data_3ECW
# 
_entry.id   3ECW 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.350 
_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   3ECW         pdb_00003ecw 10.2210/pdb3ecw/pdb 
RCSB  RCSB049164   ?            ?                   
WWPDB D_1000049164 ?            ?                   
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 3ECU . unspecified 
PDB 3ECV . unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        3ECW 
_pdbx_database_status.recvd_initial_deposition_date   2008-09-02 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
# 
_audit_author.name           'Calderone, V.' 
_audit_author.pdbx_ordinal   1 
# 
loop_
_citation.id 
_citation.title 
_citation.journal_abbrev 
_citation.journal_volume 
_citation.page_first 
_citation.page_last 
_citation.year 
_citation.journal_id_ASTM 
_citation.country 
_citation.journal_id_ISSN 
_citation.journal_id_CSD 
_citation.book_publisher 
_citation.pdbx_database_id_PubMed 
_citation.pdbx_database_id_DOI 
primary 'Structural and dynamic aspects related to oligomerization of apo SOD1 and its mutants.' Proc.Natl.Acad.Sci.USA 106 6980  
6985  2009 PNASA6 US 0027-8424 0040 ? 19369197 10.1073/pnas.0809845106 
1       
;Metal-free superoxide dismutase forms soluble oligomers under physiological conditions: a possible general mechanism for familial ALS.
;
Proc.Natl.Acad.Sci.USA 104 11263 11267 2007 PNASA6 US 0027-8424 0040 ? ?        ?                       
2       'SOD1 and amyotrophic lateral sclerosis: mutations and oligomerization.' 'PLoS ONE'             3   1677  ?     2008 ? US 
1932-6203 ?    ? ?        ?                       
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Banci, L.'        1  ? 
primary 'Bertini, I.'      2  ? 
primary 'Boca, M.'         3  ? 
primary 'Calderone, V.'    4  ? 
primary 'Cantini, F.'      5  ? 
primary 'Girotto, S.'      6  ? 
primary 'Vieru, M.'        7  ? 
1       'Banci, L.'        8  ? 
1       'Bertini, I.'      9  ? 
1       'Durazo, A.'       10 ? 
1       'Girotto, S.'      11 ? 
1       'Gralla, E.B.'     12 ? 
1       'Martinelli, M.'   13 ? 
1       'Valentine, J.S.'  14 ? 
1       'Vieru, M.'        15 ? 
1       'Whitelegge, J.P.' 16 ? 
2       'Banci, L.'        17 ? 
2       'Bertini, I.'      18 ? 
2       'Boca, M.'         19 ? 
2       'Girotto, S.'      20 ? 
2       'Martinelli, M.'   21 ? 
2       'Valentine, J.S.'  22 ? 
2       'Vieru, M.'        23 ? 
# 
_cell.entry_id           3ECW 
_cell.length_a           156.940 
_cell.length_b           34.033 
_cell.length_c           114.585 
_cell.angle_alpha        90.00 
_cell.angle_beta         112.14 
_cell.angle_gamma        90.00 
_cell.Z_PDB              16 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         3ECW 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer man 'Superoxide dismutase [Cu-Zn]' 15883.650 4   1.15.1.1 ? ? ? 
2 water   nat water                          18.015    363 ?        ? ? ? 
# 
_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       
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNRAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNRAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   THR n 
1 3   LYS n 
1 4   ALA n 
1 5   VAL n 
1 6   CYS n 
1 7   VAL n 
1 8   LEU n 
1 9   LYS n 
1 10  GLY n 
1 11  ASP n 
1 12  GLY n 
1 13  PRO n 
1 14  VAL n 
1 15  GLN n 
1 16  GLY n 
1 17  ILE n 
1 18  ILE n 
1 19  ASN n 
1 20  PHE n 
1 21  GLU n 
1 22  GLN n 
1 23  LYS n 
1 24  GLU n 
1 25  SER n 
1 26  ASN n 
1 27  GLY n 
1 28  PRO n 
1 29  VAL n 
1 30  LYS n 
1 31  VAL n 
1 32  TRP n 
1 33  GLY n 
1 34  SER n 
1 35  ILE n 
1 36  LYS n 
1 37  GLY n 
1 38  LEU n 
1 39  THR n 
1 40  GLU n 
1 41  GLY n 
1 42  LEU n 
1 43  HIS n 
1 44  GLY n 
1 45  PHE n 
1 46  HIS n 
1 47  VAL n 
1 48  HIS n 
1 49  GLU n 
1 50  PHE n 
1 51  GLY n 
1 52  ASP n 
1 53  ASN n 
1 54  ARG n 
1 55  ALA n 
1 56  GLY n 
1 57  CYS n 
1 58  THR n 
1 59  SER n 
1 60  ALA n 
1 61  GLY n 
1 62  PRO n 
1 63  HIS n 
1 64  PHE n 
1 65  ASN n 
1 66  PRO n 
1 67  LEU n 
1 68  SER n 
1 69  ARG n 
1 70  LYS n 
1 71  HIS n 
1 72  GLY n 
1 73  GLY n 
1 74  PRO n 
1 75  LYS n 
1 76  ASP n 
1 77  GLU n 
1 78  GLU n 
1 79  ARG n 
1 80  HIS n 
1 81  VAL n 
1 82  GLY n 
1 83  ASP n 
1 84  LEU n 
1 85  GLY n 
1 86  ASN n 
1 87  VAL n 
1 88  THR n 
1 89  ALA n 
1 90  ASP n 
1 91  LYS n 
1 92  ASP n 
1 93  GLY n 
1 94  VAL n 
1 95  ALA n 
1 96  ASP n 
1 97  VAL n 
1 98  SER n 
1 99  ILE n 
1 100 GLU n 
1 101 ASP n 
1 102 SER n 
1 103 VAL n 
1 104 ILE n 
1 105 SER n 
1 106 LEU n 
1 107 SER n 
1 108 GLY n 
1 109 ASP n 
1 110 HIS n 
1 111 CYS n 
1 112 ILE n 
1 113 ILE n 
1 114 GLY n 
1 115 ARG n 
1 116 THR n 
1 117 LEU n 
1 118 VAL n 
1 119 VAL n 
1 120 HIS n 
1 121 GLU n 
1 122 LYS n 
1 123 ALA n 
1 124 ASP n 
1 125 ASP n 
1 126 LEU n 
1 127 GLY n 
1 128 LYS n 
1 129 GLY n 
1 130 GLY n 
1 131 ASN n 
1 132 GLU n 
1 133 GLU n 
1 134 SER n 
1 135 THR n 
1 136 LYS n 
1 137 THR n 
1 138 GLY n 
1 139 ASN n 
1 140 ALA n 
1 141 GLY n 
1 142 SER n 
1 143 ARG n 
1 144 LEU n 
1 145 ALA n 
1 146 CYS n 
1 147 GLY n 
1 148 VAL n 
1 149 ILE n 
1 150 GLY n 
1 151 ILE n 
1 152 ALA n 
1 153 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               Human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 SOD1 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'Origami pLysS' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pENTR/TEV/D-TOPO 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    SODC_HUMAN 
_struct_ref.pdbx_db_accession          P00441 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_struct_ref.pdbx_align_begin           2 
_struct_ref.pdbx_db_isoform            ? 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 3ECW A 1 ? 153 ? P00441 2 ? 154 ? 1 153 
2 1 3ECW B 1 ? 153 ? P00441 2 ? 154 ? 1 153 
3 1 3ECW C 1 ? 153 ? P00441 2 ? 154 ? 1 153 
4 1 3ECW D 1 ? 153 ? P00441 2 ? 154 ? 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 3ECW ARG A 54 ? UNP P00441 THR 55 'engineered mutation' 54 1 
2 3ECW ARG B 54 ? UNP P00441 THR 55 'engineered mutation' 54 2 
3 3ECW ARG C 54 ? UNP P00441 THR 55 'engineered mutation' 54 3 
4 3ECW ARG D 54 ? UNP P00441 THR 55 'engineered mutation' 54 4 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
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          3ECW 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.23 
_exptl_crystal.density_percent_sol   44.86 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.temp            289.1 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              7.0 
_exptl_crystal_grow.pdbx_details    
;0.1 M HEPES 
20% PEG 3350, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 289.1K
;
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'MAR CCD 165 mm' 
_diffrn_detector.pdbx_collection_date   2007-09-07 
_diffrn_detector.details                'Si 111' 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    'Si 111 CHANNEL' 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.99180 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'EMBL/DESY, HAMBURG BEAMLINE BW7A' 
_diffrn_source.pdbx_synchrotron_site       'EMBL/DESY, HAMBURG' 
_diffrn_source.pdbx_synchrotron_beamline   BW7A 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        0.99180 
# 
_reflns.entry_id                     3ECW 
_reflns.observed_criterion_sigma_I   0 
_reflns.observed_criterion_sigma_F   0 
_reflns.d_resolution_low             39.2 
_reflns.d_resolution_high            2.1 
_reflns.number_obs                   29951 
_reflns.number_all                   29951 
_reflns.percent_possible_obs         96.0 
_reflns.pdbx_Rmerge_I_obs            0.098 
_reflns.pdbx_Rsym_value              0.098 
_reflns.pdbx_netI_over_sigmaI        6.4 
_reflns.B_iso_Wilson_estimate        29.8 
_reflns.pdbx_redundancy              3.3 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
_reflns_shell.d_res_high             2.1 
_reflns_shell.d_res_low              2.3 
_reflns_shell.percent_possible_all   91.2 
_reflns_shell.Rmerge_I_obs           0.443 
_reflns_shell.pdbx_Rsym_value        0.443 
_reflns_shell.meanI_over_sigI_obs    1.9 
_reflns_shell.pdbx_redundancy        2.6 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      4106 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_diffrn_id         ? 
_reflns_shell.pdbx_ordinal           1 
# 
_refine.entry_id                                 3ECW 
_refine.ls_number_reflns_obs                     27233 
_refine.ls_number_reflns_all                     27233 
_refine.pdbx_ls_sigma_I                          0 
_refine.pdbx_ls_sigma_F                          0 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             39.19 
_refine.ls_d_res_high                            2.15 
_refine.ls_percent_reflns_obs                    100.00 
_refine.ls_R_factor_obs                          0.20907 
_refine.ls_R_factor_all                          0.20907 
_refine.ls_R_factor_R_work                       0.20030 
_refine.ls_R_factor_R_free                       0.29720 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 9.1 
_refine.ls_number_reflns_R_free                  2715 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.939 
_refine.correlation_coeff_Fo_to_Fc_free          0.881 
_refine.B_iso_mean                               26.250 
_refine.aniso_B[1][1]                            -1.69 
_refine.aniso_B[2][2]                            2.28 
_refine.aniso_B[3][3]                            -2.54 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -2.58 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.40 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.pdbx_starting_model                      1HL5 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             Isotropic 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.301 
_refine.pdbx_overall_ESU_R_Free                  0.265 
_refine.overall_SU_ML                            0.178 
_refine.overall_SU_B                             6.750 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        4028 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.number_atoms_solvent             363 
_refine_hist.number_atoms_total               4391 
_refine_hist.d_res_high                       2.15 
_refine_hist.d_res_low                        39.19 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.025  0.021  ? 4096 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          2.248  1.942  ? 5529 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       8.506  5.000  ? 545  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       41.603 25.287 ? 174  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       19.858 15.000 ? 664  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       16.616 15.000 ? 16   'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.158  0.200  ? 616  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.009  0.020  ? 3112 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_refined                0.223  0.200  ? 1810 'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              0.306  0.200  ? 2568 'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        0.228  0.200  ? 342  'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       0.203  0.200  ? 35   'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     0.272  0.200  ? 6    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  1.306  1.500  ? 2785 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 2.128  2.000  ? 4282 'X-RAY DIFFRACTION' ? 
r_scbond_it                  3.372  3.000  ? 1462 'X-RAY DIFFRACTION' ? 
r_scangle_it                 4.896  4.500  ? 1247 'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       2.150 
_refine_ls_shell.d_res_low                        2.206 
_refine_ls_shell.number_reflns_R_work             1869 
_refine_ls_shell.R_factor_R_work                  0.237 
_refine_ls_shell.percent_reflns_obs               100.00 
_refine_ls_shell.R_factor_R_free                  0.323 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             158 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  3ECW 
_struct.title                     
'Crystal structure of the ALS-related pathological mutant T54R of human apo Cu,Zn Superoxide Dismutase (SOD1)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3ECW 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
_struct_keywords.text            
;HUMAN SUPEROXIDE DISMUTASE, HOMODIMERIC PROTEIN, APO PROTEIN, AGGREGATION, ALS, MUTANT, Acetylation, Amyotrophic lateral sclerosis, Antioxidant, Copper, Cytoplasm, Disease mutation, Metal-binding, Oxidoreductase, Ubl conjugation, Zinc
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 1 ? 
E N N 2 ? 
F N N 2 ? 
G N N 2 ? 
H N N 2 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 1 GLY A 56  ? GLY A 61  ? GLY A 56  GLY A 61  5 ? 6 
HELX_P HELX_P2 2 ASN A 131 ? THR A 135 ? ASN A 131 THR A 135 5 ? 5 
HELX_P HELX_P3 3 GLY B 56  ? GLY B 61  ? GLY B 56  GLY B 61  5 ? 6 
HELX_P HELX_P4 4 GLU B 132 ? LYS B 136 ? GLU B 132 LYS B 136 5 ? 5 
HELX_P HELX_P5 5 ALA C 55  ? GLY C 61  ? ALA C 55  GLY C 61  5 ? 7 
HELX_P HELX_P6 6 GLY D 56  ? GLY D 61  ? GLY D 56  GLY D 61  5 ? 6 
HELX_P HELX_P7 7 SER D 107 ? CYS D 111 ? SER D 107 CYS D 111 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ? ? A CYS 57 SG ? ? ? 1_555 A CYS 146 SG ? ? A CYS 57 A CYS 146 1_555 ? ? ? ? ? ? ? 2.087 ? ? 
disulf2 disulf ? ? B CYS 57 SG ? ? ? 1_555 B CYS 146 SG ? ? B CYS 57 B CYS 146 1_555 ? ? ? ? ? ? ? 2.108 ? ? 
disulf3 disulf ? ? C CYS 57 SG ? ? ? 1_555 C CYS 146 SG ? ? C CYS 57 C CYS 146 1_555 ? ? ? ? ? ? ? 2.135 ? ? 
disulf4 disulf ? ? D CYS 57 SG ? ? ? 1_555 D CYS 146 SG ? ? D CYS 57 D CYS 146 1_555 ? ? ? ? ? ? ? 2.159 ? ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 5 ? 
B ? 4 ? 
C ? 5 ? 
D ? 4 ? 
E ? 5 ? 
F ? 4 ? 
G ? 5 ? 
H ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2 ? anti-parallel 
A 2 3 ? anti-parallel 
A 3 4 ? anti-parallel 
A 4 5 ? anti-parallel 
B 1 2 ? anti-parallel 
B 2 3 ? anti-parallel 
B 3 4 ? anti-parallel 
C 1 2 ? anti-parallel 
C 2 3 ? anti-parallel 
C 3 4 ? anti-parallel 
C 4 5 ? anti-parallel 
D 1 2 ? anti-parallel 
D 2 3 ? anti-parallel 
D 3 4 ? anti-parallel 
E 1 2 ? anti-parallel 
E 2 3 ? anti-parallel 
E 3 4 ? anti-parallel 
E 4 5 ? anti-parallel 
F 1 2 ? anti-parallel 
F 2 3 ? anti-parallel 
F 3 4 ? anti-parallel 
G 1 2 ? anti-parallel 
G 2 3 ? anti-parallel 
G 3 4 ? anti-parallel 
G 4 5 ? anti-parallel 
H 1 2 ? anti-parallel 
H 2 3 ? anti-parallel 
H 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1 ALA A 95  ? ASP A 101 ? ALA A 95  ASP A 101 
A 2 VAL A 29  ? LYS A 36  ? VAL A 29  LYS A 36  
A 3 GLN A 15  ? GLN A 22  ? GLN A 15  GLN A 22  
A 4 THR A 2   ? LEU A 8   ? THR A 2   LEU A 8   
A 5 GLY A 150 ? ILE A 151 ? GLY A 150 ILE A 151 
B 1 ASP A 83  ? ALA A 89  ? ASP A 83  ALA A 89  
B 2 GLY A 41  ? HIS A 48  ? GLY A 41  HIS A 48  
B 3 THR A 116 ? HIS A 120 ? THR A 116 HIS A 120 
B 4 ARG A 143 ? VAL A 148 ? ARG A 143 VAL A 148 
C 1 ALA B 95  ? ASP B 101 ? ALA B 95  ASP B 101 
C 2 VAL B 29  ? LYS B 36  ? VAL B 29  LYS B 36  
C 3 GLN B 15  ? GLN B 22  ? GLN B 15  GLN B 22  
C 4 THR B 2   ? LYS B 9   ? THR B 2   LYS B 9   
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  ? GLN D 22  ? GLN D 15  GLN D 22  
G 4 THR D 2   ? LEU D 8   ? THR D 2   LEU D 8   
G 5 GLY D 150 ? ILE D 151 ? GLY D 150 ILE D 151 
H 1 ASP D 83  ? ALA D 89  ? ASP D 83  ALA D 89  
H 2 GLY D 41  ? HIS D 48  ? GLY D 41  HIS D 48  
H 3 THR D 116 ? HIS D 120 ? THR D 116 HIS D 120 
H 4 ARG D 143 ? VAL D 148 ? ARG D 143 VAL D 148 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2 O ASP A 101 ? O ASP A 101 N VAL A 29  ? N VAL A 29  
A 2 3 O LYS A 36  ? O LYS A 36  N GLN A 15  ? N GLN A 15  
A 3 4 O GLY A 16  ? O GLY A 16  N LEU A 8   ? N LEU A 8   
A 4 5 N VAL A 5   ? N VAL A 5   O GLY A 150 ? O GLY A 150 
B 1 2 O ALA A 89  ? O ALA A 89  N GLY A 41  ? N GLY A 41  
B 2 3 N GLY A 44  ? N GLY A 44  O HIS A 120 ? O HIS A 120 
B 3 4 N VAL A 119 ? N VAL A 119 O ALA A 145 ? O ALA A 145 
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 GLY B 16  ? O GLY B 16  N LEU B 8   ? N LEU B 8   
C 4 5 N VAL B 5   ? N VAL B 5   O GLY B 150 ? O GLY B 150 
D 1 2 O ALA B 89  ? O ALA B 89  N GLY B 41  ? N GLY B 41  
D 2 3 N HIS B 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 ILE C 18  ? O ILE C 18  N CYS C 6   ? N CYS C 6   
E 4 5 N VAL C 5   ? N VAL C 5   O GLY C 150 ? O GLY C 150 
F 1 2 O ALA C 89  ? O ALA C 89  N GLY C 41  ? N GLY C 41  
F 2 3 N HIS C 46  ? N HIS C 46  O VAL C 118 ? O VAL C 118 
F 3 4 N LEU C 117 ? N LEU C 117 O GLY C 147 ? O GLY C 147 
G 1 2 O ASP D 101 ? O ASP D 101 N VAL D 29  ? N VAL D 29  
G 2 3 O LYS D 36  ? O LYS D 36  N GLN D 15  ? N GLN D 15  
G 3 4 O GLY D 16  ? O GLY D 16  N LEU D 8   ? N LEU D 8   
G 4 5 N VAL D 5   ? N VAL D 5   O GLY D 150 ? O GLY D 150 
H 1 2 O VAL D 87  ? O VAL D 87  N HIS D 43  ? N HIS D 43  
H 2 3 N HIS D 48  ? N HIS D 48  O THR D 116 ? O THR D 116 
H 3 4 N VAL D 119 ? N VAL D 119 O LEU D 144 ? O LEU D 144 
# 
_database_PDB_matrix.entry_id          3ECW 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    3ECW 
_atom_sites.fract_transf_matrix[1][1]   0.006372 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002593 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.029383 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.009422 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ALA A 1 1   ? -3.875  -12.247 -29.102 1.00 43.10 ? 1   ALA A N   1 
ATOM   2    C CA  . ALA A 1 1   ? -2.880  -11.985 -28.007 1.00 41.99 ? 1   ALA A CA  1 
ATOM   3    C C   . ALA A 1 1   ? -1.687  -11.126 -28.471 1.00 40.92 ? 1   ALA A C   1 
ATOM   4    O O   . ALA A 1 1   ? -0.833  -11.577 -29.276 1.00 41.09 ? 1   ALA A O   1 
ATOM   5    C CB  . ALA A 1 1   ? -2.407  -13.330 -27.386 1.00 42.88 ? 1   ALA A CB  1 
ATOM   6    N N   . THR A 1 2   ? -1.611  -9.907  -27.941 1.00 38.30 ? 2   THR A N   1 
ATOM   7    C CA  . THR A 1 2   ? -0.729  -8.889  -28.535 1.00 34.51 ? 2   THR A CA  1 
ATOM   8    C C   . THR A 1 2   ? 0.838   -9.014  -28.245 1.00 33.28 ? 2   THR A C   1 
ATOM   9    O O   . THR A 1 2   ? 1.277   -9.413  -27.162 1.00 33.38 ? 2   THR A O   1 
ATOM   10   C CB  . THR A 1 2   ? -1.490  -7.483  -28.541 1.00 35.38 ? 2   THR A CB  1 
ATOM   11   O OG1 . THR A 1 2   ? -1.151  -6.693  -29.685 1.00 38.82 ? 2   THR A OG1 1 
ATOM   12   C CG2 . THR A 1 2   ? -1.481  -6.710  -27.237 1.00 35.16 ? 2   THR A CG2 1 
ATOM   13   N N   . LYS A 1 3   ? 1.633   -8.748  -29.290 1.00 30.11 ? 3   LYS A N   1 
ATOM   14   C CA  . LYS A 1 3   ? 3.100   -8.846  -29.355 1.00 29.11 ? 3   LYS A CA  1 
ATOM   15   C C   . LYS A 1 3   ? 3.763   -7.530  -29.880 1.00 26.36 ? 3   LYS A C   1 
ATOM   16   O O   . LYS A 1 3   ? 3.289   -6.944  -30.830 1.00 24.50 ? 3   LYS A O   1 
ATOM   17   C CB  . LYS A 1 3   ? 3.515   -9.978  -30.319 1.00 26.89 ? 3   LYS A CB  1 
ATOM   18   C CG  . LYS A 1 3   ? 3.499   -11.373 -29.747 1.00 29.56 ? 3   LYS A CG  1 
ATOM   19   C CD  . LYS A 1 3   ? 4.945   -11.901 -29.659 1.00 35.85 ? 3   LYS A CD  1 
ATOM   20   C CE  . LYS A 1 3   ? 5.068   -13.361 -30.207 1.00 37.91 ? 3   LYS A CE  1 
ATOM   21   N NZ  . LYS A 1 3   ? 6.463   -13.713 -30.732 1.00 36.34 ? 3   LYS A NZ  1 
ATOM   22   N N   . ALA A 1 4   ? 4.896   -7.146  -29.294 1.00 23.06 ? 4   ALA A N   1 
ATOM   23   C CA  . ALA A 1 4   ? 5.686   -6.062  -29.784 1.00 21.32 ? 4   ALA A CA  1 
ATOM   24   C C   . ALA A 1 4   ? 7.153   -6.458  -29.835 1.00 20.23 ? 4   ALA A C   1 
ATOM   25   O O   . ALA A 1 4   ? 7.534   -7.525  -29.404 1.00 19.85 ? 4   ALA A O   1 
ATOM   26   C CB  . ALA A 1 4   ? 5.436   -4.744  -28.939 1.00 19.97 ? 4   ALA A CB  1 
ATOM   27   N N   . VAL A 1 5   ? 7.988   -5.588  -30.384 1.00 20.20 ? 5   VAL A N   1 
ATOM   28   C CA  . VAL A 1 5   ? 9.396   -5.895  -30.588 1.00 18.42 ? 5   VAL A CA  1 
ATOM   29   C C   . VAL A 1 5   ? 10.109  -4.514  -30.542 1.00 18.41 ? 5   VAL A C   1 
ATOM   30   O O   . VAL A 1 5   ? 9.547   -3.548  -30.827 1.00 16.83 ? 5   VAL A O   1 
ATOM   31   C CB  . VAL A 1 5   ? 9.666   -6.729  -31.886 1.00 18.37 ? 5   VAL A CB  1 
ATOM   32   C CG1 . VAL A 1 5   ? 9.417   -5.886  -33.100 1.00 21.36 ? 5   VAL A CG1 1 
ATOM   33   C CG2 . VAL A 1 5   ? 11.128  -7.200  -31.941 1.00 17.24 ? 5   VAL A CG2 1 
ATOM   34   N N   . CYS A 1 6   ? 11.371  -4.480  -30.117 1.00 19.42 ? 6   CYS A N   1 
ATOM   35   C CA  . CYS A 1 6   ? 12.179  -3.319  -30.182 1.00 18.80 ? 6   CYS A CA  1 
ATOM   36   C C   . CYS A 1 6   ? 13.554  -3.820  -30.624 1.00 19.44 ? 6   CYS A C   1 
ATOM   37   O O   . CYS A 1 6   ? 14.089  -4.758  -30.061 1.00 19.74 ? 6   CYS A O   1 
ATOM   38   C CB  . CYS A 1 6   ? 12.244  -2.696  -28.806 1.00 17.39 ? 6   CYS A CB  1 
ATOM   39   S SG  . CYS A 1 6   ? 13.198  -1.249  -28.889 1.00 19.61 ? 6   CYS A SG  1 
ATOM   40   N N   . VAL A 1 7   ? 14.087  -3.235  -31.690 1.00 20.22 ? 7   VAL A N   1 
ATOM   41   C CA  . VAL A 1 7   ? 15.475  -3.431  -32.091 1.00 19.66 ? 7   VAL A CA  1 
ATOM   42   C C   . VAL A 1 7   ? 16.250  -2.195  -31.602 1.00 20.38 ? 7   VAL A C   1 
ATOM   43   O O   . VAL A 1 7   ? 15.928  -1.021  -31.976 1.00 18.59 ? 7   VAL A O   1 
ATOM   44   C CB  . VAL A 1 7   ? 15.566  -3.523  -33.631 1.00 20.13 ? 7   VAL A CB  1 
ATOM   45   C CG1 . VAL A 1 7   ? 17.007  -3.887  -34.101 1.00 18.68 ? 7   VAL A CG1 1 
ATOM   46   C CG2 . VAL A 1 7   ? 14.520  -4.479  -34.142 1.00 19.72 ? 7   VAL A CG2 1 
ATOM   47   N N   . LEU A 1 8   ? 17.228  -2.497  -30.741 1.00 19.68 ? 8   LEU A N   1 
ATOM   48   C CA  . LEU A 1 8   ? 18.167  -1.552  -30.117 1.00 18.71 ? 8   LEU A CA  1 
ATOM   49   C C   . LEU A 1 8   ? 19.426  -1.305  -30.942 1.00 18.62 ? 8   LEU A C   1 
ATOM   50   O O   . LEU A 1 8   ? 20.119  -2.258  -31.339 1.00 17.64 ? 8   LEU A O   1 
ATOM   51   C CB  . LEU A 1 8   ? 18.547  -2.084  -28.708 1.00 17.03 ? 8   LEU A CB  1 
ATOM   52   C CG  . LEU A 1 8   ? 17.474  -1.938  -27.582 1.00 14.91 ? 8   LEU A CG  1 
ATOM   53   C CD1 . LEU A 1 8   ? 16.122  -2.054  -28.057 1.00 22.76 ? 8   LEU A CD1 1 
ATOM   54   C CD2 . LEU A 1 8   ? 17.741  -2.911  -26.527 1.00 20.33 ? 8   LEU A CD2 1 
ATOM   55   N N   . LYS A 1 9   ? 19.705  -0.016  -31.188 1.00 20.12 ? 9   LYS A N   1 
ATOM   56   C CA  . LYS A 1 9   ? 20.858  0.439   -31.956 1.00 21.41 ? 9   LYS A CA  1 
ATOM   57   C C   . LYS A 1 9   ? 21.266  1.766   -31.368 1.00 21.85 ? 9   LYS A C   1 
ATOM   58   O O   . LYS A 1 9   ? 20.430  2.464   -30.798 1.00 21.55 ? 9   LYS A O   1 
ATOM   59   C CB  . LYS A 1 9   ? 20.459  0.707   -33.414 1.00 22.70 ? 9   LYS A CB  1 
ATOM   60   C CG  . LYS A 1 9   ? 20.324  -0.520  -34.195 1.00 28.61 ? 9   LYS A CG  1 
ATOM   61   C CD  . LYS A 1 9   ? 19.978  -0.175  -35.652 1.00 36.34 ? 9   LYS A CD  1 
ATOM   62   C CE  . LYS A 1 9   ? 20.015  -1.456  -36.564 1.00 36.51 ? 9   LYS A CE  1 
ATOM   63   N NZ  . LYS A 1 9   ? 18.699  -2.173  -36.528 1.00 39.02 ? 9   LYS A NZ  1 
ATOM   64   N N   . GLY A 1 10  ? 22.527  2.122   -31.515 1.00 20.34 ? 10  GLY A N   1 
ATOM   65   C CA  . GLY A 1 10  ? 23.033  3.391   -31.036 1.00 23.69 ? 10  GLY A CA  1 
ATOM   66   C C   . GLY A 1 10  ? 24.261  3.667   -31.876 1.00 24.42 ? 10  GLY A C   1 
ATOM   67   O O   . GLY A 1 10  ? 24.487  2.970   -32.857 1.00 24.26 ? 10  GLY A O   1 
ATOM   68   N N   . ASP A 1 11  ? 25.042  4.652   -31.462 1.00 24.66 ? 11  ASP A N   1 
ATOM   69   C CA  . ASP A 1 11  ? 26.246  5.086   -32.146 1.00 26.77 ? 11  ASP A CA  1 
ATOM   70   C C   . ASP A 1 11  ? 27.437  4.194   -31.827 1.00 26.36 ? 11  ASP A C   1 
ATOM   71   O O   . ASP A 1 11  ? 28.517  4.326   -32.406 1.00 27.82 ? 11  ASP A O   1 
ATOM   72   C CB  . ASP A 1 11  ? 26.593  6.543   -31.743 1.00 26.93 ? 11  ASP A CB  1 
ATOM   73   C CG  . ASP A 1 11  ? 25.556  7.554   -32.205 1.00 30.03 ? 11  ASP A CG  1 
ATOM   74   O OD1 . ASP A 1 11  ? 25.191  7.535   -33.416 1.00 33.93 ? 11  ASP A OD1 1 
ATOM   75   O OD2 . ASP A 1 11  ? 25.133  8.391   -31.352 1.00 33.67 ? 11  ASP A OD2 1 
ATOM   76   N N   . GLY A 1 12  ? 27.267  3.319   -30.860 1.00 25.45 ? 12  GLY A N   1 
ATOM   77   C CA  . GLY A 1 12  ? 28.366  2.455   -30.416 1.00 22.25 ? 12  GLY A CA  1 
ATOM   78   C C   . GLY A 1 12  ? 28.114  1.052   -30.899 1.00 20.96 ? 12  GLY A C   1 
ATOM   79   O O   . GLY A 1 12  ? 27.478  0.858   -31.925 1.00 21.03 ? 12  GLY A O   1 
ATOM   80   N N   . PRO A 1 13  ? 28.648  0.060   -30.182 1.00 19.51 ? 13  PRO A N   1 
ATOM   81   C CA  . PRO A 1 13  ? 28.513  -1.331  -30.605 1.00 19.23 ? 13  PRO A CA  1 
ATOM   82   C C   . PRO A 1 13  ? 27.288  -2.096  -30.060 1.00 19.87 ? 13  PRO A C   1 
ATOM   83   O O   . PRO A 1 13  ? 27.077  -3.274  -30.403 1.00 19.30 ? 13  PRO A O   1 
ATOM   84   C CB  . PRO A 1 13  ? 29.815  -1.937  -30.081 1.00 19.19 ? 13  PRO A CB  1 
ATOM   85   C CG  . PRO A 1 13  ? 29.975  -1.239  -28.743 1.00 17.26 ? 13  PRO A CG  1 
ATOM   86   C CD  . PRO A 1 13  ? 29.565  0.204   -29.014 1.00 19.11 ? 13  PRO A CD  1 
ATOM   87   N N   . VAL A 1 14  ? 26.528  -1.434  -29.209 1.00 20.71 ? 14  VAL A N   1 
ATOM   88   C CA  . VAL A 1 14  ? 25.407  -2.052  -28.502 1.00 21.55 ? 14  VAL A CA  1 
ATOM   89   C C   . VAL A 1 14  ? 24.239  -2.365  -29.468 1.00 22.39 ? 14  VAL A C   1 
ATOM   90   O O   . VAL A 1 14  ? 23.662  -1.482  -30.026 1.00 23.22 ? 14  VAL A O   1 
ATOM   91   C CB  . VAL A 1 14  ? 24.938  -1.192  -27.305 1.00 20.58 ? 14  VAL A CB  1 
ATOM   92   C CG1 . VAL A 1 14  ? 23.761  -1.847  -26.609 1.00 19.12 ? 14  VAL A CG1 1 
ATOM   93   C CG2 . VAL A 1 14  ? 26.036  -1.047  -26.287 1.00 16.13 ? 14  VAL A CG2 1 
ATOM   94   N N   . GLN A 1 15  ? 23.923  -3.641  -29.638 1.00 23.04 ? 15  GLN A N   1 
ATOM   95   C CA  . GLN A 1 15  ? 22.815  -4.105  -30.444 1.00 24.46 ? 15  GLN A CA  1 
ATOM   96   C C   . GLN A 1 15  ? 22.006  -5.110  -29.662 1.00 23.51 ? 15  GLN A C   1 
ATOM   97   O O   . GLN A 1 15  ? 22.566  -5.830  -28.812 1.00 22.12 ? 15  GLN A O   1 
ATOM   98   C CB  . GLN A 1 15  ? 23.306  -4.817  -31.699 1.00 25.32 ? 15  GLN A CB  1 
ATOM   99   C CG  . GLN A 1 15  ? 24.226  -3.998  -32.576 1.00 29.49 ? 15  GLN A CG  1 
ATOM   100  C CD  . GLN A 1 15  ? 24.544  -4.721  -33.856 1.00 30.58 ? 15  GLN A CD  1 
ATOM   101  O OE1 . GLN A 1 15  ? 23.977  -5.763  -34.118 1.00 39.25 ? 15  GLN A OE1 1 
ATOM   102  N NE2 . GLN A 1 15  ? 25.420  -4.157  -34.679 1.00 29.67 ? 15  GLN A NE2 1 
ATOM   103  N N   . GLY A 1 16  ? 20.704  -5.145  -29.961 1.00 21.30 ? 16  GLY A N   1 
ATOM   104  C CA  . GLY A 1 16  ? 19.806  -6.053  -29.303 1.00 20.76 ? 16  GLY A CA  1 
ATOM   105  C C   . GLY A 1 16  ? 18.427  -6.207  -29.879 1.00 19.22 ? 16  GLY A C   1 
ATOM   106  O O   . GLY A 1 16  ? 17.911  -5.307  -30.504 1.00 19.98 ? 16  GLY A O   1 
ATOM   107  N N   . ILE A 1 17  ? 17.836  -7.376  -29.682 1.00 19.37 ? 17  ILE A N   1 
ATOM   108  C CA  . ILE A 1 17  ? 16.409  -7.560  -29.956 1.00 19.63 ? 17  ILE A CA  1 
ATOM   109  C C   . ILE A 1 17  ? 15.636  -7.957  -28.700 1.00 19.04 ? 17  ILE A C   1 
ATOM   110  O O   . ILE A 1 17  ? 16.028  -8.861  -27.991 1.00 21.00 ? 17  ILE A O   1 
ATOM   111  C CB  . ILE A 1 17  ? 16.167  -8.578  -31.075 1.00 19.84 ? 17  ILE A CB  1 
ATOM   112  C CG1 . ILE A 1 17  ? 17.008  -8.169  -32.300 1.00 18.44 ? 17  ILE A CG1 1 
ATOM   113  C CG2 . ILE A 1 17  ? 14.713  -8.559  -31.452 1.00 17.11 ? 17  ILE A CG2 1 
ATOM   114  C CD1 . ILE A 1 17  ? 16.998  -9.227  -33.446 1.00 23.07 ? 17  ILE A CD1 1 
ATOM   115  N N   . ILE A 1 18  ? 14.512  -7.291  -28.483 1.00 18.37 ? 18  ILE A N   1 
ATOM   116  C CA  . ILE A 1 18  ? 13.717  -7.407  -27.302 1.00 18.17 ? 18  ILE A CA  1 
ATOM   117  C C   . ILE A 1 18  ? 12.270  -7.576  -27.728 1.00 17.80 ? 18  ILE A C   1 
ATOM   118  O O   . ILE A 1 18  ? 11.755  -6.783  -28.496 1.00 18.87 ? 18  ILE A O   1 
ATOM   119  C CB  . ILE A 1 18  ? 13.877  -6.134  -26.303 1.00 18.39 ? 18  ILE A CB  1 
ATOM   120  C CG1 . ILE A 1 18  ? 15.368  -5.859  -25.964 1.00 18.35 ? 18  ILE A CG1 1 
ATOM   121  C CG2 . ILE A 1 18  ? 13.048  -6.342  -25.004 1.00 14.51 ? 18  ILE A CG2 1 
ATOM   122  C CD1 . ILE A 1 18  ? 16.124  -7.008  -25.173 1.00 11.48 ? 18  ILE A CD1 1 
ATOM   123  N N   . ASN A 1 19  ? 11.633  -8.577  -27.144 1.00 17.58 ? 19  ASN A N   1 
ATOM   124  C CA  . ASN A 1 19  ? 10.329  -9.014  -27.481 1.00 18.27 ? 19  ASN A CA  1 
ATOM   125  C C   . ASN A 1 19  ? 9.456   -8.776  -26.254 1.00 18.43 ? 19  ASN A C   1 
ATOM   126  O O   . ASN A 1 19  ? 9.924   -8.903  -25.135 1.00 19.44 ? 19  ASN A O   1 
ATOM   127  C CB  . ASN A 1 19  ? 10.281  -10.548 -27.758 1.00 19.24 ? 19  ASN A CB  1 
ATOM   128  C CG  . ASN A 1 19  ? 11.086  -10.992 -29.015 1.00 16.99 ? 19  ASN A CG  1 
ATOM   129  O OD1 . ASN A 1 19  ? 10.791  -10.631 -30.143 1.00 24.70 ? 19  ASN A OD1 1 
ATOM   130  N ND2 . ASN A 1 19  ? 12.068  -11.747 -28.804 1.00 13.85 ? 19  ASN A ND2 1 
ATOM   131  N N   . PHE A 1 20  ? 8.192   -8.499  -26.496 1.00 18.60 ? 20  PHE A N   1 
ATOM   132  C CA  . PHE A 1 20  ? 7.196   -8.173  -25.498 1.00 20.90 ? 20  PHE A CA  1 
ATOM   133  C C   . PHE A 1 20  ? 5.986   -8.999  -25.816 1.00 22.16 ? 20  PHE A C   1 
ATOM   134  O O   . PHE A 1 20  ? 5.607   -9.154  -26.968 1.00 22.10 ? 20  PHE A O   1 
ATOM   135  C CB  . PHE A 1 20  ? 6.757   -6.716  -25.680 1.00 19.27 ? 20  PHE A CB  1 
ATOM   136  C CG  . PHE A 1 20  ? 7.853   -5.721  -25.470 1.00 17.39 ? 20  PHE A CG  1 
ATOM   137  C CD1 . PHE A 1 20  ? 8.792   -5.460  -26.465 1.00 17.61 ? 20  PHE A CD1 1 
ATOM   138  C CD2 . PHE A 1 20  ? 7.950   -5.049  -24.248 1.00 19.20 ? 20  PHE A CD2 1 
ATOM   139  C CE1 . PHE A 1 20  ? 9.845   -4.483  -26.249 1.00 15.78 ? 20  PHE A CE1 1 
ATOM   140  C CE2 . PHE A 1 20  ? 8.987   -4.099  -24.034 1.00 20.56 ? 20  PHE A CE2 1 
ATOM   141  C CZ  . PHE A 1 20  ? 9.915   -3.854  -25.015 1.00 17.82 ? 20  PHE A CZ  1 
ATOM   142  N N   . GLU A 1 21  ? 5.318   -9.443  -24.787 1.00 25.15 ? 21  GLU A N   1 
ATOM   143  C CA  . GLU A 1 21  ? 4.165   -10.258 -25.008 1.00 28.61 ? 21  GLU A CA  1 
ATOM   144  C C   . GLU A 1 21  ? 3.188   -10.138 -23.887 1.00 29.26 ? 21  GLU A C   1 
ATOM   145  O O   . GLU A 1 21  ? 3.528   -10.382 -22.758 1.00 31.26 ? 21  GLU A O   1 
ATOM   146  C CB  . GLU A 1 21  ? 4.582   -11.710 -25.123 1.00 28.46 ? 21  GLU A CB  1 
ATOM   147  C CG  . GLU A 1 21  ? 3.368   -12.562 -25.375 1.00 34.86 ? 21  GLU A CG  1 
ATOM   148  C CD  . GLU A 1 21  ? 3.713   -13.815 -26.040 1.00 40.90 ? 21  GLU A CD  1 
ATOM   149  O OE1 . GLU A 1 21  ? 4.065   -14.784 -25.267 1.00 40.92 ? 21  GLU A OE1 1 
ATOM   150  O OE2 . GLU A 1 21  ? 3.626   -13.791 -27.318 1.00 41.32 ? 21  GLU A OE2 1 
ATOM   151  N N   . GLN A 1 22  ? 1.964   -9.789  -24.211 1.00 30.64 ? 22  GLN A N   1 
ATOM   152  C CA  . GLN A 1 22  ? 0.925   -9.634  -23.201 1.00 31.80 ? 22  GLN A CA  1 
ATOM   153  C C   . GLN A 1 22  ? -0.291  -10.384 -23.712 1.00 33.30 ? 22  GLN A C   1 
ATOM   154  O O   . GLN A 1 22  ? -1.024  -9.881  -24.553 1.00 34.43 ? 22  GLN A O   1 
ATOM   155  C CB  . GLN A 1 22  ? 0.589   -8.164  -22.979 1.00 30.56 ? 22  GLN A CB  1 
ATOM   156  C CG  . GLN A 1 22  ? -0.384  -7.936  -21.868 1.00 25.49 ? 22  GLN A CG  1 
ATOM   157  C CD  . GLN A 1 22  ? -0.580  -6.470  -21.608 1.00 26.43 ? 22  GLN A CD  1 
ATOM   158  O OE1 . GLN A 1 22  ? -0.617  -5.660  -22.570 1.00 22.30 ? 22  GLN A OE1 1 
ATOM   159  N NE2 . GLN A 1 22  ? -0.742  -6.097  -20.317 1.00 20.21 ? 22  GLN A NE2 1 
ATOM   160  N N   . LYS A 1 23  ? -0.430  -11.624 -23.270 1.00 35.50 ? 23  LYS A N   1 
ATOM   161  C CA  . LYS A 1 23  ? -1.480  -12.500 -23.741 1.00 37.88 ? 23  LYS A CA  1 
ATOM   162  C C   . LYS A 1 23  ? -2.901  -12.031 -23.388 1.00 38.16 ? 23  LYS A C   1 
ATOM   163  O O   . LYS A 1 23  ? -3.834  -12.376 -24.128 1.00 39.80 ? 23  LYS A O   1 
ATOM   164  C CB  . LYS A 1 23  ? -1.226  -13.953 -23.301 1.00 38.05 ? 23  LYS A CB  1 
ATOM   165  C CG  . LYS A 1 23  ? -0.105  -14.610 -24.083 1.00 41.42 ? 23  LYS A CG  1 
ATOM   166  C CD  . LYS A 1 23  ? -0.598  -15.715 -25.012 1.00 45.13 ? 23  LYS A CD  1 
ATOM   167  C CE  . LYS A 1 23  ? 0.400   -15.972 -26.184 1.00 46.26 ? 23  LYS A CE  1 
ATOM   168  N NZ  . LYS A 1 23  ? -0.306  -16.183 -27.508 1.00 45.22 ? 23  LYS A NZ  1 
ATOM   169  N N   . GLU A 1 24  ? -3.081  -11.246 -22.317 1.00 38.17 ? 24  GLU A N   1 
ATOM   170  C CA  . GLU A 1 24  ? -4.390  -10.575 -22.078 1.00 39.33 ? 24  GLU A CA  1 
ATOM   171  C C   . GLU A 1 24  ? -4.256  -9.153  -21.551 1.00 38.74 ? 24  GLU A C   1 
ATOM   172  O O   . GLU A 1 24  ? -3.307  -8.872  -20.866 1.00 37.75 ? 24  GLU A O   1 
ATOM   173  C CB  . GLU A 1 24  ? -5.279  -11.366 -21.086 1.00 40.03 ? 24  GLU A CB  1 
ATOM   174  C CG  . GLU A 1 24  ? -4.710  -11.527 -19.692 1.00 41.90 ? 24  GLU A CG  1 
ATOM   175  C CD  . GLU A 1 24  ? -4.142  -12.937 -19.426 1.00 47.28 ? 24  GLU A CD  1 
ATOM   176  O OE1 . GLU A 1 24  ? -3.145  -13.052 -18.663 1.00 48.09 ? 24  GLU A OE1 1 
ATOM   177  O OE2 . GLU A 1 24  ? -4.713  -13.926 -19.958 1.00 48.78 ? 24  GLU A OE2 1 
ATOM   178  N N   . SER A 1 25  ? -5.253  -8.312  -21.811 1.00 39.02 ? 25  SER A N   1 
ATOM   179  C CA  . SER A 1 25  ? -5.174  -6.861  -21.526 1.00 40.44 ? 25  SER A CA  1 
ATOM   180  C C   . SER A 1 25  ? -4.689  -6.475  -20.106 1.00 40.91 ? 25  SER A C   1 
ATOM   181  O O   . SER A 1 25  ? -3.725  -5.725  -19.942 1.00 40.68 ? 25  SER A O   1 
ATOM   182  C CB  . SER A 1 25  ? -6.524  -6.195  -21.868 1.00 41.16 ? 25  SER A CB  1 
ATOM   183  O OG  . SER A 1 25  ? -7.195  -5.619  -20.745 1.00 43.31 ? 25  SER A OG  1 
ATOM   184  N N   . ASN A 1 26  ? -5.350  -7.031  -19.090 1.00 41.87 ? 26  ASN A N   1 
ATOM   185  C CA  . ASN A 1 26  ? -5.003  -6.864  -17.657 1.00 42.26 ? 26  ASN A CA  1 
ATOM   186  C C   . ASN A 1 26  ? -3.720  -7.585  -17.165 1.00 41.81 ? 26  ASN A C   1 
ATOM   187  O O   . ASN A 1 26  ? -3.317  -7.396  -16.036 1.00 41.94 ? 26  ASN A O   1 
ATOM   188  C CB  . ASN A 1 26  ? -6.161  -7.404  -16.799 1.00 43.05 ? 26  ASN A CB  1 
ATOM   189  C CG  . ASN A 1 26  ? -6.466  -8.898  -17.083 1.00 44.70 ? 26  ASN A CG  1 
ATOM   190  O OD1 . ASN A 1 26  ? -6.805  -9.268  -18.217 1.00 45.01 ? 26  ASN A OD1 1 
ATOM   191  N ND2 . ASN A 1 26  ? -6.368  -9.750  -16.041 1.00 45.75 ? 26  ASN A ND2 1 
ATOM   192  N N   . GLY A 1 27  ? -3.129  -8.458  -17.978 1.00 40.78 ? 27  GLY A N   1 
ATOM   193  C CA  . GLY A 1 27  ? -2.088  -9.340  -17.496 1.00 38.54 ? 27  GLY A CA  1 
ATOM   194  C C   . GLY A 1 27  ? -0.727  -8.711  -17.605 1.00 36.85 ? 27  GLY A C   1 
ATOM   195  O O   . GLY A 1 27  ? -0.594  -7.564  -18.028 1.00 36.99 ? 27  GLY A O   1 
ATOM   196  N N   . PRO A 1 28  ? 0.292   -9.456  -17.181 1.00 35.82 ? 28  PRO A N   1 
ATOM   197  C CA  . PRO A 1 28  ? 1.685   -9.024  -17.199 1.00 33.93 ? 28  PRO A CA  1 
ATOM   198  C C   . PRO A 1 28  ? 2.344   -9.121  -18.610 1.00 31.61 ? 28  PRO A C   1 
ATOM   199  O O   . PRO A 1 28  ? 2.043   -10.045 -19.392 1.00 29.78 ? 28  PRO A O   1 
ATOM   200  C CB  . PRO A 1 28  ? 2.343   -10.005 -16.234 1.00 33.86 ? 28  PRO A CB  1 
ATOM   201  C CG  . PRO A 1 28  ? 1.604   -11.241 -16.428 1.00 35.49 ? 28  PRO A CG  1 
ATOM   202  C CD  . PRO A 1 28  ? 0.161   -10.809 -16.594 1.00 36.23 ? 28  PRO A CD  1 
ATOM   203  N N   . VAL A 1 29  ? 3.233   -8.171  -18.898 1.00 28.87 ? 29  VAL A N   1 
ATOM   204  C CA  . VAL A 1 29  ? 3.982   -8.166  -20.160 1.00 26.28 ? 29  VAL A CA  1 
ATOM   205  C C   . VAL A 1 29  ? 5.258   -8.975  -19.905 1.00 25.96 ? 29  VAL A C   1 
ATOM   206  O O   . VAL A 1 29  ? 6.005   -8.685  -18.958 1.00 25.52 ? 29  VAL A O   1 
ATOM   207  C CB  . VAL A 1 29  ? 4.243   -6.748  -20.690 1.00 25.94 ? 29  VAL A CB  1 
ATOM   208  C CG1 . VAL A 1 29  ? 4.985   -6.744  -22.038 1.00 20.44 ? 29  VAL A CG1 1 
ATOM   209  C CG2 . VAL A 1 29  ? 2.950   -6.010  -20.823 1.00 23.11 ? 29  VAL A CG2 1 
ATOM   210  N N   . LYS A 1 30  ? 5.425   -10.032 -20.702 1.00 23.36 ? 30  LYS A N   1 
ATOM   211  C CA  . LYS A 1 30  ? 6.596   -10.866 -20.710 1.00 24.68 ? 30  LYS A CA  1 
ATOM   212  C C   . LYS A 1 30  ? 7.573   -10.158 -21.619 1.00 21.97 ? 30  LYS A C   1 
ATOM   213  O O   . LYS A 1 30  ? 7.193   -9.777  -22.736 1.00 20.76 ? 30  LYS A O   1 
ATOM   214  C CB  . LYS A 1 30  ? 6.262   -12.228 -21.376 1.00 25.29 ? 30  LYS A CB  1 
ATOM   215  C CG  . LYS A 1 30  ? 6.118   -13.470 -20.464 1.00 28.58 ? 30  LYS A CG  1 
ATOM   216  C CD  . LYS A 1 30  ? 6.715   -14.731 -21.233 1.00 30.21 ? 30  LYS A CD  1 
ATOM   217  C CE  . LYS A 1 30  ? 6.368   -16.145 -20.595 1.00 33.56 ? 30  LYS A CE  1 
ATOM   218  N NZ  . LYS A 1 30  ? 6.009   -17.201 -21.704 1.00 35.66 ? 30  LYS A NZ  1 
ATOM   219  N N   . VAL A 1 31  ? 8.808   -9.950  -21.167 1.00 20.69 ? 31  VAL A N   1 
ATOM   220  C CA  . VAL A 1 31  ? 9.849   -9.273  -22.001 1.00 19.91 ? 31  VAL A CA  1 
ATOM   221  C C   . VAL A 1 31  ? 11.180  -10.027 -22.029 1.00 20.87 ? 31  VAL A C   1 
ATOM   222  O O   . VAL A 1 31  ? 11.702  -10.348 -21.003 1.00 21.64 ? 31  VAL A O   1 
ATOM   223  C CB  . VAL A 1 31  ? 10.020  -7.594  -21.843 1.00 20.09 ? 31  VAL A CB  1 
ATOM   224  C CG1 . VAL A 1 31  ? 9.424   -6.964  -20.645 1.00 12.90 ? 31  VAL A CG1 1 
ATOM   225  C CG2 . VAL A 1 31  ? 11.457  -7.098  -22.071 1.00 16.05 ? 31  VAL A CG2 1 
ATOM   226  N N   . TRP A 1 32  ? 11.742  -10.245 -23.209 1.00 22.48 ? 32  TRP A N   1 
ATOM   227  C CA  . TRP A 1 32  ? 12.919  -11.131 -23.363 1.00 23.75 ? 32  TRP A CA  1 
ATOM   228  C C   . TRP A 1 32  ? 13.628  -10.938 -24.702 1.00 22.55 ? 32  TRP A C   1 
ATOM   229  O O   . TRP A 1 32  ? 12.992  -10.692 -25.701 1.00 22.41 ? 32  TRP A O   1 
ATOM   230  C CB  . TRP A 1 32  ? 12.519  -12.616 -23.239 1.00 24.05 ? 32  TRP A CB  1 
ATOM   231  C CG  . TRP A 1 32  ? 11.794  -13.182 -24.478 1.00 26.44 ? 32  TRP A CG  1 
ATOM   232  C CD1 . TRP A 1 32  ? 12.334  -14.015 -25.403 1.00 25.65 ? 32  TRP A CD1 1 
ATOM   233  C CD2 . TRP A 1 32  ? 10.437  -12.936 -24.908 1.00 26.38 ? 32  TRP A CD2 1 
ATOM   234  N NE1 . TRP A 1 32  ? 11.427  -14.308 -26.350 1.00 28.27 ? 32  TRP A NE1 1 
ATOM   235  C CE2 . TRP A 1 32  ? 10.248  -13.665 -26.077 1.00 26.96 ? 32  TRP A CE2 1 
ATOM   236  C CE3 . TRP A 1 32  ? 9.378   -12.130 -24.434 1.00 24.53 ? 32  TRP A CE3 1 
ATOM   237  C CZ2 . TRP A 1 32  ? 9.038   -13.650 -26.784 1.00 28.68 ? 32  TRP A CZ2 1 
ATOM   238  C CZ3 . TRP A 1 32  ? 8.192   -12.132 -25.094 1.00 23.45 ? 32  TRP A CZ3 1 
ATOM   239  C CH2 . TRP A 1 32  ? 8.018   -12.878 -26.277 1.00 27.48 ? 32  TRP A CH2 1 
ATOM   240  N N   . GLY A 1 33  ? 14.944  -11.098 -24.717 1.00 21.80 ? 33  GLY A N   1 
ATOM   241  C CA  . GLY A 1 33  ? 15.684  -10.942 -25.946 1.00 21.38 ? 33  GLY A CA  1 
ATOM   242  C C   . GLY A 1 33  ? 17.086  -11.003 -25.457 1.00 22.42 ? 33  GLY A C   1 
ATOM   243  O O   . GLY A 1 33  ? 17.290  -11.503 -24.383 1.00 21.59 ? 33  GLY A O   1 
ATOM   244  N N   . SER A 1 34  ? 18.006  -10.389 -26.213 1.00 23.10 ? 34  SER A N   1 
ATOM   245  C CA  . SER A 1 34  ? 19.437  -10.356 -25.959 1.00 23.42 ? 34  SER A CA  1 
ATOM   246  C C   . SER A 1 34  ? 20.002  -9.021  -26.437 1.00 22.19 ? 34  SER A C   1 
ATOM   247  O O   . SER A 1 34  ? 19.524  -8.506  -27.424 1.00 24.12 ? 34  SER A O   1 
ATOM   248  C CB  . SER A 1 34  ? 20.078  -11.406 -26.801 1.00 23.26 ? 34  SER A CB  1 
ATOM   249  O OG  . SER A 1 34  ? 21.403  -11.601 -26.395 1.00 26.42 ? 34  SER A OG  1 
ATOM   250  N N   . ILE A 1 35  ? 21.004  -8.486  -25.753 1.00 20.49 ? 35  ILE A N   1 
ATOM   251  C CA  . ILE A 1 35  ? 21.701  -7.263  -26.103 1.00 19.96 ? 35  ILE A CA  1 
ATOM   252  C C   . ILE A 1 35  ? 23.197  -7.610  -26.021 1.00 21.84 ? 35  ILE A C   1 
ATOM   253  O O   . ILE A 1 35  ? 23.646  -8.178  -25.028 1.00 24.16 ? 35  ILE A O   1 
ATOM   254  C CB  . ILE A 1 35  ? 21.368  -6.084  -25.126 1.00 20.67 ? 35  ILE A CB  1 
ATOM   255  C CG1 . ILE A 1 35  ? 19.869  -5.965  -24.880 1.00 21.26 ? 35  ILE A CG1 1 
ATOM   256  C CG2 . ILE A 1 35  ? 22.058  -4.695  -25.553 1.00 18.71 ? 35  ILE A CG2 1 
ATOM   257  C CD1 . ILE A 1 35  ? 19.454  -4.937  -23.899 1.00 15.97 ? 35  ILE A CD1 1 
ATOM   258  N N   . LYS A 1 36  ? 23.968  -7.313  -27.064 1.00 23.05 ? 36  LYS A N   1 
ATOM   259  C CA  . LYS A 1 36  ? 25.441  -7.472  -27.025 1.00 22.89 ? 36  LYS A CA  1 
ATOM   260  C C   . LYS A 1 36  ? 26.070  -6.099  -27.087 1.00 22.38 ? 36  LYS A C   1 
ATOM   261  O O   . LYS A 1 36  ? 25.346  -5.110  -27.151 1.00 21.83 ? 36  LYS A O   1 
ATOM   262  C CB  . LYS A 1 36  ? 25.894  -8.433  -28.119 1.00 23.45 ? 36  LYS A CB  1 
ATOM   263  C CG  . LYS A 1 36  ? 25.845  -7.935  -29.554 1.00 24.95 ? 36  LYS A CG  1 
ATOM   264  C CD  . LYS A 1 36  ? 25.278  -8.969  -30.496 1.00 27.49 ? 36  LYS A CD  1 
ATOM   265  C CE  . LYS A 1 36  ? 25.972  -8.890  -31.809 1.00 31.38 ? 36  LYS A CE  1 
ATOM   266  N NZ  . LYS A 1 36  ? 25.425  -7.854  -32.710 1.00 31.71 ? 36  LYS A NZ  1 
ATOM   267  N N   . GLY A 1 37  ? 27.391  -6.013  -26.960 1.00 22.64 ? 37  GLY A N   1 
ATOM   268  C CA  . GLY A 1 37  ? 28.143  -4.767  -27.032 1.00 21.48 ? 37  GLY A CA  1 
ATOM   269  C C   . GLY A 1 37  ? 28.235  -3.941  -25.767 1.00 21.93 ? 37  GLY A C   1 
ATOM   270  O O   . GLY A 1 37  ? 28.730  -2.838  -25.764 1.00 20.70 ? 37  GLY A O   1 
ATOM   271  N N   . LEU A 1 38  ? 27.765  -4.513  -24.678 1.00 23.16 ? 38  LEU A N   1 
ATOM   272  C CA  . LEU A 1 38  ? 27.706  -3.879  -23.374 1.00 23.71 ? 38  LEU A CA  1 
ATOM   273  C C   . LEU A 1 38  ? 28.951  -4.156  -22.541 1.00 25.50 ? 38  LEU A C   1 
ATOM   274  O O   . LEU A 1 38  ? 29.561  -5.245  -22.646 1.00 26.21 ? 38  LEU A O   1 
ATOM   275  C CB  . LEU A 1 38  ? 26.531  -4.522  -22.625 1.00 22.99 ? 38  LEU A CB  1 
ATOM   276  C CG  . LEU A 1 38  ? 25.155  -3.844  -22.512 1.00 22.66 ? 38  LEU A CG  1 
ATOM   277  C CD1 . LEU A 1 38  ? 25.045  -2.531  -23.208 1.00 17.18 ? 38  LEU A CD1 1 
ATOM   278  C CD2 . LEU A 1 38  ? 23.977  -4.757  -22.779 1.00 19.26 ? 38  LEU A CD2 1 
ATOM   279  N N   . THR A 1 39  ? 29.321  -3.225  -21.661 1.00 25.83 ? 39  THR A N   1 
ATOM   280  C CA  . THR A 1 39  ? 30.328  -3.587  -20.696 1.00 27.56 ? 39  THR A CA  1 
ATOM   281  C C   . THR A 1 39  ? 29.697  -4.481  -19.622 1.00 28.00 ? 39  THR A C   1 
ATOM   282  O O   . THR A 1 39  ? 28.497  -4.312  -19.285 1.00 26.35 ? 39  THR A O   1 
ATOM   283  C CB  . THR A 1 39  ? 30.924  -2.392  -19.997 1.00 28.65 ? 39  THR A CB  1 
ATOM   284  O OG1 . THR A 1 39  ? 29.929  -1.893  -19.114 1.00 31.21 ? 39  THR A OG1 1 
ATOM   285  C CG2 . THR A 1 39  ? 31.331  -1.323  -20.989 1.00 24.20 ? 39  THR A CG2 1 
ATOM   286  N N   . GLU A 1 40  ? 30.508  -5.415  -19.105 1.00 28.16 ? 40  GLU A N   1 
ATOM   287  C CA  . GLU A 1 40  ? 30.139  -6.306  -18.018 1.00 29.67 ? 40  GLU A CA  1 
ATOM   288  C C   . GLU A 1 40  ? 29.496  -5.527  -16.907 1.00 27.66 ? 40  GLU A C   1 
ATOM   289  O O   . GLU A 1 40  ? 29.912  -4.411  -16.574 1.00 27.90 ? 40  GLU A O   1 
ATOM   290  C CB  . GLU A 1 40  ? 31.389  -6.999  -17.465 1.00 31.00 ? 40  GLU A CB  1 
ATOM   291  C CG  . GLU A 1 40  ? 31.114  -8.193  -16.500 1.00 33.77 ? 40  GLU A CG  1 
ATOM   292  C CD  . GLU A 1 40  ? 32.399  -8.995  -16.186 1.00 34.57 ? 40  GLU A CD  1 
ATOM   293  O OE1 . GLU A 1 40  ? 33.523  -8.439  -16.350 1.00 34.70 ? 40  GLU A OE1 1 
ATOM   294  O OE2 . GLU A 1 40  ? 32.269  -10.191 -15.804 1.00 38.58 ? 40  GLU A OE2 1 
ATOM   295  N N   . GLY A 1 41  ? 28.430  -6.087  -16.356 1.00 27.44 ? 41  GLY A N   1 
ATOM   296  C CA  . GLY A 1 41  ? 27.720  -5.393  -15.317 1.00 25.54 ? 41  GLY A CA  1 
ATOM   297  C C   . GLY A 1 41  ? 26.314  -5.032  -15.699 1.00 25.17 ? 41  GLY A C   1 
ATOM   298  O O   . GLY A 1 41  ? 25.724  -5.561  -16.664 1.00 25.61 ? 41  GLY A O   1 
ATOM   299  N N   . LEU A 1 42  ? 25.786  -4.115  -14.889 1.00 23.86 ? 42  LEU A N   1 
ATOM   300  C CA  . LEU A 1 42  ? 24.392  -3.738  -14.859 1.00 21.53 ? 42  LEU A CA  1 
ATOM   301  C C   . LEU A 1 42  ? 24.174  -2.443  -15.635 1.00 19.56 ? 42  LEU A C   1 
ATOM   302  O O   . LEU A 1 42  ? 25.010  -1.564  -15.609 1.00 18.12 ? 42  LEU A O   1 
ATOM   303  C CB  . LEU A 1 42  ? 23.973  -3.554  -13.381 1.00 22.13 ? 42  LEU A CB  1 
ATOM   304  C CG  . LEU A 1 42  ? 22.977  -4.380  -12.630 1.00 20.08 ? 42  LEU A CG  1 
ATOM   305  C CD1 . LEU A 1 42  ? 22.812  -5.759  -13.132 1.00 26.37 ? 42  LEU A CD1 1 
ATOM   306  C CD2 . LEU A 1 42  ? 23.367  -4.324  -11.190 1.00 25.43 ? 42  LEU A CD2 1 
ATOM   307  N N   . HIS A 1 43  ? 23.045  -2.348  -16.347 1.00 18.13 ? 43  HIS A N   1 
ATOM   308  C CA  . HIS A 1 43  ? 22.738  -1.170  -17.185 1.00 17.52 ? 43  HIS A CA  1 
ATOM   309  C C   . HIS A 1 43  ? 21.245  -0.879  -17.093 1.00 16.97 ? 43  HIS A C   1 
ATOM   310  O O   . HIS A 1 43  ? 20.446  -1.788  -17.254 1.00 16.03 ? 43  HIS A O   1 
ATOM   311  C CB  . HIS A 1 43  ? 23.094  -1.506  -18.656 1.00 17.34 ? 43  HIS A CB  1 
ATOM   312  C CG  . HIS A 1 43  ? 24.537  -1.817  -18.889 1.00 17.25 ? 43  HIS A CG  1 
ATOM   313  N ND1 . HIS A 1 43  ? 25.461  -0.831  -19.184 1.00 15.19 ? 43  HIS A ND1 1 
ATOM   314  C CD2 . HIS A 1 43  ? 25.214  -2.999  -18.915 1.00 13.65 ? 43  HIS A CD2 1 
ATOM   315  C CE1 . HIS A 1 43  ? 26.645  -1.386  -19.365 1.00 15.90 ? 43  HIS A CE1 1 
ATOM   316  N NE2 . HIS A 1 43  ? 26.522  -2.698  -19.224 1.00 15.36 ? 43  HIS A NE2 1 
ATOM   317  N N   . GLY A 1 44  ? 20.871  0.378   -16.871 1.00 17.31 ? 44  GLY A N   1 
ATOM   318  C CA  . GLY A 1 44  ? 19.478  0.806   -16.885 1.00 16.24 ? 44  GLY A CA  1 
ATOM   319  C C   . GLY A 1 44  ? 18.738  0.393   -18.175 1.00 17.90 ? 44  GLY A C   1 
ATOM   320  O O   . GLY A 1 44  ? 19.338  0.418   -19.252 1.00 20.31 ? 44  GLY A O   1 
ATOM   321  N N   . PHE A 1 45  ? 17.467  -0.045  -18.036 1.00 16.39 ? 45  PHE A N   1 
ATOM   322  C CA  . PHE A 1 45  ? 16.613  -0.650  -19.039 1.00 15.18 ? 45  PHE A CA  1 
ATOM   323  C C   . PHE A 1 45  ? 15.276  0.062   -18.788 1.00 15.47 ? 45  PHE A C   1 
ATOM   324  O O   . PHE A 1 45  ? 14.502  -0.280  -17.848 1.00 13.18 ? 45  PHE A O   1 
ATOM   325  C CB  . PHE A 1 45  ? 16.562  -2.171  -18.812 1.00 15.21 ? 45  PHE A CB  1 
ATOM   326  C CG  . PHE A 1 45  ? 15.997  -2.986  -19.958 1.00 17.20 ? 45  PHE A CG  1 
ATOM   327  C CD1 . PHE A 1 45  ? 16.674  -3.101  -21.179 1.00 18.33 ? 45  PHE A CD1 1 
ATOM   328  C CD2 . PHE A 1 45  ? 14.779  -3.677  -19.810 1.00 20.78 ? 45  PHE A CD2 1 
ATOM   329  C CE1 . PHE A 1 45  ? 16.156  -3.895  -22.227 1.00 16.46 ? 45  PHE A CE1 1 
ATOM   330  C CE2 . PHE A 1 45  ? 14.267  -4.502  -20.859 1.00 20.87 ? 45  PHE A CE2 1 
ATOM   331  C CZ  . PHE A 1 45  ? 14.946  -4.564  -22.073 1.00 17.62 ? 45  PHE A CZ  1 
ATOM   332  N N   . HIS A 1 46  ? 15.066  1.156   -19.549 1.00 15.88 ? 46  HIS A N   1 
ATOM   333  C CA  . HIS A 1 46  ? 13.901  2.056   -19.336 1.00 16.22 ? 46  HIS A CA  1 
ATOM   334  C C   . HIS A 1 46  ? 13.051  2.232   -20.567 1.00 16.28 ? 46  HIS A C   1 
ATOM   335  O O   . HIS A 1 46  ? 13.603  2.408   -21.679 1.00 15.79 ? 46  HIS A O   1 
ATOM   336  C CB  . HIS A 1 46  ? 14.399  3.427   -18.908 1.00 16.11 ? 46  HIS A CB  1 
ATOM   337  C CG  . HIS A 1 46  ? 15.180  3.369   -17.651 1.00 20.46 ? 46  HIS A CG  1 
ATOM   338  N ND1 . HIS A 1 46  ? 16.395  3.981   -17.499 1.00 22.85 ? 46  HIS A ND1 1 
ATOM   339  C CD2 . HIS A 1 46  ? 14.952  2.678   -16.504 1.00 21.97 ? 46  HIS A CD2 1 
ATOM   340  C CE1 . HIS A 1 46  ? 16.875  3.676   -16.308 1.00 23.98 ? 46  HIS A CE1 1 
ATOM   341  N NE2 . HIS A 1 46  ? 16.018  2.888   -15.694 1.00 17.01 ? 46  HIS A NE2 1 
ATOM   342  N N   . VAL A 1 47  ? 11.733  2.234   -20.377 1.00 14.18 ? 47  VAL A N   1 
ATOM   343  C CA  . VAL A 1 47  ? 10.853  2.840   -21.367 1.00 15.56 ? 47  VAL A CA  1 
ATOM   344  C C   . VAL A 1 47  ? 10.804  4.423   -21.224 1.00 16.12 ? 47  VAL A C   1 
ATOM   345  O O   . VAL A 1 47  ? 10.444  4.956   -20.174 1.00 14.74 ? 47  VAL A O   1 
ATOM   346  C CB  . VAL A 1 47  ? 9.416   2.206   -21.384 1.00 15.66 ? 47  VAL A CB  1 
ATOM   347  C CG1 . VAL A 1 47  ? 8.607   2.789   -22.589 1.00 18.59 ? 47  VAL A CG1 1 
ATOM   348  C CG2 . VAL A 1 47  ? 9.492   0.694   -21.492 1.00 13.27 ? 47  VAL A CG2 1 
ATOM   349  N N   . HIS A 1 48  ? 11.168  5.128   -22.312 1.00 15.28 ? 48  HIS A N   1 
ATOM   350  C CA  . HIS A 1 48  ? 11.106  6.622   -22.435 1.00 16.14 ? 48  HIS A CA  1 
ATOM   351  C C   . HIS A 1 48  ? 9.918   7.102   -23.205 1.00 16.40 ? 48  HIS A C   1 
ATOM   352  O O   . HIS A 1 48  ? 9.339   6.340   -23.904 1.00 14.82 ? 48  HIS A O   1 
ATOM   353  C CB  . HIS A 1 48  ? 12.420  7.180   -23.068 1.00 14.08 ? 48  HIS A CB  1 
ATOM   354  C CG  . HIS A 1 48  ? 13.617  6.971   -22.178 1.00 14.35 ? 48  HIS A CG  1 
ATOM   355  N ND1 . HIS A 1 48  ? 14.315  8.016   -21.593 1.00 16.11 ? 48  HIS A ND1 1 
ATOM   356  C CD2 . HIS A 1 48  ? 14.166  5.838   -21.681 1.00 20.49 ? 48  HIS A CD2 1 
ATOM   357  C CE1 . HIS A 1 48  ? 15.266  7.532   -20.816 1.00 15.32 ? 48  HIS A CE1 1 
ATOM   358  N NE2 . HIS A 1 48  ? 15.201  6.215   -20.850 1.00 17.78 ? 48  HIS A NE2 1 
ATOM   359  N N   . GLU A 1 49  ? 9.585   8.392   -23.126 1.00 18.65 ? 49  GLU A N   1 
ATOM   360  C CA  . GLU A 1 49  ? 8.232   8.812   -23.498 1.00 20.74 ? 49  GLU A CA  1 
ATOM   361  C C   . GLU A 1 49  ? 7.926   8.757   -25.007 1.00 20.15 ? 49  GLU A C   1 
ATOM   362  O O   . GLU A 1 49  ? 6.779   8.391   -25.427 1.00 18.30 ? 49  GLU A O   1 
ATOM   363  C CB  . GLU A 1 49  ? 7.907   10.197  -22.955 1.00 21.13 ? 49  GLU A CB  1 
ATOM   364  C CG  . GLU A 1 49  ? 6.543   10.635  -23.394 1.00 26.74 ? 49  GLU A CG  1 
ATOM   365  C CD  . GLU A 1 49  ? 6.026   11.793  -22.595 1.00 29.99 ? 49  GLU A CD  1 
ATOM   366  O OE1 . GLU A 1 49  ? 6.799   12.288  -21.750 1.00 35.01 ? 49  GLU A OE1 1 
ATOM   367  O OE2 . GLU A 1 49  ? 4.866   12.183  -22.819 1.00 27.65 ? 49  GLU A OE2 1 
ATOM   368  N N   . PHE A 1 50  ? 8.933   9.111   -25.812 1.00 19.42 ? 50  PHE A N   1 
ATOM   369  C CA  . PHE A 1 50  ? 8.675   9.285   -27.242 1.00 18.13 ? 50  PHE A CA  1 
ATOM   370  C C   . PHE A 1 50  ? 9.389   8.265   -28.093 1.00 17.65 ? 50  PHE A C   1 
ATOM   371  O O   . PHE A 1 50  ? 10.541  7.947   -27.842 1.00 17.38 ? 50  PHE A O   1 
ATOM   372  C CB  . PHE A 1 50  ? 8.980   10.762  -27.710 1.00 19.49 ? 50  PHE A CB  1 
ATOM   373  C CG  . PHE A 1 50  ? 8.315   11.803  -26.857 1.00 17.84 ? 50  PHE A CG  1 
ATOM   374  C CD1 . PHE A 1 50  ? 6.935   11.872  -26.790 1.00 13.58 ? 50  PHE A CD1 1 
ATOM   375  C CD2 . PHE A 1 50  ? 9.074   12.679  -26.103 1.00 23.00 ? 50  PHE A CD2 1 
ATOM   376  C CE1 . PHE A 1 50  ? 6.293   12.803  -25.954 1.00 20.82 ? 50  PHE A CE1 1 
ATOM   377  C CE2 . PHE A 1 50  ? 8.456   13.663  -25.260 1.00 22.67 ? 50  PHE A CE2 1 
ATOM   378  C CZ  . PHE A 1 50  ? 7.052   13.708  -25.177 1.00 21.93 ? 50  PHE A CZ  1 
ATOM   379  N N   . GLY A 1 51  ? 8.691   7.810   -29.129 1.00 16.85 ? 51  GLY A N   1 
ATOM   380  C CA  . GLY A 1 51  ? 9.187   6.957   -30.163 1.00 15.52 ? 51  GLY A CA  1 
ATOM   381  C C   . GLY A 1 51  ? 9.788   7.825   -31.246 1.00 16.73 ? 51  GLY A C   1 
ATOM   382  O O   . GLY A 1 51  ? 9.589   7.557   -32.431 1.00 18.98 ? 51  GLY A O   1 
ATOM   383  N N   . ASP A 1 52  ? 10.510  8.857   -30.831 1.00 18.19 ? 52  ASP A N   1 
ATOM   384  C CA  . ASP A 1 52  ? 11.223  9.816   -31.705 1.00 18.19 ? 52  ASP A CA  1 
ATOM   385  C C   . ASP A 1 52  ? 12.777  9.622   -31.704 1.00 18.61 ? 52  ASP A C   1 
ATOM   386  O O   . ASP A 1 52  ? 13.390  9.658   -30.687 1.00 16.73 ? 52  ASP A O   1 
ATOM   387  C CB  . ASP A 1 52  ? 10.764  11.206  -31.329 1.00 17.68 ? 52  ASP A CB  1 
ATOM   388  C CG  . ASP A 1 52  ? 11.305  12.270  -32.214 1.00 20.76 ? 52  ASP A CG  1 
ATOM   389  O OD1 . ASP A 1 52  ? 12.265  11.971  -33.009 1.00 15.18 ? 52  ASP A OD1 1 
ATOM   390  O OD2 . ASP A 1 52  ? 10.779  13.415  -32.063 1.00 18.50 ? 52  ASP A OD2 1 
ATOM   391  N N   . ASN A 1 53  ? 13.385  9.354   -32.864 1.00 19.90 ? 53  ASN A N   1 
ATOM   392  C CA  . ASN A 1 53  ? 14.800  8.977   -32.957 1.00 21.90 ? 53  ASN A CA  1 
ATOM   393  C C   . ASN A 1 53  ? 15.510  9.890   -33.921 1.00 23.67 ? 53  ASN A C   1 
ATOM   394  O O   . ASN A 1 53  ? 16.597  9.580   -34.393 1.00 24.01 ? 53  ASN A O   1 
ATOM   395  C CB  . ASN A 1 53  ? 15.013  7.516   -33.444 1.00 22.80 ? 53  ASN A CB  1 
ATOM   396  C CG  . ASN A 1 53  ? 16.524  7.043   -33.313 1.00 23.72 ? 53  ASN A CG  1 
ATOM   397  O OD1 . ASN A 1 53  ? 17.135  7.104   -32.224 1.00 26.40 ? 53  ASN A OD1 1 
ATOM   398  N ND2 . ASN A 1 53  ? 17.091  6.576   -34.407 1.00 26.28 ? 53  ASN A ND2 1 
ATOM   399  N N   . ARG A 1 54  ? 14.873  11.027  -34.159 1.00 24.70 ? 54  ARG A N   1 
ATOM   400  C CA  . ARG A 1 54  ? 15.252  12.091  -35.055 1.00 26.40 ? 54  ARG A CA  1 
ATOM   401  C C   . ARG A 1 54  ? 16.688  12.607  -34.916 1.00 27.48 ? 54  ARG A C   1 
ATOM   402  O O   . ARG A 1 54  ? 17.372  12.854  -35.923 1.00 28.48 ? 54  ARG A O   1 
ATOM   403  C CB  . ARG A 1 54  ? 14.335  13.239  -34.683 1.00 26.91 ? 54  ARG A CB  1 
ATOM   404  C CG  . ARG A 1 54  ? 13.889  14.137  -35.777 1.00 26.37 ? 54  ARG A CG  1 
ATOM   405  C CD  . ARG A 1 54  ? 13.107  15.251  -35.150 1.00 23.64 ? 54  ARG A CD  1 
ATOM   406  N NE  . ARG A 1 54  ? 11.866  14.840  -34.422 1.00 25.83 ? 54  ARG A NE  1 
ATOM   407  C CZ  . ARG A 1 54  ? 10.627  15.150  -34.827 1.00 25.95 ? 54  ARG A CZ  1 
ATOM   408  N NH1 . ARG A 1 54  ? 9.523   14.816  -34.094 1.00 21.57 ? 54  ARG A NH1 1 
ATOM   409  N NH2 . ARG A 1 54  ? 10.483  15.774  -36.008 1.00 22.37 ? 54  ARG A NH2 1 
ATOM   410  N N   . ALA A 1 55  ? 17.116  12.805  -33.670 1.00 27.80 ? 55  ALA A N   1 
ATOM   411  C CA  . ALA A 1 55  ? 18.476  13.218  -33.328 1.00 28.56 ? 55  ALA A CA  1 
ATOM   412  C C   . ALA A 1 55  ? 19.135  12.184  -32.386 1.00 28.24 ? 55  ALA A C   1 
ATOM   413  O O   . ALA A 1 55  ? 19.848  12.554  -31.462 1.00 28.92 ? 55  ALA A O   1 
ATOM   414  C CB  . ALA A 1 55  ? 18.472  14.675  -32.721 1.00 27.51 ? 55  ALA A CB  1 
ATOM   415  N N   . GLY A 1 56  ? 18.910  10.884  -32.690 1.00 28.20 ? 56  GLY A N   1 
ATOM   416  C CA  . GLY A 1 56  ? 19.375  9.741   -31.919 1.00 26.44 ? 56  GLY A CA  1 
ATOM   417  C C   . GLY A 1 56  ? 18.498  9.478   -30.698 1.00 26.14 ? 56  GLY A C   1 
ATOM   418  O O   . GLY A 1 56  ? 17.369  9.932   -30.642 1.00 26.58 ? 56  GLY A O   1 
ATOM   419  N N   . CYS A 1 57  ? 19.055  8.786   -29.710 1.00 25.76 ? 57  CYS A N   1 
ATOM   420  C CA  . CYS A 1 57  ? 18.358  8.393   -28.445 1.00 25.20 ? 57  CYS A CA  1 
ATOM   421  C C   . CYS A 1 57  ? 17.911  9.543   -27.541 1.00 24.37 ? 57  CYS A C   1 
ATOM   422  O O   . CYS A 1 57  ? 16.953  9.398   -26.775 1.00 26.09 ? 57  CYS A O   1 
ATOM   423  C CB  . CYS A 1 57  ? 19.187  7.358   -27.654 1.00 23.34 ? 57  CYS A CB  1 
ATOM   424  S SG  . CYS A 1 57  ? 19.392  5.678   -28.474 1.00 28.45 ? 57  CYS A SG  1 
ATOM   425  N N   . THR A 1 58  ? 18.573  10.681  -27.630 1.00 23.77 ? 58  THR A N   1 
ATOM   426  C CA  . THR A 1 58  ? 18.084  11.925  -26.997 1.00 23.45 ? 58  THR A CA  1 
ATOM   427  C C   . THR A 1 58  ? 16.622  12.314  -27.326 1.00 22.11 ? 58  THR A C   1 
ATOM   428  O O   . THR A 1 58  ? 15.879  12.704  -26.404 1.00 22.82 ? 58  THR A O   1 
ATOM   429  C CB  . THR A 1 58  ? 19.022  13.065  -27.332 1.00 22.76 ? 58  THR A CB  1 
ATOM   430  O OG1 . THR A 1 58  ? 20.180  12.925  -26.506 1.00 28.54 ? 58  THR A OG1 1 
