data_3ECU
# 
_entry.id   3ECU 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.281 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   3ECU         
RCSB  RCSB049162   
WWPDB D_1000049162 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 3ECV . unspecified 
PDB 3ECW . unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        3ECU 
_pdbx_database_status.recvd_initial_deposition_date   2008-09-02 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_cs                  ? 
# 
_audit_author.name           'Calderone, V.' 
_audit_author.pdbx_ordinal   1 
# 
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 'Structural and dynamic aspects related to oligomerization of apo SOD1 and its mutants.' Proc.Natl.Acad.Sci.USA 106 6980  
6985  2009 PNASA6 US 0027-8424 0040 ? 19369197 10.1073/pnas.0809845106 
1       
;Metal-free superoxide dismutase forms soluble oligomers under physiological conditions: a possible general mechanism for familial ALS.
;
Proc.Natl.Acad.Sci.USA 104 11263 11267 2007 PNASA6 US 0027-8424 0040 ? ?        ?                       
2       'SOD1 and amyotrophic lateral sclerosis: mutations and oligomerization.' 'PLoS ONE'             3   1677  ?     2008 ? US 
1932-6203 ?    ? ?        ?                       
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Banci, L.'        1  
primary 'Bertini, I.'      2  
primary 'Boca, M.'         3  
primary 'Calderone, V.'    4  
primary 'Cantini, F.'      5  
primary 'Girotto, S.'      6  
primary 'Vieru, M.'        7  
1       'Banci, L.'        8  
1       'Bertini, I.'      9  
1       'Durazo, A.'       10 
1       'Girotto, S.'      11 
1       'Gralla, E.B.'     12 
1       'Martinelli, M.'   13 
1       'Valentine, J.S.'  14 
1       'Vieru, M.'        15 
1       'Whitelegge, J.P.' 16 
2       'Banci, L.'        17 
2       'Bertini, I.'      18 
2       'Boca, M.'         19 
2       'Girotto, S.'      20 
2       'Martinelli, M.'   21 
2       'Valentine, J.S.'  22 
2       'Vieru, M.'        23 
# 
_cell.entry_id           3ECU 
_cell.length_a           156.169 
_cell.length_b           33.528 
_cell.length_c           113.982 
_cell.angle_alpha        90.00 
_cell.angle_beta         111.64 
_cell.angle_gamma        90.00 
_cell.Z_PDB              16 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         3ECU 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer man 'Superoxide dismutase [Cu-Zn]' 15827.561 4   1.15.1.1 ? ? ? 
2 water   nat water                          18.015    299 ?        ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   THR n 
1 3   LYS n 
1 4   ALA n 
1 5   VAL n 
1 6   CYS n 
1 7   VAL n 
1 8   LEU n 
1 9   LYS n 
1 10  GLY n 
1 11  ASP n 
1 12  GLY n 
1 13  PRO n 
1 14  VAL n 
1 15  GLN n 
1 16  GLY n 
1 17  ILE n 
1 18  ILE n 
1 19  ASN n 
1 20  PHE n 
1 21  GLU n 
1 22  GLN n 
1 23  LYS n 
1 24  GLU n 
1 25  SER n 
1 26  ASN n 
1 27  GLY n 
1 28  PRO n 
1 29  VAL n 
1 30  LYS n 
1 31  VAL n 
1 32  TRP n 
1 33  GLY n 
1 34  SER n 
1 35  ILE n 
1 36  LYS n 
1 37  GLY n 
1 38  LEU n 
1 39  THR n 
1 40  GLU n 
1 41  GLY n 
1 42  LEU n 
1 43  HIS n 
1 44  GLY n 
1 45  PHE n 
1 46  HIS n 
1 47  VAL n 
1 48  HIS n 
1 49  GLU n 
1 50  PHE n 
1 51  GLY n 
1 52  ASP n 
1 53  ASN n 
1 54  THR n 
1 55  ALA n 
1 56  GLY n 
1 57  CYS n 
1 58  THR n 
1 59  SER n 
1 60  ALA n 
1 61  GLY n 
1 62  PRO n 
1 63  HIS n 
1 64  PHE n 
1 65  ASN n 
1 66  PRO n 
1 67  LEU n 
1 68  SER n 
1 69  ARG n 
1 70  LYS n 
1 71  HIS n 
1 72  GLY n 
1 73  GLY n 
1 74  PRO n 
1 75  LYS n 
1 76  ASP n 
1 77  GLU n 
1 78  GLU n 
1 79  ARG n 
1 80  HIS n 
1 81  VAL n 
1 82  GLY n 
1 83  ASP n 
1 84  LEU n 
1 85  GLY n 
1 86  ASN n 
1 87  VAL n 
1 88  THR n 
1 89  ALA n 
1 90  ASP n 
1 91  LYS n 
1 92  ASP n 
1 93  GLY n 
1 94  VAL n 
1 95  ALA n 
1 96  ASP n 
1 97  VAL n 
1 98  SER n 
1 99  ILE n 
1 100 GLU n 
1 101 ASP n 
1 102 SER n 
1 103 VAL n 
1 104 ILE n 
1 105 SER n 
1 106 LEU n 
1 107 SER n 
1 108 GLY n 
1 109 ASP n 
1 110 HIS n 
1 111 CYS n 
1 112 ILE n 
1 113 ILE n 
1 114 GLY n 
1 115 ARG n 
1 116 THR n 
1 117 LEU n 
1 118 VAL n 
1 119 VAL n 
1 120 HIS n 
1 121 GLU n 
1 122 LYS n 
1 123 ALA n 
1 124 ASP n 
1 125 ASP n 
1 126 LEU n 
1 127 GLY n 
1 128 LYS n 
1 129 GLY n 
1 130 GLY n 
1 131 ASN n 
1 132 GLU n 
1 133 GLU n 
1 134 SER n 
1 135 THR n 
1 136 LYS n 
1 137 THR n 
1 138 GLY n 
1 139 ASN n 
1 140 ALA n 
1 141 GLY n 
1 142 SER n 
1 143 ARG n 
1 144 LEU n 
1 145 ALA n 
1 146 CYS n 
1 147 GLY n 
1 148 VAL n 
1 149 ILE n 
1 150 GLY n 
1 151 ILE n 
1 152 ALA n 
1 153 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               Human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 SOD1 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_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               'Origami pLysS' 
_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          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pENTR/TEV/D-TOPO 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    SODC_HUMAN 
_struct_ref.pdbx_db_accession          P00441 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_struct_ref.pdbx_align_begin           2 
_struct_ref.pdbx_db_isoform            ? 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 3ECU A 1 ? 153 ? P00441 2 ? 154 ? 1 153 
2 1 3ECU B 1 ? 153 ? P00441 2 ? 154 ? 1 153 
3 1 3ECU C 1 ? 153 ? P00441 2 ? 154 ? 1 153 
4 1 3ECU D 1 ? 153 ? P00441 2 ? 154 ? 1 153 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
_exptl.entry_id          3ECU 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.19 
_exptl_crystal.density_percent_sol   43.85 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.temp            289.1 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              6.5 
_exptl_crystal_grow.pdbx_details    
;0.1 M MES 
20% PEG 3350, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 289.1K
;
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'OXFORD ONYX CCD' 
_diffrn_detector.pdbx_collection_date   2007-04-30 
_diffrn_detector.details                Mirrors 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    GRAPHITE 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.54056 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      'SEALED TUBE' 
_diffrn_source.type                        'OXFORD DIFFRACTION ENHANCE ULTRA' 
_diffrn_source.pdbx_synchrotron_site       ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        1.54056 
# 
_reflns.entry_id                     3ECU 
_reflns.observed_criterion_sigma_I   0 
_reflns.observed_criterion_sigma_F   0 
_reflns.d_resolution_low             106 
_reflns.d_resolution_high            1.9 
_reflns.number_obs                   42832 
_reflns.number_all                   42832 
_reflns.percent_possible_obs         97.6 
_reflns.pdbx_Rmerge_I_obs            0.153 
_reflns.pdbx_Rsym_value              0.153 
_reflns.pdbx_netI_over_sigmaI        4.4 
_reflns.B_iso_Wilson_estimate        10.7 
_reflns.pdbx_redundancy              6.7 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
_reflns_shell.d_res_high             1.9 
_reflns_shell.d_res_low              2.0 
_reflns_shell.percent_possible_all   92.9 
_reflns_shell.Rmerge_I_obs           0.409 
_reflns_shell.pdbx_Rsym_value        0.409 
_reflns_shell.meanI_over_sigI_obs    4.1 
_reflns_shell.pdbx_redundancy        5.0 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      5890 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_diffrn_id         ? 
_reflns_shell.pdbx_ordinal           1 
# 
_refine.entry_id                                 3ECU 
_refine.ls_number_reflns_obs                     38952 
_refine.ls_number_reflns_all                     38952 
_refine.pdbx_ls_sigma_I                          0 
_refine.pdbx_ls_sigma_F                          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                             39.01 
_refine.ls_d_res_high                            1.90 
_refine.ls_percent_reflns_obs                    100.00 
_refine.ls_R_factor_obs                          0.24308 
_refine.ls_R_factor_all                          0.24308 
_refine.ls_R_factor_R_work                       0.23948 
_refine.ls_R_factor_R_free                       0.27909 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 9.1 
_refine.ls_number_reflns_R_free                  3880 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.908 
_refine.correlation_coeff_Fo_to_Fc_free          0.876 
_refine.B_iso_mean                               18.683 
_refine.aniso_B[1][1]                            -1.44 
_refine.aniso_B[2][2]                            2.22 
_refine.aniso_B[3][3]                            -1.28 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.67 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.40 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.pdbx_starting_model                      1HL5 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             Isotropic 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.210 
_refine.pdbx_overall_ESU_R_Free                  0.182 
_refine.overall_SU_ML                            0.146 
_refine.overall_SU_B                             5.164 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        4027 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.number_atoms_solvent             299 
_refine_hist.number_atoms_total               4326 
_refine_hist.d_res_high                       1.90 
_refine_hist.d_res_low                        39.01 
# 
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 
r_bond_refined_d         0.025  0.021  ? 4095 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg      2.412  1.942  ? 5532 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg   8.401  5.000  ? 547  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg   41.373 25.556 ? 171  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg   19.496 15.000 ? 659  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg   21.335 15.000 ? 13   'X-RAY DIFFRACTION' ? 
r_chiral_restr           0.161  0.200  ? 621  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined     0.010  0.020  ? 3105 'X-RAY DIFFRACTION' ? 
r_nbd_refined            0.258  0.200  ? 1894 'X-RAY DIFFRACTION' ? 
r_nbtor_refined          0.321  0.200  ? 2671 'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined    0.239  0.200  ? 343  'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined   0.199  0.200  ? 47   'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined 0.164  0.200  ? 10   'X-RAY DIFFRACTION' ? 
r_mcbond_it              1.363  1.500  ? 2783 'X-RAY DIFFRACTION' ? 
r_mcangle_it             2.111  2.000  ? 4299 'X-RAY DIFFRACTION' ? 
r_scbond_it              3.193  3.000  ? 1456 'X-RAY DIFFRACTION' ? 
r_scangle_it             4.634  4.500  ? 1233 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       1.900 
_refine_ls_shell.d_res_low                        1.949 
_refine_ls_shell.number_reflns_R_work             2622 
_refine_ls_shell.R_factor_R_work                  0.320 
_refine_ls_shell.percent_reflns_obs               100.00 
_refine_ls_shell.R_factor_R_free                  0.364 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             255 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  3ECU 
_struct.title                     'Crystal structure of human apo Cu,Zn Superoxide Dismutase (SOD1)' 
_struct.pdbx_descriptor           'Superoxide dismutase [Cu-Zn] (E.C.1.15.1.1)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3ECU 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
_struct_keywords.text            
;HUMAN SUPEROXIDE DISMUTASE, HOMODIMERIC PROTEIN, APO PROTEIN, AGGREGATION, Acetylation, Amyotrophic lateral sclerosis, Antioxidant, Copper, Cytoplasm, Disease mutation, Metal-binding, Oxidoreductase, Ubl conjugation, Zinc
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 1 ? 
E N N 2 ? 
F N N 2 ? 
G N N 2 ? 
H N N 2 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 1 ALA A 55  ? GLY A 61  ? ALA A 55  GLY A 61  5 ? 7 
HELX_P HELX_P2 2 ASN A 131 ? THR A 135 ? ASN A 131 THR A 135 5 ? 5 
HELX_P HELX_P3 3 ALA B 55  ? GLY B 61  ? ALA B 55  GLY B 61  5 ? 7 
HELX_P HELX_P4 4 SER B 107 ? CYS B 111 ? SER B 107 CYS B 111 5 ? 5 
HELX_P HELX_P5 5 ASN B 131 ? LYS B 136 ? ASN B 131 LYS B 136 5 ? 6 
HELX_P HELX_P6 6 ALA C 55  ? GLY C 61  ? ALA C 55  GLY C 61  5 ? 7 
HELX_P HELX_P7 7 ALA D 55  ? GLY D 61  ? ALA D 55  GLY D 61  5 ? 7 
HELX_P HELX_P8 8 SER D 107 ? CYS D 111 ? SER D 107 CYS D 111 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1 disulf ? ? A CYS 57 SG ? ? ? 1_555 A CYS 146 SG ? ? A CYS 57 A CYS 146 1_555 ? ? ? ? ? ? ? 2.038 ? 
disulf2 disulf ? ? B CYS 57 SG ? ? ? 1_555 B CYS 146 SG ? ? B CYS 57 B CYS 146 1_555 ? ? ? ? ? ? ? 2.005 ? 
disulf3 disulf ? ? C CYS 57 SG ? ? ? 1_555 C CYS 146 SG ? ? C CYS 57 C CYS 146 1_555 ? ? ? ? ? ? ? 2.059 ? 
disulf4 disulf ? ? D CYS 57 SG ? ? ? 1_555 D CYS 146 SG ? ? D CYS 57 D CYS 146 1_555 ? ? ? ? ? ? ? 2.021 ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 5 ? 
B ? 4 ? 
C ? 5 ? 
D ? 4 ? 
E ? 5 ? 
F ? 4 ? 
G ? 5 ? 
H ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2 ? anti-parallel 
A 2 3 ? anti-parallel 
A 3 4 ? anti-parallel 
A 4 5 ? anti-parallel 
B 1 2 ? anti-parallel 
B 2 3 ? anti-parallel 
B 3 4 ? anti-parallel 
C 1 2 ? anti-parallel 
C 2 3 ? anti-parallel 
C 3 4 ? anti-parallel 
C 4 5 ? anti-parallel 
D 1 2 ? anti-parallel 
D 2 3 ? anti-parallel 
D 3 4 ? anti-parallel 
E 1 2 ? anti-parallel 
E 2 3 ? anti-parallel 
E 3 4 ? anti-parallel 
E 4 5 ? anti-parallel 
F 1 2 ? anti-parallel 
F 2 3 ? anti-parallel 
F 3 4 ? anti-parallel 
G 1 2 ? anti-parallel 
G 2 3 ? anti-parallel 
G 3 4 ? anti-parallel 
G 4 5 ? anti-parallel 
H 1 2 ? anti-parallel 
H 2 3 ? anti-parallel 
H 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1 ALA A 95  ? ASP A 101 ? ALA A 95  ASP A 101 
A 2 VAL A 29  ? LYS A 36  ? VAL A 29  LYS A 36  
A 3 GLN A 15  ? GLN A 22  ? GLN A 15  GLN A 22  
A 4 THR A 2   ? LEU A 8   ? THR A 2   LEU A 8   
A 5 GLY A 150 ? ILE A 151 ? GLY A 150 ILE A 151 
B 1 ASP A 83  ? ALA A 89  ? ASP A 83  ALA A 89  
B 2 GLY A 41  ? HIS A 48  ? GLY A 41  HIS A 48  
B 3 THR A 116 ? HIS A 120 ? THR A 116 HIS A 120 
B 4 ARG A 143 ? VAL A 148 ? ARG A 143 VAL A 148 
C 1 ALA B 95  ? ASP B 101 ? ALA B 95  ASP B 101 
C 2 VAL B 29  ? LYS B 36  ? VAL B 29  LYS B 36  
C 3 GLN B 15  ? GLU B 21  ? GLN B 15  GLU B 21  
C 4 LYS B 3   ? LEU B 8   ? LYS B 3   LEU B 8   
C 5 GLY B 150 ? ILE B 151 ? GLY B 150 ILE B 151 
D 1 ASP B 83  ? ALA B 89  ? ASP B 83  ALA B 89  
D 2 GLY B 41  ? HIS B 48  ? GLY B 41  HIS B 48  
D 3 THR B 116 ? HIS B 120 ? THR B 116 HIS B 120 
D 4 ARG B 143 ? VAL B 148 ? ARG B 143 VAL B 148 
E 1 ALA C 95  ? ASP C 101 ? ALA C 95  ASP C 101 
E 2 VAL C 29  ? LYS C 36  ? VAL C 29  LYS C 36  
E 3 GLN C 15  ? GLU C 21  ? GLN C 15  GLU C 21  
E 4 LYS C 3   ? LEU C 8   ? LYS C 3   LEU C 8   
E 5 GLY C 150 ? ILE C 151 ? GLY C 150 ILE C 151 
F 1 ASP C 83  ? ALA C 89  ? ASP C 83  ALA C 89  
F 2 GLY C 41  ? HIS C 48  ? GLY C 41  HIS C 48  
F 3 THR C 116 ? HIS C 120 ? THR C 116 HIS C 120 
F 4 ARG C 143 ? VAL C 148 ? ARG C 143 VAL C 148 
G 1 ALA D 95  ? ASP D 101 ? ALA D 95  ASP D 101 
G 2 VAL D 29  ? LYS D 36  ? VAL D 29  LYS D 36  
G 3 GLN D 15  ? GLU D 21  ? GLN D 15  GLU D 21  
G 4 LYS D 3   ? LEU D 8   ? LYS D 3   LEU D 8   
G 5 GLY D 150 ? ILE D 151 ? GLY D 150 ILE D 151 
H 1 ASP D 83  ? ALA D 89  ? ASP D 83  ALA D 89  
H 2 GLY D 41  ? HIS D 48  ? GLY D 41  HIS D 48  
H 3 THR D 116 ? HIS D 120 ? THR D 116 HIS D 120 
H 4 ARG D 143 ? VAL D 148 ? ARG D 143 VAL D 148 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2 O ASP A 101 ? O ASP A 101 N VAL A 29  ? N VAL A 29  
A 2 3 O LYS A 30  ? O LYS A 30  N GLU A 21  ? N GLU A 21  
A 3 4 O GLY A 16  ? O GLY A 16  N LEU A 8   ? N LEU A 8   
A 4 5 N VAL A 5   ? N VAL A 5   O GLY A 150 ? O GLY A 150 
B 1 2 O ALA A 89  ? O ALA A 89  N GLY A 41  ? N GLY A 41  
B 2 3 N GLY A 44  ? N GLY A 44  O HIS A 120 ? O HIS A 120 
B 3 4 N LEU A 117 ? N LEU A 117 O GLY A 147 ? O GLY A 147 
C 1 2 O ASP B 101 ? O ASP B 101 N VAL B 29  ? N VAL B 29  
C 2 3 O LYS B 30  ? O LYS B 30  N GLU B 21  ? N GLU B 21  
C 3 4 O GLY B 16  ? O GLY B 16  N LEU B 8   ? N LEU B 8   
C 4 5 N VAL B 5   ? N VAL B 5   O GLY B 150 ? O GLY B 150 
D 1 2 O ALA B 89  ? O ALA B 89  N GLY B 41  ? N GLY B 41  
D 2 3 N HIS B 46  ? N HIS B 46  O VAL B 118 ? O VAL B 118 
D 3 4 N LEU B 117 ? N LEU B 117 O GLY B 147 ? O GLY B 147 
E 1 2 O ASP C 101 ? O ASP C 101 N VAL C 29  ? N VAL C 29  
E 2 3 O TRP C 32  ? O TRP C 32  N ASN C 19  ? N ASN C 19  
E 3 4 O ILE C 18  ? O ILE C 18  N CYS C 6   ? N CYS C 6   
E 4 5 N VAL C 5   ? N VAL C 5   O GLY C 150 ? O GLY C 150 
F 1 2 O ALA C 89  ? O ALA C 89  N GLY C 41  ? N GLY C 41  
F 2 3 N HIS C 46  ? N HIS C 46  O VAL C 118 ? O VAL C 118 
F 3 4 N VAL C 119 ? N VAL C 119 O ALA C 145 ? O ALA C 145 
G 1 2 O ASP D 101 ? O ASP D 101 N VAL D 29  ? N VAL D 29  
G 2 3 O TRP D 32  ? O TRP D 32  N ASN D 19  ? N ASN D 19  
G 3 4 O PHE D 20  ? O PHE D 20  N ALA D 4   ? N ALA D 4   
G 4 5 N VAL D 5   ? N VAL D 5   O GLY D 150 ? O GLY D 150 
H 1 2 O ALA D 89  ? O ALA D 89  N GLY D 41  ? N GLY D 41  
H 2 3 N HIS D 48  ? N HIS D 48  O THR D 116 ? O THR D 116 
H 3 4 N VAL D 119 ? N VAL D 119 O ALA D 145 ? O ALA D 145 
# 
_database_PDB_matrix.entry_id          3ECU 
_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                    3ECU 
_atom_sites.fract_transf_matrix[1][1]   0.006403 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002540 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.029826 
_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]   0.009439 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ALA A 1 1   ? 3.916   -18.315 28.023  1.00 33.50 ? 1   ALA A N   1 
ATOM   2    C CA  . ALA A 1 1   ? 2.545   -18.005 27.430  1.00 31.97 ? 1   ALA A CA  1 
ATOM   3    C C   . ALA A 1 1   ? 1.760   -16.988 28.249  1.00 30.54 ? 1   ALA A C   1 
ATOM   4    O O   . ALA A 1 1   ? 1.013   -17.346 29.178  1.00 29.07 ? 1   ALA A O   1 
ATOM   5    C CB  . ALA A 1 1   ? 1.699   -19.312 27.182  1.00 32.51 ? 1   ALA A CB  1 
ATOM   6    N N   . THR A 1 2   ? 1.926   -15.719 27.903  1.00 27.97 ? 2   THR A N   1 
ATOM   7    C CA  . THR A 1 2   ? 1.189   -14.727 28.629  1.00 25.96 ? 2   THR A CA  1 
ATOM   8    C C   . THR A 1 2   ? -0.349  -14.862 28.341  1.00 24.26 ? 2   THR A C   1 
ATOM   9    O O   . THR A 1 2   ? -0.790  -15.394 27.313  1.00 23.99 ? 2   THR A O   1 
ATOM   10   C CB  . THR A 1 2   ? 1.834   -13.355 28.467  1.00 26.19 ? 2   THR A CB  1 
ATOM   11   O OG1 . THR A 1 2   ? 1.172   -12.376 29.278  1.00 32.26 ? 2   THR A OG1 1 
ATOM   12   C CG2 . THR A 1 2   ? 1.875   -12.922 27.042  1.00 26.08 ? 2   THR A CG2 1 
ATOM   13   N N   . LYS A 1 3   ? -1.158  -14.452 29.311  1.00 21.85 ? 3   LYS A N   1 
ATOM   14   C CA  . LYS A 1 3   ? -2.584  -14.703 29.315  1.00 19.25 ? 3   LYS A CA  1 
ATOM   15   C C   . LYS A 1 3   ? -3.260  -13.408 29.796  1.00 16.72 ? 3   LYS A C   1 
ATOM   16   O O   . LYS A 1 3   ? -2.645  -12.562 30.463  1.00 16.92 ? 3   LYS A O   1 
ATOM   17   C CB  . LYS A 1 3   ? -2.926  -15.915 30.202  1.00 19.03 ? 3   LYS A CB  1 
ATOM   18   C CG  . LYS A 1 3   ? -3.273  -17.224 29.466  1.00 20.02 ? 3   LYS A CG  1 
ATOM   19   C CD  . LYS A 1 3   ? -3.927  -18.199 30.508  1.00 23.69 ? 3   LYS A CD  1 
ATOM   20   C CE  . LYS A 1 3   ? -5.111  -19.064 30.006  1.00 29.40 ? 3   LYS A CE  1 
ATOM   21   N NZ  . LYS A 1 3   ? -6.277  -19.084 30.980  1.00 28.66 ? 3   LYS A NZ  1 
ATOM   22   N N   . ALA A 1 4   ? -4.500  -13.226 29.366  1.00 13.56 ? 4   ALA A N   1 
ATOM   23   C CA  . ALA A 1 4   ? -5.265  -12.094 29.716  1.00 11.92 ? 4   ALA A CA  1 
ATOM   24   C C   . ALA A 1 4   ? -6.773  -12.488 29.730  1.00 10.58 ? 4   ALA A C   1 
ATOM   25   O O   . ALA A 1 4   ? -7.125  -13.563 29.290  1.00 11.37 ? 4   ALA A O   1 
ATOM   26   C CB  . ALA A 1 4   ? -4.942  -10.924 28.715  1.00 10.96 ? 4   ALA A CB  1 
ATOM   27   N N   . VAL A 1 5   ? -7.653  -11.640 30.284  1.00 9.46  ? 5   VAL A N   1 
ATOM   28   C CA  . VAL A 1 5   ? -9.058  -11.972 30.498  1.00 8.17  ? 5   VAL A CA  1 
ATOM   29   C C   . VAL A 1 5   ? -9.751  -10.573 30.577  1.00 9.66  ? 5   VAL A C   1 
ATOM   30   O O   . VAL A 1 5   ? -9.085  -9.633  30.972  1.00 6.17  ? 5   VAL A O   1 
ATOM   31   C CB  . VAL A 1 5   ? -9.183  -12.973 31.750  1.00 10.56 ? 5   VAL A CB  1 
ATOM   32   C CG1 . VAL A 1 5   ? -8.849  -12.314 33.037  1.00 9.42  ? 5   VAL A CG1 1 
ATOM   33   C CG2 . VAL A 1 5   ? -10.584 -13.879 31.803  1.00 7.84  ? 5   VAL A CG2 1 
ATOM   34   N N   . CYS A 1 6   ? -11.004 -10.453 30.095  1.00 8.77  ? 6   CYS A N   1 
ATOM   35   C CA  . CYS A 1 6   ? -11.821 -9.264  30.244  1.00 9.19  ? 6   CYS A CA  1 
ATOM   36   C C   . CYS A 1 6   ? -13.131 -9.821  30.722  1.00 10.35 ? 6   CYS A C   1 
ATOM   37   O O   . CYS A 1 6   ? -13.623 -10.791 30.146  1.00 9.48  ? 6   CYS A O   1 
ATOM   38   C CB  . CYS A 1 6   ? -12.068 -8.627  28.885  1.00 6.26  ? 6   CYS A CB  1 
ATOM   39   S SG  . CYS A 1 6   ? -12.627 -6.921  28.946  1.00 9.71  ? 6   CYS A SG  1 
ATOM   40   N N   . VAL A 1 7   ? -13.734 -9.166  31.728  1.00 11.64 ? 7   VAL A N   1 
ATOM   41   C CA  . VAL A 1 7   ? -15.111 -9.433  32.175  1.00 10.52 ? 7   VAL A CA  1 
ATOM   42   C C   . VAL A 1 7   ? -15.859 -8.237  31.656  1.00 10.70 ? 7   VAL A C   1 
ATOM   43   O O   . VAL A 1 7   ? -15.466 -7.069  31.921  1.00 9.22  ? 7   VAL A O   1 
ATOM   44   C CB  . VAL A 1 7   ? -15.173 -9.669  33.750  1.00 11.26 ? 7   VAL A CB  1 
ATOM   45   C CG1 . VAL A 1 7   ? -16.577 -9.842  34.230  1.00 10.33 ? 7   VAL A CG1 1 
ATOM   46   C CG2 . VAL A 1 7   ? -14.453 -10.980 34.077  1.00 9.76  ? 7   VAL A CG2 1 
ATOM   47   N N   . LEU A 1 8   ? -16.851 -8.500  30.807  1.00 9.96  ? 8   LEU A N   1 
ATOM   48   C CA  . LEU A 1 8   ? -17.543 -7.429  30.092  1.00 10.24 ? 8   LEU A CA  1 
ATOM   49   C C   . LEU A 1 8   ? -18.858 -7.100  30.785  1.00 11.15 ? 8   LEU A C   1 
ATOM   50   O O   . LEU A 1 8   ? -19.570 -8.015  31.172  1.00 11.08 ? 8   LEU A O   1 
ATOM   51   C CB  . LEU A 1 8   ? -17.909 -7.938  28.679  1.00 9.35  ? 8   LEU A CB  1 
ATOM   52   C CG  . LEU A 1 8   ? -17.299 -7.819  27.282  1.00 11.37 ? 8   LEU A CG  1 
ATOM   53   C CD1 . LEU A 1 8   ? -16.192 -6.843  27.061  1.00 4.86  ? 8   LEU A CD1 1 
ATOM   54   C CD2 . LEU A 1 8   ? -16.916 -9.174  26.762  1.00 8.18  ? 8   LEU A CD2 1 
ATOM   55   N N   . LYS A 1 9   ? -19.222 -5.818  30.975  1.00 10.09 ? 9   LYS A N   1 
ATOM   56   C CA  . LYS A 1 9   ? -20.404 -5.526  31.724  1.00 11.22 ? 9   LYS A CA  1 
ATOM   57   C C   . LYS A 1 9   ? -20.829 -4.186  31.240  1.00 11.30 ? 9   LYS A C   1 
ATOM   58   O O   . LYS A 1 9   ? -20.022 -3.474  30.645  1.00 8.83  ? 9   LYS A O   1 
ATOM   59   C CB  . LYS A 1 9   ? -20.121 -5.434  33.229  1.00 12.17 ? 9   LYS A CB  1 
ATOM   60   C CG  . LYS A 1 9   ? -19.821 -6.746  33.889  1.00 18.00 ? 9   LYS A CG  1 
ATOM   61   C CD  . LYS A 1 9   ? -19.892 -6.626  35.419  1.00 25.42 ? 9   LYS A CD  1 
ATOM   62   C CE  . LYS A 1 9   ? -19.766 -8.041  36.084  1.00 25.40 ? 9   LYS A CE  1 
ATOM   63   N NZ  . LYS A 1 9   ? -20.927 -8.944  35.742  1.00 29.57 ? 9   LYS A NZ  1 
ATOM   64   N N   . GLY A 1 10  ? -22.087 -3.853  31.494  1.00 10.77 ? 10  GLY A N   1 
ATOM   65   C CA  . GLY A 1 10  ? -22.628 -2.565  31.071  1.00 15.30 ? 10  GLY A CA  1 
ATOM   66   C C   . GLY A 1 10  ? -23.877 -2.257  31.840  1.00 16.12 ? 10  GLY A C   1 
ATOM   67   O O   . GLY A 1 10  ? -24.180 -2.942  32.774  1.00 17.74 ? 10  GLY A O   1 
ATOM   68   N N   . ASP A 1 11  ? -24.555 -1.170  31.485  1.00 17.63 ? 11  ASP A N   1 
ATOM   69   C CA  . ASP A 1 11  ? -25.807 -0.791  32.069  1.00 17.99 ? 11  ASP A CA  1 
ATOM   70   C C   . ASP A 1 11  ? -26.930 -1.782  31.841  1.00 18.03 ? 11  ASP A C   1 
ATOM   71   O O   . ASP A 1 11  ? -28.031 -1.575  32.344  1.00 19.36 ? 11  ASP A O   1 
ATOM   72   C CB  . ASP A 1 11  ? -26.279 0.499   31.414  1.00 19.21 ? 11  ASP A CB  1 
ATOM   73   C CG  . ASP A 1 11  ? -25.295 1.604   31.547  1.00 21.14 ? 11  ASP A CG  1 
ATOM   74   O OD1 . ASP A 1 11  ? -24.592 1.647   32.582  1.00 21.99 ? 11  ASP A OD1 1 
ATOM   75   O OD2 . ASP A 1 11  ? -25.214 2.391   30.595  1.00 25.08 ? 11  ASP A OD2 1 
ATOM   76   N N   . GLY A 1 12  ? -26.690 -2.827  31.071  1.00 17.90 ? 12  GLY A N   1 
ATOM   77   C CA  . GLY A 1 12  ? -27.764 -3.666  30.543  1.00 15.01 ? 12  GLY A CA  1 
ATOM   78   C C   . GLY A 1 12  ? -27.507 -5.115  30.893  1.00 14.15 ? 12  GLY A C   1 
ATOM   79   O O   . GLY A 1 12  ? -26.828 -5.398  31.877  1.00 13.03 ? 12  GLY A O   1 
ATOM   80   N N   . PRO A 1 13  ? -28.165 -6.032  30.186  1.00 12.24 ? 13  PRO A N   1 
ATOM   81   C CA  . PRO A 1 13  ? -28.006 -7.469  30.471  1.00 13.61 ? 13  PRO A CA  1 
ATOM   82   C C   . PRO A 1 13  ? -26.818 -8.193  29.857  1.00 14.31 ? 13  PRO A C   1 
ATOM   83   O O   . PRO A 1 13  ? -26.609 -9.419  30.063  1.00 15.23 ? 13  PRO A O   1 
ATOM   84   C CB  . PRO A 1 13  ? -29.272 -8.068  29.874  1.00 12.46 ? 13  PRO A CB  1 
ATOM   85   C CG  . PRO A 1 13  ? -29.640 -7.182  28.800  1.00 9.89  ? 13  PRO A CG  1 
ATOM   86   C CD  . PRO A 1 13  ? -29.204 -5.784  29.171  1.00 11.65 ? 13  PRO A CD  1 
ATOM   87   N N   . VAL A 1 14  ? -26.015 -7.464  29.113  1.00 16.31 ? 14  VAL A N   1 
ATOM   88   C CA  . VAL A 1 14  ? -24.923 -8.094  28.385  1.00 16.01 ? 14  VAL A CA  1 
ATOM   89   C C   . VAL A 1 14  ? -23.790 -8.418  29.350  1.00 16.09 ? 14  VAL A C   1 
ATOM   90   O O   . VAL A 1 14  ? -23.166 -7.499  29.858  1.00 14.98 ? 14  VAL A O   1 
ATOM   91   C CB  . VAL A 1 14  ? -24.357 -7.110  27.282  1.00 15.60 ? 14  VAL A CB  1 
ATOM   92   C CG1 . VAL A 1 14  ? -23.217 -7.722  26.588  1.00 14.75 ? 14  VAL A CG1 1 
ATOM   93   C CG2 . VAL A 1 14  ? -25.410 -6.720  26.279  1.00 15.27 ? 14  VAL A CG2 1 
ATOM   94   N N   . GLN A 1 15  ? -23.479 -9.700  29.578  1.00 16.70 ? 15  GLN A N   1 
ATOM   95   C CA  . GLN A 1 15  ? -22.305 -10.015 30.359  1.00 17.05 ? 15  GLN A CA  1 
ATOM   96   C C   . GLN A 1 15  ? -21.459 -11.090 29.703  1.00 16.60 ? 15  GLN A C   1 
ATOM   97   O O   . GLN A 1 15  ? -21.984 -12.014 29.138  1.00 15.66 ? 15  GLN A O   1 
ATOM   98   C CB  . GLN A 1 15  ? -22.674 -10.505 31.770  1.00 19.67 ? 15  GLN A CB  1 
ATOM   99   C CG  . GLN A 1 15  ? -23.761 -9.725  32.568  1.00 23.59 ? 15  GLN A CG  1 
ATOM   100  C CD  . GLN A 1 15  ? -24.579 -10.687 33.416  1.00 28.99 ? 15  GLN A CD  1 
ATOM   101  O OE1 . GLN A 1 15  ? -24.058 -11.340 34.310  1.00 28.14 ? 15  GLN A OE1 1 
ATOM   102  N NE2 . GLN A 1 15  ? -25.862 -10.798 33.107  1.00 35.16 ? 15  GLN A NE2 1 
ATOM   103  N N   . GLY A 1 16  ? -20.138 -10.974 29.841  1.00 15.23 ? 16  GLY A N   1 
ATOM   104  C CA  . GLY A 1 16  ? -19.251 -11.875 29.152  1.00 13.12 ? 16  GLY A CA  1 
ATOM   105  C C   . GLY A 1 16  ? -17.895 -12.056 29.797  1.00 13.16 ? 16  GLY A C   1 
ATOM   106  O O   . GLY A 1 16  ? -17.409 -11.201 30.531  1.00 10.64 ? 16  GLY A O   1 
ATOM   107  N N   . ILE A 1 17  ? -17.309 -13.227 29.546  1.00 13.59 ? 17  ILE A N   1 
ATOM   108  C CA  . ILE A 1 17  ? -15.906 -13.463 29.786  1.00 14.58 ? 17  ILE A CA  1 
ATOM   109  C C   . ILE A 1 17  ? -15.201 -13.840 28.510  1.00 14.35 ? 17  ILE A C   1 
ATOM   110  O O   . ILE A 1 17  ? -15.501 -14.874 27.841  1.00 12.86 ? 17  ILE A O   1 
ATOM   111  C CB  . ILE A 1 17  ? -15.665 -14.507 30.877  1.00 16.02 ? 17  ILE A CB  1 
ATOM   112  C CG1 . ILE A 1 17  ? -16.429 -14.060 32.115  1.00 16.74 ? 17  ILE A CG1 1 
ATOM   113  C CG2 . ILE A 1 17  ? -14.202 -14.503 31.287  1.00 13.91 ? 17  ILE A CG2 1 
ATOM   114  C CD1 . ILE A 1 17  ? -16.425 -15.148 33.237  1.00 16.40 ? 17  ILE A CD1 1 
ATOM   115  N N   . ILE A 1 18  ? -14.255 -12.974 28.189  1.00 12.51 ? 18  ILE A N   1 
ATOM   116  C CA  . ILE A 1 18  ? -13.364 -13.167 27.055  1.00 13.56 ? 18  ILE A CA  1 
ATOM   117  C C   . ILE A 1 18  ? -11.922 -13.383 27.501  1.00 13.32 ? 18  ILE A C   1 
ATOM   118  O O   . ILE A 1 18  ? -11.472 -12.721 28.402  1.00 11.66 ? 18  ILE A O   1 
ATOM   119  C CB  . ILE A 1 18  ? -13.474 -12.057 26.027  1.00 14.21 ? 18  ILE A CB  1 
ATOM   120  C CG1 . ILE A 1 18  ? -14.899 -12.052 25.411  1.00 14.03 ? 18  ILE A CG1 1 
ATOM   121  C CG2 . ILE A 1 18  ? -12.482 -12.286 24.918  1.00 12.59 ? 18  ILE A CG2 1 
ATOM   122  C CD1 . ILE A 1 18  ? -15.233 -13.244 24.583  1.00 14.90 ? 18  ILE A CD1 1 
ATOM   123  N N   . ASN A 1 19  ? -11.265 -14.389 26.905  1.00 12.91 ? 19  ASN A N   1 
ATOM   124  C CA  . ASN A 1 19  ? -9.971  -14.855 27.333  1.00 12.64 ? 19  ASN A CA  1 
ATOM   125  C C   . ASN A 1 19  ? -9.050  -14.633 26.214  1.00 10.90 ? 19  ASN A C   1 
ATOM   126  O O   . ASN A 1 19  ? -9.476  -14.705 25.083  1.00 12.20 ? 19  ASN A O   1 
ATOM   127  C CB  . ASN A 1 19  ? -9.968  -16.378 27.619  1.00 13.59 ? 19  ASN A CB  1 
ATOM   128  C CG  . ASN A 1 19  ? -10.722 -16.747 28.872  1.00 13.29 ? 19  ASN A CG  1 
ATOM   129  O OD1 . ASN A 1 19  ? -11.857 -17.272 28.812  1.00 19.44 ? 19  ASN A OD1 1 
ATOM   130  N ND2 . ASN A 1 19  ? -10.126 -16.477 30.006  1.00 16.58 ? 19  ASN A ND2 1 
ATOM   131  N N   . PHE A 1 20  ? -7.798  -14.318 26.531  1.00 10.59 ? 20  PHE A N   1 
ATOM   132  C CA  . PHE A 1 20  ? -6.691  -14.171 25.550  1.00 11.59 ? 20  PHE A CA  1 
ATOM   133  C C   . PHE A 1 20  ? -5.499  -15.038 25.839  1.00 11.12 ? 20  PHE A C   1 
ATOM   134  O O   . PHE A 1 20  ? -5.179  -15.319 26.984  1.00 13.07 ? 20  PHE A O   1 
ATOM   135  C CB  . PHE A 1 20  ? -6.239  -12.715 25.420  1.00 8.97  ? 20  PHE A CB  1 
ATOM   136  C CG  . PHE A 1 20  ? -7.362  -11.771 25.274  1.00 9.28  ? 20  PHE A CG  1 
ATOM   137  C CD1 . PHE A 1 20  ? -8.131  -11.410 26.377  1.00 9.56  ? 20  PHE A CD1 1 
ATOM   138  C CD2 . PHE A 1 20  ? -7.609  -11.184 24.048  1.00 10.11 ? 20  PHE A CD2 1 
ATOM   139  C CE1 . PHE A 1 20  ? -9.214  -10.437 26.260  1.00 5.16  ? 20  PHE A CE1 1 
ATOM   140  C CE2 . PHE A 1 20  ? -8.646  -10.238 23.904  1.00 10.04 ? 20  PHE A CE2 1 
ATOM   141  C CZ  . PHE A 1 20  ? -9.463  -9.931  24.964  1.00 6.78  ? 20  PHE A CZ  1 
ATOM   142  N N   . GLU A 1 21  ? -4.883  -15.532 24.788  1.00 13.59 ? 21  GLU A N   1 
ATOM   143  C CA  . GLU A 1 21  ? -3.706  -16.383 24.934  1.00 15.52 ? 21  GLU A CA  1 
ATOM   144  C C   . GLU A 1 21  ? -2.814  -16.204 23.750  1.00 16.34 ? 21  GLU A C   1 
ATOM   145  O O   . GLU A 1 21  ? -3.271  -16.273 22.593  1.00 13.78 ? 21  GLU A O   1 
ATOM   146  C CB  . GLU A 1 21  ? -4.052  -17.867 25.024  1.00 16.62 ? 21  GLU A CB  1 
ATOM   147  C CG  . GLU A 1 21  ? -2.758  -18.692 25.162  1.00 19.43 ? 21  GLU A CG  1 
ATOM   148  C CD  . GLU A 1 21  ? -2.995  -20.129 25.598  1.00 27.45 ? 21  GLU A CD  1 
ATOM   149  O OE1 . GLU A 1 21  ? -3.600  -20.920 24.802  1.00 25.20 ? 21  GLU A OE1 1 
ATOM   150  O OE2 . GLU A 1 21  ? -2.537  -20.443 26.745  1.00 33.00 ? 21  GLU A OE2 1 
ATOM   151  N N   . GLN A 1 22  ? -1.529  -16.005 24.061  1.00 18.67 ? 22  GLN A N   1 
ATOM   152  C CA  . GLN A 1 22  ? -0.499  -15.791 23.064  1.00 20.14 ? 22  GLN A CA  1 
ATOM   153  C C   . GLN A 1 22  ? 0.645   -16.567 23.570  1.00 21.83 ? 22  GLN A C   1 
ATOM   154  O O   . GLN A 1 22  ? 1.300   -16.136 24.473  1.00 23.47 ? 22  GLN A O   1 
ATOM   155  C CB  . GLN A 1 22  ? -0.120  -14.310 22.974  1.00 19.37 ? 22  GLN A CB  1 
ATOM   156  C CG  . GLN A 1 22  ? 0.617   -13.922 21.705  1.00 17.18 ? 22  GLN A CG  1 
ATOM   157  C CD  . GLN A 1 22  ? 0.882   -12.445 21.663  1.00 16.25 ? 22  GLN A CD  1 
ATOM   158  O OE1 . GLN A 1 22  ? 0.793   -11.764 22.686  1.00 19.33 ? 22  GLN A OE1 1 
ATOM   159  N NE2 . GLN A 1 22  ? 1.195   -11.926 20.497  1.00 8.86  ? 22  GLN A NE2 1 
ATOM   160  N N   . LYS A 1 23  ? 0.865   -17.758 23.042  1.00 24.85 ? 23  LYS A N   1 
ATOM   161  C CA  . LYS A 1 23  ? 1.962   -18.579 23.550  1.00 28.43 ? 23  LYS A CA  1 
ATOM   162  C C   . LYS A 1 23  ? 3.371   -18.066 23.142  1.00 29.97 ? 23  LYS A C   1 
ATOM   163  O O   . LYS A 1 23  ? 4.362   -18.298 23.888  1.00 30.41 ? 23  LYS A O   1 
ATOM   164  C CB  . LYS A 1 23  ? 1.775   -20.057 23.188  1.00 28.39 ? 23  LYS A CB  1 
ATOM   165  C CG  . LYS A 1 23  ? 0.374   -20.504 22.793  1.00 28.81 ? 23  LYS A CG  1 
ATOM   166  C CD  . LYS A 1 23  ? 0.400   -21.998 22.269  1.00 31.79 ? 23  LYS A CD  1 
ATOM   167  C CE  . LYS A 1 23  ? 1.381   -22.209 21.065  1.00 36.15 ? 23  LYS A CE  1 
ATOM   168  N NZ  . LYS A 1 23  ? 0.810   -23.039 19.898  1.00 38.01 ? 23  LYS A NZ  1 
ATOM   169  N N   . GLU A 1 24  ? 3.463   -17.354 22.002  1.00 31.43 ? 24  GLU A N   1 
ATOM   170  C CA  . GLU A 1 24  ? 4.721   -16.731 21.548  1.00 33.15 ? 24  GLU A CA  1 
ATOM   171  C C   . GLU A 1 24  ? 4.617   -15.213 21.339  1.00 33.74 ? 24  GLU A C   1 
ATOM   172  O O   . GLU A 1 24  ? 3.622   -14.713 20.805  1.00 33.30 ? 24  GLU A O   1 
ATOM   173  C CB  . GLU A 1 24  ? 5.230   -17.367 20.247  1.00 33.45 ? 24  GLU A CB  1 
ATOM   174  C CG  . GLU A 1 24  ? 5.080   -18.899 20.116  1.00 36.06 ? 24  GLU A CG  1 
ATOM   175  C CD  . GLU A 1 24  ? 3.880   -19.328 19.242  1.00 39.69 ? 24  GLU A CD  1 
ATOM   176  O OE1 . GLU A 1 24  ? 3.158   -18.455 18.684  1.00 39.52 ? 24  GLU A OE1 1 
ATOM   177  O OE2 . GLU A 1 24  ? 3.654   -20.557 19.109  1.00 39.44 ? 24  GLU A OE2 1 
ATOM   178  N N   . SER A 1 25  ? 5.667   -14.484 21.708  1.00 34.91 ? 25  SER A N   1 
ATOM   179  C CA  . SER A 1 25  ? 5.650   -12.999 21.623  1.00 36.47 ? 25  SER A CA  1 
ATOM   180  C C   . SER A 1 25  ? 5.166   -12.443 20.268  1.00 36.94 ? 25  SER A C   1 
ATOM   181  O O   . SER A 1 25  ? 4.622   -11.342 20.175  1.00 36.97 ? 25  SER A O   1 
ATOM   182  C CB  . SER A 1 25  ? 7.042   -12.396 21.984  1.00 37.04 ? 25  SER A CB  1 
ATOM   183  O OG  . SER A 1 25  ? 7.866   -12.194 20.834  1.00 37.85 ? 25  SER A OG  1 
ATOM   184  N N   . ASN A 1 26  ? 5.372   -13.231 19.218  1.00 37.74 ? 26  ASN A N   1 
ATOM   185  C CA  . ASN A 1 26  ? 5.078   -12.826 17.850  1.00 37.31 ? 26  ASN A CA  1 
ATOM   186  C C   . ASN A 1 26  ? 3.913   -13.670 17.382  1.00 36.35 ? 26  ASN A C   1 
ATOM   187  O O   . ASN A 1 26  ? 3.380   -13.464 16.292  1.00 35.95 ? 26  ASN A O   1 
ATOM   188  C CB  . ASN A 1 26  ? 6.286   -13.133 16.958  1.00 38.45 ? 26  ASN A CB  1 
ATOM   189  C CG  . ASN A 1 26  ? 6.586   -14.643 16.873  1.00 40.66 ? 26  ASN A CG  1 
ATOM   190  O OD1 . ASN A 1 26  ? 6.626   -15.343 17.897  1.00 42.66 ? 26  ASN A OD1 1 
ATOM   191  N ND2 . ASN A 1 26  ? 6.805   -15.143 15.647  1.00 42.61 ? 26  ASN A ND2 1 
ATOM   192  N N   . GLY A 1 27  ? 3.537   -14.648 18.205  1.00 34.67 ? 27  GLY A N   1 
ATOM   193  C CA  . GLY A 1 27  ? 2.451   -15.540 17.851  1.00 32.88 ? 27  GLY A CA  1 
ATOM   194  C C   . GLY A 1 27  ? 1.128   -14.827 17.614  1.00 31.30 ? 27  GLY A C   1 
ATOM   195  O O   . GLY A 1 27  ? 0.978   -13.616 17.853  1.00 31.97 ? 27  GLY A O   1 
ATOM   196  N N   . PRO A 1 28  ? 0.159   -15.580 17.126  1.00 30.30 ? 28  PRO A N   1 
ATOM   197  C CA  . PRO A 1 28  ? -1.188  -15.096 17.022  1.00 28.45 ? 28  PRO A CA  1 
ATOM   198  C C   . PRO A 1 28  ? -1.848  -15.071 18.435  1.00 27.10 ? 28  PRO A C   1 
ATOM   199  O O   . PRO A 1 28  ? -1.489  -15.862 19.318  1.00 26.50 ? 28  PRO A O   1 
ATOM   200  C CB  . PRO A 1 28  ? -1.858  -16.112 16.084  1.00 29.04 ? 28  PRO A CB  1 
ATOM   201  C CG  . PRO A 1 28  ? -0.701  -17.025 15.554  1.00 30.84 ? 28  PRO A CG  1 
ATOM   202  C CD  . PRO A 1 28  ? 0.302   -16.968 16.658  1.00 30.18 ? 28  PRO A CD  1 
ATOM   203  N N   . VAL A 1 29  ? -2.783  -14.136 18.643  1.00 25.04 ? 29  VAL A N   1 
ATOM   204  C CA  . VAL A 1 29  ? -3.545  -14.052 19.891  1.00 21.69 ? 29  VAL A CA  1 
ATOM   205  C C   . VAL A 1 29  ? -4.851  -14.816 19.716  1.00 21.39 ? 29  VAL A C   1 
ATOM   206  O O   . VAL A 1 29  ? -5.675  -14.475 18.876  1.00 20.87 ? 29  VAL A O   1 
ATOM   207  C CB  . VAL A 1 29  ? -3.834  -12.607 20.293  1.00 21.65 ? 29  VAL A CB  1 
ATOM   208  C CG1 . VAL A 1 29  ? -4.450  -12.584 21.681  1.00 19.94 ? 29  VAL A CG1 1 
ATOM   209  C CG2 . VAL A 1 29  ? -2.568  -11.795 20.214  1.00 16.66 ? 29  VAL A CG2 1 
ATOM   210  N N   . LYS A 1 30  ? -5.019  -15.844 20.521  1.00 20.29 ? 30  LYS A N   1 
ATOM   211  C CA  . LYS A 1 30  ? -6.211  -16.678 20.489  1.00 19.93 ? 30  LYS A CA  1 
ATOM   212  C C   . LYS A 1 30  ? -7.181  -16.066 21.525  1.00 18.79 ? 30  LYS A C   1 
ATOM   213  O O   . LYS A 1 30  ? -6.812  -15.775 22.642  1.00 18.31 ? 30  LYS A O   1 
ATOM   214  C CB  . LYS A 1 30  ? -5.777  -18.113 20.793  1.00 20.92 ? 30  LYS A CB  1 
ATOM   215  C CG  . LYS A 1 30  ? -6.825  -19.253 20.868  1.00 24.81 ? 30  LYS A CG  1 
ATOM   216  C CD  . LYS A 1 30  ? -7.302  -19.891 19.498  1.00 26.39 ? 30  LYS A CD  1 
ATOM   217  C CE  . LYS A 1 30  ? -8.831  -19.552 19.219  1.00 26.01 ? 30  LYS A CE  1 
ATOM   218  N NZ  . LYS A 1 30  ? -9.732  -19.855 20.361  1.00 16.79 ? 30  LYS A NZ  1 
ATOM   219  N N   . VAL A 1 31  ? -8.410  -15.803 21.113  1.00 17.66 ? 31  VAL A N   1 
ATOM   220  C CA  . VAL A 1 31  ? -9.398  -15.163 21.993  1.00 15.34 ? 31  VAL A CA  1 
ATOM   221  C C   . VAL A 1 31  ? -10.704 -15.898 22.033  1.00 14.94 ? 31  VAL A C   1 
ATOM   222  O O   . VAL A 1 31  ? -11.388 -15.947 21.054  1.00 14.30 ? 31  VAL A O   1 
ATOM   223  C CB  . VAL A 1 31  ? -9.625  -13.665 21.627  1.00 15.29 ? 31  VAL A CB  1 
ATOM   224  C CG1 . VAL A 1 31  ? -8.933  -13.301 20.386  1.00 13.41 ? 31  VAL A CG1 1 
ATOM   225  C CG2 . VAL A 1 31  ? -11.059 -13.299 21.614  1.00 6.15  ? 31  VAL A CG2 1 
ATOM   226  N N   . TRP A 1 32  ? -11.033 -16.470 23.188  1.00 17.39 ? 32  TRP A N   1 
ATOM   227  C CA  . TRP A 1 32  ? -12.227 -17.302 23.322  1.00 18.30 ? 32  TRP A CA  1 
ATOM   228  C C   . TRP A 1 32  ? -13.001 -16.948 24.593  1.00 18.36 ? 32  TRP A C   1 
ATOM   229  O O   . TRP A 1 32  ? -12.429 -16.408 25.526  1.00 19.45 ? 32  TRP A O   1 
ATOM   230  C CB  . TRP A 1 32  ? -11.851 -18.808 23.283  1.00 17.57 ? 32  TRP A CB  1 
ATOM   231  C CG  . TRP A 1 32  ? -11.202 -19.292 24.524  1.00 16.97 ? 32  TRP A CG  1 
ATOM   232  C CD1 . TRP A 1 32  ? -11.804 -19.955 25.568  1.00 15.04 ? 32  TRP A CD1 1 
ATOM   233  C CD2 . TRP A 1 32  ? -9.843  -19.094 24.904  1.00 15.20 ? 32  TRP A CD2 1 
ATOM   234  N NE1 . TRP A 1 32  ? -10.892 -20.184 26.552  1.00 12.87 ? 32  TRP A NE1 1 
ATOM   235  C CE2 . TRP A 1 32  ? -9.682  -19.659 26.163  1.00 13.33 ? 32  TRP A CE2 1 
ATOM   236  C CE3 . TRP A 1 32  ? -8.741  -18.450 24.300  1.00 13.34 ? 32  TRP A CE3 1 
ATOM   237  C CZ2 . TRP A 1 32  ? -8.463  -19.640 26.828  1.00 19.17 ? 32  TRP A CZ2 1 
ATOM   238  C CZ3 . TRP A 1 32  ? -7.542  -18.434 24.942  1.00 16.88 ? 32  TRP A CZ3 1 
ATOM   239  C CH2 . TRP A 1 32  ? -7.394  -19.013 26.210  1.00 17.11 ? 32  TRP A CH2 1 
ATOM   240  N N   . GLY A 1 33  ? -14.309 -17.213 24.588  1.00 19.16 ? 33  GLY A N   1 
ATOM   241  C CA  . GLY A 1 33  ? -15.177 -17.071 25.761  1.00 18.91 ? 33  GLY A CA  1 
ATOM   242  C C   . GLY A 1 33  ? -16.643 -17.047 25.350  1.00 18.75 ? 33  GLY A C   1 
ATOM   243  O O   . GLY A 1 33  ? -16.983 -17.548 24.295  1.00 18.57 ? 33  GLY A O   1 
ATOM   244  N N   . SER A 1 34  ? -17.497 -16.407 26.168  1.00 19.37 ? 34  SER A N   1 
ATOM   245  C CA  . SER A 1 34  ? -18.938 -16.229 25.915  1.00 18.29 ? 34  SER A CA  1 
ATOM   246  C C   . SER A 1 34  ? -19.467 -14.841 26.285  1.00 18.00 ? 34  SER A C   1 
ATOM   247  O O   . SER A 1 34  ? -18.912 -14.181 27.152  1.00 18.32 ? 34  SER A O   1 
ATOM   248  C CB  . SER A 1 34  ? -19.728 -17.246 26.707  1.00 18.57 ? 34  SER A CB  1 
ATOM   249  O OG  . SER A 1 34  ? -21.039 -17.251 26.176  1.00 22.67 ? 34  SER A OG  1 
ATOM   250  N N   . ILE A 1 35  ? -20.545 -14.428 25.628  1.00 16.08 ? 35  ILE A N   1 
ATOM   251  C CA  . ILE A 1 35  ? -21.282 -13.233 25.952  1.00 18.49 ? 35  ILE A CA  1 
ATOM   252  C C   . ILE A 1 35  ? -22.761 -13.586 25.807  1.00 19.35 ? 35  ILE A C   1 
ATOM   253  O O   . ILE A 1 35  ? -23.177 -14.164 24.795  1.00 18.91 ? 35  ILE A O   1 
ATOM   254  C CB  . ILE A 1 35  ? -20.961 -12.043 25.020  1.00 17.61 ? 35  ILE A CB  1 
ATOM   255  C CG1 . ILE A 1 35  ? -19.461 -12.029 24.610  1.00 20.95 ? 35  ILE A CG1 1 
ATOM   256  C CG2 . ILE A 1 35  ? -21.470 -10.699 25.629  1.00 14.84 ? 35  ILE A CG2 1 
ATOM   257  C CD1 . ILE A 1 35  ? -19.003 -10.736 23.926  1.00 17.13 ? 35  ILE A CD1 1 
ATOM   258  N N   . LYS A 1 36  ? -23.541 -13.196 26.822  1.00 20.90 ? 36  LYS A N   1 
ATOM   259  C CA  . LYS A 1 36  ? -24.987 -13.372 26.858  1.00 20.63 ? 36  LYS A CA  1 
ATOM   260  C C   . LYS A 1 36  ? -25.734 -12.031 26.913  1.00 20.65 ? 36  LYS A C   1 
ATOM   261  O O   . LYS A 1 36  ? -25.120 -10.950 26.961  1.00 19.42 ? 36  LYS A O   1 
ATOM   262  C CB  . LYS A 1 36  ? -25.326 -14.330 28.002  1.00 22.80 ? 36  LYS A CB  1 
ATOM   263  C CG  . LYS A 1 36  ? -25.318 -13.728 29.398  1.00 24.28 ? 36  LYS A CG  1 
ATOM   264  C CD  . LYS A 1 36  ? -25.413 -14.781 30.451  1.00 30.45 ? 36  LYS A CD  1 
ATOM   265  C CE  . LYS A 1 36  ? -25.939 -14.174 31.740  1.00 34.74 ? 36  LYS A CE  1 
ATOM   266  N NZ  . LYS A 1 36  ? -25.541 -14.986 32.953  1.00 37.43 ? 36  LYS A NZ  1 
ATOM   267  N N   . GLY A 1 37  ? -27.053 -12.042 26.808  1.00 20.40 ? 37  GLY A N   1 
ATOM   268  C CA  . GLY A 1 37  ? -27.776 -10.746 26.841  1.00 18.51 ? 37  GLY A CA  1 
ATOM   269  C C   . GLY A 1 37  ? -27.796 -9.912  25.576  1.00 18.42 ? 37  GLY A C   1 
ATOM   270  O O   . GLY A 1 37  ? -28.133 -8.717  25.575  1.00 16.24 ? 37  GLY A O   1 
ATOM   271  N N   . LEU A 1 38  ? -27.457 -10.578 24.479  1.00 19.35 ? 38  LEU A N   1 
ATOM   272  C CA  . LEU A 1 38  ? -27.343 -9.959  23.187  1.00 20.64 ? 38  LEU A CA  1 
ATOM   273  C C   . LEU A 1 38  ? -28.565 -10.225 22.239  1.00 21.23 ? 38  LEU A C   1 
ATOM   274  O O   . LEU A 1 38  ? -29.116 -11.332 22.226  1.00 21.37 ? 38  LEU A O   1 
ATOM   275  C CB  . LEU A 1 38  ? -26.029 -10.521 22.589  1.00 20.43 ? 38  LEU A CB  1 
ATOM   276  C CG  . LEU A 1 38  ? -24.711 -9.740  22.414  1.00 19.78 ? 38  LEU A CG  1 
ATOM   277  C CD1 . LEU A 1 38  ? -24.601 -8.250  22.833  1.00 7.93  ? 38  LEU A CD1 1 
ATOM   278  C CD2 . LEU A 1 38  ? -23.510 -10.575 22.803  1.00 18.02 ? 38  LEU A CD2 1 
ATOM   279  N N   . THR A 1 39  ? -28.959 -9.226  21.437  1.00 22.04 ? 39  THR A N   1 
ATOM   280  C CA  . THR A 1 39  ? -29.953 -9.488  20.380  1.00 24.56 ? 39  THR A CA  1 
ATOM   281  C C   . THR A 1 39  ? -29.346 -10.473 19.373  1.00 25.08 ? 39  THR A C   1 
ATOM   282  O O   . THR A 1 39  ? -28.138 -10.448 19.110  1.00 26.90 ? 39  THR A O   1 
ATOM   283  C CB  . THR A 1 39  ? -30.458 -8.222  19.638  1.00 23.79 ? 39  THR A CB  1 
ATOM   284  O OG1 . THR A 1 39  ? -29.413 -7.673  18.840  1.00 28.16 ? 39  THR A OG1 1 
ATOM   285  C CG2 . THR A 1 39  ? -30.779 -7.189  20.569  1.00 25.38 ? 39  THR A CG2 1 
ATOM   286  N N   . GLU A 1 40  ? -30.167 -11.352 18.825  1.00 25.74 ? 40  GLU A N   1 
ATOM   287  C CA  . GLU A 1 40  ? -29.694 -12.259 17.786  1.00 24.93 ? 40  GLU A CA  1 
ATOM   288  C C   . GLU A 1 40  ? -28.938 -11.540 16.716  1.00 23.88 ? 40  GLU A C   1 
ATOM   289  O O   . GLU A 1 40  ? -29.293 -10.431 16.302  1.00 23.34 ? 40  GLU A O   1 
ATOM   290  C CB  . GLU A 1 40  ? -30.849 -12.946 17.109  1.00 25.77 ? 40  GLU A CB  1 
ATOM   291  C CG  . GLU A 1 40  ? -30.422 -14.255 16.544  1.00 29.13 ? 40  GLU A CG  1 
ATOM   292  C CD  . GLU A 1 40  ? -31.573 -15.079 15.984  1.00 33.14 ? 40  GLU A CD  1 
ATOM   293  O OE1 . GLU A 1 40  ? -32.755 -14.689 16.164  1.00 32.65 ? 40  GLU A OE1 1 
ATOM   294  O OE2 . GLU A 1 40  ? -31.263 -16.118 15.373  1.00 33.57 ? 40  GLU A OE2 1 
ATOM   295  N N   . GLY A 1 41  ? -27.885 -12.170 16.246  1.00 22.42 ? 41  GLY A N   1 
ATOM   296  C CA  . GLY A 1 41  ? -27.130 -11.531 15.193  1.00 22.27 ? 41  GLY A CA  1 
ATOM   297  C C   . GLY A 1 41  ? -25.710 -11.147 15.574  1.00 20.96 ? 41  GLY A C   1 
ATOM   298  O O   . GLY A 1 41  ? -25.201 -11.507 16.620  1.00 21.02 ? 41  GLY A O   1 
ATOM   299  N N   . LEU A 1 42  ? -25.107 -10.381 14.686  1.00 20.53 ? 42  LEU A N   1 
ATOM   300  C CA  . LEU A 1 42  ? -23.753 -9.908  14.775  1.00 19.52 ? 42  LEU A CA  1 
ATOM   301  C C   . LEU A 1 42  ? -23.607 -8.590  15.565  1.00 18.47 ? 42  LEU A C   1 
ATOM   302  O O   . LEU A 1 42  ? -24.403 -7.689  15.385  1.00 17.64 ? 42  LEU A O   1 
ATOM   303  C CB  . LEU A 1 42  ? -23.351 -9.597  13.334  1.00 20.61 ? 42  LEU A CB  1 
ATOM   304  C CG  . LEU A 1 42  ? -22.665 -10.551 12.375  1.00 21.79 ? 42  LEU A CG  1 
ATOM   305  C CD1 . LEU A 1 42  ? -22.697 -12.023 12.719  1.00 25.03 ? 42  LEU A CD1 1 
ATOM   306  C CD2 . LEU A 1 42  ? -23.425 -10.239 11.075  1.00 25.57 ? 42  LEU A CD2 1 
ATOM   307  N N   . HIS A 1 43  ? -22.557 -8.469  16.392  1.00 16.04 ? 43  HIS A N   1 
ATOM   308  C CA  . HIS A 1 43  ? -22.278 -7.187  17.096  1.00 14.33 ? 43  HIS A CA  1 
ATOM   309  C C   . HIS A 1 43  ? -20.813 -6.822  16.972  1.00 12.68 ? 43  HIS A C   1 
ATOM   310  O O   . HIS A 1 43  ? -19.975 -7.688  17.031  1.00 10.52 ? 43  HIS A O   1 
ATOM   311  C CB  . HIS A 1 43  ? -22.588 -7.410  18.594  1.00 14.10 ? 43  HIS A CB  1 
ATOM   312  C CG  . HIS A 1 43  ? -24.020 -7.694  18.863  1.00 11.39 ? 43  HIS A CG  1 
ATOM   313  N ND1 . HIS A 1 43  ? -24.934 -6.689  19.146  1.00 7.92  ? 43  HIS A ND1 1 
ATOM   314  C CD2 . HIS A 1 43  ? -24.702 -8.863  18.878  1.00 2.88  ? 43  HIS A CD2 1 
ATOM   315  C CE1 . HIS A 1 43  ? -26.126 -7.241  19.308  1.00 9.11  ? 43  HIS A CE1 1 
ATOM   316  N NE2 . HIS A 1 43  ? -26.009 -8.556  19.145  1.00 8.41  ? 43  HIS A NE2 1 
ATOM   317  N N   . GLY A 1 44  ? -20.473 -5.560  16.916  1.00 10.16 ? 44  GLY A N   1 
ATOM   318  C CA  . GLY A 1 44  ? -19.047 -5.262  16.713  1.00 9.16  ? 44  GLY A CA  1 
ATOM   319  C C   . GLY A 1 44  ? -18.309 -5.521  18.018  1.00 9.03  ? 44  GLY A C   1 
ATOM   320  O O   . GLY A 1 44  ? -18.883 -5.323  19.063  1.00 10.16 ? 44  GLY A O   1 
ATOM   321  N N   . PHE A 1 45  ? -17.049 -5.977  17.949  1.00 8.32  ? 45  PHE A N   1 
ATOM   322  C CA  . PHE A 1 45  ? -16.266 -6.521  19.052  1.00 8.27  ? 45  PHE A CA  1 
ATOM   323  C C   . PHE A 1 45  ? -14.981 -5.712  18.866  1.00 8.83  ? 45  PHE A C   1 
ATOM   324  O O   . PHE A 1 45  ? -14.333 -5.860  17.847  1.00 7.90  ? 45  PHE A O   1 
ATOM   325  C CB  . PHE A 1 45  ? -16.129 -8.033  18.745  1.00 7.99  ? 45  PHE A CB  1 
ATOM   326  C CG  . PHE A 1 45  ? -15.555 -8.870  19.875  1.00 10.33 ? 45  PHE A CG  1 
ATOM   327  C CD1 . PHE A 1 45  ? -16.194 -8.963  21.116  1.00 12.65 ? 45  PHE A CD1 1 
ATOM   328  C CD2 . PHE A 1 45  ? -14.391 -9.651  19.660  1.00 12.47 ? 45  PHE A CD2 1 
ATOM   329  C CE1 . PHE A 1 45  ? -15.646 -9.745  22.139  1.00 4.38  ? 45  PHE A CE1 1 
ATOM   330  C CE2 . PHE A 1 45  ? -13.861 -10.414 20.658  1.00 7.63  ? 45  PHE A CE2 1 
ATOM   331  C CZ  . PHE A 1 45  ? -14.487 -10.481 21.873  1.00 8.37  ? 45  PHE A CZ  1 
ATOM   332  N N   . HIS A 1 46  ? -14.705 -4.681  19.695  1.00 10.06 ? 46  HIS A N   1 
ATOM   333  C CA  . HIS A 1 46  ? -13.536 -3.816  19.381  1.00 8.86  ? 46  HIS A CA  1 
ATOM   334  C C   . HIS A 1 46  ? -12.642 -3.546  20.560  1.00 7.10  ? 46  HIS A C   1 
ATOM   335  O O   . HIS A 1 46  ? -13.141 -3.365  21.659  1.00 9.10  ? 46  HIS A O   1 
ATOM   336  C CB  . HIS A 1 46  ? -14.057 -2.484  18.922  1.00 10.07 ? 46  HIS A CB  1 
ATOM   337  C CG  . HIS A 1 46  ? -14.845 -2.572  17.692  1.00 12.98 ? 46  HIS A CG  1 
ATOM   338  N ND1 . HIS A 1 46  ? -15.876 -1.702  17.409  1.00 14.42 ? 46  HIS A ND1 1 
ATOM   339  C CD2 . HIS A 1 46  ? -14.713 -3.378  16.610  1.00 14.33 ? 46  HIS A CD2 1 
ATOM   340  C CE1 . HIS A 1 46  ? -16.399 -2.022  16.240  1.00 14.87 ? 46  HIS A CE1 1 
ATOM   341  N NE2 . HIS A 1 46  ? -15.708 -3.032  15.732  1.00 16.07 ? 46  HIS A NE2 1 
ATOM   342  N N   . VAL A 1 47  ? -11.337 -3.426  20.377  1.00 3.92  ? 47  VAL A N   1 
ATOM   343  C CA  . VAL A 1 47  ? -10.510 -3.040  21.512  1.00 2.92  ? 47  VAL A CA  1 
ATOM   344  C C   . VAL A 1 47  ? -10.447 -1.458  21.400  1.00 2.72  ? 47  VAL A C   1 
ATOM   345  O O   . VAL A 1 47  ? -10.128 -1.003  20.352  1.00 4.10  ? 47  VAL A O   1 
ATOM   346  C CB  . VAL A 1 47  ? -9.093  -3.606  21.404  1.00 2.00  ? 47  VAL A CB  1 
ATOM   347  C CG1 . VAL A 1 47  ? -8.235  -3.157  22.601  1.00 6.17  ? 47  VAL A CG1 1 
ATOM   348  C CG2 . VAL A 1 47  ? -9.126  -5.291  21.315  1.00 2.00  ? 47  VAL A CG2 1 
ATOM   349  N N   . HIS A 1 48  ? -10.756 -0.710  22.453  1.00 6.04  ? 48  HIS A N   1 
ATOM   350  C CA  . HIS A 1 48  ? -10.786 0.797   22.393  1.00 3.59  ? 48  HIS A CA  1 
ATOM   351  C C   . HIS A 1 48  ? -9.548  1.217   23.158  1.00 6.63  ? 48  HIS A C   1 
ATOM   352  O O   . HIS A 1 48  ? -8.895  0.380   23.775  1.00 7.92  ? 48  HIS A O   1 
ATOM   353  C CB  . HIS A 1 48  ? -12.084 1.407   23.006  1.00 2.91  ? 48  HIS A CB  1 
ATOM   354  C CG  . HIS A 1 48  ? -13.298 1.205   22.141  1.00 5.12  ? 48  HIS A CG  1 
ATOM   355  N ND1 . HIS A 1 48  ? -14.039 2.247   21.642  1.00 9.42  ? 48  HIS A ND1 1 
ATOM   356  C CD2 . HIS A 1 48  ? -13.840 0.074   21.602  1.00 5.11  ? 48  HIS A CD2 1 
ATOM   357  C CE1 . HIS A 1 48  ? -15.017 1.778   20.878  1.00 7.62  ? 48  HIS A CE1 1 
ATOM   358  N NE2 . HIS A 1 48  ? -14.919 0.459   20.845  1.00 10.62 ? 48  HIS A NE2 1 
ATOM   359  N N   . GLU A 1 49  ? -9.172  2.483   23.108  1.00 6.78  ? 49  GLU A N   1 
ATOM   360  C CA  . GLU A 1 49  ? -7.804  2.840   23.481  1.00 9.12  ? 49  GLU A CA  1 
ATOM   361  C C   . GLU A 1 49  ? -7.506  2.782   24.973  1.00 9.97  ? 49  GLU A C   1 
ATOM   362  O O   . GLU A 1 49  ? -6.457  2.217   25.426  1.00 10.29 ? 49  GLU A O   1 
ATOM   363  C CB  . GLU A 1 49  ? -7.493  4.242   22.946  1.00 9.72  ? 49  GLU A CB  1 
ATOM   364  C CG  . GLU A 1 49  ? -5.997  4.500   22.968  1.00 10.94 ? 49  GLU A CG  1 
ATOM   365  C CD  . GLU A 1 49  ? -5.688  5.813   22.340  1.00 11.13 ? 49  GLU A CD  1 
ATOM   366  O OE1 . GLU A 1 49  ? -6.570  6.351   21.630  1.00 15.05 ? 49  GLU A OE1 1 
ATOM   367  O OE2 . GLU A 1 49  ? -4.568  6.292   22.537  1.00 11.86 ? 49  GLU A OE2 1 
ATOM   368  N N   . PHE A 1 50  ? -8.445  3.280   25.778  1.00 9.23  ? 50  PHE A N   1 
ATOM   369  C CA  . PHE A 1 50  ? -8.198  3.277   27.207  1.00 7.92  ? 50  PHE A CA  1 
ATOM   370  C C   . PHE A 1 50  ? -8.903  2.217   28.063  1.00 8.65  ? 50  PHE A C   1 
ATOM   371  O O   . PHE A 1 50  ? -10.111 1.880   27.859  1.00 8.22  ? 50  PHE A O   1 
ATOM   372  C CB  . PHE A 1 50  ? -8.517  4.697   27.726  1.00 9.92  ? 50  PHE A CB  1 
ATOM   373  C CG  . PHE A 1 50  ? -7.840  5.772   26.893  1.00 5.67  ? 50  PHE A CG  1 
ATOM   374  C CD1 . PHE A 1 50  ? -6.424  5.913   26.926  1.00 3.34  ? 50  PHE A CD1 1 
ATOM   375  C CD2 . PHE A 1 50  ? -8.573  6.550   26.015  1.00 12.65 ? 50  PHE A CD2 1 
ATOM   376  C CE1 . PHE A 1 50  ? -5.786  6.886   26.125  1.00 9.03  ? 50  PHE A CE1 1 
ATOM   377  C CE2 . PHE A 1 50  ? -7.928  7.532   25.244  1.00 6.90  ? 50  PHE A CE2 1 
ATOM   378  C CZ  . PHE A 1 50  ? -6.539  7.657   25.294  1.00 4.47  ? 50  PHE A CZ  1 
ATOM   379  N N   . GLY A 1 51  ? -8.183  1.778   29.098  1.00 7.11  ? 51  GLY A N   1 
ATOM   380  C CA  . GLY A 1 51  ? -8.790  1.054   30.239  1.00 5.81  ? 51  GLY A CA  1 
ATOM   381  C C   . GLY A 1 51  ? -9.379  1.998   31.279  1.00 7.36  ? 51  GLY A C   1 
ATOM   382  O O   . GLY A 1 51  ? -9.144  1.862   32.486  1.00 7.92  ? 51  GLY A O   1 
ATOM   383  N N   . ASP A 1 52  ? -10.204 2.945   30.813  1.00 7.23  ? 52  ASP A N   1 
ATOM   384  C CA  . ASP A 1 52  ? -10.849 3.910   31.669  1.00 7.05  ? 52  ASP A CA  1 
ATOM   385  C C   . ASP A 1 52  ? -12.373 3.679   31.679  1.00 5.97  ? 52  ASP A C   1 
ATOM   386  O O   . ASP A 1 52  ? -12.993 3.676   30.668  1.00 7.65  ? 52  ASP A O   1 
ATOM   387  C CB  . ASP A 1 52  ? -10.511 5.260   31.131  1.00 8.14  ? 52  ASP A CB  1 
ATOM   388  C CG  . ASP A 1 52  ? -11.048 6.374   32.001  1.00 10.02 ? 52  ASP A CG  1 
ATOM   389  O OD1 . ASP A 1 52  ? -12.106 6.195   32.607  1.00 11.29 ? 52  ASP A OD1 1 
ATOM   390  O OD2 . ASP A 1 52  ? -10.402 7.446   32.041  1.00 18.85 ? 52  ASP A OD2 1 
ATOM   391  N N   . ASN A 1 53  ? -12.957 3.356   32.825  1.00 7.94  ? 53  ASN A N   1 
ATOM   392  C CA  . ASN A 1 53  ? -14.404 3.176   32.959  1.00 8.41  ? 53  ASN A CA  1 
ATOM   393  C C   . ASN A 1 53  ? -14.878 4.247   33.871  1.00 8.74  ? 53  ASN A C   1 
ATOM   394  O O   . ASN A 1 53  ? -15.885 4.096   34.454  1.00 9.43  ? 53  ASN A O   1 
ATOM   395  C CB  . ASN A 1 53  ? -14.784 1.824   33.609  1.00 9.18  ? 53  ASN A CB  1 
ATOM   396  C CG  . ASN A 1 53  ? -16.140 1.302   33.109  1.00 13.86 ? 53  ASN A CG  1 
ATOM   397  O OD1 . ASN A 1 53  ? -16.524 1.588   31.969  1.00 18.52 ? 53  ASN A OD1 1 
ATOM   398  N ND2 . ASN A 1 53  ? -16.856 0.531   33.927  1.00 16.57 ? 53  ASN A ND2 1 
ATOM   399  N N   . THR A 1 54  ? -14.224 5.393   33.959  1.00 11.00 ? 54  THR A N   1 
ATOM   400  C CA  . THR A 1 54  ? -14.723 6.334   34.976  1.00 11.86 ? 54  THR A CA  1 
ATOM   401  C C   . THR A 1 54  ? -16.136 6.762   34.690  1.00 13.66 ? 54  THR A C   1 
ATOM   402  O O   . THR A 1 54  ? -16.826 7.164   35.613  1.00 15.30 ? 54  THR A O   1 
ATOM   403  C CB  . THR A 1 54  ? -13.918 7.574   35.131  1.00 12.52 ? 54  THR A CB  1 
ATOM   404  O OG1 . THR A 1 54  ? -13.643 8.074   33.835  1.00 17.43 ? 54  THR A OG1 1 
ATOM   405  C CG2 . THR A 1 54  ? -12.660 7.327   35.777  1.00 13.91 ? 54  THR A CG2 1 
ATOM   406  N N   . ALA A 1 55  ? -16.559 6.676   33.416  1.00 15.54 ? 55  ALA A N   1 
ATOM   407  C CA  . ALA A 1 55  ? -17.879 7.147   32.944  1.00 15.30 ? 55  ALA A CA  1 
ATOM   408  C C   . ALA A 1 55  ? -18.539 6.043   32.164  1.00 14.48 ? 55  ALA A C   1 
ATOM   409  O O   . ALA A 1 55  ? -19.217 6.291   31.240  1.00 15.15 ? 55  ALA A O   1 
ATOM   410  C CB  . ALA A 1 55  ? -17.776 8.401   32.095  1.00 15.11 ? 55  ALA A CB  1 
ATOM   411  N N   . GLY A 1 56  ? -18.381 4.796   32.558  1.00 15.20 ? 56  GLY A N   1 
ATOM   412  C CA  . GLY A 1 56  ? -18.951 3.777   31.758  1.00 13.39 ? 56  GLY A CA  1 
ATOM   413  C C   . GLY A 1 56  ? -18.089 3.553   30.531  1.00 14.48 ? 56  GLY A C   1 
ATOM   414  O O   . GLY A 1 56  ? -16.915 3.923   30.531  1.00 14.46 ? 56  GLY A O   1 
ATOM   415  N N   . CYS A 1 57  ? -18.651 2.956   29.470  1.00 13.93 ? 57  CYS A N   1 
ATOM   416  C CA  . CYS A 1 57  ? -17.856 2.521   28.362  1.00 12.97 ? 57  CYS A CA  1 
ATOM   417  C C   . CYS A 1 57  ? -17.411 3.702   27.498  1.00 13.84 ? 57  CYS A C   1 
ATOM   418  O O   . CYS A 1 57  ? -16.375 3.652   26.855  1.00 13.96 ? 57  CYS A O   1 
ATOM   419  C CB  . CYS A 1 57  ? -18.568 1.501   27.558  1.00 13.57 ? 57  CYS A CB  1 
ATOM   420  S SG  . CYS A 1 57  ? -18.871 -0.035  28.480  1.00 11.49 ? 57  CYS A SG  1 
ATOM   421  N N   . THR A 1 58  ? -18.169 4.772   27.507  1.00 14.10 ? 58  THR A N   1 
