data_4MCM
# 
_entry.id   4MCM 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.281 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   4MCM         
RCSB  RCSB081742   
WWPDB D_1000081742 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.db_id          4MCN 
_pdbx_database_related.details        . 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        4MCM 
_pdbx_database_status.recvd_initial_deposition_date   2013-08-21 
_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.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Sea, K.'         1  
'Sohn, S.H.'      2  
'Durazo, A.'      3  
'Sheng, Y.'       4  
'Shaw, B.'        5  
'Cao, X.'         6  
'Taylor, A.B.'    7  
'Whitson, L.J.'   8  
'Holloway, S.P.'  9  
'Hart, P.J.'      10 
'Cabelli, D.E.'   11 
'Gralla, E.B.'    12 
'Valentine, J.S.' 13 
# 
_citation.id                        primary 
_citation.title                     'Insights into the role of the unusual disulfide bond in copper-zinc superoxide dismutase.' 
_citation.journal_abbrev            J.Biol.Chem. 
_citation.journal_volume            290 
_citation.page_first                2405 
_citation.page_last                 2418 
_citation.year                      2015 
_citation.journal_id_ASTM           JBCHA3 
_citation.country                   US 
_citation.journal_id_ISSN           0021-9258 
_citation.journal_id_CSD            0071 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   25433341 
_citation.pdbx_database_id_DOI      10.1074/jbc.M114.588798 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Sea, K.'         1  
primary 'Sohn, S.H.'      2  
primary 'Durazo, A.'      3  
primary 'Sheng, Y.'       4  
primary 'Shaw, B.F.'      5  
primary 'Cao, X.'         6  
primary 'Taylor, A.B.'    7  
primary 'Whitson, L.J.'   8  
primary 'Holloway, S.P.'  9  
primary 'Hart, P.J.'      10 
primary 'Cabelli, D.E.'   11 
primary 'Gralla, E.B.'    12 
primary 'Valentine, J.S.' 13 
# 
_cell.entry_id           4MCM 
_cell.length_a           74.530 
_cell.length_b           163.883 
_cell.length_c           174.140 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              48 
_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                         4MCM 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_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]' 15811.496 12   1.15.1.1 C57S 'UNP residues 2-154' ? 
2 non-polymer syn 'ZINC ION'                     65.409    24   ?        ?    ?                    ? 
3 non-polymer syn 'SULFATE ION'                  96.063    14   ?        ?    ?                    ? 
4 water       nat water                          18.015    1094 ?        ?    ?                    ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Superoxide dismutase 1, hSod1' 
# 
_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       
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGSTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGSTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_strand_id                 A,B,C,D,E,F,G,H,I,J,K,L 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   THR n 
1 3   LYS n 
1 4   ALA n 
1 5   VAL n 
1 6   CYS n 
1 7   VAL n 
1 8   LEU n 
1 9   LYS n 
1 10  GLY n 
1 11  ASP n 
1 12  GLY n 
1 13  PRO n 
1 14  VAL n 
1 15  GLN n 
1 16  GLY n 
1 17  ILE n 
1 18  ILE n 
1 19  ASN n 
1 20  PHE n 
1 21  GLU n 
1 22  GLN n 
1 23  LYS n 
1 24  GLU n 
1 25  SER n 
1 26  ASN n 
1 27  GLY n 
1 28  PRO n 
1 29  VAL n 
1 30  LYS n 
1 31  VAL n 
1 32  TRP n 
1 33  GLY n 
1 34  SER n 
1 35  ILE n 
1 36  LYS n 
1 37  GLY n 
1 38  LEU n 
1 39  THR n 
1 40  GLU n 
1 41  GLY n 
1 42  LEU n 
1 43  HIS n 
1 44  GLY n 
1 45  PHE n 
1 46  HIS n 
1 47  VAL n 
1 48  HIS n 
1 49  GLU n 
1 50  PHE n 
1 51  GLY n 
1 52  ASP n 
1 53  ASN n 
1 54  THR n 
1 55  ALA n 
1 56  GLY n 
1 57  SER 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      'SACCHAROMYCES CEREVISIAE' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     4932 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          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                       YEP351-HSOD 
_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 4MCM A 1 ? 153 ? P00441 2 ? 154 ? 1 153 
2  1 4MCM B 1 ? 153 ? P00441 2 ? 154 ? 1 153 
3  1 4MCM C 1 ? 153 ? P00441 2 ? 154 ? 1 153 
4  1 4MCM D 1 ? 153 ? P00441 2 ? 154 ? 1 153 
5  1 4MCM E 1 ? 153 ? P00441 2 ? 154 ? 1 153 
6  1 4MCM F 1 ? 153 ? P00441 2 ? 154 ? 1 153 
7  1 4MCM G 1 ? 153 ? P00441 2 ? 154 ? 1 153 
8  1 4MCM H 1 ? 153 ? P00441 2 ? 154 ? 1 153 
9  1 4MCM I 1 ? 153 ? P00441 2 ? 154 ? 1 153 
10 1 4MCM J 1 ? 153 ? P00441 2 ? 154 ? 1 153 
11 1 4MCM K 1 ? 153 ? P00441 2 ? 154 ? 1 153 
12 1 4MCM L 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  4MCM SER A 57 ? UNP P00441 CYS 58 'ENGINEERED MUTATION' 57 1  
2  4MCM SER B 57 ? UNP P00441 CYS 58 'ENGINEERED MUTATION' 57 2  
3  4MCM SER C 57 ? UNP P00441 CYS 58 'ENGINEERED MUTATION' 57 3  
4  4MCM SER D 57 ? UNP P00441 CYS 58 'ENGINEERED MUTATION' 57 4  
5  4MCM SER E 57 ? UNP P00441 CYS 58 'ENGINEERED MUTATION' 57 5  
6  4MCM SER F 57 ? UNP P00441 CYS 58 'ENGINEERED MUTATION' 57 6  
7  4MCM SER G 57 ? UNP P00441 CYS 58 'ENGINEERED MUTATION' 57 7  
8  4MCM SER H 57 ? UNP P00441 CYS 58 'ENGINEERED MUTATION' 57 8  
9  4MCM SER I 57 ? UNP P00441 CYS 58 'ENGINEERED MUTATION' 57 9  
10 4MCM SER J 57 ? UNP P00441 CYS 58 'ENGINEERED MUTATION' 57 10 
11 4MCM SER K 57 ? UNP P00441 CYS 58 'ENGINEERED MUTATION' 57 11 
12 4MCM SER L 57 ? UNP P00441 CYS 58 'ENGINEERED MUTATION' 57 12 
# 
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 
SO4 non-polymer         . 'SULFATE ION'   ? 'O4 S -2'        96.063  
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
ZN  non-polymer         . 'ZINC ION'      ? 'Zn 2'           65.409  
# 
_exptl.entry_id          4MCM 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.80 
_exptl_crystal.density_percent_sol   56.11 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.temp            295 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              5.5 
_exptl_crystal_grow.pdbx_details    
'0.2 M ammonium sulfate, 0.1 M bis-tris, 25% PEG 3350, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K' 
_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                   CUSTOM-MADE 
_diffrn_detector.pdbx_collection_date   2004-08-19 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0332 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'APS BEAMLINE 19-BM' 
_diffrn_source.pdbx_synchrotron_site       APS 
_diffrn_source.pdbx_synchrotron_beamline   19-BM 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        1.0332 
# 
_reflns.entry_id                     4MCM 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             30 
_reflns.d_resolution_high            2.2 
_reflns.number_obs                   108701 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.3 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              0.064 
_reflns.pdbx_netI_over_sigmaI        25.6 
_reflns.B_iso_Wilson_estimate        32.9 
_reflns.pdbx_redundancy              6.1 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_high             2.20 
_reflns_shell.d_res_low              2.28 
_reflns_shell.percent_possible_all   95.3 
_reflns_shell.Rmerge_I_obs           ? 
_reflns_shell.pdbx_Rsym_value        0.482 
_reflns_shell.meanI_over_sigI_obs    2.9 
_reflns_shell.pdbx_redundancy        4.4 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      10297 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.pdbx_diffrn_id         1 
# 
_refine.entry_id                                 4MCM 
_refine.ls_number_reflns_obs                     106830 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             29.836 
_refine.ls_d_res_high                            2.200 
_refine.ls_percent_reflns_obs                    98.18 
_refine.ls_R_factor_obs                          0.2130 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2105 
_refine.ls_R_factor_R_free                       0.2621 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.98 
_refine.ls_number_reflns_R_free                  5325 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               31.4 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             1.10 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  ? 
_refine.pdbx_starting_model                      'PDB entry 1AZV' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             isotropic 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            random 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.30 
_refine.pdbx_overall_phase_error                 28.28 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_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_diffrn_id                           1 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_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        13310 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         94 
_refine_hist.number_atoms_solvent             1094 
_refine_hist.number_atoms_total               14498 
_refine_hist.d_res_high                       2.200 
_refine_hist.d_res_low                        29.836 
# 
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_restraint_function 
_refine_ls_restr.pdbx_refine_id 
f_bond_d           0.008  ? ? 13588 ? 'X-RAY DIFFRACTION' 
f_angle_d          1.154  ? ? 18344 ? 'X-RAY DIFFRACTION' 
f_dihedral_angle_d 13.915 ? ? 4862  ? 'X-RAY DIFFRACTION' 
f_chiral_restr     0.074  ? ? 2015  ? 'X-RAY DIFFRACTION' 
f_plane_restr      0.004  ? ? 2472  ? 'X-RAY DIFFRACTION' 
# 
loop_
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_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 
. 2.2000 2.2250  2982 0.2807 88.00  0.3551 . . 157 . . . . 'X-RAY DIFFRACTION' 
. 2.2250 2.2512  3128 0.2703 91.00  0.3262 . . 151 . . . . 'X-RAY DIFFRACTION' 
. 2.2512 2.2786  3145 0.2673 93.00  0.3249 . . 157 . . . . 'X-RAY DIFFRACTION' 
. 2.2786 2.3074  3209 0.2594 94.00  0.3200 . . 171 . . . . 'X-RAY DIFFRACTION' 
. 2.3074 2.3378  3243 0.2542 96.00  0.3336 . . 195 . . . . 'X-RAY DIFFRACTION' 
. 2.3378 2.3698  3279 0.2523 96.00  0.3037 . . 144 . . . . 'X-RAY DIFFRACTION' 
. 2.3698 2.4036  3344 0.2506 97.00  0.2836 . . 165 . . . . 'X-RAY DIFFRACTION' 
. 2.4036 2.4395  3290 0.2531 97.00  0.3324 . . 159 . . . . 'X-RAY DIFFRACTION' 
. 2.4395 2.4776  3359 0.2552 98.00  0.2855 . . 192 . . . . 'X-RAY DIFFRACTION' 
. 2.4776 2.5182  3388 0.2560 99.00  0.2903 . . 170 . . . . 'X-RAY DIFFRACTION' 
. 2.5182 2.5616  3368 0.2554 99.00  0.3685 . . 207 . . . . 'X-RAY DIFFRACTION' 
. 2.5616 2.6082  3328 0.2403 99.00  0.2993 . . 210 . . . . 'X-RAY DIFFRACTION' 
. 2.6082 2.6583  3435 0.2488 100.00 0.3529 . . 171 . . . . 'X-RAY DIFFRACTION' 
. 2.6583 2.7125  3356 0.2446 99.00  0.3226 . . 184 . . . . 'X-RAY DIFFRACTION' 
. 2.7125 2.7715  3457 0.2372 100.00 0.2831 . . 180 . . . . 'X-RAY DIFFRACTION' 
. 2.7715 2.8359  3394 0.2373 100.00 0.2928 . . 186 . . . . 'X-RAY DIFFRACTION' 
. 2.8359 2.9067  3436 0.2471 100.00 0.3227 . . 173 . . . . 'X-RAY DIFFRACTION' 
. 2.9067 2.9853  3463 0.2343 100.00 0.2603 . . 176 . . . . 'X-RAY DIFFRACTION' 
. 2.9853 3.0730  3410 0.2358 100.00 0.3060 . . 176 . . . . 'X-RAY DIFFRACTION' 
. 3.0730 3.1721  3438 0.2226 100.00 0.2940 . . 178 . . . . 'X-RAY DIFFRACTION' 
. 3.1721 3.2853  3431 0.2119 100.00 0.2747 . . 208 . . . . 'X-RAY DIFFRACTION' 
. 3.2853 3.4167  3450 0.2105 100.00 0.2699 . . 184 . . . . 'X-RAY DIFFRACTION' 
. 3.4167 3.5720  3461 0.2089 100.00 0.2587 . . 206 . . . . 'X-RAY DIFFRACTION' 
. 3.5720 3.7599  3442 0.1931 100.00 0.2456 . . 163 . . . . 'X-RAY DIFFRACTION' 
. 3.7599 3.9950  3471 0.1888 100.00 0.2209 . . 186 . . . . 'X-RAY DIFFRACTION' 
. 3.9950 4.3026  3481 0.1683 100.00 0.2078 . . 174 . . . . 'X-RAY DIFFRACTION' 
. 4.3026 4.7341  3506 0.1611 100.00 0.2334 . . 180 . . . . 'X-RAY DIFFRACTION' 
. 4.7341 5.4156  3558 0.1642 100.00 0.2266 . . 153 . . . . 'X-RAY DIFFRACTION' 
. 5.4156 6.8096  3561 0.1901 100.00 0.1958 . . 180 . . . . 'X-RAY DIFFRACTION' 
. 6.8096 29.8388 3692 0.1918 99.00  0.1966 . . 189 . . . . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  4MCM 
_struct.title                     'Human SOD1 C57S Mutant, As-isolated' 
_struct.pdbx_descriptor           'Superoxide dismutase [Cu-Zn] (E.C.1.15.1.1)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4MCM 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
_struct_keywords.text            
'OXIDOREDUCTASE, HUMAN CU, ZN SUPEROXIDE DISMUTASE, ANTIOXIDANT, METAL-BINDING, AMYOTROPHIC LATERAL SCLEROSIS, DISULFIDE BOND' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1 ? 
B  N N 1 ? 
C  N N 1 ? 
D  N N 1 ? 
E  N N 1 ? 
F  N N 1 ? 
G  N N 1 ? 
H  N N 1 ? 
I  N N 1 ? 
J  N N 1 ? 
K  N N 1 ? 
L  N N 1 ? 
M  N N 2 ? 
N  N N 2 ? 
O  N N 3 ? 
P  N N 2 ? 
Q  N N 2 ? 
R  N N 3 ? 
S  N N 3 ? 
T  N N 2 ? 
U  N N 2 ? 
V  N N 3 ? 
W  N N 2 ? 
X  N N 2 ? 
Y  N N 3 ? 
Z  N N 2 ? 
AA N N 2 ? 
BA N N 3 ? 
CA N N 2 ? 
DA N N 2 ? 
EA N N 3 ? 
FA N N 2 ? 
GA N N 2 ? 
HA N N 3 ? 
IA N N 2 ? 
JA N N 2 ? 
KA N N 3 ? 
LA N N 3 ? 
MA N N 2 ? 
NA N N 2 ? 
OA N N 3 ? 
PA N N 2 ? 
QA N N 2 ? 
RA N N 3 ? 
SA N N 2 ? 
TA N N 2 ? 
UA N N 3 ? 
VA N N 2 ? 
WA N N 2 ? 
XA N N 3 ? 
YA N N 4 ? 
ZA N N 4 ? 
AB N N 4 ? 
BB N N 4 ? 
CB N N 4 ? 
DB N N 4 ? 
EB N N 4 ? 
FB N N 4 ? 
GB N N 4 ? 
HB N N 4 ? 
IB N N 4 ? 
JB N N 4 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  1  ALA A 55  ? GLY A 61  ? ALA A 55  GLY A 61  5 ? 7 
HELX_P HELX_P2  2  ALA B 55  ? GLY B 61  ? ALA B 55  GLY B 61  5 ? 7 
HELX_P HELX_P3  3  SER B 107 ? CYS B 111 ? SER B 107 CYS B 111 5 ? 5 
HELX_P HELX_P4  4  ALA C 55  ? GLY C 61  ? ALA C 55  GLY C 61  5 ? 7 
HELX_P HELX_P5  5  SER D 107 ? CYS D 111 ? SER D 107 CYS D 111 5 ? 5 
HELX_P HELX_P6  6  ALA E 55  ? GLY E 61  ? ALA E 55  GLY E 61  5 ? 7 
HELX_P HELX_P7  7  GLY F 56  ? GLY F 61  ? GLY F 56  GLY F 61  5 ? 6 
HELX_P HELX_P8  8  ALA G 55  ? GLY G 61  ? ALA G 55  GLY G 61  5 ? 7 
HELX_P HELX_P9  9  ALA H 55  ? GLY H 61  ? ALA H 55  GLY H 61  5 ? 7 
HELX_P HELX_P10 10 SER H 107 ? CYS H 111 ? SER H 107 CYS H 111 5 ? 5 
HELX_P HELX_P11 11 ALA I 55  ? GLY I 61  ? ALA I 55  GLY I 61  5 ? 7 
HELX_P HELX_P12 12 GLU I 132 ? LYS I 136 ? GLU I 132 LYS I 136 5 ? 5 
HELX_P HELX_P13 13 ALA J 55  ? GLY J 61  ? ALA J 55  GLY J 61  5 ? 7 
HELX_P HELX_P14 14 ASN J 131 ? LYS J 136 ? ASN J 131 LYS J 136 5 ? 6 
HELX_P HELX_P15 15 ALA K 55  ? GLY K 61  ? ALA K 55  GLY K 61  5 ? 7 
HELX_P HELX_P16 16 ALA L 55  ? ALA L 60  ? ALA L 55  ALA L 60  5 ? 6 
# 
_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 
metalc1  metalc ? ? B  ASP 83  OD1 ? ? ? 1_555 Q  ZN  . ZN ? ? B ASP 83  B ZN  202 1_555 ? ? ? ? ? ? ? 1.761 ? 
metalc2  metalc ? ? H  HIS 120 NE2 ? ? ? 1_555 IA ZN  . ZN ? ? H HIS 120 H ZN  201 1_555 ? ? ? ? ? ? ? 1.842 ? 
metalc3  metalc ? ? F  HIS 80  ND1 ? ? ? 1_555 DA ZN  . ZN ? ? F HIS 80  F ZN  202 1_555 ? ? ? ? ? ? ? 1.844 ? 
metalc4  metalc ? ? D  HIS 120 NE2 ? ? ? 1_555 W  ZN  . ZN ? ? D HIS 120 D ZN  201 1_555 ? ? ? ? ? ? ? 1.858 ? 
metalc5  metalc ? ? D  ASP 83  OD1 ? ? ? 1_555 X  ZN  . ZN ? ? D ASP 83  D ZN  202 1_555 ? ? ? ? ? ? ? 1.869 ? 
metalc6  metalc ? ? J  ASP 83  OD1 ? ? ? 1_555 QA ZN  . ZN ? ? J ASP 83  J ZN  202 1_555 ? ? ? ? ? ? ? 1.874 ? 
metalc7  metalc ? ? L  ASP 83  OD1 ? ? ? 1_555 WA ZN  . ZN ? ? L ASP 83  L ZN  202 1_555 ? ? ? ? ? ? ? 1.889 ? 
metalc8  metalc ? ? G  ASP 83  OD1 ? ? ? 1_555 GA ZN  . ZN ? ? G ASP 83  G ZN  202 1_555 ? ? ? ? ? ? ? 1.894 ? 
metalc9  metalc ? ? H  ASP 83  OD1 ? ? ? 1_555 JA ZN  . ZN ? ? H ASP 83  H ZN  202 1_555 ? ? ? ? ? ? ? 1.901 ? 
metalc10 metalc ? ? J  HIS 80  ND1 ? ? ? 1_555 QA ZN  . ZN ? ? J HIS 80  J ZN  202 1_555 ? ? ? ? ? ? ? 1.902 ? 
metalc11 metalc ? ? K  HIS 120 NE2 ? ? ? 1_555 SA ZN  . ZN ? ? K HIS 120 K ZN  201 1_555 ? ? ? ? ? ? ? 1.907 ? 
metalc12 metalc ? ? A  ASP 83  OD1 ? ? ? 1_555 N  ZN  . ZN ? ? A ASP 83  A ZN  202 1_555 ? ? ? ? ? ? ? 1.911 ? 
metalc13 metalc ? ? G  HIS 120 NE2 ? ? ? 1_555 FA ZN  . ZN ? ? G HIS 120 G ZN  201 1_555 ? ? ? ? ? ? ? 1.912 ? 
metalc14 metalc ? ? J  HIS 120 NE2 ? ? ? 1_555 PA ZN  . ZN ? ? J HIS 120 J ZN  201 1_555 ? ? ? ? ? ? ? 1.923 ? 
metalc15 metalc ? ? E  HIS 120 NE2 ? ? ? 1_555 Z  ZN  . ZN ? ? E HIS 120 E ZN  201 1_555 ? ? ? ? ? ? ? 1.928 ? 
metalc16 metalc ? ? K  ASP 83  OD1 ? ? ? 1_555 TA ZN  . ZN ? ? K ASP 83  K ZN  202 1_555 ? ? ? ? ? ? ? 1.932 ? 
metalc17 metalc ? ? I  ASP 83  OD1 ? ? ? 1_555 NA ZN  . ZN ? ? I ASP 83  I ZN  202 1_555 ? ? ? ? ? ? ? 1.941 ? 
metalc18 metalc ? ? F  HIS 71  ND1 ? ? ? 1_555 DA ZN  . ZN ? ? F HIS 71  F ZN  202 1_555 ? ? ? ? ? ? ? 1.960 ? 
metalc19 metalc ? ? B  HIS 120 NE2 ? ? ? 1_555 P  ZN  . ZN ? ? B HIS 120 B ZN  201 1_555 ? ? ? ? ? ? ? 1.966 ? 
metalc20 metalc ? ? L  HIS 80  ND1 ? ? ? 1_555 WA ZN  . ZN ? ? L HIS 80  L ZN  202 1_555 ? ? ? ? ? ? ? 1.971 ? 
metalc21 metalc ? ? F  HIS 120 NE2 ? ? ? 1_555 CA ZN  . ZN ? ? F HIS 120 F ZN  201 1_555 ? ? ? ? ? ? ? 1.978 ? 
metalc22 metalc ? ? L  HIS 63  ND1 ? ? ? 1_555 WA ZN  . ZN ? ? L HIS 63  L ZN  202 1_555 ? ? ? ? ? ? ? 1.982 ? 
metalc23 metalc ? ? I  HIS 80  ND1 ? ? ? 1_555 NA ZN  . ZN ? ? I HIS 80  I ZN  202 1_555 ? ? ? ? ? ? ? 1.991 ? 
metalc24 metalc ? ? F  HIS 48  NE2 ? ? ? 1_555 CA ZN  . ZN ? ? F HIS 48  F ZN  201 1_555 ? ? ? ? ? ? ? 1.992 ? 
metalc25 metalc ? ? J  HIS 63  ND1 ? ? ? 1_555 QA ZN  . ZN ? ? J HIS 63  J ZN  202 1_555 ? ? ? ? ? ? ? 1.996 ? 
metalc26 metalc ? ? T  ZN  .   ZN  ? ? ? 1_555 V  SO4 . O3 ? ? C ZN  201 C SO4 203 1_555 ? ? ? ? ? ? ? 2.007 ? 
metalc27 metalc ? ? A  HIS 80  ND1 ? ? ? 1_555 N  ZN  . ZN ? ? A HIS 80  A ZN  202 1_555 ? ? ? ? ? ? ? 2.007 ? 
metalc28 metalc ? ? B  HIS 63  ND1 ? ? ? 1_555 Q  ZN  . ZN ? ? B HIS 63  B ZN  202 1_555 ? ? ? ? ? ? ? 2.010 ? 
metalc29 metalc ? ? A  HIS 120 NE2 ? ? ? 1_555 M  ZN  . ZN ? ? A HIS 120 A ZN  201 1_555 ? ? ? ? ? ? ? 2.011 ? 
metalc30 metalc ? ? A  HIS 48  NE2 ? ? ? 1_555 M  ZN  . ZN ? ? A HIS 48  A ZN  201 1_555 ? ? ? ? ? ? ? 2.014 ? 
metalc31 metalc ? ? H  HIS 71  ND1 ? ? ? 1_555 JA ZN  . ZN ? ? H HIS 71  H ZN  202 1_555 ? ? ? ? ? ? ? 2.027 ? 
metalc32 metalc ? ? C  HIS 120 NE2 ? ? ? 1_555 T  ZN  . ZN ? ? C HIS 120 C ZN  201 1_555 ? ? ? ? ? ? ? 2.031 ? 
metalc33 metalc ? ? G  HIS 63  ND1 ? ? ? 1_555 GA ZN  . ZN ? ? G HIS 63  G ZN  202 1_555 ? ? ? ? ? ? ? 2.035 ? 
metalc34 metalc ? ? E  HIS 80  ND1 ? ? ? 1_555 AA ZN  . ZN ? ? E HIS 80  E ZN  202 1_555 ? ? ? ? ? ? ? 2.040 ? 
metalc35 metalc ? ? F  HIS 63  ND1 ? ? ? 1_555 DA ZN  . ZN ? ? F HIS 63  F ZN  202 1_555 ? ? ? ? ? ? ? 2.040 ? 
metalc36 metalc ? ? K  HIS 80  ND1 ? ? ? 1_555 TA ZN  . ZN ? ? K HIS 80  K ZN  202 1_555 ? ? ? ? ? ? ? 2.041 ? 
metalc37 metalc ? ? G  HIS 48  NE2 ? ? ? 1_555 FA ZN  . ZN ? ? G HIS 48  G ZN  201 1_555 ? ? ? ? ? ? ? 2.042 ? 
metalc38 metalc ? ? H  HIS 48  NE2 ? ? ? 1_555 IA ZN  . ZN ? ? H HIS 48  H ZN  201 1_555 ? ? ? ? ? ? ? 2.042 ? 
metalc39 metalc ? ? B  HIS 71  ND1 ? ? ? 1_555 Q  ZN  . ZN ? ? B HIS 71  B ZN  202 1_555 ? ? ? ? ? ? ? 2.048 ? 
metalc40 metalc ? ? J  HIS 71  ND1 ? ? ? 1_555 QA ZN  . ZN ? ? J HIS 71  J ZN  202 1_555 ? ? ? ? ? ? ? 2.048 ? 
metalc41 metalc ? ? G  HIS 80  ND1 ? ? ? 1_555 GA ZN  . ZN ? ? G HIS 80  G ZN  202 1_555 ? ? ? ? ? ? ? 2.049 ? 
metalc42 metalc ? ? G  HIS 71  ND1 ? ? ? 1_555 GA ZN  . ZN ? ? G HIS 71  G ZN  202 1_555 ? ? ? ? ? ? ? 2.056 ? 
metalc43 metalc ? ? B  HIS 80  ND1 ? ? ? 1_555 Q  ZN  . ZN ? ? B HIS 80  B ZN  202 1_555 ? ? ? ? ? ? ? 2.066 ? 
metalc44 metalc ? ? H  HIS 80  ND1 ? ? ? 1_555 JA ZN  . ZN ? ? H HIS 80  H ZN  202 1_555 ? ? ? ? ? ? ? 2.070 ? 
metalc45 metalc ? ? E  HIS 63  ND1 ? ? ? 1_555 AA ZN  . ZN ? ? E HIS 63  E ZN  202 1_555 ? ? ? ? ? ? ? 2.070 ? 
metalc46 metalc ? ? B  HIS 48  NE2 ? ? ? 1_555 P  ZN  . ZN ? ? B HIS 48  B ZN  201 1_555 ? ? ? ? ? ? ? 2.073 ? 
metalc47 metalc ? ? L  HIS 71  ND1 ? ? ? 1_555 WA ZN  . ZN ? ? L HIS 71  L ZN  202 1_555 ? ? ? ? ? ? ? 2.075 ? 
metalc48 metalc ? ? H  HIS 63  ND1 ? ? ? 1_555 JA ZN  . ZN ? ? H HIS 63  H ZN  202 1_555 ? ? ? ? ? ? ? 2.078 ? 
metalc49 metalc ? ? D  HIS 80  ND1 ? ? ? 1_555 X  ZN  . ZN ? ? D HIS 80  D ZN  202 1_555 ? ? ? ? ? ? ? 2.081 ? 
metalc50 metalc ? ? FA ZN  .   ZN  ? ? ? 1_555 HA SO4 . O1 ? ? G ZN  201 G SO4 203 1_555 ? ? ? ? ? ? ? 2.096 ? 
metalc51 metalc ? ? D  HIS 48  NE2 ? ? ? 1_555 W  ZN  . ZN ? ? D HIS 48  D ZN  201 1_555 ? ? ? ? ? ? ? 2.097 ? 
metalc52 metalc ? ? D  HIS 71  ND1 ? ? ? 1_555 X  ZN  . ZN ? ? D HIS 71  D ZN  202 1_555 ? ? ? ? ? ? ? 2.097 ? 
metalc53 metalc ? ? A  HIS 71  ND1 ? ? ? 1_555 N  ZN  . ZN ? ? A HIS 71  A ZN  202 1_555 ? ? ? ? ? ? ? 2.107 ? 
metalc54 metalc ? ? Z  ZN  .   ZN  ? ? ? 1_555 BA SO4 . O2 ? ? E ZN  201 E SO4 203 1_555 ? ? ? ? ? ? ? 2.118 ? 
metalc55 metalc ? ? E  ASP 83  OD1 ? ? ? 1_555 AA ZN  . ZN ? ? E ASP 83  E ZN  202 1_555 ? ? ? ? ? ? ? 2.121 ? 
metalc56 metalc ? ? L  HIS 120 NE2 ? ? ? 1_555 VA ZN  . ZN ? ? L HIS 120 L ZN  201 1_555 ? ? ? ? ? ? ? 2.139 ? 
metalc57 metalc ? ? A  HIS 63  ND1 ? ? ? 1_555 N  ZN  . ZN ? ? A HIS 63  A ZN  202 1_555 ? ? ? ? ? ? ? 2.140 ? 
metalc58 metalc ? ? C  ASP 83  OD1 ? ? ? 1_555 U  ZN  . ZN ? ? C ASP 83  C ZN  202 1_555 ? ? ? ? ? ? ? 2.146 ? 
metalc59 metalc ? ? F  ASP 83  OD1 ? ? ? 1_555 DA ZN  . ZN ? ? F ASP 83  F ZN  202 1_555 ? ? ? ? ? ? ? 2.149 ? 
metalc60 metalc ? ? G  HIS 46  ND1 ? ? ? 1_555 FA ZN  . ZN ? ? G HIS 46  G ZN  201 1_555 ? ? ? ? ? ? ? 2.150 ? 
metalc61 metalc ? ? D  HIS 63  ND1 ? ? ? 1_555 X  ZN  . ZN ? ? D HIS 63  D ZN  202 1_555 ? ? ? ? ? ? ? 2.151 ? 
metalc62 metalc ? ? C  HIS 80  ND1 ? ? ? 1_555 U  ZN  . ZN ? ? C HIS 80  C ZN  202 1_555 ? ? ? ? ? ? ? 2.162 ? 
metalc63 metalc ? ? SA ZN  .   ZN  ? ? ? 1_555 UA SO4 . O3 ? ? K ZN  201 K SO4 203 1_555 ? ? ? ? ? ? ? 2.172 ? 
metalc64 metalc ? ? L  HIS 48  NE2 ? ? ? 1_555 VA ZN  . ZN ? ? L HIS 48  L ZN  201 1_555 ? ? ? ? ? ? ? 2.172 ? 
metalc65 metalc ? ? VA ZN  .   ZN  ? ? ? 1_555 XA SO4 . O1 ? ? L ZN  201 L SO4 203 1_555 ? ? ? ? ? ? ? 2.173 ? 
metalc66 metalc ? ? J  HIS 48  NE2 ? ? ? 1_555 PA ZN  . ZN ? ? J HIS 48  J ZN  201 1_555 ? ? ? ? ? ? ? 2.179 ? 
metalc67 metalc ? ? M  ZN  .   ZN  ? ? ? 1_555 O  SO4 . O4 ? ? A ZN  201 A SO4 203 1_555 ? ? ? ? ? ? ? 2.182 ? 
metalc68 metalc ? ? I  HIS 120 NE2 ? ? ? 1_555 MA ZN  . ZN ? ? I HIS 120 I ZN  201 1_555 ? ? ? ? ? ? ? 2.189 ? 
metalc69 metalc ? ? I  HIS 71  ND1 ? ? ? 1_555 NA ZN  . ZN ? ? I HIS 71  I ZN  202 1_555 ? ? ? ? ? ? ? 2.190 ? 
metalc70 metalc ? ? IA ZN  .   ZN  ? ? ? 1_555 KA SO4 . O4 ? ? H ZN  201 H SO4 203 1_555 ? ? ? ? ? ? ? 2.210 ? 
metalc71 metalc ? ? A  HIS 46  ND1 ? ? ? 1_555 M  ZN  . ZN ? ? A HIS 46  A ZN  201 1_555 ? ? ? ? ? ? ? 2.227 ? 
metalc72 metalc ? ? E  HIS 48  NE2 ? ? ? 1_555 Z  ZN  . ZN ? ? E HIS 48  E ZN  201 1_555 ? ? ? ? ? ? ? 2.233 ? 
metalc73 metalc ? ? K  HIS 63  ND1 ? ? ? 1_555 TA ZN  . ZN ? ? K HIS 63  K ZN  202 1_555 ? ? ? ? ? ? ? 2.248 ? 
metalc74 metalc ? ? C  HIS 63  ND1 ? ? ? 1_555 U  ZN  . ZN ? ? C HIS 63  C ZN  202 1_555 ? ? ? ? ? ? ? 2.263 ? 
metalc75 metalc ? ? I  HIS 48  NE2 ? ? ? 1_555 MA ZN  . ZN ? ? I HIS 48  I ZN  201 1_555 ? ? ? ? ? ? ? 2.271 ? 
metalc76 metalc ? ? C  HIS 46  ND1 ? ? ? 1_555 T  ZN  . ZN ? ? C HIS 46  C ZN  201 1_555 ? ? ? ? ? ? ? 2.274 ? 
metalc77 metalc ? ? L  HIS 46  ND1 ? ? ? 1_555 VA ZN  . ZN ? ? L HIS 46  L ZN  201 1_555 ? ? ? ? ? ? ? 2.279 ? 
metalc78 metalc ? ? MA ZN  .   ZN  ? ? ? 1_555 OA SO4 . O4 ? ? I ZN  201 I SO4 203 1_555 ? ? ? ? ? ? ? 2.284 ? 
metalc79 metalc ? ? K  HIS 48  NE2 ? ? ? 1_555 SA ZN  . ZN ? ? K HIS 48  K ZN  201 1_555 ? ? ? ? ? ? ? 2.293 ? 
metalc80 metalc ? ? P  ZN  .   ZN  ? ? ? 1_555 R  SO4 . O2 ? ? B ZN  201 B SO4 203 1_555 ? ? ? ? ? ? ? 2.296 ? 
metalc81 metalc ? ? E  HIS 46  ND1 ? ? ? 1_555 Z  ZN  . ZN ? ? E HIS 46  E ZN  201 1_555 ? ? ? ? ? ? ? 2.328 ? 
metalc82 metalc ? ? E  HIS 71  ND1 ? ? ? 1_555 AA ZN  . ZN ? ? E HIS 71  E ZN  202 1_555 ? ? ? ? ? ? ? 2.334 ? 
metalc83 metalc ? ? PA ZN  .   ZN  ? ? ? 1_555 RA SO4 . O3 ? ? J ZN  201 J SO4 203 1_555 ? ? ? ? ? ? ? 2.363 ? 
metalc84 metalc ? ? I  HIS 46  ND1 ? ? ? 1_555 MA ZN  . ZN ? ? I HIS 46  I ZN  201 1_555 ? ? ? ? ? ? ? 2.432 ? 
metalc85 metalc ? ? J  HIS 46  ND1 ? ? ? 1_555 PA ZN  . ZN ? ? J HIS 46  J ZN  201 1_555 ? ? ? ? ? ? ? 2.435 ? 
metalc86 metalc ? ? B  HIS 46  ND1 ? ? ? 1_555 P  ZN  . ZN ? ? B HIS 46  B ZN  201 1_555 ? ? ? ? ? ? ? 2.451 ? 
metalc87 metalc ? ? C  ASP 83  OD2 ? ? ? 1_555 U  ZN  . ZN ? ? C ASP 83  C ZN  202 1_555 ? ? ? ? ? ? ? 2.462 ? 
metalc88 metalc ? ? K  HIS 71  ND1 ? ? ? 1_555 TA ZN  . ZN ? ? K HIS 71  K ZN  202 1_555 ? ? ? ? ? ? ? 2.478 ? 
metalc89 metalc ? ? D  HIS 46  ND1 ? ? ? 1_555 W  ZN  . ZN ? ? D HIS 46  D ZN  201 1_555 ? ? ? ? ? ? ? 2.510 ? 
metalc90 metalc ? ? K  HIS 46  ND1 ? ? ? 1_555 SA ZN  . ZN ? ? K HIS 46  K ZN  201 1_555 ? ? ? ? ? ? ? 2.515 ? 
metalc91 metalc ? ? H  HIS 46  ND1 ? ? ? 1_555 IA ZN  . ZN ? ? H HIS 46  H ZN  201 1_555 ? ? ? ? ? ? ? 2.543 ? 
metalc92 metalc ? ? C  HIS 71  ND1 ? ? ? 1_555 U  ZN  . ZN ? ? C HIS 71  C ZN  202 1_555 ? ? ? ? ? ? ? 2.548 ? 
metalc93 metalc ? ? I  HIS 63  ND1 ? ? ? 1_555 NA ZN  . ZN ? ? I HIS 63  I ZN  202 1_555 ? ? ? ? ? ? ? 2.584 ? 
metalc94 metalc ? ? F  HIS 46  ND1 ? ? ? 1_555 CA ZN  . ZN ? ? F HIS 46  F ZN  201 1_555 ? ? ? ? ? ? ? 2.593 ? 
metalc95 metalc ? ? C  HIS 48  NE2 ? ? ? 1_555 T  ZN  . ZN ? ? C HIS 48  C ZN  201 1_555 ? ? ? ? ? ? ? 2.603 ? 
# 
_struct_conn_type.id          metalc 
_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 ? 
I ? 5 ? 
J ? 4 ? 
K ? 5 ? 
L ? 4 ? 
M ? 5 ? 
N ? 4 ? 
O ? 5 ? 
P ? 4 ? 
Q ? 5 ? 
R ? 4 ? 
S ? 5 ? 
T ? 4 ? 
U ? 5 ? 
V ? 4 ? 
W ? 5 ? 
X ? 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 
I 1 2 ? anti-parallel 
I 2 3 ? anti-parallel 
I 3 4 ? anti-parallel 
I 4 5 ? anti-parallel 
J 1 2 ? anti-parallel 
J 2 3 ? anti-parallel 
J 3 4 ? anti-parallel 
K 1 2 ? anti-parallel 
K 2 3 ? anti-parallel 
K 3 4 ? anti-parallel 
K 4 5 ? anti-parallel 
L 1 2 ? anti-parallel 
L 2 3 ? anti-parallel 
L 3 4 ? anti-parallel 
M 1 2 ? anti-parallel 
M 2 3 ? anti-parallel 
M 3 4 ? anti-parallel 
M 4 5 ? anti-parallel 
N 1 2 ? anti-parallel 
N 2 3 ? anti-parallel 
N 3 4 ? anti-parallel 
O 1 2 ? anti-parallel 
O 2 3 ? anti-parallel 
O 3 4 ? anti-parallel 
O 4 5 ? anti-parallel 
P 1 2 ? anti-parallel 
P 2 3 ? anti-parallel 
P 3 4 ? anti-parallel 
Q 1 2 ? anti-parallel 
Q 2 3 ? anti-parallel 
Q 3 4 ? anti-parallel 
Q 4 5 ? anti-parallel 
R 1 2 ? anti-parallel 
R 2 3 ? anti-parallel 
R 3 4 ? anti-parallel 
S 1 2 ? anti-parallel 
S 2 3 ? anti-parallel 
S 3 4 ? anti-parallel 
S 4 5 ? anti-parallel 
T 1 2 ? anti-parallel 
T 2 3 ? anti-parallel 
T 3 4 ? anti-parallel 
U 1 2 ? anti-parallel 
U 2 3 ? anti-parallel 
U 3 4 ? anti-parallel 
U 4 5 ? anti-parallel 
V 1 2 ? anti-parallel 
V 2 3 ? anti-parallel 
V 3 4 ? anti-parallel 
W 1 2 ? anti-parallel 
W 2 3 ? anti-parallel 
W 3 4 ? anti-parallel 
W 4 5 ? anti-parallel 
X 1 2 ? anti-parallel 
X 2 3 ? anti-parallel 
X 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1 ALA A 95  ? ASP A 101 ? ALA A 95  ASP A 101 
A 2 VAL A 29  ? LYS A 36  ? VAL A 29  LYS A 36  
A 3 GLN A 15  ? GLN A 22  ? GLN A 15  GLN A 22  
A 4 THR A 2   ? LEU A 8   ? THR A 2   LEU A 8   
A 5 GLY A 150 ? ILE A 151 ? GLY A 150 ILE A 151 
B 1 ASP A 83  ? ALA A 89  ? ASP A 83  ALA A 89  
B 2 GLY A 41  ? HIS A 48  ? GLY A 41  HIS A 48  
B 3 THR A 116 ? HIS A 120 ? THR A 116 HIS A 120 
B 4 ARG A 143 ? VAL A 148 ? ARG A 143 VAL A 148 
C 1 ALA B 95  ? ASP B 101 ? ALA B 95  ASP B 101 
C 2 VAL B 29  ? LYS B 36  ? VAL B 29  LYS B 36  
C 3 GLN B 15  ? GLN B 22  ? GLN B 15  GLN B 22  
C 4 THR B 2   ? LEU B 8   ? THR B 2   LEU B 8   
C 5 GLY B 150 ? ILE B 151 ? GLY B 150 ILE B 151 
D 1 ASP B 83  ? ALA B 89  ? ASP B 83  ALA B 89  
D 2 GLY B 41  ? HIS B 48  ? GLY B 41  HIS B 48  
D 3 THR B 116 ? HIS B 120 ? THR B 116 HIS B 120 
D 4 ARG B 143 ? VAL B 148 ? ARG B 143 VAL B 148 
E 1 ALA C 95  ? ASP C 101 ? ALA C 95  ASP C 101 
E 2 VAL C 29  ? LYS C 36  ? VAL C 29  LYS C 36  
E 3 GLN C 15  ? GLU C 21  ? GLN C 15  GLU C 21  
E 4 LYS C 3   ? LEU C 8   ? LYS C 3   LEU C 8   
E 5 GLY C 150 ? ILE C 151 ? GLY C 150 ILE C 151 
F 1 ASP C 83  ? ALA C 89  ? ASP C 83  ALA C 89  
F 2 GLY C 41  ? HIS C 48  ? GLY C 41  HIS C 48  
F 3 THR C 116 ? HIS C 120 ? THR C 116 HIS C 120 
F 4 ARG C 143 ? VAL C 148 ? ARG C 143 VAL C 148 
G 1 ALA D 95  ? ASP D 101 ? ALA D 95  ASP D 101 
G 2 VAL D 29  ? LYS D 36  ? VAL D 29  LYS D 36  
G 3 GLN D 15  ? GLN D 22  ? GLN D 15  GLN D 22  
G 4 THR D 2   ? LYS D 9   ? THR D 2   LYS D 9   
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 
I 1 ALA E 95  ? ASP E 101 ? ALA E 95  ASP E 101 
I 2 VAL E 29  ? LYS E 36  ? VAL E 29  LYS E 36  
I 3 GLN E 15  ? GLU E 21  ? GLN E 15  GLU E 21  
I 4 LYS E 3   ? LEU E 8   ? LYS E 3   LEU E 8   
I 5 GLY E 150 ? ALA E 152 ? GLY E 150 ALA E 152 
J 1 ASP E 83  ? ALA E 89  ? ASP E 83  ALA E 89  
J 2 GLY E 41  ? HIS E 48  ? GLY E 41  HIS E 48  
J 3 THR E 116 ? HIS E 120 ? THR E 116 HIS E 120 
J 4 ARG E 143 ? VAL E 148 ? ARG E 143 VAL E 148 
K 1 ALA F 95  ? ASP F 101 ? ALA F 95  ASP F 101 
K 2 VAL F 29  ? LYS F 36  ? VAL F 29  LYS F 36  
K 3 GLN F 15  ? GLN F 22  ? GLN F 15  GLN F 22  
K 4 THR F 2   ? LYS F 9   ? THR F 2   LYS F 9   
K 5 GLY F 150 ? ILE F 151 ? GLY F 150 ILE F 151 
L 1 ASP F 83  ? ALA F 89  ? ASP F 83  ALA F 89  
L 2 GLY F 41  ? HIS F 48  ? GLY F 41  HIS F 48  
L 3 THR F 116 ? VAL F 119 ? THR F 116 VAL F 119 
L 4 ALA F 145 ? VAL F 148 ? ALA F 145 VAL F 148 
M 1 ALA G 95  ? ASP G 101 ? ALA G 95  ASP G 101 
M 2 VAL G 29  ? LYS G 36  ? VAL G 29  LYS G 36  
M 3 GLN G 15  ? GLN G 22  ? GLN G 15  GLN G 22  
M 4 THR G 2   ? LEU G 8   ? THR G 2   LEU G 8   
M 5 GLY G 150 ? ILE G 151 ? GLY G 150 ILE G 151 
N 1 ASP G 83  ? ALA G 89  ? ASP G 83  ALA G 89  
N 2 GLY G 41  ? HIS G 48  ? GLY G 41  HIS G 48  
N 3 THR G 116 ? HIS G 120 ? THR G 116 HIS G 120 
N 4 ARG G 143 ? VAL G 148 ? ARG G 143 VAL G 148 
O 1 ALA H 95  ? ASP H 101 ? ALA H 95  ASP H 101 
O 2 VAL H 29  ? LYS H 36  ? VAL H 29  LYS H 36  
O 3 GLN H 15  ? GLN H 22  ? GLN H 15  GLN H 22  
O 4 THR H 2   ? LEU H 8   ? THR H 2   LEU H 8   
O 5 GLY H 150 ? ILE H 151 ? GLY H 150 ILE H 151 
P 1 ASP H 83  ? ALA H 89  ? ASP H 83  ALA H 89  
P 2 GLY H 41  ? HIS H 48  ? GLY H 41  HIS H 48  
P 3 THR H 116 ? HIS H 120 ? THR H 116 HIS H 120 
P 4 ARG H 143 ? VAL H 148 ? ARG H 143 VAL H 148 
Q 1 ALA I 95  ? ASP I 101 ? ALA I 95  ASP I 101 
Q 2 VAL I 29  ? LYS I 36  ? VAL I 29  LYS I 36  
Q 3 GLN I 15  ? GLN I 22  ? GLN I 15  GLN I 22  
Q 4 THR I 2   ? LYS I 9   ? THR I 2   LYS I 9   
Q 5 GLY I 150 ? ILE I 151 ? GLY I 150 ILE I 151 
R 1 ASP I 83  ? ALA I 89  ? ASP I 83  ALA I 89  
R 2 GLY I 41  ? HIS I 48  ? GLY I 41  HIS I 48  
R 3 THR I 116 ? HIS I 120 ? THR I 116 HIS I 120 
R 4 ARG I 143 ? VAL I 148 ? ARG I 143 VAL I 148 
S 1 ALA J 95  ? ASP J 101 ? ALA J 95  ASP J 101 
S 2 VAL J 29  ? LYS J 36  ? VAL J 29  LYS J 36  
S 3 GLN J 15  ? GLN J 22  ? GLN J 15  GLN J 22  
S 4 THR J 2   ? LYS J 9   ? THR J 2   LYS J 9   
S 5 GLY J 150 ? ALA J 152 ? GLY J 150 ALA J 152 
T 1 ASP J 83  ? ALA J 89  ? ASP J 83  ALA J 89  
T 2 GLY J 41  ? HIS J 48  ? GLY J 41  HIS J 48  
T 3 THR J 116 ? HIS J 120 ? THR J 116 HIS J 120 
T 4 ARG J 143 ? VAL J 148 ? ARG J 143 VAL J 148 
U 1 VAL K 94  ? ASP K 101 ? VAL K 94  ASP K 101 
U 2 VAL K 29  ? LYS K 36  ? VAL K 29  LYS K 36  
U 3 GLN K 15  ? GLN K 22  ? GLN K 15  GLN K 22  
U 4 THR K 2   ? LYS K 9   ? THR K 2   LYS K 9   
U 5 GLY K 150 ? ILE K 151 ? GLY K 150 ILE K 151 
V 1 ASP K 83  ? ALA K 89  ? ASP K 83  ALA K 89  
V 2 GLY K 41  ? HIS K 48  ? GLY K 41  HIS K 48  
V 3 THR K 116 ? HIS K 120 ? THR K 116 HIS K 120 
V 4 ARG K 143 ? ALA K 145 ? ARG K 143 ALA K 145 
W 1 SER L 98  ? ASP L 101 ? SER L 98  ASP L 101 
W 2 VAL L 29  ? LYS L 36  ? VAL L 29  LYS L 36  
W 3 GLN L 15  ? GLN L 22  ? GLN L 15  GLN L 22  
W 4 THR L 2   ? LYS L 9   ? THR L 2   LYS L 9   
W 5 GLY L 150 ? ALA L 152 ? GLY L 150 ALA L 152 
X 1 ASP L 83  ? ALA L 89  ? ASP L 83  ALA L 89  
X 2 GLY L 41  ? HIS L 48  ? GLY L 41  HIS L 48  
X 3 THR L 116 ? HIS L 120 ? THR L 116 HIS L 120 
X 4 ARG L 143 ? VAL L 148 ? ARG L 143 VAL L 148 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2 O ASP A 101 ? O ASP A 101 N VAL A 29  ? N VAL A 29  
A 2 3 O TRP A 32  ? O TRP A 32  N ASN A 19  ? N ASN A 19  
A 3 4 O PHE A 20  ? O PHE A 20  N ALA A 4   ? N ALA A 4   
A 4 5 N VAL A 5   ? N VAL A 5   O GLY A 150 ? O GLY A 150 
B 1 2 O ALA A 89  ? O ALA A 89  N GLY A 41  ? N GLY A 41  
B 2 3 N HIS A 48  ? N HIS A 48  O THR A 116 ? O THR A 116 
B 3 4 N LEU A 117 ? N LEU A 117 O GLY A 147 ? O GLY A 147 
C 1 2 O ASP B 101 ? O ASP B 101 N VAL B 29  ? N VAL B 29  
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 LEU B 117 ? N LEU B 117 O GLY B 147 ? O GLY B 147 
E 1 2 O ASP C 101 ? O ASP C 101 N VAL C 29  ? N VAL C 29  
E 2 3 O TRP C 32  ? O TRP C 32  N ASN C 19  ? N ASN C 19  
E 3 4 O GLY C 16  ? O GLY C 16  N LEU C 8   ? N LEU C 8   
E 4 5 N VAL C 5   ? N VAL C 5   O GLY C 150 ? O GLY C 150 
F 1 2 O ALA C 89  ? O ALA C 89  N GLY C 41  ? N GLY C 41  
F 2 3 N HIS C 48  ? N HIS C 48  O THR C 116 ? O THR C 116 
F 3 4 N VAL C 119 ? N VAL C 119 O LEU C 144 ? O LEU C 144 
G 1 2 O ILE D 99  ? O ILE D 99  N VAL D 31  ? N VAL D 31  
G 2 3 O TRP D 32  ? O TRP D 32  N ASN D 19  ? N ASN D 19  
G 3 4 O 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 GLY D 85  ? O GLY D 85  N PHE D 45  ? N PHE D 45  
H 2 3 N HIS D 48  ? N HIS D 48  O THR D 116 ? O THR D 116 
H 3 4 N LEU D 117 ? N LEU D 117 O GLY D 147 ? O GLY D 147 
I 1 2 O ILE E 99  ? O ILE E 99  N VAL E 31  ? N VAL E 31  
I 2 3 O LYS E 36  ? O LYS E 36  N GLN E 15  ? N GLN E 15  
I 3 4 O GLY E 16  ? O GLY E 16  N LEU E 8   ? N LEU E 8   
I 4 5 N VAL E 5   ? N VAL E 5   O GLY E 150 ? O GLY E 150 
J 1 2 O GLY E 85  ? O GLY E 85  N PHE E 45  ? N PHE E 45  
J 2 3 N HIS E 48  ? N HIS E 48  O THR E 116 ? O THR E 116 
J 3 4 N LEU E 117 ? N LEU E 117 O GLY E 147 ? O GLY E 147 
K 1 2 O ALA F 95  ? O ALA F 95  N ILE F 35  ? N ILE F 35  
K 2 3 O TRP F 32  ? O TRP F 32  N ASN F 19  ? N ASN F 19  
K 3 4 O GLY F 16  ? O GLY F 16  N LEU F 8   ? N LEU F 8   
K 4 5 N VAL F 5   ? N VAL F 5   O GLY F 150 ? O GLY F 150 
L 1 2 O GLY F 85  ? O GLY F 85  N PHE F 45  ? N PHE F 45  
L 2 3 N HIS F 46  ? N HIS F 46  O VAL F 118 ? O VAL F 118 
L 3 4 N LEU F 117 ? N LEU F 117 O GLY F 147 ? O GLY F 147 
M 1 2 O ILE G 99  ? O ILE G 99  N VAL G 31  ? N VAL G 31  
M 2 3 O TRP G 32  ? O TRP G 32  N ASN G 19  ? N ASN G 19  
M 3 4 O GLY G 16  ? O GLY G 16  N LEU G 8   ? N LEU G 8   
M 4 5 N VAL G 5   ? N VAL G 5   O GLY G 150 ? O GLY G 150 
N 1 2 O ALA G 89  ? O ALA G 89  N GLY G 41  ? N GLY G 41  
N 2 3 N HIS G 48  ? N HIS G 48  O THR G 116 ? O THR G 116 
N 3 4 N LEU G 117 ? N LEU G 117 O GLY G 147 ? O GLY G 147 
O 1 2 O ASP H 101 ? O ASP H 101 N VAL H 29  ? N VAL H 29  
O 2 3 O TRP H 32  ? O TRP H 32  N ASN H 19  ? N ASN H 19  
O 3 4 O GLY H 16  ? O GLY H 16  N LEU H 8   ? N LEU H 8   
O 4 5 N VAL H 5   ? N VAL H 5   O GLY H 150 ? O GLY H 150 
P 1 2 O ALA H 89  ? O ALA H 89  N GLY H 41  ? N GLY H 41  
P 2 3 N HIS H 48  ? N HIS H 48  O THR H 116 ? O THR H 116 
P 3 4 N VAL H 119 ? N VAL H 119 O ALA H 145 ? O ALA H 145 
Q 1 2 O ASP I 101 ? O ASP I 101 N VAL I 29  ? N VAL I 29  
Q 2 3 O TRP I 32  ? O TRP I 32  N ASN I 19  ? N ASN I 19  
Q 3 4 O GLY I 16  ? O GLY I 16  N LEU I 8   ? N LEU I 8   
Q 4 5 N VAL I 5   ? N VAL I 5   O GLY I 150 ? O GLY I 150 
R 1 2 O VAL I 87  ? O VAL I 87  N HIS I 43  ? N HIS I 43  
R 2 3 N HIS I 48  ? N HIS I 48  O THR I 116 ? O THR I 116 
R 3 4 N VAL I 119 ? N VAL I 119 O LEU I 144 ? O LEU I 144 
S 1 2 O ALA J 95  ? O ALA J 95  N ILE J 35  ? N ILE J 35  
S 2 3 O TRP J 32  ? O TRP J 32  N ASN J 19  ? N ASN J 19  
S 3 4 O GLY J 16  ? O GLY J 16  N LEU J 8   ? N LEU J 8   
S 4 5 N VAL J 5   ? N VAL J 5   O GLY J 150 ? O GLY J 150 
T 1 2 O ALA J 89  ? O ALA J 89  N GLY J 41  ? N GLY J 41  
T 2 3 N HIS J 48  ? N HIS J 48  O THR J 116 ? O THR J 116 
T 3 4 N VAL J 119 ? N VAL J 119 O ALA J 145 ? O ALA J 145 
U 1 2 O ILE K 99  ? O ILE K 99  N VAL K 31  ? N VAL K 31  
U 2 3 O TRP K 32  ? O TRP K 32  N ASN K 19  ? N ASN K 19  
U 3 4 O PHE K 20  ? O PHE K 20  N ALA K 4   ? N ALA K 4   
U 4 5 N VAL K 5   ? N VAL K 5   O GLY K 150 ? O GLY K 150 
V 1 2 O ALA K 89  ? O ALA K 89  N GLY K 41  ? N GLY K 41  
V 2 3 N HIS K 48  ? N HIS K 48  O THR K 116 ? O THR K 116 
V 3 4 N VAL K 119 ? N VAL K 119 O LEU K 144 ? O LEU K 144 
W 1 2 O ILE L 99  ? O ILE L 99  N VAL L 31  ? N VAL L 31  
W 2 3 O TRP L 32  ? O TRP L 32  N ASN L 19  ? N ASN L 19  
W 3 4 O PHE L 20  ? O PHE L 20  N ALA L 4   ? N ALA L 4   
W 4 5 N VAL L 5   ? N VAL L 5   O GLY L 150 ? O GLY L 150 
X 1 2 O GLY L 85  ? O GLY L 85  N PHE L 45  ? N PHE L 45  
X 2 3 N HIS L 48  ? N HIS L 48  O THR L 116 ? O THR L 116 
X 3 4 N VAL L 119 ? N VAL L 119 O ALA L 145 ? O ALA L 145 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE ZN A 201'  
AC2 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE ZN A 202'  
AC3 Software ? ? ? ? 8  'BINDING SITE FOR RESIDUE SO4 A 203' 
AC4 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE ZN B 201'  
AC5 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE ZN B 202'  
AC6 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE SO4 B 203' 
AC7 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE SO4 B 204' 
AC8 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE ZN C 201'  
AC9 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE ZN C 202'  
BC1 Software ? ? ? ? 8  'BINDING SITE FOR RESIDUE SO4 C 203' 
BC2 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE ZN D 201'  
BC3 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE ZN D 202'  
BC4 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE SO4 D 203' 
BC5 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE ZN E 201'  
BC6 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE ZN E 202'  
BC7 Software ? ? ? ? 8  'BINDING SITE FOR RESIDUE SO4 E 203' 
BC8 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE ZN F 201'  
BC9 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE ZN F 202'  
CC1 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE SO4 F 203' 
CC2 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE ZN G 201'  
CC3 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE ZN G 202'  
CC4 Software ? ? ? ? 10 'BINDING SITE FOR RESIDUE SO4 G 203' 
CC5 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE ZN H 201'  
CC6 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE ZN H 202'  
CC7 Software ? ? ? ? 8  'BINDING SITE FOR RESIDUE SO4 H 203' 
CC8 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE SO4 H 204' 
CC9 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE ZN I 201'  
DC1 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE ZN I 202'  
DC2 Software ? ? ? ? 8  'BINDING SITE FOR RESIDUE SO4 I 203' 
DC3 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE ZN J 201'  
DC4 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE ZN J 202'  
DC5 Software ? ? ? ? 8  'BINDING SITE FOR RESIDUE SO4 J 203' 
DC6 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE ZN K 201'  
DC7 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE ZN K 202'  
DC8 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE SO4 K 203' 
DC9 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE ZN L 201'  
EC1 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE ZN L 202'  
EC2 Software ? ? ? ? 8  'BINDING SITE FOR RESIDUE SO4 L 203' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1   AC1 5  HIS A  46  ? HIS A 46  . ? 1_555 ? 
