data_2GBU
# 
_entry.id   2GBU 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.351 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   2GBU         pdb_00002gbu 10.2210/pdb2gbu/pdb 
RCSB  RCSB036931   ?            ?                   
WWPDB D_1000036931 ?            ?                   
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 1HL4 'apo CuZn Superoxide dismutase'                       unspecified 
PDB 2GBT 'C6A/C111A apo CuZn Superoxide dismutase'             unspecified 
PDB 2GBV 'C6A/C111A/C57A/C146A holo CuZn Superoxide dismutase' unspecified 
# 
_pdbx_database_status.entry_id                        2GBU 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.recvd_initial_deposition_date   2006-03-11 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Hornberg, A.'   1 
'Logan, D.T.'    2 
'Marklund, S.L.' 3 
'Oliveberg, M.'  4 
# 
_citation.id                        primary 
_citation.title                     
'The Coupling between Disulphide Status, Metallation and Dimer Interface Strength in Cu/Zn Superoxide Dismutase' 
_citation.journal_abbrev            J.Mol.Biol. 
_citation.journal_volume            365 
_citation.page_first                333 
_citation.page_last                 342 
_citation.year                      2007 
_citation.journal_id_ASTM           JMOBAK 
_citation.country                   UK 
_citation.journal_id_ISSN           0022-2836 
_citation.journal_id_CSD            0070 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   17070542 
_citation.pdbx_database_id_DOI      10.1016/j.jmb.2006.09.048 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Hornberg, A.'   1 ? 
primary 'Logan, D.T.'    2 ? 
primary 'Marklund, S.L.' 3 ? 
primary 'Oliveberg, M.'  4 ? 
# 
_cell.length_a           156.614 
_cell.length_b           34.427 
_cell.length_c           114.461 
_cell.angle_alpha        90.00 
_cell.angle_beta         112.17 
_cell.angle_gamma        90.00 
_cell.entry_id           2GBU 
_cell.pdbx_unique_axis   ? 
_cell.Z_PDB              16 
_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.space_group_name_H-M             'C 1 2 1' 
_symmetry.entry_id                         2GBU 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.Int_Tables_number                5 
_symmetry.cell_setting                     ? 
_symmetry.space_group_name_Hall            ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer man 'Superoxide dismutase [Cu-Zn]' 15699.299 4   1.15.1.1 C6A/C111A/C57A/C146A ? ? 
2 water   nat water                          18.015    259 ?        ?                    ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Cu/Zn superoxide dismutase' 
# 
_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       
;ATKAVAVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGATSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHAIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLAAGVIGIAQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;ATKAVAVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGATSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHAIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLAAGVIGIAQ
;
_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   ALA 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  ALA 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 ALA 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 ALA 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                     Homo 
_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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     Escherichia 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   'Escherichia coli' 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               BL21/DE3 
_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                       pACA 
_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           1 
_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 2GBU A 1 ? 153 ? P00441 1 ? 153 ? 1 153 
2 1 2GBU B 1 ? 153 ? P00441 1 ? 153 ? 1 153 
3 1 2GBU C 1 ? 153 ? P00441 1 ? 153 ? 1 153 
4 1 2GBU D 1 ? 153 ? P00441 1 ? 153 ? 1 153 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 2GBU ALA A 6   ? UNP P00441 CYS 6   'engineered mutation' 6   1  
1 2GBU ALA A 57  ? UNP P00441 CYS 57  'engineered mutation' 57  2  
1 2GBU ALA A 111 ? UNP P00441 CYS 111 'engineered mutation' 111 3  
1 2GBU ALA A 146 ? UNP P00441 CYS 146 'engineered mutation' 146 4  
2 2GBU ALA B 6   ? UNP P00441 CYS 6   'engineered mutation' 6   5  
2 2GBU ALA B 57  ? UNP P00441 CYS 57  'engineered mutation' 57  6  
2 2GBU ALA B 111 ? UNP P00441 CYS 111 'engineered mutation' 111 7  
2 2GBU ALA B 146 ? UNP P00441 CYS 146 'engineered mutation' 146 8  
3 2GBU ALA C 6   ? UNP P00441 CYS 6   'engineered mutation' 6   9  
3 2GBU ALA C 57  ? UNP P00441 CYS 57  'engineered mutation' 57  10 
3 2GBU ALA C 111 ? UNP P00441 CYS 111 'engineered mutation' 111 11 
3 2GBU ALA C 146 ? UNP P00441 CYS 146 'engineered mutation' 146 12 
4 2GBU ALA D 6   ? UNP P00441 CYS 6   'engineered mutation' 6   13 
4 2GBU ALA D 57  ? UNP P00441 CYS 57  'engineered mutation' 57  14 
4 2GBU ALA D 111 ? UNP P00441 CYS 111 'engineered mutation' 111 15 
4 2GBU ALA D 146 ? UNP P00441 CYS 146 'engineered mutation' 146 16 
# 
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          2GBU 
_exptl.crystals_number   1 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.27 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_percent_sol   45.92 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              6.5 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_details    
'25% PEG4000, 0.1M Na Cacodylate, 50mM NaAc, 1mM EDTA, 1mM NaN3, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K' 
_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                   MARRESEARCH 
_diffrn_detector.pdbx_collection_date   2004-06-20 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.monochromator                    'SI 111 CHANNEL' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.092 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'MAX II BEAMLINE I711' 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        1.092 
_diffrn_source.pdbx_synchrotron_site       'MAX II' 
_diffrn_source.pdbx_synchrotron_beamline   I711 
# 
_reflns.entry_id                     2GBU 
_reflns.observed_criterion_sigma_F   1 
_reflns.observed_criterion_sigma_I   1 
_reflns.d_resolution_high            2.0 
_reflns.d_resolution_low             20.0 
_reflns.number_all                   38835 
_reflns.number_obs                   38835 
_reflns.percent_possible_obs         99.6 
_reflns.pdbx_Rmerge_I_obs            0.072 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        ? 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              ? 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_high             2.00 
_reflns_shell.d_res_low              2.11 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.percent_possible_all   99.0 
_reflns_shell.Rmerge_I_obs           0.212 
_reflns_shell.meanI_over_sigI_obs    4.4 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.pdbx_redundancy        ? 
_reflns_shell.number_unique_all      ? 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.pdbx_diffrn_id         1 
# 
_refine.ls_d_res_high                            2.000 
_refine.ls_d_res_low                             20.000 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.ls_percent_reflns_obs                    99.610 
_refine.ls_number_reflns_obs                     38832 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.ls_R_factor_all                          0.219 
_refine.ls_R_factor_R_work                       0.217 
_refine.ls_R_factor_R_free                       0.257 
_refine.ls_percent_reflns_R_free                 5.000 
_refine.ls_number_reflns_R_free                  1953 
_refine.B_iso_mean                               36.981 
_refine.aniso_B[1][1]                            -3.870 
_refine.aniso_B[2][2]                            6.280 
_refine.aniso_B[3][3]                            -3.760 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            -1.790 
_refine.aniso_B[2][3]                            0.000 
_refine.correlation_coeff_Fo_to_Fc               0.951 
_refine.correlation_coeff_Fo_to_Fc_free          0.928 
_refine.pdbx_overall_ESU_R                       0.205 
_refine.pdbx_overall_ESU_R_Free                  0.178 
_refine.overall_SU_ML                            0.179 
_refine.overall_SU_B                             13.747 
_refine.solvent_model_details                    'BABINET MODEL WITH MASK' 
_refine.pdbx_solvent_vdw_probe_radii             1.200 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.entry_id                                 2GBU 
_refine.pdbx_ls_sigma_I                          ? 
_refine.ls_number_reflns_all                     38835 
_refine.ls_R_factor_obs                          0.219 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.pdbx_starting_model                      1HL4 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_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_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_TLS_residual_ADP_flag               'LIKELY RESIDUAL' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_overall_phase_error                 ? 
_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        4002 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.number_atoms_solvent             259 
_refine_hist.number_atoms_total               4261 
_refine_hist.d_res_high                       2.000 
_refine_hist.d_res_low                        20.000 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d         4066 0.007  0.021  ? 'X-RAY DIFFRACTION' ? 
r_bond_other_d           3645 0.001  0.020  ? 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg      5496 1.061  1.939  ? 'X-RAY DIFFRACTION' ? 
r_angle_other_deg        8510 0.660  3.000  ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg   545  6.050  5.000  ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg   171  38.654 25.556 ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg   643  11.962 15.000 ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg   13   11.012 15.000 ? 'X-RAY DIFFRACTION' ? 
r_chiral_restr           620  0.062  0.200  ? 'X-RAY DIFFRACTION' ? 
r_gen_planes_refined     4678 0.003  0.020  ? 'X-RAY DIFFRACTION' ? 
r_gen_planes_other       739  0.001  0.020  ? 'X-RAY DIFFRACTION' ? 
r_nbd_refined            621  0.173  0.200  ? 'X-RAY DIFFRACTION' ? 
r_nbd_other              3563 0.173  0.200  ? 'X-RAY DIFFRACTION' ? 
r_nbtor_refined          1946 0.159  0.200  ? 'X-RAY DIFFRACTION' ? 
r_nbtor_other            2408 0.079  0.200  ? 'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined    235  0.125  0.200  ? 'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined   11   0.063  0.200  ? 'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other     34   0.193  0.200  ? 'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined 5    0.113  0.200  ? 'X-RAY DIFFRACTION' ? 
r_mcbond_it              3549 0.499  1.500  ? 'X-RAY DIFFRACTION' ? 
r_mcbond_other           1182 0.068  1.500  ? 'X-RAY DIFFRACTION' ? 
r_mcangle_it             4271 0.585  2.000  ? 'X-RAY DIFFRACTION' ? 
r_scbond_it              1668 0.961  3.000  ? 'X-RAY DIFFRACTION' ? 
r_scangle_it             1225 1.345  4.500  ? 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.d_res_high                       2.000 
_refine_ls_shell.d_res_low                        2.051 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               97.990 
_refine_ls_shell.number_reflns_R_work             2649 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.284 
_refine_ls_shell.R_factor_R_free                  0.294 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             133 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                2782 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  2GBU 
_struct.title                     'C6A/C111A/C57A/C146A apo CuZn Superoxide dismutase' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        2GBU 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
_struct_keywords.text            'OXIDOREDUCTASE, HUMAN CU/ZN SUPEROXIDE DISMUTASE, CYSTEIN-FREE' 
# 
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 ? 
# 
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 GLU A 133 ? GLY A 138 ? GLU A 133 GLY A 138 1 ? 6 
HELX_P HELX_P2 2 GLU B 133 ? GLY B 138 ? GLU B 133 GLY B 138 1 ? 6 
HELX_P HELX_P3 3 ALA C 55  ? GLY C 61  ? ALA C 55  GLY C 61  5 ? 7 
HELX_P HELX_P4 4 ALA D 55  ? GLY D 61  ? ALA D 55  GLY D 61  5 ? 7 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_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  ? GLN B 22  ? GLN B 15  GLN B 22  
C 4 THR B 2   ? LEU B 8   ? THR B 2   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  ? GLN C 22  ? GLN C 15  GLN C 22  
E 4 THR C 2   ? LEU C 8   ? THR C 2   LEU C 8   
E 5 GLY C 150 ? ILE C 151 ? GLY C 150 ILE C 151 
F 1 ASP C 83  ? ALA C 89  ? ASP C 83  ALA C 89  
F 2 GLY C 41  ? HIS C 48  ? GLY C 41  HIS C 48  
F 3 THR C 116 ? HIS C 120 ? THR C 116 HIS C 120 
F 4 ARG C 143 ? VAL C 148 ? ARG C 143 VAL C 148 
G 1 ALA D 95  ? ASP D 101 ? ALA D 95  ASP D 101 
G 2 VAL D 29  ? 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 TRP A 32  ? O TRP A 32  N ASN A 19  ? N ASN A 19  
A 3 4 O PHE A 20  ? O PHE A 20  N ALA A 4   ? N ALA A 4   
A 4 5 N VAL A 5   ? N VAL A 5   O GLY A 150 ? O GLY A 150 
B 1 2 O ALA A 89  ? O ALA A 89  N GLY A 41  ? N GLY A 41  
B 2 3 N HIS A 48  ? N HIS A 48  O THR A 116 ? O THR A 116 
B 3 4 N LEU A 117 ? N LEU A 117 O GLY A 147 ? O GLY A 147 
C 1 2 O ALA B 95  ? O ALA B 95  N ILE B 35  ? N ILE B 35  
C 2 3 O TRP B 32  ? O TRP B 32  N ASN B 19  ? N ASN B 19  
C 3 4 O PHE B 20  ? O PHE B 20  N ALA B 4   ? N ALA B 4   
C 4 5 N VAL B 5   ? N VAL B 5   O GLY B 150 ? O GLY B 150 
D 1 2 O GLY B 85  ? O GLY B 85  N PHE B 45  ? N PHE B 45  
D 2 3 N HIS B 48  ? N HIS B 48  O THR B 116 ? O THR B 116 
D 3 4 N VAL B 119 ? N VAL B 119 O LEU B 144 ? O LEU B 144 
E 1 2 O ILE C 99  ? O ILE C 99  N VAL C 31  ? N VAL C 31  
E 2 3 O TRP C 32  ? O TRP C 32  N ASN C 19  ? N ASN C 19  
E 3 4 O GLN C 22  ? O GLN C 22  N THR C 2   ? N THR C 2   
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 48  ? N HIS C 48  O THR C 116 ? O THR C 116 
F 3 4 N LEU C 117 ? N LEU C 117 O GLY C 147 ? O GLY C 147 
G 1 2 O ILE D 99  ? O ILE D 99  N VAL D 31  ? N VAL D 31  
G 2 3 O TRP D 32  ? O TRP D 32  N ASN D 19  ? N ASN D 19  
G 3 4 O ILE D 18  ? O ILE D 18  N ALA D 6   ? N ALA D 6   
G 4 5 N VAL D 5   ? N VAL D 5   O GLY D 150 ? O GLY D 150 
H 1 2 O ALA D 89  ? O ALA D 89  N GLY D 41  ? N GLY D 41  
H 2 3 N HIS D 48  ? N HIS D 48  O THR D 116 ? O THR D 116 
H 3 4 N LEU D 117 ? N LEU D 117 O GLY D 147 ? O GLY D 147 
# 
_database_PDB_matrix.entry_id          2GBU 
_database_PDB_matrix.origx[1][1]       1.00000 
_database_PDB_matrix.origx[1][2]       0.00000 
_database_PDB_matrix.origx[1][3]       0.00000 
_database_PDB_matrix.origx[2][1]       0.00000 
_database_PDB_matrix.origx[2][2]       1.00000 
_database_PDB_matrix.origx[2][3]       0.00000 
_database_PDB_matrix.origx[3][1]       0.00000 
_database_PDB_matrix.origx[3][2]       0.00000 
_database_PDB_matrix.origx[3][3]       1.00000 
_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                    2GBU 
_atom_sites.fract_transf_matrix[1][1]   0.00638 
_atom_sites.fract_transf_matrix[1][2]   0.00000 
_atom_sites.fract_transf_matrix[1][3]   0.00260 
_atom_sites.fract_transf_matrix[2][1]   0.00000 
_atom_sites.fract_transf_matrix[2][2]   0.02905 
_atom_sites.fract_transf_matrix[2][3]   0.00000 
_atom_sites.fract_transf_matrix[3][1]   0.00000 
_atom_sites.fract_transf_matrix[3][2]   0.00000 
_atom_sites.fract_transf_matrix[3][3]   0.00943 
_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 
# 
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   ? 2.960   -14.143 27.752  1.00 45.64 ? 1   ALA A N   1 
ATOM   2    C CA  . ALA A 1 1   ? 3.535   -13.240 28.798  1.00 45.54 ? 1   ALA A CA  1 
ATOM   3    C C   . ALA A 1 1   ? 2.554   -12.122 29.184  1.00 45.44 ? 1   ALA A C   1 
ATOM   4    O O   . ALA A 1 1   ? 2.003   -12.132 30.291  1.00 46.08 ? 1   ALA A O   1 
ATOM   5    C CB  . ALA A 1 1   ? 4.880   -12.657 28.336  1.00 45.77 ? 1   ALA A CB  1 
ATOM   6    N N   . THR A 1 2   ? 2.309   -11.174 28.288  1.00 44.79 ? 2   THR A N   1 
ATOM   7    C CA  . THR A 1 2   ? 1.384   -10.100 28.627  1.00 44.38 ? 2   THR A CA  1 
ATOM   8    C C   . THR A 1 2   ? -0.060  -10.609 28.515  1.00 43.71 ? 2   THR A C   1 
ATOM   9    O O   . THR A 1 2   ? -0.454  -11.206 27.509  1.00 43.01 ? 2   THR A O   1 
ATOM   10   C CB  . THR A 1 2   ? 1.600   -8.826  27.772  1.00 44.54 ? 2   THR A CB  1 
ATOM   11   O OG1 . THR A 1 2   ? 2.977   -8.724  27.382  1.00 45.83 ? 2   THR A OG1 1 
ATOM   12   C CG2 . THR A 1 2   ? 1.218   -7.578  28.568  1.00 45.01 ? 2   THR A CG2 1 
ATOM   13   N N   . LYS A 1 3   ? -0.820  -10.383 29.585  1.00 43.26 ? 3   LYS A N   1 
ATOM   14   C CA  . LYS A 1 3   ? -2.233  -10.744 29.671  1.00 42.67 ? 3   LYS A CA  1 
ATOM   15   C C   . LYS A 1 3   ? -3.036  -9.553  30.205  1.00 41.85 ? 3   LYS A C   1 
ATOM   16   O O   . LYS A 1 3   ? -2.560  -8.807  31.070  1.00 40.88 ? 3   LYS A O   1 
ATOM   17   C CB  . LYS A 1 3   ? -2.399  -11.950 30.590  1.00 42.90 ? 3   LYS A CB  1 
ATOM   18   C CG  . LYS A 1 3   ? -3.741  -12.636 30.481  1.00 43.38 ? 3   LYS A CG  1 
ATOM   19   C CD  . LYS A 1 3   ? -3.693  -14.062 31.026  1.00 43.44 ? 3   LYS A CD  1 
ATOM   20   C CE  . LYS A 1 3   ? -4.998  -14.812 30.744  1.00 43.98 ? 3   LYS A CE  1 
ATOM   21   N NZ  . LYS A 1 3   ? -4.821  -16.309 30.644  1.00 44.77 ? 3   LYS A NZ  1 
ATOM   22   N N   . ALA A 1 4   ? -4.247  -9.380  29.683  1.00 41.15 ? 4   ALA A N   1 
ATOM   23   C CA  . ALA A 1 4   ? -5.104  -8.267  30.075  1.00 40.81 ? 4   ALA A CA  1 
ATOM   24   C C   . ALA A 1 4   ? -6.589  -8.638  30.041  1.00 40.53 ? 4   ALA A C   1 
ATOM   25   O O   . ALA A 1 4   ? -6.983  -9.658  29.468  1.00 39.68 ? 4   ALA A O   1 
ATOM   26   C CB  . ALA A 1 4   ? -4.840  -7.077  29.192  1.00 40.58 ? 4   ALA A CB  1 
ATOM   27   N N   . VAL A 1 5   ? -7.403  -7.802  30.674  1.00 39.96 ? 5   VAL A N   1 
ATOM   28   C CA  . VAL A 1 5   ? -8.825  -8.041  30.761  1.00 40.15 ? 5   VAL A CA  1 
ATOM   29   C C   . VAL A 1 5   ? -9.582  -6.716  30.863  1.00 40.25 ? 5   VAL A C   1 
ATOM   30   O O   . VAL A 1 5   ? -9.094  -5.745  31.443  1.00 39.78 ? 5   VAL A O   1 
ATOM   31   C CB  . VAL A 1 5   ? -9.164  -8.993  31.954  1.00 40.46 ? 5   VAL A CB  1 
ATOM   32   C CG1 . VAL A 1 5   ? -8.766  -8.372  33.282  1.00 41.13 ? 5   VAL A CG1 1 
ATOM   33   C CG2 . VAL A 1 5   ? -10.645 -9.381  31.956  1.00 40.48 ? 5   VAL A CG2 1 
ATOM   34   N N   . ALA A 1 6   ? -10.757 -6.680  30.243  1.00 40.02 ? 6   ALA A N   1 
ATOM   35   C CA  . ALA A 1 6   ? -11.676 -5.578  30.392  1.00 40.12 ? 6   ALA A CA  1 
ATOM   36   C C   . ALA A 1 6   ? -13.008 -6.148  30.856  1.00 40.07 ? 6   ALA A C   1 
ATOM   37   O O   . ALA A 1 6   ? -13.533 -7.088  30.257  1.00 39.91 ? 6   ALA A O   1 
ATOM   38   C CB  . ALA A 1 6   ? -11.833 -4.828  29.081  1.00 40.06 ? 6   ALA A CB  1 
ATOM   39   N N   . VAL A 1 7   ? -13.521 -5.597  31.951  1.00 40.25 ? 7   VAL A N   1 
ATOM   40   C CA  . VAL A 1 7   ? -14.881 -5.875  32.408  1.00 40.31 ? 7   VAL A CA  1 
ATOM   41   C C   . VAL A 1 7   ? -15.794 -4.813  31.794  1.00 40.17 ? 7   VAL A C   1 
ATOM   42   O O   . VAL A 1 7   ? -15.657 -3.618  32.085  1.00 39.45 ? 7   VAL A O   1 
ATOM   43   C CB  . VAL A 1 7   ? -14.982 -5.847  33.948  1.00 40.32 ? 7   VAL A CB  1 
ATOM   44   C CG1 . VAL A 1 7   ? -16.393 -6.181  34.414  1.00 40.16 ? 7   VAL A CG1 1 
ATOM   45   C CG2 . VAL A 1 7   ? -13.993 -6.815  34.556  1.00 40.65 ? 7   VAL A CG2 1 
ATOM   46   N N   . LEU A 1 8   ? -16.698 -5.249  30.924  1.00 40.13 ? 8   LEU A N   1 
ATOM   47   C CA  . LEU A 1 8   ? -17.614 -4.330  30.251  1.00 40.72 ? 8   LEU A CA  1 
ATOM   48   C C   . LEU A 1 8   ? -18.857 -4.052  31.103  1.00 40.72 ? 8   LEU A C   1 
ATOM   49   O O   . LEU A 1 8   ? -19.592 -4.969  31.450  1.00 40.12 ? 8   LEU A O   1 
ATOM   50   C CB  . LEU A 1 8   ? -18.009 -4.867  28.867  1.00 40.74 ? 8   LEU A CB  1 
ATOM   51   C CG  . LEU A 1 8   ? -16.893 -4.914  27.829  1.00 40.91 ? 8   LEU A CG  1 
ATOM   52   C CD1 . LEU A 1 8   ? -17.383 -5.600  26.574  1.00 42.41 ? 8   LEU A CD1 1 
ATOM   53   C CD2 . LEU A 1 8   ? -16.405 -3.528  27.498  1.00 40.91 ? 8   LEU A CD2 1 
ATOM   54   N N   . LYS A 1 9   ? -19.064 -2.776  31.430  1.00 40.82 ? 9   LYS A N   1 
ATOM   55   C CA  . LYS A 1 9   ? -20.151 -2.338  32.302  1.00 41.47 ? 9   LYS A CA  1 
ATOM   56   C C   . LYS A 1 9   ? -20.770 -1.064  31.750  1.00 41.38 ? 9   LYS A C   1 
ATOM   57   O O   . LYS A 1 9   ? -20.098 -0.285  31.071  1.00 40.77 ? 9   LYS A O   1 
ATOM   58   C CB  . LYS A 1 9   ? -19.627 -2.070  33.714  1.00 41.66 ? 9   LYS A CB  1 
ATOM   59   C CG  . LYS A 1 9   ? -19.371 -3.326  34.530  1.00 43.10 ? 9   LYS A CG  1 
ATOM   60   C CD  . LYS A 1 9   ? -18.701 -3.014  35.875  1.00 43.13 ? 9   LYS A CD  1 
ATOM   61   C CE  . LYS A 1 9   ? -18.713 -4.226  36.823  1.00 43.72 ? 9   LYS A CE  1 
ATOM   62   N NZ  . LYS A 1 9   ? -18.056 -3.897  38.133  1.00 44.38 ? 9   LYS A NZ  1 
ATOM   63   N N   . GLY A 1 10  ? -22.048 -0.852  32.046  1.00 41.70 ? 10  GLY A N   1 
ATOM   64   C CA  . GLY A 1 10  ? -22.756 0.343   31.592  1.00 42.15 ? 10  GLY A CA  1 
ATOM   65   C C   . GLY A 1 10  ? -24.024 0.605   32.373  1.00 42.44 ? 10  GLY A C   1 
ATOM   66   O O   . GLY A 1 10  ? -24.316 -0.101  33.335  1.00 42.61 ? 10  GLY A O   1 
ATOM   67   N N   . ASP A 1 11  ? -24.783 1.615   31.949  1.00 42.89 ? 11  ASP A N   1 
ATOM   68   C CA  . ASP A 1 11  ? -26.006 2.026   32.643  1.00 43.33 ? 11  ASP A CA  1 
ATOM   69   C C   . ASP A 1 11  ? -27.180 1.203   32.145  1.00 43.40 ? 11  ASP A C   1 
ATOM   70   O O   . ASP A 1 11  ? -28.288 1.726   32.006  1.00 43.91 ? 11  ASP A O   1 
ATOM   71   C CB  . ASP A 1 11  ? -26.296 3.521   32.406  1.00 43.66 ? 11  ASP A CB  1 
ATOM   72   C CG  . ASP A 1 11  ? -25.144 4.428   32.846  1.00 44.94 ? 11  ASP A CG  1 
ATOM   73   O OD1 . ASP A 1 11  ? -24.707 4.320   34.016  1.00 46.76 ? 11  ASP A OD1 1 
ATOM   74   O OD2 . ASP A 1 11  ? -24.674 5.250   32.020  1.00 44.78 ? 11  ASP A OD2 1 
ATOM   75   N N   . GLY A 1 12  ? -26.950 -0.088  31.901  1.00 43.16 ? 12  GLY A N   1 
ATOM   76   C CA  . GLY A 1 12  ? -27.887 -0.891  31.125  1.00 42.66 ? 12  GLY A CA  1 
ATOM   77   C C   . GLY A 1 12  ? -27.691 -2.384  31.276  1.00 42.31 ? 12  GLY A C   1 
ATOM   78   O O   . GLY A 1 12  ? -26.916 -2.827  32.123  1.00 42.16 ? 12  GLY A O   1 
ATOM   79   N N   . PRO A 1 13  ? -28.407 -3.171  30.459  1.00 41.86 ? 13  PRO A N   1 
ATOM   80   C CA  . PRO A 1 13  ? -28.339 -4.634  30.513  1.00 41.78 ? 13  PRO A CA  1 
ATOM   81   C C   . PRO A 1 13  ? -27.051 -5.240  29.928  1.00 41.46 ? 13  PRO A C   1 
ATOM   82   O O   . PRO A 1 13  ? -26.733 -6.394  30.198  1.00 41.51 ? 13  PRO A O   1 
ATOM   83   C CB  . PRO A 1 13  ? -29.567 -5.064  29.702  1.00 41.68 ? 13  PRO A CB  1 
ATOM   84   C CG  . PRO A 1 13  ? -29.785 -3.955  28.743  1.00 41.76 ? 13  PRO A CG  1 
ATOM   85   C CD  . PRO A 1 13  ? -29.354 -2.699  29.432  1.00 41.85 ? 13  PRO A CD  1 
ATOM   86   N N   . VAL A 1 14  ? -26.308 -4.475  29.146  1.00 41.33 ? 14  VAL A N   1 
ATOM   87   C CA  . VAL A 1 14  ? -25.116 -5.011  28.509  1.00 41.10 ? 14  VAL A CA  1 
ATOM   88   C C   . VAL A 1 14  ? -23.989 -5.158  29.536  1.00 41.02 ? 14  VAL A C   1 
ATOM   89   O O   . VAL A 1 14  ? -23.615 -4.202  30.213  1.00 40.60 ? 14  VAL A O   1 
ATOM   90   C CB  . VAL A 1 14  ? -24.653 -4.128  27.346  1.00 41.09 ? 14  VAL A CB  1 
ATOM   91   C CG1 . VAL A 1 14  ? -23.379 -4.692  26.725  1.00 41.01 ? 14  VAL A CG1 1 
ATOM   92   C CG2 . VAL A 1 14  ? -25.760 -4.010  26.302  1.00 41.00 ? 14  VAL A CG2 1 
ATOM   93   N N   . GLN A 1 15  ? -23.465 -6.370  29.655  1.00 40.88 ? 15  GLN A N   1 
ATOM   94   C CA  . GLN A 1 15  ? -22.294 -6.611  30.468  1.00 41.01 ? 15  GLN A CA  1 
ATOM   95   C C   . GLN A 1 15  ? -21.498 -7.768  29.880  1.00 40.86 ? 15  GLN A C   1 
ATOM   96   O O   . GLN A 1 15  ? -22.046 -8.646  29.216  1.00 40.56 ? 15  GLN A O   1 
ATOM   97   C CB  . GLN A 1 15  ? -22.683 -6.891  31.922  1.00 41.08 ? 15  GLN A CB  1 
ATOM   98   C CG  . GLN A 1 15  ? -23.681 -8.015  32.110  1.00 41.73 ? 15  GLN A CG  1 
ATOM   99   C CD  . GLN A 1 15  ? -24.019 -8.272  33.572  1.00 41.77 ? 15  GLN A CD  1 
ATOM   100  O OE1 . GLN A 1 15  ? -25.159 -8.093  33.997  1.00 42.52 ? 15  GLN A OE1 1 
ATOM   101  N NE2 . GLN A 1 15  ? -23.026 -8.696  34.346  1.00 43.87 ? 15  GLN A NE2 1 
ATOM   102  N N   . GLY A 1 16  ? -20.193 -7.745  30.101  1.00 40.59 ? 16  GLY A N   1 
ATOM   103  C CA  . GLY A 1 16  ? -19.351 -8.839  29.661  1.00 40.45 ? 16  GLY A CA  1 
ATOM   104  C C   . GLY A 1 16  ? -17.938 -8.736  30.182  1.00 40.12 ? 16  GLY A C   1 
ATOM   105  O O   . GLY A 1 16  ? -17.589 -7.796  30.903  1.00 39.90 ? 16  GLY A O   1 
ATOM   106  N N   . ILE A 1 17  ? -17.139 -9.731  29.824  1.00 39.78 ? 17  ILE A N   1 
ATOM   107  C CA  . ILE A 1 17  ? -15.734 -9.772  30.180  1.00 39.89 ? 17  ILE A CA  1 
ATOM   108  C C   . ILE A 1 17  ? -14.955 -10.261 28.968  1.00 39.74 ? 17  ILE A C   1 
ATOM   109  O O   . ILE A 1 17  ? -15.280 -11.299 28.383  1.00 38.81 ? 17  ILE A O   1 
ATOM   110  C CB  . ILE A 1 17  ? -15.463 -10.689 31.381  1.00 39.92 ? 17  ILE A CB  1 
ATOM   111  C CG1 . ILE A 1 17  ? -16.338 -10.287 32.569  1.00 39.81 ? 17  ILE A CG1 1 
ATOM   112  C CG2 . ILE A 1 17  ? -13.977 -10.618 31.787  1.00 39.86 ? 17  ILE A CG2 1 
ATOM   113  C CD1 . ILE A 1 17  ? -16.485 -11.382 33.578  1.00 40.51 ? 17  ILE A CD1 1 
ATOM   114  N N   . ILE A 1 18  ? -13.942 -9.480  28.592  1.00 39.54 ? 18  ILE A N   1 
ATOM   115  C CA  . ILE A 1 18  ? -13.112 -9.783  27.442  1.00 39.59 ? 18  ILE A CA  1 
ATOM   116  C C   . ILE A 1 18  ? -11.663 -9.912  27.884  1.00 39.45 ? 18  ILE A C   1 
ATOM   117  O O   . ILE A 1 18  ? -11.127 -9.021  28.543  1.00 38.70 ? 18  ILE A O   1 
ATOM   118  C CB  . ILE A 1 18  ? -13.204 -8.699  26.362  1.00 39.82 ? 18  ILE A CB  1 
ATOM   119  C CG1 . ILE A 1 18  ? -14.673 -8.452  25.961  1.00 40.50 ? 18  ILE A CG1 1 
ATOM   120  C CG2 . ILE A 1 18  ? -12.343 -9.090  25.153  1.00 39.24 ? 18  ILE A CG2 1 
ATOM   121  C CD1 . ILE A 1 18  ? -15.316 -9.593  25.157  1.00 39.95 ? 18  ILE A CD1 1 
ATOM   122  N N   . ASN A 1 19  ? -11.057 -11.044 27.523  1.00 39.30 ? 19  ASN A N   1 
ATOM   123  C CA  . ASN A 1 19  ? -9.668  -11.330 27.829  1.00 39.40 ? 19  ASN A CA  1 
ATOM   124  C C   . ASN A 1 19  ? -8.775  -11.028 26.635  1.00 39.48 ? 19  ASN A C   1 
ATOM   125  O O   . ASN A 1 19  ? -9.172  -11.243 25.486  1.00 39.14 ? 19  ASN A O   1 
ATOM   126  C CB  . ASN A 1 19  ? -9.523  -12.786 28.222  1.00 39.46 ? 19  ASN A CB  1 
ATOM   127  C CG  . ASN A 1 19  ? -10.500 -13.187 29.296  1.00 39.84 ? 19  ASN A CG  1 
ATOM   128  O OD1 . ASN A 1 19  ? -10.261 -12.974 30.485  1.00 40.87 ? 19  ASN A OD1 1 
ATOM   129  N ND2 . ASN A 1 19  ? -11.623 -13.751 28.882  1.00 39.66 ? 19  ASN A ND2 1 
ATOM   130  N N   . PHE A 1 20  ? -7.584  -10.502 26.926  1.00 39.70 ? 20  PHE A N   1 
ATOM   131  C CA  . PHE A 1 20  ? -6.541  -10.259 25.927  1.00 39.65 ? 20  PHE A CA  1 
ATOM   132  C C   . PHE A 1 20  ? -5.297  -11.027 26.326  1.00 39.87 ? 20  PHE A C   1 
ATOM   133  O O   . PHE A 1 20  ? -4.915  -11.025 27.492  1.00 39.57 ? 20  PHE A O   1 
ATOM   134  C CB  . PHE A 1 20  ? -6.195  -8.777  25.855  1.00 39.88 ? 20  PHE A CB  1 
ATOM   135  C CG  . PHE A 1 20  ? -7.347  -7.905  25.475  1.00 39.59 ? 20  PHE A CG  1 
ATOM   136  C CD1 . PHE A 1 20  ? -8.258  -7.489  26.430  1.00 39.35 ? 20  PHE A CD1 1 
ATOM   137  C CD2 . PHE A 1 20  ? -7.532  -7.516  24.165  1.00 39.52 ? 20  PHE A CD2 1 
ATOM   138  C CE1 . PHE A 1 20  ? -9.332  -6.701  26.085  1.00 39.18 ? 20  PHE A CE1 1 
ATOM   139  C CE2 . PHE A 1 20  ? -8.606  -6.717  23.814  1.00 39.73 ? 20  PHE A CE2 1 
ATOM   140  C CZ  . PHE A 1 20  ? -9.502  -6.310  24.777  1.00 40.03 ? 20  PHE A CZ  1 
ATOM   141  N N   . GLU A 1 21  ? -4.677  -11.705 25.367  1.00 40.07 ? 21  GLU A N   1 
ATOM   142  C CA  . GLU A 1 21  ? -3.393  -12.344 25.609  1.00 40.06 ? 21  GLU A CA  1 
ATOM   143  C C   . GLU A 1 21  ? -2.476  -12.236 24.393  1.00 39.59 ? 21  GLU A C   1 
ATOM   144  O O   . GLU A 1 21  ? -2.905  -12.411 23.256  1.00 38.65 ? 21  GLU A O   1 
ATOM   145  C CB  . GLU A 1 21  ? -3.597  -13.804 25.992  1.00 40.38 ? 21  GLU A CB  1 
ATOM   146  C CG  . GLU A 1 21  ? -2.324  -14.524 26.375  1.00 40.71 ? 21  GLU A CG  1 
ATOM   147  C CD  . GLU A 1 21  ? -2.611  -15.787 27.140  1.00 42.22 ? 21  GLU A CD  1 
ATOM   148  O OE1 . GLU A 1 21  ? -2.250  -16.880 26.655  1.00 44.72 ? 21  GLU A OE1 1 
ATOM   149  O OE2 . GLU A 1 21  ? -3.224  -15.683 28.225  1.00 47.47 ? 21  GLU A OE2 1 
ATOM   150  N N   . GLN A 1 22  ? -1.205  -11.961 24.666  1.00 39.64 ? 22  GLN A N   1 
ATOM   151  C CA  . GLN A 1 22  ? -0.199  -11.763 23.643  1.00 40.01 ? 22  GLN A CA  1 
ATOM   152  C C   . GLN A 1 22  ? 1.101   -12.389 24.130  1.00 40.41 ? 22  GLN A C   1 
ATOM   153  O O   . GLN A 1 22  ? 1.770   -11.841 25.005  1.00 40.26 ? 22  GLN A O   1 
ATOM   154  C CB  . GLN A 1 22  ? -0.021  -10.264 23.396  1.00 39.89 ? 22  GLN A CB  1 
ATOM   155  C CG  . GLN A 1 22  ? 0.895   -9.925  22.239  1.00 39.66 ? 22  GLN A CG  1 
ATOM   156  C CD  . GLN A 1 22  ? 1.158   -8.450  22.113  1.00 39.61 ? 22  GLN A CD  1 
ATOM   157  O OE1 . GLN A 1 22  ? 0.946   -7.693  23.051  1.00 39.08 ? 22  GLN A OE1 1 
ATOM   158  N NE2 . GLN A 1 22  ? 1.625   -8.032  20.945  1.00 39.48 ? 22  GLN A NE2 1 
ATOM   159  N N   . LYS A 1 23  ? 1.453   -13.544 23.567  1.00 41.12 ? 23  LYS A N   1 
ATOM   160  C CA  . LYS A 1 23  ? 2.623   -14.297 24.024  1.00 41.86 ? 23  LYS A CA  1 
ATOM   161  C C   . LYS A 1 23  ? 3.970   -13.703 23.618  1.00 42.22 ? 23  LYS A C   1 
ATOM   162  O O   . LYS A 1 23  ? 4.975   -13.954 24.277  1.00 42.48 ? 23  LYS A O   1 
ATOM   163  C CB  . LYS A 1 23  ? 2.530   -15.753 23.569  1.00 41.89 ? 23  LYS A CB  1 
ATOM   164  C CG  . LYS A 1 23  ? 1.403   -16.487 24.267  1.00 42.28 ? 23  LYS A CG  1 
ATOM   165  C CD  . LYS A 1 23  ? 1.322   -17.960 23.858  1.00 42.49 ? 23  LYS A CD  1 
ATOM   166  C CE  . LYS A 1 23  ? 0.098   -18.613 24.488  1.00 42.88 ? 23  LYS A CE  1 
ATOM   167  N NZ  . LYS A 1 23  ? 0.070   -18.424 25.977  1.00 43.16 ? 23  LYS A NZ  1 
ATOM   168  N N   . GLU A 1 24  ? 3.991   -12.930 22.539  1.00 42.75 ? 24  GLU A N   1 
ATOM   169  C CA  . GLU A 1 24  ? 5.201   -12.236 22.108  1.00 43.17 ? 24  GLU A CA  1 
ATOM   170  C C   . GLU A 1 24  ? 4.830   -10.826 21.661  1.00 43.23 ? 24  GLU A C   1 
ATOM   171  O O   . GLU A 1 24  ? 3.763   -10.618 21.081  1.00 43.14 ? 24  GLU A O   1 
ATOM   172  C CB  . GLU A 1 24  ? 5.873   -12.999 20.964  1.00 43.36 ? 24  GLU A CB  1 
ATOM   173  C CG  . GLU A 1 24  ? 5.980   -14.511 21.203  1.00 44.18 ? 24  GLU A CG  1 
ATOM   174  C CD  . GLU A 1 24  ? 6.688   -15.248 20.084  1.00 44.42 ? 24  GLU A CD  1 
ATOM   175  O OE1 . GLU A 1 24  ? 7.113   -14.590 19.107  1.00 47.07 ? 24  GLU A OE1 1 
ATOM   176  O OE2 . GLU A 1 24  ? 6.820   -16.492 20.181  1.00 45.60 ? 24  GLU A OE2 1 
ATOM   177  N N   . SER A 1 25  ? 5.716   -9.867  21.912  1.00 43.36 ? 25  SER A N   1 
ATOM   178  C CA  . SER A 1 25  ? 5.446   -8.453  21.611  1.00 43.61 ? 25  SER A CA  1 
ATOM   179  C C   . SER A 1 25  ? 5.309   -8.144  20.112  1.00 43.80 ? 25  SER A C   1 
ATOM   180  O O   . SER A 1 25  ? 4.759   -7.108  19.737  1.00 43.81 ? 25  SER A O   1 
ATOM   181  C CB  . SER A 1 25  ? 6.532   -7.565  22.230  1.00 43.74 ? 25  SER A CB  1 
ATOM   182  O OG  . SER A 1 25  ? 7.818   -7.924  21.761  1.00 43.46 ? 25  SER A OG  1 
ATOM   183  N N   . ASN A 1 26  ? 5.821   -9.038  19.269  1.00 44.05 ? 26  ASN A N   1 
ATOM   184  C CA  . ASN A 1 26  ? 5.646   -8.953  17.810  1.00 44.26 ? 26  ASN A CA  1 
ATOM   185  C C   . ASN A 1 26  ? 4.431   -9.746  17.300  1.00 44.44 ? 26  ASN A C   1 
ATOM   186  O O   . ASN A 1 26  ? 4.102   -9.694  16.107  1.00 44.86 ? 26  ASN A O   1 
ATOM   187  C CB  . ASN A 1 26  ? 6.895   -9.481  17.101  1.00 44.31 ? 26  ASN A CB  1 
ATOM   188  C CG  . ASN A 1 26  ? 7.227   -10.914 17.498  1.00 45.17 ? 26  ASN A CG  1 
ATOM   189  O OD1 . ASN A 1 26  ? 7.164   -11.264 18.680  1.00 46.09 ? 26  ASN A OD1 1 
ATOM   190  N ND2 . ASN A 1 26  ? 7.587   -11.748 16.515  1.00 44.77 ? 26  ASN A ND2 1 
ATOM   191  N N   . GLY A 1 27  ? 3.776   -10.481 18.199  1.00 43.98 ? 27  GLY A N   1 
ATOM   192  C CA  . GLY A 1 27  ? 2.738   -11.425 17.811  1.00 43.39 ? 27  GLY A CA  1 
ATOM   193  C C   . GLY A 1 27  ? 1.334   -10.870 17.928  1.00 42.85 ? 27  GLY A C   1 
ATOM   194  O O   . GLY A 1 27  ? 1.126   -9.765  18.450  1.00 42.29 ? 27  GLY A O   1 
ATOM   195  N N   . PRO A 1 28  ? 0.355   -11.634 17.425  1.00 42.29 ? 28  PRO A N   1 
ATOM   196  C CA  . PRO A 1 28  ? -1.042  -11.245 17.556  1.00 42.15 ? 28  PRO A CA  1 
ATOM   197  C C   . PRO A 1 28  ? -1.541  -11.263 19.004  1.00 41.76 ? 28  PRO A C   1 
ATOM   198  O O   . PRO A 1 28  ? -0.941  -11.917 19.868  1.00 41.65 ? 28  PRO A O   1 
ATOM   199  C CB  . PRO A 1 28  ? -1.782  -12.295 16.724  1.00 42.10 ? 28  PRO A CB  1 
ATOM   200  C CG  . PRO A 1 28  ? -0.876  -13.447 16.660  1.00 42.40 ? 28  PRO A CG  1 
ATOM   201  C CD  . PRO A 1 28  ? 0.510   -12.899 16.687  1.00 42.44 ? 28  PRO A CD  1 
ATOM   202  N N   . VAL A 1 29  ? -2.623  -10.525 19.239  1.00 41.24 ? 29  VAL A N   1 
ATOM   203  C CA  . VAL A 1 29  ? -3.316  -10.492 20.516  1.00 41.11 ? 29  VAL A CA  1 
ATOM   204  C C   . VAL A 1 29  ? -4.605  -11.301 20.374  1.00 41.03 ? 29  VAL A C   1 
ATOM   205  O O   . VAL A 1 29  ? -5.487  -10.925 19.600  1.00 40.85 ? 29  VAL A O   1 
ATOM   206  C CB  . VAL A 1 29  ? -3.644  -9.036  20.935  1.00 41.13 ? 29  VAL A CB  1 
ATOM   207  C CG1 . VAL A 1 29  ? -4.254  -8.994  22.341  1.00 41.60 ? 29  VAL A CG1 1 
ATOM   208  C CG2 . VAL A 1 29  ? -2.392  -8.176  20.879  1.00 40.57 ? 29  VAL A CG2 1 
ATOM   209  N N   . LYS A 1 30  ? -4.684  -12.430 21.089  1.00 40.93 ? 30  LYS A N   1 
ATOM   210  C CA  . LYS A 1 30  ? -5.910  -13.225 21.182  1.00 40.74 ? 30  LYS A CA  1 
ATOM   211  C C   . LYS A 1 30  ? -6.914  -12.499 22.065  1.00 40.86 ? 30  LYS A C   1 
ATOM   212  O O   . LYS A 1 30  ? -6.572  -12.022 23.149  1.00 41.18 ? 30  LYS A O   1 
ATOM   213  C CB  . LYS A 1 30  ? -5.617  -14.626 21.733  1.00 40.76 ? 30  LYS A CB  1 
ATOM   214  C CG  . LYS A 1 30  ? -4.708  -15.437 20.833  1.00 40.59 ? 30  LYS A CG  1 
ATOM   215  C CD  . LYS A 1 30  ? -4.662  -16.927 21.198  1.00 41.12 ? 30  LYS A CD  1 
ATOM   216  C CE  . LYS A 1 30  ? -4.108  -17.748 20.038  1.00 40.67 ? 30  LYS A CE  1 
ATOM   217  N NZ  . LYS A 1 30  ? -3.959  -19.217 20.343  1.00 41.00 ? 30  LYS A NZ  1 
ATOM   218  N N   . VAL A 1 31  ? -8.142  -12.375 21.570  1.00 40.79 ? 31  VAL A N   1 
ATOM   219  C CA  . VAL A 1 31  ? -9.218  -11.659 22.259  1.00 40.53 ? 31  VAL A CA  1 
ATOM   220  C C   . VAL A 1 31  ? -10.377 -12.670 22.359  1.00 40.56 ? 31  VAL A C   1 
ATOM   221  O O   . VAL A 1 31  ? -10.934 -13.102 21.341  1.00 39.70 ? 31  VAL A O   1 
ATOM   222  C CB  . VAL A 1 31  ? -9.643  -10.385 21.483  1.00 40.87 ? 31  VAL A CB  1 
ATOM   223  C CG1 . VAL A 1 31  ? -10.554 -9.456  22.328  1.00 40.90 ? 31  VAL A CG1 1 
ATOM   224  C CG2 . VAL A 1 31  ? -8.421  -9.602  21.002  1.00 40.91 ? 31  VAL A CG2 1 
ATOM   225  N N   . TRP A 1 32  ? -10.695 -13.082 23.584  1.00 40.06 ? 32  TRP A N   1 
ATOM   226  C CA  . TRP A 1 32  ? -11.835 -13.942 23.813  1.00 39.96 ? 32  TRP A CA  1 
ATOM   227  C C   . TRP A 1 32  ? -12.612 -13.573 25.073  1.00 39.84 ? 32  TRP A C   1 
ATOM   228  O O   . TRP A 1 32  ? -12.050 -13.131 26.074  1.00 39.64 ? 32  TRP A O   1 
ATOM   229  C CB  . TRP A 1 32  ? -11.385 -15.412 23.877  1.00 39.66 ? 32  TRP A CB  1 
ATOM   230  C CG  . TRP A 1 32  ? -10.670 -15.777 25.134  1.00 39.32 ? 32  TRP A CG  1 
ATOM   231  C CD1 . TRP A 1 32  ? -11.186 -16.453 26.183  1.00 40.11 ? 32  TRP A CD1 1 
ATOM   232  C CD2 . TRP A 1 32  ? -9.306  -15.479 25.479  1.00 39.89 ? 32  TRP A CD2 1 
ATOM   233  N NE1 . TRP A 1 32  ? -10.233 -16.615 27.167  1.00 40.19 ? 32  TRP A NE1 1 
ATOM   234  C CE2 . TRP A 1 32  ? -9.073  -16.019 26.759  1.00 39.84 ? 32  TRP A CE2 1 
ATOM   235  C CE3 . TRP A 1 32  ? -8.262  -14.805 24.832  1.00 39.86 ? 32  TRP A CE3 1 
ATOM   236  C CZ2 . TRP A 1 32  ? -7.838  -15.918 27.404  1.00 40.07 ? 32  TRP A CZ2 1 
ATOM   237  C CZ3 . TRP A 1 32  ? -7.034  -14.706 25.476  1.00 39.76 ? 32  TRP A CZ3 1 
ATOM   238  C CH2 . TRP A 1 32  ? -6.835  -15.255 26.751  1.00 39.61 ? 32  TRP A CH2 1 
ATOM   239  N N   . GLY A 1 33  ? -13.918 -13.788 25.003  1.00 40.11 ? 33  GLY A N   1 
ATOM   240  C CA  . GLY A 1 33  ? -14.802 -13.641 26.148  1.00 40.29 ? 33  GLY A CA  1 
ATOM   241  C C   . GLY A 1 33  ? -16.237 -13.777 25.685  1.00 40.38 ? 33  GLY A C   1 
ATOM   242  O O   . GLY A 1 33  ? -16.521 -14.484 24.715  1.00 40.15 ? 33  GLY A O   1 
ATOM   243  N N   . SER A 1 34  ? -17.143 -13.111 26.387  1.00 40.54 ? 34  SER A N   1 
ATOM   244  C CA  . SER A 1 34  ? -18.515 -13.000 25.936  1.00 40.83 ? 34  SER A CA  1 
ATOM   245  C C   . SER A 1 34  ? -19.187 -11.762 26.503  1.00 40.76 ? 34  SER A C   1 
ATOM   246  O O   . SER A 1 34  ? -18.771 -11.215 27.522  1.00 40.71 ? 34  SER A O   1 
ATOM   247  C CB  . SER A 1 34  ? -19.323 -14.248 26.286  1.00 41.25 ? 34  SER A CB  1 
ATOM   248  O OG  . SER A 1 34  ? -19.629 -14.289 27.665  1.00 43.39 ? 34  SER A OG  1 
ATOM   249  N N   . ILE A 1 35  ? -20.218 -11.322 25.796  1.00 40.78 ? 35  ILE A N   1 
ATOM   250  C CA  . ILE A 1 35  ? -21.024 -10.182 26.189  1.00 40.59 ? 35  ILE A CA  1 
ATOM   251  C C   . ILE A 1 35  ? -22.483 -10.620 26.116  1.00 40.57 ? 35  ILE A C   1 
ATOM   252  O O   . ILE A 1 35  ? -22.892 -11.248 25.141  1.00 40.30 ? 35  ILE A O   1 
ATOM   253  C CB  . ILE A 1 35  ? -20.789 -8.982  25.252  1.00 40.53 ? 35  ILE A CB  1 
ATOM   254  C CG1 . ILE A 1 35  ? -19.293 -8.722  25.095  1.00 40.04 ? 35  ILE A CG1 1 
ATOM   255  C CG2 . ILE A 1 35  ? -21.476 -7.727  25.789  1.00 40.84 ? 35  ILE A CG2 1 
ATOM   256  C CD1 . ILE A 1 35  ? -18.976 -7.661  24.093  1.00 40.44 ? 35  ILE A CD1 1 
ATOM   257  N N   . LYS A 1 36  ? -23.249 -10.296 27.155  1.00 40.49 ? 36  LYS A N   1 
ATOM   258  C CA  . LYS A 1 36  ? -24.674 -10.587 27.188  1.00 40.45 ? 36  LYS A CA  1 
ATOM   259  C C   . LYS A 1 36  ? -25.468 -9.294  27.254  1.00 40.18 ? 36  LYS A C   1 
ATOM   260  O O   . LYS A 1 36  ? -24.899 -8.217  27.420  1.00 39.75 ? 36  LYS A O   1 
ATOM   261  C CB  . LYS A 1 36  ? -25.024 -11.510 28.365  1.00 40.56 ? 36  LYS A CB  1 
ATOM   262  C CG  . LYS A 1 36  ? -24.693 -10.971 29.762  1.00 40.82 ? 36  LYS A CG  1 
ATOM   263  C CD  . LYS A 1 36  ? -24.878 -12.080 30.809  1.00 40.93 ? 36  LYS A CD  1 
ATOM   264  C CE  . LYS A 1 36  ? -24.772 -11.564 32.237  1.00 41.34 ? 36  LYS A CE  1 
ATOM   265  N NZ  . LYS A 1 36  ? -25.409 -12.502 33.226  1.00 41.62 ? 36  LYS A NZ  1 
ATOM   266  N N   . GLY A 1 37  ? -26.785 -9.418  27.101  1.00 40.15 ? 37  GLY A N   1 
ATOM   267  C CA  . GLY A 1 37  ? -27.699 -8.277  27.151  1.00 40.09 ? 37  GLY A CA  1 
ATOM   268  C C   . GLY A 1 37  ? -27.768 -7.491  25.855  1.00 40.02 ? 37  GLY A C   1 
ATOM   269  O O   . GLY A 1 37  ? -28.312 -6.381  25.817  1.00 39.88 ? 37  GLY A O   1 
ATOM   270  N N   . LEU A 1 38  ? -27.218 -8.070  24.790  1.00 40.01 ? 38  LEU A N   1 
ATOM   271  C CA  . LEU A 1 38  ? -27.143 -7.404  23.499  1.00 39.66 ? 38  LEU A CA  1 
ATOM   272  C C   . LEU A 1 38  ? -28.396 -7.698  22.700  1.00 39.64 ? 38  LEU A C   1 
ATOM   273  O O   . LEU A 1 38  ? -29.014 -8.739  22.884  1.00 39.61 ? 38  LEU A O   1 
ATOM   274  C CB  . LEU A 1 38  ? -25.917 -7.891  22.722  1.00 39.56 ? 38  LEU A CB  1 
ATOM   275  C CG  . LEU A 1 38  ? -24.556 -7.436  23.251  1.00 39.24 ? 38  LEU A CG  1 
ATOM   276  C CD1 . LEU A 1 38  ? -23.428 -8.165  22.522  1.00 38.92 ? 38  LEU A CD1 1 
ATOM   277  C CD2 . LEU A 1 38  ? -24.403 -5.914  23.133  1.00 38.63 ? 38  LEU A CD2 1 
ATOM   278  N N   . THR A 1 39  ? -28.778 -6.769  21.829  1.00 39.60 ? 39  THR A N   1 
ATOM   279  C CA  . THR A 1 39  ? -29.780 -7.052  20.811  1.00 39.50 ? 39  THR A CA  1 
ATOM   280  C C   . THR A 1 39  ? -29.132 -7.949  19.761  1.00 39.40 ? 39  THR A C   1 
ATOM   281  O O   . THR A 1 39  ? -27.938 -7.788  19.453  1.00 39.10 ? 39  THR A O   1 
ATOM   282  C CB  . THR A 1 39  ? -30.291 -5.777  20.124  1.00 39.45 ? 39  THR A CB  1 
ATOM   283  O OG1 . THR A 1 39  ? -29.214 -5.152  19.415  1.00 40.33 ? 39  THR A OG1 1 
ATOM   284  C CG2 . THR A 1 39  ? -30.853 -4.806  21.140  1.00 39.61 ? 39  THR A CG2 1 
ATOM   285  N N   . GLU A 1 40  ? -29.911 -8.894  19.228  1.00 39.28 ? 40  GLU A N   1 
ATOM   286  C CA  . GLU A 1 40  ? -29.440 -9.803  18.185  1.00 39.53 ? 40  GLU A CA  1 
ATOM   287  C C   . GLU A 1 40  ? -28.829 -9.020  17.023  1.00 39.61 ? 40  GLU A C   1 
ATOM   288  O O   . GLU A 1 40  ? -29.382 -8.009  16.586  1.00 39.84 ? 40  GLU A O   1 
ATOM   289  C CB  . GLU A 1 40  ? -30.585 -10.690 17.675  1.00 39.57 ? 40  GLU A CB  1 
ATOM   290  C CG  . GLU A 1 40  ? -30.170 -11.665 16.575  1.00 39.49 ? 40  GLU A CG  1 
ATOM   291  C CD  . GLU A 1 40  ? -31.217 -12.725 16.270  1.00 40.17 ? 40  GLU A CD  1 
ATOM   292  O OE1 . GLU A 1 40  ? -32.392 -12.578 16.690  1.00 39.96 ? 40  GLU A OE1 1 
ATOM   293  O OE2 . GLU A 1 40  ? -30.853 -13.717 15.599  1.00 41.29 ? 40  GLU A OE2 1 
ATOM   294  N N   . GLY A 1 41  ? -27.677 -9.478  16.540  1.00 39.62 ? 41  GLY A N   1 
ATOM   295  C CA  . GLY A 1 41  ? -27.009 -8.834  15.419  1.00 39.41 ? 41  GLY A CA  1 
ATOM   296  C C   . GLY A 1 41  ? -25.635 -8.305  15.761  1.00 39.45 ? 41  GLY A C   1 
ATOM   297  O O   . GLY A 1 41  ? -25.058 -8.659  16.791  1.00 39.19 ? 41  GLY A O   1 
ATOM   298  N N   . LEU A 1 42  ? -25.127 -7.442  14.881  1.00 39.47 ? 42  LEU A N   1 
ATOM   299  C CA  . LEU A 1 42  ? -23.760 -6.948  14.951  1.00 39.38 ? 42  LEU A CA  1 
ATOM   300  C C   . LEU A 1 42  ? -23.684 -5.667  15.765  1.00 39.10 ? 42  LEU A C   1 
ATOM   301  O O   . LEU A 1 42  ? -24.546 -4.803  15.645  1.00 38.85 ? 42  LEU A O   1 
ATOM   302  C CB  . LEU A 1 42  ? -23.218 -6.665  13.549  1.00 39.47 ? 42  LEU A CB  1 
ATOM   303  C CG  . LEU A 1 42  ? -23.240 -7.804  12.542  1.00 40.62 ? 42  LEU A CG  1 
ATOM   304  C CD1 . LEU A 1 42  ? -22.770 -7.289  11.200  1.00 41.54 ? 42  LEU A CD1 1 
ATOM   305  C CD2 . LEU A 1 42  ? -22.377 -8.949  13.007  1.00 41.06 ? 42  LEU A CD2 1 
ATOM   306  N N   . HIS A 1 43  ? -22.632 -5.558  16.569  1.00 38.78 ? 43  HIS A N   1 
ATOM   307  C CA  . HIS A 1 43  ? -22.386 -4.387  17.401  1.00 38.85 ? 43  HIS A CA  1 
ATOM   308  C C   . HIS A 1 43  ? -20.925 -3.978  17.294  1.00 38.77 ? 43  HIS A C   1 
ATOM   309  O O   . HIS A 1 43  ? -20.041 -4.806  17.454  1.00 38.83 ? 43  HIS A O   1 
ATOM   310  C CB  . HIS A 1 43  ? -22.708 -4.716  18.857  1.00 38.77 ? 43  HIS A CB  1 
ATOM   311  C CG  . HIS A 1 43  ? -24.162 -4.924  19.113  1.00 38.09 ? 43  HIS A CG  1 
ATOM   312  N ND1 . HIS A 1 43  ? -25.008 -3.894  19.452  1.00 38.25 ? 43  HIS A ND1 1 
ATOM   313  C CD2 . HIS A 1 43  ? -24.927 -6.039  19.052  1.00 37.82 ? 43  HIS A CD2 1 
ATOM   314  C CE1 . HIS A 1 43  ? -26.233 -4.366  19.602  1.00 38.49 ? 43  HIS A CE1 1 
ATOM   315  N NE2 . HIS A 1 43  ? -26.212 -5.665  19.361  1.00 38.28 ? 43  HIS A NE2 1 
ATOM   316  N N   . GLY A 1 44  ? -20.667 -2.702  17.037  1.00 38.95 ? 44  GLY A N   1 
ATOM   317  C CA  . GLY A 1 44  ? -19.293 -2.219  16.976  1.00 39.17 ? 44  GLY A CA  1 
ATOM   318  C C   . GLY A 1 44  ? -18.507 -2.634  18.213  1.00 39.30 ? 44  GLY A C   1 
ATOM   319  O O   . GLY A 1 44  ? -19.053 -2.702  19.309  1.00 39.61 ? 44  GLY A O   1 
ATOM   320  N N   . PHE A 1 45  ? -17.226 -2.918  18.028  1.00 39.30 ? 45  PHE A N   1 
ATOM   321  C CA  . PHE A 1 45  ? -16.369 -3.404  19.098  1.00 39.47 ? 45  PHE A CA  1 
ATOM   322  C C   . PHE A 1 45  ? -15.041 -2.673  18.968  1.00 39.48 ? 45  PHE A C   1 
ATOM   323  O O   . PHE A 1 45  ? -14.200 -3.075  18.172  1.00 39.21 ? 45  PHE A O   1 
ATOM   324  C CB  . PHE A 1 45  ? -16.210 -4.910  18.912  1.00 39.63 ? 45  PHE A CB  1 
ATOM   325  C CG  . PHE A 1 45  ? -15.575 -5.617  20.064  1.00 39.84 ? 45  PHE A CG  1 
ATOM   326  C CD1 . PHE A 1 45  ? -16.166 -5.601  21.316  1.00 40.35 ? 45  PHE A CD1 1 
ATOM   327  C CD2 . PHE A 1 45  ? -14.421 -6.371  19.877  1.00 39.99 ? 45  PHE A CD2 1 
ATOM   328  C CE1 . PHE A 1 45  ? -15.594 -6.285  22.374  1.00 40.52 ? 45  PHE A CE1 1 
ATOM   329  C CE2 . PHE A 1 45  ? -13.844 -7.043  20.928  1.00 40.26 ? 45  PHE A CE2 1 
ATOM   330  C CZ  . PHE A 1 45  ? -14.429 -7.009  22.180  1.00 40.09 ? 45  PHE A CZ  1 
ATOM   331  N N   . HIS A 1 46  ? -14.882 -1.568  19.708  1.00 39.69 ? 46  HIS A N   1 
ATOM   332  C CA  . HIS A 1 46  ? -13.751 -0.644  19.506  1.00 39.64 ? 46  HIS A CA  1 
ATOM   333  C C   . HIS A 1 46  ? -12.932 -0.331  20.766  1.00 39.36 ? 46  HIS A C   1 
ATOM   334  O O   . HIS A 1 46  ? -13.469 -0.240  21.866  1.00 39.74 ? 46  HIS A O   1 
ATOM   335  C CB  . HIS A 1 46  ? -14.256 0.695   18.926  1.00 40.26 ? 46  HIS A CB  1 
ATOM   336  C CG  . HIS A 1 46  ? -14.959 0.552   17.609  1.00 41.05 ? 46  HIS A CG  1 
ATOM   337  N ND1 . HIS A 1 46  ? -15.976 1.391   17.211  1.00 40.88 ? 46  HIS A ND1 1 
ATOM   338  C CD2 . HIS A 1 46  ? -14.806 -0.354  16.609  1.00 41.13 ? 46  HIS A CD2 1 
ATOM   339  C CE1 . HIS A 1 46  ? -16.406 1.022   16.016  1.00 41.49 ? 46  HIS A CE1 1 
ATOM   340  N NE2 . HIS A 1 46  ? -15.713 -0.036  15.629  1.00 41.22 ? 46  HIS A NE2 1 
ATOM   341  N N   . VAL A 1 47  ? -11.631 -0.129  20.580  1.00 38.46 ? 47  VAL A N   1 
ATOM   342  C CA  . VAL A 1 47  ? -10.781 0.419   21.630  1.00 38.15 ? 47  VAL A CA  1 
ATOM   343  C C   . VAL A 1 47  ? -10.743 1.949   21.452  1.00 37.69 ? 47  VAL A C   1 
ATOM   344  O O   . VAL A 1 47  ? -10.444 2.447   20.361  1.00 37.53 ? 47  VAL A O   1 
ATOM   345  C CB  . VAL A 1 47  ? -9.367  -0.179  21.581  1.00 37.99 ? 47  VAL A CB  1 
ATOM   346  C CG1 . VAL A 1 47  ? -8.502  0.384   22.692  1.00 38.00 ? 47  VAL A CG1 1 
ATOM   347  C CG2 . VAL A 1 47  ? -9.443  -1.712  21.681  1.00 38.20 ? 47  VAL A CG2 1 
ATOM   348  N N   . HIS A 1 48  ? -11.081 2.677   22.518  1.00 37.40 ? 48  HIS A N   1 
ATOM   349  C CA  . HIS A 1 48  ? -11.083 4.149   22.508  1.00 37.34 ? 48  HIS A CA  1 
ATOM   350  C C   . HIS A 1 48  ? -9.884  4.649   23.293  1.00 37.23 ? 48  HIS A C   1 
ATOM   351  O O   . HIS A 1 48  ? -9.382  3.971   24.161  1.00 37.67 ? 48  HIS A O   1 
ATOM   352  C CB  . HIS A 1 48  ? -12.404 4.677   23.076  1.00 37.00 ? 48  HIS A CB  1 
ATOM   353  C CG  . HIS A 1 48  ? -13.578 4.389   22.191  1.00 36.70 ? 48  HIS A CG  1 
ATOM   354  N ND1 . HIS A 1 48  ? -14.242 5.371   21.489  1.00 36.55 ? 48  HIS A ND1 1 
ATOM   355  C CD2 . HIS A 1 48  ? -14.172 3.219   21.852  1.00 35.66 ? 48  HIS A CD2 1 
ATOM   356  C CE1 . HIS A 1 48  ? -15.201 4.822   20.764  1.00 36.99 ? 48  HIS A CE1 1 
ATOM   357  N NE2 . HIS A 1 48  ? -15.178 3.515   20.963  1.00 35.22 ? 48  HIS A NE2 1 
ATOM   358  N N   . GLU A 1 49  ? -9.422  5.845   22.992  1.00 37.67 ? 49  GLU A N   1 
ATOM   359  C CA  . GLU A 1 49  ? -8.091  6.246   23.417  1.00 38.05 ? 49  GLU A CA  1 
ATOM   360  C C   . GLU A 1 49  ? -7.900  6.313   24.934  1.00 38.44 ? 49  GLU A C   1 
ATOM   361  O O   . GLU A 1 49  ? -6.843  5.955   25.433  1.00 38.20 ? 49  GLU A O   1 
ATOM   362  C CB  . GLU A 1 49  ? -7.750  7.585   22.790  1.00 37.83 ? 49  GLU A CB  1 
ATOM   363  C CG  . GLU A 1 49  ? -6.314  8.029   22.988  1.00 37.34 ? 49  GLU A CG  1 
ATOM   364  C CD  . GLU A 1 49  ? -6.073  9.366   22.334  1.00 37.91 ? 49  GLU A CD  1 
ATOM   365  O OE1 . GLU A 1 49  ? -6.984  9.814   21.595  1.00 36.14 ? 49  GLU A OE1 1 
ATOM   366  O OE2 . GLU A 1 49  ? -4.986  9.953   22.552  1.00 36.40 ? 49  GLU A OE2 1 
ATOM   367  N N   . PHE A 1 50  ? -8.920  6.749   25.665  1.00 39.16 ? 50  PHE A N   1 
ATOM   368  C CA  . PHE A 1 50  ? -8.747  7.111   27.069  1.00 39.75 ? 50  PHE A CA  1 
ATOM   369  C C   . PHE A 1 50  ? -9.631  6.320   28.019  1.00 40.02 ? 50  PHE A C   1 
ATOM   370  O O   . PHE A 1 50  ? -10.699 5.860   27.648  1.00 40.27 ? 50  PHE A O   1 
ATOM   371  C CB  . PHE A 1 50  ? -9.090  8.591   27.268  1.00 39.96 ? 50  PHE A CB  1 
ATOM   372  C CG  . PHE A 1 50  ? -8.272  9.530   26.437  1.00 40.88 ? 50  PHE A CG  1 
ATOM   373  C CD1 . PHE A 1 50  ? -6.911  9.661   26.663  1.00 41.02 ? 50  PHE A CD1 1 
ATOM   374  C CD2 . PHE A 1 50  ? -8.866  10.304  25.453  1.00 40.39 ? 50  PHE A CD2 1 
ATOM   375  C CE1 . PHE A 1 50  ? -6.161  10.504  25.905  1.00 40.27 ? 50  PHE A CE1 1 
ATOM   376  C CE2 . PHE A 1 50  ? -8.124  11.149  24.691  1.00 40.13 ? 50  PHE A CE2 1 
ATOM   377  C CZ  . PHE A 1 50  ? -6.771  11.266  24.916  1.00 41.40 ? 50  PHE A CZ  1 
ATOM   378  N N   . GLY A 1 51  ? -9.189  6.217   29.266  1.00 40.67 ? 51  GLY A N   1 
ATOM   379  C CA  . GLY A 1 51  ? -10.060 5.853   30.374  1.00 41.07 ? 51  GLY A CA  1 
ATOM   380  C C   . GLY A 1 51  ? -11.016 6.975   30.775  1.00 41.65 ? 51  GLY A C   1 
ATOM   381  O O   . GLY A 1 51  ? -10.712 8.173   30.620  1.00 41.27 ? 51  GLY A O   1 
ATOM   382  N N   . ASP A 1 52  ? -12.176 6.574   31.296  1.00 42.40 ? 52  ASP A N   1 
ATOM   383  C CA  . ASP A 1 52  ? -13.160 7.484   31.874  1.00 43.02 ? 52  ASP A CA  1 
ATOM   384  C C   . ASP A 1 52  ? -12.549 8.370   32.938  1.00 43.49 ? 52  ASP A C   1 
ATOM   385  O O   . ASP A 1 52  ? -11.829 7.888   33.819  1.00 43.76 ? 52  ASP A O   1 
ATOM   386  C CB  . ASP A 1 52  ? -14.288 6.698   32.545  1.00 43.28 ? 52  ASP A CB  1 
ATOM   387  C CG  . ASP A 1 52  ? -15.221 6.017   31.551  1.00 44.01 ? 52  ASP A CG  1 
ATOM   388  O OD1 . ASP A 1 52  ? -14.908 5.936   30.333  1.00 43.89 ? 52  ASP A OD1 1 
ATOM   389  O OD2 . ASP A 1 52  ? -16.280 5.543   32.021  1.00 43.77 ? 52  ASP A OD2 1 
ATOM   390  N N   . ASN A 1 53  ? -12.860 9.661   32.860  1.00 43.77 ? 53  ASN A N   1 
ATOM   391  C CA  . ASN A 1 53  ? -12.484 10.626  33.884  1.00 44.10 ? 53  ASN A CA  1 
ATOM   392  C C   . ASN A 1 53  ? -13.700 11.134  34.678  1.00 44.20 ? 53  ASN A C   1 
ATOM   393  O O   . ASN A 1 53  ? -13.587 12.088  35.450  1.00 43.80 ? 53  ASN A O   1 
ATOM   394  C CB  . ASN A 1 53  ? -11.680 11.784  33.266  1.00 44.33 ? 53  ASN A CB  1 
ATOM   395  C CG  . ASN A 1 53  ? -12.493 12.640  32.295  1.00 45.31 ? 53  ASN A CG  1 
ATOM   396  O OD1 . ASN A 1 53  ? -12.040 13.714  31.878  1.00 48.08 ? 53  ASN A OD1 1 
