 
ATOM   248  N NH1 . ARG A 1 31 ? 21.794  31.064 -54.542 1.00 52.95 ? 31  ARG A NH1 1 
ATOM   249  N NH2 . ARG A 1 31 ? 19.959  32.291 -55.314 1.00 51.39 ? 31  ARG A NH2 1 
ATOM   250  N N   . LEU A 1 32 ? 16.754  33.328 -52.031 1.00 17.16 ? 32  LEU A N   1 
ATOM   251  C CA  . LEU A 1 32 ? 15.759  33.735 -53.007 1.00 16.30 ? 32  LEU A CA  1 
ATOM   252  C C   . LEU A 1 32 ? 16.453  34.149 -54.304 1.00 16.40 ? 32  LEU A C   1 
ATOM   253  O O   . LEU A 1 32 ? 17.631  34.579 -54.313 1.00 16.56 ? 32  LEU A O   1 
ATOM   254  C CB  . LEU A 1 32 ? 14.936  34.944 -52.460 1.00 14.87 ? 32  LEU A CB  1 
ATOM   255  C CG  . LEU A 1 32 ? 14.169  34.845 -51.162 1.00 14.58 ? 32  LEU A CG  1 
ATOM   256  C CD1 . LEU A 1 32 ? 13.589  36.191 -50.763 1.00 13.81 ? 32  LEU A CD1 1 
ATOM   257  C CD2 . LEU A 1 32 ? 13.075  33.806 -51.344 1.00 18.03 ? 32  LEU A CD2 1 
ATOM   258  N N   . THR A 1 33 ? 15.697  34.033 -55.414 1.00 16.16 ? 33  THR A N   1 
ATOM   259  C CA  . THR A 1 33 ? 16.168  34.533 -56.694 1.00 14.73 ? 33  THR A CA  1 
ATOM   260  C C   . THR A 1 33 ? 15.013  35.309 -57.267 1.00 13.34 ? 33  THR A C   1 
ATOM   261  O O   . THR A 1 33 ? 13.856  34.896 -57.186 1.00 14.43 ? 33  THR A O   1 
ATOM   262  C CB  . THR A 1 33 ? 16.608  33.375 -57.620 1.00 16.04 ? 33  THR A CB  1 
ATOM   263  O OG1 . THR A 1 33 ? 17.276  34.015 -58.719 1.00 19.91 ? 33  THR A OG1 1 
ATOM   264  C CG2 . THR A 1 33 ? 15.489  32.501 -58.138 1.00 17.79 ? 33  THR A CG2 1 
ATOM   265  N N   . PHE A 1 34 ? 15.368  36.460 -57.834 1.00 14.93 ? 34  PHE A N   1 
ATOM   266  C CA  . PHE A 1 34 ? 14.413  37.402 -58.392 1.00 12.61 ? 34  PHE A CA  1 
ATOM   267  C C   . PHE A 1 34 ? 13.715  36.886 -59.636 1.00 13.67 ? 34  PHE A C   1 
ATOM   268  O O   . PHE A 1 34 ? 14.342  36.346 -60.548 1.00 13.38 ? 34  PHE A O   1 
ATOM   269  C CB  . PHE A 1 34 ? 15.105  38.706 -58.752 1.00 13.31 ? 34  PHE A CB  1 
ATOM   270  C CG  . PHE A 1 34 ? 14.197  39.756 -59.426 1.00 13.20 ? 34  PHE A CG  1 
ATOM   271  C CD1 . PHE A 1 34 ? 13.320  40.508 -58.652 1.00 11.84 ? 34  PHE A CD1 1 
ATOM   272  C CD2 . PHE A 1 34 ? 14.299  39.970 -60.807 1.00 13.06 ? 34  PHE A CD2 1 
ATOM   273  C CE1 . PHE A 1 34 ? 12.564  41.466 -59.297 1.00 12.34 ? 34  PHE A CE1 1 
ATOM   274  C CE2 . PHE A 1 34 ? 13.527  40.937 -61.439 1.00 13.50 ? 34  PHE A CE2 1 
ATOM   275  C CZ  . PHE A 1 34 ? 12.661  41.682 -60.668 1.00 12.96 ? 34  PHE A CZ  1 
ATOM   276  N N   . ASN A 1 35 ? 12.391  37.071 -59.653 1.00 9.50  ? 35  ASN A N   1 
ATOM   277  C CA  . ASN A 1 35 ? 11.640  36.706 -60.807 1.00 10.18 ? 35  ASN A CA  1 
ATOM   278  C C   . ASN A 1 35 ? 11.024  37.923 -61.437 1.00 9.85  ? 35  ASN A C   1 
ATOM   279  O O   . ASN A 1 35 ? 11.249  38.141 -62.629 1.00 11.46 ? 35  ASN A O   1 
ATOM   280  C CB  . ASN A 1 35 ? 10.509  35.761 -60.456 1.00 13.01 ? 35  ASN A CB  1 
ATOM   281  C CG  . ASN A 1 35 ? 10.943  34.410 -59.926 1.00 14.81 ? 35  ASN A CG  1 
ATOM   282  O OD1 . ASN A 1 35 ? 10.364  33.993 -58.948 1.00 16.29 ? 35  ASN A OD1 1 
ATOM   283  N ND2 . ASN A 1 35 ? 11.983  33.719 -60.339 1.00 13.65 ? 35  ASN A ND2 1 
ATOM   284  N N   . LYS A 1 36 ? 10.229  38.742 -60.732 1.00 10.01 ? 36  LYS A N   1 
ATOM   285  C CA  . LYS A 1 36 ? 9.511   39.812 -61.435 1.00 11.10 ? 36  LYS A CA  1 
ATOM   286  C C   . LYS A 1 36 ? 8.982   40.809 -60.457 1.00 7.04  ? 36  LYS A C   1 
ATOM   287  O O   . LYS A 1 36 ? 8.800   40.459 -59.301 1.00 11.32 ? 36  LYS A O   1 
ATOM   288  C CB  . LYS A 1 36 ? 8.321   39.218 -62.205 1.00 12.44 ? 36  LYS A CB  1 
ATOM   289  C CG  . LYS A 1 36 ? 7.523   40.105 -63.127 1.00 14.36 ? 36  LYS A CG  1 
ATOM   290  C CD  . LYS A 1 36 ? 6.428   39.250 -63.732 1.00 15.60 ? 36  LYS A CD  1 
ATOM   291  C CE  . LYS A 1 36 ? 5.777   40.153 -64.756 1.00 20.55 ? 36  LYS A CE  1 
ATOM   292  N NZ  . LYS A 1 36 ? 4.651   39.478 -65.342 1.00 23.57 ? 36  LYS A NZ  1 
ATOM   293  N N   . VAL A 1 37 ? 8.740   42.036 -60.928 1.00 9.46  ? 37  VAL A N   1 
ATOM   294  C CA  . VAL A 1 37 ? 8.029   43.046 -60.156 1.00 9.78  ? 37  VAL A CA  1 
ATOM   295  C C   . VAL A 1 37 ? 6.727   43.242 -60.956 1.00 10.72 ? 37  VAL A C   1 
ATOM   296  O O   . VAL A 1 37 ? 6.706   43.292 -62.185 1.00 10.71 ? 37  VAL A O   1 
ATOM   297  C CB  . VAL A 1 37 ? 8.799   44.386 -60.075 1.00 13.49 ? 37  VAL A CB  1 
ATOM   298  C CG1 . VAL A 1 37 ? 7.940   45.444 -59.380 1.00 13.20 ? 37  VAL A CG1 1 
ATOM   299  C CG2 . VAL A 1 37 ? 10.076  44.181 -59.246 1.00 16.11 ? 37  VAL A CG2 1 
ATOM   300  N N   . ILE A 1 38 ? 5.607   43.251 -60.231 1.00 12.73 ? 38  ILE A N   1 
ATOM   301  C CA  . ILE A 1 38 ? 4.285   43.451 -60.808 1.00 14.61 ? 38  ILE A CA  1 
ATOM   302  C C   . ILE A 1 38 ? 3.682   44.771 -60.333 1.00 14.46 ? 38  ILE A C   1 
ATOM   303  O O   . ILE A 1 38 ? 4.076   45.342 -59.316 1.00 15.04 ? 38  ILE A O   1 
ATOM   304  C CB  . ILE A 1 38 ? 3.341   42.296 -60.394 1.00 13.00 ? 38  ILE A CB  1 
ATOM   305  C CG1 . ILE A 1 38 ? 3.141   42.201 -58.879 1.00 13.00 ? 38  ILE A CG1 1 
ATOM   306  C CG2 . ILE A 1 38 ? 3.979   41.010 -60.937 1.00 14.70 ? 38  ILE A CG2 1 
ATOM   307  C CD1 . ILE A 1 38 ? 1.974   41.280 -58.394 1.00 15.04 ? 38  ILE A CD1 1 
ATOM   308  N N   . ARG A 1 39 ? 2.723   45.283 -61.081 1.00 14.32 ? 39  ARG A N   1 
ATOM   309  C CA  . ARG A 1 39 ? 1.979   46.466 -60.663 1.00 17.49 ? 39  ARG A CA  1 
ATOM   310  C C   . ARG A 1 39 ? 1.108   46.243 -59.416 1.00 16.27 ? 39  ARG A C   1 
ATOM   311  O O   . ARG A 1 39 ? 0.710   45.100 -59.199 1.00 15.05 ? 39  ARG A O   1 
ATOM   312  C CB  . ARG A 1 39 ? 1.083   46.909 -61.809 1.00 18.95 ? 39  ARG A CB  1 
ATOM   313  C CG  . ARG A 1 39 ? 1.759   47.298 -63.112 1.00 23.63 ? 39  ARG A CG  1 
ATOM   314  C CD  . ARG A 1 39 ? 0.656   47.518 -64.166 1.00 31.20 ? 39  ARG A CD  1 
ATOM   315  N NE  . ARG A 1 39 ? -0.103  46.289 -64.492 1.00 41.73 ? 39  ARG A NE  1 
ATOM   316  C CZ  . ARG A 1 39 ? -1.351  45.946 -64.051 1.00 44.99 ? 39  ARG A CZ  1 
ATOM   317  N NH1 . ARG A 1 39 ? -2.076  46.687 -63.197 1.00 45.70 ? 39  ARG A NH1 1 
ATOM   318  N NH2 . ARG A 1 39 ? -1.879  44.787 -64.454 1.00 44.59 ? 39  ARG A NH2 1 
ATOM   319  N N   . PRO A 1 40 ? 0.746   47.207 -58.560 1.00 15.36 ? 40  PRO A N   1 
ATOM   320  C CA  . PRO A 1 40 ? 1.209   48.598 -58.602 1.00 14.77 ? 40  PRO A CA  1 
ATOM   321  C C   . PRO A 1 40 ? 2.510   48.814 -57.841 1.00 15.09 ? 40  PRO A C   1 
ATOM   322  O O   . PRO A 1 40 ? 2.797   48.117 -56.846 1.00 16.54 ? 40  PRO A O   1 
ATOM   323  C CB  . PRO A 1 40 ? 0.041   49.379 -58.028 1.00 13.33 ? 40  PRO A CB  1 
ATOM   324  C CG  . PRO A 1 40 ? -0.448  48.458 -56.922 1.00 13.20 ? 40  PRO A CG  1 
ATOM   325  C CD  . PRO A 1 40 ? -0.300  47.064 -57.549 1.00 14.86 ? 40  PRO A CD  1 
ATOM   326  N N   . CYS A 1 41 ? 3.315   49.752 -58.304 1.00 14.22 ? 41  CYS A N   1 
ATOM   327  C CA  . CYS A 1 41 ? 4.518   50.120 -57.560 1.00 13.82 ? 41  CYS A CA  1 
ATOM   328  C C   . CYS A 1 41 ? 4.254   51.524 -57.027 1.00 11.87 ? 41  CYS A C   1 
ATOM   329  O O   . CYS A 1 41 ? 3.883   52.389 -57.834 1.00 12.49 ? 41  CYS A O   1 
ATOM   330  C CB  . CYS A 1 41 ? 5.738   50.166 -58.470 1.00 15.08 ? 41  CYS A CB  1 
ATOM   331  S SG  . CYS A 1 41 ? 7.211   50.711 -57.533 1.00 22.05 ? 41  CYS A SG  1 
ATOM   332  N N   . MET A 1 42 ? 4.387   51.803 -55.737 1.00 12.47 ? 42  MET A N   1 
ATOM   333  C CA  . MET A 1 42 ? 4.130   53.138 -55.197 1.00 14.05 ? 42  MET A CA  1 
ATOM   334  C C   . MET A 1 42 ? 5.433   53.824 -54.781 1.00 13.61 ? 42  MET A C   1 
ATOM   335  O O   . MET A 1 42 ? 6.350   53.202 -54.230 1.00 15.57 ? 42  MET A O   1 
ATOM   336  C CB  . MET A 1 42 ? 3.233   53.087 -53.968 1.00 15.11 ? 42  MET A CB  1 
ATOM   337  C CG  . MET A 1 42 ? 1.789   52.630 -54.177 1.00 26.02 ? 42  MET A CG  1 
ATOM   338  S SD  . MET A 1 42 ? 0.797   53.245 -52.767 1.00 42.60 ? 42  MET A SD  1 
ATOM   339  C CE  . MET A 1 42 ? 0.548   54.863 -53.423 1.00 31.80 ? 42  MET A CE  1 
ATOM   340  N N   . LYS A 1 43 ? 5.525   55.125 -55.004 1.00 13.40 ? 43  LYS A N   1 
ATOM   341  C CA  . LYS A 1 43 ? 6.669   55.889 -54.576 1.00 10.31 ? 43  LYS A CA  1 
ATOM   342  C C   . LYS A 1 43 ? 6.114   56.974 -53.667 1.00 12.09 ? 43  LYS A C   1 
ATOM   343  O O   . LYS A 1 43 ? 5.168   57.716 -54.007 1.00 12.00 ? 43  LYS A O   1 
ATOM   344  C CB  . LYS A 1 43 ? 7.358   56.481 -55.818 1.00 10.82 ? 43  LYS A CB  1 
ATOM   345  C CG  . LYS A 1 43 ? 8.374   57.601 -55.489 1.00 10.36 ? 43  LYS A CG  1 
ATOM   346  C CD  . LYS A 1 43 ? 8.768   58.257 -56.789 1.00 12.28 ? 43  LYS A CD  1 
ATOM   347  C CE  . LYS A 1 43 ? 9.847   59.284 -56.543 1.00 13.26 ? 43  LYS A CE  1 
ATOM   348  N NZ  . LYS A 1 43 ? 10.356  59.851 -57.783 1.00 13.11 ? 43  LYS A NZ  1 
ATOM   349  N N   . LYS A 1 44 ? 6.711   57.022 -52.473 1.00 12.00 ? 44  LYS A N   1 
ATOM   350  C CA  . LYS A 1 44 ? 6.414   58.027 -51.493 1.00 9.71  ? 44  LYS A CA  1 
ATOM   351  C C   . LYS A 1 44 ? 7.550   59.044 -51.502 1.00 11.27 ? 44  LYS A C   1 
ATOM   352  O O   . LYS A 1 44 ? 8.715   58.653 -51.430 1.00 11.22 ? 44  LYS A O   1 
ATOM   353  C CB  . LYS A 1 44 ? 6.334   57.432 -50.133 1.00 9.40  ? 44  LYS A CB  1 
ATOM   354  C CG  . LYS A 1 44 ? 5.914   58.388 -49.035 1.00 12.82 ? 44  LYS A CG  1 
ATOM   355  C CD  . LYS A 1 44 ? 6.361   57.745 -47.727 1.00 16.09 ? 44  LYS A CD  1 
ATOM   356  C CE  . LYS A 1 44 ? 5.793   58.584 -46.616 1.00 25.29 ? 44  LYS A CE  1 
ATOM   357  N NZ  . LYS A 1 44 ? 6.102   57.988 -45.313 1.00 32.41 ? 44  LYS A NZ  1 
ATOM   358  N N   . THR A 1 45 ? 7.246   60.344 -51.575 1.00 11.20 ? 45  THR A N   1 
ATOM   359  C CA  . THR A 1 45 ? 8.302   61.334 -51.362 1.00 12.75 ? 45  THR A CA  1 
ATOM   360  C C   . THR A 1 45 ? 8.082   61.936 -49.968 1.00 14.37 ? 45  THR A C   1 
ATOM   361  O O   . THR A 1 45 ? 6.945   62.289 -49.573 1.00 14.87 ? 45  THR A O   1 
ATOM   362  C CB  . THR A 1 45 ? 8.248   62.430 -52.438 1.00 9.09  ? 45  THR A CB  1 
ATOM   363  O OG1 . THR A 1 45 ? 8.325   61.825 -53.714 1.00 11.51 ? 45  THR A OG1 1 
ATOM   364  C CG2 . THR A 1 45 ? 9.401   63.404 -52.264 1.00 13.91 ? 45  THR A CG2 1 
ATOM   365  N N   . ILE A 1 46 ? 9.129   62.019 -49.162 1.00 11.57 ? 46  ILE A N   1 
ATOM   366  C CA  . ILE A 1 46 ? 9.061   62.564 -47.826 1.00 14.43 ? 46  ILE A CA  1 
ATOM   367  C C   . ILE A 1 46 ? 9.719   63.935 -47.903 1.00 15.95 ? 46  ILE A C   1 
ATOM   368  O O   . ILE A 1 46 ? 10.775  64.068 -48.527 1.00 13.99 ? 46  ILE A O   1 
ATOM   369  C CB  . ILE A 1 46 ? 9.833   61.669 -46.899 1.00 16.98 ? 46  ILE A CB  1 
ATOM   370  C CG1 . ILE A 1 46 ? 9.101   60.343 -46.855 1.00 20.14 ? 46  ILE A CG1 1 
ATOM   371  C CG2 . ILE A 1 46 ? 9.978   62.275 -45.507 1.00 15.23 ? 46  ILE A CG2 1 
ATOM   372  C CD1 . ILE A 1 46 ? 10.006  59.133 -46.524 1.00 21.93 ? 46  ILE A CD1 1 
ATOM   373  N N   . TYR A 1 47 ? 9.157   64.942 -47.245 1.00 18.27 ? 47  TYR A N   1 
ATOM   374  C CA  . TYR A 1 47 ? 9.717   66.300 -47.346 1.00 20.62 ? 47  TYR A CA  1 
ATOM   375  C C   . TYR A 1 47 ? 10.180  66.694 -45.967 1.00 24.03 ? 47  TYR A C   1 
ATOM   376  O O   . TYR A 1 47 ? 9.712   66.089 -44.993 1.00 26.21 ? 47  TYR A O   1 
ATOM   377  C CB  . TYR A 1 47 ? 8.674   67.288 -47.776 1.00 16.77 ? 47  TYR A CB  1 
ATOM   378  C CG  . TYR A 1 47 ? 8.319   67.092 -49.234 1.00 18.47 ? 47  TYR A CG  1 
ATOM   379  C CD1 . TYR A 1 47 ? 9.039   67.746 -50.214 1.00 18.13 ? 47  TYR A CD1 1 
ATOM   380  C CD2 . TYR A 1 47 ? 7.271   66.238 -49.552 1.00 18.23 ? 47  TYR A CD2 1 
ATOM   381  C CE1 . TYR A 1 47 ? 8.700   67.533 -51.533 1.00 16.94 ? 47  TYR A CE1 1 
ATOM   382  C CE2 . TYR A 1 47 ? 6.936   66.041 -50.866 1.00 17.76 ? 47  TYR A CE2 1 
ATOM   383  C CZ  . TYR A 1 47 ? 7.656   66.684 -51.838 1.00 17.14 ? 47  TYR A CZ  1 
ATOM   384  O OH  . TYR A 1 47 ? 7.294   66.451 -53.135 1.00 17.57 ? 47  TYR A OH  1 
ATOM   385  N N   . GLU A 1 48 ? 11.065  67.662 -45.853 1.00 27.87 ? 48  GLU A N   1 
ATOM   386  C CA  . GLU A 1 48 ? 11.523  68.143 -44.563 1.00 32.74 ? 48  GLU A CA  1 
ATOM   387  C C   . GLU A 1 48 ? 11.674  69.635 -44.722 1.00 34.53 ? 48  GLU A C   1 
ATOM   388  O O   . GLU A 1 48 ? 11.594  70.136 -45.835 1.00 35.00 ? 48  GLU A O   1 
ATOM   389  C CB  . GLU A 1 48 ? 12.858  67.522 -44.209 1.00 35.77 ? 48  GLU A CB  1 
ATOM   390  C CG  . GLU A 1 48 ? 14.083  67.768 -45.085 1.00 41.95 ? 48  GLU A CG  1 
ATOM   391  C CD  . GLU A 1 48 ? 15.340  67.049 -44.573 1.00 46.11 ? 48  GLU A CD  1 
ATOM   392  O OE1 . GLU A 1 48 ? 15.470  66.851 -43.362 1.00 49.13 ? 48  GLU A OE1 1 
ATOM   393  O OE2 . GLU A 1 48 ? 16.191  66.654 -45.380 1.00 50.16 ? 48  GLU A OE2 1 
ATOM   394  N N   . ASN A 1 49 ? 11.846  70.375 -43.629 1.00 38.10 ? 49  ASN A N   1 
ATOM   395  C CA  . ASN A 1 49 ? 12.081  71.828 -43.626 1.00 39.33 ? 49  ASN A CA  1 
ATOM   396  C C   . ASN A 1 49 ? 11.116  72.573 -44.552 1.00 41.40 ? 49  ASN A C   1 
ATOM   397  O O   . ASN A 1 49 ? 9.913   72.263 -44.487 1.00 41.65 ? 49  ASN A O   1 
ATOM   398  C CB  . ASN A 1 49 ? 13.512  72.129 -44.056 1.00 41.15 ? 49  ASN A CB  1 
ATOM   399  C CG  . ASN A 1 49 ? 14.681  71.542 -43.262 1.00 43.12 ? 49  ASN A CG  1 
ATOM   400  O OD1 . ASN A 1 49 ? 15.813  71.818 -43.623 1.00 43.04 ? 49  ASN A OD1 1 
ATOM   401  N ND2 . ASN A 1 49 ? 14.578  70.778 -42.182 1.00 43.52 ? 49  ASN A ND2 1 
ATOM   402  N N   . GLU A 1 50 ? 11.543  73.480 -45.452 1.00 42.98 ? 50  GLU A N   1 
ATOM   403  C CA  . GLU A 1 50 ? 10.613  74.202 -46.313 1.00 45.89 ? 50  GLU A CA  1 
ATOM   404  C C   . GLU A 1 50 ? 10.544  73.469 -47.648 1.00 44.96 ? 50  GLU A C   1 
ATOM   405  O O   . GLU A 1 50 ? 11.317  73.700 -48.574 1.00 46.52 ? 50  GLU A O   1 
ATOM   406  C CB  . GLU A 1 50 ? 11.124  75.672 -46.406 1.00 50.52 ? 50  GLU A CB  1 
ATOM   407  C CG  . GLU A 1 50 ? 11.373  76.460 -47.714 1.00 56.47 ? 50  GLU A CG  1 
ATOM   408  C CD  . GLU A 1 50 ? 12.796  77.023 -47.824 1.00 60.12 ? 50  GLU A CD  1 
ATOM   409  O OE1 . GLU A 1 50 ? 13.088  78.031 -47.163 1.00 62.83 ? 50  GLU A OE1 1 
ATOM   410  O OE2 . GLU A 1 50 ? 13.608  76.450 -48.563 1.00 60.38 ? 50  GLU A OE2 1 
ATOM   411  N N   . ARG A 1 51 ? 9.649   72.474 -47.659 1.00 42.55 ? 51  ARG A N   1 
ATOM   412  C CA  . ARG A 1 51 ? 9.343   71.607 -48.785 1.00 36.91 ? 51  ARG A CA  1 
ATOM   413  C C   . ARG A 1 51 ? 10.599  71.068 -49.461 1.00 30.62 ? 51  ARG A C   1 
ATOM   414  O O   . ARG A 1 51 ? 10.658  70.964 -50.675 1.00 28.57 ? 51  ARG A O   1 
ATOM   415  C CB  . ARG A 1 51 ? 8.467   72.387 -49.795 1.00 42.23 ? 51  ARG A CB  1 
ATOM   416  C CG  . ARG A 1 51 ? 7.100   72.905 -49.294 1.00 49.11 ? 51  ARG A CG  1 
ATOM   417  C CD  . ARG A 1 51 ? 5.881   72.377 -50.112 1.00 55.87 ? 51  ARG A CD  1 
ATOM   418  N NE  . ARG A 1 51 ? 5.829   72.710 -51.552 1.00 60.86 ? 51  ARG A NE  1 
ATOM   419  C CZ  . ARG A 1 51 ? 5.568   73.941 -52.055 1.00 62.00 ? 51  ARG A CZ  1 
ATOM   420  N NH1 . ARG A 1 51 ? 5.321   75.003 -51.262 1.00 62.83 ? 51  ARG A NH1 1 
ATOM   421  N NH2 . ARG A 1 51 ? 5.562   74.119 -53.386 1.00 61.42 ? 51  ARG A NH2 1 
ATOM   422  N N   . GLU A 1 52 ? 11.641  70.729 -48.690 1.00 25.83 ? 52  GLU A N   1 
ATOM   423  C CA  . GLU A 1 52 ? 12.865  70.145 -49.223 1.00 24.13 ? 52  GLU A CA  1 
ATOM   424  C C   . GLU A 1 52 ? 12.655  68.624 -49.255 1.00 19.97 ? 52  GLU A C   1 
ATOM   425  O O   . GLU A 1 52 ? 12.108  68.053 -48.310 1.00 17.20 ? 52  GLU A O   1 
ATOM   426  C CB  . GLU A 1 52 ? 14.037  70.361 -48.332 1.00 27.79 ? 52  GLU A CB  1 
ATOM   427  C CG  . GLU A 1 52 ? 14.004  71.677 -47.596 1.00 39.63 ? 52  GLU A CG  1 
ATOM   428  C CD  . GLU A 1 52 ? 15.014  72.694 -48.085 1.00 46.19 ? 52  GLU A CD  1 
ATOM   429  O OE1 . GLU A 1 52 ? 16.040  72.296 -48.671 1.00 48.88 ? 52  GLU A OE1 1 
ATOM   430  O OE2 . GLU A 1 52 ? 14.751  73.887 -47.855 1.00 50.00 ? 52  GLU A OE2 1 
ATOM   431  N N   . ILE A 1 53 ? 13.085  67.892 -50.283 1.00 16.56 ? 53  ILE A N   1 
ATOM   432  C CA  . ILE A 1 53 ? 12.911  66.438 -50.328 1.00 13.84 ? 53  ILE A CA  1 
ATOM   433  C C   . ILE A 1 53 ? 13.948  65.864 -49.408 1.00 13.19 ? 53  ILE A C   1 
ATOM   434  O O   . ILE A 1 53 ? 15.126  66.175 -49.552 1.00 14.74 ? 53  ILE A O   1 
ATOM   435  C CB  . ILE A 1 53 ? 13.111  65.888 -51.768 1.00 12.65 ? 53  ILE A CB  1 
ATOM   436  C CG1 . ILE A 1 53 ? 12.114  66.507 -52.740 1.00 15.54 ? 53  ILE A CG1 1 
ATOM   437  C CG2 . ILE A 1 53 ? 12.943  64.363 -51.746 1.00 10.63 ? 53  ILE A CG2 1 
ATOM   438  C CD1 . ILE A 1 53 ? 12.400  66.115 -54.192 1.00 12.54 ? 53  ILE A CD1 1 
ATOM   439  N N   . LYS A 1 54 ? 13.508  65.058 -48.447 1.00 13.64 ? 54  LYS A N   1 
ATOM   440  C CA  . LYS A 1 54 ? 14.370  64.332 -47.520 1.00 14.82 ? 54  LYS A CA  1 
ATOM   441  C C   . LYS A 1 54 ? 14.704  62.958 -48.123 1.00 15.12 ? 54  LYS A C   1 
ATOM   442  O O   . LYS A 1 54 ? 15.864  62.506 -48.078 1.00 13.79 ? 54  LYS A O   1 
ATOM   443  C CB  . LYS A 1 54 ? 13.649  64.171 -46.182 1.00 17.90 ? 54  LYS A CB  1 
ATOM   444  C CG  . LYS A 1 54 ? 14.492  63.450 -45.122 1.00 24.24 ? 54  LYS A CG  1 
ATOM   445  C CD  . LYS A 1 54 ? 13.818  63.426 -43.738 1.00 30.35 ? 54  LYS A CD  1 
ATOM   446  C CE  . LYS A 1 54 ? 14.865  63.069 -42.670 1.00 33.65 ? 54  LYS A CE  1 
ATOM   447  N NZ  . LYS A 1 54 ? 14.580  63.769 -41.420 1.00 33.10 ? 54  LYS A NZ  1 
ATOM   448  N N   . GLY A 1 55 ? 13.752  62.252 -48.744 1.00 15.68 ? 55  GLY A N   1 