ATOM   431  C CG2 . THR A 1 58  ? 18.431  14.352  -26.966 1.00 27.24 ? 58  THR A CG2 1 
ATOM   432  N N   . SER A 1 59  ? 16.203  12.219  -28.606 1.00 20.04 ? 59  SER A N   1 
ATOM   433  C CA  . SER A 1 59  ? 14.812  12.567  -29.012 1.00 19.18 ? 59  SER A CA  1 
ATOM   434  C C   . SER A 1 59  ? 13.630  11.798  -28.369 1.00 19.92 ? 59  SER A C   1 
ATOM   435  O O   . SER A 1 59  ? 12.453  12.237  -28.390 1.00 21.46 ? 59  SER A O   1 
ATOM   436  C CB  . SER A 1 59  ? 14.685  12.478  -30.524 1.00 19.61 ? 59  SER A CB  1 
ATOM   437  O OG  . SER A 1 59  ? 15.849  12.858  -31.186 1.00 19.13 ? 59  SER A OG  1 
ATOM   438  N N   . ALA A 1 60  ? 13.942  10.637  -27.811 1.00 20.67 ? 60  ALA A N   1 
ATOM   439  C CA  . ALA A 1 60  ? 13.047  9.805   -27.002 1.00 20.48 ? 60  ALA A CA  1 
ATOM   440  C C   . ALA A 1 60  ? 12.509  10.561  -25.787 1.00 20.47 ? 60  ALA A C   1 
ATOM   441  O O   . ALA A 1 60  ? 11.478  10.243  -25.247 1.00 17.37 ? 60  ALA A O   1 
ATOM   442  C CB  . ALA A 1 60  ? 13.777  8.613   -26.538 1.00 18.71 ? 60  ALA A CB  1 
ATOM   443  N N   . GLY A 1 61  ? 13.258  11.561  -25.351 1.00 21.76 ? 61  GLY A N   1 
ATOM   444  C CA  . GLY A 1 61  ? 12.875  12.336  -24.171 1.00 23.09 ? 61  GLY A CA  1 
ATOM   445  C C   . GLY A 1 61  ? 12.994  11.632  -22.855 1.00 23.78 ? 61  GLY A C   1 
ATOM   446  O O   . GLY A 1 61  ? 13.878  10.787  -22.620 1.00 26.47 ? 61  GLY A O   1 
ATOM   447  N N   . PRO A 1 62  ? 12.105  11.983  -21.946 1.00 24.56 ? 62  PRO A N   1 
ATOM   448  C CA  . PRO A 1 62  ? 12.196  11.522  -20.608 1.00 23.34 ? 62  PRO A CA  1 
ATOM   449  C C   . PRO A 1 62  ? 11.583  10.154  -20.390 1.00 22.49 ? 62  PRO A C   1 
ATOM   450  O O   . PRO A 1 62  ? 10.967  9.599   -21.289 1.00 21.58 ? 62  PRO A O   1 
ATOM   451  C CB  . PRO A 1 62  ? 11.436  12.621  -19.857 1.00 24.02 ? 62  PRO A CB  1 
ATOM   452  C CG  . PRO A 1 62  ? 10.336  12.912  -20.752 1.00 26.43 ? 62  PRO A CG  1 
ATOM   453  C CD  . PRO A 1 62  ? 11.020  12.961  -22.111 1.00 24.64 ? 62  PRO A CD  1 
ATOM   454  N N   . HIS A 1 63  ? 11.805  9.607   -19.204 1.00 21.16 ? 63  HIS A N   1 
ATOM   455  C CA  . HIS A 1 63  ? 11.163  8.380   -18.742 1.00 21.52 ? 63  HIS A CA  1 
ATOM   456  C C   . HIS A 1 63  ? 9.671   8.451   -19.002 1.00 20.91 ? 63  HIS A C   1 
ATOM   457  O O   . HIS A 1 63  ? 9.067   9.551   -18.943 1.00 21.01 ? 63  HIS A O   1 
ATOM   458  C CB  . HIS A 1 63  ? 11.400  8.162   -17.241 1.00 21.02 ? 63  HIS A CB  1 
ATOM   459  C CG  . HIS A 1 63  ? 12.770  7.648   -16.915 1.00 25.79 ? 63  HIS A CG  1 
ATOM   460  N ND1 . HIS A 1 63  ? 12.994  6.643   -15.991 1.00 29.93 ? 63  HIS A ND1 1 
ATOM   461  C CD2 . HIS A 1 63  ? 13.987  7.992   -17.388 1.00 24.05 ? 63  HIS A CD2 1 
ATOM   462  C CE1 . HIS A 1 63  ? 14.287  6.389   -15.915 1.00 28.69 ? 63  HIS A CE1 1 
ATOM   463  N NE2 . HIS A 1 63  ? 14.912  7.180   -16.764 1.00 27.59 ? 63  HIS A NE2 1 
ATOM   464  N N   . PHE A 1 64  ? 9.095   7.307   -19.334 1.00 18.27 ? 64  PHE A N   1 
ATOM   465  C CA  . PHE A 1 64  ? 7.668   7.277   -19.567 1.00 20.15 ? 64  PHE A CA  1 
ATOM   466  C C   . PHE A 1 64  ? 7.027   7.168   -18.186 1.00 20.43 ? 64  PHE A C   1 
ATOM   467  O O   . PHE A 1 64  ? 7.140   6.128   -17.534 1.00 21.00 ? 64  PHE A O   1 
ATOM   468  C CB  . PHE A 1 64  ? 7.194   6.169   -20.530 1.00 17.72 ? 64  PHE A CB  1 
ATOM   469  C CG  . PHE A 1 64  ? 5.673   6.086   -20.677 1.00 19.74 ? 64  PHE A CG  1 
ATOM   470  C CD1 . PHE A 1 64  ? 4.909   7.246   -20.951 1.00 15.44 ? 64  PHE A CD1 1 
ATOM   471  C CD2 . PHE A 1 64  ? 5.022   4.836   -20.586 1.00 15.10 ? 64  PHE A CD2 1 
ATOM   472  C CE1 . PHE A 1 64  ? 3.560   7.180   -21.063 1.00 19.53 ? 64  PHE A CE1 1 
ATOM   473  C CE2 . PHE A 1 64  ? 3.651   4.741   -20.691 1.00 21.00 ? 64  PHE A CE2 1 
ATOM   474  C CZ  . PHE A 1 64  ? 2.894   5.904   -20.967 1.00 19.42 ? 64  PHE A CZ  1 
ATOM   475  N N   . ASN A 1 65  ? 6.378   8.261   -17.784 1.00 21.79 ? 65  ASN A N   1 
ATOM   476  C CA  . ASN A 1 65  ? 5.932   8.452   -16.398 1.00 23.44 ? 65  ASN A CA  1 
ATOM   477  C C   . ASN A 1 65  ? 4.567   9.157   -16.456 1.00 25.22 ? 65  ASN A C   1 
ATOM   478  O O   . ASN A 1 65  ? 4.462   10.341  -16.073 1.00 27.18 ? 65  ASN A O   1 
ATOM   479  C CB  . ASN A 1 65  ? 6.990   9.270   -15.608 1.00 22.59 ? 65  ASN A CB  1 
ATOM   480  C CG  . ASN A 1 65  ? 6.679   9.390   -14.080 1.00 24.54 ? 65  ASN A CG  1 
ATOM   481  O OD1 . ASN A 1 65  ? 6.052   8.513   -13.464 1.00 25.60 ? 65  ASN A OD1 1 
ATOM   482  N ND2 . ASN A 1 65  ? 7.192   10.445  -13.478 1.00 26.03 ? 65  ASN A ND2 1 
ATOM   483  N N   . PRO A 1 66  ? 3.511   8.450   -16.954 1.00 25.30 ? 66  PRO A N   1 
ATOM   484  C CA  . PRO A 1 66  ? 2.230   9.140   -17.071 1.00 25.75 ? 66  PRO A CA  1 
ATOM   485  C C   . PRO A 1 66  ? 1.614   9.490   -15.715 1.00 27.18 ? 66  PRO A C   1 
ATOM   486  O O   . PRO A 1 66  ? 0.886   10.491  -15.612 1.00 26.96 ? 66  PRO A O   1 
ATOM   487  C CB  . PRO A 1 66  ? 1.324   8.145   -17.796 1.00 25.08 ? 66  PRO A CB  1 
ATOM   488  C CG  . PRO A 1 66  ? 2.002   6.809   -17.628 1.00 25.17 ? 66  PRO A CG  1 
ATOM   489  C CD  . PRO A 1 66  ? 3.434   7.013   -17.320 1.00 23.92 ? 66  PRO A CD  1 
ATOM   490  N N   . LEU A 1 67  ? 1.879   8.669   -14.702 1.00 29.46 ? 67  LEU A N   1 
ATOM   491  C CA  . LEU A 1 67  ? 1.302   8.865   -13.355 1.00 30.62 ? 67  LEU A CA  1 
ATOM   492  C C   . LEU A 1 67  ? 2.084   9.826   -12.458 1.00 30.97 ? 67  LEU A C   1 
ATOM   493  O O   . LEU A 1 67  ? 1.714   10.047  -11.304 1.00 30.98 ? 67  LEU A O   1 
ATOM   494  C CB  . LEU A 1 67  ? 1.101   7.538   -12.659 1.00 29.83 ? 67  LEU A CB  1 
ATOM   495  C CG  . LEU A 1 67  ? 0.024   6.678   -13.242 1.00 31.00 ? 67  LEU A CG  1 
ATOM   496  C CD1 . LEU A 1 67  ? 0.038   5.362   -12.526 1.00 35.63 ? 67  LEU A CD1 1 
ATOM   497  C CD2 . LEU A 1 67  ? -1.296  7.334   -13.072 1.00 34.95 ? 67  LEU A CD2 1 
ATOM   498  N N   . SER A 1 68  ? 3.156   10.402  -13.005 1.00 32.25 ? 68  SER A N   1 
ATOM   499  C CA  . SER A 1 68  ? 3.959   11.435  -12.333 1.00 32.85 ? 68  SER A CA  1 
ATOM   500  C C   . SER A 1 68  ? 4.545   10.987  -10.972 1.00 33.61 ? 68  SER A C   1 
ATOM   501  O O   . SER A 1 68  ? 4.574   11.748  -9.972  1.00 34.21 ? 68  SER A O   1 
ATOM   502  C CB  . SER A 1 68  ? 3.184   12.755  -12.252 1.00 32.19 ? 68  SER A CB  1 
ATOM   503  O OG  . SER A 1 68  ? 2.801   13.184  -13.572 1.00 35.38 ? 68  SER A OG  1 
ATOM   504  N N   . ARG A 1 69  ? 5.029   9.744   -10.961 1.00 32.58 ? 69  ARG A N   1 
ATOM   505  C CA  . ARG A 1 69  ? 5.628   9.166   -9.776  1.00 31.48 ? 69  ARG A CA  1 
ATOM   506  C C   . ARG A 1 69  ? 7.156   9.435   -9.687  1.00 30.98 ? 69  ARG A C   1 
ATOM   507  O O   . ARG A 1 69  ? 7.736   10.043  -10.620 1.00 31.37 ? 69  ARG A O   1 
ATOM   508  C CB  . ARG A 1 69  ? 5.200   7.722   -9.654  1.00 30.88 ? 69  ARG A CB  1 
ATOM   509  C CG  . ARG A 1 69  ? 3.715   7.614   -9.221  1.00 32.47 ? 69  ARG A CG  1 
ATOM   510  C CD  . ARG A 1 69  ? 3.164   6.319   -9.715  1.00 37.28 ? 69  ARG A CD  1 
ATOM   511  N NE  . ARG A 1 69  ? 2.047   5.805   -8.934  1.00 42.78 ? 69  ARG A NE  1 
ATOM   512  C CZ  . ARG A 1 69  ? 2.134   4.708   -8.176  1.00 47.26 ? 69  ARG A CZ  1 
ATOM   513  N NH1 . ARG A 1 69  ? 3.284   4.049   -8.109  1.00 45.93 ? 69  ARG A NH1 1 
ATOM   514  N NH2 . ARG A 1 69  ? 1.086   4.257   -7.492  1.00 50.04 ? 69  ARG A NH2 1 
ATOM   515  N N   . LYS A 1 70  ? 7.791   9.075   -8.558  1.00 29.01 ? 70  LYS A N   1 
ATOM   516  C CA  . LYS A 1 70  ? 9.252   9.209   -8.454  1.00 27.70 ? 70  LYS A CA  1 
ATOM   517  C C   . LYS A 1 70  ? 9.857   7.942   -9.044  1.00 25.15 ? 70  LYS A C   1 
ATOM   518  O O   . LYS A 1 70  ? 9.235   6.925   -9.029  1.00 24.23 ? 70  LYS A O   1 
ATOM   519  C CB  . LYS A 1 70  ? 9.721   9.345   -6.985  1.00 27.53 ? 70  LYS A CB  1 
ATOM   520  C CG  . LYS A 1 70  ? 9.818   10.756  -6.412  1.00 31.26 ? 70  LYS A CG  1 
ATOM   521  C CD  . LYS A 1 70  ? 9.706   10.635  -4.902  1.00 31.49 ? 70  LYS A CD  1 
ATOM   522  C CE  . LYS A 1 70  ? 8.827   9.380   -4.543  1.00 32.78 ? 70  LYS A CE  1 
ATOM   523  N NZ  . LYS A 1 70  ? 8.178   9.230   -3.173  1.00 32.58 ? 70  LYS A NZ  1 
ATOM   524  N N   . HIS A 1 71  ? 11.095  8.013   -9.484  1.00 24.20 ? 71  HIS A N   1 
ATOM   525  C CA  . HIS A 1 71  ? 11.818  6.865   -9.998  1.00 23.06 ? 71  HIS A CA  1 
ATOM   526  C C   . HIS A 1 71  ? 12.066  5.729   -8.940  1.00 23.11 ? 71  HIS A C   1 
ATOM   527  O O   . HIS A 1 71  ? 12.598  5.964   -7.874  1.00 24.01 ? 71  HIS A O   1 
ATOM   528  C CB  . HIS A 1 71  ? 13.143  7.333   -10.641 1.00 20.18 ? 71  HIS A CB  1 
ATOM   529  C CG  . HIS A 1 71  ? 14.008  6.201   -11.109 1.00 22.73 ? 71  HIS A CG  1 
ATOM   530  N ND1 . HIS A 1 71  ? 13.758  5.497   -12.269 1.00 18.57 ? 71  HIS A ND1 1 
ATOM   531  C CD2 . HIS A 1 71  ? 15.052  5.576   -10.510 1.00 20.57 ? 71  HIS A CD2 1 
ATOM   532  C CE1 . HIS A 1 71  ? 14.669  4.548   -12.403 1.00 17.93 ? 71  HIS A CE1 1 
ATOM   533  N NE2 . HIS A 1 71  ? 15.427  4.537   -11.322 1.00 20.51 ? 71  HIS A NE2 1 
ATOM   534  N N   . GLY A 1 72  ? 11.687  4.488   -9.231  1.00 23.01 ? 72  GLY A N   1 
ATOM   535  C CA  . GLY A 1 72  ? 12.203  3.381   -8.440  1.00 20.60 ? 72  GLY A CA  1 
ATOM   536  C C   . GLY A 1 72  ? 12.544  2.194   -9.284  1.00 21.73 ? 72  GLY A C   1 
ATOM   537  O O   . GLY A 1 72  ? 12.902  2.303   -10.478 1.00 22.84 ? 72  GLY A O   1 
ATOM   538  N N   . GLY A 1 73  ? 12.429  1.023   -8.684  1.00 22.21 ? 73  GLY A N   1 
ATOM   539  C CA  . GLY A 1 73  ? 12.714  -0.210  -9.365  1.00 23.18 ? 73  GLY A CA  1 
ATOM   540  C C   . GLY A 1 73  ? 11.376  -0.753  -9.778  1.00 23.82 ? 73  GLY A C   1 
ATOM   541  O O   . GLY A 1 73  ? 10.335  -0.204  -9.375  1.00 23.03 ? 73  GLY A O   1 
ATOM   542  N N   . PRO A 1 74  ? 11.390  -1.788  -10.641 1.00 25.75 ? 74  PRO A N   1 
ATOM   543  C CA  . PRO A 1 74  ? 10.155  -2.407  -11.189 1.00 26.47 ? 74  PRO A CA  1 
ATOM   544  C C   . PRO A 1 74  ? 9.215   -3.018  -10.123 1.00 27.86 ? 74  PRO A C   1 
ATOM   545  O O   . PRO A 1 74  ? 8.000   -3.056  -10.331 1.00 26.19 ? 74  PRO A O   1 
ATOM   546  C CB  . PRO A 1 74  ? 10.692  -3.446  -12.186 1.00 26.06 ? 74  PRO A CB  1 
ATOM   547  C CG  . PRO A 1 74  ? 12.109  -3.662  -11.778 1.00 24.61 ? 74  PRO A CG  1 
ATOM   548  C CD  . PRO A 1 74  ? 12.606  -2.372  -11.246 1.00 24.59 ? 74  PRO A CD  1 
ATOM   549  N N   . LYS A 1 75  ? 9.809   -3.473  -9.015  1.00 31.10 ? 75  LYS A N   1 
ATOM   550  C CA  . LYS A 1 75  ? 9.140   -4.144  -7.892  1.00 33.77 ? 75  LYS A CA  1 
ATOM   551  C C   . LYS A 1 75  ? 8.511   -3.151  -6.978  1.00 33.42 ? 75  LYS A C   1 
ATOM   552  O O   . LYS A 1 75  ? 7.545   -3.464  -6.309  1.00 34.65 ? 75  LYS A O   1 
ATOM   553  C CB  . LYS A 1 75  ? 10.113  -5.017  -7.082  1.00 33.96 ? 75  LYS A CB  1 
ATOM   554  C CG  . LYS A 1 75  ? 10.408  -6.434  -7.661  1.00 37.55 ? 75  LYS A CG  1 
ATOM   555  C CD  . LYS A 1 75  ? 11.424  -7.201  -6.763  1.00 37.07 ? 75  LYS A CD  1 
ATOM   556  C CE  . LYS A 1 75  ? 11.054  -8.719  -6.636  1.00 43.76 ? 75  LYS A CE  1 
ATOM   557  N NZ  . LYS A 1 75  ? 10.201  -9.128  -5.413  1.00 42.58 ? 75  LYS A NZ  1 
ATOM   558  N N   . ASP A 1 76  ? 9.048   -1.935  -6.980  1.00 34.05 ? 76  ASP A N   1 
ATOM   559  C CA  . ASP A 1 76  ? 8.466   -0.825  -6.212  1.00 34.23 ? 76  ASP A CA  1 
ATOM   560  C C   . ASP A 1 76  ? 7.060   -0.354  -6.655  1.00 34.32 ? 76  ASP A C   1 
ATOM   561  O O   . ASP A 1 76  ? 6.743   -0.322  -7.859  1.00 33.62 ? 76  ASP A O   1 
ATOM   562  C CB  . ASP A 1 76  ? 9.377   0.381   -6.264  1.00 33.24 ? 76  ASP A CB  1 
ATOM   563  C CG  . ASP A 1 76  ? 10.715  0.124   -5.673  1.00 36.47 ? 76  ASP A CG  1 
ATOM   564  O OD1 . ASP A 1 76  ? 10.920  -0.892  -4.969  1.00 38.02 ? 76  ASP A OD1 1 
ATOM   565  O OD2 . ASP A 1 76  ? 11.578  0.998   -5.878  1.00 39.80 ? 76  ASP A OD2 1 
ATOM   566  N N   . GLU A 1 77  ? 6.270   0.105   -5.673  1.00 33.24 ? 77  GLU A N   1 
ATOM   567  C CA  . GLU A 1 77  ? 4.956   0.685   -5.950  1.00 33.11 ? 77  GLU A CA  1 
ATOM   568  C C   . GLU A 1 77  ? 5.194   2.085   -6.471  1.00 31.40 ? 77  GLU A C   1 
ATOM   569  O O   . GLU A 1 77  ? 4.558   2.519   -7.425  1.00 32.61 ? 77  GLU A O   1 
ATOM   570  C CB  . GLU A 1 77  ? 4.009   0.600   -4.712  1.00 33.48 ? 77  GLU A CB  1 
ATOM   571  C CG  . GLU A 1 77  ? 2.891   1.674   -4.636  1.00 40.28 ? 77  GLU A CG  1 
ATOM   572  C CD  . GLU A 1 77  ? 1.615   1.285   -5.358  1.00 46.31 ? 77  GLU A CD  1 
ATOM   573  O OE1 . GLU A 1 77  ? 1.628   0.253   -6.087  1.00 49.22 ? 77  GLU A OE1 1 
ATOM   574  O OE2 . GLU A 1 77  ? 0.588   2.015   -5.193  1.00 50.34 ? 77  GLU A OE2 1 
ATOM   575  N N   . GLU A 1 78  ? 6.175   2.770   -5.904  1.00 29.81 ? 78  GLU A N   1 
ATOM   576  C CA  . GLU A 1 78  ? 6.555   4.085   -6.359  1.00 27.43 ? 78  GLU A CA  1 
ATOM   577  C C   . GLU A 1 78  ? 7.625   3.969   -7.469  1.00 24.94 ? 78  GLU A C   1 
ATOM   578  O O   . GLU A 1 78  ? 8.788   3.627   -7.208  1.00 23.49 ? 78  GLU A O   1 
ATOM   579  C CB  . GLU A 1 78  ? 7.068   4.893   -5.180  1.00 28.27 ? 78  GLU A CB  1 
ATOM   580  C CG  . GLU A 1 78  ? 6.948   6.406   -5.392  1.00 31.46 ? 78  GLU A CG  1 
ATOM   581  C CD  . GLU A 1 78  ? 5.491   6.858   -5.554  1.00 35.98 ? 78  GLU A CD  1 
ATOM   582  O OE1 . GLU A 1 78  ? 4.522   6.119   -5.169  1.00 38.12 ? 78  GLU A OE1 1 
ATOM   583  O OE2 . GLU A 1 78  ? 5.332   7.949   -6.115  1.00 35.71 ? 78  GLU A OE2 1 
ATOM   584  N N   . ARG A 1 79  ? 7.216   4.249   -8.706  1.00 22.33 ? 79  ARG A N   1 
ATOM   585  C CA  . ARG A 1 79  ? 8.060   3.965   -9.890  1.00 20.76 ? 79  ARG A CA  1 
ATOM   586  C C   . ARG A 1 79  ? 7.407   4.606   -11.081 1.00 20.82 ? 79  ARG A C   1 
ATOM   587  O O   . ARG A 1 79  ? 6.193   4.950   -11.049 1.00 20.77 ? 79  ARG A O   1 
ATOM   588  C CB  . ARG A 1 79  ? 8.203   2.418   -10.092 1.00 19.25 ? 79  ARG A CB  1 
ATOM   589  C CG  . ARG A 1 79  ? 6.928   1.748   -10.612 1.00 19.31 ? 79  ARG A CG  1 
ATOM   590  C CD  . ARG A 1 79  ? 7.150   0.314   -11.153 1.00 16.54 ? 79  ARG A CD  1 
ATOM   591  N NE  . ARG A 1 79  ? 7.246   0.300   -12.647 1.00 13.19 ? 79  ARG A NE  1 
ATOM   592  C CZ  . ARG A 1 79  ? 7.300   -0.799  -13.379 1.00 16.90 ? 79  ARG A CZ  1 
ATOM   593  N NH1 . ARG A 1 79  ? 7.301   -2.006  -12.763 1.00 8.11  ? 79  ARG A NH1 1 
ATOM   594  N NH2 . ARG A 1 79  ? 7.353   -0.702  -14.720 1.00 16.68 ? 79  ARG A NH2 1 
ATOM   595  N N   . HIS A 1 80  ? 8.174   4.778   -12.149 1.00 21.71 ? 80  HIS A N   1 
ATOM   596  C CA  . HIS A 1 80  ? 7.575   5.228   -13.454 1.00 21.45 ? 80  HIS A CA  1 
ATOM   597  C C   . HIS A 1 80  ? 7.030   4.007   -14.112 1.00 19.69 ? 80  HIS A C   1 
ATOM   598  O O   . HIS A 1 80  ? 7.551   2.905   -13.907 1.00 18.75 ? 80  HIS A O   1 
ATOM   599  C CB  . HIS A 1 80  ? 8.638   5.873   -14.396 1.00 22.29 ? 80  HIS A CB  1 
ATOM   600  C CG  . HIS A 1 80  ? 9.420   6.984   -13.774 1.00 24.51 ? 80  HIS A CG  1 
ATOM   601  N ND1 . HIS A 1 80  ? 10.648  7.379   -14.259 1.00 25.20 ? 80  HIS A ND1 1 
ATOM   602  C CD2 . HIS A 1 80  ? 9.162   7.777   -12.707 1.00 22.67 ? 80  HIS A CD2 1 
ATOM   603  C CE1 . HIS A 1 80  ? 11.090  8.401   -13.546 1.00 22.36 ? 80  HIS A CE1 1 
ATOM   604  N NE2 . HIS A 1 80  ? 10.210  8.656   -12.592 1.00 21.15 ? 80  HIS A NE2 1 
ATOM   605  N N   . VAL A 1 81  ? 5.990   4.173   -14.919 1.00 20.98 ? 81  VAL A N   1 
ATOM   606  C CA  . VAL A 1 81  ? 5.563   3.061   -15.870 1.00 19.14 ? 81  VAL A CA  1 
ATOM   607  C C   . VAL A 1 81  ? 6.792   2.465   -16.583 1.00 19.59 ? 81  VAL A C   1 
ATOM   608  O O   . VAL A 1 81  ? 7.021   1.246   -16.578 1.00 19.09 ? 81  VAL A O   1 
ATOM   609  C CB  . VAL A 1 81  ? 4.471   3.511   -16.868 1.00 18.89 ? 81  VAL A CB  1 
ATOM   610  C CG1 . VAL A 1 81  ? 4.112   2.350   -17.871 1.00 19.74 ? 81  VAL A CG1 1 
ATOM   611  C CG2 . VAL A 1 81  ? 3.242   3.865   -16.089 1.00 16.58 ? 81  VAL A CG2 1 
ATOM   612  N N   . GLY A 1 82  ? 7.640   3.322   -17.100 1.00 18.90 ? 82  GLY A N   1 
ATOM   613  C CA  . GLY A 1 82  ? 8.829   2.822   -17.764 1.00 20.60 ? 82  GLY A CA  1 
ATOM   614  C C   . GLY A 1 82  ? 10.029  2.364   -16.961 1.00 21.06 ? 82  GLY A C   1 
ATOM   615  O O   . GLY A 1 82  ? 11.111  2.229   -17.539 1.00 21.27 ? 82  GLY A O   1 
ATOM   616  N N   . ASP A 1 83  ? 9.865   2.089   -15.655 1.00 20.10 ? 83  ASP A N   1 
ATOM   617  C CA  . ASP A 1 83  ? 10.998  1.714   -14.844 1.00 18.98 ? 83  ASP A CA  1 
ATOM   618  C C   . ASP A 1 83  ? 11.227  0.190   -14.884 1.00 19.51 ? 83  ASP A C   1 
ATOM   619  O O   . ASP A 1 83  ? 10.685  -0.488  -14.059 1.00 19.77 ? 83  ASP A O   1 
ATOM   620  C CB  . ASP A 1 83  ? 10.832  2.177   -13.382 1.00 20.22 ? 83  ASP A CB  1 
ATOM   621  C CG  . ASP A 1 83  ? 11.167  3.621   -13.168 1.00 16.51 ? 83  ASP A CG  1 
ATOM   622  O OD1 . ASP A 1 83  ? 11.676  4.277   -14.092 1.00 18.55 ? 83  ASP A OD1 1 
ATOM   623  O OD2 . ASP A 1 83  ? 10.922  4.107   -12.055 1.00 16.30 ? 83  ASP A OD2 1 
ATOM   624  N N   . LEU A 1 84  ? 12.004  -0.343  -15.845 1.00 18.39 ? 84  LEU A N   1 
ATOM   625  C CA  . LEU A 1 84  ? 12.198  -1.795  -15.939 1.00 18.45 ? 84  LEU A CA  1 
ATOM   626  C C   . LEU A 1 84  ? 13.475  -2.315  -15.264 1.00 18.50 ? 84  LEU A C   1 
ATOM   627  O O   . LEU A 1 84  ? 13.826  -3.532  -15.390 1.00 15.26 ? 84  LEU A O   1 
ATOM   628  C CB  . LEU A 1 84  ? 12.094  -2.272  -17.395 1.00 18.51 ? 84  LEU A CB  1 
ATOM   629  C CG  . LEU A 1 84  ? 10.689  -2.015  -17.943 1.00 18.24 ? 84  LEU A CG  1 
ATOM   630  C CD1 . LEU A 1 84  ? 10.673  -2.178  -19.434 1.00 16.84 ? 84  LEU A CD1 1 
ATOM   631  C CD2 . LEU A 1 84  ? 9.520   -2.745  -17.163 1.00 14.80 ? 84  LEU A CD2 1 
ATOM   632  N N   . GLY A 1 85  ? 14.136  -1.392  -14.518 1.00 15.90 ? 85  GLY A N   1 
ATOM   633  C CA  . GLY A 1 85  ? 15.259  -1.781  -13.683 1.00 16.36 ? 85  GLY A CA  1 
ATOM   634  C C   . GLY A 1 85  ? 16.538  -1.840  -14.479 1.00 16.55 ? 85  GLY A C   1 
ATOM   635  O O   . GLY A 1 85  ? 16.886  -0.862  -15.138 1.00 18.54 ? 85  GLY A O   1 
ATOM   636  N N   . ASN A 1 86  ? 17.202  -2.999  -14.442 1.00 17.37 ? 86  ASN A N   1 
ATOM   637  C CA  . ASN A 1 86  ? 18.522  -3.238  -15.030 1.00 17.12 ? 86  ASN A CA  1 
ATOM   638  C C   . ASN A 1 86  ? 18.552  -4.602  -15.713 1.00 18.11 ? 86  ASN A C   1 
ATOM   639  O O   . ASN A 1 86  ? 17.859  -5.553  -15.295 1.00 19.60 ? 86  ASN A O   1 
ATOM   640  C CB  . ASN A 1 86  ? 19.644  -3.241  -13.952 1.00 16.68 ? 86  ASN A CB  1 
ATOM   641  C CG  . ASN A 1 86  ? 19.962  -1.858  -13.336 1.00 18.29 ? 86  ASN A CG  1 
ATOM   642  O OD1 . ASN A 1 86  ? 20.485  -0.987  -13.981 1.00 14.81 ? 86  ASN A OD1 1 
ATOM   643  N ND2 . ASN A 1 86  ? 19.744  -1.726  -12.013 1.00 23.68 ? 86  ASN A ND2 1 
ATOM   644  N N   . VAL A 1 87  ? 19.343  -4.689  -16.774 1.00 18.80 ? 87  VAL A N   1 
ATOM   645  C CA  . VAL A 1 87  ? 19.771  -5.975  -17.391 1.00 20.45 ? 87  VAL A CA  1 
ATOM   646  C C   . VAL A 1 87  ? 21.249  -6.173  -17.111 1.00 20.27 ? 87  VAL A C   1 
ATOM   647  O O   . VAL A 1 87  ? 21.973  -5.231  -16.812 1.00 20.20 ? 87  VAL A O   1 
ATOM   648  C CB  . VAL A 1 87  ? 19.530  -6.018  -18.954 1.00 20.28 ? 87  VAL A CB  1 
ATOM   649  C CG1 . VAL A 1 87  ? 18.091  -5.761  -19.255 1.00 16.67 ? 87  VAL A CG1 1 
ATOM   650  C CG2 . VAL A 1 87  ? 20.509  -5.043  -19.688 1.00 18.48 ? 87  VAL A CG2 1 
ATOM   651  N N   . THR A 1 88  ? 21.686  -7.413  -17.169 1.00 22.61 ? 88  THR A N   1 
ATOM   652  C CA  . THR A 1 88  ? 23.024  -7.729  -16.693 1.00 23.06 ? 88  THR A CA  1 
ATOM   653  C C   . THR A 1 88  ? 23.867  -8.255  -17.859 1.00 24.10 ? 88  THR A C   1 
ATOM   654  O O   . THR A 1 88  ? 23.562  -9.298  -18.453 1.00 23.48 ? 88  THR A O   1 
ATOM   655  C CB  . THR A 1 88  ? 23.010  -8.714  -15.484 1.00 23.01 ? 88  THR A CB  1 
ATOM   656  O OG1 . THR A 1 88  ? 22.121  -8.226  -14.453 1.00 23.83 ? 88  THR A OG1 1 
ATOM   657  C CG2 . THR A 1 88  ? 24.458  -8.906  -14.931 1.00 20.75 ? 88  THR A CG2 1 
ATOM   658  N N   . ALA A 1 89  ? 24.919  -7.505  -18.204 1.00 24.38 ? 89  ALA A N   1 
ATOM   659  C CA  . ALA A 1 89  ? 25.832  -7.981  -19.254 1.00 24.63 ? 89  ALA A CA  1 
ATOM   660  C C   . ALA A 1 89  ? 26.857  -8.875  -18.608 1.00 25.41 ? 89  ALA A C   1 
ATOM   661  O O   . ALA A 1 89  ? 27.436  -8.501  -17.586 1.00 25.16 ? 89  ALA A O   1 
ATOM   662  C CB  . ALA A 1 89  ? 26.514  -6.800  -19.981 1.00 23.52 ? 89  ALA A CB  1 
ATOM   663  N N   . ASP A 1 90  ? 27.063  -10.046 -19.193 1.00 27.35 ? 90  ASP A N   1 
ATOM   664  C CA  . ASP A 1 90  ? 28.143  -10.971 -18.803 1.00 29.66 ? 90  ASP A CA  1 
ATOM   665  C C   . ASP A 1 90  ? 29.516  -10.403 -19.236 1.00 30.67 ? 90  ASP A C   1 
ATOM   666  O O   . ASP A 1 90  ? 29.573  -9.290  -19.748 1.00 29.66 ? 90  ASP A O   1 
ATOM   667  C CB  . ASP A 1 90  ? 27.904  -12.416 -19.359 1.00 29.50 ? 90  ASP A CB  1 
ATOM   668  C CG  . ASP A 1 90  ? 28.067  -12.524 -20.891 1.00 29.99 ? 90  ASP A CG  1 
ATOM   669  O OD1 . ASP A 1 90  ? 28.668  -11.621 -21.506 1.00 31.87 ? 90  ASP A OD1 1 
ATOM   670  O OD2 . ASP A 1 90  ? 27.625  -13.537 -21.497 1.00 30.97 ? 90  ASP A OD2 1 
ATOM   671  N N   . LYS A 1 91  ? 30.585  -11.189 -19.043 1.00 32.15 ? 91  LYS A N   1 
ATOM   672  C CA  . LYS A 1 91  ? 31.977  -10.767 -19.222 1.00 33.45 ? 91  LYS A CA  1 
ATOM   673  C C   . LYS A 1 91  ? 32.327  -10.523 -20.675 1.00 33.94 ? 91  LYS A C   1 
ATOM   674  O O   . LYS A 1 91  ? 33.187  -9.682  -20.970 1.00 33.41 ? 91  LYS A O   1 
ATOM   675  C CB  . LYS A 1 91  ? 32.952  -11.812 -18.620 1.00 35.51 ? 91  LYS A CB  1 
ATOM   676  C CG  . LYS A 1 91  ? 32.935  -13.226 -19.324 1.00 35.69 ? 91  LYS A CG  1 
ATOM   677  C CD  . LYS A 1 91  ? 33.068  -14.371 -18.336 1.00 41.83 ? 91  LYS A CD  1 
ATOM   678  C CE  . LYS A 1 91  ? 32.912  -15.760 -19.018 1.00 41.63 ? 91  LYS A CE  1 
ATOM   679  N NZ  . LYS A 1 91  ? 34.258  -16.259 -19.521 1.00 44.58 ? 91  LYS A NZ  1 
ATOM   680  N N   . ASP A 1 92  ? 31.635  -11.263 -21.551 1.00 33.59 ? 92  ASP A N   1 
ATOM   681  C CA  . ASP A 1 92  ? 31.669  -11.140 -23.008 1.00 33.51 ? 92  ASP A CA  1 
ATOM   682  C C   . ASP A 1 92  ? 30.739  -10.031 -23.547 1.00 33.39 ? 92  ASP A C   1 
ATOM   683  O O   . ASP A 1 92  ? 30.519  -9.986  -24.765 1.00 33.56 ? 92  ASP A O   1 
ATOM   684  C CB  . ASP A 1 92  ? 31.174  -12.447 -23.657 1.00 33.57 ? 92  ASP A CB  1 
ATOM   685  C CG  . ASP A 1 92  ? 31.987  -13.685 -23.237 1.00 36.51 ? 92  ASP A CG  1 
ATOM   686  O OD1 . ASP A 1 92  ? 33.227  -13.620 -23.291 1.00 38.53 ? 92  ASP A OD1 1 
ATOM   687  O OD2 . ASP A 1 92  ? 31.382  -14.741 -22.883 1.00 40.89 ? 92  ASP A OD2 1 
ATOM   688  N N   . GLY A 1 93  ? 30.177  -9.191  -22.663 1.00 31.53 ? 93  GLY A N   1 
ATOM   689  C CA  . GLY A 1 93  ? 29.236  -8.134  -23.037 1.00 29.40 ? 93  GLY A CA  1 
ATOM   690  C C   . GLY A 1 93  ? 27.815  -8.502  -23.460 1.00 28.36 ? 93  GLY A C   1 
ATOM   691  O O   . GLY A 1 93  ? 27.122  -7.671  -24.008 1.00 27.96 ? 93  GLY A O   1 
ATOM   692  N N   . VAL A 1 94  ? 27.372  -9.734  -23.189 1.00 27.55 ? 94  VAL A N   1 
ATOM   693  C CA  . VAL A 1 94  ? 26.066  -10.166 -23.598 1.00 28.13 ? 94  VAL A CA  1 
ATOM   694  C C   . VAL A 1 94  ? 25.066  -10.121 -22.414 1.00 29.56 ? 94  VAL A C   1 
ATOM   695  O O   . VAL A 1 94  ? 25.339  -10.655 -21.304 1.00 29.72 ? 94  VAL A O   1 
ATOM   696  C CB  . VAL A 1 94  ? 26.068  -11.563 -24.323 1.00 28.84 ? 94  VAL A CB  1 
ATOM   697  C CG1 . VAL A 1 94  ? 24.669  -12.015 -24.735 1.00 26.01 ? 94  VAL A CG1 1 
ATOM   698  C CG2 . VAL A 1 94  ? 27.001  -11.539 -25.560 1.00 27.28 ? 94  VAL A CG2 1 
ATOM   699  N N   . ALA A 1 95  ? 23.921  -9.490  -22.685 1.00 28.48 ? 95  ALA A N   1 
ATOM   700  C CA  . ALA A 1 95  ? 22.821  -9.374  -21.721 1.00 29.52 ? 95  ALA A CA  1 
ATOM   701  C C   . ALA A 1 95  ? 21.593  -10.147 -22.155 1.00 30.00 ? 95  ALA A C   1 
ATOM   702  O O   . ALA A 1 95  ? 20.773  -9.669  -22.947 1.00 29.02 ? 95  ALA A O   1 
ATOM   703  C CB  . ALA A 1 95  ? 22.464  -7.893  -21.504 1.00 29.01 ? 95  ALA A CB  1 
ATOM   704  N N   . ASP A 1 96  ? 21.457  -11.339 -21.607 1.00 31.06 ? 96  ASP A N   1 
ATOM   705  C CA  . ASP A 1 96  ? 20.228  -12.108 -21.625 1.00 32.46 ? 96  ASP A CA  1 
ATOM   706  C C   . ASP A 1 96  ? 19.064  -11.472 -20.864 1.00 31.59 ? 96  ASP A C   1 
ATOM   707  O O   . ASP A 1 96  ? 19.090  -11.389 -19.667 1.00 33.29 ? 96  ASP A O   1 
ATOM   708  C CB  . ASP A 1 96  ? 20.536  -13.432 -20.930 1.00 34.41 ? 96  ASP A CB  1 
ATOM   709  C CG  . ASP A 1 96  ? 19.493  -14.493 -21.184 1.00 37.99 ? 96  ASP A CG  1 
ATOM   710  O OD1 . ASP A 1 96  ? 19.105  -14.658 -22.363 1.00 40.34 ? 96  ASP A OD1 1 
ATOM   711  O OD2 . ASP A 1 96  ? 19.118  -15.206 -20.202 1.00 44.84 ? 96  ASP A OD2 1 
ATOM   712  N N   . VAL A 1 97  ? 18.009  -11.053 -21.550 1.00 31.16 ? 97  VAL A N   1 
ATOM   713  C CA  . VAL A 1 97  ? 16.863  -10.402 -20.884 1.00 28.49 ? 97  VAL A CA  1 
ATOM   714  C C   . VAL A 1 97  ? 15.726  -11.378 -20.710 1.00 30.54 ? 97  VAL A C   1 
ATOM   715  O O   . VAL A 1 97  ? 15.405  -12.131 -21.635 1.00 30.40 ? 97  VAL A O   1 
ATOM   716  C CB  . VAL A 1 97  ? 16.467  -9.080  -21.626 1.00 28.47 ? 97  VAL A CB  1 
ATOM   717  C CG1 . VAL A 1 97  ? 15.340  -8.328  -20.894 1.00 21.55 ? 97  VAL A CG1 1 
ATOM   718  C CG2 . VAL A 1 97  ? 17.736  -8.217  -21.799 1.00 21.47 ? 97  VAL A CG2 1 
ATOM   719  N N   . SER A 1 98  ? 15.223  -11.477 -19.477 1.00 31.70 ? 98  SER A N   1 
ATOM   720  C CA  . SER A 1 98  ? 13.917  -12.108 -19.218 1.00 33.37 ? 98  SER A CA  1 
ATOM   721  C C   . SER A 1 98  ? 13.301  -11.349 -18.027 1.00 34.02 ? 98  SER A C   1 
ATOM   722  O O   . SER A 1 98  ? 13.977  -11.064 -17.046 1.00 35.88 ? 98  SER A O   1 
ATOM   723  C CB  . SER A 1 98  ? 14.025  -13.640 -19.016 1.00 33.98 ? 98  SER A CB  1 
ATOM   724  O OG  . SER A 1 98  ? 12.994  -14.366 -19.735 1.00 33.75 ? 98  SER A OG  1 
ATOM   725  N N   . ILE A 1 99  ? 12.056  -10.920 -18.166 1.00 34.28 ? 99  ILE A N   1 
ATOM   726  C CA  . ILE A 1 99  ? 11.445  -9.887  -17.324 1.00 32.81 ? 99  ILE A CA  1 
ATOM   727  C C   . ILE A 1 99  ? 9.972   -10.258 -17.495 1.00 32.36 ? 99  ILE A C   1 
ATOM   728  O O   . ILE A 1 99  ? 9.530   -10.705 -18.591 1.00 31.46 ? 99  ILE A O   1 
ATOM   729  C CB  . ILE A 1 99  ? 11.740  -8.392  -17.839 1.00 33.34 ? 99  ILE A CB  1 
ATOM   730  C CG1 . ILE A 1 99  ? 13.176  -7.926  -17.535 1.00 36.95 ? 99  ILE A CG1 1 
ATOM   731  C CG2 . ILE A 1 99  ? 10.830  -7.351  -17.243 1.00 32.56 ? 99  ILE A CG2 1 
ATOM   732  C CD1 . ILE A 1 99  ? 13.557  -6.439  -17.953 1.00 33.90 ? 99  ILE A CD1 1 
ATOM   733  N N   . GLU A 1 100 ? 9.216   -10.130 -16.413 1.00 31.36 ? 100 GLU A N   1 
ATOM   734  C CA  . GLU A 1 100 ? 7.795   -10.063 -16.503 1.00 30.13 ? 100 GLU A CA  1 
ATOM   735  C C   . GLU A 1 100 ? 7.464   -8.742  -15.854 1.00 28.89 ? 100 GLU A C   1 
ATOM   736  O O   . GLU A 1 100 ? 7.959   -8.462  -14.744 1.00 27.88 ? 100 GLU A O   1 
ATOM   737  C CB  . GLU A 1 100 ? 7.205   -11.188 -15.703 1.00 31.31 ? 100 GLU A CB  1 
ATOM   738  C CG  . GLU A 1 100 ? 5.807   -11.629 -16.137 1.00 36.29 ? 100 GLU A CG  1 
ATOM   739  C CD  . GLU A 1 100 ? 5.483   -13.030 -15.623 1.00 40.69 ? 100 GLU A CD  1 
ATOM   740  O OE1 . GLU A 1 100 ? 5.743   -13.986 -16.387 1.00 43.48 ? 100 GLU A OE1 1 
ATOM   741  O OE2 . GLU A 1 100 ? 4.998   -13.168 -14.467 1.00 42.15 ? 100 GLU A OE2 1 
ATOM   742  N N   . ASP A 1 101 ? 6.674   -7.903  -16.533 1.00 27.25 ? 101 ASP A N   1 
ATOM   743  C CA  . ASP A 1 101 ? 6.162   -6.688  -15.869 1.00 26.72 ? 101 ASP A CA  1 
ATOM   744  C C   . ASP A 1 101 ? 4.618   -6.514  -15.884 1.00 25.73 ? 101 ASP A C   1 
ATOM   745  O O   . ASP A 1 101 ? 3.953   -6.695  -16.883 1.00 24.52 ? 101 ASP A O   1 
ATOM   746  C CB  . ASP A 1 101 ? 6.835   -5.468  -16.445 1.00 26.45 ? 101 ASP A CB  1 
ATOM   747  C CG  . ASP A 1 101 ? 6.742   -4.265  -15.536 1.00 26.76 ? 101 ASP A CG  1 
ATOM   748  O OD1 . ASP A 1 101 ? 7.505   -4.163  -14.541 1.00 33.66 ? 101 ASP A OD1 1 
ATOM   749  O OD2 . ASP A 1 101 ? 5.943   -3.381  -15.831 1.00 25.13 ? 101 ASP A OD2 1 
ATOM   750  N N   . SER A 1 102 ? 4.078   -6.070  -14.775 1.00 26.39 ? 102 SER A N   1 
ATOM   751  C CA  . SER A 1 102 ? 2.647   -5.829  -14.644 1.00 26.70 ? 102 SER A CA  1 
ATOM   752  C C   . SER A 1 102 ? 2.231   -4.357  -14.660 1.00 25.87 ? 102 SER A C   1 
ATOM   753  O O   . SER A 1 102 ? 1.055   -4.072  -14.405 1.00 27.08 ? 102 SER A O   1 
ATOM   754  C CB  . SER A 1 102 ? 2.137   -6.427  -13.338 1.00 27.70 ? 102 SER A CB  1 
ATOM   755  O OG  . SER A 1 102 ? 1.628   -7.728  -13.603 1.00 33.11 ? 102 SER A OG  1 
ATOM   756  N N   . VAL A 1 103 ? 3.149   -3.448  -14.965 1.00 23.56 ? 103 VAL A N   1 
ATOM   757  C CA  . VAL A 1 103 ? 2.869   -2.002  -14.907 1.00 23.35 ? 103 VAL A CA  1 
ATOM   758  C C   . VAL A 1 103 ? 2.828   -1.414  -16.333 1.00 22.76 ? 103 VAL A C   1 
ATOM   759  O O   . VAL A 1 103 ? 1.800   -0.850  -16.812 1.00 24.01 ? 103 VAL A O   1 
ATOM   760  C CB  . VAL A 1 103 ? 3.864   -1.264  -13.940 1.00 22.95 ? 103 VAL A CB  1 
ATOM   761  C CG1 . VAL A 1 103 ? 3.664   0.280   -13.993 1.00 20.83 ? 103 VAL A CG1 1 
ATOM   762  C CG2 . VAL A 1 103 ? 3.700   -1.838  -12.464 1.00 25.27 ? 103 VAL A CG2 1 
ATOM   763  N N   . ILE A 1 104 ? 3.909   -1.625  -17.065 1.00 20.48 ? 104 ILE A N   1 
ATOM   764  C CA  . ILE A 1 104 ? 3.818   -1.387  -18.515 1.00 19.95 ? 104 ILE A CA  1 
ATOM   765  C C   . ILE A 1 104 ? 2.641   -2.207  -19.096 1.00 19.27 ? 104 ILE A C   1 
ATOM   766  O O   . ILE A 1 104 ? 2.225   -3.196  -18.486 1.00 19.41 ? 104 ILE A O   1 
ATOM   767  C CB  . ILE A 1 104 ? 5.140   -1.812  -19.296 1.00 17.93 ? 104 ILE A CB  1 
ATOM   768  C CG1 . ILE A 1 104 ? 5.442   -3.319  -19.125 1.00 17.69 ? 104 ILE A CG1 1 
ATOM   769  C CG2 . ILE A 1 104 ? 6.259   -0.863  -18.929 1.00 18.60 ? 104 ILE A CG2 1 
ATOM   770  C CD1 . ILE A 1 104 ? 6.731   -3.843  -19.938 1.00 16.23 ? 104 ILE A CD1 1 
ATOM   771  N N   . SER A 1 105 ? 2.155   -1.817  -20.291 1.00 19.66 ? 105 SER A N   1 
ATOM   772  C CA  . SER A 1 105 ? 1.189   -2.663  -21.028 1.00 20.40 ? 105 SER A CA  1 
ATOM   773  C C   . SER A 1 105 ? 1.331   -2.524  -22.561 1.00 21.10 ? 105 SER A C   1 
ATOM   774  O O   . SER A 1 105 ? 2.051   -1.648  -23.039 1.00 22.95 ? 105 SER A O   1 
ATOM   775  C CB  . SER A 1 105 ? -0.226  -2.306  -20.522 1.00 18.19 ? 105 SER A CB  1 
ATOM   776  O OG  . SER A 1 105 ? -1.186  -2.743  -21.420 1.00 20.47 ? 105 SER A OG  1 
ATOM   777  N N   . LEU A 1 106 ? 0.636   -3.352  -23.340 1.00 22.77 ? 106 LEU A N   1 
ATOM   778  C CA  . LEU A 1 106 ? 0.647   -3.242  -24.842 1.00 24.57 ? 106 LEU A CA  1 
ATOM   779  C C   . LEU A 1 106 ? -0.627  -2.623  -25.382 1.00 26.67 ? 106 LEU A C   1 
ATOM   780  O O   . LEU A 1 106 ? -0.751  -2.397  -26.577 1.00 27.21 ? 106 LEU A O   1 
ATOM   781  C CB  . LEU A 1 106 ? 0.907   -4.579  -25.525 1.00 24.42 ? 106 LEU A CB  1 
ATOM   782  C CG  . LEU A 1 106 ? 2.309   -5.130  -25.258 1.00 24.69 ? 106 LEU A CG  1 
ATOM   783  C CD1 . LEU A 1 106 ? 2.585   -6.414  -26.045 1.00 23.36 ? 106 LEU A CD1 1 
ATOM   784  C CD2 . LEU A 1 106 ? 3.379   -4.001  -25.428 1.00 24.89 ? 106 LEU A CD2 1 
ATOM   785  N N   . SER A 1 107 ? -1.542  -2.294  -24.465 1.00 27.73 ? 107 SER A N   1 
ATOM   786  C CA  . SER A 1 107 ? -2.750  -1.580  -24.760 1.00 29.08 ? 107 SER A CA  1 
ATOM   787  C C   . SER A 1 107 ? -3.055  -0.668  -23.574 1.00 29.53 ? 107 SER A C   1 
ATOM   788  O O   . SER A 1 107 ? -2.499  -0.869  -22.495 1.00 29.79 ? 107 SER A O   1 
ATOM   789  C CB  . SER A 1 107 ? -3.888  -2.575  -25.016 1.00 29.33 ? 107 SER A CB  1 
ATOM   790  O OG  . SER A 1 107 ? -4.002  -3.473  -23.932 1.00 26.78 ? 107 SER A OG  1 
ATOM   791  N N   . GLY A 1 108 ? -3.881  0.375   -23.769 1.00 30.85 ? 108 GLY A N   1 
ATOM   792  C CA  . GLY A 1 108 ? -4.341  1.210   -22.609 1.00 29.42 ? 108 GLY A CA  1 
ATOM   793  C C   . GLY A 1 108 ? -3.601  2.502   -22.267 1.00 29.22 ? 108 GLY A C   1 
ATOM   794  O O   . GLY A 1 108 ? -2.844  2.998   -23.089 1.00 29.39 ? 108 GLY A O   1 
ATOM   795  N N   . ASP A 1 109 ? -3.846  3.055   -21.076 1.00 28.45 ? 109 ASP A N   1 
ATOM   796  C CA  . ASP A 1 109 ? -3.172  4.297   -20.596 1.00 30.25 ? 109 ASP A CA  1 
ATOM   797  C C   . ASP A 1 109 ? -1.626  4.068   -20.461 1.00 29.08 ? 109 ASP A C   1 
ATOM   798  O O   . ASP A 1 109 ? -0.822  4.997   -20.581 1.00 28.42 ? 109 ASP A O   1 
ATOM   799  C CB  . ASP A 1 109 ? -3.665  4.695   -19.183 1.00 31.74 ? 109 ASP A CB  1 
ATOM   800  C CG  . ASP A 1 109 ? -5.037  5.434   -19.154 1.00 37.15 ? 109 ASP A CG  1 
ATOM   801  O OD1 . ASP A 1 109 ? -5.511  5.728   -18.007 1.00 41.97 ? 109 ASP A OD1 1 
ATOM   802  O OD2 . ASP A 1 109 ? -5.610  5.774   -20.213 1.00 41.33 ? 109 ASP A OD2 1 
ATOM   803  N N   . HIS A 1 110 ? -1.243  2.817   -20.186 1.00 27.70 ? 110 HIS A N   1 
ATOM   804  C CA  . HIS A 1 110 ? 0.132   2.487   -19.862 1.00 26.41 ? 110 HIS A CA  1 
ATOM   805  C C   . HIS A 1 110 ? 0.774   1.829   -21.064 1.00 24.17 ? 110 HIS A C   1 
ATOM   806  O O   . HIS A 1 110 ? 1.846   1.178   -20.906 1.00 26.07 ? 110 HIS A O   1 
ATOM   807  C CB  . HIS A 1 110 ? 0.215   1.506   -18.680 1.00 25.62 ? 110 HIS A CB  1 
ATOM   808  C CG  . HIS A 1 110 ? -0.030  2.134   -17.353 1.00 28.52 ? 110 HIS A CG  1 
ATOM   809  N ND1 . HIS A 1 110 ? 0.048   1.419   -16.165 1.00 26.68 ? 110 HIS A ND1 1 
ATOM   810  C CD2 . HIS A 1 110 ? -0.358  3.408   -17.020 1.00 26.98 ? 110 HIS A CD2 1 
ATOM   811  C CE1 . HIS A 1 110 ? -0.221  2.237   -15.163 1.00 31.93 ? 110 HIS A CE1 1 
ATOM   812  N NE2 . HIS A 1 110 ? -0.454  3.449   -15.652 1.00 30.34 ? 110 HIS A NE2 1 
ATOM   813  N N   . CYS A 1 111 ? 0.132   1.980   -22.223 1.00 22.26 ? 111 CYS A N   1 
ATOM   814  C CA  . CYS A 1 111 ? 0.562   1.338   -23.467 1.00 21.29 ? 111 CYS A CA  1 
ATOM   815  C C   . CYS A 1 111 ? 1.940   1.848   -23.871 1.00 20.34 ? 111 CYS A C   1 
ATOM   816  O O   . CYS A 1 111 ? 2.173   3.071   -23.905 1.00 19.68 ? 111 CYS A O   1 
ATOM   817  C CB  . CYS A 1 111 ? -0.391  1.596   -24.641 1.00 21.68 ? 111 CYS A CB  1 
ATOM   818  S SG  . CYS A 1 111 ? 0.184   0.630   -26.080 1.00 21.24 ? 111 CYS A SG  1 
ATOM   819  N N   . ILE A 1 112 ? 2.821   0.927   -24.186 1.00 19.53 ? 112 ILE A N   1 
ATOM   820  C CA  . ILE A 1 112 ? 4.184   1.315   -24.643 1.00 18.72 ? 112 ILE A CA  1 
ATOM   821  C C   . ILE A 1 112 ? 4.475   1.122   -26.133 1.00 18.75 ? 112 ILE A C   1 
ATOM   822  O O   . ILE A 1 112 ? 5.626   1.316   -26.578 1.00 18.14 ? 112 ILE A O   1 
ATOM   823  C CB  . ILE A 1 112 ? 5.301   0.643   -23.797 1.00 18.63 ? 112 ILE A CB  1 
ATOM   824  C CG1 . ILE A 1 112 ? 5.148   -0.903  -23.790 1.00 18.09 ? 112 ILE A CG1 1 
ATOM   825  C CG2 . ILE A 1 112 ? 5.271   1.233   -22.397 1.00 14.65 ? 112 ILE A CG2 1 
ATOM   826  C CD1 . ILE A 1 112 ? 6.406   -1.613  -23.227 1.00 18.58 ? 112 ILE A CD1 1 
ATOM   827  N N   . ILE A 1 113 ? 3.460   0.724   -26.916 1.00 18.10 ? 113 ILE A N   1 
ATOM   828  C CA  . ILE A 1 113 ? 3.685   0.597   -28.332 1.00 18.09 ? 113 ILE A CA  1 
ATOM   829  C C   . ILE A 1 113 ? 3.900   2.025   -28.884 1.00 18.75 ? 113 ILE A C   1 
ATOM   830  O O   . ILE A 1 113 ? 3.181   2.961   -28.491 1.00 18.42 ? 113 ILE A O   1 
ATOM   831  C CB  . ILE A 1 113 ? 2.696   -0.353  -29.003 1.00 18.65 ? 113 ILE A CB  1 
ATOM   832  C CG1 . ILE A 1 113 ? 3.166   -1.805  -28.669 1.00 21.50 ? 113 ILE A CG1 1 
ATOM   833  C CG2 . ILE A 1 113 ? 2.666   -0.147  -30.472 1.00 16.57 ? 113 ILE A CG2 1 
ATOM   834  C CD1 . ILE A 1 113 ? 2.068   -2.767  -28.497 1.00 24.39 ? 113 ILE A CD1 1 
ATOM   835  N N   . GLY A 1 114 ? 4.970   2.201   -29.679 1.00 16.32 ? 114 GLY A N   1 
ATOM   836  C CA  . GLY A 1 114 ? 5.276   3.503   -30.267 1.00 15.74 ? 114 GLY A CA  1 
ATOM   837  C C   . GLY A 1 114 ? 6.120   4.471   -29.449 1.00 15.94 ? 114 GLY A C   1 
ATOM   838  O O   . GLY A 1 114 ? 6.296   5.634   -29.852 1.00 16.01 ? 114 GLY A O   1 
ATOM   839  N N   . ARG A 1 115 ? 6.572   4.026   -28.262 1.00 15.59 ? 115 ARG A N   1 
ATOM   840  C CA  . ARG A 1 115 ? 7.437   4.740   -27.359 1.00 16.45 ? 115 ARG A CA  1 
ATOM   841  C C   . ARG A 1 115 ? 8.821   4.121   -27.548 1.00 18.07 ? 115 ARG A C   1 
ATOM   842  O O   . ARG A 1 115 ? 8.977   3.299   -28.485 1.00 18.50 ? 115 ARG A O   1 
ATOM   843  C CB  . ARG A 1 115 ? 6.901   4.638   -25.939 1.00 15.36 ? 115 ARG A CB  1 
ATOM   844  C CG  . ARG A 1 115 ? 5.431   5.209   -25.889 1.00 15.59 ? 115 ARG A CG  1 
ATOM   845  C CD  . ARG A 1 115 ? 4.985   5.470   -24.412 1.00 18.31 ? 115 ARG A CD  1 
ATOM   846  N NE  . ARG A 1 115 ? 3.569   5.824   -24.362 1.00 19.99 ? 115 ARG A NE  1 
ATOM   847  C CZ  . ARG A 1 115 ? 3.086   7.061   -24.523 1.00 18.18 ? 115 ARG A CZ  1 
ATOM   848  N NH1 . ARG A 1 115 ? 3.907   8.088   -24.698 1.00 20.59 ? 115 ARG A NH1 1 
ATOM   849  N NH2 . ARG A 1 115 ? 1.778   7.277   -24.448 1.00 20.89 ? 115 ARG A NH2 1 
ATOM   850  N N   . THR A 1 116 ? 9.822   4.525   -26.748 1.00 17.42 ? 116 THR A N   1 
ATOM   851  C CA  . THR A 1 116 ? 11.203  3.984   -26.894 1.00 17.75 ? 116 THR A CA  1 
ATOM   852  C C   . THR A 1 116 ? 11.679  3.122   -25.685 1.00 18.16 ? 116 THR A C   1 
ATOM   853  O O   . THR A 1 116 ? 11.339  3.344   -24.566 1.00 20.01 ? 116 THR A O   1 
ATOM   854  C CB  . THR A 1 116 ? 12.185  5.164   -27.264 1.00 17.45 ? 116 THR A CB  1 
ATOM   855  O OG1 . THR A 1 116 ? 11.764  5.689   -28.527 1.00 15.06 ? 116 THR A OG1 1 
ATOM   856  C CG2 . THR A 1 116 ? 13.754  4.767   -27.311 1.00 16.55 ? 116 THR A CG2 1 
ATOM   857  N N   . LEU A 1 117 ? 12.360  2.046   -25.962 1.00 17.50 ? 117 LEU A N   1 
ATOM   858  C CA  . LEU A 1 117 ? 13.209  1.433   -25.012 1.00 17.14 ? 117 LEU A CA  1 
ATOM   859  C C   . LEU A 1 117 ? 14.671  1.920   -25.203 1.00 18.15 ? 117 LEU A C   1 
ATOM   860  O O   . LEU A 1 117 ? 15.200  2.010   -26.317 1.00 17.49 ? 117 LEU A O   1 
ATOM   861  C CB  . LEU A 1 117 ? 13.072  -0.078  -25.231 1.00 15.84 ? 117 LEU A CB  1 
ATOM   862  C CG  . LEU A 1 117 ? 13.654  -0.963  -24.179 1.00 15.75 ? 117 LEU A CG  1 
ATOM   863  C CD1 . LEU A 1 117 ? 12.768  -0.919  -22.990 1.00 14.28 ? 117 LEU A CD1 1 
ATOM   864  C CD2 . LEU A 1 117 ? 13.852  -2.368  -24.786 1.00 4.92  ? 117 LEU A CD2 1 
ATOM   865  N N   . VAL A 1 118 ? 15.303  2.252   -24.083 1.00 18.21 ? 118 VAL A N   1 
ATOM   866  C CA  . VAL A 1 118 ? 16.670  2.678   -24.002 1.00 17.47 ? 118 VAL A CA  1 
ATOM   867  C C   . VAL A 1 118 ? 17.406  1.781   -23.006 1.00 18.85 ? 118 VAL A C   1 
ATOM   868  O O   . VAL A 1 118 ? 16.866  1.344   -21.972 1.00 20.01 ? 118 VAL A O   1 
ATOM   869  C CB  . VAL A 1 118 ? 16.807  4.182   -23.540 1.00 17.39 ? 118 VAL A CB  1 
ATOM   870  C CG1 . VAL A 1 118 ? 18.229  4.639   -23.633 1.00 15.02 ? 118 VAL A CG1 1 
ATOM   871  C CG2 . VAL A 1 118 ? 15.888  5.100   -24.368 1.00 12.72 ? 118 VAL A CG2 1 
ATOM   872  N N   . VAL A 1 119 ? 18.655  1.489   -23.349 1.00 19.99 ? 119 VAL A N   1 
ATOM   873  C CA  . VAL A 1 119 ? 19.586  0.771   -22.490 1.00 18.64 ? 119 VAL A CA  1 
ATOM   874  C C   . VAL A 1 119 ? 20.743  1.723   -22.273 1.00 19.61 ? 119 VAL A C   1 
ATOM   875  O O   . VAL A 1 119 ? 21.371  2.253   -23.217 1.00 18.48 ? 119 VAL A O   1 
ATOM   876  C CB  . VAL A 1 119 ? 20.009  -0.584  -23.061 1.00 19.34 ? 119 VAL A CB  1 
ATOM   877  C CG1 . VAL A 1 119 ? 20.779  -0.425  -24.412 1.00 17.94 ? 119 VAL A CG1 1 
ATOM   878  C CG2 . VAL A 1 119 ? 20.868  -1.428  -22.027 1.00 16.40 ? 119 VAL A CG2 1 
ATOM   879  N N   . HIS A 1 120 ? 21.003  1.936   -20.992 1.00 20.85 ? 120 HIS A N   1 
ATOM   880  C CA  . HIS A 1 120 ? 21.860  3.009   -20.528 1.00 20.89 ? 120 HIS A CA  1 
ATOM   881  C C   . HIS A 1 120 ? 23.223  2.520   -20.202 1.00 20.61 ? 120 HIS A C   1 
ATOM   882  O O   . HIS A 1 120 ? 23.476  1.327   -20.049 1.00 20.38 ? 120 HIS A O   1 
ATOM   883  C CB  . HIS A 1 120 ? 21.244  3.637   -19.279 1.00 19.89 ? 120 HIS A CB  1 
ATOM   884  C CG  . HIS A 1 120 ? 19.968  4.385   -19.559 1.00 20.16 ? 120 HIS A CG  1 
ATOM   885  N ND1 . HIS A 1 120 ? 19.937  5.744   -19.779 1.00 14.27 ? 120 HIS A ND1 1 
ATOM   886  C CD2 . HIS A 1 120 ? 18.684  3.954   -19.651 1.00 16.72 ? 120 HIS A CD2 1 
ATOM   887  C CE1 . HIS A 1 120 ? 18.690  6.121   -20.026 1.00 14.59 ? 120 HIS A CE1 1 
ATOM   888  N NE2 . HIS A 1 120 ? 17.910  5.055   -19.934 1.00 17.86 ? 120 HIS A NE2 1 
ATOM   889  N N   . GLU A 1 121 ? 24.082  3.511   -20.066 1.00 21.78 ? 121 GLU A N   1 
ATOM   890  C CA  . GLU A 1 121 ? 25.503  3.406   -19.787 1.00 22.28 ? 121 GLU A CA  1 
ATOM   891  C C   . GLU A 1 121 ? 25.890  2.585   -18.502 1.00 22.11 ? 121 GLU A C   1 
ATOM   892  O O   . GLU A 1 121 ? 26.688  1.627   -18.551 1.00 20.22 ? 121 GLU A O   1 
ATOM   893  C CB  . GLU A 1 121 ? 25.928  4.861   -19.652 1.00 21.23 ? 121 GLU A CB  1 
ATOM   894  C CG  . GLU A 1 121 ? 27.413  5.112   -19.751 1.00 24.64 ? 121 GLU A CG  1 
ATOM   895  C CD  . GLU A 1 121 ? 27.813  6.424   -19.098 1.00 30.50 ? 121 GLU A CD  1 
ATOM   896  O OE1 . GLU A 1 121 ? 29.041  6.585   -18.904 1.00 39.22 ? 121 GLU A OE1 1 
ATOM   897  O OE2 . GLU A 1 121 ? 26.950  7.308   -18.811 1.00 27.53 ? 121 GLU A OE2 1 
ATOM   898  N N   . LYS A 1 122 ? 25.258  2.971   -17.378 1.00 23.06 ? 122 LYS A N   1 
ATOM   899  C CA  . LYS A 1 122 ? 25.567  2.535   -16.013 1.00 23.47 ? 122 LYS A CA  1 
ATOM   900  C C   . LYS A 1 122 ? 24.283  1.956   -15.346 1.00 23.58 ? 122 LYS A C   1 
ATOM   901  O O   . LYS A 1 122 ? 23.146  2.232   -15.775 1.00 22.31 ? 122 LYS A O   1 
ATOM   902  C CB  . LYS A 1 122 ? 25.999  3.734   -15.152 1.00 23.41 ? 122 LYS A CB  1 
ATOM   903  C CG  . LYS A 1 122 ? 27.350  4.360   -15.456 1.00 29.69 ? 122 LYS A CG  1 
ATOM   904  C CD  . LYS A 1 122 ? 27.378  5.800   -14.969 1.00 34.00 ? 122 LYS A CD  1 
ATOM   905  C CE  . LYS A 1 122 ? 27.445  5.872   -13.427 1.00 42.06 ? 122 LYS A CE  1 
ATOM   906  N NZ  . LYS A 1 122 ? 28.826  5.684   -12.774 1.00 42.67 ? 122 LYS A NZ  1 
ATOM   907  N N   . ALA A 1 123 ? 24.499  1.204   -14.272 1.00 22.12 ? 123 ALA A N   1 
ATOM   908  C CA  . ALA A 1 123 ? 23.453  0.675   -13.402 1.00 21.52 ? 123 ALA A CA  1 
ATOM   909  C C   . ALA A 1 123 ? 22.434  1.763   -13.098 1.00 21.19 ? 123 ALA A C   1 
ATOM   910  O O   . ALA A 1 123 ? 22.791  2.904   -12.877 1.00 21.61 ? 123 ALA A O   1 
ATOM   911  C CB  . ALA A 1 123 ? 24.094  0.169   -12.080 1.00 21.01 ? 123 ALA A CB  1 
ATOM   912  N N   . ASP A 1 124 ? 21.155  1.412   -13.169 1.00 20.95 ? 124 ASP A N   1 
ATOM   913  C CA  . ASP A 1 124 ? 20.087  2.151   -12.469 1.00 20.00 ? 124 ASP A CA  1 
ATOM   914  C C   . ASP A 1 124 ? 20.237  1.841   -10.952 1.00 19.69 ? 124 ASP A C   1 
ATOM   915  O O   . ASP A 1 124 ? 20.159  0.678   -10.534 1.00 20.14 ? 124 ASP A O   1 
ATOM   916  C CB  . ASP A 1 124 ? 18.737  1.664   -13.030 1.00 18.01 ? 124 ASP A CB  1 
ATOM   917  C CG  . ASP A 1 124 ? 17.566  2.376   -12.462 1.00 19.91 ? 124 ASP A CG  1 
ATOM   918  O OD1 . ASP A 1 124 ? 17.723  3.410   -11.792 1.00 23.67 ? 124 ASP A OD1 1 
ATOM   919  O OD2 . ASP A 1 124 ? 16.439  1.926   -12.721 1.00 23.86 ? 124 ASP A OD2 1 
ATOM   920  N N   . ASP A 1 125 ? 20.472  2.857   -10.129 1.00 19.86 ? 125 ASP A N   1 
ATOM   921  C CA  . ASP A 1 125 ? 20.461  2.663   -8.645  1.00 21.00 ? 125 ASP A CA  1 
ATOM   922  C C   . ASP A 1 125 ? 19.027  2.577   -7.992  1.00 21.82 ? 125 ASP A C   1 
ATOM   923  O O   . ASP A 1 125 ? 18.874  2.402   -6.758  1.00 21.68 ? 125 ASP A O   1 
ATOM   924  C CB  . ASP A 1 125 ? 21.202  3.778   -7.979  1.00 21.43 ? 125 ASP A CB  1 
ATOM   925  C CG  . ASP A 1 125 ? 20.518  5.127   -8.175  1.00 21.80 ? 125 ASP A CG  1 
ATOM   926  O OD1 . ASP A 1 125 ? 19.279  5.135   -8.321  1.00 21.28 ? 125 ASP A OD1 1 
ATOM   927  O OD2 . ASP A 1 125 ? 21.225  6.165   -8.159  1.00 22.93 ? 125 ASP A OD2 1 
ATOM   928  N N   . LEU A 1 126 ? 18.005  2.762   -8.818  1.00 20.10 ? 126 LEU A N   1 
ATOM   929  C CA  . LEU A 1 126 ? 16.633  2.368   -8.521  1.00 19.41 ? 126 LEU A CA  1 
ATOM   930  C C   . LEU A 1 126 ? 15.991  3.254   -7.507  1.00 19.87 ? 126 LEU A C   1 
ATOM   931  O O   . LEU A 1 126 ? 15.129  2.813   -6.720  1.00 20.71 ? 126 LEU A O   1 
ATOM   932  C CB  . LEU A 1 126 ? 16.504  0.851   -8.174  1.00 18.59 ? 126 LEU A CB  1 
ATOM   933  C CG  . LEU A 1 126 ? 17.253  -0.337  -8.815  1.00 17.73 ? 126 LEU A CG  1 
ATOM   934  C CD1 . LEU A 1 126 ? 17.079  -1.534  -7.954  1.00 19.28 ? 126 LEU A CD1 1 
ATOM   935  C CD2 . LEU A 1 126 ? 16.724  -0.658  -10.196 1.00 18.05 ? 126 LEU A CD2 1 
ATOM   936  N N   . GLY A 1 127 ? 16.379  4.529   -7.510  1.00 20.86 ? 127 GLY A N   1 
ATOM   937  C CA  . GLY A 1 127 ? 15.917  5.437   -6.434  1.00 22.34 ? 127 GLY A CA  1 
ATOM   938  C C   . GLY A 1 127 ? 16.570  5.270   -5.056  1.00 23.02 ? 127 GLY A C   1 
ATOM   939  O O   . GLY A 1 127 ? 16.194  5.956   -4.109  1.00 21.67 ? 127 GLY A O   1 
ATOM   940  N N   . LYS A 1 128 ? 17.546  4.354   -4.935  1.00 24.80 ? 128 LYS A N   1 
ATOM   941  C CA  . LYS A 1 128 ? 18.319  4.126   -3.659  1.00 26.09 ? 128 LYS A CA  1 
ATOM   942  C C   . LYS A 1 128 ? 19.855  4.361   -3.727  1.00 26.83 ? 128 LYS A C   1 
ATOM   943  O O   . LYS A 1 128 ? 20.686  3.617   -3.138  1.00 27.36 ? 128 LYS A O   1 
ATOM   944  C CB  . LYS A 1 128 ? 17.937  2.815   -3.004  1.00 27.26 ? 128 LYS A CB  1 
ATOM   945  C CG  . LYS A 1 128 ? 16.578  2.977   -2.199  1.00 27.25 ? 128 LYS A CG  1 
ATOM   946  C CD  . LYS A 1 128 ? 15.898  1.617   -1.994  1.00 31.39 ? 128 LYS A CD  1 
ATOM   947  C CE  . LYS A 1 128 ? 14.476  1.818   -1.498  1.00 30.00 ? 128 LYS A CE  1 
ATOM   948  N NZ  . LYS A 1 128 ? 13.525  2.399   -2.536  1.00 32.97 ? 128 LYS A NZ  1 
ATOM   949  N N   . GLY A 1 129 ? 20.177  5.433   -4.453  1.00 26.07 ? 129 GLY A N   1 
ATOM   950  C CA  . GLY A 1 129 ? 21.526  5.855   -4.776  1.00 26.41 ? 129 GLY A CA  1 
ATOM   951  C C   . GLY A 1 129 ? 21.914  6.996   -3.876  1.00 26.50 ? 129 GLY A C   1 
ATOM   952  O O   . GLY A 1 129 ? 23.097  7.240   -3.713  1.00 26.35 ? 129 GLY A O   1 
ATOM   953  N N   . GLY A 1 130 ? 20.899  7.695   -3.350  1.00 26.24 ? 130 GLY A N   1 
ATOM   954  C CA  . GLY A 1 130 ? 20.990  8.527   -2.177  1.00 26.42 ? 130 GLY A CA  1 
ATOM   955  C C   . GLY A 1 130 ? 21.358  9.952   -2.477  1.00 27.10 ? 130 GLY A C   1 
ATOM   956  O O   . GLY A 1 130 ? 22.061  10.551  -1.692  1.00 24.38 ? 130 GLY A O   1 
ATOM   957  N N   . ASN A 1 131 ? 20.930  10.436  -3.657  1.00 28.86 ? 131 ASN A N   1 
ATOM   958  C CA  . ASN A 1 131 ? 21.131  11.821  -4.175  1.00 30.67 ? 131 ASN A CA  1 
ATOM   959  C C   . ASN A 1 131 ? 19.885  12.265  -4.960  1.00 31.85 ? 131 ASN A C   1 
ATOM   960  O O   . ASN A 1 131 ? 18.946  11.451  -5.115  1.00 31.82 ? 131 ASN A O   1 
ATOM   961  C CB  . ASN A 1 131 ? 22.440  12.007  -4.996  1.00 30.14 ? 131 ASN A CB  1 
ATOM   962  C CG  . ASN A 1 131 ? 22.609  10.970  -6.128  1.00 29.07 ? 131 ASN A CG  1 
ATOM   963  O OD1 . ASN A 1 131 ? 21.641  10.539  -6.755  1.00 25.36 ? 131 ASN A OD1 1 
ATOM   964  N ND2 . ASN A 1 131 ? 23.848  10.569  -6.376  1.00 22.04 ? 131 ASN A ND2 1 
ATOM   965  N N   . GLU A 1 132 ? 19.814  13.544  -5.392  1.00 32.82 ? 132 GLU A N   1 
ATOM   966  C CA  . GLU A 1 132 ? 18.585  14.022  -6.106  1.00 34.49 ? 132 GLU A CA  1 
ATOM   967  C C   . GLU A 1 132 ? 18.228  13.205  -7.365  1.00 32.28 ? 132 GLU A C   1 
ATOM   968  O O   . GLU A 1 132 ? 17.080  12.756  -7.545  1.00 32.23 ? 132 GLU A O   1 
ATOM   969  C CB  . GLU A 1 132 ? 18.654  15.510  -6.475  1.00 35.16 ? 132 GLU A CB  1 
ATOM   970  C CG  . GLU A 1 132 ? 17.331  16.005  -7.090  1.00 38.15 ? 132 GLU A CG  1 
ATOM   971  C CD  . GLU A 1 132 ? 17.104  17.548  -7.008  1.00 40.05 ? 132 GLU A CD  1 
ATOM   972  O OE1 . GLU A 1 132 ? 16.425  18.110  -7.913  1.00 44.18 ? 132 GLU A OE1 1 
ATOM   973  O OE2 . GLU A 1 132 ? 17.571  18.186  -6.030  1.00 48.24 ? 132 GLU A OE2 1 
ATOM   974  N N   . GLU A 1 133 ? 19.251  12.990  -8.188  1.00 30.20 ? 133 GLU A N   1 
ATOM   975  C CA  . GLU A 1 133 ? 19.124  12.451  -9.509  1.00 28.93 ? 133 GLU A CA  1 
ATOM   976  C C   . GLU A 1 133 ? 18.671  10.989  -9.456  1.00 27.87 ? 133 GLU A C   1 
ATOM   977  O O   . GLU A 1 133 ? 18.139  10.467  -10.420 1.00 25.54 ? 133 GLU A O   1 
ATOM   978  C CB  . GLU A 1 133 ? 20.478  12.662  -10.228 1.00 29.13 ? 133 GLU A CB  1 
ATOM   979  C CG  . GLU A 1 133 ? 20.545  12.532  -11.748 1.00 30.51 ? 133 GLU A CG  1 
ATOM   980  C CD  . GLU A 1 133 ? 19.435  13.184  -12.517 1.00 32.34 ? 133 GLU A CD  1 
ATOM   981  O OE1 . GLU A 1 133 ? 19.052  14.344  -12.225 1.00 37.04 ? 133 GLU A OE1 1 
ATOM   982  O OE2 . GLU A 1 133 ? 18.930  12.510  -13.449 1.00 34.77 ? 133 GLU A OE2 1 
ATOM   983  N N   . SER A 1 134 ? 18.891  10.358  -8.298  1.00 26.16 ? 134 SER A N   1 
ATOM   984  C CA  . SER A 1 134 ? 18.506  8.954   -7.996  1.00 25.49 ? 134 SER A CA  1 
ATOM   985  C C   . SER A 1 134 ? 17.023  8.672   -8.162  1.00 25.35 ? 134 SER A C   1 
ATOM   986  O O   . SER A 1 134 ? 16.615  7.610   -8.535  1.00 25.79 ? 134 SER A O   1 
ATOM   987  C CB  . SER A 1 134 ? 18.827  8.593   -6.545  1.00 23.34 ? 134 SER A CB  1 
ATOM   988  O OG  . SER A 1 134 ? 18.455  7.259   -6.395  1.00 20.03 ? 134 SER A OG  1 
ATOM   989  N N   . THR A 1 135 ? 16.231  9.650   -7.805  1.00 25.50 ? 135 THR A N   1 
ATOM   990  C CA  . THR A 1 135 ? 14.817  9.521   -7.699  1.00 25.53 ? 135 THR A CA  1 
ATOM   991  C C   . THR A 1 135 ? 14.140  10.186  -8.957  1.00 26.35 ? 135 THR A C   1 
ATOM   992  O O   . THR A 1 135 ? 12.885  10.133  -9.081  1.00 25.97 ? 135 THR A O   1 
ATOM   993  C CB  . THR A 1 135 ? 14.467  9.998   -6.247  1.00 24.59 ? 135 THR A CB  1 
ATOM   994  O OG1 . THR A 1 135 ? 13.748  8.975   -5.516  1.00 26.44 ? 135 THR A OG1 1 
ATOM   995  C CG2 . THR A 1 135 ? 13.843  11.234  -6.206  1.00 24.63 ? 135 THR A CG2 1 
ATOM   996  N N   . LYS A 1 136 ? 14.966  10.756  -9.884  1.00 26.11 ? 136 LYS A N   1 
ATOM   997  C CA  . LYS A 1 136 ? 14.507  11.166  -11.260 1.00 28.36 ? 136 LYS A CA  1 
ATOM   998  C C   . LYS A 1 136 ? 14.810  10.143  -12.310 1.00 27.68 ? 136 LYS A C   1 
ATOM   999  O O   . LYS A 1 136 ? 13.917  9.633   -12.975 1.00 27.93 ? 136 LYS A O   1 
ATOM   1000 C CB  . LYS A 1 136 ? 15.113  12.498  -11.756 1.00 28.67 ? 136 LYS A CB  1 
ATOM   1001 C CG  . LYS A 1 136 ? 15.039  13.618  -10.751 1.00 33.26 ? 136 LYS A CG  1 
ATOM   1002 C CD  . LYS A 1 136 ? 15.800  14.819  -11.260 1.00 40.74 ? 136 LYS A CD  1 
ATOM   1003 C CE  . LYS A 1 136 ? 15.600  15.965  -10.296 1.00 43.90 ? 136 LYS A CE  1 
ATOM   1004 N NZ  . LYS A 1 136 ? 16.883  16.668  -10.187 1.00 48.17 ? 136 LYS A NZ  1 
ATOM   1005 N N   . THR A 1 137 ? 16.105  9.870   -12.466 1.00 27.66 ? 137 THR A N   1 
ATOM   1006 C CA  . THR A 1 137 ? 16.584  9.001   -13.482 1.00 27.28 ? 137 THR A CA  1 
ATOM   1007 C C   . THR A 1 137 ? 17.325  7.761   -13.011 1.00 26.88 ? 137 THR A C   1 
ATOM   1008 O O   . THR A 1 137 ? 17.626  6.887   -13.863 1.00 26.50 ? 137 THR A O   1 
ATOM   1009 C CB  . THR A 1 137 ? 17.464  9.766   -14.475 1.00 29.05 ? 137 THR A CB  1 
ATOM   1010 O OG1 . THR A 1 137 ? 18.759  10.111  -13.897 1.00 29.80 ? 137 THR A OG1 1 
ATOM   1011 C CG2 . THR A 1 137 ? 16.675  11.009  -15.034 1.00 28.08 ? 137 THR A CG2 1 
ATOM   1012 N N   . GLY A 1 138 ? 17.656  7.695   -11.711 1.00 23.53 ? 138 GLY A N   1 
ATOM   1013 C CA  . GLY A 1 138 ? 18.382  6.556   -11.136 1.00 22.69 ? 138 GLY A CA  1 
ATOM   1014 C C   . GLY A 1 138 ? 19.876  6.493   -11.490 1.00 22.07 ? 138 GLY A C   1 
ATOM   1015 O O   . GLY A 1 138 ? 20.559  5.502   -11.268 1.00 21.70 ? 138 GLY A O   1 
ATOM   1016 N N   . ASN A 1 139 ? 20.371  7.544   -12.095 1.00 21.52 ? 139 ASN A N   1 
ATOM   1017 C CA  . ASN A 1 139 ? 21.774  7.696   -12.353 1.00 22.55 ? 139 ASN A CA  1 
ATOM   1018 C C   . ASN A 1 139 ? 22.397  6.776   -13.422 1.00 23.32 ? 139 ASN A C   1 
ATOM   1019 O O   . ASN A 1 139 ? 23.611  6.536   -13.380 1.00 22.01 ? 139 ASN A O   1 
ATOM   1020 C CB  . ASN A 1 139 ? 22.535  7.675   -11.014 1.00 23.38 ? 139 ASN A CB  1 
ATOM   1021 C CG  . ASN A 1 139 ? 22.323  8.952   -10.236 1.00 24.39 ? 139 ASN A CG  1 
ATOM   1022 O OD1 . ASN A 1 139 ? 22.721  9.989   -10.718 1.00 23.16 ? 139 ASN A OD1 1 
ATOM   1023 N ND2 . ASN A 1 139 ? 21.623  8.891   -9.078  1.00 21.62 ? 139 ASN A ND2 1 
ATOM   1024 N N   . ALA A 1 140 ? 21.564  6.323   -14.396 1.00 22.61 ? 140 ALA A N   1 
ATOM   1025 C CA  . ALA A 1 140 ? 21.915  5.201   -15.287 1.00 22.14 ? 140 ALA A CA  1 
ATOM   1026 C C   . ALA A 1 140 ? 22.826  5.607   -16.440 1.00 21.93 ? 140 ALA A C   1 
ATOM   1027 O O   . ALA A 1 140 ? 23.276  4.766   -17.227 1.00 20.57 ? 140 ALA A O   1 
ATOM   1028 C CB  . ALA A 1 140 ? 20.673  4.495   -15.794 1.00 21.32 ? 140 ALA A CB  1 
ATOM   1029 N N   . GLY A 1 141 ? 23.073  6.921   -16.522 1.00 21.46 ? 141 GLY A N   1 
ATOM   1030 C CA  . GLY A 1 141 ? 23.998  7.465   -17.473 1.00 20.19 ? 141 GLY A CA  1 
ATOM   1031 C C   . GLY A 1 141 ? 23.331  7.799   -18.807 1.00 19.82 ? 141 GLY A C   1 
ATOM   1032 O O   . GLY A 1 141 ? 22.109  8.038   -18.881 1.00 18.22 ? 141 GLY A O   1 
ATOM   1033 N N   . SER A 1 142 ? 24.210  7.905   -19.815 1.00 18.60 ? 142 SER A N   1 
ATOM   1034 C CA  . SER A 1 142 ? 23.895  8.100   -21.231 1.00 18.71 ? 142 SER A CA  1 
ATOM   1035 C C   . SER A 1 142 ? 23.153  6.897   -21.827 1.00 17.84 ? 142 SER A C   1 
ATOM   1036 O O   . SER A 1 142 ? 23.024  5.811   -21.224 1.00 18.29 ? 142 SER A O   1 
ATOM   1037 C CB  . SER A 1 142 ? 25.204  8.332   -22.013 1.00 18.06 ? 142 SER A CB  1 
ATOM   1038 O OG  . SER A 1 142 ? 25.792  7.028   -22.353 1.00 19.44 ? 142 SER A OG  1 
ATOM   1039 N N   . ARG A 1 143 ? 22.611  7.141   -23.018 1.00 19.03 ? 143 ARG A N   1 
ATOM   1040 C CA  . ARG A 1 143 ? 21.748  6.245   -23.718 1.00 18.64 ? 143 ARG A CA  1 
ATOM   1041 C C   . ARG A 1 143 ? 22.611  5.547   -24.750 1.00 18.77 ? 143 ARG A C   1 
ATOM   1042 O O   . ARG A 1 143 ? 23.036  6.122   -25.753 1.00 18.90 ? 143 ARG A O   1 
ATOM   1043 C CB  . ARG A 1 143 ? 20.593  7.004   -24.353 1.00 17.72 ? 143 ARG A CB  1 
ATOM   1044 C CG  . ARG A 1 143 ? 19.796  7.847   -23.309 1.00 20.58 ? 143 ARG A CG  1 
ATOM   1045 C CD  . ARG A 1 143 ? 18.587  8.581   -23.890 1.00 18.16 ? 143 ARG A CD  1 
ATOM   1046 N NE  . ARG A 1 143 ? 18.010  9.416   -22.864 1.00 18.27 ? 143 ARG A NE  1 
ATOM   1047 C CZ  . ARG A 1 143 ? 16.870  10.103  -22.958 1.00 20.75 ? 143 ARG A CZ  1 
ATOM   1048 N NH1 . ARG A 1 143 ? 16.120  9.981   -24.032 1.00 19.87 ? 143 ARG A NH1 1 
ATOM   1049 N NH2 . ARG A 1 143 ? 16.432  10.844  -21.938 1.00 13.46 ? 143 ARG A NH2 1 
ATOM   1050 N N   . LEU A 1 144 ? 22.852  4.289   -24.495 1.00 18.27 ? 144 LEU A N   1 
ATOM   1051 C CA  . LEU A 1 144 ? 23.753  3.491   -25.346 1.00 17.78 ? 144 LEU A CA  1 
ATOM   1052 C C   . LEU A 1 144 ? 23.129  3.057   -26.680 1.00 18.69 ? 144 LEU A C   1 
ATOM   1053 O O   . LEU A 1 144 ? 23.846  2.994   -27.701 1.00 18.11 ? 144 LEU A O   1 
ATOM   1054 C CB  . LEU A 1 144 ? 24.316  2.319   -24.539 1.00 16.47 ? 144 LEU A CB  1 
ATOM   1055 C CG  . LEU A 1 144 ? 25.363  2.667   -23.408 1.00 18.11 ? 144 LEU A CG  1 
ATOM   1056 C CD1 . LEU A 1 144 ? 26.066  1.427   -22.921 1.00 18.16 ? 144 LEU A CD1 1 
ATOM   1057 C CD2 . LEU A 1 144 ? 26.462  3.649   -23.821 1.00 15.04 ? 144 LEU A CD2 1 
ATOM   1058 N N   . ALA A 1 145 ? 21.822  2.710   -26.620 1.00 17.25 ? 145 ALA A N   1 
ATOM   1059 C CA  . ALA A 1 145 ? 21.044  2.161   -27.688 1.00 18.25 ? 145 ALA A CA  1 
ATOM   1060 C C   . ALA A 1 145 ? 19.553  2.319   -27.327 1.00 17.35 ? 145 ALA A C   1 