ATOM   397  N ND2 . ASN A 1 53  ? -13.692 12.192  31.948  1.00 46.07 ? 53  ASN A ND2 1 
ATOM   398  N N   . THR A 1 54  ? -14.850 10.484  34.472  1.00 44.51 ? 54  THR A N   1 
ATOM   399  C CA  . THR A 1 54  ? -16.082 10.760  35.226  1.00 44.97 ? 54  THR A CA  1 
ATOM   400  C C   . THR A 1 54  ? -16.806 9.472   35.627  1.00 45.22 ? 54  THR A C   1 
ATOM   401  O O   . THR A 1 54  ? -16.616 8.410   35.019  1.00 45.23 ? 54  THR A O   1 
ATOM   402  C CB  . THR A 1 54  ? -17.104 11.622  34.421  1.00 44.90 ? 54  THR A CB  1 
ATOM   403  O OG1 . THR A 1 54  ? -17.436 10.969  33.186  1.00 45.24 ? 54  THR A OG1 1 
ATOM   404  C CG2 . THR A 1 54  ? -16.551 13.006  34.137  1.00 45.26 ? 54  THR A CG2 1 
ATOM   405  N N   . ALA A 1 55  ? -17.639 9.592   36.659  1.00 45.76 ? 55  ALA A N   1 
ATOM   406  C CA  . ALA A 1 55  ? -18.582 8.544   37.044  1.00 46.06 ? 55  ALA A CA  1 
ATOM   407  C C   . ALA A 1 55  ? -19.734 8.495   36.034  1.00 46.42 ? 55  ALA A C   1 
ATOM   408  O O   . ALA A 1 55  ? -20.238 9.538   35.602  1.00 46.64 ? 55  ALA A O   1 
ATOM   409  C CB  . ALA A 1 55  ? -19.125 8.813   38.440  1.00 45.98 ? 55  ALA A CB  1 
ATOM   410  N N   . GLY A 1 56  ? -20.149 7.287   35.664  1.00 46.72 ? 56  GLY A N   1 
ATOM   411  C CA  . GLY A 1 56  ? -21.266 7.112   34.736  1.00 47.00 ? 56  GLY A CA  1 
ATOM   412  C C   . GLY A 1 56  ? -21.123 7.897   33.436  1.00 47.39 ? 56  GLY A C   1 
ATOM   413  O O   . GLY A 1 56  ? -22.086 8.524   32.975  1.00 47.35 ? 56  GLY A O   1 
ATOM   414  N N   . ALA A 1 57  ? -19.917 7.867   32.856  1.00 47.53 ? 57  ALA A N   1 
ATOM   415  C CA  . ALA A 1 57  ? -19.660 8.484   31.556  1.00 47.37 ? 57  ALA A CA  1 
ATOM   416  C C   . ALA A 1 57  ? -20.548 7.825   30.511  1.00 47.45 ? 57  ALA A C   1 
ATOM   417  O O   . ALA A 1 57  ? -20.715 6.605   30.506  1.00 47.62 ? 57  ALA A O   1 
ATOM   418  C CB  . ALA A 1 57  ? -18.203 8.324   31.172  1.00 47.47 ? 57  ALA A CB  1 
ATOM   419  N N   . THR A 1 58  ? -21.126 8.635   29.634  1.00 47.50 ? 58  THR A N   1 
ATOM   420  C CA  . THR A 1 58  ? -21.965 8.125   28.553  1.00 47.60 ? 58  THR A CA  1 
ATOM   421  C C   . THR A 1 58  ? -21.223 8.126   27.218  1.00 47.68 ? 58  THR A C   1 
ATOM   422  O O   . THR A 1 58  ? -21.520 7.309   26.339  1.00 47.63 ? 58  THR A O   1 
ATOM   423  C CB  . THR A 1 58  ? -23.271 8.950   28.415  1.00 47.81 ? 58  THR A CB  1 
ATOM   424  O OG1 . THR A 1 58  ? -22.962 10.352  28.356  1.00 47.79 ? 58  THR A OG1 1 
ATOM   425  C CG2 . THR A 1 58  ? -24.197 8.680   29.599  1.00 48.05 ? 58  THR A CG2 1 
ATOM   426  N N   . SER A 1 59  ? -20.265 9.040   27.060  1.00 47.60 ? 59  SER A N   1 
ATOM   427  C CA  . SER A 1 59  ? -19.514 9.137   25.817  1.00 47.42 ? 59  SER A CA  1 
ATOM   428  C C   . SER A 1 59  ? -18.480 8.036   25.711  1.00 47.32 ? 59  SER A C   1 
ATOM   429  O O   . SER A 1 59  ? -17.844 7.676   26.700  1.00 47.21 ? 59  SER A O   1 
ATOM   430  C CB  . SER A 1 59  ? -18.794 10.476  25.701  1.00 47.55 ? 59  SER A CB  1 
ATOM   431  O OG  . SER A 1 59  ? -18.108 10.542  24.458  1.00 47.89 ? 59  SER A OG  1 
ATOM   432  N N   . ALA A 1 60  ? -18.302 7.538   24.488  1.00 47.18 ? 60  ALA A N   1 
ATOM   433  C CA  . ALA A 1 60  ? -17.256 6.574   24.172  1.00 46.99 ? 60  ALA A CA  1 
ATOM   434  C C   . ALA A 1 60  ? -15.863 7.231   24.113  1.00 46.92 ? 60  ALA A C   1 
ATOM   435  O O   . ALA A 1 60  ? -14.855 6.597   24.443  1.00 47.20 ? 60  ALA A O   1 
ATOM   436  C CB  . ALA A 1 60  ? -17.574 5.898   22.859  1.00 47.13 ? 60  ALA A CB  1 
ATOM   437  N N   . GLY A 1 61  ? -15.814 8.498   23.694  1.00 46.72 ? 61  GLY A N   1 
ATOM   438  C CA  . GLY A 1 61  ? -14.550 9.235   23.543  1.00 46.04 ? 61  GLY A CA  1 
ATOM   439  C C   . GLY A 1 61  ? -13.854 8.874   22.243  1.00 45.71 ? 61  GLY A C   1 
ATOM   440  O O   . GLY A 1 61  ? -14.295 7.962   21.526  1.00 45.80 ? 61  GLY A O   1 
ATOM   441  N N   . PRO A 1 62  ? -12.752 9.568   21.924  1.00 44.81 ? 62  PRO A N   1 
ATOM   442  C CA  . PRO A 1 62  ? -12.068 9.303   20.660  1.00 44.38 ? 62  PRO A CA  1 
ATOM   443  C C   . PRO A 1 62  ? -11.635 7.847   20.477  1.00 43.90 ? 62  PRO A C   1 
ATOM   444  O O   . PRO A 1 62  ? -11.280 7.167   21.442  1.00 43.73 ? 62  PRO A O   1 
ATOM   445  C CB  . PRO A 1 62  ? -10.848 10.238  20.712  1.00 44.89 ? 62  PRO A CB  1 
ATOM   446  C CG  . PRO A 1 62  ? -11.232 11.329  21.662  1.00 44.49 ? 62  PRO A CG  1 
ATOM   447  C CD  . PRO A 1 62  ? -12.115 10.659  22.685  1.00 45.36 ? 62  PRO A CD  1 
ATOM   448  N N   . HIS A 1 63  ? -11.701 7.365   19.245  1.00 43.20 ? 63  HIS A N   1 
ATOM   449  C CA  . HIS A 1 63  ? -11.126 6.064   18.903  1.00 42.64 ? 63  HIS A CA  1 
ATOM   450  C C   . HIS A 1 63  ? -9.617  6.099   19.143  1.00 41.70 ? 63  HIS A C   1 
ATOM   451  O O   . HIS A 1 63  ? -9.000  7.158   19.063  1.00 41.01 ? 63  HIS A O   1 
ATOM   452  C CB  . HIS A 1 63  ? -11.379 5.732   17.434  1.00 43.15 ? 63  HIS A CB  1 
ATOM   453  C CG  . HIS A 1 63  ? -12.741 5.172   17.154  1.00 44.78 ? 63  HIS A CG  1 
ATOM   454  N ND1 . HIS A 1 63  ? -13.903 5.891   17.347  1.00 45.69 ? 63  HIS A ND1 1 
ATOM   455  C CD2 . HIS A 1 63  ? -13.120 3.970   16.654  1.00 45.73 ? 63  HIS A CD2 1 
ATOM   456  C CE1 . HIS A 1 63  ? -14.940 5.143   17.009  1.00 45.22 ? 63  HIS A CE1 1 
ATOM   457  N NE2 . HIS A 1 63  ? -14.493 3.976   16.579  1.00 45.11 ? 63  HIS A NE2 1 
ATOM   458  N N   . PHE A 1 64  ? -9.030  4.941   19.443  1.00 40.88 ? 64  PHE A N   1 
ATOM   459  C CA  . PHE A 1 64  ? -7.569  4.820   19.500  1.00 40.80 ? 64  PHE A CA  1 
ATOM   460  C C   . PHE A 1 64  ? -6.994  4.750   18.075  1.00 40.26 ? 64  PHE A C   1 
ATOM   461  O O   . PHE A 1 64  ? -7.085  3.717   17.400  1.00 40.24 ? 64  PHE A O   1 
ATOM   462  C CB  . PHE A 1 64  ? -7.134  3.595   20.322  1.00 40.35 ? 64  PHE A CB  1 
ATOM   463  C CG  . PHE A 1 64  ? -5.657  3.529   20.571  1.00 39.95 ? 64  PHE A CG  1 
ATOM   464  C CD1 . PHE A 1 64  ? -4.946  4.673   20.939  1.00 39.65 ? 64  PHE A CD1 1 
ATOM   465  C CD2 . PHE A 1 64  ? -4.974  2.334   20.444  1.00 39.22 ? 64  PHE A CD2 1 
ATOM   466  C CE1 . PHE A 1 64  ? -3.589  4.624   21.166  1.00 39.97 ? 64  PHE A CE1 1 
ATOM   467  C CE2 . PHE A 1 64  ? -3.613  2.278   20.677  1.00 39.56 ? 64  PHE A CE2 1 
ATOM   468  C CZ  . PHE A 1 64  ? -2.917  3.430   21.037  1.00 39.77 ? 64  PHE A CZ  1 
ATOM   469  N N   . ASN A 1 65  ? -6.405  5.859   17.646  1.00 39.75 ? 65  ASN A N   1 
ATOM   470  C CA  . ASN A 1 65  ? -6.013  6.060   16.256  1.00 39.81 ? 65  ASN A CA  1 
ATOM   471  C C   . ASN A 1 65  ? -4.740  6.901   16.195  1.00 39.64 ? 65  ASN A C   1 
ATOM   472  O O   . ASN A 1 65  ? -4.739  7.996   15.627  1.00 39.60 ? 65  ASN A O   1 
ATOM   473  C CB  . ASN A 1 65  ? -7.161  6.752   15.504  1.00 39.57 ? 65  ASN A CB  1 
ATOM   474  C CG  . ASN A 1 65  ? -6.887  6.928   14.024  1.00 39.55 ? 65  ASN A CG  1 
ATOM   475  O OD1 . ASN A 1 65  ? -6.093  6.201   13.426  1.00 37.96 ? 65  ASN A OD1 1 
ATOM   476  N ND2 . ASN A 1 65  ? -7.550  7.914   13.422  1.00 39.69 ? 65  ASN A ND2 1 
ATOM   477  N N   . PRO A 1 66  ? -3.641  6.384   16.778  1.00 39.66 ? 66  PRO A N   1 
ATOM   478  C CA  . PRO A 1 66  ? -2.390  7.142   16.862  1.00 39.82 ? 66  PRO A CA  1 
ATOM   479  C C   . PRO A 1 66  ? -1.735  7.433   15.503  1.00 39.87 ? 66  PRO A C   1 
ATOM   480  O O   . PRO A 1 66  ? -1.000  8.417   15.372  1.00 39.34 ? 66  PRO A O   1 
ATOM   481  C CB  . PRO A 1 66  ? -1.495  6.234   17.713  1.00 39.84 ? 66  PRO A CB  1 
ATOM   482  C CG  . PRO A 1 66  ? -2.028  4.866   17.481  1.00 39.31 ? 66  PRO A CG  1 
ATOM   483  C CD  . PRO A 1 66  ? -3.500  5.040   17.364  1.00 39.25 ? 66  PRO A CD  1 
ATOM   484  N N   . LEU A 1 67  ? -1.999  6.585   14.509  1.00 40.15 ? 67  LEU A N   1 
ATOM   485  C CA  . LEU A 1 67  ? -1.442  6.774   13.165  1.00 40.44 ? 67  LEU A CA  1 
ATOM   486  C C   . LEU A 1 67  ? -2.319  7.654   12.268  1.00 40.70 ? 67  LEU A C   1 
ATOM   487  O O   . LEU A 1 67  ? -1.982  7.868   11.102  1.00 40.92 ? 67  LEU A O   1 
ATOM   488  C CB  . LEU A 1 67  ? -1.207  5.417   12.493  1.00 40.40 ? 67  LEU A CB  1 
ATOM   489  C CG  . LEU A 1 67  ? -0.263  4.450   13.207  1.00 40.50 ? 67  LEU A CG  1 
ATOM   490  C CD1 . LEU A 1 67  ? 0.009   3.239   12.328  1.00 40.86 ? 67  LEU A CD1 1 
ATOM   491  C CD2 . LEU A 1 67  ? 1.049   5.139   13.586  1.00 41.74 ? 67  LEU A CD2 1 
ATOM   492  N N   . SER A 1 68  ? -3.429  8.161   12.811  1.00 40.85 ? 68  SER A N   1 
ATOM   493  C CA  . SER A 1 68  ? -4.336  9.062   12.098  1.00 41.10 ? 68  SER A CA  1 
ATOM   494  C C   . SER A 1 68  ? -4.836  8.496   10.768  1.00 41.31 ? 68  SER A C   1 
ATOM   495  O O   . SER A 1 68  ? -4.801  9.169   9.737   1.00 41.12 ? 68  SER A O   1 
ATOM   496  C CB  . SER A 1 68  ? -3.677  10.426  11.896  1.00 41.06 ? 68  SER A CB  1 
ATOM   497  O OG  . SER A 1 68  ? -3.544  11.092  13.136  1.00 41.97 ? 68  SER A OG  1 
ATOM   498  N N   . ARG A 1 69  ? -5.297  7.251   10.800  1.00 41.62 ? 69  ARG A N   1 
ATOM   499  C CA  . ARG A 1 69  ? -5.867  6.615   9.620   1.00 42.14 ? 69  ARG A CA  1 
ATOM   500  C C   . ARG A 1 69  ? -7.371  6.839   9.617   1.00 42.14 ? 69  ARG A C   1 
ATOM   501  O O   . ARG A 1 69  ? -7.940  7.307   10.603  1.00 42.32 ? 69  ARG A O   1 
ATOM   502  C CB  . ARG A 1 69  ? -5.605  5.103   9.627   1.00 43.07 ? 69  ARG A CB  1 
ATOM   503  C CG  . ARG A 1 69  ? -4.164  4.684   9.843   1.00 44.31 ? 69  ARG A CG  1 
ATOM   504  C CD  . ARG A 1 69  ? -3.305  5.070   8.683   1.00 47.60 ? 69  ARG A CD  1 
ATOM   505  N NE  . ARG A 1 69  ? -1.974  4.460   8.754   1.00 48.76 ? 69  ARG A NE  1 
ATOM   506  C CZ  . ARG A 1 69  ? -1.689  3.183   8.466   1.00 50.32 ? 69  ARG A CZ  1 
ATOM   507  N NH1 . ARG A 1 69  ? -2.642  2.326   8.093   1.00 50.68 ? 69  ARG A NH1 1 
ATOM   508  N NH2 . ARG A 1 69  ? -0.430  2.753   8.556   1.00 49.68 ? 69  ARG A NH2 1 
ATOM   509  N N   . LYS A 1 70  ? -8.017  6.493   8.509   1.00 42.01 ? 70  LYS A N   1 
ATOM   510  C CA  . LYS A 1 70  ? -9.473  6.507   8.445   1.00 41.74 ? 70  LYS A CA  1 
ATOM   511  C C   . LYS A 1 70  ? -9.983  5.229   9.091   1.00 41.34 ? 70  LYS A C   1 
ATOM   512  O O   . LYS A 1 70  ? -9.259  4.236   9.176   1.00 40.93 ? 70  LYS A O   1 
ATOM   513  C CB  . LYS A 1 70  ? -9.966  6.628   7.000   1.00 41.78 ? 70  LYS A CB  1 
ATOM   514  C CG  . LYS A 1 70  ? -9.523  7.919   6.329   1.00 42.63 ? 70  LYS A CG  1 
ATOM   515  C CD  . LYS A 1 70  ? -10.043 8.051   4.898   1.00 42.98 ? 70  LYS A CD  1 
ATOM   516  C CE  . LYS A 1 70  ? -9.255  9.101   4.096   1.00 43.59 ? 70  LYS A CE  1 
ATOM   517  N NZ  . LYS A 1 70  ? -7.983  8.567   3.495   1.00 44.08 ? 70  LYS A NZ  1 
ATOM   518  N N   . HIS A 1 71  ? -11.225 5.274   9.571   1.00 40.88 ? 71  HIS A N   1 
ATOM   519  C CA  . HIS A 1 71  ? -11.854 4.123   10.194  1.00 40.63 ? 71  HIS A CA  1 
ATOM   520  C C   . HIS A 1 71  ? -12.065 3.033   9.154   1.00 40.49 ? 71  HIS A C   1 
ATOM   521  O O   . HIS A 1 71  ? -12.508 3.311   8.043   1.00 40.39 ? 71  HIS A O   1 
ATOM   522  C CB  . HIS A 1 71  ? -13.191 4.514   10.819  1.00 40.25 ? 71  HIS A CB  1 
ATOM   523  C CG  . HIS A 1 71  ? -13.987 3.346   11.290  1.00 40.07 ? 71  HIS A CG  1 
ATOM   524  N ND1 . HIS A 1 71  ? -13.639 2.617   12.402  1.00 39.77 ? 71  HIS A ND1 1 
ATOM   525  C CD2 . HIS A 1 71  ? -15.098 2.760   10.786  1.00 39.89 ? 71  HIS A CD2 1 
ATOM   526  C CE1 . HIS A 1 71  ? -14.498 1.625   12.562  1.00 40.67 ? 71  HIS A CE1 1 
ATOM   527  N NE2 . HIS A 1 71  ? -15.393 1.688   11.593  1.00 40.00 ? 71  HIS A NE2 1 
ATOM   528  N N   . GLY A 1 72  ? -11.739 1.796   9.521   1.00 40.61 ? 72  GLY A N   1 
ATOM   529  C CA  . GLY A 1 72  ? -11.975 0.641   8.658   1.00 40.79 ? 72  GLY A CA  1 
ATOM   530  C C   . GLY A 1 72  ? -12.351 -0.609  9.434   1.00 40.86 ? 72  GLY A C   1 
ATOM   531  O O   . GLY A 1 72  ? -12.628 -0.561  10.634  1.00 41.14 ? 72  GLY A O   1 
ATOM   532  N N   . GLY A 1 73  ? -12.380 -1.731  8.736   1.00 40.98 ? 73  GLY A N   1 
ATOM   533  C CA  . GLY A 1 73  ? -12.539 -3.024  9.382   1.00 41.47 ? 73  GLY A CA  1 
ATOM   534  C C   . GLY A 1 73  ? -11.190 -3.500  9.898   1.00 41.69 ? 73  GLY A C   1 
ATOM   535  O O   . GLY A 1 73  ? -10.160 -2.919  9.565   1.00 41.64 ? 73  GLY A O   1 
ATOM   536  N N   . PRO A 1 74  ? -11.185 -4.559  10.720  1.00 42.10 ? 74  PRO A N   1 
ATOM   537  C CA  . PRO A 1 74  ? -9.928  -5.078  11.245  1.00 42.34 ? 74  PRO A CA  1 
ATOM   538  C C   . PRO A 1 74  ? -9.045  -5.780  10.215  1.00 42.77 ? 74  PRO A C   1 
ATOM   539  O O   . PRO A 1 74  ? -7.853  -5.978  10.467  1.00 42.88 ? 74  PRO A O   1 
ATOM   540  C CB  . PRO A 1 74  ? -10.384 -6.055  12.333  1.00 42.36 ? 74  PRO A CB  1 
ATOM   541  C CG  . PRO A 1 74  ? -11.741 -6.472  11.933  1.00 42.28 ? 74  PRO A CG  1 
ATOM   542  C CD  . PRO A 1 74  ? -12.350 -5.299  11.237  1.00 42.11 ? 74  PRO A CD  1 
ATOM   543  N N   . LYS A 1 75  ? -9.619  -6.168  9.079   1.00 43.09 ? 75  LYS A N   1 
ATOM   544  C CA  . LYS A 1 75  ? -8.853  -6.793  8.011   1.00 43.23 ? 75  LYS A CA  1 
ATOM   545  C C   . LYS A 1 75  ? -8.162  -5.766  7.108   1.00 43.24 ? 75  LYS A C   1 
ATOM   546  O O   . LYS A 1 75  ? -7.249  -6.119  6.358   1.00 43.42 ? 75  LYS A O   1 
ATOM   547  C CB  . LYS A 1 75  ? -9.762  -7.683  7.161   1.00 43.71 ? 75  LYS A CB  1 
ATOM   548  C CG  . LYS A 1 75  ? -10.382 -8.846  7.918   1.00 43.79 ? 75  LYS A CG  1 
ATOM   549  C CD  . LYS A 1 75  ? -11.314 -9.657  7.013   1.00 44.17 ? 75  LYS A CD  1 
ATOM   550  C CE  . LYS A 1 75  ? -11.888 -10.880 7.747   1.00 45.32 ? 75  LYS A CE  1 
ATOM   551  N NZ  . LYS A 1 75  ? -12.369 -10.545 9.151   1.00 46.44 ? 75  LYS A NZ  1 
ATOM   552  N N   . ASP A 1 76  ? -8.594  -4.506  7.183   1.00 43.05 ? 76  ASP A N   1 
ATOM   553  C CA  . ASP A 1 76  ? -8.126  -3.461  6.271   1.00 43.01 ? 76  ASP A CA  1 
ATOM   554  C C   . ASP A 1 76  ? -6.788  -2.877  6.710   1.00 42.99 ? 76  ASP A C   1 
ATOM   555  O O   . ASP A 1 76  ? -6.529  -2.760  7.902   1.00 42.72 ? 76  ASP A O   1 
ATOM   556  C CB  . ASP A 1 76  ? -9.155  -2.328  6.195   1.00 42.85 ? 76  ASP A CB  1 
ATOM   557  C CG  . ASP A 1 76  ? -10.516 -2.792  5.705   1.00 43.04 ? 76  ASP A CG  1 
ATOM   558  O OD1 . ASP A 1 76  ? -10.603 -3.793  4.962   1.00 44.30 ? 76  ASP A OD1 1 
ATOM   559  O OD2 . ASP A 1 76  ? -11.514 -2.144  6.069   1.00 43.24 ? 76  ASP A OD2 1 
ATOM   560  N N   . GLU A 1 77  ? -5.940  -2.502  5.753   1.00 43.17 ? 77  GLU A N   1 
ATOM   561  C CA  . GLU A 1 77  ? -4.684  -1.827  6.092   1.00 43.23 ? 77  GLU A CA  1 
ATOM   562  C C   . GLU A 1 77  ? -4.981  -0.411  6.600   1.00 43.04 ? 77  GLU A C   1 
ATOM   563  O O   . GLU A 1 77  ? -4.316  0.091   7.517   1.00 42.79 ? 77  GLU A O   1 
ATOM   564  C CB  . GLU A 1 77  ? -3.707  -1.782  4.902   1.00 43.55 ? 77  GLU A CB  1 
ATOM   565  C CG  . GLU A 1 77  ? -2.437  -0.962  5.197   1.00 43.82 ? 77  GLU A CG  1 
ATOM   566  C CD  . GLU A 1 77  ? -1.204  -1.371  4.379   1.00 44.81 ? 77  GLU A CD  1 
ATOM   567  O OE1 . GLU A 1 77  ? -1.346  -1.829  3.213   1.00 47.33 ? 77  GLU A OE1 1 
ATOM   568  O OE2 . GLU A 1 77  ? -0.076  -1.202  4.908   1.00 45.93 ? 77  GLU A OE2 1 
ATOM   569  N N   . GLU A 1 78  ? -5.983  0.223   5.997   1.00 42.65 ? 78  GLU A N   1 
ATOM   570  C CA  . GLU A 1 78  ? -6.439  1.532   6.433   1.00 42.07 ? 78  GLU A CA  1 
ATOM   571  C C   . GLU A 1 78  ? -7.487  1.333   7.538   1.00 41.42 ? 78  GLU A C   1 
ATOM   572  O O   . GLU A 1 78  ? -8.637  0.968   7.275   1.00 41.27 ? 78  GLU A O   1 
ATOM   573  C CB  . GLU A 1 78  ? -7.002  2.315   5.241   1.00 42.50 ? 78  GLU A CB  1 
ATOM   574  C CG  . GLU A 1 78  ? -7.283  3.799   5.520   1.00 43.17 ? 78  GLU A CG  1 
ATOM   575  C CD  . GLU A 1 78  ? -6.028  4.649   5.688   1.00 44.75 ? 78  GLU A CD  1 
ATOM   576  O OE1 . GLU A 1 78  ? -4.915  4.212   5.280   1.00 45.54 ? 78  GLU A OE1 1 
ATOM   577  O OE2 . GLU A 1 78  ? -6.171  5.772   6.228   1.00 44.29 ? 78  GLU A OE2 1 
ATOM   578  N N   . ARG A 1 79  ? -7.060  1.551   8.779   1.00 40.67 ? 79  ARG A N   1 
ATOM   579  C CA  . ARG A 1 79  ? -7.909  1.391   9.954   1.00 40.08 ? 79  ARG A CA  1 
ATOM   580  C C   . ARG A 1 79  ? -7.268  2.076   11.145  1.00 39.69 ? 79  ARG A C   1 
ATOM   581  O O   . ARG A 1 79  ? -6.082  2.373   11.124  1.00 39.58 ? 79  ARG A O   1 
ATOM   582  C CB  . ARG A 1 79  ? -8.110  -0.090  10.279  1.00 39.88 ? 79  ARG A CB  1 
ATOM   583  C CG  . ARG A 1 79  ? -6.824  -0.848  10.540  1.00 39.81 ? 79  ARG A CG  1 
ATOM   584  C CD  . ARG A 1 79  ? -7.080  -2.213  11.130  1.00 39.04 ? 79  ARG A CD  1 
ATOM   585  N NE  . ARG A 1 79  ? -7.161  -2.176  12.591  1.00 37.83 ? 79  ARG A NE  1 
ATOM   586  C CZ  . ARG A 1 79  ? -7.106  -3.249  13.373  1.00 38.23 ? 79  ARG A CZ  1 
ATOM   587  N NH1 . ARG A 1 79  ? -6.996  -4.461  12.851  1.00 35.83 ? 79  ARG A NH1 1 
ATOM   588  N NH2 . ARG A 1 79  ? -7.166  -3.107  14.691  1.00 38.66 ? 79  ARG A NH2 1 
ATOM   589  N N   . HIS A 1 80  ? -8.064  2.327   12.177  1.00 39.65 ? 80  HIS A N   1 
ATOM   590  C CA  . HIS A 1 80  ? -7.538  2.732   13.472  1.00 39.60 ? 80  HIS A CA  1 
ATOM   591  C C   . HIS A 1 80  ? -6.954  1.523   14.163  1.00 39.27 ? 80  HIS A C   1 
ATOM   592  O O   . HIS A 1 80  ? -7.359  0.395   13.900  1.00 39.40 ? 80  HIS A O   1 
ATOM   593  C CB  . HIS A 1 80  ? -8.625  3.291   14.391  1.00 39.54 ? 80  HIS A CB  1 
ATOM   594  C CG  . HIS A 1 80  ? -9.436  4.390   13.793  1.00 40.02 ? 80  HIS A CG  1 
ATOM   595  N ND1 . HIS A 1 80  ? -10.694 4.710   14.253  1.00 39.88 ? 80  HIS A ND1 1 
ATOM   596  C CD2 . HIS A 1 80  ? -9.177  5.242   12.775  1.00 39.45 ? 80  HIS A CD2 1 
ATOM   597  C CE1 . HIS A 1 80  ? -11.170 5.719   13.548  1.00 38.82 ? 80  HIS A CE1 1 
ATOM   598  N NE2 . HIS A 1 80  ? -10.273 6.054   12.639  1.00 38.23 ? 80  HIS A NE2 1 
ATOM   599  N N   . VAL A 1 81  ? -6.024  1.755   15.078  1.00 39.36 ? 81  VAL A N   1 
ATOM   600  C CA  . VAL A 1 81  ? -5.489  0.668   15.906  1.00 39.50 ? 81  VAL A CA  1 
ATOM   601  C C   . VAL A 1 81  ? -6.627  -0.042  16.661  1.00 39.50 ? 81  VAL A C   1 
ATOM   602  O O   . VAL A 1 81  ? -6.625  -1.266  16.798  1.00 39.82 ? 81  VAL A O   1 
ATOM   603  C CB  . VAL A 1 81  ? -4.408  1.180   16.891  1.00 39.48 ? 81  VAL A CB  1 
ATOM   604  C CG1 . VAL A 1 81  ? -3.982  0.086   17.860  1.00 39.11 ? 81  VAL A CG1 1 
ATOM   605  C CG2 . VAL A 1 81  ? -3.207  1.691   16.120  1.00 39.83 ? 81  VAL A CG2 1 
ATOM   606  N N   . GLY A 1 82  ? -7.610  0.728   17.120  1.00 39.44 ? 82  GLY A N   1 
ATOM   607  C CA  . GLY A 1 82  ? -8.708  0.186   17.914  1.00 38.94 ? 82  GLY A CA  1 
ATOM   608  C C   . GLY A 1 82  ? -9.878  -0.393  17.133  1.00 38.78 ? 82  GLY A C   1 
ATOM   609  O O   . GLY A 1 82  ? -10.901 -0.735  17.728  1.00 38.67 ? 82  GLY A O   1 
ATOM   610  N N   . ASP A 1 83  ? -9.746  -0.515  15.813  1.00 38.45 ? 83  ASP A N   1 
ATOM   611  C CA  . ASP A 1 83  ? -10.847 -1.004  14.972  1.00 38.12 ? 83  ASP A CA  1 
ATOM   612  C C   . ASP A 1 83  ? -10.931 -2.517  14.998  1.00 38.02 ? 83  ASP A C   1 
ATOM   613  O O   . ASP A 1 83  ? -10.411 -3.179  14.109  1.00 37.84 ? 83  ASP A O   1 
ATOM   614  C CB  . ASP A 1 83  ? -10.684 -0.552  13.517  1.00 38.12 ? 83  ASP A CB  1 
ATOM   615  C CG  . ASP A 1 83  ? -11.016 0.924   13.307  1.00 37.85 ? 83  ASP A CG  1 
ATOM   616  O OD1 . ASP A 1 83  ? -11.632 1.549   14.195  1.00 39.58 ? 83  ASP A OD1 1 
ATOM   617  O OD2 . ASP A 1 83  ? -10.670 1.444   12.230  1.00 36.98 ? 83  ASP A OD2 1 
ATOM   618  N N   . LEU A 1 84  ? -11.630 -3.051  15.993  1.00 38.30 ? 84  LEU A N   1 
ATOM   619  C CA  . LEU A 1 84  ? -11.790 -4.505  16.130  1.00 38.26 ? 84  LEU A CA  1 
ATOM   620  C C   . LEU A 1 84  ? -13.091 -5.018  15.531  1.00 38.43 ? 84  LEU A C   1 
ATOM   621  O O   . LEU A 1 84  ? -13.421 -6.202  15.653  1.00 38.46 ? 84  LEU A O   1 
ATOM   622  C CB  . LEU A 1 84  ? -11.697 -4.893  17.599  1.00 38.44 ? 84  LEU A CB  1 
ATOM   623  C CG  . LEU A 1 84  ? -10.417 -4.449  18.300  1.00 38.29 ? 84  LEU A CG  1 
ATOM   624  C CD1 . LEU A 1 84  ? -10.490 -4.803  19.769  1.00 38.06 ? 84  LEU A CD1 1 
ATOM   625  C CD2 . LEU A 1 84  ? -9.218  -5.086  17.637  1.00 39.70 ? 84  LEU A CD2 1 
ATOM   626  N N   . GLY A 1 85  ? -13.823 -4.129  14.874  1.00 38.65 ? 85  GLY A N   1 
ATOM   627  C CA  . GLY A 1 85  ? -14.935 -4.520  14.022  1.00 38.81 ? 85  GLY A CA  1 
ATOM   628  C C   . GLY A 1 85  ? -16.231 -4.714  14.767  1.00 38.75 ? 85  GLY A C   1 
ATOM   629  O O   . GLY A 1 85  ? -16.657 -3.846  15.521  1.00 38.77 ? 85  GLY A O   1 
ATOM   630  N N   . ASN A 1 86  ? -16.839 -5.876  14.559  1.00 39.02 ? 86  ASN A N   1 
ATOM   631  C CA  . ASN A 1 86  ? -18.141 -6.178  15.106  1.00 39.19 ? 86  ASN A CA  1 
ATOM   632  C C   . ASN A 1 86  ? -18.133 -7.466  15.895  1.00 39.64 ? 86  ASN A C   1 
ATOM   633  O O   . ASN A 1 86  ? -17.514 -8.466  15.489  1.00 39.61 ? 86  ASN A O   1 
ATOM   634  C CB  . ASN A 1 86  ? -19.170 -6.304  13.972  1.00 39.22 ? 86  ASN A CB  1 
ATOM   635  C CG  . ASN A 1 86  ? -19.627 -4.957  13.449  1.00 38.95 ? 86  ASN A CG  1 
ATOM   636  O OD1 . ASN A 1 86  ? -20.083 -4.119  14.215  1.00 38.29 ? 86  ASN A OD1 1 
ATOM   637  N ND2 . ASN A 1 86  ? -19.512 -4.746  12.140  1.00 38.89 ? 86  ASN A ND2 1 
ATOM   638  N N   . VAL A 1 87  ? -18.852 -7.446  17.012  1.00 39.66 ? 87  VAL A N   1 
ATOM   639  C CA  . VAL A 1 87  ? -19.231 -8.679  17.701  1.00 39.80 ? 87  VAL A CA  1 
ATOM   640  C C   . VAL A 1 87  ? -20.655 -9.046  17.289  1.00 39.59 ? 87  VAL A C   1 
ATOM   641  O O   . VAL A 1 87  ? -21.452 -8.169  16.972  1.00 39.03 ? 87  VAL A O   1 
ATOM   642  C CB  . VAL A 1 87  ? -19.121 -8.529  19.246  1.00 40.09 ? 87  VAL A CB  1 
ATOM   643  C CG1 . VAL A 1 87  ? -17.693 -8.161  19.635  1.00 40.26 ? 87  VAL A CG1 1 
ATOM   644  C CG2 . VAL A 1 87  ? -20.113 -7.490  19.797  1.00 39.94 ? 87  VAL A CG2 1 
ATOM   645  N N   . THR A 1 88  ? -20.972 -10.342 17.298  1.00 39.84 ? 88  THR A N   1 
ATOM   646  C CA  . THR A 1 88  ? -22.287 -10.819 16.875  1.00 40.06 ? 88  THR A CA  1 
ATOM   647  C C   . THR A 1 88  ? -23.054 -11.420 18.049  1.00 40.24 ? 88  THR A C   1 
ATOM   648  O O   . THR A 1 88  ? -22.595 -12.387 18.657  1.00 39.96 ? 88  THR A O   1 
ATOM   649  C CB  . THR A 1 88  ? -22.175 -11.899 15.771  1.00 40.09 ? 88  THR A CB  1 
ATOM   650  O OG1 . THR A 1 88  ? -21.372 -11.399 14.698  1.00 40.92 ? 88  THR A OG1 1 
ATOM   651  C CG2 . THR A 1 88  ? -23.548 -12.266 15.232  1.00 39.78 ? 88  THR A CG2 1 
ATOM   652  N N   . ALA A 1 89  ? -24.226 -10.853 18.337  1.00 40.30 ? 89  ALA A N   1 
ATOM   653  C CA  . ALA A 1 89  ? -25.112 -11.354 19.383  1.00 40.48 ? 89  ALA A CA  1 
ATOM   654  C C   . ALA A 1 89  ? -26.132 -12.320 18.784  1.00 40.60 ? 89  ALA A C   1 
ATOM   655  O O   . ALA A 1 89  ? -26.718 -12.046 17.739  1.00 40.68 ? 89  ALA A O   1 
ATOM   656  C CB  . ALA A 1 89  ? -25.823 -10.202 20.073  1.00 40.39 ? 89  ALA A CB  1 
ATOM   657  N N   . ASP A 1 90  ? -26.336 -13.449 19.454  1.00 40.83 ? 90  ASP A N   1 
ATOM   658  C CA  . ASP A 1 90  ? -27.339 -14.422 19.040  1.00 41.20 ? 90  ASP A CA  1 
ATOM   659  C C   . ASP A 1 90  ? -28.741 -13.936 19.436  1.00 41.20 ? 90  ASP A C   1 
ATOM   660  O O   . ASP A 1 90  ? -28.889 -12.819 19.938  1.00 41.13 ? 90  ASP A O   1 
ATOM   661  C CB  . ASP A 1 90  ? -27.012 -15.820 19.613  1.00 41.31 ? 90  ASP A CB  1 
ATOM   662  C CG  . ASP A 1 90  ? -27.090 -15.886 21.131  1.00 41.63 ? 90  ASP A CG  1 
ATOM   663  O OD1 . ASP A 1 90  ? -27.535 -14.910 21.766  1.00 42.66 ? 90  ASP A OD1 1 
ATOM   664  O OD2 . ASP A 1 90  ? -26.707 -16.933 21.694  1.00 41.70 ? 90  ASP A OD2 1 
ATOM   665  N N   . LYS A 1 91  ? -29.757 -14.769 19.210  1.00 41.36 ? 91  LYS A N   1 
ATOM   666  C CA  . LYS A 1 91  ? -31.146 -14.394 19.485  1.00 41.51 ? 91  LYS A CA  1 
ATOM   667  C C   . LYS A 1 91  ? -31.423 -14.211 20.975  1.00 41.61 ? 91  LYS A C   1 
ATOM   668  O O   . LYS A 1 91  ? -32.406 -13.570 21.346  1.00 41.83 ? 91  LYS A O   1 
ATOM   669  C CB  . LYS A 1 91  ? -32.118 -15.436 18.914  1.00 41.64 ? 91  LYS A CB  1 
ATOM   670  C CG  . LYS A 1 91  ? -32.117 -16.786 19.646  1.00 41.98 ? 91  LYS A CG  1 
ATOM   671  C CD  . LYS A 1 91  ? -33.351 -17.606 19.318  1.00 42.09 ? 91  LYS A CD  1 
ATOM   672  C CE  . LYS A 1 91  ? -33.304 -18.970 19.991  1.00 42.69 ? 91  LYS A CE  1 
ATOM   673  N NZ  . LYS A 1 91  ? -33.486 -18.873 21.465  1.00 43.29 ? 91  LYS A NZ  1 
ATOM   674  N N   . ASP A 1 92  ? -30.577 -14.807 21.817  1.00 41.54 ? 92  ASP A N   1 
ATOM   675  C CA  . ASP A 1 92  ? -30.659 -14.637 23.271  1.00 41.42 ? 92  ASP A CA  1 
ATOM   676  C C   . ASP A 1 92  ? -29.903 -13.401 23.749  1.00 40.87 ? 92  ASP A C   1 
ATOM   677  O O   . ASP A 1 92  ? -29.977 -13.049 24.919  1.00 40.43 ? 92  ASP A O   1 
ATOM   678  C CB  . ASP A 1 92  ? -30.100 -15.869 23.989  1.00 41.42 ? 92  ASP A CB  1 
ATOM   679  C CG  . ASP A 1 92  ? -30.917 -17.111 23.734  1.00 42.21 ? 92  ASP A CG  1 
ATOM   680  O OD1 . ASP A 1 92  ? -32.168 -17.040 23.786  1.00 42.72 ? 92  ASP A OD1 1 
ATOM   681  O OD2 . ASP A 1 92  ? -30.304 -18.170 23.485  1.00 42.47 ? 92  ASP A OD2 1 
ATOM   682  N N   . GLY A 1 93  ? -29.171 -12.758 22.847  1.00 40.72 ? 93  GLY A N   1 
ATOM   683  C CA  . GLY A 1 93  ? -28.408 -11.560 23.172  1.00 40.69 ? 93  GLY A CA  1 
ATOM   684  C C   . GLY A 1 93  ? -27.007 -11.813 23.696  1.00 40.41 ? 93  GLY A C   1 
ATOM   685  O O   . GLY A 1 93  ? -26.387 -10.914 24.254  1.00 40.00 ? 93  GLY A O   1 
ATOM   686  N N   . VAL A 1 94  ? -26.511 -13.034 23.510  1.00 40.57 ? 94  VAL A N   1 
ATOM   687  C CA  . VAL A 1 94  ? -25.166 -13.411 23.931  1.00 40.90 ? 94  VAL A CA  1 
ATOM   688  C C   . VAL A 1 94  ? -24.236 -13.406 22.720  1.00 41.13 ? 94  VAL A C   1 
ATOM   689  O O   . VAL A 1 94  ? -24.562 -13.948 21.664  1.00 41.24 ? 94  VAL A O   1 
ATOM   690  C CB  . VAL A 1 94  ? -25.133 -14.808 24.574  1.00 40.88 ? 94  VAL A CB  1 
ATOM   691  C CG1 . VAL A 1 94  ? -23.694 -15.208 24.934  1.00 40.70 ? 94  VAL A CG1 1 
ATOM   692  C CG2 . VAL A 1 94  ? -26.036 -14.853 25.805  1.00 40.80 ? 94  VAL A CG2 1 
ATOM   693  N N   . ALA A 1 95  ? -23.079 -12.787 22.892  1.00 41.42 ? 95  ALA A N   1 
ATOM   694  C CA  . ALA A 1 95  ? -22.076 -12.721 21.857  1.00 41.79 ? 95  ALA A CA  1 
ATOM   695  C C   . ALA A 1 95  ? -20.808 -13.317 22.409  1.00 42.01 ? 95  ALA A C   1 
ATOM   696  O O   . ALA A 1 95  ? -20.175 -12.714 23.269  1.00 42.07 ? 95  ALA A O   1 
ATOM   697  C CB  . ALA A 1 95  ? -21.834 -11.279 21.450  1.00 41.73 ? 95  ALA A CB  1 
ATOM   698  N N   . ASP A 1 96  ? -20.441 -14.501 21.925  1.00 42.38 ? 96  ASP A N   1 
ATOM   699  C CA  . ASP A 1 96  ? -19.157 -15.085 22.276  1.00 43.01 ? 96  ASP A CA  1 
ATOM   700  C C   . ASP A 1 96  ? -18.081 -14.611 21.314  1.00 43.15 ? 96  ASP A C   1 
ATOM   701  O O   . ASP A 1 96  ? -18.203 -14.759 20.093  1.00 43.05 ? 96  ASP A O   1 
ATOM   702  C CB  . ASP A 1 96  ? -19.227 -16.608 22.362  1.00 43.44 ? 96  ASP A CB  1 
ATOM   703  C CG  . ASP A 1 96  ? -19.465 -17.078 23.789  1.00 45.94 ? 96  ASP A CG  1 
ATOM   704  O OD1 . ASP A 1 96  ? -18.516 -17.625 24.398  1.00 49.65 ? 96  ASP A OD1 1 
ATOM   705  O OD2 . ASP A 1 96  ? -20.579 -16.846 24.326  1.00 48.55 ? 96  ASP A OD2 1 
ATOM   706  N N   . VAL A 1 97  ? -17.050 -13.999 21.891  1.00 43.50 ? 97  VAL A N   1 
ATOM   707  C CA  . VAL A 1 97  ? -15.980 -13.359 21.135  1.00 43.37 ? 97  VAL A CA  1 
ATOM   708  C C   . VAL A 1 97  ? -14.778 -14.297 21.110  1.00 43.60 ? 97  VAL A C   1 
ATOM   709  O O   . VAL A 1 97  ? -14.388 -14.854 22.145  1.00 43.18 ? 97  VAL A O   1 
ATOM   710  C CB  . VAL A 1 97  ? -15.589 -12.021 21.768  1.00 43.55 ? 97  VAL A CB  1 
ATOM   711  C CG1 . VAL A 1 97  ? -14.441 -11.359 20.993  1.00 43.45 ? 97  VAL A CG1 1 
ATOM   712  C CG2 . VAL A 1 97  ? -16.808 -11.092 21.839  1.00 43.08 ? 97  VAL A CG2 1 
ATOM   713  N N   . SER A 1 98  ? -14.229 -14.504 19.916  1.00 43.69 ? 98  SER A N   1 
ATOM   714  C CA  . SER A 1 98  ? -12.988 -15.247 19.750  1.00 43.63 ? 98  SER A CA  1 
ATOM   715  C C   . SER A 1 98  ? -12.279 -14.752 18.496  1.00 43.83 ? 98  SER A C   1 
ATOM   716  O O   . SER A 1 98  ? -12.478 -15.281 17.403  1.00 43.80 ? 98  SER A O   1 
ATOM   717  C CB  . SER A 1 98  ? -13.256 -16.742 19.670  1.00 43.71 ? 98  SER A CB  1 
ATOM   718  O OG  . SER A 1 98  ? -12.040 -17.468 19.692  1.00 43.67 ? 98  SER A OG  1 
ATOM   719  N N   . ILE A 1 99  ? -11.480 -13.702 18.657  1.00 43.72 ? 99  ILE A N   1 
ATOM   720  C CA  . ILE A 1 99  ? -10.737 -13.139 17.539  1.00 43.71 ? 99  ILE A CA  1 
ATOM   721  C C   . ILE A 1 99  ? -9.239  -13.099 17.832  1.00 43.51 ? 99  ILE A C   1 
ATOM   722  O O   . ILE A 1 99  ? -8.792  -13.402 18.939  1.00 43.57 ? 99  ILE A O   1 
ATOM   723  C CB  . ILE A 1 99  ? -11.258 -11.725 17.146  1.00 44.00 ? 99  ILE A CB  1 
ATOM   724  C CG1 . ILE A 1 99  ? -11.014 -10.722 18.258  1.00 43.58 ? 99  ILE A CG1 1 
ATOM   725  C CG2 . ILE A 1 99  ? -12.753 -11.785 16.804  1.00 45.05 ? 99  ILE A CG2 1 
ATOM   726  C CD1 . ILE A 1 99  ? -11.101 -9.279  17.797  1.00 44.12 ? 99  ILE A CD1 1 
ATOM   727  N N   . GLU A 1 100 ? -8.483  -12.750 16.800  1.00 43.04 ? 100 GLU A N   1 
ATOM   728  C CA  . GLU A 1 100 ? -7.048  -12.597 16.874  1.00 42.76 ? 100 GLU A CA  1 
ATOM   729  C C   . GLU A 1 100 ? -6.777  -11.307 16.122  1.00 42.34 ? 100 GLU A C   1 
ATOM   730  O O   . GLU A 1 100 ? -7.351  -11.090 15.053  1.00 42.33 ? 100 GLU A O   1 
ATOM   731  C CB  . GLU A 1 100 ? -6.376  -13.802 16.205  1.00 43.08 ? 100 GLU A CB  1 
ATOM   732  C CG  . GLU A 1 100 ? -4.908  -14.022 16.559  1.00 43.18 ? 100 GLU A CG  1 
ATOM   733  C CD  . GLU A 1 100 ? -4.468  -15.470 16.377  1.00 43.76 ? 100 GLU A CD  1 
ATOM   734  O OE1 . GLU A 1 100 ? -5.080  -16.360 17.007  1.00 45.04 ? 100 GLU A OE1 1 
ATOM   735  O OE2 . GLU A 1 100 ? -3.504  -15.717 15.612  1.00 44.32 ? 100 GLU A OE2 1 
ATOM   736  N N   . ASP A 1 101 ? -5.967  -10.422 16.693  1.00 41.69 ? 101 ASP A N   1 
ATOM   737  C CA  . ASP A 1 101 ? -5.618  -9.183  16.008  1.00 41.24 ? 101 ASP A CA  1 
ATOM   738  C C   . ASP A 1 101 ? -4.122  -8.936  16.077  1.00 40.58 ? 101 ASP A C   1 
ATOM   739  O O   . ASP A 1 101 ? -3.503  -9.146  17.115  1.00 39.89 ? 101 ASP A O   1 
ATOM   740  C CB  . ASP A 1 101 ? -6.374  -7.995  16.600  1.00 41.56 ? 101 ASP A CB  1 
ATOM   741  C CG  . ASP A 1 101 ? -6.385  -6.803  15.667  1.00 42.25 ? 101 ASP A CG  1 
ATOM   742  O OD1 . ASP A 1 101 ? -7.091  -6.855  14.636  1.00 44.31 ? 101 ASP A OD1 1 
ATOM   743  O OD2 . ASP A 1 101 ? -5.670  -5.826  15.944  1.00 44.33 ? 101 ASP A OD2 1 
ATOM   744  N N   . SER A 1 102 ? -3.551  -8.500  14.955  1.00 40.16 ? 102 SER A N   1 
ATOM   745  C CA  . SER A 1 102 ? -2.124  -8.213  14.866  1.00 39.83 ? 102 SER A CA  1 
ATOM   746  C C   . SER A 1 102 ? -1.827  -6.708  14.827  1.00 39.31 ? 102 SER A C   1 
ATOM   747  O O   . SER A 1 102 ? -0.689  -6.310  14.601  1.00 39.31 ? 102 SER A O   1 
ATOM   748  C CB  . SER A 1 102 ? -1.540  -8.901  13.630  1.00 39.97 ? 102 SER A CB  1 
ATOM   749  O OG  . SER A 1 102 ? -1.635  -10.321 13.742  1.00 41.11 ? 102 SER A OG  1 
ATOM   750  N N   . VAL A 1 103 ? -2.835  -5.874  15.061  1.00 38.86 ? 103 VAL A N   1 
ATOM   751  C CA  . VAL A 1 103 ? -2.649  -4.424  15.033  1.00 38.64 ? 103 VAL A CA  1 
ATOM   752  C C   . VAL A 1 103 ? -2.623  -3.829  16.437  1.00 38.47 ? 103 VAL A C   1 
ATOM   753  O O   . VAL A 1 103 ? -1.796  -2.964  16.741  1.00 38.69 ? 103 VAL A O   1 
ATOM   754  C CB  . VAL A 1 103 ? -3.716  -3.730  14.180  1.00 38.48 ? 103 VAL A CB  1 
ATOM   755  C CG1 . VAL A 1 103 ? -3.517  -2.217  14.210  1.00 37.78 ? 103 VAL A CG1 1 
ATOM   756  C CG2 . VAL A 1 103 ? -3.633  -4.241  12.744  1.00 38.83 ? 103 VAL A CG2 1 
ATOM   757  N N   . ILE A 1 104 ? -3.537  -4.271  17.285  1.00 38.01 ? 104 ILE A N   1 
ATOM   758  C CA  . ILE A 1 104 ? -3.457  -3.923  18.688  1.00 37.73 ? 104 ILE A CA  1 
ATOM   759  C C   . ILE A 1 104 ? -2.252  -4.608  19.282  1.00 37.36 ? 104 ILE A C   1 
ATOM   760  O O   . ILE A 1 104 ? -1.745  -5.572  18.727  1.00 37.46 ? 104 ILE A O   1 
ATOM   761  C CB  . ILE A 1 104 ? -4.724  -4.313  19.476  1.00 37.54 ? 104 ILE A CB  1 
ATOM   762  C CG1 . ILE A 1 104 ? -5.010  -5.815  19.361  1.00 37.64 ? 104 ILE A CG1 1 
ATOM   763  C CG2 . ILE A 1 104 ? -5.891  -3.503  18.993  1.00 37.59 ? 104 ILE A CG2 1 
ATOM   764  C CD1 . ILE A 1 104 ? -6.156  -6.282  20.245  1.00 37.74 ? 104 ILE A CD1 1 
ATOM   765  N N   . SER A 1 105 ? -1.794  -4.093  20.413  1.00 37.27 ? 105 SER A N   1 
ATOM   766  C CA  . SER A 1 105 ? -0.711  -4.705  21.163  1.00 37.18 ? 105 SER A CA  1 
ATOM   767  C C   . SER A 1 105 ? -0.980  -4.477  22.637  1.00 37.15 ? 105 SER A C   1 
ATOM   768  O O   . SER A 1 105 ? -1.785  -3.611  22.992  1.00 36.52 ? 105 SER A O   1 
ATOM   769  C CB  . SER A 1 105 ? 0.620   -4.075  20.770  1.00 37.19 ? 105 SER A CB  1 
ATOM   770  O OG  . SER A 1 105 ? 1.706   -4.736  21.383  1.00 36.91 ? 105 SER A OG  1 
ATOM   771  N N   . LEU A 1 106 ? -0.332  -5.272  23.486  1.00 37.43 ? 106 LEU A N   1 
ATOM   772  C CA  . LEU A 1 106 ? -0.390  -5.076  24.934  1.00 38.10 ? 106 LEU A CA  1 
ATOM   773  C C   . LEU A 1 106 ? 0.882   -4.416  25.450  1.00 38.61 ? 106 LEU A C   1 
ATOM   774  O O   . LEU A 1 106 ? 1.035   -4.228  26.652  1.00 38.81 ? 106 LEU A O   1 
ATOM   775  C CB  . LEU A 1 106 ? -0.621  -6.407  25.649  1.00 38.06 ? 106 LEU A CB  1 
ATOM   776  C CG  . LEU A 1 106 ? -1.949  -7.078  25.300  1.00 38.60 ? 106 LEU A CG  1 
ATOM   777  C CD1 . LEU A 1 106 ? -2.181  -8.251  26.215  1.00 38.84 ? 106 LEU A CD1 1 
ATOM   778  C CD2 . LEU A 1 106 ? -3.122  -6.055  25.369  1.00 38.71 ? 106 LEU A CD2 1 
ATOM   779  N N   . SER A 1 107 ? 1.791   -4.070  24.537  1.00 39.15 ? 107 SER A N   1 
ATOM   780  C CA  . SER A 1 107 ? 3.027   -3.374  24.886  1.00 39.53 ? 107 SER A CA  1 
ATOM   781  C C   . SER A 1 107 ? 3.397   -2.434  23.749  1.00 39.76 ? 107 SER A C   1 
ATOM   782  O O   . SER A 1 107 ? 2.862   -2.547  22.651  1.00 39.78 ? 107 SER A O   1 
ATOM   783  C CB  . SER A 1 107 ? 4.160   -4.376  25.171  1.00 39.63 ? 107 SER A CB  1 
ATOM   784  O OG  . SER A 1 107 ? 4.362   -5.266  24.088  1.00 40.39 ? 107 SER A OG  1 
ATOM   785  N N   . GLY A 1 108 ? 4.286   -1.485  24.027  1.00 40.11 ? 108 GLY A N   1 
ATOM   786  C CA  . GLY A 1 108 ? 4.745   -0.545  23.016  1.00 40.40 ? 108 GLY A CA  1 
ATOM   787  C C   . GLY A 1 108 ? 3.808   0.628   22.764  1.00 40.80 ? 108 GLY A C   1 
ATOM   788  O O   . GLY A 1 108 ? 2.864   0.876   23.520  1.00 40.72 ? 108 GLY A O   1 
ATOM   789  N N   . ASP A 1 109 ? 4.102   1.354   21.689  1.00 41.06 ? 109 ASP A N   1 
ATOM   790  C CA  . ASP A 1 109 ? 3.347   2.530   21.256  1.00 41.36 ? 109 ASP A CA  1 
ATOM   791  C C   . ASP A 1 109 ? 1.856   2.289   21.065  1.00 41.50 ? 109 ASP A C   1 
ATOM   792  O O   . ASP A 1 109 ? 1.039   3.150   21.399  1.00 42.13 ? 109 ASP A O   1 
ATOM   793  C CB  . ASP A 1 109 ? 3.919   3.042   19.924  1.00 41.51 ? 109 ASP A CB  1 
ATOM   794  C CG  . ASP A 1 109 ? 5.218   3.776   20.095  1.00 42.16 ? 109 ASP A CG  1 
ATOM   795  O OD1 . ASP A 1 109 ? 5.608   4.000   21.259  1.00 43.53 ? 109 ASP A OD1 1 
ATOM   796  O OD2 . ASP A 1 109 ? 5.851   4.141   19.072  1.00 42.49 ? 109 ASP A OD2 1 
ATOM   797  N N   . HIS A 1 110 ? 1.512   1.138   20.494  1.00 41.32 ? 110 HIS A N   1 
ATOM   798  C CA  . HIS A 1 110 ? 0.113   0.778   20.249  1.00 41.14 ? 110 HIS A CA  1 
ATOM   799  C C   . HIS A 1 110 ? -0.519  -0.045  21.377  1.00 40.17 ? 110 HIS A C   1 
ATOM   800  O O   . HIS A 1 110 ? -1.584  -0.615  21.181  1.00 40.68 ? 110 HIS A O   1 
ATOM   801  C CB  . HIS A 1 110 ? -0.032  0.034   18.912  1.00 41.64 ? 110 HIS A CB  1 
ATOM   802  C CG  . HIS A 1 110 ? 0.362   0.855   17.722  1.00 42.54 ? 110 HIS A CG  1 
ATOM   803  N ND1 . HIS A 1 110 ? 0.379   0.346   16.438  1.00 42.19 ? 110 HIS A ND1 1 
ATOM   804  C CD2 . HIS A 1 110 ? 0.774   2.145   17.624  1.00 42.86 ? 110 HIS A CD2 1 
ATOM   805  C CE1 . HIS A 1 110 ? 0.771   1.293   15.601  1.00 42.95 ? 110 HIS A CE1 1 
ATOM   806  N NE2 . HIS A 1 110 ? 1.020   2.392   16.295  1.00 42.66 ? 110 HIS A NE2 1 
ATOM   807  N N   . ALA A 1 111 ? 0.122   -0.088  22.548  1.00 39.24 ? 111 ALA A N   1 
ATOM   808  C CA  . ALA A 1 111 ? -0.453  -0.742  23.730  1.00 38.48 ? 111 ALA A CA  1 
ATOM   809  C C   . ALA A 1 111 ? -1.848  -0.225  24.040  1.00 37.68 ? 111 ALA A C   1 
ATOM   810  O O   . ALA A 1 111 ? -2.079  0.983   24.074  1.00 36.57 ? 111 ALA A O   1 
ATOM   811  C CB  . ALA A 1 111 ? 0.431   -0.529  24.944  1.00 38.45 ? 111 ALA A CB  1 
ATOM   812  N N   . ILE A 1 112 ? -2.767  -1.147  24.284  1.00 36.95 ? 112 ILE A N   1 
ATOM   813  C CA  . ILE A 1 112 ? -4.133  -0.796  24.648  1.00 37.02 ? 112 ILE A CA  1 
ATOM   814  C C   . ILE A 1 112 ? -4.416  -0.966  26.144  1.00 36.83 ? 112 ILE A C   1 
ATOM   815  O O   . ILE A 1 112 ? -5.546  -0.786  26.575  1.00 37.01 ? 112 ILE A O   1 
ATOM   816  C CB  . ILE A 1 112 ? -5.167  -1.568  23.822  1.00 36.61 ? 112 ILE A CB  1 
ATOM   817  C CG1 . ILE A 1 112 ? -5.029  -3.086  24.032  1.00 37.20 ? 112 ILE A CG1 1 
ATOM   818  C CG2 . ILE A 1 112 ? -5.024  -1.220  22.353  1.00 37.05 ? 112 ILE A CG2 1 
ATOM   819  C CD1 . ILE A 1 112 ? -6.083  -3.874  23.343  1.00 37.25 ? 112 ILE A CD1 1 
ATOM   820  N N   . ILE A 1 113 ? -3.389  -1.281  26.931  1.00 37.08 ? 113 ILE A N   1 
ATOM   821  C CA  . ILE A 1 113 ? -3.509  -1.324  28.386  1.00 37.09 ? 113 ILE A CA  1 
ATOM   822  C C   . ILE A 1 113 ? -3.792  0.091   28.861  1.00 36.81 ? 113 ILE A C   1 
ATOM   823  O O   . ILE A 1 113 ? -3.120  1.021   28.438  1.00 36.26 ? 113 ILE A O   1 
ATOM   824  C CB  . ILE A 1 113 ? -2.194  -1.810  29.064  1.00 37.46 ? 113 ILE A CB  1 
ATOM   825  C CG1 . ILE A 1 113 ? -1.798  -3.212  28.584  1.00 38.01 ? 113 ILE A CG1 1 
ATOM   826  C CG2 . ILE A 1 113 ? -2.316  -1.796  30.607  1.00 37.58 ? 113 ILE A CG2 1 
ATOM   827  C CD1 . ILE A 1 113 ? -2.796  -4.280  28.879  1.00 38.74 ? 113 ILE A CD1 1 
ATOM   828  N N   . GLY A 1 114 ? -4.796  0.255   29.717  1.00 36.64 ? 114 GLY A N   1 
ATOM   829  C CA  . GLY A 1 114 ? -5.172  1.582   30.206  1.00 36.90 ? 114 GLY A CA  1 
ATOM   830  C C   . GLY A 1 114 ? -6.120  2.340   29.291  1.00 36.94 ? 114 GLY A C   1 
ATOM   831  O O   . GLY A 1 114 ? -6.548  3.468   29.606  1.00 36.89 ? 114 GLY A O   1 
ATOM   832  N N   . ARG A 1 115 ? -6.458  1.726   28.160  1.00 37.21 ? 115 ARG A N   1 
ATOM   833  C CA  . ARG A 1 115 ? -7.408  2.301   27.215  1.00 37.61 ? 115 ARG A CA  1 
ATOM   834  C C   . ARG A 1 115 ? -8.745  1.608   27.413  1.00 38.14 ? 115 ARG A C   1 
ATOM   835  O O   . ARG A 1 115 ? -8.831  0.667   28.202  1.00 38.85 ? 115 ARG A O   1 
ATOM   836  C CB  . ARG A 1 115 ? -6.857  2.185   25.791  1.00 37.63 ? 115 ARG A CB  1 
ATOM   837  C CG  . ARG A 1 115 ? -5.574  3.049   25.655  1.00 37.27 ? 115 ARG A CG  1 
ATOM   838  C CD  . ARG A 1 115 ? -5.014  3.126   24.266  1.00 36.71 ? 115 ARG A CD  1 
ATOM   839  N NE  . ARG A 1 115 ? -3.649  3.671   24.291  1.00 35.98 ? 115 ARG A NE  1 
ATOM   840  C CZ  . ARG A 1 115 ? -3.355  4.962   24.471  1.00 36.62 ? 115 ARG A CZ  1 
ATOM   841  N NH1 . ARG A 1 115 ? -4.314  5.853   24.643  1.00 36.14 ? 115 ARG A NH1 1 
ATOM   842  N NH2 . ARG A 1 115 ? -2.095  5.370   24.459  1.00 35.25 ? 115 ARG A NH2 1 
ATOM   843  N N   . THR A 1 116 ? -9.781  2.069   26.720  1.00 38.41 ? 116 THR A N   1 
ATOM   844  C CA  . THR A 1 116 ? -11.144 1.601   26.998  1.00 38.76 ? 116 THR A CA  1 
ATOM   845  C C   . THR A 1 116 ? -11.704 0.729   25.884  1.00 38.96 ? 116 THR A C   1 
ATOM   846  O O   . THR A 1 116 ? -11.760 1.153   24.740  1.00 39.72 ? 116 THR A O   1 
ATOM   847  C CB  . THR A 1 116 ? -12.078 2.792   27.225  1.00 38.96 ? 116 THR A CB  1 
ATOM   848  O OG1 . THR A 1 116 ? -11.584 3.576   28.318  1.00 40.23 ? 116 THR A OG1 1 
ATOM   849  C CG2 . THR A 1 116 ? -13.485 2.345   27.556  1.00 38.85 ? 116 THR A CG2 1 
ATOM   850  N N   . LEU A 1 117 ? -12.129 -0.486  26.222  1.00 38.94 ? 117 LEU A N   1 
ATOM   851  C CA  . LEU A 1 117 ? -12.885 -1.324  25.296  1.00 38.94 ? 117 LEU A CA  1 
ATOM   852  C C   . LEU A 1 117 ? -14.376 -0.986  25.375  1.00 38.96 ? 117 LEU A C   1 
ATOM   853  O O   . LEU A 1 117 ? -14.944 -0.929  26.458  1.00 38.41 ? 117 LEU A O   1 
ATOM   854  C CB  . LEU A 1 117 ? -12.704 -2.797  25.640  1.00 38.94 ? 117 LEU A CB  1 
ATOM   855  C CG  . LEU A 1 117 ? -13.281 -3.797  24.639  1.00 39.20 ? 117 LEU A CG  1 
ATOM   856  C CD1 . LEU A 1 117 ? -12.488 -3.830  23.347  1.00 40.31 ? 117 LEU A CD1 1 
ATOM   857  C CD2 . LEU A 1 117 ? -13.304 -5.175  25.260  1.00 39.12 ? 117 LEU A CD2 1 
ATOM   858  N N   . VAL A 1 118 ? -15.002 -0.797  24.217  1.00 39.11 ? 118 VAL A N   1 
ATOM   859  C CA  . VAL A 1 118 ? -16.397 -0.397  24.138  1.00 39.09 ? 118 VAL A CA  1 
ATOM   860  C C   . VAL A 1 118 ? -17.149 -1.265  23.145  1.00 39.23 ? 118 VAL A C   1 
ATOM   861  O O   . VAL A 1 118 ? -16.715 -1.420  22.012  1.00 39.39 ? 118 VAL A O   1 
ATOM   862  C CB  . VAL A 1 118 ? -16.528 1.060   23.665  1.00 38.84 ? 118 VAL A CB  1 
ATOM   863  C CG1 . VAL A 1 118 ? -17.991 1.465   23.590  1.00 38.57 ? 118 VAL A CG1 1 
ATOM   864  C CG2 . VAL A 1 118 ? -15.781 1.979   24.589  1.00 39.32 ? 118 VAL A CG2 1 
ATOM   865  N N   . VAL A 1 119 ? -18.278 -1.822  23.580  1.00 39.48 ? 119 VAL A N   1 
ATOM   866  C CA  . VAL A 1 119 ? -19.218 -2.466  22.680  1.00 39.31 ? 119 VAL A CA  1 
ATOM   867  C C   . VAL A 1 119 ? -20.321 -1.445  22.413  1.00 39.18 ? 119 VAL A C   1 
ATOM   868  O O   . VAL A 1 119 ? -20.813 -0.794  23.338  1.00 38.94 ? 119 VAL A O   1 
ATOM   869  C CB  . VAL A 1 119 ? -19.770 -3.821  23.229  1.00 39.56 ? 119 VAL A CB  1 
ATOM   870  C CG1 . VAL A 1 119 ? -20.425 -3.679  24.607  1.00 39.80 ? 119 VAL A CG1 1 
ATOM   871  C CG2 . VAL A 1 119 ? -20.735 -4.437  22.240  1.00 39.28 ? 119 VAL A CG2 1 
ATOM   872  N N   . HIS A 1 120 ? -20.687 -1.308  21.143  1.00 39.16 ? 120 HIS A N   1 
ATOM   873  C CA  . HIS A 1 120 ? -21.537 -0.214  20.687  1.00 39.53 ? 120 HIS A CA  1 
ATOM   874  C C   . HIS A 1 120 ? -22.976 -0.623  20.376  1.00 39.68 ? 120 HIS A C   1 
ATOM   875  O O   . HIS A 1 120 ? -23.303 -1.807  20.235  1.00 39.31 ? 120 HIS A O   1 
ATOM   876  C CB  . HIS A 1 120 ? -20.924 0.439   19.446  1.00 39.58 ? 120 HIS A CB  1 
ATOM   877  C CG  . HIS A 1 120 ? -19.741 1.307   19.741  1.00 39.28 ? 120 HIS A CG  1 
ATOM   878  N ND1 . HIS A 1 120 ? -19.845 2.666   19.943  1.00 39.65 ? 120 HIS A ND1 1 
ATOM   879  C CD2 . HIS A 1 120 ? -18.429 1.004   19.875  1.00 39.28 ? 120 HIS A CD2 1 
ATOM   880  C CE1 . HIS A 1 120 ? -18.645 3.162   20.188  1.00 39.89 ? 120 HIS A CE1 1 
ATOM   881  N NE2 . HIS A 1 120 ? -17.769 2.173   20.150  1.00 40.00 ? 120 HIS A NE2 1 
ATOM   882  N N   . GLU A 1 121 ? -23.813 0.403   20.266  1.00 40.09 ? 121 GLU A N   1 
ATOM   883  C CA  . GLU A 1 121 ? -25.250 0.287   20.030  1.00 40.49 ? 121 GLU A CA  1 
ATOM   884  C C   . GLU A 1 121 ? -25.574 -0.418  18.721  1.00 40.63 ? 121 GLU A C   1 
ATOM   885  O O   . GLU A 1 121 ? -26.402 -1.334  18.687  1.00 40.34 ? 121 GLU A O   1 
ATOM   886  C CB  . GLU A 1 121 ? -25.846 1.697   20.007  1.00 40.75 ? 121 GLU A CB  1 
ATOM   887  C CG  . GLU A 1 121 ? -27.351 1.781   19.825  1.00 40.71 ? 121 GLU A CG  1 
ATOM   888  C CD  . GLU A 1 121 ? -27.814 3.191   19.480  1.00 41.57 ? 121 GLU A CD  1 
ATOM   889  O OE1 . GLU A 1 121 ? -26.964 4.043   19.103  1.00 42.19 ? 121 GLU A OE1 1 
ATOM   890  O OE2 . GLU A 1 121 ? -29.039 3.440   19.580  1.00 43.08 ? 121 GLU A OE2 1 
ATOM   891  N N   . LYS A 1 122 ? -24.910 0.019   17.651  1.00 40.80 ? 122 LYS A N   1 
ATOM   892  C CA  . LYS A 1 122 ? -25.187 -0.452  16.301  1.00 40.92 ? 122 LYS A CA  1 
ATOM   893  C C   . LYS A 1 122 ? -23.977 -1.123  15.663  1.00 40.75 ? 122 LYS A C   1 
ATOM   894  O O   . LYS A 1 122 ? -22.847 -1.002  16.146  1.00 40.68 ? 122 LYS A O   1 
ATOM   895  C CB  . LYS A 1 122 ? -25.614 0.726   15.430  1.00 41.10 ? 122 LYS A CB  1 
ATOM   896  C CG  . LYS A 1 122 ? -26.858 1.430   15.915  1.00 42.02 ? 122 LYS A CG  1 
ATOM   897  C CD  . LYS A 1 122 ? -27.077 2.751   15.183  1.00 42.25 ? 122 LYS A CD  1 
ATOM   898  C CE  . LYS A 1 122 ? -28.388 3.406   15.628  1.00 43.92 ? 122 LYS A CE  1 
ATOM   899  N NZ  . LYS A 1 122 ? -28.593 4.770   15.040  1.00 44.78 ? 122 LYS A NZ  1 
ATOM   900  N N   . ALA A 1 123 ? -24.237 -1.823  14.562  1.00 40.58 ? 123 ALA A N   1 
ATOM   901  C CA  . ALA A 1 123 ? -23.197 -2.447  13.762  1.00 40.55 ? 123 ALA A CA  1 
ATOM   902  C C   . ALA A 1 123 ? -22.242 -1.412  13.174  1.00 40.46 ? 123 ALA A C   1 
ATOM   903  O O   . ALA A 1 123 ? -22.660 -0.349  12.691  1.00 40.41 ? 123 ALA A O   1 
ATOM   904  C CB  . ALA A 1 123 ? -23.807 -3.266  12.647  1.00 40.77 ? 123 ALA A CB  1 
ATOM   905  N N   . ASP A 1 124 ? -20.953 -1.739  13.244  1.00 40.22 ? 124 ASP A N   1 
ATOM   906  C CA  . ASP A 1 124 ? -19.888 -0.979  12.583  1.00 40.03 ? 124 ASP A CA  1 
ATOM   907  C C   . ASP A 1 124 ? -19.970 -1.291  11.086  1.00 39.67 ? 124 ASP A C   1 
ATOM   908  O O   . ASP A 1 124 ? -19.869 -2.452  10.676  1.00 39.49 ? 124 ASP A O   1 
ATOM   909  C CB  . ASP A 1 124 ? -18.536 -1.415  13.169  1.00 40.00 ? 124 ASP A CB  1 
ATOM   910  C CG  . ASP A 1 124 ? -17.347 -0.671  12.581  1.00 40.15 ? 124 ASP A CG  1 
ATOM   911  O OD1 . ASP A 1 124 ? -17.487 0.056   11.582  1.00 38.65 ? 124 ASP A OD1 1 
ATOM   912  O OD2 . ASP A 1 124 ? -16.239 -0.841  13.125  1.00 40.63 ? 124 ASP A OD2 1 
ATOM   913  N N   . ASP A 1 125 ? -20.178 -0.252  10.279  1.00 39.08 ? 125 ASP A N   1 
ATOM   914  C CA  . ASP A 1 125 ? -20.245 -0.399  8.823   1.00 38.78 ? 125 ASP A CA  1 
ATOM   915  C C   . ASP A 1 125 ? -18.849 -0.552  8.162   1.00 38.41 ? 125 ASP A C   1 
ATOM   916  O O   . ASP A 1 125 ? -18.742 -0.619  6.938   1.00 37.81 ? 125 ASP A O   1 
ATOM   917  C CB  . ASP A 1 125 ? -21.045 0.765   8.205   1.00 38.48 ? 125 ASP A CB  1 
ATOM   918  C CG  . ASP A 1 125 ? -20.304 2.089   8.253   1.00 38.71 ? 125 ASP A CG  1 
ATOM   919  O OD1 . ASP A 1 125 ? -19.054 2.073   8.250   1.00 38.34 ? 125 ASP A OD1 1 
ATOM   920  O OD2 . ASP A 1 125 ? -20.973 3.153   8.273   1.00 38.44 ? 125 ASP A OD2 1 
ATOM   921  N N   . LEU A 1 126 ? -17.802 -0.589  8.987   1.00 38.31 ? 126 LEU A N   1 
ATOM   922  C CA  . LEU A 1 126 ? -16.421 -0.857  8.570   1.00 38.44 ? 126 LEU A CA  1 
ATOM   923  C C   . LEU A 1 126 ? -15.858 0.178   7.589   1.00 38.58 ? 126 LEU A C   1 
ATOM   924  O O   . LEU A 1 126 ? -14.961 -0.138  6.799   1.00 38.76 ? 126 LEU A O   1 
ATOM   925  C CB  . LEU A 1 126 ? -16.290 -2.282  7.995   1.00 38.69 ? 126 LEU A CB  1 
ATOM   926  C CG  . LEU A 1 126 ? -16.922 -3.432  8.794   1.00 38.48 ? 126 LEU A CG  1 
ATOM   927  C CD1 . LEU A 1 126 ? -16.775 -4.774  8.070   1.00 38.33 ? 126 LEU A CD1 1 
ATOM   928  C CD2 . LEU A 1 126 ? -16.335 -3.531  10.196  1.00 39.34 ? 126 LEU A CD2 1 
ATOM   929  N N   . GLY A 1 127 ? -16.373 1.410   7.654   1.00 38.41 ? 127 GLY A N   1 
ATOM   930  C CA  . GLY A 1 127 ? -15.931 2.496   6.771   1.00 38.33 ? 127 GLY A CA  1 
ATOM   931  C C   . GLY A 1 127 ? -16.547 2.483   5.374   1.00 38.22 ? 127 GLY A C   1 
ATOM   932  O O   . GLY A 1 127 ? -16.183 3.298   4.522   1.00 37.97 ? 127 GLY A O   1 
ATOM   933  N N   . LYS A 1 128 ? -17.502 1.583   5.155   1.00 38.20 ? 128 LYS A N   1 
ATOM   934  C CA  . LYS A 1 128 ? -18.131 1.384   3.847   1.00 38.23 ? 128 LYS A CA  1 
ATOM   935  C C   . LYS A 1 128 ? -19.619 1.731   3.866   1.00 38.05 ? 128 LYS A C   1 
ATOM   936  O O   . LYS A 1 128 ? -20.411 1.107   3.157   1.00 37.81 ? 128 LYS A O   1 
ATOM   937  C CB  . LYS A 1 128 ? -17.959 -0.077  3.414   1.00 38.60 ? 128 LYS A CB  1 
ATOM   938  C CG  . LYS A 1 128 ? -16.813 -0.323  2.449   1.00 40.27 ? 128 LYS A CG  1 
ATOM   939  C CD  . LYS A 1 128 ? -15.475 -0.421  3.136   1.00 41.39 ? 128 LYS A CD  1 
ATOM   940  C CE  . LYS A 1 128 ? -14.366 -0.704  2.117   1.00 41.07 ? 128 LYS A CE  1 
ATOM   941  N NZ  . LYS A 1 128 ? -13.077 -0.071  2.506   1.00 41.64 ? 128 LYS A NZ  1 
ATOM   942  N N   . GLY A 1 129 ? -19.990 2.729   4.670   1.00 37.59 ? 129 GLY A N   1 
ATOM   943  C CA  . GLY A 1 129 ? -21.387 3.157   4.812   1.00 37.29 ? 129 GLY A CA  1 
ATOM   944  C C   . GLY A 1 129 ? -21.777 4.311   3.905   1.00 36.86 ? 129 GLY A C   1 
ATOM   945  O O   . GLY A 1 129 ? -22.962 4.630   3.775   1.00 36.41 ? 129 GLY A O   1 
ATOM   946  N N   . GLY A 1 130 ? -20.780 4.962   3.305   1.00 36.84 ? 130 GLY A N   1 
ATOM   947  C CA  . GLY A 1 130 ? -21.016 5.942   2.242   1.00 36.91 ? 130 GLY A CA  1 
ATOM   948  C C   . GLY A 1 130 ? -21.365 7.347   2.689   1.00 36.81 ? 130 GLY A C   1 
ATOM   949  O O   . GLY A 1 130 ? -22.021 8.085   1.954   1.00 36.02 ? 130 GLY A O   1 
ATOM   950  N N   . ASN A 1 131 ? -20.933 7.704   3.899   1.00 37.23 ? 131 ASN A N   1 
ATOM   951  C CA  . ASN A 1 131 ? -21.042 9.072   4.416   1.00 37.40 ? 131 ASN A CA  1 
ATOM   952  C C   . ASN A 1 131 ? -19.802 9.414   5.239   1.00 37.90 ? 131 ASN A C   1 
ATOM   953  O O   . ASN A 1 131 ? -18.958 8.549   5.489   1.00 37.82 ? 131 ASN A O   1 
ATOM   954  C CB  . ASN A 1 131 ? -22.345 9.286   5.223   1.00 37.25 ? 131 ASN A CB  1 
ATOM   955  C CG  . ASN A 1 131 ? -22.577 8.226   6.296   1.00 36.45 ? 131 ASN A CG  1 
ATOM   956  O OD1 . ASN A 1 131 ? -21.645 7.750   6.930   1.00 35.10 ? 131 ASN A OD1 1 
ATOM   957  N ND2 . ASN A 1 131 ? -23.837 7.885   6.520   1.00 36.29 ? 131 ASN A ND2 1 
ATOM   958  N N   . GLU A 1 132 ? -19.686 10.677  5.637   1.00 38.49 ? 132 GLU A N   1 
ATOM   959  C CA  . GLU A 1 132 ? -18.517 11.160  6.372   1.00 38.92 ? 132 GLU A CA  1 
ATOM   960  C C   . GLU A 1 132 ? -18.327 10.445  7.694   1.00 39.07 ? 132 GLU A C   1 
ATOM   961  O O   . GLU A 1 132 ? -17.202 10.120  8.066   1.00 39.34 ? 132 GLU A O   1 
ATOM   962  C CB  . GLU A 1 132 ? -18.621 12.670  6.607   1.00 39.08 ? 132 GLU A CB  1 
ATOM   963  C CG  . GLU A 1 132 ? -18.350 13.482  5.354   1.00 39.72 ? 132 GLU A CG  1 
ATOM   964  C CD  . GLU A 1 132 ? -18.998 14.865  5.371   1.00 40.30 ? 132 GLU A CD  1 
ATOM   965  O OE1 . GLU A 1 132 ? -19.558 15.261  6.421   1.00 43.03 ? 132 GLU A OE1 1 
ATOM   966  O OE2 . GLU A 1 132 ? -18.950 15.555  4.324   1.00 40.77 ? 132 GLU A OE2 1 
ATOM   967  N N   . GLU A 1 133 ? -19.427 10.184  8.392   1.00 39.44 ? 133 GLU A N   1 
ATOM   968  C CA  . GLU A 1 133 ? -19.373 9.537   9.705   1.00 39.55 ? 133 GLU A CA  1 
ATOM   969  C C   . GLU A 1 133 ? -18.858 8.095   9.629   1.00 39.72 ? 133 GLU A C   1 
ATOM   970  O O   . GLU A 1 133 ? -18.295 7.569   10.597  1.00 39.64 ? 133 GLU A O   1 
ATOM   971  C CB  . GLU A 1 133 ? -20.760 9.577   10.360  1.00 39.89 ? 133 GLU A CB  1 
ATOM   972  C CG  . GLU A 1 133 ? -20.784 9.237   11.839  1.00 39.98 ? 133 GLU A CG  1 
ATOM   973  C CD  . GLU A 1 133 ? -19.895 10.144  12.666  1.00 40.91 ? 133 GLU A CD  1 
ATOM   974  O OE1 . GLU A 1 133 ? -19.989 11.392  12.525  1.00 41.19 ? 133 GLU A OE1 1 
ATOM   975  O OE2 . GLU A 1 133 ? -19.097 9.600   13.455  1.00 41.78 ? 133 GLU A OE2 1 