ATOM   449  C CA  . GLY A 1 55 ? 14.051  60.947 -49.311 1.00 13.99 ? 55  GLY A CA  1 
ATOM   450  C C   . GLY A 1 55 ? 12.818  60.378 -49.948 1.00 13.57 ? 55  GLY A C   1 
ATOM   451  O O   . GLY A 1 55 ? 11.847  61.123 -50.101 1.00 14.05 ? 55  GLY A O   1 
ATOM   452  N N   . TYR A 1 56 ? 12.842  59.082 -50.269 1.00 12.67 ? 56  TYR A N   1 
ATOM   453  C CA  . TYR A 1 56 ? 11.740  58.382 -50.928 1.00 12.76 ? 56  TYR A CA  1 
ATOM   454  C C   . TYR A 1 56 ? 11.563  57.024 -50.266 1.00 13.09 ? 56  TYR A C   1 
ATOM   455  O O   . TYR A 1 56 ? 12.450  56.527 -49.559 1.00 13.79 ? 56  TYR A O   1 
ATOM   456  C CB  . TYR A 1 56 ? 12.018  58.100 -52.419 1.00 11.90 ? 56  TYR A CB  1 
ATOM   457  C CG  . TYR A 1 56 ? 12.509  59.329 -53.165 1.00 13.59 ? 56  TYR A CG  1 
ATOM   458  C CD1 . TYR A 1 56 ? 11.543  60.219 -53.574 1.00 13.73 ? 56  TYR A CD1 1 
ATOM   459  C CD2 . TYR A 1 56 ? 13.872  59.555 -53.433 1.00 11.78 ? 56  TYR A CD2 1 
ATOM   460  C CE1 . TYR A 1 56 ? 11.940  61.324 -54.312 1.00 15.87 ? 56  TYR A CE1 1 
ATOM   461  C CE2 . TYR A 1 56 ? 14.271  60.675 -54.161 1.00 12.70 ? 56  TYR A CE2 1 
ATOM   462  C CZ  . TYR A 1 56 ? 13.290  61.568 -54.588 1.00 14.73 ? 56  TYR A CZ  1 
ATOM   463  O OH  . TYR A 1 56 ? 13.566  62.691 -55.350 1.00 11.02 ? 56  TYR A OH  1 
ATOM   464  N N   . GLU A 1 57 ? 10.403  56.422 -50.488 1.00 12.50 ? 57  GLU A N   1 
ATOM   465  C CA  . GLU A 1 57 ? 10.192  55.043 -50.139 1.00 14.13 ? 57  GLU A CA  1 
ATOM   466  C C   . GLU A 1 57 ? 9.446   54.413 -51.314 1.00 14.48 ? 57  GLU A C   1 
ATOM   467  O O   . GLU A 1 57 ? 8.586   55.050 -51.933 1.00 16.03 ? 57  GLU A O   1 
ATOM   468  C CB  . GLU A 1 57 ? 9.369   54.939 -48.869 1.00 20.26 ? 57  GLU A CB  1 
ATOM   469  C CG  . GLU A 1 57 ? 10.178  55.268 -47.621 1.00 26.98 ? 57  GLU A CG  1 
ATOM   470  C CD  . GLU A 1 57 ? 9.388   55.116 -46.328 1.00 34.27 ? 57  GLU A CD  1 
ATOM   471  O OE1 . GLU A 1 57 ? 8.378   54.398 -46.321 1.00 35.56 ? 57  GLU A OE1 1 
ATOM   472  O OE2 . GLU A 1 57 ? 9.815   55.707 -45.328 1.00 35.83 ? 57  GLU A OE2 1 
ATOM   473  N N   . TYR A 1 58 ? 9.768   53.191 -51.700 1.00 12.94 ? 58  TYR A N   1 
ATOM   474  C CA  . TYR A 1 58 ? 9.146   52.521 -52.827 1.00 13.09 ? 58  TYR A CA  1 
ATOM   475  C C   . TYR A 1 58 ? 8.518   51.282 -52.238 1.00 13.94 ? 58  TYR A C   1 
ATOM   476  O O   . TYR A 1 58 ? 9.176   50.580 -51.454 1.00 13.70 ? 58  TYR A O   1 
ATOM   477  C CB  . TYR A 1 58 ? 10.164  52.072 -53.862 1.00 13.34 ? 58  TYR A CB  1 
ATOM   478  C CG  . TYR A 1 58 ? 11.012  53.232 -54.370 1.00 16.10 ? 58  TYR A CG  1 
ATOM   479  C CD1 . TYR A 1 58 ? 10.590  54.000 -55.436 1.00 15.33 ? 58  TYR A CD1 1 
ATOM   480  C CD2 . TYR A 1 58 ? 12.260  53.447 -53.787 1.00 17.79 ? 58  TYR A CD2 1 
ATOM   481  C CE1 . TYR A 1 58 ? 11.399  55.026 -55.894 1.00 19.82 ? 58  TYR A CE1 1 
ATOM   482  C CE2 . TYR A 1 58 ? 13.063  54.470 -54.238 1.00 18.31 ? 58  TYR A CE2 1 
ATOM   483  C CZ  . TYR A 1 58 ? 12.623  55.220 -55.291 1.00 16.26 ? 58  TYR A CZ  1 
ATOM   484  O OH  . TYR A 1 58 ? 13.388  56.235 -55.753 1.00 23.15 ? 58  TYR A OH  1 
ATOM   485  N N   . GLN A 1 59 ? 7.237   51.072 -52.555 1.00 13.63 ? 59  GLN A N   1 
ATOM   486  C CA  . GLN A 1 59 ? 6.509   49.883 -52.105 1.00 13.85 ? 59  GLN A CA  1 
ATOM   487  C C   . GLN A 1 59 ? 6.331   49.016 -53.330 1.00 12.17 ? 59  GLN A C   1 
ATOM   488  O O   . GLN A 1 59 ? 5.734   49.469 -54.310 1.00 10.12 ? 59  GLN A O   1 
ATOM   489  C CB  . GLN A 1 59 ? 5.126   50.206 -51.574 1.00 16.56 ? 59  GLN A CB  1 
ATOM   490  C CG  . GLN A 1 59 ? 5.240   51.126 -50.374 1.00 26.02 ? 59  GLN A CG  1 
ATOM   491  C CD  . GLN A 1 59 ? 3.946   51.321 -49.587 1.00 32.49 ? 59  GLN A CD  1 
ATOM   492  O OE1 . GLN A 1 59 ? 2.818   51.047 -50.013 1.00 36.34 ? 59  GLN A OE1 1 
ATOM   493  N NE2 . GLN A 1 59 ? 4.113   51.845 -48.381 1.00 35.73 ? 59  GLN A NE2 1 
ATOM   494  N N   . LEU A 1 60 ? 6.899   47.809 -53.272 1.00 9.35  ? 60  LEU A N   1 
ATOM   495  C CA  . LEU A 1 60 ? 6.933   46.914 -54.382 1.00 9.74  ? 60  LEU A CA  1 
ATOM   496  C C   . LEU A 1 60 ? 6.270   45.577 -54.057 1.00 9.95  ? 60  LEU A C   1 
ATOM   497  O O   . LEU A 1 60 ? 6.269   45.154 -52.906 1.00 11.43 ? 60  LEU A O   1 
ATOM   498  C CB  . LEU A 1 60 ? 8.350   46.563 -54.801 1.00 12.28 ? 60  LEU A CB  1 
ATOM   499  C CG  . LEU A 1 60 ? 9.091   47.466 -55.728 1.00 17.37 ? 60  LEU A CG  1 
ATOM   500  C CD1 . LEU A 1 60 ? 9.430   48.811 -55.108 1.00 19.61 ? 60  LEU A CD1 1 
ATOM   501  C CD2 . LEU A 1 60 ? 10.322  46.692 -56.120 1.00 19.50 ? 60  LEU A CD2 1 
ATOM   502  N N   . TYR A 1 61 ? 5.697   44.982 -55.108 1.00 9.87  ? 61  TYR A N   1 
ATOM   503  C CA  . TYR A 1 61 ? 5.269   43.596 -55.100 1.00 11.97 ? 61  TYR A CA  1 
ATOM   504  C C   . TYR A 1 61 ? 6.301   42.849 -55.942 1.00 10.00 ? 61  TYR A C   1 
ATOM   505  O O   . TYR A 1 61 ? 6.516   43.169 -57.129 1.00 10.35 ? 61  TYR A O   1 
ATOM   506  C CB  . TYR A 1 61 ? 3.908   43.442 -55.743 1.00 12.93 ? 61  TYR A CB  1 
ATOM   507  C CG  . TYR A 1 61 ? 2.781   43.828 -54.857 1.00 13.35 ? 61  TYR A CG  1 
ATOM   508  C CD1 . TYR A 1 61 ? 2.223   42.851 -54.055 1.00 15.81 ? 61  TYR A CD1 1 
ATOM   509  C CD2 . TYR A 1 61 ? 2.291   45.120 -54.936 1.00 16.36 ? 61  TYR A CD2 1 
ATOM   510  C CE1 . TYR A 1 61 ? 1.122   43.178 -53.297 1.00 17.37 ? 61  TYR A CE1 1 
ATOM   511  C CE2 . TYR A 1 61 ? 1.193   45.458 -54.181 1.00 18.97 ? 61  TYR A CE2 1 
ATOM   512  C CZ  . TYR A 1 61 ? 0.623   44.483 -53.384 1.00 21.18 ? 61  TYR A CZ  1 
ATOM   513  O OH  . TYR A 1 61 ? -0.525  44.833 -52.698 1.00 26.29 ? 61  TYR A OH  1 
ATOM   514  N N   . VAL A 1 62 ? 6.915   41.842 -55.325 1.00 10.79 ? 62  VAL A N   1 
ATOM   515  C CA  . VAL A 1 62 ? 8.043   41.185 -55.961 1.00 11.62 ? 62  VAL A CA  1 
ATOM   516  C C   . VAL A 1 62 ? 7.851   39.665 -55.914 1.00 11.19 ? 62  VAL A C   1 
ATOM   517  O O   . VAL A 1 62 ? 7.681   39.100 -54.829 1.00 13.24 ? 62  VAL A O   1 
ATOM   518  C CB  . VAL A 1 62 ? 9.382   41.445 -55.234 1.00 11.23 ? 62  VAL A CB  1 
ATOM   519  C CG1 . VAL A 1 62 ? 10.455  40.989 -56.230 1.00 15.40 ? 62  VAL A CG1 1 
ATOM   520  C CG2 . VAL A 1 62 ? 9.604   42.855 -54.803 1.00 13.30 ? 62  VAL A CG2 1 
ATOM   521  N N   . TYR A 1 63 ? 7.952   38.996 -57.050 1.00 11.74 ? 63  TYR A N   1 
ATOM   522  C CA  . TYR A 1 63 ? 7.984   37.542 -57.109 1.00 11.43 ? 63  TYR A CA  1 
ATOM   523  C C   . TYR A 1 63 ? 9.447   37.180 -56.956 1.00 10.56 ? 63  TYR A C   1 
ATOM   524  O O   . TYR A 1 63 ? 10.289  37.675 -57.733 1.00 11.24 ? 63  TYR A O   1 
ATOM   525  C CB  . TYR A 1 63 ? 7.499   37.026 -58.464 1.00 13.52 ? 63  TYR A CB  1 
ATOM   526  C CG  . TYR A 1 63 ? 5.985   36.836 -58.528 1.00 14.32 ? 63  TYR A CG  1 
ATOM   527  C CD1 . TYR A 1 63 ? 5.429   35.852 -57.744 1.00 16.72 ? 63  TYR A CD1 1 
ATOM   528  C CD2 . TYR A 1 63 ? 5.189   37.637 -59.324 1.00 15.74 ? 63  TYR A CD2 1 
ATOM   529  C CE1 . TYR A 1 63 ? 4.068   35.662 -57.722 1.00 19.10 ? 63  TYR A CE1 1 
ATOM   530  C CE2 . TYR A 1 63 ? 3.820   37.456 -59.307 1.00 17.22 ? 63  TYR A CE2 1 
ATOM   531  C CZ  . TYR A 1 63 ? 3.268   36.468 -58.504 1.00 21.50 ? 63  TYR A CZ  1 
ATOM   532  O OH  . TYR A 1 63 ? 1.885   36.311 -58.409 1.00 24.90 ? 63  TYR A OH  1 
ATOM   533  N N   . ALA A 1 64 ? 9.766   36.333 -56.006 1.00 10.41 ? 64  ALA A N   1 
ATOM   534  C CA  . ALA A 1 64 ? 11.126  35.844 -55.816 1.00 10.26 ? 64  ALA A CA  1 
ATOM   535  C C   . ALA A 1 64 ? 10.958  34.372 -55.475 1.00 11.92 ? 64  ALA A C   1 
ATOM   536  O O   . ALA A 1 64 ? 10.155  34.023 -54.584 1.00 13.37 ? 64  ALA A O   1 
ATOM   537  C CB  . ALA A 1 64 ? 11.790  36.503 -54.656 1.00 8.65  ? 64  ALA A CB  1 
ATOM   538  N N   . SER A 1 65 ? 11.681  33.515 -56.211 1.00 13.30 ? 65  SER A N   1 
ATOM   539  C CA  . SER A 1 65 ? 11.553  32.055 -56.094 1.00 13.88 ? 65  SER A CA  1 
ATOM   540  C C   . SER A 1 65 ? 10.075  31.590 -56.105 1.00 14.56 ? 65  SER A C   1 
ATOM   541  O O   . SER A 1 65 ? 9.629   30.786 -55.278 1.00 14.90 ? 65  SER A O   1 
ATOM   542  C CB  . SER A 1 65 ? 12.241  31.603 -54.811 1.00 15.13 ? 65  SER A CB  1 
ATOM   543  O OG  . SER A 1 65 ? 13.644  31.848 -54.977 1.00 16.73 ? 65  SER A OG  1 
ATOM   544  N N   . ASP A 1 66 ? 9.319   32.172 -57.040 1.00 14.42 ? 66  ASP A N   1 
ATOM   545  C CA  . ASP A 1 66 ? 7.897   31.935 -57.223 1.00 17.50 ? 66  ASP A CA  1 
ATOM   546  C C   . ASP A 1 66 ? 6.908   32.292 -56.122 1.00 19.07 ? 66  ASP A C   1 
ATOM   547  O O   . ASP A 1 66 ? 5.723   31.931 -56.231 1.00 20.33 ? 66  ASP A O   1 
ATOM   548  C CB  . ASP A 1 66 ? 7.659   30.461 -57.594 1.00 19.94 ? 66  ASP A CB  1 
ATOM   549  C CG  . ASP A 1 66 ? 7.737   30.189 -59.079 1.00 27.41 ? 66  ASP A CG  1 
ATOM   550  O OD1 . ASP A 1 66 ? 7.688   31.093 -59.911 1.00 28.60 ? 66  ASP A OD1 1 
ATOM   551  O OD2 . ASP A 1 66 ? 7.840   29.015 -59.407 1.00 34.37 ? 66  ASP A OD2 1 
ATOM   552  N N   . LYS A 1 67 ? 7.327   33.028 -55.085 1.00 18.69 ? 67  LYS A N   1 
ATOM   553  C CA  . LYS A 1 67 ? 6.461   33.449 -53.998 1.00 18.27 ? 67  LYS A CA  1 
ATOM   554  C C   . LYS A 1 67 ? 6.322   34.941 -54.147 1.00 17.64 ? 67  LYS A C   1 
ATOM   555  O O   . LYS A 1 67 ? 7.238   35.585 -54.665 1.00 16.02 ? 67  LYS A O   1 
ATOM   556  C CB  . LYS A 1 67 ? 7.101   33.116 -52.672 1.00 21.09 ? 67  LYS A CB  1 
ATOM   557  C CG  . LYS A 1 67 ? 7.339   31.604 -52.458 1.00 27.33 ? 67  LYS A CG  1 
ATOM   558  C CD  . LYS A 1 67 ? 8.341   31.360 -51.298 1.00 31.99 ? 67  LYS A CD  1 
ATOM   559  C CE  . LYS A 1 67 ? 7.753   31.701 -49.893 1.00 40.56 ? 67  LYS A CE  1 
ATOM   560  N NZ  . LYS A 1 67 ? 8.702   31.709 -48.770 1.00 43.30 ? 67  LYS A NZ  1 
ATOM   561  N N   . LEU A 1 68 ? 5.195   35.540 -53.739 1.00 15.89 ? 68  LEU A N   1 
ATOM   562  C CA  . LEU A 1 68 ? 4.979   36.958 -53.943 1.00 15.24 ? 68  LEU A CA  1 
ATOM   563  C C   . LEU A 1 68 ? 5.168   37.664 -52.609 1.00 14.48 ? 68  LEU A C   1 
ATOM   564  O O   . LEU A 1 68 ? 4.521   37.358 -51.596 1.00 15.78 ? 68  LEU A O   1 
ATOM   565  C CB  . LEU A 1 68 ? 3.560   37.214 -54.446 1.00 12.48 ? 68  LEU A CB  1 
ATOM   566  C CG  . LEU A 1 68 ? 3.162   38.642 -54.699 1.00 15.16 ? 68  LEU A CG  1 
ATOM   567  C CD1 . LEU A 1 68 ? 4.088   39.305 -55.722 1.00 16.70 ? 68  LEU A CD1 1 
ATOM   568  C CD2 . LEU A 1 68 ? 1.753   38.641 -55.258 1.00 15.21 ? 68  LEU A CD2 1 
ATOM   569  N N   . PHE A 1 69 ? 6.068   38.652 -52.606 1.00 13.72 ? 69  PHE A N   1 
ATOM   570  C CA  . PHE A 1 69 ? 6.419   39.365 -51.389 1.00 14.19 ? 69  PHE A CA  1 
ATOM   571  C C   . PHE A 1 69 ? 6.108   40.845 -51.587 1.00 13.79 ? 69  PHE A C   1 
ATOM   572  O O   . PHE A 1 69 ? 6.063   41.326 -52.716 1.00 13.76 ? 69  PHE A O   1 
ATOM   573  C CB  . PHE A 1 69 ? 7.942   39.228 -51.090 1.00 12.47 ? 69  PHE A CB  1 
ATOM   574  C CG  . PHE A 1 69 ? 8.347   37.785 -50.819 1.00 14.43 ? 69  PHE A CG  1 
ATOM   575  C CD1 . PHE A 1 69 ? 8.199   37.264 -49.539 1.00 15.88 ? 69  PHE A CD1 1 
ATOM   576  C CD2 . PHE A 1 69 ? 8.876   36.989 -51.841 1.00 14.38 ? 69  PHE A CD2 1 
ATOM   577  C CE1 . PHE A 1 69 ? 8.566   35.945 -49.255 1.00 12.73 ? 69  PHE A CE1 1 
ATOM   578  C CE2 . PHE A 1 69 ? 9.241   35.677 -51.534 1.00 16.43 ? 69  PHE A CE2 1 
ATOM   579  C CZ  . PHE A 1 69 ? 9.080   35.162 -50.252 1.00 11.09 ? 69  PHE A CZ  1 
ATOM   580  N N   . ARG A 1 70 ? 5.902   41.550 -50.487 1.00 14.13 ? 70  ARG A N   1 
ATOM   581  C CA  . ARG A 1 70 ? 5.749   43.002 -50.471 1.00 16.58 ? 70  ARG A CA  1 
ATOM   582  C C   . ARG A 1 70 ? 7.061   43.562 -49.950 1.00 13.71 ? 70  ARG A C   1 
ATOM   583  O O   . ARG A 1 70 ? 7.431   43.158 -48.847 1.00 13.11 ? 70  ARG A O   1 
ATOM   584  C CB  . ARG A 1 70 ? 4.592   43.369 -49.535 1.00 18.22 ? 70  ARG A CB  1 
ATOM   585  C CG  . ARG A 1 70 ? 3.329   43.505 -50.368 1.00 21.78 ? 70  ARG A CG  1 
ATOM   586  C CD  . ARG A 1 70 ? 3.284   44.875 -51.063 1.00 23.28 ? 70  ARG A CD  1 
ATOM   587  N NE  . ARG A 1 70 ? 3.144   45.952 -50.073 1.00 26.66 ? 70  ARG A NE  1 
ATOM   588  C CZ  . ARG A 1 70 ? 4.122   46.815 -49.772 1.00 27.17 ? 70  ARG A CZ  1 
ATOM   589  N NH1 . ARG A 1 70 ? 5.312   46.713 -50.360 1.00 26.82 ? 70  ARG A NH1 1 
ATOM   590  N NH2 . ARG A 1 70 ? 3.908   47.774 -48.866 1.00 25.57 ? 70  ARG A NH2 1 
ATOM   591  N N   . ALA A 1 71 ? 7.791   44.438 -50.642 1.00 13.69 ? 71  ALA A N   1 
ATOM   592  C CA  . ALA A 1 71 ? 9.065   44.930 -50.137 1.00 10.94 ? 71  ALA A CA  1 
ATOM   593  C C   . ALA A 1 71 ? 9.005   46.441 -50.085 1.00 11.44 ? 71  ALA A C   1 
ATOM   594  O O   . ALA A 1 71 ? 8.392   47.033 -50.980 1.00 12.07 ? 71  ALA A O   1 
ATOM   595  C CB  . ALA A 1 71 ? 10.204  44.546 -51.076 1.00 10.49 ? 71  ALA A CB  1 
ATOM   596  N N   . ASP A 1 72 ? 9.524   47.096 -49.049 1.00 10.36 ? 72  ASP A N   1 
ATOM   597  C CA  . ASP A 1 72 ? 9.523   48.557 -48.973 1.00 12.74 ? 72  ASP A CA  1 
ATOM   598  C C   . ASP A 1 72 ? 10.977  48.987 -48.910 1.00 11.44 ? 72  ASP A C   1 
ATOM   599  O O   . ASP A 1 72 ? 11.715  48.415 -48.086 1.00 11.06 ? 72  ASP A O   1 
ATOM   600  C CB  . ASP A 1 72 ? 8.819   49.053 -47.720 1.00 14.06 ? 72  ASP A CB  1 
ATOM   601  C CG  . ASP A 1 72 ? 7.333   48.789 -47.702 1.00 15.10 ? 72  ASP A CG  1 
ATOM   602  O OD1 . ASP A 1 72 ? 6.686   48.655 -48.724 1.00 16.89 ? 72  ASP A OD1 1 
ATOM   603  O OD2 . ASP A 1 72 ? 6.825   48.675 -46.616 1.00 21.24 ? 72  ASP A OD2 1 
ATOM   604  N N   . ILE A 1 73 ? 11.367  49.976 -49.713 1.00 9.76  ? 73  ILE A N   1 
ATOM   605  C CA  . ILE A 1 73 ? 12.771  50.373 -49.863 1.00 11.55 ? 73  ILE A CA  1 
ATOM   606  C C   . ILE A 1 73 ? 12.819  51.864 -49.611 1.00 12.75 ? 73  ILE A C   1 
ATOM   607  O O   . ILE A 1 73 ? 11.944  52.594 -50.071 1.00 11.64 ? 73  ILE A O   1 
ATOM   608  C CB  . ILE A 1 73 ? 13.300  50.054 -51.319 1.00 11.48 ? 73  ILE A CB  1 
ATOM   609  C CG1 . ILE A 1 73 ? 13.229  48.556 -51.526 1.00 12.62 ? 73  ILE A CG1 1 
ATOM   610  C CG2 . ILE A 1 73 ? 14.751  50.487 -51.547 1.00 13.87 ? 73  ILE A CG2 1 
ATOM   611  C CD1 . ILE A 1 73 ? 13.268  48.161 -52.995 1.00 14.14 ? 73  ILE A CD1 1 
ATOM   612  N N   . SER A 1 74 ? 13.827  52.340 -48.893 1.00 14.71 ? 74  SER A N   1 
ATOM   613  C CA  . SER A 1 74 ? 14.020  53.768 -48.694 1.00 14.91 ? 74  SER A CA  1 
ATOM   614  C C   . SER A 1 74 ? 15.247  54.179 -49.494 1.00 16.00 ? 74  SER A C   1 
ATOM   615  O O   . SER A 1 74 ? 16.202  53.416 -49.733 1.00 15.97 ? 74  SER A O   1 
ATOM   616  C CB  . SER A 1 74 ? 14.237  54.091 -47.197 1.00 17.84 ? 74  SER A CB  1 
ATOM   617  O OG  . SER A 1 74 ? 15.257  53.283 -46.623 1.00 24.77 ? 74  SER A OG  1 
ATOM   618  N N   . GLU A 1 75 ? 15.203  55.422 -49.946 1.00 15.93 ? 75  GLU A N   1 
ATOM   619  C CA  . GLU A 1 75 ? 16.287  55.981 -50.701 1.00 14.32 ? 75  GLU A CA  1 
ATOM   620  C C   . GLU A 1 75 ? 16.455  57.393 -50.139 1.00 16.12 ? 75  GLU A C   1 
ATOM   621  O O   . GLU A 1 75 ? 15.530  58.210 -50.159 1.00 14.22 ? 75  GLU A O   1 
ATOM   622  C CB  . GLU A 1 75 ? 15.913  56.025 -52.137 1.00 15.54 ? 75  GLU A CB  1 
ATOM   623  C CG  . GLU A 1 75 ? 17.181  56.297 -52.935 1.00 22.84 ? 75  GLU A CG  1 
ATOM   624  C CD  . GLU A 1 75 ? 16.897  56.239 -54.432 1.00 28.28 ? 75  GLU A CD  1 
ATOM   625  O OE1 . GLU A 1 75 ? 16.418  57.239 -54.976 1.00 29.43 ? 75  GLU A OE1 1 
ATOM   626  O OE2 . GLU A 1 75 ? 17.142  55.205 -55.051 1.00 33.57 ? 75  GLU A OE2 1 
ATOM   627  N N   . ASP A 1 76 ? 17.627  57.637 -49.550 1.00 14.62 ? 76  ASP A N   1 
ATOM   628  C CA  . ASP A 1 76 ? 17.946  58.930 -48.996 1.00 16.68 ? 76  ASP A CA  1 
ATOM   629  C C   . ASP A 1 76 ? 18.249  59.911 -50.135 1.00 16.13 ? 76  ASP A C   1 
ATOM   630  O O   . ASP A 1 76 ? 19.056  59.600 -51.030 1.00 13.08 ? 76  ASP A O   1 
ATOM   631  C CB  . ASP A 1 76 ? 19.166  58.832 -48.065 1.00 16.73 ? 76  ASP A CB  1 
ATOM   632  C CG  . ASP A 1 76 ? 19.385  60.208 -47.400 1.00 18.89 ? 76  ASP A CG  1 
ATOM   633  O OD1 . ASP A 1 76 ? 18.653  60.590 -46.490 1.00 20.92 ? 76  ASP A OD1 1 
ATOM   634  O OD2 . ASP A 1 76 ? 20.262  60.940 -47.827 1.00 20.97 ? 76  ASP A OD2 1 
ATOM   635  N N   . TYR A 1 77 ? 17.656  61.117 -50.076 1.00 14.18 ? 77  TYR A N   1 
ATOM   636  C CA  . TYR A 1 77 ? 17.806  62.064 -51.165 1.00 13.28 ? 77  TYR A CA  1 
ATOM   637  C C   . TYR A 1 77 ? 19.256  62.525 -51.297 1.00 14.12 ? 77  TYR A C   1 
ATOM   638  O O   . TYR A 1 77 ? 19.791  62.545 -52.414 1.00 15.43 ? 77  TYR A O   1 
ATOM   639  C CB  . TYR A 1 77 ? 16.834  63.285 -50.919 1.00 12.46 ? 77  TYR A CB  1 
ATOM   640  C CG  . TYR A 1 77 ? 16.889  64.356 -52.018 1.00 14.63 ? 77  TYR A CG  1 
ATOM   641  C CD1 . TYR A 1 77 ? 16.076  64.237 -53.122 1.00 11.83 ? 77  TYR A CD1 1 
ATOM   642  C CD2 . TYR A 1 77 ? 17.802  65.420 -51.956 1.00 14.49 ? 77  TYR A CD2 1 
ATOM   643  C CE1 . TYR A 1 77 ? 16.177  65.150 -54.157 1.00 12.45 ? 77  TYR A CE1 1 
ATOM   644  C CE2 . TYR A 1 77 ? 17.917  66.330 -52.994 1.00 12.83 ? 77  TYR A CE2 1 
ATOM   645  C CZ  . TYR A 1 77 ? 17.101  66.173 -54.092 1.00 13.35 ? 77  TYR A CZ  1 
ATOM   646  O OH  . TYR A 1 77 ? 17.196  67.020 -55.163 1.00 14.31 ? 77  TYR A OH  1 
ATOM   647  N N   . LYS A 1 78 ? 19.854  62.933 -50.182 1.00 15.49 ? 78  LYS A N   1 
ATOM   648  C CA  . LYS A 1 78 ? 21.233  63.414 -50.252 1.00 18.98 ? 78  LYS A CA  1 
ATOM   649  C C   . LYS A 1 78 ? 22.268  62.385 -50.617 1.00 19.20 ? 78  LYS A C   1 