ATOM   422  C CA  . THR A 1 58  ? -17.757 5.981   26.808  1.00 14.78 ? 58  THR A CA  1 
ATOM   423  C C   . THR A 1 58  ? -16.284 6.317   27.045  1.00 14.99 ? 58  THR A C   1 
ATOM   424  O O   . THR A 1 58  ? -15.542 6.658   26.080  1.00 17.62 ? 58  THR A O   1 
ATOM   425  C CB  . THR A 1 58  ? -18.625 7.114   27.335  1.00 15.36 ? 58  THR A CB  1 
ATOM   426  O OG1 . THR A 1 58  ? -19.926 6.827   26.888  1.00 20.71 ? 58  THR A OG1 1 
ATOM   427  C CG2 . THR A 1 58  ? -18.251 8.459   26.750  1.00 18.24 ? 58  THR A CG2 1 
ATOM   428  N N   . SER A 1 59  ? -15.838 6.258   28.304  1.00 15.01 ? 59  SER A N   1 
ATOM   429  C CA  . SER A 1 59  ? -14.480 6.711   28.634  1.00 14.94 ? 59  SER A CA  1 
ATOM   430  C C   . SER A 1 59  ? -13.378 5.845   28.083  1.00 15.23 ? 59  SER A C   1 
ATOM   431  O O   . SER A 1 59  ? -12.237 6.265   28.127  1.00 15.81 ? 59  SER A O   1 
ATOM   432  C CB  . SER A 1 59  ? -14.243 7.012   30.123  1.00 14.73 ? 59  SER A CB  1 
ATOM   433  O OG  . SER A 1 59  ? -15.274 6.708   30.988  1.00 16.86 ? 59  SER A OG  1 
ATOM   434  N N   . ALA A 1 60  ? -13.704 4.641   27.564  1.00 14.78 ? 60  ALA A N   1 
ATOM   435  C CA  . ALA A 1 60  ? -12.711 3.842   26.876  1.00 13.99 ? 60  ALA A CA  1 
ATOM   436  C C   . ALA A 1 60  ? -12.183 4.572   25.666  1.00 15.09 ? 60  ALA A C   1 
ATOM   437  O O   . ALA A 1 60  ? -11.086 4.273   25.164  1.00 15.14 ? 60  ALA A O   1 
ATOM   438  C CB  . ALA A 1 60  ? -13.279 2.608   26.445  1.00 14.39 ? 60  ALA A CB  1 
ATOM   439  N N   . GLY A 1 61  ? -12.953 5.521   25.154  1.00 14.88 ? 61  GLY A N   1 
ATOM   440  C CA  . GLY A 1 61  ? -12.498 6.335   23.980  1.00 13.13 ? 61  GLY A CA  1 
ATOM   441  C C   . GLY A 1 61  ? -12.647 5.577   22.686  1.00 13.25 ? 61  GLY A C   1 
ATOM   442  O O   . GLY A 1 61  ? -13.518 4.711   22.551  1.00 15.75 ? 61  GLY A O   1 
ATOM   443  N N   . PRO A 1 62  ? -11.800 5.873   21.710  1.00 12.72 ? 62  PRO A N   1 
ATOM   444  C CA  . PRO A 1 62  ? -12.038 5.378   20.414  1.00 12.16 ? 62  PRO A CA  1 
ATOM   445  C C   . PRO A 1 62  ? -11.370 4.073   20.228  1.00 11.62 ? 62  PRO A C   1 
ATOM   446  O O   . PRO A 1 62  ? -10.818 3.513   21.166  1.00 12.29 ? 62  PRO A O   1 
ATOM   447  C CB  . PRO A 1 62  ? -11.442 6.487   19.522  1.00 11.84 ? 62  PRO A CB  1 
ATOM   448  C CG  . PRO A 1 62  ? -10.258 6.906   20.290  1.00 12.40 ? 62  PRO A CG  1 
ATOM   449  C CD  . PRO A 1 62  ? -10.664 6.803   21.734  1.00 13.95 ? 62  PRO A CD  1 
ATOM   450  N N   . HIS A 1 63  ? -11.439 3.547   19.032  1.00 11.87 ? 63  HIS A N   1 
ATOM   451  C CA  . HIS A 1 63  ? -10.805 2.273   18.791  1.00 11.50 ? 63  HIS A CA  1 
ATOM   452  C C   . HIS A 1 63  ? -9.324  2.494   19.010  1.00 11.67 ? 63  HIS A C   1 
ATOM   453  O O   . HIS A 1 63  ? -8.762  3.635   18.881  1.00 8.92  ? 63  HIS A O   1 
ATOM   454  C CB  . HIS A 1 63  ? -11.028 1.797   17.353  1.00 12.97 ? 63  HIS A CB  1 
ATOM   455  C CG  . HIS A 1 63  ? -12.448 1.402   17.027  1.00 14.44 ? 63  HIS A CG  1 
ATOM   456  N ND1 . HIS A 1 63  ? -12.790 0.783   15.844  1.00 15.63 ? 63  HIS A ND1 1 
ATOM   457  C CD2 . HIS A 1 63  ? -13.604 1.518   17.725  1.00 15.25 ? 63  HIS A CD2 1 
ATOM   458  C CE1 . HIS A 1 63  ? -14.096 0.574   15.810  1.00 14.88 ? 63  HIS A CE1 1 
ATOM   459  N NE2 . HIS A 1 63  ? -14.609 0.979   16.954  1.00 11.69 ? 63  HIS A NE2 1 
ATOM   460  N N   . PHE A 1 64  ? -8.658  1.401   19.314  1.00 10.48 ? 64  PHE A N   1 
ATOM   461  C CA  . PHE A 1 64  ? -7.246  1.479   19.604  1.00 11.44 ? 64  PHE A CA  1 
ATOM   462  C C   . PHE A 1 64  ? -6.658  1.423   18.225  1.00 12.54 ? 64  PHE A C   1 
ATOM   463  O O   . PHE A 1 64  ? -6.756  0.407   17.529  1.00 12.31 ? 64  PHE A O   1 
ATOM   464  C CB  . PHE A 1 64  ? -6.787  0.301   20.534  1.00 10.72 ? 64  PHE A CB  1 
ATOM   465  C CG  . PHE A 1 64  ? -5.264  0.121   20.616  1.00 7.91  ? 64  PHE A CG  1 
ATOM   466  C CD1 . PHE A 1 64  ? -4.440  1.209   20.812  1.00 3.86  ? 64  PHE A CD1 1 
ATOM   467  C CD2 . PHE A 1 64  ? -4.692  -1.145  20.552  1.00 5.59  ? 64  PHE A CD2 1 
ATOM   468  C CE1 . PHE A 1 64  ? -3.101  1.046   20.911  1.00 6.45  ? 64  PHE A CE1 1 
ATOM   469  C CE2 . PHE A 1 64  ? -3.319  -1.329  20.652  1.00 5.43  ? 64  PHE A CE2 1 
ATOM   470  C CZ  . PHE A 1 64  ? -2.516  -0.229  20.827  1.00 10.21 ? 64  PHE A CZ  1 
ATOM   471  N N   . ASN A 1 65  ? -6.074  2.540   17.797  1.00 14.38 ? 65  ASN A N   1 
ATOM   472  C CA  . ASN A 1 65  ? -5.609  2.575   16.444  1.00 16.16 ? 65  ASN A CA  1 
ATOM   473  C C   . ASN A 1 65  ? -4.257  3.247   16.448  1.00 17.66 ? 65  ASN A C   1 
ATOM   474  O O   . ASN A 1 65  ? -4.146  4.419   15.993  1.00 18.55 ? 65  ASN A O   1 
ATOM   475  C CB  . ASN A 1 65  ? -6.630  3.387   15.625  1.00 18.10 ? 65  ASN A CB  1 
ATOM   476  C CG  . ASN A 1 65  ? -6.337  3.415   14.120  1.00 19.86 ? 65  ASN A CG  1 
ATOM   477  O OD1 . ASN A 1 65  ? -5.800  2.451   13.558  1.00 24.55 ? 65  ASN A OD1 1 
ATOM   478  N ND2 . ASN A 1 65  ? -6.740  4.530   13.459  1.00 21.66 ? 65  ASN A ND2 1 
ATOM   479  N N   . PRO A 1 66  ? -3.197  2.536   16.894  1.00 16.83 ? 66  PRO A N   1 
ATOM   480  C CA  . PRO A 1 66  ? -2.005  3.342   17.023  1.00 17.16 ? 66  PRO A CA  1 
ATOM   481  C C   . PRO A 1 66  ? -1.428  3.721   15.656  1.00 18.51 ? 66  PRO A C   1 
ATOM   482  O O   . PRO A 1 66  ? -0.622  4.633   15.598  1.00 19.54 ? 66  PRO A O   1 
ATOM   483  C CB  . PRO A 1 66  ? -1.016  2.440   17.744  1.00 15.54 ? 66  PRO A CB  1 
ATOM   484  C CG  . PRO A 1 66  ? -1.508  1.066   17.624  1.00 16.40 ? 66  PRO A CG  1 
ATOM   485  C CD  . PRO A 1 66  ? -2.944  1.094   17.139  1.00 17.53 ? 66  PRO A CD  1 
ATOM   486  N N   . LEU A 1 67  ? -1.800  3.016   14.582  1.00 19.09 ? 67  LEU A N   1 
ATOM   487  C CA  . LEU A 1 67  ? -1.228  3.263   13.261  1.00 20.73 ? 67  LEU A CA  1 
ATOM   488  C C   . LEU A 1 67  ? -2.040  4.221   12.389  1.00 22.63 ? 67  LEU A C   1 
ATOM   489  O O   . LEU A 1 67  ? -1.834  4.293   11.195  1.00 23.91 ? 67  LEU A O   1 
ATOM   490  C CB  . LEU A 1 67  ? -0.935  1.952   12.498  1.00 20.18 ? 67  LEU A CB  1 
ATOM   491  C CG  . LEU A 1 67  ? -0.103  0.868   13.167  1.00 19.36 ? 67  LEU A CG  1 
ATOM   492  C CD1 . LEU A 1 67  ? -0.165  -0.430  12.394  1.00 24.38 ? 67  LEU A CD1 1 
ATOM   493  C CD2 . LEU A 1 67  ? 1.297   1.228   13.371  1.00 18.63 ? 67  LEU A CD2 1 
ATOM   494  N N   . SER A 1 68  ? -2.943  4.983   12.990  1.00 23.88 ? 68  SER A N   1 
ATOM   495  C CA  . SER A 1 68  ? -3.898  5.782   12.261  1.00 24.41 ? 68  SER A CA  1 
ATOM   496  C C   . SER A 1 68  ? -4.503  5.183   10.967  1.00 25.18 ? 68  SER A C   1 
ATOM   497  O O   . SER A 1 68  ? -4.752  5.938   10.021  1.00 25.06 ? 68  SER A O   1 
ATOM   498  C CB  . SER A 1 68  ? -3.389  7.197   12.055  1.00 25.04 ? 68  SER A CB  1 
ATOM   499  O OG  . SER A 1 68  ? -2.743  7.645   13.231  1.00 25.30 ? 68  SER A OG  1 
ATOM   500  N N   . ARG A 1 69  ? -4.759  3.865   10.928  1.00 24.11 ? 69  ARG A N   1 
ATOM   501  C CA  . ARG A 1 69  ? -5.472  3.265   9.785   1.00 24.53 ? 69  ARG A CA  1 
ATOM   502  C C   . ARG A 1 69  ? -6.946  3.669   9.750   1.00 24.78 ? 69  ARG A C   1 
ATOM   503  O O   . ARG A 1 69  ? -7.419  4.354   10.654  1.00 24.51 ? 69  ARG A O   1 
ATOM   504  C CB  . ARG A 1 69  ? -5.356  1.736   9.740   1.00 23.67 ? 69  ARG A CB  1 
ATOM   505  C CG  . ARG A 1 69  ? -4.170  1.218   8.971   1.00 26.62 ? 69  ARG A CG  1 
ATOM   506  C CD  . ARG A 1 69  ? -3.025  2.146   9.210   1.00 30.06 ? 69  ARG A CD  1 
ATOM   507  N NE  . ARG A 1 69  ? -1.661  1.679   8.988   1.00 34.16 ? 69  ARG A NE  1 
ATOM   508  C CZ  . ARG A 1 69  ? -1.238  0.433   8.804   1.00 35.20 ? 69  ARG A CZ  1 
ATOM   509  N NH1 . ARG A 1 69  ? -2.058  -0.616  8.705   1.00 35.95 ? 69  ARG A NH1 1 
ATOM   510  N NH2 . ARG A 1 69  ? 0.063   0.258   8.648   1.00 38.25 ? 69  ARG A NH2 1 
ATOM   511  N N   . LYS A 1 70  ? -7.646  3.238   8.682   1.00 25.08 ? 70  LYS A N   1 
ATOM   512  C CA  . LYS A 1 70  ? -9.085  3.410   8.532   1.00 24.11 ? 70  LYS A CA  1 
ATOM   513  C C   . LYS A 1 70  ? -9.701  2.153   9.072   1.00 22.96 ? 70  LYS A C   1 
ATOM   514  O O   . LYS A 1 70  ? -9.108  1.078   8.902   1.00 23.37 ? 70  LYS A O   1 
ATOM   515  C CB  . LYS A 1 70  ? -9.483  3.553   7.048   1.00 25.30 ? 70  LYS A CB  1 
ATOM   516  C CG  . LYS A 1 70  ? -8.998  4.855   6.362   1.00 26.40 ? 70  LYS A CG  1 
ATOM   517  C CD  . LYS A 1 70  ? -10.032 5.982   6.357   1.00 31.00 ? 70  LYS A CD  1 
ATOM   518  C CE  . LYS A 1 70  ? -9.601  7.178   5.457   1.00 31.22 ? 70  LYS A CE  1 
ATOM   519  N NZ  . LYS A 1 70  ? -8.830  8.238   6.201   1.00 34.91 ? 70  LYS A NZ  1 
ATOM   520  N N   . HIS A 1 71  ? -10.873 2.280   9.704   1.00 19.73 ? 71  HIS A N   1 
ATOM   521  C CA  . HIS A 1 71  ? -11.629 1.121   10.146  1.00 18.70 ? 71  HIS A CA  1 
ATOM   522  C C   . HIS A 1 71  ? -11.748 0.080   9.031   1.00 18.38 ? 71  HIS A C   1 
ATOM   523  O O   . HIS A 1 71  ? -12.027 0.428   7.883   1.00 19.03 ? 71  HIS A O   1 
ATOM   524  C CB  . HIS A 1 71  ? -13.020 1.518   10.707  1.00 16.95 ? 71  HIS A CB  1 
ATOM   525  C CG  . HIS A 1 71  ? -13.799 0.338   11.175  1.00 16.26 ? 71  HIS A CG  1 
ATOM   526  N ND1 . HIS A 1 71  ? -13.360 -0.461  12.199  1.00 13.69 ? 71  HIS A ND1 1 
ATOM   527  C CD2 . HIS A 1 71  ? -14.897 -0.269  10.672  1.00 16.32 ? 71  HIS A CD2 1 
ATOM   528  C CE1 . HIS A 1 71  ? -14.200 -1.474  12.365  1.00 15.27 ? 71  HIS A CE1 1 
ATOM   529  N NE2 . HIS A 1 71  ? -15.140 -1.384  11.444  1.00 17.87 ? 71  HIS A NE2 1 
ATOM   530  N N   . GLY A 1 72  ? -11.571 -1.199  9.364   1.00 18.11 ? 72  GLY A N   1 
ATOM   531  C CA  . GLY A 1 72  ? -11.835 -2.273  8.440   1.00 17.22 ? 72  GLY A CA  1 
ATOM   532  C C   . GLY A 1 72  ? -12.165 -3.473  9.290   1.00 18.11 ? 72  GLY A C   1 
ATOM   533  O O   . GLY A 1 72  ? -12.500 -3.317  10.446  1.00 18.89 ? 72  GLY A O   1 
ATOM   534  N N   . GLY A 1 73  ? -12.068 -4.673  8.727   1.00 18.34 ? 73  GLY A N   1 
ATOM   535  C CA  . GLY A 1 73  ? -12.365 -5.906  9.443   1.00 17.99 ? 73  GLY A CA  1 
ATOM   536  C C   . GLY A 1 73  ? -11.060 -6.572  9.805   1.00 18.49 ? 73  GLY A C   1 
ATOM   537  O O   . GLY A 1 73  ? -10.044 -6.192  9.297   1.00 18.58 ? 73  GLY A O   1 
ATOM   538  N N   . PRO A 1 74  ? -11.092 -7.575  10.698  1.00 19.41 ? 74  PRO A N   1 
ATOM   539  C CA  . PRO A 1 74  ? -9.913  -8.308  11.214  1.00 20.64 ? 74  PRO A CA  1 
ATOM   540  C C   . PRO A 1 74  ? -9.038  -8.974  10.147  1.00 22.28 ? 74  PRO A C   1 
ATOM   541  O O   . PRO A 1 74  ? -7.823  -9.201  10.372  1.00 21.60 ? 74  PRO A O   1 
ATOM   542  C CB  . PRO A 1 74  ? -10.524 -9.414  12.118  1.00 20.01 ? 74  PRO A CB  1 
ATOM   543  C CG  . PRO A 1 74  ? -11.947 -9.527  11.725  1.00 19.59 ? 74  PRO A CG  1 
ATOM   544  C CD  . PRO A 1 74  ? -12.338 -8.093  11.296  1.00 19.38 ? 74  PRO A CD  1 
ATOM   545  N N   . LYS A 1 75  ? -9.671  -9.324  9.029   1.00 23.58 ? 75  LYS A N   1 
ATOM   546  C CA  . LYS A 1 75  ? -9.002  -9.993  7.904   1.00 24.45 ? 75  LYS A CA  1 
ATOM   547  C C   . LYS A 1 75  ? -8.421  -9.011  6.903   1.00 23.65 ? 75  LYS A C   1 
ATOM   548  O O   . LYS A 1 75  ? -7.769  -9.426  5.964   1.00 24.08 ? 75  LYS A O   1 
ATOM   549  C CB  . LYS A 1 75  ? -9.974  -10.911 7.188   1.00 24.55 ? 75  LYS A CB  1 
ATOM   550  C CG  . LYS A 1 75  ? -10.127 -12.356 7.724   1.00 27.62 ? 75  LYS A CG  1 
ATOM   551  C CD  . LYS A 1 75  ? -11.146 -12.987 6.788   1.00 30.02 ? 75  LYS A CD  1 
ATOM   552  C CE  . LYS A 1 75  ? -12.010 -14.032 7.449   1.00 35.05 ? 75  LYS A CE  1 
ATOM   553  N NZ  . LYS A 1 75  ? -13.303 -14.293 6.676   1.00 35.98 ? 75  LYS A NZ  1 
ATOM   554  N N   . ASP A 1 76  ? -8.647  -7.714  7.120   1.00 24.35 ? 76  ASP A N   1 
ATOM   555  C CA  . ASP A 1 76  ? -8.114  -6.648  6.283   1.00 25.52 ? 76  ASP A CA  1 
ATOM   556  C C   . ASP A 1 76  ? -6.738  -6.138  6.692   1.00 26.25 ? 76  ASP A C   1 
ATOM   557  O O   . ASP A 1 76  ? -6.408  -6.010  7.884   1.00 26.96 ? 76  ASP A O   1 
ATOM   558  C CB  . ASP A 1 76  ? -9.059  -5.421  6.263   1.00 25.46 ? 76  ASP A CB  1 
ATOM   559  C CG  . ASP A 1 76  ? -10.434 -5.736  5.699   1.00 27.30 ? 76  ASP A CG  1 
ATOM   560  O OD1 . ASP A 1 76  ? -10.599 -6.773  5.007   1.00 27.69 ? 76  ASP A OD1 1 
ATOM   561  O OD2 . ASP A 1 76  ? -11.366 -4.943  5.952   1.00 27.75 ? 76  ASP A OD2 1 
ATOM   562  N N   . GLU A 1 77  ? -5.956  -5.771  5.689   1.00 26.92 ? 77  GLU A N   1 
ATOM   563  C CA  . GLU A 1 77  ? -4.702  -5.081  5.932   1.00 28.18 ? 77  GLU A CA  1 
ATOM   564  C C   . GLU A 1 77  ? -4.930  -3.656  6.417   1.00 27.53 ? 77  GLU A C   1 
ATOM   565  O O   . GLU A 1 77  ? -4.200  -3.136  7.285   1.00 28.31 ? 77  GLU A O   1 
ATOM   566  C CB  . GLU A 1 77  ? -3.862  -5.068  4.653   1.00 29.68 ? 77  GLU A CB  1 
ATOM   567  C CG  . GLU A 1 77  ? -2.465  -4.577  4.877   1.00 33.58 ? 77  GLU A CG  1 
ATOM   568  C CD  . GLU A 1 77  ? -1.689  -5.583  5.685   1.00 39.24 ? 77  GLU A CD  1 
ATOM   569  O OE1 . GLU A 1 77  ? -1.870  -6.817  5.464   1.00 39.60 ? 77  GLU A OE1 1 
ATOM   570  O OE2 . GLU A 1 77  ? -0.911  -5.140  6.560   1.00 42.77 ? 77  GLU A OE2 1 
ATOM   571  N N   . GLU A 1 78  ? -5.935  -2.987  5.866   1.00 26.31 ? 78  GLU A N   1 
ATOM   572  C CA  . GLU A 1 78  ? -6.249  -1.662  6.391   1.00 24.03 ? 78  GLU A CA  1 
ATOM   573  C C   . GLU A 1 78  ? -7.296  -1.844  7.472   1.00 22.50 ? 78  GLU A C   1 
ATOM   574  O O   . GLU A 1 78  ? -8.462  -2.084  7.159   1.00 23.82 ? 78  GLU A O   1 
ATOM   575  C CB  . GLU A 1 78  ? -6.743  -0.726  5.284   1.00 24.45 ? 78  GLU A CB  1 
ATOM   576  C CG  . GLU A 1 78  ? -6.786  0.754   5.698   1.00 24.74 ? 78  GLU A CG  1 
ATOM   577  C CD  . GLU A 1 78  ? -5.395  1.390   5.686   1.00 29.28 ? 78  GLU A CD  1 
ATOM   578  O OE1 . GLU A 1 78  ? -4.383  0.703   5.307   1.00 28.08 ? 78  GLU A OE1 1 
ATOM   579  O OE2 . GLU A 1 78  ? -5.322  2.597   6.040   1.00 27.48 ? 78  GLU A OE2 1 
ATOM   580  N N   . ARG A 1 79  ? -6.874  -1.744  8.739   1.00 20.87 ? 79  ARG A N   1 
ATOM   581  C CA  . ARG A 1 79  ? -7.743  -1.893  9.931   1.00 18.64 ? 79  ARG A CA  1 
ATOM   582  C C   . ARG A 1 79  ? -6.993  -1.311  11.106  1.00 18.32 ? 79  ARG A C   1 
ATOM   583  O O   . ARG A 1 79  ? -5.747  -1.211  11.101  1.00 19.05 ? 79  ARG A O   1 
ATOM   584  C CB  . ARG A 1 79  ? -8.046  -3.370  10.252  1.00 18.13 ? 79  ARG A CB  1 
ATOM   585  C CG  . ARG A 1 79  ? -6.816  -4.144  10.595  1.00 16.14 ? 79  ARG A CG  1 
ATOM   586  C CD  . ARG A 1 79  ? -7.053  -5.587  11.115  1.00 16.44 ? 79  ARG A CD  1 
ATOM   587  N NE  . ARG A 1 79  ? -6.973  -5.594  12.577  1.00 12.39 ? 79  ARG A NE  1 
ATOM   588  C CZ  . ARG A 1 79  ? -6.958  -6.696  13.290  1.00 13.37 ? 79  ARG A CZ  1 
ATOM   589  N NH1 . ARG A 1 79  ? -6.989  -7.863  12.670  1.00 12.11 ? 79  ARG A NH1 1 
ATOM   590  N NH2 . ARG A 1 79  ? -6.841  -6.621  14.610  1.00 10.65 ? 79  ARG A NH2 1 
ATOM   591  N N   . HIS A 1 80  ? -7.747  -0.930  12.121  1.00 16.87 ? 80  HIS A N   1 
ATOM   592  C CA  . HIS A 1 80  ? -7.180  -0.666  13.453  1.00 15.72 ? 80  HIS A CA  1 
ATOM   593  C C   . HIS A 1 80  ? -6.673  -1.926  14.058  1.00 14.31 ? 80  HIS A C   1 
ATOM   594  O O   . HIS A 1 80  ? -7.222  -2.992  13.821  1.00 13.26 ? 80  HIS A O   1 
ATOM   595  C CB  . HIS A 1 80  ? -8.280  -0.173  14.409  1.00 16.22 ? 80  HIS A CB  1 
ATOM   596  C CG  . HIS A 1 80  ? -9.076  0.963   13.854  1.00 16.57 ? 80  HIS A CG  1 
ATOM   597  N ND1 . HIS A 1 80  ? -10.375 1.224   14.240  1.00 14.59 ? 80  HIS A ND1 1 
ATOM   598  C CD2 . HIS A 1 80  ? -8.782  1.836   12.864  1.00 9.52  ? 80  HIS A CD2 1 
ATOM   599  C CE1 . HIS A 1 80  ? -10.804 2.288   13.570  1.00 14.55 ? 80  HIS A CE1 1 
ATOM   600  N NE2 . HIS A 1 80  ? -9.871  2.662   12.718  1.00 11.94 ? 80  HIS A NE2 1 
ATOM   601  N N   . VAL A 1 81  ? -5.741  -1.758  14.997  1.00 15.13 ? 81  VAL A N   1 
ATOM   602  C CA  . VAL A 1 81  ? -5.240  -2.878  15.823  1.00 12.49 ? 81  VAL A CA  1 
ATOM   603  C C   . VAL A 1 81  ? -6.431  -3.470  16.553  1.00 13.32 ? 81  VAL A C   1 
ATOM   604  O O   . VAL A 1 81  ? -6.650  -4.704  16.567  1.00 11.93 ? 81  VAL A O   1 
ATOM   605  C CB  . VAL A 1 81  ? -4.200  -2.405  16.808  1.00 12.59 ? 81  VAL A CB  1 
ATOM   606  C CG1 . VAL A 1 81  ? -3.852  -3.546  17.775  1.00 7.45  ? 81  VAL A CG1 1 
ATOM   607  C CG2 . VAL A 1 81  ? -2.994  -1.926  16.073  1.00 11.55 ? 81  VAL A CG2 1 
ATOM   608  N N   . GLY A 1 82  ? -7.241  -2.571  17.110  1.00 12.44 ? 82  GLY A N   1 
ATOM   609  C CA  . GLY A 1 82  ? -8.467  -3.002  17.751  1.00 12.86 ? 82  GLY A CA  1 
ATOM   610  C C   . GLY A 1 82  ? -9.606  -3.624  16.942  1.00 13.04 ? 82  GLY A C   1 
ATOM   611  O O   . GLY A 1 82  ? -10.555 -4.089  17.540  1.00 15.03 ? 82  GLY A O   1 
ATOM   612  N N   . ASP A 1 83  ? -9.551  -3.673  15.608  1.00 12.13 ? 83  ASP A N   1 
ATOM   613  C CA  . ASP A 1 83  ? -10.728 -4.061  14.802  1.00 9.63  ? 83  ASP A CA  1 
ATOM   614  C C   . ASP A 1 83  ? -10.864 -5.588  14.710  1.00 8.14  ? 83  ASP A C   1 
ATOM   615  O O   . ASP A 1 83  ? -10.270 -6.208  13.838  1.00 8.58  ? 83  ASP A O   1 
ATOM   616  C CB  . ASP A 1 83  ? -10.577 -3.612  13.398  1.00 7.30  ? 83  ASP A CB  1 
ATOM   617  C CG  . ASP A 1 83  ? -10.868 -2.140  13.203  1.00 9.98  ? 83  ASP A CG  1 
ATOM   618  O OD1 . ASP A 1 83  ? -11.451 -1.480  14.100  1.00 5.61  ? 83  ASP A OD1 1 
ATOM   619  O OD2 . ASP A 1 83  ? -10.557 -1.687  12.084  1.00 13.08 ? 83  ASP A OD2 1 
ATOM   620  N N   . LEU A 1 84  ? -11.709 -6.152  15.557  1.00 10.03 ? 84  LEU A N   1 
ATOM   621  C CA  . LEU A 1 84  ? -11.818 -7.647  15.707  1.00 7.96  ? 84  LEU A CA  1 
ATOM   622  C C   . LEU A 1 84  ? -13.116 -8.180  15.147  1.00 9.48  ? 84  LEU A C   1 
ATOM   623  O O   . LEU A 1 84  ? -13.437 -9.447  15.282  1.00 3.84  ? 84  LEU A O   1 
ATOM   624  C CB  . LEU A 1 84  ? -11.626 -8.107  17.181  1.00 8.48  ? 84  LEU A CB  1 
ATOM   625  C CG  . LEU A 1 84  ? -10.267 -8.162  17.897  1.00 6.71  ? 84  LEU A CG  1 
ATOM   626  C CD1 . LEU A 1 84  ? -10.356 -9.062  19.135  1.00 14.09 ? 84  LEU A CD1 1 
ATOM   627  C CD2 . LEU A 1 84  ? -9.166  -8.628  16.953  1.00 2.89  ? 84  LEU A CD2 1 
ATOM   628  N N   . GLY A 1 85  ? -13.866 -7.287  14.487  1.00 6.21  ? 85  GLY A N   1 
ATOM   629  C CA  . GLY A 1 85  ? -14.973 -7.721  13.674  1.00 8.44  ? 85  GLY A CA  1 
ATOM   630  C C   . GLY A 1 85  ? -16.265 -7.833  14.410  1.00 8.80  ? 85  GLY A C   1 
ATOM   631  O O   . GLY A 1 85  ? -16.745 -6.860  14.914  1.00 9.14  ? 85  GLY A O   1 
ATOM   632  N N   . ASN A 1 86  ? -16.861 -9.014  14.489  1.00 9.31  ? 86  ASN A N   1 
ATOM   633  C CA  . ASN A 1 86  ? -18.223 -9.077  14.973  1.00 9.19  ? 86  ASN A CA  1 
ATOM   634  C C   . ASN A 1 86  ? -18.263 -10.413 15.640  1.00 11.54 ? 86  ASN A C   1 
ATOM   635  O O   . ASN A 1 86  ? -17.533 -11.301 15.265  1.00 9.74  ? 86  ASN A O   1 
ATOM   636  C CB  . ASN A 1 86  ? -19.273 -9.219  13.843  1.00 10.31 ? 86  ASN A CB  1 
ATOM   637  C CG  . ASN A 1 86  ? -19.598 -7.939  13.130  1.00 13.81 ? 86  ASN A CG  1 
ATOM   638  O OD1 . ASN A 1 86  ? -19.968 -6.911  13.731  1.00 6.47  ? 86  ASN A OD1 1 
ATOM   639  N ND2 . ASN A 1 86  ? -19.499 -8.000  11.800  1.00 15.31 ? 86  ASN A ND2 1 
ATOM   640  N N   . VAL A 1 87  ? -19.080 -10.513 16.681  1.00 12.78 ? 87  VAL A N   1 
ATOM   641  C CA  . VAL A 1 87  ? -19.395 -11.813 17.274  1.00 12.73 ? 87  VAL A CA  1 
ATOM   642  C C   . VAL A 1 87  ? -20.887 -12.015 16.946  1.00 13.86 ? 87  VAL A C   1 
ATOM   643  O O   . VAL A 1 87  ? -21.631 -11.024 16.701  1.00 12.02 ? 87  VAL A O   1 
ATOM   644  C CB  . VAL A 1 87  ? -19.135 -11.876 18.820  1.00 12.74 ? 87  VAL A CB  1 
ATOM   645  C CG1 . VAL A 1 87  ? -17.684 -11.757 19.102  1.00 10.04 ? 87  VAL A CG1 1 
ATOM   646  C CG2 . VAL A 1 87  ? -19.935 -10.800 19.585  1.00 12.92 ? 87  VAL A CG2 1 
ATOM   647  N N   . THR A 1 88  ? -21.316 -13.283 16.958  1.00 13.72 ? 88  THR A N   1 
ATOM   648  C CA  . THR A 1 88  ? -22.650 -13.656 16.543  1.00 16.47 ? 88  THR A CA  1 
ATOM   649  C C   . THR A 1 88  ? -23.426 -14.228 17.698  1.00 17.39 ? 88  THR A C   1 
ATOM   650  O O   . THR A 1 88  ? -23.011 -15.234 18.274  1.00 19.04 ? 88  THR A O   1 
ATOM   651  C CB  . THR A 1 88  ? -22.567 -14.712 15.396  1.00 16.21 ? 88  THR A CB  1 
ATOM   652  O OG1 . THR A 1 88  ? -21.715 -14.213 14.357  1.00 15.10 ? 88  THR A OG1 1 
ATOM   653  C CG2 . THR A 1 88  ? -23.932 -15.001 14.802  1.00 17.29 ? 88  THR A CG2 1 
ATOM   654  N N   . ALA A 1 89  ? -24.533 -13.571 18.056  1.00 18.36 ? 89  ALA A N   1 
ATOM   655  C CA  . ALA A 1 89  ? -25.470 -14.039 19.103  1.00 18.82 ? 89  ALA A CA  1 
ATOM   656  C C   . ALA A 1 89  ? -26.451 -14.979 18.439  1.00 20.09 ? 89  ALA A C   1 
ATOM   657  O O   . ALA A 1 89  ? -27.092 -14.554 17.495  1.00 20.19 ? 89  ALA A O   1 
ATOM   658  C CB  . ALA A 1 89  ? -26.255 -12.845 19.668  1.00 17.23 ? 89  ALA A CB  1 
ATOM   659  N N   . ASP A 1 90  ? -26.598 -16.219 18.928  1.00 21.83 ? 90  ASP A N   1 
ATOM   660  C CA  . ASP A 1 90  ? -27.754 -17.059 18.549  1.00 22.74 ? 90  ASP A CA  1 
ATOM   661  C C   . ASP A 1 90  ? -29.068 -16.355 18.932  1.00 24.17 ? 90  ASP A C   1 
ATOM   662  O O   . ASP A 1 90  ? -29.046 -15.233 19.431  1.00 24.93 ? 90  ASP A O   1 
ATOM   663  C CB  . ASP A 1 90  ? -27.662 -18.491 19.144  1.00 22.46 ? 90  ASP A CB  1 
ATOM   664  C CG  . ASP A 1 90  ? -27.637 -18.513 20.676  1.00 21.50 ? 90  ASP A CG  1 
ATOM   665  O OD1 . ASP A 1 90  ? -28.024 -17.521 21.305  1.00 22.29 ? 90  ASP A OD1 1 
ATOM   666  O OD2 . ASP A 1 90  ? -27.249 -19.538 21.276  1.00 17.27 ? 90  ASP A OD2 1 
ATOM   667  N N   . LYS A 1 91  ? -30.202 -16.991 18.662  1.00 25.69 ? 91  LYS A N   1 
ATOM   668  C CA  . LYS A 1 91  ? -31.520 -16.441 18.993  1.00 26.00 ? 91  LYS A CA  1 
ATOM   669  C C   . LYS A 1 91  ? -31.855 -16.448 20.493  1.00 26.55 ? 91  LYS A C   1 
ATOM   670  O O   . LYS A 1 91  ? -32.799 -15.775 20.912  1.00 25.90 ? 91  LYS A O   1 
ATOM   671  C CB  . LYS A 1 91  ? -32.608 -17.184 18.193  1.00 26.90 ? 91  LYS A CB  1 
ATOM   672  C CG  . LYS A 1 91  ? -32.836 -18.653 18.630  1.00 27.54 ? 91  LYS A CG  1 
ATOM   673  C CD  . LYS A 1 91  ? -31.772 -19.607 18.123  1.00 28.52 ? 91  LYS A CD  1 
ATOM   674  C CE  . LYS A 1 91  ? -31.810 -20.976 18.876  1.00 28.78 ? 91  LYS A CE  1 
ATOM   675  N NZ  . LYS A 1 91  ? -33.177 -21.639 18.916  1.00 28.89 ? 91  LYS A NZ  1 
ATOM   676  N N   . ASP A 1 92  ? -31.108 -17.237 21.282  1.00 25.80 ? 92  ASP A N   1 
ATOM   677  C CA  . ASP A 1 92  ? -31.063 -17.114 22.758  1.00 26.23 ? 92  ASP A CA  1 
ATOM   678  C C   . ASP A 1 92  ? -30.112 -16.034 23.329  1.00 25.56 ? 92  ASP A C   1 
ATOM   679  O O   . ASP A 1 92  ? -29.936 -15.952 24.541  1.00 25.47 ? 92  ASP A O   1 
ATOM   680  C CB  . ASP A 1 92  ? -30.765 -18.482 23.402  1.00 26.00 ? 92  ASP A CB  1 
ATOM   681  C CG  . ASP A 1 92  ? -31.714 -19.540 22.929  1.00 28.32 ? 92  ASP A CG  1 
ATOM   682  O OD1 . ASP A 1 92  ? -32.904 -19.177 22.750  1.00 29.68 ? 92  ASP A OD1 1 
ATOM   683  O OD2 . ASP A 1 92  ? -31.288 -20.704 22.706  1.00 25.67 ? 92  ASP A OD2 1 
ATOM   684  N N   . GLY A 1 93  ? -29.553 -15.186 22.460  1.00 25.58 ? 93  GLY A N   1 
ATOM   685  C CA  . GLY A 1 93  ? -28.739 -14.024 22.863  1.00 24.21 ? 93  GLY A CA  1 
ATOM   686  C C   . GLY A 1 93  ? -27.274 -14.290 23.219  1.00 23.26 ? 93  GLY A C   1 
ATOM   687  O O   . GLY A 1 93  ? -26.556 -13.353 23.478  1.00 21.51 ? 93  GLY A O   1 
ATOM   688  N N   . VAL A 1 94  ? -26.867 -15.566 23.201  1.00 22.24 ? 94  VAL A N   1 
ATOM   689  C CA  . VAL A 1 94  ? -25.538 -16.080 23.555  1.00 22.19 ? 94  VAL A CA  1 
ATOM   690  C C   . VAL A 1 94  ? -24.561 -16.136 22.353  1.00 23.13 ? 94  VAL A C   1 
ATOM   691  O O   . VAL A 1 94  ? -24.895 -16.686 21.275  1.00 23.79 ? 94  VAL A O   1 
ATOM   692  C CB  . VAL A 1 94  ? -25.637 -17.498 24.200  1.00 21.34 ? 94  VAL A CB  1 
ATOM   693  C CG1 . VAL A 1 94  ? -24.251 -18.086 24.556  1.00 22.12 ? 94  VAL A CG1 1 
ATOM   694  C CG2 . VAL A 1 94  ? -26.485 -17.450 25.450  1.00 20.79 ? 94  VAL A CG2 1 
ATOM   695  N N   . ALA A 1 95  ? -23.362 -15.556 22.538  1.00 23.24 ? 95  ALA A N   1 
ATOM   696  C CA  . ALA A 1 95  ? -22.383 -15.437 21.468  1.00 21.91 ? 95  ALA A CA  1 
ATOM   697  C C   . ALA A 1 95  ? -21.166 -16.170 21.909  1.00 22.88 ? 95  ALA A C   1 
ATOM   698  O O   . ALA A 1 95  ? -20.400 -15.697 22.734  1.00 23.47 ? 95  ALA A O   1 
ATOM   699  C CB  . ALA A 1 95  ? -22.071 -14.015 21.217  1.00 22.32 ? 95  ALA A CB  1 
ATOM   700  N N   . ASP A 1 96  ? -20.974 -17.371 21.402  1.00 23.17 ? 96  ASP A N   1 
ATOM   701  C CA  . ASP A 1 96  ? -19.758 -18.035 21.718  1.00 23.21 ? 96  ASP A CA  1 
ATOM   702  C C   . ASP A 1 96  ? -18.614 -17.599 20.808  1.00 22.79 ? 96  ASP A C   1 
ATOM   703  O O   . ASP A 1 96  ? -18.656 -17.754 19.584  1.00 22.83 ? 96  ASP A O   1 
ATOM   704  C CB  . ASP A 1 96  ? -19.968 -19.543 21.835  1.00 24.62 ? 96  ASP A CB  1 
ATOM   705  C CG  . ASP A 1 96  ? -20.218 -19.940 23.278  1.00 27.56 ? 96  ASP A CG  1 
ATOM   706  O OD1 . ASP A 1 96  ? -21.389 -19.835 23.755  1.00 27.62 ? 96  ASP A OD1 1 
ATOM   707  O OD2 . ASP A 1 96  ? -19.191 -20.235 23.965  1.00 32.48 ? 96  ASP A OD2 1 
ATOM   708  N N   . VAL A 1 97  ? -17.626 -16.964 21.425  1.00 22.25 ? 97  VAL A N   1 
ATOM   709  C CA  . VAL A 1 97  ? -16.531 -16.291 20.694  1.00 19.99 ? 97  VAL A CA  1 
ATOM   710  C C   . VAL A 1 97  ? -15.354 -17.255 20.583  1.00 20.78 ? 97  VAL A C   1 
ATOM   711  O O   . VAL A 1 97  ? -14.977 -17.903 21.527  1.00 18.64 ? 97  VAL A O   1 
ATOM   712  C CB  . VAL A 1 97  ? -16.147 -14.971 21.397  1.00 20.29 ? 97  VAL A CB  1 
ATOM   713  C CG1 . VAL A 1 97  ? -14.970 -14.320 20.775  1.00 19.11 ? 97  VAL A CG1 1 
ATOM   714  C CG2 . VAL A 1 97  ? -17.348 -14.024 21.405  1.00 12.91 ? 97  VAL A CG2 1 
ATOM   715  N N   . SER A 1 98  ? -14.767 -17.352 19.405  1.00 22.27 ? 98  SER A N   1 
ATOM   716  C CA  . SER A 1 98  ? -13.543 -18.126 19.279  1.00 23.59 ? 98  SER A CA  1 
ATOM   717  C C   . SER A 1 98  ? -12.760 -17.567 18.109  1.00 24.08 ? 98  SER A C   1 
ATOM   718  O O   . SER A 1 98  ? -12.924 -18.037 16.999  1.00 25.16 ? 98  SER A O   1 
ATOM   719  C CB  . SER A 1 98  ? -13.866 -19.591 19.053  1.00 23.03 ? 98  SER A CB  1 
ATOM   720  O OG  . SER A 1 98  ? -12.678 -20.330 19.190  1.00 26.51 ? 98  SER A OG  1 
ATOM   721  N N   . ILE A 1 99  ? -11.978 -16.514 18.365  1.00 24.36 ? 99  ILE A N   1 
ATOM   722  C CA  . ILE A 1 99  ? -11.278 -15.695 17.359  1.00 22.92 ? 99  ILE A CA  1 
ATOM   723  C C   . ILE A 1 99  ? -9.788  -16.093 17.416  1.00 22.98 ? 99  ILE A C   1 
ATOM   724  O O   . ILE A 1 99  ? -9.299  -16.650 18.426  1.00 22.76 ? 99  ILE A O   1 
ATOM   725  C CB  . ILE A 1 99  ? -11.391 -14.157 17.744  1.00 23.99 ? 99  ILE A CB  1 
ATOM   726  C CG1 . ILE A 1 99  ? -12.805 -13.594 17.497  1.00 24.50 ? 99  ILE A CG1 1 
ATOM   727  C CG2 . ILE A 1 99  ? -10.457 -13.273 16.995  1.00 22.25 ? 99  ILE A CG2 1 
ATOM   728  C CD1 . ILE A 1 99  ? -13.000 -12.245 18.062  1.00 23.34 ? 99  ILE A CD1 1 
ATOM   729  N N   . GLU A 1 100 ? -9.056  -15.813 16.355  1.00 21.74 ? 100 GLU A N   1 
ATOM   730  C CA  . GLU A 1 100 ? -7.606  -15.836 16.434  1.00 21.88 ? 100 GLU A CA  1 
ATOM   731  C C   . GLU A 1 100 ? -7.113  -14.632 15.686  1.00 19.94 ? 100 GLU A C   1 
ATOM   732  O O   . GLU A 1 100 ? -7.420  -14.525 14.529  1.00 19.98 ? 100 GLU A O   1 
ATOM   733  C CB  . GLU A 1 100 ? -7.092  -17.089 15.790  1.00 21.34 ? 100 GLU A CB  1 
ATOM   734  C CG  . GLU A 1 100 ? -5.642  -17.384 16.046  1.00 27.51 ? 100 GLU A CG  1 
ATOM   735  C CD  . GLU A 1 100 ? -5.346  -18.877 15.808  1.00 29.68 ? 100 GLU A CD  1 
ATOM   736  O OE1 . GLU A 1 100 ? -6.122  -19.730 16.297  1.00 31.66 ? 100 GLU A OE1 1 
ATOM   737  O OE2 . GLU A 1 100 ? -4.331  -19.174 15.145  1.00 32.01 ? 100 GLU A OE2 1 
ATOM   738  N N   . ASP A 1 101 ? -6.392  -13.720 16.346  1.00 19.48 ? 101 ASP A N   1 
ATOM   739  C CA  . ASP A 1 101 ? -5.878  -12.489 15.709  1.00 18.60 ? 101 ASP A CA  1 
ATOM   740  C C   . ASP A 1 101 ? -4.320  -12.280 15.798  1.00 17.71 ? 101 ASP A C   1 
ATOM   741  O O   . ASP A 1 101 ? -3.671  -12.504 16.831  1.00 17.48 ? 101 ASP A O   1 
ATOM   742  C CB  . ASP A 1 101 ? -6.598  -11.254 16.252  1.00 18.14 ? 101 ASP A CB  1 
ATOM   743  C CG  . ASP A 1 101 ? -6.504  -10.076 15.325  1.00 20.54 ? 101 ASP A CG  1 
ATOM   744  O OD1 . ASP A 1 101 ? -7.257  -9.987  14.312  1.00 25.60 ? 101 ASP A OD1 1 
ATOM   745  O OD2 . ASP A 1 101 ? -5.656  -9.226  15.584  1.00 19.51 ? 101 ASP A OD2 1 
ATOM   746  N N   . SER A 1 102 ? -3.729  -11.807 14.718  1.00 16.53 ? 102 SER A N   1 
ATOM   747  C CA  . SER A 1 102 ? -2.303  -11.641 14.641  1.00 15.85 ? 102 SER A CA  1 
ATOM   748  C C   . SER A 1 102 ? -1.898  -10.186 14.534  1.00 16.27 ? 102 SER A C   1 
ATOM   749  O O   . SER A 1 102 ? -0.736  -9.923  14.243  1.00 16.57 ? 102 SER A O   1 
ATOM   750  C CB  . SER A 1 102 ? -1.737  -12.417 13.465  1.00 16.25 ? 102 SER A CB  1 
ATOM   751  O OG  . SER A 1 102 ? -1.706  -13.815 13.752  1.00 21.68 ? 102 SER A OG  1 
ATOM   752  N N   . VAL A 1 103 ? -2.820  -9.259  14.823  1.00 13.65 ? 103 VAL A N   1 
ATOM   753  C CA  . VAL A 1 103 ? -2.511  -7.792  14.848  1.00 12.97 ? 103 VAL A CA  1 
ATOM   754  C C   . VAL A 1 103 ? -2.507  -7.297  16.310  1.00 12.31 ? 103 VAL A C   1 
ATOM   755  O O   . VAL A 1 103 ? -1.624  -6.589  16.725  1.00 14.23 ? 103 VAL A O   1 
ATOM   756  C CB  . VAL A 1 103 ? -3.520  -7.104  14.015  1.00 13.41 ? 103 VAL A CB  1 
ATOM   757  C CG1 . VAL A 1 103 ? -3.232  -5.598  13.863  1.00 7.24  ? 103 VAL A CG1 1 
ATOM   758  C CG2 . VAL A 1 103 ? -3.513  -7.788  12.658  1.00 8.73  ? 103 VAL A CG2 1 
ATOM   759  N N   . ILE A 1 104 ? -3.426  -7.795  17.129  1.00 12.82 ? 104 ILE A N   1 
ATOM   760  C CA  . ILE A 1 104 ? -3.425  -7.467  18.555  1.00 12.19 ? 104 ILE A CA  1 
ATOM   761  C C   . ILE A 1 104 ? -2.268  -8.171  19.130  1.00 12.62 ? 104 ILE A C   1 
ATOM   762  O O   . ILE A 1 104 ? -1.809  -9.150  18.530  1.00 11.40 ? 104 ILE A O   1 
ATOM   763  C CB  . ILE A 1 104 ? -4.771  -7.859  19.280  1.00 11.51 ? 104 ILE A CB  1 
ATOM   764  C CG1 . ILE A 1 104 ? -5.185  -9.312  18.926  1.00 11.78 ? 104 ILE A CG1 1 
ATOM   765  C CG2 . ILE A 1 104 ? -5.792  -6.943  18.878  1.00 11.83 ? 104 ILE A CG2 1 
ATOM   766  C CD1 . ILE A 1 104 ? -6.394  -9.837  19.699  1.00 11.18 ? 104 ILE A CD1 1 
ATOM   767  N N   . SER A 1 105 ? -1.837  -7.766  20.325  1.00 12.87 ? 105 SER A N   1 
ATOM   768  C CA  . SER A 1 105 ? -0.819  -8.529  21.034  1.00 13.32 ? 105 SER A CA  1 
ATOM   769  C C   . SER A 1 105 ? -0.960  -8.402  22.536  1.00 13.36 ? 105 SER A C   1 
ATOM   770  O O   . SER A 1 105 ? -1.552  -7.441  23.014  1.00 13.50 ? 105 SER A O   1 
ATOM   771  C CB  . SER A 1 105 ? 0.575   -8.074  20.592  1.00 13.32 ? 105 SER A CB  1 
ATOM   772  O OG  . SER A 1 105 ? 1.508   -9.067  20.945  1.00 17.88 ? 105 SER A OG  1 
ATOM   773  N N   . LEU A 1 106 ? -0.405  -9.346  23.292  1.00 12.94 ? 106 LEU A N   1 
ATOM   774  C CA  . LEU A 1 106 ? -0.311  -9.178  24.741  1.00 14.17 ? 106 LEU A CA  1 
ATOM   775  C C   . LEU A 1 106 ? 1.009   -8.539  25.127  1.00 15.18 ? 106 LEU A C   1 
ATOM   776  O O   . LEU A 1 106 ? 1.213   -8.310  26.292  1.00 16.80 ? 106 LEU A O   1 
ATOM   777  C CB  . LEU A 1 106 ? -0.512  -10.508 25.528  1.00 13.88 ? 106 LEU A CB  1 
ATOM   778  C CG  . LEU A 1 106 ? -1.668  -11.412 25.081  1.00 13.56 ? 106 LEU A CG  1 
ATOM   779  C CD1 . LEU A 1 106 ? -1.881  -12.638 25.883  1.00 5.04  ? 106 LEU A CD1 1 
ATOM   780  C CD2 . LEU A 1 106 ? -2.962  -10.609 25.123  1.00 13.65 ? 106 LEU A CD2 1 
ATOM   781  N N   . SER A 1 107 ? 1.906   -8.263  24.166  1.00 16.71 ? 107 SER A N   1 
ATOM   782  C CA  . SER A 1 107 ? 3.231   -7.647  24.423  1.00 18.83 ? 107 SER A CA  1 
ATOM   783  C C   . SER A 1 107 ? 3.497   -6.539  23.451  1.00 18.19 ? 107 SER A C   1 
ATOM   784  O O   . SER A 1 107 ? 2.837   -6.470  22.472  1.00 20.40 ? 107 SER A O   1 
ATOM   785  C CB  . SER A 1 107 ? 4.376   -8.682  24.348  1.00 17.85 ? 107 SER A CB  1 
ATOM   786  O OG  . SER A 1 107 ? 4.212   -9.627  23.308  1.00 23.46 ? 107 SER A OG  1 
ATOM   787  N N   . GLY A 1 108 ? 4.443   -5.648  23.691  1.00 19.13 ? 108 GLY A N   1 
ATOM   788  C CA  . GLY A 1 108 ? 4.825   -4.681  22.613  1.00 18.99 ? 108 GLY A CA  1 
ATOM   789  C C   . GLY A 1 108 ? 3.995   -3.449  22.267  1.00 19.52 ? 108 GLY A C   1 
ATOM   790  O O   . GLY A 1 108 ? 3.120   -3.085  23.007  1.00 19.47 ? 108 GLY A O   1 
ATOM   791  N N   . ASP A 1 109 ? 4.278   -2.821  21.133  1.00 18.28 ? 109 ASP A N   1 
ATOM   792  C CA  . ASP A 1 109 ? 3.582   -1.582  20.715  1.00 20.16 ? 109 ASP A CA  1 
ATOM   793  C C   . ASP A 1 109 ? 2.017   -1.724  20.604  1.00 19.07 ? 109 ASP A C   1 
ATOM   794  O O   . ASP A 1 109 ? 1.250   -0.744  20.842  1.00 18.85 ? 109 ASP A O   1 
ATOM   795  C CB  . ASP A 1 109 ? 4.145   -1.129  19.359  1.00 20.78 ? 109 ASP A CB  1 
ATOM   796  C CG  . ASP A 1 109 ? 5.504   -0.381  19.487  1.00 25.19 ? 109 ASP A CG  1 
ATOM   797  O OD1 . ASP A 1 109 ? 6.132   -0.068  18.446  1.00 29.48 ? 109 ASP A OD1 1 
ATOM   798  O OD2 . ASP A 1 109 ? 5.907   -0.053  20.605  1.00 28.38 ? 109 ASP A OD2 1 
ATOM   799  N N   . HIS A 1 110 ? 1.608   -2.947  20.230  1.00 17.64 ? 110 HIS A N   1 
ATOM   800  C CA  . HIS A 1 110 ? 0.225   -3.332  19.921  1.00 16.21 ? 110 HIS A CA  1 
ATOM   801  C C   . HIS A 1 110 ? -0.341  -4.186  21.055  1.00 15.12 ? 110 HIS A C   1 
ATOM   802  O O   . HIS A 1 110 ? -1.357  -4.852  20.853  1.00 16.46 ? 110 HIS A O   1 
ATOM   803  C CB  . HIS A 1 110 ? 0.151   -4.104  18.596  1.00 16.90 ? 110 HIS A CB  1 
ATOM   804  C CG  . HIS A 1 110 ? 0.392   -3.264  17.367  1.00 16.26 ? 110 HIS A CG  1 
ATOM   805  N ND1 . HIS A 1 110 ? 0.508   -3.807  16.100  1.00 15.21 ? 110 HIS A ND1 1 
ATOM   806  C CD2 . HIS A 1 110 ? 0.581   -1.930  17.219  1.00 17.04 ? 110 HIS A CD2 1 
ATOM   807  C CE1 . HIS A 1 110 ? 0.706   -2.838  15.225  1.00 12.41 ? 110 HIS A CE1 1 
ATOM   808  N NE2 . HIS A 1 110 ? 0.772   -1.690  15.882  1.00 12.39 ? 110 HIS A NE2 1 
ATOM   809  N N   . CYS A 1 111 ? 0.315   -4.165  22.227  1.00 12.58 ? 111 CYS A N   1 
ATOM   810  C CA  . CYS A 1 111 ? -0.255  -4.628  23.493  1.00 10.89 ? 111 CYS A CA  1 
ATOM   811  C C   . CYS A 1 111 ? -1.626  -4.074  23.888  1.00 9.36  ? 111 CYS A C   1 
ATOM   812  O O   . CYS A 1 111 ? -1.857  -2.856  23.995  1.00 5.41  ? 111 CYS A O   1 
ATOM   813  C CB  . CYS A 1 111 ? 0.693   -4.325  24.662  1.00 13.12 ? 111 CYS A CB  1 
ATOM   814  S SG  . CYS A 1 111 ? 0.251   -5.079  26.189  1.00 13.76 ? 111 CYS A SG  1 
ATOM   815  N N   . ILE A 1 112 ? -2.542  -4.978  24.115  1.00 3.16  ? 112 ILE A N   1 
ATOM   816  C CA  . ILE A 1 112 ? -3.897  -4.496  24.520  1.00 3.94  ? 112 ILE A CA  1 
ATOM   817  C C   . ILE A 1 112 ? -4.199  -4.732  26.009  1.00 2.78  ? 112 ILE A C   1 
ATOM   818  O O   . ILE A 1 112 ? -5.323  -4.623  26.428  1.00 3.52  ? 112 ILE A O   1 
ATOM   819  C CB  . ILE A 1 112 ? -4.936  -5.215  23.717  1.00 2.90  ? 112 ILE A CB  1 
ATOM   820  C CG1 . ILE A 1 112 ? -4.653  -6.726  23.923  1.00 2.19  ? 112 ILE A CG1 1 
ATOM   821  C CG2 . ILE A 1 112 ? -4.714  -4.903  22.251  1.00 2.19  ? 112 ILE A CG2 1 
ATOM   822  C CD1 . ILE A 1 112 ? -5.759  -7.791  23.527  1.00 6.61  ? 112 ILE A CD1 1 
ATOM   823  N N   . ILE A 1 113 ? -3.219  -5.096  26.830  1.00 4.28  ? 113 ILE A N   1 
ATOM   824  C CA  . ILE A 1 113 ? -3.509  -5.453  28.224  1.00 2.92  ? 113 ILE A CA  1 
ATOM   825  C C   . ILE A 1 113 ? -3.688  -4.043  28.770  1.00 5.29  ? 113 ILE A C   1 
ATOM   826  O O   . ILE A 1 113 ? -2.880  -3.224  28.435  1.00 3.74  ? 113 ILE A O   1 
ATOM   827  C CB  . ILE A 1 113 ? -2.258  -5.920  28.833  1.00 4.13  ? 113 ILE A CB  1 
ATOM   828  C CG1 . ILE A 1 113 ? -2.022  -7.395  28.409  1.00 9.65  ? 113 ILE A CG1 1 
ATOM   829  C CG2 . ILE A 1 113 ? -2.241  -5.691  30.403  1.00 2.76  ? 113 ILE A CG2 1 
ATOM   830  C CD1 . ILE A 1 113 ? -3.223  -8.088  28.167  1.00 8.53  ? 113 ILE A CD1 1 
ATOM   831  N N   . GLY A 1 114 ? -4.674  -3.803  29.593  1.00 5.54  ? 114 GLY A N   1 
ATOM   832  C CA  . GLY A 1 114 ? -4.926  -2.408  30.095  1.00 5.49  ? 114 GLY A CA  1 
ATOM   833  C C   . GLY A 1 114 ? -5.734  -1.517  29.178  1.00 7.38  ? 114 GLY A C   1 
ATOM   834  O O   . GLY A 1 114 ? -5.875  -0.230  29.402  1.00 7.92  ? 114 GLY A O   1 
ATOM   835  N N   . ARG A 1 115 ? -6.219  -2.075  28.077  1.00 4.47  ? 115 ARG A N   1 
ATOM   836  C CA  . ARG A 1 115 ? -7.128  -1.321  27.291  1.00 4.16  ? 115 ARG A CA  1 
ATOM   837  C C   . ARG A 1 115 ? -8.458  -2.008  27.500  1.00 2.00  ? 115 ARG A C   1 
ATOM   838  O O   . ARG A 1 115 ? -8.617  -2.629  28.482  1.00 3.03  ? 115 ARG A O   1 
ATOM   839  C CB  . ARG A 1 115 ? -6.693  -1.081  25.834  1.00 2.00  ? 115 ARG A CB  1 
ATOM   840  C CG  . ARG A 1 115 ? -5.176  -0.581  25.779  1.00 2.00  ? 115 ARG A CG  1 
ATOM   841  C CD  . ARG A 1 115 ? -4.727  -0.694  24.343  1.00 2.32  ? 115 ARG A CD  1 
ATOM   842  N NE  . ARG A 1 115 ? -3.360  -0.274  24.229  1.00 5.84  ? 115 ARG A NE  1 
ATOM   843  C CZ  . ARG A 1 115 ? -2.995  1.013   24.432  1.00 7.58  ? 115 ARG A CZ  1 
ATOM   844  N NH1 . ARG A 1 115 ? -3.924  1.873   24.740  1.00 9.39  ? 115 ARG A NH1 1 
ATOM   845  N NH2 . ARG A 1 115 ? -1.712  1.414   24.318  1.00 7.39  ? 115 ARG A NH2 1 
ATOM   846  N N   . THR A 1 116 ? -9.430  -1.810  26.642  1.00 4.26  ? 116 THR A N   1 
ATOM   847  C CA  . THR A 1 116 ? -10.837 -2.065  27.012  1.00 4.40  ? 116 THR A CA  1 
ATOM   848  C C   . THR A 1 116 ? -11.416 -2.775  25.857  1.00 5.28  ? 116 THR A C   1 
ATOM   849  O O   . THR A 1 116 ? -11.385 -2.297  24.770  1.00 4.33  ? 116 THR A O   1 
ATOM   850  C CB  . THR A 1 116 ? -11.578 -0.681  27.211  1.00 3.58  ? 116 THR A CB  1 
ATOM   851  O OG1 . THR A 1 116 ? -11.239 -0.210  28.500  1.00 5.61  ? 116 THR A OG1 1 
ATOM   852  C CG2 . THR A 1 116 ? -13.166 -0.862  27.290  1.00 2.75  ? 116 THR A CG2 1 
ATOM   853  N N   . LEU A 1 117 ? -11.936 -3.982  26.069  1.00 6.84  ? 117 LEU A N   1 
ATOM   854  C CA  . LEU A 1 117 ? -12.661 -4.610  25.051  1.00 5.71  ? 117 LEU A CA  1 
ATOM   855  C C   . LEU A 1 117 ? -14.144 -4.212  25.138  1.00 7.66  ? 117 LEU A C   1 
ATOM   856  O O   . LEU A 1 117 ? -14.698 -4.198  26.231  1.00 6.77  ? 117 LEU A O   1 
ATOM   857  C CB  . LEU A 1 117 ? -12.528 -6.132  25.328  1.00 4.32  ? 117 LEU A CB  1 
ATOM   858  C CG  . LEU A 1 117 ? -13.226 -6.934  24.290  1.00 4.55  ? 117 LEU A CG  1 
ATOM   859  C CD1 . LEU A 1 117 ? -12.492 -6.826  22.982  1.00 2.00  ? 117 LEU A CD1 1 
ATOM   860  C CD2 . LEU A 1 117 ? -13.178 -8.432  24.836  1.00 2.00  ? 117 LEU A CD2 1 
ATOM   861  N N   . VAL A 1 118 ? -14.781 -3.943  24.003  1.00 8.12  ? 118 VAL A N   1 
ATOM   862  C CA  . VAL A 1 118 ? -16.177 -3.486  23.932  1.00 9.57  ? 118 VAL A CA  1 
ATOM   863  C C   . VAL A 1 118 ? -16.970 -4.304  22.938  1.00 9.92  ? 118 VAL A C   1 
ATOM   864  O O   . VAL A 1 118 ? -16.489 -4.577  21.869  1.00 8.69  ? 118 VAL A O   1 
ATOM   865  C CB  . VAL A 1 118 ? -16.294 -2.025  23.408  1.00 8.16  ? 118 VAL A CB  1 
ATOM   866  C CG1 . VAL A 1 118 ? -17.702 -1.628  23.480  1.00 14.25 ? 118 VAL A CG1 1 
ATOM   867  C CG2 . VAL A 1 118 ? -15.575 -1.042  24.259  1.00 7.13  ? 118 VAL A CG2 1 
ATOM   868  N N   . VAL A 1 119 ? -18.232 -4.646  23.264  1.00 12.78 ? 119 VAL A N   1 
ATOM   869  C CA  . VAL A 1 119 ? -19.130 -5.302  22.316  1.00 13.00 ? 119 VAL A CA  1 
ATOM   870  C C   . VAL A 1 119 ? -20.161 -4.265  21.991  1.00 13.81 ? 119 VAL A C   1 
ATOM   871  O O   . VAL A 1 119 ? -20.720 -3.617  22.901  1.00 15.48 ? 119 VAL A O   1 
ATOM   872  C CB  . VAL A 1 119 ? -19.767 -6.655  22.914  1.00 13.77 ? 119 VAL A CB  1 
ATOM   873  C CG1 . VAL A 1 119 ? -20.540 -6.458  24.241  1.00 7.84  ? 119 VAL A CG1 1 
ATOM   874  C CG2 . VAL A 1 119 ? -20.579 -7.455  21.873  1.00 13.83 ? 119 VAL A CG2 1 
ATOM   875  N N   . HIS A 1 120 ? -20.436 -4.052  20.715  1.00 13.15 ? 120 HIS A N   1 
ATOM   876  C CA  . HIS A 1 120 ? -21.379 -2.976  20.445  1.00 13.72 ? 120 HIS A CA  1 
ATOM   877  C C   . HIS A 1 120 ? -22.815 -3.448  20.177  1.00 14.62 ? 120 HIS A C   1 
ATOM   878  O O   . HIS A 1 120 ? -23.122 -4.676  20.026  1.00 13.74 ? 120 HIS A O   1 
ATOM   879  C CB  . HIS A 1 120 ? -20.879 -2.121  19.301  1.00 11.27 ? 120 HIS A CB  1 
ATOM   880  C CG  . HIS A 1 120 ? -19.668 -1.332  19.615  1.00 5.96  ? 120 HIS A CG  1 
ATOM   881  N ND1 . HIS A 1 120 ? -19.716 0.040   19.730  1.00 2.00  ? 120 HIS A ND1 1 
ATOM   882  C CD2 . HIS A 1 120 ? -18.372 -1.670  19.754  1.00 4.65  ? 120 HIS A CD2 1 
ATOM   883  C CE1 . HIS A 1 120 ? -18.513 0.502   20.004  1.00 4.89  ? 120 HIS A CE1 1 
ATOM   884  N NE2 . HIS A 1 120 ? -17.679 -0.512  20.031  1.00 9.84  ? 120 HIS A NE2 1 
ATOM   885  N N   . GLU A 1 121 ? -23.658 -2.409  20.074  1.00 15.51 ? 121 GLU A N   1 
ATOM   886  C CA  . GLU A 1 121 ? -25.091 -2.473  19.803  1.00 17.19 ? 121 GLU A CA  1 
ATOM   887  C C   . GLU A 1 121 ? -25.417 -3.273  18.523  1.00 18.07 ? 121 GLU A C   1 
ATOM   888  O O   . GLU A 1 121 ? -26.158 -4.263  18.577  1.00 17.46 ? 121 GLU A O   1 
ATOM   889  C CB  . GLU A 1 121 ? -25.613 -1.057  19.701  1.00 16.32 ? 121 GLU A CB  1 
ATOM   890  C CG  . GLU A 1 121 ? -27.085 -0.948  19.538  1.00 20.86 ? 121 GLU A CG  1 
ATOM   891  C CD  . GLU A 1 121 ? -27.548 0.442   19.149  1.00 25.30 ? 121 GLU A CD  1 
ATOM   892  O OE1 . GLU A 1 121 ? -28.768 0.596   18.988  1.00 30.05 ? 121 GLU A OE1 1 
ATOM   893  O OE2 . GLU A 1 121 ? -26.746 1.374   18.945  1.00 24.60 ? 121 GLU A OE2 1 
ATOM   894  N N   . LYS A 1 122 ? -24.811 -2.847  17.405  1.00 19.02 ? 122 LYS A N   1 
ATOM   895  C CA  . LYS A 1 122 ? -25.087 -3.334  16.028  1.00 20.60 ? 122 LYS A CA  1 
ATOM   896  C C   . LYS A 1 122 ? -23.888 -3.986  15.409  1.00 20.47 ? 122 LYS A C   1 
ATOM   897  O O   . LYS A 1 122 ? -22.741 -3.793  15.894  1.00 20.64 ? 122 LYS A O   1 
ATOM   898  C CB  . LYS A 1 122 ? -25.391 -2.128  15.121  1.00 21.19 ? 122 LYS A CB  1 
ATOM   899  C CG  . LYS A 1 122 ? -26.130 -0.968  15.761  1.00 20.08 ? 122 LYS A CG  1 
ATOM   900  C CD  . LYS A 1 122 ? -26.646 0.012   14.735  1.00 22.68 ? 122 LYS A CD  1 
ATOM   901  C CE  . LYS A 1 122 ? -26.966 -0.664  13.375  1.00 27.38 ? 122 LYS A CE  1 
ATOM   902  N NZ  . LYS A 1 122 ? -28.328 -0.242  12.774  1.00 30.09 ? 122 LYS A NZ  1 
ATOM   903  N N   . ALA A 1 123 ? -24.127 -4.705  14.311  1.00 19.35 ? 123 ALA A N   1 
ATOM   904  C CA  . ALA A 1 123 ? -23.060 -5.225  13.474  1.00 18.90 ? 123 ALA A CA  1 
ATOM   905  C C   . ALA A 1 123 ? -22.094 -4.146  13.120  1.00 18.56 ? 123 ALA A C   1 
ATOM   906  O O   . ALA A 1 123 ? -22.451 -2.942  12.995  1.00 19.35 ? 123 ALA A O   1 
ATOM   907  C CB  . ALA A 1 123 ? -23.597 -5.850  12.230  1.00 18.75 ? 123 ALA A CB  1 
ATOM   908  N N   . ASP A 1 124 ? -20.828 -4.553  13.045  1.00 18.12 ? 124 ASP A N   1 
ATOM   909  C CA  . ASP A 1 124 ? -19.791 -3.721  12.458  1.00 17.40 ? 124 ASP A CA  1 
ATOM   910  C C   . ASP A 1 124 ? -19.957 -3.943  10.916  1.00 16.69 ? 124 ASP A C   1 
ATOM   911  O O   . ASP A 1 124 ? -19.986 -5.099  10.442  1.00 16.44 ? 124 ASP A O   1 
ATOM   912  C CB  . ASP A 1 124 ? -18.398 -4.149  12.988  1.00 17.15 ? 124 ASP A CB  1 
ATOM   913  C CG  . ASP A 1 124 ? -17.233 -3.374  12.342  1.00 14.62 ? 124 ASP A CG  1 
ATOM   914  O OD1 . ASP A 1 124 ? -17.437 -2.339  11.693  1.00 18.18 ? 124 ASP A OD1 1 
ATOM   915  O OD2 . ASP A 1 124 ? -16.057 -3.735  12.545  1.00 17.45 ? 124 ASP A OD2 1 
ATOM   916  N N   . ASP A 1 125 ? -20.137 -2.860  10.145  1.00 14.47 ? 125 ASP A N   1 
ATOM   917  C CA  . ASP A 1 125 ? -20.173 -3.025  8.679   1.00 13.64 ? 125 ASP A CA  1 
ATOM   918  C C   . ASP A 1 125 ? -18.832 -3.191  8.054   1.00 13.58 ? 125 ASP A C   1 
ATOM   919  O O   . ASP A 1 125 ? -18.742 -3.311  6.855   1.00 15.11 ? 125 ASP A O   1 
ATOM   920  C CB  . ASP A 1 125 ? -20.905 -1.899  8.002   1.00 12.33 ? 125 ASP A CB  1 
ATOM   921  C CG  . ASP A 1 125 ? -20.155 -0.648  8.012   1.00 15.93 ? 125 ASP A CG  1 
ATOM   922  O OD1 . ASP A 1 125 ? -18.900 -0.739  8.061   1.00 19.23 ? 125 ASP A OD1 1 
ATOM   923  O OD2 . ASP A 1 125 ? -20.844 0.409   7.915   1.00 12.51 ? 125 ASP A OD2 1 
ATOM   924  N N   . LEU A 1 126 ? -17.776 -3.234  8.849   1.00 13.67 ? 126 LEU A N   1 
ATOM   925  C CA  . LEU A 1 126 ? -16.376 -3.560  8.385   1.00 12.92 ? 126 LEU A CA  1 
ATOM   926  C C   . LEU A 1 126 ? -15.712 -2.577  7.450   1.00 14.05 ? 126 LEU A C   1 
ATOM   927  O O   . LEU A 1 126 ? -14.797 -2.967  6.737   1.00 14.73 ? 126 LEU A O   1 
ATOM   928  C CB  . LEU A 1 126 ? -16.157 -4.982  7.871   1.00 11.37 ? 126 LEU A CB  1 
ATOM   929  C CG  . LEU A 1 126 ? -16.826 -6.092  8.670   1.00 7.32  ? 126 LEU A CG  1 
ATOM   930  C CD1 . LEU A 1 126 ? -16.826 -7.362  7.800   1.00 11.79 ? 126 LEU A CD1 1 
ATOM   931  C CD2 . LEU A 1 126 ? -16.114 -6.356  9.923   1.00 2.98  ? 126 LEU A CD2 1 
ATOM   932  N N   . GLY A 1 127 ? -16.084 -1.313  7.540   1.00 16.09 ? 127 GLY A N   1 
ATOM   933  C CA  . GLY A 1 127 ? -15.627 -0.333  6.565   1.00 17.71 ? 127 GLY A CA  1 
ATOM   934  C C   . GLY A 1 127 ? -16.313 -0.462  5.186   1.00 19.76 ? 127 GLY A C   1 
ATOM   935  O O   . GLY A 1 127 ? -16.036 0.325   4.279   1.00 20.20 ? 127 GLY A O   1 
ATOM   936  N N   . LYS A 1 128 ? -17.182 -1.460  5.026   1.00 20.47 ? 128 LYS A N   1 
ATOM   937  C CA  . LYS A 1 128 ? -18.012 -1.695  3.801   1.00 22.53 ? 128 LYS A CA  1 
ATOM   938  C C   . LYS A 1 128 ? -19.478 -1.290  3.904   1.00 22.88 ? 128 LYS A C   1 
ATOM   939  O O   . LYS A 1 128 ? -20.366 -2.066  3.537   1.00 23.66 ? 128 LYS A O   1 
ATOM   940  C CB  . LYS A 1 128 ? -18.013 -3.185  3.471   1.00 21.96 ? 128 LYS A CB  1 
ATOM   941  C CG  . LYS A 1 128 ? -17.203 -3.510  2.227   1.00 27.37 ? 128 LYS A CG  1 
ATOM   942  C CD  . LYS A 1 128 ? -15.894 -4.147  2.530   1.00 28.77 ? 128 LYS A CD  1 
ATOM   943  C CE  . LYS A 1 128 ? -14.824 -3.473  1.731   1.00 32.52 ? 128 LYS A CE  1 
ATOM   944  N NZ  . LYS A 1 128 ? -13.554 -3.570  2.507   1.00 32.79 ? 128 LYS A NZ  1 
ATOM   945  N N   . GLY A 1 129 ? -19.724 -0.069  4.390   1.00 24.27 ? 129 GLY A N   1 
ATOM   946  C CA  . GLY A 1 129 ? -21.057 0.379   4.755   1.00 22.86 ? 129 GLY A CA  1 
ATOM   947  C C   . GLY A 1 129 ? -21.560 1.480   3.870   1.00 22.44 ? 129 GLY A C   1 
ATOM   948  O O   . GLY A 1 129 ? -22.774 1.674   3.738   1.00 22.03 ? 129 GLY A O   1 
ATOM   949  N N   . GLY A 1 130 ? -20.645 2.197   3.261   1.00 21.38 ? 130 GLY A N   1 
ATOM   950  C CA  . GLY A 1 130 ? -21.027 3.016   2.172   1.00 23.23 ? 130 GLY A CA  1 
ATOM   951  C C   . GLY A 1 130 ? -21.120 4.461   2.584   1.00 23.89 ? 130 GLY A C   1 
ATOM   952  O O   . GLY A 1 130 ? -21.496 5.286   1.761   1.00 24.46 ? 130 GLY A O   1 
ATOM   953  N N   . ASN A 1 131 ? -20.764 4.765   3.835   1.00 25.10 ? 131 ASN A N   1 
ATOM   954  C CA  . ASN A 1 131 ? -20.810 6.159   4.363   1.00 27.10 ? 131 ASN A CA  1 
ATOM   955  C C   . ASN A 1 131 ? -19.571 6.561   5.135   1.00 28.47 ? 131 ASN A C   1 
ATOM   956  O O   . ASN A 1 131 ? -18.654 5.738   5.345   1.00 29.14 ? 131 ASN A O   1 
ATOM   957  C CB  . ASN A 1 131 ? -22.028 6.416   5.243   1.00 26.81 ? 131 ASN A CB  1 
ATOM   958  C CG  . ASN A 1 131 ? -22.332 5.240   6.154   1.00 27.91 ? 131 ASN A CG  1 
ATOM   959  O OD1 . ASN A 1 131 ? -21.453 4.768   6.884   1.00 26.86 ? 131 ASN A OD1 1 
ATOM   960  N ND2 . ASN A 1 131 ? -23.570 4.747   6.104   1.00 26.90 ? 131 ASN A ND2 1 
ATOM   961  N N   . GLU A 1 132 ? -19.524 7.824   5.545   1.00 29.50 ? 132 GLU A N   1 
ATOM   962  C CA  . GLU A 1 132 ? -18.300 8.343   6.156   1.00 31.94 ? 132 GLU A CA  1 
ATOM   963  C C   . GLU A 1 132 ? -17.949 7.561   7.413   1.00 31.74 ? 132 GLU A C   1 
ATOM   964  O O   . GLU A 1 132 ? -16.809 7.164   7.596   1.00 32.55 ? 132 GLU A O   1 
ATOM   965  C CB  . GLU A 1 132 ? -18.412 9.845   6.432   1.00 31.87 ? 132 GLU A CB  1 
ATOM   966  C CG  . GLU A 1 132 ? -17.147 10.450  7.046   1.00 33.52 ? 132 GLU A CG  1 
ATOM   967  C CD  . GLU A 1 132 ? -17.293 11.977  7.285   1.00 34.29 ? 132 GLU A CD  1 
ATOM   968  O OE1 . GLU A 1 132 ? -18.402 12.516  7.014   1.00 36.30 ? 132 GLU A OE1 1 
ATOM   969  O OE2 . GLU A 1 132 ? -16.310 12.618  7.725   1.00 32.29 ? 132 GLU A OE2 1 
ATOM   970  N N   . GLU A 1 133 ? -18.969 7.289   8.231   1.00 32.51 ? 133 GLU A N   1 
ATOM   971  C CA  . GLU A 1 133 ? -18.857 6.546   9.494   1.00 31.67 ? 133 GLU A CA  1 
ATOM   972  C C   . GLU A 1 133 ? -18.365 5.132   9.363   1.00 31.23 ? 133 GLU A C   1 
ATOM   973  O O   . GLU A 1 133 ? -17.809 4.572   10.301  1.00 31.46 ? 133 GLU A O   1 
ATOM   974  C CB  . GLU A 1 133 ? -20.234 6.471   10.160  1.00 32.44 ? 133 GLU A CB  1 
ATOM   975  C CG  . GLU A 1 133 ? -20.180 6.337   11.641  1.00 31.07 ? 133 GLU A CG  1 
ATOM   976  C CD  . GLU A 1 133 ? -19.189 7.282   12.277  1.00 32.04 ? 133 GLU A CD  1 
ATOM   977  O OE1 . GLU A 1 133 ? -18.971 8.398   11.761  1.00 31.08 ? 133 GLU A OE1 1 
ATOM   978  O OE2 . GLU A 1 133 ? -18.622 6.886   13.312  1.00 33.35 ? 133 GLU A OE2 1 
ATOM   979  N N   . SER A 1 134 ? -18.612 4.522   8.225   1.00 29.94 ? 134 SER A N   1 
ATOM   980  C CA  . SER A 1 134 ? -18.345 3.116   8.065   1.00 29.53 ? 134 SER A CA  1 
ATOM   981  C C   . SER A 1 134 ? -16.866 2.843   8.207   1.00 29.33 ? 134 SER A C   1 
ATOM   982  O O   . SER A 1 134 ? -16.449 1.711   8.508   1.00 29.33 ? 134 SER A O   1 
ATOM   983  C CB  . SER A 1 134 ? -18.755 2.645   6.678   1.00 28.67 ? 134 SER A CB  1 
ATOM   984  O OG  . SER A 1 134 ? -18.340 1.316   6.541   1.00 26.87 ? 134 SER A OG  1 
ATOM   985  N N   . THR A 1 135 ? -16.105 3.899   7.967   1.00 28.30 ? 135 THR A N   1 
ATOM   986  C CA  . THR A 1 135 ? -14.684 3.821   7.761   1.00 27.62 ? 135 THR A CA  1 
ATOM   987  C C   . THR A 1 135 ? -13.986 4.527   8.932   1.00 28.12 ? 135 THR A C   1 
ATOM   988  O O   . THR A 1 135 ? -12.747 4.569   9.022   1.00 28.74 ? 135 THR A O   1 
ATOM   989  C CB  . THR A 1 135 ? -14.359 4.372   6.343   1.00 27.45 ? 135 THR A CB  1 
ATOM   990  O OG1 . THR A 1 135 ? -13.516 3.448   5.661   1.00 29.44 ? 135 THR A OG1 1 
ATOM   991  C CG2 . THR A 1 135 ? -13.777 5.771   6.337   1.00 25.16 ? 135 THR A CG2 1 
ATOM   992  N N   . LYS A 1 136 ? -14.800 5.095   9.830   1.00 28.18 ? 136 LYS A N   1 
ATOM   993  C CA  . LYS A 1 136 ? -14.342 5.596   11.120  1.00 28.16 ? 136 LYS A CA  1 
ATOM   994  C C   . LYS A 1 136 ? -14.549 4.553   12.212  1.00 28.38 ? 136 LYS A C   1 
ATOM   995  O O   . LYS A 1 136 ? -13.591 4.159   12.899  1.00 28.55 ? 136 LYS A O   1 
ATOM   996  C CB  . LYS A 1 136 ? -15.067 6.873   11.481  1.00 28.01 ? 136 LYS A CB  1 
ATOM   997  C CG  . LYS A 1 136 ? -14.753 7.982   10.527  1.00 28.58 ? 136 LYS A CG  1 
ATOM   998  C CD  . LYS A 1 136 ? -15.497 9.243   10.944  1.00 34.65 ? 136 LYS A CD  1 
ATOM   999  C CE  . LYS A 1 136 ? -15.044 10.370  10.062  1.00 35.28 ? 136 LYS A CE  1 
ATOM   1000 N NZ  . LYS A 1 136 ? -13.550 10.439  10.194  1.00 38.51 ? 136 LYS A NZ  1 
ATOM   1001 N N   . THR A 1 137 ? -15.788 4.089   12.356  1.00 27.73 ? 137 THR A N   1 
ATOM   1002 C CA  . THR A 1 137 ? -16.133 3.171   13.417  1.00 27.06 ? 137 THR A CA  1 
ATOM   1003 C C   . THR A 1 137 ? -16.755 1.881   12.959  1.00 26.93 ? 137 THR A C   1 
ATOM   1004 O O   . THR A 1 137 ? -16.701 0.907   13.709  1.00 27.91 ? 137 THR A O   1 
ATOM   1005 C CB  . THR A 1 137 ? -17.085 3.803   14.444  1.00 27.01 ? 137 THR A CB  1 
ATOM   1006 O OG1 . THR A 1 137 ? -18.339 4.113   13.820  1.00 28.11 ? 137 THR A OG1 1 
ATOM   1007 C CG2 . THR A 1 137 ? -16.475 5.063   15.046  1.00 27.14 ? 137 THR A CG2 1 
ATOM   1008 N N   . GLY A 1 138 ? -17.365 1.853   11.775  1.00 25.18 ? 138 GLY A N   1 
ATOM   1009 C CA  . GLY A 1 138 ? -18.026 0.629   11.301  1.00 22.63 ? 138 GLY A CA  1 
ATOM   1010 C C   . GLY A 1 138 ? -19.504 0.557   11.634  1.00 21.63 ? 138 GLY A C   1 
ATOM   1011 O O   . GLY A 1 138 ? -20.109 -0.504  11.600  1.00 20.11 ? 138 GLY A O   1 
ATOM   1012 N N   . ASN A 1 139 ? -20.084 1.693   11.994  1.00 20.96 ? 139 ASN A N   1 
ATOM   1013 C CA  . ASN A 1 139 ? -21.502 1.769   12.387  1.00 21.86 ? 139 ASN A CA  1 
ATOM   1014 C C   . ASN A 1 139 ? -21.976 0.657   13.403  1.00 22.34 ? 139 ASN A C   1 
ATOM   1015 O O   . ASN A 1 139 ? -23.017 -0.007  13.203  1.00 22.91 ? 139 ASN A O   1 
ATOM   1016 C CB  . ASN A 1 139 ? -22.418 1.824   11.125  1.00 21.93 ? 139 ASN A CB  1 
ATOM   1017 C CG  . ASN A 1 139 ? -22.119 3.008   10.244  1.00 20.59 ? 139 ASN A CG  1 
ATOM   1018 O OD1 . ASN A 1 139 ? -22.273 4.154   10.665  1.00 25.20 ? 139 ASN A OD1 1 
ATOM   1019 N ND2 . ASN A 1 139 ? -21.668 2.750   9.027   1.00 13.97 ? 139 ASN A ND2 1 
ATOM   1020 N N   . ALA A 1 140 ? -21.239 0.445   14.490  1.00 20.32 ? 140 ALA A N   1 
ATOM   1021 C CA  . ALA A 1 140 ? -21.554 -0.707  15.324  1.00 19.43 ? 140 ALA A CA  1 
ATOM   1022 C C   . ALA A 1 140 ? -22.435 -0.171  16.443  1.00 17.63 ? 140 ALA A C   1 
ATOM   1023 O O   . ALA A 1 140 ? -23.013 -0.923  17.218  1.00 16.17 ? 140 ALA A O   1 
ATOM   1024 C CB  . ALA A 1 140 ? -20.253 -1.365  15.849  1.00 19.06 ? 140 ALA A CB  1 
ATOM   1025 N N   . GLY A 1 141 ? -22.549 1.146   16.499  1.00 16.10 ? 141 GLY A N   1 
ATOM   1026 C CA  . GLY A 1 141 ? -23.434 1.777   17.477  1.00 16.50 ? 141 GLY A CA  1 
ATOM   1027 C C   . GLY A 1 141 ? -22.847 1.873   18.859  1.00 16.82 ? 141 GLY A C   1 
ATOM   1028 O O   . GLY A 1 141 ? -21.632 1.936   19.017  1.00 15.03 ? 141 GLY A O   1 
ATOM   1029 N N   . SER A 1 142 ? -23.748 1.911   19.855  1.00 17.60 ? 142 SER A N   1 
ATOM   1030 C CA  . SER A 1 142 ? -23.463 1.984   21.299  1.00 18.05 ? 142 SER A CA  1 
ATOM   1031 C C   . SER A 1 142 ? -22.565 0.920   21.797  1.00 17.22 ? 142 SER A C   1 
ATOM   1032 O O   . SER A 1 142 ? -22.488 -0.135  21.205  1.00 18.06 ? 142 SER A O   1 
ATOM   1033 C CB  . SER A 1 142 ? -24.750 1.734   22.069  1.00 17.03 ? 142 SER A CB  1 
ATOM   1034 O OG  . SER A 1 142 ? -25.552 2.825   21.829  1.00 25.48 ? 142 SER A OG  1 
ATOM   1035 N N   . ARG A 1 143 ? -21.941 1.192   22.941  1.00 17.57 ? 143 ARG A N   1 
ATOM   1036 C CA  . ARG A 1 143 ? -21.201 0.161   23.672  1.00 16.17 ? 143 ARG A CA  1 
ATOM   1037 C C   . ARG A 1 143 ? -22.120 -0.512  24.681  1.00 14.71 ? 143 ARG A C   1 
ATOM   1038 O O   . ARG A 1 143 ? -22.464 0.037   25.697  1.00 15.89 ? 143 ARG A O   1 
ATOM   1039 C CB  . ARG A 1 143 ? -20.035 0.835   24.395  1.00 16.50 ? 143 ARG A CB  1 
ATOM   1040 C CG  . ARG A 1 143 ? -19.574 2.040   23.667  1.00 14.30 ? 143 ARG A CG  1 
ATOM   1041 C CD  . ARG A 1 143 ? -18.168 2.406   23.971  1.00 11.20 ? 143 ARG A CD  1 
ATOM   1042 N NE  . ARG A 1 143 ? -17.704 3.276   22.923  1.00 10.86 ? 143 ARG A NE  1 
ATOM   1043 C CZ  . ARG A 1 143 ? -16.570 3.977   22.979  1.00 11.03 ? 143 ARG A CZ  1 