ATOM   1061 O O   . ALA A 1 145 ? 19.178  2.310   -26.165 1.00 18.14 ? 145 ALA A O   1 
ATOM   1062 C CB  . ALA A 1 145 ? 21.377  0.634   -27.941 1.00 18.06 ? 145 ALA A CB  1 
ATOM   1063 N N   . CYS A 1 146 ? 18.739  2.562   -28.340 1.00 17.04 ? 146 CYS A N   1 
ATOM   1064 C CA  . CYS A 1 146 ? 17.293  2.640   -28.214 1.00 15.71 ? 146 CYS A CA  1 
ATOM   1065 C C   . CYS A 1 146 ? 16.647  1.961   -29.461 1.00 14.50 ? 146 CYS A C   1 
ATOM   1066 O O   . CYS A 1 146 ? 17.303  1.683   -30.467 1.00 14.29 ? 146 CYS A O   1 
ATOM   1067 C CB  . CYS A 1 146 ? 16.856  4.118   -28.082 1.00 16.99 ? 146 CYS A CB  1 
ATOM   1068 S SG  . CYS A 1 146 ? 17.563  5.167   -29.340 1.00 21.12 ? 146 CYS A SG  1 
ATOM   1069 N N   . GLY A 1 147 ? 15.364  1.670   -29.363 1.00 10.54 ? 147 GLY A N   1 
ATOM   1070 C CA  . GLY A 1 147 ? 14.575  1.442   -30.484 1.00 10.26 ? 147 GLY A CA  1 
ATOM   1071 C C   . GLY A 1 147 ? 13.119  1.720   -30.103 1.00 10.58 ? 147 GLY A C   1 
ATOM   1072 O O   . GLY A 1 147 ? 12.748  1.531   -28.974 1.00 7.73  ? 147 GLY A O   1 
ATOM   1073 N N   . VAL A 1 148 ? 12.354  2.186   -31.074 1.00 11.92 ? 148 VAL A N   1 
ATOM   1074 C CA  . VAL A 1 148 ? 10.860  2.320   -31.014 1.00 13.04 ? 148 VAL A CA  1 
ATOM   1075 C C   . VAL A 1 148 ? 10.211  0.920   -30.886 1.00 14.30 ? 148 VAL A C   1 
ATOM   1076 O O   . VAL A 1 148 ? 10.524  -0.016  -31.651 1.00 12.76 ? 148 VAL A O   1 
ATOM   1077 C CB  . VAL A 1 148 ? 10.307  3.040   -32.299 1.00 13.61 ? 148 VAL A CB  1 
ATOM   1078 C CG1 . VAL A 1 148 ? 8.730   3.308   -32.246 1.00 10.87 ? 148 VAL A CG1 1 
ATOM   1079 C CG2 . VAL A 1 148 ? 11.088  4.278   -32.577 1.00 9.49  ? 148 VAL A CG2 1 
ATOM   1080 N N   . ILE A 1 149 ? 9.340   0.811   -29.866 1.00 16.52 ? 149 ILE A N   1 
ATOM   1081 C CA  . ILE A 1 149 ? 8.498   -0.343  -29.642 1.00 17.16 ? 149 ILE A CA  1 
ATOM   1082 C C   . ILE A 1 149 ? 7.369   -0.423  -30.670 1.00 18.25 ? 149 ILE A C   1 
ATOM   1083 O O   . ILE A 1 149 ? 6.416   0.360   -30.615 1.00 18.62 ? 149 ILE A O   1 
ATOM   1084 C CB  . ILE A 1 149 ? 7.988   -0.409  -28.183 1.00 15.88 ? 149 ILE A CB  1 
ATOM   1085 C CG1 . ILE A 1 149 ? 9.173   -0.169  -27.250 1.00 16.54 ? 149 ILE A CG1 1 
ATOM   1086 C CG2 . ILE A 1 149 ? 7.352   -1.845  -27.884 1.00 15.64 ? 149 ILE A CG2 1 
ATOM   1087 C CD1 . ILE A 1 149 ? 8.850   0.196   -25.833 1.00 14.88 ? 149 ILE A CD1 1 
ATOM   1088 N N   . GLY A 1 150 ? 7.497   -1.400  -31.589 1.00 18.40 ? 150 GLY A N   1 
ATOM   1089 C CA  . GLY A 1 150 ? 6.517   -1.631  -32.645 1.00 18.93 ? 150 GLY A CA  1 
ATOM   1090 C C   . GLY A 1 150 ? 5.728   -2.919  -32.491 1.00 19.24 ? 150 GLY A C   1 
ATOM   1091 O O   . GLY A 1 150 ? 6.189   -3.834  -31.894 1.00 19.92 ? 150 GLY A O   1 
ATOM   1092 N N   . ILE A 1 151 ? 4.535   -2.962  -33.046 1.00 19.99 ? 151 ILE A N   1 
ATOM   1093 C CA  . ILE A 1 151 ? 3.741   -4.201  -33.226 1.00 20.74 ? 151 ILE A CA  1 
ATOM   1094 C C   . ILE A 1 151 ? 4.459   -5.291  -34.010 1.00 19.77 ? 151 ILE A C   1 
ATOM   1095 O O   . ILE A 1 151 ? 5.048   -5.032  -35.037 1.00 17.53 ? 151 ILE A O   1 
ATOM   1096 C CB  . ILE A 1 151 ? 2.351   -3.933  -33.904 1.00 21.54 ? 151 ILE A CB  1 
ATOM   1097 C CG1 . ILE A 1 151 ? 1.592   -2.901  -33.072 1.00 23.03 ? 151 ILE A CG1 1 
ATOM   1098 C CG2 . ILE A 1 151 ? 1.537   -5.265  -34.126 1.00 18.74 ? 151 ILE A CG2 1 
ATOM   1099 C CD1 . ILE A 1 151 ? 0.910   -1.906  -33.882 1.00 22.46 ? 151 ILE A CD1 1 
ATOM   1100 N N   . ALA A 1 152 ? 4.358   -6.513  -33.480 1.00 21.82 ? 152 ALA A N   1 
ATOM   1101 C CA  . ALA A 1 152 ? 5.035   -7.693  -34.026 1.00 24.43 ? 152 ALA A CA  1 
ATOM   1102 C C   . ALA A 1 152 ? 4.029   -8.754  -34.363 1.00 25.34 ? 152 ALA A C   1 
ATOM   1103 O O   . ALA A 1 152 ? 2.932   -8.785  -33.805 1.00 26.96 ? 152 ALA A O   1 
ATOM   1104 C CB  . ALA A 1 152 ? 5.987   -8.268  -33.040 1.00 22.40 ? 152 ALA A CB  1 
ATOM   1105 N N   . GLN A 1 153 ? 4.444   -9.653  -35.234 1.00 26.70 ? 153 GLN A N   1 
ATOM   1106 C CA  . GLN A 1 153 ? 3.668   -10.864 -35.483 1.00 29.34 ? 153 GLN A CA  1 
ATOM   1107 C C   . GLN A 1 153 ? 3.877   -11.847 -34.324 1.00 29.35 ? 153 GLN A C   1 
ATOM   1108 O O   . GLN A 1 153 ? 5.056   -12.243 -34.060 1.00 29.01 ? 153 GLN A O   1 
ATOM   1109 C CB  . GLN A 1 153 ? 4.109   -11.490 -36.791 1.00 29.14 ? 153 GLN A CB  1 
ATOM   1110 C CG  . GLN A 1 153 ? 3.236   -12.598 -37.272 1.00 31.79 ? 153 GLN A CG  1 
ATOM   1111 C CD  . GLN A 1 153 ? 3.294   -12.681 -38.758 1.00 35.74 ? 153 GLN A CD  1 
ATOM   1112 O OE1 . GLN A 1 153 ? 4.324   -12.354 -39.372 1.00 39.02 ? 153 GLN A OE1 1 
ATOM   1113 N NE2 . GLN A 1 153 ? 2.180   -13.069 -39.368 1.00 37.68 ? 153 GLN A NE2 1 
ATOM   1114 O OXT . GLN A 1 153 ? 2.877   -12.222 -33.672 1.00 28.82 ? 153 GLN A OXT 1 
ATOM   1115 N N   . ALA B 1 1   ? -3.459  17.545  -29.701 1.00 41.09 ? 1   ALA B N   1 
ATOM   1116 C CA  . ALA B 1 1   ? -3.458  16.748  -31.037 1.00 39.32 ? 1   ALA B CA  1 
ATOM   1117 C C   . ALA B 1 1   ? -2.379  15.665  -31.177 1.00 36.35 ? 1   ALA B C   1 
ATOM   1118 O O   . ALA B 1 1   ? -1.214  15.926  -30.921 1.00 37.09 ? 1   ALA B O   1 
ATOM   1119 C CB  . ALA B 1 1   ? -3.382  17.724  -32.267 1.00 39.30 ? 1   ALA B CB  1 
ATOM   1120 N N   . THR B 1 2   ? -2.770  14.479  -31.642 1.00 34.70 ? 2   THR B N   1 
ATOM   1121 C CA  . THR B 1 2   ? -1.889  13.312  -31.664 1.00 30.09 ? 2   THR B CA  1 
ATOM   1122 C C   . THR B 1 2   ? -0.874  13.481  -32.844 1.00 29.18 ? 2   THR B C   1 
ATOM   1123 O O   . THR B 1 2   ? -1.131  14.054  -33.926 1.00 28.15 ? 2   THR B O   1 
ATOM   1124 C CB  . THR B 1 2   ? -2.688  11.959  -31.302 1.00 30.69 ? 2   THR B CB  1 
ATOM   1125 O OG1 . THR B 1 2   ? -1.874  10.962  -30.647 1.00 33.90 ? 2   THR B OG1 1 
ATOM   1126 C CG2 . THR B 1 2   ? -3.499  11.369  -32.386 1.00 24.80 ? 2   THR B CG2 1 
ATOM   1127 N N   . LYS B 1 3   ? 0.356   13.183  -32.502 1.00 27.70 ? 3   LYS B N   1 
ATOM   1128 C CA  . LYS B 1 3   ? 1.545   13.474  -33.310 1.00 25.51 ? 3   LYS B CA  1 
ATOM   1129 C C   . LYS B 1 3   ? 2.311   12.171  -33.351 1.00 23.38 ? 3   LYS B C   1 
ATOM   1130 O O   . LYS B 1 3   ? 2.290   11.387  -32.376 1.00 21.12 ? 3   LYS B O   1 
ATOM   1131 C CB  . LYS B 1 3   ? 2.396   14.519  -32.597 1.00 26.27 ? 3   LYS B CB  1 
ATOM   1132 C CG  . LYS B 1 3   ? 2.412   15.926  -33.150 1.00 27.63 ? 3   LYS B CG  1 
ATOM   1133 C CD  . LYS B 1 3   ? 3.771   16.118  -33.850 1.00 36.55 ? 3   LYS B CD  1 
ATOM   1134 C CE  . LYS B 1 3   ? 3.700   17.091  -35.041 1.00 40.31 ? 3   LYS B CE  1 
ATOM   1135 N NZ  . LYS B 1 3   ? 4.187   18.514  -34.733 1.00 42.13 ? 3   LYS B NZ  1 
ATOM   1136 N N   . ALA B 1 4   ? 2.947   11.928  -34.491 1.00 22.05 ? 4   ALA B N   1 
ATOM   1137 C CA  . ALA B 1 4   ? 3.832   10.810  -34.655 1.00 20.40 ? 4   ALA B CA  1 
ATOM   1138 C C   . ALA B 1 4   ? 4.978   11.222  -35.590 1.00 19.78 ? 4   ALA B C   1 
ATOM   1139 O O   . ALA B 1 4   ? 4.893   12.223  -36.288 1.00 20.31 ? 4   ALA B O   1 
ATOM   1140 C CB  . ALA B 1 4   ? 3.075   9.555   -35.149 1.00 19.38 ? 4   ALA B CB  1 
ATOM   1141 N N   . VAL B 1 5   ? 6.049   10.455  -35.556 1.00 19.05 ? 5   VAL B N   1 
ATOM   1142 C CA  . VAL B 1 5   ? 7.257   10.637  -36.398 1.00 18.71 ? 5   VAL B CA  1 
ATOM   1143 C C   . VAL B 1 5   ? 7.782   9.202   -36.822 1.00 18.29 ? 5   VAL B C   1 
ATOM   1144 O O   . VAL B 1 5   ? 7.531   8.253   -36.165 1.00 17.13 ? 5   VAL B O   1 
ATOM   1145 C CB  . VAL B 1 5   ? 8.329   11.422  -35.608 1.00 19.77 ? 5   VAL B CB  1 
ATOM   1146 C CG1 . VAL B 1 5   ? 8.591   10.720  -34.273 1.00 20.11 ? 5   VAL B CG1 1 
ATOM   1147 C CG2 . VAL B 1 5   ? 9.688   11.631  -36.425 1.00 18.87 ? 5   VAL B CG2 1 
ATOM   1148 N N   . CYS B 1 6   ? 8.498   9.110   -37.937 1.00 20.07 ? 6   CYS B N   1 
ATOM   1149 C CA  . CYS B 1 6   ? 9.181   7.936   -38.419 1.00 19.75 ? 6   CYS B CA  1 
ATOM   1150 C C   . CYS B 1 6   ? 10.577  8.429   -38.914 1.00 20.31 ? 6   CYS B C   1 
ATOM   1151 O O   . CYS B 1 6   ? 10.665  9.364   -39.711 1.00 18.73 ? 6   CYS B O   1 
ATOM   1152 C CB  . CYS B 1 6   ? 8.386   7.319   -39.617 1.00 19.55 ? 6   CYS B CB  1 
ATOM   1153 S SG  . CYS B 1 6   ? 8.946   5.673   -40.143 1.00 21.79 ? 6   CYS B SG  1 
ATOM   1154 N N   . VAL B 1 7   ? 11.657  7.777   -38.461 1.00 20.60 ? 7   VAL B N   1 
ATOM   1155 C CA  . VAL B 1 7   ? 13.006  7.949   -39.070 1.00 19.20 ? 7   VAL B CA  1 
ATOM   1156 C C   . VAL B 1 7   ? 13.288  6.811   -40.022 1.00 17.89 ? 7   VAL B C   1 
ATOM   1157 O O   . VAL B 1 7   ? 13.238  5.670   -39.624 1.00 16.78 ? 7   VAL B O   1 
ATOM   1158 C CB  . VAL B 1 7   ? 14.099  8.117   -38.041 1.00 17.99 ? 7   VAL B CB  1 
ATOM   1159 C CG1 . VAL B 1 7   ? 15.470  8.303   -38.762 1.00 21.73 ? 7   VAL B CG1 1 
ATOM   1160 C CG2 . VAL B 1 7   ? 13.809  9.307   -37.194 1.00 20.57 ? 7   VAL B CG2 1 
ATOM   1161 N N   . LEU B 1 8   ? 13.458  7.114   -41.307 1.00 17.88 ? 8   LEU B N   1 
ATOM   1162 C CA  . LEU B 1 8   ? 13.645  6.077   -42.331 1.00 18.50 ? 8   LEU B CA  1 
ATOM   1163 C C   . LEU B 1 8   ? 15.121  5.867   -42.500 1.00 18.96 ? 8   LEU B C   1 
ATOM   1164 O O   . LEU B 1 8   ? 15.822  6.837   -42.710 1.00 19.45 ? 8   LEU B O   1 
ATOM   1165 C CB  . LEU B 1 8   ? 13.094  6.523   -43.703 1.00 18.24 ? 8   LEU B CB  1 
ATOM   1166 C CG  . LEU B 1 8   ? 11.634  6.395   -44.226 1.00 18.11 ? 8   LEU B CG  1 
ATOM   1167 C CD1 . LEU B 1 8   ? 10.665  6.033   -43.288 1.00 16.01 ? 8   LEU B CD1 1 
ATOM   1168 C CD2 . LEU B 1 8   ? 11.263  7.748   -44.968 1.00 21.48 ? 8   LEU B CD2 1 
ATOM   1169 N N   . LYS B 1 9   ? 15.543  4.600   -42.404 1.00 20.14 ? 9   LYS B N   1 
ATOM   1170 C CA  . LYS B 1 9   ? 16.888  4.104   -42.636 1.00 21.59 ? 9   LYS B CA  1 
ATOM   1171 C C   . LYS B 1 9   ? 16.748  2.788   -43.303 1.00 20.28 ? 9   LYS B C   1 
ATOM   1172 O O   . LYS B 1 9   ? 15.834  2.006   -43.012 1.00 18.69 ? 9   LYS B O   1 
ATOM   1173 C CB  . LYS B 1 9   ? 17.642  3.830   -41.291 1.00 21.88 ? 9   LYS B CB  1 
ATOM   1174 C CG  . LYS B 1 9   ? 17.677  5.016   -40.364 1.00 29.67 ? 9   LYS B CG  1 
ATOM   1175 C CD  . LYS B 1 9   ? 18.933  5.890   -40.571 1.00 38.03 ? 9   LYS B CD  1 
ATOM   1176 C CE  . LYS B 1 9   ? 18.647  7.419   -40.712 1.00 39.85 ? 9   LYS B CE  1 
ATOM   1177 N NZ  . LYS B 1 9   ? 19.960  8.052   -41.209 1.00 42.33 ? 9   LYS B NZ  1 
ATOM   1178 N N   . GLY B 1 10  ? 17.705  2.501   -44.164 1.00 21.31 ? 10  GLY B N   1 
ATOM   1179 C CA  . GLY B 1 10  ? 17.916  1.095   -44.644 1.00 22.42 ? 10  GLY B CA  1 
ATOM   1180 C C   . GLY B 1 10  ? 19.405  0.842   -44.923 1.00 23.69 ? 10  GLY B C   1 
ATOM   1181 O O   . GLY B 1 10  ? 20.296  1.406   -44.255 1.00 23.70 ? 10  GLY B O   1 
ATOM   1182 N N   . ASP B 1 11  ? 19.684  0.065   -45.942 1.00 24.84 ? 11  ASP B N   1 
ATOM   1183 C CA  . ASP B 1 11  ? 21.049  -0.486  -46.099 1.00 27.56 ? 11  ASP B CA  1 
ATOM   1184 C C   . ASP B 1 11  ? 21.994  0.395   -46.873 1.00 27.54 ? 11  ASP B C   1 
ATOM   1185 O O   . ASP B 1 11  ? 23.211  0.268   -46.697 1.00 28.55 ? 11  ASP B O   1 
ATOM   1186 C CB  . ASP B 1 11  ? 21.039  -1.952  -46.633 1.00 27.40 ? 11  ASP B CB  1 
ATOM   1187 C CG  . ASP B 1 11  ? 20.603  -2.967  -45.565 1.00 31.56 ? 11  ASP B CG  1 
ATOM   1188 O OD1 . ASP B 1 11  ? 20.881  -2.744  -44.365 1.00 35.50 ? 11  ASP B OD1 1 
ATOM   1189 O OD2 . ASP B 1 11  ? 19.982  -4.019  -45.910 1.00 37.57 ? 11  ASP B OD2 1 
ATOM   1190 N N   . GLY B 1 12  ? 21.435  1.335   -47.660 1.00 26.64 ? 12  GLY B N   1 
ATOM   1191 C CA  . GLY B 1 12  ? 22.222  2.259   -48.454 1.00 24.16 ? 12  GLY B CA  1 
ATOM   1192 C C   . GLY B 1 12  ? 22.051  3.722   -48.157 1.00 23.46 ? 12  GLY B C   1 
ATOM   1193 O O   . GLY B 1 12  ? 22.047  4.171   -46.965 1.00 24.37 ? 12  GLY B O   1 
ATOM   1194 N N   . PRO B 1 13  ? 21.989  4.530   -49.224 1.00 22.12 ? 13  PRO B N   1 
ATOM   1195 C CA  . PRO B 1 13  ? 21.896  5.954   -48.950 1.00 20.30 ? 13  PRO B CA  1 
ATOM   1196 C C   . PRO B 1 13  ? 20.483  6.532   -48.525 1.00 20.78 ? 13  PRO B C   1 
ATOM   1197 O O   . PRO B 1 13  ? 20.331  7.764   -48.261 1.00 15.22 ? 13  PRO B O   1 
ATOM   1198 C CB  . PRO B 1 13  ? 22.395  6.546   -50.240 1.00 21.08 ? 13  PRO B CB  1 
ATOM   1199 C CG  . PRO B 1 13  ? 21.862  5.562   -51.257 1.00 20.26 ? 13  PRO B CG  1 
ATOM   1200 C CD  . PRO B 1 13  ? 22.103  4.243   -50.675 1.00 20.73 ? 13  PRO B CD  1 
ATOM   1201 N N   . VAL B 1 14  ? 19.463  5.676   -48.468 1.00 19.89 ? 14  VAL B N   1 
ATOM   1202 C CA  . VAL B 1 14  ? 18.125  6.254   -48.331 1.00 21.36 ? 14  VAL B CA  1 
ATOM   1203 C C   . VAL B 1 14  ? 17.820  6.571   -46.869 1.00 22.22 ? 14  VAL B C   1 
ATOM   1204 O O   . VAL B 1 14  ? 17.925  5.692   -45.982 1.00 22.82 ? 14  VAL B O   1 
ATOM   1205 C CB  . VAL B 1 14  ? 16.984  5.440   -49.057 1.00 20.92 ? 14  VAL B CB  1 
ATOM   1206 C CG1 . VAL B 1 14  ? 15.681  6.207   -48.907 1.00 21.82 ? 14  VAL B CG1 1 
ATOM   1207 C CG2 . VAL B 1 14  ? 17.269  5.273   -50.506 1.00 17.34 ? 14  VAL B CG2 1 
ATOM   1208 N N   . GLN B 1 15  ? 17.447  7.821   -46.620 1.00 22.75 ? 15  GLN B N   1 
ATOM   1209 C CA  . GLN B 1 15  ? 17.133  8.323   -45.251 1.00 23.62 ? 15  GLN B CA  1 
ATOM   1210 C C   . GLN B 1 15  ? 16.184  9.533   -45.246 1.00 23.96 ? 15  GLN B C   1 
ATOM   1211 O O   . GLN B 1 15  ? 16.099  10.319  -46.227 1.00 23.05 ? 15  GLN B O   1 
ATOM   1212 C CB  . GLN B 1 15  ? 18.393  8.664   -44.442 1.00 23.14 ? 15  GLN B CB  1 
ATOM   1213 C CG  . GLN B 1 15  ? 19.359  9.634   -45.110 1.00 24.43 ? 15  GLN B CG  1 
ATOM   1214 C CD  . GLN B 1 15  ? 20.774  9.594   -44.515 1.00 26.19 ? 15  GLN B CD  1 
ATOM   1215 O OE1 . GLN B 1 15  ? 20.970  9.726   -43.287 1.00 31.13 ? 15  GLN B OE1 1 
ATOM   1216 N NE2 . GLN B 1 15  ? 21.755  9.370   -45.373 1.00 29.76 ? 15  GLN B NE2 1 
ATOM   1217 N N   . GLY B 1 16  ? 15.473  9.668   -44.126 1.00 23.33 ? 16  GLY B N   1 
ATOM   1218 C CA  . GLY B 1 16  ? 14.653  10.837  -43.896 1.00 22.21 ? 16  GLY B CA  1 
ATOM   1219 C C   . GLY B 1 16  ? 13.699  10.802  -42.711 1.00 21.87 ? 16  GLY B C   1 
ATOM   1220 O O   . GLY B 1 16  ? 13.670  9.863   -41.958 1.00 20.13 ? 16  GLY B O   1 
ATOM   1221 N N   . ILE B 1 17  ? 12.911  11.867  -42.577 1.00 21.86 ? 17  ILE B N   1 
ATOM   1222 C CA  . ILE B 1 17  ? 12.044  12.063  -41.423 1.00 21.01 ? 17  ILE B CA  1 
ATOM   1223 C C   . ILE B 1 17  ? 10.664  12.536  -41.858 1.00 20.06 ? 17  ILE B C   1 
ATOM   1224 O O   . ILE B 1 17  ? 10.537  13.552  -42.589 1.00 19.30 ? 17  ILE B O   1 
ATOM   1225 C CB  . ILE B 1 17  ? 12.636  13.022  -40.380 1.00 21.78 ? 17  ILE B CB  1 
ATOM   1226 C CG1 . ILE B 1 17  ? 14.030  12.535  -39.932 1.00 22.15 ? 17  ILE B CG1 1 
ATOM   1227 C CG2 . ILE B 1 17  ? 11.647  13.196  -39.196 1.00 20.66 ? 17  ILE B CG2 1 
ATOM   1228 C CD1 . ILE B 1 17  ? 14.917  13.652  -39.344 1.00 28.29 ? 17  ILE B CD1 1 
ATOM   1229 N N   . ILE B 1 18  ? 9.664   11.750  -41.416 1.00 16.02 ? 18  ILE B N   1 
ATOM   1230 C CA  . ILE B 1 18  ? 8.283   11.830  -41.873 1.00 16.30 ? 18  ILE B CA  1 
ATOM   1231 C C   . ILE B 1 18  ? 7.488   12.075  -40.611 1.00 16.32 ? 18  ILE B C   1 
ATOM   1232 O O   . ILE B 1 18  ? 7.611   11.343  -39.675 1.00 16.24 ? 18  ILE B O   1 
ATOM   1233 C CB  . ILE B 1 18  ? 7.877   10.504  -42.699 1.00 16.85 ? 18  ILE B CB  1 
ATOM   1234 C CG1 . ILE B 1 18  ? 8.800   10.352  -43.954 1.00 12.55 ? 18  ILE B CG1 1 
ATOM   1235 C CG2 . ILE B 1 18  ? 6.360   10.419  -43.027 1.00 11.37 ? 18  ILE B CG2 1 
ATOM   1236 C CD1 . ILE B 1 18  ? 8.570   11.330  -44.996 1.00 12.50 ? 18  ILE B CD1 1 
ATOM   1237 N N   . ASN B 1 19  ? 6.802   13.212  -40.567 1.00 17.22 ? 19  ASN B N   1 
ATOM   1238 C CA  . ASN B 1 19  ? 5.990   13.628  -39.435 1.00 16.25 ? 19  ASN B CA  1 
ATOM   1239 C C   . ASN B 1 19  ? 4.548   13.263  -39.761 1.00 16.49 ? 19  ASN B C   1 
ATOM   1240 O O   . ASN B 1 19  ? 4.208   13.185  -40.889 1.00 15.05 ? 19  ASN B O   1 
ATOM   1241 C CB  . ASN B 1 19  ? 6.082   15.154  -39.230 1.00 15.75 ? 19  ASN B CB  1 
ATOM   1242 C CG  . ASN B 1 19  ? 7.471   15.589  -38.829 1.00 14.13 ? 19  ASN B CG  1 
ATOM   1243 O OD1 . ASN B 1 19  ? 7.972   15.234  -37.781 1.00 14.05 ? 19  ASN B OD1 1 
ATOM   1244 N ND2 . ASN B 1 19  ? 8.030   16.428  -39.597 1.00 7.85  ? 19  ASN B ND2 1 
ATOM   1245 N N   . PHE B 1 20  ? 3.727   13.074  -38.740 1.00 17.82 ? 20  PHE B N   1 
ATOM   1246 C CA  . PHE B 1 20  ? 2.306   12.712  -38.874 1.00 19.01 ? 20  PHE B CA  1 
ATOM   1247 C C   . PHE B 1 20  ? 1.603   13.587  -37.813 1.00 20.46 ? 20  PHE B C   1 
ATOM   1248 O O   . PHE B 1 20  ? 2.028   13.646  -36.677 1.00 20.24 ? 20  PHE B O   1 
ATOM   1249 C CB  . PHE B 1 20  ? 2.034   11.214  -38.505 1.00 18.59 ? 20  PHE B CB  1 
ATOM   1250 C CG  . PHE B 1 20  ? 2.799   10.213  -39.315 1.00 17.94 ? 20  PHE B CG  1 
ATOM   1251 C CD1 . PHE B 1 20  ? 4.158   9.999   -39.078 1.00 19.08 ? 20  PHE B CD1 1 
ATOM   1252 C CD2 . PHE B 1 20  ? 2.163   9.458   -40.332 1.00 15.61 ? 20  PHE B CD2 1 
ATOM   1253 C CE1 . PHE B 1 20  ? 4.879   9.077   -39.814 1.00 15.44 ? 20  PHE B CE1 1 
ATOM   1254 C CE2 . PHE B 1 20  ? 2.892   8.492   -41.069 1.00 15.30 ? 20  PHE B CE2 1 
ATOM   1255 C CZ  . PHE B 1 20  ? 4.236   8.327   -40.824 1.00 16.59 ? 20  PHE B CZ  1 
ATOM   1256 N N   . GLU B 1 21  ? 0.558   14.302  -38.206 1.00 23.05 ? 21  GLU B N   1 
ATOM   1257 C CA  . GLU B 1 21  ? -0.301  15.003  -37.285 1.00 23.94 ? 21  GLU B CA  1 
ATOM   1258 C C   . GLU B 1 21  ? -1.794  14.762  -37.605 1.00 23.94 ? 21  GLU B C   1 
ATOM   1259 O O   . GLU B 1 21  ? -2.207  14.864  -38.788 1.00 22.38 ? 21  GLU B O   1 
ATOM   1260 C CB  . GLU B 1 21  ? 0.007   16.523  -37.291 1.00 24.89 ? 21  GLU B CB  1 
ATOM   1261 C CG  . GLU B 1 21  ? -0.772  17.222  -36.191 1.00 30.18 ? 21  GLU B CG  1 
ATOM   1262 C CD  . GLU B 1 21  ? -0.248  18.598  -35.882 1.00 36.65 ? 21  GLU B CD  1 
ATOM   1263 O OE1 . GLU B 1 21  ? -0.428  19.496  -36.750 1.00 39.53 ? 21  GLU B OE1 1 
ATOM   1264 O OE2 . GLU B 1 21  ? 0.305   18.764  -34.767 1.00 38.54 ? 21  GLU B OE2 1 
ATOM   1265 N N   . GLN B 1 22  ? -2.553  14.415  -36.540 1.00 24.03 ? 22  GLN B N   1 
ATOM   1266 C CA  . GLN B 1 22  ? -3.996  14.159  -36.547 1.00 24.32 ? 22  GLN B CA  1 
ATOM   1267 C C   . GLN B 1 22  ? -4.681  14.885  -35.369 1.00 25.95 ? 22  GLN B C   1 
ATOM   1268 O O   . GLN B 1 22  ? -4.784  14.331  -34.270 1.00 26.13 ? 22  GLN B O   1 
ATOM   1269 C CB  . GLN B 1 22  ? -4.318  12.656  -36.481 1.00 23.93 ? 22  GLN B CB  1 
ATOM   1270 C CG  . GLN B 1 22  ? -5.793  12.310  -36.836 1.00 19.77 ? 22  GLN B CG  1 
ATOM   1271 C CD  . GLN B 1 22  ? -6.166  10.830  -36.748 1.00 21.68 ? 22  GLN B CD  1 
ATOM   1272 O OE1 . GLN B 1 22  ? -5.553  10.038  -36.038 1.00 14.41 ? 22  GLN B OE1 1 
ATOM   1273 N NE2 . GLN B 1 22  ? -7.205  10.471  -37.450 1.00 19.43 ? 22  GLN B NE2 1 
ATOM   1274 N N   . LYS B 1 23  ? -5.114  16.126  -35.580 1.00 28.98 ? 23  LYS B N   1 
ATOM   1275 C CA  . LYS B 1 23  ? -5.742  16.919  -34.485 1.00 32.11 ? 23  LYS B CA  1 
ATOM   1276 C C   . LYS B 1 23  ? -7.120  16.421  -34.052 1.00 31.98 ? 23  LYS B C   1 
ATOM   1277 O O   . LYS B 1 23  ? -7.383  16.352  -32.842 1.00 34.80 ? 23  LYS B O   1 
ATOM   1278 C CB  . LYS B 1 23  ? -5.728  18.431  -34.718 1.00 32.18 ? 23  LYS B CB  1 
ATOM   1279 C CG  . LYS B 1 23  ? -4.328  19.080  -34.429 1.00 33.53 ? 23  LYS B CG  1 
ATOM   1280 C CD  . LYS B 1 23  ? -4.210  20.537  -34.940 1.00 35.46 ? 23  LYS B CD  1 
ATOM   1281 C CE  . LYS B 1 23  ? -2.786  21.219  -34.742 1.00 38.55 ? 23  LYS B CE  1 
ATOM   1282 N NZ  . LYS B 1 23  ? -2.343  21.564  -33.303 1.00 42.41 ? 23  LYS B NZ  1 
ATOM   1283 N N   . GLU B 1 24  ? -7.945  15.967  -34.995 1.00 31.77 ? 24  GLU B N   1 
ATOM   1284 C CA  . GLU B 1 24  ? -9.192  15.245  -34.636 1.00 31.59 ? 24  GLU B CA  1 
ATOM   1285 C C   . GLU B 1 24  ? -9.170  13.728  -34.947 1.00 29.27 ? 24  GLU B C   1 
ATOM   1286 O O   . GLU B 1 24  ? -8.773  13.306  -35.998 1.00 29.59 ? 24  GLU B O   1 
ATOM   1287 C CB  . GLU B 1 24  ? -10.464 15.949  -35.178 1.00 31.79 ? 24  GLU B CB  1 
ATOM   1288 C CG  . GLU B 1 24  ? -10.523 16.150  -36.699 1.00 38.56 ? 24  GLU B CG  1 
ATOM   1289 C CD  . GLU B 1 24  ? -10.332 17.612  -37.115 1.00 47.65 ? 24  GLU B CD  1 
ATOM   1290 O OE1 . GLU B 1 24  ? -9.430  17.869  -37.996 1.00 52.87 ? 24  GLU B OE1 1 
ATOM   1291 O OE2 . GLU B 1 24  ? -11.089 18.482  -36.586 1.00 44.42 ? 24  GLU B OE2 1 
ATOM   1292 N N   . SER B 1 25  ? -9.594  12.925  -34.008 1.00 26.77 ? 25  SER B N   1 
ATOM   1293 C CA  . SER B 1 25  ? -9.428  11.492  -34.130 1.00 27.89 ? 25  SER B CA  1 
ATOM   1294 C C   . SER B 1 25  ? -10.236 10.874  -35.320 1.00 27.25 ? 25  SER B C   1 
ATOM   1295 O O   . SER B 1 25  ? -10.016 9.729   -35.696 1.00 26.59 ? 25  SER B O   1 
ATOM   1296 C CB  . SER B 1 25  ? -9.752  10.791  -32.794 1.00 27.17 ? 25  SER B CB  1 
ATOM   1297 O OG  . SER B 1 25  ? -11.123 10.986  -32.462 1.00 29.41 ? 25  SER B OG  1 
ATOM   1298 N N   . ASN B 1 26  ? -11.099 11.679  -35.934 1.00 28.20 ? 26  ASN B N   1 
ATOM   1299 C CA  . ASN B 1 26  ? -11.876 11.301  -37.106 1.00 29.14 ? 26  ASN B CA  1 
ATOM   1300 C C   . ASN B 1 26  ? -11.654 12.164  -38.333 1.00 30.41 ? 26  ASN B C   1 
ATOM   1301 O O   . ASN B 1 26  ? -12.267 11.939  -39.346 1.00 31.38 ? 26  ASN B O   1 
ATOM   1302 C CB  . ASN B 1 26  ? -13.361 11.290  -36.806 1.00 30.13 ? 26  ASN B CB  1 
ATOM   1303 C CG  . ASN B 1 26  ? -13.855 12.566  -36.127 1.00 29.04 ? 26  ASN B CG  1 
ATOM   1304 O OD1 . ASN B 1 26  ? -14.882 12.522  -35.561 1.00 36.47 ? 26  ASN B OD1 1 
ATOM   1305 N ND2 . ASN B 1 26  ? -13.141 13.681  -36.212 1.00 30.90 ? 26  ASN B ND2 1 
ATOM   1306 N N   . GLY B 1 27  ? -10.805 13.185  -38.211 1.00 30.77 ? 27  GLY B N   1 
ATOM   1307 C CA  . GLY B 1 27  ? -10.271 13.896  -39.360 1.00 29.23 ? 27  GLY B CA  1 
ATOM   1308 C C   . GLY B 1 27  ? -9.125  13.175  -40.054 1.00 28.33 ? 27  GLY B C   1 
ATOM   1309 O O   . GLY B 1 27  ? -8.763  12.029  -39.702 1.00 27.95 ? 27  GLY B O   1 
ATOM   1310 N N   . PRO B 1 28  ? -8.658  13.778  -41.145 1.00 27.99 ? 28  PRO B N   1 
ATOM   1311 C CA  . PRO B 1 28  ? -7.496  13.208  -41.809 1.00 27.38 ? 28  PRO B CA  1 
ATOM   1312 C C   . PRO B 1 28  ? -6.199  13.318  -41.002 1.00 26.42 ? 28  PRO B C   1 
ATOM   1313 O O   . PRO B 1 28  ? -6.069  14.171  -40.076 1.00 26.13 ? 28  PRO B O   1 
ATOM   1314 C CB  . PRO B 1 28  ? -7.391  14.021  -43.134 1.00 26.97 ? 28  PRO B CB  1 
ATOM   1315 C CG  . PRO B 1 28  ? -8.210  15.229  -42.972 1.00 26.78 ? 28  PRO B CG  1 
ATOM   1316 C CD  . PRO B 1 28  ? -9.245  14.921  -41.892 1.00 28.42 ? 28  PRO B CD  1 
ATOM   1317 N N   . VAL B 1 29  ? -5.232  12.473  -41.404 1.00 25.73 ? 29  VAL B N   1 
ATOM   1318 C CA  . VAL B 1 29  ? -3.802  12.577  -40.993 1.00 24.40 ? 29  VAL B CA  1 
ATOM   1319 C C   . VAL B 1 29  ? -2.907  13.286  -42.066 1.00 24.48 ? 29  VAL B C   1 
ATOM   1320 O O   . VAL B 1 29  ? -2.776  12.830  -43.230 1.00 23.53 ? 29  VAL B O   1 
ATOM   1321 C CB  . VAL B 1 29  ? -3.205  11.181  -40.629 1.00 24.46 ? 29  VAL B CB  1 
ATOM   1322 C CG1 . VAL B 1 29  ? -1.723  11.262  -40.136 1.00 20.79 ? 29  VAL B CG1 1 
ATOM   1323 C CG2 . VAL B 1 29  ? -4.105  10.441  -39.617 1.00 21.98 ? 29  VAL B CG2 1 
ATOM   1324 N N   . LYS B 1 30  ? -2.282  14.369  -41.621 1.00 24.54 ? 30  LYS B N   1 
ATOM   1325 C CA  . LYS B 1 30  ? -1.236  15.112  -42.362 1.00 25.97 ? 30  LYS B CA  1 
ATOM   1326 C C   . LYS B 1 30  ? 0.109   14.397  -42.266 1.00 25.28 ? 30  LYS B C   1 
ATOM   1327 O O   . LYS B 1 30  ? 0.654   14.218  -41.170 1.00 24.43 ? 30  LYS B O   1 
ATOM   1328 C CB  . LYS B 1 30  ? -1.055  16.549  -41.835 1.00 24.39 ? 30  LYS B CB  1 
ATOM   1329 C CG  . LYS B 1 30  ? -2.398  17.355  -41.765 1.00 29.99 ? 30  LYS B CG  1 
ATOM   1330 C CD  . LYS B 1 30  ? -2.298  18.873  -41.262 1.00 28.16 ? 30  LYS B CD  1 
ATOM   1331 C CE  . LYS B 1 30  ? -3.479  19.681  -41.833 1.00 30.25 ? 30  LYS B CE  1 
ATOM   1332 N NZ  . LYS B 1 30  ? -3.348  21.196  -41.901 1.00 32.90 ? 30  LYS B NZ  1 
ATOM   1333 N N   . VAL B 1 31  ? 0.636   13.996  -43.414 1.00 25.00 ? 31  VAL B N   1 
ATOM   1334 C CA  . VAL B 1 31  ? 1.937   13.370  -43.410 1.00 25.27 ? 31  VAL B CA  1 
ATOM   1335 C C   . VAL B 1 31  ? 2.916   14.221  -44.218 1.00 24.82 ? 31  VAL B C   1 
ATOM   1336 O O   . VAL B 1 31  ? 2.601   14.683  -45.333 1.00 24.83 ? 31  VAL B O   1 
ATOM   1337 C CB  . VAL B 1 31  ? 1.909   11.743  -43.558 1.00 26.65 ? 31  VAL B CB  1 
ATOM   1338 C CG1 . VAL B 1 31  ? 0.626   11.199  -44.097 1.00 25.68 ? 31  VAL B CG1 1 
ATOM   1339 C CG2 . VAL B 1 31  ? 3.197   11.150  -44.187 1.00 24.86 ? 31  VAL B CG2 1 
ATOM   1340 N N   . TRP B 1 32  ? 4.040   14.564  -43.587 1.00 23.01 ? 32  TRP B N   1 
ATOM   1341 C CA  . TRP B 1 32  ? 4.983   15.403  -44.255 1.00 22.26 ? 32  TRP B CA  1 
ATOM   1342 C C   . TRP B 1 32  ? 6.410   15.182  -43.784 1.00 20.91 ? 32  TRP B C   1 
ATOM   1343 O O   . TRP B 1 32  ? 6.685   14.912  -42.631 1.00 20.37 ? 32  TRP B O   1 
ATOM   1344 C CB  . TRP B 1 32  ? 4.592   16.917  -44.096 1.00 22.37 ? 32  TRP B CB  1 
ATOM   1345 C CG  . TRP B 1 32  ? 4.915   17.493  -42.758 1.00 21.11 ? 32  TRP B CG  1 
ATOM   1346 C CD1 . TRP B 1 32  ? 5.990   18.233  -42.448 1.00 22.76 ? 32  TRP B CD1 1 
ATOM   1347 C CD2 . TRP B 1 32  ? 4.124   17.400  -41.543 1.00 19.91 ? 32  TRP B CD2 1 
ATOM   1348 N NE1 . TRP B 1 32  ? 5.952   18.581  -41.121 1.00 23.36 ? 32  TRP B NE1 1 
ATOM   1349 C CE2 . TRP B 1 32  ? 4.790   18.108  -40.567 1.00 16.55 ? 32  TRP B CE2 1 
ATOM   1350 C CE3 . TRP B 1 32  ? 2.885   16.802  -41.221 1.00 19.20 ? 32  TRP B CE3 1 
ATOM   1351 C CZ2 . TRP B 1 32  ? 4.317   18.204  -39.262 1.00 23.10 ? 32  TRP B CZ2 1 
ATOM   1352 C CZ3 . TRP B 1 32  ? 2.399   16.918  -39.965 1.00 21.80 ? 32  TRP B CZ3 1 
ATOM   1353 C CH2 . TRP B 1 32  ? 3.131   17.590  -38.965 1.00 24.03 ? 32  TRP B CH2 1 
ATOM   1354 N N   . GLY B 1 33  ? 7.347   15.356  -44.685 1.00 20.98 ? 33  GLY B N   1 
ATOM   1355 C CA  . GLY B 1 33  ? 8.713   15.492  -44.234 1.00 21.29 ? 33  GLY B CA  1 
ATOM   1356 C C   . GLY B 1 33  ? 9.597   15.544  -45.448 1.00 21.95 ? 33  GLY B C   1 
ATOM   1357 O O   . GLY B 1 33  ? 9.216   16.112  -46.456 1.00 19.90 ? 33  GLY B O   1 
ATOM   1358 N N   . SER B 1 34  ? 10.762  14.901  -45.343 1.00 23.66 ? 34  SER B N   1 
ATOM   1359 C CA  . SER B 1 34  ? 11.663  14.735  -46.483 1.00 25.47 ? 34  SER B CA  1 
ATOM   1360 C C   . SER B 1 34  ? 12.429  13.395  -46.492 1.00 24.65 ? 34  SER B C   1 
ATOM   1361 O O   . SER B 1 34  ? 12.789  12.846  -45.428 1.00 24.96 ? 34  SER B O   1 
ATOM   1362 C CB  . SER B 1 34  ? 12.636  15.909  -46.528 1.00 25.98 ? 34  SER B CB  1 
ATOM   1363 O OG  . SER B 1 34  ? 13.428  15.917  -47.697 1.00 30.17 ? 34  SER B OG  1 
ATOM   1364 N N   . ILE B 1 35  ? 12.676  12.891  -47.710 1.00 24.43 ? 35  ILE B N   1 
ATOM   1365 C CA  . ILE B 1 35  ? 13.569  11.736  -47.968 1.00 21.49 ? 35  ILE B CA  1 
ATOM   1366 C C   . ILE B 1 35  ? 14.687  12.152  -48.992 1.00 21.15 ? 35  ILE B C   1 
ATOM   1367 O O   . ILE B 1 35  ? 14.376  12.691  -50.023 1.00 21.23 ? 35  ILE B O   1 
ATOM   1368 C CB  . ILE B 1 35  ? 12.739  10.534  -48.449 1.00 21.52 ? 35  ILE B CB  1 
ATOM   1369 C CG1 . ILE B 1 35  ? 11.516  10.278  -47.523 1.00 22.34 ? 35  ILE B CG1 1 
ATOM   1370 C CG2 . ILE B 1 35  ? 13.587  9.227   -48.529 1.00 21.70 ? 35  ILE B CG2 1 
ATOM   1371 C CD1 . ILE B 1 35  ? 10.332  9.584   -48.172 1.00 15.35 ? 35  ILE B CD1 1 
ATOM   1372 N N   . LYS B 1 36  ? 15.964  11.884  -48.679 1.00 20.85 ? 36  LYS B N   1 
ATOM   1373 C CA  . LYS B 1 36  ? 17.154  11.927  -49.599 1.00 20.38 ? 36  LYS B CA  1 
ATOM   1374 C C   . LYS B 1 36  ? 17.718  10.486  -49.908 1.00 20.49 ? 36  LYS B C   1 
ATOM   1375 O O   . LYS B 1 36  ? 17.206  9.499   -49.386 1.00 17.97 ? 36  LYS B O   1 
ATOM   1376 C CB  . LYS B 1 36  ? 18.214  12.866  -48.958 1.00 21.18 ? 36  LYS B CB  1 
ATOM   1377 C CG  . LYS B 1 36  ? 18.876  12.249  -47.615 1.00 22.07 ? 36  LYS B CG  1 
ATOM   1378 C CD  . LYS B 1 36  ? 19.046  13.266  -46.453 1.00 22.83 ? 36  LYS B CD  1 
ATOM   1379 C CE  . LYS B 1 36  ? 20.242  14.163  -46.720 1.00 22.89 ? 36  LYS B CE  1 
ATOM   1380 N NZ  . LYS B 1 36  ? 21.332  13.792  -45.814 1.00 25.50 ? 36  LYS B NZ  1 
ATOM   1381 N N   . GLY B 1 37  ? 18.728  10.381  -50.788 1.00 20.12 ? 37  GLY B N   1 
ATOM   1382 C CA  . GLY B 1 37  ? 19.291  9.126   -51.280 1.00 19.65 ? 37  GLY B CA  1 
ATOM   1383 C C   . GLY B 1 37  ? 18.602  8.357   -52.380 1.00 20.16 ? 37  GLY B C   1 
ATOM   1384 O O   . GLY B 1 37  ? 18.919  7.196   -52.647 1.00 19.59 ? 37  GLY B O   1 
ATOM   1385 N N   . LEU B 1 38  ? 17.620  9.001   -53.002 1.00 21.04 ? 38  LEU B N   1 
ATOM   1386 C CA  . LEU B 1 38  ? 16.622  8.384   -53.865 1.00 21.88 ? 38  LEU B CA  1 
ATOM   1387 C C   . LEU B 1 38  ? 17.006  8.579   -55.344 1.00 22.39 ? 38  LEU B C   1 
ATOM   1388 O O   . LEU B 1 38  ? 17.525  9.640   -55.708 1.00 22.92 ? 38  LEU B O   1 
ATOM   1389 C CB  . LEU B 1 38  ? 15.254  9.056   -53.558 1.00 21.56 ? 38  LEU B CB  1 
ATOM   1390 C CG  . LEU B 1 38  ? 14.122  8.337   -52.795 1.00 22.42 ? 38  LEU B CG  1 
ATOM   1391 C CD1 . LEU B 1 38  ? 14.404  6.895   -52.230 1.00 12.22 ? 38  LEU B CD1 1 
ATOM   1392 C CD2 . LEU B 1 38  ? 13.258  9.162   -51.850 1.00 22.17 ? 38  LEU B CD2 1 
ATOM   1393 N N   . THR B 1 39  ? 16.794  7.561   -56.172 1.00 23.66 ? 39  THR B N   1 
ATOM   1394 C CA  . THR B 1 39  ? 16.769  7.740   -57.640 1.00 27.34 ? 39  THR B CA  1 
ATOM   1395 C C   . THR B 1 39  ? 15.605  8.646   -58.056 1.00 28.97 ? 39  THR B C   1 
ATOM   1396 O O   . THR B 1 39  ? 14.474  8.530   -57.500 1.00 30.71 ? 39  THR B O   1 
ATOM   1397 C CB  . THR B 1 39  ? 16.554  6.448   -58.436 1.00 27.29 ? 39  THR B CB  1 
ATOM   1398 O OG1 . THR B 1 39  ? 15.389  5.825   -57.936 1.00 29.77 ? 39  THR B OG1 1 
ATOM   1399 C CG2 . THR B 1 39  ? 17.724  5.483   -58.312 1.00 23.43 ? 39  THR B CG2 1 
ATOM   1400 N N   . GLU B 1 40  ? 15.869  9.538   -59.014 1.00 28.31 ? 40  GLU B N   1 
ATOM   1401 C CA  . GLU B 1 40  ? 14.838  10.425  -59.543 1.00 28.97 ? 40  GLU B CA  1 
ATOM   1402 C C   . GLU B 1 40  ? 13.546  9.711   -59.877 1.00 27.67 ? 40  GLU B C   1 
ATOM   1403 O O   . GLU B 1 40  ? 13.522  8.684   -60.525 1.00 27.78 ? 40  GLU B O   1 
ATOM   1404 C CB  . GLU B 1 40  ? 15.340  11.101  -60.804 1.00 30.43 ? 40  GLU B CB  1 
ATOM   1405 C CG  . GLU B 1 40  ? 14.664  12.389  -61.131 1.00 33.20 ? 40  GLU B CG  1 
ATOM   1406 C CD  . GLU B 1 40  ? 15.445  13.157  -62.201 1.00 39.11 ? 40  GLU B CD  1 
ATOM   1407 O OE1 . GLU B 1 40  ? 16.437  12.580  -62.734 1.00 39.77 ? 40  GLU B OE1 1 
ATOM   1408 O OE2 . GLU B 1 40  ? 15.075  14.320  -62.510 1.00 38.91 ? 40  GLU B OE2 1 
ATOM   1409 N N   . GLY B 1 41  ? 12.448  10.263  -59.419 1.00 27.32 ? 41  GLY B N   1 
ATOM   1410 C CA  . GLY B 1 41  ? 11.166  9.792   -59.883 1.00 25.69 ? 41  GLY B CA  1 
ATOM   1411 C C   . GLY B 1 41  ? 10.323  9.427   -58.710 1.00 25.21 ? 41  GLY B C   1 
ATOM   1412 O O   . GLY B 1 41  ? 10.543  9.900   -57.614 1.00 26.37 ? 41  GLY B O   1 
ATOM   1413 N N   . LEU B 1 42  ? 9.448   8.457   -58.951 1.00 24.74 ? 42  LEU B N   1 
ATOM   1414 C CA  . LEU B 1 42  ? 8.344   8.115   -58.144 1.00 22.06 ? 42  LEU B CA  1 
ATOM   1415 C C   . LEU B 1 42  ? 8.707   6.850   -57.357 1.00 22.03 ? 42  LEU B C   1 
ATOM   1416 O O   . LEU B 1 42  ? 9.244   5.855   -57.945 1.00 20.76 ? 42  LEU B O   1 
ATOM   1417 C CB  . LEU B 1 42  ? 7.222   7.834   -59.133 1.00 22.77 ? 42  LEU B CB  1 
ATOM   1418 C CG  . LEU B 1 42  ? 5.849   8.460   -59.178 1.00 21.42 ? 42  LEU B CG  1 
ATOM   1419 C CD1 . LEU B 1 42  ? 5.966   9.950   -58.913 1.00 18.74 ? 42  LEU B CD1 1 
ATOM   1420 C CD2 . LEU B 1 42  ? 5.179   8.126   -60.526 1.00 22.80 ? 42  LEU B CD2 1 
ATOM   1421 N N   . HIS B 1 43  ? 8.434   6.893   -56.040 1.00 19.52 ? 43  HIS B N   1 
ATOM   1422 C CA  . HIS B 1 43  ? 8.823   5.824   -55.136 1.00 20.21 ? 43  HIS B CA  1 
ATOM   1423 C C   . HIS B 1 43  ? 7.654   5.360   -54.259 1.00 19.39 ? 43  HIS B C   1 
ATOM   1424 O O   . HIS B 1 43  ? 7.064   6.164   -53.573 1.00 19.22 ? 43  HIS B O   1 
ATOM   1425 C CB  . HIS B 1 43  ? 10.044  6.262   -54.304 1.00 20.23 ? 43  HIS B CB  1 
ATOM   1426 C CG  . HIS B 1 43  ? 11.316  6.375   -55.126 1.00 20.64 ? 43  HIS B CG  1 
ATOM   1427 N ND1 . HIS B 1 43  ? 12.119  5.285   -55.395 1.00 23.79 ? 43  HIS B ND1 1 
ATOM   1428 C CD2 . HIS B 1 43  ? 11.923  7.437   -55.709 1.00 13.71 ? 43  HIS B CD2 1 
ATOM   1429 C CE1 . HIS B 1 43  ? 13.158  5.669   -56.117 1.00 19.94 ? 43  HIS B CE1 1 
ATOM   1430 N NE2 . HIS B 1 43  ? 13.055  6.962   -56.339 1.00 16.54 ? 43  HIS B NE2 1 
ATOM   1431 N N   . GLY B 1 44  ? 7.314   4.074   -54.280 1.00 17.68 ? 44  GLY B N   1 
ATOM   1432 C CA  . GLY B 1 44  ? 6.145   3.665   -53.525 1.00 17.41 ? 44  GLY B CA  1 
ATOM   1433 C C   . GLY B 1 44  ? 6.247   3.960   -52.036 1.00 18.22 ? 44  GLY B C   1 
ATOM   1434 O O   . GLY B 1 44  ? 7.344   4.037   -51.477 1.00 16.25 ? 44  GLY B O   1 
ATOM   1435 N N   . PHE B 1 45  ? 5.109   4.135   -51.367 1.00 18.65 ? 45  PHE B N   1 
ATOM   1436 C CA  . PHE B 1 45  ? 5.171   4.770   -50.061 1.00 18.72 ? 45  PHE B CA  1 
ATOM   1437 C C   . PHE B 1 45  ? 4.035   4.208   -49.260 1.00 18.66 ? 45  PHE B C   1 
ATOM   1438 O O   . PHE B 1 45  ? 2.900   4.521   -49.521 1.00 16.80 ? 45  PHE B O   1 
ATOM   1439 C CB  . PHE B 1 45  ? 5.147   6.296   -50.229 1.00 19.77 ? 45  PHE B CB  1 
ATOM   1440 C CG  . PHE B 1 45  ? 5.381   7.092   -48.944 1.00 20.91 ? 45  PHE B CG  1 
ATOM   1441 C CD1 . PHE B 1 45  ? 6.634   7.209   -48.396 1.00 19.84 ? 45  PHE B CD1 1 
ATOM   1442 C CD2 . PHE B 1 45  ? 4.318   7.810   -48.349 1.00 27.22 ? 45  PHE B CD2 1 
ATOM   1443 C CE1 . PHE B 1 45  ? 6.874   8.005   -47.192 1.00 22.35 ? 45  PHE B CE1 1 
ATOM   1444 C CE2 . PHE B 1 45  ? 4.506   8.627   -47.200 1.00 22.91 ? 45  PHE B CE2 1 
ATOM   1445 C CZ  . PHE B 1 45  ? 5.819   8.720   -46.616 1.00 25.51 ? 45  PHE B CZ  1 
ATOM   1446 N N   . HIS B 1 46  ? 4.374   3.249   -48.360 1.00 18.11 ? 46  HIS B N   1 
ATOM   1447 C CA  . HIS B 1 46  ? 3.389   2.365   -47.797 1.00 17.80 ? 46  HIS B CA  1 
ATOM   1448 C C   . HIS B 1 46  ? 3.578   2.204   -46.337 1.00 16.50 ? 46  HIS B C   1 
ATOM   1449 O O   . HIS B 1 46  ? 4.725   2.159   -45.881 1.00 16.43 ? 46  HIS B O   1 
ATOM   1450 C CB  . HIS B 1 46  ? 3.524   0.997   -48.453 1.00 18.37 ? 46  HIS B CB  1 
ATOM   1451 C CG  . HIS B 1 46  ? 3.348   1.040   -49.931 1.00 22.82 ? 46  HIS B CG  1 
ATOM   1452 N ND1 . HIS B 1 46  ? 4.166   0.359   -50.802 1.00 28.11 ? 46  HIS B ND1 1 
ATOM   1453 C CD2 . HIS B 1 46  ? 2.438   1.682   -50.695 1.00 23.15 ? 46  HIS B CD2 1 
ATOM   1454 C CE1 . HIS B 1 46  ? 3.767   0.579   -52.041 1.00 21.26 ? 46  HIS B CE1 1 
ATOM   1455 N NE2 . HIS B 1 46  ? 2.727   1.382   -51.996 1.00 23.89 ? 46  HIS B NE2 1 
ATOM   1456 N N   . VAL B 1 47  ? 2.462   2.119   -45.603 1.00 15.79 ? 47  VAL B N   1 
ATOM   1457 C CA  . VAL B 1 47  ? 2.497   1.633   -44.220 1.00 14.79 ? 47  VAL B CA  1 
ATOM   1458 C C   . VAL B 1 47  ? 2.426   0.124   -44.309 1.00 14.98 ? 47  VAL B C   1 
ATOM   1459 O O   . VAL B 1 47  ? 1.474   -0.395  -44.830 1.00 15.18 ? 47  VAL B O   1 
ATOM   1460 C CB  . VAL B 1 47  ? 1.424   2.275   -43.262 1.00 14.32 ? 47  VAL B CB  1 
ATOM   1461 C CG1 . VAL B 1 47  ? 1.652   1.847   -41.787 1.00 13.10 ? 47  VAL B CG1 1 
ATOM   1462 C CG2 . VAL B 1 47  ? 1.591   3.746   -43.257 1.00 15.16 ? 47  VAL B CG2 1 
ATOM   1463 N N   . HIS B 1 48  ? 3.488   -0.559  -43.821 1.00 16.20 ? 48  HIS B N   1 
ATOM   1464 C CA  . HIS B 1 48  ? 3.501   -2.004  -43.597 1.00 16.75 ? 48  HIS B CA  1 
ATOM   1465 C C   . HIS B 1 48  ? 3.003   -2.469  -42.197 1.00 17.35 ? 48  HIS B C   1 
ATOM   1466 O O   . HIS B 1 48  ? 2.980   -1.697  -41.242 1.00 13.81 ? 48  HIS B O   1 
ATOM   1467 C CB  . HIS B 1 48  ? 4.919   -2.535  -43.917 1.00 15.59 ? 48  HIS B CB  1 
ATOM   1468 C CG  . HIS B 1 48  ? 5.214   -2.570  -45.379 1.00 14.46 ? 48  HIS B CG  1 
ATOM   1469 N ND1 . HIS B 1 48  ? 5.272   -3.749  -46.100 1.00 16.08 ? 48  HIS B ND1 1 
ATOM   1470 C CD2 . HIS B 1 48  ? 5.442   -1.573  -46.271 1.00 19.02 ? 48  HIS B CD2 1 
ATOM   1471 C CE1 . HIS B 1 48  ? 5.555   -3.474  -47.358 1.00 16.52 ? 48  HIS B CE1 1 
ATOM   1472 N NE2 . HIS B 1 48  ? 5.665   -2.164  -47.495 1.00 11.99 ? 48  HIS B NE2 1 
ATOM   1473 N N   . GLU B 1 49  ? 2.640   -3.764  -42.071 1.00 18.56 ? 49  GLU B N   1 
ATOM   1474 C CA  . GLU B 1 49  ? 1.884   -4.208  -40.879 1.00 18.98 ? 49  GLU B CA  1 
ATOM   1475 C C   . GLU B 1 49  ? 2.629   -4.144  -39.510 1.00 18.73 ? 49  GLU B C   1 
ATOM   1476 O O   . GLU B 1 49  ? 2.044   -3.797  -38.447 1.00 18.66 ? 49  GLU B O   1 
ATOM   1477 C CB  . GLU B 1 49  ? 1.354   -5.625  -41.134 1.00 19.64 ? 49  GLU B CB  1 
ATOM   1478 C CG  . GLU B 1 49  ? 0.194   -5.943  -40.213 1.00 21.17 ? 49  GLU B CG  1 
ATOM   1479 C CD  . GLU B 1 49  ? -0.266  -7.363  -40.347 1.00 21.53 ? 49  GLU B CD  1 
ATOM   1480 O OE1 . GLU B 1 49  ? 0.138   -8.013  -41.312 1.00 28.56 ? 49  GLU B OE1 1 
ATOM   1481 O OE2 . GLU B 1 49  ? -1.077  -7.827  -39.516 1.00 22.52 ? 49  GLU B OE2 1 
ATOM   1482 N N   . PHE B 1 50  ? 3.912   -4.492  -39.538 1.00 17.77 ? 50  PHE B N   1 
ATOM   1483 C CA  . PHE B 1 50  ? 4.658   -4.687  -38.291 1.00 17.93 ? 50  PHE B CA  1 
ATOM   1484 C C   . PHE B 1 50  ? 5.744   -3.654  -38.101 1.00 17.63 ? 50  PHE B C   1 
ATOM   1485 O O   . PHE B 1 50  ? 6.335   -3.256  -39.074 1.00 17.33 ? 50  PHE B O   1 
ATOM   1486 C CB  . PHE B 1 50  ? 5.187   -6.144  -38.192 1.00 18.31 ? 50  PHE B CB  1 
ATOM   1487 C CG  . PHE B 1 50  ? 4.104   -7.162  -38.299 1.00 15.48 ? 50  PHE B CG  1 
ATOM   1488 C CD1 . PHE B 1 50  ? 2.989   -7.057  -37.502 1.00 15.09 ? 50  PHE B CD1 1 
ATOM   1489 C CD2 . PHE B 1 50  ? 4.194   -8.174  -39.206 1.00 16.98 ? 50  PHE B CD2 1 
ATOM   1490 C CE1 . PHE B 1 50  ? 1.953   -7.954  -37.595 1.00 19.51 ? 50  PHE B CE1 1 
ATOM   1491 C CE2 . PHE B 1 50  ? 3.154   -9.127  -39.345 1.00 19.86 ? 50  PHE B CE2 1 
ATOM   1492 C CZ  . PHE B 1 50  ? 2.034   -9.022  -38.550 1.00 21.72 ? 50  PHE B CZ  1 
ATOM   1493 N N   . GLY B 1 51  ? 5.929   -3.172  -36.858 1.00 17.32 ? 51  GLY B N   1 
ATOM   1494 C CA  . GLY B 1 51  ? 7.080   -2.388  -36.490 1.00 17.09 ? 51  GLY B CA  1 
ATOM   1495 C C   . GLY B 1 51  ? 8.292   -3.228  -36.053 1.00 19.06 ? 51  GLY B C   1 
ATOM   1496 O O   . GLY B 1 51  ? 8.904   -3.035  -34.947 1.00 17.44 ? 51  GLY B O   1 
ATOM   1497 N N   . ASP B 1 52  ? 8.616   -4.174  -36.936 1.00 18.79 ? 52  ASP B N   1 
ATOM   1498 C CA  . ASP B 1 52  ? 9.591   -5.125  -36.671 1.00 20.96 ? 52  ASP B CA  1 
ATOM   1499 C C   . ASP B 1 52  ? 10.715  -4.915  -37.699 1.00 21.95 ? 52  ASP B C   1 
ATOM   1500 O O   . ASP B 1 52  ? 10.525  -4.924  -38.922 1.00 22.24 ? 52  ASP B O   1 
ATOM   1501 C CB  . ASP B 1 52  ? 8.940   -6.498  -36.636 1.00 22.19 ? 52  ASP B CB  1 
ATOM   1502 C CG  . ASP B 1 52  ? 9.871   -7.573  -36.251 1.00 26.93 ? 52  ASP B CG  1 
ATOM   1503 O OD1 . ASP B 1 52  ? 11.090  -7.293  -36.098 1.00 29.37 ? 52  ASP B OD1 1 
ATOM   1504 O OD2 . ASP B 1 52  ? 9.379   -8.730  -36.196 1.00 30.02 ? 52  ASP B OD2 1 
ATOM   1505 N N   . ASN B 1 53  ? 11.891  -4.579  -37.185 1.00 21.84 ? 53  ASN B N   1 
ATOM   1506 C CA  . ASN B 1 53  ? 12.989  -4.366  -38.074 1.00 23.08 ? 53  ASN B CA  1 
ATOM   1507 C C   . ASN B 1 53  ? 14.102  -5.276  -37.704 1.00 22.69 ? 53  ASN B C   1 
ATOM   1508 O O   . ASN B 1 53  ? 15.238  -4.890  -37.835 1.00 23.78 ? 53  ASN B O   1 
ATOM   1509 C CB  . ASN B 1 53  ? 13.489  -2.941  -37.993 1.00 22.72 ? 53  ASN B CB  1 
ATOM   1510 C CG  . ASN B 1 53  ? 14.472  -2.662  -39.056 1.00 27.95 ? 53  ASN B CG  1 
ATOM   1511 O OD1 . ASN B 1 53  ? 14.126  -2.723  -40.240 1.00 32.14 ? 53  ASN B OD1 1 
ATOM   1512 N ND2 . ASN B 1 53  ? 15.717  -2.427  -38.681 1.00 27.79 ? 53  ASN B ND2 1 
ATOM   1513 N N   . ARG B 1 54  ? 13.790  -6.463  -37.193 1.00 23.14 ? 54  ARG B N   1 
ATOM   1514 C CA  . ARG B 1 54  ? 14.805  -7.252  -36.546 1.00 24.40 ? 54  ARG B CA  1 
ATOM   1515 C C   . ARG B 1 54  ? 15.821  -7.908  -37.513 1.00 26.24 ? 54  ARG B C   1 
ATOM   1516 O O   . ARG B 1 54  ? 17.014  -8.047  -37.161 1.00 27.91 ? 54  ARG B O   1 
ATOM   1517 C CB  . ARG B 1 54  ? 14.160  -8.224  -35.595 1.00 24.30 ? 54  ARG B CB  1 
ATOM   1518 C CG  . ARG B 1 54  ? 13.667  -9.509  -36.186 1.00 25.13 ? 54  ARG B CG  1 
ATOM   1519 C CD  . ARG B 1 54  ? 13.095  -10.424 -35.065 1.00 23.12 ? 54  ARG B CD  1 
ATOM   1520 N NE  . ARG B 1 54  ? 11.751  -9.980  -34.670 1.00 29.77 ? 54  ARG B NE  1 
ATOM   1521 C CZ  . ARG B 1 54  ? 11.053  -10.432 -33.628 1.00 32.45 ? 54  ARG B CZ  1 
ATOM   1522 N NH1 . ARG B 1 54  ? 11.572  -11.331 -32.786 1.00 25.60 ? 54  ARG B NH1 1 
ATOM   1523 N NH2 . ARG B 1 54  ? 9.818   -9.953  -33.418 1.00 33.17 ? 54  ARG B NH2 1 
ATOM   1524 N N   . ALA B 1 55  ? 15.343  -8.287  -38.702 1.00 26.28 ? 55  ALA B N   1 
ATOM   1525 C CA  . ALA B 1 55  ? 16.169  -8.658  -39.844 1.00 26.10 ? 55  ALA B CA  1 
ATOM   1526 C C   . ALA B 1 55  ? 16.078  -7.648  -41.012 1.00 26.18 ? 55  ALA B C   1 
ATOM   1527 O O   . ALA B 1 55  ? 16.103  -8.058  -42.172 1.00 27.24 ? 55  ALA B O   1 
ATOM   1528 C CB  . ALA B 1 55  ? 15.781  -10.057 -40.343 1.00 26.21 ? 55  ALA B CB  1 
ATOM   1529 N N   . GLY B 1 56  ? 16.022  -6.335  -40.724 1.00 24.47 ? 56  GLY B N   1 
ATOM   1530 C CA  . GLY B 1 56  ? 15.802  -5.359  -41.751 1.00 21.80 ? 56  GLY B CA  1 
ATOM   1531 C C   . GLY B 1 56  ? 14.354  -4.951  -42.078 1.00 22.05 ? 56  GLY B C   1 
ATOM   1532 O O   . GLY B 1 56  ? 13.424  -5.314  -41.401 1.00 19.76 ? 56  GLY B O   1 
ATOM   1533 N N   . CYS B 1 57  ? 14.199  -4.148  -43.127 1.00 22.68 ? 57  CYS B N   1 
ATOM   1534 C CA  . CYS B 1 57  ? 12.885  -3.759  -43.665 1.00 25.12 ? 57  CYS B CA  1 
ATOM   1535 C C   . CYS B 1 57  ? 11.921  -4.923  -44.034 1.00 24.60 ? 57  CYS B C   1 
ATOM   1536 O O   . CYS B 1 57  ? 10.731  -4.762  -43.875 1.00 24.87 ? 57  CYS B O   1 
ATOM   1537 C CB  . CYS B 1 57  ? 13.050  -2.786  -44.857 1.00 26.19 ? 57  CYS B CB  1 
ATOM   1538 S SG  . CYS B 1 57  ? 13.734  -1.162  -44.436 1.00 31.05 ? 57  CYS B SG  1 
ATOM   1539 N N   . THR B 1 58  ? 12.437  -6.067  -44.498 1.00 23.98 ? 58  THR B N   1 
ATOM   1540 C CA  . THR B 1 58  ? 11.708  -7.346  -44.663 1.00 23.73 ? 58  THR B CA  1 
ATOM   1541 C C   . THR B 1 58  ? 10.854  -7.770  -43.432 1.00 22.89 ? 58  THR B C   1 
ATOM   1542 O O   . THR B 1 58  ? 9.742   -8.353  -43.590 1.00 20.10 ? 58  THR B O   1 
ATOM   1543 C CB  . THR B 1 58  ? 12.735  -8.480  -45.060 1.00 24.13 ? 58  THR B CB  1 
ATOM   1544 O OG1 . THR B 1 58  ? 12.752  -8.642  -46.480 1.00 29.50 ? 58  THR B OG1 1 
ATOM   1545 C CG2 . THR B 1 58  ? 12.449  -9.815  -44.476 1.00 27.32 ? 58  THR B CG2 1 
ATOM   1546 N N   . SER B 1 59  ? 11.359  -7.491  -42.218 1.00 20.67 ? 59  SER B N   1 
ATOM   1547 C CA  . SER B 1 59  ? 10.633  -7.854  -41.008 1.00 21.03 ? 59  SER B CA  1 
ATOM   1548 C C   . SER B 1 59  ? 9.234   -7.176  -40.822 1.00 20.07 ? 59  SER B C   1 
ATOM   1549 O O   . SER B 1 59  ? 8.342   -7.642  -40.058 1.00 20.10 ? 59  SER B O   1 
ATOM   1550 C CB  . SER B 1 59  ? 11.535  -7.576  -39.817 1.00 20.53 ? 59  SER B CB  1 
ATOM   1551 O OG  . SER B 1 59  ? 12.560  -8.523  -39.751 1.00 20.38 ? 59  SER B OG  1 
ATOM   1552 N N   . ALA B 1 60  ? 9.061   -6.081  -41.529 1.00 18.89 ? 60  ALA B N   1 
ATOM   1553 C CA  . ALA B 1 60  ? 7.862   -5.280  -41.461 1.00 19.68 ? 60  ALA B CA  1 
ATOM   1554 C C   . ALA B 1 60  ? 6.643   -5.999  -42.021 1.00 20.62 ? 60  ALA B C   1 
ATOM   1555 O O   . ALA B 1 60  ? 5.520   -5.570  -41.794 1.00 20.73 ? 60  ALA B O   1 
ATOM   1556 C CB  . ALA B 1 60  ? 8.103   -3.913  -42.189 1.00 20.32 ? 60  ALA B CB  1 
ATOM   1557 N N   . GLY B 1 61  ? 6.848   -7.120  -42.740 1.00 21.39 ? 61  GLY B N   1 
ATOM   1558 C CA  . GLY B 1 61  ? 5.757   -7.875  -43.296 1.00 21.89 ? 61  GLY B CA  1 
ATOM   1559 C C   . GLY B 1 61  ? 5.063   -7.180  -44.448 1.00 22.20 ? 61  GLY B C   1 
ATOM   1560 O O   . GLY B 1 61  ? 5.618   -6.314  -45.064 1.00 23.22 ? 61  GLY B O   1 
ATOM   1561 N N   . PRO B 1 62  ? 3.808   -7.565  -44.733 1.00 23.51 ? 62  PRO B N   1 
ATOM   1562 C CA  . PRO B 1 62  ? 2.978   -7.057  -45.886 1.00 23.71 ? 62  PRO B CA  1 
ATOM   1563 C C   . PRO B 1 62  ? 2.439   -5.605  -45.653 1.00 23.98 ? 62  PRO B C   1 
ATOM   1564 O O   . PRO B 1 62  ? 2.706   -5.027  -44.580 1.00 23.95 ? 62  PRO B O   1 
ATOM   1565 C CB  . PRO B 1 62  ? 1.847   -8.113  -45.978 1.00 23.18 ? 62  PRO B CB  1 
ATOM   1566 C CG  . PRO B 1 62  ? 1.668   -8.602  -44.562 1.00 23.84 ? 62  PRO B CG  1 
ATOM   1567 C CD  . PRO B 1 62  ? 3.087   -8.582  -43.915 1.00 23.14 ? 62  PRO B CD  1 
ATOM   1568 N N   . HIS B 1 63  ? 1.742   -4.987  -46.624 1.00 23.79 ? 63  HIS B N   1 
ATOM   1569 C CA  . HIS B 1 63  ? 1.033   -3.724  -46.338 1.00 23.12 ? 63  HIS B CA  1 
ATOM   1570 C C   . HIS B 1 63  ? 0.069   -3.851  -45.172 1.00 23.09 ? 63  HIS B C   1 
ATOM   1571 O O   . HIS B 1 63  ? -0.479  -4.900  -44.906 1.00 23.54 ? 63  HIS B O   1 
ATOM   1572 C CB  . HIS B 1 63  ? 0.213   -3.125  -47.520 1.00 23.68 ? 63  HIS B CB  1 
ATOM   1573 C CG  . HIS B 1 63  ? 0.993   -2.847  -48.753 1.00 23.50 ? 63  HIS B CG  1 
ATOM   1574 N ND1 . HIS B 1 63  ? 0.387   -2.637  -49.966 1.00 23.36 ? 63  HIS B ND1 1 
ATOM   1575 C CD2 . HIS B 1 63  ? 2.319   -2.889  -49.000 1.00 24.55 ? 63  HIS B CD2 1 
ATOM   1576 C CE1 . HIS B 1 63  ? 1.311   -2.529  -50.906 1.00 23.51 ? 63  HIS B CE1 1 
ATOM   1577 N NE2 . HIS B 1 63  ? 2.492   -2.699  -50.347 1.00 25.11 ? 63  HIS B NE2 1 
ATOM   1578 N N   . PHE B 1 64  ? -0.186  -2.747  -44.509 1.00 22.88 ? 64  PHE B N   1 
ATOM   1579 C CA  . PHE B 1 64  ? -1.159  -2.765  -43.461 1.00 23.11 ? 64  PHE B CA  1 
ATOM   1580 C C   . PHE B 1 64  ? -2.555  -2.797  -44.148 1.00 24.73 ? 64  PHE B C   1 
ATOM   1581 O O   . PHE B 1 64  ? -3.042  -1.776  -44.657 1.00 25.07 ? 64  PHE B O   1 
ATOM   1582 C CB  . PHE B 1 64  ? -0.950  -1.570  -42.564 1.00 20.89 ? 64  PHE B CB  1 
ATOM   1583 C CG  . PHE B 1 64  ? -1.928  -1.510  -41.413 1.00 23.02 ? 64  PHE B CG  1 
ATOM   1584 C CD1 . PHE B 1 64  ? -2.333  -2.674  -40.753 1.00 18.41 ? 64  PHE B CD1 1 
ATOM   1585 C CD2 . PHE B 1 64  ? -2.473  -0.315  -41.014 1.00 17.33 ? 64  PHE B CD2 1 
ATOM   1586 C CE1 . PHE B 1 64  ? -3.244  -2.621  -39.741 1.00 17.72 ? 64  PHE B CE1 1 
ATOM   1587 C CE2 . PHE B 1 64  ? -3.383  -0.301  -39.984 1.00 14.08 ? 64  PHE B CE2 1 
ATOM   1588 C CZ  . PHE B 1 64  ? -3.768  -1.429  -39.358 1.00 17.81 ? 64  PHE B CZ  1 
ATOM   1589 N N   . ASN B 1 65  ? -3.146  -3.995  -44.201 1.00 24.62 ? 65  ASN B N   1 
ATOM   1590 C CA  . ASN B 1 65  ? -4.406  -4.234  -44.906 1.00 25.71 ? 65  ASN B CA  1 
ATOM   1591 C C   . ASN B 1 65  ? -5.460  -4.845  -43.997 1.00 25.96 ? 65  ASN B C   1 
ATOM   1592 O O   . ASN B 1 65  ? -5.777  -6.010  -44.213 1.00 25.62 ? 65  ASN B O   1 
ATOM   1593 C CB  . ASN B 1 65  ? -4.144  -5.281  -45.996 1.00 25.37 ? 65  ASN B CB  1 
ATOM   1594 C CG  . ASN B 1 65  ? -5.299  -5.438  -46.996 1.00 26.88 ? 65  ASN B CG  1 
ATOM   1595 O OD1 . ASN B 1 65  ? -6.202  -4.568  -47.101 1.00 27.33 ? 65  ASN B OD1 1 
ATOM   1596 N ND2 . ASN B 1 65  ? -5.203  -6.522  -47.836 1.00 22.84 ? 65  ASN B ND2 1 
ATOM   1597 N N   . PRO B 1 66  ? -5.931  -4.122  -42.952 1.00 27.09 ? 66  PRO B N   1 
ATOM   1598 C CA  . PRO B 1 66  ? -6.849  -4.744  -41.974 1.00 28.60 ? 66  PRO B CA  1 
ATOM   1599 C C   . PRO B 1 66  ? -8.186  -5.216  -42.559 1.00 30.91 ? 66  PRO B C   1 
ATOM   1600 O O   . PRO B 1 66  ? -8.725  -6.267  -42.128 1.00 32.19 ? 66  PRO B O   1 
ATOM   1601 C CB  . PRO B 1 66  ? -7.083  -3.647  -40.931 1.00 28.91 ? 66  PRO B CB  1 
ATOM   1602 C CG  . PRO B 1 66  ? -6.598  -2.372  -41.571 1.00 25.90 ? 66  PRO B CG  1 
ATOM   1603 C CD  . PRO B 1 66  ? -5.614  -2.719  -42.602 1.00 26.69 ? 66  PRO B CD  1 
ATOM   1604 N N   . LEU B 1 67  ? -8.699  -4.486  -43.548 1.00 32.06 ? 67  LEU B N   1 
ATOM   1605 C CA  . LEU B 1 67  ? -9.970  -4.833  -44.191 1.00 32.70 ? 67  LEU B CA  1 
ATOM   1606 C C   . LEU B 1 67  ? -9.839  -5.795  -45.378 1.00 33.36 ? 67  LEU B C   1 
ATOM   1607 O O   . LEU B 1 67  ? -10.697 -5.791  -46.230 1.00 34.37 ? 67  LEU B O   1 
ATOM   1608 C CB  . LEU B 1 67  ? -10.671 -3.582  -44.689 1.00 32.48 ? 67  LEU B CB  1 
ATOM   1609 C CG  . LEU B 1 67  ? -10.809 -2.385  -43.772 1.00 33.04 ? 67  LEU B CG  1 
ATOM   1610 C CD1 . LEU B 1 67  ? -11.452 -1.297  -44.576 1.00 32.86 ? 67  LEU B CD1 1 
ATOM   1611 C CD2 . LEU B 1 67  ? -11.613 -2.785  -42.529 1.00 36.58 ? 67  LEU B CD2 1 
ATOM   1612 N N   . SER B 1 68  ? -8.788  -6.612  -45.408 1.00 33.26 ? 68  SER B N   1 
ATOM   1613 C CA  . SER B 1 68  ? -8.460  -7.558  -46.524 1.00 33.49 ? 68  SER B CA  1 
ATOM   1614 C C   . SER B 1 68  ? -8.820  -7.146  -47.944 1.00 33.36 ? 68  SER B C   1 
ATOM   1615 O O   . SER B 1 68  ? -9.165  -8.010  -48.755 1.00 33.35 ? 68  SER B O   1 
ATOM   1616 C CB  . SER B 1 68  ? -8.946  -8.977  -46.255 1.00 32.15 ? 68  SER B CB  1 
ATOM   1617 O OG  . SER B 1 68  ? -8.251  -9.478  -45.137 1.00 34.21 ? 68  SER B OG  1 
ATOM   1618 N N   . ARG B 1 69  ? -8.685  -5.846  -48.232 1.00 33.29 ? 69  ARG B N   1 
ATOM   1619 C CA  . ARG B 1 69  ? -9.036  -5.253  -49.521 1.00 33.17 ? 69  ARG B CA  1 
ATOM   1620 C C   . ARG B 1 69  ? -7.926  -5.412  -50.546 1.00 33.29 ? 69  ARG B C   1 
ATOM   1621 O O   . ARG B 1 69  ? -6.881  -5.989  -50.265 1.00 32.97 ? 69  ARG B O   1 
ATOM   1622 C CB  . ARG B 1 69  ? -9.461  -3.797  -49.316 1.00 32.76 ? 69  ARG B CB  1 
ATOM   1623 C CG  . ARG B 1 69  ? -10.840 -3.782  -48.664 1.00 36.74 ? 69  ARG B CG  1 
ATOM   1624 C CD  . ARG B 1 69  ? -11.365 -2.438  -48.344 1.00 43.04 ? 69  ARG B CD  1 
ATOM   1625 N NE  . ARG B 1 69  ? -12.402 -2.039  -49.263 1.00 49.18 ? 69  ARG B NE  1 
ATOM   1626 C CZ  . ARG B 1 69  ? -12.979 -0.840  -49.240 1.00 53.23 ? 69  ARG B CZ  1 
ATOM   1627 N NH1 . ARG B 1 69  ? -12.581 0.053   -48.328 1.00 53.03 ? 69  ARG B NH1 1 
ATOM   1628 N NH2 . ARG B 1 69  ? -13.938 -0.533  -50.137 1.00 54.71 ? 69  ARG B NH2 1 
ATOM   1629 N N   . LYS B 1 70  ? -8.145  -4.935  -51.764 1.00 33.21 ? 70  LYS B N   1 
ATOM   1630 C CA  . LYS B 1 70  ? -7.097  -5.078  -52.754 1.00 32.53 ? 70  LYS B CA  1 
ATOM   1631 C C   . LYS B 1 70  ? -6.401  -3.760  -52.848 1.00 29.91 ? 70  LYS B C   1 
ATOM   1632 O O   . LYS B 1 70  ? -6.937  -2.738  -52.461 1.00 28.40 ? 70  LYS B O   1 
ATOM   1633 C CB  . LYS B 1 70  ? -7.632  -5.536  -54.121 1.00 33.77 ? 70  LYS B CB  1 
ATOM   1634 C CG  . LYS B 1 70  ? -8.272  -6.944  -54.123 1.00 34.78 ? 70  LYS B CG  1 
ATOM   1635 C CD  . LYS B 1 70  ? -8.703  -7.394  -55.542 1.00 36.96 ? 70  LYS B CD  1 
ATOM   1636 C CE  . LYS B 1 70  ? -9.950  -6.640  -56.071 1.00 41.51 ? 70  LYS B CE  1 
ATOM   1637 N NZ  . LYS B 1 70  ? -9.689  -5.178  -56.524 1.00 44.55 ? 70  LYS B NZ  1 
ATOM   1638 N N   . HIS B 1 71  ? -5.199  -3.825  -53.392 1.00 28.54 ? 71  HIS B N   1 
ATOM   1639 C CA  . HIS B 1 71  ? -4.279  -2.722  -53.433 1.00 26.73 ? 71  HIS B CA  1 
ATOM   1640 C C   . HIS B 1 71  ? -4.823  -1.629  -54.334 1.00 26.45 ? 71  HIS B C   1 
ATOM   1641 O O   . HIS B 1 71  ? -5.332  -1.899  -55.401 1.00 27.24 ? 71  HIS B O   1 
ATOM   1642 C CB  . HIS B 1 71  ? -2.886  -3.244  -53.862 1.00 26.12 ? 71  HIS B CB  1 
ATOM   1643 C CG  . HIS B 1 71  ? -1.843  -2.181  -53.889 1.00 25.66 ? 71  HIS B CG  1 
ATOM   1644 N ND1 . HIS B 1 71  ? -1.518  -1.429  -52.781 1.00 21.57 ? 71  HIS B ND1 1 
ATOM   1645 C CD2 . HIS B 1 71  ? -1.115  -1.687  -54.917 1.00 26.15 ? 71  HIS B CD2 1 
ATOM   1646 C CE1 . HIS B 1 71  ? -0.622  -0.527  -53.130 1.00 25.94 ? 71  HIS B CE1 1 
ATOM   1647 N NE2 . HIS B 1 71  ? -0.371  -0.653  -54.424 1.00 26.11 ? 71  HIS B NE2 1 
ATOM   1648 N N   . GLY B 1 72  ? -4.715  -0.381  -53.903 1.00 26.04 ? 72  GLY B N   1 
ATOM   1649 C CA  . GLY B 1 72  ? -5.122  0.720   -54.744 1.00 25.13 ? 72  GLY B CA  1 
ATOM   1650 C C   . GLY B 1 72  ? -4.187  1.865   -54.556 1.00 24.92 ? 72  GLY B C   1 
ATOM   1651 O O   . GLY B 1 72  ? -3.169  1.731   -53.906 1.00 26.62 ? 72  GLY B O   1 
ATOM   1652 N N   . GLY B 1 73  ? -4.525  3.010   -55.127 1.00 24.47 ? 73  GLY B N   1 
ATOM   1653 C CA  . GLY B 1 73  ? -3.937  4.252   -54.714 1.00 24.51 ? 73  GLY B CA  1 
ATOM   1654 C C   . GLY B 1 73  ? -4.735  4.820   -53.558 1.00 25.24 ? 73  GLY B C   1 
ATOM   1655 O O   . GLY B 1 73  ? -5.787  4.291   -53.154 1.00 25.02 ? 73  GLY B O   1 
ATOM   1656 N N   . PRO B 1 74  ? -4.222  5.885   -52.993 1.00 26.33 ? 74  PRO B N   1 
ATOM   1657 C CA  . PRO B 1 74  ? -4.765  6.635   -51.863 1.00 27.06 ? 74  PRO B CA  1 
ATOM   1658 C C   . PRO B 1 74  ? -6.216  7.076   -52.063 1.00 28.39 ? 74  PRO B C   1 
ATOM   1659 O O   . PRO B 1 74  ? -6.986  7.076   -51.101 1.00 26.52 ? 74  PRO B O   1 
ATOM   1660 C CB  . PRO B 1 74  ? -3.852  7.852   -51.800 1.00 26.67 ? 74  PRO B CB  1 
ATOM   1661 C CG  . PRO B 1 74  ? -2.592  7.419   -52.483 1.00 26.28 ? 74  PRO B CG  1 
ATOM   1662 C CD  . PRO B 1 74  ? -2.915  6.395   -53.461 1.00 25.95 ? 74  PRO B CD  1 
ATOM   1663 N N   . LYS B 1 75  ? -6.545  7.453   -53.315 1.00 30.90 ? 75  LYS B N   1 
ATOM   1664 C CA  . LYS B 1 75  ? -7.800  8.143   -53.692 1.00 32.01 ? 75  LYS B CA  1 
ATOM   1665 C C   . LYS B 1 75  ? -8.851  7.125   -54.007 1.00 32.12 ? 75  LYS B C   1 
ATOM   1666 O O   . LYS B 1 75  ? -9.991  7.490   -54.245 1.00 34.50 ? 75  LYS B O   1 
ATOM   1667 C CB  . LYS B 1 75  ? -7.613  8.953   -54.968 1.00 32.33 ? 75  LYS B CB  1 
ATOM   1668 C CG  . LYS B 1 75  ? -6.995  10.360  -54.854 1.00 35.65 ? 75  LYS B CG  1 
ATOM   1669 C CD  . LYS B 1 75  ? -6.059  10.506  -56.062 1.00 38.65 ? 75  LYS B CD  1 
ATOM   1670 C CE  . LYS B 1 75  ? -6.187  11.848  -56.753 1.00 41.67 ? 75  LYS B CE  1 
ATOM   1671 N NZ  . LYS B 1 75  ? -5.982  11.664  -58.225 1.00 40.75 ? 75  LYS B NZ  1 
ATOM   1672 N N   . ASP B 1 76  ? -8.469  5.854   -54.070 1.00 31.27 ? 76  ASP B N   1 
ATOM   1673 C CA  . ASP B 1 76  ? -9.413  4.815   -54.390 1.00 30.33 ? 76  ASP B CA  1 
ATOM   1674 C C   . ASP B 1 76  ? -10.193 4.394   -53.141 1.00 30.57 ? 76  ASP B C   1 
ATOM   1675 O O   . ASP B 1 76  ? -9.679  4.459   -52.005 1.00 27.91 ? 76  ASP B O   1 
ATOM   1676 C CB  . ASP B 1 76  ? -8.696  3.587   -54.970 1.00 31.31 ? 76  ASP B CB  1 
ATOM   1677 C CG  . ASP B 1 76  ? -7.892  3.886   -56.265 1.00 32.08 ? 76  ASP B CG  1 
ATOM   1678 O OD1 . ASP B 1 76  ? -8.021  4.972   -56.881 1.00 29.55 ? 76  ASP B OD1 1 
ATOM   1679 O OD2 . ASP B 1 76  ? -7.113  2.990   -56.653 1.00 32.32 ? 76  ASP B OD2 1 
ATOM   1680 N N   . GLU B 1 77  ? -11.425 3.946   -53.375 1.00 29.75 ? 77  GLU B N   1 
ATOM   1681 C CA  . GLU B 1 77  ? -12.256 3.321   -52.348 1.00 31.15 ? 77  GLU B CA  1 
ATOM   1682 C C   . GLU B 1 77  ? -11.682 1.970   -51.969 1.00 30.24 ? 77  GLU B C   1 
ATOM   1683 O O   . GLU B 1 77  ? -11.563 1.607   -50.759 1.00 31.97 ? 77  GLU B O   1 
ATOM   1684 C CB  . GLU B 1 77  ? -13.727 3.201   -52.816 1.00 31.98 ? 77  GLU B CB  1 
ATOM   1685 C CG  . GLU B 1 77  ? -14.676 2.461   -51.841 1.00 36.04 ? 77  GLU B CG  1 
ATOM   1686 C CD  . GLU B 1 77  ? -14.595 2.962   -50.393 1.00 43.66 ? 77  GLU B CD  1 
ATOM   1687 O OE1 . GLU B 1 77  ? -14.156 4.145   -50.162 1.00 42.40 ? 77  GLU B OE1 1 
ATOM   1688 O OE2 . GLU B 1 77  ? -14.990 2.164   -49.488 1.00 47.05 ? 77  GLU B OE2 1 
ATOM   1689 N N   . GLU B 1 78  ? -11.284 1.244   -52.994 1.00 29.45 ? 78  GLU B N   1 