ATOM   650  O O   . LYS A 1 78 ? 23.113  62.632 -51.459 1.00 20.51 ? 78  LYS A O   1 
ATOM   651  C CB  . LYS A 1 78 ? 21.663  64.027 -48.947 1.00 26.03 ? 78  LYS A CB  1 
ATOM   652  C CG  . LYS A 1 78 ? 20.886  65.305 -48.621 1.00 36.13 ? 78  LYS A CG  1 
ATOM   653  C CD  . LYS A 1 78 ? 21.177  65.654 -47.181 1.00 41.95 ? 78  LYS A CD  1 
ATOM   654  C CE  . LYS A 1 78 ? 20.232  66.701 -46.610 1.00 46.22 ? 78  LYS A CE  1 
ATOM   655  N NZ  . LYS A 1 78 ? 20.603  66.968 -45.220 1.00 49.96 ? 78  LYS A NZ  1 
ATOM   656  N N   . THR A 1 79 ? 22.271  61.210 -50.020 1.00 20.29 ? 79  THR A N   1 
ATOM   657  C CA  . THR A 1 79 ? 23.314  60.250 -50.302 1.00 17.98 ? 79  THR A CA  1 
ATOM   658  C C   . THR A 1 79 ? 22.962  59.296 -51.425 1.00 17.88 ? 79  THR A C   1 
ATOM   659  O O   . THR A 1 79 ? 23.846  58.569 -51.880 1.00 17.71 ? 79  THR A O   1 
ATOM   660  C CB  . THR A 1 79 ? 23.607  59.477 -48.999 1.00 18.52 ? 79  THR A CB  1 
ATOM   661  O OG1 . THR A 1 79 ? 22.444  58.706 -48.751 1.00 21.64 ? 79  THR A OG1 1 
ATOM   662  C CG2 . THR A 1 79 ? 23.898  60.360 -47.785 1.00 17.66 ? 79  THR A CG2 1 
ATOM   663  N N   . ARG A 1 80 ? 21.682  59.285 -51.846 1.00 17.11 ? 80  ARG A N   1 
ATOM   664  C CA  . ARG A 1 80 ? 21.064  58.308 -52.752 1.00 18.01 ? 80  ARG A CA  1 
ATOM   665  C C   . ARG A 1 80 ? 21.230  56.862 -52.254 1.00 17.47 ? 80  ARG A C   1 
ATOM   666  O O   . ARG A 1 80 ? 21.017  55.893 -52.985 1.00 17.81 ? 80  ARG A O   1 
ATOM   667  C CB  . ARG A 1 80 ? 21.616  58.373 -54.197 1.00 21.79 ? 80  ARG A CB  1 
ATOM   668  C CG  . ARG A 1 80 ? 21.538  59.771 -54.811 1.00 26.29 ? 80  ARG A CG  1 
ATOM   669  C CD  . ARG A 1 80 ? 21.027  59.855 -56.248 1.00 29.81 ? 80  ARG A CD  1 
ATOM   670  N NE  . ARG A 1 80 ? 21.798  59.132 -57.244 1.00 33.45 ? 80  ARG A NE  1 
ATOM   671  C CZ  . ARG A 1 80 ? 21.171  58.283 -58.065 1.00 35.35 ? 80  ARG A CZ  1 
ATOM   672  N NH1 . ARG A 1 80 ? 19.842  58.080 -57.944 1.00 34.57 ? 80  ARG A NH1 1 
ATOM   673  N NH2 . ARG A 1 80 ? 21.867  57.617 -58.990 1.00 32.75 ? 80  ARG A NH2 1 
ATOM   674  N N   . GLY A 1 81 ? 21.434  56.691 -50.952 1.00 15.56 ? 81  GLY A N   1 
ATOM   675  C CA  . GLY A 1 81 ? 21.657  55.365 -50.385 1.00 15.24 ? 81  GLY A CA  1 
ATOM   676  C C   . GLY A 1 81 ? 20.311  54.671 -50.209 1.00 14.88 ? 81  GLY A C   1 
ATOM   677  O O   . GLY A 1 81 ? 19.329  55.311 -49.805 1.00 14.61 ? 81  GLY A O   1 
ATOM   678  N N   . ARG A 1 82 ? 20.263  53.391 -50.537 1.00 14.63 ? 82  ARG A N   1 
ATOM   679  C CA  . ARG A 1 82 ? 19.045  52.609 -50.461 1.00 16.32 ? 82  ARG A CA  1 
ATOM   680  C C   . ARG A 1 82 ? 19.107  51.694 -49.263 1.00 15.19 ? 82  ARG A C   1 
ATOM   681  O O   . ARG A 1 82 ? 20.169  51.184 -48.936 1.00 14.73 ? 82  ARG A O   1 
ATOM   682  C CB  . ARG A 1 82 ? 18.879  51.728 -51.695 1.00 17.52 ? 82  ARG A CB  1 
ATOM   683  C CG  . ARG A 1 82 ? 18.743  52.507 -52.989 1.00 21.54 ? 82  ARG A CG  1 
ATOM   684  C CD  . ARG A 1 82 ? 18.634  51.603 -54.220 1.00 19.77 ? 82  ARG A CD  1 
ATOM   685  N NE  . ARG A 1 82 ? 18.159  52.490 -55.275 1.00 20.41 ? 82  ARG A NE  1 
ATOM   686  C CZ  . ARG A 1 82 ? 17.978  52.108 -56.529 1.00 20.40 ? 82  ARG A CZ  1 
ATOM   687  N NH1 . ARG A 1 82 ? 18.216  50.843 -56.941 1.00 21.94 ? 82  ARG A NH1 1 
ATOM   688  N NH2 . ARG A 1 82 ? 17.528  53.044 -57.356 1.00 22.49 ? 82  ARG A NH2 1 
ATOM   689  N N   . LYS A 1 83 ? 17.999  51.372 -48.657 1.00 14.83 ? 83  LYS A N   1 
ATOM   690  C CA  . LYS A 1 83 ? 17.964  50.494 -47.507 1.00 16.47 ? 83  LYS A CA  1 
ATOM   691  C C   . LYS A 1 83 ? 16.667  49.686 -47.582 1.00 16.49 ? 83  LYS A C   1 
ATOM   692  O O   . LYS A 1 83 ? 15.596  50.241 -47.926 1.00 16.11 ? 83  LYS A O   1 
ATOM   693  C CB  . LYS A 1 83 ? 18.025  51.400 -46.312 1.00 21.95 ? 83  LYS A CB  1 
ATOM   694  C CG  . LYS A 1 83 ? 17.871  50.935 -44.910 1.00 31.32 ? 83  LYS A CG  1 
ATOM   695  C CD  . LYS A 1 83 ? 18.029  52.227 -44.104 1.00 39.71 ? 83  LYS A CD  1 
ATOM   696  C CE  . LYS A 1 83 ? 17.985  51.997 -42.583 1.00 46.04 ? 83  LYS A CE  1 
ATOM   697  N NZ  . LYS A 1 83 ? 16.658  51.694 -42.050 1.00 51.18 ? 83  LYS A NZ  1 
ATOM   698  N N   . LEU A 1 84 ? 16.735  48.375 -47.291 1.00 12.95 ? 84  LEU A N   1 
ATOM   699  C CA  . LEU A 1 84 ? 15.533  47.562 -47.285 1.00 11.08 ? 84  LEU A CA  1 
ATOM   700  C C   . LEU A 1 84 ? 14.813  47.809 -45.987 1.00 11.76 ? 84  LEU A C   1 
ATOM   701  O O   . LEU A 1 84 ? 15.409  47.563 -44.933 1.00 15.66 ? 84  LEU A O   1 
ATOM   702  C CB  . LEU A 1 84 ? 15.854  46.052 -47.397 1.00 12.48 ? 84  LEU A CB  1 
ATOM   703  C CG  . LEU A 1 84 ? 14.647  45.070 -47.378 1.00 12.35 ? 84  LEU A CG  1 
ATOM   704  C CD1 . LEU A 1 84 ? 13.747  45.240 -48.626 1.00 12.88 ? 84  LEU A CD1 1 
ATOM   705  C CD2 . LEU A 1 84 ? 15.216  43.672 -47.230 1.00 14.63 ? 84  LEU A CD2 1 
ATOM   706  N N   . LEU A 1 85 ? 13.569  48.312 -46.000 1.00 10.62 ? 85  LEU A N   1 
ATOM   707  C CA  . LEU A 1 85 ? 12.844  48.581 -44.780 1.00 12.96 ? 85  LEU A CA  1 
ATOM   708  C C   . LEU A 1 85 ? 12.084  47.370 -44.272 1.00 16.62 ? 85  LEU A C   1 
ATOM   709  O O   . LEU A 1 85 ? 12.078  47.091 -43.062 1.00 17.09 ? 85  LEU A O   1 
ATOM   710  C CB  . LEU A 1 85 ? 11.879  49.680 -45.015 1.00 14.57 ? 85  LEU A CB  1 
ATOM   711  C CG  . LEU A 1 85 ? 12.502  51.010 -45.307 1.00 16.47 ? 85  LEU A CG  1 
ATOM   712  C CD1 . LEU A 1 85 ? 11.380  52.042 -45.422 1.00 19.59 ? 85  LEU A CD1 1 
ATOM   713  C CD2 . LEU A 1 85 ? 13.455  51.397 -44.193 1.00 20.39 ? 85  LEU A CD2 1 
ATOM   714  N N   . ARG A 1 86 ? 11.365  46.688 -45.179 1.00 17.84 ? 86  ARG A N   1 
ATOM   715  C CA  . ARG A 1 86 ? 10.697  45.450 -44.840 1.00 17.87 ? 86  ARG A CA  1 
ATOM   716  C C   . ARG A 1 86 ? 10.431  44.625 -46.059 1.00 15.54 ? 86  ARG A C   1 
ATOM   717  O O   . ARG A 1 86 ? 10.438  45.134 -47.186 1.00 13.41 ? 86  ARG A O   1 
ATOM   718  C CB  . ARG A 1 86 ? 9.395   45.708 -44.099 1.00 22.31 ? 86  ARG A CB  1 
ATOM   719  C CG  . ARG A 1 86 ? 8.357   46.583 -44.694 1.00 28.82 ? 86  ARG A CG  1 
ATOM   720  C CD  . ARG A 1 86 ? 7.459   47.104 -43.521 1.00 33.97 ? 86  ARG A CD  1 
ATOM   721  N NE  . ARG A 1 86 ? 8.133   48.011 -42.589 1.00 37.23 ? 86  ARG A NE  1 
ATOM   722  C CZ  . ARG A 1 86 ? 8.389   49.311 -42.875 1.00 39.45 ? 86  ARG A CZ  1 
ATOM   723  N NH1 . ARG A 1 86 ? 8.087   49.937 -44.030 1.00 36.50 ? 86  ARG A NH1 1 
ATOM   724  N NH2 . ARG A 1 86 ? 9.002   50.029 -41.956 1.00 40.77 ? 86  ARG A NH2 1 
ATOM   725  N N   . PHE A 1 87 ? 10.325  43.321 -45.824 1.00 15.29 ? 87  PHE A N   1 
ATOM   726  C CA  . PHE A 1 87 ? 10.145  42.352 -46.882 1.00 14.89 ? 87  PHE A CA  1 
ATOM   727  C C   . PHE A 1 87 ? 9.259   41.298 -46.237 1.00 18.26 ? 87  PHE A C   1 
ATOM   728  O O   . PHE A 1 87 ? 9.696   40.618 -45.291 1.00 19.16 ? 87  PHE A O   1 
ATOM   729  C CB  . PHE A 1 87 ? 11.510  41.850 -47.210 1.00 13.45 ? 87  PHE A CB  1 
ATOM   730  C CG  . PHE A 1 87 ? 11.594  41.010 -48.436 1.00 12.10 ? 87  PHE A CG  1 
ATOM   731  C CD1 . PHE A 1 87 ? 11.195  39.681 -48.387 1.00 12.43 ? 87  PHE A CD1 1 
ATOM   732  C CD2 . PHE A 1 87 ? 12.088  41.576 -49.599 1.00 11.76 ? 87  PHE A CD2 1 
ATOM   733  C CE1 . PHE A 1 87 ? 11.288  38.918 -49.514 1.00 10.45 ? 87  PHE A CE1 1 
ATOM   734  C CE2 . PHE A 1 87 ? 12.192  40.790 -50.724 1.00 13.22 ? 87  PHE A CE2 1 
ATOM   735  C CZ  . PHE A 1 87 ? 11.786  39.459 -50.681 1.00 13.27 ? 87  PHE A CZ  1 
ATOM   736  N N   . ASN A 1 88 ? 8.026   41.149 -46.699 1.00 17.79 ? 88  ASN A N   1 
ATOM   737  C CA  . ASN A 1 88 ? 7.080   40.267 -46.047 1.00 19.72 ? 88  ASN A CA  1 
ATOM   738  C C   . ASN A 1 88 ? 6.301   39.484 -47.036 1.00 18.09 ? 88  ASN A C   1 
ATOM   739  O O   . ASN A 1 88 ? 5.963   39.986 -48.099 1.00 16.28 ? 88  ASN A O   1 
ATOM   740  C CB  . ASN A 1 88 ? 6.001   40.967 -45.245 1.00 24.39 ? 88  ASN A CB  1 
ATOM   741  C CG  . ASN A 1 88 ? 6.511   41.451 -43.927 1.00 30.78 ? 88  ASN A CG  1 
ATOM   742  O OD1 . ASN A 1 88 ? 6.796   42.643 -43.758 1.00 35.95 ? 88  ASN A OD1 1 
ATOM   743  N ND2 . ASN A 1 88 ? 6.681   40.561 -42.955 1.00 33.77 ? 88  ASN A ND2 1 
ATOM   744  N N   . GLY A 1 89 ? 6.010   38.251 -46.682 1.00 20.06 ? 89  GLY A N   1 
ATOM   745  C CA  . GLY A 1 89 ? 5.132   37.488 -47.504 1.00 18.09 ? 89  GLY A CA  1 
ATOM   746  C C   . GLY A 1 89 ? 5.205   36.001 -47.201 1.00 19.54 ? 89  GLY A C   1 
ATOM   747  O O   . GLY A 1 89 ? 5.778   35.627 -46.175 1.00 19.72 ? 89  GLY A O   1 
ATOM   748  N N   . PRO A 1 90 ? 4.668   35.127 -48.059 1.00 19.50 ? 90  PRO A N   1 
ATOM   749  C CA  . PRO A 1 90 ? 3.895   35.477 -49.248 1.00 19.76 ? 90  PRO A CA  1 
ATOM   750  C C   . PRO A 1 90 ? 2.596   36.222 -48.949 1.00 19.42 ? 90  PRO A C   1 
ATOM   751  O O   . PRO A 1 90 ? 1.974   36.091 -47.872 1.00 18.97 ? 90  PRO A O   1 
ATOM   752  C CB  . PRO A 1 90 ? 3.656   34.168 -49.929 1.00 21.12 ? 90  PRO A CB  1 
ATOM   753  C CG  . PRO A 1 90 ? 4.696   33.251 -49.369 1.00 21.54 ? 90  PRO A CG  1 
ATOM   754  C CD  . PRO A 1 90 ? 4.763   33.685 -47.928 1.00 21.67 ? 90  PRO A CD  1 
ATOM   755  N N   . VAL A 1 91 ? 2.286   37.111 -49.876 1.00 18.34 ? 91  VAL A N   1 
ATOM   756  C CA  . VAL A 1 91 ? 1.120   37.972 -49.770 1.00 17.97 ? 91  VAL A CA  1 
ATOM   757  C C   . VAL A 1 91 ? 0.239   37.609 -50.958 1.00 18.57 ? 91  VAL A C   1 
ATOM   758  O O   . VAL A 1 91 ? 0.719   37.108 -51.990 1.00 16.16 ? 91  VAL A O   1 
ATOM   759  C CB  . VAL A 1 91 ? 1.500   39.536 -49.826 1.00 18.26 ? 91  VAL A CB  1 
ATOM   760  C CG1 . VAL A 1 91 ? 2.463   39.840 -48.690 1.00 21.33 ? 91  VAL A CG1 1 
ATOM   761  C CG2 . VAL A 1 91 ? 2.193   39.958 -51.112 1.00 17.06 ? 91  VAL A CG2 1 
ATOM   762  N N   . PRO A 1 92 ? -1.081  37.822 -50.899 1.00 21.20 ? 92  PRO A N   1 
ATOM   763  C CA  . PRO A 1 92 ? -1.958  37.595 -52.045 1.00 23.30 ? 92  PRO A CA  1 
ATOM   764  C C   . PRO A 1 92 ? -1.707  38.617 -53.164 1.00 22.73 ? 92  PRO A C   1 
ATOM   765  O O   . PRO A 1 92 ? -1.311  39.747 -52.870 1.00 24.63 ? 92  PRO A O   1 
ATOM   766  C CB  . PRO A 1 92 ? -3.314  37.656 -51.387 1.00 22.86 ? 92  PRO A CB  1 
ATOM   767  C CG  . PRO A 1 92 ? -3.149  38.660 -50.281 1.00 22.89 ? 92  PRO A CG  1 
ATOM   768  C CD  . PRO A 1 92 ? -1.797  38.322 -49.729 1.00 21.24 ? 92  PRO A CD  1 
ATOM   769  N N   . PRO A 1 93 ? -1.874  38.309 -54.443 1.00 23.60 ? 93  PRO A N   1 
ATOM   770  C CA  . PRO A 1 93 ? -1.737  39.269 -55.534 1.00 24.95 ? 93  PRO A CA  1 
ATOM   771  C C   . PRO A 1 93 ? -2.651  40.452 -55.324 1.00 25.50 ? 93  PRO A C   1 
ATOM   772  O O   . PRO A 1 93 ? -3.711  40.238 -54.742 1.00 27.18 ? 93  PRO A O   1 
ATOM   773  C CB  . PRO A 1 93 ? -2.072  38.507 -56.786 1.00 25.75 ? 93  PRO A CB  1 
ATOM   774  C CG  . PRO A 1 93 ? -1.839  37.056 -56.389 1.00 26.79 ? 93  PRO A CG  1 
ATOM   775  C CD  . PRO A 1 93 ? -2.326  37.018 -54.943 1.00 26.09 ? 93  PRO A CD  1 
ATOM   776  N N   . PRO A 1 94 ? -2.303  41.668 -55.715 1.00 27.86 ? 94  PRO A N   1 
ATOM   777  C CA  . PRO A 1 94 ? -3.191  42.819 -55.597 1.00 28.36 ? 94  PRO A CA  1 
ATOM   778  C C   . PRO A 1 94 ? -4.260  42.851 -56.706 1.00 29.39 ? 94  PRO A C   1 
ATOM   779  O O   . PRO A 1 94 ? -4.086  42.236 -57.771 1.00 27.52 ? 94  PRO A O   1 
ATOM   780  C CB  . PRO A 1 94 ? -2.234  43.963 -55.621 1.00 27.34 ? 94  PRO A CB  1 
ATOM   781  C CG  . PRO A 1 94 ? -1.231  43.531 -56.697 1.00 27.13 ? 94  PRO A CG  1 
ATOM   782  C CD  . PRO A 1 94 ? -1.036  42.048 -56.360 1.00 27.26 ? 94  PRO A CD  1 
ATOM   783  O OXT . PRO A 1 94 ? -5.290  43.482 -56.460 1.00 36.83 ? 94  PRO A OXT 1 
ATOM   784  N N   . GLY B 1 1  ? -5.240  44.882 -63.026 1.00 44.20 ? 1   GLY B N   1 
ATOM   785  C CA  . GLY B 1 1  ? -6.303  45.888 -62.994 1.00 43.11 ? 1   GLY B CA  1 
ATOM   786  C C   . GLY B 1 1  ? -5.612  47.132 -63.506 1.00 40.95 ? 1   GLY B C   1 
ATOM   787  O O   . GLY B 1 1  ? -4.540  47.016 -64.112 1.00 42.05 ? 1   GLY B O   1 
ATOM   788  N N   . GLU B 1 2  ? -6.305  48.248 -63.383 1.00 38.32 ? 2   GLU B N   1 
ATOM   789  C CA  . GLU B 1 2  ? -5.745  49.548 -63.669 1.00 34.12 ? 2   GLU B CA  1 
ATOM   790  C C   . GLU B 1 2  ? -5.802  50.161 -62.273 1.00 29.65 ? 2   GLU B C   1 
ATOM   791  O O   . GLU B 1 2  ? -6.756  49.948 -61.523 1.00 27.41 ? 2   GLU B O   1 
ATOM   792  C CB  . GLU B 1 2  ? -6.628  50.275 -64.661 1.00 38.47 ? 2   GLU B CB  1 
ATOM   793  C CG  . GLU B 1 2  ? -6.402  51.780 -64.749 1.00 44.25 ? 2   GLU B CG  1 
ATOM   794  C CD  . GLU B 1 2  ? -7.725  52.520 -64.924 1.00 49.27 ? 2   GLU B CD  1 
ATOM   795  O OE1 . GLU B 1 2  ? -8.501  52.135 -65.815 1.00 51.70 ? 2   GLU B OE1 1 
ATOM   796  O OE2 . GLU B 1 2  ? -7.965  53.467 -64.161 1.00 51.02 ? 2   GLU B OE2 1 
ATOM   797  N N   . TRP B 1 3  ? -4.774  50.929 -61.946 1.00 24.10 ? 3   TRP B N   1 
ATOM   798  C CA  . TRP B 1 3  ? -4.579  51.371 -60.567 1.00 23.59 ? 3   TRP B CA  1 
ATOM   799  C C   . TRP B 1 3  ? -4.417  52.868 -60.490 1.00 21.56 ? 3   TRP B C   1 
ATOM   800  O O   . TRP B 1 3  ? -3.709  53.428 -61.327 1.00 21.84 ? 3   TRP B O   1 
ATOM   801  C CB  . TRP B 1 3  ? -3.322  50.760 -59.966 1.00 21.15 ? 3   TRP B CB  1 
ATOM   802  C CG  . TRP B 1 3  ? -3.443  49.289 -59.677 1.00 19.39 ? 3   TRP B CG  1 
ATOM   803  C CD1 . TRP B 1 3  ? -2.996  48.332 -60.559 1.00 19.12 ? 3   TRP B CD1 1 
ATOM   804  C CD2 . TRP B 1 3  ? -3.937  48.786 -58.518 1.00 19.73 ? 3   TRP B CD2 1 
ATOM   805  N NE1 . TRP B 1 3  ? -3.202  47.197 -59.935 1.00 22.60 ? 3   TRP B NE1 1 
ATOM   806  C CE2 . TRP B 1 3  ? -3.755  47.425 -58.722 1.00 20.02 ? 3   TRP B CE2 1 
ATOM   807  C CE3 . TRP B 1 3  ? -4.477  49.298 -57.362 1.00 20.36 ? 3   TRP B CE3 1 
ATOM   808  C CZ2 . TRP B 1 3  ? -4.107  46.536 -57.738 1.00 19.28 ? 3   TRP B CZ2 1 
ATOM   809  C CZ3 . TRP B 1 3  ? -4.823  48.396 -56.376 1.00 23.48 ? 3   TRP B CZ3 1 
ATOM   810  C CH2 . TRP B 1 3  ? -4.644  47.035 -56.575 1.00 20.47 ? 3   TRP B CH2 1 
ATOM   811  N N   . GLU B 1 4  ? -5.035  53.561 -59.555 1.00 19.50 ? 4   GLU B N   1 
ATOM   812  C CA  . GLU B 1 4  ? -4.771  54.978 -59.428 1.00 19.82 ? 4   GLU B CA  1 
ATOM   813  C C   . GLU B 1 4  ? -4.862  55.354 -57.981 1.00 18.93 ? 4   GLU B C   1 
ATOM   814  O O   . GLU B 1 4  ? -5.430  54.593 -57.213 1.00 18.87 ? 4   GLU B O   1 
ATOM   815  C CB  . GLU B 1 4  ? -5.781  55.766 -60.238 1.00 21.81 ? 4   GLU B CB  1 
ATOM   816  C CG  . GLU B 1 4  ? -7.168  55.761 -59.698 1.00 29.93 ? 4   GLU B CG  1 
ATOM   817  C CD  . GLU B 1 4  ? -8.131  56.324 -60.721 1.00 35.16 ? 4   GLU B CD  1 
ATOM   818  O OE1 . GLU B 1 4  ? -8.196  57.554 -60.863 1.00 35.68 ? 4   GLU B OE1 1 
ATOM   819  O OE2 . GLU B 1 4  ? -8.788  55.499 -61.364 1.00 36.75 ? 4   GLU B OE2 1 
ATOM   820  N N   . ILE B 1 5  ? -4.296  56.472 -57.562 1.00 18.77 ? 5   ILE B N   1 
ATOM   821  C CA  . ILE B 1 5  ? -4.440  56.960 -56.211 1.00 19.79 ? 5   ILE B CA  1 
ATOM   822  C C   . ILE B 1 5  ? -5.560  57.980 -56.266 1.00 20.52 ? 5   ILE B C   1 
ATOM   823  O O   . ILE B 1 5  ? -5.572  58.823 -57.176 1.00 19.58 ? 5   ILE B O   1 
ATOM   824  C CB  . ILE B 1 5  ? -3.101  57.597 -55.772 1.00 20.91 ? 5   ILE B CB  1 
ATOM   825  C CG1 . ILE B 1 5  ? -2.166  56.469 -55.433 1.00 21.54 ? 5   ILE B CG1 1 
ATOM   826  C CG2 . ILE B 1 5  ? -3.219  58.474 -54.562 1.00 16.92 ? 5   ILE B CG2 1 
ATOM   827  C CD1 . ILE B 1 5  ? -0.810  56.880 -55.986 1.00 22.25 ? 5   ILE B CD1 1 
ATOM   828  N N   . ILE B 1 6  ? -6.513  57.901 -55.340 1.00 18.76 ? 6   ILE B N   1 
ATOM   829  C CA  . ILE B 1 6  ? -7.540  58.903 -55.311 1.00 22.08 ? 6   ILE B CA  1 
ATOM   830  C C   . ILE B 1 6  ? -7.347  59.812 -54.102 1.00 24.68 ? 6   ILE B C   1 
ATOM   831  O O   . ILE B 1 6  ? -6.736  59.443 -53.099 1.00 24.38 ? 6   ILE B O   1 
ATOM   832  C CB  . ILE B 1 6  ? -8.967  58.229 -55.305 1.00 21.74 ? 6   ILE B CB  1 
ATOM   833  C CG1 . ILE B 1 6  ? -9.200  57.288 -54.127 1.00 20.30 ? 6   ILE B CG1 1 
ATOM   834  C CG2 . ILE B 1 6  ? -9.100  57.590 -56.703 1.00 21.05 ? 6   ILE B CG2 1 
ATOM   835  C CD1 . ILE B 1 6  ? -10.610 56.668 -54.066 1.00 22.92 ? 6   ILE B CD1 1 
ATOM   836  N N   . ASP B 1 7  ? -7.864  61.031 -54.178 1.00 28.07 ? 7   ASP B N   1 
ATOM   837  C CA  . ASP B 1 7  ? -7.690  61.976 -53.097 1.00 32.36 ? 7   ASP B CA  1 
ATOM   838  C C   . ASP B 1 7  ? -8.607  61.656 -51.932 1.00 34.22 ? 7   ASP B C   1 
ATOM   839  O O   . ASP B 1 7  ? -9.644  61.032 -52.140 1.00 37.72 ? 7   ASP B O   1 
ATOM   840  C CB  . ASP B 1 7  ? -7.960  63.373 -53.647 1.00 37.44 ? 7   ASP B CB  1 
ATOM   841  C CG  . ASP B 1 7  ? -7.093  63.782 -54.853 1.00 40.44 ? 7   ASP B CG  1 
ATOM   842  O OD1 . ASP B 1 7  ? -5.953  63.319 -54.997 1.00 43.69 ? 7   ASP B OD1 1 
ATOM   843  O OD2 . ASP B 1 7  ? -7.584  64.572 -55.665 1.00 43.70 ? 7   ASP B OD2 1 
ATOM   844  N N   . ILE B 1 8  ? -8.313  62.068 -50.693 1.00 34.59 ? 8   ILE B N   1 
ATOM   845  C CA  . ILE B 1 8  ? -9.120  61.672 -49.527 1.00 32.84 ? 8   ILE B CA  1 
ATOM   846  C C   . ILE B 1 8  ? -10.305 62.539 -49.051 1.00 31.76 ? 8   ILE B C   1 
ATOM   847  O O   . ILE B 1 8  ? -10.490 62.785 -47.850 1.00 36.12 ? 8   ILE B O   1 
ATOM   848  C CB  . ILE B 1 8  ? -8.172  61.424 -48.292 1.00 31.29 ? 8   ILE B CB  1 
ATOM   849  C CG1 . ILE B 1 8  ? -7.318  62.617 -48.064 1.00 30.38 ? 8   ILE B CG1 1 
ATOM   850  C CG2 . ILE B 1 8  ? -7.354  60.152 -48.506 1.00 28.86 ? 8   ILE B CG2 1 