ATOM   1044 N NH1 . ARG A 1 143 ? -15.830 3.917   24.051  1.00 13.01 ? 143 ARG A NH1 1 
ATOM   1045 N NH2 . ARG A 1 143 ? -16.145 4.718   21.966  1.00 11.19 ? 143 ARG A NH2 1 
ATOM   1046 N N   . LEU A 1 144 ? -22.497 -1.740  24.395  1.00 14.35 ? 144 LEU A N   1 
ATOM   1047 C CA  . LEU A 1 144 ? -23.372 -2.471  25.288  1.00 11.78 ? 144 LEU A CA  1 
ATOM   1048 C C   . LEU A 1 144 ? -22.730 -2.823  26.665  1.00 10.64 ? 144 LEU A C   1 
ATOM   1049 O O   . LEU A 1 144 ? -23.410 -2.858  27.703  1.00 9.34  ? 144 LEU A O   1 
ATOM   1050 C CB  . LEU A 1 144 ? -23.895 -3.704  24.543  1.00 13.20 ? 144 LEU A CB  1 
ATOM   1051 C CG  . LEU A 1 144 ? -24.847 -3.483  23.364  1.00 11.35 ? 144 LEU A CG  1 
ATOM   1052 C CD1 . LEU A 1 144 ? -25.654 -4.773  23.218  1.00 15.52 ? 144 LEU A CD1 1 
ATOM   1053 C CD2 . LEU A 1 144 ? -25.743 -2.254  23.535  1.00 10.23 ? 144 LEU A CD2 1 
ATOM   1054 N N   . ALA A 1 145 ? -21.415 -3.048  26.656  1.00 8.19  ? 145 ALA A N   1 
ATOM   1055 C CA  . ALA A 1 145 ? -20.718 -3.755  27.711  1.00 9.44  ? 145 ALA A CA  1 
ATOM   1056 C C   . ALA A 1 145 ? -19.219 -3.704  27.333  1.00 9.16  ? 145 ALA A C   1 
ATOM   1057 O O   . ALA A 1 145 ? -18.898 -3.862  26.140  1.00 9.28  ? 145 ALA A O   1 
ATOM   1058 C CB  . ALA A 1 145 ? -21.175 -5.250  27.767  1.00 8.53  ? 145 ALA A CB  1 
ATOM   1059 N N   . CYS A 1 146 ? -18.333 -3.457  28.318  1.00 9.76  ? 146 CYS A N   1 
ATOM   1060 C CA  . CYS A 1 146 ? -16.882 -3.445  28.075  1.00 7.24  ? 146 CYS A CA  1 
ATOM   1061 C C   . CYS A 1 146 ? -16.226 -3.982  29.315  1.00 7.59  ? 146 CYS A C   1 
ATOM   1062 O O   . CYS A 1 146 ? -16.916 -4.201  30.363  1.00 7.89  ? 146 CYS A O   1 
ATOM   1063 C CB  . CYS A 1 146 ? -16.489 -1.971  27.765  1.00 9.04  ? 146 CYS A CB  1 
ATOM   1064 S SG  . CYS A 1 146 ? -17.105 -0.882  29.043  1.00 13.02 ? 146 CYS A SG  1 
ATOM   1065 N N   . GLY A 1 147 ? -14.922 -4.352  29.214  1.00 6.08  ? 147 GLY A N   1 
ATOM   1066 C CA  . GLY A 1 147 ? -14.093 -4.653  30.392  1.00 3.01  ? 147 GLY A CA  1 
ATOM   1067 C C   . GLY A 1 147 ? -12.647 -4.329  30.056  1.00 3.09  ? 147 GLY A C   1 
ATOM   1068 O O   . GLY A 1 147 ? -12.301 -4.452  28.909  1.00 2.00  ? 147 GLY A O   1 
ATOM   1069 N N   . VAL A 1 148 ? -11.858 -3.852  31.066  1.00 4.64  ? 148 VAL A N   1 
ATOM   1070 C CA  . VAL A 1 148 ? -10.372 -3.682  30.987  1.00 2.35  ? 148 VAL A CA  1 
ATOM   1071 C C   . VAL A 1 148 ? -9.781  -5.054  30.818  1.00 5.77  ? 148 VAL A C   1 
ATOM   1072 O O   . VAL A 1 148 ? -10.192 -5.953  31.590  1.00 2.49  ? 148 VAL A O   1 
ATOM   1073 C CB  . VAL A 1 148 ? -9.800  -2.946  32.229  1.00 4.38  ? 148 VAL A CB  1 
ATOM   1074 C CG1 . VAL A 1 148 ? -8.236  -2.576  32.070  1.00 2.00  ? 148 VAL A CG1 1 
ATOM   1075 C CG2 . VAL A 1 148 ? -10.595 -1.724  32.363  1.00 2.00  ? 148 VAL A CG2 1 
ATOM   1076 N N   . ILE A 1 149 ? -8.910  -5.187  29.805  1.00 5.47  ? 149 ILE A N   1 
ATOM   1077 C CA  . ILE A 1 149 ? -8.106  -6.417  29.607  1.00 7.33  ? 149 ILE A CA  1 
ATOM   1078 C C   . ILE A 1 149 ? -6.976  -6.516  30.605  1.00 8.74  ? 149 ILE A C   1 
ATOM   1079 O O   . ILE A 1 149 ? -6.057  -5.650  30.637  1.00 12.66 ? 149 ILE A O   1 
ATOM   1080 C CB  . ILE A 1 149 ? -7.637  -6.575  28.179  1.00 5.54  ? 149 ILE A CB  1 
ATOM   1081 C CG1 . ILE A 1 149 ? -8.864  -6.394  27.325  1.00 2.00  ? 149 ILE A CG1 1 
ATOM   1082 C CG2 . ILE A 1 149 ? -6.993  -8.103  27.915  1.00 7.97  ? 149 ILE A CG2 1 
ATOM   1083 C CD1 . ILE A 1 149 ? -8.548  -5.904  25.939  1.00 2.00  ? 149 ILE A CD1 1 
ATOM   1084 N N   . GLY A 1 150 ? -7.054  -7.565  31.432  1.00 8.52  ? 150 GLY A N   1 
ATOM   1085 C CA  . GLY A 1 150 ? -6.174  -7.728  32.519  1.00 8.70  ? 150 GLY A CA  1 
ATOM   1086 C C   . GLY A 1 150 ? -5.322  -8.934  32.389  1.00 11.31 ? 150 GLY A C   1 
ATOM   1087 O O   . GLY A 1 150 ? -5.751  -9.905  31.815  1.00 10.82 ? 150 GLY A O   1 
ATOM   1088 N N   . ILE A 1 151 ? -4.157  -8.909  33.036  1.00 12.44 ? 151 ILE A N   1 
ATOM   1089 C CA  . ILE A 1 151 ? -3.237  -10.049 33.083  1.00 12.38 ? 151 ILE A CA  1 
ATOM   1090 C C   . ILE A 1 151 ? -3.927  -11.244 33.800  1.00 12.78 ? 151 ILE A C   1 
ATOM   1091 O O   . ILE A 1 151 ? -4.596  -11.063 34.821  1.00 11.28 ? 151 ILE A O   1 
ATOM   1092 C CB  . ILE A 1 151 ? -1.962  -9.615  33.819  1.00 12.66 ? 151 ILE A CB  1 
ATOM   1093 C CG1 . ILE A 1 151 ? -1.349  -8.382  33.120  1.00 11.22 ? 151 ILE A CG1 1 
ATOM   1094 C CG2 . ILE A 1 151 ? -1.007  -10.704 33.899  1.00 10.50 ? 151 ILE A CG2 1 
ATOM   1095 C CD1 . ILE A 1 151 ? 0.037   -8.085  33.498  1.00 6.13  ? 151 ILE A CD1 1 
ATOM   1096 N N   . ALA A 1 152 ? -3.804  -12.448 33.259  1.00 14.51 ? 152 ALA A N   1 
ATOM   1097 C CA  . ALA A 1 152 ? -4.465  -13.568 33.894  1.00 15.81 ? 152 ALA A CA  1 
ATOM   1098 C C   . ALA A 1 152 ? -3.552  -14.735 34.167  1.00 17.17 ? 152 ALA A C   1 
ATOM   1099 O O   . ALA A 1 152 ? -2.505  -14.843 33.604  1.00 16.96 ? 152 ALA A O   1 
ATOM   1100 C CB  . ALA A 1 152 ? -5.609  -14.052 33.024  1.00 17.21 ? 152 ALA A CB  1 
ATOM   1101 N N   . GLN A 1 153 ? -4.005  -15.619 35.037  1.00 18.24 ? 153 GLN A N   1 
ATOM   1102 C CA  . GLN A 1 153 ? -3.314  -16.860 35.298  1.00 20.26 ? 153 GLN A CA  1 
ATOM   1103 C C   . GLN A 1 153 ? -3.949  -17.915 34.400  1.00 20.64 ? 153 GLN A C   1 
ATOM   1104 O O   . GLN A 1 153 ? -5.195  -18.165 34.368  1.00 19.74 ? 153 GLN A O   1 
ATOM   1105 C CB  . GLN A 1 153 ? -3.532  -17.189 36.736  1.00 19.95 ? 153 GLN A CB  1 
ATOM   1106 C CG  . GLN A 1 153 ? -2.700  -18.275 37.348  1.00 24.71 ? 153 GLN A CG  1 
ATOM   1107 C CD  . GLN A 1 153 ? -2.958  -18.290 38.850  1.00 28.51 ? 153 GLN A CD  1 
ATOM   1108 O OE1 . GLN A 1 153 ? -4.096  -18.072 39.299  1.00 27.09 ? 153 GLN A OE1 1 
ATOM   1109 N NE2 . GLN A 1 153 ? -1.889  -18.490 39.641  1.00 33.93 ? 153 GLN A NE2 1 
ATOM   1110 O OXT . GLN A 1 153 ? -3.192  -18.516 33.645  1.00 22.53 ? 153 GLN A OXT 1 
ATOM   1111 N N   . ALA B 1 1   ? 3.948   4.338   29.375  1.00 19.08 ? 1   ALA B N   1 
ATOM   1112 C CA  . ALA B 1 1   ? 2.569   4.757   29.797  1.00 18.09 ? 1   ALA B CA  1 
ATOM   1113 C C   . ALA B 1 1   ? 2.848   5.631   30.978  1.00 17.63 ? 1   ALA B C   1 
ATOM   1114 O O   . ALA B 1 1   ? 3.584   5.194   31.878  1.00 16.55 ? 1   ALA B O   1 
ATOM   1115 C CB  . ALA B 1 1   ? 1.737   3.579   30.218  1.00 18.91 ? 1   ALA B CB  1 
ATOM   1116 N N   . THR B 1 2   ? 2.324   6.862   30.991  1.00 15.32 ? 2   THR B N   1 
ATOM   1117 C CA  . THR B 1 2   ? 2.525   7.720   32.137  1.00 14.41 ? 2   THR B CA  1 
ATOM   1118 C C   . THR B 1 2   ? 1.242   7.950   33.016  1.00 14.50 ? 2   THR B C   1 
ATOM   1119 O O   . THR B 1 2   ? 1.339   8.476   34.102  1.00 14.37 ? 2   THR B O   1 
ATOM   1120 C CB  . THR B 1 2   ? 3.022   9.098   31.711  1.00 14.01 ? 2   THR B CB  1 
ATOM   1121 O OG1 . THR B 1 2   ? 1.988   9.682   30.986  1.00 11.63 ? 2   THR B OG1 1 
ATOM   1122 C CG2 . THR B 1 2   ? 4.233   9.005   30.797  1.00 15.72 ? 2   THR B CG2 1 
ATOM   1123 N N   . LYS B 1 3   ? 0.063   7.524   32.561  1.00 14.75 ? 3   LYS B N   1 
ATOM   1124 C CA  . LYS B 1 3   ? -1.167  7.609   33.355  1.00 13.87 ? 3   LYS B CA  1 
ATOM   1125 C C   . LYS B 1 3   ? -1.935  6.334   33.394  1.00 11.90 ? 3   LYS B C   1 
ATOM   1126 O O   . LYS B 1 3   ? -2.018  5.575   32.409  1.00 12.96 ? 3   LYS B O   1 
ATOM   1127 C CB  . LYS B 1 3   ? -2.137  8.609   32.792  1.00 14.24 ? 3   LYS B CB  1 
ATOM   1128 C CG  . LYS B 1 3   ? -1.677  10.041  32.866  1.00 18.05 ? 3   LYS B CG  1 
ATOM   1129 C CD  . LYS B 1 3   ? -2.897  10.998  33.019  1.00 21.20 ? 3   LYS B CD  1 
ATOM   1130 C CE  . LYS B 1 3   ? -3.366  11.085  34.444  1.00 22.07 ? 3   LYS B CE  1 
ATOM   1131 N NZ  . LYS B 1 3   ? -3.789  12.529  34.642  1.00 24.76 ? 3   LYS B NZ  1 
ATOM   1132 N N   . ALA B 1 4   ? -2.568  6.096   34.522  1.00 11.33 ? 4   ALA B N   1 
ATOM   1133 C CA  . ALA B 1 4   ? -3.403  4.879   34.597  1.00 9.46  ? 4   ALA B CA  1 
ATOM   1134 C C   . ALA B 1 4   ? -4.561  5.207   35.508  1.00 8.89  ? 4   ALA B C   1 
ATOM   1135 O O   . ALA B 1 4   ? -4.617  6.320   36.062  1.00 9.76  ? 4   ALA B O   1 
ATOM   1136 C CB  . ALA B 1 4   ? -2.651  3.765   35.064  1.00 8.89  ? 4   ALA B CB  1 
ATOM   1137 N N   . VAL B 1 5   ? -5.562  4.330   35.591  1.00 7.69  ? 5   VAL B N   1 
ATOM   1138 C CA  . VAL B 1 5   ? -6.760  4.628   36.378  1.00 4.79  ? 5   VAL B CA  1 
ATOM   1139 C C   . VAL B 1 5   ? -7.422  3.309   36.676  1.00 5.33  ? 5   VAL B C   1 
ATOM   1140 O O   . VAL B 1 5   ? -7.124  2.376   35.987  1.00 2.00  ? 5   VAL B O   1 
ATOM   1141 C CB  . VAL B 1 5   ? -7.631  5.691   35.698  1.00 9.04  ? 5   VAL B CB  1 
ATOM   1142 C CG1 . VAL B 1 5   ? -8.210  5.272   34.364  1.00 4.57  ? 5   VAL B CG1 1 
ATOM   1143 C CG2 . VAL B 1 5   ? -8.705  6.439   36.726  1.00 8.88  ? 5   VAL B CG2 1 
ATOM   1144 N N   . CYS B 1 6   ? -8.187  3.275   37.752  1.00 4.17  ? 6   CYS B N   1 
ATOM   1145 C CA  . CYS B 1 6   ? -8.865  2.055   38.256  1.00 4.81  ? 6   CYS B CA  1 
ATOM   1146 C C   . CYS B 1 6   ? -10.199 2.531   38.798  1.00 6.02  ? 6   CYS B C   1 
ATOM   1147 O O   . CYS B 1 6   ? -10.221 3.350   39.744  1.00 4.50  ? 6   CYS B O   1 
ATOM   1148 C CB  . CYS B 1 6   ? -8.167  1.515   39.468  1.00 2.67  ? 6   CYS B CB  1 
ATOM   1149 S SG  . CYS B 1 6   ? -8.504  -0.303  39.838  1.00 4.12  ? 6   CYS B SG  1 
ATOM   1150 N N   . VAL B 1 7   ? -11.267 1.813   38.398  1.00 7.11  ? 7   VAL B N   1 
ATOM   1151 C CA  . VAL B 1 7   ? -12.626 1.981   38.983  1.00 6.47  ? 7   VAL B CA  1 
ATOM   1152 C C   . VAL B 1 7   ? -12.880 0.836   39.917  1.00 4.61  ? 7   VAL B C   1 
ATOM   1153 O O   . VAL B 1 7   ? -12.865 -0.400  39.486  1.00 5.62  ? 7   VAL B O   1 
ATOM   1154 C CB  . VAL B 1 7   ? -13.648 2.162   37.846  1.00 7.27  ? 7   VAL B CB  1 
ATOM   1155 C CG1 . VAL B 1 7   ? -15.112 2.343   38.392  1.00 11.52 ? 7   VAL B CG1 1 
ATOM   1156 C CG2 . VAL B 1 7   ? -13.226 3.337   37.106  1.00 5.43  ? 7   VAL B CG2 1 
ATOM   1157 N N   . LEU B 1 8   ? -12.983 1.183   41.207  1.00 3.62  ? 8   LEU B N   1 
ATOM   1158 C CA  . LEU B 1 8   ? -13.240 0.165   42.250  1.00 3.35  ? 8   LEU B CA  1 
ATOM   1159 C C   . LEU B 1 8   ? -14.708 -0.074  42.501  1.00 5.04  ? 8   LEU B C   1 
ATOM   1160 O O   . LEU B 1 8   ? -15.380 0.843   42.767  1.00 3.58  ? 8   LEU B O   1 
ATOM   1161 C CB  . LEU B 1 8   ? -12.608 0.423   43.594  1.00 2.00  ? 8   LEU B CB  1 
ATOM   1162 C CG  . LEU B 1 8   ? -11.134 0.328   44.090  1.00 3.97  ? 8   LEU B CG  1 
ATOM   1163 C CD1 . LEU B 1 8   ? -10.285 -0.184  43.124  1.00 2.00  ? 8   LEU B CD1 1 
ATOM   1164 C CD2 . LEU B 1 8   ? -10.696 1.742   44.378  1.00 7.74  ? 8   LEU B CD2 1 
ATOM   1165 N N   . LYS B 1 9   ? -15.142 -1.351  42.532  1.00 2.26  ? 9   LYS B N   1 
ATOM   1166 C CA  . LYS B 1 9   ? -16.534 -1.711  42.678  1.00 5.37  ? 9   LYS B CA  1 
ATOM   1167 C C   . LYS B 1 9   ? -16.421 -3.113  43.310  1.00 5.50  ? 9   LYS B C   1 
ATOM   1168 O O   . LYS B 1 9   ? -15.408 -3.747  43.155  1.00 2.41  ? 9   LYS B O   1 
ATOM   1169 C CB  . LYS B 1 9   ? -17.217 -1.869  41.304  1.00 6.75  ? 9   LYS B CB  1 
ATOM   1170 C CG  . LYS B 1 9   ? -17.454 -0.483  40.572  1.00 11.15 ? 9   LYS B CG  1 
ATOM   1171 C CD  . LYS B 1 9   ? -18.819 0.198   40.918  1.00 16.73 ? 9   LYS B CD  1 
ATOM   1172 C CE  . LYS B 1 9   ? -18.718 1.804   41.084  1.00 17.99 ? 9   LYS B CE  1 
ATOM   1173 N NZ  . LYS B 1 9   ? -17.353 2.259   40.654  1.00 12.98 ? 9   LYS B NZ  1 
ATOM   1174 N N   . GLY B 1 10  ? -17.439 -3.515  44.028  1.00 7.92  ? 10  GLY B N   1 
ATOM   1175 C CA  . GLY B 1 10  ? -17.433 -4.825  44.729  1.00 12.06 ? 10  GLY B CA  1 
ATOM   1176 C C   . GLY B 1 10  ? -18.899 -5.100  44.999  1.00 14.60 ? 10  GLY B C   1 
ATOM   1177 O O   . GLY B 1 10  ? -19.765 -4.433  44.450  1.00 14.25 ? 10  GLY B O   1 
ATOM   1178 N N   . ASP B 1 11  ? -19.147 -6.052  45.886  1.00 16.48 ? 11  ASP B N   1 
ATOM   1179 C CA  . ASP B 1 11  ? -20.469 -6.609  46.063  1.00 18.20 ? 11  ASP B CA  1 
ATOM   1180 C C   . ASP B 1 11  ? -21.384 -5.804  46.970  1.00 17.73 ? 11  ASP B C   1 
ATOM   1181 O O   . ASP B 1 11  ? -22.601 -6.071  46.997  1.00 21.15 ? 11  ASP B O   1 
ATOM   1182 C CB  . ASP B 1 11  ? -20.352 -8.060  46.524  1.00 17.76 ? 11  ASP B CB  1 
ATOM   1183 C CG  . ASP B 1 11  ? -20.124 -9.011  45.344  1.00 21.71 ? 11  ASP B CG  1 
ATOM   1184 O OD1 . ASP B 1 11  ? -19.690 -10.167 45.529  1.00 22.94 ? 11  ASP B OD1 1 
ATOM   1185 O OD2 . ASP B 1 11  ? -20.380 -8.609  44.183  1.00 24.80 ? 11  ASP B OD2 1 
ATOM   1186 N N   . GLY B 1 12  ? -20.826 -4.828  47.670  1.00 16.06 ? 12  GLY B N   1 
ATOM   1187 C CA  . GLY B 1 12  ? -21.531 -3.952  48.612  1.00 13.86 ? 12  GLY B CA  1 
ATOM   1188 C C   . GLY B 1 12  ? -21.359 -2.517  48.217  1.00 12.26 ? 12  GLY B C   1 
ATOM   1189 O O   . GLY B 1 12  ? -21.319 -2.233  47.053  1.00 14.63 ? 12  GLY B O   1 
ATOM   1190 N N   . PRO B 1 13  ? -21.372 -1.586  49.159  1.00 10.71 ? 13  PRO B N   1 
ATOM   1191 C CA  . PRO B 1 13  ? -21.330 -0.188  48.674  1.00 11.44 ? 13  PRO B CA  1 
ATOM   1192 C C   . PRO B 1 13  ? -19.946 0.390   48.359  1.00 12.82 ? 13  PRO B C   1 
ATOM   1193 O O   . PRO B 1 13  ? -19.781 1.628   48.188  1.00 11.92 ? 13  PRO B O   1 
ATOM   1194 C CB  . PRO B 1 13  ? -21.904 0.588   49.838  1.00 9.64  ? 13  PRO B CB  1 
ATOM   1195 C CG  . PRO B 1 13  ? -21.437 -0.083  50.987  1.00 8.49  ? 13  PRO B CG  1 
ATOM   1196 C CD  . PRO B 1 13  ? -21.479 -1.634  50.609  1.00 8.55  ? 13  PRO B CD  1 
ATOM   1197 N N   . VAL B 1 14  ? -18.918 -0.437  48.350  1.00 13.43 ? 14  VAL B N   1 
ATOM   1198 C CA  . VAL B 1 14  ? -17.613 0.206   48.193  1.00 15.06 ? 14  VAL B CA  1 
ATOM   1199 C C   . VAL B 1 14  ? -17.313 0.560   46.728  1.00 14.71 ? 14  VAL B C   1 
ATOM   1200 O O   . VAL B 1 14  ? -17.284 -0.309  45.895  1.00 13.71 ? 14  VAL B O   1 
ATOM   1201 C CB  . VAL B 1 14  ? -16.461 -0.516  48.982  1.00 14.62 ? 14  VAL B CB  1 
ATOM   1202 C CG1 . VAL B 1 14  ? -15.119 0.283   48.889  1.00 16.26 ? 14  VAL B CG1 1 
ATOM   1203 C CG2 . VAL B 1 14  ? -16.807 -0.564  50.377  1.00 13.05 ? 14  VAL B CG2 1 
ATOM   1204 N N   . GLN B 1 15  ? -17.109 1.864   46.449  1.00 14.98 ? 15  GLN B N   1 
ATOM   1205 C CA  . GLN B 1 15  ? -16.850 2.338   45.107  1.00 16.40 ? 15  GLN B CA  1 
ATOM   1206 C C   . GLN B 1 15  ? -15.819 3.471   45.070  1.00 15.34 ? 15  GLN B C   1 
ATOM   1207 O O   . GLN B 1 15  ? -15.761 4.246   45.966  1.00 14.89 ? 15  GLN B O   1 
ATOM   1208 C CB  . GLN B 1 15  ? -18.136 2.797   44.400  1.00 17.36 ? 15  GLN B CB  1 
ATOM   1209 C CG  . GLN B 1 15  ? -18.939 3.850   45.101  1.00 20.76 ? 15  GLN B CG  1 
ATOM   1210 C CD  . GLN B 1 15  ? -20.329 3.964   44.499  1.00 30.82 ? 15  GLN B CD  1 
ATOM   1211 O OE1 . GLN B 1 15  ? -20.502 3.774   43.301  1.00 35.17 ? 15  GLN B OE1 1 
ATOM   1212 N NE2 . GLN B 1 15  ? -21.333 4.236   45.335  1.00 32.01 ? 15  GLN B NE2 1 
ATOM   1213 N N   . GLY B 1 16  ? -15.016 3.565   44.017  1.00 14.66 ? 16  GLY B N   1 
ATOM   1214 C CA  . GLY B 1 16  ? -13.974 4.581   44.010  1.00 13.57 ? 16  GLY B CA  1 
ATOM   1215 C C   . GLY B 1 16  ? -13.210 4.718   42.720  1.00 14.44 ? 16  GLY B C   1 
ATOM   1216 O O   . GLY B 1 16  ? -13.253 3.818   41.840  1.00 14.69 ? 16  GLY B O   1 
ATOM   1217 N N   . ILE B 1 17  ? -12.594 5.906   42.561  1.00 14.58 ? 17  ILE B N   1 
ATOM   1218 C CA  . ILE B 1 17  ? -11.720 6.183   41.411  1.00 14.18 ? 17  ILE B CA  1 
ATOM   1219 C C   . ILE B 1 17  ? -10.296 6.592   41.843  1.00 12.60 ? 17  ILE B C   1 
ATOM   1220 O O   . ILE B 1 17  ? -10.097 7.689   42.385  1.00 12.93 ? 17  ILE B O   1 
ATOM   1221 C CB  . ILE B 1 17  ? -12.305 7.263   40.414  1.00 13.56 ? 17  ILE B CB  1 
ATOM   1222 C CG1 . ILE B 1 17  ? -13.690 6.846   39.904  1.00 15.41 ? 17  ILE B CG1 1 
ATOM   1223 C CG2 . ILE B 1 17  ? -11.349 7.528   39.268  1.00 8.71  ? 17  ILE B CG2 1 
ATOM   1224 C CD1 . ILE B 1 17  ? -14.423 7.990   39.174  1.00 14.68 ? 17  ILE B CD1 1 
ATOM   1225 N N   . ILE B 1 18  ? -9.327  5.734   41.499  1.00 11.68 ? 18  ILE B N   1 
ATOM   1226 C CA  . ILE B 1 18  ? -7.873  5.911   41.858  1.00 9.04  ? 18  ILE B CA  1 
ATOM   1227 C C   . ILE B 1 18  ? -7.061  6.107   40.578  1.00 10.59 ? 18  ILE B C   1 
ATOM   1228 O O   . ILE B 1 18  ? -7.176  5.312   39.627  1.00 10.57 ? 18  ILE B O   1 
ATOM   1229 C CB  . ILE B 1 18  ? -7.349  4.684   42.671  1.00 9.96  ? 18  ILE B CB  1 
ATOM   1230 C CG1 . ILE B 1 18  ? -8.095  4.565   44.011  1.00 9.78  ? 18  ILE B CG1 1 
ATOM   1231 C CG2 . ILE B 1 18  ? -5.871  4.748   42.922  1.00 5.80  ? 18  ILE B CG2 1 
ATOM   1232 C CD1 . ILE B 1 18  ? -8.019  5.768   44.916  1.00 2.00  ? 18  ILE B CD1 1 
ATOM   1233 N N   . ASN B 1 19  ? -6.324  7.253   40.510  1.00 9.01  ? 19  ASN B N   1 
ATOM   1234 C CA  . ASN B 1 19  ? -5.555  7.666   39.357  1.00 7.25  ? 19  ASN B CA  1 
ATOM   1235 C C   . ASN B 1 19  ? -4.126  7.406   39.694  1.00 5.21  ? 19  ASN B C   1 
ATOM   1236 O O   . ASN B 1 19  ? -3.783  7.495   40.838  1.00 4.33  ? 19  ASN B O   1 
ATOM   1237 C CB  . ASN B 1 19  ? -5.759  9.211   39.184  1.00 8.77  ? 19  ASN B CB  1 
ATOM   1238 C CG  . ASN B 1 19  ? -7.189  9.567   38.953  1.00 8.40  ? 19  ASN B CG  1 
ATOM   1239 O OD1 . ASN B 1 19  ? -7.875  10.076  39.847  1.00 12.83 ? 19  ASN B OD1 1 
ATOM   1240 N ND2 . ASN B 1 19  ? -7.686  9.209   37.789  1.00 8.10  ? 19  ASN B ND2 1 
ATOM   1241 N N   . PHE B 1 20  ? -3.301  7.059   38.700  1.00 7.66  ? 20  PHE B N   1 
ATOM   1242 C CA  . PHE B 1 20  ? -1.842  6.792   38.842  1.00 7.78  ? 20  PHE B CA  1 
ATOM   1243 C C   . PHE B 1 20  ? -1.128  7.621   37.843  1.00 8.43  ? 20  PHE B C   1 
ATOM   1244 O O   . PHE B 1 20  ? -1.534  7.644   36.738  1.00 8.71  ? 20  PHE B O   1 
ATOM   1245 C CB  . PHE B 1 20  ? -1.515  5.314   38.476  1.00 7.68  ? 20  PHE B CB  1 
ATOM   1246 C CG  . PHE B 1 20  ? -2.311  4.336   39.277  1.00 4.61  ? 20  PHE B CG  1 
ATOM   1247 C CD1 . PHE B 1 20  ? -3.610  4.091   38.967  1.00 2.01  ? 20  PHE B CD1 1 
ATOM   1248 C CD2 . PHE B 1 20  ? -1.787  3.771   40.406  1.00 6.93  ? 20  PHE B CD2 1 
ATOM   1249 C CE1 . PHE B 1 20  ? -4.391  3.237   39.789  1.00 2.00  ? 20  PHE B CE1 1 
ATOM   1250 C CE2 . PHE B 1 20  ? -2.550  2.983   41.170  1.00 2.44  ? 20  PHE B CE2 1 
ATOM   1251 C CZ  . PHE B 1 20  ? -3.876  2.771   40.839  1.00 2.00  ? 20  PHE B CZ  1 
ATOM   1252 N N   . GLU B 1 21  ? -0.035  8.279   38.225  1.00 11.02 ? 21  GLU B N   1 
ATOM   1253 C CA  . GLU B 1 21  ? 0.760   9.078   37.296  1.00 10.45 ? 21  GLU B CA  1 
ATOM   1254 C C   . GLU B 1 21  ? 2.246   8.801   37.536  1.00 9.47  ? 21  GLU B C   1 
ATOM   1255 O O   . GLU B 1 21  ? 2.708   8.840   38.656  1.00 8.38  ? 21  GLU B O   1 
ATOM   1256 C CB  . GLU B 1 21  ? 0.496   10.591  37.494  1.00 12.43 ? 21  GLU B CB  1 
ATOM   1257 C CG  . GLU B 1 21  ? 1.158   11.453  36.430  1.00 17.50 ? 21  GLU B CG  1 
ATOM   1258 C CD  . GLU B 1 21  ? 1.507   12.840  36.968  1.00 23.57 ? 21  GLU B CD  1 
ATOM   1259 O OE1 . GLU B 1 21  ? 2.668   13.041  37.427  1.00 24.09 ? 21  GLU B OE1 1 
ATOM   1260 O OE2 . GLU B 1 21  ? 0.590   13.698  36.953  1.00 28.13 ? 21  GLU B OE2 1 
ATOM   1261 N N   . GLN B 1 22  ? 2.980   8.513   36.461  1.00 9.78  ? 22  GLN B N   1 
ATOM   1262 C CA  . GLN B 1 22  ? 4.441   8.368   36.511  1.00 10.93 ? 22  GLN B CA  1 
ATOM   1263 C C   . GLN B 1 22  ? 5.039   9.136   35.360  1.00 13.94 ? 22  GLN B C   1 
ATOM   1264 O O   . GLN B 1 22  ? 5.216   8.583   34.299  1.00 14.38 ? 22  GLN B O   1 
ATOM   1265 C CB  . GLN B 1 22  ? 4.852   6.883   36.369  1.00 9.03  ? 22  GLN B CB  1 
ATOM   1266 C CG  . GLN B 1 22  ? 6.263   6.592   36.613  1.00 4.34  ? 22  GLN B CG  1 
ATOM   1267 C CD  . GLN B 1 22  ? 6.485   5.136   36.599  1.00 7.38  ? 22  GLN B CD  1 
ATOM   1268 O OE1 . GLN B 1 22  ? 5.701   4.410   36.034  1.00 4.91  ? 22  GLN B OE1 1 
ATOM   1269 N NE2 . GLN B 1 22  ? 7.547   4.705   37.162  1.00 2.38  ? 22  GLN B NE2 1 
ATOM   1270 N N   . LYS B 1 23  ? 5.318   10.418  35.541  1.00 18.19 ? 23  LYS B N   1 
ATOM   1271 C CA  . LYS B 1 23  ? 5.928   11.169  34.445  1.00 21.75 ? 23  LYS B CA  1 
ATOM   1272 C C   . LYS B 1 23  ? 7.358   10.713  34.071  1.00 23.13 ? 23  LYS B C   1 
ATOM   1273 O O   . LYS B 1 23  ? 7.871   11.119  33.012  1.00 25.82 ? 23  LYS B O   1 
ATOM   1274 C CB  . LYS B 1 23  ? 5.973   12.663  34.757  1.00 22.94 ? 23  LYS B CB  1 
ATOM   1275 C CG  . LYS B 1 23  ? 4.651   13.315  35.061  1.00 25.09 ? 23  LYS B CG  1 
ATOM   1276 C CD  . LYS B 1 23  ? 3.838   13.551  33.780  1.00 31.63 ? 23  LYS B CD  1 
ATOM   1277 C CE  . LYS B 1 23  ? 2.953   14.827  33.936  1.00 33.90 ? 23  LYS B CE  1 
ATOM   1278 N NZ  . LYS B 1 23  ? 2.647   15.525  32.638  1.00 35.18 ? 23  LYS B NZ  1 
ATOM   1279 N N   . GLU B 1 24  ? 8.005   9.905   34.917  1.00 23.23 ? 24  GLU B N   1 
ATOM   1280 C CA  . GLU B 1 24  ? 9.384   9.431   34.683  1.00 21.57 ? 24  GLU B CA  1 
ATOM   1281 C C   . GLU B 1 24  ? 9.486   7.926   34.860  1.00 20.34 ? 24  GLU B C   1 
ATOM   1282 O O   . GLU B 1 24  ? 9.246   7.485   35.949  1.00 20.49 ? 24  GLU B O   1 
ATOM   1283 C CB  . GLU B 1 24  ? 10.342  10.154  35.656  1.00 22.47 ? 24  GLU B CB  1 
ATOM   1284 C CG  . GLU B 1 24  ? 10.588  11.587  35.209  1.00 24.52 ? 24  GLU B CG  1 
ATOM   1285 C CD  . GLU B 1 24  ? 11.188  12.517  36.242  1.00 29.29 ? 24  GLU B CD  1 
ATOM   1286 O OE1 . GLU B 1 24  ? 11.896  12.064  37.173  1.00 32.25 ? 24  GLU B OE1 1 
ATOM   1287 O OE2 . GLU B 1 24  ? 11.001  13.741  36.075  1.00 29.17 ? 24  GLU B OE2 1 
ATOM   1288 N N   . SER B 1 25  ? 9.856   7.134   33.848  1.00 17.73 ? 25  SER B N   1 
ATOM   1289 C CA  . SER B 1 25  ? 9.748   5.652   33.999  1.00 17.87 ? 25  SER B CA  1 
ATOM   1290 C C   . SER B 1 25  ? 10.491  4.999   35.150  1.00 18.20 ? 25  SER B C   1 
ATOM   1291 O O   . SER B 1 25  ? 10.237  3.821   35.492  1.00 19.82 ? 25  SER B O   1 
ATOM   1292 C CB  . SER B 1 25  ? 10.166  4.922   32.726  1.00 17.82 ? 25  SER B CB  1 
ATOM   1293 O OG  . SER B 1 25  ? 11.427  5.397   32.318  1.00 17.88 ? 25  SER B OG  1 
ATOM   1294 N N   . ASN B 1 26  ? 11.461  5.723   35.685  1.00 18.05 ? 26  ASN B N   1 
ATOM   1295 C CA  . ASN B 1 26  ? 12.305  5.227   36.761  1.00 17.93 ? 26  ASN B CA  1 
ATOM   1296 C C   . ASN B 1 26  ? 12.124  6.152   37.971  1.00 18.26 ? 26  ASN B C   1 
ATOM   1297 O O   . ASN B 1 26  ? 12.891  6.063   38.953  1.00 18.41 ? 26  ASN B O   1 
ATOM   1298 C CB  . ASN B 1 26  ? 13.812  5.099   36.319  1.00 17.22 ? 26  ASN B CB  1 
ATOM   1299 C CG  . ASN B 1 26  ? 14.474  6.475   36.107  1.00 13.83 ? 26  ASN B CG  1 
ATOM   1300 O OD1 . ASN B 1 26  ? 13.790  7.416   35.771  1.00 13.51 ? 26  ASN B OD1 1 
ATOM   1301 N ND2 . ASN B 1 26  ? 15.768  6.595   36.385  1.00 12.72 ? 26  ASN B ND2 1 
ATOM   1302 N N   . GLY B 1 27  ? 11.090  7.005   37.903  1.00 17.67 ? 27  GLY B N   1 
ATOM   1303 C CA  . GLY B 1 27  ? 10.575  7.745   39.045  1.00 17.16 ? 27  GLY B CA  1 
ATOM   1304 C C   . GLY B 1 27  ? 9.409   7.087   39.789  1.00 16.32 ? 27  GLY B C   1 
ATOM   1305 O O   . GLY B 1 27  ? 8.995   5.918   39.471  1.00 15.69 ? 27  GLY B O   1 
ATOM   1306 N N   . PRO B 1 28  ? 8.951   7.758   40.859  1.00 15.19 ? 28  PRO B N   1 
ATOM   1307 C CA  . PRO B 1 28  ? 7.814   7.315   41.646  1.00 14.71 ? 28  PRO B CA  1 
ATOM   1308 C C   . PRO B 1 28  ? 6.501   7.473   40.880  1.00 14.43 ? 28  PRO B C   1 
ATOM   1309 O O   . PRO B 1 28  ? 6.413   8.239   39.901  1.00 11.51 ? 28  PRO B O   1 
ATOM   1310 C CB  . PRO B 1 28  ? 7.853   8.190   42.893  1.00 14.36 ? 28  PRO B CB  1 
ATOM   1311 C CG  . PRO B 1 28  ? 8.529   9.462   42.465  1.00 16.92 ? 28  PRO B CG  1 
ATOM   1312 C CD  . PRO B 1 28  ? 9.533   9.018   41.389  1.00 17.23 ? 28  PRO B CD  1 
ATOM   1313 N N   . VAL B 1 29  ? 5.513   6.654   41.290  1.00 14.52 ? 29  VAL B N   1 
ATOM   1314 C CA  . VAL B 1 29  ? 4.148   6.710   40.746  1.00 12.85 ? 29  VAL B CA  1 
ATOM   1315 C C   . VAL B 1 29  ? 3.289   7.544   41.719  1.00 12.71 ? 29  VAL B C   1 
ATOM   1316 O O   . VAL B 1 29  ? 3.314   7.239   42.897  1.00 12.57 ? 29  VAL B O   1 
ATOM   1317 C CB  . VAL B 1 29  ? 3.637   5.234   40.559  1.00 13.39 ? 29  VAL B CB  1 
ATOM   1318 C CG1 . VAL B 1 29  ? 2.292   5.169   39.948  1.00 13.60 ? 29  VAL B CG1 1 
ATOM   1319 C CG2 . VAL B 1 29  ? 4.580   4.507   39.679  1.00 6.25  ? 29  VAL B CG2 1 
ATOM   1320 N N   . LYS B 1 30  ? 2.615   8.617   41.259  1.00 13.56 ? 30  LYS B N   1 
ATOM   1321 C CA  . LYS B 1 30  ? 1.628   9.270   42.142  1.00 13.47 ? 30  LYS B CA  1 
ATOM   1322 C C   . LYS B 1 30  ? 0.319   8.492   42.083  1.00 12.35 ? 30  LYS B C   1 
ATOM   1323 O O   . LYS B 1 30  ? -0.114  8.078   41.016  1.00 10.91 ? 30  LYS B O   1 
ATOM   1324 C CB  . LYS B 1 30  ? 1.388   10.796  41.904  1.00 14.28 ? 30  LYS B CB  1 
ATOM   1325 C CG  . LYS B 1 30  ? 2.647   11.602  41.627  1.00 16.06 ? 30  LYS B CG  1 
ATOM   1326 C CD  . LYS B 1 30  ? 2.427   13.172  41.549  1.00 15.08 ? 30  LYS B CD  1 
ATOM   1327 C CE  . LYS B 1 30  ? 3.791   13.882  41.294  1.00 15.98 ? 30  LYS B CE  1 
ATOM   1328 N NZ  . LYS B 1 30  ? 3.818   15.443  41.655  1.00 21.10 ? 30  LYS B NZ  1 
ATOM   1329 N N   . VAL B 1 31  ? -0.304  8.293   43.255  1.00 11.94 ? 31  VAL B N   1 
ATOM   1330 C CA  . VAL B 1 31  ? -1.553  7.567   43.383  1.00 12.09 ? 31  VAL B CA  1 
ATOM   1331 C C   . VAL B 1 31  ? -2.550  8.419   44.122  1.00 13.39 ? 31  VAL B C   1 
ATOM   1332 O O   . VAL B 1 31  ? -2.237  8.934   45.174  1.00 14.45 ? 31  VAL B O   1 
ATOM   1333 C CB  . VAL B 1 31  ? -1.328  6.253   44.131  1.00 12.49 ? 31  VAL B CB  1 
ATOM   1334 C CG1 . VAL B 1 31  ? -2.607  5.436   44.115  1.00 9.73  ? 31  VAL B CG1 1 
ATOM   1335 C CG2 . VAL B 1 31  ? -0.229  5.509   43.429  1.00 10.42 ? 31  VAL B CG2 1 
ATOM   1336 N N   . TRP B 1 32  ? -3.730  8.628   43.560  1.00 14.05 ? 32  TRP B N   1 
ATOM   1337 C CA  . TRP B 1 32  ? -4.631  9.617   44.147  1.00 14.03 ? 32  TRP B CA  1 
ATOM   1338 C C   . TRP B 1 32  ? -6.080  9.465   43.689  1.00 13.41 ? 32  TRP B C   1 
ATOM   1339 O O   . TRP B 1 32  ? -6.354  8.987   42.575  1.00 12.98 ? 32  TRP B O   1 
ATOM   1340 C CB  . TRP B 1 32  ? -4.113  11.069  43.880  1.00 14.20 ? 32  TRP B CB  1 
ATOM   1341 C CG  . TRP B 1 32  ? -4.545  11.573  42.590  1.00 14.08 ? 32  TRP B CG  1 
ATOM   1342 C CD1 . TRP B 1 32  ? -5.752  12.134  42.310  1.00 19.04 ? 32  TRP B CD1 1 
ATOM   1343 C CD2 . TRP B 1 32  ? -3.838  11.491  41.338  1.00 12.01 ? 32  TRP B CD2 1 
ATOM   1344 N NE1 . TRP B 1 32  ? -5.824  12.441  40.966  1.00 19.29 ? 32  TRP B NE1 1 
ATOM   1345 C CE2 . TRP B 1 32  ? -4.667  12.028  40.354  1.00 16.37 ? 32  TRP B CE2 1 
ATOM   1346 C CE3 . TRP B 1 32  ? -2.576  11.039  40.971  1.00 13.54 ? 32  TRP B CE3 1 
ATOM   1347 C CZ2 . TRP B 1 32  ? -4.276  12.127  39.007  1.00 17.49 ? 32  TRP B CZ2 1 
ATOM   1348 C CZ3 . TRP B 1 32  ? -2.188  11.140  39.651  1.00 16.42 ? 32  TRP B CZ3 1 
ATOM   1349 C CH2 . TRP B 1 32  ? -3.039  11.655  38.683  1.00 17.97 ? 32  TRP B CH2 1 
ATOM   1350 N N   . GLY B 1 33  ? -7.000  9.898   44.543  1.00 12.27 ? 33  GLY B N   1 
ATOM   1351 C CA  . GLY B 1 33  ? -8.431  9.732   44.281  1.00 13.49 ? 33  GLY B CA  1 
ATOM   1352 C C   . GLY B 1 33  ? -9.236  9.692   45.556  1.00 12.89 ? 33  GLY B C   1 
ATOM   1353 O O   . GLY B 1 33  ? -8.777  10.203  46.572  1.00 14.04 ? 33  GLY B O   1 
ATOM   1354 N N   . SER B 1 34  ? -10.457 9.129   45.511  1.00 14.87 ? 34  SER B N   1 
ATOM   1355 C CA  . SER B 1 34  ? -11.306 8.857   46.694  1.00 14.80 ? 34  SER B CA  1 
ATOM   1356 C C   . SER B 1 34  ? -11.959 7.468   46.570  1.00 15.53 ? 34  SER B C   1 
ATOM   1357 O O   . SER B 1 34  ? -12.165 6.945   45.478  1.00 16.28 ? 34  SER B O   1 
ATOM   1358 C CB  . SER B 1 34  ? -12.429 9.855   46.830  1.00 16.49 ? 34  SER B CB  1 
ATOM   1359 O OG  . SER B 1 34  ? -11.885 11.158  46.714  1.00 21.65 ? 34  SER B OG  1 
ATOM   1360 N N   . ILE B 1 35  ? -12.276 6.899   47.707  1.00 14.99 ? 35  ILE B N   1 
ATOM   1361 C CA  . ILE B 1 35  ? -13.073 5.688   47.784  1.00 12.95 ? 35  ILE B CA  1 
ATOM   1362 C C   . ILE B 1 35  ? -14.147 6.109   48.826  1.00 14.02 ? 35  ILE B C   1 
ATOM   1363 O O   . ILE B 1 35  ? -13.785 6.652   49.861  1.00 14.75 ? 35  ILE B O   1 
ATOM   1364 C CB  . ILE B 1 35  ? -12.252 4.426   48.247  1.00 13.27 ? 35  ILE B CB  1 
ATOM   1365 C CG1 . ILE B 1 35  ? -11.022 4.144   47.370  1.00 9.15  ? 35  ILE B CG1 1 
ATOM   1366 C CG2 . ILE B 1 35  ? -13.100 3.179   48.075  1.00 14.20 ? 35  ILE B CG2 1 
ATOM   1367 C CD1 . ILE B 1 35  ? -9.763  3.777   48.172  1.00 6.47  ? 35  ILE B CD1 1 
ATOM   1368 N N   . LYS B 1 36  ? -15.439 5.899   48.552  1.00 14.58 ? 36  LYS B N   1 
ATOM   1369 C CA  . LYS B 1 36  ? -16.488 6.009   49.591  1.00 15.22 ? 36  LYS B CA  1 
ATOM   1370 C C   . LYS B 1 36  ? -17.169 4.617   49.854  1.00 15.18 ? 36  LYS B C   1 
ATOM   1371 O O   . LYS B 1 36  ? -16.903 3.680   49.128  1.00 13.73 ? 36  LYS B O   1 
ATOM   1372 C CB  . LYS B 1 36  ? -17.471 7.147   49.233  1.00 16.91 ? 36  LYS B CB  1 
ATOM   1373 C CG  . LYS B 1 36  ? -17.781 7.221   47.760  1.00 18.72 ? 36  LYS B CG  1 
ATOM   1374 C CD  . LYS B 1 36  ? -19.105 7.821   47.471  1.00 20.85 ? 36  LYS B CD  1 
ATOM   1375 C CE  . LYS B 1 36  ? -19.598 7.288   46.168  1.00 20.03 ? 36  LYS B CE  1 
ATOM   1376 N NZ  . LYS B 1 36  ? -20.933 7.869   45.939  1.00 22.30 ? 36  LYS B NZ  1 
ATOM   1377 N N   . GLY B 1 37  ? -17.983 4.469   50.909  1.00 15.11 ? 37  GLY B N   1 
ATOM   1378 C CA  . GLY B 1 37  ? -18.715 3.190   51.192  1.00 15.10 ? 37  GLY B CA  1 
ATOM   1379 C C   . GLY B 1 37  ? -18.068 2.407   52.326  1.00 14.82 ? 37  GLY B C   1 
ATOM   1380 O O   . GLY B 1 37  ? -18.315 1.160   52.588  1.00 15.23 ? 37  GLY B O   1 
ATOM   1381 N N   . LEU B 1 38  ? -17.173 3.123   52.983  1.00 13.79 ? 38  LEU B N   1 
ATOM   1382 C CA  . LEU B 1 38  ? -16.147 2.467   53.770  1.00 13.29 ? 38  LEU B CA  1 
ATOM   1383 C C   . LEU B 1 38  ? -16.437 2.641   55.231  1.00 13.40 ? 38  LEU B C   1 
ATOM   1384 O O   . LEU B 1 38  ? -16.803 3.722   55.650  1.00 11.56 ? 38  LEU B O   1 
ATOM   1385 C CB  . LEU B 1 38  ? -14.771 3.014   53.374  1.00 12.32 ? 38  LEU B CB  1 
ATOM   1386 C CG  . LEU B 1 38  ? -13.677 2.179   52.655  1.00 10.51 ? 38  LEU B CG  1 
ATOM   1387 C CD1 . LEU B 1 38  ? -13.829 0.662   52.114  1.00 2.00  ? 38  LEU B CD1 1 
ATOM   1388 C CD2 . LEU B 1 38  ? -12.954 2.952   51.665  1.00 8.96  ? 38  LEU B CD2 1 
ATOM   1389 N N   . THR B 1 39  ? -16.261 1.576   56.023  1.00 14.30 ? 39  THR B N   1 
ATOM   1390 C CA  . THR B 1 39  ? -16.273 1.779   57.474  1.00 15.57 ? 39  THR B CA  1 
ATOM   1391 C C   . THR B 1 39  ? -15.109 2.663   57.875  1.00 18.16 ? 39  THR B C   1 
ATOM   1392 O O   . THR B 1 39  ? -13.970 2.391   57.456  1.00 17.82 ? 39  THR B O   1 
ATOM   1393 C CB  . THR B 1 39  ? -16.017 0.495   58.223  1.00 15.67 ? 39  THR B CB  1 
ATOM   1394 O OG1 . THR B 1 39  ? -14.730 0.053   57.853  1.00 10.67 ? 39  THR B OG1 1 
ATOM   1395 C CG2 . THR B 1 39  ? -17.080 -0.580  57.906  1.00 14.44 ? 39  THR B CG2 1 
ATOM   1396 N N   . GLU B 1 40  ? -15.366 3.710   58.685  1.00 20.76 ? 40  GLU B N   1 
ATOM   1397 C CA  . GLU B 1 40  ? -14.319 4.635   59.125  1.00 22.63 ? 40  GLU B CA  1 
ATOM   1398 C C   . GLU B 1 40  ? -13.123 3.871   59.695  1.00 22.37 ? 40  GLU B C   1 
ATOM   1399 O O   . GLU B 1 40  ? -13.250 2.799   60.307  1.00 23.03 ? 40  GLU B O   1 
ATOM   1400 C CB  . GLU B 1 40  ? -14.879 5.663   60.113  1.00 22.67 ? 40  GLU B CB  1 
ATOM   1401 C CG  . GLU B 1 40  ? -13.948 6.265   61.157  1.00 23.57 ? 40  GLU B CG  1 
ATOM   1402 C CD  . GLU B 1 40  ? -14.706 7.128   62.186  1.00 26.42 ? 40  GLU B CD  1 
ATOM   1403 O OE1 . GLU B 1 40  ? -15.808 6.718   62.673  1.00 27.05 ? 40  GLU B OE1 1 
ATOM   1404 O OE2 . GLU B 1 40  ? -14.196 8.234   62.507  1.00 30.17 ? 40  GLU B OE2 1 
ATOM   1405 N N   . GLY B 1 41  ? -11.945 4.407   59.449  1.00 22.59 ? 41  GLY B N   1 
ATOM   1406 C CA  . GLY B 1 41  ? -10.740 3.688   59.810  1.00 22.05 ? 41  GLY B CA  1 
ATOM   1407 C C   . GLY B 1 41  ? -9.881  3.250   58.651  1.00 21.25 ? 41  GLY B C   1 
ATOM   1408 O O   . GLY B 1 41  ? -9.980  3.762   57.544  1.00 22.67 ? 41  GLY B O   1 
ATOM   1409 N N   . LEU B 1 42  ? -9.009  2.288   58.943  1.00 19.76 ? 42  LEU B N   1 
ATOM   1410 C CA  . LEU B 1 42  ? -7.891  1.998   58.108  1.00 17.29 ? 42  LEU B CA  1 
ATOM   1411 C C   . LEU B 1 42  ? -8.256  0.799   57.261  1.00 16.58 ? 42  LEU B C   1 
ATOM   1412 O O   . LEU B 1 42  ? -8.847  -0.182  57.795  1.00 17.96 ? 42  LEU B O   1 
ATOM   1413 C CB  . LEU B 1 42  ? -6.743  1.671   59.035  1.00 16.07 ? 42  LEU B CB  1 
ATOM   1414 C CG  . LEU B 1 42  ? -5.449  2.450   58.880  1.00 16.77 ? 42  LEU B CG  1 
ATOM   1415 C CD1 . LEU B 1 42  ? -5.603  3.826   58.266  1.00 15.93 ? 42  LEU B CD1 1 
ATOM   1416 C CD2 . LEU B 1 42  ? -4.856  2.565   60.243  1.00 20.30 ? 42  LEU B CD2 1 
ATOM   1417 N N   . HIS B 1 43  ? -7.899  0.846   55.976  1.00 14.24 ? 43  HIS B N   1 
ATOM   1418 C CA  . HIS B 1 43  ? -8.209  -0.227  55.051  1.00 13.15 ? 43  HIS B CA  1 
ATOM   1419 C C   . HIS B 1 43  ? -7.045  -0.679  54.186  1.00 12.48 ? 43  HIS B C   1 
ATOM   1420 O O   . HIS B 1 43  ? -6.490  0.102   53.428  1.00 12.10 ? 43  HIS B O   1 
ATOM   1421 C CB  . HIS B 1 43  ? -9.362  0.221   54.131  1.00 14.60 ? 43  HIS B CB  1 
ATOM   1422 C CG  . HIS B 1 43  ? -10.682 0.282   54.829  1.00 13.71 ? 43  HIS B CG  1 
ATOM   1423 N ND1 . HIS B 1 43  ? -11.422 -0.855  55.128  1.00 5.14  ? 43  HIS B ND1 1 
ATOM   1424 C CD2 . HIS B 1 43  ? -11.366 1.336   55.334  1.00 2.00  ? 43  HIS B CD2 1 
ATOM   1425 C CE1 . HIS B 1 43  ? -12.533 -0.493  55.761  1.00 9.46  ? 43  HIS B CE1 1 
ATOM   1426 N NE2 . HIS B 1 43  ? -12.513 0.832   55.913  1.00 6.90  ? 43  HIS B NE2 1 
ATOM   1427 N N   . GLY B 1 44  ? -6.693  -1.952  54.221  1.00 11.16 ? 44  GLY B N   1 
ATOM   1428 C CA  . GLY B 1 44  ? -5.670  -2.416  53.293  1.00 10.95 ? 44  GLY B CA  1 
ATOM   1429 C C   . GLY B 1 44  ? -5.830  -1.929  51.848  1.00 10.59 ? 44  GLY B C   1 
ATOM   1430 O O   . GLY B 1 44  ? -6.917  -1.837  51.345  1.00 11.86 ? 44  GLY B O   1 
ATOM   1431 N N   . PHE B 1 45  ? -4.734  -1.736  51.133  1.00 10.04 ? 45  PHE B N   1 
ATOM   1432 C CA  . PHE B 1 45  ? -4.775  -1.106  49.852  1.00 10.03 ? 45  PHE B CA  1 
ATOM   1433 C C   . PHE B 1 45  ? -3.623  -1.700  49.075  1.00 11.44 ? 45  PHE B C   1 
ATOM   1434 O O   . PHE B 1 45  ? -2.505  -1.420  49.389  1.00 12.38 ? 45  PHE B O   1 
ATOM   1435 C CB  . PHE B 1 45  ? -4.645  0.380   50.123  1.00 10.00 ? 45  PHE B CB  1 
ATOM   1436 C CG  . PHE B 1 45  ? -4.836  1.238   48.921  1.00 9.40  ? 45  PHE B CG  1 
ATOM   1437 C CD1 . PHE B 1 45  ? -6.074  1.255   48.241  1.00 11.39 ? 45  PHE B CD1 1 
ATOM   1438 C CD2 . PHE B 1 45  ? -3.797  2.011   48.477  1.00 11.06 ? 45  PHE B CD2 1 
ATOM   1439 C CE1 . PHE B 1 45  ? -6.300  2.069   47.145  1.00 4.29  ? 45  PHE B CE1 1 
ATOM   1440 C CE2 . PHE B 1 45  ? -3.965  2.778   47.352  1.00 7.09  ? 45  PHE B CE2 1 
ATOM   1441 C CZ  . PHE B 1 45  ? -5.254  2.836   46.708  1.00 9.14  ? 45  PHE B CZ  1 
ATOM   1442 N N   . HIS B 1 46  ? -3.900  -2.638  48.149  1.00 10.08 ? 46  HIS B N   1 
ATOM   1443 C CA  . HIS B 1 46  ? -2.864  -3.531  47.625  1.00 9.77  ? 46  HIS B CA  1 
ATOM   1444 C C   . HIS B 1 46  ? -3.065  -3.785  46.177  1.00 7.85  ? 46  HIS B C   1 
ATOM   1445 O O   . HIS B 1 46  ? -4.270  -3.887  45.731  1.00 8.51  ? 46  HIS B O   1 
ATOM   1446 C CB  . HIS B 1 46  ? -3.012  -4.931  48.254  1.00 9.15  ? 46  HIS B CB  1 
ATOM   1447 C CG  . HIS B 1 46  ? -2.961  -4.970  49.743  1.00 9.31  ? 46  HIS B CG  1 
ATOM   1448 N ND1 . HIS B 1 46  ? -3.797  -5.792  50.467  1.00 9.49  ? 46  HIS B ND1 1 
ATOM   1449 C CD2 . HIS B 1 46  ? -2.167  -4.352  50.651  1.00 9.86  ? 46  HIS B CD2 1 
ATOM   1450 C CE1 . HIS B 1 46  ? -3.573  -5.636  51.751  1.00 6.80  ? 46  HIS B CE1 1 
ATOM   1451 N NE2 . HIS B 1 46  ? -2.580  -4.777  51.893  1.00 7.67  ? 46  HIS B NE2 1 
ATOM   1452 N N   . VAL B 1 47  ? -1.949  -3.986  45.446  1.00 7.43  ? 47  VAL B N   1 
ATOM   1453 C CA  . VAL B 1 47  ? -1.959  -4.515  44.096  1.00 2.79  ? 47  VAL B CA  1 
ATOM   1454 C C   . VAL B 1 47  ? -1.904  -6.070  44.234  1.00 5.61  ? 47  VAL B C   1 
ATOM   1455 O O   . VAL B 1 47  ? -0.958  -6.609  44.825  1.00 3.28  ? 47  VAL B O   1 
ATOM   1456 C CB  . VAL B 1 47  ? -0.862  -3.895  43.164  1.00 5.50  ? 47  VAL B CB  1 
ATOM   1457 C CG1 . VAL B 1 47  ? -1.080  -4.303  41.733  1.00 6.48  ? 47  VAL B CG1 1 
ATOM   1458 C CG2 . VAL B 1 47  ? -0.962  -2.338  43.238  1.00 2.00  ? 47  VAL B CG2 1 
ATOM   1459 N N   . HIS B 1 48  ? -2.921  -6.700  43.658  1.00 5.39  ? 48  HIS B N   1 
ATOM   1460 C CA  . HIS B 1 48  ? -3.000  -8.211  43.553  1.00 5.96  ? 48  HIS B CA  1 
ATOM   1461 C C   . HIS B 1 48  ? -2.556  -8.692  42.197  1.00 5.34  ? 48  HIS B C   1 
ATOM   1462 O O   . HIS B 1 48  ? -2.558  -7.929  41.257  1.00 3.52  ? 48  HIS B O   1 
ATOM   1463 C CB  . HIS B 1 48  ? -4.450  -8.603  43.833  1.00 2.78  ? 48  HIS B CB  1 
ATOM   1464 C CG  . HIS B 1 48  ? -4.767  -8.564  45.283  1.00 7.30  ? 48  HIS B CG  1 
ATOM   1465 N ND1 . HIS B 1 48  ? -5.006  -9.702  46.021  1.00 6.56  ? 48  HIS B ND1 1 
ATOM   1466 C CD2 . HIS B 1 48  ? -4.884  -7.528  46.135  1.00 2.46  ? 48  HIS B CD2 1 
ATOM   1467 C CE1 . HIS B 1 48  ? -5.248  -9.375  47.268  1.00 8.76  ? 48  HIS B CE1 1 
ATOM   1468 N NE2 . HIS B 1 48  ? -5.143  -8.062  47.372  1.00 3.77  ? 48  HIS B NE2 1 
ATOM   1469 N N   . GLU B 1 49  ? -2.214  -9.990  42.022  1.00 5.96  ? 49  GLU B N   1 
ATOM   1470 C CA  . GLU B 1 49  ? -1.362  -10.285 40.832  1.00 7.03  ? 49  GLU B CA  1 
ATOM   1471 C C   . GLU B 1 49  ? -2.105  -10.131 39.490  1.00 8.89  ? 49  GLU B C   1 
ATOM   1472 O O   . GLU B 1 49  ? -1.525  -9.806  38.432  1.00 9.39  ? 49  GLU B O   1 
ATOM   1473 C CB  . GLU B 1 49  ? -0.809  -11.725 40.966  1.00 7.41  ? 49  GLU B CB  1 
ATOM   1474 C CG  . GLU B 1 49  ? 0.478   -11.953 40.252  1.00 8.60  ? 49  GLU B CG  1 
ATOM   1475 C CD  . GLU B 1 49  ? 0.833   -13.428 40.297  1.00 12.28 ? 49  GLU B CD  1 
ATOM   1476 O OE1 . GLU B 1 49  ? 0.542   -14.069 41.325  1.00 9.91  ? 49  GLU B OE1 1 
ATOM   1477 O OE2 . GLU B 1 49  ? 1.394   -13.915 39.320  1.00 12.66 ? 49  GLU B OE2 1 
ATOM   1478 N N   . PHE B 1 50  ? -3.405  -10.376 39.509  1.00 9.32  ? 50  PHE B N   1 
ATOM   1479 C CA  . PHE B 1 50  ? -4.144  -10.601 38.285  1.00 8.06  ? 50  PHE B CA  1 
ATOM   1480 C C   . PHE B 1 50  ? -5.247  -9.638  38.001  1.00 9.21  ? 50  PHE B C   1 
ATOM   1481 O O   . PHE B 1 50  ? -6.055  -9.320  38.895  1.00 7.26  ? 50  PHE B O   1 
ATOM   1482 C CB  . PHE B 1 50  ? -4.695  -12.047 38.298  1.00 11.44 ? 50  PHE B CB  1 
ATOM   1483 C CG  . PHE B 1 50  ? -3.637  -13.052 38.455  1.00 8.42  ? 50  PHE B CG  1 
ATOM   1484 C CD1 . PHE B 1 50  ? -2.635  -13.151 37.513  1.00 13.24 ? 50  PHE B CD1 1 
ATOM   1485 C CD2 . PHE B 1 50  ? -3.637  -13.914 39.527  1.00 16.06 ? 50  PHE B CD2 1 
ATOM   1486 C CE1 . PHE B 1 50  ? -1.597  -14.133 37.623  1.00 16.81 ? 50  PHE B CE1 1 
ATOM   1487 C CE2 . PHE B 1 50  ? -2.604  -14.921 39.687  1.00 17.12 ? 50  PHE B CE2 1 
ATOM   1488 C CZ  . PHE B 1 50  ? -1.583  -15.025 38.721  1.00 16.66 ? 50  PHE B CZ  1 
ATOM   1489 N N   . GLY B 1 51  ? -5.364  -9.232  36.736  1.00 7.41  ? 51  GLY B N   1 
ATOM   1490 C CA  . GLY B 1 51  ? -6.574  -8.512  36.361  1.00 10.12 ? 51  GLY B CA  1 
ATOM   1491 C C   . GLY B 1 51  ? -7.796  -9.338  35.976  1.00 10.81 ? 51  GLY B C   1 
ATOM   1492 O O   . GLY B 1 51  ? -8.419  -9.118  34.890  1.00 10.81 ? 51  GLY B O   1 
ATOM   1493 N N   . ASP B 1 52  ? -8.174  -10.250 36.894  1.00 10.16 ? 52  ASP B N   1 
ATOM   1494 C CA  . ASP B 1 52  ? -9.155  -11.277 36.621  1.00 9.74  ? 52  ASP B CA  1 
ATOM   1495 C C   . ASP B 1 52  ? -10.278 -11.054 37.618  1.00 8.26  ? 52  ASP B C   1 
ATOM   1496 O O   . ASP B 1 52  ? -10.088 -11.115 38.848  1.00 8.55  ? 52  ASP B O   1 
ATOM   1497 C CB  . ASP B 1 52  ? -8.459  -12.625 36.832  1.00 9.29  ? 52  ASP B CB  1 
ATOM   1498 C CG  . ASP B 1 52  ? -9.294  -13.793 36.423  1.00 13.89 ? 52  ASP B CG  1 
ATOM   1499 O OD1 . ASP B 1 52  ? -10.520 -13.721 36.562  1.00 16.77 ? 52  ASP B OD1 1 
ATOM   1500 O OD2 . ASP B 1 52  ? -8.714  -14.826 36.033  1.00 19.72 ? 52  ASP B OD2 1 
ATOM   1501 N N   . ASN B 1 53  ? -11.441 -10.720 37.082  1.00 8.32  ? 53  ASN B N   1 
ATOM   1502 C CA  . ASN B 1 53  ? -12.595 -10.450 37.871  1.00 6.00  ? 53  ASN B CA  1 
ATOM   1503 C C   . ASN B 1 53  ? -13.746 -11.349 37.586  1.00 9.06  ? 53  ASN B C   1 
ATOM   1504 O O   . ASN B 1 53  ? -14.902 -11.037 37.895  1.00 7.31  ? 53  ASN B O   1 
ATOM   1505 C CB  . ASN B 1 53  ? -13.066 -8.994  37.770  1.00 7.82  ? 53  ASN B CB  1 
ATOM   1506 C CG  . ASN B 1 53  ? -13.991 -8.733  38.809  1.00 8.40  ? 53  ASN B CG  1 
ATOM   1507 O OD1 . ASN B 1 53  ? -13.643 -8.912  40.003  1.00 14.25 ? 53  ASN B OD1 1 
ATOM   1508 N ND2 . ASN B 1 53  ? -15.247 -8.548  38.438  1.00 12.87 ? 53  ASN B ND2 1 
ATOM   1509 N N   . THR B 1 54  ? -13.391 -12.515 37.051  1.00 10.29 ? 54  THR B N   1 
ATOM   1510 C CA  . THR B 1 54  ? -14.356 -13.456 36.504  1.00 14.64 ? 54  THR B CA  1 
ATOM   1511 C C   . THR B 1 54  ? -15.259 -13.954 37.579  1.00 14.69 ? 54  THR B C   1 
ATOM   1512 O O   . THR B 1 54  ? -16.414 -14.268 37.303  1.00 16.71 ? 54  THR B O   1 
ATOM   1513 C CB  . THR B 1 54  ? -13.659 -14.634 36.007  1.00 12.58 ? 54  THR B CB  1 
ATOM   1514 O OG1 . THR B 1 54  ? -12.691 -14.901 36.972  1.00 14.62 ? 54  THR B OG1 1 
ATOM   1515 C CG2 . THR B 1 54  ? -12.930 -14.303 34.705  1.00 17.58 ? 54  THR B CG2 1 
ATOM   1516 N N   . ALA B 1 55  ? -14.718 -14.038 38.792  1.00 16.03 ? 55  ALA B N   1 
ATOM   1517 C CA  . ALA B 1 55  ? -15.450 -14.513 39.986  1.00 14.87 ? 55  ALA B CA  1 
ATOM   1518 C C   . ALA B 1 55  ? -15.368 -13.440 41.068  1.00 13.83 ? 55  ALA B C   1 
ATOM   1519 O O   . ALA B 1 55  ? -15.413 -13.682 42.245  1.00 13.79 ? 55  ALA B O   1 
ATOM   1520 C CB  . ALA B 1 55  ? -14.916 -15.842 40.481  1.00 15.13 ? 55  ALA B CB  1 
ATOM   1521 N N   . GLY B 1 56  ? -15.325 -12.205 40.662  1.00 13.83 ? 56  GLY B N   1 
ATOM   1522 C CA  . GLY B 1 56  ? -15.317 -11.113 41.636  1.00 11.23 ? 56  GLY B CA  1 
ATOM   1523 C C   . GLY B 1 56  ? -13.896 -10.831 41.998  1.00 10.80 ? 56  GLY B C   1 
ATOM   1524 O O   . GLY B 1 56  ? -13.003 -11.255 41.273  1.00 12.53 ? 56  GLY B O   1 
ATOM   1525 N N   . CYS B 1 57  ? -13.673 -10.163 43.129  1.00 12.00 ? 57  CYS B N   1 
ATOM   1526 C CA  . CYS B 1 57  ? -12.352 -9.816  43.559  1.00 11.55 ? 57  CYS B CA  1 
ATOM   1527 C C   . CYS B 1 57  ? -11.472 -11.001 43.947  1.00 12.82 ? 57  CYS B C   1 
ATOM   1528 O O   . CYS B 1 57  ? -10.248 -10.876 43.919  1.00 13.20 ? 57  CYS B O   1 
ATOM   1529 C CB  . CYS B 1 57  ? -12.374 -8.814  44.664  1.00 12.29 ? 57  CYS B CB  1 
ATOM   1530 S SG  . CYS B 1 57  ? -13.245 -7.258  44.186  1.00 10.50 ? 57  CYS B SG  1 
ATOM   1531 N N   . THR B 1 58  ? -12.054 -12.125 44.342  1.00 10.73 ? 58  THR B N   1 
ATOM   1532 C CA  . THR B 1 58  ? -11.198 -13.240 44.738  1.00 12.24 ? 58  THR B CA  1 
ATOM   1533 C C   . THR B 1 58  ? -10.251 -13.710 43.629  1.00 12.18 ? 58  THR B C   1 
ATOM   1534 O O   . THR B 1 58  ? -9.213  -14.321 43.889  1.00 12.00 ? 58  THR B O   1 
ATOM   1535 C CB  . THR B 1 58  ? -12.020 -14.371 45.308  1.00 11.21 ? 58  THR B CB  1 
ATOM   1536 O OG1 . THR B 1 58  ? -12.801 -14.901 44.280  1.00 13.80 ? 58  THR B OG1 1 
ATOM   1537 C CG2 . THR B 1 58  ? -12.991 -13.857 46.277  1.00 13.21 ? 58  THR B CG2 1 
ATOM   1538 N N   . SER B 1 59  ? -10.577 -13.317 42.391  1.00 14.06 ? 59  SER B N   1 
ATOM   1539 C CA  . SER B 1 59  ? -9.949  -13.827 41.178  1.00 12.99 ? 59  SER B CA  1 
ATOM   1540 C C   . SER B 1 59  ? -8.598  -13.185 40.903  1.00 12.07 ? 59  SER B C   1 
ATOM   1541 O O   . SER B 1 59  ? -7.748  -13.742 40.204  1.00 12.19 ? 59  SER B O   1 
ATOM   1542 C CB  . SER B 1 59  ? -10.864 -13.514 40.039  1.00 12.01 ? 59  SER B CB  1 
ATOM   1543 O OG  . SER B 1 59  ? -12.178 -13.838 40.353  1.00 14.25 ? 59  SER B OG  1 
ATOM   1544 N N   . ALA B 1 60  ? -8.442  -11.963 41.418  1.00 11.51 ? 60  ALA B N   1 
ATOM   1545 C CA  . ALA B 1 60  ? -7.236  -11.238 41.345  1.00 10.63 ? 60  ALA B CA  1 
ATOM   1546 C C   . ALA B 1 60  ? -6.113  -12.060 41.917  1.00 11.47 ? 60  ALA B C   1 
ATOM   1547 O O   . ALA B 1 60  ? -4.965  -11.836 41.628  1.00 10.55 ? 60  ALA B O   1 
ATOM   1548 C CB  . ALA B 1 60  ? -7.367  -10.057 42.150  1.00 9.63  ? 60  ALA B CB  1 
ATOM   1549 N N   . GLY B 1 61  ? -6.430  -12.970 42.821  1.00 12.38 ? 61  GLY B N   1 
ATOM   1550 C CA  . GLY B 1 61  ? -5.393  -13.719 43.500  1.00 11.66 ? 61  GLY B CA  1 
ATOM   1551 C C   . GLY B 1 61  ? -4.647  -12.997 44.587  1.00 11.97 ? 61  GLY B C   1 
ATOM   1552 O O   . GLY B 1 61  ? -5.224  -12.106 45.292  1.00 11.23 ? 61  GLY B O   1 
ATOM   1553 N N   . PRO B 1 62  ? -3.378  -13.407 44.790  1.00 12.63 ? 62  PRO B N   1 
ATOM   1554 C CA  . PRO B 1 62  ? -2.426  -12.884 45.797  1.00 11.56 ? 62  PRO B CA  1 
ATOM   1555 C C   . PRO B 1 62  ? -1.969  -11.447 45.509  1.00 13.31 ? 62  PRO B C   1 
ATOM   1556 O O   . PRO B 1 62  ? -2.482  -10.826 44.586  1.00 13.98 ? 62  PRO B O   1 
ATOM   1557 C CB  . PRO B 1 62  ? -1.249  -13.860 45.727  1.00 12.27 ? 62  PRO B CB  1 
ATOM   1558 C CG  . PRO B 1 62  ? -1.338  -14.526 44.329  1.00 12.85 ? 62  PRO B CG  1 
ATOM   1559 C CD  . PRO B 1 62  ? -2.836  -14.569 43.999  1.00 12.93 ? 62  PRO B CD  1 
ATOM   1560 N N   . HIS B 1 63  ? -1.052  -10.925 46.314  1.00 13.40 ? 63  HIS B N   1 
ATOM   1561 C CA  . HIS B 1 63  ? -0.475  -9.593  46.118  1.00 13.74 ? 63  HIS B CA  1 
ATOM   1562 C C   . HIS B 1 63  ? 0.404   -9.614  44.925  1.00 13.35 ? 63  HIS B C   1 
ATOM   1563 O O   . HIS B 1 63  ? 1.023   -10.628 44.616  1.00 12.50 ? 63  HIS B O   1 
ATOM   1564 C CB  . HIS B 1 63  ? 0.343   -9.192  47.337  1.00 14.19 ? 63  HIS B CB  1 
ATOM   1565 C CG  . HIS B 1 63  ? -0.503  -8.855  48.517  1.00 14.59 ? 63  HIS B CG  1 
ATOM   1566 N ND1 . HIS B 1 63  ? 0.007   -8.392  49.714  1.00 13.44 ? 63  HIS B ND1 1 
ATOM   1567 C CD2 . HIS B 1 63  ? -1.838  -8.938  48.683  1.00 11.11 ? 63  HIS B CD2 1 
ATOM   1568 C CE1 . HIS B 1 63  ? -0.977  -8.259  50.578  1.00 12.72 ? 63  HIS B CE1 1 
ATOM   1569 N NE2 . HIS B 1 63  ? -2.109  -8.565  49.966  1.00 13.52 ? 63  HIS B NE2 1 
ATOM   1570 N N   . PHE B 1 64  ? 0.515   -8.508  44.214  1.00 11.86 ? 64  PHE B N   1 
ATOM   1571 C CA  . PHE B 1 64  ? 1.608   -8.558  43.279  1.00 11.85 ? 64  PHE B CA  1 
ATOM   1572 C C   . PHE B 1 64  ? 2.937   -8.591  44.096  1.00 11.78 ? 64  PHE B C   1 
ATOM   1573 O O   . PHE B 1 64  ? 3.303   -7.584  44.751  1.00 11.67 ? 64  PHE B O   1 
ATOM   1574 C CB  . PHE B 1 64  ? 1.512   -7.377  42.332  1.00 10.04 ? 64  PHE B CB  1 
ATOM   1575 C CG  . PHE B 1 64  ? 2.538   -7.390  41.239  1.00 8.06  ? 64  PHE B CG  1 
ATOM   1576 C CD1 . PHE B 1 64  ? 2.848   -8.572  40.584  1.00 5.28  ? 64  PHE B CD1 1 
ATOM   1577 C CD2 . PHE B 1 64  ? 3.094   -6.221  40.785  1.00 2.00  ? 64  PHE B CD2 1 
ATOM   1578 C CE1 . PHE B 1 64  ? 3.748   -8.599  39.645  1.00 3.62  ? 64  PHE B CE1 1 
ATOM   1579 C CE2 . PHE B 1 64  ? 3.945   -6.268  39.769  1.00 2.00  ? 64  PHE B CE2 1 
ATOM   1580 C CZ  . PHE B 1 64  ? 4.286   -7.447  39.207  1.00 8.03  ? 64  PHE B CZ  1 
ATOM   1581 N N   . ASN B 1 65  ? 3.660   -9.719  44.009  1.00 13.34 ? 65  ASN B N   1 
ATOM   1582 C CA  . ASN B 1 65  ? 4.974   -9.977  44.692  1.00 14.24 ? 65  ASN B CA  1 
ATOM   1583 C C   . ASN B 1 65  ? 5.982   -10.704 43.740  1.00 15.48 ? 65  ASN B C   1 
ATOM   1584 O O   . ASN B 1 65  ? 6.220   -11.906 43.894  1.00 14.85 ? 65  ASN B O   1 
ATOM   1585 C CB  . ASN B 1 65  ? 4.686   -10.838 45.920  1.00 14.36 ? 65  ASN B CB  1 
ATOM   1586 C CG  . ASN B 1 65  ? 5.887   -11.071 46.846  1.00 15.18 ? 65  ASN B CG  1 
ATOM   1587 O OD1 . ASN B 1 65  ? 6.930   -10.381 46.834  1.00 9.10  ? 65  ASN B OD1 1 
ATOM   1588 N ND2 . ASN B 1 65  ? 5.706   -12.064 47.710  1.00 15.47 ? 65  ASN B ND2 1 
ATOM   1589 N N   . PRO B 1 66  ? 6.461   -10.021 42.677  1.00 15.42 ? 66  PRO B N   1 
ATOM   1590 C CA  . PRO B 1 66  ? 7.232   -10.727 41.685  1.00 15.56 ? 66  PRO B CA  1 
ATOM   1591 C C   . PRO B 1 66  ? 8.595   -11.289 42.197  1.00 18.34 ? 66  PRO B C   1 
ATOM   1592 O O   . PRO B 1 66  ? 9.189   -12.217 41.559  1.00 17.80 ? 66  PRO B O   1 
ATOM   1593 C CB  . PRO B 1 66  ? 7.429   -9.685  40.600  1.00 14.95 ? 66  PRO B CB  1 
ATOM   1594 C CG  . PRO B 1 66  ? 7.208   -8.390  41.190  1.00 12.91 ? 66  PRO B CG  1 
ATOM   1595 C CD  . PRO B 1 66  ? 6.322   -8.587  42.354  1.00 14.00 ? 66  PRO B CD  1 
ATOM   1596 N N   . LEU B 1 67  ? 9.065   -10.695 43.304  1.00 19.42 ? 67  LEU B N   1 
ATOM   1597 C CA  . LEU B 1 67  ? 10.394  -10.884 43.880  1.00 20.79 ? 67  LEU B CA  1 
ATOM   1598 C C   . LEU B 1 67  ? 10.331  -11.794 45.101  1.00 21.81 ? 67  LEU B C   1 
ATOM   1599 O O   . LEU B 1 67  ? 11.329  -12.021 45.711  1.00 23.46 ? 67  LEU B O   1 
ATOM   1600 C CB  . LEU B 1 67  ? 10.968  -9.547  44.355  1.00 18.98 ? 67  LEU B CB  1 
ATOM   1601 C CG  . LEU B 1 67  ? 11.100  -8.405  43.378  1.00 20.30 ? 67  LEU B CG  1 
ATOM   1602 C CD1 . LEU B 1 67  ? 11.893  -7.251  44.073  1.00 19.64 ? 67  LEU B CD1 1 
ATOM   1603 C CD2 . LEU B 1 67  ? 11.731  -8.874  42.054  1.00 19.03 ? 67  LEU B CD2 1 
ATOM   1604 N N   . SER B 1 68  ? 9.151   -12.250 45.484  1.00 23.72 ? 68  SER B N   1 
ATOM   1605 C CA  . SER B 1 68  ? 8.960   -13.283 46.535  1.00 24.99 ? 68  SER B CA  1 
ATOM   1606 C C   . SER B 1 68  ? 9.341   -12.910 47.977  1.00 25.15 ? 68  SER B C   1 
ATOM   1607 O O   . SER B 1 68  ? 9.792   -13.755 48.746  1.00 25.26 ? 68  SER B O   1 
ATOM   1608 C CB  . SER B 1 68  ? 9.599   -14.603 46.115  1.00 24.88 ? 68  SER B CB  1 
ATOM   1609 O OG  . SER B 1 68  ? 8.724   -15.273 45.247  1.00 24.54 ? 68  SER B OG  1 
ATOM   1610 N N   . ARG B 1 69  ? 9.082   -11.653 48.330  1.00 25.35 ? 69  ARG B N   1 
ATOM   1611 C CA  . ARG B 1 69  ? 9.454   -11.102 49.622  1.00 24.85 ? 69  ARG B CA  1 
ATOM   1612 C C   . ARG B 1 69  ? 8.344   -11.321 50.651  1.00 24.90 ? 69  ARG B C   1 
ATOM   1613 O O   . ARG B 1 69  ? 7.226   -11.711 50.322  1.00 24.45 ? 69  ARG B O   1 
ATOM   1614 C CB  . ARG B 1 69  ? 9.772   -9.596  49.496  1.00 24.71 ? 69  ARG B CB  1 
ATOM   1615 C CG  . ARG B 1 69  ? 10.833  -9.218  48.470  1.00 26.65 ? 69  ARG B CG  1 
ATOM   1616 C CD  . ARG B 1 69  ? 12.289  -9.271  48.973  1.00 33.60 ? 69  ARG B CD  1 
ATOM   1617 N NE  . ARG B 1 69  ? 13.158  -8.626  47.974  1.00 39.15 ? 69  ARG B NE  1 
ATOM   1618 C CZ  . ARG B 1 69  ? 13.972  -9.264  47.109  1.00 41.14 ? 69  ARG B CZ  1 
ATOM   1619 N NH1 . ARG B 1 69  ? 14.114  -10.599 47.145  1.00 39.09 ? 69  ARG B NH1 1 
ATOM   1620 N NH2 . ARG B 1 69  ? 14.673  -8.551  46.208  1.00 41.94 ? 69  ARG B NH2 1 
ATOM   1621 N N   . LYS B 1 70  ? 8.660   -11.047 51.905  1.00 24.03 ? 70  LYS B N   1 
ATOM   1622 C CA  . LYS B 1 70  ? 7.642   -11.040 52.922  1.00 23.92 ? 70  LYS B CA  1 
ATOM   1623 C C   . LYS B 1 70  ? 6.856   -9.707  52.824  1.00 21.64 ? 70  LYS B C   1 
ATOM   1624 O O   . LYS B 1 70  ? 7.390   -8.669  52.384  1.00 20.85 ? 70  LYS B O   1 
ATOM   1625 C CB  . LYS B 1 70  ? 8.260   -11.367 54.326  1.00 23.96 ? 70  LYS B CB  1 
ATOM   1626 C CG  . LYS B 1 70  ? 8.390   -10.198 55.268  1.00 26.69 ? 70  LYS B CG  1 
ATOM   1627 C CD  . LYS B 1 70  ? 9.380   -10.437 56.420  1.00 26.76 ? 70  LYS B CD  1 
ATOM   1628 C CE  . LYS B 1 70  ? 9.570   -9.133  57.181  1.00 29.37 ? 70  LYS B CE  1 
ATOM   1629 N NZ  . LYS B 1 70  ? 8.245   -8.443  57.314  1.00 28.03 ? 70  LYS B NZ  1 
ATOM   1630 N N   . HIS B 1 71  ? 5.588   -9.802  53.205  1.00 20.64 ? 71  HIS B N   1 
ATOM   1631 C CA  . HIS B 1 71  ? 4.681   -8.667  53.315  1.00 19.29 ? 71  HIS B CA  1 
ATOM   1632 C C   . HIS B 1 71  ? 5.144   -7.688  54.363  1.00 19.51 ? 71  HIS B C   1 
ATOM   1633 O O   . HIS B 1 71  ? 5.435   -8.078  55.491  1.00 20.27 ? 71  HIS B O   1 
ATOM   1634 C CB  . HIS B 1 71  ? 3.225   -9.105  53.632  1.00 18.33 ? 71  HIS B CB  1 
ATOM   1635 C CG  . HIS B 1 71  ? 2.272   -7.952  53.769  1.00 16.44 ? 71  HIS B CG  1 
ATOM   1636 N ND1 . HIS B 1 71  ? 1.865   -7.202  52.692  1.00 13.77 ? 71  HIS B ND1 1 
ATOM   1637 C CD2 . HIS B 1 71  ? 1.650   -7.429  54.847  1.00 13.64 ? 71  HIS B CD2 1 
ATOM   1638 C CE1 . HIS B 1 71  ? 1.053   -6.240  53.106  1.00 17.41 ? 71  HIS B CE1 1 
ATOM   1639 N NE2 . HIS B 1 71  ? 0.891   -6.364  54.408  1.00 17.60 ? 71  HIS B NE2 1 
ATOM   1640 N N   . GLY B 1 72  ? 5.117   -6.407  53.997  1.00 19.30 ? 72  GLY B N   1 
ATOM   1641 C CA  . GLY B 1 72  ? 5.550   -5.303  54.838  1.00 17.65 ? 72  GLY B CA  1 
ATOM   1642 C C   . GLY B 1 72  ? 4.739   -4.088  54.444  1.00 17.61 ? 72  GLY B C   1 
ATOM   1643 O O   . GLY B 1 72  ? 3.780   -4.200  53.693  1.00 18.25 ? 72  GLY B O   1 
ATOM   1644 N N   . GLY B 1 73  ? 5.072   -2.911  54.962  1.00 17.58 ? 73  GLY B N   1 
ATOM   1645 C CA  . GLY B 1 73  ? 4.342   -1.681  54.546  1.00 18.62 ? 73  GLY B CA  1 
ATOM   1646 C C   . GLY B 1 73  ? 5.043   -0.903  53.447  1.00 18.36 ? 73  GLY B C   1 
ATOM   1647 O O   . GLY B 1 73  ? 6.201   -1.149  53.167  1.00 18.38 ? 73  GLY B O   1 
ATOM   1648 N N   . PRO B 1 74  ? 4.388   0.101   52.864  1.00 18.56 ? 74  PRO B N   1 
ATOM   1649 C CA  . PRO B 1 74  ? 5.003   0.703   51.646  1.00 19.09 ? 74  PRO B CA  1 
ATOM   1650 C C   . PRO B 1 74  ? 6.426   1.207   51.859  1.00 20.21 ? 74  PRO B C   1 
ATOM   1651 O O   . PRO B 1 74  ? 7.179   1.164   50.922  1.00 19.70 ? 74  PRO B O   1 
ATOM   1652 C CB  . PRO B 1 74  ? 4.107   1.910   51.314  1.00 17.88 ? 74  PRO B CB  1 
ATOM   1653 C CG  . PRO B 1 74  ? 3.333   2.162   52.553  1.00 17.61 ? 74  PRO B CG  1 
ATOM   1654 C CD  . PRO B 1 74  ? 3.170   0.810   53.273  1.00 17.48 ? 74  PRO B CD  1 
ATOM   1655 N N   . LYS B 1 75  ? 6.760   1.673   53.080  1.00 22.54 ? 75  LYS B N   1 
ATOM   1656 C CA  . LYS B 1 75  ? 8.027   2.331   53.423  1.00 23.52 ? 75  LYS B CA  1 
ATOM   1657 C C   . LYS B 1 75  ? 9.085   1.353   53.802  1.00 24.19 ? 75  LYS B C   1 
ATOM   1658 O O   . LYS B 1 75  ? 10.229  1.742   53.877  1.00 25.42 ? 75  LYS B O   1 
ATOM   1659 C CB  . LYS B 1 75  ? 7.835   3.262   54.580  1.00 24.70 ? 75  LYS B CB  1 
ATOM   1660 C CG  . LYS B 1 75  ? 7.220   4.606   54.165  1.00 28.71 ? 75  LYS B CG  1 
ATOM   1661 C CD  . LYS B 1 75  ? 8.197   5.830   54.333  1.00 31.72 ? 75  LYS B CD  1 
ATOM   1662 C CE  . LYS B 1 75  ? 8.222   6.361   55.810  1.00 33.17 ? 75  LYS B CE  1 
ATOM   1663 N NZ  . LYS B 1 75  ? 6.890   6.595   56.478  1.00 28.56 ? 75  LYS B NZ  1 
ATOM   1664 N N   . ASP B 1 76  ? 8.723   0.083   54.016  1.00 24.66 ? 76  ASP B N   1 
ATOM   1665 C CA  . ASP B 1 76  ? 9.687   -0.977  54.299  1.00 24.48 ? 76  ASP B CA  1 