2   AC1 5  HIS A  48  ? HIS A 48  . ? 1_555 ? 
3   AC1 5  HIS A  63  ? HIS A 63  . ? 1_555 ? 
4   AC1 5  HIS A  120 ? HIS A 120 . ? 1_555 ? 
5   AC1 5  SO4 O  .   ? SO4 A 203 . ? 1_555 ? 
6   AC2 5  HIS A  63  ? HIS A 63  . ? 1_555 ? 
7   AC2 5  HIS A  71  ? HIS A 71  . ? 1_555 ? 
8   AC2 5  HIS A  80  ? HIS A 80  . ? 1_555 ? 
9   AC2 5  ASP A  83  ? ASP A 83  . ? 1_555 ? 
10  AC2 5  LYS A  136 ? LYS A 136 . ? 1_555 ? 
11  AC3 8  HIS A  46  ? HIS A 46  . ? 1_555 ? 
12  AC3 8  HIS A  48  ? HIS A 48  . ? 1_555 ? 
13  AC3 8  HIS A  63  ? HIS A 63  . ? 1_555 ? 
14  AC3 8  HIS A  120 ? HIS A 120 . ? 1_555 ? 
15  AC3 8  THR A  137 ? THR A 137 . ? 1_555 ? 
16  AC3 8  ARG A  143 ? ARG A 143 . ? 1_555 ? 
17  AC3 8  ZN  M  .   ? ZN  A 201 . ? 1_555 ? 
18  AC3 8  HOH YA .   ? HOH A 379 . ? 1_555 ? 
19  AC4 5  HIS B  46  ? HIS B 46  . ? 1_555 ? 
20  AC4 5  HIS B  48  ? HIS B 48  . ? 1_555 ? 
21  AC4 5  HIS B  63  ? HIS B 63  . ? 1_555 ? 
22  AC4 5  HIS B  120 ? HIS B 120 . ? 1_555 ? 
23  AC4 5  SO4 R  .   ? SO4 B 203 . ? 1_555 ? 
24  AC5 4  HIS B  63  ? HIS B 63  . ? 1_555 ? 
25  AC5 4  HIS B  71  ? HIS B 71  . ? 1_555 ? 
26  AC5 4  HIS B  80  ? HIS B 80  . ? 1_555 ? 
27  AC5 4  ASP B  83  ? ASP B 83  . ? 1_555 ? 
28  AC6 7  HIS B  48  ? HIS B 48  . ? 1_555 ? 
29  AC6 7  HIS B  63  ? HIS B 63  . ? 1_555 ? 
30  AC6 7  HIS B  120 ? HIS B 120 . ? 1_555 ? 
31  AC6 7  THR B  137 ? THR B 137 . ? 1_555 ? 
32  AC6 7  ARG B  143 ? ARG B 143 . ? 1_555 ? 
33  AC6 7  ZN  P  .   ? ZN  B 201 . ? 1_555 ? 
34  AC6 7  HOH ZA .   ? HOH B 353 . ? 1_555 ? 
35  AC7 4  LYS B  75  ? LYS B 75  . ? 1_555 ? 
36  AC7 4  LYS B  128 ? LYS B 128 . ? 1_555 ? 
37  AC7 4  LYS D  128 ? LYS D 128 . ? 1_555 ? 
38  AC7 4  LYS F  128 ? LYS F 128 . ? 1_555 ? 
39  AC8 5  HIS C  46  ? HIS C 46  . ? 1_555 ? 
40  AC8 5  HIS C  48  ? HIS C 48  . ? 1_555 ? 
41  AC8 5  HIS C  63  ? HIS C 63  . ? 1_555 ? 
42  AC8 5  HIS C  120 ? HIS C 120 . ? 1_555 ? 
43  AC8 5  SO4 V  .   ? SO4 C 203 . ? 1_555 ? 
44  AC9 5  HIS C  63  ? HIS C 63  . ? 1_555 ? 
45  AC9 5  HIS C  71  ? HIS C 71  . ? 1_555 ? 
46  AC9 5  HIS C  80  ? HIS C 80  . ? 1_555 ? 
47  AC9 5  ASP C  83  ? ASP C 83  . ? 1_555 ? 
48  AC9 5  LYS C  136 ? LYS C 136 . ? 1_555 ? 
49  BC1 8  HIS C  46  ? HIS C 46  . ? 1_555 ? 
50  BC1 8  HIS C  48  ? HIS C 48  . ? 1_555 ? 
51  BC1 8  HIS C  63  ? HIS C 63  . ? 1_555 ? 
52  BC1 8  HIS C  120 ? HIS C 120 . ? 1_555 ? 
53  BC1 8  THR C  137 ? THR C 137 . ? 1_555 ? 
54  BC1 8  ARG C  143 ? ARG C 143 . ? 1_555 ? 
55  BC1 8  ZN  T  .   ? ZN  C 201 . ? 1_555 ? 
56  BC1 8  HOH AB .   ? HOH C 317 . ? 1_555 ? 
57  BC2 5  HIS D  46  ? HIS D 46  . ? 1_555 ? 
58  BC2 5  HIS D  48  ? HIS D 48  . ? 1_555 ? 
59  BC2 5  HIS D  63  ? HIS D 63  . ? 1_555 ? 
60  BC2 5  HIS D  120 ? HIS D 120 . ? 1_555 ? 
61  BC2 5  SO4 Y  .   ? SO4 D 203 . ? 1_555 ? 
62  BC3 4  HIS D  63  ? HIS D 63  . ? 1_555 ? 
63  BC3 4  HIS D  71  ? HIS D 71  . ? 1_555 ? 
64  BC3 4  HIS D  80  ? HIS D 80  . ? 1_555 ? 
65  BC3 4  ASP D  83  ? ASP D 83  . ? 1_555 ? 
66  BC4 6  HIS D  48  ? HIS D 48  . ? 1_555 ? 
67  BC4 6  HIS D  63  ? HIS D 63  . ? 1_555 ? 
68  BC4 6  HIS D  120 ? HIS D 120 . ? 1_555 ? 
69  BC4 6  THR D  137 ? THR D 137 . ? 1_555 ? 
70  BC4 6  ARG D  143 ? ARG D 143 . ? 1_555 ? 
71  BC4 6  ZN  W  .   ? ZN  D 201 . ? 1_555 ? 
72  BC5 5  HIS E  46  ? HIS E 46  . ? 1_555 ? 
73  BC5 5  HIS E  48  ? HIS E 48  . ? 1_555 ? 
74  BC5 5  HIS E  63  ? HIS E 63  . ? 1_555 ? 
75  BC5 5  HIS E  120 ? HIS E 120 . ? 1_555 ? 
76  BC5 5  SO4 BA .   ? SO4 E 203 . ? 1_555 ? 
77  BC6 4  HIS E  63  ? HIS E 63  . ? 1_555 ? 
78  BC6 4  HIS E  71  ? HIS E 71  . ? 1_555 ? 
79  BC6 4  HIS E  80  ? HIS E 80  . ? 1_555 ? 
80  BC6 4  ASP E  83  ? ASP E 83  . ? 1_555 ? 
81  BC7 8  HIS E  46  ? HIS E 46  . ? 1_555 ? 
82  BC7 8  HIS E  48  ? HIS E 48  . ? 1_555 ? 
83  BC7 8  HIS E  63  ? HIS E 63  . ? 1_555 ? 
84  BC7 8  HIS E  120 ? HIS E 120 . ? 1_555 ? 
85  BC7 8  THR E  137 ? THR E 137 . ? 1_555 ? 
86  BC7 8  ARG E  143 ? ARG E 143 . ? 1_555 ? 
87  BC7 8  ZN  Z  .   ? ZN  E 201 . ? 1_555 ? 
88  BC7 8  HOH CB .   ? HOH E 333 . ? 1_555 ? 
89  BC8 5  HIS F  46  ? HIS F 46  . ? 1_555 ? 
90  BC8 5  HIS F  48  ? HIS F 48  . ? 1_555 ? 
91  BC8 5  HIS F  63  ? HIS F 63  . ? 1_555 ? 
92  BC8 5  HIS F  120 ? HIS F 120 . ? 1_555 ? 
93  BC8 5  SO4 EA .   ? SO4 F 203 . ? 1_555 ? 
94  BC9 4  HIS F  63  ? HIS F 63  . ? 1_555 ? 
95  BC9 4  HIS F  71  ? HIS F 71  . ? 1_555 ? 
96  BC9 4  HIS F  80  ? HIS F 80  . ? 1_555 ? 
97  BC9 4  ASP F  83  ? ASP F 83  . ? 1_555 ? 
98  CC1 6  HIS F  48  ? HIS F 48  . ? 1_555 ? 
99  CC1 6  HIS F  63  ? HIS F 63  . ? 1_555 ? 
100 CC1 6  HIS F  120 ? HIS F 120 . ? 1_555 ? 
101 CC1 6  THR F  137 ? THR F 137 . ? 1_555 ? 
102 CC1 6  ARG F  143 ? ARG F 143 . ? 1_555 ? 
103 CC1 6  ZN  CA .   ? ZN  F 201 . ? 1_555 ? 
104 CC2 5  HIS G  46  ? HIS G 46  . ? 1_555 ? 
105 CC2 5  HIS G  48  ? HIS G 48  . ? 1_555 ? 
106 CC2 5  HIS G  63  ? HIS G 63  . ? 1_555 ? 
107 CC2 5  HIS G  120 ? HIS G 120 . ? 1_555 ? 
108 CC2 5  SO4 HA .   ? SO4 G 203 . ? 1_555 ? 
109 CC3 4  HIS G  63  ? HIS G 63  . ? 1_555 ? 
110 CC3 4  HIS G  71  ? HIS G 71  . ? 1_555 ? 
111 CC3 4  HIS G  80  ? HIS G 80  . ? 1_555 ? 
112 CC3 4  ASP G  83  ? ASP G 83  . ? 1_555 ? 
113 CC4 10 HIS G  46  ? HIS G 46  . ? 1_555 ? 
114 CC4 10 HIS G  48  ? HIS G 48  . ? 1_555 ? 
115 CC4 10 HIS G  63  ? HIS G 63  . ? 1_555 ? 
116 CC4 10 HIS G  120 ? HIS G 120 . ? 1_555 ? 
117 CC4 10 THR G  137 ? THR G 137 . ? 1_555 ? 
118 CC4 10 ARG G  143 ? ARG G 143 . ? 1_555 ? 
119 CC4 10 ZN  FA .   ? ZN  G 201 . ? 1_555 ? 
120 CC4 10 HOH EB .   ? HOH G 307 . ? 1_555 ? 
121 CC4 10 HOH EB .   ? HOH G 341 . ? 1_555 ? 
122 CC4 10 HOH EB .   ? HOH G 350 . ? 1_555 ? 
123 CC5 5  HIS H  46  ? HIS H 46  . ? 1_555 ? 
124 CC5 5  HIS H  48  ? HIS H 48  . ? 1_555 ? 
125 CC5 5  HIS H  63  ? HIS H 63  . ? 1_555 ? 
126 CC5 5  HIS H  120 ? HIS H 120 . ? 1_555 ? 
127 CC5 5  SO4 KA .   ? SO4 H 203 . ? 1_555 ? 
128 CC6 4  HIS H  63  ? HIS H 63  . ? 1_555 ? 
129 CC6 4  HIS H  71  ? HIS H 71  . ? 1_555 ? 
130 CC6 4  HIS H  80  ? HIS H 80  . ? 1_555 ? 
131 CC6 4  ASP H  83  ? ASP H 83  . ? 1_555 ? 
132 CC7 8  HIS H  48  ? HIS H 48  . ? 1_555 ? 
133 CC7 8  HIS H  63  ? HIS H 63  . ? 1_555 ? 
134 CC7 8  HIS H  120 ? HIS H 120 . ? 1_555 ? 
135 CC7 8  THR H  137 ? THR H 137 . ? 1_555 ? 
136 CC7 8  ARG H  143 ? ARG H 143 . ? 1_555 ? 
137 CC7 8  ZN  IA .   ? ZN  H 201 . ? 1_555 ? 
138 CC7 8  HOH FB .   ? HOH H 342 . ? 1_555 ? 
139 CC7 8  HOH FB .   ? HOH H 438 . ? 1_555 ? 
140 CC8 3  LYS H  128 ? LYS H 128 . ? 1_555 ? 
141 CC8 3  LYS J  75  ? LYS J 75  . ? 1_555 ? 
142 CC8 3  LYS L  128 ? LYS L 128 . ? 1_555 ? 
143 CC9 5  HIS I  46  ? HIS I 46  . ? 1_555 ? 
144 CC9 5  HIS I  48  ? HIS I 48  . ? 1_555 ? 
145 CC9 5  HIS I  63  ? HIS I 63  . ? 1_555 ? 
146 CC9 5  HIS I  120 ? HIS I 120 . ? 1_555 ? 
147 CC9 5  SO4 OA .   ? SO4 I 203 . ? 1_555 ? 
148 DC1 4  HIS I  63  ? HIS I 63  . ? 1_555 ? 
149 DC1 4  HIS I  71  ? HIS I 71  . ? 1_555 ? 
150 DC1 4  HIS I  80  ? HIS I 80  . ? 1_555 ? 
151 DC1 4  ASP I  83  ? ASP I 83  . ? 1_555 ? 
152 DC2 8  HIS I  48  ? HIS I 48  . ? 1_555 ? 
153 DC2 8  HIS I  63  ? HIS I 63  . ? 1_555 ? 
154 DC2 8  HIS I  120 ? HIS I 120 . ? 1_555 ? 
155 DC2 8  THR I  137 ? THR I 137 . ? 1_555 ? 
156 DC2 8  ARG I  143 ? ARG I 143 . ? 1_555 ? 
157 DC2 8  ZN  MA .   ? ZN  I 201 . ? 1_555 ? 
158 DC2 8  HOH GB .   ? HOH I 306 . ? 1_555 ? 
159 DC2 8  HOH GB .   ? HOH I 347 . ? 1_555 ? 
160 DC3 6  HIS J  46  ? HIS J 46  . ? 1_555 ? 
161 DC3 6  HIS J  48  ? HIS J 48  . ? 1_555 ? 
162 DC3 6  HIS J  63  ? HIS J 63  . ? 1_555 ? 
163 DC3 6  HIS J  120 ? HIS J 120 . ? 1_555 ? 
164 DC3 6  SO4 RA .   ? SO4 J 203 . ? 1_555 ? 
165 DC3 6  HOH HB .   ? HOH J 351 . ? 1_555 ? 
166 DC4 4  HIS J  63  ? HIS J 63  . ? 1_555 ? 
167 DC4 4  HIS J  71  ? HIS J 71  . ? 1_555 ? 
168 DC4 4  HIS J  80  ? HIS J 80  . ? 1_555 ? 
169 DC4 4  ASP J  83  ? ASP J 83  . ? 1_555 ? 
170 DC5 8  HIS J  48  ? HIS J 48  . ? 1_555 ? 
171 DC5 8  HIS J  63  ? HIS J 63  . ? 1_555 ? 
172 DC5 8  HIS J  120 ? HIS J 120 . ? 1_555 ? 
173 DC5 8  THR J  137 ? THR J 137 . ? 1_555 ? 
174 DC5 8  ARG J  143 ? ARG J 143 . ? 1_555 ? 
175 DC5 8  ZN  PA .   ? ZN  J 201 . ? 1_555 ? 
176 DC5 8  HOH HB .   ? HOH J 351 . ? 1_555 ? 
177 DC5 8  HOH HB .   ? HOH J 397 . ? 1_555 ? 
178 DC6 5  HIS K  46  ? HIS K 46  . ? 1_555 ? 
179 DC6 5  HIS K  48  ? HIS K 48  . ? 1_555 ? 
180 DC6 5  HIS K  63  ? HIS K 63  . ? 1_555 ? 
181 DC6 5  HIS K  120 ? HIS K 120 . ? 1_555 ? 
182 DC6 5  SO4 UA .   ? SO4 K 203 . ? 1_555 ? 
183 DC7 4  HIS K  63  ? HIS K 63  . ? 1_555 ? 
184 DC7 4  HIS K  71  ? HIS K 71  . ? 1_555 ? 
185 DC7 4  HIS K  80  ? HIS K 80  . ? 1_555 ? 
186 DC7 4  ASP K  83  ? ASP K 83  . ? 1_555 ? 
187 DC8 7  HIS K  48  ? HIS K 48  . ? 1_555 ? 
188 DC8 7  HIS K  63  ? HIS K 63  . ? 1_555 ? 
189 DC8 7  HIS K  120 ? HIS K 120 . ? 1_555 ? 
190 DC8 7  THR K  137 ? THR K 137 . ? 1_555 ? 
191 DC8 7  ARG K  143 ? ARG K 143 . ? 1_555 ? 
192 DC8 7  ZN  SA .   ? ZN  K 201 . ? 1_555 ? 
193 DC8 7  HOH IB .   ? HOH K 322 . ? 1_555 ? 
194 DC9 5  HIS L  46  ? HIS L 46  . ? 1_555 ? 
195 DC9 5  HIS L  48  ? HIS L 48  . ? 1_555 ? 
196 DC9 5  HIS L  63  ? HIS L 63  . ? 1_555 ? 
197 DC9 5  HIS L  120 ? HIS L 120 . ? 1_555 ? 
198 DC9 5  SO4 XA .   ? SO4 L 203 . ? 1_555 ? 
199 EC1 4  HIS L  63  ? HIS L 63  . ? 1_555 ? 
200 EC1 4  HIS L  71  ? HIS L 71  . ? 1_555 ? 
201 EC1 4  HIS L  80  ? HIS L 80  . ? 1_555 ? 
202 EC1 4  ASP L  83  ? ASP L 83  . ? 1_555 ? 
203 EC2 8  HIS L  46  ? HIS L 46  . ? 1_555 ? 
204 EC2 8  HIS L  48  ? HIS L 48  . ? 1_555 ? 
205 EC2 8  HIS L  63  ? HIS L 63  . ? 1_555 ? 
206 EC2 8  HIS L  120 ? HIS L 120 . ? 1_555 ? 
207 EC2 8  THR L  137 ? THR L 137 . ? 1_555 ? 
208 EC2 8  ARG L  143 ? ARG L 143 . ? 1_555 ? 
209 EC2 8  ZN  VA .   ? ZN  L 201 . ? 1_555 ? 
210 EC2 8  HOH JB .   ? HOH L 302 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          4MCM 
_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                    4MCM 
_atom_sites.fract_transf_matrix[1][1]   0.013417 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.006102 
_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]   0.005743 
_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  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N   . ALA A  1 1   ? 8.646   125.895 31.279  1.00 30.29 ? 1   ALA A N   1 
ATOM   2     C  CA  . ALA A  1 1   ? 9.574   126.100 30.170  1.00 32.35 ? 1   ALA A CA  1 
ATOM   3     C  C   . ALA A  1 1   ? 10.451  124.869 29.914  1.00 27.80 ? 1   ALA A C   1 
ATOM   4     O  O   . ALA A  1 1   ? 11.153  124.408 30.817  1.00 32.10 ? 1   ALA A O   1 
ATOM   5     C  CB  . ALA A  1 1   ? 10.453  127.339 30.435  1.00 30.14 ? 1   ALA A CB  1 
ATOM   6     N  N   . THR A  1 2   ? 10.415  124.344 28.692  1.00 23.17 ? 2   THR A N   1 
ATOM   7     C  CA  . THR A  1 2   ? 11.331  123.275 28.311  1.00 22.79 ? 2   THR A CA  1 
ATOM   8     C  C   . THR A  1 2   ? 12.736  123.875 28.157  1.00 22.17 ? 2   THR A C   1 
ATOM   9     O  O   . THR A  1 2   ? 12.897  124.977 27.641  1.00 21.42 ? 2   THR A O   1 
ATOM   10    C  CB  . THR A  1 2   ? 10.880  122.546 27.019  1.00 22.61 ? 2   THR A CB  1 
ATOM   11    O  OG1 . THR A  1 2   ? 9.463   122.354 27.048  1.00 37.55 ? 2   THR A OG1 1 
ATOM   12    C  CG2 . THR A  1 2   ? 11.533  121.192 26.908  1.00 21.85 ? 2   THR A CG2 1 
ATOM   13    N  N   . LYS A  1 3   ? 13.740  123.167 28.656  1.00 17.98 ? 3   LYS A N   1 
ATOM   14    C  CA  . LYS A  1 3   ? 15.121  123.641 28.611  1.00 18.12 ? 3   LYS A CA  1 
ATOM   15    C  C   . LYS A  1 3   ? 16.008  122.540 28.085  1.00 16.37 ? 3   LYS A C   1 
ATOM   16    O  O   . LYS A  1 3   ? 15.743  121.356 28.294  1.00 16.74 ? 3   LYS A O   1 
ATOM   17    C  CB  . LYS A  1 3   ? 15.618  124.060 29.997  1.00 19.80 ? 3   LYS A CB  1 
ATOM   18    C  CG  . LYS A  1 3   ? 14.799  125.177 30.633  1.00 26.02 ? 3   LYS A CG  1 
ATOM   19    C  CD  . LYS A  1 3   ? 15.356  125.594 31.982  1.00 30.49 ? 3   LYS A CD  1 
ATOM   20    C  CE  . LYS A  1 3   ? 16.797  126.089 31.866  1.00 39.70 ? 3   LYS A CE  1 
ATOM   21    N  NZ  . LYS A  1 3   ? 16.947  127.241 30.907  1.00 42.38 ? 3   LYS A NZ  1 
ATOM   22    N  N   . ALA A  1 4   ? 17.060  122.921 27.384  1.00 12.60 ? 4   ALA A N   1 
ATOM   23    C  CA  . ALA A  1 4   ? 18.004  121.928 26.914  1.00 14.20 ? 4   ALA A CA  1 
ATOM   24    C  C   . ALA A  1 4   ? 19.407  122.508 26.982  1.00 12.60 ? 4   ALA A C   1 
ATOM   25    O  O   . ALA A  1 4   ? 19.574  123.728 27.127  1.00 12.05 ? 4   ALA A O   1 
ATOM   26    C  CB  . ALA A  1 4   ? 17.638  121.443 25.497  1.00 7.45  ? 4   ALA A CB  1 
ATOM   27    N  N   . VAL A  1 5   ? 20.411  121.639 26.919  1.00 10.69 ? 5   VAL A N   1 
ATOM   28    C  CA  . VAL A  1 5   ? 21.799  122.089 27.001  1.00 9.26  ? 5   VAL A CA  1 
ATOM   29    C  C   . VAL A  1 5   ? 22.646  121.207 26.105  1.00 11.30 ? 5   VAL A C   1 
ATOM   30    O  O   . VAL A  1 5   ? 22.278  120.072 25.808  1.00 13.44 ? 5   VAL A O   1 
ATOM   31    C  CB  . VAL A  1 5   ? 22.329  122.032 28.454  1.00 11.81 ? 5   VAL A CB  1 
ATOM   32    C  CG1 . VAL A  1 5   ? 22.233  120.620 29.005  1.00 9.05  ? 5   VAL A CG1 1 
ATOM   33    C  CG2 . VAL A  1 5   ? 23.794  122.615 28.569  1.00 7.39  ? 5   VAL A CG2 1 
ATOM   34    N  N   . CYS A  1 6   ? 23.768  121.738 25.657  1.00 8.65  ? 6   CYS A N   1 
ATOM   35    C  CA  . CYS A  1 6   ? 24.698  120.986 24.861  1.00 10.86 ? 6   CYS A CA  1 
ATOM   36    C  C   . CYS A  1 6   ? 26.107  121.387 25.281  1.00 8.77  ? 6   CYS A C   1 
ATOM   37    O  O   . CYS A  1 6   ? 26.409  122.569 25.401  1.00 11.69 ? 6   CYS A O   1 
ATOM   38    C  CB  . CYS A  1 6   ? 24.470  121.306 23.382  1.00 8.34  ? 6   CYS A CB  1 
ATOM   39    S  SG  . CYS A  1 6   ? 25.420  120.290 22.245  1.00 12.84 ? 6   CYS A SG  1 
ATOM   40    N  N   . VAL A  1 7   ? 26.960  120.403 25.510  1.00 9.74  ? 7   VAL A N   1 
ATOM   41    C  CA  . VAL A  1 7   ? 28.370  120.658 25.760  1.00 10.36 ? 7   VAL A CA  1 
ATOM   42    C  C   . VAL A  1 7   ? 29.128  120.353 24.472  1.00 12.67 ? 7   VAL A C   1 
ATOM   43    O  O   . VAL A  1 7   ? 29.173  119.214 24.031  1.00 13.38 ? 7   VAL A O   1 
ATOM   44    C  CB  . VAL A  1 7   ? 28.905  119.756 26.861  1.00 13.46 ? 7   VAL A CB  1 
ATOM   45    C  CG1 . VAL A  1 7   ? 30.441  119.859 26.944  1.00 15.37 ? 7   VAL A CG1 1 
ATOM   46    C  CG2 . VAL A  1 7   ? 28.261  120.106 28.186  1.00 13.05 ? 7   VAL A CG2 1 
ATOM   47    N  N   . LEU A  1 8   ? 29.708  121.373 23.860  1.00 11.46 ? 8   LEU A N   1 
ATOM   48    C  CA  . LEU A  1 8   ? 30.421  121.181 22.606  1.00 15.12 ? 8   LEU A CA  1 
ATOM   49    C  C   . LEU A  1 8   ? 31.876  120.831 22.868  1.00 14.84 ? 8   LEU A C   1 
ATOM   50    O  O   . LEU A  1 8   ? 32.558  121.533 23.605  1.00 13.75 ? 8   LEU A O   1 
ATOM   51    C  CB  . LEU A  1 8   ? 30.357  122.456 21.768  1.00 11.82 ? 8   LEU A CB  1 
ATOM   52    C  CG  . LEU A  1 8   ? 28.987  122.868 21.240  1.00 15.75 ? 8   LEU A CG  1 
ATOM   53    C  CD1 . LEU A  1 8   ? 29.067  124.334 20.799  1.00 14.81 ? 8   LEU A CD1 1 
ATOM   54    C  CD2 . LEU A  1 8   ? 28.566  121.958 20.081  1.00 9.62  ? 8   LEU A CD2 1 
ATOM   55    N  N   . LYS A  1 9   ? 32.352  119.760 22.251  1.00 14.07 ? 9   LYS A N   1 
ATOM   56    C  CA  . LYS A  1 9   ? 33.736  119.355 22.432  1.00 18.67 ? 9   LYS A CA  1 
ATOM   57    C  C   . LYS A  1 9   ? 34.269  118.668 21.180  1.00 18.87 ? 9   LYS A C   1 
ATOM   58    O  O   . LYS A  1 9   ? 33.504  118.077 20.399  1.00 16.29 ? 9   LYS A O   1 
ATOM   59    C  CB  . LYS A  1 9   ? 33.871  118.411 23.640  1.00 20.32 ? 9   LYS A CB  1 
ATOM   60    C  CG  . LYS A  1 9   ? 33.410  116.977 23.342  1.00 24.95 ? 9   LYS A CG  1 
ATOM   61    C  CD  . LYS A  1 9   ? 33.801  115.960 24.451  1.00 44.36 ? 9   LYS A CD  1 
ATOM   62    C  CE  . LYS A  1 9   ? 33.243  114.533 24.193  1.00 38.67 ? 9   LYS A CE  1 
ATOM   63    N  NZ  . LYS A  1 9   ? 33.725  113.926 22.902  1.00 40.05 ? 9   LYS A NZ  1 
ATOM   64    N  N   . GLY A  1 10  ? 35.585  118.733 20.997  1.00 21.31 ? 10  GLY A N   1 
ATOM   65    C  CA  . GLY A  1 10  ? 36.219  118.103 19.852  1.00 23.65 ? 10  GLY A CA  1 
ATOM   66    C  C   . GLY A  1 10  ? 37.672  117.768 20.125  1.00 24.55 ? 10  GLY A C   1 
ATOM   67    O  O   . GLY A  1 10  ? 38.111  117.832 21.263  1.00 24.37 ? 10  GLY A O   1 
ATOM   68    N  N   . ASP A  1 11  ? 38.407  117.443 19.065  1.00 28.71 ? 11  ASP A N   1 
ATOM   69    C  CA  . ASP A  1 11  ? 39.829  117.087 19.134  1.00 33.12 ? 11  ASP A CA  1 
ATOM   70    C  C   . ASP A  1 11  ? 40.779  118.199 19.567  1.00 33.14 ? 11  ASP A C   1 
ATOM   71    O  O   . ASP A  1 11  ? 41.806  117.938 20.198  1.00 37.07 ? 11  ASP A O   1 
ATOM   72    C  CB  . ASP A  1 11  ? 40.297  116.603 17.766  1.00 32.51 ? 11  ASP A CB  1 
ATOM   73    C  CG  . ASP A  1 11  ? 39.580  115.380 17.332  1.00 42.20 ? 11  ASP A CG  1 
ATOM   74    O  OD1 . ASP A  1 11  ? 39.184  114.605 18.230  1.00 45.19 ? 11  ASP A OD1 1 
ATOM   75    O  OD2 . ASP A  1 11  ? 39.401  115.194 16.109  1.00 50.12 ? 11  ASP A OD2 1 
ATOM   76    N  N   . GLY A  1 12  ? 40.466  119.429 19.186  1.00 30.55 ? 12  GLY A N   1 
ATOM   77    C  CA  . GLY A  1 12  ? 41.360  120.540 19.437  1.00 20.35 ? 12  GLY A CA  1 
ATOM   78    C  C   . GLY A  1 12  ? 40.893  121.379 20.599  1.00 22.59 ? 12  GLY A C   1 
ATOM   79    O  O   . GLY A  1 12  ? 40.254  120.874 21.523  1.00 24.32 ? 12  GLY A O   1 
ATOM   80    N  N   . PRO A  1 13  ? 41.203  122.679 20.546  1.00 21.26 ? 13  PRO A N   1 
ATOM   81    C  CA  . PRO A  1 13  ? 40.914  123.672 21.581  1.00 20.01 ? 13  PRO A CA  1 
ATOM   82    C  C   . PRO A  1 13  ? 39.468  124.201 21.595  1.00 19.91 ? 13  PRO A C   1 
ATOM   83    O  O   . PRO A  1 13  ? 39.072  124.822 22.577  1.00 18.99 ? 13  PRO A O   1 
ATOM   84    C  CB  . PRO A  1 13  ? 41.861  124.813 21.228  1.00 17.33 ? 13  PRO A CB  1 
ATOM   85    C  CG  . PRO A  1 13  ? 42.013  124.711 19.749  1.00 21.50 ? 13  PRO A CG  1 
ATOM   86    C  CD  . PRO A  1 13  ? 41.994  123.245 19.436  1.00 19.29 ? 13  PRO A CD  1 
ATOM   87    N  N   . VAL A  1 14  ? 38.695  123.977 20.540  1.00 18.75 ? 14  VAL A N   1 
ATOM   88    C  CA  . VAL A  1 14  ? 37.348  124.551 20.503  1.00 17.36 ? 14  VAL A CA  1 
ATOM   89    C  C   . VAL A  1 14  ? 36.455  123.801 21.456  1.00 14.19 ? 14  VAL A C   1 
ATOM   90    O  O   . VAL A  1 14  ? 36.336  122.595 21.373  1.00 13.42 ? 14  VAL A O   1 
ATOM   91    C  CB  . VAL A  1 14  ? 36.720  124.489 19.096  1.00 17.72 ? 14  VAL A CB  1 
ATOM   92    C  CG1 . VAL A  1 14  ? 35.263  124.939 19.149  1.00 17.08 ? 14  VAL A CG1 1 
ATOM   93    C  CG2 . VAL A  1 14  ? 37.518  125.331 18.100  1.00 13.06 ? 14  VAL A CG2 1 
ATOM   94    N  N   . GLN A  1 15  ? 35.828  124.520 22.369  1.00 17.82 ? 15  GLN A N   1 
ATOM   95    C  CA  . GLN A  1 15  ? 34.854  123.908 23.262  1.00 21.18 ? 15  GLN A CA  1 
ATOM   96    C  C   . GLN A  1 15  ? 33.882  124.955 23.762  1.00 18.14 ? 15  GLN A C   1 
ATOM   97    O  O   . GLN A  1 15  ? 34.143  126.148 23.668  1.00 19.22 ? 15  GLN A O   1 
ATOM   98    C  CB  . GLN A  1 15  ? 35.540  123.199 24.435  1.00 20.42 ? 15  GLN A CB  1 
ATOM   99    C  CG  . GLN A  1 15  ? 36.523  124.044 25.158  1.00 23.82 ? 15  GLN A CG  1 
ATOM   100   C  CD  . GLN A  1 15  ? 37.117  123.322 26.356  1.00 34.66 ? 15  GLN A CD  1 
ATOM   101   O  OE1 . GLN A  1 15  ? 38.058  122.531 26.221  1.00 38.10 ? 15  GLN A OE1 1 
ATOM   102   N  NE2 . GLN A  1 15  ? 36.557  123.577 27.534  1.00 31.64 ? 15  GLN A NE2 1 
ATOM   103   N  N   . GLY A  1 16  ? 32.738  124.513 24.267  1.00 16.41 ? 16  GLY A N   1 
ATOM   104   C  CA  . GLY A  1 16  ? 31.738  125.455 24.714  1.00 13.41 ? 16  GLY A CA  1 
ATOM   105   C  C   . GLY A  1 16  ? 30.498  124.807 25.256  1.00 13.94 ? 16  GLY A C   1 
ATOM   106   O  O   . GLY A  1 16  ? 30.369  123.583 25.273  1.00 13.22 ? 16  GLY A O   1 
ATOM   107   N  N   . ILE A  1 17  ? 29.584  125.663 25.698  1.00 13.95 ? 17  ILE A N   1 
ATOM   108   C  CA  . ILE A  1 17  ? 28.342  125.263 26.332  1.00 11.30 ? 17  ILE A CA  1 
ATOM   109   C  C   . ILE A  1 17  ? 27.237  126.129 25.765  1.00 14.83 ? 17  ILE A C   1 
ATOM   110   O  O   . ILE A  1 17  ? 27.332  127.360 25.768  1.00 11.66 ? 17  ILE A O   1 
ATOM   111   C  CB  . ILE A  1 17  ? 28.413  125.456 27.864  1.00 15.96 ? 17  ILE A CB  1 
ATOM   112   C  CG1 . ILE A  1 17  ? 29.412  124.465 28.468  1.00 15.72 ? 17  ILE A CG1 1 
ATOM   113   C  CG2 . ILE A  1 17  ? 27.037  125.313 28.503  1.00 11.46 ? 17  ILE A CG2 1 
ATOM   114   C  CD1 . ILE A  1 17  ? 29.436  124.463 29.983  1.00 17.61 ? 17  ILE A CD1 1 
ATOM   115   N  N   . ILE A  1 18  ? 26.198  125.480 25.249  1.00 13.17 ? 18  ILE A N   1 
ATOM   116   C  CA  . ILE A  1 18  ? 25.092  126.197 24.641  1.00 13.10 ? 18  ILE A CA  1 
ATOM   117   C  C   . ILE A  1 18  ? 23.832  125.777 25.345  1.00 13.39 ? 18  ILE A C   1 
ATOM   118   O  O   . ILE A  1 18  ? 23.605  124.583 25.524  1.00 14.33 ? 18  ILE A O   1 
ATOM   119   C  CB  . ILE A  1 18  ? 24.932  125.827 23.173  1.00 9.13  ? 18  ILE A CB  1 
ATOM   120   C  CG1 . ILE A  1 18  ? 26.198  126.169 22.383  1.00 12.91 ? 18  ILE A CG1 1 
ATOM   121   C  CG2 . ILE A  1 18  ? 23.709  126.507 22.605  1.00 10.24 ? 18  ILE A CG2 1 
ATOM   122   C  CD1 . ILE A  1 18  ? 26.455  127.650 22.203  1.00 12.27 ? 18  ILE A CD1 1 
ATOM   123   N  N   . ASN A  1 19  ? 23.022  126.754 25.735  1.00 13.30 ? 19  ASN A N   1 
ATOM   124   C  CA  . ASN A  1 19  ? 21.767  126.504 26.416  1.00 12.58 ? 19  ASN A CA  1 
ATOM   125   C  C   . ASN A  1 19  ? 20.614  126.818 25.493  1.00 16.21 ? 19  ASN A C   1 
ATOM   126   O  O   . ASN A  1 19  ? 20.733  127.671 24.613  1.00 16.47 ? 19  ASN A O   1 
ATOM   127   C  CB  . ASN A  1 19  ? 21.658  127.381 27.664  1.00 13.88 ? 19  ASN A CB  1 
ATOM   128   C  CG  . ASN A  1 19  ? 22.863  127.259 28.556  1.00 17.41 ? 19  ASN A CG  1 
ATOM   129   O  OD1 . ASN A  1 19  ? 22.920  126.374 29.409  1.00 15.74 ? 19  ASN A OD1 1 
ATOM   130   N  ND2 . ASN A  1 19  ? 23.852  128.138 28.357  1.00 15.49 ? 19  ASN A ND2 1 
ATOM   131   N  N   . PHE A  1 20  ? 19.494  126.137 25.711  1.00 15.15 ? 20  PHE A N   1 
ATOM   132   C  CA  . PHE A  1 20  ? 18.284  126.363 24.938  1.00 14.16 ? 20  PHE A CA  1 
ATOM   133   C  C   . PHE A  1 20  ? 17.118  126.515 25.908  1.00 16.51 ? 20  PHE A C   1 
ATOM   134   O  O   . PHE A  1 20  ? 17.016  125.795 26.907  1.00 16.16 ? 20  PHE A O   1 
ATOM   135   C  CB  . PHE A  1 20  ? 17.971  125.172 24.039  1.00 10.27 ? 20  PHE A CB  1 
ATOM   136   C  CG  . PHE A  1 20  ? 19.057  124.809 23.079  1.00 12.94 ? 20  PHE A CG  1 
ATOM   137   C  CD1 . PHE A  1 20  ? 20.179  124.101 23.505  1.00 12.76 ? 20  PHE A CD1 1 
ATOM   138   C  CD2 . PHE A  1 20  ? 18.943  125.141 21.736  1.00 10.57 ? 20  PHE A CD2 1 
ATOM   139   C  CE1 . PHE A  1 20  ? 21.159  123.741 22.613  1.00 10.44 ? 20  PHE A CE1 1 
ATOM   140   C  CE2 . PHE A  1 20  ? 19.928  124.791 20.842  1.00 9.79  ? 20  PHE A CE2 1 
ATOM   141   C  CZ  . PHE A  1 20  ? 21.037  124.097 21.278  1.00 9.40  ? 20  PHE A CZ  1 
ATOM   142   N  N   . GLU A  1 21  ? 16.230  127.444 25.602  1.00 16.02 ? 21  GLU A N   1 
ATOM   143   C  CA  . GLU A  1 21  ? 15.023  127.607 26.380  1.00 20.48 ? 21  GLU A CA  1 
ATOM   144   C  C   . GLU A  1 21  ? 13.830  127.934 25.484  1.00 16.45 ? 21  GLU A C   1 
ATOM   145   O  O   . GLU A  1 21  ? 13.925  128.741 24.562  1.00 15.99 ? 21  GLU A O   1 
ATOM   146   C  CB  . GLU A  1 21  ? 15.208  128.666 27.476  1.00 21.18 ? 21  GLU A CB  1 
ATOM   147   C  CG  . GLU A  1 21  ? 13.957  128.882 28.315  1.00 28.16 ? 21  GLU A CG  1 
ATOM   148   C  CD  . GLU A  1 21  ? 14.209  129.749 29.545  1.00 35.44 ? 21  GLU A CD  1 
ATOM   149   O  OE1 . GLU A  1 21  ? 15.166  129.470 30.298  1.00 37.83 ? 21  GLU A OE1 1 
ATOM   150   O  OE2 . GLU A  1 21  ? 13.447  130.712 29.756  1.00 38.71 ? 21  GLU A OE2 1 
ATOM   151   N  N   . GLN A  1 22  ? 12.717  127.268 25.758  1.00 16.23 ? 22  GLN A N   1 
ATOM   152   C  CA  . GLN A  1 22  ? 11.493  127.452 25.001  1.00 18.06 ? 22  GLN A CA  1 
ATOM   153   C  C   . GLN A  1 22  ? 10.324  127.479 25.986  1.00 18.78 ? 22  GLN A C   1 
ATOM   154   O  O   . GLN A  1 22  ? 9.863   126.430 26.415  1.00 19.36 ? 22  GLN A O   1 
ATOM   155   C  CB  . GLN A  1 22  ? 11.321  126.307 24.009  1.00 14.04 ? 22  GLN A CB  1 
ATOM   156   C  CG  . GLN A  1 22  ? 10.325  126.612 22.907  1.00 16.50 ? 22  GLN A CG  1 
ATOM   157   C  CD  . GLN A  1 22  ? 10.034  125.415 22.031  1.00 16.28 ? 22  GLN A CD  1 
ATOM   158   O  OE1 . GLN A  1 22  ? 10.392  124.290 22.372  1.00 16.95 ? 22  GLN A OE1 1 
ATOM   159   N  NE2 . GLN A  1 22  ? 9.360   125.648 20.895  1.00 15.84 ? 22  GLN A NE2 1 
ATOM   160   N  N   . LYS A  1 23  ? 9.869   128.674 26.361  1.00 23.62 ? 23  LYS A N   1 
ATOM   161   C  CA  . LYS A  1 23  ? 8.767   128.822 27.327  1.00 23.13 ? 23  LYS A CA  1 
ATOM   162   C  C   . LYS A  1 23  ? 7.454   128.219 26.828  1.00 20.24 ? 23  LYS A C   1 
ATOM   163   O  O   . LYS A  1 23  ? 6.760   127.509 27.540  1.00 27.19 ? 23  LYS A O   1 
ATOM   164   C  CB  . LYS A  1 23  ? 8.555   130.300 27.647  1.00 27.38 ? 23  LYS A CB  1 
ATOM   165   C  CG  . LYS A  1 23  ? 9.604   130.875 28.576  1.00 35.62 ? 23  LYS A CG  1 
ATOM   166   C  CD  . LYS A  1 23  ? 9.516   132.395 28.655  1.00 51.31 ? 23  LYS A CD  1 
ATOM   167   C  CE  . LYS A  1 23  ? 10.543  132.956 29.645  1.00 49.33 ? 23  LYS A CE  1 
ATOM   168   N  NZ  . LYS A  1 23  ? 10.418  134.434 29.813  1.00 59.30 ? 23  LYS A NZ  1 
ATOM   169   N  N   . GLU A  1 24  ? 7.121   128.496 25.584  1.00 19.73 ? 24  GLU A N   1 
ATOM   170   C  CA  . GLU A  1 24  ? 5.885   127.997 25.024  1.00 18.74 ? 24  GLU A CA  1 
ATOM   171   C  C   . GLU A  1 24  ? 6.184   126.978 23.945  1.00 17.64 ? 24  GLU A C   1 
ATOM   172   O  O   . GLU A  1 24  ? 7.044   127.216 23.088  1.00 16.04 ? 24  GLU A O   1 
ATOM   173   C  CB  . GLU A  1 24  ? 5.065   129.162 24.461  1.00 21.55 ? 24  GLU A CB  1 
ATOM   174   C  CG  . GLU A  1 24  ? 4.647   130.183 25.517  1.00 22.38 ? 24  GLU A CG  1 
ATOM   175   C  CD  . GLU A  1 24  ? 3.842   129.536 26.639  1.00 26.54 ? 24  GLU A CD  1 
ATOM   176   O  OE1 . GLU A  1 24  ? 3.132   128.543 26.366  1.00 27.75 ? 24  GLU A OE1 1 
ATOM   177   O  OE2 . GLU A  1 24  ? 3.924   130.009 27.795  1.00 30.91 ? 24  GLU A OE2 1 
ATOM   178   N  N   . SER A  1 25  ? 5.470   125.852 23.982  1.00 15.84 ? 25  SER A N   1 
ATOM   179   C  CA  . SER A  1 25  ? 5.672   124.779 23.013  1.00 16.61 ? 25  SER A CA  1 
ATOM   180   C  C   . SER A  1 25  ? 5.459   125.230 21.570  1.00 17.00 ? 25  SER A C   1 
ATOM   181   O  O   . SER A  1 25  ? 5.990   124.624 20.645  1.00 18.23 ? 25  SER A O   1 
ATOM   182   C  CB  . SER A  1 25  ? 4.769   123.594 23.325  1.00 17.87 ? 25  SER A CB  1 
ATOM   183   O  OG  . SER A  1 25  ? 3.412   123.928 23.118  1.00 16.35 ? 25  SER A OG  1 
ATOM   184   N  N   . ASN A  1 26  ? 4.674   126.286 21.384  1.00 18.20 ? 26  ASN A N   1 
ATOM   185   C  CA  . ASN A  1 26  ? 4.465   126.856 20.053  1.00 17.28 ? 26  ASN A CA  1 
ATOM   186   C  C   . ASN A  1 26  ? 5.154   128.210 19.916  1.00 15.99 ? 26  ASN A C   1 
ATOM   187   O  O   . ASN A  1 26  ? 4.788   129.027 19.081  1.00 22.06 ? 26  ASN A O   1 
ATOM   188   C  CB  . ASN A  1 26  ? 2.968   126.989 19.749  1.00 16.25 ? 26  ASN A CB  1 
ATOM   189   C  CG  . ASN A  1 26  ? 2.283   128.017 20.639  1.00 19.67 ? 26  ASN A CG  1 
ATOM   190   O  OD1 . ASN A  1 26  ? 2.644   128.180 21.808  1.00 19.87 ? 26  ASN A OD1 1 
ATOM   191   N  ND2 . ASN A  1 26  ? 1.297   128.729 20.080  1.00 16.75 ? 26  ASN A ND2 1 
ATOM   192   N  N   . GLY A  1 27  ? 6.151   128.454 20.753  1.00 19.94 ? 27  GLY A N   1 
ATOM   193   C  CA  . GLY A  1 27  ? 6.896   129.698 20.692  1.00 21.34 ? 27  GLY A CA  1 
ATOM   194   C  C   . GLY A  1 27  ? 8.347   129.461 20.317  1.00 21.28 ? 27  GLY A C   1 
ATOM   195   O  O   . GLY A  1 27  ? 8.778   128.318 20.195  1.00 18.07 ? 27  GLY A O   1 
ATOM   196   N  N   . PRO A  1 28  ? 9.107   130.547 20.140  1.00 21.59 ? 28  PRO A N   1 
ATOM   197   C  CA  . PRO A  1 28  ? 10.511  130.487 19.718  1.00 20.13 ? 28  PRO A CA  1 
ATOM   198   C  C   . PRO A  1 28  ? 11.424  129.869 20.766  1.00 16.48 ? 28  PRO A C   1 
ATOM   199   O  O   . PRO A  1 28  ? 11.132  129.858 21.961  1.00 15.55 ? 28  PRO A O   1 
ATOM   200   C  CB  . PRO A  1 28  ? 10.892  131.966 19.539  1.00 21.96 ? 28  PRO A CB  1 
ATOM   201   C  CG  . PRO A  1 28  ? 9.573   132.707 19.462  1.00 28.78 ? 28  PRO A CG  1 
ATOM   202   C  CD  . PRO A  1 28  ? 8.658   131.931 20.358  1.00 24.01 ? 28  PRO A CD  1 
ATOM   203   N  N   . VAL A  1 29  ? 12.557  129.370 20.297  1.00 21.62 ? 29  VAL A N   1 
ATOM   204   C  CA  . VAL A  1 29  ? 13.592  128.857 21.168  1.00 15.29 ? 29  VAL A CA  1 
ATOM   205   C  C   . VAL A  1 29  ? 14.685  129.906 21.318  1.00 14.82 ? 29  VAL A C   1 
ATOM   206   O  O   . VAL A  1 29  ? 15.231  130.386 20.331  1.00 16.27 ? 29  VAL A O   1 
ATOM   207   C  CB  . VAL A  1 29  ? 14.232  127.601 20.593  1.00 13.88 ? 29  VAL A CB  1 
ATOM   208   C  CG1 . VAL A  1 29  ? 15.349  127.107 21.536  1.00 11.90 ? 29  VAL A CG1 1 
ATOM   209   C  CG2 . VAL A  1 29  ? 13.186  126.524 20.364  1.00 16.74 ? 29  VAL A CG2 1 
ATOM   210   N  N   . LYS A  1 30  ? 15.015  130.260 22.554  1.00 17.29 ? 30  LYS A N   1 
ATOM   211   C  CA  . LYS A  1 30  ? 16.152  131.139 22.783  1.00 15.78 ? 30  LYS A CA  1 
ATOM   212   C  C   . LYS A  1 30  ? 17.409  130.275 22.950  1.00 17.95 ? 30  LYS A C   1 
ATOM   213   O  O   . LYS A  1 30  ? 17.378  129.261 23.642  1.00 15.31 ? 30  LYS A O   1 
ATOM   214   C  CB  . LYS A  1 30  ? 15.908  132.038 23.990  1.00 17.94 ? 30  LYS A CB  1 
ATOM   215   C  CG  . LYS A  1 30  ? 17.105  132.907 24.377  1.00 28.82 ? 30  LYS A CG  1 
ATOM   216   C  CD  . LYS A  1 30  ? 16.960  133.497 25.797  1.00 42.12 ? 30  LYS A CD  1 
ATOM   217   C  CE  . LYS A  1 30  ? 18.122  134.463 26.145  1.00 45.78 ? 30  LYS A CE  1 
ATOM   218   N  NZ  . LYS A  1 30  ? 18.041  135.048 27.526  1.00 40.80 ? 30  LYS A NZ  1 
ATOM   219   N  N   . VAL A  1 31  ? 18.489  130.653 22.265  1.00 18.23 ? 31  VAL A N   1 
ATOM   220   C  CA  . VAL A  1 31  ? 19.745  129.904 22.282  1.00 18.40 ? 31  VAL A CA  1 
ATOM   221   C  C   . VAL A  1 31  ? 20.911  130.812 22.710  1.00 20.62 ? 31  VAL A C   1 
ATOM   222   O  O   . VAL A  1 31  ? 21.189  131.823 22.059  1.00 17.88 ? 31  VAL A O   1 
ATOM   223   C  CB  . VAL A  1 31  ? 20.059  129.355 20.891  1.00 16.68 ? 31  VAL A CB  1 
ATOM   224   C  CG1 . VAL A  1 31  ? 21.233  128.430 20.944  1.00 15.05 ? 31  VAL A CG1 1 
ATOM   225   C  CG2 . VAL A  1 31  ? 18.826  128.644 20.288  1.00 17.52 ? 31  VAL A CG2 1 
ATOM   226   N  N   . TRP A  1 32  ? 21.609  130.451 23.786  1.00 17.25 ? 32  TRP A N   1 
ATOM   227   C  CA  . TRP A  1 32  ? 22.705  131.286 24.270  1.00 17.02 ? 32  TRP A CA  1 
ATOM   228   C  C   . TRP A  1 32  ? 23.812  130.490 24.934  1.00 17.70 ? 32  TRP A C   1 
ATOM   229   O  O   . TRP A  1 32  ? 23.584  129.419 25.492  1.00 18.39 ? 32  TRP A O   1 
ATOM   230   C  CB  . TRP A  1 32  ? 22.178  132.352 25.231  1.00 18.86 ? 32  TRP A CB  1 
ATOM   231   C  CG  . TRP A  1 32  ? 21.909  131.833 26.605  1.00 21.97 ? 32  TRP A CG  1 
ATOM   232   C  CD1 . TRP A  1 32  ? 22.742  131.908 27.677  1.00 24.02 ? 32  TRP A CD1 1 
ATOM   233   C  CD2 . TRP A  1 32  ? 20.741  131.144 27.055  1.00 21.77 ? 32  TRP A CD2 1 
ATOM   234   N  NE1 . TRP A  1 32  ? 22.167  131.319 28.768  1.00 26.75 ? 32  TRP A NE1 1 
ATOM   235   C  CE2 . TRP A  1 32  ? 20.933  130.846 28.418  1.00 22.16 ? 32  TRP A CE2 1 
ATOM   236   C  CE3 . TRP A  1 32  ? 19.545  130.758 26.441  1.00 23.62 ? 32  TRP A CE3 1 
ATOM   237   C  CZ2 . TRP A  1 32  ? 19.983  130.173 29.179  1.00 25.84 ? 32  TRP A CZ2 1 
ATOM   238   C  CZ3 . TRP A  1 32  ? 18.602  130.083 27.190  1.00 24.93 ? 32  TRP A CZ3 1 
ATOM   239   C  CH2 . TRP A  1 32  ? 18.823  129.800 28.553  1.00 28.44 ? 32  TRP A CH2 1 
ATOM   240   N  N   . GLY A  1 33  ? 25.023  131.012 24.860  1.00 20.03 ? 33  GLY A N   1 
ATOM   241   C  CA  . GLY A  1 33  ? 26.147  130.407 25.550  1.00 16.38 ? 33  GLY A CA  1 
ATOM   242   C  C   . GLY A  1 33  ? 27.457  130.978 25.049  1.00 18.86 ? 33  GLY A C   1 
ATOM   243   O  O   . GLY A  1 33  ? 27.506  132.105 24.557  1.00 21.97 ? 33  GLY A O   1 
ATOM   244   N  N   . SER A  1 34  ? 28.517  130.191 25.140  1.00 19.24 ? 34  SER A N   1 
ATOM   245   C  CA  . SER A  1 34  ? 29.830  130.671 24.763  1.00 19.42 ? 34  SER A CA  1 
ATOM   246   C  C   . SER A  1 34  ? 30.680  129.555 24.225  1.00 15.79 ? 34  SER A C   1 
ATOM   247   O  O   . SER A  1 34  ? 30.658  128.450 24.738  1.00 19.09 ? 34  SER A O   1 
ATOM   248   C  CB  . SER A  1 34  ? 30.520  131.289 25.974  1.00 21.94 ? 34  SER A CB  1 
ATOM   249   O  OG  . SER A  1 34  ? 31.835  131.674 25.636  1.00 24.27 ? 34  SER A OG  1 
ATOM   250   N  N   . ILE A  1 35  ? 31.434  129.852 23.180  1.00 18.55 ? 35  ILE A N   1 
ATOM   251   C  CA  . ILE A  1 35  ? 32.345  128.894 22.596  1.00 16.14 ? 35  ILE A CA  1 
ATOM   252   C  C   . ILE A  1 35  ? 33.708  129.561 22.562  1.00 19.50 ? 35  ILE A C   1 
ATOM   253   O  O   . ILE A  1 35  ? 33.809  130.723 22.194  1.00 18.20 ? 35  ILE A O   1 
ATOM   254   C  CB  . ILE A  1 35  ? 31.926  128.517 21.168  1.00 13.63 ? 35  ILE A CB  1 
ATOM   255   C  CG1 . ILE A  1 35  ? 30.420  128.202 21.108  1.00 14.90 ? 35  ILE A CG1 1 
ATOM   256   C  CG2 . ILE A  1 35  ? 32.708  127.343 20.696  1.00 14.05 ? 35  ILE A CG2 1 
ATOM   257   C  CD1 . ILE A  1 35  ? 29.967  127.719 19.735  1.00 12.75 ? 35  ILE A CD1 1 
ATOM   258   N  N   . LYS A  1 36  ? 34.751  128.845 22.968  1.00 15.19 ? 36  LYS A N   1 
ATOM   259   C  CA  . LYS A  1 36  ? 36.091  129.418 22.914  1.00 21.75 ? 36  LYS A CA  1 
ATOM   260   C  C   . LYS A  1 36  ? 37.003  128.560 22.058  1.00 20.05 ? 36  LYS A C   1 
ATOM   261   O  O   . LYS A  1 36  ? 36.616  127.445 21.663  1.00 17.39 ? 36  LYS A O   1 
ATOM   262   C  CB  . LYS A  1 36  ? 36.671  129.628 24.327  1.00 22.04 ? 36  LYS A CB  1 
ATOM   263   C  CG  . LYS A  1 36  ? 36.918  128.356 25.129  1.00 19.66 ? 36  LYS A CG  1 
ATOM   264   C  CD  . LYS A  1 36  ? 36.980  128.703 26.615  1.00 31.13 ? 36  LYS A CD  1 
ATOM   265   C  CE  . LYS A  1 36  ? 37.451  127.530 27.469  1.00 37.94 ? 36  LYS A CE  1 
ATOM   266   N  NZ  . LYS A  1 36  ? 37.521  127.905 28.916  1.00 36.60 ? 36  LYS A NZ  1 
ATOM   267   N  N   . GLY A  1 37  ? 38.202  129.081 21.770  1.00 18.87 ? 37  GLY A N   1 
ATOM   268   C  CA  . GLY A  1 37  ? 39.198  128.359 20.996  1.00 15.06 ? 37  GLY A CA  1 
ATOM   269   C  C   . GLY A  1 37  ? 39.060  128.534 19.494  1.00 16.20 ? 37  GLY A C   1 
ATOM   270   O  O   . GLY A  1 37  ? 39.695  127.799 18.740  1.00 15.20 ? 37  GLY A O   1 
ATOM   271   N  N   . LEU A  1 38  ? 38.243  129.501 19.059  1.00 15.68 ? 38  LEU A N   1 
ATOM   272   C  CA  . LEU A  1 38  ? 37.913  129.670 17.629  1.00 16.55 ? 38  LEU A CA  1 
ATOM   273   C  C   . LEU A  1 38  ? 38.751  130.732 16.918  1.00 18.34 ? 38  LEU A C   1 
ATOM   274   O  O   . LEU A  1 38  ? 39.137  131.745 17.520  1.00 17.69 ? 38  LEU A O   1 
ATOM   275   C  CB  . LEU A  1 38  ? 36.443  130.071 17.459  1.00 15.29 ? 38  LEU A CB  1 
ATOM   276   C  CG  . LEU A  1 38  ? 35.387  129.083 17.934  1.00 16.80 ? 38  LEU A CG  1 
ATOM   277   C  CD1 . LEU A  1 38  ? 34.079  129.798 18.199  1.00 16.13 ? 38  LEU A CD1 1 
ATOM   278   C  CD2 . LEU A  1 38  ? 35.233  128.004 16.880  1.00 16.10 ? 38  LEU A CD2 1 
ATOM   279   N  N   . THR A  1 39  ? 39.002  130.517 15.631  1.00 14.22 ? 39  THR A N   1 
ATOM   280   C  CA  . THR A  1 39  ? 39.595  131.568 14.812  1.00 19.92 ? 39  THR A CA  1 
ATOM   281   C  C   . THR A  1 39  ? 38.601  132.695 14.783  1.00 18.89 ? 39  THR A C   1 
ATOM   282   O  O   . THR A  1 39  ? 37.403  132.448 14.703  1.00 21.44 ? 39  THR A O   1 
ATOM   283   C  CB  . THR A  1 39  ? 39.880  131.106 13.363  1.00 24.05 ? 39  THR A CB  1 
ATOM   284   O  OG1 . THR A  1 39  ? 38.694  130.534 12.776  1.00 22.88 ? 39  THR A OG1 1 
ATOM   285   C  CG2 . THR A  1 39  ? 40.960  130.075 13.360  1.00 18.23 ? 39  THR A CG2 1 
ATOM   286   N  N   . GLU A  1 40  ? 39.096  133.926 14.879  1.00 21.93 ? 40  GLU A N   1 
ATOM   287   C  CA  . GLU A  1 40  ? 38.265  135.129 14.828  1.00 20.78 ? 40  GLU A CA  1 
ATOM   288   C  C   . GLU A  1 40  ? 37.401  135.167 13.569  1.00 18.98 ? 40  GLU A C   1 
ATOM   289   O  O   . GLU A  1 40  ? 37.830  134.760 12.493  1.00 19.91 ? 40  GLU A O   1 
ATOM   290   C  CB  . GLU A  1 40  ? 39.142  136.389 14.874  1.00 23.43 ? 40  GLU A CB  1 
ATOM   291   C  CG  . GLU A  1 40  ? 38.366  137.713 14.966  1.00 23.19 ? 40  GLU A CG  1 
ATOM   292   C  CD  . GLU A  1 40  ? 39.295  138.922 15.097  1.00 35.43 ? 40  GLU A CD  1 
ATOM   293   O  OE1 . GLU A  1 40  ? 40.515  138.765 14.846  1.00 35.28 ? 40  GLU A OE1 1 
ATOM   294   O  OE2 . GLU A  1 40  ? 38.809  140.020 15.458  1.00 32.06 ? 40  GLU A OE2 1 
ATOM   295   N  N   . GLY A  1 41  ? 36.171  135.641 13.719  1.00 21.68 ? 41  GLY A N   1 
ATOM   296   C  CA  . GLY A  1 41  ? 35.254  135.662 12.602  1.00 21.37 ? 41  GLY A CA  1 
ATOM   297   C  C   . GLY A  1 41  ? 34.102  134.672 12.712  1.00 22.79 ? 41  GLY A C   1 
ATOM   298   O  O   . GLY A  1 41  ? 33.738  134.202 13.811  1.00 21.09 ? 41  GLY A O   1 
ATOM   299   N  N   . LEU A  1 42  ? 33.561  134.349 11.543  1.00 20.87 ? 42  LEU A N   1 
ATOM   300   C  CA  . LEU A  1 42  ? 32.312  133.616 11.385  1.00 22.26 ? 42  LEU A CA  1 
ATOM   301   C  C   . LEU A  1 42  ? 32.516  132.117 11.359  1.00 17.75 ? 42  LEU A C   1 
ATOM   302   O  O   . LEU A  1 42  ? 33.438  131.620 10.723  1.00 17.51 ? 42  LEU A O   1 
ATOM   303   C  CB  . LEU A  1 42  ? 31.635  134.042 10.078  1.00 18.75 ? 42  LEU A CB  1 
ATOM   304   C  CG  . LEU A  1 42  ? 30.491  135.053 10.159  1.00 25.99 ? 42  LEU A CG  1 
ATOM   305   C  CD1 . LEU A  1 42  ? 30.875  136.264 10.988  1.00 29.82 ? 42  LEU A CD1 1 
ATOM   306   C  CD2 . LEU A  1 42  ? 30.054  135.476 8.756   1.00 23.99 ? 42  LEU A CD2 1 
ATOM   307   N  N   . HIS A  1 43  ? 31.632  131.408 12.052  1.00 16.27 ? 43  HIS A N   1 
ATOM   308   C  CA  . HIS A  1 43  ? 31.664  129.956 12.131  1.00 16.40 ? 43  HIS A CA  1 
ATOM   309   C  C   . HIS A  1 43  ? 30.262  129.357 11.986  1.00 14.61 ? 43  HIS A C   1 
ATOM   310   O  O   . HIS A  1 43  ? 29.345  129.716 12.731  1.00 13.06 ? 43  HIS A O   1 
ATOM   311   C  CB  . HIS A  1 43  ? 32.255  129.529 13.475  1.00 15.23 ? 43  HIS A CB  1 
ATOM   312   C  CG  . HIS A  1 43  ? 33.721  129.795 13.592  1.00 17.69 ? 43  HIS A CG  1 
ATOM   313   N  ND1 . HIS A  1 43  ? 34.670  128.914 13.122  1.00 17.91 ? 43  HIS A ND1 1 
ATOM   314   C  CD2 . HIS A  1 43  ? 34.401  130.848 14.106  1.00 16.41 ? 43  HIS A CD2 1 
ATOM   315   C  CE1 . HIS A  1 43  ? 35.874  129.409 13.350  1.00 19.93 ? 43  HIS A CE1 1 
ATOM   316   N  NE2 . HIS A  1 43  ? 35.738  130.582 13.943  1.00 20.87 ? 43  HIS A NE2 1 
ATOM   317   N  N   . GLY A  1 44  ? 30.111  128.443 11.034  1.00 14.35 ? 44  GLY A N   1 
ATOM   318   C  CA  . GLY A  1 44  ? 28.853  127.746 10.820  1.00 13.70 ? 44  GLY A CA  1 
ATOM   319   C  C   . GLY A  1 44  ? 28.388  127.071 12.097  1.00 13.19 ? 44  GLY A C   1 
ATOM   320   O  O   . GLY A  1 44  ? 29.198  126.623 12.904  1.00 13.15 ? 44  GLY A O   1 
ATOM   321   N  N   . PHE A  1 45  ? 27.078  126.988 12.268  1.00 10.85 ? 45  PHE A N   1 
ATOM   322   C  CA  . PHE A  1 45  ? 26.496  126.612 13.540  1.00 12.27 ? 45  PHE A CA  1 
ATOM   323   C  C   . PHE A  1 45  ? 25.190  125.887 13.188  1.00 11.43 ? 45  PHE A C   1 
ATOM   324   O  O   . PHE A  1 45  ? 24.208  126.524 12.816  1.00 11.79 ? 45  PHE A O   1 
ATOM   325   C  CB  . PHE A  1 45  ? 26.274  127.881 14.364  1.00 9.95  ? 45  PHE A CB  1 
ATOM   326   C  CG  . PHE A  1 45  ? 25.877  127.640 15.799  1.00 9.12  ? 45  PHE A CG  1 
ATOM   327   C  CD1 . PHE A  1 45  ? 26.746  127.034 16.682  1.00 12.80 ? 45  PHE A CD1 1 
ATOM   328   C  CD2 . PHE A  1 45  ? 24.651  128.082 16.275  1.00 9.65  ? 45  PHE A CD2 1 
ATOM   329   C  CE1 . PHE A  1 45  ? 26.390  126.838 18.009  1.00 10.15 ? 45  PHE A CE1 1 
ATOM   330   C  CE2 . PHE A  1 45  ? 24.291  127.886 17.611  1.00 11.71 ? 45  PHE A CE2 1 
ATOM   331   C  CZ  . PHE A  1 45  ? 25.165  127.265 18.469  1.00 10.52 ? 45  PHE A CZ  1 
ATOM   332   N  N   . HIS A  1 46  ? 25.218  124.556 13.279  1.00 9.02  ? 46  HIS A N   1 
ATOM   333   C  CA  . HIS A  1 46  ? 24.169  123.681 12.755  1.00 9.30  ? 46  HIS A CA  1 
ATOM   334   C  C   . HIS A  1 46  ? 23.665  122.666 13.760  1.00 11.44 ? 46  HIS A C   1 
ATOM   335   O  O   . HIS A  1 46  ? 24.425  122.171 14.614  1.00 10.40 ? 46  HIS A O   1 
ATOM   336   C  CB  . HIS A  1 46  ? 24.691  122.897 11.552  1.00 11.39 ? 46  HIS A CB  1 
ATOM   337   C  CG  . HIS A  1 46  ? 25.270  123.764 10.484  1.00 11.98 ? 46  HIS A CG  1 
ATOM   338   N  ND1 . HIS A  1 46  ? 26.392  123.416 9.772   1.00 16.62 ? 46  HIS A ND1 1 
ATOM   339   C  CD2 . HIS A  1 46  ? 24.906  124.988 10.039  1.00 14.11 ? 46  HIS A CD2 1 
ATOM   340   C  CE1 . HIS A  1 46  ? 26.680  124.374 8.911   1.00 15.98 ? 46  HIS A CE1 1 
ATOM   341   N  NE2 . HIS A  1 46  ? 25.803  125.350 9.066   1.00 12.63 ? 46  HIS A NE2 1 
ATOM   342   N  N   . VAL A  1 47  ? 22.380  122.354 13.662  1.00 7.52  ? 47  VAL A N   1 
ATOM   343   C  CA  . VAL A  1 47  ? 21.889  121.136 14.266  1.00 8.92  ? 47  VAL A CA  1 
ATOM   344   C  C   . VAL A  1 47  ? 21.962  120.038 13.209  1.00 9.32  ? 47  VAL A C   1 
ATOM   345   O  O   . VAL A  1 47  ? 21.309  120.132 12.170  1.00 10.20 ? 47  VAL A O   1 
ATOM   346   C  CB  . VAL A  1 47  ? 20.435  121.292 14.809  1.00 9.71  ? 47  VAL A CB  1 
ATOM   347   C  CG1 . VAL A  1 47  ? 19.886  119.951 15.311  1.00 8.66  ? 47  VAL A CG1 1 
ATOM   348   C  CG2 . VAL A  1 47  ? 20.404  122.307 15.926  1.00 8.45  ? 47  VAL A CG2 1 
ATOM   349   N  N   . HIS A  1 48  ? 22.763  119.003 13.459  1.00 8.94  ? 48  HIS A N   1 
ATOM   350   C  CA  . HIS A  1 48  ? 22.848  117.849 12.550  1.00 9.61  ? 48  HIS A CA  1 
ATOM   351   C  C   . HIS A  1 48  ? 21.881  116.749 12.981  1.00 9.84  ? 48  HIS A C   1 
ATOM   352   O  O   . HIS A  1 48  ? 21.457  116.741 14.127  1.00 8.59  ? 48  HIS A O   1 
ATOM   353   C  CB  . HIS A  1 48  ? 24.275  117.311 12.500  1.00 10.05 ? 48  HIS A CB  1 
ATOM   354   C  CG  . HIS A  1 48  ? 25.205  118.144 11.671  1.00 10.49 ? 48  HIS A CG  1 
ATOM   355   N  ND1 . HIS A  1 48  ? 25.804  117.671 10.525  1.00 15.87 ? 48  HIS A ND1 1 
ATOM   356   C  CD2 . HIS A  1 48  ? 25.633  119.417 11.819  1.00 10.41 ? 48  HIS A CD2 1 
ATOM   357   C  CE1 . HIS A  1 48  ? 26.560  118.618 10.000  1.00 14.86 ? 48  HIS A CE1 1 
ATOM   358   N  NE2 . HIS A  1 48  ? 26.481  119.683 10.771  1.00 14.48 ? 48  HIS A NE2 1 
ATOM   359   N  N   . GLU A  1 49  ? 21.545  115.826 12.075  1.00 11.05 ? 49  GLU A N   1 
ATOM   360   C  CA  . GLU A  1 49  ? 20.407  114.913 12.274  1.00 11.58 ? 49  GLU A CA  1 
ATOM   361   C  C   . GLU A  1 49  ? 20.546  113.939 13.457  1.00 13.03 ? 49  GLU A C   1 
ATOM   362   O  O   . GLU A  1 49  ? 19.608  113.748 14.239  1.00 10.54 ? 49  GLU A O   1 
ATOM   363   C  CB  . GLU A  1 49  ? 20.110  114.121 11.004  1.00 11.85 ? 49  GLU A CB  1 
ATOM   364   C  CG  . GLU A  1 49  ? 18.792  113.328 11.064  1.00 13.90 ? 49  GLU A CG  1 
ATOM   365   C  CD  . GLU A  1 49  ? 18.458  112.573 9.760   1.00 14.90 ? 49  GLU A CD  1 
ATOM   366   O  OE1 . GLU A  1 49  ? 19.179  112.697 8.756   1.00 15.56 ? 49  GLU A OE1 1 
ATOM   367   O  OE2 . GLU A  1 49  ? 17.458  111.840 9.742   1.00 20.30 ? 49  GLU A OE2 1 
ATOM   368   N  N   . PHE A  1 50  ? 21.713  113.331 13.598  1.00 10.47 ? 50  PHE A N   1 
ATOM   369   C  CA  . PHE A  1 50  ? 21.839  112.243 14.559  1.00 15.00 ? 50  PHE A CA  1 
ATOM   370   C  C   . PHE A  1 50  ? 22.640  112.596 15.804  1.00 15.10 ? 50  PHE A C   1 
ATOM   371   O  O   . PHE A  1 50  ? 23.725  113.181 15.701  1.00 16.93 ? 50  PHE A O   1 
ATOM   372   C  CB  . PHE A  1 50  ? 22.448  111.021 13.873  1.00 14.82 ? 50  PHE A CB  1 
ATOM   373   C  CG  . PHE A  1 50  ? 21.708  110.604 12.652  1.00 15.69 ? 50  PHE A CG  1 
ATOM   374   C  CD1 . PHE A  1 50  ? 20.369  110.279 12.728  1.00 17.74 ? 50  PHE A CD1 1 
ATOM   375   C  CD2 . PHE A  1 50  ? 22.342  110.541 11.431  1.00 17.14 ? 50  PHE A CD2 1 
ATOM   376   C  CE1 . PHE A  1 50  ? 19.669  109.889 11.612  1.00 17.30 ? 50  PHE A CE1 1 
ATOM   377   C  CE2 . PHE A  1 50  ? 21.654  110.155 10.300  1.00 18.60 ? 50  PHE A CE2 1 
ATOM   378   C  CZ  . PHE A  1 50  ? 20.308  109.830 10.393  1.00 20.35 ? 50  PHE A CZ  1 
ATOM   379   N  N   . GLY A  1 51  ? 22.105  112.226 16.972  1.00 10.02 ? 51  GLY A N   1 
ATOM   380   C  CA  . GLY A  1 51  ? 22.836  112.309 18.224  1.00 9.26  ? 51  GLY A CA  1 
ATOM   381   C  C   . GLY A  1 51  ? 23.805  111.134 18.377  1.00 14.13 ? 51  GLY A C   1 
ATOM   382   O  O   . GLY A  1 51  ? 23.879  110.511 19.435  1.00 11.47 ? 51  GLY A O   1 
ATOM   383   N  N   . ASP A  1 52  ? 24.547  110.850 17.306  1.00 14.16 ? 52  ASP A N   1 
ATOM   384   C  CA  . ASP A  1 52  ? 25.466  109.724 17.223  1.00 15.09 ? 52  ASP A CA  1 
ATOM   385   C  C   . ASP A  1 52  ? 26.908  110.217 17.129  1.00 18.66 ? 52  ASP A C   1 
ATOM   386   O  O   . ASP A  1 52  ? 27.335  110.736 16.089  1.00 16.55 ? 52  ASP A O   1 
ATOM   387   C  CB  . ASP A  1 52  ? 25.147  108.884 15.990  1.00 14.24 ? 52  ASP A CB  1 
ATOM   388   C  CG  . ASP A  1 52  ? 25.947  107.590 15.942  1.00 17.90 ? 52  ASP A CG  1 
ATOM   389   O  OD1 . ASP A  1 52  ? 27.062  107.530 16.503  1.00 18.28 ? 52  ASP A OD1 1 
ATOM   390   O  OD2 . ASP A  1 52  ? 25.444  106.619 15.352  1.00 19.63 ? 52  ASP A OD2 1 
ATOM   391   N  N   . ASN A  1 53  ? 27.652  110.022 18.212  1.00 18.39 ? 53  ASN A N   1 
ATOM   392   C  CA  . ASN A  1 53  ? 29.045  110.451 18.313  1.00 20.90 ? 53  ASN A CA  1 
ATOM   393   C  C   . ASN A  1 53  ? 30.013  109.260 18.310  1.00 18.07 ? 53  ASN A C   1 
ATOM   394   O  O   . ASN A  1 53  ? 31.176  109.384 18.698  1.00 20.61 ? 53  ASN A O   1 
ATOM   395   C  CB  . ASN A  1 53  ? 29.223  111.312 19.578  1.00 19.21 ? 53  ASN A CB  1 
ATOM   396   C  CG  . ASN A  1 53  ? 30.617  111.914 19.694  1.00 28.87 ? 53  ASN A CG  1 
ATOM   397   O  OD1 . ASN A  1 53  ? 31.341  111.635 20.659  1.00 27.97 ? 53  ASN A OD1 1 
ATOM   398   N  ND2 . ASN A  1 53  ? 31.008  112.731 18.704  1.00 27.39 ? 53  ASN A ND2 1 
ATOM   399   N  N   . THR A  1 54  ? 29.543  108.109 17.844  1.00 18.38 ? 54  THR A N   1 
ATOM   400   C  CA  . THR A  1 54  ? 30.379  106.902 17.852  1.00 22.55 ? 54  THR A CA  1 
ATOM   401   C  C   . THR A  1 54  ? 31.645  107.005 16.988  1.00 27.15 ? 54  THR A C   1 
ATOM   402   O  O   . THR A  1 54  ? 32.679  106.433 17.323  1.00 30.03 ? 54  THR A O   1 
ATOM   403   C  CB  . THR A  1 54  ? 29.597  105.637 17.437  1.00 19.78 ? 54  THR A CB  1 
ATOM   404   O  OG1 . THR A  1 54  ? 29.133  105.770 16.085  1.00 22.91 ? 54  THR A OG1 1 
ATOM   405   C  CG2 . THR A  1 54  ? 28.429  105.392 18.385  1.00 16.37 ? 54  THR A CG2 1 
ATOM   406   N  N   . ALA A  1 55  ? 31.561  107.720 15.876  1.00 25.11 ? 55  ALA A N   1 
ATOM   407   C  CA  . ALA A  1 55  ? 32.737  107.975 15.053  1.00 24.70 ? 55  ALA A CA  1 
ATOM   408   C  C   . ALA A  1 55  ? 32.979  109.469 15.074  1.00 27.06 ? 55  ALA A C   1 
ATOM   409   O  O   . ALA A  1 55  ? 33.027  110.110 14.027  1.00 32.55 ? 55  ALA A O   1 
ATOM   410   C  CB  . ALA A  1 55  ? 32.512  107.493 13.627  1.00 22.10 ? 55  ALA A CB  1 
ATOM   411   N  N   . GLY A  1 56  ? 33.102  110.014 16.281  1.00 24.87 ? 56  GLY A N   1 
ATOM   412   C  CA  . GLY A  1 56  ? 33.267  111.440 16.479  1.00 22.41 ? 56  GLY A CA  1 
ATOM   413   C  C   . GLY A  1 56  ? 32.140  112.242 15.846  1.00 31.91 ? 56  GLY A C   1 
ATOM   414   O  O   . GLY A  1 56  ? 30.963  111.843 15.878  1.00 29.23 ? 56  GLY A O   1 
ATOM   415   N  N   . SER A  1 57  ? 32.508  113.369 15.244  1.00 29.87 ? 57  SER A N   1 
ATOM   416   C  CA  . SER A  1 57  ? 31.543  114.304 14.693  1.00 24.64 ? 57  SER A CA  1 
ATOM   417   C  C   . SER A  1 57  ? 30.965  113.818 13.374  1.00 27.12 ? 57  SER A C   1 
ATOM   418   O  O   . SER A  1 57  ? 29.889  114.255 12.966  1.00 28.13 ? 57  SER A O   1 
ATOM   419   C  CB  . SER A  1 57  ? 32.212  115.660 14.490  1.00 29.90 ? 57  SER A CB  1 
ATOM   420   O  OG  . SER A  1 57  ? 33.553  115.480 14.056  1.00 35.26 ? 57  SER A OG  1 
ATOM   421   N  N   . THR A  1 58  ? 31.655  112.897 12.715  1.00 26.23 ? 58  THR A N   1 
ATOM   422   C  CA  . THR A  1 58  ? 31.272  112.535 11.357  1.00 30.32 ? 58  THR A CA  1 
ATOM   423   C  C   . THR A  1 58  ? 29.998  111.675 11.309  1.00 26.28 ? 58  THR A C   1 
ATOM   424   O  O   . THR A  1 58  ? 29.274  111.676 10.310  1.00 27.32 ? 58  THR A O   1 
ATOM   425   C  CB  . THR A  1 58  ? 32.453  111.891 10.587  1.00 30.32 ? 58  THR A CB  1 
ATOM   426   O  OG1 . THR A  1 58  ? 32.122  110.548 10.204  1.00 33.65 ? 58  THR A OG1 1 
ATOM   427   C  CG2 . THR A  1 58  ? 33.710  111.885 11.449  1.00 29.96 ? 58  THR A CG2 1 
ATOM   428   N  N   . SER A  1 59  ? 29.722  110.968 12.402  1.00 23.50 ? 59  SER A N   1 
ATOM   429   C  CA  . SER A  1 59  ? 28.524  110.136 12.508  1.00 23.86 ? 59  SER A CA  1 
ATOM   430   C  C   . SER A  1 59  ? 27.262  110.944 12.830  1.00 23.11 ? 59  SER A C   1 
ATOM   431   O  O   . SER A  1 59  ? 26.166  110.390 12.913  1.00 19.60 ? 59  SER A O   1 
ATOM   432   C  CB  . SER A  1 59  ? 28.718  109.018 13.550  1.00 22.83 ? 59  SER A CB  1 
ATOM   433   O  OG  . SER A  1 59  ? 29.376  109.494 14.716  1.00 24.39 ? 59  SER A OG  1 
ATOM   434   N  N   . ALA A  1 60  ? 27.429  112.248 13.025  1.00 21.87 ? 60  ALA A N   1 
ATOM   435   C  CA  . ALA A  1 60  ? 26.311  113.135 13.313  1.00 17.19 ? 60  ALA A CA  1 
ATOM   436   C  C   . ALA A  1 60  ? 25.351  113.272 12.113  1.00 17.83 ? 60  ALA A C   1 
ATOM   437   O  O   . ALA A  1 60  ? 24.222  113.730 12.267  1.00 16.20 ? 60  ALA A O   1 
ATOM   438   C  CB  . ALA A  1 60  ? 26.835  114.500 13.748  1.00 12.90 ? 60  ALA A CB  1 
ATOM   439   N  N   . GLY A  1 61  ? 25.810  112.894 10.918  1.00 17.98 ? 61  GLY A N   1 
ATOM   440   C  CA  . GLY A  1 61  ? 24.990  112.989 9.722   1.00 17.15 ? 61  GLY A CA  1 
ATOM   441   C  C   . GLY A  1 61  ? 24.842  114.391 9.134   1.00 18.79 ? 61  GLY A C   1 
ATOM   442   O  O   . GLY A  1 61  ? 25.598  115.300 9.489   1.00 19.38 ? 61  GLY A O   1 
ATOM   443   N  N   . PRO A  1 62  ? 23.863  114.576 8.222   1.00 16.93 ? 62  PRO A N   1 
ATOM   444   C  CA  . PRO A  1 62  ? 23.641  115.855 7.534   1.00 15.46 ? 62  PRO A CA  1 
ATOM   445   C  C   . PRO A  1 62  ? 22.859  116.797 8.422   1.00 13.58 ? 62  PRO A C   1 
ATOM   446   O  O   . PRO A  1 62  ? 22.426  116.382 9.484   1.00 12.69 ? 62  PRO A O   1 
ATOM   447   C  CB  . PRO A  1 62  ? 22.764  115.469 6.335   1.00 15.24 ? 62  PRO A CB  1 
ATOM   448   C  CG  . PRO A  1 62  ? 22.274  114.046 6.601   1.00 14.48 ? 62  PRO A CG  1 
ATOM   449   C  CD  . PRO A  1 62  ? 22.789  113.610 7.939   1.00 17.51 ? 62  PRO A CD  1 
ATOM   450   N  N   . HIS A  1 63  ? 22.659  118.031 7.985   1.00 10.97 ? 63  HIS A N   1 
ATOM   451   C  CA  . HIS A  1 63  ? 21.822  118.966 8.725   1.00 10.68 ? 63  HIS A CA  1 
ATOM   452   C  C   . HIS A  1 63  ? 20.440  118.381 8.970   1.00 11.81 ? 63  HIS A C   1 
ATOM   453   O  O   . HIS A  1 63  ? 19.902  117.685 8.119   1.00 13.12 ? 63  HIS A O   1 
ATOM   454   C  CB  . HIS A  1 63  ? 21.705  120.285 7.964   1.00 13.21 ? 63  HIS A CB  1 
ATOM   455   C  CG  . HIS A  1 63  ? 23.021  120.940 7.697   1.00 14.10 ? 63  HIS A CG  1 
ATOM   456   N  ND1 . HIS A  1 63  ? 23.135  122.108 6.980   1.00 13.72 ? 63  HIS A ND1 1 
ATOM   457   C  CD2 . HIS A  1 63  ? 24.279  120.607 8.082   1.00 13.25 ? 63  HIS A CD2 1 
ATOM   458   C  CE1 . HIS A  1 63  ? 24.408  122.462 6.926   1.00 15.69 ? 63  HIS A CE1 1 
ATOM   459   N  NE2 . HIS A  1 63  ? 25.121  121.568 7.586   1.00 14.04 ? 63  HIS A NE2 1 
ATOM   460   N  N   . PHE A  1 64  ? 19.903  118.626 10.160  1.00 10.53 ? 64  PHE A N   1 
ATOM   461   C  CA  . PHE A  1 64  ? 18.573  118.180 10.515  1.00 10.37 ? 64  PHE A CA  1 
ATOM   462   C  C   . PHE A  1 64  ? 17.589  118.791 9.543   1.00 9.97  ? 64  PHE A C   1 
ATOM   463   O  O   . PHE A  1 64  ? 17.426  120.007 9.509   1.00 11.05 ? 64  PHE A O   1 
ATOM   464   C  CB  . PHE A  1 64  ? 18.220  118.646 11.929  1.00 10.12 ? 64  PHE A CB  1 
ATOM   465   C  CG  . PHE A  1 64  ? 16.887  118.162 12.399  1.00 11.05 ? 64  PHE A CG  1 
ATOM   466   C  CD1 . PHE A  1 64  ? 16.453  116.882 12.082  1.00 12.31 ? 64  PHE A CD1 1 
ATOM   467   C  CD2 . PHE A  1 64  ? 16.074  118.969 13.181  1.00 11.27 ? 64  PHE A CD2 1 
ATOM   468   C  CE1 . PHE A  1 64  ? 15.213  116.420 12.501  1.00 11.71 ? 64  PHE A CE1 1 
ATOM   469   C  CE2 . PHE A  1 64  ? 14.833  118.508 13.630  1.00 12.69 ? 64  PHE A CE2 1 
ATOM   470   C  CZ  . PHE A  1 64  ? 14.402  117.229 13.283  1.00 12.16 ? 64  PHE A CZ  1 
ATOM   471   N  N   . ASN A  1 65  ? 16.905  117.953 8.779   1.00 13.83 ? 65  ASN A N   1 
ATOM   472   C  CA  . ASN A  1 65  ? 16.076  118.459 7.679   1.00 16.92 ? 65  ASN A CA  1 
ATOM   473   C  C   . ASN A  1 65  ? 14.754  117.713 7.523   1.00 13.20 ? 65  ASN A C   1 
ATOM   474   O  O   . ASN A  1 65  ? 14.537  117.044 6.524   1.00 15.69 ? 65  ASN A O   1 
ATOM   475   C  CB  . ASN A  1 65  ? 16.888  118.399 6.373   1.00 14.41 ? 65  ASN A CB  1 
ATOM   476   C  CG  . ASN A  1 65  ? 16.195  119.107 5.209   1.00 17.33 ? 65  ASN A CG  1 
ATOM   477   O  OD1 . ASN A  1 65  ? 15.293  119.918 5.410   1.00 15.37 ? 65  ASN A OD1 1 
ATOM   478   N  ND2 . ASN A  1 65  ? 16.640  118.812 3.984   1.00 17.23 ? 65  ASN A ND2 1 
ATOM   479   N  N   . PRO A  1 66  ? 13.867  117.816 8.518   1.00 14.99 ? 66  PRO A N   1 
ATOM   480   C  CA  . PRO A  1 66  ? 12.658  116.992 8.435   1.00 18.02 ? 66  PRO A CA  1 
ATOM   481   C  C   . PRO A  1 66  ? 11.689  117.391 7.314   1.00 18.51 ? 66  PRO A C   1 
ATOM   482   O  O   . PRO A  1 66  ? 10.932  116.533 6.905   1.00 19.68 ? 66  PRO A O   1 
ATOM   483   C  CB  . PRO A  1 66  ? 12.012  117.158 9.821   1.00 17.40 ? 66  PRO A CB  1 
ATOM   484   C  CG  . PRO A  1 66  ? 12.552  118.433 10.341  1.00 15.31 ? 66  PRO A CG  1 
ATOM   485   C  CD  . PRO A  1 66  ? 13.948  118.550 9.792   1.00 13.78 ? 66  PRO A CD  1 
ATOM   486   N  N   . LEU A  1 67  ? 11.733  118.624 6.813   1.00 17.55 ? 67  LEU A N   1 
ATOM   487   C  CA  . LEU A  1 67  ? 10.834  119.034 5.733   1.00 18.63 ? 67  LEU A CA  1 
ATOM   488   C  C   . LEU A  1 67  ? 11.493  118.946 4.363   1.00 24.44 ? 67  LEU A C   1 
ATOM   489   O  O   . LEU A  1 67  ? 10.943  119.436 3.375   1.00 27.13 ? 67  LEU A O   1 
ATOM   490   C  CB  . LEU A  1 67  ? 10.323  120.456 5.954   1.00 17.80 ? 67  LEU A CB  1 
ATOM   491   C  CG  . LEU A  1 67  ? 9.852   120.764 7.364   1.00 17.05 ? 67  LEU A CG  1 
ATOM   492   C  CD1 . LEU A  1 67  ? 9.557   122.239 7.518   1.00 20.99 ? 67  LEU A CD1 1 
ATOM   493   C  CD2 . LEU A  1 67  ? 8.603   119.953 7.675   1.00 24.18 ? 67  LEU A CD2 1 
ATOM   494   N  N   . SER A  1 68  ? 12.672  118.334 4.314   1.00 21.49 ? 68  SER A N   1 
ATOM   495   C  CA  . SER A  1 68  ? 13.377  118.089 3.066   1.00 18.32 ? 68  SER A CA  1 
ATOM   496   C  C   . SER A  1 68  ? 13.588  119.359 2.239   1.00 23.81 ? 68  SER A C   1 
ATOM   497   O  O   . SER A  1 68  ? 13.332  119.369 1.043   1.00 27.14 ? 68  SER A O   1 
ATOM   498   C  CB  . SER A  1 68  ? 12.628  117.037 2.223   1.00 28.72 ? 68  SER A CB  1 
ATOM   499   O  OG  . SER A  1 68  ? 12.313  115.864 2.965   1.00 24.43 ? 68  SER A OG  1 
ATOM   500   N  N   . ARG A  1 69  ? 14.055  120.430 2.862   1.00 22.32 ? 69  ARG A N   1 
ATOM   501   C  CA  . ARG A  1 69  ? 14.292  121.661 2.127   1.00 20.20 ? 69  ARG A CA  1 
ATOM   502   C  C   . ARG A  1 69  ? 15.749  121.752 1.689   1.00 24.27 ? 69  ARG A C   1 
ATOM   503   O  O   . ARG A  1 69  ? 16.551  120.849 1.960   1.00 21.41 ? 69  ARG A O   1 
ATOM   504   C  CB  . ARG A  1 69  ? 13.951  122.884 2.990   1.00 18.21 ? 69  ARG A CB  1 
ATOM   505   C  CG  . ARG A  1 69  ? 12.669  122.775 3.760   1.00 23.44 ? 69  ARG A CG  1 
ATOM   506   C  CD  . ARG A  1 69  ? 11.475  122.679 2.853   1.00 27.60 ? 69  ARG A CD  1 
ATOM   507   N  NE  . ARG A  1 69  ? 11.152  123.985 2.308   1.00 41.17 ? 69  ARG A NE  1 
ATOM   508   C  CZ  . ARG A  1 69  ? 10.498  124.928 2.981   1.00 44.70 ? 69  ARG A CZ  1 
ATOM   509   N  NH1 . ARG A  1 69  ? 10.091  124.699 4.231   1.00 35.97 ? 69  ARG A NH1 1 
ATOM   510   N  NH2 . ARG A  1 69  ? 10.255  126.104 2.402   1.00 41.94 ? 69  ARG A NH2 1 