ATOM   851  C CD1 . ILE B 1 8  ? -7.304  62.984 -46.584 1.00 35.75 ? 8   ILE B CD1 1 
ATOM   852  N N   . GLY B 1 9  ? -11.196 62.933 -49.952 1.00 28.51 ? 9   GLY B N   1 
ATOM   853  C CA  . GLY B 1 9  ? -12.313 63.756 -49.587 1.00 23.26 ? 9   GLY B CA  1 
ATOM   854  C C   . GLY B 1 9  ? -13.470 62.947 -49.042 1.00 23.61 ? 9   GLY B C   1 
ATOM   855  O O   . GLY B 1 9  ? -13.309 61.851 -48.488 1.00 22.87 ? 9   GLY B O   1 
ATOM   856  N N   . PRO B 1 10 ? -14.687 63.456 -49.226 1.00 22.98 ? 10  PRO B N   1 
ATOM   857  C CA  . PRO B 1 10 ? -15.939 62.867 -48.762 1.00 22.16 ? 10  PRO B CA  1 
ATOM   858  C C   . PRO B 1 10 ? -16.195 61.444 -49.230 1.00 22.09 ? 10  PRO B C   1 
ATOM   859  O O   . PRO B 1 10 ? -16.679 60.628 -48.439 1.00 20.44 ? 10  PRO B O   1 
ATOM   860  C CB  . PRO B 1 10 ? -17.023 63.806 -49.241 1.00 22.86 ? 10  PRO B CB  1 
ATOM   861  C CG  . PRO B 1 10 ? -16.320 65.126 -49.345 1.00 24.04 ? 10  PRO B CG  1 
ATOM   862  C CD  . PRO B 1 10 ? -14.963 64.718 -49.909 1.00 24.27 ? 10  PRO B CD  1 
ATOM   863  N N   . PHE B 1 11 ? -15.860 61.121 -50.495 1.00 21.67 ? 11  PHE B N   1 
ATOM   864  C CA  . PHE B 1 11 ? -16.068 59.769 -51.014 1.00 21.12 ? 11  PHE B CA  1 
ATOM   865  C C   . PHE B 1 11 ? -15.251 58.753 -50.245 1.00 19.54 ? 11  PHE B C   1 
ATOM   866  O O   . PHE B 1 11 ? -15.809 57.750 -49.788 1.00 18.77 ? 11  PHE B O   1 
ATOM   867  C CB  . PHE B 1 11 ? -15.670 59.664 -52.486 1.00 21.31 ? 11  PHE B CB  1 
ATOM   868  C CG  . PHE B 1 11 ? -15.906 58.296 -53.136 1.00 23.12 ? 11  PHE B CG  1 
ATOM   869  C CD1 . PHE B 1 11 ? -17.195 57.870 -53.406 1.00 20.47 ? 11  PHE B CD1 1 
ATOM   870  C CD2 . PHE B 1 11 ? -14.825 57.488 -53.473 1.00 22.22 ? 11  PHE B CD2 1 
ATOM   871  C CE1 . PHE B 1 11 ? -17.391 56.649 -54.009 1.00 20.81 ? 11  PHE B CE1 1 
ATOM   872  C CE2 . PHE B 1 11 ? -15.058 56.272 -54.084 1.00 19.89 ? 11  PHE B CE2 1 
ATOM   873  C CZ  . PHE B 1 11 ? -16.329 55.850 -54.351 1.00 19.95 ? 11  PHE B CZ  1 
ATOM   874  N N   . THR B 1 12 ? -13.959 58.999 -50.055 1.00 20.34 ? 12  THR B N   1 
ATOM   875  C CA  . THR B 1 12 ? -13.136 58.018 -49.371 1.00 21.52 ? 12  THR B CA  1 
ATOM   876  C C   . THR B 1 12 ? -13.439 57.957 -47.884 1.00 20.65 ? 12  THR B C   1 
ATOM   877  O O   . THR B 1 12 ? -13.430 56.858 -47.313 1.00 19.40 ? 12  THR B O   1 
ATOM   878  C CB  . THR B 1 12 ? -11.665 58.321 -49.629 1.00 24.73 ? 12  THR B CB  1 
ATOM   879  O OG1 . THR B 1 12 ? -11.322 59.530 -48.964 1.00 31.17 ? 12  THR B OG1 1 
ATOM   880  C CG2 . THR B 1 12 ? -11.415 58.434 -51.136 1.00 24.91 ? 12  THR B CG2 1 
ATOM   881  N N   . GLN B 1 13 ? -13.818 59.084 -47.257 1.00 18.84 ? 13  GLN B N   1 
ATOM   882  C CA  . GLN B 1 13 ? -14.231 59.041 -45.861 1.00 19.19 ? 13  GLN B CA  1 
ATOM   883  C C   . GLN B 1 13 ? -15.404 58.100 -45.727 1.00 19.22 ? 13  GLN B C   1 
ATOM   884  O O   . GLN B 1 13 ? -15.425 57.279 -44.807 1.00 19.78 ? 13  GLN B O   1 
ATOM   885  C CB  . GLN B 1 13 ? -14.661 60.438 -45.304 1.00 20.16 ? 13  GLN B CB  1 
ATOM   886  C CG  . GLN B 1 13 ? -13.515 61.466 -45.174 1.00 22.95 ? 13  GLN B CG  1 
ATOM   887  C CD  . GLN B 1 13 ? -12.172 60.859 -44.701 1.00 26.13 ? 13  GLN B CD  1 
ATOM   888  O OE1 . GLN B 1 13 ? -12.108 60.154 -43.668 1.00 21.96 ? 13  GLN B OE1 1 
ATOM   889  N NE2 . GLN B 1 13 ? -11.082 61.054 -45.474 1.00 22.50 ? 13  GLN B NE2 1 
ATOM   890  N N   . ASN B 1 14 ? -16.348 58.132 -46.688 1.00 19.63 ? 14  ASN B N   1 
ATOM   891  C CA  . ASN B 1 14 ? -17.515 57.271 -46.627 1.00 19.38 ? 14  ASN B CA  1 
ATOM   892  C C   . ASN B 1 14 ? -17.157 55.805 -46.801 1.00 18.49 ? 14  ASN B C   1 
ATOM   893  O O   . ASN B 1 14 ? -17.770 54.904 -46.218 1.00 15.76 ? 14  ASN B O   1 
ATOM   894  C CB  . ASN B 1 14 ? -18.523 57.671 -47.700 1.00 27.38 ? 14  ASN B CB  1 
ATOM   895  C CG  . ASN B 1 14 ? -19.850 56.966 -47.410 1.00 35.79 ? 14  ASN B CG  1 
ATOM   896  O OD1 . ASN B 1 14 ? -20.347 57.070 -46.274 1.00 40.45 ? 14  ASN B OD1 1 
ATOM   897  N ND2 . ASN B 1 14 ? -20.551 56.288 -48.329 1.00 38.49 ? 14  ASN B ND2 1 
ATOM   898  N N   . LEU B 1 15 ? -16.121 55.528 -47.621 1.00 18.34 ? 15  LEU B N   1 
ATOM   899  C CA  . LEU B 1 15 ? -15.615 54.169 -47.777 1.00 17.06 ? 15  LEU B CA  1 
ATOM   900  C C   . LEU B 1 15 ? -15.034 53.719 -46.434 1.00 16.73 ? 15  LEU B C   1 
ATOM   901  O O   . LEU B 1 15 ? -15.262 52.574 -46.019 1.00 14.79 ? 15  LEU B O   1 
ATOM   902  C CB  . LEU B 1 15 ? -14.525 54.124 -48.853 1.00 18.63 ? 15  LEU B CB  1 
ATOM   903  C CG  . LEU B 1 15 ? -14.901 54.175 -50.332 1.00 18.81 ? 15  LEU B CG  1 
ATOM   904  C CD1 . LEU B 1 15 ? -13.631 54.376 -51.118 1.00 18.28 ? 15  LEU B CD1 1 
ATOM   905  C CD2 . LEU B 1 15 ? -15.636 52.901 -50.755 1.00 16.79 ? 15  LEU B CD2 1 
ATOM   906  N N   . GLY B 1 16 ? -14.315 54.574 -45.683 1.00 15.35 ? 16  GLY B N   1 
ATOM   907  C CA  . GLY B 1 16 ? -13.760 54.217 -44.367 1.00 15.35 ? 16  GLY B CA  1 
ATOM   908  C C   . GLY B 1 16 ? -14.837 53.916 -43.328 1.00 17.90 ? 16  GLY B C   1 
ATOM   909  O O   . GLY B 1 16 ? -14.736 52.928 -42.574 1.00 15.19 ? 16  GLY B O   1 
ATOM   910  N N   . LYS B 1 17 ? -15.881 54.762 -43.299 1.00 15.69 ? 17  LYS B N   1 
ATOM   911  C CA  . LYS B 1 17 ? -17.023 54.467 -42.458 1.00 17.86 ? 17  LYS B CA  1 
ATOM   912  C C   . LYS B 1 17 ? -17.688 53.100 -42.799 1.00 17.28 ? 17  LYS B C   1 
ATOM   913  O O   . LYS B 1 17 ? -18.013 52.324 -41.903 1.00 16.38 ? 17  LYS B O   1 
ATOM   914  C CB  . LYS B 1 17 ? -17.997 55.652 -42.591 1.00 22.33 ? 17  LYS B CB  1 
ATOM   915  C CG  . LYS B 1 17 ? -19.253 55.303 -41.794 1.00 31.01 ? 17  LYS B CG  1 
ATOM   916  C CD  . LYS B 1 17 ? -20.442 56.245 -41.877 1.00 36.53 ? 17  LYS B CD  1 
ATOM   917  C CE  . LYS B 1 17 ? -21.705 55.478 -41.397 1.00 38.24 ? 17  LYS B CE  1 
ATOM   918  N NZ  . LYS B 1 17 ? -21.578 54.930 -40.053 1.00 41.13 ? 17  LYS B NZ  1 
ATOM   919  N N   . PHE B 1 18 ? -17.857 52.699 -44.055 1.00 18.00 ? 18  PHE B N   1 
ATOM   920  C CA  . PHE B 1 18 ? -18.380 51.399 -44.457 1.00 16.99 ? 18  PHE B CA  1 
ATOM   921  C C   . PHE B 1 18 ? -17.506 50.303 -43.903 1.00 16.10 ? 18  PHE B C   1 
ATOM   922  O O   . PHE B 1 18 ? -18.024 49.331 -43.368 1.00 16.52 ? 18  PHE B O   1 
ATOM   923  C CB  . PHE B 1 18 ? -18.434 51.305 -46.026 1.00 17.43 ? 18  PHE B CB  1 
ATOM   924  C CG  . PHE B 1 18 ? -18.724 49.902 -46.561 1.00 19.39 ? 18  PHE B CG  1 
ATOM   925  C CD1 . PHE B 1 18 ? -20.020 49.390 -46.533 1.00 19.67 ? 18  PHE B CD1 1 
ATOM   926  C CD2 . PHE B 1 18 ? -17.690 49.098 -46.985 1.00 16.29 ? 18  PHE B CD2 1 
ATOM   927  C CE1 . PHE B 1 18 ? -20.249 48.087 -46.918 1.00 17.96 ? 18  PHE B CE1 1 
ATOM   928  C CE2 . PHE B 1 18 ? -17.939 47.790 -47.368 1.00 18.74 ? 18  PHE B CE2 1 
ATOM   929  C CZ  . PHE B 1 18 ? -19.209 47.280 -47.337 1.00 17.79 ? 18  PHE B CZ  1 
ATOM   930  N N   . ALA B 1 19 ? -16.181 50.417 -44.052 1.00 15.50 ? 19  ALA B N   1 
ATOM   931  C CA  . ALA B 1 19 ? -15.243 49.409 -43.594 1.00 14.72 ? 19  ALA B CA  1 
ATOM   932  C C   . ALA B 1 19 ? -15.371 49.144 -42.105 1.00 17.92 ? 19  ALA B C   1 
ATOM   933  O O   . ALA B 1 19 ? -15.392 48.000 -41.617 1.00 18.37 ? 19  ALA B O   1 
ATOM   934  C CB  . ALA B 1 19 ? -13.836 49.867 -43.866 1.00 16.45 ? 19  ALA B CB  1 
ATOM   935  N N   . VAL B 1 20 ? -15.473 50.212 -41.319 1.00 20.12 ? 20  VAL B N   1 
ATOM   936  C CA  . VAL B 1 20 ? -15.611 50.053 -39.879 1.00 20.85 ? 20  VAL B CA  1 
ATOM   937  C C   . VAL B 1 20 ? -16.991 49.504 -39.494 1.00 21.47 ? 20  VAL B C   1 
ATOM   938  O O   . VAL B 1 20 ? -17.037 48.611 -38.650 1.00 23.40 ? 20  VAL B O   1 
ATOM   939  C CB  . VAL B 1 20 ? -15.291 51.429 -39.252 1.00 20.50 ? 20  VAL B CB  1 
ATOM   940  C CG1 . VAL B 1 20 ? -15.427 51.369 -37.730 1.00 20.40 ? 20  VAL B CG1 1 
ATOM   941  C CG2 . VAL B 1 20 ? -13.837 51.804 -39.613 1.00 17.83 ? 20  VAL B CG2 1 
ATOM   942  N N   . ASP B 1 21 ? -18.111 49.930 -40.099 1.00 21.16 ? 21  ASP B N   1 
ATOM   943  C CA  . ASP B 1 21 ? -19.455 49.395 -39.827 1.00 20.94 ? 21  ASP B CA  1 
ATOM   944  C C   . ASP B 1 21 ? -19.499 47.927 -40.205 1.00 19.74 ? 21  ASP B C   1 
ATOM   945  O O   . ASP B 1 21 ? -20.039 47.119 -39.461 1.00 19.56 ? 21  ASP B O   1 
ATOM   946  C CB  . ASP B 1 21 ? -20.558 50.075 -40.645 1.00 23.59 ? 21  ASP B CB  1 
ATOM   947  C CG  . ASP B 1 21 ? -20.910 51.518 -40.290 1.00 27.28 ? 21  ASP B CG  1 
ATOM   948  O OD1 . ASP B 1 21 ? -20.774 51.944 -39.143 1.00 29.55 ? 21  ASP B OD1 1 
ATOM   949  O OD2 . ASP B 1 21 ? -21.347 52.223 -41.193 1.00 30.70 ? 21  ASP B OD2 1 
ATOM   950  N N   . GLU B 1 22 ? -18.888 47.516 -41.309 1.00 18.19 ? 22  GLU B N   1 
ATOM   951  C CA  . GLU B 1 22 ? -18.789 46.100 -41.655 1.00 17.71 ? 22  GLU B CA  1 
ATOM   952  C C   . GLU B 1 22 ? -17.962 45.250 -40.703 1.00 19.52 ? 22  GLU B C   1 
ATOM   953  O O   . GLU B 1 22 ? -18.398 44.176 -40.271 1.00 18.74 ? 22  GLU B O   1 
ATOM   954  C CB  . GLU B 1 22 ? -18.196 45.894 -43.026 1.00 16.76 ? 22  GLU B CB  1 
ATOM   955  C CG  . GLU B 1 22 ? -19.119 46.370 -44.111 1.00 21.81 ? 22  GLU B CG  1 
ATOM   956  C CD  . GLU B 1 22 ? -20.481 45.700 -44.114 1.00 24.54 ? 22  GLU B CD  1 
ATOM   957  O OE1 . GLU B 1 22 ? -20.577 44.548 -44.482 1.00 25.91 ? 22  GLU B OE1 1 
ATOM   958  O OE2 . GLU B 1 22 ? -21.448 46.377 -43.801 1.00 25.74 ? 22  GLU B OE2 1 
ATOM   959  N N   . GLU B 1 23 ? -16.766 45.729 -40.338 1.00 19.00 ? 23  GLU B N   1 
ATOM   960  C CA  . GLU B 1 23 ? -15.915 45.008 -39.433 1.00 21.70 ? 23  GLU B CA  1 
ATOM   961  C C   . GLU B 1 23 ? -16.625 44.923 -38.073 1.00 24.04 ? 23  GLU B C   1 
ATOM   962  O O   . GLU B 1 23 ? -16.519 43.877 -37.407 1.00 24.85 ? 23  GLU B O   1 
ATOM   963  C CB  . GLU B 1 23 ? -14.570 45.726 -39.286 1.00 22.67 ? 23  GLU B CB  1 
ATOM   964  C CG  . GLU B 1 23 ? -13.586 44.980 -38.386 1.00 24.58 ? 23  GLU B CG  1 
ATOM   965  C CD  . GLU B 1 23 ? -13.220 43.551 -38.808 1.00 25.89 ? 23  GLU B CD  1 
ATOM   966  O OE1 . GLU B 1 23 ? -13.284 43.184 -39.977 1.00 27.29 ? 23  GLU B OE1 1 
ATOM   967  O OE2 . GLU B 1 23 ? -12.851 42.770 -37.944 1.00 32.57 ? 23  GLU B OE2 1 
ATOM   968  N N   . ASN B 1 24 ? -17.374 45.960 -37.660 1.00 22.33 ? 24  ASN B N   1 
ATOM   969  C CA  . ASN B 1 24 ? -18.130 45.852 -36.417 1.00 22.48 ? 24  ASN B CA  1 
ATOM   970  C C   . ASN B 1 24 ? -19.146 44.745 -36.377 1.00 24.61 ? 24  ASN B C   1 
ATOM   971  O O   . ASN B 1 24 ? -19.507 44.249 -35.313 1.00 25.20 ? 24  ASN B O   1 
ATOM   972  C CB  . ASN B 1 24 ? -18.874 47.115 -36.110 1.00 19.49 ? 24  ASN B CB  1 
ATOM   973  C CG  . ASN B 1 24 ? -17.999 48.123 -35.416 1.00 22.12 ? 24  ASN B CG  1 
ATOM   974  O OD1 . ASN B 1 24 ? -16.989 47.753 -34.820 1.00 23.87 ? 24  ASN B OD1 1 
ATOM   975  N ND2 . ASN B 1 24 ? -18.295 49.420 -35.401 1.00 21.86 ? 24  ASN B ND2 1 
ATOM   976  N N   . LYS B 1 25 ? -19.641 44.332 -37.549 1.00 28.18 ? 25  LYS B N   1 
ATOM   977  C CA  . LYS B 1 25 ? -20.603 43.224 -37.623 1.00 28.32 ? 25  LYS B CA  1 
ATOM   978  C C   . LYS B 1 25 ? -19.884 41.884 -37.426 1.00 30.68 ? 25  LYS B C   1 
ATOM   979  O O   . LYS B 1 25 ? -20.539 40.872 -37.187 1.00 32.66 ? 25  LYS B O   1 
ATOM   980  C CB  . LYS B 1 25 ? -21.312 43.248 -38.978 1.00 22.45 ? 25  LYS B CB  1 
ATOM   981  C CG  . LYS B 1 25 ? -22.195 44.441 -39.145 1.00 20.33 ? 25  LYS B CG  1 
ATOM   982  C CD  . LYS B 1 25 ? -22.771 44.390 -40.529 1.00 24.21 ? 25  LYS B CD  1 
ATOM   983  C CE  . LYS B 1 25 ? -23.353 45.725 -40.951 1.00 25.99 ? 25  LYS B CE  1 
ATOM   984  N NZ  . LYS B 1 25 ? -23.802 45.668 -42.339 1.00 28.96 ? 25  LYS B NZ  1 
ATOM   985  N N   . ILE B 1 26 ? -18.554 41.850 -37.531 1.00 30.39 ? 26  ILE B N   1 
ATOM   986  C CA  . ILE B 1 26 ? -17.808 40.618 -37.407 1.00 32.44 ? 26  ILE B CA  1 
ATOM   987  C C   . ILE B 1 26 ? -17.335 40.421 -35.978 1.00 33.40 ? 26  ILE B C   1 
ATOM   988  O O   . ILE B 1 26 ? -17.373 39.282 -35.525 1.00 34.64 ? 26  ILE B O   1 
ATOM   989  C CB  . ILE B 1 26 ? -16.603 40.626 -38.406 1.00 31.28 ? 26  ILE B CB  1 
ATOM   990  C CG1 . ILE B 1 26 ? -17.178 40.775 -39.808 1.00 30.73 ? 26  ILE B CG1 1 
ATOM   991  C CG2 . ILE B 1 26 ? -15.775 39.328 -38.330 1.00 31.18 ? 26  ILE B CG2 1 
ATOM   992  C CD1 . ILE B 1 26 ? -16.180 40.914 -40.948 1.00 31.79 ? 26  ILE B CD1 1 
ATOM   993  N N   . GLY B 1 27 ? -16.871 41.465 -35.284 1.00 33.84 ? 27  GLY B N   1 
ATOM   994  C CA  . GLY B 1 27 ? -16.473 41.365 -33.897 1.00 33.55 ? 27  GLY B CA  1 
ATOM   995  C C   . GLY B 1 27 ? -15.017 41.025 -33.638 1.00 34.13 ? 27  GLY B C   1 
ATOM   996  O O   . GLY B 1 27 ? -14.541 41.056 -32.511 1.00 32.50 ? 27  GLY B O   1 
ATOM   997  N N   . GLN B 1 28 ? -14.231 40.742 -34.670 1.00 36.02 ? 28  GLN B N   1 
ATOM   998  C CA  . GLN B 1 28 ? -12.828 40.386 -34.507 1.00 36.51 ? 28  GLN B CA  1 
ATOM   999  C C   . GLN B 1 28 ? -12.004 41.459 -33.787 1.00 35.81 ? 28  GLN B C   1 
ATOM   1000 O O   . GLN B 1 28 ? -11.074 41.124 -33.063 1.00 35.83 ? 28  GLN B O   1 
ATOM   1001 C CB  . GLN B 1 28 ? -12.252 40.129 -35.904 1.00 39.16 ? 28  GLN B CB  1 
ATOM   1002 C CG  . GLN B 1 28 ? -11.487 38.813 -35.985 1.00 44.45 ? 28  GLN B CG  1 
ATOM   1003 C CD  . GLN B 1 28 ? -10.182 38.882 -35.220 1.00 49.38 ? 28  GLN B CD  1 
ATOM   1004 O OE1 . GLN B 1 28 ? -9.312  39.679 -35.584 1.00 51.76 ? 28  GLN B OE1 1 
ATOM   1005 N NE2 . GLN B 1 28 ? -9.999  38.073 -34.174 1.00 50.73 ? 28  GLN B NE2 1 
ATOM   1006 N N   . TYR B 1 29 ? -12.403 42.749 -33.834 1.00 34.93 ? 29  TYR B N   1 
ATOM   1007 C CA  . TYR B 1 29 ? -11.615 43.803 -33.166 1.00 34.70 ? 29  TYR B CA  1 
ATOM   1008 C C   . TYR B 1 29 ? -12.471 44.476 -32.118 1.00 33.67 ? 29  TYR B C   1 
ATOM   1009 O O   . TYR B 1 29 ? -12.189 45.581 -31.691 1.00 35.05 ? 29  TYR B O   1 
ATOM   1010 C CB  . TYR B 1 29 ? -11.112 44.861 -34.198 1.00 31.46 ? 29  TYR B CB  1 
ATOM   1011 C CG  . TYR B 1 29 ? -10.030 44.313 -35.108 1.00 28.32 ? 29  TYR B CG  1 
ATOM   1012 C CD1 . TYR B 1 29 ? -8.744  44.228 -34.636 1.00 29.09 ? 29  TYR B CD1 1 
ATOM   1013 C CD2 . TYR B 1 29 ? -10.334 43.821 -36.350 1.00 27.46 ? 29  TYR B CD2 1 
ATOM   1014 C CE1 . TYR B 1 29 ? -7.758  43.634 -35.384 1.00 27.29 ? 29  TYR B CE1 1 
ATOM   1015 C CE2 . TYR B 1 29 ? -9.357  43.223 -37.107 1.00 26.65 ? 29  TYR B CE2 1 
ATOM   1016 C CZ  . TYR B 1 29 ? -8.072  43.144 -36.621 1.00 28.20 ? 29  TYR B CZ  1 
ATOM   1017 O OH  . TYR B 1 29 ? -7.053  42.588 -37.385 1.00 33.01 ? 29  TYR B OH  1 
ATOM   1018 N N   . GLY B 1 30 ? -13.528 43.862 -31.629 1.00 31.23 ? 30  GLY B N   1 
ATOM   1019 C CA  . GLY B 1 30 ? -14.379 44.570 -30.704 1.00 33.09 ? 30  GLY B CA  1 
ATOM   1020 C C   . GLY B 1 30 ? -15.117 45.655 -31.496 1.00 36.05 ? 30  GLY B C   1 
ATOM   1021 O O   . GLY B 1 30 ? -15.244 45.534 -32.716 1.00 38.17 ? 30  GLY B O   1 
ATOM   1022 N N   . ARG B 1 31 ? -15.518 46.720 -30.823 1.00 34.50 ? 31  ARG B N   1 
ATOM   1023 C CA  . ARG B 1 31 ? -16.352 47.741 -31.417 1.00 35.34 ? 31  ARG B CA  1 
ATOM   1024 C C   . ARG B 1 31 ? -15.410 48.870 -31.776 1.00 33.52 ? 31  ARG B C   1 
ATOM   1025 O O   . ARG B 1 31 ? -14.662 49.338 -30.927 1.00 36.06 ? 31  ARG B O   1 
ATOM   1026 C CB  . ARG B 1 31 ? -17.379 48.107 -30.359 1.00 38.06 ? 31  ARG B CB  1 
ATOM   1027 C CG  . ARG B 1 31 ? -17.957 49.498 -30.357 1.00 40.70 ? 31  ARG B CG  1 
ATOM   1028 C CD  . ARG B 1 31 ? -19.084 49.648 -31.310 1.00 44.13 ? 31  ARG B CD  1 
ATOM   1029 N NE  . ARG B 1 31 ? -18.753 50.806 -32.116 1.00 53.06 ? 31  ARG B NE  1 
ATOM   1030 C CZ  . ARG B 1 31 ? -19.654 51.724 -32.484 1.00 54.07 ? 31  ARG B CZ  1 
ATOM   1031 N NH1 . ARG B 1 31 ? -20.925 51.624 -32.091 1.00 55.64 ? 31  ARG B NH1 1 
ATOM   1032 N NH2 . ARG B 1 31 ? -19.257 52.753 -33.243 1.00 53.95 ? 31  ARG B NH2 1 
ATOM   1033 N N   . LEU B 1 32 ? -15.401 49.299 -33.024 1.00 29.93 ? 32  LEU B N   1 
ATOM   1034 C CA  . LEU B 1 32 ? -14.519 50.359 -33.446 1.00 26.10 ? 32  LEU B CA  1 
ATOM   1035 C C   . LEU B 1 32 ? -15.313 51.596 -33.743 1.00 23.86 ? 32  LEU B C   1 
ATOM   1036 O O   . LEU B 1 32 ? -16.481 51.508 -34.132 1.00 24.27 ? 32  LEU B O   1 
ATOM   1037 C CB  . LEU B 1 32 ? -13.771 49.913 -34.680 1.00 26.16 ? 32  LEU B CB  1 
ATOM   1038 C CG  . LEU B 1 32 ? -12.872 48.685 -34.542 1.00 28.31 ? 32  LEU B CG  1 
ATOM   1039 C CD1 . LEU B 1 32 ? -12.337 48.363 -35.907 1.00 28.69 ? 32  LEU B CD1 1 
ATOM   1040 C CD2 . LEU B 1 32 ? -11.695 48.932 -33.592 1.00 27.63 ? 32  LEU B CD2 1 
ATOM   1041 N N   . THR B 1 33 ? -14.728 52.756 -33.504 1.00 20.91 ? 33  THR B N   1 
ATOM   1042 C CA  . THR B 1 33 ? -15.313 54.026 -33.897 1.00 22.14 ? 33  THR B CA  1 
ATOM   1043 C C   . THR B 1 33 ? -14.458 54.591 -35.012 1.00 22.39 ? 33  THR B C   1 
ATOM   1044 O O   . THR B 1 33 ? -13.248 54.761 -34.836 1.00 24.80 ? 33  THR B O   1 
ATOM   1045 C CB  . THR B 1 33 ? -15.309 54.976 -32.718 1.00 23.55 ? 33  THR B CB  1 
ATOM   1046 O OG1 . THR B 1 33 ? -16.168 54.396 -31.740 1.00 31.58 ? 33  THR B OG1 1 
ATOM   1047 C CG2 . THR B 1 33 ? -15.797 56.379 -33.082 1.00 27.12 ? 33  THR B CG2 1 
ATOM   1048 N N   . PHE B 1 34 ? -15.036 54.836 -36.171 1.00 21.86 ? 34  PHE B N   1 
ATOM   1049 C CA  . PHE B 1 34 ? -14.332 55.373 -37.304 1.00 21.26 ? 34  PHE B CA  1 
ATOM   1050 C C   . PHE B 1 34 ? -13.851 56.739 -36.918 1.00 21.72 ? 34  PHE B C   1 
ATOM   1051 O O   . PHE B 1 34 ? -14.555 57.474 -36.240 1.00 24.95 ? 34  PHE B O   1 