ATOM   976  N N   . SER A 1 134 ? -19.047 7.458   8.480   1.00 39.77 ? 134 SER A N   1 
ATOM   977  C CA  . SER A 1 134 ? -18.567 6.096   8.276   1.00 39.91 ? 134 SER A CA  1 
ATOM   978  C C   . SER A 1 134 ? -17.048 6.005   8.411   1.00 40.03 ? 134 SER A C   1 
ATOM   979  O O   . SER A 1 134 ? -16.535 5.059   8.998   1.00 40.11 ? 134 SER A O   1 
ATOM   980  C CB  . SER A 1 134 ? -19.004 5.569   6.906   1.00 39.92 ? 134 SER A CB  1 
ATOM   981  O OG  . SER A 1 134 ? -18.641 4.204   6.745   1.00 39.41 ? 134 SER A OG  1 
ATOM   982  N N   . THR A 1 135 ? -16.336 6.997   7.891   1.00 40.43 ? 135 THR A N   1 
ATOM   983  C CA  . THR A 1 135 ? -14.873 7.003   7.938   1.00 40.81 ? 135 THR A CA  1 
ATOM   984  C C   . THR A 1 135 ? -14.301 7.504   9.274   1.00 40.97 ? 135 THR A C   1 
ATOM   985  O O   . THR A 1 135 ? -13.078 7.598   9.420   1.00 40.95 ? 135 THR A O   1 
ATOM   986  C CB  . THR A 1 135 ? -14.267 7.862   6.806   1.00 40.99 ? 135 THR A CB  1 
ATOM   987  O OG1 . THR A 1 135 ? -14.578 9.245   7.028   1.00 41.72 ? 135 THR A OG1 1 
ATOM   988  C CG2 . THR A 1 135 ? -14.788 7.429   5.443   1.00 41.22 ? 135 THR A CG2 1 
ATOM   989  N N   . LYS A 1 136 ? -15.180 7.821   10.229  1.00 41.09 ? 136 LYS A N   1 
ATOM   990  C CA  . LYS A 1 136 ? -14.792 8.255   11.574  1.00 41.38 ? 136 LYS A CA  1 
ATOM   991  C C   . LYS A 1 136 ? -15.056 7.198   12.642  1.00 41.32 ? 136 LYS A C   1 
ATOM   992  O O   . LYS A 1 136 ? -14.196 6.938   13.479  1.00 41.59 ? 136 LYS A O   1 
ATOM   993  C CB  . LYS A 1 136 ? -15.569 9.509   11.965  1.00 41.56 ? 136 LYS A CB  1 
ATOM   994  C CG  . LYS A 1 136 ? -15.336 10.691  11.066  1.00 42.20 ? 136 LYS A CG  1 
ATOM   995  C CD  . LYS A 1 136 ? -16.182 11.870  11.522  1.00 42.12 ? 136 LYS A CD  1 
ATOM   996  C CE  . LYS A 1 136 ? -15.905 13.114  10.689  1.00 42.79 ? 136 LYS A CE  1 
ATOM   997  N NZ  . LYS A 1 136 ? -17.018 14.101  10.782  1.00 42.85 ? 136 LYS A NZ  1 
ATOM   998  N N   . THR A 1 137 ? -16.262 6.628   12.629  1.00 41.24 ? 137 THR A N   1 
ATOM   999  C CA  . THR A 1 137 ? -16.723 5.722   13.682  1.00 41.13 ? 137 THR A CA  1 
ATOM   1000 C C   . THR A 1 137 ? -17.414 4.444   13.197  1.00 41.00 ? 137 THR A C   1 
ATOM   1001 O O   . THR A 1 137 ? -17.747 3.563   14.006  1.00 40.90 ? 137 THR A O   1 
ATOM   1002 C CB  . THR A 1 137 ? -17.717 6.454   14.598  1.00 41.69 ? 137 THR A CB  1 
ATOM   1003 O OG1 . THR A 1 137 ? -18.767 7.044   13.807  1.00 42.48 ? 137 THR A OG1 1 
ATOM   1004 C CG2 . THR A 1 137 ? -17.010 7.557   15.374  1.00 42.32 ? 137 THR A CG2 1 
ATOM   1005 N N   . GLY A 1 138 ? -17.647 4.332   11.896  1.00 40.59 ? 138 GLY A N   1 
ATOM   1006 C CA  . GLY A 1 138 ? -18.362 3.183   11.358  1.00 40.27 ? 138 GLY A CA  1 
ATOM   1007 C C   . GLY A 1 138 ? -19.858 3.242   11.615  1.00 39.98 ? 138 GLY A C   1 
ATOM   1008 O O   . GLY A 1 138 ? -20.562 2.258   11.396  1.00 39.90 ? 138 GLY A O   1 
ATOM   1009 N N   . ASN A 1 139 ? -20.341 4.403   12.055  1.00 39.74 ? 139 ASN A N   1 
ATOM   1010 C CA  . ASN A 1 139 ? -21.744 4.599   12.437  1.00 39.72 ? 139 ASN A CA  1 
ATOM   1011 C C   . ASN A 1 139 ? -22.262 3.588   13.484  1.00 39.64 ? 139 ASN A C   1 
ATOM   1012 O O   . ASN A 1 139 ? -23.445 3.242   13.505  1.00 39.22 ? 139 ASN A O   1 
ATOM   1013 C CB  . ASN A 1 139 ? -22.628 4.627   11.183  1.00 39.63 ? 139 ASN A CB  1 
ATOM   1014 C CG  . ASN A 1 139 ? -22.411 5.885   10.346  1.00 39.33 ? 139 ASN A CG  1 
ATOM   1015 O OD1 . ASN A 1 139 ? -22.874 6.962   10.705  1.00 38.65 ? 139 ASN A OD1 1 
ATOM   1016 N ND2 . ASN A 1 139 ? -21.713 5.745   9.223   1.00 38.98 ? 139 ASN A ND2 1 
ATOM   1017 N N   . ALA A 1 140 ? -21.360 3.157   14.367  1.00 39.57 ? 140 ALA A N   1 
ATOM   1018 C CA  . ALA A 1 140 ? -21.659 2.179   15.414  1.00 39.62 ? 140 ALA A CA  1 
ATOM   1019 C C   . ALA A 1 140 ? -22.541 2.746   16.529  1.00 39.68 ? 140 ALA A C   1 
ATOM   1020 O O   . ALA A 1 140 ? -23.096 1.999   17.329  1.00 39.62 ? 140 ALA A O   1 
ATOM   1021 C CB  . ALA A 1 140 ? -20.375 1.644   15.999  1.00 39.68 ? 140 ALA A CB  1 
ATOM   1022 N N   . GLY A 1 141 ? -22.662 4.067   16.588  1.00 39.62 ? 141 GLY A N   1 
ATOM   1023 C CA  . GLY A 1 141 ? -23.573 4.695   17.520  1.00 39.77 ? 141 GLY A CA  1 
ATOM   1024 C C   . GLY A 1 141 ? -23.039 4.670   18.931  1.00 39.81 ? 141 GLY A C   1 
ATOM   1025 O O   . GLY A 1 141 ? -21.828 4.636   19.143  1.00 39.74 ? 141 GLY A O   1 
ATOM   1026 N N   . SER A 1 142 ? -23.952 4.653   19.897  1.00 39.89 ? 142 SER A N   1 
ATOM   1027 C CA  . SER A 1 142 ? -23.599 4.920   21.287  1.00 39.85 ? 142 SER A CA  1 
ATOM   1028 C C   . SER A 1 142 ? -22.886 3.765   21.968  1.00 39.78 ? 142 SER A C   1 
ATOM   1029 O O   . SER A 1 142 ? -22.971 2.610   21.554  1.00 39.80 ? 142 SER A O   1 
ATOM   1030 C CB  . SER A 1 142 ? -24.838 5.322   22.088  1.00 39.86 ? 142 SER A CB  1 
ATOM   1031 O OG  . SER A 1 142 ? -25.816 4.305   22.047  1.00 40.36 ? 142 SER A OG  1 
ATOM   1032 N N   . ARG A 1 143 ? -22.156 4.118   23.014  1.00 39.95 ? 143 ARG A N   1 
ATOM   1033 C CA  . ARG A 1 143 ? -21.519 3.159   23.912  1.00 39.90 ? 143 ARG A CA  1 
ATOM   1034 C C   . ARG A 1 143 ? -22.570 2.496   24.799  1.00 39.59 ? 143 ARG A C   1 
ATOM   1035 O O   . ARG A 1 143 ? -23.275 3.176   25.545  1.00 39.51 ? 143 ARG A O   1 
ATOM   1036 C CB  . ARG A 1 143 ? -20.484 3.902   24.764  1.00 40.16 ? 143 ARG A CB  1 
ATOM   1037 C CG  . ARG A 1 143 ? -20.223 3.362   26.150  1.00 40.37 ? 143 ARG A CG  1 
ATOM   1038 C CD  . ARG A 1 143 ? -19.302 4.315   26.878  1.00 40.87 ? 143 ARG A CD  1 
ATOM   1039 N NE  . ARG A 1 143 ? -19.014 3.867   28.229  1.00 41.33 ? 143 ARG A NE  1 
ATOM   1040 C CZ  . ARG A 1 143 ? -18.266 4.542   29.095  1.00 42.42 ? 143 ARG A CZ  1 
ATOM   1041 N NH1 . ARG A 1 143 ? -17.724 5.707   28.754  1.00 42.98 ? 143 ARG A NH1 1 
ATOM   1042 N NH2 . ARG A 1 143 ? -18.062 4.048   30.313  1.00 42.74 ? 143 ARG A NH2 1 
ATOM   1043 N N   . LEU A 1 144 ? -22.674 1.172   24.707  1.00 39.45 ? 144 LEU A N   1 
ATOM   1044 C CA  . LEU A 1 144 ? -23.607 0.415   25.545  1.00 39.13 ? 144 LEU A CA  1 
ATOM   1045 C C   . LEU A 1 144 ? -22.954 -0.050  26.841  1.00 38.87 ? 144 LEU A C   1 
ATOM   1046 O O   . LEU A 1 144 ? -23.603 -0.133  27.880  1.00 38.79 ? 144 LEU A O   1 
ATOM   1047 C CB  . LEU A 1 144 ? -24.157 -0.788  24.781  1.00 39.05 ? 144 LEU A CB  1 
ATOM   1048 C CG  . LEU A 1 144 ? -25.074 -0.457  23.598  1.00 38.81 ? 144 LEU A CG  1 
ATOM   1049 C CD1 . LEU A 1 144 ? -25.689 -1.757  23.088  1.00 39.00 ? 144 LEU A CD1 1 
ATOM   1050 C CD2 . LEU A 1 144 ? -26.164 0.560   23.949  1.00 37.74 ? 144 LEU A CD2 1 
ATOM   1051 N N   . ALA A 1 145 ? -21.668 -0.358  26.760  1.00 38.61 ? 145 ALA A N   1 
ATOM   1052 C CA  . ALA A 1 145 ? -20.902 -0.818  27.900  1.00 38.32 ? 145 ALA A CA  1 
ATOM   1053 C C   . ALA A 1 145 ? -19.433 -0.583  27.592  1.00 38.02 ? 145 ALA A C   1 
ATOM   1054 O O   . ALA A 1 145 ? -19.032 -0.579  26.429  1.00 37.81 ? 145 ALA A O   1 
ATOM   1055 C CB  . ALA A 1 145 ? -21.158 -2.286  28.149  1.00 38.18 ? 145 ALA A CB  1 
ATOM   1056 N N   . ALA A 1 146 ? -18.640 -0.384  28.638  1.00 37.84 ? 146 ALA A N   1 
ATOM   1057 C CA  . ALA A 1 146 ? -17.209 -0.166  28.484  1.00 37.80 ? 146 ALA A CA  1 
ATOM   1058 C C   . ALA A 1 146 ? -16.431 -0.643  29.698  1.00 37.84 ? 146 ALA A C   1 
ATOM   1059 O O   . ALA A 1 146 ? -16.981 -0.814  30.789  1.00 37.60 ? 146 ALA A O   1 
ATOM   1060 C CB  . ALA A 1 146 ? -16.930 1.299   28.249  1.00 37.37 ? 146 ALA A CB  1 
ATOM   1061 N N   . GLY A 1 147 ? -15.139 -0.851  29.491  1.00 37.85 ? 147 GLY A N   1 
ATOM   1062 C CA  . GLY A 1 147 ? -14.232 -1.181  30.570  1.00 37.86 ? 147 GLY A CA  1 
ATOM   1063 C C   . GLY A 1 147 ? -12.840 -0.724  30.211  1.00 37.97 ? 147 GLY A C   1 
ATOM   1064 O O   . GLY A 1 147 ? -12.441 -0.806  29.055  1.00 38.17 ? 147 GLY A O   1 
ATOM   1065 N N   . VAL A 1 148 ? -12.111 -0.226  31.199  1.00 37.85 ? 148 VAL A N   1 
ATOM   1066 C CA  . VAL A 1 148 ? -10.689 0.057   31.039  1.00 37.97 ? 148 VAL A CA  1 
ATOM   1067 C C   . VAL A 1 148 ? -9.965  -1.287  30.932  1.00 37.99 ? 148 VAL A C   1 
ATOM   1068 O O   . VAL A 1 148 ? -10.282 -2.221  31.666  1.00 37.36 ? 148 VAL A O   1 
ATOM   1069 C CB  . VAL A 1 148 ? -10.154 0.902   32.217  1.00 38.19 ? 148 VAL A CB  1 
ATOM   1070 C CG1 . VAL A 1 148 ? -8.640  1.107   32.132  1.00 38.55 ? 148 VAL A CG1 1 
ATOM   1071 C CG2 . VAL A 1 148 ? -10.865 2.261   32.251  1.00 37.89 ? 148 VAL A CG2 1 
ATOM   1072 N N   . ILE A 1 149 ? -9.025  -1.383  29.992  1.00 37.94 ? 149 ILE A N   1 
ATOM   1073 C CA  . ILE A 1 149 ? -8.257  -2.613  29.779  1.00 37.99 ? 149 ILE A CA  1 
ATOM   1074 C C   . ILE A 1 149 ? -7.138  -2.664  30.824  1.00 38.12 ? 149 ILE A C   1 
ATOM   1075 O O   . ILE A 1 149 ? -6.231  -1.821  30.836  1.00 37.58 ? 149 ILE A O   1 
ATOM   1076 C CB  . ILE A 1 149 ? -7.691  -2.685  28.334  1.00 37.92 ? 149 ILE A CB  1 
ATOM   1077 C CG1 . ILE A 1 149 ? -8.844  -2.649  27.321  1.00 37.73 ? 149 ILE A CG1 1 
ATOM   1078 C CG2 . ILE A 1 149 ? -6.848  -3.945  28.138  1.00 38.34 ? 149 ILE A CG2 1 
ATOM   1079 C CD1 . ILE A 1 149 ? -8.434  -2.390  25.882  1.00 37.43 ? 149 ILE A CD1 1 
ATOM   1080 N N   . GLY A 1 150 ? -7.237  -3.636  31.724  1.00 38.07 ? 150 GLY A N   1 
ATOM   1081 C CA  . GLY A 1 150 ? -6.306  -3.765  32.838  1.00 38.45 ? 150 GLY A CA  1 
ATOM   1082 C C   . GLY A 1 150 ? -5.517  -5.053  32.787  1.00 38.51 ? 150 GLY A C   1 
ATOM   1083 O O   . GLY A 1 150 ? -5.895  -5.996  32.097  1.00 38.19 ? 150 GLY A O   1 
ATOM   1084 N N   . ILE A 1 151 ? -4.410  -5.077  33.521  1.00 38.84 ? 151 ILE A N   1 
ATOM   1085 C CA  . ILE A 1 151 ? -3.527  -6.241  33.564  1.00 39.14 ? 151 ILE A CA  1 
ATOM   1086 C C   . ILE A 1 151 ? -4.231  -7.357  34.318  1.00 39.35 ? 151 ILE A C   1 
ATOM   1087 O O   . ILE A 1 151 ? -4.911  -7.097  35.305  1.00 39.46 ? 151 ILE A O   1 
ATOM   1088 C CB  . ILE A 1 151 ? -2.166  -5.863  34.198  1.00 39.19 ? 151 ILE A CB  1 
ATOM   1089 C CG1 . ILE A 1 151 ? -1.448  -4.893  33.259  1.00 38.46 ? 151 ILE A CG1 1 
ATOM   1090 C CG2 . ILE A 1 151 ? -1.313  -7.099  34.461  1.00 38.85 ? 151 ILE A CG2 1 
ATOM   1091 C CD1 . ILE A 1 151 ? -0.306  -4.185  33.872  1.00 39.59 ? 151 ILE A CD1 1 
ATOM   1092 N N   . ALA A 1 152 ? -4.068  -8.595  33.846  1.00 39.59 ? 152 ALA A N   1 
ATOM   1093 C CA  . ALA A 1 152 ? -4.887  -9.717  34.284  1.00 39.77 ? 152 ALA A CA  1 
ATOM   1094 C C   . ALA A 1 152 ? -4.058  -10.825 34.939  1.00 40.18 ? 152 ALA A C   1 
ATOM   1095 O O   . ALA A 1 152 ? -2.884  -11.017 34.599  1.00 39.99 ? 152 ALA A O   1 
ATOM   1096 C CB  . ALA A 1 152 ? -5.648  -10.284 33.093  1.00 39.62 ? 152 ALA A CB  1 
ATOM   1097 N N   . GLN A 1 153 ? -4.686  -11.541 35.875  1.00 40.39 ? 153 GLN A N   1 
ATOM   1098 C CA  . GLN A 1 153 ? -4.033  -12.628 36.617  1.00 40.85 ? 153 GLN A CA  1 
ATOM   1099 C C   . GLN A 1 153 ? -4.036  -13.912 35.806  1.00 41.43 ? 153 GLN A C   1 
ATOM   1100 O O   . GLN A 1 153 ? -4.875  -14.078 34.908  1.00 41.83 ? 153 GLN A O   1 
ATOM   1101 C CB  . GLN A 1 153 ? -4.747  -12.881 37.953  1.00 40.79 ? 153 GLN A CB  1 
ATOM   1102 C CG  . GLN A 1 153 ? -4.105  -13.988 38.797  1.00 40.85 ? 153 GLN A CG  1 
ATOM   1103 C CD  . GLN A 1 153 ? -4.554  -13.983 40.244  1.00 41.53 ? 153 GLN A CD  1 
ATOM   1104 O OE1 . GLN A 1 153 ? -3.862  -14.500 41.121  1.00 42.47 ? 153 GLN A OE1 1 
ATOM   1105 N NE2 . GLN A 1 153 ? -5.722  -13.413 40.500  1.00 43.39 ? 153 GLN A NE2 1 
ATOM   1106 O OXT . GLN A 1 153 ? -3.230  -14.822 36.058  1.00 41.95 ? 153 GLN A OXT 1 
ATOM   1107 N N   . ALA B 1 1   ? 4.328   15.178  29.646  1.00 44.87 ? 1   ALA B N   1 
ATOM   1108 C CA  . ALA B 1 1   ? 3.792   14.597  30.915  1.00 44.49 ? 1   ALA B CA  1 
ATOM   1109 C C   . ALA B 1 1   ? 2.886   13.390  30.633  1.00 44.32 ? 1   ALA B C   1 
ATOM   1110 O O   . ALA B 1 1   ? 2.154   13.371  29.638  1.00 44.68 ? 1   ALA B O   1 
ATOM   1111 C CB  . ALA B 1 1   ? 3.034   15.668  31.714  1.00 44.71 ? 1   ALA B CB  1 
ATOM   1112 N N   . THR B 1 2   ? 2.959   12.387  31.505  1.00 43.63 ? 2   THR B N   1 
ATOM   1113 C CA  . THR B 1 2   ? 2.042   11.252  31.486  1.00 43.00 ? 2   THR B CA  1 
ATOM   1114 C C   . THR B 1 2   ? 0.903   11.560  32.450  1.00 42.29 ? 2   THR B C   1 
ATOM   1115 O O   . THR B 1 2   ? 1.144   12.008  33.570  1.00 42.20 ? 2   THR B O   1 
ATOM   1116 C CB  . THR B 1 2   ? 2.757   9.961   31.944  1.00 43.18 ? 2   THR B CB  1 
ATOM   1117 O OG1 . THR B 1 2   ? 4.104   9.977   31.464  1.00 44.68 ? 2   THR B OG1 1 
ATOM   1118 C CG2 . THR B 1 2   ? 2.063   8.718   31.418  1.00 43.55 ? 2   THR B CG2 1 
ATOM   1119 N N   . LYS B 1 3   ? -0.332  11.331  32.006  1.00 41.49 ? 3   LYS B N   1 
ATOM   1120 C CA  . LYS B 1 3   ? -1.522  11.484  32.844  1.00 41.06 ? 3   LYS B CA  1 
ATOM   1121 C C   . LYS B 1 3   ? -2.299  10.174  32.910  1.00 39.90 ? 3   LYS B C   1 
ATOM   1122 O O   . LYS B 1 3   ? -2.400  9.454   31.920  1.00 38.58 ? 3   LYS B O   1 
ATOM   1123 C CB  . LYS B 1 3   ? -2.438  12.569  32.292  1.00 41.19 ? 3   LYS B CB  1 
ATOM   1124 C CG  . LYS B 1 3   ? -1.794  13.943  32.240  1.00 42.41 ? 3   LYS B CG  1 
ATOM   1125 C CD  . LYS B 1 3   ? -2.693  14.977  31.565  1.00 42.72 ? 3   LYS B CD  1 
ATOM   1126 C CE  . LYS B 1 3   ? -1.869  16.129  30.965  1.00 43.67 ? 3   LYS B CE  1 
ATOM   1127 N NZ  . LYS B 1 3   ? -1.103  15.740  29.725  1.00 44.65 ? 3   LYS B NZ  1 
ATOM   1128 N N   . ALA B 1 4   ? -2.837  9.884   34.089  1.00 39.20 ? 4   ALA B N   1 
ATOM   1129 C CA  . ALA B 1 4   ? -3.732  8.754   34.284  1.00 39.10 ? 4   ALA B CA  1 
ATOM   1130 C C   . ALA B 1 4   ? -4.866  9.162   35.208  1.00 38.62 ? 4   ALA B C   1 
ATOM   1131 O O   . ALA B 1 4   ? -4.804  10.195  35.871  1.00 37.96 ? 4   ALA B O   1 
ATOM   1132 C CB  . ALA B 1 4   ? -2.980  7.545   34.847  1.00 38.62 ? 4   ALA B CB  1 
ATOM   1133 N N   . VAL B 1 5   ? -5.914  8.346   35.220  1.00 38.48 ? 5   VAL B N   1 
ATOM   1134 C CA  . VAL B 1 5   ? -7.079  8.597   36.042  1.00 38.50 ? 5   VAL B CA  1 
ATOM   1135 C C   . VAL B 1 5   ? -7.735  7.270   36.407  1.00 38.21 ? 5   VAL B C   1 
ATOM   1136 O O   . VAL B 1 5   ? -7.767  6.347   35.600  1.00 37.70 ? 5   VAL B O   1 
ATOM   1137 C CB  . VAL B 1 5   ? -8.083  9.551   35.336  1.00 38.64 ? 5   VAL B CB  1 
ATOM   1138 C CG1 . VAL B 1 5   ? -8.543  8.985   33.997  1.00 38.66 ? 5   VAL B CG1 1 
ATOM   1139 C CG2 . VAL B 1 5   ? -9.281  9.852   36.243  1.00 38.59 ? 5   VAL B CG2 1 
ATOM   1140 N N   . ALA B 1 6   ? -8.207  7.188   37.645  1.00 38.23 ? 6   ALA B N   1 
ATOM   1141 C CA  . ALA B 1 6   ? -8.969  6.055   38.136  1.00 38.70 ? 6   ALA B CA  1 
ATOM   1142 C C   . ALA B 1 6   ? -10.312 6.555   38.650  1.00 38.89 ? 6   ALA B C   1 
ATOM   1143 O O   . ALA B 1 6   ? -10.374 7.506   39.430  1.00 38.52 ? 6   ALA B O   1 
ATOM   1144 C CB  . ALA B 1 6   ? -8.220  5.351   39.231  1.00 39.01 ? 6   ALA B CB  1 
ATOM   1145 N N   . VAL B 1 7   ? -11.389 5.921   38.189  1.00 39.14 ? 7   VAL B N   1 
ATOM   1146 C CA  . VAL B 1 7   ? -12.729 6.225   38.677  1.00 39.16 ? 7   VAL B CA  1 
ATOM   1147 C C   . VAL B 1 7   ? -13.062 5.154   39.705  1.00 39.21 ? 7   VAL B C   1 
ATOM   1148 O O   . VAL B 1 7   ? -13.225 3.986   39.360  1.00 38.52 ? 7   VAL B O   1 
ATOM   1149 C CB  . VAL B 1 7   ? -13.745 6.253   37.537  1.00 39.21 ? 7   VAL B CB  1 
ATOM   1150 C CG1 . VAL B 1 7   ? -15.151 6.413   38.066  1.00 39.77 ? 7   VAL B CG1 1 
ATOM   1151 C CG2 . VAL B 1 7   ? -13.420 7.389   36.593  1.00 39.17 ? 7   VAL B CG2 1 
ATOM   1152 N N   . LEU B 1 8   ? -13.110 5.556   40.974  1.00 39.29 ? 8   LEU B N   1 
ATOM   1153 C CA  . LEU B 1 8   ? -13.352 4.624   42.069  1.00 39.69 ? 8   LEU B CA  1 
ATOM   1154 C C   . LEU B 1 8   ? -14.846 4.371   42.191  1.00 40.07 ? 8   LEU B C   1 
ATOM   1155 O O   . LEU B 1 8   ? -15.621 5.281   42.461  1.00 39.70 ? 8   LEU B O   1 
ATOM   1156 C CB  . LEU B 1 8   ? -12.778 5.157   43.379  1.00 39.38 ? 8   LEU B CB  1 
ATOM   1157 C CG  . LEU B 1 8   ? -11.252 5.361   43.440  1.00 38.91 ? 8   LEU B CG  1 
ATOM   1158 C CD1 . LEU B 1 8   ? -10.815 5.715   44.856  1.00 39.08 ? 8   LEU B CD1 1 
ATOM   1159 C CD2 . LEU B 1 8   ? -10.489 4.127   42.981  1.00 39.88 ? 8   LEU B CD2 1 
ATOM   1160 N N   . LYS B 1 9   ? -15.235 3.123   41.960  1.00 40.98 ? 9   LYS B N   1 
ATOM   1161 C CA  . LYS B 1 9   ? -16.633 2.710   41.999  1.00 41.64 ? 9   LYS B CA  1 
ATOM   1162 C C   . LYS B 1 9   ? -16.828 1.535   42.948  1.00 41.77 ? 9   LYS B C   1 
ATOM   1163 O O   . LYS B 1 9   ? -15.982 0.643   43.042  1.00 41.10 ? 9   LYS B O   1 
ATOM   1164 C CB  . LYS B 1 9   ? -17.107 2.334   40.594  1.00 41.97 ? 9   LYS B CB  1 
ATOM   1165 C CG  . LYS B 1 9   ? -17.511 3.543   39.750  1.00 43.04 ? 9   LYS B CG  1 
ATOM   1166 C CD  . LYS B 1 9   ? -17.676 3.197   38.266  1.00 42.95 ? 9   LYS B CD  1 
ATOM   1167 C CE  . LYS B 1 9   ? -18.377 4.333   37.509  1.00 43.42 ? 9   LYS B CE  1 
ATOM   1168 N NZ  . LYS B 1 9   ? -18.295 4.160   36.025  1.00 43.86 ? 9   LYS B NZ  1 
ATOM   1169 N N   . GLY B 1 10  ? -17.959 1.547   43.646  1.00 42.46 ? 10  GLY B N   1 
ATOM   1170 C CA  . GLY B 1 10  ? -18.310 0.490   44.589  1.00 42.94 ? 10  GLY B CA  1 
ATOM   1171 C C   . GLY B 1 10  ? -19.793 0.182   44.587  1.00 43.25 ? 10  GLY B C   1 
ATOM   1172 O O   . GLY B 1 10  ? -20.559 0.744   43.796  1.00 43.20 ? 10  GLY B O   1 
ATOM   1173 N N   . ASP B 1 11  ? -20.193 -0.730  45.466  1.00 43.61 ? 11  ASP B N   1 
ATOM   1174 C CA  . ASP B 1 11  ? -21.607 -1.062  45.636  1.00 44.06 ? 11  ASP B CA  1 
ATOM   1175 C C   . ASP B 1 11  ? -22.307 -0.088  46.583  1.00 43.84 ? 11  ASP B C   1 
ATOM   1176 O O   . ASP B 1 11  ? -23.507 0.165   46.443  1.00 44.38 ? 11  ASP B O   1 
ATOM   1177 C CB  . ASP B 1 11  ? -21.763 -2.490  46.162  1.00 44.45 ? 11  ASP B CB  1 
ATOM   1178 C CG  . ASP B 1 11  ? -21.207 -3.538  45.198  1.00 46.05 ? 11  ASP B CG  1 
ATOM   1179 O OD1 . ASP B 1 11  ? -20.567 -3.164  44.183  1.00 48.10 ? 11  ASP B OD1 1 
ATOM   1180 O OD2 . ASP B 1 11  ? -21.413 -4.746  45.465  1.00 45.91 ? 11  ASP B OD2 1 
ATOM   1181 N N   . GLY B 1 12  ? -21.561 0.441   47.549  1.00 43.30 ? 12  GLY B N   1 
ATOM   1182 C CA  . GLY B 1 12  ? -22.115 1.341   48.556  1.00 42.88 ? 12  GLY B CA  1 
ATOM   1183 C C   . GLY B 1 12  ? -22.054 2.774   48.080  1.00 42.44 ? 12  GLY B C   1 
ATOM   1184 O O   . GLY B 1 12  ? -22.050 3.020   46.873  1.00 42.23 ? 12  GLY B O   1 
ATOM   1185 N N   . PRO B 1 13  ? -22.011 3.736   49.023  1.00 42.06 ? 13  PRO B N   1 
ATOM   1186 C CA  . PRO B 1 13  ? -21.941 5.156   48.661  1.00 41.78 ? 13  PRO B CA  1 
ATOM   1187 C C   . PRO B 1 13  ? -20.531 5.669   48.311  1.00 41.26 ? 13  PRO B C   1 
ATOM   1188 O O   . PRO B 1 13  ? -20.384 6.821   47.880  1.00 40.71 ? 13  PRO B O   1 
ATOM   1189 C CB  . PRO B 1 13  ? -22.494 5.854   49.908  1.00 41.91 ? 13  PRO B CB  1 
ATOM   1190 C CG  . PRO B 1 13  ? -22.137 4.954   51.031  1.00 42.09 ? 13  PRO B CG  1 
ATOM   1191 C CD  . PRO B 1 13  ? -22.058 3.546   50.484  1.00 42.14 ? 13  PRO B CD  1 
ATOM   1192 N N   . VAL B 1 14  ? -19.520 4.817   48.457  1.00 40.94 ? 14  VAL B N   1 
ATOM   1193 C CA  . VAL B 1 14  ? -18.143 5.235   48.256  1.00 40.96 ? 14  VAL B CA  1 
ATOM   1194 C C   . VAL B 1 14  ? -17.871 5.366   46.760  1.00 40.95 ? 14  VAL B C   1 
ATOM   1195 O O   . VAL B 1 14  ? -18.002 4.396   46.011  1.00 40.83 ? 14  VAL B O   1 
ATOM   1196 C CB  . VAL B 1 14  ? -17.126 4.260   48.903  1.00 40.87 ? 14  VAL B CB  1 
ATOM   1197 C CG1 . VAL B 1 14  ? -15.713 4.866   48.891  1.00 40.95 ? 14  VAL B CG1 1 
ATOM   1198 C CG2 . VAL B 1 14  ? -17.522 3.935   50.320  1.00 41.04 ? 14  VAL B CG2 1 
ATOM   1199 N N   . GLN B 1 15  ? -17.515 6.581   46.336  1.00 40.92 ? 15  GLN B N   1 
ATOM   1200 C CA  . GLN B 1 15  ? -17.137 6.860   44.953  1.00 40.89 ? 15  GLN B CA  1 
ATOM   1201 C C   . GLN B 1 15  ? -16.139 8.009   44.893  1.00 40.65 ? 15  GLN B C   1 
ATOM   1202 O O   . GLN B 1 15  ? -16.122 8.881   45.760  1.00 40.54 ? 15  GLN B O   1 
ATOM   1203 C CB  . GLN B 1 15  ? -18.364 7.188   44.097  1.00 40.96 ? 15  GLN B CB  1 
ATOM   1204 C CG  . GLN B 1 15  ? -19.171 8.398   44.539  1.00 41.66 ? 15  GLN B CG  1 
ATOM   1205 C CD  . GLN B 1 15  ? -20.338 8.703   43.593  1.00 42.24 ? 15  GLN B CD  1 
ATOM   1206 O OE1 . GLN B 1 15  ? -21.507 8.505   43.935  1.00 44.23 ? 15  GLN B OE1 1 
ATOM   1207 N NE2 . GLN B 1 15  ? -20.018 9.180   42.395  1.00 45.07 ? 15  GLN B NE2 1 
ATOM   1208 N N   . GLY B 1 16  ? -15.308 8.006   43.863  1.00 40.31 ? 16  GLY B N   1 
ATOM   1209 C CA  . GLY B 1 16  ? -14.310 9.047   43.702  1.00 40.32 ? 16  GLY B CA  1 
ATOM   1210 C C   . GLY B 1 16  ? -13.608 9.043   42.357  1.00 40.30 ? 16  GLY B C   1 
ATOM   1211 O O   . GLY B 1 16  ? -13.746 8.126   41.552  1.00 40.40 ? 16  GLY B O   1 
ATOM   1212 N N   . ILE B 1 17  ? -12.862 10.108  42.120  1.00 40.21 ? 17  ILE B N   1 
ATOM   1213 C CA  . ILE B 1 17  ? -12.084 10.271  40.913  1.00 40.06 ? 17  ILE B CA  1 
ATOM   1214 C C   . ILE B 1 17  ? -10.698 10.684  41.374  1.00 39.61 ? 17  ILE B C   1 
ATOM   1215 O O   . ILE B 1 17  ? -10.549 11.669  42.087  1.00 39.54 ? 17  ILE B O   1 
ATOM   1216 C CB  . ILE B 1 17  ? -12.723 11.327  39.980  1.00 40.08 ? 17  ILE B CB  1 
ATOM   1217 C CG1 . ILE B 1 17  ? -14.044 10.774  39.424  1.00 40.07 ? 17  ILE B CG1 1 
ATOM   1218 C CG2 . ILE B 1 17  ? -11.764 11.705  38.834  1.00 40.07 ? 17  ILE B CG2 1 
ATOM   1219 C CD1 . ILE B 1 17  ? -14.990 11.821  38.918  1.00 40.44 ? 17  ILE B CD1 1 
ATOM   1220 N N   . ILE B 1 18  ? -9.703  9.881   41.014  1.00 39.31 ? 18  ILE B N   1 
ATOM   1221 C CA  . ILE B 1 18  ? -8.318  10.145  41.373  1.00 39.13 ? 18  ILE B CA  1 
ATOM   1222 C C   . ILE B 1 18  ? -7.503  10.265  40.097  1.00 38.91 ? 18  ILE B C   1 
ATOM   1223 O O   . ILE B 1 18  ? -7.492  9.365   39.254  1.00 38.17 ? 18  ILE B O   1 
ATOM   1224 C CB  . ILE B 1 18  ? -7.731  9.038   42.258  1.00 38.99 ? 18  ILE B CB  1 
ATOM   1225 C CG1 . ILE B 1 18  ? -8.554  8.885   43.547  1.00 39.54 ? 18  ILE B CG1 1 
ATOM   1226 C CG2 . ILE B 1 18  ? -6.268  9.330   42.589  1.00 39.02 ? 18  ILE B CG2 1 
ATOM   1227 C CD1 . ILE B 1 18  ? -8.546  10.111  44.486  1.00 38.87 ? 18  ILE B CD1 1 
ATOM   1228 N N   . ASN B 1 19  ? -6.829  11.399  39.982  1.00 38.81 ? 19  ASN B N   1 
ATOM   1229 C CA  . ASN B 1 19  ? -5.956  11.705  38.865  1.00 38.90 ? 19  ASN B CA  1 
ATOM   1230 C C   . ASN B 1 19  ? -4.512  11.475  39.252  1.00 38.50 ? 19  ASN B C   1 
ATOM   1231 O O   . ASN B 1 19  ? -4.137  11.681  40.403  1.00 38.07 ? 19  ASN B O   1 
ATOM   1232 C CB  . ASN B 1 19  ? -6.130  13.170  38.465  1.00 39.00 ? 19  ASN B CB  1 
ATOM   1233 C CG  . ASN B 1 19  ? -7.477  13.442  37.841  1.00 40.09 ? 19  ASN B CG  1 
ATOM   1234 O OD1 . ASN B 1 19  ? -7.719  13.080  36.689  1.00 42.48 ? 19  ASN B OD1 1 
ATOM   1235 N ND2 . ASN B 1 19  ? -8.357  14.091  38.590  1.00 40.44 ? 19  ASN B ND2 1 
ATOM   1236 N N   . PHE B 1 20  ? -3.715  11.053  38.272  1.00 38.76 ? 20  PHE B N   1 
ATOM   1237 C CA  . PHE B 1 20  ? -2.266  10.914  38.413  1.00 38.53 ? 20  PHE B CA  1 
ATOM   1238 C C   . PHE B 1 20  ? -1.604  11.751  37.333  1.00 38.40 ? 20  PHE B C   1 
ATOM   1239 O O   . PHE B 1 20  ? -2.060  11.750  36.190  1.00 38.07 ? 20  PHE B O   1 
ATOM   1240 C CB  . PHE B 1 20  ? -1.829  9.465   38.222  1.00 38.79 ? 20  PHE B CB  1 
ATOM   1241 C CG  . PHE B 1 20  ? -2.521  8.495   39.118  1.00 38.52 ? 20  PHE B CG  1 
ATOM   1242 C CD1 . PHE B 1 20  ? -3.849  8.161   38.917  1.00 39.60 ? 20  PHE B CD1 1 
ATOM   1243 C CD2 . PHE B 1 20  ? -1.840  7.892   40.159  1.00 39.74 ? 20  PHE B CD2 1 
ATOM   1244 C CE1 . PHE B 1 20  ? -4.483  7.252   39.755  1.00 38.15 ? 20  PHE B CE1 1 
ATOM   1245 C CE2 . PHE B 1 20  ? -2.476  6.990   40.994  1.00 38.48 ? 20  PHE B CE2 1 
ATOM   1246 C CZ  . PHE B 1 20  ? -3.790  6.682   40.789  1.00 37.98 ? 20  PHE B CZ  1 
ATOM   1247 N N   . GLU B 1 21  ? -0.538  12.459  37.695  1.00 38.08 ? 21  GLU B N   1 
ATOM   1248 C CA  . GLU B 1 21  ? 0.290   13.157  36.723  1.00 38.29 ? 21  GLU B CA  1 
ATOM   1249 C C   . GLU B 1 21  ? 1.776   12.967  37.032  1.00 37.98 ? 21  GLU B C   1 
ATOM   1250 O O   . GLU B 1 21  ? 2.185   12.958  38.196  1.00 38.19 ? 21  GLU B O   1 
ATOM   1251 C CB  . GLU B 1 21  ? -0.037  14.653  36.715  1.00 38.28 ? 21  GLU B CB  1 
ATOM   1252 C CG  . GLU B 1 21  ? 0.433   15.350  35.464  1.00 38.55 ? 21  GLU B CG  1 
ATOM   1253 C CD  . GLU B 1 21  ? 0.542   16.854  35.623  1.00 39.96 ? 21  GLU B CD  1 
ATOM   1254 O OE1 . GLU B 1 21  ? 0.755   17.336  36.760  1.00 43.08 ? 21  GLU B OE1 1 
ATOM   1255 O OE2 . GLU B 1 21  ? 0.432   17.549  34.592  1.00 40.98 ? 21  GLU B OE2 1 
ATOM   1256 N N   . GLN B 1 22  ? 2.573   12.831  35.978  1.00 37.86 ? 22  GLN B N   1 
ATOM   1257 C CA  . GLN B 1 22  ? 4.015   12.675  36.093  1.00 37.93 ? 22  GLN B CA  1 
ATOM   1258 C C   . GLN B 1 22  ? 4.688   13.562  35.032  1.00 38.02 ? 22  GLN B C   1 
ATOM   1259 O O   . GLN B 1 22  ? 4.729   13.201  33.861  1.00 37.80 ? 22  GLN B O   1 
ATOM   1260 C CB  . GLN B 1 22  ? 4.392   11.193  35.918  1.00 37.62 ? 22  GLN B CB  1 
ATOM   1261 C CG  . GLN B 1 22  ? 5.644   10.779  36.668  1.00 37.63 ? 22  GLN B CG  1 
ATOM   1262 C CD  . GLN B 1 22  ? 6.070   9.340   36.429  1.00 37.54 ? 22  GLN B CD  1 
ATOM   1263 O OE1 . GLN B 1 22  ? 5.439   8.606   35.681  1.00 36.82 ? 22  GLN B OE1 1 
ATOM   1264 N NE2 . GLN B 1 22  ? 7.159   8.932   37.079  1.00 36.16 ? 22  GLN B NE2 1 
ATOM   1265 N N   . LYS B 1 23  ? 5.190   14.729  35.439  1.00 38.49 ? 23  LYS B N   1 
ATOM   1266 C CA  . LYS B 1 23  ? 5.891   15.630  34.511  1.00 38.76 ? 23  LYS B CA  1 
ATOM   1267 C C   . LYS B 1 23  ? 7.131   14.974  33.881  1.00 38.58 ? 23  LYS B C   1 
ATOM   1268 O O   . LYS B 1 23  ? 7.385   15.139  32.679  1.00 38.43 ? 23  LYS B O   1 
ATOM   1269 C CB  . LYS B 1 23  ? 6.349   16.924  35.205  1.00 39.55 ? 23  LYS B CB  1 
ATOM   1270 C CG  . LYS B 1 23  ? 5.252   17.788  35.817  1.00 41.16 ? 23  LYS B CG  1 
ATOM   1271 C CD  . LYS B 1 23  ? 4.375   18.453  34.771  1.00 42.70 ? 23  LYS B CD  1 
ATOM   1272 C CE  . LYS B 1 23  ? 3.408   19.455  35.423  1.00 43.26 ? 23  LYS B CE  1 
ATOM   1273 N NZ  . LYS B 1 23  ? 2.109   19.548  34.673  1.00 43.85 ? 23  LYS B NZ  1 
ATOM   1274 N N   . GLU B 1 24  ? 7.908   14.271  34.707  1.00 38.08 ? 24  GLU B N   1 
ATOM   1275 C CA  . GLU B 1 24  ? 9.155   13.634  34.277  1.00 38.12 ? 24  GLU B CA  1 
ATOM   1276 C C   . GLU B 1 24  ? 9.084   12.146  34.540  1.00 37.41 ? 24  GLU B C   1 
ATOM   1277 O O   . GLU B 1 24  ? 8.676   11.736  35.616  1.00 37.00 ? 24  GLU B O   1 
ATOM   1278 C CB  . GLU B 1 24  ? 10.342  14.198  35.057  1.00 38.65 ? 24  GLU B CB  1 
ATOM   1279 C CG  . GLU B 1 24  ? 10.542  15.706  34.940  1.00 39.64 ? 24  GLU B CG  1 
ATOM   1280 C CD  . GLU B 1 24  ? 10.888  16.145  33.534  1.00 42.32 ? 24  GLU B CD  1 
ATOM   1281 O OE1 . GLU B 1 24  ? 11.710  15.460  32.878  1.00 44.18 ? 24  GLU B OE1 1 
ATOM   1282 O OE2 . GLU B 1 24  ? 10.349  17.186  33.082  1.00 43.25 ? 24  GLU B OE2 1 
ATOM   1283 N N   . SER B 1 25  ? 9.528   11.334  33.584  1.00 37.18 ? 25  SER B N   1 
ATOM   1284 C CA  . SER B 1 25  ? 9.418   9.872   33.714  1.00 37.26 ? 25  SER B CA  1 
ATOM   1285 C C   . SER B 1 25  ? 10.262  9.276   34.851  1.00 36.97 ? 25  SER B C   1 
ATOM   1286 O O   . SER B 1 25  ? 10.015  8.147   35.276  1.00 36.98 ? 25  SER B O   1 
ATOM   1287 C CB  . SER B 1 25  ? 9.702   9.163   32.377  1.00 36.98 ? 25  SER B CB  1 
ATOM   1288 O OG  . SER B 1 25  ? 11.051  9.281   31.974  1.00 37.61 ? 25  SER B OG  1 
ATOM   1289 N N   . ASN B 1 26  ? 11.251  10.024  35.334  1.00 36.84 ? 26  ASN B N   1 
ATOM   1290 C CA  . ASN B 1 26  ? 11.990  9.643   36.537  1.00 36.83 ? 26  ASN B CA  1 
ATOM   1291 C C   . ASN B 1 26  ? 11.702  10.590  37.700  1.00 37.18 ? 26  ASN B C   1 
ATOM   1292 O O   . ASN B 1 26  ? 12.474  10.666  38.650  1.00 37.71 ? 26  ASN B O   1 
ATOM   1293 C CB  . ASN B 1 26  ? 13.500  9.562   36.256  1.00 36.72 ? 26  ASN B CB  1 
ATOM   1294 C CG  . ASN B 1 26  ? 14.112  10.908  35.934  1.00 36.18 ? 26  ASN B CG  1 
ATOM   1295 O OD1 . ASN B 1 26  ? 13.453  11.773  35.365  1.00 35.83 ? 26  ASN B OD1 1 
ATOM   1296 N ND2 . ASN B 1 26  ? 15.379  11.088  36.288  1.00 35.83 ? 26  ASN B ND2 1 
ATOM   1297 N N   . GLY B 1 27  ? 10.587  11.308  37.621  1.00 37.40 ? 27  GLY B N   1 
ATOM   1298 C CA  . GLY B 1 27  ? 10.183  12.223  38.672  1.00 37.64 ? 27  GLY B CA  1 
ATOM   1299 C C   . GLY B 1 27  ? 9.001   11.665  39.441  1.00 37.82 ? 27  GLY B C   1 
ATOM   1300 O O   . GLY B 1 27  ? 8.505   10.570  39.132  1.00 37.97 ? 27  GLY B O   1 
ATOM   1301 N N   . PRO B 1 28  ? 8.561   12.398  40.474  1.00 38.11 ? 28  PRO B N   1 
ATOM   1302 C CA  . PRO B 1 28  ? 7.416   11.983  41.266  1.00 38.41 ? 28  PRO B CA  1 
ATOM   1303 C C   . PRO B 1 28  ? 6.094   11.996  40.502  1.00 38.56 ? 28  PRO B C   1 
ATOM   1304 O O   . PRO B 1 28  ? 5.940   12.742  39.525  1.00 38.45 ? 28  PRO B O   1 
ATOM   1305 C CB  . PRO B 1 28  ? 7.383   13.006  42.402  1.00 38.36 ? 28  PRO B CB  1 
ATOM   1306 C CG  . PRO B 1 28  ? 8.105   14.179  41.894  1.00 38.84 ? 28  PRO B CG  1 
ATOM   1307 C CD  . PRO B 1 28  ? 9.158   13.644  40.982  1.00 38.44 ? 28  PRO B CD  1 
ATOM   1308 N N   . VAL B 1 29  ? 5.174   11.142  40.948  1.00 38.92 ? 29  VAL B N   1 
ATOM   1309 C CA  . VAL B 1 29  ? 3.788   11.120  40.473  1.00 39.36 ? 29  VAL B CA  1 
ATOM   1310 C C   . VAL B 1 29  ? 2.903   11.942  41.433  1.00 39.95 ? 29  VAL B C   1 
ATOM   1311 O O   . VAL B 1 29  ? 2.886   11.702  42.647  1.00 39.77 ? 29  VAL B O   1 
ATOM   1312 C CB  . VAL B 1 29  ? 3.241   9.668   40.371  1.00 39.16 ? 29  VAL B CB  1 
ATOM   1313 C CG1 . VAL B 1 29  ? 1.846   9.660   39.777  1.00 39.84 ? 29  VAL B CG1 1 
ATOM   1314 C CG2 . VAL B 1 29  ? 4.151   8.802   39.519  1.00 38.72 ? 29  VAL B CG2 1 
ATOM   1315 N N   . LYS B 1 30  ? 2.190   12.921  40.883  1.00 40.58 ? 30  LYS B N   1 
ATOM   1316 C CA  . LYS B 1 30  ? 1.224   13.714  41.640  1.00 40.79 ? 30  LYS B CA  1 
ATOM   1317 C C   . LYS B 1 30  ? -0.108  12.970  41.625  1.00 41.05 ? 30  LYS B C   1 
ATOM   1318 O O   . LYS B 1 30  ? -0.624  12.624  40.558  1.00 41.09 ? 30  LYS B O   1 
ATOM   1319 C CB  . LYS B 1 30  ? 1.073   15.085  40.993  1.00 41.16 ? 30  LYS B CB  1 
ATOM   1320 C CG  . LYS B 1 30  ? 0.242   16.098  41.771  1.00 41.65 ? 30  LYS B CG  1 
ATOM   1321 C CD  . LYS B 1 30  ? 0.067   17.380  40.940  1.00 41.94 ? 30  LYS B CD  1 
ATOM   1322 C CE  . LYS B 1 30  ? -1.212  18.141  41.277  1.00 42.90 ? 30  LYS B CE  1 
ATOM   1323 N NZ  . LYS B 1 30  ? -1.487  19.208  40.248  1.00 43.01 ? 30  LYS B NZ  1 
ATOM   1324 N N   . VAL B 1 31  ? -0.645  12.684  42.807  1.00 41.05 ? 31  VAL B N   1 
ATOM   1325 C CA  . VAL B 1 31  ? -1.929  11.996  42.922  1.00 40.72 ? 31  VAL B CA  1 
ATOM   1326 C C   . VAL B 1 31  ? -2.911  12.944  43.611  1.00 40.59 ? 31  VAL B C   1 
ATOM   1327 O O   . VAL B 1 31  ? -2.675  13.401  44.728  1.00 40.43 ? 31  VAL B O   1 
ATOM   1328 C CB  . VAL B 1 31  ? -1.799  10.685  43.693  1.00 40.57 ? 31  VAL B CB  1 
ATOM   1329 C CG1 . VAL B 1 31  ? -3.097  9.855   43.610  1.00 40.80 ? 31  VAL B CG1 1 
ATOM   1330 C CG2 . VAL B 1 31  ? -0.611  9.881   43.165  1.00 40.83 ? 31  VAL B CG2 1 
ATOM   1331 N N   . TRP B 1 32  ? -4.002  13.266  42.930  1.00 40.33 ? 32  TRP B N   1 
ATOM   1332 C CA  . TRP B 1 32  ? -5.011  14.107  43.533  1.00 40.54 ? 32  TRP B CA  1 
ATOM   1333 C C   . TRP B 1 32  ? -6.416  13.788  43.036  1.00 40.13 ? 32  TRP B C   1 
ATOM   1334 O O   . TRP B 1 32  ? -6.612  13.238  41.951  1.00 39.68 ? 32  TRP B O   1 
ATOM   1335 C CB  . TRP B 1 32  ? -4.674  15.589  43.305  1.00 40.71 ? 32  TRP B CB  1 
ATOM   1336 C CG  . TRP B 1 32  ? -5.086  16.119  41.960  1.00 41.18 ? 32  TRP B CG  1 
ATOM   1337 C CD1 . TRP B 1 32  ? -6.171  16.901  41.689  1.00 41.34 ? 32  TRP B CD1 1 
ATOM   1338 C CD2 . TRP B 1 32  ? -4.418  15.913  40.710  1.00 40.80 ? 32  TRP B CD2 1 
ATOM   1339 N NE1 . TRP B 1 32  ? -6.222  17.192  40.350  1.00 41.65 ? 32  TRP B NE1 1 
ATOM   1340 C CE2 . TRP B 1 32  ? -5.160  16.594  39.724  1.00 41.47 ? 32  TRP B CE2 1 
ATOM   1341 C CE3 . TRP B 1 32  ? -3.267  15.219  40.329  1.00 41.26 ? 32  TRP B CE3 1 
ATOM   1342 C CZ2 . TRP B 1 32  ? -4.782  16.608  38.382  1.00 41.40 ? 32  TRP B CZ2 1 
ATOM   1343 C CZ3 . TRP B 1 32  ? -2.894  15.227  38.993  1.00 41.11 ? 32  TRP B CZ3 1 
ATOM   1344 C CH2 . TRP B 1 32  ? -3.654  15.909  38.035  1.00 41.34 ? 32  TRP B CH2 1 
ATOM   1345 N N   . GLY B 1 33  ? -7.385  14.168  43.852  1.00 40.23 ? 33  GLY B N   1 
ATOM   1346 C CA  . GLY B 1 33  ? -8.788  13.952  43.551  1.00 40.33 ? 33  GLY B CA  1 
ATOM   1347 C C   . GLY B 1 33  ? -9.602  14.010  44.825  1.00 40.45 ? 33  GLY B C   1 
ATOM   1348 O O   . GLY B 1 33  ? -9.241  14.711  45.780  1.00 40.10 ? 33  GLY B O   1 
ATOM   1349 N N   . SER B 1 34  ? -10.699 13.261  44.843  1.00 40.30 ? 34  SER B N   1 
ATOM   1350 C CA  . SER B 1 34  ? -11.611 13.290  45.974  1.00 40.09 ? 34  SER B CA  1 
ATOM   1351 C C   . SER B 1 34  ? -12.378 11.992  46.054  1.00 39.51 ? 34  SER B C   1 
ATOM   1352 O O   . SER B 1 34  ? -12.722 11.411  45.027  1.00 39.18 ? 34  SER B O   1 
ATOM   1353 C CB  . SER B 1 34  ? -12.581 14.462  45.844  1.00 40.08 ? 34  SER B CB  1 
ATOM   1354 O OG  . SER B 1 34  ? -13.431 14.540  46.972  1.00 41.18 ? 34  SER B OG  1 
ATOM   1355 N N   . ILE B 1 35  ? -12.618 11.542  47.280  1.00 39.22 ? 35  ILE B N   1 
ATOM   1356 C CA  . ILE B 1 35  ? -13.447 10.369  47.534  1.00 39.45 ? 35  ILE B CA  1 
ATOM   1357 C C   . ILE B 1 35  ? -14.534 10.739  48.538  1.00 39.23 ? 35  ILE B C   1 
ATOM   1358 O O   . ILE B 1 35  ? -14.260 11.399  49.536  1.00 38.72 ? 35  ILE B O   1 
ATOM   1359 C CB  . ILE B 1 35  ? -12.632 9.184   48.071  1.00 39.20 ? 35  ILE B CB  1 
ATOM   1360 C CG1 . ILE B 1 35  ? -11.385 8.958   47.203  1.00 39.29 ? 35  ILE B CG1 1 
ATOM   1361 C CG2 . ILE B 1 35  ? -13.511 7.919   48.126  1.00 39.32 ? 35  ILE B CG2 1 
ATOM   1362 C CD1 . ILE B 1 35  ? -10.418 7.915   47.749  1.00 39.62 ? 35  ILE B CD1 1 
ATOM   1363 N N   . LYS B 1 36  ? -15.764 10.317  48.258  1.00 39.06 ? 36  LYS B N   1 
ATOM   1364 C CA  . LYS B 1 36  ? -16.887 10.574  49.151  1.00 39.42 ? 36  LYS B CA  1 
ATOM   1365 C C   . LYS B 1 36  ? -17.599 9.268   49.504  1.00 38.94 ? 36  LYS B C   1 
ATOM   1366 O O   . LYS B 1 36  ? -17.318 8.228   48.921  1.00 38.53 ? 36  LYS B O   1 
ATOM   1367 C CB  . LYS B 1 36  ? -17.859 11.596  48.540  1.00 39.48 ? 36  LYS B CB  1 
ATOM   1368 C CG  . LYS B 1 36  ? -18.191 11.363  47.074  1.00 40.68 ? 36  LYS B CG  1 
ATOM   1369 C CD  . LYS B 1 36  ? -19.188 12.392  46.561  1.00 40.97 ? 36  LYS B CD  1 
ATOM   1370 C CE  . LYS B 1 36  ? -20.623 11.931  46.745  1.00 42.95 ? 36  LYS B CE  1 
ATOM   1371 N NZ  . LYS B 1 36  ? -21.038 10.986  45.678  1.00 44.15 ? 36  LYS B NZ  1 
ATOM   1372 N N   . GLY B 1 37  ? -18.491 9.336   50.487  1.00 38.77 ? 37  GLY B N   1 
ATOM   1373 C CA  . GLY B 1 37  ? -19.220 8.169   50.975  1.00 38.67 ? 37  GLY B CA  1 
ATOM   1374 C C   . GLY B 1 37  ? -18.474 7.344   52.007  1.00 38.39 ? 37  GLY B C   1 
ATOM   1375 O O   . GLY B 1 37  ? -18.869 6.216   52.307  1.00 37.88 ? 37  GLY B O   1 
ATOM   1376 N N   . LEU B 1 38  ? -17.406 7.910   52.563  1.00 38.43 ? 38  LEU B N   1 
ATOM   1377 C CA  . LEU B 1 38  ? -16.548 7.201   53.511  1.00 38.62 ? 38  LEU B CA  1 
ATOM   1378 C C   . LEU B 1 38  ? -16.931 7.523   54.948  1.00 38.65 ? 38  LEU B C   1 
ATOM   1379 O O   . LEU B 1 38  ? -17.493 8.581   55.230  1.00 38.53 ? 38  LEU B O   1 
ATOM   1380 C CB  . LEU B 1 38  ? -15.087 7.606   53.296  1.00 38.56 ? 38  LEU B CB  1 
ATOM   1381 C CG  . LEU B 1 38  ? -14.450 7.211   51.968  1.00 39.08 ? 38  LEU B CG  1 
ATOM   1382 C CD1 . LEU B 1 38  ? -13.213 8.057   51.719  1.00 39.47 ? 38  LEU B CD1 1 
ATOM   1383 C CD2 . LEU B 1 38  ? -14.110 5.719   51.956  1.00 38.82 ? 38  LEU B CD2 1 
ATOM   1384 N N   . THR B 1 39  ? -16.620 6.607   55.862  1.00 38.68 ? 39  THR B N   1 
ATOM   1385 C CA  . THR B 1 39  ? -16.692 6.922   57.278  1.00 38.71 ? 39  THR B CA  1 
ATOM   1386 C C   . THR B 1 39  ? -15.571 7.913   57.589  1.00 38.69 ? 39  THR B C   1 
ATOM   1387 O O   . THR B 1 39  ? -14.510 7.887   56.952  1.00 38.04 ? 39  THR B O   1 
ATOM   1388 C CB  . THR B 1 39  ? -16.523 5.676   58.178  1.00 38.93 ? 39  THR B CB  1 
ATOM   1389 O OG1 . THR B 1 39  ? -15.293 5.016   57.866  1.00 38.62 ? 39  THR B OG1 1 
ATOM   1390 C CG2 . THR B 1 39  ? -17.673 4.712   57.990  1.00 38.93 ? 39  THR B CG2 1 
ATOM   1391 N N   . GLU B 1 40  ? -15.817 8.784   58.562  1.00 38.85 ? 40  GLU B N   1 
ATOM   1392 C CA  . GLU B 1 40  ? -14.796 9.701   59.059  1.00 39.01 ? 40  GLU B CA  1 
ATOM   1393 C C   . GLU B 1 40  ? -13.551 8.926   59.515  1.00 38.94 ? 40  GLU B C   1 
ATOM   1394 O O   . GLU B 1 40  ? -13.662 7.933   60.230  1.00 38.99 ? 40  GLU B O   1 
ATOM   1395 C CB  . GLU B 1 40  ? -15.364 10.512  60.225  1.00 39.25 ? 40  GLU B CB  1 
ATOM   1396 C CG  . GLU B 1 40  ? -14.483 11.653  60.686  1.00 39.26 ? 40  GLU B CG  1 
ATOM   1397 C CD  . GLU B 1 40  ? -15.093 12.456  61.817  1.00 39.88 ? 40  GLU B CD  1 
ATOM   1398 O OE1 . GLU B 1 40  ? -16.250 12.191  62.229  1.00 41.45 ? 40  GLU B OE1 1 
ATOM   1399 O OE2 . GLU B 1 40  ? -14.396 13.369  62.301  1.00 41.47 ? 40  GLU B OE2 1 
ATOM   1400 N N   . GLY B 1 41  ? -12.374 9.371   59.087  1.00 38.82 ? 41  GLY B N   1 
ATOM   1401 C CA  . GLY B 1 41  ? -11.123 8.761   59.520  1.00 38.97 ? 41  GLY B CA  1 
ATOM   1402 C C   . GLY B 1 41  ? -10.278 8.182   58.403  1.00 38.96 ? 41  GLY B C   1 
ATOM   1403 O O   . GLY B 1 41  ? -10.557 8.377   57.220  1.00 39.25 ? 41  GLY B O   1 
ATOM   1404 N N   . LEU B 1 42  ? -9.238  7.458   58.796  1.00 38.94 ? 42  LEU B N   1 
ATOM   1405 C CA  . LEU B 1 42  ? -8.240  6.952   57.864  1.00 39.18 ? 42  LEU B CA  1 
ATOM   1406 C C   . LEU B 1 42  ? -8.737  5.735   57.076  1.00 39.07 ? 42  LEU B C   1 
ATOM   1407 O O   . LEU B 1 42  ? -9.389  4.855   57.626  1.00 38.69 ? 42  LEU B O   1 
ATOM   1408 C CB  . LEU B 1 42  ? -6.945  6.606   58.616  1.00 39.21 ? 42  LEU B CB  1 
ATOM   1409 C CG  . LEU B 1 42  ? -6.205  7.766   59.289  1.00 39.85 ? 42  LEU B CG  1 
ATOM   1410 C CD1 . LEU B 1 42  ? -5.074  7.241   60.149  1.00 40.76 ? 42  LEU B CD1 1 
ATOM   1411 C CD2 . LEU B 1 42  ? -5.660  8.729   58.285  1.00 40.06 ? 42  LEU B CD2 1 
ATOM   1412 N N   . HIS B 1 43  ? -8.426  5.712   55.782  1.00 39.19 ? 43  HIS B N   1 
ATOM   1413 C CA  . HIS B 1 43  ? -8.769  4.596   54.898  1.00 39.42 ? 43  HIS B CA  1 
ATOM   1414 C C   . HIS B 1 43  ? -7.584  4.216   54.024  1.00 39.23 ? 43  HIS B C   1 
ATOM   1415 O O   . HIS B 1 43  ? -7.008  5.070   53.354  1.00 39.27 ? 43  HIS B O   1 
ATOM   1416 C CB  . HIS B 1 43  ? -9.947  4.964   53.994  1.00 39.62 ? 43  HIS B CB  1 
ATOM   1417 C CG  . HIS B 1 43  ? -11.231 5.144   54.735  1.00 39.53 ? 43  HIS B CG  1 
ATOM   1418 N ND1 . HIS B 1 43  ? -12.065 4.092   55.031  1.00 39.23 ? 43  HIS B ND1 1 
ATOM   1419 C CD2 . HIS B 1 43  ? -11.810 6.249   55.262  1.00 39.70 ? 43  HIS B CD2 1 
ATOM   1420 C CE1 . HIS B 1 43  ? -13.108 4.540   55.707  1.00 40.04 ? 43  HIS B CE1 1 
ATOM   1421 N NE2 . HIS B 1 43  ? -12.978 5.846   55.860  1.00 40.00 ? 43  HIS B NE2 1 
ATOM   1422 N N   . GLY B 1 44  ? -7.254  2.928   54.012  1.00 39.34 ? 44  GLY B N   1 
ATOM   1423 C CA  . GLY B 1 44  ? -6.150  2.425   53.210  1.00 39.66 ? 44  GLY B CA  1 
ATOM   1424 C C   . GLY B 1 44  ? -6.314  2.763   51.740  1.00 39.99 ? 44  GLY B C   1 
ATOM   1425 O O   . GLY B 1 44  ? -7.424  2.712   51.200  1.00 40.23 ? 44  GLY B O   1 
ATOM   1426 N N   . PHE B 1 45  ? -5.200  3.091   51.089  1.00 40.08 ? 45  PHE B N   1 
ATOM   1427 C CA  . PHE B 1 45  ? -5.213  3.627   49.731  1.00 40.01 ? 45  PHE B CA  1 
ATOM   1428 C C   . PHE B 1 45  ? -4.075  2.957   48.987  1.00 40.20 ? 45  PHE B C   1 
ATOM   1429 O O   . PHE B 1 45  ? -2.920  3.355   49.140  1.00 40.43 ? 45  PHE B O   1 
ATOM   1430 C CB  . PHE B 1 45  ? -5.030  5.148   49.823  1.00 40.05 ? 45  PHE B CB  1 
ATOM   1431 C CG  . PHE B 1 45  ? -5.286  5.897   48.541  1.00 40.05 ? 45  PHE B CG  1 
ATOM   1432 C CD1 . PHE B 1 45  ? -6.538  5.890   47.954  1.00 39.77 ? 45  PHE B CD1 1 
ATOM   1433 C CD2 . PHE B 1 45  ? -4.283  6.663   47.960  1.00 40.12 ? 45  PHE B CD2 1 
ATOM   1434 C CE1 . PHE B 1 45  ? -6.779  6.593   46.792  1.00 40.20 ? 45  PHE B CE1 1 
ATOM   1435 C CE2 . PHE B 1 45  ? -4.520  7.373   46.789  1.00 40.26 ? 45  PHE B CE2 1 
ATOM   1436 C CZ  . PHE B 1 45  ? -5.768  7.338   46.207  1.00 39.51 ? 45  PHE B CZ  1 
ATOM   1437 N N   . HIS B 1 46  ? -4.394  1.904   48.226  1.00 40.23 ? 46  HIS B N   1 
ATOM   1438 C CA  . HIS B 1 46  ? -3.375  1.028   47.633  1.00 40.03 ? 46  HIS B CA  1 
ATOM   1439 C C   . HIS B 1 46  ? -3.589  0.738   46.160  1.00 39.81 ? 46  HIS B C   1 
ATOM   1440 O O   . HIS B 1 46  ? -4.726  0.687   45.689  1.00 39.97 ? 46  HIS B O   1 
ATOM   1441 C CB  . HIS B 1 46  ? -3.343  -0.320  48.347  1.00 40.54 ? 46  HIS B CB  1 
ATOM   1442 C CG  . HIS B 1 46  ? -3.141  -0.215  49.823  1.00 40.76 ? 46  HIS B CG  1 
ATOM   1443 N ND1 . HIS B 1 46  ? -3.824  -1.001  50.721  1.00 40.27 ? 46  HIS B ND1 1 
ATOM   1444 C CD2 . HIS B 1 46  ? -2.347  0.600   50.557  1.00 41.48 ? 46  HIS B CD2 1 
ATOM   1445 C CE1 . HIS B 1 46  ? -3.449  -0.686  51.948  1.00 41.54 ? 46  HIS B CE1 1 
ATOM   1446 N NE2 . HIS B 1 46  ? -2.557  0.286   51.875  1.00 41.39 ? 46  HIS B NE2 1 
ATOM   1447 N N   . VAL B 1 47  ? -2.486  0.526   45.446  1.00 39.22 ? 47  VAL B N   1 
ATOM   1448 C CA  . VAL B 1 47  ? -2.531  0.024   44.081  1.00 38.92 ? 47  VAL B CA  1 
ATOM   1449 C C   . VAL B 1 47  ? -2.378  -1.486  44.182  1.00 38.56 ? 47  VAL B C   1 
ATOM   1450 O O   . VAL B 1 47  ? -1.410  -1.984  44.775  1.00 38.38 ? 47  VAL B O   1 
ATOM   1451 C CB  . VAL B 1 47  ? -1.420  0.618   43.175  1.00 39.01 ? 47  VAL B CB  1 
ATOM   1452 C CG1 . VAL B 1 47  ? -1.631  0.208   41.731  1.00 38.76 ? 47  VAL B CG1 1 
ATOM   1453 C CG2 . VAL B 1 47  ? -1.392  2.137   43.269  1.00 38.85 ? 47  VAL B CG2 1 
ATOM   1454 N N   . HIS B 1 48  ? -3.341  -2.204  43.612  1.00 38.15 ? 48  HIS B N   1 
ATOM   1455 C CA  . HIS B 1 48  ? -3.336  -3.660  43.605  1.00 38.33 ? 48  HIS B CA  1 
ATOM   1456 C C   . HIS B 1 48  ? -2.908  -4.202  42.237  1.00 38.40 ? 48  HIS B C   1 
ATOM   1457 O O   . HIS B 1 48  ? -3.005  -3.519  41.231  1.00 38.27 ? 48  HIS B O   1 
ATOM   1458 C CB  . HIS B 1 48  ? -4.717  -4.180  44.016  1.00 37.92 ? 48  HIS B CB  1 
ATOM   1459 C CG  . HIS B 1 48  ? -5.024  -3.973  45.466  1.00 37.11 ? 48  HIS B CG  1 
ATOM   1460 N ND1 . HIS B 1 48  ? -5.036  -5.005  46.380  1.00 37.78 ? 48  HIS B ND1 1 
ATOM   1461 C CD2 . HIS B 1 48  ? -5.308  -2.849  46.165  1.00 37.23 ? 48  HIS B CD2 1 
ATOM   1462 C CE1 . HIS B 1 48  ? -5.325  -4.526  47.577  1.00 38.13 ? 48  HIS B CE1 1 
ATOM   1463 N NE2 . HIS B 1 48  ? -5.491  -3.218  47.474  1.00 37.32 ? 48  HIS B NE2 1 
ATOM   1464 N N   . GLU B 1 49  ? -2.446  -5.444  42.207  1.00 38.98 ? 49  GLU B N   1 
ATOM   1465 C CA  . GLU B 1 49  ? -1.743  -5.954  41.040  1.00 39.47 ? 49  GLU B CA  1 
ATOM   1466 C C   . GLU B 1 49  ? -2.605  -6.076  39.786  1.00 39.84 ? 49  GLU B C   1 
ATOM   1467 O O   . GLU B 1 49  ? -2.135  -5.801  38.691  1.00 39.58 ? 49  GLU B O   1 
ATOM   1468 C CB  . GLU B 1 49  ? -1.097  -7.306  41.357  1.00 39.23 ? 49  GLU B CB  1 
ATOM   1469 C CG  . GLU B 1 49  ? -0.118  -7.768  40.292  1.00 39.29 ? 49  GLU B CG  1 
ATOM   1470 C CD  . GLU B 1 49  ? 0.515   -9.106  40.611  1.00 39.26 ? 49  GLU B CD  1 
ATOM   1471 O OE1 . GLU B 1 49  ? 0.321   -9.599  41.739  1.00 39.93 ? 49  GLU B OE1 1 
ATOM   1472 O OE2 . GLU B 1 49  ? 1.214   -9.653  39.732  1.00 38.83 ? 49  GLU B OE2 1 
ATOM   1473 N N   . PHE B 1 50  ? -3.855  -6.492  39.935  1.00 40.75 ? 50  PHE B N   1 
ATOM   1474 C CA  . PHE B 1 50  ? -4.674  -6.863  38.781  1.00 41.86 ? 50  PHE B CA  1 
ATOM   1475 C C   . PHE B 1 50  ? -5.995  -6.101  38.671  1.00 42.90 ? 50  PHE B C   1 
ATOM   1476 O O   . PHE B 1 50  ? -6.583  -5.694  39.681  1.00 43.11 ? 50  PHE B O   1 
ATOM   1477 C CB  . PHE B 1 50  ? -5.001  -8.349  38.844  1.00 41.80 ? 50  PHE B CB  1 
ATOM   1478 C CG  . PHE B 1 50  ? -3.794  -9.237  38.838  1.00 42.12 ? 50  PHE B CG  1 
ATOM   1479 C CD1 . PHE B 1 50  ? -2.974  -9.301  37.721  1.00 42.17 ? 50  PHE B CD1 1 
ATOM   1480 C CD2 . PHE B 1 50  ? -3.491  -10.023 39.937  1.00 41.23 ? 50  PHE B CD2 1 
ATOM   1481 C CE1 . PHE B 1 50  ? -1.865  -10.135 37.705  1.00 41.79 ? 50  PHE B CE1 1 
ATOM   1482 C CE2 . PHE B 1 50  ? -2.388  -10.841 39.930  1.00 41.41 ? 50  PHE B CE2 1 
ATOM   1483 C CZ  . PHE B 1 50  ? -1.571  -10.902 38.811  1.00 41.44 ? 50  PHE B CZ  1 
ATOM   1484 N N   . GLY B 1 51  ? -6.458  -5.937  37.430  1.00 43.99 ? 51  GLY B N   1 
ATOM   1485 C CA  . GLY B 1 51  ? -7.810  -5.453  37.153  1.00 44.26 ? 51  GLY B CA  1 
ATOM   1486 C C   . GLY B 1 51  ? -8.791  -6.589  37.350  1.00 45.00 ? 51  GLY B C   1 
ATOM   1487 O O   . GLY B 1 51  ? -8.417  -7.761  37.224  1.00 44.81 ? 51  GLY B O   1 
ATOM   1488 N N   . ASP B 1 52  ? -10.043 -6.247  37.665  1.00 45.55 ? 52  ASP B N   1 
ATOM   1489 C CA  . ASP B 1 52  ? -11.092 -7.248  37.863  1.00 45.96 ? 52  ASP B CA  1 
ATOM   1490 C C   . ASP B 1 52  ? -11.188 -8.152  36.639  1.00 46.34 ? 52  ASP B C   1 
ATOM   1491 O O   . ASP B 1 52  ? -11.118 -7.677  35.509  1.00 46.61 ? 52  ASP B O   1 
ATOM   1492 C CB  . ASP B 1 52  ? -12.466 -6.593  38.096  1.00 46.06 ? 52  ASP B CB  1 
ATOM   1493 C CG  . ASP B 1 52  ? -12.524 -5.743  39.376  1.00 47.02 ? 52  ASP B CG  1 
ATOM   1494 O OD1 . ASP B 1 52  ? -11.490 -5.610  40.090  1.00 46.89 ? 52  ASP B OD1 1 
ATOM   1495 O OD2 . ASP B 1 52  ? -13.621 -5.199  39.654  1.00 46.30 ? 52  ASP B OD2 1 
ATOM   1496 N N   . ASN B 1 53  ? -11.331 -9.452  36.868  1.00 46.64 ? 53  ASN B N   1 
ATOM   1497 C CA  . ASN B 1 53  ? -11.643 -10.398 35.794  1.00 46.95 ? 53  ASN B CA  1 
ATOM   1498 C C   . ASN B 1 53  ? -13.075 -10.901 35.947  1.00 47.19 ? 53  ASN B C   1 
ATOM   1499 O O   . ASN B 1 53  ? -13.466 -11.908 35.344  1.00 47.25 ? 53  ASN B O   1 
ATOM   1500 C CB  . ASN B 1 53  ? -10.627 -11.558 35.757  1.00 47.13 ? 53  ASN B CB  1 
ATOM   1501 C CG  . ASN B 1 53  ? -10.778 -12.553 36.927  1.00 47.72 ? 53  ASN B CG  1 
ATOM   1502 O OD1 . ASN B 1 53  ? -10.173 -13.629 36.905  1.00 46.49 ? 53  ASN B OD1 1 
ATOM   1503 N ND2 . ASN B 1 53  ? -11.577 -12.200 37.937  1.00 47.96 ? 53  ASN B ND2 1 
ATOM   1504 N N   . THR B 1 54  ? -13.846 -10.192 36.773  1.00 47.53 ? 54  THR B N   1 
ATOM   1505 C CA  . THR B 1 54  ? -15.233 -10.542 37.027  1.00 47.88 ? 54  THR B CA  1 
ATOM   1506 C C   . THR B 1 54  ? -16.084 -9.291  37.278  1.00 48.16 ? 54  THR B C   1 
ATOM   1507 O O   . THR B 1 54  ? -15.580 -8.243  37.719  1.00 47.77 ? 54  THR B O   1 
ATOM   1508 C CB  . THR B 1 54  ? -15.353 -11.550 38.208  1.00 47.95 ? 54  THR B CB  1 
ATOM   1509 O OG1 . THR B 1 54  ? -16.660 -12.127 38.217  1.00 48.10 ? 54  THR B OG1 1 
ATOM   1510 C CG2 . THR B 1 54  ? -15.069 -10.885 39.555  1.00 48.13 ? 54  THR B CG2 1 
ATOM   1511 N N   . ALA B 1 55  ? -17.374 -9.419  36.970  1.00 48.64 ? 55  ALA B N   1 
ATOM   1512 C CA  . ALA B 1 55  ? -18.349 -8.345  37.159  1.00 48.97 ? 55  ALA B CA  1 
ATOM   1513 C C   . ALA B 1 55  ? -18.822 -8.281  38.617  1.00 49.21 ? 55  ALA B C   1 
ATOM   1514 O O   . ALA B 1 55  ? -19.234 -9.293  39.191  1.00 49.43 ? 55  ALA B O   1 
ATOM   1515 C CB  . ALA B 1 55  ? -19.542 -8.561  36.231  1.00 48.99 ? 55  ALA B CB  1 
ATOM   1516 N N   . GLY B 1 56  ? -18.770 -7.091  39.207  1.00 49.54 ? 56  GLY B N   1 
ATOM   1517 C CA  . GLY B 1 56  ? -19.208 -6.902  40.591  1.00 49.78 ? 56  GLY B CA  1 
ATOM   1518 C C   . GLY B 1 56  ? -18.285 -7.550  41.616  1.00 50.06 ? 56  GLY B C   1 
ATOM   1519 O O   . GLY B 1 56  ? -18.744 -7.995  42.678  1.00 50.13 ? 56  GLY B O   1 
ATOM   1520 N N   . ALA B 1 57  ? -16.988 -7.597  41.293  1.00 50.19 ? 57  ALA B N   1 
ATOM   1521 C CA  . ALA B 1 57  ? -15.961 -8.166  42.173  1.00 50.15 ? 57  ALA B CA  1 
ATOM   1522 C C   . ALA B 1 57  ? -15.921 -7.430  43.515  1.00 50.33 ? 57  ALA B C   1 
ATOM   1523 O O   . ALA B 1 57  ? -15.956 -6.195  43.553  1.00 50.98 ? 57  ALA B O   1 
ATOM   1524 C CB  . ALA B 1 57  ? -14.596 -8.085  41.500  1.00 50.15 ? 57  ALA B CB  1 
ATOM   1525 N N   . THR B 1 58  ? -15.845 -8.188  44.609  1.00 50.28 ? 58  THR B N   1 
ATOM   1526 C CA  . THR B 1 58  ? -15.784 -7.604  45.961  1.00 50.11 ? 58  THR B CA  1 
ATOM   1527 C C   . THR B 1 58  ? -14.378 -7.654  46.577  1.00 49.90 ? 58  THR B C   1 
ATOM   1528 O O   . THR B 1 58  ? -14.107 -6.978  47.582  1.00 49.76 ? 58  THR B O   1 
ATOM   1529 C CB  . THR B 1 58  ? -16.782 -8.300  46.923  1.00 50.17 ? 58  THR B CB  1 
ATOM   1530 O OG1 . THR B 1 58  ? -16.380 -9.657  47.153  1.00 50.49 ? 58  THR B OG1 1 
ATOM   1531 C CG2 . THR B 1 58  ? -18.203 -8.272  46.349  1.00 50.53 ? 58  THR B CG2 1 
ATOM   1532 N N   . SER B 1 59  ? -13.493 -8.451  45.979  1.00 49.55 ? 59  SER B N   1 
ATOM   1533 C CA  . SER B 1 59  ? -12.131 -8.597  46.472  1.00 49.42 ? 59  SER B CA  1 
ATOM   1534 C C   . SER B 1 59  ? -11.181 -7.675  45.719  1.00 49.30 ? 59  SER B C   1 
ATOM   1535 O O   . SER B 1 59  ? -11.240 -7.580  44.491  1.00 49.38 ? 59  SER B O   1 
ATOM   1536 C CB  . SER B 1 59  ? -11.670 -10.045 46.328  1.00 49.45 ? 59  SER B CB  1 
ATOM   1537 O OG  . SER B 1 59  ? -12.480 -10.901 47.123  1.00 50.17 ? 59  SER B OG  1 
ATOM   1538 N N   . ALA B 1 60  ? -10.335 -6.974  46.475  1.00 48.93 ? 60  ALA B N   1 
ATOM   1539 C CA  . ALA B 1 60  ? -9.141  -6.335  45.930  1.00 48.61 ? 60  ALA B CA  1 
ATOM   1540 C C   . ALA B 1 60  ? -8.051  -7.385  46.013  1.00 48.39 ? 60  ALA B C   1 
ATOM   1541 O O   . ALA B 1 60  ? -7.765  -7.899  47.105  1.00 49.03 ? 60  ALA B O   1 
ATOM   1542 C CB  . ALA B 1 60  ? -8.761  -5.130  46.743  1.00 48.67 ? 60  ALA B CB  1 
ATOM   1543 N N   . GLY B 1 61  ? -7.444  -7.714  44.879  1.00 47.79 ? 61  GLY B N   1 
ATOM   1544 C CA  . GLY B 1 61  ? -6.526  -8.855  44.823  1.00 47.21 ? 61  GLY B CA  1 
ATOM   1545 C C   . GLY B 1 61  ? -5.185  -8.550  45.466  1.00 46.63 ? 61  GLY B C   1 
ATOM   1546 O O   . GLY B 1 61  ? -5.100  -7.716  46.376  1.00 46.66 ? 61  GLY B O   1 
ATOM   1547 N N   . PRO B 1 62  ? -4.124  -9.233  45.010  1.00 45.87 ? 62  PRO B N   1 
ATOM   1548 C CA  . PRO B 1 62  ? -2.808  -8.983  45.584  1.00 45.32 ? 62  PRO B CA  1 
ATOM   1549 C C   . PRO B 1 62  ? -2.413  -7.519  45.506  1.00 44.82 ? 62  PRO B C   1 
ATOM   1550 O O   . PRO B 1 62  ? -2.870  -6.784  44.620  1.00 44.41 ? 62  PRO B O   1 
ATOM   1551 C CB  . PRO B 1 62  ? -1.870  -9.838  44.719  1.00 45.63 ? 62  PRO B CB  1 
ATOM   1552 C CG  . PRO B 1 62  ? -2.734  -10.906 44.128  1.00 45.47 ? 62  PRO B CG  1 
ATOM   1553 C CD  . PRO B 1 62  ? -4.101  -10.295 43.984  1.00 45.98 ? 62  PRO B CD  1 