ATOM   1666 C C   . ASP B 1 76  ? 10.478  -1.395  53.079  1.00 24.69 ? 76  ASP B C   1 
ATOM   1667 O O   . ASP B 1 76  ? 9.993   -1.287  51.947  1.00 24.70 ? 76  ASP B O   1 
ATOM   1668 C CB  . ASP B 1 76  ? 8.999   -2.219  54.890  1.00 25.10 ? 76  ASP B CB  1 
ATOM   1669 C CG  . ASP B 1 76  ? 8.267   -1.915  56.182  1.00 26.36 ? 76  ASP B CG  1 
ATOM   1670 O OD1 . ASP B 1 76  ? 8.432   -0.789  56.719  1.00 30.53 ? 76  ASP B OD1 1 
ATOM   1671 O OD2 . ASP B 1 76  ? 7.492   -2.762  56.645  1.00 25.14 ? 76  ASP B OD2 1 
ATOM   1672 N N   . GLU B 1 77  ? 11.694  -1.888  53.321  1.00 24.93 ? 77  GLU B N   1 
ATOM   1673 C CA  . GLU B 1 77  ? 12.507  -2.482  52.287  1.00 25.01 ? 77  GLU B CA  1 
ATOM   1674 C C   . GLU B 1 77  ? 12.063  -3.873  52.011  1.00 24.35 ? 77  GLU B C   1 
ATOM   1675 O O   . GLU B 1 77  ? 12.125  -4.316  50.881  1.00 25.83 ? 77  GLU B O   1 
ATOM   1676 C CB  . GLU B 1 77  ? 13.988  -2.484  52.664  1.00 26.45 ? 77  GLU B CB  1 
ATOM   1677 C CG  . GLU B 1 77  ? 14.959  -2.938  51.542  1.00 30.48 ? 77  GLU B CG  1 
ATOM   1678 C CD  . GLU B 1 77  ? 14.572  -2.469  50.100  1.00 37.25 ? 77  GLU B CD  1 
ATOM   1679 O OE1 . GLU B 1 77  ? 14.392  -1.231  49.860  1.00 36.91 ? 77  GLU B OE1 1 
ATOM   1680 O OE2 . GLU B 1 77  ? 14.474  -3.362  49.204  1.00 38.34 ? 77  GLU B OE2 1 
ATOM   1681 N N   . GLU B 1 78  ? 11.618  -4.579  53.036  1.00 23.46 ? 78  GLU B N   1 
ATOM   1682 C CA  . GLU B 1 78  ? 11.056  -5.899  52.835  1.00 22.17 ? 78  GLU B CA  1 
ATOM   1683 C C   . GLU B 1 78  ? 9.518   -5.771  52.708  1.00 21.25 ? 78  GLU B C   1 
ATOM   1684 O O   . GLU B 1 78  ? 8.814   -5.433  53.679  1.00 21.39 ? 78  GLU B O   1 
ATOM   1685 C CB  . GLU B 1 78  ? 11.513  -6.872  53.936  1.00 23.75 ? 78  GLU B CB  1 
ATOM   1686 C CG  . GLU B 1 78  ? 11.011  -8.327  53.789  1.00 23.76 ? 78  GLU B CG  1 
ATOM   1687 C CD  . GLU B 1 78  ? 11.769  -9.185  52.789  1.00 28.22 ? 78  GLU B CD  1 
ATOM   1688 O OE1 . GLU B 1 78  ? 12.777  -8.711  52.210  1.00 31.72 ? 78  GLU B OE1 1 
ATOM   1689 O OE2 . GLU B 1 78  ? 11.333  -10.361 52.578  1.00 29.74 ? 78  GLU B OE2 1 
ATOM   1690 N N   . ARG B 1 79  ? 9.023   -6.000  51.479  1.00 19.02 ? 79  ARG B N   1 
ATOM   1691 C CA  . ARG B 1 79  ? 7.604   -5.799  51.090  1.00 17.08 ? 79  ARG B CA  1 
ATOM   1692 C C   . ARG B 1 79  ? 7.354   -6.419  49.727  1.00 16.21 ? 79  ARG B C   1 
ATOM   1693 O O   . ARG B 1 79  ? 8.325   -6.727  48.996  1.00 16.03 ? 79  ARG B O   1 
ATOM   1694 C CB  . ARG B 1 79  ? 7.131   -4.293  51.126  1.00 15.94 ? 79  ARG B CB  1 
ATOM   1695 C CG  . ARG B 1 79  ? 7.873   -3.222  50.303  1.00 14.93 ? 79  ARG B CG  1 
ATOM   1696 C CD  . ARG B 1 79  ? 6.917   -2.695  49.198  1.00 17.73 ? 79  ARG B CD  1 
ATOM   1697 N NE  . ARG B 1 79  ? 6.904   -1.246  49.221  1.00 21.45 ? 79  ARG B NE  1 
ATOM   1698 C CZ  . ARG B 1 79  ? 6.229   -0.505  48.387  1.00 16.47 ? 79  ARG B CZ  1 
ATOM   1699 N NH1 . ARG B 1 79  ? 5.446   -1.052  47.428  1.00 19.71 ? 79  ARG B NH1 1 
ATOM   1700 N NH2 . ARG B 1 79  ? 6.342   0.805   48.519  1.00 21.67 ? 79  ARG B NH2 1 
ATOM   1701 N N   . HIS B 1 80  ? 6.062   -6.661  49.394  1.00 13.57 ? 80  HIS B N   1 
ATOM   1702 C CA  . HIS B 1 80  ? 5.630   -6.970  48.000  1.00 11.05 ? 80  HIS B CA  1 
ATOM   1703 C C   . HIS B 1 80  ? 5.674   -5.733  47.141  1.00 10.87 ? 80  HIS B C   1 
ATOM   1704 O O   . HIS B 1 80  ? 5.535   -4.652  47.676  1.00 10.69 ? 80  HIS B O   1 
ATOM   1705 C CB  . HIS B 1 80  ? 4.180   -7.481  48.007  1.00 10.22 ? 80  HIS B CB  1 
ATOM   1706 C CG  . HIS B 1 80  ? 3.976   -8.618  48.931  1.00 9.02  ? 80  HIS B CG  1 
ATOM   1707 N ND1 . HIS B 1 80  ? 2.807   -8.820  49.628  1.00 13.17 ? 80  HIS B ND1 1 
ATOM   1708 C CD2 . HIS B 1 80  ? 4.831   -9.582  49.338  1.00 13.00 ? 80  HIS B CD2 1 
ATOM   1709 C CE1 . HIS B 1 80  ? 2.918   -9.928  50.356  1.00 10.01 ? 80  HIS B CE1 1 
ATOM   1710 N NE2 . HIS B 1 80  ? 4.139   -10.403 50.199  1.00 13.48 ? 80  HIS B NE2 1 
ATOM   1711 N N   . VAL B 1 81  ? 5.826   -5.853  45.811  1.00 10.32 ? 81  VAL B N   1 
ATOM   1712 C CA  . VAL B 1 81  ? 5.538   -4.674  44.921  1.00 9.77  ? 81  VAL B CA  1 
ATOM   1713 C C   . VAL B 1 81  ? 4.177   -4.030  45.223  1.00 10.69 ? 81  VAL B C   1 
ATOM   1714 O O   . VAL B 1 81  ? 4.074   -2.771  45.307  1.00 12.73 ? 81  VAL B O   1 
ATOM   1715 C CB  . VAL B 1 81  ? 5.526   -5.060  43.432  1.00 9.38  ? 81  VAL B CB  1 
ATOM   1716 C CG1 . VAL B 1 81  ? 5.614   -3.800  42.563  1.00 5.20  ? 81  VAL B CG1 1 
ATOM   1717 C CG2 . VAL B 1 81  ? 6.680   -5.981  43.108  1.00 8.25  ? 81  VAL B CG2 1 
ATOM   1718 N N   . GLY B 1 82  ? 3.147   -4.883  45.386  1.00 10.02 ? 82  GLY B N   1 
ATOM   1719 C CA  . GLY B 1 82  ? 1.723   -4.461  45.665  1.00 10.28 ? 82  GLY B CA  1 
ATOM   1720 C C   . GLY B 1 82  ? 1.326   -3.906  47.054  1.00 9.00  ? 82  GLY B C   1 
ATOM   1721 O O   . GLY B 1 82  ? 0.193   -3.534  47.268  1.00 9.90  ? 82  GLY B O   1 
ATOM   1722 N N   . ASP B 1 83  ? 2.229   -3.958  48.033  1.00 7.65  ? 83  ASP B N   1 
ATOM   1723 C CA  . ASP B 1 83  ? 1.968   -3.529  49.357  1.00 6.05  ? 83  ASP B CA  1 
ATOM   1724 C C   . ASP B 1 83  ? 1.947   -1.980  49.415  1.00 6.04  ? 83  ASP B C   1 
ATOM   1725 O O   . ASP B 1 83  ? 2.931   -1.413  49.802  1.00 5.36  ? 83  ASP B O   1 
ATOM   1726 C CB  . ASP B 1 83  ? 3.154   -3.900  50.182  1.00 5.94  ? 83  ASP B CB  1 
ATOM   1727 C CG  . ASP B 1 83  ? 3.092   -5.336  50.631  1.00 12.10 ? 83  ASP B CG  1 
ATOM   1728 O OD1 . ASP B 1 83  ? 2.051   -5.942  50.317  1.00 4.13  ? 83  ASP B OD1 1 
ATOM   1729 O OD2 . ASP B 1 83  ? 4.027   -5.793  51.299  1.00 14.55 ? 83  ASP B OD2 1 
ATOM   1730 N N   . LEU B 1 84  ? 0.800   -1.369  49.210  1.00 6.59  ? 84  LEU B N   1 
ATOM   1731 C CA  . LEU B 1 84  ? 0.657   0.142   49.295  1.00 6.61  ? 84  LEU B CA  1 
ATOM   1732 C C   . LEU B 1 84  ? 0.034   0.685   50.554  1.00 8.50  ? 84  LEU B C   1 
ATOM   1733 O O   . LEU B 1 84  ? -0.381  1.872   50.606  1.00 6.56  ? 84  LEU B O   1 
ATOM   1734 C CB  . LEU B 1 84  ? -0.175  0.693   48.117  1.00 6.83  ? 84  LEU B CB  1 
ATOM   1735 C CG  . LEU B 1 84  ? 0.400   0.280   46.786  1.00 8.63  ? 84  LEU B CG  1 
ATOM   1736 C CD1 . LEU B 1 84  ? -0.495  0.703   45.671  1.00 5.94  ? 84  LEU B CD1 1 
ATOM   1737 C CD2 . LEU B 1 84  ? 1.787   0.806   46.684  1.00 6.20  ? 84  LEU B CD2 1 
ATOM   1738 N N   . GLY B 1 85  ? -0.080  -0.166  51.553  1.00 8.24  ? 85  GLY B N   1 
ATOM   1739 C CA  . GLY B 1 85  ? -0.286  0.349   52.909  1.00 10.52 ? 85  GLY B CA  1 
ATOM   1740 C C   . GLY B 1 85  ? -1.768  0.320   53.229  1.00 10.93 ? 85  GLY B C   1 
ATOM   1741 O O   . GLY B 1 85  ? -2.445  -0.629  52.880  1.00 10.84 ? 85  GLY B O   1 
ATOM   1742 N N   . ASN B 1 86  ? -2.276  1.376   53.877  1.00 9.78  ? 86  ASN B N   1 
ATOM   1743 C CA  . ASN B 1 86  ? -3.630  1.374   54.319  1.00 10.74 ? 86  ASN B CA  1 
ATOM   1744 C C   . ASN B 1 86  ? -4.169  2.645   53.750  1.00 12.59 ? 86  ASN B C   1 
ATOM   1745 O O   . ASN B 1 86  ? -3.387  3.554   53.566  1.00 13.62 ? 86  ASN B O   1 
ATOM   1746 C CB  . ASN B 1 86  ? -3.666  1.388   55.878  1.00 8.93  ? 86  ASN B CB  1 
ATOM   1747 C CG  . ASN B 1 86  ? -3.509  -0.009  56.474  1.00 9.96  ? 86  ASN B CG  1 
ATOM   1748 O OD1 . ASN B 1 86  ? -4.337  -0.840  56.249  1.00 4.95  ? 86  ASN B OD1 1 
ATOM   1749 N ND2 . ASN B 1 86  ? -2.464  -0.250  57.233  1.00 8.07  ? 86  ASN B ND2 1 
ATOM   1750 N N   . VAL B 1 87  ? -5.435  2.699   53.365  1.00 12.83 ? 87  VAL B N   1 
ATOM   1751 C CA  . VAL B 1 87  ? -6.039  4.051   53.201  1.00 14.42 ? 87  VAL B CA  1 
ATOM   1752 C C   . VAL B 1 87  ? -6.885  4.270   54.452  1.00 14.55 ? 87  VAL B C   1 
ATOM   1753 O O   . VAL B 1 87  ? -7.315  3.296   55.094  1.00 13.65 ? 87  VAL B O   1 
ATOM   1754 C CB  . VAL B 1 87  ? -6.869  4.243   51.835  1.00 14.59 ? 87  VAL B CB  1 
ATOM   1755 C CG1 . VAL B 1 87  ? -5.918  4.259   50.636  1.00 16.65 ? 87  VAL B CG1 1 
ATOM   1756 C CG2 . VAL B 1 87  ? -7.887  3.130   51.629  1.00 14.49 ? 87  VAL B CG2 1 
ATOM   1757 N N   . THR B 1 88  ? -7.126  5.540   54.799  1.00 16.21 ? 88  THR B N   1 
ATOM   1758 C CA  . THR B 1 88  ? -7.964  5.861   55.956  1.00 18.10 ? 88  THR B CA  1 
ATOM   1759 C C   . THR B 1 88  ? -9.283  6.543   55.582  1.00 17.94 ? 88  THR B C   1 
ATOM   1760 O O   . THR B 1 88  ? -9.298  7.613   54.988  1.00 16.12 ? 88  THR B O   1 
ATOM   1761 C CB  . THR B 1 88  ? -7.215  6.788   56.919  1.00 19.60 ? 88  THR B CB  1 
ATOM   1762 O OG1 . THR B 1 88  ? -5.895  6.240   57.204  1.00 21.42 ? 88  THR B OG1 1 
ATOM   1763 C CG2 . THR B 1 88  ? -8.040  6.958   58.245  1.00 21.93 ? 88  THR B CG2 1 
ATOM   1764 N N   . ALA B 1 89  ? -10.386 5.899   55.950  1.00 18.22 ? 89  ALA B N   1 
ATOM   1765 C CA  . ALA B 1 89  ? -11.721 6.462   55.741  1.00 17.64 ? 89  ALA B CA  1 
ATOM   1766 C C   . ALA B 1 89  ? -12.120 7.335   56.942  1.00 18.15 ? 89  ALA B C   1 
ATOM   1767 O O   . ALA B 1 89  ? -11.875 6.980   58.067  1.00 19.22 ? 89  ALA B O   1 
ATOM   1768 C CB  . ALA B 1 89  ? -12.686 5.376   55.511  1.00 17.11 ? 89  ALA B CB  1 
ATOM   1769 N N   . ASP B 1 90  ? -12.615 8.536   56.676  1.00 18.65 ? 90  ASP B N   1 
ATOM   1770 C CA  . ASP B 1 90  ? -13.110 9.391   57.718  1.00 19.57 ? 90  ASP B CA  1 
ATOM   1771 C C   . ASP B 1 90  ? -14.424 8.873   58.341  1.00 20.58 ? 90  ASP B C   1 
ATOM   1772 O O   . ASP B 1 90  ? -14.857 7.705   58.085  1.00 19.91 ? 90  ASP B O   1 
ATOM   1773 C CB  . ASP B 1 90  ? -13.144 10.892  57.240  1.00 18.91 ? 90  ASP B CB  1 
ATOM   1774 C CG  . ASP B 1 90  ? -14.242 11.238  56.160  1.00 20.82 ? 90  ASP B CG  1 
ATOM   1775 O OD1 . ASP B 1 90  ? -15.184 10.486  55.843  1.00 20.64 ? 90  ASP B OD1 1 
ATOM   1776 O OD2 . ASP B 1 90  ? -14.183 12.363  55.625  1.00 21.52 ? 90  ASP B OD2 1 
ATOM   1777 N N   . LYS B 1 91  ? -15.034 9.708   59.194  1.00 21.61 ? 91  LYS B N   1 
ATOM   1778 C CA  . LYS B 1 91  ? -16.291 9.359   59.882  1.00 22.58 ? 91  LYS B CA  1 
ATOM   1779 C C   . LYS B 1 91  ? -17.439 9.143   58.908  1.00 23.57 ? 91  LYS B C   1 
ATOM   1780 O O   . LYS B 1 91  ? -18.469 8.493   59.266  1.00 23.48 ? 91  LYS B O   1 
ATOM   1781 C CB  . LYS B 1 91  ? -16.728 10.498  60.829  1.00 23.29 ? 91  LYS B CB  1 
ATOM   1782 C CG  . LYS B 1 91  ? -16.864 11.830  60.131  1.00 22.48 ? 91  LYS B CG  1 
ATOM   1783 C CD  . LYS B 1 91  ? -17.460 12.926  61.018  1.00 23.07 ? 91  LYS B CD  1 
ATOM   1784 C CE  . LYS B 1 91  ? -17.514 14.187  60.241  1.00 26.81 ? 91  LYS B CE  1 
ATOM   1785 N NZ  . LYS B 1 91  ? -17.536 15.373  61.152  1.00 31.01 ? 91  LYS B NZ  1 
ATOM   1786 N N   . ASP B 1 92  ? -17.278 9.733   57.710  1.00 24.24 ? 92  ASP B N   1 
ATOM   1787 C CA  . ASP B 1 92  ? -18.281 9.725   56.632  1.00 24.10 ? 92  ASP B CA  1 
ATOM   1788 C C   . ASP B 1 92  ? -18.088 8.569   55.632  1.00 23.79 ? 92  ASP B C   1 
ATOM   1789 O O   . ASP B 1 92  ? -18.787 8.482   54.624  1.00 25.13 ? 92  ASP B O   1 
ATOM   1790 C CB  . ASP B 1 92  ? -18.360 11.092  55.938  1.00 24.31 ? 92  ASP B CB  1 
ATOM   1791 C CG  . ASP B 1 92  ? -19.128 12.183  56.815  1.00 24.66 ? 92  ASP B CG  1 
ATOM   1792 O OD1 . ASP B 1 92  ? -20.049 11.791  57.600  1.00 23.33 ? 92  ASP B OD1 1 
ATOM   1793 O OD2 . ASP B 1 92  ? -18.813 13.410  56.703  1.00 24.02 ? 92  ASP B OD2 1 
ATOM   1794 N N   . GLY B 1 93  ? -17.168 7.669   55.939  1.00 22.94 ? 93  GLY B N   1 
ATOM   1795 C CA  . GLY B 1 93  ? -16.825 6.557   55.041  1.00 21.48 ? 93  GLY B CA  1 
ATOM   1796 C C   . GLY B 1 93  ? -16.046 6.934   53.759  1.00 19.71 ? 93  GLY B C   1 
ATOM   1797 O O   . GLY B 1 93  ? -15.868 6.081   52.911  1.00 19.19 ? 93  GLY B O   1 
ATOM   1798 N N   . VAL B 1 94  ? -15.583 8.192   53.644  1.00 18.74 ? 94  VAL B N   1 
ATOM   1799 C CA  . VAL B 1 94  ? -14.801 8.691   52.518  1.00 17.68 ? 94  VAL B CA  1 
ATOM   1800 C C   . VAL B 1 94  ? -13.277 8.682   52.816  1.00 18.52 ? 94  VAL B C   1 
ATOM   1801 O O   . VAL B 1 94  ? -12.790 9.385   53.715  1.00 18.38 ? 94  VAL B O   1 
ATOM   1802 C CB  . VAL B 1 94  ? -15.200 10.131  52.070  1.00 16.39 ? 94  VAL B CB  1 
ATOM   1803 C CG1 . VAL B 1 94  ? -14.403 10.555  50.879  1.00 16.38 ? 94  VAL B CG1 1 
ATOM   1804 C CG2 . VAL B 1 94  ? -16.622 10.183  51.653  1.00 15.73 ? 94  VAL B CG2 1 
ATOM   1805 N N   . ALA B 1 95  ? -12.553 7.897   52.007  1.00 18.34 ? 95  ALA B N   1 
ATOM   1806 C CA  . ALA B 1 95  ? -11.121 7.865   52.031  1.00 18.78 ? 95  ALA B CA  1 
ATOM   1807 C C   . ALA B 1 95  ? -10.581 8.609   50.856  1.00 18.54 ? 95  ALA B C   1 
ATOM   1808 O O   . ALA B 1 95  ? -10.741 8.181   49.718  1.00 18.86 ? 95  ALA B O   1 
ATOM   1809 C CB  . ALA B 1 95  ? -10.643 6.466   51.993  1.00 17.03 ? 95  ALA B CB  1 
ATOM   1810 N N   . ASP B 1 96  ? -9.905  9.708   51.140  1.00 19.86 ? 96  ASP B N   1 
ATOM   1811 C CA  . ASP B 1 96  ? -9.163  10.439  50.167  1.00 20.69 ? 96  ASP B CA  1 
ATOM   1812 C C   . ASP B 1 96  ? -7.741  9.830   50.112  1.00 20.88 ? 96  ASP B C   1 
ATOM   1813 O O   . ASP B 1 96  ? -7.116  9.580   51.149  1.00 22.08 ? 96  ASP B O   1 
ATOM   1814 C CB  . ASP B 1 96  ? -9.153  11.880  50.623  1.00 21.97 ? 96  ASP B CB  1 
ATOM   1815 C CG  . ASP B 1 96  ? -8.120  12.738  49.898  1.00 27.03 ? 96  ASP B CG  1 
ATOM   1816 O OD1 . ASP B 1 96  ? -8.170  13.975  49.987  1.00 26.85 ? 96  ASP B OD1 1 
ATOM   1817 O OD2 . ASP B 1 96  ? -7.228  12.175  49.256  1.00 35.43 ? 96  ASP B OD2 1 
ATOM   1818 N N   . VAL B 1 97  ? -7.231  9.569   48.908  1.00 20.65 ? 97  VAL B N   1 
ATOM   1819 C CA  . VAL B 1 97  ? -5.999  8.786   48.727  1.00 18.98 ? 97  VAL B CA  1 
ATOM   1820 C C   . VAL B 1 97  ? -4.953  9.748   48.175  1.00 19.46 ? 97  VAL B C   1 
ATOM   1821 O O   . VAL B 1 97  ? -5.269  10.545  47.312  1.00 18.73 ? 97  VAL B O   1 
ATOM   1822 C CB  . VAL B 1 97  ? -6.222  7.486   47.829  1.00 19.12 ? 97  VAL B CB  1 
ATOM   1823 C CG1 . VAL B 1 97  ? -4.950  6.629   47.695  1.00 16.30 ? 97  VAL B CG1 1 
ATOM   1824 C CG2 . VAL B 1 97  ? -7.333  6.615   48.382  1.00 16.28 ? 97  VAL B CG2 1 
ATOM   1825 N N   . SER B 1 98  ? -3.757  9.743   48.761  1.00 19.91 ? 98  SER B N   1 
ATOM   1826 C CA  . SER B 1 98  ? -2.576  10.440  48.221  1.00 20.91 ? 98  SER B CA  1 
ATOM   1827 C C   . SER B 1 98  ? -1.291  9.697   48.624  1.00 19.52 ? 98  SER B C   1 
ATOM   1828 O O   . SER B 1 98  ? -0.879  9.704   49.765  1.00 21.99 ? 98  SER B O   1 
ATOM   1829 C CB  . SER B 1 98  ? -2.511  11.895  48.669  1.00 21.05 ? 98  SER B CB  1 
ATOM   1830 O OG  . SER B 1 98  ? -2.091  12.748  47.600  1.00 23.39 ? 98  SER B OG  1 
ATOM   1831 N N   . ILE B 1 99  ? -0.658  9.051   47.667  1.00 18.44 ? 99  ILE B N   1 
ATOM   1832 C CA  . ILE B 1 99  ? 0.414   8.135   47.924  1.00 16.82 ? 99  ILE B CA  1 
ATOM   1833 C C   . ILE B 1 99  ? 1.413   8.577   46.876  1.00 16.94 ? 99  ILE B C   1 
ATOM   1834 O O   . ILE B 1 99  ? 1.002   8.992   45.804  1.00 17.51 ? 99  ILE B O   1 
ATOM   1835 C CB  . ILE B 1 99  ? -0.116  6.675   47.671  1.00 16.34 ? 99  ILE B CB  1 
ATOM   1836 C CG1 . ILE B 1 99  ? -1.255  6.352   48.598  1.00 20.02 ? 99  ILE B CG1 1 
ATOM   1837 C CG2 . ILE B 1 99  ? 0.889   5.487   47.939  1.00 16.80 ? 99  ILE B CG2 1 
ATOM   1838 C CD1 . ILE B 1 99  ? -1.665  4.896   48.553  1.00 16.89 ? 99  ILE B CD1 1 
ATOM   1839 N N   . GLU B 1 100 ? 2.711   8.599   47.191  1.00 15.74 ? 100 GLU B N   1 
ATOM   1840 C CA  . GLU B 1 100 ? 3.711   8.190   46.180  1.00 16.19 ? 100 GLU B CA  1 
ATOM   1841 C C   . GLU B 1 100 ? 4.392   6.883   46.516  1.00 14.05 ? 100 GLU B C   1 
ATOM   1842 O O   . GLU B 1 100 ? 4.601   6.563   47.663  1.00 15.04 ? 100 GLU B O   1 
ATOM   1843 C CB  . GLU B 1 100 ? 4.732   9.278   45.912  1.00 16.68 ? 100 GLU B CB  1 
ATOM   1844 C CG  . GLU B 1 100 ? 4.151   10.389  45.187  1.00 20.04 ? 100 GLU B CG  1 
ATOM   1845 C CD  . GLU B 1 100 ? 5.042   11.567  45.262  1.00 29.90 ? 100 GLU B CD  1 
ATOM   1846 O OE1 . GLU B 1 100 ? 6.282   11.348  45.367  1.00 33.28 ? 100 GLU B OE1 1 
ATOM   1847 O OE2 . GLU B 1 100 ? 4.502   12.704  45.243  1.00 33.12 ? 100 GLU B OE2 1 
ATOM   1848 N N   . ASP B 1 101 ? 4.727   6.114   45.498  1.00 13.25 ? 101 ASP B N   1 
ATOM   1849 C CA  . ASP B 1 101 ? 5.461   4.875   45.660  1.00 12.85 ? 101 ASP B CA  1 
ATOM   1850 C C   . ASP B 1 101 ? 6.507   4.730   44.541  1.00 12.13 ? 101 ASP B C   1 
ATOM   1851 O O   . ASP B 1 101 ? 6.231   5.034   43.346  1.00 12.19 ? 101 ASP B O   1 
ATOM   1852 C CB  . ASP B 1 101 ? 4.508   3.708   45.573  1.00 12.57 ? 101 ASP B CB  1 
ATOM   1853 C CG  . ASP B 1 101 ? 5.076   2.463   46.123  1.00 11.97 ? 101 ASP B CG  1 
ATOM   1854 O OD1 . ASP B 1 101 ? 5.176   2.348   47.333  1.00 14.14 ? 101 ASP B OD1 1 
ATOM   1855 O OD2 . ASP B 1 101 ? 5.380   1.543   45.353  1.00 15.87 ? 101 ASP B OD2 1 
ATOM   1856 N N   . SER B 1 102 ? 7.681   4.198   44.928  1.00 10.89 ? 102 SER B N   1 
ATOM   1857 C CA  . SER B 1 102 ? 8.810   3.999   44.064  1.00 9.41  ? 102 SER B CA  1 
ATOM   1858 C C   . SER B 1 102 ? 9.015   2.529   43.880  1.00 10.61 ? 102 SER B C   1 
ATOM   1859 O O   . SER B 1 102 ? 9.974   2.131   43.253  1.00 10.73 ? 102 SER B O   1 
ATOM   1860 C CB  . SER B 1 102 ? 10.058  4.513   44.763  1.00 12.12 ? 102 SER B CB  1 
ATOM   1861 O OG  . SER B 1 102 ? 10.056  5.941   44.777  1.00 13.18 ? 102 SER B OG  1 
ATOM   1862 N N   . VAL B 1 103 ? 8.153   1.691   44.445  1.00 8.55  ? 103 VAL B N   1 
ATOM   1863 C CA  . VAL B 1 103 ? 8.319   0.285   44.114  1.00 8.07  ? 103 VAL B CA  1 
ATOM   1864 C C   . VAL B 1 103 ? 7.406   -0.042  42.913  1.00 9.40  ? 103 VAL B C   1 
ATOM   1865 O O   . VAL B 1 103 ? 7.885   -0.496  41.892  1.00 12.26 ? 103 VAL B O   1 
ATOM   1866 C CB  . VAL B 1 103 ? 8.137   -0.590  45.281  1.00 5.69  ? 103 VAL B CB  1 
ATOM   1867 C CG1 . VAL B 1 103 ? 8.378   -2.039  44.863  1.00 5.23  ? 103 VAL B CG1 1 
ATOM   1868 C CG2 . VAL B 1 103 ? 9.127   -0.254  46.314  1.00 6.71  ? 103 VAL B CG2 1 
ATOM   1869 N N   . ILE B 1 104 ? 6.093   0.153   43.018  1.00 8.99  ? 104 ILE B N   1 
ATOM   1870 C CA  . ILE B 1 104 ? 5.231   -0.068  41.849  1.00 9.17  ? 104 ILE B CA  1 
ATOM   1871 C C   . ILE B 1 104 ? 5.673   0.765   40.612  1.00 11.26 ? 104 ILE B C   1 
ATOM   1872 O O   . ILE B 1 104 ? 6.241   1.891   40.774  1.00 14.07 ? 104 ILE B O   1 
ATOM   1873 C CB  . ILE B 1 104 ? 3.729   0.259   42.161  1.00 9.10  ? 104 ILE B CB  1 
ATOM   1874 C CG1 . ILE B 1 104 ? 3.571   1.646   42.807  1.00 5.18  ? 104 ILE B CG1 1 
ATOM   1875 C CG2 . ILE B 1 104 ? 3.155   -0.767  43.002  1.00 3.46  ? 104 ILE B CG2 1 
ATOM   1876 C CD1 . ILE B 1 104 ? 2.327   2.455   42.287  1.00 9.28  ? 104 ILE B CD1 1 
ATOM   1877 N N   . SER B 1 105 ? 5.435   0.236   39.397  1.00 9.93  ? 105 SER B N   1 
ATOM   1878 C CA  . SER B 1 105 ? 5.582   1.000   38.179  1.00 10.80 ? 105 SER B CA  1 
ATOM   1879 C C   . SER B 1 105 ? 4.406   1.044   37.227  1.00 10.86 ? 105 SER B C   1 
ATOM   1880 O O   . SER B 1 105 ? 3.481   0.238   37.328  1.00 12.07 ? 105 SER B O   1 
ATOM   1881 C CB  . SER B 1 105 ? 6.892   0.781   37.411  1.00 8.85  ? 105 SER B CB  1 
ATOM   1882 O OG  . SER B 1 105 ? 7.197   2.042   36.719  1.00 11.22 ? 105 SER B OG  1 
ATOM   1883 N N   . LEU B 1 106 ? 4.397   2.043   36.347  1.00 11.13 ? 106 LEU B N   1 
ATOM   1884 C CA  . LEU B 1 106 ? 3.491   1.998   35.202  1.00 12.36 ? 106 LEU B CA  1 
ATOM   1885 C C   . LEU B 1 106 ? 4.059   1.330   33.942  1.00 11.97 ? 106 LEU B C   1 
ATOM   1886 O O   . LEU B 1 106 ? 3.362   1.239   32.943  1.00 11.73 ? 106 LEU B O   1 
ATOM   1887 C CB  . LEU B 1 106 ? 2.898   3.404   34.930  1.00 11.96 ? 106 LEU B CB  1 
ATOM   1888 C CG  . LEU B 1 106 ? 2.047   3.916   36.085  1.00 13.85 ? 106 LEU B CG  1 
ATOM   1889 C CD1 . LEU B 1 106 ? 1.463   5.069   35.568  1.00 9.44  ? 106 LEU B CD1 1 
ATOM   1890 C CD2 . LEU B 1 106 ? 0.927   2.945   36.639  1.00 10.70 ? 106 LEU B CD2 1 
ATOM   1891 N N   . SER B 1 107 ? 5.328   0.876   34.009  1.00 13.60 ? 107 SER B N   1 
ATOM   1892 C CA  . SER B 1 107 ? 6.101   0.138   32.956  1.00 14.66 ? 107 SER B CA  1 
ATOM   1893 C C   . SER B 1 107 ? 7.072   -0.898  33.568  1.00 15.52 ? 107 SER B C   1 
ATOM   1894 O O   . SER B 1 107 ? 7.340   -0.916  34.762  1.00 14.99 ? 107 SER B O   1 
ATOM   1895 C CB  . SER B 1 107 ? 6.869   1.071   32.016  1.00 15.66 ? 107 SER B CB  1 
ATOM   1896 O OG  . SER B 1 107 ? 7.255   2.330   32.638  1.00 16.26 ? 107 SER B OG  1 
ATOM   1897 N N   . GLY B 1 108 ? 7.550   -1.798  32.725  1.00 16.52 ? 108 GLY B N   1 
ATOM   1898 C CA  . GLY B 1 108 ? 8.687   -2.647  33.053  1.00 16.74 ? 108 GLY B CA  1 
ATOM   1899 C C   . GLY B 1 108 ? 8.184   -3.800  33.837  1.00 17.21 ? 108 GLY B C   1 
ATOM   1900 O O   . GLY B 1 108 ? 7.004   -4.073  33.790  1.00 15.66 ? 108 GLY B O   1 
ATOM   1901 N N   . ASP B 1 109 ? 9.067   -4.434  34.613  1.00 17.62 ? 109 ASP B N   1 
ATOM   1902 C CA  . ASP B 1 109 ? 8.683   -5.610  35.377  1.00 18.46 ? 109 ASP B CA  1 
ATOM   1903 C C   . ASP B 1 109 ? 7.822   -5.324  36.608  1.00 17.38 ? 109 ASP B C   1 
ATOM   1904 O O   . ASP B 1 109 ? 7.131   -6.229  37.087  1.00 15.95 ? 109 ASP B O   1 
ATOM   1905 C CB  . ASP B 1 109 ? 9.922   -6.367  35.844  1.00 20.71 ? 109 ASP B CB  1 
ATOM   1906 C CG  . ASP B 1 109 ? 10.693  -6.990  34.708  1.00 25.76 ? 109 ASP B CG  1 
ATOM   1907 O OD1 . ASP B 1 109 ? 10.096  -7.665  33.835  1.00 32.58 ? 109 ASP B OD1 1 
ATOM   1908 O OD2 . ASP B 1 109 ? 11.929  -6.839  34.733  1.00 33.60 ? 109 ASP B OD2 1 
ATOM   1909 N N   . HIS B 1 110 ? 7.877   -4.095  37.155  1.00 15.09 ? 110 HIS B N   1 
ATOM   1910 C CA  . HIS B 1 110 ? 7.016   -3.793  38.340  1.00 14.04 ? 110 HIS B CA  1 
ATOM   1911 C C   . HIS B 1 110 ? 5.669   -3.149  37.977  1.00 12.57 ? 110 HIS B C   1 
ATOM   1912 O O   . HIS B 1 110 ? 5.029   -2.420  38.774  1.00 12.87 ? 110 HIS B O   1 
ATOM   1913 C CB  . HIS B 1 110 ? 7.781   -2.969  39.371  1.00 13.42 ? 110 HIS B CB  1 
ATOM   1914 C CG  . HIS B 1 110 ? 8.775   -3.746  40.190  1.00 16.40 ? 110 HIS B CG  1 
ATOM   1915 N ND1 . HIS B 1 110 ? 9.488   -3.167  41.233  1.00 16.04 ? 110 HIS B ND1 1 
ATOM   1916 C CD2 . HIS B 1 110 ? 9.178   -5.049  40.132  1.00 15.97 ? 110 HIS B CD2 1 
ATOM   1917 C CE1 . HIS B 1 110 ? 10.269  -4.080  41.778  1.00 14.58 ? 110 HIS B CE1 1 
ATOM   1918 N NE2 . HIS B 1 110 ? 10.087  -5.231  41.142  1.00 12.95 ? 110 HIS B NE2 1 
ATOM   1919 N N   . CYS B 1 111 ? 5.318   -3.373  36.719  1.00 11.68 ? 111 CYS B N   1 
ATOM   1920 C CA  . CYS B 1 111 ? 4.221   -2.707  36.019  1.00 10.08 ? 111 CYS B CA  1 
ATOM   1921 C C   . CYS B 1 111 ? 2.974   -3.205  36.650  1.00 7.53  ? 111 CYS B C   1 
ATOM   1922 O O   . CYS B 1 111 ? 2.754   -4.346  36.709  1.00 4.56  ? 111 CYS B O   1 
ATOM   1923 C CB  . CYS B 1 111 ? 4.192   -3.057  34.522  1.00 8.96  ? 111 CYS B CB  1 
ATOM   1924 S SG  . CYS B 1 111 ? 2.886   -2.120  33.663  1.00 13.63 ? 111 CYS B SG  1 
ATOM   1925 N N   . ILE B 1 112 ? 2.102   -2.312  37.064  1.00 6.77  ? 112 ILE B N   1 
ATOM   1926 C CA  . ILE B 1 112 ? 0.827   -2.787  37.643  1.00 4.58  ? 112 ILE B CA  1 
ATOM   1927 C C   . ILE B 1 112 ? -0.378  -2.592  36.698  1.00 6.60  ? 112 ILE B C   1 
ATOM   1928 O O   . ILE B 1 112 ? -1.505  -2.944  37.082  1.00 4.98  ? 112 ILE B O   1 
ATOM   1929 C CB  . ILE B 1 112 ? 0.578   -2.214  39.038  1.00 5.65  ? 112 ILE B CB  1 
ATOM   1930 C CG1 . ILE B 1 112 ? 0.440   -0.692  38.926  1.00 2.00  ? 112 ILE B CG1 1 
ATOM   1931 C CG2 . ILE B 1 112 ? 1.748   -2.545  40.009  1.00 6.32  ? 112 ILE B CG2 1 
ATOM   1932 C CD1 . ILE B 1 112 ? 0.089   0.062   40.142  1.00 4.55  ? 112 ILE B CD1 1 
ATOM   1933 N N   . ILE B 1 113 ? -0.170  -2.030  35.495  1.00 9.52  ? 113 ILE B N   1 
ATOM   1934 C CA  . ILE B 1 113 ? -1.261  -1.873  34.528  1.00 10.36 ? 113 ILE B CA  1 
ATOM   1935 C C   . ILE B 1 113 ? -1.741  -3.262  34.187  1.00 10.54 ? 113 ILE B C   1 
ATOM   1936 O O   . ILE B 1 113 ? -0.925  -4.084  33.886  1.00 7.81  ? 113 ILE B O   1 
ATOM   1937 C CB  . ILE B 1 113 ? -0.818  -1.077  33.326  1.00 11.49 ? 113 ILE B CB  1 
ATOM   1938 C CG1 . ILE B 1 113 ? -0.725  0.400   33.800  1.00 8.28  ? 113 ILE B CG1 1 
ATOM   1939 C CG2 . ILE B 1 113 ? -1.821  -1.252  32.169  1.00 11.79 ? 113 ILE B CG2 1 
ATOM   1940 C CD1 . ILE B 1 113 ? -0.208  1.442   32.824  1.00 15.21 ? 113 ILE B CD1 1 
ATOM   1941 N N   . GLY B 1 114 ? -3.043  -3.526  34.254  1.00 10.19 ? 114 GLY B N   1 
ATOM   1942 C CA  . GLY B 1 114 ? -3.509  -4.861  33.832  1.00 5.64  ? 114 GLY B CA  1 
ATOM   1943 C C   . GLY B 1 114 ? -3.613  -5.722  35.034  1.00 5.88  ? 114 GLY B C   1 
ATOM   1944 O O   . GLY B 1 114 ? -3.873  -6.975  34.958  1.00 2.00  ? 114 GLY B O   1 
ATOM   1945 N N   . ARG B 1 115 ? -3.263  -5.132  36.176  1.00 5.45  ? 115 ARG B N   1 
ATOM   1946 C CA  . ARG B 1 115 ? -3.469  -5.884  37.429  1.00 5.37  ? 115 ARG B CA  1 
ATOM   1947 C C   . ARG B 1 115 ? -4.664  -5.293  38.188  1.00 6.11  ? 115 ARG B C   1 
ATOM   1948 O O   . ARG B 1 115 ? -5.458  -4.542  37.600  1.00 6.53  ? 115 ARG B O   1 
ATOM   1949 C CB  . ARG B 1 115 ? -2.189  -6.071  38.286  1.00 6.80  ? 115 ARG B CB  1 
ATOM   1950 C CG  . ARG B 1 115 ? -0.998  -6.830  37.486  1.00 2.01  ? 115 ARG B CG  1 
ATOM   1951 C CD  . ARG B 1 115 ? 0.289   -6.741  38.228  1.00 2.00  ? 115 ARG B CD  1 
ATOM   1952 N NE  . ARG B 1 115 ? 1.375   -7.123  37.314  1.00 2.00  ? 115 ARG B NE  1 
ATOM   1953 C CZ  . ARG B 1 115 ? 1.638   -8.408  36.959  1.00 2.00  ? 115 ARG B CZ  1 
ATOM   1954 N NH1 . ARG B 1 115 ? 0.919   -9.451  37.366  1.00 2.98  ? 115 ARG B NH1 1 
ATOM   1955 N NH2 . ARG B 1 115 ? 2.612   -8.641  36.157  1.00 2.24  ? 115 ARG B NH2 1 
ATOM   1956 N N   . THR B 1 116 ? -4.778  -5.605  39.476  1.00 6.39  ? 116 THR B N   1 
ATOM   1957 C CA  . THR B 1 116 ? -5.969  -5.250  40.293  1.00 6.02  ? 116 THR B CA  1 
ATOM   1958 C C   . THR B 1 116 ? -5.613  -4.423  41.517  1.00 8.06  ? 116 THR B C   1 
ATOM   1959 O O   . THR B 1 116 ? -4.706  -4.732  42.292  1.00 9.78  ? 116 THR B O   1 
ATOM   1960 C CB  . THR B 1 116 ? -6.672  -6.601  40.701  1.00 4.79  ? 116 THR B CB  1 
ATOM   1961 O OG1 . THR B 1 116 ? -7.173  -7.191  39.502  1.00 3.70  ? 116 THR B OG1 1 
ATOM   1962 C CG2 . THR B 1 116 ? -7.825  -6.348  41.533  1.00 4.29  ? 116 THR B CG2 1 
ATOM   1963 N N   . LEU B 1 117 ? -6.274  -3.291  41.697  1.00 8.40  ? 117 LEU B N   1 
ATOM   1964 C CA  . LEU B 1 117 ? -6.190  -2.603  42.948  1.00 6.51  ? 117 LEU B CA  1 
ATOM   1965 C C   . LEU B 1 117 ? -7.389  -3.100  43.757  1.00 7.38  ? 117 LEU B C   1 
ATOM   1966 O O   . LEU B 1 117 ? -8.494  -3.140  43.238  1.00 5.08  ? 117 LEU B O   1 
ATOM   1967 C CB  . LEU B 1 117 ? -6.355  -1.097  42.678  1.00 7.67  ? 117 LEU B CB  1 
ATOM   1968 C CG  . LEU B 1 117 ? -6.113  -0.136  43.780  1.00 7.54  ? 117 LEU B CG  1 
ATOM   1969 C CD1 . LEU B 1 117 ? -4.757  -0.444  44.404  1.00 13.16 ? 117 LEU B CD1 1 
ATOM   1970 C CD2 . LEU B 1 117 ? -6.235  1.359   43.247  1.00 9.41  ? 117 LEU B CD2 1 
ATOM   1971 N N   . VAL B 1 118 ? -7.188  -3.404  45.047  1.00 8.06  ? 118 VAL B N   1 
ATOM   1972 C CA  . VAL B 1 118 ? -8.208  -4.018  45.954  1.00 8.98  ? 118 VAL B CA  1 
ATOM   1973 C C   . VAL B 1 118 ? -8.139  -3.183  47.192  1.00 9.09  ? 118 VAL B C   1 
ATOM   1974 O O   . VAL B 1 118 ? -7.035  -2.936  47.641  1.00 10.90 ? 118 VAL B O   1 
ATOM   1975 C CB  . VAL B 1 118 ? -7.919  -5.538  46.307  1.00 6.60  ? 118 VAL B CB  1 
ATOM   1976 C CG1 . VAL B 1 118 ? -8.891  -6.062  47.328  1.00 4.31  ? 118 VAL B CG1 1 
ATOM   1977 C CG2 . VAL B 1 118 ? -8.002  -6.513  45.103  1.00 9.11  ? 118 VAL B CG2 1 
ATOM   1978 N N   . VAL B 1 119 ? -9.278  -2.631  47.654  1.00 7.79  ? 119 VAL B N   1 
ATOM   1979 C CA  . VAL B 1 119 ? -9.440  -2.066  49.010  1.00 7.22  ? 119 VAL B CA  1 
ATOM   1980 C C   . VAL B 1 119 ? -9.990  -3.214  49.936  1.00 8.00  ? 119 VAL B C   1 
ATOM   1981 O O   . VAL B 1 119 ? -10.821 -4.013  49.507  1.00 7.31  ? 119 VAL B O   1 
ATOM   1982 C CB  . VAL B 1 119 ? -10.152 -0.569  49.035  1.00 8.08  ? 119 VAL B CB  1 
ATOM   1983 C CG1 . VAL B 1 119 ? -11.604 -0.492  48.414  1.00 7.27  ? 119 VAL B CG1 1 
ATOM   1984 C CG2 . VAL B 1 119 ? -10.084 0.082   50.384  1.00 6.66  ? 119 VAL B CG2 1 
ATOM   1985 N N   . HIS B 1 120 ? -9.421  -3.369  51.135  1.00 8.91  ? 120 HIS B N   1 
ATOM   1986 C CA  . HIS B 1 120 ? -9.751  -4.472  52.000  1.00 10.51 ? 120 HIS B CA  1 
ATOM   1987 C C   . HIS B 1 120 ? -10.608 -4.025  53.161  1.00 11.59 ? 120 HIS B C   1 
ATOM   1988 O O   . HIS B 1 120 ? -10.676 -2.820  53.530  1.00 9.64  ? 120 HIS B O   1 
ATOM   1989 C CB  . HIS B 1 120 ? -8.454  -5.177  52.478  1.00 10.43 ? 120 HIS B CB  1 
ATOM   1990 C CG  . HIS B 1 120 ? -7.836  -6.101  51.459  1.00 6.00  ? 120 HIS B CG  1 
ATOM   1991 N ND1 . HIS B 1 120 ? -8.021  -7.476  51.494  1.00 8.21  ? 120 HIS B ND1 1 
ATOM   1992 C CD2 . HIS B 1 120 ? -7.022  -5.865  50.401  1.00 4.86  ? 120 HIS B CD2 1 
ATOM   1993 C CE1 . HIS B 1 120 ? -7.371  -8.028  50.493  1.00 5.23  ? 120 HIS B CE1 1 
ATOM   1994 N NE2 . HIS B 1 120 ? -6.711  -7.084  49.853  1.00 7.78  ? 120 HIS B NE2 1 
ATOM   1995 N N   . GLU B 1 121 ? -11.272 -5.023  53.734  1.00 11.47 ? 121 GLU B N   1 
ATOM   1996 C CA  . GLU B 1 121 ? -12.114 -4.916  54.933  1.00 13.70 ? 121 GLU B CA  1 
ATOM   1997 C C   . GLU B 1 121 ? -11.531 -4.195  56.176  1.00 15.54 ? 121 GLU B C   1 
ATOM   1998 O O   . GLU B 1 121 ? -12.174 -3.275  56.735  1.00 17.59 ? 121 GLU B O   1 
ATOM   1999 C CB  . GLU B 1 121 ? -12.489 -6.343  55.306  1.00 11.86 ? 121 GLU B CB  1 
ATOM   2000 C CG  . GLU B 1 121 ? -13.219 -6.438  56.560  1.00 15.30 ? 121 GLU B CG  1 
ATOM   2001 C CD  . GLU B 1 121 ? -13.448 -7.874  56.921  1.00 16.37 ? 121 GLU B CD  1 
ATOM   2002 O OE1 . GLU B 1 121 ? -14.228 -8.062  57.861  1.00 18.33 ? 121 GLU B OE1 1 
ATOM   2003 O OE2 . GLU B 1 121 ? -12.868 -8.783  56.262  1.00 14.44 ? 121 GLU B OE2 1 
ATOM   2004 N N   . LYS B 1 122 ? -10.316 -4.581  56.601  1.00 15.76 ? 122 LYS B N   1 
ATOM   2005 C CA  . LYS B 1 122 ? -9.682  -4.044  57.816  1.00 17.43 ? 122 LYS B CA  1 
ATOM   2006 C C   . LYS B 1 122 ? -8.282  -3.539  57.469  1.00 17.12 ? 122 LYS B C   1 
ATOM   2007 O O   . LYS B 1 122 ? -7.757  -3.847  56.410  1.00 15.90 ? 122 LYS B O   1 
ATOM   2008 C CB  . LYS B 1 122 ? -9.484  -5.145  58.920  1.00 17.55 ? 122 LYS B CB  1 
ATOM   2009 C CG  . LYS B 1 122 ? -10.437 -6.341  59.005  1.00 16.87 ? 122 LYS B CG  1 
ATOM   2010 C CD  . LYS B 1 122 ? -9.715  -7.576  59.635  1.00 19.14 ? 122 LYS B CD  1 
ATOM   2011 C CE  . LYS B 1 122 ? -10.608 -8.841  59.712  1.00 20.73 ? 122 LYS B CE  1 
ATOM   2012 N NZ  . LYS B 1 122 ? -9.838  -10.212 59.753  1.00 23.56 ? 122 LYS B NZ  1 
ATOM   2013 N N   . ALA B 1 123 ? -7.655  -2.826  58.409  1.00 16.81 ? 123 ALA B N   1 
ATOM   2014 C CA  . ALA B 1 123 ? -6.199  -2.587  58.406  1.00 15.77 ? 123 ALA B CA  1 
ATOM   2015 C C   . ALA B 1 123 ? -5.283  -3.764  58.058  1.00 16.95 ? 123 ALA B C   1 
ATOM   2016 O O   . ALA B 1 123 ? -5.358  -4.901  58.632  1.00 16.29 ? 123 ALA B O   1 
ATOM   2017 C CB  . ALA B 1 123 ? -5.786  -2.011  59.732  1.00 16.19 ? 123 ALA B CB  1 
ATOM   2018 N N   . ASP B 1 124 ? -4.403  -3.472  57.108  1.00 16.68 ? 124 ASP B N   1 
ATOM   2019 C CA  . ASP B 1 124 ? -3.139  -4.221  56.894  1.00 16.63 ? 124 ASP B CA  1 
ATOM   2020 C C   . ASP B 1 124 ? -2.297  -3.912  58.151  1.00 15.79 ? 124 ASP B C   1 
ATOM   2021 O O   . ASP B 1 124 ? -2.014  -2.720  58.464  1.00 14.00 ? 124 ASP B O   1 
ATOM   2022 C CB  . ASP B 1 124 ? -2.473  -3.656  55.610  1.00 16.06 ? 124 ASP B CB  1 
ATOM   2023 C CG  . ASP B 1 124 ? -1.185  -4.346  55.242  1.00 15.72 ? 124 ASP B CG  1 
ATOM   2024 O OD1 . ASP B 1 124 ? -0.797  -5.359  55.837  1.00 20.75 ? 124 ASP B OD1 1 
ATOM   2025 O OD2 . ASP B 1 124 ? -0.581  -3.930  54.266  1.00 10.12 ? 124 ASP B OD2 1 
ATOM   2026 N N   . ASP B 1 125 ? -1.972  -4.944  58.911  1.00 13.40 ? 125 ASP B N   1 
ATOM   2027 C CA  . ASP B 1 125 ? -1.098  -4.744  60.081  1.00 14.21 ? 125 ASP B CA  1 
ATOM   2028 C C   . ASP B 1 125 ? 0.343   -4.618  59.623  1.00 14.28 ? 125 ASP B C   1 
ATOM   2029 O O   . ASP B 1 125 ? 1.242   -4.703  60.416  1.00 16.18 ? 125 ASP B O   1 
ATOM   2030 C CB  . ASP B 1 125 ? -1.237  -5.905  61.090  1.00 12.13 ? 125 ASP B CB  1 
ATOM   2031 C CG  . ASP B 1 125 ? -0.778  -7.198  60.523  1.00 13.24 ? 125 ASP B CG  1 
ATOM   2032 O OD1 . ASP B 1 125 ? 0.038   -7.109  59.593  1.00 16.03 ? 125 ASP B OD1 1 
ATOM   2033 O OD2 . ASP B 1 125 ? -1.185  -8.296  61.004  1.00 12.20 ? 125 ASP B OD2 1 
ATOM   2034 N N   . LEU B 1 126 ? 0.593   -4.403  58.350  1.00 15.02 ? 126 LEU B N   1 
ATOM   2035 C CA  . LEU B 1 126 ? 1.969   -4.162  57.845  1.00 14.67 ? 126 LEU B CA  1 
ATOM   2036 C C   . LEU B 1 126 ? 3.040   -5.198  58.185  1.00 15.81 ? 126 LEU B C   1 
ATOM   2037 O O   . LEU B 1 126 ? 4.186   -4.862  58.241  1.00 17.43 ? 126 LEU B O   1 
ATOM   2038 C CB  . LEU B 1 126 ? 2.465   -2.736  58.209  1.00 14.35 ? 126 LEU B CB  1 
ATOM   2039 C CG  . LEU B 1 126 ? 1.563   -1.522  57.942  1.00 12.14 ? 126 LEU B CG  1 
ATOM   2040 C CD1 . LEU B 1 126 ? 2.229   -0.210  58.255  1.00 16.45 ? 126 LEU B CD1 1 
ATOM   2041 C CD2 . LEU B 1 126 ? 0.981   -1.468  56.564  1.00 14.82 ? 126 LEU B CD2 1 
ATOM   2042 N N   . GLY B 1 127 ? 2.690   -6.462  58.359  1.00 18.35 ? 127 GLY B N   1 
ATOM   2043 C CA  . GLY B 1 127 ? 3.656   -7.492  58.793  1.00 17.70 ? 127 GLY B CA  1 
ATOM   2044 C C   . GLY B 1 127 ? 4.057   -7.480  60.258  1.00 19.39 ? 127 GLY B C   1 
ATOM   2045 O O   . GLY B 1 127 ? 4.723   -8.427  60.721  1.00 17.91 ? 127 GLY B O   1 
ATOM   2046 N N   . LYS B 1 128 ? 3.643   -6.424  60.975  1.00 20.21 ? 128 LYS B N   1 
ATOM   2047 C CA  . LYS B 1 128 ? 3.777   -6.261  62.452  1.00 21.84 ? 128 LYS B CA  1 
ATOM   2048 C C   . LYS B 1 128 ? 2.486   -6.505  63.255  1.00 21.83 ? 128 LYS B C   1 
ATOM   2049 O O   . LYS B 1 128 ? 2.127   -5.721  64.120  1.00 22.03 ? 128 LYS B O   1 
ATOM   2050 C CB  . LYS B 1 128 ? 4.331   -4.873  62.814  1.00 23.21 ? 128 LYS B CB  1 
ATOM   2051 C CG  . LYS B 1 128 ? 5.405   -4.438  61.856  1.00 23.72 ? 128 LYS B CG  1 
ATOM   2052 C CD  . LYS B 1 128 ? 6.483   -3.618  62.503  1.00 30.02 ? 128 LYS B CD  1 
ATOM   2053 C CE  . LYS B 1 128 ? 7.594   -3.288  61.476  1.00 31.39 ? 128 LYS B CE  1 
ATOM   2054 N NZ  . LYS B 1 128 ? 8.143   -4.522  60.739  1.00 29.03 ? 128 LYS B NZ  1 
ATOM   2055 N N   . GLY B 1 129 ? 1.835   -7.630  62.993  1.00 21.65 ? 129 GLY B N   1 
ATOM   2056 C CA  . GLY B 1 129 ? 0.614   -8.041  63.708  1.00 21.59 ? 129 GLY B CA  1 
ATOM   2057 C C   . GLY B 1 129 ? 0.718   -9.254  64.600  1.00 21.21 ? 129 GLY B C   1 
ATOM   2058 O O   . GLY B 1 129 ? -0.220  -9.564  65.302  1.00 20.96 ? 129 GLY B O   1 
ATOM   2059 N N   . GLY B 1 130 ? 1.859   -9.947  64.581  1.00 21.48 ? 130 GLY B N   1 
ATOM   2060 C CA  . GLY B 1 130 ? 2.155   -10.953 65.602  1.00 21.35 ? 130 GLY B CA  1 
ATOM   2061 C C   . GLY B 1 130 ? 1.809   -12.372 65.263  1.00 21.32 ? 130 GLY B C   1 
ATOM   2062 O O   . GLY B 1 130 ? 1.914   -13.257 66.117  1.00 21.13 ? 130 GLY B O   1 
ATOM   2063 N N   . ASN B 1 131 ? 1.394   -12.610 64.031  1.00 21.47 ? 131 ASN B N   1 
ATOM   2064 C CA  . ASN B 1 131 ? 1.097   -13.969 63.614  1.00 22.37 ? 131 ASN B CA  1 
ATOM   2065 C C   . ASN B 1 131 ? 1.583   -14.281 62.199  1.00 22.89 ? 131 ASN B C   1 
ATOM   2066 O O   . ASN B 1 131 ? 2.028   -13.404 61.479  1.00 21.99 ? 131 ASN B O   1 
ATOM   2067 C CB  . ASN B 1 131 ? -0.400  -14.311 63.789  1.00 22.01 ? 131 ASN B CB  1 
ATOM   2068 C CG  . ASN B 1 131 ? -1.296  -13.365 63.044  1.00 20.89 ? 131 ASN B CG  1 
ATOM   2069 O OD1 . ASN B 1 131 ? -0.882  -12.788 62.063  1.00 20.80 ? 131 ASN B OD1 1 
ATOM   2070 N ND2 . ASN B 1 131 ? -2.534  -13.201 63.502  1.00 18.58 ? 131 ASN B ND2 1 
ATOM   2071 N N   . GLU B 1 132 ? 1.489   -15.550 61.832  1.00 23.94 ? 132 GLU B N   1 
ATOM   2072 C CA  . GLU B 1 132 ? 2.005   -16.016 60.598  1.00 25.40 ? 132 GLU B CA  1 
ATOM   2073 C C   . GLU B 1 132 ? 1.308   -15.434 59.382  1.00 26.38 ? 132 GLU B C   1 
ATOM   2074 O O   . GLU B 1 132 ? 1.966   -15.229 58.367  1.00 27.05 ? 132 GLU B O   1 
ATOM   2075 C CB  . GLU B 1 132 ? 1.927   -17.520 60.584  1.00 27.18 ? 132 GLU B CB  1 
ATOM   2076 C CG  . GLU B 1 132 ? 2.167   -18.126 59.249  1.00 28.66 ? 132 GLU B CG  1 
ATOM   2077 C CD  . GLU B 1 132 ? 2.148   -19.630 59.343  1.00 34.61 ? 132 GLU B CD  1 
ATOM   2078 O OE1 . GLU B 1 132 ? 1.013   -20.200 59.383  1.00 33.54 ? 132 GLU B OE1 1 
ATOM   2079 O OE2 . GLU B 1 132 ? 3.267   -20.204 59.392  1.00 31.68 ? 132 GLU B OE2 1 
ATOM   2080 N N   . GLU B 1 133 ? 0.000   -15.150 59.482  1.00 26.61 ? 133 GLU B N   1 
ATOM   2081 C CA  . GLU B 1 133 ? -0.760  -14.492 58.403  1.00 26.46 ? 133 GLU B CA  1 
ATOM   2082 C C   . GLU B 1 133 ? -0.284  -13.054 58.135  1.00 25.98 ? 133 GLU B C   1 
ATOM   2083 O O   . GLU B 1 133 ? -0.318  -12.571 57.012  1.00 25.26 ? 133 GLU B O   1 
ATOM   2084 C CB  . GLU B 1 133 ? -2.266  -14.452 58.739  1.00 26.89 ? 133 GLU B CB  1 
ATOM   2085 C CG  . GLU B 1 133 ? -3.172  -14.229 57.541  1.00 28.73 ? 133 GLU B CG  1 
ATOM   2086 C CD  . GLU B 1 133 ? -2.764  -15.062 56.324  1.00 35.28 ? 133 GLU B CD  1 
ATOM   2087 O OE1 . GLU B 1 133 ? -2.251  -16.203 56.502  1.00 35.92 ? 133 GLU B OE1 1 
ATOM   2088 O OE2 . GLU B 1 133 ? -2.949  -14.565 55.182  1.00 35.25 ? 133 GLU B OE2 1 
ATOM   2089 N N   . SER B 1 134 ? 0.137   -12.375 59.187  1.00 25.79 ? 134 SER B N   1 
ATOM   2090 C CA  . SER B 1 134 ? 0.658   -11.021 59.082  1.00 25.32 ? 134 SER B CA  1 
ATOM   2091 C C   . SER B 1 134 ? 1.800   -10.846 58.060  1.00 25.34 ? 134 SER B C   1 
ATOM   2092 O O   . SER B 1 134 ? 1.875   -9.825  57.382  1.00 26.16 ? 134 SER B O   1 
ATOM   2093 C CB  . SER B 1 134 ? 1.112   -10.539 60.454  1.00 25.59 ? 134 SER B CB  1 
ATOM   2094 O OG  . SER B 1 134 ? 1.116   -9.130  60.482  1.00 22.23 ? 134 SER B OG  1 
ATOM   2095 N N   . THR B 1 135 ? 2.675   -11.845 57.947  1.00 25.37 ? 135 THR B N   1 
ATOM   2096 C CA  . THR B 1 135 ? 3.852   -11.743 57.105  1.00 24.89 ? 135 THR B CA  1 
ATOM   2097 C C   . THR B 1 135 ? 3.555   -12.302 55.708  1.00 24.96 ? 135 THR B C   1 
ATOM   2098 O O   . THR B 1 135 ? 4.431   -12.374 54.861  1.00 25.90 ? 135 THR B O   1 
ATOM   2099 C CB  . THR B 1 135 ? 5.068   -12.480 57.736  1.00 25.06 ? 135 THR B CB  1 
ATOM   2100 O OG1 . THR B 1 135 ? 4.774   -13.884 57.913  1.00 26.20 ? 135 THR B OG1 1 
ATOM   2101 C CG2 . THR B 1 135 ? 5.433   -11.903 59.057  1.00 23.63 ? 135 THR B CG2 1 
ATOM   2102 N N   . LYS B 1 136 ? 2.325   -12.735 55.478  1.00 24.51 ? 136 LYS B N   1 
ATOM   2103 C CA  . LYS B 1 136 ? 1.862   -13.044 54.152  1.00 24.82 ? 136 LYS B CA  1 
ATOM   2104 C C   . LYS B 1 136 ? 0.991   -11.929 53.562  1.00 25.02 ? 136 LYS B C   1 
ATOM   2105 O O   . LYS B 1 136 ? 1.353   -11.350 52.570  1.00 26.07 ? 136 LYS B O   1 
ATOM   2106 C CB  . LYS B 1 136 ? 1.151   -14.389 54.150  1.00 25.33 ? 136 LYS B CB  1 
ATOM   2107 C CG  . LYS B 1 136 ? 2.081   -15.447 54.566  1.00 26.24 ? 136 LYS B CG  1 
ATOM   2108 C CD  . LYS B 1 136 ? 1.572   -16.834 54.359  1.00 30.82 ? 136 LYS B CD  1 
ATOM   2109 C CE  . LYS B 1 136 ? 2.365   -17.714 55.287  1.00 31.34 ? 136 LYS B CE  1 
ATOM   2110 N NZ  . LYS B 1 136 ? 1.728   -19.032 55.421  1.00 36.13 ? 136 LYS B NZ  1 
ATOM   2111 N N   . THR B 1 137 ? -0.157  -11.641 54.175  1.00 25.07 ? 137 THR B N   1 
ATOM   2112 C CA  . THR B 1 137 ? -1.172  -10.739 53.633  1.00 24.28 ? 137 THR B CA  1 
ATOM   2113 C C   . THR B 1 137 ? -1.453  -9.524  54.521  1.00 24.14 ? 137 THR B C   1 
ATOM   2114 O O   . THR B 1 137 ? -2.250  -8.644  54.178  1.00 24.76 ? 137 THR B O   1 
ATOM   2115 C CB  . THR B 1 137 ? -2.437  -11.494 53.581  1.00 24.38 ? 137 THR B CB  1 
ATOM   2116 O OG1 . THR B 1 137 ? -2.867  -11.751 54.917  1.00 26.05 ? 137 THR B OG1 1 
ATOM   2117 C CG2 . THR B 1 137 ? -2.216  -12.835 52.878  1.00 24.59 ? 137 THR B CG2 1 
ATOM   2118 N N   . GLY B 1 138 ? -0.846  -9.482  55.705  1.00 23.90 ? 138 GLY B N   1 
ATOM   2119 C CA  . GLY B 1 138 ? -1.046  -8.352  56.609  1.00 21.83 ? 138 GLY B CA  1 
ATOM   2120 C C   . GLY B 1 138 ? -2.399  -8.351  57.315  1.00 20.57 ? 138 GLY B C   1 
ATOM   2121 O O   . GLY B 1 138 ? -2.730  -7.375  57.949  1.00 19.96 ? 138 GLY B O   1 
ATOM   2122 N N   . ASN B 1 139 ? -3.154  -9.446  57.186  1.00 19.62 ? 139 ASN B N   1 
ATOM   2123 C CA  . ASN B 1 139 ? -4.489  -9.628  57.795  1.00 20.04 ? 139 ASN B CA  1 
ATOM   2124 C C   . ASN B 1 139 ? -5.529  -8.528  57.522  1.00 19.15 ? 139 ASN B C   1 
ATOM   2125 O O   . ASN B 1 139 ? -6.263  -8.134  58.432  1.00 19.26 ? 139 ASN B O   1 
ATOM   2126 C CB  . ASN B 1 139 ? -4.325  -9.690  59.304  1.00 20.40 ? 139 ASN B CB  1 
ATOM   2127 C CG  . ASN B 1 139 ? -3.814  -11.032 59.797  1.00 25.20 ? 139 ASN B CG  1 
ATOM   2128 O OD1 . ASN B 1 139 ? -4.076  -12.083 59.201  1.00 26.72 ? 139 ASN B OD1 1 
ATOM   2129 N ND2 . ASN B 1 139 ? -3.065  -10.993 60.905  1.00 30.57 ? 139 ASN B ND2 1 
ATOM   2130 N N   . ALA B 1 140 ? -5.605  -8.023  56.295  1.00 18.80 ? 140 ALA B N   1 
ATOM   2131 C CA  . ALA B 1 140 ? -6.456  -6.859  55.999  1.00 18.29 ? 140 ALA B CA  1 
ATOM   2132 C C   . ALA B 1 140 ? -7.941  -7.278  55.741  1.00 18.25 ? 140 ALA B C   1 
ATOM   2133 O O   . ALA B 1 140 ? -8.844  -6.428  55.705  1.00 17.39 ? 140 ALA B O   1 
ATOM   2134 C CB  . ALA B 1 140 ? -5.847  -6.040  54.851  1.00 18.09 ? 140 ALA B CB  1 
ATOM   2135 N N   . GLY B 1 141 ? -8.190  -8.579  55.649  1.00 16.11 ? 141 GLY B N   1 
ATOM   2136 C CA  . GLY B 1 141 ? -9.582  -9.092  55.645  1.00 16.87 ? 141 GLY B CA  1 
ATOM   2137 C C   . GLY B 1 141 ? -9.983  -9.287  54.215  1.00 16.72 ? 141 GLY B C   1 
ATOM   2138 O O   . GLY B 1 141 ? -9.128  -9.390  53.368  1.00 16.93 ? 141 GLY B O   1 
ATOM   2139 N N   . SER B 1 142 ? -11.284 -9.311  53.930  1.00 17.54 ? 142 SER B N   1 
ATOM   2140 C CA  . SER B 1 142 ? -11.763 -9.547  52.572  1.00 16.15 ? 142 SER B CA  1 
ATOM   2141 C C   . SER B 1 142 ? -11.665 -8.322  51.659  1.00 17.01 ? 142 SER B C   1 
ATOM   2142 O O   . SER B 1 142 ? -11.278 -7.234  52.080  1.00 13.73 ? 142 SER B O   1 
ATOM   2143 C CB  . SER B 1 142 ? -13.204 -10.045 52.619  1.00 18.29 ? 142 SER B CB  1 
ATOM   2144 O OG  . SER B 1 142 ? -13.941 -9.140  53.372  1.00 13.31 ? 142 SER B OG  1 
ATOM   2145 N N   . ARG B 1 143 ? -12.047 -8.557  50.408  1.00 16.71 ? 143 ARG B N   1 
ATOM   2146 C CA  . ARG B 1 143 ? -11.834 -7.664  49.321  1.00 17.33 ? 143 ARG B CA  1 
ATOM   2147 C C   . ARG B 1 143 ? -13.158 -6.924  49.124  1.00 16.90 ? 143 ARG B C   1 
ATOM   2148 O O   . ARG B 1 143 ? -14.142 -7.481  48.619  1.00 17.97 ? 143 ARG B O   1 
ATOM   2149 C CB  . ARG B 1 143 ? -11.409 -8.525  48.121  1.00 16.87 ? 143 ARG B CB  1 
ATOM   2150 C CG  . ARG B 1 143 ? -10.111 -9.348  48.391  1.00 17.68 ? 143 ARG B CG  1 
ATOM   2151 C CD  . ARG B 1 143 ? -9.625  -10.269 47.235  1.00 15.81 ? 143 ARG B CD  1 
ATOM   2152 N NE  . ARG B 1 143 ? -8.493  -11.085 47.690  1.00 18.14 ? 143 ARG B NE  1 
ATOM   2153 C CZ  . ARG B 1 143 ? -7.656  -11.774 46.899  1.00 12.82 ? 143 ARG B CZ  1 
ATOM   2154 N NH1 . ARG B 1 143 ? -7.736  -11.686 45.568  1.00 12.17 ? 143 ARG B NH1 1 
ATOM   2155 N NH2 . ARG B 1 143 ? -6.661  -12.482 47.435  1.00 11.68 ? 143 ARG B NH2 1 
ATOM   2156 N N   . LEU B 1 144 ? -13.200 -5.650  49.521  1.00 15.81 ? 144 LEU B N   1 
ATOM   2157 C CA  . LEU B 1 144 ? -14.484 -4.890  49.499  1.00 14.27 ? 144 LEU B CA  1 
ATOM   2158 C C   . LEU B 1 144 ? -14.854 -4.422  48.102  1.00 13.57 ? 144 LEU B C   1 
ATOM   2159 O O   . LEU B 1 144 ? -16.039 -4.395  47.699  1.00 13.17 ? 144 LEU B O   1 
ATOM   2160 C CB  . LEU B 1 144 ? -14.388 -3.656  50.387  1.00 12.40 ? 144 LEU B CB  1 
ATOM   2161 C CG  . LEU B 1 144 ? -14.056 -3.892  51.842  1.00 13.04 ? 144 LEU B CG  1 
ATOM   2162 C CD1 . LEU B 1 144 ? -13.874 -2.520  52.511  1.00 18.65 ? 144 LEU B CD1 1 
ATOM   2163 C CD2 . LEU B 1 144 ? -15.119 -4.761  52.491  1.00 18.28 ? 144 LEU B CD2 1 
ATOM   2164 N N   . ALA B 1 145 ? -13.816 -4.037  47.376  1.00 12.25 ? 145 ALA B N   1 
ATOM   2165 C CA  . ALA B 1 145 ? -13.920 -3.390  46.110  1.00 9.68  ? 145 ALA B CA  1 
ATOM   2166 C C   . ALA B 1 145 ? -12.571 -3.642  45.374  1.00 9.95  ? 145 ALA B C   1 
ATOM   2167 O O   . ALA B 1 145 ? -11.511 -3.656  46.011  1.00 7.76  ? 145 ALA B O   1 
ATOM   2168 C CB  . ALA B 1 145 ? -14.171 -1.877  46.328  1.00 11.76 ? 145 ALA B CB  1 
ATOM   2169 N N   . CYS B 1 146 ? -12.636 -3.827  44.044  1.00 8.57  ? 146 CYS B N   1 
ATOM   2170 C CA  . CYS B 1 146 ? -11.463 -4.008  43.157  1.00 6.33  ? 146 CYS B CA  1 
ATOM   2171 C C   . CYS B 1 146 ? -11.686 -3.478  41.767  1.00 3.83  ? 146 CYS B C   1 
ATOM   2172 O O   . CYS B 1 146 ? -12.802 -3.237  41.353  1.00 7.82  ? 146 CYS B O   1 
ATOM   2173 C CB  . CYS B 1 146 ? -11.076 -5.506  43.108  1.00 6.58  ? 146 CYS B CB  1 
ATOM   2174 S SG  . CYS B 1 146 ? -12.279 -6.555  42.576  1.00 10.66 ? 146 CYS B SG  1 
ATOM   2175 N N   . GLY B 1 147 ? -10.643 -3.229  41.022  1.00 2.00  ? 147 GLY B N   1 
ATOM   2176 C CA  . GLY B 1 147 ? -10.781 -2.865  39.649  1.00 2.00  ? 147 GLY B CA  1 
ATOM   2177 C C   . GLY B 1 147 ? -9.425  -3.022  38.981  1.00 2.00  ? 147 GLY B C   1 
ATOM   2178 O O   . GLY B 1 147 ? -8.390  -2.756  39.603  1.00 2.00  ? 147 GLY B O   1 
ATOM   2179 N N   . VAL B 1 148 ? -9.447  -3.552  37.731  1.00 3.57  ? 148 VAL B N   1 
ATOM   2180 C CA  . VAL B 1 148 ? -8.275  -3.761  36.878  1.00 2.00  ? 148 VAL B CA  1 
ATOM   2181 C C   . VAL B 1 148 ? -7.731  -2.349  36.575  1.00 4.44  ? 148 VAL B C   1 
ATOM   2182 O O   . VAL B 1 148 ? -8.517  -1.447  36.200  1.00 2.00  ? 148 VAL B O   1 
ATOM   2183 C CB  . VAL B 1 148 ? -8.731  -4.522  35.603  1.00 2.70  ? 148 VAL B CB  1 
ATOM   2184 C CG1 . VAL B 1 148 ? -7.651  -4.738  34.613  1.00 3.85  ? 148 VAL B CG1 1 
ATOM   2185 C CG2 . VAL B 1 148 ? -9.311  -5.854  36.011  1.00 3.34  ? 148 VAL B CG2 1 
ATOM   2186 N N   . ILE B 1 149 ? -6.419  -2.188  36.774  1.00 3.09  ? 149 ILE B N   1 
ATOM   2187 C CA  . ILE B 1 149 ? -5.795  -0.896  36.479  1.00 4.85  ? 149 ILE B CA  1 
ATOM   2188 C C   . ILE B 1 149 ? -5.599  -0.794  34.966  1.00 5.87  ? 149 ILE B C   1 
ATOM   2189 O O   . ILE B 1 149 ? -5.031  -1.696  34.311  1.00 6.18  ? 149 ILE B O   1 
ATOM   2190 C CB  . ILE B 1 149 ? -4.452  -0.722  37.252  1.00 4.84  ? 149 ILE B CB  1 
ATOM   2191 C CG1 . ILE B 1 149 ? -4.656  -0.813  38.770  1.00 2.00  ? 149 ILE B CG1 1 
ATOM   2192 C CG2 . ILE B 1 149 ? -3.728  0.605   36.799  1.00 2.00  ? 149 ILE B CG2 1 
ATOM   2193 C CD1 . ILE B 1 149 ? -3.507  -1.339  39.494  1.00 2.00  ? 149 ILE B CD1 1 
ATOM   2194 N N   . GLY B 1 150 ? -5.972  0.363   34.374  1.00 5.84  ? 150 GLY B N   1 
ATOM   2195 C CA  . GLY B 1 150 ? -5.957  0.440   32.976  1.00 3.09  ? 150 GLY B CA  1 
ATOM   2196 C C   . GLY B 1 150 ? -5.294  1.731   32.569  1.00 6.32  ? 150 GLY B C   1 
ATOM   2197 O O   . GLY B 1 150 ? -5.191  2.660   33.396  1.00 4.26  ? 150 GLY B O   1 
ATOM   2198 N N   . ILE B 1 151 ? -4.787  1.761   31.329  1.00 6.72  ? 151 ILE B N   1 
ATOM   2199 C CA  . ILE B 1 151 ? -4.092  2.889   30.712  1.00 7.18  ? 151 ILE B CA  1 
ATOM   2200 C C   . ILE B 1 151 ? -5.082  4.061   30.723  1.00 9.01  ? 151 ILE B C   1 
ATOM   2201 O O   . ILE B 1 151 ? -6.221  3.879   30.448  1.00 8.51  ? 151 ILE B O   1 
ATOM   2202 C CB  . ILE B 1 151 ? -3.823  2.432   29.270  1.00 9.01  ? 151 ILE B CB  1 
ATOM   2203 C CG1 . ILE B 1 151 ? -3.194  1.049   29.318  1.00 2.00  ? 151 ILE B CG1 1 
ATOM   2204 C CG2 . ILE B 1 151 ? -2.847  3.250   28.532  1.00 3.44  ? 151 ILE B CG2 1 
ATOM   2205 C CD1 . ILE B 1 151 ? -2.298  0.816   28.182  1.00 2.00  ? 151 ILE B CD1 1 
ATOM   2206 N N   . ALA B 1 152 ? -4.666  5.298   30.943  1.00 11.38 ? 152 ALA B N   1 
ATOM   2207 C CA  . ALA B 1 152 ? -5.640  6.329   30.939  1.00 12.66 ? 152 ALA B CA  1 
ATOM   2208 C C   . ALA B 1 152 ? -5.075  7.390   30.074  1.00 15.43 ? 152 ALA B C   1 
ATOM   2209 O O   . ALA B 1 152 ? -3.879  7.361   29.745  1.00 15.53 ? 152 ALA B O   1 
ATOM   2210 C CB  . ALA B 1 152 ? -5.833  6.876   32.329  1.00 13.87 ? 152 ALA B CB  1 
ATOM   2211 N N   . GLN B 1 153 ? -5.935  8.325   29.721  1.00 15.86 ? 153 GLN B N   1 
ATOM   2212 C CA  . GLN B 1 153 ? -5.583  9.430   28.852  1.00 18.32 ? 153 GLN B CA  1 
ATOM   2213 C C   . GLN B 1 153 ? -4.917  10.478  29.664  1.00 18.51 ? 153 GLN B C   1 
ATOM   2214 O O   . GLN B 1 153 ? -5.483  10.902  30.683  1.00 18.76 ? 153 GLN B O   1 
ATOM   2215 C CB  . GLN B 1 153 ? -6.810  10.022  28.170  1.00 16.45 ? 153 GLN B CB  1 
ATOM   2216 C CG  . GLN B 1 153 ? -6.445  10.789  26.911  1.00 20.18 ? 153 GLN B CG  1 
ATOM   2217 C CD  . GLN B 1 153 ? -7.599  10.883  25.971  1.00 19.70 ? 153 GLN B CD  1 
ATOM   2218 O OE1 . GLN B 1 153 ? -8.616  10.250  26.188  1.00 20.11 ? 153 GLN B OE1 1 
ATOM   2219 N NE2 . GLN B 1 153 ? -7.458  11.661  24.920  1.00 22.20 ? 153 GLN B NE2 1 
ATOM   2220 O OXT . GLN B 1 153 ? -3.832  10.899  29.210  1.00 21.33 ? 153 GLN B OXT 1 
ATOM   2221 N N   . ALA C 1 1   ? 15.259  -1.752  27.472  1.00 20.03 ? 1   ALA C N   1 
ATOM   2222 C CA  . ALA C 1 1   ? 16.550  -2.594  27.552  1.00 17.98 ? 1   ALA C CA  1 
ATOM   2223 C C   . ALA C 1 1   ? 17.049  -2.818  28.973  1.00 16.88 ? 1   ALA C C   1 
ATOM   2224 O O   . ALA C 1 1   ? 16.836  -1.985  29.818  1.00 16.67 ? 1   ALA C O   1 
ATOM   2225 C CB  . ALA C 1 1   ? 17.646  -1.951  26.702  1.00 19.19 ? 1   ALA C CB  1 
ATOM   2226 N N   . THR C 1 2   ? 17.655  -3.973  29.262  1.00 15.52 ? 2   THR C N   1 
ATOM   2227 C CA  . THR C 1 2   ? 18.286  -4.183  30.565  1.00 14.97 ? 2   THR C CA  1 
ATOM   2228 C C   . THR C 1 2   ? 19.841  -3.967  30.563  1.00 14.07 ? 2   THR C C   1 
ATOM   2229 O O   . THR C 1 2   ? 20.450  -3.987  31.613  1.00 13.85 ? 2   THR C O   1 
ATOM   2230 C CB  . THR C 1 2   ? 17.973  -5.586  31.202  1.00 17.35 ? 2   THR C CB  1 
ATOM   2231 O OG1 . THR C 1 2   ? 18.497  -6.597  30.377  1.00 14.83 ? 2   THR C OG1 1 
ATOM   2232 C CG2 . THR C 1 2   ? 16.455  -5.843  31.381  1.00 17.08 ? 2   THR C CG2 1 
ATOM   2233 N N   . LYS C 1 3   ? 20.451  -3.692  29.405  1.00 13.07 ? 3   LYS C N   1 
ATOM   2234 C CA  . LYS C 1 3   ? 21.918  -3.726  29.228  1.00 12.26 ? 3   LYS C CA  1 
ATOM   2235 C C   . LYS C 1 3   ? 22.334  -2.882  28.086  1.00 11.28 ? 3   LYS C C   1 
ATOM   2236 O O   . LYS C 1 3   ? 21.692  -2.857  27.009  1.00 10.38 ? 3   LYS C O   1 
ATOM   2237 C CB  . LYS C 1 3   ? 22.377  -5.157  28.877  1.00 12.51 ? 3   LYS C CB  1 
ATOM   2238 C CG  . LYS C 1 3   ? 22.759  -5.955  30.031  1.00 16.77 ? 3   LYS C CG  1 
ATOM   2239 C CD  . LYS C 1 3   ? 24.062  -6.657  29.743  1.00 22.97 ? 3   LYS C CD  1 
ATOM   2240 C CE  . LYS C 1 3   ? 24.983  -6.495  30.942  1.00 29.08 ? 3   LYS C CE  1 
ATOM   2241 N NZ  . LYS C 1 3   ? 26.467  -6.838  30.760  1.00 34.06 ? 3   LYS C NZ  1 
ATOM   2242 N N   . ALA C 1 4   ? 23.454  -2.212  28.291  1.00 10.80 ? 4   ALA C N   1 
ATOM   2243 C CA  . ALA C 1 4   ? 23.993  -1.351  27.306  1.00 10.07 ? 4   ALA C CA  1 
ATOM   2244 C C   . ALA C 1 4   ? 25.541  -1.470  27.444  1.00 10.59 ? 4   ALA C C   1 
ATOM   2245 O O   . ALA C 1 4   ? 26.078  -2.176  28.350  1.00 10.94 ? 4   ALA C O   1 
ATOM   2246 C CB  . ALA C 1 4   ? 23.450  0.148   27.484  1.00 8.43  ? 4   ALA C CB  1 
ATOM   2247 N N   . VAL C 1 5   ? 26.241  -0.828  26.523  1.00 10.92 ? 5   VAL C N   1 
ATOM   2248 C CA  . VAL C 1 5   ? 27.708  -0.923  26.410  1.00 9.38  ? 5   VAL C CA  1 
ATOM   2249 C C   . VAL C 1 5   ? 28.128  0.343   25.657  1.00 9.58  ? 5   VAL C C   1 
ATOM   2250 O O   . VAL C 1 5   ? 27.324  0.888   24.906  1.00 6.47  ? 5   VAL C O   1 
ATOM   2251 C CB  . VAL C 1 5   ? 28.092  -2.174  25.604  1.00 9.15  ? 5   VAL C CB  1 
ATOM   2252 C CG1 . VAL C 1 5   ? 27.891  -1.885  24.190  1.00 11.68 ? 5   VAL C CG1 1 
ATOM   2253 C CG2 . VAL C 1 5   ? 29.577  -2.675  25.898  1.00 10.86 ? 5   VAL C CG2 1 
ATOM   2254 N N   . CYS C 1 6   ? 29.401  0.703   25.778  1.00 10.55 ? 6   CYS C N   1 
ATOM   2255 C CA  . CYS C 1 6   ? 29.964  1.920   25.264  1.00 12.02 ? 6   CYS C CA  1 
ATOM   2256 C C   . CYS C 1 6   ? 31.420  1.545   25.133  1.00 12.66 ? 6   CYS C C   1 
ATOM   2257 O O   . CYS C 1 6   ? 31.967  0.934   26.019  1.00 12.00 ? 6   CYS C O   1 
ATOM   2258 C CB  . CYS C 1 6   ? 29.770  3.061   26.226  1.00 10.38 ? 6   CYS C CB  1 
ATOM   2259 S SG  . CYS C 1 6   ? 30.249  4.595   25.568  1.00 14.55 ? 6   CYS C SG  1 
ATOM   2260 N N   . VAL C 1 7   ? 32.028  1.880   23.990  1.00 13.89 ? 7   VAL C N   1 
ATOM   2261 C CA  . VAL C 1 7   ? 33.482  1.797   23.750  1.00 12.18 ? 7   VAL C CA  1 
ATOM   2262 C C   . VAL C 1 7   ? 33.866  3.284   23.586  1.00 11.22 ? 7   VAL C C   1 
ATOM   2263 O O   . VAL C 1 7   ? 33.286  3.910   22.788  1.00 9.57  ? 7   VAL C O   1 
ATOM   2264 C CB  . VAL C 1 7   ? 33.702  0.995   22.475  1.00 13.13 ? 7   VAL C CB  1 
ATOM   2265 C CG1 . VAL C 1 7   ? 35.193  0.847   22.117  1.00 15.58 ? 7   VAL C CG1 1 
ATOM   2266 C CG2 . VAL C 1 7   ? 33.137  -0.400  22.633  1.00 16.45 ? 7   VAL C CG2 1 
ATOM   2267 N N   . LEU C 1 8   ? 34.801  3.815   24.391  1.00 12.46 ? 8   LEU C N   1 
ATOM   2268 C CA  . LEU C 1 8   ? 35.257  5.220   24.370  1.00 12.12 ? 8   LEU C CA  1 
ATOM   2269 C C   . LEU C 1 8   ? 36.606  5.286   23.599  1.00 11.08 ? 8   LEU C C   1 
ATOM   2270 O O   . LEU C 1 8   ? 37.353  4.373   23.663  1.00 10.74 ? 8   LEU C O   1 
ATOM   2271 C CB  . LEU C 1 8   ? 35.461  5.746   25.811  1.00 12.36 ? 8   LEU C CB  1 
ATOM   2272 C CG  . LEU C 1 8   ? 34.323  5.693   26.842  1.00 13.46 ? 8   LEU C CG  1 
ATOM   2273 C CD1 . LEU C 1 8   ? 34.827  5.347   28.268  1.00 15.07 ? 8   LEU C CD1 1 
ATOM   2274 C CD2 . LEU C 1 8   ? 33.752  7.022   26.896  1.00 12.41 ? 8   LEU C CD2 1 
ATOM   2275 N N   . LYS C 1 9   ? 36.831  6.328   22.784  1.00 9.31  ? 9   LYS C N   1 
ATOM   2276 C CA  . LYS C 1 9   ? 38.020  6.554   22.014  1.00 8.96  ? 9   LYS C CA  1 
ATOM   2277 C C   . LYS C 1 9   ? 37.933  8.040   21.743  1.00 10.35 ? 9   LYS C C   1 
ATOM   2278 O O   . LYS C 1 9   ? 36.861  8.643   21.849  1.00 7.72  ? 9   LYS C O   1 
ATOM   2279 C CB  . LYS C 1 9   ? 38.056  5.764   20.711  1.00 11.28 ? 9   LYS C CB  1 
ATOM   2280 C CG  . LYS C 1 9   ? 37.971  4.198   20.998  1.00 10.24 ? 9   LYS C CG  1 
ATOM   2281 C CD  . LYS C 1 9   ? 38.193  3.385   19.730  1.00 18.20 ? 9   LYS C CD  1 
ATOM   2282 C CE  . LYS C 1 9   ? 38.282  1.881   20.068  1.00 19.47 ? 9   LYS C CE  1 
ATOM   2283 N NZ  . LYS C 1 9   ? 39.323  1.662   21.127  1.00 25.42 ? 9   LYS C NZ  1 
ATOM   2284 N N   . GLY C 1 10  ? 39.060  8.640   21.466  1.00 12.18 ? 10  GLY C N   1 
ATOM   2285 C CA  . GLY C 1 10  ? 39.084  10.128  21.261  1.00 11.37 ? 10  GLY C CA  1 
ATOM   2286 C C   . GLY C 1 10  ? 40.340  10.330  20.483  1.00 14.42 ? 10  GLY C C   1 
ATOM   2287 O O   . GLY C 1 10  ? 40.905  9.368   19.968  1.00 14.21 ? 10  GLY C O   1 