ATOM   1690 C CA  . GLU B 1 78  ? -10.706 -0.040  -52.838 1.00 28.61 ? 78  GLU B CA  1 
ATOM   1691 C C   . GLU B 1 78  ? -9.189  0.185   -52.756 1.00 28.15 ? 78  GLU B C   1 
ATOM   1692 O O   . GLU B 1 78  ? -8.535  0.634   -53.740 1.00 28.01 ? 78  GLU B O   1 
ATOM   1693 C CB  . GLU B 1 78  ? -11.152 -0.972  -53.989 1.00 29.68 ? 78  GLU B CB  1 
ATOM   1694 C CG  . GLU B 1 78  ? -10.732 -2.462  -53.873 1.00 32.46 ? 78  GLU B CG  1 
ATOM   1695 C CD  . GLU B 1 78  ? -11.449 -3.265  -52.783 1.00 38.35 ? 78  GLU B CD  1 
ATOM   1696 O OE1 . GLU B 1 78  ? -12.300 -2.661  -52.069 1.00 37.50 ? 78  GLU B OE1 1 
ATOM   1697 O OE2 . GLU B 1 78  ? -11.152 -4.513  -52.644 1.00 37.33 ? 78  GLU B OE2 1 
ATOM   1698 N N   . ARG B 1 79  ? -8.639  -0.058  -51.550 1.00 25.71 ? 79  ARG B N   1 
ATOM   1699 C CA  . ARG B 1 79  ? -7.201  0.228   -51.281 1.00 24.88 ? 79  ARG B CA  1 
ATOM   1700 C C   . ARG B 1 79  ? -6.904  -0.333  -49.908 1.00 24.01 ? 79  ARG B C   1 
ATOM   1701 O O   . ARG B 1 79  ? -7.876  -0.586  -49.149 1.00 23.83 ? 79  ARG B O   1 
ATOM   1702 C CB  . ARG B 1 79  ? -6.978  1.738   -51.315 1.00 23.59 ? 79  ARG B CB  1 
ATOM   1703 C CG  . ARG B 1 79  ? -7.667  2.464   -50.167 1.00 22.57 ? 79  ARG B CG  1 
ATOM   1704 C CD  . ARG B 1 79  ? -6.978  3.753   -49.881 1.00 18.16 ? 79  ARG B CD  1 
ATOM   1705 N NE  . ARG B 1 79  ? -5.984  3.690   -48.785 1.00 19.02 ? 79  ARG B NE  1 
ATOM   1706 C CZ  . ARG B 1 79  ? -5.476  4.793   -48.215 1.00 21.90 ? 79  ARG B CZ  1 
ATOM   1707 N NH1 . ARG B 1 79  ? -5.872  5.998   -48.637 1.00 17.12 ? 79  ARG B NH1 1 
ATOM   1708 N NH2 . ARG B 1 79  ? -4.591  4.703   -47.216 1.00 21.97 ? 79  ARG B NH2 1 
ATOM   1709 N N   . HIS B 1 80  ? -5.629  -0.594  -49.566 1.00 23.87 ? 80  HIS B N   1 
ATOM   1710 C CA  . HIS B 1 80  ? -5.267  -1.078  -48.138 1.00 22.06 ? 80  HIS B CA  1 
ATOM   1711 C C   . HIS B 1 80  ? -5.309  0.143   -47.221 1.00 20.75 ? 80  HIS B C   1 
ATOM   1712 O O   . HIS B 1 80  ? -5.226  1.258   -47.702 1.00 18.97 ? 80  HIS B O   1 
ATOM   1713 C CB  . HIS B 1 80  ? -3.842  -1.694  -48.009 1.00 21.68 ? 80  HIS B CB  1 
ATOM   1714 C CG  . HIS B 1 80  ? -3.530  -2.831  -48.965 1.00 19.22 ? 80  HIS B CG  1 
ATOM   1715 N ND1 . HIS B 1 80  ? -2.272  -3.035  -49.485 1.00 16.26 ? 80  HIS B ND1 1 
ATOM   1716 C CD2 . HIS B 1 80  ? -4.302  -3.814  -49.484 1.00 17.37 ? 80  HIS B CD2 1 
ATOM   1717 C CE1 . HIS B 1 80  ? -2.275  -4.102  -50.270 1.00 15.62 ? 80  HIS B CE1 1 
ATOM   1718 N NE2 . HIS B 1 80  ? -3.503  -4.569  -50.313 1.00 18.03 ? 80  HIS B NE2 1 
ATOM   1719 N N   . VAL B 1 81  ? -5.358  -0.016  -45.885 1.00 22.63 ? 81  VAL B N   1 
ATOM   1720 C CA  . VAL B 1 81  ? -5.180  1.244   -45.029 1.00 20.76 ? 81  VAL B CA  1 
ATOM   1721 C C   . VAL B 1 81  ? -3.833  1.959   -45.369 1.00 21.24 ? 81  VAL B C   1 
ATOM   1722 O O   . VAL B 1 81  ? -3.687  3.187   -45.300 1.00 23.56 ? 81  VAL B O   1 
ATOM   1723 C CB  . VAL B 1 81  ? -5.364  0.938   -43.499 1.00 20.96 ? 81  VAL B CB  1 
ATOM   1724 C CG1 . VAL B 1 81  ? -4.863  2.099   -42.563 1.00 17.39 ? 81  VAL B CG1 1 
ATOM   1725 C CG2 . VAL B 1 81  ? -6.862  0.672   -43.206 1.00 19.83 ? 81  VAL B CG2 1 
ATOM   1726 N N   . GLY B 1 82  ? -2.848  1.190   -45.762 1.00 20.69 ? 82  GLY B N   1 
ATOM   1727 C CA  . GLY B 1 82  ? -1.482  1.659   -45.771 1.00 20.85 ? 82  GLY B CA  1 
ATOM   1728 C C   . GLY B 1 82  ? -0.988  1.970   -47.146 1.00 20.08 ? 82  GLY B C   1 
ATOM   1729 O O   . GLY B 1 82  ? 0.204   2.265   -47.324 1.00 19.98 ? 82  GLY B O   1 
ATOM   1730 N N   . ASP B 1 83  ? -1.893  1.949   -48.115 1.00 19.05 ? 83  ASP B N   1 
ATOM   1731 C CA  . ASP B 1 83  ? -1.586  2.463   -49.456 1.00 20.00 ? 83  ASP B CA  1 
ATOM   1732 C C   . ASP B 1 83  ? -1.504  3.992   -49.524 1.00 19.33 ? 83  ASP B C   1 
ATOM   1733 O O   . ASP B 1 83  ? -2.501  4.595   -49.848 1.00 19.23 ? 83  ASP B O   1 
ATOM   1734 C CB  . ASP B 1 83  ? -2.677  2.026   -50.432 1.00 20.56 ? 83  ASP B CB  1 
ATOM   1735 C CG  . ASP B 1 83  ? -2.630  0.530   -50.693 1.00 21.32 ? 83  ASP B CG  1 
ATOM   1736 O OD1 . ASP B 1 83  ? -1.562  -0.058  -50.459 1.00 21.20 ? 83  ASP B OD1 1 
ATOM   1737 O OD2 . ASP B 1 83  ? -3.628  -0.050  -51.142 1.00 21.39 ? 83  ASP B OD2 1 
ATOM   1738 N N   . LEU B 1 84  ? -0.330  4.602   -49.289 1.00 18.10 ? 84  LEU B N   1 
ATOM   1739 C CA  . LEU B 1 84  ? -0.201  6.076   -49.423 1.00 18.90 ? 84  LEU B CA  1 
ATOM   1740 C C   . LEU B 1 84  ? 0.449   6.538   -50.697 1.00 19.56 ? 84  LEU B C   1 
ATOM   1741 O O   . LEU B 1 84  ? 0.970   7.684   -50.751 1.00 19.60 ? 84  LEU B O   1 
ATOM   1742 C CB  . LEU B 1 84  ? 0.534   6.709   -48.202 1.00 18.88 ? 84  LEU B CB  1 
ATOM   1743 C CG  . LEU B 1 84  ? -0.098  6.265   -46.864 1.00 18.65 ? 84  LEU B CG  1 
ATOM   1744 C CD1 . LEU B 1 84  ? 0.822   6.258   -45.701 1.00 16.82 ? 84  LEU B CD1 1 
ATOM   1745 C CD2 . LEU B 1 84  ? -1.385  7.146   -46.671 1.00 17.17 ? 84  LEU B CD2 1 
ATOM   1746 N N   . GLY B 1 85  ? 0.369   5.697   -51.733 1.00 19.29 ? 85  GLY B N   1 
ATOM   1747 C CA  . GLY B 1 85  ? 0.717   6.118   -53.086 1.00 19.22 ? 85  GLY B CA  1 
ATOM   1748 C C   . GLY B 1 85  ? 2.222   6.117   -53.298 1.00 20.03 ? 85  GLY B C   1 
ATOM   1749 O O   . GLY B 1 85  ? 2.888   5.190   -52.890 1.00 20.38 ? 85  GLY B O   1 
ATOM   1750 N N   . ASN B 1 86  ? 2.722   7.190   -53.932 1.00 21.02 ? 86  ASN B N   1 
ATOM   1751 C CA  . ASN B 1 86  ? 4.092   7.387   -54.344 1.00 20.93 ? 86  ASN B CA  1 
ATOM   1752 C C   . ASN B 1 86  ? 4.521   8.710   -53.780 1.00 21.59 ? 86  ASN B C   1 
ATOM   1753 O O   . ASN B 1 86  ? 3.696   9.586   -53.493 1.00 20.79 ? 86  ASN B O   1 
ATOM   1754 C CB  . ASN B 1 86  ? 4.242   7.437   -55.897 1.00 19.33 ? 86  ASN B CB  1 
ATOM   1755 C CG  . ASN B 1 86  ? 4.088   6.073   -56.539 1.00 21.46 ? 86  ASN B CG  1 
ATOM   1756 O OD1 . ASN B 1 86  ? 4.935   5.218   -56.373 1.00 14.84 ? 86  ASN B OD1 1 
ATOM   1757 N ND2 . ASN B 1 86  ? 3.001   5.867   -57.316 1.00 23.98 ? 86  ASN B ND2 1 
ATOM   1758 N N   . VAL B 1 87  ? 5.831   8.833   -53.568 1.00 21.61 ? 87  VAL B N   1 
ATOM   1759 C CA  . VAL B 1 87  ? 6.438   10.145  -53.302 1.00 21.58 ? 87  VAL B CA  1 
ATOM   1760 C C   . VAL B 1 87  ? 7.368   10.290  -54.470 1.00 21.67 ? 87  VAL B C   1 
ATOM   1761 O O   . VAL B 1 87  ? 7.731   9.280   -55.139 1.00 20.81 ? 87  VAL B O   1 
ATOM   1762 C CB  . VAL B 1 87  ? 7.277   10.197  -51.975 1.00 22.51 ? 87  VAL B CB  1 
ATOM   1763 C CG1 . VAL B 1 87  ? 6.331   10.036  -50.778 1.00 22.79 ? 87  VAL B CG1 1 
ATOM   1764 C CG2 . VAL B 1 87  ? 8.400   9.115   -51.932 1.00 21.67 ? 87  VAL B CG2 1 
ATOM   1765 N N   . THR B 1 88  ? 7.718   11.529  -54.762 1.00 22.07 ? 88  THR B N   1 
ATOM   1766 C CA  . THR B 1 88  ? 8.493   11.827  -55.950 1.00 22.40 ? 88  THR B CA  1 
ATOM   1767 C C   . THR B 1 88  ? 9.798   12.442  -55.559 1.00 23.39 ? 88  THR B C   1 
ATOM   1768 O O   . THR B 1 88  ? 9.828   13.549  -54.946 1.00 24.29 ? 88  THR B O   1 
ATOM   1769 C CB  . THR B 1 88  ? 7.756   12.808  -56.944 1.00 22.83 ? 88  THR B CB  1 
ATOM   1770 O OG1 . THR B 1 88  ? 6.417   12.369  -57.192 1.00 15.64 ? 88  THR B OG1 1 
ATOM   1771 C CG2 . THR B 1 88  ? 8.552   12.895  -58.323 1.00 21.43 ? 88  THR B CG2 1 
ATOM   1772 N N   . ALA B 1 89  ? 10.875  11.745  -55.921 1.00 24.77 ? 89  ALA B N   1 
ATOM   1773 C CA  . ALA B 1 89  ? 12.263  12.294  -55.778 1.00 26.52 ? 89  ALA B CA  1 
ATOM   1774 C C   . ALA B 1 89  ? 12.659  13.167  -56.988 1.00 27.85 ? 89  ALA B C   1 
ATOM   1775 O O   . ALA B 1 89  ? 12.473  12.752  -58.154 1.00 29.85 ? 89  ALA B O   1 
ATOM   1776 C CB  . ALA B 1 89  ? 13.221  11.207  -55.601 1.00 25.43 ? 89  ALA B CB  1 
ATOM   1777 N N   . ASP B 1 90  ? 13.123  14.386  -56.703 1.00 28.29 ? 90  ASP B N   1 
ATOM   1778 C CA  . ASP B 1 90  ? 13.685  15.317  -57.698 1.00 29.08 ? 90  ASP B CA  1 
ATOM   1779 C C   . ASP B 1 90  ? 14.989  14.780  -58.260 1.00 29.88 ? 90  ASP B C   1 
ATOM   1780 O O   . ASP B 1 90  ? 15.369  13.631  -58.009 1.00 29.94 ? 90  ASP B O   1 
ATOM   1781 C CB  . ASP B 1 90  ? 13.848  16.768  -57.131 1.00 29.10 ? 90  ASP B CB  1 
ATOM   1782 C CG  . ASP B 1 90  ? 14.952  16.915  -55.994 1.00 28.48 ? 90  ASP B CG  1 
ATOM   1783 O OD1 . ASP B 1 90  ? 15.897  16.126  -55.919 1.00 31.65 ? 90  ASP B OD1 1 
ATOM   1784 O OD2 . ASP B 1 90  ? 14.907  17.880  -55.192 1.00 26.77 ? 90  ASP B OD2 1 
ATOM   1785 N N   . LYS B 1 91  ? 15.698  15.627  -58.992 1.00 32.31 ? 91  LYS B N   1 
ATOM   1786 C CA  . LYS B 1 91  ? 16.810  15.158  -59.830 1.00 32.58 ? 91  LYS B CA  1 
ATOM   1787 C C   . LYS B 1 91  ? 17.992  14.888  -58.951 1.00 32.93 ? 91  LYS B C   1 
ATOM   1788 O O   . LYS B 1 91  ? 18.824  14.006  -59.261 1.00 33.37 ? 91  LYS B O   1 
ATOM   1789 C CB  . LYS B 1 91  ? 17.180  16.180  -60.908 1.00 33.45 ? 91  LYS B CB  1 
ATOM   1790 C CG  . LYS B 1 91  ? 17.514  17.568  -60.437 1.00 33.51 ? 91  LYS B CG  1 
ATOM   1791 C CD  . LYS B 1 91  ? 18.379  18.219  -61.500 1.00 38.52 ? 91  LYS B CD  1 
ATOM   1792 C CE  . LYS B 1 91  ? 17.931  19.648  -61.822 1.00 38.26 ? 91  LYS B CE  1 
ATOM   1793 N NZ  . LYS B 1 91  ? 18.152  20.607  -60.702 1.00 38.49 ? 91  LYS B NZ  1 
ATOM   1794 N N   . ASP B 1 92  ? 18.045  15.660  -57.858 1.00 31.56 ? 92  ASP B N   1 
ATOM   1795 C CA  . ASP B 1 92  ? 19.035  15.511  -56.822 1.00 29.95 ? 92  ASP B CA  1 
ATOM   1796 C C   . ASP B 1 92  ? 18.684  14.495  -55.707 1.00 29.06 ? 92  ASP B C   1 
ATOM   1797 O O   . ASP B 1 92  ? 19.275  14.552  -54.626 1.00 28.04 ? 92  ASP B O   1 
ATOM   1798 C CB  . ASP B 1 92  ? 19.333  16.898  -56.224 1.00 31.38 ? 92  ASP B CB  1 
ATOM   1799 C CG  . ASP B 1 92  ? 20.085  17.793  -57.198 1.00 32.91 ? 92  ASP B CG  1 
ATOM   1800 O OD1 . ASP B 1 92  ? 21.069  17.328  -57.855 1.00 37.39 ? 92  ASP B OD1 1 
ATOM   1801 O OD2 . ASP B 1 92  ? 19.671  18.964  -57.330 1.00 36.66 ? 92  ASP B OD2 1 
ATOM   1802 N N   . GLY B 1 93  ? 17.725  13.590  -55.963 1.00 29.02 ? 93  GLY B N   1 
ATOM   1803 C CA  . GLY B 1 93  ? 17.416  12.439  -55.048 1.00 27.17 ? 93  GLY B CA  1 
ATOM   1804 C C   . GLY B 1 93  ? 16.578  12.728  -53.797 1.00 26.21 ? 93  GLY B C   1 
ATOM   1805 O O   . GLY B 1 93  ? 16.266  11.784  -52.987 1.00 24.45 ? 93  GLY B O   1 
ATOM   1806 N N   . VAL B 1 94  ? 16.187  14.001  -53.663 1.00 24.31 ? 94  VAL B N   1 
ATOM   1807 C CA  . VAL B 1 94  ? 15.334  14.544  -52.567 1.00 24.98 ? 94  VAL B CA  1 
ATOM   1808 C C   . VAL B 1 94  ? 13.779  14.527  -52.785 1.00 26.72 ? 94  VAL B C   1 
ATOM   1809 O O   . VAL B 1 94  ? 13.259  15.169  -53.750 1.00 27.83 ? 94  VAL B O   1 
ATOM   1810 C CB  . VAL B 1 94  ? 15.804  15.973  -52.233 1.00 23.72 ? 94  VAL B CB  1 
ATOM   1811 C CG1 . VAL B 1 94  ? 14.923  16.661  -51.207 1.00 22.22 ? 94  VAL B CG1 1 
ATOM   1812 C CG2 . VAL B 1 94  ? 17.218  15.934  -51.807 1.00 20.45 ? 94  VAL B CG2 1 
ATOM   1813 N N   . ALA B 1 95  ? 13.034  13.816  -51.908 1.00 26.57 ? 95  ALA B N   1 
ATOM   1814 C CA  . ALA B 1 95  ? 11.564  13.881  -51.965 1.00 26.95 ? 95  ALA B CA  1 
ATOM   1815 C C   . ALA B 1 95  ? 10.969  14.649  -50.842 1.00 27.44 ? 95  ALA B C   1 
ATOM   1816 O O   . ALA B 1 95  ? 11.093  14.234  -49.700 1.00 28.42 ? 95  ALA B O   1 
ATOM   1817 C CB  . ALA B 1 95  ? 10.884  12.507  -52.065 1.00 26.55 ? 95  ALA B CB  1 
ATOM   1818 N N   . ASP B 1 96  ? 10.307  15.755  -51.190 1.00 28.64 ? 96  ASP B N   1 
ATOM   1819 C CA  . ASP B 1 96  ? 9.524   16.559  -50.257 1.00 30.42 ? 96  ASP B CA  1 
ATOM   1820 C C   . ASP B 1 96  ? 8.109   15.938  -50.175 1.00 30.12 ? 96  ASP B C   1 
ATOM   1821 O O   . ASP B 1 96  ? 7.289   16.085  -51.078 1.00 31.75 ? 96  ASP B O   1 
ATOM   1822 C CB  . ASP B 1 96  ? 9.486   18.017  -50.720 1.00 31.36 ? 96  ASP B CB  1 
ATOM   1823 C CG  . ASP B 1 96  ? 8.573   18.883  -49.852 1.00 35.90 ? 96  ASP B CG  1 
ATOM   1824 O OD1 . ASP B 1 96  ? 9.021   19.341  -48.761 1.00 44.85 ? 96  ASP B OD1 1 
ATOM   1825 O OD2 . ASP B 1 96  ? 7.401   19.107  -50.232 1.00 41.96 ? 96  ASP B OD2 1 
ATOM   1826 N N   . VAL B 1 97  ? 7.864   15.180  -49.130 1.00 28.84 ? 97  VAL B N   1 
ATOM   1827 C CA  . VAL B 1 97  ? 6.579   14.535  -48.896 1.00 28.47 ? 97  VAL B CA  1 
ATOM   1828 C C   . VAL B 1 97  ? 5.541   15.541  -48.323 1.00 28.54 ? 97  VAL B C   1 
ATOM   1829 O O   . VAL B 1 97  ? 5.820   16.286  -47.398 1.00 29.80 ? 97  VAL B O   1 
ATOM   1830 C CB  . VAL B 1 97  ? 6.814   13.291  -47.932 1.00 28.57 ? 97  VAL B CB  1 
ATOM   1831 C CG1 . VAL B 1 97  ? 5.522   12.483  -47.699 1.00 28.70 ? 97  VAL B CG1 1 
ATOM   1832 C CG2 . VAL B 1 97  ? 7.943   12.365  -48.521 1.00 26.30 ? 97  VAL B CG2 1 
ATOM   1833 N N   . SER B 1 98  ? 4.365   15.596  -48.904 1.00 29.09 ? 98  SER B N   1 
ATOM   1834 C CA  . SER B 1 98  ? 3.224   16.331  -48.335 1.00 28.82 ? 98  SER B CA  1 
ATOM   1835 C C   . SER B 1 98  ? 1.944   15.551  -48.761 1.00 28.83 ? 98  SER B C   1 
ATOM   1836 O O   . SER B 1 98  ? 1.726   15.273  -49.949 1.00 27.09 ? 98  SER B O   1 
ATOM   1837 C CB  . SER B 1 98  ? 3.170   17.780  -48.826 1.00 29.74 ? 98  SER B CB  1 
ATOM   1838 O OG  . SER B 1 98  ? 2.746   18.625  -47.750 1.00 32.55 ? 98  SER B OG  1 
ATOM   1839 N N   . ILE B 1 99  ? 1.137   15.143  -47.791 1.00 27.77 ? 99  ILE B N   1 
ATOM   1840 C CA  . ILE B 1 99  ? 0.111   14.162  -48.051 1.00 27.47 ? 99  ILE B CA  1 
ATOM   1841 C C   . ILE B 1 99  ? -0.912  14.434  -46.990 1.00 27.13 ? 99  ILE B C   1 
ATOM   1842 O O   . ILE B 1 99  ? -0.548  14.788  -45.885 1.00 25.54 ? 99  ILE B O   1 
ATOM   1843 C CB  . ILE B 1 99  ? 0.665   12.690  -47.913 1.00 27.18 ? 99  ILE B CB  1 
ATOM   1844 C CG1 . ILE B 1 99  ? 1.610   12.298  -49.074 1.00 28.03 ? 99  ILE B CG1 1 
ATOM   1845 C CG2 . ILE B 1 99  ? -0.421  11.683  -47.823 1.00 27.25 ? 99  ILE B CG2 1 
ATOM   1846 C CD1 . ILE B 1 99  ? 2.261   10.848  -48.916 1.00 27.71 ? 99  ILE B CD1 1 
ATOM   1847 N N   . GLU B 1 100 ? -2.197  14.351  -47.357 1.00 28.68 ? 100 GLU B N   1 
ATOM   1848 C CA  . GLU B 1 100 ? -3.284  14.271  -46.384 1.00 29.45 ? 100 GLU B CA  1 
ATOM   1849 C C   . GLU B 1 100 ? -4.123  13.045  -46.697 1.00 26.82 ? 100 GLU B C   1 
ATOM   1850 O O   . GLU B 1 100 ? -4.534  12.871  -47.827 1.00 26.34 ? 100 GLU B O   1 
ATOM   1851 C CB  . GLU B 1 100 ? -4.088  15.568  -46.320 1.00 29.99 ? 100 GLU B CB  1 
ATOM   1852 C CG  . GLU B 1 100 ? -3.871  16.371  -45.032 1.00 33.55 ? 100 GLU B CG  1 
ATOM   1853 C CD  . GLU B 1 100 ? -4.363  17.846  -45.113 1.00 35.70 ? 100 GLU B CD  1 
ATOM   1854 O OE1 . GLU B 1 100 ? -3.465  18.737  -45.088 1.00 42.59 ? 100 GLU B OE1 1 
ATOM   1855 O OE2 . GLU B 1 100 ? -5.621  18.109  -45.200 1.00 39.23 ? 100 GLU B OE2 1 
ATOM   1856 N N   . ASP B 1 101 ? -4.315  12.183  -45.696 1.00 25.11 ? 101 ASP B N   1 
ATOM   1857 C CA  . ASP B 1 101 ? -5.046  10.906  -45.822 1.00 24.42 ? 101 ASP B CA  1 
ATOM   1858 C C   . ASP B 1 101 ? -6.111  10.657  -44.708 1.00 24.33 ? 101 ASP B C   1 
ATOM   1859 O O   . ASP B 1 101 ? -5.892  10.954  -43.494 1.00 23.76 ? 101 ASP B O   1 
ATOM   1860 C CB  . ASP B 1 101 ? -4.045  9.758   -45.825 1.00 23.26 ? 101 ASP B CB  1 
ATOM   1861 C CG  . ASP B 1 101 ? -4.621  8.482   -46.376 1.00 23.37 ? 101 ASP B CG  1 
ATOM   1862 O OD1 . ASP B 1 101 ? -4.679  8.293   -47.621 1.00 26.30 ? 101 ASP B OD1 1 
ATOM   1863 O OD2 . ASP B 1 101 ? -4.959  7.626   -45.567 1.00 23.09 ? 101 ASP B OD2 1 
ATOM   1864 N N   . SER B 1 102 ? -7.238  10.047  -45.098 1.00 23.76 ? 102 SER B N   1 
ATOM   1865 C CA  . SER B 1 102 ? -8.405  9.947   -44.237 1.00 21.39 ? 102 SER B CA  1 
ATOM   1866 C C   . SER B 1 102 ? -8.667  8.466   -44.016 1.00 21.19 ? 102 SER B C   1 
ATOM   1867 O O   . SER B 1 102 ? -9.710  8.068   -43.429 1.00 19.26 ? 102 SER B O   1 
ATOM   1868 C CB  . SER B 1 102 ? -9.610  10.640  -44.905 1.00 22.62 ? 102 SER B CB  1 
ATOM   1869 O OG  . SER B 1 102 ? -9.416  12.066  -45.148 1.00 24.32 ? 102 SER B OG  1 
ATOM   1870 N N   . VAL B 1 103 ? -7.753  7.623   -44.490 1.00 19.72 ? 103 VAL B N   1 
ATOM   1871 C CA  . VAL B 1 103 ? -7.909  6.174   -44.195 1.00 20.19 ? 103 VAL B CA  1 
ATOM   1872 C C   . VAL B 1 103 ? -7.022  5.639   -43.018 1.00 19.91 ? 103 VAL B C   1 
ATOM   1873 O O   . VAL B 1 103 ? -7.489  4.922   -42.122 1.00 20.51 ? 103 VAL B O   1 
ATOM   1874 C CB  . VAL B 1 103 ? -7.802  5.272   -45.480 1.00 20.40 ? 103 VAL B CB  1 
ATOM   1875 C CG1 . VAL B 1 103 ? -8.029  3.844   -45.094 1.00 21.04 ? 103 VAL B CG1 1 
ATOM   1876 C CG2 . VAL B 1 103 ? -8.847  5.636   -46.540 1.00 20.40 ? 103 VAL B CG2 1 
ATOM   1877 N N   . ILE B 1 104 ? -5.716  5.895   -43.072 1.00 19.39 ? 104 ILE B N   1 
ATOM   1878 C CA  . ILE B 1 104 ? -4.917  5.844   -41.852 1.00 17.26 ? 104 ILE B CA  1 
ATOM   1879 C C   . ILE B 1 104 ? -5.440  6.720   -40.668 1.00 17.86 ? 104 ILE B C   1 
ATOM   1880 O O   . ILE B 1 104 ? -6.138  7.773   -40.829 1.00 19.73 ? 104 ILE B O   1 
ATOM   1881 C CB  . ILE B 1 104 ? -3.435  6.270   -42.112 1.00 17.59 ? 104 ILE B CB  1 
ATOM   1882 C CG1 . ILE B 1 104 ? -3.321  7.744   -42.509 1.00 14.77 ? 104 ILE B CG1 1 
ATOM   1883 C CG2 . ILE B 1 104 ? -2.768  5.347   -43.091 1.00 9.33  ? 104 ILE B CG2 1 
ATOM   1884 C CD1 . ILE B 1 104 ? -1.828  8.264   -42.350 1.00 15.14 ? 104 ILE B CD1 1 
ATOM   1885 N N   . SER B 1 105 ? -5.079  6.268   -39.479 1.00 17.44 ? 105 SER B N   1 
ATOM   1886 C CA  . SER B 1 105 ? -5.284  6.994   -38.256 1.00 17.90 ? 105 SER B CA  1 
ATOM   1887 C C   . SER B 1 105 ? -4.066  6.849   -37.315 1.00 18.86 ? 105 SER B C   1 
ATOM   1888 O O   . SER B 1 105 ? -3.194  5.930   -37.482 1.00 18.06 ? 105 SER B O   1 
ATOM   1889 C CB  . SER B 1 105 ? -6.572  6.551   -37.544 1.00 17.13 ? 105 SER B CB  1 
ATOM   1890 O OG  . SER B 1 105 ? -6.951  7.560   -36.624 1.00 18.27 ? 105 SER B OG  1 
ATOM   1891 N N   . LEU B 1 106 ? -4.024  7.742   -36.328 1.00 18.65 ? 106 LEU B N   1 
ATOM   1892 C CA  . LEU B 1 106 ? -3.080  7.626   -35.211 1.00 21.97 ? 106 LEU B CA  1 
ATOM   1893 C C   . LEU B 1 106 ? -3.754  7.047   -33.963 1.00 23.20 ? 106 LEU B C   1 
ATOM   1894 O O   . LEU B 1 106 ? -3.098  6.837   -32.984 1.00 23.49 ? 106 LEU B O   1 
ATOM   1895 C CB  . LEU B 1 106 ? -2.450  8.973   -34.886 1.00 20.30 ? 106 LEU B CB  1 
ATOM   1896 C CG  . LEU B 1 106 ? -1.812  9.696   -36.053 1.00 22.01 ? 106 LEU B CG  1 
ATOM   1897 C CD1 . LEU B 1 106 ? -1.132  10.933  -35.549 1.00 16.74 ? 106 LEU B CD1 1 
ATOM   1898 C CD2 . LEU B 1 106 ? -0.819  8.727   -36.699 1.00 20.37 ? 106 LEU B CD2 1 
ATOM   1899 N N   . SER B 1 107 ? -5.073  6.780   -34.042 1.00 25.58 ? 107 SER B N   1 
ATOM   1900 C CA  . SER B 1 107 ? -5.825  6.019   -33.045 1.00 24.87 ? 107 SER B CA  1 
ATOM   1901 C C   . SER B 1 107 ? -6.862  5.072   -33.688 1.00 26.02 ? 107 SER B C   1 
ATOM   1902 O O   . SER B 1 107 ? -7.149  5.153   -34.883 1.00 26.06 ? 107 SER B O   1 
ATOM   1903 C CB  . SER B 1 107 ? -6.465  6.941   -32.011 1.00 24.83 ? 107 SER B CB  1 
ATOM   1904 O OG  . SER B 1 107 ? -7.105  8.068   -32.616 1.00 25.35 ? 107 SER B OG  1 
ATOM   1905 N N   . GLY B 1 108 ? -7.333  4.099   -32.911 1.00 26.92 ? 108 GLY B N   1 
ATOM   1906 C CA  . GLY B 1 108 ? -8.353  3.157   -33.360 1.00 27.29 ? 108 GLY B CA  1 
ATOM   1907 C C   . GLY B 1 108 ? -7.825  1.906   -34.045 1.00 27.81 ? 108 GLY B C   1 
ATOM   1908 O O   . GLY B 1 108 ? -6.675  1.497   -33.883 1.00 26.07 ? 108 GLY B O   1 
ATOM   1909 N N   . ASP B 1 109 ? -8.682  1.335   -34.865 1.00 28.44 ? 109 ASP B N   1 
ATOM   1910 C CA  . ASP B 1 109 ? -8.371  0.111   -35.592 1.00 30.92 ? 109 ASP B CA  1 
ATOM   1911 C C   . ASP B 1 109 ? -7.440  0.365   -36.758 1.00 30.85 ? 109 ASP B C   1 
ATOM   1912 O O   . ASP B 1 109 ? -6.695  -0.535  -37.122 1.00 32.61 ? 109 ASP B O   1 
ATOM   1913 C CB  . ASP B 1 109 ? -9.655  -0.534  -36.091 1.00 31.12 ? 109 ASP B CB  1 
ATOM   1914 C CG  . ASP B 1 109 ? -10.855 -0.247  -35.160 1.00 34.48 ? 109 ASP B CG  1 
ATOM   1915 O OD1 . ASP B 1 109 ? -11.427 0.918   -35.157 1.00 31.74 ? 109 ASP B OD1 1 
ATOM   1916 O OD2 . ASP B 1 109 ? -11.157 -1.206  -34.412 1.00 35.81 ? 109 ASP B OD2 1 
ATOM   1917 N N   . HIS B 1 110 ? -7.543  1.566   -37.363 1.00 31.30 ? 110 HIS B N   1 
ATOM   1918 C CA  . HIS B 1 110 ? -6.713  2.016   -38.531 1.00 28.75 ? 110 HIS B CA  1 
ATOM   1919 C C   . HIS B 1 110 ? -5.380  2.657   -38.045 1.00 26.87 ? 110 HIS B C   1 
ATOM   1920 O O   . HIS B 1 110 ? -4.633  3.237   -38.860 1.00 25.06 ? 110 HIS B O   1 
ATOM   1921 C CB  . HIS B 1 110 ? -7.496  2.986   -39.451 1.00 27.95 ? 110 HIS B CB  1 
ATOM   1922 C CG  . HIS B 1 110 ? -8.530  2.325   -40.353 1.00 31.40 ? 110 HIS B CG  1 
ATOM   1923 N ND1 . HIS B 1 110 ? -9.207  3.017   -41.350 1.00 28.00 ? 110 HIS B ND1 1 
ATOM   1924 C CD2 . HIS B 1 110 ? -8.972  1.037   -40.437 1.00 32.73 ? 110 HIS B CD2 1 
ATOM   1925 C CE1 . HIS B 1 110 ? -10.031 2.193   -41.976 1.00 30.07 ? 110 HIS B CE1 1 
ATOM   1926 N NE2 . HIS B 1 110 ? -9.891  0.984   -41.462 1.00 30.09 ? 110 HIS B NE2 1 
ATOM   1927 N N   . CYS B 1 111 ? -5.094  2.521   -36.730 1.00 23.15 ? 111 CYS B N   1 
ATOM   1928 C CA  . CYS B 1 111 ? -3.893  3.093   -36.152 1.00 21.51 ? 111 CYS B CA  1 
ATOM   1929 C C   . CYS B 1 111 ? -2.574  2.579   -36.723 1.00 19.01 ? 111 CYS B C   1 
ATOM   1930 O O   . CYS B 1 111 ? -2.294  1.367   -36.840 1.00 18.46 ? 111 CYS B O   1 
ATOM   1931 C CB  . CYS B 1 111 ? -3.870  2.990   -34.624 1.00 21.93 ? 111 CYS B CB  1 
ATOM   1932 S SG  . CYS B 1 111 ? -2.497  3.884   -33.854 1.00 19.92 ? 111 CYS B SG  1 
ATOM   1933 N N   . ILE B 1 112 ? -1.742  3.524   -37.088 1.00 18.41 ? 112 ILE B N   1 
ATOM   1934 C CA  . ILE B 1 112 ? -0.451  3.193   -37.681 1.00 16.67 ? 112 ILE B CA  1 
ATOM   1935 C C   . ILE B 1 112 ? 0.756   3.438   -36.737 1.00 17.90 ? 112 ILE B C   1 
ATOM   1936 O O   . ILE B 1 112 ? 1.904   3.264   -37.151 1.00 16.95 ? 112 ILE B O   1 
ATOM   1937 C CB  . ILE B 1 112 ? -0.278  3.852   -39.046 1.00 18.51 ? 112 ILE B CB  1 
ATOM   1938 C CG1 . ILE B 1 112 ? -0.218  5.401   -38.928 1.00 15.37 ? 112 ILE B CG1 1 
ATOM   1939 C CG2 . ILE B 1 112 ? -1.360  3.324   -40.054 1.00 15.81 ? 112 ILE B CG2 1 
ATOM   1940 C CD1 . ILE B 1 112 ? 0.248   6.006   -40.186 1.00 18.37 ? 112 ILE B CD1 1 
ATOM   1941 N N   . ILE B 1 113 ? 0.496   3.798   -35.471 1.00 17.48 ? 113 ILE B N   1 
ATOM   1942 C CA  . ILE B 1 113 ? 1.553   3.880   -34.481 1.00 18.53 ? 113 ILE B CA  1 
ATOM   1943 C C   . ILE B 1 113 ? 2.111   2.482   -34.154 1.00 17.89 ? 113 ILE B C   1 
ATOM   1944 O O   . ILE B 1 113 ? 1.364   1.510   -33.925 1.00 20.56 ? 113 ILE B O   1 
ATOM   1945 C CB  . ILE B 1 113 ? 1.228   4.869   -33.251 1.00 18.26 ? 113 ILE B CB  1 
ATOM   1946 C CG1 . ILE B 1 113 ? 1.320   6.318   -33.740 1.00 18.76 ? 113 ILE B CG1 1 
ATOM   1947 C CG2 . ILE B 1 113 ? 2.173   4.578   -32.022 1.00 16.90 ? 113 ILE B CG2 1 
ATOM   1948 C CD1 . ILE B 1 113 ? 0.670   7.477   -32.868 1.00 21.24 ? 113 ILE B CD1 1 
ATOM   1949 N N   . GLY B 1 114 ? 3.431   2.339   -34.241 1.00 16.77 ? 114 GLY B N   1 
ATOM   1950 C CA  . GLY B 1 114 ? 4.038   1.048   -33.982 1.00 16.53 ? 114 GLY B CA  1 
ATOM   1951 C C   . GLY B 1 114 ? 4.004   0.137   -35.192 1.00 15.43 ? 114 GLY B C   1 
ATOM   1952 O O   . GLY B 1 114 ? 4.288   -1.043  -35.071 1.00 16.51 ? 114 GLY B O   1 
ATOM   1953 N N   . ARG B 1 115 ? 3.666   0.677   -36.363 1.00 14.68 ? 115 ARG B N   1 
ATOM   1954 C CA  . ARG B 1 115 ? 3.725   -0.105  -37.595 1.00 15.04 ? 115 ARG B CA  1 
ATOM   1955 C C   . ARG B 1 115 ? 4.890   0.541   -38.362 1.00 16.21 ? 115 ARG B C   1 
ATOM   1956 O O   . ARG B 1 115 ? 5.600   1.434   -37.805 1.00 15.24 ? 115 ARG B O   1 
ATOM   1957 C CB  . ARG B 1 115 ? 2.384   -0.059  -38.394 1.00 14.28 ? 115 ARG B CB  1 
ATOM   1958 C CG  . ARG B 1 115 ? 1.285   -1.083  -37.744 1.00 16.18 ? 115 ARG B CG  1 
ATOM   1959 C CD  . ARG B 1 115 ? -0.155  -0.798  -38.164 1.00 12.63 ? 115 ARG B CD  1 
ATOM   1960 N NE  . ARG B 1 115 ? -1.186  -1.280  -37.218 1.00 12.22 ? 115 ARG B NE  1 
ATOM   1961 C CZ  . ARG B 1 115 ? -1.380  -2.585  -36.917 1.00 13.89 ? 115 ARG B CZ  1 
ATOM   1962 N NH1 . ARG B 1 115 ? -0.584  -3.495  -37.420 1.00 7.81  ? 115 ARG B NH1 1 
ATOM   1963 N NH2 . ARG B 1 115 ? -2.340  -2.977  -36.122 1.00 18.67 ? 115 ARG B NH2 1 
ATOM   1964 N N   . THR B 1 116 ? 5.072   0.137   -39.626 1.00 16.23 ? 116 THR B N   1 
ATOM   1965 C CA  . THR B 1 116 ? 6.251   0.644   -40.377 1.00 17.00 ? 116 THR B CA  1 
ATOM   1966 C C   . THR B 1 116 ? 5.972   1.486   -41.631 1.00 15.90 ? 116 THR B C   1 
ATOM   1967 O O   . THR B 1 116 ? 5.273   1.101   -42.480 1.00 17.65 ? 116 THR B O   1 
ATOM   1968 C CB  . THR B 1 116 ? 7.202   -0.576  -40.651 1.00 15.99 ? 116 THR B CB  1 
ATOM   1969 O OG1 . THR B 1 116 ? 7.805   -0.996  -39.423 1.00 15.90 ? 116 THR B OG1 1 
ATOM   1970 C CG2 . THR B 1 116 ? 8.303   -0.304  -41.652 1.00 15.31 ? 116 THR B CG2 1 
ATOM   1971 N N   . LEU B 1 117 ? 6.568   2.649   -41.760 1.00 18.13 ? 117 LEU B N   1 
ATOM   1972 C CA  . LEU B 1 117 ? 6.545   3.348   -42.995 1.00 16.65 ? 117 LEU B CA  1 
ATOM   1973 C C   . LEU B 1 117 ? 7.721   2.836   -43.876 1.00 18.38 ? 117 LEU B C   1 
ATOM   1974 O O   . LEU B 1 117 ? 8.854   2.649   -43.401 1.00 20.82 ? 117 LEU B O   1 
ATOM   1975 C CB  . LEU B 1 117 ? 6.625   4.820   -42.690 1.00 18.36 ? 117 LEU B CB  1 
ATOM   1976 C CG  . LEU B 1 117 ? 6.377   5.773   -43.857 1.00 16.14 ? 117 LEU B CG  1 
ATOM   1977 C CD1 . LEU B 1 117 ? 4.903   5.735   -44.322 1.00 20.42 ? 117 LEU B CD1 1 
ATOM   1978 C CD2 . LEU B 1 117 ? 6.760   7.128   -43.345 1.00 15.59 ? 117 LEU B CD2 1 
ATOM   1979 N N   . VAL B 1 118 ? 7.459   2.518   -45.146 1.00 18.08 ? 118 VAL B N   1 
ATOM   1980 C CA  . VAL B 1 118 ? 8.537   2.001   -46.017 1.00 16.44 ? 118 VAL B CA  1 
ATOM   1981 C C   . VAL B 1 118 ? 8.502   2.739   -47.303 1.00 17.57 ? 118 VAL B C   1 
ATOM   1982 O O   . VAL B 1 118 ? 7.431   2.982   -47.829 1.00 16.63 ? 118 VAL B O   1 
ATOM   1983 C CB  . VAL B 1 118 ? 8.351   0.471   -46.459 1.00 15.71 ? 118 VAL B CB  1 
ATOM   1984 C CG1 . VAL B 1 118 ? 9.393   0.117   -47.532 1.00 15.78 ? 118 VAL B CG1 1 
ATOM   1985 C CG2 . VAL B 1 118 ? 8.421   -0.551  -45.304 1.00 10.75 ? 118 VAL B CG2 1 
ATOM   1986 N N   . VAL B 1 119 ? 9.701   3.100   -47.791 1.00 19.66 ? 119 VAL B N   1 
ATOM   1987 C CA  . VAL B 1 119 ? 9.926   3.685   -49.102 1.00 20.41 ? 119 VAL B CA  1 
ATOM   1988 C C   . VAL B 1 119 ? 10.609  2.608   -49.948 1.00 20.74 ? 119 VAL B C   1 
ATOM   1989 O O   . VAL B 1 119 ? 11.597  1.955   -49.515 1.00 20.93 ? 119 VAL B O   1 
ATOM   1990 C CB  . VAL B 1 119 ? 10.681  5.066   -49.040 1.00 20.50 ? 119 VAL B CB  1 
ATOM   1991 C CG1 . VAL B 1 119 ? 12.095  4.953   -48.490 1.00 20.88 ? 119 VAL B CG1 1 
ATOM   1992 C CG2 . VAL B 1 119 ? 10.678  5.844   -50.449 1.00 19.09 ? 119 VAL B CG2 1 
ATOM   1993 N N   . HIS B 1 120 ? 10.006  2.415   -51.121 1.00 20.59 ? 120 HIS B N   1 
ATOM   1994 C CA  . HIS B 1 120 ? 10.279  1.394   -52.108 1.00 21.28 ? 120 HIS B CA  1 
ATOM   1995 C C   . HIS B 1 120 ? 11.090  1.877   -53.273 1.00 22.36 ? 120 HIS B C   1 
ATOM   1996 O O   . HIS B 1 120 ? 11.175  3.099   -53.528 1.00 22.61 ? 120 HIS B O   1 
ATOM   1997 C CB  . HIS B 1 120 ? 8.954   0.851   -52.629 1.00 20.03 ? 120 HIS B CB  1 
ATOM   1998 C CG  . HIS B 1 120 ? 8.239   0.029   -51.601 1.00 18.04 ? 120 HIS B CG  1 
ATOM   1999 N ND1 . HIS B 1 120 ? 8.406   -1.335  -51.479 1.00 13.30 ? 120 HIS B ND1 1 
ATOM   2000 C CD2 . HIS B 1 120 ? 7.412   0.404   -50.601 1.00 10.33 ? 120 HIS B CD2 1 
ATOM   2001 C CE1 . HIS B 1 120 ? 7.686   -1.775  -50.466 1.00 15.02 ? 120 HIS B CE1 1 
ATOM   2002 N NE2 . HIS B 1 120 ? 7.054   -0.745  -49.931 1.00 19.55 ? 120 HIS B NE2 1 
ATOM   2003 N N   . GLU B 1 121 ? 11.687  0.884   -53.923 1.00 23.57 ? 121 GLU B N   1 
ATOM   2004 C CA  . GLU B 1 121 ? 12.583  0.961   -55.118 1.00 25.97 ? 121 GLU B CA  1 
ATOM   2005 C C   . GLU B 1 121 ? 12.017  1.799   -56.247 1.00 25.85 ? 121 GLU B C   1 
ATOM   2006 O O   . GLU B 1 121 ? 12.670  2.728   -56.737 1.00 27.13 ? 121 GLU B O   1 
ATOM   2007 C CB  . GLU B 1 121 ? 12.879  -0.497  -55.597 1.00 24.78 ? 121 GLU B CB  1 
ATOM   2008 C CG  . GLU B 1 121 ? 13.757  -0.779  -56.856 1.00 25.47 ? 121 GLU B CG  1 
ATOM   2009 C CD  . GLU B 1 121 ? 14.012  -2.297  -57.044 1.00 29.92 ? 121 GLU B CD  1 
ATOM   2010 O OE1 . GLU B 1 121 ? 15.126  -2.685  -57.496 1.00 36.88 ? 121 GLU B OE1 1 
ATOM   2011 O OE2 . GLU B 1 121 ? 13.128  -3.147  -56.697 1.00 29.75 ? 121 GLU B OE2 1 
ATOM   2012 N N   . LYS B 1 122 ? 10.758  1.525   -56.594 1.00 26.05 ? 122 LYS B N   1 
ATOM   2013 C CA  . LYS B 1 122 ? 10.185  1.964   -57.839 1.00 26.04 ? 122 LYS B CA  1 
ATOM   2014 C C   . LYS B 1 122 ? 8.802   2.522   -57.516 1.00 24.88 ? 122 LYS B C   1 
ATOM   2015 O O   . LYS B 1 122 ? 8.322   2.377   -56.403 1.00 22.48 ? 122 LYS B O   1 
ATOM   2016 C CB  . LYS B 1 122 ? 9.902   0.731   -58.739 1.00 26.30 ? 122 LYS B CB  1 
ATOM   2017 C CG  . LYS B 1 122 ? 11.041  -0.094  -59.300 1.00 29.14 ? 122 LYS B CG  1 
ATOM   2018 C CD  . LYS B 1 122 ? 10.491  -1.373  -59.963 1.00 29.43 ? 122 LYS B CD  1 
ATOM   2019 C CE  . LYS B 1 122 ? 11.614  -2.374  -60.270 1.00 39.21 ? 122 LYS B CE  1 
ATOM   2020 N NZ  . LYS B 1 122 ? 12.253  -2.211  -61.669 1.00 44.17 ? 122 LYS B NZ  1 
ATOM   2021 N N   . ALA B 1 123 ? 8.136   3.059   -58.555 1.00 24.08 ? 123 ALA B N   1 
ATOM   2022 C CA  . ALA B 1 123 ? 6.710   3.407   -58.486 1.00 23.16 ? 123 ALA B CA  1 
ATOM   2023 C C   . ALA B 1 123 ? 5.792   2.302   -58.014 1.00 22.84 ? 123 ALA B C   1 
ATOM   2024 O O   . ALA B 1 123 ? 5.737   1.212   -58.585 1.00 21.59 ? 123 ALA B O   1 
ATOM   2025 C CB  . ALA B 1 123 ? 6.243   3.873   -59.772 1.00 22.80 ? 123 ALA B CB  1 
ATOM   2026 N N   . ASP B 1 124 ? 5.014   2.630   -56.984 1.00 23.70 ? 124 ASP B N   1 
ATOM   2027 C CA  . ASP B 1 124 ? 3.682   1.991   -56.832 1.00 22.07 ? 124 ASP B CA  1 
ATOM   2028 C C   . ASP B 1 124 ? 2.831   2.289   -58.168 1.00 20.63 ? 124 ASP B C   1 
ATOM   2029 O O   . ASP B 1 124 ? 2.525   3.452   -58.503 1.00 18.38 ? 124 ASP B O   1 
ATOM   2030 C CB  . ASP B 1 124 ? 3.050   2.465   -55.511 1.00 19.96 ? 124 ASP B CB  1 
ATOM   2031 C CG  . ASP B 1 124 ? 1.743   1.813   -55.220 1.00 21.16 ? 124 ASP B CG  1 
ATOM   2032 O OD1 . ASP B 1 124 ? 1.322   0.868   -55.964 1.00 28.61 ? 124 ASP B OD1 1 
ATOM   2033 O OD2 . ASP B 1 124 ? 1.135   2.168   -54.193 1.00 18.65 ? 124 ASP B OD2 1 
ATOM   2034 N N   . ASP B 1 125 ? 2.528   1.226   -58.921 1.00 19.82 ? 125 ASP B N   1 
ATOM   2035 C CA  . ASP B 1 125 ? 1.553   1.294   -60.044 1.00 22.88 ? 125 ASP B CA  1 
ATOM   2036 C C   . ASP B 1 125 ? 0.069   1.416   -59.658 1.00 22.52 ? 125 ASP B C   1 
ATOM   2037 O O   . ASP B 1 125 ? -0.750  1.661   -60.540 1.00 22.90 ? 125 ASP B O   1 
ATOM   2038 C CB  . ASP B 1 125 ? 1.716   0.176   -61.137 1.00 21.86 ? 125 ASP B CB  1 
ATOM   2039 C CG  . ASP B 1 125 ? 1.365   -1.214  -60.644 1.00 23.29 ? 125 ASP B CG  1 
ATOM   2040 O OD1 . ASP B 1 125 ? 0.494   -1.418  -59.741 1.00 26.51 ? 125 ASP B OD1 1 
ATOM   2041 O OD2 . ASP B 1 125 ? 1.976   -2.154  -61.189 1.00 23.07 ? 125 ASP B OD2 1 
ATOM   2042 N N   . LEU B 1 126 ? -0.246  1.251   -58.368 1.00 22.68 ? 126 LEU B N   1 
ATOM   2043 C CA  . LEU B 1 126 ? -1.537  1.643   -57.753 1.00 21.57 ? 126 LEU B CA  1 
ATOM   2044 C C   . LEU B 1 126 ? -2.695  0.787   -58.177 1.00 23.68 ? 126 LEU B C   1 
ATOM   2045 O O   . LEU B 1 126 ? -3.830  1.276   -58.344 1.00 24.95 ? 126 LEU B O   1 
ATOM   2046 C CB  . LEU B 1 126 ? -1.918  3.109   -57.966 1.00 20.94 ? 126 LEU B CB  1 
ATOM   2047 C CG  . LEU B 1 126 ? -0.978  4.286   -57.843 1.00 16.62 ? 126 LEU B CG  1 
ATOM   2048 C CD1 . LEU B 1 126 ? -1.756  5.486   -58.381 1.00 22.72 ? 126 LEU B CD1 1 
ATOM   2049 C CD2 . LEU B 1 126 ? -0.530  4.516   -56.469 1.00 16.25 ? 126 LEU B CD2 1 
ATOM   2050 N N   . GLY B 1 127 ? -2.439  -0.499  -58.338 1.00 24.34 ? 127 GLY B N   1 
ATOM   2051 C CA  . GLY B 1 127 ? -3.464  -1.381  -58.853 1.00 25.57 ? 127 GLY B CA  1 
ATOM   2052 C C   . GLY B 1 127 ? -3.674  -1.369  -60.348 1.00 27.86 ? 127 GLY B C   1 
ATOM   2053 O O   . GLY B 1 127 ? -4.249  -2.305  -60.873 1.00 26.87 ? 127 GLY B O   1 
ATOM   2054 N N   . LYS B 1 128 ? -3.168  -0.317  -61.024 1.00 30.11 ? 128 LYS B N   1 
ATOM   2055 C CA  . LYS B 1 128 ? -3.342  -0.076  -62.457 1.00 31.14 ? 128 LYS B CA  1 
ATOM   2056 C C   . LYS B 1 128 ? -2.136  -0.476  -63.292 1.00 32.27 ? 128 LYS B C   1 
ATOM   2057 O O   . LYS B 1 128 ? -1.841  0.203   -64.274 1.00 32.12 ? 128 LYS B O   1 
ATOM   2058 C CB  . LYS B 1 128 ? -3.654  1.410   -62.687 1.00 32.72 ? 128 LYS B CB  1 
ATOM   2059 C CG  . LYS B 1 128 ? -5.191  1.730   -62.753 1.00 34.73 ? 128 LYS B CG  1 
ATOM   2060 C CD  . LYS B 1 128 ? -5.612  2.870   -61.821 1.00 37.00 ? 128 LYS B CD  1 
ATOM   2061 C CE  . LYS B 1 128 ? -7.169  3.066   -61.886 1.00 38.21 ? 128 LYS B CE  1 
ATOM   2062 N NZ  . LYS B 1 128 ? -7.920  3.674   -60.705 1.00 38.49 ? 128 LYS B NZ  1 
ATOM   2063 N N   . GLY B 1 129 ? -1.467  -1.588  -62.929 1.00 31.93 ? 129 GLY B N   1 
ATOM   2064 C CA  . GLY B 1 129 ? -0.195  -1.994  -63.554 1.00 32.22 ? 129 GLY B CA  1 
ATOM   2065 C C   . GLY B 1 129 ? -0.156  -3.249  -64.422 1.00 32.01 ? 129 GLY B C   1 
ATOM   2066 O O   . GLY B 1 129 ? 0.863   -3.599  -65.001 1.00 31.51 ? 129 GLY B O   1 
ATOM   2067 N N   . GLY B 1 130 ? -1.288  -3.907  -64.524 1.00 32.77 ? 130 GLY B N   1 
ATOM   2068 C CA  . GLY B 1 130 ? -1.553  -4.801  -65.643 1.00 32.13 ? 130 GLY B CA  1 
ATOM   2069 C C   . GLY B 1 130 ? -1.232  -6.227  -65.334 1.00 31.03 ? 130 GLY B C   1 
ATOM   2070 O O   . GLY B 1 130 ? -1.340  -7.070  -66.172 1.00 31.21 ? 130 GLY B O   1 
ATOM   2071 N N   . ASN B 1 131 ? -0.812  -6.513  -64.120 1.00 31.81 ? 131 ASN B N   1 
ATOM   2072 C CA  . ASN B 1 131 ? -0.582  -7.915  -63.744 1.00 32.09 ? 131 ASN B CA  1 
ATOM   2073 C C   . ASN B 1 131 ? -1.116  -8.198  -62.350 1.00 32.93 ? 131 ASN B C   1 
ATOM   2074 O O   . ASN B 1 131 ? -1.600  -7.318  -61.669 1.00 32.19 ? 131 ASN B O   1 
ATOM   2075 C CB  . ASN B 1 131 ? 0.925   -8.303  -63.869 1.00 31.61 ? 131 ASN B CB  1 
ATOM   2076 C CG  . ASN B 1 131 ? 1.820   -7.382  -63.063 1.00 30.56 ? 131 ASN B CG  1 
ATOM   2077 O OD1 . ASN B 1 131 ? 1.465   -7.024  -61.958 1.00 25.14 ? 131 ASN B OD1 1 
ATOM   2078 N ND2 . ASN B 1 131 ? 2.984   -6.996  -63.612 1.00 27.60 ? 131 ASN B ND2 1 
ATOM   2079 N N   . GLU B 1 132 ? -1.037  -9.467  -61.978 1.00 34.60 ? 132 GLU B N   1 
ATOM   2080 C CA  . GLU B 1 132 ? -1.323  -9.983  -60.660 1.00 35.68 ? 132 GLU B CA  1 
ATOM   2081 C C   . GLU B 1 132 ? -0.675  -9.165  -59.544 1.00 34.78 ? 132 GLU B C   1 
ATOM   2082 O O   . GLU B 1 132 ? -1.338  -8.695  -58.597 1.00 34.72 ? 132 GLU B O   1 
ATOM   2083 C CB  . GLU B 1 132 ? -0.743  -11.397 -60.607 1.00 36.87 ? 132 GLU B CB  1 
ATOM   2084 C CG  . GLU B 1 132 ? -1.307  -12.218 -59.514 1.00 41.33 ? 132 GLU B CG  1 
ATOM   2085 C CD  . GLU B 1 132 ? -2.692  -12.705 -59.887 1.00 47.60 ? 132 GLU B CD  1 
ATOM   2086 O OE1 . GLU B 1 132 ? -3.567  -12.758 -58.983 1.00 49.87 ? 132 GLU B OE1 1 
ATOM   2087 O OE2 . GLU B 1 132 ? -2.896  -13.016 -61.097 1.00 48.95 ? 132 GLU B OE2 1 
ATOM   2088 N N   . GLU B 1 133 ? 0.640   -9.028  -59.641 1.00 32.86 ? 133 GLU B N   1 
ATOM   2089 C CA  . GLU B 1 133 ? 1.385   -8.425  -58.547 1.00 31.50 ? 133 GLU B CA  1 
ATOM   2090 C C   . GLU B 1 133 ? 0.859   -7.022  -58.243 1.00 28.91 ? 133 GLU B C   1 
ATOM   2091 O O   . GLU B 1 133 ? 0.821   -6.586  -57.081 1.00 25.19 ? 133 GLU B O   1 
ATOM   2092 C CB  . GLU B 1 133 ? 2.881   -8.454  -58.873 1.00 31.94 ? 133 GLU B CB  1 
ATOM   2093 C CG  . GLU B 1 133 ? 3.872   -8.190  -57.722 1.00 36.47 ? 133 GLU B CG  1 
ATOM   2094 C CD  . GLU B 1 133 ? 3.456   -8.726  -56.361 1.00 38.29 ? 133 GLU B CD  1 
ATOM   2095 O OE1 . GLU B 1 133 ? 2.688   -9.715  -56.244 1.00 42.97 ? 133 GLU B OE1 1 
ATOM   2096 O OE2 . GLU B 1 133 ? 3.926   -8.131  -55.385 1.00 41.47 ? 133 GLU B OE2 1 
ATOM   2097 N N   . SER B 1 134 ? 0.437   -6.339  -59.311 1.00 27.06 ? 134 SER B N   1 
ATOM   2098 C CA  . SER B 1 134 ? -0.066  -4.953  -59.268 1.00 25.70 ? 134 SER B CA  1 
ATOM   2099 C C   . SER B 1 134 ? -1.189  -4.707  -58.267 1.00 26.14 ? 134 SER B C   1 
ATOM   2100 O O   . SER B 1 134 ? -1.300  -3.675  -57.621 1.00 26.41 ? 134 SER B O   1 
ATOM   2101 C CB  . SER B 1 134 ? -0.605  -4.574  -60.672 1.00 25.13 ? 134 SER B CB  1 
ATOM   2102 O OG  . SER B 1 134 ? -1.000  -3.200  -60.744 1.00 20.89 ? 134 SER B OG  1 
ATOM   2103 N N   . THR B 1 135 ? -2.093  -5.661  -58.223 1.00 28.20 ? 135 THR B N   1 
ATOM   2104 C CA  . THR B 1 135 ? -3.294  -5.539  -57.464 1.00 30.17 ? 135 THR B CA  1 
ATOM   2105 C C   . THR B 1 135 ? -3.024  -6.126  -56.079 1.00 29.89 ? 135 THR B C   1 
ATOM   2106 O O   . THR B 1 135 ? -3.908  -6.228  -55.262 1.00 30.37 ? 135 THR B O   1 
ATOM   2107 C CB  . THR B 1 135 ? -4.432  -6.247  -58.266 1.00 30.49 ? 135 THR B CB  1 
ATOM   2108 O OG1 . THR B 1 135 ? -5.655  -5.626  -57.945 1.00 37.37 ? 135 THR B OG1 1 
ATOM   2109 C CG2 . THR B 1 135 ? -4.537  -7.729  -57.970 1.00 30.23 ? 135 THR B CG2 1 
ATOM   2110 N N   . LYS B 1 136 ? -1.793  -6.555  -55.832 1.00 30.14 ? 136 LYS B N   1 
ATOM   2111 C CA  . LYS B 1 136 ? -1.436  -6.958  -54.482 1.00 31.35 ? 136 LYS B CA  1 
ATOM   2112 C C   . LYS B 1 136 ? -0.516  -6.006  -53.717 1.00 29.68 ? 136 LYS B C   1 
ATOM   2113 O O   . LYS B 1 136 ? -0.745  -5.770  -52.557 1.00 30.86 ? 136 LYS B O   1 
ATOM   2114 C CB  . LYS B 1 136 ? -0.923  -8.408  -54.440 1.00 32.16 ? 136 LYS B CB  1 
ATOM   2115 C CG  . LYS B 1 136 ? -1.737  -9.344  -55.287 1.00 33.93 ? 136 LYS B CG  1 
ATOM   2116 C CD  . LYS B 1 136 ? -0.984  -10.658 -55.373 1.00 41.41 ? 136 LYS B CD  1 
ATOM   2117 C CE  . LYS B 1 136 ? -1.876  -11.834 -55.740 1.00 41.48 ? 136 LYS B CE  1 
ATOM   2118 N NZ  . LYS B 1 136 ? -0.985  -13.015 -55.653 1.00 44.65 ? 136 LYS B NZ  1 
ATOM   2119 N N   . THR B 1 137 ? 0.498   -5.450  -54.374 1.00 29.70 ? 137 THR B N   1 
ATOM   2120 C CA  . THR B 1 137 ? 1.550   -4.656  -53.758 1.00 28.50 ? 137 THR B CA  1 
ATOM   2121 C C   . THR B 1 137 ? 1.828   -3.433  -54.612 1.00 28.51 ? 137 THR B C   1 
ATOM   2122 O O   . THR B 1 137 ? 2.403   -2.447  -54.128 1.00 29.47 ? 137 THR B O   1 
ATOM   2123 C CB  . THR B 1 137 ? 2.849   -5.414  -53.695 1.00 29.81 ? 137 THR B CB  1 
ATOM   2124 O OG1 . THR B 1 137 ? 3.422   -5.529  -55.019 1.00 33.04 ? 137 THR B OG1 1 
ATOM   2125 C CG2 . THR B 1 137 ? 2.675   -6.806  -53.037 1.00 31.53 ? 137 THR B CG2 1 
ATOM   2126 N N   . GLY B 1 138 ? 1.428   -3.483  -55.892 1.00 26.60 ? 138 GLY B N   1 
ATOM   2127 C CA  . GLY B 1 138 ? 1.605   -2.346  -56.789 1.00 22.85 ? 138 GLY B CA  1 
ATOM   2128 C C   . GLY B 1 138 ? 2.958   -2.340  -57.471 1.00 21.14 ? 138 GLY B C   1 
ATOM   2129 O O   . GLY B 1 138 ? 3.412   -1.335  -57.993 1.00 19.11 ? 138 GLY B O   1 
ATOM   2130 N N   . ASN B 1 139 ? 3.602   -3.486  -57.471 1.00 21.25 ? 139 ASN B N   1 
ATOM   2131 C CA  . ASN B 1 139 ? 4.953   -3.612  -58.008 1.00 22.83 ? 139 ASN B CA  1 
ATOM   2132 C C   . ASN B 1 139 ? 5.943   -2.521  -57.623 1.00 23.07 ? 139 ASN B C   1 
ATOM   2133 O O   . ASN B 1 139 ? 6.552   -1.922  -58.529 1.00 22.23 ? 139 ASN B O   1 
ATOM   2134 C CB  . ASN B 1 139 ? 4.899   -3.698  -59.561 1.00 22.57 ? 139 ASN B CB  1 
ATOM   2135 C CG  . ASN B 1 139 ? 4.134   -4.862  -60.035 1.00 25.23 ? 139 ASN B CG  1 
ATOM   2136 O OD1 . ASN B 1 139 ? 4.395   -5.981  -59.606 1.00 32.03 ? 139 ASN B OD1 1 
ATOM   2137 N ND2 . ASN B 1 139 ? 3.120   -4.620  -60.841 1.00 30.20 ? 139 ASN B ND2 1 
ATOM   2138 N N   . ALA B 1 140 ? 6.099   -2.183  -56.330 1.00 23.16 ? 140 ALA B N   1 
ATOM   2139 C CA  . ALA B 1 140 ? 6.957   -0.982  -56.054 1.00 22.33 ? 140 ALA B CA  1 
ATOM   2140 C C   . ALA B 1 140 ? 8.421   -1.368  -55.775 1.00 21.62 ? 140 ALA B C   1 
ATOM   2141 O O   . ALA B 1 140 ? 9.299   -0.546  -55.709 1.00 20.89 ? 140 ALA B O   1 
ATOM   2142 C CB  . ALA B 1 140 ? 6.383   -0.086  -54.954 1.00 22.93 ? 140 ALA B CB  1 
ATOM   2143 N N   . GLY B 1 141 ? 8.663   -2.652  -55.670 1.00 22.57 ? 141 GLY B N   1 
ATOM   2144 C CA  . GLY B 1 141 ? 10.017  -3.183  -55.629 1.00 22.18 ? 141 GLY B CA  1 
ATOM   2145 C C   . GLY B 1 141 ? 10.506  -3.330  -54.193 1.00 21.39 ? 141 GLY B C   1 
ATOM   2146 O O   . GLY B 1 141 ? 9.721   -3.445  -53.225 1.00 21.22 ? 141 GLY B O   1 
ATOM   2147 N N   . SER B 1 142 ? 11.832  -3.308  -54.094 1.00 21.18 ? 142 SER B N   1 
ATOM   2148 C CA  . SER B 1 142 ? 12.589  -3.471  -52.891 1.00 21.20 ? 142 SER B CA  1 
ATOM   2149 C C   . SER B 1 142 ? 12.286  -2.353  -51.863 1.00 21.21 ? 142 SER B C   1 
ATOM   2150 O O   . SER B 1 142 ? 11.802  -1.277  -52.189 1.00 21.43 ? 142 SER B O   1 
ATOM   2151 C CB  . SER B 1 142 ? 14.081  -3.502  -53.273 1.00 19.52 ? 142 SER B CB  1 
ATOM   2152 O OG  . SER B 1 142 ? 14.635  -2.202  -53.160 1.00 22.44 ? 142 SER B OG  1 
ATOM   2153 N N   . ARG B 1 143 ? 12.631  -2.622  -50.609 1.00 21.87 ? 143 ARG B N   1 
ATOM   2154 C CA  . ARG B 1 143 ? 12.374  -1.685  -49.549 1.00 20.29 ? 143 ARG B CA  1 
ATOM   2155 C C   . ARG B 1 143 ? 13.715  -1.005  -49.333 1.00 20.24 ? 143 ARG B C   1 
ATOM   2156 O O   . ARG B 1 143 ? 14.672  -1.658  -48.944 1.00 19.95 ? 143 ARG B O   1 
ATOM   2157 C CB  . ARG B 1 143 ? 11.918  -2.458  -48.351 1.00 19.99 ? 143 ARG B CB  1 
ATOM   2158 C CG  . ARG B 1 143 ? 10.594  -3.156  -48.536 1.00 18.29 ? 143 ARG B CG  1 
ATOM   2159 C CD  . ARG B 1 143 ? 10.315  -4.061  -47.364 1.00 21.06 ? 143 ARG B CD  1 
ATOM   2160 N NE  . ARG B 1 143 ? 9.255   -4.981  -47.754 1.00 24.06 ? 143 ARG B NE  1 
ATOM   2161 C CZ  . ARG B 1 143 ? 8.363   -5.550  -46.939 1.00 26.97 ? 143 ARG B CZ  1 
ATOM   2162 N NH1 . ARG B 1 143 ? 8.312   -5.254  -45.644 1.00 22.73 ? 143 ARG B NH1 1 
ATOM   2163 N NH2 . ARG B 1 143 ? 7.459   -6.384  -47.464 1.00 26.65 ? 143 ARG B NH2 1 
ATOM   2164 N N   . LEU B 1 144 ? 13.783  0.303   -49.591 1.00 18.17 ? 144 LEU B N   1 
ATOM   2165 C CA  . LEU B 1 144 ? 15.036  1.079   -49.532 1.00 16.49 ? 144 LEU B CA  1 
ATOM   2166 C C   . LEU B 1 144 ? 15.379  1.600   -48.130 1.00 16.55 ? 144 LEU B C   1 
ATOM   2167 O O   . LEU B 1 144 ? 16.569  1.708   -47.756 1.00 16.14 ? 144 LEU B O   1 
ATOM   2168 C CB  . LEU B 1 144 ? 14.929  2.281   -50.468 1.00 15.19 ? 144 LEU B CB  1 
ATOM   2169 C CG  . LEU B 1 144 ? 14.666  2.022   -51.956 1.00 15.11 ? 144 LEU B CG  1 
ATOM   2170 C CD1 . LEU B 1 144 ? 14.913  3.309   -52.810 1.00 16.54 ? 144 LEU B CD1 1 
ATOM   2171 C CD2 . LEU B 1 144 ? 15.627  0.898   -52.512 1.00 19.66 ? 144 LEU B CD2 1 
ATOM   2172 N N   . ALA B 1 145 ? 14.335  1.989   -47.387 1.00 16.15 ? 145 ALA B N   1 
ATOM   2173 C CA  . ALA B 1 145 ? 14.446  2.587   -46.092 1.00 16.26 ? 145 ALA B CA  1 
ATOM   2174 C C   . ALA B 1 145 ? 13.046  2.435   -45.441 1.00 17.72 ? 145 ALA B C   1 
ATOM   2175 O O   . ALA B 1 145 ? 12.022  2.377   -46.132 1.00 14.98 ? 145 ALA B O   1 
ATOM   2176 C CB  . ALA B 1 145 ? 14.822  4.021   -46.188 1.00 17.01 ? 145 ALA B CB  1 
ATOM   2177 N N   . CYS B 1 146 ? 13.075  2.287   -44.112 1.00 17.05 ? 146 CYS B N   1 
ATOM   2178 C CA  . CYS B 1 146 ? 11.907  2.102   -43.254 1.00 17.48 ? 146 CYS B CA  1 
ATOM   2179 C C   . CYS B 1 146 ? 12.223  2.622   -41.865 1.00 13.80 ? 146 CYS B C   1 
ATOM   2180 O O   . CYS B 1 146 ? 13.366  2.919   -41.498 1.00 14.08 ? 146 CYS B O   1 
ATOM   2181 C CB  . CYS B 1 146 ? 11.483  0.596   -43.177 1.00 16.90 ? 146 CYS B CB  1 
ATOM   2182 S SG  . CYS B 1 146 ? 12.799  -0.516  -42.661 1.00 27.15 ? 146 CYS B SG  1 
ATOM   2183 N N   . GLY B 1 147 ? 11.177  2.715   -41.077 1.00 11.81 ? 147 GLY B N   1 
ATOM   2184 C CA  . GLY B 1 147 ? 11.309  2.750   -39.673 1.00 9.27  ? 147 GLY B CA  1 
ATOM   2185 C C   . GLY B 1 147 ? 9.922   2.647   -39.074 1.00 10.54 ? 147 GLY B C   1 
ATOM   2186 O O   . GLY B 1 147 ? 8.929   2.791   -39.748 1.00 8.60  ? 147 GLY B O   1 
ATOM   2187 N N   . VAL B 1 148 ? 9.908   2.490   -37.773 1.00 11.46 ? 148 VAL B N   1 
ATOM   2188 C CA  . VAL B 1 148 ? 8.704   2.275   -36.987 1.00 13.48 ? 148 VAL B CA  1 
ATOM   2189 C C   . VAL B 1 148 ? 8.097   3.653   -36.689 1.00 13.62 ? 148 VAL B C   1 
ATOM   2190 O O   . VAL B 1 148 ? 8.826   4.612   -36.377 1.00 13.78 ? 148 VAL B O   1 
ATOM   2191 C CB  . VAL B 1 148 ? 9.056   1.576   -35.672 1.00 11.35 ? 148 VAL B CB  1 
ATOM   2192 C CG1 . VAL B 1 148 ? 7.826   1.121   -34.921 1.00 15.01 ? 148 VAL B CG1 1 
ATOM   2193 C CG2 . VAL B 1 148 ? 9.998   0.400   -35.966 1.00 8.15  ? 148 VAL B CG2 1 
ATOM   2194 N N   . ILE B 1 149 ? 6.766   3.709   -36.777 1.00 14.28 ? 149 ILE B N   1 
ATOM   2195 C CA  . ILE B 1 149 ? 6.089   4.956   -36.559 1.00 15.27 ? 149 ILE B CA  1 
ATOM   2196 C C   . ILE B 1 149 ? 5.899   5.057   -35.072 1.00 16.42 ? 149 ILE B C   1 
ATOM   2197 O O   . ILE B 1 149 ? 5.340   4.133   -34.426 1.00 16.80 ? 149 ILE B O   1 
ATOM   2198 C CB  . ILE B 1 149 ? 4.739   5.014   -37.304 1.00 15.49 ? 149 ILE B CB  1 
ATOM   2199 C CG1 . ILE B 1 149 ? 4.984   4.796   -38.800 1.00 15.18 ? 149 ILE B CG1 1 
ATOM   2200 C CG2 . ILE B 1 149 ? 3.976   6.421   -36.982 1.00 6.24  ? 149 ILE B CG2 1 
ATOM   2201 C CD1 . ILE B 1 149 ? 3.709   4.477   -39.590 1.00 16.49 ? 149 ILE B CD1 1 
ATOM   2202 N N   . GLY B 1 150 ? 6.391   6.160   -34.533 1.00 16.61 ? 150 GLY B N   1 
ATOM   2203 C CA  . GLY B 1 150 ? 6.417   6.333   -33.119 1.00 17.19 ? 150 GLY B CA  1 
ATOM   2204 C C   . GLY B 1 150 ? 5.671   7.552   -32.708 1.00 19.44 ? 150 GLY B C   1 
ATOM   2205 O O   . GLY B 1 150 ? 5.476   8.419   -33.520 1.00 20.62 ? 150 GLY B O   1 
ATOM   2206 N N   . ILE B 1 151 ? 5.252   7.579   -31.444 1.00 20.83 ? 151 ILE B N   1 
ATOM   2207 C CA  . ILE B 1 151 ? 4.675   8.713   -30.720 1.00 22.57 ? 151 ILE B CA  1 
ATOM   2208 C C   . ILE B 1 151 ? 5.683   9.903   -30.557 1.00 22.40 ? 151 ILE B C   1 
ATOM   2209 O O   . ILE B 1 151 ? 6.769   9.746   -30.008 1.00 22.78 ? 151 ILE B O   1 
ATOM   2210 C CB  . ILE B 1 151 ? 4.203   8.173   -29.326 1.00 23.06 ? 151 ILE B CB  1 
ATOM   2211 C CG1 . ILE B 1 151 ? 2.987   7.263   -29.511 1.00 22.46 ? 151 ILE B CG1 1 
ATOM   2212 C CG2 . ILE B 1 151 ? 3.909   9.278   -28.357 1.00 24.67 ? 151 ILE B CG2 1 
ATOM   2213 C CD1 . ILE B 1 151 ? 2.554   6.516   -28.285 1.00 21.44 ? 151 ILE B CD1 1 
ATOM   2214 N N   . ALA B 1 152 ? 5.297   11.072  -31.039 1.00 22.25 ? 152 ALA B N   1 
ATOM   2215 C CA  . ALA B 1 152 ? 6.132   12.289  -31.025 1.00 23.65 ? 152 ALA B CA  1 
ATOM   2216 C C   . ALA B 1 152 ? 5.519   13.328  -30.112 1.00 24.74 ? 152 ALA B C   1 
ATOM   2217 O O   . ALA B 1 152 ? 4.313   13.303  -29.890 1.00 24.48 ? 152 ALA B O   1 
ATOM   2218 C CB  . ALA B 1 152 ? 6.213   12.862  -32.455 1.00 22.53 ? 152 ALA B CB  1 
ATOM   2219 N N   . GLN B 1 153 ? 6.321   14.272  -29.613 1.00 27.18 ? 153 GLN B N   1 
ATOM   2220 C CA  . GLN B 1 153 ? 5.825   15.345  -28.722 1.00 29.20 ? 153 GLN B CA  1 
ATOM   2221 C C   . GLN B 1 153 ? 4.917   16.439  -29.341 1.00 31.24 ? 153 GLN B C   1 
ATOM   2222 O O   . GLN B 1 153 ? 5.142   17.000  -30.456 1.00 32.17 ? 153 GLN B O   1 
ATOM   2223 C CB  . GLN B 1 153 ? 6.976   16.014  -28.000 1.00 29.67 ? 153 GLN B CB  1 
ATOM   2224 C CG  . GLN B 1 153 ? 6.473   16.970  -26.949 1.00 31.34 ? 153 GLN B CG  1 
ATOM   2225 C CD  . GLN B 1 153 ? 7.464   17.294  -25.878 1.00 29.51 ? 153 GLN B CD  1 
ATOM   2226 O OE1 . GLN B 1 153 ? 8.643   16.982  -25.987 1.00 26.88 ? 153 GLN B OE1 1 
ATOM   2227 N NE2 . GLN B 1 153 ? 6.979   17.935  -24.817 1.00 30.28 ? 153 GLN B NE2 1 
ATOM   2228 O OXT . GLN B 1 153 ? 3.924   16.832  -28.693 1.00 31.58 ? 153 GLN B OXT 1 
ATOM   2229 N N   . ALA C 1 1   ? -16.132 -0.605  -32.192 1.00 39.11 ? 1   ALA C N   1 
ATOM   2230 C CA  . ALA C 1 1   ? -17.598 -0.662  -32.488 1.00 36.51 ? 1   ALA C CA  1 
ATOM   2231 C C   . ALA C 1 1   ? -18.131 -0.094  -31.203 1.00 34.53 ? 1   ALA C C   1 
ATOM   2232 O O   . ALA C 1 1   ? -18.804 -0.764  -30.389 1.00 33.88 ? 1   ALA C O   1 
ATOM   2233 C CB  . ALA C 1 1   ? -18.066 -2.119  -32.765 1.00 38.37 ? 1   ALA C CB  1 
ATOM   2234 N N   . THR C 1 2   ? -17.715 1.155   -31.001 1.00 31.89 ? 2   THR C N   1 
ATOM   2235 C CA  . THR C 1 2   ? -18.136 1.911   -29.873 1.00 29.14 ? 2   THR C CA  1 
ATOM   2236 C C   . THR C 1 2   ? -19.667 2.151   -30.249 1.00 27.92 ? 2   THR C C   1 
ATOM   2237 O O   . THR C 1 2   ? -20.079 2.309   -31.420 1.00 28.71 ? 2   THR C O   1 
ATOM   2238 C CB  . THR C 1 2   ? -16.962 2.989   -29.408 1.00 28.11 ? 2   THR C CB  1 
ATOM   2239 O OG1 . THR C 1 2   ? -17.058 3.435   -28.039 1.00 32.94 ? 2   THR C OG1 1 
ATOM   2240 C CG2 . THR C 1 2   ? -16.766 4.129   -30.268 1.00 26.70 ? 2   THR C CG2 1 
ATOM   2241 N N   . LYS C 1 3   ? -20.500 1.901   -29.270 1.00 25.66 ? 3   LYS C N   1 
ATOM   2242 C CA  . LYS C 1 3   ? -21.938 2.013   -29.317 1.00 25.41 ? 3   LYS C CA  1 
ATOM   2243 C C   . LYS C 1 3   ? -22.285 2.978   -28.170 1.00 23.52 ? 3   LYS C C   1 
ATOM   2244 O O   . LYS C 1 3   ? -21.637 2.972   -27.124 1.00 23.65 ? 3   LYS C O   1 
ATOM   2245 C CB  . LYS C 1 3   ? -22.618 0.654   -29.071 1.00 26.35 ? 3   LYS C CB  1 
ATOM   2246 C CG  . LYS C 1 3   ? -22.182 -0.484  -29.958 1.00 30.02 ? 3   LYS C CG  1 
ATOM   2247 C CD  . LYS C 1 3   ? -23.285 -1.530  -29.995 1.00 36.27 ? 3   LYS C CD  1 
ATOM   2248 C CE  . LYS C 1 3   ? -22.770 -2.919  -30.546 1.00 41.38 ? 3   LYS C CE  1 
ATOM   2249 N NZ  . LYS C 1 3   ? -23.901 -3.909  -30.886 1.00 36.00 ? 3   LYS C NZ  1 
ATOM   2250 N N   . ALA C 1 4   ? -23.260 3.844   -28.423 1.00 22.22 ? 4   ALA C N   1 
ATOM   2251 C CA  . ALA C 1 4   ? -23.856 4.705   -27.451 1.00 19.61 ? 4   ALA C CA  1 
ATOM   2252 C C   . ALA C 1 4   ? -25.415 4.729   -27.624 1.00 19.20 ? 4   ALA C C   1 
ATOM   2253 O O   . ALA C 1 4   ? -25.991 4.300   -28.636 1.00 21.16 ? 4   ALA C O   1 
ATOM   2254 C CB  . ALA C 1 4   ? -23.203 6.104   -27.469 1.00 19.44 ? 4   ALA C CB  1 
ATOM   2255 N N   . VAL C 1 5   ? -26.109 5.142   -26.596 1.00 19.06 ? 5   VAL C N   1 
ATOM   2256 C CA  . VAL C 1 5   ? -27.569 5.171   -26.555 1.00 18.05 ? 5   VAL C CA  1 
ATOM   2257 C C   . VAL C 1 5   ? -28.007 6.455   -25.767 1.00 18.39 ? 5   VAL C C   1 
ATOM   2258 O O   . VAL C 1 5   ? -27.285 6.990   -24.934 1.00 16.43 ? 5   VAL C O   1 
ATOM   2259 C CB  . VAL C 1 5   ? -28.124 3.934   -25.858 1.00 18.93 ? 5   VAL C CB  1 
ATOM   2260 C CG1 . VAL C 1 5   ? -27.502 3.846   -24.478 1.00 17.44 ? 5   VAL C CG1 1 
ATOM   2261 C CG2 . VAL C 1 5   ? -29.774 3.931   -25.780 1.00 18.09 ? 5   VAL C CG2 1 
ATOM   2262 N N   . CYS C 1 6   ? -29.207 6.931   -26.067 1.00 18.03 ? 6   CYS C N   1 
ATOM   2263 C CA  . CYS C 1 6   ? -29.760 8.064   -25.439 1.00 17.62 ? 6   CYS C CA  1 
ATOM   2264 C C   . CYS C 1 6   ? -31.270 7.788   -25.366 1.00 18.44 ? 6   CYS C C   1 
ATOM   2265 O O   . CYS C 1 6   ? -31.884 7.491   -26.373 1.00 19.60 ? 6   CYS C O   1 
ATOM   2266 C CB  . CYS C 1 6   ? -29.446 9.257   -26.293 1.00 16.27 ? 6   CYS C CB  1 
ATOM   2267 S SG  . CYS C 1 6   ? -30.221 10.651  -25.708 1.00 18.26 ? 6   CYS C SG  1 
ATOM   2268 N N   . VAL C 1 7   ? -31.843 7.834   -24.156 1.00 19.03 ? 7   VAL C N   1 
ATOM   2269 C CA  . VAL C 1 7   ? -33.290 7.796   -23.905 1.00 18.69 ? 7   VAL C CA  1 
ATOM   2270 C C   . VAL C 1 7   ? -33.757 9.271   -23.724 1.00 19.56 ? 7   VAL C C   1 
ATOM   2271 O O   . VAL C 1 7   ? -33.337 9.904   -22.771 1.00 21.82 ? 7   VAL C O   1 
ATOM   2272 C CB  . VAL C 1 7   ? -33.566 6.948   -22.640 1.00 19.38 ? 7   VAL C CB  1 
ATOM   2273 C CG1 . VAL C 1 7   ? -35.075 6.973   -22.211 1.00 20.81 ? 7   VAL C CG1 1 
ATOM   2274 C CG2 . VAL C 1 7   ? -33.076 5.495   -22.816 1.00 18.05 ? 7   VAL C CG2 1 
ATOM   2275 N N   . LEU C 1 8   ? -34.581 9.817   -24.644 1.00 19.26 ? 8   LEU C N   1 
ATOM   2276 C CA  . LEU C 1 8   ? -35.130 11.189  -24.564 1.00 19.50 ? 8   LEU C CA  1 
ATOM   2277 C C   . LEU C 1 8   ? -36.404 11.237  -23.749 1.00 19.37 ? 8   LEU C C   1 
ATOM   2278 O O   . LEU C 1 8   ? -37.247 10.397  -23.904 1.00 19.60 ? 8   LEU C O   1 
ATOM   2279 C CB  . LEU C 1 8   ? -35.486 11.812  -25.959 1.00 19.67 ? 8   LEU C CB  1 
ATOM   2280 C CG  . LEU C 1 8   ? -34.584 12.497  -27.006 1.00 21.27 ? 8   LEU C CG  1 
ATOM   2281 C CD1 . LEU C 1 8   ? -33.287 12.578  -26.480 1.00 13.66 ? 8   LEU C CD1 1 
ATOM   2282 C CD2 . LEU C 1 8   ? -34.547 11.723  -28.332 1.00 22.90 ? 8   LEU C CD2 1 
ATOM   2283 N N   . LYS C 1 9   ? -36.503 12.205  -22.850 1.00 20.36 ? 9   LYS C N   1 
ATOM   2284 C CA  . LYS C 1 9   ? -37.659 12.441  -22.024 1.00 22.03 ? 9   LYS C CA  1 
ATOM   2285 C C   . LYS C 1 9   ? -37.731 13.955  -21.967 1.00 21.38 ? 9   LYS C C   1 
ATOM   2286 O O   . LYS C 1 9   ? -36.699 14.637  -22.093 1.00 18.89 ? 9   LYS C O   1 
ATOM   2287 C CB  . LYS C 1 9   ? -37.429 11.903  -20.581 1.00 22.76 ? 9   LYS C CB  1 
ATOM   2288 C CG  . LYS C 1 9   ? -37.772 10.384  -20.472 1.00 27.81 ? 9   LYS C CG  1 
ATOM   2289 C CD  . LYS C 1 9   ? -38.126 10.005  -19.005 1.00 27.42 ? 9   LYS C CD  1 
ATOM   2290 C CE  . LYS C 1 9   ? -38.152 8.467   -18.770 1.00 32.26 ? 9   LYS C CE  1 
ATOM   2291 N NZ  . LYS C 1 9   ? -37.060 7.743   -19.494 1.00 37.17 ? 9   LYS C NZ  1 
ATOM   2292 N N   . GLY C 1 10  ? -38.931 14.475  -21.742 1.00 21.68 ? 10  GLY C N   1 
ATOM   2293 C CA  . GLY C 1 10  ? -39.137 15.886  -21.523 1.00 22.08 ? 10  GLY C CA  1 
ATOM   2294 C C   . GLY C 1 10  ? -40.232 16.159  -20.492 1.00 23.93 ? 10  GLY C C   1 
ATOM   2295 O O   . GLY C 1 10  ? -40.576 15.296  -19.675 1.00 23.03 ? 10  GLY C O   1 
ATOM   2296 N N   . ASP C 1 11  ? -40.737 17.386  -20.519 1.00 24.96 ? 11  ASP C N   1 
ATOM   2297 C CA  . ASP C 1 11  ? -41.873 17.816  -19.702 1.00 27.88 ? 11  ASP C CA  1 
ATOM   2298 C C   . ASP C 1 11  ? -43.233 17.432  -20.346 1.00 28.26 ? 11  ASP C C   1 
ATOM   2299 O O   . ASP C 1 11  ? -44.267 17.353  -19.652 1.00 29.30 ? 11  ASP C O   1 
ATOM   2300 C CB  . ASP C 1 11  ? -41.771 19.325  -19.532 1.00 29.12 ? 11  ASP C CB  1 
ATOM   2301 C CG  . ASP C 1 11  ? -40.653 19.728  -18.573 1.00 35.42 ? 11  ASP C CG  1 
ATOM   2302 O OD1 . ASP C 1 11  ? -40.204 18.893  -17.746 1.00 36.78 ? 11  ASP C OD1 1 
ATOM   2303 O OD2 . ASP C 1 11  ? -40.237 20.911  -18.615 1.00 41.23 ? 11  ASP C OD2 1 
ATOM   2304 N N   . GLY C 1 12  ? -43.218 17.212  -21.669 1.00 26.99 ? 12  GLY C N   1 
ATOM   2305 C CA  . GLY C 1 12  ? -44.402 16.848  -22.426 1.00 26.01 ? 12  GLY C CA  1 
ATOM   2306 C C   . GLY C 1 12  ? -44.496 15.378  -22.717 1.00 24.79 ? 12  GLY C C   1 
ATOM   2307 O O   . GLY C 1 12  ? -43.897 14.603  -22.004 1.00 25.06 ? 12  GLY C O   1 
ATOM   2308 N N   . PRO C 1 13  ? -45.281 14.959  -23.758 1.00 25.37 ? 13  PRO C N   1 
ATOM   2309 C CA  . PRO C 1 13  ? -45.324 13.482  -24.010 1.00 25.91 ? 13  PRO C CA  1 
ATOM   2310 C C   . PRO C 1 13  ? -44.170 12.981  -24.898 1.00 27.01 ? 13  PRO C C   1 
ATOM   2311 O O   . PRO C 1 13  ? -44.170 11.794  -25.305 1.00 26.88 ? 13  PRO C O   1 
ATOM   2312 C CB  . PRO C 1 13  ? -46.622 13.312  -24.782 1.00 25.07 ? 13  PRO C CB  1 
ATOM   2313 C CG  . PRO C 1 13  ? -46.660 14.529  -25.620 1.00 26.09 ? 13  PRO C CG  1 
ATOM   2314 C CD  . PRO C 1 13  ? -46.118 15.673  -24.738 1.00 24.45 ? 13  PRO C CD  1 
ATOM   2315 N N   . VAL C 1 14  ? -43.210 13.851  -25.231 1.00 27.17 ? 14  VAL C N   1 
ATOM   2316 C CA  . VAL C 1 14  ? -42.175 13.399  -26.206 1.00 28.15 ? 14  VAL C CA  1 
ATOM   2317 C C   . VAL C 1 14  ? -41.227 12.470  -25.534 1.00 28.19 ? 14  VAL C C   1 
ATOM   2318 O O   . VAL C 1 14  ? -40.614 12.820  -24.530 1.00 27.67 ? 14  VAL C O   1 