ATOM   1554 N N   . HIS B 1 63  ? -1.588  -7.094  46.452  1.00 44.20 ? 63  HIS B N   1 
ATOM   1555 C CA  . HIS B 1 63  ? -0.977  -5.774  46.379  1.00 43.83 ? 63  HIS B CA  1 
ATOM   1556 C C   . HIS B 1 63  ? -0.004  -5.755  45.198  1.00 42.94 ? 63  HIS B C   1 
ATOM   1557 O O   . HIS B 1 63  ? 0.592   -6.782  44.868  1.00 42.27 ? 63  HIS B O   1 
ATOM   1558 C CB  . HIS B 1 63  ? -0.239  -5.451  47.682  1.00 44.16 ? 63  HIS B CB  1 
ATOM   1559 C CG  . HIS B 1 63  ? -1.116  -4.887  48.756  1.00 44.71 ? 63  HIS B CG  1 
ATOM   1560 N ND1 . HIS B 1 63  ? -0.846  -3.684  49.377  1.00 45.05 ? 63  HIS B ND1 1 
ATOM   1561 C CD2 . HIS B 1 63  ? -2.250  -5.360  49.328  1.00 45.55 ? 63  HIS B CD2 1 
ATOM   1562 C CE1 . HIS B 1 63  ? -1.777  -3.441  50.285  1.00 45.41 ? 63  HIS B CE1 1 
ATOM   1563 N NE2 . HIS B 1 63  ? -2.644  -4.440  50.272  1.00 45.48 ? 63  HIS B NE2 1 
ATOM   1564 N N   . PHE B 1 64  ? 0.151   -4.594  44.562  1.00 41.70 ? 64  PHE B N   1 
ATOM   1565 C CA  . PHE B 1 64  ? 1.142   -4.444  43.498  1.00 41.49 ? 64  PHE B CA  1 
ATOM   1566 C C   . PHE B 1 64  ? 2.520   -4.315  44.145  1.00 40.94 ? 64  PHE B C   1 
ATOM   1567 O O   . PHE B 1 64  ? 2.876   -3.258  44.684  1.00 40.67 ? 64  PHE B O   1 
ATOM   1568 C CB  . PHE B 1 64  ? 0.826   -3.235  42.607  1.00 40.70 ? 64  PHE B CB  1 
ATOM   1569 C CG  . PHE B 1 64  ? 1.791   -3.045  41.467  1.00 40.70 ? 64  PHE B CG  1 
ATOM   1570 C CD1 . PHE B 1 64  ? 2.096   -4.086  40.611  1.00 40.20 ? 64  PHE B CD1 1 
ATOM   1571 C CD2 . PHE B 1 64  ? 2.385   -1.814  41.241  1.00 40.03 ? 64  PHE B CD2 1 
ATOM   1572 C CE1 . PHE B 1 64  ? 2.991   -3.902  39.566  1.00 40.15 ? 64  PHE B CE1 1 
ATOM   1573 C CE2 . PHE B 1 64  ? 3.264   -1.635  40.193  1.00 39.57 ? 64  PHE B CE2 1 
ATOM   1574 C CZ  . PHE B 1 64  ? 3.565   -2.675  39.358  1.00 39.74 ? 64  PHE B CZ  1 
ATOM   1575 N N   . ASN B 1 65  ? 3.272   -5.412  44.096  1.00 40.71 ? 65  ASN B N   1 
ATOM   1576 C CA  . ASN B 1 65  ? 4.550   -5.527  44.791  1.00 40.86 ? 65  ASN B CA  1 
ATOM   1577 C C   . ASN B 1 65  ? 5.550   -6.251  43.900  1.00 40.79 ? 65  ASN B C   1 
ATOM   1578 O O   . ASN B 1 65  ? 5.930   -7.384  44.180  1.00 40.31 ? 65  ASN B O   1 
ATOM   1579 C CB  . ASN B 1 65  ? 4.360   -6.280  46.122  1.00 40.61 ? 65  ASN B CB  1 
ATOM   1580 C CG  . ASN B 1 65  ? 5.626   -6.308  46.981  1.00 40.64 ? 65  ASN B CG  1 
ATOM   1581 O OD1 . ASN B 1 65  ? 6.562   -5.536  46.768  1.00 39.13 ? 65  ASN B OD1 1 
ATOM   1582 N ND2 . ASN B 1 65  ? 5.647   -7.201  47.964  1.00 40.18 ? 65  ASN B ND2 1 
ATOM   1583 N N   . PRO B 1 66  ? 5.962   -5.603  42.800  1.00 41.13 ? 66  PRO B N   1 
ATOM   1584 C CA  . PRO B 1 66  ? 6.859   -6.274  41.863  1.00 41.51 ? 66  PRO B CA  1 
ATOM   1585 C C   . PRO B 1 66  ? 8.256   -6.538  42.429  1.00 41.92 ? 66  PRO B C   1 
ATOM   1586 O O   . PRO B 1 66  ? 8.915   -7.466  41.981  1.00 41.87 ? 66  PRO B O   1 
ATOM   1587 C CB  . PRO B 1 66  ? 6.915   -5.310  40.672  1.00 41.43 ? 66  PRO B CB  1 
ATOM   1588 C CG  . PRO B 1 66  ? 6.572   -3.992  41.224  1.00 40.98 ? 66  PRO B CG  1 
ATOM   1589 C CD  . PRO B 1 66  ? 5.620   -4.241  42.358  1.00 41.06 ? 66  PRO B CD  1 
ATOM   1590 N N   . LEU B 1 67  ? 8.690   -5.747  43.413  1.00 42.44 ? 67  LEU B N   1 
ATOM   1591 C CA  . LEU B 1 67  ? 10.037  -5.892  43.993  1.00 42.71 ? 67  LEU B CA  1 
ATOM   1592 C C   . LEU B 1 67  ? 10.070  -6.818  45.218  1.00 42.84 ? 67  LEU B C   1 
ATOM   1593 O O   . LEU B 1 67  ? 11.129  -7.036  45.808  1.00 42.72 ? 67  LEU B O   1 
ATOM   1594 C CB  . LEU B 1 67  ? 10.619  -4.513  44.327  1.00 42.96 ? 67  LEU B CB  1 
ATOM   1595 C CG  . LEU B 1 67  ? 10.588  -3.506  43.158  1.00 43.90 ? 67  LEU B CG  1 
ATOM   1596 C CD1 . LEU B 1 67  ? 11.103  -2.124  43.583  1.00 44.98 ? 67  LEU B CD1 1 
ATOM   1597 C CD2 . LEU B 1 67  ? 11.381  -4.012  41.956  1.00 44.22 ? 67  LEU B CD2 1 
ATOM   1598 N N   . SER B 1 68  ? 8.910   -7.363  45.581  1.00 43.05 ? 68  SER B N   1 
ATOM   1599 C CA  . SER B 1 68  ? 8.777   -8.378  46.633  1.00 43.29 ? 68  SER B CA  1 
ATOM   1600 C C   . SER B 1 68  ? 9.244   -7.907  48.009  1.00 43.39 ? 68  SER B C   1 
ATOM   1601 O O   . SER B 1 68  ? 9.938   -8.635  48.713  1.00 43.26 ? 68  SER B O   1 
ATOM   1602 C CB  . SER B 1 68  ? 9.512   -9.663  46.237  1.00 43.48 ? 68  SER B CB  1 
ATOM   1603 O OG  . SER B 1 68  ? 9.171   -10.053 44.915  1.00 44.32 ? 68  SER B OG  1 
ATOM   1604 N N   . ARG B 1 69  ? 8.842   -6.693  48.385  1.00 43.54 ? 69  ARG B N   1 
ATOM   1605 C CA  . ARG B 1 69  ? 9.142   -6.145  49.706  1.00 43.61 ? 69  ARG B CA  1 
ATOM   1606 C C   . ARG B 1 69  ? 8.000   -6.474  50.672  1.00 43.52 ? 69  ARG B C   1 
ATOM   1607 O O   . ARG B 1 69  ? 6.980   -7.041  50.277  1.00 43.61 ? 69  ARG B O   1 
ATOM   1608 C CB  . ARG B 1 69  ? 9.325   -4.620  49.652  1.00 43.98 ? 69  ARG B CB  1 
ATOM   1609 C CG  . ARG B 1 69  ? 10.127  -4.077  48.473  1.00 45.24 ? 69  ARG B CG  1 
ATOM   1610 C CD  . ARG B 1 69  ? 11.534  -4.626  48.393  1.00 47.72 ? 69  ARG B CD  1 
ATOM   1611 N NE  . ARG B 1 69  ? 12.353  -4.329  49.571  1.00 48.65 ? 69  ARG B NE  1 
ATOM   1612 C CZ  . ARG B 1 69  ? 12.867  -3.133  49.877  1.00 49.23 ? 69  ARG B CZ  1 
ATOM   1613 N NH1 . ARG B 1 69  ? 12.647  -2.062  49.111  1.00 49.14 ? 69  ARG B NH1 1 
ATOM   1614 N NH2 . ARG B 1 69  ? 13.602  -3.007  50.975  1.00 48.92 ? 69  ARG B NH2 1 
ATOM   1615 N N   . LYS B 1 70  ? 8.175   -6.092  51.936  1.00 43.11 ? 70  LYS B N   1 
ATOM   1616 C CA  . LYS B 1 70  ? 7.125   -6.219  52.940  1.00 42.93 ? 70  LYS B CA  1 
ATOM   1617 C C   . LYS B 1 70  ? 6.269   -4.965  52.916  1.00 42.36 ? 70  LYS B C   1 
ATOM   1618 O O   . LYS B 1 70  ? 6.715   -3.915  52.457  1.00 42.10 ? 70  LYS B O   1 
ATOM   1619 C CB  . LYS B 1 70  ? 7.731   -6.399  54.332  1.00 43.23 ? 70  LYS B CB  1 
ATOM   1620 C CG  . LYS B 1 70  ? 8.585   -7.663  54.495  1.00 44.53 ? 70  LYS B CG  1 
ATOM   1621 C CD  . LYS B 1 70  ? 7.735   -8.926  54.348  1.00 45.45 ? 70  LYS B CD  1 
ATOM   1622 C CE  . LYS B 1 70  ? 8.395   -10.143 54.970  1.00 45.53 ? 70  LYS B CE  1 
ATOM   1623 N NZ  . LYS B 1 70  ? 7.404   -11.237 55.190  1.00 46.29 ? 70  LYS B NZ  1 
ATOM   1624 N N   . HIS B 1 71  ? 5.044   -5.071  53.419  1.00 41.85 ? 71  HIS B N   1 
ATOM   1625 C CA  . HIS B 1 71  ? 4.146   -3.920  53.457  1.00 41.92 ? 71  HIS B CA  1 
ATOM   1626 C C   . HIS B 1 71  ? 4.664   -2.855  54.419  1.00 41.92 ? 71  HIS B C   1 
ATOM   1627 O O   . HIS B 1 71  ? 5.176   -3.177  55.491  1.00 42.16 ? 71  HIS B O   1 
ATOM   1628 C CB  . HIS B 1 71  ? 2.731   -4.336  53.868  1.00 41.44 ? 71  HIS B CB  1 
ATOM   1629 C CG  . HIS B 1 71  ? 1.785   -3.184  54.004  1.00 41.24 ? 71  HIS B CG  1 
ATOM   1630 N ND1 . HIS B 1 71  ? 1.260   -2.518  52.916  1.00 40.08 ? 71  HIS B ND1 1 
ATOM   1631 C CD2 . HIS B 1 71  ? 1.277   -2.574  55.099  1.00 40.86 ? 71  HIS B CD2 1 
ATOM   1632 C CE1 . HIS B 1 71  ? 0.466   -1.550  53.337  1.00 40.67 ? 71  HIS B CE1 1 
ATOM   1633 N NE2 . HIS B 1 71  ? 0.462   -1.559  54.658  1.00 41.15 ? 71  HIS B NE2 1 
ATOM   1634 N N   . GLY B 1 72  ? 4.514   -1.591  54.030  1.00 41.80 ? 72  GLY B N   1 
ATOM   1635 C CA  . GLY B 1 72  ? 4.907   -0.471  54.863  1.00 41.66 ? 72  GLY B CA  1 
ATOM   1636 C C   . GLY B 1 72  ? 4.094   0.753   54.515  1.00 41.62 ? 72  GLY B C   1 
ATOM   1637 O O   . GLY B 1 72  ? 3.095   0.666   53.812  1.00 41.70 ? 72  GLY B O   1 
ATOM   1638 N N   . GLY B 1 73  ? 4.519   1.898   55.025  1.00 41.85 ? 73  GLY B N   1 
ATOM   1639 C CA  . GLY B 1 73  ? 3.908   3.165   54.670  1.00 42.02 ? 73  GLY B CA  1 
ATOM   1640 C C   . GLY B 1 73  ? 4.617   3.730   53.460  1.00 42.08 ? 73  GLY B C   1 
ATOM   1641 O O   . GLY B 1 73  ? 5.686   3.241   53.098  1.00 41.73 ? 73  GLY B O   1 
ATOM   1642 N N   . PRO B 1 74  ? 4.027   4.761   52.827  1.00 42.30 ? 74  PRO B N   1 
ATOM   1643 C CA  . PRO B 1 74  ? 4.644   5.430   51.674  1.00 42.65 ? 74  PRO B CA  1 
ATOM   1644 C C   . PRO B 1 74  ? 6.024   6.041   51.954  1.00 42.84 ? 74  PRO B C   1 
ATOM   1645 O O   . PRO B 1 74  ? 6.827   6.132   51.040  1.00 42.64 ? 74  PRO B O   1 
ATOM   1646 C CB  . PRO B 1 74  ? 3.640   6.534   51.323  1.00 42.76 ? 74  PRO B CB  1 
ATOM   1647 C CG  . PRO B 1 74  ? 2.795   6.704   52.537  1.00 42.74 ? 74  PRO B CG  1 
ATOM   1648 C CD  . PRO B 1 74  ? 2.729   5.362   53.177  1.00 42.32 ? 74  PRO B CD  1 
ATOM   1649 N N   . LYS B 1 75  ? 6.283   6.462   53.193  1.00 43.18 ? 75  LYS B N   1 
ATOM   1650 C CA  . LYS B 1 75  ? 7.580   7.040   53.564  1.00 43.82 ? 75  LYS B CA  1 
ATOM   1651 C C   . LYS B 1 75  ? 8.643   5.986   53.857  1.00 43.82 ? 75  LYS B C   1 
ATOM   1652 O O   . LYS B 1 75  ? 9.815   6.325   53.987  1.00 43.69 ? 75  LYS B O   1 
ATOM   1653 C CB  . LYS B 1 75  ? 7.451   7.935   54.803  1.00 44.23 ? 75  LYS B CB  1 
ATOM   1654 C CG  . LYS B 1 75  ? 6.668   9.224   54.591  1.00 45.07 ? 75  LYS B CG  1 
ATOM   1655 C CD  . LYS B 1 75  ? 6.477   9.990   55.915  1.00 45.09 ? 75  LYS B CD  1 
ATOM   1656 C CE  . LYS B 1 75  ? 5.237   10.889  55.858  1.00 46.35 ? 75  LYS B CE  1 
ATOM   1657 N NZ  . LYS B 1 75  ? 4.867   11.475  57.191  1.00 47.72 ? 75  LYS B NZ  1 
ATOM   1658 N N   . ASP B 1 76  ? 8.238   4.726   53.997  1.00 43.89 ? 76  ASP B N   1 
ATOM   1659 C CA  . ASP B 1 76  ? 9.170   3.658   54.345  1.00 44.12 ? 76  ASP B CA  1 
ATOM   1660 C C   . ASP B 1 76  ? 9.918   3.197   53.105  1.00 44.13 ? 76  ASP B C   1 
ATOM   1661 O O   . ASP B 1 76  ? 9.382   3.220   51.997  1.00 44.16 ? 76  ASP B O   1 
ATOM   1662 C CB  . ASP B 1 76  ? 8.443   2.469   54.979  1.00 44.18 ? 76  ASP B CB  1 
ATOM   1663 C CG  . ASP B 1 76  ? 7.717   2.835   56.264  1.00 45.11 ? 76  ASP B CG  1 
ATOM   1664 O OD1 . ASP B 1 76  ? 8.010   3.906   56.841  1.00 46.17 ? 76  ASP B OD1 1 
ATOM   1665 O OD2 . ASP B 1 76  ? 6.849   2.043   56.704  1.00 44.40 ? 76  ASP B OD2 1 
ATOM   1666 N N   . GLU B 1 77  ? 11.166  2.791   53.297  1.00 44.30 ? 77  GLU B N   1 
ATOM   1667 C CA  . GLU B 1 77  ? 11.948  2.196   52.221  1.00 44.07 ? 77  GLU B CA  1 
ATOM   1668 C C   . GLU B 1 77  ? 11.482  0.757   51.988  1.00 43.75 ? 77  GLU B C   1 
ATOM   1669 O O   . GLU B 1 77  ? 11.442  0.284   50.847  1.00 43.73 ? 77  GLU B O   1 
ATOM   1670 C CB  . GLU B 1 77  ? 13.435  2.246   52.563  1.00 44.82 ? 77  GLU B CB  1 
ATOM   1671 C CG  . GLU B 1 77  ? 14.355  1.823   51.419  1.00 45.36 ? 77  GLU B CG  1 
ATOM   1672 C CD  . GLU B 1 77  ? 14.594  0.324   51.358  1.00 47.74 ? 77  GLU B CD  1 
ATOM   1673 O OE1 . GLU B 1 77  ? 14.519  -0.354  52.413  1.00 48.50 ? 77  GLU B OE1 1 
ATOM   1674 O OE2 . GLU B 1 77  ? 14.871  -0.173  50.243  1.00 48.70 ? 77  GLU B OE2 1 
ATOM   1675 N N   . GLU B 1 78  ? 11.126  0.072   53.072  1.00 43.22 ? 78  GLU B N   1 
ATOM   1676 C CA  . GLU B 1 78  ? 10.508  -1.245  52.983  1.00 42.82 ? 78  GLU B CA  1 
ATOM   1677 C C   . GLU B 1 78  ? 9.006   -1.071  52.779  1.00 42.24 ? 78  GLU B C   1 
ATOM   1678 O O   . GLU B 1 78  ? 8.262   -0.848  53.731  1.00 42.03 ? 78  GLU B O   1 
ATOM   1679 C CB  . GLU B 1 78  ? 10.788  -2.078  54.242  1.00 43.16 ? 78  GLU B CB  1 
ATOM   1680 C CG  . GLU B 1 78  ? 10.420  -3.569  54.107  1.00 43.88 ? 78  GLU B CG  1 
ATOM   1681 C CD  . GLU B 1 78  ? 11.409  -4.345  53.244  1.00 45.85 ? 78  GLU B CD  1 
ATOM   1682 O OE1 . GLU B 1 78  ? 12.610  -3.994  53.277  1.00 47.98 ? 78  GLU B OE1 1 
ATOM   1683 O OE2 . GLU B 1 78  ? 11.001  -5.308  52.548  1.00 44.89 ? 78  GLU B OE2 1 
ATOM   1684 N N   . ARG B 1 79  ? 8.580   -1.161  51.522  1.00 41.63 ? 79  ARG B N   1 
ATOM   1685 C CA  . ARG B 1 79  ? 7.173   -1.037  51.145  1.00 41.17 ? 79  ARG B CA  1 
ATOM   1686 C C   . ARG B 1 79  ? 6.956   -1.680  49.785  1.00 40.98 ? 79  ARG B C   1 
ATOM   1687 O O   . ARG B 1 79  ? 7.915   -1.886  49.032  1.00 40.67 ? 79  ARG B O   1 
ATOM   1688 C CB  . ARG B 1 79  ? 6.763   0.434   51.060  1.00 40.97 ? 79  ARG B CB  1 
ATOM   1689 C CG  . ARG B 1 79  ? 7.569   1.222   50.039  1.00 40.64 ? 79  ARG B CG  1 
ATOM   1690 C CD  . ARG B 1 79  ? 7.023   2.608   49.803  1.00 40.46 ? 79  ARG B CD  1 
ATOM   1691 N NE  . ARG B 1 79  ? 6.056   2.625   48.714  1.00 39.53 ? 79  ARG B NE  1 
ATOM   1692 C CZ  . ARG B 1 79  ? 5.579   3.728   48.147  1.00 40.24 ? 79  ARG B CZ  1 
ATOM   1693 N NH1 . ARG B 1 79  ? 5.960   4.923   48.568  1.00 39.62 ? 79  ARG B NH1 1 
ATOM   1694 N NH2 . ARG B 1 79  ? 4.716   3.632   47.146  1.00 40.55 ? 79  ARG B NH2 1 
ATOM   1695 N N   . HIS B 1 80  ? 5.694   -1.976  49.478  1.00 40.63 ? 80  HIS B N   1 
ATOM   1696 C CA  . HIS B 1 80  ? 5.294   -2.337  48.119  1.00 40.28 ? 80  HIS B CA  1 
ATOM   1697 C C   . HIS B 1 80  ? 5.259   -1.079  47.267  1.00 40.01 ? 80  HIS B C   1 
ATOM   1698 O O   . HIS B 1 80  ? 5.109   0.032   47.781  1.00 39.81 ? 80  HIS B O   1 
ATOM   1699 C CB  . HIS B 1 80  ? 3.889   -2.942  48.065  1.00 40.10 ? 80  HIS B CB  1 
ATOM   1700 C CG  . HIS B 1 80  ? 3.645   -4.046  49.040  1.00 39.97 ? 80  HIS B CG  1 
ATOM   1701 N ND1 . HIS B 1 80  ? 2.376   -4.412  49.430  1.00 40.26 ? 80  HIS B ND1 1 
ATOM   1702 C CD2 . HIS B 1 80  ? 4.493   -4.868  49.702  1.00 40.27 ? 80  HIS B CD2 1 
ATOM   1703 C CE1 . HIS B 1 80  ? 2.452   -5.420  50.279  1.00 39.21 ? 80  HIS B CE1 1 
ATOM   1704 N NE2 . HIS B 1 80  ? 3.724   -5.711  50.467  1.00 39.05 ? 80  HIS B NE2 1 
ATOM   1705 N N   . VAL B 1 81  ? 5.348   -1.259  45.955  1.00 39.68 ? 81  VAL B N   1 
ATOM   1706 C CA  . VAL B 1 81  ? 5.181   -0.138  45.039  1.00 39.54 ? 81  VAL B CA  1 
ATOM   1707 C C   . VAL B 1 81  ? 3.803   0.505   45.269  1.00 39.21 ? 81  VAL B C   1 
ATOM   1708 O O   . VAL B 1 81  ? 3.682   1.722   45.275  1.00 39.14 ? 81  VAL B O   1 
ATOM   1709 C CB  . VAL B 1 81  ? 5.391   -0.571  43.554  1.00 39.55 ? 81  VAL B CB  1 
ATOM   1710 C CG1 . VAL B 1 81  ? 4.916   0.502   42.580  1.00 38.95 ? 81  VAL B CG1 1 
ATOM   1711 C CG2 . VAL B 1 81  ? 6.861   -0.897  43.307  1.00 39.70 ? 81  VAL B CG2 1 
ATOM   1712 N N   . GLY B 1 82  ? 2.781   -0.311  45.500  1.00 38.78 ? 82  GLY B N   1 
ATOM   1713 C CA  . GLY B 1 82  ? 1.417   0.190   45.663  1.00 38.71 ? 82  GLY B CA  1 
ATOM   1714 C C   . GLY B 1 82  ? 1.024   0.636   47.064  1.00 38.56 ? 82  GLY B C   1 
ATOM   1715 O O   . GLY B 1 82  ? -0.154  0.844   47.327  1.00 38.67 ? 82  GLY B O   1 
ATOM   1716 N N   . ASP B 1 83  ? 1.991   0.774   47.967  1.00 38.47 ? 83  ASP B N   1 
ATOM   1717 C CA  . ASP B 1 83  ? 1.718   1.215   49.334  1.00 38.28 ? 83  ASP B CA  1 
ATOM   1718 C C   . ASP B 1 83  ? 1.608   2.736   49.406  1.00 38.52 ? 83  ASP B C   1 
ATOM   1719 O O   . ASP B 1 83  ? 2.571   3.413   49.778  1.00 38.25 ? 83  ASP B O   1 
ATOM   1720 C CB  . ASP B 1 83  ? 2.833   0.766   50.288  1.00 38.19 ? 83  ASP B CB  1 
ATOM   1721 C CG  . ASP B 1 83  ? 2.752   -0.709  50.654  1.00 37.95 ? 83  ASP B CG  1 
ATOM   1722 O OD1 . ASP B 1 83  ? 1.687   -1.329  50.468  1.00 37.74 ? 83  ASP B OD1 1 
ATOM   1723 O OD2 . ASP B 1 83  ? 3.763   -1.234  51.154  1.00 37.48 ? 83  ASP B OD2 1 
ATOM   1724 N N   . LEU B 1 84  ? 0.433   3.269   49.093  1.00 38.82 ? 84  LEU B N   1 
ATOM   1725 C CA  . LEU B 1 84  ? 0.222   4.719   49.146  1.00 39.31 ? 84  LEU B CA  1 
ATOM   1726 C C   . LEU B 1 84  ? -0.432  5.173   50.443  1.00 39.71 ? 84  LEU B C   1 
ATOM   1727 O O   . LEU B 1 84  ? -0.976  6.282   50.514  1.00 40.58 ? 84  LEU B O   1 
ATOM   1728 C CB  . LEU B 1 84  ? -0.599  5.190   47.942  1.00 39.45 ? 84  LEU B CB  1 
ATOM   1729 C CG  . LEU B 1 84  ? -0.022  4.826   46.566  1.00 40.40 ? 84  LEU B CG  1 
ATOM   1730 C CD1 . LEU B 1 84  ? -0.945  5.314   45.465  1.00 40.51 ? 84  LEU B CD1 1 
ATOM   1731 C CD2 . LEU B 1 84  ? 1.386   5.388   46.382  1.00 40.90 ? 84  LEU B CD2 1 
ATOM   1732 N N   . GLY B 1 85  ? -0.375  4.331   51.472  1.00 39.72 ? 85  GLY B N   1 
ATOM   1733 C CA  . GLY B 1 85  ? -0.811  4.716   52.809  1.00 39.63 ? 85  GLY B CA  1 
ATOM   1734 C C   . GLY B 1 85  ? -2.309  4.885   53.004  1.00 39.50 ? 85  GLY B C   1 
ATOM   1735 O O   . GLY B 1 85  ? -3.101  4.002   52.661  1.00 39.55 ? 85  GLY B O   1 
ATOM   1736 N N   . ASN B 1 86  ? -2.680  6.028   53.569  1.00 39.55 ? 86  ASN B N   1 
ATOM   1737 C CA  . ASN B 1 86  ? -4.049  6.302   53.969  1.00 39.80 ? 86  ASN B CA  1 
ATOM   1738 C C   . ASN B 1 86  ? -4.530  7.601   53.377  1.00 40.12 ? 86  ASN B C   1 
ATOM   1739 O O   . ASN B 1 86  ? -3.753  8.554   53.245  1.00 40.12 ? 86  ASN B O   1 
ATOM   1740 C CB  . ASN B 1 86  ? -4.152  6.440   55.493  1.00 39.66 ? 86  ASN B CB  1 
ATOM   1741 C CG  . ASN B 1 86  ? -3.990  5.129   56.213  1.00 39.18 ? 86  ASN B CG  1 
ATOM   1742 O OD1 . ASN B 1 86  ? -4.738  4.193   55.979  1.00 37.83 ? 86  ASN B OD1 1 
ATOM   1743 N ND2 . ASN B 1 86  ? -3.020  5.060   57.111  1.00 39.65 ? 86  ASN B ND2 1 
ATOM   1744 N N   . VAL B 1 87  ? -5.817  7.642   53.040  1.00 40.16 ? 87  VAL B N   1 
ATOM   1745 C CA  . VAL B 1 87  ? -6.507  8.918   52.854  1.00 40.03 ? 87  VAL B CA  1 
ATOM   1746 C C   . VAL B 1 87  ? -7.395  9.161   54.063  1.00 39.94 ? 87  VAL B C   1 
ATOM   1747 O O   . VAL B 1 87  ? -7.779  8.224   54.753  1.00 39.53 ? 87  VAL B O   1 
ATOM   1748 C CB  . VAL B 1 87  ? -7.329  8.985   51.552  1.00 40.13 ? 87  VAL B CB  1 
ATOM   1749 C CG1 . VAL B 1 87  ? -6.400  8.890   50.359  1.00 40.39 ? 87  VAL B CG1 1 
ATOM   1750 C CG2 . VAL B 1 87  ? -8.440  7.907   51.506  1.00 40.33 ? 87  VAL B CG2 1 
ATOM   1751 N N   . THR B 1 88  ? -7.693  10.430  54.317  1.00 40.00 ? 88  THR B N   1 
ATOM   1752 C CA  . THR B 1 88  ? -8.452  10.835  55.490  1.00 40.01 ? 88  THR B CA  1 
ATOM   1753 C C   . THR B 1 88  ? -9.763  11.481  55.072  1.00 40.01 ? 88  THR B C   1 
ATOM   1754 O O   . THR B 1 88  ? -9.774  12.468  54.336  1.00 39.78 ? 88  THR B O   1 
ATOM   1755 C CB  . THR B 1 88  ? -7.654  11.830  56.336  1.00 40.01 ? 88  THR B CB  1 
ATOM   1756 O OG1 . THR B 1 88  ? -6.438  11.212  56.760  1.00 40.01 ? 88  THR B OG1 1 
ATOM   1757 C CG2 . THR B 1 88  ? -8.442  12.272  57.564  1.00 40.06 ? 88  THR B CG2 1 
ATOM   1758 N N   . ALA B 1 89  ? -10.861 10.900  55.547  1.00 40.23 ? 89  ALA B N   1 
ATOM   1759 C CA  . ALA B 1 89  ? -12.201 11.411  55.299  1.00 40.21 ? 89  ALA B CA  1 
ATOM   1760 C C   . ALA B 1 89  ? -12.608 12.313  56.454  1.00 40.27 ? 89  ALA B C   1 
ATOM   1761 O O   . ALA B 1 89  ? -12.407 11.970  57.619  1.00 40.11 ? 89  ALA B O   1 
ATOM   1762 C CB  . ALA B 1 89  ? -13.178 10.256  55.164  1.00 40.10 ? 89  ALA B CB  1 
ATOM   1763 N N   . ASP B 1 90  ? -13.178 13.467  56.123  1.00 40.55 ? 90  ASP B N   1 
ATOM   1764 C CA  . ASP B 1 90  ? -13.696 14.386  57.122  1.00 40.84 ? 90  ASP B CA  1 
ATOM   1765 C C   . ASP B 1 90  ? -15.021 13.863  57.712  1.00 41.08 ? 90  ASP B C   1 
ATOM   1766 O O   . ASP B 1 90  ? -15.445 12.745  57.406  1.00 41.11 ? 90  ASP B O   1 
ATOM   1767 C CB  . ASP B 1 90  ? -13.835 15.806  56.531  1.00 40.95 ? 90  ASP B CB  1 
ATOM   1768 C CG  . ASP B 1 90  ? -14.892 15.912  55.432  1.00 41.11 ? 90  ASP B CG  1 
ATOM   1769 O OD1 . ASP B 1 90  ? -15.719 14.988  55.265  1.00 40.27 ? 90  ASP B OD1 1 
ATOM   1770 O OD2 . ASP B 1 90  ? -14.896 16.953  54.737  1.00 41.22 ? 90  ASP B OD2 1 
ATOM   1771 N N   . LYS B 1 91  ? -15.662 14.663  58.563  1.00 41.18 ? 91  LYS B N   1 
ATOM   1772 C CA  . LYS B 1 91  ? -16.930 14.274  59.187  1.00 41.25 ? 91  LYS B CA  1 
ATOM   1773 C C   . LYS B 1 91  ? -18.077 14.158  58.175  1.00 41.24 ? 91  LYS B C   1 
ATOM   1774 O O   . LYS B 1 91  ? -19.059 13.456  58.419  1.00 41.42 ? 91  LYS B O   1 
ATOM   1775 C CB  . LYS B 1 91  ? -17.307 15.266  60.293  1.00 41.46 ? 91  LYS B CB  1 
ATOM   1776 C CG  . LYS B 1 91  ? -17.636 16.674  59.796  1.00 41.69 ? 91  LYS B CG  1 
ATOM   1777 C CD  . LYS B 1 91  ? -18.011 17.595  60.944  1.00 41.97 ? 91  LYS B CD  1 
ATOM   1778 C CE  . LYS B 1 91  ? -18.201 19.031  60.464  1.00 42.60 ? 91  LYS B CE  1 
ATOM   1779 N NZ  . LYS B 1 91  ? -16.962 19.577  59.825  1.00 42.95 ? 91  LYS B NZ  1 
ATOM   1780 N N   . ASP B 1 92  ? -17.951 14.862  57.051  1.00 41.15 ? 92  ASP B N   1 
ATOM   1781 C CA  . ASP B 1 92  ? -18.898 14.754  55.934  1.00 40.90 ? 92  ASP B CA  1 
ATOM   1782 C C   . ASP B 1 92  ? -18.606 13.537  55.047  1.00 40.41 ? 92  ASP B C   1 
ATOM   1783 O O   . ASP B 1 92  ? -19.306 13.296  54.062  1.00 39.69 ? 92  ASP B O   1 
ATOM   1784 C CB  . ASP B 1 92  ? -18.853 16.025  55.075  1.00 41.07 ? 92  ASP B CB  1 
ATOM   1785 C CG  . ASP B 1 92  ? -19.119 17.292  55.876  1.00 41.08 ? 92  ASP B CG  1 
ATOM   1786 O OD1 . ASP B 1 92  ? -19.812 17.221  56.912  1.00 40.46 ? 92  ASP B OD1 1 
ATOM   1787 O OD2 . ASP B 1 92  ? -18.630 18.363  55.454  1.00 41.36 ? 92  ASP B OD2 1 
ATOM   1788 N N   . GLY B 1 93  ? -17.568 12.782  55.395  1.00 40.35 ? 93  GLY B N   1 
ATOM   1789 C CA  . GLY B 1 93  ? -17.207 11.554  54.677  1.00 40.47 ? 93  GLY B CA  1 
ATOM   1790 C C   . GLY B 1 93  ? -16.446 11.761  53.380  1.00 40.15 ? 93  GLY B C   1 
ATOM   1791 O O   . GLY B 1 93  ? -16.365 10.852  52.564  1.00 39.99 ? 93  GLY B O   1 
ATOM   1792 N N   . VAL B 1 94  ? -15.882 12.950  53.196  1.00 40.38 ? 94  VAL B N   1 
ATOM   1793 C CA  . VAL B 1 94  ? -15.147 13.296  51.980  1.00 40.58 ? 94  VAL B CA  1 
ATOM   1794 C C   . VAL B 1 94  ? -13.654 13.359  52.265  1.00 40.84 ? 94  VAL B C   1 
ATOM   1795 O O   . VAL B 1 94  ? -13.219 14.031  53.201  1.00 40.56 ? 94  VAL B O   1 
ATOM   1796 C CB  . VAL B 1 94  ? -15.587 14.662  51.425  1.00 40.49 ? 94  VAL B CB  1 
ATOM   1797 C CG1 . VAL B 1 94  ? -14.707 15.077  50.234  1.00 40.44 ? 94  VAL B CG1 1 
ATOM   1798 C CG2 . VAL B 1 94  ? -17.060 14.632  51.037  1.00 40.09 ? 94  VAL B CG2 1 
ATOM   1799 N N   . ALA B 1 95  ? -12.880 12.649  51.446  1.00 41.52 ? 95  ALA B N   1 
ATOM   1800 C CA  . ALA B 1 95  ? -11.422 12.649  51.521  1.00 41.82 ? 95  ALA B CA  1 
ATOM   1801 C C   . ALA B 1 95  ? -10.842 13.409  50.331  1.00 42.22 ? 95  ALA B C   1 
ATOM   1802 O O   . ALA B 1 95  ? -10.931 12.955  49.199  1.00 42.42 ? 95  ALA B O   1 
ATOM   1803 C CB  . ALA B 1 95  ? -10.902 11.225  51.546  1.00 41.71 ? 95  ALA B CB  1 
ATOM   1804 N N   . ASP B 1 96  ? -10.286 14.586  50.593  1.00 43.17 ? 96  ASP B N   1 
ATOM   1805 C CA  . ASP B 1 96  ? -9.537  15.334  49.592  1.00 43.34 ? 96  ASP B CA  1 
ATOM   1806 C C   . ASP B 1 96  ? -8.144  14.725  49.471  1.00 43.58 ? 96  ASP B C   1 
ATOM   1807 O O   . ASP B 1 96  ? -7.353  14.803  50.410  1.00 43.55 ? 96  ASP B O   1 
ATOM   1808 C CB  . ASP B 1 96  ? -9.414  16.801  50.008  1.00 43.77 ? 96  ASP B CB  1 
ATOM   1809 C CG  . ASP B 1 96  ? -8.529  17.606  49.062  1.00 45.04 ? 96  ASP B CG  1 
ATOM   1810 O OD1 . ASP B 1 96  ? -7.328  17.799  49.381  1.00 49.23 ? 96  ASP B OD1 1 
ATOM   1811 O OD2 . ASP B 1 96  ? -9.029  18.032  47.991  1.00 50.13 ? 96  ASP B OD2 1 
ATOM   1812 N N   . VAL B 1 97  ? -7.849  14.111  48.327  1.00 43.98 ? 97  VAL B N   1 
ATOM   1813 C CA  . VAL B 1 97  ? -6.551  13.455  48.110  1.00 43.87 ? 97  VAL B CA  1 
ATOM   1814 C C   . VAL B 1 97  ? -5.557  14.419  47.434  1.00 44.06 ? 97  VAL B C   1 
ATOM   1815 O O   . VAL B 1 97  ? -5.879  15.069  46.435  1.00 43.65 ? 97  VAL B O   1 
ATOM   1816 C CB  . VAL B 1 97  ? -6.718  12.161  47.305  1.00 43.97 ? 97  VAL B CB  1 
ATOM   1817 C CG1 . VAL B 1 97  ? -5.379  11.415  47.175  1.00 43.90 ? 97  VAL B CG1 1 
ATOM   1818 C CG2 . VAL B 1 97  ? -7.762  11.271  47.979  1.00 43.56 ? 97  VAL B CG2 1 
ATOM   1819 N N   . SER B 1 98  ? -4.371  14.537  48.030  1.00 44.41 ? 98  SER B N   1 
ATOM   1820 C CA  . SER B 1 98  ? -3.285  15.346  47.482  1.00 44.56 ? 98  SER B CA  1 
ATOM   1821 C C   . SER B 1 98  ? -1.930  14.762  47.912  1.00 44.81 ? 98  SER B C   1 
ATOM   1822 O O   . SER B 1 98  ? -1.363  15.143  48.940  1.00 44.58 ? 98  SER B O   1 
ATOM   1823 C CB  . SER B 1 98  ? -3.424  16.798  47.922  1.00 44.73 ? 98  SER B CB  1 
ATOM   1824 O OG  . SER B 1 98  ? -2.677  17.645  47.064  1.00 45.08 ? 98  SER B OG  1 
ATOM   1825 N N   . ILE B 1 99  ? -1.444  13.819  47.105  1.00 45.13 ? 99  ILE B N   1 
ATOM   1826 C CA  . ILE B 1 99  ? -0.259  13.020  47.387  1.00 45.15 ? 99  ILE B CA  1 
ATOM   1827 C C   . ILE B 1 99  ? 0.798   13.308  46.325  1.00 45.01 ? 99  ILE B C   1 
ATOM   1828 O O   . ILE B 1 99  ? 0.471   13.712  45.196  1.00 44.92 ? 99  ILE B O   1 
ATOM   1829 C CB  . ILE B 1 99  ? -0.608  11.506  47.331  1.00 45.35 ? 99  ILE B CB  1 
ATOM   1830 C CG1 . ILE B 1 99  ? -1.510  11.119  48.502  1.00 46.62 ? 99  ILE B CG1 1 
ATOM   1831 C CG2 . ILE B 1 99  ? 0.637   10.633  47.352  1.00 45.91 ? 99  ILE B CG2 1 
ATOM   1832 C CD1 . ILE B 1 99  ? -1.999  9.665   48.441  1.00 46.65 ? 99  ILE B CD1 1 
ATOM   1833 N N   . GLU B 1 100 ? 2.062   13.110  46.699  1.00 44.56 ? 100 GLU B N   1 
ATOM   1834 C CA  . GLU B 1 100 ? 3.162   13.027  45.750  1.00 44.15 ? 100 GLU B CA  1 
ATOM   1835 C C   . GLU B 1 100 ? 3.998   11.793  46.125  1.00 43.37 ? 100 GLU B C   1 
ATOM   1836 O O   . GLU B 1 100 ? 4.270   11.570  47.300  1.00 43.13 ? 100 GLU B O   1 
ATOM   1837 C CB  . GLU B 1 100 ? 3.984   14.315  45.789  1.00 44.45 ? 100 GLU B CB  1 
ATOM   1838 C CG  . GLU B 1 100 ? 4.955   14.447  44.644  1.00 45.21 ? 100 GLU B CG  1 
ATOM   1839 C CD  . GLU B 1 100 ? 5.842   15.671  44.762  1.00 46.39 ? 100 GLU B CD  1 
ATOM   1840 O OE1 . GLU B 1 100 ? 5.358   16.770  44.406  1.00 49.82 ? 100 GLU B OE1 1 
ATOM   1841 O OE2 . GLU B 1 100 ? 7.025   15.532  45.188  1.00 48.05 ? 100 GLU B OE2 1 
ATOM   1842 N N   . ASP B 1 101 ? 4.374   10.985  45.134  1.00 42.61 ? 101 ASP B N   1 
ATOM   1843 C CA  . ASP B 1 101 ? 5.089   9.724   45.372  1.00 42.27 ? 101 ASP B CA  1 
ATOM   1844 C C   . ASP B 1 101 ? 6.170   9.436   44.313  1.00 41.66 ? 101 ASP B C   1 
ATOM   1845 O O   . ASP B 1 101 ? 5.959   9.628   43.114  1.00 41.34 ? 101 ASP B O   1 
ATOM   1846 C CB  . ASP B 1 101 ? 4.096   8.560   45.411  1.00 42.22 ? 101 ASP B CB  1 
ATOM   1847 C CG  . ASP B 1 101 ? 4.673   7.317   46.081  1.00 42.75 ? 101 ASP B CG  1 
ATOM   1848 O OD1 . ASP B 1 101 ? 4.754   7.306   47.324  1.00 42.48 ? 101 ASP B OD1 1 
ATOM   1849 O OD2 . ASP B 1 101 ? 5.035   6.354   45.370  1.00 42.18 ? 101 ASP B OD2 1 
ATOM   1850 N N   . SER B 1 102 ? 7.325   8.964   44.776  1.00 41.08 ? 102 SER B N   1 
ATOM   1851 C CA  . SER B 1 102 ? 8.461   8.718   43.918  1.00 40.54 ? 102 SER B CA  1 
ATOM   1852 C C   . SER B 1 102 ? 8.763   7.235   43.771  1.00 40.12 ? 102 SER B C   1 
ATOM   1853 O O   . SER B 1 102 ? 9.769   6.867   43.178  1.00 40.10 ? 102 SER B O   1 
ATOM   1854 C CB  . SER B 1 102 ? 9.682   9.453   44.463  1.00 40.83 ? 102 SER B CB  1 
ATOM   1855 O OG  . SER B 1 102 ? 9.537   10.854  44.286  1.00 41.54 ? 102 SER B OG  1 
ATOM   1856 N N   . VAL B 1 103 ? 7.893   6.375   44.284  1.00 39.55 ? 103 VAL B N   1 
ATOM   1857 C CA  . VAL B 1 103 ? 8.061   4.933   44.087  1.00 39.46 ? 103 VAL B CA  1 
ATOM   1858 C C   . VAL B 1 103 ? 7.198   4.465   42.915  1.00 39.17 ? 103 VAL B C   1 
ATOM   1859 O O   . VAL B 1 103 ? 7.666   3.723   42.055  1.00 38.67 ? 103 VAL B O   1 
ATOM   1860 C CB  . VAL B 1 103 ? 7.763   4.145   45.375  1.00 39.07 ? 103 VAL B CB  1 
ATOM   1861 C CG1 . VAL B 1 103 ? 7.858   2.632   45.141  1.00 39.24 ? 103 VAL B CG1 1 
ATOM   1862 C CG2 . VAL B 1 103 ? 8.740   4.561   46.455  1.00 39.18 ? 103 VAL B CG2 1 
ATOM   1863 N N   . ILE B 1 104 ? 5.946   4.910   42.882  1.00 39.08 ? 104 ILE B N   1 
ATOM   1864 C CA  . ILE B 1 104 ? 5.067   4.591   41.765  1.00 39.35 ? 104 ILE B CA  1 
ATOM   1865 C C   . ILE B 1 104 ? 5.515   5.332   40.504  1.00 39.49 ? 104 ILE B C   1 
ATOM   1866 O O   . ILE B 1 104 ? 6.085   6.431   40.586  1.00 39.23 ? 104 ILE B O   1 
ATOM   1867 C CB  . ILE B 1 104 ? 3.585   4.893   42.083  1.00 39.21 ? 104 ILE B CB  1 
ATOM   1868 C CG1 . ILE B 1 104 ? 3.349   6.387   42.350  1.00 39.91 ? 104 ILE B CG1 1 
ATOM   1869 C CG2 . ILE B 1 104 ? 3.137   4.087   43.286  1.00 39.42 ? 104 ILE B CG2 1 
ATOM   1870 C CD1 . ILE B 1 104 ? 1.891   6.760   42.370  1.00 39.91 ? 104 ILE B CD1 1 
ATOM   1871 N N   . SER B 1 105 ? 5.292   4.715   39.344  1.00 39.42 ? 105 SER B N   1 
ATOM   1872 C CA  . SER B 1 105 ? 5.484   5.408   38.067  1.00 39.45 ? 105 SER B CA  1 
ATOM   1873 C C   . SER B 1 105 ? 4.315   5.146   37.135  1.00 39.13 ? 105 SER B C   1 
ATOM   1874 O O   . SER B 1 105 ? 3.635   4.138   37.246  1.00 39.33 ? 105 SER B O   1 
ATOM   1875 C CB  . SER B 1 105 ? 6.798   5.003   37.384  1.00 39.30 ? 105 SER B CB  1 
ATOM   1876 O OG  . SER B 1 105 ? 7.171   5.965   36.403  1.00 39.61 ? 105 SER B OG  1 
ATOM   1877 N N   . LEU B 1 106 ? 4.085   6.086   36.229  1.00 39.17 ? 106 LEU B N   1 
ATOM   1878 C CA  . LEU B 1 106 ? 3.088   5.938   35.184  1.00 39.45 ? 106 LEU B CA  1 
ATOM   1879 C C   . LEU B 1 106 ? 3.695   5.335   33.916  1.00 39.67 ? 106 LEU B C   1 
ATOM   1880 O O   . LEU B 1 106 ? 2.973   5.086   32.957  1.00 39.62 ? 106 LEU B O   1 
ATOM   1881 C CB  . LEU B 1 106 ? 2.452   7.299   34.869  1.00 39.39 ? 106 LEU B CB  1 
ATOM   1882 C CG  . LEU B 1 106 ? 1.681   7.987   35.997  1.00 39.12 ? 106 LEU B CG  1 
ATOM   1883 C CD1 . LEU B 1 106 ? 0.949   9.191   35.466  1.00 39.07 ? 106 LEU B CD1 1 
ATOM   1884 C CD2 . LEU B 1 106 ? 0.685   7.003   36.614  1.00 41.19 ? 106 LEU B CD2 1 
ATOM   1885 N N   . SER B 1 107 ? 5.010   5.093   33.916  1.00 40.11 ? 107 SER B N   1 
ATOM   1886 C CA  . SER B 1 107 ? 5.702   4.473   32.773  1.00 40.32 ? 107 SER B CA  1 
ATOM   1887 C C   . SER B 1 107 ? 6.760   3.450   33.209  1.00 40.32 ? 107 SER B C   1 
ATOM   1888 O O   . SER B 1 107 ? 7.080   3.322   34.388  1.00 39.95 ? 107 SER B O   1 
ATOM   1889 C CB  . SER B 1 107 ? 6.331   5.556   31.871  1.00 40.74 ? 107 SER B CB  1 
ATOM   1890 O OG  . SER B 1 107 ? 6.964   6.592   32.626  1.00 42.00 ? 107 SER B OG  1 
ATOM   1891 N N   . GLY B 1 108 ? 7.285   2.711   32.240  1.00 40.61 ? 108 GLY B N   1 
ATOM   1892 C CA  . GLY B 1 108 ? 8.326   1.716   32.483  1.00 40.89 ? 108 GLY B CA  1 
ATOM   1893 C C   . GLY B 1 108 ? 7.741   0.357   32.769  1.00 41.10 ? 108 GLY B C   1 
ATOM   1894 O O   . GLY B 1 108 ? 6.539   0.161   32.655  1.00 41.23 ? 108 GLY B O   1 
ATOM   1895 N N   . ASP B 1 109 ? 8.595   -0.580  33.154  1.00 41.64 ? 109 ASP B N   1 
ATOM   1896 C CA  . ASP B 1 109 ? 8.179   -1.969  33.365  1.00 41.88 ? 109 ASP B CA  1 
ATOM   1897 C C   . ASP B 1 109 ? 7.199   -2.135  34.509  1.00 41.45 ? 109 ASP B C   1 
ATOM   1898 O O   . ASP B 1 109 ? 6.357   -3.029  34.471  1.00 41.48 ? 109 ASP B O   1 
ATOM   1899 C CB  . ASP B 1 109 ? 9.396   -2.872  33.633  1.00 42.41 ? 109 ASP B CB  1 
ATOM   1900 C CG  . ASP B 1 109 ? 10.165  -3.205  32.379  1.00 43.69 ? 109 ASP B CG  1 
ATOM   1901 O OD1 . ASP B 1 109 ? 9.718   -2.811  31.275  1.00 46.74 ? 109 ASP B OD1 1 
ATOM   1902 O OD2 . ASP B 1 109 ? 11.223  -3.870  32.495  1.00 43.87 ? 109 ASP B OD2 1 
ATOM   1903 N N   . HIS B 1 110 ? 7.328   -1.297  35.534  1.00 41.14 ? 110 HIS B N   1 
ATOM   1904 C CA  . HIS B 1 110 ? 6.490   -1.394  36.733  1.00 40.46 ? 110 HIS B CA  1 
ATOM   1905 C C   . HIS B 1 110 ? 5.495   -0.226  36.820  1.00 39.79 ? 110 HIS B C   1 
ATOM   1906 O O   . HIS B 1 110 ? 5.146   0.232   37.911  1.00 39.48 ? 110 HIS B O   1 
ATOM   1907 C CB  . HIS B 1 110 ? 7.371   -1.458  37.983  1.00 40.37 ? 110 HIS B CB  1 
ATOM   1908 C CG  . HIS B 1 110 ? 8.280   -2.644  38.017  1.00 40.57 ? 110 HIS B CG  1 
ATOM   1909 N ND1 . HIS B 1 110 ? 9.627   -2.544  38.294  1.00 40.80 ? 110 HIS B ND1 1 
ATOM   1910 C CD2 . HIS B 1 110 ? 8.037   -3.958  37.796  1.00 40.22 ? 110 HIS B CD2 1 
ATOM   1911 C CE1 . HIS B 1 110 ? 10.173  -3.748  38.249  1.00 40.45 ? 110 HIS B CE1 1 
ATOM   1912 N NE2 . HIS B 1 110 ? 9.230   -4.623  37.950  1.00 40.27 ? 110 HIS B NE2 1 
ATOM   1913 N N   . ALA B 1 111 ? 5.038   0.235   35.660  1.00 39.20 ? 111 ALA B N   1 
ATOM   1914 C CA  . ALA B 1 111 ? 3.989   1.249   35.566  1.00 38.81 ? 111 ALA B CA  1 
ATOM   1915 C C   . ALA B 1 111 ? 2.713   0.764   36.241  1.00 38.46 ? 111 ALA B C   1 
ATOM   1916 O O   . ALA B 1 111 ? 2.381   -0.422  36.177  1.00 37.93 ? 111 ALA B O   1 
ATOM   1917 C CB  . ALA B 1 111 ? 3.707   1.555   34.119  1.00 38.79 ? 111 ALA B CB  1 
ATOM   1918 N N   . ILE B 1 112 ? 2.010   1.678   36.895  1.00 38.38 ? 112 ILE B N   1 
ATOM   1919 C CA  . ILE B 1 112 ? 0.744   1.347   37.557  1.00 38.39 ? 112 ILE B CA  1 
ATOM   1920 C C   . ILE B 1 112 ? -0.453  1.487   36.615  1.00 38.48 ? 112 ILE B C   1 
ATOM   1921 O O   . ILE B 1 112 ? -1.562  1.080   36.961  1.00 38.23 ? 112 ILE B O   1 
ATOM   1922 C CB  . ILE B 1 112 ? 0.507   2.181   38.846  1.00 38.38 ? 112 ILE B CB  1 
ATOM   1923 C CG1 . ILE B 1 112 ? 0.385   3.676   38.536  1.00 38.47 ? 112 ILE B CG1 1 
ATOM   1924 C CG2 . ILE B 1 112 ? 1.643   1.931   39.848  1.00 38.72 ? 112 ILE B CG2 1 
ATOM   1925 C CD1 . ILE B 1 112 ? -0.023  4.538   39.724  1.00 38.19 ? 112 ILE B CD1 1 
ATOM   1926 N N   . ILE B 1 113 ? -0.235  2.077   35.436  1.00 38.39 ? 113 ILE B N   1 
ATOM   1927 C CA  . ILE B 1 113 ? -1.278  2.154   34.429  1.00 38.23 ? 113 ILE B CA  1 
ATOM   1928 C C   . ILE B 1 113 ? -1.708  0.732   34.111  1.00 37.96 ? 113 ILE B C   1 
ATOM   1929 O O   . ILE B 1 113 ? -0.877  -0.125  33.842  1.00 38.20 ? 113 ILE B O   1 
ATOM   1930 C CB  . ILE B 1 113 ? -0.826  2.939   33.174  1.00 38.15 ? 113 ILE B CB  1 
ATOM   1931 C CG1 . ILE B 1 113 ? -0.914  4.444   33.472  1.00 38.77 ? 113 ILE B CG1 1 
ATOM   1932 C CG2 . ILE B 1 113 ? -1.692  2.597   31.958  1.00 38.54 ? 113 ILE B CG2 1 
ATOM   1933 C CD1 . ILE B 1 113 ? -0.446  5.344   32.343  1.00 39.20 ? 113 ILE B CD1 1 
ATOM   1934 N N   . GLY B 1 114 ? -3.013  0.482   34.179  1.00 37.89 ? 114 GLY B N   1 
ATOM   1935 C CA  . GLY B 1 114 ? -3.556  -0.866  34.003  1.00 37.38 ? 114 GLY B CA  1 
ATOM   1936 C C   . GLY B 1 114 ? -3.703  -1.652  35.299  1.00 37.14 ? 114 GLY B C   1 
ATOM   1937 O O   . GLY B 1 114 ? -4.194  -2.774  35.285  1.00 36.04 ? 114 GLY B O   1 
ATOM   1938 N N   . ARG B 1 115 ? -3.270  -1.068  36.418  1.00 37.29 ? 115 ARG B N   1 
ATOM   1939 C CA  . ARG B 1 115 ? -3.435  -1.687  37.729  1.00 37.75 ? 115 ARG B CA  1 
ATOM   1940 C C   . ARG B 1 115 ? -4.682  -1.097  38.377  1.00 38.08 ? 115 ARG B C   1 
ATOM   1941 O O   . ARG B 1 115 ? -5.310  -0.205  37.811  1.00 38.38 ? 115 ARG B O   1 
ATOM   1942 C CB  . ARG B 1 115 ? -2.205  -1.439  38.613  1.00 37.48 ? 115 ARG B CB  1 
ATOM   1943 C CG  . ARG B 1 115 ? -0.867  -1.766  37.978  1.00 37.65 ? 115 ARG B CG  1 
ATOM   1944 C CD  . ARG B 1 115 ? -0.684  -3.252  37.840  1.00 37.80 ? 115 ARG B CD  1 
ATOM   1945 N NE  . ARG B 1 115 ? 0.576   -3.585  37.177  1.00 38.04 ? 115 ARG B NE  1 
ATOM   1946 C CZ  . ARG B 1 115 ? 1.011   -4.828  36.980  1.00 38.39 ? 115 ARG B CZ  1 
ATOM   1947 N NH1 . ARG B 1 115 ? 0.295   -5.867  37.398  1.00 37.67 ? 115 ARG B NH1 1 
ATOM   1948 N NH2 . ARG B 1 115 ? 2.166   -5.038  36.362  1.00 38.80 ? 115 ARG B NH2 1 
ATOM   1949 N N   . THR B 1 116 ? -5.032  -1.584  39.565  1.00 38.35 ? 116 THR B N   1 
ATOM   1950 C CA  . THR B 1 116 ? -6.260  -1.150  40.247  1.00 38.46 ? 116 THR B CA  1 
ATOM   1951 C C   . THR B 1 116 ? -5.950  -0.299  41.482  1.00 38.85 ? 116 THR B C   1 
ATOM   1952 O O   . THR B 1 116 ? -5.213  -0.730  42.363  1.00 39.33 ? 116 THR B O   1 
ATOM   1953 C CB  . THR B 1 116 ? -7.111  -2.377  40.646  1.00 38.72 ? 116 THR B CB  1 
ATOM   1954 O OG1 . THR B 1 116 ? -7.500  -3.091  39.463  1.00 38.71 ? 116 THR B OG1 1 
ATOM   1955 C CG2 . THR B 1 116 ? -8.363  -1.977  41.397  1.00 38.71 ? 116 THR B CG2 1 
ATOM   1956 N N   . LEU B 1 117 ? -6.515  0.908   41.532  1.00 38.66 ? 117 LEU B N   1 
ATOM   1957 C CA  . LEU B 1 117 ? -6.504  1.725   42.732  1.00 38.62 ? 117 LEU B CA  1 
ATOM   1958 C C   . LEU B 1 117 ? -7.706  1.370   43.602  1.00 38.57 ? 117 LEU B C   1 
ATOM   1959 O O   . LEU B 1 117 ? -8.837  1.321   43.122  1.00 38.26 ? 117 LEU B O   1 
ATOM   1960 C CB  . LEU B 1 117 ? -6.558  3.209   42.376  1.00 38.85 ? 117 LEU B CB  1 
ATOM   1961 C CG  . LEU B 1 117 ? -6.366  4.216   43.520  1.00 39.07 ? 117 LEU B CG  1 
ATOM   1962 C CD1 . LEU B 1 117 ? -4.956  4.153   44.110  1.00 40.24 ? 117 LEU B CD1 1 
ATOM   1963 C CD2 . LEU B 1 117 ? -6.656  5.605   43.022  1.00 39.39 ? 117 LEU B CD2 1 
ATOM   1964 N N   . VAL B 1 118 ? -7.450  1.147   44.886  1.00 38.43 ? 118 VAL B N   1 
ATOM   1965 C CA  . VAL B 1 118 ? -8.465  0.683   45.813  1.00 38.48 ? 118 VAL B CA  1 
ATOM   1966 C C   . VAL B 1 118 ? -8.455  1.503   47.083  1.00 38.33 ? 118 VAL B C   1 
ATOM   1967 O O   . VAL B 1 118 ? -7.398  1.724   47.684  1.00 38.15 ? 118 VAL B O   1 
ATOM   1968 C CB  . VAL B 1 118 ? -8.247  -0.788  46.212  1.00 38.20 ? 118 VAL B CB  1 
ATOM   1969 C CG1 . VAL B 1 118 ? -9.312  -1.223  47.206  1.00 38.48 ? 118 VAL B CG1 1 
ATOM   1970 C CG2 . VAL B 1 118 ? -8.277  -1.683  44.993  1.00 38.95 ? 118 VAL B CG2 1 
ATOM   1971 N N   . VAL B 1 119 ? -9.647  1.939   47.483  1.00 38.51 ? 119 VAL B N   1 
ATOM   1972 C CA  . VAL B 1 119 ? -9.844  2.571   48.770  1.00 38.64 ? 119 VAL B CA  1 
ATOM   1973 C C   . VAL B 1 119 ? -10.455 1.518   49.687  1.00 38.79 ? 119 VAL B C   1 
ATOM   1974 O O   . VAL B 1 119 ? -11.400 0.819   49.305  1.00 38.18 ? 119 VAL B O   1 
ATOM   1975 C CB  . VAL B 1 119 ? -10.687 3.869   48.659  1.00 38.77 ? 119 VAL B CB  1 
ATOM   1976 C CG1 . VAL B 1 119 ? -12.105 3.582   48.196  1.00 38.56 ? 119 VAL B CG1 1 
ATOM   1977 C CG2 . VAL B 1 119 ? -10.671 4.631   49.985  1.00 38.96 ? 119 VAL B CG2 1 
ATOM   1978 N N   . HIS B 1 120 ? -9.882  1.383   50.881  1.00 38.98 ? 120 HIS B N   1 
ATOM   1979 C CA  . HIS B 1 120 ? -10.209 0.272   51.771  1.00 39.20 ? 120 HIS B CA  1 
ATOM   1980 C C   . HIS B 1 120 ? -11.097 0.664   52.943  1.00 39.43 ? 120 HIS B C   1 
ATOM   1981 O O   . HIS B 1 120 ? -11.200 1.839   53.313  1.00 39.22 ? 120 HIS B O   1 
ATOM   1982 C CB  . HIS B 1 120 ? -8.932  -0.397  52.301  1.00 39.16 ? 120 HIS B CB  1 
ATOM   1983 C CG  . HIS B 1 120 ? -8.213  -1.228  51.281  1.00 39.06 ? 120 HIS B CG  1 
ATOM   1984 N ND1 . HIS B 1 120 ? -8.417  -2.585  51.146  1.00 38.48 ? 120 HIS B ND1 1 
ATOM   1985 C CD2 . HIS B 1 120 ? -7.289  -0.891  50.350  1.00 38.90 ? 120 HIS B CD2 1 
ATOM   1986 C CE1 . HIS B 1 120 ? -7.652  -3.047  50.173  1.00 38.87 ? 120 HIS B CE1 1 
ATOM   1987 N NE2 . HIS B 1 120 ? -6.956  -2.040  49.677  1.00 39.44 ? 120 HIS B NE2 1 
ATOM   1988 N N   . GLU B 1 121 ? -11.718 -0.373  53.509  1.00 39.75 ? 121 GLU B N   1 
ATOM   1989 C CA  . GLU B 1 121 ? -12.654 -0.305  54.632  1.00 39.75 ? 121 GLU B CA  1 
ATOM   1990 C C   . GLU B 1 121 ? -12.116 0.454   55.837  1.00 39.85 ? 121 GLU B C   1 
ATOM   1991 O O   . GLU B 1 121 ? -12.838 1.231   56.459  1.00 39.70 ? 121 GLU B O   1 
ATOM   1992 C CB  . GLU B 1 121 ? -12.989 -1.730  55.075  1.00 39.73 ? 121 GLU B CB  1 
ATOM   1993 C CG  . GLU B 1 121 ? -14.046 -1.830  56.151  1.00 40.03 ? 121 GLU B CG  1 
ATOM   1994 C CD  . GLU B 1 121 ? -14.092 -3.198  56.813  1.00 40.21 ? 121 GLU B CD  1 
ATOM   1995 O OE1 . GLU B 1 121 ? -13.383 -4.125  56.356  1.00 41.11 ? 121 GLU B OE1 1 
ATOM   1996 O OE2 . GLU B 1 121 ? -14.840 -3.339  57.803  1.00 41.03 ? 121 GLU B OE2 1 
ATOM   1997 N N   . LYS B 1 122 ? -10.860 0.201   56.187  1.00 39.80 ? 122 LYS B N   1 
ATOM   1998 C CA  . LYS B 1 122 ? -10.272 0.843   57.351  1.00 39.95 ? 122 LYS B CA  1 
ATOM   1999 C C   . LYS B 1 122 ? -8.837  1.251   57.108  1.00 39.82 ? 122 LYS B C   1 
ATOM   2000 O O   . LYS B 1 122 ? -8.278  1.000   56.044  1.00 39.60 ? 122 LYS B O   1 
ATOM   2001 C CB  . LYS B 1 122 ? -10.407 -0.036  58.604  1.00 40.23 ? 122 LYS B CB  1 
ATOM   2002 C CG  . LYS B 1 122 ? -10.384 -1.538  58.372  1.00 40.48 ? 122 LYS B CG  1 
ATOM   2003 C CD  . LYS B 1 122 ? -10.723 -2.274  59.650  1.00 40.20 ? 122 LYS B CD  1 
ATOM   2004 C CE  . LYS B 1 122 ? -10.957 -3.747  59.392  1.00 41.17 ? 122 LYS B CE  1 
ATOM   2005 N NZ  . LYS B 1 122 ? -11.368 -4.467  60.636  1.00 40.88 ? 122 LYS B NZ  1 
ATOM   2006 N N   . ALA B 1 123 ? -8.277  1.924   58.103  1.00 39.77 ? 123 ALA B N   1 
ATOM   2007 C CA  . ALA B 1 123 ? -6.926  2.452   58.041  1.00 39.82 ? 123 ALA B CA  1 
ATOM   2008 C C   . ALA B 1 123 ? -5.877  1.371   57.803  1.00 39.77 ? 123 ALA B C   1 
ATOM   2009 O O   . ALA B 1 123 ? -5.961  0.255   58.311  1.00 39.91 ? 123 ALA B O   1 
ATOM   2010 C CB  . ALA B 1 123 ? -6.599  3.209   59.328  1.00 39.89 ? 123 ALA B CB  1 
ATOM   2011 N N   . ASP B 1 124 ? -4.889  1.735   57.003  1.00 39.78 ? 124 ASP B N   1 
ATOM   2012 C CA  . ASP B 1 124 ? -3.670  0.966   56.845  1.00 39.49 ? 124 ASP B CA  1 
ATOM   2013 C C   . ASP B 1 124 ? -2.853  1.203   58.127  1.00 39.14 ? 124 ASP B C   1 
ATOM   2014 O O   . ASP B 1 124 ? -2.644  2.352   58.523  1.00 38.91 ? 124 ASP B O   1 
ATOM   2015 C CB  . ASP B 1 124 ? -2.956  1.486   55.593  1.00 39.56 ? 124 ASP B CB  1 
ATOM   2016 C CG  . ASP B 1 124 ? -1.682  0.740   55.265  1.00 39.61 ? 124 ASP B CG  1 
ATOM   2017 O OD1 . ASP B 1 124 ? -1.187  -0.058  56.079  1.00 39.26 ? 124 ASP B OD1 1 
ATOM   2018 O OD2 . ASP B 1 124 ? -1.156  0.987   54.166  1.00 39.85 ? 124 ASP B OD2 1 
ATOM   2019 N N   . ASP B 1 125 ? -2.418  0.128   58.786  1.00 38.87 ? 125 ASP B N   1 
ATOM   2020 C CA  . ASP B 1 125 ? -1.566  0.252   59.987  1.00 38.54 ? 125 ASP B CA  1 
ATOM   2021 C C   . ASP B 1 125 ? -0.074  0.445   59.658  1.00 38.31 ? 125 ASP B C   1 
ATOM   2022 O O   . ASP B 1 125 ? 0.756   0.577   60.564  1.00 37.86 ? 125 ASP B O   1 
ATOM   2023 C CB  . ASP B 1 125 ? -1.783  -0.926  60.955  1.00 38.73 ? 125 ASP B CB  1 
ATOM   2024 C CG  . ASP B 1 125 ? -1.287  -2.270  60.412  1.00 38.78 ? 125 ASP B CG  1 
ATOM   2025 O OD1 . ASP B 1 125 ? -0.374  -2.301  59.561  1.00 38.72 ? 125 ASP B OD1 1 
ATOM   2026 O OD2 . ASP B 1 125 ? -1.818  -3.310  60.864  1.00 38.24 ? 125 ASP B OD2 1 
ATOM   2027 N N   . LEU B 1 126 ? 0.240   0.461   58.358  1.00 38.00 ? 126 LEU B N   1 
ATOM   2028 C CA  . LEU B 1 126 ? 1.581   0.751   57.822  1.00 37.75 ? 126 LEU B CA  1 
ATOM   2029 C C   . LEU B 1 126 ? 2.638   -0.294  58.200  1.00 37.52 ? 126 LEU B C   1 
ATOM   2030 O O   . LEU B 1 126 ? 3.828   0.000   58.230  1.00 37.35 ? 126 LEU B O   1 
ATOM   2031 C CB  . LEU B 1 126 ? 2.034   2.165   58.213  1.00 37.72 ? 126 LEU B CB  1 
ATOM   2032 C CG  . LEU B 1 126 ? 1.027   3.309   58.027  1.00 37.74 ? 126 LEU B CG  1 
ATOM   2033 C CD1 . LEU B 1 126 ? 1.671   4.659   58.369  1.00 38.29 ? 126 LEU B CD1 1 
ATOM   2034 C CD2 . LEU B 1 126 ? 0.463   3.346   56.626  1.00 37.52 ? 126 LEU B CD2 1 
ATOM   2035 N N   . GLY B 1 127 ? 2.196   -1.521  58.461  1.00 37.46 ? 127 GLY B N   1 
ATOM   2036 C CA  . GLY B 1 127 ? 3.100   -2.608  58.830  1.00 37.38 ? 127 GLY B CA  1 
ATOM   2037 C C   . GLY B 1 127 ? 3.438   -2.654  60.308  1.00 37.37 ? 127 GLY B C   1 
ATOM   2038 O O   . GLY B 1 127 ? 4.167   -3.541  60.746  1.00 36.92 ? 127 GLY B O   1 
ATOM   2039 N N   . LYS B 1 128 ? 2.890   -1.714  61.082  1.00 37.55 ? 128 LYS B N   1 
ATOM   2040 C CA  . LYS B 1 128 ? 3.207   -1.587  62.505  1.00 37.47 ? 128 LYS B CA  1 
ATOM   2041 C C   . LYS B 1 128 ? 2.025   -2.024  63.365  1.00 37.24 ? 128 LYS B C   1 
ATOM   2042 O O   . LYS B 1 128 ? 1.782   -1.461  64.436  1.00 37.18 ? 128 LYS B O   1 
ATOM   2043 C CB  . LYS B 1 128 ? 3.600   -0.139  62.828  1.00 37.89 ? 128 LYS B CB  1 
ATOM   2044 C CG  . LYS B 1 128 ? 4.765   0.403   61.997  1.00 38.55 ? 128 LYS B CG  1 
ATOM   2045 C CD  . LYS B 1 128 ? 6.114   -0.193  62.398  1.00 39.94 ? 128 LYS B CD  1 
ATOM   2046 C CE  . LYS B 1 128 ? 7.194   0.056   61.324  1.00 39.82 ? 128 LYS B CE  1 
ATOM   2047 N NZ  . LYS B 1 128 ? 7.013   -0.805  60.105  1.00 40.83 ? 128 LYS B NZ  1 
ATOM   2048 N N   . GLY B 1 129 ? 1.315   -3.053  62.902  1.00 36.79 ? 129 GLY B N   1 
ATOM   2049 C CA  . GLY B 1 129 ? 0.086   -3.511  63.539  1.00 36.58 ? 129 GLY B CA  1 
ATOM   2050 C C   . GLY B 1 129 ? 0.252   -4.668  64.499  1.00 36.29 ? 129 GLY B C   1 
ATOM   2051 O O   . GLY B 1 129 ? -0.664  -4.969  65.258  1.00 36.09 ? 129 GLY B O   1 
ATOM   2052 N N   . GLY B 1 130 ? 1.408   -5.328  64.455  1.00 36.18 ? 130 GLY B N   1 
ATOM   2053 C CA  . GLY B 1 130 ? 1.761   -6.355  65.438  1.00 36.18 ? 130 GLY B CA  1 
ATOM   2054 C C   . GLY B 1 130 ? 1.249   -7.760  65.170  1.00 36.11 ? 130 GLY B C   1 
ATOM   2055 O O   . GLY B 1 130 ? 1.144   -8.559  66.098  1.00 35.70 ? 130 GLY B O   1 
ATOM   2056 N N   . ASN B 1 131 ? 0.922   -8.060  63.912  1.00 36.33 ? 131 ASN B N   1 
ATOM   2057 C CA  . ASN B 1 131 ? 0.585   -9.425  63.485  1.00 36.75 ? 131 ASN B CA  1 
ATOM   2058 C C   . ASN B 1 131 ? 1.070   -9.674  62.051  1.00 37.22 ? 131 ASN B C   1 
ATOM   2059 O O   . ASN B 1 131 ? 1.656   -8.780  61.441  1.00 36.75 ? 131 ASN B O   1 
ATOM   2060 C CB  . ASN B 1 131 ? -0.920  -9.695  63.635  1.00 36.59 ? 131 ASN B CB  1 
ATOM   2061 C CG  . ASN B 1 131 ? -1.793  -8.677  62.902  1.00 36.07 ? 131 ASN B CG  1 
ATOM   2062 O OD1 . ASN B 1 131 ? -1.435  -8.166  61.848  1.00 34.72 ? 131 ASN B OD1 1 
ATOM   2063 N ND2 . ASN B 1 131 ? -2.961  -8.402  63.464  1.00 36.12 ? 131 ASN B ND2 1 
ATOM   2064 N N   . GLU B 1 132 ? 0.841   -10.876 61.519  1.00 37.95 ? 132 GLU B N   1 
ATOM   2065 C CA  . GLU B 1 132 ? 1.346   -11.220 60.183  1.00 38.48 ? 132 GLU B CA  1 
ATOM   2066 C C   . GLU B 1 132 ? 0.638   -10.453 59.061  1.00 38.68 ? 132 GLU B C   1 
ATOM   2067 O O   . GLU B 1 132 ? 1.284   -9.964  58.138  1.00 38.63 ? 132 GLU B O   1 
ATOM   2068 C CB  . GLU B 1 132 ? 1.283   -12.734 59.923  1.00 38.71 ? 132 GLU B CB  1 
ATOM   2069 C CG  . GLU B 1 132 ? 1.649   -13.108 58.471  1.00 38.96 ? 132 GLU B CG  1 
ATOM   2070 C CD  . GLU B 1 132 ? 2.453   -14.399 58.342  1.00 39.54 ? 132 GLU B CD  1 
ATOM   2071 O OE1 . GLU B 1 132 ? 2.085   -15.414 58.971  1.00 41.05 ? 132 GLU B OE1 1 
ATOM   2072 O OE2 . GLU B 1 132 ? 3.456   -14.394 57.589  1.00 40.76 ? 132 GLU B OE2 1 
ATOM   2073 N N   . GLU B 1 133 ? -0.682  -10.345 59.145  1.00 39.09 ? 133 GLU B N   1 
ATOM   2074 C CA  . GLU B 1 133 ? -1.454  -9.635  58.131  1.00 39.33 ? 133 GLU B CA  1 
ATOM   2075 C C   . GLU B 1 133 ? -1.003  -8.178  58.009  1.00 39.50 ? 133 GLU B C   1 
ATOM   2076 O O   . GLU B 1 133 ? -1.104  -7.577  56.937  1.00 39.30 ? 133 GLU B O   1 
ATOM   2077 C CB  . GLU B 1 133 ? -2.948  -9.699  58.468  1.00 39.68 ? 133 GLU B CB  1 
ATOM   2078 C CG  . GLU B 1 133 ? -3.878  -9.163  57.390  1.00 39.80 ? 133 GLU B CG  1 
ATOM   2079 C CD  . GLU B 1 133 ? -3.763  -9.929  56.084  1.00 41.52 ? 133 GLU B CD  1 
ATOM   2080 O OE1 . GLU B 1 133 ? -3.560  -11.166 56.126  1.00 43.48 ? 133 GLU B OE1 1 
ATOM   2081 O OE2 . GLU B 1 133 ? -3.877  -9.298  55.016  1.00 41.31 ? 133 GLU B OE2 1 
ATOM   2082 N N   . SER B 1 134 ? -0.498  -7.615  59.106  1.00 39.72 ? 134 SER B N   1 
ATOM   2083 C CA  . SER B 1 134 ? 0.008   -6.238  59.100  1.00 39.74 ? 134 SER B CA  1 
ATOM   2084 C C   . SER B 1 134 ? 1.104   -6.015  58.050  1.00 39.93 ? 134 SER B C   1 
ATOM   2085 O O   . SER B 1 134 ? 1.080   -5.016  57.323  1.00 39.57 ? 134 SER B O   1 
ATOM   2086 C CB  . SER B 1 134 ? 0.545   -5.857  60.477  1.00 39.65 ? 134 SER B CB  1 
ATOM   2087 O OG  . SER B 1 134 ? 0.861   -4.477  60.518  1.00 39.96 ? 134 SER B OG  1 
ATOM   2088 N N   . THR B 1 135 ? 2.054   -6.949  57.977  1.00 40.08 ? 135 THR B N   1 
ATOM   2089 C CA  . THR B 1 135 ? 3.181   -6.847  57.047  1.00 40.40 ? 135 THR B CA  1 
ATOM   2090 C C   . THR B 1 135 ? 2.845   -7.315  55.627  1.00 40.74 ? 135 THR B C   1 
ATOM   2091 O O   . THR B 1 135 ? 3.710   -7.295  54.747  1.00 41.05 ? 135 THR B O   1 
ATOM   2092 C CB  . THR B 1 135 ? 4.389   -7.650  57.548  1.00 40.26 ? 135 THR B CB  1 
ATOM   2093 O OG1 . THR B 1 135 ? 4.038   -9.034  57.657  1.00 40.14 ? 135 THR B OG1 1 
ATOM   2094 C CG2 . THR B 1 135 ? 4.851   -7.135  58.901  1.00 40.32 ? 135 THR B CG2 1 
ATOM   2095 N N   . LYS B 1 136 ? 1.596   -7.729  55.412  1.00 40.99 ? 136 LYS B N   1 
ATOM   2096 C CA  . LYS B 1 136 ? 1.107   -8.138  54.097  1.00 41.13 ? 136 LYS B CA  1 
ATOM   2097 C C   . LYS B 1 136 ? 0.186   -7.093  53.493  1.00 41.23 ? 136 LYS B C   1 
ATOM   2098 O O   . LYS B 1 136 ? 0.373   -6.706  52.343  1.00 41.32 ? 136 LYS B O   1 
ATOM   2099 C CB  . LYS B 1 136 ? 0.356   -9.464  54.197  1.00 41.23 ? 136 LYS B CB  1 
ATOM   2100 C CG  . LYS B 1 136 ? 1.259   -10.643 54.473  1.00 41.47 ? 136 LYS B CG  1 
ATOM   2101 C CD  . LYS B 1 136 ? 0.467   -11.915 54.721  1.00 41.69 ? 136 LYS B CD  1 
ATOM   2102 C CE  . LYS B 1 136 ? 1.402   -13.101 54.938  1.00 41.81 ? 136 LYS B CE  1 
ATOM   2103 N NZ  . LYS B 1 136 ? 0.715   -14.263 55.542  1.00 41.69 ? 136 LYS B NZ  1 
ATOM   2104 N N   . THR B 1 137 ? -0.812  -6.654  54.264  1.00 41.38 ? 137 THR B N   1 
ATOM   2105 C CA  . THR B 1 137 ? -1.821  -5.697  53.785  1.00 41.15 ? 137 THR B CA  1 
ATOM   2106 C C   . THR B 1 137 ? -2.020  -4.462  54.655  1.00 41.04 ? 137 THR B C   1 
ATOM   2107 O O   . THR B 1 137 ? -2.732  -3.536  54.253  1.00 40.98 ? 137 THR B O   1 
ATOM   2108 C CB  . THR B 1 137 ? -3.202  -6.374  53.665  1.00 41.72 ? 137 THR B CB  1 
ATOM   2109 O OG1 . THR B 1 137 ? -3.594  -6.926  54.938  1.00 42.08 ? 137 THR B OG1 1 
ATOM   2110 C CG2 . THR B 1 137 ? -3.164  -7.479  52.618  1.00 41.87 ? 137 THR B CG2 1 
ATOM   2111 N N   . GLY B 1 138 ? -1.424  -4.446  55.845  1.00 40.68 ? 138 GLY B N   1 
ATOM   2112 C CA  . GLY B 1 138 ? -1.653  -3.368  56.796  1.00 40.39 ? 138 GLY B CA  1 
ATOM   2113 C C   . GLY B 1 138 ? -3.023  -3.394  57.460  1.00 40.19 ? 138 GLY B C   1 
ATOM   2114 O O   . GLY B 1 138 ? -3.421  -2.419  58.091  1.00 40.14 ? 138 GLY B O   1 
ATOM   2115 N N   . ASN B 1 139 ? -3.741  -4.510  57.325  1.00 40.23 ? 139 ASN B N   1 
ATOM   2116 C CA  . ASN B 1 139 ? -5.062  -4.706  57.938  1.00 40.07 ? 139 ASN B CA  1 
ATOM   2117 C C   . ASN B 1 139 ? -6.100  -3.654  57.565  1.00 39.94 ? 139 ASN B C   1 
ATOM   2118 O O   . ASN B 1 139 ? -6.981  -3.337  58.363  1.00 40.14 ? 139 ASN B O   1 
ATOM   2119 C CB  . ASN B 1 139 ? -4.925  -4.787  59.462  1.00 40.03 ? 139 ASN B CB  1 
ATOM   2120 C CG  . ASN B 1 139 ? -4.192  -6.012  59.902  1.00 40.13 ? 139 ASN B CG  1 
ATOM   2121 O OD1 . ASN B 1 139 ? -4.709  -7.117  59.791  1.00 40.57 ? 139 ASN B OD1 1 
ATOM   2122 N ND2 . ASN B 1 139 ? -2.978  -5.832  60.410  1.00 40.60 ? 139 ASN B ND2 1 
ATOM   2123 N N   . ALA B 1 140 ? -6.006  -3.135  56.344  1.00 39.93 ? 140 ALA B N   1 
ATOM   2124 C CA  . ALA B 1 140 ? -6.901  -2.079  55.870  1.00 39.80 ? 140 ALA B CA  1 
ATOM   2125 C C   . ALA B 1 140 ? -8.306  -2.598  55.547  1.00 39.92 ? 140 ALA B C   1 
ATOM   2126 O O   . ALA B 1 140 ? -9.233  -1.811  55.327  1.00 39.76 ? 140 ALA B O   1 
ATOM   2127 C CB  . ALA B 1 140 ? -6.301  -1.408  54.658  1.00 39.90 ? 140 ALA B CB  1 
ATOM   2128 N N   . GLY B 1 141 ? -8.453  -3.920  55.497  1.00 39.71 ? 141 GLY B N   1 
ATOM   2129 C CA  . GLY B 1 141 ? -9.759  -4.537  55.394  1.00 39.81 ? 141 GLY B CA  1 
ATOM   2130 C C   . GLY B 1 141 ? -10.302 -4.566  53.985  1.00 39.95 ? 141 GLY B C   1 
ATOM   2131 O O   . GLY B 1 141 ? -9.552  -4.458  53.016  1.00 40.24 ? 141 GLY B O   1 
ATOM   2132 N N   . SER B 1 142 ? -11.619 -4.698  53.875  1.00 39.83 ? 142 SER B N   1 