ATOM   2288 N N   . ASP C 1 11  ? 40.808  11.564  20.416  1.00 15.97 ? 11  ASP C N   1 
ATOM   2289 C CA  . ASP C 1 11  ? 42.012  11.885  19.649  1.00 18.69 ? 11  ASP C CA  1 
ATOM   2290 C C   . ASP C 1 11  ? 43.381  11.455  20.244  1.00 17.88 ? 11  ASP C C   1 
ATOM   2291 O O   . ASP C 1 11  ? 44.343  11.378  19.508  1.00 18.16 ? 11  ASP C O   1 
ATOM   2292 C CB  . ASP C 1 11  ? 42.032  13.402  19.490  1.00 19.38 ? 11  ASP C CB  1 
ATOM   2293 C CG  . ASP C 1 11  ? 40.861  13.899  18.700  1.00 24.88 ? 11  ASP C CG  1 
ATOM   2294 O OD1 . ASP C 1 11  ? 40.360  13.110  17.835  1.00 28.23 ? 11  ASP C OD1 1 
ATOM   2295 O OD2 . ASP C 1 11  ? 40.471  15.085  18.927  1.00 29.07 ? 11  ASP C OD2 1 
ATOM   2296 N N   . GLY C 1 12  ? 43.454  11.296  21.578  1.00 17.28 ? 12  GLY C N   1 
ATOM   2297 C CA  . GLY C 1 12  ? 44.657  10.983  22.328  1.00 16.07 ? 12  GLY C CA  1 
ATOM   2298 C C   . GLY C 1 12  ? 44.577  9.468   22.565  1.00 15.78 ? 12  GLY C C   1 
ATOM   2299 O O   . GLY C 1 12  ? 43.829  8.799   21.862  1.00 16.04 ? 12  GLY C O   1 
ATOM   2300 N N   . PRO C 1 13  ? 45.306  8.935   23.570  1.00 15.80 ? 13  PRO C N   1 
ATOM   2301 C CA  . PRO C 1 13  ? 45.407  7.520   23.932  1.00 15.69 ? 13  PRO C CA  1 
ATOM   2302 C C   . PRO C 1 13  ? 44.235  6.935   24.763  1.00 17.75 ? 13  PRO C C   1 
ATOM   2303 O O   . PRO C 1 13  ? 44.159  5.693   24.970  1.00 17.88 ? 13  PRO C O   1 
ATOM   2304 C CB  . PRO C 1 13  ? 46.641  7.511   24.811  1.00 15.20 ? 13  PRO C CB  1 
ATOM   2305 C CG  . PRO C 1 13  ? 46.601  8.758   25.505  1.00 16.54 ? 13  PRO C CG  1 
ATOM   2306 C CD  . PRO C 1 13  ? 46.096  9.758   24.504  1.00 15.42 ? 13  PRO C CD  1 
ATOM   2307 N N   . VAL C 1 14  ? 43.346  7.784   25.268  1.00 17.60 ? 14  VAL C N   1 
ATOM   2308 C CA  . VAL C 1 14  ? 42.283  7.313   26.194  1.00 19.70 ? 14  VAL C CA  1 
ATOM   2309 C C   . VAL C 1 14  ? 41.308  6.331   25.536  1.00 20.53 ? 14  VAL C C   1 
ATOM   2310 O O   . VAL C 1 14  ? 40.764  6.594   24.486  1.00 21.80 ? 14  VAL C O   1 
ATOM   2311 C CB  . VAL C 1 14  ? 41.571  8.527   26.874  1.00 19.55 ? 14  VAL C CB  1 
ATOM   2312 C CG1 . VAL C 1 14  ? 40.507  8.084   27.851  1.00 19.46 ? 14  VAL C CG1 1 
ATOM   2313 C CG2 . VAL C 1 14  ? 42.594  9.357   27.636  1.00 19.44 ? 14  VAL C CG2 1 
ATOM   2314 N N   . GLN C 1 15  ? 41.106  5.174   26.144  1.00 21.35 ? 15  GLN C N   1 
ATOM   2315 C CA  . GLN C 1 15  ? 40.117  4.225   25.660  1.00 21.64 ? 15  GLN C CA  1 
ATOM   2316 C C   . GLN C 1 15  ? 39.702  3.123   26.653  1.00 20.18 ? 15  GLN C C   1 
ATOM   2317 O O   . GLN C 1 15  ? 40.460  2.697   27.501  1.00 20.27 ? 15  GLN C O   1 
ATOM   2318 C CB  . GLN C 1 15  ? 40.594  3.596   24.382  1.00 22.55 ? 15  GLN C CB  1 
ATOM   2319 C CG  . GLN C 1 15  ? 42.054  3.279   24.349  1.00 25.72 ? 15  GLN C CG  1 
ATOM   2320 C CD  . GLN C 1 15  ? 42.249  1.902   23.813  1.00 30.10 ? 15  GLN C CD  1 
ATOM   2321 O OE1 . GLN C 1 15  ? 41.489  0.997   24.156  1.00 33.09 ? 15  GLN C OE1 1 
ATOM   2322 N NE2 . GLN C 1 15  ? 43.235  1.725   22.977  1.00 29.02 ? 15  GLN C NE2 1 
ATOM   2323 N N   . GLY C 1 16  ? 38.466  2.668   26.538  1.00 19.74 ? 16  GLY C N   1 
ATOM   2324 C CA  . GLY C 1 16  ? 37.833  1.809   27.560  1.00 19.46 ? 16  GLY C CA  1 
ATOM   2325 C C   . GLY C 1 16  ? 36.511  1.189   27.119  1.00 17.99 ? 16  GLY C C   1 
ATOM   2326 O O   . GLY C 1 16  ? 35.957  1.617   26.142  1.00 18.47 ? 16  GLY C O   1 
ATOM   2327 N N   . ILE C 1 17  ? 36.066  0.138   27.809  1.00 16.14 ? 17  ILE C N   1 
ATOM   2328 C CA  . ILE C 1 17  ? 34.742  -0.470  27.650  1.00 14.55 ? 17  ILE C CA  1 
ATOM   2329 C C   . ILE C 1 17  ? 33.920  -0.253  28.940  1.00 14.03 ? 17  ILE C C   1 
ATOM   2330 O O   . ILE C 1 17  ? 34.405  -0.512  30.022  1.00 14.62 ? 17  ILE C O   1 
ATOM   2331 C CB  . ILE C 1 17  ? 34.949  -1.978  27.362  1.00 15.45 ? 17  ILE C CB  1 
ATOM   2332 C CG1 . ILE C 1 17  ? 35.676  -2.115  25.988  1.00 14.12 ? 17  ILE C CG1 1 
ATOM   2333 C CG2 . ILE C 1 17  ? 33.643  -2.781  27.482  1.00 15.60 ? 17  ILE C CG2 1 
ATOM   2334 C CD1 . ILE C 1 17  ? 35.895  -3.562  25.461  1.00 15.44 ? 17  ILE C CD1 1 
ATOM   2335 N N   . ILE C 1 18  ? 32.702  0.270   28.855  1.00 12.63 ? 18  ILE C N   1 
ATOM   2336 C CA  . ILE C 1 18  ? 31.955  0.689   30.035  1.00 10.71 ? 18  ILE C CA  1 
ATOM   2337 C C   . ILE C 1 18  ? 30.651  -0.073  29.846  1.00 11.27 ? 18  ILE C C   1 
ATOM   2338 O O   . ILE C 1 18  ? 30.022  0.065   28.837  1.00 9.58  ? 18  ILE C O   1 
ATOM   2339 C CB  . ILE C 1 18  ? 31.697  2.293   30.065  1.00 11.74 ? 18  ILE C CB  1 
ATOM   2340 C CG1 . ILE C 1 18  ? 32.945  3.066   30.405  1.00 10.49 ? 18  ILE C CG1 1 
ATOM   2341 C CG2 . ILE C 1 18  ? 30.799  2.670   31.186  1.00 10.01 ? 18  ILE C CG2 1 
ATOM   2342 C CD1 . ILE C 1 18  ? 33.585  2.654   31.804  1.00 10.17 ? 18  ILE C CD1 1 
ATOM   2343 N N   . ASN C 1 19  ? 30.294  -0.965  30.759  1.00 12.01 ? 19  ASN C N   1 
ATOM   2344 C CA  . ASN C 1 19  ? 28.994  -1.607  30.722  1.00 12.70 ? 19  ASN C CA  1 
ATOM   2345 C C   . ASN C 1 19  ? 27.973  -0.902  31.584  1.00 11.66 ? 19  ASN C C   1 
ATOM   2346 O O   . ASN C 1 19  ? 28.341  -0.396  32.592  1.00 9.83  ? 19  ASN C O   1 
ATOM   2347 C CB  . ASN C 1 19  ? 29.140  -3.079  31.116  1.00 10.76 ? 19  ASN C CB  1 
ATOM   2348 C CG  . ASN C 1 19  ? 30.296  -3.680  30.423  1.00 13.44 ? 19  ASN C CG  1 
ATOM   2349 O OD1 . ASN C 1 19  ? 31.412  -3.696  30.936  1.00 18.58 ? 19  ASN C OD1 1 
ATOM   2350 N ND2 . ASN C 1 19  ? 30.092  -4.034  29.203  1.00 10.21 ? 19  ASN C ND2 1 
ATOM   2351 N N   . PHE C 1 20  ? 26.689  -0.916  31.163  1.00 11.88 ? 20  PHE C N   1 
ATOM   2352 C CA  . PHE C 1 20  ? 25.548  -0.593  32.017  1.00 10.09 ? 20  PHE C CA  1 
ATOM   2353 C C   . PHE C 1 20  ? 24.594  -1.763  32.154  1.00 11.52 ? 20  PHE C C   1 
ATOM   2354 O O   . PHE C 1 20  ? 24.354  -2.420  31.194  1.00 10.81 ? 20  PHE C O   1 
ATOM   2355 C CB  . PHE C 1 20  ? 24.778  0.520   31.413  1.00 9.69  ? 20  PHE C CB  1 
ATOM   2356 C CG  . PHE C 1 20  ? 25.637  1.662   31.023  1.00 3.21  ? 20  PHE C CG  1 
ATOM   2357 C CD1 . PHE C 1 20  ? 26.478  1.554   29.950  1.00 3.93  ? 20  PHE C CD1 1 
ATOM   2358 C CD2 . PHE C 1 20  ? 25.618  2.830   31.705  1.00 4.40  ? 20  PHE C CD2 1 
ATOM   2359 C CE1 . PHE C 1 20  ? 27.292  2.644   29.518  1.00 7.02  ? 20  PHE C CE1 1 
ATOM   2360 C CE2 . PHE C 1 20  ? 26.435  3.904   31.273  1.00 4.11  ? 20  PHE C CE2 1 
ATOM   2361 C CZ  . PHE C 1 20  ? 27.265  3.784   30.203  1.00 3.31  ? 20  PHE C CZ  1 
ATOM   2362 N N   . GLU C 1 21  ? 24.010  -1.927  33.328  1.00 12.97 ? 21  GLU C N   1 
ATOM   2363 C CA  . GLU C 1 21  ? 22.950  -2.853  33.537  1.00 15.14 ? 21  GLU C CA  1 
ATOM   2364 C C   . GLU C 1 21  ? 21.819  -2.298  34.418  1.00 15.66 ? 21  GLU C C   1 
ATOM   2365 O O   . GLU C 1 21  ? 22.068  -1.616  35.414  1.00 13.68 ? 21  GLU C O   1 
ATOM   2366 C CB  . GLU C 1 21  ? 23.472  -4.131  34.156  1.00 17.58 ? 21  GLU C CB  1 
ATOM   2367 C CG  . GLU C 1 21  ? 22.345  -5.131  34.355  1.00 22.51 ? 21  GLU C CG  1 
ATOM   2368 C CD  . GLU C 1 21  ? 22.868  -6.476  34.609  1.00 29.42 ? 21  GLU C CD  1 
ATOM   2369 O OE1 . GLU C 1 21  ? 23.791  -6.550  35.430  1.00 35.14 ? 21  GLU C OE1 1 
ATOM   2370 O OE2 . GLU C 1 21  ? 22.369  -7.445  34.004  1.00 29.25 ? 21  GLU C OE2 1 
ATOM   2371 N N   . GLN C 1 22  ? 20.573  -2.600  34.037  1.00 15.31 ? 22  GLN C N   1 
ATOM   2372 C CA  . GLN C 1 22  ? 19.396  -2.167  34.808  1.00 15.62 ? 22  GLN C CA  1 
ATOM   2373 C C   . GLN C 1 22  ? 18.434  -3.321  34.900  1.00 16.85 ? 22  GLN C C   1 
ATOM   2374 O O   . GLN C 1 22  ? 17.702  -3.521  33.971  1.00 16.91 ? 22  GLN C O   1 
ATOM   2375 C CB  . GLN C 1 22  ? 18.699  -1.003  34.105  1.00 14.64 ? 22  GLN C CB  1 
ATOM   2376 C CG  . GLN C 1 22  ? 17.815  -0.268  35.070  1.00 12.59 ? 22  GLN C CG  1 
ATOM   2377 C CD  . GLN C 1 22  ? 17.251  0.984   34.501  1.00 9.91  ? 22  GLN C CD  1 
ATOM   2378 O OE1 . GLN C 1 22  ? 17.161  1.160   33.313  1.00 9.93  ? 22  GLN C OE1 1 
ATOM   2379 N NE2 . GLN C 1 22  ? 16.788  1.837   35.370  1.00 11.02 ? 22  GLN C NE2 1 
ATOM   2380 N N   . LYS C 1 23  ? 18.435  -4.058  36.009  1.00 18.62 ? 23  LYS C N   1 
ATOM   2381 C CA  . LYS C 1 23  ? 17.529  -5.197  36.174  1.00 22.38 ? 23  LYS C CA  1 
ATOM   2382 C C   . LYS C 1 23  ? 16.033  -4.849  36.379  1.00 22.39 ? 23  LYS C C   1 
ATOM   2383 O O   . LYS C 1 23  ? 15.192  -5.694  36.131  1.00 23.79 ? 23  LYS C O   1 
ATOM   2384 C CB  . LYS C 1 23  ? 17.993  -6.120  37.305  1.00 23.08 ? 23  LYS C CB  1 
ATOM   2385 C CG  . LYS C 1 23  ? 19.334  -6.852  37.055  1.00 22.63 ? 23  LYS C CG  1 
ATOM   2386 C CD  . LYS C 1 23  ? 19.942  -7.311  38.405  1.00 26.84 ? 23  LYS C CD  1 
ATOM   2387 C CE  . LYS C 1 23  ? 20.884  -8.565  38.303  1.00 29.44 ? 23  LYS C CE  1 
ATOM   2388 N NZ  . LYS C 1 23  ? 20.652  -9.503  39.488  1.00 34.33 ? 23  LYS C NZ  1 
ATOM   2389 N N   . GLU C 1 24  ? 15.696  -3.631  36.818  1.00 20.68 ? 24  GLU C N   1 
ATOM   2390 C CA  . GLU C 1 24  ? 14.293  -3.249  36.914  1.00 19.15 ? 24  GLU C CA  1 
ATOM   2391 C C   . GLU C 1 24  ? 14.223  -1.884  36.360  1.00 17.20 ? 24  GLU C C   1 
ATOM   2392 O O   . GLU C 1 24  ? 15.071  -1.105  36.700  1.00 15.25 ? 24  GLU C O   1 
ATOM   2393 C CB  . GLU C 1 24  ? 13.845  -3.220  38.383  1.00 20.73 ? 24  GLU C CB  1 
ATOM   2394 C CG  . GLU C 1 24  ? 13.842  -4.622  39.044  1.00 25.85 ? 24  GLU C CG  1 
ATOM   2395 C CD  . GLU C 1 24  ? 14.034  -4.522  40.544  1.00 32.60 ? 24  GLU C CD  1 
ATOM   2396 O OE1 . GLU C 1 24  ? 14.223  -3.361  40.990  1.00 36.80 ? 24  GLU C OE1 1 
ATOM   2397 O OE2 . GLU C 1 24  ? 13.992  -5.578  41.254  1.00 35.28 ? 24  GLU C OE2 1 
ATOM   2398 N N   . SER C 1 25  ? 13.187  -1.606  35.571  1.00 13.44 ? 25  SER C N   1 
ATOM   2399 C CA  . SER C 1 25  ? 13.074  -0.429  34.765  1.00 12.36 ? 25  SER C CA  1 
ATOM   2400 C C   . SER C 1 25  ? 12.954  0.768   35.632  1.00 12.54 ? 25  SER C C   1 
ATOM   2401 O O   . SER C 1 25  ? 13.285  1.916   35.230  1.00 11.69 ? 25  SER C O   1 
ATOM   2402 C CB  . SER C 1 25  ? 11.860  -0.551  33.858  1.00 12.24 ? 25  SER C CB  1 
ATOM   2403 O OG  . SER C 1 25  ? 10.616  -0.714  34.557  1.00 11.94 ? 25  SER C OG  1 
ATOM   2404 N N   . ASN C 1 26  ? 12.507  0.525   36.874  1.00 12.86 ? 26  ASN C N   1 
ATOM   2405 C CA  . ASN C 1 26  ? 12.402  1.636   37.839  1.00 14.24 ? 26  ASN C CA  1 
ATOM   2406 C C   . ASN C 1 26  ? 13.477  1.643   38.925  1.00 14.88 ? 26  ASN C C   1 
ATOM   2407 O O   . ASN C 1 26  ? 13.345  2.398   39.932  1.00 16.68 ? 26  ASN C O   1 
ATOM   2408 C CB  . ASN C 1 26  ? 10.984  1.856   38.408  1.00 13.18 ? 26  ASN C CB  1 
ATOM   2409 C CG  . ASN C 1 26  ? 10.534  0.761   39.302  1.00 15.00 ? 26  ASN C CG  1 
ATOM   2410 O OD1 . ASN C 1 26  ? 10.965  -0.411  39.175  1.00 11.21 ? 26  ASN C OD1 1 
ATOM   2411 N ND2 . ASN C 1 26  ? 9.650   1.118   40.241  1.00 10.48 ? 26  ASN C ND2 1 
ATOM   2412 N N   . GLY C 1 27  ? 14.524  0.835   38.673  1.00 13.19 ? 27  GLY C N   1 
ATOM   2413 C CA  . GLY C 1 27  ? 15.673  0.638   39.543  1.00 12.43 ? 27  GLY C CA  1 
ATOM   2414 C C   . GLY C 1 27  ? 16.925  1.351   39.047  1.00 11.71 ? 27  GLY C C   1 
ATOM   2415 O O   . GLY C 1 27  ? 16.913  2.056   38.016  1.00 10.68 ? 27  GLY C O   1 
ATOM   2416 N N   . PRO C 1 28  ? 17.982  1.326   39.864  1.00 13.20 ? 28  PRO C N   1 
ATOM   2417 C CA  . PRO C 1 28  ? 19.338  1.808   39.445  1.00 12.82 ? 28  PRO C CA  1 
ATOM   2418 C C   . PRO C 1 28  ? 20.099  1.086   38.337  1.00 13.41 ? 28  PRO C C   1 
ATOM   2419 O O   . PRO C 1 28  ? 19.918  -0.138  38.088  1.00 11.76 ? 28  PRO C O   1 
ATOM   2420 C CB  . PRO C 1 28  ? 20.172  1.691   40.731  1.00 13.88 ? 28  PRO C CB  1 
ATOM   2421 C CG  . PRO C 1 28  ? 19.391  0.731   41.609  1.00 12.83 ? 28  PRO C CG  1 
ATOM   2422 C CD  . PRO C 1 28  ? 17.940  1.056   41.306  1.00 11.10 ? 28  PRO C CD  1 
ATOM   2423 N N   . VAL C 1 29  ? 21.003  1.850   37.706  1.00 11.95 ? 29  VAL C N   1 
ATOM   2424 C CA  . VAL C 1 29  ? 21.802  1.342   36.591  1.00 12.23 ? 29  VAL C CA  1 
ATOM   2425 C C   . VAL C 1 29  ? 23.196  1.038   37.163  1.00 13.31 ? 29  VAL C C   1 
ATOM   2426 O O   . VAL C 1 29  ? 23.793  1.883   37.734  1.00 10.21 ? 29  VAL C O   1 
ATOM   2427 C CB  . VAL C 1 29  ? 21.888  2.428   35.453  1.00 12.42 ? 29  VAL C CB  1 
ATOM   2428 C CG1 . VAL C 1 29  ? 22.403  1.803   34.153  1.00 11.69 ? 29  VAL C CG1 1 
ATOM   2429 C CG2 . VAL C 1 29  ? 20.559  2.934   35.151  1.00 13.69 ? 29  VAL C CG2 1 
ATOM   2430 N N   . LYS C 1 30  ? 23.695  -0.200  37.079  1.00 15.17 ? 30  LYS C N   1 
ATOM   2431 C CA  . LYS C 1 30  ? 25.078  -0.456  37.463  1.00 16.28 ? 30  LYS C CA  1 
ATOM   2432 C C   . LYS C 1 30  ? 25.915  -0.064  36.264  1.00 16.52 ? 30  LYS C C   1 
ATOM   2433 O O   . LYS C 1 30  ? 25.557  -0.396  35.148  1.00 18.04 ? 30  LYS C O   1 
ATOM   2434 C CB  . LYS C 1 30  ? 25.269  -1.948  37.828  1.00 17.22 ? 30  LYS C CB  1 
ATOM   2435 C CG  . LYS C 1 30  ? 24.230  -2.423  38.801  1.00 20.58 ? 30  LYS C CG  1 
ATOM   2436 C CD  . LYS C 1 30  ? 24.587  -3.823  39.415  1.00 22.15 ? 30  LYS C CD  1 
ATOM   2437 C CE  . LYS C 1 30  ? 23.350  -4.802  39.402  1.00 30.45 ? 30  LYS C CE  1 
ATOM   2438 N NZ  . LYS C 1 30  ? 22.923  -5.260  37.989  1.00 25.85 ? 30  LYS C NZ  1 
ATOM   2439 N N   . VAL C 1 31  ? 27.021  0.660   36.493  1.00 15.51 ? 31  VAL C N   1 
ATOM   2440 C CA  . VAL C 1 31  ? 27.924  1.140   35.477  1.00 12.91 ? 31  VAL C CA  1 
ATOM   2441 C C   . VAL C 1 31  ? 29.294  0.569   35.809  1.00 13.43 ? 31  VAL C C   1 
ATOM   2442 O O   . VAL C 1 31  ? 29.773  0.704   36.914  1.00 13.30 ? 31  VAL C O   1 
ATOM   2443 C CB  . VAL C 1 31  ? 27.990  2.697   35.530  1.00 13.28 ? 31  VAL C CB  1 
ATOM   2444 C CG1 . VAL C 1 31  ? 28.955  3.193   34.537  1.00 10.92 ? 31  VAL C CG1 1 
ATOM   2445 C CG2 . VAL C 1 31  ? 26.618  3.270   35.333  1.00 8.30  ? 31  VAL C CG2 1 
ATOM   2446 N N   . TRP C 1 32  ? 29.905  -0.162  34.914  1.00 13.77 ? 32  TRP C N   1 
ATOM   2447 C CA  . TRP C 1 32  ? 31.195  -0.709  35.296  1.00 14.12 ? 32  TRP C CA  1 
ATOM   2448 C C   . TRP C 1 32  ? 32.081  -0.969  34.098  1.00 13.88 ? 32  TRP C C   1 
ATOM   2449 O O   . TRP C 1 32  ? 31.574  -1.076  32.996  1.00 12.27 ? 32  TRP C O   1 
ATOM   2450 C CB  . TRP C 1 32  ? 30.985  -1.968  36.079  1.00 15.40 ? 32  TRP C CB  1 
ATOM   2451 C CG  . TRP C 1 32  ? 30.677  -3.152  35.269  1.00 16.62 ? 32  TRP C CG  1 
ATOM   2452 C CD1 . TRP C 1 32  ? 31.541  -4.075  34.830  1.00 18.66 ? 32  TRP C CD1 1 
ATOM   2453 C CD2 . TRP C 1 32  ? 29.379  -3.590  34.880  1.00 20.57 ? 32  TRP C CD2 1 
ATOM   2454 N NE1 . TRP C 1 32  ? 30.889  -5.054  34.142  1.00 19.78 ? 32  TRP C NE1 1 
ATOM   2455 C CE2 . TRP C 1 32  ? 29.546  -4.796  34.175  1.00 20.83 ? 32  TRP C CE2 1 
ATOM   2456 C CE3 . TRP C 1 32  ? 28.085  -3.090  35.075  1.00 19.56 ? 32  TRP C CE3 1 
ATOM   2457 C CZ2 . TRP C 1 32  ? 28.468  -5.498  33.618  1.00 22.30 ? 32  TRP C CZ2 1 
ATOM   2458 C CZ3 . TRP C 1 32  ? 27.009  -3.785  34.517  1.00 20.86 ? 32  TRP C CZ3 1 
ATOM   2459 C CH2 . TRP C 1 32  ? 27.207  -4.984  33.811  1.00 18.86 ? 32  TRP C CH2 1 
ATOM   2460 N N   . GLY C 1 33  ? 33.399  -1.074  34.303  1.00 13.54 ? 33  GLY C N   1 
ATOM   2461 C CA  . GLY C 1 33  ? 34.312  -1.340  33.204  1.00 13.45 ? 33  GLY C CA  1 
ATOM   2462 C C   . GLY C 1 33  ? 35.713  -0.938  33.533  1.00 13.72 ? 33  GLY C C   1 
ATOM   2463 O O   . GLY C 1 33  ? 36.097  -1.031  34.654  1.00 13.21 ? 33  GLY C O   1 
ATOM   2464 N N   . SER C 1 34  ? 36.476  -0.479  32.538  1.00 16.60 ? 34  SER C N   1 
ATOM   2465 C CA  . SER C 1 34  ? 37.892  -0.100  32.687  1.00 17.09 ? 34  SER C CA  1 
ATOM   2466 C C   . SER C 1 34  ? 38.230  0.871   31.557  1.00 18.33 ? 34  SER C C   1 
ATOM   2467 O O   . SER C 1 34  ? 37.778  0.703   30.420  1.00 18.02 ? 34  SER C O   1 
ATOM   2468 C CB  . SER C 1 34  ? 38.749  -1.352  32.566  1.00 20.09 ? 34  SER C CB  1 
ATOM   2469 O OG  . SER C 1 34  ? 40.129  -1.022  32.509  1.00 24.04 ? 34  SER C OG  1 
ATOM   2470 N N   . ILE C 1 35  ? 39.048  1.859   31.853  1.00 18.23 ? 35  ILE C N   1 
ATOM   2471 C CA  . ILE C 1 35  ? 39.426  2.922   30.887  1.00 18.26 ? 35  ILE C CA  1 
ATOM   2472 C C   . ILE C 1 35  ? 40.940  3.143   31.033  1.00 20.16 ? 35  ILE C C   1 
ATOM   2473 O O   . ILE C 1 35  ? 41.382  3.576   32.120  1.00 21.83 ? 35  ILE C O   1 
ATOM   2474 C CB  . ILE C 1 35  ? 38.773  4.239   31.227  1.00 18.76 ? 35  ILE C CB  1 
ATOM   2475 C CG1 . ILE C 1 35  ? 37.233  4.161   31.321  1.00 19.53 ? 35  ILE C CG1 1 
ATOM   2476 C CG2 . ILE C 1 35  ? 39.136  5.341   30.227  1.00 14.99 ? 35  ILE C CG2 1 
ATOM   2477 C CD1 . ILE C 1 35  ? 36.657  5.605   31.648  1.00 17.88 ? 35  ILE C CD1 1 
ATOM   2478 N N   . LYS C 1 36  ? 41.737  2.853   29.997  1.00 19.94 ? 36  LYS C N   1 
ATOM   2479 C CA  . LYS C 1 36  ? 43.190  3.069   30.066  1.00 19.61 ? 36  LYS C CA  1 
ATOM   2480 C C   . LYS C 1 36  ? 43.636  4.389   29.404  1.00 19.29 ? 36  LYS C C   1 
ATOM   2481 O O   . LYS C 1 36  ? 42.828  5.075   28.781  1.00 19.84 ? 36  LYS C O   1 
ATOM   2482 C CB  . LYS C 1 36  ? 43.974  1.856   29.504  1.00 20.36 ? 36  LYS C CB  1 
ATOM   2483 C CG  . LYS C 1 36  ? 43.618  1.334   28.096  1.00 20.79 ? 36  LYS C CG  1 
ATOM   2484 C CD  . LYS C 1 36  ? 44.880  1.156   27.155  1.00 24.67 ? 36  LYS C CD  1 
ATOM   2485 C CE  . LYS C 1 36  ? 44.757  -0.089  26.195  1.00 24.43 ? 36  LYS C CE  1 
ATOM   2486 N NZ  . LYS C 1 36  ? 45.243  -1.367  26.807  1.00 26.42 ? 36  LYS C NZ  1 
ATOM   2487 N N   . GLY C 1 37  ? 44.912  4.776   29.562  1.00 18.55 ? 37  GLY C N   1 
ATOM   2488 C CA  . GLY C 1 37  ? 45.446  5.862   28.736  1.00 15.49 ? 37  GLY C CA  1 
ATOM   2489 C C   . GLY C 1 37  ? 45.192  7.145   29.439  1.00 16.38 ? 37  GLY C C   1 
ATOM   2490 O O   . GLY C 1 37  ? 45.353  8.198   28.880  1.00 16.41 ? 37  GLY C O   1 
ATOM   2491 N N   . LEU C 1 38  ? 44.813  7.071   30.700  1.00 17.54 ? 38  LEU C N   1 
ATOM   2492 C CA  . LEU C 1 38  ? 44.494  8.281   31.495  1.00 18.50 ? 38  LEU C CA  1 
ATOM   2493 C C   . LEU C 1 38  ? 45.635  8.819   32.419  1.00 19.60 ? 38  LEU C C   1 
ATOM   2494 O O   . LEU C 1 38  ? 46.345  8.028   33.021  1.00 19.46 ? 38  LEU C O   1 
ATOM   2495 C CB  . LEU C 1 38  ? 43.364  7.873   32.413  1.00 17.59 ? 38  LEU C CB  1 
ATOM   2496 C CG  . LEU C 1 38  ? 41.888  8.204   32.338  1.00 18.26 ? 38  LEU C CG  1 
ATOM   2497 C CD1 . LEU C 1 38  ? 41.405  9.033   31.180  1.00 15.32 ? 38  LEU C CD1 1 
ATOM   2498 C CD2 . LEU C 1 38  ? 41.160  6.833   32.568  1.00 17.72 ? 38  LEU C CD2 1 
ATOM   2499 N N   . THR C 1 39  ? 45.778  10.131  32.571  1.00 20.93 ? 39  THR C N   1 
ATOM   2500 C CA  . THR C 1 39  ? 46.693  10.619  33.589  1.00 24.15 ? 39  THR C CA  1 
ATOM   2501 C C   . THR C 1 39  ? 46.103  10.190  34.962  1.00 25.50 ? 39  THR C C   1 
ATOM   2502 O O   . THR C 1 39  ? 44.879  10.320  35.191  1.00 25.45 ? 39  THR C O   1 
ATOM   2503 C CB  . THR C 1 39  ? 46.787  12.131  33.645  1.00 24.10 ? 39  THR C CB  1 
ATOM   2504 O OG1 . THR C 1 39  ? 45.542  12.606  34.159  1.00 29.92 ? 39  THR C OG1 1 
ATOM   2505 C CG2 . THR C 1 39  ? 47.065  12.784  32.295  1.00 21.61 ? 39  THR C CG2 1 
ATOM   2506 N N   . GLU C 1 40  ? 46.976  9.728   35.870  1.00 26.31 ? 40  GLU C N   1 
ATOM   2507 C CA  . GLU C 1 40  ? 46.649  9.342   37.236  1.00 25.76 ? 40  GLU C CA  1 
ATOM   2508 C C   . GLU C 1 40  ? 45.800  10.412  37.948  1.00 25.98 ? 40  GLU C C   1 
ATOM   2509 O O   . GLU C 1 40  ? 46.066  11.634  37.808  1.00 24.93 ? 40  GLU C O   1 
ATOM   2510 C CB  . GLU C 1 40  ? 47.943  9.115   37.986  1.00 27.09 ? 40  GLU C CB  1 
ATOM   2511 C CG  . GLU C 1 40  ? 47.758  8.393   39.307  1.00 30.53 ? 40  GLU C CG  1 
ATOM   2512 C CD  . GLU C 1 40  ? 48.999  8.443   40.165  1.00 35.43 ? 40  GLU C CD  1 
ATOM   2513 O OE1 . GLU C 1 40  ? 50.051  8.867   39.634  1.00 34.53 ? 40  GLU C OE1 1 
ATOM   2514 O OE2 . GLU C 1 40  ? 48.905  8.068   41.360  1.00 36.88 ? 40  GLU C OE2 1 
ATOM   2515 N N   . GLY C 1 41  ? 44.743  9.967   38.642  1.00 23.98 ? 41  GLY C N   1 
ATOM   2516 C CA  . GLY C 1 41  ? 43.824  10.910  39.260  1.00 24.32 ? 41  GLY C CA  1 
ATOM   2517 C C   . GLY C 1 41  ? 42.409  10.890  38.706  1.00 24.58 ? 41  GLY C C   1 
ATOM   2518 O O   . GLY C 1 41  ? 41.976  9.919   38.064  1.00 23.91 ? 41  GLY C O   1 
ATOM   2519 N N   . LEU C 1 42  ? 41.723  12.021  38.869  1.00 24.16 ? 42  LEU C N   1 
ATOM   2520 C CA  . LEU C 1 42  ? 40.284  12.051  38.799  1.00 24.83 ? 42  LEU C CA  1 
ATOM   2521 C C   . LEU C 1 42  ? 39.856  12.798  37.546  1.00 24.47 ? 42  LEU C C   1 
ATOM   2522 O O   . LEU C 1 42  ? 40.358  13.917  37.280  1.00 25.50 ? 42  LEU C O   1 
ATOM   2523 C CB  . LEU C 1 42  ? 39.785  12.764  40.048  1.00 24.90 ? 42  LEU C CB  1 
ATOM   2524 C CG  . LEU C 1 42  ? 38.641  12.363  40.956  1.00 25.24 ? 42  LEU C CG  1 
ATOM   2525 C CD1 . LEU C 1 42  ? 38.757  10.973  41.491  1.00 26.56 ? 42  LEU C CD1 1 
ATOM   2526 C CD2 . LEU C 1 42  ? 38.641  13.357  42.089  1.00 27.53 ? 42  LEU C CD2 1 
ATOM   2527 N N   . HIS C 1 43  ? 38.918  12.198  36.788  1.00 22.08 ? 43  HIS C N   1 
ATOM   2528 C CA  . HIS C 1 43  ? 38.425  12.753  35.525  1.00 20.13 ? 43  HIS C CA  1 
ATOM   2529 C C   . HIS C 1 43  ? 36.904  12.745  35.458  1.00 19.19 ? 43  HIS C C   1 
ATOM   2530 O O   . HIS C 1 43  ? 36.298  11.728  35.727  1.00 19.01 ? 43  HIS C O   1 
ATOM   2531 C CB  . HIS C 1 43  ? 38.969  11.906  34.362  1.00 19.88 ? 43  HIS C CB  1 
ATOM   2532 C CG  . HIS C 1 43  ? 40.462  11.908  34.264  1.00 17.89 ? 43  HIS C CG  1 
ATOM   2533 N ND1 . HIS C 1 43  ? 41.182  13.028  33.890  1.00 17.34 ? 43  HIS C ND1 1 
ATOM   2534 C CD2 . HIS C 1 43  ? 41.367  10.936  34.514  1.00 12.12 ? 43  HIS C CD2 1 
ATOM   2535 C CE1 . HIS C 1 43  ? 42.471  12.731  33.911  1.00 17.86 ? 43  HIS C CE1 1 
ATOM   2536 N NE2 . HIS C 1 43  ? 42.605  11.465  34.289  1.00 15.67 ? 43  HIS C NE2 1 
ATOM   2537 N N   . GLY C 1 44  ? 36.310  13.860  35.038  1.00 16.78 ? 44  GLY C N   1 
ATOM   2538 C CA  . GLY C 1 44  ? 34.875  14.008  34.941  1.00 16.00 ? 44  GLY C CA  1 
ATOM   2539 C C   . GLY C 1 44  ? 34.264  12.952  34.040  1.00 15.08 ? 44  GLY C C   1 
ATOM   2540 O O   . GLY C 1 44  ? 34.848  12.598  33.031  1.00 14.84 ? 44  GLY C O   1 
ATOM   2541 N N   . PHE C 1 45  ? 33.066  12.474  34.361  1.00 14.03 ? 45  PHE C N   1 
ATOM   2542 C CA  . PHE C 1 45  ? 32.524  11.293  33.686  1.00 12.52 ? 45  PHE C CA  1 
ATOM   2543 C C   . PHE C 1 45  ? 31.061  11.628  33.404  1.00 14.40 ? 45  PHE C C   1 
ATOM   2544 O O   . PHE C 1 45  ? 30.306  11.812  34.340  1.00 15.51 ? 45  PHE C O   1 
ATOM   2545 C CB  . PHE C 1 45  ? 32.629  10.159  34.654  1.00 11.25 ? 45  PHE C CB  1 
ATOM   2546 C CG  . PHE C 1 45  ? 32.496  8.798   34.035  1.00 8.63  ? 45  PHE C CG  1 
ATOM   2547 C CD1 . PHE C 1 45  ? 33.097  8.486   32.802  1.00 7.81  ? 45  PHE C CD1 1 
ATOM   2548 C CD2 . PHE C 1 45  ? 31.817  7.813   34.707  1.00 9.23  ? 45  PHE C CD2 1 
ATOM   2549 C CE1 . PHE C 1 45  ? 32.975  7.233   32.238  1.00 10.96 ? 45  PHE C CE1 1 
ATOM   2550 C CE2 . PHE C 1 45  ? 31.709  6.514   34.152  1.00 3.33  ? 45  PHE C CE2 1 
ATOM   2551 C CZ  . PHE C 1 45  ? 32.308  6.221   32.932  1.00 5.74  ? 45  PHE C CZ  1 
ATOM   2552 N N   . HIS C 1 46  ? 30.648  11.800  32.148  1.00 14.05 ? 46  HIS C N   1 
ATOM   2553 C CA  . HIS C 1 46  ? 29.267  12.238  31.898  1.00 15.89 ? 46  HIS C CA  1 
ATOM   2554 C C   . HIS C 1 46  ? 28.594  11.588  30.707  1.00 14.87 ? 46  HIS C C   1 
ATOM   2555 O O   . HIS C 1 46  ? 29.283  11.171  29.768  1.00 16.77 ? 46  HIS C O   1 
ATOM   2556 C CB  . HIS C 1 46  ? 29.259  13.732  31.636  1.00 16.29 ? 46  HIS C CB  1 
ATOM   2557 C CG  . HIS C 1 46  ? 29.466  14.554  32.868  1.00 19.58 ? 46  HIS C CG  1 
ATOM   2558 N ND1 . HIS C 1 46  ? 30.721  14.904  33.327  1.00 21.44 ? 46  HIS C ND1 1 
ATOM   2559 C CD2 . HIS C 1 46  ? 28.575  15.138  33.714  1.00 20.62 ? 46  HIS C CD2 1 
ATOM   2560 C CE1 . HIS C 1 46  ? 30.595  15.671  34.402  1.00 22.67 ? 46  HIS C CE1 1 
ATOM   2561 N NE2 . HIS C 1 46  ? 29.306  15.818  34.667  1.00 22.23 ? 46  HIS C NE2 1 
ATOM   2562 N N   . VAL C 1 47  ? 27.252  11.580  30.725  1.00 12.35 ? 47  VAL C N   1 
ATOM   2563 C CA  . VAL C 1 47  ? 26.419  11.394  29.544  1.00 9.41  ? 47  VAL C CA  1 
ATOM   2564 C C   . VAL C 1 47  ? 26.125  12.771  29.007  1.00 11.06 ? 47  VAL C C   1 
ATOM   2565 O O   . VAL C 1 47  ? 25.873  13.674  29.795  1.00 10.54 ? 47  VAL C O   1 
ATOM   2566 C CB  . VAL C 1 47  ? 25.168  10.570  29.843  1.00 9.06  ? 47  VAL C CB  1 
ATOM   2567 C CG1 . VAL C 1 47  ? 24.444  10.181  28.578  1.00 11.05 ? 47  VAL C CG1 1 
ATOM   2568 C CG2 . VAL C 1 47  ? 25.589  9.246   30.501  1.00 6.44  ? 47  VAL C CG2 1 
ATOM   2569 N N   . HIS C 1 48  ? 26.330  12.934  27.677  1.00 12.19 ? 48  HIS C N   1 
ATOM   2570 C CA  . HIS C 1 48  ? 26.100  14.192  26.951  1.00 10.36 ? 48  HIS C CA  1 
ATOM   2571 C C   . HIS C 1 48  ? 24.930  13.911  26.097  1.00 10.90 ? 48  HIS C C   1 
ATOM   2572 O O   . HIS C 1 48  ? 24.572  12.748  25.887  1.00 8.22  ? 48  HIS C O   1 
ATOM   2573 C CB  . HIS C 1 48  ? 27.329  14.579  26.128  1.00 11.84 ? 48  HIS C CB  1 
ATOM   2574 C CG  . HIS C 1 48  ? 28.437  15.117  26.976  1.00 9.45  ? 48  HIS C CG  1 
ATOM   2575 N ND1 . HIS C 1 48  ? 28.753  16.465  27.031  1.00 8.95  ? 48  HIS C ND1 1 
ATOM   2576 C CD2 . HIS C 1 48  ? 29.195  14.511  27.906  1.00 5.70  ? 48  HIS C CD2 1 
ATOM   2577 C CE1 . HIS C 1 48  ? 29.728  16.638  27.903  1.00 5.82  ? 48  HIS C CE1 1 
ATOM   2578 N NE2 . HIS C 1 48  ? 29.992  15.470  28.472  1.00 12.09 ? 48  HIS C NE2 1 
ATOM   2579 N N   . GLU C 1 49  ? 24.305  14.953  25.601  1.00 9.05  ? 49  GLU C N   1 
ATOM   2580 C CA  . GLU C 1 49  ? 23.026  14.770  24.983  1.00 10.81 ? 49  GLU C CA  1 
ATOM   2581 C C   . GLU C 1 49  ? 22.934  13.857  23.726  1.00 10.60 ? 49  GLU C C   1 
ATOM   2582 O O   . GLU C 1 49  ? 21.930  13.163  23.498  1.00 9.53  ? 49  GLU C O   1 
ATOM   2583 C CB  . GLU C 1 49  ? 22.501  16.158  24.602  1.00 9.80  ? 49  GLU C CB  1 
ATOM   2584 C CG  . GLU C 1 49  ? 21.080  15.982  24.373  1.00 13.15 ? 49  GLU C CG  1 
ATOM   2585 C CD  . GLU C 1 49  ? 20.293  17.218  24.356  1.00 17.19 ? 49  GLU C CD  1 
ATOM   2586 O OE1 . GLU C 1 49  ? 20.813  18.310  24.698  1.00 18.93 ? 49  GLU C OE1 1 
ATOM   2587 O OE2 . GLU C 1 49  ? 19.127  17.070  23.985  1.00 16.62 ? 49  GLU C OE2 1 
ATOM   2588 N N   . PHE C 1 50  ? 23.949  13.901  22.867  1.00 12.40 ? 50  PHE C N   1 
ATOM   2589 C CA  . PHE C 1 50  ? 23.791  13.439  21.491  1.00 12.13 ? 50  PHE C CA  1 
ATOM   2590 C C   . PHE C 1 50  ? 24.677  12.261  21.174  1.00 13.44 ? 50  PHE C C   1 
ATOM   2591 O O   . PHE C 1 50  ? 25.847  12.254  21.561  1.00 15.57 ? 50  PHE C O   1 
ATOM   2592 C CB  . PHE C 1 50  ? 24.042  14.570  20.541  1.00 11.17 ? 50  PHE C CB  1 
ATOM   2593 C CG  . PHE C 1 50  ? 23.071  15.692  20.679  1.00 10.56 ? 50  PHE C CG  1 
ATOM   2594 C CD1 . PHE C 1 50  ? 21.691  15.471  20.563  1.00 6.21  ? 50  PHE C CD1 1 
ATOM   2595 C CD2 . PHE C 1 50  ? 23.520  16.964  20.864  1.00 7.91  ? 50  PHE C CD2 1 
ATOM   2596 C CE1 . PHE C 1 50  ? 20.730  16.539  20.685  1.00 14.53 ? 50  PHE C CE1 1 
ATOM   2597 C CE2 . PHE C 1 50  ? 22.609  17.999  20.998  1.00 9.43  ? 50  PHE C CE2 1 
ATOM   2598 C CZ  . PHE C 1 50  ? 21.221  17.805  20.883  1.00 9.17  ? 50  PHE C CZ  1 
ATOM   2599 N N   . GLY C 1 51  ? 24.128  11.250  20.533  1.00 13.88 ? 51  GLY C N   1 
ATOM   2600 C CA  . GLY C 1 51  ? 24.943  10.100  20.153  1.00 16.62 ? 51  GLY C CA  1 
ATOM   2601 C C   . GLY C 1 51  ? 25.698  10.491  18.899  1.00 18.49 ? 51  GLY C C   1 
ATOM   2602 O O   . GLY C 1 51  ? 25.879  9.675   17.989  1.00 20.33 ? 51  GLY C O   1 
ATOM   2603 N N   . ASP C 1 52  ? 26.125  11.760  18.819  1.00 20.14 ? 52  ASP C N   1 
ATOM   2604 C CA  . ASP C 1 52  ? 26.711  12.254  17.585  1.00 20.09 ? 52  ASP C CA  1 
ATOM   2605 C C   . ASP C 1 52  ? 28.216  12.401  17.731  1.00 21.36 ? 52  ASP C C   1 
ATOM   2606 O O   . ASP C 1 52  ? 28.689  13.288  18.407  1.00 22.12 ? 52  ASP C O   1 
ATOM   2607 C CB  . ASP C 1 52  ? 25.985  13.528  17.165  1.00 20.47 ? 52  ASP C CB  1 
ATOM   2608 C CG  . ASP C 1 52  ? 26.546  14.185  15.917  1.00 20.03 ? 52  ASP C CG  1 
ATOM   2609 O OD1 . ASP C 1 52  ? 27.461  13.650  15.271  1.00 16.99 ? 52  ASP C OD1 1 
ATOM   2610 O OD2 . ASP C 1 52  ? 26.041  15.275  15.573  1.00 22.12 ? 52  ASP C OD2 1 
ATOM   2611 N N   . ASN C 1 53  ? 28.969  11.523  17.073  1.00 23.04 ? 53  ASN C N   1 
ATOM   2612 C CA  . ASN C 1 53  ? 30.393  11.737  17.043  1.00 24.45 ? 53  ASN C CA  1 
ATOM   2613 C C   . ASN C 1 53  ? 31.028  12.104  15.694  1.00 24.69 ? 53  ASN C C   1 
ATOM   2614 O O   . ASN C 1 53  ? 32.197  11.847  15.475  1.00 25.08 ? 53  ASN C O   1 
ATOM   2615 C CB  . ASN C 1 53  ? 31.114  10.659  17.866  1.00 25.44 ? 53  ASN C CB  1 
ATOM   2616 C CG  . ASN C 1 53  ? 30.848  10.828  19.435  1.00 27.87 ? 53  ASN C CG  1 
ATOM   2617 O OD1 . ASN C 1 53  ? 30.683  9.834   20.172  1.00 20.62 ? 53  ASN C OD1 1 
ATOM   2618 N ND2 . ASN C 1 53  ? 30.803  12.116  19.917  1.00 21.97 ? 53  ASN C ND2 1 
ATOM   2619 N N   . THR C 1 54  ? 30.261  12.772  14.833  1.00 24.68 ? 54  THR C N   1 
ATOM   2620 C CA  . THR C 1 54  ? 30.688  13.074  13.468  1.00 25.25 ? 54  THR C CA  1 
ATOM   2621 C C   . THR C 1 54  ? 31.942  13.927  13.481  1.00 26.39 ? 54  THR C C   1 
ATOM   2622 O O   . THR C 1 54  ? 32.858  13.671  12.690  1.00 27.80 ? 54  THR C O   1 
ATOM   2623 C CB  . THR C 1 54  ? 29.629  13.817  12.689  1.00 23.98 ? 54  THR C CB  1 
ATOM   2624 O OG1 . THR C 1 54  ? 29.356  15.040  13.342  1.00 24.52 ? 54  THR C OG1 1 
ATOM   2625 C CG2 . THR C 1 54  ? 28.377  13.036  12.621  1.00 25.45 ? 54  THR C CG2 1 
ATOM   2626 N N   . ALA C 1 55  ? 32.010  14.898  14.404  1.00 26.92 ? 55  ALA C N   1 
ATOM   2627 C CA  . ALA C 1 55  ? 33.233  15.672  14.646  1.00 27.38 ? 55  ALA C CA  1 
ATOM   2628 C C   . ALA C 1 55  ? 33.943  15.337  16.002  1.00 27.97 ? 55  ALA C C   1 
ATOM   2629 O O   . ALA C 1 55  ? 34.244  16.242  16.776  1.00 28.78 ? 55  ALA C O   1 
ATOM   2630 C CB  . ALA C 1 55  ? 32.897  17.157  14.564  1.00 27.78 ? 55  ALA C CB  1 
ATOM   2631 N N   . GLY C 1 56  ? 34.219  14.053  16.282  1.00 27.42 ? 56  GLY C N   1 
ATOM   2632 C CA  . GLY C 1 56  ? 34.732  13.629  17.606  1.00 26.93 ? 56  GLY C CA  1 
ATOM   2633 C C   . GLY C 1 56  ? 33.783  13.917  18.782  1.00 26.48 ? 56  GLY C C   1 
ATOM   2634 O O   . GLY C 1 56  ? 32.573  14.036  18.579  1.00 27.38 ? 56  GLY C O   1 
ATOM   2635 N N   . CYS C 1 57  ? 34.314  14.029  20.004  1.00 25.27 ? 57  CYS C N   1 
ATOM   2636 C CA  . CYS C 1 57  ? 33.462  14.181  21.196  1.00 23.57 ? 57  CYS C CA  1 
ATOM   2637 C C   . CYS C 1 57  ? 32.759  15.529  21.331  1.00 23.40 ? 57  CYS C C   1 
ATOM   2638 O O   . CYS C 1 57  ? 31.884  15.690  22.166  1.00 22.63 ? 57  CYS C O   1 
ATOM   2639 C CB  . CYS C 1 57  ? 34.241  13.916  22.466  1.00 22.99 ? 57  CYS C CB  1 
ATOM   2640 S SG  . CYS C 1 57  ? 34.995  12.359  22.491  1.00 20.43 ? 57  CYS C SG  1 
ATOM   2641 N N   . THR C 1 58  ? 33.146  16.494  20.517  1.00 22.95 ? 58  THR C N   1 
ATOM   2642 C CA  . THR C 1 58  ? 32.581  17.841  20.632  1.00 23.28 ? 58  THR C CA  1 
ATOM   2643 C C   . THR C 1 58  ? 31.139  17.913  20.184  1.00 22.93 ? 58  THR C C   1 
ATOM   2644 O O   . THR C 1 58  ? 30.427  18.842  20.559  1.00 24.59 ? 58  THR C O   1 
ATOM   2645 C CB  . THR C 1 58  ? 33.416  18.798  19.737  1.00 24.33 ? 58  THR C CB  1 
ATOM   2646 O OG1 . THR C 1 58  ? 34.817  18.571  19.992  1.00 24.99 ? 58  THR C OG1 1 
ATOM   2647 C CG2 . THR C 1 58  ? 33.045  20.283  19.934  1.00 25.16 ? 58  THR C CG2 1 
ATOM   2648 N N   . SER C 1 59  ? 30.734  16.972  19.322  1.00 22.40 ? 59  SER C N   1 
ATOM   2649 C CA  . SER C 1 59  ? 29.400  16.915  18.715  1.00 21.36 ? 59  SER C CA  1 
ATOM   2650 C C   . SER C 1 59  ? 28.383  16.361  19.663  1.00 19.92 ? 59  SER C C   1 
ATOM   2651 O O   . SER C 1 59  ? 27.205  16.568  19.434  1.00 19.84 ? 59  SER C O   1 
ATOM   2652 C CB  . SER C 1 59  ? 29.379  16.026  17.474  1.00 21.67 ? 59  SER C CB  1 
ATOM   2653 O OG  . SER C 1 59  ? 30.677  15.805  17.020  1.00 23.82 ? 59  SER C OG  1 
ATOM   2654 N N   . ALA C 1 60  ? 28.829  15.676  20.724  1.00 20.57 ? 60  ALA C N   1 
ATOM   2655 C CA  . ALA C 1 60  ? 27.940  15.122  21.781  1.00 19.56 ? 60  ALA C CA  1 
ATOM   2656 C C   . ALA C 1 60  ? 27.175  16.181  22.514  1.00 19.48 ? 60  ALA C C   1 
ATOM   2657 O O   . ALA C 1 60  ? 26.289  15.856  23.313  1.00 19.06 ? 60  ALA C O   1 
ATOM   2658 C CB  . ALA C 1 60  ? 28.687  14.263  22.771  1.00 20.21 ? 60  ALA C CB  1 
ATOM   2659 N N   . GLY C 1 61  ? 27.442  17.454  22.235  1.00 18.87 ? 61  GLY C N   1 
ATOM   2660 C CA  . GLY C 1 61  ? 26.565  18.479  22.797  1.00 18.16 ? 61  GLY C CA  1 
ATOM   2661 C C   . GLY C 1 61  ? 26.721  18.579  24.290  1.00 17.00 ? 61  GLY C C   1 
ATOM   2662 O O   . GLY C 1 61  ? 27.758  18.230  24.767  1.00 16.02 ? 61  GLY C O   1 
ATOM   2663 N N   . PRO C 1 62  ? 25.717  19.113  25.045  1.00 18.11 ? 62  PRO C N   1 
ATOM   2664 C CA  . PRO C 1 62  ? 26.123  19.346  26.421  1.00 18.20 ? 62  PRO C CA  1 
ATOM   2665 C C   . PRO C 1 62  ? 25.869  18.119  27.319  1.00 18.88 ? 62  PRO C C   1 
ATOM   2666 O O   . PRO C 1 62  ? 25.591  17.046  26.786  1.00 17.73 ? 62  PRO C O   1 
ATOM   2667 C CB  . PRO C 1 62  ? 25.298  20.574  26.834  1.00 18.10 ? 62  PRO C CB  1 
ATOM   2668 C CG  . PRO C 1 62  ? 24.174  20.703  25.779  1.00 18.31 ? 62  PRO C CG  1 
ATOM   2669 C CD  . PRO C 1 62  ? 24.310  19.502  24.858  1.00 17.94 ? 62  PRO C CD  1 
ATOM   2670 N N   . HIS C 1 63  ? 26.045  18.260  28.630  1.00 18.23 ? 63  HIS C N   1 
ATOM   2671 C CA  . HIS C 1 63  ? 25.521  17.287  29.591  1.00 19.73 ? 63  HIS C CA  1 
ATOM   2672 C C   . HIS C 1 63  ? 24.079  17.003  29.208  1.00 20.01 ? 63  HIS C C   1 
ATOM   2673 O O   . HIS C 1 63  ? 23.305  17.883  28.771  1.00 19.49 ? 63  HIS C O   1 
ATOM   2674 C CB  . HIS C 1 63  ? 25.627  17.747  31.080  1.00 20.56 ? 63  HIS C CB  1 
ATOM   2675 C CG  . HIS C 1 63  ? 27.038  17.996  31.576  1.00 22.27 ? 63  HIS C CG  1 
ATOM   2676 N ND1 . HIS C 1 63  ? 27.376  19.107  32.326  1.00 18.49 ? 63  HIS C ND1 1 
ATOM   2677 C CD2 . HIS C 1 63  ? 28.185  17.278  31.434  1.00 22.32 ? 63  HIS C CD2 1 
ATOM   2678 C CE1 . HIS C 1 63  ? 28.666  19.062  32.620  1.00 22.74 ? 63  HIS C CE1 1 
ATOM   2679 N NE2 . HIS C 1 63  ? 29.185  17.965  32.086  1.00 23.10 ? 63  HIS C NE2 1 
ATOM   2680 N N   . PHE C 1 64  ? 23.726  15.738  29.360  1.00 20.21 ? 64  PHE C N   1 
ATOM   2681 C CA  . PHE C 1 64  ? 22.335  15.316  29.199  1.00 19.83 ? 64  PHE C CA  1 
ATOM   2682 C C   . PHE C 1 64  ? 21.510  15.718  30.454  1.00 21.54 ? 64  PHE C C   1 
ATOM   2683 O O   . PHE C 1 64  ? 21.911  15.468  31.601  1.00 21.90 ? 64  PHE C O   1 
ATOM   2684 C CB  . PHE C 1 64  ? 22.317  13.789  29.035  1.00 16.92 ? 64  PHE C CB  1 
ATOM   2685 C CG  . PHE C 1 64  ? 20.944  13.213  28.937  1.00 15.53 ? 64  PHE C CG  1 
ATOM   2686 C CD1 . PHE C 1 64  ? 20.001  13.806  28.146  1.00 11.14 ? 64  PHE C CD1 1 
ATOM   2687 C CD2 . PHE C 1 64  ? 20.620  12.021  29.600  1.00 7.93  ? 64  PHE C CD2 1 
ATOM   2688 C CE1 . PHE C 1 64  ? 18.710  13.241  28.029  1.00 12.80 ? 64  PHE C CE1 1 
ATOM   2689 C CE2 . PHE C 1 64  ? 19.325  11.500  29.509  1.00 5.95  ? 64  PHE C CE2 1 
ATOM   2690 C CZ  . PHE C 1 64  ? 18.389  12.058  28.720  1.00 10.63 ? 64  PHE C CZ  1 
ATOM   2691 N N   . ASN C 1 65  ? 20.322  16.234  30.237  1.00 24.78 ? 65  ASN C N   1 
ATOM   2692 C CA  . ASN C 1 65  ? 19.642  16.966  31.252  1.00 29.08 ? 65  ASN C CA  1 
ATOM   2693 C C   . ASN C 1 65  ? 18.245  17.145  30.654  1.00 31.75 ? 65  ASN C C   1 
ATOM   2694 O O   . ASN C 1 65  ? 17.936  18.220  30.118  1.00 33.32 ? 65  ASN C O   1 
ATOM   2695 C CB  . ASN C 1 65  ? 20.400  18.288  31.284  1.00 30.46 ? 65  ASN C CB  1 
ATOM   2696 C CG  . ASN C 1 65  ? 20.094  19.136  32.450  1.00 32.66 ? 65  ASN C CG  1 
ATOM   2697 O OD1 . ASN C 1 65  ? 19.890  18.644  33.562  1.00 34.76 ? 65  ASN C OD1 1 
ATOM   2698 N ND2 . ASN C 1 65  ? 20.143  20.454  32.226  1.00 33.72 ? 65  ASN C ND2 1 
ATOM   2699 N N   . PRO C 1 66  ? 17.411  16.081  30.632  1.00 33.42 ? 66  PRO C N   1 
ATOM   2700 C CA  . PRO C 1 66  ? 16.154  16.230  29.911  1.00 35.08 ? 66  PRO C CA  1 
ATOM   2701 C C   . PRO C 1 66  ? 15.218  17.331  30.423  1.00 37.60 ? 66  PRO C C   1 
ATOM   2702 O O   . PRO C 1 66  ? 14.687  18.115  29.592  1.00 39.02 ? 66  PRO C O   1 
ATOM   2703 C CB  . PRO C 1 66  ? 15.506  14.870  30.086  1.00 34.32 ? 66  PRO C CB  1 
ATOM   2704 C CG  . PRO C 1 66  ? 16.122  14.339  31.304  1.00 34.38 ? 66  PRO C CG  1 
ATOM   2705 C CD  . PRO C 1 66  ? 17.527  14.734  31.187  1.00 33.36 ? 66  PRO C CD  1 
ATOM   2706 N N   . LEU C 1 67  ? 15.005  17.409  31.747  1.00 39.22 ? 67  LEU C N   1 
ATOM   2707 C CA  . LEU C 1 67  ? 13.873  18.200  32.263  1.00 41.11 ? 67  LEU C CA  1 
ATOM   2708 C C   . LEU C 1 67  ? 14.038  19.704  32.106  1.00 42.05 ? 67  LEU C C   1 
ATOM   2709 O O   . LEU C 1 67  ? 13.484  20.270  31.147  1.00 42.84 ? 67  LEU C O   1 
ATOM   2710 C CB  . LEU C 1 67  ? 13.446  17.792  33.686  1.00 41.32 ? 67  LEU C CB  1 
ATOM   2711 C CG  . LEU C 1 67  ? 12.757  16.415  33.781  1.00 43.13 ? 67  LEU C CG  1 
ATOM   2712 C CD1 . LEU C 1 67  ? 11.860  16.062  32.572  1.00 40.20 ? 67  LEU C CD1 1 
ATOM   2713 C CD2 . LEU C 1 67  ? 13.757  15.258  34.046  1.00 45.63 ? 67  LEU C CD2 1 
ATOM   2714 N N   . ARG C 1 79  ? 21.960  17.540  40.250  1.00 32.94 ? 79  ARG C N   1 
ATOM   2715 C CA  . ARG C 1 79  ? 22.997  17.415  39.212  1.00 32.68 ? 79  ARG C CA  1 
ATOM   2716 C C   . ARG C 1 79  ? 22.291  17.093  37.930  1.00 31.58 ? 79  ARG C C   1 
ATOM   2717 O O   . ARG C 1 79  ? 21.118  16.719  37.952  1.00 32.55 ? 79  ARG C O   1 
ATOM   2718 C CB  . ARG C 1 79  ? 23.980  16.252  39.504  1.00 32.88 ? 79  ARG C CB  1 
ATOM   2719 C CG  . ARG C 1 79  ? 23.349  14.966  40.102  1.00 34.02 ? 79  ARG C CG  1 
ATOM   2720 C CD  . ARG C 1 79  ? 22.601  14.006  39.128  1.00 36.82 ? 79  ARG C CD  1 
ATOM   2721 N NE  . ARG C 1 79  ? 22.729  12.636  39.623  1.00 34.87 ? 79  ARG C NE  1 
ATOM   2722 C CZ  . ARG C 1 79  ? 23.095  11.564  38.898  1.00 36.90 ? 79  ARG C CZ  1 
ATOM   2723 N NH1 . ARG C 1 79  ? 23.281  11.628  37.575  1.00 29.85 ? 79  ARG C NH1 1 
ATOM   2724 N NH2 . ARG C 1 79  ? 23.199  10.382  39.511  1.00 32.19 ? 79  ARG C NH2 1 
ATOM   2725 N N   . HIS C 1 80  ? 23.024  17.158  36.830  1.00 29.40 ? 80  HIS C N   1 
ATOM   2726 C CA  . HIS C 1 80  ? 22.487  16.803  35.551  1.00 27.52 ? 80  HIS C CA  1 
ATOM   2727 C C   . HIS C 1 80  ? 22.175  15.305  35.481  1.00 26.19 ? 80  HIS C C   1 
ATOM   2728 O O   . HIS C 1 80  ? 22.787  14.481  36.194  1.00 25.56 ? 80  HIS C O   1 
ATOM   2729 C CB  . HIS C 1 80  ? 23.416  17.355  34.480  1.00 27.88 ? 80  HIS C CB  1 
ATOM   2730 C CG  . HIS C 1 80  ? 23.647  18.835  34.641  1.00 31.80 ? 80  HIS C CG  1 
ATOM   2731 N ND1 . HIS C 1 80  ? 24.654  19.530  33.995  1.00 36.06 ? 80  HIS C ND1 1 
ATOM   2732 C CD2 . HIS C 1 80  ? 23.000  19.748  35.413  1.00 33.88 ? 80  HIS C CD2 1 
ATOM   2733 C CE1 . HIS C 1 80  ? 24.602  20.805  34.347  1.00 37.96 ? 80  HIS C CE1 1 
ATOM   2734 N NE2 . HIS C 1 80  ? 23.612  20.962  35.213  1.00 37.33 ? 80  HIS C NE2 1 
ATOM   2735 N N   . VAL C 1 81  ? 21.182  14.935  34.684  1.00 24.59 ? 81  VAL C N   1 
ATOM   2736 C CA  . VAL C 1 81  ? 20.801  13.507  34.624  1.00 24.09 ? 81  VAL C CA  1 
ATOM   2737 C C   . VAL C 1 81  ? 22.027  12.682  34.240  1.00 23.88 ? 81  VAL C C   1 
ATOM   2738 O O   . VAL C 1 81  ? 22.264  11.625  34.818  1.00 24.09 ? 81  VAL C O   1 
ATOM   2739 C CB  . VAL C 1 81  ? 19.583  13.240  33.681  1.00 23.97 ? 81  VAL C CB  1 
ATOM   2740 C CG1 . VAL C 1 81  ? 19.460  11.747  33.269  1.00 22.33 ? 81  VAL C CG1 1 
ATOM   2741 C CG2 . VAL C 1 81  ? 18.294  13.779  34.331  1.00 24.36 ? 81  VAL C CG2 1 
ATOM   2742 N N   . GLY C 1 82  ? 22.820  13.225  33.311  1.00 23.17 ? 82  GLY C N   1 
ATOM   2743 C CA  . GLY C 1 82  ? 24.084  12.643  32.862  1.00 21.30 ? 82  GLY C CA  1 
ATOM   2744 C C   . GLY C 1 82  ? 25.235  12.412  33.841  1.00 19.40 ? 82  GLY C C   1 
ATOM   2745 O O   . GLY C 1 82  ? 26.086  11.522  33.607  1.00 17.75 ? 82  GLY C O   1 
ATOM   2746 N N   . ASP C 1 83  ? 25.256  13.194  34.920  1.00 17.44 ? 83  ASP C N   1 
ATOM   2747 C CA  . ASP C 1 83  ? 26.366  13.256  35.925  1.00 17.07 ? 83  ASP C CA  1 
ATOM   2748 C C   . ASP C 1 83  ? 26.705  11.973  36.689  1.00 16.33 ? 83  ASP C C   1 
ATOM   2749 O O   . ASP C 1 83  ? 26.039  11.623  37.648  1.00 16.94 ? 83  ASP C O   1 
ATOM   2750 C CB  . ASP C 1 83  ? 26.065  14.342  36.943  1.00 17.07 ? 83  ASP C CB  1 
ATOM   2751 C CG  . ASP C 1 83  ? 27.318  14.893  37.630  1.00 18.45 ? 83  ASP C CG  1 
ATOM   2752 O OD1 . ASP C 1 83  ? 28.272  14.122  37.893  0.50 12.57 ? 83  ASP C OD1 1 
ATOM   2753 O OD2 . ASP C 1 83  ? 27.314  16.132  37.909  0.50 17.32 ? 83  ASP C OD2 1 
ATOM   2754 N N   . LEU C 1 84  ? 27.776  11.307  36.284  1.00 15.04 ? 84  LEU C N   1 
ATOM   2755 C CA  . LEU C 1 84  ? 28.194  10.056  36.896  1.00 13.99 ? 84  LEU C CA  1 
ATOM   2756 C C   . LEU C 1 84  ? 29.511  10.210  37.694  1.00 14.21 ? 84  LEU C C   1 
ATOM   2757 O O   . LEU C 1 84  ? 30.295  9.247   37.804  1.00 14.15 ? 84  LEU C O   1 
ATOM   2758 C CB  . LEU C 1 84  ? 28.388  9.017   35.809  1.00 13.30 ? 84  LEU C CB  1 
ATOM   2759 C CG  . LEU C 1 84  ? 27.247  8.629   34.881  1.00 15.60 ? 84  LEU C CG  1 
ATOM   2760 C CD1 . LEU C 1 84  ? 27.790  7.586   33.944  1.00 14.02 ? 84  LEU C CD1 1 
ATOM   2761 C CD2 . LEU C 1 84  ? 26.098  8.018   35.712  1.00 15.12 ? 84  LEU C CD2 1 
ATOM   2762 N N   . GLY C 1 85  ? 29.760  11.425  38.190  1.00 13.85 ? 85  GLY C N   1 
ATOM   2763 C CA  . GLY C 1 85  ? 30.922  11.722  39.015  1.00 13.35 ? 85  GLY C CA  1 
ATOM   2764 C C   . GLY C 1 85  ? 32.193  11.828  38.200  1.00 13.46 ? 85  GLY C C   1 
ATOM   2765 O O   . GLY C 1 85  ? 32.194  12.398  37.089  1.00 14.58 ? 85  GLY C O   1 
ATOM   2766 N N   . ASN C 1 86  ? 33.260  11.272  38.744  1.00 14.74 ? 86  ASN C N   1 
ATOM   2767 C CA  . ASN C 1 86  ? 34.576  11.289  38.147  1.00 15.25 ? 86  ASN C CA  1 
ATOM   2768 C C   . ASN C 1 86  ? 34.956  9.836   38.011  1.00 17.25 ? 86  ASN C C   1 
ATOM   2769 O O   . ASN C 1 86  ? 34.342  8.966   38.648  1.00 17.61 ? 86  ASN C O   1 
ATOM   2770 C CB  . ASN C 1 86  ? 35.617  11.973  39.044  1.00 15.23 ? 86  ASN C CB  1 
ATOM   2771 C CG  . ASN C 1 86  ? 35.367  13.506  39.235  1.00 17.50 ? 86  ASN C CG  1 
ATOM   2772 O OD1 . ASN C 1 86  ? 35.478  14.305  38.311  1.00 16.80 ? 86  ASN C OD1 1 
ATOM   2773 N ND2 . ASN C 1 86  ? 35.031  13.885  40.448  1.00 18.24 ? 86  ASN C ND2 1 
ATOM   2774 N N   . VAL C 1 87  ? 35.941  9.525   37.165  1.00 18.00 ? 87  VAL C N   1 
ATOM   2775 C CA  . VAL C 1 87  ? 36.606  8.225   37.371  1.00 19.53 ? 87  VAL C CA  1 
ATOM   2776 C C   . VAL C 1 87  ? 38.036  8.499   37.849  1.00 20.15 ? 87  VAL C C   1 
ATOM   2777 O O   . VAL C 1 87  ? 38.528  9.657   37.773  1.00 20.63 ? 87  VAL C O   1 
ATOM   2778 C CB  . VAL C 1 87  ? 36.466  7.201   36.197  1.00 17.96 ? 87  VAL C CB  1 
ATOM   2779 C CG1 . VAL C 1 87  ? 34.994  6.900   35.987  1.00 18.76 ? 87  VAL C CG1 1 
ATOM   2780 C CG2 . VAL C 1 87  ? 37.107  7.743   34.907  1.00 20.44 ? 87  VAL C CG2 1 
ATOM   2781 N N   . THR C 1 88  ? 38.654  7.468   38.412  1.00 21.80 ? 88  THR C N   1 
ATOM   2782 C CA  . THR C 1 88  ? 39.972  7.618   39.058  1.00 22.05 ? 88  THR C CA  1 
ATOM   2783 C C   . THR C 1 88  ? 40.954  6.681   38.425  1.00 22.84 ? 88  THR C C   1 
ATOM   2784 O O   . THR C 1 88  ? 40.922  5.453   38.652  1.00 22.28 ? 88  THR C O   1 
ATOM   2785 C CB  . THR C 1 88  ? 39.924  7.254   40.554  1.00 21.58 ? 88  THR C CB  1 
ATOM   2786 O OG1 . THR C 1 88  ? 38.881  8.003   41.191  1.00 21.79 ? 88  THR C OG1 1 
ATOM   2787 C CG2 . THR C 1 88  ? 41.258  7.525   41.231  1.00 20.21 ? 88  THR C CG2 1 
ATOM   2788 N N   . ALA C 1 89  ? 41.852  7.298   37.670  1.00 23.13 ? 89  ALA C N   1 
ATOM   2789 C CA  . ALA C 1 89  ? 42.954  6.615   37.099  1.00 23.54 ? 89  ALA C CA  1 
ATOM   2790 C C   . ALA C 1 89  ? 44.068  6.583   38.147  1.00 24.67 ? 89  ALA C C   1 
ATOM   2791 O O   . ALA C 1 89  ? 44.367  7.602   38.815  1.00 24.79 ? 89  ALA C O   1 
ATOM   2792 C CB  . ALA C 1 89  ? 43.373  7.353   35.914  1.00 23.07 ? 89  ALA C CB  1 
ATOM   2793 N N   . ASP C 1 90  ? 44.649  5.402   38.278  1.00 24.73 ? 90  ASP C N   1 
ATOM   2794 C CA  . ASP C 1 90  ? 45.804  5.107   39.131  1.00 26.02 ? 90  ASP C CA  1 
ATOM   2795 C C   . ASP C 1 90  ? 47.112  5.627   38.477  1.00 26.74 ? 90  ASP C C   1 
ATOM   2796 O O   . ASP C 1 90  ? 47.072  6.262   37.408  1.00 25.75 ? 90  ASP C O   1 
ATOM   2797 C CB  . ASP C 1 90  ? 45.862  3.569   39.358  1.00 24.97 ? 90  ASP C CB  1 
ATOM   2798 C CG  . ASP C 1 90  ? 46.189  2.829   38.107  1.00 25.64 ? 90  ASP C CG  1 
ATOM   2799 O OD1 . ASP C 1 90  ? 46.577  3.577   37.185  1.00 22.14 ? 90  ASP C OD1 1 
ATOM   2800 O OD2 . ASP C 1 90  ? 46.092  1.555   38.016  1.00 15.54 ? 90  ASP C OD2 1 
ATOM   2801 N N   . LYS C 1 91  ? 48.267  5.347   39.104  1.00 28.55 ? 91  LYS C N   1 
ATOM   2802 C CA  . LYS C 1 91  ? 49.606  5.714   38.511  1.00 29.44 ? 91  LYS C CA  1 
ATOM   2803 C C   . LYS C 1 91  ? 49.991  5.063   37.127  1.00 29.62 ? 91  LYS C C   1 
ATOM   2804 O O   . LYS C 1 91  ? 50.739  5.654   36.346  1.00 28.63 ? 91  LYS C O   1 
ATOM   2805 C CB  . LYS C 1 91  ? 50.753  5.544   39.533  1.00 29.17 ? 91  LYS C CB  1 
ATOM   2806 C CG  . LYS C 1 91  ? 50.728  4.276   40.347  1.00 29.24 ? 91  LYS C CG  1 
ATOM   2807 C CD  . LYS C 1 91  ? 51.155  3.022   39.557  1.00 32.45 ? 91  LYS C CD  1 
ATOM   2808 C CE  . LYS C 1 91  ? 51.886  2.028   40.465  1.00 34.91 ? 91  LYS C CE  1 
ATOM   2809 N NZ  . LYS C 1 91  ? 52.610  0.923   39.736  1.00 35.08 ? 91  LYS C NZ  1 
ATOM   2810 N N   . ASP C 1 92  ? 49.504  3.849   36.878  1.00 29.13 ? 92  ASP C N   1 
ATOM   2811 C CA  . ASP C 1 92  ? 49.575  3.213   35.572  1.00 29.38 ? 92  ASP C CA  1 
ATOM   2812 C C   . ASP C 1 92  ? 48.565  3.735   34.485  1.00 29.40 ? 92  ASP C C   1 
ATOM   2813 O O   . ASP C 1 92  ? 48.457  3.145   33.374  1.00 29.38 ? 92  ASP C O   1 
ATOM   2814 C CB  . ASP C 1 92  ? 49.421  1.699   35.766  1.00 29.44 ? 92  ASP C CB  1 
ATOM   2815 C CG  . ASP C 1 92  ? 50.716  1.040   36.297  1.00 33.50 ? 92  ASP C CG  1 
ATOM   2816 O OD1 . ASP C 1 92  ? 51.841  1.608   36.094  1.00 32.69 ? 92  ASP C OD1 1 
ATOM   2817 O OD2 . ASP C 1 92  ? 50.604  -0.059  36.892  1.00 32.22 ? 92  ASP C OD2 1 
ATOM   2818 N N   . GLY C 1 93  ? 47.837  4.810   34.818  1.00 28.93 ? 93  GLY C N   1 
ATOM   2819 C CA  . GLY C 1 93  ? 46.851  5.464   33.922  1.00 28.10 ? 93  GLY C CA  1 
ATOM   2820 C C   . GLY C 1 93  ? 45.483  4.780   33.757  1.00 27.25 ? 93  GLY C C   1 
ATOM   2821 O O   . GLY C 1 93  ? 44.634  5.267   33.031  1.00 26.44 ? 93  GLY C O   1 
ATOM   2822 N N   . VAL C 1 94  ? 45.317  3.639   34.428  1.00 25.73 ? 94  VAL C N   1 
ATOM   2823 C CA  . VAL C 1 94  ? 44.155  2.779   34.375  1.00 25.37 ? 94  VAL C CA  1 
ATOM   2824 C C   . VAL C 1 94  ? 43.071  3.170   35.389  1.00 25.86 ? 94  VAL C C   1 
ATOM   2825 O O   . VAL C 1 94  ? 43.395  3.419   36.559  1.00 26.94 ? 94  VAL C O   1 
ATOM   2826 C CB  . VAL C 1 94  ? 44.607  1.352   34.688  1.00 24.19 ? 94  VAL C CB  1 
ATOM   2827 C CG1 . VAL C 1 94  ? 43.470  0.380   34.590  1.00 24.02 ? 94  VAL C CG1 1 
ATOM   2828 C CG2 . VAL C 1 94  ? 45.661  0.949   33.757  1.00 24.66 ? 94  VAL C CG2 1 
ATOM   2829 N N   . ALA C 1 95  ? 41.798  3.222   34.945  1.00 25.62 ? 95  ALA C N   1 
ATOM   2830 C CA  . ALA C 1 95  ? 40.646  3.551   35.815  1.00 24.87 ? 95  ALA C CA  1 
ATOM   2831 C C   . ALA C 1 95  ? 39.728  2.388   35.778  1.00 24.74 ? 95  ALA C C   1 
ATOM   2832 O O   . ALA C 1 95  ? 39.214  2.061   34.722  1.00 25.04 ? 95  ALA C O   1 
ATOM   2833 C CB  . ALA C 1 95  ? 39.897  4.797   35.366  1.00 24.30 ? 95  ALA C CB  1 
ATOM   2834 N N   . ASP C 1 96  ? 39.538  1.740   36.922  1.00 24.24 ? 96  ASP C N   1 
ATOM   2835 C CA  . ASP C 1 96  ? 38.534  0.698   37.022  1.00 24.60 ? 96  ASP C CA  1 
ATOM   2836 C C   . ASP C 1 96  ? 37.226  1.342   37.509  1.00 23.10 ? 96  ASP C C   1 
ATOM   2837 O O   . ASP C 1 96  ? 37.261  2.224   38.382  1.00 23.02 ? 96  ASP C O   1 
ATOM   2838 C CB  . ASP C 1 96  ? 39.037  -0.423  37.925  1.00 25.85 ? 96  ASP C CB  1 
ATOM   2839 C CG  . ASP C 1 96  ? 40.307  -1.075  37.365  1.00 31.07 ? 96  ASP C CG  1 
ATOM   2840 O OD1 . ASP C 1 96  ? 41.461  -0.604  37.708  1.00 33.84 ? 96  ASP C OD1 1 
ATOM   2841 O OD2 . ASP C 1 96  ? 40.140  -2.024  36.535  1.00 34.39 ? 96  ASP C OD2 1 
ATOM   2842 N N   . VAL C 1 97  ? 36.091  0.974   36.898  1.00 19.82 ? 97  VAL C N   1 
ATOM   2843 C CA  . VAL C 1 97  ? 34.855  1.722   37.182  1.00 16.37 ? 97  VAL C CA  1 
ATOM   2844 C C   . VAL C 1 97  ? 33.912  0.762   37.836  1.00 16.42 ? 97  VAL C C   1 
ATOM   2845 O O   . VAL C 1 97  ? 33.761  -0.360  37.363  1.00 15.31 ? 97  VAL C O   1 
ATOM   2846 C CB  . VAL C 1 97  ? 34.287  2.347   35.898  1.00 16.40 ? 97  VAL C CB  1 
ATOM   2847 C CG1 . VAL C 1 97  ? 33.028  3.160   36.163  1.00 16.13 ? 97  VAL C CG1 1 
ATOM   2848 C CG2 . VAL C 1 97  ? 35.331  3.218   35.286  1.00 8.36  ? 97  VAL C CG2 1 
ATOM   2849 N N   . SER C 1 98  ? 33.377  1.153   38.988  1.00 17.09 ? 98  SER C N   1 
ATOM   2850 C CA  . SER C 1 98  ? 32.215  0.502   39.577  1.00 19.04 ? 98  SER C CA  1 
ATOM   2851 C C   . SER C 1 98  ? 31.388  1.578   40.151  1.00 19.84 ? 98  SER C C   1 
ATOM   2852 O O   . SER C 1 98  ? 31.855  2.286   41.031  1.00 21.69 ? 98  SER C O   1 
ATOM   2853 C CB  . SER C 1 98  ? 32.572  -0.424  40.700  1.00 18.54 ? 98  SER C CB  1 
ATOM   2854 O OG  . SER C 1 98  ? 31.407  -1.176  40.994  1.00 22.19 ? 98  SER C OG  1 
ATOM   2855 N N   . ILE C 1 99  ? 30.183  1.766   39.615  1.00 20.51 ? 99  ILE C N   1 
ATOM   2856 C CA  . ILE C 1 99  ? 29.322  2.922   39.940  1.00 19.77 ? 99  ILE C CA  1 
ATOM   2857 C C   . ILE C 1 99  ? 27.887  2.375   39.855  1.00 19.86 ? 99  ILE C C   1 
ATOM   2858 O O   . ILE C 1 99  ? 27.648  1.358   39.217  1.00 18.42 ? 99  ILE C O   1 
ATOM   2859 C CB  . ILE C 1 99  ? 29.387  4.044   38.885  1.00 19.63 ? 99  ILE C CB  1 
ATOM   2860 C CG1 . ILE C 1 99  ? 30.774  4.654   38.748  1.00 20.04 ? 99  ILE C CG1 1 
ATOM   2861 C CG2 . ILE C 1 99  ? 28.404  5.130   39.182  1.00 20.47 ? 99  ILE C CG2 1 
ATOM   2862 C CD1 . ILE C 1 99  ? 30.851  5.942   37.860  1.00 21.25 ? 99  ILE C CD1 1 
ATOM   2863 N N   . GLU C 1 100 ? 26.945  3.072   40.476  1.00 19.09 ? 100 GLU C N   1 
ATOM   2864 C CA  . GLU C 1 100 ? 25.542  2.669   40.462  1.00 19.81 ? 100 GLU C CA  1 
ATOM   2865 C C   . GLU C 1 100 ? 24.802  3.992   40.602  1.00 19.52 ? 100 GLU C C   1 
ATOM   2866 O O   . GLU C 1 100 ? 25.085  4.758   41.493  1.00 21.12 ? 100 GLU C O   1 
ATOM   2867 C CB  . GLU C 1 100 ? 25.190  1.726   41.600  1.00 20.13 ? 100 GLU C CB  1 
ATOM   2868 C CG  . GLU C 1 100 ? 23.663  1.547   41.715  1.00 20.82 ? 100 GLU C CG  1 
ATOM   2869 C CD  . GLU C 1 100 ? 23.205  0.314   42.457  0.50 20.20 ? 100 GLU C CD  1 
ATOM   2870 O OE1 . GLU C 1 100 ? 23.461  -0.812  41.972  0.50 19.83 ? 100 GLU C OE1 1 
ATOM   2871 O OE2 . GLU C 1 100 ? 22.518  0.494   43.486  0.50 19.52 ? 100 GLU C OE2 1 
ATOM   2872 N N   . ASP C 1 101 ? 23.942  4.283   39.644  1.00 18.46 ? 101 ASP C N   1 
ATOM   2873 C CA  . ASP C 1 101 ? 23.223  5.547   39.580  1.00 16.84 ? 101 ASP C CA  1 
ATOM   2874 C C   . ASP C 1 101 ? 21.707  5.321   39.482  1.00 17.40 ? 101 ASP C C   1 
ATOM   2875 O O   . ASP C 1 101 ? 21.234  4.332   38.901  1.00 17.74 ? 101 ASP C O   1 
ATOM   2876 C CB  . ASP C 1 101 ? 23.627  6.311   38.352  1.00 15.28 ? 101 ASP C CB  1 
ATOM   2877 C CG  . ASP C 1 101 ? 23.058  7.724   38.335  1.00 15.91 ? 101 ASP C CG  1 
ATOM   2878 O OD1 . ASP C 1 101 ? 23.809  8.566   38.749  1.00 13.11 ? 101 ASP C OD1 1 
ATOM   2879 O OD2 . ASP C 1 101 ? 21.914  8.000   37.931  1.00 13.30 ? 101 ASP C OD2 1 
ATOM   2880 N N   . SER C 1 102 ? 20.968  6.318   39.979  1.00 17.21 ? 102 SER C N   1 
ATOM   2881 C CA  . SER C 1 102 ? 19.546  6.225   40.136  1.00 16.82 ? 102 SER C CA  1 
ATOM   2882 C C   . SER C 1 102 ? 18.770  7.242   39.353  1.00 16.30 ? 102 SER C C   1 
ATOM   2883 O O   . SER C 1 102 ? 17.517  7.226   39.412  1.00 15.40 ? 102 SER C O   1 
ATOM   2884 C CB  . SER C 1 102 ? 19.224  6.351   41.618  1.00 18.40 ? 102 SER C CB  1 
ATOM   2885 O OG  . SER C 1 102 ? 19.352  5.043   42.175  1.00 18.54 ? 102 SER C OG  1 
ATOM   2886 N N   . VAL C 1 103 ? 19.500  8.108   38.627  1.00 13.21 ? 103 VAL C N   1 
ATOM   2887 C CA  . VAL C 1 103 ? 18.887  9.150   37.774  1.00 13.62 ? 103 VAL C CA  1 
ATOM   2888 C C   . VAL C 1 103 ? 18.807  8.758   36.244  1.00 12.28 ? 103 VAL C C   1 
ATOM   2889 O O   . VAL C 1 103 ? 17.777  8.919   35.603  1.00 12.01 ? 103 VAL C O   1 
ATOM   2890 C CB  . VAL C 1 103 ? 19.623  10.513  37.992  1.00 13.39 ? 103 VAL C CB  1 
ATOM   2891 C CG1 . VAL C 1 103 ? 18.989  11.652  37.162  1.00 13.10 ? 103 VAL C CG1 1 
ATOM   2892 C CG2 . VAL C 1 103 ? 19.733  10.867  39.524  1.00 10.56 ? 103 VAL C CG2 1 
ATOM   2893 N N   . ILE C 1 104 ? 19.895  8.219   35.707  1.00 12.39 ? 104 ILE C N   1 
ATOM   2894 C CA  . ILE C 1 104 ? 19.954  7.670   34.382  1.00 10.85 ? 104 ILE C CA  1 
ATOM   2895 C C   . ILE C 1 104 ? 19.161  6.386   34.321  1.00 11.86 ? 104 ILE C C   1 
ATOM   2896 O O   . ILE C 1 104 ? 19.122  5.645   35.283  1.00 13.41 ? 104 ILE C O   1 
ATOM   2897 C CB  . ILE C 1 104 ? 21.454  7.236   33.937  1.00 10.35 ? 104 ILE C CB  1 
ATOM   2898 C CG1 . ILE C 1 104 ? 21.999  6.071   34.746  1.00 9.83  ? 104 ILE C CG1 1 
ATOM   2899 C CG2 . ILE C 1 104 ? 22.436  8.460   33.783  1.00 8.31  ? 104 ILE C CG2 1 
ATOM   2900 C CD1 . ILE C 1 104 ? 23.391  5.591   34.335  1.00 8.23  ? 104 ILE C CD1 1 
ATOM   2901 N N   . SER C 1 105 ? 18.635  6.091   33.151  1.00 12.57 ? 105 SER C N   1 
ATOM   2902 C CA  . SER C 1 105 ? 17.976  4.854   32.924  1.00 12.91 ? 105 SER C CA  1 
ATOM   2903 C C   . SER C 1 105 ? 18.379  4.255   31.594  1.00 12.26 ? 105 SER C C   1 
ATOM   2904 O O   . SER C 1 105 ? 18.898  4.944   30.756  1.00 11.41 ? 105 SER C O   1 
ATOM   2905 C CB  . SER C 1 105 ? 16.440  5.019   33.008  1.00 13.14 ? 105 SER C CB  1 
ATOM   2906 O OG  . SER C 1 105 ? 15.981  3.665   33.210  1.00 13.71 ? 105 SER C OG  1 
ATOM   2907 N N   . LEU C 1 106 ? 18.132  2.958   31.404  1.00 11.49 ? 106 LEU C N   1 
ATOM   2908 C CA  . LEU C 1 106 ? 18.234  2.373   30.077  1.00 9.84  ? 106 LEU C CA  1 
ATOM   2909 C C   . LEU C 1 106 ? 16.858  2.323   29.312  1.00 10.50 ? 106 LEU C C   1 
ATOM   2910 O O   . LEU C 1 106 ? 16.795  1.796   28.251  1.00 8.67  ? 106 LEU C O   1 