ATOM   2319 C CB  . VAL C 1 14  ? -41.422 14.581  -26.912 1.00 27.72 ? 14  VAL C CB  1 
ATOM   2320 C CG1 . VAL C 1 14  ? -40.277 14.077  -27.819 1.00 27.43 ? 14  VAL C CG1 1 
ATOM   2321 C CG2 . VAL C 1 14  ? -42.397 15.409  -27.718 1.00 29.63 ? 14  VAL C CG2 1 
ATOM   2322 N N   . GLN C 1 15  ? -41.146 11.261  -26.070 1.00 29.84 ? 15  GLN C N   1 
ATOM   2323 C CA  . GLN C 1 15  ? -40.184 10.283  -25.623 1.00 29.92 ? 15  GLN C CA  1 
ATOM   2324 C C   . GLN C 1 15  ? -39.575 9.433   -26.760 1.00 29.07 ? 15  GLN C C   1 
ATOM   2325 O O   . GLN C 1 15  ? -40.184 9.254   -27.813 1.00 28.19 ? 15  GLN C O   1 
ATOM   2326 C CB  . GLN C 1 15  ? -40.804 9.419   -24.541 1.00 32.53 ? 15  GLN C CB  1 
ATOM   2327 C CG  . GLN C 1 15  ? -41.784 8.361   -25.001 1.00 35.50 ? 15  GLN C CG  1 
ATOM   2328 C CD  . GLN C 1 15  ? -42.664 7.893   -23.868 1.00 42.54 ? 15  GLN C CD  1 
ATOM   2329 O OE1 . GLN C 1 15  ? -42.398 6.852   -23.253 1.00 46.63 ? 15  GLN C OE1 1 
ATOM   2330 N NE2 . GLN C 1 15  ? -43.705 8.663   -23.566 1.00 39.74 ? 15  GLN C NE2 1 
ATOM   2331 N N   . GLY C 1 16  ? -38.357 8.946   -26.560 1.00 27.67 ? 16  GLY C N   1 
ATOM   2332 C CA  . GLY C 1 16  ? -37.750 8.029   -27.538 1.00 26.79 ? 16  GLY C CA  1 
ATOM   2333 C C   . GLY C 1 16  ? -36.453 7.382   -27.117 1.00 24.40 ? 16  GLY C C   1 
ATOM   2334 O O   . GLY C 1 16  ? -35.937 7.686   -26.051 1.00 24.54 ? 16  GLY C O   1 
ATOM   2335 N N   . ILE C 1 17  ? -35.940 6.506   -27.982 1.00 24.69 ? 17  ILE C N   1 
ATOM   2336 C CA  . ILE C 1 17  ? -34.665 5.777   -27.799 1.00 23.61 ? 17  ILE C CA  1 
ATOM   2337 C C   . ILE C 1 17  ? -33.810 5.957   -29.026 1.00 22.49 ? 17  ILE C C   1 
ATOM   2338 O O   . ILE C 1 17  ? -34.276 5.638   -30.071 1.00 23.29 ? 17  ILE C O   1 
ATOM   2339 C CB  . ILE C 1 17  ? -34.910 4.252   -27.670 1.00 24.78 ? 17  ILE C CB  1 
ATOM   2340 C CG1 . ILE C 1 17  ? -36.124 3.979   -26.710 1.00 27.53 ? 17  ILE C CG1 1 
ATOM   2341 C CG2 . ILE C 1 17  ? -33.604 3.503   -27.388 1.00 22.31 ? 17  ILE C CG2 1 
ATOM   2342 C CD1 . ILE C 1 17  ? -35.951 2.988   -25.545 1.00 19.96 ? 17  ILE C CD1 1 
ATOM   2343 N N   . ILE C 1 18  ? -32.564 6.435   -28.920 1.00 20.65 ? 18  ILE C N   1 
ATOM   2344 C CA  . ILE C 1 18  ? -31.734 6.706   -30.109 1.00 17.53 ? 18  ILE C CA  1 
ATOM   2345 C C   . ILE C 1 18  ? -30.379 6.007   -29.968 1.00 17.91 ? 18  ILE C C   1 
ATOM   2346 O O   . ILE C 1 18  ? -29.703 6.103   -28.936 1.00 15.01 ? 18  ILE C O   1 
ATOM   2347 C CB  . ILE C 1 18  ? -31.489 8.283   -30.322 1.00 19.98 ? 18  ILE C CB  1 
ATOM   2348 C CG1 . ILE C 1 18  ? -32.787 9.067   -30.559 1.00 13.56 ? 18  ILE C CG1 1 
ATOM   2349 C CG2 . ILE C 1 18  ? -30.481 8.574   -31.515 1.00 19.68 ? 18  ILE C CG2 1 
ATOM   2350 C CD1 . ILE C 1 18  ? -33.611 8.620   -31.831 1.00 10.40 ? 18  ILE C CD1 1 
ATOM   2351 N N   . ASN C 1 19  ? -30.037 5.215   -30.977 1.00 17.70 ? 19  ASN C N   1 
ATOM   2352 C CA  . ASN C 1 19  ? -28.878 4.387   -30.955 1.00 18.44 ? 19  ASN C CA  1 
ATOM   2353 C C   . ASN C 1 19  ? -27.818 5.066   -31.762 1.00 18.41 ? 19  ASN C C   1 
ATOM   2354 O O   . ASN C 1 19  ? -28.128 5.769   -32.698 1.00 18.24 ? 19  ASN C O   1 
ATOM   2355 C CB  . ASN C 1 19  ? -29.162 2.970   -31.466 1.00 17.69 ? 19  ASN C CB  1 
ATOM   2356 C CG  . ASN C 1 19  ? -30.093 2.228   -30.569 1.00 18.94 ? 19  ASN C CG  1 
ATOM   2357 O OD1 . ASN C 1 19  ? -29.762 1.957   -29.401 1.00 18.50 ? 19  ASN C OD1 1 
ATOM   2358 N ND2 . ASN C 1 19  ? -31.238 1.816   -31.115 1.00 16.36 ? 19  ASN C ND2 1 
ATOM   2359 N N   . PHE C 1 20  ? -26.572 4.888   -31.354 1.00 18.82 ? 20  PHE C N   1 
ATOM   2360 C CA  . PHE C 1 20  ? -25.426 5.413   -32.099 1.00 19.96 ? 20  PHE C CA  1 
ATOM   2361 C C   . PHE C 1 20  ? -24.453 4.288   -32.357 1.00 21.38 ? 20  PHE C C   1 
ATOM   2362 O O   . PHE C 1 20  ? -24.260 3.443   -31.495 1.00 21.51 ? 20  PHE C O   1 
ATOM   2363 C CB  . PHE C 1 20  ? -24.721 6.505   -31.283 1.00 19.14 ? 20  PHE C CB  1 
ATOM   2364 C CG  . PHE C 1 20  ? -25.575 7.745   -30.970 1.00 18.12 ? 20  PHE C CG  1 
ATOM   2365 C CD1 . PHE C 1 20  ? -26.428 7.774   -29.855 1.00 20.93 ? 20  PHE C CD1 1 
ATOM   2366 C CD2 . PHE C 1 20  ? -25.458 8.886   -31.729 1.00 20.10 ? 20  PHE C CD2 1 
ATOM   2367 C CE1 . PHE C 1 20  ? -27.205 8.892   -29.560 1.00 14.84 ? 20  PHE C CE1 1 
ATOM   2368 C CE2 . PHE C 1 20  ? -26.214 10.080  -31.412 1.00 19.80 ? 20  PHE C CE2 1 
ATOM   2369 C CZ  . PHE C 1 20  ? -27.070 10.053  -30.300 1.00 16.73 ? 20  PHE C CZ  1 
ATOM   2370 N N   . GLU C 1 21  ? -23.790 4.280   -33.499 1.00 23.29 ? 21  GLU C N   1 
ATOM   2371 C CA  . GLU C 1 21  ? -22.773 3.279   -33.731 1.00 25.97 ? 21  GLU C CA  1 
ATOM   2372 C C   . GLU C 1 21  ? -21.602 3.802   -34.606 1.00 24.67 ? 21  GLU C C   1 
ATOM   2373 O O   . GLU C 1 21  ? -21.823 4.381   -35.626 1.00 22.70 ? 21  GLU C O   1 
ATOM   2374 C CB  . GLU C 1 21  ? -23.378 1.995   -34.353 1.00 25.07 ? 21  GLU C CB  1 
ATOM   2375 C CG  . GLU C 1 21  ? -22.798 0.744   -33.651 1.00 31.72 ? 21  GLU C CG  1 
ATOM   2376 C CD  . GLU C 1 21  ? -22.875 -0.567  -34.425 1.00 34.16 ? 21  GLU C CD  1 
ATOM   2377 O OE1 . GLU C 1 21  ? -23.454 -0.557  -35.553 1.00 41.09 ? 21  GLU C OE1 1 
ATOM   2378 O OE2 . GLU C 1 21  ? -22.351 -1.606  -33.878 1.00 40.60 ? 21  GLU C OE2 1 
ATOM   2379 N N   . GLN C 1 22  ? -20.366 3.563   -34.172 1.00 25.33 ? 22  GLN C N   1 
ATOM   2380 C CA  . GLN C 1 22  ? -19.180 3.903   -34.950 1.00 27.11 ? 22  GLN C CA  1 
ATOM   2381 C C   . GLN C 1 22  ? -18.284 2.701   -34.933 1.00 28.28 ? 22  GLN C C   1 
ATOM   2382 O O   . GLN C 1 22  ? -17.609 2.465   -33.935 1.00 28.69 ? 22  GLN C O   1 
ATOM   2383 C CB  . GLN C 1 22  ? -18.438 5.078   -34.310 1.00 25.88 ? 22  GLN C CB  1 
ATOM   2384 C CG  . GLN C 1 22  ? -17.600 5.929   -35.212 1.00 22.77 ? 22  GLN C CG  1 
ATOM   2385 C CD  . GLN C 1 22  ? -16.896 6.981   -34.413 1.00 17.13 ? 22  GLN C CD  1 
ATOM   2386 O OE1 . GLN C 1 22  ? -16.917 6.906   -33.209 1.00 20.01 ? 22  GLN C OE1 1 
ATOM   2387 N NE2 . GLN C 1 22  ? -16.272 7.948   -35.059 1.00 12.74 ? 22  GLN C NE2 1 
ATOM   2388 N N   . LYS C 1 23  ? -18.276 1.959   -36.035 1.00 31.00 ? 23  LYS C N   1 
ATOM   2389 C CA  . LYS C 1 23  ? -17.388 0.786   -36.233 1.00 32.56 ? 23  LYS C CA  1 
ATOM   2390 C C   . LYS C 1 23  ? -15.894 1.117   -36.410 1.00 31.25 ? 23  LYS C C   1 
ATOM   2391 O O   . LYS C 1 23  ? -15.040 0.319   -36.049 1.00 31.04 ? 23  LYS C O   1 
ATOM   2392 C CB  . LYS C 1 23  ? -17.894 -0.113  -37.387 1.00 34.20 ? 23  LYS C CB  1 
ATOM   2393 C CG  . LYS C 1 23  ? -18.980 -1.153  -36.943 1.00 37.19 ? 23  LYS C CG  1 
ATOM   2394 C CD  . LYS C 1 23  ? -18.307 -2.383  -36.239 1.00 41.91 ? 23  LYS C CD  1 
ATOM   2395 C CE  . LYS C 1 23  ? -19.341 -3.487  -35.905 1.00 42.73 ? 23  LYS C CE  1 
ATOM   2396 N NZ  . LYS C 1 23  ? -18.798 -4.908  -35.906 1.00 43.17 ? 23  LYS C NZ  1 
ATOM   2397 N N   . GLU C 1 24  ? -15.575 2.295   -36.954 1.00 31.37 ? 24  GLU C N   1 
ATOM   2398 C CA  . GLU C 1 24  ? -14.174 2.719   -37.018 1.00 30.16 ? 24  GLU C CA  1 
ATOM   2399 C C   . GLU C 1 24  ? -13.994 4.126   -36.418 1.00 27.97 ? 24  GLU C C   1 
ATOM   2400 O O   . GLU C 1 24  ? -14.705 5.026   -36.751 1.00 27.29 ? 24  GLU C O   1 
ATOM   2401 C CB  . GLU C 1 24  ? -13.547 2.594   -38.440 1.00 31.92 ? 24  GLU C CB  1 
ATOM   2402 C CG  . GLU C 1 24  ? -14.403 2.969   -39.641 1.00 37.86 ? 24  GLU C CG  1 
ATOM   2403 C CD  . GLU C 1 24  ? -14.757 1.788   -40.575 1.00 47.85 ? 24  GLU C CD  1 
ATOM   2404 O OE1 . GLU C 1 24  ? -15.899 1.832   -41.141 1.00 51.11 ? 24  GLU C OE1 1 
ATOM   2405 O OE2 . GLU C 1 24  ? -13.909 0.847   -40.794 1.00 50.58 ? 24  GLU C OE2 1 
ATOM   2406 N N   . SER C 1 25  ? -13.039 4.265   -35.519 1.00 26.30 ? 25  SER C N   1 
ATOM   2407 C CA  . SER C 1 25  ? -12.797 5.492   -34.753 1.00 25.40 ? 25  SER C CA  1 
ATOM   2408 C C   . SER C 1 25  ? -12.672 6.699   -35.592 1.00 24.72 ? 25  SER C C   1 
ATOM   2409 O O   . SER C 1 25  ? -12.918 7.764   -35.098 1.00 25.48 ? 25  SER C O   1 
ATOM   2410 C CB  . SER C 1 25  ? -11.547 5.342   -33.896 1.00 24.89 ? 25  SER C CB  1 
ATOM   2411 O OG  . SER C 1 25  ? -10.401 5.297   -34.717 1.00 25.64 ? 25  SER C OG  1 
ATOM   2412 N N   . ASN C 1 26  ? -12.306 6.531   -36.876 1.00 26.28 ? 26  ASN C N   1 
ATOM   2413 C CA  . ASN C 1 26  ? -12.236 7.629   -37.880 1.00 25.92 ? 26  ASN C CA  1 
ATOM   2414 C C   . ASN C 1 26  ? -13.330 7.575   -38.944 1.00 25.27 ? 26  ASN C C   1 
ATOM   2415 O O   . ASN C 1 26  ? -13.217 8.111   -40.038 1.00 25.32 ? 26  ASN C O   1 
ATOM   2416 C CB  . ASN C 1 26  ? -10.838 7.787   -38.548 1.00 26.26 ? 26  ASN C CB  1 
ATOM   2417 C CG  . ASN C 1 26  ? -10.473 6.648   -39.449 1.00 24.61 ? 26  ASN C CG  1 
ATOM   2418 O OD1 . ASN C 1 26  ? -11.087 5.621   -39.426 1.00 31.04 ? 26  ASN C OD1 1 
ATOM   2419 N ND2 . ASN C 1 26  ? -9.464  6.839   -40.260 1.00 23.30 ? 26  ASN C ND2 1 
ATOM   2420 N N   . GLY C 1 27  ? -14.409 6.941   -38.605 1.00 24.52 ? 27  GLY C N   1 
ATOM   2421 C CA  . GLY C 1 27  ? -15.463 6.778   -39.561 1.00 24.93 ? 27  GLY C CA  1 
ATOM   2422 C C   . GLY C 1 27  ? -16.754 7.414   -39.082 1.00 24.72 ? 27  GLY C C   1 
ATOM   2423 O O   . GLY C 1 27  ? -16.829 7.965   -37.956 1.00 25.09 ? 27  GLY C O   1 
ATOM   2424 N N   . PRO C 1 28  ? -17.797 7.304   -39.915 1.00 25.14 ? 28  PRO C N   1 
ATOM   2425 C CA  . PRO C 1 28  ? -19.082 7.863   -39.530 1.00 23.98 ? 28  PRO C CA  1 
ATOM   2426 C C   . PRO C 1 28  ? -19.755 7.144   -38.367 1.00 22.95 ? 28  PRO C C   1 
ATOM   2427 O O   . PRO C 1 28  ? -19.449 6.021   -38.054 1.00 23.93 ? 28  PRO C O   1 
ATOM   2428 C CB  . PRO C 1 28  ? -19.934 7.761   -40.826 1.00 23.35 ? 28  PRO C CB  1 
ATOM   2429 C CG  . PRO C 1 28  ? -19.354 6.630   -41.595 1.00 27.31 ? 28  PRO C CG  1 
ATOM   2430 C CD  . PRO C 1 28  ? -17.832 6.672   -41.261 1.00 25.10 ? 28  PRO C CD  1 
ATOM   2431 N N   . VAL C 1 29  ? -20.737 7.825   -37.781 1.00 23.36 ? 29  VAL C N   1 
ATOM   2432 C CA  . VAL C 1 29  ? -21.582 7.321   -36.742 1.00 20.96 ? 29  VAL C CA  1 
ATOM   2433 C C   . VAL C 1 29  ? -22.972 7.097   -37.386 1.00 22.18 ? 29  VAL C C   1 
ATOM   2434 O O   . VAL C 1 29  ? -23.479 7.943   -38.048 1.00 21.46 ? 29  VAL C O   1 
ATOM   2435 C CB  . VAL C 1 29  ? -21.658 8.320   -35.570 1.00 21.21 ? 29  VAL C CB  1 
ATOM   2436 C CG1 . VAL C 1 29  ? -22.569 7.770   -34.450 1.00 16.87 ? 29  VAL C CG1 1 
ATOM   2437 C CG2 . VAL C 1 29  ? -20.258 8.659   -35.063 1.00 17.01 ? 29  VAL C CG2 1 
ATOM   2438 N N   . LYS C 1 30  ? -23.536 5.909   -37.235 1.00 22.77 ? 30  LYS C N   1 
ATOM   2439 C CA  . LYS C 1 30  ? -24.934 5.692   -37.535 1.00 23.95 ? 30  LYS C CA  1 
ATOM   2440 C C   . LYS C 1 30  ? -25.743 6.094   -36.326 1.00 22.95 ? 30  LYS C C   1 
ATOM   2441 O O   . LYS C 1 30  ? -25.440 5.699   -35.213 1.00 23.50 ? 30  LYS C O   1 
ATOM   2442 C CB  . LYS C 1 30  ? -25.201 4.210   -37.849 1.00 25.37 ? 30  LYS C CB  1 
ATOM   2443 C CG  . LYS C 1 30  ? -24.289 3.653   -38.960 1.00 29.69 ? 30  LYS C CG  1 
ATOM   2444 C CD  . LYS C 1 30  ? -24.732 2.280   -39.331 1.00 35.61 ? 30  LYS C CD  1 
ATOM   2445 C CE  . LYS C 1 30  ? -24.425 2.008   -40.812 1.00 39.29 ? 30  LYS C CE  1 
ATOM   2446 N NZ  . LYS C 1 30  ? -24.549 0.540   -41.029 1.00 43.31 ? 30  LYS C NZ  1 
ATOM   2447 N N   . VAL C 1 31  ? -26.766 6.891   -36.549 1.00 22.36 ? 31  VAL C N   1 
ATOM   2448 C CA  . VAL C 1 31  ? -27.784 7.148   -35.533 1.00 22.32 ? 31  VAL C CA  1 
ATOM   2449 C C   . VAL C 1 31  ? -29.149 6.699   -36.002 1.00 22.07 ? 31  VAL C C   1 
ATOM   2450 O O   . VAL C 1 31  ? -29.590 6.927   -37.150 1.00 21.63 ? 31  VAL C O   1 
ATOM   2451 C CB  . VAL C 1 31  ? -27.766 8.641   -34.914 1.00 23.46 ? 31  VAL C CB  1 
ATOM   2452 C CG1 . VAL C 1 31  ? -26.998 9.596   -35.780 1.00 20.98 ? 31  VAL C CG1 1 
ATOM   2453 C CG2 . VAL C 1 31  ? -29.170 9.154   -34.505 1.00 22.00 ? 31  VAL C CG2 1 
ATOM   2454 N N   . TRP C 1 32  ? -29.818 6.009   -35.118 1.00 20.45 ? 32  TRP C N   1 
ATOM   2455 C CA  . TRP C 1 32  ? -31.051 5.460   -35.536 1.00 21.26 ? 32  TRP C CA  1 
ATOM   2456 C C   . TRP C 1 32  ? -31.868 5.243   -34.313 1.00 20.12 ? 32  TRP C C   1 
ATOM   2457 O O   . TRP C 1 32  ? -31.296 5.025   -33.267 1.00 20.51 ? 32  TRP C O   1 
ATOM   2458 C CB  . TRP C 1 32  ? -30.805 4.128   -36.292 1.00 21.80 ? 32  TRP C CB  1 
ATOM   2459 C CG  . TRP C 1 32  ? -30.573 2.948   -35.461 1.00 21.21 ? 32  TRP C CG  1 
ATOM   2460 C CD1 . TRP C 1 32  ? -31.504 2.041   -35.023 1.00 25.14 ? 32  TRP C CD1 1 
ATOM   2461 C CD2 . TRP C 1 32  ? -29.291 2.461   -35.023 1.00 20.76 ? 32  TRP C CD2 1 
ATOM   2462 N NE1 . TRP C 1 32  ? -30.870 1.023   -34.312 1.00 21.24 ? 32  TRP C NE1 1 
ATOM   2463 C CE2 . TRP C 1 32  ? -29.515 1.269   -34.309 1.00 20.09 ? 32  TRP C CE2 1 
ATOM   2464 C CE3 . TRP C 1 32  ? -27.966 2.921   -35.192 1.00 21.38 ? 32  TRP C CE3 1 
ATOM   2465 C CZ2 . TRP C 1 32  ? -28.481 0.554   -33.737 1.00 23.24 ? 32  TRP C CZ2 1 
ATOM   2466 C CZ3 . TRP C 1 32  ? -26.963 2.247   -34.627 1.00 22.84 ? 32  TRP C CZ3 1 
ATOM   2467 C CH2 . TRP C 1 32  ? -27.208 1.053   -33.892 1.00 24.35 ? 32  TRP C CH2 1 
ATOM   2468 N N   . GLY C 1 33  ? -33.188 5.304   -34.453 1.00 20.69 ? 33  GLY C N   1 
ATOM   2469 C CA  . GLY C 1 33  ? -34.151 4.814   -33.427 1.00 20.67 ? 33  GLY C CA  1 
ATOM   2470 C C   . GLY C 1 33  ? -35.519 5.329   -33.719 1.00 21.96 ? 33  GLY C C   1 
ATOM   2471 O O   . GLY C 1 33  ? -35.866 5.558   -34.864 1.00 23.29 ? 33  GLY C O   1 
ATOM   2472 N N   . SER C 1 34  ? -36.310 5.555   -32.686 1.00 24.50 ? 34  SER C N   1 
ATOM   2473 C CA  . SER C 1 34  ? -37.691 6.041   -32.831 1.00 26.11 ? 34  SER C CA  1 
ATOM   2474 C C   . SER C 1 34  ? -38.057 7.014   -31.707 1.00 26.75 ? 34  SER C C   1 
ATOM   2475 O O   . SER C 1 34  ? -37.773 6.740   -30.531 1.00 28.41 ? 34  SER C O   1 
ATOM   2476 C CB  . SER C 1 34  ? -38.616 4.854   -32.829 1.00 25.50 ? 34  SER C CB  1 
ATOM   2477 O OG  . SER C 1 34  ? -39.860 5.146   -32.208 1.00 32.38 ? 34  SER C OG  1 
ATOM   2478 N N   . ILE C 1 35  ? -38.656 8.154   -32.060 1.00 27.01 ? 35  ILE C N   1 
ATOM   2479 C CA  . ILE C 1 35  ? -39.223 9.137   -31.104 1.00 26.26 ? 35  ILE C CA  1 
ATOM   2480 C C   . ILE C 1 35  ? -40.751 9.225   -31.285 1.00 27.22 ? 35  ILE C C   1 
ATOM   2481 O O   . ILE C 1 35  ? -41.190 9.323   -32.424 1.00 28.09 ? 35  ILE C O   1 
ATOM   2482 C CB  . ILE C 1 35  ? -38.570 10.520  -31.323 1.00 26.01 ? 35  ILE C CB  1 
ATOM   2483 C CG1 . ILE C 1 35  ? -37.032 10.357  -31.504 1.00 26.06 ? 35  ILE C CG1 1 
ATOM   2484 C CG2 . ILE C 1 35  ? -38.964 11.491  -30.245 1.00 24.02 ? 35  ILE C CG2 1 
ATOM   2485 C CD1 . ILE C 1 35  ? -36.333 11.586  -31.764 1.00 21.56 ? 35  ILE C CD1 1 
ATOM   2486 N N   . LYS C 1 36  ? -41.564 9.164   -30.209 1.00 27.92 ? 36  LYS C N   1 
ATOM   2487 C CA  . LYS C 1 36  ? -43.041 9.503   -30.271 1.00 28.00 ? 36  LYS C CA  1 
ATOM   2488 C C   . LYS C 1 36  ? -43.494 10.743  -29.455 1.00 28.16 ? 36  LYS C C   1 
ATOM   2489 O O   . LYS C 1 36  ? -42.715 11.285  -28.710 1.00 28.31 ? 36  LYS C O   1 
ATOM   2490 C CB  . LYS C 1 36  ? -43.927 8.300   -29.934 1.00 29.49 ? 36  LYS C CB  1 
ATOM   2491 C CG  . LYS C 1 36  ? -43.655 7.548   -28.610 1.00 30.74 ? 36  LYS C CG  1 
ATOM   2492 C CD  . LYS C 1 36  ? -44.975 6.907   -28.142 1.00 35.81 ? 36  LYS C CD  1 
ATOM   2493 C CE  . LYS C 1 36  ? -44.948 6.349   -26.706 1.00 35.58 ? 36  LYS C CE  1 
ATOM   2494 N NZ  . LYS C 1 36  ? -44.653 4.862   -26.672 1.00 36.77 ? 36  LYS C NZ  1 
ATOM   2495 N N   . GLY C 1 37  ? -44.758 11.180  -29.594 1.00 28.01 ? 37  GLY C N   1 
ATOM   2496 C CA  . GLY C 1 37  ? -45.307 12.378  -28.891 1.00 26.13 ? 37  GLY C CA  1 
ATOM   2497 C C   . GLY C 1 37  ? -45.082 13.672  -29.632 1.00 25.44 ? 37  GLY C C   1 
ATOM   2498 O O   . GLY C 1 37  ? -45.307 14.763  -29.092 1.00 25.18 ? 37  GLY C O   1 
ATOM   2499 N N   . LEU C 1 38  ? -44.622 13.574  -30.882 1.00 25.24 ? 38  LEU C N   1 
ATOM   2500 C CA  . LEU C 1 38  ? -44.327 14.771  -31.687 1.00 25.31 ? 38  LEU C CA  1 
ATOM   2501 C C   . LEU C 1 38  ? -45.522 15.267  -32.545 1.00 25.40 ? 38  LEU C C   1 
ATOM   2502 O O   . LEU C 1 38  ? -46.330 14.452  -33.049 1.00 23.85 ? 38  LEU C O   1 
ATOM   2503 C CB  . LEU C 1 38  ? -43.057 14.528  -32.576 1.00 25.32 ? 38  LEU C CB  1 
ATOM   2504 C CG  . LEU C 1 38  ? -41.710 14.401  -31.845 1.00 24.42 ? 38  LEU C CG  1 
ATOM   2505 C CD1 . LEU C 1 38  ? -40.592 13.847  -32.774 1.00 24.88 ? 38  LEU C CD1 1 
ATOM   2506 C CD2 . LEU C 1 38  ? -41.315 15.762  -31.140 1.00 22.54 ? 38  LEU C CD2 1 
ATOM   2507 N N   . THR C 1 39  ? -45.618 16.591  -32.719 1.00 25.41 ? 39  THR C N   1 
ATOM   2508 C CA  . THR C 1 39  ? -46.555 17.149  -33.673 1.00 28.03 ? 39  THR C CA  1 
ATOM   2509 C C   . THR C 1 39  ? -46.040 16.800  -35.088 1.00 30.21 ? 39  THR C C   1 
ATOM   2510 O O   . THR C 1 39  ? -44.808 16.921  -35.354 1.00 31.72 ? 39  THR C O   1 
ATOM   2511 C CB  . THR C 1 39  ? -46.779 18.693  -33.471 1.00 28.74 ? 39  THR C CB  1 
ATOM   2512 O OG1 . THR C 1 39  ? -45.713 19.457  -34.073 1.00 32.01 ? 39  THR C OG1 1 
ATOM   2513 C CG2 . THR C 1 39  ? -46.852 19.031  -32.038 1.00 26.03 ? 39  THR C CG2 1 
ATOM   2514 N N   . GLU C 1 40  ? -46.948 16.305  -35.959 1.00 31.39 ? 40  GLU C N   1 
ATOM   2515 C CA  . GLU C 1 40  ? -46.661 16.035  -37.384 1.00 31.54 ? 40  GLU C CA  1 
ATOM   2516 C C   . GLU C 1 40  ? -45.613 16.954  -37.948 1.00 30.93 ? 40  GLU C C   1 
ATOM   2517 O O   . GLU C 1 40  ? -45.660 18.202  -37.773 1.00 30.35 ? 40  GLU C O   1 
ATOM   2518 C CB  . GLU C 1 40  ? -47.894 16.158  -38.266 1.00 31.81 ? 40  GLU C CB  1 
ATOM   2519 C CG  . GLU C 1 40  ? -47.597 15.823  -39.765 1.00 37.67 ? 40  GLU C CG  1 
ATOM   2520 C CD  . GLU C 1 40  ? -48.753 15.061  -40.456 1.00 43.05 ? 40  GLU C CD  1 
ATOM   2521 O OE1 . GLU C 1 40  ? -49.913 15.194  -39.952 1.00 42.41 ? 40  GLU C OE1 1 
ATOM   2522 O OE2 . GLU C 1 40  ? -48.491 14.335  -41.474 1.00 41.44 ? 40  GLU C OE2 1 
ATOM   2523 N N   . GLY C 1 41  ? -44.643 16.333  -38.615 1.00 29.65 ? 41  GLY C N   1 
ATOM   2524 C CA  . GLY C 1 41  ? -43.613 17.108  -39.234 1.00 29.63 ? 41  GLY C CA  1 
ATOM   2525 C C   . GLY C 1 41  ? -42.204 16.979  -38.717 1.00 29.53 ? 41  GLY C C   1 
ATOM   2526 O O   . GLY C 1 41  ? -41.799 15.948  -38.139 1.00 29.45 ? 41  GLY C O   1 
ATOM   2527 N N   . LEU C 1 42  ? -41.476 18.075  -38.918 1.00 28.45 ? 42  LEU C N   1 
ATOM   2528 C CA  . LEU C 1 42  ? -40.032 18.074  -38.926 1.00 28.23 ? 42  LEU C CA  1 
ATOM   2529 C C   . LEU C 1 42  ? -39.539 18.899  -37.747 1.00 27.15 ? 42  LEU C C   1 
ATOM   2530 O O   . LEU C 1 42  ? -39.887 20.086  -37.595 1.00 27.34 ? 42  LEU C O   1 
ATOM   2531 C CB  . LEU C 1 42  ? -39.607 18.611  -40.305 1.00 29.18 ? 42  LEU C CB  1 
ATOM   2532 C CG  . LEU C 1 42  ? -38.302 18.680  -41.075 1.00 29.85 ? 42  LEU C CG  1 
ATOM   2533 C CD1 . LEU C 1 42  ? -37.727 17.296  -41.419 1.00 31.07 ? 42  LEU C CD1 1 
ATOM   2534 C CD2 . LEU C 1 42  ? -38.629 19.504  -42.323 1.00 28.29 ? 42  LEU C CD2 1 
ATOM   2535 N N   . HIS C 1 43  ? -38.769 18.241  -36.874 1.00 25.46 ? 43  HIS C N   1 
ATOM   2536 C CA  . HIS C 1 43  ? -38.290 18.826  -35.585 1.00 23.66 ? 43  HIS C CA  1 
ATOM   2537 C C   . HIS C 1 43  ? -36.740 18.801  -35.529 1.00 23.10 ? 43  HIS C C   1 
ATOM   2538 O O   . HIS C 1 43  ? -36.148 17.813  -35.896 1.00 22.55 ? 43  HIS C O   1 
ATOM   2539 C CB  . HIS C 1 43  ? -38.872 18.064  -34.415 1.00 22.90 ? 43  HIS C CB  1 
ATOM   2540 C CG  . HIS C 1 43  ? -40.379 18.039  -34.369 1.00 23.52 ? 43  HIS C CG  1 
ATOM   2541 N ND1 . HIS C 1 43  ? -41.134 19.122  -33.976 1.00 23.13 ? 43  HIS C ND1 1 
ATOM   2542 C CD2 . HIS C 1 43  ? -41.263 17.050  -34.646 1.00 21.12 ? 43  HIS C CD2 1 
ATOM   2543 C CE1 . HIS C 1 43  ? -42.414 18.813  -34.046 1.00 26.19 ? 43  HIS C CE1 1 
ATOM   2544 N NE2 . HIS C 1 43  ? -42.518 17.558  -34.454 1.00 24.39 ? 43  HIS C NE2 1 
ATOM   2545 N N   . GLY C 1 44  ? -36.086 19.903  -35.146 1.00 22.21 ? 44  GLY C N   1 
ATOM   2546 C CA  . GLY C 1 44  ? -34.629 19.912  -35.044 1.00 21.56 ? 44  GLY C CA  1 
ATOM   2547 C C   . GLY C 1 44  ? -34.021 18.950  -33.991 1.00 20.93 ? 44  GLY C C   1 
ATOM   2548 O O   . GLY C 1 44  ? -34.613 18.674  -32.969 1.00 18.95 ? 44  GLY C O   1 
ATOM   2549 N N   . PHE C 1 45  ? -32.797 18.492  -34.238 1.00 20.19 ? 45  PHE C N   1 
ATOM   2550 C CA  . PHE C 1 45  ? -32.234 17.292  -33.582 1.00 20.29 ? 45  PHE C CA  1 
ATOM   2551 C C   . PHE C 1 45  ? -30.714 17.636  -33.449 1.00 20.49 ? 45  PHE C C   1 
ATOM   2552 O O   . PHE C 1 45  ? -29.982 17.693  -34.460 1.00 20.29 ? 45  PHE C O   1 
ATOM   2553 C CB  . PHE C 1 45  ? -32.558 16.111  -34.485 1.00 19.15 ? 45  PHE C CB  1 
ATOM   2554 C CG  . PHE C 1 45  ? -32.263 14.725  -33.929 1.00 22.45 ? 45  PHE C CG  1 
ATOM   2555 C CD1 . PHE C 1 45  ? -32.874 14.255  -32.762 1.00 22.31 ? 45  PHE C CD1 1 
ATOM   2556 C CD2 . PHE C 1 45  ? -31.460 13.831  -34.668 1.00 17.67 ? 45  PHE C CD2 1 
ATOM   2557 C CE1 . PHE C 1 45  ? -32.654 12.984  -32.305 1.00 25.10 ? 45  PHE C CE1 1 
ATOM   2558 C CE2 . PHE C 1 45  ? -31.224 12.535  -34.221 1.00 21.56 ? 45  PHE C CE2 1 
ATOM   2559 C CZ  . PHE C 1 45  ? -31.805 12.100  -33.013 1.00 23.91 ? 45  PHE C CZ  1 
ATOM   2560 N N   . HIS C 1 46  ? -30.269 17.923  -32.220 1.00 18.96 ? 46  HIS C N   1 
ATOM   2561 C CA  . HIS C 1 46  ? -28.972 18.562  -31.988 1.00 18.76 ? 46  HIS C CA  1 
ATOM   2562 C C   . HIS C 1 46  ? -28.357 17.900  -30.808 1.00 17.66 ? 46  HIS C C   1 
ATOM   2563 O O   . HIS C 1 46  ? -29.048 17.626  -29.867 1.00 15.48 ? 46  HIS C O   1 
ATOM   2564 C CB  . HIS C 1 46  ? -29.165 20.100  -31.699 1.00 19.13 ? 46  HIS C CB  1 
ATOM   2565 C CG  . HIS C 1 46  ? -29.080 20.928  -32.932 1.00 20.90 ? 46  HIS C CG  1 
ATOM   2566 N ND1 . HIS C 1 46  ? -30.193 21.404  -33.601 1.00 24.42 ? 46  HIS C ND1 1 
ATOM   2567 C CD2 . HIS C 1 46  ? -28.005 21.298  -33.664 1.00 15.72 ? 46  HIS C CD2 1 
ATOM   2568 C CE1 . HIS C 1 46  ? -29.789 22.036  -34.687 1.00 23.59 ? 46  HIS C CE1 1 
ATOM   2569 N NE2 . HIS C 1 46  ? -28.463 21.976  -34.747 1.00 16.80 ? 46  HIS C NE2 1 
ATOM   2570 N N   . VAL C 1 47  ? -27.046 17.620  -30.890 1.00 17.85 ? 47  VAL C N   1 
ATOM   2571 C CA  . VAL C 1 47  ? -26.248 17.284  -29.713 1.00 17.76 ? 47  VAL C CA  1 
ATOM   2572 C C   . VAL C 1 47  ? -25.873 18.644  -29.090 1.00 19.72 ? 47  VAL C C   1 
ATOM   2573 O O   . VAL C 1 47  ? -25.517 19.569  -29.820 1.00 19.39 ? 47  VAL C O   1 
ATOM   2574 C CB  . VAL C 1 47  ? -25.008 16.389  -30.021 1.00 16.88 ? 47  VAL C CB  1 
ATOM   2575 C CG1 . VAL C 1 47  ? -24.158 16.227  -28.774 1.00 12.83 ? 47  VAL C CG1 1 
ATOM   2576 C CG2 . VAL C 1 47  ? -25.429 14.990  -30.675 1.00 16.98 ? 47  VAL C CG2 1 
ATOM   2577 N N   . HIS C 1 48  ? -26.056 18.759  -27.754 1.00 19.54 ? 48  HIS C N   1 
ATOM   2578 C CA  . HIS C 1 48  ? -25.790 19.956  -27.017 1.00 21.09 ? 48  HIS C CA  1 
ATOM   2579 C C   . HIS C 1 48  ? -24.590 19.709  -26.123 1.00 20.88 ? 48  HIS C C   1 
ATOM   2580 O O   . HIS C 1 48  ? -24.218 18.570  -25.932 1.00 19.01 ? 48  HIS C O   1 
ATOM   2581 C CB  . HIS C 1 48  ? -27.036 20.317  -26.234 1.00 21.94 ? 48  HIS C CB  1 
ATOM   2582 C CG  . HIS C 1 48  ? -28.105 20.946  -27.086 1.00 24.02 ? 48  HIS C CG  1 
ATOM   2583 N ND1 . HIS C 1 48  ? -28.344 22.295  -27.094 1.00 21.65 ? 48  HIS C ND1 1 
ATOM   2584 C CD2 . HIS C 1 48  ? -28.989 20.410  -27.955 1.00 24.95 ? 48  HIS C CD2 1 
ATOM   2585 C CE1 . HIS C 1 48  ? -29.325 22.576  -27.916 1.00 21.26 ? 48  HIS C CE1 1 
ATOM   2586 N NE2 . HIS C 1 48  ? -29.747 21.450  -28.445 1.00 25.07 ? 48  HIS C NE2 1 
ATOM   2587 N N   . GLU C 1 49  ? -23.986 20.764  -25.594 1.00 20.10 ? 49  GLU C N   1 
ATOM   2588 C CA  . GLU C 1 49  ? -22.663 20.673  -24.952 1.00 21.96 ? 49  GLU C CA  1 
ATOM   2589 C C   . GLU C 1 49  ? -22.549 19.885  -23.652 1.00 21.79 ? 49  GLU C C   1 
ATOM   2590 O O   . GLU C 1 49  ? -21.521 19.248  -23.418 1.00 21.10 ? 49  GLU C O   1 
ATOM   2591 C CB  . GLU C 1 49  ? -22.056 22.059  -24.733 1.00 20.43 ? 49  GLU C CB  1 
ATOM   2592 C CG  . GLU C 1 49  ? -20.567 21.994  -24.297 1.00 24.96 ? 49  GLU C CG  1 
ATOM   2593 C CD  . GLU C 1 49  ? -19.884 23.367  -24.159 1.00 23.90 ? 49  GLU C CD  1 
ATOM   2594 O OE1 . GLU C 1 49  ? -20.364 24.351  -24.781 1.00 33.53 ? 49  GLU C OE1 1 
ATOM   2595 O OE2 . GLU C 1 49  ? -18.870 23.477  -23.436 1.00 25.77 ? 49  GLU C OE2 1 
ATOM   2596 N N   . PHE C 1 50  ? -23.545 20.003  -22.768 1.00 22.62 ? 50  PHE C N   1 
ATOM   2597 C CA  . PHE C 1 50  ? -23.396 19.463  -21.427 1.00 22.53 ? 50  PHE C CA  1 
ATOM   2598 C C   . PHE C 1 50  ? -24.360 18.385  -21.242 1.00 23.15 ? 50  PHE C C   1 
ATOM   2599 O O   . PHE C 1 50  ? -25.453 18.386  -21.855 1.00 24.12 ? 50  PHE C O   1 
ATOM   2600 C CB  . PHE C 1 50  ? -23.523 20.534  -20.303 1.00 23.35 ? 50  PHE C CB  1 
ATOM   2601 C CG  . PHE C 1 50  ? -22.664 21.733  -20.531 1.00 23.60 ? 50  PHE C CG  1 
ATOM   2602 C CD1 . PHE C 1 50  ? -21.265 21.617  -20.483 1.00 21.86 ? 50  PHE C CD1 1 
ATOM   2603 C CD2 . PHE C 1 50  ? -23.247 22.982  -20.830 1.00 19.39 ? 50  PHE C CD2 1 
ATOM   2604 C CE1 . PHE C 1 50  ? -20.466 22.711  -20.736 1.00 22.77 ? 50  PHE C CE1 1 
ATOM   2605 C CE2 . PHE C 1 50  ? -22.443 24.059  -21.102 1.00 18.00 ? 50  PHE C CE2 1 
ATOM   2606 C CZ  . PHE C 1 50  ? -21.063 23.936  -21.072 1.00 20.91 ? 50  PHE C CZ  1 
ATOM   2607 N N   . GLY C 1 51  ? -23.943 17.420  -20.426 1.00 23.31 ? 51  GLY C N   1 
ATOM   2608 C CA  . GLY C 1 51  ? -24.725 16.252  -20.162 1.00 22.83 ? 51  GLY C CA  1 
ATOM   2609 C C   . GLY C 1 51  ? -25.409 16.466  -18.839 1.00 24.20 ? 51  GLY C C   1 
ATOM   2610 O O   . GLY C 1 51  ? -25.407 15.565  -18.001 1.00 24.51 ? 51  GLY C O   1 
ATOM   2611 N N   . ASP C 1 52  ? -25.985 17.666  -18.689 1.00 24.64 ? 52  ASP C N   1 
ATOM   2612 C CA  . ASP C 1 52  ? -26.637 18.181  -17.493 1.00 25.08 ? 52  ASP C CA  1 
ATOM   2613 C C   . ASP C 1 52  ? -28.094 18.369  -17.790 1.00 25.94 ? 52  ASP C C   1 
ATOM   2614 O O   . ASP C 1 52  ? -28.453 18.992  -18.769 1.00 26.76 ? 52  ASP C O   1 
ATOM   2615 C CB  . ASP C 1 52  ? -26.009 19.523  -17.160 1.00 25.64 ? 52  ASP C CB  1 
ATOM   2616 C CG  . ASP C 1 52  ? -26.372 20.063  -15.742 1.00 26.67 ? 52  ASP C CG  1 
ATOM   2617 O OD1 . ASP C 1 52  ? -27.393 19.690  -15.071 1.00 21.53 ? 52  ASP C OD1 1 
ATOM   2618 O OD2 . ASP C 1 52  ? -25.585 20.926  -15.343 1.00 31.98 ? 52  ASP C OD2 1 
ATOM   2619 N N   . ASN C 1 53  ? -28.926 17.813  -16.933 1.00 27.32 ? 53  ASN C N   1 
ATOM   2620 C CA  . ASN C 1 53  ? -30.353 17.842  -17.034 1.00 28.61 ? 53  ASN C CA  1 
ATOM   2621 C C   . ASN C 1 53  ? -30.910 18.386  -15.699 1.00 29.53 ? 53  ASN C C   1 
ATOM   2622 O O   . ASN C 1 53  ? -32.107 18.228  -15.408 1.00 29.93 ? 53  ASN C O   1 
ATOM   2623 C CB  . ASN C 1 53  ? -30.891 16.400  -17.265 1.00 29.85 ? 53  ASN C CB  1 
ATOM   2624 C CG  . ASN C 1 53  ? -32.372 16.370  -17.662 1.00 31.49 ? 53  ASN C CG  1 
ATOM   2625 O OD1 . ASN C 1 53  ? -32.808 17.078  -18.586 1.00 28.80 ? 53  ASN C OD1 1 
ATOM   2626 N ND2 . ASN C 1 53  ? -33.155 15.557  -16.955 1.00 36.61 ? 53  ASN C ND2 1 
ATOM   2627 N N   . ARG C 1 54  ? -30.057 18.981  -14.873 1.00 29.76 ? 54  ARG C N   1 
ATOM   2628 C CA  . ARG C 1 54  ? -30.507 19.450  -13.529 1.00 31.50 ? 54  ARG C CA  1 
ATOM   2629 C C   . ARG C 1 54  ? -31.840 20.124  -13.573 1.00 31.86 ? 54  ARG C C   1 
ATOM   2630 O O   . ARG C 1 54  ? -32.760 19.726  -12.879 1.00 32.66 ? 54  ARG C O   1 
ATOM   2631 C CB  . ARG C 1 54  ? -29.549 20.473  -12.965 1.00 30.81 ? 54  ARG C CB  1 
ATOM   2632 C CG  . ARG C 1 54  ? -28.599 19.947  -11.993 1.00 32.36 ? 54  ARG C CG  1 
ATOM   2633 C CD  . ARG C 1 54  ? -27.613 21.026  -11.702 1.00 30.01 ? 54  ARG C CD  1 
ATOM   2634 N NE  . ARG C 1 54  ? -26.455 20.931  -12.571 1.00 34.25 ? 54  ARG C NE  1 
ATOM   2635 C CZ  . ARG C 1 54  ? -25.210 20.823  -12.120 1.00 35.41 ? 54  ARG C CZ  1 
ATOM   2636 N NH1 . ARG C 1 54  ? -25.028 20.780  -10.799 1.00 32.39 ? 54  ARG C NH1 1 
ATOM   2637 N NH2 . ARG C 1 54  ? -24.174 20.738  -12.966 1.00 32.64 ? 54  ARG C NH2 1 
ATOM   2638 N N   . ALA C 1 55  ? -31.930 21.166  -14.402 1.00 33.05 ? 55  ALA C N   1 
ATOM   2639 C CA  . ALA C 1 55  ? -33.129 21.987  -14.529 1.00 33.31 ? 55  ALA C CA  1 
ATOM   2640 C C   . ALA C 1 55  ? -33.874 21.703  -15.857 1.00 33.05 ? 55  ALA C C   1 
ATOM   2641 O O   . ALA C 1 55  ? -34.426 22.596  -16.470 1.00 34.59 ? 55  ALA C O   1 
ATOM   2642 C CB  . ALA C 1 55  ? -32.729 23.498  -14.386 1.00 33.90 ? 55  ALA C CB  1 
ATOM   2643 N N   . GLY C 1 56  ? -33.877 20.441  -16.288 1.00 32.64 ? 56  GLY C N   1 
ATOM   2644 C CA  . GLY C 1 56  ? -34.549 19.996  -17.493 1.00 30.32 ? 56  GLY C CA  1 
ATOM   2645 C C   . GLY C 1 56  ? -33.615 20.017  -18.663 1.00 28.85 ? 56  GLY C C   1 
ATOM   2646 O O   . GLY C 1 56  ? -32.413 20.024  -18.500 1.00 29.79 ? 56  GLY C O   1 
ATOM   2647 N N   . CYS C 1 57  ? -34.192 20.076  -19.847 1.00 28.62 ? 57  CYS C N   1 
ATOM   2648 C CA  . CYS C 1 57  ? -33.474 20.144  -21.108 1.00 28.36 ? 57  CYS C CA  1 
ATOM   2649 C C   . CYS C 1 57  ? -32.628 21.355  -21.282 1.00 27.73 ? 57  CYS C C   1 
ATOM   2650 O O   . CYS C 1 57  ? -31.682 21.328  -22.065 1.00 26.68 ? 57  CYS C O   1 
ATOM   2651 C CB  . CYS C 1 57  ? -34.432 20.030  -22.292 1.00 27.22 ? 57  CYS C CB  1 
ATOM   2652 S SG  . CYS C 1 57  ? -35.001 18.332  -22.409 1.00 30.13 ? 57  CYS C SG  1 
ATOM   2653 N N   . THR C 1 58  ? -33.013 22.408  -20.570 1.00 27.83 ? 58  THR C N   1 
ATOM   2654 C CA  . THR C 1 58  ? -32.324 23.691  -20.592 1.00 28.98 ? 58  THR C CA  1 
ATOM   2655 C C   . THR C 1 58  ? -30.887 23.721  -20.091 1.00 26.86 ? 58  THR C C   1 
ATOM   2656 O O   . THR C 1 58  ? -30.220 24.659  -20.418 1.00 26.85 ? 58  THR C O   1 
ATOM   2657 C CB  . THR C 1 58  ? -33.117 24.702  -19.801 1.00 29.98 ? 58  THR C CB  1 
ATOM   2658 O OG1 . THR C 1 58  ? -34.416 24.801  -20.420 1.00 35.10 ? 58  THR C OG1 1 
ATOM   2659 C CG2 . THR C 1 58  ? -32.443 26.063  -19.881 1.00 32.12 ? 58  THR C CG2 1 
ATOM   2660 N N   . SER C 1 59  ? -30.424 22.706  -19.329 1.00 24.63 ? 59  SER C N   1 
ATOM   2661 C CA  . SER C 1 59  ? -29.110 22.719  -18.678 1.00 23.06 ? 59  SER C CA  1 
ATOM   2662 C C   . SER C 1 59  ? -28.061 22.103  -19.564 1.00 22.94 ? 59  SER C C   1 
ATOM   2663 O O   . SER C 1 59  ? -26.838 22.163  -19.225 1.00 21.65 ? 59  SER C O   1 
ATOM   2664 C CB  . SER C 1 59  ? -29.084 21.936  -17.374 1.00 21.13 ? 59  SER C CB  1 
ATOM   2665 O OG  . SER C 1 59  ? -30.332 21.861  -16.775 1.00 26.68 ? 59  SER C OG  1 
ATOM   2666 N N   . ALA C 1 60  ? -28.569 21.422  -20.608 1.00 23.36 ? 60  ALA C N   1 
ATOM   2667 C CA  . ALA C 1 60  ? -27.832 20.955  -21.823 1.00 23.96 ? 60  ALA C CA  1 
ATOM   2668 C C   . ALA C 1 60  ? -26.938 21.996  -22.468 1.00 25.00 ? 60  ALA C C   1 
ATOM   2669 O O   . ALA C 1 60  ? -25.964 21.625  -23.120 1.00 27.69 ? 60  ALA C O   1 
ATOM   2670 C CB  . ALA C 1 60  ? -28.783 20.411  -22.828 1.00 23.16 ? 60  ALA C CB  1 
ATOM   2671 N N   . GLY C 1 61  ? -27.243 23.289  -22.278 1.00 24.37 ? 61  GLY C N   1 
ATOM   2672 C CA  . GLY C 1 61  ? -26.449 24.361  -22.786 1.00 23.76 ? 61  GLY C CA  1 
ATOM   2673 C C   . GLY C 1 61  ? -26.637 24.572  -24.287 1.00 24.14 ? 61  GLY C C   1 
ATOM   2674 O O   . GLY C 1 61  ? -27.675 24.187  -24.823 1.00 24.31 ? 61  GLY C O   1 
ATOM   2675 N N   . PRO C 1 62  ? -25.615 25.141  -24.971 1.00 22.95 ? 62  PRO C N   1 
ATOM   2676 C CA  . PRO C 1 62  ? -25.593 25.366  -26.385 1.00 24.30 ? 62  PRO C CA  1 
ATOM   2677 C C   . PRO C 1 62  ? -25.345 24.072  -27.191 1.00 25.14 ? 62  PRO C C   1 
ATOM   2678 O O   . PRO C 1 62  ? -24.974 23.054  -26.623 1.00 23.83 ? 62  PRO C O   1 
ATOM   2679 C CB  . PRO C 1 62  ? -24.393 26.322  -26.558 1.00 25.67 ? 62  PRO C CB  1 
ATOM   2680 C CG  . PRO C 1 62  ? -23.412 25.846  -25.535 1.00 22.59 ? 62  PRO C CG  1 
ATOM   2681 C CD  . PRO C 1 62  ? -24.363 25.587  -24.341 1.00 23.69 ? 62  PRO C CD  1 
ATOM   2682 N N   . HIS C 1 63  ? -25.531 24.172  -28.511 1.00 25.00 ? 63  HIS C N   1 
ATOM   2683 C CA  . HIS C 1 63  ? -25.198 23.153  -29.482 1.00 25.88 ? 63  HIS C CA  1 
ATOM   2684 C C   . HIS C 1 63  ? -23.775 22.744  -29.262 1.00 26.44 ? 63  HIS C C   1 
ATOM   2685 O O   . HIS C 1 63  ? -22.905 23.592  -29.084 1.00 26.28 ? 63  HIS C O   1 
ATOM   2686 C CB  . HIS C 1 63  ? -25.318 23.699  -30.939 1.00 24.87 ? 63  HIS C CB  1 
ATOM   2687 C CG  . HIS C 1 63  ? -26.720 23.977  -31.382 1.00 27.45 ? 63  HIS C CG  1 
ATOM   2688 N ND1 . HIS C 1 63  ? -27.009 24.751  -32.485 1.00 29.92 ? 63  HIS C ND1 1 
ATOM   2689 C CD2 . HIS C 1 63  ? -27.917 23.617  -30.858 1.00 26.46 ? 63  HIS C CD2 1 
ATOM   2690 C CE1 . HIS C 1 63  ? -28.316 24.812  -32.648 1.00 27.62 ? 63  HIS C CE1 1 
ATOM   2691 N NE2 . HIS C 1 63  ? -28.887 24.156  -31.656 1.00 27.33 ? 63  HIS C NE2 1 
ATOM   2692 N N   . PHE C 1 64  ? -23.492 21.442  -29.384 1.00 28.29 ? 64  PHE C N   1 
ATOM   2693 C CA  . PHE C 1 64  ? -22.104 21.018  -29.210 1.00 29.74 ? 64  PHE C CA  1 
ATOM   2694 C C   . PHE C 1 64  ? -21.198 21.616  -30.336 1.00 31.77 ? 64  PHE C C   1 
ATOM   2695 O O   . PHE C 1 64  ? -21.443 21.408  -31.490 1.00 31.60 ? 64  PHE C O   1 
ATOM   2696 C CB  . PHE C 1 64  ? -22.024 19.484  -29.096 1.00 28.71 ? 64  PHE C CB  1 
ATOM   2697 C CG  . PHE C 1 64  ? -20.634 18.968  -28.917 1.00 28.20 ? 64  PHE C CG  1 
ATOM   2698 C CD1 . PHE C 1 64  ? -19.791 19.524  -27.942 1.00 25.45 ? 64  PHE C CD1 1 
ATOM   2699 C CD2 . PHE C 1 64  ? -20.152 17.938  -29.735 1.00 26.16 ? 64  PHE C CD2 1 
ATOM   2700 C CE1 . PHE C 1 64  ? -18.530 19.064  -27.760 1.00 27.14 ? 64  PHE C CE1 1 
ATOM   2701 C CE2 . PHE C 1 64  ? -18.850 17.479  -29.570 1.00 26.55 ? 64  PHE C CE2 1 
ATOM   2702 C CZ  . PHE C 1 64  ? -18.043 18.005  -28.581 1.00 24.57 ? 64  PHE C CZ  1 
ATOM   2703 N N   . ASN C 1 65  ? -20.165 22.386  -30.003 1.00 35.15 ? 65  ASN C N   1 
ATOM   2704 C CA  . ASN C 1 65  ? -19.363 23.027  -31.061 1.00 37.64 ? 65  ASN C CA  1 
ATOM   2705 C C   . ASN C 1 65  ? -17.861 23.002  -30.752 1.00 39.07 ? 65  ASN C C   1 
ATOM   2706 O O   . ASN C 1 65  ? -17.267 24.050  -30.612 1.00 39.60 ? 65  ASN C O   1 
ATOM   2707 C CB  . ASN C 1 65  ? -19.836 24.481  -31.235 1.00 38.52 ? 65  ASN C CB  1 
ATOM   2708 C CG  . ASN C 1 65  ? -19.334 25.134  -32.523 1.00 40.13 ? 65  ASN C CG  1 
ATOM   2709 O OD1 . ASN C 1 65  ? -19.387 24.557  -33.604 1.00 43.94 ? 65  ASN C OD1 1 
ATOM   2710 N ND2 . ASN C 1 65  ? -18.837 26.346  -32.394 1.00 43.25 ? 65  ASN C ND2 1 
ATOM   2711 N N   . PRO C 1 66  ? -17.234 21.808  -30.665 1.00 39.77 ? 66  PRO C N   1 
ATOM   2712 C CA  . PRO C 1 66  ? -15.963 21.713  -29.929 1.00 40.93 ? 66  PRO C CA  1 
ATOM   2713 C C   . PRO C 1 66  ? -14.947 22.779  -30.326 1.00 42.60 ? 66  PRO C C   1 
ATOM   2714 O O   . PRO C 1 66  ? -14.178 23.232  -29.446 1.00 43.85 ? 66  PRO C O   1 
ATOM   2715 C CB  . PRO C 1 66  ? -15.458 20.291  -30.233 1.00 40.58 ? 66  PRO C CB  1 
ATOM   2716 C CG  . PRO C 1 66  ? -16.314 19.791  -31.330 1.00 40.20 ? 66  PRO C CG  1 
ATOM   2717 C CD  . PRO C 1 66  ? -17.629 20.514  -31.227 1.00 39.47 ? 66  PRO C CD  1 
ATOM   2718 N N   . LEU C 1 67  ? -14.947 23.179  -31.610 1.00 42.66 ? 67  LEU C N   1 
ATOM   2719 C CA  . LEU C 1 67  ? -14.261 24.411  -32.026 1.00 43.19 ? 67  LEU C CA  1 
ATOM   2720 C C   . LEU C 1 67  ? -15.255 25.507  -32.497 1.00 43.49 ? 67  LEU C C   1 
ATOM   2721 O O   . LEU C 1 67  ? -15.091 26.168  -33.541 1.00 43.92 ? 67  LEU C O   1 
ATOM   2722 C CB  . LEU C 1 67  ? -13.140 24.133  -33.040 1.00 43.21 ? 67  LEU C CB  1 
ATOM   2723 C CG  . LEU C 1 67  ? -12.490 22.742  -32.937 1.00 42.78 ? 67  LEU C CG  1 
ATOM   2724 C CD1 . LEU C 1 67  ? -12.971 21.824  -34.109 1.00 40.27 ? 67  LEU C CD1 1 
ATOM   2725 C CD2 . LEU C 1 67  ? -10.978 22.828  -32.847 1.00 41.24 ? 67  LEU C CD2 1 
ATOM   2726 N N   . HIS C 1 80  ? -22.202 23.358  -36.978 1.00 32.26 ? 80  HIS C N   1 
ATOM   2727 C CA  . HIS C 1 80  ? -21.881 22.852  -35.617 1.00 33.09 ? 80  HIS C CA  1 
ATOM   2728 C C   . HIS C 1 80  ? -21.733 21.319  -35.601 1.00 31.39 ? 80  HIS C C   1 
ATOM   2729 O O   . HIS C 1 80  ? -22.520 20.615  -36.266 1.00 31.60 ? 80  HIS C O   1 
ATOM   2730 C CB  . HIS C 1 80  ? -22.921 23.344  -34.552 1.00 34.18 ? 80  HIS C CB  1 
ATOM   2731 C CG  . HIS C 1 80  ? -23.229 24.820  -34.622 1.00 39.98 ? 80  HIS C CG  1 
ATOM   2732 N ND1 . HIS C 1 80  ? -23.893 25.493  -33.614 1.00 44.78 ? 80  HIS C ND1 1 
ATOM   2733 C CD2 . HIS C 1 80  ? -22.945 25.756  -35.566 1.00 44.73 ? 80  HIS C CD2 1 
ATOM   2734 C CE1 . HIS C 1 80  ? -24.020 26.769  -33.940 1.00 46.14 ? 80  HIS C CE1 1 
ATOM   2735 N NE2 . HIS C 1 80  ? -23.451 26.958  -35.120 1.00 46.82 ? 80  HIS C NE2 1 
ATOM   2736 N N   . VAL C 1 81  ? -20.725 20.816  -34.879 1.00 29.15 ? 81  VAL C N   1 
ATOM   2737 C CA  . VAL C 1 81  ? -20.468 19.361  -34.783 1.00 28.33 ? 81  VAL C CA  1 
ATOM   2738 C C   . VAL C 1 81  ? -21.735 18.587  -34.381 1.00 28.51 ? 81  VAL C C   1 
ATOM   2739 O O   . VAL C 1 81  ? -22.170 17.728  -35.135 1.00 30.92 ? 81  VAL C O   1 
ATOM   2740 C CB  . VAL C 1 81  ? -19.228 18.996  -33.907 1.00 27.02 ? 81  VAL C CB  1 
ATOM   2741 C CG1 . VAL C 1 81  ? -19.163 17.516  -33.558 1.00 26.50 ? 81  VAL C CG1 1 
ATOM   2742 C CG2 . VAL C 1 81  ? -17.952 19.410  -34.604 1.00 27.60 ? 81  VAL C CG2 1 
ATOM   2743 N N   . GLY C 1 82  ? -22.387 18.935  -33.284 1.00 27.81 ? 82  GLY C N   1 
ATOM   2744 C CA  . GLY C 1 82  ? -23.658 18.255  -32.926 1.00 27.12 ? 82  GLY C CA  1 
ATOM   2745 C C   . GLY C 1 82  ? -24.907 18.341  -33.805 1.00 25.40 ? 82  GLY C C   1 
ATOM   2746 O O   . GLY C 1 82  ? -25.963 17.802  -33.465 1.00 22.33 ? 82  GLY C O   1 
ATOM   2747 N N   . ASP C 1 83  ? -24.804 19.068  -34.916 1.00 26.39 ? 83  ASP C N   1 
ATOM   2748 C CA  . ASP C 1 83  ? -25.935 19.333  -35.834 1.00 27.26 ? 83  ASP C CA  1 
ATOM   2749 C C   . ASP C 1 83  ? -26.436 18.099  -36.591 1.00 27.38 ? 83  ASP C C   1 
ATOM   2750 O O   . ASP C 1 83  ? -25.829 17.706  -37.602 1.00 29.01 ? 83  ASP C O   1 
ATOM   2751 C CB  . ASP C 1 83  ? -25.532 20.450  -36.850 1.00 28.54 ? 83  ASP C CB  1 
ATOM   2752 C CG  . ASP C 1 83  ? -25.463 21.844  -36.210 1.00 33.97 ? 83  ASP C CG  1 
ATOM   2753 O OD1 . ASP C 1 83  ? -25.318 21.935  -34.945 1.00 37.38 ? 83  ASP C OD1 1 
ATOM   2754 O OD2 . ASP C 1 83  ? -25.550 22.882  -36.962 1.00 41.32 ? 83  ASP C OD2 1 
ATOM   2755 N N   . LEU C 1 84  ? -27.518 17.469  -36.136 1.00 25.60 ? 84  LEU C N   1 
ATOM   2756 C CA  . LEU C 1 84  ? -27.993 16.291  -36.848 1.00 24.04 ? 84  LEU C CA  1 
ATOM   2757 C C   . LEU C 1 84  ? -29.215 16.525  -37.743 1.00 23.24 ? 84  LEU C C   1 
ATOM   2758 O O   . LEU C 1 84  ? -29.894 15.572  -38.141 1.00 21.52 ? 84  LEU C O   1 
ATOM   2759 C CB  . LEU C 1 84  ? -28.223 15.085  -35.899 1.00 24.23 ? 84  LEU C CB  1 
ATOM   2760 C CG  . LEU C 1 84  ? -27.094 14.718  -34.940 1.00 22.04 ? 84  LEU C CG  1 
ATOM   2761 C CD1 . LEU C 1 84  ? -27.685 13.682  -34.013 1.00 23.84 ? 84  LEU C CD1 1 
ATOM   2762 C CD2 . LEU C 1 84  ? -25.891 14.203  -35.750 1.00 20.42 ? 84  LEU C CD2 1 
ATOM   2763 N N   . GLY C 1 85  ? -29.457 17.798  -38.068 1.00 22.91 ? 85  GLY C N   1 
ATOM   2764 C CA  . GLY C 1 85  ? -30.596 18.188  -38.897 1.00 22.64 ? 85  GLY C CA  1 
ATOM   2765 C C   . GLY C 1 85  ? -31.906 18.219  -38.113 1.00 21.94 ? 85  GLY C C   1 
ATOM   2766 O O   . GLY C 1 85  ? -32.021 18.956  -37.110 1.00 22.65 ? 85  GLY C O   1 
ATOM   2767 N N   . ASN C 1 86  ? -32.860 17.457  -38.624 1.00 21.71 ? 86  ASN C N   1 
ATOM   2768 C CA  . ASN C 1 86  ? -34.227 17.360  -38.171 1.00 22.95 ? 86  ASN C CA  1 
ATOM   2769 C C   . ASN C 1 86  ? -34.591 15.898  -38.142 1.00 22.75 ? 86  ASN C C   1 
ATOM   2770 O O   . ASN C 1 86  ? -34.013 15.094  -38.865 1.00 20.62 ? 86  ASN C O   1 
ATOM   2771 C CB  . ASN C 1 86  ? -35.200 17.975  -39.193 1.00 24.21 ? 86  ASN C CB  1 
ATOM   2772 C CG  . ASN C 1 86  ? -35.064 19.471  -39.322 1.00 24.59 ? 86  ASN C CG  1 
ATOM   2773 O OD1 . ASN C 1 86  ? -35.388 20.205  -38.385 1.00 24.68 ? 86  ASN C OD1 1 
ATOM   2774 N ND2 . ASN C 1 86  ? -34.534 19.936  -40.484 1.00 24.54 ? 86  ASN C ND2 1 
ATOM   2775 N N   . VAL C 1 87  ? -35.563 15.567  -37.302 1.00 21.72 ? 87  VAL C N   1 
ATOM   2776 C CA  . VAL C 1 87  ? -36.297 14.314  -37.500 1.00 23.01 ? 87  VAL C CA  1 
ATOM   2777 C C   . VAL C 1 87  ? -37.743 14.682  -37.905 1.00 22.78 ? 87  VAL C C   1 
ATOM   2778 O O   . VAL C 1 87  ? -38.152 15.805  -37.671 1.00 22.34 ? 87  VAL C O   1 
ATOM   2779 C CB  . VAL C 1 87  ? -36.254 13.377  -36.286 1.00 21.25 ? 87  VAL C CB  1 
ATOM   2780 C CG1 . VAL C 1 87  ? -34.769 12.987  -35.999 1.00 23.61 ? 87  VAL C CG1 1 
ATOM   2781 C CG2 . VAL C 1 87  ? -36.956 14.030  -35.100 1.00 21.82 ? 87  VAL C CG2 1 
ATOM   2782 N N   . THR C 1 88  ? -38.462 13.722  -38.502 1.00 23.14 ? 88  THR C N   1 
ATOM   2783 C CA  . THR C 1 88  ? -39.808 13.943  -39.107 1.00 23.52 ? 88  THR C CA  1 
ATOM   2784 C C   . THR C 1 88  ? -40.828 13.018  -38.465 1.00 22.97 ? 88  THR C C   1 
ATOM   2785 O O   . THR C 1 88  ? -40.735 11.797  -38.614 1.00 22.43 ? 88  THR C O   1 
ATOM   2786 C CB  . THR C 1 88  ? -39.869 13.636  -40.644 1.00 22.09 ? 88  THR C CB  1 
ATOM   2787 O OG1 . THR C 1 88  ? -38.801 14.258  -41.367 1.00 22.55 ? 88  THR C OG1 1 
ATOM   2788 C CG2 . THR C 1 88  ? -41.170 14.061  -41.233 1.00 24.26 ? 88  THR C CG2 1 
ATOM   2789 N N   . ALA C 1 89  ? -41.772 13.606  -37.738 1.00 23.84 ? 89  ALA C N   1 
ATOM   2790 C CA  . ALA C 1 89  ? -42.905 12.845  -37.205 1.00 25.16 ? 89  ALA C CA  1 
ATOM   2791 C C   . ALA C 1 89  ? -43.955 12.730  -38.302 1.00 26.35 ? 89  ALA C C   1 
ATOM   2792 O O   . ALA C 1 89  ? -44.290 13.735  -38.986 1.00 25.01 ? 89  ALA C O   1 
ATOM   2793 C CB  . ALA C 1 89  ? -43.484 13.575  -36.043 1.00 24.02 ? 89  ALA C CB  1 
ATOM   2794 N N   . ASP C 1 90  ? -44.467 11.519  -38.452 1.00 27.92 ? 90  ASP C N   1 
ATOM   2795 C CA  . ASP C 1 90  ? -45.684 11.223  -39.219 1.00 29.50 ? 90  ASP C CA  1 
ATOM   2796 C C   . ASP C 1 90  ? -46.894 11.811  -38.473 1.00 31.32 ? 90  ASP C C   1 
ATOM   2797 O O   . ASP C 1 90  ? -46.743 12.555  -37.515 1.00 30.61 ? 90  ASP C O   1 
ATOM   2798 C CB  . ASP C 1 90  ? -45.811 9.681   -39.517 1.00 30.03 ? 90  ASP C CB  1 
ATOM   2799 C CG  . ASP C 1 90  ? -46.076 8.819   -38.283 1.00 29.18 ? 90  ASP C CG  1 
ATOM   2800 O OD1 . ASP C 1 90  ? -46.436 9.384   -37.250 1.00 29.11 ? 90  ASP C OD1 1 
ATOM   2801 O OD2 . ASP C 1 90  ? -45.962 7.548   -38.328 1.00 28.98 ? 90  ASP C OD2 1 
ATOM   2802 N N   . LYS C 1 91  ? -48.095 11.515  -38.946 1.00 33.86 ? 91  LYS C N   1 
ATOM   2803 C CA  . LYS C 1 91  ? -49.310 12.175  -38.468 1.00 34.55 ? 91  LYS C CA  1 
ATOM   2804 C C   . LYS C 1 91  ? -49.727 11.670  -37.080 1.00 35.46 ? 91  LYS C C   1 
ATOM   2805 O O   . LYS C 1 91  ? -50.211 12.459  -36.235 1.00 35.97 ? 91  LYS C O   1 
ATOM   2806 C CB  . LYS C 1 91  ? -50.433 11.956  -39.506 1.00 36.22 ? 91  LYS C CB  1 
ATOM   2807 C CG  . LYS C 1 91  ? -50.664 10.481  -39.849 1.00 35.44 ? 91  LYS C CG  1 
ATOM   2808 C CD  . LYS C 1 91  ? -51.001 10.266  -41.343 1.00 42.39 ? 91  LYS C CD  1 
ATOM   2809 C CE  . LYS C 1 91  ? -51.878 8.997   -41.515 1.00 41.46 ? 91  LYS C CE  1 
ATOM   2810 N NZ  . LYS C 1 91  ? -52.923 8.955   -40.407 1.00 42.17 ? 91  LYS C NZ  1 
ATOM   2811 N N   . ASP C 1 92  ? -49.565 10.350  -36.885 1.00 35.44 ? 92  ASP C N   1 
ATOM   2812 C CA  . ASP C 1 92  ? -49.500 9.662   -35.581 1.00 35.08 ? 92  ASP C CA  1 
ATOM   2813 C C   . ASP C 1 92  ? -48.428 10.116  -34.522 1.00 34.55 ? 92  ASP C C   1 
ATOM   2814 O O   . ASP C 1 92  ? -48.377 9.533   -33.439 1.00 34.01 ? 92  ASP C O   1 
ATOM   2815 C CB  . ASP C 1 92  ? -49.318 8.158   -35.827 1.00 35.83 ? 92  ASP C CB  1 
ATOM   2816 C CG  . ASP C 1 92  ? -50.567 7.504   -36.448 1.00 40.15 ? 92  ASP C CG  1 
ATOM   2817 O OD1 . ASP C 1 92  ? -51.723 7.947   -36.128 1.00 42.71 ? 92  ASP C OD1 1 
ATOM   2818 O OD2 . ASP C 1 92  ? -50.376 6.553   -37.243 1.00 38.94 ? 92  ASP C OD2 1 
ATOM   2819 N N   . GLY C 1 93  ? -47.610 11.135  -34.834 1.00 34.14 ? 93  GLY C N   1 
ATOM   2820 C CA  . GLY C 1 93  ? -46.584 11.712  -33.902 1.00 33.15 ? 93  GLY C CA  1 
ATOM   2821 C C   . GLY C 1 93  ? -45.281 10.910  -33.753 1.00 32.17 ? 93  GLY C C   1 
ATOM   2822 O O   . GLY C 1 93  ? -44.398 11.253  -32.932 1.00 32.18 ? 93  GLY C O   1 
ATOM   2823 N N   . VAL C 1 94  ? -45.155 9.855   -34.547 1.00 30.11 ? 94  VAL C N   1 
ATOM   2824 C CA  . VAL C 1 94  ? -43.959 9.006   -34.544 1.00 29.92 ? 94  VAL C CA  1 
ATOM   2825 C C   . VAL C 1 94  ? -42.948 9.395   -35.649 1.00 31.67 ? 94  VAL C C   1 
ATOM   2826 O O   . VAL C 1 94  ? -43.343 9.594   -36.833 1.00 31.14 ? 94  VAL C O   1 
ATOM   2827 C CB  . VAL C 1 94  ? -44.348 7.593   -34.614 1.00 28.39 ? 94  VAL C CB  1 
ATOM   2828 C CG1 . VAL C 1 94  ? -43.157 6.649   -34.399 1.00 29.28 ? 94  VAL C CG1 1 
ATOM   2829 C CG2 . VAL C 1 94  ? -45.408 7.369   -33.580 1.00 27.78 ? 94  VAL C CG2 1 
ATOM   2830 N N   . ALA C 1 95  ? -41.663 9.516   -35.218 1.00 30.71 ? 95  ALA C N   1 
ATOM   2831 C CA  . ALA C 1 95  ? -40.500 9.837   -36.036 1.00 30.09 ? 95  ALA C CA  1 
ATOM   2832 C C   . ALA C 1 95  ? -39.587 8.656   -36.018 1.00 30.63 ? 95  ALA C C   1 
ATOM   2833 O O   . ALA C 1 95  ? -39.100 8.292   -34.976 1.00 30.85 ? 95  ALA C O   1 
ATOM   2834 C CB  . ALA C 1 95  ? -39.758 11.085  -35.483 1.00 28.56 ? 95  ALA C CB  1 
ATOM   2835 N N   . ASP C 1 96  ? -39.390 8.014   -37.165 1.00 31.72 ? 96  ASP C N   1 
ATOM   2836 C CA  . ASP C 1 96  ? -38.348 6.997   -37.273 1.00 33.04 ? 96  ASP C CA  1 
ATOM   2837 C C   . ASP C 1 96  ? -37.047 7.691   -37.764 1.00 31.78 ? 96  ASP C C   1 
ATOM   2838 O O   . ASP C 1 96  ? -37.081 8.540   -38.665 1.00 32.41 ? 96  ASP C O   1 
ATOM   2839 C CB  . ASP C 1 96  ? -38.794 5.780   -38.105 1.00 33.63 ? 96  ASP C CB  1 
ATOM   2840 C CG  . ASP C 1 96  ? -39.712 4.829   -37.278 1.00 40.01 ? 96  ASP C CG  1 
ATOM   2841 O OD1 . ASP C 1 96  ? -40.997 4.896   -37.461 1.00 40.86 ? 96  ASP C OD1 1 
ATOM   2842 O OD2 . ASP C 1 96  ? -39.135 4.060   -36.416 1.00 37.91 ? 96  ASP C OD2 1 
ATOM   2843 N N   . VAL C 1 97  ? -35.941 7.422   -37.065 1.00 29.94 ? 97  VAL C N   1 
ATOM   2844 C CA  . VAL C 1 97  ? -34.716 8.185   -37.260 1.00 26.65 ? 97  VAL C CA  1 
ATOM   2845 C C   . VAL C 1 97  ? -33.746 7.278   -37.885 1.00 26.90 ? 97  VAL C C   1 
ATOM   2846 O O   . VAL C 1 97  ? -33.566 6.161   -37.386 1.00 27.17 ? 97  VAL C O   1 
ATOM   2847 C CB  . VAL C 1 97  ? -34.153 8.750   -35.942 1.00 26.99 ? 97  VAL C CB  1 
ATOM   2848 C CG1 . VAL C 1 97  ? -32.920 9.561   -36.194 1.00 22.25 ? 97  VAL C CG1 1 
ATOM   2849 C CG2 . VAL C 1 97  ? -35.226 9.617   -35.239 1.00 23.11 ? 97  VAL C CG2 1 
ATOM   2850 N N   . SER C 1 98  ? -33.167 7.745   -38.996 1.00 26.55 ? 98  SER C N   1 
ATOM   2851 C CA  . SER C 1 98  ? -31.960 7.151   -39.650 1.00 29.40 ? 98  SER C CA  1 
ATOM   2852 C C   . SER C 1 98  ? -31.024 8.242   -40.191 1.00 29.68 ? 98  SER C C   1 
ATOM   2853 O O   . SER C 1 98  ? -31.376 8.935   -41.174 1.00 29.89 ? 98  SER C O   1 
ATOM   2854 C CB  . SER C 1 98  ? -32.310 6.228   -40.820 1.00 28.89 ? 98  SER C CB  1 
ATOM   2855 O OG  . SER C 1 98  ? -31.629 4.985   -40.684 1.00 33.39 ? 98  SER C OG  1 
ATOM   2856 N N   . ILE C 1 99  ? -29.845 8.381   -39.556 1.00 28.93 ? 99  ILE C N   1 
ATOM   2857 C CA  . ILE C 1 99  ? -28.878 9.423   -39.863 1.00 29.25 ? 99  ILE C CA  1 
ATOM   2858 C C   . ILE C 1 99  ? -27.476 8.777   -39.869 1.00 29.61 ? 99  ILE C C   1 
ATOM   2859 O O   . ILE C 1 99  ? -27.196 7.880   -39.089 1.00 29.87 ? 99  ILE C O   1 
ATOM   2860 C CB  . ILE C 1 99  ? -29.018 10.636  -38.824 1.00 29.38 ? 99  ILE C CB  1 
ATOM   2861 C CG1 . ILE C 1 99  ? -30.458 11.150  -38.785 1.00 27.66 ? 99  ILE C CG1 1 
ATOM   2862 C CG2 . ILE C 1 99  ? -28.017 11.736  -39.056 1.00 28.91 ? 99  ILE C CG2 1 
ATOM   2863 C CD1 . ILE C 1 99  ? -30.811 12.162  -37.707 1.00 29.44 ? 99  ILE C CD1 1 
ATOM   2864 N N   . GLU C 1 100 ? -26.629 9.183   -40.811 1.00 30.01 ? 100 GLU C N   1 
ATOM   2865 C CA  . GLU C 1 100 ? -25.198 8.912   -40.756 1.00 30.46 ? 100 GLU C CA  1 
ATOM   2866 C C   . GLU C 1 100 ? -24.447 10.259  -40.700 1.00 29.92 ? 100 GLU C C   1 
ATOM   2867 O O   . GLU C 1 100 ? -24.697 11.124  -41.509 1.00 30.27 ? 100 GLU C O   1 
ATOM   2868 C CB  . GLU C 1 100 ? -24.764 8.123   -41.989 1.00 31.06 ? 100 GLU C CB  1 
ATOM   2869 C CG  . GLU C 1 100 ? -23.272 8.293   -42.283 1.00 32.78 ? 100 GLU C CG  1 
ATOM   2870 C CD  . GLU C 1 100 ? -22.650 7.125   -43.104 1.00 36.87 ? 100 GLU C CD  1 
ATOM   2871 O OE1 . GLU C 1 100 ? -23.008 5.942   -42.840 1.00 35.30 ? 100 GLU C OE1 1 
ATOM   2872 O OE2 . GLU C 1 100 ? -21.796 7.426   -43.984 1.00 33.94 ? 100 GLU C OE2 1 
ATOM   2873 N N   . ASP C 1 101 ? -23.562 10.456  -39.729 1.00 28.41 ? 101 ASP C N   1 
ATOM   2874 C CA  . ASP C 1 101 ? -22.829 11.717  -39.604 1.00 27.12 ? 101 ASP C CA  1 
ATOM   2875 C C   . ASP C 1 101 ? -21.316 11.387  -39.511 1.00 27.05 ? 101 ASP C C   1 
ATOM   2876 O O   . ASP C 1 101 ? -20.910 10.387  -38.878 1.00 24.29 ? 101 ASP C O   1 
ATOM   2877 C CB  . ASP C 1 101 ? -23.286 12.521  -38.381 1.00 26.41 ? 101 ASP C CB  1 
ATOM   2878 C CG  . ASP C 1 101 ? -22.888 13.984  -38.435 1.00 27.68 ? 101 ASP C CG  1 
ATOM   2879 O OD1 . ASP C 1 101 ? -23.603 14.763  -39.083 1.00 30.42 ? 101 ASP C OD1 1 
ATOM   2880 O OD2 . ASP C 1 101 ? -21.873 14.398  -37.800 1.00 28.07 ? 101 ASP C OD2 1 
ATOM   2881 N N   . SER C 1 102 ? -20.528 12.221  -40.202 1.00 25.90 ? 102 SER C N   1 
ATOM   2882 C CA  . SER C 1 102 ? -19.088 12.158  -40.193 1.00 25.96 ? 102 SER C CA  1 
ATOM   2883 C C   . SER C 1 102 ? -18.427 13.310  -39.405 1.00 24.94 ? 102 SER C C   1 
ATOM   2884 O O   . SER C 1 102 ? -17.176 13.435  -39.449 1.00 24.26 ? 102 SER C O   1 
ATOM   2885 C CB  . SER C 1 102 ? -18.567 12.152  -41.643 1.00 26.53 ? 102 SER C CB  1 
ATOM   2886 O OG  . SER C 1 102 ? -19.085 11.056  -42.358 1.00 25.95 ? 102 SER C OG  1 
ATOM   2887 N N   . VAL C 1 103 ? -19.221 14.121  -38.675 1.00 23.40 ? 103 VAL C N   1 
ATOM   2888 C CA  . VAL C 1 103 ? -18.627 15.205  -37.849 1.00 22.53 ? 103 VAL C CA  1 
ATOM   2889 C C   . VAL C 1 103 ? -18.506 14.811  -36.361 1.00 23.01 ? 103 VAL C C   1 
ATOM   2890 O O   . VAL C 1 103 ? -17.407 14.813  -35.766 1.00 22.14 ? 103 VAL C O   1 
ATOM   2891 C CB  . VAL C 1 103 ? -19.352 16.604  -38.071 1.00 23.24 ? 103 VAL C CB  1 
ATOM   2892 C CG1 . VAL C 1 103 ? -18.501 17.723  -37.571 1.00 22.65 ? 103 VAL C CG1 1 
ATOM   2893 C CG2 . VAL C 1 103 ? -19.644 16.806  -39.542 1.00 21.37 ? 103 VAL C CG2 1 
ATOM   2894 N N   . ILE C 1 104 ? -19.635 14.439  -35.771 1.00 22.33 ? 104 ILE C N   1 
ATOM   2895 C CA  . ILE C 1 104 ? -19.667 13.739  -34.481 1.00 21.25 ? 104 ILE C CA  1 
ATOM   2896 C C   . ILE C 1 104 ? -18.853 12.434  -34.490 1.00 20.80 ? 104 ILE C C   1 
ATOM   2897 O O   . ILE C 1 104 ? -18.623 11.818  -35.528 1.00 19.95 ? 104 ILE C O   1 
ATOM   2898 C CB  . ILE C 1 104 ? -21.142 13.349  -34.004 1.00 20.97 ? 104 ILE C CB  1 
ATOM   2899 C CG1 . ILE C 1 104 ? -21.679 12.122  -34.758 1.00 22.03 ? 104 ILE C CG1 1 
ATOM   2900 C CG2 . ILE C 1 104 ? -22.093 14.538  -34.044 1.00 19.01 ? 104 ILE C CG2 1 
ATOM   2901 C CD1 . ILE C 1 104 ? -23.115 11.728  -34.414 1.00 21.42 ? 104 ILE C CD1 1 
ATOM   2902 N N   . SER C 1 105 ? -18.471 12.033  -33.289 1.00 20.20 ? 105 SER C N   1 
ATOM   2903 C CA  . SER C 1 105 ? -17.724 10.842  -33.076 1.00 20.43 ? 105 SER C CA  1 
ATOM   2904 C C   . SER C 1 105 ? -18.062 10.297  -31.719 1.00 20.03 ? 105 SER C C   1 
ATOM   2905 O O   . SER C 1 105 ? -18.640 10.977  -30.905 1.00 19.75 ? 105 SER C O   1 
ATOM   2906 C CB  . SER C 1 105 ? -16.230 11.171  -33.207 1.00 21.44 ? 105 SER C CB  1 
ATOM   2907 O OG  . SER C 1 105 ? -15.532 9.973   -33.329 1.00 21.46 ? 105 SER C OG  1 
ATOM   2908 N N   . LEU C 1 106 ? -17.802 9.026   -31.520 1.00 19.31 ? 106 LEU C N   1 
ATOM   2909 C CA  . LEU C 1 106 ? -17.947 8.424   -30.239 1.00 20.06 ? 106 LEU C CA  1 
ATOM   2910 C C   . LEU C 1 106 ? -16.568 8.401   -29.453 1.00 19.78 ? 106 LEU C C   1 
ATOM   2911 O O   . LEU C 1 106 ? -16.498 7.821   -28.417 1.00 20.03 ? 106 LEU C O   1 
ATOM   2912 C CB  . LEU C 1 106 ? -18.578 6.982   -30.370 1.00 21.25 ? 106 LEU C CB  1 
ATOM   2913 C CG  . LEU C 1 106 ? -20.017 6.804   -30.927 1.00 20.88 ? 106 LEU C CG  1 
ATOM   2914 C CD1 . LEU C 1 106 ? -20.540 5.345   -30.689 1.00 18.95 ? 106 LEU C CD1 1 
ATOM   2915 C CD2 . LEU C 1 106 ? -21.005 7.836   -30.330 1.00 20.14 ? 106 LEU C CD2 1 
ATOM   2916 N N   . SER C 1 107 ? -15.523 9.065   -29.965 1.00 19.47 ? 107 SER C N   1 
ATOM   2917 C CA  . SER C 1 107 ? -14.272 9.275   -29.278 1.00 19.47 ? 107 SER C CA  1 
ATOM   2918 C C   . SER C 1 107 ? -13.485 10.497  -29.798 1.00 19.59 ? 107 SER C C   1 
ATOM   2919 O O   . SER C 1 107 ? -13.753 11.012  -30.883 1.00 19.15 ? 107 SER C O   1 
ATOM   2920 C CB  . SER C 1 107 ? -13.412 8.015   -29.369 1.00 18.94 ? 107 SER C CB  1 
ATOM   2921 O OG  . SER C 1 107 ? -13.062 7.769   -30.716 1.00 22.57 ? 107 SER C OG  1 
ATOM   2922 N N   . GLY C 1 108 ? -12.502 10.948  -29.028 1.00 20.51 ? 108 GLY C N   1 
ATOM   2923 C CA  . GLY C 1 108 ? -11.646 12.037  -29.458 1.00 23.55 ? 108 GLY C CA  1 
ATOM   2924 C C   . GLY C 1 108 ? -12.291 13.368  -29.204 1.00 25.60 ? 108 GLY C C   1 
ATOM   2925 O O   . GLY C 1 108 ? -13.270 13.457  -28.461 1.00 26.49 ? 108 GLY C O   1 
ATOM   2926 N N   . ASP C 1 109 ? -11.771 14.402  -29.857 1.00 28.70 ? 109 ASP C N   1 
ATOM   2927 C CA  . ASP C 1 109 ? -12.192 15.817  -29.654 1.00 30.62 ? 109 ASP C CA  1 
ATOM   2928 C C   . ASP C 1 109 ? -13.663 16.087  -30.011 1.00 28.99 ? 109 ASP C C   1 
ATOM   2929 O O   . ASP C 1 109 ? -14.348 16.983  -29.434 1.00 30.25 ? 109 ASP C O   1 
ATOM   2930 C CB  . ASP C 1 109 ? -11.249 16.753  -30.466 1.00 32.80 ? 109 ASP C CB  1 
ATOM   2931 C CG  . ASP C 1 109 ? -9.985  17.207  -29.649 1.00 39.51 ? 109 ASP C CG  1 
ATOM   2932 O OD1 . ASP C 1 109 ? -9.009  17.723  -30.254 1.00 43.57 ? 109 ASP C OD1 1 
ATOM   2933 O OD2 . ASP C 1 109 ? -9.967  17.065  -28.387 1.00 47.34 ? 109 ASP C OD2 1 
ATOM   2934 N N   . HIS C 1 110 ? -14.155 15.301  -30.949 1.00 28.78 ? 110 HIS C N   1 
ATOM   2935 C CA  . HIS C 1 110 ? -15.578 15.354  -31.378 1.00 27.42 ? 110 HIS C CA  1 
ATOM   2936 C C   . HIS C 1 110 ? -16.485 14.330  -30.719 1.00 26.08 ? 110 HIS C C   1 
ATOM   2937 O O   . HIS C 1 110 ? -17.538 14.045  -31.258 1.00 27.47 ? 110 HIS C O   1 
ATOM   2938 C CB  . HIS C 1 110 ? -15.646 15.133  -32.872 1.00 27.47 ? 110 HIS C CB  1 
ATOM   2939 C CG  . HIS C 1 110 ? -15.242 16.310  -33.691 1.00 24.75 ? 110 HIS C CG  1 
ATOM   2940 N ND1 . HIS C 1 110 ? -15.509 16.378  -35.038 1.00 24.32 ? 110 HIS C ND1 1 
ATOM   2941 C CD2 . HIS C 1 110 ? -14.646 17.478  -33.371 1.00 26.66 ? 110 HIS C CD2 1 
ATOM   2942 C CE1 . HIS C 1 110 ? -15.086 17.524  -35.521 1.00 23.13 ? 110 HIS C CE1 1 
ATOM   2943 N NE2 . HIS C 1 110 ? -14.553 18.212  -34.534 1.00 27.71 ? 110 HIS C NE2 1 
ATOM   2944 N N   . CYS C 1 111 ? -16.075 13.769  -29.571 1.00 25.30 ? 111 CYS C N   1 
ATOM   2945 C CA  . CYS C 1 111 ? -16.854 12.783  -28.813 1.00 23.05 ? 111 CYS C CA  1 
ATOM   2946 C C   . CYS C 1 111 ? -18.129 13.416  -28.265 1.00 22.79 ? 111 CYS C C   1 
ATOM   2947 O O   . CYS C 1 111 ? -18.121 14.542  -27.743 1.00 21.47 ? 111 CYS C O   1 