ATOM   2133 C CA  . SER B 1 142 ? -12.258 -4.922  52.596  1.00 39.86 ? 142 SER B CA  1 
ATOM   2134 C C   . SER B 1 142 ? -12.138 -3.745  51.629  1.00 39.78 ? 142 SER B C   1 
ATOM   2135 O O   . SER B 1 142 ? -11.906 -2.607  52.017  1.00 39.93 ? 142 SER B O   1 
ATOM   2136 C CB  . SER B 1 142 ? -13.737 -5.277  52.794  1.00 40.11 ? 142 SER B CB  1 
ATOM   2137 O OG  . SER B 1 142 ? -14.480 -4.156  53.247  1.00 40.53 ? 142 SER B OG  1 
ATOM   2138 N N   . ARG B 1 143 ? -12.298 -4.057  50.352  1.00 39.82 ? 143 ARG B N   1 
ATOM   2139 C CA  . ARG B 1 143 ? -12.401 -3.061  49.302  1.00 39.48 ? 143 ARG B CA  1 
ATOM   2140 C C   . ARG B 1 143 ? -13.756 -2.359  49.354  1.00 38.89 ? 143 ARG B C   1 
ATOM   2141 O O   . ARG B 1 143 ? -14.792 -3.019  49.350  1.00 38.66 ? 143 ARG B O   1 
ATOM   2142 C CB  . ARG B 1 143 ? -12.222 -3.763  47.965  1.00 39.71 ? 143 ARG B CB  1 
ATOM   2143 C CG  . ARG B 1 143 ? -12.879 -3.103  46.774  1.00 40.35 ? 143 ARG B CG  1 
ATOM   2144 C CD  . ARG B 1 143 ? -12.795 -4.037  45.611  1.00 40.76 ? 143 ARG B CD  1 
ATOM   2145 N NE  . ARG B 1 143 ? -13.491 -3.533  44.445  1.00 41.51 ? 143 ARG B NE  1 
ATOM   2146 C CZ  . ARG B 1 143 ? -13.585 -4.197  43.297  1.00 42.56 ? 143 ARG B CZ  1 
ATOM   2147 N NH1 . ARG B 1 143 ? -13.031 -5.404  43.176  1.00 43.12 ? 143 ARG B NH1 1 
ATOM   2148 N NH2 . ARG B 1 143 ? -14.242 -3.660  42.274  1.00 42.22 ? 143 ARG B NH2 1 
ATOM   2149 N N   . LEU B 1 144 ? -13.746 -1.027  49.405  1.00 38.34 ? 144 LEU B N   1 
ATOM   2150 C CA  . LEU B 1 144 ? -14.984 -0.237  49.363  1.00 38.20 ? 144 LEU B CA  1 
ATOM   2151 C C   . LEU B 1 144 ? -15.252 0.293   47.956  1.00 37.90 ? 144 LEU B C   1 
ATOM   2152 O O   . LEU B 1 144 ? -16.385 0.301   47.498  1.00 37.45 ? 144 LEU B O   1 
ATOM   2153 C CB  . LEU B 1 144 ? -14.911 0.952   50.321  1.00 38.15 ? 144 LEU B CB  1 
ATOM   2154 C CG  . LEU B 1 144 ? -14.782 0.691   51.822  1.00 38.21 ? 144 LEU B CG  1 
ATOM   2155 C CD1 . LEU B 1 144 ? -14.685 2.031   52.561  1.00 37.95 ? 144 LEU B CD1 1 
ATOM   2156 C CD2 . LEU B 1 144 ? -15.940 -0.130  52.332  1.00 38.19 ? 144 LEU B CD2 1 
ATOM   2157 N N   . ALA B 1 145 ? -14.206 0.775   47.292  1.00 37.60 ? 145 ALA B N   1 
ATOM   2158 C CA  . ALA B 1 145 ? -14.315 1.247   45.911  1.00 37.58 ? 145 ALA B CA  1 
ATOM   2159 C C   . ALA B 1 145 ? -12.992 1.033   45.175  1.00 37.21 ? 145 ALA B C   1 
ATOM   2160 O O   . ALA B 1 145 ? -11.923 1.034   45.783  1.00 36.58 ? 145 ALA B O   1 
ATOM   2161 C CB  . ALA B 1 145 ? -14.730 2.709   45.865  1.00 37.20 ? 145 ALA B CB  1 
ATOM   2162 N N   . ALA B 1 146 ? -13.090 0.838   43.865  1.00 37.27 ? 146 ALA B N   1 
ATOM   2163 C CA  . ALA B 1 146 ? -11.950 0.498   43.045  1.00 37.49 ? 146 ALA B CA  1 
ATOM   2164 C C   . ALA B 1 146 ? -12.157 0.918   41.593  1.00 37.61 ? 146 ALA B C   1 
ATOM   2165 O O   . ALA B 1 146 ? -13.284 1.066   41.113  1.00 37.17 ? 146 ALA B O   1 
ATOM   2166 C CB  . ALA B 1 146 ? -11.680 -0.996  43.118  1.00 37.53 ? 146 ALA B CB  1 
ATOM   2167 N N   . GLY B 1 147 ? -11.039 1.125   40.911  1.00 37.65 ? 147 GLY B N   1 
ATOM   2168 C CA  . GLY B 1 147 ? -11.041 1.451   39.497  1.00 37.67 ? 147 GLY B CA  1 
ATOM   2169 C C   . GLY B 1 147 ? -9.699  1.143   38.878  1.00 37.57 ? 147 GLY B C   1 
ATOM   2170 O O   . GLY B 1 147 ? -8.668  1.255   39.533  1.00 37.59 ? 147 GLY B O   1 
ATOM   2171 N N   . VAL B 1 148 ? -9.714  0.752   37.611  1.00 37.54 ? 148 VAL B N   1 
ATOM   2172 C CA  . VAL B 1 148 ? -8.484  0.538   36.872  1.00 37.69 ? 148 VAL B CA  1 
ATOM   2173 C C   . VAL B 1 148 ? -7.891  1.908   36.565  1.00 37.67 ? 148 VAL B C   1 
ATOM   2174 O O   . VAL B 1 148 ? -8.606  2.853   36.254  1.00 37.76 ? 148 VAL B O   1 
ATOM   2175 C CB  . VAL B 1 148 ? -8.722  -0.257  35.575  1.00 37.66 ? 148 VAL B CB  1 
ATOM   2176 C CG1 . VAL B 1 148 ? -7.413  -0.477  34.825  1.00 38.42 ? 148 VAL B CG1 1 
ATOM   2177 C CG2 . VAL B 1 148 ? -9.388  -1.588  35.879  1.00 37.39 ? 148 VAL B CG2 1 
ATOM   2178 N N   . ILE B 1 149 ? -6.575  2.002   36.679  1.00 37.90 ? 149 ILE B N   1 
ATOM   2179 C CA  . ILE B 1 149 ? -5.863  3.237   36.409  1.00 37.88 ? 149 ILE B CA  1 
ATOM   2180 C C   . ILE B 1 149 ? -5.693  3.295   34.894  1.00 38.07 ? 149 ILE B C   1 
ATOM   2181 O O   . ILE B 1 149 ? -4.979  2.473   34.305  1.00 38.11 ? 149 ILE B O   1 
ATOM   2182 C CB  . ILE B 1 149 ? -4.508  3.269   37.141  1.00 38.00 ? 149 ILE B CB  1 
ATOM   2183 C CG1 . ILE B 1 149 ? -4.720  3.022   38.643  1.00 37.61 ? 149 ILE B CG1 1 
ATOM   2184 C CG2 . ILE B 1 149 ? -3.803  4.621   36.905  1.00 37.91 ? 149 ILE B CG2 1 
ATOM   2185 C CD1 . ILE B 1 149 ? -3.462  2.726   39.422  1.00 37.58 ? 149 ILE B CD1 1 
ATOM   2186 N N   . GLY B 1 150 ? -6.399  4.235   34.269  1.00 38.01 ? 150 GLY B N   1 
ATOM   2187 C CA  . GLY B 1 150 ? -6.409  4.377   32.817  1.00 38.24 ? 150 GLY B CA  1 
ATOM   2188 C C   . GLY B 1 150 ? -5.693  5.634   32.362  1.00 38.40 ? 150 GLY B C   1 
ATOM   2189 O O   . GLY B 1 150 ? -5.438  6.533   33.147  1.00 37.83 ? 150 GLY B O   1 
ATOM   2190 N N   . ILE B 1 151 ? -5.381  5.677   31.074  1.00 38.77 ? 151 ILE B N   1 
ATOM   2191 C CA  . ILE B 1 151 ? -4.735  6.828   30.447  1.00 38.89 ? 151 ILE B CA  1 
ATOM   2192 C C   . ILE B 1 151 ? -5.733  7.984   30.342  1.00 39.21 ? 151 ILE B C   1 
ATOM   2193 O O   . ILE B 1 151 ? -6.858  7.793   29.906  1.00 39.06 ? 151 ILE B O   1 
ATOM   2194 C CB  . ILE B 1 151 ? -4.172  6.433   29.057  1.00 38.78 ? 151 ILE B CB  1 
ATOM   2195 C CG1 . ILE B 1 151 ? -3.082  5.364   29.230  1.00 37.87 ? 151 ILE B CG1 1 
ATOM   2196 C CG2 . ILE B 1 151 ? -3.636  7.661   28.311  1.00 38.90 ? 151 ILE B CG2 1 
ATOM   2197 C CD1 . ILE B 1 151 ? -2.624  4.714   27.958  1.00 38.93 ? 151 ILE B CD1 1 
ATOM   2198 N N   . ALA B 1 152 ? -5.301  9.177   30.749  1.00 39.74 ? 152 ALA B N   1 
ATOM   2199 C CA  . ALA B 1 152 ? -6.172  10.349  30.880  1.00 40.47 ? 152 ALA B CA  1 
ATOM   2200 C C   . ALA B 1 152 ? -5.906  11.374  29.788  1.00 41.01 ? 152 ALA B C   1 
ATOM   2201 O O   . ALA B 1 152 ? -4.776  11.508  29.327  1.00 41.06 ? 152 ALA B O   1 
ATOM   2202 C CB  . ALA B 1 152 ? -5.967  10.992  32.241  1.00 40.34 ? 152 ALA B CB  1 
ATOM   2203 N N   . GLN B 1 153 ? -6.943  12.112  29.401  1.00 41.98 ? 153 GLN B N   1 
ATOM   2204 C CA  . GLN B 1 153 ? -6.829  13.114  28.338  1.00 42.42 ? 153 GLN B CA  1 
ATOM   2205 C C   . GLN B 1 153 ? -6.201  14.421  28.820  1.00 43.47 ? 153 GLN B C   1 
ATOM   2206 O O   . GLN B 1 153 ? -6.485  14.901  29.933  1.00 44.47 ? 153 GLN B O   1 
ATOM   2207 C CB  . GLN B 1 153 ? -8.199  13.405  27.730  1.00 42.57 ? 153 GLN B CB  1 
ATOM   2208 C CG  . GLN B 1 153 ? -8.162  14.421  26.579  1.00 42.47 ? 153 GLN B CG  1 
ATOM   2209 C CD  . GLN B 1 153 ? -9.459  14.475  25.808  1.00 42.86 ? 153 GLN B CD  1 
ATOM   2210 O OE1 . GLN B 1 153 ? -10.516 14.081  26.310  1.00 44.84 ? 153 GLN B OE1 1 
ATOM   2211 N NE2 . GLN B 1 153 ? -9.391  14.972  24.581  1.00 43.22 ? 153 GLN B NE2 1 
ATOM   2212 O OXT . GLN B 1 153 ? -5.417  15.043  28.084  1.00 44.04 ? 153 GLN B OXT 1 
ATOM   2213 N N   . ALA C 1 1   ? 15.837  -3.500  32.898  1.00 44.29 ? 1   ALA C N   1 
ATOM   2214 C CA  . ALA C 1 1   ? 16.891  -2.439  32.986  1.00 44.08 ? 1   ALA C CA  1 
ATOM   2215 C C   . ALA C 1 1   ? 17.218  -1.844  31.615  1.00 43.98 ? 1   ALA C C   1 
ATOM   2216 O O   . ALA C 1 1   ? 17.128  -2.529  30.596  1.00 44.05 ? 1   ALA C O   1 
ATOM   2217 C CB  . ALA C 1 1   ? 18.159  -3.002  33.636  1.00 44.41 ? 1   ALA C CB  1 
ATOM   2218 N N   . THR C 1 2   ? 17.565  -0.560  31.601  1.00 43.45 ? 2   THR C N   1 
ATOM   2219 C CA  . THR C 1 2   ? 18.034  0.116   30.396  1.00 43.14 ? 2   THR C CA  1 
ATOM   2220 C C   . THR C 1 2   ? 19.532  0.338   30.540  1.00 42.36 ? 2   THR C C   1 
ATOM   2221 O O   . THR C 1 2   ? 20.026  0.620   31.630  1.00 41.46 ? 2   THR C O   1 
ATOM   2222 C CB  . THR C 1 2   ? 17.386  1.513   30.187  1.00 43.31 ? 2   THR C CB  1 
ATOM   2223 O OG1 . THR C 1 2   ? 16.082  1.551   30.773  1.00 45.60 ? 2   THR C OG1 1 
ATOM   2224 C CG2 . THR C 1 2   ? 17.275  1.835   28.714  1.00 43.60 ? 2   THR C CG2 1 
ATOM   2225 N N   . LYS C 1 3   ? 20.243  0.206   29.428  1.00 41.93 ? 3   LYS C N   1 
ATOM   2226 C CA  . LYS C 1 3   ? 21.689  0.361   29.409  1.00 41.68 ? 3   LYS C CA  1 
ATOM   2227 C C   . LYS C 1 3   ? 22.125  1.258   28.272  1.00 40.58 ? 3   LYS C C   1 
ATOM   2228 O O   . LYS C 1 3   ? 21.483  1.331   27.226  1.00 39.40 ? 3   LYS C O   1 
ATOM   2229 C CB  . LYS C 1 3   ? 22.371  -0.996  29.259  1.00 41.66 ? 3   LYS C CB  1 
ATOM   2230 C CG  . LYS C 1 3   ? 22.091  -1.957  30.399  1.00 42.96 ? 3   LYS C CG  1 
ATOM   2231 C CD  . LYS C 1 3   ? 23.072  -3.130  30.422  1.00 43.20 ? 3   LYS C CD  1 
ATOM   2232 C CE  . LYS C 1 3   ? 24.509  -2.693  30.781  1.00 44.72 ? 3   LYS C CE  1 
ATOM   2233 N NZ  . LYS C 1 3   ? 25.344  -3.881  31.212  1.00 44.65 ? 3   LYS C NZ  1 
ATOM   2234 N N   . ALA C 1 4   ? 23.252  1.915   28.481  1.00 40.15 ? 4   ALA C N   1 
ATOM   2235 C CA  . ALA C 1 4   ? 23.836  2.765   27.462  1.00 40.29 ? 4   ALA C CA  1 
ATOM   2236 C C   . ALA C 1 4   ? 25.351  2.825   27.660  1.00 40.20 ? 4   ALA C C   1 
ATOM   2237 O O   . ALA C 1 4   ? 25.891  2.253   28.632  1.00 40.03 ? 4   ALA C O   1 
ATOM   2238 C CB  . ALA C 1 4   ? 23.227  4.132   27.511  1.00 40.12 ? 4   ALA C CB  1 
ATOM   2239 N N   . VAL C 1 5   ? 26.024  3.467   26.707  1.00 39.55 ? 5   VAL C N   1 
ATOM   2240 C CA  . VAL C 1 5   ? 27.471  3.523   26.678  1.00 39.47 ? 5   VAL C CA  1 
ATOM   2241 C C   . VAL C 1 5   ? 27.931  4.676   25.793  1.00 39.10 ? 5   VAL C C   1 
ATOM   2242 O O   . VAL C 1 5   ? 27.294  5.015   24.801  1.00 38.40 ? 5   VAL C O   1 
ATOM   2243 C CB  . VAL C 1 5   ? 28.071  2.221   26.138  1.00 39.87 ? 5   VAL C CB  1 
ATOM   2244 C CG1 . VAL C 1 5   ? 27.779  2.074   24.644  1.00 40.71 ? 5   VAL C CG1 1 
ATOM   2245 C CG2 . VAL C 1 5   ? 29.592  2.146   26.411  1.00 40.08 ? 5   VAL C CG2 1 
ATOM   2246 N N   . ALA C 1 6   ? 29.053  5.258   26.174  1.00 38.86 ? 6   ALA C N   1 
ATOM   2247 C CA  . ALA C 1 6   ? 29.652  6.357   25.448  1.00 38.81 ? 6   ALA C CA  1 
ATOM   2248 C C   . ALA C 1 6   ? 31.139  6.080   25.340  1.00 38.79 ? 6   ALA C C   1 
ATOM   2249 O O   . ALA C 1 6   ? 31.818  5.925   26.355  1.00 38.54 ? 6   ALA C O   1 
ATOM   2250 C CB  . ALA C 1 6   ? 29.418  7.636   26.187  1.00 38.71 ? 6   ALA C CB  1 
ATOM   2251 N N   . VAL C 1 7   ? 31.637  5.985   24.112  1.00 39.01 ? 7   VAL C N   1 
ATOM   2252 C CA  . VAL C 1 7   ? 33.072  5.853   23.873  1.00 39.45 ? 7   VAL C CA  1 
ATOM   2253 C C   . VAL C 1 7   ? 33.629  7.260   23.679  1.00 39.52 ? 7   VAL C C   1 
ATOM   2254 O O   . VAL C 1 7   ? 33.231  7.964   22.759  1.00 39.37 ? 7   VAL C O   1 
ATOM   2255 C CB  . VAL C 1 7   ? 33.365  4.976   22.639  1.00 39.22 ? 7   VAL C CB  1 
ATOM   2256 C CG1 . VAL C 1 7   ? 34.867  4.887   22.383  1.00 40.09 ? 7   VAL C CG1 1 
ATOM   2257 C CG2 . VAL C 1 7   ? 32.781  3.594   22.833  1.00 38.99 ? 7   VAL C CG2 1 
ATOM   2258 N N   . LEU C 1 8   ? 34.549  7.664   24.547  1.00 40.16 ? 8   LEU C N   1 
ATOM   2259 C CA  . LEU C 1 8   ? 35.071  9.033   24.532  1.00 40.68 ? 8   LEU C CA  1 
ATOM   2260 C C   . LEU C 1 8   ? 36.343  9.089   23.718  1.00 41.04 ? 8   LEU C C   1 
ATOM   2261 O O   . LEU C 1 8   ? 37.252  8.278   23.929  1.00 41.48 ? 8   LEU C O   1 
ATOM   2262 C CB  . LEU C 1 8   ? 35.373  9.521   25.948  1.00 40.82 ? 8   LEU C CB  1 
ATOM   2263 C CG  . LEU C 1 8   ? 34.223  9.442   26.948  1.00 41.72 ? 8   LEU C CG  1 
ATOM   2264 C CD1 . LEU C 1 8   ? 34.781  9.485   28.345  1.00 43.16 ? 8   LEU C CD1 1 
ATOM   2265 C CD2 . LEU C 1 8   ? 33.233  10.574  26.724  1.00 42.46 ? 8   LEU C CD2 1 
ATOM   2266 N N   . LYS C 1 9   ? 36.394  10.040  22.788  1.00 41.29 ? 9   LYS C N   1 
ATOM   2267 C CA  . LYS C 1 9   ? 37.567  10.271  21.947  1.00 41.80 ? 9   LYS C CA  1 
ATOM   2268 C C   . LYS C 1 9   ? 37.685  11.757  21.671  1.00 41.49 ? 9   LYS C C   1 
ATOM   2269 O O   . LYS C 1 9   ? 36.692  12.466  21.690  1.00 41.27 ? 9   LYS C O   1 
ATOM   2270 C CB  . LYS C 1 9   ? 37.458  9.523   20.620  1.00 42.07 ? 9   LYS C CB  1 
ATOM   2271 C CG  . LYS C 1 9   ? 37.372  7.992   20.751  1.00 43.47 ? 9   LYS C CG  1 
ATOM   2272 C CD  . LYS C 1 9   ? 37.709  7.307   19.416  1.00 43.97 ? 9   LYS C CD  1 
ATOM   2273 C CE  . LYS C 1 9   ? 37.669  5.767   19.502  1.00 44.99 ? 9   LYS C CE  1 
ATOM   2274 N NZ  . LYS C 1 9   ? 36.326  5.224   19.136  1.00 46.86 ? 9   LYS C NZ  1 
ATOM   2275 N N   . GLY C 1 10  ? 38.904  12.213  21.414  1.00 41.61 ? 10  GLY C N   1 
ATOM   2276 C CA  . GLY C 1 10  ? 39.164  13.615  21.091  1.00 41.75 ? 10  GLY C CA  1 
ATOM   2277 C C   . GLY C 1 10  ? 40.430  13.773  20.268  1.00 41.84 ? 10  GLY C C   1 
ATOM   2278 O O   . GLY C 1 10  ? 40.979  12.797  19.753  1.00 41.89 ? 10  GLY C O   1 
ATOM   2279 N N   . ASP C 1 11  ? 40.901  15.008  20.151  1.00 41.95 ? 11  ASP C N   1 
ATOM   2280 C CA  . ASP C 1 11  ? 42.087  15.305  19.352  1.00 42.10 ? 11  ASP C CA  1 
ATOM   2281 C C   . ASP C 1 11  ? 43.391  15.092  20.112  1.00 41.74 ? 11  ASP C C   1 
ATOM   2282 O O   . ASP C 1 11  ? 44.469  15.191  19.521  1.00 41.84 ? 11  ASP C O   1 
ATOM   2283 C CB  . ASP C 1 11  ? 42.033  16.747  18.858  1.00 42.43 ? 11  ASP C CB  1 
ATOM   2284 C CG  . ASP C 1 11  ? 40.843  17.014  17.954  1.00 43.58 ? 11  ASP C CG  1 
ATOM   2285 O OD1 . ASP C 1 11  ? 40.289  16.050  17.362  1.00 43.42 ? 11  ASP C OD1 1 
ATOM   2286 O OD2 . ASP C 1 11  ? 40.474  18.206  17.836  1.00 43.54 ? 11  ASP C OD2 1 
ATOM   2287 N N   . GLY C 1 12  ? 43.287  14.836  21.416  1.00 41.30 ? 12  GLY C N   1 
ATOM   2288 C CA  . GLY C 1 12  ? 44.438  14.530  22.262  1.00 41.04 ? 12  GLY C CA  1 
ATOM   2289 C C   . GLY C 1 12  ? 44.418  13.062  22.641  1.00 40.67 ? 12  GLY C C   1 
ATOM   2290 O O   . GLY C 1 12  ? 43.750  12.270  21.981  1.00 40.37 ? 12  GLY C O   1 
ATOM   2291 N N   . PRO C 1 13  ? 45.144  12.691  23.708  1.00 40.48 ? 13  PRO C N   1 
ATOM   2292 C CA  . PRO C 1 13  ? 45.230  11.312  24.173  1.00 40.64 ? 13  PRO C CA  1 
ATOM   2293 C C   . PRO C 1 13  ? 44.069  10.864  25.062  1.00 40.62 ? 13  PRO C C   1 
ATOM   2294 O O   . PRO C 1 13  ? 44.048  9.711   25.492  1.00 40.31 ? 13  PRO C O   1 
ATOM   2295 C CB  . PRO C 1 13  ? 46.512  11.325  24.998  1.00 40.60 ? 13  PRO C CB  1 
ATOM   2296 C CG  . PRO C 1 13  ? 46.506  12.655  25.607  1.00 40.50 ? 13  PRO C CG  1 
ATOM   2297 C CD  . PRO C 1 13  ? 45.962  13.580  24.548  1.00 40.60 ? 13  PRO C CD  1 
ATOM   2298 N N   . VAL C 1 14  ? 43.126  11.759  25.351  1.00 40.75 ? 14  VAL C N   1 
ATOM   2299 C CA  . VAL C 1 14  ? 42.028  11.425  26.245  1.00 41.06 ? 14  VAL C CA  1 
ATOM   2300 C C   . VAL C 1 14  ? 41.069  10.464  25.540  1.00 41.32 ? 14  VAL C C   1 
ATOM   2301 O O   . VAL C 1 14  ? 40.508  10.777  24.487  1.00 40.97 ? 14  VAL C O   1 
ATOM   2302 C CB  . VAL C 1 14  ? 41.273  12.679  26.734  1.00 41.05 ? 14  VAL C CB  1 
ATOM   2303 C CG1 . VAL C 1 14  ? 40.115  12.298  27.665  1.00 41.42 ? 14  VAL C CG1 1 
ATOM   2304 C CG2 . VAL C 1 14  ? 42.228  13.612  27.438  1.00 40.84 ? 14  VAL C CG2 1 
ATOM   2305 N N   . GLN C 1 15  ? 40.916  9.283   26.128  1.00 41.54 ? 15  GLN C N   1 
ATOM   2306 C CA  . GLN C 1 15  ? 39.999  8.285   25.616  1.00 41.79 ? 15  GLN C CA  1 
ATOM   2307 C C   . GLN C 1 15  ? 39.472  7.407   26.750  1.00 41.44 ? 15  GLN C C   1 
ATOM   2308 O O   . GLN C 1 15  ? 40.145  7.196   27.753  1.00 41.17 ? 15  GLN C O   1 
ATOM   2309 C CB  . GLN C 1 15  ? 40.693  7.424   24.562  1.00 42.14 ? 15  GLN C CB  1 
ATOM   2310 C CG  . GLN C 1 15  ? 41.995  6.817   25.028  1.00 43.11 ? 15  GLN C CG  1 
ATOM   2311 C CD  . GLN C 1 15  ? 42.506  5.746   24.096  1.00 43.76 ? 15  GLN C CD  1 
ATOM   2312 O OE1 . GLN C 1 15  ? 43.102  6.039   23.058  1.00 45.95 ? 15  GLN C OE1 1 
ATOM   2313 N NE2 . GLN C 1 15  ? 42.287  4.486   24.469  1.00 46.38 ? 15  GLN C NE2 1 
ATOM   2314 N N   . GLY C 1 16  ? 38.257  6.898   26.581  1.00 41.16 ? 16  GLY C N   1 
ATOM   2315 C CA  . GLY C 1 16  ? 37.670  6.025   27.581  1.00 40.84 ? 16  GLY C CA  1 
ATOM   2316 C C   . GLY C 1 16  ? 36.324  5.457   27.185  1.00 40.46 ? 16  GLY C C   1 
ATOM   2317 O O   . GLY C 1 16  ? 35.825  5.686   26.086  1.00 40.52 ? 16  GLY C O   1 
ATOM   2318 N N   . ILE C 1 17  ? 35.756  4.696   28.106  1.00 39.89 ? 17  ILE C N   1 
ATOM   2319 C CA  . ILE C 1 17  ? 34.463  4.050   27.929  1.00 39.35 ? 17  ILE C CA  1 
ATOM   2320 C C   . ILE C 1 17  ? 33.671  4.279   29.212  1.00 38.88 ? 17  ILE C C   1 
ATOM   2321 O O   . ILE C 1 17  ? 34.177  4.015   30.307  1.00 38.84 ? 17  ILE C O   1 
ATOM   2322 C CB  . ILE C 1 17  ? 34.625  2.547   27.663  1.00 39.09 ? 17  ILE C CB  1 
ATOM   2323 C CG1 . ILE C 1 17  ? 35.352  2.328   26.329  1.00 38.95 ? 17  ILE C CG1 1 
ATOM   2324 C CG2 . ILE C 1 17  ? 33.258  1.862   27.652  1.00 39.69 ? 17  ILE C CG2 1 
ATOM   2325 C CD1 . ILE C 1 17  ? 35.652  0.863   25.995  1.00 39.17 ? 17  ILE C CD1 1 
ATOM   2326 N N   . ILE C 1 18  ? 32.451  4.790   29.067  1.00 38.16 ? 18  ILE C N   1 
ATOM   2327 C CA  . ILE C 1 18  ? 31.597  5.118   30.201  1.00 38.11 ? 18  ILE C CA  1 
ATOM   2328 C C   . ILE C 1 18  ? 30.280  4.387   29.996  1.00 38.20 ? 18  ILE C C   1 
ATOM   2329 O O   . ILE C 1 18  ? 29.619  4.569   28.975  1.00 37.82 ? 18  ILE C O   1 
ATOM   2330 C CB  . ILE C 1 18  ? 31.391  6.658   30.341  1.00 38.15 ? 18  ILE C CB  1 
ATOM   2331 C CG1 . ILE C 1 18  ? 32.729  7.350   30.628  1.00 37.82 ? 18  ILE C CG1 1 
ATOM   2332 C CG2 . ILE C 1 18  ? 30.361  6.990   31.428  1.00 38.10 ? 18  ILE C CG2 1 
ATOM   2333 C CD1 . ILE C 1 18  ? 33.368  7.007   31.954  1.00 38.40 ? 18  ILE C CD1 1 
ATOM   2334 N N   . ASN C 1 19  ? 29.963  3.491   30.938  1.00 38.33 ? 19  ASN C N   1 
ATOM   2335 C CA  . ASN C 1 19  ? 28.731  2.712   30.918  1.00 38.11 ? 19  ASN C CA  1 
ATOM   2336 C C   . ASN C 1 19  ? 27.648  3.368   31.766  1.00 37.85 ? 19  ASN C C   1 
ATOM   2337 O O   . ASN C 1 19  ? 27.939  3.980   32.787  1.00 37.60 ? 19  ASN C O   1 
ATOM   2338 C CB  . ASN C 1 19  ? 29.022  1.308   31.421  1.00 37.83 ? 19  ASN C CB  1 
ATOM   2339 C CG  . ASN C 1 19  ? 30.172  0.669   30.683  1.00 37.67 ? 19  ASN C CG  1 
ATOM   2340 O OD1 . ASN C 1 19  ? 31.304  0.602   31.191  1.00 37.56 ? 19  ASN C OD1 1 
ATOM   2341 N ND2 . ASN C 1 19  ? 29.907  0.234   29.461  1.00 35.34 ? 19  ASN C ND2 1 
ATOM   2342 N N   . PHE C 1 20  ? 26.401  3.260   31.316  1.00 38.40 ? 20  PHE C N   1 
ATOM   2343 C CA  . PHE C 1 20  ? 25.240  3.763   32.063  1.00 38.66 ? 20  PHE C CA  1 
ATOM   2344 C C   . PHE C 1 20  ? 24.264  2.611   32.250  1.00 38.96 ? 20  PHE C C   1 
ATOM   2345 O O   . PHE C 1 20  ? 24.016  1.850   31.316  1.00 39.26 ? 20  PHE C O   1 
ATOM   2346 C CB  . PHE C 1 20  ? 24.511  4.881   31.323  1.00 38.37 ? 20  PHE C CB  1 
ATOM   2347 C CG  . PHE C 1 20  ? 25.364  6.078   30.982  1.00 38.13 ? 20  PHE C CG  1 
ATOM   2348 C CD1 . PHE C 1 20  ? 26.219  6.052   29.894  1.00 38.51 ? 20  PHE C CD1 1 
ATOM   2349 C CD2 . PHE C 1 20  ? 25.252  7.251   31.705  1.00 38.35 ? 20  PHE C CD2 1 
ATOM   2350 C CE1 . PHE C 1 20  ? 26.985  7.149   29.566  1.00 37.88 ? 20  PHE C CE1 1 
ATOM   2351 C CE2 . PHE C 1 20  ? 26.009  8.359   31.373  1.00 38.09 ? 20  PHE C CE2 1 
ATOM   2352 C CZ  . PHE C 1 20  ? 26.868  8.308   30.304  1.00 38.06 ? 20  PHE C CZ  1 
ATOM   2353 N N   . GLU C 1 21  ? 23.713  2.483   33.452  1.00 39.46 ? 21  GLU C N   1 
ATOM   2354 C CA  . GLU C 1 21  ? 22.694  1.477   33.728  1.00 39.32 ? 21  GLU C CA  1 
ATOM   2355 C C   . GLU C 1 21  ? 21.616  2.036   34.658  1.00 39.22 ? 21  GLU C C   1 
ATOM   2356 O O   . GLU C 1 21  ? 21.915  2.671   35.674  1.00 38.97 ? 21  GLU C O   1 
ATOM   2357 C CB  . GLU C 1 21  ? 23.323  0.224   34.327  1.00 39.97 ? 21  GLU C CB  1 
ATOM   2358 C CG  . GLU C 1 21  ? 22.361  -0.964  34.413  1.00 39.95 ? 21  GLU C CG  1 
ATOM   2359 C CD  . GLU C 1 21  ? 23.071  -2.258  34.768  1.00 41.42 ? 21  GLU C CD  1 
ATOM   2360 O OE1 . GLU C 1 21  ? 24.269  -2.194  35.141  1.00 44.76 ? 21  GLU C OE1 1 
ATOM   2361 O OE2 . GLU C 1 21  ? 22.434  -3.337  34.681  1.00 43.23 ? 21  GLU C OE2 1 
ATOM   2362 N N   . GLN C 1 22  ? 20.360  1.802   34.280  1.00 39.18 ? 22  GLN C N   1 
ATOM   2363 C CA  . GLN C 1 22  ? 19.197  2.250   35.030  1.00 39.02 ? 22  GLN C CA  1 
ATOM   2364 C C   . GLN C 1 22  ? 18.217  1.082   35.227  1.00 39.05 ? 22  GLN C C   1 
ATOM   2365 O O   . GLN C 1 22  ? 17.541  0.680   34.284  1.00 38.87 ? 22  GLN C O   1 
ATOM   2366 C CB  . GLN C 1 22  ? 18.520  3.381   34.280  1.00 38.60 ? 22  GLN C CB  1 
ATOM   2367 C CG  . GLN C 1 22  ? 17.515  4.127   35.115  1.00 39.13 ? 22  GLN C CG  1 
ATOM   2368 C CD  . GLN C 1 22  ? 16.906  5.301   34.386  1.00 39.02 ? 22  GLN C CD  1 
ATOM   2369 O OE1 . GLN C 1 22  ? 17.053  5.430   33.174  1.00 39.90 ? 22  GLN C OE1 1 
ATOM   2370 N NE2 . GLN C 1 22  ? 16.205  6.158   35.120  1.00 37.96 ? 22  GLN C NE2 1 
ATOM   2371 N N   . LYS C 1 23  ? 18.147  0.554   36.449  1.00 39.15 ? 23  LYS C N   1 
ATOM   2372 C CA  . LYS C 1 23  ? 17.315  -0.619  36.753  1.00 39.39 ? 23  LYS C CA  1 
ATOM   2373 C C   . LYS C 1 23  ? 15.813  -0.337  36.704  1.00 38.87 ? 23  LYS C C   1 
ATOM   2374 O O   . LYS C 1 23  ? 15.045  -1.166  36.224  1.00 38.62 ? 23  LYS C O   1 
ATOM   2375 C CB  . LYS C 1 23  ? 17.686  -1.206  38.119  1.00 40.26 ? 23  LYS C CB  1 
ATOM   2376 C CG  . LYS C 1 23  ? 19.091  -1.815  38.164  1.00 42.44 ? 23  LYS C CG  1 
ATOM   2377 C CD  . LYS C 1 23  ? 19.155  -3.180  37.435  1.00 44.36 ? 23  LYS C CD  1 
ATOM   2378 C CE  . LYS C 1 23  ? 20.485  -3.925  37.696  1.00 44.19 ? 23  LYS C CE  1 
ATOM   2379 N NZ  . LYS C 1 23  ? 20.315  -5.420  37.696  1.00 44.37 ? 23  LYS C NZ  1 
ATOM   2380 N N   . GLU C 1 24  ? 15.402  0.824   37.210  1.00 38.54 ? 24  GLU C N   1 
ATOM   2381 C CA  . GLU C 1 24  ? 13.998  1.241   37.164  1.00 38.13 ? 24  GLU C CA  1 
ATOM   2382 C C   . GLU C 1 24  ? 13.909  2.535   36.383  1.00 37.48 ? 24  GLU C C   1 
ATOM   2383 O O   . GLU C 1 24  ? 14.755  3.404   36.535  1.00 37.10 ? 24  GLU C O   1 
ATOM   2384 C CB  . GLU C 1 24  ? 13.442  1.441   38.574  1.00 38.29 ? 24  GLU C CB  1 
ATOM   2385 C CG  . GLU C 1 24  ? 13.582  0.228   39.491  1.00 39.27 ? 24  GLU C CG  1 
ATOM   2386 C CD  . GLU C 1 24  ? 12.707  -0.947  39.087  1.00 41.02 ? 24  GLU C CD  1 
ATOM   2387 O OE1 . GLU C 1 24  ? 11.627  -0.724  38.493  1.00 42.85 ? 24  GLU C OE1 1 
ATOM   2388 O OE2 . GLU C 1 24  ? 13.093  -2.103  39.384  1.00 41.45 ? 24  GLU C OE2 1 
ATOM   2389 N N   . SER C 1 25  ? 12.878  2.675   35.557  1.00 37.12 ? 25  SER C N   1 
ATOM   2390 C CA  . SER C 1 25  ? 12.741  3.861   34.701  1.00 36.98 ? 25  SER C CA  1 
ATOM   2391 C C   . SER C 1 25  ? 12.630  5.158   35.508  1.00 36.75 ? 25  SER C C   1 
ATOM   2392 O O   . SER C 1 25  ? 12.974  6.228   35.013  1.00 36.57 ? 25  SER C O   1 
ATOM   2393 C CB  . SER C 1 25  ? 11.545  3.715   33.755  1.00 36.65 ? 25  SER C CB  1 
ATOM   2394 O OG  . SER C 1 25  ? 10.331  3.584   34.464  1.00 35.84 ? 25  SER C OG  1 
ATOM   2395 N N   . ASN C 1 26  ? 12.156  5.052   36.749  1.00 36.74 ? 26  ASN C N   1 
ATOM   2396 C CA  . ASN C 1 26  ? 12.111  6.187   37.664  1.00 36.77 ? 26  ASN C CA  1 
ATOM   2397 C C   . ASN C 1 26  ? 13.156  6.104   38.764  1.00 36.96 ? 26  ASN C C   1 
ATOM   2398 O O   . ASN C 1 26  ? 13.052  6.798   39.763  1.00 37.13 ? 26  ASN C O   1 
ATOM   2399 C CB  . ASN C 1 26  ? 10.706  6.373   38.254  1.00 36.60 ? 26  ASN C CB  1 
ATOM   2400 C CG  . ASN C 1 26  ? 10.284  5.235   39.176  1.00 36.45 ? 26  ASN C CG  1 
ATOM   2401 O OD1 . ASN C 1 26  ? 10.677  4.084   38.990  1.00 34.78 ? 26  ASN C OD1 1 
ATOM   2402 N ND2 . ASN C 1 26  ? 9.460   5.559   40.166  1.00 35.86 ? 26  ASN C ND2 1 
ATOM   2403 N N   . GLY C 1 27  ? 14.174  5.269   38.559  1.00 37.32 ? 27  GLY C N   1 
ATOM   2404 C CA  . GLY C 1 27  ? 15.254  5.092   39.518  1.00 37.53 ? 27  GLY C CA  1 
ATOM   2405 C C   . GLY C 1 27  ? 16.531  5.776   39.067  1.00 37.72 ? 27  GLY C C   1 
ATOM   2406 O O   . GLY C 1 27  ? 16.582  6.356   37.980  1.00 37.86 ? 27  GLY C O   1 
ATOM   2407 N N   . PRO C 1 28  ? 17.576  5.724   39.907  1.00 38.19 ? 28  PRO C N   1 
ATOM   2408 C CA  . PRO C 1 28  ? 18.854  6.365   39.554  1.00 38.31 ? 28  PRO C CA  1 
ATOM   2409 C C   . PRO C 1 28  ? 19.628  5.614   38.463  1.00 38.58 ? 28  PRO C C   1 
ATOM   2410 O O   . PRO C 1 28  ? 19.404  4.413   38.250  1.00 37.74 ? 28  PRO C O   1 
ATOM   2411 C CB  . PRO C 1 28  ? 19.627  6.360   40.874  1.00 38.05 ? 28  PRO C CB  1 
ATOM   2412 C CG  . PRO C 1 28  ? 19.041  5.272   41.658  1.00 38.35 ? 28  PRO C CG  1 
ATOM   2413 C CD  . PRO C 1 28  ? 17.623  5.085   41.232  1.00 37.84 ? 28  PRO C CD  1 
ATOM   2414 N N   . VAL C 1 29  ? 20.520  6.337   37.781  1.00 38.96 ? 29  VAL C N   1 
ATOM   2415 C CA  . VAL C 1 29  ? 21.391  5.766   36.768  1.00 39.47 ? 29  VAL C CA  1 
ATOM   2416 C C   . VAL C 1 29  ? 22.779  5.557   37.361  1.00 39.81 ? 29  VAL C C   1 
ATOM   2417 O O   . VAL C 1 29  ? 23.346  6.472   37.944  1.00 40.10 ? 29  VAL C O   1 
ATOM   2418 C CB  . VAL C 1 29  ? 21.524  6.690   35.529  1.00 39.43 ? 29  VAL C CB  1 
ATOM   2419 C CG1 . VAL C 1 29  ? 22.378  6.024   34.452  1.00 39.03 ? 29  VAL C CG1 1 
ATOM   2420 C CG2 . VAL C 1 29  ? 20.152  7.064   34.969  1.00 39.75 ? 29  VAL C CG2 1 
ATOM   2421 N N   . LYS C 1 30  ? 23.313  4.352   37.208  1.00 40.57 ? 30  LYS C N   1 
ATOM   2422 C CA  . LYS C 1 30  ? 24.687  4.046   37.599  1.00 40.88 ? 30  LYS C CA  1 
ATOM   2423 C C   . LYS C 1 30  ? 25.591  4.393   36.423  1.00 40.84 ? 30  LYS C C   1 
ATOM   2424 O O   . LYS C 1 30  ? 25.380  3.908   35.313  1.00 40.44 ? 30  LYS C O   1 
ATOM   2425 C CB  . LYS C 1 30  ? 24.829  2.560   37.972  1.00 41.16 ? 30  LYS C CB  1 
ATOM   2426 C CG  . LYS C 1 30  ? 26.184  2.180   38.589  1.00 41.94 ? 30  LYS C CG  1 
ATOM   2427 C CD  . LYS C 1 30  ? 26.465  0.644   38.522  1.00 43.03 ? 30  LYS C CD  1 
ATOM   2428 C CE  . LYS C 1 30  ? 27.941  0.309   38.852  1.00 44.38 ? 30  LYS C CE  1 
ATOM   2429 N NZ  . LYS C 1 30  ? 28.330  -1.128  38.591  1.00 44.66 ? 30  LYS C NZ  1 
ATOM   2430 N N   . VAL C 1 31  ? 26.580  5.250   36.673  1.00 40.77 ? 31  VAL C N   1 
ATOM   2431 C CA  . VAL C 1 31  ? 27.543  5.672   35.659  1.00 40.61 ? 31  VAL C CA  1 
ATOM   2432 C C   . VAL C 1 31  ? 28.916  5.169   36.092  1.00 40.53 ? 31  VAL C C   1 
ATOM   2433 O O   . VAL C 1 31  ? 29.357  5.454   37.197  1.00 40.40 ? 31  VAL C O   1 
ATOM   2434 C CB  . VAL C 1 31  ? 27.591  7.217   35.513  1.00 40.58 ? 31  VAL C CB  1 
ATOM   2435 C CG1 . VAL C 1 31  ? 28.542  7.624   34.397  1.00 40.72 ? 31  VAL C CG1 1 
ATOM   2436 C CG2 . VAL C 1 31  ? 26.193  7.796   35.267  1.00 40.49 ? 31  VAL C CG2 1 
ATOM   2437 N N   . TRP C 1 32  ? 29.573  4.382   35.246  1.00 40.58 ? 32  TRP C N   1 
ATOM   2438 C CA  . TRP C 1 32  ? 30.888  3.861   35.588  1.00 40.27 ? 32  TRP C CA  1 
ATOM   2439 C C   . TRP C 1 32  ? 31.731  3.559   34.368  1.00 39.98 ? 32  TRP C C   1 
ATOM   2440 O O   . TRP C 1 32  ? 31.222  3.374   33.269  1.00 39.40 ? 32  TRP C O   1 
ATOM   2441 C CB  . TRP C 1 32  ? 30.768  2.610   36.461  1.00 40.57 ? 32  TRP C CB  1 
ATOM   2442 C CG  . TRP C 1 32  ? 30.442  1.349   35.723  1.00 40.50 ? 32  TRP C CG  1 
ATOM   2443 C CD1 . TRP C 1 32  ? 31.301  0.340   35.407  1.00 40.58 ? 32  TRP C CD1 1 
ATOM   2444 C CD2 . TRP C 1 32  ? 29.163  0.956   35.230  1.00 40.52 ? 32  TRP C CD2 1 
ATOM   2445 N NE1 . TRP C 1 32  ? 30.640  -0.653  34.737  1.00 40.63 ? 32  TRP C NE1 1 
ATOM   2446 C CE2 . TRP C 1 32  ? 29.322  -0.303  34.619  1.00 40.63 ? 32  TRP C CE2 1 
ATOM   2447 C CE3 . TRP C 1 32  ? 27.895  1.543   35.249  1.00 40.72 ? 32  TRP C CE3 1 
ATOM   2448 C CZ2 . TRP C 1 32  ? 28.262  -0.979  34.021  1.00 41.11 ? 32  TRP C CZ2 1 
ATOM   2449 C CZ3 . TRP C 1 32  ? 26.840  0.871   34.656  1.00 40.91 ? 32  TRP C CZ3 1 
ATOM   2450 C CH2 . TRP C 1 32  ? 27.029  -0.377  34.046  1.00 40.93 ? 32  TRP C CH2 1 
ATOM   2451 N N   . GLY C 1 33  ? 33.038  3.514   34.594  1.00 39.98 ? 33  GLY C N   1 
ATOM   2452 C CA  . GLY C 1 33  ? 34.003  3.138   33.570  1.00 40.16 ? 33  GLY C CA  1 
ATOM   2453 C C   . GLY C 1 33  ? 35.372  3.693   33.885  1.00 39.88 ? 33  GLY C C   1 
ATOM   2454 O O   . GLY C 1 33  ? 35.682  3.970   35.032  1.00 39.46 ? 33  GLY C O   1 
ATOM   2455 N N   . SER C 1 34  ? 36.188  3.851   32.852  1.00 40.25 ? 34  SER C N   1 
ATOM   2456 C CA  . SER C 1 34  ? 37.534  4.397   33.002  1.00 40.21 ? 34  SER C CA  1 
ATOM   2457 C C   . SER C 1 34  ? 37.909  5.266   31.807  1.00 40.11 ? 34  SER C C   1 
ATOM   2458 O O   . SER C 1 34  ? 37.551  4.966   30.665  1.00 40.08 ? 34  SER C O   1 
ATOM   2459 C CB  . SER C 1 34  ? 38.554  3.277   33.192  1.00 40.45 ? 34  SER C CB  1 
ATOM   2460 O OG  . SER C 1 34  ? 38.688  2.505   32.018  1.00 41.98 ? 34  SER C OG  1 
ATOM   2461 N N   . ILE C 1 35  ? 38.594  6.370   32.104  1.00 39.79 ? 35  ILE C N   1 
ATOM   2462 C CA  . ILE C 1 35  ? 39.132  7.275   31.105  1.00 39.43 ? 35  ILE C CA  1 
ATOM   2463 C C   . ILE C 1 35  ? 40.632  7.387   31.373  1.00 39.29 ? 35  ILE C C   1 
ATOM   2464 O O   . ILE C 1 35  ? 41.046  7.490   32.529  1.00 38.77 ? 35  ILE C O   1 
ATOM   2465 C CB  . ILE C 1 35  ? 38.513  8.690   31.214  1.00 39.40 ? 35  ILE C CB  1 
ATOM   2466 C CG1 . ILE C 1 35  ? 36.978  8.619   31.306  1.00 39.85 ? 35  ILE C CG1 1 
ATOM   2467 C CG2 . ILE C 1 35  ? 38.941  9.555   30.025  1.00 39.49 ? 35  ILE C CG2 1 
ATOM   2468 C CD1 . ILE C 1 35  ? 36.305  9.960   31.613  1.00 39.52 ? 35  ILE C CD1 1 
ATOM   2469 N N   . LYS C 1 36  ? 41.437  7.364   30.313  1.00 38.98 ? 36  LYS C N   1 
ATOM   2470 C CA  . LYS C 1 36  ? 42.873  7.585   30.438  1.00 38.98 ? 36  LYS C CA  1 
ATOM   2471 C C   . LYS C 1 36  ? 43.325  8.779   29.598  1.00 38.75 ? 36  LYS C C   1 
ATOM   2472 O O   . LYS C 1 36  ? 42.533  9.375   28.863  1.00 38.59 ? 36  LYS C O   1 
ATOM   2473 C CB  . LYS C 1 36  ? 43.646  6.322   30.065  1.00 39.00 ? 36  LYS C CB  1 
ATOM   2474 C CG  . LYS C 1 36  ? 43.508  5.874   28.614  1.00 39.72 ? 36  LYS C CG  1 
ATOM   2475 C CD  . LYS C 1 36  ? 44.325  4.600   28.372  1.00 39.77 ? 36  LYS C CD  1 
ATOM   2476 C CE  . LYS C 1 36  ? 44.342  4.193   26.910  1.00 39.99 ? 36  LYS C CE  1 
ATOM   2477 N NZ  . LYS C 1 36  ? 45.506  3.315   26.608  1.00 40.25 ? 36  LYS C NZ  1 
ATOM   2478 N N   . GLY C 1 37  ? 44.601  9.135   29.739  1.00 38.59 ? 37  GLY C N   1 
ATOM   2479 C CA  . GLY C 1 37  ? 45.196  10.244  28.999  1.00 38.24 ? 37  GLY C CA  1 
ATOM   2480 C C   . GLY C 1 37  ? 44.909  11.622  29.568  1.00 37.91 ? 37  GLY C C   1 
ATOM   2481 O O   . GLY C 1 37  ? 45.181  12.629  28.919  1.00 37.71 ? 37  GLY C O   1 
ATOM   2482 N N   . LEU C 1 38  ? 44.380  11.676  30.788  1.00 37.79 ? 38  LEU C N   1 
ATOM   2483 C CA  . LEU C 1 38  ? 44.029  12.950  31.420  1.00 37.61 ? 38  LEU C CA  1 
ATOM   2484 C C   . LEU C 1 38  ? 45.196  13.502  32.217  1.00 37.45 ? 38  LEU C C   1 
ATOM   2485 O O   . LEU C 1 38  ? 46.045  12.744  32.680  1.00 37.47 ? 38  LEU C O   1 
ATOM   2486 C CB  . LEU C 1 38  ? 42.835  12.761  32.348  1.00 37.36 ? 38  LEU C CB  1 
ATOM   2487 C CG  . LEU C 1 38  ? 41.512  12.453  31.653  1.00 37.27 ? 38  LEU C CG  1 
ATOM   2488 C CD1 . LEU C 1 38  ? 40.555  11.739  32.599  1.00 37.04 ? 38  LEU C CD1 1 
ATOM   2489 C CD2 . LEU C 1 38  ? 40.908  13.728  31.115  1.00 37.08 ? 38  LEU C CD2 1 
ATOM   2490 N N   . THR C 1 39  ? 45.239  14.821  32.379  1.00 37.38 ? 39  THR C N   1 
ATOM   2491 C CA  . THR C 1 39  ? 46.133  15.424  33.364  1.00 37.60 ? 39  THR C CA  1 
ATOM   2492 C C   . THR C 1 39  ? 45.609  15.085  34.769  1.00 37.47 ? 39  THR C C   1 
ATOM   2493 O O   . THR C 1 39  ? 44.412  14.875  34.967  1.00 37.62 ? 39  THR C O   1 
ATOM   2494 C CB  . THR C 1 39  ? 46.269  16.968  33.201  1.00 37.69 ? 39  THR C CB  1 
ATOM   2495 O OG1 . THR C 1 39  ? 45.005  17.603  33.446  1.00 38.84 ? 39  THR C OG1 1 
ATOM   2496 C CG2 . THR C 1 39  ? 46.745  17.328  31.811  1.00 37.31 ? 39  THR C CG2 1 
ATOM   2497 N N   . GLU C 1 40  ? 46.511  15.024  35.739  1.00 37.49 ? 40  GLU C N   1 
ATOM   2498 C CA  . GLU C 1 40  ? 46.148  14.655  37.101  1.00 37.37 ? 40  GLU C CA  1 
ATOM   2499 C C   . GLU C 1 40  ? 45.179  15.666  37.721  1.00 37.31 ? 40  GLU C C   1 
ATOM   2500 O O   . GLU C 1 40  ? 45.381  16.879  37.617  1.00 37.39 ? 40  GLU C O   1 
ATOM   2501 C CB  . GLU C 1 40  ? 47.402  14.552  37.963  1.00 37.58 ? 40  GLU C CB  1 
ATOM   2502 C CG  . GLU C 1 40  ? 47.163  13.980  39.350  1.00 37.56 ? 40  GLU C CG  1 
ATOM   2503 C CD  . GLU C 1 40  ? 48.438  13.880  40.164  1.00 37.70 ? 40  GLU C CD  1 
ATOM   2504 O OE1 . GLU C 1 40  ? 49.529  14.176  39.623  1.00 37.56 ? 40  GLU C OE1 1 
ATOM   2505 O OE2 . GLU C 1 40  ? 48.342  13.505  41.354  1.00 38.50 ? 40  GLU C OE2 1 
ATOM   2506 N N   . GLY C 1 41  ? 44.128  15.152  38.360  1.00 36.93 ? 41  GLY C N   1 
ATOM   2507 C CA  . GLY C 1 41  ? 43.194  15.977  39.109  1.00 36.91 ? 41  GLY C CA  1 
ATOM   2508 C C   . GLY C 1 41  ? 41.769  15.887  38.606  1.00 36.67 ? 41  GLY C C   1 
ATOM   2509 O O   . GLY C 1 41  ? 41.385  14.922  37.947  1.00 36.74 ? 41  GLY C O   1 
ATOM   2510 N N   . LEU C 1 42  ? 40.994  16.918  38.916  1.00 36.44 ? 42  LEU C N   1 
ATOM   2511 C CA  . LEU C 1 42  ? 39.576  16.952  38.612  1.00 36.49 ? 42  LEU C CA  1 
ATOM   2512 C C   . LEU C 1 42  ? 39.318  17.412  37.178  1.00 36.19 ? 42  LEU C C   1 
ATOM   2513 O O   . LEU C 1 42  ? 39.989  18.305  36.671  1.00 36.06 ? 42  LEU C O   1 
ATOM   2514 C CB  . LEU C 1 42  ? 38.867  17.896  39.584  1.00 36.50 ? 42  LEU C CB  1 
ATOM   2515 C CG  . LEU C 1 42  ? 38.806  17.457  41.048  1.00 37.38 ? 42  LEU C CG  1 
ATOM   2516 C CD1 . LEU C 1 42  ? 38.399  18.628  41.955  1.00 37.37 ? 42  LEU C CD1 1 
ATOM   2517 C CD2 . LEU C 1 42  ? 37.851  16.278  41.227  1.00 37.70 ? 42  LEU C CD2 1 
ATOM   2518 N N   . HIS C 1 43  ? 38.335  16.797  36.532  1.00 36.24 ? 43  HIS C N   1 
ATOM   2519 C CA  . HIS C 1 43  ? 37.905  17.208  35.202  1.00 36.23 ? 43  HIS C CA  1 
ATOM   2520 C C   . HIS C 1 43  ? 36.395  17.212  35.147  1.00 36.29 ? 43  HIS C C   1 
ATOM   2521 O O   . HIS C 1 43  ? 35.766  16.199  35.439  1.00 36.61 ? 43  HIS C O   1 
ATOM   2522 C CB  . HIS C 1 43  ? 38.453  16.251  34.147  1.00 36.27 ? 43  HIS C CB  1 
ATOM   2523 C CG  . HIS C 1 43  ? 39.941  16.291  34.024  1.00 36.38 ? 43  HIS C CG  1 
ATOM   2524 N ND1 . HIS C 1 43  ? 40.595  17.191  33.212  1.00 36.76 ? 43  HIS C ND1 1 
ATOM   2525 C CD2 . HIS C 1 43  ? 40.904  15.561  34.632  1.00 35.87 ? 43  HIS C CD2 1 
ATOM   2526 C CE1 . HIS C 1 43  ? 41.897  17.009  33.322  1.00 36.68 ? 43  HIS C CE1 1 
ATOM   2527 N NE2 . HIS C 1 43  ? 42.111  16.025  34.177  1.00 35.89 ? 43  HIS C NE2 1 
ATOM   2528 N N   . GLY C 1 44  ? 35.816  18.350  34.776  1.00 36.30 ? 44  GLY C N   1 
ATOM   2529 C CA  . GLY C 1 44  ? 34.378  18.450  34.527  1.00 36.23 ? 44  GLY C CA  1 
ATOM   2530 C C   . GLY C 1 44  ? 33.850  17.278  33.720  1.00 36.19 ? 44  GLY C C   1 
ATOM   2531 O O   . GLY C 1 44  ? 34.510  16.796  32.800  1.00 35.87 ? 44  GLY C O   1 
ATOM   2532 N N   . PHE C 1 45  ? 32.649  16.830  34.071  1.00 36.31 ? 45  PHE C N   1 
ATOM   2533 C CA  . PHE C 1 45  ? 32.069  15.613  33.513  1.00 36.61 ? 45  PHE C CA  1 
ATOM   2534 C C   . PHE C 1 45  ? 30.592  15.881  33.244  1.00 36.69 ? 45  PHE C C   1 
ATOM   2535 O O   . PHE C 1 45  ? 29.805  15.991  34.176  1.00 36.57 ? 45  PHE C O   1 
ATOM   2536 C CB  . PHE C 1 45  ? 32.247  14.475  34.516  1.00 36.86 ? 45  PHE C CB  1 
ATOM   2537 C CG  . PHE C 1 45  ? 32.057  13.099  33.935  1.00 36.72 ? 45  PHE C CG  1 
ATOM   2538 C CD1 . PHE C 1 45  ? 32.677  12.727  32.743  1.00 37.58 ? 45  PHE C CD1 1 
ATOM   2539 C CD2 . PHE C 1 45  ? 31.301  12.157  34.609  1.00 37.20 ? 45  PHE C CD2 1 
ATOM   2540 C CE1 . PHE C 1 45  ? 32.519  11.449  32.228  1.00 37.07 ? 45  PHE C CE1 1 
ATOM   2541 C CE2 . PHE C 1 45  ? 31.138  10.883  34.096  1.00 36.65 ? 45  PHE C CE2 1 
ATOM   2542 C CZ  . PHE C 1 45  ? 31.751  10.530  32.911  1.00 36.98 ? 45  PHE C CZ  1 
ATOM   2543 N N   . HIS C 1 46  ? 30.236  16.023  31.967  1.00 36.67 ? 46  HIS C N   1 
ATOM   2544 C CA  . HIS C 1 46  ? 28.947  16.592  31.591  1.00 36.76 ? 46  HIS C CA  1 
ATOM   2545 C C   . HIS C 1 46  ? 28.317  15.933  30.387  1.00 36.39 ? 46  HIS C C   1 
ATOM   2546 O O   . HIS C 1 46  ? 28.988  15.675  29.385  1.00 35.89 ? 46  HIS C O   1 
ATOM   2547 C CB  . HIS C 1 46  ? 29.096  18.074  31.241  1.00 36.90 ? 46  HIS C CB  1 
ATOM   2548 C CG  . HIS C 1 46  ? 29.332  18.959  32.419  1.00 37.50 ? 46  HIS C CG  1 
ATOM   2549 N ND1 . HIS C 1 46  ? 30.551  19.550  32.677  1.00 37.59 ? 46  HIS C ND1 1 
ATOM   2550 C CD2 . HIS C 1 46  ? 28.499  19.373  33.400  1.00 38.70 ? 46  HIS C CD2 1 
ATOM   2551 C CE1 . HIS C 1 46  ? 30.466  20.269  33.780  1.00 37.31 ? 46  HIS C CE1 1 
ATOM   2552 N NE2 . HIS C 1 46  ? 29.226  20.191  34.233  1.00 38.76 ? 46  HIS C NE2 1 
ATOM   2553 N N   . VAL C 1 47  ? 27.002  15.737  30.486  1.00 36.29 ? 47  VAL C N   1 
ATOM   2554 C CA  . VAL C 1 47  ? 26.153  15.468  29.337  1.00 36.43 ? 47  VAL C CA  1 
ATOM   2555 C C   . VAL C 1 47  ? 25.778  16.778  28.650  1.00 36.27 ? 47  VAL C C   1 
ATOM   2556 O O   . VAL C 1 47  ? 25.204  17.672  29.273  1.00 35.29 ? 47  VAL C O   1 
ATOM   2557 C CB  . VAL C 1 47  ? 24.872  14.739  29.747  1.00 36.69 ? 47  VAL C CB  1 
ATOM   2558 C CG1 . VAL C 1 47  ? 23.964  14.512  28.538  1.00 37.40 ? 47  VAL C CG1 1 
ATOM   2559 C CG2 . VAL C 1 47  ? 25.224  13.412  30.404  1.00 36.07 ? 47  VAL C CG2 1 
ATOM   2560 N N   . HIS C 1 48  ? 26.109  16.874  27.363  1.00 36.53 ? 48  HIS C N   1 
ATOM   2561 C CA  . HIS C 1 48  ? 25.742  18.028  26.544  1.00 36.84 ? 48  HIS C CA  1 
ATOM   2562 C C   . HIS C 1 48  ? 24.555  17.686  25.652  1.00 37.31 ? 48  HIS C C   1 
ATOM   2563 O O   . HIS C 1 48  ? 24.232  16.521  25.452  1.00 36.77 ? 48  HIS C O   1 
ATOM   2564 C CB  . HIS C 1 48  ? 26.942  18.491  25.734  1.00 36.76 ? 48  HIS C CB  1 
ATOM   2565 C CG  . HIS C 1 48  ? 28.040  19.053  26.581  1.00 35.75 ? 48  HIS C CG  1 
ATOM   2566 N ND1 . HIS C 1 48  ? 28.492  20.346  26.451  1.00 36.20 ? 48  HIS C ND1 1 
ATOM   2567 C CD2 . HIS C 1 48  ? 28.749  18.505  27.596  1.00 33.69 ? 48  HIS C CD2 1 
ATOM   2568 C CE1 . HIS C 1 48  ? 29.450  20.564  27.334  1.00 35.97 ? 48  HIS C CE1 1 
ATOM   2569 N NE2 . HIS C 1 48  ? 29.626  19.460  28.039  1.00 36.03 ? 48  HIS C NE2 1 
ATOM   2570 N N   . GLU C 1 49  ? 23.901  18.710  25.126  1.00 37.87 ? 49  GLU C N   1 
ATOM   2571 C CA  . GLU C 1 49  ? 22.561  18.547  24.575  1.00 38.46 ? 49  GLU C CA  1 
ATOM   2572 C C   . GLU C 1 49  ? 22.505  17.761  23.278  1.00 39.10 ? 49  GLU C C   1 
ATOM   2573 O O   . GLU C 1 49  ? 21.570  17.001  23.057  1.00 39.38 ? 49  GLU C O   1 
ATOM   2574 C CB  . GLU C 1 49  ? 21.940  19.922  24.351  1.00 38.47 ? 49  GLU C CB  1 
ATOM   2575 C CG  . GLU C 1 49  ? 20.490  19.913  23.895  1.00 38.25 ? 49  GLU C CG  1 
ATOM   2576 C CD  . GLU C 1 49  ? 19.970  21.319  23.746  1.00 38.73 ? 49  GLU C CD  1 
ATOM   2577 O OE1 . GLU C 1 49  ? 20.772  22.239  23.987  1.00 40.28 ? 49  GLU C OE1 1 
ATOM   2578 O OE2 . GLU C 1 49  ? 18.784  21.506  23.394  1.00 39.38 ? 49  GLU C OE2 1 
ATOM   2579 N N   . PHE C 1 50  ? 23.483  17.960  22.403  1.00 39.50 ? 50  PHE C N   1 
ATOM   2580 C CA  . PHE C 1 50  ? 23.433  17.341  21.081  1.00 39.53 ? 50  PHE C CA  1 
ATOM   2581 C C   . PHE C 1 50  ? 24.438  16.223  20.949  1.00 39.73 ? 50  PHE C C   1 
ATOM   2582 O O   . PHE C 1 50  ? 25.563  16.318  21.456  1.00 39.28 ? 50  PHE C O   1 
ATOM   2583 C CB  . PHE C 1 50  ? 23.646  18.400  19.998  1.00 38.98 ? 50  PHE C CB  1 
ATOM   2584 C CG  . PHE C 1 50  ? 22.702  19.558  20.116  1.00 39.33 ? 50  PHE C CG  1 
ATOM   2585 C CD1 . PHE C 1 50  ? 21.346  19.390  19.864  1.00 38.42 ? 50  PHE C CD1 1 
ATOM   2586 C CD2 . PHE C 1 50  ? 23.160  20.807  20.520  1.00 38.12 ? 50  PHE C CD2 1 
ATOM   2587 C CE1 . PHE C 1 50  ? 20.465  20.449  19.986  1.00 38.55 ? 50  PHE C CE1 1 
ATOM   2588 C CE2 . PHE C 1 50  ? 22.284  21.867  20.652  1.00 38.87 ? 50  PHE C CE2 1 
ATOM   2589 C CZ  . PHE C 1 50  ? 20.932  21.688  20.385  1.00 38.93 ? 50  PHE C CZ  1 
ATOM   2590 N N   . GLY C 1 51  ? 24.011  15.155  20.274  1.00 40.49 ? 51  GLY C N   1 
ATOM   2591 C CA  . GLY C 1 51  ? 24.882  14.043  19.915  1.00 40.93 ? 51  GLY C CA  1 
ATOM   2592 C C   . GLY C 1 51  ? 25.584  14.299  18.598  1.00 41.52 ? 51  GLY C C   1 
ATOM   2593 O O   . GLY C 1 51  ? 25.696  13.406  17.758  1.00 41.81 ? 51  GLY C O   1 
ATOM   2594 N N   . ASP C 1 52  ? 26.062  15.528  18.421  1.00 42.04 ? 52  ASP C N   1 
ATOM   2595 C CA  . ASP C 1 52  ? 26.643  15.964  17.165  1.00 42.22 ? 52  ASP C CA  1 
ATOM   2596 C C   . ASP C 1 52  ? 28.151  16.030  17.329  1.00 42.89 ? 52  ASP C C   1 
ATOM   2597 O O   . ASP C 1 52  ? 28.673  16.893  18.040  1.00 42.85 ? 52  ASP C O   1 
ATOM   2598 C CB  . ASP C 1 52  ? 26.081  17.334  16.774  1.00 42.27 ? 52  ASP C CB  1 
ATOM   2599 C CG  . ASP C 1 52  ? 26.460  17.749  15.356  1.00 42.20 ? 52  ASP C CG  1 
ATOM   2600 O OD1 . ASP C 1 52  ? 27.495  17.266  14.842  1.00 41.68 ? 52  ASP C OD1 1 
ATOM   2601 O OD2 . ASP C 1 52  ? 25.710  18.556  14.759  1.00 41.46 ? 52  ASP C OD2 1 
ATOM   2602 N N   . ASN C 1 53  ? 28.839  15.109  16.654  1.00 43.50 ? 53  ASN C N   1 
ATOM   2603 C CA  . ASN C 1 53  ? 30.296  15.015  16.703  1.00 43.50 ? 53  ASN C CA  1 
ATOM   2604 C C   . ASN C 1 53  ? 30.972  15.552  15.436  1.00 43.39 ? 53  ASN C C   1 
ATOM   2605 O O   . ASN C 1 53  ? 32.178  15.397  15.268  1.00 43.58 ? 53  ASN C O   1 
ATOM   2606 C CB  . ASN C 1 53  ? 30.700  13.555  16.922  1.00 44.03 ? 53  ASN C CB  1 
ATOM   2607 C CG  . ASN C 1 53  ? 31.739  13.394  18.009  1.00 44.94 ? 53  ASN C CG  1 
ATOM   2608 O OD1 . ASN C 1 53  ? 31.527  12.645  18.975  1.00 49.93 ? 53  ASN C OD1 1 
ATOM   2609 N ND2 . ASN C 1 53  ? 32.859  14.101  17.876  1.00 46.28 ? 53  ASN C ND2 1 
ATOM   2610 N N   . THR C 1 54  ? 30.203  16.176  14.549  1.00 43.18 ? 54  THR C N   1 
ATOM   2611 C CA  . THR C 1 54  ? 30.723  16.602  13.240  1.00 43.40 ? 54  THR C CA  1 
ATOM   2612 C C   . THR C 1 54  ? 31.889  17.584  13.351  1.00 43.41 ? 54  THR C C   1 
ATOM   2613 O O   . THR C 1 54  ? 32.783  17.577  12.507  1.00 43.51 ? 54  THR C O   1 
ATOM   2614 C CB  . THR C 1 54  ? 29.628  17.247  12.355  1.00 43.28 ? 54  THR C CB  1 
ATOM   2615 O OG1 . THR C 1 54  ? 28.955  18.275  13.090  1.00 43.12 ? 54  THR C OG1 1 
ATOM   2616 C CG2 . THR C 1 54  ? 28.623  16.210  11.902  1.00 43.32 ? 54  THR C CG2 1 
ATOM   2617 N N   . ALA C 1 55  ? 31.868  18.433  14.376  1.00 43.54 ? 55  ALA C N   1 
ATOM   2618 C CA  . ALA C 1 55  ? 32.998  19.329  14.668  1.00 43.57 ? 55  ALA C CA  1 
ATOM   2619 C C   . ALA C 1 55  ? 33.652  18.942  16.002  1.00 43.61 ? 55  ALA C C   1 
ATOM   2620 O O   . ALA C 1 55  ? 34.130  19.800  16.747  1.00 43.89 ? 55  ALA C O   1 
ATOM   2621 C CB  . ALA C 1 55  ? 32.532  20.777  14.695  1.00 43.56 ? 55  ALA C CB  1 
ATOM   2622 N N   . GLY C 1 56  ? 33.676  17.645  16.287  1.00 43.28 ? 56  GLY C N   1 
ATOM   2623 C CA  . GLY C 1 56  ? 34.174  17.148  17.555  1.00 43.35 ? 56  GLY C CA  1 
ATOM   2624 C C   . GLY C 1 56  ? 33.226  17.403  18.717  1.00 43.14 ? 56  GLY C C   1 
ATOM   2625 O O   . GLY C 1 56  ? 32.006  17.371  18.564  1.00 43.19 ? 56  GLY C O   1 
ATOM   2626 N N   . ALA C 1 57  ? 33.805  17.658  19.886  1.00 42.89 ? 57  ALA C N   1 
ATOM   2627 C CA  . ALA C 1 57  ? 33.035  17.971  21.088  1.00 42.86 ? 57  ALA C CA  1 
ATOM   2628 C C   . ALA C 1 57  ? 32.392  19.364  21.015  1.00 42.80 ? 57  ALA C C   1 
ATOM   2629 O O   . ALA C 1 57  ? 31.477  19.673  21.769  1.00 43.10 ? 57  ALA C O   1 
ATOM   2630 C CB  . ALA C 1 57  ? 33.937  17.876  22.318  1.00 42.92 ? 57  ALA C CB  1 
ATOM   2631 N N   . THR C 1 58  ? 32.878  20.197  20.112  1.00 42.35 ? 58  THR C N   1 
ATOM   2632 C CA  . THR C 1 58  ? 32.355  21.554  19.951  1.00 42.51 ? 58  THR C CA  1 
ATOM   2633 C C   . THR C 1 58  ? 30.887  21.558  19.526  1.00 42.48 ? 58  THR C C   1 
ATOM   2634 O O   . THR C 1 58  ? 30.095  22.361  20.009  1.00 42.51 ? 58  THR C O   1 
ATOM   2635 C CB  . THR C 1 58  ? 33.182  22.301  18.905  1.00 42.45 ? 58  THR C CB  1 
ATOM   2636 O OG1 . THR C 1 58  ? 34.574  22.130  19.208  1.00 42.81 ? 58  THR C OG1 1 
ATOM   2637 C CG2 . THR C 1 58  ? 32.829  23.798  18.876  1.00 42.26 ? 58  THR C CG2 1 
ATOM   2638 N N   . SER C 1 59  ? 30.537  20.647  18.625  1.00 42.42 ? 59  SER C N   1 
ATOM   2639 C CA  . SER C 1 59  ? 29.199  20.594  18.047  1.00 42.32 ? 59  SER C CA  1 
ATOM   2640 C C   . SER C 1 59  ? 28.174  19.980  19.016  1.00 42.17 ? 59  SER C C   1 
ATOM   2641 O O   . SER C 1 59  ? 26.964  20.084  18.795  1.00 42.05 ? 59  SER C O   1 
ATOM   2642 C CB  . SER C 1 59  ? 29.245  19.816  16.727  1.00 42.39 ? 59  SER C CB  1 
ATOM   2643 O OG  . SER C 1 59  ? 30.077  18.673  16.849  1.00 43.06 ? 59  SER C OG  1 
ATOM   2644 N N   . ALA C 1 60  ? 28.672  19.362  20.088  1.00 41.95 ? 60  ALA C N   1 
ATOM   2645 C CA  . ALA C 1 60  ? 27.848  18.825  21.178  1.00 41.77 ? 60  ALA C CA  1 
ATOM   2646 C C   . ALA C 1 60  ? 26.950  19.859  21.861  1.00 41.84 ? 60  ALA C C   1 
ATOM   2647 O O   . ALA C 1 60  ? 25.984  19.500  22.530  1.00 42.04 ? 60  ALA C O   1 
ATOM   2648 C CB  . ALA C 1 60  ? 28.734  18.179  22.212  1.00 41.81 ? 60  ALA C CB  1 
ATOM   2649 N N   . GLY C 1 61  ? 27.286  21.135  21.716  1.00 41.47 ? 61  GLY C N   1 
ATOM   2650 C CA  . GLY C 1 61  ? 26.460  22.208  22.250  1.00 41.54 ? 61  GLY C CA  1 
ATOM   2651 C C   . GLY C 1 61  ? 26.633  22.392  23.747  1.00 41.33 ? 61  GLY C C   1 
ATOM   2652 O O   . GLY C 1 61  ? 27.630  21.961  24.318  1.00 41.03 ? 61  GLY C O   1 
ATOM   2653 N N   . PRO C 1 62  ? 25.645  23.026  24.398  1.00 41.38 ? 62  PRO C N   1 
ATOM   2654 C CA  . PRO C 1 62  ? 25.779  23.386  25.793  1.00 41.18 ? 62  PRO C CA  1 
ATOM   2655 C C   . PRO C 1 62  ? 25.468  22.223  26.711  1.00 41.14 ? 62  PRO C C   1 
ATOM   2656 O O   . PRO C 1 62  ? 25.034  21.157  26.260  1.00 40.73 ? 62  PRO C O   1 
ATOM   2657 C CB  . PRO C 1 62  ? 24.733  24.491  25.952  1.00 41.51 ? 62  PRO C CB  1 
ATOM   2658 C CG  . PRO C 1 62  ? 23.635  24.048  25.040  1.00 41.57 ? 62  PRO C CG  1 
ATOM   2659 C CD  . PRO C 1 62  ? 24.333  23.428  23.856  1.00 41.50 ? 62  PRO C CD  1 
ATOM   2660 N N   . HIS C 1 63  ? 25.705  22.433  27.999  1.00 41.11 ? 63  HIS C N   1 
ATOM   2661 C CA  . HIS C 1 63  ? 25.286  21.490  29.014  1.00 40.79 ? 63  HIS C CA  1 
ATOM   2662 C C   . HIS C 1 63  ? 23.834  21.152  28.718  1.00 40.61 ? 63  HIS C C   1 
ATOM   2663 O O   . HIS C 1 63  ? 23.068  22.014  28.309  1.00 39.85 ? 63  HIS C O   1 
ATOM   2664 C CB  . HIS C 1 63  ? 25.394  22.115  30.408  1.00 40.93 ? 63  HIS C CB  1 
ATOM   2665 C CG  . HIS C 1 63  ? 26.800  22.289  30.904  1.00 41.04 ? 63  HIS C CG  1 
ATOM   2666 N ND1 . HIS C 1 63  ? 27.087  22.676  32.196  1.00 40.88 ? 63  HIS C ND1 1 
ATOM   2667 C CD2 . HIS C 1 63  ? 27.994  22.117  30.290  1.00 40.92 ? 63  HIS C CD2 1 
ATOM   2668 C CE1 . HIS C 1 63  ? 28.397  22.735  32.355  1.00 40.98 ? 63  HIS C CE1 1 
ATOM   2669 N NE2 . HIS C 1 63  ? 28.970  22.396  31.214  1.00 40.39 ? 63  HIS C NE2 1 
ATOM   2670 N N   . PHE C 1 64  ? 23.456  19.893  28.902  1.00 40.62 ? 64  PHE C N   1 
ATOM   2671 C CA  . PHE C 1 64  ? 22.072  19.500  28.701  1.00 41.07 ? 64  PHE C CA  1 
ATOM   2672 C C   . PHE C 1 64  ? 21.217  20.095  29.815  1.00 41.73 ? 64  PHE C C   1 
ATOM   2673 O O   . PHE C 1 64  ? 21.520  19.929  30.999  1.00 41.74 ? 64  PHE C O   1 
ATOM   2674 C CB  . PHE C 1 64  ? 21.948  17.974  28.672  1.00 40.63 ? 64  PHE C CB  1 
ATOM   2675 C CG  . PHE C 1 64  ? 20.553  17.487  28.443  1.00 40.28 ? 64  PHE C CG  1 
ATOM   2676 C CD1 . PHE C 1 64  ? 19.738  18.081  27.479  1.00 39.54 ? 64  PHE C CD1 1 
ATOM   2677 C CD2 . PHE C 1 64  ? 20.055  16.420  29.177  1.00 39.34 ? 64  PHE C CD2 1 
ATOM   2678 C CE1 . PHE C 1 64  ? 18.452  17.630  27.262  1.00 40.18 ? 64  PHE C CE1 1 
ATOM   2679 C CE2 . PHE C 1 64  ? 18.770  15.964  28.964  1.00 39.93 ? 64  PHE C CE2 1 
ATOM   2680 C CZ  . PHE C 1 64  ? 17.963  16.567  28.004  1.00 39.93 ? 64  PHE C CZ  1 
ATOM   2681 N N   . ASN C 1 65  ? 20.164  20.812  29.431  1.00 42.78 ? 65  ASN C N   1 
ATOM   2682 C CA  . ASN C 1 65  ? 19.321  21.512  30.389  1.00 43.25 ? 65  ASN C CA  1 
ATOM   2683 C C   . ASN C 1 65  ? 17.918  21.717  29.817  1.00 43.84 ? 65  ASN C C   1 
ATOM   2684 O O   . ASN C 1 65  ? 17.578  22.818  29.374  1.00 44.08 ? 65  ASN C O   1 
ATOM   2685 C CB  . ASN C 1 65  ? 19.964  22.853  30.759  1.00 43.52 ? 65  ASN C CB  1 
ATOM   2686 C CG  . ASN C 1 65  ? 19.321  23.498  31.968  1.00 43.48 ? 65  ASN C CG  1 
ATOM   2687 O OD1 . ASN C 1 65  ? 18.991  22.818  32.942  1.00 45.77 ? 65  ASN C OD1 1 
ATOM   2688 N ND2 . ASN C 1 65  ? 19.151  24.815  31.919  1.00 43.49 ? 65  ASN C ND2 1 
ATOM   2689 N N   . PRO C 1 66  ? 17.094  20.652  29.826  1.00 44.43 ? 66  PRO C N   1 
ATOM   2690 C CA  . PRO C 1 66  ? 15.759  20.652  29.209  1.00 44.83 ? 66  PRO C CA  1 
ATOM   2691 C C   . PRO C 1 66  ? 14.710  21.509  29.939  1.00 45.27 ? 66  PRO C C   1 
ATOM   2692 O O   . PRO C 1 66  ? 15.067  22.335  30.782  1.00 45.32 ? 66  PRO C O   1 
ATOM   2693 C CB  . PRO C 1 66  ? 15.375  19.162  29.213  1.00 45.00 ? 66  PRO C CB  1 
ATOM   2694 C CG  . PRO C 1 66  ? 16.145  18.565  30.305  1.00 44.73 ? 66  PRO C CG  1 
ATOM   2695 C CD  . PRO C 1 66  ? 17.412  19.354  30.446  1.00 44.41 ? 66  PRO C CD  1 
ATOM   2696 N N   . LEU C 1 67  ? 13.435  21.314  29.582  1.00 45.76 ? 67  LEU C N   1 
ATOM   2697 C CA  . LEU C 1 67  ? 12.271  22.019  30.165  1.00 45.82 ? 67  LEU C CA  1 
ATOM   2698 C C   . LEU C 1 67  ? 12.053  23.347  29.464  1.00 45.86 ? 67  LEU C C   1 
ATOM   2699 O O   . LEU C 1 67  ? 11.253  24.160  29.917  1.00 46.08 ? 67  LEU C O   1 
ATOM   2700 C CB  . LEU C 1 67  ? 12.388  22.254  31.683  1.00 46.04 ? 67  LEU C CB  1 
ATOM   2701 C CG  . LEU C 1 67  ? 12.763  21.091  32.605  1.00 47.11 ? 67  LEU C CG  1 
ATOM   2702 C CD1 . LEU C 1 67  ? 12.720  21.564  34.054  1.00 47.77 ? 67  LEU C CD1 1 
ATOM   2703 C CD2 . LEU C 1 67  ? 11.858  19.871  32.393  1.00 47.41 ? 67  LEU C CD2 1 
ATOM   2704 N N   . HIS C 1 80  ? 21.456  21.939  34.725  1.00 47.24 ? 80  HIS C N   1 
ATOM   2705 C CA  . HIS C 1 80  ? 21.765  21.041  35.826  1.00 46.84 ? 80  HIS C CA  1 
ATOM   2706 C C   . HIS C 1 80  ? 21.749  19.596  35.360  1.00 46.48 ? 80  HIS C C   1 
ATOM   2707 O O   . HIS C 1 80  ? 22.572  18.811  35.801  1.00 46.84 ? 80  HIS C O   1 
ATOM   2708 C CB  . HIS C 1 80  ? 20.751  21.200  36.969  1.00 47.18 ? 80  HIS C CB  1 
ATOM   2709 C CG  . HIS C 1 80  ? 21.223  22.061  38.099  1.00 47.81 ? 80  HIS C CG  1 
ATOM   2710 N ND1 . HIS C 1 80  ? 22.156  21.634  39.024  1.00 48.31 ? 80  HIS C ND1 1 