ATOM   2911 C CB  . LEU C 1 106 ? 18.853  0.970   30.164  1.00 11.27 ? 106 LEU C CB  1 
ATOM   2912 C CG  . LEU C 1 106 ? 20.235  0.618   30.720  1.00 9.19  ? 106 LEU C CG  1 
ATOM   2913 C CD1 . LEU C 1 106 ? 20.603  -0.892  30.482  1.00 4.96  ? 106 LEU C CD1 1 
ATOM   2914 C CD2 . LEU C 1 106 ? 21.254  1.443   30.058  1.00 5.14  ? 106 LEU C CD2 1 
ATOM   2915 N N   . SER C 1 107 ? 15.771  2.894   29.850  1.00 10.52 ? 107 SER C N   1 
ATOM   2916 C CA  . SER C 1 107 ? 14.506  3.060   29.117  1.00 12.07 ? 107 SER C CA  1 
ATOM   2917 C C   . SER C 1 107 ? 13.864  4.354   29.566  1.00 13.43 ? 107 SER C C   1 
ATOM   2918 O O   . SER C 1 107 ? 14.209  4.816   30.633  1.00 16.44 ? 107 SER C O   1 
ATOM   2919 C CB  . SER C 1 107 ? 13.550  1.953   29.471  1.00 11.22 ? 107 SER C CB  1 
ATOM   2920 O OG  . SER C 1 107 ? 13.571  1.775   30.864  1.00 12.42 ? 107 SER C OG  1 
ATOM   2921 N N   . GLY C 1 108 ? 12.965  4.955   28.761  1.00 14.51 ? 108 GLY C N   1 
ATOM   2922 C CA  . GLY C 1 108 ? 12.055  5.996   29.248  1.00 14.76 ? 108 GLY C CA  1 
ATOM   2923 C C   . GLY C 1 108 ? 12.551  7.414   29.124  1.00 16.53 ? 108 GLY C C   1 
ATOM   2924 O O   . GLY C 1 108 ? 13.444  7.631   28.367  1.00 16.95 ? 108 GLY C O   1 
ATOM   2925 N N   . ASP C 1 109 ? 12.029  8.366   29.915  1.00 18.80 ? 109 ASP C N   1 
ATOM   2926 C CA  . ASP C 1 109 ? 12.481  9.793   29.861  1.00 20.93 ? 109 ASP C CA  1 
ATOM   2927 C C   . ASP C 1 109 ? 13.995  9.997   29.919  1.00 19.70 ? 109 ASP C C   1 
ATOM   2928 O O   . ASP C 1 109 ? 14.541  10.815  29.194  1.00 20.16 ? 109 ASP C O   1 
ATOM   2929 C CB  . ASP C 1 109 ? 11.864  10.636  31.028  1.00 22.84 ? 109 ASP C CB  1 
ATOM   2930 C CG  . ASP C 1 109 ? 12.038  12.163  30.805  1.00 29.56 ? 109 ASP C CG  1 
ATOM   2931 O OD1 . ASP C 1 109 ? 12.028  12.528  29.604  1.00 38.56 ? 109 ASP C OD1 1 
ATOM   2932 O OD2 . ASP C 1 109 ? 12.205  12.987  31.773  1.00 32.10 ? 109 ASP C OD2 1 
ATOM   2933 N N   . HIS C 1 110 ? 14.634  9.262   30.838  1.00 18.65 ? 110 HIS C N   1 
ATOM   2934 C CA  . HIS C 1 110 ? 16.047  9.396   31.203  1.00 17.25 ? 110 HIS C CA  1 
ATOM   2935 C C   . HIS C 1 110 ? 16.886  8.342   30.454  1.00 17.03 ? 110 HIS C C   1 
ATOM   2936 O O   . HIS C 1 110 ? 17.977  8.013   30.885  1.00 17.24 ? 110 HIS C O   1 
ATOM   2937 C CB  . HIS C 1 110 ? 16.186  9.172   32.718  1.00 17.36 ? 110 HIS C CB  1 
ATOM   2938 C CG  . HIS C 1 110 ? 15.739  10.332  33.565  1.00 14.34 ? 110 HIS C CG  1 
ATOM   2939 N ND1 . HIS C 1 110 ? 16.080  10.456  34.893  1.00 14.08 ? 110 HIS C ND1 1 
ATOM   2940 C CD2 . HIS C 1 110 ? 15.036  11.448  33.256  1.00 17.67 ? 110 HIS C CD2 1 
ATOM   2941 C CE1 . HIS C 1 110 ? 15.588  11.587  35.370  1.00 16.22 ? 110 HIS C CE1 1 
ATOM   2942 N NE2 . HIS C 1 110 ? 14.955  12.211  34.394  1.00 12.80 ? 110 HIS C NE2 1 
ATOM   2943 N N   . CYS C 1 111 ? 16.362  7.816   29.332  1.00 15.78 ? 111 CYS C N   1 
ATOM   2944 C CA  . CYS C 1 111 ? 17.098  6.807   28.558  1.00 15.23 ? 111 CYS C CA  1 
ATOM   2945 C C   . CYS C 1 111 ? 18.401  7.384   28.081  1.00 15.33 ? 111 CYS C C   1 
ATOM   2946 O O   . CYS C 1 111 ? 18.445  8.528   27.598  1.00 14.92 ? 111 CYS C O   1 
ATOM   2947 C CB  . CYS C 1 111 ? 16.357  6.383   27.345  1.00 15.30 ? 111 CYS C CB  1 
ATOM   2948 S SG  . CYS C 1 111 ? 17.021  4.838   26.753  1.00 15.23 ? 111 CYS C SG  1 
ATOM   2949 N N   . ILE C 1 112 ? 19.476  6.626   28.275  1.00 15.47 ? 112 ILE C N   1 
ATOM   2950 C CA  . ILE C 1 112 ? 20.815  7.129   27.862  1.00 13.75 ? 112 ILE C CA  1 
ATOM   2951 C C   . ILE C 1 112 ? 21.327  6.461   26.576  1.00 13.34 ? 112 ILE C C   1 
ATOM   2952 O O   . ILE C 1 112 ? 22.218  6.937   25.951  1.00 12.37 ? 112 ILE C O   1 
ATOM   2953 C CB  . ILE C 1 112 ? 21.820  7.030   29.038  1.00 14.01 ? 112 ILE C CB  1 
ATOM   2954 C CG1 . ILE C 1 112 ? 21.790  5.621   29.656  1.00 13.35 ? 112 ILE C CG1 1 
ATOM   2955 C CG2 . ILE C 1 112 ? 21.460  8.025   30.078  1.00 13.64 ? 112 ILE C CG2 1 
ATOM   2956 C CD1 . ILE C 1 112 ? 23.055  5.229   30.376  1.00 12.33 ? 112 ILE C CD1 1 
ATOM   2957 N N   . ILE C 1 113 ? 20.750  5.326   26.218  1.00 13.05 ? 113 ILE C N   1 
ATOM   2958 C CA  . ILE C 1 113 ? 20.986  4.669   24.978  1.00 12.90 ? 113 ILE C CA  1 
ATOM   2959 C C   . ILE C 1 113 ? 20.802  5.570   23.734  1.00 11.72 ? 113 ILE C C   1 
ATOM   2960 O O   . ILE C 1 113 ? 19.813  6.305   23.657  1.00 14.49 ? 113 ILE C O   1 
ATOM   2961 C CB  . ILE C 1 113 ? 20.047  3.426   24.850  1.00 11.44 ? 113 ILE C CB  1 
ATOM   2962 C CG1 . ILE C 1 113 ? 20.458  2.387   25.923  1.00 14.97 ? 113 ILE C CG1 1 
ATOM   2963 C CG2 . ILE C 1 113 ? 20.150  2.932   23.441  1.00 10.85 ? 113 ILE C CG2 1 
ATOM   2964 C CD1 . ILE C 1 113 ? 19.567  1.081   25.976  1.00 12.25 ? 113 ILE C CD1 1 
ATOM   2965 N N   . GLY C 1 114 ? 21.789  5.554   22.819  1.00 9.23  ? 114 GLY C N   1 
ATOM   2966 C CA  . GLY C 1 114 ? 21.873  6.481   21.687  1.00 7.92  ? 114 GLY C CA  1 
ATOM   2967 C C   . GLY C 1 114 ? 22.398  7.846   22.121  1.00 8.62  ? 114 GLY C C   1 
ATOM   2968 O O   . GLY C 1 114 ? 22.412  8.811   21.329  1.00 8.76  ? 114 GLY C O   1 
ATOM   2969 N N   . ARG C 1 115 ? 22.883  7.913   23.365  1.00 7.70  ? 115 ARG C N   1 
ATOM   2970 C CA  . ARG C 1 115 ? 23.524  9.130   23.829  1.00 8.71  ? 115 ARG C CA  1 
ATOM   2971 C C   . ARG C 1 115 ? 24.981  8.754   23.898  1.00 8.30  ? 115 ARG C C   1 
ATOM   2972 O O   . ARG C 1 115 ? 25.374  7.613   23.466  1.00 8.24  ? 115 ARG C O   1 
ATOM   2973 C CB  . ARG C 1 115 ? 22.916  9.593   25.186  1.00 9.94  ? 115 ARG C CB  1 
ATOM   2974 C CG  . ARG C 1 115 ? 21.381  9.547   25.264  1.00 8.70  ? 115 ARG C CG  1 
ATOM   2975 C CD  . ARG C 1 115 ? 20.817  10.912  25.637  1.00 10.85 ? 115 ARG C CD  1 
ATOM   2976 N NE  . ARG C 1 115 ? 19.369  10.818  25.573  1.00 12.70 ? 115 ARG C NE  1 
ATOM   2977 C CZ  . ARG C 1 115 ? 18.557  11.582  24.844  1.00 17.50 ? 115 ARG C CZ  1 
ATOM   2978 N NH1 . ARG C 1 115 ? 18.980  12.662  24.135  1.00 15.57 ? 115 ARG C NH1 1 
ATOM   2979 N NH2 . ARG C 1 115 ? 17.261  11.310  24.885  1.00 22.19 ? 115 ARG C NH2 1 
ATOM   2980 N N   . THR C 1 116 ? 25.792  9.666   24.423  1.00 9.25  ? 116 THR C N   1 
ATOM   2981 C CA  . THR C 1 116 ? 27.277  9.583   24.430  1.00 9.92  ? 116 THR C CA  1 
ATOM   2982 C C   . THR C 1 116 ? 27.883  9.691   25.854  1.00 10.81 ? 116 THR C C   1 
ATOM   2983 O O   . THR C 1 116 ? 27.578  10.667  26.575  1.00 10.09 ? 116 THR C O   1 
ATOM   2984 C CB  . THR C 1 116 ? 27.883  10.736  23.564  1.00 12.33 ? 116 THR C CB  1 
ATOM   2985 O OG1 . THR C 1 116 ? 27.513  10.486  22.215  1.00 12.01 ? 116 THR C OG1 1 
ATOM   2986 C CG2 . THR C 1 116 ? 29.464  10.744  23.624  1.00 9.16  ? 116 THR C CG2 1 
ATOM   2987 N N   . LEU C 1 117 ? 28.656  8.655   26.266  1.00 8.18  ? 117 LEU C N   1 
ATOM   2988 C CA  . LEU C 1 117 ? 29.487  8.680   27.515  1.00 10.10 ? 117 LEU C CA  1 
ATOM   2989 C C   . LEU C 1 117 ? 30.808  9.384   27.276  1.00 9.61  ? 117 LEU C C   1 
ATOM   2990 O O   . LEU C 1 117 ? 31.488  8.990   26.372  1.00 6.67  ? 117 LEU C O   1 
ATOM   2991 C CB  . LEU C 1 117 ? 29.871  7.268   27.958  1.00 10.47 ? 117 LEU C CB  1 
ATOM   2992 C CG  . LEU C 1 117 ? 30.475  7.105   29.355  1.00 8.56  ? 117 LEU C CG  1 
ATOM   2993 C CD1 . LEU C 1 117 ? 29.600  7.732   30.401  1.00 10.40 ? 117 LEU C CD1 1 
ATOM   2994 C CD2 . LEU C 1 117 ? 30.558  5.645   29.563  1.00 9.48  ? 117 LEU C CD2 1 
ATOM   2995 N N   . VAL C 1 118 ? 31.124  10.459  28.029  1.00 10.45 ? 118 VAL C N   1 
ATOM   2996 C CA  . VAL C 1 118 ? 32.375  11.211  27.792  1.00 8.99  ? 118 VAL C CA  1 
ATOM   2997 C C   . VAL C 1 118 ? 33.248  11.115  29.080  1.00 11.30 ? 118 VAL C C   1 
ATOM   2998 O O   . VAL C 1 118 ? 32.752  11.329  30.175  1.00 10.15 ? 118 VAL C O   1 
ATOM   2999 C CB  . VAL C 1 118 ? 32.152  12.764  27.399  1.00 9.61  ? 118 VAL C CB  1 
ATOM   3000 C CG1 . VAL C 1 118 ? 33.502  13.435  27.008  1.00 8.30  ? 118 VAL C CG1 1 
ATOM   3001 C CG2 . VAL C 1 118 ? 31.266  12.913  26.270  1.00 8.91  ? 118 VAL C CG2 1 
ATOM   3002 N N   . VAL C 1 119 ? 34.546  10.810  28.931  1.00 14.06 ? 119 VAL C N   1 
ATOM   3003 C CA  . VAL C 1 119 ? 35.538  10.884  30.002  1.00 15.24 ? 119 VAL C CA  1 
ATOM   3004 C C   . VAL C 1 119 ? 36.328  12.150  29.749  1.00 17.42 ? 119 VAL C C   1 
ATOM   3005 O O   . VAL C 1 119 ? 36.820  12.392  28.639  1.00 18.44 ? 119 VAL C O   1 
ATOM   3006 C CB  . VAL C 1 119 ? 36.426  9.586   30.046  1.00 14.20 ? 119 VAL C CB  1 
ATOM   3007 C CG1 . VAL C 1 119 ? 37.157  9.438   28.810  1.00 13.96 ? 119 VAL C CG1 1 
ATOM   3008 C CG2 . VAL C 1 119 ? 37.403  9.601   31.230  1.00 14.20 ? 119 VAL C CG2 1 
ATOM   3009 N N   . HIS C 1 120 ? 36.392  13.013  30.767  1.00 18.99 ? 120 HIS C N   1 
ATOM   3010 C CA  . HIS C 1 120 ? 36.842  14.358  30.566  1.00 20.02 ? 120 HIS C CA  1 
ATOM   3011 C C   . HIS C 1 120 ? 38.269  14.495  31.126  1.00 22.15 ? 120 HIS C C   1 
ATOM   3012 O O   . HIS C 1 120 ? 38.777  13.608  31.846  1.00 21.48 ? 120 HIS C O   1 
ATOM   3013 C CB  . HIS C 1 120 ? 35.907  15.329  31.277  1.00 19.44 ? 120 HIS C CB  1 
ATOM   3014 C CG  . HIS C 1 120 ? 34.618  15.631  30.559  1.00 20.76 ? 120 HIS C CG  1 
ATOM   3015 N ND1 . HIS C 1 120 ? 34.409  16.807  29.867  1.00 18.26 ? 120 HIS C ND1 1 
ATOM   3016 C CD2 . HIS C 1 120 ? 33.438  14.964  30.513  1.00 18.86 ? 120 HIS C CD2 1 
ATOM   3017 C CE1 . HIS C 1 120 ? 33.169  16.847  29.419  1.00 20.11 ? 120 HIS C CE1 1 
ATOM   3018 N NE2 . HIS C 1 120 ? 32.569  15.728  29.773  1.00 14.65 ? 120 HIS C NE2 1 
ATOM   3019 N N   . GLU C 1 121 ? 38.933  15.600  30.785  1.00 24.77 ? 121 GLU C N   1 
ATOM   3020 C CA  . GLU C 1 121 ? 40.385  15.772  31.119  1.00 28.85 ? 121 GLU C CA  1 
ATOM   3021 C C   . GLU C 1 121 ? 40.639  16.083  32.626  1.00 29.03 ? 121 GLU C C   1 
ATOM   3022 O O   . GLU C 1 121 ? 41.455  15.437  33.331  1.00 28.32 ? 121 GLU C O   1 
ATOM   3023 C CB  . GLU C 1 121 ? 40.937  16.904  30.255  1.00 29.33 ? 121 GLU C CB  1 
ATOM   3024 C CG  . GLU C 1 121 ? 42.391  17.247  30.436  1.00 31.18 ? 121 GLU C CG  1 
ATOM   3025 C CD  . GLU C 1 121 ? 42.750  18.514  29.648  1.00 32.60 ? 121 GLU C CD  1 
ATOM   3026 O OE1 . GLU C 1 121 ? 43.835  18.514  29.006  1.00 38.18 ? 121 GLU C OE1 1 
ATOM   3027 O OE2 . GLU C 1 121 ? 41.938  19.483  29.648  1.00 36.58 ? 121 GLU C OE2 1 
ATOM   3028 N N   . LYS C 1 122 ? 39.902  17.104  33.071  1.00 30.07 ? 122 LYS C N   1 
ATOM   3029 C CA  . LYS C 1 122 ? 39.927  17.606  34.415  1.00 31.62 ? 122 LYS C CA  1 
ATOM   3030 C C   . LYS C 1 122 ? 38.931  16.840  35.303  1.00 33.03 ? 122 LYS C C   1 
ATOM   3031 O O   . LYS C 1 122 ? 37.913  16.344  34.814  1.00 32.76 ? 122 LYS C O   1 
ATOM   3032 C CB  . LYS C 1 122 ? 39.643  19.134  34.411  1.00 30.43 ? 122 LYS C CB  1 
ATOM   3033 C CG  . LYS C 1 122 ? 40.810  20.001  33.914  1.00 30.34 ? 122 LYS C CG  1 
ATOM   3034 C CD  . LYS C 1 122 ? 42.206  19.428  34.333  1.00 30.43 ? 122 LYS C CD  1 
ATOM   3035 C CE  . LYS C 1 122 ? 43.334  19.899  33.405  1.00 28.80 ? 122 LYS C CE  1 
ATOM   3036 N NZ  . LYS C 1 122 ? 44.345  18.836  33.081  1.00 27.52 ? 122 LYS C NZ  1 
ATOM   3037 N N   . ALA C 1 123 ? 39.271  16.721  36.591  1.00 34.55 ? 123 ALA C N   1 
ATOM   3038 C CA  . ALA C 1 123 ? 38.297  16.423  37.650  1.00 36.19 ? 123 ALA C CA  1 
ATOM   3039 C C   . ALA C 1 123 ? 37.144  17.441  37.610  1.00 37.11 ? 123 ALA C C   1 
ATOM   3040 O O   . ALA C 1 123 ? 37.347  18.616  37.303  1.00 36.78 ? 123 ALA C O   1 
ATOM   3041 C CB  . ALA C 1 123 ? 38.986  16.408  39.038  1.00 35.63 ? 123 ALA C CB  1 
ATOM   3042 N N   . ASP C 1 124 ? 35.938  16.978  37.931  1.00 38.64 ? 124 ASP C N   1 
ATOM   3043 C CA  . ASP C 1 124 ? 34.749  17.783  37.747  1.00 39.74 ? 124 ASP C CA  1 
ATOM   3044 C C   . ASP C 1 124 ? 34.187  18.276  39.082  1.00 39.86 ? 124 ASP C C   1 
ATOM   3045 O O   . ASP C 1 124 ? 34.908  18.856  39.910  1.00 39.43 ? 124 ASP C O   1 
ATOM   3046 C CB  . ASP C 1 124 ? 33.714  16.945  36.990  1.00 40.60 ? 124 ASP C CB  1 
ATOM   3047 C CG  . ASP C 1 124 ? 32.368  17.641  36.840  1.00 43.22 ? 124 ASP C CG  1 
ATOM   3048 O OD1 . ASP C 1 124 ? 32.235  18.579  36.004  1.00 44.29 ? 124 ASP C OD1 1 
ATOM   3049 O OD2 . ASP C 1 124 ? 31.423  17.208  37.537  1.00 47.50 ? 124 ASP C OD2 1 
ATOM   3050 N N   . GLY C 1 141 ? 37.399  18.899  32.152  1.00 36.55 ? 141 GLY C N   1 
ATOM   3051 C CA  . GLY C 1 141 ? 38.066  19.689  31.115  1.00 36.53 ? 141 GLY C CA  1 
ATOM   3052 C C   . GLY C 1 141 ? 37.583  19.339  29.710  1.00 35.97 ? 141 GLY C C   1 
ATOM   3053 O O   . GLY C 1 141 ? 36.400  18.916  29.541  1.00 36.18 ? 141 GLY C O   1 
ATOM   3054 N N   . SER C 1 142 ? 38.467  19.529  28.709  1.00 34.12 ? 142 SER C N   1 
ATOM   3055 C CA  . SER C 1 142 ? 38.163  19.141  27.326  1.00 32.03 ? 142 SER C CA  1 
ATOM   3056 C C   . SER C 1 142 ? 37.885  17.613  27.248  1.00 31.02 ? 142 SER C C   1 
ATOM   3057 O O   . SER C 1 142 ? 38.131  16.885  28.219  1.00 31.73 ? 142 SER C O   1 
ATOM   3058 C CB  . SER C 1 142 ? 39.288  19.615  26.391  1.00 32.80 ? 142 SER C CB  1 
ATOM   3059 O OG  . SER C 1 142 ? 40.233  18.597  26.095  1.00 29.83 ? 142 SER C OG  1 
ATOM   3060 N N   . ARG C 1 143 ? 37.383  17.122  26.113  1.00 29.38 ? 143 ARG C N   1 
ATOM   3061 C CA  . ARG C 1 143 ? 36.899  15.731  26.004  1.00 27.14 ? 143 ARG C CA  1 
ATOM   3062 C C   . ARG C 1 143 ? 37.867  14.672  25.463  1.00 25.79 ? 143 ARG C C   1 
ATOM   3063 O O   . ARG C 1 143 ? 38.317  14.755  24.345  1.00 26.23 ? 143 ARG C O   1 
ATOM   3064 C CB  . ARG C 1 143 ? 35.590  15.735  25.214  1.00 27.75 ? 143 ARG C CB  1 
ATOM   3065 C CG  . ARG C 1 143 ? 34.709  16.929  25.590  1.00 26.23 ? 143 ARG C CG  1 
ATOM   3066 C CD  . ARG C 1 143 ? 33.391  16.816  24.988  1.00 24.09 ? 143 ARG C CD  1 
ATOM   3067 N NE  . ARG C 1 143 ? 32.535  17.869  25.479  1.00 19.90 ? 143 ARG C NE  1 
ATOM   3068 C CZ  . ARG C 1 143 ? 31.336  18.144  24.991  1.00 22.37 ? 143 ARG C CZ  1 
ATOM   3069 N NH1 . ARG C 1 143 ? 30.846  17.450  23.985  1.00 23.11 ? 143 ARG C NH1 1 
ATOM   3070 N NH2 . ARG C 1 143 ? 30.633  19.130  25.503  1.00 22.83 ? 143 ARG C NH2 1 
ATOM   3071 N N   . LEU C 1 144 ? 38.138  13.641  26.235  1.00 22.68 ? 144 LEU C N   1 
ATOM   3072 C CA  . LEU C 1 144 ? 39.284  12.827  25.947  1.00 21.38 ? 144 LEU C CA  1 
ATOM   3073 C C   . LEU C 1 144 ? 38.940  11.600  25.144  1.00 20.51 ? 144 LEU C C   1 
ATOM   3074 O O   . LEU C 1 144 ? 39.718  11.122  24.334  1.00 20.82 ? 144 LEU C O   1 
ATOM   3075 C CB  . LEU C 1 144 ? 39.963  12.395  27.244  1.00 21.88 ? 144 LEU C CB  1 
ATOM   3076 C CG  . LEU C 1 144 ? 40.520  13.396  28.268  1.00 22.68 ? 144 LEU C CG  1 
ATOM   3077 C CD1 . LEU C 1 144 ? 41.395  12.689  29.303  1.00 22.49 ? 144 LEU C CD1 1 
ATOM   3078 C CD2 . LEU C 1 144 ? 41.269  14.574  27.620  1.00 21.75 ? 144 LEU C CD2 1 
ATOM   3079 N N   . ALA C 1 145 ? 37.767  11.062  25.428  1.00 18.79 ? 145 ALA C N   1 
ATOM   3080 C CA  . ALA C 1 145 ? 37.248  9.892   24.807  1.00 17.59 ? 145 ALA C CA  1 
ATOM   3081 C C   . ALA C 1 145 ? 35.742  9.909   25.081  1.00 16.93 ? 145 ALA C C   1 
ATOM   3082 O O   . ALA C 1 145 ? 35.270  10.436  26.074  1.00 17.75 ? 145 ALA C O   1 
ATOM   3083 C CB  . ALA C 1 145 ? 37.860  8.694   25.384  1.00 14.75 ? 145 ALA C CB  1 
ATOM   3084 N N   . CYS C 1 146 ? 34.994  9.338   24.163  1.00 18.03 ? 146 CYS C N   1 
ATOM   3085 C CA  . CYS C 1 146 ? 33.547  9.256   24.265  1.00 16.13 ? 146 CYS C CA  1 
ATOM   3086 C C   . CYS C 1 146 ? 33.186  8.197   23.299  1.00 12.96 ? 146 CYS C C   1 
ATOM   3087 O O   . CYS C 1 146 ? 33.920  7.966   22.355  1.00 11.59 ? 146 CYS C O   1 
ATOM   3088 C CB  . CYS C 1 146 ? 32.942  10.527  23.792  1.00 14.36 ? 146 CYS C CB  1 
ATOM   3089 S SG  . CYS C 1 146 ? 33.516  10.965  22.160  1.00 18.29 ? 146 CYS C SG  1 
ATOM   3090 N N   . GLY C 1 147 ? 31.967  7.704   23.452  1.00 12.74 ? 147 GLY C N   1 
ATOM   3091 C CA  . GLY C 1 147 ? 31.402  6.618   22.612  1.00 10.87 ? 147 GLY C CA  1 
ATOM   3092 C C   . GLY C 1 147 ? 29.891  6.612   22.752  1.00 11.43 ? 147 GLY C C   1 
ATOM   3093 O O   . GLY C 1 147 ? 29.373  7.080   23.754  1.00 12.39 ? 147 GLY C O   1 
ATOM   3094 N N   . VAL C 1 148 ? 29.178  6.116   21.742  1.00 9.13  ? 148 VAL C N   1 
ATOM   3095 C CA  . VAL C 1 148 ? 27.740  6.087   21.799  1.00 9.76  ? 148 VAL C CA  1 
ATOM   3096 C C   . VAL C 1 148 ? 27.323  4.862   22.592  1.00 11.08 ? 148 VAL C C   1 
ATOM   3097 O O   . VAL C 1 148 ? 27.977  3.817   22.444  1.00 12.77 ? 148 VAL C O   1 
ATOM   3098 C CB  . VAL C 1 148 ? 27.165  6.050   20.390  1.00 10.57 ? 148 VAL C CB  1 
ATOM   3099 C CG1 . VAL C 1 148 ? 25.646  6.072   20.423  1.00 11.01 ? 148 VAL C CG1 1 
ATOM   3100 C CG2 . VAL C 1 148 ? 27.613  7.294   19.647  1.00 8.74  ? 148 VAL C CG2 1 
ATOM   3101 N N   . ILE C 1 149 ? 26.269  5.008   23.418  1.00 10.00 ? 149 ILE C N   1 
ATOM   3102 C CA  . ILE C 1 149 ? 25.716  3.953   24.278  1.00 9.54  ? 149 ILE C CA  1 
ATOM   3103 C C   . ILE C 1 149 ? 24.743  3.112   23.486  1.00 9.34  ? 149 ILE C C   1 
ATOM   3104 O O   . ILE C 1 149 ? 23.787  3.641   22.873  1.00 5.96  ? 149 ILE C O   1 
ATOM   3105 C CB  . ILE C 1 149 ? 25.063  4.614   25.566  1.00 10.58 ? 149 ILE C CB  1 
ATOM   3106 C CG1 . ILE C 1 149 ? 26.070  5.615   26.202  1.00 8.55  ? 149 ILE C CG1 1 
ATOM   3107 C CG2 . ILE C 1 149 ? 24.698  3.592   26.576  1.00 8.08  ? 149 ILE C CG2 1 
ATOM   3108 C CD1 . ILE C 1 149 ? 25.623  6.506   27.399  1.00 8.10  ? 149 ILE C CD1 1 
ATOM   3109 N N   . GLY C 1 150 ? 24.946  1.777   23.477  1.00 7.38  ? 150 GLY C N   1 
ATOM   3110 C CA  . GLY C 1 150 ? 24.190  0.977   22.578  1.00 5.78  ? 150 GLY C CA  1 
ATOM   3111 C C   . GLY C 1 150 ? 23.684  -0.197  23.345  1.00 6.36  ? 150 GLY C C   1 
ATOM   3112 O O   . GLY C 1 150 ? 24.100  -0.423  24.407  1.00 4.43  ? 150 GLY C O   1 
ATOM   3113 N N   . ILE C 1 151 ? 22.713  -0.872  22.786  1.00 7.81  ? 151 ILE C N   1 
ATOM   3114 C CA  . ILE C 1 151 ? 21.966  -1.923  23.442  1.00 11.53 ? 151 ILE C CA  1 
ATOM   3115 C C   . ILE C 1 151 ? 22.932  -3.069  23.416  1.00 12.06 ? 151 ILE C C   1 
ATOM   3116 O O   . ILE C 1 151 ? 23.597  -3.231  22.441  1.00 12.74 ? 151 ILE C O   1 
ATOM   3117 C CB  . ILE C 1 151 ? 20.688  -2.234  22.613  1.00 11.17 ? 151 ILE C CB  1 
ATOM   3118 C CG1 . ILE C 1 151 ? 19.752  -1.040  22.761  1.00 8.69  ? 151 ILE C CG1 1 
ATOM   3119 C CG2 . ILE C 1 151 ? 20.018  -3.559  23.032  1.00 11.14 ? 151 ILE C CG2 1 
ATOM   3120 C CD1 . ILE C 1 151 ? 18.574  -0.921  21.785  1.00 10.79 ? 151 ILE C CD1 1 
ATOM   3121 N N   . ALA C 1 152 ? 22.997  -3.855  24.485  1.00 14.75 ? 152 ALA C N   1 
ATOM   3122 C CA  . ALA C 1 152 ? 23.913  -4.988  24.501  1.00 15.28 ? 152 ALA C CA  1 
ATOM   3123 C C   . ALA C 1 152 ? 23.190  -6.276  24.729  1.00 16.52 ? 152 ALA C C   1 
ATOM   3124 O O   . ALA C 1 152 ? 22.084  -6.351  25.185  1.00 13.84 ? 152 ALA C O   1 
ATOM   3125 C CB  . ALA C 1 152 ? 24.994  -4.840  25.548  1.00 14.79 ? 152 ALA C CB  1 
ATOM   3126 N N   . GLN C 1 153 ? 23.911  -7.313  24.406  1.00 19.40 ? 153 GLN C N   1 
ATOM   3127 C CA  . GLN C 1 153 ? 23.340  -8.597  24.255  1.00 23.18 ? 153 GLN C CA  1 
ATOM   3128 C C   . GLN C 1 153 ? 23.130  -9.094  25.649  1.00 23.95 ? 153 GLN C C   1 
ATOM   3129 O O   . GLN C 1 153 ? 24.026  -9.570  26.380  1.00 26.04 ? 153 GLN C O   1 
ATOM   3130 C CB  . GLN C 1 153 ? 24.289  -9.470  23.443  1.00 22.79 ? 153 GLN C CB  1 
ATOM   3131 C CG  . GLN C 1 153 ? 23.553  -10.610 22.840  1.00 29.62 ? 153 GLN C CG  1 
ATOM   3132 C CD  . GLN C 1 153 ? 24.416  -11.494 22.012  1.00 31.25 ? 153 GLN C CD  1 
ATOM   3133 O OE1 . GLN C 1 153 ? 25.645  -11.342 21.965  1.00 32.66 ? 153 GLN C OE1 1 
ATOM   3134 N NE2 . GLN C 1 153 ? 23.780  -12.438 21.343  1.00 36.70 ? 153 GLN C NE2 1 
ATOM   3135 O OXT . GLN C 1 153 ? 21.987  -8.976  26.056  1.00 24.86 ? 153 GLN C OXT 1 
ATOM   3136 N N   . ALA D 1 1   ? 12.481  10.803  19.073  1.00 32.22 ? 1   ALA D N   1 
ATOM   3137 C CA  . ALA D 1 1   ? 13.558  11.478  18.280  1.00 31.35 ? 1   ALA D CA  1 
ATOM   3138 C C   . ALA D 1 1   ? 13.194  11.551  16.792  1.00 30.44 ? 1   ALA D C   1 
ATOM   3139 O O   . ALA D 1 1   ? 12.624  10.620  16.215  1.00 30.46 ? 1   ALA D O   1 
ATOM   3140 C CB  . ALA D 1 1   ? 14.929  10.798  18.506  1.00 31.41 ? 1   ALA D CB  1 
ATOM   3141 N N   . THR D 1 2   ? 13.466  12.705  16.192  1.00 28.89 ? 2   THR D N   1 
ATOM   3142 C CA  . THR D 1 2   ? 13.212  12.872  14.786  1.00 26.85 ? 2   THR D CA  1 
ATOM   3143 C C   . THR D 1 2   ? 14.476  12.601  13.998  1.00 24.22 ? 2   THR D C   1 
ATOM   3144 O O   . THR D 1 2   ? 14.383  12.274  12.835  1.00 23.76 ? 2   THR D O   1 
ATOM   3145 C CB  . THR D 1 2   ? 12.702  14.279  14.455  1.00 27.05 ? 2   THR D CB  1 
ATOM   3146 O OG1 . THR D 1 2   ? 13.466  15.247  15.199  1.00 30.70 ? 2   THR D OG1 1 
ATOM   3147 C CG2 . THR D 1 2   ? 11.194  14.412  14.757  1.00 27.96 ? 2   THR D CG2 1 
ATOM   3148 N N   . LYS D 1 3   ? 15.640  12.719  14.637  1.00 22.75 ? 3   LYS D N   1 
ATOM   3149 C CA  . LYS D 1 3   ? 16.951  12.685  13.963  1.00 21.02 ? 3   LYS D CA  1 
ATOM   3150 C C   . LYS D 1 3   ? 17.970  11.774  14.618  1.00 19.80 ? 3   LYS D C   1 
ATOM   3151 O O   . LYS D 1 3   ? 17.987  11.591  15.830  1.00 20.40 ? 3   LYS D O   1 
ATOM   3152 C CB  . LYS D 1 3   ? 17.536  14.089  13.836  1.00 21.00 ? 3   LYS D CB  1 
ATOM   3153 C CG  . LYS D 1 3   ? 16.841  14.929  12.812  1.00 22.77 ? 3   LYS D CG  1 
ATOM   3154 C CD  . LYS D 1 3   ? 17.189  16.428  12.924  1.00 27.27 ? 3   LYS D CD  1 
ATOM   3155 C CE  . LYS D 1 3   ? 15.992  17.253  12.361  1.00 31.70 ? 3   LYS D CE  1 
ATOM   3156 N NZ  . LYS D 1 3   ? 16.343  18.577  11.744  1.00 32.38 ? 3   LYS D NZ  1 
ATOM   3157 N N   . ALA D 1 4   ? 18.825  11.176  13.805  1.00 18.62 ? 4   ALA D N   1 
ATOM   3158 C CA  . ALA D 1 4   ? 19.783  10.221  14.327  1.00 17.62 ? 4   ALA D CA  1 
ATOM   3159 C C   . ALA D 1 4   ? 20.990  10.292  13.430  1.00 16.38 ? 4   ALA D C   1 
ATOM   3160 O O   . ALA D 1 4   ? 20.896  10.867  12.331  1.00 16.68 ? 4   ALA D O   1 
ATOM   3161 C CB  . ALA D 1 4   ? 19.202  8.865   14.321  1.00 17.27 ? 4   ALA D CB  1 
ATOM   3162 N N   . VAL D 1 5   ? 22.119  9.753   13.888  1.00 14.56 ? 5   VAL D N   1 
ATOM   3163 C CA  . VAL D 1 5   ? 23.346  9.869   13.120  1.00 13.85 ? 5   VAL D CA  1 
ATOM   3164 C C   . VAL D 1 5   ? 24.190  8.658   13.354  1.00 12.75 ? 5   VAL D C   1 
ATOM   3165 O O   . VAL D 1 5   ? 24.033  7.961   14.337  1.00 11.86 ? 5   VAL D O   1 
ATOM   3166 C CB  . VAL D 1 5   ? 24.116  11.141  13.460  1.00 13.07 ? 5   VAL D CB  1 
ATOM   3167 C CG1 . VAL D 1 5   ? 24.799  10.991  14.741  1.00 15.28 ? 5   VAL D CG1 1 
ATOM   3168 C CG2 . VAL D 1 5   ? 25.159  11.493  12.367  1.00 13.36 ? 5   VAL D CG2 1 
ATOM   3169 N N   . CYS D 1 6   ? 25.115  8.407   12.438  1.00 13.72 ? 6   CYS D N   1 
ATOM   3170 C CA  . CYS D 1 6   ? 25.972  7.215   12.547  1.00 12.89 ? 6   CYS D CA  1 
ATOM   3171 C C   . CYS D 1 6   ? 27.290  7.544   11.868  1.00 13.85 ? 6   CYS D C   1 
ATOM   3172 O O   . CYS D 1 6   ? 27.291  8.135   10.776  1.00 14.09 ? 6   CYS D O   1 
ATOM   3173 C CB  . CYS D 1 6   ? 25.301  5.989   12.024  1.00 12.83 ? 6   CYS D CB  1 
ATOM   3174 S SG  . CYS D 1 6   ? 26.236  4.456   12.284  1.00 13.72 ? 6   CYS D SG  1 
ATOM   3175 N N   . VAL D 1 7   ? 28.401  7.305   12.596  1.00 16.00 ? 7   VAL D N   1 
ATOM   3176 C CA  . VAL D 1 7   ? 29.772  7.376   12.084  1.00 15.19 ? 7   VAL D CA  1 
ATOM   3177 C C   . VAL D 1 7   ? 30.192  5.896   11.871  1.00 15.93 ? 7   VAL D C   1 
ATOM   3178 O O   . VAL D 1 7   ? 30.165  5.096   12.839  1.00 15.57 ? 7   VAL D O   1 
ATOM   3179 C CB  . VAL D 1 7   ? 30.687  8.183   13.057  1.00 15.43 ? 7   VAL D CB  1 
ATOM   3180 C CG1 . VAL D 1 7   ? 32.131  8.227   12.569  1.00 14.75 ? 7   VAL D CG1 1 
ATOM   3181 C CG2 . VAL D 1 7   ? 30.162  9.699   13.228  1.00 15.79 ? 7   VAL D CG2 1 
ATOM   3182 N N   . LEU D 1 8   ? 30.493  5.515   10.609  1.00 15.86 ? 8   LEU D N   1 
ATOM   3183 C CA  . LEU D 1 8   ? 30.929  4.122   10.253  1.00 16.23 ? 8   LEU D CA  1 
ATOM   3184 C C   . LEU D 1 8   ? 32.462  4.209   10.218  1.00 16.83 ? 8   LEU D C   1 
ATOM   3185 O O   . LEU D 1 8   ? 32.993  5.238   9.804   1.00 16.42 ? 8   LEU D O   1 
ATOM   3186 C CB  . LEU D 1 8   ? 30.458  3.730   8.876   1.00 15.71 ? 8   LEU D CB  1 
ATOM   3187 C CG  . LEU D 1 8   ? 29.180  2.972   8.419   1.00 17.28 ? 8   LEU D CG  1 
ATOM   3188 C CD1 . LEU D 1 8   ? 28.244  2.621   9.419   1.00 13.34 ? 8   LEU D CD1 1 
ATOM   3189 C CD2 . LEU D 1 8   ? 28.496  3.838   7.300   1.00 18.52 ? 8   LEU D CD2 1 
ATOM   3190 N N   . LYS D 1 9   ? 33.154  3.202   10.755  1.00 17.45 ? 9   LYS D N   1 
ATOM   3191 C CA  . LYS D 1 9   ? 34.613  3.200   10.916  1.00 18.73 ? 9   LYS D CA  1 
ATOM   3192 C C   . LYS D 1 9   ? 34.832  1.728   11.102  1.00 19.73 ? 9   LYS D C   1 
ATOM   3193 O O   . LYS D 1 9   ? 33.955  1.087   11.627  1.00 18.86 ? 9   LYS D O   1 
ATOM   3194 C CB  . LYS D 1 9   ? 35.019  3.988   12.172  1.00 19.48 ? 9   LYS D CB  1 
ATOM   3195 C CG  . LYS D 1 9   ? 35.382  5.472   11.849  1.00 20.34 ? 9   LYS D CG  1 
ATOM   3196 C CD  . LYS D 1 9   ? 35.737  6.392   13.043  1.00 20.89 ? 9   LYS D CD  1 
ATOM   3197 C CE  . LYS D 1 9   ? 36.192  7.748   12.489  1.00 21.87 ? 9   LYS D CE  1 
ATOM   3198 N NZ  . LYS D 1 9   ? 35.651  8.934   13.222  1.00 24.62 ? 9   LYS D NZ  1 
ATOM   3199 N N   . GLY D 1 10  ? 35.927  1.175   10.579  1.00 21.03 ? 10  GLY D N   1 
ATOM   3200 C CA  . GLY D 1 10  ? 36.238  -0.233  10.756  1.00 23.41 ? 10  GLY D CA  1 
ATOM   3201 C C   . GLY D 1 10  ? 37.748  -0.349  10.844  1.00 26.04 ? 10  GLY D C   1 
ATOM   3202 O O   . GLY D 1 10  ? 38.442  0.664   11.093  1.00 26.46 ? 10  GLY D O   1 
ATOM   3203 N N   . ASP D 1 11  ? 38.247  -1.566  10.639  1.00 27.48 ? 11  ASP D N   1 
ATOM   3204 C CA  . ASP D 1 11  ? 39.702  -1.874  10.623  1.00 29.90 ? 11  ASP D CA  1 
ATOM   3205 C C   . ASP D 1 11  ? 40.433  -1.277  9.389   1.00 29.94 ? 11  ASP D C   1 
ATOM   3206 O O   . ASP D 1 11  ? 41.565  -0.744  9.529   1.00 30.99 ? 11  ASP D O   1 
ATOM   3207 C CB  . ASP D 1 11  ? 39.966  -3.400  10.691  1.00 29.86 ? 11  ASP D CB  1 
ATOM   3208 C CG  . ASP D 1 11  ? 39.334  -4.073  11.934  1.00 33.78 ? 11  ASP D CG  1 
ATOM   3209 O OD1 . ASP D 1 11  ? 39.014  -5.288  11.867  1.00 33.94 ? 11  ASP D OD1 1 
ATOM   3210 O OD2 . ASP D 1 11  ? 39.135  -3.399  12.977  1.00 34.41 ? 11  ASP D OD2 1 
ATOM   3211 N N   . GLY D 1 12  ? 39.795  -1.381  8.209   1.00 28.92 ? 12  GLY D N   1 
ATOM   3212 C CA  . GLY D 1 12  ? 40.311  -0.913  6.944   1.00 26.58 ? 12  GLY D CA  1 
ATOM   3213 C C   . GLY D 1 12  ? 39.951  0.535   6.727   1.00 26.16 ? 12  GLY D C   1 
ATOM   3214 O O   . GLY D 1 12  ? 39.706  1.236   7.701   1.00 24.64 ? 12  GLY D O   1 
ATOM   3215 N N   . PRO D 1 13  ? 39.945  0.993   5.448   1.00 26.49 ? 13  PRO D N   1 
ATOM   3216 C CA  . PRO D 1 13  ? 39.730  2.419   5.023   1.00 27.22 ? 13  PRO D CA  1 
ATOM   3217 C C   . PRO D 1 13  ? 38.256  2.897   4.886   1.00 26.78 ? 13  PRO D C   1 
ATOM   3218 O O   . PRO D 1 13  ? 38.011  4.102   4.745   1.00 27.43 ? 13  PRO D O   1 
ATOM   3219 C CB  . PRO D 1 13  ? 40.451  2.507   3.680   1.00 26.97 ? 13  PRO D CB  1 
ATOM   3220 C CG  . PRO D 1 13  ? 40.418  1.109   3.137   1.00 27.17 ? 13  PRO D CG  1 
ATOM   3221 C CD  . PRO D 1 13  ? 40.143  0.115   4.278   1.00 27.04 ? 13  PRO D CD  1 
ATOM   3222 N N   . VAL D 1 14  ? 37.310  1.963   4.965   1.00 26.85 ? 14  VAL D N   1 
ATOM   3223 C CA  . VAL D 1 14  ? 35.865  2.255   4.916   1.00 26.72 ? 14  VAL D CA  1 
ATOM   3224 C C   . VAL D 1 14  ? 35.342  3.156   6.051   1.00 26.72 ? 14  VAL D C   1 
ATOM   3225 O O   . VAL D 1 14  ? 35.322  2.778   7.197   1.00 26.42 ? 14  VAL D O   1 
ATOM   3226 C CB  . VAL D 1 14  ? 35.028  0.956   4.918   1.00 26.63 ? 14  VAL D CB  1 
ATOM   3227 C CG1 . VAL D 1 14  ? 33.585  1.296   4.604   1.00 28.15 ? 14  VAL D CG1 1 
ATOM   3228 C CG2 . VAL D 1 14  ? 35.584  -0.077  3.920   1.00 25.48 ? 14  VAL D CG2 1 
ATOM   3229 N N   . GLN D 1 15  ? 34.907  4.355   5.719   1.00 27.20 ? 15  GLN D N   1 
ATOM   3230 C CA  . GLN D 1 15  ? 34.327  5.229   6.724   1.00 28.42 ? 15  GLN D CA  1 
ATOM   3231 C C   . GLN D 1 15  ? 33.234  6.165   6.216   1.00 26.82 ? 15  GLN D C   1 
ATOM   3232 O O   . GLN D 1 15  ? 33.315  6.682   5.115   1.00 26.40 ? 15  GLN D O   1 
ATOM   3233 C CB  . GLN D 1 15  ? 35.433  6.021   7.431   1.00 28.90 ? 15  GLN D CB  1 
ATOM   3234 C CG  . GLN D 1 15  ? 36.138  7.056   6.605   1.00 32.38 ? 15  GLN D CG  1 
ATOM   3235 C CD  . GLN D 1 15  ? 37.070  7.912   7.446   1.00 34.69 ? 15  GLN D CD  1 
ATOM   3236 O OE1 . GLN D 1 15  ? 36.720  8.314   8.559   1.00 40.88 ? 15  GLN D OE1 1 
ATOM   3237 N NE2 . GLN D 1 15  ? 38.254  8.198   6.923   1.00 38.20 ? 15  GLN D NE2 1 
ATOM   3238 N N   . GLY D 1 16  ? 32.233  6.427   7.049   1.00 26.42 ? 16  GLY D N   1 
ATOM   3239 C CA  . GLY D 1 16  ? 31.068  7.169   6.596   1.00 25.16 ? 16  GLY D CA  1 
ATOM   3240 C C   . GLY D 1 16  ? 30.317  7.982   7.630   1.00 24.49 ? 16  GLY D C   1 
ATOM   3241 O O   . GLY D 1 16  ? 30.639  7.968   8.773   1.00 23.94 ? 16  GLY D O   1 
ATOM   3242 N N   . ILE D 1 17  ? 29.340  8.749   7.175   1.00 24.37 ? 17  ILE D N   1 
ATOM   3243 C CA  . ILE D 1 17  ? 28.398  9.450   8.031   1.00 23.43 ? 17  ILE D CA  1 
ATOM   3244 C C   . ILE D 1 17  ? 27.008  9.309   7.417   1.00 22.54 ? 17  ILE D C   1 
ATOM   3245 O O   . ILE D 1 17  ? 26.707  9.947   6.394   1.00 21.88 ? 17  ILE D O   1 
ATOM   3246 C CB  . ILE D 1 17  ? 28.745  10.941  8.166   1.00 23.89 ? 17  ILE D CB  1 
ATOM   3247 C CG1 . ILE D 1 17  ? 30.213  11.108  8.589   1.00 24.82 ? 17  ILE D CG1 1 
ATOM   3248 C CG2 . ILE D 1 17  ? 27.764  11.632  9.131   1.00 23.53 ? 17  ILE D CG2 1 
ATOM   3249 C CD1 . ILE D 1 17  ? 30.662  12.574  8.686   1.00 24.19 ? 17  ILE D CD1 1 
ATOM   3250 N N   . ILE D 1 18  ? 26.179  8.478   8.042   1.00 21.26 ? 18  ILE D N   1 
ATOM   3251 C CA  . ILE D 1 18  ? 24.793  8.266   7.641   1.00 19.87 ? 18  ILE D CA  1 
ATOM   3252 C C   . ILE D 1 18  ? 23.881  9.006   8.601   1.00 19.61 ? 18  ILE D C   1 
ATOM   3253 O O   . ILE D 1 18  ? 23.919  8.777   9.796   1.00 18.23 ? 18  ILE D O   1 
ATOM   3254 C CB  . ILE D 1 18  ? 24.416  6.748   7.556   1.00 20.69 ? 18  ILE D CB  1 
ATOM   3255 C CG1 . ILE D 1 18  ? 25.261  6.037   6.478   1.00 19.06 ? 18  ILE D CG1 1 
ATOM   3256 C CG2 . ILE D 1 18  ? 22.960  6.543   7.203   1.00 17.89 ? 18  ILE D CG2 1 
ATOM   3257 C CD1 . ILE D 1 18  ? 25.407  6.803   5.072   1.00 20.71 ? 18  ILE D CD1 1 
ATOM   3258 N N   . ASN D 1 19  ? 23.101  9.927   8.052   1.00 18.59 ? 19  ASN D N   1 
ATOM   3259 C CA  . ASN D 1 19  ? 22.008  10.516  8.772   1.00 17.91 ? 19  ASN D CA  1 
ATOM   3260 C C   . ASN D 1 19  ? 20.655  9.825   8.632   1.00 17.62 ? 19  ASN D C   1 
ATOM   3261 O O   . ASN D 1 19  ? 20.295  9.423   7.537   1.00 15.67 ? 19  ASN D O   1 
ATOM   3262 C CB  . ASN D 1 19  ? 21.779  11.880  8.221   1.00 18.95 ? 19  ASN D CB  1 
ATOM   3263 C CG  . ASN D 1 19  ? 22.985  12.700  8.261   1.00 19.81 ? 19  ASN D CG  1 
ATOM   3264 O OD1 . ASN D 1 19  ? 23.748  12.702  7.305   1.00 23.69 ? 19  ASN D OD1 1 
ATOM   3265 N ND2 . ASN D 1 19  ? 23.179  13.430  9.360   1.00 17.36 ? 19  ASN D ND2 1 
ATOM   3266 N N   . PHE D 1 20  ? 19.881  9.809   9.723   1.00 17.58 ? 20  PHE D N   1 
ATOM   3267 C CA  . PHE D 1 20  ? 18.432  9.436   9.745   1.00 18.38 ? 20  PHE D CA  1 
ATOM   3268 C C   . PHE D 1 20  ? 17.498  10.600  10.106  1.00 19.56 ? 20  PHE D C   1 
ATOM   3269 O O   . PHE D 1 20  ? 17.883  11.548  10.803  1.00 20.44 ? 20  PHE D O   1 
ATOM   3270 C CB  . PHE D 1 20  ? 18.168  8.273   10.693  1.00 16.66 ? 20  PHE D CB  1 
ATOM   3271 C CG  . PHE D 1 20  ? 19.092  7.095   10.476  1.00 15.61 ? 20  PHE D CG  1 
ATOM   3272 C CD1 . PHE D 1 20  ? 20.430  7.147   10.870  1.00 14.44 ? 20  PHE D CD1 1 
ATOM   3273 C CD2 . PHE D 1 20  ? 18.625  5.954   9.859   1.00 15.14 ? 20  PHE D CD2 1 
ATOM   3274 C CE1 . PHE D 1 20  ? 21.279  6.055   10.665  1.00 14.55 ? 20  PHE D CE1 1 
ATOM   3275 C CE2 . PHE D 1 20  ? 19.458  4.860   9.667   1.00 14.15 ? 20  PHE D CE2 1 
ATOM   3276 C CZ  . PHE D 1 20  ? 20.796  4.933   10.091  1.00 14.78 ? 20  PHE D CZ  1 
ATOM   3277 N N   . GLU D 1 21  ? 16.295  10.552  9.537   1.00 21.40 ? 21  GLU D N   1 
ATOM   3278 C CA  . GLU D 1 21  ? 15.261  11.526  9.814   1.00 23.83 ? 21  GLU D CA  1 
ATOM   3279 C C   . GLU D 1 21  ? 13.868  10.964  9.679   1.00 23.91 ? 21  GLU D C   1 
ATOM   3280 O O   . GLU D 1 21  ? 13.539  10.407  8.663   1.00 24.20 ? 21  GLU D O   1 
ATOM   3281 C CB  . GLU D 1 21  ? 15.369  12.754  8.918   1.00 24.51 ? 21  GLU D CB  1 
ATOM   3282 C CG  . GLU D 1 21  ? 14.540  13.830  9.474   1.00 28.87 ? 21  GLU D CG  1 
ATOM   3283 C CD  . GLU D 1 21  ? 14.699  15.152  8.716   1.00 37.71 ? 21  GLU D CD  1 
ATOM   3284 O OE1 . GLU D 1 21  ? 15.720  15.852  8.903   1.00 40.66 ? 21  GLU D OE1 1 
ATOM   3285 O OE2 . GLU D 1 21  ? 13.779  15.498  7.938   1.00 42.42 ? 21  GLU D OE2 1 
ATOM   3286 N N   . GLN D 1 22  ? 13.046  11.129  10.705  1.00 26.04 ? 22  GLN D N   1 
ATOM   3287 C CA  . GLN D 1 22  ? 11.630  10.703  10.662  1.00 27.66 ? 22  GLN D CA  1 
ATOM   3288 C C   . GLN D 1 22  ? 10.762  11.874  11.119  1.00 29.99 ? 22  GLN D C   1 
ATOM   3289 O O   . GLN D 1 22  ? 10.522  12.056  12.299  1.00 29.89 ? 22  GLN D O   1 
ATOM   3290 C CB  . GLN D 1 22  ? 11.411  9.477   11.557  1.00 26.97 ? 22  GLN D CB  1 
ATOM   3291 C CG  . GLN D 1 22  ? 10.203  8.652   11.208  1.00 25.13 ? 22  GLN D CG  1 
ATOM   3292 C CD  . GLN D 1 22  ? 10.115  7.410   12.042  1.00 27.04 ? 22  GLN D CD  1 
ATOM   3293 O OE1 . GLN D 1 22  ? 10.816  7.270   13.049  1.00 27.40 ? 22  GLN D OE1 1 
ATOM   3294 N NE2 . GLN D 1 22  ? 9.255   6.483   11.628  1.00 25.32 ? 22  GLN D NE2 1 
ATOM   3295 N N   . LYS D 1 23  ? 10.347  12.702  10.176  1.00 33.66 ? 23  LYS D N   1 
ATOM   3296 C CA  . LYS D 1 23  ? 9.423   13.806  10.440  1.00 37.26 ? 23  LYS D CA  1 
ATOM   3297 C C   . LYS D 1 23  ? 8.087   13.368  11.101  1.00 38.91 ? 23  LYS D C   1 
ATOM   3298 O O   . LYS D 1 23  ? 7.402   14.205  11.705  1.00 39.69 ? 23  LYS D O   1 
ATOM   3299 C CB  . LYS D 1 23  ? 9.138   14.601  9.140   1.00 37.78 ? 23  LYS D CB  1 
ATOM   3300 C CG  . LYS D 1 23  ? 8.670   13.729  7.914   1.00 38.63 ? 23  LYS D CG  1 
ATOM   3301 C CD  . LYS D 1 23  ? 8.276   14.558  6.675   1.00 38.95 ? 23  LYS D CD  1 
ATOM   3302 C CE  . LYS D 1 23  ? 9.218   15.777  6.430   1.00 40.79 ? 23  LYS D CE  1 
ATOM   3303 N NZ  . LYS D 1 23  ? 8.969   16.482  5.133   1.00 39.58 ? 23  LYS D NZ  1 
ATOM   3304 N N   . GLU D 1 24  ? 7.711   12.085  11.005  1.00 40.41 ? 24  GLU D N   1 
ATOM   3305 C CA  . GLU D 1 24  ? 6.522   11.636  11.724  1.00 42.28 ? 24  GLU D CA  1 
ATOM   3306 C C   . GLU D 1 24  ? 6.501   10.199  12.229  1.00 41.41 ? 24  GLU D C   1 
ATOM   3307 O O   . GLU D 1 24  ? 6.953   9.297   11.573  1.00 41.72 ? 24  GLU D O   1 
ATOM   3308 C CB  . GLU D 1 24  ? 5.244   11.970  10.936  1.00 42.52 ? 24  GLU D CB  1 
ATOM   3309 C CG  . GLU D 1 24  ? 5.114   11.343  9.527   1.00 45.69 ? 24  GLU D CG  1 
ATOM   3310 C CD  . GLU D 1 24  ? 3.624   11.124  9.105   1.00 45.95 ? 24  GLU D CD  1 
ATOM   3311 O OE1 . GLU D 1 24  ? 2.739   11.768  9.754   1.00 51.82 ? 24  GLU D OE1 1 
ATOM   3312 O OE2 . GLU D 1 24  ? 3.344   10.317  8.160   1.00 46.04 ? 24  GLU D OE2 1 
ATOM   3313 N N   . SER D 1 25  ? 5.932   10.030  13.408  1.00 41.23 ? 25  SER D N   1 
ATOM   3314 C CA  . SER D 1 25  ? 5.739   8.754   14.099  1.00 41.27 ? 25  SER D CA  1 
ATOM   3315 C C   . SER D 1 25  ? 5.677   7.417   13.326  1.00 40.91 ? 25  SER D C   1 
ATOM   3316 O O   . SER D 1 25  ? 6.484   6.557   13.602  1.00 40.92 ? 25  SER D O   1 
ATOM   3317 C CB  . SER D 1 25  ? 4.508   8.884   15.013  1.00 41.81 ? 25  SER D CB  1 
ATOM   3318 O OG  . SER D 1 25  ? 4.621   8.107   16.197  1.00 44.55 ? 25  SER D OG  1 
ATOM   3319 N N   . ASN D 1 26  ? 4.686   7.178   12.453  1.00 40.93 ? 26  ASN D N   1 
ATOM   3320 C CA  . ASN D 1 26  ? 4.625   5.875   11.698  1.00 40.68 ? 26  ASN D CA  1 
ATOM   3321 C C   . ASN D 1 26  ? 5.135   6.057   10.281  1.00 39.23 ? 26  ASN D C   1 
ATOM   3322 O O   . ASN D 1 26  ? 5.127   5.106   9.469   1.00 40.10 ? 26  ASN D O   1 
ATOM   3323 C CB  . ASN D 1 26  ? 3.219   5.225   11.587  1.00 41.48 ? 26  ASN D CB  1 
ATOM   3324 C CG  . ASN D 1 26  ? 2.402   5.275   12.888  1.00 43.30 ? 26  ASN D CG  1 
ATOM   3325 O OD1 . ASN D 1 26  ? 1.340   5.920   12.923  1.00 42.94 ? 26  ASN D OD1 1 
ATOM   3326 N ND2 . ASN D 1 26  ? 2.879   4.584   13.950  1.00 44.28 ? 26  ASN D ND2 1 
ATOM   3327 N N   . GLY D 1 27  ? 5.557   7.286   9.992   1.00 36.96 ? 27  GLY D N   1 
ATOM   3328 C CA  . GLY D 1 27  ? 6.112   7.633   8.715   1.00 33.81 ? 27  GLY D CA  1 
ATOM   3329 C C   . GLY D 1 27  ? 7.472   7.029   8.388   1.00 31.77 ? 27  GLY D C   1 
ATOM   3330 O O   . GLY D 1 27  ? 8.136   6.356   9.203   1.00 31.22 ? 27  GLY D O   1 
ATOM   3331 N N   . PRO D 1 28  ? 7.910   7.293   7.166   1.00 29.83 ? 28  PRO D N   1 
ATOM   3332 C CA  . PRO D 1 28  ? 9.195   6.780   6.731   1.00 28.02 ? 28  PRO D CA  1 
ATOM   3333 C C   . PRO D 1 28  ? 10.387  7.581   7.295   1.00 25.49 ? 28  PRO D C   1 
ATOM   3334 O O   . PRO D 1 28  ? 10.272  8.769   7.657   1.00 25.25 ? 28  PRO D O   1 
ATOM   3335 C CB  . PRO D 1 28  ? 9.107   6.849   5.198   1.00 26.88 ? 28  PRO D CB  1 
ATOM   3336 C CG  . PRO D 1 28  ? 8.170   8.056   4.932   1.00 29.41 ? 28  PRO D CG  1 
ATOM   3337 C CD  . PRO D 1 28  ? 7.222   8.108   6.135   1.00 30.38 ? 28  PRO D CD  1 
ATOM   3338 N N   . VAL D 1 29  ? 11.527  6.898   7.323   1.00 24.15 ? 29  VAL D N   1 
ATOM   3339 C CA  . VAL D 1 29  ? 12.800  7.440   7.767   1.00 21.52 ? 29  VAL D CA  1 
ATOM   3340 C C   . VAL D 1 29  ? 13.649  7.607   6.499   1.00 21.42 ? 29  VAL D C   1 
ATOM   3341 O O   . VAL D 1 29  ? 13.886  6.665   5.750   1.00 19.24 ? 29  VAL D O   1 
ATOM   3342 C CB  . VAL D 1 29  ? 13.522  6.459   8.735   1.00 21.45 ? 29  VAL D CB  1 
ATOM   3343 C CG1 . VAL D 1 29  ? 14.660  7.115   9.411   1.00 17.69 ? 29  VAL D CG1 1 
ATOM   3344 C CG2 . VAL D 1 29  ? 12.598  5.902   9.771   1.00 21.55 ? 29  VAL D CG2 1 
ATOM   3345 N N   . LYS D 1 30  ? 14.071  8.831   6.234   1.00 20.88 ? 30  LYS D N   1 
ATOM   3346 C CA  . LYS D 1 30  ? 15.076  9.067   5.225   1.00 22.05 ? 30  LYS D CA  1 
ATOM   3347 C C   . LYS D 1 30  ? 16.515  8.761   5.724   1.00 21.34 ? 30  LYS D C   1 
ATOM   3348 O O   . LYS D 1 30  ? 17.091  9.544   6.461   1.00 22.45 ? 30  LYS D O   1 
ATOM   3349 C CB  . LYS D 1 30  ? 14.984  10.541  4.736   1.00 21.66 ? 30  LYS D CB  1 
ATOM   3350 C CG  . LYS D 1 30  ? 13.588  11.088  4.352   1.00 23.85 ? 30  LYS D CG  1 
ATOM   3351 C CD  . LYS D 1 30  ? 13.453  12.687  4.600   1.00 27.22 ? 30  LYS D CD  1 
ATOM   3352 C CE  . LYS D 1 30  ? 12.732  13.085  5.987   1.00 33.93 ? 30  LYS D CE  1 
ATOM   3353 N NZ  . LYS D 1 30  ? 11.518  12.190  6.438   1.00 37.66 ? 30  LYS D NZ  1 
ATOM   3354 N N   . VAL D 1 31  ? 17.132  7.657   5.305   1.00 21.30 ? 31  VAL D N   1 
ATOM   3355 C CA  . VAL D 1 31  ? 18.583  7.504   5.468   1.00 20.27 ? 31  VAL D CA  1 
ATOM   3356 C C   . VAL D 1 31  ? 19.454  8.087   4.274   1.00 22.07 ? 31  VAL D C   1 
ATOM   3357 O O   . VAL D 1 31  ? 19.352  7.617   3.129   1.00 21.88 ? 31  VAL D O   1 
ATOM   3358 C CB  . VAL D 1 31  ? 18.965  6.053   5.978   1.00 20.44 ? 31  VAL D CB  1 
ATOM   3359 C CG1 . VAL D 1 31  ? 17.820  5.060   5.822   1.00 17.72 ? 31  VAL D CG1 1 
ATOM   3360 C CG2 . VAL D 1 31  ? 20.200  5.557   5.415   1.00 15.46 ? 31  VAL D CG2 1 
ATOM   3361 N N   . TRP D 1 32  ? 20.244  9.148   4.551   1.00 22.46 ? 32  TRP D N   1 
ATOM   3362 C CA  . TRP D 1 32  ? 21.180  9.764   3.597   1.00 21.87 ? 32  TRP D CA  1 
ATOM   3363 C C   . TRP D 1 32  ? 22.579  10.012  4.162   1.00 22.37 ? 32  TRP D C   1 
ATOM   3364 O O   . TRP D 1 32  ? 22.789  9.958   5.369   1.00 22.50 ? 32  TRP D O   1 
ATOM   3365 C CB  . TRP D 1 32  ? 20.607  11.072  3.081   1.00 22.83 ? 32  TRP D CB  1 
ATOM   3366 C CG  . TRP D 1 32  ? 20.743  12.241  3.979   1.00 22.33 ? 32  TRP D CG  1 
ATOM   3367 C CD1 . TRP D 1 32  ? 21.660  13.235  3.877   1.00 24.80 ? 32  TRP D CD1 1 
ATOM   3368 C CD2 . TRP D 1 32  ? 19.895  12.587  5.065   1.00 25.03 ? 32  TRP D CD2 1 
ATOM   3369 N NE1 . TRP D 1 32  ? 21.477  14.175  4.865   1.00 24.97 ? 32  TRP D NE1 1 
ATOM   3370 C CE2 . TRP D 1 32  ? 20.388  13.803  5.611   1.00 25.29 ? 32  TRP D CE2 1 
ATOM   3371 C CE3 . TRP D 1 32  ? 18.790  11.964  5.675   1.00 26.22 ? 32  TRP D CE3 1 
ATOM   3372 C CZ2 . TRP D 1 32  ? 19.797  14.431  6.729   1.00 25.67 ? 32  TRP D CZ2 1 
ATOM   3373 C CZ3 . TRP D 1 32  ? 18.177  12.602  6.783   1.00 26.10 ? 32  TRP D CZ3 1 
ATOM   3374 C CH2 . TRP D 1 32  ? 18.688  13.815  7.298   1.00 24.95 ? 32  TRP D CH2 1 
ATOM   3375 N N   . GLY D 1 33  ? 23.537  10.283  3.276   1.00 22.79 ? 33  GLY D N   1 
ATOM   3376 C CA  . GLY D 1 33  ? 24.925  10.598  3.653   1.00 22.38 ? 33  GLY D CA  1 
ATOM   3377 C C   . GLY D 1 33  ? 25.949  10.028  2.678   1.00 23.95 ? 33  GLY D C   1 
ATOM   3378 O O   . GLY D 1 33  ? 25.637  9.756   1.512   1.00 24.04 ? 33  GLY D O   1 
ATOM   3379 N N   . SER D 1 34  ? 27.178  9.850   3.141   1.00 23.94 ? 34  SER D N   1 
ATOM   3380 C CA  . SER D 1 34  ? 28.267  9.403   2.281   1.00 24.53 ? 34  SER D CA  1 
ATOM   3381 C C   . SER D 1 34  ? 29.196  8.405   2.971   1.00 24.48 ? 34  SER D C   1 
ATOM   3382 O O   . SER D 1 34  ? 29.650  8.664   4.085   1.00 24.42 ? 34  SER D O   1 
ATOM   3383 C CB  . SER D 1 34  ? 29.042  10.655  1.815   1.00 24.59 ? 34  SER D CB  1 
ATOM   3384 O OG  . SER D 1 34  ? 29.885  10.403  0.670   1.00 28.56 ? 34  SER D OG  1 
ATOM   3385 N N   . ILE D 1 35  ? 29.440  7.257   2.325   1.00 25.57 ? 35  ILE D N   1 
ATOM   3386 C CA  . ILE D 1 35  ? 30.555  6.342   2.638   1.00 25.70 ? 35  ILE D CA  1 
ATOM   3387 C C   . ILE D 1 35  ? 31.729  6.461   1.624   1.00 26.43 ? 35  ILE D C   1 
ATOM   3388 O O   . ILE D 1 35  ? 31.489  6.459   0.425   1.00 27.19 ? 35  ILE D O   1 
ATOM   3389 C CB  . ILE D 1 35  ? 30.109  4.836   2.677   1.00 25.38 ? 35  ILE D CB  1 
ATOM   3390 C CG1 . ILE D 1 35  ? 28.764  4.684   3.417   1.00 24.85 ? 35  ILE D CG1 1 
ATOM   3391 C CG2 . ILE D 1 35  ? 31.227  3.983   3.266   1.00 24.85 ? 35  ILE D CG2 1 
ATOM   3392 C CD1 . ILE D 1 35  ? 28.048  3.391   3.181   1.00 27.19 ? 35  ILE D CD1 1 
ATOM   3393 N N   . LYS D 1 36  ? 32.983  6.543   2.109   1.00 26.98 ? 36  LYS D N   1 
ATOM   3394 C CA  . LYS D 1 36  ? 34.233  6.374   1.284   1.00 26.23 ? 36  LYS D CA  1 
ATOM   3395 C C   . LYS D 1 36  ? 35.082  5.102   1.578   1.00 24.47 ? 36  LYS D C   1 
ATOM   3396 O O   . LYS D 1 36  ? 34.728  4.277   2.406   1.00 22.10 ? 36  LYS D O   1 
ATOM   3397 C CB  . LYS D 1 36  ? 35.076  7.674   1.215   1.00 27.07 ? 36  LYS D CB  1 
ATOM   3398 C CG  . LYS D 1 36  ? 35.851  8.091   2.481   1.00 29.80 ? 36  LYS D CG  1 
ATOM   3399 C CD  . LYS D 1 36  ? 36.768  9.303   2.170   1.00 28.80 ? 36  LYS D CD  1 
ATOM   3400 C CE  . LYS D 1 36  ? 37.395  9.916   3.438   1.00 31.48 ? 36  LYS D CE  1 
ATOM   3401 N NZ  . LYS D 1 36  ? 38.029  11.276  3.176   1.00 33.25 ? 36  LYS D NZ  1 
ATOM   3402 N N   . GLY D 1 37  ? 36.165  4.918   0.827   1.00 23.79 ? 37  GLY D N   1 
ATOM   3403 C CA  . GLY D 1 37  ? 37.099  3.804   1.057   1.00 23.00 ? 37  GLY D CA  1 
ATOM   3404 C C   . GLY D 1 37  ? 36.534  2.441   0.694   1.00 22.71 ? 37  GLY D C   1 
ATOM   3405 O O   . GLY D 1 37  ? 37.082  1.409   1.052   1.00 21.72 ? 37  GLY D O   1 
ATOM   3406 N N   . LEU D 1 38  ? 35.460  2.451   -0.078  1.00 22.76 ? 38  LEU D N   1 
ATOM   3407 C CA  . LEU D 1 38  ? 34.768  1.229   -0.454  1.00 23.23 ? 38  LEU D CA  1 
ATOM   3408 C C   . LEU D 1 38  ? 35.200  0.743   -1.826  1.00 23.93 ? 38  LEU D C   1 
ATOM   3409 O O   . LEU D 1 38  ? 35.498  1.571   -2.725  1.00 23.36 ? 38  LEU D O   1 
ATOM   3410 C CB  . LEU D 1 38  ? 33.258  1.556   -0.460  1.00 22.74 ? 38  LEU D CB  1 
ATOM   3411 C CG  . LEU D 1 38  ? 32.102  0.843   0.244   1.00 22.03 ? 38  LEU D CG  1 
ATOM   3412 C CD1 . LEU D 1 38  ? 32.372  0.138   1.505   1.00 12.28 ? 38  LEU D CD1 1 
ATOM   3413 C CD2 . LEU D 1 38  ? 30.966  1.867   0.385   1.00 22.31 ? 38  LEU D CD2 1 
ATOM   3414 N N   . THR D 1 39  ? 35.183  -0.589  -2.013  1.00 24.34 ? 39  THR D N   1 
ATOM   3415 C CA  . THR D 1 39  ? 35.275  -1.135  -3.393  1.00 26.51 ? 39  THR D CA  1 
ATOM   3416 C C   . THR D 1 39  ? 34.092  -0.726  -4.317  1.00 26.50 ? 39  THR D C   1 
ATOM   3417 O O   . THR D 1 39  ? 32.967  -0.542  -3.863  1.00 26.41 ? 39  THR D O   1 
ATOM   3418 C CB  . THR D 1 39  ? 35.468  -2.684  -3.458  1.00 25.32 ? 39  THR D CB  1 
ATOM   3419 O OG1 . THR D 1 39  ? 34.440  -3.339  -2.718  1.00 27.27 ? 39  THR D OG1 1 
ATOM   3420 C CG2 . THR D 1 39  ? 36.852  -3.084  -2.905  1.00 27.73 ? 39  THR D CG2 1 
ATOM   3421 N N   . GLU D 1 40  ? 34.358  -0.596  -5.613  1.00 27.73 ? 40  GLU D N   1 
ATOM   3422 C CA  . GLU D 1 40  ? 33.292  -0.283  -6.576  1.00 28.29 ? 40  GLU D CA  1 
ATOM   3423 C C   . GLU D 1 40  ? 32.286  -1.429  -6.696  1.00 27.31 ? 40  GLU D C   1 
ATOM   3424 O O   . GLU D 1 40  ? 32.620  -2.637  -6.623  1.00 27.72 ? 40  GLU D O   1 
ATOM   3425 C CB  . GLU D 1 40  ? 33.838  0.163   -7.939  1.00 28.86 ? 40  GLU D CB  1 
ATOM   3426 C CG  . GLU D 1 40  ? 32.762  0.737   -8.896  1.00 29.83 ? 40  GLU D CG  1 
ATOM   3427 C CD  . GLU D 1 40  ? 33.209  0.742   -10.357 1.00 30.02 ? 40  GLU D CD  1 
ATOM   3428 O OE1 . GLU D 1 40  ? 33.604  -0.319  -10.865 1.00 27.52 ? 40  GLU D OE1 1 
ATOM   3429 O OE2 . GLU D 1 40  ? 33.136  1.813   -10.987 1.00 34.72 ? 40  GLU D OE2 1 
ATOM   3430 N N   . GLY D 1 41  ? 31.028  -1.033  -6.827  1.00 26.60 ? 41  GLY D N   1 
ATOM   3431 C CA  . GLY D 1 41  ? 29.932  -1.989  -6.669  1.00 24.34 ? 41  GLY D CA  1 
ATOM   3432 C C   . GLY D 1 41  ? 29.074  -1.788  -5.432  1.00 23.82 ? 41  GLY D C   1 
ATOM   3433 O O   . GLY D 1 41  ? 29.099  -0.714  -4.753  1.00 22.42 ? 41  GLY D O   1 
ATOM   3434 N N   . LEU D 1 42  ? 28.396  -2.879  -5.090  1.00 22.92 ? 42  LEU D N   1 
ATOM   3435 C CA  . LEU D 1 42  ? 27.151  -2.836  -4.323  1.00 22.19 ? 42  LEU D CA  1 
ATOM   3436 C C   . LEU D 1 42  ? 27.363  -3.487  -2.947  1.00 21.59 ? 42  LEU D C   1 
ATOM   3437 O O   . LEU D 1 42  ? 27.734  -4.686  -2.857  1.00 20.18 ? 42  LEU D O   1 
ATOM   3438 C CB  . LEU D 1 42  ? 26.109  -3.652  -5.117  1.00 23.04 ? 42  LEU D CB  1 
ATOM   3439 C CG  . LEU D 1 42  ? 24.641  -3.347  -5.412  1.00 22.60 ? 42  LEU D CG  1 
ATOM   3440 C CD1 . LEU D 1 42  ? 24.452  -1.977  -5.958  1.00 20.70 ? 42  LEU D CD1 1 
ATOM   3441 C CD2 . LEU D 1 42  ? 24.098  -4.376  -6.384  1.00 21.08 ? 42  LEU D CD2 1 
ATOM   3442 N N   . HIS D 1 43  ? 27.129  -2.738  -1.876  1.00 18.80 ? 43  HIS D N   1 
ATOM   3443 C CA  . HIS D 1 43  ? 27.474  -3.288  -0.525  1.00 18.96 ? 43  HIS D CA  1 
ATOM   3444 C C   . HIS D 1 43  ? 26.255  -3.482  0.361   1.00 17.27 ? 43  HIS D C   1 
ATOM   3445 O O   . HIS D 1 43  ? 25.467  -2.578  0.409   1.00 17.17 ? 43  HIS D O   1 
ATOM   3446 C CB  . HIS D 1 43  ? 28.524  -2.374  0.129   1.00 19.56 ? 43  HIS D CB  1 
ATOM   3447 C CG  . HIS D 1 43  ? 29.840  -2.433  -0.572  1.00 21.67 ? 43  HIS D CG  1 
ATOM   3448 N ND1 . HIS D 1 43  ? 30.639  -3.554  -0.523  1.00 20.35 ? 43  HIS D ND1 1 
ATOM   3449 C CD2 . HIS D 1 43  ? 30.446  -1.564  -1.416  1.00 18.99 ? 43  HIS D CD2 1 
ATOM   3450 C CE1 . HIS D 1 43  ? 31.702  -3.358  -1.284  1.00 22.76 ? 43  HIS D CE1 1 
ATOM   3451 N NE2 . HIS D 1 43  ? 31.605  -2.159  -1.840  1.00 21.69 ? 43  HIS D NE2 1 
ATOM   3452 N N   . GLY D 1 44  ? 26.056  -4.666  0.968   1.00 16.57 ? 44  GLY D N   1 
ATOM   3453 C CA  . GLY D 1 44  ? 24.911  -4.914  1.898   1.00 14.90 ? 44  GLY D CA  1 
ATOM   3454 C C   . GLY D 1 44  ? 24.890  -3.825  3.003   1.00 14.69 ? 44  GLY D C   1 
ATOM   3455 O O   . GLY D 1 44  ? 25.956  -3.468  3.531   1.00 12.36 ? 44  GLY D O   1 
ATOM   3456 N N   . PHE D 1 45  ? 23.701  -3.315  3.368   1.00 14.37 ? 45  PHE D N   1 
ATOM   3457 C CA  . PHE D 1 45  ? 23.589  -2.112  4.235   1.00 13.54 ? 45  PHE D CA  1 
ATOM   3458 C C   . PHE D 1 45  ? 22.549  -2.496  5.231   1.00 14.70 ? 45  PHE D C   1 
ATOM   3459 O O   . PHE D 1 45  ? 21.373  -2.536  4.834   1.00 14.87 ? 45  PHE D O   1 
ATOM   3460 C CB  . PHE D 1 45  ? 23.083  -0.912  3.444   1.00 12.47 ? 45  PHE D CB  1 
ATOM   3461 C CG  . PHE D 1 45  ? 23.416  0.436   4.083   1.00 13.63 ? 45  PHE D CG  1 
ATOM   3462 C CD1 . PHE D 1 45  ? 24.644  0.632   4.777   1.00 7.74  ? 45  PHE D CD1 1 
ATOM   3463 C CD2 . PHE D 1 45  ? 22.542  1.507   3.980   1.00 12.53 ? 45  PHE D CD2 1 
ATOM   3464 C CE1 . PHE D 1 45  ? 24.973  1.892   5.327   1.00 15.61 ? 45  PHE D CE1 1 
ATOM   3465 C CE2 . PHE D 1 45  ? 22.877  2.745   4.560   1.00 12.59 ? 45  PHE D CE2 1 
ATOM   3466 C CZ  . PHE D 1 45  ? 24.095  2.922   5.207   1.00 10.77 ? 45  PHE D CZ  1 
ATOM   3467 N N   . HIS D 1 46  ? 22.940  -2.777  6.492   1.00 15.79 ? 46  HIS D N   1 
ATOM   3468 C CA  . HIS D 1 46  ? 21.989  -3.325  7.492   1.00 17.38 ? 46  HIS D CA  1 
ATOM   3469 C C   . HIS D 1 46  ? 22.148  -2.705  8.834   1.00 16.84 ? 46  HIS D C   1 
ATOM   3470 O O   . HIS D 1 46  ? 23.235  -2.290  9.194   1.00 17.37 ? 46  HIS D O   1 
ATOM   3471 C CB  . HIS D 1 46  ? 22.201  -4.816  7.776   1.00 17.19 ? 46  HIS D CB  1 
ATOM   3472 C CG  . HIS D 1 46  ? 21.910  -5.720  6.622   1.00 21.02 ? 46  HIS D CG  1 
ATOM   3473 N ND1 . HIS D 1 46  ? 22.830  -5.966  5.623   1.00 26.33 ? 46  HIS D ND1 1 
ATOM   3474 C CD2 . HIS D 1 46  ? 20.834  -6.490  6.345   1.00 19.78 ? 46  HIS D CD2 1 
ATOM   3475 C CE1 . HIS D 1 46  ? 22.321  -6.831  4.766   1.00 22.76 ? 46  HIS D CE1 1 
ATOM   3476 N NE2 . HIS D 1 46  ? 21.104  -7.145  5.174   1.00 24.50 ? 46  HIS D NE2 1 
ATOM   3477 N N   . VAL D 1 47  ? 21.059  -2.738  9.600   1.00 16.30 ? 47  VAL D N   1 
ATOM   3478 C CA  . VAL D 1 47  ? 21.059  -2.418  11.032  1.00 13.77 ? 47  VAL D CA  1 
ATOM   3479 C C   . VAL D 1 47  ? 21.149  -3.801  11.660  1.00 15.16 ? 47  VAL D C   1 
ATOM   3480 O O   . VAL D 1 47  ? 20.381  -4.690  11.275  1.00 14.45 ? 47  VAL D O   1 
ATOM   3481 C CB  . VAL D 1 47  ? 19.788  -1.626  11.444  1.00 13.86 ? 47  VAL D CB  1 
ATOM   3482 C CG1 . VAL D 1 47  ? 19.871  -1.195  12.888  1.00 9.70  ? 47  VAL D CG1 1 
ATOM   3483 C CG2 . VAL D 1 47  ? 19.680  -0.396  10.580  1.00 12.03 ? 47  VAL D CG2 1 
ATOM   3484 N N   . HIS D 1 48  ? 22.169  -3.985  12.517  1.00 14.60 ? 48  HIS D N   1 
ATOM   3485 C CA  . HIS D 1 48  ? 22.382  -5.224  13.266  1.00 17.03 ? 48  HIS D CA  1 
ATOM   3486 C C   . HIS D 1 48  ? 21.851  -5.078  14.707  1.00 16.39 ? 48  HIS D C   1 
ATOM   3487 O O   . HIS D 1 48  ? 21.612  -3.952  15.154  1.00 16.14 ? 48  HIS D O   1 
ATOM   3488 C CB  . HIS D 1 48  ? 23.860  -5.633  13.138  1.00 17.16 ? 48  HIS D CB  1 
ATOM   3489 C CG  . HIS D 1 48  ? 24.208  -6.174  11.782  1.00 18.31 ? 48  HIS D CG  1 
ATOM   3490 N ND1 . HIS D 1 48  ? 24.441  -7.517  11.550  1.00 20.93 ? 48  HIS D ND1 1 
ATOM   3491 C CD2 . HIS D 1 48  ? 24.330  -5.559  10.581  1.00 17.54 ? 48  HIS D CD2 1 
ATOM   3492 C CE1 . HIS D 1 48  ? 24.683  -7.704  10.259  1.00 20.19 ? 48  HIS D CE1 1 
ATOM   3493 N NE2 . HIS D 1 48  ? 24.610  -6.532  9.652   1.00 19.79 ? 48  HIS D NE2 1 
ATOM   3494 N N   . GLU D 1 49  ? 21.566  -6.190  15.394  1.00 15.97 ? 49  GLU D N   1 
ATOM   3495 C CA  . GLU D 1 49  ? 20.826  -6.106  16.657  1.00 17.91 ? 49  GLU D CA  1 
ATOM   3496 C C   . GLU D 1 49  ? 21.400  -5.185  17.763  1.00 18.91 ? 49  GLU D C   1 
ATOM   3497 O O   . GLU D 1 49  ? 20.635  -4.440  18.384  1.00 21.88 ? 49  GLU D O   1 
ATOM   3498 C CB  . GLU D 1 49  ? 20.547  -7.501  17.247  1.00 16.58 ? 49  GLU D CB  1 
ATOM   3499 C CG  . GLU D 1 49  ? 19.400  -7.449  18.138  1.00 19.87 ? 49  GLU D CG  1 
ATOM   3500 C CD  . GLU D 1 49  ? 18.953  -8.795  18.583  1.00 24.01 ? 49  GLU D CD  1 
ATOM   3501 O OE1 . GLU D 1 49  ? 19.583  -9.794  18.181  1.00 24.48 ? 49  GLU D OE1 1 
ATOM   3502 O OE2 . GLU D 1 49  ? 17.961  -8.869  19.352  1.00 26.79 ? 49  GLU D OE2 1 
ATOM   3503 N N   . PHE D 1 50  ? 22.727  -5.231  18.021  1.00 18.70 ? 50  PHE D N   1 
ATOM   3504 C CA  . PHE D 1 50  ? 23.339  -4.618  19.207  1.00 16.99 ? 50  PHE D CA  1 
ATOM   3505 C C   . PHE D 1 50  ? 24.282  -3.493  18.882  1.00 17.49 ? 50  PHE D C   1 
ATOM   3506 O O   . PHE D 1 50  ? 25.024  -3.554  17.906  1.00 18.39 ? 50  PHE D O   1 
ATOM   3507 C CB  . PHE D 1 50  ? 24.100  -5.670  20.001  1.00 17.31 ? 50  PHE D CB  1 
ATOM   3508 C CG  . PHE D 1 50  ? 23.311  -6.887  20.258  1.00 13.16 ? 50  PHE D CG  1 
ATOM   3509 C CD1 . PHE D 1 50  ? 22.250  -6.838  21.128  1.00 14.69 ? 50  PHE D CD1 1 
ATOM   3510 C CD2 . PHE D 1 50  ? 23.605  -8.072  19.640  1.00 19.42 ? 50  PHE D CD2 1 
ATOM   3511 C CE1 . PHE D 1 50  ? 21.462  -7.966  21.395  1.00 14.04 ? 50  PHE D CE1 1 
ATOM   3512 C CE2 . PHE D 1 50  ? 22.827  -9.249  19.906  1.00 16.14 ? 50  PHE D CE2 1 
ATOM   3513 C CZ  . PHE D 1 50  ? 21.771  -9.183  20.798  1.00 13.77 ? 50  PHE D CZ  1 
ATOM   3514 N N   . GLY D 1 51  ? 24.256  -2.466  19.709  1.00 16.46 ? 51  GLY D N   1 
ATOM   3515 C CA  . GLY D 1 51  ? 25.092  -1.324  19.497  1.00 16.95 ? 51  GLY D CA  1 
ATOM   3516 C C   . GLY D 1 51  ? 26.373  -1.543  20.271  1.00 18.33 ? 51  GLY D C   1 
ATOM   3517 O O   . GLY D 1 51  ? 26.832  -0.658  20.971  1.00 16.80 ? 51  GLY D O   1 
ATOM   3518 N N   . ASP D 1 52  ? 26.908  -2.757  20.142  1.00 19.19 ? 52  ASP D N   1 
ATOM   3519 C CA  . ASP D 1 52  ? 28.069  -3.240  20.830  1.00 21.48 ? 52  ASP D CA  1 
ATOM   3520 C C   . ASP D 1 52  ? 29.234  -3.168  19.815  1.00 22.83 ? 52  ASP D C   1 
ATOM   3521 O O   . ASP D 1 52  ? 29.268  -3.911  18.824  1.00 24.13 ? 52  ASP D O   1 
ATOM   3522 C CB  . ASP D 1 52  ? 27.790  -4.698  21.259  1.00 20.96 ? 52  ASP D CB  1 
ATOM   3523 C CG  . ASP D 1 52  ? 28.815  -5.258  22.260  1.00 21.72 ? 52  ASP D CG  1 
ATOM   3524 O OD1 . ASP D 1 52  ? 30.009  -4.938  22.175  1.00 23.30 ? 52  ASP D OD1 1 
ATOM   3525 O OD2 . ASP D 1 52  ? 28.405  -6.057  23.122  1.00 20.11 ? 52  ASP D OD2 1 
ATOM   3526 N N   . ASN D 1 53  ? 30.183  -2.283  20.050  1.00 23.48 ? 53  ASN D N   1 
ATOM   3527 C CA  . ASN D 1 53  ? 31.391  -2.295  19.228  1.00 24.56 ? 53  ASN D CA  1 
ATOM   3528 C C   . ASN D 1 53  ? 32.621  -2.960  19.834  1.00 24.95 ? 53  ASN D C   1 
ATOM   3529 O O   . ASN D 1 53  ? 33.751  -2.634  19.411  1.00 26.38 ? 53  ASN D O   1 
ATOM   3530 C CB  . ASN D 1 53  ? 31.769  -0.852  18.837  1.00 24.65 ? 53  ASN D CB  1 
ATOM   3531 C CG  . ASN D 1 53  ? 33.015  -0.793  17.947  1.00 26.46 ? 53  ASN D CG  1 
ATOM   3532 O OD1 . ASN D 1 53  ? 32.994  -1.323  16.851  1.00 32.00 ? 53  ASN D OD1 1 