ATOM   2948 C CB  . CYS C 1 111 ? -16.041 12.276  -27.643 1.00 22.65 ? 111 CYS C CB  1 
ATOM   2949 S SG  . CYS C 1 111 ? -16.705 10.811  -26.761 1.00 24.56 ? 111 CYS C SG  1 
ATOM   2950 N N   . ILE C 1 112 ? -19.222 12.658  -28.315 1.00 21.77 ? 112 ILE C N   1 
ATOM   2951 C CA  . ILE C 1 112 ? -20.542 13.188  -27.916 1.00 20.71 ? 112 ILE C CA  1 
ATOM   2952 C C   . ILE C 1 112 ? -21.107 12.467  -26.699 1.00 20.38 ? 112 ILE C C   1 
ATOM   2953 O O   . ILE C 1 112 ? -22.056 12.932  -26.100 1.00 19.84 ? 112 ILE C O   1 
ATOM   2954 C CB  . ILE C 1 112 ? -21.549 13.175  -29.113 1.00 20.42 ? 112 ILE C CB  1 
ATOM   2955 C CG1 . ILE C 1 112 ? -21.847 11.742  -29.561 1.00 20.15 ? 112 ILE C CG1 1 
ATOM   2956 C CG2 . ILE C 1 112 ? -21.008 13.999  -30.237 1.00 19.72 ? 112 ILE C CG2 1 
ATOM   2957 C CD1 . ILE C 1 112 ? -22.988 11.598  -30.465 1.00 20.52 ? 112 ILE C CD1 1 
ATOM   2958 N N   . ILE C 1 113 ? -20.533 11.321  -26.360 1.00 19.59 ? 113 ILE C N   1 
ATOM   2959 C CA  . ILE C 1 113 ? -20.769 10.700  -25.106 1.00 19.69 ? 113 ILE C CA  1 
ATOM   2960 C C   . ILE C 1 113 ? -20.523 11.593  -23.891 1.00 18.18 ? 113 ILE C C   1 
ATOM   2961 O O   . ILE C 1 113 ? -19.497 12.276  -23.806 1.00 18.66 ? 113 ILE C O   1 
ATOM   2962 C CB  . ILE C 1 113 ? -19.922 9.419   -24.975 1.00 21.72 ? 113 ILE C CB  1 
ATOM   2963 C CG1 . ILE C 1 113 ? -20.492 8.345   -25.906 1.00 20.22 ? 113 ILE C CG1 1 
ATOM   2964 C CG2 . ILE C 1 113 ? -19.950 8.932   -23.507 1.00 20.58 ? 113 ILE C CG2 1 
ATOM   2965 C CD1 . ILE C 1 113 ? -19.489 7.612   -26.638 1.00 26.00 ? 113 ILE C CD1 1 
ATOM   2966 N N   . GLY C 1 114 ? -21.485 11.574  -22.965 1.00 17.16 ? 114 GLY C N   1 
ATOM   2967 C CA  . GLY C 1 114 ? -21.471 12.420  -21.808 1.00 14.90 ? 114 GLY C CA  1 
ATOM   2968 C C   . GLY C 1 114 ? -22.052 13.778  -22.187 1.00 16.26 ? 114 GLY C C   1 
ATOM   2969 O O   . GLY C 1 114 ? -22.205 14.576  -21.321 1.00 15.24 ? 114 GLY C O   1 
ATOM   2970 N N   . ARG C 1 115 ? -22.437 14.028  -23.456 1.00 15.65 ? 115 ARG C N   1 
ATOM   2971 C CA  . ARG C 1 115 ? -23.231 15.238  -23.789 1.00 16.64 ? 115 ARG C CA  1 
ATOM   2972 C C   . ARG C 1 115 ? -24.718 14.926  -23.897 1.00 16.86 ? 115 ARG C C   1 
ATOM   2973 O O   . ARG C 1 115 ? -25.111 13.800  -23.578 1.00 18.44 ? 115 ARG C O   1 
ATOM   2974 C CB  . ARG C 1 115 ? -22.656 15.907  -25.042 1.00 15.91 ? 115 ARG C CB  1 
ATOM   2975 C CG  . ARG C 1 115 ? -21.201 16.223  -24.786 1.00 15.67 ? 115 ARG C CG  1 
ATOM   2976 C CD  . ARG C 1 115 ? -20.399 16.622  -25.959 1.00 19.52 ? 115 ARG C CD  1 
ATOM   2977 N NE  . ARG C 1 115 ? -18.971 16.632  -25.610 1.00 23.75 ? 115 ARG C NE  1 
ATOM   2978 C CZ  . ARG C 1 115 ? -18.316 17.517  -24.842 1.00 24.09 ? 115 ARG C CZ  1 
ATOM   2979 N NH1 . ARG C 1 115 ? -18.877 18.598  -24.264 1.00 22.80 ? 115 ARG C NH1 1 
ATOM   2980 N NH2 . ARG C 1 115 ? -17.012 17.346  -24.702 1.00 26.90 ? 115 ARG C NH2 1 
ATOM   2981 N N   . THR C 1 116 ? -25.538 15.884  -24.367 1.00 16.44 ? 116 THR C N   1 
ATOM   2982 C CA  . THR C 1 116 ? -27.028 15.685  -24.449 1.00 16.53 ? 116 THR C CA  1 
ATOM   2983 C C   . THR C 1 116 ? -27.596 15.684  -25.876 1.00 16.30 ? 116 THR C C   1 
ATOM   2984 O O   . THR C 1 116 ? -27.294 16.578  -26.620 1.00 17.14 ? 116 THR C O   1 
ATOM   2985 C CB  . THR C 1 116 ? -27.785 16.778  -23.617 1.00 15.48 ? 116 THR C CB  1 
ATOM   2986 O OG1 . THR C 1 116 ? -27.426 16.615  -22.256 1.00 21.53 ? 116 THR C OG1 1 
ATOM   2987 C CG2 . THR C 1 116 ? -29.356 16.671  -23.648 1.00 14.98 ? 116 THR C CG2 1 
ATOM   2988 N N   . LEU C 1 117 ? -28.462 14.751  -26.215 1.00 14.81 ? 117 LEU C N   1 
ATOM   2989 C CA  . LEU C 1 117 ? -29.254 14.852  -27.513 1.00 15.52 ? 117 LEU C CA  1 
ATOM   2990 C C   . LEU C 1 117 ? -30.631 15.495  -27.291 1.00 16.49 ? 117 LEU C C   1 
ATOM   2991 O O   . LEU C 1 117 ? -31.388 15.060  -26.418 1.00 14.37 ? 117 LEU C O   1 
ATOM   2992 C CB  . LEU C 1 117 ? -29.431 13.476  -28.138 1.00 15.54 ? 117 LEU C CB  1 
ATOM   2993 C CG  . LEU C 1 117 ? -30.220 13.311  -29.449 1.00 14.71 ? 117 LEU C CG  1 
ATOM   2994 C CD1 . LEU C 1 117 ? -29.437 13.867  -30.595 1.00 19.22 ? 117 LEU C CD1 1 
ATOM   2995 C CD2 . LEU C 1 117 ? -30.472 11.857  -29.593 1.00 19.08 ? 117 LEU C CD2 1 
ATOM   2996 N N   . VAL C 1 118 ? -30.915 16.596  -28.022 1.00 17.25 ? 118 VAL C N   1 
ATOM   2997 C CA  . VAL C 1 118 ? -32.181 17.337  -27.868 1.00 16.32 ? 118 VAL C CA  1 
ATOM   2998 C C   . VAL C 1 118 ? -33.021 17.271  -29.141 1.00 17.68 ? 118 VAL C C   1 
ATOM   2999 O O   . VAL C 1 118 ? -32.502 17.323  -30.244 1.00 18.91 ? 118 VAL C O   1 
ATOM   3000 C CB  . VAL C 1 118 ? -31.981 18.879  -27.438 1.00 15.17 ? 118 VAL C CB  1 
ATOM   3001 C CG1 . VAL C 1 118 ? -33.326 19.496  -27.006 1.00 16.05 ? 118 VAL C CG1 1 
ATOM   3002 C CG2 . VAL C 1 118 ? -31.115 19.036  -26.306 1.00 14.89 ? 118 VAL C CG2 1 
ATOM   3003 N N   . VAL C 1 119 ? -34.322 17.137  -28.964 1.00 19.66 ? 119 VAL C N   1 
ATOM   3004 C CA  . VAL C 1 119 ? -35.313 17.246  -30.013 1.00 22.29 ? 119 VAL C CA  1 
ATOM   3005 C C   . VAL C 1 119 ? -36.116 18.533  -29.762 1.00 24.16 ? 119 VAL C C   1 
ATOM   3006 O O   . VAL C 1 119 ? -36.622 18.784  -28.645 1.00 23.99 ? 119 VAL C O   1 
ATOM   3007 C CB  . VAL C 1 119 ? -36.185 15.934  -30.208 1.00 22.51 ? 119 VAL C CB  1 
ATOM   3008 C CG1 . VAL C 1 119 ? -37.006 15.638  -29.045 1.00 22.99 ? 119 VAL C CG1 1 
ATOM   3009 C CG2 . VAL C 1 119 ? -37.100 16.029  -31.456 1.00 23.40 ? 119 VAL C CG2 1 
ATOM   3010 N N   . HIS C 1 120 ? -36.163 19.378  -30.780 1.00 25.60 ? 120 HIS C N   1 
ATOM   3011 C CA  . HIS C 1 120 ? -36.703 20.715  -30.631 1.00 28.62 ? 120 HIS C CA  1 
ATOM   3012 C C   . HIS C 1 120 ? -38.122 20.814  -31.230 1.00 30.11 ? 120 HIS C C   1 
ATOM   3013 O O   . HIS C 1 120 ? -38.599 19.945  -31.968 1.00 30.34 ? 120 HIS C O   1 
ATOM   3014 C CB  . HIS C 1 120 ? -35.767 21.759  -31.263 1.00 26.93 ? 120 HIS C CB  1 
ATOM   3015 C CG  . HIS C 1 120 ? -34.404 21.811  -30.640 1.00 27.36 ? 120 HIS C CG  1 
ATOM   3016 N ND1 . HIS C 1 120 ? -33.998 22.845  -29.831 1.00 23.52 ? 120 HIS C ND1 1 
ATOM   3017 C CD2 . HIS C 1 120 ? -33.335 20.982  -30.741 1.00 25.99 ? 120 HIS C CD2 1 
ATOM   3018 C CE1 . HIS C 1 120 ? -32.750 22.657  -29.454 1.00 24.27 ? 120 HIS C CE1 1 
ATOM   3019 N NE2 . HIS C 1 120 ? -32.326 21.532  -29.991 1.00 25.12 ? 120 HIS C NE2 1 
ATOM   3020 N N   . GLU C 1 121 ? -38.775 21.901  -30.886 1.00 33.38 ? 121 GLU C N   1 
ATOM   3021 C CA  . GLU C 1 121 ? -40.181 22.139  -31.233 1.00 35.95 ? 121 GLU C CA  1 
ATOM   3022 C C   . GLU C 1 121 ? -40.413 22.442  -32.730 1.00 36.14 ? 121 GLU C C   1 
ATOM   3023 O O   . GLU C 1 121 ? -41.416 22.016  -33.322 1.00 36.09 ? 121 GLU C O   1 
ATOM   3024 C CB  . GLU C 1 121 ? -40.720 23.307  -30.405 1.00 35.24 ? 121 GLU C CB  1 
ATOM   3025 C CG  . GLU C 1 121 ? -42.222 23.382  -30.363 1.00 38.33 ? 121 GLU C CG  1 
ATOM   3026 C CD  . GLU C 1 121 ? -42.688 24.696  -29.790 1.00 44.23 ? 121 GLU C CD  1 
ATOM   3027 O OE1 . GLU C 1 121 ? -43.913 24.840  -29.544 1.00 48.16 ? 121 GLU C OE1 1 
ATOM   3028 O OE2 . GLU C 1 121 ? -41.831 25.576  -29.580 1.00 44.74 ? 121 GLU C OE2 1 
ATOM   3029 N N   . LYS C 1 122 ? -39.500 23.210  -33.294 1.00 36.82 ? 122 LYS C N   1 
ATOM   3030 C CA  . LYS C 1 122 ? -39.633 23.715  -34.637 1.00 38.26 ? 122 LYS C CA  1 
ATOM   3031 C C   . LYS C 1 122 ? -38.538 23.074  -35.479 1.00 37.88 ? 122 LYS C C   1 
ATOM   3032 O O   . LYS C 1 122 ? -37.603 22.445  -34.938 1.00 37.64 ? 122 LYS C O   1 
ATOM   3033 C CB  . LYS C 1 122 ? -39.445 25.243  -34.659 1.00 38.67 ? 122 LYS C CB  1 
ATOM   3034 C CG  . LYS C 1 122 ? -40.433 26.058  -33.813 1.00 40.10 ? 122 LYS C CG  1 
ATOM   3035 C CD  . LYS C 1 122 ? -40.116 27.544  -33.869 1.00 41.47 ? 122 LYS C CD  1 
ATOM   3036 C CE  . LYS C 1 122 ? -40.706 28.191  -35.157 1.00 46.71 ? 122 LYS C CE  1 
ATOM   3037 N NZ  . LYS C 1 122 ? -40.003 29.462  -35.571 1.00 48.16 ? 122 LYS C NZ  1 
ATOM   3038 N N   . ALA C 1 123 ? -38.662 23.255  -36.786 1.00 37.29 ? 123 ALA C N   1 
ATOM   3039 C CA  . ALA C 1 123 ? -37.745 22.699  -37.767 1.00 38.81 ? 123 ALA C CA  1 
ATOM   3040 C C   . ALA C 1 123 ? -36.506 23.557  -37.741 1.00 40.08 ? 123 ALA C C   1 
ATOM   3041 O O   . ALA C 1 123 ? -36.543 24.744  -37.307 1.00 41.23 ? 123 ALA C O   1 
ATOM   3042 C CB  . ALA C 1 123 ? -38.387 22.655  -39.191 1.00 37.66 ? 123 ALA C CB  1 
ATOM   3043 N N   . ASP C 1 124 ? -35.393 22.964  -38.157 1.00 41.33 ? 124 ASP C N   1 
ATOM   3044 C CA  . ASP C 1 124 ? -34.162 23.730  -38.267 1.00 43.16 ? 124 ASP C CA  1 
ATOM   3045 C C   . ASP C 1 124 ? -34.117 24.394  -39.668 1.00 43.29 ? 124 ASP C C   1 
ATOM   3046 O O   . ASP C 1 124 ? -35.134 24.865  -40.203 1.00 42.25 ? 124 ASP C O   1 
ATOM   3047 C CB  . ASP C 1 124 ? -32.951 22.818  -38.041 1.00 43.98 ? 124 ASP C CB  1 
ATOM   3048 C CG  . ASP C 1 124 ? -31.771 23.538  -37.400 1.00 47.41 ? 124 ASP C CG  1 
ATOM   3049 O OD1 . ASP C 1 124 ? -31.781 23.780  -36.155 1.00 48.66 ? 124 ASP C OD1 1 
ATOM   3050 O OD2 . ASP C 1 124 ? -30.808 23.834  -38.151 1.00 51.18 ? 124 ASP C OD2 1 
ATOM   3051 N N   . SER C 1 142 ? -38.075 26.085  -27.915 1.00 31.94 ? 142 SER C N   1 
ATOM   3052 C CA  . SER C 1 142 ? -38.377 25.126  -26.864 1.00 31.79 ? 142 SER C CA  1 
ATOM   3053 C C   . SER C 1 142 ? -37.759 23.718  -27.078 1.00 31.30 ? 142 SER C C   1 
ATOM   3054 O O   . SER C 1 142 ? -37.821 23.135  -28.182 1.00 31.26 ? 142 SER C O   1 
ATOM   3055 C CB  . SER C 1 142 ? -39.898 25.080  -26.676 1.00 32.23 ? 142 SER C CB  1 
ATOM   3056 O OG  . SER C 1 142 ? -40.310 24.146  -25.690 1.00 34.34 ? 142 SER C OG  1 
ATOM   3057 N N   . ARG C 1 143 ? -37.202 23.168  -25.988 1.00 30.32 ? 143 ARG C N   1 
ATOM   3058 C CA  . ARG C 1 143 ? -36.513 21.888  -26.019 1.00 29.27 ? 143 ARG C CA  1 
ATOM   3059 C C   . ARG C 1 143 ? -37.429 20.840  -25.453 1.00 28.22 ? 143 ARG C C   1 
ATOM   3060 O O   . ARG C 1 143 ? -37.861 20.955  -24.323 1.00 29.61 ? 143 ARG C O   1 
ATOM   3061 C CB  . ARG C 1 143 ? -35.210 21.935  -25.226 1.00 28.12 ? 143 ARG C CB  1 
ATOM   3062 C CG  . ARG C 1 143 ? -34.179 22.843  -25.847 1.00 25.60 ? 143 ARG C CG  1 
ATOM   3063 C CD  . ARG C 1 143 ? -33.022 23.027  -24.906 1.00 25.57 ? 143 ARG C CD  1 
ATOM   3064 N NE  . ARG C 1 143 ? -32.081 23.968  -25.480 1.00 21.19 ? 143 ARG C NE  1 
ATOM   3065 C CZ  . ARG C 1 143 ? -30.889 24.287  -24.994 1.00 21.84 ? 143 ARG C CZ  1 
ATOM   3066 N NH1 . ARG C 1 143 ? -30.473 23.738  -23.904 1.00 24.04 ? 143 ARG C NH1 1 
ATOM   3067 N NH2 . ARG C 1 143 ? -30.116 25.186  -25.626 1.00 26.92 ? 143 ARG C NH2 1 
ATOM   3068 N N   . LEU C 1 144 ? -37.723 19.810  -26.228 1.00 25.91 ? 144 LEU C N   1 
ATOM   3069 C CA  . LEU C 1 144 ? -38.954 19.074  -26.005 1.00 24.44 ? 144 LEU C CA  1 
ATOM   3070 C C   . LEU C 1 144 ? -38.722 17.777  -25.281 1.00 24.55 ? 144 LEU C C   1 
ATOM   3071 O O   . LEU C 1 144 ? -39.610 17.257  -24.601 1.00 24.02 ? 144 LEU C O   1 
ATOM   3072 C CB  . LEU C 1 144 ? -39.596 18.785  -27.341 1.00 25.10 ? 144 LEU C CB  1 
ATOM   3073 C CG  . LEU C 1 144 ? -40.272 19.812  -28.238 1.00 25.16 ? 144 LEU C CG  1 
ATOM   3074 C CD1 . LEU C 1 144 ? -41.325 19.026  -28.983 1.00 25.82 ? 144 LEU C CD1 1 
ATOM   3075 C CD2 . LEU C 1 144 ? -40.897 21.075  -27.509 1.00 26.35 ? 144 LEU C CD2 1 
ATOM   3076 N N   . ALA C 1 145 ? -37.534 17.217  -25.533 1.00 22.92 ? 145 ALA C N   1 
ATOM   3077 C CA  . ALA C 1 145 ? -37.070 16.008  -24.941 1.00 21.84 ? 145 ALA C CA  1 
ATOM   3078 C C   . ALA C 1 145 ? -35.576 15.964  -25.202 1.00 21.22 ? 145 ALA C C   1 
ATOM   3079 O O   . ALA C 1 145 ? -35.093 16.376  -26.262 1.00 21.19 ? 145 ALA C O   1 
ATOM   3080 C CB  . ALA C 1 145 ? -37.738 14.838  -25.579 1.00 22.82 ? 145 ALA C CB  1 
ATOM   3081 N N   . CYS C 1 146 ? -34.832 15.545  -24.201 1.00 21.30 ? 146 CYS C N   1 
ATOM   3082 C CA  . CYS C 1 146 ? -33.407 15.430  -24.315 1.00 20.67 ? 146 CYS C CA  1 
ATOM   3083 C C   . CYS C 1 146 ? -33.057 14.186  -23.538 1.00 19.31 ? 146 CYS C C   1 
ATOM   3084 O O   . CYS C 1 146 ? -33.838 13.754  -22.730 1.00 17.45 ? 146 CYS C O   1 
ATOM   3085 C CB  . CYS C 1 146 ? -32.707 16.621  -23.645 1.00 22.46 ? 146 CYS C CB  1 
ATOM   3086 S SG  . CYS C 1 146 ? -33.302 17.119  -21.960 1.00 28.33 ? 146 CYS C SG  1 
ATOM   3087 N N   . GLY C 1 147 ? -31.841 13.675  -23.737 1.00 16.31 ? 147 GLY C N   1 
ATOM   3088 C CA  . GLY C 1 147 ? -31.203 12.927  -22.700 1.00 14.71 ? 147 GLY C CA  1 
ATOM   3089 C C   . GLY C 1 147 ? -29.681 12.903  -22.872 1.00 15.72 ? 147 GLY C C   1 
ATOM   3090 O O   . GLY C 1 147 ? -29.151 13.305  -23.941 1.00 13.42 ? 147 GLY C O   1 
ATOM   3091 N N   . VAL C 1 148 ? -29.016 12.370  -21.822 1.00 14.83 ? 148 VAL C N   1 
ATOM   3092 C CA  . VAL C 1 148 ? -27.577 12.143  -21.845 1.00 17.82 ? 148 VAL C CA  1 
ATOM   3093 C C   . VAL C 1 148 ? -27.196 10.922  -22.685 1.00 17.94 ? 148 VAL C C   1 
ATOM   3094 O O   . VAL C 1 148 ? -27.789 9.812   -22.525 1.00 18.14 ? 148 VAL C O   1 
ATOM   3095 C CB  . VAL C 1 148 ? -26.966 11.930  -20.423 1.00 15.88 ? 148 VAL C CB  1 
ATOM   3096 C CG1 . VAL C 1 148 ? -25.421 12.054  -20.454 1.00 16.86 ? 148 VAL C CG1 1 
ATOM   3097 C CG2 . VAL C 1 148 ? -27.578 12.836  -19.502 1.00 17.30 ? 148 VAL C CG2 1 
ATOM   3098 N N   . ILE C 1 149 ? -26.203 11.155  -23.559 1.00 18.92 ? 149 ILE C N   1 
ATOM   3099 C CA  . ILE C 1 149 ? -25.655 10.128  -24.395 1.00 18.08 ? 149 ILE C CA  1 
ATOM   3100 C C   . ILE C 1 149 ? -24.639 9.367   -23.594 1.00 18.67 ? 149 ILE C C   1 
ATOM   3101 O O   . ILE C 1 149 ? -23.635 9.932   -23.086 1.00 17.90 ? 149 ILE C O   1 
ATOM   3102 C CB  . ILE C 1 149 ? -25.037 10.690  -25.703 1.00 20.24 ? 149 ILE C CB  1 
ATOM   3103 C CG1 . ILE C 1 149 ? -26.092 11.534  -26.453 1.00 18.25 ? 149 ILE C CG1 1 
ATOM   3104 C CG2 . ILE C 1 149 ? -24.458 9.489   -26.594 1.00 11.86 ? 149 ILE C CG2 1 
ATOM   3105 C CD1 . ILE C 1 149 ? -25.489 12.593  -27.390 1.00 14.95 ? 149 ILE C CD1 1 
ATOM   3106 N N   . GLY C 1 150 ? -24.899 8.071   -23.497 1.00 17.17 ? 150 GLY C N   1 
ATOM   3107 C CA  . GLY C 1 150 ? -24.115 7.215   -22.686 1.00 19.22 ? 150 GLY C CA  1 
ATOM   3108 C C   . GLY C 1 150 ? -23.594 6.018   -23.465 1.00 19.87 ? 150 GLY C C   1 
ATOM   3109 O O   . GLY C 1 150 ? -24.098 5.707   -24.509 1.00 18.59 ? 150 GLY C O   1 
ATOM   3110 N N   . ILE C 1 151 ? -22.537 5.412   -22.936 1.00 21.09 ? 151 ILE C N   1 
ATOM   3111 C CA  . ILE C 1 151 ? -21.935 4.159   -23.424 1.00 22.37 ? 151 ILE C CA  1 
ATOM   3112 C C   . ILE C 1 151 ? -22.943 2.981   -23.350 1.00 22.53 ? 151 ILE C C   1 
ATOM   3113 O O   . ILE C 1 151 ? -23.569 2.763   -22.312 1.00 17.27 ? 151 ILE C O   1 
ATOM   3114 C CB  . ILE C 1 151 ? -20.667 3.810   -22.611 1.00 23.15 ? 151 ILE C CB  1 
ATOM   3115 C CG1 . ILE C 1 151 ? -19.647 4.957   -22.688 1.00 22.29 ? 151 ILE C CG1 1 
ATOM   3116 C CG2 . ILE C 1 151 ? -20.027 2.556   -23.141 1.00 21.28 ? 151 ILE C CG2 1 
ATOM   3117 C CD1 . ILE C 1 151 ? -18.630 4.998   -21.455 1.00 21.74 ? 151 ILE C CD1 1 
ATOM   3118 N N   . ALA C 1 152 ? -23.057 2.231   -24.466 1.00 23.97 ? 152 ALA C N   1 
ATOM   3119 C CA  . ALA C 1 152 ? -24.000 1.077   -24.556 1.00 25.97 ? 152 ALA C CA  1 
ATOM   3120 C C   . ALA C 1 152 ? -23.303 -0.244  -24.784 1.00 27.70 ? 152 ALA C C   1 
ATOM   3121 O O   . ALA C 1 152 ? -22.219 -0.281  -25.341 1.00 27.40 ? 152 ALA C O   1 
ATOM   3122 C CB  . ALA C 1 152 ? -24.982 1.326   -25.677 1.00 25.01 ? 152 ALA C CB  1 
ATOM   3123 N N   . GLN C 1 153 ? -23.921 -1.352  -24.391 1.00 30.59 ? 153 GLN C N   1 
ATOM   3124 C CA  . GLN C 1 153 ? -23.255 -2.655  -24.600 1.00 33.45 ? 153 GLN C CA  1 
ATOM   3125 C C   . GLN C 1 153 ? -23.076 -3.219  -26.039 1.00 35.10 ? 153 GLN C C   1 
ATOM   3126 O O   . GLN C 1 153 ? -23.988 -3.686  -26.749 1.00 36.08 ? 153 GLN C O   1 
ATOM   3127 C CB  . GLN C 1 153 ? -23.735 -3.751  -23.677 1.00 32.89 ? 153 GLN C CB  1 
ATOM   3128 C CG  . GLN C 1 153 ? -22.537 -4.761  -23.509 1.00 36.73 ? 153 GLN C CG  1 
ATOM   3129 C CD  . GLN C 1 153 ? -22.737 -5.877  -22.452 1.00 35.47 ? 153 GLN C CD  1 
ATOM   3130 O OE1 . GLN C 1 153 ? -23.833 -6.041  -21.888 1.00 33.46 ? 153 GLN C OE1 1 
ATOM   3131 N NE2 . GLN C 1 153 ? -21.681 -6.683  -22.251 1.00 34.59 ? 153 GLN C NE2 1 
ATOM   3132 O OXT . GLN C 1 153 ? -21.928 -3.260  -26.514 1.00 35.87 ? 153 GLN C OXT 1 
ATOM   3133 N N   . ALA D 1 1   ? -10.256 21.968  -15.307 1.00 41.99 ? 1   ALA D N   1 
ATOM   3134 C CA  . ALA D 1 1   ? -10.418 20.855  -14.323 1.00 41.80 ? 1   ALA D CA  1 
ATOM   3135 C C   . ALA D 1 1   ? -11.844 20.290  -14.379 1.00 40.89 ? 1   ALA D C   1 
ATOM   3136 O O   . ALA D 1 1   ? -12.813 21.002  -14.154 1.00 41.70 ? 1   ALA D O   1 
ATOM   3137 C CB  . ALA D 1 1   ? -10.056 21.335  -12.901 1.00 42.15 ? 1   ALA D CB  1 
ATOM   3138 N N   . THR D 1 2   ? -11.974 19.009  -14.691 1.00 40.52 ? 2   THR D N   1 
ATOM   3139 C CA  . THR D 1 2   ? -13.234 18.559  -15.281 1.00 39.18 ? 2   THR D CA  1 
ATOM   3140 C C   . THR D 1 2   ? -14.327 18.285  -14.237 1.00 37.51 ? 2   THR D C   1 
ATOM   3141 O O   . THR D 1 2   ? -14.078 18.030  -13.045 1.00 36.65 ? 2   THR D O   1 
ATOM   3142 C CB  . THR D 1 2   ? -13.036 17.562  -16.536 1.00 39.36 ? 2   THR D CB  1 
ATOM   3143 O OG1 . THR D 1 2   ? -14.218 16.768  -16.837 1.00 42.60 ? 2   THR D OG1 1 
ATOM   3144 C CG2 . THR D 1 2   ? -11.844 16.687  -16.373 1.00 37.35 ? 2   THR D CG2 1 
ATOM   3145 N N   . LYS D 1 3   ? -15.544 18.499  -14.712 1.00 35.88 ? 3   LYS D N   1 
ATOM   3146 C CA  . LYS D 1 3   ? -16.747 18.447  -13.932 1.00 33.42 ? 3   LYS D CA  1 
ATOM   3147 C C   . LYS D 1 3   ? -17.714 17.498  -14.654 1.00 31.19 ? 3   LYS D C   1 
ATOM   3148 O O   . LYS D 1 3   ? -17.724 17.401  -15.873 1.00 30.26 ? 3   LYS D O   1 
ATOM   3149 C CB  . LYS D 1 3   ? -17.310 19.851  -13.761 1.00 33.59 ? 3   LYS D CB  1 
ATOM   3150 C CG  . LYS D 1 3   ? -16.431 20.708  -12.838 1.00 35.83 ? 3   LYS D CG  1 
ATOM   3151 C CD  . LYS D 1 3   ? -16.752 22.209  -12.923 1.00 40.80 ? 3   LYS D CD  1 
ATOM   3152 C CE  . LYS D 1 3   ? -15.671 23.075  -12.231 1.00 41.57 ? 3   LYS D CE  1 
ATOM   3153 N NZ  . LYS D 1 3   ? -16.026 24.548  -12.281 1.00 41.71 ? 3   LYS D NZ  1 
ATOM   3154 N N   . ALA D 1 4   ? -18.491 16.762  -13.881 1.00 28.07 ? 4   ALA D N   1 
ATOM   3155 C CA  . ALA D 1 4   ? -19.545 15.938  -14.438 1.00 25.00 ? 4   ALA D CA  1 
ATOM   3156 C C   . ALA D 1 4   ? -20.764 16.024  -13.507 1.00 23.21 ? 4   ALA D C   1 
ATOM   3157 O O   . ALA D 1 4   ? -20.656 16.587  -12.382 1.00 23.98 ? 4   ALA D O   1 
ATOM   3158 C CB  . ALA D 1 4   ? -19.049 14.496  -14.620 1.00 22.65 ? 4   ALA D CB  1 
ATOM   3159 N N   . VAL D 1 5   ? -21.909 15.512  -13.977 1.00 21.05 ? 5   VAL D N   1 
ATOM   3160 C CA  . VAL D 1 5   ? -23.178 15.510  -13.237 1.00 19.92 ? 5   VAL D CA  1 
ATOM   3161 C C   . VAL D 1 5   ? -24.027 14.249  -13.524 1.00 20.07 ? 5   VAL D C   1 
ATOM   3162 O O   . VAL D 1 5   ? -23.881 13.593  -14.521 1.00 21.74 ? 5   VAL D O   1 
ATOM   3163 C CB  . VAL D 1 5   ? -24.015 16.864  -13.316 1.00 18.32 ? 5   VAL D CB  1 
ATOM   3164 C CG1 . VAL D 1 5   ? -24.505 17.166  -14.669 1.00 15.87 ? 5   VAL D CG1 1 
ATOM   3165 C CG2 . VAL D 1 5   ? -25.249 16.807  -12.398 1.00 19.61 ? 5   VAL D CG2 1 
ATOM   3166 N N   . CYS D 1 6   ? -24.863 13.869  -12.586 1.00 19.92 ? 6   CYS D N   1 
ATOM   3167 C CA  . CYS D 1 6   ? -25.805 12.824  -12.789 1.00 18.12 ? 6   CYS D CA  1 
ATOM   3168 C C   . CYS D 1 6   ? -27.065 13.296  -12.077 1.00 17.93 ? 6   CYS D C   1 
ATOM   3169 O O   . CYS D 1 6   ? -26.997 13.760  -10.928 1.00 17.25 ? 6   CYS D O   1 
ATOM   3170 C CB  . CYS D 1 6   ? -25.256 11.588  -12.123 1.00 18.03 ? 6   CYS D CB  1 
ATOM   3171 S SG  . CYS D 1 6   ? -26.234 10.148  -12.353 1.00 20.66 ? 6   CYS D SG  1 
ATOM   3172 N N   . VAL D 1 7   ? -28.208 13.188  -12.763 1.00 18.11 ? 7   VAL D N   1 
ATOM   3173 C CA  . VAL D 1 7   ? -29.532 13.491  -12.206 1.00 16.51 ? 7   VAL D CA  1 
ATOM   3174 C C   . VAL D 1 7   ? -30.139 12.117  -12.054 1.00 18.28 ? 7   VAL D C   1 
ATOM   3175 O O   . VAL D 1 7   ? -30.141 11.390  -13.038 1.00 16.49 ? 7   VAL D O   1 
ATOM   3176 C CB  . VAL D 1 7   ? -30.458 14.364  -13.154 1.00 16.41 ? 7   VAL D CB  1 
ATOM   3177 C CG1 . VAL D 1 7   ? -31.996 14.479  -12.534 1.00 12.57 ? 7   VAL D CG1 1 
ATOM   3178 C CG2 . VAL D 1 7   ? -29.841 15.808  -13.385 1.00 14.73 ? 7   VAL D CG2 1 
ATOM   3179 N N   . LEU D 1 8   ? -30.646 11.770  -10.860 1.00 18.05 ? 8   LEU D N   1 
ATOM   3180 C CA  . LEU D 1 8   ? -31.077 10.394  -10.611 1.00 19.90 ? 8   LEU D CA  1 
ATOM   3181 C C   . LEU D 1 8   ? -32.596 10.366  -10.486 1.00 18.99 ? 8   LEU D C   1 
ATOM   3182 O O   . LEU D 1 8   ? -33.148 11.234  -9.844  1.00 19.18 ? 8   LEU D O   1 
ATOM   3183 C CB  . LEU D 1 8   ? -30.421 9.781   -9.362  1.00 19.88 ? 8   LEU D CB  1 
ATOM   3184 C CG  . LEU D 1 8   ? -28.890 9.670   -9.369  1.00 23.09 ? 8   LEU D CG  1 
ATOM   3185 C CD1 . LEU D 1 8   ? -28.461 10.731  -8.505  1.00 20.82 ? 8   LEU D CD1 1 
ATOM   3186 C CD2 . LEU D 1 8   ? -28.353 8.341   -8.812  1.00 19.27 ? 8   LEU D CD2 1 
ATOM   3187 N N   . LYS D 1 9   ? -33.232 9.393   -11.162 1.00 21.22 ? 9   LYS D N   1 
ATOM   3188 C CA  . LYS D 1 9   ? -34.691 9.136   -11.147 1.00 22.87 ? 9   LYS D CA  1 
ATOM   3189 C C   . LYS D 1 9   ? -34.832 7.647   -11.317 1.00 23.13 ? 9   LYS D C   1 
ATOM   3190 O O   . LYS D 1 9   ? -33.979 7.011   -11.892 1.00 22.17 ? 9   LYS D O   1 
ATOM   3191 C CB  . LYS D 1 9   ? -35.484 9.796   -12.314 1.00 24.21 ? 9   LYS D CB  1 
ATOM   3192 C CG  . LYS D 1 9   ? -34.921 11.083  -12.936 1.00 28.32 ? 9   LYS D CG  1 
ATOM   3193 C CD  . LYS D 1 9   ? -36.010 12.186  -13.072 1.00 33.06 ? 9   LYS D CD  1 
ATOM   3194 C CE  . LYS D 1 9   ? -35.498 13.578  -12.664 1.00 33.90 ? 9   LYS D CE  1 
ATOM   3195 N NZ  . LYS D 1 9   ? -35.214 13.722  -11.159 1.00 37.12 ? 9   LYS D NZ  1 
ATOM   3196 N N   . GLY D 1 10  ? -35.923 7.111   -10.810 1.00 24.01 ? 10  GLY D N   1 
ATOM   3197 C CA  . GLY D 1 10  ? -36.268 5.718   -10.988 1.00 26.90 ? 10  GLY D CA  1 
ATOM   3198 C C   . GLY D 1 10  ? -37.787 5.649   -11.044 1.00 30.31 ? 10  GLY D C   1 
ATOM   3199 O O   . GLY D 1 10  ? -38.473 6.676   -11.242 1.00 29.52 ? 10  GLY D O   1 
ATOM   3200 N N   . ASP D 1 11  ? -38.345 4.442   -10.882 1.00 32.61 ? 11  ASP D N   1 
ATOM   3201 C CA  . ASP D 1 11  ? -39.807 4.306   -10.925 1.00 34.45 ? 11  ASP D CA  1 
ATOM   3202 C C   . ASP D 1 11  ? -40.541 4.707   -9.638  1.00 34.46 ? 11  ASP D C   1 
ATOM   3203 O O   . ASP D 1 11  ? -41.737 4.417   -9.524  1.00 35.78 ? 11  ASP D O   1 
ATOM   3204 C CB  . ASP D 1 11  ? -40.188 2.887   -11.339 1.00 35.64 ? 11  ASP D CB  1 
ATOM   3205 C CG  . ASP D 1 11  ? -39.682 2.536   -12.737 1.00 41.06 ? 11  ASP D CG  1 
ATOM   3206 O OD1 . ASP D 1 11  ? -39.501 3.483   -13.597 1.00 45.92 ? 11  ASP D OD1 1 
ATOM   3207 O OD2 . ASP D 1 11  ? -39.441 1.316   -12.964 1.00 43.31 ? 11  ASP D OD2 1 
ATOM   3208 N N   . GLY D 1 12  ? -39.852 5.384   -8.698  1.00 34.30 ? 12  GLY D N   1 
ATOM   3209 C CA  . GLY D 1 12  ? -40.366 5.637   -7.343  1.00 32.02 ? 12  GLY D CA  1 
ATOM   3210 C C   . GLY D 1 12  ? -40.170 7.056   -6.900  1.00 32.69 ? 12  GLY D C   1 
ATOM   3211 O O   . GLY D 1 12  ? -40.074 7.992   -7.746  1.00 31.48 ? 12  GLY D O   1 
ATOM   3212 N N   . PRO D 1 13  ? -40.129 7.268   -5.563  1.00 32.17 ? 13  PRO D N   1 
ATOM   3213 C CA  . PRO D 1 13  ? -39.890 8.647   -5.115  1.00 31.39 ? 13  PRO D CA  1 
ATOM   3214 C C   . PRO D 1 13  ? -38.378 9.052   -5.019  1.00 30.59 ? 13  PRO D C   1 
ATOM   3215 O O   . PRO D 1 13  ? -38.077 10.184  -4.666  1.00 29.74 ? 13  PRO D O   1 
ATOM   3216 C CB  . PRO D 1 13  ? -40.612 8.701   -3.757  1.00 30.97 ? 13  PRO D CB  1 
ATOM   3217 C CG  . PRO D 1 13  ? -40.647 7.270   -3.267  1.00 30.04 ? 13  PRO D CG  1 
ATOM   3218 C CD  . PRO D 1 13  ? -40.331 6.346   -4.427  1.00 32.15 ? 13  PRO D CD  1 
ATOM   3219 N N   . VAL D 1 14  ? -37.459 8.137   -5.359  1.00 30.32 ? 14  VAL D N   1 
ATOM   3220 C CA  . VAL D 1 14  ? -35.983 8.405   -5.265  1.00 29.54 ? 14  VAL D CA  1 
ATOM   3221 C C   . VAL D 1 14  ? -35.443 9.324   -6.361  1.00 28.75 ? 14  VAL D C   1 
ATOM   3222 O O   . VAL D 1 14  ? -35.513 8.999   -7.546  1.00 28.70 ? 14  VAL D O   1 
ATOM   3223 C CB  . VAL D 1 14  ? -35.145 7.109   -5.174  1.00 29.26 ? 14  VAL D CB  1 
ATOM   3224 C CG1 . VAL D 1 14  ? -33.684 7.417   -4.788  1.00 28.02 ? 14  VAL D CG1 1 
ATOM   3225 C CG2 . VAL D 1 14  ? -35.758 6.172   -4.129  1.00 27.91 ? 14  VAL D CG2 1 
ATOM   3226 N N   . GLN D 1 15  ? -34.904 10.468  -5.951  1.00 28.30 ? 15  GLN D N   1 
ATOM   3227 C CA  . GLN D 1 15  ? -34.349 11.437  -6.895  1.00 28.89 ? 15  GLN D CA  1 
ATOM   3228 C C   . GLN D 1 15  ? -33.297 12.414  -6.307  1.00 27.91 ? 15  GLN D C   1 
ATOM   3229 O O   . GLN D 1 15  ? -33.368 12.818  -5.144  1.00 26.47 ? 15  GLN D O   1 
ATOM   3230 C CB  . GLN D 1 15  ? -35.470 12.187  -7.616  1.00 29.60 ? 15  GLN D CB  1 
ATOM   3231 C CG  . GLN D 1 15  ? -36.329 13.040  -6.708  1.00 32.86 ? 15  GLN D CG  1 
ATOM   3232 C CD  . GLN D 1 15  ? -37.609 13.434  -7.405  1.00 39.19 ? 15  GLN D CD  1 
ATOM   3233 O OE1 . GLN D 1 15  ? -37.984 14.637  -7.480  1.00 39.35 ? 15  GLN D OE1 1 
ATOM   3234 N NE2 . GLN D 1 15  ? -38.299 12.424  -7.940  1.00 37.58 ? 15  GLN D NE2 1 
ATOM   3235 N N   . GLY D 1 16  ? -32.307 12.762  -7.114  1.00 26.11 ? 16  GLY D N   1 
ATOM   3236 C CA  . GLY D 1 16  ? -31.163 13.453  -6.589  1.00 26.61 ? 16  GLY D CA  1 
ATOM   3237 C C   . GLY D 1 16  ? -30.230 13.945  -7.658  1.00 26.55 ? 16  GLY D C   1 
ATOM   3238 O O   . GLY D 1 16  ? -30.401 13.600  -8.805  1.00 27.90 ? 16  GLY D O   1 
ATOM   3239 N N   . ILE D 1 17  ? -29.297 14.821  -7.277  1.00 25.91 ? 17  ILE D N   1 
ATOM   3240 C CA  . ILE D 1 17  ? -28.331 15.418  -8.215  1.00 24.16 ? 17  ILE D CA  1 
ATOM   3241 C C   . ILE D 1 17  ? -26.988 15.197  -7.600  1.00 21.84 ? 17  ILE D C   1 
ATOM   3242 O O   . ILE D 1 17  ? -26.762 15.462  -6.434  1.00 20.97 ? 17  ILE D O   1 
ATOM   3243 C CB  . ILE D 1 17  ? -28.598 16.953  -8.548  1.00 24.59 ? 17  ILE D CB  1 
ATOM   3244 C CG1 . ILE D 1 17  ? -29.876 17.082  -9.354  1.00 26.17 ? 17  ILE D CG1 1 
ATOM   3245 C CG2 . ILE D 1 17  ? -27.374 17.609  -9.302  1.00 25.40 ? 17  ILE D CG2 1 
ATOM   3246 C CD1 . ILE D 1 17  ? -30.578 18.432  -9.229  1.00 28.86 ? 17  ILE D CD1 1 
ATOM   3247 N N   . ILE D 1 18  ? -26.083 14.704  -8.399  1.00 19.57 ? 18  ILE D N   1 
ATOM   3248 C CA  . ILE D 1 18  ? -24.768 14.360  -7.908  1.00 18.51 ? 18  ILE D CA  1 
ATOM   3249 C C   . ILE D 1 18  ? -23.753 14.997  -8.822  1.00 17.93 ? 18  ILE D C   1 
ATOM   3250 O O   . ILE D 1 18  ? -23.896 14.998  -10.024 1.00 17.38 ? 18  ILE D O   1 
ATOM   3251 C CB  . ILE D 1 18  ? -24.587 12.762  -7.755  1.00 17.80 ? 18  ILE D CB  1 
ATOM   3252 C CG1 . ILE D 1 18  ? -25.558 12.228  -6.674  1.00 15.70 ? 18  ILE D CG1 1 
ATOM   3253 C CG2 . ILE D 1 18  ? -23.122 12.356  -7.424  1.00 18.82 ? 18  ILE D CG2 1 
ATOM   3254 C CD1 . ILE D 1 18  ? -25.237 12.786  -5.166  1.00 14.36 ? 18  ILE D CD1 1 
ATOM   3255 N N   . ASN D 1 19  ? -22.738 15.552  -8.215  1.00 18.65 ? 19  ASN D N   1 
ATOM   3256 C CA  . ASN D 1 19  ? -21.686 16.256  -8.891  1.00 19.48 ? 19  ASN D CA  1 
ATOM   3257 C C   . ASN D 1 19  ? -20.414 15.550  -8.709  1.00 19.34 ? 19  ASN D C   1 
ATOM   3258 O O   . ASN D 1 19  ? -20.207 14.932  -7.663  1.00 20.36 ? 19  ASN D O   1 
ATOM   3259 C CB  . ASN D 1 19  ? -21.520 17.657  -8.271  1.00 20.98 ? 19  ASN D CB  1 
ATOM   3260 C CG  . ASN D 1 19  ? -22.719 18.531  -8.496  1.00 22.35 ? 19  ASN D CG  1 
ATOM   3261 O OD1 . ASN D 1 19  ? -23.076 18.887  -9.664  1.00 24.56 ? 19  ASN D OD1 1 
ATOM   3262 N ND2 . ASN D 1 19  ? -23.330 18.934  -7.394  1.00 17.50 ? 19  ASN D ND2 1 
ATOM   3263 N N   . PHE D 1 20  ? -19.520 15.723  -9.685  1.00 20.19 ? 20  PHE D N   1 
ATOM   3264 C CA  . PHE D 1 20  ? -18.191 15.140  -9.689  1.00 20.96 ? 20  PHE D CA  1 
ATOM   3265 C C   . PHE D 1 20  ? -17.247 16.227  -10.093 1.00 24.04 ? 20  PHE D C   1 
ATOM   3266 O O   . PHE D 1 20  ? -17.547 17.060  -10.993 1.00 25.62 ? 20  PHE D O   1 
ATOM   3267 C CB  . PHE D 1 20  ? -18.067 13.987  -10.720 1.00 21.52 ? 20  PHE D CB  1 
ATOM   3268 C CG  . PHE D 1 20  ? -19.016 12.826  -10.488 1.00 16.84 ? 20  PHE D CG  1 
ATOM   3269 C CD1 . PHE D 1 20  ? -20.347 12.869  -10.968 1.00 14.99 ? 20  PHE D CD1 1 
ATOM   3270 C CD2 . PHE D 1 20  ? -18.585 11.726  -9.812  1.00 18.40 ? 20  PHE D CD2 1 
ATOM   3271 C CE1 . PHE D 1 20  ? -21.231 11.821  -10.765 1.00 13.43 ? 20  PHE D CE1 1 
ATOM   3272 C CE2 . PHE D 1 20  ? -19.464 10.624  -9.565  1.00 17.95 ? 20  PHE D CE2 1 
ATOM   3273 C CZ  . PHE D 1 20  ? -20.777 10.677  -10.066 1.00 14.97 ? 20  PHE D CZ  1 
ATOM   3274 N N   . GLU D 1 21  ? -16.109 16.245  -9.443  1.00 25.02 ? 21  GLU D N   1 
ATOM   3275 C CA  . GLU D 1 21  ? -15.066 17.158  -9.819  1.00 27.69 ? 21  GLU D CA  1 
ATOM   3276 C C   . GLU D 1 21  ? -13.723 16.512  -9.645  1.00 27.60 ? 21  GLU D C   1 
ATOM   3277 O O   . GLU D 1 21  ? -13.455 15.947  -8.616  1.00 28.08 ? 21  GLU D O   1 
ATOM   3278 C CB  . GLU D 1 21  ? -15.125 18.416  -8.961  1.00 28.45 ? 21  GLU D CB  1 
ATOM   3279 C CG  . GLU D 1 21  ? -14.163 19.503  -9.349  1.00 31.74 ? 21  GLU D CG  1 
ATOM   3280 C CD  . GLU D 1 21  ? -14.606 20.811  -8.738  1.00 44.73 ? 21  GLU D CD  1 
ATOM   3281 O OE1 . GLU D 1 21  ? -13.764 21.491  -8.077  1.00 46.44 ? 21  GLU D OE1 1 
ATOM   3282 O OE2 . GLU D 1 21  ? -15.829 21.134  -8.885  1.00 46.84 ? 21  GLU D OE2 1 
ATOM   3283 N N   . GLN D 1 22  ? -12.879 16.637  -10.654 1.00 28.71 ? 22  GLN D N   1 
ATOM   3284 C CA  . GLN D 1 22  ? -11.500 16.155  -10.601 1.00 30.17 ? 22  GLN D CA  1 
ATOM   3285 C C   . GLN D 1 22  ? -10.599 17.301  -10.988 1.00 32.23 ? 22  GLN D C   1 
ATOM   3286 O O   . GLN D 1 22  ? -10.455 17.599  -12.159 1.00 32.80 ? 22  GLN D O   1 
ATOM   3287 C CB  . GLN D 1 22  ? -11.281 14.981  -11.571 1.00 27.87 ? 22  GLN D CB  1 
ATOM   3288 C CG  . GLN D 1 22  ? -10.143 14.136  -11.177 1.00 26.75 ? 22  GLN D CG  1 
ATOM   3289 C CD  . GLN D 1 22  ? -9.988  12.959  -12.083 1.00 23.83 ? 22  GLN D CD  1 
ATOM   3290 O OE1 . GLN D 1 22  ? -10.460 13.012  -13.230 1.00 23.33 ? 22  GLN D OE1 1 
ATOM   3291 N NE2 . GLN D 1 22  ? -9.329  11.879  -11.596 1.00 11.11 ? 22  GLN D NE2 1 
ATOM   3292 N N   . LYS D 1 23  ? -9.981  17.896  -9.979  1.00 35.81 ? 23  LYS D N   1 
ATOM   3293 C CA  . LYS D 1 23  ? -9.025  19.042  -10.051 1.00 38.59 ? 23  LYS D CA  1 
ATOM   3294 C C   . LYS D 1 23  ? -7.936  18.901  -11.112 1.00 38.57 ? 23  LYS D C   1 
ATOM   3295 O O   . LYS D 1 23  ? -7.468  19.885  -11.695 1.00 39.02 ? 23  LYS D O   1 
ATOM   3296 C CB  . LYS D 1 23  ? -8.291  19.179  -8.666  1.00 39.02 ? 23  LYS D CB  1 
ATOM   3297 C CG  . LYS D 1 23  ? -9.019  19.848  -7.447  1.00 41.50 ? 23  LYS D CG  1 
ATOM   3298 C CD  . LYS D 1 23  ? -9.142  21.401  -7.573  1.00 45.05 ? 23  LYS D CD  1 
ATOM   3299 C CE  . LYS D 1 23  ? -10.299 21.814  -8.539  1.00 47.36 ? 23  LYS D CE  1 
ATOM   3300 N NZ  . LYS D 1 23  ? -9.923  22.872  -9.575  1.00 49.03 ? 23  LYS D NZ  1 
ATOM   3301 N N   . GLU D 1 24  ? -7.553  17.651  -11.323 1.00 39.23 ? 24  GLU D N   1 
ATOM   3302 C CA  . GLU D 1 24  ? -6.291  17.218  -11.903 1.00 40.96 ? 24  GLU D CA  1 
ATOM   3303 C C   . GLU D 1 24  ? -6.451  15.711  -12.228 1.00 39.18 ? 24  GLU D C   1 
ATOM   3304 O O   . GLU D 1 24  ? -6.869  14.956  -11.375 1.00 37.98 ? 24  GLU D O   1 
ATOM   3305 C CB  . GLU D 1 24  ? -5.142  17.425  -10.865 1.00 41.43 ? 24  GLU D CB  1 
ATOM   3306 C CG  . GLU D 1 24  ? -5.427  16.817  -9.452  1.00 43.32 ? 24  GLU D CG  1 
ATOM   3307 C CD  . GLU D 1 24  ? -4.227  16.771  -8.472  1.00 45.17 ? 24  GLU D CD  1 
ATOM   3308 O OE1 . GLU D 1 24  ? -4.497  16.847  -7.241  1.00 50.27 ? 24  GLU D OE1 1 
ATOM   3309 O OE2 . GLU D 1 24  ? -3.041  16.609  -8.890  1.00 48.41 ? 24  GLU D OE2 1 
ATOM   3310 N N   . SER D 1 25  ? -6.094  15.295  -13.442 1.00 39.98 ? 25  SER D N   1 
ATOM   3311 C CA  . SER D 1 25  ? -6.331  13.923  -13.956 1.00 40.49 ? 25  SER D CA  1 
ATOM   3312 C C   . SER D 1 25  ? -5.733  12.685  -13.237 1.00 41.00 ? 25  SER D C   1 
ATOM   3313 O O   . SER D 1 25  ? -6.213  11.572  -13.422 1.00 41.07 ? 25  SER D O   1 
ATOM   3314 C CB  . SER D 1 25  ? -5.982  13.843  -15.451 1.00 41.51 ? 25  SER D CB  1 
ATOM   3315 O OG  . SER D 1 25  ? -4.898  14.698  -15.807 1.00 42.34 ? 25  SER D OG  1 
ATOM   3316 N N   . ASN D 1 26  ? -4.667  12.820  -12.459 1.00 42.14 ? 26  ASN D N   1 
ATOM   3317 C CA  . ASN D 1 26  ? -4.270  11.676  -11.613 1.00 42.87 ? 26  ASN D CA  1 
ATOM   3318 C C   . ASN D 1 26  ? -5.089  11.759  -10.341 1.00 41.75 ? 26  ASN D C   1 
ATOM   3319 O O   . ASN D 1 26  ? -5.212  10.782  -9.613  1.00 42.79 ? 26  ASN D O   1 
ATOM   3320 C CB  . ASN D 1 26  ? -2.787  11.678  -11.259 1.00 43.28 ? 26  ASN D CB  1 
ATOM   3321 C CG  . ASN D 1 26  ? -1.895  11.510  -12.462 1.00 46.23 ? 26  ASN D CG  1 
ATOM   3322 O OD1 . ASN D 1 26  ? -0.707  11.870  -12.405 1.00 49.79 ? 26  ASN D OD1 1 
ATOM   3323 N ND2 . ASN D 1 26  ? -2.444  10.958  -13.570 1.00 49.39 ? 26  ASN D ND2 1 
ATOM   3324 N N   . GLY D 1 27  ? -5.688  12.931  -10.136 1.00 39.76 ? 27  GLY D N   1 
ATOM   3325 C CA  . GLY D 1 27  ? -6.324  13.292  -8.912  1.00 36.94 ? 27  GLY D CA  1 
ATOM   3326 C C   . GLY D 1 27  ? -7.517  12.480  -8.480  1.00 35.60 ? 27  GLY D C   1 
ATOM   3327 O O   . GLY D 1 27  ? -8.011  11.551  -9.219  1.00 35.64 ? 27  GLY D O   1 
ATOM   3328 N N   . PRO D 1 28  ? -7.929  12.739  -7.223  1.00 33.55 ? 28  PRO D N   1 
ATOM   3329 C CA  . PRO D 1 28  ? -9.189  12.224  -6.728  1.00 31.12 ? 28  PRO D CA  1 
ATOM   3330 C C   . PRO D 1 28  ? -10.361 13.019  -7.232  1.00 28.52 ? 28  PRO D C   1 
ATOM   3331 O O   . PRO D 1 28  ? -10.259 14.200  -7.549  1.00 27.01 ? 28  PRO D O   1 
ATOM   3332 C CB  . PRO D 1 28  ? -9.061  12.343  -5.213  1.00 29.64 ? 28  PRO D CB  1 
ATOM   3333 C CG  . PRO D 1 28  ? -8.154  13.540  -5.041  1.00 34.19 ? 28  PRO D CG  1 
ATOM   3334 C CD  . PRO D 1 28  ? -7.145  13.425  -6.168  1.00 33.05 ? 28  PRO D CD  1 
ATOM   3335 N N   . VAL D 1 29  ? -11.487 12.332  -7.269  1.00 27.11 ? 29  VAL D N   1 
ATOM   3336 C CA  . VAL D 1 29  ? -12.740 12.914  -7.732  1.00 25.25 ? 29  VAL D CA  1 
ATOM   3337 C C   . VAL D 1 29  ? -13.566 13.141  -6.508  1.00 24.31 ? 29  VAL D C   1 
ATOM   3338 O O   . VAL D 1 29  ? -13.703 12.274  -5.675  1.00 24.80 ? 29  VAL D O   1 
ATOM   3339 C CB  . VAL D 1 29  ? -13.451 11.946  -8.749  1.00 25.41 ? 29  VAL D CB  1 
ATOM   3340 C CG1 . VAL D 1 29  ? -14.797 12.550  -9.247  1.00 22.65 ? 29  VAL D CG1 1 
ATOM   3341 C CG2 . VAL D 1 29  ? -12.487 11.663  -9.917  1.00 21.65 ? 29  VAL D CG2 1 
ATOM   3342 N N   . LYS D 1 30  ? -14.090 14.341  -6.395  1.00 23.46 ? 30  LYS D N   1 
ATOM   3343 C CA  . LYS D 1 30  ? -14.992 14.666  -5.342  1.00 23.58 ? 30  LYS D CA  1 
ATOM   3344 C C   . LYS D 1 30  ? -16.413 14.481  -5.851  1.00 22.86 ? 30  LYS D C   1 
ATOM   3345 O O   . LYS D 1 30  ? -16.735 14.899  -6.933  1.00 25.01 ? 30  LYS D O   1 
ATOM   3346 C CB  . LYS D 1 30  ? -14.743 16.124  -4.902  1.00 20.47 ? 30  LYS D CB  1 
ATOM   3347 C CG  . LYS D 1 30  ? -13.654 16.198  -3.850  1.00 26.79 ? 30  LYS D CG  1 
ATOM   3348 C CD  . LYS D 1 30  ? -12.505 17.171  -4.256  1.00 33.38 ? 30  LYS D CD  1 
ATOM   3349 C CE  . LYS D 1 30  ? -11.883 17.801  -3.017  1.00 31.24 ? 30  LYS D CE  1 
ATOM   3350 N NZ  . LYS D 1 30  ? -13.008 18.694  -2.430  1.00 34.09 ? 30  LYS D NZ  1 
ATOM   3351 N N   . VAL D 1 31  ? -17.257 13.862  -5.039  1.00 24.23 ? 31  VAL D N   1 
ATOM   3352 C CA  . VAL D 1 31  ? -18.632 13.594  -5.357  1.00 22.39 ? 31  VAL D CA  1 
ATOM   3353 C C   . VAL D 1 31  ? -19.540 13.969  -4.214  1.00 23.40 ? 31  VAL D C   1 
ATOM   3354 O O   . VAL D 1 31  ? -19.327 13.559  -3.077  1.00 23.39 ? 31  VAL D O   1 
ATOM   3355 C CB  . VAL D 1 31  ? -18.858 12.079  -5.880  1.00 23.72 ? 31  VAL D CB  1 
ATOM   3356 C CG1 . VAL D 1 31  ? -17.672 11.151  -5.611  1.00 19.29 ? 31  VAL D CG1 1 
ATOM   3357 C CG2 . VAL D 1 31  ? -20.238 11.539  -5.535  1.00 15.56 ? 31  VAL D CG2 1 
ATOM   3358 N N   . TRP D 1 32  ? -20.552 14.769  -4.545  1.00 24.30 ? 32  TRP D N   1 
ATOM   3359 C CA  . TRP D 1 32  ? -21.439 15.416  -3.569  1.00 24.33 ? 32  TRP D CA  1 
ATOM   3360 C C   . TRP D 1 32  ? -22.734 15.848  -4.217  1.00 23.49 ? 32  TRP D C   1 
ATOM   3361 O O   . TRP D 1 32  ? -22.776 16.135  -5.432  1.00 21.12 ? 32  TRP D O   1 
ATOM   3362 C CB  . TRP D 1 32  ? -20.732 16.645  -2.929  1.00 26.34 ? 32  TRP D CB  1 
ATOM   3363 C CG  . TRP D 1 32  ? -20.761 17.882  -3.763  1.00 25.70 ? 32  TRP D CG  1 
ATOM   3364 C CD1 . TRP D 1 32  ? -21.601 18.954  -3.606  1.00 26.50 ? 32  TRP D CD1 1 
ATOM   3365 C CD2 . TRP D 1 32  ? -19.933 18.189  -4.894  1.00 28.65 ? 32  TRP D CD2 1 
ATOM   3366 N NE1 . TRP D 1 32  ? -21.357 19.890  -4.571  1.00 24.02 ? 32  TRP D NE1 1 
ATOM   3367 C CE2 . TRP D 1 32  ? -20.322 19.464  -5.359  1.00 26.39 ? 32  TRP D CE2 1 
ATOM   3368 C CE3 . TRP D 1 32  ? -18.890 17.514  -5.564  1.00 29.63 ? 32  TRP D CE3 1 
ATOM   3369 C CZ2 . TRP D 1 32  ? -19.705 20.085  -6.475  1.00 30.20 ? 32  TRP D CZ2 1 
ATOM   3370 C CZ3 . TRP D 1 32  ? -18.267 18.140  -6.671  1.00 29.15 ? 32  TRP D CZ3 1 
ATOM   3371 C CH2 . TRP D 1 32  ? -18.689 19.400  -7.121  1.00 27.65 ? 32  TRP D CH2 1 
ATOM   3372 N N   . GLY D 1 33  ? -23.780 15.950  -3.389  1.00 22.62 ? 33  GLY D N   1 
ATOM   3373 C CA  . GLY D 1 33  ? -25.082 16.351  -3.869  1.00 22.36 ? 33  GLY D CA  1 
ATOM   3374 C C   . GLY D 1 33  ? -26.096 15.871  -2.869  1.00 24.33 ? 33  GLY D C   1 
ATOM   3375 O O   . GLY D 1 33  ? -25.746 15.538  -1.771  1.00 25.06 ? 33  GLY D O   1 
ATOM   3376 N N   . SER D 1 34  ? -27.364 15.815  -3.247  1.00 25.61 ? 34  SER D N   1 
ATOM   3377 C CA  . SER D 1 34  ? -28.394 15.289  -2.374  1.00 26.42 ? 34  SER D CA  1 
ATOM   3378 C C   . SER D 1 34  ? -29.333 14.314  -3.077  1.00 26.26 ? 34  SER D C   1 
ATOM   3379 O O   . SER D 1 34  ? -29.602 14.449  -4.274  1.00 25.89 ? 34  SER D O   1 
ATOM   3380 C CB  . SER D 1 34  ? -29.192 16.463  -1.814  1.00 26.30 ? 34  SER D CB  1 
ATOM   3381 O OG  . SER D 1 34  ? -30.071 15.971  -0.790  1.00 32.94 ? 34  SER D OG  1 
ATOM   3382 N N   . ILE D 1 35  ? -29.853 13.344  -2.320  1.00 27.93 ? 35  ILE D N   1 
ATOM   3383 C CA  . ILE D 1 35  ? -30.849 12.371  -2.811  1.00 29.04 ? 35  ILE D CA  1 
ATOM   3384 C C   . ILE D 1 35  ? -32.055 12.223  -1.858  1.00 30.40 ? 35  ILE D C   1 
ATOM   3385 O O   . ILE D 1 35  ? -31.914 11.864  -0.707  1.00 31.83 ? 35  ILE D O   1 
ATOM   3386 C CB  . ILE D 1 35  ? -30.262 10.988  -3.062  1.00 28.56 ? 35  ILE D CB  1 
ATOM   3387 C CG1 . ILE D 1 35  ? -28.853 11.060  -3.671  1.00 30.73 ? 35  ILE D CG1 1 
ATOM   3388 C CG2 . ILE D 1 35  ? -31.187 10.202  -3.993  1.00 30.07 ? 35  ILE D CG2 1 
ATOM   3389 C CD1 . ILE D 1 35  ? -28.147 9.685   -3.704  1.00 28.28 ? 35  ILE D CD1 1 
ATOM   3390 N N   . LYS D 1 36  ? -33.254 12.453  -2.358  1.00 31.06 ? 36  LYS D N   1 
ATOM   3391 C CA  . LYS D 1 36  ? -34.456 12.369  -1.534  1.00 31.84 ? 36  LYS D CA  1 
ATOM   3392 C C   . LYS D 1 36  ? -35.278 11.094  -1.818  1.00 29.24 ? 36  LYS D C   1 
ATOM   3393 O O   . LYS D 1 36  ? -34.995 10.360  -2.759  1.00 27.33 ? 36  LYS D O   1 
ATOM   3394 C CB  . LYS D 1 36  ? -35.268 13.676  -1.679  1.00 31.98 ? 36  LYS D CB  1 
ATOM   3395 C CG  . LYS D 1 36  ? -35.870 13.927  -3.076  1.00 34.18 ? 36  LYS D CG  1 
ATOM   3396 C CD  . LYS D 1 36  ? -36.951 15.038  -2.989  1.00 35.85 ? 36  LYS D CD  1 
ATOM   3397 C CE  . LYS D 1 36  ? -37.143 15.852  -4.309  1.00 40.81 ? 36  LYS D CE  1 
ATOM   3398 N NZ  . LYS D 1 36  ? -37.708 17.250  -4.070  1.00 39.19 ? 36  LYS D NZ  1 
ATOM   3399 N N   . GLY D 1 37  ? -36.284 10.830  -0.989  1.00 28.93 ? 37  GLY D N   1 
ATOM   3400 C CA  . GLY D 1 37  ? -37.199 9.711   -1.225  1.00 28.59 ? 37  GLY D CA  1 
ATOM   3401 C C   . GLY D 1 37  ? -36.722 8.338   -0.780  1.00 29.48 ? 37  GLY D C   1 
ATOM   3402 O O   . GLY D 1 37  ? -37.411 7.311   -0.996  1.00 31.54 ? 37  GLY D O   1 
ATOM   3403 N N   . LEU D 1 38  ? -35.537 8.281   -0.194  1.00 29.03 ? 38  LEU D N   1 
ATOM   3404 C CA  . LEU D 1 38  ? -34.954 7.023   0.310   1.00 29.13 ? 38  LEU D CA  1 
ATOM   3405 C C   . LEU D 1 38  ? -35.500 6.629   1.674   1.00 29.52 ? 38  LEU D C   1 
ATOM   3406 O O   . LEU D 1 38  ? -35.849 7.498   2.492   1.00 30.39 ? 38  LEU D O   1 
ATOM   3407 C CB  . LEU D 1 38  ? -33.429 7.191   0.479   1.00 28.68 ? 38  LEU D CB  1 
ATOM   3408 C CG  . LEU D 1 38  ? -32.363 6.901   -0.592  1.00 27.99 ? 38  LEU D CG  1 
ATOM   3409 C CD1 . LEU D 1 38  ? -32.812 6.036   -1.721  1.00 19.02 ? 38  LEU D CD1 1 
ATOM   3410 C CD2 . LEU D 1 38  ? -31.695 8.164   -1.057  1.00 29.28 ? 38  LEU D CD2 1 
ATOM   3411 N N   . THR D 1 39  ? -35.564 5.317   1.932   1.00 29.84 ? 39  THR D N   1 
ATOM   3412 C CA  . THR D 1 39  ? -35.757 4.821   3.293   1.00 30.42 ? 39  THR D CA  1 
ATOM   3413 C C   . THR D 1 39  ? -34.513 5.108   4.130   1.00 31.14 ? 39  THR D C   1 
ATOM   3414 O O   . THR D 1 39  ? -33.388 5.231   3.578   1.00 31.21 ? 39  THR D O   1 
ATOM   3415 C CB  . THR D 1 39  ? -36.045 3.328   3.302   1.00 29.51 ? 39  THR D CB  1 
ATOM   3416 O OG1 . THR D 1 39  ? -35.033 2.685   2.536   1.00 28.06 ? 39  THR D OG1 1 
ATOM   3417 C CG2 . THR D 1 39  ? -37.433 3.066   2.664   1.00 29.33 ? 39  THR D CG2 1 
ATOM   3418 N N   . GLU D 1 40  ? -34.719 5.151   5.449   1.00 30.98 ? 40  GLU D N   1 
ATOM   3419 C CA  . GLU D 1 40  ? -33.703 5.548   6.415   1.00 31.79 ? 40  GLU D CA  1 
ATOM   3420 C C   . GLU D 1 40  ? -32.530 4.574   6.446   1.00 29.44 ? 40  GLU D C   1 
ATOM   3421 O O   . GLU D 1 40  ? -32.724 3.385   6.442   1.00 29.08 ? 40  GLU D O   1 
ATOM   3422 C CB  . GLU D 1 40  ? -34.322 5.778   7.796   1.00 31.01 ? 40  GLU D CB  1 
ATOM   3423 C CG  . GLU D 1 40  ? -33.325 5.722   8.979   1.00 35.71 ? 40  GLU D CG  1 
ATOM   3424 C CD  . GLU D 1 40  ? -33.775 6.470   10.264  1.00 35.31 ? 40  GLU D CD  1 
ATOM   3425 O OE1 . GLU D 1 40  ? -34.994 6.655   10.533  1.00 38.41 ? 40  GLU D OE1 1 
ATOM   3426 O OE2 . GLU D 1 40  ? -32.853 6.883   10.996  1.00 42.47 ? 40  GLU D OE2 1 
ATOM   3427 N N   . GLY D 1 41  ? -31.303 5.093   6.443   1.00 29.29 ? 41  GLY D N   1 
ATOM   3428 C CA  . GLY D 1 41  ? -30.167 4.174   6.521   1.00 28.70 ? 41  GLY D CA  1 
ATOM   3429 C C   . GLY D 1 41  ? -29.314 4.108   5.275   1.00 27.25 ? 41  GLY D C   1 
ATOM   3430 O O   . GLY D 1 41  ? -29.341 5.031   4.443   1.00 28.66 ? 41  GLY D O   1 
ATOM   3431 N N   . LEU D 1 42  ? -28.612 2.995   5.128   1.00 26.46 ? 42  LEU D N   1 
ATOM   3432 C CA  . LEU D 1 42  ? -27.515 2.841   4.167   1.00 26.07 ? 42  LEU D CA  1 
ATOM   3433 C C   . LEU D 1 42  ? -27.921 2.334   2.796   1.00 23.59 ? 42  LEU D C   1 
ATOM   3434 O O   . LEU D 1 42  ? -28.470 1.212   2.682   1.00 22.66 ? 42  LEU D O   1 
ATOM   3435 C CB  . LEU D 1 42  ? -26.477 1.851   4.708   1.00 26.37 ? 42  LEU D CB  1 
ATOM   3436 C CG  . LEU D 1 42  ? -25.061 2.197   5.157   1.00 28.09 ? 42  LEU D CG  1 
ATOM   3437 C CD1 . LEU D 1 42  ? -24.839 3.631   5.393   1.00 29.31 ? 42  LEU D CD1 1 
ATOM   3438 C CD2 . LEU D 1 42  ? -24.828 1.400   6.433   1.00 24.65 ? 42  LEU D CD2 1 
ATOM   3439 N N   . HIS D 1 43  ? -27.570 3.100   1.755   1.00 20.74 ? 43  HIS D N   1 
ATOM   3440 C CA  . HIS D 1 43  ? -27.889 2.631   0.356   1.00 19.75 ? 43  HIS D CA  1 
ATOM   3441 C C   . HIS D 1 43  ? -26.650 2.415   -0.498  1.00 19.05 ? 43  HIS D C   1 
ATOM   3442 O O   . HIS D 1 43  ? -25.861 3.311   -0.624  1.00 18.38 ? 43  HIS D O   1 
ATOM   3443 C CB  . HIS D 1 43  ? -28.815 3.624   -0.311  1.00 19.73 ? 43  HIS D CB  1 
ATOM   3444 C CG  . HIS D 1 43  ? -30.091 3.800   0.440   1.00 20.44 ? 43  HIS D CG  1 
ATOM   3445 N ND1 . HIS D 1 43  ? -31.142 2.903   0.336   1.00 22.04 ? 43  HIS D ND1 1 
ATOM   3446 C CD2 . HIS D 1 43  ? -30.430 4.671   1.406   1.00 15.29 ? 43  HIS D CD2 1 
ATOM   3447 C CE1 . HIS D 1 43  ? -32.099 3.262   1.174   1.00 15.54 ? 43  HIS D CE1 1 
ATOM   3448 N NE2 . HIS D 1 43  ? -31.695 4.327   1.830   1.00 20.34 ? 43  HIS D NE2 1 
ATOM   3449 N N   . GLY D 1 44  ? -26.459 1.223   -1.029  1.00 18.55 ? 44  GLY D N   1 
ATOM   3450 C CA  . GLY D 1 44  ? -25.356 0.969   -1.974  1.00 19.88 ? 44  GLY D CA  1 
ATOM   3451 C C   . GLY D 1 44  ? -25.223 2.062   -3.053  1.00 20.91 ? 44  GLY D C   1 
ATOM   3452 O O   . GLY D 1 44  ? -26.239 2.581   -3.569  1.00 19.17 ? 44  GLY D O   1 
ATOM   3453 N N   . PHE D 1 45  ? -23.982 2.493   -3.313  1.00 21.59 ? 45  PHE D N   1 
ATOM   3454 C CA  . PHE D 1 45  ? -23.760 3.608   -4.212  1.00 21.76 ? 45  PHE D CA  1 
ATOM   3455 C C   . PHE D 1 45  ? -22.716 3.195   -5.187  1.00 23.28 ? 45  PHE D C   1 
ATOM   3456 O O   . PHE D 1 45  ? -21.551 3.014   -4.799  1.00 23.44 ? 45  PHE D O   1 
ATOM   3457 C CB  . PHE D 1 45  ? -23.285 4.809   -3.419  1.00 22.55 ? 45  PHE D CB  1 
ATOM   3458 C CG  . PHE D 1 45  ? -23.506 6.147   -4.077  1.00 19.82 ? 45  PHE D CG  1 
ATOM   3459 C CD1 . PHE D 1 45  ? -24.678 6.428   -4.782  1.00 21.19 ? 45  PHE D CD1 1 
ATOM   3460 C CD2 . PHE D 1 45  ? -22.551 7.152   -3.939  1.00 20.92 ? 45  PHE D CD2 1 
ATOM   3461 C CE1 . PHE D 1 45  ? -24.895 7.692   -5.352  1.00 21.28 ? 45  PHE D CE1 1 
ATOM   3462 C CE2 . PHE D 1 45  ? -22.747 8.451   -4.514  1.00 20.88 ? 45  PHE D CE2 1 
ATOM   3463 C CZ  . PHE D 1 45  ? -23.913 8.717   -5.199  1.00 17.88 ? 45  PHE D CZ  1 
ATOM   3464 N N   . HIS D 1 46  ? -23.125 3.026   -6.461  1.00 24.26 ? 46  HIS D N   1 
ATOM   3465 C CA  . HIS D 1 46  ? -22.227 2.442   -7.490  1.00 23.53 ? 46  HIS D CA  1 
ATOM   3466 C C   . HIS D 1 46  ? -22.263 3.125   -8.837  1.00 22.87 ? 46  HIS D C   1 
ATOM   3467 O O   . HIS D 1 46  ? -23.297 3.656   -9.252  1.00 22.65 ? 46  HIS D O   1 
ATOM   3468 C CB  . HIS D 1 46  ? -22.565 0.959   -7.724  1.00 22.35 ? 46  HIS D CB  1 
ATOM   3469 C CG  . HIS D 1 46  ? -22.192 0.081   -6.581  1.00 26.01 ? 46  HIS D CG  1 
ATOM   3470 N ND1 . HIS D 1 46  ? -23.094 -0.267  -5.589  1.00 26.62 ? 46  HIS D ND1 1 
ATOM   3471 C CD2 . HIS D 1 46  ? -21.011 -0.496  -6.247  1.00 20.97 ? 46  HIS D CD2 1 
ATOM   3472 C CE1 . HIS D 1 46  ? -22.477 -1.013  -4.694  1.00 26.63 ? 46  HIS D CE1 1 
ATOM   3473 N NE2 . HIS D 1 46  ? -21.213 -1.156  -5.062  1.00 26.87 ? 46  HIS D NE2 1 
ATOM   3474 N N   . VAL D 1 47  ? -21.113 3.091   -9.511  1.00 21.30 ? 47  VAL D N   1 
ATOM   3475 C CA  . VAL D 1 47  ? -21.044 3.309   -10.975 1.00 20.25 ? 47  VAL D CA  1 
ATOM   3476 C C   . VAL D 1 47  ? -21.220 1.925   -11.686 1.00 20.61 ? 47  VAL D C   1 
ATOM   3477 O O   . VAL D 1 47  ? -20.629 0.906   -11.295 1.00 19.82 ? 47  VAL D O   1 
ATOM   3478 C CB  . VAL D 1 47  ? -19.759 4.102   -11.403 1.00 19.34 ? 47  VAL D CB  1 
ATOM   3479 C CG1 . VAL D 1 47  ? -19.801 4.525   -12.904 1.00 19.66 ? 47  VAL D CG1 1 
ATOM   3480 C CG2 . VAL D 1 47  ? -19.584 5.344   -10.513 1.00 18.88 ? 47  VAL D CG2 1 
ATOM   3481 N N   . HIS D 1 48  ? -22.118 1.877   -12.657 1.00 20.48 ? 48  HIS D N   1 
ATOM   3482 C CA  . HIS D 1 48  ? -22.366 0.657   -13.414 1.00 22.37 ? 48  HIS D CA  1 
ATOM   3483 C C   . HIS D 1 48  ? -21.836 0.874   -14.843 1.00 21.96 ? 48  HIS D C   1 
ATOM   3484 O O   . HIS D 1 48  ? -21.728 1.997   -15.275 1.00 21.78 ? 48  HIS D O   1 
ATOM   3485 C CB  . HIS D 1 48  ? -23.856 0.362   -13.384 1.00 21.22 ? 48  HIS D CB  1 
ATOM   3486 C CG  . HIS D 1 48  ? -24.303 -0.173  -12.067 1.00 23.87 ? 48  HIS D CG  1 
ATOM   3487 N ND1 . HIS D 1 48  ? -24.683 -1.488  -11.897 1.00 22.01 ? 48  HIS D ND1 1 
ATOM   3488 C CD2 . HIS D 1 48  ? -24.351 0.400   -10.835 1.00 22.16 ? 48  HIS D CD2 1 
ATOM   3489 C CE1 . HIS D 1 48  ? -24.989 -1.695  -10.626 1.00 21.01 ? 48  HIS D CE1 1 
ATOM   3490 N NE2 . HIS D 1 48  ? -24.802 -0.568  -9.964  1.00 23.77 ? 48  HIS D NE2 1 
ATOM   3491 N N   . GLU D 1 49  ? -21.491 -0.180  -15.560 1.00 22.59 ? 49  GLU D N   1 
ATOM   3492 C CA  . GLU D 1 49  ? -20.746 -0.009  -16.807 1.00 23.45 ? 49  GLU D CA  1 
ATOM   3493 C C   . GLU D 1 49  ? -21.386 0.810   -18.012 1.00 23.04 ? 49  GLU D C   1 
ATOM   3494 O O   . GLU D 1 49  ? -20.674 1.402   -18.818 1.00 22.60 ? 49  GLU D O   1 
ATOM   3495 C CB  . GLU D 1 49  ? -20.233 -1.347  -17.249 1.00 23.44 ? 49  GLU D CB  1 
ATOM   3496 C CG  . GLU D 1 49  ? -19.336 -1.227  -18.393 1.00 28.37 ? 49  GLU D CG  1 
ATOM   3497 C CD  . GLU D 1 49  ? -18.929 -2.545  -18.906 1.00 34.21 ? 49  GLU D CD  1 
ATOM   3498 O OE1 . GLU D 1 49  ? -19.462 -3.524  -18.336 1.00 35.87 ? 49  GLU D OE1 1 
ATOM   3499 O OE2 . GLU D 1 49  ? -18.107 -2.583  -19.883 1.00 35.79 ? 49  GLU D OE2 1 
ATOM   3500 N N   . PHE D 1 50  ? -22.715 0.829   -18.136 1.00 23.73 ? 50  PHE D N   1 
ATOM   3501 C CA  . PHE D 1 50  ? -23.371 1.345   -19.353 1.00 22.75 ? 50  PHE D CA  1 
ATOM   3502 C C   . PHE D 1 50  ? -24.297 2.469   -19.015 1.00 23.28 ? 50  PHE D C   1 
ATOM   3503 O O   . PHE D 1 50  ? -25.065 2.332   -18.069 1.00 24.42 ? 50  PHE D O   1 
ATOM   3504 C CB  . PHE D 1 50  ? -24.192 0.246   -20.038 1.00 22.31 ? 50  PHE D CB  1 
ATOM   3505 C CG  . PHE D 1 50  ? -23.395 -0.951  -20.349 1.00 23.17 ? 50  PHE D CG  1 
ATOM   3506 C CD1 . PHE D 1 50  ? -22.344 -0.863  -21.209 1.00 24.45 ? 50  PHE D CD1 1 
ATOM   3507 C CD2 . PHE D 1 50  ? -23.647 -2.139  -19.723 1.00 22.85 ? 50  PHE D CD2 1 
ATOM   3508 C CE1 . PHE D 1 50  ? -21.572 -1.956  -21.457 1.00 27.12 ? 50  PHE D CE1 1 
ATOM   3509 C CE2 . PHE D 1 50  ? -22.883 -3.239  -19.968 1.00 23.02 ? 50  PHE D CE2 1 
ATOM   3510 C CZ  . PHE D 1 50  ? -21.850 -3.144  -20.829 1.00 25.21 ? 50  PHE D CZ  1 
ATOM   3511 N N   . GLY D 1 51  ? -24.228 3.540   -19.810 1.00 22.29 ? 51  GLY D N   1 
ATOM   3512 C CA  . GLY D 1 51  ? -25.056 4.718   -19.667 1.00 23.68 ? 51  GLY D CA  1 
ATOM   3513 C C   . GLY D 1 51  ? -26.319 4.524   -20.451 1.00 24.78 ? 51  GLY D C   1 
ATOM   3514 O O   . GLY D 1 51  ? -26.704 5.389   -21.187 1.00 24.57 ? 51  GLY D O   1 
ATOM   3515 N N   . ASP D 1 52  ? -26.895 3.330   -20.317 1.00 25.66 ? 52  ASP D N   1 
ATOM   3516 C CA  . ASP D 1 52  ? -28.101 2.867   -20.979 1.00 26.88 ? 52  ASP D CA  1 
ATOM   3517 C C   . ASP D 1 52  ? -29.292 2.812   -19.987 1.00 27.61 ? 52  ASP D C   1 
ATOM   3518 O O   . ASP D 1 52  ? -29.286 2.033   -19.058 1.00 29.61 ? 52  ASP D O   1 
ATOM   3519 C CB  . ASP D 1 52  ? -27.778 1.478   -21.532 1.00 25.97 ? 52  ASP D CB  1 
ATOM   3520 C CG  . ASP D 1 52  ? -28.791 0.975   -22.540 1.00 29.16 ? 52  ASP D CG  1 
ATOM   3521 O OD1 . ASP D 1 52  ? -29.967 1.423   -22.513 1.00 25.69 ? 52  ASP D OD1 1 
ATOM   3522 O OD2 . ASP D 1 52  ? -28.380 0.080   -23.333 1.00 29.64 ? 52  ASP D OD2 1 
ATOM   3523 N N   . ASN D 1 53  ? -30.307 3.642   -20.183 1.00 29.34 ? 53  ASN D N   1 
ATOM   3524 C CA  . ASN D 1 53  ? -31.516 3.660   -19.343 1.00 30.91 ? 53  ASN D CA  1 
ATOM   3525 C C   . ASN D 1 53  ? -32.752 3.088   -20.023 1.00 31.16 ? 53  ASN D C   1 
ATOM   3526 O O   . ASN D 1 53  ? -33.879 3.313   -19.573 1.00 31.02 ? 53  ASN D O   1 
ATOM   3527 C CB  . ASN D 1 53  ? -31.902 5.114   -18.957 1.00 31.62 ? 53  ASN D CB  1 
ATOM   3528 C CG  . ASN D 1 53  ? -32.965 5.156   -17.852 1.00 34.39 ? 53  ASN D CG  1 
ATOM   3529 O OD1 . ASN D 1 53  ? -32.922 4.330   -16.937 1.00 37.48 ? 53  ASN D OD1 1 
ATOM   3530 N ND2 . ASN D 1 53  ? -33.929 6.075   -17.941 1.00 34.85 ? 53  ASN D ND2 1 
ATOM   3531 N N   . ARG D 1 54  ? -32.564 2.400   -21.131 1.00 33.05 ? 54  ARG D N   1 
ATOM   3532 C CA  . ARG D 1 54  ? -33.700 2.146   -22.041 1.00 34.15 ? 54  ARG D CA  1 
ATOM   3533 C C   . ARG D 1 54  ? -34.785 1.231   -21.455 1.00 34.66 ? 54  ARG D C   1 
ATOM   3534 O O   . ARG D 1 54  ? -35.966 1.430   -21.731 1.00 34.19 ? 54  ARG D O   1 
ATOM   3535 C CB  . ARG D 1 54  ? -33.227 1.733   -23.441 1.00 33.80 ? 54  ARG D CB  1 
ATOM   3536 C CG  . ARG D 1 54  ? -32.998 0.300   -23.576 1.00 33.71 ? 54  ARG D CG  1 
ATOM   3537 C CD  . ARG D 1 54  ? -32.405 -0.005  -24.936 1.00 34.39 ? 54  ARG D CD  1 
ATOM   3538 N NE  . ARG D 1 54  ? -30.942 -0.026  -24.956 1.00 31.77 ? 54  ARG D NE  1 
ATOM   3539 C CZ  . ARG D 1 54  ? -30.232 -0.185  -26.077 1.00 36.48 ? 54  ARG D CZ  1 
ATOM   3540 N NH1 . ARG D 1 54  ? -30.876 -0.305  -27.256 1.00 36.36 ? 54  ARG D NH1 1 
ATOM   3541 N NH2 . ARG D 1 54  ? -28.890 -0.219  -26.037 1.00 34.41 ? 54  ARG D NH2 1 
ATOM   3542 N N   . ALA D 1 55  ? -34.382 0.308   -20.577 1.00 34.96 ? 55  ALA D N   1 
ATOM   3543 C CA  . ALA D 1 55  ? -35.332 -0.562  -19.910 1.00 33.93 ? 55  ALA D CA  1 
ATOM   3544 C C   . ALA D 1 55  ? -35.333 -0.223  -18.428 1.00 33.21 ? 55  ALA D C   1 
ATOM   3545 O O   . ALA D 1 55  ? -35.703 -1.033  -17.569 1.00 34.01 ? 55  ALA D O   1 
ATOM   3546 C CB  . ALA D 1 55  ? -34.952 -2.012  -20.155 1.00 35.35 ? 55  ALA D CB  1 
ATOM   3547 N N   . GLY D 1 56  ? -34.917 1.002   -18.133 1.00 31.30 ? 56  GLY D N   1 
ATOM   3548 C CA  . GLY D 1 56  ? -34.786 1.453   -16.766 1.00 29.67 ? 56  GLY D CA  1 
ATOM   3549 C C   . GLY D 1 56  ? -33.387 1.240   -16.214 1.00 28.09 ? 56  GLY D C   1 
ATOM   3550 O O   . GLY D 1 56  ? -32.377 1.229   -16.950 1.00 26.14 ? 56  GLY D O   1 
ATOM   3551 N N   . CYS D 1 57  ? -33.338 1.042   -14.900 1.00 27.44 ? 57  CYS D N   1 
ATOM   3552 C CA  . CYS D 1 57  ? -32.041 0.989   -14.182 1.00 28.13 ? 57  CYS D CA  1 
ATOM   3553 C C   . CYS D 1 57  ? -31.255 -0.245  -14.489 1.00 27.13 ? 57  CYS D C   1 
ATOM   3554 O O   . CYS D 1 57  ? -30.009 -0.219  -14.491 1.00 26.92 ? 57  CYS D O   1 
ATOM   3555 C CB  . CYS D 1 57  ? -32.219 1.167   -12.680 1.00 27.26 ? 57  CYS D CB  1 
ATOM   3556 S SG  . CYS D 1 57  ? -32.426 2.913   -12.236 1.00 29.67 ? 57  CYS D SG  1 
ATOM   3557 N N   . THR D 1 58  ? -32.000 -1.314  -14.749 1.00 27.01 ? 58  THR D N   1 
ATOM   3558 C CA  . THR D 1 58  ? -31.475 -2.638  -15.155 1.00 26.74 ? 58  THR D CA  1 
ATOM   3559 C C   . THR D 1 58  ? -30.566 -2.685  -16.412 1.00 25.97 ? 58  THR D C   1 
ATOM   3560 O O   . THR D 1 58  ? -29.700 -3.608  -16.525 1.00 24.95 ? 58  THR D O   1 
ATOM   3561 C CB  . THR D 1 58  ? -32.643 -3.633  -15.250 1.00 27.66 ? 58  THR D CB  1 
ATOM   3562 O OG1 . THR D 1 58  ? -33.202 -3.762  -13.936 1.00 31.73 ? 58  THR D OG1 1 
ATOM   3563 C CG2 . THR D 1 58  ? -32.164 -5.028  -15.622 1.00 30.30 ? 58  THR D CG2 1 
ATOM   3564 N N   . SER D 1 59  ? -30.726 -1.693  -17.323 1.00 23.86 ? 59  SER D N   1 
ATOM   3565 C CA  . SER D 1 59  ? -29.962 -1.654  -18.581 1.00 22.99 ? 59  SER D CA  1 
ATOM   3566 C C   . SER D 1 59  ? -28.510 -1.232  -18.391 1.00 22.80 ? 59  SER D C   1 
ATOM   3567 O O   . SER D 1 59  ? -27.648 -1.462  -19.246 1.00 21.74 ? 59  SER D O   1 
ATOM   3568 C CB  . SER D 1 59  ? -30.634 -0.749  -19.597 1.00 22.08 ? 59  SER D CB  1 
ATOM   3569 O OG  . SER D 1 59  ? -32.007 -0.808  -19.465 1.00 23.87 ? 59  SER D OG  1 
ATOM   3570 N N   . ALA D 1 60  ? -28.292 -0.612  -17.236 1.00 22.58 ? 60  ALA D N   1 
ATOM   3571 C CA  . ALA D 1 60  ? -27.027 -0.114  -16.752 1.00 22.72 ? 60  ALA D CA  1 
ATOM   3572 C C   . ALA D 1 60  ? -25.921 -1.157  -16.664 1.00 22.64 ? 60  ALA D C   1 
ATOM   3573 O O   . ALA D 1 60  ? -24.736 -0.803  -16.625 1.00 21.16 ? 60  ALA D O   1 
ATOM   3574 C CB  . ALA D 1 60  ? -27.255 0.544   -15.371 1.00 22.40 ? 60  ALA D CB  1 
ATOM   3575 N N   . GLY D 1 61  ? -26.322 -2.439  -16.567 1.00 24.20 ? 61  GLY D N   1 
ATOM   3576 C CA  . GLY D 1 61  ? -25.406 -3.557  -16.561 1.00 24.32 ? 61  GLY D CA  1 