ATOM   2711 C CD2 . HIS C 1 80  ? 20.857  23.310  38.482  1.00 49.22 ? 80  HIS C CD2 1 
ATOM   2712 C CE1 . HIS C 1 80  ? 22.356  22.591  39.916  1.00 49.04 ? 80  HIS C CE1 1 
ATOM   2713 N NE2 . HIS C 1 80  ? 21.580  23.620  39.611  1.00 49.00 ? 80  HIS C NE2 1 
ATOM   2714 N N   . VAL C 1 81  ? 20.821  19.244  34.473  1.00 46.08 ? 81  VAL C N   1 
ATOM   2715 C CA  . VAL C 1 81  ? 20.526  17.826  34.199  1.00 46.02 ? 81  VAL C CA  1 
ATOM   2716 C C   . VAL C 1 81  ? 21.742  17.035  33.724  1.00 45.90 ? 81  VAL C C   1 
ATOM   2717 O O   . VAL C 1 81  ? 21.940  15.893  34.123  1.00 46.73 ? 81  VAL C O   1 
ATOM   2718 C CB  . VAL C 1 81  ? 19.371  17.653  33.195  1.00 45.82 ? 81  VAL C CB  1 
ATOM   2719 C CG1 . VAL C 1 81  ? 19.166  16.182  32.862  1.00 45.67 ? 81  VAL C CG1 1 
ATOM   2720 C CG2 . VAL C 1 81  ? 18.101  18.242  33.765  1.00 46.42 ? 81  VAL C CG2 1 
ATOM   2721 N N   . GLY C 1 82  ? 22.562  17.637  32.879  1.00 45.75 ? 82  GLY C N   1 
ATOM   2722 C CA  . GLY C 1 82  ? 23.802  16.988  32.458  1.00 45.18 ? 82  GLY C CA  1 
ATOM   2723 C C   . GLY C 1 82  ? 24.923  16.954  33.493  1.00 44.62 ? 82  GLY C C   1 
ATOM   2724 O O   . GLY C 1 82  ? 25.880  16.203  33.331  1.00 44.31 ? 82  GLY C O   1 
ATOM   2725 N N   . ASP C 1 83  ? 24.818  17.756  34.552  1.00 44.12 ? 83  ASP C N   1 
ATOM   2726 C CA  . ASP C 1 83  ? 25.932  17.920  35.500  1.00 43.93 ? 83  ASP C CA  1 
ATOM   2727 C C   . ASP C 1 83  ? 26.198  16.656  36.301  1.00 43.69 ? 83  ASP C C   1 
ATOM   2728 O O   . ASP C 1 83  ? 25.481  16.356  37.252  1.00 43.83 ? 83  ASP C O   1 
ATOM   2729 C CB  . ASP C 1 83  ? 25.680  19.094  36.454  1.00 43.97 ? 83  ASP C CB  1 
ATOM   2730 C CG  . ASP C 1 83  ? 26.927  19.494  37.248  1.00 44.04 ? 83  ASP C CG  1 
ATOM   2731 O OD1 . ASP C 1 83  ? 27.857  18.668  37.402  0.50 43.56 ? 83  ASP C OD1 1 
ATOM   2732 O OD2 . ASP C 1 83  ? 26.969  20.648  37.721  0.50 43.65 ? 83  ASP C OD2 1 
ATOM   2733 N N   . LEU C 1 84  ? 27.247  15.934  35.917  1.00 43.14 ? 84  LEU C N   1 
ATOM   2734 C CA  . LEU C 1 84  ? 27.654  14.732  36.620  1.00 43.02 ? 84  LEU C CA  1 
ATOM   2735 C C   . LEU C 1 84  ? 28.896  14.977  37.472  1.00 42.87 ? 84  LEU C C   1 
ATOM   2736 O O   . LEU C 1 84  ? 29.657  14.050  37.743  1.00 43.11 ? 84  LEU C O   1 
ATOM   2737 C CB  . LEU C 1 84  ? 27.919  13.624  35.612  1.00 43.06 ? 84  LEU C CB  1 
ATOM   2738 C CG  . LEU C 1 84  ? 26.722  13.171  34.788  1.00 43.42 ? 84  LEU C CG  1 
ATOM   2739 C CD1 . LEU C 1 84  ? 27.185  12.150  33.776  1.00 43.12 ? 84  LEU C CD1 1 
ATOM   2740 C CD2 . LEU C 1 84  ? 25.633  12.580  35.688  1.00 44.27 ? 84  LEU C CD2 1 
ATOM   2741 N N   . GLY C 1 85  ? 29.094  16.227  37.887  1.00 42.44 ? 85  GLY C N   1 
ATOM   2742 C CA  . GLY C 1 85  ? 30.207  16.606  38.747  1.00 42.16 ? 85  GLY C CA  1 
ATOM   2743 C C   . GLY C 1 85  ? 31.532  16.618  38.018  1.00 41.87 ? 85  GLY C C   1 
ATOM   2744 O O   . GLY C 1 85  ? 31.642  17.195  36.942  1.00 41.97 ? 85  GLY C O   1 
ATOM   2745 N N   . ASN C 1 86  ? 32.541  15.994  38.621  1.00 41.57 ? 86  ASN C N   1 
ATOM   2746 C CA  . ASN C 1 86  ? 33.857  15.840  38.004  1.00 41.31 ? 86  ASN C CA  1 
ATOM   2747 C C   . ASN C 1 86  ? 34.237  14.375  37.985  1.00 41.12 ? 86  ASN C C   1 
ATOM   2748 O O   . ASN C 1 86  ? 33.579  13.548  38.610  1.00 40.88 ? 86  ASN C O   1 
ATOM   2749 C CB  . ASN C 1 86  ? 34.936  16.583  38.794  1.00 41.18 ? 86  ASN C CB  1 
ATOM   2750 C CG  . ASN C 1 86  ? 34.696  18.072  38.880  1.00 41.16 ? 86  ASN C CG  1 
ATOM   2751 O OD1 . ASN C 1 86  ? 34.947  18.812  37.927  1.00 41.30 ? 86  ASN C OD1 1 
ATOM   2752 N ND2 . ASN C 1 86  ? 34.262  18.532  40.049  1.00 40.19 ? 86  ASN C ND2 1 
ATOM   2753 N N   . VAL C 1 87  ? 35.307  14.070  37.260  1.00 41.13 ? 87  VAL C N   1 
ATOM   2754 C CA  . VAL C 1 87  ? 36.005  12.787  37.382  1.00 41.13 ? 87  VAL C CA  1 
ATOM   2755 C C   . VAL C 1 87  ? 37.433  13.092  37.801  1.00 40.81 ? 87  VAL C C   1 
ATOM   2756 O O   . VAL C 1 87  ? 37.928  14.187  37.560  1.00 40.48 ? 87  VAL C O   1 
ATOM   2757 C CB  . VAL C 1 87  ? 35.972  11.950  36.080  1.00 41.21 ? 87  VAL C CB  1 
ATOM   2758 C CG1 . VAL C 1 87  ? 34.556  11.428  35.833  1.00 41.21 ? 87  VAL C CG1 1 
ATOM   2759 C CG2 . VAL C 1 87  ? 36.478  12.766  34.876  1.00 41.72 ? 87  VAL C CG2 1 
ATOM   2760 N N   . THR C 1 88  ? 38.079  12.125  38.439  1.00 40.77 ? 88  THR C N   1 
ATOM   2761 C CA  . THR C 1 88  ? 39.381  12.343  39.062  1.00 40.87 ? 88  THR C CA  1 
ATOM   2762 C C   . THR C 1 88  ? 40.422  11.426  38.447  1.00 40.84 ? 88  THR C C   1 
ATOM   2763 O O   . THR C 1 88  ? 40.330  10.206  38.581  1.00 40.70 ? 88  THR C O   1 
ATOM   2764 C CB  . THR C 1 88  ? 39.314  12.096  40.596  1.00 40.65 ? 88  THR C CB  1 
ATOM   2765 O OG1 . THR C 1 88  ? 38.283  12.906  41.163  1.00 39.83 ? 88  THR C OG1 1 
ATOM   2766 C CG2 . THR C 1 88  ? 40.632  12.445  41.273  1.00 40.96 ? 88  THR C CG2 1 
ATOM   2767 N N   . ALA C 1 89  ? 41.408  12.017  37.778  1.00 40.99 ? 89  ALA C N   1 
ATOM   2768 C CA  . ALA C 1 89  ? 42.496  11.252  37.193  1.00 41.31 ? 89  ALA C CA  1 
ATOM   2769 C C   . ALA C 1 89  ? 43.628  11.129  38.208  1.00 41.59 ? 89  ALA C C   1 
ATOM   2770 O O   . ALA C 1 89  ? 43.894  12.065  38.969  1.00 41.68 ? 89  ALA C O   1 
ATOM   2771 C CB  . ALA C 1 89  ? 42.985  11.912  35.917  1.00 41.37 ? 89  ALA C CB  1 
ATOM   2772 N N   . ASP C 1 90  ? 44.288  9.974   38.221  1.00 41.83 ? 90  ASP C N   1 
ATOM   2773 C CA  . ASP C 1 90  ? 45.397  9.730   39.145  1.00 42.02 ? 90  ASP C CA  1 
ATOM   2774 C C   . ASP C 1 90  ? 46.721  10.252  38.570  1.00 42.12 ? 90  ASP C C   1 
ATOM   2775 O O   . ASP C 1 90  ? 46.720  11.012  37.594  1.00 41.82 ? 90  ASP C O   1 
ATOM   2776 C CB  . ASP C 1 90  ? 45.478  8.235   39.510  1.00 42.09 ? 90  ASP C CB  1 
ATOM   2777 C CG  . ASP C 1 90  ? 45.848  7.347   38.328  1.00 42.33 ? 90  ASP C CG  1 
ATOM   2778 O OD1 . ASP C 1 90  ? 46.243  7.868   37.264  1.00 42.48 ? 90  ASP C OD1 1 
ATOM   2779 O OD2 . ASP C 1 90  ? 45.736  6.111   38.470  1.00 42.43 ? 90  ASP C OD2 1 
ATOM   2780 N N   . LYS C 1 91  ? 47.829  9.859   39.206  1.00 42.26 ? 91  LYS C N   1 
ATOM   2781 C CA  . LYS C 1 91  ? 49.187  10.179  38.747  1.00 42.48 ? 91  LYS C CA  1 
ATOM   2782 C C   . LYS C 1 91  ? 49.485  9.706   37.323  1.00 42.56 ? 91  LYS C C   1 
ATOM   2783 O O   . LYS C 1 91  ? 50.162  10.406  36.572  1.00 42.63 ? 91  LYS C O   1 
ATOM   2784 C CB  . LYS C 1 91  ? 50.244  9.594   39.709  1.00 42.60 ? 91  LYS C CB  1 
ATOM   2785 C CG  . LYS C 1 91  ? 50.067  8.103   40.049  1.00 42.83 ? 91  LYS C CG  1 
ATOM   2786 C CD  . LYS C 1 91  ? 51.244  7.540   40.852  1.00 42.90 ? 91  LYS C CD  1 
ATOM   2787 C CE  . LYS C 1 91  ? 52.452  7.238   39.973  1.00 43.27 ? 91  LYS C CE  1 
ATOM   2788 N NZ  . LYS C 1 91  ? 53.346  6.214   40.582  1.00 43.14 ? 91  LYS C NZ  1 
ATOM   2789 N N   . ASP C 1 92  ? 48.980  8.526   36.960  1.00 42.51 ? 92  ASP C N   1 
ATOM   2790 C CA  . ASP C 1 92  ? 49.224  7.942   35.633  1.00 42.38 ? 92  ASP C CA  1 
ATOM   2791 C C   . ASP C 1 92  ? 48.213  8.404   34.587  1.00 42.23 ? 92  ASP C C   1 
ATOM   2792 O O   . ASP C 1 92  ? 48.219  7.914   33.455  1.00 42.21 ? 92  ASP C O   1 
ATOM   2793 C CB  . ASP C 1 92  ? 49.229  6.411   35.724  1.00 42.54 ? 92  ASP C CB  1 
ATOM   2794 C CG  . ASP C 1 92  ? 50.404  5.879   36.538  1.00 42.73 ? 92  ASP C CG  1 
ATOM   2795 O OD1 . ASP C 1 92  ? 51.557  6.307   36.291  1.00 42.78 ? 92  ASP C OD1 1 
ATOM   2796 O OD2 . ASP C 1 92  ? 50.170  5.028   37.423  1.00 42.74 ? 92  ASP C OD2 1 
ATOM   2797 N N   . GLY C 1 93  ? 47.347  9.343   34.974  1.00 42.03 ? 93  GLY C N   1 
ATOM   2798 C CA  . GLY C 1 93  ? 46.386  9.968   34.066  1.00 41.72 ? 93  GLY C CA  1 
ATOM   2799 C C   . GLY C 1 93  ? 45.090  9.200   33.913  1.00 41.45 ? 93  GLY C C   1 
ATOM   2800 O O   . GLY C 1 93  ? 44.292  9.505   33.022  1.00 41.14 ? 93  GLY C O   1 
ATOM   2801 N N   . VAL C 1 94  ? 44.875  8.214   34.784  1.00 41.18 ? 94  VAL C N   1 
ATOM   2802 C CA  . VAL C 1 94  ? 43.713  7.340   34.690  1.00 41.32 ? 94  VAL C CA  1 
ATOM   2803 C C   . VAL C 1 94  ? 42.648  7.749   35.702  1.00 41.34 ? 94  VAL C C   1 
ATOM   2804 O O   . VAL C 1 94  ? 42.944  7.938   36.878  1.00 41.24 ? 94  VAL C O   1 
ATOM   2805 C CB  . VAL C 1 94  ? 44.098  5.859   34.910  1.00 41.16 ? 94  VAL C CB  1 
ATOM   2806 C CG1 . VAL C 1 94  ? 42.873  4.957   34.773  1.00 40.93 ? 94  VAL C CG1 1 
ATOM   2807 C CG2 . VAL C 1 94  ? 45.175  5.442   33.918  1.00 40.96 ? 94  VAL C CG2 1 
ATOM   2808 N N   . ALA C 1 95  ? 41.410  7.890   35.224  1.00 41.70 ? 95  ALA C N   1 
ATOM   2809 C CA  . ALA C 1 95  ? 40.255  8.162   36.075  1.00 41.79 ? 95  ALA C CA  1 
ATOM   2810 C C   . ALA C 1 95  ? 39.278  7.004   35.995  1.00 41.92 ? 95  ALA C C   1 
ATOM   2811 O O   . ALA C 1 95  ? 38.651  6.793   34.962  1.00 41.94 ? 95  ALA C O   1 
ATOM   2812 C CB  . ALA C 1 95  ? 39.564  9.454   35.645  1.00 41.82 ? 95  ALA C CB  1 
ATOM   2813 N N   . ASP C 1 96  ? 39.148  6.255   37.085  1.00 42.18 ? 96  ASP C N   1 
ATOM   2814 C CA  . ASP C 1 96  ? 38.096  5.249   37.186  1.00 42.41 ? 96  ASP C CA  1 
ATOM   2815 C C   . ASP C 1 96  ? 36.851  5.942   37.726  1.00 42.31 ? 96  ASP C C   1 
ATOM   2816 O O   . ASP C 1 96  ? 36.879  6.545   38.795  1.00 42.71 ? 96  ASP C O   1 
ATOM   2817 C CB  . ASP C 1 96  ? 38.519  4.067   38.065  1.00 42.72 ? 96  ASP C CB  1 
ATOM   2818 C CG  . ASP C 1 96  ? 39.620  3.213   37.414  1.00 43.57 ? 96  ASP C CG  1 
ATOM   2819 O OD1 . ASP C 1 96  ? 39.524  2.917   36.197  1.00 44.74 ? 96  ASP C OD1 1 
ATOM   2820 O OD2 . ASP C 1 96  ? 40.588  2.836   38.122  1.00 43.45 ? 96  ASP C OD2 1 
ATOM   2821 N N   . VAL C 1 97  ? 35.773  5.877   36.953  1.00 41.95 ? 97  VAL C N   1 
ATOM   2822 C CA  . VAL C 1 97  ? 34.537  6.580   37.260  1.00 41.72 ? 97  VAL C CA  1 
ATOM   2823 C C   . VAL C 1 97  ? 33.556  5.652   37.953  1.00 41.42 ? 97  VAL C C   1 
ATOM   2824 O O   . VAL C 1 97  ? 33.365  4.508   37.527  1.00 41.10 ? 97  VAL C O   1 
ATOM   2825 C CB  . VAL C 1 97  ? 33.878  7.138   35.976  1.00 41.69 ? 97  VAL C CB  1 
ATOM   2826 C CG1 . VAL C 1 97  ? 32.553  7.805   36.303  1.00 41.19 ? 97  VAL C CG1 1 
ATOM   2827 C CG2 . VAL C 1 97  ? 34.837  8.122   35.266  1.00 41.91 ? 97  VAL C CG2 1 
ATOM   2828 N N   . SER C 1 98  ? 32.957  6.151   39.033  1.00 41.31 ? 98  SER C N   1 
ATOM   2829 C CA  . SER C 1 98  ? 31.849  5.474   39.700  1.00 41.40 ? 98  SER C CA  1 
ATOM   2830 C C   . SER C 1 98  ? 30.892  6.507   40.290  1.00 41.52 ? 98  SER C C   1 
ATOM   2831 O O   . SER C 1 98  ? 31.150  7.077   41.352  1.00 41.61 ? 98  SER C O   1 
ATOM   2832 C CB  . SER C 1 98  ? 32.352  4.523   40.782  1.00 41.44 ? 98  SER C CB  1 
ATOM   2833 O OG  . SER C 1 98  ? 31.277  3.770   41.309  1.00 41.27 ? 98  SER C OG  1 
ATOM   2834 N N   . ILE C 1 99  ? 29.791  6.734   39.581  1.00 41.41 ? 99  ILE C N   1 
ATOM   2835 C CA  . ILE C 1 99  ? 28.827  7.780   39.895  1.00 41.53 ? 99  ILE C CA  1 
ATOM   2836 C C   . ILE C 1 99  ? 27.436  7.155   39.933  1.00 41.49 ? 99  ILE C C   1 
ATOM   2837 O O   . ILE C 1 99  ? 27.181  6.149   39.260  1.00 41.64 ? 99  ILE C O   1 
ATOM   2838 C CB  . ILE C 1 99  ? 28.870  8.879   38.805  1.00 41.64 ? 99  ILE C CB  1 
ATOM   2839 C CG1 . ILE C 1 99  ? 30.173  9.671   38.911  1.00 42.02 ? 99  ILE C CG1 1 
ATOM   2840 C CG2 . ILE C 1 99  ? 27.661  9.829   38.888  1.00 41.80 ? 99  ILE C CG2 1 
ATOM   2841 C CD1 . ILE C 1 99  ? 30.459  10.552  37.699  1.00 42.28 ? 99  ILE C CD1 1 
ATOM   2842 N N   . GLU C 1 100 ? 26.554  7.725   40.747  1.00 41.21 ? 100 GLU C N   1 
ATOM   2843 C CA  . GLU C 1 100 ? 25.131  7.396   40.700  1.00 41.16 ? 100 GLU C CA  1 
ATOM   2844 C C   . GLU C 1 100 ? 24.366  8.712   40.674  1.00 41.03 ? 100 GLU C C   1 
ATOM   2845 O O   . GLU C 1 100 ? 24.634  9.605   41.475  1.00 41.01 ? 100 GLU C O   1 
ATOM   2846 C CB  . GLU C 1 100 ? 24.727  6.534   41.897  1.00 41.11 ? 100 GLU C CB  1 
ATOM   2847 C CG  . GLU C 1 100 ? 23.241  6.233   41.966  1.00 41.34 ? 100 GLU C CG  1 
ATOM   2848 C CD  . GLU C 1 100 ? 22.899  5.146   42.970  0.50 41.21 ? 100 GLU C CD  1 
ATOM   2849 O OE1 . GLU C 1 100 ? 23.515  4.060   42.905  0.50 41.60 ? 100 GLU C OE1 1 
ATOM   2850 O OE2 . GLU C 1 100 ? 22.004  5.377   43.812  0.50 40.44 ? 100 GLU C OE2 1 
ATOM   2851 N N   . ASP C 1 101 ? 23.442  8.849   39.727  1.00 41.13 ? 101 ASP C N   1 
ATOM   2852 C CA  . ASP C 1 101 ? 22.704  10.097  39.563  1.00 40.84 ? 101 ASP C CA  1 
ATOM   2853 C C   . ASP C 1 101 ? 21.207  9.838   39.438  1.00 40.40 ? 101 ASP C C   1 
ATOM   2854 O O   . ASP C 1 101 ? 20.786  8.850   38.847  1.00 40.03 ? 101 ASP C O   1 
ATOM   2855 C CB  . ASP C 1 101 ? 23.223  10.870  38.341  1.00 41.24 ? 101 ASP C CB  1 
ATOM   2856 C CG  . ASP C 1 101 ? 22.718  12.320  38.302  1.00 41.90 ? 101 ASP C CG  1 
ATOM   2857 O OD1 . ASP C 1 101 ? 23.222  13.160  39.085  1.00 44.13 ? 101 ASP C OD1 1 
ATOM   2858 O OD2 . ASP C 1 101 ? 21.812  12.616  37.489  1.00 43.40 ? 101 ASP C OD2 1 
ATOM   2859 N N   . SER C 1 102 ? 20.417  10.737  40.013  1.00 40.10 ? 102 SER C N   1 
ATOM   2860 C CA  . SER C 1 102 ? 18.971  10.627  40.013  1.00 40.13 ? 102 SER C CA  1 
ATOM   2861 C C   . SER C 1 102 ? 18.260  11.688  39.188  1.00 39.66 ? 102 SER C C   1 
ATOM   2862 O O   . SER C 1 102 ? 17.037  11.674  39.111  1.00 39.81 ? 102 SER C O   1 
ATOM   2863 C CB  . SER C 1 102 ? 18.452  10.677  41.448  1.00 40.47 ? 102 SER C CB  1 
ATOM   2864 O OG  . SER C 1 102 ? 18.359  9.361   41.955  1.00 42.57 ? 102 SER C OG  1 
ATOM   2865 N N   . VAL C 1 103 ? 19.007  12.600  38.574  1.00 39.15 ? 103 VAL C N   1 
ATOM   2866 C CA  . VAL C 1 103 ? 18.417  13.615  37.723  1.00 38.92 ? 103 VAL C CA  1 
ATOM   2867 C C   . VAL C 1 103 ? 18.392  13.150  36.268  1.00 38.85 ? 103 VAL C C   1 
ATOM   2868 O O   . VAL C 1 103 ? 17.392  13.345  35.581  1.00 39.12 ? 103 VAL C O   1 
ATOM   2869 C CB  . VAL C 1 103 ? 19.159  14.948  37.838  1.00 38.80 ? 103 VAL C CB  1 
ATOM   2870 C CG1 . VAL C 1 103 ? 18.523  15.997  36.926  1.00 38.72 ? 103 VAL C CG1 1 
ATOM   2871 C CG2 . VAL C 1 103 ? 19.147  15.421  39.281  1.00 38.81 ? 103 VAL C CG2 1 
ATOM   2872 N N   . ILE C 1 104 ? 19.482  12.551  35.792  1.00 38.71 ? 104 ILE C N   1 
ATOM   2873 C CA  . ILE C 1 104 ? 19.509  12.020  34.428  1.00 38.59 ? 104 ILE C CA  1 
ATOM   2874 C C   . ILE C 1 104 ? 18.669  10.747  34.329  1.00 38.66 ? 104 ILE C C   1 
ATOM   2875 O O   . ILE C 1 104 ? 18.443  10.061  35.334  1.00 38.19 ? 104 ILE C O   1 
ATOM   2876 C CB  . ILE C 1 104 ? 20.956  11.724  33.904  1.00 38.78 ? 104 ILE C CB  1 
ATOM   2877 C CG1 . ILE C 1 104 ? 21.714  10.729  34.804  1.00 38.58 ? 104 ILE C CG1 1 
ATOM   2878 C CG2 . ILE C 1 104 ? 21.750  13.019  33.757  1.00 38.39 ? 104 ILE C CG2 1 
ATOM   2879 C CD1 . ILE C 1 104 ? 22.970  10.139  34.163  1.00 38.62 ? 104 ILE C CD1 1 
ATOM   2880 N N   . SER C 1 105 ? 18.226  10.432  33.114  1.00 38.61 ? 105 SER C N   1 
ATOM   2881 C CA  . SER C 1 105 ? 17.528  9.168   32.845  1.00 38.91 ? 105 SER C CA  1 
ATOM   2882 C C   . SER C 1 105 ? 17.923  8.606   31.472  1.00 39.00 ? 105 SER C C   1 
ATOM   2883 O O   . SER C 1 105 ? 18.267  9.362   30.562  1.00 39.05 ? 105 SER C O   1 
ATOM   2884 C CB  . SER C 1 105 ? 16.017  9.386   32.926  1.00 38.92 ? 105 SER C CB  1 
ATOM   2885 O OG  . SER C 1 105 ? 15.312  8.160   32.934  1.00 38.88 ? 105 SER C OG  1 
ATOM   2886 N N   . LEU C 1 106 ? 17.896  7.282   31.336  1.00 38.97 ? 106 LEU C N   1 
ATOM   2887 C CA  . LEU C 1 106 ? 18.125  6.639   30.046  1.00 39.34 ? 106 LEU C CA  1 
ATOM   2888 C C   . LEU C 1 106 ? 16.840  6.496   29.214  1.00 39.76 ? 106 LEU C C   1 
ATOM   2889 O O   . LEU C 1 106 ? 16.898  6.040   28.073  1.00 40.03 ? 106 LEU C O   1 
ATOM   2890 C CB  . LEU C 1 106 ? 18.802  5.271   30.220  1.00 39.49 ? 106 LEU C CB  1 
ATOM   2891 C CG  . LEU C 1 106 ? 20.171  5.236   30.925  1.00 39.55 ? 106 LEU C CG  1 
ATOM   2892 C CD1 . LEU C 1 106 ? 20.776  3.854   30.812  1.00 40.43 ? 106 LEU C CD1 1 
ATOM   2893 C CD2 . LEU C 1 106 ? 21.140  6.277   30.380  1.00 40.69 ? 106 LEU C CD2 1 
ATOM   2894 N N   . SER C 1 107 ? 15.696  6.897   29.774  1.00 40.10 ? 107 SER C N   1 
ATOM   2895 C CA  . SER C 1 107 ? 14.422  6.862   29.064  1.00 40.29 ? 107 SER C CA  1 
ATOM   2896 C C   . SER C 1 107 ? 13.615  8.141   29.323  1.00 40.48 ? 107 SER C C   1 
ATOM   2897 O O   . SER C 1 107 ? 14.018  8.996   30.113  1.00 39.67 ? 107 SER C O   1 
ATOM   2898 C CB  . SER C 1 107 ? 13.615  5.616   29.464  1.00 40.56 ? 107 SER C CB  1 
ATOM   2899 O OG  . SER C 1 107 ? 13.366  5.566   30.864  1.00 41.19 ? 107 SER C OG  1 
ATOM   2900 N N   . GLY C 1 108 ? 12.491  8.268   28.616  1.00 41.07 ? 108 GLY C N   1 
ATOM   2901 C CA  . GLY C 1 108 ? 11.604  9.428   28.733  1.00 41.53 ? 108 GLY C CA  1 
ATOM   2902 C C   . GLY C 1 108 ? 11.966  10.507  27.743  1.00 41.93 ? 108 GLY C C   1 
ATOM   2903 O O   . GLY C 1 108 ? 12.937  10.374  27.012  1.00 42.35 ? 108 GLY C O   1 
ATOM   2904 N N   . ASP C 1 109 ? 11.190  11.589  27.735  1.00 42.61 ? 109 ASP C N   1 
ATOM   2905 C CA  . ASP C 1 109 ? 11.387  12.696  26.784  1.00 42.74 ? 109 ASP C CA  1 
ATOM   2906 C C   . ASP C 1 109 ? 12.698  13.439  26.990  1.00 42.66 ? 109 ASP C C   1 
ATOM   2907 O O   . ASP C 1 109 ? 13.162  14.122  26.083  1.00 42.89 ? 109 ASP C O   1 
ATOM   2908 C CB  . ASP C 1 109 ? 10.229  13.703  26.864  1.00 42.95 ? 109 ASP C CB  1 
ATOM   2909 C CG  . ASP C 1 109 ? 8.950   13.167  26.263  1.00 44.11 ? 109 ASP C CG  1 
ATOM   2910 O OD1 . ASP C 1 109 ? 9.001   12.082  25.642  1.00 46.69 ? 109 ASP C OD1 1 
ATOM   2911 O OD2 . ASP C 1 109 ? 7.893   13.822  26.403  1.00 44.07 ? 109 ASP C OD2 1 
ATOM   2912 N N   . HIS C 1 110 ? 13.283  13.319  28.178  1.00 42.49 ? 110 HIS C N   1 
ATOM   2913 C CA  . HIS C 1 110 ? 14.549  13.977  28.481  1.00 42.12 ? 110 HIS C CA  1 
ATOM   2914 C C   . HIS C 1 110 ? 15.706  12.991  28.654  1.00 41.80 ? 110 HIS C C   1 
ATOM   2915 O O   . HIS C 1 110 ? 16.734  13.322  29.243  1.00 42.10 ? 110 HIS C O   1 
ATOM   2916 C CB  . HIS C 1 110 ? 14.369  14.860  29.709  1.00 42.28 ? 110 HIS C CB  1 
ATOM   2917 C CG  . HIS C 1 110 ? 13.299  15.892  29.537  1.00 42.57 ? 110 HIS C CG  1 
ATOM   2918 N ND1 . HIS C 1 110 ? 12.265  16.055  30.431  1.00 42.60 ? 110 HIS C ND1 1 
ATOM   2919 C CD2 . HIS C 1 110 ? 13.086  16.792  28.548  1.00 43.06 ? 110 HIS C CD2 1 
ATOM   2920 C CE1 . HIS C 1 110 ? 11.473  17.026  30.012  1.00 42.84 ? 110 HIS C CE1 1 
ATOM   2921 N NE2 . HIS C 1 110 ? 11.951  17.492  28.873  1.00 42.60 ? 110 HIS C NE2 1 
ATOM   2922 N N   . ALA C 1 111 ? 15.543  11.788  28.107  1.00 41.53 ? 111 ALA C N   1 
ATOM   2923 C CA  . ALA C 1 111 ? 16.593  10.774  28.098  1.00 41.07 ? 111 ALA C CA  1 
ATOM   2924 C C   . ALA C 1 111 ? 17.899  11.344  27.572  1.00 40.85 ? 111 ALA C C   1 
ATOM   2925 O O   . ALA C 1 111 ? 17.891  12.194  26.683  1.00 40.45 ? 111 ALA C O   1 
ATOM   2926 C CB  . ALA C 1 111 ? 16.173  9.608   27.236  1.00 40.61 ? 111 ALA C CB  1 
ATOM   2927 N N   . ILE C 1 112 ? 19.019  10.845  28.095  1.00 40.87 ? 112 ILE C N   1 
ATOM   2928 C CA  . ILE C 1 112 ? 20.349  11.288  27.633  1.00 40.79 ? 112 ILE C CA  1 
ATOM   2929 C C   . ILE C 1 112 ? 20.862  10.491  26.426  1.00 40.39 ? 112 ILE C C   1 
ATOM   2930 O O   . ILE C 1 112 ? 21.932  10.774  25.906  1.00 39.96 ? 112 ILE C O   1 
ATOM   2931 C CB  . ILE C 1 112 ? 21.392  11.266  28.765  1.00 40.82 ? 112 ILE C CB  1 
ATOM   2932 C CG1 . ILE C 1 112 ? 21.641  9.838   29.269  1.00 41.49 ? 112 ILE C CG1 1 
ATOM   2933 C CG2 . ILE C 1 112 ? 20.934  12.174  29.887  1.00 41.26 ? 112 ILE C CG2 1 
ATOM   2934 C CD1 . ILE C 1 112 ? 22.740  9.727   30.325  1.00 41.30 ? 112 ILE C CD1 1 
ATOM   2935 N N   . ILE C 1 113 ? 20.079  9.511   25.984  1.00 40.30 ? 113 ILE C N   1 
ATOM   2936 C CA  . ILE C 1 113 ? 20.399  8.723   24.799  1.00 39.89 ? 113 ILE C CA  1 
ATOM   2937 C C   . ILE C 1 113 ? 20.401  9.609   23.553  1.00 39.56 ? 113 ILE C C   1 
ATOM   2938 O O   . ILE C 1 113 ? 19.483  10.402  23.340  1.00 39.32 ? 113 ILE C O   1 
ATOM   2939 C CB  . ILE C 1 113 ? 19.369  7.601   24.580  1.00 40.01 ? 113 ILE C CB  1 
ATOM   2940 C CG1 . ILE C 1 113 ? 19.256  6.699   25.820  1.00 40.63 ? 113 ILE C CG1 1 
ATOM   2941 C CG2 . ILE C 1 113 ? 19.717  6.800   23.346  1.00 40.07 ? 113 ILE C CG2 1 
ATOM   2942 C CD1 . ILE C 1 113 ? 20.500  5.920   26.180  1.00 40.24 ? 113 ILE C CD1 1 
ATOM   2943 N N   . GLY C 1 114 ? 21.443  9.470   22.735  1.00 39.22 ? 114 GLY C N   1 
ATOM   2944 C CA  . GLY C 1 114 ? 21.615  10.304  21.549  1.00 38.86 ? 114 GLY C CA  1 
ATOM   2945 C C   . GLY C 1 114 ? 22.231  11.657  21.838  1.00 38.87 ? 114 GLY C C   1 
ATOM   2946 O O   . GLY C 1 114 ? 22.327  12.504  20.953  1.00 38.72 ? 114 GLY C O   1 
ATOM   2947 N N   . ARG C 1 115 ? 22.624  11.888  23.086  1.00 38.92 ? 115 ARG C N   1 
ATOM   2948 C CA  . ARG C 1 115 ? 23.269  13.134  23.460  1.00 38.61 ? 115 ARG C CA  1 
ATOM   2949 C C   . ARG C 1 115 ? 24.739  12.806  23.696  1.00 38.54 ? 115 ARG C C   1 
ATOM   2950 O O   . ARG C 1 115 ? 25.152  11.692  23.446  1.00 37.97 ? 115 ARG C O   1 
ATOM   2951 C CB  . ARG C 1 115 ? 22.587  13.752  24.683  1.00 38.45 ? 115 ARG C CB  1 
ATOM   2952 C CG  . ARG C 1 115 ? 21.078  13.794  24.544  1.00 38.64 ? 115 ARG C CG  1 
ATOM   2953 C CD  . ARG C 1 115 ? 20.420  14.808  25.463  1.00 38.72 ? 115 ARG C CD  1 
ATOM   2954 N NE  . ARG C 1 115 ? 18.968  14.839  25.254  1.00 38.83 ? 115 ARG C NE  1 
ATOM   2955 C CZ  . ARG C 1 115 ? 18.320  15.677  24.440  1.00 39.04 ? 115 ARG C CZ  1 
ATOM   2956 N NH1 . ARG C 1 115 ? 18.964  16.607  23.740  1.00 39.85 ? 115 ARG C NH1 1 
ATOM   2957 N NH2 . ARG C 1 115 ? 16.997  15.608  24.337  1.00 38.06 ? 115 ARG C NH2 1 
ATOM   2958 N N   . THR C 1 116 ? 25.535  13.781  24.133  1.00 38.60 ? 116 THR C N   1 
ATOM   2959 C CA  . THR C 1 116 ? 26.991  13.613  24.172  1.00 38.36 ? 116 THR C CA  1 
ATOM   2960 C C   . THR C 1 116 ? 27.530  13.722  25.594  1.00 38.35 ? 116 THR C C   1 
ATOM   2961 O O   . THR C 1 116 ? 27.166  14.630  26.321  1.00 37.93 ? 116 THR C O   1 
ATOM   2962 C CB  . THR C 1 116 ? 27.688  14.640  23.272  1.00 38.45 ? 116 THR C CB  1 
ATOM   2963 O OG1 . THR C 1 116 ? 27.303  14.424  21.912  1.00 36.86 ? 116 THR C OG1 1 
ATOM   2964 C CG2 . THR C 1 116 ? 29.212  14.511  23.369  1.00 38.93 ? 116 THR C CG2 1 
ATOM   2965 N N   . LEU C 1 117 ? 28.365  12.760  25.987  1.00 38.35 ? 117 LEU C N   1 
ATOM   2966 C CA  . LEU C 1 117 ? 29.126  12.842  27.242  1.00 38.69 ? 117 LEU C CA  1 
ATOM   2967 C C   . LEU C 1 117 ? 30.485  13.472  26.952  1.00 38.81 ? 117 LEU C C   1 
ATOM   2968 O O   . LEU C 1 117 ? 31.210  12.990  26.091  1.00 38.74 ? 117 LEU C O   1 
ATOM   2969 C CB  . LEU C 1 117 ? 29.332  11.443  27.818  1.00 38.18 ? 117 LEU C CB  1 
ATOM   2970 C CG  . LEU C 1 117 ? 30.124  11.247  29.109  1.00 37.69 ? 117 LEU C CG  1 
ATOM   2971 C CD1 . LEU C 1 117 ? 29.343  11.793  30.258  1.00 37.57 ? 117 LEU C CD1 1 
ATOM   2972 C CD2 . LEU C 1 117 ? 30.417  9.738   29.326  1.00 38.96 ? 117 LEU C CD2 1 
ATOM   2973 N N   . VAL C 1 118 ? 30.815  14.543  27.664  1.00 39.44 ? 118 VAL C N   1 
ATOM   2974 C CA  . VAL C 1 118 ? 32.073  15.269  27.479  1.00 39.47 ? 118 VAL C CA  1 
ATOM   2975 C C   . VAL C 1 118 ? 32.880  15.249  28.784  1.00 39.59 ? 118 VAL C C   1 
ATOM   2976 O O   . VAL C 1 118 ? 32.321  15.371  29.876  1.00 39.58 ? 118 VAL C O   1 
ATOM   2977 C CB  . VAL C 1 118 ? 31.820  16.746  27.052  1.00 39.54 ? 118 VAL C CB  1 
ATOM   2978 C CG1 . VAL C 1 118 ? 33.133  17.492  26.865  1.00 39.84 ? 118 VAL C CG1 1 
ATOM   2979 C CG2 . VAL C 1 118 ? 30.993  16.814  25.754  1.00 39.83 ? 118 VAL C CG2 1 
ATOM   2980 N N   . VAL C 1 119 ? 34.192  15.062  28.665  1.00 40.02 ? 119 VAL C N   1 
ATOM   2981 C CA  . VAL C 1 119 ? 35.103  15.294  29.777  1.00 40.25 ? 119 VAL C CA  1 
ATOM   2982 C C   . VAL C 1 119 ? 35.935  16.536  29.439  1.00 40.36 ? 119 VAL C C   1 
ATOM   2983 O O   . VAL C 1 119 ? 36.475  16.666  28.345  1.00 39.64 ? 119 VAL C O   1 
ATOM   2984 C CB  . VAL C 1 119 ? 35.967  14.049  30.141  1.00 40.54 ? 119 VAL C CB  1 
ATOM   2985 C CG1 . VAL C 1 119 ? 36.692  13.470  28.933  1.00 41.31 ? 119 VAL C CG1 1 
ATOM   2986 C CG2 . VAL C 1 119 ? 36.957  14.384  31.279  1.00 40.30 ? 119 VAL C CG2 1 
ATOM   2987 N N   . HIS C 1 120 ? 35.993  17.462  30.388  1.00 40.90 ? 120 HIS C N   1 
ATOM   2988 C CA  . HIS C 1 120 ? 36.521  18.791  30.136  1.00 41.43 ? 120 HIS C CA  1 
ATOM   2989 C C   . HIS C 1 120 ? 37.934  18.933  30.661  1.00 42.06 ? 120 HIS C C   1 
ATOM   2990 O O   . HIS C 1 120 ? 38.407  18.124  31.454  1.00 41.83 ? 120 HIS C O   1 
ATOM   2991 C CB  . HIS C 1 120 ? 35.615  19.842  30.761  1.00 41.20 ? 120 HIS C CB  1 
ATOM   2992 C CG  . HIS C 1 120 ? 34.271  19.928  30.113  1.00 41.13 ? 120 HIS C CG  1 
ATOM   2993 N ND1 . HIS C 1 120 ? 33.889  20.998  29.333  1.00 40.98 ? 120 HIS C ND1 1 
ATOM   2994 C CD2 . HIS C 1 120 ? 33.222  19.073  30.123  1.00 40.76 ? 120 HIS C CD2 1 
ATOM   2995 C CE1 . HIS C 1 120 ? 32.661  20.796  28.890  1.00 41.80 ? 120 HIS C CE1 1 
ATOM   2996 N NE2 . HIS C 1 120 ? 32.236  19.631  29.349  1.00 40.32 ? 120 HIS C NE2 1 
ATOM   2997 N N   . GLU C 1 121 ? 38.599  19.982  30.198  1.00 43.38 ? 121 GLU C N   1 
ATOM   2998 C CA  . GLU C 1 121 ? 39.986  20.243  30.554  1.00 44.02 ? 121 GLU C CA  1 
ATOM   2999 C C   . GLU C 1 121 ? 40.128  20.515  32.044  1.00 44.46 ? 121 GLU C C   1 
ATOM   3000 O O   . GLU C 1 121 ? 40.996  19.945  32.704  1.00 44.45 ? 121 GLU C O   1 
ATOM   3001 C CB  . GLU C 1 121 ? 40.513  21.432  29.754  1.00 44.25 ? 121 GLU C CB  1 
ATOM   3002 C CG  . GLU C 1 121 ? 42.018  21.513  29.689  1.00 44.45 ? 121 GLU C CG  1 
ATOM   3003 C CD  . GLU C 1 121 ? 42.501  22.717  28.895  1.00 45.62 ? 121 GLU C CD  1 
ATOM   3004 O OE1 . GLU C 1 121 ? 41.650  23.509  28.419  1.00 48.84 ? 121 GLU C OE1 1 
ATOM   3005 O OE2 . GLU C 1 121 ? 43.737  22.879  28.758  1.00 47.09 ? 121 GLU C OE2 1 
ATOM   3006 N N   . LYS C 1 122 ? 39.259  21.378  32.563  1.00 44.88 ? 122 LYS C N   1 
ATOM   3007 C CA  . LYS C 1 122 ? 39.352  21.832  33.939  1.00 45.51 ? 122 LYS C CA  1 
ATOM   3008 C C   . LYS C 1 122 ? 38.227  21.245  34.771  1.00 45.85 ? 122 LYS C C   1 
ATOM   3009 O O   . LYS C 1 122 ? 37.325  20.593  34.246  1.00 45.81 ? 122 LYS C O   1 
ATOM   3010 C CB  . LYS C 1 122 ? 39.293  23.363  33.987  1.00 45.53 ? 122 LYS C CB  1 
ATOM   3011 C CG  . LYS C 1 122 ? 40.381  24.058  33.159  1.00 45.99 ? 122 LYS C CG  1 
ATOM   3012 C CD  . LYS C 1 122 ? 40.071  25.539  32.938  1.00 45.99 ? 122 LYS C CD  1 
ATOM   3013 C CE  . LYS C 1 122 ? 40.926  26.125  31.819  1.00 46.59 ? 122 LYS C CE  1 
ATOM   3014 N NZ  . LYS C 1 122 ? 40.706  27.600  31.645  1.00 46.85 ? 122 LYS C NZ  1 
ATOM   3015 N N   . ALA C 1 123 ? 38.302  21.470  36.080  1.00 46.47 ? 123 ALA C N   1 
ATOM   3016 C CA  . ALA C 1 123 ? 37.197  21.178  36.985  1.00 47.00 ? 123 ALA C CA  1 
ATOM   3017 C C   . ALA C 1 123 ? 36.114  22.237  36.780  1.00 47.48 ? 123 ALA C C   1 
ATOM   3018 O O   . ALA C 1 123 ? 36.424  23.402  36.501  1.00 47.65 ? 123 ALA C O   1 
ATOM   3019 C CB  . ALA C 1 123 ? 37.686  21.185  38.428  1.00 46.95 ? 123 ALA C CB  1 
ATOM   3020 N N   . ASP C 1 124 ? 34.850  21.843  36.912  1.00 48.07 ? 124 ASP C N   1 
ATOM   3021 C CA  . ASP C 1 124 ? 33.741  22.801  36.767  1.00 48.57 ? 124 ASP C CA  1 
ATOM   3022 C C   . ASP C 1 124 ? 33.494  23.574  38.063  1.00 48.58 ? 124 ASP C C   1 
ATOM   3023 O O   . ASP C 1 124 ? 34.342  23.597  38.958  1.00 48.65 ? 124 ASP C O   1 
ATOM   3024 C CB  . ASP C 1 124 ? 32.455  22.101  36.293  1.00 48.93 ? 124 ASP C CB  1 
ATOM   3025 C CG  . ASP C 1 124 ? 31.939  21.069  37.288  1.00 50.03 ? 124 ASP C CG  1 
ATOM   3026 O OD1 . ASP C 1 124 ? 32.625  20.842  38.312  1.00 52.50 ? 124 ASP C OD1 1 
ATOM   3027 O OD2 . ASP C 1 124 ? 30.853  20.476  37.048  1.00 49.97 ? 124 ASP C OD2 1 
ATOM   3028 N N   . SER C 1 142 ? 37.975  23.781  28.175  1.00 44.29 ? 142 SER C N   1 
ATOM   3029 C CA  . SER C 1 142 ? 37.671  23.214  26.869  1.00 44.15 ? 142 SER C CA  1 
ATOM   3030 C C   . SER C 1 142 ? 37.337  21.720  27.007  1.00 43.96 ? 142 SER C C   1 
ATOM   3031 O O   . SER C 1 142 ? 37.235  21.203  28.119  1.00 43.79 ? 142 SER C O   1 
ATOM   3032 C CB  . SER C 1 142 ? 38.841  23.445  25.897  1.00 44.49 ? 142 SER C CB  1 
ATOM   3033 O OG  . SER C 1 142 ? 39.842  22.441  26.016  1.00 45.51 ? 142 SER C OG  1 
ATOM   3034 N N   . ARG C 1 143 ? 37.169  21.037  25.879  1.00 43.67 ? 143 ARG C N   1 
ATOM   3035 C CA  . ARG C 1 143 ? 36.607  19.689  25.864  1.00 43.30 ? 143 ARG C CA  1 
ATOM   3036 C C   . ARG C 1 143 ? 37.617  18.686  25.336  1.00 43.08 ? 143 ARG C C   1 
ATOM   3037 O O   . ARG C 1 143 ? 37.942  18.683  24.149  1.00 43.34 ? 143 ARG C O   1 
ATOM   3038 C CB  . ARG C 1 143 ? 35.343  19.677  25.007  1.00 43.46 ? 143 ARG C CB  1 
ATOM   3039 C CG  . ARG C 1 143 ? 34.367  20.768  25.412  1.00 43.76 ? 143 ARG C CG  1 
ATOM   3040 C CD  . ARG C 1 143 ? 33.097  20.786  24.582  1.00 43.59 ? 143 ARG C CD  1 
ATOM   3041 N NE  . ARG C 1 143 ? 32.300  21.975  24.898  1.00 43.47 ? 143 ARG C NE  1 
ATOM   3042 C CZ  . ARG C 1 143 ? 31.061  22.200  24.467  1.00 43.32 ? 143 ARG C CZ  1 
ATOM   3043 N NH1 . ARG C 1 143 ? 30.451  21.324  23.672  1.00 42.66 ? 143 ARG C NH1 1 
ATOM   3044 N NH2 . ARG C 1 143 ? 30.433  23.315  24.832  1.00 43.50 ? 143 ARG C NH2 1 
ATOM   3045 N N   . LEU C 1 144 ? 38.093  17.819  26.222  1.00 42.41 ? 144 LEU C N   1 
ATOM   3046 C CA  . LEU C 1 144 ? 39.191  16.925  25.905  1.00 41.94 ? 144 LEU C CA  1 
ATOM   3047 C C   . LEU C 1 144 ? 38.735  15.760  25.064  1.00 41.48 ? 144 LEU C C   1 
ATOM   3048 O O   . LEU C 1 144 ? 39.403  15.379  24.112  1.00 41.43 ? 144 LEU C O   1 
ATOM   3049 C CB  . LEU C 1 144 ? 39.824  16.391  27.183  1.00 42.00 ? 144 LEU C CB  1 
ATOM   3050 C CG  . LEU C 1 144 ? 40.360  17.435  28.160  1.00 41.85 ? 144 LEU C CG  1 
ATOM   3051 C CD1 . LEU C 1 144 ? 40.866  16.734  29.403  1.00 41.41 ? 144 LEU C CD1 1 
ATOM   3052 C CD2 . LEU C 1 144 ? 41.441  18.278  27.509  1.00 42.09 ? 144 LEU C CD2 1 
ATOM   3053 N N   . ALA C 1 145 ? 37.604  15.178  25.438  1.00 41.15 ? 145 ALA C N   1 
ATOM   3054 C CA  . ALA C 1 145 ? 37.050  14.044  24.722  1.00 40.76 ? 145 ALA C CA  1 
ATOM   3055 C C   . ALA C 1 145 ? 35.536  14.076  24.808  1.00 40.35 ? 145 ALA C C   1 
ATOM   3056 O O   . ALA C 1 145 ? 34.966  14.662  25.729  1.00 40.46 ? 145 ALA C O   1 
ATOM   3057 C CB  . ALA C 1 145 ? 37.587  12.745  25.293  1.00 40.86 ? 145 ALA C CB  1 
ATOM   3058 N N   . ALA C 1 146 ? 34.893  13.470  23.822  1.00 39.95 ? 146 ALA C N   1 
ATOM   3059 C CA  . ALA C 1 146 ? 33.442  13.418  23.760  1.00 39.82 ? 146 ALA C CA  1 
ATOM   3060 C C   . ALA C 1 146 ? 33.017  12.090  23.173  1.00 39.31 ? 146 ALA C C   1 
ATOM   3061 O O   . ALA C 1 146 ? 33.779  11.444  22.462  1.00 39.25 ? 146 ALA C O   1 
ATOM   3062 C CB  . ALA C 1 146 ? 32.901  14.554  22.915  1.00 39.95 ? 146 ALA C CB  1 
ATOM   3063 N N   . GLY C 1 147 ? 31.782  11.704  23.457  1.00 39.03 ? 147 GLY C N   1 
ATOM   3064 C CA  . GLY C 1 147 ? 31.228  10.450  22.949  1.00 38.74 ? 147 GLY C CA  1 
ATOM   3065 C C   . GLY C 1 147 ? 29.716  10.529  22.954  1.00 38.36 ? 147 GLY C C   1 
ATOM   3066 O O   . GLY C 1 147 ? 29.125  11.045  23.908  1.00 38.37 ? 147 GLY C O   1 
ATOM   3067 N N   . VAL C 1 148 ? 29.093  10.054  21.881  1.00 38.14 ? 148 VAL C N   1 
ATOM   3068 C CA  . VAL C 1 148 ? 27.638  10.031  21.792  1.00 38.33 ? 148 VAL C CA  1 
ATOM   3069 C C   . VAL C 1 148 ? 27.138  8.873   22.631  1.00 38.23 ? 148 VAL C C   1 
ATOM   3070 O O   . VAL C 1 148 ? 27.626  7.738   22.496  1.00 37.91 ? 148 VAL C O   1 
ATOM   3071 C CB  . VAL C 1 148 ? 27.126  9.887   20.335  1.00 38.33 ? 148 VAL C CB  1 
ATOM   3072 C CG1 . VAL C 1 148 ? 25.600  9.851   20.300  1.00 39.12 ? 148 VAL C CG1 1 
ATOM   3073 C CG2 . VAL C 1 148 ? 27.636  11.025  19.463  1.00 39.08 ? 148 VAL C CG2 1 
ATOM   3074 N N   . ILE C 1 149 ? 26.150  9.154   23.476  1.00 38.18 ? 149 ILE C N   1 
ATOM   3075 C CA  . ILE C 1 149 ? 25.576  8.142   24.382  1.00 38.25 ? 149 ILE C CA  1 
ATOM   3076 C C   . ILE C 1 149 ? 24.615  7.226   23.628  1.00 38.36 ? 149 ILE C C   1 
ATOM   3077 O O   . ILE C 1 149 ? 23.551  7.658   23.188  1.00 38.06 ? 149 ILE C O   1 
ATOM   3078 C CB  . ILE C 1 149 ? 24.847  8.805   25.565  1.00 38.44 ? 149 ILE C CB  1 
ATOM   3079 C CG1 . ILE C 1 149 ? 25.812  9.729   26.328  1.00 37.64 ? 149 ILE C CG1 1 
ATOM   3080 C CG2 . ILE C 1 149 ? 24.275  7.742   26.494  1.00 37.78 ? 149 ILE C CG2 1 
ATOM   3081 C CD1 . ILE C 1 149 ? 25.155  10.631  27.342  1.00 38.12 ? 149 ILE C CD1 1 
ATOM   3082 N N   . GLY C 1 150 ? 24.983  5.950   23.503  1.00 38.42 ? 150 GLY C N   1 
ATOM   3083 C CA  . GLY C 1 150 ? 24.241  5.029   22.674  1.00 38.54 ? 150 GLY C CA  1 
ATOM   3084 C C   . GLY C 1 150 ? 23.639  3.874   23.446  1.00 38.90 ? 150 GLY C C   1 
ATOM   3085 O O   . GLY C 1 150 ? 24.119  3.500   24.506  1.00 38.56 ? 150 GLY C O   1 
ATOM   3086 N N   . ILE C 1 151 ? 22.575  3.313   22.893  1.00 38.88 ? 151 ILE C N   1 
ATOM   3087 C CA  . ILE C 1 151 ? 21.891  2.182   23.486  1.00 38.89 ? 151 ILE C CA  1 
ATOM   3088 C C   . ILE C 1 151 ? 22.840  0.985   23.498  1.00 39.23 ? 151 ILE C C   1 
ATOM   3089 O O   . ILE C 1 151 ? 23.439  0.650   22.473  1.00 39.01 ? 151 ILE C O   1 
ATOM   3090 C CB  . ILE C 1 151 ? 20.598  1.866   22.693  1.00 38.90 ? 151 ILE C CB  1 
ATOM   3091 C CG1 . ILE C 1 151 ? 19.566  2.978   22.919  1.00 38.26 ? 151 ILE C CG1 1 
ATOM   3092 C CG2 . ILE C 1 151 ? 20.035  0.493   23.066  1.00 38.83 ? 151 ILE C CG2 1 
ATOM   3093 C CD1 . ILE C 1 151 ? 18.485  3.049   21.864  1.00 38.50 ? 151 ILE C CD1 1 
ATOM   3094 N N   . ALA C 1 152 ? 22.977  0.357   24.664  1.00 39.75 ? 152 ALA C N   1 
ATOM   3095 C CA  . ALA C 1 152 ? 23.841  -0.817  24.842  1.00 39.81 ? 152 ALA C CA  1 
ATOM   3096 C C   . ALA C 1 152 ? 22.996  -2.049  25.109  1.00 40.51 ? 152 ALA C C   1 
ATOM   3097 O O   . ALA C 1 152 ? 21.849  -1.951  25.552  1.00 40.92 ? 152 ALA C O   1 
ATOM   3098 C CB  . ALA C 1 152 ? 24.823  -0.599  25.990  1.00 39.42 ? 152 ALA C CB  1 
ATOM   3099 N N   . GLN C 1 153 ? 23.581  -3.206  24.827  1.00 41.07 ? 153 GLN C N   1 
ATOM   3100 C CA  . GLN C 1 153 ? 22.899  -4.485  24.920  1.00 41.61 ? 153 GLN C CA  1 
ATOM   3101 C C   . GLN C 1 153 ? 22.768  -4.982  26.367  1.00 42.36 ? 153 GLN C C   1 
ATOM   3102 O O   . GLN C 1 153 ? 23.637  -4.714  27.210  1.00 42.68 ? 153 GLN C O   1 
ATOM   3103 C CB  . GLN C 1 153 ? 23.680  -5.512  24.102  1.00 41.75 ? 153 GLN C CB  1 
ATOM   3104 C CG  . GLN C 1 153 ? 22.963  -6.823  23.874  1.00 41.53 ? 153 GLN C CG  1 
ATOM   3105 C CD  . GLN C 1 153 ? 23.694  -7.706  22.868  1.00 42.26 ? 153 GLN C CD  1 
ATOM   3106 O OE1 . GLN C 1 153 ? 24.904  -7.544  22.645  1.00 42.56 ? 153 GLN C OE1 1 
ATOM   3107 N NE2 . GLN C 1 153 ? 22.966  -8.661  22.263  1.00 42.70 ? 153 GLN C NE2 1 
ATOM   3108 O OXT . GLN C 1 153 ? 21.808  -5.695  26.722  1.00 43.17 ? 153 GLN C OXT 1 
ATOM   3109 N N   . THR D 1 2   ? 13.300  15.868  15.794  1.00 42.58 ? 2   THR D N   1 
ATOM   3110 C CA  . THR D 1 2   ? 13.131  16.166  14.338  1.00 42.57 ? 2   THR D CA  1 
ATOM   3111 C C   . THR D 1 2   ? 14.431  16.077  13.531  1.00 42.38 ? 2   THR D C   1 
ATOM   3112 O O   . THR D 1 2   ? 14.374  15.960  12.314  1.00 42.10 ? 2   THR D O   1 
ATOM   3113 C CB  . THR D 1 2   ? 12.467  17.551  14.075  1.00 42.78 ? 2   THR D CB  1 
ATOM   3114 O OG1 . THR D 1 2   ? 13.275  18.608  14.610  1.00 43.99 ? 2   THR D OG1 1 
ATOM   3115 C CG2 . THR D 1 2   ? 11.077  17.620  14.696  1.00 43.16 ? 2   THR D CG2 1 
ATOM   3116 N N   . LYS D 1 3   ? 15.586  16.147  14.195  1.00 42.28 ? 3   LYS D N   1 
ATOM   3117 C CA  . LYS D 1 3   ? 16.883  16.047  13.515  1.00 42.04 ? 3   LYS D CA  1 
ATOM   3118 C C   . LYS D 1 3   ? 17.871  15.149  14.250  1.00 41.79 ? 3   LYS D C   1 
ATOM   3119 O O   . LYS D 1 3   ? 17.868  15.051  15.477  1.00 41.91 ? 3   LYS D O   1 
ATOM   3120 C CB  . LYS D 1 3   ? 17.511  17.434  13.337  1.00 42.18 ? 3   LYS D CB  1 
ATOM   3121 C CG  . LYS D 1 3   ? 16.890  18.260  12.238  1.00 42.31 ? 3   LYS D CG  1 
ATOM   3122 C CD  . LYS D 1 3   ? 17.158  19.747  12.431  1.00 42.28 ? 3   LYS D CD  1 
ATOM   3123 C CE  . LYS D 1 3   ? 16.065  20.596  11.792  1.00 42.90 ? 3   LYS D CE  1 
ATOM   3124 N NZ  . LYS D 1 3   ? 16.225  22.051  12.092  1.00 42.48 ? 3   LYS D NZ  1 
ATOM   3125 N N   . ALA D 1 4   ? 18.729  14.501  13.473  1.00 41.42 ? 4   ALA D N   1 
ATOM   3126 C CA  . ALA D 1 4   ? 19.790  13.683  14.015  1.00 41.11 ? 4   ALA D CA  1 
ATOM   3127 C C   . ALA D 1 4   ? 20.996  13.700  13.076  1.00 40.89 ? 4   ALA D C   1 
ATOM   3128 O O   . ALA D 1 4   ? 20.934  14.282  11.985  1.00 39.75 ? 4   ALA D O   1 
ATOM   3129 C CB  . ALA D 1 4   ? 19.291  12.294  14.223  1.00 40.68 ? 4   ALA D CB  1 
ATOM   3130 N N   . VAL D 1 5   ? 22.090  13.074  13.515  1.00 40.71 ? 5   VAL D N   1 
ATOM   3131 C CA  . VAL D 1 5   ? 23.353  13.072  12.763  1.00 40.84 ? 5   VAL D CA  1 
ATOM   3132 C C   . VAL D 1 5   ? 24.190  11.865  13.171  1.00 41.30 ? 5   VAL D C   1 
ATOM   3133 O O   . VAL D 1 5   ? 24.179  11.467  14.343  1.00 42.18 ? 5   VAL D O   1 
ATOM   3134 C CB  . VAL D 1 5   ? 24.146  14.387  13.011  1.00 40.73 ? 5   VAL D CB  1 
ATOM   3135 C CG1 . VAL D 1 5   ? 24.608  14.464  14.448  1.00 41.22 ? 5   VAL D CG1 1 
ATOM   3136 C CG2 . VAL D 1 5   ? 25.330  14.516  12.060  1.00 40.31 ? 5   VAL D CG2 1 
ATOM   3137 N N   . ALA D 1 6   ? 24.861  11.251  12.199  1.00 41.50 ? 6   ALA D N   1 
ATOM   3138 C CA  . ALA D 1 6   ? 25.825  10.174  12.453  1.00 40.81 ? 6   ALA D CA  1 
ATOM   3139 C C   . ALA D 1 6   ? 27.153  10.484  11.747  1.00 41.00 ? 6   ALA D C   1 
ATOM   3140 O O   . ALA D 1 6   ? 27.199  10.688  10.527  1.00 40.14 ? 6   ALA D O   1 
ATOM   3141 C CB  . ALA D 1 6   ? 25.282  8.844   11.985  1.00 41.13 ? 6   ALA D CB  1 
ATOM   3142 N N   . VAL D 1 7   ? 28.233  10.535  12.525  1.00 41.30 ? 7   VAL D N   1 
ATOM   3143 C CA  . VAL D 1 7   ? 29.563  10.748  11.985  1.00 41.54 ? 7   VAL D CA  1 
ATOM   3144 C C   . VAL D 1 7   ? 30.171  9.372   11.825  1.00 41.39 ? 7   VAL D C   1 
ATOM   3145 O O   . VAL D 1 7   ? 30.408  8.710   12.812  1.00 42.13 ? 7   VAL D O   1 
ATOM   3146 C CB  . VAL D 1 7   ? 30.410  11.599  12.939  1.00 41.56 ? 7   VAL D CB  1 
ATOM   3147 C CG1 . VAL D 1 7   ? 31.867  11.723  12.439  1.00 41.50 ? 7   VAL D CG1 1 
ATOM   3148 C CG2 . VAL D 1 7   ? 29.789  12.977  13.085  1.00 42.70 ? 7   VAL D CG2 1 
ATOM   3149 N N   . LEU D 1 8   ? 30.414  8.938   10.591  1.00 41.53 ? 8   LEU D N   1 
ATOM   3150 C CA  . LEU D 1 8   ? 30.915  7.573   10.337  1.00 41.87 ? 8   LEU D CA  1 
ATOM   3151 C C   . LEU D 1 8   ? 32.440  7.519   10.368  1.00 42.07 ? 8   LEU D C   1 
ATOM   3152 O O   . LEU D 1 8   ? 33.097  8.320   9.720   1.00 41.78 ? 8   LEU D O   1 
ATOM   3153 C CB  . LEU D 1 8   ? 30.429  7.057   8.976   1.00 41.71 ? 8   LEU D CB  1 
ATOM   3154 C CG  . LEU D 1 8   ? 28.913  7.026   8.745   1.00 42.32 ? 8   LEU D CG  1 
ATOM   3155 C CD1 . LEU D 1 8   ? 28.582  6.808   7.283   1.00 43.82 ? 8   LEU D CD1 1 
ATOM   3156 C CD2 . LEU D 1 8   ? 28.271  5.954   9.571   1.00 40.07 ? 8   LEU D CD2 1 
ATOM   3157 N N   . LYS D 1 9   ? 32.990  6.573   11.125  1.00 42.56 ? 9   LYS D N   1 
ATOM   3158 C CA  . LYS D 1 9   ? 34.431  6.311   11.145  1.00 43.08 ? 9   LYS D CA  1 
ATOM   3159 C C   . LYS D 1 9   ? 34.700  4.820   11.349  1.00 43.12 ? 9   LYS D C   1 
ATOM   3160 O O   . LYS D 1 9   ? 33.853  4.100   11.874  1.00 42.79 ? 9   LYS D O   1 
ATOM   3161 C CB  . LYS D 1 9   ? 35.123  7.109   12.250  1.00 43.26 ? 9   LYS D CB  1 
ATOM   3162 C CG  . LYS D 1 9   ? 35.262  8.597   11.944  1.00 44.35 ? 9   LYS D CG  1 
ATOM   3163 C CD  . LYS D 1 9   ? 36.547  9.179   12.536  1.00 44.63 ? 9   LYS D CD  1 
ATOM   3164 C CE  . LYS D 1 9   ? 36.695  10.666  12.207  1.00 46.05 ? 9   LYS D CE  1 
ATOM   3165 N NZ  . LYS D 1 9   ? 35.668  11.487  12.914  1.00 47.02 ? 9   LYS D NZ  1 
ATOM   3166 N N   . GLY D 1 10  ? 35.882  4.372   10.929  1.00 43.28 ? 10  GLY D N   1 
ATOM   3167 C CA  . GLY D 1 10  ? 36.271  2.966   11.048  1.00 43.55 ? 10  GLY D CA  1 
ATOM   3168 C C   . GLY D 1 10  ? 37.776  2.787   11.070  1.00 43.65 ? 10  GLY D C   1 
ATOM   3169 O O   . GLY D 1 10  ? 38.519  3.752   11.229  1.00 43.88 ? 10  GLY D O   1 
ATOM   3170 N N   . ASP D 1 11  ? 38.227  1.547   10.902  1.00 43.94 ? 11  ASP D N   1 
ATOM   3171 C CA  . ASP D 1 11  ? 39.660  1.237   10.924  1.00 44.23 ? 11  ASP D CA  1 
ATOM   3172 C C   . ASP D 1 11  ? 40.385  1.662   9.642   1.00 44.18 ? 11  ASP D C   1 
ATOM   3173 O O   . ASP D 1 11  ? 41.584  1.927   9.679   1.00 44.73 ? 11  ASP D O   1 
ATOM   3174 C CB  . ASP D 1 11  ? 39.881  -0.265  11.158  1.00 44.51 ? 11  ASP D CB  1 
ATOM   3175 C CG  . ASP D 1 11  ? 39.194  -0.774  12.424  1.00 45.36 ? 11  ASP D CG  1 
ATOM   3176 O OD1 . ASP D 1 11  ? 39.121  -0.019  13.416  1.00 46.66 ? 11  ASP D OD1 1 
ATOM   3177 O OD2 . ASP D 1 11  ? 38.722  -1.931  12.423  1.00 45.41 ? 11  ASP D OD2 1 
ATOM   3178 N N   . GLY D 1 12  ? 39.666  1.703   8.520   1.00 43.86 ? 12  GLY D N   1 
ATOM   3179 C CA  . GLY D 1 12  ? 40.228  2.093   7.225   1.00 43.58 ? 12  GLY D CA  1 
ATOM   3180 C C   . GLY D 1 12  ? 39.956  3.553   6.896   1.00 43.38 ? 12  GLY D C   1 
ATOM   3181 O O   . GLY D 1 12  ? 39.737  4.356   7.797   1.00 43.08 ? 12  GLY D O   1 
ATOM   3182 N N   . PRO D 1 13  ? 39.957  3.905   5.595   1.00 43.32 ? 13  PRO D N   1 
ATOM   3183 C CA  . PRO D 1 13  ? 39.827  5.297   5.165   1.00 43.26 ? 13  PRO D CA  1 
ATOM   3184 C C   . PRO D 1 13  ? 38.390  5.799   4.973   1.00 43.14 ? 13  PRO D C   1 
ATOM   3185 O O   . PRO D 1 13  ? 38.199  6.946   4.567   1.00 43.03 ? 13  PRO D O   1 
ATOM   3186 C CB  . PRO D 1 13  ? 40.552  5.291   3.819   1.00 43.24 ? 13  PRO D CB  1 
ATOM   3187 C CG  . PRO D 1 13  ? 40.238  3.946   3.255   1.00 43.27 ? 13  PRO D CG  1 
ATOM   3188 C CD  . PRO D 1 13  ? 40.094  3.002   4.435   1.00 43.34 ? 13  PRO D CD  1 
ATOM   3189 N N   . VAL D 1 14  ? 37.395  4.959   5.253   1.00 43.16 ? 14  VAL D N   1 
ATOM   3190 C CA  . VAL D 1 14  ? 35.995  5.338   5.042   1.00 43.07 ? 14  VAL D CA  1 
ATOM   3191 C C   . VAL D 1 14  ? 35.494  6.260   6.157   1.00 42.99 ? 14  VAL D C   1 
ATOM   3192 O O   . VAL D 1 14  ? 35.529  5.905   7.334   1.00 43.16 ? 14  VAL D O   1 
ATOM   3193 C CB  . VAL D 1 14  ? 35.070  4.104   4.956   1.00 43.04 ? 14  VAL D CB  1 
ATOM   3194 C CG1 . VAL D 1 14  ? 33.612  4.539   4.721   1.00 43.37 ? 14  VAL D CG1 1 
ATOM   3195 C CG2 . VAL D 1 14  ? 35.533  3.172   3.852   1.00 43.00 ? 14  VAL D CG2 1 
ATOM   3196 N N   . GLN D 1 15  ? 35.036  7.448   5.780   1.00 42.95 ? 15  GLN D N   1 
ATOM   3197 C CA  . GLN D 1 15  ? 34.437  8.364   6.737   1.00 42.88 ? 15  GLN D CA  1 
ATOM   3198 C C   . GLN D 1 15  ? 33.371  9.240   6.093   1.00 42.54 ? 15  GLN D C   1 
ATOM   3199 O O   . GLN D 1 15  ? 33.387  9.477   4.891   1.00 42.53 ? 15  GLN D O   1 
ATOM   3200 C CB  . GLN D 1 15  ? 35.508  9.216   7.428   1.00 43.10 ? 15  GLN D CB  1 
ATOM   3201 C CG  . GLN D 1 15  ? 36.302  10.156  6.535   1.00 43.62 ? 15  GLN D CG  1 
ATOM   3202 C CD  . GLN D 1 15  ? 37.422  10.873  7.305   1.00 44.40 ? 15  GLN D CD  1 
ATOM   3203 O OE1 . GLN D 1 15  ? 38.608  10.609  7.090   1.00 45.08 ? 15  GLN D OE1 1 
ATOM   3204 N NE2 . GLN D 1 15  ? 37.043  11.771  8.216   1.00 47.29 ? 15  GLN D NE2 1 
ATOM   3205 N N   . GLY D 1 16  ? 32.435  9.716   6.904   1.00 42.30 ? 16  GLY D N   1 
ATOM   3206 C CA  . GLY D 1 16  ? 31.378  10.579  6.401   1.00 41.93 ? 16  GLY D CA  1 
ATOM   3207 C C   . GLY D 1 16  ? 30.524  11.214  7.474   1.00 41.41 ? 16  GLY D C   1 
ATOM   3208 O O   . GLY D 1 16  ? 30.819  11.138  8.658   1.00 41.89 ? 16  GLY D O   1 
ATOM   3209 N N   . ILE D 1 17  ? 29.465  11.869  7.035   1.00 41.02 ? 17  ILE D N   1 
ATOM   3210 C CA  . ILE D 1 17  ? 28.521  12.533  7.922   1.00 40.68 ? 17  ILE D CA  1 
ATOM   3211 C C   . ILE D 1 17  ? 27.144  12.368  7.289   1.00 40.27 ? 17  ILE D C   1 
ATOM   3212 O O   . ILE D 1 17  ? 26.928  12.832  6.172   1.00 40.33 ? 17  ILE D O   1 
ATOM   3213 C CB  . ILE D 1 17  ? 28.865  14.026  8.084   1.00 40.67 ? 17  ILE D CB  1 
ATOM   3214 C CG1 . ILE D 1 17  ? 30.216  14.177  8.798   1.00 40.54 ? 17  ILE D CG1 1 
ATOM   3215 C CG2 . ILE D 1 17  ? 27.760  14.746  8.853   1.00 40.98 ? 17  ILE D CG2 1 
ATOM   3216 C CD1 . ILE D 1 17  ? 30.758  15.604  8.822   1.00 40.61 ? 17  ILE D CD1 1 
ATOM   3217 N N   . ILE D 1 18  ? 26.234  11.683  7.985   1.00 39.78 ? 18  ILE D N   1 
ATOM   3218 C CA  . ILE D 1 18  ? 24.890  11.418  7.480   1.00 39.38 ? 18  ILE D CA  1 
ATOM   3219 C C   . ILE D 1 18  ? 23.892  12.131  8.383   1.00 39.22 ? 18  ILE D C   1 
ATOM   3220 O O   . ILE D 1 18  ? 23.916  11.956  9.603   1.00 38.09 ? 18  ILE D O   1 
ATOM   3221 C CB  . ILE D 1 18  ? 24.616  9.897   7.416   1.00 39.97 ? 18  ILE D CB  1 
ATOM   3222 C CG1 . ILE D 1 18  ? 25.647  9.208   6.499   1.00 40.83 ? 18  ILE D CG1 1 
ATOM   3223 C CG2 . ILE D 1 18  ? 23.186  9.614   6.952   1.00 39.79 ? 18  ILE D CG2 1 
ATOM   3224 C CD1 . ILE D 1 18  ? 25.686  9.740   5.028   1.00 40.93 ? 18  ILE D CD1 1 
ATOM   3225 N N   . ASN D 1 19  ? 23.082  13.017  7.783   1.00 39.61 ? 19  ASN D N   1 
ATOM   3226 C CA  . ASN D 1 19  ? 22.050  13.775  8.502   1.00 38.73 ? 19  ASN D CA  1 
ATOM   3227 C C   . ASN D 1 19  ? 20.676  13.115  8.360   1.00 39.24 ? 19  ASN D C   1 
ATOM   3228 O O   . ASN D 1 19  ? 20.356  12.559  7.313   1.00 39.55 ? 19  ASN D O   1 
ATOM   3229 C CB  . ASN D 1 19  ? 21.984  15.193  7.972   1.00 38.42 ? 19  ASN D CB  1 
ATOM   3230 C CG  . ASN D 1 19  ? 23.338  15.856  7.948   1.00 35.17 ? 19  ASN D CG  1 
ATOM   3231 O OD1 . ASN D 1 19  ? 23.967  15.966  6.893   1.00 31.87 ? 19  ASN D OD1 1 
ATOM   3232 N ND2 . ASN D 1 19  ? 23.820  16.239  9.114   1.00 27.47 ? 19  ASN D ND2 1 
ATOM   3233 N N   . PHE D 1 20  ? 19.878  13.181  9.424   1.00 39.30 ? 20  PHE D N   1 
ATOM   3234 C CA  . PHE D 1 20  ? 18.497  12.706  9.422   1.00 39.30 ? 20  PHE D CA  1 
ATOM   3235 C C   . PHE D 1 20  ? 17.562  13.858  9.779   1.00 39.41 ? 20  PHE D C   1 
ATOM   3236 O O   . PHE D 1 20  ? 17.840  14.618  10.703  1.00 38.92 ? 20  PHE D O   1 
ATOM   3237 C CB  . PHE D 1 20  ? 18.313  11.602  10.446  1.00 38.99 ? 20  PHE D CB  1 
ATOM   3238 C CG  . PHE D 1 20  ? 19.182  10.398  10.213  1.00 38.82 ? 20  PHE D CG  1 
ATOM   3239 C CD1 . PHE D 1 20  ? 20.497  10.384  10.660  1.00 39.06 ? 20  PHE D CD1 1 
ATOM   3240 C CD2 . PHE D 1 20  ? 18.683  9.280   9.565   1.00 39.15 ? 20  PHE D CD2 1 
ATOM   3241 C CE1 . PHE D 1 20  ? 21.310  9.297   10.455  1.00 38.39 ? 20  PHE D CE1 1 
ATOM   3242 C CE2 . PHE D 1 20  ? 19.490  8.156   9.362   1.00 38.85 ? 20  PHE D CE2 1 
ATOM   3243 C CZ  . PHE D 1 20  ? 20.804  8.164   9.810   1.00 38.84 ? 20  PHE D CZ  1 
ATOM   3244 N N   . GLU D 1 21  ? 16.454  13.970  9.055   1.00 39.85 ? 21  GLU D N   1 
ATOM   3245 C CA  . GLU D 1 21  ? 15.446  14.979  9.349   1.00 40.32 ? 21  GLU D CA  1 
ATOM   3246 C C   . GLU D 1 21  ? 14.050  14.384  9.196   1.00 40.58 ? 21  GLU D C   1 
ATOM   3247 O O   . GLU D 1 21  ? 13.778  13.679  8.224   1.00 40.44 ? 21  GLU D O   1 
ATOM   3248 C CB  . GLU D 1 21  ? 15.627  16.184  8.441   1.00 40.23 ? 21  GLU D CB  1 
ATOM   3249 C CG  . GLU D 1 21  ? 14.912  17.447  8.938   1.00 40.37 ? 21  GLU D CG  1 
ATOM   3250 C CD  . GLU D 1 21  ? 15.406  18.706  8.248   1.00 41.39 ? 21  GLU D CD  1 
ATOM   3251 O OE1 . GLU D 1 21  ? 16.482  18.653  7.608   1.00 43.25 ? 21  GLU D OE1 1 
ATOM   3252 O OE2 . GLU D 1 21  ? 14.721  19.758  8.337   1.00 41.60 ? 21  GLU D OE2 1 
ATOM   3253 N N   . GLN D 1 22  ? 13.191  14.656  10.179  1.00 40.81 ? 22  GLN D N   1 
ATOM   3254 C CA  . GLN D 1 22  ? 11.820  14.168  10.208  1.00 41.08 ? 22  GLN D CA  1 
ATOM   3255 C C   . GLN D 1 22  ? 10.921  15.299  10.694  1.00 41.52 ? 22  GLN D C   1 
ATOM   3256 O O   . GLN D 1 22  ? 10.786  15.526  11.897  1.00 41.51 ? 22  GLN D O   1 
ATOM   3257 C CB  . GLN D 1 22  ? 11.708  12.949  11.132  1.00 40.95 ? 22  GLN D CB  1 
ATOM   3258 C CG  . GLN D 1 22  ? 10.314  12.336  11.199  1.00 40.85 ? 22  GLN D CG  1 
ATOM   3259 C CD  . GLN D 1 22  ? 10.259  11.042  12.003  1.00 40.84 ? 22  GLN D CD  1 
ATOM   3260 O OE1 . GLN D 1 22  ? 10.826  10.948  13.086  1.00 40.09 ? 22  GLN D OE1 1 
ATOM   3261 N NE2 . GLN D 1 22  ? 9.552   10.051  11.479  1.00 40.46 ? 22  GLN D NE2 1 
ATOM   3262 N N   . LYS D 1 23  ? 10.324  16.023  9.752   1.00 42.23 ? 23  LYS D N   1 
ATOM   3263 C CA  . LYS D 1 23  ? 9.500   17.188  10.087  1.00 42.70 ? 23  LYS D CA  1 
ATOM   3264 C C   . LYS D 1 23  ? 8.178   16.815  10.774  1.00 43.09 ? 23  LYS D C   1 
ATOM   3265 O O   . LYS D 1 23  ? 7.727   17.531  11.668  1.00 43.35 ? 23  LYS D O   1 
ATOM   3266 C CB  . LYS D 1 23  ? 9.253   18.068  8.852   1.00 42.91 ? 23  LYS D CB  1 
ATOM   3267 C CG  . LYS D 1 23  ? 8.654   17.361  7.638   1.00 43.07 ? 23  LYS D CG  1 
ATOM   3268 C CD  . LYS D 1 23  ? 8.499   18.329  6.467   1.00 43.35 ? 23  LYS D CD  1 
ATOM   3269 C CE  . LYS D 1 23  ? 8.365   17.594  5.133   1.00 43.78 ? 23  LYS D CE  1 
ATOM   3270 N NZ  . LYS D 1 23  ? 7.922   18.493  4.025   1.00 43.62 ? 23  LYS D NZ  1 
ATOM   3271 N N   . GLU D 1 24  ? 7.580   15.692  10.370  1.00 43.49 ? 24  GLU D N   1 
ATOM   3272 C CA  . GLU D 1 24  ? 6.301   15.224  10.928  1.00 43.55 ? 24  GLU D CA  1 
ATOM   3273 C C   . GLU D 1 24  ? 6.514   13.971  11.782  1.00 43.52 ? 24  GLU D C   1 
ATOM   3274 O O   . GLU D 1 24  ? 7.317   13.109  11.443  1.00 43.39 ? 24  GLU D O   1 
ATOM   3275 C CB  . GLU D 1 24  ? 5.284   14.952  9.802   1.00 43.76 ? 24  GLU D CB  1 
ATOM   3276 C CG  . GLU D 1 24  ? 4.053   15.879  9.777   1.00 44.11 ? 24  GLU D CG  1 
ATOM   3277 C CD  . GLU D 1 24  ? 4.341   17.312  9.312   1.00 45.33 ? 24  GLU D CD  1 
ATOM   3278 O OE1 . GLU D 1 24  ? 5.094   17.497  8.329   1.00 46.01 ? 24  GLU D OE1 1 
ATOM   3279 O OE2 . GLU D 1 24  ? 3.784   18.255  9.922   1.00 45.06 ? 24  GLU D OE2 1 
ATOM   3280 N N   . SER D 1 25  ? 5.761   13.873  12.873  1.00 43.80 ? 25  SER D N   1 
ATOM   3281 C CA  . SER D 1 25  ? 5.989   12.873  13.929  1.00 43.92 ? 25  SER D CA  1 
ATOM   3282 C C   . SER D 1 25  ? 6.126   11.423  13.446  1.00 44.09 ? 25  SER D C   1 
ATOM   3283 O O   . SER D 1 25  ? 7.043   10.704  13.866  1.00 44.32 ? 25  SER D O   1 
ATOM   3284 C CB  . SER D 1 25  ? 4.863   12.962  14.969  1.00 43.98 ? 25  SER D CB  1 
ATOM   3285 O OG  . SER D 1 25  ? 5.040   12.015  16.009  1.00 44.08 ? 25  SER D OG  1 
ATOM   3286 N N   . ASN D 1 26  ? 5.208   10.993  12.584  1.00 44.33 ? 26  ASN D N   1 
ATOM   3287 C CA  . ASN D 1 26  ? 5.205   9.616   12.074  1.00 44.04 ? 26  ASN D CA  1 
ATOM   3288 C C   . ASN D 1 26  ? 5.498   9.583   10.573  1.00 43.89 ? 26  ASN D C   1 
ATOM   3289 O O   . ASN D 1 26  ? 5.312   8.556   9.911   1.00 43.98 ? 26  ASN D O   1 