ATOM   3533 N ND2 . ASN D 1 53  ? 34.096  -0.183  18.428  1.00 26.00 ? 53  ASN D ND2 1 
ATOM   3534 N N   . THR D 1 54  ? 32.445  -3.858  20.800  1.00 25.24 ? 54  THR D N   1 
ATOM   3535 C CA  . THR D 1 54  ? 33.568  -4.183  21.687  1.00 26.68 ? 54  THR D CA  1 
ATOM   3536 C C   . THR D 1 54  ? 34.602  -5.132  21.101  1.00 26.22 ? 54  THR D C   1 
ATOM   3537 O O   . THR D 1 54  ? 35.727  -5.192  21.558  1.00 25.15 ? 54  THR D O   1 
ATOM   3538 C CB  . THR D 1 54  ? 33.138  -4.748  23.081  1.00 26.11 ? 54  THR D CB  1 
ATOM   3539 O OG1 . THR D 1 54  ? 32.319  -5.906  22.886  1.00 29.26 ? 54  THR D OG1 1 
ATOM   3540 C CG2 . THR D 1 54  ? 32.423  -3.699  23.903  1.00 24.87 ? 54  THR D CG2 1 
ATOM   3541 N N   . ALA D 1 55  ? 34.199  -5.902  20.118  1.00 27.12 ? 55  ALA D N   1 
ATOM   3542 C CA  . ALA D 1 55  ? 35.144  -6.783  19.452  1.00 27.17 ? 55  ALA D CA  1 
ATOM   3543 C C   . ALA D 1 55  ? 35.138  -6.436  17.976  1.00 27.21 ? 55  ALA D C   1 
ATOM   3544 O O   . ALA D 1 55  ? 35.351  -7.293  17.134  1.00 27.88 ? 55  ALA D O   1 
ATOM   3545 C CB  . ALA D 1 55  ? 34.780  -8.266  19.695  1.00 28.08 ? 55  ALA D CB  1 
ATOM   3546 N N   . GLY D 1 56  ? 34.896  -5.157  17.677  1.00 26.08 ? 56  GLY D N   1 
ATOM   3547 C CA  . GLY D 1 56  ? 34.654  -4.701  16.308  1.00 25.68 ? 56  GLY D CA  1 
ATOM   3548 C C   . GLY D 1 56  ? 33.210  -4.846  15.863  1.00 24.93 ? 56  GLY D C   1 
ATOM   3549 O O   . GLY D 1 56  ? 32.274  -4.752  16.664  1.00 25.41 ? 56  GLY D O   1 
ATOM   3550 N N   . CYS D 1 57  ? 33.023  -5.102  14.570  1.00 24.23 ? 57  CYS D N   1 
ATOM   3551 C CA  . CYS D 1 57  ? 31.683  -5.113  13.998  1.00 22.92 ? 57  CYS D CA  1 
ATOM   3552 C C   . CYS D 1 57  ? 31.011  -6.446  14.251  1.00 22.26 ? 57  CYS D C   1 
ATOM   3553 O O   . CYS D 1 57  ? 29.814  -6.551  14.038  1.00 22.95 ? 57  CYS D O   1 
ATOM   3554 C CB  . CYS D 1 57  ? 31.705  -4.765  12.520  1.00 21.83 ? 57  CYS D CB  1 
ATOM   3555 S SG  . CYS D 1 57  ? 32.229  -3.066  12.190  1.00 22.83 ? 57  CYS D SG  1 
ATOM   3556 N N   . THR D 1 58  ? 31.759  -7.435  14.753  1.00 21.72 ? 58  THR D N   1 
ATOM   3557 C CA  . THR D 1 58  ? 31.196  -8.802  15.002  1.00 21.27 ? 58  THR D CA  1 
ATOM   3558 C C   . THR D 1 58  ? 30.284  -8.809  16.201  1.00 20.95 ? 58  THR D C   1 
ATOM   3559 O O   . THR D 1 58  ? 29.384  -9.673  16.325  1.00 22.26 ? 58  THR D O   1 
ATOM   3560 C CB  . THR D 1 58  ? 32.305  -9.862  15.255  1.00 21.12 ? 58  THR D CB  1 
ATOM   3561 O OG1 . THR D 1 58  ? 33.438  -9.571  14.458  1.00 24.16 ? 58  THR D OG1 1 
ATOM   3562 C CG2 . THR D 1 58  ? 31.826  -11.376 14.985  1.00 20.98 ? 58  THR D CG2 1 
ATOM   3563 N N   . SER D 1 59  ? 30.517  -7.842  17.101  1.00 20.20 ? 59  SER D N   1 
ATOM   3564 C CA  . SER D 1 59  ? 29.826  -7.835  18.391  1.00 19.87 ? 59  SER D CA  1 
ATOM   3565 C C   . SER D 1 59  ? 28.384  -7.213  18.398  1.00 19.04 ? 59  SER D C   1 
ATOM   3566 O O   . SER D 1 59  ? 27.601  -7.432  19.346  1.00 17.70 ? 59  SER D O   1 
ATOM   3567 C CB  . SER D 1 59  ? 30.771  -7.338  19.492  1.00 19.29 ? 59  SER D CB  1 
ATOM   3568 O OG  . SER D 1 59  ? 31.363  -6.128  19.077  1.00 24.01 ? 59  SER D OG  1 
ATOM   3569 N N   . ALA D 1 60  ? 28.090  -6.482  17.315  1.00 17.98 ? 60  ALA D N   1 
ATOM   3570 C CA  . ALA D 1 60  ? 26.755  -6.032  16.853  1.00 17.34 ? 60  ALA D CA  1 
ATOM   3571 C C   . ALA D 1 60  ? 25.788  -7.109  16.651  1.00 17.37 ? 60  ALA D C   1 
ATOM   3572 O O   . ALA D 1 60  ? 24.607  -6.809  16.600  1.00 16.69 ? 60  ALA D O   1 
ATOM   3573 C CB  . ALA D 1 60  ? 26.871  -5.301  15.511  1.00 17.40 ? 60  ALA D CB  1 
ATOM   3574 N N   . GLY D 1 61  ? 26.235  -8.349  16.457  1.00 18.03 ? 61  GLY D N   1 
ATOM   3575 C CA  . GLY D 1 61  ? 25.274  -9.471  16.359  1.00 19.03 ? 61  GLY D CA  1 
ATOM   3576 C C   . GLY D 1 61  ? 24.551  -9.669  15.013  1.00 19.92 ? 61  GLY D C   1 
ATOM   3577 O O   . GLY D 1 61  ? 25.100  -9.379  13.956  1.00 19.88 ? 61  GLY D O   1 
ATOM   3578 N N   . PRO D 1 62  ? 23.313  -10.221 15.015  1.00 21.24 ? 62  PRO D N   1 
ATOM   3579 C CA  . PRO D 1 62  ? 22.770  -10.402 13.697  1.00 20.88 ? 62  PRO D CA  1 
ATOM   3580 C C   . PRO D 1 62  ? 21.918  -9.240  13.252  1.00 20.65 ? 62  PRO D C   1 
ATOM   3581 O O   . PRO D 1 62  ? 21.886  -8.182  13.914  1.00 19.94 ? 62  PRO D O   1 
ATOM   3582 C CB  . PRO D 1 62  ? 21.975  -11.689 13.834  1.00 21.22 ? 62  PRO D CB  1 
ATOM   3583 C CG  . PRO D 1 62  ? 21.498  -11.680 15.256  1.00 22.59 ? 62  PRO D CG  1 
ATOM   3584 C CD  . PRO D 1 62  ? 22.410  -10.744 16.038  1.00 22.11 ? 62  PRO D CD  1 
ATOM   3585 N N   . HIS D 1 63  ? 21.239  -9.453  12.120  1.00 20.71 ? 63  HIS D N   1 
ATOM   3586 C CA  . HIS D 1 63  ? 20.278  -8.489  11.568  1.00 19.99 ? 63  HIS D CA  1 
ATOM   3587 C C   . HIS D 1 63  ? 19.216  -8.183  12.547  1.00 19.38 ? 63  HIS D C   1 
ATOM   3588 O O   . HIS D 1 63  ? 18.590  -9.063  13.139  1.00 18.22 ? 63  HIS D O   1 
ATOM   3589 C CB  . HIS D 1 63  ? 19.595  -8.953  10.284  1.00 20.66 ? 63  HIS D CB  1 
ATOM   3590 C CG  . HIS D 1 63  ? 20.515  -9.144  9.121   1.00 23.33 ? 63  HIS D CG  1 
ATOM   3591 N ND1 . HIS D 1 63  ? 20.258  -10.062 8.128   1.00 22.56 ? 63  HIS D ND1 1 
ATOM   3592 C CD2 . HIS D 1 63  ? 21.677  -8.537  8.785   1.00 23.67 ? 63  HIS D CD2 1 
ATOM   3593 C CE1 . HIS D 1 63  ? 21.240  -10.030 7.246   1.00 26.37 ? 63  HIS D CE1 1 
ATOM   3594 N NE2 . HIS D 1 63  ? 22.113  -9.114  7.623   1.00 24.30 ? 63  HIS D NE2 1 
ATOM   3595 N N   . PHE D 1 64  ? 18.974  -6.896  12.683  1.00 19.13 ? 64  PHE D N   1 
ATOM   3596 C CA  . PHE D 1 64  ? 17.916  -6.473  13.559  1.00 19.65 ? 64  PHE D CA  1 
ATOM   3597 C C   . PHE D 1 64  ? 16.603  -7.048  13.030  1.00 21.50 ? 64  PHE D C   1 
ATOM   3598 O O   . PHE D 1 64  ? 16.154  -6.753  11.935  1.00 20.47 ? 64  PHE D O   1 
ATOM   3599 C CB  . PHE D 1 64  ? 17.902  -4.939  13.722  1.00 19.31 ? 64  PHE D CB  1 
ATOM   3600 C CG  . PHE D 1 64  ? 16.809  -4.460  14.613  1.00 18.11 ? 64  PHE D CG  1 
ATOM   3601 C CD1 . PHE D 1 64  ? 16.506  -5.157  15.787  1.00 12.66 ? 64  PHE D CD1 1 
ATOM   3602 C CD2 . PHE D 1 64  ? 16.084  -3.311  14.307  1.00 21.11 ? 64  PHE D CD2 1 
ATOM   3603 C CE1 . PHE D 1 64  ? 15.463  -4.735  16.635  1.00 14.04 ? 64  PHE D CE1 1 
ATOM   3604 C CE2 . PHE D 1 64  ? 15.033  -2.876  15.179  1.00 18.93 ? 64  PHE D CE2 1 
ATOM   3605 C CZ  . PHE D 1 64  ? 14.750  -3.563  16.326  1.00 15.72 ? 64  PHE D CZ  1 
ATOM   3606 N N   . ASN D 1 65  ? 16.038  -7.961  13.804  1.00 24.98 ? 65  ASN D N   1 
ATOM   3607 C CA  . ASN D 1 65  ? 14.828  -8.658  13.405  1.00 27.46 ? 65  ASN D CA  1 
ATOM   3608 C C   . ASN D 1 65  ? 14.023  -9.001  14.663  1.00 28.77 ? 65  ASN D C   1 
ATOM   3609 O O   . ASN D 1 65  ? 14.198  -10.109 15.203  1.00 30.42 ? 65  ASN D O   1 
ATOM   3610 C CB  . ASN D 1 65  ? 15.198  -9.949  12.644  1.00 27.88 ? 65  ASN D CB  1 
ATOM   3611 C CG  . ASN D 1 65  ? 14.019  -10.554 11.925  1.00 29.55 ? 65  ASN D CG  1 
ATOM   3612 O OD1 . ASN D 1 65  ? 13.286  -9.854  11.216  1.00 30.57 ? 65  ASN D OD1 1 
ATOM   3613 N ND2 . ASN D 1 65  ? 13.840  -11.874 12.078  1.00 28.91 ? 65  ASN D ND2 1 
ATOM   3614 N N   . PRO D 1 66  ? 13.149  -8.070  15.125  1.00 28.72 ? 66  PRO D N   1 
ATOM   3615 C CA  . PRO D 1 66  ? 12.463  -8.132  16.416  1.00 29.45 ? 66  PRO D CA  1 
ATOM   3616 C C   . PRO D 1 66  ? 11.333  -9.185  16.508  1.00 31.02 ? 66  PRO D C   1 
ATOM   3617 O O   . PRO D 1 66  ? 11.277  -9.957  17.501  1.00 32.50 ? 66  PRO D O   1 
ATOM   3618 C CB  . PRO D 1 66  ? 11.882  -6.732  16.560  1.00 28.84 ? 66  PRO D CB  1 
ATOM   3619 C CG  . PRO D 1 66  ? 12.365  -5.947  15.392  1.00 28.00 ? 66  PRO D CG  1 
ATOM   3620 C CD  . PRO D 1 66  ? 12.733  -6.887  14.357  1.00 27.93 ? 66  PRO D CD  1 
ATOM   3621 N N   . HIS D 1 80  ? 13.860  -8.913  7.072   1.00 27.72 ? 80  HIS D N   1 
ATOM   3622 C CA  . HIS D 1 80  ? 14.230  -8.392  8.390   1.00 28.85 ? 80  HIS D CA  1 
ATOM   3623 C C   . HIS D 1 80  ? 14.074  -6.862  8.443   1.00 28.21 ? 80  HIS D C   1 
ATOM   3624 O O   . HIS D 1 80  ? 14.268  -6.169  7.456   1.00 28.46 ? 80  HIS D O   1 
ATOM   3625 C CB  . HIS D 1 80  ? 15.696  -8.671  8.819   1.00 29.25 ? 80  HIS D CB  1 
ATOM   3626 C CG  . HIS D 1 80  ? 16.220  -10.038 8.513   1.00 33.56 ? 80  HIS D CG  1 
ATOM   3627 N ND1 . HIS D 1 80  ? 15.552  -11.197 8.852   1.00 39.25 ? 80  HIS D ND1 1 
ATOM   3628 C CD2 . HIS D 1 80  ? 17.396  -10.433 7.961   1.00 36.31 ? 80  HIS D CD2 1 
ATOM   3629 C CE1 . HIS D 1 80  ? 16.273  -12.245 8.481   1.00 38.28 ? 80  HIS D CE1 1 
ATOM   3630 N NE2 . HIS D 1 80  ? 17.404  -11.808 7.956   1.00 37.51 ? 80  HIS D NE2 1 
ATOM   3631 N N   . VAL D 1 81  ? 13.818  -6.350  9.642   1.00 27.76 ? 81  VAL D N   1 
ATOM   3632 C CA  . VAL D 1 81  ? 13.606  -4.918  9.880   1.00 26.17 ? 81  VAL D CA  1 
ATOM   3633 C C   . VAL D 1 81  ? 14.846  -4.042  9.489   1.00 26.78 ? 81  VAL D C   1 
ATOM   3634 O O   . VAL D 1 81  ? 14.716  -2.928  8.906   1.00 27.55 ? 81  VAL D O   1 
ATOM   3635 C CB  . VAL D 1 81  ? 13.116  -4.676  11.377  1.00 25.72 ? 81  VAL D CB  1 
ATOM   3636 C CG1 . VAL D 1 81  ? 12.967  -3.181  11.699  1.00 23.44 ? 81  VAL D CG1 1 
ATOM   3637 C CG2 . VAL D 1 81  ? 11.832  -5.474  11.675  1.00 21.56 ? 81  VAL D CG2 1 
ATOM   3638 N N   . GLY D 1 82  ? 16.037  -4.516  9.814   1.00 25.34 ? 82  GLY D N   1 
ATOM   3639 C CA  . GLY D 1 82  ? 17.226  -3.731  9.508   1.00 24.93 ? 82  GLY D CA  1 
ATOM   3640 C C   . GLY D 1 82  ? 17.730  -3.680  8.064   1.00 24.36 ? 82  GLY D C   1 
ATOM   3641 O O   . GLY D 1 82  ? 18.711  -3.004  7.773   1.00 23.55 ? 82  GLY D O   1 
ATOM   3642 N N   . ASP D 1 83  ? 17.043  -4.373  7.167   1.00 23.74 ? 83  ASP D N   1 
ATOM   3643 C CA  . ASP D 1 83  ? 17.512  -4.663  5.809   1.00 24.34 ? 83  ASP D CA  1 
ATOM   3644 C C   . ASP D 1 83  ? 17.429  -3.490  4.868   1.00 23.37 ? 83  ASP D C   1 
ATOM   3645 O O   . ASP D 1 83  ? 16.410  -3.336  4.220   1.00 23.15 ? 83  ASP D O   1 
ATOM   3646 C CB  . ASP D 1 83  ? 16.644  -5.809  5.228   1.00 24.82 ? 83  ASP D CB  1 
ATOM   3647 C CG  . ASP D 1 83  ? 17.330  -6.567  4.114   1.00 27.60 ? 83  ASP D CG  1 
ATOM   3648 O OD1 . ASP D 1 83  ? 17.106  -7.811  4.025   1.00 28.03 ? 83  ASP D OD1 1 
ATOM   3649 O OD2 . ASP D 1 83  ? 18.112  -5.927  3.351   1.00 32.27 ? 83  ASP D OD2 1 
ATOM   3650 N N   . LEU D 1 84  ? 18.499  -2.705  4.712   1.00 21.63 ? 84  LEU D N   1 
ATOM   3651 C CA  . LEU D 1 84  ? 18.339  -1.437  4.009   1.00 20.03 ? 84  LEU D CA  1 
ATOM   3652 C C   . LEU D 1 84  ? 18.751  -1.512  2.559   1.00 19.63 ? 84  LEU D C   1 
ATOM   3653 O O   . LEU D 1 84  ? 18.925  -0.494  1.890   1.00 20.90 ? 84  LEU D O   1 
ATOM   3654 C CB  . LEU D 1 84  ? 19.004  -0.282  4.754   1.00 18.71 ? 84  LEU D CB  1 
ATOM   3655 C CG  . LEU D 1 84  ? 18.535  0.004   6.187   1.00 15.68 ? 84  LEU D CG  1 
ATOM   3656 C CD1 . LEU D 1 84  ? 19.441  1.017   6.793   1.00 12.72 ? 84  LEU D CD1 1 
ATOM   3657 C CD2 . LEU D 1 84  ? 17.087  0.484   6.084   1.00 10.69 ? 84  LEU D CD2 1 
ATOM   3658 N N   . GLY D 1 85  ? 18.847  -2.718  2.028   1.00 19.47 ? 85  GLY D N   1 
ATOM   3659 C CA  . GLY D 1 85  ? 19.310  -2.867  0.650   1.00 18.73 ? 85  GLY D CA  1 
ATOM   3660 C C   . GLY D 1 85  ? 20.832  -2.928  0.532   1.00 18.30 ? 85  GLY D C   1 
ATOM   3661 O O   . GLY D 1 85  ? 21.487  -3.730  1.195   1.00 19.53 ? 85  GLY D O   1 
ATOM   3662 N N   . ASN D 1 86  ? 21.388  -2.074  -0.312  1.00 18.19 ? 86  ASN D N   1 
ATOM   3663 C CA  . ASN D 1 86  ? 22.792  -2.093  -0.666  1.00 16.94 ? 86  ASN D CA  1 
ATOM   3664 C C   . ASN D 1 86  ? 23.078  -0.640  -0.790  1.00 17.62 ? 86  ASN D C   1 
ATOM   3665 O O   . ASN D 1 86  ? 22.149  0.154   -1.004  1.00 17.55 ? 86  ASN D O   1 
ATOM   3666 C CB  . ASN D 1 86  ? 22.977  -2.680  -2.034  1.00 17.61 ? 86  ASN D CB  1 
ATOM   3667 C CG  . ASN D 1 86  ? 22.960  -4.208  -2.022  1.00 18.20 ? 86  ASN D CG  1 
ATOM   3668 O OD1 . ASN D 1 86  ? 23.713  -4.791  -1.309  1.00 24.22 ? 86  ASN D OD1 1 
ATOM   3669 N ND2 . ASN D 1 86  ? 22.067  -4.845  -2.811  1.00 18.81 ? 86  ASN D ND2 1 
ATOM   3670 N N   . VAL D 1 87  ? 24.321  -0.253  -0.564  1.00 16.72 ? 87  VAL D N   1 
ATOM   3671 C CA  . VAL D 1 87  ? 24.735  1.042   -1.051  1.00 15.29 ? 87  VAL D CA  1 
ATOM   3672 C C   . VAL D 1 87  ? 25.657  0.773   -2.285  1.00 13.84 ? 87  VAL D C   1 
ATOM   3673 O O   . VAL D 1 87  ? 26.114  -0.376  -2.488  1.00 9.95  ? 87  VAL D O   1 
ATOM   3674 C CB  . VAL D 1 87  ? 25.342  1.902   0.071   1.00 16.93 ? 87  VAL D CB  1 
ATOM   3675 C CG1 . VAL D 1 87  ? 24.240  2.349   1.010   1.00 12.77 ? 87  VAL D CG1 1 
ATOM   3676 C CG2 . VAL D 1 87  ? 26.523  1.197   0.807   1.00 13.89 ? 87  VAL D CG2 1 
ATOM   3677 N N   . THR D 1 88  ? 25.893  1.772   -3.123  1.00 10.65 ? 88  THR D N   1 
ATOM   3678 C CA  . THR D 1 88  ? 26.690  1.541   -4.302  1.00 12.30 ? 88  THR D CA  1 
ATOM   3679 C C   . THR D 1 88  ? 27.880  2.469   -4.333  1.00 14.04 ? 88  THR D C   1 
ATOM   3680 O O   . THR D 1 88  ? 27.688  3.688   -4.429  1.00 12.29 ? 88  THR D O   1 
ATOM   3681 C CB  . THR D 1 88  ? 25.922  1.733   -5.640  1.00 11.77 ? 88  THR D CB  1 
ATOM   3682 O OG1 . THR D 1 88  ? 24.724  0.925   -5.662  1.00 15.52 ? 88  THR D OG1 1 
ATOM   3683 C CG2 . THR D 1 88  ? 26.781  1.225   -6.777  1.00 12.65 ? 88  THR D CG2 1 
ATOM   3684 N N   . ALA D 1 89  ? 29.080  1.888   -4.337  1.00 14.15 ? 89  ALA D N   1 
ATOM   3685 C CA  . ALA D 1 89  ? 30.291  2.679   -4.543  1.00 16.56 ? 89  ALA D CA  1 
ATOM   3686 C C   . ALA D 1 89  ? 30.651  2.854   -5.996  1.00 17.74 ? 89  ALA D C   1 
ATOM   3687 O O   . ALA D 1 89  ? 30.811  1.907   -6.726  1.00 20.24 ? 89  ALA D O   1 
ATOM   3688 C CB  . ALA D 1 89  ? 31.435  2.097   -3.730  1.00 15.97 ? 89  ALA D CB  1 
ATOM   3689 N N   . ASP D 1 90  ? 30.732  4.099   -6.411  1.00 20.47 ? 90  ASP D N   1 
ATOM   3690 C CA  . ASP D 1 90  ? 31.194  4.508   -7.720  1.00 21.84 ? 90  ASP D CA  1 
ATOM   3691 C C   . ASP D 1 90  ? 32.649  4.113   -7.866  1.00 23.66 ? 90  ASP D C   1 
ATOM   3692 O O   . ASP D 1 90  ? 33.259  3.651   -6.892  1.00 23.79 ? 90  ASP D O   1 
ATOM   3693 C CB  . ASP D 1 90  ? 31.130  6.032   -7.807  1.00 20.14 ? 90  ASP D CB  1 
ATOM   3694 C CG  . ASP D 1 90  ? 32.228  6.683   -7.013  1.00 22.75 ? 90  ASP D CG  1 
ATOM   3695 O OD1 . ASP D 1 90  ? 33.103  5.921   -6.592  1.00 19.99 ? 90  ASP D OD1 1 
ATOM   3696 O OD2 . ASP D 1 90  ? 32.270  7.921   -6.781  1.00 17.00 ? 90  ASP D OD2 1 
ATOM   3697 N N   . LYS D 1 91  ? 33.214  4.372   -9.058  1.00 25.98 ? 91  LYS D N   1 
ATOM   3698 C CA  . LYS D 1 91  ? 34.619  4.096   -9.427  1.00 28.20 ? 91  LYS D CA  1 
ATOM   3699 C C   . LYS D 1 91  ? 35.709  4.552   -8.477  1.00 28.76 ? 91  LYS D C   1 
ATOM   3700 O O   . LYS D 1 91  ? 36.744  3.892   -8.378  1.00 29.39 ? 91  LYS D O   1 
ATOM   3701 C CB  . LYS D 1 91  ? 34.933  4.645   -10.837 1.00 28.19 ? 91  LYS D CB  1 
ATOM   3702 C CG  . LYS D 1 91  ? 35.005  6.169   -10.997 1.00 29.58 ? 91  LYS D CG  1 
ATOM   3703 C CD  . LYS D 1 91  ? 35.438  6.533   -12.442 1.00 30.32 ? 91  LYS D CD  1 
ATOM   3704 C CE  . LYS D 1 91  ? 36.522  5.529   -12.975 1.00 32.81 ? 91  LYS D CE  1 
ATOM   3705 N NZ  . LYS D 1 91  ? 37.338  6.002   -14.165 1.00 33.27 ? 91  LYS D NZ  1 
ATOM   3706 N N   . ASP D 1 92  ? 35.503  5.703   -7.835  1.00 29.15 ? 92  ASP D N   1 
ATOM   3707 C CA  . ASP D 1 92  ? 36.431  6.249   -6.873  1.00 28.89 ? 92  ASP D CA  1 
ATOM   3708 C C   . ASP D 1 92  ? 36.203  5.638   -5.449  1.00 28.88 ? 92  ASP D C   1 
ATOM   3709 O O   . ASP D 1 92  ? 36.810  6.112   -4.475  1.00 28.77 ? 92  ASP D O   1 
ATOM   3710 C CB  . ASP D 1 92  ? 36.304  7.801   -6.853  1.00 29.61 ? 92  ASP D CB  1 
ATOM   3711 C CG  . ASP D 1 92  ? 36.794  8.491   -8.165  1.00 32.34 ? 92  ASP D CG  1 
ATOM   3712 O OD1 . ASP D 1 92  ? 37.741  8.016   -8.862  1.00 32.48 ? 92  ASP D OD1 1 
ATOM   3713 O OD2 . ASP D 1 92  ? 36.244  9.584   -8.477  1.00 35.75 ? 92  ASP D OD2 1 
ATOM   3714 N N   . GLY D 1 93  ? 35.379  4.577   -5.316  1.00 28.10 ? 93  GLY D N   1 
ATOM   3715 C CA  . GLY D 1 93  ? 35.018  4.005   -3.994  1.00 27.44 ? 93  GLY D CA  1 
ATOM   3716 C C   . GLY D 1 93  ? 33.990  4.736   -3.112  1.00 27.11 ? 93  GLY D C   1 
ATOM   3717 O O   . GLY D 1 93  ? 33.669  4.273   -2.043  1.00 27.41 ? 93  GLY D O   1 
ATOM   3718 N N   . VAL D 1 94  ? 33.474  5.877   -3.568  1.00 26.80 ? 94  VAL D N   1 
ATOM   3719 C CA  . VAL D 1 94  ? 32.479  6.674   -2.837  1.00 25.72 ? 94  VAL D CA  1 
ATOM   3720 C C   . VAL D 1 94  ? 31.014  6.234   -3.108  1.00 26.01 ? 94  VAL D C   1 
ATOM   3721 O O   . VAL D 1 94  ? 30.553  6.260   -4.240  1.00 25.65 ? 94  VAL D O   1 
ATOM   3722 C CB  . VAL D 1 94  ? 32.623  8.174   -3.149  1.00 25.22 ? 94  VAL D CB  1 
ATOM   3723 C CG1 . VAL D 1 94  ? 31.601  8.964   -2.406  1.00 24.32 ? 94  VAL D CG1 1 
ATOM   3724 C CG2 . VAL D 1 94  ? 34.026  8.675   -2.772  1.00 24.67 ? 94  VAL D CG2 1 
ATOM   3725 N N   . ALA D 1 95  ? 30.318  5.823   -2.039  1.00 26.76 ? 95  ALA D N   1 
ATOM   3726 C CA  . ALA D 1 95  ? 28.840  5.686   -1.990  1.00 27.52 ? 95  ALA D CA  1 
ATOM   3727 C C   . ALA D 1 95  ? 28.138  6.984   -1.515  1.00 28.19 ? 95  ALA D C   1 
ATOM   3728 O O   . ALA D 1 95  ? 28.436  7.506   -0.432  1.00 29.04 ? 95  ALA D O   1 
ATOM   3729 C CB  . ALA D 1 95  ? 28.442  4.514   -1.111  1.00 27.06 ? 95  ALA D CB  1 
ATOM   3730 N N   . ASP D 1 96  ? 27.262  7.549   -2.349  1.00 27.62 ? 96  ASP D N   1 
ATOM   3731 C CA  . ASP D 1 96  ? 26.426  8.614   -1.895  1.00 28.14 ? 96  ASP D CA  1 
ATOM   3732 C C   . ASP D 1 96  ? 25.013  8.061   -1.718  1.00 26.87 ? 96  ASP D C   1 
ATOM   3733 O O   . ASP D 1 96  ? 24.257  7.864   -2.684  1.00 25.98 ? 96  ASP D O   1 
ATOM   3734 C CB  . ASP D 1 96  ? 26.505  9.845   -2.791  1.00 28.94 ? 96  ASP D CB  1 
ATOM   3735 C CG  . ASP D 1 96  ? 27.467  10.899  -2.210  1.00 34.90 ? 96  ASP D CG  1 
ATOM   3736 O OD1 . ASP D 1 96  ? 28.628  11.060  -2.708  1.00 39.30 ? 96  ASP D OD1 1 
ATOM   3737 O OD2 . ASP D 1 96  ? 27.069  11.534  -1.201  1.00 38.51 ? 96  ASP D OD2 1 
ATOM   3738 N N   . VAL D 1 97  ? 24.695  7.857   -0.436  1.00 24.95 ? 97  VAL D N   1 
ATOM   3739 C CA  . VAL D 1 97  ? 23.525  7.153   0.029   1.00 22.99 ? 97  VAL D CA  1 
ATOM   3740 C C   . VAL D 1 97  ? 22.319  8.071   0.144   1.00 23.67 ? 97  VAL D C   1 
ATOM   3741 O O   . VAL D 1 97  ? 22.386  9.142   0.769   1.00 23.23 ? 97  VAL D O   1 
ATOM   3742 C CB  . VAL D 1 97  ? 23.819  6.438   1.389   1.00 21.72 ? 97  VAL D CB  1 
ATOM   3743 C CG1 . VAL D 1 97  ? 22.625  5.846   1.889   1.00 15.46 ? 97  VAL D CG1 1 
ATOM   3744 C CG2 . VAL D 1 97  ? 24.856  5.387   1.190   1.00 20.10 ? 97  VAL D CG2 1 
ATOM   3745 N N   . SER D 1 98  ? 21.248  7.666   -0.539  1.00 24.89 ? 98  SER D N   1 
ATOM   3746 C CA  . SER D 1 98  ? 19.920  8.272   -0.421  1.00 25.76 ? 98  SER D CA  1 
ATOM   3747 C C   . SER D 1 98  ? 18.887  7.168   -0.467  1.00 26.14 ? 98  SER D C   1 
ATOM   3748 O O   . SER D 1 98  ? 18.609  6.659   -1.545  1.00 27.52 ? 98  SER D O   1 
ATOM   3749 C CB  . SER D 1 98  ? 19.675  9.295   -1.513  1.00 25.79 ? 98  SER D CB  1 
ATOM   3750 O OG  . SER D 1 98  ? 18.480  10.036  -1.224  1.00 28.85 ? 98  SER D OG  1 
ATOM   3751 N N   . ILE D 1 99  ? 18.371  6.771   0.712   1.00 25.68 ? 99  ILE D N   1 
ATOM   3752 C CA  . ILE D 1 99  ? 17.410  5.678   0.897   1.00 24.21 ? 99  ILE D CA  1 
ATOM   3753 C C   . ILE D 1 99  ? 16.186  6.184   1.673   1.00 25.05 ? 99  ILE D C   1 
ATOM   3754 O O   . ILE D 1 99  ? 16.331  7.057   2.519   1.00 25.01 ? 99  ILE D O   1 
ATOM   3755 C CB  . ILE D 1 99  ? 18.068  4.511   1.649   1.00 24.34 ? 99  ILE D CB  1 
ATOM   3756 C CG1 . ILE D 1 99  ? 19.077  3.820   0.724   1.00 23.82 ? 99  ILE D CG1 1 
ATOM   3757 C CG2 . ILE D 1 99  ? 17.033  3.498   2.173   1.00 22.92 ? 99  ILE D CG2 1 
ATOM   3758 C CD1 . ILE D 1 99  ? 20.131  2.971   1.418   1.00 23.78 ? 99  ILE D CD1 1 
ATOM   3759 N N   . GLU D 1 100 ? 14.980  5.694   1.350   1.00 24.86 ? 100 GLU D N   1 
ATOM   3760 C CA  . GLU D 1 100 ? 13.787  5.883   2.205   1.00 25.55 ? 100 GLU D CA  1 
ATOM   3761 C C   . GLU D 1 100 ? 13.369  4.506   2.665   1.00 24.14 ? 100 GLU D C   1 
ATOM   3762 O O   . GLU D 1 100 ? 13.374  3.591   1.869   1.00 25.69 ? 100 GLU D O   1 
ATOM   3763 C CB  . GLU D 1 100 ? 12.590  6.458   1.432   1.00 25.65 ? 100 GLU D CB  1 
ATOM   3764 C CG  . GLU D 1 100 ? 12.390  7.967   1.462   1.00 28.61 ? 100 GLU D CG  1 
ATOM   3765 C CD  . GLU D 1 100 ? 10.919  8.350   1.680   1.00 31.78 ? 100 GLU D CD  1 
ATOM   3766 O OE1 . GLU D 1 100 ? 10.676  9.468   2.192   1.00 33.49 ? 100 GLU D OE1 1 
ATOM   3767 O OE2 . GLU D 1 100 ? 10.011  7.536   1.348   1.00 31.80 ? 100 GLU D OE2 1 
ATOM   3768 N N   . ASP D 1 101 ? 12.990  4.366   3.929   1.00 23.15 ? 101 ASP D N   1 
ATOM   3769 C CA  . ASP D 1 101 ? 12.529  3.104   4.465   1.00 21.52 ? 101 ASP D CA  1 
ATOM   3770 C C   . ASP D 1 101 ? 11.429  3.395   5.527   1.00 22.16 ? 101 ASP D C   1 
ATOM   3771 O O   . ASP D 1 101 ? 11.415  4.473   6.225   1.00 22.17 ? 101 ASP D O   1 
ATOM   3772 C CB  . ASP D 1 101 ? 13.702  2.284   5.009   1.00 20.37 ? 101 ASP D CB  1 
ATOM   3773 C CG  . ASP D 1 101 ? 13.334  0.849   5.282   1.00 20.46 ? 101 ASP D CG  1 
ATOM   3774 O OD1 . ASP D 1 101 ? 13.633  0.020   4.440   1.00 23.42 ? 101 ASP D OD1 1 
ATOM   3775 O OD2 . ASP D 1 101 ? 12.736  0.512   6.312   1.00 21.32 ? 101 ASP D OD2 1 
ATOM   3776 N N   . SER D 1 102 ? 10.462  2.497   5.574   1.00 21.65 ? 102 SER D N   1 
ATOM   3777 C CA  . SER D 1 102 ? 9.279   2.683   6.384   1.00 22.57 ? 102 SER D CA  1 
ATOM   3778 C C   . SER D 1 102 ? 9.041   1.471   7.247   1.00 22.49 ? 102 SER D C   1 
ATOM   3779 O O   . SER D 1 102 ? 8.006   1.392   7.925   1.00 23.87 ? 102 SER D O   1 
ATOM   3780 C CB  . SER D 1 102 ? 8.051   2.949   5.516   1.00 24.13 ? 102 SER D CB  1 
ATOM   3781 O OG  . SER D 1 102 ? 7.909   1.976   4.478   1.00 27.84 ? 102 SER D OG  1 
ATOM   3782 N N   . VAL D 1 103 ? 9.997   0.544   7.244   1.00 19.63 ? 103 VAL D N   1 
ATOM   3783 C CA  . VAL D 1 103 ? 10.022  -0.546  8.205   1.00 18.91 ? 103 VAL D CA  1 
ATOM   3784 C C   . VAL D 1 103 ? 10.843  -0.147  9.429   1.00 18.80 ? 103 VAL D C   1 
ATOM   3785 O O   . VAL D 1 103 ? 10.533  -0.504  10.580  1.00 18.71 ? 103 VAL D O   1 
ATOM   3786 C CB  . VAL D 1 103 ? 10.495  -1.830  7.531   1.00 18.31 ? 103 VAL D CB  1 
ATOM   3787 C CG1 . VAL D 1 103 ? 10.447  -3.032  8.454   1.00 16.97 ? 103 VAL D CG1 1 
ATOM   3788 C CG2 . VAL D 1 103 ? 9.557   -2.083  6.367   1.00 21.84 ? 103 VAL D CG2 1 
ATOM   3789 N N   . ILE D 1 104 ? 11.881  0.643   9.216   1.00 16.72 ? 104 ILE D N   1 
ATOM   3790 C CA  . ILE D 1 104 ? 12.685  1.024   10.373  1.00 15.65 ? 104 ILE D CA  1 
ATOM   3791 C C   . ILE D 1 104 ? 11.943  2.147   11.022  1.00 16.46 ? 104 ILE D C   1 
ATOM   3792 O O   . ILE D 1 104 ? 11.090  2.707   10.371  1.00 17.00 ? 104 ILE D O   1 
ATOM   3793 C CB  . ILE D 1 104 ? 14.180  1.368   10.006  1.00 13.94 ? 104 ILE D CB  1 
ATOM   3794 C CG1 . ILE D 1 104 ? 14.307  2.479   8.986   1.00 10.29 ? 104 ILE D CG1 1 
ATOM   3795 C CG2 . ILE D 1 104 ? 14.883  0.103   9.501   1.00 13.42 ? 104 ILE D CG2 1 
ATOM   3796 C CD1 . ILE D 1 104 ? 15.742  2.847   8.823   1.00 6.62  ? 104 ILE D CD1 1 
ATOM   3797 N N   . SER D 1 105 ? 12.227  2.423   12.297  1.00 16.47 ? 105 SER D N   1 
ATOM   3798 C CA  . SER D 1 105 ? 11.755  3.625   12.937  1.00 16.35 ? 105 SER D CA  1 
ATOM   3799 C C   . SER D 1 105 ? 12.807  4.199   13.894  1.00 16.89 ? 105 SER D C   1 
ATOM   3800 O O   . SER D 1 105 ? 13.771  3.510   14.263  1.00 14.63 ? 105 SER D O   1 
ATOM   3801 C CB  . SER D 1 105 ? 10.453  3.306   13.698  1.00 16.81 ? 105 SER D CB  1 
ATOM   3802 O OG  . SER D 1 105 ? 9.829   4.501   14.133  1.00 18.47 ? 105 SER D OG  1 
ATOM   3803 N N   . LEU D 1 106 ? 12.608  5.485   14.266  1.00 17.77 ? 106 LEU D N   1 
ATOM   3804 C CA  . LEU D 1 106 ? 13.376  6.175   15.306  1.00 18.18 ? 106 LEU D CA  1 
ATOM   3805 C C   . LEU D 1 106 ? 12.702  6.122   16.700  1.00 19.34 ? 106 LEU D C   1 
ATOM   3806 O O   . LEU D 1 106 ? 13.199  6.683   17.655  1.00 19.14 ? 106 LEU D O   1 
ATOM   3807 C CB  . LEU D 1 106 ? 13.682  7.609   14.878  1.00 15.96 ? 106 LEU D CB  1 
ATOM   3808 C CG  . LEU D 1 106 ? 14.617  7.786   13.675  1.00 13.77 ? 106 LEU D CG  1 
ATOM   3809 C CD1 . LEU D 1 106 ? 15.065  9.238   13.636  1.00 8.43  ? 106 LEU D CD1 1 
ATOM   3810 C CD2 . LEU D 1 106 ? 15.787  6.878   13.729  1.00 7.47  ? 106 LEU D CD2 1 
ATOM   3811 N N   . SER D 1 107 ? 11.605  5.359   16.813  1.00 21.14 ? 107 SER D N   1 
ATOM   3812 C CA  . SER D 1 107 ? 10.897  5.141   18.081  1.00 21.66 ? 107 SER D CA  1 
ATOM   3813 C C   . SER D 1 107 ? 10.163  3.808   18.010  1.00 21.14 ? 107 SER D C   1 
ATOM   3814 O O   . SER D 1 107 ? 9.981   3.260   16.941  1.00 21.74 ? 107 SER D O   1 
ATOM   3815 C CB  . SER D 1 107 ? 9.868   6.261   18.338  1.00 22.91 ? 107 SER D CB  1 
ATOM   3816 O OG  . SER D 1 107 ? 8.867   6.282   17.307  1.00 23.28 ? 107 SER D OG  1 
ATOM   3817 N N   . GLY D 1 108 ? 9.712   3.325   19.150  1.00 21.29 ? 108 GLY D N   1 
ATOM   3818 C CA  . GLY D 1 108 ? 8.861   2.165   19.213  1.00 21.48 ? 108 GLY D CA  1 
ATOM   3819 C C   . GLY D 1 108 ? 9.612   0.883   18.994  1.00 21.92 ? 108 GLY D C   1 
ATOM   3820 O O   . GLY D 1 108 ? 10.801  0.791   19.255  1.00 23.01 ? 108 GLY D O   1 
ATOM   3821 N N   . ASP D 1 109 ? 8.901   -0.102  18.493  1.00 21.86 ? 109 ASP D N   1 
ATOM   3822 C CA  . ASP D 1 109 ? 9.339   -1.498  18.360  1.00 22.12 ? 109 ASP D CA  1 
ATOM   3823 C C   . ASP D 1 109 ? 10.409  -1.660  17.296  1.00 20.53 ? 109 ASP D C   1 
ATOM   3824 O O   . ASP D 1 109 ? 11.185  -2.615  17.291  1.00 19.30 ? 109 ASP D O   1 
ATOM   3825 C CB  . ASP D 1 109 ? 8.104   -2.292  17.906  1.00 23.25 ? 109 ASP D CB  1 
ATOM   3826 C CG  . ASP D 1 109 ? 8.249   -3.822  18.068  1.00 28.80 ? 109 ASP D CG  1 
ATOM   3827 O OD1 . ASP D 1 109 ? 9.390   -4.355  18.080  1.00 35.22 ? 109 ASP D OD1 1 
ATOM   3828 O OD2 . ASP D 1 109 ? 7.188   -4.496  18.140  1.00 32.35 ? 109 ASP D OD2 1 
ATOM   3829 N N   . HIS D 1 110 ? 10.410  -0.736  16.357  1.00 19.74 ? 110 HIS D N   1 
ATOM   3830 C CA  . HIS D 1 110 ? 11.281  -0.849  15.221  1.00 18.92 ? 110 HIS D CA  1 
ATOM   3831 C C   . HIS D 1 110 ? 12.295  0.219   15.357  1.00 18.71 ? 110 HIS D C   1 
ATOM   3832 O O   . HIS D 1 110 ? 12.842  0.701   14.375  1.00 19.48 ? 110 HIS D O   1 
ATOM   3833 C CB  . HIS D 1 110 ? 10.444  -0.660  13.955  1.00 19.15 ? 110 HIS D CB  1 
ATOM   3834 C CG  . HIS D 1 110 ? 9.692   -1.895  13.576  1.00 17.14 ? 110 HIS D CG  1 
ATOM   3835 N ND1 . HIS D 1 110 ? 9.168   -2.082  12.325  1.00 15.66 ? 110 HIS D ND1 1 
ATOM   3836 C CD2 . HIS D 1 110 ? 9.455   -3.042  14.270  1.00 13.88 ? 110 HIS D CD2 1 
ATOM   3837 C CE1 . HIS D 1 110 ? 8.623   -3.292  12.268  1.00 18.02 ? 110 HIS D CE1 1 
ATOM   3838 N NE2 . HIS D 1 110 ? 8.772   -3.883  13.436  1.00 11.61 ? 110 HIS D NE2 1 
ATOM   3839 N N   . CYS D 1 111 ? 12.504  0.620   16.605  1.00 18.04 ? 111 CYS D N   1 
ATOM   3840 C CA  . CYS D 1 111 ? 13.551  1.572   16.963  1.00 15.83 ? 111 CYS D CA  1 
ATOM   3841 C C   . CYS D 1 111 ? 14.913  1.034   16.636  1.00 14.10 ? 111 CYS D C   1 
ATOM   3842 O O   . CYS D 1 111 ? 15.263  -0.161  16.913  1.00 12.94 ? 111 CYS D O   1 
ATOM   3843 C CB  . CYS D 1 111 ? 13.564  1.921   18.421  1.00 16.67 ? 111 CYS D CB  1 
ATOM   3844 S SG  . CYS D 1 111 ? 14.418  3.479   18.569  1.00 18.52 ? 111 CYS D SG  1 
ATOM   3845 N N   . ILE D 1 112 ? 15.650  1.894   15.954  1.00 12.10 ? 112 ILE D N   1 
ATOM   3846 C CA  . ILE D 1 112 ? 16.993  1.541   15.525  1.00 11.79 ? 112 ILE D CA  1 
ATOM   3847 C C   . ILE D 1 112 ? 18.110  2.305   16.264  1.00 12.38 ? 112 ILE D C   1 
ATOM   3848 O O   . ILE D 1 112 ? 19.251  1.937   16.103  1.00 13.11 ? 112 ILE D O   1 
ATOM   3849 C CB  . ILE D 1 112 ? 17.209  1.565   13.974  1.00 10.62 ? 112 ILE D CB  1 
ATOM   3850 C CG1 . ILE D 1 112 ? 17.054  2.965   13.389  1.00 13.04 ? 112 ILE D CG1 1 
ATOM   3851 C CG2 . ILE D 1 112 ? 16.396  0.552   13.258  1.00 8.29  ? 112 ILE D CG2 1 
ATOM   3852 C CD1 . ILE D 1 112 ? 17.768  3.148   11.975  1.00 10.50 ? 112 ILE D CD1 1 
ATOM   3853 N N   . ILE D 1 113 ? 17.763  3.334   17.066  1.00 12.72 ? 113 ILE D N   1 
ATOM   3854 C CA  . ILE D 1 113 ? 18.731  4.117   17.860  1.00 12.50 ? 113 ILE D CA  1 
ATOM   3855 C C   . ILE D 1 113 ? 19.360  3.221   18.902  1.00 12.59 ? 113 ILE D C   1 
ATOM   3856 O O   . ILE D 1 113 ? 18.636  2.439   19.505  1.00 13.03 ? 113 ILE D O   1 
ATOM   3857 C CB  . ILE D 1 113 ? 18.014  5.332   18.551  1.00 12.99 ? 113 ILE D CB  1 
ATOM   3858 C CG1 . ILE D 1 113 ? 17.621  6.382   17.486  1.00 11.34 ? 113 ILE D CG1 1 
ATOM   3859 C CG2 . ILE D 1 113 ? 18.873  5.859   19.698  1.00 13.62 ? 113 ILE D CG2 1 
ATOM   3860 C CD1 . ILE D 1 113 ? 17.029  7.718   18.108  1.00 13.50 ? 113 ILE D CD1 1 
ATOM   3861 N N   . GLY D 1 114 ? 20.687  3.273   19.103  1.00 9.52  ? 114 GLY D N   1 
ATOM   3862 C CA  . GLY D 1 114 ? 21.292  2.391   20.079  1.00 7.78  ? 114 GLY D CA  1 
ATOM   3863 C C   . GLY D 1 114 ? 21.640  1.034   19.488  1.00 7.61  ? 114 GLY D C   1 
ATOM   3864 O O   . GLY D 1 114 ? 22.152  0.134   20.184  1.00 8.48  ? 114 GLY D O   1 
ATOM   3865 N N   . ARG D 1 115 ? 21.416  0.868   18.194  1.00 7.70  ? 115 ARG D N   1 
ATOM   3866 C CA  . ARG D 1 115 ? 21.899  -0.366  17.527  1.00 9.49  ? 115 ARG D CA  1 
ATOM   3867 C C   . ARG D 1 115 ? 22.974  0.036   16.516  1.00 10.63 ? 115 ARG D C   1 
ATOM   3868 O O   . ARG D 1 115 ? 23.403  1.215   16.468  1.00 9.10  ? 115 ARG D O   1 
ATOM   3869 C CB  . ARG D 1 115 ? 20.742  -1.150  16.880  1.00 12.20 ? 115 ARG D CB  1 
ATOM   3870 C CG  . ARG D 1 115 ? 19.384  -0.875  17.493  1.00 12.15 ? 115 ARG D CG  1 
ATOM   3871 C CD  . ARG D 1 115 ? 18.594  -2.095  17.463  1.00 13.05 ? 115 ARG D CD  1 
ATOM   3872 N NE  . ARG D 1 115 ? 17.472  -2.121  18.419  1.00 16.74 ? 115 ARG D NE  1 
ATOM   3873 C CZ  . ARG D 1 115 ? 17.252  -3.101  19.301  1.00 15.73 ? 115 ARG D CZ  1 
ATOM   3874 N NH1 . ARG D 1 115 ? 18.074  -4.146  19.441  1.00 8.91  ? 115 ARG D NH1 1 
ATOM   3875 N NH2 . ARG D 1 115 ? 16.192  -3.027  20.084  1.00 19.51 ? 115 ARG D NH2 1 
ATOM   3876 N N   . THR D 1 116 ? 23.412  -0.931  15.704  1.00 11.82 ? 116 THR D N   1 
ATOM   3877 C CA  . THR D 1 116 ? 24.555  -0.746  14.821  1.00 10.16 ? 116 THR D CA  1 
ATOM   3878 C C   . THR D 1 116 ? 24.254  -0.890  13.322  1.00 10.69 ? 116 THR D C   1 
ATOM   3879 O O   . THR D 1 116 ? 23.793  -1.948  12.879  1.00 10.44 ? 116 THR D O   1 
ATOM   3880 C CB  . THR D 1 116 ? 25.675  -1.724  15.148  1.00 12.03 ? 116 THR D CB  1 
ATOM   3881 O OG1 . THR D 1 116 ? 25.962  -1.751  16.567  1.00 12.51 ? 116 THR D OG1 1 
ATOM   3882 C CG2 . THR D 1 116 ? 26.920  -1.276  14.401  1.00 9.51  ? 116 THR D CG2 1 
ATOM   3883 N N   . LEU D 1 117 ? 24.514  0.156   12.540  1.00 6.97  ? 117 LEU D N   1 
ATOM   3884 C CA  . LEU D 1 117 ? 24.555  0.107   11.068  1.00 9.15  ? 117 LEU D CA  1 
ATOM   3885 C C   . LEU D 1 117 ? 25.863  -0.469  10.598  1.00 12.75 ? 117 LEU D C   1 
ATOM   3886 O O   . LEU D 1 117 ? 26.921  -0.045  11.036  1.00 13.17 ? 117 LEU D O   1 
ATOM   3887 C CB  . LEU D 1 117 ? 24.507  1.532   10.516  1.00 9.62  ? 117 LEU D CB  1 
ATOM   3888 C CG  . LEU D 1 117 ? 24.393  1.851   9.027   1.00 4.37  ? 117 LEU D CG  1 
ATOM   3889 C CD1 . LEU D 1 117 ? 22.967  1.428   8.702   1.00 5.59  ? 117 LEU D CD1 1 
ATOM   3890 C CD2 . LEU D 1 117 ? 24.507  3.395   8.880   1.00 6.65  ? 117 LEU D CD2 1 
ATOM   3891 N N   . VAL D 1 118 ? 25.798  -1.445  9.701   1.00 16.57 ? 118 VAL D N   1 
ATOM   3892 C CA  . VAL D 1 118 ? 26.972  -2.149  9.171   1.00 16.93 ? 118 VAL D CA  1 
ATOM   3893 C C   . VAL D 1 118 ? 26.935  -2.009  7.645   1.00 18.43 ? 118 VAL D C   1 
ATOM   3894 O O   . VAL D 1 118 ? 25.843  -2.064  7.022   1.00 18.94 ? 118 VAL D O   1 
ATOM   3895 C CB  . VAL D 1 118 ? 26.921  -3.682  9.508   1.00 17.17 ? 118 VAL D CB  1 
ATOM   3896 C CG1 . VAL D 1 118 ? 28.123  -4.373  8.940   1.00 15.67 ? 118 VAL D CG1 1 
ATOM   3897 C CG2 . VAL D 1 118 ? 26.830  -3.906  10.965  1.00 17.04 ? 118 VAL D CG2 1 
ATOM   3898 N N   . VAL D 1 119 ? 28.107  -1.802  7.046   1.00 20.30 ? 119 VAL D N   1 
ATOM   3899 C CA  . VAL D 1 119 ? 28.243  -1.978  5.608   1.00 21.52 ? 119 VAL D CA  1 
ATOM   3900 C C   . VAL D 1 119 ? 29.056  -3.248  5.386   1.00 23.06 ? 119 VAL D C   1 
ATOM   3901 O O   . VAL D 1 119 ? 30.014  -3.482  6.117   1.00 22.60 ? 119 VAL D O   1 
ATOM   3902 C CB  . VAL D 1 119 ? 28.660  -0.663  4.830   1.00 21.24 ? 119 VAL D CB  1 
ATOM   3903 C CG1 . VAL D 1 119 ? 29.658  0.158   5.562   1.00 19.68 ? 119 VAL D CG1 1 
ATOM   3904 C CG2 . VAL D 1 119 ? 29.099  -0.988  3.448   1.00 21.12 ? 119 VAL D CG2 1 
ATOM   3905 N N   . HIS D 1 120 ? 28.571  -4.130  4.510   1.00 23.88 ? 120 HIS D N   1 
ATOM   3906 C CA  . HIS D 1 120 ? 29.182  -5.466  4.343   1.00 25.92 ? 120 HIS D CA  1 
ATOM   3907 C C   . HIS D 1 120 ? 30.084  -5.554  3.126   1.00 27.52 ? 120 HIS D C   1 
ATOM   3908 O O   . HIS D 1 120 ? 30.126  -4.604  2.321   1.00 27.24 ? 120 HIS D O   1 
ATOM   3909 C CB  . HIS D 1 120 ? 28.163  -6.570  4.280   1.00 25.00 ? 120 HIS D CB  1 
ATOM   3910 C CG  . HIS D 1 120 ? 27.369  -6.712  5.528   1.00 24.63 ? 120 HIS D CG  1 
ATOM   3911 N ND1 . HIS D 1 120 ? 27.469  -7.816  6.343   1.00 22.72 ? 120 HIS D ND1 1 
ATOM   3912 C CD2 . HIS D 1 120 ? 26.440  -5.903  6.091   1.00 20.84 ? 120 HIS D CD2 1 
ATOM   3913 C CE1 . HIS D 1 120 ? 26.625  -7.689  7.345   1.00 22.39 ? 120 HIS D CE1 1 
ATOM   3914 N NE2 . HIS D 1 120 ? 25.997  -6.530  7.223   1.00 21.29 ? 120 HIS D NE2 1 
ATOM   3915 N N   . GLU D 1 121 ? 30.810  -6.683  3.007   1.00 30.12 ? 121 GLU D N   1 
ATOM   3916 C CA  . GLU D 1 121 ? 31.847  -6.837  1.960   1.00 32.00 ? 121 GLU D CA  1 
ATOM   3917 C C   . GLU D 1 121 ? 31.139  -6.906  0.656   1.00 32.38 ? 121 GLU D C   1 
ATOM   3918 O O   . GLU D 1 121 ? 31.366  -6.089  -0.236  1.00 32.82 ? 121 GLU D O   1 
ATOM   3919 C CB  . GLU D 1 121 ? 32.653  -8.123  2.163   1.00 32.29 ? 121 GLU D CB  1 
ATOM   3920 C CG  . GLU D 1 121 ? 34.013  -8.188  1.444   1.00 34.26 ? 121 GLU D CG  1 
ATOM   3921 C CD  . GLU D 1 121 ? 34.649  -9.594  1.542   1.00 34.50 ? 121 GLU D CD  1 
ATOM   3922 O OE1 . GLU D 1 121 ? 33.962  -10.592 1.883   1.00 37.30 ? 121 GLU D OE1 1 
ATOM   3923 O OE2 . GLU D 1 121 ? 35.858  -9.706  1.283   1.00 38.84 ? 121 GLU D OE2 1 
ATOM   3924 N N   . LYS D 1 122 ? 30.233  -7.866  0.600   1.00 32.79 ? 122 LYS D N   1 
ATOM   3925 C CA  . LYS D 1 122 ? 29.522  -8.222  -0.583  1.00 33.75 ? 122 LYS D CA  1 
ATOM   3926 C C   . LYS D 1 122 ? 28.180  -7.487  -0.716  1.00 33.93 ? 122 LYS D C   1 
ATOM   3927 O O   . LYS D 1 122 ? 27.609  -7.015  0.296   1.00 32.67 ? 122 LYS D O   1 
ATOM   3928 C CB  . LYS D 1 122 ? 29.370  -9.752  -0.577  1.00 33.76 ? 122 LYS D CB  1 
ATOM   3929 C CG  . LYS D 1 122 ? 30.754  -10.372 -0.421  1.00 35.42 ? 122 LYS D CG  1 
ATOM   3930 C CD  . LYS D 1 122 ? 30.816  -11.887 -0.625  1.00 37.34 ? 122 LYS D CD  1 
ATOM   3931 C CE  . LYS D 1 122 ? 32.295  -12.341 -0.839  1.00 37.39 ? 122 LYS D CE  1 
ATOM   3932 N NZ  . LYS D 1 122 ? 32.496  -13.877 -0.820  1.00 37.01 ? 122 LYS D NZ  1 
ATOM   3933 N N   . ALA D 1 123 ? 27.745  -7.355  -1.989  1.00 34.30 ? 123 ALA D N   1 
ATOM   3934 C CA  . ALA D 1 123 ? 26.351  -7.059  -2.393  1.00 34.21 ? 123 ALA D CA  1 
ATOM   3935 C C   . ALA D 1 123 ? 25.324  -7.963  -1.672  1.00 34.65 ? 123 ALA D C   1 
ATOM   3936 O O   . ALA D 1 123 ? 25.522  -9.188  -1.570  1.00 33.91 ? 123 ALA D O   1 
ATOM   3937 C CB  . ALA D 1 123 ? 26.204  -7.191  -3.874  1.00 33.81 ? 123 ALA D CB  1 
ATOM   3938 N N   . ASP D 1 124 ? 24.248  -7.335  -1.176  1.00 34.75 ? 124 ASP D N   1 
ATOM   3939 C CA  . ASP D 1 124 ? 23.350  -7.944  -0.171  1.00 35.83 ? 124 ASP D CA  1 
ATOM   3940 C C   . ASP D 1 124 ? 22.832  -9.313  -0.621  1.00 35.76 ? 124 ASP D C   1 
ATOM   3941 O O   . ASP D 1 124 ? 22.314  -9.440  -1.730  1.00 35.22 ? 124 ASP D O   1 
ATOM   3942 C CB  . ASP D 1 124 ? 22.187  -6.955  0.096   1.00 36.73 ? 124 ASP D CB  1 
ATOM   3943 C CG  . ASP D 1 124 ? 21.333  -7.289  1.353   1.00 37.26 ? 124 ASP D CG  1 
ATOM   3944 O OD1 . ASP D 1 124 ? 21.372  -8.449  1.867   1.00 36.31 ? 124 ASP D OD1 1 
ATOM   3945 O OD2 . ASP D 1 124 ? 20.611  -6.344  1.782   1.00 31.85 ? 124 ASP D OD2 1 
ATOM   3946 N N   . SER D 1 142 ? 31.909  -10.199 5.292   1.00 27.67 ? 142 SER D N   1 
ATOM   3947 C CA  . SER D 1 142 ? 32.664  -9.569  6.350   1.00 26.94 ? 142 SER D CA  1 
ATOM   3948 C C   . SER D 1 142 ? 32.293  -8.059  6.445   1.00 26.56 ? 142 SER D C   1 
ATOM   3949 O O   . SER D 1 142 ? 31.894  -7.408  5.460   1.00 26.24 ? 142 SER D O   1 
ATOM   3950 C CB  . SER D 1 142 ? 34.157  -9.743  6.107   1.00 28.25 ? 142 SER D CB  1 
ATOM   3951 O OG  . SER D 1 142 ? 34.752  -8.490  5.779   1.00 28.40 ? 142 SER D OG  1 
ATOM   3952 N N   . ARG D 1 143 ? 32.428  -7.514  7.642   1.00 24.36 ? 143 ARG D N   1 
ATOM   3953 C CA  . ARG D 1 143 ? 31.713  -6.299  7.950   1.00 23.05 ? 143 ARG D CA  1 
ATOM   3954 C C   . ARG D 1 143 ? 32.696  -5.217  7.787   1.00 21.68 ? 143 ARG D C   1 
ATOM   3955 O O   . ARG D 1 143 ? 33.533  -5.021  8.589   1.00 22.20 ? 143 ARG D O   1 
ATOM   3956 C CB  . ARG D 1 143 ? 31.099  -6.352  9.352   1.00 23.18 ? 143 ARG D CB  1 
ATOM   3957 C CG  . ARG D 1 143 ? 30.206  -7.584  9.549   1.00 22.03 ? 143 ARG D CG  1 
ATOM   3958 C CD  . ARG D 1 143 ? 29.616  -7.678  10.953  1.00 22.20 ? 143 ARG D CD  1 
ATOM   3959 N NE  . ARG D 1 143 ? 28.635  -8.741  11.003  1.00 20.71 ? 143 ARG D NE  1 
ATOM   3960 C CZ  . ARG D 1 143 ? 27.864  -9.014  12.054  1.00 25.24 ? 143 ARG D CZ  1 
ATOM   3961 N NH1 . ARG D 1 143 ? 27.913  -8.257  13.143  1.00 26.75 ? 143 ARG D NH1 1 
ATOM   3962 N NH2 . ARG D 1 143 ? 27.018  -10.027 12.010  1.00 22.95 ? 143 ARG D NH2 1 
ATOM   3963 N N   . LEU D 1 144 ? 32.605  -4.534  6.686   1.00 22.22 ? 144 LEU D N   1 
ATOM   3964 C CA  . LEU D 1 144 ? 33.576  -3.539  6.366   1.00 21.67 ? 144 LEU D CA  1 
ATOM   3965 C C   . LEU D 1 144 ? 33.682  -2.416  7.390   1.00 21.61 ? 144 LEU D C   1 
ATOM   3966 O O   . LEU D 1 144 ? 34.784  -2.019  7.761   1.00 22.28 ? 144 LEU D O   1 
ATOM   3967 C CB  . LEU D 1 144 ? 33.366  -3.067  4.942   1.00 21.94 ? 144 LEU D CB  1 
ATOM   3968 C CG  . LEU D 1 144 ? 33.617  -4.186  3.912   1.00 22.02 ? 144 LEU D CG  1 
ATOM   3969 C CD1 . LEU D 1 144 ? 33.138  -3.701  2.577   1.00 21.96 ? 144 LEU D CD1 1 
ATOM   3970 C CD2 . LEU D 1 144 ? 35.071  -4.537  3.775   1.00 22.16 ? 144 LEU D CD2 1 
ATOM   3971 N N   . ALA D 1 145 ? 32.548  -1.947  7.896   1.00 20.12 ? 145 ALA D N   1 
ATOM   3972 C CA  . ALA D 1 145 ? 32.551  -0.827  8.838   1.00 19.13 ? 145 ALA D CA  1 
ATOM   3973 C C   . ALA D 1 145 ? 31.190  -0.848  9.523   1.00 19.60 ? 145 ALA D C   1 
ATOM   3974 O O   . ALA D 1 145 ? 30.252  -1.503  9.037   1.00 20.00 ? 145 ALA D O   1 
ATOM   3975 C CB  . ALA D 1 145 ? 32.793  0.516   8.126   1.00 17.83 ? 145 ALA D CB  1 
ATOM   3976 N N   . CYS D 1 146 ? 31.103  -0.158  10.664  1.00 20.15 ? 146 CYS D N   1 
ATOM   3977 C CA  . CYS D 1 146 ? 29.886  -0.072  11.469  1.00 20.22 ? 146 CYS D CA  1 
ATOM   3978 C C   . CYS D 1 146 ? 29.970  1.164   12.394  1.00 20.08 ? 146 CYS D C   1 
ATOM   3979 O O   . CYS D 1 146 ? 31.040  1.785   12.540  1.00 21.06 ? 146 CYS D O   1 
ATOM   3980 C CB  . CYS D 1 146 ? 29.651  -1.376  12.220  1.00 19.73 ? 146 CYS D CB  1 
ATOM   3981 S SG  . CYS D 1 146 ? 31.015  -1.906  13.314  1.00 23.50 ? 146 CYS D SG  1 
ATOM   3982 N N   . GLY D 1 147 ? 28.833  1.592   12.940  1.00 18.13 ? 147 GLY D N   1 
ATOM   3983 C CA  . GLY D 1 147 ? 28.855  2.375   14.141  1.00 16.23 ? 147 GLY D CA  1 
ATOM   3984 C C   . GLY D 1 147 ? 27.505  2.278   14.821  1.00 15.71 ? 147 GLY D C   1 
ATOM   3985 O O   . GLY D 1 147 ? 26.538  1.864   14.210  1.00 15.60 ? 147 GLY D O   1 
ATOM   3986 N N   . VAL D 1 148 ? 27.424  2.725   16.061  1.00 13.43 ? 148 VAL D N   1 
ATOM   3987 C CA  . VAL D 1 148 ? 26.172  2.691   16.796  1.00 11.64 ? 148 VAL D CA  1 
ATOM   3988 C C   . VAL D 1 148 ? 25.281  3.841   16.307  1.00 12.74 ? 148 VAL D C   1 
ATOM   3989 O O   . VAL D 1 148 ? 25.815  4.902   16.039  1.00 10.22 ? 148 VAL D O   1 
ATOM   3990 C CB  . VAL D 1 148 ? 26.455  2.744   18.363  1.00 11.71 ? 148 VAL D CB  1 
ATOM   3991 C CG1 . VAL D 1 148 ? 25.197  2.890   19.145  1.00 8.19  ? 148 VAL D CG1 1 
ATOM   3992 C CG2 . VAL D 1 148 ? 27.166  1.421   18.849  1.00 13.12 ? 148 VAL D CG2 1 
ATOM   3993 N N   . ILE D 1 149 ? 23.939  3.641   16.238  1.00 10.60 ? 149 ILE D N   1 
ATOM   3994 C CA  . ILE D 1 149 ? 23.072  4.693   15.798  1.00 10.22 ? 149 ILE D CA  1 
ATOM   3995 C C   . ILE D 1 149 ? 22.754  5.564   16.995  1.00 10.30 ? 149 ILE D C   1 
ATOM   3996 O O   . ILE D 1 149 ? 22.278  5.078   17.975  1.00 10.18 ? 149 ILE D O   1 
ATOM   3997 C CB  . ILE D 1 149 ? 21.762  4.150   15.027  1.00 11.45 ? 149 ILE D CB  1 
ATOM   3998 C CG1 . ILE D 1 149 ? 22.101  3.420   13.719  1.00 9.58  ? 149 ILE D CG1 1 
ATOM   3999 C CG2 . ILE D 1 149 ? 20.866  5.304   14.603  1.00 11.28 ? 149 ILE D CG2 1 
ATOM   4000 C CD1 . ILE D 1 149 ? 21.399  2.122   13.473  1.00 12.34 ? 149 ILE D CD1 1 
ATOM   4001 N N   . GLY D 1 150 ? 23.007  6.875   16.960  1.00 10.15 ? 150 GLY D N   1 
ATOM   4002 C CA  . GLY D 1 150 ? 22.702  7.655   18.126  1.00 9.29  ? 150 GLY D CA  1 
ATOM   4003 C C   . GLY D 1 150 ? 21.798  8.827   17.748  1.00 11.80 ? 150 GLY D C   1 
ATOM   4004 O O   . GLY D 1 150 ? 21.605  9.085   16.562  1.00 10.33 ? 150 GLY D O   1 
ATOM   4005 N N   . ILE D 1 151 ? 21.245  9.479   18.781  1.00 11.66 ? 151 ILE D N   1 
ATOM   4006 C CA  . ILE D 1 151 ? 20.278  10.535  18.687  1.00 12.53 ? 151 ILE D CA  1 
ATOM   4007 C C   . ILE D 1 151 ? 21.021  11.712  18.142  1.00 14.34 ? 151 ILE D C   1 
ATOM   4008 O O   . ILE D 1 151 ? 22.079  11.971  18.622  1.00 15.03 ? 151 ILE D O   1 
ATOM   4009 C CB  . ILE D 1 151 ? 19.795  10.848  20.115  1.00 12.74 ? 151 ILE D CB  1 
ATOM   4010 C CG1 . ILE D 1 151 ? 18.937  9.698   20.587  1.00 10.26 ? 151 ILE D CG1 1 
ATOM   4011 C CG2 . ILE D 1 151 ? 19.104  12.256  20.230  1.00 9.95  ? 151 ILE D CG2 1 
ATOM   4012 C CD1 . ILE D 1 151 ? 18.532  9.704   22.041  1.00 12.12 ? 151 ILE D CD1 1 
ATOM   4013 N N   . ALA D 1 152 ? 20.455  12.499  17.225  1.00 16.37 ? 152 ALA D N   1 
ATOM   4014 C CA  . ALA D 1 152 ? 21.227  13.584  16.683  1.00 17.09 ? 152 ALA D CA  1 
ATOM   4015 C C   . ALA D 1 152 ? 20.552  14.877  16.923  1.00 19.89 ? 152 ALA D C   1 
ATOM   4016 O O   . ALA D 1 152 ? 19.380  14.939  17.250  1.00 19.71 ? 152 ALA D O   1 
ATOM   4017 C CB  . ALA D 1 152 ? 21.456  13.418  15.234  1.00 17.97 ? 152 ALA D CB  1 
ATOM   4018 N N   . GLN D 1 153 ? 21.291  15.944  16.730  1.00 23.47 ? 153 GLN D N   1 
ATOM   4019 C CA  . GLN D 1 153 ? 20.758  17.235  17.060  1.00 26.48 ? 153 GLN D CA  1 
ATOM   4020 C C   . GLN D 1 153 ? 19.691  17.702  16.058  1.00 28.10 ? 153 GLN D C   1 
ATOM   4021 O O   . GLN D 1 153 ? 19.968  18.025  14.888  1.00 28.21 ? 153 GLN D O   1 
ATOM   4022 C CB  . GLN D 1 153 ? 21.869  18.249  17.205  1.00 27.28 ? 153 GLN D CB  1 
ATOM   4023 C CG  . GLN D 1 153 ? 21.341  19.435  17.957  1.00 31.55 ? 153 GLN D CG  1 
ATOM   4024 C CD  . GLN D 1 153 ? 22.416  20.437  18.372  1.00 37.49 ? 153 GLN D CD  1 
ATOM   4025 O OE1 . GLN D 1 153 ? 23.622  20.262  18.112  1.00 38.60 ? 153 GLN D OE1 1 
ATOM   4026 N NE2 . GLN D 1 153 ? 21.968  21.508  19.035  1.00 40.94 ? 153 GLN D NE2 1 
ATOM   4027 O OXT . GLN D 1 153 ? 18.500  17.729  16.424  1.00 30.05 ? 153 GLN D OXT 1 
HETATM 4028 O O   . HOH E 2 .   ? -13.139 -4.293  33.889  1.00 4.57  ? 154 HOH A O   1 
HETATM 4029 O O   . HOH E 2 .   ? -13.542 -0.417  30.596  1.00 4.94  ? 155 HOH A O   1 
HETATM 4030 O O   . HOH E 2 .   ? -10.736 1.913   34.439  1.00 2.62  ? 156 HOH A O   1 
HETATM 4031 O O   . HOH E 2 .   ? -13.535 -11.792 14.657  1.00 6.27  ? 157 HOH A O   1 
HETATM 4032 O O   . HOH E 2 .   ? -12.094 -6.975  33.118  1.00 11.18 ? 158 HOH A O   1 
HETATM 4033 O O   . HOH E 2 .   ? -24.069 -5.479  32.103  1.00 12.76 ? 159 HOH A O   1 
HETATM 4034 O O   . HOH E 2 .   ? -3.191  -1.472  12.481  1.00 13.80 ? 160 HOH A O   1 
HETATM 4035 O O   . HOH E 2 .   ? -15.816 -5.044  33.914  1.00 14.57 ? 161 HOH A O   1 
HETATM 4036 O O   . HOH E 2 .   ? -14.308 1.890   30.013  1.00 18.94 ? 162 HOH A O   1 
HETATM 4037 O O   . HOH E 2 .   ? -25.509 -4.057  28.489  1.00 14.31 ? 163 HOH A O   1 
HETATM 4038 O O   . HOH E 2 .   ? -21.700 8.452   8.078   1.00 21.65 ? 164 HOH A O   1 
HETATM 4039 O O   . HOH E 2 .   ? -17.119 -2.815  32.730  1.00 13.74 ? 165 HOH A O   1 
HETATM 4040 O O   . HOH E 2 .   ? -13.682 -4.907  12.757  1.00 10.29 ? 166 HOH A O   1 
HETATM 4041 O O   . HOH E 2 .   ? -7.718  -16.177 30.227  1.00 14.62 ? 167 HOH A O   1 
HETATM 4042 O O   . HOH E 2 .   ? -12.631 -9.324  7.850   1.00 18.35 ? 168 HOH A O   1 
HETATM 4043 O O   . HOH E 2 .   ? -17.767 1.735   2.703   1.00 22.90 ? 169 HOH A O   1 
HETATM 4044 O O   . HOH E 2 .   ? -27.377 -3.421  26.773  1.00 15.32 ? 170 HOH A O   1 
HETATM 4045 O O   . HOH E 2 .   ? -28.738 -6.507  24.834  1.00 17.64 ? 171 HOH A O   1 
HETATM 4046 O O   . HOH E 2 .   ? -3.802  0.871   13.963  1.00 16.73 ? 172 HOH A O   1 
HETATM 4047 O O   . HOH E 2 .   ? -27.871 -6.042  21.647  1.00 18.95 ? 173 HOH A O   1 
HETATM 4048 O O   . HOH E 2 .   ? -26.982 -7.112  15.087  1.00 17.64 ? 174 HOH A O   1 
HETATM 4049 O O   . HOH E 2 .   ? -8.684  -12.005 13.667  1.00 19.80 ? 175 HOH A O   1 
HETATM 4050 O O   . HOH E 2 .   ? -32.670 -12.370 20.354  1.00 20.86 ? 176 HOH A O   1 
HETATM 4051 O O   . HOH E 2 .   ? -24.378 -0.079  28.546  1.00 26.29 ? 177 HOH A O   1 
HETATM 4052 O O   . HOH E 2 .   ? -12.709 4.852   16.276  1.00 17.30 ? 178 HOH A O   1 
HETATM 4053 O O   . HOH E 2 .   ? -22.288 3.990   24.181  1.00 20.54 ? 179 HOH A O   1 
HETATM 4054 O O   . HOH E 2 .   ? -13.990 9.826   30.981  1.00 28.76 ? 180 HOH A O   1 
HETATM 4055 O O   . HOH E 2 .   ? -16.229 -15.124 17.126  1.00 16.53 ? 181 HOH A O   1 
HETATM 4056 O O   . HOH E 2 .   ? -5.415  4.797   18.920  1.00 45.09 ? 182 HOH A O   1 
HETATM 4057 O O   . HOH E 2 .   ? -4.071  -7.179  8.824   1.00 14.73 ? 183 HOH A O   1 
HETATM 4058 O O   . HOH E 2 .   ? -14.607 -21.042 22.975  1.00 18.06 ? 184 HOH A O   1 
HETATM 4059 O O   . HOH E 2 .   ? 0.126   -0.816  23.575  1.00 12.37 ? 185 HOH A O   1 
HETATM 4060 O O   . HOH E 2 .   ? -11.667 -12.711 13.499  1.00 19.62 ? 186 HOH A O   1 
HETATM 4061 O O   . HOH E 2 .   ? 4.434   -8.886  20.144  1.00 17.31 ? 187 HOH A O   1 
HETATM 4062 O O   . HOH E 2 .   ? 1.320   -0.586  26.014  1.00 10.44 ? 188 HOH A O   1 
HETATM 4063 O O   . HOH E 2 .   ? -31.318 -12.631 22.556  1.00 28.43 ? 189 HOH A O   1 
HETATM 4064 O O   . HOH E 2 .   ? -3.125  4.890   24.032  1.00 27.25 ? 190 HOH A O   1 
HETATM 4065 O O   . HOH E 2 .   ? -20.905 8.437   30.670  1.00 22.71 ? 191 HOH A O   1 
HETATM 4066 O O   . HOH E 2 .   ? -21.088 0.957   30.530  1.00 30.57 ? 192 HOH A O   1 
HETATM 4067 O O   . HOH E 2 .   ? -19.375 -15.136 17.911  1.00 19.58 ? 193 HOH A O   1 
HETATM 4068 O O   . HOH E 2 .   ? -5.398  4.996   6.329   1.00 17.16 ? 194 HOH A O   1 
HETATM 4069 O O   . HOH E 2 .   ? -17.105 0.771   16.954  1.00 19.31 ? 195 HOH A O   1 
HETATM 4070 O O   . HOH E 2 .   ? -6.919  -3.825  2.947   1.00 22.10 ? 196 HOH A O   1 
HETATM 4071 O O   . HOH E 2 .   ? -18.838 -5.511  4.790   1.00 24.72 ? 197 HOH A O   1 
HETATM 4072 O O   . HOH E 2 .   ? -22.398 -15.603 12.018  1.00 24.02 ? 198 HOH A O   1 
HETATM 4073 O O   . HOH E 2 .   ? -13.659 -0.659  3.009   1.00 26.75 ? 199 HOH A O   1 
HETATM 4074 O O   . HOH E 2 .   ? -7.111  -6.392  2.520   1.00 19.82 ? 200 HOH A O   1 
HETATM 4075 O O   . HOH E 2 .   ? 3.019   -5.606  19.434  1.00 24.24 ? 201 HOH A O   1 
HETATM 4076 O O   . HOH E 2 .   ? -1.952  -18.272 42.364  1.00 23.69 ? 202 HOH A O   1 
HETATM 4077 O O   . HOH E 2 .   ? -3.554  -5.154  9.561   1.00 15.59 ? 203 HOH A O   1 
HETATM 4078 O O   . HOH E 2 .   ? -27.064 -4.627  13.454  1.00 24.08 ? 204 HOH A O   1 
HETATM 4079 O O   . HOH E 2 .   ? -5.442  -11.544 12.100  1.00 20.20 ? 205 HOH A O   1 
HETATM 4080 O O   . HOH E 2 .   ? -21.735 -13.764 9.826   1.00 24.79 ? 206 HOH A O   1 
HETATM 4081 O O   . HOH E 2 .   ? -16.150 -0.467  36.720  1.00 25.33 ? 207 HOH A O   1 
HETATM 4082 O O   . HOH E 2 .   ? -29.489 -19.736 16.742  1.00 32.02 ? 208 HOH A O   1 
HETATM 4083 O O   . HOH E 2 .   ? -18.601 -10.078 10.391  1.00 21.45 ? 209 HOH A O   1 
HETATM 4084 O O   . HOH E 2 .   ? -16.646 4.106   19.099  1.00 33.76 ? 210 HOH A O   1 
HETATM 4085 O O   . HOH E 2 .   ? -15.957 -13.204 15.823  1.00 24.76 ? 211 HOH A O   1 
HETATM 4086 O O   . HOH E 2 .   ? -14.740 7.577   21.395  1.00 27.11 ? 212 HOH A O   1 
HETATM 4087 O O   . HOH E 2 .   ? -3.468  -1.497  4.640   1.00 28.47 ? 213 HOH A O   1 
HETATM 4088 O O   . HOH E 2 .   ? -15.888 -10.512 11.868  1.00 23.87 ? 214 HOH A O   1 
HETATM 4089 O O   . HOH E 2 .   ? -18.055 3.767   36.284  1.00 20.99 ? 215 HOH A O   1 
HETATM 4090 O O   . HOH E 2 .   ? 0.399   -10.776 17.380  1.00 23.91 ? 216 HOH A O   1 
HETATM 4091 O O   . HOH E 2 .   ? -0.271  -14.417 33.374  1.00 28.03 ? 217 HOH A O   1 
HETATM 4092 O O   . HOH E 2 .   ? -15.435 6.698   19.137  1.00 27.34 ? 218 HOH A O   1 
HETATM 4093 O O   . HOH E 2 .   ? -11.031 5.476   11.182  1.00 23.17 ? 219 HOH A O   1 
HETATM 4094 O O   . HOH E 2 .   ? -26.510 2.427   12.821  1.00 35.40 ? 220 HOH A O   1 
HETATM 4095 O O   . HOH E 2 .   ? -30.967 -4.690  19.421  1.00 44.50 ? 221 HOH A O   1 
HETATM 4096 O O   . HOH E 2 .   ? -2.167  -3.302  11.547  1.00 30.71 ? 222 HOH A O   1 
HETATM 4097 O O   . HOH E 2 .   ? -22.504 -11.737 8.112   1.00 31.67 ? 223 HOH A O   1 
HETATM 4098 O O   . HOH E 2 .   ? -1.898  -18.259 20.179  1.00 28.13 ? 224 HOH A O   1 
HETATM 4099 O O   . HOH E 2 .   ? -19.764 -10.346 33.240  1.00 35.57 ? 225 HOH A O   1 
HETATM 4100 O O   . HOH E 2 .   ? -8.416  6.045   17.650  1.00 23.26 ? 226 HOH A O   1 
HETATM 4101 O O   . HOH E 2 .   ? -19.166 -12.436 33.575  1.00 27.42 ? 228 HOH A O   1 
HETATM 4102 O O   . HOH E 2 .   ? -26.491 2.436   10.387  1.00 34.30 ? 229 HOH A O   1 
HETATM 4103 O O   . HOH E 2 .   ? -24.564 -1.529  10.996  1.00 28.04 ? 230 HOH A O   1 
HETATM 4104 O O   . HOH E 2 .   ? 5.304   -0.871  16.265  1.00 27.30 ? 231 HOH A O   1 
HETATM 4105 O O   . HOH E 2 .   ? -18.785 -1.242  33.286  1.00 35.81 ? 232 HOH A O   1 
HETATM 4106 O O   . HOH E 2 .   ? -23.961 6.369   9.396   1.00 26.07 ? 234 HOH A O   1 
HETATM 4107 O O   . HOH E 2 .   ? -7.340  9.140   21.366  1.00 28.73 ? 235 HOH A O   1 
HETATM 4108 O O   . HOH E 2 .   ? -10.331 -2.635  5.351   1.00 27.79 ? 236 HOH A O   1 
HETATM 4109 O O   . HOH E 2 .   ? -29.294 -7.684  16.210  1.00 26.69 ? 237 HOH A O   1 
HETATM 4110 O O   . HOH E 2 .   ? -14.626 -17.526 31.025  1.00 51.77 ? 238 HOH A O   1 
HETATM 4111 O O   . HOH E 2 .   ? -26.990 -16.496 15.360  1.00 31.01 ? 239 HOH A O   1 
HETATM 4112 O O   . HOH F 2 .   ? 9.342   1.589   34.703  1.00 10.11 ? 234 HOH B O   1 
HETATM 4113 O O   . HOH F 2 .   ? 4.728   6.351   23.004  1.00 38.81 ? 240 HOH B O   1 
HETATM 4114 O O   . HOH F 2 .   ? -10.767 -0.174  36.300  1.00 2.66  ? 241 HOH B O   1 
HETATM 4115 O O   . HOH F 2 .   ? -10.639 -9.016  40.232  1.00 7.26  ? 242 HOH B O   1 
HETATM 4116 O O   . HOH F 2 .   ? -10.934 -9.198  34.458  1.00 9.29  ? 243 HOH B O   1 
HETATM 4117 O O   . HOH F 2 .   ? -6.240  7.553   52.893  1.00 16.65 ? 244 HOH B O   1 
HETATM 4118 O O   . HOH F 2 .   ? -15.792 -1.072  54.880  1.00 20.21 ? 245 HOH B O   1 
HETATM 4119 O O   . HOH F 2 .   ? 7.776   -8.200  45.402  1.00 18.40 ? 246 HOH B O   1 
HETATM 4120 O O   . HOH F 2 .   ? -12.744 -11.314 49.522  1.00 11.92 ? 247 HOH B O   1 
HETATM 4121 O O   . HOH F 2 .   ? -18.572 -3.049  48.524  1.00 11.45 ? 248 HOH B O   1 
HETATM 4122 O O   . HOH F 2 .   ? -17.857 -1.264  53.190  1.00 9.18  ? 249 HOH B O   1 
HETATM 4123 O O   . HOH F 2 .   ? 12.011  -4.291  35.112  1.00 22.07 ? 250 HOH B O   1 
HETATM 4124 O O   . HOH F 2 .   ? -18.712 -3.696  52.243  1.00 17.19 ? 251 HOH B O   1 
HETATM 4125 O O   . HOH F 2 .   ? -8.681  7.964   29.913  1.00 10.53 ? 252 HOH B O   1 
HETATM 4126 O O   . HOH F 2 .   ? -10.099 -7.049  39.188  1.00 2.00  ? 253 HOH B O   1 
HETATM 4127 O O   . HOH F 2 .   ? -14.668 -4.645  39.772  1.00 7.78  ? 254 HOH B O   1 
HETATM 4128 O O   . HOH F 2 .   ? -2.531  5.389   52.042  1.00 15.87 ? 255 HOH B O   1 
HETATM 4129 O O   . HOH F 2 .   ? -19.231 -1.969  44.863  1.00 18.89 ? 256 HOH B O   1 
HETATM 4130 O O   . HOH F 2 .   ? 9.441   -2.061  36.872  1.00 9.78  ? 257 HOH B O   1 
HETATM 4131 O O   . HOH F 2 .   ? 6.170   4.519   32.802  1.00 14.76 ? 258 HOH B O   1 
HETATM 4132 O O   . HOH F 2 .   ? -6.235  8.851   35.827  1.00 5.15  ? 259 HOH B O   1 
HETATM 4133 O O   . HOH F 2 .   ? 4.504   6.439   28.452  1.00 27.12 ? 260 HOH B O   1 
HETATM 4134 O O   . HOH F 2 .   ? 2.883   7.717   50.612  1.00 23.17 ? 261 HOH B O   1 
HETATM 4135 O O   . HOH F 2 .   ? -18.379 -7.166  50.449  1.00 28.15 ? 262 HOH B O   1 
HETATM 4136 O O   . HOH F 2 .   ? 4.527   -5.790  35.182  1.00 27.11 ? 263 HOH B O   1 
HETATM 4137 O O   . HOH F 2 .   ? 5.239   1.985   55.902  1.00 21.94 ? 264 HOH B O   1 
HETATM 4138 O O   . HOH F 2 .   ? -18.969 6.386   52.504  1.00 19.33 ? 265 HOH B O   1 
HETATM 4139 O O   . HOH F 2 .   ? -3.982  5.647   55.544  1.00 15.57 ? 266 HOH B O   1 
HETATM 4140 O O   . HOH F 2 .   ? 3.728   -11.524 42.116  1.00 15.52 ? 267 HOH B O   1 
HETATM 4141 O O   . HOH F 2 .   ? -8.052  -11.709 50.725  1.00 16.49 ? 268 HOH B O   1 
HETATM 4142 O O   . HOH F 2 .   ? -1.878  -16.571 61.321  1.00 19.64 ? 269 HOH B O   1 
HETATM 4143 O O   . HOH F 2 .   ? 1.738   -12.365 36.873  1.00 22.49 ? 270 HOH B O   1 
HETATM 4144 O O   . HOH F 2 .   ? 13.407  10.246  37.676  1.00 14.52 ? 271 HOH B O   1 
HETATM 4145 O O   . HOH F 2 .   ? -3.581  7.675   51.300  1.00 23.20 ? 272 HOH B O   1 
HETATM 4146 O O   . HOH F 2 .   ? -4.276  -8.480  51.386  1.00 15.67 ? 273 HOH B O   1 
HETATM 4147 O O   . HOH F 2 .   ? -10.896 -0.869  59.518  1.00 17.13 ? 274 HOH B O   1 
HETATM 4148 O O   . HOH F 2 .   ? -12.802 -5.379  38.114  1.00 18.33 ? 275 HOH B O   1 
HETATM 4149 O O   . HOH F 2 .   ? 0.321   2.545   55.343  1.00 21.46 ? 276 HOH B O   1 
HETATM 4150 O O   . HOH F 2 .   ? -9.481  13.156  46.950  1.00 20.79 ? 277 HOH B O   1 
HETATM 4151 O O   . HOH F 2 .   ? -9.103  -2.717  61.302  1.00 23.32 ? 278 HOH B O   1 
HETATM 4152 O O   . HOH F 2 .   ? -21.984 4.437   48.195  1.00 35.58 ? 279 HOH B O   1 
HETATM 4153 O O   . HOH F 2 .   ? -16.165 -9.682  44.482  1.00 16.39 ? 280 HOH B O   1 
HETATM 4154 O O   . HOH F 2 .   ? 5.853   4.209   27.780  1.00 34.98 ? 281 HOH B O   1 