ATOM   1052 C CB  . PHE B 1 34 ? -15.282 55.456 -38.480 1.00 21.03 ? 34  PHE B CB  1 
ATOM   1053 C CG  . PHE B 1 34 ? -14.794 56.274 -39.670 1.00 23.49 ? 34  PHE B CG  1 
ATOM   1054 C CD1 . PHE B 1 34 ? -13.729 55.839 -40.444 1.00 22.08 ? 34  PHE B CD1 1 
ATOM   1055 C CD2 . PHE B 1 34 ? -15.431 57.481 -39.967 1.00 23.32 ? 34  PHE B CD2 1 
ATOM   1056 C CE1 . PHE B 1 34 ? -13.297 56.608 -41.508 1.00 20.91 ? 34  PHE B CE1 1 
ATOM   1057 C CE2 . PHE B 1 34 ? -14.986 58.236 -41.032 1.00 22.54 ? 34  PHE B CE2 1 
ATOM   1058 C CZ  . PHE B 1 34 ? -13.918 57.798 -41.799 1.00 22.24 ? 34  PHE B CZ  1 
ATOM   1059 N N   . ASN B 1 35 ? -12.645 57.077 -37.325 1.00 24.19 ? 35  ASN B N   1 
ATOM   1060 C CA  . ASN B 1 35 ? -12.105 58.410 -37.129 1.00 24.94 ? 35  ASN B CA  1 
ATOM   1061 C C   . ASN B 1 35 ? -11.900 58.997 -38.519 1.00 25.85 ? 35  ASN B C   1 
ATOM   1062 O O   . ASN B 1 35 ? -12.661 59.919 -38.857 1.00 27.15 ? 35  ASN B O   1 
ATOM   1063 C CB  . ASN B 1 35 ? -10.796 58.322 -36.351 1.00 24.70 ? 35  ASN B CB  1 
ATOM   1064 C CG  . ASN B 1 35 ? -11.003 57.709 -34.988 1.00 28.39 ? 35  ASN B CG  1 
ATOM   1065 O OD1 . ASN B 1 35 ? -10.159 56.947 -34.509 1.00 31.09 ? 35  ASN B OD1 1 
ATOM   1066 N ND2 . ASN B 1 35 ? -12.147 57.912 -34.330 1.00 33.31 ? 35  ASN B ND2 1 
ATOM   1067 N N   . LYS B 1 36 ? -10.990 58.464 -39.365 1.00 22.67 ? 36  LYS B N   1 
ATOM   1068 C CA  . LYS B 1 36 ? -10.741 59.031 -40.679 1.00 22.43 ? 36  LYS B CA  1 
ATOM   1069 C C   . LYS B 1 36 ? -9.932  58.103 -41.561 1.00 19.86 ? 36  LYS B C   1 
ATOM   1070 O O   . LYS B 1 36 ? -9.280  57.195 -41.047 1.00 21.57 ? 36  LYS B O   1 
ATOM   1071 C CB  . LYS B 1 36 ? -9.960  60.358 -40.601 1.00 25.27 ? 36  LYS B CB  1 
ATOM   1072 C CG  . LYS B 1 36 ? -8.522  60.292 -40.096 1.00 29.20 ? 36  LYS B CG  1 
ATOM   1073 C CD  . LYS B 1 36 ? -8.084  61.733 -39.909 1.00 34.21 ? 36  LYS B CD  1 
ATOM   1074 C CE  . LYS B 1 36 ? -6.707  61.765 -39.270 1.00 39.37 ? 36  LYS B CE  1 
ATOM   1075 N NZ  . LYS B 1 36 ? -6.298  63.134 -38.987 1.00 41.93 ? 36  LYS B NZ  1 
ATOM   1076 N N   . VAL B 1 37 ? -9.991  58.304 -42.864 1.00 17.80 ? 37  VAL B N   1 
ATOM   1077 C CA  . VAL B 1 37 ? -9.171  57.602 -43.842 1.00 18.47 ? 37  VAL B CA  1 
ATOM   1078 C C   . VAL B 1 37 ? -8.017  58.546 -44.176 1.00 19.93 ? 37  VAL B C   1 
ATOM   1079 O O   . VAL B 1 37 ? -8.252  59.760 -44.327 1.00 19.98 ? 37  VAL B O   1 
ATOM   1080 C CB  . VAL B 1 37 ? -9.999  57.274 -45.125 1.00 19.04 ? 37  VAL B CB  1 
ATOM   1081 C CG1 . VAL B 1 37 ? -9.128  56.769 -46.259 1.00 16.80 ? 37  VAL B CG1 1 
ATOM   1082 C CG2 . VAL B 1 37 ? -10.936 56.115 -44.828 1.00 16.67 ? 37  VAL B CG2 1 
ATOM   1083 N N   . ILE B 1 38 ? -6.792  58.053 -44.322 1.00 19.39 ? 38  ILE B N   1 
ATOM   1084 C CA  . ILE B 1 38 ? -5.651  58.929 -44.640 1.00 18.79 ? 38  ILE B CA  1 
ATOM   1085 C C   . ILE B 1 38 ? -5.064  58.506 -45.969 1.00 19.45 ? 38  ILE B C   1 
ATOM   1086 O O   . ILE B 1 38 ? -5.435  57.486 -46.543 1.00 19.18 ? 38  ILE B O   1 
ATOM   1087 C CB  . ILE B 1 38 ? -4.531  58.856 -43.546 1.00 18.78 ? 38  ILE B CB  1 
ATOM   1088 C CG1 . ILE B 1 38 ? -3.964  57.424 -43.469 1.00 16.57 ? 38  ILE B CG1 1 
ATOM   1089 C CG2 . ILE B 1 38 ? -5.097  59.418 -42.209 1.00 17.93 ? 38  ILE B CG2 1 
ATOM   1090 C CD1 . ILE B 1 38 ? -2.968  57.138 -42.345 1.00 13.55 ? 38  ILE B CD1 1 
ATOM   1091 N N   . ARG B 1 39 ? -4.138  59.290 -46.500 1.00 17.68 ? 39  ARG B N   1 
ATOM   1092 C CA  . ARG B 1 39 ? -3.490  58.958 -47.747 1.00 18.69 ? 39  ARG B CA  1 
ATOM   1093 C C   . ARG B 1 39 ? -2.481  57.858 -47.471 1.00 17.88 ? 39  ARG B C   1 
ATOM   1094 O O   . ARG B 1 39 ? -2.034  57.747 -46.319 1.00 17.68 ? 39  ARG B O   1 
ATOM   1095 C CB  . ARG B 1 39 ? -2.748  60.163 -48.307 1.00 22.93 ? 39  ARG B CB  1 
ATOM   1096 C CG  . ARG B 1 39 ? -3.574  61.364 -48.762 1.00 27.40 ? 39  ARG B CG  1 
ATOM   1097 C CD  . ARG B 1 39 ? -2.499  62.383 -49.138 1.00 33.82 ? 39  ARG B CD  1 
ATOM   1098 N NE  . ARG B 1 39 ? -1.887  62.921 -47.924 1.00 36.39 ? 39  ARG B NE  1 
ATOM   1099 C CZ  . ARG B 1 39 ? -0.770  63.659 -47.921 1.00 37.88 ? 39  ARG B CZ  1 
ATOM   1100 N NH1 . ARG B 1 39 ? -0.094  63.967 -49.024 1.00 36.92 ? 39  ARG B NH1 1 
ATOM   1101 N NH2 . ARG B 1 39 ? -0.315  64.093 -46.757 1.00 39.59 ? 39  ARG B NH2 1 
ATOM   1102 N N   . PRO B 1 40 ? -2.085  57.010 -48.424 1.00 15.54 ? 40  PRO B N   1 
ATOM   1103 C CA  . PRO B 1 40 ? -2.644  56.915 -49.761 1.00 17.18 ? 40  PRO B CA  1 
ATOM   1104 C C   . PRO B 1 40 ? -3.941  56.065 -49.889 1.00 15.56 ? 40  PRO B C   1 
ATOM   1105 O O   . PRO B 1 40 ? -4.097  55.042 -49.205 1.00 15.03 ? 40  PRO B O   1 
ATOM   1106 C CB  . PRO B 1 40 ? -1.480  56.361 -50.539 1.00 15.83 ? 40  PRO B CB  1 
ATOM   1107 C CG  . PRO B 1 40 ? -0.973  55.314 -49.556 1.00 13.97 ? 40  PRO B CG  1 
ATOM   1108 C CD  . PRO B 1 40 ? -1.002  56.044 -48.244 1.00 15.85 ? 40  PRO B CD  1 
ATOM   1109 N N   . CYS B 1 41 ? -4.850  56.431 -50.771 1.00 15.45 ? 41  CYS B N   1 
ATOM   1110 C CA  . CYS B 1 41 ? -5.978  55.556 -51.039 1.00 16.87 ? 41  CYS B CA  1 
ATOM   1111 C C   . CYS B 1 41 ? -5.796  55.055 -52.443 1.00 15.64 ? 41  CYS B C   1 
ATOM   1112 O O   . CYS B 1 41 ? -5.657  55.857 -53.357 1.00 15.85 ? 41  CYS B O   1 
ATOM   1113 C CB  . CYS B 1 41 ? -7.303  56.313 -50.927 1.00 18.97 ? 41  CYS B CB  1 
ATOM   1114 S SG  . CYS B 1 41 ? -8.686  55.190 -51.300 1.00 24.30 ? 41  CYS B SG  1 
ATOM   1115 N N   . MET B 1 42 ? -5.766  53.749 -52.663 1.00 15.21 ? 42  MET B N   1 
ATOM   1116 C CA  . MET B 1 42 ? -5.598  53.186 -53.987 1.00 18.43 ? 42  MET B CA  1 
ATOM   1117 C C   . MET B 1 42 ? -6.888  52.591 -54.518 1.00 17.37 ? 42  MET B C   1 
ATOM   1118 O O   . MET B 1 42 ? -7.623  51.913 -53.789 1.00 16.01 ? 42  MET B O   1 
ATOM   1119 C CB  . MET B 1 42 ? -4.602  52.065 -53.998 1.00 24.20 ? 42  MET B CB  1 
ATOM   1120 C CG  . MET B 1 42 ? -3.132  52.457 -53.913 1.00 32.67 ? 42  MET B CG  1 
ATOM   1121 S SD  . MET B 1 42 ? -2.286  51.074 -54.724 1.00 43.24 ? 42  MET B SD  1 
ATOM   1122 C CE  . MET B 1 42 ? -2.377  51.852 -56.302 1.00 37.53 ? 42  MET B CE  1 
ATOM   1123 N N   . LYS B 1 43 ? -7.097  52.785 -55.809 1.00 14.55 ? 43  LYS B N   1 
ATOM   1124 C CA  . LYS B 1 43 ? -8.294  52.310 -56.475 1.00 16.02 ? 43  LYS B CA  1 
ATOM   1125 C C   . LYS B 1 43 ? -7.926  51.444 -57.678 1.00 14.32 ? 43  LYS B C   1 
ATOM   1126 O O   . LYS B 1 43 ? -7.161  51.852 -58.546 1.00 13.68 ? 43  LYS B O   1 
ATOM   1127 C CB  . LYS B 1 43 ? -9.110  53.520 -56.917 1.00 17.72 ? 43  LYS B CB  1 
ATOM   1128 C CG  . LYS B 1 43 ? -10.379 53.134 -57.680 1.00 20.70 ? 43  LYS B CG  1 
ATOM   1129 C CD  . LYS B 1 43 ? -10.816 54.424 -58.347 1.00 27.11 ? 43  LYS B CD  1 
ATOM   1130 C CE  . LYS B 1 43 ? -11.966 54.218 -59.318 1.00 31.41 ? 43  LYS B CE  1 
ATOM   1131 N NZ  . LYS B 1 43 ? -12.161 55.391 -60.155 1.00 33.47 ? 43  LYS B NZ  1 
ATOM   1132 N N   . LYS B 1 44 ? -8.459  50.242 -57.740 1.00 13.38 ? 44  LYS B N   1 
ATOM   1133 C CA  . LYS B 1 44 ? -8.268  49.361 -58.881 1.00 16.54 ? 44  LYS B CA  1 
ATOM   1134 C C   . LYS B 1 44 ? -9.592  49.271 -59.665 1.00 18.14 ? 44  LYS B C   1 
ATOM   1135 O O   . LYS B 1 44 ? -10.657 48.984 -59.064 1.00 14.89 ? 44  LYS B O   1 
ATOM   1136 C CB  . LYS B 1 44 ? -7.897  47.964 -58.392 1.00 18.46 ? 44  LYS B CB  1 
ATOM   1137 C CG  . LYS B 1 44 ? -7.624  46.939 -59.495 1.00 22.11 ? 44  LYS B CG  1 
ATOM   1138 C CD  . LYS B 1 44 ? -7.589  45.570 -58.822 1.00 23.20 ? 44  LYS B CD  1 
ATOM   1139 C CE  . LYS B 1 44 ? -6.857  44.670 -59.791 1.00 28.54 ? 44  LYS B CE  1 
ATOM   1140 N NZ  . LYS B 1 44 ? -6.676  43.320 -59.286 1.00 31.02 ? 44  LYS B NZ  1 
ATOM   1141 N N   . THR B 1 45 ? -9.537  49.580 -60.962 1.00 16.64 ? 45  THR B N   1 
ATOM   1142 C CA  . THR B 1 45 ? -10.707 49.356 -61.803 1.00 17.33 ? 45  THR B CA  1 
ATOM   1143 C C   . THR B 1 45 ? -10.631 47.987 -62.515 1.00 18.98 ? 45  THR B C   1 
ATOM   1144 O O   . THR B 1 45 ? -9.594  47.573 -63.068 1.00 19.80 ? 45  THR B O   1 
ATOM   1145 C CB  . THR B 1 45 ? -10.817 50.541 -62.804 1.00 15.94 ? 45  THR B CB  1 
ATOM   1146 O OG1 . THR B 1 45 ? -10.944 51.743 -62.024 1.00 18.75 ? 45  THR B OG1 1 
ATOM   1147 C CG2 . THR B 1 45 ? -12.022 50.423 -63.736 1.00 18.53 ? 45  THR B CG2 1 
ATOM   1148 N N   . ILE B 1 46 ? -11.720 47.227 -62.431 1.00 18.53 ? 46  ILE B N   1 
ATOM   1149 C CA  . ILE B 1 46 ? -11.813 45.925 -63.062 1.00 21.28 ? 46  ILE B CA  1 
ATOM   1150 C C   . ILE B 1 46 ? -12.879 46.049 -64.146 1.00 22.75 ? 46  ILE B C   1 
ATOM   1151 O O   . ILE B 1 46 ? -13.969 46.605 -63.953 1.00 21.32 ? 46  ILE B O   1 
ATOM   1152 C CB  . ILE B 1 46 ? -12.203 44.887 -61.993 1.00 21.53 ? 46  ILE B CB  1 
ATOM   1153 C CG1 . ILE B 1 46 ? -11.153 44.820 -60.872 1.00 20.93 ? 46  ILE B CG1 1 
ATOM   1154 C CG2 . ILE B 1 46 ? -12.342 43.536 -62.669 1.00 22.90 ? 46  ILE B CG2 1 
ATOM   1155 C CD1 . ILE B 1 46 ? -11.779 44.744 -59.464 1.00 20.68 ? 46  ILE B CD1 1 
ATOM   1156 N N   . TYR B 1 47 ? -12.535 45.590 -65.338 1.00 25.98 ? 47  TYR B N   1 
ATOM   1157 C CA  . TYR B 1 47 ? -13.412 45.636 -66.507 1.00 28.90 ? 47  TYR B CA  1 
ATOM   1158 C C   . TYR B 1 47 ? -14.024 44.285 -66.832 1.00 29.81 ? 47  TYR B C   1 
ATOM   1159 O O   . TYR B 1 47 ? -13.421 43.231 -66.664 1.00 30.22 ? 47  TYR B O   1 
ATOM   1160 C CB  . TYR B 1 47 ? -12.651 46.109 -67.710 1.00 29.58 ? 47  TYR B CB  1 
ATOM   1161 C CG  . TYR B 1 47 ? -12.246 47.567 -67.597 1.00 33.36 ? 47  TYR B CG  1 
ATOM   1162 C CD1 . TYR B 1 47 ? -11.123 47.894 -66.864 1.00 35.25 ? 47  TYR B CD1 1 
ATOM   1163 C CD2 . TYR B 1 47 ? -13.012 48.544 -68.212 1.00 34.87 ? 47  TYR B CD2 1 
ATOM   1164 C CE1 . TYR B 1 47 ? -10.744 49.214 -66.747 1.00 38.97 ? 47  TYR B CE1 1 
ATOM   1165 C CE2 . TYR B 1 47 ? -12.641 49.867 -68.097 1.00 38.22 ? 47  TYR B CE2 1 
ATOM   1166 C CZ  . TYR B 1 47 ? -11.510 50.193 -67.357 1.00 38.45 ? 47  TYR B CZ  1 
ATOM   1167 O OH  . TYR B 1 47 ? -11.135 51.517 -67.214 1.00 39.87 ? 47  TYR B OH  1 
ATOM   1168 N N   . GLU B 1 48 ? -15.267 44.351 -67.264 1.00 32.88 ? 48  GLU B N   1 
ATOM   1169 C CA  . GLU B 1 48 ? -16.080 43.210 -67.656 1.00 35.72 ? 48  GLU B CA  1 
ATOM   1170 C C   . GLU B 1 48 ? -15.700 42.770 -69.056 1.00 36.40 ? 48  GLU B C   1 
ATOM   1171 O O   . GLU B 1 48 ? -15.604 41.582 -69.356 1.00 37.89 ? 48  GLU B O   1 
ATOM   1172 C CB  . GLU B 1 48 ? -17.544 43.605 -67.631 1.00 36.76 ? 48  GLU B CB  1 
ATOM   1173 C CG  . GLU B 1 48 ? -18.498 42.505 -68.032 1.00 39.60 ? 48  GLU B CG  1 
ATOM   1174 C CD  . GLU B 1 48 ? -18.383 41.238 -67.200 1.00 42.07 ? 48  GLU B CD  1 
ATOM   1175 O OE1 . GLU B 1 48 ? -18.773 41.231 -66.039 1.00 43.38 ? 48  GLU B OE1 1 
ATOM   1176 O OE2 . GLU B 1 48 ? -17.903 40.241 -67.728 1.00 44.06 ? 48  GLU B OE2 1 
ATOM   1177 N N   . ASN B 1 49 ? -15.520 43.764 -69.906 1.00 37.18 ? 49  ASN B N   1 
ATOM   1178 C CA  . ASN B 1 49 ? -15.111 43.586 -71.292 1.00 40.43 ? 49  ASN B CA  1 
ATOM   1179 C C   . ASN B 1 49 ? -14.652 44.948 -71.742 1.00 40.75 ? 49  ASN B C   1 
ATOM   1180 O O   . ASN B 1 49 ? -14.667 45.844 -70.912 1.00 40.35 ? 49  ASN B O   1 
ATOM   1181 C CB  . ASN B 1 49 ? -16.268 43.137 -72.196 1.00 39.84 ? 49  ASN B CB  1 
ATOM   1182 C CG  . ASN B 1 49 ? -17.554 43.894 -71.981 1.00 40.43 ? 49  ASN B CG  1 
ATOM   1183 O OD1 . ASN B 1 49 ? -17.647 45.100 -72.165 1.00 37.57 ? 49  ASN B OD1 1 
ATOM   1184 N ND2 . ASN B 1 49 ? -18.585 43.195 -71.564 1.00 42.07 ? 49  ASN B ND2 1 
ATOM   1185 N N   . GLU B 1 50 ? -14.328 45.182 -73.017 1.00 43.94 ? 50  GLU B N   1 
ATOM   1186 C CA  . GLU B 1 50 ? -13.849 46.483 -73.485 1.00 46.39 ? 50  GLU B CA  1 
ATOM   1187 C C   . GLU B 1 50 ? -14.884 47.589 -73.336 1.00 47.32 ? 50  GLU B C   1 
ATOM   1188 O O   . GLU B 1 50 ? -14.596 48.778 -73.492 1.00 47.39 ? 50  GLU B O   1 
ATOM   1189 C CB  . GLU B 1 50 ? -13.438 46.299 -74.933 1.00 49.56 ? 50  GLU B CB  1 
ATOM   1190 C CG  . GLU B 1 50 ? -13.121 47.522 -75.735 1.00 58.84 ? 50  GLU B CG  1 
ATOM   1191 C CD  . GLU B 1 50 ? -13.718 47.611 -77.139 1.00 65.41 ? 50  GLU B CD  1 
ATOM   1192 O OE1 . GLU B 1 50 ? -14.678 46.897 -77.451 1.00 68.81 ? 50  GLU B OE1 1 
ATOM   1193 O OE2 . GLU B 1 50 ? -13.228 48.428 -77.924 1.00 66.36 ? 50  GLU B OE2 1 
ATOM   1194 N N   . ARG B 1 51 ? -16.115 47.182 -73.040 1.00 46.84 ? 51  ARG B N   1 
ATOM   1195 C CA  . ARG B 1 51 ? -17.189 48.124 -72.947 1.00 47.46 ? 51  ARG B CA  1 
ATOM   1196 C C   . ARG B 1 51 ? -17.561 48.401 -71.498 1.00 45.94 ? 51  ARG B C   1 
ATOM   1197 O O   . ARG B 1 51 ? -17.678 49.563 -71.112 1.00 46.59 ? 51  ARG B O   1 
ATOM   1198 C CB  . ARG B 1 51 ? -18.377 47.555 -73.760 1.00 50.14 ? 51  ARG B CB  1 
ATOM   1199 C CG  . ARG B 1 51 ? -18.204 47.409 -75.301 1.00 53.76 ? 51  ARG B CG  1 
ATOM   1200 C CD  . ARG B 1 51 ? -18.002 45.989 -75.895 1.00 54.91 ? 51  ARG B CD  1 
ATOM   1201 N NE  . ARG B 1 51 ? -16.606 45.556 -76.004 1.00 56.42 ? 51  ARG B NE  1 
ATOM   1202 C CZ  . ARG B 1 51 ? -16.234 44.270 -75.876 1.00 56.99 ? 51  ARG B CZ  1 
ATOM   1203 N NH1 . ARG B 1 51 ? -17.085 43.272 -75.611 1.00 58.89 ? 51  ARG B NH1 1 
ATOM   1204 N NH2 . ARG B 1 51 ? -14.964 43.957 -76.001 1.00 54.53 ? 51  ARG B NH2 1 
ATOM   1205 N N   . GLU B 1 52 ? -17.700 47.410 -70.639 1.00 43.19 ? 52  GLU B N   1 
ATOM   1206 C CA  . GLU B 1 52 ? -18.217 47.697 -69.316 1.00 41.63 ? 52  GLU B CA  1 
ATOM   1207 C C   . GLU B 1 52 ? -17.183 47.508 -68.219 1.00 36.36 ? 52  GLU B C   1 
ATOM   1208 O O   . GLU B 1 52 ? -16.307 46.644 -68.329 1.00 33.93 ? 52  GLU B O   1 
ATOM   1209 C CB  . GLU B 1 52 ? -19.468 46.799 -69.107 1.00 46.05 ? 52  GLU B CB  1 
ATOM   1210 C CG  . GLU B 1 52 ? -20.242 46.740 -67.738 1.00 52.90 ? 52  GLU B CG  1 
ATOM   1211 C CD  . GLU B 1 52 ? -21.267 47.814 -67.319 1.00 54.11 ? 52  GLU B CD  1 
ATOM   1212 O OE1 . GLU B 1 52 ? -21.708 48.615 -68.149 1.00 55.44 ? 52  GLU B OE1 1 
ATOM   1213 O OE2 . GLU B 1 52 ? -21.638 47.826 -66.144 1.00 54.63 ? 52  GLU B OE2 1 
ATOM   1214 N N   . ILE B 1 53 ? -17.295 48.360 -67.196 1.00 30.47 ? 53  ILE B N   1 
ATOM   1215 C CA  . ILE B 1 53 ? -16.526 48.269 -65.965 1.00 25.52 ? 53  ILE B CA  1 
ATOM   1216 C C   . ILE B 1 53 ? -17.353 47.278 -65.171 1.00 21.54 ? 53  ILE B C   1 
ATOM   1217 O O   . ILE B 1 53 ? -18.578 47.347 -65.128 1.00 22.50 ? 53  ILE B O   1 
ATOM   1218 C CB  . ILE B 1 53 ? -16.460 49.633 -65.181 1.00 26.06 ? 53  ILE B CB  1 
ATOM   1219 C CG1 . ILE B 1 53 ? -15.634 50.603 -66.004 1.00 25.52 ? 53  ILE B CG1 1 
ATOM   1220 C CG2 . ILE B 1 53 ? -15.795 49.486 -63.795 1.00 25.23 ? 53  ILE B CG2 1 
ATOM   1221 C CD1 . ILE B 1 53 ? -15.845 52.054 -65.590 1.00 26.21 ? 53  ILE B CD1 1 
ATOM   1222 N N   . LYS B 1 54 ? -16.669 46.336 -64.554 1.00 21.17 ? 54  LYS B N   1 
ATOM   1223 C CA  . LYS B 1 54 ? -17.297 45.352 -63.695 1.00 21.41 ? 54  LYS B CA  1 
ATOM   1224 C C   . LYS B 1 54 ? -17.384 45.898 -62.249 1.00 19.78 ? 54  LYS B C   1 
ATOM   1225 O O   . LYS B 1 54 ? -18.440 45.818 -61.592 1.00 20.01 ? 54  LYS B O   1 
ATOM   1226 C CB  . LYS B 1 54 ? -16.482 44.030 -63.750 1.00 19.97 ? 54  LYS B CB  1 
ATOM   1227 C CG  . LYS B 1 54 ? -17.238 42.882 -63.077 1.00 27.13 ? 54  LYS B CG  1 
ATOM   1228 C CD  . LYS B 1 54 ? -18.764 42.901 -63.450 1.00 33.78 ? 54  LYS B CD  1 
ATOM   1229 C CE  . LYS B 1 54 ? -19.703 41.888 -62.757 1.00 38.69 ? 54  LYS B CE  1 
ATOM   1230 N NZ  . LYS B 1 54 ? -20.989 41.809 -63.444 1.00 40.38 ? 54  LYS B NZ  1 
ATOM   1231 N N   . GLY B 1 55 ? -16.325 46.524 -61.745 1.00 16.15 ? 55  GLY B N   1 
ATOM   1232 C CA  . GLY B 1 55 ? -16.360 47.029 -60.407 1.00 13.39 ? 55  GLY B CA  1 
ATOM   1233 C C   . GLY B 1 55 ? -14.995 47.569 -60.031 1.00 13.76 ? 55  GLY B C   1 
ATOM   1234 O O   . GLY B 1 55 ? -14.133 47.769 -60.904 1.00 13.91 ? 55  GLY B O   1 
ATOM   1235 N N   . TYR B 1 56 ? -14.810 47.812 -58.747 1.00 14.47 ? 56  TYR B N   1 
ATOM   1236 C CA  . TYR B 1 56 ? -13.615 48.491 -58.267 1.00 14.84 ? 56  TYR B CA  1 
ATOM   1237 C C   . TYR B 1 56 ? -13.179 47.785 -57.011 1.00 15.95 ? 56  TYR B C   1 
ATOM   1238 O O   . TYR B 1 56 ? -13.963 47.098 -56.346 1.00 14.74 ? 56  TYR B O   1 
ATOM   1239 C CB  . TYR B 1 56 ? -13.851 49.955 -57.854 1.00 15.02 ? 56  TYR B CB  1 
ATOM   1240 C CG  . TYR B 1 56 ? -14.522 50.792 -58.937 1.00 14.60 ? 56  TYR B CG  1 
ATOM   1241 C CD1 . TYR B 1 56 ? -13.782 51.338 -59.963 1.00 16.10 ? 56  TYR B CD1 1 
ATOM   1242 C CD2 . TYR B 1 56 ? -15.905 50.974 -58.860 1.00 16.00 ? 56  TYR B CD2 1 
ATOM   1243 C CE1 . TYR B 1 56 ? -14.432 52.077 -60.928 1.00 19.00 ? 56  TYR B CE1 1 
ATOM   1244 C CE2 . TYR B 1 56 ? -16.563 51.706 -59.808 1.00 15.55 ? 56  TYR B CE2 1 
ATOM   1245 C CZ  . TYR B 1 56 ? -15.812 52.251 -60.826 1.00 20.74 ? 56  TYR B CZ  1 
ATOM   1246 O OH  . TYR B 1 56 ? -16.465 53.039 -61.744 1.00 24.17 ? 56  TYR B OH  1 
ATOM   1247 N N   . GLU B 1 57 ? -11.915 47.984 -56.637 1.00 14.29 ? 57  GLU B N   1 
ATOM   1248 C CA  . GLU B 1 57 ? -11.430 47.520 -55.351 1.00 15.41 ? 57  GLU B CA  1 
ATOM   1249 C C   . GLU B 1 57 ? -10.614 48.666 -54.776 1.00 13.48 ? 57  GLU B C   1 
ATOM   1250 O O   . GLU B 1 57 ? -9.929  49.333 -55.561 1.00 15.56 ? 57  GLU B O   1 
ATOM   1251 C CB  . GLU B 1 57 ? -10.533 46.299 -55.503 1.00 17.19 ? 57  GLU B CB  1 
ATOM   1252 C CG  . GLU B 1 57 ? -11.341 45.030 -55.637 1.00 24.08 ? 57  GLU B CG  1 