ATOM   3290 C CB  . ASN D 1 26  ? 3.853   8.948   12.372  1.00 44.48 ? 26  ASN D CB  1 
ATOM   3291 C CG  . ASN D 1 26  ? 3.996   7.474   12.737  1.00 45.28 ? 26  ASN D CG  1 
ATOM   3292 O OD1 . ASN D 1 26  ? 4.382   6.643   11.902  1.00 47.15 ? 26  ASN D OD1 1 
ATOM   3293 N ND2 . ASN D 1 26  ? 3.689   7.145   13.993  1.00 46.91 ? 26  ASN D ND2 1 
ATOM   3294 N N   . GLY D 1 27  ? 5.966   10.713  10.047  1.00 43.30 ? 27  GLY D N   1 
ATOM   3295 C CA  . GLY D 1 27  ? 6.201   10.868  8.625   1.00 42.74 ? 27  GLY D CA  1 
ATOM   3296 C C   . GLY D 1 27  ? 7.547   10.318  8.207   1.00 42.11 ? 27  GLY D C   1 
ATOM   3297 O O   . GLY D 1 27  ? 8.243   9.701   9.011   1.00 41.63 ? 27  GLY D O   1 
ATOM   3298 N N   . PRO D 1 28  ? 7.919   10.545  6.938   1.00 41.74 ? 28  PRO D N   1 
ATOM   3299 C CA  . PRO D 1 28  ? 9.186   10.057  6.396   1.00 41.64 ? 28  PRO D CA  1 
ATOM   3300 C C   . PRO D 1 28  ? 10.404  10.799  6.954   1.00 41.27 ? 28  PRO D C   1 
ATOM   3301 O O   . PRO D 1 28  ? 10.290  11.939  7.402   1.00 40.97 ? 28  PRO D O   1 
ATOM   3302 C CB  . PRO D 1 28  ? 9.051   10.307  4.885   1.00 41.70 ? 28  PRO D CB  1 
ATOM   3303 C CG  . PRO D 1 28  ? 7.633   10.736  4.655   1.00 41.71 ? 28  PRO D CG  1 
ATOM   3304 C CD  . PRO D 1 28  ? 7.143   11.292  5.933   1.00 41.65 ? 28  PRO D CD  1 
ATOM   3305 N N   . VAL D 1 29  ? 11.553  10.135  6.925   1.00 41.24 ? 29  VAL D N   1 
ATOM   3306 C CA  . VAL D 1 29  ? 12.825  10.721  7.342   1.00 41.20 ? 29  VAL D CA  1 
ATOM   3307 C C   . VAL D 1 29  ? 13.707  10.904  6.108   1.00 41.20 ? 29  VAL D C   1 
ATOM   3308 O O   . VAL D 1 29  ? 13.916  9.955   5.351   1.00 40.95 ? 29  VAL D O   1 
ATOM   3309 C CB  . VAL D 1 29  ? 13.563  9.803   8.334   1.00 40.98 ? 29  VAL D CB  1 
ATOM   3310 C CG1 . VAL D 1 29  ? 14.816  10.481  8.879   1.00 40.58 ? 29  VAL D CG1 1 
ATOM   3311 C CG2 . VAL D 1 29  ? 12.643  9.405   9.472   1.00 41.06 ? 29  VAL D CG2 1 
ATOM   3312 N N   . LYS D 1 30  ? 14.218  12.112  5.899   1.00 41.17 ? 30  LYS D N   1 
ATOM   3313 C CA  . LYS D 1 30  ? 15.172  12.346  4.825   1.00 41.53 ? 30  LYS D CA  1 
ATOM   3314 C C   . LYS D 1 30  ? 16.557  12.036  5.360   1.00 41.62 ? 30  LYS D C   1 
ATOM   3315 O O   . LYS D 1 30  ? 16.924  12.516  6.430   1.00 42.02 ? 30  LYS D O   1 
ATOM   3316 C CB  . LYS D 1 30  ? 15.120  13.794  4.334   1.00 41.68 ? 30  LYS D CB  1 
ATOM   3317 C CG  . LYS D 1 30  ? 13.857  14.162  3.562   1.00 42.29 ? 30  LYS D CG  1 
ATOM   3318 C CD  . LYS D 1 30  ? 13.833  15.658  3.242   1.00 42.29 ? 30  LYS D CD  1 
ATOM   3319 C CE  . LYS D 1 30  ? 12.634  16.044  2.391   1.00 42.66 ? 30  LYS D CE  1 
ATOM   3320 N NZ  . LYS D 1 30  ? 12.586  17.519  2.118   1.00 42.83 ? 30  LYS D NZ  1 
ATOM   3321 N N   . VAL D 1 31  ? 17.311  11.222  4.623   1.00 41.54 ? 31  VAL D N   1 
ATOM   3322 C CA  . VAL D 1 31  ? 18.685  10.875  4.978   1.00 41.38 ? 31  VAL D CA  1 
ATOM   3323 C C   . VAL D 1 31  ? 19.615  11.396  3.886   1.00 41.47 ? 31  VAL D C   1 
ATOM   3324 O O   . VAL D 1 31  ? 19.490  11.001  2.734   1.00 41.64 ? 31  VAL D O   1 
ATOM   3325 C CB  . VAL D 1 31  ? 18.861  9.355   5.112   1.00 41.40 ? 31  VAL D CB  1 
ATOM   3326 C CG1 . VAL D 1 31  ? 20.264  9.008   5.634   1.00 41.08 ? 31  VAL D CG1 1 
ATOM   3327 C CG2 . VAL D 1 31  ? 17.778  8.773   6.023   1.00 41.39 ? 31  VAL D CG2 1 
ATOM   3328 N N   . TRP D 1 32  ? 20.526  12.301  4.239   1.00 41.26 ? 32  TRP D N   1 
ATOM   3329 C CA  . TRP D 1 32  ? 21.486  12.822  3.274   1.00 41.00 ? 32  TRP D CA  1 
ATOM   3330 C C   . TRP D 1 32  ? 22.839  13.102  3.906   1.00 40.39 ? 32  TRP D C   1 
ATOM   3331 O O   . TRP D 1 32  ? 22.959  13.307  5.112   1.00 39.45 ? 32  TRP D O   1 
ATOM   3332 C CB  . TRP D 1 32  ? 20.959  14.094  2.606   1.00 41.27 ? 32  TRP D CB  1 
ATOM   3333 C CG  . TRP D 1 32  ? 21.051  15.313  3.462   1.00 41.58 ? 32  TRP D CG  1 
ATOM   3334 C CD1 . TRP D 1 32  ? 21.934  16.354  3.327   1.00 41.69 ? 32  TRP D CD1 1 
ATOM   3335 C CD2 . TRP D 1 32  ? 20.221  15.637  4.581   1.00 41.54 ? 32  TRP D CD2 1 
ATOM   3336 N NE1 . TRP D 1 32  ? 21.702  17.302  4.296   1.00 41.49 ? 32  TRP D NE1 1 
ATOM   3337 C CE2 . TRP D 1 32  ? 20.657  16.884  5.078   1.00 41.70 ? 32  TRP D CE2 1 
ATOM   3338 C CE3 . TRP D 1 32  ? 19.143  15.002  5.203   1.00 41.52 ? 32  TRP D CE3 1 
ATOM   3339 C CZ2 . TRP D 1 32  ? 20.061  17.497  6.182   1.00 42.08 ? 32  TRP D CZ2 1 
ATOM   3340 C CZ3 . TRP D 1 32  ? 18.546  15.616  6.293   1.00 41.80 ? 32  TRP D CZ3 1 
ATOM   3341 C CH2 . TRP D 1 32  ? 19.009  16.848  6.776   1.00 41.74 ? 32  TRP D CH2 1 
ATOM   3342 N N   . GLY D 1 33  ? 23.855  13.124  3.060   1.00 40.36 ? 33  GLY D N   1 
ATOM   3343 C CA  . GLY D 1 33  ? 25.197  13.411  3.507   1.00 40.63 ? 33  GLY D CA  1 
ATOM   3344 C C   . GLY D 1 33  ? 26.214  13.031  2.467   1.00 40.59 ? 33  GLY D C   1 
ATOM   3345 O O   . GLY D 1 33  ? 25.895  12.910  1.285   1.00 40.69 ? 33  GLY D O   1 
ATOM   3346 N N   . SER D 1 34  ? 27.445  12.838  2.920   1.00 40.85 ? 34  SER D N   1 
ATOM   3347 C CA  . SER D 1 34  ? 28.540  12.444  2.051   1.00 40.70 ? 34  SER D CA  1 
ATOM   3348 C C   . SER D 1 34  ? 29.409  11.429  2.784   1.00 40.69 ? 34  SER D C   1 
ATOM   3349 O O   . SER D 1 34  ? 29.645  11.559  3.987   1.00 40.76 ? 34  SER D O   1 
ATOM   3350 C CB  . SER D 1 34  ? 29.358  13.673  1.655   1.00 40.86 ? 34  SER D CB  1 
ATOM   3351 O OG  . SER D 1 34  ? 30.226  13.384  0.575   1.00 41.62 ? 34  SER D OG  1 
ATOM   3352 N N   . ILE D 1 35  ? 29.850  10.412  2.055   1.00 40.52 ? 35  ILE D N   1 
ATOM   3353 C CA  . ILE D 1 35  ? 30.799  9.429   2.552   1.00 40.27 ? 35  ILE D CA  1 
ATOM   3354 C C   . ILE D 1 35  ? 31.942  9.355   1.546   1.00 39.99 ? 35  ILE D C   1 
ATOM   3355 O O   . ILE D 1 35  ? 31.708  9.371   0.342   1.00 39.68 ? 35  ILE D O   1 
ATOM   3356 C CB  . ILE D 1 35  ? 30.150  8.029   2.701   1.00 40.51 ? 35  ILE D CB  1 
ATOM   3357 C CG1 . ILE D 1 35  ? 28.842  8.115   3.498   1.00 40.38 ? 35  ILE D CG1 1 
ATOM   3358 C CG2 . ILE D 1 35  ? 31.120  7.044   3.369   1.00 40.76 ? 35  ILE D CG2 1 
ATOM   3359 C CD1 . ILE D 1 35  ? 28.154  6.794   3.676   1.00 40.24 ? 35  ILE D CD1 1 
ATOM   3360 N N   . LYS D 1 36  ? 33.173  9.283   2.042   1.00 39.92 ? 36  LYS D N   1 
ATOM   3361 C CA  . LYS D 1 36  ? 34.348  9.184   1.185   1.00 39.77 ? 36  LYS D CA  1 
ATOM   3362 C C   . LYS D 1 36  ? 35.214  7.999   1.574   1.00 39.45 ? 36  LYS D C   1 
ATOM   3363 O O   . LYS D 1 36  ? 34.999  7.382   2.618   1.00 39.09 ? 36  LYS D O   1 
ATOM   3364 C CB  . LYS D 1 36  ? 35.160  10.476  1.239   1.00 40.02 ? 36  LYS D CB  1 
ATOM   3365 C CG  . LYS D 1 36  ? 35.667  10.868  2.624   1.00 40.30 ? 36  LYS D CG  1 
ATOM   3366 C CD  . LYS D 1 36  ? 36.558  12.102  2.532   1.00 40.24 ? 36  LYS D CD  1 
ATOM   3367 C CE  . LYS D 1 36  ? 37.061  12.557  3.892   1.00 40.77 ? 36  LYS D CE  1 
ATOM   3368 N NZ  . LYS D 1 36  ? 37.965  13.744  3.749   1.00 40.79 ? 36  LYS D NZ  1 
ATOM   3369 N N   . GLY D 1 37  ? 36.182  7.685   0.717   1.00 39.29 ? 37  GLY D N   1 
ATOM   3370 C CA  . GLY D 1 37  ? 37.146  6.607   0.970   1.00 39.25 ? 37  GLY D CA  1 
ATOM   3371 C C   . GLY D 1 37  ? 36.642  5.213   0.646   1.00 39.08 ? 37  GLY D C   1 
ATOM   3372 O O   . GLY D 1 37  ? 37.263  4.219   1.028   1.00 38.93 ? 37  GLY D O   1 
ATOM   3373 N N   . LEU D 1 38  ? 35.528  5.150   -0.081  1.00 38.87 ? 38  LEU D N   1 
ATOM   3374 C CA  . LEU D 1 38  ? 34.849  3.896   -0.409  1.00 38.55 ? 38  LEU D CA  1 
ATOM   3375 C C   . LEU D 1 38  ? 35.308  3.367   -1.749  1.00 38.35 ? 38  LEU D C   1 
ATOM   3376 O O   . LEU D 1 38  ? 35.632  4.150   -2.630  1.00 38.60 ? 38  LEU D O   1 
ATOM   3377 C CB  . LEU D 1 38  ? 33.343  4.140   -0.509  1.00 38.52 ? 38  LEU D CB  1 
ATOM   3378 C CG  . LEU D 1 38  ? 32.568  4.464   0.757   1.00 37.65 ? 38  LEU D CG  1 
ATOM   3379 C CD1 . LEU D 1 38  ? 31.192  4.989   0.380   1.00 37.42 ? 38  LEU D CD1 1 
ATOM   3380 C CD2 . LEU D 1 38  ? 32.462  3.227   1.630   1.00 37.40 ? 38  LEU D CD2 1 
ATOM   3381 N N   . THR D 1 39  ? 35.306  2.047   -1.925  1.00 38.08 ? 39  THR D N   1 
ATOM   3382 C CA  . THR D 1 39  ? 35.534  1.473   -3.250  1.00 37.94 ? 39  THR D CA  1 
ATOM   3383 C C   . THR D 1 39  ? 34.349  1.832   -4.142  1.00 37.96 ? 39  THR D C   1 
ATOM   3384 O O   . THR D 1 39  ? 33.230  1.972   -3.649  1.00 38.09 ? 39  THR D O   1 
ATOM   3385 C CB  . THR D 1 39  ? 35.695  -0.065  -3.217  1.00 37.91 ? 39  THR D CB  1 
ATOM   3386 O OG1 . THR D 1 39  ? 34.511  -0.667  -2.688  1.00 37.64 ? 39  THR D OG1 1 
ATOM   3387 C CG2 . THR D 1 39  ? 36.905  -0.479  -2.380  1.00 37.56 ? 39  THR D CG2 1 
ATOM   3388 N N   . GLU D 1 40  ? 34.594  1.995   -5.442  1.00 37.87 ? 40  GLU D N   1 
ATOM   3389 C CA  . GLU D 1 40  ? 33.545  2.386   -6.394  1.00 37.77 ? 40  GLU D CA  1 
ATOM   3390 C C   . GLU D 1 40  ? 32.450  1.328   -6.482  1.00 37.62 ? 40  GLU D C   1 
ATOM   3391 O O   . GLU D 1 40  ? 32.739  0.141   -6.612  1.00 37.96 ? 40  GLU D O   1 
ATOM   3392 C CB  . GLU D 1 40  ? 34.151  2.604   -7.783  1.00 37.99 ? 40  GLU D CB  1 
ATOM   3393 C CG  . GLU D 1 40  ? 33.156  3.007   -8.881  1.00 37.87 ? 40  GLU D CG  1 
ATOM   3394 C CD  . GLU D 1 40  ? 33.775  2.994   -10.264 1.00 38.00 ? 40  GLU D CD  1 
ATOM   3395 O OE1 . GLU D 1 40  ? 35.014  2.866   -10.364 1.00 38.55 ? 40  GLU D OE1 1 
ATOM   3396 O OE2 . GLU D 1 40  ? 33.023  3.108   -11.257 1.00 38.66 ? 40  GLU D OE2 1 
ATOM   3397 N N   . GLY D 1 41  ? 31.196  1.765   -6.426  1.00 37.40 ? 41  GLY D N   1 
ATOM   3398 C CA  . GLY D 1 41  ? 30.053  0.855   -6.505  1.00 37.26 ? 41  GLY D CA  1 
ATOM   3399 C C   . GLY D 1 41  ? 29.131  0.940   -5.305  1.00 37.07 ? 41  GLY D C   1 
ATOM   3400 O O   . GLY D 1 41  ? 29.192  1.892   -4.533  1.00 36.97 ? 41  GLY D O   1 
ATOM   3401 N N   . LEU D 1 42  ? 28.296  -0.086  -5.148  1.00 36.95 ? 42  LEU D N   1 
ATOM   3402 C CA  . LEU D 1 42  ? 27.239  -0.128  -4.130  1.00 36.85 ? 42  LEU D CA  1 
ATOM   3403 C C   . LEU D 1 42  ? 27.706  -0.660  -2.775  1.00 36.66 ? 42  LEU D C   1 
ATOM   3404 O O   . LEU D 1 42  ? 28.422  -1.659  -2.695  1.00 36.38 ? 42  LEU D O   1 
ATOM   3405 C CB  . LEU D 1 42  ? 26.086  -1.013  -4.615  1.00 36.74 ? 42  LEU D CB  1 
ATOM   3406 C CG  . LEU D 1 42  ? 25.273  -0.476  -5.787  1.00 36.85 ? 42  LEU D CG  1 
ATOM   3407 C CD1 . LEU D 1 42  ? 24.504  -1.594  -6.452  1.00 37.72 ? 42  LEU D CD1 1 
ATOM   3408 C CD2 . LEU D 1 42  ? 24.336  0.614   -5.318  1.00 37.05 ? 42  LEU D CD2 1 
ATOM   3409 N N   . HIS D 1 43  ? 27.253  -0.006  -1.711  1.00 36.54 ? 43  HIS D N   1 
ATOM   3410 C CA  . HIS D 1 43  ? 27.583  -0.410  -0.354  1.00 36.74 ? 43  HIS D CA  1 
ATOM   3411 C C   . HIS D 1 43  ? 26.336  -0.416  0.519   1.00 36.74 ? 43  HIS D C   1 
ATOM   3412 O O   . HIS D 1 43  ? 25.654  0.603   0.631   1.00 36.94 ? 43  HIS D O   1 
ATOM   3413 C CB  . HIS D 1 43  ? 28.612  0.556   0.232   1.00 36.93 ? 43  HIS D CB  1 
ATOM   3414 C CG  . HIS D 1 43  ? 29.941  0.494   -0.445  1.00 36.87 ? 43  HIS D CG  1 
ATOM   3415 N ND1 . HIS D 1 43  ? 30.926  -0.387  -0.063  1.00 36.68 ? 43  HIS D ND1 1 
ATOM   3416 C CD2 . HIS D 1 43  ? 30.442  1.193   -1.490  1.00 37.36 ? 43  HIS D CD2 1 
ATOM   3417 C CE1 . HIS D 1 43  ? 31.978  -0.229  -0.845  1.00 37.11 ? 43  HIS D CE1 1 
ATOM   3418 N NE2 . HIS D 1 43  ? 31.711  0.723   -1.721  1.00 36.92 ? 43  HIS D NE2 1 
ATOM   3419 N N   . GLY D 1 44  ? 26.051  -1.556  1.140   1.00 36.52 ? 44  GLY D N   1 
ATOM   3420 C CA  . GLY D 1 44  ? 24.937  -1.676  2.076   1.00 36.63 ? 44  GLY D CA  1 
ATOM   3421 C C   . GLY D 1 44  ? 24.966  -0.608  3.158   1.00 36.76 ? 44  GLY D C   1 
ATOM   3422 O O   . GLY D 1 44  ? 26.025  -0.295  3.704   1.00 36.07 ? 44  GLY D O   1 
ATOM   3423 N N   . PHE D 1 45  ? 23.790  -0.060  3.460   1.00 37.02 ? 45  PHE D N   1 
ATOM   3424 C CA  . PHE D 1 45  ? 23.645  1.101   4.336   1.00 37.49 ? 45  PHE D CA  1 
ATOM   3425 C C   . PHE D 1 45  ? 22.558  0.734   5.340   1.00 37.78 ? 45  PHE D C   1 
ATOM   3426 O O   . PHE D 1 45  ? 21.382  0.626   4.974   1.00 37.89 ? 45  PHE D O   1 
ATOM   3427 C CB  . PHE D 1 45  ? 23.248  2.300   3.480   1.00 37.44 ? 45  PHE D CB  1 
ATOM   3428 C CG  . PHE D 1 45  ? 23.433  3.639   4.131   1.00 37.61 ? 45  PHE D CG  1 
ATOM   3429 C CD1 . PHE D 1 45  ? 24.595  3.967   4.813   1.00 38.14 ? 45  PHE D CD1 1 
ATOM   3430 C CD2 . PHE D 1 45  ? 22.465  4.615   3.974   1.00 38.03 ? 45  PHE D CD2 1 
ATOM   3431 C CE1 . PHE D 1 45  ? 24.756  5.218   5.367   1.00 38.11 ? 45  PHE D CE1 1 
ATOM   3432 C CE2 . PHE D 1 45  ? 22.622  5.862   4.522   1.00 37.41 ? 45  PHE D CE2 1 
ATOM   3433 C CZ  . PHE D 1 45  ? 23.769  6.166   5.213   1.00 38.06 ? 45  PHE D CZ  1 
ATOM   3434 N N   . HIS D 1 46  ? 22.960  0.515   6.596   1.00 38.06 ? 46  HIS D N   1 
ATOM   3435 C CA  . HIS D 1 46  ? 22.095  -0.132  7.590   1.00 37.85 ? 46  HIS D CA  1 
ATOM   3436 C C   . HIS D 1 46  ? 22.156  0.513   8.959   1.00 37.57 ? 46  HIS D C   1 
ATOM   3437 O O   . HIS D 1 46  ? 23.235  0.842   9.442   1.00 37.37 ? 46  HIS D O   1 
ATOM   3438 C CB  . HIS D 1 46  ? 22.512  -1.589  7.785   1.00 38.12 ? 46  HIS D CB  1 
ATOM   3439 C CG  . HIS D 1 46  ? 22.139  -2.492  6.658   1.00 38.53 ? 46  HIS D CG  1 
ATOM   3440 N ND1 . HIS D 1 46  ? 20.845  -2.906  6.435   1.00 40.30 ? 46  HIS D ND1 1 
ATOM   3441 C CD2 . HIS D 1 46  ? 22.900  -3.117  5.728   1.00 40.23 ? 46  HIS D CD2 1 
ATOM   3442 C CE1 . HIS D 1 46  ? 20.820  -3.728  5.399   1.00 39.92 ? 46  HIS D CE1 1 
ATOM   3443 N NE2 . HIS D 1 46  ? 22.054  -3.869  4.948   1.00 39.74 ? 46  HIS D NE2 1 
ATOM   3444 N N   . VAL D 1 47  ? 20.995  0.641   9.598   1.00 37.81 ? 47  VAL D N   1 
ATOM   3445 C CA  . VAL D 1 47  ? 20.928  0.954   11.017  1.00 37.95 ? 47  VAL D CA  1 
ATOM   3446 C C   . VAL D 1 47  ? 21.038  -0.347  11.781  1.00 38.29 ? 47  VAL D C   1 
ATOM   3447 O O   . VAL D 1 47  ? 20.300  -1.336  11.519  1.00 36.77 ? 47  VAL D O   1 
ATOM   3448 C CB  . VAL D 1 47  ? 19.639  1.716   11.413  1.00 38.74 ? 47  VAL D CB  1 
ATOM   3449 C CG1 . VAL D 1 47  ? 19.671  2.118   12.894  1.00 39.26 ? 47  VAL D CG1 1 
ATOM   3450 C CG2 . VAL D 1 47  ? 19.492  2.957   10.568  1.00 37.87 ? 47  VAL D CG2 1 
ATOM   3451 N N   . HIS D 1 48  ? 22.003  -0.368  12.698  1.00 38.24 ? 48  HIS D N   1 
ATOM   3452 C CA  . HIS D 1 48  ? 22.211  -1.536  13.549  1.00 37.78 ? 48  HIS D CA  1 
ATOM   3453 C C   . HIS D 1 48  ? 21.739  -1.178  14.939  1.00 37.87 ? 48  HIS D C   1 
ATOM   3454 O O   . HIS D 1 48  ? 21.694  -0.001  15.314  1.00 38.32 ? 48  HIS D O   1 
ATOM   3455 C CB  . HIS D 1 48  ? 23.674  -1.964  13.525  1.00 37.44 ? 48  HIS D CB  1 
ATOM   3456 C CG  . HIS D 1 48  ? 24.085  -2.595  12.229  1.00 37.88 ? 48  HIS D CG  1 
ATOM   3457 N ND1 . HIS D 1 48  ? 24.392  -3.936  12.113  1.00 37.80 ? 48  HIS D ND1 1 
ATOM   3458 C CD2 . HIS D 1 48  ? 24.199  -2.076  10.984  1.00 37.92 ? 48  HIS D CD2 1 
ATOM   3459 C CE1 . HIS D 1 48  ? 24.708  -4.207  10.860  1.00 37.19 ? 48  HIS D CE1 1 
ATOM   3460 N NE2 . HIS D 1 48  ? 24.596  -3.097  10.154  1.00 37.87 ? 48  HIS D NE2 1 
ATOM   3461 N N   . GLU D 1 49  ? 21.392  -2.192  15.704  1.00 38.09 ? 49  GLU D N   1 
ATOM   3462 C CA  . GLU D 1 49  ? 20.593  -2.010  16.896  1.00 37.98 ? 49  GLU D CA  1 
ATOM   3463 C C   . GLU D 1 49  ? 21.272  -1.235  18.007  1.00 37.98 ? 49  GLU D C   1 
ATOM   3464 O O   . GLU D 1 49  ? 20.667  -0.347  18.606  1.00 39.11 ? 49  GLU D O   1 
ATOM   3465 C CB  . GLU D 1 49  ? 20.201  -3.371  17.410  1.00 37.82 ? 49  GLU D CB  1 
ATOM   3466 C CG  . GLU D 1 49  ? 19.182  -3.343  18.509  1.00 37.91 ? 49  GLU D CG  1 
ATOM   3467 C CD  . GLU D 1 49  ? 18.892  -4.720  18.962  1.00 38.34 ? 49  GLU D CD  1 
ATOM   3468 O OE1 . GLU D 1 49  ? 19.495  -5.615  18.351  1.00 38.53 ? 49  GLU D OE1 1 
ATOM   3469 O OE2 . GLU D 1 49  ? 18.083  -4.906  19.898  1.00 39.74 ? 49  GLU D OE2 1 
ATOM   3470 N N   . PHE D 1 50  ? 22.533  -1.535  18.283  1.00 37.52 ? 50  PHE D N   1 
ATOM   3471 C CA  . PHE D 1 50  ? 23.183  -0.910  19.433  1.00 37.32 ? 50  PHE D CA  1 
ATOM   3472 C C   . PHE D 1 50  ? 24.034  0.298   19.047  1.00 36.60 ? 50  PHE D C   1 
ATOM   3473 O O   . PHE D 1 50  ? 24.718  0.299   18.030  1.00 35.39 ? 50  PHE D O   1 
ATOM   3474 C CB  . PHE D 1 50  ? 23.977  -1.955  20.208  1.00 36.98 ? 50  PHE D CB  1 
ATOM   3475 C CG  . PHE D 1 50  ? 23.144  -3.133  20.598  1.00 36.37 ? 50  PHE D CG  1 
ATOM   3476 C CD1 . PHE D 1 50  ? 22.071  -2.972  21.463  1.00 36.40 ? 50  PHE D CD1 1 
ATOM   3477 C CD2 . PHE D 1 50  ? 23.383  -4.377  20.058  1.00 38.05 ? 50  PHE D CD2 1 
ATOM   3478 C CE1 . PHE D 1 50  ? 21.270  -4.038  21.803  1.00 36.60 ? 50  PHE D CE1 1 
ATOM   3479 C CE2 . PHE D 1 50  ? 22.588  -5.453  20.388  1.00 36.03 ? 50  PHE D CE2 1 
ATOM   3480 C CZ  . PHE D 1 50  ? 21.527  -5.278  21.265  1.00 36.75 ? 50  PHE D CZ  1 
ATOM   3481 N N   . GLY D 1 51  ? 23.972  1.337   19.869  1.00 37.61 ? 51  GLY D N   1 
ATOM   3482 C CA  . GLY D 1 51  ? 24.874  2.480   19.721  1.00 37.45 ? 51  GLY D CA  1 
ATOM   3483 C C   . GLY D 1 51  ? 26.160  2.211   20.479  1.00 38.16 ? 51  GLY D C   1 
ATOM   3484 O O   . GLY D 1 51  ? 26.625  3.043   21.246  1.00 37.52 ? 51  GLY D O   1 
ATOM   3485 N N   . ASP D 1 52  ? 26.715  1.008   20.304  1.00 38.95 ? 52  ASP D N   1 
ATOM   3486 C CA  . ASP D 1 52  ? 27.860  0.570   21.082  1.00 39.43 ? 52  ASP D CA  1 
ATOM   3487 C C   . ASP D 1 52  ? 29.068  0.531   20.148  1.00 40.32 ? 52  ASP D C   1 
ATOM   3488 O O   . ASP D 1 52  ? 29.160  -0.358  19.296  1.00 40.55 ? 52  ASP D O   1 
ATOM   3489 C CB  . ASP D 1 52  ? 27.583  -0.819  21.687  1.00 39.58 ? 52  ASP D CB  1 
ATOM   3490 C CG  . ASP D 1 52  ? 28.654  -1.257  22.666  1.00 39.32 ? 52  ASP D CG  1 
ATOM   3491 O OD1 . ASP D 1 52  ? 29.805  -0.793  22.538  1.00 40.20 ? 52  ASP D OD1 1 
ATOM   3492 O OD2 . ASP D 1 52  ? 28.351  -2.072  23.563  1.00 39.86 ? 52  ASP D OD2 1 
ATOM   3493 N N   . ASN D 1 53  ? 29.986  1.486   20.307  1.00 40.85 ? 53  ASN D N   1 
ATOM   3494 C CA  . ASN D 1 53  ? 31.191  1.551   19.470  1.00 40.92 ? 53  ASN D CA  1 
ATOM   3495 C C   . ASN D 1 53  ? 32.471  1.086   20.180  1.00 41.11 ? 53  ASN D C   1 
ATOM   3496 O O   . ASN D 1 53  ? 33.577  1.329   19.706  1.00 41.27 ? 53  ASN D O   1 
ATOM   3497 C CB  . ASN D 1 53  ? 31.376  2.978   18.936  1.00 41.55 ? 53  ASN D CB  1 
ATOM   3498 C CG  . ASN D 1 53  ? 32.241  3.026   17.687  1.00 42.70 ? 53  ASN D CG  1 
ATOM   3499 O OD1 . ASN D 1 53  ? 33.219  3.774   17.625  1.00 43.77 ? 53  ASN D OD1 1 
ATOM   3500 N ND2 . ASN D 1 53  ? 31.903  2.192   16.693  1.00 46.88 ? 53  ASN D ND2 1 
ATOM   3501 N N   . THR D 1 54  ? 32.319  0.394   21.302  1.00 40.97 ? 54  THR D N   1 
ATOM   3502 C CA  . THR D 1 54  ? 33.453  0.013   22.119  1.00 40.82 ? 54  THR D CA  1 
ATOM   3503 C C   . THR D 1 54  ? 34.402  -0.898  21.342  1.00 40.78 ? 54  THR D C   1 
ATOM   3504 O O   . THR D 1 54  ? 35.616  -0.793  21.482  1.00 40.58 ? 54  THR D O   1 
ATOM   3505 C CB  . THR D 1 54  ? 33.003  -0.693  23.418  1.00 40.85 ? 54  THR D CB  1 
ATOM   3506 O OG1 . THR D 1 54  ? 32.100  -1.760  23.102  1.00 41.09 ? 54  THR D OG1 1 
ATOM   3507 C CG2 . THR D 1 54  ? 32.312  0.287   24.341  1.00 41.35 ? 54  THR D CG2 1 
ATOM   3508 N N   . ALA D 1 55  ? 33.842  -1.789  20.530  1.00 40.54 ? 55  ALA D N   1 
ATOM   3509 C CA  . ALA D 1 55  ? 34.636  -2.639  19.655  1.00 40.43 ? 55  ALA D CA  1 
ATOM   3510 C C   . ALA D 1 55  ? 34.442  -2.236  18.198  1.00 40.32 ? 55  ALA D C   1 
ATOM   3511 O O   . ALA D 1 55  ? 34.370  -3.081  17.322  1.00 40.59 ? 55  ALA D O   1 
ATOM   3512 C CB  . ALA D 1 55  ? 34.253  -4.093  19.862  1.00 40.47 ? 55  ALA D CB  1 
ATOM   3513 N N   . GLY D 1 56  ? 34.353  -0.939  17.935  1.00 40.16 ? 56  GLY D N   1 
ATOM   3514 C CA  . GLY D 1 56  ? 34.113  -0.463  16.587  1.00 39.94 ? 56  GLY D CA  1 
ATOM   3515 C C   . GLY D 1 56  ? 32.715  -0.809  16.111  1.00 39.88 ? 56  GLY D C   1 
ATOM   3516 O O   . GLY D 1 56  ? 31.785  -0.901  16.910  1.00 40.00 ? 56  GLY D O   1 
ATOM   3517 N N   . ALA D 1 57  ? 32.572  -1.000  14.801  1.00 39.87 ? 57  ALA D N   1 
ATOM   3518 C CA  . ALA D 1 57  ? 31.284  -1.318  14.179  1.00 39.85 ? 57  ALA D CA  1 
ATOM   3519 C C   . ALA D 1 57  ? 30.752  -2.680  14.636  1.00 39.80 ? 57  ALA D C   1 
ATOM   3520 O O   . ALA D 1 57  ? 29.548  -2.923  14.599  1.00 39.78 ? 57  ALA D O   1 
ATOM   3521 C CB  . ALA D 1 57  ? 31.416  -1.302  12.660  1.00 39.74 ? 57  ALA D CB  1 
ATOM   3522 N N   . THR D 1 58  ? 31.659  -3.548  15.063  1.00 39.56 ? 58  THR D N   1 
ATOM   3523 C CA  . THR D 1 58  ? 31.322  -4.915  15.486  1.00 39.72 ? 58  THR D CA  1 
ATOM   3524 C C   . THR D 1 58  ? 30.335  -4.976  16.656  1.00 39.71 ? 58  THR D C   1 
ATOM   3525 O O   . THR D 1 58  ? 29.513  -5.906  16.741  1.00 39.85 ? 58  THR D O   1 
ATOM   3526 C CB  . THR D 1 58  ? 32.602  -5.670  15.899  1.00 39.85 ? 58  THR D CB  1 
ATOM   3527 O OG1 . THR D 1 58  ? 33.644  -5.371  14.962  1.00 41.49 ? 58  THR D OG1 1 
ATOM   3528 C CG2 . THR D 1 58  ? 32.368  -7.181  15.939  1.00 39.37 ? 58  THR D CG2 1 
ATOM   3529 N N   . SER D 1 59  ? 30.433  -3.998  17.555  1.00 39.22 ? 59  SER D N   1 
ATOM   3530 C CA  . SER D 1 59  ? 29.633  -3.975  18.772  1.00 39.24 ? 59  SER D CA  1 
ATOM   3531 C C   . SER D 1 59  ? 28.246  -3.328  18.577  1.00 39.10 ? 59  SER D C   1 
ATOM   3532 O O   . SER D 1 59  ? 27.409  -3.362  19.481  1.00 39.07 ? 59  SER D O   1 
ATOM   3533 C CB  . SER D 1 59  ? 30.411  -3.266  19.874  1.00 39.13 ? 59  SER D CB  1 
ATOM   3534 O OG  . SER D 1 59  ? 30.882  -2.030  19.391  1.00 39.40 ? 59  SER D OG  1 
ATOM   3535 N N   . ALA D 1 60  ? 27.997  -2.776  17.391  1.00 39.00 ? 60  ALA D N   1 
ATOM   3536 C CA  . ALA D 1 60  ? 26.663  -2.311  17.001  1.00 38.77 ? 60  ALA D CA  1 
ATOM   3537 C C   . ALA D 1 60  ? 25.626  -3.440  16.903  1.00 38.69 ? 60  ALA D C   1 
ATOM   3538 O O   . ALA D 1 60  ? 24.419  -3.195  16.869  1.00 38.94 ? 60  ALA D O   1 
ATOM   3539 C CB  . ALA D 1 60  ? 26.749  -1.582  15.672  1.00 39.24 ? 60  ALA D CB  1 
ATOM   3540 N N   . GLY D 1 61  ? 26.072  -4.682  16.853  1.00 38.46 ? 61  GLY D N   1 
ATOM   3541 C CA  . GLY D 1 61  ? 25.123  -5.777  16.801  1.00 38.37 ? 61  GLY D CA  1 
ATOM   3542 C C   . GLY D 1 61  ? 24.462  -5.882  15.443  1.00 38.22 ? 61  GLY D C   1 
ATOM   3543 O O   . GLY D 1 61  ? 25.005  -5.407  14.451  1.00 37.78 ? 61  GLY D O   1 
ATOM   3544 N N   . PRO D 1 62  ? 23.296  -6.538  15.383  1.00 38.97 ? 62  PRO D N   1 
ATOM   3545 C CA  . PRO D 1 62  ? 22.682  -6.823  14.110  1.00 39.09 ? 62  PRO D CA  1 
ATOM   3546 C C   . PRO D 1 62  ? 21.895  -5.662  13.529  1.00 39.34 ? 62  PRO D C   1 
ATOM   3547 O O   . PRO D 1 62  ? 21.868  -4.540  14.087  1.00 39.78 ? 62  PRO D O   1 
ATOM   3548 C CB  . PRO D 1 62  ? 21.753  -7.999  14.450  1.00 39.15 ? 62  PRO D CB  1 
ATOM   3549 C CG  . PRO D 1 62  ? 21.314  -7.705  15.828  1.00 38.41 ? 62  PRO D CG  1 
ATOM   3550 C CD  . PRO D 1 62  ? 22.517  -7.119  16.498  1.00 39.16 ? 62  PRO D CD  1 
ATOM   3551 N N   . HIS D 1 63  ? 21.290  -5.934  12.381  1.00 39.60 ? 63  HIS D N   1 
ATOM   3552 C CA  . HIS D 1 63  ? 20.357  -5.019  11.752  1.00 40.08 ? 63  HIS D CA  1 
ATOM   3553 C C   . HIS D 1 63  ? 19.243  -4.697  12.747  1.00 40.05 ? 63  HIS D C   1 
ATOM   3554 O O   . HIS D 1 63  ? 18.708  -5.596  13.405  1.00 38.92 ? 63  HIS D O   1 
ATOM   3555 C CB  . HIS D 1 63  ? 19.762  -5.659  10.488  1.00 40.23 ? 63  HIS D CB  1 
ATOM   3556 C CG  . HIS D 1 63  ? 20.743  -5.815  9.366   1.00 40.75 ? 63  HIS D CG  1 
ATOM   3557 N ND1 . HIS D 1 63  ? 20.590  -6.750  8.367   1.00 40.71 ? 63  HIS D ND1 1 
ATOM   3558 C CD2 . HIS D 1 63  ? 21.888  -5.148  9.082   1.00 42.38 ? 63  HIS D CD2 1 
ATOM   3559 C CE1 . HIS D 1 63  ? 21.600  -6.658  7.519   1.00 41.16 ? 63  HIS D CE1 1 
ATOM   3560 N NE2 . HIS D 1 63  ? 22.408  -5.701  7.936   1.00 40.91 ? 63  HIS D NE2 1 
ATOM   3561 N N   . PHE D 1 64  ? 18.914  -3.417  12.879  1.00 39.94 ? 64  PHE D N   1 
ATOM   3562 C CA  . PHE D 1 64  ? 17.830  -3.008  13.758  1.00 40.50 ? 64  PHE D CA  1 
ATOM   3563 C C   . PHE D 1 64  ? 16.523  -3.555  13.207  1.00 40.83 ? 64  PHE D C   1 
ATOM   3564 O O   . PHE D 1 64  ? 16.134  -3.255  12.077  1.00 41.21 ? 64  PHE D O   1 
ATOM   3565 C CB  . PHE D 1 64  ? 17.781  -1.484  13.876  1.00 40.23 ? 64  PHE D CB  1 
ATOM   3566 C CG  . PHE D 1 64  ? 16.702  -0.968  14.794  1.00 40.20 ? 64  PHE D CG  1 
ATOM   3567 C CD1 . PHE D 1 64  ? 16.449  -1.573  16.021  1.00 40.83 ? 64  PHE D CD1 1 
ATOM   3568 C CD2 . PHE D 1 64  ? 15.957  0.158   14.444  1.00 40.53 ? 64  PHE D CD2 1 
ATOM   3569 C CE1 . PHE D 1 64  ? 15.466  -1.072  16.874  1.00 40.77 ? 64  PHE D CE1 1 
ATOM   3570 C CE2 . PHE D 1 64  ? 14.972  0.658   15.294  1.00 39.90 ? 64  PHE D CE2 1 
ATOM   3571 C CZ  . PHE D 1 64  ? 14.728  0.045   16.504  1.00 39.99 ? 64  PHE D CZ  1 
ATOM   3572 N N   . ASN D 1 65  ? 15.871  -4.387  14.004  1.00 41.70 ? 65  ASN D N   1 
ATOM   3573 C CA  . ASN D 1 65  ? 14.663  -5.082  13.578  1.00 41.91 ? 65  ASN D CA  1 
ATOM   3574 C C   . ASN D 1 65  ? 13.763  -5.374  14.773  1.00 42.16 ? 65  ASN D C   1 
ATOM   3575 O O   . ASN D 1 65  ? 13.566  -6.547  15.125  1.00 42.06 ? 65  ASN D O   1 
ATOM   3576 C CB  . ASN D 1 65  ? 15.024  -6.389  12.856  1.00 42.12 ? 65  ASN D CB  1 
ATOM   3577 C CG  . ASN D 1 65  ? 13.893  -6.915  12.008  1.00 42.47 ? 65  ASN D CG  1 
ATOM   3578 O OD1 . ASN D 1 65  ? 13.779  -8.122  11.779  1.00 44.42 ? 65  ASN D OD1 1 
ATOM   3579 N ND2 . ASN D 1 65  ? 13.039  -6.010  11.531  1.00 43.92 ? 65  ASN D ND2 1 
ATOM   3580 N N   . PRO D 1 66  ? 13.191  -4.308  15.381  1.00 42.16 ? 66  PRO D N   1 
ATOM   3581 C CA  . PRO D 1 66  ? 12.454  -4.390  16.645  1.00 42.30 ? 66  PRO D CA  1 
ATOM   3582 C C   . PRO D 1 66  ? 11.143  -5.154  16.514  1.00 42.65 ? 66  PRO D C   1 
ATOM   3583 O O   . PRO D 1 66  ? 10.875  -6.061  17.307  1.00 43.48 ? 66  PRO D O   1 
ATOM   3584 C CB  . PRO D 1 66  ? 12.175  -2.921  16.979  1.00 42.35 ? 66  PRO D CB  1 
ATOM   3585 C CG  . PRO D 1 66  ? 12.135  -2.246  15.661  1.00 42.07 ? 66  PRO D CG  1 
ATOM   3586 C CD  . PRO D 1 66  ? 13.175  -2.934  14.838  1.00 42.02 ? 66  PRO D CD  1 
ATOM   3587 N N   . ARG D 1 79  ? 13.429  -6.238  4.618   1.00 48.92 ? 79  ARG D N   1 
ATOM   3588 C CA  . ARG D 1 79  ? 12.319  -5.459  5.164   1.00 48.60 ? 79  ARG D CA  1 
ATOM   3589 C C   . ARG D 1 79  ? 12.557  -4.943  6.585   1.00 48.30 ? 79  ARG D C   1 
ATOM   3590 O O   . ARG D 1 79  ? 11.647  -4.353  7.168   1.00 48.26 ? 79  ARG D O   1 
ATOM   3591 C CB  . ARG D 1 79  ? 11.022  -6.282  5.121   1.00 48.70 ? 79  ARG D CB  1 
ATOM   3592 C CG  . ARG D 1 79  ? 10.146  -5.967  3.926   1.00 49.19 ? 79  ARG D CG  1 
ATOM   3593 C CD  . ARG D 1 79  ? 8.825   -6.696  3.982   1.00 49.04 ? 79  ARG D CD  1 
ATOM   3594 N NE  . ARG D 1 79  ? 8.126   -6.607  2.702   1.00 49.23 ? 79  ARG D NE  1 
ATOM   3595 C CZ  . ARG D 1 79  ? 7.103   -7.378  2.331   1.00 49.69 ? 79  ARG D CZ  1 
ATOM   3596 N NH1 . ARG D 1 79  ? 6.619   -8.321  3.142   1.00 50.04 ? 79  ARG D NH1 1 
ATOM   3597 N NH2 . ARG D 1 79  ? 6.553   -7.206  1.132   1.00 49.81 ? 79  ARG D NH2 1 
ATOM   3598 N N   . HIS D 1 80  ? 13.756  -5.143  7.141   1.00 47.89 ? 80  HIS D N   1 
ATOM   3599 C CA  . HIS D 1 80  ? 14.046  -4.667  8.503   1.00 47.77 ? 80  HIS D CA  1 
ATOM   3600 C C   . HIS D 1 80  ? 13.891  -3.149  8.575   1.00 47.35 ? 80  HIS D C   1 
ATOM   3601 O O   . HIS D 1 80  ? 13.993  -2.460  7.557   1.00 47.34 ? 80  HIS D O   1 
ATOM   3602 C CB  . HIS D 1 80  ? 15.474  -5.004  8.969   1.00 48.48 ? 80  HIS D CB  1 
ATOM   3603 C CG  . HIS D 1 80  ? 15.897  -6.416  8.714   1.00 48.89 ? 80  HIS D CG  1 
ATOM   3604 N ND1 . HIS D 1 80  ? 15.010  -7.473  8.682   1.00 50.17 ? 80  HIS D ND1 1 
ATOM   3605 C CD2 . HIS D 1 80  ? 17.125  -6.946  8.497   1.00 49.35 ? 80  HIS D CD2 1 
ATOM   3606 C CE1 . HIS D 1 80  ? 15.672  -8.592  8.440   1.00 50.02 ? 80  HIS D CE1 1 
ATOM   3607 N NE2 . HIS D 1 80  ? 16.958  -8.300  8.327   1.00 50.44 ? 80  HIS D NE2 1 
ATOM   3608 N N   . VAL D 1 81  ? 13.689  -2.634  9.785   1.00 46.73 ? 81  VAL D N   1 
ATOM   3609 C CA  . VAL D 1 81  ? 13.510  -1.198  9.984   1.00 46.44 ? 81  VAL D CA  1 
ATOM   3610 C C   . VAL D 1 81  ? 14.779  -0.453  9.561   1.00 46.34 ? 81  VAL D C   1 
ATOM   3611 O O   . VAL D 1 81  ? 14.706  0.570   8.870   1.00 46.89 ? 81  VAL D O   1 
ATOM   3612 C CB  . VAL D 1 81  ? 13.125  -0.856  11.454  1.00 46.30 ? 81  VAL D CB  1 
ATOM   3613 C CG1 . VAL D 1 81  ? 13.029  0.660   11.671  1.00 45.81 ? 81  VAL D CG1 1 
ATOM   3614 C CG2 . VAL D 1 81  ? 11.802  -1.529  11.838  1.00 46.37 ? 81  VAL D CG2 1 
ATOM   3615 N N   . GLY D 1 82  ? 15.940  -0.983  9.935   1.00 45.77 ? 82  GLY D N   1 
ATOM   3616 C CA  . GLY D 1 82  ? 17.214  -0.332  9.607   1.00 45.34 ? 82  GLY D CA  1 
ATOM   3617 C C   . GLY D 1 82  ? 17.710  -0.428  8.163   1.00 44.74 ? 82  GLY D C   1 
ATOM   3618 O O   . GLY D 1 82  ? 18.760  0.119   7.832   1.00 44.03 ? 82  GLY D O   1 
ATOM   3619 N N   . ASP D 1 83  ? 16.964  -1.117  7.306   1.00 44.09 ? 83  ASP D N   1 
ATOM   3620 C CA  . ASP D 1 83  ? 17.432  -1.458  5.969   1.00 43.81 ? 83  ASP D CA  1 
ATOM   3621 C C   . ASP D 1 83  ? 17.216  -0.280  5.017   1.00 43.25 ? 83  ASP D C   1 
ATOM   3622 O O   . ASP D 1 83  ? 16.151  -0.157  4.411   1.00 43.33 ? 83  ASP D O   1 
ATOM   3623 C CB  . ASP D 1 83  ? 16.697  -2.721  5.486   1.00 43.64 ? 83  ASP D CB  1 
ATOM   3624 C CG  . ASP D 1 83  ? 17.399  -3.414  4.333   1.00 44.10 ? 83  ASP D CG  1 
ATOM   3625 O OD1 . ASP D 1 83  ? 18.052  -2.727  3.521   1.00 45.15 ? 83  ASP D OD1 1 
ATOM   3626 O OD2 . ASP D 1 83  ? 17.286  -4.662  4.233   1.00 44.96 ? 83  ASP D OD2 1 
ATOM   3627 N N   . LEU D 1 84  ? 18.230  0.586   4.905   1.00 42.46 ? 84  LEU D N   1 
ATOM   3628 C CA  . LEU D 1 84  ? 18.165  1.782   4.057   1.00 41.96 ? 84  LEU D CA  1 
ATOM   3629 C C   . LEU D 1 84  ? 18.714  1.570   2.634   1.00 41.50 ? 84  LEU D C   1 
ATOM   3630 O O   . LEU D 1 84  ? 18.975  2.534   1.916   1.00 41.24 ? 84  LEU D O   1 
ATOM   3631 C CB  . LEU D 1 84  ? 18.911  2.938   4.730   1.00 42.05 ? 84  LEU D CB  1 
ATOM   3632 C CG  . LEU D 1 84  ? 18.457  3.285   6.150   1.00 41.87 ? 84  LEU D CG  1 
ATOM   3633 C CD1 . LEU D 1 84  ? 19.298  4.397   6.718   1.00 41.21 ? 84  LEU D CD1 1 
ATOM   3634 C CD2 . LEU D 1 84  ? 16.997  3.668   6.157   1.00 43.15 ? 84  LEU D CD2 1 
ATOM   3635 N N   . GLY D 1 85  ? 18.877  0.312   2.229   1.00 40.87 ? 85  GLY D N   1 
ATOM   3636 C CA  . GLY D 1 85  ? 19.342  -0.020  0.892   1.00 40.55 ? 85  GLY D CA  1 
ATOM   3637 C C   . GLY D 1 85  ? 20.844  0.116   0.762   1.00 40.17 ? 85  GLY D C   1 
ATOM   3638 O O   . GLY D 1 85  ? 21.588  -0.358  1.616   1.00 40.13 ? 85  GLY D O   1 
ATOM   3639 N N   . ASN D 1 86  ? 21.288  0.758   -0.317  1.00 39.80 ? 86  ASN D N   1 
ATOM   3640 C CA  . ASN D 1 86  ? 22.705  0.992   -0.554  1.00 39.49 ? 86  ASN D CA  1 
ATOM   3641 C C   . ASN D 1 86  ? 22.998  2.461   -0.678  1.00 39.28 ? 86  ASN D C   1 
ATOM   3642 O O   . ASN D 1 86  ? 22.094  3.269   -0.863  1.00 39.37 ? 86  ASN D O   1 
ATOM   3643 C CB  . ASN D 1 86  ? 23.164  0.317   -1.844  1.00 39.07 ? 86  ASN D CB  1 
ATOM   3644 C CG  . ASN D 1 86  ? 22.988  -1.174  -1.817  1.00 38.56 ? 86  ASN D CG  1 
ATOM   3645 O OD1 . ASN D 1 86  ? 23.758  -1.881  -1.174  1.00 36.73 ? 86  ASN D OD1 1 
ATOM   3646 N ND2 . ASN D 1 86  ? 21.983  -1.670  -2.533  1.00 37.05 ? 86  ASN D ND2 1 
ATOM   3647 N N   . VAL D 1 87  ? 24.280  2.788   -0.551  1.00 39.48 ? 87  VAL D N   1 
ATOM   3648 C CA  . VAL D 1 87  ? 24.838  4.056   -1.024  1.00 39.47 ? 87  VAL D CA  1 
ATOM   3649 C C   . VAL D 1 87  ? 25.781  3.691   -2.173  1.00 39.44 ? 87  VAL D C   1 
ATOM   3650 O O   . VAL D 1 87  ? 26.292  2.567   -2.231  1.00 39.18 ? 87  VAL D O   1 
ATOM   3651 C CB  . VAL D 1 87  ? 25.574  4.844   0.090   1.00 39.44 ? 87  VAL D CB  1 
ATOM   3652 C CG1 . VAL D 1 87  ? 24.594  5.243   1.190   1.00 39.66 ? 87  VAL D CG1 1 
ATOM   3653 C CG2 . VAL D 1 87  ? 26.738  4.046   0.674   1.00 39.72 ? 87  VAL D CG2 1 
ATOM   3654 N N   . THR D 1 88  ? 25.986  4.627   -3.094  1.00 39.45 ? 88  THR D N   1 
ATOM   3655 C CA  . THR D 1 88  ? 26.802  4.373   -4.271  1.00 39.47 ? 88  THR D CA  1 
ATOM   3656 C C   . THR D 1 88  ? 27.988  5.326   -4.305  1.00 39.56 ? 88  THR D C   1 
ATOM   3657 O O   . THR D 1 88  ? 27.818  6.546   -4.345  1.00 39.40 ? 88  THR D O   1 
ATOM   3658 C CB  . THR D 1 88  ? 25.990  4.525   -5.579  1.00 39.52 ? 88  THR D CB  1 
ATOM   3659 O OG1 . THR D 1 88  ? 24.816  3.705   -5.518  1.00 38.76 ? 88  THR D OG1 1 
ATOM   3660 C CG2 . THR D 1 88  ? 26.831  4.120   -6.805  1.00 39.52 ? 88  THR D CG2 1 
ATOM   3661 N N   . ALA D 1 89  ? 29.184  4.743   -4.285  1.00 39.61 ? 89  ALA D N   1 
ATOM   3662 C CA  . ALA D 1 89  ? 30.424  5.480   -4.463  1.00 39.65 ? 89  ALA D CA  1 
ATOM   3663 C C   . ALA D 1 89  ? 30.733  5.617   -5.950  1.00 39.69 ? 89  ALA D C   1 
ATOM   3664 O O   . ALA D 1 89  ? 30.557  4.678   -6.727  1.00 39.46 ? 89  ALA D O   1 
ATOM   3665 C CB  . ALA D 1 89  ? 31.564  4.763   -3.755  1.00 39.61 ? 89  ALA D CB  1 
ATOM   3666 N N   . ASP D 1 90  ? 31.206  6.798   -6.329  1.00 40.03 ? 90  ASP D N   1 
ATOM   3667 C CA  . ASP D 1 90  ? 31.641  7.075   -7.693  1.00 40.25 ? 90  ASP D CA  1 
ATOM   3668 C C   . ASP D 1 90  ? 33.107  6.651   -7.873  1.00 40.31 ? 90  ASP D C   1 
ATOM   3669 O O   . ASP D 1 90  ? 33.688  6.012   -6.991  1.00 40.32 ? 90  ASP D O   1 
ATOM   3670 C CB  . ASP D 1 90  ? 31.443  8.567   -8.002  1.00 40.19 ? 90  ASP D CB  1 
ATOM   3671 C CG  . ASP D 1 90  ? 32.345  9.473   -7.173  1.00 40.67 ? 90  ASP D CG  1 
ATOM   3672 O OD1 . ASP D 1 90  ? 33.360  8.996   -6.625  1.00 41.40 ? 90  ASP D OD1 1 
ATOM   3673 O OD2 . ASP D 1 90  ? 32.039  10.674  -7.063  1.00 40.94 ? 90  ASP D OD2 1 
ATOM   3674 N N   . LYS D 1 91  ? 33.696  7.015   -9.013  1.00 40.54 ? 91  LYS D N   1 
ATOM   3675 C CA  . LYS D 1 91  ? 35.099  6.696   -9.341  1.00 40.65 ? 91  LYS D CA  1 
ATOM   3676 C C   . LYS D 1 91  ? 36.122  7.196   -8.315  1.00 40.68 ? 91  LYS D C   1 
ATOM   3677 O O   . LYS D 1 91  ? 37.202  6.619   -8.181  1.00 40.66 ? 91  LYS D O   1 
ATOM   3678 C CB  . LYS D 1 91  ? 35.463  7.285   -10.712 1.00 40.64 ? 91  LYS D CB  1 
ATOM   3679 C CG  . LYS D 1 91  ? 35.503  8.819   -10.744 1.00 40.73 ? 91  LYS D CG  1 
ATOM   3680 C CD  . LYS D 1 91  ? 35.750  9.360   -12.144 1.00 40.97 ? 91  LYS D CD  1 
ATOM   3681 C CE  . LYS D 1 91  ? 35.908  10.873  -12.129 1.00 40.77 ? 91  LYS D CE  1 
ATOM   3682 N NZ  . LYS D 1 91  ? 35.698  11.449  -13.477 1.00 40.93 ? 91  LYS D NZ  1 
ATOM   3683 N N   . ASP D 1 92  ? 35.780  8.285   -7.627  1.00 40.69 ? 92  ASP D N   1 
ATOM   3684 C CA  . ASP D 1 92  ? 36.649  8.917   -6.634  1.00 40.69 ? 92  ASP D CA  1 
ATOM   3685 C C   . ASP D 1 92  ? 36.440  8.318   -5.242  1.00 40.46 ? 92  ASP D C   1 
ATOM   3686 O O   . ASP D 1 92  ? 37.073  8.749   -4.280  1.00 40.36 ? 92  ASP D O   1 
ATOM   3687 C CB  . ASP D 1 92  ? 36.368  10.423  -6.573  1.00 40.65 ? 92  ASP D CB  1 
ATOM   3688 C CG  . ASP D 1 92  ? 36.403  11.086  -7.937  1.00 41.34 ? 92  ASP D CG  1 
ATOM   3689 O OD1 . ASP D 1 92  ? 37.420  10.944  -8.651  1.00 41.42 ? 92  ASP D OD1 1 
ATOM   3690 O OD2 . ASP D 1 92  ? 35.408  11.756  -8.293  1.00 41.64 ? 92  ASP D OD2 1 
ATOM   3691 N N   . GLY D 1 93  ? 35.542  7.340   -5.136  1.00 40.40 ? 93  GLY D N   1 
ATOM   3692 C CA  . GLY D 1 93  ? 35.223  6.705   -3.864  1.00 40.28 ? 93  GLY D CA  1 
ATOM   3693 C C   . GLY D 1 93  ? 34.304  7.522   -2.982  1.00 40.20 ? 93  GLY D C   1 
ATOM   3694 O O   . GLY D 1 93  ? 34.213  7.272   -1.781  1.00 40.42 ? 93  GLY D O   1 
ATOM   3695 N N   . VAL D 1 94  ? 33.613  8.492   -3.578  1.00 40.19 ? 94  VAL D N   1 
ATOM   3696 C CA  . VAL D 1 94  ? 32.719  9.386   -2.849  1.00 40.18 ? 94  VAL D CA  1 
ATOM   3697 C C   . VAL D 1 94  ? 31.250  9.071   -3.145  1.00 40.22 ? 94  VAL D C   1 
ATOM   3698 O O   . VAL D 1 94  ? 30.838  8.973   -4.305  1.00 39.91 ? 94  VAL D O   1 
ATOM   3699 C CB  . VAL D 1 94  ? 32.995  10.854  -3.201  1.00 40.07 ? 94  VAL D CB  1 
ATOM   3700 C CG1 . VAL D 1 94  ? 31.947  11.777  -2.564  1.00 40.36 ? 94  VAL D CG1 1 
ATOM   3701 C CG2 . VAL D 1 94  ? 34.394  11.242  -2.756  1.00 40.39 ? 94  VAL D CG2 1 
ATOM   3702 N N   . ALA D 1 95  ? 30.469  8.930   -2.079  1.00 40.34 ? 95  ALA D N   1 
ATOM   3703 C CA  . ALA D 1 95  ? 29.035  8.705   -2.182  1.00 40.45 ? 95  ALA D CA  1 
ATOM   3704 C C   . ALA D 1 95  ? 28.286  9.905   -1.622  1.00 40.57 ? 95  ALA D C   1 
ATOM   3705 O O   . ALA D 1 95  ? 28.318  10.149  -0.415  1.00 40.79 ? 95  ALA D O   1 
ATOM   3706 C CB  . ALA D 1 95  ? 28.646  7.445   -1.423  1.00 40.29 ? 95  ALA D CB  1 
ATOM   3707 N N   . ASP D 1 96  ? 27.636  10.661  -2.502  1.00 40.66 ? 96  ASP D N   1 
ATOM   3708 C CA  . ASP D 1 96  ? 26.682  11.675  -2.083  1.00 40.93 ? 96  ASP D CA  1 
ATOM   3709 C C   . ASP D 1 96  ? 25.372  10.958  -1.803  1.00 40.82 ? 96  ASP D C   1 
ATOM   3710 O O   . ASP D 1 96  ? 24.779  10.364  -2.708  1.00 41.06 ? 96  ASP D O   1 
ATOM   3711 C CB  . ASP D 1 96  ? 26.499  12.740  -3.165  1.00 41.28 ? 96  ASP D CB  1 
ATOM   3712 C CG  . ASP D 1 96  ? 27.787  13.517  -3.450  1.00 42.46 ? 96  ASP D CG  1 
ATOM   3713 O OD1 . ASP D 1 96  ? 28.716  13.487  -2.598  1.00 43.94 ? 96  ASP D OD1 1 
ATOM   3714 O OD2 . ASP D 1 96  ? 27.865  14.166  -4.526  1.00 42.41 ? 96  ASP D OD2 1 
ATOM   3715 N N   . VAL D 1 97  ? 24.940  10.994  -0.543  1.00 40.35 ? 97  VAL D N   1 
ATOM   3716 C CA  . VAL D 1 97  ? 23.773  10.245  -0.088  1.00 39.90 ? 97  VAL D CA  1 
ATOM   3717 C C   . VAL D 1 97  ? 22.518  11.123  -0.092  1.00 39.77 ? 97  VAL D C   1 
ATOM   3718 O O   . VAL D 1 97  ? 22.532  12.256  0.404   1.00 39.35 ? 97  VAL D O   1 
ATOM   3719 C CB  . VAL D 1 97  ? 24.010  9.674   1.330   1.00 39.64 ? 97  VAL D CB  1 
ATOM   3720 C CG1 . VAL D 1 97  ? 22.782  8.939   1.834   1.00 39.45 ? 97  VAL D CG1 1 
ATOM   3721 C CG2 . VAL D 1 97  ? 25.237  8.757   1.343   1.00 39.13 ? 97  VAL D CG2 1 
ATOM   3722 N N   . SER D 1 98  ? 21.445  10.599  -0.682  1.00 39.80 ? 98  SER D N   1 
ATOM   3723 C CA  . SER D 1 98  ? 20.121  11.202  -0.579  1.00 40.02 ? 98  SER D CA  1 
ATOM   3724 C C   . SER D 1 98  ? 19.075  10.098  -0.616  1.00 40.13 ? 98  SER D C   1 
ATOM   3725 O O   . SER D 1 98  ? 18.871  9.468   -1.637  1.00 40.00 ? 98  SER D O   1 
ATOM   3726 C CB  . SER D 1 98  ? 19.881  12.194  -1.705  1.00 40.06 ? 98  SER D CB  1 
ATOM   3727 O OG  . SER D 1 98  ? 18.558  12.690  -1.658  1.00 40.08 ? 98  SER D OG  1 
ATOM   3728 N N   . ILE D 1 99  ? 18.444  9.857   0.526   1.00 40.57 ? 99  ILE D N   1 
ATOM   3729 C CA  . ILE D 1 99  ? 17.473  8.787   0.700   1.00 40.80 ? 99  ILE D CA  1 
ATOM   3730 C C   . ILE D 1 99  ? 16.278  9.378   1.434   1.00 41.01 ? 99  ILE D C   1 
ATOM   3731 O O   . ILE D 1 99  ? 16.430  10.277  2.260   1.00 41.32 ? 99  ILE D O   1 
ATOM   3732 C CB  . ILE D 1 99  ? 18.071  7.620   1.535   1.00 40.83 ? 99  ILE D CB  1 
ATOM   3733 C CG1 . ILE D 1 99  ? 19.214  6.945   0.783   1.00 40.82 ? 99  ILE D CG1 1 
ATOM   3734 C CG2 . ILE D 1 99  ? 17.023  6.558   1.864   1.00 40.95 ? 99  ILE D CG2 1 
ATOM   3735 C CD1 . ILE D 1 99  ? 20.073  6.063   1.653   1.00 41.13 ? 99  ILE D CD1 1 
ATOM   3736 N N   . GLU D 1 100 ? 15.089  8.892   1.110   1.00 41.28 ? 100 GLU D N   1 
ATOM   3737 C CA  . GLU D 1 100 ? 13.899  9.174   1.900   1.00 41.38 ? 100 GLU D CA  1 
ATOM   3738 C C   . GLU D 1 100 ? 13.332  7.836   2.365   1.00 41.38 ? 100 GLU D C   1 
ATOM   3739 O O   . GLU D 1 100 ? 12.979  6.996   1.539   1.00 41.56 ? 100 GLU D O   1 
ATOM   3740 C CB  . GLU D 1 100 ? 12.862  9.930   1.077   1.00 41.32 ? 100 GLU D CB  1 
ATOM   3741 C CG  . GLU D 1 100 ? 11.641  10.335  1.882   1.00 41.54 ? 100 GLU D CG  1 
ATOM   3742 C CD  . GLU D 1 100 ? 10.688  11.227  1.110   1.00 42.07 ? 100 GLU D CD  1 
ATOM   3743 O OE1 . GLU D 1 100 ? 10.352  10.896  -0.050  1.00 43.92 ? 100 GLU D OE1 1 
ATOM   3744 O OE2 . GLU D 1 100 ? 10.260  12.258  1.671   1.00 42.37 ? 100 GLU D OE2 1 
ATOM   3745 N N   . ASP D 1 101 ? 13.255  7.636   3.678   1.00 41.37 ? 101 ASP D N   1 
ATOM   3746 C CA  . ASP D 1 101 ? 12.729  6.393   4.221   1.00 41.37 ? 101 ASP D CA  1 
ATOM   3747 C C   . ASP D 1 101 ? 11.480  6.634   5.064   1.00 41.34 ? 101 ASP D C   1 
ATOM   3748 O O   . ASP D 1 101 ? 11.441  7.540   5.904   1.00 41.25 ? 101 ASP D O   1 
ATOM   3749 C CB  . ASP D 1 101 ? 13.786  5.658   5.048   1.00 41.42 ? 101 ASP D CB  1 
ATOM   3750 C CG  . ASP D 1 101 ? 13.404  4.212   5.310   1.00 41.83 ? 101 ASP D CG  1 
ATOM   3751 O OD1 . ASP D 1 101 ? 13.701  3.360   4.450   1.00 44.46 ? 101 ASP D OD1 1 
ATOM   3752 O OD2 . ASP D 1 101 ? 12.780  3.924   6.353   1.00 42.59 ? 101 ASP D OD2 1 
ATOM   3753 N N   . SER D 1 102 ? 10.462  5.806   4.840   1.00 41.30 ? 102 SER D N   1 
ATOM   3754 C CA  . SER D 1 102 ? 9.194   5.947   5.541   1.00 41.12 ? 102 SER D CA  1 
ATOM   3755 C C   . SER D 1 102 ? 9.039   4.950   6.692   1.00 40.87 ? 102 SER D C   1 
ATOM   3756 O O   . SER D 1 102 ? 8.017   4.967   7.385   1.00 40.92 ? 102 SER D O   1 
ATOM   3757 C CB  . SER D 1 102 ? 8.040   5.786   4.555   1.00 41.39 ? 102 SER D CB  1 
ATOM   3758 O OG  . SER D 1 102 ? 7.670   4.424   4.416   1.00 42.48 ? 102 SER D OG  1 
ATOM   3759 N N   . VAL D 1 103 ? 10.038  4.085   6.892   1.00 40.41 ? 103 VAL D N   1 
ATOM   3760 C CA  . VAL D 1 103 ? 9.952   3.020   7.898   1.00 40.10 ? 103 VAL D CA  1 
ATOM   3761 C C   . VAL D 1 103 ? 10.698  3.378   9.179   1.00 39.79 ? 103 VAL D C   1 
ATOM   3762 O O   . VAL D 1 103 ? 10.221  3.077   10.277  1.00 39.72 ? 103 VAL D O   1 
ATOM   3763 C CB  . VAL D 1 103 ? 10.441  1.662   7.336   1.00 40.02 ? 103 VAL D CB  1 
ATOM   3764 C CG1 . VAL D 1 103 ? 10.479  0.590   8.423   1.00 39.97 ? 103 VAL D CG1 1 
ATOM   3765 C CG2 . VAL D 1 103 ? 9.521   1.214   6.214   1.00 40.12 ? 103 VAL D CG2 1 
ATOM   3766 N N   . ILE D 1 104 ? 11.860  4.015   9.048   1.00 39.41 ? 104 ILE D N   1 
ATOM   3767 C CA  . ILE D 1 104 ? 12.575  4.498   10.222  1.00 39.18 ? 104 ILE D CA  1 
ATOM   3768 C C   . ILE D 1 104 ? 11.890  5.727   10.786  1.00 39.20 ? 104 ILE D C   1 
ATOM   3769 O O   . ILE D 1 104 ? 11.128  6.407   10.096  1.00 38.69 ? 104 ILE D O   1 
ATOM   3770 C CB  . ILE D 1 104 ? 14.067  4.852   9.943   1.00 39.01 ? 104 ILE D CB  1 
ATOM   3771 C CG1 . ILE D 1 104 ? 14.189  5.938   8.874   1.00 38.49 ? 104 ILE D CG1 1 
ATOM   3772 C CG2 . ILE D 1 104 ? 14.847  3.597   9.574   1.00 38.88 ? 104 ILE D CG2 1 
ATOM   3773 C CD1 . ILE D 1 104 ? 15.572  6.483   8.709   1.00 38.83 ? 104 ILE D CD1 1 
ATOM   3774 N N   . SER D 1 105 ? 12.197  6.008   12.046  1.00 39.17 ? 105 SER D N   1 
ATOM   3775 C CA  . SER D 1 105 ? 11.685  7.177   12.727  1.00 39.38 ? 105 SER D CA  1 
ATOM   3776 C C   . SER D 1 105 ? 12.755  7.698   13.666  1.00 39.66 ? 105 SER D C   1 
ATOM   3777 O O   . SER D 1 105 ? 13.705  6.982   13.998  1.00 39.73 ? 105 SER D O   1 
ATOM   3778 C CB  . SER D 1 105 ? 10.429  6.813   13.514  1.00 39.22 ? 105 SER D CB  1 
ATOM   3779 O OG  . SER D 1 105 ? 9.822   7.968   14.049  1.00 39.06 ? 105 SER D OG  1 
ATOM   3780 N N   . LEU D 1 106 ? 12.614  8.955   14.068  1.00 39.60 ? 106 LEU D N   1 
ATOM   3781 C CA  . LEU D 1 106 ? 13.471  9.531   15.096  1.00 39.88 ? 106 LEU D CA  1 
ATOM   3782 C C   . LEU D 1 106 ? 12.810  9.478   16.477  1.00 40.05 ? 106 LEU D C   1 
ATOM   3783 O O   . LEU D 1 106 ? 13.443  9.816   17.471  1.00 40.46 ? 106 LEU D O   1 
ATOM   3784 C CB  . LEU D 1 106 ? 13.839  10.974  14.745  1.00 39.82 ? 106 LEU D CB  1 
ATOM   3785 C CG  . LEU D 1 106 ? 14.547  11.144  13.404  1.00 40.23 ? 106 LEU D CG  1 
ATOM   3786 C CD1 . LEU D 1 106 ? 14.976  12.578  13.241  1.00 41.23 ? 106 LEU D CD1 1 
ATOM   3787 C CD2 . LEU D 1 106 ? 15.750  10.216  13.279  1.00 41.45 ? 106 LEU D CD2 1 
ATOM   3788 N N   . SER D 1 107 ? 11.549  9.051   16.536  1.00 40.12 ? 107 SER D N   1 
ATOM   3789 C CA  . SER D 1 107 ? 10.823  8.934   17.797  1.00 40.17 ? 107 SER D CA  1 
ATOM   3790 C C   . SER D 1 107 ? 10.074  7.612   17.866  1.00 40.19 ? 107 SER D C   1 
ATOM   3791 O O   . SER D 1 107 ? 10.009  6.883   16.882  1.00 40.20 ? 107 SER D O   1 
ATOM   3792 C CB  . SER D 1 107 ? 9.842   10.100  17.961  1.00 40.36 ? 107 SER D CB  1 
ATOM   3793 O OG  . SER D 1 107 ? 8.719   9.970   17.112  1.00 40.38 ? 107 SER D OG  1 
ATOM   3794 N N   . GLY D 1 108 ? 9.534   7.306   19.042  1.00 40.41 ? 108 GLY D N   1 
ATOM   3795 C CA  . GLY D 1 108 ? 8.716   6.117   19.239  1.00 40.69 ? 108 GLY D CA  1 
ATOM   3796 C C   . GLY D 1 108 ? 9.542   4.854   19.315  1.00 40.91 ? 108 GLY D C   1 
ATOM   3797 O O   . GLY D 1 108 ? 10.728  4.904   19.611  1.00 41.01 ? 108 GLY D O   1 
ATOM   3798 N N   . ASP D 1 109 ? 8.900   3.722   19.040  1.00 41.50 ? 109 ASP D N   1 
ATOM   3799 C CA  . ASP D 1 109 ? 9.543   2.404   19.074  1.00 41.75 ? 109 ASP D CA  1 
ATOM   3800 C C   . ASP D 1 109 ? 10.503  2.182   17.915  1.00 42.03 ? 109 ASP D C   1 
ATOM   3801 O O   . ASP D 1 109 ? 11.488  1.464   18.051  1.00 42.63 ? 109 ASP D O   1 
ATOM   3802 C CB  . ASP D 1 109 ? 8.481   1.295   19.030  1.00 41.95 ? 109 ASP D CB  1 
ATOM   3803 C CG  . ASP D 1 109 ? 7.564   1.315   20.228  1.00 41.95 ? 109 ASP D CG  1 
ATOM   3804 O OD1 . ASP D 1 109 ? 7.998   1.798   21.296  1.00 43.06 ? 109 ASP D OD1 1 
ATOM   3805 O OD2 . ASP D 1 109 ? 6.412   0.846   20.098  1.00 41.52 ? 109 ASP D OD2 1 
ATOM   3806 N N   . HIS D 1 110 ? 10.204  2.774   16.764  1.00 42.11 ? 110 HIS D N   1 
ATOM   3807 C CA  . HIS D 1 110 ? 11.082  2.664   15.598  1.00 42.01 ? 110 HIS D CA  1 
ATOM   3808 C C   . HIS D 1 110 ? 12.212  3.709   15.639  1.00 41.68 ? 110 HIS D C   1 
ATOM   3809 O O   . HIS D 1 110 ? 12.859  3.947   14.614  1.00 41.84 ? 110 HIS D O   1 
ATOM   3810 C CB  . HIS D 1 110 ? 10.268  2.820   14.296  1.00 42.59 ? 110 HIS D CB  1 
ATOM   3811 C CG  . HIS D 1 110 ? 9.407   1.638   13.963  1.00 42.98 ? 110 HIS D CG  1 
ATOM   3812 N ND1 . HIS D 1 110 ? 8.942   1.397   12.687  1.00 42.92 ? 110 HIS D ND1 1 
ATOM   3813 C CD2 . HIS D 1 110 ? 8.945   0.621   14.730  1.00 43.42 ? 110 HIS D CD2 1 
ATOM   3814 C CE1 . HIS D 1 110 ? 8.218   0.291   12.686  1.00 43.18 ? 110 HIS D CE1 1 
ATOM   3815 N NE2 . HIS D 1 110 ? 8.207   -0.201  13.913  1.00 43.62 ? 110 HIS D NE2 1 
ATOM   3816 N N   . ALA D 1 111 ? 12.446  4.326   16.801  1.00 40.67 ? 111 ALA D N   1 
ATOM   3817 C CA  . ALA D 1 111 ? 13.436  5.392   16.915  1.00 40.39 ? 111 ALA D CA  1 
ATOM   3818 C C   . ALA D 1 111 ? 14.849  4.862   16.706  1.00 39.88 ? 111 ALA D C   1 
ATOM   3819 O O   . ALA D 1 111 ? 15.256  3.889   17.326  1.00 39.21 ? 111 ALA D O   1 
ATOM   3820 C CB  . ALA D 1 111 ? 13.336  6.082   18.256  1.00 40.35 ? 111 ALA D CB  1 
ATOM   3821 N N   . ILE D 1 112 ? 15.593  5.516   15.825  1.00 39.64 ? 112 ILE D N   1 
ATOM   3822 C CA  . ILE D 1 112 ? 16.974  5.127   15.568  1.00 39.82 ? 112 ILE D CA  1 
ATOM   3823 C C   . ILE D 1 112 ? 17.973  6.012   16.326  1.00 38.92 ? 112 ILE D C   1 
ATOM   3824 O O   . ILE D 1 112 ? 19.163  5.845   16.178  1.00 38.85 ? 112 ILE D O   1 
ATOM   3825 C CB  . ILE D 1 112 ? 17.290  5.084   14.050  1.00 39.70 ? 112 ILE D CB  1 
ATOM   3826 C CG1 . ILE D 1 112 ? 17.142  6.472   13.417  1.00 40.78 ? 112 ILE D CG1 1 
ATOM   3827 C CG2 . ILE D 1 112 ? 16.393  4.052   13.373  1.00 39.76 ? 112 ILE D CG2 1 
ATOM   3828 C CD1 . ILE D 1 112 ? 17.522  6.528   11.960  1.00 40.79 ? 112 ILE D CD1 1 
ATOM   3829 N N   . ILE D 1 113 ? 17.486  6.921   17.161  1.00 39.11 ? 113 ILE D N   1 
ATOM   3830 C CA  . ILE D 1 113 ? 18.377  7.733   18.000  1.00 38.88 ? 113 ILE D CA  1 
ATOM   3831 C C   . ILE D 1 113 ? 19.091  6.806   18.986  1.00 38.24 ? 113 ILE D C   1 
ATOM   3832 O O   . ILE D 1 113 ? 18.471  5.934   19.595  1.00 37.86 ? 113 ILE D O   1 
ATOM   3833 C CB  . ILE D 1 113 ? 17.628  8.856   18.762  1.00 39.27 ? 113 ILE D CB  1 
ATOM   3834 C CG1 . ILE D 1 113 ? 16.864  9.767   17.796  1.00 39.78 ? 113 ILE D CG1 1 
ATOM   3835 C CG2 . ILE D 1 113 ? 18.591  9.705   19.605  1.00 39.14 ? 113 ILE D CG2 1 
ATOM   3836 C CD1 . ILE D 1 113 ? 17.728  10.544  16.804  1.00 40.49 ? 113 ILE D CD1 1 
ATOM   3837 N N   . GLY D 1 114 ? 20.407  6.970   19.099  1.00 37.53 ? 114 GLY D N   1 
ATOM   3838 C CA  . GLY D 1 114 ? 21.200  6.160   20.002  1.00 37.13 ? 114 GLY D CA  1 
ATOM   3839 C C   . GLY D 1 114 ? 21.597  4.809   19.454  1.00 36.48 ? 114 GLY D C   1 
ATOM   3840 O O   . GLY D 1 114 ? 22.265  4.051   20.148  1.00 36.22 ? 114 GLY D O   1 
ATOM   3841 N N   . ARG D 1 115 ? 21.203  4.492   18.216  1.00 36.27 ? 115 ARG D N   1 
ATOM   3842 C CA  . ARG D 1 115 ? 21.642  3.247   17.567  1.00 36.30 ? 115 ARG D CA  1 
ATOM   3843 C C   . ARG D 1 115 ? 22.781  3.599   16.609  1.00 36.33 ? 115 ARG D C   1 
ATOM   3844 O O   . ARG D 1 115 ? 23.267  4.716   16.644  1.00 34.24 ? 115 ARG D O   1 
ATOM   3845 C CB  . ARG D 1 115 ? 20.466  2.564   16.882  1.00 36.27 ? 115 ARG D CB  1 
ATOM   3846 C CG  . ARG D 1 115 ? 19.261  2.530   17.798  1.00 36.36 ? 115 ARG D CG  1 
ATOM   3847 C CD  . ARG D 1 115 ? 18.224  1.529   17.387  1.00 36.22 ? 115 ARG D CD  1 
ATOM   3848 N NE  . ARG D 1 115 ? 17.136  1.534   18.363  1.00 36.67 ? 115 ARG D NE  1 
ATOM   3849 C CZ  . ARG D 1 115 ? 16.979  0.655   19.351  1.00 36.21 ? 115 ARG D CZ  1 
ATOM   3850 N NH1 . ARG D 1 115 ? 17.815  -0.362  19.528  1.00 35.47 ? 115 ARG D NH1 1 
ATOM   3851 N NH2 . ARG D 1 115 ? 15.945  0.781   20.164  1.00 36.91 ? 115 ARG D NH2 1 
ATOM   3852 N N   . THR D 1 116 ? 23.246  2.648   15.794  1.00 35.99 ? 116 THR D N   1 
ATOM   3853 C CA  . THR D 1 116 ? 24.451  2.882   14.965  1.00 36.57 ? 116 THR D CA  1 
ATOM   3854 C C   . THR D 1 116 ? 24.160  2.835   13.457  1.00 36.60 ? 116 THR D C   1 
ATOM   3855 O O   . THR D 1 116 ? 23.522  1.920   12.984  1.00 36.33 ? 116 THR D O   1 
ATOM   3856 C CB  . THR D 1 116 ? 25.574  1.871   15.335  1.00 36.64 ? 116 THR D CB  1 
ATOM   3857 O OG1 . THR D 1 116 ? 26.009  2.121   16.677  1.00 36.95 ? 116 THR D OG1 1 
ATOM   3858 C CG2 . THR D 1 116 ? 26.775  2.004   14.421  1.00 36.21 ? 116 THR D CG2 1 
ATOM   3859 N N   . LEU D 1 117 ? 24.607  3.855   12.715  1.00 36.85 ? 117 LEU D N   1 
ATOM   3860 C CA  . LEU D 1 117 ? 24.539  3.818   11.251  1.00 37.03 ? 117 LEU D CA  1 
ATOM   3861 C C   . LEU D 1 117 ? 25.841  3.236   10.724  1.00 37.70 ? 117 LEU D C   1 
ATOM   3862 O O   . LEU D 1 117 ? 26.909  3.785   11.006  1.00 37.18 ? 117 LEU D O   1 
ATOM   3863 C CB  . LEU D 1 117 ? 24.334  5.217   10.680  1.00 37.12 ? 117 LEU D CB  1 
ATOM   3864 C CG  . LEU D 1 117 ? 24.278  5.369   9.154   1.00 36.24 ? 117 LEU D CG  1 
ATOM   3865 C CD1 . LEU D 1 117 ? 23.004  4.788   8.601   1.00 35.97 ? 117 LEU D CD1 1 
ATOM   3866 C CD2 . LEU D 1 117 ? 24.387  6.869   8.787   1.00 36.94 ? 117 LEU D CD2 1 
ATOM   3867 N N   . VAL D 1 118 ? 25.735  2.125   9.981   1.00 37.82 ? 118 VAL D N   1 