ATOM   511   N  N   . LYS A  1 70  ? 16.088  122.854 1.019   1.00 20.87 ? 70  LYS A N   1 
ATOM   512   C  CA  . LYS A  1 70  ? 17.475  123.153 0.684   1.00 21.35 ? 70  LYS A CA  1 
ATOM   513   C  C   . LYS A  1 70  ? 18.083  123.967 1.825   1.00 15.86 ? 70  LYS A C   1 
ATOM   514   O  O   . LYS A  1 70  ? 17.347  124.564 2.624   1.00 16.71 ? 70  LYS A O   1 
ATOM   515   C  CB  . LYS A  1 70  ? 17.566  123.921 -0.648  1.00 21.16 ? 70  LYS A CB  1 
ATOM   516   C  CG  . LYS A  1 70  ? 17.184  123.086 -1.882  1.00 30.09 ? 70  LYS A CG  1 
ATOM   517   C  CD  . LYS A  1 70  ? 18.146  121.895 -2.054  1.00 30.82 ? 70  LYS A CD  1 
ATOM   518   C  CE  . LYS A  1 70  ? 17.580  120.800 -2.974  1.00 35.93 ? 70  LYS A CE  1 
ATOM   519   N  NZ  . LYS A  1 70  ? 18.610  119.748 -3.322  1.00 34.25 ? 70  LYS A NZ  1 
ATOM   520   N  N   . HIS A  1 71  ? 19.410  123.982 1.902   1.00 11.59 ? 71  HIS A N   1 
ATOM   521   C  CA  . HIS A  1 71  ? 20.140  124.711 2.945   1.00 14.44 ? 71  HIS A CA  1 
ATOM   522   C  C   . HIS A  1 71  ? 20.020  126.220 2.737   1.00 13.90 ? 71  HIS A C   1 
ATOM   523   O  O   . HIS A  1 71  ? 20.056  126.695 1.606   1.00 15.36 ? 71  HIS A O   1 
ATOM   524   C  CB  . HIS A  1 71  ? 21.630  124.314 2.918   1.00 14.52 ? 71  HIS A CB  1 
ATOM   525   C  CG  . HIS A  1 71  ? 22.484  125.106 3.858   1.00 14.94 ? 71  HIS A CG  1 
ATOM   526   N  ND1 . HIS A  1 71  ? 22.575  124.822 5.205   1.00 11.19 ? 71  HIS A ND1 1 
ATOM   527   C  CD2 . HIS A  1 71  ? 23.277  126.184 3.648   1.00 15.08 ? 71  HIS A CD2 1 
ATOM   528   C  CE1 . HIS A  1 71  ? 23.383  125.691 5.782   1.00 11.76 ? 71  HIS A CE1 1 
ATOM   529   N  NE2 . HIS A  1 71  ? 23.826  126.527 4.861   1.00 11.28 ? 71  HIS A NE2 1 
ATOM   530   N  N   . GLY A  1 72  ? 19.900  126.964 3.831   1.00 13.87 ? 72  GLY A N   1 
ATOM   531   C  CA  . GLY A  1 72  ? 19.925  128.419 3.813   1.00 14.51 ? 72  GLY A CA  1 
ATOM   532   C  C   . GLY A  1 72  ? 20.421  128.927 5.162   1.00 15.68 ? 72  GLY A C   1 
ATOM   533   O  O   . GLY A  1 72  ? 20.918  128.143 5.961   1.00 11.79 ? 72  GLY A O   1 
ATOM   534   N  N   . GLY A  1 73  ? 20.294  130.233 5.400   1.00 13.78 ? 73  GLY A N   1 
ATOM   535   C  CA  . GLY A  1 73  ? 20.544  130.841 6.689   1.00 14.37 ? 73  GLY A CA  1 
ATOM   536   C  C   . GLY A  1 73  ? 19.274  130.859 7.516   1.00 14.75 ? 73  GLY A C   1 
ATOM   537   O  O   . GLY A  1 73  ? 18.221  130.495 7.019   1.00 17.08 ? 73  GLY A O   1 
ATOM   538   N  N   . PRO A  1 74  ? 19.362  131.272 8.787   1.00 15.21 ? 74  PRO A N   1 
ATOM   539   C  CA  . PRO A  1 74  ? 18.188  131.124 9.671   1.00 14.41 ? 74  PRO A CA  1 
ATOM   540   C  C   . PRO A  1 74  ? 16.996  132.037 9.335   1.00 18.77 ? 74  PRO A C   1 
ATOM   541   O  O   . PRO A  1 74  ? 15.852  131.754 9.724   1.00 14.59 ? 74  PRO A O   1 
ATOM   542   C  CB  . PRO A  1 74  ? 18.747  131.423 11.072  1.00 11.06 ? 74  PRO A CB  1 
ATOM   543   C  CG  . PRO A  1 74  ? 20.056  132.163 10.838  1.00 14.16 ? 74  PRO A CG  1 
ATOM   544   C  CD  . PRO A  1 74  ? 20.587  131.623 9.524   1.00 13.19 ? 74  PRO A CD  1 
ATOM   545   N  N   . LYS A  1 75  ? 17.248  133.116 8.607   1.00 19.25 ? 75  LYS A N   1 
ATOM   546   C  CA  . LYS A  1 75  ? 16.166  134.029 8.272   1.00 18.81 ? 75  LYS A CA  1 
ATOM   547   C  C   . LYS A  1 75  ? 15.464  133.589 6.998   1.00 23.00 ? 75  LYS A C   1 
ATOM   548   O  O   . LYS A  1 75  ? 14.408  134.104 6.677   1.00 21.44 ? 75  LYS A O   1 
ATOM   549   C  CB  . LYS A  1 75  ? 16.676  135.464 8.144   1.00 24.37 ? 75  LYS A CB  1 
ATOM   550   C  CG  . LYS A  1 75  ? 17.279  136.014 9.449   1.00 26.10 ? 75  LYS A CG  1 
ATOM   551   C  CD  . LYS A  1 75  ? 17.349  137.541 9.447   1.00 38.96 ? 75  LYS A CD  1 
ATOM   552   C  CE  . LYS A  1 75  ? 18.563  138.055 8.707   1.00 34.81 ? 75  LYS A CE  1 
ATOM   553   N  NZ  . LYS A  1 75  ? 19.782  137.984 9.577   1.00 47.93 ? 75  LYS A NZ  1 
ATOM   554   N  N   . ASP A  1 76  ? 16.044  132.626 6.282   1.00 19.20 ? 76  ASP A N   1 
ATOM   555   C  CA  . ASP A  1 76  ? 15.445  132.146 5.029   1.00 22.24 ? 76  ASP A CA  1 
ATOM   556   C  C   . ASP A  1 76  ? 14.207  131.277 5.203   1.00 19.19 ? 76  ASP A C   1 
ATOM   557   O  O   . ASP A  1 76  ? 14.080  130.509 6.167   1.00 18.82 ? 76  ASP A O   1 
ATOM   558   C  CB  . ASP A  1 76  ? 16.473  131.416 4.167   1.00 21.33 ? 76  ASP A CB  1 
ATOM   559   C  CG  . ASP A  1 76  ? 17.616  132.319 3.753   1.00 22.10 ? 76  ASP A CG  1 
ATOM   560   O  OD1 . ASP A  1 76  ? 17.415  133.548 3.774   1.00 25.43 ? 76  ASP A OD1 1 
ATOM   561   O  OD2 . ASP A  1 76  ? 18.712  131.809 3.437   1.00 22.15 ? 76  ASP A OD2 1 
ATOM   562   N  N   . GLU A  1 77  ? 13.280  131.410 4.264   1.00 20.91 ? 77  GLU A N   1 
ATOM   563   C  CA  . GLU A  1 77  ? 12.120  130.536 4.259   1.00 24.83 ? 77  GLU A CA  1 
ATOM   564   C  C   . GLU A  1 77  ? 12.584  129.157 3.812   1.00 21.89 ? 77  GLU A C   1 
ATOM   565   O  O   . GLU A  1 77  ? 12.169  128.138 4.369   1.00 26.06 ? 77  GLU A O   1 
ATOM   566   C  CB  . GLU A  1 77  ? 11.012  131.084 3.348   1.00 29.47 ? 77  GLU A CB  1 
ATOM   567   C  CG  . GLU A  1 77  ? 9.612   130.934 3.920   1.00 35.00 ? 77  GLU A CG  1 
ATOM   568   C  CD  . GLU A  1 77  ? 9.139   129.490 3.947   1.00 37.63 ? 77  GLU A CD  1 
ATOM   569   O  OE1 . GLU A  1 77  ? 9.541   128.716 3.052   1.00 40.39 ? 77  GLU A OE1 1 
ATOM   570   O  OE2 . GLU A  1 77  ? 8.366   129.125 4.863   1.00 47.71 ? 77  GLU A OE2 1 
ATOM   571   N  N   . GLU A  1 78  ? 13.464  129.128 2.819   1.00 19.41 ? 78  GLU A N   1 
ATOM   572   C  CA  . GLU A  1 78  ? 14.072  127.874 2.377   1.00 22.64 ? 78  GLU A CA  1 
ATOM   573   C  C   . GLU A  1 78  ? 15.317  127.539 3.218   1.00 21.52 ? 78  GLU A C   1 
ATOM   574   O  O   . GLU A  1 78  ? 16.440  127.947 2.882   1.00 19.33 ? 78  GLU A O   1 
ATOM   575   C  CB  . GLU A  1 78  ? 14.441  127.949 0.896   1.00 17.04 ? 78  GLU A CB  1 
ATOM   576   C  CG  . GLU A  1 78  ? 14.871  126.620 0.275   1.00 19.00 ? 78  GLU A CG  1 
ATOM   577   C  CD  . GLU A  1 78  ? 13.711  125.630 0.103   1.00 28.33 ? 78  GLU A CD  1 
ATOM   578   O  OE1 . GLU A  1 78  ? 12.552  125.960 0.453   1.00 33.19 ? 78  GLU A OE1 1 
ATOM   579   O  OE2 . GLU A  1 78  ? 13.958  124.512 -0.391  1.00 30.82 ? 78  GLU A OE2 1 
ATOM   580   N  N   . ARG A  1 79  ? 15.110  126.812 4.313   1.00 14.70 ? 79  ARG A N   1 
ATOM   581   C  CA  . ARG A  1 79  ? 16.219  126.380 5.161   1.00 15.75 ? 79  ARG A CA  1 
ATOM   582   C  C   . ARG A  1 79  ? 15.955  125.003 5.747   1.00 16.45 ? 79  ARG A C   1 
ATOM   583   O  O   . ARG A  1 79  ? 14.817  124.516 5.779   1.00 15.15 ? 79  ARG A O   1 
ATOM   584   C  CB  . ARG A  1 79  ? 16.424  127.351 6.307   1.00 13.72 ? 79  ARG A CB  1 
ATOM   585   C  CG  . ARG A  1 79  ? 15.153  127.557 7.139   1.00 14.25 ? 79  ARG A CG  1 
ATOM   586   C  CD  . ARG A  1 79  ? 15.451  128.370 8.392   1.00 15.06 ? 79  ARG A CD  1 
ATOM   587   N  NE  . ARG A  1 79  ? 15.956  127.541 9.483   1.00 13.05 ? 79  ARG A NE  1 
ATOM   588   C  CZ  . ARG A  1 79  ? 15.937  127.923 10.753  1.00 14.82 ? 79  ARG A CZ  1 
ATOM   589   N  NH1 . ARG A  1 79  ? 15.455  129.111 11.069  1.00 14.72 ? 79  ARG A NH1 1 
ATOM   590   N  NH2 . ARG A  1 79  ? 16.395  127.123 11.706  1.00 13.65 ? 79  ARG A NH2 1 
ATOM   591   N  N   . HIS A  1 80  ? 17.022  124.368 6.200   1.00 12.07 ? 80  HIS A N   1 
ATOM   592   C  CA  . HIS A  1 80  ? 16.903  123.149 6.955   1.00 11.84 ? 80  HIS A CA  1 
ATOM   593   C  C   . HIS A  1 80  ? 16.420  123.587 8.336   1.00 12.96 ? 80  HIS A C   1 
ATOM   594   O  O   . HIS A  1 80  ? 16.709  124.706 8.749   1.00 10.67 ? 80  HIS A O   1 
ATOM   595   C  CB  . HIS A  1 80  ? 18.279  122.500 7.052   1.00 12.02 ? 80  HIS A CB  1 
ATOM   596   C  CG  . HIS A  1 80  ? 18.822  122.042 5.737   1.00 11.87 ? 80  HIS A CG  1 
ATOM   597   N  ND1 . HIS A  1 80  ? 20.168  122.066 5.438   1.00 12.04 ? 80  HIS A ND1 1 
ATOM   598   C  CD2 . HIS A  1 80  ? 18.206  121.508 4.660   1.00 12.73 ? 80  HIS A CD2 1 
ATOM   599   C  CE1 . HIS A  1 80  ? 20.357  121.574 4.226   1.00 14.25 ? 80  HIS A CE1 1 
ATOM   600   N  NE2 . HIS A  1 80  ? 19.180  121.229 3.729   1.00 17.02 ? 80  HIS A NE2 1 
ATOM   601   N  N   . VAL A  1 81  ? 15.696  122.733 9.055   1.00 11.21 ? 81  VAL A N   1 
ATOM   602   C  CA  . VAL A  1 81  ? 15.395  123.062 10.453  1.00 11.62 ? 81  VAL A CA  1 
ATOM   603   C  C   . VAL A  1 81  ? 16.670  123.326 11.234  1.00 11.37 ? 81  VAL A C   1 
ATOM   604   O  O   . VAL A  1 81  ? 16.707  124.217 12.072  1.00 10.70 ? 81  VAL A O   1 
ATOM   605   C  CB  . VAL A  1 81  ? 14.531  121.980 11.144  1.00 12.92 ? 81  VAL A CB  1 
ATOM   606   C  CG1 . VAL A  1 81  ? 14.513  122.160 12.671  1.00 10.13 ? 81  VAL A CG1 1 
ATOM   607   C  CG2 . VAL A  1 81  ? 13.090  122.038 10.568  1.00 12.88 ? 81  VAL A CG2 1 
ATOM   608   N  N   . GLY A  1 82  ? 17.731  122.587 10.919  1.00 10.59 ? 82  GLY A N   1 
ATOM   609   C  CA  . GLY A  1 82  ? 18.987  122.746 11.633  1.00 10.87 ? 82  GLY A CA  1 
ATOM   610   C  C   . GLY A  1 82  ? 19.849  123.955 11.279  1.00 12.59 ? 82  GLY A C   1 
ATOM   611   O  O   . GLY A  1 82  ? 20.943  124.110 11.846  1.00 10.49 ? 82  GLY A O   1 
ATOM   612   N  N   . ASP A  1 83  ? 19.389  124.815 10.363  1.00 9.30  ? 83  ASP A N   1 
ATOM   613   C  CA  . ASP A  1 83  ? 20.244  125.927 9.903   1.00 10.32 ? 83  ASP A CA  1 
ATOM   614   C  C   . ASP A  1 83  ? 20.190  127.130 10.826  1.00 12.52 ? 83  ASP A C   1 
ATOM   615   O  O   . ASP A  1 83  ? 19.263  127.940 10.744  1.00 13.90 ? 83  ASP A O   1 
ATOM   616   C  CB  . ASP A  1 83  ? 19.884  126.386 8.491   1.00 10.22 ? 83  ASP A CB  1 
ATOM   617   C  CG  . ASP A  1 83  ? 20.108  125.312 7.449   1.00 12.48 ? 83  ASP A CG  1 
ATOM   618   O  OD1 . ASP A  1 83  ? 20.912  124.396 7.679   1.00 9.14  ? 83  ASP A OD1 1 
ATOM   619   O  OD2 . ASP A  1 83  ? 19.480  125.388 6.382   1.00 12.19 ? 83  ASP A OD2 1 
ATOM   620   N  N   . LEU A  1 84  ? 21.186  127.263 11.694  1.00 13.91 ? 84  LEU A N   1 
ATOM   621   C  CA  . LEU A  1 84  ? 21.220  128.380 12.637  1.00 12.57 ? 84  LEU A CA  1 
ATOM   622   C  C   . LEU A  1 84  ? 22.301  129.372 12.229  1.00 11.90 ? 84  LEU A C   1 
ATOM   623   O  O   . LEU A  1 84  ? 22.676  130.251 13.002  1.00 15.15 ? 84  LEU A O   1 
ATOM   624   C  CB  . LEU A  1 84  ? 21.435  127.890 14.079  1.00 10.12 ? 84  LEU A CB  1 
ATOM   625   C  CG  . LEU A  1 84  ? 20.380  126.900 14.608  1.00 12.30 ? 84  LEU A CG  1 
ATOM   626   C  CD1 . LEU A  1 84  ? 20.763  126.369 16.014  1.00 11.01 ? 84  LEU A CD1 1 
ATOM   627   C  CD2 . LEU A  1 84  ? 18.968  127.513 14.628  1.00 11.22 ? 84  LEU A CD2 1 
ATOM   628   N  N   . GLY A  1 85  ? 22.797  129.231 11.005  1.00 14.94 ? 85  GLY A N   1 
ATOM   629   C  CA  . GLY A  1 85  ? 23.672  130.236 10.416  1.00 12.33 ? 85  GLY A CA  1 
ATOM   630   C  C   . GLY A  1 85  ? 25.057  130.271 11.014  1.00 14.31 ? 85  GLY A C   1 
ATOM   631   O  O   . GLY A  1 85  ? 25.758  129.248 11.016  1.00 13.27 ? 85  GLY A O   1 
ATOM   632   N  N   . ASN A  1 86  ? 25.459  131.438 11.520  1.00 12.80 ? 86  ASN A N   1 
ATOM   633   C  CA  . ASN A  1 86  ? 26.818  131.597 12.042  1.00 17.10 ? 86  ASN A CA  1 
ATOM   634   C  C   . ASN A  1 86  ? 26.867  132.175 13.440  1.00 13.69 ? 86  ASN A C   1 
ATOM   635   O  O   . ASN A  1 86  ? 26.005  132.948 13.818  1.00 18.97 ? 86  ASN A O   1 
ATOM   636   C  CB  . ASN A  1 86  ? 27.661  132.495 11.128  1.00 15.91 ? 86  ASN A CB  1 
ATOM   637   C  CG  . ASN A  1 86  ? 27.887  131.893 9.776   1.00 18.01 ? 86  ASN A CG  1 
ATOM   638   O  OD1 . ASN A  1 86  ? 28.614  130.901 9.639   1.00 16.41 ? 86  ASN A OD1 1 
ATOM   639   N  ND2 . ASN A  1 86  ? 27.287  132.499 8.748   1.00 18.45 ? 86  ASN A ND2 1 
ATOM   640   N  N   . VAL A  1 87  ? 27.893  131.796 14.194  1.00 14.56 ? 87  VAL A N   1 
ATOM   641   C  CA  . VAL A  1 87  ? 28.268  132.510 15.406  1.00 17.04 ? 87  VAL A CA  1 
ATOM   642   C  C   . VAL A  1 87  ? 29.550  133.266 15.125  1.00 18.56 ? 87  VAL A C   1 
ATOM   643   O  O   . VAL A  1 87  ? 30.318  132.895 14.228  1.00 18.04 ? 87  VAL A O   1 
ATOM   644   C  CB  . VAL A  1 87  ? 28.501  131.560 16.575  1.00 13.41 ? 87  VAL A CB  1 
ATOM   645   C  CG1 . VAL A  1 87  ? 27.212  130.781 16.857  1.00 16.49 ? 87  VAL A CG1 1 
ATOM   646   C  CG2 . VAL A  1 87  ? 29.630  130.615 16.266  1.00 11.85 ? 87  VAL A CG2 1 
ATOM   647   N  N   . THR A  1 88  ? 29.795  134.319 15.891  1.00 18.64 ? 88  THR A N   1 
ATOM   648   C  CA  . THR A  1 88  ? 30.969  135.144 15.640  1.00 20.66 ? 88  THR A CA  1 
ATOM   649   C  C   . THR A  1 88  ? 31.978  135.084 16.768  1.00 17.34 ? 88  THR A C   1 
ATOM   650   O  O   . THR A  1 88  ? 31.656  135.415 17.906  1.00 18.57 ? 88  THR A O   1 
ATOM   651   C  CB  . THR A  1 88  ? 30.592  136.622 15.414  1.00 21.63 ? 88  THR A CB  1 
ATOM   652   O  OG1 . THR A  1 88  ? 29.678  136.722 14.319  1.00 23.59 ? 88  THR A OG1 1 
ATOM   653   C  CG2 . THR A  1 88  ? 31.842  137.443 15.093  1.00 20.38 ? 88  THR A CG2 1 
ATOM   654   N  N   . ALA A  1 89  ? 33.205  134.687 16.447  1.00 20.30 ? 89  ALA A N   1 
ATOM   655   C  CA  . ALA A  1 89  ? 34.281  134.687 17.445  1.00 24.53 ? 89  ALA A CA  1 
ATOM   656   C  C   . ALA A  1 89  ? 35.093  135.990 17.432  1.00 23.55 ? 89  ALA A C   1 
ATOM   657   O  O   . ALA A  1 89  ? 35.541  136.448 16.375  1.00 21.08 ? 89  ALA A O   1 
ATOM   658   C  CB  . ALA A  1 89  ? 35.206  133.494 17.259  1.00 17.47 ? 89  ALA A CB  1 
ATOM   659   N  N   . ASP A  1 90  ? 35.278  136.566 18.616  1.00 25.74 ? 90  ASP A N   1 
ATOM   660   C  CA  . ASP A  1 90  ? 36.025  137.814 18.772  1.00 26.27 ? 90  ASP A CA  1 
ATOM   661   C  C   . ASP A  1 90  ? 37.514  137.606 18.565  1.00 24.44 ? 90  ASP A C   1 
ATOM   662   O  O   . ASP A  1 90  ? 37.946  136.494 18.267  1.00 25.26 ? 90  ASP A O   1 
ATOM   663   C  CB  . ASP A  1 90  ? 35.749  138.447 20.143  1.00 24.89 ? 90  ASP A CB  1 
ATOM   664   C  CG  . ASP A  1 90  ? 36.255  137.595 21.318  1.00 22.72 ? 90  ASP A CG  1 
ATOM   665   O  OD1 . ASP A  1 90  ? 37.121  136.709 21.138  1.00 22.71 ? 90  ASP A OD1 1 
ATOM   666   O  OD2 . ASP A  1 90  ? 35.789  137.840 22.450  1.00 22.98 ? 90  ASP A OD2 1 
ATOM   667   N  N   . LYS A  1 91  ? 38.303  138.665 18.741  1.00 29.46 ? 91  LYS A N   1 
ATOM   668   C  CA  . LYS A  1 91  ? 39.758  138.575 18.542  1.00 30.42 ? 91  LYS A CA  1 
ATOM   669   C  C   . LYS A  1 91  ? 40.434  137.594 19.511  1.00 29.43 ? 91  LYS A C   1 
ATOM   670   O  O   . LYS A  1 91  ? 41.510  137.062 19.213  1.00 33.55 ? 91  LYS A O   1 
ATOM   671   C  CB  . LYS A  1 91  ? 40.410  139.956 18.643  1.00 29.66 ? 91  LYS A CB  1 
ATOM   672   C  CG  . LYS A  1 91  ? 39.782  140.860 19.696  1.00 36.69 ? 91  LYS A CG  1 
ATOM   673   C  CD  . LYS A  1 91  ? 40.838  141.539 20.565  1.00 33.51 ? 91  LYS A CD  1 
ATOM   674   C  CE  . LYS A  1 91  ? 40.212  142.598 21.449  1.00 42.62 ? 91  LYS A CE  1 
ATOM   675   N  NZ  . LYS A  1 91  ? 41.219  143.284 22.309  1.00 39.62 ? 91  LYS A NZ  1 
ATOM   676   N  N   . ASP A  1 92  ? 39.792  137.355 20.655  1.00 21.36 ? 92  ASP A N   1 
ATOM   677   C  CA  . ASP A  1 92  ? 40.274  136.391 21.639  1.00 28.14 ? 92  ASP A CA  1 
ATOM   678   C  C   . ASP A  1 92  ? 39.749  134.986 21.417  1.00 30.44 ? 92  ASP A C   1 
ATOM   679   O  O   . ASP A  1 92  ? 40.044  134.090 22.207  1.00 27.02 ? 92  ASP A O   1 
ATOM   680   C  CB  . ASP A  1 92  ? 39.870  136.819 23.039  1.00 28.01 ? 92  ASP A CB  1 
ATOM   681   C  CG  . ASP A  1 92  ? 40.541  138.086 23.452  1.00 29.26 ? 92  ASP A CG  1 
ATOM   682   O  OD1 . ASP A  1 92  ? 41.629  138.367 22.899  1.00 33.82 ? 92  ASP A OD1 1 
ATOM   683   O  OD2 . ASP A  1 92  ? 39.977  138.797 24.307  1.00 32.48 ? 92  ASP A OD2 1 
ATOM   684   N  N   . GLY A  1 93  ? 38.944  134.806 20.371  1.00 22.64 ? 93  GLY A N   1 
ATOM   685   C  CA  . GLY A  1 93  ? 38.534  133.482 19.942  1.00 22.52 ? 93  GLY A CA  1 
ATOM   686   C  C   . GLY A  1 93  ? 37.314  132.945 20.658  1.00 20.31 ? 93  GLY A C   1 
ATOM   687   O  O   . GLY A  1 93  ? 37.046  131.742 20.622  1.00 20.40 ? 93  GLY A O   1 
ATOM   688   N  N   . VAL A  1 94  ? 36.592  133.853 21.303  1.00 21.45 ? 94  VAL A N   1 
ATOM   689   C  CA  . VAL A  1 94  ? 35.369  133.553 22.024  1.00 19.60 ? 94  VAL A CA  1 
ATOM   690   C  C   . VAL A  1 94  ? 34.143  134.025 21.250  1.00 22.59 ? 94  VAL A C   1 
ATOM   691   O  O   . VAL A  1 94  ? 34.023  135.203 20.873  1.00 20.52 ? 94  VAL A O   1 
ATOM   692   C  CB  . VAL A  1 94  ? 35.376  134.214 23.416  1.00 20.03 ? 94  VAL A CB  1 
ATOM   693   C  CG1 . VAL A  1 94  ? 34.015  134.071 24.097  1.00 17.70 ? 94  VAL A CG1 1 
ATOM   694   C  CG2 . VAL A  1 94  ? 36.445  133.585 24.272  1.00 20.74 ? 94  VAL A CG2 1 
ATOM   695   N  N   . ALA A  1 95  ? 33.232  133.094 21.004  1.00 15.98 ? 95  ALA A N   1 
ATOM   696   C  CA  . ALA A  1 95  ? 31.967  133.445 20.385  1.00 19.03 ? 95  ALA A CA  1 
ATOM   697   C  C   . ALA A  1 95  ? 30.899  133.489 21.432  1.00 19.92 ? 95  ALA A C   1 
ATOM   698   O  O   . ALA A  1 95  ? 30.593  132.482 22.061  1.00 21.23 ? 95  ALA A O   1 
ATOM   699   C  CB  . ALA A  1 95  ? 31.585  132.451 19.276  1.00 19.34 ? 95  ALA A CB  1 
ATOM   700   N  N   . ASP A  1 96  ? 30.353  134.670 21.649  1.00 18.12 ? 96  ASP A N   1 
ATOM   701   C  CA  A ASP A  1 96  ? 29.210  134.841 22.529  0.43 22.93 ? 96  ASP A CA  1 
ATOM   702   C  CA  B ASP A  1 96  ? 29.218  134.778 22.534  0.57 22.94 ? 96  ASP A CA  1 
ATOM   703   C  C   . ASP A  1 96  ? 27.957  134.581 21.702  1.00 22.90 ? 96  ASP A C   1 
ATOM   704   O  O   . ASP A  1 96  ? 27.678  135.313 20.754  1.00 22.84 ? 96  ASP A O   1 
ATOM   705   C  CB  A ASP A  1 96  ? 29.196  136.261 23.106  0.43 21.64 ? 96  ASP A CB  1 
ATOM   706   C  CB  B ASP A  1 96  ? 29.237  136.079 23.356  0.57 21.56 ? 96  ASP A CB  1 
ATOM   707   C  CG  A ASP A  1 96  ? 28.012  136.517 24.009  0.43 22.79 ? 96  ASP A CG  1 
ATOM   708   C  CG  B ASP A  1 96  ? 30.258  136.035 24.494  0.57 24.95 ? 96  ASP A CG  1 
ATOM   709   O  OD1 A ASP A  1 96  ? 27.438  135.547 24.536  0.43 25.09 ? 96  ASP A OD1 1 
ATOM   710   O  OD1 B ASP A  1 96  ? 30.092  135.190 25.400  0.57 25.97 ? 96  ASP A OD1 1 
ATOM   711   O  OD2 A ASP A  1 96  ? 27.653  137.696 24.200  0.43 26.87 ? 96  ASP A OD2 1 
ATOM   712   O  OD2 B ASP A  1 96  ? 31.225  136.836 24.495  0.57 24.52 ? 96  ASP A OD2 1 
ATOM   713   N  N   . VAL A  1 97  ? 27.221  133.536 22.044  1.00 21.15 ? 97  VAL A N   1 
ATOM   714   C  CA  . VAL A  1 97  ? 26.067  133.144 21.253  1.00 22.14 ? 97  VAL A CA  1 
ATOM   715   C  C   . VAL A  1 97  ? 24.805  133.642 21.911  1.00 22.95 ? 97  VAL A C   1 
ATOM   716   O  O   . VAL A  1 97  ? 24.619  133.499 23.115  1.00 21.85 ? 97  VAL A O   1 
ATOM   717   C  CB  . VAL A  1 97  ? 26.013  131.613 21.048  1.00 18.00 ? 97  VAL A CB  1 
ATOM   718   C  CG1 . VAL A  1 97  ? 24.833  131.230 20.164  1.00 22.27 ? 97  VAL A CG1 1 
ATOM   719   C  CG2 . VAL A  1 97  ? 27.298  131.128 20.426  1.00 16.71 ? 97  VAL A CG2 1 
ATOM   720   N  N   . SER A  1 98  ? 23.950  134.266 21.115  1.00 27.67 ? 98  SER A N   1 
ATOM   721   C  CA  . SER A  1 98  ? 22.653  134.680 21.601  1.00 24.83 ? 98  SER A CA  1 
ATOM   722   C  C   . SER A  1 98  ? 21.732  134.802 20.411  1.00 28.97 ? 98  SER A C   1 
ATOM   723   O  O   . SER A  1 98  ? 21.841  135.736 19.632  1.00 34.92 ? 98  SER A O   1 
ATOM   724   C  CB  . SER A  1 98  ? 22.738  135.988 22.366  1.00 27.17 ? 98  SER A CB  1 
ATOM   725   O  OG  . SER A  1 98  ? 21.629  136.112 23.248  1.00 34.26 ? 98  SER A OG  1 
ATOM   726   N  N   . ILE A  1 99  ? 20.837  133.827 20.284  1.00 24.47 ? 99  ILE A N   1 
ATOM   727   C  CA  . ILE A  1 99  ? 20.031  133.622 19.096  1.00 22.55 ? 99  ILE A CA  1 
ATOM   728   C  C   . ILE A  1 99  ? 18.600  133.399 19.555  1.00 21.25 ? 99  ILE A C   1 
ATOM   729   O  O   . ILE A  1 99  ? 18.341  132.887 20.651  1.00 17.08 ? 99  ILE A O   1 
ATOM   730   C  CB  . ILE A  1 99  ? 20.497  132.339 18.339  1.00 21.02 ? 99  ILE A CB  1 
ATOM   731   C  CG1 . ILE A  1 99  ? 21.911  132.476 17.800  1.00 28.12 ? 99  ILE A CG1 1 
ATOM   732   C  CG2 . ILE A  1 99  ? 19.613  132.009 17.153  1.00 24.43 ? 99  ILE A CG2 1 
ATOM   733   C  CD1 . ILE A  1 99  ? 22.296  131.316 16.856  1.00 21.53 ? 99  ILE A CD1 1 
ATOM   734   N  N   . GLU A  1 100 ? 17.655  133.791 18.729  1.00 23.82 ? 100 GLU A N   1 
ATOM   735   C  CA  . GLU A  1 100 ? 16.307  133.312 18.929  1.00 21.45 ? 100 GLU A CA  1 
ATOM   736   C  C   . GLU A  1 100 ? 15.853  132.725 17.606  1.00 17.69 ? 100 GLU A C   1 
ATOM   737   O  O   . GLU A  1 100 ? 16.126  133.297 16.545  1.00 17.13 ? 100 GLU A O   1 
ATOM   738   C  CB  . GLU A  1 100 ? 15.391  134.428 19.404  1.00 24.56 ? 100 GLU A CB  1 
ATOM   739   C  CG  . GLU A  1 100 ? 14.010  133.923 19.773  1.00 28.65 ? 100 GLU A CG  1 
ATOM   740   C  CD  . GLU A  1 100 ? 13.028  135.044 20.067  1.00 37.29 ? 100 GLU A CD  1 
ATOM   741   O  OE1 . GLU A  1 100 ? 13.112  135.617 21.181  1.00 39.69 ? 100 GLU A OE1 1 
ATOM   742   O  OE2 . GLU A  1 100 ? 12.177  135.336 19.187  1.00 27.35 ? 100 GLU A OE2 1 
ATOM   743   N  N   . ASP A  1 101 ? 15.201  131.568 17.665  1.00 13.32 ? 101 ASP A N   1 
ATOM   744   C  CA  . ASP A  1 101 ? 14.788  130.874 16.454  1.00 15.88 ? 101 ASP A CA  1 
ATOM   745   C  C   . ASP A  1 101 ? 13.394  130.273 16.599  1.00 16.99 ? 101 ASP A C   1 
ATOM   746   O  O   . ASP A  1 101 ? 13.045  129.754 17.671  1.00 17.26 ? 101 ASP A O   1 
ATOM   747   C  CB  . ASP A  1 101 ? 15.813  129.797 16.063  1.00 12.80 ? 101 ASP A CB  1 
ATOM   748   C  CG  . ASP A  1 101 ? 15.633  129.326 14.634  1.00 16.42 ? 101 ASP A CG  1 
ATOM   749   O  OD1 . ASP A  1 101 ? 16.097  130.029 13.711  1.00 17.60 ? 101 ASP A OD1 1 
ATOM   750   O  OD2 . ASP A  1 101 ? 15.010  128.261 14.421  1.00 15.76 ? 101 ASP A OD2 1 
ATOM   751   N  N   . SER A  1 102 ? 12.609  130.331 15.522  1.00 15.41 ? 102 SER A N   1 
ATOM   752   C  CA  . SER A  1 102 ? 11.201  129.923 15.566  1.00 19.85 ? 102 SER A CA  1 
ATOM   753   C  C   . SER A  1 102 ? 10.930  128.653 14.785  1.00 18.40 ? 102 SER A C   1 
ATOM   754   O  O   . SER A  1 102 ? 9.788   128.211 14.702  1.00 16.76 ? 102 SER A O   1 
ATOM   755   C  CB  . SER A  1 102 ? 10.297  131.014 14.986  1.00 19.19 ? 102 SER A CB  1 
ATOM   756   O  OG  . SER A  1 102 ? 10.329  132.181 15.781  1.00 33.25 ? 102 SER A OG  1 
ATOM   757   N  N   . VAL A  1 103 ? 11.971  128.103 14.171  1.00 16.03 ? 103 VAL A N   1 
ATOM   758   C  CA  . VAL A  1 103 ? 11.848  126.878 13.385  1.00 14.83 ? 103 VAL A CA  1 
ATOM   759   C  C   . VAL A  1 103 ? 12.307  125.655 14.199  1.00 15.55 ? 103 VAL A C   1 
ATOM   760   O  O   . VAL A  1 103 ? 11.674  124.601 14.163  1.00 15.61 ? 103 VAL A O   1 
ATOM   761   C  CB  . VAL A  1 103 ? 12.647  126.967 12.066  1.00 13.14 ? 103 VAL A CB  1 
ATOM   762   C  CG1 . VAL A  1 103 ? 12.594  125.642 11.322  1.00 12.03 ? 103 VAL A CG1 1 
ATOM   763   C  CG2 . VAL A  1 103 ? 12.076  128.077 11.194  1.00 15.91 ? 103 VAL A CG2 1 
ATOM   764   N  N   . ILE A  1 104 ? 13.400  125.783 14.939  1.00 12.47 ? 104 ILE A N   1 
ATOM   765   C  CA  . ILE A  1 104 ? 13.756  124.685 15.820  1.00 12.68 ? 104 ILE A CA  1 
ATOM   766   C  C   . ILE A  1 104 ? 12.760  124.628 16.968  1.00 13.12 ? 104 ILE A C   1 
ATOM   767   O  O   . ILE A  1 104 ? 12.081  125.616 17.264  1.00 13.60 ? 104 ILE A O   1 
ATOM   768   C  CB  . ILE A  1 104 ? 15.193  124.782 16.362  1.00 10.90 ? 104 ILE A CB  1 
ATOM   769   C  CG1 . ILE A  1 104 ? 15.423  126.110 17.078  1.00 11.69 ? 104 ILE A CG1 1 
ATOM   770   C  CG2 . ILE A  1 104 ? 16.215  124.566 15.227  1.00 9.56  ? 104 ILE A CG2 1 
ATOM   771   C  CD1 . ILE A  1 104 ? 16.600  126.072 18.080  1.00 9.24  ? 104 ILE A CD1 1 
ATOM   772   N  N   . SER A  1 105 ? 12.654  123.465 17.597  1.00 12.12 ? 105 SER A N   1 
ATOM   773   C  CA  . SER A  1 105 ? 11.762  123.316 18.730  1.00 13.54 ? 105 SER A CA  1 
ATOM   774   C  C   . SER A  1 105 ? 12.367  122.330 19.707  1.00 12.65 ? 105 SER A C   1 
ATOM   775   O  O   . SER A  1 105 ? 13.197  121.513 19.317  1.00 12.46 ? 105 SER A O   1 
ATOM   776   C  CB  . SER A  1 105 ? 10.398  122.816 18.253  1.00 15.72 ? 105 SER A CB  1 
ATOM   777   O  OG  . SER A  1 105 ? 9.448   122.905 19.289  1.00 15.26 ? 105 SER A OG  1 
ATOM   778   N  N   . LEU A  1 106 ? 11.950  122.417 20.967  1.00 13.35 ? 106 LEU A N   1 
ATOM   779   C  CA  . LEU A  1 106 ? 12.406  121.505 22.010  1.00 12.73 ? 106 LEU A CA  1 
ATOM   780   C  C   . LEU A  1 106 ? 11.383  120.401 22.260  1.00 15.50 ? 106 LEU A C   1 
ATOM   781   O  O   . LEU A  1 106 ? 11.549  119.575 23.151  1.00 16.18 ? 106 LEU A O   1 
ATOM   782   C  CB  . LEU A  1 106 ? 12.707  122.255 23.309  1.00 11.53 ? 106 LEU A CB  1 
ATOM   783   C  CG  . LEU A  1 106 ? 13.826  123.284 23.238  1.00 12.44 ? 106 LEU A CG  1 
ATOM   784   C  CD1 . LEU A  1 106 ? 14.165  123.819 24.636  1.00 13.32 ? 106 LEU A CD1 1 
ATOM   785   C  CD2 . LEU A  1 106 ? 15.086  122.708 22.538  1.00 9.43  ? 106 LEU A CD2 1 
ATOM   786   N  N   . SER A  1 107 ? 10.331  120.387 21.452  1.00 15.96 ? 107 SER A N   1 
ATOM   787   C  CA  . SER A  1 107 ? 9.327   119.343 21.512  1.00 18.63 ? 107 SER A CA  1 
ATOM   788   C  C   . SER A  1 107 ? 8.710   119.192 20.113  1.00 20.29 ? 107 SER A C   1 
ATOM   789   O  O   . SER A  1 107 ? 8.954   120.027 19.233  1.00 17.65 ? 107 SER A O   1 
ATOM   790   C  CB  . SER A  1 107 ? 8.270   119.689 22.560  1.00 17.15 ? 107 SER A CB  1 
ATOM   791   O  OG  . SER A  1 107 ? 7.693   120.957 22.291  1.00 18.38 ? 107 SER A OG  1 
ATOM   792   N  N   . GLY A  1 108 ? 7.951   118.115 19.893  1.00 23.02 ? 108 GLY A N   1 
ATOM   793   C  CA  . GLY A  1 108 ? 7.247   117.907 18.633  1.00 20.58 ? 108 GLY A CA  1 
ATOM   794   C  C   . GLY A  1 108 ? 8.089   117.476 17.449  1.00 27.92 ? 108 GLY A C   1 
ATOM   795   O  O   . GLY A  1 108 ? 9.108   116.815 17.605  1.00 30.39 ? 108 GLY A O   1 
ATOM   796   N  N   . ASP A  1 109 ? 7.664   117.854 16.244  1.00 31.10 ? 109 ASP A N   1 
ATOM   797   C  CA  . ASP A  1 109 ? 8.273   117.338 15.011  1.00 27.07 ? 109 ASP A CA  1 
ATOM   798   C  C   . ASP A  1 109 ? 9.600   118.014 14.690  1.00 28.31 ? 109 ASP A C   1 
ATOM   799   O  O   . ASP A  1 109 ? 10.525  117.371 14.204  1.00 27.50 ? 109 ASP A O   1 
ATOM   800   C  CB  . ASP A  1 109 ? 7.302   117.485 13.830  1.00 35.83 ? 109 ASP A CB  1 
ATOM   801   C  CG  . ASP A  1 109 ? 7.728   116.707 12.587  1.00 43.65 ? 109 ASP A CG  1 
ATOM   802   O  OD1 . ASP A  1 109 ? 8.936   116.654 12.249  1.00 35.90 ? 109 ASP A OD1 1 
ATOM   803   O  OD2 . ASP A  1 109 ? 6.814   116.160 11.925  1.00 55.88 ? 109 ASP A OD2 1 
ATOM   804   N  N   . HIS A  1 110 ? 9.702   119.310 14.952  1.00 23.35 ? 110 HIS A N   1 
ATOM   805   C  CA  . HIS A  1 110 ? 10.965  119.992 14.711  1.00 20.56 ? 110 HIS A CA  1 
ATOM   806   C  C   . HIS A  1 110 ? 11.917  119.806 15.888  1.00 18.17 ? 110 HIS A C   1 
ATOM   807   O  O   . HIS A  1 110 ? 12.891  120.542 16.015  1.00 17.36 ? 110 HIS A O   1 
ATOM   808   C  CB  . HIS A  1 110 ? 10.730  121.490 14.435  1.00 19.20 ? 110 HIS A CB  1 
ATOM   809   C  CG  . HIS A  1 110 ? 10.082  121.769 13.114  1.00 22.92 ? 110 HIS A CG  1 
ATOM   810   N  ND1 . HIS A  1 110 ? 9.927   123.048 12.614  1.00 21.85 ? 110 HIS A ND1 1 
ATOM   811   C  CD2 . HIS A  1 110 ? 9.564   120.934 12.181  1.00 23.84 ? 110 HIS A CD2 1 
ATOM   812   C  CE1 . HIS A  1 110 ? 9.341   122.986 11.432  1.00 21.34 ? 110 HIS A CE1 1 
ATOM   813   N  NE2 . HIS A  1 110 ? 9.116   121.716 11.143  1.00 25.97 ? 110 HIS A NE2 1 
ATOM   814   N  N   . CYS A  1 111 ? 11.628  118.837 16.755  1.00 19.61 ? 111 CYS A N   1 
ATOM   815   C  CA  . CYS A  1 111 ? 12.377  118.687 18.013  1.00 17.30 ? 111 CYS A CA  1 
ATOM   816   C  C   . CYS A  1 111 ? 13.851  118.325 17.819  1.00 12.53 ? 111 CYS A C   1 
ATOM   817   O  O   . CYS A  1 111 ? 14.183  117.343 17.150  1.00 11.93 ? 111 CYS A O   1 
ATOM   818   C  CB  . CYS A  1 111 ? 11.702  117.641 18.903  1.00 20.83 ? 111 CYS A CB  1 
ATOM   819   S  SG  . CYS A  1 111 ? 12.519  117.346 20.445  1.00 20.44 ? 111 CYS A SG  1 
ATOM   820   N  N   . ILE A  1 112 ? 14.734  119.115 18.414  1.00 10.54 ? 112 ILE A N   1 
ATOM   821   C  CA  . ILE A  1 112 ? 16.164  118.903 18.245  1.00 12.13 ? 112 ILE A CA  1 
ATOM   822   C  C   . ILE A  1 112 ? 16.837  118.197 19.431  1.00 11.99 ? 112 ILE A C   1 
ATOM   823   O  O   . ILE A  1 112 ? 18.058  118.015 19.433  1.00 12.34 ? 112 ILE A O   1 
ATOM   824   C  CB  . ILE A  1 112 ? 16.890  120.240 17.996  1.00 10.41 ? 112 ILE A CB  1 
ATOM   825   C  CG1 . ILE A  1 112 ? 16.701  121.134 19.231  1.00 11.05 ? 112 ILE A CG1 1 
ATOM   826   C  CG2 . ILE A  1 112 ? 16.376  120.889 16.701  1.00 10.89 ? 112 ILE A CG2 1 
ATOM   827   C  CD1 . ILE A  1 112 ? 17.532  122.365 19.234  1.00 13.59 ? 112 ILE A CD1 1 
ATOM   828   N  N   . ILE A  1 113 ? 16.061  117.822 20.440  1.00 11.21 ? 113 ILE A N   1 
ATOM   829   C  CA  . ILE A  1 113 ? 16.603  117.102 21.582  1.00 11.41 ? 113 ILE A CA  1 
ATOM   830   C  C   . ILE A  1 113 ? 17.121  115.759 21.102  1.00 13.84 ? 113 ILE A C   1 
ATOM   831   O  O   . ILE A  1 113 ? 16.462  115.108 20.319  1.00 12.97 ? 113 ILE A O   1 
ATOM   832   C  CB  . ILE A  1 113 ? 15.567  116.963 22.717  1.00 13.53 ? 113 ILE A CB  1 
ATOM   833   C  CG1 . ILE A  1 113 ? 15.395  118.328 23.399  1.00 12.47 ? 113 ILE A CG1 1 
ATOM   834   C  CG2 . ILE A  1 113 ? 16.027  115.928 23.754  1.00 9.71  ? 113 ILE A CG2 1 
ATOM   835   C  CD1 . ILE A  1 113 ? 14.193  118.452 24.192  1.00 14.55 ? 113 ILE A CD1 1 
ATOM   836   N  N   . GLY A  1 114 ? 18.327  115.373 21.517  1.00 9.84  ? 114 GLY A N   1 
ATOM   837   C  CA  . GLY A  1 114 ? 18.896  114.121 21.055  1.00 7.05  ? 114 GLY A CA  1 
ATOM   838   C  C   . GLY A  1 114 ? 19.536  114.173 19.679  1.00 11.17 ? 114 GLY A C   1 
ATOM   839   O  O   . GLY A  1 114 ? 19.924  113.143 19.142  1.00 8.93  ? 114 GLY A O   1 
ATOM   840   N  N   . ARG A  1 115 ? 19.633  115.366 19.097  1.00 9.66  ? 115 ARG A N   1 
ATOM   841   C  CA  . ARG A  1 115 ? 20.428  115.553 17.893  1.00 12.75 ? 115 ARG A CA  1 
ATOM   842   C  C   . ARG A  1 115 ? 21.779  116.225 18.210  1.00 9.62  ? 115 ARG A C   1 
ATOM   843   O  O   . ARG A  1 115 ? 22.096  116.453 19.368  1.00 9.18  ? 115 ARG A O   1 
ATOM   844   C  CB  . ARG A  1 115 ? 19.609  116.290 16.840  1.00 9.81  ? 115 ARG A CB  1 
ATOM   845   C  CG  . ARG A  1 115 ? 18.258  115.587 16.689  1.00 11.99 ? 115 ARG A CG  1 
ATOM   846   C  CD  . ARG A  1 115 ? 17.474  116.040 15.503  1.00 14.32 ? 115 ARG A CD  1 
ATOM   847   N  NE  . ARG A  1 115 ? 16.130  115.476 15.515  1.00 14.96 ? 115 ARG A NE  1 
ATOM   848   C  CZ  . ARG A  1 115 ? 15.795  114.333 14.933  1.00 14.72 ? 115 ARG A CZ  1 
ATOM   849   N  NH1 . ARG A  1 115 ? 16.709  113.617 14.286  1.00 11.66 ? 115 ARG A NH1 1 
ATOM   850   N  NH2 . ARG A  1 115 ? 14.531  113.924 14.977  1.00 17.88 ? 115 ARG A NH2 1 
ATOM   851   N  N   . THR A  1 116 ? 22.577  116.515 17.190  1.00 12.21 ? 116 THR A N   1 
ATOM   852   C  CA  . THR A  1 116 ? 23.934  116.993 17.431  1.00 11.46 ? 116 THR A CA  1 
ATOM   853   C  C   . THR A  1 116 ? 24.104  118.442 17.050  1.00 11.20 ? 116 THR A C   1 
ATOM   854   O  O   . THR A  1 116 ? 23.842  118.837 15.919  1.00 11.01 ? 116 THR A O   1 
ATOM   855   C  CB  . THR A  1 116 ? 24.962  116.129 16.700  1.00 10.48 ? 116 THR A CB  1 
ATOM   856   O  OG1 . THR A  1 116 ? 24.904  114.802 17.235  1.00 11.38 ? 116 THR A OG1 1 
ATOM   857   C  CG2 . THR A  1 116 ? 26.382  116.701 16.867  1.00 11.24 ? 116 THR A CG2 1 
ATOM   858   N  N   . LEU A  1 117 ? 24.509  119.250 18.020  1.00 9.46  ? 117 LEU A N   1 
ATOM   859   C  CA  . LEU A  1 117 ? 24.874  120.624 17.739  1.00 9.80  ? 117 LEU A CA  1 
ATOM   860   C  C   . LEU A  1 117 ? 26.332  120.637 17.257  1.00 10.51 ? 117 LEU A C   1 
ATOM   861   O  O   . LEU A  1 117 ? 27.190  120.029 17.886  1.00 11.22 ? 117 LEU A O   1 
ATOM   862   C  CB  . LEU A  1 117 ? 24.715  121.457 18.999  1.00 9.01  ? 117 LEU A CB  1 
ATOM   863   C  CG  . LEU A  1 117 ? 24.965  122.943 18.796  1.00 12.78 ? 117 LEU A CG  1 
ATOM   864   C  CD1 . LEU A  1 117 ? 23.971  123.467 17.768  1.00 9.94  ? 117 LEU A CD1 1 
ATOM   865   C  CD2 . LEU A  1 117 ? 24.825  123.665 20.097  1.00 6.65  ? 117 LEU A CD2 1 
ATOM   866   N  N   . VAL A  1 118 ? 26.615  121.305 16.147  1.00 11.34 ? 118 VAL A N   1 
ATOM   867   C  CA  . VAL A  1 118 ? 27.981  121.339 15.606  1.00 11.08 ? 118 VAL A CA  1 
ATOM   868   C  C   . VAL A  1 118 ? 28.445  122.781 15.341  1.00 15.02 ? 118 VAL A C   1 
ATOM   869   O  O   . VAL A  1 118 ? 27.684  123.594 14.798  1.00 11.66 ? 118 VAL A O   1 
ATOM   870   C  CB  . VAL A  1 118 ? 28.112  120.539 14.295  1.00 12.25 ? 118 VAL A CB  1 
ATOM   871   C  CG1 . VAL A  1 118 ? 29.554  120.608 13.743  1.00 10.61 ? 118 VAL A CG1 1 
ATOM   872   C  CG2 . VAL A  1 118 ? 27.679  119.098 14.479  1.00 8.94  ? 118 VAL A CG2 1 
ATOM   873   N  N   . VAL A  1 119 ? 29.677  123.103 15.743  1.00 11.29 ? 119 VAL A N   1 
ATOM   874   C  CA  . VAL A  1 119 ? 30.295  124.363 15.319  1.00 12.46 ? 119 VAL A CA  1 
ATOM   875   C  C   . VAL A  1 119 ? 31.454  124.104 14.318  1.00 14.18 ? 119 VAL A C   1 
ATOM   876   O  O   . VAL A  1 119 ? 32.239  123.157 14.486  1.00 13.27 ? 119 VAL A O   1 
ATOM   877   C  CB  . VAL A  1 119 ? 30.715  125.246 16.520  1.00 10.84 ? 119 VAL A CB  1 
ATOM   878   C  CG1 . VAL A  1 119 ? 31.822  124.572 17.339  1.00 13.47 ? 119 VAL A CG1 1 
ATOM   879   C  CG2 . VAL A  1 119 ? 31.159  126.644 16.038  1.00 11.27 ? 119 VAL A CG2 1 
ATOM   880   N  N   . HIS A  1 120 ? 31.536  124.933 13.271  1.00 10.68 ? 120 HIS A N   1 
ATOM   881   C  CA  . HIS A  1 120 ? 32.347  124.613 12.099  1.00 14.92 ? 120 HIS A CA  1 
ATOM   882   C  C   . HIS A  1 120 ? 33.613  125.440 11.900  1.00 14.66 ? 120 HIS A C   1 
ATOM   883   O  O   . HIS A  1 120 ? 33.774  126.521 12.454  1.00 16.47 ? 120 HIS A O   1 
ATOM   884   C  CB  . HIS A  1 120 ? 31.511  124.731 10.811  1.00 15.09 ? 120 HIS A CB  1 
ATOM   885   C  CG  . HIS A  1 120 ? 30.663  123.535 10.530  1.00 13.44 ? 120 HIS A CG  1 
ATOM   886   N  ND1 . HIS A  1 120 ? 31.084  122.497 9.728   1.00 14.96 ? 120 HIS A ND1 1 
ATOM   887   C  CD2 . HIS A  1 120 ? 29.409  123.218 10.932  1.00 10.89 ? 120 HIS A CD2 1 
ATOM   888   C  CE1 . HIS A  1 120 ? 30.126  121.589 9.649   1.00 14.72 ? 120 HIS A CE1 1 
ATOM   889   N  NE2 . HIS A  1 120 ? 29.100  122.004 10.371  1.00 12.89 ? 120 HIS A NE2 1 
ATOM   890   N  N   . GLU A  1 121 ? 34.483  124.910 11.056  1.00 14.73 ? 121 GLU A N   1 
ATOM   891   C  CA  . GLU A  1 121 ? 35.743  125.541 10.696  1.00 14.81 ? 121 GLU A CA  1 
ATOM   892   C  C   . GLU A  1 121 ? 35.564  126.937 10.102  1.00 19.83 ? 121 GLU A C   1 
ATOM   893   O  O   . GLU A  1 121 ? 36.191  127.893 10.572  1.00 17.25 ? 121 GLU A O   1 
ATOM   894   C  CB  . GLU A  1 121 ? 36.474  124.639 9.700   1.00 19.46 ? 121 GLU A CB  1 
ATOM   895   C  CG  . GLU A  1 121 ? 37.858  125.101 9.286   1.00 18.65 ? 121 GLU A CG  1 
ATOM   896   C  CD  . GLU A  1 121 ? 38.373  124.324 8.093   1.00 26.74 ? 121 GLU A CD  1 
ATOM   897   O  OE1 . GLU A  1 121 ? 39.575  124.451 7.774   1.00 36.74 ? 121 GLU A OE1 1 
ATOM   898   O  OE2 . GLU A  1 121 ? 37.576  123.574 7.477   1.00 25.45 ? 121 GLU A OE2 1 
ATOM   899   N  N   . LYS A  1 122 ? 34.695  127.053 9.092   1.00 16.29 ? 122 LYS A N   1 
ATOM   900   C  CA  . LYS A  1 122 ? 34.522  128.311 8.365   1.00 20.39 ? 122 LYS A CA  1 
ATOM   901   C  C   . LYS A  1 122 ? 33.101  128.856 8.461   1.00 20.10 ? 122 LYS A C   1 
ATOM   902   O  O   . LYS A  1 122 ? 32.231  128.268 9.101   1.00 19.14 ? 122 LYS A O   1 
ATOM   903   C  CB  . LYS A  1 122 ? 34.822  128.130 6.872   1.00 18.14 ? 122 LYS A CB  1 
ATOM   904   C  CG  . LYS A  1 122 ? 35.993  127.258 6.521   1.00 21.55 ? 122 LYS A CG  1 
ATOM   905   C  CD  . LYS A  1 122 ? 36.215  127.235 4.998   1.00 24.20 ? 122 LYS A CD  1 
ATOM   906   C  CE  . LYS A  1 122 ? 37.504  126.493 4.652   1.00 32.74 ? 122 LYS A CE  1 
ATOM   907   N  NZ  . LYS A  1 122 ? 37.940  126.734 3.248   1.00 42.21 ? 122 LYS A NZ  1 
ATOM   908   N  N   . ALA A  1 123 ? 32.879  129.979 7.789   1.00 15.70 ? 123 ALA A N   1 
ATOM   909   C  CA  . ALA A  1 123 ? 31.543  130.559 7.641   1.00 20.85 ? 123 ALA A CA  1 
ATOM   910   C  C   . ALA A  1 123 ? 30.588  129.632 6.891   1.00 13.03 ? 123 ALA A C   1 
ATOM   911   O  O   . ALA A  1 123 ? 30.977  128.950 5.945   1.00 15.49 ? 123 ALA A O   1 
ATOM   912   C  CB  . ALA A  1 123 ? 31.634  131.892 6.897   1.00 18.49 ? 123 ALA A CB  1 
ATOM   913   N  N   . ASP A  1 124 ? 29.342  129.612 7.335   1.00 13.51 ? 124 ASP A N   1 
ATOM   914   C  CA  . ASP A  1 124 ? 28.235  129.070 6.556   1.00 12.79 ? 124 ASP A CA  1 
ATOM   915   C  C   . ASP A  1 124 ? 27.943  130.121 5.484   1.00 15.42 ? 124 ASP A C   1 
ATOM   916   O  O   . ASP A  1 124 ? 27.714  131.283 5.827   1.00 15.94 ? 124 ASP A O   1 
ATOM   917   C  CB  . ASP A  1 124 ? 27.033  128.929 7.487   1.00 16.90 ? 124 ASP A CB  1 
ATOM   918   C  CG  . ASP A  1 124 ? 25.871  128.181 6.858   1.00 15.26 ? 124 ASP A CG  1 
ATOM   919   O  OD1 . ASP A  1 124 ? 25.669  128.307 5.627   1.00 12.60 ? 124 ASP A OD1 1 
ATOM   920   O  OD2 . ASP A  1 124 ? 25.162  127.468 7.609   1.00 12.73 ? 124 ASP A OD2 1 
ATOM   921   N  N   . ASP A  1 125 ? 27.970  129.751 4.199   1.00 17.05 ? 125 ASP A N   1 
ATOM   922   C  CA  . ASP A  1 125 ? 27.630  130.726 3.138   1.00 15.65 ? 125 ASP A CA  1 
ATOM   923   C  C   . ASP A  1 125 ? 26.116  130.945 2.940   1.00 17.22 ? 125 ASP A C   1 
ATOM   924   O  O   . ASP A  1 125 ? 25.693  131.521 1.940   1.00 17.84 ? 125 ASP A O   1 
ATOM   925   C  CB  . ASP A  1 125 ? 28.335  130.422 1.798   1.00 16.42 ? 125 ASP A CB  1 
ATOM   926   C  CG  . ASP A  1 125 ? 27.832  129.158 1.119   1.00 17.41 ? 125 ASP A CG  1 
ATOM   927   O  OD1 . ASP A  1 125 ? 26.702  128.708 1.386   1.00 16.16 ? 125 ASP A OD1 1 
ATOM   928   O  OD2 . ASP A  1 125 ? 28.573  128.601 0.284   1.00 19.30 ? 125 ASP A OD2 1 
ATOM   929   N  N   . LEU A  1 126 ? 25.318  130.468 3.891   1.00 12.89 ? 126 LEU A N   1 
ATOM   930   C  CA  . LEU A  1 126 ? 23.857  130.605 3.864   1.00 12.63 ? 126 LEU A CA  1 
ATOM   931   C  C   . LEU A  1 126 ? 23.181  130.159 2.555   1.00 18.98 ? 126 LEU A C   1 
ATOM   932   O  O   . LEU A  1 126 ? 22.077  130.589 2.242   1.00 19.40 ? 126 LEU A O   1 
ATOM   933   C  CB  . LEU A  1 126 ? 23.448  132.034 4.245   1.00 12.66 ? 126 LEU A CB  1 
ATOM   934   C  CG  . LEU A  1 126 ? 24.278  132.589 5.414   1.00 17.12 ? 126 LEU A CG  1 
ATOM   935   C  CD1 . LEU A  1 126 ? 23.975  134.054 5.716   1.00 19.48 ? 126 LEU A CD1 1 
ATOM   936   C  CD2 . LEU A  1 126 ? 24.049  131.741 6.652   1.00 12.90 ? 126 LEU A CD2 1 
ATOM   937   N  N   . GLY A  1 127 ? 23.844  129.295 1.794   1.00 15.81 ? 127 GLY A N   1 
ATOM   938   C  CA  . GLY A  1 127 ? 23.274  128.789 0.567   1.00 13.93 ? 127 GLY A CA  1 
ATOM   939   C  C   . GLY A  1 127 ? 23.441  129.717 -0.614  1.00 22.93 ? 127 GLY A C   1 
ATOM   940   O  O   . GLY A  1 127 ? 22.793  129.540 -1.643  1.00 24.00 ? 127 GLY A O   1 
ATOM   941   N  N   . LYS A  1 128 ? 24.314  130.709 -0.471  1.00 25.68 ? 128 LYS A N   1 
ATOM   942   C  CA  . LYS A  1 128 ? 24.521  131.702 -1.516  1.00 22.56 ? 128 LYS A CA  1 
ATOM   943   C  C   . LYS A  1 128 ? 25.892  131.545 -2.130  1.00 23.84 ? 128 LYS A C   1 
ATOM   944   O  O   . LYS A  1 128 ? 26.414  132.468 -2.740  1.00 29.49 ? 128 LYS A O   1 
ATOM   945   C  CB  . LYS A  1 128 ? 24.372  133.110 -0.942  1.00 23.74 ? 128 LYS A CB  1 
ATOM   946   C  CG  . LYS A  1 128 ? 23.011  133.382 -0.297  1.00 26.70 ? 128 LYS A CG  1 
ATOM   947   C  CD  . LYS A  1 128 ? 21.883  133.285 -1.311  1.00 31.43 ? 128 LYS A CD  1 
ATOM   948   C  CE  . LYS A  1 128 ? 20.569  133.911 -0.804  1.00 41.20 ? 128 LYS A CE  1 
ATOM   949   N  NZ  . LYS A  1 128 ? 19.822  133.066 0.187   1.00 40.70 ? 128 LYS A NZ  1 
ATOM   950   N  N   . GLY A  1 129 ? 26.485  130.371 -1.960  1.00 21.38 ? 129 GLY A N   1 
ATOM   951   C  CA  . GLY A  1 129 ? 27.812  130.108 -2.492  1.00 19.60 ? 129 GLY A CA  1 
ATOM   952   C  C   . GLY A  1 129 ? 27.926  129.830 -3.989  1.00 26.12 ? 129 GLY A C   1 
ATOM   953   O  O   . GLY A  1 129 ? 28.985  130.058 -4.567  1.00 26.99 ? 129 GLY A O   1 
ATOM   954   N  N   . GLY A  1 130 ? 26.872  129.328 -4.627  1.00 21.26 ? 130 GLY A N   1 
ATOM   955   C  CA  . GLY A  1 130 ? 26.928  129.106 -6.071  1.00 22.78 ? 130 GLY A CA  1 
ATOM   956   C  C   . GLY A  1 130 ? 27.411  127.741 -6.549  1.00 27.31 ? 130 GLY A C   1 
ATOM   957   O  O   . GLY A  1 130 ? 27.566  127.530 -7.755  1.00 32.28 ? 130 GLY A O   1 
ATOM   958   N  N   . ASN A  1 131 ? 27.652  126.812 -5.622  1.00 19.03 ? 131 ASN A N   1 
ATOM   959   C  CA  . ASN A  1 131 ? 27.990  125.433 -5.969  1.00 20.40 ? 131 ASN A CA  1 
ATOM   960   C  C   . ASN A  1 131 ? 27.015  124.460 -5.313  1.00 23.00 ? 131 ASN A C   1 
ATOM   961   O  O   . ASN A  1 131 ? 26.131  124.873 -4.555  1.00 19.39 ? 131 ASN A O   1 
ATOM   962   C  CB  . ASN A  1 131 ? 29.426  125.109 -5.560  1.00 22.96 ? 131 ASN A CB  1 
ATOM   963   C  CG  . ASN A  1 131 ? 29.705  125.440 -4.093  1.00 25.40 ? 131 ASN A CG  1 
ATOM   964   O  OD1 . ASN A  1 131 ? 28.964  125.033 -3.196  1.00 22.01 ? 131 ASN A OD1 1 
ATOM   965   N  ND2 . ASN A  1 131 ? 30.768  126.200 -3.852  1.00 25.88 ? 131 ASN A ND2 1 
ATOM   966   N  N   . GLU A  1 132 ? 27.166  123.172 -5.593  1.00 21.99 ? 132 GLU A N   1 
ATOM   967   C  CA  . GLU A  1 132 ? 26.216  122.200 -5.066  1.00 22.37 ? 132 GLU A CA  1 
ATOM   968   C  C   . GLU A  1 132 ? 26.236  122.178 -3.536  1.00 25.08 ? 132 GLU A C   1 
ATOM   969   O  O   . GLU A  1 132 ? 25.180  122.162 -2.887  1.00 20.34 ? 132 GLU A O   1 
ATOM   970   C  CB  . GLU A  1 132 ? 26.497  120.797 -5.603  1.00 22.98 ? 132 GLU A CB  1 
ATOM   971   C  CG  . GLU A  1 132 ? 25.405  119.816 -5.220  1.00 25.60 ? 132 GLU A CG  1 
ATOM   972   C  CD  . GLU A  1 132 ? 25.697  118.401 -5.672  1.00 30.04 ? 132 GLU A CD  1 
ATOM   973   O  OE1 . GLU A  1 132 ? 26.769  118.171 -6.278  1.00 23.23 ? 132 GLU A OE1 1 
ATOM   974   O  OE2 . GLU A  1 132 ? 24.849  117.516 -5.408  1.00 33.17 ? 132 GLU A OE2 1 
ATOM   975   N  N   . GLU A  1 133 ? 27.444  122.205 -2.975  1.00 25.00 ? 133 GLU A N   1 
ATOM   976   C  CA  . GLU A  1 133 ? 27.641  122.062 -1.531  1.00 25.99 ? 133 GLU A CA  1 
ATOM   977   C  C   . GLU A  1 133 ? 26.984  123.189 -0.744  1.00 22.28 ? 133 GLU A C   1 
ATOM   978   O  O   . GLU A  1 133 ? 26.550  122.985 0.372   1.00 20.19 ? 133 GLU A O   1 
ATOM   979   C  CB  . GLU A  1 133 ? 29.133  121.965 -1.187  1.00 28.57 ? 133 GLU A CB  1 
ATOM   980   C  CG  . GLU A  1 133 ? 29.443  120.848 -0.217  1.00 33.17 ? 133 GLU A CG  1 
ATOM   981   C  CD  . GLU A  1 133 ? 28.625  119.596 -0.500  1.00 38.98 ? 133 GLU A CD  1 
ATOM   982   O  OE1 . GLU A  1 133 ? 28.678  119.073 -1.640  1.00 44.68 ? 133 GLU A OE1 1 
ATOM   983   O  OE2 . GLU A  1 133 ? 27.906  119.144 0.418   1.00 40.99 ? 133 GLU A OE2 1 
ATOM   984   N  N   . SER A  1 134 ? 26.897  124.369 -1.354  1.00 21.52 ? 134 SER A N   1 
ATOM   985   C  CA  . SER A  1 134 ? 26.222  125.496 -0.741  1.00 19.08 ? 134 SER A CA  1 
ATOM   986   C  C   . SER A  1 134 ? 24.757  125.170 -0.431  1.00 19.50 ? 134 SER A C   1 
ATOM   987   O  O   . SER A  1 134 ? 24.224  125.595 0.586   1.00 16.52 ? 134 SER A O   1 
ATOM   988   C  CB  . SER A  1 134 ? 26.320  126.722 -1.646  1.00 19.61 ? 134 SER A CB  1 
ATOM   989   O  OG  . SER A  1 134 ? 25.946  127.896 -0.936  1.00 21.78 ? 134 SER A OG  1 
ATOM   990   N  N   . THR A  1 135 ? 24.119  124.407 -1.311  1.00 18.95 ? 135 THR A N   1 
ATOM   991   C  CA  . THR A  1 135 ? 22.721  124.046 -1.143  1.00 16.57 ? 135 THR A CA  1 
ATOM   992   C  C   . THR A  1 135 ? 22.530  122.892 -0.169  1.00 16.03 ? 135 THR A C   1 
ATOM   993   O  O   . THR A  1 135 ? 21.395  122.547 0.152   1.00 18.20 ? 135 THR A O   1 
ATOM   994   C  CB  . THR A  1 135 ? 22.072  123.652 -2.486  1.00 17.85 ? 135 THR A CB  1 
ATOM   995   O  OG1 . THR A  1 135 ? 22.647  122.426 -2.955  1.00 24.59 ? 135 THR A OG1 1 
ATOM   996   C  CG2 . THR A  1 135 ? 22.284  124.727 -3.519  1.00 14.41 ? 135 THR A CG2 1 
ATOM   997   N  N   . LYS A  1 136 ? 23.636  122.298 0.290   1.00 17.56 ? 136 LYS A N   1 
ATOM   998   C  CA  . LYS A  1 136 ? 23.590  121.222 1.295   1.00 21.93 ? 136 LYS A CA  1 
ATOM   999   C  C   . LYS A  1 136 ? 24.168  121.624 2.656   1.00 21.20 ? 136 LYS A C   1 
ATOM   1000  O  O   . LYS A  1 136 ? 23.505  121.479 3.697   1.00 21.30 ? 136 LYS A O   1 
ATOM   1001  C  CB  . LYS A  1 136 ? 24.348  119.983 0.810   1.00 24.20 ? 136 LYS A CB  1 
ATOM   1002  C  CG  . LYS A  1 136 ? 23.901  119.452 -0.540  1.00 30.67 ? 136 LYS A CG  1 
ATOM   1003  C  CD  . LYS A  1 136 ? 24.574  118.118 -0.835  1.00 35.84 ? 136 LYS A CD  1 
ATOM   1004  C  CE  . LYS A  1 136 ? 24.359  117.691 -2.275  1.00 38.95 ? 136 LYS A CE  1 
ATOM   1005  N  NZ  . LYS A  1 136 ? 22.948  117.358 -2.605  1.00 39.91 ? 136 LYS A NZ  1 
ATOM   1006  N  N   . THR A  1 137 ? 25.408  122.109 2.659   1.00 16.63 ? 137 THR A N   1 
ATOM   1007  C  CA  . THR A  1 137 ? 26.111  122.328 3.919   1.00 17.21 ? 137 THR A CA  1 
ATOM   1008  C  C   . THR A  1 137 ? 26.400  123.789 4.172   1.00 17.01 ? 137 THR A C   1 
ATOM   1009  O  O   . THR A  1 137 ? 26.576  124.187 5.311   1.00 14.90 ? 137 THR A O   1 
ATOM   1010  C  CB  . THR A  1 137 ? 27.439  121.572 3.961   1.00 21.43 ? 137 THR A CB  1 
ATOM   1011  O  OG1 . THR A  1 137 ? 28.275  122.025 2.893   1.00 17.59 ? 137 THR A OG1 1 
ATOM   1012  C  CG2 . THR A  1 137 ? 27.195  120.071 3.824   1.00 23.90 ? 137 THR A CG2 1 
ATOM   1013  N  N   . GLY A  1 138 ? 26.424  124.597 3.117   1.00 14.79 ? 138 GLY A N   1 
ATOM   1014  C  CA  . GLY A  1 138 ? 26.841  125.982 3.270   1.00 13.88 ? 138 GLY A CA  1 
ATOM   1015  C  C   . GLY A  1 138 ? 28.355  126.151 3.173   1.00 15.43 ? 138 GLY A C   1 
ATOM   1016  O  O   . GLY A  1 138 ? 28.859  127.259 3.341   1.00 15.58 ? 138 GLY A O   1 
ATOM   1017  N  N   . ASN A  1 139 ? 29.072  125.064 2.875   1.00 14.88 ? 139 ASN A N   1 
ATOM   1018  C  CA  . ASN A  1 139 ? 30.541  125.091 2.738   1.00 18.07 ? 139 ASN A CA  1 
ATOM   1019  C  C   . ASN A  1 139 ? 31.251  125.585 4.003   1.00 14.78 ? 139 ASN A C   1 
ATOM   1020  O  O   . ASN A  1 139 ? 32.229  126.318 3.899   1.00 16.31 ? 139 ASN A O   1 
ATOM   1021  C  CB  . ASN A  1 139 ? 31.017  125.948 1.531   1.00 17.34 ? 139 ASN A CB  1 
ATOM   1022  C  CG  . ASN A  1 139 ? 30.456  125.467 0.176   1.00 23.17 ? 139 ASN A CG  1 
ATOM   1023  O  OD1 . ASN A  1 139 ? 30.899  124.455 -0.380  1.00 24.01 ? 139 ASN A OD1 1 
ATOM   1024  N  ND2 . ASN A  1 139 ? 29.490  126.215 -0.365  1.00 19.57 ? 139 ASN A ND2 1 
ATOM   1025  N  N   . ALA A  1 140 ? 30.781  125.177 5.186   1.00 13.47 ? 140 ALA A N   1 
ATOM   1026  C  CA  . ALA A  1 140 ? 31.373  125.662 6.435   1.00 14.00 ? 140 ALA A CA  1 
ATOM   1027  C  C   . ALA A  1 140 ? 32.585  124.833 6.896   1.00 14.68 ? 140 ALA A C   1 
ATOM   1028  O  O   . ALA A  1 140 ? 33.103  125.036 7.992   1.00 15.97 ? 140 ALA A O   1 
ATOM   1029  C  CB  . ALA A  1 140 ? 30.337  125.779 7.539   1.00 12.54 ? 140 ALA A CB  1 
ATOM   1030  N  N   . GLY A  1 141 ? 33.055  123.946 6.027   1.00 14.16 ? 141 GLY A N   1 
ATOM   1031  C  CA  . GLY A  1 141 ? 34.226  123.135 6.292   1.00 15.78 ? 141 GLY A CA  1 
ATOM   1032  C  C   . GLY A  1 141 ? 34.066  122.253 7.523   1.00 16.76 ? 141 GLY A C   1 
ATOM   1033  O  O   . GLY A  1 141 ? 32.960  121.838 7.860   1.00 18.73 ? 141 GLY A O   1 
ATOM   1034  N  N   . SER A  1 142 ? 35.174  122.010 8.212   1.00 16.02 ? 142 SER A N   1 
ATOM   1035  C  CA  . SER A  1 142 ? 35.264  120.969 9.235   1.00 20.08 ? 142 SER A CA  1 
ATOM   1036  C  C   . SER A  1 142 ? 34.340  121.134 10.421  1.00 15.14 ? 142 SER A C   1 
ATOM   1037  O  O   . SER A  1 142 ? 34.010  122.246 10.812  1.00 14.51 ? 142 SER A O   1 
ATOM   1038  C  CB  . SER A  1 142 ? 36.692  120.908 9.793   1.00 18.16 ? 142 SER A CB  1 
ATOM   1039  O  OG  . SER A  1 142 ? 37.529  120.197 8.915   1.00 33.17 ? 142 SER A OG  1 
ATOM   1040  N  N   . ARG A  1 143 ? 34.010  120.007 11.035  1.00 20.21 ? 143 ARG A N   1 
ATOM   1041  C  CA  . ARG A  1 143 ? 33.320  119.987 12.325  1.00 18.29 ? 143 ARG A CA  1 
ATOM   1042  C  C   . ARG A  1 143 ? 34.341  120.085 13.439  1.00 18.69 ? 143 ARG A C   1 
ATOM   1043  O  O   . ARG A  1 143 ? 35.021  119.107 13.735  1.00 20.83 ? 143 ARG A O   1 
ATOM   1044  C  CB  . ARG A  1 143 ? 32.508  118.695 12.447  1.00 19.34 ? 143 ARG A CB  1 
ATOM   1045  C  CG  . ARG A  1 143 ? 31.533  118.543 11.283  1.00 18.38 ? 143 ARG A CG  1 
ATOM   1046  C  CD  . ARG A  1 143 ? 30.846  117.188 11.160  1.00 22.94 ? 143 ARG A CD  1 
ATOM   1047  N  NE  . ARG A  1 143 ? 30.058  117.149 9.918   1.00 26.20 ? 143 ARG A NE  1 
ATOM   1048  C  CZ  . ARG A  1 143 ? 28.984  116.381 9.700   1.00 26.71 ? 143 ARG A CZ  1 
ATOM   1049  N  NH1 . ARG A  1 143 ? 28.535  115.549 10.638  1.00 21.39 ? 143 ARG A NH1 1 
ATOM   1050  N  NH2 . ARG A  1 143 ? 28.353  116.443 8.528   1.00 20.33 ? 143 ARG A NH2 1 
ATOM   1051  N  N   . LEU A  1 144 ? 34.454  121.266 14.049  1.00 15.97 ? 144 LEU A N   1 
ATOM   1052  C  CA  . LEU A  1 144 ? 35.456  121.508 15.091  1.00 13.01 ? 144 LEU A CA  1 
ATOM   1053  C  C   . LEU A  1 144 ? 35.074  120.972 16.471  1.00 17.54 ? 144 LEU A C   1 
ATOM   1054  O  O   . LEU A  1 144 ? 35.934  120.482 17.201  1.00 14.95 ? 144 LEU A O   1 
ATOM   1055  C  CB  . LEU A  1 144 ? 35.770  123.006 15.215  1.00 15.06 ? 144 LEU A CB  1 
ATOM   1056  C  CG  . LEU A  1 144 ? 36.408  123.705 14.008  1.00 19.55 ? 144 LEU A CG  1 
ATOM   1057  C  CD1 . LEU A  1 144 ? 36.602  125.199 14.285  1.00 18.42 ? 144 LEU A CD1 1 
ATOM   1058  C  CD2 . LEU A  1 144 ? 37.735  123.038 13.665  1.00 16.13 ? 144 LEU A CD2 1 
ATOM   1059  N  N   . ALA A  1 145 ? 33.798  121.105 16.844  1.00 12.86 ? 145 ALA A N   1 
ATOM   1060  C  CA  . ALA A  1 145 ? 33.327  120.625 18.136  1.00 14.35 ? 145 ALA A CA  1 
ATOM   1061  C  C   . ALA A  1 145 ? 31.859  120.255 18.016  1.00 15.85 ? 145 ALA A C   1 
ATOM   1062  O  O   . ALA A  1 145 ? 31.124  120.833 17.208  1.00 14.71 ? 145 ALA A O   1 
ATOM   1063  C  CB  . ALA A  1 145 ? 33.525  121.686 19.216  1.00 12.79 ? 145 ALA A CB  1 
ATOM   1064  N  N   . CYS A  1 146 ? 31.424  119.281 18.800  1.00 13.67 ? 146 CYS A N   1 
ATOM   1065  C  CA  . CYS A  1 146 ? 30.024  118.907 18.763  1.00 14.40 ? 146 CYS A CA  1 
ATOM   1066  C  C   . CYS A  1 146 ? 29.572  118.344 20.099  1.00 13.91 ? 146 CYS A C   1 
ATOM   1067  O  O   . CYS A  1 146 ? 30.385  118.057 20.969  1.00 13.12 ? 146 CYS A O   1 
ATOM   1068  C  CB  . CYS A  1 146 ? 29.763  117.918 17.640  1.00 12.05 ? 146 CYS A CB  1 
ATOM   1069  S  SG  . CYS A  1 146 ? 30.482  116.290 17.847  1.00 17.42 ? 146 CYS A SG  1 
ATOM   1070  N  N   . GLY A  1 147 ? 28.262  118.204 20.251  1.00 14.94 ? 147 GLY A N   1 
ATOM   1071  C  CA  . GLY A  1 147 ? 27.679  117.594 21.432  1.00 11.58 ? 147 GLY A CA  1 
ATOM   1072  C  C   . GLY A  1 147 ? 26.243  117.183 21.136  1.00 11.99 ? 147 GLY A C   1 
ATOM   1073  O  O   . GLY A  1 147 ? 25.603  117.711 20.222  1.00 11.19 ? 147 GLY A O   1 
ATOM   1074  N  N   . VAL A  1 148 ? 25.737  116.227 21.898  1.00 9.38  ? 148 VAL A N   1 
ATOM   1075  C  CA  . VAL A  1 148 ? 24.341  115.843 21.784  1.00 11.64 ? 148 VAL A CA  1 
ATOM   1076  C  C   . VAL A  1 148 ? 23.491  116.806 22.607  1.00 10.03 ? 148 VAL A C   1 
ATOM   1077  O  O   . VAL A  1 148 ? 23.886  117.211 23.692  1.00 8.91  ? 148 VAL A O   1 
ATOM   1078  C  CB  . VAL A  1 148 ? 24.161  114.401 22.246  1.00 13.10 ? 148 VAL A CB  1 
ATOM   1079  C  CG1 . VAL A  1 148 ? 22.694  113.957 22.116  1.00 7.32  ? 148 VAL A CG1 1 
ATOM   1080  C  CG2 . VAL A  1 148 ? 25.104  113.504 21.430  1.00 10.25 ? 148 VAL A CG2 1 
ATOM   1081  N  N   . ILE A  1 149 ? 22.334  117.193 22.080  1.00 11.04 ? 149 ILE A N   1 
ATOM   1082  C  CA  . ILE A  1 149 ? 21.485  118.163 22.766  1.00 8.50  ? 149 ILE A CA  1 
ATOM   1083  C  C   . ILE A  1 149 ? 20.634  117.407 23.790  1.00 9.74  ? 149 ILE A C   1 
ATOM   1084  O  O   . ILE A  1 149 ? 19.860  116.519 23.428  1.00 8.84  ? 149 ILE A O   1 
ATOM   1085  C  CB  . ILE A  1 149 ? 20.607  118.939 21.754  1.00 8.74  ? 149 ILE A CB  1 
ATOM   1086  C  CG1 . ILE A  1 149 ? 21.504  119.721 20.796  1.00 10.32 ? 149 ILE A CG1 1 
ATOM   1087  C  CG2 . ILE A  1 149 ? 19.624  119.847 22.469  1.00 10.62 ? 149 ILE A CG2 1 
ATOM   1088  C  CD1 . ILE A  1 149 ? 20.773  120.297 19.579  1.00 9.36  ? 149 ILE A CD1 1 
ATOM   1089  N  N   . GLY A  1 150 ? 20.804  117.747 25.067  1.00 10.59 ? 150 GLY A N   1 
ATOM   1090  C  CA  . GLY A  1 150 ? 20.204  117.000 26.166  1.00 9.43  ? 150 GLY A CA  1 
ATOM   1091  C  C   . GLY A  1 150 ? 19.154  117.787 26.922  1.00 8.80  ? 150 GLY A C   1 
ATOM   1092  O  O   . GLY A  1 150 ? 19.190  119.008 26.947  1.00 10.77 ? 150 GLY A O   1 
ATOM   1093  N  N   . ILE A  1 151 ? 18.194  117.089 27.517  1.00 10.72 ? 151 ILE A N   1 
ATOM   1094  C  CA  . ILE A  1 151 ? 17.173  117.761 28.325  1.00 11.88 ? 151 ILE A CA  1 
ATOM   1095  C  C   . ILE A  1 151 ? 17.837  118.330 29.566  1.00 10.42 ? 151 ILE A C   1 
ATOM   1096  O  O   . ILE A  1 151 ? 18.616  117.637 30.203  1.00 10.14 ? 151 ILE A O   1 
ATOM   1097  C  CB  . ILE A  1 151 ? 16.056  116.778 28.761  1.00 13.11 ? 151 ILE A CB  1 
ATOM   1098  C  CG1 . ILE A  1 151 ? 15.421  116.106 27.536  1.00 10.64 ? 151 ILE A CG1 1 
ATOM   1099  C  CG2 . ILE A  1 151 ? 15.011  117.489 29.582  1.00 10.36 ? 151 ILE A CG2 1 
ATOM   1100  C  CD1 . ILE A  1 151 ? 14.247  115.203 27.879  1.00 12.20 ? 151 ILE A CD1 1 
ATOM   1101  N  N   . ALA A  1 152 ? 17.559  119.593 29.895  1.00 12.11 ? 152 ALA A N   1 
ATOM   1102  C  CA  . ALA A  1 152 ? 18.132  120.215 31.091  1.00 13.82 ? 152 ALA A CA  1 
ATOM   1103  C  C   . ALA A  1 152 ? 17.057  120.584 32.107  1.00 17.17 ? 152 ALA A C   1 
ATOM   1104  O  O   . ALA A  1 152 ? 15.866  120.613 31.795  1.00 15.13 ? 152 ALA A O   1 
ATOM   1105  C  CB  . ALA A  1 152 ? 18.947  121.447 30.731  1.00 13.01 ? 152 ALA A CB  1 
ATOM   1106  N  N   . GLN A  1 153 ? 17.502  120.868 33.321  1.00 18.65 ? 153 GLN A N   1 
ATOM   1107  C  CA  . GLN A  1 153 ? 16.612  121.202 34.425  1.00 25.35 ? 153 GLN A CA  1 
ATOM   1108  C  C   . GLN A  1 153 ? 16.145  122.641 34.286  1.00 26.86 ? 153 GLN A C   1 
ATOM   1109  O  O   . GLN A  1 153 ? 16.955  123.539 34.023  1.00 31.55 ? 153 GLN A O   1 
ATOM   1110  C  CB  . GLN A  1 153 ? 17.354  121.016 35.761  1.00 23.74 ? 153 GLN A CB  1 
ATOM   1111  C  CG  . GLN A  1 153 ? 16.485  121.166 37.001  1.00 25.89 ? 153 GLN A CG  1 
ATOM   1112  C  CD  . GLN A  1 153 ? 17.217  120.749 38.271  1.00 31.73 ? 153 GLN A CD  1 
ATOM   1113  O  OE1 . GLN A  1 153 ? 18.397  121.064 38.456  1.00 35.11 ? 153 GLN A OE1 1 
ATOM   1114  N  NE2 . GLN A  1 153 ? 16.529  120.019 39.138  1.00 25.89 ? 153 GLN A NE2 1 
ATOM   1115  O  OXT . GLN A  1 153 ? 14.966  122.943 34.438  1.00 29.29 ? 153 GLN A OXT 1 
ATOM   1116  N  N   . ALA B  1 1   ? 10.241  101.902 14.322  1.00 43.02 ? 1   ALA B N   1 
ATOM   1117  C  CA  . ALA B  1 1   ? 11.552  101.314 14.607  1.00 36.57 ? 1   ALA B CA  1 
ATOM   1118  C  C   . ALA B  1 1   ? 12.630  102.361 14.923  1.00 27.68 ? 1   ALA B C   1 
ATOM   1119  O  O   . ALA B  1 1   ? 13.611  102.497 14.188  1.00 33.29 ? 1   ALA B O   1 
ATOM   1120  C  CB  . ALA B  1 1   ? 12.000  100.399 13.441  1.00 29.34 ? 1   ALA B CB  1 
ATOM   1121  N  N   . THR B  1 2   ? 12.463  103.097 16.015  1.00 26.27 ? 2   THR B N   1 
ATOM   1122  C  CA  . THR B  1 2   ? 13.476  104.078 16.377  1.00 19.47 ? 2   THR B CA  1 
ATOM   1123  C  C   . THR B  1 2   ? 14.736  103.434 16.979  1.00 18.47 ? 2   THR B C   1 
ATOM   1124  O  O   . THR B  1 2   ? 14.717  102.306 17.502  1.00 14.01 ? 2   THR B O   1 
ATOM   1125  C  CB  . THR B  1 2   ? 12.951  105.213 17.297  1.00 17.40 ? 2   THR B CB  1 
ATOM   1126  O  OG1 . THR B  1 2   ? 11.733  104.816 17.926  1.00 27.01 ? 2   THR B OG1 1 
ATOM   1127  C  CG2 . THR B  1 2   ? 12.718  106.501 16.506  1.00 25.06 ? 2   THR B CG2 1 
ATOM   1128  N  N   . LYS B  1 3   ? 15.831  104.173 16.870  1.00 11.53 ? 3   LYS B N   1 
ATOM   1129  C  CA  . LYS B  1 3   ? 17.121  103.749 17.378  1.00 14.70 ? 3   LYS B CA  1 
ATOM   1130  C  C   . LYS B  1 3   ? 17.755  104.914 18.104  1.00 11.96 ? 3   LYS B C   1 
ATOM   1131  O  O   . LYS B  1 3   ? 17.457  106.080 17.834  1.00 12.35 ? 3   LYS B O   1 
ATOM   1132  C  CB  . LYS B  1 3   ? 18.055  103.301 16.259  1.00 11.53 ? 3   LYS B CB  1 
ATOM   1133  C  CG  . LYS B  1 3   ? 17.546  102.138 15.448  1.00 18.98 ? 3   LYS B CG  1 