ATOM   3577 C C   . GLY D 1 61  ? -24.726 -3.636  -15.209 1.00 24.72 ? 61  GLY D C   1 
ATOM   3578 O O   . GLY D 1 61  ? -25.244 -3.071  -14.227 1.00 25.52 ? 61  GLY D O   1 
ATOM   3579 N N   . PRO D 1 62  ? -23.578 -4.338  -15.136 1.00 24.53 ? 62  PRO D N   1 
ATOM   3580 C CA  . PRO D 1 62  ? -22.991 -4.630  -13.821 1.00 23.97 ? 62  PRO D CA  1 
ATOM   3581 C C   . PRO D 1 62  ? -22.143 -3.433  -13.358 1.00 23.58 ? 62  PRO D C   1 
ATOM   3582 O O   . PRO D 1 62  ? -21.949 -2.493  -14.128 1.00 21.44 ? 62  PRO D O   1 
ATOM   3583 C CB  . PRO D 1 62  ? -22.089 -5.779  -14.127 1.00 22.80 ? 62  PRO D CB  1 
ATOM   3584 C CG  . PRO D 1 62  ? -21.579 -5.433  -15.473 1.00 24.67 ? 62  PRO D CG  1 
ATOM   3585 C CD  . PRO D 1 62  ? -22.727 -4.848  -16.219 1.00 23.74 ? 62  PRO D CD  1 
ATOM   3586 N N   . HIS D 1 63  ? -21.591 -3.534  -12.152 1.00 23.89 ? 63  HIS D N   1 
ATOM   3587 C CA  . HIS D 1 63  ? -20.615 -2.606  -11.639 1.00 24.16 ? 63  HIS D CA  1 
ATOM   3588 C C   . HIS D 1 63  ? -19.552 -2.328  -12.670 1.00 25.53 ? 63  HIS D C   1 
ATOM   3589 O O   . HIS D 1 63  ? -19.051 -3.228  -13.320 1.00 24.92 ? 63  HIS D O   1 
ATOM   3590 C CB  . HIS D 1 63  ? -19.966 -3.117  -10.347 1.00 24.68 ? 63  HIS D CB  1 
ATOM   3591 C CG  . HIS D 1 63  ? -20.921 -3.271  -9.201  1.00 25.59 ? 63  HIS D CG  1 
ATOM   3592 N ND1 . HIS D 1 63  ? -20.573 -3.881  -8.018  1.00 29.58 ? 63  HIS D ND1 1 
ATOM   3593 C CD2 . HIS D 1 63  ? -22.216 -2.910  -9.061  1.00 26.67 ? 63  HIS D CD2 1 
ATOM   3594 C CE1 . HIS D 1 63  ? -21.595 -3.860  -7.185  1.00 24.96 ? 63  HIS D CE1 1 
ATOM   3595 N NE2 . HIS D 1 63  ? -22.608 -3.283  -7.795  1.00 25.63 ? 63  HIS D NE2 1 
ATOM   3596 N N   . PHE D 1 64  ? -19.206 -1.063  -12.811 1.00 25.90 ? 64  PHE D N   1 
ATOM   3597 C CA  . PHE D 1 64  ? -18.102 -0.728  -13.669 1.00 29.04 ? 64  PHE D CA  1 
ATOM   3598 C C   . PHE D 1 64  ? -16.807 -1.262  -13.036 1.00 30.67 ? 64  PHE D C   1 
ATOM   3599 O O   . PHE D 1 64  ? -16.433 -0.893  -11.918 1.00 29.31 ? 64  PHE D O   1 
ATOM   3600 C CB  . PHE D 1 64  ? -18.105 0.769   -13.944 1.00 27.35 ? 64  PHE D CB  1 
ATOM   3601 C CG  . PHE D 1 64  ? -16.918 1.255   -14.642 1.00 28.18 ? 64  PHE D CG  1 
ATOM   3602 C CD1 . PHE D 1 64  ? -16.621 0.813   -15.922 1.00 28.34 ? 64  PHE D CD1 1 
ATOM   3603 C CD2 . PHE D 1 64  ? -16.107 2.221   -14.040 1.00 23.75 ? 64  PHE D CD2 1 
ATOM   3604 C CE1 . PHE D 1 64  ? -15.513 1.275   -16.579 1.00 27.23 ? 64  PHE D CE1 1 
ATOM   3605 C CE2 . PHE D 1 64  ? -15.000 2.713   -14.695 1.00 28.57 ? 64  PHE D CE2 1 
ATOM   3606 C CZ  . PHE D 1 64  ? -14.687 2.253   -15.978 1.00 26.76 ? 64  PHE D CZ  1 
ATOM   3607 N N   . ASN D 1 65  ? -16.172 -2.168  -13.768 1.00 33.71 ? 65  ASN D N   1 
ATOM   3608 C CA  . ASN D 1 65  ? -14.950 -2.822  -13.324 1.00 36.24 ? 65  ASN D CA  1 
ATOM   3609 C C   . ASN D 1 65  ? -14.062 -3.139  -14.514 1.00 37.37 ? 65  ASN D C   1 
ATOM   3610 O O   . ASN D 1 65  ? -14.067 -4.297  -14.987 1.00 37.76 ? 65  ASN D O   1 
ATOM   3611 C CB  . ASN D 1 65  ? -15.252 -4.131  -12.573 1.00 37.01 ? 65  ASN D CB  1 
ATOM   3612 C CG  . ASN D 1 65  ? -14.148 -4.527  -11.562 1.00 39.34 ? 65  ASN D CG  1 
ATOM   3613 O OD1 . ASN D 1 65  ? -13.264 -3.717  -11.201 1.00 42.42 ? 65  ASN D OD1 1 
ATOM   3614 N ND2 . ASN D 1 65  ? -14.219 -5.780  -11.086 1.00 39.69 ? 65  ASN D ND2 1 
ATOM   3615 N N   . PRO D 1 66  ? -13.272 -2.141  -14.976 1.00 37.56 ? 66  PRO D N   1 
ATOM   3616 C CA  . PRO D 1 66  ? -12.276 -2.295  -16.019 1.00 38.25 ? 66  PRO D CA  1 
ATOM   3617 C C   . PRO D 1 66  ? -11.246 -3.361  -15.578 1.00 38.83 ? 66  PRO D C   1 
ATOM   3618 O O   . PRO D 1 66  ? -10.717 -4.120  -16.400 1.00 39.47 ? 66  PRO D O   1 
ATOM   3619 C CB  . PRO D 1 66  ? -11.565 -0.947  -16.026 1.00 38.17 ? 66  PRO D CB  1 
ATOM   3620 C CG  . PRO D 1 66  ? -12.453 -0.018  -15.378 1.00 38.90 ? 66  PRO D CG  1 
ATOM   3621 C CD  . PRO D 1 66  ? -13.249 -0.793  -14.398 1.00 38.42 ? 66  PRO D CD  1 
ATOM   3622 N N   . HIS D 1 80  ? -14.066 -3.041  -6.964  1.00 39.03 ? 80  HIS D N   1 
ATOM   3623 C CA  . HIS D 1 80  ? -14.524 -2.522  -8.256  1.00 39.14 ? 80  HIS D CA  1 
ATOM   3624 C C   . HIS D 1 80  ? -14.185 -1.035  -8.354  1.00 36.65 ? 80  HIS D C   1 
ATOM   3625 O O   . HIS D 1 80  ? -14.173 -0.347  -7.364  1.00 36.87 ? 80  HIS D O   1 
ATOM   3626 C CB  . HIS D 1 80  ? -16.057 -2.701  -8.459  1.00 40.69 ? 80  HIS D CB  1 
ATOM   3627 C CG  . HIS D 1 80  ? -16.556 -4.124  -8.353  1.00 46.04 ? 80  HIS D CG  1 
ATOM   3628 N ND1 . HIS D 1 80  ? -17.799 -4.436  -7.842  1.00 47.52 ? 80  HIS D ND1 1 
ATOM   3629 C CD2 . HIS D 1 80  ? -15.996 -5.310  -8.719  1.00 51.04 ? 80  HIS D CD2 1 
ATOM   3630 C CE1 . HIS D 1 80  ? -17.983 -5.745  -7.898  1.00 49.69 ? 80  HIS D CE1 1 
ATOM   3631 N NE2 . HIS D 1 80  ? -16.902 -6.299  -8.421  1.00 50.67 ? 80  HIS D NE2 1 
ATOM   3632 N N   . VAL D 1 81  ? -13.908 -0.555  -9.556  1.00 35.40 ? 81  VAL D N   1 
ATOM   3633 C CA  . VAL D 1 81  ? -13.691 0.885   -9.839  1.00 33.01 ? 81  VAL D CA  1 
ATOM   3634 C C   . VAL D 1 81  ? -14.961 1.740   -9.533  1.00 32.37 ? 81  VAL D C   1 
ATOM   3635 O O   . VAL D 1 81  ? -14.903 2.871   -8.998  1.00 33.49 ? 81  VAL D O   1 
ATOM   3636 C CB  . VAL D 1 81  ? -13.261 1.074   -11.321 1.00 32.58 ? 81  VAL D CB  1 
ATOM   3637 C CG1 . VAL D 1 81  ? -13.202 2.534   -11.701 1.00 31.35 ? 81  VAL D CG1 1 
ATOM   3638 C CG2 . VAL D 1 81  ? -11.911 0.420   -11.604 1.00 32.54 ? 81  VAL D CG2 1 
ATOM   3639 N N   . GLY D 1 82  ? -16.103 1.175   -9.860  1.00 29.96 ? 82  GLY D N   1 
ATOM   3640 C CA  . GLY D 1 82  ? -17.365 1.788   -9.599  1.00 27.76 ? 82  GLY D CA  1 
ATOM   3641 C C   . GLY D 1 82  ? -17.794 1.982   -8.180  1.00 27.02 ? 82  GLY D C   1 
ATOM   3642 O O   . GLY D 1 82  ? -18.632 2.830   -7.927  1.00 24.64 ? 82  GLY D O   1 
ATOM   3643 N N   . ASP D 1 83  ? -17.234 1.168   -7.271  1.00 26.74 ? 83  ASP D N   1 
ATOM   3644 C CA  . ASP D 1 83  ? -17.680 0.989   -5.858  1.00 27.06 ? 83  ASP D CA  1 
ATOM   3645 C C   . ASP D 1 83  ? -17.569 2.283   -5.112  1.00 26.67 ? 83  ASP D C   1 
ATOM   3646 O O   . ASP D 1 83  ? -16.463 2.615   -4.660  1.00 27.98 ? 83  ASP D O   1 
ATOM   3647 C CB  . ASP D 1 83  ? -16.714 0.019   -5.154  1.00 27.50 ? 83  ASP D CB  1 
ATOM   3648 C CG  . ASP D 1 83  ? -17.401 -1.035  -4.322  1.00 30.84 ? 83  ASP D CG  1 
ATOM   3649 O OD1 . ASP D 1 83  ? -16.995 -2.253  -4.517  1.00 31.73 ? 83  ASP D OD1 1 
ATOM   3650 O OD2 . ASP D 1 83  ? -18.294 -0.689  -3.448  1.00 28.83 ? 83  ASP D OD2 1 
ATOM   3651 N N   . LEU D 1 84  ? -18.668 3.005   -4.899  1.00 25.72 ? 84  LEU D N   1 
ATOM   3652 C CA  . LEU D 1 84  ? -18.501 4.210   -4.136  1.00 25.47 ? 84  LEU D CA  1 
ATOM   3653 C C   . LEU D 1 84  ? -18.937 4.058   -2.657  1.00 25.74 ? 84  LEU D C   1 
ATOM   3654 O O   . LEU D 1 84  ? -19.123 5.039   -1.944  1.00 26.24 ? 84  LEU D O   1 
ATOM   3655 C CB  . LEU D 1 84  ? -19.129 5.424   -4.863  1.00 25.91 ? 84  LEU D CB  1 
ATOM   3656 C CG  . LEU D 1 84  ? -18.551 5.766   -6.245  1.00 24.49 ? 84  LEU D CG  1 
ATOM   3657 C CD1 . LEU D 1 84  ? -19.301 6.980   -6.824  1.00 24.06 ? 84  LEU D CD1 1 
ATOM   3658 C CD2 . LEU D 1 84  ? -17.037 6.079   -6.153  1.00 19.78 ? 84  LEU D CD2 1 
ATOM   3659 N N   . GLY D 1 85  ? -19.035 2.819   -2.189  1.00 24.50 ? 85  GLY D N   1 
ATOM   3660 C CA  . GLY D 1 85  ? -19.619 2.571   -0.894  1.00 24.49 ? 85  GLY D CA  1 
ATOM   3661 C C   . GLY D 1 85  ? -21.140 2.830   -0.778  1.00 23.68 ? 85  GLY D C   1 
ATOM   3662 O O   . GLY D 1 85  ? -21.923 2.453   -1.657  1.00 23.65 ? 85  GLY D O   1 
ATOM   3663 N N   . ASN D 1 86  ? -21.560 3.423   0.340   1.00 21.75 ? 86  ASN D N   1 
ATOM   3664 C CA  . ASN D 1 86  ? -22.953 3.733   0.548   1.00 20.61 ? 86  ASN D CA  1 
ATOM   3665 C C   . ASN D 1 86  ? -23.104 5.241   0.679   1.00 19.14 ? 86  ASN D C   1 
ATOM   3666 O O   . ASN D 1 86  ? -22.109 5.992   0.644   1.00 17.57 ? 86  ASN D O   1 
ATOM   3667 C CB  . ASN D 1 86  ? -23.575 3.083   1.804   1.00 22.19 ? 86  ASN D CB  1 
ATOM   3668 C CG  . ASN D 1 86  ? -23.220 1.616   1.976   1.00 23.59 ? 86  ASN D CG  1 
ATOM   3669 O OD1 . ASN D 1 86  ? -23.803 0.738   1.336   1.00 27.63 ? 86  ASN D OD1 1 
ATOM   3670 N ND2 . ASN D 1 86  ? -22.260 1.336   2.874   1.00 27.26 ? 86  ASN D ND2 1 
ATOM   3671 N N   . VAL D 1 87  ? -24.369 5.647   0.603   1.00 17.70 ? 87  VAL D N   1 
ATOM   3672 C CA  . VAL D 1 87  ? -24.859 6.960   0.948   1.00 17.63 ? 87  VAL D CA  1 
ATOM   3673 C C   . VAL D 1 87  ? -25.898 6.669   2.069   1.00 17.34 ? 87  VAL D C   1 
ATOM   3674 O O   . VAL D 1 87  ? -26.428 5.533   2.150   1.00 14.37 ? 87  VAL D O   1 
ATOM   3675 C CB  . VAL D 1 87  ? -25.444 7.796   -0.227  1.00 17.77 ? 87  VAL D CB  1 
ATOM   3676 C CG1 . VAL D 1 87  ? -24.357 8.052   -1.255  1.00 16.70 ? 87  VAL D CG1 1 
ATOM   3677 C CG2 . VAL D 1 87  ? -26.731 7.209   -0.818  1.00 17.07 ? 87  VAL D CG2 1 
ATOM   3678 N N   . THR D 1 88  ? -26.074 7.636   2.973   1.00 16.91 ? 88  THR D N   1 
ATOM   3679 C CA  . THR D 1 88  ? -26.946 7.406   4.126   1.00 18.22 ? 88  THR D CA  1 
ATOM   3680 C C   . THR D 1 88  ? -28.136 8.346   4.181   1.00 18.91 ? 88  THR D C   1 
ATOM   3681 O O   . THR D 1 88  ? -27.976 9.589   4.175   1.00 16.12 ? 88  THR D O   1 
ATOM   3682 C CB  . THR D 1 88  ? -26.181 7.363   5.499   1.00 19.27 ? 88  THR D CB  1 
ATOM   3683 O OG1 . THR D 1 88  ? -24.862 6.769   5.344   1.00 26.21 ? 88  THR D OG1 1 
ATOM   3684 C CG2 . THR D 1 88  ? -26.954 6.443   6.508   1.00 16.75 ? 88  THR D CG2 1 
ATOM   3685 N N   . ALA D 1 89  ? -29.334 7.759   4.270   1.00 20.03 ? 89  ALA D N   1 
ATOM   3686 C CA  . ALA D 1 89  ? -30.532 8.607   4.343   1.00 22.83 ? 89  ALA D CA  1 
ATOM   3687 C C   . ALA D 1 89  ? -30.890 8.936   5.802   1.00 24.16 ? 89  ALA D C   1 
ATOM   3688 O O   . ALA D 1 89  ? -30.853 8.056   6.643   1.00 26.84 ? 89  ALA D O   1 
ATOM   3689 C CB  . ALA D 1 89  ? -31.699 7.999   3.564   1.00 21.24 ? 89  ALA D CB  1 
ATOM   3690 N N   . ASP D 1 90  ? -31.112 10.221  6.118   1.00 26.62 ? 90  ASP D N   1 
ATOM   3691 C CA  . ASP D 1 90  ? -31.527 10.679  7.466   1.00 27.07 ? 90  ASP D CA  1 
ATOM   3692 C C   . ASP D 1 90  ? -32.964 10.211  7.730   1.00 28.60 ? 90  ASP D C   1 
ATOM   3693 O O   . ASP D 1 90  ? -33.522 9.455   6.918   1.00 28.14 ? 90  ASP D O   1 
ATOM   3694 C CB  . ASP D 1 90  ? -31.423 12.227  7.602   1.00 26.65 ? 90  ASP D CB  1 
ATOM   3695 C CG  . ASP D 1 90  ? -32.419 12.982  6.716   1.00 26.89 ? 90  ASP D CG  1 
ATOM   3696 O OD1 . ASP D 1 90  ? -33.212 12.352  5.982   1.00 28.72 ? 90  ASP D OD1 1 
ATOM   3697 O OD2 . ASP D 1 90  ? -32.443 14.228  6.760   1.00 26.97 ? 90  ASP D OD2 1 
ATOM   3698 N N   . LYS D 1 91  ? -33.581 10.663  8.834   1.00 29.51 ? 91  LYS D N   1 
ATOM   3699 C CA  . LYS D 1 91  ? -34.926 10.187  9.176   1.00 31.70 ? 91  LYS D CA  1 
ATOM   3700 C C   . LYS D 1 91  ? -36.029 10.525  8.168   1.00 32.15 ? 91  LYS D C   1 
ATOM   3701 O O   . LYS D 1 91  ? -37.024 9.789   8.068   1.00 32.73 ? 91  LYS D O   1 
ATOM   3702 C CB  . LYS D 1 91  ? -35.365 10.581  10.613  1.00 31.73 ? 91  LYS D CB  1 
ATOM   3703 C CG  . LYS D 1 91  ? -35.569 12.062  10.878  1.00 32.68 ? 91  LYS D CG  1 
ATOM   3704 C CD  . LYS D 1 91  ? -36.133 12.269  12.295  1.00 34.81 ? 91  LYS D CD  1 
ATOM   3705 C CE  . LYS D 1 91  ? -35.945 13.714  12.764  1.00 39.30 ? 91  LYS D CE  1 
ATOM   3706 N NZ  . LYS D 1 91  ? -36.466 14.723  11.765  1.00 41.80 ? 91  LYS D NZ  1 
ATOM   3707 N N   . ASP D 1 92  ? -35.870 11.645  7.460   1.00 32.23 ? 92  ASP D N   1 
ATOM   3708 C CA  . ASP D 1 92  ? -36.856 12.080  6.506   1.00 32.31 ? 92  ASP D CA  1 
ATOM   3709 C C   . ASP D 1 92  ? -36.527 11.601  5.103   1.00 31.45 ? 92  ASP D C   1 
ATOM   3710 O O   . ASP D 1 92  ? -37.141 12.076  4.161   1.00 30.79 ? 92  ASP D O   1 
ATOM   3711 C CB  . ASP D 1 92  ? -37.020 13.605  6.501   1.00 33.47 ? 92  ASP D CB  1 
ATOM   3712 C CG  . ASP D 1 92  ? -37.289 14.183  7.896   1.00 35.72 ? 92  ASP D CG  1 
ATOM   3713 O OD1 . ASP D 1 92  ? -38.140 13.624  8.637   1.00 37.22 ? 92  ASP D OD1 1 
ATOM   3714 O OD2 . ASP D 1 92  ? -36.628 15.198  8.232   1.00 39.01 ? 92  ASP D OD2 1 
ATOM   3715 N N   . GLY D 1 93  ? -35.596 10.661  4.977   1.00 29.89 ? 93  GLY D N   1 
ATOM   3716 C CA  . GLY D 1 93  ? -35.264 10.073  3.659   1.00 30.49 ? 93  GLY D CA  1 
ATOM   3717 C C   . GLY D 1 93  ? -34.307 10.888  2.774   1.00 30.63 ? 93  GLY D C   1 
ATOM   3718 O O   . GLY D 1 93  ? -34.188 10.625  1.575   1.00 30.80 ? 93  GLY D O   1 
ATOM   3719 N N   . VAL D 1 94  ? -33.589 11.839  3.376   1.00 29.96 ? 94  VAL D N   1 
ATOM   3720 C CA  . VAL D 1 94  ? -32.687 12.709  2.640   1.00 29.51 ? 94  VAL D CA  1 
ATOM   3721 C C   . VAL D 1 94  ? -31.232 12.304  2.937   1.00 30.01 ? 94  VAL D C   1 
ATOM   3722 O O   . VAL D 1 94  ? -30.849 12.136  4.099   1.00 29.36 ? 94  VAL D O   1 
ATOM   3723 C CB  . VAL D 1 94  ? -32.963 14.209  2.948   1.00 29.64 ? 94  VAL D CB  1 
ATOM   3724 C CG1 . VAL D 1 94  ? -31.882 15.128  2.315   1.00 28.90 ? 94  VAL D CG1 1 
ATOM   3725 C CG2 . VAL D 1 94  ? -34.320 14.586  2.459   1.00 24.66 ? 94  VAL D CG2 1 
ATOM   3726 N N   . ALA D 1 95  ? -30.464 12.086  1.875   1.00 29.19 ? 95  ALA D N   1 
ATOM   3727 C CA  . ALA D 1 95  ? -29.047 11.806  1.971   1.00 29.71 ? 95  ALA D CA  1 
ATOM   3728 C C   . ALA D 1 95  ? -28.226 12.932  1.366   1.00 30.69 ? 95  ALA D C   1 
ATOM   3729 O O   . ALA D 1 95  ? -28.385 13.231  0.188   1.00 30.07 ? 95  ALA D O   1 
ATOM   3730 C CB  . ALA D 1 95  ? -28.706 10.462  1.270   1.00 29.00 ? 95  ALA D CB  1 
ATOM   3731 N N   . ASP D 1 96  ? -27.356 13.529  2.187   1.00 31.74 ? 96  ASP D N   1 
ATOM   3732 C CA  . ASP D 1 96  ? -26.444 14.582  1.779   1.00 32.41 ? 96  ASP D CA  1 
ATOM   3733 C C   . ASP D 1 96  ? -25.137 13.896  1.514   1.00 31.35 ? 96  ASP D C   1 
ATOM   3734 O O   . ASP D 1 96  ? -24.427 13.453  2.432   1.00 32.31 ? 96  ASP D O   1 
ATOM   3735 C CB  . ASP D 1 96  ? -26.327 15.728  2.831   1.00 32.81 ? 96  ASP D CB  1 
ATOM   3736 C CG  . ASP D 1 96  ? -27.601 16.635  2.858   1.00 39.60 ? 96  ASP D CG  1 
ATOM   3737 O OD1 . ASP D 1 96  ? -27.968 17.211  1.773   1.00 39.01 ? 96  ASP D OD1 1 
ATOM   3738 O OD2 . ASP D 1 96  ? -28.255 16.743  3.953   1.00 43.99 ? 96  ASP D OD2 1 
ATOM   3739 N N   . VAL D 1 97  ? -24.819 13.804  0.230   1.00 29.39 ? 97  VAL D N   1 
ATOM   3740 C CA  . VAL D 1 97  ? -23.727 12.966  -0.201  1.00 26.28 ? 97  VAL D CA  1 
ATOM   3741 C C   . VAL D 1 97  ? -22.457 13.769  -0.200  1.00 25.92 ? 97  VAL D C   1 
ATOM   3742 O O   . VAL D 1 97  ? -22.426 14.957  -0.554  1.00 25.71 ? 97  VAL D O   1 
ATOM   3743 C CB  . VAL D 1 97  ? -24.053 12.331  -1.544  1.00 26.51 ? 97  VAL D CB  1 
ATOM   3744 C CG1 . VAL D 1 97  ? -22.918 11.426  -1.999  1.00 24.03 ? 97  VAL D CG1 1 
ATOM   3745 C CG2 . VAL D 1 97  ? -25.333 11.635  -1.392  1.00 18.02 ? 97  VAL D CG2 1 
ATOM   3746 N N   . SER D 1 98  ? -21.424 13.165  0.338   1.00 25.44 ? 98  SER D N   1 
ATOM   3747 C CA  . SER D 1 98  ? -20.087 13.785  0.269   1.00 26.66 ? 98  SER D CA  1 
ATOM   3748 C C   . SER D 1 98  ? -19.050 12.693  0.314   1.00 26.24 ? 98  SER D C   1 
ATOM   3749 O O   . SER D 1 98  ? -18.925 11.996  1.363   1.00 27.80 ? 98  SER D O   1 
ATOM   3750 C CB  . SER D 1 98  ? -19.871 14.750  1.406   1.00 25.33 ? 98  SER D CB  1 
ATOM   3751 O OG  . SER D 1 98  ? -18.592 15.320  1.275   1.00 30.53 ? 98  SER D OG  1 
ATOM   3752 N N   . ILE D 1 99  ? -18.335 12.530  -0.806  1.00 25.38 ? 99  ILE D N   1 
ATOM   3753 C CA  . ILE D 1 99  ? -17.344 11.470  -0.994  1.00 24.42 ? 99  ILE D CA  1 
ATOM   3754 C C   . ILE D 1 99  ? -16.095 12.012  -1.744  1.00 26.57 ? 99  ILE D C   1 
ATOM   3755 O O   . ILE D 1 99  ? -16.218 12.931  -2.539  1.00 26.55 ? 99  ILE D O   1 
ATOM   3756 C CB  . ILE D 1 99  ? -17.976 10.242  -1.757  1.00 24.45 ? 99  ILE D CB  1 
ATOM   3757 C CG1 . ILE D 1 99  ? -19.088 9.596   -0.936  1.00 22.12 ? 99  ILE D CG1 1 
ATOM   3758 C CG2 . ILE D 1 99  ? -16.920 9.145   -2.116  1.00 25.15 ? 99  ILE D CG2 1 
ATOM   3759 C CD1 . ILE D 1 99  ? -20.176 8.799   -1.755  1.00 23.21 ? 99  ILE D CD1 1 
ATOM   3760 N N   . GLU D 1 100 ? -14.912 11.427  -1.470  1.00 28.30 ? 100 GLU D N   1 
ATOM   3761 C CA  . GLU D 1 100 ? -13.752 11.465  -2.349  1.00 29.60 ? 100 GLU D CA  1 
ATOM   3762 C C   . GLU D 1 100 ? -13.316 10.039  -2.797  1.00 30.55 ? 100 GLU D C   1 
ATOM   3763 O O   . GLU D 1 100 ? -13.176 9.123   -1.989  1.00 31.07 ? 100 GLU D O   1 
ATOM   3764 C CB  . GLU D 1 100 ? -12.622 12.198  -1.645  1.00 30.66 ? 100 GLU D CB  1 
ATOM   3765 C CG  . GLU D 1 100 ? -11.477 12.568  -2.565  1.00 34.58 ? 100 GLU D CG  1 
ATOM   3766 C CD  . GLU D 1 100 ? -10.332 13.227  -1.786  1.00 39.51 ? 100 GLU D CD  1 
ATOM   3767 O OE1 . GLU D 1 100 ? -10.225 14.475  -1.856  1.00 36.50 ? 100 GLU D OE1 1 
ATOM   3768 O OE2 . GLU D 1 100 ? -9.580  12.480  -1.083  1.00 41.62 ? 100 GLU D OE2 1 
ATOM   3769 N N   . ASP D 1 101 ? -13.124 9.835   -4.099  1.00 31.46 ? 101 ASP D N   1 
ATOM   3770 C CA  . ASP D 1 101 ? -12.549 8.591   -4.594  1.00 30.56 ? 101 ASP D CA  1 
ATOM   3771 C C   . ASP D 1 101 ? -11.351 8.814   -5.547  1.00 31.42 ? 101 ASP D C   1 
ATOM   3772 O O   . ASP D 1 101 ? -11.408 9.657   -6.469  1.00 31.17 ? 101 ASP D O   1 
ATOM   3773 C CB  . ASP D 1 101 ? -13.612 7.771   -5.291  1.00 30.17 ? 101 ASP D CB  1 
ATOM   3774 C CG  . ASP D 1 101 ? -13.202 6.293   -5.439  1.00 30.96 ? 101 ASP D CG  1 
ATOM   3775 O OD1 . ASP D 1 101 ? -13.050 5.620   -4.397  1.00 34.95 ? 101 ASP D OD1 1 
ATOM   3776 O OD2 . ASP D 1 101 ? -12.974 5.800   -6.570  1.00 28.41 ? 101 ASP D OD2 1 
ATOM   3777 N N   . SER D 1 102 ? -10.290 8.019   -5.350  1.00 31.62 ? 102 SER D N   1 
ATOM   3778 C CA  . SER D 1 102 ? -9.054  8.030   -6.188  1.00 32.26 ? 102 SER D CA  1 
ATOM   3779 C C   . SER D 1 102 ? -9.006  6.870   -7.174  1.00 32.06 ? 102 SER D C   1 
ATOM   3780 O O   . SER D 1 102 ? -7.926  6.564   -7.739  1.00 33.03 ? 102 SER D O   1 
ATOM   3781 C CB  . SER D 1 102 ? -7.791  7.883   -5.300  1.00 33.00 ? 102 SER D CB  1 
ATOM   3782 O OG  . SER D 1 102 ? -7.936  8.519   -4.031  1.00 34.62 ? 102 SER D OG  1 
ATOM   3783 N N   . VAL D 1 103 ? -10.123 6.159   -7.348  1.00 30.65 ? 103 VAL D N   1 
ATOM   3784 C CA  . VAL D 1 103 ? -10.099 4.969   -8.244  1.00 29.73 ? 103 VAL D CA  1 
ATOM   3785 C C   . VAL D 1 103 ? -10.868 5.334   -9.521  1.00 29.69 ? 103 VAL D C   1 
ATOM   3786 O O   . VAL D 1 103 ? -10.370 5.129   -10.646 1.00 29.42 ? 103 VAL D O   1 
ATOM   3787 C CB  . VAL D 1 103 ? -10.571 3.686   -7.523  1.00 29.10 ? 103 VAL D CB  1 
ATOM   3788 C CG1 . VAL D 1 103 ? -10.855 2.569   -8.478  1.00 29.16 ? 103 VAL D CG1 1 
ATOM   3789 C CG2 . VAL D 1 103 ? -9.541  3.282   -6.497  1.00 30.54 ? 103 VAL D CG2 1 
ATOM   3790 N N   . ILE D 1 104 ? -12.043 5.945   -9.327  1.00 27.70 ? 104 ILE D N   1 
ATOM   3791 C CA  . ILE D 1 104 ? -12.786 6.510   -10.432 1.00 26.02 ? 104 ILE D CA  1 
ATOM   3792 C C   . ILE D 1 104 ? -11.991 7.711   -10.956 1.00 25.74 ? 104 ILE D C   1 
ATOM   3793 O O   . ILE D 1 104 ? -11.098 8.189   -10.280 1.00 26.67 ? 104 ILE D O   1 
ATOM   3794 C CB  . ILE D 1 104 ? -14.277 6.898   -10.047 1.00 24.86 ? 104 ILE D CB  1 
ATOM   3795 C CG1 . ILE D 1 104 ? -14.324 8.102   -9.108  1.00 23.86 ? 104 ILE D CG1 1 
ATOM   3796 C CG2 . ILE D 1 104 ? -14.995 5.688   -9.479  1.00 24.76 ? 104 ILE D CG2 1 
ATOM   3797 C CD1 . ILE D 1 104 ? -15.712 8.513   -8.634  1.00 21.21 ? 104 ILE D CD1 1 
ATOM   3798 N N   . SER D 1 105 ? -12.343 8.168   -12.155 1.00 24.57 ? 105 SER D N   1 
ATOM   3799 C CA  . SER D 1 105 ? -11.709 9.280   -12.824 1.00 24.33 ? 105 SER D CA  1 
ATOM   3800 C C   . SER D 1 105 ? -12.720 9.895   -13.796 1.00 24.54 ? 105 SER D C   1 
ATOM   3801 O O   . SER D 1 105 ? -13.765 9.326   -14.119 1.00 23.64 ? 105 SER D O   1 
ATOM   3802 C CB  . SER D 1 105 ? -10.403 8.785   -13.550 1.00 24.52 ? 105 SER D CB  1 
ATOM   3803 O OG  . SER D 1 105 ? -9.719  9.821   -14.266 1.00 22.83 ? 105 SER D OG  1 
ATOM   3804 N N   . LEU D 1 106 ? -12.404 11.088  -14.284 1.00 25.26 ? 106 LEU D N   1 
ATOM   3805 C CA  . LEU D 1 106 ? -13.224 11.768  -15.277 1.00 25.69 ? 106 LEU D CA  1 
ATOM   3806 C C   . LEU D 1 106 ? -12.529 11.817  -16.660 1.00 26.15 ? 106 LEU D C   1 
ATOM   3807 O O   . LEU D 1 106 ? -12.894 12.621  -17.491 1.00 26.99 ? 106 LEU D O   1 
ATOM   3808 C CB  . LEU D 1 106 ? -13.578 13.176  -14.753 1.00 24.51 ? 106 LEU D CB  1 
ATOM   3809 C CG  . LEU D 1 106 ? -14.507 13.186  -13.518 1.00 23.12 ? 106 LEU D CG  1 
ATOM   3810 C CD1 . LEU D 1 106 ? -14.832 14.645  -13.281 1.00 19.97 ? 106 LEU D CD1 1 
ATOM   3811 C CD2 . LEU D 1 106 ? -15.863 12.290  -13.648 1.00 18.94 ? 106 LEU D CD2 1 
ATOM   3812 N N   . SER D 1 107 ? -11.521 10.965  -16.878 1.00 26.80 ? 107 SER D N   1 
ATOM   3813 C CA  . SER D 1 107 ? -10.731 10.836  -18.146 1.00 27.96 ? 107 SER D CA  1 
ATOM   3814 C C   . SER D 1 107 ? -9.947  9.511   -18.089 1.00 28.16 ? 107 SER D C   1 
ATOM   3815 O O   . SER D 1 107 ? -9.922  8.884   -17.031 1.00 28.79 ? 107 SER D O   1 
ATOM   3816 C CB  . SER D 1 107 ? -9.760  12.007  -18.388 1.00 28.12 ? 107 SER D CB  1 
ATOM   3817 O OG  . SER D 1 107 ? -8.599  11.925  -17.546 1.00 31.96 ? 107 SER D OG  1 
ATOM   3818 N N   . GLY D 1 108 ? -9.334  9.072   -19.195 1.00 27.82 ? 108 GLY D N   1 
ATOM   3819 C CA  . GLY D 1 108 ? -8.519  7.859   -19.174 1.00 27.78 ? 108 GLY D CA  1 
ATOM   3820 C C   . GLY D 1 108 ? -9.329  6.600   -18.891 1.00 28.85 ? 108 GLY D C   1 
ATOM   3821 O O   . GLY D 1 108 ? -10.546 6.674   -18.910 1.00 29.62 ? 108 GLY D O   1 
ATOM   3822 N N   . ASP D 1 109 ? -8.647  5.481   -18.590 1.00 28.31 ? 109 ASP D N   1 
ATOM   3823 C CA  . ASP D 1 109 ? -9.220  4.098   -18.440 1.00 28.25 ? 109 ASP D CA  1 
ATOM   3824 C C   . ASP D 1 109 ? -10.239 3.955   -17.320 1.00 26.43 ? 109 ASP D C   1 
ATOM   3825 O O   . ASP D 1 109 ? -10.994 2.980   -17.264 1.00 25.20 ? 109 ASP D O   1 
ATOM   3826 C CB  . ASP D 1 109 ? -8.075  3.075   -18.149 1.00 28.59 ? 109 ASP D CB  1 
ATOM   3827 C CG  . ASP D 1 109 ? -7.213  2.715   -19.423 1.00 35.29 ? 109 ASP D CG  1 
ATOM   3828 O OD1 . ASP D 1 109 ? -6.218  1.942   -19.284 1.00 35.39 ? 109 ASP D OD1 1 
ATOM   3829 O OD2 . ASP D 1 109 ? -7.536  3.173   -20.574 1.00 39.92 ? 109 ASP D OD2 1 
ATOM   3830 N N   . HIS D 1 110 ? -10.173 4.879   -16.364 1.00 25.05 ? 110 HIS D N   1 
ATOM   3831 C CA  . HIS D 1 110 ? -11.036 4.771   -15.215 1.00 25.02 ? 110 HIS D CA  1 
ATOM   3832 C C   . HIS D 1 110 ? -12.208 5.715   -15.329 1.00 23.59 ? 110 HIS D C   1 
ATOM   3833 O O   . HIS D 1 110 ? -13.004 5.761   -14.419 1.00 22.66 ? 110 HIS D O   1 
ATOM   3834 C CB  . HIS D 1 110 ? -10.227 4.925   -13.887 1.00 25.31 ? 110 HIS D CB  1 
ATOM   3835 C CG  . HIS D 1 110 ? -9.631  3.634   -13.435 1.00 26.42 ? 110 HIS D CG  1 
ATOM   3836 N ND1 . HIS D 1 110 ? -9.314  3.368   -12.123 1.00 31.58 ? 110 HIS D ND1 1 
ATOM   3837 C CD2 . HIS D 1 110 ? -9.364  2.493   -14.128 1.00 23.54 ? 110 HIS D CD2 1 
ATOM   3838 C CE1 . HIS D 1 110 ? -8.893  2.110   -12.024 1.00 26.69 ? 110 HIS D CE1 1 
ATOM   3839 N NE2 . HIS D 1 110 ? -8.919  1.566   -13.226 1.00 24.89 ? 110 HIS D NE2 1 
ATOM   3840 N N   . CYS D 1 111 ? -12.299 6.400   -16.493 1.00 23.58 ? 111 CYS D N   1 
ATOM   3841 C CA  . CYS D 1 111 ? -13.372 7.354   -16.850 1.00 22.92 ? 111 CYS D CA  1 
ATOM   3842 C C   . CYS D 1 111 ? -14.816 6.852   -16.645 1.00 21.67 ? 111 CYS D C   1 
ATOM   3843 O O   . CYS D 1 111 ? -15.210 5.787   -17.109 1.00 21.12 ? 111 CYS D O   1 
ATOM   3844 C CB  . CYS D 1 111 ? -13.263 7.824   -18.292 1.00 22.30 ? 111 CYS D CB  1 
ATOM   3845 S SG  . CYS D 1 111 ? -14.310 9.294   -18.579 1.00 23.05 ? 111 CYS D SG  1 
ATOM   3846 N N   . ILE D 1 112 ? -15.581 7.655   -15.954 1.00 20.47 ? 112 ILE D N   1 
ATOM   3847 C CA  . ILE D 1 112 ? -16.909 7.272   -15.637 1.00 20.60 ? 112 ILE D CA  1 
ATOM   3848 C C   . ILE D 1 112 ? -17.997 8.066   -16.437 1.00 20.63 ? 112 ILE D C   1 
ATOM   3849 O O   . ILE D 1 112 ? -19.152 7.705   -16.342 1.00 19.10 ? 112 ILE D O   1 
ATOM   3850 C CB  . ILE D 1 112 ? -17.160 7.396   -14.116 1.00 20.52 ? 112 ILE D CB  1 
ATOM   3851 C CG1 . ILE D 1 112 ? -16.879 8.840   -13.619 1.00 22.16 ? 112 ILE D CG1 1 
ATOM   3852 C CG2 . ILE D 1 112 ? -16.363 6.324   -13.352 1.00 19.29 ? 112 ILE D CG2 1 
ATOM   3853 C CD1 . ILE D 1 112 ? -17.597 9.232   -12.358 1.00 19.61 ? 112 ILE D CD1 1 
ATOM   3854 N N   . ILE D 1 113 ? -17.606 9.108   -17.205 1.00 20.01 ? 113 ILE D N   1 
ATOM   3855 C CA  . ILE D 1 113 ? -18.535 9.964   -17.987 1.00 21.08 ? 113 ILE D CA  1 
ATOM   3856 C C   . ILE D 1 113 ? -19.149 9.055   -19.006 1.00 20.72 ? 113 ILE D C   1 
ATOM   3857 O O   . ILE D 1 113 ? -18.423 8.241   -19.602 1.00 21.95 ? 113 ILE D O   1 
ATOM   3858 C CB  . ILE D 1 113 ? -17.778 11.193  -18.661 1.00 23.08 ? 113 ILE D CB  1 
ATOM   3859 C CG1 . ILE D 1 113 ? -16.785 11.771  -17.667 1.00 20.46 ? 113 ILE D CG1 1 
ATOM   3860 C CG2 . ILE D 1 113 ? -18.725 12.301  -19.102 1.00 22.13 ? 113 ILE D CG2 1 
ATOM   3861 C CD1 . ILE D 1 113 ? -16.617 13.215  -17.731 1.00 25.10 ? 113 ILE D CD1 1 
ATOM   3862 N N   . GLY D 1 114 ? -20.473 9.089   -19.143 1.00 19.50 ? 114 GLY D N   1 
ATOM   3863 C CA  . GLY D 1 114 ? -21.177 8.248   -20.076 1.00 17.33 ? 114 GLY D CA  1 
ATOM   3864 C C   . GLY D 1 114 ? -21.602 6.890   -19.534 1.00 17.84 ? 114 GLY D C   1 
ATOM   3865 O O   . GLY D 1 114 ? -22.154 6.065   -20.274 1.00 18.23 ? 114 GLY D O   1 
ATOM   3866 N N   . ARG D 1 115 ? -21.327 6.642   -18.239 1.00 18.69 ? 115 ARG D N   1 
ATOM   3867 C CA  . ARG D 1 115 ? -21.711 5.415   -17.508 1.00 18.62 ? 115 ARG D CA  1 
ATOM   3868 C C   . ARG D 1 115 ? -22.880 5.756   -16.577 1.00 17.97 ? 115 ARG D C   1 
ATOM   3869 O O   . ARG D 1 115 ? -23.289 6.914   -16.608 1.00 16.62 ? 115 ARG D O   1 
ATOM   3870 C CB  . ARG D 1 115 ? -20.503 4.796   -16.766 1.00 17.62 ? 115 ARG D CB  1 
ATOM   3871 C CG  . ARG D 1 115 ? -19.289 4.659   -17.763 1.00 18.99 ? 115 ARG D CG  1 
ATOM   3872 C CD  . ARG D 1 115 ? -18.247 3.632   -17.349 1.00 19.71 ? 115 ARG D CD  1 
ATOM   3873 N NE  . ARG D 1 115 ? -17.141 3.482   -18.340 1.00 21.56 ? 115 ARG D NE  1 
ATOM   3874 C CZ  . ARG D 1 115 ? -17.093 2.573   -19.332 1.00 19.76 ? 115 ARG D CZ  1 
ATOM   3875 N NH1 . ARG D 1 115 ? -18.071 1.740   -19.502 1.00 17.65 ? 115 ARG D NH1 1 
ATOM   3876 N NH2 . ARG D 1 115 ? -16.037 2.480   -20.177 1.00 23.34 ? 115 ARG D NH2 1 
ATOM   3877 N N   . THR D 1 116 ? -23.403 4.758   -15.788 1.00 16.18 ? 116 THR D N   1 
ATOM   3878 C CA  . THR D 1 116 ? -24.569 4.962   -14.914 1.00 15.37 ? 116 THR D CA  1 
ATOM   3879 C C   . THR D 1 116 ? -24.181 5.022   -13.419 1.00 16.12 ? 116 THR D C   1 
ATOM   3880 O O   . THR D 1 116 ? -23.388 4.247   -12.987 1.00 18.47 ? 116 THR D O   1 
ATOM   3881 C CB  . THR D 1 116 ? -25.712 4.024   -15.276 1.00 14.63 ? 116 THR D CB  1 
ATOM   3882 O OG1 . THR D 1 116 ? -26.099 4.307   -16.643 1.00 19.13 ? 116 THR D OG1 1 
ATOM   3883 C CG2 . THR D 1 116 ? -27.006 4.252   -14.457 1.00 14.17 ? 116 THR D CG2 1 
ATOM   3884 N N   . LEU D 1 117 ? -24.646 6.020   -12.682 1.00 14.76 ? 117 LEU D N   1 
ATOM   3885 C CA  . LEU D 1 117 ? -24.552 6.031   -11.252 1.00 16.08 ? 117 LEU D CA  1 
ATOM   3886 C C   . LEU D 1 117 ? -25.929 5.516   -10.742 1.00 17.80 ? 117 LEU D C   1 
ATOM   3887 O O   . LEU D 1 117 ? -26.965 6.020   -11.126 1.00 18.08 ? 117 LEU D O   1 
ATOM   3888 C CB  . LEU D 1 117 ? -24.228 7.452   -10.753 1.00 16.08 ? 117 LEU D CB  1 
ATOM   3889 C CG  . LEU D 1 117 ? -24.301 7.684   -9.245  1.00 13.65 ? 117 LEU D CG  1 
ATOM   3890 C CD1 . LEU D 1 117 ? -23.076 7.077   -8.630  1.00 17.34 ? 117 LEU D CD1 1 
ATOM   3891 C CD2 . LEU D 1 117 ? -24.348 9.114   -8.930  1.00 13.15 ? 117 LEU D CD2 1 
ATOM   3892 N N   . VAL D 1 118 ? -25.908 4.485   -9.889  1.00 19.27 ? 118 VAL D N   1 
ATOM   3893 C CA  . VAL D 1 118 ? -27.103 3.860   -9.374  1.00 19.48 ? 118 VAL D CA  1 
ATOM   3894 C C   . VAL D 1 118 ? -27.133 3.889   -7.834  1.00 20.47 ? 118 VAL D C   1 
ATOM   3895 O O   . VAL D 1 118 ? -26.089 3.822   -7.201  1.00 19.58 ? 118 VAL D O   1 
ATOM   3896 C CB  . VAL D 1 118 ? -27.168 2.359   -9.804  1.00 19.53 ? 118 VAL D CB  1 
ATOM   3897 C CG1 . VAL D 1 118 ? -28.388 1.703   -9.174  1.00 18.76 ? 118 VAL D CG1 1 
ATOM   3898 C CG2 . VAL D 1 118 ? -27.201 2.221   -11.365 1.00 17.85 ? 118 VAL D CG2 1 
ATOM   3899 N N   . VAL D 1 119 ? -28.345 3.981   -7.265  1.00 21.38 ? 119 VAL D N   1 
ATOM   3900 C CA  . VAL D 1 119 ? -28.555 3.945   -5.819  1.00 23.65 ? 119 VAL D CA  1 
ATOM   3901 C C   . VAL D 1 119 ? -29.434 2.746   -5.465  1.00 26.10 ? 119 VAL D C   1 
ATOM   3902 O O   . VAL D 1 119 ? -30.470 2.470   -6.093  1.00 25.46 ? 119 VAL D O   1 
ATOM   3903 C CB  . VAL D 1 119 ? -28.922 5.342   -5.108  1.00 24.48 ? 119 VAL D CB  1 
ATOM   3904 C CG1 . VAL D 1 119 ? -29.902 6.238   -5.892  1.00 21.90 ? 119 VAL D CG1 1 
ATOM   3905 C CG2 . VAL D 1 119 ? -29.328 5.157   -3.587  1.00 20.83 ? 119 VAL D CG2 1 
ATOM   3906 N N   . HIS D 1 120 ? -28.908 1.939   -4.548  1.00 27.46 ? 120 HIS D N   1 
ATOM   3907 C CA  . HIS D 1 120 ? -29.439 0.575   -4.353  1.00 28.67 ? 120 HIS D CA  1 
ATOM   3908 C C   . HIS D 1 120 ? -30.407 0.443   -3.189  1.00 29.14 ? 120 HIS D C   1 
ATOM   3909 O O   . HIS D 1 120 ? -30.400 1.265   -2.313  1.00 29.10 ? 120 HIS D O   1 
ATOM   3910 C CB  . HIS D 1 120 ? -28.302 -0.361  -4.261  1.00 26.91 ? 120 HIS D CB  1 
ATOM   3911 C CG  . HIS D 1 120 ? -27.651 -0.604  -5.578  1.00 27.98 ? 120 HIS D CG  1 
ATOM   3912 N ND1 . HIS D 1 120 ? -28.032 -1.628  -6.418  1.00 26.79 ? 120 HIS D ND1 1 
ATOM   3913 C CD2 . HIS D 1 120 ? -26.644 0.036   -6.205  1.00 27.69 ? 120 HIS D CD2 1 
ATOM   3914 C CE1 . HIS D 1 120 ? -27.286 -1.615  -7.499  1.00 23.11 ? 120 HIS D CE1 1 
ATOM   3915 N NE2 . HIS D 1 120 ? -26.431 -0.616  -7.397  1.00 28.22 ? 120 HIS D NE2 1 
ATOM   3916 N N   . GLU D 1 121 ? -31.295 -0.549  -3.231  1.00 32.71 ? 121 GLU D N   1 
ATOM   3917 C CA  . GLU D 1 121 ? -32.291 -0.775  -2.150  1.00 35.56 ? 121 GLU D CA  1 
ATOM   3918 C C   . GLU D 1 121 ? -31.572 -0.929  -0.804  1.00 35.85 ? 121 GLU D C   1 
ATOM   3919 O O   . GLU D 1 121 ? -31.846 -0.237  0.169   1.00 36.43 ? 121 GLU D O   1 
ATOM   3920 C CB  . GLU D 1 121 ? -33.031 -2.085  -2.445  1.00 35.99 ? 121 GLU D CB  1 
ATOM   3921 C CG  . GLU D 1 121 ? -34.492 -2.134  -1.996  1.00 39.87 ? 121 GLU D CG  1 
ATOM   3922 C CD  . GLU D 1 121 ? -35.083 -3.558  -1.917  1.00 40.09 ? 121 GLU D CD  1 
ATOM   3923 O OE1 . GLU D 1 121 ? -35.608 -3.865  -0.817  1.00 47.49 ? 121 GLU D OE1 1 
ATOM   3924 O OE2 . GLU D 1 121 ? -35.015 -4.352  -2.904  1.00 40.32 ? 121 GLU D OE2 1 
ATOM   3925 N N   . LYS D 1 122 ? -30.624 -1.842  -0.787  1.00 36.76 ? 122 LYS D N   1 
ATOM   3926 C CA  . LYS D 1 122 ? -29.911 -2.231  0.404   1.00 39.09 ? 122 LYS D CA  1 
ATOM   3927 C C   . LYS D 1 122 ? -28.531 -1.609  0.493   1.00 38.79 ? 122 LYS D C   1 
ATOM   3928 O O   . LYS D 1 122 ? -27.980 -1.096  -0.509  1.00 39.32 ? 122 LYS D O   1 
ATOM   3929 C CB  . LYS D 1 122 ? -29.746 -3.762  0.403   1.00 38.59 ? 122 LYS D CB  1 
ATOM   3930 C CG  . LYS D 1 122 ? -31.048 -4.579  0.631   1.00 42.00 ? 122 LYS D CG  1 
ATOM   3931 C CD  . LYS D 1 122 ? -30.783 -5.947  1.340   1.00 41.15 ? 122 LYS D CD  1 
ATOM   3932 C CE  . LYS D 1 122 ? -30.012 -5.777  2.689   1.00 43.95 ? 122 LYS D CE  1 
ATOM   3933 N NZ  . LYS D 1 122 ? -30.199 -6.856  3.732   1.00 46.42 ? 122 LYS D NZ  1 
ATOM   3934 N N   . ALA D 1 123 ? -27.954 -1.726  1.695   1.00 38.68 ? 123 ALA D N   1 
ATOM   3935 C CA  . ALA D 1 123 ? -26.555 -1.360  1.991   1.00 37.75 ? 123 ALA D CA  1 
ATOM   3936 C C   . ALA D 1 123 ? -25.561 -2.174  1.188   1.00 37.71 ? 123 ALA D C   1 
ATOM   3937 O O   . ALA D 1 123 ? -25.854 -3.293  0.794   1.00 37.72 ? 123 ALA D O   1 
ATOM   3938 C CB  . ALA D 1 123 ? -26.274 -1.480  3.522   1.00 37.40 ? 123 ALA D CB  1 
ATOM   3939 N N   . ASP D 1 124 ? -24.392 -1.600  0.912   1.00 38.53 ? 124 ASP D N   1 
ATOM   3940 C CA  . ASP D 1 124 ? -23.313 -2.319  0.224   1.00 39.02 ? 124 ASP D CA  1 
ATOM   3941 C C   . ASP D 1 124 ? -22.840 -3.545  1.037   1.00 39.36 ? 124 ASP D C   1 
ATOM   3942 O O   . ASP D 1 124 ? -22.747 -3.474  2.280   1.00 38.55 ? 124 ASP D O   1 
ATOM   3943 C CB  . ASP D 1 124 ? -22.140 -1.359  0.011   1.00 40.12 ? 124 ASP D CB  1 
ATOM   3944 C CG  . ASP D 1 124 ? -21.595 -1.393  -1.393  1.00 41.06 ? 124 ASP D CG  1 
ATOM   3945 O OD1 . ASP D 1 124 ? -22.161 -2.177  -2.194  1.00 42.28 ? 124 ASP D OD1 1 
ATOM   3946 O OD2 . ASP D 1 124 ? -20.611 -0.642  -1.677  1.00 41.71 ? 124 ASP D OD2 1 
ATOM   3947 N N   . SER D 1 142 ? -32.212 -4.262  -5.691  1.00 33.60 ? 142 SER D N   1 
ATOM   3948 C CA  . SER D 1 142 ? -33.091 -3.332  -6.423  1.00 30.59 ? 142 SER D CA  1 
ATOM   3949 C C   . SER D 1 142 ? -32.528 -1.892  -6.599  1.00 29.73 ? 142 SER D C   1 
ATOM   3950 O O   . SER D 1 142 ? -32.076 -1.218  -5.661  1.00 28.26 ? 142 SER D O   1 
ATOM   3951 C CB  . SER D 1 142 ? -34.467 -3.288  -5.783  1.00 31.77 ? 142 SER D CB  1 
ATOM   3952 O OG  . SER D 1 142 ? -35.429 -2.614  -6.590  1.00 31.36 ? 142 SER D OG  1 
ATOM   3953 N N   . ARG D 1 143 ? -32.604 -1.435  -7.838  1.00 27.86 ? 143 ARG D N   1 
ATOM   3954 C CA  . ARG D 1 143 ? -32.012 -0.191  -8.223  1.00 26.89 ? 143 ARG D CA  1 
ATOM   3955 C C   . ARG D 1 143 ? -33.064 0.838   -8.023  1.00 25.70 ? 143 ARG D C   1 
ATOM   3956 O O   . ARG D 1 143 ? -34.069 0.855   -8.690  1.00 27.07 ? 143 ARG D O   1 
ATOM   3957 C CB  . ARG D 1 143 ? -31.476 -0.278  -9.650  1.00 26.00 ? 143 ARG D CB  1 
ATOM   3958 C CG  . ARG D 1 143 ? -30.567 -1.588  -9.829  1.00 25.63 ? 143 ARG D CG  1 
ATOM   3959 C CD  . ARG D 1 143 ? -29.850 -1.615  -11.197 1.00 25.92 ? 143 ARG D CD  1 
ATOM   3960 N NE  . ARG D 1 143 ? -28.850 -2.667  -11.259 1.00 25.96 ? 143 ARG D NE  1 
ATOM   3961 C CZ  . ARG D 1 143 ? -28.018 -2.883  -12.274 1.00 29.23 ? 143 ARG D CZ  1 
ATOM   3962 N NH1 . ARG D 1 143 ? -28.007 -2.071  -13.316 1.00 25.54 ? 143 ARG D NH1 1 
ATOM   3963 N NH2 . ARG D 1 143 ? -27.154 -3.913  -12.229 1.00 27.98 ? 143 ARG D NH2 1 
ATOM   3964 N N   . LEU D 1 144 ? -32.865 1.652   -7.018  1.00 24.43 ? 144 LEU D N   1 
ATOM   3965 C CA  . LEU D 1 144 ? -33.831 2.711   -6.675  1.00 22.02 ? 144 LEU D CA  1 
ATOM   3966 C C   . LEU D 1 144 ? -33.948 3.812   -7.736  1.00 21.35 ? 144 LEU D C   1 
ATOM   3967 O O   . LEU D 1 144 ? -35.056 4.208   -8.175  1.00 20.91 ? 144 LEU D O   1 
ATOM   3968 C CB  . LEU D 1 144 ? -33.474 3.251   -5.307  1.00 21.15 ? 144 LEU D CB  1 
ATOM   3969 C CG  . LEU D 1 144 ? -33.754 2.177   -4.238  1.00 21.27 ? 144 LEU D CG  1 
ATOM   3970 C CD1 . LEU D 1 144 ? -33.707 2.775   -2.823  1.00 19.50 ? 144 LEU D CD1 1 
ATOM   3971 C CD2 . LEU D 1 144 ? -35.132 1.602   -4.476  1.00 17.30 ? 144 LEU D CD2 1 
ATOM   3972 N N   . ALA D 1 145 ? -32.784 4.294   -8.151  1.00 19.24 ? 145 ALA D N   1 
ATOM   3973 C CA  . ALA D 1 145 ? -32.718 5.284   -9.119  1.00 18.29 ? 145 ALA D CA  1 
ATOM   3974 C C   . ALA D 1 145 ? -31.341 5.224   -9.769  1.00 18.50 ? 145 ALA D C   1 
ATOM   3975 O O   . ALA D 1 145 ? -30.384 4.656   -9.235  1.00 17.61 ? 145 ALA D O   1 
ATOM   3976 C CB  . ALA D 1 145 ? -32.999 6.687   -8.456  1.00 18.64 ? 145 ALA D CB  1 
ATOM   3977 N N   . CYS D 1 146 ? -31.248 5.799   -10.947 1.00 18.71 ? 146 CYS D N   1 
ATOM   3978 C CA  . CYS D 1 146 ? -29.981 5.916   -11.645 1.00 20.37 ? 146 CYS D CA  1 
ATOM   3979 C C   . CYS D 1 146 ? -30.042 7.150   -12.549 1.00 19.07 ? 146 CYS D C   1 
ATOM   3980 O O   . CYS D 1 146 ? -31.099 7.772   -12.701 1.00 18.16 ? 146 CYS D O   1 
ATOM   3981 C CB  . CYS D 1 146 ? -29.766 4.652   -12.503 1.00 22.51 ? 146 CYS D CB  1 
ATOM   3982 S SG  . CYS D 1 146 ? -31.214 4.164   -13.512 1.00 29.07 ? 146 CYS D SG  1 
ATOM   3983 N N   . GLY D 1 147 ? -28.900 7.480   -13.141 1.00 18.70 ? 147 GLY D N   1 
ATOM   3984 C CA  . GLY D 1 147 ? -28.774 8.531   -14.124 1.00 18.70 ? 147 GLY D CA  1 
ATOM   3985 C C   . GLY D 1 147 ? -27.447 8.362   -14.861 1.00 18.07 ? 147 GLY D C   1 
ATOM   3986 O O   . GLY D 1 147 ? -26.483 7.873   -14.283 1.00 19.45 ? 147 GLY D O   1 
ATOM   3987 N N   . VAL D 1 148 ? -27.413 8.731   -16.132 1.00 17.40 ? 148 VAL D N   1 
ATOM   3988 C CA  . VAL D 1 148 ? -26.159 8.779   -16.898 1.00 17.52 ? 148 VAL D CA  1 
ATOM   3989 C C   . VAL D 1 148 ? -25.285 9.944   -16.404 1.00 18.75 ? 148 VAL D C   1 
ATOM   3990 O O   . VAL D 1 148 ? -25.796 11.042  -16.174 1.00 16.34 ? 148 VAL D O   1 
ATOM   3991 C CB  . VAL D 1 148 ? -26.401 8.938   -18.433 1.00 17.56 ? 148 VAL D CB  1 
ATOM   3992 C CG1 . VAL D 1 148 ? -25.116 8.724   -19.254 1.00 10.55 ? 148 VAL D CG1 1 
ATOM   3993 C CG2 . VAL D 1 148 ? -27.502 8.025   -18.877 1.00 16.30 ? 148 VAL D CG2 1 
ATOM   3994 N N   . ILE D 1 149 ? -23.981 9.670   -16.247 1.00 18.84 ? 149 ILE D N   1 
ATOM   3995 C CA  . ILE D 1 149 ? -23.008 10.667  -15.808 1.00 19.87 ? 149 ILE D CA  1 
ATOM   3996 C C   . ILE D 1 149 ? -22.496 11.449  -16.994 1.00 21.27 ? 149 ILE D C   1 
ATOM   3997 O O   . ILE D 1 149 ? -21.766 10.912  -17.819 1.00 21.08 ? 149 ILE D O   1 
ATOM   3998 C CB  . ILE D 1 149 ? -21.798 9.982   -15.010 1.00 19.89 ? 149 ILE D CB  1 
ATOM   3999 C CG1 . ILE D 1 149 ? -22.364 9.118   -13.871 1.00 19.09 ? 149 ILE D CG1 1 
ATOM   4000 C CG2 . ILE D 1 149 ? -20.735 11.009  -14.560 1.00 17.05 ? 149 ILE D CG2 1 
ATOM   4001 C CD1 . ILE D 1 149 ? -21.354 8.231   -13.261 1.00 17.86 ? 149 ILE D CD1 1 
ATOM   4002 N N   . GLY D 1 150 ? -22.850 12.739  -17.043 1.00 21.10 ? 150 GLY D N   1 
ATOM   4003 C CA  . GLY D 1 150 ? -22.568 13.579  -18.168 1.00 19.69 ? 150 GLY D CA  1 
ATOM   4004 C C   . GLY D 1 150 ? -21.688 14.732  -17.778 1.00 21.19 ? 150 GLY D C   1 
ATOM   4005 O O   . GLY D 1 150 ? -21.429 14.922  -16.597 1.00 18.33 ? 150 GLY D O   1 
ATOM   4006 N N   . ILE D 1 151 ? -21.212 15.469  -18.787 1.00 21.18 ? 151 ILE D N   1 
ATOM   4007 C CA  . ILE D 1 151 ? -20.162 16.479  -18.646 1.00 22.57 ? 151 ILE D CA  1 
ATOM   4008 C C   . ILE D 1 151 ? -20.887 17.742  -18.179 1.00 22.14 ? 151 ILE D C   1 
ATOM   4009 O O   . ILE D 1 151 ? -21.873 18.084  -18.769 1.00 21.84 ? 151 ILE D O   1 
ATOM   4010 C CB  . ILE D 1 151 ? -19.449 16.686  -20.001 1.00 21.96 ? 151 ILE D CB  1 
ATOM   4011 C CG1 . ILE D 1 151 ? -18.789 15.392  -20.469 1.00 23.23 ? 151 ILE D CG1 1 
ATOM   4012 C CG2 . ILE D 1 151 ? -18.482 17.855  -19.958 1.00 24.15 ? 151 ILE D CG2 1 
ATOM   4013 C CD1 . ILE D 1 151 ? -18.220 15.392  -21.885 1.00 25.11 ? 151 ILE D CD1 1 
ATOM   4014 N N   . ALA D 1 152 ? -20.448 18.396  -17.094 1.00 23.55 ? 152 ALA D N   1 
ATOM   4015 C CA  . ALA D 1 152 ? -21.150 19.603  -16.587 1.00 24.92 ? 152 ALA D CA  1 
ATOM   4016 C C   . ALA D 1 152 ? -20.435 20.868  -16.986 1.00 27.36 ? 152 ALA D C   1 
ATOM   4017 O O   . ALA D 1 152 ? -19.251 20.813  -17.347 1.00 27.10 ? 152 ALA D O   1 
ATOM   4018 C CB  . ALA D 1 152 ? -21.279 19.555  -15.086 1.00 24.61 ? 152 ALA D CB  1 
ATOM   4019 N N   . GLN D 1 153 ? -21.144 22.007  -16.898 1.00 29.91 ? 153 GLN D N   1 
ATOM   4020 C CA  . GLN D 1 153 ? -20.557 23.331  -17.206 1.00 34.46 ? 153 GLN D CA  1 
ATOM   4021 C C   . GLN D 1 153 ? -19.528 23.832  -16.142 1.00 35.96 ? 153 GLN D C   1 
ATOM   4022 O O   . GLN D 1 153 ? -19.917 24.100  -14.968 1.00 36.59 ? 153 GLN D O   1 
ATOM   4023 C CB  . GLN D 1 153 ? -21.669 24.405  -17.417 1.00 34.55 ? 153 GLN D CB  1 
ATOM   4024 C CG  . GLN D 1 153 ? -21.106 25.654  -18.056 1.00 35.71 ? 153 GLN D CG  1 
ATOM   4025 C CD  . GLN D 1 153 ? -22.161 26.662  -18.594 1.00 37.03 ? 153 GLN D CD  1 
ATOM   4026 O OE1 . GLN D 1 153 ? -23.390 26.519  -18.426 1.00 36.03 ? 153 GLN D OE1 1 
ATOM   4027 N NE2 . GLN D 1 153 ? -21.650 27.690  -19.245 1.00 36.43 ? 153 GLN D NE2 1 
ATOM   4028 O OXT . GLN D 1 153 ? -18.302 24.003  -16.422 1.00 36.98 ? 153 GLN D OXT 1 
HETATM 4029 O O   . HOH E 2 .   ? 11.461  8.072   -34.763 1.00 16.50 ? 154 HOH A O   1 
HETATM 4030 O O   . HOH E 2 .   ? 29.013  -0.543  -24.831 1.00 19.06 ? 155 HOH A O   1 
HETATM 4031 O O   . HOH E 2 .   ? 12.451  -0.693  -33.084 1.00 17.01 ? 156 HOH A O   1 
HETATM 4032 O O   . HOH E 2 .   ? 3.677   4.452   -12.458 1.00 24.71 ? 157 HOH A O   1 
HETATM 4033 O O   . HOH E 2 .   ? 16.165  0.683   -33.768 1.00 29.02 ? 158 HOH A O   1 
HETATM 4034 O O   . HOH E 2 .   ? 17.819  7.580   -2.440  1.00 32.97 ? 159 HOH A O   1 
HETATM 4035 O O   . HOH E 2 .   ? 14.008  0.834   -12.735 1.00 12.03 ? 160 HOH A O   1 
HETATM 4036 O O   . HOH E 2 .   ? 15.014  13.673  -21.326 1.00 30.36 ? 161 HOH A O   1 
HETATM 4037 O O   . HOH E 2 .   ? 19.593  -8.034  -14.027 1.00 19.97 ? 163 HOH A O   1 
HETATM 4038 O O   . HOH E 2 .   ? 28.456  -0.781  -22.014 1.00 21.64 ? 164 HOH A O   1 
HETATM 4039 O O   . HOH E 2 .   ? 13.924  6.235   -30.340 1.00 30.90 ? 165 HOH A O   1 
HETATM 4040 O O   . HOH E 2 .   ? 24.659  0.344   -32.111 1.00 13.24 ? 166 HOH A O   1 
HETATM 4041 O O   . HOH E 2 .   ? 22.218  14.403  -7.966  1.00 29.92 ? 167 HOH A O   1 
HETATM 4042 O O   . HOH E 2 .   ? 27.642  -15.883 -19.481 1.00 40.38 ? 168 HOH A O   1 
HETATM 4043 O O   . HOH E 2 .   ? 23.915  6.267   -7.907  1.00 32.65 ? 169 HOH A O   1 
HETATM 4044 O O   . HOH E 2 .   ? 13.585  1.677   -34.102 1.00 10.86 ? 170 HOH A O   1 
HETATM 4045 O O   . HOH E 2 .   ? -0.111  -4.236  -17.374 1.00 32.31 ? 171 HOH A O   1 
HETATM 4046 O O   . HOH E 2 .   ? 15.268  8.038   -29.644 1.00 22.08 ? 172 HOH A O   1 
HETATM 4047 O O   . HOH E 2 .   ? 0.480   -13.407 -29.212 1.00 39.21 ? 173 HOH A O   1 
HETATM 4048 O O   . HOH E 2 .   ? 14.844  -12.528 -29.950 1.00 30.06 ? 174 HOH A O   1 
HETATM 4049 O O   . HOH E 2 .   ? 19.293  -9.373  -17.845 1.00 18.51 ? 175 HOH A O   1 
HETATM 4050 O O   . HOH E 2 .   ? 25.908  2.038   -28.686 1.00 18.60 ? 176 HOH A O   1 
HETATM 4051 O O   . HOH E 2 .   ? 15.203  4.559   -32.670 1.00 23.51 ? 177 HOH A O   1 
HETATM 4052 O O   . HOH E 2 .   ? 14.136  0.795   -5.330  1.00 26.01 ? 178 HOH A O   1 
HETATM 4053 O O   . HOH E 2 .   ? 17.049  9.298   -18.865 1.00 32.45 ? 179 HOH A O   1 
HETATM 4054 O O   . HOH E 2 .   ? 20.569  -3.645  -33.580 1.00 32.58 ? 180 HOH A O   1 
HETATM 4055 O O   . HOH E 2 .   ? 4.219   6.627   -13.920 1.00 20.31 ? 181 HOH A O   1 
HETATM 4056 O O   . HOH E 2 .   ? 12.986  -3.787  -8.053  1.00 21.94 ? 182 HOH A O   1 
HETATM 4057 O O   . HOH E 2 .   ? 22.896  9.675   -24.188 1.00 20.53 ? 184 HOH A O   1 
HETATM 4058 O O   . HOH E 2 .   ? -0.613  7.480   -9.044  1.00 47.55 ? 185 HOH A O   1 
HETATM 4059 O O   . HOH E 2 .   ? 20.593  10.653  -20.749 1.00 33.29 ? 186 HOH A O   1 
HETATM 4060 O O   . HOH E 2 .   ? 4.077   1.146   -9.881  1.00 29.62 ? 187 HOH A O   1 
HETATM 4061 O O   . HOH E 2 .   ? 16.978  -9.428  -17.266 1.00 15.93 ? 188 HOH A O   1 
HETATM 4062 O O   . HOH E 2 .   ? 8.519   -10.081 -30.867 1.00 30.70 ? 189 HOH A O   1 
HETATM 4063 O O   . HOH E 2 .   ? 30.309  -7.393  -27.354 1.00 37.79 ? 190 HOH A O   1 
HETATM 4064 O O   . HOH E 2 .   ? 13.694  5.653   -3.184  1.00 23.40 ? 191 HOH A O   1 
HETATM 4065 O O   . HOH E 2 .   ? 29.577  -1.566  -16.685 1.00 26.76 ? 192 HOH A O   1 
HETATM 4066 O O   . HOH E 2 .   ? 0.059   -8.744  -32.221 1.00 31.00 ? 193 HOH A O   1 
HETATM 4067 O O   . HOH E 2 .   ? 17.661  3.737   -32.748 1.00 17.18 ? 194 HOH A O   1 
HETATM 4068 O O   . HOH E 2 .   ? 16.209  -4.594  -11.761 1.00 26.45 ? 195 HOH A O   1 
HETATM 4069 O O   . HOH E 2 .   ? 24.211  11.803  -9.800  1.00 24.60 ? 196 HOH A O   1 
HETATM 4070 O O   . HOH E 2 .   ? 27.869  -9.558  -14.900 1.00 37.53 ? 197 HOH A O   1 
HETATM 4071 O O   . HOH E 2 .   ? 17.513  11.207  -38.105 1.00 23.94 ? 198 HOH A O   1 
HETATM 4072 O O   . HOH E 2 .   ? 24.723  10.275  -2.378  1.00 16.39 ? 199 HOH A O   1 
HETATM 4073 O O   . HOH E 2 .   ? 30.247  -12.762 -16.181 1.00 35.47 ? 200 HOH A O   1 
HETATM 4074 O O   . HOH E 2 .   ? 15.509  -4.626  -9.631  1.00 26.11 ? 201 HOH A O   1 
HETATM 4075 O O   . HOH E 2 .   ? 11.275  -9.538  -13.837 1.00 26.08 ? 202 HOH A O   1 
HETATM 4076 O O   . HOH E 2 .   ? 17.586  7.610   -17.104 1.00 31.60 ? 203 HOH A O   1 
HETATM 4077 O O   . HOH E 2 .   ? 18.002  -4.207  -38.302 1.00 29.03 ? 204 HOH A O   1 
HETATM 4078 O O   . HOH E 2 .   ? 14.110  -6.024  -14.539 1.00 19.39 ? 205 HOH A O   1 
HETATM 4079 O O   . HOH E 2 .   ? 16.242  -7.545  -15.663 1.00 28.09 ? 206 HOH A O   1 
HETATM 4080 O O   . HOH E 2 .   ? 6.679   -9.616  -36.333 1.00 19.27 ? 207 HOH A O   1 
HETATM 4081 O O   . HOH E 2 .   ? 2.338   2.901   -11.585 1.00 24.09 ? 208 HOH A O   1 
HETATM 4082 O O   . HOH E 2 .   ? 4.811   10.886  -19.324 1.00 29.01 ? 209 HOH A O   1 
HETATM 4083 O O   . HOH E 2 .   ? 12.756  17.048  -37.839 1.00 27.02 ? 210 HOH A O   1 
HETATM 4084 O O   . HOH E 2 .   ? 5.349   10.474  -6.111  1.00 31.46 ? 211 HOH A O   1 
HETATM 4085 O O   . HOH E 2 .   ? 28.139  2.720   -26.669 1.00 32.87 ? 212 HOH A O   1 
HETATM 4086 O O   . HOH E 2 .   ? 20.960  11.376  -29.268 1.00 29.06 ? 221 HOH A O   1 
HETATM 4087 O O   . HOH E 2 .   ? 11.149  10.922  -11.574 1.00 31.87 ? 224 HOH A O   1 
HETATM 4088 O O   . HOH E 2 .   ? 9.059   -6.290  -13.528 1.00 26.61 ? 225 HOH A O   1 
HETATM 4089 O O   . HOH E 2 .   ? 5.995   -8.179  -12.295 1.00 35.06 ? 226 HOH A O   1 
HETATM 4090 O O   . HOH E 2 .   ? 16.380  5.169   -37.016 1.00 23.51 ? 231 HOH A O   1 
HETATM 4091 O O   . HOH E 2 .   ? 19.000  -4.371  -10.363 1.00 28.28 ? 233 HOH A O   1 
HETATM 4092 O O   . HOH E 2 .   ? 20.091  8.428   -17.431 1.00 28.61 ? 234 HOH A O   1 
HETATM 4093 O O   . HOH E 2 .   ? 11.065  4.512   -5.579  1.00 29.63 ? 235 HOH A O   1 
HETATM 4094 O O   . HOH E 2 .   ? -2.485  0.438   -19.707 1.00 30.32 ? 236 HOH A O   1 
HETATM 4095 O O   . HOH E 2 .   ? 12.616  15.479  -31.136 1.00 26.87 ? 239 HOH A O   1 
HETATM 4096 O O   . HOH E 2 .   ? 18.787  6.292   -37.812 1.00 39.30 ? 241 HOH A O   1 
HETATM 4097 O O   . HOH E 2 .   ? -3.095  -5.525  -24.003 1.00 29.67 ? 242 HOH A O   1 
HETATM 4098 O O   . HOH E 2 .   ? 8.733   -6.796  -9.528  1.00 42.06 ? 244 HOH A O   1 
HETATM 4099 O O   . HOH E 2 .   ? 7.072   -0.661  -2.512  1.00 28.65 ? 248 HOH A O   1 
HETATM 4100 O O   . HOH E 2 .   ? 23.308  -10.917 -28.177 1.00 40.22 ? 251 HOH A O   1 
HETATM 4101 O O   . HOH E 2 .   ? 21.236  9.959   -15.150 1.00 41.66 ? 253 HOH A O   1 
HETATM 4102 O O   . HOH E 2 .   ? 3.068   10.581  -24.619 1.00 32.50 ? 254 HOH A O   1 
HETATM 4103 O O   . HOH E 2 .   ? 27.367  -3.781  -12.723 1.00 36.84 ? 255 HOH A O   1 
HETATM 4104 O O   . HOH E 2 .   ? 28.214  -5.041  -31.430 1.00 29.96 ? 256 HOH A O   1 
HETATM 4105 O O   . HOH E 2 .   ? 27.625  -1.082  -15.446 1.00 38.61 ? 258 HOH A O   1 
HETATM 4106 O O   . HOH E 2 .   ? 5.932   -5.477  -12.168 1.00 31.56 ? 259 HOH A O   1 
HETATM 4107 O O   . HOH E 2 .   ? 6.696   -11.456 -11.648 1.00 25.28 ? 262 HOH A O   1 
HETATM 4108 O O   . HOH E 2 .   ? 27.070  8.689   -12.214 1.00 43.21 ? 263 HOH A O   1 
HETATM 4109 O O   . HOH E 2 .   ? 23.343  11.993  -28.241 1.00 37.88 ? 264 HOH A O   1 
HETATM 4110 O O   . HOH E 2 .   ? 27.389  0.471   -13.533 1.00 34.53 ? 267 HOH A O   1 
HETATM 4111 O O   . HOH E 2 .   ? 23.274  -9.306  -11.891 1.00 43.60 ? 269 HOH A O   1 
HETATM 4112 O O   . HOH E 2 .   ? 12.318  -6.903  -10.645 1.00 26.31 ? 274 HOH A O   1 
HETATM 4113 O O   . HOH E 2 .   ? 4.490   -9.804  -13.391 1.00 37.81 ? 275 HOH A O   1 
HETATM 4114 O O   . HOH E 2 .   ? 12.122  -0.193  -2.178  1.00 36.62 ? 287 HOH A O   1 
HETATM 4115 O O   . HOH E 2 .   ? 21.956  5.982   -38.506 1.00 40.38 ? 299 HOH A O   1 
HETATM 4116 O O   . HOH E 2 .   ? 16.205  15.510  -26.903 1.00 38.70 ? 310 HOH A O   1 
HETATM 4117 O O   . HOH E 2 .   ? 7.196   -12.057 -35.010 1.00 32.98 ? 314 HOH A O   1 
HETATM 4118 O O   . HOH E 2 .   ? -4.119  -9.902  -14.665 1.00 50.14 ? 317 HOH A O   1 
HETATM 4119 O O   . HOH E 2 .   ? 5.808   9.128   -2.550  1.00 35.95 ? 320 HOH A O   1 
HETATM 4120 O O   . HOH E 2 .   ? 22.959  6.527   -28.408 1.00 27.12 ? 322 HOH A O   1 
HETATM 4121 O O   . HOH E 2 .   ? 29.969  5.373   -20.837 1.00 44.08 ? 325 HOH A O   1 
HETATM 4122 O O   . HOH E 2 .   ? 16.522  16.252  -29.479 1.00 33.48 ? 337 HOH A O   1 
HETATM 4123 O O   . HOH E 2 .   ? 14.811  15.429  -31.538 1.00 38.41 ? 348 HOH A O   1 
HETATM 4124 O O   . HOH E 2 .   ? 15.602  17.426  -33.218 1.00 27.79 ? 361 HOH A O   1 
HETATM 4125 O O   . HOH E 2 .   ? 0.379   -11.244 -33.065 1.00 42.92 ? 369 HOH A O   1 
HETATM 4126 O O   . HOH E 2 .   ? 15.631  -12.662 -14.728 1.00 36.58 ? 375 HOH A O   1 
HETATM 4127 O O   . HOH E 2 .   ? 9.793   3.124   -2.630  1.00 32.09 ? 386 HOH A O   1 
HETATM 4128 O O   . HOH E 2 .   ? 14.944  17.208  -38.889 1.00 39.25 ? 388 HOH A O   1 
HETATM 4129 O O   . HOH E 2 .   ? 26.266  -11.675 -15.613 1.00 41.51 ? 394 HOH A O   1 
HETATM 4130 O O   . HOH E 2 .   ? 22.472  8.741   -37.553 1.00 36.04 ? 395 HOH A O   1 
HETATM 4131 O O   . HOH E 2 .   ? 8.730   -13.525 -31.227 1.00 46.31 ? 400 HOH A O   1 
HETATM 4132 O O   . HOH E 2 .   ? -2.414  -8.160  -11.834 1.00 35.55 ? 406 HOH A O   1 
HETATM 4133 O O   . HOH E 2 .   ? -5.175  -4.696  -29.002 1.00 29.40 ? 420 HOH A O   1 
HETATM 4134 O O   . HOH F 2 .   ? 14.573  17.817  -60.145 1.00 36.13 ? 154 HOH B O   1 
HETATM 4135 O O   . HOH F 2 .   ? 18.331  5.090   -53.558 1.00 11.08 ? 155 HOH B O   1 
HETATM 4136 O O   . HOH F 2 .   ? -7.173  15.712  -38.417 1.00 19.04 ? 156 HOH B O   1 
HETATM 4137 O O   . HOH F 2 .   ? 11.625  16.010  -42.280 1.00 25.48 ? 157 HOH B O   1 
HETATM 4138 O O   . HOH F 2 .   ? -8.161  9.104   -40.549 1.00 16.18 ? 158 HOH B O   1 
HETATM 4139 O O   . HOH F 2 .   ? 24.298  9.542   -46.241 1.00 20.90 ? 159 HOH B O   1 
HETATM 4140 O O   . HOH F 2 .   ? 8.897   14.076  -30.166 1.00 28.95 ? 160 HOH B O   1 
HETATM 4141 O O   . HOH F 2 .   ? 4.023   -1.749  -62.273 1.00 20.87 ? 161 HOH B O   1 
HETATM 4142 O O   . HOH F 2 .   ? 16.425  -0.876  -35.700 1.00 41.96 ? 162 HOH B O   1 
HETATM 4143 O O   . HOH F 2 .   ? 19.858  4.786   -44.952 1.00 28.09 ? 163 HOH B O   1 
HETATM 4144 O O   . HOH F 2 .   ? -2.307  13.717  -50.507 1.00 25.49 ? 164 HOH B O   1 
HETATM 4145 O O   . HOH F 2 .   ? 12.991  -5.096  -49.921 1.00 25.84 ? 165 HOH B O   1 
HETATM 4146 O O   . HOH F 2 .   ? 14.613  4.341   -38.075 1.00 31.35 ? 166 HOH B O   1 
HETATM 4147 O O   . HOH F 2 .   ? 9.654   15.935  -28.076 1.00 35.74 ? 167 HOH B O   1 
HETATM 4148 O O   . HOH F 2 .   ? -2.607  -6.112  -42.193 1.00 33.86 ? 168 HOH B O   1 
HETATM 4149 O O   . HOH F 2 .   ? -11.831 1.758   -56.135 1.00 28.08 ? 169 HOH B O   1 
HETATM 4150 O O   . HOH F 2 .   ? 11.233  5.782   -36.301 1.00 6.81  ? 170 HOH B O   1 
HETATM 4151 O O   . HOH F 2 .   ? -3.543  -4.049  -62.830 1.00 22.87 ? 171 HOH B O   1 
HETATM 4152 O O   . HOH F 2 .   ? 8.845   -5.533  -51.056 1.00 29.51 ? 172 HOH B O   1 
HETATM 4153 O O   . HOH F 2 .   ? -5.953  10.583  -33.460 1.00 25.50 ? 173 HOH B O   1 
HETATM 4154 O O   . HOH F 2 .   ? -12.664 9.318   -33.055 1.00 16.18 ? 174 HOH B O   1 
HETATM 4155 O O   . HOH F 2 .   ? 0.761   -6.427  -49.318 1.00 28.47 ? 175 HOH B O   1 
HETATM 4156 O O   . HOH F 2 .   ? 5.698   -8.884  -47.057 1.00 31.33 ? 176 HOH B O   1 
HETATM 4157 O O   . HOH F 2 .   ? 12.735  2.967   -36.318 1.00 26.79 ? 177 HOH B O   1 
HETATM 4158 O O   . HOH F 2 .   ? -9.748  6.442   -50.129 1.00 31.23 ? 178 HOH B O   1 
HETATM 4159 O O   . HOH F 2 .   ? -2.553  9.169   -56.346 1.00 44.31 ? 179 HOH B O   1 
HETATM 4160 O O   . HOH F 2 .   ? -4.672  7.616   -55.905 1.00 25.56 ? 180 HOH B O   1 
HETATM 4161 O O   . HOH F 2 .   ? -11.414 -6.807  -52.101 1.00 36.58 ? 181 HOH B O   1 
HETATM 4162 O O   . HOH F 2 .   ? -3.860  12.574  -28.280 1.00 38.74 ? 182 HOH B O   1 
HETATM 4163 O O   . HOH F 2 .   ? -1.316  -6.066  -36.927 1.00 27.33 ? 183 HOH B O   1 
HETATM 4164 O O   . HOH F 2 .   ? 12.097  -10.902 -39.277 1.00 27.41 ? 184 HOH B O   1 
HETATM 4165 O O   . HOH F 2 .   ? 0.275   -11.520 -63.911 1.00 32.40 ? 185 HOH B O   1 
HETATM 4166 O O   . HOH F 2 .   ? -11.029 1.750   -37.547 1.00 32.60 ? 186 HOH B O   1 
HETATM 4167 O O   . HOH F 2 .   ? 19.054  2.711   -48.406 1.00 19.29 ? 187 HOH B O   1 
HETATM 4168 O O   . HOH F 2 .   ? 11.481  -3.221  -34.585 1.00 11.05 ? 188 HOH B O   1 
HETATM 4169 O O   . HOH F 2 .   ? 4.105   13.585  -51.428 1.00 29.62 ? 189 HOH B O   1 
HETATM 4170 O O   . HOH F 2 .   ? 11.651  15.697  -25.485 1.00 33.55 ? 190 HOH B O   1 
HETATM 4171 O O   . HOH F 2 .   ? -4.155  10.535  -49.338 1.00 24.14 ? 191 HOH B O   1 
HETATM 4172 O O   . HOH F 2 .   ? -9.260  3.937   -37.106 1.00 22.46 ? 192 HOH B O   1 
HETATM 4173 O O   . HOH F 2 .   ? 6.558   13.325  -52.878 1.00 19.44 ? 193 HOH B O   1 
HETATM 4174 O O   . HOH F 2 .   ? -0.852  2.784   -52.884 1.00 18.54 ? 194 HOH B O   1 
HETATM 4175 O O   . HOH F 2 .   ? -3.550  10.468  -29.000 1.00 31.05 ? 195 HOH B O   1 
HETATM 4176 O O   . HOH F 2 .   ? 15.454  -5.279  -59.260 1.00 50.32 ? 196 HOH B O   1 
HETATM 4177 O O   . HOH F 2 .   ? 19.857  12.399  -52.337 1.00 26.19 ? 197 HOH B O   1 
HETATM 4178 O O   . HOH F 2 .   ? 9.918   -4.619  -59.493 1.00 43.37 ? 198 HOH B O   1 
HETATM 4179 O O   . HOH F 2 .   ? 18.869  -1.438  -50.599 1.00 22.97 ? 199 HOH B O   1 
HETATM 4180 O O   . HOH F 2 .   ? -7.951  -1.409  -55.855 1.00 28.35 ? 201 HOH B O   1 
HETATM 4181 O O   . HOH F 2 .   ? 18.201  -0.879  -47.855 1.00 32.89 ? 202 HOH B O   1 
HETATM 4182 O O   . HOH F 2 .   ? 7.355   -5.380  -56.205 1.00 36.11 ? 203 HOH B O   1 
HETATM 4183 O O   . HOH F 2 .   ? -5.510  2.799   -58.603 1.00 38.15 ? 204 HOH B O   1 
HETATM 4184 O O   . HOH F 2 .   ? 11.578  5.318   -59.738 1.00 27.83 ? 205 HOH B O   1 
HETATM 4185 O O   . HOH F 2 .   ? 16.787  -3.304  -44.387 1.00 17.39 ? 206 HOH B O   1 
HETATM 4186 O O   . HOH F 2 .   ? 4.024   -6.609  -49.281 1.00 37.07 ? 207 HOH B O   1 
HETATM 4187 O O   . HOH F 2 .   ? -1.977  11.142  -51.072 1.00 17.75 ? 208 HOH B O   1 
HETATM 4188 O O   . HOH F 2 .   ? 6.328   14.894  -35.909 1.00 24.04 ? 209 HOH B O   1 
HETATM 4189 O O   . HOH F 2 .   ? 11.778  17.860  -53.736 1.00 29.44 ? 210 HOH B O   1 
HETATM 4190 O O   . HOH F 2 .   ? 5.703   -5.031  -50.471 1.00 32.62 ? 211 HOH B O   1 
HETATM 4191 O O   . HOH F 2 .   ? -10.835 2.846   -48.421 1.00 30.03 ? 212 HOH B O   1 
HETATM 4192 O O   . HOH F 2 .   ? -9.125  7.660   -34.941 1.00 19.17 ? 213 HOH B O   1 
HETATM 4193 O O   . HOH F 2 .   ? 16.371  5.077   -55.109 1.00 19.92 ? 215 HOH B O   1 
HETATM 4194 O O   . HOH F 2 .   ? 9.143   7.370   -61.977 1.00 23.24 ? 216 HOH B O   1 
HETATM 4195 O O   . HOH F 2 .   ? 15.217  -6.911  -44.493 1.00 32.46 ? 217 HOH B O   1 
HETATM 4196 O O   . HOH F 2 .   ? 16.949  -1.644  -42.095 1.00 28.03 ? 218 HOH B O   1 
HETATM 4197 O O   . HOH F 2 .   ? 17.928  -10.870 -37.167 1.00 29.05 ? 219 HOH B O   1 
HETATM 4198 O O   . HOH F 2 .   ? 16.287  13.953  -45.610 1.00 28.42 ? 220 HOH B O   1 
HETATM 4199 O O   . HOH F 2 .   ? 12.940  0.277   -38.609 1.00 33.09 ? 221 HOH B O   1 
HETATM 4200 O O   . HOH F 2 .   ? -0.042  8.986   -55.199 1.00 20.84 ? 222 HOH B O   1 
HETATM 4201 O O   . HOH F 2 .   ? 10.959  13.109  -60.396 1.00 41.66 ? 223 HOH B O   1 
HETATM 4202 O O   . HOH F 2 .   ? 4.974   -3.063  -51.624 1.00 27.40 ? 229 HOH B O   1 
HETATM 4203 O O   . HOH F 2 .   ? 19.472  1.975   -51.629 1.00 23.67 ? 230 HOH B O   1 
HETATM 4204 O O   . HOH F 2 .   ? 5.685   12.908  -59.876 1.00 39.76 ? 237 HOH B O   1 
HETATM 4205 O O   . HOH F 2 .   ? 17.180  12.927  -43.299 1.00 34.26 ? 247 HOH B O   1 