ATOM   1253 C CD  . GLU B 1 57 ? -10.504 43.789 -55.930 1.00 28.35 ? 57  GLU B CD  1 
ATOM   1254 O OE1 . GLU B 1 57 ? -9.303  43.833 -55.660 1.00 31.71 ? 57  GLU B OE1 1 
ATOM   1255 O OE2 . GLU B 1 57 ? -11.043 42.798 -56.448 1.00 29.06 ? 57  GLU B OE2 1 
ATOM   1256 N N   . TYR B 1 58 ? -10.675 48.942 -53.473 1.00 13.23 ? 58  TYR B N   1 
ATOM   1257 C CA  . TYR B 1 58 ? -10.002 50.085 -52.869 1.00 14.59 ? 58  TYR B CA  1 
ATOM   1258 C C   . TYR B 1 58 ? -9.188  49.536 -51.727 1.00 15.14 ? 58  TYR B C   1 
ATOM   1259 O O   . TYR B 1 58 ? -9.634  48.628 -51.018 1.00 15.38 ? 58  TYR B O   1 
ATOM   1260 C CB  . TYR B 1 58 ? -10.959 51.103 -52.257 1.00 13.78 ? 58  TYR B CB  1 
ATOM   1261 C CG  . TYR B 1 58 ? -12.005 51.601 -53.240 1.00 14.42 ? 58  TYR B CG  1 
ATOM   1262 C CD1 . TYR B 1 58 ? -13.211 50.938 -53.375 1.00 14.47 ? 58  TYR B CD1 1 
ATOM   1263 C CD2 . TYR B 1 58 ? -11.729 52.734 -53.973 1.00 14.15 ? 58  TYR B CD2 1 
ATOM   1264 C CE1 . TYR B 1 58 ? -14.176 51.438 -54.223 1.00 15.97 ? 58  TYR B CE1 1 
ATOM   1265 C CE2 . TYR B 1 58 ? -12.701 53.242 -54.819 1.00 19.24 ? 58  TYR B CE2 1 
ATOM   1266 C CZ  . TYR B 1 58 ? -13.907 52.577 -54.940 1.00 17.82 ? 58  TYR B CZ  1 
ATOM   1267 O OH  . TYR B 1 58 ? -14.872 53.119 -55.757 1.00 21.22 ? 58  TYR B OH  1 
ATOM   1268 N N   . GLN B 1 59 ? -7.969  50.040 -51.603 1.00 14.42 ? 59  GLN B N   1 
ATOM   1269 C CA  . GLN B 1 59 ? -7.090  49.690 -50.492 1.00 15.13 ? 59  GLN B CA  1 
ATOM   1270 C C   . GLN B 1 59 ? -6.985  50.954 -49.640 1.00 13.90 ? 59  GLN B C   1 
ATOM   1271 O O   . GLN B 1 59 ? -6.516  52.007 -50.108 1.00 13.04 ? 59  GLN B O   1 
ATOM   1272 C CB  . GLN B 1 59 ? -5.695  49.312 -50.966 1.00 18.29 ? 59  GLN B CB  1 
ATOM   1273 C CG  . GLN B 1 59 ? -5.721  48.132 -51.943 1.00 24.27 ? 59  GLN B CG  1 
ATOM   1274 C CD  . GLN B 1 59 ? -4.335  47.559 -52.224 1.00 30.07 ? 59  GLN B CD  1 
ATOM   1275 O OE1 . GLN B 1 59 ? -3.311  48.146 -51.844 1.00 35.15 ? 59  GLN B OE1 1 
ATOM   1276 N NE2 . GLN B 1 59 ? -4.184  46.427 -52.887 1.00 33.44 ? 59  GLN B NE2 1 
ATOM   1277 N N   . LEU B 1 60 ? -7.441  50.892 -48.392 1.00 14.38 ? 60  LEU B N   1 
ATOM   1278 C CA  . LEU B 1 60 ? -7.510  52.052 -47.528 1.00 15.54 ? 60  LEU B CA  1 
ATOM   1279 C C   . LEU B 1 60 ? -6.657  51.894 -46.264 1.00 14.75 ? 60  LEU B C   1 
ATOM   1280 O O   . LEU B 1 60 ? -6.457  50.759 -45.780 1.00 13.98 ? 60  LEU B O   1 
ATOM   1281 C CB  . LEU B 1 60 ? -8.938  52.306 -47.018 1.00 18.61 ? 60  LEU B CB  1 
ATOM   1282 C CG  . LEU B 1 60 ? -10.152 52.619 -47.834 1.00 22.89 ? 60  LEU B CG  1 
ATOM   1283 C CD1 . LEU B 1 60 ? -9.870  53.724 -48.819 1.00 21.06 ? 60  LEU B CD1 1 
ATOM   1284 C CD2 . LEU B 1 60 ? -10.569 51.364 -48.532 1.00 26.79 ? 60  LEU B CD2 1 
ATOM   1285 N N   . TYR B 1 61 ? -6.260  53.055 -45.707 1.00 11.96 ? 61  TYR B N   1 
ATOM   1286 C CA  . TYR B 1 61 ? -5.692  53.152 -44.381 1.00 12.62 ? 61  TYR B CA  1 
ATOM   1287 C C   . TYR B 1 61 ? -6.741  53.865 -43.568 1.00 13.69 ? 61  TYR B C   1 
ATOM   1288 O O   . TYR B 1 61 ? -7.111  54.998 -43.889 1.00 15.23 ? 61  TYR B O   1 
ATOM   1289 C CB  . TYR B 1 61 ? -4.461  53.993 -44.361 1.00 13.62 ? 61  TYR B CB  1 
ATOM   1290 C CG  . TYR B 1 61 ? -3.262  53.192 -44.785 1.00 17.69 ? 61  TYR B CG  1 
ATOM   1291 C CD1 . TYR B 1 61 ? -2.531  52.463 -43.868 1.00 20.60 ? 61  TYR B CD1 1 
ATOM   1292 C CD2 . TYR B 1 61 ? -2.921  53.200 -46.119 1.00 16.59 ? 61  TYR B CD2 1 
ATOM   1293 C CE1 . TYR B 1 61 ? -1.430  51.741 -44.311 1.00 24.75 ? 61  TYR B CE1 1 
ATOM   1294 C CE2 . TYR B 1 61 ? -1.849  52.477 -46.560 1.00 21.36 ? 61  TYR B CE2 1 
ATOM   1295 C CZ  . TYR B 1 61 ? -1.109  51.755 -45.653 1.00 24.43 ? 61  TYR B CZ  1 
ATOM   1296 O OH  . TYR B 1 61 ? -0.033  51.024 -46.132 1.00 30.73 ? 61  TYR B OH  1 
ATOM   1297 N N   . VAL B 1 62 ? -7.265  53.217 -42.543 1.00 13.45 ? 62  VAL B N   1 
ATOM   1298 C CA  . VAL B 1 62 ? -8.368  53.776 -41.765 1.00 16.32 ? 62  VAL B CA  1 
ATOM   1299 C C   . VAL B 1 62 ? -7.997  53.863 -40.303 1.00 15.56 ? 62  VAL B C   1 
ATOM   1300 O O   . VAL B 1 62 ? -7.550  52.882 -39.726 1.00 15.76 ? 62  VAL B O   1 
ATOM   1301 C CB  . VAL B 1 62 ? -9.665  52.906 -41.840 1.00 17.53 ? 62  VAL B CB  1 
ATOM   1302 C CG1 . VAL B 1 62 ? -10.842 53.732 -41.293 1.00 19.18 ? 62  VAL B CG1 1 
ATOM   1303 C CG2 . VAL B 1 62 ? -9.893  52.406 -43.227 1.00 19.51 ? 62  VAL B CG2 1 
ATOM   1304 N N   . TYR B 1 63 ? -8.182  55.015 -39.688 1.00 16.74 ? 63  TYR B N   1 
ATOM   1305 C CA  . TYR B 1 63 ? -8.008  55.201 -38.268 1.00 17.49 ? 63  TYR B CA  1 
ATOM   1306 C C   . TYR B 1 63 ? -9.380  54.994 -37.634 1.00 19.06 ? 63  TYR B C   1 
ATOM   1307 O O   . TYR B 1 63 ? -10.362 55.667 -38.014 1.00 17.48 ? 63  TYR B O   1 
ATOM   1308 C CB  . TYR B 1 63 ? -7.572  56.609 -37.977 1.00 20.33 ? 63  TYR B CB  1 
ATOM   1309 C CG  . TYR B 1 63 ? -6.078  56.820 -37.867 1.00 21.36 ? 63  TYR B CG  1 
ATOM   1310 C CD1 . TYR B 1 63 ? -5.365  56.190 -36.847 1.00 21.36 ? 63  TYR B CD1 1 
ATOM   1311 C CD2 . TYR B 1 63 ? -5.451  57.641 -38.791 1.00 23.14 ? 63  TYR B CD2 1 
ATOM   1312 C CE1 . TYR B 1 63 ? -4.004  56.382 -36.759 1.00 23.16 ? 63  TYR B CE1 1 
ATOM   1313 C CE2 . TYR B 1 63 ? -4.083  57.833 -38.706 1.00 23.05 ? 63  TYR B CE2 1 
ATOM   1314 C CZ  . TYR B 1 63 ? -3.389  57.200 -37.693 1.00 24.26 ? 63  TYR B CZ  1 
ATOM   1315 O OH  . TYR B 1 63 ? -2.027  57.350 -37.601 1.00 27.02 ? 63  TYR B OH  1 
ATOM   1316 N N   . ALA B 1 64 ? -9.442  54.066 -36.698 1.00 19.27 ? 64  ALA B N   1 
ATOM   1317 C CA  . ALA B 1 64 ? -10.665 53.778 -35.971 1.00 21.34 ? 64  ALA B CA  1 
ATOM   1318 C C   . ALA B 1 64 ? -10.255 53.519 -34.543 1.00 21.76 ? 64  ALA B C   1 
ATOM   1319 O O   . ALA B 1 64 ? -9.395  52.666 -34.330 1.00 23.50 ? 64  ALA B O   1 
ATOM   1320 C CB  . ALA B 1 64 ? -11.359 52.500 -36.467 1.00 19.89 ? 64  ALA B CB  1 
ATOM   1321 N N   . SER B 1 65 ? -10.889 54.176 -33.561 1.00 23.81 ? 65  SER B N   1 
ATOM   1322 C CA  . SER B 1 65 ? -10.584 54.060 -32.141 1.00 25.86 ? 65  SER B CA  1 
ATOM   1323 C C   . SER B 1 65 ? -9.116  54.311 -31.932 1.00 24.91 ? 65  SER B C   1 
ATOM   1324 O O   . SER B 1 65 ? -8.464  53.560 -31.230 1.00 26.45 ? 65  SER B O   1 
ATOM   1325 C CB  . SER B 1 65 ? -10.983 52.670 -31.622 1.00 27.19 ? 65  SER B CB  1 
ATOM   1326 O OG  . SER B 1 65 ? -12.314 52.542 -32.055 1.00 32.27 ? 65  SER B OG  1 
ATOM   1327 N N   . ASP B 1 66 ? -8.618  55.344 -32.610 1.00 26.33 ? 66  ASP B N   1 
ATOM   1328 C CA  . ASP B 1 66 ? -7.224  55.766 -32.620 1.00 27.63 ? 66  ASP B CA  1 
ATOM   1329 C C   . ASP B 1 66 ? -6.217  54.719 -33.044 1.00 26.77 ? 66  ASP B C   1 
ATOM   1330 O O   . ASP B 1 66 ? -5.018  54.857 -32.770 1.00 29.45 ? 66  ASP B O   1 
ATOM   1331 C CB  . ASP B 1 66 ? -6.802  56.297 -31.227 1.00 29.95 ? 66  ASP B CB  1 
ATOM   1332 C CG  . ASP B 1 66 ? -7.759  57.340 -30.674 1.00 33.29 ? 66  ASP B CG  1 
ATOM   1333 O OD1 . ASP B 1 66 ? -8.081  58.305 -31.369 1.00 35.23 ? 66  ASP B OD1 1 
ATOM   1334 O OD2 . ASP B 1 66 ? -8.188  57.157 -29.539 1.00 38.76 ? 66  ASP B OD2 1 
ATOM   1335 N N   . LYS B 1 67 ? -6.628  53.652 -33.713 1.00 23.89 ? 67  LYS B N   1 
ATOM   1336 C CA  . LYS B 1 67 ? -5.647  52.724 -34.208 1.00 24.47 ? 67  LYS B CA  1 
ATOM   1337 C C   . LYS B 1 67 ? -5.759  52.706 -35.732 1.00 22.31 ? 67  LYS B C   1 
ATOM   1338 O O   . LYS B 1 67 ? -6.787  53.081 -36.298 1.00 20.96 ? 67  LYS B O   1 
ATOM   1339 C CB  . LYS B 1 67 ? -5.900  51.353 -33.590 1.00 28.51 ? 67  LYS B CB  1 
ATOM   1340 C CG  . LYS B 1 67 ? -5.568  51.400 -32.101 1.00 33.13 ? 67  LYS B CG  1 
ATOM   1341 C CD  . LYS B 1 67 ? -5.605  50.024 -31.491 1.00 36.86 ? 67  LYS B CD  1 
ATOM   1342 C CE  . LYS B 1 67 ? -7.010  49.438 -31.462 1.00 43.30 ? 67  LYS B CE  1 
ATOM   1343 N NZ  . LYS B 1 67 ? -7.885  50.153 -30.538 1.00 47.78 ? 67  LYS B NZ  1 
ATOM   1344 N N   . LEU B 1 68 ? -4.684  52.368 -36.441 1.00 19.49 ? 68  LEU B N   1 
ATOM   1345 C CA  . LEU B 1 68 ? -4.699  52.423 -37.890 1.00 16.87 ? 68  LEU B CA  1 
ATOM   1346 C C   . LEU B 1 68 ? -4.779  51.030 -38.462 1.00 15.88 ? 68  LEU B C   1 
ATOM   1347 O O   . LEU B 1 68 ? -4.036  50.133 -38.081 1.00 14.36 ? 68  LEU B O   1 
ATOM   1348 C CB  . LEU B 1 68 ? -3.437  53.125 -38.399 1.00 14.69 ? 68  LEU B CB  1 
ATOM   1349 C CG  . LEU B 1 68 ? -3.357  53.383 -39.885 1.00 15.19 ? 68  LEU B CG  1 
ATOM   1350 C CD1 . LEU B 1 68 ? -4.353  54.449 -40.252 1.00 12.60 ? 68  LEU B CD1 1 
ATOM   1351 C CD2 . LEU B 1 68 ? -1.955  53.817 -40.270 1.00 16.21 ? 68  LEU B CD2 1 
ATOM   1352 N N   . PHE B 1 69 ? -5.676  50.863 -39.411 1.00 15.98 ? 69  PHE B N   1 
ATOM   1353 C CA  . PHE B 1 69 ? -5.955  49.576 -39.994 1.00 16.81 ? 69  PHE B CA  1 
ATOM   1354 C C   . PHE B 1 69 ? -5.827  49.656 -41.496 1.00 15.42 ? 69  PHE B C   1 
ATOM   1355 O O   . PHE B 1 69 ? -5.975  50.741 -42.065 1.00 16.55 ? 69  PHE B O   1 
ATOM   1356 C CB  . PHE B 1 69 ? -7.377  49.149 -39.648 1.00 15.46 ? 69  PHE B CB  1 
ATOM   1357 C CG  . PHE B 1 69 ? -7.546  48.832 -38.176 1.00 17.01 ? 69  PHE B CG  1 
ATOM   1358 C CD1 . PHE B 1 69 ? -7.184  47.558 -37.712 1.00 16.62 ? 69  PHE B CD1 1 
ATOM   1359 C CD2 . PHE B 1 69 ? -8.003  49.817 -37.321 1.00 14.62 ? 69  PHE B CD2 1 
ATOM   1360 C CE1 . PHE B 1 69 ? -7.278  47.286 -36.372 1.00 19.79 ? 69  PHE B CE1 1 
ATOM   1361 C CE2 . PHE B 1 69 ? -8.096  49.524 -35.974 1.00 18.99 ? 69  PHE B CE2 1 
ATOM   1362 C CZ  . PHE B 1 69 ? -7.736  48.275 -35.502 1.00 17.54 ? 69  PHE B CZ  1 
ATOM   1363 N N   . ARG B 1 70 ? -5.549  48.524 -42.139 1.00 15.78 ? 70  ARG B N   1 
ATOM   1364 C CA  . ARG B 1 70 ? -5.641  48.407 -43.590 1.00 16.43 ? 70  ARG B CA  1 
ATOM   1365 C C   . ARG B 1 70 ? -6.977  47.694 -43.952 1.00 15.18 ? 70  ARG B C   1 
ATOM   1366 O O   . ARG B 1 70 ? -7.290  46.609 -43.430 1.00 14.58 ? 70  ARG B O   1 
ATOM   1367 C CB  . ARG B 1 70 ? -4.421  47.616 -44.085 1.00 14.58 ? 70  ARG B CB  1 
ATOM   1368 C CG  . ARG B 1 70 ? -3.263  48.568 -44.446 1.00 20.29 ? 70  ARG B CG  1 
ATOM   1369 C CD  . ARG B 1 70 ? -3.447  49.158 -45.857 1.00 21.63 ? 70  ARG B CD  1 
ATOM   1370 N NE  . ARG B 1 70 ? -3.315  48.115 -46.877 1.00 21.46 ? 70  ARG B NE  1 
ATOM   1371 C CZ  . ARG B 1 70 ? -4.340  47.751 -47.680 1.00 24.79 ? 70  ARG B CZ  1 
ATOM   1372 N NH1 . ARG B 1 70 ? -5.543  48.332 -47.560 1.00 22.40 ? 70  ARG B NH1 1 
ATOM   1373 N NH2 . ARG B 1 70 ? -4.165  46.791 -48.599 1.00 19.87 ? 70  ARG B NH2 1 
ATOM   1374 N N   . ALA B 1 71 ? -7.807  48.293 -44.817 1.00 13.05 ? 71  ALA B N   1 
ATOM   1375 C CA  . ALA B 1 71 ? -9.078  47.691 -45.223 1.00 13.30 ? 71  ALA B CA  1 
ATOM   1376 C C   . ALA B 1 71 ? -9.130  47.557 -46.737 1.00 11.35 ? 71  ALA B C   1 
ATOM   1377 O O   . ALA B 1 71 ? -8.692  48.499 -47.407 1.00 13.03 ? 71  ALA B O   1 
ATOM   1378 C CB  . ALA B 1 71 ? -10.265 48.565 -44.812 1.00 11.83 ? 71  ALA B CB  1 
ATOM   1379 N N   . ASP B 1 72 ? -9.506  46.430 -47.348 1.00 11.38 ? 72  ASP B N   1 
ATOM   1380 C CA  . ASP B 1 72 ? -9.685  46.339 -48.800 1.00 12.29 ? 72  ASP B CA  1 
ATOM   1381 C C   . ASP B 1 72 ? -11.162 46.146 -49.042 1.00 14.00 ? 72  ASP B C   1 
ATOM   1382 O O   . ASP B 1 72 ? -11.753 45.284 -48.378 1.00 12.83 ? 72  ASP B O   1 
ATOM   1383 C CB  . ASP B 1 72 ? -9.019  45.165 -49.408 1.00 14.56 ? 72  ASP B CB  1 
ATOM   1384 C CG  . ASP B 1 72 ? -7.530  45.214 -49.171 1.00 19.52 ? 72  ASP B CG  1 
ATOM   1385 O OD1 . ASP B 1 72 ? -6.966  46.300 -49.114 1.00 21.41 ? 72  ASP B OD1 1 
ATOM   1386 O OD2 . ASP B 1 72 ? -6.930  44.165 -49.016 1.00 22.66 ? 72  ASP B OD2 1 
ATOM   1387 N N   . ILE B 1 73 ? -11.758 46.919 -49.936 1.00 12.99 ? 73  ILE B N   1 
ATOM   1388 C CA  . ILE B 1 73 ? -13.201 46.912 -50.129 1.00 13.91 ? 73  ILE B CA  1 
ATOM   1389 C C   . ILE B 1 73 ? -13.453 46.663 -51.611 1.00 13.53 ? 73  ILE B C   1 
ATOM   1390 O O   . ILE B 1 73 ? -12.673 47.182 -52.418 1.00 13.93 ? 73  ILE B O   1 
ATOM   1391 C CB  . ILE B 1 73 ? -13.754 48.302 -49.687 1.00 14.45 ? 73  ILE B CB  1 
ATOM   1392 C CG1 . ILE B 1 73 ? -13.578 48.480 -48.201 1.00 15.59 ? 73  ILE B CG1 1 
ATOM   1393 C CG2 . ILE B 1 73 ? -15.254 48.442 -50.009 1.00 17.02 ? 73  ILE B CG2 1 
ATOM   1394 C CD1 . ILE B 1 73 ? -13.769 49.968 -47.875 1.00 17.55 ? 73  ILE B CD1 1 
ATOM   1395 N N   . SER B 1 74 ? -14.446 45.868 -52.029 1.00 12.54 ? 74  SER B N   1 
ATOM   1396 C CA  . SER B 1 74 ? -14.781 45.778 -53.434 1.00 13.65 ? 74  SER B CA  1 
ATOM   1397 C C   . SER B 1 74 ? -16.095 46.532 -53.672 1.00 14.22 ? 74  SER B C   1 
ATOM   1398 O O   . SER B 1 74 ? -16.910 46.690 -52.774 1.00 13.97 ? 74  SER B O   1 
ATOM   1399 C CB  . SER B 1 74 ? -14.946 44.332 -53.880 1.00 16.04 ? 74  SER B CB  1 
ATOM   1400 O OG  . SER B 1 74 ? -16.037 43.702 -53.239 1.00 22.34 ? 74  SER B OG  1 
ATOM   1401 N N   . GLU B 1 75 ? -16.368 47.045 -54.857 1.00 15.41 ? 75  GLU B N   1 
ATOM   1402 C CA  . GLU B 1 75 ? -17.600 47.750 -55.137 1.00 15.70 ? 75  GLU B CA  1 
ATOM   1403 C C   . GLU B 1 75 ? -18.051 47.252 -56.508 1.00 15.45 ? 75  GLU B C   1 
ATOM   1404 O O   . GLU B 1 75 ? -17.278 47.201 -57.461 1.00 13.91 ? 75  GLU B O   1 
ATOM   1405 C CB  . GLU B 1 75 ? -17.354 49.247 -55.173 1.00 17.98 ? 75  GLU B CB  1 
ATOM   1406 C CG  . GLU B 1 75 ? -18.669 49.934 -55.452 1.00 25.86 ? 75  GLU B CG  1 
ATOM   1407 C CD  . GLU B 1 75 ? -18.682 51.444 -55.372 1.00 31.93 ? 75  GLU B CD  1 
ATOM   1408 O OE1 . GLU B 1 75 ? -17.628 52.053 -55.276 1.00 32.40 ? 75  GLU B OE1 1 
ATOM   1409 O OE2 . GLU B 1 75 ? -19.780 52.004 -55.387 1.00 39.01 ? 75  GLU B OE2 1 
ATOM   1410 N N   . ASP B 1 76 ? -19.340 46.926 -56.617 1.00 13.56 ? 76  ASP B N   1 
ATOM   1411 C CA  . ASP B 1 76 ? -19.862 46.486 -57.877 1.00 13.82 ? 76  ASP B CA  1 
ATOM   1412 C C   . ASP B 1 76 ? -20.288 47.736 -58.629 1.00 14.19 ? 76  ASP B C   1 
ATOM   1413 O O   . ASP B 1 76 ? -20.909 48.652 -58.077 1.00 16.50 ? 76  ASP B O   1 
ATOM   1414 C CB  . ASP B 1 76 ? -21.065 45.526 -57.642 1.00 16.31 ? 76  ASP B CB  1 
ATOM   1415 C CG  . ASP B 1 76 ? -21.654 45.001 -58.952 1.00 16.44 ? 76  ASP B CG  1 
ATOM   1416 O OD1 . ASP B 1 76 ? -21.036 44.202 -59.653 1.00 21.13 ? 76  ASP B OD1 1 
ATOM   1417 O OD2 . ASP B 1 76 ? -22.722 45.437 -59.325 1.00 20.12 ? 76  ASP B OD2 1 
ATOM   1418 N N   . TYR B 1 77 ? -19.962 47.788 -59.904 1.00 12.81 ? 77  TYR B N   1 
ATOM   1419 C CA  . TYR B 1 77 ? -20.240 48.961 -60.681 1.00 13.99 ? 77  TYR B CA  1 
ATOM   1420 C C   . TYR B 1 77 ? -21.745 49.151 -60.839 1.00 14.14 ? 77  TYR B C   1 
ATOM   1421 O O   . TYR B 1 77 ? -22.240 50.260 -60.677 1.00 14.65 ? 77  TYR B O   1 
ATOM   1422 C CB  . TYR B 1 77 ? -19.557 48.810 -62.028 1.00 14.63 ? 77  TYR B CB  1 
ATOM   1423 C CG  . TYR B 1 77 ? -19.799 49.990 -62.933 1.00 17.90 ? 77  TYR B CG  1 
ATOM   1424 C CD1 . TYR B 1 77 ? -19.108 51.158 -62.766 1.00 21.01 ? 77  TYR B CD1 1 
ATOM   1425 C CD2 . TYR B 1 77 ? -20.730 49.853 -63.931 1.00 23.10 ? 77  TYR B CD2 1 
ATOM   1426 C CE1 . TYR B 1 77 ? -19.364 52.222 -63.600 1.00 25.97 ? 77  TYR B CE1 1 
ATOM   1427 C CE2 . TYR B 1 77 ? -21.002 50.900 -64.774 1.00 26.20 ? 77  TYR B CE2 1 
ATOM   1428 C CZ  . TYR B 1 77 ? -20.312 52.073 -64.598 1.00 27.44 ? 77  TYR B CZ  1 
ATOM   1429 O OH  . TYR B 1 77 ? -20.597 53.121 -65.444 1.00 33.69 ? 77  TYR B OH  1 
ATOM   1430 N N   . LYS B 1 78 ? -22.488 48.087 -61.150 1.00 15.71 ? 78  LYS B N   1 
ATOM   1431 C CA  . LYS B 1 78 ? -23.918 48.268 -61.444 1.00 14.64 ? 78  LYS B CA  1 
ATOM   1432 C C   . LYS B 1 78 ? -24.807 48.476 -60.240 1.00 14.18 ? 78  LYS B C   1 
ATOM   1433 O O   . LYS B 1 78 ? -25.739 49.274 -60.267 1.00 15.77 ? 78  LYS B O   1 
ATOM   1434 C CB  . LYS B 1 78 ? -24.455 47.074 -62.191 1.00 18.20 ? 78  LYS B CB  1 
ATOM   1435 C CG  . LYS B 1 78 ? -23.936 46.862 -63.592 1.00 21.62 ? 78  LYS B CG  1 
ATOM   1436 C CD  . LYS B 1 78 ? -24.891 45.783 -64.149 1.00 28.33 ? 78  LYS B CD  1 
ATOM   1437 C CE  . LYS B 1 78 ? -24.168 44.614 -64.761 1.00 31.25 ? 78  LYS B CE  1 
ATOM   1438 N NZ  . LYS B 1 78 ? -23.249 43.995 -63.813 1.00 34.97 ? 78  LYS B NZ  1 
ATOM   1439 N N   . THR B 1 79 ? -24.609 47.762 -59.159 1.00 11.66 ? 79  THR B N   1 
ATOM   1440 C CA  . THR B 1 79 ? -25.432 47.864 -57.983 1.00 14.29 ? 79  THR B CA  1 
ATOM   1441 C C   . THR B 1 79 ? -24.908 48.906 -57.006 1.00 15.21 ? 79  THR B C   1 
ATOM   1442 O O   . THR B 1 79 ? -25.667 49.316 -56.135 1.00 14.73 ? 79  THR B O   1 
ATOM   1443 C CB  . THR B 1 79 ? -25.522 46.495 -57.241 1.00 14.18 ? 79  THR B CB  1 
ATOM   1444 O OG1 . THR B 1 79 ? -24.172 46.123 -56.917 1.00 17.59 ? 79  THR B OG1 1 
ATOM   1445 C CG2 . THR B 1 79 ? -26.102 45.379 -58.060 1.00 14.55 ? 79  THR B CG2 1 
ATOM   1446 N N   . ARG B 1 80 ? -23.621 49.292 -57.129 1.00 14.69 ? 80  ARG B N   1 
ATOM   1447 C CA  . ARG B 1 80 ? -22.899 50.113 -56.163 1.00 16.83 ? 80  ARG B CA  1 
ATOM   1448 C C   . ARG B 1 80 ? -22.829 49.521 -54.732 1.00 17.43 ? 80  ARG B C   1 
ATOM   1449 O O   . ARG B 1 80 ? -22.461 50.148 -53.735 1.00 19.22 ? 80  ARG B O   1 
ATOM   1450 C CB  . ARG B 1 80 ? -23.513 51.514 -56.171 1.00 19.30 ? 80  ARG B CB  1 
ATOM   1451 C CG  . ARG B 1 80 ? -23.477 52.035 -57.610 1.00 20.33 ? 80  ARG B CG  1 
ATOM   1452 C CD  . ARG B 1 80 ? -23.668 53.538 -57.778 1.00 24.43 ? 80  ARG B CD  1 
ATOM   1453 N NE  . ARG B 1 80 ? -24.940 54.017 -57.267 1.00 24.70 ? 80  ARG B NE  1 
ATOM   1454 C CZ  . ARG B 1 80 ? -25.024 54.661 -56.100 1.00 23.74 ? 80  ARG B CZ  1 