ATOM   3868 C CA  . VAL D 1 118 ? 26.874  1.411   9.389   1.00 38.03 ? 118 VAL D CA  1 
ATOM   3869 C C   . VAL D 1 118 ? 26.852  1.378   7.846   1.00 38.36 ? 118 VAL D C   1 
ATOM   3870 O O   . VAL D 1 118 ? 25.822  1.080   7.234   1.00 38.21 ? 118 VAL D O   1 
ATOM   3871 C CB  . VAL D 1 118 ? 26.904  -0.082  9.836   1.00 37.72 ? 118 VAL D CB  1 
ATOM   3872 C CG1 . VAL D 1 118 ? 28.161  -0.755  9.324   1.00 38.23 ? 118 VAL D CG1 1 
ATOM   3873 C CG2 . VAL D 1 118 ? 26.827  -0.206  11.355  1.00 37.86 ? 118 VAL D CG2 1 
ATOM   3874 N N   . VAL D 1 119 ? 28.007  1.643   7.226   1.00 38.83 ? 119 VAL D N   1 
ATOM   3875 C CA  . VAL D 1 119 ? 28.175  1.397   5.793   1.00 39.05 ? 119 VAL D CA  1 
ATOM   3876 C C   . VAL D 1 119 ? 29.017  0.135   5.608   1.00 39.28 ? 119 VAL D C   1 
ATOM   3877 O O   . VAL D 1 119 ? 30.046  -0.035  6.262   1.00 38.88 ? 119 VAL D O   1 
ATOM   3878 C CB  . VAL D 1 119 ? 28.781  2.595   5.031   1.00 39.39 ? 119 VAL D CB  1 
ATOM   3879 C CG1 . VAL D 1 119 ? 30.109  3.022   5.618   1.00 39.45 ? 119 VAL D CG1 1 
ATOM   3880 C CG2 . VAL D 1 119 ? 28.921  2.256   3.546   1.00 39.16 ? 119 VAL D CG2 1 
ATOM   3881 N N   . HIS D 1 120 ? 28.571  -0.734  4.705   1.00 39.59 ? 120 HIS D N   1 
ATOM   3882 C CA  . HIS D 1 120 ? 29.137  -2.072  4.566   1.00 40.02 ? 120 HIS D CA  1 
ATOM   3883 C C   . HIS D 1 120 ? 29.996  -2.241  3.324   1.00 40.64 ? 120 HIS D C   1 
ATOM   3884 O O   . HIS D 1 120 ? 29.891  -1.479  2.367   1.00 40.42 ? 120 HIS D O   1 
ATOM   3885 C CB  . HIS D 1 120 ? 28.021  -3.100  4.561   1.00 40.02 ? 120 HIS D CB  1 
ATOM   3886 C CG  . HIS D 1 120 ? 27.362  -3.268  5.890   1.00 39.33 ? 120 HIS D CG  1 
ATOM   3887 N ND1 . HIS D 1 120 ? 27.719  -4.259  6.777   1.00 39.01 ? 120 HIS D ND1 1 
ATOM   3888 C CD2 . HIS D 1 120 ? 26.365  -2.574  6.480   1.00 39.12 ? 120 HIS D CD2 1 
ATOM   3889 C CE1 . HIS D 1 120 ? 26.972  -4.163  7.861   1.00 39.52 ? 120 HIS D CE1 1 
ATOM   3890 N NE2 . HIS D 1 120 ? 26.145  -3.144  7.707   1.00 39.45 ? 120 HIS D NE2 1 
ATOM   3891 N N   . GLU D 1 121 ? 30.835  -3.274  3.352   1.00 41.52 ? 121 GLU D N   1 
ATOM   3892 C CA  . GLU D 1 121 ? 31.863  -3.479  2.335   1.00 42.02 ? 121 GLU D CA  1 
ATOM   3893 C C   . GLU D 1 121 ? 31.275  -3.754  0.951   1.00 42.40 ? 121 GLU D C   1 
ATOM   3894 O O   . GLU D 1 121 ? 31.757  -3.234  -0.059  1.00 42.22 ? 121 GLU D O   1 
ATOM   3895 C CB  . GLU D 1 121 ? 32.755  -4.650  2.737   1.00 42.21 ? 121 GLU D CB  1 
ATOM   3896 C CG  . GLU D 1 121 ? 34.071  -4.706  1.966   1.00 42.36 ? 121 GLU D CG  1 
ATOM   3897 C CD  . GLU D 1 121 ? 34.683  -6.088  1.940   1.00 42.85 ? 121 GLU D CD  1 
ATOM   3898 O OE1 . GLU D 1 121 ? 34.037  -7.038  2.433   1.00 44.87 ? 121 GLU D OE1 1 
ATOM   3899 O OE2 . GLU D 1 121 ? 35.811  -6.225  1.415   1.00 43.73 ? 121 GLU D OE2 1 
ATOM   3900 N N   . LYS D 1 122 ? 30.246  -4.591  0.925   1.00 42.80 ? 122 LYS D N   1 
ATOM   3901 C CA  . LYS D 1 122 ? 29.609  -5.005  -0.309  1.00 43.29 ? 122 LYS D CA  1 
ATOM   3902 C C   . LYS D 1 122 ? 28.196  -4.453  -0.376  1.00 43.50 ? 122 LYS D C   1 
ATOM   3903 O O   . LYS D 1 122 ? 27.671  -3.932  0.607   1.00 43.09 ? 122 LYS D O   1 
ATOM   3904 C CB  . LYS D 1 122 ? 29.563  -6.529  -0.384  1.00 43.20 ? 122 LYS D CB  1 
ATOM   3905 C CG  . LYS D 1 122 ? 30.921  -7.193  -0.541  1.00 43.83 ? 122 LYS D CG  1 
ATOM   3906 C CD  . LYS D 1 122 ? 30.782  -8.713  -0.523  1.00 43.65 ? 122 LYS D CD  1 
ATOM   3907 C CE  . LYS D 1 122 ? 32.019  -9.403  -1.062  1.00 44.09 ? 122 LYS D CE  1 
ATOM   3908 N NZ  . LYS D 1 122 ? 31.844  -10.883 -1.157  1.00 44.13 ? 122 LYS D NZ  1 
ATOM   3909 N N   . ALA D 1 123 ? 27.591  -4.583  -1.551  1.00 44.10 ? 123 ALA D N   1 
ATOM   3910 C CA  . ALA D 1 123 ? 26.216  -4.169  -1.771  1.00 44.74 ? 123 ALA D CA  1 
ATOM   3911 C C   . ALA D 1 123 ? 25.264  -4.988  -0.912  1.00 45.35 ? 123 ALA D C   1 
ATOM   3912 O O   . ALA D 1 123 ? 25.545  -6.136  -0.552  1.00 45.58 ? 123 ALA D O   1 
ATOM   3913 C CB  . ALA D 1 123 ? 25.846  -4.314  -3.242  1.00 44.73 ? 123 ALA D CB  1 
ATOM   3914 N N   . ASP D 1 124 ? 24.120  -4.390  -0.615  1.00 46.10 ? 124 ASP D N   1 
ATOM   3915 C CA  . ASP D 1 124 ? 23.140  -4.985  0.279   1.00 46.37 ? 124 ASP D CA  1 
ATOM   3916 C C   . ASP D 1 124 ? 22.517  -6.245  -0.316  1.00 46.36 ? 124 ASP D C   1 
ATOM   3917 O O   . ASP D 1 124 ? 22.499  -6.424  -1.534  1.00 46.67 ? 124 ASP D O   1 
ATOM   3918 C CB  . ASP D 1 124 ? 22.059  -3.946  0.589   1.00 46.73 ? 124 ASP D CB  1 
ATOM   3919 C CG  . ASP D 1 124 ? 21.222  -4.301  1.803   1.00 47.46 ? 124 ASP D CG  1 
ATOM   3920 O OD1 . ASP D 1 124 ? 21.534  -5.317  2.479   1.00 49.46 ? 124 ASP D OD1 1 
ATOM   3921 O OD2 . ASP D 1 124 ? 20.251  -3.544  2.072   1.00 47.61 ? 124 ASP D OD2 1 
ATOM   3922 N N   . SER D 1 142 ? 32.003  -7.209  5.689   1.00 43.23 ? 142 SER D N   1 
ATOM   3923 C CA  . SER D 1 142 ? 32.534  -6.418  6.789   1.00 43.33 ? 142 SER D CA  1 
ATOM   3924 C C   . SER D 1 142 ? 31.941  -4.999  6.844   1.00 43.34 ? 142 SER D C   1 
ATOM   3925 O O   . SER D 1 142 ? 31.265  -4.542  5.910   1.00 43.43 ? 142 SER D O   1 
ATOM   3926 C CB  . SER D 1 142 ? 34.060  -6.336  6.699   1.00 43.57 ? 142 SER D CB  1 
ATOM   3927 O OG  . SER D 1 142 ? 34.469  -5.641  5.531   1.00 44.49 ? 142 SER D OG  1 
ATOM   3928 N N   . ARG D 1 143 ? 32.220  -4.320  7.955   1.00 42.88 ? 143 ARG D N   1 
ATOM   3929 C CA  . ARG D 1 143 ? 31.648  -3.026  8.261   1.00 42.62 ? 143 ARG D CA  1 
ATOM   3930 C C   . ARG D 1 143 ? 32.741  -1.975  8.139   1.00 42.42 ? 143 ARG D C   1 
ATOM   3931 O O   . ARG D 1 143 ? 33.653  -1.909  8.972   1.00 42.42 ? 143 ARG D O   1 
ATOM   3932 C CB  . ARG D 1 143 ? 31.063  -3.053  9.681   1.00 43.02 ? 143 ARG D CB  1 
ATOM   3933 C CG  . ARG D 1 143 ? 30.189  -4.286  9.942   1.00 42.55 ? 143 ARG D CG  1 
ATOM   3934 C CD  . ARG D 1 143 ? 29.325  -4.149  11.189  1.00 42.32 ? 143 ARG D CD  1 
ATOM   3935 N NE  . ARG D 1 143 ? 28.447  -5.312  11.340  1.00 43.33 ? 143 ARG D NE  1 
ATOM   3936 C CZ  . ARG D 1 143 ? 27.729  -5.601  12.427  1.00 42.69 ? 143 ARG D CZ  1 
ATOM   3937 N NH1 . ARG D 1 143 ? 27.754  -4.806  13.494  1.00 41.02 ? 143 ARG D NH1 1 
ATOM   3938 N NH2 . ARG D 1 143 ? 26.971  -6.700  12.437  1.00 41.71 ? 143 ARG D NH2 1 
ATOM   3939 N N   . LEU D 1 144 ? 32.642  -1.157  7.097   1.00 41.88 ? 144 LEU D N   1 
ATOM   3940 C CA  . LEU D 1 144 ? 33.701  -0.216  6.745   1.00 41.41 ? 144 LEU D CA  1 
ATOM   3941 C C   . LEU D 1 144 ? 33.778  0.949   7.712   1.00 40.89 ? 144 LEU D C   1 
ATOM   3942 O O   . LEU D 1 144 ? 34.870  1.385   8.080   1.00 40.79 ? 144 LEU D O   1 
ATOM   3943 C CB  . LEU D 1 144 ? 33.493  0.323   5.332   1.00 41.50 ? 144 LEU D CB  1 
ATOM   3944 C CG  . LEU D 1 144 ? 33.345  -0.692  4.195   1.00 42.16 ? 144 LEU D CG  1 
ATOM   3945 C CD1 . LEU D 1 144 ? 33.225  0.063   2.882   1.00 42.61 ? 144 LEU D CD1 1 
ATOM   3946 C CD2 . LEU D 1 144 ? 34.507  -1.681  4.151   1.00 42.47 ? 144 LEU D CD2 1 
ATOM   3947 N N   . ALA D 1 145 ? 32.618  1.461   8.108   1.00 40.43 ? 145 ALA D N   1 
ATOM   3948 C CA  . ALA D 1 145 ? 32.551  2.579   9.041   1.00 40.01 ? 145 ALA D CA  1 
ATOM   3949 C C   . ALA D 1 145 ? 31.215  2.612   9.759   1.00 39.80 ? 145 ALA D C   1 
ATOM   3950 O O   . ALA D 1 145 ? 30.198  2.159   9.223   1.00 39.73 ? 145 ALA D O   1 
ATOM   3951 C CB  . ALA D 1 145 ? 32.785  3.880   8.317   1.00 40.03 ? 145 ALA D CB  1 
ATOM   3952 N N   . ALA D 1 146 ? 31.235  3.138   10.983  1.00 39.47 ? 146 ALA D N   1 
ATOM   3953 C CA  . ALA D 1 146 ? 30.033  3.271   11.790  1.00 39.08 ? 146 ALA D CA  1 
ATOM   3954 C C   . ALA D 1 146 ? 30.042  4.573   12.559  1.00 38.70 ? 146 ALA D C   1 
ATOM   3955 O O   . ALA D 1 146 ? 31.088  5.205   12.733  1.00 38.54 ? 146 ALA D O   1 
ATOM   3956 C CB  . ALA D 1 146 ? 29.907  2.119   12.741  1.00 39.26 ? 146 ALA D CB  1 
ATOM   3957 N N   . GLY D 1 147 ? 28.860  4.963   13.021  1.00 38.29 ? 147 GLY D N   1 
ATOM   3958 C CA  . GLY D 1 147 ? 28.704  6.151   13.851  1.00 37.76 ? 147 GLY D CA  1 
ATOM   3959 C C   . GLY D 1 147 ? 27.418  6.071   14.640  1.00 37.45 ? 147 GLY D C   1 
ATOM   3960 O O   . GLY D 1 147 ? 26.389  5.711   14.088  1.00 38.08 ? 147 GLY D O   1 
ATOM   3961 N N   . VAL D 1 148 ? 27.462  6.398   15.928  1.00 37.02 ? 148 VAL D N   1 
ATOM   3962 C CA  . VAL D 1 148 ? 26.245  6.417   16.734  1.00 37.06 ? 148 VAL D CA  1 
ATOM   3963 C C   . VAL D 1 148 ? 25.350  7.535   16.247  1.00 37.51 ? 148 VAL D C   1 
ATOM   3964 O O   . VAL D 1 148 ? 25.817  8.667   16.051  1.00 35.87 ? 148 VAL D O   1 
ATOM   3965 C CB  . VAL D 1 148 ? 26.537  6.611   18.238  1.00 36.91 ? 148 VAL D CB  1 
ATOM   3966 C CG1 . VAL D 1 148 ? 25.240  6.820   19.012  1.00 36.71 ? 148 VAL D CG1 1 
ATOM   3967 C CG2 . VAL D 1 148 ? 27.289  5.413   18.794  1.00 39.59 ? 148 VAL D CG2 1 
ATOM   3968 N N   . ILE D 1 149 ? 24.061  7.242   16.086  1.00 37.06 ? 149 ILE D N   1 
ATOM   3969 C CA  . ILE D 1 149 ? 23.103  8.298   15.653  1.00 36.74 ? 149 ILE D CA  1 
ATOM   3970 C C   . ILE D 1 149 ? 22.655  9.181   16.821  1.00 35.83 ? 149 ILE D C   1 
ATOM   3971 O O   . ILE D 1 149 ? 22.009  8.713   17.749  1.00 34.02 ? 149 ILE D O   1 
ATOM   3972 C CB  . ILE D 1 149 ? 21.856  7.646   14.997  1.00 37.44 ? 149 ILE D CB  1 
ATOM   3973 C CG1 . ILE D 1 149 ? 22.289  6.728   13.840  1.00 36.59 ? 149 ILE D CG1 1 
ATOM   3974 C CG2 . ILE D 1 149 ? 20.894  8.717   14.516  1.00 37.00 ? 149 ILE D CG2 1 
ATOM   3975 C CD1 . ILE D 1 149 ? 21.221  5.853   13.302  1.00 37.07 ? 149 ILE D CD1 1 
ATOM   3976 N N   . GLY D 1 150 ? 22.948  10.484  16.767  1.00 35.97 ? 150 GLY D N   1 
ATOM   3977 C CA  . GLY D 1 150 ? 22.651  11.336  17.890  1.00 36.08 ? 150 GLY D CA  1 
ATOM   3978 C C   . GLY D 1 150 ? 21.808  12.536  17.491  1.00 36.50 ? 150 GLY D C   1 
ATOM   3979 O O   . GLY D 1 150 ? 21.638  12.830  16.313  1.00 35.65 ? 150 GLY D O   1 
ATOM   3980 N N   . ILE D 1 151 ? 21.286  13.212  18.501  1.00 36.66 ? 151 ILE D N   1 
ATOM   3981 C CA  . ILE D 1 151 ? 20.341  14.288  18.320  1.00 36.78 ? 151 ILE D CA  1 
ATOM   3982 C C   . ILE D 1 151 ? 21.123  15.473  17.793  1.00 37.22 ? 151 ILE D C   1 
ATOM   3983 O O   . ILE D 1 151 ? 22.233  15.736  18.259  1.00 36.87 ? 151 ILE D O   1 
ATOM   3984 C CB  . ILE D 1 151 ? 19.644  14.618  19.661  1.00 36.68 ? 151 ILE D CB  1 
ATOM   3985 C CG1 . ILE D 1 151 ? 18.823  13.411  20.137  1.00 36.99 ? 151 ILE D CG1 1 
ATOM   3986 C CG2 . ILE D 1 151 ? 18.748  15.844  19.529  1.00 36.89 ? 151 ILE D CG2 1 
ATOM   3987 C CD1 . ILE D 1 151 ? 18.229  13.563  21.527  1.00 36.74 ? 151 ILE D CD1 1 
ATOM   3988 N N   . ALA D 1 152 ? 20.544  16.170  16.812  1.00 38.09 ? 152 ALA D N   1 
ATOM   3989 C CA  . ALA D 1 152 ? 21.180  17.308  16.159  1.00 37.86 ? 152 ALA D CA  1 
ATOM   3990 C C   . ALA D 1 152 ? 20.380  18.578  16.405  1.00 38.76 ? 152 ALA D C   1 
ATOM   3991 O O   . ALA D 1 152 ? 19.191  18.513  16.754  1.00 39.05 ? 152 ALA D O   1 
ATOM   3992 C CB  . ALA D 1 152 ? 21.318  17.051  14.670  1.00 37.58 ? 152 ALA D CB  1 
ATOM   3993 N N   . GLN D 1 153 ? 21.037  19.729  16.217  1.00 38.97 ? 153 GLN D N   1 
ATOM   3994 C CA  . GLN D 1 153 ? 20.427  21.022  16.511  1.00 39.22 ? 153 GLN D CA  1 
ATOM   3995 C C   . GLN D 1 153 ? 19.493  21.461  15.399  1.00 40.12 ? 153 GLN D C   1 
ATOM   3996 O O   . GLN D 1 153 ? 19.739  21.151  14.229  1.00 40.81 ? 153 GLN D O   1 
ATOM   3997 C CB  . GLN D 1 153 ? 21.497  22.109  16.735  1.00 38.97 ? 153 GLN D CB  1 
ATOM   3998 C CG  . GLN D 1 153 ? 20.954  23.323  17.473  1.00 39.08 ? 153 GLN D CG  1 
ATOM   3999 C CD  . GLN D 1 153 ? 22.047  24.253  18.016  1.00 38.84 ? 153 GLN D CD  1 
ATOM   4000 O OE1 . GLN D 1 153 ? 23.105  24.418  17.394  1.00 35.81 ? 153 GLN D OE1 1 
ATOM   4001 N NE2 . GLN D 1 153 ? 21.783  24.878  19.170  1.00 36.43 ? 153 GLN D NE2 1 
ATOM   4002 O OXT . GLN D 1 153 ? 18.499  22.173  15.644  1.00 41.04 ? 153 GLN D OXT 1 
HETATM 4003 O O   . HOH E 2 .   ? -10.307 5.743   33.954  1.00 38.02 ? 154 HOH A O   1 
HETATM 4004 O O   . HOH E 2 .   ? -28.621 -3.923  24.793  1.00 39.67 ? 155 HOH A O   1 
HETATM 4005 O O   . HOH E 2 .   ? -4.246  4.454   14.003  1.00 27.46 ? 156 HOH A O   1 
HETATM 4006 O O   . HOH E 2 .   ? -11.892 -3.726  33.205  1.00 31.71 ? 157 HOH A O   1 
HETATM 4007 O O   . HOH E 2 .   ? -7.082  -0.693  3.392   1.00 35.86 ? 158 HOH A O   1 
HETATM 4008 O O   . HOH E 2 .   ? -3.611  2.465   12.533  1.00 28.57 ? 159 HOH A O   1 
HETATM 4009 O O   . HOH E 2 .   ? -20.558 2.010   29.942  1.00 31.99 ? 160 HOH A O   1 
HETATM 4010 O O   . HOH E 2 .   ? -24.727 1.084   12.061  1.00 35.07 ? 161 HOH A O   1 
HETATM 4011 O O   . HOH E 2 .   ? -9.305  9.394   14.721  1.00 43.39 ? 162 HOH A O   1 
HETATM 4012 O O   . HOH E 2 .   ? -13.758 -1.778  12.921  1.00 27.80 ? 163 HOH A O   1 
HETATM 4013 O O   . HOH E 2 .   ? -12.579 -6.231  8.140   1.00 33.58 ? 164 HOH A O   1 
HETATM 4014 O O   . HOH E 2 .   ? -23.531 -3.293  32.827  1.00 53.25 ? 165 HOH A O   1 
HETATM 4015 O O   . HOH E 2 .   ? -0.264  2.838   23.830  1.00 38.16 ? 166 HOH A O   1 
HETATM 4016 O O   . HOH E 2 .   ? -25.979 8.628   4.884   1.00 47.41 ? 167 HOH A O   1 
HETATM 4017 O O   . HOH E 2 .   ? -13.670 -8.573  14.718  1.00 35.67 ? 168 HOH A O   1 
HETATM 4018 O O   . HOH E 2 .   ? -3.197  8.765   24.037  1.00 46.10 ? 169 HOH A O   1 
HETATM 4019 O O   . HOH E 2 .   ? -31.565 -9.470  22.776  1.00 47.69 ? 170 HOH A O   1 
HETATM 4020 O O   . HOH E 2 .   ? -17.833 1.503   32.208  1.00 35.66 ? 171 HOH A O   1 
HETATM 4021 O O   . HOH E 2 .   ? -5.057  -8.131  12.565  1.00 42.58 ? 172 HOH A O   1 
HETATM 4022 O O   . HOH E 2 .   ? -5.963  8.367   19.076  1.00 42.18 ? 173 HOH A O   1 
HETATM 4023 O O   . HOH E 2 .   ? 5.526   2.808   16.607  1.00 53.86 ? 174 HOH A O   1 
HETATM 4024 O O   . HOH E 2 .   ? 0.474   -8.999  31.862  1.00 38.33 ? 175 HOH A O   1 
HETATM 4025 O O   . HOH E 2 .   ? -13.351 0.137   33.829  1.00 33.76 ? 176 HOH A O   1 
HETATM 4026 O O   . HOH E 2 .   ? -8.673  -8.903  13.792  1.00 42.80 ? 177 HOH A O   1 
HETATM 4027 O O   . HOH E 2 .   ? -26.659 -7.115  12.526  1.00 40.10 ? 178 HOH A O   1 
HETATM 4028 O O   . HOH E 2 .   ? -14.700 2.323   32.667  1.00 41.27 ? 179 HOH A O   1 
HETATM 4029 O O   . HOH E 2 .   ? -10.846 8.234   11.265  1.00 34.41 ? 180 HOH A O   1 
HETATM 4030 O O   . HOH E 2 .   ? -25.375 5.975   9.078   1.00 53.29 ? 181 HOH A O   1 
HETATM 4031 O O   . HOH E 2 .   ? -0.420  1.423   27.670  1.00 41.27 ? 182 HOH A O   1 
HETATM 4032 O O   . HOH E 2 .   ? -21.311 -3.990  9.129   1.00 51.09 ? 183 HOH A O   1 
HETATM 4033 O O   . HOH E 2 .   ? -27.090 -4.129  15.021  1.00 44.62 ? 184 HOH A O   1 
HETATM 4034 O O   . HOH E 2 .   ? -17.893 4.961   2.976   1.00 45.93 ? 185 HOH A O   1 
HETATM 4035 O O   . HOH E 2 .   ? -20.001 -2.635  5.958   1.00 52.40 ? 186 HOH A O   1 
HETATM 4036 O O   . HOH E 2 .   ? -32.882 -8.911  20.443  1.00 43.06 ? 187 HOH A O   1 
HETATM 4037 O O   . HOH E 2 .   ? -4.142  12.377  22.054  1.00 37.06 ? 188 HOH A O   1 
HETATM 4038 O O   . HOH E 2 .   ? -7.275  -12.485 30.716  1.00 42.28 ? 189 HOH A O   1 
HETATM 4039 O O   . HOH E 2 .   ? -14.056 -2.169  34.334  1.00 44.18 ? 190 HOH A O   1 
HETATM 4040 O O   . HOH E 2 .   ? -23.109 -10.549 36.372  1.00 59.57 ? 191 HOH A O   1 
HETATM 4041 O O   . HOH E 2 .   ? 3.802   -10.171 25.087  1.00 50.49 ? 192 HOH A O   1 
HETATM 4042 O O   . HOH E 2 .   ? 4.081   -4.751  20.799  1.00 43.42 ? 193 HOH A O   1 
HETATM 4043 O O   . HOH E 2 .   ? 8.726   -14.230 16.460  1.00 56.37 ? 194 HOH A O   1 
HETATM 4044 O O   . HOH E 2 .   ? 0.346   -7.186  17.804  1.00 35.63 ? 195 HOH A O   1 
HETATM 4045 O O   . HOH E 2 .   ? -15.111 -17.083 23.339  1.00 43.40 ? 196 HOH A O   1 
HETATM 4046 O O   . HOH E 2 .   ? -17.869 -13.942 30.246  1.00 49.55 ? 197 HOH A O   1 
HETATM 4047 O O   . HOH E 2 .   ? -11.665 7.779   24.732  1.00 44.44 ? 198 HOH A O   1 
HETATM 4048 O O   . HOH E 2 .   ? -13.519 3.917   30.539  1.00 37.80 ? 199 HOH A O   1 
HETATM 4049 O O   . HOH E 2 .   ? -9.546  10.777  30.231  1.00 30.16 ? 200 HOH A O   1 
HETATM 4050 O O   . HOH E 2 .   ? -15.241 10.208  30.953  1.00 41.02 ? 201 HOH A O   1 
HETATM 4051 O O   . HOH E 2 .   ? -21.756 11.319  30.826  1.00 48.56 ? 202 HOH A O   1 
HETATM 4052 O O   . HOH E 2 .   ? -18.783 11.113  28.720  1.00 47.42 ? 203 HOH A O   1 
HETATM 4053 O O   . HOH E 2 .   ? -9.007  9.122   17.374  1.00 54.87 ? 204 HOH A O   1 
HETATM 4054 O O   . HOH E 2 .   ? 0.001   9.296   17.547  1.00 50.41 ? 205 HOH A O   1 
HETATM 4055 O O   . HOH E 2 .   ? -2.413  0.566   11.681  1.00 36.58 ? 206 HOH A O   1 
HETATM 4056 O O   . HOH E 2 .   ? -3.162  -1.318  9.952   1.00 37.89 ? 207 HOH A O   1 
HETATM 4057 O O   . HOH E 2 .   ? -13.872 -2.277  5.095   1.00 47.58 ? 208 HOH A O   1 
HETATM 4058 O O   . HOH E 2 .   ? -6.675  -3.393  2.912   1.00 41.89 ? 209 HOH A O   1 
HETATM 4059 O O   . HOH E 2 .   ? -18.493 -7.087  10.628  1.00 32.82 ? 210 HOH A O   1 
HETATM 4060 O O   . HOH E 2 .   ? -15.336 -8.230  12.895  1.00 38.88 ? 211 HOH A O   1 
HETATM 4061 O O   . HOH E 2 .   ? -18.871 -12.402 18.567  1.00 38.68 ? 212 HOH A O   1 
HETATM 4062 O O   . HOH E 2 .   ? -21.980 -14.984 18.778  1.00 56.71 ? 213 HOH A O   1 
HETATM 4063 O O   . HOH E 2 .   ? -25.562 -18.632 19.986  1.00 49.01 ? 214 HOH A O   1 
HETATM 4064 O O   . HOH E 2 .   ? -29.453 -16.965 17.630  1.00 49.63 ? 215 HOH A O   1 
HETATM 4065 O O   . HOH E 2 .   ? -15.295 -14.972 17.006  1.00 49.17 ? 216 HOH A O   1 
HETATM 4066 O O   . HOH E 2 .   ? -9.845  -12.688 14.195  1.00 50.10 ? 217 HOH A O   1 
HETATM 4067 O O   . HOH E 2 .   ? -11.155 -10.165 13.563  1.00 42.76 ? 218 HOH A O   1 
HETATM 4068 O O   . HOH E 2 .   ? -8.910  -9.465  11.128  1.00 46.44 ? 219 HOH A O   1 
HETATM 4069 O O   . HOH E 2 .   ? -17.096 -16.767 18.209  1.00 41.08 ? 220 HOH A O   1 
HETATM 4070 O O   . HOH E 2 .   ? -21.306 6.623   15.180  1.00 40.55 ? 221 HOH A O   1 
HETATM 4071 O O   . HOH E 2 .   ? 6.320   -3.075  21.121  1.00 49.13 ? 222 HOH A O   1 
HETATM 4072 O O   . HOH E 2 .   ? -19.464 -16.625 30.033  1.00 49.19 ? 223 HOH A O   1 
HETATM 4073 O O   . HOH E 2 .   ? -26.886 -13.417 15.473  1.00 45.53 ? 224 HOH A O   1 
HETATM 4074 O O   . HOH E 2 .   ? -15.919 9.729   28.199  1.00 46.59 ? 225 HOH A O   1 
HETATM 4075 O O   . HOH E 2 .   ? -10.901 1.942   5.687   1.00 46.03 ? 226 HOH A O   1 
HETATM 4076 O O   . HOH E 2 .   ? -5.097  -5.804  3.764   1.00 55.05 ? 227 HOH A O   1 
HETATM 4077 O O   . HOH E 2 .   ? 2.879   -1.208  19.839  1.00 39.17 ? 228 HOH A O   1 
HETATM 4078 O O   . HOH E 2 .   ? 3.093   -7.543  24.655  1.00 44.34 ? 229 HOH A O   1 
HETATM 4079 O O   . HOH E 2 .   ? 3.887   -0.555  26.921  1.00 52.20 ? 230 HOH A O   1 
HETATM 4080 O O   . HOH E 2 .   ? 3.532   2.037   26.359  1.00 43.53 ? 231 HOH A O   1 
HETATM 4081 O O   . HOH E 2 .   ? 0.624   5.780   20.903  1.00 47.22 ? 232 HOH A O   1 
HETATM 4082 O O   . HOH E 2 .   ? -25.038 1.314   9.268   1.00 41.03 ? 233 HOH A O   1 
HETATM 4083 O O   . HOH E 2 .   ? -21.851 12.141  4.533   1.00 43.62 ? 234 HOH A O   1 
HETATM 4084 O O   . HOH E 2 .   ? -21.850 11.567  8.210   1.00 47.72 ? 235 HOH A O   1 
HETATM 4085 O O   . HOH E 2 .   ? -12.750 8.667   15.441  1.00 46.42 ? 236 HOH A O   1 
HETATM 4086 O O   . HOH E 2 .   ? -10.507 -16.940 16.035  1.00 53.10 ? 237 HOH A O   1 
HETATM 4087 O O   . HOH E 2 .   ? -5.854  14.402  21.960  1.00 45.14 ? 238 HOH A O   1 
HETATM 4088 O O   . HOH F 2 .   ? 5.201   2.047   39.493  1.00 28.85 ? 154 HOH B O   1 
HETATM 4089 O O   . HOH F 2 .   ? -0.414  8.780   51.160  1.00 37.15 ? 155 HOH B O   1 
HETATM 4090 O O   . HOH F 2 .   ? -10.959 3.989   35.995  1.00 25.79 ? 156 HOH B O   1 
HETATM 4091 O O   . HOH F 2 .   ? 8.465   1.573   35.967  1.00 36.54 ? 157 HOH B O   1 
HETATM 4092 O O   . HOH F 2 .   ? -12.547 -6.929  49.663  1.00 35.40 ? 158 HOH B O   1 
HETATM 4093 O O   . HOH F 2 .   ? 1.713   -8.499  37.423  1.00 38.07 ? 159 HOH B O   1 
HETATM 4094 O O   . HOH F 2 .   ? 12.526  3.803   56.077  1.00 38.76 ? 160 HOH B O   1 
HETATM 4095 O O   . HOH F 2 .   ? -16.149 3.914   54.910  1.00 34.33 ? 161 HOH B O   1 
HETATM 4096 O O   . HOH F 2 .   ? 3.970   9.337   48.933  1.00 34.90 ? 162 HOH B O   1 
HETATM 4097 O O   . HOH F 2 .   ? -1.544  7.131   57.739  1.00 34.55 ? 163 HOH B O   1 
HETATM 4098 O O   . HOH F 2 .   ? 8.274   8.086   40.423  1.00 34.29 ? 164 HOH B O   1 
HETATM 4099 O O   . HOH F 2 .   ? 7.524   8.676   47.757  1.00 35.92 ? 165 HOH B O   1 
HETATM 4100 O O   . HOH F 2 .   ? 7.249   -3.571  45.381  1.00 31.66 ? 166 HOH B O   1 
HETATM 4101 O O   . HOH F 2 .   ? 7.640   14.009  37.478  1.00 34.18 ? 167 HOH B O   1 
HETATM 4102 O O   . HOH F 2 .   ? -2.537  11.402  27.931  1.00 43.58 ? 168 HOH B O   1 
HETATM 4103 O O   . HOH F 2 .   ? 11.025  11.045  41.971  1.00 55.58 ? 169 HOH B O   1 
HETATM 4104 O O   . HOH F 2 .   ? -20.653 4.129   44.892  1.00 44.27 ? 170 HOH B O   1 
HETATM 4105 O O   . HOH F 2 .   ? -6.697  12.655  52.279  1.00 45.13 ? 171 HOH B O   1 
HETATM 4106 O O   . HOH F 2 .   ? -13.805 16.713  59.677  1.00 43.68 ? 172 HOH B O   1 
HETATM 4107 O O   . HOH F 2 .   ? -19.703 12.001  51.701  1.00 38.61 ? 173 HOH B O   1 
HETATM 4108 O O   . HOH F 2 .   ? -19.566 4.321   42.548  1.00 44.15 ? 174 HOH B O   1 
HETATM 4109 O O   . HOH F 2 .   ? 2.765   -7.561  42.565  1.00 41.09 ? 175 HOH B O   1 
HETATM 4110 O O   . HOH F 2 .   ? 0.760   2.058   52.753  1.00 31.85 ? 176 HOH B O   1 
HETATM 4111 O O   . HOH F 2 .   ? 4.595   15.201  38.408  1.00 38.40 ? 177 HOH B O   1 
HETATM 4112 O O   . HOH F 2 .   ? -9.210  6.819   61.667  1.00 44.95 ? 178 HOH B O   1 
HETATM 4113 O O   . HOH F 2 .   ? -9.028  14.897  53.751  1.00 49.25 ? 179 HOH B O   1 
HETATM 4114 O O   . HOH F 2 .   ? -14.177 2.240   37.425  1.00 42.50 ? 180 HOH B O   1 
HETATM 4115 O O   . HOH F 2 .   ? -2.663  -11.500 61.348  1.00 51.99 ? 181 HOH B O   1 
HETATM 4116 O O   . HOH F 2 .   ? 13.891  12.758  32.946  1.00 42.49 ? 182 HOH B O   1 
HETATM 4117 O O   . HOH F 2 .   ? 3.055   -7.542  35.083  1.00 43.92 ? 183 HOH B O   1 
HETATM 4118 O O   . HOH F 2 .   ? 6.231   11.441  32.495  1.00 33.08 ? 184 HOH B O   1 
HETATM 4119 O O   . HOH F 2 .   ? -12.550 -2.130  38.389  1.00 46.76 ? 185 HOH B O   1 
HETATM 4120 O O   . HOH F 2 .   ? -20.167 9.325   54.986  1.00 39.68 ? 186 HOH B O   1 
HETATM 4121 O O   . HOH F 2 .   ? -18.598 8.792   59.681  1.00 40.15 ? 187 HOH B O   1 
HETATM 4122 O O   . HOH F 2 .   ? -17.293 17.763  52.742  1.00 56.80 ? 188 HOH B O   1 
HETATM 4123 O O   . HOH F 2 .   ? 3.586   -5.139  62.694  1.00 49.88 ? 189 HOH B O   1 
HETATM 4124 O O   . HOH F 2 .   ? 5.860   8.905   33.193  1.00 32.51 ? 190 HOH B O   1 
HETATM 4125 O O   . HOH F 2 .   ? 6.552   5.890   57.953  1.00 43.70 ? 191 HOH B O   1 
HETATM 4126 O O   . HOH F 2 .   ? -4.492  11.087  55.075  1.00 40.47 ? 192 HOH B O   1 
HETATM 4127 O O   . HOH F 2 .   ? -2.501  9.673   57.284  1.00 41.58 ? 193 HOH B O   1 
HETATM 4128 O O   . HOH F 2 .   ? -2.207  3.681   60.607  1.00 40.62 ? 194 HOH B O   1 
HETATM 4129 O O   . HOH F 2 .   ? -3.926  -2.883  62.502  1.00 43.76 ? 195 HOH B O   1 
HETATM 4130 O O   . HOH F 2 .   ? -0.758  19.428  37.245  1.00 44.62 ? 196 HOH B O   1 
HETATM 4131 O O   . HOH F 2 .   ? -7.177  18.878  38.256  1.00 52.33 ? 197 HOH B O   1 
HETATM 4132 O O   . HOH F 2 .   ? -18.449 3.765   53.466  1.00 40.29 ? 198 HOH B O   1 
HETATM 4133 O O   . HOH F 2 .   ? -19.740 1.592   52.753  1.00 47.21 ? 199 HOH B O   1 
HETATM 4134 O O   . HOH F 2 .   ? -10.123 -5.517  34.510  1.00 36.47 ? 200 HOH B O   1 
HETATM 4135 O O   . HOH F 2 .   ? -10.184 -3.399  38.736  1.00 41.90 ? 201 HOH B O   1 
HETATM 4136 O O   . HOH F 2 .   ? 1.849   -9.183  45.612  1.00 44.41 ? 202 HOH B O   1 
HETATM 4137 O O   . HOH F 2 .   ? 5.346   -10.020 44.433  1.00 47.86 ? 203 HOH B O   1 
HETATM 4138 O O   . HOH F 2 .   ? 10.264  4.807   49.962  1.00 45.02 ? 204 HOH B O   1 
HETATM 4139 O O   . HOH F 2 .   ? -7.294  17.313  45.983  1.00 44.59 ? 205 HOH B O   1 
HETATM 4140 O O   . HOH F 2 .   ? -4.212  12.724  50.664  1.00 38.32 ? 206 HOH B O   1 
HETATM 4141 O O   . HOH F 2 .   ? -5.554  16.632  51.278  1.00 52.14 ? 207 HOH B O   1 
HETATM 4142 O O   . HOH F 2 .   ? -12.803 -6.874  56.179  1.00 56.47 ? 208 HOH B O   1 
HETATM 4143 O O   . HOH F 2 .   ? -5.152  -9.140  61.544  1.00 48.29 ? 209 HOH B O   1 
HETATM 4144 O O   . HOH F 2 .   ? -18.068 -1.681  46.835  1.00 47.72 ? 210 HOH B O   1 
HETATM 4145 O O   . HOH F 2 .   ? -12.237 0.446   36.374  1.00 38.69 ? 211 HOH B O   1 
HETATM 4146 O O   . HOH F 2 .   ? -16.834 7.906   40.695  1.00 39.62 ? 212 HOH B O   1 
HETATM 4147 O O   . HOH F 2 .   ? 10.615  12.739  30.972  1.00 40.89 ? 213 HOH B O   1 
HETATM 4148 O O   . HOH F 2 .   ? -16.115 13.849  46.513  1.00 51.50 ? 214 HOH B O   1 
HETATM 4149 O O   . HOH F 2 .   ? -5.466  -7.324  42.348  1.00 44.34 ? 215 HOH B O   1 
HETATM 4150 O O   . HOH F 2 .   ? -7.417  -5.289  42.649  1.00 44.58 ? 216 HOH B O   1 
HETATM 4151 O O   . HOH F 2 .   ? 4.648   6.176   55.910  1.00 39.85 ? 217 HOH B O   1 
HETATM 4152 O O   . HOH F 2 .   ? 5.615   1.785   58.876  1.00 43.78 ? 218 HOH B O   1 
HETATM 4153 O O   . HOH F 2 .   ? 8.368   -1.105  56.478  1.00 42.70 ? 219 HOH B O   1 
HETATM 4154 O O   . HOH F 2 .   ? 0.502   6.876   55.456  1.00 48.56 ? 220 HOH B O   1 
HETATM 4155 O O   . HOH F 2 .   ? 1.883   10.185  50.744  1.00 40.43 ? 221 HOH B O   1 
HETATM 4156 O O   . HOH F 2 .   ? -1.099  16.458  44.925  1.00 54.24 ? 222 HOH B O   1 
HETATM 4157 O O   . HOH F 2 .   ? 2.958   13.729  49.225  1.00 46.02 ? 223 HOH B O   1 
HETATM 4158 O O   . HOH F 2 .   ? 5.558   13.376  49.261  1.00 46.30 ? 224 HOH B O   1 
HETATM 4159 O O   . HOH F 2 .   ? 7.647   12.743  45.889  1.00 48.55 ? 225 HOH B O   1 
HETATM 4160 O O   . HOH F 2 .   ? 2.453   3.795   30.696  1.00 46.13 ? 226 HOH B O   1 
HETATM 4161 O O   . HOH F 2 .   ? 9.296   -0.554  29.240  1.00 57.35 ? 227 HOH B O   1 
HETATM 4162 O O   . HOH F 2 .   ? 3.246   -2.473  34.837  1.00 51.24 ? 228 HOH B O   1 
HETATM 4163 O O   . HOH F 2 .   ? -15.513 1.624   56.210  1.00 46.65 ? 229 HOH B O   1 
HETATM 4164 O O   . HOH F 2 .   ? -9.089  1.693   61.209  1.00 55.05 ? 230 HOH B O   1 
HETATM 4165 O O   . HOH F 2 .   ? -7.026  -1.103  60.216  1.00 46.50 ? 231 HOH B O   1 
HETATM 4166 O O   . HOH F 2 .   ? -6.750  -6.633  55.358  1.00 47.90 ? 232 HOH B O   1 
HETATM 4167 O O   . HOH F 2 .   ? -6.809  -5.340  52.736  1.00 43.52 ? 233 HOH B O   1 
HETATM 4168 O O   . HOH G 2 .   ? 17.857  12.856  31.350  1.00 37.14 ? 154 HOH C O   1 
HETATM 4169 O O   . HOH G 2 .   ? 8.938   5.756   34.325  1.00 32.76 ? 155 HOH C O   1 
HETATM 4170 O O   . HOH G 2 .   ? 41.363  10.711  22.094  1.00 33.44 ? 156 HOH C O   1 
HETATM 4171 O O   . HOH G 2 .   ? 15.143  3.934   31.900  1.00 28.71 ? 157 HOH C O   1 
HETATM 4172 O O   . HOH G 2 .   ? 29.974  6.221   21.875  1.00 29.80 ? 158 HOH C O   1 
HETATM 4173 O O   . HOH G 2 .   ? 46.761  7.874   30.934  1.00 45.14 ? 159 HOH C O   1 
HETATM 4174 O O   . HOH G 2 .   ? 12.813  7.580   32.786  1.00 33.11 ? 160 HOH C O   1 
HETATM 4175 O O   . HOH G 2 .   ? 17.045  8.840   37.306  1.00 34.30 ? 161 HOH C O   1 
HETATM 4176 O O   . HOH G 2 .   ? 27.256  12.791  15.853  1.00 29.91 ? 162 HOH C O   1 
HETATM 4177 O O   . HOH G 2 .   ? 17.133  2.627   38.543  1.00 35.31 ? 163 HOH C O   1 
HETATM 4178 O O   . HOH G 2 .   ? 9.283   0.008   40.259  1.00 44.46 ? 164 HOH C O   1 
HETATM 4179 O O   . HOH G 2 .   ? 31.150  13.659  39.808  1.00 34.57 ? 165 HOH C O   1 
HETATM 4180 O O   . HOH G 2 .   ? 13.073  11.965  30.620  1.00 36.50 ? 166 HOH C O   1 
HETATM 4181 O O   . HOH G 2 .   ? 26.107  12.481  40.033  1.00 45.81 ? 167 HOH C O   1 
HETATM 4182 O O   . HOH G 2 .   ? 22.668  15.118  36.818  1.00 36.30 ? 168 HOH C O   1 
HETATM 4183 O O   . HOH G 2 .   ? 36.579  9.655   38.741  1.00 34.02 ? 169 HOH C O   1 
HETATM 4184 O O   . HOH G 2 .   ? 45.143  15.307  28.480  1.00 37.95 ? 170 HOH C O   1 
HETATM 4185 O O   . HOH G 2 .   ? 9.018   2.222   38.260  1.00 43.03 ? 171 HOH C O   1 
HETATM 4186 O O   . HOH G 2 .   ? 46.763  11.471  42.433  1.00 43.50 ? 172 HOH C O   1 
HETATM 4187 O O   . HOH G 2 .   ? 42.080  19.537  40.220  1.00 40.36 ? 173 HOH C O   1 
HETATM 4188 O O   . HOH G 2 .   ? 48.629  12.641  33.616  1.00 40.94 ? 174 HOH C O   1 
HETATM 4189 O O   . HOH G 2 .   ? 15.108  1.337   33.428  1.00 36.78 ? 175 HOH C O   1 
HETATM 4190 O O   . HOH G 2 .   ? 17.681  19.152  22.492  1.00 48.35 ? 176 HOH C O   1 
HETATM 4191 O O   . HOH G 2 .   ? 15.754  12.869  25.096  1.00 40.50 ? 177 HOH C O   1 
HETATM 4192 O O   . HOH G 2 .   ? 22.146  16.940  38.069  1.00 44.49 ? 178 HOH C O   1 
HETATM 4193 O O   . HOH G 2 .   ? 17.026  10.707  23.509  1.00 39.26 ? 179 HOH C O   1 
HETATM 4194 O O   . HOH G 2 .   ? 45.700  7.906   25.460  1.00 43.82 ? 180 HOH C O   1 
HETATM 4195 O O   . HOH G 2 .   ? 14.587  13.338  39.181  1.00 46.95 ? 181 HOH C O   1 
HETATM 4196 O O   . HOH G 2 .   ? 29.205  13.184  41.649  1.00 45.64 ? 182 HOH C O   1 
HETATM 4197 O O   . HOH G 2 .   ? 27.385  -0.230  28.935  1.00 39.24 ? 183 HOH C O   1 
HETATM 4198 O O   . HOH G 2 .   ? 35.228  1.091   31.131  1.00 46.62 ? 184 HOH C O   1 
HETATM 4199 O O   . HOH G 2 .   ? 10.965  0.515   35.511  1.00 37.66 ? 185 HOH C O   1 
HETATM 4200 O O   . HOH G 2 .   ? 30.395  8.683   19.585  1.00 38.42 ? 186 HOH C O   1 
HETATM 4201 O O   . HOH G 2 .   ? 20.565  1.710   38.405  1.00 38.98 ? 187 HOH C O   1 
HETATM 4202 O O   . HOH G 2 .   ? 43.731  16.670  30.408  1.00 41.82 ? 188 HOH C O   1 
HETATM 4203 O O   . HOH G 2 .   ? 36.685  16.667  20.065  1.00 46.06 ? 189 HOH C O   1 
HETATM 4204 O O   . HOH G 2 .   ? 21.546  12.528  41.723  1.00 42.56 ? 190 HOH C O   1 
HETATM 4205 O O   . HOH G 2 .   ? 16.059  14.313  33.282  1.00 40.14 ? 191 HOH C O   1 
HETATM 4206 O O   . HOH G 2 .   ? 38.309  5.621   23.010  1.00 53.02 ? 192 HOH C O   1 
HETATM 4207 O O   . HOH G 2 .   ? 42.925  15.018  15.908  1.00 61.37 ? 193 HOH C O   1 
HETATM 4208 O O   . HOH G 2 .   ? 41.374  3.149   31.570  1.00 48.50 ? 194 HOH C O   1 
HETATM 4209 O O   . HOH G 2 .   ? 43.670  19.319  31.246  1.00 49.10 ? 195 HOH C O   1 
HETATM 4210 O O   . HOH G 2 .   ? 49.511  14.705  35.017  1.00 43.60 ? 196 HOH C O   1 
HETATM 4211 O O   . HOH G 2 .   ? 16.968  19.928  24.996  1.00 49.86 ? 197 HOH C O   1 
HETATM 4212 O O   . HOH G 2 .   ? 15.633  17.054  21.759  1.00 50.97 ? 198 HOH C O   1 
HETATM 4213 O O   . HOH G 2 .   ? 27.021  25.076  28.832  1.00 47.89 ? 199 HOH C O   1 
HETATM 4214 O O   . HOH G 2 .   ? 39.159  8.093   39.857  1.00 45.12 ? 200 HOH C O   1 
HETATM 4215 O O   . HOH G 2 .   ? 11.999  6.440   26.605  1.00 50.14 ? 201 HOH C O   1 
HETATM 4216 O O   . HOH G 2 .   ? 9.355   9.610   25.425  1.00 46.41 ? 202 HOH C O   1 
HETATM 4217 O O   . HOH G 2 .   ? 37.519  23.234  31.121  1.00 47.91 ? 203 HOH C O   1 
HETATM 4218 O O   . HOH H 2 .   ? 23.829  3.287   -7.965  1.00 32.71 ? 154 HOH D O   1 
HETATM 4219 O O   . HOH H 2 .   ? 27.967  10.283  15.373  1.00 26.90 ? 155 HOH D O   1 
HETATM 4220 O O   . HOH H 2 .   ? 8.391   13.823  8.356   1.00 37.69 ? 156 HOH D O   1 
HETATM 4221 O O   . HOH H 2 .   ? 32.582  5.920   15.104  1.00 36.70 ? 157 HOH D O   1 
HETATM 4222 O O   . HOH H 2 .   ? 29.095  3.661   21.952  1.00 26.36 ? 158 HOH D O   1 
HETATM 4223 O O   . HOH H 2 .   ? 17.461  -2.702  21.587  1.00 45.58 ? 159 HOH D O   1 
HETATM 4224 O O   . HOH H 2 .   ? 26.067  -3.429  23.632  1.00 37.50 ? 160 HOH D O   1 
HETATM 4225 O O   . HOH H 2 .   ? 29.613  8.062   17.058  1.00 41.20 ? 161 HOH D O   1 
HETATM 4226 O O   . HOH H 2 .   ? 37.302  8.947   -1.615  1.00 36.64 ? 162 HOH D O   1 
HETATM 4227 O O   . HOH H 2 .   ? 13.073  -0.546  5.098   1.00 45.62 ? 163 HOH D O   1 
HETATM 4228 O O   . HOH H 2 .   ? 22.077  -8.427  11.035  1.00 46.00 ? 164 HOH D O   1 
HETATM 4229 O O   . HOH H 2 .   ? 32.278  7.469   -11.198 1.00 48.50 ? 165 HOH D O   1 
HETATM 4230 O O   . HOH H 2 .   ? 28.295  -2.147  -7.386  1.00 35.28 ? 166 HOH D O   1 
HETATM 4231 O O   . HOH H 2 .   ? 19.461  3.243   -0.597  1.00 41.77 ? 167 HOH D O   1 
HETATM 4232 O O   . HOH H 2 .   ? 24.857  7.234   -2.388  1.00 35.54 ? 168 HOH D O   1 
HETATM 4233 O O   . HOH H 2 .   ? 37.169  2.178   6.971   1.00 42.26 ? 169 HOH D O   1 
HETATM 4234 O O   . HOH H 2 .   ? 10.517  3.720   2.499   1.00 45.68 ? 170 HOH D O   1 
HETATM 4235 O O   . HOH H 2 .   ? 7.230   7.411   14.712  1.00 42.21 ? 171 HOH D O   1 
HETATM 4236 O O   . HOH H 2 .   ? 28.614  -7.811  9.412   1.00 51.17 ? 172 HOH D O   1 
HETATM 4237 O O   . HOH H 2 .   ? 34.813  0.724   0.279   1.00 46.47 ? 173 HOH D O   1 
HETATM 4238 O O   . HOH H 2 .   ? 17.122  -5.322  16.456  1.00 42.30 ? 174 HOH D O   1 
HETATM 4239 O O   . HOH H 2 .   ? 16.479  17.700  16.797  1.00 41.46 ? 175 HOH D O   1 
HETATM 4240 O O   . HOH H 2 .   ? 33.432  -6.096  9.982   1.00 52.68 ? 176 HOH D O   1 
HETATM 4241 O O   . HOH H 2 .   ? 25.704  -9.353  12.345  1.00 43.73 ? 177 HOH D O   1 
HETATM 4242 O O   . HOH H 2 .   ? 14.386  3.337   19.814  1.00 51.01 ? 178 HOH D O   1 
HETATM 4243 O O   . HOH H 2 .   ? 17.010  -7.518  21.652  1.00 56.97 ? 179 HOH D O   1 
HETATM 4244 O O   . HOH H 2 .   ? 12.235  6.162   21.377  1.00 46.29 ? 180 HOH D O   1 
HETATM 4245 O O   . HOH H 2 .   ? 10.302  9.244   21.306  1.00 57.78 ? 181 HOH D O   1 
HETATM 4246 O O   . HOH H 2 .   ? 15.963  5.606   20.414  1.00 37.49 ? 182 HOH D O   1 
HETATM 4247 O O   . HOH H 2 .   ? 26.061  17.941  9.865   1.00 40.96 ? 183 HOH D O   1 
HETATM 4248 O O   . HOH H 2 .   ? 33.145  3.184   14.452  1.00 46.14 ? 184 HOH D O   1 
HETATM 4249 O O   . HOH H 2 .   ? 29.069  1.702   16.853  1.00 53.05 ? 185 HOH D O   1 
HETATM 4250 O O   . HOH H 2 .   ? 31.912  -6.375  12.349  1.00 48.23 ? 186 HOH D O   1 
HETATM 4251 O O   . HOH H 2 .   ? 26.742  -5.622  21.137  1.00 44.51 ? 187 HOH D O   1 
HETATM 4252 O O   . HOH H 2 .   ? 6.563   1.689   4.042   1.00 47.45 ? 188 HOH D O   1 
HETATM 4253 O O   . HOH H 2 .   ? 10.189  6.027   0.765   1.00 59.62 ? 189 HOH D O   1 
HETATM 4254 O O   . HOH H 2 .   ? 8.377   7.453   10.779  1.00 44.89 ? 190 HOH D O   1 
HETATM 4255 O O   . HOH H 2 .   ? 12.571  -8.165  8.250   1.00 53.36 ? 191 HOH D O   1 
HETATM 4256 O O   . HOH H 2 .   ? 29.693  -6.469  3.310   1.00 43.51 ? 192 HOH D O   1 
HETATM 4257 O O   . HOH H 2 .   ? 22.147  16.696  10.810  1.00 36.08 ? 193 HOH D O   1 
HETATM 4258 O O   . HOH H 2 .   ? 37.322  1.537   1.101   1.00 53.91 ? 194 HOH D O   1 
HETATM 4259 O O   . HOH H 2 .   ? 38.407  4.691   -3.927  1.00 50.25 ? 195 HOH D O   1 
HETATM 4260 O O   . HOH H 2 .   ? 29.007  -2.277  26.113  1.00 50.31 ? 196 HOH D O   1 
HETATM 4261 O O   . HOH H 2 .   ? 34.829  0.412   13.150  1.00 48.83 ? 197 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   ALA 6   6   6   ALA ALA 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  ALA 57  57  57  ALA ALA 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 ALA 111 111 111 ALA ALA 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 ALA 146 146 146 ALA ALA 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   ALA 6   6   6   ALA ALA 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  ALA 57  57  57  ALA ALA 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 ALA 111 111 111 ALA ALA 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 ALA 146 146 146 ALA ALA 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   ALA 6   6   6   ALA ALA 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  ALA 57  57  57  ALA ALA 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  ?   ?   ?   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 ALA 111 111 111 ALA ALA 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 ?   ?   ?   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 ALA 146 146 146 ALA ALA 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   ?   ?   ?   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   ALA 6   6   6   ALA ALA 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  ALA 57  57  57  ALA ALA 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  79  ARG ARG D . n 
D 1 80  HIS 80  80  80  HIS HIS D . n 
D 1 81  VAL 81  81  81  VAL VAL D . n 
D 1 82  GLY 82  82  82  GLY GLY D . n 
D 1 83  ASP 83  83  83  ASP ASP D . n 
D 1 84  LEU 84  84  84  LEU LEU D . n 
D 1 85  GLY 85  85  85  GLY GLY D . n 
D 1 86  ASN 86  86  86  ASN ASN D . n 
D 1 87  VAL 87  87  87  VAL VAL D . n 
D 1 88  THR 88  88  88  THR THR D . n 
D 1 89  ALA 89  89  89  ALA ALA D . n 
D 1 90  ASP 90  90  90  ASP ASP D . n 
D 1 91  LYS 91  91  91  LYS LYS D . n 
D 1 92  ASP 92  92  92  ASP ASP D . n 
D 1 93  GLY 93  93  93  GLY GLY D . n 
D 1 94  VAL 94  94  94  VAL VAL D . n 
D 1 95  ALA 95  95  95  ALA ALA D . n 
D 1 96  ASP 96  96  96  ASP ASP D . n 
D 1 97  VAL 97  97  97  VAL VAL D . n 
D 1 98  SER 98  98  98  SER SER D . n 
D 1 99  ILE 99  99  99  ILE ILE D . n 
D 1 100 GLU 100 100 100 GLU GLU D . n 
D 1 101 ASP 101 101 101 ASP ASP D . n 
D 1 102 SER 102 102 102 SER SER D . n 
D 1 103 VAL 103 103 103 VAL VAL D . n 
D 1 104 ILE 104 104 104 ILE ILE D . n 
D 1 105 SER 105 105 105 SER SER D . n 
D 1 106 LEU 106 106 106 LEU LEU D . n 
D 1 107 SER 107 107 107 SER SER D . n 
D 1 108 GLY 108 108 108 GLY GLY D . n 
D 1 109 ASP 109 109 109 ASP ASP D . n 
D 1 110 HIS 110 110 110 HIS HIS D . n 
D 1 111 ALA 111 111 111 ALA ALA 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 ALA 146 146 146 ALA ALA 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_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 11  HOH HOH A . 
E 2 HOH 2  155 12  HOH HOH A . 
E 2 HOH 3  156 15  HOH HOH A . 
E 2 HOH 4  157 16  HOH HOH A . 
E 2 HOH 5  158 19  HOH HOH A . 
E 2 HOH 6  159 23  HOH HOH A . 
E 2 HOH 7  160 26  HOH HOH A . 
E 2 HOH 8  161 29  HOH HOH A . 
E 2 HOH 9  162 32  HOH HOH A . 
E 2 HOH 10 163 33  HOH HOH A . 
E 2 HOH 11 164 42  HOH HOH A . 
E 2 HOH 12 165 44  HOH HOH A . 
E 2 HOH 13 166 48  HOH HOH A . 
E 2 HOH 14 167 53  HOH HOH A . 
E 2 HOH 15 168 54  HOH HOH A . 
E 2 HOH 16 169 65  HOH HOH A . 
E 2 HOH 17 170 67  HOH HOH A . 
E 2 HOH 18 171 68  HOH HOH A . 
E 2 HOH 19 172 69  HOH HOH A . 
E 2 HOH 20 173 74  HOH HOH A . 
E 2 HOH 21 174 78  HOH HOH A . 
E 2 HOH 22 175 79  HOH HOH A . 
E 2 HOH 23 176 80  HOH HOH A . 
E 2 HOH 24 177 82  HOH HOH A . 
E 2 HOH 25 178 83  HOH HOH A . 
E 2 HOH 26 179 86  HOH HOH A . 
E 2 HOH 27 180 92  HOH HOH A . 
E 2 HOH 28 181 96  HOH HOH A . 
E 2 HOH 29 182 106 HOH HOH A . 
E 2 HOH 30 183 113 HOH HOH A . 
E 2 HOH 31 184 115 HOH HOH A . 
E 2 HOH 32 185 118 HOH HOH A . 
E 2 HOH 33 186 119 HOH HOH A . 
E 2 HOH 34 187 122 HOH HOH A . 
E 2 HOH 35 188 123 HOH HOH A . 
E 2 HOH 36 189 137 HOH HOH A . 
E 2 HOH 37 190 138 HOH HOH A . 
E 2 HOH 38 191 139 HOH HOH A . 
E 2 HOH 39 192 140 HOH HOH A . 
E 2 HOH 40 193 141 HOH HOH A . 
E 2 HOH 41 194 142 HOH HOH A . 
E 2 HOH 42 195 143 HOH HOH A . 
E 2 HOH 43 196 144 HOH HOH A . 
E 2 HOH 44 197 145 HOH HOH A . 
E 2 HOH 45 198 146 HOH HOH A . 
E 2 HOH 46 199 147 HOH HOH A . 
E 2 HOH 47 200 148 HOH HOH A . 
E 2 HOH 48 201 149 HOH HOH A . 
E 2 HOH 49 202 150 HOH HOH A . 
E 2 HOH 50 203 151 HOH HOH A . 
E 2 HOH 51 204 152 HOH HOH A . 
E 2 HOH 52 205 153 HOH HOH A . 
E 2 HOH 53 206 154 HOH HOH A . 
E 2 HOH 54 207 155 HOH HOH A . 
E 2 HOH 55 208 156 HOH HOH A . 
E 2 HOH 56 209 157 HOH HOH A . 
E 2 HOH 57 210 158 HOH HOH A . 
E 2 HOH 58 211 159 HOH HOH A . 
E 2 HOH 59 212 160 HOH HOH A . 
E 2 HOH 60 213 161 HOH HOH A . 
E 2 HOH 61 214 162 HOH HOH A . 
E 2 HOH 62 215 163 HOH HOH A . 
E 2 HOH 63 216 165 HOH HOH A . 
E 2 HOH 64 217 166 HOH HOH A . 
E 2 HOH 65 218 167 HOH HOH A . 
E 2 HOH 66 219 168 HOH HOH A . 
E 2 HOH 67 220 169 HOH HOH A . 
E 2 HOH 68 221 172 HOH HOH A . 
E 2 HOH 69 222 202 HOH HOH A . 
E 2 HOH 70 223 203 HOH HOH A . 
E 2 HOH 71 224 204 HOH HOH A . 
E 2 HOH 72 225 205 HOH HOH A . 
E 2 HOH 73 226 206 HOH HOH A . 
E 2 HOH 74 227 207 HOH HOH A . 
E 2 HOH 75 228 208 HOH HOH A . 
E 2 HOH 76 229 209 HOH HOH A . 
E 2 HOH 77 230 210 HOH HOH A . 
E 2 HOH 78 231 211 HOH HOH A . 
E 2 HOH 79 232 212 HOH HOH A . 
E 2 HOH 80 233 213 HOH HOH A . 
E 2 HOH 81 234 214 HOH HOH A . 
E 2 HOH 82 235 215 HOH HOH A . 
E 2 HOH 83 236 216 HOH HOH A . 
E 2 HOH 84 237 217 HOH HOH A . 
E 2 HOH 85 238 241 HOH HOH A . 
F 2 HOH 1  154 1   HOH HOH B . 
F 2 HOH 2  155 3   HOH HOH B . 
F 2 HOH 3  156 4   HOH HOH B . 
F 2 HOH 4  157 9   HOH HOH B . 
F 2 HOH 5  158 13  HOH HOH B . 
F 2 HOH 6  159 17  HOH HOH B . 
F 2 HOH 7  160 25  HOH HOH B . 
F 2 HOH 8  161 28  HOH HOH B . 
F 2 HOH 9  162 38  HOH HOH B . 
F 2 HOH 10 163 41  HOH HOH B . 
F 2 HOH 11 164 45  HOH HOH B . 
F 2 HOH 12 165 46  HOH HOH B . 
F 2 HOH 13 166 51  HOH HOH B . 
F 2 HOH 14 167 52  HOH HOH B . 
F 2 HOH 15 168 60  HOH HOH B . 
F 2 HOH 16 169 61  HOH HOH B . 
F 2 HOH 17 170 62  HOH HOH B . 
F 2 HOH 18 171 63  HOH HOH B . 
F 2 HOH 19 172 64  HOH HOH B . 
F 2 HOH 20 173 70  HOH HOH B . 
F 2 HOH 21 174 71  HOH HOH B . 
F 2 HOH 22 175 72  HOH HOH B . 
F 2 HOH 23 176 76  HOH HOH B . 
F 2 HOH 24 177 77  HOH HOH B . 
F 2 HOH 25 178 84  HOH HOH B . 
F 2 HOH 26 179 90  HOH HOH B . 
F 2 HOH 27 180 94  HOH HOH B . 
F 2 HOH 28 181 99  HOH HOH B . 
F 2 HOH 29 182 100 HOH HOH B . 
F 2 HOH 30 183 104 HOH HOH B . 
F 2 HOH 31 184 105 HOH HOH B . 
F 2 HOH 32 185 108 HOH HOH B . 
F 2 HOH 33 186 109 HOH HOH B . 
F 2 HOH 34 187 112 HOH HOH B . 
F 2 HOH 35 188 120 HOH HOH B . 
F 2 HOH 36 189 121 HOH HOH B . 
F 2 HOH 37 190 125 HOH HOH B . 
F 2 HOH 38 191 129 HOH HOH B . 
F 2 HOH 39 192 130 HOH HOH B . 
F 2 HOH 40 193 131 HOH HOH B . 
F 2 HOH 41 194 132 HOH HOH B . 
F 2 HOH 42 195 133 HOH HOH B . 
F 2 HOH 43 196 173 HOH HOH B . 
F 2 HOH 44 197 174 HOH HOH B . 
F 2 HOH 45 198 175 HOH HOH B . 
F 2 HOH 46 199 176 HOH HOH B . 
F 2 HOH 47 200 177 HOH HOH B . 
F 2 HOH 48 201 178 HOH HOH B . 
F 2 HOH 49 202 179 HOH HOH B . 
F 2 HOH 50 203 180 HOH HOH B . 
F 2 HOH 51 204 181 HOH HOH B . 
F 2 HOH 52 205 182 HOH HOH B . 
F 2 HOH 53 206 183 HOH HOH B . 
F 2 HOH 54 207 184 HOH HOH B . 
F 2 HOH 55 208 185 HOH HOH B . 
F 2 HOH 56 209 186 HOH HOH B . 
F 2 HOH 57 210 187 HOH HOH B . 
F 2 HOH 58 211 188 HOH HOH B . 
F 2 HOH 59 212 218 HOH HOH B . 
F 2 HOH 60 213 219 HOH HOH B . 
F 2 HOH 61 214 220 HOH HOH B . 
F 2 HOH 62 215 221 HOH HOH B . 
F 2 HOH 63 216 222 HOH HOH B . 
F 2 HOH 64 217 223 HOH HOH B . 
F 2 HOH 65 218 224 HOH HOH B . 
F 2 HOH 66 219 225 HOH HOH B . 
F 2 HOH 67 220 226 HOH HOH B . 
F 2 HOH 68 221 227 HOH HOH B . 
F 2 HOH 69 222 228 HOH HOH B . 
F 2 HOH 70 223 229 HOH HOH B . 
F 2 HOH 71 224 230 HOH HOH B . 
F 2 HOH 72 225 232 HOH HOH B . 
F 2 HOH 73 226 233 HOH HOH B . 
F 2 HOH 74 227 234 HOH HOH B . 
F 2 HOH 75 228 235 HOH HOH B . 
F 2 HOH 76 229 236 HOH HOH B . 
F 2 HOH 77 230 237 HOH HOH B . 
F 2 HOH 78 231 238 HOH HOH B . 
F 2 HOH 79 232 239 HOH HOH B . 
F 2 HOH 80 233 240 HOH HOH B . 
G 2 HOH 1  154 2   HOH HOH C . 
G 2 HOH 2  155 6   HOH HOH C . 
G 2 HOH 3  156 7   HOH HOH C . 
G 2 HOH 4  157 8   HOH HOH C . 
G 2 HOH 5  158 10  HOH HOH C . 
G 2 HOH 6  159 22  HOH HOH C . 
G 2 HOH 7  160 24  HOH HOH C . 
G 2 HOH 8  161 30  HOH HOH C . 
G 2 HOH 9  162 31  HOH HOH C . 
G 2 HOH 10 163 35  HOH HOH C . 
G 2 HOH 11 164 36  HOH HOH C . 
G 2 HOH 12 165 37  HOH HOH C . 
G 2 HOH 13 166 50  HOH HOH C . 
G 2 HOH 14 167 57  HOH HOH C . 
G 2 HOH 15 168 66  HOH HOH C . 
G 2 HOH 16 169 73  HOH HOH C . 
G 2 HOH 17 170 81  HOH HOH C . 
G 2 HOH 18 171 87  HOH HOH C . 
G 2 HOH 19 172 88  HOH HOH C . 
G 2 HOH 20 173 89  HOH HOH C . 
G 2 HOH 21 174 98  HOH HOH C . 
G 2 HOH 22 175 101 HOH HOH C . 
G 2 HOH 23 176 102 HOH HOH C . 
G 2 HOH 24 177 107 HOH HOH C . 
G 2 HOH 25 178 110 HOH HOH C . 
G 2 HOH 26 179 111 HOH HOH C . 
G 2 HOH 27 180 117 HOH HOH C . 
G 2 HOH 28 181 124 HOH HOH C . 
G 2 HOH 29 182 126 HOH HOH C . 
G 2 HOH 30 183 134 HOH HOH C . 
G 2 HOH 31 184 135 HOH HOH C . 
G 2 HOH 32 185 136 HOH HOH C . 
G 2 HOH 33 186 170 HOH HOH C . 
G 2 HOH 34 187 189 HOH HOH C . 
G 2 HOH 35 188 190 HOH HOH C . 
G 2 HOH 36 189 191 HOH HOH C . 
G 2 HOH 37 190 192 HOH HOH C . 
G 2 HOH 38 191 193 HOH HOH C . 
G 2 HOH 39 192 242 HOH HOH C . 
G 2 HOH 40 193 243 HOH HOH C . 
G 2 HOH 41 194 244 HOH HOH C . 
G 2 HOH 42 195 245 HOH HOH C . 
G 2 HOH 43 196 246 HOH HOH C . 
G 2 HOH 44 197 247 HOH HOH C . 
G 2 HOH 45 198 248 HOH HOH C . 
G 2 HOH 46 199 250 HOH HOH C . 
G 2 HOH 47 200 251 HOH HOH C . 
G 2 HOH 48 201 252 HOH HOH C . 
G 2 HOH 49 202 253 HOH HOH C . 
G 2 HOH 50 203 254 HOH HOH C . 
H 2 HOH 1  154 5   HOH HOH D . 
H 2 HOH 2  155 14  HOH HOH D . 
H 2 HOH 3  156 18  HOH HOH D . 
H 2 HOH 4  157 20  HOH HOH D . 
H 2 HOH 5  158 21  HOH HOH D . 
H 2 HOH 6  159 27  HOH HOH D . 
H 2 HOH 7  160 34  HOH HOH D . 
H 2 HOH 8  161 39  HOH HOH D . 
H 2 HOH 9  162 40  HOH HOH D . 
H 2 HOH 10 163 43  HOH HOH D . 
H 2 HOH 11 164 47  HOH HOH D . 
H 2 HOH 12 165 49  HOH HOH D . 
H 2 HOH 13 166 55  HOH HOH D . 
H 2 HOH 14 167 56  HOH HOH D . 
H 2 HOH 15 168 58  HOH HOH D . 
H 2 HOH 16 169 59  HOH HOH D . 
H 2 HOH 17 170 75  HOH HOH D . 
H 2 HOH 18 171 85  HOH HOH D . 
H 2 HOH 19 172 91  HOH HOH D . 
H 2 HOH 20 173 93  HOH HOH D . 
H 2 HOH 21 174 95  HOH HOH D . 
H 2 HOH 22 175 97  HOH HOH D . 
H 2 HOH 23 176 103 HOH HOH D . 
H 2 HOH 24 177 114 HOH HOH D . 
H 2 HOH 25 178 116 HOH HOH D . 
H 2 HOH 26 179 127 HOH HOH D . 
H 2 HOH 27 180 128 HOH HOH D . 
H 2 HOH 28 181 164 HOH HOH D . 
H 2 HOH 29 182 171 HOH HOH D . 
H 2 HOH 30 183 194 HOH HOH D . 
H 2 HOH 31 184 195 HOH HOH D . 
H 2 HOH 32 185 196 HOH HOH D . 
H 2 HOH 33 186 197 HOH HOH D . 
H 2 HOH 34 187 198 HOH HOH D . 
H 2 HOH 35 188 199 HOH HOH D . 
H 2 HOH 36 189 200 HOH HOH D . 
H 2 HOH 37 190 201 HOH HOH D . 
H 2 HOH 38 191 231 HOH HOH D . 
H 2 HOH 39 192 249 HOH HOH D . 
H 2 HOH 40 193 255 HOH HOH D . 
H 2 HOH 41 194 256 HOH HOH D . 
H 2 HOH 42 195 257 HOH HOH D . 
H 2 HOH 43 196 258 HOH HOH D . 
H 2 HOH 44 197 259 HOH HOH D . 
# 
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)' 1740  ? 
1 MORE         -11   ? 
1 'SSA (A^2)'  14140 ? 
2 'ABSA (A^2)' 1420  ? 
2 MORE         -11   ? 
2 'SSA (A^2)'  11950 ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2007-01-02 
2 'Structure model' 1 1 2008-05-01 
3 'Structure model' 1 2 2011-07-13 
4 'Structure model' 1 3 2018-05-23 
5 'Structure model' 1 4 2021-11-10 
# 
_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_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' Advisory                    
3 3 'Structure model' 'Version format compliance' 
4 4 'Structure model' 'Data collection'           
5 5 'Structure model' 'Database references'       
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 4 'Structure model' diffrn_source      
2 5 'Structure model' database_2         
3 5 'Structure model' struct_ref_seq_dif 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 4 'Structure model' '_diffrn_source.pdbx_synchrotron_site' 
2 5 'Structure model' '_database_2.pdbx_DOI'                 
3 5 'Structure model' '_database_2.pdbx_database_accession'  
4 5 'Structure model' '_struct_ref_seq_dif.details'          
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.pdbx_refine_id 
1 ? refined -12.9308 -2.9374 20.9595 -0.0960 -0.1532 -0.0897 -0.0608 0.0136  -0.0265 2.8461 1.4835 4.8554 0.3183  1.2102  -0.2165 
0.0357 -0.0626 0.0268  0.0680  -0.1595 -0.0535 -0.0364 0.1502  -0.2909 'X-RAY DIFFRACTION' 
2 ? refined -3.8552  3.2768  46.0547 -0.1228 -0.1002 -0.0978 -0.0203 -0.0036 -0.0154 3.0144 0.8733 3.8579 -0.0563 -0.2020 -0.0266 
0.0533 0.0062  -0.0595 -0.2574 -0.0581 0.0227  0.0639  0.0877  -0.0706 'X-RAY DIFFRACTION' 
3 ? refined 29.3538  11.3719 30.2515 -0.1128 -0.1633 -0.0889 -0.0319 0.0047  -0.0111 5.2341 1.2707 4.6151 0.5718  -0.5285 0.3502  
0.0748 0.0483  -0.1232 -0.3906 0.2998  -0.0432 -0.0761 -0.2085 0.2498  'X-RAY DIFFRACTION' 
4 ? refined 23.0829  5.0498  8.3130  -0.0701 -0.2004 -0.0737 -0.0304 -0.0074 0.0201  3.3333 2.1571 7.0345 -0.5038 -0.0658 0.5773  
0.0315 -0.0340 0.0025  0.4811  -0.1582 0.0916  -0.0645 0.0302  -0.1055 'X-RAY DIFFRACTION' 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.selection_details 
1 1 A 1 A 153 ALL A 1 A 153 'X-RAY DIFFRACTION' ? 
2 2 B 1 B 153 ALL B 1 B 153 'X-RAY DIFFRACTION' ? 
3 3 C 1 C 153 ALL C 1 C 153 'X-RAY DIFFRACTION' ? 
4 4 D 2 D 153 ALL D 2 D 153 'X-RAY DIFFRACTION' ? 
# 
loop_
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
_software.pdbx_ordinal 
SCALA       .         ?              program 'Phil Evans'      pre@mrc-lmb.cam.ac.uk    'data scaling'    
http://www.ccp4.ac.uk/dist/html/INDEX.html Fortran ? 1 
REFMAC      .         ?              program 'Murshudov, G.N.' ccp4@dl.ac.uk            refinement        
http://www.ccp4.ac.uk/main.html            Fortran ? 2 
PDB_EXTRACT 1.701     'Nov. 1, 2005' package PDB               sw-help@rcsb.rutgers.edu 'data extraction' 
http://pdb.rutgers.edu/software/           C++     ? 3 
MOSFLM      .         ?              ?       ?                 ?                        'data reduction'  ? ?       ? 4 
CCP4        '(SCALA)' ?              ?       ?                 ?                        'data scaling'    ? ?       ? 5 
CNS         .         ?              ?       ?                 ?                        phasing           ? ?       ? 6 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASP A 11 ? ? -86.55  38.76   
2 1 SER A 98 ? ? -152.12 86.87   
3 1 SER B 98 ? ? -151.12 87.53   
4 1 ASN C 65 ? ? -155.11 77.56   
5 1 PRO C 66 ? ? -70.53  -166.35 
6 1 ASN D 65 ? ? -151.43 67.85   
# 
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 ARG 79  ? C ARG 79  
13 1 Y 1 C ASP 125 ? C ASP 125 
14 1 Y 1 C LEU 126 ? C LEU 126 
15 1 Y 1 C GLY 127 ? C GLY 127 
16 1 Y 1 C LYS 128 ? C LYS 128 
17 1 Y 1 C GLY 129 ? C GLY 129 
18 1 Y 1 C GLY 130 ? C GLY 130 
19 1 Y 1 C ASN 131 ? C ASN 131 
20 1 Y 1 C GLU 132 ? C GLU 132 
21 1 Y 1 C GLU 133 ? C GLU 133 
22 1 Y 1 C SER 134 ? C SER 134 
23 1 Y 1 C THR 135 ? C THR 135 
24 1 Y 1 C LYS 136 ? C LYS 136 
25 1 Y 1 C THR 137 ? C THR 137 
26 1 Y 1 C GLY 138 ? C GLY 138 
27 1 Y 1 C ASN 139 ? C ASN 139 
28 1 Y 1 C ALA 140 ? C ALA 140 
29 1 Y 1 C GLY 141 ? C GLY 141 
30 1 Y 1 D ALA 1   ? D ALA 1   
31 1 Y 1 D LEU 67  ? D LEU 67  
32 1 Y 1 D SER 68  ? D SER 68  
33 1 Y 1 D ARG 69  ? D ARG 69  
34 1 Y 1 D LYS 70  ? D LYS 70  
35 1 Y 1 D HIS 71  ? D HIS 71  
36 1 Y 1 D GLY 72  ? D GLY 72  
37 1 Y 1 D GLY 73  ? D GLY 73  
38 1 Y 1 D PRO 74  ? D PRO 74  
39 1 Y 1 D LYS 75  ? D LYS 75  
40 1 Y 1 D ASP 76  ? D ASP 76  
41 1 Y 1 D GLU 77  ? D GLU 77  
42 1 Y 1 D GLU 78  ? D GLU 78  
43 1 Y 1 D ASP 125 ? D ASP 125 
44 1 Y 1 D LEU 126 ? D LEU 126 
45 1 Y 1 D GLY 127 ? D GLY 127 
46 1 Y 1 D LYS 128 ? D LYS 128 
47 1 Y 1 D GLY 129 ? D GLY 129 
48 1 Y 1 D GLY 130 ? D GLY 130 
49 1 Y 1 D ASN 131 ? D ASN 131 
50 1 Y 1 D GLU 132 ? D GLU 132 
51 1 Y 1 D GLU 133 ? D GLU 133 
52 1 Y 1 D SER 134 ? D SER 134 
53 1 Y 1 D THR 135 ? D THR 135 
54 1 Y 1 D LYS 136 ? D LYS 136 
55 1 Y 1 D THR 137 ? D THR 137 
56 1 Y 1 D GLY 138 ? D GLY 138 
57 1 Y 1 D ASN 139 ? D ASN 139 
58 1 Y 1 D ALA 140 ? D ALA 140 
59 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 
# 