HETATM 4206 O O   . HOH F 2 .   ? 13.512  -12.934 -38.349 1.00 34.55 ? 252 HOH B O   1 
HETATM 4207 O O   . HOH F 2 .   ? 1.858   5.402   -61.092 1.00 38.10 ? 257 HOH B O   1 
HETATM 4208 O O   . HOH F 2 .   ? 16.928  10.314  -40.953 1.00 33.42 ? 261 HOH B O   1 
HETATM 4209 O O   . HOH F 2 .   ? 1.525   -10.024 -52.882 1.00 42.66 ? 268 HOH B O   1 
HETATM 4210 O O   . HOH F 2 .   ? 1.616   8.168   -57.850 1.00 25.92 ? 277 HOH B O   1 
HETATM 4211 O O   . HOH F 2 .   ? -7.468  13.335  -46.409 1.00 32.84 ? 278 HOH B O   1 
HETATM 4212 O O   . HOH F 2 .   ? 16.855  -10.605 -43.344 1.00 36.26 ? 286 HOH B O   1 
HETATM 4213 O O   . HOH F 2 .   ? -7.660  9.701   -48.413 1.00 31.21 ? 288 HOH B O   1 
HETATM 4214 O O   . HOH F 2 .   ? -4.377  -5.601  -39.657 1.00 40.11 ? 290 HOH B O   1 
HETATM 4215 O O   . HOH F 2 .   ? 14.413  -12.200 -32.973 1.00 34.39 ? 291 HOH B O   1 
HETATM 4216 O O   . HOH F 2 .   ? -2.721  -7.281  -48.131 1.00 35.92 ? 292 HOH B O   1 
HETATM 4217 O O   . HOH F 2 .   ? 11.739  11.526  -63.104 1.00 31.60 ? 294 HOH B O   1 
HETATM 4218 O O   . HOH F 2 .   ? 9.436   3.056   -61.331 1.00 33.96 ? 295 HOH B O   1 
HETATM 4219 O O   . HOH F 2 .   ? -6.296  6.304   -57.934 1.00 43.97 ? 296 HOH B O   1 
HETATM 4220 O O   . HOH F 2 .   ? -0.303  -7.786  -35.151 1.00 31.86 ? 301 HOH B O   1 
HETATM 4221 O O   . HOH F 2 .   ? 11.404  -6.934  -49.823 1.00 46.98 ? 304 HOH B O   1 
HETATM 4222 O O   . HOH F 2 .   ? 16.509  2.398   -59.214 1.00 41.91 ? 305 HOH B O   1 
HETATM 4223 O O   . HOH F 2 .   ? -9.530  5.103   -30.090 1.00 32.88 ? 306 HOH B O   1 
HETATM 4224 O O   . HOH F 2 .   ? 16.470  -12.767 -33.858 1.00 32.85 ? 307 HOH B O   1 
HETATM 4225 O O   . HOH F 2 .   ? -4.950  -4.997  -37.284 1.00 30.86 ? 308 HOH B O   1 
HETATM 4226 O O   . HOH F 2 .   ? 4.109   12.296  -55.935 1.00 32.32 ? 313 HOH B O   1 
HETATM 4227 O O   . HOH F 2 .   ? 22.223  14.219  -55.269 1.00 26.91 ? 315 HOH B O   1 
HETATM 4228 O O   . HOH F 2 .   ? 9.932   -10.837 -37.727 1.00 29.74 ? 318 HOH B O   1 
HETATM 4229 O O   . HOH F 2 .   ? 9.851   -8.746  -48.688 1.00 36.05 ? 319 HOH B O   1 
HETATM 4230 O O   . HOH F 2 .   ? 6.729   19.135  -46.906 1.00 34.49 ? 321 HOH B O   1 
HETATM 4231 O O   . HOH F 2 .   ? 15.049  1.068   -39.987 1.00 24.33 ? 323 HOH B O   1 
HETATM 4232 O O   . HOH F 2 .   ? -8.904  -7.534  -39.499 1.00 47.32 ? 327 HOH B O   1 
HETATM 4233 O O   . HOH F 2 .   ? 2.274   10.376  -57.151 1.00 32.58 ? 331 HOH B O   1 
HETATM 4234 O O   . HOH F 2 .   ? 5.307   17.902  -51.874 1.00 34.21 ? 333 HOH B O   1 
HETATM 4235 O O   . HOH F 2 .   ? -3.447  11.599  -53.732 1.00 35.71 ? 335 HOH B O   1 
HETATM 4236 O O   . HOH F 2 .   ? 6.418   21.244  -48.933 1.00 35.68 ? 339 HOH B O   1 
HETATM 4237 O O   . HOH F 2 .   ? -13.207 15.031  -40.530 1.00 55.67 ? 343 HOH B O   1 
HETATM 4238 O O   . HOH F 2 .   ? 6.523   18.334  -36.242 1.00 37.16 ? 345 HOH B O   1 
HETATM 4239 O O   . HOH F 2 .   ? 15.592  2.756   -56.605 1.00 34.14 ? 347 HOH B O   1 
HETATM 4240 O O   . HOH F 2 .   ? 23.582  2.791   -45.105 1.00 36.65 ? 370 HOH B O   1 
HETATM 4241 O O   . HOH F 2 .   ? 18.834  -6.233  -36.230 1.00 41.49 ? 383 HOH B O   1 
HETATM 4242 O O   . HOH F 2 .   ? 5.534   -6.948  -62.293 1.00 44.13 ? 391 HOH B O   1 
HETATM 4243 O O   . HOH F 2 .   ? 18.680  0.556   -40.503 1.00 44.11 ? 393 HOH B O   1 
HETATM 4244 O O   . HOH F 2 .   ? 0.593   -14.895 -57.288 1.00 42.11 ? 398 HOH B O   1 
HETATM 4245 O O   . HOH F 2 .   ? 14.644  14.054  -43.986 1.00 46.59 ? 401 HOH B O   1 
HETATM 4246 O O   . HOH F 2 .   ? -13.743 1.112   -33.302 1.00 36.10 ? 411 HOH B O   1 
HETATM 4247 O O   . HOH F 2 .   ? 17.842  1.830   -38.469 1.00 35.31 ? 415 HOH B O   1 
HETATM 4248 O O   . HOH F 2 .   ? 20.379  -8.138  -40.539 1.00 27.75 ? 425 HOH B O   1 
HETATM 4249 O O   . HOH G 2 .   ? -36.839 11.112  -38.866 1.00 16.24 ? 154 HOH C O   1 
HETATM 4250 O O   . HOH G 2 .   ? -27.245 15.156  -16.190 1.00 15.93 ? 155 HOH C O   1 
HETATM 4251 O O   . HOH G 2 .   ? -9.288  14.040  -31.009 1.00 29.44 ? 156 HOH C O   1 
HETATM 4252 O O   . HOH G 2 .   ? -38.622 8.446   -22.642 1.00 38.90 ? 157 HOH C O   1 
HETATM 4253 O O   . HOH G 2 .   ? -14.972 5.508   -31.601 1.00 18.40 ? 158 HOH C O   1 
HETATM 4254 O O   . HOH G 2 .   ? -44.160 18.478  -30.777 1.00 26.79 ? 159 HOH C O   1 
HETATM 4255 O O   . HOH G 2 .   ? -42.039 16.335  -24.156 1.00 21.31 ? 160 HOH C O   1 
HETATM 4256 O O   . HOH G 2 .   ? -26.719 14.795  -40.534 1.00 43.05 ? 161 HOH C O   1 
HETATM 4257 O O   . HOH G 2 .   ? -31.543 14.814  -40.156 1.00 26.72 ? 162 HOH C O   1 
HETATM 4258 O O   . HOH G 2 .   ? -17.547 4.004   -38.261 1.00 25.30 ? 163 HOH C O   1 
HETATM 4259 O O   . HOH G 2 .   ? -21.848 14.635  -42.262 1.00 32.53 ? 164 HOH C O   1 
HETATM 4260 O O   . HOH G 2 .   ? -27.705 20.695  -37.856 1.00 24.49 ? 165 HOH C O   1 
HETATM 4261 O O   . HOH G 2 .   ? -44.137 13.344  -42.362 1.00 25.83 ? 166 HOH C O   1 
HETATM 4262 O O   . HOH G 2 .   ? -26.755 26.963  -29.122 1.00 33.02 ? 167 HOH C O   1 
HETATM 4263 O O   . HOH G 2 .   ? -30.108 8.845   -21.791 1.00 5.34  ? 168 HOH C O   1 
HETATM 4264 O O   . HOH G 2 .   ? -29.697 15.720  -20.456 1.00 42.04 ? 169 HOH C O   1 
HETATM 4265 O O   . HOH G 2 .   ? -24.927 21.302  -32.841 1.00 33.86 ? 170 HOH C O   1 
HETATM 4266 O O   . HOH G 2 .   ? -17.204 10.301  -37.662 1.00 14.28 ? 171 HOH C O   1 
HETATM 4267 O O   . HOH G 2 .   ? -22.675 -4.001  -34.662 1.00 38.33 ? 172 HOH C O   1 
HETATM 4268 O O   . HOH G 2 .   ? -18.986 22.368  -27.404 1.00 40.86 ? 173 HOH C O   1 
HETATM 4269 O O   . HOH G 2 .   ? -12.084 19.630  -31.978 1.00 36.31 ? 174 HOH C O   1 
HETATM 4270 O O   . HOH G 2 .   ? -27.538 1.658   -28.863 1.00 15.63 ? 175 HOH C O   1 
HETATM 4271 O O   . HOH G 2 .   ? -28.773 4.388   -39.659 1.00 30.69 ? 176 HOH C O   1 
HETATM 4272 O O   . HOH G 2 .   ? -35.532 4.124   -37.929 1.00 33.64 ? 177 HOH C O   1 
HETATM 4273 O O   . HOH G 2 .   ? -41.404 12.539  -21.992 1.00 21.06 ? 178 HOH C O   1 
HETATM 4274 O O   . HOH G 2 .   ? -28.131 11.058  -43.087 1.00 24.13 ? 179 HOH C O   1 
HETATM 4275 O O   . HOH G 2 .   ? -33.852 10.892  -20.091 1.00 25.99 ? 180 HOH C O   1 
HETATM 4276 O O   . HOH G 2 .   ? -30.750 25.629  -29.270 1.00 34.14 ? 181 HOH C O   1 
HETATM 4277 O O   . HOH G 2 .   ? -15.084 6.578   -26.150 1.00 25.55 ? 182 HOH C O   1 
HETATM 4278 O O   . HOH G 2 .   ? -32.174 26.215  -17.036 1.00 31.03 ? 183 HOH C O   1 
HETATM 4279 O O   . HOH G 2 .   ? -15.211 3.203   -33.235 1.00 19.81 ? 184 HOH C O   1 
HETATM 4280 O O   . HOH G 2 .   ? -47.332 8.192   -30.744 1.00 27.00 ? 191 HOH C O   1 
HETATM 4281 O O   . HOH G 2 .   ? -13.211 13.206  -32.930 1.00 23.90 ? 196 HOH C O   1 
HETATM 4282 O O   . HOH G 2 .   ? -21.890 19.106  -39.208 1.00 26.13 ? 200 HOH C O   1 
HETATM 4283 O O   . HOH G 2 .   ? -26.804 18.805  -40.587 1.00 39.74 ? 201 HOH C O   1 
HETATM 4284 O O   . HOH G 2 .   ? -19.588 5.952   -45.328 1.00 37.35 ? 202 HOH C O   1 
HETATM 4285 O O   . HOH G 2 .   ? -18.899 4.804   -48.229 1.00 34.66 ? 203 HOH C O   1 
HETATM 4286 O O   . HOH G 2 .   ? -22.851 17.197  -37.376 1.00 27.77 ? 204 HOH C O   1 
HETATM 4287 O O   . HOH G 2 .   ? -42.536 5.305   -30.661 1.00 35.31 ? 208 HOH C O   1 
HETATM 4288 O O   . HOH G 2 .   ? -25.910 -5.902  -23.171 1.00 32.50 ? 215 HOH C O   1 
HETATM 4289 O O   . HOH G 2 .   ? -11.385 18.177  -26.043 1.00 33.19 ? 216 HOH C O   1 
HETATM 4290 O O   . HOH G 2 .   ? -37.466 25.131  -31.718 1.00 29.63 ? 218 HOH C O   1 
HETATM 4291 O O   . HOH G 2 .   ? -30.652 10.839  -43.120 1.00 23.41 ? 219 HOH C O   1 
HETATM 4292 O O   . HOH G 2 .   ? -15.484 10.998  -40.233 1.00 29.27 ? 223 HOH C O   1 
HETATM 4293 O O   . HOH G 2 .   ? -17.297 20.785  -22.842 1.00 36.91 ? 228 HOH C O   1 
HETATM 4294 O O   . HOH G 2 .   ? -9.262  8.806   -29.093 1.00 27.59 ? 232 HOH C O   1 
HETATM 4295 O O   . HOH G 2 .   ? -14.207 4.793   -42.404 1.00 34.42 ? 238 HOH C O   1 
HETATM 4296 O O   . HOH G 2 .   ? -30.532 11.086  -19.637 1.00 25.58 ? 245 HOH C O   1 
HETATM 4297 O O   . HOH G 2 .   ? -15.672 15.518  -26.350 1.00 29.14 ? 246 HOH C O   1 
HETATM 4298 O O   . HOH G 2 .   ? -11.980 9.433   -26.513 1.00 32.70 ? 249 HOH C O   1 
HETATM 4299 O O   . HOH G 2 .   ? -29.649 5.747   -43.516 1.00 33.64 ? 250 HOH C O   1 
HETATM 4300 O O   . HOH G 2 .   ? -21.360 2.393   -38.125 1.00 32.03 ? 270 HOH C O   1 
HETATM 4301 O O   . HOH G 2 .   ? -39.797 9.871   -39.612 1.00 34.63 ? 271 HOH C O   1 
HETATM 4302 O O   . HOH G 2 .   ? -35.613 2.485   -30.659 1.00 34.16 ? 273 HOH C O   1 
HETATM 4303 O O   . HOH G 2 .   ? -42.513 20.033  -41.234 1.00 28.83 ? 282 HOH C O   1 
HETATM 4304 O O   . HOH G 2 .   ? -49.586 15.510  -34.871 1.00 29.20 ? 284 HOH C O   1 
HETATM 4305 O O   . HOH G 2 .   ? -47.004 18.710  -18.988 1.00 40.91 ? 293 HOH C O   1 
HETATM 4306 O O   . HOH G 2 .   ? -42.242 7.157   -38.507 1.00 38.67 ? 298 HOH C O   1 
HETATM 4307 O O   . HOH G 2 .   ? -36.600 4.730   -19.677 1.00 35.81 ? 300 HOH C O   1 
HETATM 4308 O O   . HOH G 2 .   ? -44.943 17.340  -28.600 1.00 34.77 ? 302 HOH C O   1 
HETATM 4309 O O   . HOH G 2 .   ? -37.220 18.861  -19.750 1.00 42.14 ? 311 HOH C O   1 
HETATM 4310 O O   . HOH G 2 .   ? -14.861 14.104  -24.619 1.00 37.26 ? 329 HOH C O   1 
HETATM 4311 O O   . HOH G 2 .   ? -48.860 19.483  -16.723 1.00 44.81 ? 334 HOH C O   1 
HETATM 4312 O O   . HOH G 2 .   ? -6.626  17.144  -30.390 1.00 38.59 ? 338 HOH C O   1 
HETATM 4313 O O   . HOH G 2 .   ? -7.468  12.240  -30.023 1.00 31.74 ? 344 HOH C O   1 
HETATM 4314 O O   . HOH G 2 .   ? -33.432 25.900  -27.893 1.00 35.00 ? 349 HOH C O   1 
HETATM 4315 O O   . HOH G 2 .   ? -14.554 4.509   -27.671 1.00 41.16 ? 359 HOH C O   1 
HETATM 4316 O O   . HOH G 2 .   ? -13.335 2.475   -28.794 1.00 46.29 ? 365 HOH C O   1 
HETATM 4317 O O   . HOH G 2 .   ? -21.435 23.571  -39.059 1.00 46.94 ? 366 HOH C O   1 
HETATM 4318 O O   . HOH G 2 .   ? -26.759 21.304  -8.435  1.00 36.84 ? 376 HOH C O   1 
HETATM 4319 O O   . HOH G 2 .   ? -19.438 8.421   -45.627 1.00 36.77 ? 384 HOH C O   1 
HETATM 4320 O O   . HOH G 2 .   ? -24.156 14.235  -43.332 1.00 38.02 ? 389 HOH C O   1 
HETATM 4321 O O   . HOH G 2 .   ? -28.387 1.148   -38.320 1.00 43.93 ? 390 HOH C O   1 
HETATM 4322 O O   . HOH G 2 .   ? -13.672 11.153  -25.207 1.00 33.00 ? 392 HOH C O   1 
HETATM 4323 O O   . HOH G 2 .   ? -47.986 19.019  -40.235 1.00 49.62 ? 399 HOH C O   1 
HETATM 4324 O O   . HOH G 2 .   ? -33.196 12.625  -16.013 1.00 38.09 ? 419 HOH C O   1 
HETATM 4325 O O   . HOH G 2 .   ? -31.407 14.474  -19.470 1.00 26.54 ? 426 HOH C O   1 
HETATM 4326 O O   . HOH H 2 .   ? -26.152 -1.098  -23.175 1.00 24.38 ? 154 HOH D O   1 
HETATM 4327 O O   . HOH H 2 .   ? -34.069 8.390   -18.951 1.00 26.29 ? 155 HOH D O   1 
HETATM 4328 O O   . HOH H 2 .   ? -10.879 16.646  -6.744  1.00 31.48 ? 156 HOH D O   1 
HETATM 4329 O O   . HOH H 2 .   ? -34.845 0.474   -0.146  1.00 18.44 ? 157 HOH D O   1 
HETATM 4330 O O   . HOH H 2 .   ? -20.991 -6.391  -10.347 1.00 44.44 ? 158 HOH D O   1 
HETATM 4331 O O   . HOH H 2 .   ? -29.584 6.367   -21.727 1.00 16.88 ? 159 HOH D O   1 
HETATM 4332 O O   . HOH H 2 .   ? -24.921 -1.680  -3.511  1.00 30.64 ? 160 HOH D O   1 
HETATM 4333 O O   . HOH H 2 .   ? -29.709 3.113   -16.467 1.00 43.00 ? 162 HOH D O   1 
HETATM 4334 O O   . HOH H 2 .   ? -29.774 10.249  -17.432 1.00 21.02 ? 163 HOH D O   1 
HETATM 4335 O O   . HOH H 2 .   ? -9.737  14.536  -15.556 1.00 40.03 ? 164 HOH D O   1 
HETATM 4336 O O   . HOH H 2 .   ? -24.491 -3.411  -6.020  1.00 25.83 ? 165 HOH D O   1 
HETATM 4337 O O   . HOH H 2 .   ? -13.825 4.280   -19.185 1.00 19.60 ? 166 HOH D O   1 
HETATM 4338 O O   . HOH H 2 .   ? -34.197 -3.145  -10.039 1.00 29.74 ? 167 HOH D O   1 
HETATM 4339 O O   . HOH H 2 .   ? -7.236  10.032  -15.200 1.00 24.60 ? 168 HOH D O   1 
HETATM 4340 O O   . HOH H 2 .   ? -18.733 -0.781  -8.569  1.00 46.60 ? 169 HOH D O   1 
HETATM 4341 O O   . HOH H 2 .   ? -31.843 11.023  11.049  1.00 27.97 ? 170 HOH D O   1 
HETATM 4342 O O   . HOH H 2 .   ? -29.861 6.093   -16.576 1.00 23.58 ? 171 HOH D O   1 
HETATM 4343 O O   . HOH H 2 .   ? -27.798 12.693  -15.785 1.00 20.98 ? 172 HOH D O   1 
HETATM 4344 O O   . HOH H 2 .   ? -21.766 19.263  -11.483 1.00 26.23 ? 173 HOH D O   1 
HETATM 4345 O O   . HOH H 2 .   ? -7.066  8.174   -11.159 1.00 38.25 ? 174 HOH D O   1 
HETATM 4346 O O   . HOH H 2 .   ? -30.833 0.588   3.531   1.00 34.86 ? 175 HOH D O   1 
HETATM 4347 O O   . HOH H 2 .   ? -38.803 12.512  -3.993  1.00 46.50 ? 176 HOH D O   1 
HETATM 4348 O O   . HOH H 2 .   ? -17.140 -3.107  -16.358 1.00 39.75 ? 177 HOH D O   1 
HETATM 4349 O O   . HOH H 2 .   ? -34.942 4.483   -14.729 1.00 33.47 ? 178 HOH D O   1 
HETATM 4350 O O   . HOH H 2 .   ? -26.222 -5.108  -9.216  1.00 24.05 ? 179 HOH D O   1 
HETATM 4351 O O   . HOH H 2 .   ? -35.612 2.483   -13.483 1.00 33.08 ? 180 HOH D O   1 
HETATM 4352 O O   . HOH H 2 .   ? -19.473 6.117   0.408   1.00 24.07 ? 181 HOH D O   1 
HETATM 4353 O O   . HOH H 2 .   ? -8.512  15.913  -8.615  1.00 35.04 ? 182 HOH D O   1 
HETATM 4354 O O   . HOH H 2 .   ? -37.269 12.785  1.112   1.00 34.58 ? 183 HOH D O   1 
HETATM 4355 O O   . HOH H 2 .   ? -14.164 3.045   -6.238  1.00 28.68 ? 187 HOH D O   1 
HETATM 4356 O O   . HOH H 2 .   ? -3.396  7.801   -6.843  1.00 36.30 ? 188 HOH D O   1 
HETATM 4357 O O   . HOH H 2 .   ? -4.618  9.626   -6.097  1.00 24.81 ? 189 HOH D O   1 
HETATM 4358 O O   . HOH H 2 .   ? -23.434 21.947  -16.210 1.00 48.38 ? 199 HOH D O   1 
HETATM 4359 O O   . HOH H 2 .   ? -33.789 -0.219  -28.041 1.00 31.42 ? 205 HOH D O   1 
HETATM 4360 O O   . HOH H 2 .   ? -17.518 10.599  2.629   1.00 21.49 ? 207 HOH D O   1 
HETATM 4361 O O   . HOH H 2 .   ? -30.614 -4.292  -3.399  1.00 41.42 ? 211 HOH D O   1 
HETATM 4362 O O   . HOH H 2 .   ? -15.393 1.834   -1.914  1.00 30.69 ? 213 HOH D O   1 
HETATM 4363 O O   . HOH H 2 .   ? -28.537 13.599  5.259   1.00 32.82 ? 214 HOH D O   1 
HETATM 4364 O O   . HOH H 2 .   ? -31.830 10.540  -15.049 1.00 32.33 ? 217 HOH D O   1 
HETATM 4365 O O   . HOH H 2 .   ? -38.015 1.428   -15.118 1.00 31.19 ? 227 HOH D O   1 
HETATM 4366 O O   . HOH H 2 .   ? -18.429 -6.022  -13.839 1.00 39.91 ? 240 HOH D O   1 
HETATM 4367 O O   . HOH H 2 .   ? -12.640 1.086   -5.852  1.00 44.79 ? 265 HOH D O   1 
HETATM 4368 O O   . HOH H 2 .   ? -10.450 2.243   -21.408 1.00 33.67 ? 266 HOH D O   1 
HETATM 4369 O O   . HOH H 2 .   ? -26.891 18.395  -5.865  1.00 45.48 ? 272 HOH D O   1 
HETATM 4370 O O   . HOH H 2 .   ? -29.749 18.503  -5.113  1.00 37.36 ? 279 HOH D O   1 
HETATM 4371 O O   . HOH H 2 .   ? -29.727 6.931   8.858   1.00 33.94 ? 283 HOH D O   1 
HETATM 4372 O O   . HOH H 2 .   ? -14.914 9.783   1.136   1.00 29.25 ? 285 HOH D O   1 
HETATM 4373 O O   . HOH H 2 .   ? -8.998  17.020  -14.660 1.00 34.54 ? 289 HOH D O   1 
HETATM 4374 O O   . HOH H 2 .   ? -18.979 27.143  -19.566 1.00 40.56 ? 303 HOH D O   1 
HETATM 4375 O O   . HOH H 2 .   ? -5.980  9.232   -18.329 1.00 42.32 ? 309 HOH D O   1 
HETATM 4376 O O   . HOH H 2 .   ? -24.351 -5.752  4.108   1.00 31.89 ? 328 HOH D O   1 
HETATM 4377 O O   . HOH H 2 .   ? -6.581  -0.588  -19.388 1.00 35.64 ? 342 HOH D O   1 
HETATM 4378 O O   . HOH H 2 .   ? -36.155 16.047  5.771   1.00 29.92 ? 346 HOH D O   1 
HETATM 4379 O O   . HOH H 2 .   ? -19.040 -4.145  -4.830  1.00 44.25 ? 352 HOH D O   1 
HETATM 4380 O O   . HOH H 2 .   ? -37.460 4.995   6.658   1.00 33.13 ? 355 HOH D O   1 
HETATM 4381 O O   . HOH H 2 .   ? -38.450 10.732  -9.897  1.00 32.48 ? 356 HOH D O   1 
HETATM 4382 O O   . HOH H 2 .   ? -7.365  19.225  -15.496 1.00 43.47 ? 357 HOH D O   1 
HETATM 4383 O O   . HOH H 2 .   ? -11.092 7.181   -0.506  1.00 31.34 ? 358 HOH D O   1 
HETATM 4384 O O   . HOH H 2 .   ? -14.498 -0.367  -1.608  1.00 38.40 ? 373 HOH D O   1 
HETATM 4385 O O   . HOH H 2 .   ? -12.610 20.005  -6.434  1.00 43.19 ? 374 HOH D O   1 
HETATM 4386 O O   . HOH H 2 .   ? -18.056 -0.911  -21.584 1.00 39.00 ? 378 HOH D O   1 
HETATM 4387 O O   . HOH H 2 .   ? -35.157 9.014   -16.341 1.00 37.16 ? 381 HOH D O   1 
HETATM 4388 O O   . HOH H 2 .   ? -15.369 5.330   -1.141  1.00 36.56 ? 396 HOH D O   1 
HETATM 4389 O O   . HOH H 2 .   ? -25.681 -6.387  -12.553 1.00 37.47 ? 402 HOH D O   1 
HETATM 4390 O O   . HOH H 2 .   ? -30.495 -2.741  -22.863 1.00 34.63 ? 410 HOH D O   1 
HETATM 4391 O O   . HOH H 2 .   ? -25.946 11.950  4.612   1.00 37.68 ? 416 HOH D O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ALA 1   1   1   ALA ALA A . n 
A 1 2   THR 2   2   2   THR THR A . n 
A 1 3   LYS 3   3   3   LYS LYS A . n 
A 1 4   ALA 4   4   4   ALA ALA A . n 
A 1 5   VAL 5   5   5   VAL VAL A . n 
A 1 6   CYS 6   6   6   CYS CYS A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   LEU 8   8   8   LEU LEU A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  GLY 10  10  10  GLY GLY A . n 
A 1 11  ASP 11  11  11  ASP ASP A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  VAL 14  14  14  VAL VAL A . n 
A 1 15  GLN 15  15  15  GLN GLN A . n 
A 1 16  GLY 16  16  16  GLY GLY A . n 
A 1 17  ILE 17  17  17  ILE ILE A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  ASN 19  19  19  ASN ASN A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  GLU 21  21  21  GLU GLU A . n 
A 1 22  GLN 22  22  22  GLN GLN A . n 
A 1 23  LYS 23  23  23  LYS LYS A . n 
A 1 24  GLU 24  24  24  GLU GLU A . n 
A 1 25  SER 25  25  25  SER SER A . n 
A 1 26  ASN 26  26  26  ASN ASN A . n 
A 1 27  GLY 27  27  27  GLY GLY A . n 
A 1 28  PRO 28  28  28  PRO PRO A . n 
A 1 29  VAL 29  29  29  VAL VAL A . n 
A 1 30  LYS 30  30  30  LYS LYS A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  TRP 32  32  32  TRP TRP A . n 
A 1 33  GLY 33  33  33  GLY GLY A . n 
A 1 34  SER 34  34  34  SER SER A . n 
A 1 35  ILE 35  35  35  ILE ILE A . n 
A 1 36  LYS 36  36  36  LYS LYS A . n 
A 1 37  GLY 37  37  37  GLY GLY A . n 
A 1 38  LEU 38  38  38  LEU LEU A . n 
A 1 39  THR 39  39  39  THR THR A . n 
A 1 40  GLU 40  40  40  GLU GLU A . n 
A 1 41  GLY 41  41  41  GLY GLY A . n 
A 1 42  LEU 42  42  42  LEU LEU A . n 
A 1 43  HIS 43  43  43  HIS HIS A . n 
A 1 44  GLY 44  44  44  GLY GLY A . n 
A 1 45  PHE 45  45  45  PHE PHE A . n 
A 1 46  HIS 46  46  46  HIS HIS A . n 
A 1 47  VAL 47  47  47  VAL VAL A . n 
A 1 48  HIS 48  48  48  HIS HIS A . n 
A 1 49  GLU 49  49  49  GLU GLU A . n 
A 1 50  PHE 50  50  50  PHE PHE A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  ARG 54  54  54  ARG ARG A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  GLY 56  56  56  GLY GLY A . n 
A 1 57  CYS 57  57  57  CYS CYS A . n 
A 1 58  THR 58  58  58  THR THR A . n 
A 1 59  SER 59  59  59  SER SER A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  GLY 61  61  61  GLY GLY A . n 
A 1 62  PRO 62  62  62  PRO PRO A . n 
A 1 63  HIS 63  63  63  HIS HIS A . n 
A 1 64  PHE 64  64  64  PHE PHE A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  PRO 66  66  66  PRO PRO A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  SER 68  68  68  SER SER A . n 
A 1 69  ARG 69  69  69  ARG ARG A . n 
A 1 70  LYS 70  70  70  LYS LYS A . n 
A 1 71  HIS 71  71  71  HIS HIS A . n 
A 1 72  GLY 72  72  72  GLY GLY A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LYS 75  75  75  LYS LYS A . n 
A 1 76  ASP 76  76  76  ASP ASP A . n 
A 1 77  GLU 77  77  77  GLU GLU A . n 
A 1 78  GLU 78  78  78  GLU GLU A . n 
A 1 79  ARG 79  79  79  ARG ARG A . n 
A 1 80  HIS 80  80  80  HIS HIS A . n 
A 1 81  VAL 81  81  81  VAL VAL A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  ASP 83  83  83  ASP ASP A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  ASN 86  86  86  ASN ASN A . n 
A 1 87  VAL 87  87  87  VAL VAL A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  ASP 90  90  90  ASP ASP A . n 
A 1 91  LYS 91  91  91  LYS LYS A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  GLY 93  93  93  GLY GLY A . n 
A 1 94  VAL 94  94  94  VAL VAL A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  ASP 96  96  96  ASP ASP A . n 
A 1 97  VAL 97  97  97  VAL VAL A . n 
A 1 98  SER 98  98  98  SER SER A . n 
A 1 99  ILE 99  99  99  ILE ILE A . n 
A 1 100 GLU 100 100 100 GLU GLU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 SER 102 102 102 SER SER A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 ILE 104 104 104 ILE ILE A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 SER 107 107 107 SER SER A . n 
A 1 108 GLY 108 108 108 GLY GLY A . n 
A 1 109 ASP 109 109 109 ASP ASP A . n 
A 1 110 HIS 110 110 110 HIS HIS A . n 
A 1 111 CYS 111 111 111 CYS CYS A . n 
A 1 112 ILE 112 112 112 ILE ILE A . n 
A 1 113 ILE 113 113 113 ILE ILE A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 ARG 115 115 115 ARG ARG A . n 
A 1 116 THR 116 116 116 THR THR A . n 
A 1 117 LEU 117 117 117 LEU LEU A . n 
A 1 118 VAL 118 118 118 VAL VAL A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 HIS 120 120 120 HIS HIS A . n 
A 1 121 GLU 121 121 121 GLU GLU A . n 
A 1 122 LYS 122 122 122 LYS LYS A . n 
A 1 123 ALA 123 123 123 ALA ALA A . n 
A 1 124 ASP 124 124 124 ASP ASP A . n 
A 1 125 ASP 125 125 125 ASP ASP A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 GLY 127 127 127 GLY GLY A . n 
A 1 128 LYS 128 128 128 LYS LYS A . n 
A 1 129 GLY 129 129 129 GLY GLY A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ASN 131 131 131 ASN ASN A . n 
A 1 132 GLU 132 132 132 GLU GLU A . n 
A 1 133 GLU 133 133 133 GLU GLU A . n 
A 1 134 SER 134 134 134 SER SER A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 LYS 136 136 136 LYS LYS A . n 
A 1 137 THR 137 137 137 THR THR A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 ASN 139 139 139 ASN ASN A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 GLY 141 141 141 GLY GLY A . n 
A 1 142 SER 142 142 142 SER SER A . n 
A 1 143 ARG 143 143 143 ARG ARG A . n 
A 1 144 LEU 144 144 144 LEU LEU A . n 
A 1 145 ALA 145 145 145 ALA ALA A . n 
A 1 146 CYS 146 146 146 CYS CYS A . n 
A 1 147 GLY 147 147 147 GLY GLY A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 ILE 149 149 149 ILE ILE A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 ILE 151 151 151 ILE ILE A . n 
A 1 152 ALA 152 152 152 ALA ALA A . n 
A 1 153 GLN 153 153 153 GLN GLN A . n 
B 1 1   ALA 1   1   1   ALA ALA B . n 
B 1 2   THR 2   2   2   THR THR B . n 
B 1 3   LYS 3   3   3   LYS LYS B . n 
B 1 4   ALA 4   4   4   ALA ALA B . n 
B 1 5   VAL 5   5   5   VAL VAL B . n 
B 1 6   CYS 6   6   6   CYS CYS B . n 
B 1 7   VAL 7   7   7   VAL VAL B . n 
B 1 8   LEU 8   8   8   LEU LEU B . n 
B 1 9   LYS 9   9   9   LYS LYS B . n 
B 1 10  GLY 10  10  10  GLY GLY B . n 
B 1 11  ASP 11  11  11  ASP ASP B . n 
B 1 12  GLY 12  12  12  GLY GLY B . n 
B 1 13  PRO 13  13  13  PRO PRO B . n 
B 1 14  VAL 14  14  14  VAL VAL B . n 
B 1 15  GLN 15  15  15  GLN GLN B . n 
B 1 16  GLY 16  16  16  GLY GLY B . n 
B 1 17  ILE 17  17  17  ILE ILE B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  ASN 19  19  19  ASN ASN B . n 
B 1 20  PHE 20  20  20  PHE PHE B . n 
B 1 21  GLU 21  21  21  GLU GLU B . n 
B 1 22  GLN 22  22  22  GLN GLN B . n 
B 1 23  LYS 23  23  23  LYS LYS B . n 
B 1 24  GLU 24  24  24  GLU GLU B . n 
B 1 25  SER 25  25  25  SER SER B . n 
B 1 26  ASN 26  26  26  ASN ASN B . n 
B 1 27  GLY 27  27  27  GLY GLY B . n 
B 1 28  PRO 28  28  28  PRO PRO B . n 
B 1 29  VAL 29  29  29  VAL VAL B . n 
B 1 30  LYS 30  30  30  LYS LYS B . n 
B 1 31  VAL 31  31  31  VAL VAL B . n 
B 1 32  TRP 32  32  32  TRP TRP B . n 
B 1 33  GLY 33  33  33  GLY GLY B . n 
B 1 34  SER 34  34  34  SER SER B . n 
B 1 35  ILE 35  35  35  ILE ILE B . n 
B 1 36  LYS 36  36  36  LYS LYS B . n 
B 1 37  GLY 37  37  37  GLY GLY B . n 
B 1 38  LEU 38  38  38  LEU LEU B . n 
B 1 39  THR 39  39  39  THR THR B . n 
B 1 40  GLU 40  40  40  GLU GLU B . n 
B 1 41  GLY 41  41  41  GLY GLY B . n 
B 1 42  LEU 42  42  42  LEU LEU B . n 
B 1 43  HIS 43  43  43  HIS HIS B . n 
B 1 44  GLY 44  44  44  GLY GLY B . n 
B 1 45  PHE 45  45  45  PHE PHE B . n 
B 1 46  HIS 46  46  46  HIS HIS B . n 
B 1 47  VAL 47  47  47  VAL VAL B . n 
B 1 48  HIS 48  48  48  HIS HIS B . n 
B 1 49  GLU 49  49  49  GLU GLU B . n 
B 1 50  PHE 50  50  50  PHE PHE B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ASP 52  52  52  ASP ASP B . n 
B 1 53  ASN 53  53  53  ASN ASN B . n 
B 1 54  ARG 54  54  54  ARG ARG B . n 
B 1 55  ALA 55  55  55  ALA ALA B . n 
B 1 56  GLY 56  56  56  GLY GLY B . n 
B 1 57  CYS 57  57  57  CYS CYS B . n 
B 1 58  THR 58  58  58  THR THR B . n 
B 1 59  SER 59  59  59  SER SER B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  GLY 61  61  61  GLY GLY B . n 
B 1 62  PRO 62  62  62  PRO PRO B . n 
B 1 63  HIS 63  63  63  HIS HIS B . n 
B 1 64  PHE 64  64  64  PHE PHE B . n 
B 1 65  ASN 65  65  65  ASN ASN B . n 
B 1 66  PRO 66  66  66  PRO PRO B . n 
B 1 67  LEU 67  67  67  LEU LEU B . n 
B 1 68  SER 68  68  68  SER SER B . n 
B 1 69  ARG 69  69  69  ARG ARG B . n 
B 1 70  LYS 70  70  70  LYS LYS B . n 
B 1 71  HIS 71  71  71  HIS HIS B . n 
B 1 72  GLY 72  72  72  GLY GLY B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  LYS 75  75  75  LYS LYS B . n 
B 1 76  ASP 76  76  76  ASP ASP B . n 
B 1 77  GLU 77  77  77  GLU GLU B . n 
B 1 78  GLU 78  78  78  GLU GLU B . n 
B 1 79  ARG 79  79  79  ARG ARG B . n 
B 1 80  HIS 80  80  80  HIS HIS B . n 
B 1 81  VAL 81  81  81  VAL VAL B . n 
B 1 82  GLY 82  82  82  GLY GLY B . n 
B 1 83  ASP 83  83  83  ASP ASP B . n 
B 1 84  LEU 84  84  84  LEU LEU B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  ASN 86  86  86  ASN ASN B . n 
B 1 87  VAL 87  87  87  VAL VAL B . n 
B 1 88  THR 88  88  88  THR THR B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  ASP 90  90  90  ASP ASP B . n 
B 1 91  LYS 91  91  91  LYS LYS B . n 
B 1 92  ASP 92  92  92  ASP ASP B . n 
B 1 93  GLY 93  93  93  GLY GLY B . n 
B 1 94  VAL 94  94  94  VAL VAL B . n 
B 1 95  ALA 95  95  95  ALA ALA B . n 
B 1 96  ASP 96  96  96  ASP ASP B . n 
B 1 97  VAL 97  97  97  VAL VAL B . n 
B 1 98  SER 98  98  98  SER SER B . n 
B 1 99  ILE 99  99  99  ILE ILE B . n 
B 1 100 GLU 100 100 100 GLU GLU B . n 
B 1 101 ASP 101 101 101 ASP ASP B . n 
B 1 102 SER 102 102 102 SER SER B . n 
B 1 103 VAL 103 103 103 VAL VAL B . n 
B 1 104 ILE 104 104 104 ILE ILE B . n 
B 1 105 SER 105 105 105 SER SER B . n 
B 1 106 LEU 106 106 106 LEU LEU B . n 
B 1 107 SER 107 107 107 SER SER B . n 
B 1 108 GLY 108 108 108 GLY GLY B . n 
B 1 109 ASP 109 109 109 ASP ASP B . n 
B 1 110 HIS 110 110 110 HIS HIS B . n 
B 1 111 CYS 111 111 111 CYS CYS B . n 
B 1 112 ILE 112 112 112 ILE ILE B . n 
B 1 113 ILE 113 113 113 ILE ILE B . n 
B 1 114 GLY 114 114 114 GLY GLY B . n 
B 1 115 ARG 115 115 115 ARG ARG B . n 
B 1 116 THR 116 116 116 THR THR B . n 
B 1 117 LEU 117 117 117 LEU LEU B . n 
B 1 118 VAL 118 118 118 VAL VAL B . n 
B 1 119 VAL 119 119 119 VAL VAL B . n 
B 1 120 HIS 120 120 120 HIS HIS B . n 
B 1 121 GLU 121 121 121 GLU GLU B . n 
B 1 122 LYS 122 122 122 LYS LYS B . n 
B 1 123 ALA 123 123 123 ALA ALA B . n 
B 1 124 ASP 124 124 124 ASP ASP B . n 
B 1 125 ASP 125 125 125 ASP ASP B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 GLY 127 127 127 GLY GLY B . n 
B 1 128 LYS 128 128 128 LYS LYS B . n 
B 1 129 GLY 129 129 129 GLY GLY B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 ASN 131 131 131 ASN ASN B . n 
B 1 132 GLU 132 132 132 GLU GLU B . n 
B 1 133 GLU 133 133 133 GLU GLU B . n 
B 1 134 SER 134 134 134 SER SER B . n 
B 1 135 THR 135 135 135 THR THR B . n 
B 1 136 LYS 136 136 136 LYS LYS B . n 
B 1 137 THR 137 137 137 THR THR B . n 
B 1 138 GLY 138 138 138 GLY GLY B . n 
B 1 139 ASN 139 139 139 ASN ASN B . n 
B 1 140 ALA 140 140 140 ALA ALA B . n 
B 1 141 GLY 141 141 141 GLY GLY B . n 
B 1 142 SER 142 142 142 SER SER B . n 
B 1 143 ARG 143 143 143 ARG ARG B . n 
B 1 144 LEU 144 144 144 LEU LEU B . n 
B 1 145 ALA 145 145 145 ALA ALA B . n 
B 1 146 CYS 146 146 146 CYS CYS B . n 
B 1 147 GLY 147 147 147 GLY GLY B . n 
B 1 148 VAL 148 148 148 VAL VAL B . n 
B 1 149 ILE 149 149 149 ILE ILE B . n 
B 1 150 GLY 150 150 150 GLY GLY B . n 
B 1 151 ILE 151 151 151 ILE ILE B . n 
B 1 152 ALA 152 152 152 ALA ALA B . n 
B 1 153 GLN 153 153 153 GLN GLN B . n 
C 1 1   ALA 1   1   1   ALA ALA C . n 
C 1 2   THR 2   2   2   THR THR C . n 
C 1 3   LYS 3   3   3   LYS LYS C . n 
C 1 4   ALA 4   4   4   ALA ALA C . n 
C 1 5   VAL 5   5   5   VAL VAL C . n 
C 1 6   CYS 6   6   6   CYS CYS C . n 
C 1 7   VAL 7   7   7   VAL VAL C . n 
C 1 8   LEU 8   8   8   LEU LEU C . n 
C 1 9   LYS 9   9   9   LYS LYS C . n 
C 1 10  GLY 10  10  10  GLY GLY C . n 
C 1 11  ASP 11  11  11  ASP ASP C . n 
C 1 12  GLY 12  12  12  GLY GLY C . n 
C 1 13  PRO 13  13  13  PRO PRO C . n 
C 1 14  VAL 14  14  14  VAL VAL C . n 
C 1 15  GLN 15  15  15  GLN GLN C . n 
C 1 16  GLY 16  16  16  GLY GLY C . n 
C 1 17  ILE 17  17  17  ILE ILE C . n 
C 1 18  ILE 18  18  18  ILE ILE C . n 
C 1 19  ASN 19  19  19  ASN ASN C . n 
C 1 20  PHE 20  20  20  PHE PHE C . n 
C 1 21  GLU 21  21  21  GLU GLU C . n 
C 1 22  GLN 22  22  22  GLN GLN C . n 
C 1 23  LYS 23  23  23  LYS LYS C . n 
C 1 24  GLU 24  24  24  GLU GLU C . n 
C 1 25  SER 25  25  25  SER SER C . n 
C 1 26  ASN 26  26  26  ASN ASN C . n 
C 1 27  GLY 27  27  27  GLY GLY C . n 
C 1 28  PRO 28  28  28  PRO PRO C . n 
C 1 29  VAL 29  29  29  VAL VAL C . n 
C 1 30  LYS 30  30  30  LYS LYS C . n 
C 1 31  VAL 31  31  31  VAL VAL C . n 
C 1 32  TRP 32  32  32  TRP TRP C . n 
C 1 33  GLY 33  33  33  GLY GLY C . n 
C 1 34  SER 34  34  34  SER SER C . n 
C 1 35  ILE 35  35  35  ILE ILE C . n 
C 1 36  LYS 36  36  36  LYS LYS C . n 
C 1 37  GLY 37  37  37  GLY GLY C . n 
C 1 38  LEU 38  38  38  LEU LEU C . n 
C 1 39  THR 39  39  39  THR THR C . n 
C 1 40  GLU 40  40  40  GLU GLU C . n 
C 1 41  GLY 41  41  41  GLY GLY C . n 
C 1 42  LEU 42  42  42  LEU LEU C . n 
C 1 43  HIS 43  43  43  HIS HIS C . n 
C 1 44  GLY 44  44  44  GLY GLY C . n 
C 1 45  PHE 45  45  45  PHE PHE C . n 
C 1 46  HIS 46  46  46  HIS HIS C . n 
C 1 47  VAL 47  47  47  VAL VAL C . n 
C 1 48  HIS 48  48  48  HIS HIS C . n 
C 1 49  GLU 49  49  49  GLU GLU C . n 
C 1 50  PHE 50  50  50  PHE PHE C . n 
C 1 51  GLY 51  51  51  GLY GLY C . n 
C 1 52  ASP 52  52  52  ASP ASP C . n 
C 1 53  ASN 53  53  53  ASN ASN C . n 
C 1 54  ARG 54  54  54  ARG ARG C . n 
C 1 55  ALA 55  55  55  ALA ALA C . n 
C 1 56  GLY 56  56  56  GLY GLY C . n 
C 1 57  CYS 57  57  57  CYS CYS C . n 
C 1 58  THR 58  58  58  THR THR C . n 
C 1 59  SER 59  59  59  SER SER C . n 
C 1 60  ALA 60  60  60  ALA ALA C . n 
C 1 61  GLY 61  61  61  GLY GLY C . n 
C 1 62  PRO 62  62  62  PRO PRO C . n 
C 1 63  HIS 63  63  63  HIS HIS C . n 
C 1 64  PHE 64  64  64  PHE PHE C . n 
C 1 65  ASN 65  65  65  ASN ASN C . n 
C 1 66  PRO 66  66  66  PRO PRO C . n 
C 1 67  LEU 67  67  67  LEU LEU C . n 
C 1 68  SER 68  68  ?   ?   ?   C . n 
C 1 69  ARG 69  69  ?   ?   ?   C . n 
C 1 70  LYS 70  70  ?   ?   ?   C . n 
C 1 71  HIS 71  71  ?   ?   ?   C . n 
C 1 72  GLY 72  72  ?   ?   ?   C . n 
C 1 73  GLY 73  73  ?   ?   ?   C . n 
C 1 74  PRO 74  74  ?   ?   ?   C . n 
C 1 75  LYS 75  75  ?   ?   ?   C . n 
C 1 76  ASP 76  76  ?   ?   ?   C . n 
C 1 77  GLU 77  77  ?   ?   ?   C . n 
C 1 78  GLU 78  78  ?   ?   ?   C . n 
C 1 79  ARG 79  79  ?   ?   ?   C . n 
C 1 80  HIS 80  80  80  HIS HIS C . n 
C 1 81  VAL 81  81  81  VAL VAL C . n 
C 1 82  GLY 82  82  82  GLY GLY C . n 
C 1 83  ASP 83  83  83  ASP ASP C . n 
C 1 84  LEU 84  84  84  LEU LEU C . n 
C 1 85  GLY 85  85  85  GLY GLY C . n 
C 1 86  ASN 86  86  86  ASN ASN C . n 
C 1 87  VAL 87  87  87  VAL VAL C . n 
C 1 88  THR 88  88  88  THR THR C . n 
C 1 89  ALA 89  89  89  ALA ALA C . n 
C 1 90  ASP 90  90  90  ASP ASP C . n 
C 1 91  LYS 91  91  91  LYS LYS C . n 
C 1 92  ASP 92  92  92  ASP ASP C . n 
C 1 93  GLY 93  93  93  GLY GLY C . n 
C 1 94  VAL 94  94  94  VAL VAL C . n 
C 1 95  ALA 95  95  95  ALA ALA C . n 
C 1 96  ASP 96  96  96  ASP ASP C . n 
C 1 97  VAL 97  97  97  VAL VAL C . n 
C 1 98  SER 98  98  98  SER SER C . n 
C 1 99  ILE 99  99  99  ILE ILE C . n 
C 1 100 GLU 100 100 100 GLU GLU C . n 
C 1 101 ASP 101 101 101 ASP ASP C . n 
C 1 102 SER 102 102 102 SER SER C . n 
C 1 103 VAL 103 103 103 VAL VAL C . n 
C 1 104 ILE 104 104 104 ILE ILE C . n 
C 1 105 SER 105 105 105 SER SER C . n 
C 1 106 LEU 106 106 106 LEU LEU C . n 
C 1 107 SER 107 107 107 SER SER C . n 
C 1 108 GLY 108 108 108 GLY GLY C . n 
C 1 109 ASP 109 109 109 ASP ASP C . n 
C 1 110 HIS 110 110 110 HIS HIS C . n 
C 1 111 CYS 111 111 111 CYS CYS C . n 
C 1 112 ILE 112 112 112 ILE ILE C . n 
C 1 113 ILE 113 113 113 ILE ILE C . n 
C 1 114 GLY 114 114 114 GLY GLY C . n 
C 1 115 ARG 115 115 115 ARG ARG C . n 
C 1 116 THR 116 116 116 THR THR C . n 
C 1 117 LEU 117 117 117 LEU LEU C . n 
C 1 118 VAL 118 118 118 VAL VAL C . n 
C 1 119 VAL 119 119 119 VAL VAL C . n 
C 1 120 HIS 120 120 120 HIS HIS C . n 
C 1 121 GLU 121 121 121 GLU GLU C . n 
C 1 122 LYS 122 122 122 LYS LYS C . n 
C 1 123 ALA 123 123 123 ALA ALA C . n 
C 1 124 ASP 124 124 124 ASP ASP C . n 
C 1 125 ASP 125 125 ?   ?   ?   C . n 
C 1 126 LEU 126 126 ?   ?   ?   C . n 
C 1 127 GLY 127 127 ?   ?   ?   C . n 
C 1 128 LYS 128 128 ?   ?   ?   C . n 
C 1 129 GLY 129 129 ?   ?   ?   C . n 
C 1 130 GLY 130 130 ?   ?   ?   C . n 
C 1 131 ASN 131 131 ?   ?   ?   C . n 
C 1 132 GLU 132 132 ?   ?   ?   C . n 
C 1 133 GLU 133 133 ?   ?   ?   C . n 
C 1 134 SER 134 134 ?   ?   ?   C . n 
C 1 135 THR 135 135 ?   ?   ?   C . n 
C 1 136 LYS 136 136 ?   ?   ?   C . n 
C 1 137 THR 137 137 ?   ?   ?   C . n 
C 1 138 GLY 138 138 ?   ?   ?   C . n 
C 1 139 ASN 139 139 ?   ?   ?   C . n 
C 1 140 ALA 140 140 ?   ?   ?   C . n 
C 1 141 GLY 141 141 ?   ?   ?   C . n 
C 1 142 SER 142 142 142 SER SER C . n 
C 1 143 ARG 143 143 143 ARG ARG C . n 
C 1 144 LEU 144 144 144 LEU LEU C . n 
C 1 145 ALA 145 145 145 ALA ALA C . n 
C 1 146 CYS 146 146 146 CYS CYS C . n 
C 1 147 GLY 147 147 147 GLY GLY C . n 
C 1 148 VAL 148 148 148 VAL VAL C . n 
C 1 149 ILE 149 149 149 ILE ILE C . n 
C 1 150 GLY 150 150 150 GLY GLY C . n 
C 1 151 ILE 151 151 151 ILE ILE C . n 
C 1 152 ALA 152 152 152 ALA ALA C . n 
C 1 153 GLN 153 153 153 GLN GLN C . n 
D 1 1   ALA 1   1   1   ALA ALA D . n 
D 1 2   THR 2   2   2   THR THR D . n 
D 1 3   LYS 3   3   3   LYS LYS D . n 
D 1 4   ALA 4   4   4   ALA ALA D . n 
D 1 5   VAL 5   5   5   VAL VAL D . n 
D 1 6   CYS 6   6   6   CYS CYS D . n 
D 1 7   VAL 7   7   7   VAL VAL D . n 
D 1 8   LEU 8   8   8   LEU LEU D . n 
D 1 9   LYS 9   9   9   LYS LYS D . n 
D 1 10  GLY 10  10  10  GLY GLY D . n 
D 1 11  ASP 11  11  11  ASP ASP D . n 
D 1 12  GLY 12  12  12  GLY GLY D . n 
D 1 13  PRO 13  13  13  PRO PRO D . n 
D 1 14  VAL 14  14  14  VAL VAL D . n 
D 1 15  GLN 15  15  15  GLN GLN D . n 
D 1 16  GLY 16  16  16  GLY GLY D . n 
D 1 17  ILE 17  17  17  ILE ILE D . n 
D 1 18  ILE 18  18  18  ILE ILE D . n 
D 1 19  ASN 19  19  19  ASN ASN D . n 
D 1 20  PHE 20  20  20  PHE PHE D . n 
D 1 21  GLU 21  21  21  GLU GLU D . n 
D 1 22  GLN 22  22  22  GLN GLN D . n 
D 1 23  LYS 23  23  23  LYS LYS D . n 
D 1 24  GLU 24  24  24  GLU GLU D . n 
D 1 25  SER 25  25  25  SER SER D . n 
D 1 26  ASN 26  26  26  ASN ASN D . n 
D 1 27  GLY 27  27  27  GLY GLY D . n 
D 1 28  PRO 28  28  28  PRO PRO D . n 
D 1 29  VAL 29  29  29  VAL VAL D . n 
D 1 30  LYS 30  30  30  LYS LYS D . n 
D 1 31  VAL 31  31  31  VAL VAL D . n 
D 1 32  TRP 32  32  32  TRP TRP D . n 
D 1 33  GLY 33  33  33  GLY GLY D . n 
D 1 34  SER 34  34  34  SER SER D . n 
D 1 35  ILE 35  35  35  ILE ILE D . n 
D 1 36  LYS 36  36  36  LYS LYS D . n 
D 1 37  GLY 37  37  37  GLY GLY D . n 
D 1 38  LEU 38  38  38  LEU LEU D . n 
D 1 39  THR 39  39  39  THR THR D . n 
D 1 40  GLU 40  40  40  GLU GLU D . n 
D 1 41  GLY 41  41  41  GLY GLY D . n 
D 1 42  LEU 42  42  42  LEU LEU D . n 
D 1 43  HIS 43  43  43  HIS HIS D . n 
D 1 44  GLY 44  44  44  GLY GLY D . n 
D 1 45  PHE 45  45  45  PHE PHE D . n 
D 1 46  HIS 46  46  46  HIS HIS D . n 
D 1 47  VAL 47  47  47  VAL VAL D . n 
D 1 48  HIS 48  48  48  HIS HIS D . n 
D 1 49  GLU 49  49  49  GLU GLU D . n 
D 1 50  PHE 50  50  50  PHE PHE D . n 
D 1 51  GLY 51  51  51  GLY GLY D . n 
D 1 52  ASP 52  52  52  ASP ASP D . n 
D 1 53  ASN 53  53  53  ASN ASN D . n 
D 1 54  ARG 54  54  54  ARG ARG D . n 
D 1 55  ALA 55  55  55  ALA ALA D . n 
D 1 56  GLY 56  56  56  GLY GLY D . n 
D 1 57  CYS 57  57  57  CYS CYS D . n 
D 1 58  THR 58  58  58  THR THR D . n 
D 1 59  SER 59  59  59  SER SER D . n 
D 1 60  ALA 60  60  60  ALA ALA D . n 
D 1 61  GLY 61  61  61  GLY GLY D . n 
D 1 62  PRO 62  62  62  PRO PRO D . n 
D 1 63  HIS 63  63  63  HIS HIS D . n 
D 1 64  PHE 64  64  64  PHE PHE D . n 
D 1 65  ASN 65  65  65  ASN ASN D . n 
D 1 66  PRO 66  66  66  PRO PRO D . n 
D 1 67  LEU 67  67  ?   ?   ?   D . n 
D 1 68  SER 68  68  ?   ?   ?   D . n 
D 1 69  ARG 69  69  ?   ?   ?   D . n 
D 1 70  LYS 70  70  ?   ?   ?   D . n 
D 1 71  HIS 71  71  ?   ?   ?   D . n 
D 1 72  GLY 72  72  ?   ?   ?   D . n 
D 1 73  GLY 73  73  ?   ?   ?   D . n 
D 1 74  PRO 74  74  ?   ?   ?   D . n 
D 1 75  LYS 75  75  ?   ?   ?   D . n 
D 1 76  ASP 76  76  ?   ?   ?   D . n 
D 1 77  GLU 77  77  ?   ?   ?   D . n 
D 1 78  GLU 78  78  ?   ?   ?   D . n 
D 1 79  ARG 79  79  ?   ?   ?   D . n 
D 1 80  HIS 80  80  80  HIS HIS D . n 
D 1 81  VAL 81  81  81  VAL VAL D . n 
D 1 82  GLY 82  82  82  GLY GLY D . n 
D 1 83  ASP 83  83  83  ASP ASP D . n 
D 1 84  LEU 84  84  84  LEU LEU D . n 
D 1 85  GLY 85  85  85  GLY GLY D . n 
D 1 86  ASN 86  86  86  ASN ASN D . n 
D 1 87  VAL 87  87  87  VAL VAL D . n 
D 1 88  THR 88  88  88  THR THR D . n 
D 1 89  ALA 89  89  89  ALA ALA D . n 
D 1 90  ASP 90  90  90  ASP ASP D . n 
D 1 91  LYS 91  91  91  LYS LYS D . n 
D 1 92  ASP 92  92  92  ASP ASP D . n 
D 1 93  GLY 93  93  93  GLY GLY D . n 
D 1 94  VAL 94  94  94  VAL VAL D . n 
D 1 95  ALA 95  95  95  ALA ALA D . n 
D 1 96  ASP 96  96  96  ASP ASP D . n 
D 1 97  VAL 97  97  97  VAL VAL D . n 
D 1 98  SER 98  98  98  SER SER D . n 
D 1 99  ILE 99  99  99  ILE ILE D . n 
D 1 100 GLU 100 100 100 GLU GLU D . n 
D 1 101 ASP 101 101 101 ASP ASP D . n 
D 1 102 SER 102 102 102 SER SER D . n 
D 1 103 VAL 103 103 103 VAL VAL D . n 
D 1 104 ILE 104 104 104 ILE ILE D . n 
D 1 105 SER 105 105 105 SER SER D . n 
D 1 106 LEU 106 106 106 LEU LEU D . n 
D 1 107 SER 107 107 107 SER SER D . n 
D 1 108 GLY 108 108 108 GLY GLY D . n 
D 1 109 ASP 109 109 109 ASP ASP D . n 
D 1 110 HIS 110 110 110 HIS HIS D . n 
D 1 111 CYS 111 111 111 CYS CYS D . n 
D 1 112 ILE 112 112 112 ILE ILE D . n 
D 1 113 ILE 113 113 113 ILE ILE D . n 
D 1 114 GLY 114 114 114 GLY GLY D . n 
D 1 115 ARG 115 115 115 ARG ARG D . n 
D 1 116 THR 116 116 116 THR THR D . n 
D 1 117 LEU 117 117 117 LEU LEU D . n 
D 1 118 VAL 118 118 118 VAL VAL D . n 
D 1 119 VAL 119 119 119 VAL VAL D . n 
D 1 120 HIS 120 120 120 HIS HIS D . n 
D 1 121 GLU 121 121 121 GLU GLU D . n 
D 1 122 LYS 122 122 122 LYS LYS D . n 
D 1 123 ALA 123 123 123 ALA ALA D . n 
D 1 124 ASP 124 124 124 ASP ASP D . n 
D 1 125 ASP 125 125 ?   ?   ?   D . n 
D 1 126 LEU 126 126 ?   ?   ?   D . n 
D 1 127 GLY 127 127 ?   ?   ?   D . n 
D 1 128 LYS 128 128 ?   ?   ?   D . n 
D 1 129 GLY 129 129 ?   ?   ?   D . n 
D 1 130 GLY 130 130 ?   ?   ?   D . n 
D 1 131 ASN 131 131 ?   ?   ?   D . n 
D 1 132 GLU 132 132 ?   ?   ?   D . n 
D 1 133 GLU 133 133 ?   ?   ?   D . n 
D 1 134 SER 134 134 ?   ?   ?   D . n 
D 1 135 THR 135 135 ?   ?   ?   D . n 
D 1 136 LYS 136 136 ?   ?   ?   D . n 
D 1 137 THR 137 137 ?   ?   ?   D . n 
D 1 138 GLY 138 138 ?   ?   ?   D . n 
D 1 139 ASN 139 139 ?   ?   ?   D . n 
D 1 140 ALA 140 140 ?   ?   ?   D . n 
D 1 141 GLY 141 141 ?   ?   ?   D . n 
D 1 142 SER 142 142 142 SER SER D . n 
D 1 143 ARG 143 143 143 ARG ARG D . n 
D 1 144 LEU 144 144 144 LEU LEU D . n 
D 1 145 ALA 145 145 145 ALA ALA D . n 
D 1 146 CYS 146 146 146 CYS CYS D . n 
D 1 147 GLY 147 147 147 GLY GLY D . n 
D 1 148 VAL 148 148 148 VAL VAL D . n 
D 1 149 ILE 149 149 149 ILE ILE D . n 
D 1 150 GLY 150 150 150 GLY GLY D . n 
D 1 151 ILE 151 151 151 ILE ILE D . n 
D 1 152 ALA 152 152 152 ALA ALA D . n 
D 1 153 GLN 153 153 153 GLN GLN D . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 2 HOH 1   154 154 HOH HOH A . 
E 2 HOH 2   155 155 HOH HOH A . 
E 2 HOH 3   156 156 HOH HOH A . 
E 2 HOH 4   157 157 HOH HOH A . 
E 2 HOH 5   158 158 HOH HOH A . 
E 2 HOH 6   159 159 HOH HOH A . 
E 2 HOH 7   160 160 HOH HOH A . 
E 2 HOH 8   161 161 HOH HOH A . 
E 2 HOH 9   163 163 HOH HOH A . 
E 2 HOH 10  164 164 HOH HOH A . 
E 2 HOH 11  165 165 HOH HOH A . 
E 2 HOH 12  166 166 HOH HOH A . 
E 2 HOH 13  167 167 HOH HOH A . 
E 2 HOH 14  168 168 HOH HOH A . 
E 2 HOH 15  169 169 HOH HOH A . 
E 2 HOH 16  170 170 HOH HOH A . 
E 2 HOH 17  171 171 HOH HOH A . 
E 2 HOH 18  172 172 HOH HOH A . 
E 2 HOH 19  173 173 HOH HOH A . 
E 2 HOH 20  174 174 HOH HOH A . 
E 2 HOH 21  175 175 HOH HOH A . 
E 2 HOH 22  176 176 HOH HOH A . 
E 2 HOH 23  177 177 HOH HOH A . 
E 2 HOH 24  178 178 HOH HOH A . 
E 2 HOH 25  179 179 HOH HOH A . 
E 2 HOH 26  180 180 HOH HOH A . 
E 2 HOH 27  181 181 HOH HOH A . 
E 2 HOH 28  182 182 HOH HOH A . 
E 2 HOH 29  184 184 HOH HOH A . 
E 2 HOH 30  185 185 HOH HOH A . 
E 2 HOH 31  186 186 HOH HOH A . 
E 2 HOH 32  187 187 HOH HOH A . 
E 2 HOH 33  188 188 HOH HOH A . 
E 2 HOH 34  189 189 HOH HOH A . 
E 2 HOH 35  190 190 HOH HOH A . 
E 2 HOH 36  191 191 HOH HOH A . 
E 2 HOH 37  192 192 HOH HOH A . 
E 2 HOH 38  193 193 HOH HOH A . 
E 2 HOH 39  194 194 HOH HOH A . 
E 2 HOH 40  195 195 HOH HOH A . 
E 2 HOH 41  196 196 HOH HOH A . 
E 2 HOH 42  197 197 HOH HOH A . 
E 2 HOH 43  198 198 HOH HOH A . 
E 2 HOH 44  199 199 HOH HOH A . 
E 2 HOH 45  200 200 HOH HOH A . 
E 2 HOH 46  201 201 HOH HOH A . 
E 2 HOH 47  202 202 HOH HOH A . 
E 2 HOH 48  203 203 HOH HOH A . 
E 2 HOH 49  204 204 HOH HOH A . 
E 2 HOH 50  205 205 HOH HOH A . 
E 2 HOH 51  206 206 HOH HOH A . 
E 2 HOH 52  207 207 HOH HOH A . 
E 2 HOH 53  208 208 HOH HOH A . 
E 2 HOH 54  209 209 HOH HOH A . 
E 2 HOH 55  210 210 HOH HOH A . 
E 2 HOH 56  211 211 HOH HOH A . 
E 2 HOH 57  212 212 HOH HOH A . 
E 2 HOH 58  221 221 HOH HOH A . 
E 2 HOH 59  224 224 HOH HOH A . 
E 2 HOH 60  225 225 HOH HOH A . 
E 2 HOH 61  226 226 HOH HOH A . 
E 2 HOH 62  231 231 HOH HOH A . 
E 2 HOH 63  233 233 HOH HOH A . 
E 2 HOH 64  234 234 HOH HOH A . 
E 2 HOH 65  235 235 HOH HOH A . 
E 2 HOH 66  236 236 HOH HOH A . 
E 2 HOH 67  239 239 HOH HOH A . 
E 2 HOH 68  241 241 HOH HOH A . 
E 2 HOH 69  242 242 HOH HOH A . 
E 2 HOH 70  244 244 HOH HOH A . 
E 2 HOH 71  248 248 HOH HOH A . 
E 2 HOH 72  251 251 HOH HOH A . 
E 2 HOH 73  253 253 HOH HOH A . 
E 2 HOH 74  254 254 HOH HOH A . 
E 2 HOH 75  255 255 HOH HOH A . 
E 2 HOH 76  256 256 HOH HOH A . 
E 2 HOH 77  258 258 HOH HOH A . 
E 2 HOH 78  259 259 HOH HOH A . 
E 2 HOH 79  262 262 HOH HOH A . 
E 2 HOH 80  263 263 HOH HOH A . 
E 2 HOH 81  264 264 HOH HOH A . 
E 2 HOH 82  267 267 HOH HOH A . 
E 2 HOH 83  269 269 HOH HOH A . 
E 2 HOH 84  274 274 HOH HOH A . 
E 2 HOH 85  275 275 HOH HOH A . 
E 2 HOH 86  287 287 HOH HOH A . 
E 2 HOH 87  299 299 HOH HOH A . 
E 2 HOH 88  310 310 HOH HOH A . 
E 2 HOH 89  314 314 HOH HOH A . 
E 2 HOH 90  317 317 HOH HOH A . 
E 2 HOH 91  320 320 HOH HOH A . 
E 2 HOH 92  322 322 HOH HOH A . 
E 2 HOH 93  325 325 HOH HOH A . 
E 2 HOH 94  337 337 HOH HOH A . 
E 2 HOH 95  348 348 HOH HOH A . 
E 2 HOH 96  361 361 HOH HOH A . 
E 2 HOH 97  369 369 HOH HOH A . 
E 2 HOH 98  375 375 HOH HOH A . 
E 2 HOH 99  386 386 HOH HOH A . 
E 2 HOH 100 388 388 HOH HOH A . 
E 2 HOH 101 394 394 HOH HOH A . 
E 2 HOH 102 395 395 HOH HOH A . 
E 2 HOH 103 400 400 HOH HOH A . 
E 2 HOH 104 406 406 HOH HOH A . 
E 2 HOH 105 420 420 HOH HOH A . 
F 2 HOH 1   154 154 HOH HOH B . 
F 2 HOH 2   155 155 HOH HOH B . 
F 2 HOH 3   156 156 HOH HOH B . 
F 2 HOH 4   157 157 HOH HOH B . 
F 2 HOH 5   158 158 HOH HOH B . 
F 2 HOH 6   159 159 HOH HOH B . 
F 2 HOH 7   160 160 HOH HOH B . 
F 2 HOH 8   161 161 HOH HOH B . 
F 2 HOH 9   162 162 HOH HOH B . 
F 2 HOH 10  163 163 HOH HOH B . 
F 2 HOH 11  164 164 HOH HOH B . 
F 2 HOH 12  165 165 HOH HOH B . 
F 2 HOH 13  166 166 HOH HOH B . 
F 2 HOH 14  167 162 HOH HOH B . 
F 2 HOH 15  168 168 HOH HOH B . 
F 2 HOH 16  169 169 HOH HOH B . 
F 2 HOH 17  170 170 HOH HOH B . 
F 2 HOH 18  171 171 HOH HOH B . 
F 2 HOH 19  172 172 HOH HOH B . 
F 2 HOH 20  173 173 HOH HOH B . 
F 2 HOH 21  174 174 HOH HOH B . 
F 2 HOH 22  175 175 HOH HOH B . 
F 2 HOH 23  176 176 HOH HOH B . 
F 2 HOH 24  177 177 HOH HOH B . 
F 2 HOH 25  178 178 HOH HOH B . 
F 2 HOH 26  179 179 HOH HOH B . 
F 2 HOH 27  180 180 HOH HOH B . 
F 2 HOH 28  181 181 HOH HOH B . 
F 2 HOH 29  182 182 HOH HOH B . 
F 2 HOH 30  183 183 HOH HOH B . 
F 2 HOH 31  184 184 HOH HOH B . 
F 2 HOH 32  185 185 HOH HOH B . 
F 2 HOH 33  186 186 HOH HOH B . 
F 2 HOH 34  187 187 HOH HOH B . 
F 2 HOH 35  188 188 HOH HOH B . 
F 2 HOH 36  189 189 HOH HOH B . 
F 2 HOH 37  190 190 HOH HOH B . 
F 2 HOH 38  191 191 HOH HOH B . 
F 2 HOH 39  192 192 HOH HOH B . 
F 2 HOH 40  193 193 HOH HOH B . 
F 2 HOH 41  194 194 HOH HOH B . 
F 2 HOH 42  195 195 HOH HOH B . 
F 2 HOH 43  196 196 HOH HOH B . 
F 2 HOH 44  197 197 HOH HOH B . 
F 2 HOH 45  198 198 HOH HOH B . 
F 2 HOH 46  199 199 HOH HOH B . 
F 2 HOH 47  201 201 HOH HOH B . 
F 2 HOH 48  202 202 HOH HOH B . 
F 2 HOH 49  203 203 HOH HOH B . 
F 2 HOH 50  204 204 HOH HOH B . 
F 2 HOH 51  205 205 HOH HOH B . 
F 2 HOH 52  206 206 HOH HOH B . 
F 2 HOH 53  207 207 HOH HOH B . 
F 2 HOH 54  208 208 HOH HOH B . 
F 2 HOH 55  209 209 HOH HOH B . 
F 2 HOH 56  210 210 HOH HOH B . 
F 2 HOH 57  211 211 HOH HOH B . 
F 2 HOH 58  212 212 HOH HOH B . 
F 2 HOH 59  213 213 HOH HOH B . 
F 2 HOH 60  215 215 HOH HOH B . 
F 2 HOH 61  216 216 HOH HOH B . 
F 2 HOH 62  217 217 HOH HOH B . 
F 2 HOH 63  218 218 HOH HOH B . 
F 2 HOH 64  219 219 HOH HOH B . 
F 2 HOH 65  220 220 HOH HOH B . 
F 2 HOH 66  221 221 HOH HOH B . 
F 2 HOH 67  222 222 HOH HOH B . 
F 2 HOH 68  223 223 HOH HOH B . 
F 2 HOH 69  229 229 HOH HOH B . 
F 2 HOH 70  230 230 HOH HOH B . 
F 2 HOH 71  237 237 HOH HOH B . 
F 2 HOH 72  247 247 HOH HOH B . 
F 2 HOH 73  252 252 HOH HOH B . 
F 2 HOH 74  257 257 HOH HOH B . 
F 2 HOH 75  261 261 HOH HOH B . 
F 2 HOH 76  268 268 HOH HOH B . 
F 2 HOH 77  277 277 HOH HOH B . 
F 2 HOH 78  278 278 HOH HOH B . 
F 2 HOH 79  286 286 HOH HOH B . 
F 2 HOH 80  288 288 HOH HOH B . 
F 2 HOH 81  290 290 HOH HOH B . 
F 2 HOH 82  291 291 HOH HOH B . 
F 2 HOH 83  292 292 HOH HOH B . 
F 2 HOH 84  294 294 HOH HOH B . 
F 2 HOH 85  295 295 HOH HOH B . 
F 2 HOH 86  296 296 HOH HOH B . 
F 2 HOH 87  301 301 HOH HOH B . 
F 2 HOH 88  304 304 HOH HOH B . 
F 2 HOH 89  305 305 HOH HOH B . 
F 2 HOH 90  306 306 HOH HOH B . 
F 2 HOH 91  307 307 HOH HOH B . 
F 2 HOH 92  308 308 HOH HOH B . 
F 2 HOH 93  313 313 HOH HOH B . 
F 2 HOH 94  315 315 HOH HOH B . 
F 2 HOH 95  318 318 HOH HOH B . 
F 2 HOH 96  319 319 HOH HOH B . 
F 2 HOH 97  321 321 HOH HOH B . 
F 2 HOH 98  323 323 HOH HOH B . 
F 2 HOH 99  327 327 HOH HOH B . 
F 2 HOH 100 331 331 HOH HOH B . 
F 2 HOH 101 333 333 HOH HOH B . 
F 2 HOH 102 335 335 HOH HOH B . 
F 2 HOH 103 339 339 HOH HOH B . 
F 2 HOH 104 343 343 HOH HOH B . 
F 2 HOH 105 345 345 HOH HOH B . 
F 2 HOH 106 347 347 HOH HOH B . 
F 2 HOH 107 370 370 HOH HOH B . 
F 2 HOH 108 383 383 HOH HOH B . 
F 2 HOH 109 391 391 HOH HOH B . 
F 2 HOH 110 393 393 HOH HOH B . 
F 2 HOH 111 398 398 HOH HOH B . 
F 2 HOH 112 401 401 HOH HOH B . 
F 2 HOH 113 411 411 HOH HOH B . 
F 2 HOH 114 415 415 HOH HOH B . 
F 2 HOH 115 425 425 HOH HOH B . 
G 2 HOH 1   154 154 HOH HOH C . 
G 2 HOH 2   155 155 HOH HOH C . 
G 2 HOH 3   156 156 HOH HOH C . 
G 2 HOH 4   157 157 HOH HOH C . 
G 2 HOH 5   158 158 HOH HOH C . 
G 2 HOH 6   159 159 HOH HOH C . 
G 2 HOH 7   160 160 HOH HOH C . 
G 2 HOH 8   161 161 HOH HOH C . 
G 2 HOH 9   162 162 HOH HOH C . 
G 2 HOH 10  163 163 HOH HOH C . 
G 2 HOH 11  164 164 HOH HOH C . 
G 2 HOH 12  165 165 HOH HOH C . 
G 2 HOH 13  166 166 HOH HOH C . 
G 2 HOH 14  167 167 HOH HOH C . 
G 2 HOH 15  168 168 HOH HOH C . 
G 2 HOH 16  169 169 HOH HOH C . 
G 2 HOH 17  170 170 HOH HOH C . 
G 2 HOH 18  171 171 HOH HOH C . 
G 2 HOH 19  172 172 HOH HOH C . 
G 2 HOH 20  173 173 HOH HOH C . 
G 2 HOH 21  174 174 HOH HOH C . 
G 2 HOH 22  175 175 HOH HOH C . 
G 2 HOH 23  176 176 HOH HOH C . 
G 2 HOH 24  177 177 HOH HOH C . 
G 2 HOH 25  178 178 HOH HOH C . 
G 2 HOH 26  179 179 HOH HOH C . 
G 2 HOH 27  180 180 HOH HOH C . 
G 2 HOH 28  181 181 HOH HOH C . 
G 2 HOH 29  182 182 HOH HOH C . 
G 2 HOH 30  183 183 HOH HOH C . 
G 2 HOH 31  184 184 HOH HOH C . 
G 2 HOH 32  191 191 HOH HOH C . 
G 2 HOH 33  196 196 HOH HOH C . 
G 2 HOH 34  200 200 HOH HOH C . 
G 2 HOH 35  201 201 HOH HOH C . 
G 2 HOH 36  202 202 HOH HOH C . 
G 2 HOH 37  203 203 HOH HOH C . 
G 2 HOH 38  204 204 HOH HOH C . 
G 2 HOH 39  208 208 HOH HOH C . 
G 2 HOH 40  215 215 HOH HOH C . 
G 2 HOH 41  216 216 HOH HOH C . 
G 2 HOH 42  218 218 HOH HOH C . 
G 2 HOH 43  219 219 HOH HOH C . 
G 2 HOH 44  223 223 HOH HOH C . 
G 2 HOH 45  228 228 HOH HOH C . 
G 2 HOH 46  232 232 HOH HOH C . 
G 2 HOH 47  238 238 HOH HOH C . 
G 2 HOH 48  245 245 HOH HOH C . 
G 2 HOH 49  246 246 HOH HOH C . 
G 2 HOH 50  249 249 HOH HOH C . 
G 2 HOH 51  250 250 HOH HOH C . 
G 2 HOH 52  270 270 HOH HOH C . 
G 2 HOH 53  271 271 HOH HOH C . 
G 2 HOH 54  273 273 HOH HOH C . 
G 2 HOH 55  282 282 HOH HOH C . 
G 2 HOH 56  284 284 HOH HOH C . 
G 2 HOH 57  293 293 HOH HOH C . 
G 2 HOH 58  298 298 HOH HOH C . 
G 2 HOH 59  300 300 HOH HOH C . 
G 2 HOH 60  302 302 HOH HOH C . 
G 2 HOH 61  311 311 HOH HOH C . 
G 2 HOH 62  329 329 HOH HOH C . 
G 2 HOH 63  334 334 HOH HOH C . 
G 2 HOH 64  338 338 HOH HOH C . 
G 2 HOH 65  344 344 HOH HOH C . 
G 2 HOH 66  349 349 HOH HOH C . 
G 2 HOH 67  359 359 HOH HOH C . 
G 2 HOH 68  365 365 HOH HOH C . 
G 2 HOH 69  366 366 HOH HOH C . 
G 2 HOH 70  376 376 HOH HOH C . 
G 2 HOH 71  384 384 HOH HOH C . 
G 2 HOH 72  389 389 HOH HOH C . 
G 2 HOH 73  390 390 HOH HOH C . 
G 2 HOH 74  392 392 HOH HOH C . 
G 2 HOH 75  399 399 HOH HOH C . 
G 2 HOH 76  419 419 HOH HOH C . 
G 2 HOH 77  426 426 HOH HOH C . 
H 2 HOH 1   154 154 HOH HOH D . 
H 2 HOH 2   155 155 HOH HOH D . 
H 2 HOH 3   156 156 HOH HOH D . 
H 2 HOH 4   157 157 HOH HOH D . 
H 2 HOH 5   158 158 HOH HOH D . 
H 2 HOH 6   159 159 HOH HOH D . 
H 2 HOH 7   160 160 HOH HOH D . 
H 2 HOH 8   162 162 HOH HOH D . 
H 2 HOH 9   163 163 HOH HOH D . 
H 2 HOH 10  164 164 HOH HOH D . 
H 2 HOH 11  165 165 HOH HOH D . 
H 2 HOH 12  166 166 HOH HOH D . 
H 2 HOH 13  167 167 HOH HOH D . 
H 2 HOH 14  168 168 HOH HOH D . 
H 2 HOH 15  169 169 HOH HOH D . 
H 2 HOH 16  170 170 HOH HOH D . 
H 2 HOH 17  171 171 HOH HOH D . 
H 2 HOH 18  172 172 HOH HOH D . 
H 2 HOH 19  173 173 HOH HOH D . 
H 2 HOH 20  174 174 HOH HOH D . 
H 2 HOH 21  175 175 HOH HOH D . 
H 2 HOH 22  176 176 HOH HOH D . 
H 2 HOH 23  177 177 HOH HOH D . 
H 2 HOH 24  178 178 HOH HOH D . 
H 2 HOH 25  179 179 HOH HOH D . 
H 2 HOH 26  180 180 HOH HOH D . 
H 2 HOH 27  181 181 HOH HOH D . 
H 2 HOH 28  182 182 HOH HOH D . 
H 2 HOH 29  183 183 HOH HOH D . 
H 2 HOH 30  187 187 HOH HOH D . 
H 2 HOH 31  188 188 HOH HOH D . 
H 2 HOH 32  189 189 HOH HOH D . 
H 2 HOH 33  199 199 HOH HOH D . 
H 2 HOH 34  205 205 HOH HOH D . 
H 2 HOH 35  207 207 HOH HOH D . 
H 2 HOH 36  211 211 HOH HOH D . 
H 2 HOH 37  213 213 HOH HOH D . 
H 2 HOH 38  214 214 HOH HOH D . 
H 2 HOH 39  217 217 HOH HOH D . 
H 2 HOH 40  227 227 HOH HOH D . 
H 2 HOH 41  240 240 HOH HOH D . 
H 2 HOH 42  265 265 HOH HOH D . 
H 2 HOH 43  266 266 HOH HOH D . 
H 2 HOH 44  272 272 HOH HOH D . 
H 2 HOH 45  279 279 HOH HOH D . 
H 2 HOH 46  283 283 HOH HOH D . 
H 2 HOH 47  285 285 HOH HOH D . 
H 2 HOH 48  289 289 HOH HOH D . 
H 2 HOH 49  303 303 HOH HOH D . 
H 2 HOH 50  309 309 HOH HOH D . 
H 2 HOH 51  328 328 HOH HOH D . 
H 2 HOH 52  342 342 HOH HOH D . 
H 2 HOH 53  346 346 HOH HOH D . 
H 2 HOH 54  352 352 HOH HOH D . 
H 2 HOH 55  355 355 HOH HOH D . 
H 2 HOH 56  356 356 HOH HOH D . 
H 2 HOH 57  357 357 HOH HOH D . 
H 2 HOH 58  358 358 HOH HOH D . 
H 2 HOH 59  373 373 HOH HOH D . 
H 2 HOH 60  374 374 HOH HOH D . 
H 2 HOH 61  378 378 HOH HOH D . 
H 2 HOH 62  381 381 HOH HOH D . 
H 2 HOH 63  396 396 HOH HOH D . 
H 2 HOH 64  402 402 HOH HOH D . 
H 2 HOH 65  410 410 HOH HOH D . 
H 2 HOH 66  416 416 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_defined_assembly ? dimeric 2 
2 author_defined_assembly ? 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 
# 
_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 2009-05-19 
2 'Structure model' 1 1 2011-07-13 
3 'Structure model' 1 2 2021-10-20 
# 
_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' 'Data collection'           
3 3 '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 3 'Structure model' database_2         
2 3 'Structure model' diffrn_source      
3 3 '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 3 'Structure model' '_database_2.pdbx_DOI'                 
2 3 'Structure model' '_database_2.pdbx_database_accession'  
3 3 'Structure model' '_diffrn_source.pdbx_synchrotron_site' 
4 3 'Structure model' '_struct_ref_seq_dif.details'          
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
MAR345dtb 'data collection' .        ? 1 
MOLREP    phasing           .        ? 2 
REFMAC    refinement        5.2.0019 ? 3 
MOSFLM    'data reduction'  .        ? 4 
SCALA     'data scaling'    .        ? 5 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   NH1 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   ARG 
_pdbx_validate_close_contact.auth_seq_id_1    69 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   GLU 
_pdbx_validate_close_contact.auth_seq_id_2    77 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.11 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CA A VAL 31 ? ? CB  A VAL 31 ? ? 1.695 1.543 0.152  0.021 N 
2 1 CB C VAL 5  ? ? CG2 C VAL 5  ? ? 1.652 1.524 0.128  0.021 N 
3 1 CB C CYS 6  ? ? SG  C CYS 6  ? ? 1.699 1.812 -0.113 0.016 N 
4 1 CB D VAL 7  ? ? CG1 D VAL 7  ? ? 1.662 1.524 0.138  0.021 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CB C THR 2   ? ? CA C THR 2   ? ? C   C THR 2   ? ? 130.33 111.60 18.73 2.70 N 
2 1 CA C LEU 8   ? ? CB C LEU 8   ? ? CG  C LEU 8   ? ? 130.34 115.30 15.04 2.30 N 
3 1 CA C LEU 42  ? ? CB C LEU 42  ? ? CG  C LEU 42  ? ? 135.07 115.30 19.77 2.30 N 
4 1 CB C ASP 52  ? ? CG C ASP 52  ? ? OD1 C ASP 52  ? ? 124.22 118.30 5.92  0.90 N 
5 1 CB C ASP 52  ? ? CG C ASP 52  ? ? OD2 C ASP 52  ? ? 112.80 118.30 -5.50 0.90 N 
6 1 NE C ARG 115 ? ? CZ C ARG 115 ? ? NH1 C ARG 115 ? ? 124.81 120.30 4.51  0.50 N 
7 1 NE C ARG 115 ? ? CZ C ARG 115 ? ? NH2 C ARG 115 ? ? 117.15 120.30 -3.15 0.50 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 LEU A 126 ? ? 73.03  32.13   
2  1 LYS A 136 ? ? -97.30 -60.65  
3  1 SER B 68  ? ? 33.02  36.27   
4  1 ASP B 90  ? ? -66.84 -169.09 
5  1 LEU B 126 ? ? 70.42  37.21   
6  1 GLU C 40  ? ? -29.80 130.95  
7  1 ASP C 83  ? ? -68.15 99.14   
8  1 ASP C 90  ? ? -68.87 -172.90 
9  1 ASP C 92  ? ? -55.97 0.83    
10 1 ASP D 90  ? ? -69.37 -172.14 
# 
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 LEU 67  ? D LEU 67  
31 1 Y 1 D SER 68  ? D SER 68  
32 1 Y 1 D ARG 69  ? D ARG 69  
33 1 Y 1 D LYS 70  ? D LYS 70  
34 1 Y 1 D HIS 71  ? D HIS 71  
35 1 Y 1 D GLY 72  ? D GLY 72  
36 1 Y 1 D GLY 73  ? D GLY 73  
37 1 Y 1 D PRO 74  ? D PRO 74  
38 1 Y 1 D LYS 75  ? D LYS 75  
39 1 Y 1 D ASP 76  ? D ASP 76  
40 1 Y 1 D GLU 77  ? D GLU 77  
41 1 Y 1 D GLU 78  ? D GLU 78  
42 1 Y 1 D ARG 79  ? D ARG 79  
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 
# 