ATOM   1134  C  CD  . LYS B  1 3   ? 18.632  101.575 14.549  1.00 26.91 ? 3   LYS B CD  1 
ATOM   1135  C  CE  . LYS B  1 3   ? 18.038  100.698 13.450  1.00 40.36 ? 3   LYS B CE  1 
ATOM   1136  N  NZ  . LYS B  1 3   ? 19.081  100.054 12.604  1.00 42.68 ? 3   LYS B NZ  1 
ATOM   1137  N  N   . ALA B  1 4   ? 18.638  104.586 19.026  1.00 8.18  ? 4   ALA B N   1 
ATOM   1138  C  CA  . ALA B  1 4   ? 19.349  105.589 19.770  1.00 9.81  ? 4   ALA B CA  1 
ATOM   1139  C  C   . ALA B  1 4   ? 20.698  105.000 20.120  1.00 11.83 ? 4   ALA B C   1 
ATOM   1140  O  O   . ALA B  1 4   ? 20.934  103.801 19.946  1.00 12.16 ? 4   ALA B O   1 
ATOM   1141  C  CB  . ALA B  1 4   ? 18.559  105.985 21.038  1.00 7.51  ? 4   ALA B CB  1 
ATOM   1142  N  N   . VAL B  1 5   ? 21.588  105.838 20.615  1.00 8.73  ? 5   VAL B N   1 
ATOM   1143  C  CA  . VAL B  1 5   ? 22.939  105.401 20.844  1.00 9.07  ? 5   VAL B CA  1 
ATOM   1144  C  C   . VAL B  1 5   ? 23.534  106.356 21.862  1.00 9.15  ? 5   VAL B C   1 
ATOM   1145  O  O   . VAL B  1 5   ? 23.111  107.504 21.981  1.00 8.89  ? 5   VAL B O   1 
ATOM   1146  C  CB  . VAL B  1 5   ? 23.733  105.435 19.523  1.00 12.19 ? 5   VAL B CB  1 
ATOM   1147  C  CG1 . VAL B  1 5   ? 23.946  106.879 19.069  1.00 11.46 ? 5   VAL B CG1 1 
ATOM   1148  C  CG2 . VAL B  1 5   ? 25.048  104.707 19.651  1.00 8.88  ? 5   VAL B CG2 1 
ATOM   1149  N  N   . CYS B  1 6   ? 24.506  105.874 22.619  1.00 10.27 ? 6   CYS B N   1 
ATOM   1150  C  CA  . CYS B  1 6   ? 25.067  106.668 23.687  1.00 9.75  ? 6   CYS B CA  1 
ATOM   1151  C  C   . CYS B  1 6   ? 26.537  106.354 23.757  1.00 10.51 ? 6   CYS B C   1 
ATOM   1152  O  O   . CYS B  1 6   ? 26.930  105.183 23.818  1.00 11.49 ? 6   CYS B O   1 
ATOM   1153  C  CB  . CYS B  1 6   ? 24.403  106.301 25.007  1.00 6.52  ? 6   CYS B CB  1 
ATOM   1154  S  SG  . CYS B  1 6   ? 24.994  107.254 26.393  1.00 10.86 ? 6   CYS B SG  1 
ATOM   1155  N  N   . VAL B  1 7   ? 27.357  107.394 23.750  1.00 11.11 ? 7   VAL B N   1 
ATOM   1156  C  CA  . VAL B  1 7   ? 28.781  107.205 23.974  1.00 9.63  ? 7   VAL B CA  1 
ATOM   1157  C  C   . VAL B  1 7   ? 29.111  107.458 25.444  1.00 9.22  ? 7   VAL B C   1 
ATOM   1158  O  O   . VAL B  1 7   ? 28.910  108.550 25.963  1.00 10.18 ? 7   VAL B O   1 
ATOM   1159  C  CB  . VAL B  1 7   ? 29.630  108.073 23.016  1.00 13.84 ? 7   VAL B CB  1 
ATOM   1160  C  CG1 . VAL B  1 7   ? 31.131  107.940 23.351  1.00 11.06 ? 7   VAL B CG1 1 
ATOM   1161  C  CG2 . VAL B  1 7   ? 29.356  107.649 21.554  1.00 8.68  ? 7   VAL B CG2 1 
ATOM   1162  N  N   . LEU B  1 8   ? 29.588  106.427 26.120  1.00 9.88  ? 8   LEU B N   1 
ATOM   1163  C  CA  . LEU B  1 8   ? 29.972  106.533 27.530  1.00 8.52  ? 8   LEU B CA  1 
ATOM   1164  C  C   . LEU B  1 8   ? 31.452  106.920 27.721  1.00 8.35  ? 8   LEU B C   1 
ATOM   1165  O  O   . LEU B  1 8   ? 32.353  106.254 27.224  1.00 10.19 ? 8   LEU B O   1 
ATOM   1166  C  CB  . LEU B  1 8   ? 29.696  105.208 28.222  1.00 7.28  ? 8   LEU B CB  1 
ATOM   1167  C  CG  . LEU B  1 8   ? 28.207  104.798 28.263  1.00 10.69 ? 8   LEU B CG  1 
ATOM   1168  C  CD1 . LEU B  1 8   ? 28.040  103.352 28.672  1.00 9.59  ? 8   LEU B CD1 1 
ATOM   1169  C  CD2 . LEU B  1 8   ? 27.467  105.667 29.265  1.00 8.39  ? 8   LEU B CD2 1 
ATOM   1170  N  N   . LYS B  1 9   ? 31.690  107.988 28.464  1.00 10.08 ? 9   LYS B N   1 
ATOM   1171  C  CA  . LYS B  1 9   ? 33.030  108.482 28.742  1.00 10.83 ? 9   LYS B CA  1 
ATOM   1172  C  C   . LYS B  1 9   ? 33.014  109.076 30.143  1.00 11.19 ? 9   LYS B C   1 
ATOM   1173  O  O   . LYS B  1 9   ? 31.977  109.565 30.597  1.00 7.48  ? 9   LYS B O   1 
ATOM   1174  C  CB  . LYS B  1 9   ? 33.402  109.581 27.744  1.00 12.77 ? 9   LYS B CB  1 
ATOM   1175  C  CG  . LYS B  1 9   ? 33.618  109.091 26.317  1.00 17.78 ? 9   LYS B CG  1 
ATOM   1176  C  CD  . LYS B  1 9   ? 33.589  110.242 25.299  1.00 29.95 ? 9   LYS B CD  1 
ATOM   1177  C  CE  . LYS B  1 9   ? 34.894  111.017 25.268  1.00 38.23 ? 9   LYS B CE  1 
ATOM   1178  N  NZ  . LYS B  1 9   ? 35.993  110.249 24.593  1.00 44.41 ? 9   LYS B NZ  1 
ATOM   1179  N  N   . GLY B  1 10  ? 34.169  109.056 30.811  1.00 12.93 ? 10  GLY B N   1 
ATOM   1180  C  CA  . GLY B  1 10  ? 34.325  109.666 32.122  1.00 10.62 ? 10  GLY B CA  1 
ATOM   1181  C  C   . GLY B  1 10  ? 35.749  110.121 32.388  1.00 10.23 ? 10  GLY B C   1 
ATOM   1182  O  O   . GLY B  1 10  ? 36.533  110.293 31.469  1.00 9.85  ? 10  GLY B O   1 
ATOM   1183  N  N   . ASP B  1 11  ? 36.082  110.313 33.657  1.00 13.44 ? 11  ASP B N   1 
ATOM   1184  C  CA  . ASP B  1 11  ? 37.405  110.780 34.039  1.00 15.00 ? 11  ASP B CA  1 
ATOM   1185  C  C   . ASP B  1 11  ? 38.356  109.596 34.092  1.00 14.89 ? 11  ASP B C   1 
ATOM   1186  O  O   . ASP B  1 11  ? 39.572  109.769 34.029  1.00 20.14 ? 11  ASP B O   1 
ATOM   1187  C  CB  . ASP B  1 11  ? 37.360  111.478 35.407  1.00 17.88 ? 11  ASP B CB  1 
ATOM   1188  C  CG  . ASP B  1 11  ? 38.670  112.174 35.750  1.00 27.62 ? 11  ASP B CG  1 
ATOM   1189  O  OD1 . ASP B  1 11  ? 39.191  112.907 34.869  1.00 29.26 ? 11  ASP B OD1 1 
ATOM   1190  O  OD2 . ASP B  1 11  ? 39.193  111.975 36.882  1.00 25.89 ? 11  ASP B OD2 1 
ATOM   1191  N  N   . GLY B  1 12  ? 37.802  108.393 34.201  1.00 12.75 ? 12  GLY B N   1 
ATOM   1192  C  CA  . GLY B  1 12  ? 38.596  107.192 34.378  1.00 9.76  ? 12  GLY B CA  1 
ATOM   1193  C  C   . GLY B  1 12  ? 38.636  106.380 33.109  1.00 8.58  ? 12  GLY B C   1 
ATOM   1194  O  O   . GLY B  1 12  ? 38.310  106.899 32.055  1.00 9.48  ? 12  GLY B O   1 
ATOM   1195  N  N   . PRO B  1 13  ? 38.997  105.094 33.208  1.00 7.55  ? 13  PRO B N   1 
ATOM   1196  C  CA  . PRO B  1 13  ? 39.190  104.258 32.015  1.00 9.22  ? 13  PRO B CA  1 
ATOM   1197  C  C   . PRO B  1 13  ? 37.912  103.675 31.402  1.00 11.64 ? 13  PRO B C   1 
ATOM   1198  O  O   . PRO B  1 13  ? 38.000  102.981 30.388  1.00 13.70 ? 13  PRO B O   1 
ATOM   1199  C  CB  . PRO B  1 13  ? 40.044  103.105 32.543  1.00 9.31  ? 13  PRO B CB  1 
ATOM   1200  C  CG  . PRO B  1 13  ? 39.652  102.964 33.972  1.00 8.69  ? 13  PRO B CG  1 
ATOM   1201  C  CD  . PRO B  1 13  ? 39.370  104.391 34.445  1.00 8.70  ? 13  PRO B CD  1 
ATOM   1202  N  N   . VAL B  1 14  ? 36.747  103.930 31.978  1.00 10.37 ? 14  VAL B N   1 
ATOM   1203  C  CA  . VAL B  1 14  ? 35.531  103.297 31.450  1.00 9.71  ? 14  VAL B CA  1 
ATOM   1204  C  C   . VAL B  1 14  ? 35.089  104.002 30.184  1.00 11.12 ? 14  VAL B C   1 
ATOM   1205  O  O   . VAL B  1 14  ? 34.838  105.203 30.211  1.00 11.85 ? 14  VAL B O   1 
ATOM   1206  C  CB  . VAL B  1 14  ? 34.369  103.357 32.463  1.00 10.81 ? 14  VAL B CB  1 
ATOM   1207  C  CG1 . VAL B  1 14  ? 33.080  102.889 31.822  1.00 6.98  ? 14  VAL B CG1 1 
ATOM   1208  C  CG2 . VAL B  1 14  ? 34.706  102.549 33.744  1.00 7.34  ? 14  VAL B CG2 1 
ATOM   1209  N  N   . GLN B  1 15  ? 34.984  103.251 29.088  1.00 8.61  ? 15  GLN B N   1 
ATOM   1210  C  CA  . GLN B  1 15  ? 34.651  103.798 27.786  1.00 12.43 ? 15  GLN B CA  1 
ATOM   1211  C  C   . GLN B  1 15  ? 33.731  102.799 27.133  1.00 11.62 ? 15  GLN B C   1 
ATOM   1212  O  O   . GLN B  1 15  ? 33.968  101.590 27.219  1.00 10.33 ? 15  GLN B O   1 
ATOM   1213  C  CB  . GLN B  1 15  ? 35.875  103.885 26.884  1.00 12.84 ? 15  GLN B CB  1 
ATOM   1214  C  CG  . GLN B  1 15  ? 37.045  104.673 27.399  1.00 17.68 ? 15  GLN B CG  1 
ATOM   1215  C  CD  . GLN B  1 15  ? 38.130  104.766 26.337  1.00 17.61 ? 15  GLN B CD  1 
ATOM   1216  O  OE1 . GLN B  1 15  ? 38.068  105.624 25.473  1.00 23.15 ? 15  GLN B OE1 1 
ATOM   1217  N  NE2 . GLN B  1 15  ? 39.106  103.854 26.380  1.00 16.35 ? 15  GLN B NE2 1 
ATOM   1218  N  N   . GLY B  1 16  ? 32.679  103.285 26.484  1.00 9.56  ? 16  GLY B N   1 
ATOM   1219  C  CA  . GLY B  1 16  ? 31.791  102.371 25.794  1.00 9.22  ? 16  GLY B CA  1 
ATOM   1220  C  C   . GLY B  1 16  ? 30.747  102.991 24.900  1.00 7.99  ? 16  GLY B C   1 
ATOM   1221  O  O   . GLY B  1 16  ? 30.514  104.196 24.923  1.00 8.74  ? 16  GLY B O   1 
ATOM   1222  N  N   . ILE B  1 17  ? 30.105  102.132 24.125  1.00 9.11  ? 17  ILE B N   1 
ATOM   1223  C  CA  . ILE B  1 17  ? 29.053  102.525 23.213  1.00 9.66  ? 17  ILE B CA  1 
ATOM   1224  C  C   . ILE B  1 17  ? 27.857  101.646 23.509  1.00 10.31 ? 17  ILE B C   1 
ATOM   1225  O  O   . ILE B  1 17  ? 27.956  100.426 23.461  1.00 12.07 ? 17  ILE B O   1 
ATOM   1226  C  CB  . ILE B  1 17  ? 29.489  102.307 21.760  1.00 10.50 ? 17  ILE B CB  1 
ATOM   1227  C  CG1 . ILE B  1 17  ? 30.688  103.207 21.424  1.00 16.13 ? 17  ILE B CG1 1 
ATOM   1228  C  CG2 . ILE B  1 17  ? 28.329  102.559 20.800  1.00 9.55  ? 17  ILE B CG2 1 
ATOM   1229  C  CD1 . ILE B  1 17  ? 31.173  103.081 19.960  1.00 13.91 ? 17  ILE B CD1 1 
ATOM   1230  N  N   . ILE B  1 18  ? 26.732  102.258 23.839  1.00 9.34  ? 18  ILE B N   1 
ATOM   1231  C  CA  . ILE B  1 18  ? 25.512  101.499 24.107  1.00 9.09  ? 18  ILE B CA  1 
ATOM   1232  C  C   . ILE B  1 18  ? 24.455  101.842 23.078  1.00 9.89  ? 18  ILE B C   1 
ATOM   1233  O  O   . ILE B  1 18  ? 24.160  103.022 22.885  1.00 8.86  ? 18  ILE B O   1 
ATOM   1234  C  CB  . ILE B  1 18  ? 24.951  101.808 25.511  1.00 7.69  ? 18  ILE B CB  1 
ATOM   1235  C  CG1 . ILE B  1 18  ? 25.898  101.296 26.608  1.00 8.49  ? 18  ILE B CG1 1 
ATOM   1236  C  CG2 . ILE B  1 18  ? 23.551  101.198 25.696  1.00 5.50  ? 18  ILE B CG2 1 
ATOM   1237  C  CD1 . ILE B  1 18  ? 26.195  99.776  26.509  1.00 6.93  ? 18  ILE B CD1 1 
ATOM   1238  N  N   . ASN B  1 19  ? 23.885  100.812 22.441  1.00 8.79  ? 19  ASN B N   1 
ATOM   1239  C  CA  . ASN B  1 19  ? 22.805  100.967 21.462  1.00 10.16 ? 19  ASN B CA  1 
ATOM   1240  C  C   . ASN B  1 19  ? 21.413  100.685 22.043  1.00 12.57 ? 19  ASN B C   1 
ATOM   1241  O  O   . ASN B  1 19  ? 21.258  99.823  22.913  1.00 11.31 ? 19  ASN B O   1 
ATOM   1242  C  CB  . ASN B  1 19  ? 23.007  100.031 20.269  1.00 9.37  ? 19  ASN B CB  1 
ATOM   1243  C  CG  . ASN B  1 19  ? 24.381  100.167 19.642  1.00 13.57 ? 19  ASN B CG  1 
ATOM   1244  O  OD1 . ASN B  1 19  ? 24.627  101.082 18.860  1.00 13.40 ? 19  ASN B OD1 1 
ATOM   1245  N  ND2 . ASN B  1 19  ? 25.287  99.246  19.981  1.00 13.66 ? 19  ASN B ND2 1 
ATOM   1246  N  N   . PHE B  1 20  ? 20.410  101.391 21.521  1.00 9.64  ? 20  PHE B N   1 
ATOM   1247  C  CA  . PHE B  1 20  ? 19.005  101.160 21.863  1.00 11.83 ? 20  PHE B CA  1 
ATOM   1248  C  C   . PHE B  1 20  ? 18.189  100.928 20.599  1.00 11.51 ? 20  PHE B C   1 
ATOM   1249  O  O   . PHE B  1 20  ? 18.368  101.610 19.586  1.00 14.97 ? 20  PHE B O   1 
ATOM   1250  C  CB  . PHE B  1 20  ? 18.406  102.351 22.607  1.00 8.19  ? 20  PHE B CB  1 
ATOM   1251  C  CG  . PHE B  1 20  ? 19.148  102.728 23.853  1.00 8.17  ? 20  PHE B CG  1 
ATOM   1252  C  CD1 . PHE B  1 20  ? 20.281  103.521 23.779  1.00 7.54  ? 20  PHE B CD1 1 
ATOM   1253  C  CD2 . PHE B  1 20  ? 18.701  102.315 25.095  1.00 7.19  ? 20  PHE B CD2 1 
ATOM   1254  C  CE1 . PHE B  1 20  ? 20.960  103.875 24.899  1.00 7.06  ? 20  PHE B CE1 1 
ATOM   1255  C  CE2 . PHE B  1 20  ? 19.366  102.680 26.228  1.00 8.23  ? 20  PHE B CE2 1 
ATOM   1256  C  CZ  . PHE B  1 20  ? 20.509  103.444 26.138  1.00 7.16  ? 20  PHE B CZ  1 
ATOM   1257  N  N   . GLU B  1 21  ? 17.283  99.970  20.644  1.00 11.01 ? 21  GLU B N   1 
ATOM   1258  C  CA  . GLU B  1 21  ? 16.423  99.752  19.494  1.00 12.29 ? 21  GLU B CA  1 
ATOM   1259  C  C   . GLU B  1 21  ? 15.034  99.414  19.973  1.00 14.90 ? 21  GLU B C   1 
ATOM   1260  O  O   . GLU B  1 21  ? 14.867  98.586  20.874  1.00 13.33 ? 21  GLU B O   1 
ATOM   1261  C  CB  . GLU B  1 21  ? 16.975  98.644  18.599  1.00 13.27 ? 21  GLU B CB  1 
ATOM   1262  C  CG  . GLU B  1 21  ? 16.134  98.365  17.351  1.00 25.35 ? 21  GLU B CG  1 
ATOM   1263  C  CD  . GLU B  1 21  ? 16.939  97.666  16.258  1.00 33.05 ? 21  GLU B CD  1 
ATOM   1264  O  OE1 . GLU B  1 21  ? 16.499  97.656  15.083  1.00 35.53 ? 21  GLU B OE1 1 
ATOM   1265  O  OE2 . GLU B  1 21  ? 18.024  97.133  16.580  1.00 31.35 ? 21  GLU B OE2 1 
ATOM   1266  N  N   . GLN B  1 22  ? 14.040  100.084 19.396  1.00 13.86 ? 22  GLN B N   1 
ATOM   1267  C  CA  . GLN B  1 22  ? 12.655  99.836  19.745  1.00 16.34 ? 22  GLN B CA  1 
ATOM   1268  C  C   . GLN B  1 22  ? 11.872  99.742  18.454  1.00 17.45 ? 22  GLN B C   1 
ATOM   1269  O  O   . GLN B  1 22  ? 11.593  100.752 17.846  1.00 23.97 ? 22  GLN B O   1 
ATOM   1270  C  CB  . GLN B  1 22  ? 12.104  100.970 20.618  1.00 14.55 ? 22  GLN B CB  1 
ATOM   1271  C  CG  . GLN B  1 22  ? 10.705  100.698 21.189  1.00 16.53 ? 22  GLN B CG  1 
ATOM   1272  C  CD  . GLN B  1 22  ? 10.191  101.860 22.011  1.00 13.79 ? 22  GLN B CD  1 
ATOM   1273  O  OE1 . GLN B  1 22  ? 10.542  103.009 21.748  1.00 13.17 ? 22  GLN B OE1 1 
ATOM   1274  N  NE2 . GLN B  1 22  ? 9.386   101.568 23.042  1.00 16.82 ? 22  GLN B NE2 1 
ATOM   1275  N  N   . LYS B  1 23  ? 11.508  98.531  18.049  1.00 20.16 ? 23  LYS B N   1 
ATOM   1276  C  CA  . LYS B  1 23  ? 10.863  98.323  16.751  1.00 28.30 ? 23  LYS B CA  1 
ATOM   1277  C  C   . LYS B  1 23  ? 9.458   98.895  16.685  1.00 27.79 ? 23  LYS B C   1 
ATOM   1278  O  O   . LYS B  1 23  ? 9.058   99.425  15.650  1.00 30.62 ? 23  LYS B O   1 
ATOM   1279  C  CB  . LYS B  1 23  ? 10.862  96.845  16.352  1.00 30.35 ? 23  LYS B CB  1 
ATOM   1280  C  CG  . LYS B  1 23  ? 12.265  96.277  16.070  1.00 36.47 ? 23  LYS B CG  1 
ATOM   1281  C  CD  . LYS B  1 23  ? 12.236  94.752  15.979  1.00 40.72 ? 23  LYS B CD  1 
ATOM   1282  C  CE  . LYS B  1 23  ? 13.641  94.160  15.828  1.00 46.35 ? 23  LYS B CE  1 
ATOM   1283  N  NZ  . LYS B  1 23  ? 13.624  92.657  15.804  1.00 44.94 ? 23  LYS B NZ  1 
ATOM   1284  N  N   . GLU B  1 24  ? 8.714   98.800  17.781  1.00 24.07 ? 24  GLU B N   1 
ATOM   1285  C  CA  . GLU B  1 24  ? 7.373   99.380  17.839  1.00 23.31 ? 24  GLU B CA  1 
ATOM   1286  C  C   . GLU B  1 24  ? 7.152   100.235 19.078  1.00 28.82 ? 24  GLU B C   1 
ATOM   1287  O  O   . GLU B  1 24  ? 7.707   99.953  20.143  1.00 23.53 ? 24  GLU B O   1 
ATOM   1288  C  CB  . GLU B  1 24  ? 6.315   98.295  17.767  1.00 31.99 ? 24  GLU B CB  1 
ATOM   1289  C  CG  . GLU B  1 24  ? 6.735   97.004  18.401  1.00 33.76 ? 24  GLU B CG  1 
ATOM   1290  C  CD  . GLU B  1 24  ? 6.615   95.842  17.439  1.00 49.74 ? 24  GLU B CD  1 
ATOM   1291  O  OE1 . GLU B  1 24  ? 6.315   96.105  16.252  1.00 51.10 ? 24  GLU B OE1 1 
ATOM   1292  O  OE2 . GLU B  1 24  ? 6.811   94.674  17.862  1.00 55.96 ? 24  GLU B OE2 1 
ATOM   1293  N  N   . SER B  1 25  ? 6.333   101.276 18.936  1.00 24.62 ? 25  SER B N   1 
ATOM   1294  C  CA  . SER B  1 25  ? 6.199   102.289 19.977  1.00 27.53 ? 25  SER B CA  1 
ATOM   1295  C  C   . SER B  1 25  ? 5.678   101.717 21.295  1.00 25.80 ? 25  SER B C   1 
ATOM   1296  O  O   . SER B  1 25  ? 5.991   102.215 22.378  1.00 28.36 ? 25  SER B O   1 
ATOM   1297  C  CB  . SER B  1 25  ? 5.293   103.423 19.495  1.00 28.86 ? 25  SER B CB  1 
ATOM   1298  O  OG  . SER B  1 25  ? 4.055   102.908 19.037  1.00 36.61 ? 25  SER B OG  1 
ATOM   1299  N  N   . ASN B  1 26  ? 4.892   100.656 21.201  1.00 23.63 ? 26  ASN B N   1 
ATOM   1300  C  CA  . ASN B  1 26  ? 4.327   100.032 22.393  1.00 27.61 ? 26  ASN B CA  1 
ATOM   1301  C  C   . ASN B  1 26  ? 5.192   98.871  22.897  1.00 31.97 ? 26  ASN B C   1 
ATOM   1302  O  O   . ASN B  1 26  ? 4.746   98.063  23.716  1.00 34.00 ? 26  ASN B O   1 
ATOM   1303  C  CB  . ASN B  1 26  ? 2.872   99.575  22.131  1.00 28.94 ? 26  ASN B CB  1 
ATOM   1304  C  CG  . ASN B  1 26  ? 2.773   98.420  21.120  1.00 36.92 ? 26  ASN B CG  1 
ATOM   1305  O  OD1 . ASN B  1 26  ? 3.653   98.231  20.266  1.00 38.31 ? 26  ASN B OD1 1 
ATOM   1306  N  ND2 . ASN B  1 26  ? 1.685   97.646  21.213  1.00 28.90 ? 26  ASN B ND2 1 
ATOM   1307  N  N   . GLY B  1 27  ? 6.434   98.801  22.415  1.00 23.91 ? 27  GLY B N   1 
ATOM   1308  C  CA  . GLY B  1 27  ? 7.211   97.587  22.548  1.00 23.30 ? 27  GLY B CA  1 
ATOM   1309  C  C   . GLY B  1 27  ? 8.437   97.712  23.430  1.00 19.69 ? 27  GLY B C   1 
ATOM   1310  O  O   . GLY B  1 27  ? 8.772   98.795  23.897  1.00 15.73 ? 27  GLY B O   1 
ATOM   1311  N  N   . PRO B  1 28  ? 9.101   96.580  23.667  1.00 17.03 ? 28  PRO B N   1 
ATOM   1312  C  CA  . PRO B  1 28  ? 10.324  96.472  24.468  1.00 18.58 ? 28  PRO B CA  1 
ATOM   1313  C  C   . PRO B  1 28  ? 11.479  97.207  23.792  1.00 15.42 ? 28  PRO B C   1 
ATOM   1314  O  O   . PRO B  1 28  ? 11.539  97.228  22.563  1.00 14.25 ? 28  PRO B O   1 
ATOM   1315  C  CB  . PRO B  1 28  ? 10.613  94.958  24.486  1.00 17.89 ? 28  PRO B CB  1 
ATOM   1316  C  CG  . PRO B  1 28  ? 9.363   94.295  24.038  1.00 25.78 ? 28  PRO B CG  1 
ATOM   1317  C  CD  . PRO B  1 28  ? 8.627   95.275  23.175  1.00 19.60 ? 28  PRO B CD  1 
ATOM   1318  N  N   . VAL B  1 29  ? 12.367  97.797  24.588  1.00 14.96 ? 29  VAL B N   1 
ATOM   1319  C  CA  . VAL B  1 29  ? 13.613  98.377  24.070  1.00 15.77 ? 29  VAL B CA  1 
ATOM   1320  C  C   . VAL B  1 29  ? 14.762  97.404  24.268  1.00 13.99 ? 29  VAL B C   1 
ATOM   1321  O  O   . VAL B  1 29  ? 15.030  96.995  25.396  1.00 14.88 ? 29  VAL B O   1 
ATOM   1322  C  CB  . VAL B  1 29  ? 14.003  99.702  24.803  1.00 12.43 ? 29  VAL B CB  1 
ATOM   1323  C  CG1 . VAL B  1 29  ? 15.282  100.314 24.181  1.00 9.62  ? 29  VAL B CG1 1 
ATOM   1324  C  CG2 . VAL B  1 29  ? 12.864  100.703 24.765  1.00 11.78 ? 29  VAL B CG2 1 
ATOM   1325  N  N   . LYS B  1 30  ? 15.455  97.047  23.194  1.00 11.15 ? 30  LYS B N   1 
ATOM   1326  C  CA  . LYS B  1 30  ? 16.686  96.287  23.327  1.00 14.62 ? 30  LYS B CA  1 
ATOM   1327  C  C   . LYS B  1 30  ? 17.860  97.222  23.529  1.00 12.78 ? 30  LYS B C   1 
ATOM   1328  O  O   . LYS B  1 30  ? 18.022  98.186  22.786  1.00 13.64 ? 30  LYS B O   1 
ATOM   1329  C  CB  . LYS B  1 30  ? 16.936  95.384  22.121  1.00 15.47 ? 30  LYS B CB  1 
ATOM   1330  C  CG  . LYS B  1 30  ? 15.943  94.228  22.003  1.00 23.45 ? 30  LYS B CG  1 
ATOM   1331  C  CD  . LYS B  1 30  ? 16.271  93.372  20.777  1.00 26.92 ? 30  LYS B CD  1 
ATOM   1332  C  CE  . LYS B  1 30  ? 15.148  92.406  20.421  1.00 28.55 ? 30  LYS B CE  1 
ATOM   1333  N  NZ  . LYS B  1 30  ? 15.625  91.416  19.409  1.00 29.56 ? 30  LYS B NZ  1 
ATOM   1334  N  N   . VAL B  1 31  ? 18.667  96.919  24.543  1.00 11.41 ? 31  VAL B N   1 
ATOM   1335  C  CA  . VAL B  1 31  ? 19.828  97.717  24.930  1.00 11.32 ? 31  VAL B CA  1 
ATOM   1336  C  C   . VAL B  1 31  ? 21.064  96.822  24.836  1.00 14.25 ? 31  VAL B C   1 
ATOM   1337  O  O   . VAL B  1 31  ? 21.159  95.818  25.539  1.00 13.45 ? 31  VAL B O   1 
ATOM   1338  C  CB  . VAL B  1 31  ? 19.681  98.225  26.369  1.00 11.09 ? 31  VAL B CB  1 
ATOM   1339  C  CG1 . VAL B  1 31  ? 20.788  99.188  26.720  1.00 8.10  ? 31  VAL B CG1 1 
ATOM   1340  C  CG2 . VAL B  1 31  ? 18.299  98.901  26.578  1.00 8.41  ? 31  VAL B CG2 1 
ATOM   1341  N  N   . TRP B  1 32  ? 22.002  97.150  23.953  1.00 11.80 ? 32  TRP B N   1 
ATOM   1342  C  CA  . TRP B  1 32  ? 23.207  96.318  23.828  1.00 14.18 ? 32  TRP B CA  1 
ATOM   1343  C  C   . TRP B  1 32  ? 24.428  97.128  23.419  1.00 13.38 ? 32  TRP B C   1 
ATOM   1344  O  O   . TRP B  1 32  ? 24.308  98.190  22.806  1.00 11.70 ? 32  TRP B O   1 
ATOM   1345  C  CB  . TRP B  1 32  ? 22.999  95.178  22.828  1.00 12.91 ? 32  TRP B CB  1 
ATOM   1346  C  CG  . TRP B  1 32  ? 23.147  95.630  21.416  1.00 16.94 ? 32  TRP B CG  1 
ATOM   1347  C  CD1 . TRP B  1 32  ? 24.278  95.550  20.637  1.00 17.01 ? 32  TRP B CD1 1 
ATOM   1348  C  CD2 . TRP B  1 32  ? 22.147  96.254  20.606  1.00 14.97 ? 32  TRP B CD2 1 
ATOM   1349  N  NE1 . TRP B  1 32  ? 24.032  96.088  19.399  1.00 17.95 ? 32  TRP B NE1 1 
ATOM   1350  C  CE2 . TRP B  1 32  ? 22.733  96.526  19.355  1.00 16.12 ? 32  TRP B CE2 1 
ATOM   1351  C  CE3 . TRP B  1 32  ? 20.813  96.611  20.818  1.00 17.23 ? 32  TRP B CE3 1 
ATOM   1352  C  CZ2 . TRP B  1 32  ? 22.029  97.134  18.316  1.00 21.10 ? 32  TRP B CZ2 1 
ATOM   1353  C  CZ3 . TRP B  1 32  ? 20.113  97.211  19.782  1.00 18.86 ? 32  TRP B CZ3 1 
ATOM   1354  C  CH2 . TRP B  1 32  ? 20.723  97.457  18.542  1.00 20.58 ? 32  TRP B CH2 1 
ATOM   1355  N  N   . GLY B  1 33  ? 25.609  96.615  23.742  1.00 14.74 ? 33  GLY B N   1 
ATOM   1356  C  CA  . GLY B  1 33  ? 26.837  97.323  23.432  1.00 12.32 ? 33  GLY B CA  1 
ATOM   1357  C  C   . GLY B  1 33  ? 27.956  96.785  24.291  1.00 14.76 ? 33  GLY B C   1 
ATOM   1358  O  O   . GLY B  1 33  ? 27.741  95.881  25.098  1.00 17.26 ? 33  GLY B O   1 
ATOM   1359  N  N   . SER B  1 34  ? 29.149  97.342  24.120  1.00 11.58 ? 34  SER B N   1 
ATOM   1360  C  CA  . SER B  1 34  ? 30.317  96.904  24.856  1.00 11.00 ? 34  SER B CA  1 
ATOM   1361  C  C   . SER B  1 34  ? 30.823  98.036  25.738  1.00 10.16 ? 34  SER B C   1 
ATOM   1362  O  O   . SER B  1 34  ? 30.913  99.178  25.298  1.00 12.06 ? 34  SER B O   1 
ATOM   1363  C  CB  . SER B  1 34  ? 31.399  96.503  23.862  1.00 10.65 ? 34  SER B CB  1 
ATOM   1364  O  OG  . SER B  1 34  ? 32.566  96.122  24.553  1.00 22.72 ? 34  SER B OG  1 
ATOM   1365  N  N   . ILE B  1 35  ? 31.131  97.745  26.990  1.00 10.40 ? 35  ILE B N   1 
ATOM   1366  C  CA  . ILE B  1 35  ? 31.770  98.735  27.837  1.00 8.30  ? 35  ILE B CA  1 
ATOM   1367  C  C   . ILE B  1 35  ? 33.070  98.149  28.348  1.00 13.24 ? 35  ILE B C   1 
ATOM   1368  O  O   . ILE B  1 35  ? 33.067  97.032  28.882  1.00 15.10 ? 35  ILE B O   1 
ATOM   1369  C  CB  . ILE B  1 35  ? 30.921  99.102  29.054  1.00 8.87  ? 35  ILE B CB  1 
ATOM   1370  C  CG1 . ILE B  1 35  ? 29.459  99.416  28.652  1.00 13.81 ? 35  ILE B CG1 1 
ATOM   1371  C  CG2 . ILE B  1 35  ? 31.547  100.279 29.789  1.00 6.19  ? 35  ILE B CG2 1 
ATOM   1372  C  CD1 . ILE B  1 35  ? 28.587  99.846  29.862  1.00 9.72  ? 35  ILE B CD1 1 
ATOM   1373  N  N   . LYS B  1 36  ? 34.180  98.876  28.200  1.00 10.48 ? 36  LYS B N   1 
ATOM   1374  C  CA  . LYS B  1 36  ? 35.463  98.337  28.657  1.00 10.64 ? 36  LYS B CA  1 
ATOM   1375  C  C   . LYS B  1 36  ? 36.036  99.213  29.753  1.00 11.41 ? 36  LYS B C   1 
ATOM   1376  O  O   . LYS B  1 36  ? 35.491  100.278 30.015  1.00 11.42 ? 36  LYS B O   1 
ATOM   1377  C  CB  . LYS B  1 36  ? 36.441  98.207  27.486  1.00 13.84 ? 36  LYS B CB  1 
ATOM   1378  C  CG  . LYS B  1 36  ? 36.806  99.528  26.844  1.00 17.16 ? 36  LYS B CG  1 
ATOM   1379  C  CD  . LYS B  1 36  ? 37.670  99.336  25.583  1.00 20.69 ? 36  LYS B CD  1 
ATOM   1380  C  CE  . LYS B  1 36  ? 38.253  100.674 25.111  1.00 15.98 ? 36  LYS B CE  1 
ATOM   1381  N  NZ  . LYS B  1 36  ? 38.731  100.611 23.703  1.00 24.83 ? 36  LYS B NZ  1 
ATOM   1382  N  N   . GLY B  1 37  ? 37.112  98.769  30.410  1.00 10.76 ? 37  GLY B N   1 
ATOM   1383  C  CA  . GLY B  1 37  ? 37.726  99.542  31.488  1.00 10.68 ? 37  GLY B CA  1 
ATOM   1384  C  C   . GLY B  1 37  ? 37.063  99.484  32.869  1.00 10.68 ? 37  GLY B C   1 
ATOM   1385  O  O   . GLY B  1 37  ? 37.332  100.319 33.761  1.00 9.04  ? 37  GLY B O   1 
ATOM   1386  N  N   . LEU B  1 38  ? 36.201  98.492  33.054  1.00 10.06 ? 38  LEU B N   1 
ATOM   1387  C  CA  . LEU B  1 38  ? 35.455  98.352  34.283  1.00 12.45 ? 38  LEU B CA  1 
ATOM   1388  C  C   . LEU B  1 38  ? 36.106  97.307  35.149  1.00 11.68 ? 38  LEU B C   1 
ATOM   1389  O  O   . LEU B  1 38  ? 36.653  96.344  34.639  1.00 13.96 ? 38  LEU B O   1 
ATOM   1390  C  CB  . LEU B  1 38  ? 34.009  97.893  33.978  1.00 11.48 ? 38  LEU B CB  1 
ATOM   1391  C  CG  . LEU B  1 38  ? 32.996  98.914  33.444  1.00 10.53 ? 38  LEU B CG  1 
ATOM   1392  C  CD1 . LEU B  1 38  ? 31.839  98.217  32.740  1.00 9.87  ? 38  LEU B CD1 1 
ATOM   1393  C  CD2 . LEU B  1 38  ? 32.464  99.781  34.565  1.00 10.00 ? 38  LEU B CD2 1 
ATOM   1394  N  N   . THR B  1 39  ? 35.996  97.456  36.465  1.00 13.38 ? 39  THR B N   1 
ATOM   1395  C  CA  . THR B  1 39  ? 36.416  96.379  37.331  1.00 17.21 ? 39  THR B CA  1 
ATOM   1396  C  C   . THR B  1 39  ? 35.460  95.213  37.183  1.00 13.64 ? 39  THR B C   1 
ATOM   1397  O  O   . THR B  1 39  ? 34.265  95.393  36.894  1.00 11.64 ? 39  THR B O   1 
ATOM   1398  C  CB  . THR B  1 39  ? 36.535  96.817  38.806  1.00 17.86 ? 39  THR B CB  1 
ATOM   1399  O  OG1 . THR B  1 39  ? 35.255  97.261  39.279  1.00 16.73 ? 39  THR B OG1 1 
ATOM   1400  C  CG2 . THR B  1 39  ? 37.567  97.952  38.939  1.00 13.42 ? 39  THR B CG2 1 
ATOM   1401  N  N   . GLU B  1 40  ? 36.005  94.020  37.381  1.00 11.05 ? 40  GLU B N   1 
ATOM   1402  C  CA  . GLU B  1 40  ? 35.283  92.771  37.205  1.00 17.97 ? 40  GLU B CA  1 
ATOM   1403  C  C   . GLU B  1 40  ? 34.107  92.721  38.146  1.00 15.75 ? 40  GLU B C   1 
ATOM   1404  O  O   . GLU B  1 40  ? 34.212  93.115  39.303  1.00 14.09 ? 40  GLU B O   1 
ATOM   1405  C  CB  . GLU B  1 40  ? 36.212  91.592  37.491  1.00 15.51 ? 40  GLU B CB  1 
ATOM   1406  C  CG  . GLU B  1 40  ? 35.654  90.229  37.114  1.00 21.29 ? 40  GLU B CG  1 
ATOM   1407  C  CD  . GLU B  1 40  ? 36.626  89.085  37.455  1.00 25.10 ? 40  GLU B CD  1 
ATOM   1408  O  OE1 . GLU B  1 40  ? 37.769  89.377  37.856  1.00 27.58 ? 40  GLU B OE1 1 
ATOM   1409  O  OE2 . GLU B  1 40  ? 36.247  87.901  37.331  1.00 26.83 ? 40  GLU B OE2 1 
ATOM   1410  N  N   . GLY B  1 41  ? 32.981  92.235  37.651  1.00 15.26 ? 41  GLY B N   1 
ATOM   1411  C  CA  . GLY B  1 41  ? 31.808  92.132  38.493  1.00 11.22 ? 41  GLY B CA  1 
ATOM   1412  C  C   . GLY B  1 41  ? 30.705  93.103  38.134  1.00 15.24 ? 41  GLY B C   1 
ATOM   1413  O  O   . GLY B  1 41  ? 30.655  93.641  37.022  1.00 14.30 ? 41  GLY B O   1 
ATOM   1414  N  N   . LEU B  1 42  ? 29.819  93.334  39.097  1.00 17.46 ? 42  LEU B N   1 
ATOM   1415  C  CA  . LEU B  1 42  ? 28.551  94.019  38.857  1.00 14.40 ? 42  LEU B CA  1 
ATOM   1416  C  C   . LEU B  1 42  ? 28.664  95.541  38.863  1.00 11.17 ? 42  LEU B C   1 
ATOM   1417  O  O   . LEU B  1 42  ? 29.342  96.116  39.700  1.00 13.18 ? 42  LEU B O   1 
ATOM   1418  C  CB  . LEU B  1 42  ? 27.556  93.600  39.941  1.00 16.16 ? 42  LEU B CB  1 
ATOM   1419  C  CG  . LEU B  1 42  ? 26.380  92.656  39.697  1.00 17.70 ? 42  LEU B CG  1 
ATOM   1420  C  CD1 . LEU B  1 42  ? 26.588  91.700  38.558  1.00 19.63 ? 42  LEU B CD1 1 
ATOM   1421  C  CD2 . LEU B  1 42  ? 26.075  91.909  40.984  1.00 21.21 ? 42  LEU B CD2 1 
ATOM   1422  N  N   . HIS B  1 43  ? 27.940  96.196  37.966  1.00 10.13 ? 43  HIS B N   1 
ATOM   1423  C  CA  . HIS B  1 43  ? 27.921  97.656  37.946  1.00 11.25 ? 43  HIS B CA  1 
ATOM   1424  C  C   . HIS B  1 43  ? 26.526  98.196  37.668  1.00 9.21  ? 43  HIS B C   1 
ATOM   1425  O  O   . HIS B  1 43  ? 25.898  97.800  36.701  1.00 9.64  ? 43  HIS B O   1 
ATOM   1426  C  CB  . HIS B  1 43  ? 28.893  98.177  36.877  1.00 9.84  ? 43  HIS B CB  1 
ATOM   1427  C  CG  . HIS B  1 43  ? 30.324  97.876  37.174  1.00 12.60 ? 43  HIS B CG  1 
ATOM   1428  N  ND1 . HIS B  1 43  ? 31.110  98.710  37.933  1.00 10.68 ? 43  HIS B ND1 1 
ATOM   1429  C  CD2 . HIS B  1 43  ? 31.101  96.818  36.843  1.00 8.75  ? 43  HIS B CD2 1 
ATOM   1430  C  CE1 . HIS B  1 43  ? 32.316  98.188  38.049  1.00 11.57 ? 43  HIS B CE1 1 
ATOM   1431  N  NE2 . HIS B  1 43  ? 32.337  97.043  37.397  1.00 12.15 ? 43  HIS B NE2 1 
ATOM   1432  N  N   . GLY B  1 44  ? 26.062  99.111  38.509  1.00 10.76 ? 44  GLY B N   1 
ATOM   1433  C  CA  . GLY B  1 44  ? 24.763  99.734  38.315  1.00 11.41 ? 44  GLY B CA  1 
ATOM   1434  C  C   . GLY B  1 44  ? 24.683  100.480 36.995  1.00 11.91 ? 44  GLY B C   1 
ATOM   1435  O  O   . GLY B  1 44  ? 25.660  101.079 36.538  1.00 9.68  ? 44  GLY B O   1 
ATOM   1436  N  N   . PHE B  1 45  ? 23.520  100.422 36.364  1.00 10.05 ? 45  PHE B N   1 
ATOM   1437  C  CA  . PHE B  1 45  ? 23.366  100.867 34.983  1.00 9.03  ? 45  PHE B CA  1 
ATOM   1438  C  C   . PHE B  1 45  ? 22.039  101.604 34.959  1.00 10.31 ? 45  PHE B C   1 
ATOM   1439  O  O   . PHE B  1 45  ? 20.987  100.967 35.095  1.00 8.02  ? 45  PHE B O   1 
ATOM   1440  C  CB  . PHE B  1 45  ? 23.333  99.634  34.088  1.00 8.59  ? 45  PHE B CB  1 
ATOM   1441  C  CG  . PHE B  1 45  ? 23.481  99.919  32.594  1.00 9.37  ? 45  PHE B CG  1 
ATOM   1442  C  CD1 . PHE B  1 45  ? 24.609  100.553 32.095  1.00 11.00 ? 45  PHE B CD1 1 
ATOM   1443  C  CD2 . PHE B  1 45  ? 22.501  99.511  31.694  1.00 7.88  ? 45  PHE B CD2 1 
ATOM   1444  C  CE1 . PHE B  1 45  ? 24.764  100.790 30.724  1.00 6.99  ? 45  PHE B CE1 1 
ATOM   1445  C  CE2 . PHE B  1 45  ? 22.637  99.753  30.337  1.00 9.46  ? 45  PHE B CE2 1 
ATOM   1446  C  CZ  . PHE B  1 45  ? 23.779  100.392 29.843  1.00 6.18  ? 45  PHE B CZ  1 
ATOM   1447  N  N   . HIS B  1 46  ? 22.077  102.938 34.869  1.00 9.09  ? 46  HIS B N   1 
ATOM   1448  C  CA  . HIS B  1 46  ? 20.828  103.722 34.946  1.00 11.21 ? 46  HIS B CA  1 
ATOM   1449  C  C   . HIS B  1 46  ? 20.706  104.825 33.922  1.00 9.83  ? 46  HIS B C   1 
ATOM   1450  O  O   . HIS B  1 46  ? 21.714  105.411 33.503  1.00 8.46  ? 46  HIS B O   1 
ATOM   1451  C  CB  . HIS B  1 46  ? 20.704  104.418 36.289  1.00 9.06  ? 46  HIS B CB  1 
ATOM   1452  C  CG  . HIS B  1 46  ? 21.092  103.565 37.440  1.00 13.11 ? 46  HIS B CG  1 
ATOM   1453  N  ND1 . HIS B  1 46  ? 21.925  104.010 38.441  1.00 13.54 ? 46  HIS B ND1 1 
ATOM   1454  C  CD2 . HIS B  1 46  ? 20.776  102.286 37.746  1.00 11.48 ? 46  HIS B CD2 1 
ATOM   1455  C  CE1 . HIS B  1 46  ? 22.083  103.045 39.331  1.00 14.18 ? 46  HIS B CE1 1 
ATOM   1456  N  NE2 . HIS B  1 46  ? 21.411  101.984 38.924  1.00 10.51 ? 46  HIS B NE2 1 
ATOM   1457  N  N   . VAL B  1 47  ? 19.466  105.139 33.565  1.00 7.48  ? 47  VAL B N   1 
ATOM   1458  C  CA  . VAL B  1 47  ? 19.185  106.394 32.893  1.00 8.34  ? 47  VAL B CA  1 
ATOM   1459  C  C   . VAL B  1 47  ? 18.891  107.464 33.929  1.00 9.41  ? 47  VAL B C   1 
ATOM   1460  O  O   . VAL B  1 47  ? 17.980  107.317 34.738  1.00 11.26 ? 47  VAL B O   1 
ATOM   1461  C  CB  . VAL B  1 47  ? 18.025  106.285 31.930  1.00 8.90  ? 47  VAL B CB  1 
ATOM   1462  C  CG1 . VAL B  1 47  ? 17.785  107.646 31.235  1.00 10.60 ? 47  VAL B CG1 1 
ATOM   1463  C  CG2 . VAL B  1 47  ? 18.291  105.185 30.906  1.00 8.44  ? 47  VAL B CG2 1 
ATOM   1464  N  N   . HIS B  1 48  ? 19.694  108.520 33.937  1.00 7.53  ? 48  HIS B N   1 
ATOM   1465  C  CA  . HIS B  1 48  ? 19.431  109.641 34.818  1.00 9.89  ? 48  HIS B CA  1 
ATOM   1466  C  C   . HIS B  1 48  ? 18.646  110.683 34.040  1.00 11.48 ? 48  HIS B C   1 
ATOM   1467  O  O   . HIS B  1 48  ? 18.688  110.713 32.785  1.00 10.30 ? 48  HIS B O   1 
ATOM   1468  C  CB  . HIS B  1 48  ? 20.730  110.265 35.359  1.00 9.67  ? 48  HIS B CB  1 
ATOM   1469  C  CG  . HIS B  1 48  ? 21.417  109.438 36.401  1.00 10.81 ? 48  HIS B CG  1 
ATOM   1470  N  ND1 . HIS B  1 48  ? 21.601  109.876 37.694  1.00 12.73 ? 48  HIS B ND1 1 
ATOM   1471  C  CD2 . HIS B  1 48  ? 21.944  108.190 36.348  1.00 9.97  ? 48  HIS B CD2 1 
ATOM   1472  C  CE1 . HIS B  1 48  ? 22.222  108.943 38.390  1.00 12.94 ? 48  HIS B CE1 1 
ATOM   1473  N  NE2 . HIS B  1 48  ? 22.457  107.919 37.593  1.00 11.72 ? 48  HIS B NE2 1 
ATOM   1474  N  N   . GLU B  1 49  ? 17.969  111.546 34.798  1.00 11.72 ? 49  GLU B N   1 
ATOM   1475  C  CA  . GLU B  1 49  ? 16.984  112.492 34.283  1.00 11.40 ? 49  GLU B CA  1 
ATOM   1476  C  C   . GLU B  1 49  ? 17.486  113.497 33.232  1.00 12.57 ? 49  GLU B C   1 
ATOM   1477  O  O   . GLU B  1 49  ? 16.818  113.716 32.224  1.00 10.53 ? 49  GLU B O   1 
ATOM   1478  C  CB  . GLU B  1 49  ? 16.358  113.253 35.447  1.00 12.28 ? 49  GLU B CB  1 
ATOM   1479  C  CG  . GLU B  1 49  ? 15.200  114.117 35.040  1.00 12.13 ? 49  GLU B CG  1 
ATOM   1480  C  CD  . GLU B  1 49  ? 14.479  114.772 36.222  1.00 16.95 ? 49  GLU B CD  1 
ATOM   1481  O  OE1 . GLU B  1 49  ? 14.935  114.641 37.386  1.00 12.13 ? 49  GLU B OE1 1 
ATOM   1482  O  OE2 . GLU B  1 49  ? 13.458  115.447 35.963  1.00 18.51 ? 49  GLU B OE2 1 
ATOM   1483  N  N   . PHE B  1 50  ? 18.636  114.129 33.470  1.00 10.73 ? 50  PHE B N   1 
ATOM   1484  C  CA  . PHE B  1 50  ? 19.031  115.251 32.615  1.00 11.36 ? 50  PHE B CA  1 
ATOM   1485  C  C   . PHE B  1 50  ? 20.185  114.907 31.664  1.00 11.17 ? 50  PHE B C   1 
ATOM   1486  O  O   . PHE B  1 50  ? 21.154  114.281 32.077  1.00 9.78  ? 50  PHE B O   1 
ATOM   1487  C  CB  . PHE B  1 50  ? 19.389  116.465 33.468  1.00 12.31 ? 50  PHE B CB  1 
ATOM   1488  C  CG  . PHE B  1 50  ? 18.295  116.889 34.401  1.00 13.50 ? 50  PHE B CG  1 
ATOM   1489  C  CD1 . PHE B  1 50  ? 17.063  117.285 33.909  1.00 15.06 ? 50  PHE B CD1 1 
ATOM   1490  C  CD2 . PHE B  1 50  ? 18.502  116.911 35.763  1.00 16.16 ? 50  PHE B CD2 1 
ATOM   1491  C  CE1 . PHE B  1 50  ? 16.056  117.676 34.751  1.00 16.24 ? 50  PHE B CE1 1 
ATOM   1492  C  CE2 . PHE B  1 50  ? 17.481  117.301 36.627  1.00 20.94 ? 50  PHE B CE2 1 
ATOM   1493  C  CZ  . PHE B  1 50  ? 16.261  117.685 36.118  1.00 16.95 ? 50  PHE B CZ  1 
ATOM   1494  N  N   . GLY B  1 51  ? 20.071  115.310 30.399  1.00 8.36  ? 51  GLY B N   1 
ATOM   1495  C  CA  . GLY B  1 51  ? 21.141  115.118 29.430  1.00 6.47  ? 51  GLY B CA  1 
ATOM   1496  C  C   . GLY B  1 51  ? 22.102  116.292 29.521  1.00 9.83  ? 51  GLY B C   1 
ATOM   1497  O  O   . GLY B  1 51  ? 22.432  116.934 28.519  1.00 9.66  ? 51  GLY B O   1 
ATOM   1498  N  N   . ASP B  1 52  ? 22.548  116.567 30.741  1.00 10.02 ? 52  ASP B N   1 
ATOM   1499  C  CA  . ASP B  1 52  ? 23.302  117.765 31.059  1.00 11.01 ? 52  ASP B CA  1 
ATOM   1500  C  C   . ASP B  1 52  ? 24.655  117.375 31.620  1.00 15.59 ? 52  ASP B C   1 
ATOM   1501  O  O   . ASP B  1 52  ? 24.761  116.913 32.755  1.00 13.71 ? 52  ASP B O   1 
ATOM   1502  C  CB  . ASP B  1 52  ? 22.538  118.622 32.075  1.00 11.06 ? 52  ASP B CB  1 
ATOM   1503  C  CG  . ASP B  1 52  ? 23.251  119.921 32.408  1.00 14.29 ? 52  ASP B CG  1 
ATOM   1504  O  OD1 . ASP B  1 52  ? 24.492  119.998 32.308  1.00 13.59 ? 52  ASP B OD1 1 
ATOM   1505  O  OD2 . ASP B  1 52  ? 22.553  120.886 32.772  1.00 19.09 ? 52  ASP B OD2 1 
ATOM   1506  N  N   . ASN B  1 53  ? 25.686  117.587 30.817  1.00 12.47 ? 53  ASN B N   1 
ATOM   1507  C  CA  . ASN B  1 53  ? 27.029  117.167 31.167  1.00 18.49 ? 53  ASN B CA  1 
ATOM   1508  C  C   . ASN B  1 53  ? 27.938  118.358 31.504  1.00 18.57 ? 53  ASN B C   1 
ATOM   1509  O  O   . ASN B  1 53  ? 29.148  118.229 31.509  1.00 22.28 ? 53  ASN B O   1 
ATOM   1510  C  CB  . ASN B  1 53  ? 27.613  116.331 30.012  1.00 20.01 ? 53  ASN B CB  1 
ATOM   1511  C  CG  . ASN B  1 53  ? 28.891  115.624 30.394  1.00 27.69 ? 53  ASN B CG  1 
ATOM   1512  O  OD1 . ASN B  1 53  ? 29.020  115.125 31.517  1.00 29.62 ? 53  ASN B OD1 1 
ATOM   1513  N  ND2 . ASN B  1 53  ? 29.865  115.605 29.476  1.00 24.85 ? 53  ASN B ND2 1 
ATOM   1514  N  N   . THR B  1 54  ? 27.350  119.518 31.777  1.00 17.74 ? 54  THR B N   1 
ATOM   1515  C  CA  . THR B  1 54  ? 28.132  120.730 32.006  1.00 19.83 ? 54  THR B CA  1 
ATOM   1516  C  C   . THR B  1 54  ? 29.083  120.611 33.211  1.00 24.03 ? 54  THR B C   1 
ATOM   1517  O  O   . THR B  1 54  ? 30.236  121.049 33.145  1.00 23.71 ? 54  THR B O   1 
ATOM   1518  C  CB  . THR B  1 54  ? 27.225  121.968 32.172  1.00 18.02 ? 54  THR B CB  1 
ATOM   1519  O  OG1 . THR B  1 54  ? 26.212  121.699 33.154  1.00 17.87 ? 54  THR B OG1 1 
ATOM   1520  C  CG2 . THR B  1 54  ? 26.559  122.316 30.854  1.00 14.23 ? 54  THR B CG2 1 
ATOM   1521  N  N   . ALA B  1 55  ? 28.598  120.001 34.293  1.00 20.91 ? 55  ALA B N   1 
ATOM   1522  C  CA  . ALA B  1 55  ? 29.413  119.762 35.481  1.00 21.84 ? 55  ALA B CA  1 
ATOM   1523  C  C   . ALA B  1 55  ? 29.780  118.282 35.572  1.00 23.77 ? 55  ALA B C   1 
ATOM   1524  O  O   . ALA B  1 55  ? 29.765  117.693 36.650  1.00 23.83 ? 55  ALA B O   1 
ATOM   1525  C  CB  . ALA B  1 55  ? 28.670  120.219 36.731  1.00 19.45 ? 55  ALA B CB  1 
ATOM   1526  N  N   . GLY B  1 56  ? 30.100  117.686 34.426  1.00 17.43 ? 56  GLY B N   1 
ATOM   1527  C  CA  . GLY B  1 56  ? 30.343  116.264 34.361  1.00 22.09 ? 56  GLY B CA  1 
ATOM   1528  C  C   . GLY B  1 56  ? 29.083  115.443 34.583  1.00 26.15 ? 56  GLY B C   1 
ATOM   1529  O  O   . GLY B  1 56  ? 27.968  115.946 34.437  1.00 22.02 ? 56  GLY B O   1 
ATOM   1530  N  N   . SER B  1 57  ? 29.273  114.173 34.940  1.00 23.94 ? 57  SER B N   1 
ATOM   1531  C  CA  . SER B  1 57  ? 28.171  113.269 35.258  1.00 22.28 ? 57  SER B CA  1 
ATOM   1532  C  C   . SER B  1 57  ? 27.312  113.769 36.430  1.00 22.16 ? 57  SER B C   1 
ATOM   1533  O  O   . SER B  1 57  ? 26.179  113.329 36.610  1.00 23.05 ? 57  SER B O   1 
ATOM   1534  C  CB  . SER B  1 57  ? 28.715  111.869 35.580  1.00 21.96 ? 57  SER B CB  1 
ATOM   1535  O  OG  . SER B  1 57  ? 29.419  111.871 36.824  1.00 24.22 ? 57  SER B OG  1 
ATOM   1536  N  N   . THR B  1 58  ? 27.840  114.677 37.242  1.00 21.43 ? 58  THR B N   1 
ATOM   1537  C  CA  . THR B  1 58  ? 27.076  115.115 38.406  1.00 21.24 ? 58  THR B CA  1 
ATOM   1538  C  C   . THR B  1 58  ? 25.879  116.006 38.052  1.00 23.46 ? 58  THR B C   1 
ATOM   1539  O  O   . THR B  1 58  ? 24.929  116.101 38.813  1.00 19.15 ? 58  THR B O   1 
ATOM   1540  C  CB  . THR B  1 58  ? 27.961  115.727 39.534  1.00 25.61 ? 58  THR B CB  1 
ATOM   1541  O  OG1 . THR B  1 58  ? 27.440  116.998 39.943  1.00 32.52 ? 58  THR B OG1 1 
ATOM   1542  C  CG2 . THR B  1 58  ? 29.415  115.855 39.095  1.00 28.11 ? 58  THR B CG2 1 
ATOM   1543  N  N   . SER B  1 59  ? 25.894  116.614 36.872  1.00 20.69 ? 59  SER B N   1 
ATOM   1544  C  CA  . SER B  1 59  ? 24.772  117.451 36.471  1.00 17.14 ? 59  SER B CA  1 
ATOM   1545  C  C   . SER B  1 59  ? 23.651  116.650 35.801  1.00 14.11 ? 59  SER B C   1 
ATOM   1546  O  O   . SER B  1 59  ? 22.662  117.218 35.344  1.00 16.87 ? 59  SER B O   1 
ATOM   1547  C  CB  . SER B  1 59  ? 25.250  118.613 35.584  1.00 15.31 ? 59  SER B CB  1 
ATOM   1548  O  OG  . SER B  1 59  ? 26.187  118.159 34.621  1.00 21.59 ? 59  SER B OG  1 
ATOM   1549  N  N   . ALA B  1 60  ? 23.791  115.332 35.750  1.00 13.81 ? 60  ALA B N   1 
ATOM   1550  C  CA  . ALA B  1 60  ? 22.764  114.500 35.126  1.00 14.43 ? 60  ALA B CA  1 
ATOM   1551  C  C   . ALA B  1 60  ? 21.558  114.260 36.060  1.00 13.01 ? 60  ALA B C   1 
ATOM   1552  O  O   . ALA B  1 60  ? 20.590  113.607 35.685  1.00 11.49 ? 60  ALA B O   1 
ATOM   1553  C  CB  . ALA B  1 60  ? 23.356  113.186 34.641  1.00 11.97 ? 60  ALA B CB  1 
ATOM   1554  N  N   . GLY B  1 61  ? 21.609  114.808 37.268  1.00 14.10 ? 61  GLY B N   1 
ATOM   1555  C  CA  . GLY B  1 61  ? 20.483  114.677 38.172  1.00 15.85 ? 61  GLY B CA  1 
ATOM   1556  C  C   . GLY B  1 61  ? 20.259  113.246 38.624  1.00 16.66 ? 61  GLY B C   1 
ATOM   1557  O  O   . GLY B  1 61  ? 21.134  112.398 38.461  1.00 15.03 ? 61  GLY B O   1 
ATOM   1558  N  N   . PRO B  1 62  ? 19.079  112.967 39.202  1.00 16.78 ? 62  PRO B N   1 
ATOM   1559  C  CA  . PRO B  1 62  ? 18.803  111.637 39.752  1.00 13.70 ? 62  PRO B CA  1 
ATOM   1560  C  C   . PRO B  1 62  ? 18.335  110.657 38.683  1.00 13.73 ? 62  PRO B C   1 
ATOM   1561  O  O   . PRO B  1 62  ? 18.297  111.005 37.503  1.00 12.70 ? 62  PRO B O   1 
ATOM   1562  C  CB  . PRO B  1 62  ? 17.699  111.906 40.773  1.00 16.95 ? 62  PRO B CB  1 
ATOM   1563  C  CG  . PRO B  1 62  ? 17.011  113.126 40.284  1.00 17.31 ? 62  PRO B CG  1 
ATOM   1564  C  CD  . PRO B  1 62  ? 17.991  113.922 39.455  1.00 15.28 ? 62  PRO B CD  1 
ATOM   1565  N  N   . HIS B  1 63  ? 18.027  109.428 39.087  1.00 14.94 ? 63  HIS B N   1 
ATOM   1566  C  CA  . HIS B  1 63  ? 17.438  108.446 38.180  1.00 14.23 ? 63  HIS B CA  1 
ATOM   1567  C  C   . HIS B  1 63  ? 16.189  109.009 37.508  1.00 14.83 ? 63  HIS B C   1 
ATOM   1568  O  O   . HIS B  1 63  ? 15.377  109.689 38.153  1.00 12.33 ? 63  HIS B O   1 
ATOM   1569  C  CB  . HIS B  1 63  ? 17.067  107.169 38.938  1.00 12.92 ? 63  HIS B CB  1 
ATOM   1570  C  CG  . HIS B  1 63  ? 18.233  106.479 39.561  1.00 16.85 ? 63  HIS B CG  1 
ATOM   1571  N  ND1 . HIS B  1 63  ? 18.119  105.266 40.198  1.00 14.77 ? 63  HIS B ND1 1 
ATOM   1572  C  CD2 . HIS B  1 63  ? 19.543  106.821 39.631  1.00 16.29 ? 63  HIS B CD2 1 
ATOM   1573  C  CE1 . HIS B  1 63  ? 19.304  104.892 40.642  1.00 14.99 ? 63  HIS B CE1 1 
ATOM   1574  N  NE2 . HIS B  1 63  ? 20.185  105.818 40.311  1.00 16.73 ? 63  HIS B NE2 1 
ATOM   1575  N  N   . PHE B  1 64  ? 16.049  108.731 36.214  1.00 10.66 ? 64  PHE B N   1 
ATOM   1576  C  CA  . PHE B  1 64  ? 14.876  109.169 35.483  1.00 14.12 ? 64  PHE B CA  1 
ATOM   1577  C  C   . PHE B  1 64  ? 13.652  108.514 36.093  1.00 12.65 ? 64  PHE B C   1 
ATOM   1578  O  O   . PHE B  1 64  ? 13.532  107.296 36.069  1.00 10.81 ? 64  PHE B O   1 
ATOM   1579  C  CB  . PHE B  1 64  ? 14.971  108.782 34.016  1.00 11.01 ? 64  PHE B CB  1 
ATOM   1580  C  CG  . PHE B  1 64  ? 13.793  109.233 33.208  1.00 12.41 ? 64  PHE B CG  1 
ATOM   1581  C  CD1 . PHE B  1 64  ? 13.248  110.487 33.405  1.00 13.80 ? 64  PHE B CD1 1 
ATOM   1582  C  CD2 . PHE B  1 64  ? 13.232  108.407 32.239  1.00 12.82 ? 64  PHE B CD2 1 
ATOM   1583  C  CE1 . PHE B  1 64  ? 12.145  110.904 32.672  1.00 11.69 ? 64  PHE B CE1 1 
ATOM   1584  C  CE2 . PHE B  1 64  ? 12.140  108.827 31.495  1.00 11.72 ? 64  PHE B CE2 1 
ATOM   1585  C  CZ  . PHE B  1 64  ? 11.608  110.085 31.706  1.00 12.77 ? 64  PHE B CZ  1 
ATOM   1586  N  N   . ASN B  1 65  ? 12.747  109.335 36.615  1.00 16.24 ? 65  ASN B N   1 
ATOM   1587  C  CA  . ASN B  1 65  ? 11.677  108.871 37.499  1.00 14.29 ? 65  ASN B CA  1 
ATOM   1588  C  C   . ASN B  1 65  ? 10.399  109.693 37.325  1.00 18.13 ? 65  ASN B C   1 
ATOM   1589  O  O   . ASN B  1 65  ? 9.981   110.383 38.251  1.00 22.51 ? 65  ASN B O   1 
ATOM   1590  C  CB  . ASN B  1 65  ? 12.161  108.973 38.949  1.00 11.55 ? 65  ASN B CB  1 
ATOM   1591  C  CG  . ASN B  1 65  ? 11.159  108.398 39.973  1.00 16.91 ? 65  ASN B CG  1 
ATOM   1592  O  OD1 . ASN B  1 65  ? 10.345  107.513 39.670  1.00 15.47 ? 65  ASN B OD1 1 
ATOM   1593  N  ND2 . ASN B  1 65  ? 11.243  108.894 41.192  1.00 14.49 ? 65  ASN B ND2 1 
ATOM   1594  N  N   . PRO B  1 66  ? 9.777   109.630 36.137  1.00 19.24 ? 66  PRO B N   1 
ATOM   1595  C  CA  . PRO B  1 66  ? 8.581   110.443 35.901  1.00 20.36 ? 66  PRO B CA  1 
ATOM   1596  C  C   . PRO B  1 66  ? 7.357   110.012 36.724  1.00 27.52 ? 66  PRO B C   1 
ATOM   1597  O  O   . PRO B  1 66  ? 6.496   110.854 36.935  1.00 28.63 ? 66  PRO B O   1 
ATOM   1598  C  CB  . PRO B  1 66  ? 8.317   110.249 34.404  1.00 22.07 ? 66  PRO B CB  1 
ATOM   1599  C  CG  . PRO B  1 66  ? 8.944   108.924 34.078  1.00 15.93 ? 66  PRO B CG  1 
ATOM   1600  C  CD  . PRO B  1 66  ? 10.152  108.838 34.949  1.00 14.21 ? 66  PRO B CD  1 
ATOM   1601  N  N   . LEU B  1 67  ? 7.281   108.759 37.178  1.00 26.69 ? 67  LEU B N   1 
ATOM   1602  C  CA  . LEU B  1 67  ? 6.153   108.304 38.001  1.00 23.25 ? 67  LEU B CA  1 
ATOM   1603  C  C   . LEU B  1 67  ? 6.381   108.453 39.499  1.00 26.83 ? 67  LEU B C   1 
ATOM   1604  O  O   . LEU B  1 67  ? 5.616   107.915 40.294  1.00 29.51 ? 67  LEU B O   1 
ATOM   1605  C  CB  . LEU B  1 67  ? 5.809   106.849 37.705  1.00 21.47 ? 67  LEU B CB  1 
ATOM   1606  C  CG  . LEU B  1 67  ? 5.808   106.489 36.222  1.00 26.13 ? 67  LEU B CG  1 
ATOM   1607  C  CD1 . LEU B  1 67  ? 5.491   105.022 36.032  1.00 28.77 ? 67  LEU B CD1 1 
ATOM   1608  C  CD2 . LEU B  1 67  ? 4.831   107.360 35.462  1.00 28.47 ? 67  LEU B CD2 1 
ATOM   1609  N  N   . SER B  1 68  ? 7.420   109.184 39.887  1.00 27.61 ? 68  SER B N   1 
ATOM   1610  C  CA  . SER B  1 68  ? 7.706   109.431 41.306  1.00 25.45 ? 68  SER B CA  1 
ATOM   1611  C  C   . SER B  1 68  ? 7.649   108.167 42.138  1.00 26.38 ? 68  SER B C   1 
ATOM   1612  O  O   . SER B  1 68  ? 7.042   108.158 43.201  1.00 25.31 ? 68  SER B O   1 
ATOM   1613  C  CB  . SER B  1 68  ? 6.729   110.444 41.903  1.00 24.74 ? 68  SER B CB  1 
ATOM   1614  O  OG  . SER B  1 68  ? 6.763   111.664 41.191  1.00 31.73 ? 68  SER B OG  1 
ATOM   1615  N  N   . ARG B  1 69  ? 8.255   107.095 41.638  1.00 23.95 ? 69  ARG B N   1 
ATOM   1616  C  CA  . ARG B  1 69  ? 8.288   105.852 42.375  1.00 18.48 ? 69  ARG B CA  1 
ATOM   1617  C  C   . ARG B  1 69  ? 9.590   105.704 43.146  1.00 21.23 ? 69  ARG B C   1 
ATOM   1618  O  O   . ARG B  1 69  ? 10.409  106.617 43.169  1.00 21.82 ? 69  ARG B O   1 
ATOM   1619  C  CB  . ARG B  1 69  ? 8.015   104.667 41.456  1.00 20.59 ? 69  ARG B CB  1 
ATOM   1620  C  CG  . ARG B  1 69  ? 6.544   104.538 41.098  1.00 24.00 ? 69  ARG B CG  1 
ATOM   1621  C  CD  . ARG B  1 69  ? 6.301   103.344 40.204  1.00 30.51 ? 69  ARG B CD  1 
ATOM   1622  N  NE  . ARG B  1 69  ? 4.963   103.390 39.623  1.00 34.65 ? 69  ARG B NE  1 
ATOM   1623  C  CZ  . ARG B  1 69  ? 4.517   102.550 38.696  1.00 35.83 ? 69  ARG B CZ  1 
ATOM   1624  N  NH1 . ARG B  1 69  ? 5.302   101.585 38.241  1.00 36.26 ? 69  ARG B NH1 1 
ATOM   1625  N  NH2 . ARG B  1 69  ? 3.283   102.681 38.219  1.00 37.20 ? 69  ARG B NH2 1 
ATOM   1626  N  N   . LYS B  1 70  ? 9.735   104.577 43.833  1.00 22.08 ? 70  LYS B N   1 
ATOM   1627  C  CA  . LYS B  1 70  ? 10.933  104.251 44.586  1.00 17.15 ? 70  LYS B CA  1 
ATOM   1628  C  C   . LYS B  1 70  ? 11.870  103.473 43.675  1.00 15.24 ? 70  LYS B C   1 
ATOM   1629  O  O   . LYS B  1 70  ? 11.434  102.891 42.685  1.00 13.37 ? 70  LYS B O   1 
ATOM   1630  C  CB  . LYS B  1 70  ? 10.556  103.334 45.738  1.00 20.40 ? 70  LYS B CB  1 
ATOM   1631  C  CG  . LYS B  1 70  ? 10.896  103.857 47.118  1.00 21.81 ? 70  LYS B CG  1 
ATOM   1632  C  CD  . LYS B  1 70  ? 9.895   104.880 47.616  1.00 30.49 ? 70  LYS B CD  1 
ATOM   1633  C  CE  . LYS B  1 70  ? 10.254  105.309 49.055  1.00 42.30 ? 70  LYS B CE  1 
ATOM   1634  N  NZ  . LYS B  1 70  ? 9.350   106.360 49.616  1.00 47.97 ? 70  LYS B NZ  1 
ATOM   1635  N  N   . HIS B  1 71  ? 13.148  103.426 44.037  1.00 15.67 ? 71  HIS B N   1 
ATOM   1636  C  CA  . HIS B  1 71  ? 14.161  102.700 43.268  1.00 13.04 ? 71  HIS B CA  1 
ATOM   1637  C  C   . HIS B  1 71  ? 14.014  101.179 43.444  1.00 15.19 ? 71  HIS B C   1 
ATOM   1638  O  O   . HIS B  1 71  ? 13.904  100.684 44.564  1.00 11.84 ? 71  HIS B O   1 
ATOM   1639  C  CB  . HIS B  1 71  ? 15.568  103.166 43.697  1.00 14.49 ? 71  HIS B CB  1 
ATOM   1640  C  CG  . HIS B  1 71  ? 16.687  102.422 43.038  1.00 11.67 ? 71  HIS B CG  1 
ATOM   1641  N  ND1 . HIS B  1 71  ? 17.157  102.739 41.783  1.00 11.06 ? 71  HIS B ND1 1 
ATOM   1642  C  CD2 . HIS B  1 71  ? 17.424  101.369 43.463  1.00 11.90 ? 71  HIS B CD2 1 
ATOM   1643  C  CE1 . HIS B  1 71  ? 18.123  101.901 41.453  1.00 14.92 ? 71  HIS B CE1 1 
ATOM   1644  N  NE2 . HIS B  1 71  ? 18.317  101.069 42.462  1.00 13.47 ? 71  HIS B NE2 1 
ATOM   1645  N  N   . GLY B  1 72  ? 14.035  100.439 42.339  1.00 10.47 ? 72  GLY B N   1 
ATOM   1646  C  CA  . GLY B  1 72  ? 14.025  98.990  42.410  1.00 12.06 ? 72  GLY B CA  1 
ATOM   1647  C  C   . GLY B  1 72  ? 14.916  98.407  41.335  1.00 12.78 ? 72  GLY B C   1 
ATOM   1648  O  O   . GLY B  1 72  ? 15.735  99.118  40.769  1.00 12.84 ? 72  GLY B O   1 
ATOM   1649  N  N   . GLY B  1 73  ? 14.752  97.121  41.050  1.00 13.07 ? 73  GLY B N   1 
ATOM   1650  C  CA  . GLY B  1 73  ? 15.417  96.499  39.931  1.00 14.71 ? 73  GLY B CA  1 
ATOM   1651  C  C   . GLY B  1 73  ? 14.475  96.552  38.739  1.00 17.15 ? 73  GLY B C   1 
ATOM   1652  O  O   . GLY B  1 73  ? 13.296  96.851  38.908  1.00 15.58 ? 73  GLY B O   1 
ATOM   1653  N  N   . PRO B  1 74  ? 14.991  96.269  37.533  1.00 14.95 ? 74  PRO B N   1 
ATOM   1654  C  CA  . PRO B  1 74  ? 14.209  96.336  36.291  1.00 14.42 ? 74  PRO B CA  1 
ATOM   1655  C  C   . PRO B  1 74  ? 13.016  95.386  36.266  1.00 18.61 ? 74  PRO B C   1 
ATOM   1656  O  O   . PRO B  1 74  ? 12.082  95.638  35.497  1.00 14.67 ? 74  PRO B O   1 
ATOM   1657  C  CB  . PRO B  1 74  ? 15.214  95.938  35.202  1.00 14.55 ? 74  PRO B CB  1 
ATOM   1658  C  CG  . PRO B  1 74  ? 16.412  95.343  35.950  1.00 15.30 ? 74  PRO B CG  1 
ATOM   1659  C  CD  . PRO B  1 74  ? 16.418  96.003  37.285  1.00 10.38 ? 74  PRO B CD  1 
ATOM   1660  N  N   . LYS B  1 75  ? 13.049  94.321  37.072  1.00 18.24 ? 75  LYS B N   1 
ATOM   1661  C  CA  . LYS B  1 75  ? 11.939  93.362  37.135  1.00 15.59 ? 75  LYS B CA  1 
ATOM   1662  C  C   . LYS B  1 75  ? 10.839  93.815  38.095  1.00 19.53 ? 75  LYS B C   1 
ATOM   1663  O  O   . LYS B  1 75  ? 9.729   93.310  38.062  1.00 19.83 ? 75  LYS B O   1 
ATOM   1664  C  CB  . LYS B  1 75  ? 12.428  91.962  37.530  1.00 18.21 ? 75  LYS B CB  1 
ATOM   1665  C  CG  . LYS B  1 75  ? 13.181  91.222  36.433  1.00 17.87 ? 75  LYS B CG  1 
ATOM   1666  C  CD  . LYS B  1 75  ? 14.028  90.077  37.021  1.00 23.62 ? 75  LYS B CD  1 
ATOM   1667  C  CE  . LYS B  1 75  ? 13.184  88.859  37.428  1.00 24.22 ? 75  LYS B CE  1 
ATOM   1668  N  NZ  . LYS B  1 75  ? 13.774  88.183  38.631  1.00 29.25 ? 75  LYS B NZ  1 
ATOM   1669  N  N   . ASP B  1 76  ? 11.138  94.790  38.934  1.00 15.99 ? 76  ASP B N   1 
ATOM   1670  C  CA  . ASP B  1 76  ? 10.171  95.232  39.908  1.00 17.36 ? 76  ASP B CA  1 
ATOM   1671  C  C   . ASP B  1 76  ? 9.161   96.177  39.298  1.00 21.07 ? 76  ASP B C   1 
ATOM   1672  O  O   . ASP B  1 76  ? 9.488   97.004  38.445  1.00 15.94 ? 76  ASP B O   1 
ATOM   1673  C  CB  . ASP B  1 76  ? 10.857  95.942  41.063  1.00 15.65 ? 76  ASP B CB  1 
ATOM   1674  C  CG  . ASP B  1 76  ? 11.872  95.061  41.781  1.00 21.24 ? 76  ASP B CG  1 
ATOM   1675  O  OD1 . ASP B  1 76  ? 11.625  93.845  41.961  1.00 25.40 ? 76  ASP B OD1 1 
ATOM   1676  O  OD2 . ASP B  1 76  ? 12.918  95.598  42.186  1.00 20.62 ? 76  ASP B OD2 1 
ATOM   1677  N  N   . GLU B  1 77  ? 7.931   96.056  39.774  1.00 16.12 ? 77  GLU B N   1 
ATOM   1678  C  CA  . GLU B  1 77  ? 6.893   96.997  39.461  1.00 22.21 ? 77  GLU B CA  1 
ATOM   1679  C  C   . GLU B  1 77  ? 7.189   98.343  40.139  1.00 18.11 ? 77  GLU B C   1 
ATOM   1680  O  O   . GLU B  1 77  ? 6.989   99.416  39.567  1.00 17.34 ? 77  GLU B O   1 
ATOM   1681  C  CB  . GLU B  1 77  ? 5.565   96.436  39.951  1.00 24.70 ? 77  GLU B CB  1 
ATOM   1682  C  CG  . GLU B  1 77  ? 4.475   97.444  39.934  1.00 28.68 ? 77  GLU B CG  1 
ATOM   1683  C  CD  . GLU B  1 77  ? 3.439   97.117  38.913  1.00 39.54 ? 77  GLU B CD  1 
ATOM   1684  O  OE1 . GLU B  1 77  ? 2.254   97.021  39.304  1.00 40.70 ? 77  GLU B OE1 1 
ATOM   1685  O  OE2 . GLU B  1 77  ? 3.814   96.946  37.729  1.00 44.84 ? 77  GLU B OE2 1 
ATOM   1686  N  N   . GLU B  1 78  ? 7.680   98.295  41.361  1.00 15.45 ? 78  GLU B N   1 
ATOM   1687  C  CA  . GLU B  1 78  ? 8.114   99.533  41.991  1.00 18.41 ? 78  GLU B CA  1 
ATOM   1688  C  C   . GLU B  1 78  ? 9.570   99.823  41.585  1.00 16.35 ? 78  GLU B C   1 
ATOM   1689  O  O   . GLU B  1 78  ? 10.499  99.276  42.171  1.00 17.67 ? 78  GLU B O   1 
ATOM   1690  C  CB  . GLU B  1 78  ? 7.943   99.461  43.515  1.00 13.88 ? 78  GLU B CB  1 
ATOM   1691  C  CG  . GLU B  1 78  ? 8.251   100.752 44.275  1.00 15.78 ? 78  GLU B CG  1 
ATOM   1692  C  CD  . GLU B  1 78  ? 7.163   101.825 44.102  1.00 22.96 ? 78  GLU B CD  1 
ATOM   1693  O  OE1 . GLU B  1 78  ? 6.117   101.537 43.464  1.00 24.74 ? 78  GLU B OE1 1 
ATOM   1694  O  OE2 . GLU B  1 78  ? 7.352   102.963 44.603  1.00 23.15 ? 78  GLU B OE2 1 
ATOM   1695  N  N   . ARG B  1 79  ? 9.748   100.660 40.564  1.00 14.04 ? 79  ARG B N   1 
ATOM   1696  C  CA  . ARG B  1 79  ? 11.073  101.110 40.139  1.00 15.14 ? 79  ARG B CA  1 
ATOM   1697  C  C   . ARG B  1 79  ? 10.984  102.484 39.486  1.00 16.85 ? 79  ARG B C   1 
ATOM   1698  O  O   . ARG B  1 79  ? 9.911   102.951 39.108  1.00 12.85 ? 79  ARG B O   1 
ATOM   1699  C  CB  . ARG B  1 79  ? 11.696  100.133 39.137  1.00 10.40 ? 79  ARG B CB  1 
ATOM   1700  C  CG  . ARG B  1 79  ? 10.777  99.883  37.938  1.00 14.71 ? 79  ARG B CG  1 
ATOM   1701  C  CD  . ARG B  1 79  ? 11.402  99.065  36.844  1.00 13.47 ? 79  ARG B CD  1 
ATOM   1702  N  NE  . ARG B  1 79  ? 12.036  99.917  35.845  1.00 11.59 ? 79  ARG B NE  1 
ATOM   1703  C  CZ  . ARG B  1 79  ? 12.429  99.497  34.643  1.00 9.78  ? 79  ARG B CZ  1 
ATOM   1704  N  NH1 . ARG B  1 79  ? 12.247  98.237  34.278  1.00 8.65  ? 79  ARG B NH1 1 
ATOM   1705  N  NH2 . ARG B  1 79  ? 12.993  100.351 33.798  1.00 10.51 ? 79  ARG B NH2 1 
ATOM   1706  N  N   . HIS B  1 80  ? 12.137  103.128 39.359  1.00 16.22 ? 80  HIS B N   1 
ATOM   1707  C  CA  . HIS B  1 80  ? 12.280  104.288 38.488  1.00 12.64 ? 80  HIS B CA  1 
ATOM   1708  C  C   . HIS B  1 80  ? 12.309  103.781 37.047  1.00 13.05 ? 80  HIS B C   1 
ATOM   1709  O  O   . HIS B  1 80  ? 12.845  102.696 36.772  1.00 10.32 ? 80  HIS B O   1 
ATOM   1710  C  CB  . HIS B  1 80  ? 13.592  105.011 38.809  1.00 12.09 ? 80  HIS B CB  1 
ATOM   1711  C  CG  . HIS B  1 80  ? 13.700  105.464 40.230  1.00 13.12 ? 80  HIS B CG  1 
ATOM   1712  N  ND1 . HIS B  1 80  ? 14.881  105.419 40.943  1.00 12.08 ? 80  HIS B ND1 1 
ATOM   1713  C  CD2 . HIS B  1 80  ? 12.774  105.984 41.066  1.00 13.09 ? 80  HIS B CD2 1 
ATOM   1714  C  CE1 . HIS B  1 80  ? 14.673  105.893 42.156  1.00 13.84 ? 80  HIS B CE1 1 
ATOM   1715  N  NE2 . HIS B  1 80  ? 13.403  106.240 42.256  1.00 17.00 ? 80  HIS B NE2 1 
ATOM   1716  N  N   . VAL B  1 81  ? 11.738  104.559 36.128  1.00 11.24 ? 81  VAL B N   1 
ATOM   1717  C  CA  . VAL B  1 81  ? 11.848  104.243 34.716  1.00 9.65  ? 81  VAL B CA  1 
ATOM   1718  C  C   . VAL B  1 81  ? 13.316  104.001 34.329  1.00 9.97  ? 81  VAL B C   1 
ATOM   1719  O  O   . VAL B  1 81  ? 13.613  103.082 33.588  1.00 8.78  ? 81  VAL B O   1 
ATOM   1720  C  CB  . VAL B  1 81  ? 11.172  105.326 33.820  1.00 13.49 ? 81  VAL B CB  1 
ATOM   1721  C  CG1 . VAL B  1 81  ? 11.618  105.210 32.369  1.00 11.18 ? 81  VAL B CG1 1 
ATOM   1722  C  CG2 . VAL B  1 81  ? 9.647   105.185 33.888  1.00 15.16 ? 81  VAL B CG2 1 
ATOM   1723  N  N   . GLY B  1 82  ? 14.239  104.770 34.887  1.00 8.32  ? 82  GLY B N   1 
ATOM   1724  C  CA  . GLY B  1 82  ? 15.629  104.610 34.492  1.00 11.26 ? 82  GLY B CA  1 
ATOM   1725  C  C   . GLY B  1 82  ? 16.398  103.479 35.161  1.00 13.51 ? 82  GLY B C   1 
ATOM   1726  O  O   . GLY B  1 82  ? 17.606  103.359 34.965  1.00 10.19 ? 82  GLY B O   1 
ATOM   1727  N  N   . ASP B  1 83  ? 15.712  102.656 35.956  1.00 10.62 ? 83  ASP B N   1 
ATOM   1728  C  CA  . ASP B  1 83  ? 16.375  101.603 36.695  1.00 9.54  ? 83  ASP B CA  1 
ATOM   1729  C  C   . ASP B  1 83  ? 16.615  100.394 35.802  1.00 8.47  ? 83  ASP B C   1 
ATOM   1730  O  O   . ASP B  1 83  ? 15.751  99.552  35.676  1.00 8.85  ? 83  ASP B O   1 
ATOM   1731  C  CB  . ASP B  1 83  ? 15.548  101.181 37.900  1.00 8.61  ? 83  ASP B CB  1 
ATOM   1732  C  CG  . ASP B  1 83  ? 15.514  102.227 39.006  1.00 11.52 ? 83  ASP B CG  1 
ATOM   1733  O  OD1 . ASP B  1 83  ? 16.421  103.073 39.110  1.00 7.69  ? 83  ASP B OD1 1 
ATOM   1734  O  OD2 . ASP B  1 83  ? 14.569  102.170 39.815  1.00 11.43 ? 83  ASP B OD2 1 
ATOM   1735  N  N   . LEU B  1 84  ? 17.787  100.299 35.182  1.00 8.08  ? 84  LEU B N   1 
ATOM   1736  C  CA  . LEU B  1 84  ? 18.085  99.146  34.319  1.00 7.03  ? 84  LEU B CA  1 
ATOM   1737  C  C   . LEU B  1 84  ? 18.904  98.055  35.041  1.00 8.94  ? 84  LEU B C   1 
ATOM   1738  O  O   . LEU B  1 84  ? 19.333  97.085  34.425  1.00 15.15 ? 84  LEU B O   1 
ATOM   1739  C  CB  . LEU B  1 84  ? 18.763  99.573  32.996  1.00 7.31  ? 84  LEU B CB  1 
ATOM   1740  C  CG  . LEU B  1 84  ? 17.949  100.482 32.062  1.00 11.85 ? 84  LEU B CG  1 
ATOM   1741  C  CD1 . LEU B  1 84  ? 18.707  100.864 30.766  1.00 9.14  ? 84  LEU B CD1 1 
ATOM   1742  C  CD2 . LEU B  1 84  ? 16.633  99.818  31.692  1.00 11.42 ? 84  LEU B CD2 1 
ATOM   1743  N  N   . GLY B  1 85  ? 19.114  98.187  36.343  1.00 11.12 ? 85  GLY B N   1 
ATOM   1744  C  CA  . GLY B  1 85  ? 19.726  97.088  37.072  1.00 12.23 ? 85  GLY B CA  1 
ATOM   1745  C  C   . GLY B  1 85  ? 21.245  97.114  37.006  1.00 11.31 ? 85  GLY B C   1 
ATOM   1746  O  O   . GLY B  1 85  ? 21.832  98.151  37.261  1.00 9.13  ? 85  GLY B O   1 
ATOM   1747  N  N   . ASN B  1 86  ? 21.864  95.974  36.703  1.00 11.17 ? 86  ASN B N   1 
ATOM   1748  C  CA  . ASN B  1 86  ? 23.311  95.878  36.618  1.00 11.97 ? 86  ASN B CA  1 
ATOM   1749  C  C   . ASN B  1 86  ? 23.788  95.355  35.283  1.00 11.51 ? 86  ASN B C   1 
ATOM   1750  O  O   . ASN B  1 86  ? 23.064  94.636  34.587  1.00 11.01 ? 86  ASN B O   1 
ATOM   1751  C  CB  . ASN B  1 86  ? 23.886  94.968  37.707  1.00 10.99 ? 86  ASN B CB  1 
ATOM   1752  C  CG  . ASN B  1 86  ? 23.672  95.512  39.087  1.00 12.43 ? 86  ASN B CG  1 
ATOM   1753  O  OD1 . ASN B  1 86  ? 24.253  96.536  39.457  1.00 10.40 ? 86  ASN B OD1 1 
ATOM   1754  N  ND2 . ASN B  1 86  ? 22.820  94.830  39.874  1.00 13.12 ? 86  ASN B ND2 1 
ATOM   1755  N  N   . VAL B  1 87  ? 25.028  95.709  34.944  1.00 9.29  ? 87  VAL B N   1 