ATOM   1455 N NH1 . ARG B 1 80 ? -23.940 54.856 -55.331 1.00 26.19 ? 80  ARG B NH1 1 
ATOM   1456 N NH2 . ARG B 1 80 ? -26.221 55.086 -55.708 1.00 22.51 ? 80  ARG B NH2 1 
ATOM   1457 N N   . GLY B 1 81 ? -23.068 48.212 -54.589 1.00 15.89 ? 81  GLY B N   1 
ATOM   1458 C CA  . GLY B 1 81 ? -22.957 47.509 -53.324 1.00 13.39 ? 81  GLY B CA  1 
ATOM   1459 C C   . GLY B 1 81 ? -21.494 47.241 -53.090 1.00 12.02 ? 81  GLY B C   1 
ATOM   1460 O O   . GLY B 1 81 ? -20.723 47.140 -54.036 1.00 14.68 ? 81  GLY B O   1 
ATOM   1461 N N   . ARG B 1 82 ? -21.128 47.102 -51.843 1.00 14.09 ? 82  ARG B N   1 
ATOM   1462 C CA  . ARG B 1 82 ? -19.756 47.041 -51.425 1.00 15.69 ? 82  ARG B CA  1 
ATOM   1463 C C   . ARG B 1 82 ? -19.603 45.859 -50.524 1.00 16.18 ? 82  ARG B C   1 
ATOM   1464 O O   . ARG B 1 82 ? -20.567 45.504 -49.872 1.00 17.26 ? 82  ARG B O   1 
ATOM   1465 C CB  . ARG B 1 82 ? -19.406 48.304 -50.674 1.00 16.88 ? 82  ARG B CB  1 
ATOM   1466 C CG  . ARG B 1 82 ? -19.287 49.447 -51.645 1.00 18.75 ? 82  ARG B CG  1 
ATOM   1467 C CD  . ARG B 1 82 ? -19.316 50.771 -50.934 1.00 22.65 ? 82  ARG B CD  1 
ATOM   1468 N NE  . ARG B 1 82 ? -18.968 51.755 -51.928 1.00 24.67 ? 82  ARG B NE  1 
ATOM   1469 C CZ  . ARG B 1 82 ? -18.823 53.041 -51.645 1.00 26.80 ? 82  ARG B CZ  1 
ATOM   1470 N NH1 . ARG B 1 82 ? -19.019 53.495 -50.392 1.00 28.50 ? 82  ARG B NH1 1 
ATOM   1471 N NH2 . ARG B 1 82 ? -18.339 53.840 -52.613 1.00 26.18 ? 82  ARG B NH2 1 
ATOM   1472 N N   . LYS B 1 83 ? -18.401 45.306 -50.449 1.00 17.85 ? 83  LYS B N   1 
ATOM   1473 C CA  . LYS B 1 83 ? -18.030 44.134 -49.682 1.00 19.34 ? 83  LYS B CA  1 
ATOM   1474 C C   . LYS B 1 83 ? -16.707 44.455 -48.991 1.00 18.20 ? 83  LYS B C   1 
ATOM   1475 O O   . LYS B 1 83 ? -15.791 44.967 -49.654 1.00 15.82 ? 83  LYS B O   1 
ATOM   1476 C CB  . LYS B 1 83 ? -17.719 42.932 -50.555 1.00 23.08 ? 83  LYS B CB  1 
ATOM   1477 C CG  . LYS B 1 83 ? -18.837 42.066 -50.948 1.00 33.76 ? 83  LYS B CG  1 
ATOM   1478 C CD  . LYS B 1 83 ? -19.055 41.167 -49.739 1.00 43.30 ? 83  LYS B CD  1 
ATOM   1479 C CE  . LYS B 1 83 ? -20.253 40.227 -50.007 1.00 49.81 ? 83  LYS B CE  1 
ATOM   1480 N NZ  . LYS B 1 83 ? -20.004 39.351 -51.149 1.00 53.58 ? 83  LYS B NZ  1 
ATOM   1481 N N   . LEU B 1 84 ? -16.596 44.172 -47.692 1.00 17.78 ? 84  LEU B N   1 
ATOM   1482 C CA  . LEU B 1 84 ? -15.291 44.283 -47.039 1.00 19.63 ? 84  LEU B CA  1 
ATOM   1483 C C   . LEU B 1 84 ? -14.516 43.001 -47.351 1.00 20.08 ? 84  LEU B C   1 
ATOM   1484 O O   . LEU B 1 84 ? -14.970 41.897 -47.042 1.00 22.39 ? 84  LEU B O   1 
ATOM   1485 C CB  . LEU B 1 84 ? -15.482 44.415 -45.542 1.00 18.58 ? 84  LEU B CB  1 
ATOM   1486 C CG  . LEU B 1 84 ? -14.262 44.508 -44.662 1.00 18.97 ? 84  LEU B CG  1 
ATOM   1487 C CD1 . LEU B 1 84 ? -13.563 45.857 -44.812 1.00 16.51 ? 84  LEU B CD1 1 
ATOM   1488 C CD2 . LEU B 1 84 ? -14.739 44.275 -43.236 1.00 20.87 ? 84  LEU B CD2 1 
ATOM   1489 N N   . LEU B 1 85 ? -13.379 43.097 -48.042 1.00 19.89 ? 85  LEU B N   1 
ATOM   1490 C CA  . LEU B 1 85 ? -12.565 41.926 -48.354 1.00 19.01 ? 85  LEU B CA  1 
ATOM   1491 C C   . LEU B 1 85 ? -11.598 41.620 -47.218 1.00 20.69 ? 85  LEU B C   1 
ATOM   1492 O O   . LEU B 1 85 ? -11.383 40.450 -46.921 1.00 21.41 ? 85  LEU B O   1 
ATOM   1493 C CB  . LEU B 1 85 ? -11.740 42.148 -49.590 1.00 15.50 ? 85  LEU B CB  1 
ATOM   1494 C CG  . LEU B 1 85 ? -12.526 42.674 -50.761 1.00 18.67 ? 85  LEU B CG  1 
ATOM   1495 C CD1 . LEU B 1 85 ? -11.599 42.944 -51.927 1.00 18.30 ? 85  LEU B CD1 1 
ATOM   1496 C CD2 . LEU B 1 85 ? -13.626 41.680 -51.087 1.00 18.59 ? 85  LEU B CD2 1 
ATOM   1497 N N   . ARG B 1 86 ? -10.973 42.602 -46.565 1.00 19.85 ? 86  ARG B N   1 
ATOM   1498 C CA  . ARG B 1 86 ? -9.979  42.326 -45.533 1.00 20.53 ? 86  ARG B CA  1 
ATOM   1499 C C   . ARG B 1 86 ? -9.936  43.541 -44.669 1.00 18.51 ? 86  ARG B C   1 
ATOM   1500 O O   . ARG B 1 86 ? -10.134 44.640 -45.195 1.00 16.24 ? 86  ARG B O   1 
ATOM   1501 C CB  . ARG B 1 86 ? -8.545  42.186 -46.059 1.00 25.88 ? 86  ARG B CB  1 
ATOM   1502 C CG  . ARG B 1 86 ? -8.315  41.344 -47.311 1.00 33.89 ? 86  ARG B CG  1 
ATOM   1503 C CD  . ARG B 1 86 ? -6.860  41.340 -47.742 1.00 37.83 ? 86  ARG B CD  1 
ATOM   1504 N NE  . ARG B 1 86 ? -6.621  40.545 -48.936 1.00 41.47 ? 86  ARG B NE  1 
ATOM   1505 C CZ  . ARG B 1 86 ? -7.083  40.857 -50.151 1.00 45.10 ? 86  ARG B CZ  1 
ATOM   1506 N NH1 . ARG B 1 86 ? -7.854  41.925 -50.375 1.00 45.98 ? 86  ARG B NH1 1 
ATOM   1507 N NH2 . ARG B 1 86 ? -6.774  40.061 -51.185 1.00 48.36 ? 86  ARG B NH2 1 
ATOM   1508 N N   . PHE B 1 87 ? -9.648  43.378 -43.381 1.00 18.10 ? 87  PHE B N   1 
ATOM   1509 C CA  . PHE B 1 87 ? -9.501  44.478 -42.436 1.00 19.51 ? 87  PHE B CA  1 
ATOM   1510 C C   . PHE B 1 87 ? -8.348  43.970 -41.566 1.00 23.03 ? 87  PHE B C   1 
ATOM   1511 O O   . PHE B 1 87 ? -8.454  42.877 -40.977 1.00 24.73 ? 87  PHE B O   1 
ATOM   1512 C CB  . PHE B 1 87 ? -10.775 44.609 -41.644 1.00 16.88 ? 87  PHE B CB  1 
ATOM   1513 C CG  . PHE B 1 87 ? -10.897 45.906 -40.861 1.00 17.41 ? 87  PHE B CG  1 
ATOM   1514 C CD1 . PHE B 1 87 ? -10.331 45.992 -39.615 1.00 16.31 ? 87  PHE B CD1 1 
ATOM   1515 C CD2 . PHE B 1 87 ? -11.616 46.961 -41.389 1.00 15.79 ? 87  PHE B CD2 1 
ATOM   1516 C CE1 . PHE B 1 87 ? -10.489 47.162 -38.923 1.00 19.42 ? 87  PHE B CE1 1 
ATOM   1517 C CE2 . PHE B 1 87 ? -11.756 48.124 -40.683 1.00 17.35 ? 87  PHE B CE2 1 
ATOM   1518 C CZ  . PHE B 1 87 ? -11.207 48.222 -39.440 1.00 17.49 ? 87  PHE B CZ  1 
ATOM   1519 N N   . ASN B 1 88 ? -7.198  44.628 -41.486 1.00 21.46 ? 88  ASN B N   1 
ATOM   1520 C CA  . ASN B 1 88 ? -6.098  44.057 -40.723 1.00 22.67 ? 88  ASN B CA  1 
ATOM   1521 C C   . ASN B 1 88 ? -5.408  45.146 -39.997 1.00 21.11 ? 88  ASN B C   1 
ATOM   1522 O O   . ASN B 1 88 ? -5.449  46.290 -40.418 1.00 20.33 ? 88  ASN B O   1 
ATOM   1523 C CB  . ASN B 1 88 ? -5.017  43.407 -41.569 1.00 28.38 ? 88  ASN B CB  1 
ATOM   1524 C CG  . ASN B 1 88 ? -5.394  42.040 -42.098 1.00 35.38 ? 88  ASN B CG  1 
ATOM   1525 O OD1 . ASN B 1 88 ? -5.425  41.805 -43.301 1.00 36.59 ? 88  ASN B OD1 1 
ATOM   1526 N ND2 . ASN B 1 88 ? -5.751  41.070 -41.262 1.00 41.12 ? 88  ASN B ND2 1 
ATOM   1527 N N   . GLY B 1 89 ? -4.837  44.835 -38.857 1.00 22.38 ? 89  GLY B N   1 
ATOM   1528 C CA  . GLY B 1 89 ? -3.995  45.783 -38.159 1.00 22.13 ? 89  GLY B CA  1 
ATOM   1529 C C   . GLY B 1 89 ? -3.932  45.487 -36.666 1.00 23.30 ? 89  GLY B C   1 
ATOM   1530 O O   . GLY B 1 89 ? -4.313  44.376 -36.278 1.00 22.04 ? 89  GLY B O   1 
ATOM   1531 N N   . PRO B 1 90 ? -3.567  46.442 -35.799 1.00 24.30 ? 90  PRO B N   1 
ATOM   1532 C CA  . PRO B 1 90 ? -3.085  47.780 -36.157 1.00 24.04 ? 90  PRO B CA  1 
ATOM   1533 C C   . PRO B 1 90 ? -1.836  47.768 -37.005 1.00 24.51 ? 90  PRO B C   1 
ATOM   1534 O O   . PRO B 1 90 ? -1.060  46.824 -36.943 1.00 24.53 ? 90  PRO B O   1 
ATOM   1535 C CB  . PRO B 1 90 ? -2.883  48.464 -34.856 1.00 25.53 ? 90  PRO B CB  1 
ATOM   1536 C CG  . PRO B 1 90 ? -4.040  47.914 -34.071 1.00 28.77 ? 90  PRO B CG  1 
ATOM   1537 C CD  . PRO B 1 90 ? -3.978  46.431 -34.404 1.00 26.10 ? 90  PRO B CD  1 
ATOM   1538 N N   . VAL B 1 91 ? -1.670  48.770 -37.856 1.00 23.30 ? 91  VAL B N   1 
ATOM   1539 C CA  . VAL B 1 91 ? -0.598  48.806 -38.833 1.00 22.42 ? 91  VAL B CA  1 
ATOM   1540 C C   . VAL B 1 91 ? 0.223   50.070 -38.570 1.00 23.42 ? 91  VAL B C   1 
ATOM   1541 O O   . VAL B 1 91 ? -0.342  51.060 -38.062 1.00 21.84 ? 91  VAL B O   1 
ATOM   1542 C CB  . VAL B 1 91 ? -1.398  48.709 -40.180 1.00 25.07 ? 91  VAL B CB  1 
ATOM   1543 C CG1 . VAL B 1 91 ? -1.427  49.997 -40.982 1.00 22.82 ? 91  VAL B CG1 1 
ATOM   1544 C CG2 . VAL B 1 91 ? -0.846  47.499 -40.876 1.00 25.19 ? 91  VAL B CG2 1 
ATOM   1545 N N   . PRO B 1 92 ? 1.536   50.130 -38.876 1.00 23.13 ? 92  PRO B N   1 
ATOM   1546 C CA  . PRO B 1 92 ? 2.342   51.356 -38.803 1.00 22.37 ? 92  PRO B CA  1 
ATOM   1547 C C   . PRO B 1 92 ? 1.866   52.449 -39.755 1.00 21.33 ? 92  PRO B C   1 
ATOM   1548 O O   . PRO B 1 92 ? 1.357   52.108 -40.825 1.00 22.45 ? 92  PRO B O   1 
ATOM   1549 C CB  . PRO B 1 92 ? 3.733   50.909 -39.130 1.00 20.88 ? 92  PRO B CB  1 
ATOM   1550 C CG  . PRO B 1 92 ? 3.676   49.418 -39.067 1.00 24.72 ? 92  PRO B CG  1 
ATOM   1551 C CD  . PRO B 1 92 ? 2.288   49.086 -39.549 1.00 22.85 ? 92  PRO B CD  1 
ATOM   1552 N N   . PRO B 1 93 ? 1.987   53.750 -39.510 1.00 22.56 ? 93  PRO B N   1 
ATOM   1553 C CA  . PRO B 1 93 ? 1.583   54.784 -40.465 1.00 22.01 ? 93  PRO B CA  1 
ATOM   1554 C C   . PRO B 1 93 ? 2.336   54.595 -41.783 1.00 23.62 ? 93  PRO B C   1 
ATOM   1555 O O   . PRO B 1 93 ? 3.507   54.195 -41.693 1.00 22.71 ? 93  PRO B O   1 
ATOM   1556 C CB  . PRO B 1 93 ? 1.915   56.070 -39.775 1.00 22.93 ? 93  PRO B CB  1 
ATOM   1557 C CG  . PRO B 1 93 ? 1.894   55.746 -38.318 1.00 23.60 ? 93  PRO B CG  1 
ATOM   1558 C CD  . PRO B 1 93 ? 2.509   54.351 -38.293 1.00 23.15 ? 93  PRO B CD  1 
ATOM   1559 N N   . PRO B 1 94 ? 1.700   54.775 -42.968 1.00 23.00 ? 94  PRO B N   1 
ATOM   1560 C CA  . PRO B 1 94 ? 2.361   54.731 -44.278 1.00 22.78 ? 94  PRO B CA  1 
ATOM   1561 C C   . PRO B 1 94 ? 3.340   55.893 -44.566 1.00 23.02 ? 94  PRO B C   1 
ATOM   1562 O O   . PRO B 1 94 ? 3.166   57.020 -44.098 1.00 26.73 ? 94  PRO B O   1 
ATOM   1563 C CB  . PRO B 1 94 ? 1.199   54.659 -45.239 1.00 21.01 ? 94  PRO B CB  1 
ATOM   1564 C CG  . PRO B 1 94 ? 0.146   55.511 -44.563 1.00 20.65 ? 94  PRO B CG  1 
ATOM   1565 C CD  . PRO B 1 94 ? 0.279   55.098 -43.103 1.00 21.93 ? 94  PRO B CD  1 
ATOM   1566 O OXT . PRO B 1 94 ? 4.291   55.657 -45.293 1.00 24.66 ? 94  PRO B OXT 1 
HETATM 1567 O O   . HOH C 2 .  ? 8.927   36.782 -64.575 1.00 18.74 ? 301 HOH A O   1 
HETATM 1568 O O   . HOH C 2 .  ? 16.000  35.399 -46.919 1.00 20.19 ? 302 HOH A O   1 
HETATM 1569 O O   . HOH C 2 .  ? 10.328  26.471 -59.713 1.00 18.92 ? 303 HOH A O   1 
HETATM 1570 O O   . HOH C 2 .  ? 8.154   44.497 -64.509 1.00 23.93 ? 304 HOH A O   1 
HETATM 1571 O O   . HOH C 2 .  ? 6.031   60.724 -54.608 1.00 15.00 ? 306 HOH A O   1 
HETATM 1572 O O   . HOH C 2 .  ? 18.537  40.062 -57.065 1.00 22.19 ? 307 HOH A O   1 
HETATM 1573 O O   . HOH C 2 .  ? 5.304   46.720 -57.328 1.00 11.12 ? 309 HOH A O   1 
HETATM 1574 O O   . HOH C 2 .  ? 8.831   61.882 -58.499 1.00 28.32 ? 310 HOH A O   1 
HETATM 1575 O O   . HOH C 2 .  ? 2.797   50.494 -61.184 1.00 15.02 ? 311 HOH A O   1 
HETATM 1576 O O   . HOH C 2 .  ? 1.849   43.337 -63.615 1.00 27.28 ? 312 HOH A O   1 
HETATM 1577 O O   . HOH C 2 .  ? -0.186  62.037 -52.261 1.00 22.64 ? 318 HOH A O   1 
HETATM 1578 O O   . HOH C 2 .  ? 18.114  54.882 -47.299 1.00 24.02 ? 320 HOH A O   1 
HETATM 1579 O O   . HOH C 2 .  ? 18.477  38.931 -63.303 1.00 26.51 ? 323 HOH A O   1 
HETATM 1580 O O   . HOH C 2 .  ? 10.646  42.785 -42.815 1.00 28.86 ? 324 HOH A O   1 
HETATM 1581 O O   . HOH C 2 .  ? -0.029  58.398 -59.333 1.00 22.97 ? 325 HOH A O   1 
HETATM 1582 O O   . HOH C 2 .  ? 22.616  34.290 -50.333 1.00 30.31 ? 326 HOH A O   1 
HETATM 1583 O O   . HOH C 2 .  ? 16.634  58.722 -45.292 1.00 60.79 ? 327 HOH A O   1 
HETATM 1584 O O   . HOH C 2 .  ? 19.995  43.764 -45.388 1.00 37.55 ? 328 HOH A O   1 
HETATM 1585 O O   . HOH C 2 .  ? 15.900  45.403 -65.850 1.00 22.06 ? 336 HOH A O   1 
HETATM 1586 O O   . HOH C 2 .  ? 10.429  44.016 -68.465 1.00 68.50 ? 343 HOH A O   1 
HETATM 1587 O O   . HOH C 2 .  ? 18.342  44.402 -64.296 1.00 24.43 ? 344 HOH A O   1 
HETATM 1588 O O   . HOH C 2 .  ? 21.219  37.811 -53.405 1.00 35.78 ? 345 HOH A O   1 
HETATM 1589 O O   . HOH C 2 .  ? 19.187  47.346 -46.370 1.00 17.91 ? 346 HOH A O   1 
HETATM 1590 O O   . HOH C 2 .  ? 2.742   48.601 -53.999 1.00 28.93 ? 348 HOH A O   1 
HETATM 1591 O O   . HOH C 2 .  ? 13.575  57.777 -47.214 1.00 25.84 ? 349 HOH A O   1 
HETATM 1592 O O   . HOH C 2 .  ? 13.619  58.657 -56.615 1.00 39.40 ? 350 HOH A O   1 
HETATM 1593 O O   . HOH C 2 .  ? 7.569   59.532 -61.200 1.00 26.84 ? 351 HOH A O   1 
HETATM 1594 O O   . HOH C 2 .  ? 8.338   71.508 -53.254 1.00 30.16 ? 354 HOH A O   1 
HETATM 1595 O O   . HOH C 2 .  ? 9.131   61.825 -61.330 1.00 23.12 ? 358 HOH A O   1 
HETATM 1596 O O   . HOH C 2 .  ? 18.430  63.471 -47.542 1.00 29.27 ? 359 HOH A O   1 
HETATM 1597 O O   . HOH C 2 .  ? 10.475  52.119 -63.431 1.00 28.92 ? 362 HOH A O   1 
HETATM 1598 O O   . HOH C 2 .  ? 5.391   61.204 -44.234 1.00 31.82 ? 364 HOH A O   1 
HETATM 1599 O O   . HOH C 2 .  ? 23.044  46.061 -46.367 1.00 26.46 ? 367 HOH A O   1 
HETATM 1600 O O   . HOH C 2 .  ? 22.343  44.628 -52.092 1.00 31.15 ? 377 HOH A O   1 
HETATM 1601 O O   . HOH C 2 .  ? 21.407  41.653 -58.400 1.00 30.79 ? 382 HOH A O   1 
HETATM 1602 O O   . HOH C 2 .  ? 22.527  52.148 -51.670 1.00 31.16 ? 384 HOH A O   1 
HETATM 1603 O O   . HOH C 2 .  ? 18.873  47.659 -43.719 1.00 45.77 ? 388 HOH A O   1 
HETATM 1604 O O   . HOH C 2 .  ? 2.899   33.959 -53.574 1.00 30.66 ? 410 HOH A O   1 
HETATM 1605 O O   . HOH C 2 .  ? 16.396  53.239 -65.299 1.00 62.48 ? 414 HOH A O   1 
HETATM 1606 O O   . HOH C 2 .  ? 6.448   64.555 -45.985 1.00 30.38 ? 420 HOH A O   1 
HETATM 1607 O O   . HOH C 2 .  ? -0.797  43.358 -60.739 1.00 47.13 ? 421 HOH A O   1 
HETATM 1608 O O   . HOH C 2 .  ? 22.834  39.001 -51.554 1.00 31.50 ? 423 HOH A O   1 
HETATM 1609 O O   . HOH C 2 .  ? -2.528  60.831 -52.374 1.00 43.89 ? 424 HOH A O   1 
HETATM 1610 O O   . HOH C 2 .  ? 16.492  49.165 -42.556 1.00 36.46 ? 427 HOH A O   1 
HETATM 1611 O O   . HOH C 2 .  ? 17.580  51.185 -63.320 1.00 43.67 ? 429 HOH A O   1 
HETATM 1612 O O   . HOH C 2 .  ? 14.066  29.990 -50.455 1.00 36.73 ? 431 HOH A O   1 
HETATM 1613 O O   . HOH C 2 .  ? 21.784  61.691 -45.396 1.00 53.37 ? 436 HOH A O   1 
HETATM 1614 O O   . HOH C 2 .  ? 7.431   50.459 -38.668 1.00 62.55 ? 451 HOH A O   1 
HETATM 1615 O O   . HOH C 2 .  ? 4.073   58.953 -61.584 1.00 35.11 ? 463 HOH A O   1 
HETATM 1616 O O   . HOH C 2 .  ? 11.606  54.660 -64.230 1.00 46.09 ? 465 HOH A O   1 
HETATM 1617 O O   . HOH C 2 .  ? 3.888   49.423 -45.686 1.00 53.78 ? 476 HOH A O   1 
HETATM 1618 O O   . HOH C 2 .  ? 2.668   32.477 -55.949 1.00 55.22 ? 478 HOH A O   1 
HETATM 1619 O O   . HOH C 2 .  ? 21.637  35.012 -54.610 1.00 37.85 ? 480 HOH A O   1 
HETATM 1620 O O   . HOH C 2 .  ? 23.148  56.194 -60.800 1.00 30.14 ? 481 HOH A O   1 
HETATM 1621 O O   . HOH C 2 .  ? 6.140   51.720 -68.847 1.00 40.59 ? 483 HOH A O   1 
HETATM 1622 O O   . HOH C 2 .  ? 12.840  52.693 -65.524 1.00 31.44 ? 516 HOH A O   1 
HETATM 1623 O O   . HOH C 2 .  ? 2.546   59.229 -45.986 1.00 42.16 ? 524 HOH A O   1 
HETATM 1624 O O   . HOH C 2 .  ? 21.218  42.280 -62.566 1.00 54.04 ? 535 HOH A O   1 
HETATM 1625 O O   . HOH C 2 .  ? 24.102  37.569 -49.140 1.00 53.24 ? 536 HOH A O   1 
HETATM 1626 O O   . HOH C 2 .  ? 16.250  28.307 -51.230 1.00 50.26 ? 537 HOH A O   1 
HETATM 1627 O O   . HOH C 2 .  ? 17.644  66.659 -48.824 1.00 53.83 ? 546 HOH A O   1 
HETATM 1628 O O   . HOH C 2 .  ? 21.616  37.302 -40.286 1.00 51.97 ? 551 HOH A O   1 
HETATM 1629 O O   . HOH C 2 .  ? 1.004   49.141 -48.400 1.00 53.65 ? 552 HOH A O   1 
HETATM 1630 O O   . HOH C 2 .  ? 13.517  30.055 -43.671 1.00 35.96 ? 563 HOH A O   1 
HETATM 1631 O O   . HOH C 2 .  ? 6.982   43.995 -67.248 1.00 55.07 ? 570 HOH A O   1 
HETATM 1632 O O   . HOH C 2 .  ? 8.691   58.079 -43.531 1.00 61.78 ? 572 HOH A O   1 
HETATM 1633 O O   . HOH C 2 .  ? 6.357   44.937 -46.555 1.00 51.06 ? 573 HOH A O   1 
HETATM 1634 O O   . HOH C 2 .  ? 18.252  58.992 -55.775 1.00 43.03 ? 574 HOH A O   1 
HETATM 1635 O O   . HOH C 2 .  ? 13.317  48.401 -40.810 1.00 59.96 ? 575 HOH A O   1 
HETATM 1636 O O   . HOH C 2 .  ? 20.816  38.984 -59.547 1.00 64.07 ? 581 HOH A O   1 
HETATM 1637 O O   . HOH C 2 .  ? 22.202  38.027 -56.764 1.00 41.18 ? 588 HOH A O   1 
HETATM 1638 O O   . HOH C 2 .  ? 24.096  42.451 -56.380 1.00 56.29 ? 589 HOH A O   1 
HETATM 1639 O O   . HOH C 2 .  ? -2.222  40.750 -59.370 1.00 49.60 ? 590 HOH A O   1 
HETATM 1640 O O   . HOH C 2 .  ? 0.035   46.523 -49.396 1.00 48.78 ? 595 HOH A O   1 
HETATM 1641 O O   . HOH C 2 .  ? 1.705   43.346 -46.071 1.00 47.80 ? 596 HOH A O   1 
HETATM 1642 O O   . HOH D 2 .  ? -6.323  55.173 -47.631 1.00 12.24 ? 305 HOH B O   1 
HETATM 1643 O O   . HOH D 2 .  ? -23.280 47.654 -49.607 1.00 22.46 ? 308 HOH B O   1 
HETATM 1644 O O   . HOH D 2 .  ? -24.333 44.429 -54.777 1.00 28.60 ? 313 HOH B O   1 
HETATM 1645 O O   . HOH D 2 .  ? -22.257 48.857 -43.555 1.00 33.97 ? 316 HOH B O   1 
HETATM 1646 O O   . HOH D 2 .  ? -3.690  52.540 -50.033 1.00 23.39 ? 319 HOH B O   1 
HETATM 1647 O O   . HOH D 2 .  ? 1.907   50.589 -42.984 1.00 24.11 ? 321 HOH B O   1 
HETATM 1648 O O   . HOH D 2 .  ? -2.774  57.786 -59.677 1.00 30.40 ? 322 HOH B O   1 
HETATM 1649 O O   . HOH D 2 .  ? -4.506  59.055 -51.519 1.00 21.40 ? 329 HOH B O   1 
HETATM 1650 O O   . HOH D 2 .  ? -3.404  61.773 -44.950 1.00 28.23 ? 330 HOH B O   1 
HETATM 1651 O O   . HOH D 2 .  ? -20.489 37.805 -36.212 1.00 34.88 ? 333 HOH B O   1 
HETATM 1652 O O   . HOH D 2 .  ? -18.515 43.317 -59.289 1.00 26.46 ? 334 HOH B O   1 
HETATM 1653 O O   . HOH D 2 .  ? -18.745 44.286 -54.012 1.00 30.09 ? 340 HOH B O   1 
HETATM 1654 O O   . HOH D 2 .  ? 0.058   58.840 -39.253 1.00 42.46 ? 352 HOH B O   1 
HETATM 1655 O O   . HOH D 2 .  ? -0.567  55.756 -35.798 1.00 28.19 ? 353 HOH B O   1 