HETATM 4155 O O   . HOH F 2 .   ? 4.165   -10.224 62.600  1.00 21.70 ? 282 HOH B O   1 
HETATM 4156 O O   . HOH F 2 .   ? -10.881 10.169  42.145  1.00 27.59 ? 283 HOH B O   1 
HETATM 4157 O O   . HOH F 2 .   ? -13.957 9.539   43.055  1.00 22.36 ? 284 HOH B O   1 
HETATM 4158 O O   . HOH F 2 .   ? 6.585   6.862   32.744  1.00 19.45 ? 285 HOH B O   1 
HETATM 4159 O O   . HOH F 2 .   ? -12.264 -3.525  36.421  1.00 13.67 ? 286 HOH B O   1 
HETATM 4160 O O   . HOH F 2 .   ? -3.346  -8.658  61.974  1.00 24.05 ? 287 HOH B O   1 
HETATM 4161 O O   . HOH F 2 .   ? -5.800  -5.971  60.643  1.00 22.90 ? 288 HOH B O   1 
HETATM 4162 O O   . HOH F 2 .   ? 3.079   -11.027 35.368  1.00 21.21 ? 289 HOH B O   1 
HETATM 4163 O O   . HOH F 2 .   ? 12.702  -12.134 51.326  1.00 29.76 ? 290 HOH B O   1 
HETATM 4164 O O   . HOH F 2 .   ? -10.451 7.815   60.426  1.00 26.95 ? 291 HOH B O   1 
HETATM 4165 O O   . HOH F 2 .   ? 2.559   4.829   51.204  1.00 15.47 ? 292 HOH B O   1 
HETATM 4166 O O   . HOH F 2 .   ? 6.399   -8.277  64.404  1.00 30.65 ? 293 HOH B O   1 
HETATM 4167 O O   . HOH F 2 .   ? 7.680   9.994   38.267  1.00 11.81 ? 294 HOH B O   1 
HETATM 4168 O O   . HOH F 2 .   ? -10.411 12.316  43.559  1.00 18.71 ? 295 HOH B O   1 
HETATM 4169 O O   . HOH F 2 .   ? 4.242   -8.754  65.790  1.00 23.56 ? 296 HOH B O   1 
HETATM 4170 O O   . HOH F 2 .   ? 1.284   16.593  35.583  1.00 23.19 ? 297 HOH B O   1 
HETATM 4171 O O   . HOH F 2 .   ? -6.255  -15.121 36.412  1.00 19.33 ? 298 HOH B O   1 
HETATM 4172 O O   . HOH F 2 .   ? 11.118  -4.348  37.321  1.00 52.33 ? 299 HOH B O   1 
HETATM 4173 O O   . HOH F 2 .   ? -14.614 -2.093  38.861  1.00 25.76 ? 300 HOH B O   1 
HETATM 4174 O O   . HOH F 2 .   ? -5.609  -15.194 47.141  1.00 22.48 ? 301 HOH B O   1 
HETATM 4175 O O   . HOH F 2 .   ? -17.493 -9.726  38.224  1.00 20.15 ? 302 HOH B O   1 
HETATM 4176 O O   . HOH F 2 .   ? 7.997   8.886   46.484  1.00 24.23 ? 303 HOH B O   1 
HETATM 4177 O O   . HOH F 2 .   ? -21.019 5.278   52.980  0.50 25.47 ? 304 HOH B O   1 
HETATM 4178 O O   . HOH F 2 .   ? 4.303   4.371   25.670  1.00 31.24 ? 305 HOH B O   1 
HETATM 4179 O O   . HOH F 2 .   ? 0.661   -17.395 63.595  1.00 25.65 ? 306 HOH B O   1 
HETATM 4180 O O   . HOH F 2 .   ? -11.175 -12.927 48.968  1.00 37.24 ? 307 HOH B O   1 
HETATM 4181 O O   . HOH F 2 .   ? 13.736  -5.205  32.903  1.00 21.45 ? 308 HOH B O   1 
HETATM 4182 O O   . HOH F 2 .   ? -12.478 -17.235 44.747  1.00 29.38 ? 309 HOH B O   1 
HETATM 4183 O O   . HOH F 2 .   ? 8.923   4.427   29.448  1.00 18.66 ? 310 HOH B O   1 
HETATM 4184 O O   . HOH F 2 .   ? -9.458  -15.224 48.677  1.00 24.74 ? 311 HOH B O   1 
HETATM 4185 O O   . HOH F 2 .   ? 9.670   2.343   29.686  1.00 21.62 ? 312 HOH B O   1 
HETATM 4186 O O   . HOH F 2 .   ? -13.586 12.387  60.481  1.00 27.31 ? 313 HOH B O   1 
HETATM 4187 O O   . HOH F 2 .   ? 4.052   5.285   53.631  1.00 24.26 ? 314 HOH B O   1 
HETATM 4188 O O   . HOH F 2 .   ? -4.247  -16.731 45.967  1.00 22.79 ? 315 HOH B O   1 
HETATM 4189 O O   . HOH F 2 .   ? 3.067   -12.815 48.039  1.00 30.00 ? 316 HOH B O   1 
HETATM 4190 O O   . HOH F 2 .   ? 7.937   3.590   48.168  1.00 21.65 ? 317 HOH B O   1 
HETATM 4191 O O   . HOH F 2 .   ? 11.884  -3.931  55.890  1.00 32.47 ? 318 HOH B O   1 
HETATM 4192 O O   . HOH F 2 .   ? -4.444  11.538  52.213  1.00 20.79 ? 319 HOH B O   1 
HETATM 4193 O O   . HOH F 2 .   ? 10.144  -0.277  30.127  1.00 31.13 ? 320 HOH B O   1 
HETATM 4194 O O   . HOH F 2 .   ? -5.345  -11.482 50.356  1.00 29.69 ? 321 HOH B O   1 
HETATM 4195 O O   . HOH F 2 .   ? -0.175  4.292   51.546  1.00 18.44 ? 322 HOH B O   1 
HETATM 4196 O O   . HOH F 2 .   ? 9.333   -6.624  46.319  1.00 31.42 ? 323 HOH B O   1 
HETATM 4197 O O   . HOH F 2 .   ? -15.490 -8.581  46.509  1.00 28.05 ? 324 HOH B O   1 
HETATM 4198 O O   . HOH F 2 .   ? -14.274 11.982  63.662  1.00 24.38 ? 325 HOH B O   1 
HETATM 4199 O O   . HOH F 2 .   ? -17.341 -7.437  37.519  1.00 29.27 ? 326 HOH B O   1 
HETATM 4200 O O   . HOH F 2 .   ? 6.037   10.575  39.956  1.00 28.25 ? 327 HOH B O   1 
HETATM 4201 O O   . HOH F 2 .   ? -18.109 3.954   59.596  1.00 26.28 ? 328 HOH B O   1 
HETATM 4202 O O   . HOH F 2 .   ? -17.618 -11.845 36.733  1.00 33.40 ? 329 HOH B O   1 
HETATM 4203 O O   . HOH F 2 .   ? -6.854  -15.887 43.024  1.00 33.31 ? 330 HOH B O   1 
HETATM 4204 O O   . HOH F 2 .   ? -20.001 -4.398  41.390  1.00 28.04 ? 331 HOH B O   1 
HETATM 4205 O O   . HOH F 2 .   ? -0.124  -12.506 49.502  1.00 21.15 ? 332 HOH B O   1 
HETATM 4206 O O   . HOH F 2 .   ? 1.069   -3.100  52.893  1.00 17.56 ? 334 HOH B O   1 
HETATM 4207 O O   . HOH F 2 .   ? 4.694   -11.748 39.601  1.00 34.96 ? 335 HOH B O   1 
HETATM 4208 O O   . HOH F 2 .   ? 0.352   16.601  33.344  1.00 31.57 ? 336 HOH B O   1 
HETATM 4209 O O   . HOH F 2 .   ? -21.713 8.539   55.294  1.00 24.24 ? 337 HOH B O   1 
HETATM 4210 O O   . HOH F 2 .   ? -12.528 -17.398 37.635  1.00 30.45 ? 338 HOH B O   1 
HETATM 4211 O O   . HOH F 2 .   ? -11.827 12.419  53.302  1.00 32.20 ? 339 HOH B O   1 
HETATM 4212 O O   . HOH F 2 .   ? 8.058   12.337  38.803  1.00 28.13 ? 340 HOH B O   1 
HETATM 4213 O O   . HOH F 2 .   ? 6.348   4.968   51.399  1.00 32.01 ? 341 HOH B O   1 
HETATM 4214 O O   . HOH F 2 .   ? 8.927   -5.176  56.005  1.00 34.60 ? 342 HOH B O   1 
HETATM 4215 O O   . HOH F 2 .   ? -15.547 7.580   44.417  1.00 43.11 ? 343 HOH B O   1 
HETATM 4216 O O   . HOH F 2 .   ? 13.341  -6.038  49.106  1.00 32.99 ? 344 HOH B O   1 
HETATM 4217 O O   . HOH G 2 .   ? 46.293  12.115  27.120  1.00 26.66 ? 233 HOH C O   1 
HETATM 4218 O O   . HOH G 2 .   ? 8.784   3.466   40.434  1.00 4.96  ? 235 HOH C O   1 
HETATM 4219 O O   . HOH G 2 .   ? 30.012  2.103   21.918  1.00 4.00  ? 236 HOH C O   1 
HETATM 4220 O O   . HOH G 2 .   ? 31.050  14.305  37.853  1.00 17.90 ? 237 HOH C O   1 
HETATM 4221 O O   . HOH G 2 .   ? 17.309  4.431   37.777  1.00 23.80 ? 238 HOH C O   1 
HETATM 4222 O O   . HOH G 2 .   ? 39.168  12.947  21.631  1.00 16.82 ? 239 HOH C O   1 
HETATM 4223 O O   . HOH G 2 .   ? 37.300  4.619   38.689  1.00 13.99 ? 240 HOH C O   1 
HETATM 4224 O O   . HOH G 2 .   ? 9.951   8.845   31.355  1.00 20.45 ? 241 HOH C O   1 
HETATM 4225 O O   . HOH G 2 .   ? 14.958  -0.303  31.537  1.00 18.67 ? 242 HOH C O   1 
HETATM 4226 O O   . HOH G 2 .   ? 44.420  12.401  30.855  1.00 19.30 ? 243 HOH C O   1 
HETATM 4227 O O   . HOH G 2 .   ? 22.136  8.580   41.998  1.00 21.70 ? 244 HOH C O   1 
HETATM 4228 O O   . HOH G 2 .   ? 15.644  5.280   40.033  1.00 15.96 ? 245 HOH C O   1 
HETATM 4229 O O   . HOH G 2 .   ? 25.469  15.309  33.020  1.00 41.73 ? 246 HOH C O   1 
HETATM 4230 O O   . HOH G 2 .   ? 20.638  -2.598  38.343  1.00 23.65 ? 247 HOH C O   1 
HETATM 4231 O O   . HOH G 2 .   ? 35.362  -3.153  30.454  1.00 17.87 ? 248 HOH C O   1 
HETATM 4232 O O   . HOH G 2 .   ? 18.113  15.056  23.152  1.00 25.91 ? 249 HOH C O   1 
HETATM 4233 O O   . HOH G 2 .   ? 27.584  8.931   15.993  1.00 15.04 ? 250 HOH C O   1 
HETATM 4234 O O   . HOH G 2 .   ? 33.234  9.561   16.543  1.00 48.35 ? 251 HOH C O   1 
HETATM 4235 O O   . HOH G 2 .   ? 22.613  20.429  29.828  1.00 25.40 ? 252 HOH C O   1 
HETATM 4236 O O   . HOH G 2 .   ? 22.794  4.802   43.273  1.00 22.70 ? 253 HOH C O   1 
HETATM 4237 O O   . HOH G 2 .   ? 27.332  13.040  40.769  1.00 25.36 ? 254 HOH C O   1 
HETATM 4238 O O   . HOH G 2 .   ? 41.503  6.894   22.076  1.00 18.36 ? 255 HOH C O   1 
HETATM 4239 O O   . HOH G 2 .   ? 41.726  5.055   20.504  1.00 26.29 ? 256 HOH C O   1 
HETATM 4240 O O   . HOH G 2 .   ? 48.039  3.810   42.158  1.00 27.74 ? 257 HOH C O   1 
HETATM 4241 O O   . HOH G 2 .   ? 42.409  10.691  24.519  1.00 36.09 ? 258 HOH C O   1 
HETATM 4242 O O   . HOH G 2 .   ? 31.243  7.556   19.638  1.00 16.49 ? 259 HOH C O   1 
HETATM 4243 O O   . HOH G 2 .   ? 26.224  8.343   40.327  1.00 30.98 ? 260 HOH C O   1 
HETATM 4244 O O   . HOH G 2 .   ? 30.781  -7.181  33.012  1.00 20.39 ? 261 HOH C O   1 
HETATM 4245 O O   . HOH G 2 .   ? 42.735  22.253  27.514  1.00 26.96 ? 262 HOH C O   1 
HETATM 4246 O O   . HOH G 2 .   ? 31.981  1.282   33.303  1.00 20.41 ? 263 HOH C O   1 
HETATM 4247 O O   . HOH G 2 .   ? 33.236  20.053  27.427  1.00 21.20 ? 264 HOH C O   1 
HETATM 4248 O O   . HOH G 2 .   ? 15.344  0.547   26.266  1.00 20.01 ? 265 HOH C O   1 
HETATM 4249 O O   . HOH G 2 .   ? 16.213  9.161   26.070  1.00 22.44 ? 266 HOH C O   1 
HETATM 4250 O O   . HOH G 2 .   ? 23.821  15.197  12.921  1.00 24.86 ? 267 HOH C O   1 
HETATM 4251 O O   . HOH G 2 .   ? 31.498  19.596  29.375  1.00 24.57 ? 268 HOH C O   1 
HETATM 4252 O O   . HOH G 2 .   ? 42.091  1.743   38.798  1.00 23.30 ? 269 HOH C O   1 
HETATM 4253 O O   . HOH G 2 .   ? 51.710  7.958   36.864  1.00 22.97 ? 270 HOH C O   1 
HETATM 4254 O O   . HOH G 2 .   ? 13.540  -3.392  28.000  1.00 33.34 ? 271 HOH C O   1 
HETATM 4255 O O   . HOH G 2 .   ? 36.979  13.150  19.368  1.00 25.92 ? 272 HOH C O   1 
HETATM 4256 O O   . HOH G 2 .   ? 42.656  0.314   30.479  1.00 25.18 ? 273 HOH C O   1 
HETATM 4257 O O   . HOH G 2 .   ? 33.200  7.093   15.686  1.00 31.67 ? 274 HOH C O   1 
HETATM 4258 O O   . HOH G 2 .   ? 15.638  -0.719  23.821  1.00 24.36 ? 275 HOH C O   1 
HETATM 4259 O O   . HOH G 2 .   ? 19.410  -4.636  26.582  1.00 28.83 ? 276 HOH C O   1 
HETATM 4260 O O   . HOH G 2 .   ? 47.018  1.555   30.601  1.00 29.04 ? 277 HOH C O   1 
HETATM 4261 O O   . HOH G 2 .   ? 45.172  10.607  28.812  1.00 24.03 ? 278 HOH C O   1 
HETATM 4262 O O   . HOH G 2 .   ? 34.479  -2.819  38.012  1.00 26.81 ? 279 HOH C O   1 
HETATM 4263 O O   . HOH G 2 .   ? 42.852  13.655  41.362  1.00 16.85 ? 280 HOH C O   1 
HETATM 4264 O O   . HOH G 2 .   ? 14.662  0.208   21.422  1.00 20.95 ? 281 HOH C O   1 
HETATM 4265 O O   . HOH G 2 .   ? 33.927  4.531   20.174  1.00 22.68 ? 282 HOH C O   1 
HETATM 4266 O O   . HOH G 2 .   ? 20.882  18.984  41.800  1.00 36.11 ? 283 HOH C O   1 
HETATM 4267 O O   . HOH G 2 .   ? 49.673  8.467   34.540  1.00 35.16 ? 284 HOH C O   1 
HETATM 4268 O O   . HOH G 2 .   ? 24.737  13.162  42.089  1.00 37.66 ? 285 HOH C O   1 
HETATM 4269 O O   . HOH G 2 .   ? 19.549  -6.912  24.431  1.00 30.29 ? 286 HOH C O   1 
HETATM 4270 O O   . HOH G 2 .   ? 43.943  12.260  25.773  1.00 34.13 ? 287 HOH C O   1 
HETATM 4271 O O   . HOH G 2 .   ? 44.688  10.799  17.011  1.00 25.86 ? 288 HOH C O   1 
HETATM 4272 O O   . HOH G 2 .   ? 29.380  17.502  13.037  1.00 34.71 ? 289 HOH C O   1 
HETATM 4273 O O   . HOH G 2 .   ? 20.926  20.652  23.816  1.00 36.18 ? 290 HOH C O   1 
HETATM 4274 O O   . HOH G 2 .   ? 44.328  7.996   42.189  1.00 40.79 ? 291 HOH C O   1 
HETATM 4275 O O   . HOH G 2 .   ? 33.847  6.765   19.957  1.00 32.98 ? 292 HOH C O   1 
HETATM 4276 O O   . HOH G 2 .   ? 46.520  -1.457  30.777  1.00 28.84 ? 293 HOH C O   1 
HETATM 4277 O O   . HOH G 2 .   ? 12.567  2.950   26.666  1.00 29.21 ? 294 HOH C O   1 
HETATM 4278 O O   . HOH G 2 .   ? 27.925  -7.020  36.860  1.00 21.85 ? 295 HOH C O   1 
HETATM 4279 O O   . HOH H 2 .   ? 27.996  6.628   15.458  1.00 5.75  ? 154 HOH D O   1 
HETATM 4280 O O   . HOH H 2 .   ? 6.616   -3.443  20.132  1.00 25.71 ? 155 HOH D O   1 
HETATM 4281 O O   . HOH H 2 .   ? 29.579  -0.235  21.745  1.00 9.29  ? 156 HOH D O   1 
HETATM 4282 O O   . HOH H 2 .   ? 29.863  3.826   17.333  1.00 15.66 ? 157 HOH D O   1 
HETATM 4283 O O   . HOH H 2 .   ? 24.925  4.083   -2.454  1.00 10.61 ? 158 HOH D O   1 
HETATM 4284 O O   . HOH H 2 .   ? 27.517  -9.283  20.733  1.00 20.63 ? 159 HOH D O   1 
HETATM 4285 O O   . HOH H 2 .   ? 34.925  7.378   10.118  1.00 32.09 ? 160 HOH D O   1 
HETATM 4286 O O   . HOH H 2 .   ? 17.406  4.634   -2.921  1.00 19.77 ? 161 HOH D O   1 
HETATM 4287 O O   . HOH H 2 .   ? 18.191  -6.805  8.343   1.00 31.43 ? 162 HOH D O   1 
HETATM 4288 O O   . HOH H 2 .   ? 31.654  5.035   -10.963 1.00 23.95 ? 163 HOH D O   1 
HETATM 4289 O O   . HOH H 2 .   ? 4.815   4.355   5.954   1.00 20.36 ? 164 HOH D O   1 
HETATM 4290 O O   . HOH H 2 .   ? 34.302  2.361   18.665  1.00 20.72 ? 165 HOH D O   1 
HETATM 4291 O O   . HOH H 2 .   ? 13.680  -2.186  5.959   1.00 28.36 ? 166 HOH D O   1 
HETATM 4292 O O   . HOH H 2 .   ? 17.685  -6.726  20.380  1.00 30.27 ? 167 HOH D O   1 
HETATM 4293 O O   . HOH H 2 .   ? 29.413  -2.291  16.578  1.00 22.00 ? 168 HOH D O   1 
HETATM 4294 O O   . HOH H 2 .   ? 11.270  1.341   0.818   1.00 22.50 ? 169 HOH D O   1 
HETATM 4295 O O   . HOH H 2 .   ? 4.077   11.339  15.647  1.00 32.56 ? 170 HOH D O   1 
HETATM 4296 O O   . HOH H 2 .   ? 23.629  0.393   -7.961  1.00 19.87 ? 171 HOH D O   1 
HETATM 4297 O O   . HOH H 2 .   ? 26.235  -6.797  23.091  1.00 18.57 ? 172 HOH D O   1 
HETATM 4298 O O   . HOH H 2 .   ? 8.166   10.391  8.830   1.00 29.65 ? 173 HOH D O   1 
HETATM 4299 O O   . HOH H 2 .   ? 27.927  5.870   -5.020  1.00 15.74 ? 174 HOH D O   1 
HETATM 4300 O O   . HOH H 2 .   ? 34.564  -5.527  -0.180  1.00 14.54 ? 175 HOH D O   1 
HETATM 4301 O O   . HOH H 2 .   ? 28.000  8.191   -4.902  1.00 18.51 ? 176 HOH D O   1 
HETATM 4302 O O   . HOH H 2 .   ? 19.370  0.377   -0.373  1.00 26.24 ? 177 HOH D O   1 
HETATM 4303 O O   . HOH H 2 .   ? 28.867  -9.942  5.961   1.00 16.56 ? 178 HOH D O   1 
HETATM 4304 O O   . HOH H 2 .   ? 10.206  -0.273  3.404   1.00 35.36 ? 179 HOH D O   1 
HETATM 4305 O O   . HOH H 2 .   ? 33.576  9.387   9.125   1.00 27.03 ? 180 HOH D O   1 
HETATM 4306 O O   . HOH H 2 .   ? 37.139  -4.443  9.464   1.00 33.79 ? 181 HOH D O   1 
HETATM 4307 O O   . HOH H 2 .   ? 6.713   -2.706  9.519   1.00 23.78 ? 182 HOH D O   1 
HETATM 4308 O O   . HOH H 2 .   ? 28.117  -10.946 8.849   1.00 26.63 ? 183 HOH D O   1 
HETATM 4309 O O   . HOH H 2 .   ? 29.430  -10.148 3.113   1.00 36.06 ? 184 HOH D O   1 
HETATM 4310 O O   . HOH H 2 .   ? 27.894  -12.308 5.401   1.00 21.52 ? 185 HOH D O   1 
HETATM 4311 O O   . HOH H 2 .   ? 33.292  9.043   4.261   1.00 28.67 ? 186 HOH D O   1 
HETATM 4312 O O   . HOH H 2 .   ? 34.720  -3.113  -0.182  1.00 25.67 ? 187 HOH D O   1 
HETATM 4313 O O   . HOH H 2 .   ? 25.379  -10.987 9.114   1.00 26.51 ? 188 HOH D O   1 
HETATM 4314 O O   . HOH H 2 .   ? 24.260  -9.499  5.798   1.00 23.01 ? 189 HOH D O   1 
HETATM 4315 O O   . HOH H 2 .   ? 14.876  3.944   -0.874  1.00 18.92 ? 190 HOH D O   1 
HETATM 4316 O O   . HOH H 2 .   ? 27.454  12.743  5.308   1.00 29.20 ? 191 HOH D O   1 
HETATM 4317 O O   . HOH H 2 .   ? 29.685  0.051   16.496  1.00 34.66 ? 192 HOH D O   1 
HETATM 4318 O O   . HOH H 2 .   ? 37.094  -0.931  0.946   1.00 25.70 ? 193 HOH D O   1 
HETATM 4319 O O   . HOH H 2 .   ? 34.107  -2.698  -11.480 1.00 32.98 ? 194 HOH D O   1 
HETATM 4320 O O   . HOH H 2 .   ? 16.474  -9.182  15.906  1.00 23.60 ? 195 HOH D O   1 
HETATM 4321 O O   . HOH H 2 .   ? 27.771  13.115  2.538   1.00 38.96 ? 196 HOH D O   1 
HETATM 4322 O O   . HOH H 2 .   ? 35.197  13.349  3.240   1.00 30.67 ? 197 HOH D O   1 
HETATM 4323 O O   . HOH H 2 .   ? 28.658  -10.049 -3.846  1.00 40.04 ? 198 HOH D O   1 
HETATM 4324 O O   . HOH H 2 .   ? 28.343  -5.205  -7.192  1.00 26.23 ? 199 HOH D O   1 
HETATM 4325 O O   . HOH H 2 .   ? 33.703  -9.315  9.943   1.00 26.80 ? 200 HOH D O   1 
HETATM 4326 O O   . HOH H 2 .   ? 13.707  -2.192  19.110  1.00 33.80 ? 201 HOH D O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ALA 1   1   1   ALA ALA A . n 
A 1 2   THR 2   2   2   THR THR A . n 
A 1 3   LYS 3   3   3   LYS LYS A . n 
A 1 4   ALA 4   4   4   ALA ALA A . n 
A 1 5   VAL 5   5   5   VAL VAL A . n 
A 1 6   CYS 6   6   6   CYS CYS A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   LEU 8   8   8   LEU LEU A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  GLY 10  10  10  GLY GLY A . n 
A 1 11  ASP 11  11  11  ASP ASP A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  VAL 14  14  14  VAL VAL A . n 
A 1 15  GLN 15  15  15  GLN GLN A . n 
A 1 16  GLY 16  16  16  GLY GLY A . n 
A 1 17  ILE 17  17  17  ILE ILE A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  ASN 19  19  19  ASN ASN A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  GLU 21  21  21  GLU GLU A . n 
A 1 22  GLN 22  22  22  GLN GLN A . n 
A 1 23  LYS 23  23  23  LYS LYS A . n 
A 1 24  GLU 24  24  24  GLU GLU A . n 
A 1 25  SER 25  25  25  SER SER A . n 
A 1 26  ASN 26  26  26  ASN ASN A . n 
A 1 27  GLY 27  27  27  GLY GLY A . n 
A 1 28  PRO 28  28  28  PRO PRO A . n 
A 1 29  VAL 29  29  29  VAL VAL A . n 
A 1 30  LYS 30  30  30  LYS LYS A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  TRP 32  32  32  TRP TRP A . n 
A 1 33  GLY 33  33  33  GLY GLY A . n 
A 1 34  SER 34  34  34  SER SER A . n 
A 1 35  ILE 35  35  35  ILE ILE A . n 
A 1 36  LYS 36  36  36  LYS LYS A . n 
A 1 37  GLY 37  37  37  GLY GLY A . n 
A 1 38  LEU 38  38  38  LEU LEU A . n 
A 1 39  THR 39  39  39  THR THR A . n 
A 1 40  GLU 40  40  40  GLU GLU A . n 
A 1 41  GLY 41  41  41  GLY GLY A . n 
A 1 42  LEU 42  42  42  LEU LEU A . n 
A 1 43  HIS 43  43  43  HIS HIS A . n 
A 1 44  GLY 44  44  44  GLY GLY A . n 
A 1 45  PHE 45  45  45  PHE PHE A . n 
A 1 46  HIS 46  46  46  HIS HIS A . n 
A 1 47  VAL 47  47  47  VAL VAL A . n 
A 1 48  HIS 48  48  48  HIS HIS A . n 
A 1 49  GLU 49  49  49  GLU GLU A . n 
A 1 50  PHE 50  50  50  PHE PHE A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  THR 54  54  54  THR THR A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  GLY 56  56  56  GLY GLY A . n 
A 1 57  CYS 57  57  57  CYS CYS A . n 
A 1 58  THR 58  58  58  THR THR A . n 
A 1 59  SER 59  59  59  SER SER A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  GLY 61  61  61  GLY GLY A . n 
A 1 62  PRO 62  62  62  PRO PRO A . n 
A 1 63  HIS 63  63  63  HIS HIS A . n 
A 1 64  PHE 64  64  64  PHE PHE A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  PRO 66  66  66  PRO PRO A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  SER 68  68  68  SER SER A . n 
A 1 69  ARG 69  69  69  ARG ARG A . n 
A 1 70  LYS 70  70  70  LYS LYS A . n 
A 1 71  HIS 71  71  71  HIS HIS A . n 
A 1 72  GLY 72  72  72  GLY GLY A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LYS 75  75  75  LYS LYS A . n 
A 1 76  ASP 76  76  76  ASP ASP A . n 
A 1 77  GLU 77  77  77  GLU GLU A . n 
A 1 78  GLU 78  78  78  GLU GLU A . n 
A 1 79  ARG 79  79  79  ARG ARG A . n 
A 1 80  HIS 80  80  80  HIS HIS A . n 
A 1 81  VAL 81  81  81  VAL VAL A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  ASP 83  83  83  ASP ASP A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  ASN 86  86  86  ASN ASN A . n 
A 1 87  VAL 87  87  87  VAL VAL A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  ASP 90  90  90  ASP ASP A . n 
A 1 91  LYS 91  91  91  LYS LYS A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  GLY 93  93  93  GLY GLY A . n 
A 1 94  VAL 94  94  94  VAL VAL A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  ASP 96  96  96  ASP ASP A . n 
A 1 97  VAL 97  97  97  VAL VAL A . n 
A 1 98  SER 98  98  98  SER SER A . n 
A 1 99  ILE 99  99  99  ILE ILE A . n 
A 1 100 GLU 100 100 100 GLU GLU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 SER 102 102 102 SER SER A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 ILE 104 104 104 ILE ILE A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 SER 107 107 107 SER SER A . n 
A 1 108 GLY 108 108 108 GLY GLY A . n 
A 1 109 ASP 109 109 109 ASP ASP A . n 
A 1 110 HIS 110 110 110 HIS HIS A . n 
A 1 111 CYS 111 111 111 CYS CYS A . n 
A 1 112 ILE 112 112 112 ILE ILE A . n 
A 1 113 ILE 113 113 113 ILE ILE A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 ARG 115 115 115 ARG ARG A . n 
A 1 116 THR 116 116 116 THR THR A . n 
A 1 117 LEU 117 117 117 LEU LEU A . n 
A 1 118 VAL 118 118 118 VAL VAL A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 HIS 120 120 120 HIS HIS A . n 
A 1 121 GLU 121 121 121 GLU GLU A . n 
A 1 122 LYS 122 122 122 LYS LYS A . n 
A 1 123 ALA 123 123 123 ALA ALA A . n 
A 1 124 ASP 124 124 124 ASP ASP A . n 
A 1 125 ASP 125 125 125 ASP ASP A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 GLY 127 127 127 GLY GLY A . n 
A 1 128 LYS 128 128 128 LYS LYS A . n 
A 1 129 GLY 129 129 129 GLY GLY A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ASN 131 131 131 ASN ASN A . n 
A 1 132 GLU 132 132 132 GLU GLU A . n 
A 1 133 GLU 133 133 133 GLU GLU A . n 
A 1 134 SER 134 134 134 SER SER A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 LYS 136 136 136 LYS LYS A . n 
A 1 137 THR 137 137 137 THR THR A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 ASN 139 139 139 ASN ASN A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 GLY 141 141 141 GLY GLY A . n 
A 1 142 SER 142 142 142 SER SER A . n 
A 1 143 ARG 143 143 143 ARG ARG A . n 
A 1 144 LEU 144 144 144 LEU LEU A . n 
A 1 145 ALA 145 145 145 ALA ALA A . n 
A 1 146 CYS 146 146 146 CYS CYS A . n 
A 1 147 GLY 147 147 147 GLY GLY A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 ILE 149 149 149 ILE ILE A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 ILE 151 151 151 ILE ILE A . n 
A 1 152 ALA 152 152 152 ALA ALA A . n 
A 1 153 GLN 153 153 153 GLN GLN A . n 
B 1 1   ALA 1   1   1   ALA ALA B . n 
B 1 2   THR 2   2   2   THR THR B . n 
B 1 3   LYS 3   3   3   LYS LYS B . n 
B 1 4   ALA 4   4   4   ALA ALA B . n 
B 1 5   VAL 5   5   5   VAL VAL B . n 
B 1 6   CYS 6   6   6   CYS CYS B . n 
B 1 7   VAL 7   7   7   VAL VAL B . n 
B 1 8   LEU 8   8   8   LEU LEU B . n 
B 1 9   LYS 9   9   9   LYS LYS B . n 
B 1 10  GLY 10  10  10  GLY GLY B . n 
B 1 11  ASP 11  11  11  ASP ASP B . n 
B 1 12  GLY 12  12  12  GLY GLY B . n 
B 1 13  PRO 13  13  13  PRO PRO B . n 
B 1 14  VAL 14  14  14  VAL VAL B . n 
B 1 15  GLN 15  15  15  GLN GLN B . n 
B 1 16  GLY 16  16  16  GLY GLY B . n 
B 1 17  ILE 17  17  17  ILE ILE B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  ASN 19  19  19  ASN ASN B . n 
B 1 20  PHE 20  20  20  PHE PHE B . n 
B 1 21  GLU 21  21  21  GLU GLU B . n 
B 1 22  GLN 22  22  22  GLN GLN B . n 
B 1 23  LYS 23  23  23  LYS LYS B . n 
B 1 24  GLU 24  24  24  GLU GLU B . n 
B 1 25  SER 25  25  25  SER SER B . n 
B 1 26  ASN 26  26  26  ASN ASN B . n 
B 1 27  GLY 27  27  27  GLY GLY B . n 
B 1 28  PRO 28  28  28  PRO PRO B . n 
B 1 29  VAL 29  29  29  VAL VAL B . n 
B 1 30  LYS 30  30  30  LYS LYS B . n 
B 1 31  VAL 31  31  31  VAL VAL B . n 
B 1 32  TRP 32  32  32  TRP TRP B . n 
B 1 33  GLY 33  33  33  GLY GLY B . n 
B 1 34  SER 34  34  34  SER SER B . n 
B 1 35  ILE 35  35  35  ILE ILE B . n 
B 1 36  LYS 36  36  36  LYS LYS B . n 
B 1 37  GLY 37  37  37  GLY GLY B . n 
B 1 38  LEU 38  38  38  LEU LEU B . n 
B 1 39  THR 39  39  39  THR THR B . n 
B 1 40  GLU 40  40  40  GLU GLU B . n 
B 1 41  GLY 41  41  41  GLY GLY B . n 
B 1 42  LEU 42  42  42  LEU LEU B . n 
B 1 43  HIS 43  43  43  HIS HIS B . n 
B 1 44  GLY 44  44  44  GLY GLY B . n 
B 1 45  PHE 45  45  45  PHE PHE B . n 
B 1 46  HIS 46  46  46  HIS HIS B . n 
B 1 47  VAL 47  47  47  VAL VAL B . n 
B 1 48  HIS 48  48  48  HIS HIS B . n 
B 1 49  GLU 49  49  49  GLU GLU B . n 
B 1 50  PHE 50  50  50  PHE PHE B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ASP 52  52  52  ASP ASP B . n 
B 1 53  ASN 53  53  53  ASN ASN B . n 
B 1 54  THR 54  54  54  THR THR B . n 
B 1 55  ALA 55  55  55  ALA ALA B . n 
B 1 56  GLY 56  56  56  GLY GLY B . n 
B 1 57  CYS 57  57  57  CYS CYS B . n 
B 1 58  THR 58  58  58  THR THR B . n 
B 1 59  SER 59  59  59  SER SER B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  GLY 61  61  61  GLY GLY B . n 
B 1 62  PRO 62  62  62  PRO PRO B . n 
B 1 63  HIS 63  63  63  HIS HIS B . n 
B 1 64  PHE 64  64  64  PHE PHE B . n 
B 1 65  ASN 65  65  65  ASN ASN B . n 
B 1 66  PRO 66  66  66  PRO PRO B . n 
B 1 67  LEU 67  67  67  LEU LEU B . n 
B 1 68  SER 68  68  68  SER SER B . n 
B 1 69  ARG 69  69  69  ARG ARG B . n 
B 1 70  LYS 70  70  70  LYS LYS B . n 
B 1 71  HIS 71  71  71  HIS HIS B . n 
B 1 72  GLY 72  72  72  GLY GLY B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  LYS 75  75  75  LYS LYS B . n 
B 1 76  ASP 76  76  76  ASP ASP B . n 
B 1 77  GLU 77  77  77  GLU GLU B . n 
B 1 78  GLU 78  78  78  GLU GLU B . n 
B 1 79  ARG 79  79  79  ARG ARG B . n 
B 1 80  HIS 80  80  80  HIS HIS B . n 
B 1 81  VAL 81  81  81  VAL VAL B . n 
B 1 82  GLY 82  82  82  GLY GLY B . n 
B 1 83  ASP 83  83  83  ASP ASP B . n 
B 1 84  LEU 84  84  84  LEU LEU B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  ASN 86  86  86  ASN ASN B . n 
B 1 87  VAL 87  87  87  VAL VAL B . n 
B 1 88  THR 88  88  88  THR THR B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  ASP 90  90  90  ASP ASP B . n 
B 1 91  LYS 91  91  91  LYS LYS B . n 
B 1 92  ASP 92  92  92  ASP ASP B . n 
B 1 93  GLY 93  93  93  GLY GLY B . n 
B 1 94  VAL 94  94  94  VAL VAL B . n 
B 1 95  ALA 95  95  95  ALA ALA B . n 
B 1 96  ASP 96  96  96  ASP ASP B . n 
B 1 97  VAL 97  97  97  VAL VAL B . n 
B 1 98  SER 98  98  98  SER SER B . n 
B 1 99  ILE 99  99  99  ILE ILE B . n 
B 1 100 GLU 100 100 100 GLU GLU B . n 
B 1 101 ASP 101 101 101 ASP ASP B . n 
B 1 102 SER 102 102 102 SER SER B . n 
B 1 103 VAL 103 103 103 VAL VAL B . n 
B 1 104 ILE 104 104 104 ILE ILE B . n 
B 1 105 SER 105 105 105 SER SER B . n 
B 1 106 LEU 106 106 106 LEU LEU B . n 
B 1 107 SER 107 107 107 SER SER B . n 
B 1 108 GLY 108 108 108 GLY GLY B . n 
B 1 109 ASP 109 109 109 ASP ASP B . n 
B 1 110 HIS 110 110 110 HIS HIS B . n 
B 1 111 CYS 111 111 111 CYS CYS B . n 
B 1 112 ILE 112 112 112 ILE ILE B . n 
B 1 113 ILE 113 113 113 ILE ILE B . n 
B 1 114 GLY 114 114 114 GLY GLY B . n 
B 1 115 ARG 115 115 115 ARG ARG B . n 
B 1 116 THR 116 116 116 THR THR B . n 
B 1 117 LEU 117 117 117 LEU LEU B . n 
B 1 118 VAL 118 118 118 VAL VAL B . n 
B 1 119 VAL 119 119 119 VAL VAL B . n 
B 1 120 HIS 120 120 120 HIS HIS B . n 
B 1 121 GLU 121 121 121 GLU GLU B . n 
B 1 122 LYS 122 122 122 LYS LYS B . n 
B 1 123 ALA 123 123 123 ALA ALA B . n 
B 1 124 ASP 124 124 124 ASP ASP B . n 
B 1 125 ASP 125 125 125 ASP ASP B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 GLY 127 127 127 GLY GLY B . n 
B 1 128 LYS 128 128 128 LYS LYS B . n 
B 1 129 GLY 129 129 129 GLY GLY B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 ASN 131 131 131 ASN ASN B . n 
B 1 132 GLU 132 132 132 GLU GLU B . n 
B 1 133 GLU 133 133 133 GLU GLU B . n 
B 1 134 SER 134 134 134 SER SER B . n 
B 1 135 THR 135 135 135 THR THR B . n 
B 1 136 LYS 136 136 136 LYS LYS B . n 
B 1 137 THR 137 137 137 THR THR B . n 
B 1 138 GLY 138 138 138 GLY GLY B . n 
B 1 139 ASN 139 139 139 ASN ASN B . n 
B 1 140 ALA 140 140 140 ALA ALA B . n 
B 1 141 GLY 141 141 141 GLY GLY B . n 
B 1 142 SER 142 142 142 SER SER B . n 
B 1 143 ARG 143 143 143 ARG ARG B . n 
B 1 144 LEU 144 144 144 LEU LEU B . n 
B 1 145 ALA 145 145 145 ALA ALA B . n 
B 1 146 CYS 146 146 146 CYS CYS B . n 
B 1 147 GLY 147 147 147 GLY GLY B . n 
B 1 148 VAL 148 148 148 VAL VAL B . n 
B 1 149 ILE 149 149 149 ILE ILE B . n 
B 1 150 GLY 150 150 150 GLY GLY B . n 
B 1 151 ILE 151 151 151 ILE ILE B . n 
B 1 152 ALA 152 152 152 ALA ALA B . n 
B 1 153 GLN 153 153 153 GLN GLN B . n 
C 1 1   ALA 1   1   1   ALA ALA C . n 
C 1 2   THR 2   2   2   THR THR C . n 
C 1 3   LYS 3   3   3   LYS LYS C . n 
C 1 4   ALA 4   4   4   ALA ALA C . n 
C 1 5   VAL 5   5   5   VAL VAL C . n 
C 1 6   CYS 6   6   6   CYS CYS C . n 
C 1 7   VAL 7   7   7   VAL VAL C . n 
C 1 8   LEU 8   8   8   LEU LEU C . n 
C 1 9   LYS 9   9   9   LYS LYS C . n 
C 1 10  GLY 10  10  10  GLY GLY C . n 
C 1 11  ASP 11  11  11  ASP ASP C . n 
C 1 12  GLY 12  12  12  GLY GLY C . n 
C 1 13  PRO 13  13  13  PRO PRO C . n 
C 1 14  VAL 14  14  14  VAL VAL C . n 
C 1 15  GLN 15  15  15  GLN GLN C . n 
C 1 16  GLY 16  16  16  GLY GLY C . n 
C 1 17  ILE 17  17  17  ILE ILE C . n 
C 1 18  ILE 18  18  18  ILE ILE C . n 
C 1 19  ASN 19  19  19  ASN ASN C . n 
C 1 20  PHE 20  20  20  PHE PHE C . n 
C 1 21  GLU 21  21  21  GLU GLU C . n 
C 1 22  GLN 22  22  22  GLN GLN C . n 
C 1 23  LYS 23  23  23  LYS LYS C . n 
C 1 24  GLU 24  24  24  GLU GLU C . n 
C 1 25  SER 25  25  25  SER SER C . n 
C 1 26  ASN 26  26  26  ASN ASN C . n 
C 1 27  GLY 27  27  27  GLY GLY C . n 
C 1 28  PRO 28  28  28  PRO PRO C . n 
C 1 29  VAL 29  29  29  VAL VAL C . n 
C 1 30  LYS 30  30  30  LYS LYS C . n 
C 1 31  VAL 31  31  31  VAL VAL C . n 
C 1 32  TRP 32  32  32  TRP TRP C . n 
C 1 33  GLY 33  33  33  GLY GLY C . n 
C 1 34  SER 34  34  34  SER SER C . n 
C 1 35  ILE 35  35  35  ILE ILE C . n 
C 1 36  LYS 36  36  36  LYS LYS C . n 
C 1 37  GLY 37  37  37  GLY GLY C . n 
C 1 38  LEU 38  38  38  LEU LEU C . n 
C 1 39  THR 39  39  39  THR THR C . n 
C 1 40  GLU 40  40  40  GLU GLU C . n 
C 1 41  GLY 41  41  41  GLY GLY C . n 
C 1 42  LEU 42  42  42  LEU LEU C . n 
C 1 43  HIS 43  43  43  HIS HIS C . n 
C 1 44  GLY 44  44  44  GLY GLY C . n 
C 1 45  PHE 45  45  45  PHE PHE C . n 
C 1 46  HIS 46  46  46  HIS HIS C . n 
C 1 47  VAL 47  47  47  VAL VAL C . n 
C 1 48  HIS 48  48  48  HIS HIS C . n 
C 1 49  GLU 49  49  49  GLU GLU C . n 
C 1 50  PHE 50  50  50  PHE PHE C . n 
C 1 51  GLY 51  51  51  GLY GLY C . n 
C 1 52  ASP 52  52  52  ASP ASP C . n 
C 1 53  ASN 53  53  53  ASN ASN C . n 
C 1 54  THR 54  54  54  THR THR C . n 
C 1 55  ALA 55  55  55  ALA ALA C . n 
C 1 56  GLY 56  56  56  GLY GLY C . n 
C 1 57  CYS 57  57  57  CYS CYS C . n 
C 1 58  THR 58  58  58  THR THR C . n 
C 1 59  SER 59  59  59  SER SER C . n 
C 1 60  ALA 60  60  60  ALA ALA C . n 
C 1 61  GLY 61  61  61  GLY GLY C . n 
C 1 62  PRO 62  62  62  PRO PRO C . n 
C 1 63  HIS 63  63  63  HIS HIS C . n 
C 1 64  PHE 64  64  64  PHE PHE C . n 
C 1 65  ASN 65  65  65  ASN ASN C . n 
C 1 66  PRO 66  66  66  PRO PRO C . n 
C 1 67  LEU 67  67  67  LEU LEU C . n 
C 1 68  SER 68  68  ?   ?   ?   C . n 
C 1 69  ARG 69  69  ?   ?   ?   C . n 
C 1 70  LYS 70  70  ?   ?   ?   C . n 
C 1 71  HIS 71  71  ?   ?   ?   C . n 
C 1 72  GLY 72  72  ?   ?   ?   C . n 
C 1 73  GLY 73  73  ?   ?   ?   C . n 
C 1 74  PRO 74  74  ?   ?   ?   C . n 
C 1 75  LYS 75  75  ?   ?   ?   C . n 
C 1 76  ASP 76  76  ?   ?   ?   C . n 
C 1 77  GLU 77  77  ?   ?   ?   C . n 
C 1 78  GLU 78  78  ?   ?   ?   C . n 
C 1 79  ARG 79  79  79  ARG ARG C . n 
C 1 80  HIS 80  80  80  HIS HIS C . n 
C 1 81  VAL 81  81  81  VAL VAL C . n 
C 1 82  GLY 82  82  82  GLY GLY C . n 
C 1 83  ASP 83  83  83  ASP ASP C . n 
C 1 84  LEU 84  84  84  LEU LEU C . n 
C 1 85  GLY 85  85  85  GLY GLY C . n 
C 1 86  ASN 86  86  86  ASN ASN C . n 
C 1 87  VAL 87  87  87  VAL VAL C . n 
C 1 88  THR 88  88  88  THR THR C . n 
C 1 89  ALA 89  89  89  ALA ALA C . n 
C 1 90  ASP 90  90  90  ASP ASP C . n 
C 1 91  LYS 91  91  91  LYS LYS C . n 
C 1 92  ASP 92  92  92  ASP ASP C . n 
C 1 93  GLY 93  93  93  GLY GLY C . n 
C 1 94  VAL 94  94  94  VAL VAL C . n 
C 1 95  ALA 95  95  95  ALA ALA C . n 
C 1 96  ASP 96  96  96  ASP ASP C . n 
C 1 97  VAL 97  97  97  VAL VAL C . n 
C 1 98  SER 98  98  98  SER SER C . n 
C 1 99  ILE 99  99  99  ILE ILE C . n 
C 1 100 GLU 100 100 100 GLU GLU C . n 
C 1 101 ASP 101 101 101 ASP ASP C . n 
C 1 102 SER 102 102 102 SER SER C . n 
C 1 103 VAL 103 103 103 VAL VAL C . n 
C 1 104 ILE 104 104 104 ILE ILE C . n 
C 1 105 SER 105 105 105 SER SER C . n 
C 1 106 LEU 106 106 106 LEU LEU C . n 
C 1 107 SER 107 107 107 SER SER C . n 
C 1 108 GLY 108 108 108 GLY GLY C . n 
C 1 109 ASP 109 109 109 ASP ASP C . n 
C 1 110 HIS 110 110 110 HIS HIS C . n 
C 1 111 CYS 111 111 111 CYS CYS C . n 
C 1 112 ILE 112 112 112 ILE ILE C . n 
C 1 113 ILE 113 113 113 ILE ILE C . n 
C 1 114 GLY 114 114 114 GLY GLY C . n 
C 1 115 ARG 115 115 115 ARG ARG C . n 
C 1 116 THR 116 116 116 THR THR C . n 
C 1 117 LEU 117 117 117 LEU LEU C . n 
C 1 118 VAL 118 118 118 VAL VAL C . n 
C 1 119 VAL 119 119 119 VAL VAL C . n 
C 1 120 HIS 120 120 120 HIS HIS C . n 
C 1 121 GLU 121 121 121 GLU GLU C . n 
C 1 122 LYS 122 122 122 LYS LYS C . n 
C 1 123 ALA 123 123 123 ALA ALA C . n 
C 1 124 ASP 124 124 124 ASP ASP C . n 
C 1 125 ASP 125 125 ?   ?   ?   C . n 
C 1 126 LEU 126 126 ?   ?   ?   C . n 
C 1 127 GLY 127 127 ?   ?   ?   C . n 
C 1 128 LYS 128 128 ?   ?   ?   C . n 
C 1 129 GLY 129 129 ?   ?   ?   C . n 
C 1 130 GLY 130 130 ?   ?   ?   C . n 
C 1 131 ASN 131 131 ?   ?   ?   C . n 
C 1 132 GLU 132 132 ?   ?   ?   C . n 
C 1 133 GLU 133 133 ?   ?   ?   C . n 
C 1 134 SER 134 134 ?   ?   ?   C . n 
C 1 135 THR 135 135 ?   ?   ?   C . n 
C 1 136 LYS 136 136 ?   ?   ?   C . n 
C 1 137 THR 137 137 ?   ?   ?   C . n 
C 1 138 GLY 138 138 ?   ?   ?   C . n 
C 1 139 ASN 139 139 ?   ?   ?   C . n 
C 1 140 ALA 140 140 ?   ?   ?   C . n 
C 1 141 GLY 141 141 141 GLY GLY C . n 
C 1 142 SER 142 142 142 SER SER C . n 
C 1 143 ARG 143 143 143 ARG ARG C . n 
C 1 144 LEU 144 144 144 LEU LEU C . n 
C 1 145 ALA 145 145 145 ALA ALA C . n 
C 1 146 CYS 146 146 146 CYS CYS C . n 
C 1 147 GLY 147 147 147 GLY GLY C . n 
C 1 148 VAL 148 148 148 VAL VAL C . n 
C 1 149 ILE 149 149 149 ILE ILE C . n 
C 1 150 GLY 150 150 150 GLY GLY C . n 
C 1 151 ILE 151 151 151 ILE ILE C . n 
C 1 152 ALA 152 152 152 ALA ALA C . n 
C 1 153 GLN 153 153 153 GLN GLN C . n 
D 1 1   ALA 1   1   1   ALA ALA D . n 
D 1 2   THR 2   2   2   THR THR D . n 
D 1 3   LYS 3   3   3   LYS LYS D . n 
D 1 4   ALA 4   4   4   ALA ALA D . n 
D 1 5   VAL 5   5   5   VAL VAL D . n 
D 1 6   CYS 6   6   6   CYS CYS D . n 
D 1 7   VAL 7   7   7   VAL VAL D . n 
D 1 8   LEU 8   8   8   LEU LEU D . n 
D 1 9   LYS 9   9   9   LYS LYS D . n 
D 1 10  GLY 10  10  10  GLY GLY D . n 
D 1 11  ASP 11  11  11  ASP ASP D . n 
D 1 12  GLY 12  12  12  GLY GLY D . n 
D 1 13  PRO 13  13  13  PRO PRO D . n 
D 1 14  VAL 14  14  14  VAL VAL D . n 
D 1 15  GLN 15  15  15  GLN GLN D . n 
D 1 16  GLY 16  16  16  GLY GLY D . n 
D 1 17  ILE 17  17  17  ILE ILE D . n 
D 1 18  ILE 18  18  18  ILE ILE D . n 
D 1 19  ASN 19  19  19  ASN ASN D . n 
D 1 20  PHE 20  20  20  PHE PHE D . n 
D 1 21  GLU 21  21  21  GLU GLU D . n 
D 1 22  GLN 22  22  22  GLN GLN D . n 
D 1 23  LYS 23  23  23  LYS LYS D . n 
D 1 24  GLU 24  24  24  GLU GLU D . n 
D 1 25  SER 25  25  25  SER SER D . n 
D 1 26  ASN 26  26  26  ASN ASN D . n 
D 1 27  GLY 27  27  27  GLY GLY D . n 
D 1 28  PRO 28  28  28  PRO PRO D . n 
D 1 29  VAL 29  29  29  VAL VAL D . n 
D 1 30  LYS 30  30  30  LYS LYS D . n 
D 1 31  VAL 31  31  31  VAL VAL D . n 
D 1 32  TRP 32  32  32  TRP TRP D . n 
D 1 33  GLY 33  33  33  GLY GLY D . n 
D 1 34  SER 34  34  34  SER SER D . n 
D 1 35  ILE 35  35  35  ILE ILE D . n 
D 1 36  LYS 36  36  36  LYS LYS D . n 
D 1 37  GLY 37  37  37  GLY GLY D . n 
D 1 38  LEU 38  38  38  LEU LEU D . n 
D 1 39  THR 39  39  39  THR THR D . n 
D 1 40  GLU 40  40  40  GLU GLU D . n 
D 1 41  GLY 41  41  41  GLY GLY D . n 
D 1 42  LEU 42  42  42  LEU LEU D . n 
D 1 43  HIS 43  43  43  HIS HIS D . n 
D 1 44  GLY 44  44  44  GLY GLY D . n 
D 1 45  PHE 45  45  45  PHE PHE D . n 
D 1 46  HIS 46  46  46  HIS HIS D . n 
D 1 47  VAL 47  47  47  VAL VAL D . n 
D 1 48  HIS 48  48  48  HIS HIS D . n 
D 1 49  GLU 49  49  49  GLU GLU D . n 
D 1 50  PHE 50  50  50  PHE PHE D . n 
D 1 51  GLY 51  51  51  GLY GLY D . n 
D 1 52  ASP 52  52  52  ASP ASP D . n 
D 1 53  ASN 53  53  53  ASN ASN D . n 
D 1 54  THR 54  54  54  THR THR D . n 
D 1 55  ALA 55  55  55  ALA ALA D . n 
D 1 56  GLY 56  56  56  GLY GLY D . n 
D 1 57  CYS 57  57  57  CYS CYS D . n 
D 1 58  THR 58  58  58  THR THR D . n 
D 1 59  SER 59  59  59  SER SER D . n 
D 1 60  ALA 60  60  60  ALA ALA D . n 
D 1 61  GLY 61  61  61  GLY GLY D . n 
D 1 62  PRO 62  62  62  PRO PRO D . n 
D 1 63  HIS 63  63  63  HIS HIS D . n 
D 1 64  PHE 64  64  64  PHE PHE D . n 
D 1 65  ASN 65  65  65  ASN ASN D . n 
D 1 66  PRO 66  66  66  PRO PRO D . n 
D 1 67  LEU 67  67  ?   ?   ?   D . n 
D 1 68  SER 68  68  ?   ?   ?   D . n 
D 1 69  ARG 69  69  ?   ?   ?   D . n 
D 1 70  LYS 70  70  ?   ?   ?   D . n 
D 1 71  HIS 71  71  ?   ?   ?   D . n 
D 1 72  GLY 72  72  ?   ?   ?   D . n 
D 1 73  GLY 73  73  ?   ?   ?   D . n 
D 1 74  PRO 74  74  ?   ?   ?   D . n 
D 1 75  LYS 75  75  ?   ?   ?   D . n 
D 1 76  ASP 76  76  ?   ?   ?   D . n 
D 1 77  GLU 77  77  ?   ?   ?   D . n 
D 1 78  GLU 78  78  ?   ?   ?   D . n 
D 1 79  ARG 79  79  ?   ?   ?   D . n 
D 1 80  HIS 80  80  80  HIS HIS D . n 
D 1 81  VAL 81  81  81  VAL VAL D . n 
D 1 82  GLY 82  82  82  GLY GLY D . n 
D 1 83  ASP 83  83  83  ASP ASP D . n 
D 1 84  LEU 84  84  84  LEU LEU D . n 
D 1 85  GLY 85  85  85  GLY GLY D . n 
D 1 86  ASN 86  86  86  ASN ASN D . n 
D 1 87  VAL 87  87  87  VAL VAL D . n 
D 1 88  THR 88  88  88  THR THR D . n 
D 1 89  ALA 89  89  89  ALA ALA D . n 
D 1 90  ASP 90  90  90  ASP ASP D . n 
D 1 91  LYS 91  91  91  LYS LYS D . n 
D 1 92  ASP 92  92  92  ASP ASP D . n 
D 1 93  GLY 93  93  93  GLY GLY D . n 
D 1 94  VAL 94  94  94  VAL VAL D . n 
D 1 95  ALA 95  95  95  ALA ALA D . n 
D 1 96  ASP 96  96  96  ASP ASP D . n 
D 1 97  VAL 97  97  97  VAL VAL D . n 
D 1 98  SER 98  98  98  SER SER D . n 
D 1 99  ILE 99  99  99  ILE ILE D . n 
D 1 100 GLU 100 100 100 GLU GLU D . n 
D 1 101 ASP 101 101 101 ASP ASP D . n 
D 1 102 SER 102 102 102 SER SER D . n 
D 1 103 VAL 103 103 103 VAL VAL D . n 
D 1 104 ILE 104 104 104 ILE ILE D . n 
D 1 105 SER 105 105 105 SER SER D . n 
D 1 106 LEU 106 106 106 LEU LEU D . n 
D 1 107 SER 107 107 107 SER SER D . n 
D 1 108 GLY 108 108 108 GLY GLY D . n 
D 1 109 ASP 109 109 109 ASP ASP D . n 
D 1 110 HIS 110 110 110 HIS HIS D . n 
D 1 111 CYS 111 111 111 CYS CYS D . n 
D 1 112 ILE 112 112 112 ILE ILE D . n 
D 1 113 ILE 113 113 113 ILE ILE D . n 
D 1 114 GLY 114 114 114 GLY GLY D . n 
D 1 115 ARG 115 115 115 ARG ARG D . n 
D 1 116 THR 116 116 116 THR THR D . n 
D 1 117 LEU 117 117 117 LEU LEU D . n 
D 1 118 VAL 118 118 118 VAL VAL D . n 
D 1 119 VAL 119 119 119 VAL VAL D . n 
D 1 120 HIS 120 120 120 HIS HIS D . n 
D 1 121 GLU 121 121 121 GLU GLU D . n 
D 1 122 LYS 122 122 122 LYS LYS D . n 
D 1 123 ALA 123 123 123 ALA ALA D . n 
D 1 124 ASP 124 124 124 ASP ASP D . n 
D 1 125 ASP 125 125 ?   ?   ?   D . n 
D 1 126 LEU 126 126 ?   ?   ?   D . n 
D 1 127 GLY 127 127 ?   ?   ?   D . n 
D 1 128 LYS 128 128 ?   ?   ?   D . n 
D 1 129 GLY 129 129 ?   ?   ?   D . n 
D 1 130 GLY 130 130 ?   ?   ?   D . n 
D 1 131 ASN 131 131 ?   ?   ?   D . n 
D 1 132 GLU 132 132 ?   ?   ?   D . n 
D 1 133 GLU 133 133 ?   ?   ?   D . n 
D 1 134 SER 134 134 ?   ?   ?   D . n 
D 1 135 THR 135 135 ?   ?   ?   D . n 
D 1 136 LYS 136 136 ?   ?   ?   D . n 
D 1 137 THR 137 137 ?   ?   ?   D . n 
D 1 138 GLY 138 138 ?   ?   ?   D . n 
D 1 139 ASN 139 139 ?   ?   ?   D . n 
D 1 140 ALA 140 140 ?   ?   ?   D . n 
D 1 141 GLY 141 141 ?   ?   ?   D . n 
D 1 142 SER 142 142 142 SER SER D . n 
D 1 143 ARG 143 143 143 ARG ARG D . n 
D 1 144 LEU 144 144 144 LEU LEU D . n 
D 1 145 ALA 145 145 145 ALA ALA D . n 
D 1 146 CYS 146 146 146 CYS CYS D . n 
D 1 147 GLY 147 147 147 GLY GLY D . n 
D 1 148 VAL 148 148 148 VAL VAL D . n 
D 1 149 ILE 149 149 149 ILE ILE D . n 
D 1 150 GLY 150 150 150 GLY GLY D . n 
D 1 151 ILE 151 151 151 ILE ILE D . n 
D 1 152 ALA 152 152 152 ALA ALA D . n 
D 1 153 GLN 153 153 153 GLN GLN D . n 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA dimeric 2 
2 author_and_software_defined_assembly PISA dimeric 2 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,E,F 
2 1 C,D,G,H 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1410  ? 
1 MORE         -12   ? 
1 'SSA (A^2)'  13780 ? 
2 'ABSA (A^2)' 1440  ? 
2 MORE         -12   ? 
2 'SSA (A^2)'  11310 ? 
# 
_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 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    B 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     304 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   F 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
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 2009-05-19 
2 'Structure model' 1 1 2011-07-13 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Version format compliance' 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
CrysalisPro 'data collection' .        ? 1 
MOLREP      phasing           .        ? 2 
REFMAC      refinement        5.2.0019 ? 3 
MOSFLM      'data reduction'  .        ? 4 
SCALA       'data scaling'    .        ? 5 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   NH2 
_pdbx_validate_close_contact.auth_asym_id_1   C 
_pdbx_validate_close_contact.auth_comp_id_1   ARG 
_pdbx_validate_close_contact.auth_seq_id_1    79 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   OD1 
_pdbx_validate_close_contact.auth_asym_id_2   C 
_pdbx_validate_close_contact.auth_comp_id_2   ASP 
_pdbx_validate_close_contact.auth_seq_id_2    101 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.06 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CB A VAL 5   ? ? CG2 A VAL 5   ? ? 1.669 1.524 0.145  0.021 N 
2 1 CB A VAL 47  ? ? CG2 A VAL 47  ? ? 1.688 1.524 0.164  0.021 N 
3 1 CB B VAL 5   ? ? CG2 B VAL 5   ? ? 1.664 1.524 0.140  0.021 N 
4 1 CB B CYS 146 ? ? SG  B CYS 146 ? ? 1.682 1.812 -0.130 0.016 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1  1 CA A LEU 8   ? ? CB A LEU 8   ? ? CG  A LEU 8   ? ? 135.65 115.30 20.35  2.30 N 
2  1 CB A LEU 42  ? ? CG A LEU 42  ? ? CD2 A LEU 42  ? ? 100.57 111.00 -10.43 1.70 N 
3  1 NE A ARG 69  ? ? CZ A ARG 69  ? ? NH1 A ARG 69  ? ? 123.47 120.30 3.17   0.50 N 
4  1 NE A ARG 69  ? ? CZ A ARG 69  ? ? NH2 A ARG 69  ? ? 116.99 120.30 -3.31  0.50 N 
5  1 CA B LEU 8   ? ? CB B LEU 8   ? ? CG  B LEU 8   ? ? 132.07 115.30 16.77  2.30 N 
6  1 CB B LEU 38  ? ? CG B LEU 38  ? ? CD1 B LEU 38  ? ? 126.36 111.00 15.36  1.70 N 
7  1 NE B ARG 79  ? ? CZ B ARG 79  ? ? NH2 B ARG 79  ? ? 117.08 120.30 -3.22  0.50 N 
8  1 CB B ASP 90  ? ? CG B ASP 90  ? ? OD1 B ASP 90  ? ? 124.58 118.30 6.28   0.90 N 
9  1 NE B ARG 115 ? ? CZ B ARG 115 ? ? NH1 B ARG 115 ? ? 123.83 120.30 3.53   0.50 N 
10 1 CA C LEU 38  ? ? CB C LEU 38  ? ? CG  C LEU 38  ? ? 129.74 115.30 14.44  2.30 N 
11 1 NE C ARG 115 ? ? CZ C ARG 115 ? ? NH1 C ARG 115 ? ? 123.46 120.30 3.16   0.50 N 
12 1 CA D LEU 8   ? ? CB D LEU 8   ? ? CG  D LEU 8   ? ? 130.72 115.30 15.42  2.30 N 
13 1 CA D LEU 38  ? ? CB D LEU 38  ? ? CG  D LEU 38  ? ? 129.65 115.30 14.35  2.30 N 
14 1 CA D LEU 42  ? ? CB D LEU 42  ? ? CG  D LEU 42  ? ? 129.97 115.30 14.67  2.30 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 SER A 68  ? ? 37.96   36.36   
2  1 ASP A 90  ? ? -58.76  -179.58 
3  1 SER A 98  ? ? -153.48 84.64   
4  1 ARG A 115 ? ? -109.30 -160.80 
5  1 LYS A 128 ? ? -103.25 48.71   
6  1 ALA A 145 ? ? -176.55 137.94  
7  1 PRO B 62  ? ? -68.53  -175.97 
8  1 ASP B 90  ? ? -69.99  -171.54 
9  1 ARG B 115 ? ? -106.37 -162.83 
10 1 LYS B 128 ? ? -102.91 50.17   
11 1 LYS B 136 ? ? -101.38 -62.86  
12 1 ALA C 55  ? ? -108.52 52.03   
13 1 ASN C 65  ? ? -170.35 74.76   
14 1 SER D 25  ? ? -24.24  -64.07  
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   ILE 
_pdbx_validate_peptide_omega.auth_asym_id_1   B 
_pdbx_validate_peptide_omega.auth_seq_id_1    99 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   GLU 
_pdbx_validate_peptide_omega.auth_asym_id_2   B 
_pdbx_validate_peptide_omega.auth_seq_id_2    100 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            142.01 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 C SER 68  ? C SER 68  
2  1 Y 1 C ARG 69  ? C ARG 69  
3  1 Y 1 C LYS 70  ? C LYS 70  
4  1 Y 1 C HIS 71  ? C HIS 71  
5  1 Y 1 C GLY 72  ? C GLY 72  
6  1 Y 1 C GLY 73  ? C GLY 73  
7  1 Y 1 C PRO 74  ? C PRO 74  
8  1 Y 1 C LYS 75  ? C LYS 75  
9  1 Y 1 C ASP 76  ? C ASP 76  
10 1 Y 1 C GLU 77  ? C GLU 77  
11 1 Y 1 C GLU 78  ? C GLU 78  
12 1 Y 1 C ASP 125 ? C ASP 125 
13 1 Y 1 C LEU 126 ? C LEU 126 
14 1 Y 1 C GLY 127 ? C GLY 127 
15 1 Y 1 C LYS 128 ? C LYS 128 
16 1 Y 1 C GLY 129 ? C GLY 129 
17 1 Y 1 C GLY 130 ? C GLY 130 
18 1 Y 1 C ASN 131 ? C ASN 131 
19 1 Y 1 C GLU 132 ? C GLU 132 
20 1 Y 1 C GLU 133 ? C GLU 133 
21 1 Y 1 C SER 134 ? C SER 134 
22 1 Y 1 C THR 135 ? C THR 135 
23 1 Y 1 C LYS 136 ? C LYS 136 
24 1 Y 1 C THR 137 ? C THR 137 
25 1 Y 1 C GLY 138 ? C GLY 138 
26 1 Y 1 C ASN 139 ? C ASN 139 
27 1 Y 1 C ALA 140 ? C ALA 140 
28 1 Y 1 D LEU 67  ? D LEU 67  
29 1 Y 1 D SER 68  ? D SER 68  
30 1 Y 1 D ARG 69  ? D ARG 69  
31 1 Y 1 D LYS 70  ? D LYS 70  
32 1 Y 1 D HIS 71  ? D HIS 71  
33 1 Y 1 D GLY 72  ? D GLY 72  
34 1 Y 1 D GLY 73  ? D GLY 73  
35 1 Y 1 D PRO 74  ? D PRO 74  
36 1 Y 1 D LYS 75  ? D LYS 75  
37 1 Y 1 D ASP 76  ? D ASP 76  
38 1 Y 1 D GLU 77  ? D GLU 77  
39 1 Y 1 D GLU 78  ? D GLU 78  
40 1 Y 1 D ARG 79  ? D ARG 79  
41 1 Y 1 D ASP 125 ? D ASP 125 
42 1 Y 1 D LEU 126 ? D LEU 126 
43 1 Y 1 D GLY 127 ? D GLY 127 
44 1 Y 1 D LYS 128 ? D LYS 128 
45 1 Y 1 D GLY 129 ? D GLY 129 
46 1 Y 1 D GLY 130 ? D GLY 130 
47 1 Y 1 D ASN 131 ? D ASN 131 
48 1 Y 1 D GLU 132 ? D GLU 132 
49 1 Y 1 D GLU 133 ? D GLU 133 
50 1 Y 1 D SER 134 ? D SER 134 
51 1 Y 1 D THR 135 ? D THR 135 
52 1 Y 1 D LYS 136 ? D LYS 136 
53 1 Y 1 D THR 137 ? D THR 137 
54 1 Y 1 D GLY 138 ? D GLY 138 
55 1 Y 1 D ASN 139 ? D ASN 139 
56 1 Y 1 D ALA 140 ? D ALA 140 
57 1 Y 1 D GLY 141 ? D GLY 141 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
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 
E 2 HOH 1   154 154 HOH HOH A . 
E 2 HOH 2   155 155 HOH HOH A . 
E 2 HOH 3   156 156 HOH HOH A . 
E 2 HOH 4   157 157 HOH HOH A . 
E 2 HOH 5   158 158 HOH HOH A . 
E 2 HOH 6   159 159 HOH HOH A . 
E 2 HOH 7   160 160 HOH HOH A . 
E 2 HOH 8   161 161 HOH HOH A . 
E 2 HOH 9   162 162 HOH HOH A . 
E 2 HOH 10  163 163 HOH HOH A . 
E 2 HOH 11  164 164 HOH HOH A . 
E 2 HOH 12  165 165 HOH HOH A . 
E 2 HOH 13  166 166 HOH HOH A . 
E 2 HOH 14  167 167 HOH HOH A . 
E 2 HOH 15  168 168 HOH HOH A . 
E 2 HOH 16  169 169 HOH HOH A . 
E 2 HOH 17  170 170 HOH HOH A . 
E 2 HOH 18  171 171 HOH HOH A . 
E 2 HOH 19  172 172 HOH HOH A . 
E 2 HOH 20  173 173 HOH HOH A . 
E 2 HOH 21  174 174 HOH HOH A . 
E 2 HOH 22  175 175 HOH HOH A . 
E 2 HOH 23  176 176 HOH HOH A . 
E 2 HOH 24  177 177 HOH HOH A . 
E 2 HOH 25  178 178 HOH HOH A . 
E 2 HOH 26  179 179 HOH HOH A . 
E 2 HOH 27  180 180 HOH HOH A . 
E 2 HOH 28  181 181 HOH HOH A . 
E 2 HOH 29  182 182 HOH HOH A . 
E 2 HOH 30  183 183 HOH HOH A . 
E 2 HOH 31  184 184 HOH HOH A . 
E 2 HOH 32  185 185 HOH HOH A . 
E 2 HOH 33  186 186 HOH HOH A . 
E 2 HOH 34  187 187 HOH HOH A . 
E 2 HOH 35  188 188 HOH HOH A . 
E 2 HOH 36  189 189 HOH HOH A . 
E 2 HOH 37  190 190 HOH HOH A . 
E 2 HOH 38  191 191 HOH HOH A . 
E 2 HOH 39  192 192 HOH HOH A . 
E 2 HOH 40  193 193 HOH HOH A . 
E 2 HOH 41  194 194 HOH HOH A . 
E 2 HOH 42  195 195 HOH HOH A . 
E 2 HOH 43  196 196 HOH HOH A . 
E 2 HOH 44  197 197 HOH HOH A . 
E 2 HOH 45  198 198 HOH HOH A . 
E 2 HOH 46  199 199 HOH HOH A . 
E 2 HOH 47  200 200 HOH HOH A . 
E 2 HOH 48  201 201 HOH HOH A . 
E 2 HOH 49  202 202 HOH HOH A . 
E 2 HOH 50  203 203 HOH HOH A . 
E 2 HOH 51  204 204 HOH HOH A . 
E 2 HOH 52  205 205 HOH HOH A . 
E 2 HOH 53  206 206 HOH HOH A . 
E 2 HOH 54  207 207 HOH HOH A . 
E 2 HOH 55  208 208 HOH HOH A . 
E 2 HOH 56  209 209 HOH HOH A . 
E 2 HOH 57  210 210 HOH HOH A . 
E 2 HOH 58  211 211 HOH HOH A . 
E 2 HOH 59  212 212 HOH HOH A . 
E 2 HOH 60  213 213 HOH HOH A . 
E 2 HOH 61  214 214 HOH HOH A . 
E 2 HOH 62  215 215 HOH HOH A . 
E 2 HOH 63  216 216 HOH HOH A . 
E 2 HOH 64  217 217 HOH HOH A . 
E 2 HOH 65  218 218 HOH HOH A . 
E 2 HOH 66  219 219 HOH HOH A . 
E 2 HOH 67  220 220 HOH HOH A . 
E 2 HOH 68  221 221 HOH HOH A . 
E 2 HOH 69  222 222 HOH HOH A . 
E 2 HOH 70  223 223 HOH HOH A . 
E 2 HOH 71  224 224 HOH HOH A . 
E 2 HOH 72  225 225 HOH HOH A . 
E 2 HOH 73  226 226 HOH HOH A . 
E 2 HOH 74  228 228 HOH HOH A . 
E 2 HOH 75  229 229 HOH HOH A . 
E 2 HOH 76  230 230 HOH HOH A . 
E 2 HOH 77  231 231 HOH HOH A . 
E 2 HOH 78  232 232 HOH HOH A . 
E 2 HOH 79  234 234 HOH HOH A . 
E 2 HOH 80  235 235 HOH HOH A . 
E 2 HOH 81  236 236 HOH HOH A . 
E 2 HOH 82  237 237 HOH HOH A . 
E 2 HOH 83  238 238 HOH HOH A . 
E 2 HOH 84  239 239 HOH HOH A . 
F 2 HOH 1   234 234 HOH HOH B . 
F 2 HOH 2   240 240 HOH HOH B . 
F 2 HOH 3   241 241 HOH HOH B . 
F 2 HOH 4   242 242 HOH HOH B . 
F 2 HOH 5   243 243 HOH HOH B . 
F 2 HOH 6   244 244 HOH HOH B . 
F 2 HOH 7   245 245 HOH HOH B . 
F 2 HOH 8   246 246 HOH HOH B . 
F 2 HOH 9   247 247 HOH HOH B . 
F 2 HOH 10  248 248 HOH HOH B . 
F 2 HOH 11  249 249 HOH HOH B . 
F 2 HOH 12  250 250 HOH HOH B . 
F 2 HOH 13  251 251 HOH HOH B . 
F 2 HOH 14  252 252 HOH HOH B . 
F 2 HOH 15  253 253 HOH HOH B . 
F 2 HOH 16  254 254 HOH HOH B . 
F 2 HOH 17  255 255 HOH HOH B . 
F 2 HOH 18  256 256 HOH HOH B . 
F 2 HOH 19  257 257 HOH HOH B . 
F 2 HOH 20  258 258 HOH HOH B . 
F 2 HOH 21  259 259 HOH HOH B . 
F 2 HOH 22  260 260 HOH HOH B . 
F 2 HOH 23  261 261 HOH HOH B . 
F 2 HOH 24  262 262 HOH HOH B . 
F 2 HOH 25  263 263 HOH HOH B . 
F 2 HOH 26  264 264 HOH HOH B . 
F 2 HOH 27  265 265 HOH HOH B . 
F 2 HOH 28  266 266 HOH HOH B . 
F 2 HOH 29  267 267 HOH HOH B . 
F 2 HOH 30  268 268 HOH HOH B . 
F 2 HOH 31  269 269 HOH HOH B . 
F 2 HOH 32  270 270 HOH HOH B . 
F 2 HOH 33  271 271 HOH HOH B . 
F 2 HOH 34  272 272 HOH HOH B . 
F 2 HOH 35  273 273 HOH HOH B . 
F 2 HOH 36  274 274 HOH HOH B . 
F 2 HOH 37  275 275 HOH HOH B . 
F 2 HOH 38  276 276 HOH HOH B . 
F 2 HOH 39  277 277 HOH HOH B . 
F 2 HOH 40  278 278 HOH HOH B . 
F 2 HOH 41  279 279 HOH HOH B . 
F 2 HOH 42  280 280 HOH HOH B . 
F 2 HOH 43  281 281 HOH HOH B . 
F 2 HOH 44  282 282 HOH HOH B . 
F 2 HOH 45  283 283 HOH HOH B . 
F 2 HOH 46  284 284 HOH HOH B . 
F 2 HOH 47  285 285 HOH HOH B . 
F 2 HOH 48  286 286 HOH HOH B . 
F 2 HOH 49  287 287 HOH HOH B . 
F 2 HOH 50  288 288 HOH HOH B . 
F 2 HOH 51  289 289 HOH HOH B . 
F 2 HOH 52  290 290 HOH HOH B . 
F 2 HOH 53  291 291 HOH HOH B . 
F 2 HOH 54  292 292 HOH HOH B . 
F 2 HOH 55  293 293 HOH HOH B . 
F 2 HOH 56  294 294 HOH HOH B . 
F 2 HOH 57  295 295 HOH HOH B . 
F 2 HOH 58  296 296 HOH HOH B . 
F 2 HOH 59  297 297 HOH HOH B . 
F 2 HOH 60  298 298 HOH HOH B . 
F 2 HOH 61  299 299 HOH HOH B . 
F 2 HOH 62  300 300 HOH HOH B . 
F 2 HOH 63  301 301 HOH HOH B . 
F 2 HOH 64  302 302 HOH HOH B . 
F 2 HOH 65  303 303 HOH HOH B . 
F 2 HOH 66  304 304 HOH HOH B . 
F 2 HOH 67  305 305 HOH HOH B . 
F 2 HOH 68  306 306 HOH HOH B . 
F 2 HOH 69  307 307 HOH HOH B . 
F 2 HOH 70  308 308 HOH HOH B . 
F 2 HOH 71  309 309 HOH HOH B . 
F 2 HOH 72  310 310 HOH HOH B . 
F 2 HOH 73  311 311 HOH HOH B . 
F 2 HOH 74  312 312 HOH HOH B . 
F 2 HOH 75  313 313 HOH HOH B . 
F 2 HOH 76  314 314 HOH HOH B . 
F 2 HOH 77  315 315 HOH HOH B . 
F 2 HOH 78  316 316 HOH HOH B . 
F 2 HOH 79  317 317 HOH HOH B . 
F 2 HOH 80  318 318 HOH HOH B . 
F 2 HOH 81  319 319 HOH HOH B . 
F 2 HOH 82  320 320 HOH HOH B . 
F 2 HOH 83  321 321 HOH HOH B . 
F 2 HOH 84  322 322 HOH HOH B . 
F 2 HOH 85  323 323 HOH HOH B . 
F 2 HOH 86  324 324 HOH HOH B . 
F 2 HOH 87  325 325 HOH HOH B . 
F 2 HOH 88  326 326 HOH HOH B . 
F 2 HOH 89  327 327 HOH HOH B . 
F 2 HOH 90  328 328 HOH HOH B . 
F 2 HOH 91  329 329 HOH HOH B . 
F 2 HOH 92  330 330 HOH HOH B . 
F 2 HOH 93  331 331 HOH HOH B . 
F 2 HOH 94  332 332 HOH HOH B . 
F 2 HOH 95  334 334 HOH HOH B . 
F 2 HOH 96  335 335 HOH HOH B . 
F 2 HOH 97  336 336 HOH HOH B . 
F 2 HOH 98  337 337 HOH HOH B . 
F 2 HOH 99  338 338 HOH HOH B . 
F 2 HOH 100 339 339 HOH HOH B . 
F 2 HOH 101 340 340 HOH HOH B . 
F 2 HOH 102 341 341 HOH HOH B . 
F 2 HOH 103 342 342 HOH HOH B . 
F 2 HOH 104 343 343 HOH HOH B . 
F 2 HOH 105 344 344 HOH HOH B . 
G 2 HOH 1   233 233 HOH HOH C . 
G 2 HOH 2   235 235 HOH HOH C . 
G 2 HOH 3   236 236 HOH HOH C . 
G 2 HOH 4   237 237 HOH HOH C . 
G 2 HOH 5   238 238 HOH HOH C . 
G 2 HOH 6   239 239 HOH HOH C . 
G 2 HOH 7   240 240 HOH HOH C . 
G 2 HOH 8   241 241 HOH HOH C . 
G 2 HOH 9   242 242 HOH HOH C . 
G 2 HOH 10  243 243 HOH HOH C . 
G 2 HOH 11  244 244 HOH HOH C . 
G 2 HOH 12  245 245 HOH HOH C . 
G 2 HOH 13  246 246 HOH HOH C . 
G 2 HOH 14  247 247 HOH HOH C . 
G 2 HOH 15  248 248 HOH HOH C . 
G 2 HOH 16  249 249 HOH HOH C . 
G 2 HOH 17  250 250 HOH HOH C . 
G 2 HOH 18  251 251 HOH HOH C . 
G 2 HOH 19  252 252 HOH HOH C . 
G 2 HOH 20  253 253 HOH HOH C . 
G 2 HOH 21  254 254 HOH HOH C . 
G 2 HOH 22  255 255 HOH HOH C . 
G 2 HOH 23  256 256 HOH HOH C . 
G 2 HOH 24  257 257 HOH HOH C . 
G 2 HOH 25  258 258 HOH HOH C . 
G 2 HOH 26  259 259 HOH HOH C . 
G 2 HOH 27  260 260 HOH HOH C . 
G 2 HOH 28  261 261 HOH HOH C . 
G 2 HOH 29  262 262 HOH HOH C . 
G 2 HOH 30  263 263 HOH HOH C . 
G 2 HOH 31  264 264 HOH HOH C . 
G 2 HOH 32  265 265 HOH HOH C . 
G 2 HOH 33  266 266 HOH HOH C . 
G 2 HOH 34  267 267 HOH HOH C . 
G 2 HOH 35  268 268 HOH HOH C . 
G 2 HOH 36  269 269 HOH HOH C . 
G 2 HOH 37  270 270 HOH HOH C . 
G 2 HOH 38  271 271 HOH HOH C . 
G 2 HOH 39  272 272 HOH HOH C . 
G 2 HOH 40  273 273 HOH HOH C . 
G 2 HOH 41  274 274 HOH HOH C . 
G 2 HOH 42  275 275 HOH HOH C . 
G 2 HOH 43  276 276 HOH HOH C . 
G 2 HOH 44  277 277 HOH HOH C . 
G 2 HOH 45  278 278 HOH HOH C . 
G 2 HOH 46  279 279 HOH HOH C . 
G 2 HOH 47  280 280 HOH HOH C . 
G 2 HOH 48  281 281 HOH HOH C . 
G 2 HOH 49  282 282 HOH HOH C . 
G 2 HOH 50  283 283 HOH HOH C . 
G 2 HOH 51  284 284 HOH HOH C . 
G 2 HOH 52  285 285 HOH HOH C . 
G 2 HOH 53  286 286 HOH HOH C . 
G 2 HOH 54  287 287 HOH HOH C . 
G 2 HOH 55  288 288 HOH HOH C . 
G 2 HOH 56  289 289 HOH HOH C . 
G 2 HOH 57  290 290 HOH HOH C . 
G 2 HOH 58  291 291 HOH HOH C . 
G 2 HOH 59  292 292 HOH HOH C . 
G 2 HOH 60  293 293 HOH HOH C . 
G 2 HOH 61  294 294 HOH HOH C . 
G 2 HOH 62  295 295 HOH HOH C . 
H 2 HOH 1   154 154 HOH HOH D . 
H 2 HOH 2   155 155 HOH HOH D . 
H 2 HOH 3   156 156 HOH HOH D . 
H 2 HOH 4   157 157 HOH HOH D . 
H 2 HOH 5   158 158 HOH HOH D . 
H 2 HOH 6   159 159 HOH HOH D . 
H 2 HOH 7   160 160 HOH HOH D . 
H 2 HOH 8   161 161 HOH HOH D . 
H 2 HOH 9   162 162 HOH HOH D . 
H 2 HOH 10  163 163 HOH HOH D . 
H 2 HOH 11  164 164 HOH HOH D . 
H 2 HOH 12  165 165 HOH HOH D . 
H 2 HOH 13  166 166 HOH HOH D . 
H 2 HOH 14  167 167 HOH HOH D . 
H 2 HOH 15  168 168 HOH HOH D . 
H 2 HOH 16  169 169 HOH HOH D . 
H 2 HOH 17  170 170 HOH HOH D . 
H 2 HOH 18  171 171 HOH HOH D . 
H 2 HOH 19  172 172 HOH HOH D . 
H 2 HOH 20  173 173 HOH HOH D . 
H 2 HOH 21  174 174 HOH HOH D . 
H 2 HOH 22  175 175 HOH HOH D . 
H 2 HOH 23  176 176 HOH HOH D . 
H 2 HOH 24  177 177 HOH HOH D . 
H 2 HOH 25  178 178 HOH HOH D . 
H 2 HOH 26  179 179 HOH HOH D . 
H 2 HOH 27  180 180 HOH HOH D . 
H 2 HOH 28  181 181 HOH HOH D . 
H 2 HOH 29  182 182 HOH HOH D . 
H 2 HOH 30  183 183 HOH HOH D . 
H 2 HOH 31  184 184 HOH HOH D . 
H 2 HOH 32  185 185 HOH HOH D . 
H 2 HOH 33  186 186 HOH HOH D . 
H 2 HOH 34  187 187 HOH HOH D . 
H 2 HOH 35  188 188 HOH HOH D . 
H 2 HOH 36  189 189 HOH HOH D . 
H 2 HOH 37  190 190 HOH HOH D . 
H 2 HOH 38  191 191 HOH HOH D . 
H 2 HOH 39  192 192 HOH HOH D . 
H 2 HOH 40  193 193 HOH HOH D . 
H 2 HOH 41  194 194 HOH HOH D . 
H 2 HOH 42  195 195 HOH HOH D . 
H 2 HOH 43  196 196 HOH HOH D . 
H 2 HOH 44  197 197 HOH HOH D . 
H 2 HOH 45  198 198 HOH HOH D . 
H 2 HOH 46  199 199 HOH HOH D . 
H 2 HOH 47  200 200 HOH HOH D . 
H 2 HOH 48  201 201 HOH HOH D . 
# 