ATOM   1756  C  CA  . VAL B  1 87  ? 25.739  95.007  33.901  1.00 9.58  ? 87  VAL B CA  1 
ATOM   1757  C  C   . VAL B  1 87  ? 26.965  94.319  34.527  1.00 12.11 ? 87  VAL B C   1 
ATOM   1758  O  O   . VAL B  1 87  ? 27.465  94.747  35.581  1.00 11.87 ? 87  VAL B O   1 
ATOM   1759  C  CB  . VAL B  1 87  ? 26.133  95.944  32.757  1.00 14.38 ? 87  VAL B CB  1 
ATOM   1760  C  CG1 . VAL B  1 87  ? 24.876  96.635  32.160  1.00 10.68 ? 87  VAL B CG1 1 
ATOM   1761  C  CG2 . VAL B  1 87  ? 27.158  96.957  33.228  1.00 7.83  ? 87  VAL B CG2 1 
ATOM   1762  N  N   . THR B  1 88  ? 27.439  93.256  33.883  1.00 10.77 ? 88  THR B N   1 
ATOM   1763  C  CA  . THR B  1 88  ? 28.535  92.458  34.428  1.00 15.62 ? 88  THR B CA  1 
ATOM   1764  C  C   . THR B  1 88  ? 29.795  92.616  33.572  1.00 13.30 ? 88  THR B C   1 
ATOM   1765  O  O   . THR B  1 88  ? 29.773  92.376  32.374  1.00 12.54 ? 88  THR B O   1 
ATOM   1766  C  CB  . THR B  1 88  ? 28.142  90.954  34.537  1.00 17.66 ? 88  THR B CB  1 
ATOM   1767  O  OG1 . THR B  1 88  ? 27.009  90.818  35.408  1.00 17.02 ? 88  THR B OG1 1 
ATOM   1768  C  CG2 . THR B  1 88  ? 29.305  90.118  35.098  1.00 13.94 ? 88  THR B CG2 1 
ATOM   1769  N  N   . ALA B  1 89  ? 30.883  93.055  34.188  1.00 14.02 ? 89  ALA B N   1 
ATOM   1770  C  CA  . ALA B  1 89  ? 32.157  93.125  33.480  1.00 16.00 ? 89  ALA B CA  1 
ATOM   1771  C  C   . ALA B  1 89  ? 32.939  91.836  33.743  1.00 17.87 ? 89  ALA B C   1 
ATOM   1772  O  O   . ALA B  1 89  ? 33.053  91.400  34.896  1.00 16.90 ? 89  ALA B O   1 
ATOM   1773  C  CB  . ALA B  1 89  ? 32.951  94.325  33.945  1.00 13.17 ? 89  ALA B CB  1 
ATOM   1774  N  N   . ASP B  1 90  ? 33.465  91.232  32.681  1.00 17.17 ? 90  ASP B N   1 
ATOM   1775  C  CA  . ASP B  1 90  ? 34.235  89.999  32.814  1.00 17.76 ? 90  ASP B CA  1 
ATOM   1776  C  C   . ASP B  1 90  ? 35.625  90.231  33.400  1.00 18.57 ? 90  ASP B C   1 
ATOM   1777  O  O   . ASP B  1 90  ? 35.924  91.323  33.894  1.00 18.86 ? 90  ASP B O   1 
ATOM   1778  C  CB  . ASP B  1 90  ? 34.328  89.254  31.484  1.00 19.21 ? 90  ASP B CB  1 
ATOM   1779  C  CG  . ASP B  1 90  ? 35.086  90.039  30.405  1.00 18.03 ? 90  ASP B CG  1 
ATOM   1780  O  OD1 . ASP B  1 90  ? 35.834  90.997  30.706  1.00 14.12 ? 90  ASP B OD1 1 
ATOM   1781  O  OD2 . ASP B  1 90  ? 34.920  89.670  29.232  1.00 19.88 ? 90  ASP B OD2 1 
ATOM   1782  N  N   . LYS B  1 91  ? 36.477  89.207  33.352  1.00 18.70 ? 91  LYS B N   1 
ATOM   1783  C  CA  . LYS B  1 91  ? 37.796  89.308  33.997  1.00 21.25 ? 91  LYS B CA  1 
ATOM   1784  C  C   . LYS B  1 91  ? 38.711  90.306  33.279  1.00 20.51 ? 91  LYS B C   1 
ATOM   1785  O  O   . LYS B  1 91  ? 39.638  90.844  33.883  1.00 17.99 ? 91  LYS B O   1 
ATOM   1786  C  CB  . LYS B  1 91  ? 38.460  87.937  34.087  1.00 22.45 ? 91  LYS B CB  1 
ATOM   1787  C  CG  . LYS B  1 91  ? 38.525  87.207  32.743  1.00 27.58 ? 91  LYS B CG  1 
ATOM   1788  C  CD  . LYS B  1 91  ? 39.083  85.793  32.905  1.00 34.09 ? 91  LYS B CD  1 
ATOM   1789  C  CE  . LYS B  1 91  ? 39.491  85.205  31.564  1.00 36.59 ? 91  LYS B CE  1 
ATOM   1790  N  NZ  . LYS B  1 91  ? 40.474  84.083  31.728  1.00 48.68 ? 91  LYS B NZ  1 
ATOM   1791  N  N   . ASP B  1 92  ? 38.428  90.570  32.001  1.00 14.12 ? 92  ASP B N   1 
ATOM   1792  C  CA  . ASP B  1 92  ? 39.205  91.536  31.223  1.00 16.83 ? 92  ASP B CA  1 
ATOM   1793  C  C   . ASP B  1 92  ? 38.610  92.931  31.327  1.00 18.99 ? 92  ASP B C   1 
ATOM   1794  O  O   . ASP B  1 92  ? 39.015  93.839  30.598  1.00 16.52 ? 92  ASP B O   1 
ATOM   1795  C  CB  . ASP B  1 92  ? 39.257  91.124  29.749  1.00 16.87 ? 92  ASP B CB  1 
ATOM   1796  C  CG  . ASP B  1 92  ? 39.791  89.715  29.560  1.00 26.33 ? 92  ASP B CG  1 
ATOM   1797  O  OD1 . ASP B  1 92  ? 40.793  89.361  30.234  1.00 25.33 ? 92  ASP B OD1 1 
ATOM   1798  O  OD2 . ASP B  1 92  ? 39.199  88.965  28.756  1.00 26.82 ? 92  ASP B OD2 1 
ATOM   1799  N  N   . GLY B  1 93  ? 37.631  93.092  32.210  1.00 12.45 ? 93  GLY B N   1 
ATOM   1800  C  CA  . GLY B  1 93  ? 36.993  94.384  32.403  1.00 14.37 ? 93  GLY B CA  1 
ATOM   1801  C  C   . GLY B  1 93  ? 35.956  94.774  31.354  1.00 11.62 ? 93  GLY B C   1 
ATOM   1802  O  O   . GLY B  1 93  ? 35.573  95.930  31.267  1.00 13.04 ? 93  GLY B O   1 
ATOM   1803  N  N   . VAL B  1 94  ? 35.520  93.820  30.548  1.00 12.98 ? 94  VAL B N   1 
ATOM   1804  C  CA  . VAL B  1 94  ? 34.566  94.103  29.479  1.00 14.53 ? 94  VAL B CA  1 
ATOM   1805  C  C   . VAL B  1 94  ? 33.163  93.645  29.877  1.00 15.40 ? 94  VAL B C   1 
ATOM   1806  O  O   . VAL B  1 94  ? 32.955  92.495  30.263  1.00 16.92 ? 94  VAL B O   1 
ATOM   1807  C  CB  . VAL B  1 94  ? 34.968  93.447  28.149  1.00 14.04 ? 94  VAL B CB  1 
ATOM   1808  C  CG1 . VAL B  1 94  ? 33.943  93.765  27.048  1.00 16.60 ? 94  VAL B CG1 1 
ATOM   1809  C  CG2 . VAL B  1 94  ? 36.344  93.916  27.710  1.00 16.49 ? 94  VAL B CG2 1 
ATOM   1810  N  N   . ALA B  1 95  ? 32.218  94.568  29.823  1.00 12.02 ? 95  ALA B N   1 
ATOM   1811  C  CA  . ALA B  1 95  ? 30.804  94.226  29.967  1.00 15.41 ? 95  ALA B CA  1 
ATOM   1812  C  C   . ALA B  1 95  ? 30.148  94.221  28.600  1.00 15.40 ? 95  ALA B C   1 
ATOM   1813  O  O   . ALA B  1 95  ? 30.028  95.279  27.960  1.00 14.20 ? 95  ALA B O   1 
ATOM   1814  C  CB  . ALA B  1 95  ? 30.107  95.218  30.841  1.00 12.19 ? 95  ALA B CB  1 
ATOM   1815  N  N   . ASP B  1 96  ? 29.741  93.043  28.143  1.00 12.79 ? 96  ASP B N   1 
ATOM   1816  C  CA  . ASP B  1 96  ? 28.952  92.961  26.923  1.00 18.76 ? 96  ASP B CA  1 
ATOM   1817  C  C   . ASP B  1 96  ? 27.470  93.054  27.254  1.00 17.11 ? 96  ASP B C   1 
ATOM   1818  O  O   . ASP B  1 96  ? 26.810  92.058  27.479  1.00 17.74 ? 96  ASP B O   1 
ATOM   1819  C  CB  . ASP B  1 96  ? 29.276  91.687  26.140  1.00 23.07 ? 96  ASP B CB  1 
ATOM   1820  C  CG  . ASP B  1 96  ? 30.714  91.667  25.677  1.00 23.42 ? 96  ASP B CG  1 
ATOM   1821  O  OD1 . ASP B  1 96  ? 31.078  92.537  24.853  1.00 23.64 ? 96  ASP B OD1 1 
ATOM   1822  O  OD2 . ASP B  1 96  ? 31.490  90.819  26.170  1.00 26.11 ? 96  ASP B OD2 1 
ATOM   1823  N  N   . VAL B  1 97  ? 26.968  94.276  27.276  1.00 15.30 ? 97  VAL B N   1 
ATOM   1824  C  CA  . VAL B  1 97  ? 25.619  94.557  27.723  1.00 14.54 ? 97  VAL B CA  1 
ATOM   1825  C  C   . VAL B  1 97  ? 24.581  93.945  26.780  1.00 14.90 ? 97  VAL B C   1 
ATOM   1826  O  O   . VAL B  1 97  ? 24.697  94.046  25.577  1.00 13.37 ? 97  VAL B O   1 
ATOM   1827  C  CB  . VAL B  1 97  ? 25.423  96.075  27.846  1.00 14.69 ? 97  VAL B CB  1 
ATOM   1828  C  CG1 . VAL B  1 97  ? 23.979  96.427  28.245  1.00 9.34  ? 97  VAL B CG1 1 
ATOM   1829  C  CG2 . VAL B  1 97  ? 26.444  96.644  28.833  1.00 9.65  ? 97  VAL B CG2 1 
ATOM   1830  N  N   . SER B  1 98  ? 23.597  93.262  27.346  1.00 15.96 ? 98  SER B N   1 
ATOM   1831  C  CA  . SER B  1 98  ? 22.442  92.799  26.580  1.00 16.87 ? 98  SER B CA  1 
ATOM   1832  C  C   . SER B  1 98  ? 21.233  92.769  27.487  1.00 17.10 ? 98  SER B C   1 
ATOM   1833  O  O   . SER B  1 98  ? 21.125  91.937  28.397  1.00 19.80 ? 98  SER B O   1 
ATOM   1834  C  CB  . SER B  1 98  ? 22.665  91.429  25.951  1.00 19.30 ? 98  SER B CB  1 
ATOM   1835  O  OG  . SER B  1 98  ? 21.740  91.240  24.888  1.00 25.69 ? 98  SER B OG  1 
ATOM   1836  N  N   . ILE B  1 99  ? 20.330  93.706  27.246  1.00 14.22 ? 99  ILE B N   1 
ATOM   1837  C  CA  . ILE B  1 99  ? 19.229  93.950  28.147  1.00 13.41 ? 99  ILE B CA  1 
ATOM   1838  C  C   . ILE B  1 99  ? 18.003  94.210  27.281  1.00 14.62 ? 99  ILE B C   1 
ATOM   1839  O  O   . ILE B  1 99  ? 18.122  94.679  26.144  1.00 14.29 ? 99  ILE B O   1 
ATOM   1840  C  CB  . ILE B  1 99  ? 19.581  95.122  29.091  1.00 12.55 ? 99  ILE B CB  1 
ATOM   1841  C  CG1 . ILE B  1 99  ? 20.514  94.634  30.190  1.00 15.17 ? 99  ILE B CG1 1 
ATOM   1842  C  CG2 . ILE B  1 99  ? 18.370  95.728  29.768  1.00 12.57 ? 99  ILE B CG2 1 
ATOM   1843  C  CD1 . ILE B  1 99  ? 20.956  95.748  31.120  1.00 13.37 ? 99  ILE B CD1 1 
ATOM   1844  N  N   . GLU B  1 100 ? 16.833  93.845  27.786  1.00 15.55 ? 100 GLU B N   1 
ATOM   1845  C  CA  . GLU B  1 100 ? 15.594  94.154  27.100  1.00 14.74 ? 100 GLU B CA  1 
ATOM   1846  C  C   . GLU B  1 100 ? 14.668  94.697  28.165  1.00 15.44 ? 100 GLU B C   1 
ATOM   1847  O  O   . GLU B  1 100 ? 14.517  94.096  29.215  1.00 14.28 ? 100 GLU B O   1 
ATOM   1848  C  CB  . GLU B  1 100 ? 15.041  92.915  26.407  1.00 15.63 ? 100 GLU B CB  1 
ATOM   1849  C  CG  . GLU B  1 100 ? 13.759  93.151  25.620  1.00 23.59 ? 100 GLU B CG  1 
ATOM   1850  C  CD  . GLU B  1 100 ? 13.502  92.070  24.559  1.00 30.11 ? 100 GLU B CD  1 
ATOM   1851  O  OE1 . GLU B  1 100 ? 14.436  91.309  24.213  1.00 33.71 ? 100 GLU B OE1 1 
ATOM   1852  O  OE2 . GLU B  1 100 ? 12.366  91.985  24.057  1.00 29.64 ? 100 GLU B OE2 1 
ATOM   1853  N  N   . ASP B  1 101 ? 14.108  95.875  27.932  1.00 11.99 ? 101 ASP B N   1 
ATOM   1854  C  CA  . ASP B  1 101 ? 13.299  96.517  28.961  1.00 16.94 ? 101 ASP B CA  1 
ATOM   1855  C  C   . ASP B  1 101 ? 12.063  97.140  28.334  1.00 17.37 ? 101 ASP B C   1 
ATOM   1856  O  O   . ASP B  1 101 ? 12.112  97.676  27.219  1.00 10.95 ? 101 ASP B O   1 
ATOM   1857  C  CB  . ASP B  1 101 ? 14.098  97.573  29.737  1.00 12.24 ? 101 ASP B CB  1 
ATOM   1858  C  CG  . ASP B  1 101 ? 13.391  98.038  31.014  1.00 15.74 ? 101 ASP B CG  1 
ATOM   1859  O  OD1 . ASP B  1 101 ? 13.469  97.314  32.034  1.00 15.91 ? 101 ASP B OD1 1 
ATOM   1860  O  OD2 . ASP B  1 101 ? 12.797  99.147  31.024  1.00 12.20 ? 101 ASP B OD2 1 
ATOM   1861  N  N   . SER B  1 102 ? 10.971  97.087  29.089  1.00 15.64 ? 102 SER B N   1 
ATOM   1862  C  CA  . SER B  1 102 ? 9.671   97.479  28.600  1.00 14.29 ? 102 SER B CA  1 
ATOM   1863  C  C   . SER B  1 102 ? 9.145   98.732  29.281  1.00 16.10 ? 102 SER B C   1 
ATOM   1864  O  O   . SER B  1 102 ? 8.051   99.214  28.971  1.00 18.42 ? 102 SER B O   1 
ATOM   1865  C  CB  . SER B  1 102 ? 8.718   96.317  28.819  1.00 19.51 ? 102 SER B CB  1 
ATOM   1866  O  OG  . SER B  1 102 ? 8.996   95.324  27.850  1.00 25.06 ? 102 SER B OG  1 
ATOM   1867  N  N   . VAL B  1 103 ? 9.930   99.268  30.201  1.00 13.73 ? 103 VAL B N   1 
ATOM   1868  C  CA  . VAL B  1 103 ? 9.545   100.477 30.909  1.00 10.39 ? 103 VAL B CA  1 
ATOM   1869  C  C   . VAL B  1 103 ? 10.212  101.721 30.301  1.00 16.92 ? 103 VAL B C   1 
ATOM   1870  O  O   . VAL B  1 103 ? 9.543   102.733 30.091  1.00 14.19 ? 103 VAL B O   1 
ATOM   1871  C  CB  . VAL B  1 103 ? 9.823   100.326 32.418  1.00 13.69 ? 103 VAL B CB  1 
ATOM   1872  C  CG1 . VAL B  1 103 ? 9.335   101.532 33.199  1.00 10.47 ? 103 VAL B CG1 1 
ATOM   1873  C  CG2 . VAL B  1 103 ? 9.128   99.050  32.929  1.00 14.60 ? 103 VAL B CG2 1 
ATOM   1874  N  N   . ILE B  1 104 ? 11.518  101.666 30.003  1.00 12.15 ? 104 ILE B N   1 
ATOM   1875  C  CA  . ILE B  1 104 ? 12.104  102.765 29.242  1.00 12.48 ? 104 ILE B CA  1 
ATOM   1876  C  C   . ILE B  1 104 ? 11.436  102.743 27.871  1.00 9.79  ? 104 ILE B C   1 
ATOM   1877  O  O   . ILE B  1 104 ? 10.936  101.703 27.456  1.00 9.63  ? 104 ILE B O   1 
ATOM   1878  C  CB  . ILE B  1 104 ? 13.647  102.644 29.081  1.00 8.04  ? 104 ILE B CB  1 
ATOM   1879  C  CG1 . ILE B  1 104 ? 14.011  101.328 28.398  1.00 9.98  ? 104 ILE B CG1 1 
ATOM   1880  C  CG2 . ILE B  1 104 ? 14.336  102.811 30.464  1.00 8.87  ? 104 ILE B CG2 1 
ATOM   1881  C  CD1 . ILE B  1 104 ? 15.475  101.214 27.880  1.00 10.38 ? 104 ILE B CD1 1 
ATOM   1882  N  N   . SER B  1 105 ? 11.424  103.884 27.184  1.00 10.02 ? 105 SER B N   1 
ATOM   1883  C  CA  . SER B  1 105 ? 10.967  103.932 25.796  1.00 11.14 ? 105 SER B CA  1 
ATOM   1884  C  C   . SER B  1 105 ? 11.760  104.945 24.971  1.00 12.06 ? 105 SER B C   1 
ATOM   1885  O  O   . SER B  1 105 ? 12.433  105.814 25.521  1.00 11.22 ? 105 SER B O   1 
ATOM   1886  C  CB  . SER B  1 105 ? 9.459   104.266 25.733  1.00 9.89  ? 105 SER B CB  1 
ATOM   1887  O  OG  . SER B  1 105 ? 9.036   104.213 24.391  1.00 11.94 ? 105 SER B OG  1 
ATOM   1888  N  N   . LEU B  1 106 ? 11.679  104.849 23.649  1.00 11.87 ? 106 LEU B N   1 
ATOM   1889  C  CA  . LEU B  1 106 ? 12.347  105.844 22.818  1.00 13.47 ? 106 LEU B CA  1 
ATOM   1890  C  C   . LEU B  1 106 ? 11.339  106.874 22.319  1.00 17.67 ? 106 LEU B C   1 
ATOM   1891  O  O   . LEU B  1 106 ? 11.628  107.629 21.384  1.00 16.17 ? 106 LEU B O   1 
ATOM   1892  C  CB  . LEU B  1 106 ? 13.081  105.207 21.639  1.00 9.00  ? 106 LEU B CB  1 
ATOM   1893  C  CG  . LEU B  1 106 ? 14.190  104.194 21.942  1.00 11.64 ? 106 LEU B CG  1 
ATOM   1894  C  CD1 . LEU B  1 106 ? 14.841  103.718 20.627  1.00 10.49 ? 106 LEU B CD1 1 
ATOM   1895  C  CD2 . LEU B  1 106 ? 15.220  104.772 22.879  1.00 7.12  ? 106 LEU B CD2 1 
ATOM   1896  N  N   . SER B  1 107 ? 10.163  106.901 22.951  1.00 14.21 ? 107 SER B N   1 
ATOM   1897  C  CA  . SER B  1 107 ? 9.141   107.897 22.620  1.00 16.08 ? 107 SER B CA  1 
ATOM   1898  C  C   . SER B  1 107 ? 8.116   108.015 23.742  1.00 16.48 ? 107 SER B C   1 
ATOM   1899  O  O   . SER B  1 107 ? 8.050   107.155 24.619  1.00 14.79 ? 107 SER B O   1 
ATOM   1900  C  CB  . SER B  1 107 ? 8.442   107.525 21.313  1.00 17.66 ? 107 SER B CB  1 
ATOM   1901  O  OG  . SER B  1 107 ? 7.844   106.236 21.409  1.00 24.97 ? 107 SER B OG  1 
ATOM   1902  N  N   . GLY B  1 108 ? 7.322   109.081 23.723  1.00 17.68 ? 108 GLY B N   1 
ATOM   1903  C  CA  . GLY B  1 108 ? 6.277   109.255 24.717  1.00 19.08 ? 108 GLY B CA  1 
ATOM   1904  C  C   . GLY B  1 108 ? 6.835   109.694 26.057  1.00 20.59 ? 108 GLY B C   1 
ATOM   1905  O  O   . GLY B  1 108 ? 7.967   110.163 26.165  1.00 18.26 ? 108 GLY B O   1 
ATOM   1906  N  N   . ASP B  1 109 ? 6.073   109.533 27.117  1.00 18.02 ? 109 ASP B N   1 
ATOM   1907  C  CA  . ASP B  1 109 ? 6.557   110.125 28.354  1.00 23.17 ? 109 ASP B CA  1 
ATOM   1908  C  C   . ASP B  1 109 ? 7.589   109.303 29.133  1.00 16.83 ? 109 ASP B C   1 
ATOM   1909  O  O   . ASP B  1 109 ? 8.126   109.785 30.122  1.00 15.30 ? 109 ASP B O   1 
ATOM   1910  C  CB  . ASP B  1 109 ? 5.404   110.596 29.237  1.00 26.71 ? 109 ASP B CB  1 
ATOM   1911  C  CG  . ASP B  1 109 ? 4.290   109.613 29.286  1.00 33.12 ? 109 ASP B CG  1 
ATOM   1912  O  OD1 . ASP B  1 109 ? 4.596   108.394 29.186  1.00 28.31 ? 109 ASP B OD1 1 
ATOM   1913  O  OD2 . ASP B  1 109 ? 3.126   110.066 29.421  1.00 32.28 ? 109 ASP B OD2 1 
ATOM   1914  N  N   . HIS B  1 110 ? 7.875   108.087 28.680  1.00 14.32 ? 110 HIS B N   1 
ATOM   1915  C  CA  . HIS B  1 110 ? 9.022   107.341 29.211  1.00 17.22 ? 110 HIS B CA  1 
ATOM   1916  C  C   . HIS B  1 110 ? 10.251  107.475 28.303  1.00 14.57 ? 110 HIS B C   1 
ATOM   1917  O  O   . HIS B  1 110 ? 11.207  106.663 28.373  1.00 11.80 ? 110 HIS B O   1 
ATOM   1918  C  CB  . HIS B  1 110 ? 8.684   105.858 29.417  1.00 17.25 ? 110 HIS B CB  1 
ATOM   1919  C  CG  . HIS B  1 110 ? 7.639   105.624 30.461  1.00 23.46 ? 110 HIS B CG  1 
ATOM   1920  N  ND1 . HIS B  1 110 ? 7.049   104.394 30.665  1.00 26.70 ? 110 HIS B ND1 1 
ATOM   1921  C  CD2 . HIS B  1 110 ? 7.065   106.471 31.348  1.00 25.01 ? 110 HIS B CD2 1 
ATOM   1922  C  CE1 . HIS B  1 110 ? 6.156   104.494 31.634  1.00 29.12 ? 110 HIS B CE1 1 
ATOM   1923  N  NE2 . HIS B  1 110 ? 6.150   105.742 32.070  1.00 29.26 ? 110 HIS B NE2 1 
ATOM   1924  N  N   . CYS B  1 111 ? 10.226  108.493 27.452  1.00 12.66 ? 111 CYS B N   1 
ATOM   1925  C  CA  . CYS B  1 111 ? 11.290  108.662 26.469  1.00 13.14 ? 111 CYS B CA  1 
ATOM   1926  C  C   . CYS B  1 111 ? 12.611  108.916 27.185  1.00 11.09 ? 111 CYS B C   1 
ATOM   1927  O  O   . CYS B  1 111 ? 12.673  109.702 28.129  1.00 10.31 ? 111 CYS B O   1 
ATOM   1928  C  CB  . CYS B  1 111 ? 10.974  109.818 25.517  1.00 12.17 ? 111 CYS B CB  1 
ATOM   1929  S  SG  . CYS B  1 111 ? 12.188  110.026 24.197  1.00 16.21 ? 111 CYS B SG  1 
ATOM   1930  N  N   . ILE B  1 112 ? 13.671  108.250 26.755  1.00 8.96  ? 112 ILE B N   1 
ATOM   1931  C  CA  . ILE B  1 112 ? 14.970  108.491 27.395  1.00 9.03  ? 112 ILE B CA  1 
ATOM   1932  C  C   . ILE B  1 112 ? 15.941  109.246 26.488  1.00 9.91  ? 112 ILE B C   1 
ATOM   1933  O  O   . ILE B  1 112 ? 17.076  109.524 26.875  1.00 8.01  ? 112 ILE B O   1 
ATOM   1934  C  CB  . ILE B  1 112 ? 15.609  107.197 27.844  1.00 7.57  ? 112 ILE B CB  1 
ATOM   1935  C  CG1 . ILE B  1 112 ? 15.760  106.258 26.640  1.00 6.78  ? 112 ILE B CG1 1 
ATOM   1936  C  CG2 . ILE B  1 112 ? 14.780  106.564 28.983  1.00 7.62  ? 112 ILE B CG2 1 
ATOM   1937  C  CD1 . ILE B  1 112 ? 16.478  104.978 26.978  1.00 7.32  ? 112 ILE B CD1 1 
ATOM   1938  N  N   . ILE B  1 113 ? 15.487  109.564 25.278  1.00 9.82  ? 113 ILE B N   1 
ATOM   1939  C  CA  . ILE B  1 113 ? 16.308  110.307 24.330  1.00 9.95  ? 113 ILE B CA  1 
ATOM   1940  C  C   . ILE B  1 113 ? 16.589  111.681 24.914  1.00 9.63  ? 113 ILE B C   1 
ATOM   1941  O  O   . ILE B  1 113 ? 15.691  112.317 25.464  1.00 8.46  ? 113 ILE B O   1 
ATOM   1942  C  CB  . ILE B  1 113 ? 15.606  110.417 22.962  1.00 11.40 ? 113 ILE B CB  1 
ATOM   1943  C  CG1 . ILE B  1 113 ? 15.473  109.012 22.366  1.00 9.93  ? 113 ILE B CG1 1 
ATOM   1944  C  CG2 . ILE B  1 113 ? 16.369  111.378 22.043  1.00 11.91 ? 113 ILE B CG2 1 
ATOM   1945  C  CD1 . ILE B  1 113 ? 15.053  108.981 20.981  1.00 13.13 ? 113 ILE B CD1 1 
ATOM   1946  N  N   . GLY B  1 114 ? 17.847  112.114 24.871  1.00 8.80  ? 114 GLY B N   1 
ATOM   1947  C  CA  . GLY B  1 114 ? 18.201  113.400 25.456  1.00 6.88  ? 114 GLY B CA  1 
ATOM   1948  C  C   . GLY B  1 114 ? 18.434  113.328 26.963  1.00 5.86  ? 114 GLY B C   1 
ATOM   1949  O  O   . GLY B  1 114 ? 18.595  114.344 27.645  1.00 4.92  ? 114 GLY B O   1 
ATOM   1950  N  N   . ARG B  1 115 ? 18.419  112.124 27.496  1.00 5.10  ? 115 ARG B N   1 
ATOM   1951  C  CA  . ARG B  1 115 ? 18.761  111.948 28.899  1.00 8.06  ? 115 ARG B CA  1 
ATOM   1952  C  C   . ARG B  1 115 ? 20.154  111.276 28.961  1.00 7.73  ? 115 ARG B C   1 
ATOM   1953  O  O   . ARG B  1 115 ? 20.804  111.068 27.912  1.00 7.50  ? 115 ARG B O   1 
ATOM   1954  C  CB  . ARG B  1 115 ? 17.649  111.181 29.630  1.00 7.74  ? 115 ARG B CB  1 
ATOM   1955  C  CG  . ARG B  1 115 ? 16.265  111.864 29.441  1.00 9.83  ? 115 ARG B CG  1 
ATOM   1956  C  CD  . ARG B  1 115 ? 15.111  111.239 30.259  1.00 13.92 ? 115 ARG B CD  1 
ATOM   1957  N  NE  . ARG B  1 115 ? 13.800  111.799 29.890  1.00 11.10 ? 115 ARG B NE  1 
ATOM   1958  C  CZ  . ARG B  1 115 ? 13.289  112.918 30.397  1.00 13.96 ? 115 ARG B CZ  1 
ATOM   1959  N  NH1 . ARG B  1 115 ? 13.951  113.599 31.325  1.00 9.46  ? 115 ARG B NH1 1 
ATOM   1960  N  NH2 . ARG B  1 115 ? 12.091  113.344 29.991  1.00 14.61 ? 115 ARG B NH2 1 
ATOM   1961  N  N   . THR B  1 116 ? 20.609  110.951 30.163  1.00 7.69  ? 116 THR B N   1 
ATOM   1962  C  CA  . THR B  1 116 ? 21.984  110.499 30.386  1.00 7.94  ? 116 THR B CA  1 
ATOM   1963  C  C   . THR B  1 116 ? 22.042  109.061 30.865  1.00 8.67  ? 116 THR B C   1 
ATOM   1964  O  O   . THR B  1 116 ? 21.439  108.703 31.882  1.00 8.26  ? 116 THR B O   1 
ATOM   1965  C  CB  . THR B  1 116 ? 22.707  111.364 31.446  1.00 8.36  ? 116 THR B CB  1 
ATOM   1966  O  OG1 . THR B  1 116 ? 22.929  112.688 30.938  1.00 7.44  ? 116 THR B OG1 1 
ATOM   1967  C  CG2 . THR B  1 116 ? 24.049  110.750 31.809  1.00 6.50  ? 116 THR B CG2 1 
ATOM   1968  N  N   . LEU B  1 117 ? 22.752  108.228 30.115  1.00 7.38  ? 117 LEU B N   1 
ATOM   1969  C  CA  . LEU B  1 117 ? 23.027  106.879 30.562  1.00 6.49  ? 117 LEU B CA  1 
ATOM   1970  C  C   . LEU B  1 117 ? 24.250  106.936 31.479  1.00 9.44  ? 117 LEU B C   1 
ATOM   1971  O  O   . LEU B  1 117 ? 25.215  107.622 31.164  1.00 8.59  ? 117 LEU B O   1 
ATOM   1972  C  CB  . LEU B  1 117 ? 23.295  106.001 29.353  1.00 6.19  ? 117 LEU B CB  1 
ATOM   1973  C  CG  . LEU B  1 117 ? 23.507  104.517 29.616  1.00 6.68  ? 117 LEU B CG  1 
ATOM   1974  C  CD1 . LEU B  1 117 ? 22.253  103.909 30.225  1.00 10.34 ? 117 LEU B CD1 1 
ATOM   1975  C  CD2 . LEU B  1 117 ? 23.856  103.813 28.332  1.00 7.24  ? 117 LEU B CD2 1 
ATOM   1976  N  N   . VAL B  1 118 ? 24.204  106.240 32.613  1.00 8.72  ? 118 VAL B N   1 
ATOM   1977  C  CA  . VAL B  1 118 ? 25.329  106.208 33.556  1.00 8.34  ? 118 VAL B CA  1 
ATOM   1978  C  C   . VAL B  1 118 ? 25.698  104.770 33.962  1.00 9.28  ? 118 VAL B C   1 
ATOM   1979  O  O   . VAL B  1 118 ? 24.827  103.978 34.342  1.00 8.94  ? 118 VAL B O   1 
ATOM   1980  C  CB  . VAL B  1 118 ? 25.025  107.039 34.829  1.00 10.15 ? 118 VAL B CB  1 
ATOM   1981  C  CG1 . VAL B  1 118 ? 26.247  107.088 35.771  1.00 9.97  ? 118 VAL B CG1 1 
ATOM   1982  C  CG2 . VAL B  1 118 ? 24.564  108.450 34.453  1.00 9.16  ? 118 VAL B CG2 1 
ATOM   1983  N  N   . VAL B  1 119 ? 26.979  104.427 33.881  1.00 7.33  ? 119 VAL B N   1 
ATOM   1984  C  CA  . VAL B  1 119 ? 27.444  103.192 34.491  1.00 6.81  ? 119 VAL B CA  1 
ATOM   1985  C  C   . VAL B  1 119 ? 28.200  103.521 35.784  1.00 9.72  ? 119 VAL B C   1 
ATOM   1986  O  O   . VAL B  1 119 ? 29.014  104.451 35.828  1.00 8.78  ? 119 VAL B O   1 
ATOM   1987  C  CB  . VAL B  1 119 ? 28.254  102.306 33.521  1.00 10.73 ? 119 VAL B CB  1 
ATOM   1988  C  CG1 . VAL B  1 119 ? 29.516  103.028 33.018  1.00 8.20  ? 119 VAL B CG1 1 
ATOM   1989  C  CG2 . VAL B  1 119 ? 28.593  100.931 34.179  1.00 7.76  ? 119 VAL B CG2 1 
ATOM   1990  N  N   . HIS B  1 120 ? 27.902  102.757 36.831  1.00 7.52  ? 120 HIS B N   1 
ATOM   1991  C  CA  . HIS B  1 120 ? 28.315  103.067 38.191  1.00 12.32 ? 120 HIS B CA  1 
ATOM   1992  C  C   . HIS B  1 120 ? 29.493  102.255 38.721  1.00 10.27 ? 120 HIS B C   1 
ATOM   1993  O  O   . HIS B  1 120 ? 29.798  101.174 38.237  1.00 10.46 ? 120 HIS B O   1 
ATOM   1994  C  CB  . HIS B  1 120 ? 27.119  102.890 39.142  1.00 11.01 ? 120 HIS B CB  1 
ATOM   1995  C  CG  . HIS B  1 120 ? 26.232  104.090 39.202  1.00 13.29 ? 120 HIS B CG  1 
ATOM   1996  N  ND1 . HIS B  1 120 ? 26.363  105.064 40.172  1.00 12.61 ? 120 HIS B ND1 1 
ATOM   1997  C  CD2 . HIS B  1 120 ? 25.234  104.501 38.385  1.00 9.87  ? 120 HIS B CD2 1 
ATOM   1998  C  CE1 . HIS B  1 120 ? 25.467  106.010 39.963  1.00 11.78 ? 120 HIS B CE1 1 
ATOM   1999  N  NE2 . HIS B  1 120 ? 24.780  105.699 38.880  1.00 10.44 ? 120 HIS B NE2 1 
ATOM   2000  N  N   . GLU B  1 121 ? 30.123  102.793 39.748  1.00 13.51 ? 121 GLU B N   1 
ATOM   2001  C  CA  . GLU B  1 121 ? 31.283  102.161 40.379  1.00 13.44 ? 121 GLU B CA  1 
ATOM   2002  C  C   . GLU B  1 121 ? 31.017  100.766 40.967  1.00 14.88 ? 121 GLU B C   1 
ATOM   2003  O  O   . GLU B  1 121 ? 31.819  99.848  40.761  1.00 12.83 ? 121 GLU B O   1 
ATOM   2004  C  CB  . GLU B  1 121 ? 31.815  103.077 41.458  1.00 12.68 ? 121 GLU B CB  1 
ATOM   2005  C  CG  . GLU B  1 121 ? 32.835  102.425 42.378  1.00 18.50 ? 121 GLU B CG  1 
ATOM   2006  C  CD  . GLU B  1 121 ? 33.080  103.263 43.607  1.00 19.98 ? 121 GLU B CD  1 
ATOM   2007  O  OE1 . GLU B  1 121 ? 34.225  103.264 44.095  1.00 24.94 ? 121 GLU B OE1 1 
ATOM   2008  O  OE2 . GLU B  1 121 ? 32.123  103.924 44.085  1.00 18.77 ? 121 GLU B OE2 1 
ATOM   2009  N  N   . LYS B  1 122 ? 29.898  100.606 41.680  1.00 11.53 ? 122 LYS B N   1 
ATOM   2010  C  CA  . LYS B  1 122 ? 29.558  99.315  42.295  1.00 14.70 ? 122 LYS B CA  1 
ATOM   2011  C  C   . LYS B  1 122 ? 28.198  98.768  41.827  1.00 14.02 ? 122 LYS B C   1 
ATOM   2012  O  O   . LYS B  1 122 ? 27.532  99.363  40.997  1.00 12.12 ? 122 LYS B O   1 
ATOM   2013  C  CB  . LYS B  1 122 ? 29.492  99.430  43.820  1.00 16.84 ? 122 LYS B CB  1 
ATOM   2014  C  CG  . LYS B  1 122 ? 30.483  100.355 44.456  1.00 15.54 ? 122 LYS B CG  1 
ATOM   2015  C  CD  . LYS B  1 122 ? 30.103  100.602 45.914  1.00 22.18 ? 122 LYS B CD  1 
ATOM   2016  C  CE  . LYS B  1 122 ? 31.234  101.322 46.667  1.00 32.68 ? 122 LYS B CE  1 
ATOM   2017  N  NZ  . LYS B  1 122 ? 30.890  101.552 48.100  1.00 35.47 ? 122 LYS B NZ  1 
ATOM   2018  N  N   . ALA B  1 123 ? 27.797  97.641  42.409  1.00 13.09 ? 123 ALA B N   1 
ATOM   2019  C  CA  . ALA B  1 123 ? 26.512  97.026  42.146  1.00 12.76 ? 123 ALA B CA  1 
ATOM   2020  C  C   . ALA B  1 123 ? 25.346  97.852  42.689  1.00 9.60  ? 123 ALA B C   1 
ATOM   2021  O  O   . ALA B  1 123 ? 25.411  98.445  43.773  1.00 12.10 ? 123 ALA B O   1 
ATOM   2022  C  CB  . ALA B  1 123 ? 26.483  95.607  42.719  1.00 12.55 ? 123 ALA B CB  1 
ATOM   2023  N  N   . ASP B  1 124 ? 24.295  97.917  41.890  1.00 13.54 ? 124 ASP B N   1 
ATOM   2024  C  CA  . ASP B  1 124 ? 22.987  98.425  42.328  1.00 12.25 ? 124 ASP B CA  1 
ATOM   2025  C  C   . ASP B  1 124 ? 22.389  97.337  43.229  1.00 10.07 ? 124 ASP B C   1 
ATOM   2026  O  O   . ASP B  1 124 ? 22.327  96.180  42.831  1.00 9.65  ? 124 ASP B O   1 
ATOM   2027  C  CB  . ASP B  1 124 ? 22.119  98.646  41.083  1.00 11.68 ? 124 ASP B CB  1 
ATOM   2028  C  CG  . ASP B  1 124 ? 20.767  99.322  41.377  1.00 11.99 ? 124 ASP B CG  1 
ATOM   2029  O  OD1 . ASP B  1 124 ? 20.188  99.143  42.468  1.00 11.79 ? 124 ASP B OD1 1 
ATOM   2030  O  OD2 . ASP B  1 124 ? 20.281  100.030 40.476  1.00 11.95 ? 124 ASP B OD2 1 
ATOM   2031  N  N   . ASP B  1 125 ? 21.986  97.676  44.454  1.00 13.50 ? 125 ASP B N   1 
ATOM   2032  C  CA  . ASP B  1 125 ? 21.359  96.653  45.313  1.00 13.88 ? 125 ASP B CA  1 
ATOM   2033  C  C   . ASP B  1 125 ? 19.870  96.377  44.994  1.00 15.76 ? 125 ASP B C   1 
ATOM   2034  O  O   . ASP B  1 125 ? 19.194  95.641  45.732  1.00 12.26 ? 125 ASP B O   1 
ATOM   2035  C  CB  . ASP B  1 125 ? 21.575  96.922  46.809  1.00 11.15 ? 125 ASP B CB  1 
ATOM   2036  C  CG  . ASP B  1 125 ? 20.902  98.189  47.290  1.00 15.34 ? 125 ASP B CG  1 
ATOM   2037  O  OD1 . ASP B  1 125 ? 19.895  98.638  46.694  1.00 12.13 ? 125 ASP B OD1 1 
ATOM   2038  O  OD2 . ASP B  1 125 ? 21.376  98.734  48.308  1.00 18.22 ? 125 ASP B OD2 1 
ATOM   2039  N  N   . LEU B  1 126 ? 19.388  96.971  43.896  1.00 12.70 ? 126 LEU B N   1 
ATOM   2040  C  CA  . LEU B  1 126 ? 18.012  96.806  43.415  1.00 12.32 ? 126 LEU B CA  1 
ATOM   2041  C  C   . LEU B  1 126 ? 16.953  97.131  44.478  1.00 13.89 ? 126 LEU B C   1 
ATOM   2042  O  O   . LEU B  1 126 ? 15.856  96.587  44.440  1.00 15.09 ? 126 LEU B O   1 
ATOM   2043  C  CB  . LEU B  1 126 ? 17.816  95.399  42.842  1.00 10.03 ? 126 LEU B CB  1 
ATOM   2044  C  CG  . LEU B  1 126 ? 18.992  94.927  41.966  1.00 13.30 ? 126 LEU B CG  1 
ATOM   2045  C  CD1 . LEU B  1 126 ? 18.751  93.526  41.454  1.00 14.38 ? 126 LEU B CD1 1 
ATOM   2046  C  CD2 . LEU B  1 126 ? 19.212  95.874  40.793  1.00 13.67 ? 126 LEU B CD2 1 
ATOM   2047  N  N   . GLY B  1 127 ? 17.294  98.024  45.410  1.00 12.34 ? 127 GLY B N   1 
ATOM   2048  C  CA  . GLY B  1 127 ? 16.383  98.466  46.449  1.00 12.91 ? 127 GLY B CA  1 
ATOM   2049  C  C   . GLY B  1 127 ? 16.246  97.541  47.656  1.00 18.17 ? 127 GLY B C   1 
ATOM   2050  O  O   . GLY B  1 127 ? 15.406  97.777  48.531  1.00 14.67 ? 127 GLY B O   1 
ATOM   2051  N  N   . LYS B  1 128 ? 17.087  96.511  47.726  1.00 16.73 ? 128 LYS B N   1 
ATOM   2052  C  CA  . LYS B  1 128 ? 17.006  95.518  48.790  1.00 18.10 ? 128 LYS B CA  1 
ATOM   2053  C  C   . LYS B  1 128 ? 18.096  95.674  49.861  1.00 16.67 ? 128 LYS B C   1 
ATOM   2054  O  O   . LYS B  1 128 ? 18.455  94.708  50.517  1.00 18.34 ? 128 LYS B O   1 
ATOM   2055  C  CB  . LYS B  1 128 ? 17.080  94.102  48.198  1.00 14.94 ? 128 LYS B CB  1 
ATOM   2056  C  CG  . LYS B  1 128 ? 16.092  93.832  47.109  1.00 14.51 ? 128 LYS B CG  1 
ATOM   2057  C  CD  . LYS B  1 128 ? 16.406  92.547  46.381  1.00 24.33 ? 128 LYS B CD  1 
ATOM   2058  C  CE  . LYS B  1 128 ? 15.842  91.327  47.111  1.00 32.12 ? 128 LYS B CE  1 
ATOM   2059  N  NZ  . LYS B  1 128 ? 15.961  90.070  46.281  1.00 29.38 ? 128 LYS B NZ  1 
ATOM   2060  N  N   . GLY B  1 129 ? 18.633  96.872  50.027  1.00 16.72 ? 129 GLY B N   1 
ATOM   2061  C  CA  . GLY B  1 129 ? 19.713  97.069  50.978  1.00 18.43 ? 129 GLY B CA  1 
ATOM   2062  C  C   . GLY B  1 129 ? 19.342  97.469  52.403  1.00 18.61 ? 129 GLY B C   1 
ATOM   2063  O  O   . GLY B  1 129 ? 20.171  97.410  53.317  1.00 17.59 ? 129 GLY B O   1 
ATOM   2064  N  N   . GLY B  1 130 ? 18.104  97.895  52.607  1.00 18.11 ? 130 GLY B N   1 
ATOM   2065  C  CA  . GLY B  1 130 ? 17.633  98.147  53.952  1.00 16.39 ? 130 GLY B CA  1 
ATOM   2066  C  C   . GLY B  1 130 ? 18.008  99.495  54.518  1.00 21.75 ? 130 GLY B C   1 
ATOM   2067  O  O   . GLY B  1 130 ? 18.000  99.697  55.742  1.00 19.76 ? 130 GLY B O   1 
ATOM   2068  N  N   . ASN B  1 131 ? 18.344  100.429 53.637  1.00 20.86 ? 131 ASN B N   1 
ATOM   2069  C  CA  . ASN B  1 131 ? 18.599  101.803 54.056  1.00 21.05 ? 131 ASN B CA  1 
ATOM   2070  C  C   . ASN B  1 131 ? 17.914  102.752 53.101  1.00 21.57 ? 131 ASN B C   1 
ATOM   2071  O  O   . ASN B  1 131 ? 17.455  102.337 52.036  1.00 23.81 ? 131 ASN B O   1 
ATOM   2072  C  CB  . ASN B  1 131 ? 20.100  102.108 54.186  1.00 24.87 ? 131 ASN B CB  1 
ATOM   2073  C  CG  . ASN B  1 131 ? 20.879  101.878 52.892  1.00 22.99 ? 131 ASN B CG  1 
ATOM   2074  O  OD1 . ASN B  1 131 ? 20.331  101.928 51.801  1.00 20.43 ? 131 ASN B OD1 1 
ATOM   2075  N  ND2 . ASN B  1 131 ? 22.176  101.630 53.024  1.00 24.36 ? 131 ASN B ND2 1 
ATOM   2076  N  N   . GLU B  1 132 ? 17.829  104.019 53.477  1.00 21.15 ? 132 GLU B N   1 
ATOM   2077  C  CA  . GLU B  1 132 ? 17.069  104.980 52.684  1.00 27.26 ? 132 GLU B CA  1 
ATOM   2078  C  C   . GLU B  1 132 ? 17.719  105.179 51.329  1.00 27.02 ? 132 GLU B C   1 
ATOM   2079  O  O   . GLU B  1 132 ? 17.033  105.413 50.339  1.00 27.78 ? 132 GLU B O   1 
ATOM   2080  C  CB  . GLU B  1 132 ? 16.900  106.317 53.414  1.00 28.57 ? 132 GLU B CB  1 
ATOM   2081  C  CG  . GLU B  1 132 ? 18.191  107.092 53.607  1.00 36.00 ? 132 GLU B CG  1 
ATOM   2082  C  CD  . GLU B  1 132 ? 19.274  106.265 54.284  1.00 42.29 ? 132 GLU B CD  1 
ATOM   2083  O  OE1 . GLU B  1 132 ? 20.342  106.046 53.646  1.00 41.91 ? 132 GLU B OE1 1 
ATOM   2084  O  OE2 . GLU B  1 132 ? 19.033  105.803 55.436  1.00 38.91 ? 132 GLU B OE2 1 
ATOM   2085  N  N   . GLU B  1 133 ? 19.043  105.055 51.285  1.00 26.87 ? 133 GLU B N   1 
ATOM   2086  C  CA  . GLU B  1 133 ? 19.766  105.246 50.041  1.00 27.55 ? 133 GLU B CA  1 
ATOM   2087  C  C   . GLU B  1 133 ? 19.416  104.139 49.045  1.00 23.03 ? 133 GLU B C   1 
ATOM   2088  O  O   . GLU B  1 133 ? 19.336  104.392 47.848  1.00 20.58 ? 133 GLU B O   1 
ATOM   2089  C  CB  . GLU B  1 133 ? 21.270  105.309 50.308  1.00 25.53 ? 133 GLU B CB  1 
ATOM   2090  C  CG  . GLU B  1 133 ? 22.113  105.792 49.145  1.00 32.54 ? 133 GLU B CG  1 
ATOM   2091  C  CD  . GLU B  1 133 ? 21.883  107.259 48.799  1.00 38.19 ? 133 GLU B CD  1 
ATOM   2092  O  OE1 . GLU B  1 133 ? 21.424  108.033 49.674  1.00 39.47 ? 133 GLU B OE1 1 
ATOM   2093  O  OE2 . GLU B  1 133 ? 22.164  107.631 47.637  1.00 36.92 ? 133 GLU B OE2 1 
ATOM   2094  N  N   . SER B  1 134 ? 19.200  102.920 49.547  1.00 20.14 ? 134 SER B N   1 
ATOM   2095  C  CA  . SER B  1 134 ? 18.843  101.780 48.695  1.00 19.02 ? 134 SER B CA  1 
ATOM   2096  C  C   . SER B  1 134 ? 17.608  102.054 47.823  1.00 16.25 ? 134 SER B C   1 
ATOM   2097  O  O   . SER B  1 134 ? 17.555  101.658 46.651  1.00 13.33 ? 134 SER B O   1 
ATOM   2098  C  CB  . SER B  1 134 ? 18.599  100.532 49.547  1.00 15.77 ? 134 SER B CB  1 
ATOM   2099  O  OG  . SER B  1 134 ? 18.383  99.392  48.734  1.00 15.86 ? 134 SER B OG  1 
ATOM   2100  N  N   . THR B  1 135 ? 16.624  102.744 48.395  1.00 16.08 ? 135 THR B N   1 
ATOM   2101  C  CA  . THR B  1 135 ? 15.374  103.017 47.677  1.00 17.03 ? 135 THR B CA  1 
ATOM   2102  C  C   . THR B  1 135 ? 15.446  104.315 46.908  1.00 16.47 ? 135 THR B C   1 
ATOM   2103  O  O   . THR B  1 135 ? 14.472  104.714 46.279  1.00 18.71 ? 135 THR B O   1 
ATOM   2104  C  CB  . THR B  1 135 ? 14.160  103.073 48.614  1.00 23.09 ? 135 THR B CB  1 
ATOM   2105  O  OG1 . THR B  1 135 ? 14.482  103.889 49.748  1.00 22.06 ? 135 THR B OG1 1 
ATOM   2106  C  CG2 . THR B  1 135 ? 13.800  101.680 49.075  1.00 17.10 ? 135 THR B CG2 1 
ATOM   2107  N  N   . LYS B  1 136 ? 16.612  104.957 46.955  1.00 17.98 ? 136 LYS B N   1 
ATOM   2108  C  CA  . LYS B  1 136 ? 16.885  106.146 46.163  1.00 20.71 ? 136 LYS B CA  1 
ATOM   2109  C  C   . LYS B  1 136 ? 17.814  105.853 44.975  1.00 19.00 ? 136 LYS B C   1 
ATOM   2110  O  O   . LYS B  1 136 ? 17.462  106.124 43.819  1.00 15.23 ? 136 LYS B O   1 
ATOM   2111  C  CB  . LYS B  1 136 ? 17.493  107.239 47.034  1.00 26.26 ? 136 LYS B CB  1 
ATOM   2112  C  CG  . LYS B  1 136 ? 16.499  107.876 47.981  1.00 30.74 ? 136 LYS B CG  1 
ATOM   2113  C  CD  . LYS B  1 136 ? 17.147  108.943 48.858  1.00 41.16 ? 136 LYS B CD  1 
ATOM   2114  C  CE  . LYS B  1 136 ? 16.073  109.752 49.591  1.00 41.09 ? 136 LYS B CE  1 
ATOM   2115  N  NZ  . LYS B  1 136 ? 15.031  110.273 48.647  1.00 37.67 ? 136 LYS B NZ  1 
ATOM   2116  N  N   . THR B  1 137 ? 18.984  105.294 45.263  1.00 15.77 ? 137 THR B N   1 
ATOM   2117  C  CA  . THR B  1 137 ? 20.009  105.114 44.241  1.00 16.10 ? 137 THR B CA  1 
ATOM   2118  C  C   . THR B  1 137 ? 20.465  103.674 44.127  1.00 17.39 ? 137 THR B C   1 
ATOM   2119  O  O   . THR B  1 137 ? 21.244  103.344 43.249  1.00 17.47 ? 137 THR B O   1 
ATOM   2120  C  CB  . THR B  1 137 ? 21.274  105.928 44.573  1.00 20.69 ? 137 THR B CB  1 
ATOM   2121  O  OG1 . THR B  1 137 ? 21.843  105.421 45.782  1.00 19.63 ? 137 THR B OG1 1 
ATOM   2122  C  CG2 . THR B  1 137 ? 20.940  107.405 44.765  1.00 19.53 ? 137 THR B CG2 1 
ATOM   2123  N  N   . GLY B  1 138 ? 20.040  102.812 45.042  1.00 15.38 ? 138 GLY B N   1 
ATOM   2124  C  CA  . GLY B  1 138 ? 20.511  101.441 44.992  1.00 13.27 ? 138 GLY B CA  1 
ATOM   2125  C  C   . GLY B  1 138 ? 21.962  101.276 45.450  1.00 15.04 ? 138 GLY B C   1 
ATOM   2126  O  O   . GLY B  1 138 ? 22.557  100.202 45.286  1.00 14.80 ? 138 GLY B O   1 
ATOM   2127  N  N   . ASN B  1 139 ? 22.533  102.328 46.027  1.00 13.61 ? 139 ASN B N   1 
ATOM   2128  C  CA  . ASN B  1 139 ? 23.884  102.250 46.578  1.00 17.33 ? 139 ASN B CA  1 
ATOM   2129  C  C   . ASN B  1 139 ? 24.962  101.808 45.595  1.00 14.17 ? 139 ASN B C   1 
ATOM   2130  O  O   . ASN B  1 139 ? 25.900  101.136 46.015  1.00 17.60 ? 139 ASN B O   1 
ATOM   2131  C  CB  . ASN B  1 139 ? 23.911  101.316 47.800  1.00 15.15 ? 139 ASN B CB  1 
ATOM   2132  C  CG  . ASN B  1 139 ? 23.079  101.847 48.949  1.00 22.07 ? 139 ASN B CG  1 
ATOM   2133  O  OD1 . ASN B  1 139 ? 23.310  102.952 49.439  1.00 27.07 ? 139 ASN B OD1 1 
ATOM   2134  N  ND2 . ASN B  1 139 ? 22.074  101.083 49.353  1.00 20.13 ? 139 ASN B ND2 1 
ATOM   2135  N  N   . ALA B  1 140 ? 24.851  102.194 44.315  1.00 11.03 ? 140 ALA B N   1 
ATOM   2136  C  CA  . ALA B  1 140 ? 25.822  101.776 43.287  1.00 14.17 ? 140 ALA B CA  1 
ATOM   2137  C  C   . ALA B  1 140 ? 27.104  102.613 43.221  1.00 13.14 ? 140 ALA B C   1 
ATOM   2138  O  O   . ALA B  1 140 ? 27.911  102.457 42.302  1.00 15.79 ? 140 ALA B O   1 
ATOM   2139  C  CB  . ALA B  1 140 ? 25.178  101.701 41.912  1.00 10.62 ? 140 ALA B CB  1 
ATOM   2140  N  N   . GLY B  1 141 ? 27.295  103.499 44.184  1.00 13.39 ? 141 GLY B N   1 
ATOM   2141  C  CA  . GLY B  1 141 ? 28.491  104.319 44.231  1.00 13.42 ? 141 GLY B CA  1 
ATOM   2142  C  C   . GLY B  1 141 ? 28.607  105.351 43.129  1.00 18.00 ? 141 GLY B C   1 
ATOM   2143  O  O   . GLY B  1 141 ? 27.615  105.817 42.562  1.00 15.83 ? 141 GLY B O   1 
ATOM   2144  N  N   . SER B  1 142 ? 29.844  105.686 42.794  1.00 14.70 ? 142 SER B N   1 
ATOM   2145  C  CA  . SER B  1 142 ? 30.125  106.816 41.934  1.00 12.79 ? 142 SER B CA  1 
ATOM   2146  C  C   . SER B  1 142 ? 29.748  106.573 40.466  1.00 13.17 ? 142 SER B C   1 
ATOM   2147  O  O   . SER B  1 142 ? 29.575  105.433 40.018  1.00 12.48 ? 142 SER B O   1 
ATOM   2148  C  CB  . SER B  1 142 ? 31.621  107.176 42.047  1.00 13.74 ? 142 SER B CB  1 
ATOM   2149  O  OG  . SER B  1 142 ? 32.401  106.257 41.296  1.00 16.50 ? 142 SER B OG  1 
ATOM   2150  N  N   . ARG B  1 143 ? 29.625  107.664 39.723  1.00 13.83 ? 143 ARG B N   1 
ATOM   2151  C  CA  . ARG B  1 143 ? 29.314  107.615 38.301  1.00 16.34 ? 143 ARG B CA  1 
ATOM   2152  C  C   . ARG B  1 143 ? 30.626  107.548 37.536  1.00 13.92 ? 143 ARG B C   1 
ATOM   2153  O  O   . ARG B  1 143 ? 31.315  108.545 37.419  1.00 14.39 ? 143 ARG B O   1 
ATOM   2154  C  CB  . ARG B  1 143 ? 28.537  108.881 37.912  1.00 16.28 ? 143 ARG B CB  1 
ATOM   2155  C  CG  . ARG B  1 143 ? 27.338  109.105 38.818  1.00 15.18 ? 143 ARG B CG  1 
ATOM   2156  C  CD  . ARG B  1 143 ? 26.517  110.362 38.545  1.00 17.06 ? 143 ARG B CD  1 
ATOM   2157  N  NE  . ARG B  1 143 ? 25.441  110.451 39.533  1.00 20.86 ? 143 ARG B NE  1 
ATOM   2158  C  CZ  . ARG B  1 143 ? 24.411  111.296 39.480  1.00 20.28 ? 143 ARG B CZ  1 
ATOM   2159  N  NH1 . ARG B  1 143 ? 24.299  112.147 38.470  1.00 18.60 ? 143 ARG B NH1 1 
ATOM   2160  N  NH2 . ARG B  1 143 ? 23.488  111.282 40.437  1.00 12.89 ? 143 ARG B NH2 1 
ATOM   2161  N  N   . LEU B  1 144 ? 30.979  106.372 37.029  1.00 13.57 ? 144 LEU B N   1 
ATOM   2162  C  CA  . LEU B  1 144 ? 32.268  106.183 36.358  1.00 10.54 ? 144 LEU B CA  1 
ATOM   2163  C  C   . LEU B  1 144 ? 32.299  106.681 34.914  1.00 12.57 ? 144 LEU B C   1 
ATOM   2164  O  O   . LEU B  1 144 ? 33.343  107.101 34.418  1.00 9.18  ? 144 LEU B O   1 
ATOM   2165  C  CB  . LEU B  1 144 ? 32.665  104.708 36.389  1.00 10.52 ? 144 LEU B CB  1 
ATOM   2166  C  CG  . LEU B  1 144 ? 32.945  104.101 37.775  1.00 12.41 ? 144 LEU B CG  1 
ATOM   2167  C  CD1 . LEU B  1 144 ? 33.632  102.766 37.627  1.00 11.85 ? 144 LEU B CD1 1 
ATOM   2168  C  CD2 . LEU B  1 144 ? 33.789  105.009 38.625  1.00 12.56 ? 144 LEU B CD2 1 
ATOM   2169  N  N   . ALA B  1 145 ? 31.177  106.585 34.211  1.00 8.11  ? 145 ALA B N   1 
ATOM   2170  C  CA  . ALA B  1 145 ? 31.115  107.110 32.861  1.00 7.62  ? 145 ALA B CA  1 
ATOM   2171  C  C   . ALA B  1 145 ? 29.679  107.419 32.526  1.00 9.64  ? 145 ALA B C   1 
ATOM   2172  O  O   . ALA B  1 145 ? 28.760  106.852 33.137  1.00 9.45  ? 145 ALA B O   1 
ATOM   2173  C  CB  . ALA B  1 145 ? 31.672  106.112 31.859  1.00 7.44  ? 145 ALA B CB  1 
ATOM   2174  N  N   . CYS B  1 146 ? 29.488  108.294 31.544  1.00 8.17  ? 146 CYS B N   1 
ATOM   2175  C  CA  . CYS B  1 146 ? 28.155  108.716 31.148  1.00 9.92  ? 146 CYS B CA  1 
ATOM   2176  C  C   . CYS B  1 146 ? 28.169  109.328 29.757  1.00 10.49 ? 146 CYS B C   1 
ATOM   2177  O  O   . CYS B  1 146 ? 29.241  109.608 29.195  1.00 8.80  ? 146 CYS B O   1 
ATOM   2178  C  CB  . CYS B  1 146 ? 27.614  109.725 32.155  1.00 9.62  ? 146 CYS B CB  1 
ATOM   2179  S  SG  . CYS B  1 146 ? 28.317  111.360 31.966  1.00 18.87 ? 146 CYS B SG  1 
ATOM   2180  N  N   . GLY B  1 147 ? 26.979  109.507 29.194  1.00 7.66  ? 147 GLY B N   1 
ATOM   2181  C  CA  . GLY B  1 147 ? 26.809  110.208 27.931  1.00 9.20  ? 147 GLY B CA  1 
ATOM   2182  C  C   . GLY B  1 147 ? 25.327  110.474 27.661  1.00 10.47 ? 147 GLY B C   1 
ATOM   2183  O  O   . GLY B  1 147 ? 24.469  109.839 28.265  1.00 7.69  ? 147 GLY B O   1 
ATOM   2184  N  N   . VAL B  1 148 ? 25.033  111.434 26.786  1.00 8.09  ? 148 VAL B N   1 
ATOM   2185  C  CA  . VAL B  1 148 ? 23.662  111.781 26.464  1.00 8.34  ? 148 VAL B CA  1 
ATOM   2186  C  C   . VAL B  1 148 ? 23.144  110.795 25.417  1.00 8.18  ? 148 VAL B C   1 
ATOM   2187  O  O   . VAL B  1 148 ? 23.864  110.423 24.495  1.00 8.36  ? 148 VAL B O   1 
ATOM   2188  C  CB  . VAL B  1 148 ? 23.568  113.217 25.929  1.00 11.09 ? 148 VAL B CB  1 
ATOM   2189  C  CG1 . VAL B  1 148 ? 22.134  113.589 25.648  1.00 7.22  ? 148 VAL B CG1 1 
ATOM   2190  C  CG2 . VAL B  1 148 ? 24.205  114.189 26.930  1.00 9.89  ? 148 VAL B CG2 1 
ATOM   2191  N  N   . ILE B  1 149 ? 21.913  110.335 25.589  1.00 6.89  ? 149 ILE B N   1 
ATOM   2192  C  CA  . ILE B  1 149 ? 21.325  109.366 24.666  1.00 8.25  ? 149 ILE B CA  1 
ATOM   2193  C  C   . ILE B  1 149 ? 20.801  110.119 23.442  1.00 10.79 ? 149 ILE B C   1 
ATOM   2194  O  O   . ILE B  1 149 ? 19.967  111.025 23.573  1.00 9.92  ? 149 ILE B O   1 
ATOM   2195  C  CB  . ILE B  1 149 ? 20.212  108.564 25.381  1.00 8.50  ? 149 ILE B CB  1 
ATOM   2196  C  CG1 . ILE B  1 149 ? 20.819  107.738 26.533  1.00 6.80  ? 149 ILE B CG1 1 
ATOM   2197  C  CG2 . ILE B  1 149 ? 19.428  107.684 24.424  1.00 7.28  ? 149 ILE B CG2 1 
ATOM   2198  C  CD1 . ILE B  1 149 ? 19.742  107.292 27.551  1.00 8.24  ? 149 ILE B CD1 1 
ATOM   2199  N  N   . GLY B  1 150 ? 21.329  109.778 22.267  1.00 8.38  ? 150 GLY B N   1 
ATOM   2200  C  CA  . GLY B  1 150 ? 21.049  110.532 21.052  1.00 9.02  ? 150 GLY B CA  1 
ATOM   2201  C  C   . GLY B  1 150 ? 20.306  109.706 20.025  1.00 10.52 ? 150 GLY B C   1 
ATOM   2202  O  O   . GLY B  1 150 ? 20.381  108.476 20.058  1.00 10.65 ? 150 GLY B O   1 
ATOM   2203  N  N   . ILE B  1 151 ? 19.560  110.366 19.143  1.00 9.53  ? 151 ILE B N   1 
ATOM   2204  C  CA  . ILE B  1 151 ? 18.831  109.665 18.080  1.00 10.41 ? 151 ILE B CA  1 
ATOM   2205  C  C   . ILE B  1 151 ? 19.836  109.129 17.084  1.00 11.07 ? 151 ILE B C   1 
ATOM   2206  O  O   . ILE B  1 151 ? 20.787  109.818 16.727  1.00 12.08 ? 151 ILE B O   1 
ATOM   2207  C  CB  . ILE B  1 151 ? 17.861  110.615 17.356  1.00 11.41 ? 151 ILE B CB  1 
ATOM   2208  C  CG1 . ILE B  1 151 ? 16.825  111.154 18.335  1.00 12.38 ? 151 ILE B CG1 1 
ATOM   2209  C  CG2 . ILE B  1 151 ? 17.192  109.925 16.171  1.00 12.71 ? 151 ILE B CG2 1 
ATOM   2210  C  CD1 . ILE B  1 151 ? 15.977  112.336 17.771  1.00 14.59 ? 151 ILE B CD1 1 
ATOM   2211  N  N   . ALA B  1 152 ? 19.636  107.891 16.655  1.00 12.85 ? 152 ALA B N   1 
ATOM   2212  C  CA  . ALA B  1 152 ? 20.573  107.193 15.782  1.00 15.09 ? 152 ALA B CA  1 
ATOM   2213  C  C   . ALA B  1 152 ? 19.934  106.881 14.412  1.00 16.91 ? 152 ALA B C   1 
ATOM   2214  O  O   . ALA B  1 152 ? 18.719  106.807 14.281  1.00 16.72 ? 152 ALA B O   1 
ATOM   2215  C  CB  . ALA B  1 152 ? 21.041  105.890 16.464  1.00 8.82  ? 152 ALA B CB  1 
ATOM   2216  N  N   . GLN B  1 153 ? 20.751  106.686 13.392  1.00 20.55 ? 153 GLN B N   1 
ATOM   2217  C  CA  . GLN B  1 153 ? 20.205  106.396 12.065  1.00 26.58 ? 153 GLN B CA  1 
ATOM   2218  C  C   . GLN B  1 153 ? 19.568  105.012 11.989  1.00 30.65 ? 153 GLN B C   1 
ATOM   2219  O  O   . GLN B  1 153 ? 20.195  104.024 12.391  1.00 33.02 ? 153 GLN B O   1 
ATOM   2220  C  CB  . GLN B  1 153 ? 21.278  106.508 10.993  1.00 23.20 ? 153 GLN B CB  1 
ATOM   2221  C  CG  . GLN B  1 153 ? 20.726  106.297 9.597   1.00 24.00 ? 153 GLN B CG  1 
ATOM   2222  C  CD  . GLN B  1 153 ? 21.653  106.830 8.533   1.00 28.94 ? 153 GLN B CD  1 
ATOM   2223  O  OE1 . GLN B  1 153 ? 21.210  107.417 7.544   1.00 34.01 ? 153 GLN B OE1 1 
ATOM   2224  N  NE2 . GLN B  1 153 ? 22.952  106.640 8.734   1.00 26.31 ? 153 GLN B NE2 1 
ATOM   2225  O  OXT . GLN B  1 153 ? 18.434  104.855 11.516  1.00 29.16 ? 153 GLN B OXT 1 
ATOM   2226  N  N   . THR C  1 2   ? -0.022  82.269  78.569  1.00 37.13 ? 2   THR C N   1 
ATOM   2227  C  CA  . THR C  1 2   ? 1.235   82.803  78.057  1.00 36.20 ? 2   THR C CA  1 
ATOM   2228  C  C   . THR C  1 2   ? 2.291   82.958  79.155  1.00 39.34 ? 2   THR C C   1 
ATOM   2229  O  O   . THR C  1 2   ? 1.992   82.861  80.349  1.00 40.70 ? 2   THR C O   1 
ATOM   2230  C  CB  . THR C  1 2   ? 1.036   84.162  77.334  1.00 36.40 ? 2   THR C CB  1 
ATOM   2231  O  OG1 . THR C  1 2   ? 0.147   84.996  78.084  1.00 34.00 ? 2   THR C OG1 1 
ATOM   2232  C  CG2 . THR C  1 2   ? 0.464   83.962  75.934  1.00 44.87 ? 2   THR C CG2 1 
ATOM   2233  N  N   . LYS C  1 3   ? 3.532   83.188  78.741  1.00 31.40 ? 3   LYS C N   1 
ATOM   2234  C  CA  . LYS C  1 3   ? 4.639   83.386  79.670  1.00 31.24 ? 3   LYS C CA  1 
ATOM   2235  C  C   . LYS C  1 3   ? 5.460   84.603  79.272  1.00 34.35 ? 3   LYS C C   1 
ATOM   2236  O  O   . LYS C  1 3   ? 5.574   84.938  78.091  1.00 30.94 ? 3   LYS C O   1 
ATOM   2237  C  CB  . LYS C  1 3   ? 5.546   82.159  79.681  1.00 31.87 ? 3   LYS C CB  1 
ATOM   2238  C  CG  . LYS C  1 3   ? 4.925   80.937  80.324  1.00 38.50 ? 3   LYS C CG  1 
ATOM   2239  C  CD  . LYS C  1 3   ? 5.914   79.783  80.398  1.00 38.93 ? 3   LYS C CD  1 
ATOM   2240  C  CE  . LYS C  1 3   ? 5.310   78.595  81.146  1.00 49.60 ? 3   LYS C CE  1 
ATOM   2241  N  NZ  . LYS C  1 3   ? 6.205   77.400  81.180  1.00 54.54 ? 3   LYS C NZ  1 
ATOM   2242  N  N   . ALA C  1 4   ? 6.042   85.272  80.254  1.00 36.72 ? 4   ALA C N   1 
ATOM   2243  C  CA  . ALA C  1 4   ? 6.974   86.349  79.958  1.00 29.06 ? 4   ALA C CA  1 
ATOM   2244  C  C   . ALA C  1 4   ? 8.218   86.236  80.837  1.00 35.24 ? 4   ALA C C   1 
ATOM   2245  O  O   . ALA C  1 4   ? 8.289   85.393  81.747  1.00 34.23 ? 4   ALA C O   1 
ATOM   2246  C  CB  . ALA C  1 4   ? 6.314   87.705  80.119  1.00 23.52 ? 4   ALA C CB  1 
ATOM   2247  N  N   . VAL C  1 5   ? 9.193   87.090  80.548  1.00 27.82 ? 5   VAL C N   1 
ATOM   2248  C  CA  . VAL C  1 5   ? 10.490  87.026  81.186  1.00 30.40 ? 5   VAL C CA  1 
ATOM   2249  C  C   . VAL C  1 5   ? 11.130  88.409  81.107  1.00 33.57 ? 5   VAL C C   1 
ATOM   2250  O  O   . VAL C  1 5   ? 10.739  89.244  80.287  1.00 32.73 ? 5   VAL C O   1 
ATOM   2251  C  CB  . VAL C  1 5   ? 11.369  85.990  80.491  1.00 30.76 ? 5   VAL C CB  1 
ATOM   2252  C  CG1 . VAL C  1 5   ? 11.969  86.577  79.231  1.00 28.76 ? 5   VAL C CG1 1 
ATOM   2253  C  CG2 . VAL C  1 5   ? 12.457  85.501  81.437  1.00 34.55 ? 5   VAL C CG2 1 
ATOM   2254  N  N   . CYS C  1 6   ? 12.102  88.669  81.968  1.00 38.10 ? 6   CYS C N   1 
ATOM   2255  C  CA  . CYS C  1 6   ? 12.688  90.001  82.027  1.00 34.14 ? 6   CYS C CA  1 
ATOM   2256  C  C   . CYS C  1 6   ? 14.031  89.999  82.720  1.00 37.32 ? 6   CYS C C   1 
ATOM   2257  O  O   . CYS C  1 6   ? 14.147  89.593  83.873  1.00 36.86 ? 6   CYS C O   1 
ATOM   2258  C  CB  . CYS C  1 6   ? 11.751  90.981  82.727  1.00 28.22 ? 6   CYS C CB  1 
ATOM   2259  S  SG  . CYS C  1 6   ? 12.388  92.668  82.764  1.00 34.73 ? 6   CYS C SG  1 
ATOM   2260  N  N   . VAL C  1 7   ? 15.047  90.443  81.993  1.00 39.83 ? 7   VAL C N   1 
ATOM   2261  C  CA  . VAL C  1 7   ? 16.378  90.585  82.534  1.00 38.57 ? 7   VAL C CA  1 
ATOM   2262  C  C   . VAL C  1 7   ? 16.508  92.009  83.043  1.00 41.93 ? 7   VAL C C   1 
ATOM   2263  O  O   . VAL C  1 7   ? 16.228  92.959  82.315  1.00 38.78 ? 7   VAL C O   1 
ATOM   2264  C  CB  . VAL C  1 7   ? 17.441  90.328  81.461  1.00 44.69 ? 7   VAL C CB  1 
ATOM   2265  C  CG1 . VAL C  1 7   ? 18.830  90.628  82.011  1.00 47.94 ? 7   VAL C CG1 1 
ATOM   2266  C  CG2 . VAL C  1 7   ? 17.352  88.889  80.958  1.00 42.06 ? 7   VAL C CG2 1 
ATOM   2267  N  N   . LEU C  1 8   ? 16.909  92.151  84.305  1.00 46.71 ? 8   LEU C N   1 
ATOM   2268  C  CA  . LEU C  1 8   ? 17.074  93.466  84.915  1.00 45.29 ? 8   LEU C CA  1 
ATOM   2269  C  C   . LEU C  1 8   ? 18.544  93.873  84.923  1.00 48.89 ? 8   LEU C C   1 
ATOM   2270  O  O   . LEU C  1 8   ? 19.421  93.066  85.235  1.00 50.31 ? 8   LEU C O   1 
ATOM   2271  C  CB  . LEU C  1 8   ? 16.510  93.465  86.334  1.00 44.94 ? 8   LEU C CB  1 
ATOM   2272  C  CG  . LEU C  1 8   ? 14.993  93.355  86.435  1.00 41.58 ? 8   LEU C CG  1 
ATOM   2273  C  CD1 . LEU C  1 8   ? 14.591  93.061  87.857  1.00 44.72 ? 8   LEU C CD1 1 
ATOM   2274  C  CD2 . LEU C  1 8   ? 14.350  94.639  85.972  1.00 40.07 ? 8   LEU C CD2 1 
ATOM   2275  N  N   . LYS C  1 9   ? 18.809  95.126  84.572  1.00 47.32 ? 9   LYS C N   1 
ATOM   2276  C  CA  . LYS C  1 9   ? 20.178  95.605  84.445  1.00 47.13 ? 9   LYS C CA  1 
ATOM   2277  C  C   . LYS C  1 9   ? 20.223  97.095  84.685  1.00 52.55 ? 9   LYS C C   1 
ATOM   2278  O  O   . LYS C  1 9   ? 19.244  97.806  84.442  1.00 51.02 ? 9   LYS C O   1 
ATOM   2279  C  CB  . LYS C  1 9   ? 20.734  95.295  83.052  1.00 48.68 ? 9   LYS C CB  1 
ATOM   2280  C  CG  . LYS C  1 9   ? 21.260  93.875  82.892  1.00 51.49 ? 9   LYS C CG  1 
ATOM   2281  C  CD  . LYS C  1 9   ? 21.526  93.529  81.433  1.00 59.98 ? 9   LYS C CD  1 
ATOM   2282  C  CE  . LYS C  1 9   ? 22.058  92.103  81.287  1.00 59.58 ? 9   LYS C CE  1 
ATOM   2283  N  NZ  . LYS C  1 9   ? 22.201  91.694  79.857  1.00 63.27 ? 9   LYS C NZ  1 
ATOM   2284  N  N   . GLY C  1 10  ? 21.364  97.570  85.165  1.00 53.26 ? 10  GLY C N   1 
ATOM   2285  C  CA  . GLY C  1 10  ? 21.552  98.990  85.379  1.00 53.48 ? 10  GLY C CA  1 
ATOM   2286  C  C   . GLY C  1 10  ? 23.015  99.368  85.329  1.00 53.35 ? 10  GLY C C   1 
ATOM   2287  O  O   . GLY C  1 10  ? 23.867  98.575  84.929  1.00 53.86 ? 10  GLY C O   1 
ATOM   2288  N  N   . ASP C  1 11  ? 23.312  100.593 85.735  1.00 57.36 ? 11  ASP C N   1 
ATOM   2289  C  CA  . ASP C  1 11  ? 24.693  101.036 85.804  1.00 57.63 ? 11  ASP C CA  1 
ATOM   2290  C  C   . ASP C  1 11  ? 25.350  100.416 87.027  1.00 57.69 ? 11  ASP C C   1 
ATOM   2291  O  O   . ASP C  1 11  ? 26.521  100.038 86.995  1.00 63.70 ? 11  ASP C O   1 
ATOM   2292  C  CB  . ASP C  1 11  ? 24.748  102.561 85.847  1.00 60.23 ? 11  ASP C CB  1 
ATOM   2293  C  CG  . ASP C  1 11  ? 24.179  103.190 84.587  1.00 65.73 ? 11  ASP C CG  1 
ATOM   2294  O  OD1 . ASP C  1 11  ? 24.537  102.709 83.487  1.00 62.22 ? 11  ASP C OD1 1 
ATOM   2295  O  OD2 . ASP C  1 11  ? 23.363  104.138 84.691  1.00 61.38 ? 11  ASP C OD2 1 
ATOM   2296  N  N   . GLY C  1 12  ? 24.568  100.273 88.091  1.00 55.05 ? 12  GLY C N   1 
ATOM   2297  C  CA  . GLY C  1 12  ? 25.062  99.751  89.349  1.00 54.76 ? 12  GLY C CA  1 
ATOM   2298  C  C   . GLY C  1 12  ? 25.208  98.245  89.366  1.00 55.61 ? 12  GLY C C   1 
ATOM   2299  O  O   . GLY C  1 12  ? 25.284  97.611  88.309  1.00 56.36 ? 12  GLY C O   1 
ATOM   2300  N  N   . PRO C  1 13  ? 25.240  97.662  90.577  1.00 56.84 ? 13  PRO C N   1 
ATOM   2301  C  CA  . PRO C  1 13  ? 25.479  96.233  90.801  1.00 57.95 ? 13  PRO C CA  1 
ATOM   2302  C  C   . PRO C  1 13  ? 24.188  95.427  90.700  1.00 54.83 ? 13  PRO C C   1 
ATOM   2303  O  O   . PRO C  1 13  ? 24.244  94.209  90.536  1.00 54.64 ? 13  PRO C O   1 
ATOM   2304  C  CB  . PRO C  1 13  ? 25.981  96.206  92.242  1.00 51.41 ? 13  PRO C CB  1 
ATOM   2305  C  CG  . PRO C  1 13  ? 25.179  97.297  92.900  1.00 52.72 ? 13  PRO C CG  1 
ATOM   2306  C  CD  . PRO C  1 13  ? 25.010  98.381  91.847  1.00 53.63 ? 13  PRO C CD  1 
ATOM   2307  N  N   . VAL C  1 14  ? 23.048  96.110  90.799  1.00 50.79 ? 14  VAL C N   1 
ATOM   2308  C  CA  . VAL C  1 14  ? 21.740  95.470  90.769  1.00 50.02 ? 14  VAL C CA  1 
ATOM   2309  C  C   . VAL C  1 14  ? 21.473  94.789  89.431  1.00 56.33 ? 14  VAL C C   1 
ATOM   2310  O  O   . VAL C  1 14  ? 21.543  95.422  88.367  1.00 52.86 ? 14  VAL C O   1 
ATOM   2311  C  CB  . VAL C  1 14  ? 20.614  96.483  91.030  1.00 49.68 ? 14  VAL C CB  1 
ATOM   2312  C  CG1 . VAL C  1 14  ? 19.279  95.772  91.101  1.00 47.06 ? 14  VAL C CG1 1 
ATOM   2313  C  CG2 . VAL C  1 14  ? 20.875  97.246  92.316  1.00 53.54 ? 14  VAL C CG2 1 
ATOM   2314  N  N   . GLN C  1 15  ? 21.169  93.495  89.494  1.00 51.46 ? 15  GLN C N   1 
ATOM   2315  C  CA  . GLN C  1 15  ? 20.827  92.727  88.306  1.00 52.95 ? 15  GLN C CA  1 
ATOM   2316  C  C   . GLN C  1 15  ? 20.085  91.452  88.674  1.00 56.75 ? 15  GLN C C   1 
ATOM   2317  O  O   . GLN C  1 15  ? 20.232  90.929  89.788  1.00 52.47 ? 15  GLN C O   1 
ATOM   2318  C  CB  . GLN C  1 15  ? 22.075  92.377  87.515  1.00 50.11 ? 15  GLN C CB  1 
ATOM   2319  C  CG  . GLN C  1 15  ? 22.960  91.386  88.203  1.00 50.39 ? 15  GLN C CG  1 
ATOM   2320  C  CD  . GLN C  1 15  ? 24.009  90.838  87.269  1.00 61.70 ? 15  GLN C CD  1 
ATOM   2321  O  OE1 . GLN C  1 15  ? 23.915  89.694  86.821  1.00 65.77 ? 15  GLN C OE1 1 
ATOM   2322  N  NE2 . GLN C  1 15  ? 25.011  91.655  86.953  1.00 56.30 ? 15  GLN C NE2 1 
ATOM   2323  N  N   . GLY C  1 16  ? 19.290  90.954  87.730  1.00 53.61 ? 16  GLY C N   1 
ATOM   2324  C  CA  . GLY C  1 16  ? 18.466  89.785  87.971  1.00 50.05 ? 16  GLY C CA  1 
ATOM   2325  C  C   . GLY C  1 16  ? 17.450  89.481  86.884  1.00 45.30 ? 16  GLY C C   1 
ATOM   2326  O  O   . GLY C  1 16  ? 17.322  90.214  85.901  1.00 43.40 ? 16  GLY C O   1 
ATOM   2327  N  N   . ILE C  1 17  ? 16.726  88.387  87.092  1.00 44.33 ? 17  ILE C N   1 
ATOM   2328  C  CA  . ILE C  1 17  ? 15.780  87.846  86.135  1.00 42.91 ? 17  ILE C CA  1 
ATOM   2329  C  C   . ILE C  1 17  ? 14.437  87.602  86.798  1.00 45.20 ? 17  ILE C C   1 
ATOM   2330  O  O   . ILE C  1 17  ? 14.351  86.812  87.734  1.00 48.80 ? 17  ILE C O   1 
ATOM   2331  C  CB  . ILE C  1 17  ? 16.256  86.485  85.639  1.00 43.70 ? 17  ILE C CB  1 
ATOM   2332  C  CG1 . ILE C  1 17  ? 17.593  86.615  84.915  1.00 35.98 ? 17  ILE C CG1 1 
ATOM   2333  C  CG2 . ILE C  1 17  ? 15.202  85.845  84.752  1.00 44.69 ? 17  ILE C CG2 1 
ATOM   2334  C  CD1 . ILE C  1 17  ? 18.179  85.268  84.509  1.00 34.92 ? 17  ILE C CD1 1 
ATOM   2335  N  N   . ILE C  1 18  ? 13.392  88.262  86.303  1.00 39.40 ? 18  ILE C N   1 
ATOM   2336  C  CA  . ILE C  1 18  ? 12.032  88.053  86.793  1.00 37.62 ? 18  ILE C CA  1 
ATOM   2337  C  C   . ILE C  1 18  ? 11.209  87.255  85.772  1.00 42.89 ? 18  ILE C C   1 
ATOM   2338  O  O   . ILE C  1 18  ? 11.199  87.583  84.576  1.00 37.84 ? 18  ILE C O   1 
ATOM   2339  C  CB  . ILE C  1 18  ? 11.317  89.407  87.076  1.00 38.79 ? 18  ILE C CB  1 
ATOM   2340  C  CG1 . ILE C  1 18  ? 12.072  90.212  88.133  1.00 44.15 ? 18  ILE C CG1 1 
ATOM   2341  C  CG2 . ILE C  1 18  ? 9.890   89.188  87.514  1.00 34.17 ? 18  ILE C CG2 1 
ATOM   2342  C  CD1 . ILE C  1 18  ? 12.418  89.412  89.373  1.00 41.67 ? 18  ILE C CD1 1 
ATOM   2343  N  N   . ASN C  1 19  ? 10.528  86.208  86.235  1.00 39.64 ? 19  ASN C N   1 
ATOM   2344  C  CA  . ASN C  1 19  ? 9.635   85.443  85.368  1.00 36.24 ? 19  ASN C CA  1 
ATOM   2345  C  C   . ASN C  1 19  ? 8.176   85.836  85.547  1.00 39.24 ? 19  ASN C C   1 
ATOM   2346  O  O   . ASN C  1 19  ? 7.783   86.370  86.590  1.00 37.02 ? 19  ASN C O   1 
ATOM   2347  C  CB  . ASN C  1 19  ? 9.784   83.940  85.588  1.00 38.25 ? 19  ASN C CB  1 
ATOM   2348  C  CG  . ASN C  1 19  ? 11.190  83.450  85.340  1.00 42.03 ? 19  ASN C CG  1 
ATOM   2349  O  OD1 . ASN C  1 19  ? 11.572  83.167  84.206  1.00 44.61 ? 19  ASN C OD1 1 
ATOM   2350  N  ND2 . ASN C  1 19  ? 11.970  83.334  86.408  1.00 43.22 ? 19  ASN C ND2 1 
ATOM   2351  N  N   . PHE C  1 20  ? 7.375   85.577  84.518  1.00 35.89 ? 20  PHE C N   1 
ATOM   2352  C  CA  . PHE C  1 20  ? 5.946   85.826  84.578  1.00 28.50 ? 20  PHE C CA  1 
ATOM   2353  C  C   . PHE C  1 20  ? 5.221   84.654  83.966  1.00 34.81 ? 20  PHE C C   1 
ATOM   2354  O  O   . PHE C  1 20  ? 5.748   83.969  83.084  1.00 37.25 ? 20  PHE C O   1 
ATOM   2355  C  CB  . PHE C  1 20  ? 5.553   87.061  83.792  1.00 28.34 ? 20  PHE C CB  1 
ATOM   2356  C  CG  . PHE C  1 20  ? 6.203   88.322  84.252  1.00 35.75 ? 20  PHE C CG  1 
ATOM   2357  C  CD1 . PHE C  1 20  ? 7.502   88.631  83.875  1.00 32.94 ? 20  PHE C CD1 1 
ATOM   2358  C  CD2 . PHE C  1 20  ? 5.496   89.232  85.012  1.00 33.74 ? 20  PHE C CD2 1 
ATOM   2359  C  CE1 . PHE C  1 20  ? 8.089   89.806  84.269  1.00 33.19 ? 20  PHE C CE1 1 
ATOM   2360  C  CE2 . PHE C  1 20  ? 6.079   90.410  85.406  1.00 34.57 ? 20  PHE C CE2 1 
ATOM   2361  C  CZ  . PHE C  1 20  ? 7.380   90.701  85.033  1.00 30.77 ? 20  PHE C CZ  1 
ATOM   2362  N  N   . GLU C  1 21  ? 3.998   84.438  84.427  1.00 36.76 ? 21  GLU C N   1 
ATOM   2363  C  CA  . GLU C  1 21  ? 3.155   83.396  83.884  1.00 37.78 ? 21  GLU C CA  1 
ATOM   2364  C  C   . GLU C  1 21  ? 1.700   83.633  84.248  1.00 39.60 ? 21  GLU C C   1 
ATOM   2365  O  O   . GLU C  1 21  ? 1.382   84.047  85.374  1.00 39.14 ? 21  GLU C O   1 
ATOM   2366  C  CB  . GLU C  1 21  ? 3.611   82.020  84.351  1.00 37.60 ? 21  GLU C CB  1 
ATOM   2367  C  CG  . GLU C  1 21  ? 2.800   80.892  83.743  1.00 39.06 ? 21  GLU C CG  1 
ATOM   2368  C  CD  . GLU C  1 21  ? 3.231   79.542  84.257  1.00 46.73 ? 21  GLU C CD  1 
ATOM   2369  O  OE1 . GLU C  1 21  ? 4.394   79.427  84.698  1.00 56.68 ? 21  GLU C OE1 1 
ATOM   2370  O  OE2 . GLU C  1 21  ? 2.411   78.599  84.228  1.00 51.51 ? 21  GLU C OE2 1 
ATOM   2371  N  N   . GLN C  1 22  ? 0.825   83.371  83.281  1.00 33.84 ? 22  GLN C N   1 
ATOM   2372  C  CA  . GLN C  1 22  ? -0.597  83.632  83.424  1.00 36.13 ? 22  GLN C CA  1 
ATOM   2373  C  C   . GLN C  1 22  ? -1.366  82.558  82.673  1.00 36.80 ? 22  GLN C C   1 
ATOM   2374  O  O   . GLN C  1 22  ? -1.541  82.647  81.460  1.00 42.27 ? 22  GLN C O   1 
ATOM   2375  C  CB  . GLN C  1 22  ? -0.923  85.014  82.867  1.00 36.09 ? 22  GLN C CB  1 
ATOM   2376  C  CG  . GLN C  1 22  ? -2.368  85.443  83.026  1.00 34.06 ? 22  GLN C CG  1 
ATOM   2377  C  CD  . GLN C  1 22  ? -2.651  86.756  82.311  1.00 36.77 ? 22  GLN C CD  1 
ATOM   2378  O  OE1 . GLN C  1 22  ? -1.898  87.162  81.423  1.00 35.63 ? 22  GLN C OE1 1 