HETATM 1656 O O   . HOH D 2 .  ? -18.946 43.195 -46.536 1.00 21.74 ? 356 HOH B O   1 
HETATM 1657 O O   . HOH D 2 .  ? -9.218  61.746 -56.855 1.00 42.03 ? 357 HOH B O   1 
HETATM 1658 O O   . HOH D 2 .  ? -23.909 43.384 -60.430 1.00 28.60 ? 363 HOH B O   1 
HETATM 1659 O O   . HOH D 2 .  ? -14.645 43.956 -34.843 1.00 27.27 ? 369 HOH B O   1 
HETATM 1660 O O   . HOH D 2 .  ? -0.539  59.628 -44.531 1.00 30.84 ? 371 HOH B O   1 
HETATM 1661 O O   . HOH D 2 .  ? -21.243 45.540 -62.034 1.00 28.35 ? 373 HOH B O   1 
HETATM 1662 O O   . HOH D 2 .  ? 1.000   58.288 -42.782 1.00 34.09 ? 378 HOH B O   1 
HETATM 1663 O O   . HOH D 2 .  ? -11.620 56.908 -31.620 1.00 34.22 ? 386 HOH B O   1 
HETATM 1664 O O   . HOH D 2 .  ? -3.272  44.475 -61.309 1.00 49.64 ? 403 HOH B O   1 
HETATM 1665 O O   . HOH D 2 .  ? -13.858 42.277 -56.330 1.00 46.04 ? 404 HOH B O   1 
HETATM 1666 O O   . HOH D 2 .  ? -18.156 56.406 -50.508 1.00 31.38 ? 406 HOH B O   1 
HETATM 1667 O O   . HOH D 2 .  ? -2.172  54.861 -33.151 1.00 41.17 ? 408 HOH B O   1 
HETATM 1668 O O   . HOH D 2 .  ? -20.022 51.441 -58.682 1.00 38.02 ? 419 HOH B O   1 
HETATM 1669 O O   . HOH D 2 .  ? -15.098 44.596 -57.657 1.00 36.07 ? 428 HOH B O   1 
HETATM 1670 O O   . HOH D 2 .  ? -10.059 44.032 -65.558 1.00 36.92 ? 442 HOH B O   1 
HETATM 1671 O O   . HOH D 2 .  ? -8.958  66.904 -37.190 1.00 45.60 ? 471 HOH B O   1 
HETATM 1672 O O   . HOH D 2 .  ? -2.114  50.169 -50.132 1.00 41.63 ? 474 HOH B O   1 
HETATM 1673 O O   . HOH D 2 .  ? -18.722 53.807 -38.903 1.00 43.41 ? 479 HOH B O   1 
HETATM 1674 O O   . HOH D 2 .  ? -19.340 50.476 -67.487 1.00 40.02 ? 485 HOH B O   1 
HETATM 1675 O O   . HOH D 2 .  ? -17.827 53.886 -36.276 1.00 38.62 ? 486 HOH B O   1 
HETATM 1676 O O   . HOH D 2 .  ? -20.752 50.202 -36.400 1.00 41.47 ? 526 HOH B O   1 
HETATM 1677 O O   . HOH D 2 .  ? -19.224 59.497 -45.343 1.00 38.10 ? 529 HOH B O   1 
HETATM 1678 O O   . HOH D 2 .  ? -7.389  59.835 -59.625 1.00 45.42 ? 539 HOH B O   1 
HETATM 1679 O O   . HOH D 2 .  ? -13.171 61.259 -51.964 1.00 44.55 ? 540 HOH B O   1 
HETATM 1680 O O   . HOH D 2 .  ? -8.051  44.169 -53.147 1.00 52.14 ? 541 HOH B O   1 
HETATM 1681 O O   . HOH D 2 .  ? -23.567 52.528 -61.765 1.00 59.32 ? 542 HOH B O   1 
HETATM 1682 O O   . HOH D 2 .  ? -9.721  40.429 -42.757 1.00 41.14 ? 543 HOH B O   1 
HETATM 1683 O O   . HOH D 2 .  ? -5.572  63.766 -51.417 1.00 44.27 ? 548 HOH B O   1 
HETATM 1684 O O   . HOH D 2 .  ? -0.078  50.828 -62.444 1.00 29.61 ? 549 HOH B O   1 
HETATM 1685 O O   . HOH D 2 .  ? -8.154  52.753 -61.280 1.00 26.04 ? 554 HOH B O   1 
HETATM 1686 O O   . HOH D 2 .  ? -16.188 63.266 -52.594 1.00 33.33 ? 555 HOH B O   1 
HETATM 1687 O O   . HOH D 2 .  ? -15.053 61.224 -38.820 1.00 44.88 ? 558 HOH B O   1 
HETATM 1688 O O   . HOH D 2 .  ? -27.197 51.382 -61.275 1.00 28.96 ? 561 HOH B O   1 
HETATM 1689 O O   . HOH D 2 .  ? -12.367 41.201 -42.479 1.00 52.67 ? 562 HOH B O   1 
HETATM 1690 O O   . HOH D 2 .  ? -14.775 54.922 -57.821 1.00 74.07 ? 568 HOH B O   1 
HETATM 1691 O O   . HOH D 2 .  ? -9.091  51.630 -27.923 1.00 72.20 ? 569 HOH B O   1 
HETATM 1692 O O   . HOH D 2 .  ? -17.994 58.713 -37.436 1.00 56.15 ? 577 HOH B O   1 
HETATM 1693 O O   . HOH D 2 .  ? -21.793 54.937 -52.371 1.00 45.29 ? 578 HOH B O   1 
HETATM 1694 O O   . HOH D 2 .  ? -21.745 43.074 -51.923 1.00 35.12 ? 579 HOH B O   1 
HETATM 1695 O O   . HOH D 2 .  ? 0.264   47.537 -44.344 1.00 50.92 ? 580 HOH B O   1 
HETATM 1696 O O   . HOH D 2 .  ? -2.453  49.879 -63.140 1.00 51.40 ? 582 HOH B O   1 
HETATM 1697 O O   . HOH D 2 .  ? -19.145 55.512 -32.959 1.00 62.16 ? 591 HOH B O   1 
HETATM 1698 O O   . HOH D 2 .  ? -10.999 55.816 -28.732 1.00 53.46 ? 592 HOH B O   1 
HETATM 1699 O O   . HOH D 2 .  ? -0.397  46.537 -46.754 1.00 48.61 ? 593 HOH B O   1 
HETATM 1700 O O   . HOH D 2 .  ? -5.610  40.706 -60.941 1.00 76.71 ? 594 HOH B 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  GLY 1  1  1  GLY GLY A . n 
A 1 2  GLU 2  2  2  GLU GLU A . n 
A 1 3  TRP 3  3  3  TRP TRP A . n 
A 1 4  GLU 4  4  4  GLU GLU A . n 
A 1 5  ILE 5  5  5  ILE ILE A . n 
A 1 6  ILE 6  6  6  ILE ILE A . n 
A 1 7  ASP 7  7  7  ASP ASP A . n 
A 1 8  ILE 8  8  8  ILE ILE A . n 
A 1 9  GLY 9  9  9  GLY GLY A . n 
A 1 10 PRO 10 10 10 PRO PRO A . n 
A 1 11 PHE 11 11 11 PHE PHE A . n 
A 1 12 THR 12 12 12 THR THR A . n 
A 1 13 GLN 13 13 13 GLN GLN A . n 
A 1 14 ASN 14 14 14 ASN ASN A . n 
A 1 15 LEU 15 15 15 LEU LEU A . n 
A 1 16 GLY 16 16 16 GLY GLY A . n 
A 1 17 LYS 17 17 17 LYS LYS A . n 
A 1 18 PHE 18 18 18 PHE PHE A . n 
A 1 19 ALA 19 19 19 ALA ALA A . n 
A 1 20 VAL 20 20 20 VAL VAL A . n 
A 1 21 ASP 21 21 21 ASP ASP A . n 
A 1 22 GLU 22 22 22 GLU GLU A . n 
A 1 23 GLU 23 23 23 GLU GLU A . n 
A 1 24 ASN 24 24 24 ASN ASN A . n 
A 1 25 LYS 25 25 25 LYS LYS A . n 
A 1 26 ILE 26 26 26 ILE ILE A . n 
A 1 27 GLY 27 27 27 GLY GLY A . n 
A 1 28 GLN 28 28 28 GLN GLN A . n 
A 1 29 TYR 29 29 29 TYR TYR A . n 
A 1 30 GLY 30 30 30 GLY GLY A . n 
A 1 31 ARG 31 31 31 ARG ARG A . n 
A 1 32 LEU 32 32 32 LEU LEU A . n 
A 1 33 THR 33 33 33 THR THR A . n 
A 1 34 PHE 34 34 34 PHE PHE A . n 
A 1 35 ASN 35 35 35 ASN ASN A . n 
A 1 36 LYS 36 36 36 LYS LYS A . n 
A 1 37 VAL 37 37 37 VAL VAL A . n 
A 1 38 ILE 38 38 38 ILE ILE A . n 
A 1 39 ARG 39 39 39 ARG ARG A . n 
A 1 40 PRO 40 40 40 PRO PRO A . n 
A 1 41 CYS 41 41 41 CYS CYS A . n 
A 1 42 MET 42 42 42 MET MET A . n 
A 1 43 LYS 43 43 43 LYS LYS A . n 
A 1 44 LYS 44 44 44 LYS LYS A . n 
A 1 45 THR 45 45 45 THR THR A . n 
A 1 46 ILE 46 46 46 ILE ILE A . n 
A 1 47 TYR 47 47 47 TYR TYR A . n 
A 1 48 GLU 48 48 48 GLU GLU A . n 
A 1 49 ASN 49 49 49 ASN ASN A . n 
A 1 50 GLU 50 50 50 GLU GLU A . n 
A 1 51 ARG 51 51 51 ARG ARG A . n 
A 1 52 GLU 52 52 52 GLU GLU A . n 
A 1 53 ILE 53 53 53 ILE ILE A . n 
A 1 54 LYS 54 54 54 LYS LYS A . n 
A 1 55 GLY 55 55 55 GLY GLY A . n 
A 1 56 TYR 56 56 56 TYR TYR A . n 
A 1 57 GLU 57 57 57 GLU GLU A . n 
A 1 58 TYR 58 58 58 TYR TYR A . n 
A 1 59 GLN 59 59 59 GLN GLN A . n 
A 1 60 LEU 60 60 60 LEU LEU A . n 
A 1 61 TYR 61 61 61 TYR TYR A . n 
A 1 62 VAL 62 62 62 VAL VAL A . n 
A 1 63 TYR 63 63 63 TYR TYR A . n 
A 1 64 ALA 64 64 64 ALA ALA A . n 
A 1 65 SER 65 65 65 SER SER A . n 
A 1 66 ASP 66 66 66 ASP ASP A . n 
A 1 67 LYS 67 67 67 LYS LYS A . n 
A 1 68 LEU 68 68 68 LEU LEU A . n 
A 1 69 PHE 69 69 69 PHE PHE A . n 
A 1 70 ARG 70 70 70 ARG ARG A . n 
A 1 71 ALA 71 71 71 ALA ALA A . n 
A 1 72 ASP 72 72 72 ASP ASP A . n 
A 1 73 ILE 73 73 73 ILE ILE A . n 
A 1 74 SER 74 74 74 SER SER A . n 
A 1 75 GLU 75 75 75 GLU GLU A . n 
A 1 76 ASP 76 76 76 ASP ASP A . n 
A 1 77 TYR 77 77 77 TYR TYR A . n 
A 1 78 LYS 78 78 78 LYS LYS A . n 
A 1 79 THR 79 79 79 THR THR A . n 
A 1 80 ARG 80 80 80 ARG ARG A . n 
A 1 81 GLY 81 81 81 GLY GLY A . n 
A 1 82 ARG 82 82 82 ARG ARG A . n 
A 1 83 LYS 83 83 83 LYS LYS A . n 
A 1 84 LEU 84 84 84 LEU LEU A . n 
A 1 85 LEU 85 85 85 LEU LEU A . n 
A 1 86 ARG 86 86 86 ARG ARG A . n 
A 1 87 PHE 87 87 87 PHE PHE A . n 
A 1 88 ASN 88 88 88 ASN ASN A . n 
A 1 89 GLY 89 89 89 GLY GLY A . n 
A 1 90 PRO 90 90 90 PRO PRO A . n 
A 1 91 VAL 91 91 91 VAL VAL A . n 
A 1 92 PRO 92 92 92 PRO PRO A . n 
A 1 93 PRO 93 93 93 PRO PRO A . n 
A 1 94 PRO 94 94 94 PRO PRO A . n 
B 1 1  GLY 1  1  1  GLY GLY B . n 
B 1 2  GLU 2  2  2  GLU GLU B . n 
B 1 3  TRP 3  3  3  TRP TRP B . n 
B 1 4  GLU 4  4  4  GLU GLU B . n 
B 1 5  ILE 5  5  5  ILE ILE B . n 
B 1 6  ILE 6  6  6  ILE ILE B . n 
B 1 7  ASP 7  7  7  ASP ASP B . n 
B 1 8  ILE 8  8  8  ILE ILE B . n 
B 1 9  GLY 9  9  9  GLY GLY B . n 
B 1 10 PRO 10 10 10 PRO PRO B . n 
B 1 11 PHE 11 11 11 PHE PHE B . n 
B 1 12 THR 12 12 12 THR THR B . n 
B 1 13 GLN 13 13 13 GLN GLN B . n 
B 1 14 ASN 14 14 14 ASN ASN B . n 
B 1 15 LEU 15 15 15 LEU LEU B . n 
B 1 16 GLY 16 16 16 GLY GLY B . n 
B 1 17 LYS 17 17 17 LYS LYS B . n 
B 1 18 PHE 18 18 18 PHE PHE B . n 
B 1 19 ALA 19 19 19 ALA ALA B . n 
B 1 20 VAL 20 20 20 VAL VAL B . n 
B 1 21 ASP 21 21 21 ASP ASP B . n 
B 1 22 GLU 22 22 22 GLU GLU B . n 
B 1 23 GLU 23 23 23 GLU GLU B . n 
B 1 24 ASN 24 24 24 ASN ASN B . n 
B 1 25 LYS 25 25 25 LYS LYS B . n 
B 1 26 ILE 26 26 26 ILE ILE B . n 
B 1 27 GLY 27 27 27 GLY GLY B . n 
B 1 28 GLN 28 28 28 GLN GLN B . n 
B 1 29 TYR 29 29 29 TYR TYR B . n 
B 1 30 GLY 30 30 30 GLY GLY B . n 
B 1 31 ARG 31 31 31 ARG ARG B . n 
B 1 32 LEU 32 32 32 LEU LEU B . n 
B 1 33 THR 33 33 33 THR THR B . n 
B 1 34 PHE 34 34 34 PHE PHE B . n 
B 1 35 ASN 35 35 35 ASN ASN B . n 
B 1 36 LYS 36 36 36 LYS LYS B . n 
B 1 37 VAL 37 37 37 VAL VAL B . n 
B 1 38 ILE 38 38 38 ILE ILE B . n 
B 1 39 ARG 39 39 39 ARG ARG B . n 
B 1 40 PRO 40 40 40 PRO PRO B . n 
B 1 41 CYS 41 41 41 CYS CYS B . n 
B 1 42 MET 42 42 42 MET MET B . n 
B 1 43 LYS 43 43 43 LYS LYS B . n 
B 1 44 LYS 44 44 44 LYS LYS B . n 
B 1 45 THR 45 45 45 THR THR B . n 
B 1 46 ILE 46 46 46 ILE ILE B . n 
B 1 47 TYR 47 47 47 TYR TYR B . n 
B 1 48 GLU 48 48 48 GLU GLU B . n 
B 1 49 ASN 49 49 49 ASN ASN B . n 
B 1 50 GLU 50 50 50 GLU GLU B . n 
B 1 51 ARG 51 51 51 ARG ARG B . n 
B 1 52 GLU 52 52 52 GLU GLU B . n 
B 1 53 ILE 53 53 53 ILE ILE B . n 
B 1 54 LYS 54 54 54 LYS LYS B . n 
B 1 55 GLY 55 55 55 GLY GLY B . n 
B 1 56 TYR 56 56 56 TYR TYR B . n 
B 1 57 GLU 57 57 57 GLU GLU B . n 
B 1 58 TYR 58 58 58 TYR TYR B . n 
B 1 59 GLN 59 59 59 GLN GLN B . n 
B 1 60 LEU 60 60 60 LEU LEU B . n 
B 1 61 TYR 61 61 61 TYR TYR B . n 
B 1 62 VAL 62 62 62 VAL VAL B . n 
B 1 63 TYR 63 63 63 TYR TYR B . n 
B 1 64 ALA 64 64 64 ALA ALA B . n 
B 1 65 SER 65 65 65 SER SER B . n 
B 1 66 ASP 66 66 66 ASP ASP B . n 
B 1 67 LYS 67 67 67 LYS LYS B . n 
B 1 68 LEU 68 68 68 LEU LEU B . n 
B 1 69 PHE 69 69 69 PHE PHE B . n 
B 1 70 ARG 70 70 70 ARG ARG B . n 
B 1 71 ALA 71 71 71 ALA ALA B . n 
B 1 72 ASP 72 72 72 ASP ASP B . n 
B 1 73 ILE 73 73 73 ILE ILE B . n 
B 1 74 SER 74 74 74 SER SER B . n 
B 1 75 GLU 75 75 75 GLU GLU B . n 
B 1 76 ASP 76 76 76 ASP ASP B . n 
B 1 77 TYR 77 77 77 TYR TYR B . n 
B 1 78 LYS 78 78 78 LYS LYS B . n 
B 1 79 THR 79 79 79 THR THR B . n 
B 1 80 ARG 80 80 80 ARG ARG B . n 
B 1 81 GLY 81 81 81 GLY GLY B . n 
B 1 82 ARG 82 82 82 ARG ARG B . n 
B 1 83 LYS 83 83 83 LYS LYS B . n 
B 1 84 LEU 84 84 84 LEU LEU B . n 
B 1 85 LEU 85 85 85 LEU LEU B . n 
B 1 86 ARG 86 86 86 ARG ARG B . n 
B 1 87 PHE 87 87 87 PHE PHE B . n 
B 1 88 ASN 88 88 88 ASN ASN B . n 
B 1 89 GLY 89 89 89 GLY GLY B . n 
B 1 90 PRO 90 90 90 PRO PRO B . n 
B 1 91 VAL 91 91 91 VAL VAL B . n 
B 1 92 PRO 92 92 92 PRO PRO B . n 
B 1 93 PRO 93 93 93 PRO PRO B . n 
B 1 94 PRO 94 94 94 PRO PRO B . 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 
C 2 HOH 1  301 301 HOH HOH A . 
C 2 HOH 2  302 302 HOH HOH A . 
C 2 HOH 3  303 303 HOH HOH A . 
C 2 HOH 4  304 304 HOH HOH A . 
C 2 HOH 5  306 306 HOH HOH A . 
C 2 HOH 6  307 307 HOH HOH A . 
C 2 HOH 7  309 309 HOH HOH A . 
C 2 HOH 8  310 310 HOH HOH A . 
C 2 HOH 9  311 311 HOH HOH A . 
C 2 HOH 10 312 312 HOH HOH A . 
C 2 HOH 11 318 318 HOH HOH A . 
C 2 HOH 12 320 320 HOH HOH A . 
C 2 HOH 13 323 323 HOH HOH A . 
C 2 HOH 14 324 324 HOH HOH A . 
C 2 HOH 15 325 325 HOH HOH A . 
C 2 HOH 16 326 326 HOH HOH A . 
C 2 HOH 17 327 327 HOH HOH A . 
C 2 HOH 18 328 328 HOH HOH A . 
C 2 HOH 19 336 336 HOH HOH A . 
C 2 HOH 20 343 343 HOH HOH A . 
C 2 HOH 21 344 344 HOH HOH A . 
C 2 HOH 22 345 345 HOH HOH A . 
C 2 HOH 23 346 346 HOH HOH A . 
C 2 HOH 24 348 348 HOH HOH A . 
C 2 HOH 25 349 349 HOH HOH A . 
C 2 HOH 26 350 350 HOH HOH A . 
C 2 HOH 27 351 351 HOH HOH A . 
C 2 HOH 28 354 354 HOH HOH A . 
C 2 HOH 29 358 358 HOH HOH A . 
C 2 HOH 30 359 359 HOH HOH A . 
C 2 HOH 31 362 362 HOH HOH A . 
C 2 HOH 32 364 364 HOH HOH A . 
C 2 HOH 33 367 367 HOH HOH A . 
C 2 HOH 34 377 377 HOH HOH A . 
C 2 HOH 35 382 382 HOH HOH A . 
C 2 HOH 36 384 384 HOH HOH A . 
C 2 HOH 37 388 388 HOH HOH A . 
C 2 HOH 38 410 410 HOH HOH A . 
C 2 HOH 39 414 414 HOH HOH A . 
C 2 HOH 40 420 420 HOH HOH A . 
C 2 HOH 41 421 421 HOH HOH A . 
C 2 HOH 42 423 423 HOH HOH A . 
C 2 HOH 43 424 424 HOH HOH A . 
C 2 HOH 44 427 427 HOH HOH A . 
C 2 HOH 45 429 429 HOH HOH A . 
C 2 HOH 46 431 431 HOH HOH A . 
C 2 HOH 47 436 436 HOH HOH A . 
C 2 HOH 48 451 451 HOH HOH A . 
C 2 HOH 49 463 463 HOH HOH A . 
C 2 HOH 50 465 465 HOH HOH A . 
C 2 HOH 51 476 476 HOH HOH A . 
C 2 HOH 52 478 478 HOH HOH A . 
C 2 HOH 53 480 480 HOH HOH A . 
C 2 HOH 54 481 481 HOH HOH A . 
C 2 HOH 55 483 483 HOH HOH A . 
C 2 HOH 56 516 516 HOH HOH A . 
C 2 HOH 57 524 524 HOH HOH A . 
C 2 HOH 58 535 535 HOH HOH A . 
C 2 HOH 59 536 536 HOH HOH A . 
C 2 HOH 60 537 537 HOH HOH A . 
C 2 HOH 61 546 546 HOH HOH A . 
C 2 HOH 62 551 551 HOH HOH A . 
C 2 HOH 63 552 552 HOH HOH A . 
C 2 HOH 64 563 563 HOH HOH A . 
C 2 HOH 65 570 570 HOH HOH A . 
C 2 HOH 66 572 572 HOH HOH A . 
C 2 HOH 67 573 573 HOH HOH A . 
C 2 HOH 68 574 574 HOH HOH A . 
C 2 HOH 69 575 575 HOH HOH A . 
C 2 HOH 70 581 581 HOH HOH A . 
C 2 HOH 71 588 588 HOH HOH A . 
C 2 HOH 72 589 589 HOH HOH A . 
C 2 HOH 73 590 590 HOH HOH A . 
C 2 HOH 74 595 595 HOH HOH A . 
C 2 HOH 75 596 596 HOH HOH A . 
D 2 HOH 1  305 305 HOH HOH B . 
D 2 HOH 2  308 308 HOH HOH B . 
D 2 HOH 3  313 313 HOH HOH B . 
D 2 HOH 4  316 316 HOH HOH B . 
D 2 HOH 5  319 319 HOH HOH B . 
D 2 HOH 6  321 321 HOH HOH B . 
D 2 HOH 7  322 322 HOH HOH B . 
D 2 HOH 8  329 329 HOH HOH B . 
D 2 HOH 9  330 330 HOH HOH B . 
D 2 HOH 10 333 333 HOH HOH B . 
D 2 HOH 11 334 334 HOH HOH B . 
D 2 HOH 12 340 340 HOH HOH B . 
D 2 HOH 13 352 352 HOH HOH B . 
D 2 HOH 14 353 353 HOH HOH B . 
D 2 HOH 15 356 356 HOH HOH B . 
D 2 HOH 16 357 357 HOH HOH B . 
D 2 HOH 17 363 363 HOH HOH B . 
D 2 HOH 18 369 369 HOH HOH B . 
D 2 HOH 19 371 371 HOH HOH B . 
D 2 HOH 20 373 373 HOH HOH B . 
D 2 HOH 21 378 378 HOH HOH B . 
D 2 HOH 22 386 386 HOH HOH B . 
D 2 HOH 23 403 403 HOH HOH B . 
D 2 HOH 24 404 404 HOH HOH B . 
D 2 HOH 25 406 406 HOH HOH B . 
D 2 HOH 26 408 408 HOH HOH B . 
D 2 HOH 27 419 419 HOH HOH B . 
D 2 HOH 28 428 428 HOH HOH B . 
D 2 HOH 29 442 442 HOH HOH B . 
D 2 HOH 30 471 471 HOH HOH B . 
D 2 HOH 31 474 474 HOH HOH B . 
D 2 HOH 32 479 479 HOH HOH B . 
D 2 HOH 33 485 485 HOH HOH B . 
D 2 HOH 34 486 486 HOH HOH B . 
D 2 HOH 35 526 526 HOH HOH B . 
D 2 HOH 36 529 529 HOH HOH B . 
D 2 HOH 37 539 539 HOH HOH B . 
D 2 HOH 38 540 540 HOH HOH B . 
D 2 HOH 39 541 541 HOH HOH B . 
D 2 HOH 40 542 542 HOH HOH B . 
D 2 HOH 41 543 543 HOH HOH B . 
D 2 HOH 42 548 548 HOH HOH B . 
D 2 HOH 43 549 549 HOH HOH B . 
D 2 HOH 44 554 554 HOH HOH B . 
D 2 HOH 45 555 555 HOH HOH B . 
D 2 HOH 46 558 558 HOH HOH B . 
D 2 HOH 47 561 561 HOH HOH B . 
D 2 HOH 48 562 562 HOH HOH B . 
D 2 HOH 49 568 568 HOH HOH B . 
D 2 HOH 50 569 569 HOH HOH B . 
D 2 HOH 51 577 577 HOH HOH B . 
D 2 HOH 52 578 578 HOH HOH B . 
D 2 HOH 53 579 579 HOH HOH B . 
D 2 HOH 54 580 580 HOH HOH B . 
D 2 HOH 55 582 582 HOH HOH B . 
D 2 HOH 56 591 591 HOH HOH B . 
D 2 HOH 57 592 592 HOH HOH B . 
D 2 HOH 58 593 593 HOH HOH B . 
D 2 HOH 59 594 594 HOH HOH B . 
# 
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_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C 
2 1 B,D 
# 
_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_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 1994-05-31 
2 'Structure model' 1 1 2008-03-24 
3 'Structure model' 1 2 2011-07-13 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
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' 
# 
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 
# 
loop_
_pdbx_database_remark.id 
_pdbx_database_remark.text 
650 
;HELIX
THERE IS A SINGLE RIGHT-HANDED ALPHA-HELIX IN EACH OF THE
MONOMERS PRESENT IN THE ASYMMETRIC UNIT.
;
700 
;SHEET
EACH OF THE MONOMERS IN THE ASYMMETRIC UNIT CONTAINS A
SINGLE, FIVE-STRAND ANTIPARALLEL BETA-SHEET.
;
# 
_pdbx_entry_details.entry_id             1MOL 
_pdbx_entry_details.compound_details     ? 
_pdbx_entry_details.source_details       ? 
_pdbx_entry_details.nonpolymer_details   ? 
_pdbx_entry_details.sequence_details     
;SEQUENCE ADVISORY NOTICE
     DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE.

     SWISS-PROT ENTRY NAME: MONB_DIOCU

     SWISS-PROT RESIDUE      PDB SEQRES

       NAME   NUMBER         NAME   CHAIN  SEQ/INSERT CODE
       GLU       49          ASN     A       49
       ASN       50          GLU     A       50
;
# 
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 3  ? ? CG  A TRP 3  ? ? CD2 A TRP 3  ? ? 112.33 106.30 6.03  0.80 N 
2  1 CE2 A TRP 3  ? ? CD2 A TRP 3  ? ? CG  A TRP 3  ? ? 101.88 107.30 -5.42 0.80 N 
3  1 NE  A ARG 39 ? ? CZ  A ARG 39 ? ? NH1 A ARG 39 ? ? 124.01 120.30 3.71  0.50 N 
4  1 CB  A TYR 56 ? ? CG  A TYR 56 ? ? CD1 A TYR 56 ? ? 116.26 121.00 -4.74 0.60 N 
5  1 NE  A ARG 82 ? ? CZ  A ARG 82 ? ? NH2 A ARG 82 ? ? 115.67 120.30 -4.63 0.50 N 
6  1 NE  A ARG 86 ? ? CZ  A ARG 86 ? ? NH1 A ARG 86 ? ? 125.72 120.30 5.42  0.50 N 
7  1 CD1 B TRP 3  ? ? CG  B TRP 3  ? ? CD2 B TRP 3  ? ? 114.08 106.30 7.78  0.80 N 
8  1 CE2 B TRP 3  ? ? CD2 B TRP 3  ? ? CG  B TRP 3  ? ? 100.97 107.30 -6.33 0.80 N 
9  1 NE  B ARG 39 ? ? CZ  B ARG 39 ? ? NH1 B ARG 39 ? ? 123.36 120.30 3.06  0.50 N 
10 1 NE  B ARG 51 ? ? CZ  B ARG 51 ? ? NH1 B ARG 51 ? ? 123.79 120.30 3.49  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 ASN A 49 ? ? 46.42  -130.84 
2 1 ILE B 8  ? ? -91.37 49.33   
3 1 ASP B 66 ? ? 56.50  18.34   
4 1 ARG B 80 ? ? 58.40  18.61   
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