ATOM   2379  N  NE2 . GLN C  1 22  ? -3.725  87.435  82.707  1.00 36.44 ? 22  GLN C NE2 1 
ATOM   2380  N  N   . LYS C  1 23  ? -1.807  81.534  83.393  1.00 39.84 ? 23  LYS C N   1 
ATOM   2381  C  CA  . LYS C  1 23  ? -2.457  80.379  82.772  1.00 42.94 ? 23  LYS C CA  1 
ATOM   2382  C  C   . LYS C  1 23  ? -3.767  80.727  82.048  1.00 39.99 ? 23  LYS C C   1 
ATOM   2383  O  O   . LYS C  1 23  ? -4.065  80.152  81.008  1.00 44.62 ? 23  LYS C O   1 
ATOM   2384  C  CB  . LYS C  1 23  ? -2.702  79.282  83.808  1.00 42.44 ? 23  LYS C CB  1 
ATOM   2385  C  CG  . LYS C  1 23  ? -1.446  78.579  84.285  1.00 44.99 ? 23  LYS C CG  1 
ATOM   2386  C  CD  . LYS C  1 23  ? -1.759  77.595  85.423  1.00 49.11 ? 23  LYS C CD  1 
ATOM   2387  C  CE  . LYS C  1 23  ? -0.492  76.917  85.950  1.00 48.31 ? 23  LYS C CE  1 
ATOM   2388  N  NZ  . LYS C  1 23  ? 0.254   76.179  84.875  1.00 39.30 ? 23  LYS C NZ  1 
ATOM   2389  N  N   . GLU C  1 24  ? -4.539  81.663  82.598  1.00 36.83 ? 24  GLU C N   1 
ATOM   2390  C  CA  . GLU C  1 24  ? -5.790  82.102  81.981  1.00 39.41 ? 24  GLU C CA  1 
ATOM   2391  C  C   . GLU C  1 24  ? -5.738  83.602  81.759  1.00 40.63 ? 24  GLU C C   1 
ATOM   2392  O  O   . GLU C  1 24  ? -5.197  84.336  82.596  1.00 35.29 ? 24  GLU C O   1 
ATOM   2393  C  CB  . GLU C  1 24  ? -6.984  81.774  82.884  1.00 39.78 ? 24  GLU C CB  1 
ATOM   2394  C  CG  . GLU C  1 24  ? -6.906  80.397  83.528  1.00 42.37 ? 24  GLU C CG  1 
ATOM   2395  C  CD  . GLU C  1 24  ? -6.967  79.274  82.514  1.00 43.86 ? 24  GLU C CD  1 
ATOM   2396  O  OE1 . GLU C  1 24  ? -7.963  79.226  81.768  1.00 47.41 ? 24  GLU C OE1 1 
ATOM   2397  O  OE2 . GLU C  1 24  ? -6.032  78.442  82.464  1.00 45.84 ? 24  GLU C OE2 1 
ATOM   2398  N  N   . SER C  1 25  ? -6.313  84.064  80.652  1.00 32.99 ? 25  SER C N   1 
ATOM   2399  C  CA  . SER C  1 25  ? -6.244  85.484  80.299  1.00 37.25 ? 25  SER C CA  1 
ATOM   2400  C  C   . SER C  1 25  ? -6.991  86.408  81.274  1.00 35.73 ? 25  SER C C   1 
ATOM   2401  O  O   . SER C  1 25  ? -6.762  87.628  81.313  1.00 34.43 ? 25  SER C O   1 
ATOM   2402  C  CB  . SER C  1 25  ? -6.736  85.710  78.864  1.00 34.63 ? 25  SER C CB  1 
ATOM   2403  O  OG  . SER C  1 25  ? -8.025  85.157  78.665  1.00 32.32 ? 25  SER C OG  1 
ATOM   2404  N  N   . ASN C  1 26  ? -7.887  85.832  82.061  1.00 37.09 ? 26  ASN C N   1 
ATOM   2405  C  CA  . ASN C  1 26  ? -8.604  86.621  83.055  1.00 37.94 ? 26  ASN C CA  1 
ATOM   2406  C  C   . ASN C  1 26  ? -8.199  86.177  84.451  1.00 37.11 ? 26  ASN C C   1 
ATOM   2407  O  O   . ASN C  1 26  ? -8.929  86.383  85.421  1.00 40.64 ? 26  ASN C O   1 
ATOM   2408  C  CB  . ASN C  1 26  ? -10.115 86.498  82.863  1.00 34.63 ? 26  ASN C CB  1 
ATOM   2409  C  CG  . ASN C  1 26  ? -10.630 85.106  83.171  1.00 33.85 ? 26  ASN C CG  1 
ATOM   2410  O  OD1 . ASN C  1 26  ? -9.964  84.100  82.902  1.00 31.38 ? 26  ASN C OD1 1 
ATOM   2411  N  ND2 . ASN C  1 26  ? -11.827 85.042  83.749  1.00 35.78 ? 26  ASN C ND2 1 
ATOM   2412  N  N   . GLY C  1 27  ? -7.030  85.552  84.532  1.00 33.91 ? 27  GLY C N   1 
ATOM   2413  C  CA  . GLY C  1 27  ? -6.507  85.042  85.783  1.00 38.71 ? 27  GLY C CA  1 
ATOM   2414  C  C   . GLY C  1 27  ? -5.331  85.855  86.302  1.00 41.40 ? 27  GLY C C   1 
ATOM   2415  O  O   . GLY C  1 27  ? -4.878  86.792  85.644  1.00 32.51 ? 27  GLY C O   1 
ATOM   2416  N  N   . PRO C  1 28  ? -4.833  85.504  87.501  1.00 41.65 ? 28  PRO C N   1 
ATOM   2417  C  CA  . PRO C  1 28  ? -3.706  86.222  88.102  1.00 40.51 ? 28  PRO C CA  1 
ATOM   2418  C  C   . PRO C  1 28  ? -2.386  85.850  87.438  1.00 38.52 ? 28  PRO C C   1 
ATOM   2419  O  O   . PRO C  1 28  ? -2.221  84.738  86.926  1.00 35.60 ? 28  PRO C O   1 
ATOM   2420  C  CB  . PRO C  1 28  ? -3.711  85.712  89.541  1.00 43.19 ? 28  PRO C CB  1 
ATOM   2421  C  CG  . PRO C  1 28  ? -4.224  84.324  89.417  1.00 44.30 ? 28  PRO C CG  1 
ATOM   2422  C  CD  . PRO C  1 28  ? -5.287  84.389  88.348  1.00 35.96 ? 28  PRO C CD  1 
ATOM   2423  N  N   . VAL C  1 29  ? -1.445  86.782  87.456  1.00 38.59 ? 29  VAL C N   1 
ATOM   2424  C  CA  . VAL C  1 29  ? -0.112  86.508  86.945  1.00 41.04 ? 29  VAL C CA  1 
ATOM   2425  C  C   . VAL C  1 29  ? 0.803   86.071  88.086  1.00 37.12 ? 29  VAL C C   1 
ATOM   2426  O  O   . VAL C  1 29  ? 0.927   86.775  89.084  1.00 38.62 ? 29  VAL C O   1 
ATOM   2427  C  CB  . VAL C  1 29  ? 0.487   87.765  86.275  1.00 38.59 ? 29  VAL C CB  1 
ATOM   2428  C  CG1 . VAL C  1 29  ? 1.870   87.463  85.709  1.00 33.76 ? 29  VAL C CG1 1 
ATOM   2429  C  CG2 . VAL C  1 29  ? -0.458  88.284  85.193  1.00 35.15 ? 29  VAL C CG2 1 
ATOM   2430  N  N   . LYS C  1 30  ? 1.434   84.912  87.945  1.00 37.98 ? 30  LYS C N   1 
ATOM   2431  C  CA  . LYS C  1 30  ? 2.538   84.555  88.833  1.00 41.21 ? 30  LYS C CA  1 
ATOM   2432  C  C   . LYS C  1 30  ? 3.812   85.287  88.401  1.00 42.03 ? 30  LYS C C   1 
ATOM   2433  O  O   . LYS C  1 30  ? 4.243   85.168  87.252  1.00 39.64 ? 30  LYS C O   1 
ATOM   2434  C  CB  . LYS C  1 30  ? 2.769   83.042  88.841  1.00 37.61 ? 30  LYS C CB  1 
ATOM   2435  C  CG  . LYS C  1 30  ? 1.509   82.243  89.188  1.00 48.44 ? 30  LYS C CG  1 
ATOM   2436  C  CD  . LYS C  1 30  ? 1.791   81.157  90.223  1.00 48.57 ? 30  LYS C CD  1 
ATOM   2437  C  CE  . LYS C  1 30  ? 0.503   80.630  90.855  1.00 48.28 ? 30  LYS C CE  1 
ATOM   2438  N  NZ  . LYS C  1 30  ? -0.252  79.710  89.956  1.00 52.45 ? 30  LYS C NZ  1 
ATOM   2439  N  N   . VAL C  1 31  ? 4.392   86.058  89.320  1.00 35.08 ? 31  VAL C N   1 
ATOM   2440  C  CA  . VAL C  1 31  ? 5.628   86.798  89.075  1.00 37.28 ? 31  VAL C CA  1 
ATOM   2441  C  C   . VAL C  1 31  ? 6.716   86.319  90.029  1.00 42.81 ? 31  VAL C C   1 
ATOM   2442  O  O   . VAL C  1 31  ? 6.557   86.421  91.251  1.00 44.04 ? 31  VAL C O   1 
ATOM   2443  C  CB  . VAL C  1 31  ? 5.433   88.294  89.324  1.00 41.10 ? 31  VAL C CB  1 
ATOM   2444  C  CG1 . VAL C  1 31  ? 6.723   89.039  89.063  1.00 40.91 ? 31  VAL C CG1 1 
ATOM   2445  C  CG2 . VAL C  1 31  ? 4.294   88.849  88.470  1.00 37.08 ? 31  VAL C CG2 1 
ATOM   2446  N  N   . TRP C  1 32  ? 7.819   85.804  89.491  1.00 38.16 ? 32  TRP C N   1 
ATOM   2447  C  CA  . TRP C  1 32  ? 8.839   85.191  90.343  1.00 43.03 ? 32  TRP C CA  1 
ATOM   2448  C  C   . TRP C  1 32  ? 10.261  85.175  89.775  1.00 46.66 ? 32  TRP C C   1 
ATOM   2449  O  O   . TRP C  1 32  ? 10.461  85.052  88.561  1.00 43.72 ? 32  TRP C O   1 
ATOM   2450  C  CB  . TRP C  1 32  ? 8.437   83.759  90.689  1.00 41.91 ? 32  TRP C CB  1 
ATOM   2451  C  CG  . TRP C  1 32  ? 9.037   82.727  89.781  1.00 41.23 ? 32  TRP C CG  1 
ATOM   2452  C  CD1 . TRP C  1 32  ? 10.265  82.130  89.905  1.00 39.80 ? 32  TRP C CD1 1 
ATOM   2453  C  CD2 . TRP C  1 32  ? 8.431   82.160  88.618  1.00 44.90 ? 32  TRP C CD2 1 
ATOM   2454  N  NE1 . TRP C  1 32  ? 10.459  81.234  88.884  1.00 46.68 ? 32  TRP C NE1 1 
ATOM   2455  C  CE2 . TRP C  1 32  ? 9.348   81.231  88.081  1.00 45.30 ? 32  TRP C CE2 1 
ATOM   2456  C  CE3 . TRP C  1 32  ? 7.203   82.348  87.974  1.00 44.98 ? 32  TRP C CE3 1 
ATOM   2457  C  CZ2 . TRP C  1 32  ? 9.072   80.491  86.934  1.00 45.30 ? 32  TRP C CZ2 1 
ATOM   2458  C  CZ3 . TRP C  1 32  ? 6.932   81.615  86.833  1.00 42.20 ? 32  TRP C CZ3 1 
ATOM   2459  C  CH2 . TRP C  1 32  ? 7.863   80.698  86.325  1.00 43.61 ? 32  TRP C CH2 1 
ATOM   2460  N  N   . GLY C  1 33  ? 11.245  85.250  90.671  1.00 43.74 ? 33  GLY C N   1 
ATOM   2461  C  CA  . GLY C  1 33  ? 12.644  85.139  90.294  1.00 43.86 ? 33  GLY C CA  1 
ATOM   2462  C  C   . GLY C  1 33  ? 13.581  85.712  91.338  1.00 53.13 ? 33  GLY C C   1 
ATOM   2463  O  O   . GLY C  1 33  ? 13.212  85.829  92.512  1.00 56.47 ? 33  GLY C O   1 
ATOM   2464  N  N   . SER C  1 34  ? 14.787  86.083  90.910  1.00 53.48 ? 34  SER C N   1 
ATOM   2465  C  CA  . SER C  1 34  ? 15.810  86.596  91.819  1.00 54.32 ? 34  SER C CA  1 
ATOM   2466  C  C   . SER C  1 34  ? 16.430  87.900  91.332  1.00 46.82 ? 34  SER C C   1 
ATOM   2467  O  O   . SER C  1 34  ? 16.848  87.996  90.178  1.00 43.46 ? 34  SER C O   1 
ATOM   2468  C  CB  . SER C  1 34  ? 16.919  85.557  92.002  1.00 50.27 ? 34  SER C CB  1 
ATOM   2469  O  OG  . SER C  1 34  ? 16.375  84.289  92.319  1.00 52.70 ? 34  SER C OG  1 
ATOM   2470  N  N   . ILE C  1 35  ? 16.490  88.888  92.223  1.00 42.10 ? 35  ILE C N   1 
ATOM   2471  C  CA  . ILE C  1 35  ? 17.248  90.119  92.001  1.00 45.11 ? 35  ILE C CA  1 
ATOM   2472  C  C   . ILE C  1 35  ? 18.409  90.229  93.005  1.00 55.27 ? 35  ILE C C   1 
ATOM   2473  O  O   . ILE C  1 35  ? 18.186  90.380  94.213  1.00 49.57 ? 35  ILE C O   1 
ATOM   2474  C  CB  . ILE C  1 35  ? 16.373  91.373  92.192  1.00 39.78 ? 35  ILE C CB  1 
ATOM   2475  C  CG1 . ILE C  1 35  ? 15.145  91.346  91.286  1.00 43.01 ? 35  ILE C CG1 1 
ATOM   2476  C  CG2 . ILE C  1 35  ? 17.183  92.641  91.948  1.00 38.32 ? 35  ILE C CG2 1 
ATOM   2477  C  CD1 . ILE C  1 35  ? 14.314  92.613  91.402  1.00 32.19 ? 35  ILE C CD1 1 
ATOM   2478  N  N   . LYS C  1 36  ? 19.646  90.171  92.522  1.00 51.13 ? 36  LYS C N   1 
ATOM   2479  C  CA  . LYS C  1 36  ? 20.780  90.254  93.432  1.00 51.19 ? 36  LYS C CA  1 
ATOM   2480  C  C   . LYS C  1 36  ? 21.435  91.630  93.452  1.00 51.99 ? 36  LYS C C   1 
ATOM   2481  O  O   . LYS C  1 36  ? 21.169  92.474  92.592  1.00 51.01 ? 36  LYS C O   1 
ATOM   2482  C  CB  . LYS C  1 36  ? 21.809  89.171  93.127  1.00 48.92 ? 36  LYS C CB  1 
ATOM   2483  C  CG  . LYS C  1 36  ? 22.502  89.312  91.798  1.00 49.68 ? 36  LYS C CG  1 
ATOM   2484  C  CD  . LYS C  1 36  ? 23.280  88.040  91.485  1.00 58.44 ? 36  LYS C CD  1 
ATOM   2485  C  CE  . LYS C  1 36  ? 22.445  86.799  91.810  1.00 56.55 ? 36  LYS C CE  1 
ATOM   2486  N  NZ  . LYS C  1 36  ? 23.059  85.539  91.303  1.00 56.28 ? 36  LYS C NZ  1 
ATOM   2487  N  N   . GLY C  1 37  ? 22.273  91.853  94.459  1.00 52.32 ? 37  GLY C N   1 
ATOM   2488  C  CA  . GLY C  1 37  ? 23.015  93.093  94.576  1.00 45.84 ? 37  GLY C CA  1 
ATOM   2489  C  C   . GLY C  1 37  ? 22.198  94.260  95.083  1.00 48.51 ? 37  GLY C C   1 
ATOM   2490  O  O   . GLY C  1 37  ? 22.486  95.408  94.754  1.00 53.88 ? 37  GLY C O   1 
ATOM   2491  N  N   . LEU C  1 38  ? 21.182  93.971  95.891  1.00 52.71 ? 38  LEU C N   1 
ATOM   2492  C  CA  . LEU C  1 38  ? 20.336  95.011  96.468  1.00 54.90 ? 38  LEU C CA  1 
ATOM   2493  C  C   . LEU C  1 38  ? 20.726  95.310  97.911  1.00 59.51 ? 38  LEU C C   1 
ATOM   2494  O  O   . LEU C  1 38  ? 20.993  94.392  98.686  1.00 55.65 ? 38  LEU C O   1 
ATOM   2495  C  CB  . LEU C  1 38  ? 18.872  94.569  96.455  1.00 61.65 ? 38  LEU C CB  1 
ATOM   2496  C  CG  . LEU C  1 38  ? 18.036  94.640  95.176  1.00 58.66 ? 38  LEU C CG  1 
ATOM   2497  C  CD1 . LEU C  1 38  ? 16.680  93.992  95.421  1.00 56.76 ? 38  LEU C CD1 1 
ATOM   2498  C  CD2 . LEU C  1 38  ? 17.864  96.084  94.737  1.00 53.22 ? 38  LEU C CD2 1 
ATOM   2499  N  N   . THR C  1 39  ? 20.733  96.586  98.284  1.00 56.23 ? 39  THR C N   1 
ATOM   2500  C  CA  . THR C  1 39  ? 20.934  96.932  99.682  1.00 58.88 ? 39  THR C CA  1 
ATOM   2501  C  C   . THR C  1 39  ? 19.783  96.353  100.484 1.00 61.81 ? 39  THR C C   1 
ATOM   2502  O  O   . THR C  1 39  ? 18.627  96.503  100.099 1.00 58.87 ? 39  THR C O   1 
ATOM   2503  C  CB  . THR C  1 39  ? 20.978  98.450  99.917  1.00 58.59 ? 39  THR C CB  1 
ATOM   2504  O  OG1 . THR C  1 39  ? 19.750  99.039  99.475  1.00 61.53 ? 39  THR C OG1 1 
ATOM   2505  C  CG2 . THR C  1 39  ? 22.150  99.080  99.177  1.00 60.61 ? 39  THR C CG2 1 
ATOM   2506  N  N   . GLU C  1 40  ? 20.117  95.682  101.585 1.00 63.30 ? 40  GLU C N   1 
ATOM   2507  C  CA  . GLU C  1 40  ? 19.139  95.084  102.491 1.00 59.61 ? 40  GLU C CA  1 
ATOM   2508  C  C   . GLU C  1 40  ? 17.964  96.026  102.746 1.00 58.13 ? 40  GLU C C   1 
ATOM   2509  O  O   . GLU C  1 40  ? 18.136  97.244  102.818 1.00 58.21 ? 40  GLU C O   1 
ATOM   2510  C  CB  . GLU C  1 40  ? 19.818  94.716  103.814 1.00 63.16 ? 40  GLU C CB  1 
ATOM   2511  C  CG  . GLU C  1 40  ? 19.029  93.777  104.718 1.00 63.44 ? 40  GLU C CG  1 
ATOM   2512  C  CD  . GLU C  1 40  ? 19.782  93.435  106.000 1.00 67.19 ? 40  GLU C CD  1 
ATOM   2513  O  OE1 . GLU C  1 40  ? 20.295  94.374  106.647 1.00 57.34 ? 40  GLU C OE1 1 
ATOM   2514  O  OE2 . GLU C  1 40  ? 19.869  92.233  106.357 1.00 63.98 ? 40  GLU C OE2 1 
ATOM   2515  N  N   . GLY C  1 41  ? 16.767  95.462  102.854 1.00 55.52 ? 41  GLY C N   1 
ATOM   2516  C  CA  . GLY C  1 41  ? 15.579  96.262  103.069 1.00 51.00 ? 41  GLY C CA  1 
ATOM   2517  C  C   . GLY C  1 41  ? 14.577  96.134  101.939 1.00 59.65 ? 41  GLY C C   1 
ATOM   2518  O  O   . GLY C  1 41  ? 14.551  95.140  101.208 1.00 58.62 ? 41  GLY C O   1 
ATOM   2519  N  N   . LEU C  1 42  ? 13.744  97.152  101.787 1.00 54.63 ? 42  LEU C N   1 
ATOM   2520  C  CA  . LEU C  1 42  ? 12.647  97.067  100.839 1.00 58.21 ? 42  LEU C CA  1 
ATOM   2521  C  C   . LEU C  1 42  ? 12.830  98.004  99.640  1.00 65.23 ? 42  LEU C C   1 
ATOM   2522  O  O   . LEU C  1 42  ? 13.157  99.183  99.801  1.00 65.34 ? 42  LEU C O   1 
ATOM   2523  C  CB  . LEU C  1 42  ? 11.311  97.307  101.548 1.00 57.28 ? 42  LEU C CB  1 
ATOM   2524  C  CG  . LEU C  1 42  ? 10.595  96.073  102.122 1.00 53.47 ? 42  LEU C CG  1 
ATOM   2525  C  CD1 . LEU C  1 42  ? 11.494  95.227  103.004 1.00 53.45 ? 42  LEU C CD1 1 
ATOM   2526  C  CD2 . LEU C  1 42  ? 9.360   96.498  102.890 1.00 51.69 ? 42  LEU C CD2 1 
ATOM   2527  N  N   . HIS C  1 43  ? 12.634  97.459  98.440  1.00 61.56 ? 43  HIS C N   1 
ATOM   2528  C  CA  . HIS C  1 43  ? 12.820  98.209  97.198  1.00 61.15 ? 43  HIS C CA  1 
ATOM   2529  C  C   . HIS C  1 43  ? 11.530  98.329  96.392  1.00 55.63 ? 43  HIS C C   1 
ATOM   2530  O  O   . HIS C  1 43  ? 10.826  97.341  96.187  1.00 50.58 ? 43  HIS C O   1 
ATOM   2531  C  CB  . HIS C  1 43  ? 13.882  97.539  96.329  1.00 57.88 ? 43  HIS C CB  1 
ATOM   2532  C  CG  . HIS C  1 43  ? 15.188  97.331  97.027  1.00 62.59 ? 43  HIS C CG  1 
ATOM   2533  N  ND1 . HIS C  1 43  ? 16.213  98.252  96.977  1.00 65.78 ? 43  HIS C ND1 1 
ATOM   2534  C  CD2 . HIS C  1 43  ? 15.637  96.308  97.791  1.00 59.07 ? 43  HIS C CD2 1 
ATOM   2535  C  CE1 . HIS C  1 43  ? 17.238  97.805  97.680  1.00 61.86 ? 43  HIS C CE1 1 
ATOM   2536  N  NE2 . HIS C  1 43  ? 16.914  96.627  98.183  1.00 62.15 ? 43  HIS C NE2 1 
ATOM   2537  N  N   . GLY C  1 44  ? 11.235  99.543  95.936  1.00 52.38 ? 44  GLY C N   1 
ATOM   2538  C  CA  . GLY C  1 44  ? 10.132  99.773  95.021  1.00 58.95 ? 44  GLY C CA  1 
ATOM   2539  C  C   . GLY C  1 44  ? 10.253  98.895  93.785  1.00 59.07 ? 44  GLY C C   1 
ATOM   2540  O  O   . GLY C  1 44  ? 11.364  98.626  93.306  1.00 52.32 ? 44  GLY C O   1 
ATOM   2541  N  N   . PHE C  1 45  ? 9.107   98.453  93.271  1.00 52.03 ? 45  PHE C N   1 
ATOM   2542  C  CA  . PHE C  1 45  ? 9.070   97.414  92.250  1.00 55.68 ? 45  PHE C CA  1 
ATOM   2543  C  C   . PHE C  1 45  ? 7.923   97.676  91.277  1.00 53.91 ? 45  PHE C C   1 
ATOM   2544  O  O   . PHE C  1 45  ? 6.800   97.215  91.487  1.00 54.00 ? 45  PHE C O   1 
ATOM   2545  C  CB  . PHE C  1 45  ? 8.883   96.065  92.940  1.00 52.11 ? 45  PHE C CB  1 
ATOM   2546  C  CG  . PHE C  1 45  ? 9.163   94.884  92.069  1.00 48.98 ? 45  PHE C CG  1 
ATOM   2547  C  CD1 . PHE C  1 45  ? 10.371  94.763  91.415  1.00 49.50 ? 45  PHE C CD1 1 
ATOM   2548  C  CD2 . PHE C  1 45  ? 8.232   93.870  91.944  1.00 44.26 ? 45  PHE C CD2 1 
ATOM   2549  C  CE1 . PHE C  1 45  ? 10.635  93.662  90.626  1.00 48.43 ? 45  PHE C CE1 1 
ATOM   2550  C  CE2 . PHE C  1 45  ? 8.493   92.765  91.165  1.00 45.12 ? 45  PHE C CE2 1 
ATOM   2551  C  CZ  . PHE C  1 45  ? 9.694   92.659  90.502  1.00 44.32 ? 45  PHE C CZ  1 
ATOM   2552  N  N   . HIS C  1 46  ? 8.205   98.419  90.212  1.00 50.10 ? 46  HIS C N   1 
ATOM   2553  C  CA  . HIS C  1 46  ? 7.146   98.883  89.322  1.00 50.76 ? 46  HIS C CA  1 
ATOM   2554  C  C   . HIS C  1 46  ? 7.281   98.449  87.862  1.00 49.89 ? 46  HIS C C   1 
ATOM   2555  O  O   . HIS C  1 46  ? 8.370   98.137  87.367  1.00 44.86 ? 46  HIS C O   1 
ATOM   2556  C  CB  . HIS C  1 46  ? 7.062   100.409 89.346  1.00 53.42 ? 46  HIS C CB  1 
ATOM   2557  C  CG  . HIS C  1 46  ? 6.975   100.994 90.719  1.00 59.85 ? 46  HIS C CG  1 
ATOM   2558  N  ND1 . HIS C  1 46  ? 7.890   101.907 91.196  1.00 58.97 ? 46  HIS C ND1 1 
ATOM   2559  C  CD2 . HIS C  1 46  ? 6.073   100.810 91.711  1.00 55.08 ? 46  HIS C CD2 1 
ATOM   2560  C  CE1 . HIS C  1 46  ? 7.561   102.254 92.426  1.00 58.66 ? 46  HIS C CE1 1 
ATOM   2561  N  NE2 . HIS C  1 46  ? 6.462   101.603 92.763  1.00 59.21 ? 46  HIS C NE2 1 
ATOM   2562  N  N   . VAL C  1 47  ? 6.146   98.452  87.180  1.00 46.19 ? 47  VAL C N   1 
ATOM   2563  C  CA  . VAL C  1 47  ? 6.121   98.384  85.732  1.00 42.86 ? 47  VAL C CA  1 
ATOM   2564  C  C   . VAL C  1 47  ? 5.879   99.795  85.238  1.00 41.35 ? 47  VAL C C   1 
ATOM   2565  O  O   . VAL C  1 47  ? 4.825   100.376 85.491  1.00 41.51 ? 47  VAL C O   1 
ATOM   2566  C  CB  . VAL C  1 47  ? 4.983   97.488  85.237  1.00 44.48 ? 47  VAL C CB  1 
ATOM   2567  C  CG1 . VAL C  1 47  ? 4.803   97.641  83.725  1.00 44.92 ? 47  VAL C CG1 1 
ATOM   2568  C  CG2 . VAL C  1 47  ? 5.234   96.039  85.631  1.00 39.89 ? 47  VAL C CG2 1 
ATOM   2569  N  N   . HIS C  1 48  ? 6.867   100.362 84.562  1.00 40.80 ? 48  HIS C N   1 
ATOM   2570  C  CA  . HIS C  1 48  ? 6.697   101.671 83.947  1.00 44.69 ? 48  HIS C CA  1 
ATOM   2571  C  C   . HIS C  1 48  ? 6.056   101.556 82.565  1.00 43.16 ? 48  HIS C C   1 
ATOM   2572  O  O   . HIS C  1 48  ? 6.001   100.470 81.984  1.00 43.21 ? 48  HIS C O   1 
ATOM   2573  C  CB  . HIS C  1 48  ? 8.031   102.415 83.876  1.00 47.24 ? 48  HIS C CB  1 
ATOM   2574  C  CG  . HIS C  1 48  ? 8.505   102.915 85.204  1.00 51.56 ? 48  HIS C CG  1 
ATOM   2575  N  ND1 . HIS C  1 48  ? 8.333   104.220 85.613  1.00 54.04 ? 48  HIS C ND1 1 
ATOM   2576  C  CD2 . HIS C  1 48  ? 9.112   102.275 86.231  1.00 51.15 ? 48  HIS C CD2 1 
ATOM   2577  C  CE1 . HIS C  1 48  ? 8.835   104.367 86.827  1.00 54.14 ? 48  HIS C CE1 1 
ATOM   2578  N  NE2 . HIS C  1 48  ? 9.315   103.202 87.224  1.00 55.60 ? 48  HIS C NE2 1 
ATOM   2579  N  N   . GLU C  1 49  ? 5.573   102.680 82.051  1.00 43.30 ? 49  GLU C N   1 
ATOM   2580  C  CA  . GLU C  1 49  ? 4.796   102.691 80.817  1.00 46.43 ? 49  GLU C CA  1 
ATOM   2581  C  C   . GLU C  1 49  ? 5.576   102.228 79.577  1.00 46.81 ? 49  GLU C C   1 
ATOM   2582  O  O   . GLU C  1 49  ? 5.077   101.418 78.801  1.00 41.99 ? 49  GLU C O   1 
ATOM   2583  C  CB  . GLU C  1 49  ? 4.205   104.079 80.572  1.00 44.18 ? 49  GLU C CB  1 
ATOM   2584  C  CG  . GLU C  1 49  ? 3.164   104.105 79.467  1.00 50.26 ? 49  GLU C CG  1 
ATOM   2585  C  CD  . GLU C  1 49  ? 2.556   105.479 79.263  1.00 51.19 ? 49  GLU C CD  1 
ATOM   2586  O  OE1 . GLU C  1 49  ? 2.914   106.416 80.015  1.00 46.91 ? 49  GLU C OE1 1 
ATOM   2587  O  OE2 . GLU C  1 49  ? 1.716   105.618 78.348  1.00 51.97 ? 49  GLU C OE2 1 
ATOM   2588  N  N   . PHE C  1 50  ? 6.791   102.733 79.387  1.00 42.87 ? 50  PHE C N   1 
ATOM   2589  C  CA  . PHE C  1 50  ? 7.510   102.459 78.140  1.00 39.84 ? 50  PHE C CA  1 
ATOM   2590  C  C   . PHE C  1 50  ? 8.605   101.406 78.249  1.00 41.93 ? 50  PHE C C   1 
ATOM   2591  O  O   . PHE C  1 50  ? 9.396   101.392 79.199  1.00 42.11 ? 50  PHE C O   1 
ATOM   2592  C  CB  . PHE C  1 50  ? 8.088   103.749 77.556  1.00 40.09 ? 50  PHE C CB  1 
ATOM   2593  C  CG  . PHE C  1 50  ? 7.111   104.875 77.519  1.00 41.54 ? 50  PHE C CG  1 
ATOM   2594  C  CD1 . PHE C  1 50  ? 5.851   104.695 76.973  1.00 44.64 ? 50  PHE C CD1 1 
ATOM   2595  C  CD2 . PHE C  1 50  ? 7.435   106.106 78.061  1.00 46.69 ? 50  PHE C CD2 1 
ATOM   2596  C  CE1 . PHE C  1 50  ? 4.939   105.725 76.947  1.00 45.16 ? 50  PHE C CE1 1 
ATOM   2597  C  CE2 . PHE C  1 50  ? 6.524   107.144 78.044  1.00 49.35 ? 50  PHE C CE2 1 
ATOM   2598  C  CZ  . PHE C  1 50  ? 5.272   106.951 77.491  1.00 49.16 ? 50  PHE C CZ  1 
ATOM   2599  N  N   . GLY C  1 51  ? 8.647   100.525 77.255  1.00 38.36 ? 51  GLY C N   1 
ATOM   2600  C  CA  . GLY C  1 51  ? 9.769   99.624  77.081  1.00 36.15 ? 51  GLY C CA  1 
ATOM   2601  C  C   . GLY C  1 51  ? 10.916  100.304 76.346  1.00 39.24 ? 51  GLY C C   1 
ATOM   2602  O  O   . GLY C  1 51  ? 11.701  99.649  75.644  1.00 35.47 ? 51  GLY C O   1 
ATOM   2603  N  N   . ASP C  1 52  ? 10.996  101.625 76.494  1.00 36.01 ? 52  ASP C N   1 
ATOM   2604  C  CA  . ASP C  1 52  ? 12.096  102.402 75.947  1.00 37.75 ? 52  ASP C CA  1 
ATOM   2605  C  C   . ASP C  1 52  ? 13.251  102.482 76.932  1.00 44.75 ? 52  ASP C C   1 
ATOM   2606  O  O   . ASP C  1 52  ? 13.104  102.997 78.038  1.00 46.89 ? 52  ASP C O   1 
ATOM   2607  C  CB  . ASP C  1 52  ? 11.637  103.818 75.595  1.00 36.75 ? 52  ASP C CB  1 
ATOM   2608  C  CG  . ASP C  1 52  ? 12.703  104.603 74.839  1.00 42.21 ? 52  ASP C CG  1 
ATOM   2609  O  OD1 . ASP C  1 52  ? 13.855  104.121 74.762  1.00 38.39 ? 52  ASP C OD1 1 
ATOM   2610  O  OD2 . ASP C  1 52  ? 12.391  105.698 74.326  1.00 38.99 ? 52  ASP C OD2 1 
ATOM   2611  N  N   . ASN C  1 53  ? 14.410  101.987 76.520  1.00 47.63 ? 53  ASN C N   1 
ATOM   2612  C  CA  . ASN C  1 53  ? 15.607  102.124 77.336  1.00 46.57 ? 53  ASN C CA  1 
ATOM   2613  C  C   . ASN C  1 53  ? 16.668  102.929 76.597  1.00 49.90 ? 53  ASN C C   1 
ATOM   2614  O  O   . ASN C  1 53  ? 17.858  102.776 76.852  1.00 50.02 ? 53  ASN C O   1 
ATOM   2615  C  CB  . ASN C  1 53  ? 16.160  100.757 77.758  1.00 49.59 ? 53  ASN C CB  1 
ATOM   2616  C  CG  . ASN C  1 53  ? 15.258  100.034 78.767  1.00 57.53 ? 53  ASN C CG  1 
ATOM   2617  O  OD1 . ASN C  1 53  ? 14.288  100.604 79.288  1.00 54.27 ? 53  ASN C OD1 1 
ATOM   2618  N  ND2 . ASN C  1 53  ? 15.590  98.773  79.056  1.00 49.90 ? 53  ASN C ND2 1 
ATOM   2619  N  N   . THR C  1 54  ? 16.222  103.791 75.684  1.00 51.35 ? 54  THR C N   1 
ATOM   2620  C  CA  . THR C  1 54  ? 17.130  104.635 74.907  1.00 50.05 ? 54  THR C CA  1 
ATOM   2621  C  C   . THR C  1 54  ? 18.040  105.467 75.816  1.00 51.66 ? 54  THR C C   1 
ATOM   2622  O  O   . THR C  1 54  ? 19.210  105.686 75.499  1.00 49.01 ? 54  THR C O   1 
ATOM   2623  C  CB  . THR C  1 54  ? 16.360  105.545 73.891  1.00 49.28 ? 54  THR C CB  1 
ATOM   2624  O  OG1 . THR C  1 54  ? 17.272  106.101 72.936  1.00 53.10 ? 54  THR C OG1 1 
ATOM   2625  C  CG2 . THR C  1 54  ? 15.602  106.670 74.592  1.00 41.94 ? 54  THR C CG2 1 
ATOM   2626  N  N   . ALA C  1 55  ? 17.494  105.898 76.953  1.00 53.92 ? 55  ALA C N   1 
ATOM   2627  C  CA  . ALA C  1 55  ? 18.224  106.685 77.943  1.00 54.62 ? 55  ALA C CA  1 
ATOM   2628  C  C   . ALA C  1 55  ? 18.188  105.985 79.297  1.00 57.52 ? 55  ALA C C   1 
ATOM   2629  O  O   . ALA C  1 55  ? 18.036  106.625 80.344  1.00 62.70 ? 55  ALA C O   1 
ATOM   2630  C  CB  . ALA C  1 55  ? 17.626  108.082 78.054  1.00 57.54 ? 55  ALA C CB  1 
ATOM   2631  N  N   . GLY C  1 56  ? 18.330  104.664 79.273  1.00 56.23 ? 56  GLY C N   1 
ATOM   2632  C  CA  . GLY C  1 56  ? 18.244  103.875 80.485  1.00 56.40 ? 56  GLY C CA  1 
ATOM   2633  C  C   . GLY C  1 56  ? 16.829  103.883 81.024  1.00 58.87 ? 56  GLY C C   1 
ATOM   2634  O  O   . GLY C  1 56  ? 15.871  104.121 80.283  1.00 57.90 ? 56  GLY C O   1 
ATOM   2635  N  N   . SER C  1 57  ? 16.696  103.641 82.323  1.00 59.86 ? 57  SER C N   1 
ATOM   2636  C  CA  . SER C  1 57  ? 15.384  103.535 82.959  1.00 58.05 ? 57  SER C CA  1 
ATOM   2637  C  C   . SER C  1 57  ? 14.586  104.846 82.980  1.00 55.92 ? 57  SER C C   1 
ATOM   2638  O  O   . SER C  1 57  ? 13.376  104.840 83.201  1.00 54.14 ? 57  SER C O   1 
ATOM   2639  C  CB  . SER C  1 57  ? 15.542  102.982 84.379  1.00 56.77 ? 57  SER C CB  1 
ATOM   2640  O  OG  . SER C  1 57  ? 16.763  103.420 84.952  1.00 54.04 ? 57  SER C OG  1 
ATOM   2641  N  N   . THR C  1 58  ? 15.257  105.969 82.748  1.00 57.07 ? 58  THR C N   1 
ATOM   2642  C  CA  . THR C  1 58  ? 14.585  107.264 82.810  1.00 58.67 ? 58  THR C CA  1 
ATOM   2643  C  C   . THR C  1 58  ? 13.662  107.486 81.605  1.00 60.38 ? 58  THR C C   1 
ATOM   2644  O  O   . THR C  1 58  ? 12.663  108.204 81.702  1.00 56.78 ? 58  THR C O   1 
ATOM   2645  C  CB  . THR C  1 58  ? 15.588  108.431 82.920  1.00 58.36 ? 58  THR C CB  1 
ATOM   2646  O  OG1 . THR C  1 58  ? 15.767  109.032 81.634  1.00 59.83 ? 58  THR C OG1 1 
ATOM   2647  C  CG2 . THR C  1 58  ? 16.930  107.941 83.454  1.00 60.18 ? 58  THR C CG2 1 
ATOM   2648  N  N   . SER C  1 59  ? 14.000  106.867 80.474  1.00 60.79 ? 59  SER C N   1 
ATOM   2649  C  CA  . SER C  1 59  ? 13.156  106.934 79.281  1.00 54.52 ? 59  SER C CA  1 
ATOM   2650  C  C   . SER C  1 59  ? 11.991  105.943 79.353  1.00 49.91 ? 59  SER C C   1 
ATOM   2651  O  O   . SER C  1 59  ? 11.182  105.862 78.432  1.00 49.58 ? 59  SER C O   1 
ATOM   2652  C  CB  . SER C  1 59  ? 13.981  106.690 78.016  1.00 50.31 ? 59  SER C CB  1 
ATOM   2653  O  OG  . SER C  1 59  ? 14.658  105.449 78.083  1.00 49.85 ? 59  SER C OG  1 
ATOM   2654  N  N   . ALA C  1 60  ? 11.910  105.203 80.457  1.00 50.17 ? 60  ALA C N   1 
ATOM   2655  C  CA  . ALA C  1 60  ? 10.815  104.261 80.681  1.00 47.80 ? 60  ALA C CA  1 
ATOM   2656  C  C   . ALA C  1 60  ? 9.546   104.948 81.186  1.00 47.59 ? 60  ALA C C   1 
ATOM   2657  O  O   . ALA C  1 60  ? 8.503   104.307 81.341  1.00 48.34 ? 60  ALA C O   1 
ATOM   2658  C  CB  . ALA C  1 60  ? 11.244  103.167 81.641  1.00 48.19 ? 60  ALA C CB  1 
ATOM   2659  N  N   . GLY C  1 61  ? 9.640   106.250 81.444  1.00 45.85 ? 61  GLY C N   1 
ATOM   2660  C  CA  . GLY C  1 61  ? 8.485   107.047 81.816  1.00 47.79 ? 61  GLY C CA  1 
ATOM   2661  C  C   . GLY C  1 61  ? 7.860   106.729 83.167  1.00 49.05 ? 61  GLY C C   1 
ATOM   2662  O  O   . GLY C  1 61  ? 8.455   106.035 83.992  1.00 44.52 ? 61  GLY C O   1 
ATOM   2663  N  N   . PRO C  1 62  ? 6.635   107.230 83.390  1.00 48.51 ? 62  PRO C N   1 
ATOM   2664  C  CA  . PRO C  1 62  ? 5.897   107.117 84.652  1.00 46.78 ? 62  PRO C CA  1 
ATOM   2665  C  C   . PRO C  1 62  ? 5.564   105.678 84.968  1.00 48.73 ? 62  PRO C C   1 
ATOM   2666  O  O   . PRO C  1 62  ? 5.898   104.780 84.202  1.00 48.03 ? 62  PRO C O   1 
ATOM   2667  C  CB  . PRO C  1 62  ? 4.591   107.858 84.364  1.00 44.38 ? 62  PRO C CB  1 
ATOM   2668  C  CG  . PRO C  1 62  ? 4.846   108.671 83.146  1.00 48.31 ? 62  PRO C CG  1 
ATOM   2669  C  CD  . PRO C  1 62  ? 5.838   107.899 82.351  1.00 49.72 ? 62  PRO C CD  1 
ATOM   2670  N  N   . HIS C  1 63  ? 4.902   105.464 86.096  1.00 47.44 ? 63  HIS C N   1 
ATOM   2671  C  CA  . HIS C  1 63  ? 4.353   104.154 86.403  1.00 50.47 ? 63  HIS C CA  1 
ATOM   2672  C  C   . HIS C  1 63  ? 3.325   103.827 85.327  1.00 45.73 ? 63  HIS C C   1 
ATOM   2673  O  O   . HIS C  1 63  ? 2.710   104.736 84.761  1.00 44.38 ? 63  HIS C O   1 
ATOM   2674  C  CB  . HIS C  1 63  ? 3.693   104.158 87.787  1.00 49.91 ? 63  HIS C CB  1 
ATOM   2675  C  CG  . HIS C  1 63  ? 4.665   104.276 88.921  1.00 53.79 ? 63  HIS C CG  1 
ATOM   2676  N  ND1 . HIS C  1 63  ? 4.319   104.020 90.230  1.00 54.63 ? 63  HIS C ND1 1 
ATOM   2677  C  CD2 . HIS C  1 63  ? 5.976   104.614 88.938  1.00 58.52 ? 63  HIS C CD2 1 
ATOM   2678  C  CE1 . HIS C  1 63  ? 5.375   104.196 91.004  1.00 59.47 ? 63  HIS C CE1 1 
ATOM   2679  N  NE2 . HIS C  1 63  ? 6.395   104.556 90.245  1.00 58.26 ? 63  HIS C NE2 1 
ATOM   2680  N  N   . PHE C  1 64  ? 3.151   102.539 85.038  1.00 48.25 ? 64  PHE C N   1 
ATOM   2681  C  CA  . PHE C  1 64  ? 2.134   102.097 84.090  1.00 43.76 ? 64  PHE C CA  1 
ATOM   2682  C  C   . PHE C  1 64  ? 0.756   102.409 84.635  1.00 42.79 ? 64  PHE C C   1 
ATOM   2683  O  O   . PHE C  1 64  ? 0.231   101.660 85.449  1.00 45.54 ? 64  PHE C O   1 
ATOM   2684  C  CB  . PHE C  1 64  ? 2.237   100.595 83.840  1.00 42.93 ? 64  PHE C CB  1 
ATOM   2685  C  CG  . PHE C  1 64  ? 1.367   100.107 82.713  1.00 44.27 ? 64  PHE C CG  1 
ATOM   2686  C  CD1 . PHE C  1 64  ? 1.010   100.959 81.674  1.00 44.99 ? 64  PHE C CD1 1 
ATOM   2687  C  CD2 . PHE C  1 64  ? 0.903   98.796  82.692  1.00 42.63 ? 64  PHE C CD2 1 
ATOM   2688  C  CE1 . PHE C  1 64  ? 0.209   100.512 80.636  1.00 47.00 ? 64  PHE C CE1 1 
ATOM   2689  C  CE2 . PHE C  1 64  ? 0.103   98.341  81.659  1.00 41.18 ? 64  PHE C CE2 1 
ATOM   2690  C  CZ  . PHE C  1 64  ? -0.248  99.199  80.629  1.00 43.08 ? 64  PHE C CZ  1 
ATOM   2691  N  N   . ASN C  1 65  ? 0.165   103.504 84.169  1.00 45.61 ? 65  ASN C N   1 
ATOM   2692  C  CA  . ASN C  1 65  ? -1.120  103.952 84.692  1.00 48.03 ? 65  ASN C CA  1 
ATOM   2693  C  C   . ASN C  1 65  ? -2.220  104.126 83.643  1.00 46.63 ? 65  ASN C C   1 
ATOM   2694  O  O   . ASN C  1 65  ? -2.674  105.248 83.402  1.00 45.05 ? 65  ASN C O   1 
ATOM   2695  C  CB  . ASN C  1 65  ? -0.940  105.254 85.484  1.00 53.47 ? 65  ASN C CB  1 
ATOM   2696  C  CG  . ASN C  1 65  ? -2.190  105.652 86.258  1.00 58.06 ? 65  ASN C CG  1 
ATOM   2697  O  OD1 . ASN C  1 65  ? -3.063  104.818 86.537  1.00 54.34 ? 65  ASN C OD1 1 
ATOM   2698  N  ND2 . ASN C  1 65  ? -2.278  106.932 86.617  1.00 60.33 ? 65  ASN C ND2 1 
ATOM   2699  N  N   . PRO C  1 66  ? -2.671  103.014 83.029  1.00 50.92 ? 66  PRO C N   1 
ATOM   2700  C  CA  . PRO C  1 66  ? -3.723  103.114 82.010  1.00 49.54 ? 66  PRO C CA  1 
ATOM   2701  C  C   . PRO C  1 66  ? -5.061  103.609 82.559  1.00 53.30 ? 66  PRO C C   1 
ATOM   2702  O  O   . PRO C  1 66  ? -5.765  104.364 81.880  1.00 49.24 ? 66  PRO C O   1 
ATOM   2703  C  CB  . PRO C  1 66  ? -3.871  101.668 81.523  1.00 46.65 ? 66  PRO C CB  1 
ATOM   2704  C  CG  . PRO C  1 66  ? -3.375  100.835 82.650  1.00 42.42 ? 66  PRO C CG  1 
ATOM   2705  C  CD  . PRO C  1 66  ? -2.220  101.621 83.197  1.00 43.05 ? 66  PRO C CD  1 
ATOM   2706  N  N   . LEU C  1 67  ? -5.408  103.186 83.770  1.00 52.42 ? 67  LEU C N   1 
ATOM   2707  C  CA  . LEU C  1 67  ? -6.723  103.493 84.326  1.00 55.00 ? 67  LEU C CA  1 
ATOM   2708  C  C   . LEU C  1 67  ? -6.787  104.872 84.987  1.00 61.50 ? 67  LEU C C   1 
ATOM   2709  O  O   . LEU C  1 67  ? -7.844  105.288 85.470  1.00 61.03 ? 67  LEU C O   1 
ATOM   2710  C  CB  . LEU C  1 67  ? -7.168  102.384 85.282  1.00 54.52 ? 67  LEU C CB  1 
ATOM   2711  C  CG  . LEU C  1 67  ? -7.186  101.023 84.579  1.00 51.69 ? 67  LEU C CG  1 
ATOM   2712  C  CD1 . LEU C  1 67  ? -7.609  99.908  85.510  1.00 55.07 ? 67  LEU C CD1 1 
ATOM   2713  C  CD2 . LEU C  1 67  ? -8.096  101.077 83.368  1.00 47.96 ? 67  LEU C CD2 1 
ATOM   2714  N  N   . SER C  1 68  ? -5.656  105.579 84.983  1.00 57.51 ? 68  SER C N   1 
ATOM   2715  C  CA  . SER C  1 68  ? -5.583  106.955 85.480  1.00 58.71 ? 68  SER C CA  1 
ATOM   2716  C  C   . SER C  1 68  ? -6.077  107.099 86.924  1.00 65.54 ? 68  SER C C   1 
ATOM   2717  O  O   . SER C  1 68  ? -7.167  107.623 87.175  1.00 60.49 ? 68  SER C O   1 
ATOM   2718  C  CB  . SER C  1 68  ? -6.343  107.904 84.550  1.00 55.55 ? 68  SER C CB  1 
ATOM   2719  O  OG  . SER C  1 68  ? -5.711  107.978 83.285  1.00 56.08 ? 68  SER C OG  1 
ATOM   2720  N  N   . ARG C  1 69  ? -5.258  106.636 87.864  1.00 66.25 ? 69  ARG C N   1 
ATOM   2721  C  CA  . ARG C  1 69  ? -5.618  106.624 89.276  1.00 64.31 ? 69  ARG C CA  1 
ATOM   2722  C  C   . ARG C  1 69  ? -4.611  107.442 90.084  1.00 68.05 ? 69  ARG C C   1 
ATOM   2723  O  O   . ARG C  1 69  ? -4.192  108.523 89.665  1.00 70.11 ? 69  ARG C O   1 
ATOM   2724  C  CB  . ARG C  1 69  ? -5.651  105.183 89.796  1.00 61.21 ? 69  ARG C CB  1 
ATOM   2725  C  CG  . ARG C  1 69  ? -6.446  104.226 88.932  1.00 61.58 ? 69  ARG C CG  1 
ATOM   2726  C  CD  . ARG C  1 69  ? -7.931  104.403 89.136  1.00 60.87 ? 69  ARG C CD  1 
ATOM   2727  N  NE  . ARG C  1 69  ? -8.509  103.272 89.858  1.00 68.35 ? 69  ARG C NE  1 
ATOM   2728  C  CZ  . ARG C  1 69  ? -9.088  102.225 89.274  1.00 63.68 ? 69  ARG C CZ  1 
ATOM   2729  N  NH1 . ARG C  1 69  ? -9.173  102.163 87.953  1.00 66.88 ? 69  ARG C NH1 1 
ATOM   2730  N  NH2 . ARG C  1 69  ? -9.583  101.240 90.010  1.00 66.24 ? 69  ARG C NH2 1 
ATOM   2731  N  N   . LYS C  1 70  ? -4.238  106.918 91.249  1.00 66.34 ? 70  LYS C N   1 
ATOM   2732  C  CA  . LYS C  1 70  ? -3.210  107.511 92.093  1.00 63.32 ? 70  LYS C CA  1 
ATOM   2733  C  C   . LYS C  1 70  ? -2.303  106.378 92.543  1.00 61.51 ? 70  LYS C C   1 
ATOM   2734  O  O   . LYS C  1 70  ? -2.759  105.244 92.686  1.00 61.46 ? 70  LYS C O   1 
ATOM   2735  C  CB  . LYS C  1 70  ? -3.838  108.202 93.304  1.00 63.03 ? 70  LYS C CB  1 
ATOM   2736  C  CG  . LYS C  1 70  ? -4.953  109.181 92.943  1.00 69.85 ? 70  LYS C CG  1 
ATOM   2737  C  CD  . LYS C  1 70  ? -5.662  109.737 94.173  1.00 72.63 ? 70  LYS C CD  1 
ATOM   2738  C  CE  . LYS C  1 70  ? -4.719  110.564 95.036  1.00 74.94 ? 70  LYS C CE  1 
ATOM   2739  N  NZ  . LYS C  1 70  ? -5.420  111.233 96.173  1.00 76.89 ? 70  LYS C NZ  1 
ATOM   2740  N  N   . HIS C  1 71  ? -1.024  106.670 92.754  1.00 56.60 ? 71  HIS C N   1 
ATOM   2741  C  CA  . HIS C  1 71  ? -0.085  105.623 93.132  1.00 58.24 ? 71  HIS C CA  1 
ATOM   2742  C  C   . HIS C  1 71  ? -0.509  104.950 94.423  1.00 63.08 ? 71  HIS C C   1 
ATOM   2743  O  O   . HIS C  1 71  ? -1.002  105.605 95.341  1.00 68.02 ? 71  HIS C O   1 
ATOM   2744  C  CB  . HIS C  1 71  ? 1.336   106.164 93.280  1.00 57.91 ? 71  HIS C CB  1 
ATOM   2745  C  CG  . HIS C  1 71  ? 2.300   105.168 93.846  1.00 59.09 ? 71  HIS C CG  1 
ATOM   2746  N  ND1 . HIS C  1 71  ? 2.649   104.007 93.189  1.00 60.32 ? 71  HIS C ND1 1 
ATOM   2747  C  CD2 . HIS C  1 71  ? 2.971   105.147 95.021  1.00 63.30 ? 71  HIS C CD2 1 
ATOM   2748  C  CE1 . HIS C  1 71  ? 3.506   103.324 93.927  1.00 58.62 ? 71  HIS C CE1 1 
ATOM   2749  N  NE2 . HIS C  1 71  ? 3.720   103.996 95.043  1.00 59.18 ? 71  HIS C NE2 1 
ATOM   2750  N  N   . GLY C  1 72  ? -0.323  103.638 94.482  1.00 59.27 ? 72  GLY C N   1 
ATOM   2751  C  CA  . GLY C  1 72  ? -0.636  102.892 95.680  1.00 56.79 ? 72  GLY C CA  1 
ATOM   2752  C  C   . GLY C  1 72  ? 0.237   101.664 95.816  1.00 56.78 ? 72  GLY C C   1 
ATOM   2753  O  O   . GLY C  1 72  ? 1.239   101.501 95.103  1.00 53.74 ? 72  GLY C O   1 
ATOM   2754  N  N   . GLY C  1 73  ? -0.145  100.809 96.759  1.00 54.73 ? 73  GLY C N   1 
ATOM   2755  C  CA  . GLY C  1 73  ? 0.454   99.501  96.903  1.00 48.52 ? 73  GLY C CA  1 
ATOM   2756  C  C   . GLY C  1 73  ? -0.501  98.523  96.260  1.00 49.35 ? 73  GLY C C   1 
ATOM   2757  O  O   . GLY C  1 73  ? -1.664  98.865  96.021  1.00 47.60 ? 73  GLY C O   1 
ATOM   2758  N  N   . PRO C  1 74  ? -0.008  97.316  95.956  1.00 47.55 ? 74  PRO C N   1 
ATOM   2759  C  CA  . PRO C  1 74  ? -0.746  96.216  95.332  1.00 50.15 ? 74  PRO C CA  1 
ATOM   2760  C  C   . PRO C  1 74  ? -2.150  96.015  95.890  1.00 52.12 ? 74  PRO C C   1 
ATOM   2761  O  O   . PRO C  1 74  ? -3.100  95.988  95.108  1.00 53.45 ? 74  PRO C O   1 
ATOM   2762  C  CB  . PRO C  1 74  ? 0.132   94.988  95.628  1.00 45.75 ? 74  PRO C CB  1 
ATOM   2763  C  CG  . PRO C  1 74  ? 1.456   95.530  96.122  1.00 43.43 ? 74  PRO C CG  1 
ATOM   2764  C  CD  . PRO C  1 74  ? 1.429   97.021  96.013  1.00 46.52 ? 74  PRO C CD  1 
ATOM   2765  N  N   . LYS C  1 75  ? -2.282  95.890  97.208  1.00 51.44 ? 75  LYS C N   1 
ATOM   2766  C  CA  . LYS C  1 75  ? -3.569  95.543  97.812  1.00 51.72 ? 75  LYS C CA  1 
ATOM   2767  C  C   . LYS C  1 75  ? -4.661  96.601  97.608  1.00 51.84 ? 75  LYS C C   1 
ATOM   2768  O  O   . LYS C  1 75  ? -5.838  96.266  97.502  1.00 46.94 ? 75  LYS C O   1 
ATOM   2769  C  CB  . LYS C  1 75  ? -3.408  95.258  99.307  1.00 54.05 ? 75  LYS C CB  1 
ATOM   2770  C  CG  . LYS C  1 75  ? -2.457  94.123  99.646  1.00 51.66 ? 75  LYS C CG  1 
ATOM   2771  C  CD  . LYS C  1 75  ? -2.695  93.643  101.077 1.00 57.47 ? 75  LYS C CD  1 
ATOM   2772  C  CE  . LYS C  1 75  ? -2.808  94.812  102.052 1.00 48.38 ? 75  LYS C CE  1 
ATOM   2773  N  NZ  . LYS C  1 75  ? -3.037  94.353  103.448 1.00 42.72 ? 75  LYS C NZ  1 
ATOM   2774  N  N   . ASP C  1 76  ? -4.267  97.870  97.557  1.00 52.68 ? 76  ASP C N   1 
ATOM   2775  C  CA  . ASP C  1 76  ? -5.228  98.967  97.449  1.00 54.22 ? 76  ASP C CA  1 
ATOM   2776  C  C   . ASP C  1 76  ? -6.008  98.918  96.137  1.00 60.08 ? 76  ASP C C   1 
ATOM   2777  O  O   . ASP C  1 76  ? -5.507  98.436  95.118  1.00 56.14 ? 76  ASP C O   1 
ATOM   2778  C  CB  . ASP C  1 76  ? -4.527  100.324 97.576  1.00 54.66 ? 76  ASP C CB  1 
ATOM   2779  C  CG  . ASP C  1 76  ? -3.571  100.386 98.753  1.00 58.54 ? 76  ASP C CG  1 
ATOM   2780  O  OD1 . ASP C  1 76  ? -3.799  99.671  99.755  1.00 60.27 ? 76  ASP C OD1 1 
ATOM   2781  O  OD2 . ASP C  1 76  ? -2.587  101.153 98.673  1.00 57.67 ? 76  ASP C OD2 1 
ATOM   2782  N  N   . GLU C  1 77  ? -7.237  99.418  96.168  1.00 61.02 ? 77  GLU C N   1 
ATOM   2783  C  CA  . GLU C  1 77  ? -8.040  99.499  94.962  1.00 58.18 ? 77  GLU C CA  1 
ATOM   2784  C  C   . GLU C  1 77  ? -7.586  100.691 94.120  1.00 61.09 ? 77  GLU C C   1 
ATOM   2785  O  O   . GLU C  1 77  ? -7.527  100.607 92.892  1.00 64.18 ? 77  GLU C O   1 
ATOM   2786  C  CB  . GLU C  1 77  ? -9.524  99.604  95.310  1.00 59.94 ? 77  GLU C CB  1 
ATOM   2787  C  CG  . GLU C  1 77  ? -10.396 98.632  94.540  1.00 63.90 ? 77  GLU C CG  1 
ATOM   2788  C  CD  . GLU C  1 77  ? -11.510 99.328  93.780  1.00 70.37 ? 77  GLU C CD  1 
ATOM   2789  O  OE1 . GLU C  1 77  ? -12.512 99.714  94.420  1.00 73.73 ? 77  GLU C OE1 1 
ATOM   2790  O  OE2 . GLU C  1 77  ? -11.381 99.495  92.544  1.00 68.65 ? 77  GLU C OE2 1 
ATOM   2791  N  N   . GLU C  1 78  ? -7.256  101.797 94.780  1.00 57.42 ? 78  GLU C N   1 
ATOM   2792  C  CA  . GLU C  1 78  ? -6.733  102.967 94.079  1.00 59.42 ? 78  GLU C CA  1 
ATOM   2793  C  C   . GLU C  1 78  ? -5.221  102.838 93.892  1.00 59.07 ? 78  GLU C C   1 
ATOM   2794  O  O   . GLU C  1 78  ? -4.443  103.051 94.817  1.00 59.96 ? 78  GLU C O   1 
ATOM   2795  C  CB  . GLU C  1 78  ? -7.085  104.262 94.824  1.00 59.62 ? 78  GLU C CB  1 
ATOM   2796  C  CG  . GLU C  1 78  ? -6.729  105.554 94.074  1.00 62.75 ? 78  GLU C CG  1 
ATOM   2797  C  CD  . GLU C  1 78  ? -7.754  105.948 93.006  1.00 62.73 ? 78  GLU C CD  1 
ATOM   2798  O  OE1 . GLU C  1 78  ? -8.742  105.211 92.791  1.00 61.22 ? 78  GLU C OE1 1 
ATOM   2799  O  OE2 . GLU C  1 78  ? -7.570  107.011 92.379  1.00 57.04 ? 78  GLU C OE2 1 
ATOM   2800  N  N   . ARG C  1 79  ? -4.814  102.480 92.680  1.00 58.48 ? 79  ARG C N   1 
ATOM   2801  C  CA  . ARG C  1 79  ? -3.414  102.217 92.383  1.00 52.88 ? 79  ARG C CA  1 
ATOM   2802  C  C   . ARG C  1 79  ? -3.164  102.307 90.881  1.00 53.79 ? 79  ARG C C   1 
ATOM   2803  O  O   . ARG C  1 79  ? -4.092  102.200 90.079  1.00 51.91 ? 79  ARG C O   1 
ATOM   2804  C  CB  . ARG C  1 79  ? -3.030  100.827 92.877  1.00 49.87 ? 79  ARG C CB  1 
ATOM   2805  C  CG  . ARG C  1 79  ? -4.029  99.754  92.481  1.00 49.00 ? 79  ARG C CG  1 
ATOM   2806  C  CD  . ARG C  1 79  ? -3.441  98.368  92.620  1.00 46.99 ? 79  ARG C CD  1 
ATOM   2807  N  NE  . ARG C  1 79  ? -2.435  98.100  91.596  1.00 52.25 ? 79  ARG C NE  1 
ATOM   2808  C  CZ  . ARG C  1 79  ? -1.812  96.935  91.440  1.00 48.03 ? 79  ARG C CZ  1 
ATOM   2809  N  NH1 . ARG C  1 79  ? -2.097  95.913  92.240  1.00 38.81 ? 79  ARG C NH1 1 
ATOM   2810  N  NH2 . ARG C  1 79  ? -0.918  96.781  90.469  1.00 42.97 ? 79  ARG C NH2 1 
ATOM   2811  N  N   . HIS C  1 80  ? -1.910  102.517 90.505  1.00 53.67 ? 80  HIS C N   1 
ATOM   2812  C  CA  . HIS C  1 80  ? -1.524  102.421 89.107  1.00 50.85 ? 80  HIS C CA  1 
ATOM   2813  C  C   . HIS C  1 80  ? -1.309  100.936 88.818  1.00 48.86 ? 80  HIS C C   1 
ATOM   2814  O  O   . HIS C  1 80  ? -0.885  100.192 89.710  1.00 46.81 ? 80  HIS C O   1 
ATOM   2815  C  CB  . HIS C  1 80  ? -0.240  103.216 88.844  1.00 47.04 ? 80  HIS C CB  1 
ATOM   2816  C  CG  . HIS C  1 80  ? -0.317  104.659 89.245  1.00 51.51 ? 80  HIS C CG  1 
ATOM   2817  N  ND1 . HIS C  1 80  ? 0.783   105.371 89.678  1.00 47.51 ? 80  HIS C ND1 1 
ATOM   2818  C  CD2 . HIS C  1 80  ? -1.357  105.527 89.265  1.00 56.44 ? 80  HIS C CD2 1 
ATOM   2819  C  CE1 . HIS C  1 80  ? 0.426   106.616 89.937  1.00 51.74 ? 80  HIS C CE1 1 
ATOM   2820  N  NE2 . HIS C  1 80  ? -0.868  106.736 89.699  1.00 58.11 ? 80  HIS C NE2 1 
ATOM   2821  N  N   . VAL C  1 81  ? -1.607  100.508 87.588  1.00 47.71 ? 81  VAL C N   1 
ATOM   2822  C  CA  . VAL C  1 81  ? -1.475  99.098  87.184  1.00 39.22 ? 81  VAL C CA  1 
ATOM   2823  C  C   . VAL C  1 81  ? -0.045  98.582  87.341  1.00 37.30 ? 81  VAL C C   1 
ATOM   2824  O  O   . VAL C  1 81  ? 0.176   97.415  87.682  1.00 38.12 ? 81  VAL C O   1 
ATOM   2825  C  CB  . VAL C  1 81  ? -1.989  98.875  85.731  1.00 43.35 ? 81  VAL C CB  1 
ATOM   2826  C  CG1 . VAL C  1 81  ? -1.530  97.519  85.155  1.00 36.31 ? 81  VAL C CG1 1 
ATOM   2827  C  CG2 . VAL C  1 81  ? -3.510  98.999  85.682  1.00 38.92 ? 81  VAL C CG2 1 
ATOM   2828  N  N   . GLY C  1 82  ? 0.924   99.462  87.112  1.00 40.49 ? 82  GLY C N   1 
ATOM   2829  C  CA  . GLY C  1 82  ? 2.325   99.108  87.270  1.00 45.22 ? 82  GLY C CA  1 
ATOM   2830  C  C   . GLY C  1 82  ? 2.801   98.925  88.710  1.00 46.18 ? 82  GLY C C   1 
ATOM   2831  O  O   . GLY C  1 82  ? 3.914   98.441  88.935  1.00 47.53 ? 82  GLY C O   1 
ATOM   2832  N  N   . ASP C  1 83  ? 1.969   99.293  89.685  1.00 45.60 ? 83  ASP C N   1 
ATOM   2833  C  CA  . ASP C  1 83  ? 2.367   99.228  91.102  1.00 45.35 ? 83  ASP C CA  1 
ATOM   2834  C  C   . ASP C  1 83  ? 2.367   97.825  91.715  1.00 42.43 ? 83  ASP C C   1 
ATOM   2835  O  O   . ASP C  1 83  ? 1.318   97.322  92.132  1.00 40.20 ? 83  ASP C O   1 
ATOM   2836  C  CB  . ASP C  1 83  ? 1.478   100.138 91.942  1.00 37.27 ? 83  ASP C CB  1 
ATOM   2837  C  CG  . ASP C  1 83  ? 1.615   101.582 91.564  1.00 41.47 ? 83  ASP C CG  1 
ATOM   2838  O  OD1 . ASP C  1 83  ? 2.754   102.049 91.318  1.00 42.93 ? 83  ASP C OD1 1 
ATOM   2839  O  OD2 . ASP C  1 83  ? 0.576   102.255 91.526  1.00 45.92 ? 83  ASP C OD2 1 
ATOM   2840  N  N   . LEU C  1 84  ? 3.550   97.215  91.782  1.00 42.15 ? 84  LEU C N   1 
ATOM   2841  C  CA  . LEU C  1 84  ? 3.734   95.931  92.454  1.00 46.55 ? 84  LEU C CA  1 
ATOM   2842  C  C   . LEU C  1 84  ? 4.433   96.050  93.819  1.00 50.58 ? 84  LEU C C   1 
ATOM   2843  O  O   . LEU C  1 84  ? 5.087   95.101  94.276  1.00 48.68 ? 84  LEU C O   1 
ATOM   2844  C  CB  . LEU C  1 84  ? 4.490   94.951  91.553  1.00 46.82 ? 84  LEU C CB  1 
ATOM   2845  C  CG  . LEU C  1 84  ? 3.617   94.343  90.449  1.00 49.96 ? 84  LEU C CG  1 
ATOM   2846  C  CD1 . LEU C  1 84  ? 4.117   94.770  89.087  1.00 45.20 ? 84  LEU C CD1 1 
ATOM   2847  C  CD2 . LEU C  1 84  ? 3.557   92.817  90.561  1.00 44.06 ? 84  LEU C CD2 1 
ATOM   2848  N  N   . GLY C  1 85  ? 4.286   97.216  94.455  1.00 50.84 ? 85  GLY C N   1 
ATOM   2849  C  CA  . GLY C  1 85  ? 4.808   97.465  95.790  1.00 51.92 ? 85  GLY C CA  1 
ATOM   2850  C  C   . GLY C  1 85  ? 6.309   97.319  95.951  1.00 56.58 ? 85  GLY C C   1 
ATOM   2851  O  O   . GLY C  1 85  ? 7.083   97.961  95.237  1.00 56.40 ? 85  GLY C O   1 
ATOM   2852  N  N   . ASN C  1 86  ? 6.719   96.471  96.892  1.00 52.18 ? 86  ASN C N   1 
ATOM   2853  C  CA  . ASN C  1 86  ? 8.131   96.334  97.238  1.00 53.86 ? 86  ASN C CA  1 
ATOM   2854  C  C   . ASN C  1 86  ? 8.639   94.901  97.146  1.00 52.09 ? 86  ASN C C   1 
ATOM   2855  O  O   . ASN C  1 86  ? 7.865   93.950  97.256  1.00 48.10 ? 86  ASN C O   1 
ATOM   2856  C  CB  . ASN C  1 86  ? 8.411   96.887  98.650  1.00 52.27 ? 86  ASN C CB  1 
ATOM   2857  C  CG  . ASN C  1 86  ? 8.124   98.381  98.768  1.00 55.97 ? 86  ASN C CG  1 
ATOM   2858  O  OD1 . ASN C  1 86  ? 8.865   99.214  98.237  1.00 54.21 ? 86  ASN C OD1 1 
ATOM   2859  N  ND2 . ASN C  1 86  ? 7.050   98.726  99.476  1.00 57.08 ? 86  ASN C ND2 1 
ATOM   2860  N  N   . VAL C  1 87  ? 9.942   94.754  96.927  1.00 50.08 ? 87  VAL C N   1 
ATOM   2861  C  CA  . VAL C  1 87  ? 10.606  93.466  97.099  1.00 51.40 ? 87  VAL C CA  1 
ATOM   2862  C  C   . VAL C  1 87  ? 11.488  93.574  98.327  1.00 54.69 ? 87  VAL C C   1 
ATOM   2863  O  O   . VAL C  1 87  ? 11.723  94.679  98.812  1.00 53.74 ? 87  VAL C O   1 
ATOM   2864  C  CB  . VAL C  1 87  ? 11.478  93.088  95.898  1.00 46.79 ? 87  VAL C CB  1 
ATOM   2865  C  CG1 . VAL C  1 87  ? 10.614  92.616  94.739  1.00 51.33 ? 87  VAL C CG1 1 
ATOM   2866  C  CG2 . VAL C  1 87  ? 12.355  94.260  95.501  1.00 50.16 ? 87  VAL C CG2 1 
ATOM   2867  N  N   . THR C  1 88  ? 11.990  92.444  98.820  1.00 55.64 ? 88  THR C N   1 
ATOM   2868  C  CA  . THR C  1 88  ? 12.747  92.451  100.073 1.00 59.04 ? 88  THR C CA  1 
ATOM   2869  C  C   . THR C  1 88  ? 14.161  91.895  99.972  1.00 54.93 ? 88  THR C C   1 
ATOM   2870  O  O   . THR C  1 88  ? 14.370  90.690  99.809  1.00 51.83 ? 88  THR C O   1 
ATOM   2871  C  CB  . THR C  1 88  ? 11.993  91.723  101.190 1.00 59.47 ? 88  THR C CB  1 
ATOM   2872  O  OG1 . THR C  1 88  ? 10.794  92.445  101.487 1.00 55.33 ? 88  THR C OG1 1 
ATOM   2873  C  CG2 . THR C  1 88  ? 12.854  91.637  102.447 1.00 59.15 ? 88  THR C CG2 1 
ATOM   2874  N  N   . ALA C  1 89  ? 15.129  92.796  100.091 1.00 55.22 ? 89  ALA C N   1 
ATOM   2875  C  CA  . ALA C  1 89  ? 16.535  92.420  100.062 1.00 61.78 ? 89  ALA C CA  1 
ATOM   2876  C  C   . ALA C  1 89  ? 17.015  91.991  101.446 1.00 65.58 ? 89  ALA C C   1 
ATOM   2877  O  O   . ALA C  1 89  ? 16.909  92.744  102.418 1.00 61.09 ? 89  ALA C O   1 
ATOM   2878  C  CB  . ALA C  1 89  ? 17.375  93.570  99.546  1.00 57.59 ? 89  ALA C CB  1 
ATOM   2879  N  N   . ASP C  1 90  ? 17.543  90.775  101.523 1.00 64.23 ? 90  ASP C N   1 
ATOM   2880  C  CA  . ASP C  1 90  ? 18.096  90.259  102.765 1.00 65.65 ? 90  ASP C CA  1 
ATOM   2881  C  C   . ASP C  1 90  ? 19.498  90.823  103.012 1.00 70.43 ? 90  ASP C C   1 
ATOM   2882  O  O   . ASP C  1 90  ? 19.883  91.840  102.430 1.00 68.01 ? 90  ASP C O   1 
ATOM   2883  C  CB  . ASP C  1 90  ? 18.142  88.732  102.727 1.00 65.10 ? 90  ASP C CB  1 
ATOM   2884  C  CG  . ASP C  1 90  ? 18.965  88.203  101.567 1.00 63.92 ? 90  ASP C CG  1 
ATOM   2885  O  OD1 . ASP C  1 90  ? 19.642  89.010  100.897 1.00 62.33 ? 90  ASP C OD1 1 
ATOM   2886  O  OD2 . ASP C  1 90  ? 18.938  86.978  101.321 1.00 63.59 ? 90  ASP C OD2 1 
ATOM   2887  N  N   . LYS C  1 91  ? 20.263  90.131  103.854 1.00 72.96 ? 91  LYS C N   1 
ATOM   2888  C  CA  . LYS C  1 91  ? 21.600  90.572  104.251 1.00 72.99 ? 91  LYS C CA  1 
ATOM   2889  C  C   . LYS C  1 91  ? 22.654  90.387  103.155 1.00 71.21 ? 91  LYS C C   1 
ATOM   2890  O  O   . LYS C  1 91  ? 23.529  91.241  102.976 1.00 67.63 ? 91  LYS C O   1 
ATOM   2891  C  CB  . LYS C  1 91  ? 22.041  89.880  105.552 1.00 68.07 ? 91  LYS C CB  1 
ATOM   2892  C  CG  . LYS C  1 91  ? 22.272  88.361  105.448 1.00 72.02 ? 91  LYS C CG  1 
ATOM   2893  C  CD  . LYS C  1 91  ? 20.975  87.553  105.531 1.00 67.50 ? 91  LYS C CD  1 
ATOM   2894  C  CE  . LYS C  1 91  ? 21.252  86.054  105.566 1.00 66.42 ? 91  LYS C CE  1 
ATOM   2895  N  NZ  . LYS C  1 91  ? 21.966  85.635  106.815 1.00 54.78 ? 91  LYS C NZ  1 
ATOM   2896  N  N   . ASP C  1 92  ? 22.578  89.282  102.419 1.00 67.75 ? 92  ASP C N   1 
ATOM   2897  C  CA  . ASP C  1 92  ? 23.546  89.058  101.351 1.00 71.87 ? 92  ASP C CA  1 
ATOM   2898  C  C   . ASP C  1 92  ? 23.137  89.755  100.041 1.00 67.92 ? 92  ASP C C   1 
ATOM   2899  O  O   . ASP C  1 92  ? 23.763  89.557  98.997  1.00 61.75 ? 92  ASP C O   1 
ATOM   2900  C  CB  . ASP C  1 92  ? 23.863  87.562  101.162 1.00 72.36 ? 92  ASP C CB  1 
ATOM   2901  C  CG  . ASP C  1 92  ? 22.688  86.762  100.608 1.00 76.54 ? 92  ASP C CG  1 
ATOM   2902  O  OD1 . ASP C  1 92  ? 21.549  87.264  100.618 1.00 70.49 ? 92  ASP C OD1 1 
ATOM   2903  O  OD2 . ASP C  1 92  ? 22.910  85.613  100.167 1.00 74.84 ? 92  ASP C OD2 1 
ATOM   2904  N  N   . GLY C  1 93  ? 22.092  90.578  100.115 1.00 64.34 ? 93  GLY C N   1 
ATOM   2905  C  CA  . GLY C  1 93  ? 21.729  91.466  99.022  1.00 61.47 ? 93  GLY C CA  1 
ATOM   2906  C  C   . GLY C  1 93  ? 20.647  90.966  98.081  1.00 62.05 ? 93  GLY C C   1 
ATOM   2907  O  O   . GLY C  1 93  ? 20.094  91.735  97.293  1.00 58.54 ? 93  GLY C O   1 
ATOM   2908  N  N   . VAL C  1 94  ? 20.344  89.676  98.174  1.00 61.59 ? 94  VAL C N   1 
ATOM   2909  C  CA  . VAL C  1 94  ? 19.418  89.004  97.265  1.00 58.29 ? 94  VAL C CA  1 
ATOM   2910  C  C   . VAL C  1 94  ? 17.952  89.209  97.672  1.00 58.26 ? 94  VAL C C   1 
ATOM   2911  O  O   . VAL C  1 94  ? 17.641  89.436  98.842  1.00 60.22 ? 94  VAL C O   1 
ATOM   2912  C  CB  . VAL C  1 94  ? 19.757  87.490  97.182  1.00 57.84 ? 94  VAL C CB  1 
ATOM   2913  C  CG1 . VAL C  1 94  ? 18.938  86.785  96.105  1.00 54.95 ? 94  VAL C CG1 1 
ATOM   2914  C  CG2 . VAL C  1 94  ? 21.249  87.302  96.929  1.00 52.30 ? 94  VAL C CG2 1 
ATOM   2915  N  N   . ALA C  1 95  ? 17.057  89.153  96.691  1.00 55.22 ? 95  ALA C N   1 
ATOM   2916  C  CA  . ALA C  1 95  ? 15.630  89.240  96.944  1.00 52.37 ? 95  ALA C CA  1 
ATOM   2917  C  C   . ALA C  1 95  ? 14.904  88.251  96.049  1.00 53.44 ? 95  ALA C C   1 
ATOM   2918  O  O   . ALA C  1 95  ? 14.663  88.537  94.878  1.00 53.96 ? 95  ALA C O   1 
ATOM   2919  C  CB  . ALA C  1 95  ? 15.133  90.653  96.683  1.00 52.89 ? 95  ALA C CB  1 
ATOM   2920  N  N   . ASP C  1 96  ? 14.570  87.084  96.593  1.00 55.07 ? 96  ASP C N   1 
ATOM   2921  C  CA  . ASP C  1 96  ? 13.854  86.066  95.826  1.00 53.80 ? 96  ASP C CA  1 
ATOM   2922  C  C   . ASP C  1 96  ? 12.391  86.450  95.689  1.00 52.87 ? 96  ASP C C   1 
ATOM   2923  O  O   . ASP C  1 96  ? 11.631  86.367  96.652  1.00 50.14 ? 96  ASP C O   1 
ATOM   2924  C  CB  . ASP C  1 96  ? 13.981  84.682  96.471  1.00 52.84 ? 96  ASP C CB  1 
ATOM   2925  C  CG  . ASP C  1 96  ? 15.387  84.104  96.356  1.00 61.65 ? 96  ASP C CG  1 
ATOM   2926  O  OD1 . ASP C  1 96  ? 16.018  84.243  95.284  1.00 59.65 ? 96  ASP C OD1 1 
ATOM   2927  O  OD2 . ASP C  1 96  ? 15.864  83.504  97.344  1.00 71.51 ? 96  ASP C OD2 1 
ATOM   2928  N  N   . VAL C  1 97  ? 12.004  86.865  94.483  1.00 49.69 ? 97  VAL C N   1 
ATOM   2929  C  CA  . VAL C  1 97  ? 10.660  87.387  94.245  1.00 48.33 ? 97  VAL C CA  1 
ATOM   2930  C  C   . VAL C  1 97  ? 9.649   86.265  94.052  1.00 43.39 ? 97  VAL C C   1 
ATOM   2931  O  O   . VAL C  1 97  ? 9.976   85.211  93.502  1.00 43.38 ? 97  VAL C O   1 
ATOM   2932  C  CB  . VAL C  1 97  ? 10.635  88.340  93.036  1.00 50.64 ? 97  VAL C CB  1 
ATOM   2933  C  CG1 . VAL C  1 97  ? 9.290   89.059  92.933  1.00 46.67 ? 97  VAL C CG1 1 
ATOM   2934  C  CG2 . VAL C  1 97  ? 11.771  89.351  93.147  1.00 50.90 ? 97  VAL C CG2 1 
ATOM   2935  N  N   . SER C  1 98  ? 8.441   86.490  94.560  1.00 44.87 ? 98  SER C N   1 
ATOM   2936  C  CA  . SER C  1 98  ? 7.315   85.583  94.385  1.00 44.27 ? 98  SER C CA  1 
ATOM   2937  C  C   . SER C  1 98  ? 6.025   86.320  94.735  1.00 52.42 ? 98  SER C C   1 
ATOM   2938  O  O   . SER C  1 98  ? 5.632   86.402  95.898  1.00 53.27 ? 98  SER C O   1 
ATOM   2939  C  CB  . SER C  1 98  ? 7.462   84.325  95.234  1.00 47.11 ? 98  SER C CB  1 
ATOM   2940  O  OG  . SER C  1 98  ? 6.286   83.536  95.155  1.00 52.03 ? 98  SER C OG  1 
ATOM   2941  N  N   . ILE C  1 99  ? 5.384   86.859  93.705  1.00 47.52 ? 99  ILE C N   1 
ATOM   2942  C  CA  . ILE C  1 99  ? 4.209   87.701  93.835  1.00 42.62 ? 99  ILE C CA  1 
ATOM   2943  C  C   . ILE C  1 99  ? 3.106   87.040  93.023  1.00 49.03 ? 99  ILE C C   1 
ATOM   2944  O  O   . ILE C  1 99  ? 3.392   86.335  92.054  1.00 47.51 ? 99  ILE C O   1 
ATOM   2945  C  CB  . ILE C  1 99  ? 4.506   89.120  93.249  1.00 45.25 ? 99  ILE C CB  1 
ATOM   2946  C  CG1 . ILE C  1 99  ? 5.265   89.988  94.252  1.00 53.19 ? 99  ILE C CG1 1 
ATOM   2947  C  CG2 . ILE C  1 99  ? 3.243   89.849  92.823  1.00 44.30 ? 99  ILE C CG2 1 
ATOM   2948  C  CD1 . ILE C  1 99  ? 5.431   91.424  93.791  1.00 44.03 ? 99  ILE C CD1 1 
ATOM   2949  N  N   . GLU C  1 100 ? 1.852   87.227  93.420  1.00 43.08 ? 100 GLU C N   1 
ATOM   2950  C  CA  . GLU C  1 100 ? 0.751   86.887  92.537  1.00 44.63 ? 100 GLU C CA  1 
ATOM   2951  C  C   . GLU C  1 100 ? -0.191  88.069  92.445  1.00 44.65 ? 100 GLU C C   1 
ATOM   2952  O  O   . GLU C  1 100 ? -0.886  88.388  93.405  1.00 48.84 ? 100 GLU C O   1 
ATOM   2953  C  CB  . GLU C  1 100 ? 0.008   85.643  93.007  1.00 44.99 ? 100 GLU C CB  1 
ATOM   2954  C  CG  . GLU C  1 100 ? -1.190  85.339  92.136  1.00 46.09 ? 100 GLU C CG  1 
ATOM   2955  C  CD  . GLU C  1 100 ? -1.870  84.028  92.481  1.00 50.20 ? 100 GLU C CD  1 
ATOM   2956  O  OE1 . GLU C  1 100 ? -1.179  82.981  92.516  1.00 49.12 ? 100 GLU C OE1 1 
ATOM   2957  O  OE2 . GLU C  1 100 ? -3.102  84.050  92.709  1.00 52.46 ? 100 GLU C OE2 1 
ATOM   2958  N  N   . ASP C  1 101 ? -0.198  88.729  91.292  1.00 38.80 ? 101 ASP C N   1 
ATOM   2959  C  CA  . ASP C  1 101 ? -1.016  89.918  91.105  1.00 34.60 ? 101 ASP C CA  1 
ATOM   2960  C  C   . ASP C  1 101 ? -2.107  89.645  90.071  1.00 38.28 ? 101 ASP C C   1 
ATOM   2961  O  O   . ASP C  1 101 ? -1.905  88.875  89.136  1.00 44.49 ? 101 ASP C O   1 
ATOM   2962  C  CB  . ASP C  1 101 ? -0.140  91.101  90.703  1.00 33.75 ? 101 ASP C CB  1 
ATOM   2963  C  CG  . ASP C  1 101 ? -0.931  92.384  90.530  1.00 46.22 ? 101 ASP C CG  1 
ATOM   2964  O  OD1 . ASP C  1 101 ? -1.546  92.555  89.452  1.00 43.26 ? 101 ASP C OD1 1 
ATOM   2965  O  OD2 . ASP C  1 101 ? -0.935  93.223  91.462  1.00 46.30 ? 101 ASP C OD2 1 
ATOM   2966  N  N   . SER C  1 102 ? -3.265  90.272  90.240  1.00 36.73 ? 102 SER C N   1 
ATOM   2967  C  CA  . SER C  1 102 ? -4.412  89.990  89.389  1.00 37.96 ? 102 SER C CA  1 
ATOM   2968  C  C   . SER C  1 102 ? -4.966  91.231  88.689  1.00 36.70 ? 102 SER C C   1 
ATOM   2969  O  O   . SER C  1 102 ? -6.080  91.205  88.177  1.00 40.75 ? 102 SER C O   1 
ATOM   2970  C  CB  . SER C  1 102 ? -5.511  89.320  90.211  1.00 43.76 ? 102 SER C CB  1 
ATOM   2971  O  OG  . SER C  1 102 ? -4.952  88.425  91.163  1.00 50.59 ? 102 SER C OG  1 
ATOM   2972  N  N   . VAL C  1 103 ? -4.193  92.312  88.671  1.00 36.75 ? 103 VAL C N   1 
ATOM   2973  C  CA  . VAL C  1 103 ? -4.553  93.504  87.895  1.00 41.34 ? 103 VAL C CA  1 
ATOM   2974  C  C   . VAL C  1 103 ? -3.603  93.702  86.690  1.00 41.97 ? 103 VAL C C   1 
ATOM   2975  O  O   . VAL C  1 103 ? -3.993  94.263  85.655  1.00 42.57 ? 103 VAL C O   1 
ATOM   2976  C  CB  . VAL C  1 103 ? -4.620  94.766  88.792  1.00 44.77 ? 103 VAL C CB  1 
ATOM   2977  C  CG1 . VAL C  1 103 ? -3.400  94.851  89.629  1.00 46.76 ? 103 VAL C CG1 1 
ATOM   2978  C  CG2 . VAL C  1 103 ? -4.790  96.049  87.974  1.00 42.39 ? 103 VAL C CG2 1 
ATOM   2979  N  N   . ILE C  1 104 ? -2.367  93.224  86.811  1.00 41.98 ? 104 ILE C N   1 
ATOM   2980  C  CA  . ILE C  1 104 ? -1.494  93.139  85.641  1.00 42.42 ? 104 ILE C CA  1 
ATOM   2981  C  C   . ILE C  1 104 ? -1.879  91.916  84.804  1.00 40.02 ? 104 ILE C C   1 
ATOM   2982  O  O   . ILE C  1 104 ? -2.424  90.940  85.321  1.00 40.90 ? 104 ILE C O   1 
ATOM   2983  C  CB  . ILE C  1 104 ? 0.003   93.040  86.005  1.00 35.83 ? 104 ILE C CB  1 
ATOM   2984  C  CG1 . ILE C  1 104 ? 0.345   91.660  86.567  1.00 33.90 ? 104 ILE C CG1 1 
ATOM   2985  C  CG2 . ILE C  1 104 ? 0.409   94.166  86.947  1.00 46.44 ? 104 ILE C CG2 1 
ATOM   2986  C  CD1 . ILE C  1 104 ? 1.836   91.422  86.698  1.00 31.13 ? 104 ILE C CD1 1 
ATOM   2987  N  N   . SER C  1 105 ? -1.601  91.971  83.509  1.00 38.98 ? 105 SER C N   1 
ATOM   2988  C  CA  . SER C  1 105 ? -1.908  90.843  82.643  1.00 38.16 ? 105 SER C CA  1 
ATOM   2989  C  C   . SER C  1 105 ? -0.868  90.727  81.549  1.00 33.89 ? 105 SER C C   1 
ATOM   2990  O  O   . SER C  1 105 ? -0.281  91.723  81.130  1.00 37.38 ? 105 SER C O   1 
ATOM   2991  C  CB  . SER C  1 105 ? -3.298  90.997  82.025  1.00 35.27 ? 105 SER C CB  1 
ATOM   2992  O  OG  . SER C  1 105 ? -3.683  89.804  81.369  1.00 36.54 ? 105 SER C OG  1 
ATOM   2993  N  N   . LEU C  1 106 ? -0.638  89.508  81.083  1.00 33.81 ? 106 LEU C N   1 
ATOM   2994  C  CA  . LEU C  1 106 ? 0.266   89.307  79.960  1.00 36.79 ? 106 LEU C CA  1 
ATOM   2995  C  C   . LEU C  1 106 ? -0.447  89.441  78.605  1.00 37.45 ? 106 LEU C C   1 
ATOM   2996  O  O   . LEU C  1 106 ? 0.127   89.136  77.562  1.00 37.31 ? 106 LEU C O   1 
ATOM   2997  C  CB  . LEU C  1 106 ? 0.971   87.958  80.086  1.00 32.40 ? 106 LEU C CB  1 
ATOM   2998  C  CG  . LEU C  1 106 ? 1.754   87.837  81.397  1.00 31.46 ? 106 LEU C CG  1 
ATOM   2999  C  CD1 . LEU C  1 106 ? 2.532   86.538  81.445  1.00 25.27 ? 106 LEU C CD1 1 
ATOM   3000  C  CD2 . LEU C  1 106 ? 2.671   89.039  81.587  1.00 28.57 ? 106 LEU C CD2 1 
ATOM   3001  N  N   . SER C  1 107 ? -1.689  89.915  78.625  1.00 35.07 ? 107 SER C N   1 
ATOM   3002  C  CA  . SER C  1 107 ? -2.478  90.023  77.406  1.00 36.06 ? 107 SER C CA  1 
ATOM   3003  C  C   . SER C  1 107 ? -3.565  91.094  77.505  1.00 38.76 ? 107 SER C C   1 
ATOM   3004  O  O   . SER C  1 107 ? -3.826  91.656  78.576  1.00 33.00 ? 107 SER C O   1 
ATOM   3005  C  CB  . SER C  1 107 ? -3.131  88.682  77.089  1.00 37.19 ? 107 SER C CB  1 
ATOM   3006  O  OG  . SER C  1 107 ? -4.287  88.506  77.885  1.00 33.12 ? 107 SER C OG  1 
ATOM   3007  N  N   . GLY C  1 108 ? -4.210  91.359  76.375  1.00 33.76 ? 108 GLY C N   1 
ATOM   3008  C  CA  . GLY C  1 108 ? -5.252  92.363  76.325  1.00 37.17 ? 108 GLY C CA  1 
ATOM   3009  C  C   . GLY C  1 108 ? -4.626  93.715  76.087  1.00 42.27 ? 108 GLY C C   1 
ATOM   3010  O  O   . GLY C  1 108 ? -3.401  93.828  76.052  1.00 43.62 ? 108 GLY C O   1 
ATOM   3011  N  N   . ASP C  1 109 ? -5.459  94.743  75.950  1.00 47.79 ? 109 ASP C N   1 
ATOM   3012  C  CA  . ASP C  1 109 ? -4.985  96.068  75.554  1.00 49.60 ? 109 ASP C CA  1 
ATOM   3013  C  C   . ASP C  1 109 ? -4.035  96.678  76.580  1.00 49.63 ? 109 ASP C C   1 
ATOM   3014  O  O   . ASP C  1 109 ? -3.064  97.358  76.230  1.00 52.42 ? 109 ASP C O   1 
ATOM   3015  C  CB  . ASP C  1 109 ? -6.169  97.013  75.315  1.00 55.07 ? 109 ASP C CB  1 
ATOM   3016  C  CG  . ASP C  1 109 ? -7.108  96.519  74.225  1.00 58.27 ? 109 ASP C CG  1 
ATOM   3017  O  OD1 . ASP C  1 109 ? -6.633  95.875  73.260  1.00 59.94 ? 109 ASP C OD1 1 
ATOM   3018  O  OD2 . ASP C  1 109 ? -8.326  96.781  74.337  1.00 55.11 ? 109 ASP C OD2 1 
ATOM   3019  N  N   . HIS C  1 110 ? -4.317  96.427  77.850  1.00 49.49 ? 110 HIS C N   1 
ATOM   3020  C  CA  . HIS C  1 110 ? -3.566  97.050  78.931  1.00 46.45 ? 110 HIS C CA  1 
ATOM   3021  C  C   . HIS C  1 110 ? -2.504  96.103  79.497  1.00 44.58 ? 110 HIS C C   1 
ATOM   3022  O  O   . HIS C  1 110 ? -2.244  96.115  80.702  1.00 41.97 ? 110 HIS C O   1 
ATOM   3023  C  CB  . HIS C  1 110 ? -4.534  97.476  80.032  1.00 45.49 ? 110 HIS C CB  1 
ATOM   3024  C  CG  . HIS C  1 110 ? -5.718  98.246  79.530  1.00 47.87 ? 110 HIS C CG  1 
ATOM   3025  N  ND1 . HIS C  1 110 ? -5.787  99.622  79.577  1.00 48.65 ? 110 HIS C ND1 1 
ATOM   3026  C  CD2 . HIS C  1 110 ? -6.879  97.832  78.971  1.00 53.79 ? 110 HIS C CD2 1 
ATOM   3027  C  CE1 . HIS C  1 110 ? -6.938  100.023 79.069  1.00 51.08 ? 110 HIS C CE1 1 
ATOM   3028  N  NE2 . HIS C  1 110 ? -7.620  98.955  78.694  1.00 54.88 ? 110 HIS C NE2 1 
ATOM   3029  N  N   . CYS C  1 111 ? -1.883  95.298  78.630  1.00 41.67 ? 111 CYS C N   1 
ATOM   3030  C  CA  . CYS C  1 111 ? -0.929  94.281  79.086  1.00 38.08 ? 111 CYS C CA  1 
ATOM   3031  C  C   . CYS C  1 111 ? 0.464   94.859  79.302  1.00 37.79 ? 111 CYS C C   1 
ATOM   3032  O  O   . CYS C  1 111 ? 0.729   96.008  78.943  1.00 37.61 ? 111 CYS C O   1 
ATOM   3033  C  CB  . CYS C  1 111 ? -0.882  93.085  78.128  1.00 40.03 ? 111 CYS C CB  1 
ATOM   3034  S  SG  . CYS C  1 111 ? 0.207   93.234  76.686  1.00 38.92 ? 111 CYS C SG  1 
ATOM   3035  N  N   . ILE C  1 112 ? 1.355   94.059  79.885  1.00 36.63 ? 112 ILE C N   1 
ATOM   3036  C  CA  . ILE C  1 112 ? 2.672   94.562  80.286  1.00 38.28 ? 112 ILE C CA  1 
ATOM   3037  C  C   . ILE C  1 112 ? 3.831   94.053  79.414  1.00 29.71 ? 112 ILE C C   1 
ATOM   3038  O  O   . ILE C  1 112 ? 4.977   94.476  79.579  1.00 27.28 ? 112 ILE C O   1 
ATOM   3039  C  CB  . ILE C  1 112 ? 2.950   94.286  81.783  1.00 33.47 ? 112 ILE C CB  1 
ATOM   3040  C  CG1 . ILE C  1 112 ? 3.099   92.785  82.034  1.00 31.08 ? 112 ILE C CG1 1 
ATOM   3041  C  CG2 . ILE C  1 112 ? 1.841   94.878  82.639  1.00 32.51 ? 112 ILE C CG2 1 
ATOM   3042  C  CD1 . ILE C  1 112 ? 3.600   92.450  83.423  1.00 32.94 ? 112 ILE C CD1 1 
ATOM   3043  N  N   . ILE C  1 113 ? 3.522   93.144  78.496  1.00 35.01 ? 113 ILE C N   1 
ATOM   3044  C  CA  . ILE C  1 113 ? 4.456   92.760  77.442  1.00 28.81 ? 113 ILE C CA  1 
ATOM   3045  C  C   . ILE C  1 113 ? 4.965   94.013  76.741  1.00 25.29 ? 113 ILE C C   1 
ATOM   3046  O  O   . ILE C  1 113 ? 4.191   94.886  76.378  1.00 28.24 ? 113 ILE C O   1 
ATOM   3047  C  CB  . ILE C  1 113 ? 3.786   91.838  76.430  1.00 27.00 ? 113 ILE C CB  1 
ATOM   3048  C  CG1 . ILE C  1 113 ? 3.342   90.557  77.125  1.00 24.74 ? 113 ILE C CG1 1 
ATOM   3049  C  CG2 . ILE C  1 113 ? 4.744   91.515  75.278  1.00 24.73 ? 113 ILE C CG2 1 
ATOM   3050  C  CD1 . ILE C  1 113 ? 4.490   89.834  77.810  1.00 29.15 ? 113 ILE C CD1 1 
ATOM   3051  N  N   . GLY C  1 114 ? 6.277   94.133  76.610  1.00 24.37 ? 114 GLY C N   1 
ATOM   3052  C  CA  . GLY C  1 114 ? 6.849   95.307  75.983  1.00 25.64 ? 114 GLY C CA  1 
ATOM   3053  C  C   . GLY C  1 114 ? 6.933   96.547  76.858  1.00 30.21 ? 114 GLY C C   1 
ATOM   3054  O  O   . GLY C  1 114 ? 7.172   97.649  76.359  1.00 27.71 ? 114 GLY C O   1 
ATOM   3055  N  N   . ARG C  1 115 ? 6.743   96.385  78.165  1.00 32.70 ? 115 ARG C N   1 
ATOM   3056  C  CA  . ARG C  1 115 ? 6.915   97.513  79.067  1.00 33.38 ? 115 ARG C CA  1 
ATOM   3057  C  C   . ARG C  1 115 ? 8.114   97.270  79.977  1.00 36.32 ? 115 ARG C C   1 
ATOM   3058  O  O   . ARG C  1 115 ? 8.712   96.191  79.971  1.00 36.10 ? 115 ARG C O   1 
ATOM   3059  C  CB  . ARG C  1 115 ? 5.646   97.784  79.868  1.00 31.55 ? 115 ARG C CB  1 
ATOM   3060  C  CG  . ARG C  1 115 ? 4.376   97.621  79.065  1.00 36.24 ? 115 ARG C CG  1 
ATOM   3061  C  CD  . ARG C  1 115 ? 3.537   98.871  79.116  1.00 36.63 ? 115 ARG C CD  1 
ATOM   3062  N  NE  . ARG C  1 115 ? 2.246   98.705  78.455  1.00 31.86 ? 115 ARG C NE  1 
ATOM   3063  C  CZ  . ARG C  1 115 ? 1.611   99.676  77.808  1.00 35.06 ? 115 ARG C CZ  1 
ATOM   3064  N  NH1 . ARG C  1 115 ? 2.153   100.886 77.716  1.00 37.81 ? 115 ARG C NH1 1 
ATOM   3065  N  NH2 . ARG C  1 115 ? 0.437   99.434  77.243  1.00 34.47 ? 115 ARG C NH2 1 
ATOM   3066  N  N   . THR C  1 116 ? 8.475   98.286  80.745  1.00 39.62 ? 116 THR C N   1 
ATOM   3067  C  CA  . THR C  1 116 ? 9.691   98.224  81.536  1.00 38.03 ? 116 THR C CA  1 
ATOM   3068  C  C   . THR C  1 116 ? 9.423   97.934  83.017  1.00 42.93 ? 116 THR C C   1 
ATOM   3069  O  O   . THR C  1 116 ? 8.684   98.661  83.696  1.00 38.38 ? 116 THR C O   1 
ATOM   3070  C  CB  . THR C  1 116 ? 10.513  99.507  81.369  1.00 43.27 ? 116 THR C CB  1 
ATOM   3071  O  OG1 . THR C  1 116 ? 11.045  99.556  80.036  1.00 40.20 ? 116 THR C OG1 1 
ATOM   3072  C  CG2 . THR C  1 116 ? 11.647  99.552  82.370  1.00 39.33 ? 116 THR C CG2 1 
ATOM   3073  N  N   . LEU C  1 117 ? 10.010  96.838  83.486  1.00 39.78 ? 117 LEU C N   1 
ATOM   3074  C  CA  . LEU C  1 117 ? 9.980   96.469  84.886  1.00 42.98 ? 117 LEU C CA  1 
ATOM   3075  C  C   . LEU C  1 117 ? 11.193  97.081  85.575  1.00 49.38 ? 117 LEU C C   1 
ATOM   3076  O  O   . LEU C  1 117 ? 12.306  96.979  85.062  1.00 45.71 ? 117 LEU C O   1 
ATOM   3077  C  CB  . LEU C  1 117 ? 10.046  94.953  85.019  1.00 41.91 ? 117 LEU C CB  1 
ATOM   3078  C  CG  . LEU C  1 117 ? 10.195  94.469  86.460  1.00 41.91 ? 117 LEU C CG  1 
ATOM   3079  C  CD1 . LEU C  1 117 ? 9.021   94.970  87.275  1.00 40.77 ? 117 LEU C CD1 1 
ATOM   3080  C  CD2 . LEU C  1 117 ? 10.309  92.950  86.527  1.00 40.53 ? 117 LEU C CD2 1 
ATOM   3081  N  N   . VAL C  1 118 ? 10.993  97.710  86.733  1.00 48.86 ? 118 VAL C N   1 
ATOM   3082  C  CA  . VAL C  1 118 ? 12.111  98.339  87.441  1.00 50.18 ? 118 VAL C CA  1 
ATOM   3083  C  C   . VAL C  1 118 ? 12.225  97.943  88.918  1.00 54.03 ? 118 VAL C C   1 
ATOM   3084  O  O   . VAL C  1 118 ? 11.242  97.562  89.557  1.00 54.90 ? 118 VAL C O   1 
ATOM   3085  C  CB  . VAL C  1 118 ? 12.039  99.880  87.371  1.00 53.94 ? 118 VAL C CB  1 
ATOM   3086  C  CG1 . VAL C  1 118 ? 11.904  100.356 85.931  1.00 51.53 ? 118 VAL C CG1 1 
ATOM   3087  C  CG2 . VAL C  1 118 ? 10.881  100.384 88.210  1.00 56.41 ? 118 VAL C CG2 1 
ATOM   3088  N  N   . VAL C  1 119 ? 13.438  98.043  89.450  1.00 52.83 ? 119 VAL C N   1 
ATOM   3089  C  CA  . VAL C  1 119 ? 13.662  97.921  90.886  1.00 53.37 ? 119 VAL C CA  1 
ATOM   3090  C  C   . VAL C  1 119 ? 14.364  99.188  91.406  1.00 54.13 ? 119 VAL C C   1 
ATOM   3091  O  O   . VAL C  1 119 ? 15.327  99.670  90.800  1.00 52.17 ? 119 VAL C O   1 
ATOM   3092  C  CB  . VAL C  1 119 ? 14.447  96.637  91.226  1.00 49.47 ? 119 VAL C CB  1 
ATOM   3093  C  CG1 . VAL C  1 119 ? 15.797  96.633  90.547  1.00 42.45 ? 119 VAL C CG1 1 
ATOM   3094  C  CG2 . VAL C  1 119 ? 14.584  96.477  92.730  1.00 55.16 ? 119 VAL C CG2 1 
ATOM   3095  N  N   . HIS C  1 120 ? 13.866  99.738  92.511  1.00 59.16 ? 120 HIS C N   1 
ATOM   3096  C  CA  . HIS C  1 120 ? 14.326  101.046 93.001  1.00 60.20 ? 120 HIS C CA  1 
ATOM   3097  C  C   . HIS C  1 120 ? 15.306  100.992 94.170  1.00 60.42 ? 120 HIS C C   1 
ATOM   3098  O  O   . HIS C  1 120 ? 15.632  99.911  94.668  1.00 58.73 ? 120 HIS C O   1 
ATOM   3099  C  CB  . HIS C  1 120 ? 13.135  101.908 93.401  1.00 57.81 ? 120 HIS C CB  1 
ATOM   3100  C  CG  . HIS C  1 120 ? 12.260  102.297 92.255  1.00 58.26 ? 120 HIS C CG  1 
ATOM   3101  N  ND1 . HIS C  1 120 ? 12.271  103.562 91.709  1.00 58.55 ? 120 HIS C ND1 1 
ATOM   3102  C  CD2 . HIS C  1 120 ? 11.342  101.590 91.555  1.00 58.41 ? 120 HIS C CD2 1 
ATOM   3103  C  CE1 . HIS C  1 120 ? 11.398  103.617 90.718  1.00 61.19 ? 120 HIS C CE1 1 
ATOM   3104  N  NE2 . HIS C  1 120 ? 10.821  102.434 90.604  1.00 59.05 ? 120 HIS C NE2 1 
ATOM   3105  N  N   . GLU C  1 121 ? 15.768  102.164 94.612  1.00 61.80 ? 121 GLU C N   1 
ATOM   3106  C  CA  . GLU C  1 121 ? 16.673  102.219 95.763  1.00 64.83 ? 121 GLU C CA  1 
ATOM   3107  C  C   . GLU C  1 121 ? 15.920  102.072 97.088  1.00 64.91 ? 121 GLU C C   1 
ATOM   3108  O  O   . GLU C  1 121 ? 16.136  101.104 97.818  1.00 66.63 ? 121 GLU C O   1 
ATOM   3109  C  CB  . GLU C  1 121 ? 17.587  103.466 95.754  1.00 66.27 ? 121 GLU C CB  1 
ATOM   3110  C  CG  . GLU C  1 121 ? 16.890  104.836 95.750  1.00 68.44 ? 121 GLU C CG  1 
ATOM   3111  C  CD  . GLU C  1 121 ? 17.797  105.975 96.238  1.00 70.75 ? 121 GLU C CD  1 
ATOM   3112  O  OE1 . GLU C  1 121 ? 18.596  105.748 97.175  1.00 75.13 ? 121 GLU C OE1 1 
ATOM   3113  O  OE2 . GLU C  1 121 ? 17.710  107.101 95.692  1.00 63.42 ? 121 GLU C OE2 1 
ATOM   3114  N  N   . LYS C  1 122 ? 15.024  103.013 97.376  1.00 66.80 ? 122 LYS C N   1 
ATOM   3115  C  CA  . LYS C  1 122 ? 14.247  103.006 98.615  1.00 60.90 ? 122 LYS C CA  1 
ATOM   3116  C  C   . LYS C  1 122 ? 12.970  102.201 98.408  1.00 63.67 ? 122 LYS C C   1 
ATOM   3117  O  O   . LYS C  1 122 ? 12.687  101.742 97.299  1.00 61.88 ? 122 LYS C O   1 
ATOM   3118  C  CB  . LYS C  1 122 ? 13.886  104.437 99.031  1.00 60.21 ? 122 LYS C CB  1 
ATOM   3119  C  CG  . LYS C  1 122 ? 15.063  105.410 99.061  1.00 64.35 ? 122 LYS C CG  1 
ATOM   3120  C  CD  . LYS C  1 122 ? 14.606  106.870 99.192  1.00 60.20 ? 122 LYS C CD  1 
ATOM   3121  C  CE  . LYS C  1 122 ? 15.730  107.830 98.779  1.00 63.82 ? 122 LYS C CE  1 
ATOM   3122  N  NZ  . LYS C  1 122 ? 15.332  109.271 98.712  1.00 57.72 ? 122 LYS C NZ  1 
ATOM   3123  N  N   . ALA C  1 123 ? 12.191  102.038 99.471  1.00 60.92 ? 123 ALA C N   1 
ATOM   3124  C  CA  . ALA C  1 123 ? 10.933  101.314 99.365  1.00 58.18 ? 123 ALA C CA  1 
ATOM   3125  C  C   . ALA C  1 123 ? 9.805   102.207 98.865  1.00 60.32 ? 123 ALA C C   1 
ATOM   3126  O  O   . ALA C  1 123 ? 10.000  103.387 98.565  1.00 57.87 ? 123 ALA C O   1 
ATOM   3127  C  CB  . ALA C  1 123 ? 10.561  100.676 100.693 1.00 56.06 ? 123 ALA C CB  1 
ATOM   3128  N  N   . ASP C  1 124 ? 8.619   101.622 98.783  1.00 58.58 ? 124 ASP C N   1 
ATOM   3129  C  CA  . ASP C  1 124 ? 7.461   102.304 98.239  1.00 62.17 ? 124 ASP C CA  1 
ATOM   3130  C  C   . ASP C  1 124 ? 6.479   102.608 99.366  1.00 56.68 ? 124 ASP C C   1 
ATOM   3131  O  O   . ASP C  1 124 ? 5.987   101.695 100.034 1.00 46.70 ? 124 ASP C O   1 
ATOM   3132  C  CB  . ASP C  1 124 ? 6.819   101.411 97.168  1.00 60.20 ? 124 ASP C CB  1 
ATOM   3133  C  CG  . ASP C  1 124 ? 5.664   102.076 96.456  1.00 57.57 ? 124 ASP C CG  1 
ATOM   3134  O  OD1 . ASP C  1 124 ? 5.596   103.322 96.461  1.00 62.19 ? 124 ASP C OD1 1 
ATOM   3135  O  OD2 . ASP C  1 124 ? 4.827   101.347 95.879  1.00 60.57 ? 124 ASP C OD2 1 
ATOM   3136  N  N   . ASP C  1 125 ? 6.188   103.890 99.574  1.00 58.26 ? 125 ASP C N   1 
ATOM   3137  C  CA  . ASP C  1 125 ? 5.316   104.289 100.679 1.00 61.90 ? 125 ASP C CA  1 
ATOM   3138  C  C   . ASP C  1 125 ? 3.873   103.841 100.471 1.00 60.93 ? 125 ASP C C   1 
ATOM   3139  O  O   . ASP C  1 125 ? 3.042   103.973 101.362 1.00 58.33 ? 125 ASP C O   1 
ATOM   3140  C  CB  . ASP C  1 125 ? 5.417   105.799 100.988 1.00 64.93 ? 125 ASP C CB  1 
ATOM   3141  C  CG  . ASP C  1 125 ? 4.872   106.692 99.869  1.00 70.16 ? 125 ASP C CG  1 
ATOM   3142  O  OD1 . ASP C  1 125 ? 3.723   106.496 99.416  1.00 71.80 ? 125 ASP C OD1 1 
ATOM   3143  O  OD2 . ASP C  1 125 ? 5.596   107.623 99.456  1.00 71.67 ? 125 ASP C OD2 1 
ATOM   3144  N  N   . LEU C  1 126 ? 3.601   103.315 99.278  1.00 63.07 ? 126 LEU C N   1 
ATOM   3145  C  CA  . LEU C  1 126 ? 2.298   102.763 98.911  1.00 58.26 ? 126 LEU C CA  1 
ATOM   3146  C  C   . LEU C  1 126 ? 1.196   103.819 98.913  1.00 62.11 ? 126 LEU C C   1 
ATOM   3147  O  O   . LEU C  1 126 ? 0.016   103.497 99.074  1.00 63.74 ? 126 LEU C O   1 
ATOM   3148  C  CB  . LEU C  1 126 ? 1.930   101.569 99.801  1.00 53.38 ? 126 LEU C CB  1 
ATOM   3149  C  CG  . LEU C  1 126 ? 3.028   100.515 99.981  1.00 49.65 ? 126 LEU C CG  1 
ATOM   3150  C  CD1 . LEU C  1 126 ? 2.531   99.328  100.770 1.00 49.02 ? 126 LEU C CD1 1 
ATOM   3151  C  CD2 . LEU C  1 126 ? 3.576   100.056 98.638  1.00 57.74 ? 126 LEU C CD2 1 
ATOM   3152  N  N   . GLY C  1 127 ? 1.586   105.075 98.711  1.00 63.95 ? 127 GLY C N   1 
ATOM   3153  C  CA  . GLY C  1 127 ? 0.639   106.176 98.709  1.00 70.12 ? 127 GLY C CA  1 
ATOM   3154  C  C   . GLY C  1 127 ? 0.307   106.652 100.114 1.00 72.23 ? 127 GLY C C   1 
ATOM   3155  O  O   . GLY C  1 127 ? -0.647  107.406 100.321 1.00 70.31 ? 127 GLY C O   1 
ATOM   3156  N  N   . LYS C  1 128 ? 1.097   106.199 101.084 1.00 71.83 ? 128 LYS C N   1 
ATOM   3157  C  CA  . LYS C  1 128 ? 0.895   106.569 102.481 1.00 71.67 ? 128 LYS C CA  1 
ATOM   3158  C  C   . LYS C  1 128 ? 2.108   107.309 103.014 1.00 70.30 ? 128 LYS C C   1 
ATOM   3159  O  O   . LYS C  1 128 ? 2.845   106.798 103.859 1.00 70.50 ? 128 LYS C O   1 
ATOM   3160  C  CB  . LYS C  1 128 ? 0.618   105.331 103.334 1.00 65.05 ? 128 LYS C CB  1 
ATOM   3161  C  CG  . LYS C  1 128 ? -0.666  104.627 102.961 1.00 66.83 ? 128 LYS C CG  1 
ATOM   3162  C  CD  . LYS C  1 128 ? -1.803  105.628 102.819 1.00 68.27 ? 128 LYS C CD  1 
ATOM   3163  C  CE  . LYS C  1 128 ? -2.865  105.114 101.855 1.00 75.51 ? 128 LYS C CE  1 
ATOM   3164  N  NZ  . LYS C  1 128 ? -2.311  104.888 100.489 1.00 67.96 ? 128 LYS C NZ  1 
ATOM   3165  N  N   . GLY C  1 129 ? 2.312   108.518 102.507 1.00 69.86 ? 129 GLY C N   1 
ATOM   3166  C  CA  . GLY C  1 129 ? 3.467   109.301 102.887 1.00 73.67 ? 129 GLY C CA  1 
ATOM   3167  C  C   . GLY C  1 129 ? 3.119   110.764 103.016 1.00 76.88 ? 129 GLY C C   1 
ATOM   3168  O  O   . GLY C  1 129 ? 4.002   111.599 103.195 1.00 80.19 ? 129 GLY C O   1 
ATOM   3169  N  N   . GLY C  1 130 ? 1.831   111.078 102.908 1.00 75.65 ? 130 GLY C N   1 
ATOM   3170  C  CA  . GLY C  1 130 ? 1.359   112.441 103.081 1.00 77.27 ? 130 GLY C CA  1 
ATOM   3171  C  C   . GLY C  1 130 ? 1.769   113.401 101.976 1.00 82.95 ? 130 GLY C C   1 
ATOM   3172  O  O   . GLY C  1 130 ? 0.968   114.231 101.541 1.00 82.61 ? 130 GLY C O   1 
ATOM   3173  N  N   . ASN C  1 131 ? 3.019   113.297 101.527 1.00 85.57 ? 131 ASN C N   1 
ATOM   3174  C  CA  . ASN C  1 131 ? 3.538   114.155 100.459 1.00 84.58 ? 131 ASN C CA  1 
ATOM   3175  C  C   . ASN C  1 131 ? 2.900   113.872 99.094  1.00 82.08 ? 131 ASN C C   1 
ATOM   3176  O  O   . ASN C  1 131 ? 2.336   112.798 98.871  1.00 81.22 ? 131 ASN C O   1 
ATOM   3177  C  CB  . ASN C  1 131 ? 5.075   114.091 100.390 1.00 79.55 ? 131 ASN C CB  1 
ATOM   3178  C  CG  . ASN C  1 131 ? 5.612   112.667 100.341 1.00 79.90 ? 131 ASN C CG  1 
ATOM   3179  O  OD1 . ASN C  1 131 ? 5.711   112.068 99.270  1.00 79.50 ? 131 ASN C OD1 1 
ATOM   3180  N  ND2 . ASN C  1 131 ? 5.985   112.128 101.502 1.00 73.32 ? 131 ASN C ND2 1 
ATOM   3181  N  N   . GLU C  1 132 ? 2.986   114.841 98.188  1.00 80.59 ? 132 GLU C N   1 
ATOM   3182  C  CA  . GLU C  1 132 ? 2.292   114.745 96.905  1.00 82.99 ? 132 GLU C CA  1 
ATOM   3183  C  C   . GLU C  1 132 ? 3.030   113.889 95.874  1.00 83.26 ? 132 GLU C C   1 
ATOM   3184  O  O   . GLU C  1 132 ? 2.520   113.664 94.774  1.00 82.36 ? 132 GLU C O   1 
ATOM   3185  C  CB  . GLU C  1 132 ? 1.998   116.141 96.337  1.00 82.89 ? 132 GLU C CB  1 
ATOM   3186  C  CG  . GLU C  1 132 ? 0.543   116.361 95.910  1.00 81.03 ? 132 GLU C CG  1 
ATOM   3187  C  CD  . GLU C  1 132 ? -0.412  116.563 97.092  1.00 88.12 ? 132 GLU C CD  1 
ATOM   3188  O  OE1 . GLU C  1 132 ? 0.025   116.432 98.258  1.00 89.56 ? 132 GLU C OE1 1 
ATOM   3189  O  OE2 . GLU C  1 132 ? -1.605  116.861 96.856  1.00 84.00 ? 132 GLU C OE2 1 
ATOM   3190  N  N   . GLU C  1 133 ? 4.226   113.420 96.224  1.00 83.69 ? 133 GLU C N   1 
ATOM   3191  C  CA  . GLU C  1 133 ? 4.961   112.493 95.364  1.00 81.22 ? 133 GLU C CA  1 
ATOM   3192  C  C   . GLU C  1 133 ? 4.713   111.052 95.799  1.00 77.92 ? 133 GLU C C   1 
ATOM   3193  O  O   . GLU C  1 133 ? 5.128   110.108 95.126  1.00 76.30 ? 133 GLU C O   1 
ATOM   3194  C  CB  . GLU C  1 133 ? 6.463   112.800 95.350  1.00 80.98 ? 133 GLU C CB  1 
ATOM   3195  C  CG  . GLU C  1 133 ? 6.828   114.131 94.720  1.00 78.08 ? 133 GLU C CG  1 
ATOM   3196  C  CD  . GLU C  1 133 ? 6.972   115.237 95.745  1.00 77.59 ? 133 GLU C CD  1 
ATOM   3197  O  OE1 . GLU C  1 133 ? 7.531   114.967 96.830  1.00 76.15 ? 133 GLU C OE1 1 
ATOM   3198  O  OE2 . GLU C  1 133 ? 6.524   116.372 95.468  1.00 74.05 ? 133 GLU C OE2 1 
ATOM   3199  N  N   . SER C  1 134 ? 4.034   110.894 96.931  1.00 77.74 ? 134 SER C N   1 
ATOM   3200  C  CA  . SER C  1 134 ? 3.611   109.582 97.396  1.00 77.04 ? 134 SER C CA  1 
ATOM   3201  C  C   . SER C  1 134 ? 2.373   109.205 96.609  1.00 73.32 ? 134 SER C C   1 
ATOM   3202  O  O   . SER C  1 134 ? 1.932   108.056 96.620  1.00 71.55 ? 134 SER C O   1 
ATOM   3203  C  CB  . SER C  1 134 ? 3.278   109.625 98.887  1.00 77.62 ? 134 SER C CB  1 
ATOM   3204  O  OG  . SER C  1 134 ? 2.139   110.431 99.136  1.00 77.71 ? 134 SER C OG  1 
ATOM   3205  N  N   . THR C  1 135 ? 1.815   110.198 95.928  1.00 73.74 ? 135 THR C N   1 
ATOM   3206  C  CA  . THR C  1 135 ? 0.621   110.010 95.122  1.00 76.50 ? 135 THR C CA  1 
ATOM   3207  C  C   . THR C  1 135 ? 0.980   109.597 93.687  1.00 73.41 ? 135 THR C C   1 
ATOM   3208  O  O   . THR C  1 135 ? 0.129   109.120 92.935  1.00 72.31 ? 135 THR C O   1 
ATOM   3209  C  CB  . THR C  1 135 ? -0.260  111.289 95.128  1.00 80.06 ? 135 THR C CB  1 
ATOM   3210  O  OG1 . THR C  1 135 ? -1.634  110.931 95.332  1.00 75.78 ? 135 THR C OG1 1 
ATOM   3211  C  CG2 . THR C  1 135 ? -0.112  112.083 93.824  1.00 76.97 ? 135 THR C CG2 1 
ATOM   3212  N  N   . LYS C  1 136 ? 2.245   109.764 93.314  1.00 72.41 ? 136 LYS C N   1 
ATOM   3213  C  CA  . LYS C  1 136 ? 2.676   109.386 91.970  1.00 70.95 ? 136 LYS C CA  1 
ATOM   3214  C  C   . LYS C  1 136 ? 3.674   108.231 91.945  1.00 67.05 ? 136 LYS C C   1 
ATOM   3215  O  O   . LYS C  1 136 ? 3.509   107.277 91.185  1.00 68.53 ? 136 LYS C O   1 
ATOM   3216  C  CB  . LYS C  1 136 ? 3.248   110.586 91.209  1.00 73.79 ? 136 LYS C CB  1 
ATOM   3217  C  CG  . LYS C  1 136 ? 3.511   111.815 92.056  1.00 77.25 ? 136 LYS C CG  1 
ATOM   3218  C  CD  . LYS C  1 136 ? 3.780   113.027 91.177  1.00 76.81 ? 136 LYS C CD  1 
ATOM   3219  C  CE  . LYS C  1 136 ? 2.672   113.211 90.147  1.00 75.49 ? 136 LYS C CE  1 
ATOM   3220  N  NZ  . LYS C  1 136 ? 1.317   113.150 90.767  1.00 68.54 ? 136 LYS C NZ  1 
ATOM   3221  N  N   . THR C  1 137 ? 4.710   108.316 92.767  1.00 62.75 ? 137 THR C N   1 
ATOM   3222  C  CA  . THR C  1 137 ? 5.782   107.337 92.701  1.00 62.49 ? 137 THR C CA  1 
ATOM   3223  C  C   . THR C  1 137 ? 5.965   106.580 94.005  1.00 64.27 ? 137 THR C C   1 
ATOM   3224  O  O   . THR C  1 137 ? 6.640   105.550 94.043  1.00 63.60 ? 137 THR C O   1 
ATOM   3225  C  CB  . THR C  1 137 ? 7.114   108.010 92.339  1.00 70.11 ? 137 THR C CB  1 
ATOM   3226  O  OG1 . THR C  1 137 ? 7.737   108.526 93.524  1.00 72.06 ? 137 THR C OG1 1 
ATOM   3227  C  CG2 . THR C  1 137 ? 6.886   109.142 91.341  1.00 68.73 ? 137 THR C CG2 1 
ATOM   3228  N  N   . GLY C  1 138 ? 5.375   107.101 95.075  1.00 68.98 ? 138 GLY C N   1 
ATOM   3229  C  CA  . GLY C  1 138 ? 5.554   106.529 96.397  1.00 68.41 ? 138 GLY C CA  1 
ATOM   3230  C  C   . GLY C  1 138 ? 6.953   106.740 96.941  1.00 66.49 ? 138 GLY C C   1 
ATOM   3231  O  O   . GLY C  1 138 ? 7.383   106.024 97.847  1.00 65.11 ? 138 GLY C O   1 
ATOM   3232  N  N   . ASN C  1 139 ? 7.655   107.724 96.380  1.00 67.47 ? 139 ASN C N   1 
ATOM   3233  C  CA  . ASN C  1 139 ? 8.990   108.101 96.834  1.00 72.21 ? 139 ASN C CA  1 
ATOM   3234  C  C   . ASN C  1 139 ? 9.938   106.906 96.930  1.00 72.36 ? 139 ASN C C   1 
ATOM   3235  O  O   . ASN C  1 139 ? 10.618  106.712 97.943  1.00 67.84 ? 139 ASN C O   1 
ATOM   3236  C  CB  . ASN C  1 139 ? 8.901   108.839 98.174  1.00 71.70 ? 139 ASN C CB  1 
ATOM   3237  C  CG  . ASN C  1 139 ? 7.852   109.942 98.160  1.00 78.77 ? 139 ASN C CG  1 
ATOM   3238  O  OD1 . ASN C  1 139 ? 7.772   110.726 97.212  1.00 78.18 ? 139 ASN C OD1 1 
ATOM   3239  N  ND2 . ASN C  1 139 ? 7.032   109.995 99.206  1.00 79.97 ? 139 ASN C ND2 1 
ATOM   3240  N  N   . ALA C  1 140 ? 9.966   106.105 95.868  1.00 66.96 ? 140 ALA C N   1 
ATOM   3241  C  CA  . ALA C  1 140 ? 10.793  104.905 95.832  1.00 62.97 ? 140 ALA C CA  1 
ATOM   3242  C  C   . ALA C  1 140 ? 12.239  105.252 95.480  1.00 60.67 ? 140 ALA C C   1 
ATOM   3243  O  O   . ALA C  1 140 ? 13.141  104.412 95.573  1.00 57.01 ? 140 ALA C O   1 
ATOM   3244  C  CB  . ALA C  1 140 ? 10.221  103.908 94.843  1.00 63.27 ? 140 ALA C CB  1 
ATOM   3245  N  N   . GLY C  1 141 ? 12.447  106.501 95.074  1.00 63.10 ? 141 GLY C N   1 
ATOM   3246  C  CA  . GLY C  1 141 ? 13.769  106.978 94.723  1.00 63.54 ? 141 GLY C CA  1 
ATOM   3247  C  C   . GLY C  1 141 ? 14.251  106.530 93.356  1.00 62.02 ? 141 GLY C C   1 
ATOM   3248  O  O   . GLY C  1 141 ? 13.460  106.371 92.423  1.00 63.29 ? 141 GLY C O   1 
ATOM   3249  N  N   . SER C  1 142 ? 15.560  106.314 93.257  1.00 60.97 ? 142 SER C N   1 
ATOM   3250  C  CA  . SER C  1 142 ? 16.240  106.059 91.991  1.00 61.55 ? 142 SER C CA  1 
ATOM   3251  C  C   . SER C  1 142 ? 15.943  104.684 91.401  1.00 63.05 ? 142 SER C C   1 
ATOM   3252  O  O   . SER C  1 142 ? 15.677  103.728 92.134  1.00 60.11 ? 142 SER C O   1 
ATOM   3253  C  CB  . SER C  1 142 ? 17.754  106.201 92.171  1.00 61.44 ? 142 SER C CB  1 
ATOM   3254  O  OG  . SER C  1 142 ? 18.307  105.056 92.804  1.00 56.39 ? 142 SER C OG  1 
ATOM   3255  N  N   . ARG C  1 143 ? 16.014  104.599 90.071  1.00 60.14 ? 143 ARG C N   1 
ATOM   3256  C  CA  . ARG C  1 143 ? 15.823  103.344 89.350  1.00 56.49 ? 143 ARG C CA  1 
ATOM   3257  C  C   . ARG C  1 143 ? 17.154  102.599 89.218  1.00 56.37 ? 143 ARG C C   1 
ATOM   3258  O  O   . ARG C  1 143 ? 18.063  103.035 88.501  1.00 54.73 ? 143 ARG C O   1 
ATOM   3259  C  CB  . ARG C  1 143 ? 15.198  103.617 87.976  1.00 52.87 ? 143 ARG C CB  1 
ATOM   3260  C  CG  . ARG C  1 143 ? 13.970  104.511 88.066  1.00 58.89 ? 143 ARG C CG  1 
ATOM   3261  C  CD  . ARG C  1 143 ? 13.429  104.977 86.719  1.00 53.47 ? 143 ARG C CD  1 
ATOM   3262  N  NE  . ARG C  1 143 ? 12.337  105.925 86.925  1.00 54.04 ? 143 ARG C NE  1 
ATOM   3263  C  CZ  . ARG C  1 143 ? 11.485  106.326 85.986  1.00 56.60 ? 143 ARG C CZ  1 
ATOM   3264  N  NH1 . ARG C  1 143 ? 11.580  105.867 84.742  1.00 56.37 ? 143 ARG C NH1 1 
ATOM   3265  N  NH2 . ARG C  1 143 ? 10.530  107.192 86.298  1.00 53.70 ? 143 ARG C NH2 1 
ATOM   3266  N  N   . LEU C  1 144 ? 17.262  101.477 89.923  1.00 53.12 ? 144 LEU C N   1 
ATOM   3267  C  CA  . LEU C  1 144 ? 18.522  100.746 90.009  1.00 56.41 ? 144 LEU C CA  1 
ATOM   3268  C  C   . LEU C  1 144 ? 18.757  99.837  88.814  1.00 50.11 ? 144 LEU C C   1 
ATOM   3269  O  O   . LEU C  1 144 ? 19.887  99.691  88.340  1.00 48.38 ? 144 LEU C O   1 
ATOM   3270  C  CB  . LEU C  1 144 ? 18.584  99.927  91.304  1.00 55.19 ? 144 LEU C CB  1 
ATOM   3271  C  CG  . LEU C  1 144 ? 18.768  100.718 92.602  1.00 58.69 ? 144 LEU C CG  1 
ATOM   3272  C  CD1 . LEU C  1 144 ? 18.790  99.790  93.806  1.00 56.36 ? 144 LEU C CD1 1 
ATOM   3273  C  CD2 . LEU C  1 144 ? 20.039  101.552 92.541  1.00 55.06 ? 144 LEU C CD2 1 
ATOM   3274  N  N   . ALA C  1 145 ? 17.689  99.210  88.344  1.00 48.38 ? 145 ALA C N   1 
ATOM   3275  C  CA  . ALA C  1 145 ? 17.792  98.265  87.240  1.00 51.32 ? 145 ALA C CA  1 
ATOM   3276  C  C   . ALA C  1 145 ? 16.445  98.040  86.567  1.00 48.82 ? 145 ALA C C   1 
ATOM   3277  O  O   . ALA C  1 145 ? 15.403  97.974  87.227  1.00 47.49 ? 145 ALA C O   1 
ATOM   3278  C  CB  . ALA C  1 145 ? 18.385  96.942  87.711  1.00 47.16 ? 145 ALA C CB  1 
ATOM   3279  N  N   . CYS C  1 146 ? 16.484  97.927  85.246  1.00 48.81 ? 146 CYS C N   1 
ATOM   3280  C  CA  . CYS C  1 146 ? 15.281  97.733  84.458  1.00 45.50 ? 146 CYS C CA  1 
ATOM   3281  C  C   . CYS C  1 146 ? 15.530  96.780  83.295  1.00 44.21 ? 146 CYS C C   1 
ATOM   3282  O  O   . CYS C  1 146 ? 16.654  96.345  83.052  1.00 42.67 ? 146 CYS C O   1 
ATOM   3283  C  CB  . CYS C  1 146 ? 14.756  99.073  83.939  1.00 48.51 ? 146 CYS C CB  1 
ATOM   3284  S  SG  . CYS C  1 146 ? 15.809  99.884  82.704  1.00 55.23 ? 146 CYS C SG  1 
ATOM   3285  N  N   . GLY C  1 147 ? 14.461  96.455  82.585  1.00 41.75 ? 147 GLY C N   1 
ATOM   3286  C  CA  . GLY C  1 147 ? 14.547  95.594  81.425  1.00 39.80 ? 147 GLY C CA  1 
ATOM   3287  C  C   . GLY C  1 147 ? 13.174  95.485  80.806  1.00 37.01 ? 147 GLY C C   1 
ATOM   3288  O  O   . GLY C  1 147 ? 12.172  95.459  81.525  1.00 38.36 ? 147 GLY C O   1 
ATOM   3289  N  N   . VAL C  1 148 ? 13.115  95.429  79.481  1.00 29.76 ? 148 VAL C N   1 
ATOM   3290  C  CA  . VAL C  1 148 ? 11.828  95.314  78.800  1.00 31.58 ? 148 VAL C CA  1 
ATOM   3291  C  C   . VAL C  1 148 ? 11.236  93.936  79.066  1.00 28.54 ? 148 VAL C C   1 
ATOM   3292  O  O   . VAL C  1 148 ? 11.950  92.937  79.078  1.00 31.38 ? 148 VAL C O   1 
ATOM   3293  C  CB  . VAL C  1 148 ? 11.962  95.555  77.283  1.00 32.05 ? 148 VAL C CB  1 
ATOM   3294  C  CG1 . VAL C  1 148 ? 10.593  95.565  76.630  1.00 31.99 ? 148 VAL C CG1 1 
ATOM   3295  C  CG2 . VAL C  1 148 ? 12.697  96.877  77.018  1.00 30.24 ? 148 VAL C CG2 1 
ATOM   3296  N  N   . ILE C  1 149 ? 9.935   93.885  79.310  1.00 27.40 ? 149 ILE C N   1 
ATOM   3297  C  CA  . ILE C  1 149 ? 9.263   92.607  79.465  1.00 26.54 ? 149 ILE C CA  1 
ATOM   3298  C  C   . ILE C  1 149 ? 9.005   91.933  78.104  1.00 28.82 ? 149 ILE C C   1 
ATOM   3299  O  O   . ILE C  1 149 ? 8.320   92.485  77.231  1.00 26.35 ? 149 ILE C O   1 
ATOM   3300  C  CB  . ILE C  1 149 ? 7.958   92.780  80.243  1.00 28.02 ? 149 ILE C CB  1 
ATOM   3301  C  CG1 . ILE C  1 149 ? 8.280   93.263  81.665  1.00 34.45 ? 149 ILE C CG1 1 
ATOM   3302  C  CG2 . ILE C  1 149 ? 7.203   91.478  80.283  1.00 24.95 ? 149 ILE C CG2 1 
ATOM   3303  C  CD1 . ILE C  1 149 ? 7.205   94.109  82.303  1.00 31.53 ? 149 ILE C CD1 1 
ATOM   3304  N  N   . GLY C  1 150 ? 9.558   90.737  77.931  1.00 25.90 ? 150 GLY C N   1 
ATOM   3305  C  CA  . GLY C  1 150 ? 9.435   90.018  76.677  1.00 27.39 ? 150 GLY C CA  1 
ATOM   3306  C  C   . GLY C  1 150 ? 8.701   88.693  76.777  1.00 29.15 ? 150 GLY C C   1 
ATOM   3307  O  O   . GLY C  1 150 ? 8.745   88.030  77.817  1.00 25.43 ? 150 GLY C O   1 
ATOM   3308  N  N   . ILE C  1 151 ? 8.013   88.323  75.692  1.00 23.63 ? 151 ILE C N   1 
ATOM   3309  C  CA  . ILE C  1 151 ? 7.326   87.044  75.583  1.00 21.93 ? 151 ILE C CA  1 
ATOM   3310  C  C   . ILE C  1 151 ? 8.347   85.931  75.703  1.00 26.40 ? 151 ILE C C   1 
ATOM   3311  O  O   . ILE C  1 151 ? 9.435   86.027  75.139  1.00 27.76 ? 151 ILE C O   1 
ATOM   3312  C  CB  . ILE C  1 151 ? 6.598   86.919  74.220  1.00 29.24 ? 151 ILE C CB  1 
ATOM   3313  C  CG1 . ILE C  1 151 ? 5.686   88.123  73.996  1.00 27.94 ? 151 ILE C CG1 1 
ATOM   3314  C  CG2 . ILE C  1 151 ? 5.787   85.636  74.147  1.00 27.41 ? 151 ILE C CG2 1 
ATOM   3315  C  CD1 . ILE C  1 151 ? 5.076   88.174  72.632  1.00 27.23 ? 151 ILE C CD1 1 
ATOM   3316  N  N   . ALA C  1 152 ? 8.007   84.882  76.445  1.00 28.13 ? 152 ALA C N   1 
ATOM   3317  C  CA  . ALA C  1 152 ? 8.960   83.821  76.727  1.00 26.36 ? 152 ALA C CA  1 
ATOM   3318  C  C   . ALA C  1 152 ? 8.450   82.500  76.198  1.00 27.96 ? 152 ALA C C   1 
ATOM   3319  O  O   . ALA C  1 152 ? 7.248   82.305  76.086  1.00 29.37 ? 152 ALA C O   1 
ATOM   3320  C  CB  . ALA C  1 152 ? 9.211   83.724  78.213  1.00 28.37 ? 152 ALA C CB  1 
ATOM   3321  N  N   . GLN C  1 153 ? 9.360   81.587  75.877  1.00 29.71 ? 153 GLN C N   1 
ATOM   3322  C  CA  . GLN C  1 153 ? 8.942   80.288  75.371  1.00 33.57 ? 153 GLN C CA  1 
ATOM   3323  C  C   . GLN C  1 153 ? 8.053   79.539  76.360  1.00 42.17 ? 153 GLN C C   1 
ATOM   3324  O  O   . GLN C  1 153 ? 8.376   79.392  77.544  1.00 41.55 ? 153 GLN C O   1 
ATOM   3325  C  CB  . GLN C  1 153 ? 10.141  79.426  74.982  1.00 37.19 ? 153 GLN C CB  1 
ATOM   3326  C  CG  . GLN C  1 153 ? 9.729   78.088  74.394  1.00 35.69 ? 153 GLN C CG  1 
ATOM   3327  C  CD  . GLN C  1 153 ? 10.910  77.236  74.017  1.00 42.67 ? 153 GLN C CD  1 
ATOM   3328  O  OE1 . GLN C  1 153 ? 12.043  77.514  74.416  1.00 50.64 ? 153 GLN C OE1 1 
ATOM   3329  N  NE2 . GLN C  1 153 ? 10.658  76.188  73.243  1.00 43.73 ? 153 GLN C NE2 1 
ATOM   3330  O  OXT . GLN C  1 153 ? 6.979   79.074  75.981  1.00 49.00 ? 153 GLN C OXT 1 
ATOM   3331  N  N   . ALA D  1 1   ? -1.354  106.349 66.245  1.00 50.36 ? 1   ALA D N   1 
ATOM   3332  C  CA  . ALA D  1 1   ? -0.061  105.829 65.804  1.00 49.92 ? 1   ALA D CA  1 
ATOM   3333  C  C   . ALA D  1 1   ? 0.707   105.095 66.912  1.00 46.47 ? 1   ALA D C   1 
ATOM   3334  O  O   . ALA D  1 1   ? 1.176   105.710 67.872  1.00 45.19 ? 1   ALA D O   1 
ATOM   3335  C  CB  . ALA D  1 1   ? 0.797   106.957 65.212  1.00 47.99 ? 1   ALA D CB  1 
ATOM   3336  N  N   . THR D  1 2   ? 0.834   103.780 66.767  1.00 43.06 ? 2   THR D N   1 
ATOM   3337  C  CA  . THR D  1 2   ? 1.684   102.997 67.656  1.00 41.42 ? 2   THR D CA  1 
ATOM   3338  C  C   . THR D  1 2   ? 3.178   103.221 67.349  1.00 39.99 ? 2   THR D C   1 
ATOM   3339  O  O   . THR D  1 2   ? 3.604   103.301 66.185  1.00 34.11 ? 2   THR D O   1 
ATOM   3340  C  CB  . THR D  1 2   ? 1.357   101.480 67.584  1.00 41.56 ? 2   THR D CB  1 
ATOM   3341  O  OG1 . THR D  1 2   ? -0.050  101.292 67.402  1.00 41.81 ? 2   THR D OG1 1 
ATOM   3342  C  CG2 . THR D  1 2   ? 1.795   100.771 68.861  1.00 38.07 ? 2   THR D CG2 1 
ATOM   3343  N  N   . LYS D  1 3   ? 3.969   103.334 68.407  1.00 35.59 ? 3   LYS D N   1 
ATOM   3344  C  CA  . LYS D  1 3   ? 5.405   103.430 68.266  1.00 33.03 ? 3   LYS D CA  1 
ATOM   3345  C  C   . LYS D  1 3   ? 6.022   102.318 69.084  1.00 33.64 ? 3   LYS D C   1 
ATOM   3346  O  O   . LYS D  1 3   ? 5.430   101.852 70.060  1.00 29.61 ? 3   LYS D O   1 
ATOM   3347  C  CB  . LYS D  1 3   ? 5.908   104.789 68.751  1.00 33.54 ? 3   LYS D CB  1 
ATOM   3348  C  CG  . LYS D  1 3   ? 5.356   105.968 67.956  1.00 41.77 ? 3   LYS D CG  1 
ATOM   3349  C  CD  . LYS D  1 3   ? 5.841   107.296 68.519  1.00 46.83 ? 3   LYS D CD  1 
ATOM   3350  C  CE  . LYS D  1 3   ? 5.554   108.461 67.581  1.00 51.90 ? 3   LYS D CE  1 
ATOM   3351  N  NZ  . LYS D  1 3   ? 5.951   109.767 68.193  1.00 53.14 ? 3   LYS D NZ  1 
ATOM   3352  N  N   . ALA D  1 4   ? 7.198   101.872 68.664  1.00 28.74 ? 4   ALA D N   1 
ATOM   3353  C  CA  . ALA D  1 4   ? 7.977   100.924 69.442  1.00 27.48 ? 4   ALA D CA  1 
ATOM   3354  C  C   . ALA D  1 4   ? 9.453   101.212 69.232  1.00 28.93 ? 4   ALA D C   1 
ATOM   3355  O  O   . ALA D  1 4   ? 9.832   101.952 68.318  1.00 30.52 ? 4   ALA D O   1 
ATOM   3356  C  CB  . ALA D  1 4   ? 7.647   99.500  69.062  1.00 26.02 ? 4   ALA D CB  1 
ATOM   3357  N  N   . VAL D  1 5   ? 10.287  100.640 70.086  1.00 23.18 ? 5   VAL D N   1 
ATOM   3358  C  CA  . VAL D  1 5   ? 11.700  100.929 70.040  1.00 23.97 ? 5   VAL D CA  1 
ATOM   3359  C  C   . VAL D  1 5   ? 12.458  99.710  70.532  1.00 24.78 ? 5   VAL D C   1 
ATOM   3360  O  O   . VAL D  1 5   ? 11.935  98.936  71.330  1.00 24.20 ? 5   VAL D O   1 
ATOM   3361  C  CB  . VAL D  1 5   ? 12.021  102.183 70.885  1.00 30.59 ? 5   VAL D CB  1 
ATOM   3362  C  CG1 . VAL D  1 5   ? 11.699  101.938 72.365  1.00 31.58 ? 5   VAL D CG1 1 
ATOM   3363  C  CG2 . VAL D  1 5   ? 13.465  102.623 70.682  1.00 22.37 ? 5   VAL D CG2 1 
ATOM   3364  N  N   . CYS D  1 6   ? 13.669  99.516  70.016  1.00 24.30 ? 6   CYS D N   1 
ATOM   3365  C  CA  . CYS D  1 6   ? 14.531  98.422  70.445  1.00 25.73 ? 6   CYS D CA  1 
ATOM   3366  C  C   . CYS D  1 6   ? 15.978  98.884  70.523  1.00 29.11 ? 6   CYS D C   1 
ATOM   3367  O  O   . CYS D  1 6   ? 16.504  99.493  69.585  1.00 27.40 ? 6   CYS D O   1 
ATOM   3368  C  CB  . CYS D  1 6   ? 14.441  97.222  69.490  1.00 23.22 ? 6   CYS D CB  1 
ATOM   3369  S  SG  . CYS D  1 6   ? 15.493  95.782  69.955  1.00 21.95 ? 6   CYS D SG  1 
ATOM   3370  N  N   . VAL D  1 7   ? 16.619  98.586  71.646  1.00 27.95 ? 7   VAL D N   1 
ATOM   3371  C  CA  . VAL D  1 7   ? 18.041  98.852  71.819  1.00 22.93 ? 7   VAL D CA  1 
ATOM   3372  C  C   . VAL D  1 7   ? 18.774  97.559  71.532  1.00 25.49 ? 7   VAL D C   1 
ATOM   3373  O  O   . VAL D  1 7   ? 18.518  96.547  72.172  1.00 26.59 ? 7   VAL D O   1 
ATOM   3374  C  CB  . VAL D  1 7   ? 18.342  99.303  73.255  1.00 25.92 ? 7   VAL D CB  1 
ATOM   3375  C  CG1 . VAL D  1 7   ? 19.840  99.428  73.479  1.00 30.21 ? 7   VAL D CG1 1 
ATOM   3376  C  CG2 . VAL D  1 7   ? 17.624  100.620 73.551  1.00 29.05 ? 7   VAL D CG2 1 
ATOM   3377  N  N   . LEU D  1 8   ? 19.658  97.577  70.543  1.00 22.29 ? 8   LEU D N   1 
ATOM   3378  C  CA  . LEU D  1 8   ? 20.429  96.390  70.215  1.00 26.08 ? 8   LEU D CA  1 
ATOM   3379  C  C   . LEU D  1 8   ? 21.761  96.405  70.972  1.00 27.78 ? 8   LEU D C   1 
ATOM   3380  O  O   . LEU D  1 8   ? 22.468  97.409  70.983  1.00 25.40 ? 8   LEU D O   1 
ATOM   3381  C  CB  . LEU D  1 8   ? 20.700  96.315  68.707  1.00 27.42 ? 8   LEU D CB  1 
ATOM   3382  C  CG  . LEU D  1 8   ? 19.526  96.230  67.724  1.00 27.45 ? 8   LEU D CG  1 
ATOM   3383  C  CD1 . LEU D  1 8   ? 20.049  96.103  66.324  1.00 19.71 ? 8   LEU D CD1 1 
ATOM   3384  C  CD2 . LEU D  1 8   ? 18.618  95.059  68.034  1.00 24.13 ? 8   LEU D CD2 1 
ATOM   3385  N  N   . LYS D  1 9   ? 22.093  95.279  71.593  1.00 26.62 ? 9   LYS D N   1 
ATOM   3386  C  CA  . LYS D  1 9   ? 23.350  95.118  72.297  1.00 28.27 ? 9   LYS D CA  1 
ATOM   3387  C  C   . LYS D  1 9   ? 23.795  93.680  72.141  1.00 28.18 ? 9   LYS D C   1 
ATOM   3388  O  O   . LYS D  1 9   ? 22.968  92.774  72.091  1.00 31.87 ? 9   LYS D O   1 
ATOM   3389  C  CB  . LYS D  1 9   ? 23.191  95.454  73.786  1.00 31.44 ? 9   LYS D CB  1 
ATOM   3390  C  CG  . LYS D  1 9   ? 23.206  96.952  74.103  1.00 37.93 ? 9   LYS D CG  1 
ATOM   3391  C  CD  . LYS D  1 9   ? 23.518  97.216  75.581  1.00 43.62 ? 9   LYS D CD  1 
ATOM   3392  C  CE  . LYS D  1 9   ? 23.765  98.696  75.853  1.00 46.01 ? 9   LYS D CE  1 
ATOM   3393  N  NZ  . LYS D  1 9   ? 22.509  99.496  75.866  1.00 43.69 ? 9   LYS D NZ  1 
ATOM   3394  N  N   . GLY D  1 10  ? 25.101  93.469  72.063  1.00 31.23 ? 10  GLY D N   1 
ATOM   3395  C  CA  . GLY D  1 10  ? 25.653  92.134  71.943  1.00 33.46 ? 10  GLY D CA  1 
ATOM   3396  C  C   . GLY D  1 10  ? 26.930  92.011  72.749  1.00 40.62 ? 10  GLY D C   1 
ATOM   3397  O  O   . GLY D  1 10  ? 27.277  92.910  73.522  1.00 34.88 ? 10  GLY D O   1 
ATOM   3398  N  N   . ASP D  1 11  ? 27.626  90.890  72.582  1.00 43.68 ? 11  ASP D N   1 
ATOM   3399  C  CA  . ASP D  1 11  ? 28.916  90.695  73.227  1.00 43.40 ? 11  ASP D CA  1 
ATOM   3400  C  C   . ASP D  1 11  ? 29.898  91.722  72.723  1.00 41.48 ? 11  ASP D C   1 
ATOM   3401  O  O   . ASP D  1 11  ? 30.378  92.565  73.481  1.00 47.34 ? 11  ASP D O   1 
ATOM   3402  C  CB  . ASP D  1 11  ? 29.473  89.306  72.930  1.00 44.94 ? 11  ASP D CB  1 
ATOM   3403  C  CG  . ASP D  1 11  ? 28.715  88.218  73.639  1.00 50.23 ? 11  ASP D CG  1 
ATOM   3404  O  OD1 . ASP D  1 11  ? 27.895  88.552  74.521  1.00 53.32 ? 11  ASP D OD1 1 
ATOM   3405  O  OD2 . ASP D  1 11  ? 28.948  87.031  73.324  1.00 53.41 ? 11  ASP D OD2 1 
ATOM   3406  N  N   . GLY D  1 12  ? 30.189  91.639  71.431  1.00 37.11 ? 12  GLY D N   1 
ATOM   3407  C  CA  . GLY D  1 12  ? 31.192  92.477  70.805  1.00 33.40 ? 12  GLY D CA  1 
ATOM   3408  C  C   . GLY D  1 12  ? 30.788  93.931  70.697  1.00 27.14 ? 12  GLY D C   1 
ATOM   3409  O  O   . GLY D  1 12  ? 30.110  94.457  71.572  1.00 31.35 ? 12  GLY D O   1 
ATOM   3410  N  N   . PRO D  1 13  ? 31.203  94.584  69.604  1.00 26.86 ? 13  PRO D N   1 
ATOM   3411  C  CA  . PRO D  1 13  ? 31.067  96.024  69.362  1.00 29.00 ? 13  PRO D CA  1 
ATOM   3412  C  C   . PRO D  1 13  ? 29.774  96.460  68.653  1.00 31.16 ? 13  PRO D C   1 
ATOM   3413  O  O   . PRO D  1 13  ? 29.564  97.667  68.477  1.00 31.15 ? 13  PRO D O   1 
ATOM   3414  C  CB  . PRO D  1 13  ? 32.269  96.334  68.457  1.00 24.93 ? 13  PRO D CB  1 
ATOM   3415  C  CG  . PRO D  1 13  ? 32.799  94.990  67.986  1.00 22.95 ? 13  PRO D CG  1 
ATOM   3416  C  CD  . PRO D  1 13  ? 31.915  93.918  68.503  1.00 29.72 ? 13  PRO D CD  1 
ATOM   3417  N  N   . VAL D  1 14  ? 28.919  95.525  68.247  1.00 27.25 ? 14  VAL D N   1 
ATOM   3418  C  CA  . VAL D  1 14  ? 27.706  95.942  67.548  1.00 25.96 ? 14  VAL D CA  1 
ATOM   3419  C  C   . VAL D  1 14  ? 26.671  96.494  68.507  1.00 27.58 ? 14  VAL D C   1 
ATOM   3420  O  O   . VAL D  1 14  ? 26.257  95.820  69.448  1.00 28.83 ? 14  VAL D O   1 
ATOM   3421  C  CB  . VAL D  1 14  ? 27.053  94.810  66.765  1.00 30.33 ? 14  VAL D CB  1 
ATOM   3422  C  CG1 . VAL D  1 14  ? 25.782  95.332  66.079  1.00 27.36 ? 14  VAL D CG1 1 
ATOM   3423  C  CG2 . VAL D  1 14  ? 28.020  94.236  65.750  1.00 26.32 ? 14  VAL D CG2 1 
ATOM   3424  N  N   . GLN D  1 15  ? 26.254  97.729  68.275  1.00 26.02 ? 15  GLN D N   1 
ATOM   3425  C  CA  . GLN D  1 15  ? 25.162  98.276  69.047  1.00 30.53 ? 15  GLN D CA  1 
ATOM   3426  C  C   . GLN D  1 15  ? 24.364  99.256  68.204  1.00 29.21 ? 15  GLN D C   1 
ATOM   3427  O  O   . GLN D  1 15  ? 24.835  99.725  67.161  1.00 28.65 ? 15  GLN D O   1 
ATOM   3428  C  CB  . GLN D  1 15  ? 25.671  98.927  70.344  1.00 33.63 ? 15  GLN D CB  1 
ATOM   3429  C  CG  . GLN D  1 15  ? 26.642  100.091 70.166  1.00 34.88 ? 15  GLN D CG  1 
ATOM   3430  C  CD  . GLN D  1 15  ? 27.355  100.470 71.480  1.00 42.85 ? 15  GLN D CD  1 
ATOM   3431  O  OE1 . GLN D  1 15  ? 27.191  101.578 72.000  1.00 43.54 ? 15  GLN D OE1 1 
ATOM   3432  N  NE2 . GLN D  1 15  ? 28.141  99.543  72.015  1.00 32.75 ? 15  GLN D NE2 1 
ATOM   3433  N  N   . GLY D  1 16  ? 23.149  99.552  68.652  1.00 26.96 ? 16  GLY D N   1 
ATOM   3434  C  CA  . GLY D  1 16  ? 22.341  100.557 68.001  1.00 24.20 ? 16  GLY D CA  1 
ATOM   3435  C  C   . GLY D  1 16  ? 20.933  100.649 68.541  1.00 22.90 ? 16  GLY D C   1 
ATOM   3436  O  O   . GLY D  1 16  ? 20.564  99.922  69.456  1.00 26.35 ? 16  GLY D O   1 
ATOM   3437  N  N   . ILE D  1 17  ? 20.151  101.548 67.953  1.00 22.87 ? 17  ILE D N   1 
ATOM   3438  C  CA  . ILE D  1 17  ? 18.761  101.764 68.333  1.00 27.04 ? 17  ILE D CA  1 
ATOM   3439  C  C   . ILE D  1 17  ? 17.870  101.773 67.097  1.00 27.84 ? 17  ILE D C   1 
ATOM   3440  O  O   . ILE D  1 17  ? 18.142  102.471 66.116  1.00 27.49 ? 17  ILE D O   1 
ATOM   3441  C  CB  . ILE D  1 17  ? 18.575  103.098 69.060  1.00 27.24 ? 17  ILE D CB  1 
ATOM   3442  C  CG1 . ILE D  1 17  ? 19.555  103.197 70.240  1.00 33.81 ? 17  ILE D CG1 1 
ATOM   3443  C  CG2 . ILE D  1 17  ? 17.127  103.263 69.518  1.00 31.05 ? 17  ILE D CG2 1 
ATOM   3444  C  CD1 . ILE D  1 17  ? 19.920  104.619 70.593  1.00 33.79 ? 17  ILE D CD1 1 
ATOM   3445  N  N   . ILE D  1 18  ? 16.798  100.998 67.162  1.00 25.68 ? 18  ILE D N   1 
ATOM   3446  C  CA  . ILE D  1 18  ? 15.869  100.870 66.061  1.00 21.28 ? 18  ILE D CA  1 
ATOM   3447  C  C   . ILE D  1 18  ? 14.465  101.265 66.502  1.00 24.80 ? 18  ILE D C   1 
ATOM   3448  O  O   . ILE D  1 18  ? 13.930  100.721 67.461  1.00 27.18 ? 18  ILE D O   1 
ATOM   3449  C  CB  . ILE D  1 18  ? 15.869  99.427  65.550  1.00 23.44 ? 18  ILE D CB  1 
ATOM   3450  C  CG1 . ILE D  1 18  ? 17.269  99.044  65.052  1.00 20.91 ? 18  ILE D CG1 1 
ATOM   3451  C  CG2 . ILE D  1 18  ? 14.846  99.256  64.433  1.00 22.56 ? 18  ILE D CG2 1 
ATOM   3452  C  CD1 . ILE D  1 18  ? 17.711  99.870  63.852  1.00 20.59 ? 18  ILE D CD1 1 
ATOM   3453  N  N   . ASN D  1 19  ? 13.879  102.224 65.800  1.00 22.29 ? 19  ASN D N   1 
ATOM   3454  C  CA  . ASN D  1 19  ? 12.519  102.656 66.058  1.00 25.16 ? 19  ASN D CA  1 
ATOM   3455  C  C   . ASN D  1 19  ? 11.504  102.010 65.107  1.00 27.85 ? 19  ASN D C   1 
ATOM   3456  O  O   . ASN D  1 19  ? 11.840  101.569 64.005  1.00 21.71 ? 19  ASN D O   1 
ATOM   3457  C  CB  . ASN D  1 19  ? 12.430  104.175 65.954  1.00 26.94 ? 19  ASN D CB  1 
ATOM   3458  C  CG  . ASN D  1 19  ? 13.574  104.874 66.667  1.00 27.64 ? 19  ASN D CG  1 
ATOM   3459  O  OD1 . ASN D  1 19  ? 13.529  105.066 67.873  1.00 29.62 ? 19  ASN D OD1 1 
ATOM   3460  N  ND2 . ASN D  1 19  ? 14.601  105.258 65.921  1.00 27.50 ? 19  ASN D ND2 1 
ATOM   3461  N  N   . PHE D  1 20  ? 10.258  101.956 65.546  1.00 25.73 ? 20  PHE D N   1 
ATOM   3462  C  CA  . PHE D  1 20  ? 9.183   101.418 64.731  1.00 25.92 ? 20  PHE D CA  1 
ATOM   3463  C  C   . PHE D  1 20  ? 8.052   102.406 64.819  1.00 28.44 ? 20  PHE D C   1 
ATOM   3464  O  O   . PHE D  1 20  ? 7.910   103.101 65.827  1.00 30.29 ? 20  PHE D O   1 
ATOM   3465  C  CB  . PHE D  1 20  ? 8.693   100.071 65.270  1.00 20.79 ? 20  PHE D CB  1 
ATOM   3466  C  CG  . PHE D  1 20  ? 9.731   98.981  65.249  1.00 21.51 ? 20  PHE D CG  1 
ATOM   3467  C  CD1 . PHE D  1 20  ? 10.714  98.913  66.226  1.00 26.01 ? 20  PHE D CD1 1 
ATOM   3468  C  CD2 . PHE D  1 20  ? 9.704   98.000  64.273  1.00 20.13 ? 20  PHE D CD2 1 
ATOM   3469  C  CE1 . PHE D  1 20  ? 11.662  97.887  66.214  1.00 19.79 ? 20  PHE D CE1 1 
ATOM   3470  C  CE2 . PHE D  1 20  ? 10.633  96.985  64.263  1.00 18.64 ? 20  PHE D CE2 1 
ATOM   3471  C  CZ  . PHE D  1 20  ? 11.613  96.932  65.237  1.00 19.18 ? 20  PHE D CZ  1 
ATOM   3472  N  N   . GLU D  1 21  ? 7.241   102.474 63.774  1.00 26.16 ? 21  GLU D N   1 
ATOM   3473  C  CA  . GLU D  1 21  ? 6.052   103.304 63.825  1.00 29.43 ? 21  GLU D CA  1 
ATOM   3474  C  C   . GLU D  1 21  ? 4.974   102.763 62.898  1.00 30.40 ? 21  GLU D C   1 
ATOM   3475  O  O   . GLU D  1 21  ? 5.239   102.439 61.735  1.00 27.34 ? 21  GLU D O   1 
ATOM   3476  C  CB  . GLU D  1 21  ? 6.396   104.749 63.484  1.00 35.72 ? 21  GLU D CB  1 
ATOM   3477  C  CG  . GLU D  1 21  ? 5.247   105.721 63.670  1.00 43.20 ? 21  GLU D CG  1 
ATOM   3478  C  CD  . GLU D  1 21  ? 5.677   107.165 63.467  1.00 52.59 ? 21  GLU D CD  1 
ATOM   3479  O  OE1 . GLU D  1 21  ? 4.791   108.047 63.374  1.00 61.20 ? 21  GLU D OE1 1 
ATOM   3480  O  OE2 . GLU D  1 21  ? 6.903   107.412 63.400  1.00 48.87 ? 21  GLU D OE2 1 
ATOM   3481  N  N   . GLN D  1 22  ? 3.765   102.635 63.428  1.00 25.76 ? 22  GLN D N   1 
ATOM   3482  C  CA  . GLN D  1 22  ? 2.652   102.128 62.647  1.00 30.19 ? 22  GLN D CA  1 
ATOM   3483  C  C   . GLN D  1 22  ? 1.479   103.062 62.848  1.00 36.87 ? 22  GLN D C   1 
ATOM   3484  O  O   . GLN D  1 22  ? 0.778   102.979 63.853  1.00 38.56 ? 22  GLN D O   1 
ATOM   3485  C  CB  . GLN D  1 22  ? 2.282   100.712 63.093  1.00 29.81 ? 22  GLN D CB  1 
ATOM   3486  C  CG  . GLN D  1 22  ? 1.336   99.990  62.138  1.00 28.47 ? 22  GLN D CG  1 
ATOM   3487  C  CD  . GLN D  1 22  ? 1.057   98.559  62.554  1.00 29.31 ? 22  GLN D CD  1 
ATOM   3488  O  OE1 . GLN D  1 22  ? 1.274   98.183  63.711  1.00 30.11 ? 22  GLN D OE1 1 
ATOM   3489  N  NE2 . GLN D  1 22  ? 0.578   97.748  61.611  1.00 22.28 ? 22  GLN D NE2 1 
ATOM   3490  N  N   . LYS D  1 23  ? 1.266   103.959 61.895  1.00 36.41 ? 23  LYS D N   1 
ATOM   3491  C  CA  . LYS D  1 23  ? 0.238   104.975 62.048  1.00 42.14 ? 23  LYS D CA  1 
ATOM   3492  C  C   . LYS D  1 23  ? -1.180  104.391 62.012  1.00 43.43 ? 23  LYS D C   1 
ATOM   3493  O  O   . LYS D  1 23  ? -2.123  105.031 62.463  1.00 51.76 ? 23  LYS D O   1 
ATOM   3494  C  CB  . LYS D  1 23  ? 0.410   106.074 60.992  1.00 45.29 ? 23  LYS D CB  1 
ATOM   3495  C  CG  . LYS D  1 23  ? 1.727   106.846 61.114  1.00 49.08 ? 23  LYS D CG  1 
ATOM   3496  C  CD  . LYS D  1 23  ? 2.125   107.541 59.800  1.00 61.43 ? 23  LYS D CD  1 
ATOM   3497  C  CE  . LYS D  1 23  ? 1.169   108.672 59.419  1.00 67.06 ? 23  LYS D CE  1 
ATOM   3498  N  NZ  . LYS D  1 23  ? 1.534   109.316 58.119  1.00 61.12 ? 23  LYS D NZ  1 
ATOM   3499  N  N   . GLU D  1 24  ? -1.333  103.182 61.484  1.00 36.29 ? 24  GLU D N   1 
ATOM   3500  C  CA  . GLU D  1 24  ? -2.652  102.559 61.389  1.00 39.53 ? 24  GLU D CA  1 
ATOM   3501  C  C   . GLU D  1 24  ? -2.576  101.068 61.665  1.00 40.47 ? 24  GLU D C   1 
ATOM   3502  O  O   . GLU D  1 24  ? -1.620  100.411 61.262  1.00 38.81 ? 24  GLU D O   1 
ATOM   3503  C  CB  . GLU D  1 24  ? -3.266  102.786 60.009  1.00 42.88 ? 24  GLU D CB  1 
ATOM   3504  C  CG  . GLU D  1 24  ? -3.669  104.220 59.737  1.00 51.10 ? 24  GLU D CG  1 
ATOM   3505  C  CD  . GLU D  1 24  ? -3.494  104.590 58.280  1.00 57.73 ? 24  GLU D CD  1 
ATOM   3506  O  OE1 . GLU D  1 24  ? -3.717  103.712 57.415  1.00 62.55 ? 24  GLU D OE1 1 
ATOM   3507  O  OE2 . GLU D  1 24  ? -3.121  105.752 58.002  1.00 57.82 ? 24  GLU D OE2 1 
ATOM   3508  N  N   . SER D  1 25  ? -3.605  100.545 62.329  1.00 38.08 ? 25  SER D N   1 
ATOM   3509  C  CA  . SER D  1 25  ? -3.650  99.154  62.787  1.00 39.71 ? 25  SER D CA  1 
ATOM   3510  C  C   . SER D  1 25  ? -3.349  98.130  61.699  1.00 39.16 ? 25  SER D C   1 
ATOM   3511  O  O   . SER D  1 25  ? -2.802  97.061  61.966  1.00 43.57 ? 25  SER D O   1 
ATOM   3512  C  CB  . SER D  1 25  ? -5.025  98.855  63.395  1.00 42.88 ? 25  SER D CB  1 
ATOM   3513  O  OG  . SER D  1 25  ? -6.052  99.262  62.506  1.00 44.47 ? 25  SER D OG  1 
ATOM   3514  N  N   . ASN D  1 26  ? -3.710  98.457  60.470  1.00 38.56 ? 26  ASN D N   1 
ATOM   3515  C  CA  . ASN D  1 26  ? -3.532  97.532  59.367  1.00 42.83 ? 26  ASN D CA  1 
ATOM   3516  C  C   . ASN D  1 26  ? -2.451  98.016  58.409  1.00 38.49 ? 26  ASN D C   1 
ATOM   3517  O  O   . ASN D  1 26  ? -2.223  97.411  57.361  1.00 38.54 ? 26  ASN D O   1 
ATOM   3518  C  CB  . ASN D  1 26  ? -4.842  97.441  58.603  1.00 41.63 ? 26  ASN D CB  1 
ATOM   3519  C  CG  . ASN D  1 26  ? -5.364  98.808  58.226  1.00 44.14 ? 26  ASN D CG  1 
ATOM   3520  O  OD1 . ASN D  1 26  ? -5.408  99.715  59.065  1.00 48.95 ? 26  ASN D OD1 1 
ATOM   3521  N  ND2 . ASN D  1 26  ? -5.732  98.982  56.958  1.00 44.26 ? 26  ASN D ND2 1 
ATOM   3522  N  N   . GLY D  1 27  ? -1.809  99.125  58.757  1.00 34.83 ? 27  GLY D N   1 
ATOM   3523  C  CA  . GLY D  1 27  ? -0.891  99.782  57.847  1.00 31.38 ? 27  GLY D CA  1 
ATOM   3524  C  C   . GLY D  1 27  ? 0.518   99.237  57.959  1.00 28.64 ? 27  GLY D C   1 
ATOM   3525  O  O   . GLY D  1 27  ? 0.792   98.373  58.797  1.00 21.28 ? 27  GLY D O   1 
ATOM   3526  N  N   . PRO D  1 28  ? 1.420   99.735  57.099  1.00 29.18 ? 28  PRO D N   1 
ATOM   3527  C  CA  . PRO D  1 28  ? 2.821   99.326  57.138  1.00 26.65 ? 28  PRO D CA  1 
ATOM   3528  C  C   . PRO D  1 28  ? 3.459   99.842  58.404  1.00 20.79 ? 28  PRO D C   1 
ATOM   3529  O  O   . PRO D  1 28  ? 2.959   100.795 59.007  1.00 19.50 ? 28  PRO D O   1 
ATOM   3530  C  CB  . PRO D  1 28  ? 3.437   100.041 55.921  1.00 23.09 ? 28  PRO D CB  1 
ATOM   3531  C  CG  . PRO D  1 28  ? 2.305   100.452 55.092  1.00 28.99 ? 28  PRO D CG  1 
ATOM   3532  C  CD  . PRO D  1 28  ? 1.175   100.712 56.028  1.00 27.65 ? 28  PRO D CD  1 
ATOM   3533  N  N   . VAL D  1 29  ? 4.547   99.196  58.794  1.00 21.86 ? 29  VAL D N   1 
ATOM   3534  C  CA  . VAL D  1 29  ? 5.385   99.632  59.895  1.00 19.74 ? 29  VAL D CA  1 
ATOM   3535  C  C   . VAL D  1 29  ? 6.666   100.213 59.323  1.00 19.68 ? 29  VAL D C   1 
ATOM   3536  O  O   . VAL D  1 29  ? 7.360   99.549  58.573  1.00 22.97 ? 29  VAL D O   1 
ATOM   3537  C  CB  . VAL D  1 29  ? 5.787   98.442  60.793  1.00 21.81 ? 29  VAL D CB  1 
ATOM   3538  C  CG1 . VAL D  1 29  ? 6.686   98.916  61.927  1.00 19.88 ? 29  VAL D CG1 1 
ATOM   3539  C  CG2 . VAL D  1 29  ? 4.561   97.737  61.330  1.00 19.29 ? 29  VAL D CG2 1 
ATOM   3540  N  N   . LYS D  1 30  ? 6.983   101.451 59.673  1.00 24.27 ? 30  LYS D N   1 
ATOM   3541  C  CA  . LYS D  1 30  ? 8.275   102.015 59.325  1.00 25.79 ? 30  LYS D CA  1 
ATOM   3542  C  C   . LYS D  1 30  ? 9.333   101.581 60.333  1.00 26.09 ? 30  LYS D C   1 
ATOM   3543  O  O   . LYS D  1 30  ? 9.124   101.667 61.542  1.00 24.85 ? 30  LYS D O   1 
ATOM   3544  C  CB  . LYS D  1 30  ? 8.198   103.543 59.241  1.00 26.16 ? 30  LYS D CB  1 
ATOM   3545  C  CG  . LYS D  1 30  ? 7.425   104.048 58.021  1.00 33.87 ? 30  LYS D CG  1 
ATOM   3546  C  CD  . LYS D  1 30  ? 7.282   105.571 58.018  1.00 39.90 ? 30  LYS D CD  1 
ATOM   3547  C  CE  . LYS D  1 30  ? 6.706   106.106 59.338  1.00 47.36 ? 30  LYS D CE  1 
ATOM   3548  N  NZ  . LYS D  1 30  ? 5.340   105.593 59.662  1.00 39.53 ? 30  LYS D NZ  1 
ATOM   3549  N  N   . VAL D  1 31  ? 10.467  101.103 59.834  1.00 22.15 ? 31  VAL D N   1 
ATOM   3550  C  CA  . VAL D  1 31  ? 11.552  100.676 60.708  1.00 23.27 ? 31  VAL D CA  1 
ATOM   3551  C  C   . VAL D  1 31  ? 12.799  101.495 60.384  1.00 25.32 ? 31  VAL D C   1 
ATOM   3552  O  O   . VAL D  1 31  ? 13.283  101.494 59.254  1.00 27.73 ? 31  VAL D O   1 
ATOM   3553  C  CB  . VAL D  1 31  ? 11.861  99.169  60.554  1.00 23.71 ? 31  VAL D CB  1 
ATOM   3554  C  CG1 . VAL D  1 31  ? 12.817  98.710  61.647  1.00 20.69 ? 31  VAL D CG1 1 
ATOM   3555  C  CG2 . VAL D  1 31  ? 10.577  98.340  60.595  1.00 19.71 ? 31  VAL D CG2 1 
ATOM   3556  N  N   . TRP D  1 32  ? 13.322  102.212 61.364  1.00 25.98 ? 32  TRP D N   1 
ATOM   3557  C  CA  . TRP D  1 32  ? 14.460  103.065 61.086  1.00 25.28 ? 32  TRP D CA  1 
ATOM   3558  C  C   . TRP D  1 32  ? 15.321  103.251 62.330  1.00 29.08 ? 32  TRP D C   1 
ATOM   3559  O  O   . TRP D  1 32  ? 14.823  103.246 63.461  1.00 23.23 ? 32  TRP D O   1 
ATOM   3560  C  CB  . TRP D  1 32  ? 13.991  104.417 60.540  1.00 24.09 ? 32  TRP D CB  1 
ATOM   3561  C  CG  . TRP D  1 32  ? 13.642  105.397 61.605  1.00 26.62 ? 32  TRP D CG  1 
ATOM   3562  C  CD1 . TRP D  1 32  ? 14.465  106.348 62.144  1.00 31.32 ? 32  TRP D CD1 1 
ATOM   3563  C  CD2 . TRP D  1 32  ? 12.391  105.518 62.282  1.00 30.68 ? 32  TRP D CD2 1 
ATOM   3564  N  NE1 . TRP D  1 32  ? 13.797  107.057 63.111  1.00 37.23 ? 32  TRP D NE1 1 
ATOM   3565  C  CE2 . TRP D  1 32  ? 12.520  106.569 63.214  1.00 30.84 ? 32  TRP D CE2 1 
ATOM   3566  C  CE3 . TRP D  1 32  ? 11.166  104.844 62.188  1.00 33.58 ? 32  TRP D CE3 1 
ATOM   3567  C  CZ2 . TRP D  1 32  ? 11.470  106.968 64.048  1.00 33.83 ? 32  TRP D CZ2 1 
ATOM   3568  C  CZ3 . TRP D  1 32  ? 10.124  105.235 63.024  1.00 34.14 ? 32  TRP D CZ3 1 
ATOM   3569  C  CH2 . TRP D  1 32  ? 10.287  106.290 63.943  1.00 31.78 ? 32  TRP D CH2 1 
ATOM   3570  N  N   . GLY D  1 33  ? 16.618  103.426 62.115  1.00 23.73 ? 33  GLY D N   1 
ATOM   3571  C  CA  . GLY D  1 33  ? 17.530  103.595 63.223  1.00 23.77 ? 33  GLY D CA  1 
ATOM   3572  C  C   . GLY D  1 33  ? 18.978  103.515 62.799  1.00 26.84 ? 33  GLY D C   1 
ATOM   3573  O  O   . GLY D  1 33  ? 19.306  103.606 61.615  1.00 28.47 ? 33  GLY D O   1 
ATOM   3574  N  N   . SER D  1 34  ? 19.851  103.342 63.778  1.00 25.76 ? 34  SER D N   1 
ATOM   3575  C  CA  . SER D  1 34  ? 21.267  103.278 63.509  1.00 29.99 ? 34  SER D CA  1 
ATOM   3576  C  C   . SER D  1 34  ? 21.907  102.109 64.249  1.00 28.99 ? 34  SER D C   1 
ATOM   3577  O  O   . SER D  1 34  ? 21.647  101.883 65.424  1.00 28.49 ? 34  SER D O   1 
ATOM   3578  C  CB  . SER D  1 34  ? 21.937  104.587 63.906  1.00 26.47 ? 34  SER D CB  1 
ATOM   3579  O  OG  . SER D  1 34  ? 23.244  104.627 63.369  1.00 34.03 ? 34  SER D OG  1 
ATOM   3580  N  N   . ILE D  1 35  ? 22.733  101.360 63.537  1.00 23.68 ? 35  ILE D N   1 
ATOM   3581  C  CA  . ILE D  1 35  ? 23.524  100.301 64.128  1.00 23.40 ? 35  ILE D CA  1 
ATOM   3582  C  C   . ILE D  1 35  ? 24.970  100.532 63.704  1.00 30.14 ? 35  ILE D C   1 
ATOM   3583  O  O   . ILE D  1 35  ? 25.244  100.848 62.540  1.00 30.15 ? 35  ILE D O   1 
ATOM   3584  C  CB  . ILE D  1 35  ? 23.088  98.944  63.596  1.00 24.84 ? 35  ILE D CB  1 
ATOM   3585  C  CG1 . ILE D  1 35  ? 21.574  98.777  63.715  1.00 23.31 ? 35  ILE D CG1 1 
ATOM   3586  C  CG2 . ILE D  1 35  ? 23.822  97.825  64.297  1.00 20.53 ? 35  ILE D CG2 1 
ATOM   3587  C  CD1 . ILE D  1 35  ? 21.096  97.465  63.128  1.00 17.35 ? 35  ILE D CD1 1 
ATOM   3588  N  N   . LYS D  1 36  ? 25.896  100.388 64.641  1.00 29.44 ? 36  LYS D N   1 
ATOM   3589  C  CA  . LYS D  1 36  ? 27.303  100.597 64.327  1.00 29.83 ? 36  LYS D CA  1 
ATOM   3590  C  C   . LYS D  1 36  ? 28.140  99.410  64.777  1.00 27.90 ? 36  LYS D C   1 
ATOM   3591  O  O   . LYS D  1 36  ? 27.630  98.473  65.399  1.00 25.19 ? 36  LYS D O   1 
ATOM   3592  C  CB  . LYS D  1 36  ? 27.809  101.892 64.971  1.00 30.63 ? 36  LYS D CB  1 
ATOM   3593  C  CG  . LYS D  1 36  ? 27.722  101.876 66.473  1.00 35.28 ? 36  LYS D CG  1 
ATOM   3594  C  CD  . LYS D  1 36  ? 28.263  103.144 67.086  1.00 36.97 ? 36  LYS D CD  1 
ATOM   3595  C  CE  . LYS D  1 36  ? 28.426  102.969 68.591  1.00 32.03 ? 36  LYS D CE  1 
ATOM   3596  N  NZ  . LYS D  1 36  ? 28.564  104.274 69.290  1.00 42.45 ? 36  LYS D NZ  1 
ATOM   3597  N  N   . GLY D  1 37  ? 29.427  99.450  64.441  1.00 30.10 ? 37  GLY D N   1 
ATOM   3598  C  CA  . GLY D  1 37  ? 30.358  98.408  64.827  1.00 22.97 ? 37  GLY D CA  1 
ATOM   3599  C  C   . GLY D  1 37  ? 30.266  97.204  63.928  1.00 25.81 ? 37  GLY D C   1 
ATOM   3600  O  O   . GLY D  1 37  ? 30.811  96.141  64.234  1.00 25.62 ? 37  GLY D O   1 
ATOM   3601  N  N   . LEU D  1 38  ? 29.569  97.366  62.808  1.00 30.60 ? 38  LEU D N   1 
ATOM   3602  C  CA  . LEU D  1 38  ? 29.381  96.272  61.860  1.00 27.46 ? 38  LEU D CA  1 
ATOM   3603  C  C   . LEU D  1 38  ? 30.521  96.197  60.863  1.00 27.47 ? 38  LEU D C   1 
ATOM   3604  O  O   . LEU D  1 38  ? 31.180  97.193  60.590  1.00 26.98 ? 38  LEU D O   1 
ATOM   3605  C  CB  . LEU D  1 38  ? 28.082  96.475  61.094  1.00 30.30 ? 38  LEU D CB  1 
ATOM   3606  C  CG  . LEU D  1 38  ? 26.798  96.404  61.916  1.00 24.97 ? 38  LEU D CG  1 
ATOM   3607  C  CD1 . LEU D  1 38  ? 25.668  97.021  61.109  1.00 21.20 ? 38  LEU D CD1 1 
ATOM   3608  C  CD2 . LEU D  1 38  ? 26.499  94.958  62.260  1.00 19.71 ? 38  LEU D CD2 1 
ATOM   3609  N  N   . THR D  1 39  ? 30.745  95.009  60.313  1.00 27.54 ? 39  THR D N   1 
ATOM   3610  C  CA  . THR D  1 39  ? 31.583  94.882  59.134  1.00 24.36 ? 39  THR D CA  1 
ATOM   3611  C  C   . THR D  1 39  ? 30.806  95.460  57.967  1.00 27.38 ? 39  THR D C   1 
ATOM   3612  O  O   . THR D  1 39  ? 29.571  95.497  57.992  1.00 31.75 ? 39  THR D O   1 
ATOM   3613  C  CB  . THR D  1 39  ? 31.942  93.417  58.828  1.00 26.70 ? 39  THR D CB  1 
ATOM   3614  O  OG1 . THR D  1 39  ? 30.778  92.716  58.391  1.00 24.68 ? 39  THR D OG1 1 
ATOM   3615  C  CG2 . THR D  1 39  ? 32.472  92.738  60.056  1.00 23.60 ? 39  THR D CG2 1 
ATOM   3616  N  N   . GLU D  1 40  ? 31.518  95.914  56.943  1.00 29.54 ? 40  GLU D N   1 
ATOM   3617  C  CA  . GLU D  1 40  ? 30.881  96.590  55.821  1.00 26.25 ? 40  GLU D CA  1 
ATOM   3618  C  C   . GLU D  1 40  ? 30.106  95.568  55.021  1.00 24.95 ? 40  GLU D C   1 
ATOM   3619  O  O   . GLU D  1 40  ? 30.562  94.434  54.859  1.00 21.07 ? 40  GLU D O   1 
ATOM   3620  C  CB  . GLU D  1 40  ? 31.940  97.263  54.941  1.00 30.05 ? 40  GLU D CB  1 
ATOM   3621  C  CG  . GLU D  1 40  ? 31.382  98.165  53.857  1.00 34.96 ? 40  GLU D CG  1 
ATOM   3622  C  CD  . GLU D  1 40  ? 32.467  98.660  52.903  1.00 47.53 ? 40  GLU D CD  1 
ATOM   3623  O  OE1 . GLU D  1 40  ? 33.588  98.092  52.926  1.00 46.66 ? 40  GLU D OE1 1 
ATOM   3624  O  OE2 . GLU D  1 40  ? 32.198  99.612  52.133  1.00 41.41 ? 40  GLU D OE2 1 
ATOM   3625  N  N   . GLY D  1 41  ? 28.938  95.957  54.518  1.00 25.52 ? 41  GLY D N   1 
ATOM   3626  C  CA  . GLY D  1 41  ? 28.124  95.040  53.735  1.00 18.50 ? 41  GLY D CA  1 
ATOM   3627  C  C   . GLY D  1 41  ? 26.804  94.619  54.377  1.00 19.79 ? 41  GLY D C   1 
ATOM   3628  O  O   . GLY D  1 41  ? 26.314  95.251  55.311  1.00 20.46 ? 41  GLY D O   1 
ATOM   3629  N  N   . LEU D  1 42  ? 26.235  93.534  53.859  1.00 22.41 ? 42  LEU D N   1 
ATOM   3630  C  CA  . LEU D  1 42  ? 24.899  93.067  54.228  1.00 20.90 ? 42  LEU D CA  1 
ATOM   3631  C  C   . LEU D  1 42  ? 24.848  92.305  55.567  1.00 20.90 ? 42  LEU D C   1 
ATOM   3632  O  O   . LEU D  1 42  ? 25.661  91.427  55.818  1.00 21.67 ? 42  LEU D O   1 
ATOM   3633  C  CB  . LEU D  1 42  ? 24.394  92.127  53.137  1.00 22.13 ? 42  LEU D CB  1 
ATOM   3634  C  CG  . LEU D  1 42  ? 23.405  92.526  52.040  1.00 23.91 ? 42  LEU D CG  1 
ATOM   3635  C  CD1 . LEU D  1 42  ? 23.067  94.015  52.015  1.00 19.81 ? 42  LEU D CD1 1 
ATOM   3636  C  CD2 . LEU D  1 42  ? 23.958  92.065  50.718  1.00 17.03 ? 42  LEU D CD2 1 
ATOM   3637  N  N   . HIS D  1 43  ? 23.878  92.623  56.415  1.00 20.02 ? 43  HIS D N   1 
ATOM   3638  C  CA  . HIS D  1 43  ? 23.666  91.836  57.630  1.00 19.85 ? 43  HIS D CA  1 
ATOM   3639  C  C   . HIS D  1 43  ? 22.184  91.486  57.770  1.00 20.45 ? 43  HIS D C   1 
ATOM   3640  O  O   . HIS D  1 43  ? 21.338  92.375  57.749  1.00 17.96 ? 43  HIS D O   1 
ATOM   3641  C  CB  . HIS D  1 43  ? 24.163  92.609  58.852  1.00 20.23 ? 43  HIS D CB  1 
ATOM   3642  C  CG  . HIS D  1 43  ? 25.650  92.792  58.882  1.00 25.66 ? 43  HIS D CG  1 
ATOM   3643  N  ND1 . HIS D  1 43  ? 26.499  91.897  59.504  1.00 25.63 ? 43  HIS D ND1 1 
ATOM   3644  C  CD2 . HIS D  1 43  ? 26.442  93.756  58.352  1.00 22.88 ? 43  HIS D CD2 1 
ATOM   3645  C  CE1 . HIS D  1 43  ? 27.748  92.303  59.355  1.00 27.10 ? 43  HIS D CE1 1 
ATOM   3646  N  NE2 . HIS D  1 43  ? 27.743  93.430  58.665  1.00 25.90 ? 43  HIS D NE2 1 
ATOM   3647  N  N   . GLY D  1 44  ? 21.878  90.192  57.872  1.00 19.46 ? 44  GLY D N   1 
ATOM   3648  C  CA  . GLY D  1 44  ? 20.530  89.738  58.195  1.00 15.52 ? 44  GLY D CA  1 
ATOM   3649  C  C   . GLY D  1 44  ? 19.883  90.500  59.344  1.00 19.19 ? 44  GLY D C   1 
ATOM   3650  O  O   . GLY D  1 44  ? 20.539  90.867  60.339  1.00 15.87 ? 44  GLY D O   1 
ATOM   3651  N  N   . PHE D  1 45  ? 18.575  90.721  59.230  1.00 15.89 ? 45  PHE D N   1 
ATOM   3652  C  CA  . PHE D  1 45  ? 17.865  91.593  60.161  1.00 13.48 ? 45  PHE D CA  1 
ATOM   3653  C  C   . PHE D  1 45  ? 16.488  90.984  60.376  1.00 19.67 ? 45  PHE D C   1 
ATOM   3654  O  O   . PHE D  1 45  ? 15.604  91.080  59.506  1.00 14.42 ? 45  PHE D O   1 
ATOM   3655  C  CB  . PHE D  1 45  ? 17.813  93.009  59.573  1.00 12.30 ? 45  PHE D CB  1 
ATOM   3656  C  CG  . PHE D  1 45  ? 17.331  94.087  60.512  1.00 13.64 ? 45  PHE D CG  1 
ATOM   3657  C  CD1 . PHE D  1 45  ? 18.057  94.432  61.640  1.00 14.73 ? 45  PHE D CD1 1 
ATOM   3658  C  CD2 . PHE D  1 45  ? 16.178  94.820  60.207  1.00 12.75 ? 45  PHE D CD2 1 
ATOM   3659  C  CE1 . PHE D  1 45  ? 17.624  95.462  62.491  1.00 18.81 ? 45  PHE D CE1 1 
ATOM   3660  C  CE2 . PHE D  1 45  ? 15.740  95.845  61.029  1.00 15.74 ? 45  PHE D CE2 1 
ATOM   3661  C  CZ  . PHE D  1 45  ? 16.448  96.167  62.191  1.00 16.42 ? 45  PHE D CZ  1 
ATOM   3662  N  N   . HIS D  1 46  ? 16.326  90.342  61.538  1.00 20.67 ? 46  HIS D N   1 
ATOM   3663  C  CA  . HIS D  1 46  ? 15.170  89.491  61.824  1.00 18.60 ? 46  HIS D CA  1 
ATOM   3664  C  C   . HIS D  1 46  ? 14.539  89.755  63.185  1.00 17.25 ? 46  HIS D C   1 
ATOM   3665  O  O   . HIS D  1 46  ? 15.227  90.106  64.138  1.00 17.96 ? 46  HIS D O   1 
ATOM   3666  C  CB  . HIS D  1 46  ? 15.579  88.026  61.816  1.00 18.04 ? 46  HIS D CB  1 
ATOM   3667  C  CG  . HIS D  1 46  ? 16.361  87.618  60.616  1.00 17.25 ? 46  HIS D CG  1 
ATOM   3668  N  ND1 . HIS D  1 46  ? 17.604  87.044  60.709  1.00 17.45 ? 46  HIS D ND1 1 
ATOM   3669  C  CD2 . HIS D  1 46  ? 16.063  87.661  59.297  1.00 17.26 ? 46  HIS D CD2 1 
ATOM   3670  C  CE1 . HIS D  1 46  ? 18.051  86.762  59.499  1.00 18.20 ? 46  HIS D CE1 1 
ATOM   3671  N  NE2 . HIS D  1 46  ? 17.135  87.129  58.623  1.00 19.14 ? 46  HIS D NE2 1 
ATOM   3672  N  N   . VAL D  1 47  ? 13.222  89.559  63.263  1.00 17.41 ? 47  VAL D N   1 
ATOM   3673  C  CA  . VAL D  1 47  ? 12.507  89.525  64.535  1.00 18.48 ? 47  VAL D CA  1 
ATOM   3674  C  C   . VAL D  1 47  ? 12.375  88.067  64.933  1.00 18.08 ? 47  VAL D C   1 
ATOM   3675  O  O   . VAL D  1 47  ? 11.751  87.275  64.209  1.00 18.20 ? 47  VAL D O   1 
ATOM   3676  C  CB  . VAL D  1 47  ? 11.109  90.150  64.412  1.00 19.79 ? 47  VAL D CB  1 
ATOM   3677  C  CG1 . VAL D  1 47  ? 10.380  90.097  65.746  1.00 18.10 ? 47  VAL D CG1 1 
ATOM   3678  C  CG2 . VAL D  1 47  ? 11.227  91.589  63.936  1.00 18.04 ? 47  VAL D CG2 1 
ATOM   3679  N  N   . HIS D  1 48  ? 12.981  87.705  66.062  1.00 16.95 ? 48  HIS D N   1 
ATOM   3680  C  CA  . HIS D  1 48  ? 12.928  86.324  66.549  1.00 17.77 ? 48  HIS D CA  1 
ATOM   3681  C  C   . HIS D  1 48  ? 11.774  86.122  67.518  1.00 18.64 ? 48  HIS D C   1 
ATOM   3682  O  O   . HIS D  1 48  ? 11.303  87.075  68.114  1.00 17.76 ? 48  HIS D O   1 
ATOM   3683  C  CB  . HIS D  1 48  ? 14.245  85.934  67.219  1.00 17.22 ? 48  HIS D CB  1 
ATOM   3684  C  CG  . HIS D  1 48  ? 15.352  85.666  66.256  1.00 19.90 ? 48  HIS D CG  1 
ATOM   3685  N  ND1 . HIS D  1 48  ? 15.913  84.419  66.099  1.00 23.36 ? 48  HIS D ND1 1 
ATOM   3686  C  CD2 . HIS D  1 48  ? 15.988  86.479  65.380  1.00 18.00 ? 48  HIS D CD2 1 
ATOM   3687  C  CE1 . HIS D  1 48  ? 16.862  84.478  65.182  1.00 21.86 ? 48  HIS D CE1 1 
ATOM   3688  N  NE2 . HIS D  1 48  ? 16.930  85.719  64.734  1.00 22.69 ? 48  HIS D NE2 1 
ATOM   3689  N  N   . GLU D  1 49  ? 11.346  84.873  67.691  1.00 20.93 ? 49  GLU D N   1 
ATOM   3690  C  CA  . GLU D  1 49  ? 10.105  84.561  68.428  1.00 26.76 ? 49  GLU D CA  1 
ATOM   3691  C  C   . GLU D  1 49  ? 10.000  85.066  69.883  1.00 24.19 ? 49  GLU D C   1 
ATOM   3692  O  O   . GLU D  1 49  ? 8.983   85.641  70.277  1.00 21.93 ? 49  GLU D O   1 
ATOM   3693  C  CB  . GLU D  1 49  ? 9.819   83.050  68.399  1.00 21.93 ? 49  GLU D CB  1 
ATOM   3694  C  CG  . GLU D  1 49  ? 8.438   82.697  68.919  1.00 22.70 ? 49  GLU D CG  1 
ATOM   3695  C  CD  . GLU D  1 49  ? 8.085   81.246  68.722  1.00 21.50 ? 49  GLU D CD  1 
ATOM   3696  O  OE1 . GLU D  1 49  ? 8.965   80.458  68.320  1.00 26.36 ? 49  GLU D OE1 1 
ATOM   3697  O  OE2 . GLU D  1 49  ? 6.917   80.886  68.976  1.00 28.73 ? 49  GLU D OE2 1 
ATOM   3698  N  N   . PHE D  1 50  ? 11.039  84.845  70.680  1.00 27.59 ? 50  PHE D N   1 
ATOM   3699  C  CA  . PHE D  1 50  ? 10.941  85.134  72.114  1.00 27.71 ? 50  PHE D CA  1 
ATOM   3700  C  C   . PHE D  1 50  ? 11.706  86.380  72.558  1.00 26.18 ? 50  PHE D C   1 
ATOM   3701  O  O   . PHE D  1 50  ? 12.872  86.538  72.226  1.00 27.31 ? 50  PHE D O   1 
ATOM   3702  C  CB  . PHE D  1 50  ? 11.407  83.919  72.915  1.00 25.72 ? 50  PHE D CB  1 
ATOM   3703  C  CG  . PHE D  1 50  ? 10.754  82.643  72.488  1.00 28.35 ? 50  PHE D CG  1 
ATOM   3704  C  CD1 . PHE D  1 50  ? 9.376   82.499  72.564  1.00 22.85 ? 50  PHE D CD1 1 
ATOM   3705  C  CD2 . PHE D  1 50  ? 11.511  81.591  72.002  1.00 25.99 ? 50  PHE D CD2 1 
ATOM   3706  C  CE1 . PHE D  1 50  ? 8.777   81.334  72.165  1.00 26.78 ? 50  PHE D CE1 1 
ATOM   3707  C  CE2 . PHE D  1 50  ? 10.910  80.422  71.600  1.00 26.60 ? 50  PHE D CE2 1 
ATOM   3708  C  CZ  . PHE D  1 50  ? 9.544   80.295  71.679  1.00 25.50 ? 50  PHE D CZ  1 
ATOM   3709  N  N   . GLY D  1 51  ? 11.052  87.250  73.329  1.00 25.77 ? 51  GLY D N   1 
ATOM   3710  C  CA  . GLY D  1 51  ? 11.745  88.371  73.937  1.00 27.05 ? 51  GLY D CA  1 
ATOM   3711  C  C   . GLY D  1 51  ? 12.458  87.911  75.206  1.00 32.45 ? 51  GLY D C   1 
ATOM   3712  O  O   . GLY D  1 51  ? 12.270  88.485  76.277  1.00 29.91 ? 51  GLY D O   1 
ATOM   3713  N  N   . ASP D  1 52  ? 13.279  86.871  75.067  1.00 31.89 ? 52  ASP D N   1 
ATOM   3714  C  CA  . ASP D  1 52  ? 13.925  86.191  76.183  1.00 34.53 ? 52  ASP D CA  1 
ATOM   3715  C  C   . ASP D  1 52  ? 15.436  86.283  76.056  1.00 36.19 ? 52  ASP D C   1 
ATOM   3716  O  O   . ASP D  1 52  ? 16.060  85.521  75.311  1.00 34.20 ? 52  ASP D O   1 
ATOM   3717  C  CB  . ASP D  1 52  ? 13.513  84.711  76.209  1.00 32.22 ? 52  ASP D CB  1 
ATOM   3718  C  CG  . ASP D  1 52  ? 14.130  83.929  77.382  1.00 36.19 ? 52  ASP D CG  1 
ATOM   3719  O  OD1 . ASP D  1 52  ? 15.101  84.401  78.008  1.00 34.02 ? 52  ASP D OD1 1 
ATOM   3720  O  OD2 . ASP D  1 52  ? 13.640  82.817  77.678  1.00 36.94 ? 52  ASP D OD2 1 
ATOM   3721  N  N   . ASN D  1 53  ? 16.022  87.182  76.834  1.00 39.72 ? 53  ASN D N   1 
ATOM   3722  C  CA  . ASN D  1 53  ? 17.460  87.407  76.790  1.00 43.97 ? 53  ASN D CA  1 
ATOM   3723  C  C   . ASN D  1 53  ? 18.240  86.748  77.948  1.00 47.29 ? 53  ASN D C   1 
ATOM   3724  O  O   . ASN D  1 53  ? 19.364  87.151  78.244  1.00 45.14 ? 53  ASN D O   1 
ATOM   3725  C  CB  . ASN D  1 53  ? 17.736  88.917  76.743  1.00 46.17 ? 53  ASN D CB  1 
ATOM   3726  C  CG  . ASN D  1 53  ? 19.139  89.243  76.263  1.00 47.22 ? 53  ASN D CG  1 
ATOM   3727  O  OD1 . ASN D  1 53  ? 19.350  89.598  75.101  1.00 48.46 ? 53  ASN D OD1 1 
ATOM   3728  N  ND2 . ASN D  1 53  ? 20.111  89.122  77.163  1.00 54.00 ? 53  ASN D ND2 1 
ATOM   3729  N  N   . THR D  1 54  ? 17.656  85.736  78.593  1.00 47.32 ? 54  THR D N   1 
ATOM   3730  C  CA  . THR D  1 54  ? 18.323  85.065  79.714  1.00 40.99 ? 54  THR D CA  1 
ATOM   3731  C  C   . THR D  1 54  ? 19.610  84.368  79.280  1.00 50.26 ? 54  THR D C   1 
ATOM   3732  O  O   . THR D  1 54  ? 20.590  84.334  80.027  1.00 48.24 ? 54  THR D O   1 
ATOM   3733  C  CB  . THR D  1 54  ? 17.409  84.044  80.436  1.00 41.39 ? 54  THR D CB  1 
ATOM   3734  O  OG1 . THR D  1 54  ? 17.131  82.932  79.575  1.00 46.09 ? 54  THR D OG1 1 
ATOM   3735  C  CG2 . THR D  1 54  ? 16.104  84.698  80.884  1.00 37.27 ? 54  THR D CG2 1 
ATOM   3736  N  N   . ALA D  1 55  ? 19.607  83.815  78.071  1.00 48.18 ? 55  ALA D N   1 
ATOM   3737  C  CA  . ALA D  1 55  ? 20.806  83.176  77.535  1.00 50.32 ? 55  ALA D CA  1 
ATOM   3738  C  C   . ALA D  1 55  ? 21.477  84.103  76.527  1.00 48.24 ? 55  ALA D C   1 
ATOM   3739  O  O   . ALA D  1 55  ? 22.277  83.674  75.697  1.00 45.79 ? 55  ALA D O   1 
ATOM   3740  C  CB  . ALA D  1 55  ? 20.465  81.833  76.898  1.00 47.78 ? 55  ALA D CB  1 
ATOM   3741  N  N   . GLY D  1 56  ? 21.151  85.386  76.619  1.00 47.44 ? 56  GLY D N   1 
ATOM   3742  C  CA  . GLY D  1 56  ? 21.624  86.348  75.644  1.00 48.59 ? 56  GLY D CA  1 
ATOM   3743  C  C   . GLY D  1 56  ? 20.750  86.330  74.404  1.00 46.36 ? 56  GLY D C   1 
ATOM   3744  O  O   . GLY D  1 56  ? 19.549  86.585  74.488  1.00 46.30 ? 56  GLY D O   1 
ATOM   3745  N  N   . SER D  1 57  ? 21.350  86.021  73.256  1.00 40.50 ? 57  SER D N   1 
ATOM   3746  C  CA  . SER D  1 57  ? 20.630  86.019  71.988  1.00 40.24 ? 57  SER D CA  1 
ATOM   3747  C  C   . SER D  1 57  ? 20.129  84.630  71.616  1.00 40.58 ? 57  SER D C   1 
ATOM   3748  O  O   . SER D  1 57  ? 19.129  84.491  70.910  1.00 36.59 ? 57  SER D O   1 
ATOM   3749  C  CB  . SER D  1 57  ? 21.513  86.568  70.861  1.00 42.26 ? 57  SER D CB  1 
ATOM   3750  O  OG  . SER D  1 57  ? 22.748  85.876  70.789  1.00 45.48 ? 57  SER D OG  1 
ATOM   3751  N  N   . THR D  1 58  ? 20.815  83.602  72.099  1.00 40.77 ? 58  THR D N   1 
ATOM   3752  C  CA  . THR D  1 58  ? 20.505  82.236  71.692  1.00 40.70 ? 58  THR D CA  1 
ATOM   3753  C  C   . THR D  1 58  ? 19.177  81.729  72.247  1.00 36.49 ? 58  THR D C   1 
ATOM   3754  O  O   . THR D  1 58  ? 18.706  80.667  71.849  1.00 34.97 ? 58  THR D O   1 
ATOM   3755  C  CB  . THR D  1 58  ? 21.624  81.263  72.079  1.00 42.30 ? 58  THR D CB  1 
ATOM   3756  O  OG1 . THR D  1 58  ? 21.162  79.919  71.901  1.00 50.17 ? 58  THR D OG1 1 
ATOM   3757  C  CG2 . THR D  1 58  ? 22.009  81.465  73.522  1.00 44.41 ? 58  THR D CG2 1 
ATOM   3758  N  N   . SER D  1 59  ? 18.576  82.493  73.156  1.00 37.25 ? 59  SER D N   1 
ATOM   3759  C  CA  . SER D  1 59  ? 17.282  82.124  73.727  1.00 39.12 ? 59  SER D CA  1 
ATOM   3760  C  C   . SER D  1 59  ? 16.115  82.931  73.140  1.00 36.65 ? 59  SER D C   1 
ATOM   3761  O  O   . SER D  1 59  ? 14.967  82.806  73.584  1.00 32.76 ? 59  SER D O   1 
ATOM   3762  C  CB  . SER D  1 59  ? 17.315  82.237  75.255  1.00 38.98 ? 59  SER D CB  1 
ATOM   3763  O  OG  . SER D  1 59  ? 17.921  83.450  75.664  1.00 43.78 ? 59  SER D OG  1 
ATOM   3764  N  N   . ALA D  1 60  ? 16.407  83.738  72.123  1.00 35.71 ? 60  ALA D N   1 
ATOM   3765  C  CA  . ALA D  1 60  ? 15.374  84.514  71.451  1.00 29.41 ? 60  ALA D CA  1 
ATOM   3766  C  C   . ALA D  1 60  ? 14.523  83.588  70.587  1.00 26.53 ? 60  ALA D C   1 
ATOM   3767  O  O   . ALA D  1 60  ? 13.425  83.950  70.147  1.00 24.43 ? 60  ALA D O   1 
ATOM   3768  C  CB  . ALA D  1 60  ? 15.998  85.615  70.615  1.00 26.79 ? 60  ALA D CB  1 
ATOM   3769  N  N   . GLY D  1 61  ? 15.043  82.387  70.359  1.00 27.58 ? 61  GLY D N   1 
ATOM   3770  C  CA  . GLY D  1 61  ? 14.388  81.408  69.514  1.00 31.02 ? 61  GLY D CA  1 
ATOM   3771  C  C   . GLY D  1 61  ? 14.605  81.610  68.023  1.00 30.57 ? 61  GLY D C   1 
ATOM   3772  O  O   . GLY D  1 61  ? 15.475  82.375  67.596  1.00 22.41 ? 61  GLY D O   1 
ATOM   3773  N  N   . PRO D  1 62  ? 13.791  80.919  67.214  1.00 27.45 ? 62  PRO D N   1 
ATOM   3774  C  CA  . PRO D  1 62  ? 13.832  80.995  65.752  1.00 24.86 ? 62  PRO D CA  1 
ATOM   3775  C  C   . PRO D  1 62  ? 13.176  82.274  65.263  1.00 16.77 ? 62  PRO D C   1 
ATOM   3776  O  O   . PRO D  1 62  ? 12.714  83.084  66.065  1.00 16.40 ? 62  PRO D O   1 
ATOM   3777  C  CB  . PRO D  1 62  ? 12.985  79.797  65.306  1.00 22.85 ? 62  PRO D CB  1 
ATOM   3778  C  CG  . PRO D  1 62  ? 12.531  79.103  66.593  1.00 31.21 ? 62  PRO D CG  1 
ATOM   3779  C  CD  . PRO D  1 62  ? 12.689  80.078  67.693  1.00 25.96 ? 62  PRO D CD  1 
ATOM   3780  N  N   . HIS D  1 63  ? 13.121  82.446  63.947  1.00 19.54 ? 63  HIS D N   1 
ATOM   3781  C  CA  . HIS D  1 63  ? 12.486  83.635  63.383  1.00 20.87 ? 63  HIS D CA  1 
ATOM   3782  C  C   . HIS D  1 63  ? 11.002  83.572  63.755  1.00 17.71 ? 63  HIS D C   1 
ATOM   3783  O  O   . HIS D  1 63  ? 10.425  82.490  63.721  1.00 16.25 ? 63  HIS D O   1 
ATOM   3784  C  CB  . HIS D  1 63  ? 12.681  83.679  61.861  1.00 14.78 ? 63  HIS D CB  1 
ATOM   3785  C  CG  . HIS D  1 63  ? 14.113  83.779  61.439  1.00 19.21 ? 63  HIS D CG  1 
ATOM   3786  N  ND1 . HIS D  1 63  ? 14.504  83.778  60.115  1.00 14.78 ? 63  HIS D ND1 1 
ATOM   3787  C  CD2 . HIS D  1 63  ? 15.250  83.902  62.168  1.00 20.80 ? 63  HIS D CD2 1 
ATOM   3788  C  CE1 . HIS D  1 63  ? 15.819  83.880  60.049  1.00 20.19 ? 63  HIS D CE1 1 
ATOM   3789  N  NE2 . HIS D  1 63  ? 16.297  83.953  61.280  1.00 20.84 ? 63  HIS D NE2 1 
ATOM   3790  N  N   . PHE D  1 64  ? 10.422  84.707  64.151  1.00 14.20 ? 64  PHE D N   1 
ATOM   3791  C  CA  . PHE D  1 64  ? 9.004   84.793  64.468  1.00 16.34 ? 64  PHE D CA  1 
ATOM   3792  C  C   . PHE D  1 64  ? 8.223   84.325  63.261  1.00 17.04 ? 64  PHE D C   1 
ATOM   3793  O  O   . PHE D  1 64  ? 8.272   84.945  62.186  1.00 15.94 ? 64  PHE D O   1 
ATOM   3794  C  CB  . PHE D  1 64  ? 8.609   86.227  64.802  1.00 18.30 ? 64  PHE D CB  1 
ATOM   3795  C  CG  . PHE D  1 64  ? 7.166   86.389  65.216  1.00 21.69 ? 64  PHE D CG  1 
ATOM   3796  C  CD1 . PHE D  1 64  ? 6.501   85.380  65.922  1.00 24.56 ? 64  PHE D CD1 1 
ATOM   3797  C  CD2 . PHE D  1 64  ? 6.476   87.556  64.920  1.00 19.32 ? 64  PHE D CD2 1 
ATOM   3798  C  CE1 . PHE D  1 64  ? 5.157   85.531  66.318  1.00 20.09 ? 64  PHE D CE1 1 
ATOM   3799  C  CE2 . PHE D  1 64  ? 5.146   87.719  65.316  1.00 25.96 ? 64  PHE D CE2 1 
ATOM   3800  C  CZ  . PHE D  1 64  ? 4.482   86.697  66.018  1.00 21.96 ? 64  PHE D CZ  1 
ATOM   3801  N  N   . ASN D  1 65  ? 7.511   83.222  63.444  1.00 15.66 ? 65  ASN D N   1 
ATOM   3802  C  CA  . ASN D  1 65  ? 6.910   82.490  62.345  1.00 18.30 ? 65  ASN D CA  1 
ATOM   3803  C  C   . ASN D  1 65  ? 5.511   81.947  62.708  1.00 19.03 ? 65  ASN D C   1 
ATOM   3804  O  O   . ASN D  1 65  ? 5.294   80.737  62.734  1.00 19.53 ? 65  ASN D O   1 
ATOM   3805  C  CB  . ASN D  1 65  ? 7.866   81.356  61.940  1.00 16.82 ? 65  ASN D CB  1 
ATOM   3806  C  CG  . ASN D  1 65  ? 7.397   80.609  60.706  1.00 17.62 ? 65  ASN D CG  1 
ATOM   3807  O  OD1 . ASN D  1 65  ? 6.601   81.132  59.926  1.00 22.27 ? 65  ASN D OD1 1 
ATOM   3808  N  ND2 . ASN D  1 65  ? 7.863   79.378  60.535  1.00 17.21 ? 65  ASN D ND2 1 
ATOM   3809  N  N   . PRO D  1 66  ? 4.554   82.846  62.995  1.00 17.91 ? 66  PRO D N   1 
ATOM   3810  C  CA  . PRO D  1 66  ? 3.241   82.363  63.435  1.00 24.76 ? 66  PRO D CA  1 
ATOM   3811  C  C   . PRO D  1 66  ? 2.441   81.611  62.367  1.00 25.93 ? 66  PRO D C   1 
ATOM   3812  O  O   . PRO D  1 66  ? 1.480   80.936  62.728  1.00 27.29 ? 66  PRO D O   1 
ATOM   3813  C  CB  . PRO D  1 66  ? 2.513   83.649  63.863  1.00 19.28 ? 66  PRO D CB  1 
ATOM   3814  C  CG  . PRO D  1 66  ? 3.184   84.735  63.098  1.00 22.19 ? 66  PRO D CG  1 
ATOM   3815  C  CD  . PRO D  1 66  ? 4.628   84.320  62.994  1.00 17.23 ? 66  PRO D CD  1 
ATOM   3816  N  N   . LEU D  1 67  ? 2.812   81.705  61.094  1.00 24.98 ? 67  LEU D N   1 
ATOM   3817  C  CA  . LEU D  1 67  ? 2.042   81.019  60.053  1.00 25.39 ? 67  LEU D CA  1 
ATOM   3818  C  C   . LEU D  1 67  ? 2.762   79.793  59.484  1.00 29.37 ? 67  LEU D C   1 
ATOM   3819  O  O   . LEU D  1 67  ? 2.339   79.237  58.472  1.00 27.06 ? 67  LEU D O   1 
ATOM   3820  C  CB  . LEU D  1 67  ? 1.655   81.975  58.931  1.00 23.15 ? 67  LEU D CB  1 
ATOM   3821  C  CG  . LEU D  1 67  ? 1.105   83.343  59.334  1.00 27.27 ? 67  LEU D CG  1 
ATOM   3822  C  CD1 . LEU D  1 67  ? 0.998   84.260  58.127  1.00 25.45 ? 67  LEU D CD1 1 
ATOM   3823  C  CD2 . LEU D  1 67  ? -0.239  83.205  60.039  1.00 30.85 ? 67  LEU D CD2 1 
ATOM   3824  N  N   . SER D  1 68  ? 3.853   79.388  60.128  1.00 23.20 ? 68  SER D N   1 
ATOM   3825  C  CA  . SER D  1 68  ? 4.562   78.166  59.741  1.00 26.58 ? 68  SER D CA  1 
ATOM   3826  C  C   . SER D  1 68  ? 4.941   78.135  58.259  1.00 28.53 ? 68  SER D C   1 
ATOM   3827  O  O   . SER D  1 68  ? 4.773   77.127  57.571  1.00 28.15 ? 68  SER D O   1 
ATOM   3828  C  CB  . SER D  1 68  ? 3.743   76.922  60.117  1.00 26.80 ? 68  SER D CB  1 
ATOM   3829  O  OG  . SER D  1 68  ? 3.458   76.912  61.511  1.00 32.54 ? 68  SER D OG  1 
ATOM   3830  N  N   . ARG D  1 69  ? 5.451   79.253  57.764  1.00 28.59 ? 69  ARG D N   1 
ATOM   3831  C  CA  . ARG D  1 69  ? 5.946   79.290  56.402  1.00 22.67 ? 69  ARG D CA  1 
ATOM   3832  C  C   . ARG D  1 69  ? 7.455   79.038  56.406  1.00 22.57 ? 69  ARG D C   1 
ATOM   3833  O  O   . ARG D  1 69  ? 8.078   78.923  57.461  1.00 21.40 ? 69  ARG D O   1 
ATOM   3834  C  CB  . ARG D  1 69  ? 5.659   80.647  55.768  1.00 25.15 ? 69  ARG D CB  1 
ATOM   3835  C  CG  . ARG D  1 69  ? 4.220   81.149  55.874  1.00 31.56 ? 69  ARG D CG  1 
ATOM   3836  C  CD  . ARG D  1 69  ? 3.193   80.174  55.316  1.00 30.83 ? 69  ARG D CD  1 
ATOM   3837  N  NE  . ARG D  1 69  ? 1.849   80.514  55.796  1.00 36.34 ? 69  ARG D NE  1 
ATOM   3838  C  CZ  . ARG D  1 69  ? 0.792   79.696  55.770  1.00 42.12 ? 69  ARG D CZ  1 
ATOM   3839  N  NH1 . ARG D  1 69  ? 0.898   78.462  55.286  1.00 42.46 ? 69  ARG D NH1 1 
ATOM   3840  N  NH2 . ARG D  1 69  ? -0.377  80.111  56.240  1.00 37.04 ? 69  ARG D NH2 1 
ATOM   3841  N  N   . LYS D  1 70  ? 8.041   78.979  55.219  1.00 23.93 ? 70  LYS D N   1 
ATOM   3842  C  CA  . LYS D  1 70  ? 9.489   78.893  55.087  1.00 25.98 ? 70  LYS D CA  1 
ATOM   3843  C  C   . LYS D  1 70  ? 10.113  80.296  55.139  1.00 19.44 ? 70  LYS D C   1 
ATOM   3844  O  O   . LYS D  1 70  ? 9.410   81.304  54.966  1.00 15.26 ? 70  LYS D O   1 
ATOM   3845  C  CB  . LYS D  1 70  ? 9.869   78.186  53.778  1.00 26.58 ? 70  LYS D CB  1 
ATOM   3846  C  CG  . LYS D  1 70  ? 9.371   76.745  53.656  1.00 25.59 ? 70  LYS D CG  1 
ATOM   3847  C  CD  . LYS D  1 70  ? 9.791   76.156  52.313  1.00 38.68 ? 70  LYS D CD  1 
ATOM   3848  C  CE  . LYS D  1 70  ? 9.096   74.828  52.001  1.00 45.97 ? 70  LYS D CE  1 
ATOM   3849  N  NZ  . LYS D  1 70  ? 9.518   74.290  50.666  1.00 46.57 ? 70  LYS D NZ  1 
ATOM   3850  N  N   . HIS D  1 71  ? 11.422  80.346  55.401  1.00 17.37 ? 71  HIS D N   1 
ATOM   3851  C  CA  . HIS D  1 71  ? 12.175  81.599  55.396  1.00 17.27 ? 71  HIS D CA  1 
ATOM   3852  C  C   . HIS D  1 71  ? 12.197  82.219  53.999  1.00 16.89 ? 71  HIS D C   1 
ATOM   3853  O  O   . HIS D  1 71  ? 12.369  81.516  53.011  1.00 17.88 ? 71  HIS D O   1 
ATOM   3854  C  CB  . HIS D  1 71  ? 13.613  81.369  55.849  1.00 13.03 ? 71  HIS D CB  1 
ATOM   3855  C  CG  . HIS D  1 71  ? 14.434  82.618  55.874  1.00 15.34 ? 71  HIS D CG  1 
ATOM   3856  N  ND1 . HIS D  1 71  ? 14.219  83.629  56.784  1.00 15.55 ? 71  HIS D ND1 1 
ATOM   3857  C  CD2 . HIS D  1 71  ? 15.448  83.036  55.079  1.00 14.05 ? 71  HIS D CD2 1 
ATOM   3858  C  CE1 . HIS D  1 71  ? 15.070  84.613  56.558  1.00 14.36 ? 71  HIS D CE1 1 
ATOM   3859  N  NE2 . HIS D  1 71  ? 15.832  84.275  55.532  1.00 15.06 ? 71  HIS D NE2 1 
ATOM   3860  N  N   . GLY D  1 72  ? 12.017  83.532  53.922  1.00 15.63 ? 72  GLY D N   1 
ATOM   3861  C  CA  . GLY D  1 72  ? 12.220  84.244  52.668  1.00 17.21 ? 72  GLY D CA  1 
ATOM   3862  C  C   . GLY D  1 72  ? 12.699  85.657  52.939  1.00 15.94 ? 72  GLY D C   1 
ATOM   3863  O  O   . GLY D  1 72  ? 13.181  85.948  54.048  1.00 15.63 ? 72  GLY D O   1 
ATOM   3864  N  N   . GLY D  1 73  ? 12.567  86.531  51.943  1.00 11.56 ? 73  GLY D N   1 
ATOM   3865  C  CA  . GLY D  1 73  ? 12.871  87.942  52.106  1.00 13.00 ? 73  GLY D CA  1 
ATOM   3866  C  C   . GLY D  1 73  ? 11.588  88.726  52.328  1.00 15.86 ? 73  GLY D C   1 
ATOM   3867  O  O   . GLY D  1 73  ? 10.506  88.187  52.167  1.00 14.89 ? 73  GLY D O   1 
ATOM   3868  N  N   . PRO D  1 74  ? 11.700  90.007  52.695  1.00 13.69 ? 74  PRO D N   1 
ATOM   3869  C  CA  . PRO D  1 74  ? 10.500  90.757  53.068  1.00 15.42 ? 74  PRO D CA  1 
ATOM   3870  C  C   . PRO D  1 74  ? 9.506   90.885  51.908  1.00 20.21 ? 74  PRO D C   1 
ATOM   3871  O  O   . PRO D  1 74  ? 8.308   90.989  52.178  1.00 17.15 ? 74  PRO D O   1 
ATOM   3872  C  CB  . PRO D  1 74  ? 11.048  92.126  53.483  1.00 14.10 ? 74  PRO D CB  1 
ATOM   3873  C  CG  . PRO D  1 74  ? 12.409  92.215  52.857  1.00 13.10 ? 74  PRO D CG  1 
ATOM   3874  C  CD  . PRO D  1 74  ? 12.924  90.813  52.794  1.00 13.20 ? 74  PRO D CD  1 
ATOM   3875  N  N   . LYS D  1 75  ? 9.987   90.842  50.660  1.00 16.03 ? 75  LYS D N   1 
ATOM   3876  C  CA  . LYS D  1 75  ? 9.122   90.992  49.485  1.00 17.98 ? 75  LYS D CA  1 
ATOM   3877  C  C   . LYS D  1 75  ? 8.360   89.724  49.082  1.00 17.45 ? 75  LYS D C   1 
ATOM   3878  O  O   . LYS D  1 75  ? 7.406   89.808  48.315  1.00 18.14 ? 75  LYS D O   1 
ATOM   3879  C  CB  . LYS D  1 75  ? 9.919   91.516  48.268  1.00 20.58 ? 75  LYS D CB  1 
ATOM   3880  C  CG  . LYS D  1 75  ? 10.587  92.863  48.489  1.00 21.88 ? 75  LYS D CG  1 
ATOM   3881  C  CD  . LYS D  1 75  ? 10.947  93.570  47.193  1.00 32.71 ? 75  LYS D CD  1 
ATOM   3882  C  CE  . LYS D  1 75  ? 11.905  92.766  46.326  1.00 30.82 ? 75  LYS D CE  1 
ATOM   3883  N  NZ  . LYS D  1 75  ? 12.287  93.525  45.082  1.00 32.32 ? 75  LYS D NZ  1 
ATOM   3884  N  N   . ASP D  1 76  ? 8.793   88.562  49.569  1.00 13.69 ? 76  ASP D N   1 
ATOM   3885  C  CA  . ASP D  1 76  ? 8.139   87.294  49.246  1.00 18.85 ? 76  ASP D CA  1 
ATOM   3886  C  C   . ASP D  1 76  ? 6.817   87.102  50.009  1.00 21.26 ? 76  ASP D C   1 
ATOM   3887  O  O   . ASP D  1 76  ? 6.675   87.554  51.140  1.00 16.79 ? 76  ASP D O   1 
ATOM   3888  C  CB  . ASP D  1 76  ? 9.051   86.106  49.592  1.00 15.01 ? 76  ASP D CB  1 
ATOM   3889  C  CG  . ASP D  1 76  ? 10.316  86.056  48.746  1.00 21.84 ? 76  ASP D CG  1 
ATOM   3890  O  OD1 . ASP D  1 76  ? 10.220  86.259  47.515  1.00 24.94 ? 76  ASP D OD1 1 
ATOM   3891  O  OD2 . ASP D  1 76  ? 11.406  85.801  49.310  1.00 15.47 ? 76  ASP D OD2 1 
ATOM   3892  N  N   . GLU D  1 77  ? 5.873   86.399  49.394  1.00 23.40 ? 77  GLU D N   1 
ATOM   3893  C  CA  . GLU D  1 77  ? 4.697   85.908  50.107  1.00 22.49 ? 77  GLU D CA  1 
ATOM   3894  C  C   . GLU D  1 77  ? 5.104   84.808  51.061  1.00 22.46 ? 77  GLU D C   1 
ATOM   3895  O  O   . GLU D  1 77  ? 4.630   84.763  52.195  1.00 18.81 ? 77  GLU D O   1 
ATOM   3896  C  CB  . GLU D  1 77  ? 3.654   85.337  49.143  1.00 25.66 ? 77  GLU D CB  1 
ATOM   3897  C  CG  . GLU D  1 77  ? 2.763   86.382  48.491  1.00 39.07 ? 77  GLU D CG  1 
ATOM   3898  C  CD  . GLU D  1 77  ? 2.134   87.321  49.511  1.00 47.84 ? 77  GLU D CD  1 
ATOM   3899  O  OE1 . GLU D  1 77  ? 1.237   86.869  50.262  1.00 42.03 ? 77  GLU D OE1 1 
ATOM   3900  O  OE2 . GLU D  1 77  ? 2.550   88.507  49.562  1.00 48.06 ? 77  GLU D OE2 1 
ATOM   3901  N  N   . GLU D  1 78  ? 5.951   83.895  50.589  1.00 17.90 ? 78  GLU D N   1 
ATOM   3902  C  CA  . GLU D  1 78  ? 6.436   82.829  51.446  1.00 19.48 ? 78  GLU D CA  1 
ATOM   3903  C  C   . GLU D  1 78  ? 7.613   83.353  52.252  1.00 20.15 ? 78  GLU D C   1 
ATOM   3904  O  O   . GLU D  1 78  ? 8.742   83.390  51.755  1.00 17.53 ? 78  GLU D O   1 
ATOM   3905  C  CB  . GLU D  1 78  ? 6.823   81.594  50.634  1.00 20.45 ? 78  GLU D CB  1 
ATOM   3906  C  CG  . GLU D  1 78  ? 7.253   80.368  51.451  1.00 23.40 ? 78  GLU D CG  1 
ATOM   3907  C  CD  . GLU D  1 78  ? 6.092   79.655  52.172  1.00 30.67 ? 78  GLU D CD  1 
ATOM   3908  O  OE1 . GLU D  1 78  ? 4.937   80.129  52.062  1.00 31.40 ? 78  GLU D OE1 1 
ATOM   3909  O  OE2 . GLU D  1 78  ? 6.339   78.625  52.858  1.00 26.43 ? 78  GLU D OE2 1 
ATOM   3910  N  N   . ARG D  1 79  ? 7.325   83.786  53.483  1.00 18.93 ? 79  ARG D N   1 
ATOM   3911  C  CA  . ARG D  1 79  ? 8.340   84.278  54.418  1.00 16.71 ? 79  ARG D CA  1 
ATOM   3912  C  C   . ARG D  1 79  ? 7.837   84.065  55.833  1.00 18.30 ? 79  ARG D C   1 
ATOM   3913  O  O   . ARG D  1 79  ? 6.670   83.734  56.046  1.00 15.55 ? 79  ARG D O   1 
ATOM   3914  C  CB  . ARG D  1 79  ? 8.589   85.777  54.238  1.00 11.82 ? 79  ARG D CB  1 
ATOM   3915  C  CG  . ARG D  1 79  ? 7.304   86.612  54.336  1.00 14.06 ? 79  ARG D CG  1 
ATOM   3916  C  CD  . ARG D  1 79  ? 7.578   88.099  54.304  1.00 11.92 ? 79  ARG D CD  1 
ATOM   3917  N  NE  . ARG D  1 79  ? 7.827   88.646  55.630  1.00 13.67 ? 79  ARG D NE  1 
ATOM   3918  C  CZ  . ARG D  1 79  ? 7.853   89.945  55.903  1.00 15.51 ? 79  ARG D CZ  1 
ATOM   3919  N  NH1 . ARG D  1 79  ? 7.664   90.845  54.936  1.00 10.41 ? 79  ARG D NH1 1 
ATOM   3920  N  NH2 . ARG D  1 79  ? 8.058   90.344  57.146  1.00 11.20 ? 79  ARG D NH2 1 
ATOM   3921  N  N   . HIS D  1 80  ? 8.741   84.260  56.783  1.00 14.43 ? 80  HIS D N   1 
ATOM   3922  C  CA  . HIS D  1 80  ? 8.420   84.334  58.198  1.00 15.94 ? 80  HIS D CA  1 
ATOM   3923  C  C   . HIS D  1 80  ? 7.963   85.765  58.445  1.00 14.34 ? 80  HIS D C   1 
ATOM   3924  O  O   . HIS D  1 80  ? 8.397   86.687  57.752  1.00 12.73 ? 80  HIS D O   1 
ATOM   3925  C  CB  . HIS D  1 80  ? 9.678   84.029  59.027  1.00 10.55 ? 80  HIS D CB  1 
ATOM   3926  C  CG  . HIS D  1 80  ? 10.221  82.647  58.824  1.00 14.03 ? 80  HIS D CG  1 
ATOM   3927  N  ND1 . HIS D  1 80  ? 11.567  82.355  58.887  1.00 18.95 ? 80  HIS D ND1 1 
ATOM   3928  C  CD2 . HIS D  1 80  ? 9.599   81.475  58.552  1.00 17.48 ? 80  HIS D CD2 1 
ATOM   3929  C  CE1 . HIS D  1 80  ? 11.751  81.063  58.681  1.00 15.80 ? 80  HIS D CE1 1 
ATOM   3930  N  NE2 . HIS D  1 80  ? 10.571  80.504  58.477  1.00 17.29 ? 80  HIS D NE2 1 
ATOM   3931  N  N   . VAL D  1 81  ? 7.099   85.974  59.422  1.00 11.04 ? 81  VAL D N   1 
ATOM   3932  C  CA  . VAL D  1 81  ? 6.704   87.342  59.768  1.00 13.13 ? 81  VAL D CA  1 
ATOM   3933  C  C   . VAL D  1 81  ? 7.920   88.185  60.139  1.00 12.63 ? 81  VAL D C   1 
ATOM   3934  O  O   . VAL D  1 81  ? 7.979   89.371  59.831  1.00 13.53 ? 81  VAL D O   1 
ATOM   3935  C  CB  . VAL D  1 81  ? 5.675   87.365  60.932  1.00 15.89 ? 81  VAL D CB  1 
ATOM   3936  C  CG1 . VAL D  1 81  ? 5.454   88.778  61.439  1.00 15.61 ? 81  VAL D CG1 1 
ATOM   3937  C  CG2 . VAL D  1 81  ? 4.361   86.768  60.468  1.00 17.78 ? 81  VAL D CG2 1 
ATOM   3938  N  N   . GLY D  1 82  ? 8.889   87.565  60.802  1.00 12.47 ? 82  GLY D N   1 
ATOM   3939  C  CA  . GLY D  1 82  ? 10.064  88.275  61.275  1.00 15.98 ? 82  GLY D CA  1 
ATOM   3940  C  C   . GLY D  1 82  ? 11.148  88.499  60.229  1.00 15.21 ? 82  GLY D C   1 
ATOM   3941  O  O   . GLY D  1 82  ? 12.226  88.998  60.558  1.00 15.69 ? 82  GLY D O   1 
ATOM   3942  N  N   . ASP D  1 83  ? 10.878  88.136  58.972  1.00 11.58 ? 83  ASP D N   1 
ATOM   3943  C  CA  . ASP D  1 83  ? 11.905  88.201  57.925  1.00 13.33 ? 83  ASP D CA  1 
ATOM   3944  C  C   . ASP D  1 83  ? 12.009  89.608  57.351  1.00 15.05 ? 83  ASP D C   1 
ATOM   3945  O  O   . ASP D  1 83  ? 11.320  89.937  56.391  1.00 15.86 ? 83  ASP D O   1 
ATOM   3946  C  CB  . ASP D  1 83  ? 11.605  87.200  56.807  1.00 11.78 ? 83  ASP D CB  1 
ATOM   3947  C  CG  . ASP D  1 83  ? 11.878  85.764  57.221  1.00 14.95 ? 83  ASP D CG  1 
ATOM   3948  O  OD1 . ASP D  1 83  ? 12.519  85.539  58.295  1.00 11.29 ? 83  ASP D OD1 1 
ATOM   3949  O  OD2 . ASP D  1 83  ? 11.447  84.860  56.461  1.00 11.31 ? 83  ASP D OD2 1 
ATOM   3950  N  N   . LEU D  1 84  ? 12.844  90.451  57.946  1.00 10.43 ? 84  LEU D N   1 
ATOM   3951  C  CA  . LEU D  1 84  ? 12.949  91.817  57.460  1.00 13.07 ? 84  LEU D CA  1 
ATOM   3952  C  C   . LEU D  1 84  ? 14.130  91.992  56.496  1.00 13.72 ? 84  LEU D C   1 
ATOM   3953  O  O   . LEU D  1 84  ? 14.449  93.099  56.100  1.00 14.69 ? 84  LEU D O   1 
ATOM   3954  C  CB  . LEU D  1 84  ? 13.013  92.831  58.607  1.00 11.56 ? 84  LEU D CB  1 
ATOM   3955  C  CG  . LEU D  1 84  ? 11.786  92.878  59.514  1.00 14.49 ? 84  LEU D CG  1 
ATOM   3956  C  CD1 . LEU D  1 84  ? 12.013  93.878  60.659  1.00 16.89 ? 84  LEU D CD1 1 
ATOM   3957  C  CD2 . LEU D  1 84  ? 10.507  93.213  58.736  1.00 12.51 ? 84  LEU D CD2 1 
ATOM   3958  N  N   . GLY D  1 85  ? 14.749  90.891  56.095  1.00 13.95 ? 85  GLY D N   1 
ATOM   3959  C  CA  . GLY D  1 85  ? 15.778  90.947  55.073  1.00 15.91 ? 85  GLY D CA  1 
ATOM   3960  C  C   . GLY D  1 85  ? 17.131  91.354  55.621  1.00 19.33 ? 85  GLY D C   1 
ATOM   3961  O  O   . GLY D  1 85  ? 17.547  90.907  56.709  1.00 14.26 ? 85  GLY D O   1 
ATOM   3962  N  N   . ASN D  1 86  ? 17.817  92.210  54.869  1.00 13.95 ? 86  ASN D N   1 
ATOM   3963  C  CA  . ASN D  1 86  ? 19.130  92.707  55.266  1.00 12.58 ? 86  ASN D CA  1 
ATOM   3964  C  C   . ASN D  1 86  ? 19.139  94.200  55.570  1.00 15.86 ? 86  ASN D C   1 
ATOM   3965  O  O   . ASN D  1 86  ? 18.317  94.964  55.050  1.00 14.50 ? 86  ASN D O   1 
ATOM   3966  C  CB  . ASN D  1 86  ? 20.155  92.440  54.159  1.00 15.31 ? 86  ASN D CB  1 
ATOM   3967  C  CG  . ASN D  1 86  ? 20.441  90.963  53.960  1.00 15.44 ? 86  ASN D CG  1 
ATOM   3968  O  OD1 . ASN D  1 86  ? 20.991  90.302  54.845  1.00 14.08 ? 86  ASN D OD1 1 
ATOM   3969  N  ND2 . ASN D  1 86  ? 20.108  90.444  52.776  1.00 12.55 ? 86  ASN D ND2 1 
ATOM   3970  N  N   . VAL D  1 87  ? 20.086  94.620  56.404  1.00 17.05 ? 87  VAL D N   1 
ATOM   3971  C  CA  . VAL D  1 87  ? 20.490  96.020  56.440  1.00 16.19 ? 87  VAL D CA  1 
ATOM   3972  C  C   . VAL D  1 87  ? 21.933  96.163  55.921  1.00 20.27 ? 87  VAL D C   1 
ATOM   3973  O  O   . VAL D  1 87  ? 22.702  95.195  55.907  1.00 20.43 ? 87  VAL D O   1 
ATOM   3974  C  CB  . VAL D  1 87  ? 20.382  96.597  57.832  1.00 13.84 ? 87  VAL D CB  1 
ATOM   3975  C  CG1 . VAL D  1 87  ? 18.926  96.602  58.269  1.00 14.74 ? 87  VAL D CG1 1 
ATOM   3976  C  CG2 . VAL D  1 87  ? 21.255  95.800  58.798  1.00 15.14 ? 87  VAL D CG2 1 
ATOM   3977  N  N   . THR D  1 88  ? 22.306  97.362  55.490  1.00 19.42 ? 88  THR D N   1 
ATOM   3978  C  CA  . THR D  1 88  ? 23.636  97.547  54.907  1.00 20.91 ? 88  THR D CA  1 
ATOM   3979  C  C   . THR D  1 88  ? 24.489  98.495  55.726  1.00 21.32 ? 88  THR D C   1 
ATOM   3980  O  O   . THR D  1 88  ? 24.116  99.638  55.957  1.00 19.98 ? 88  THR D O   1 
ATOM   3981  C  CB  . THR D  1 88  ? 23.568  98.067  53.469  1.00 21.81 ? 88  THR D CB  1 
ATOM   3982  O  OG1 . THR D  1 88  ? 22.871  97.118  52.649  1.00 17.16 ? 88  THR D OG1 1 
ATOM   3983  C  CG2 . THR D  1 88  ? 24.981  98.254  52.920  1.00 20.78 ? 88  THR D CG2 1 
ATOM   3984  N  N   . ALA D  1 89  ? 25.626  97.988  56.183  1.00 23.64 ? 89  ALA D N   1 
ATOM   3985  C  CA  . ALA D  1 89  ? 26.624  98.788  56.877  1.00 25.22 ? 89  ALA D CA  1 
ATOM   3986  C  C   . ALA D  1 89  ? 27.520  99.473  55.851  1.00 26.11 ? 89  ALA D C   1 
ATOM   3987  O  O   . ALA D  1 89  ? 27.876  98.864  54.836  1.00 26.37 ? 89  ALA D O   1 
ATOM   3988  C  CB  . ALA D  1 89  ? 27.465  97.891  57.749  1.00 22.27 ? 89  ALA D CB  1 
ATOM   3989  N  N   . ASP D  1 90  ? 27.890  100.724 56.117  1.00 28.77 ? 90  ASP D N   1 
ATOM   3990  C  CA  . ASP D  1 90  ? 28.856  101.427 55.264  1.00 30.98 ? 90  ASP D CA  1 
ATOM   3991  C  C   . ASP D  1 90  ? 30.292  101.078 55.639  1.00 32.09 ? 90  ASP D C   1 
ATOM   3992  O  O   . ASP D  1 90  ? 30.521  100.233 56.505  1.00 28.94 ? 90  ASP D O   1 
ATOM   3993  C  CB  . ASP D  1 90  ? 28.638  102.951 55.278  1.00 29.84 ? 90  ASP D CB  1 
ATOM   3994  C  CG  . ASP D  1 90  ? 28.922  103.598 56.645  1.00 30.64 ? 90  ASP D CG  1 
ATOM   3995  O  OD1 . ASP D  1 90  ? 29.609  103.012 57.509  1.00 33.68 ? 90  ASP D OD1 1 
ATOM   3996  O  OD2 . ASP D  1 90  ? 28.451  104.728 56.857  1.00 34.93 ? 90  ASP D OD2 1 
ATOM   3997  N  N   . LYS D  1 91  ? 31.251  101.741 54.990  1.00 39.38 ? 91  LYS D N   1 
ATOM   3998  C  CA  . LYS D  1 91  ? 32.684  101.549 55.271  1.00 37.50 ? 91  LYS D CA  1 
ATOM   3999  C  C   . LYS D  1 91  ? 33.054  101.777 56.744  1.00 37.53 ? 91  LYS D C   1 
ATOM   4000  O  O   . LYS D  1 91  ? 33.935  101.103 57.280  1.00 38.37 ? 91  LYS D O   1 
ATOM   4001  C  CB  . LYS D  1 91  ? 33.521  102.468 54.381  1.00 40.79 ? 91  LYS D CB  1 
ATOM   4002  C  CG  . LYS D  1 91  ? 34.976  102.060 54.254  1.00 49.91 ? 91  LYS D CG  1 
ATOM   4003  C  CD  . LYS D  1 91  ? 35.095  100.573 53.943  1.00 49.77 ? 91  LYS D CD  1 
ATOM   4004  C  CE  . LYS D  1 91  ? 36.426  100.220 53.283  1.00 52.83 ? 91  LYS D CE  1 
ATOM   4005  N  NZ  . LYS D  1 91  ? 36.418  100.498 51.811  1.00 56.87 ? 91  LYS D NZ  1 
ATOM   4006  N  N   . ASP D  1 92  ? 32.376  102.720 57.394  1.00 33.66 ? 92  ASP D N   1 
ATOM   4007  C  CA  . ASP D  1 92  ? 32.601  103.002 58.810  1.00 35.41 ? 92  ASP D CA  1 
ATOM   4008  C  C   . ASP D  1 92  ? 31.880  102.034 59.739  1.00 37.50 ? 92  ASP D C   1 
ATOM   4009  O  O   . ASP D  1 92  ? 31.855  102.242 60.953  1.00 41.30 ? 92  ASP D O   1 
ATOM   4010  C  CB  . ASP D  1 92  ? 32.119  104.410 59.147  1.00 37.80 ? 92  ASP D CB  1 
ATOM   4011  C  CG  . ASP D  1 92  ? 32.878  105.472 58.400  1.00 44.70 ? 92  ASP D CG  1 
ATOM   4012  O  OD1 . ASP D  1 92  ? 34.009  105.179 57.958  1.00 54.04 ? 92  ASP D OD1 1 
ATOM   4013  O  OD2 . ASP D  1 92  ? 32.351  106.597 58.259  1.00 52.73 ? 92  ASP D OD2 1 
ATOM   4014  N  N   . GLY D  1 93  ? 31.265  101.000 59.176  1.00 34.42 ? 93  GLY D N   1 
ATOM   4015  C  CA  . GLY D  1 93  ? 30.521  100.040 59.975  1.00 29.26 ? 93  GLY D CA  1 
ATOM   4016  C  C   . GLY D  1 93  ? 29.208  100.555 60.534  1.00 27.73 ? 93  GLY D C   1 
ATOM   4017  O  O   . GLY D  1 93  ? 28.684  100.008 61.510  1.00 28.80 ? 93  GLY D O   1 
ATOM   4018  N  N   . VAL D  1 94  ? 28.672  101.605 59.923  1.00 27.01 ? 94  VAL D N   1 
ATOM   4019  C  CA  . VAL D  1 94  ? 27.372  102.131 60.316  1.00 29.21 ? 94  VAL D CA  1 
ATOM   4020  C  C   . VAL D  1 94  ? 26.286  101.718 59.331  1.00 32.04 ? 94  VAL D C   1 
ATOM   4021  O  O   . VAL D  1 94  ? 26.470  101.789 58.108  1.00 27.90 ? 94  VAL D O   1 
ATOM   4022  C  CB  . VAL D  1 94  ? 27.394  103.657 60.457  1.00 29.88 ? 94  VAL D CB  1 
ATOM   4023  C  CG1 . VAL D  1 94  ? 25.980  104.203 60.588  1.00 34.89 ? 94  VAL D CG1 1 
ATOM   4024  C  CG2 . VAL D  1 94  ? 28.245  104.056 61.669  1.00 35.49 ? 94  VAL D CG2 1 
ATOM   4025  N  N   . ALA D  1 95  ? 25.166  101.247 59.869  1.00 28.45 ? 95  ALA D N   1 
ATOM   4026  C  CA  . ALA D  1 95  ? 23.992  100.970 59.044  1.00 25.39 ? 95  ALA D CA  1 
ATOM   4027  C  C   . ALA D  1 95  ? 22.874  101.932 59.413  1.00 29.12 ? 95  ALA D C   1 
ATOM   4028  O  O   . ALA D  1 95  ? 22.340  101.884 60.526  1.00 28.86 ? 95  ALA D O   1 
ATOM   4029  C  CB  . ALA D  1 95  ? 23.538  99.519  59.217  1.00 23.14 ? 95  ALA D CB  1 
ATOM   4030  N  N   . ASP D  1 96  ? 22.525  102.819 58.487  1.00 30.83 ? 96  ASP D N   1 
ATOM   4031  C  CA  . ASP D  1 96  ? 21.416  103.735 58.717  1.00 29.19 ? 96  ASP D CA  1 
ATOM   4032  C  C   . ASP D  1 96  ? 20.144  103.070 58.239  1.00 28.22 ? 96  ASP D C   1 
ATOM   4033  O  O   . ASP D  1 96  ? 19.747  103.199 57.076  1.00 26.44 ? 96  ASP D O   1 
ATOM   4034  C  CB  . ASP D  1 96  ? 21.646  105.069 58.013  1.00 31.09 ? 96  ASP D CB  1 
ATOM   4035  C  CG  . ASP D  1 96  ? 22.824  105.839 58.603  1.00 42.41 ? 96  ASP D CG  1 
ATOM   4036  O  OD1 . ASP D  1 96  ? 22.826  106.076 59.840  1.00 41.36 ? 96  ASP D OD1 1 
ATOM   4037  O  OD2 . ASP D  1 96  ? 23.759  106.177 57.835  1.00 40.49 ? 96  ASP D OD2 1 
ATOM   4038  N  N   . VAL D  1 97  ? 19.515  102.351 59.158  1.00 24.27 ? 97  VAL D N   1 
ATOM   4039  C  CA  . VAL D  1 97  ? 18.416  101.462 58.820  1.00 22.17 ? 97  VAL D CA  1 
ATOM   4040  C  C   . VAL D  1 97  ? 17.172  102.223 58.422  1.00 23.82 ? 97  VAL D C   1 
ATOM   4041  O  O   . VAL D  1 97  ? 16.764  103.171 59.084  1.00 26.27 ? 97  VAL D O   1 
ATOM   4042  C  CB  . VAL D  1 97  ? 18.097  100.531 59.996  1.00 23.11 ? 97  VAL D CB  1 
ATOM   4043  C  CG1 . VAL D  1 97  ? 16.789  99.808  59.772  1.00 18.24 ? 97  VAL D CG1 1 
ATOM   4044  C  CG2 . VAL D  1 97  ? 19.249  99.553  60.208  1.00 18.48 ? 97  VAL D CG2 1 
ATOM   4045  N  N   . SER D  1 98  ? 16.580  101.812 57.317  1.00 22.64 ? 98  SER D N   1 
ATOM   4046  C  CA  . SER D  1 98  ? 15.320  102.371 56.895  1.00 23.51 ? 98  SER D CA  1 
ATOM   4047  C  C   . SER D  1 98  ? 14.604  101.309 56.102  1.00 24.72 ? 98  SER D C   1 
ATOM   4048  O  O   . SER D  1 98  ? 15.021  100.963 54.993  1.00 24.73 ? 98  SER D O   1 
ATOM   4049  C  CB  . SER D  1 98  ? 15.541  103.611 56.038  1.00 30.00 ? 98  SER D CB  1 
ATOM   4050  O  OG  . SER D  1 98  ? 14.319  104.285 55.848  1.00 31.24 ? 98  SER D OG  1 
ATOM   4051  N  N   . ILE D  1 99  ? 13.537  100.778 56.689  1.00 22.84 ? 99  ILE D N   1 
ATOM   4052  C  CA  . ILE D  1 99  ? 12.786  99.679  56.099  1.00 21.47 ? 99  ILE D CA  1 
ATOM   4053  C  C   . ILE D  1 99  ? 11.304  99.953  56.335  1.00 26.44 ? 99  ILE D C   1 
ATOM   4054  O  O   . ILE D  1 99  ? 10.930  100.506 57.364  1.00 25.16 ? 99  ILE D O   1 
ATOM   4055  C  CB  . ILE D  1 99  ? 13.170  98.331  56.765  1.00 22.84 ? 99  ILE D CB  1 
ATOM   4056  C  CG1 . ILE D  1 99  ? 14.568  97.889  56.331  1.00 18.99 ? 99  ILE D CG1 1 
ATOM   4057  C  CG2 . ILE D  1 99  ? 12.160  97.248  56.452  1.00 22.01 ? 99  ILE D CG2 1 
ATOM   4058  C  CD1 . ILE D  1 99  ? 15.116  96.677  57.112  1.00 17.03 ? 99  ILE D CD1 1 
ATOM   4059  N  N   . GLU D  1 100 ? 10.466  99.593  55.373  1.00 23.10 ? 100 GLU D N   1 
ATOM   4060  C  CA  . GLU D  1 100 ? 9.029   99.678  55.562  1.00 22.01 ? 100 GLU D CA  1 
ATOM   4061  C  C   . GLU D  1 100 ? 8.439   98.313  55.270  1.00 19.90 ? 100 GLU D C   1 
ATOM   4062  O  O   . GLU D  1 100 ? 8.750   97.711  54.248  1.00 20.99 ? 100 GLU D O   1 
ATOM   4063  C  CB  . GLU D  1 100 ? 8.437   100.731 54.635  1.00 25.11 ? 100 GLU D CB  1 
ATOM   4064  C  CG  . GLU D  1 100 ? 6.984   101.030 54.903  1.00 29.38 ? 100 GLU D CG  1 
ATOM   4065  C  CD  . GLU D  1 100 ? 6.517   102.275 54.192  1.00 37.65 ? 100 GLU D CD  1 
ATOM   4066  O  OE1 . GLU D  1 100 ? 7.200   103.320 54.312  1.00 43.13 ? 100 GLU D OE1 1 
ATOM   4067  O  OE2 . GLU D  1 100 ? 5.480   102.198 53.500  1.00 36.24 ? 100 GLU D OE2 1 
ATOM   4068  N  N   . ASP D  1 101 ? 7.608   97.801  56.168  1.00 21.56 ? 101 ASP D N   1 
ATOM   4069  C  CA  . ASP D  1 101 ? 7.096   96.443  56.003  1.00 18.76 ? 101 ASP D CA  1 
ATOM   4070  C  C   . ASP D  1 101 ? 5.650   96.303  56.448  1.00 23.58 ? 101 ASP D C   1 
ATOM   4071  O  O   . ASP D  1 101 ? 5.241   96.881  57.469  1.00 18.78 ? 101 ASP D O   1 
ATOM   4072  C  CB  . ASP D  1 101 ? 7.960   95.474  56.796  1.00 16.66 ? 101 ASP D CB  1 
ATOM   4073  C  CG  . ASP D  1 101 ? 7.703   94.041  56.435  1.00 17.75 ? 101 ASP D CG  1 
ATOM   4074  O  OD1 . ASP D  1 101 ? 8.144   93.617  55.345  1.00 19.99 ? 101 ASP D OD1 1 
ATOM   4075  O  OD2 . ASP D  1 101 ? 7.076   93.320  57.241  1.00 19.29 ? 101 ASP D OD2 1 
ATOM   4076  N  N   . SER D  1 102 ? 4.890   95.500  55.707  1.00 18.75 ? 102 SER D N   1 
ATOM   4077  C  CA  . SER D  1 102 ? 3.459   95.374  55.957  1.00 23.68 ? 102 SER D CA  1 
ATOM   4078  C  C   . SER D  1 102 ? 3.055   94.057  56.585  1.00 19.22 ? 102 SER D C   1 
ATOM   4079  O  O   . SER D  1 102 ? 1.878   93.832  56.832  1.00 20.90 ? 102 SER D O   1 
ATOM   4080  C  CB  . SER D  1 102 ? 2.664   95.577  54.660  1.00 22.51 ? 102 SER D CB  1 
ATOM   4081  O  OG  . SER D  1 102 ? 2.547   96.961  54.391  1.00 28.15 ? 102 SER D OG  1 
ATOM   4082  N  N   . VAL D  1 103 ? 4.021   93.184  56.840  1.00 18.48 ? 103 VAL D N   1 
ATOM   4083  C  CA  . VAL D  1 103 ? 3.699   91.873  57.386  1.00 15.81 ? 103 VAL D CA  1 
ATOM   4084  C  C   . VAL D  1 103 ? 3.869   91.868  58.906  1.00 22.01 ? 103 VAL D C   1 
ATOM   4085  O  O   . VAL D  1 103 ? 3.052   91.283  59.629  1.00 23.67 ? 103 VAL D O   1 
ATOM   4086  C  CB  . VAL D  1 103 ? 4.542   90.762  56.739  1.00 17.10 ? 103 VAL D CB  1 
ATOM   4087  C  CG1 . VAL D  1 103 ? 4.211   89.439  57.357  1.00 16.96 ? 103 VAL D CG1 1 
ATOM   4088  C  CG2 . VAL D  1 103 ? 4.268   90.717  55.233  1.00 21.48 ? 103 VAL D CG2 1 
ATOM   4089  N  N   . ILE D  1 104 ? 4.911   92.529  59.401  1.00 17.92 ? 104 ILE D N   1 
ATOM   4090  C  CA  . ILE D  1 104 ? 5.031   92.712  60.842  1.00 20.16 ? 104 ILE D CA  1 
ATOM   4091  C  C   . ILE D  1 104 ? 3.985   93.732  61.237  1.00 22.74 ? 104 ILE D C   1 
ATOM   4092  O  O   . ILE D  1 104 ? 3.527   94.516  60.400  1.00 19.77 ? 104 ILE D O   1 
ATOM   4093  C  CB  . ILE D  1 104 ? 6.418   93.237  61.281  1.00 14.60 ? 104 ILE D CB  1 
ATOM   4094  C  CG1 . ILE D  1 104 ? 6.722   94.587  60.640  1.00 17.06 ? 104 ILE D CG1 1 
ATOM   4095  C  CG2 . ILE D  1 104 ? 7.498   92.234  60.946  1.00 17.28 ? 104 ILE D CG2 1 
ATOM   4096  C  CD1 . ILE D  1 104 ? 7.991   95.247  61.154  1.00 14.92 ? 104 ILE D CD1 1 
ATOM   4097  N  N   . SER D  1 105 ? 3.601   93.719  62.507  1.00 21.64 ? 105 SER D N   1 
ATOM   4098  C  CA  . SER D  1 105 ? 2.699   94.732  63.024  1.00 22.16 ? 105 SER D CA  1 
ATOM   4099  C  C   . SER D  1 105 ? 3.044   95.078  64.476  1.00 24.66 ? 105 SER D C   1 
ATOM   4100  O  O   . SER D  1 105 ? 3.743   94.335  65.166  1.00 24.19 ? 105 SER D O   1 
ATOM   4101  C  CB  . SER D  1 105 ? 1.246   94.260  62.920  1.00 21.04 ? 105 SER D CB  1 
ATOM   4102  O  OG  . SER D  1 105 ? 0.366   95.353  63.094  1.00 24.28 ? 105 SER D OG  1 
ATOM   4103  N  N   . LEU D  1 106 ? 2.562   96.224  64.926  1.00 24.93 ? 106 LEU D N   1 
ATOM   4104  C  CA  . LEU D  1 106 ? 2.719   96.598  66.307  1.00 24.89 ? 106 LEU D CA  1 
ATOM   4105  C  C   . LEU D  1 106 ? 1.431   96.260  67.074  1.00 31.15 ? 106 LEU D C   1 
ATOM   4106  O  O   . LEU D  1 106 ? 1.242   96.728  68.199  1.00 29.15 ? 106 LEU D O   1 
ATOM   4107  C  CB  . LEU D  1 106 ? 3.089   98.077  66.425  1.00 24.12 ? 106 LEU D CB  1 
ATOM   4108  C  CG  . LEU D  1 106 ? 4.408   98.557  65.784  1.00 26.67 ? 106 LEU D CG  1 
ATOM   4109  C  CD1 . LEU D  1 106 ? 4.735   99.991  66.217  1.00 28.30 ? 106 LEU D CD1 1 
ATOM   4110  C  CD2 . LEU D  1 106 ? 5.604   97.627  66.063  1.00 17.95 ? 106 LEU D CD2 1 
ATOM   4111  N  N   . SER D  1 107 ? 0.565   95.439  66.460  1.00 26.49 ? 107 SER D N   1 
ATOM   4112  C  CA  . SER D  1 107 ? -0.625  94.894  67.130  1.00 30.29 ? 107 SER D CA  1 
ATOM   4113  C  C   . SER D  1 107 ? -1.156  93.645  66.440  1.00 31.94 ? 107 SER D C   1 
ATOM   4114  O  O   . SER D  1 107 ? -0.641  93.247  65.401  1.00 30.55 ? 107 SER D O   1 
ATOM   4115  C  CB  . SER D  1 107 ? -1.739  95.928  67.191  1.00 27.11 ? 107 SER D CB  1 
ATOM   4116  O  OG  . SER D  1 107 ? -2.200  96.204  65.892  1.00 30.22 ? 107 SER D OG  1 
ATOM   4117  N  N   . GLY D  1 108 ? -2.197  93.035  67.012  1.00 33.66 ? 108 GLY D N   1 
ATOM   4118  C  CA  . GLY D  1 108 ? -2.775  91.821  66.453  1.00 24.64 ? 108 GLY D CA  1 
ATOM   4119  C  C   . GLY D  1 108 ? -1.790  90.676  66.548  1.00 29.67 ? 108 GLY D C   1 
ATOM   4120  O  O   . GLY D  1 108 ? -0.756  90.808  67.189  1.00 28.81 ? 108 GLY D O   1 
ATOM   4121  N  N   . ASP D  1 109 ? -2.081  89.555  65.901  1.00 27.32 ? 109 ASP D N   1 
ATOM   4122  C  CA  . ASP D  1 109 ? -1.227  88.385  66.058  1.00 29.84 ? 109 ASP D CA  1 
ATOM   4123  C  C   . ASP D  1 109 ? 0.083   88.401  65.249  1.00 30.71 ? 109 ASP D C   1 
ATOM   4124  O  O   . ASP D  1 109 ? 0.883   87.479  65.362  1.00 24.59 ? 109 ASP D O   1 
ATOM   4125  C  CB  . ASP D  1 109 ? -2.015  87.086  65.834  1.00 33.54 ? 109 ASP D CB  1 
ATOM   4126  C  CG  . ASP D  1 109 ? -2.836  87.118  64.587  1.00 38.59 ? 109 ASP D CG  1 
ATOM   4127  O  OD1 . ASP D  1 109 ? -2.341  87.705  63.597  1.00 37.14 ? 109 ASP D OD1 1 
ATOM   4128  O  OD2 . ASP D  1 109 ? -3.972  86.570  64.600  1.00 34.68 ? 109 ASP D OD2 1 
ATOM   4129  N  N   . HIS D  1 110 ? 0.298   89.436  64.440  1.00 24.56 ? 110 HIS D N   1 
ATOM   4130  C  CA  . HIS D  1 110 ? 1.595   89.624  63.795  1.00 30.05 ? 110 HIS D CA  1 
ATOM   4131  C  C   . HIS D  1 110 ? 2.428   90.611  64.613  1.00 26.70 ? 110 HIS D C   1 
ATOM   4132  O  O   . HIS D  1 110 ? 3.472   91.073  64.150  1.00 23.76 ? 110 HIS D O   1 
ATOM   4133  C  CB  . HIS D  1 110 ? 1.451   90.143  62.354  1.00 23.42 ? 110 HIS D CB  1 
ATOM   4134  C  CG  . HIS D  1 110 ? 0.946   89.123  61.382  1.00 29.84 ? 110 HIS D CG  1 
ATOM   4135  N  ND1 . HIS D  1 110 ? 0.785   89.392  60.036  1.00 36.74 ? 110 HIS D ND1 1 
ATOM   4136  C  CD2 . HIS D  1 110 ? 0.574   87.833  61.554  1.00 29.19 ? 110 HIS D CD2 1 
ATOM   4137  C  CE1 . HIS D  1 110 ? 0.337   88.312  59.423  1.00 27.93 ? 110 HIS D CE1 1 
ATOM   4138  N  NE2 . HIS D  1 110 ? 0.191   87.354  60.323  1.00 34.63 ? 110 HIS D NE2 1 
ATOM   4139  N  N   . CYS D  1 111 ? 1.947   90.941  65.814  1.00 22.20 ? 111 CYS D N   1 
ATOM   4140  C  CA  . CYS D  1 111 ? 2.627   91.888  66.699  1.00 25.17 ? 111 CYS D CA  1 
ATOM   4141  C  C   . CYS D  1 111 ? 4.042   91.429  67.005  1.00 21.49 ? 111 CYS D C   1 
ATOM   4142  O  O   . CYS D  1 111 ? 4.275   90.259  67.315  1.00 19.50 ? 111 CYS D O   1 
ATOM   4143  C  CB  . CYS D  1 111 ? 1.860   92.065  68.024  1.00 26.77 ? 111 CYS D CB  1 
ATOM   4144  S  SG  . CYS D  1 111 ? 2.272   93.567  68.969  1.00 27.46 ? 111 CYS D SG  1 
ATOM   4145  N  N   . ILE D  1 112 ? 4.989   92.352  66.927  1.00 20.58 ? 112 ILE D N   1 
ATOM   4146  C  CA  . ILE D  1 112 ? 6.371   92.010  67.255  1.00 21.93 ? 112 ILE D CA  1 
ATOM   4147  C  C   . ILE D  1 112 ? 6.803   92.607  68.599  1.00 22.47 ? 112 ILE D C   1 
ATOM   4148  O  O   . ILE D  1 112 ? 7.925   92.382  69.053  1.00 22.67 ? 112 ILE D O   1 
ATOM   4149  C  CB  . ILE D  1 112 ? 7.324   92.424  66.132  1.00 16.11 ? 112 ILE D CB  1 
ATOM   4150  C  CG1 . ILE D  1 112 ? 7.190   93.923  65.869  1.00 15.91 ? 112 ILE D CG1 1 
ATOM   4151  C  CG2 . ILE D  1 112 ? 6.977   91.646  64.859  1.00 18.16 ? 112 ILE D CG2 1 
ATOM   4152  C  CD1 . ILE D  1 112 ? 8.288   94.488  65.028  1.00 21.76 ? 112 ILE D CD1 1 
ATOM   4153  N  N   . ILE D  1 113 ? 5.913   93.358  69.239  1.00 20.43 ? 113 ILE D N   1 
ATOM   4154  C  CA  . ILE D  1 113 ? 6.222   93.910  70.553  1.00 23.48 ? 113 ILE D CA  1 
ATOM   4155  C  C   . ILE D  1 113 ? 6.435   92.782  71.571  1.00 23.95 ? 113 ILE D C   1 
ATOM   4156  O  O   . ILE D  1 113 ? 5.608   91.889  71.707  1.00 21.64 ? 113 ILE D O   1 
ATOM   4157  C  CB  . ILE D  1 113 ? 5.134   94.872  71.035  1.00 21.76 ? 113 ILE D CB  1 
ATOM   4158  C  CG1 . ILE D  1 113 ? 5.074   96.085  70.114  1.00 23.31 ? 113 ILE D CG1 1 
ATOM   4159  C  CG2 . ILE D  1 113 ? 5.412   95.324  72.470  1.00 26.81 ? 113 ILE D CG2 1 
ATOM   4160  C  CD1 . ILE D  1 113 ? 4.013   97.107  70.503  1.00 25.33 ? 113 ILE D CD1 1 
ATOM   4161  N  N   . GLY D  1 114 ? 7.573   92.799  72.252  1.00 24.92 ? 114 GLY D N   1 
ATOM   4162  C  CA  . GLY D  1 114 ? 7.844   91.784  73.257  1.00 25.13 ? 114 GLY D CA  1 
ATOM   4163  C  C   . GLY D  1 114 ? 8.691   90.661  72.695  1.00 24.13 ? 114 GLY D C   1 
ATOM   4164  O  O   . GLY D  1 114 ? 9.006   89.685  73.385  1.00 23.46 ? 114 GLY D O   1 
ATOM   4165  N  N   . ARG D  1 115 ? 9.070   90.792  71.429  1.00 22.77 ? 115 ARG D N   1 
ATOM   4166  C  CA  . ARG D  1 115 ? 9.958   89.811  70.819  1.00 19.70 ? 115 ARG D CA  1 
ATOM   4167  C  C   . ARG D  1 115 ? 11.325  90.439  70.593  1.00 21.01 ? 115 ARG D C   1 
ATOM   4168  O  O   . ARG D  1 115 ? 11.558  91.587  70.975  1.00 26.34 ? 115 ARG D O   1 
ATOM   4169  C  CB  . ARG D  1 115 ? 9.334   89.264  69.537  1.00 26.69 ? 115 ARG D CB  1 
ATOM   4170  C  CG  . ARG D  1 115 ? 7.930   88.718  69.790  1.00 26.25 ? 115 ARG D CG  1 
ATOM   4171  C  CD  . ARG D  1 115 ? 7.291   88.171  68.546  1.00 24.60 ? 115 ARG D CD  1 
ATOM   4172  N  NE  . ARG D  1 115 ? 5.861   87.937  68.741  1.00 27.67 ? 115 ARG D NE  1 
ATOM   4173  C  CZ  . ARG D  1 115 ? 5.345   86.841  69.289  1.00 26.72 ? 115 ARG D CZ  1 
ATOM   4174  N  NH1 . ARG D  1 115 ? 6.137   85.870  69.715  1.00 24.04 ? 115 ARG D NH1 1 
ATOM   4175  N  NH2 . ARG D  1 115 ? 4.029   86.717  69.407  1.00 26.45 ? 115 ARG D NH2 1 
ATOM   4176  N  N   . THR D  1 116 ? 12.232  89.696  69.980  1.00 20.06 ? 116 THR D N   1 
ATOM   4177  C  CA  . THR D  1 116 ? 13.626  90.108  69.933  1.00 23.28 ? 116 THR D CA  1 
ATOM   4178  C  C   . THR D  1 116 ? 14.074  90.477  68.511  1.00 22.66 ? 116 THR D C   1 
ATOM   4179  O  O   . THR D  1 116 ? 13.988  89.665  67.590  1.00 17.30 ? 116 THR D O   1 
ATOM   4180  C  CB  . THR D  1 116 ? 14.529  88.995  70.516  1.00 20.56 ? 116 THR D CB  1 
ATOM   4181  O  OG1 . THR D  1 116 ? 14.169  88.771  71.881  1.00 24.67 ? 116 THR D OG1 1 
ATOM   4182  C  CG2 . THR D  1 116 ? 16.003  89.372  70.449  1.00 22.37 ? 116 THR D CG2 1 
ATOM   4183  N  N   . LEU D  1 117 ? 14.511  91.721  68.342  1.00 19.71 ? 117 LEU D N   1 
ATOM   4184  C  CA  . LEU D  1 117 ? 15.152  92.140  67.104  1.00 18.98 ? 117 LEU D CA  1 
ATOM   4185  C  C   . LEU D  1 117 ? 16.602  91.644  67.138  1.00 22.08 ? 117 LEU D C   1 
ATOM   4186  O  O   . LEU D  1 117 ? 17.263  91.745  68.176  1.00 20.18 ? 117 LEU D O   1 
ATOM   4187  C  CB  . LEU D  1 117 ? 15.115  93.665  66.984  1.00 17.22 ? 117 LEU D CB  1 
ATOM   4188  C  CG  . LEU D  1 117 ? 15.592  94.231  65.645  1.00 18.12 ? 117 LEU D CG  1 
ATOM   4189  C  CD1 . LEU D  1 117 ? 14.789  93.598  64.526  1.00 13.86 ? 117 LEU D CD1 1 
ATOM   4190  C  CD2 . LEU D  1 117 ? 15.470  95.743  65.616  1.00 16.85 ? 117 LEU D CD2 1 
ATOM   4191  N  N   . VAL D  1 118 ? 17.088  91.083  66.032  1.00 18.38 ? 118 VAL D N   1 
ATOM   4192  C  CA  . VAL D  1 118 ? 18.468  90.600  65.972  1.00 15.53 ? 118 VAL D CA  1 
ATOM   4193  C  C   . VAL D  1 118 ? 19.151  91.069  64.685  1.00 24.44 ? 118 VAL D C   1 
ATOM   4194  O  O   . VAL D  1 118 ? 18.553  91.022  63.593  1.00 21.84 ? 118 VAL D O   1 
ATOM   4195  C  CB  . VAL D  1 118 ? 18.531  89.053  65.998  1.00 18.37 ? 118 VAL D CB  1 
ATOM   4196  C  CG1 . VAL D  1 118 ? 19.960  88.560  65.937  1.00 19.22 ? 118 VAL D CG1 1 
ATOM   4197  C  CG2 . VAL D  1 118 ? 17.837  88.492  67.223  1.00 19.49 ? 118 VAL D CG2 1 
ATOM   4198  N  N   . VAL D  1 119 ? 20.402  91.510  64.802  1.00 19.49 ? 119 VAL D N   1 
ATOM   4199  C  CA  . VAL D  1 119 ? 21.220  91.785  63.627  1.00 20.65 ? 119 VAL D CA  1 
ATOM   4200  C  C   . VAL D  1 119 ? 22.296  90.707  63.547  1.00 22.39 ? 119 VAL D C   1 
ATOM   4201  O  O   . VAL D  1 119 ? 22.936  90.374  64.546  1.00 23.69 ? 119 VAL D O   1 
ATOM   4202  C  CB  . VAL D  1 119 ? 21.782  93.229  63.621  1.00 20.52 ? 119 VAL D CB  1 
ATOM   4203  C  CG1 . VAL D  1 119 ? 22.756  93.469  64.774  1.00 21.37 ? 119 VAL D CG1 1 
ATOM   4204  C  CG2 . VAL D  1 119 ? 22.440  93.533  62.297  1.00 24.32 ? 119 VAL D CG2 1 
ATOM   4205  N  N   . HIS D  1 120 ? 22.456  90.127  62.364  1.00 20.50 ? 120 HIS D N   1 
ATOM   4206  C  CA  . HIS D  1 120 ? 23.296  88.950  62.191  1.00 20.75 ? 120 HIS D CA  1 
ATOM   4207  C  C   . HIS D  1 120 ? 24.656  89.203  61.594  1.00 22.65 ? 120 HIS D C   1 
ATOM   4208  O  O   . HIS D  1 120 ? 24.907  90.239  60.984  1.00 20.63 ? 120 HIS D O   1 
ATOM   4209  C  CB  . HIS D  1 120 ? 22.614  87.929  61.301  1.00 18.85 ? 120 HIS D CB  1 
ATOM   4210  C  CG  . HIS D  1 120 ? 21.565  87.138  62.000  1.00 21.80 ? 120 HIS D CG  1 
ATOM   4211  N  ND1 . HIS D  1 120 ? 21.780  85.853  62.451  1.00 22.16 ? 120 HIS D ND1 1 
ATOM   4212  C  CD2 . HIS D  1 120 ? 20.299  87.457  62.348  1.00 19.58 ? 120 HIS D CD2 1 
ATOM   4213  C  CE1 . HIS D  1 120 ? 20.685  85.410  63.037  1.00 24.81 ? 120 HIS D CE1 1 
ATOM   4214  N  NE2 . HIS D  1 120 ? 19.774  86.366  62.992  1.00 22.64 ? 120 HIS D NE2 1 
ATOM   4215  N  N   . GLU D  1 121 ? 25.490  88.178  61.738  1.00 25.02 ? 121 GLU D N   1 
ATOM   4216  C  CA  . GLU D  1 121 ? 26.878  88.145  61.301  1.00 24.76 ? 121 GLU D CA  1 
ATOM   4217  C  C   . GLU D  1 121 ? 27.050  88.279  59.794  1.00 25.22 ? 121 GLU D C   1 
ATOM   4218  O  O   . GLU D  1 121 ? 27.913  89.026  59.331  1.00 22.24 ? 121 GLU D O   1 
ATOM   4219  C  CB  . GLU D  1 121 ? 27.508  86.827  61.768  1.00 28.12 ? 121 GLU D CB  1 
ATOM   4220  C  CG  . GLU D  1 121 ? 28.955  86.617  61.351  1.00 30.40 ? 121 GLU D CG  1 
ATOM   4221  C  CD  . GLU D  1 121 ? 29.305  85.144  61.246  1.00 34.48 ? 121 GLU D CD  1 
ATOM   4222  O  OE1 . GLU D  1 121 ? 30.362  84.830  60.657  1.00 44.62 ? 121 GLU D OE1 1 
ATOM   4223  O  OE2 . GLU D  1 121 ? 28.517  84.297  61.730  1.00 30.41 ? 121 GLU D OE2 1 
ATOM   4224  N  N   . LYS D  1 122 ? 26.232  87.545  59.043  1.00 24.06 ? 122 LYS D N   1 
ATOM   4225  C  CA  . LYS D  1 122 ? 26.319  87.498  57.589  1.00 22.39 ? 122 LYS D CA  1 
ATOM   4226  C  C   . LYS D  1 122 ? 25.027  87.976  56.905  1.00 25.58 ? 122 LYS D C   1 
ATOM   4227  O  O   . LYS D  1 122 ? 24.016  88.261  57.552  1.00 20.62 ? 122 LYS D O   1 
ATOM   4228  C  CB  . LYS D  1 122 ? 26.630  86.068  57.133  1.00 24.30 ? 122 LYS D CB  1 
ATOM   4229  C  CG  . LYS D  1 122 ? 27.948  85.504  57.690  1.00 32.73 ? 122 LYS D CG  1 
ATOM   4230  C  CD  . LYS D  1 122 ? 28.417  84.250  56.941  1.00 32.19 ? 122 LYS D CD  1 
ATOM   4231  C  CE  . LYS D  1 122 ? 27.747  82.972  57.470  1.00 40.74 ? 122 LYS D CE  1 
ATOM   4232  N  NZ  . LYS D  1 122 ? 28.226  81.734  56.767  1.00 42.88 ? 122 LYS D NZ  1 
ATOM   4233  N  N   . ALA D  1 123 ? 25.080  88.050  55.581  1.00 23.24 ? 123 ALA D N   1 
ATOM   4234  C  CA  . ALA D  1 123 ? 23.929  88.408  54.774  1.00 18.17 ? 123 ALA D CA  1 
ATOM   4235  C  C   . ALA D  1 123 ? 22.840  87.346  54.884  1.00 18.80 ? 123 ALA D C   1 
ATOM   4236  O  O   . ALA D  1 123 ? 23.127  86.153  54.939  1.00 17.37 ? 123 ALA D O   1 
ATOM   4237  C  CB  . ALA D  1 123 ? 24.351  88.563  53.313  1.00 19.23 ? 123 ALA D CB  1 
ATOM   4238  N  N   . ASP D  1 124 ? 21.588  87.791  54.899  1.00 16.18 ? 124 ASP D N   1 
ATOM   4239  C  CA  . ASP D  1 124 ? 20.462  86.883  54.749  1.00 15.84 ? 124 ASP D CA  1 
ATOM   4240  C  C   . ASP D  1 124 ? 20.336  86.614  53.252  1.00 14.90 ? 124 ASP D C   1 
ATOM   4241  O  O   . ASP D  1 124 ? 20.267  87.561  52.468  1.00 13.64 ? 124 ASP D O   1 
ATOM   4242  C  CB  . ASP D  1 124 ? 19.210  87.555  55.321  1.00 14.05 ? 124 ASP D CB  1 
ATOM   4243  C  CG  . ASP D  1 124 ? 17.951  86.728  55.152  1.00 14.29 ? 124 ASP D CG  1 
ATOM   4244  O  OD1 . ASP D  1 124 ? 17.891  85.814  54.299  1.00 14.87 ? 124 ASP D OD1 1 
ATOM   4245  O  OD2 . ASP D  1 124 ? 16.999  86.999  55.902  1.00 15.22 ? 124 ASP D OD2 1 
ATOM   4246  N  N   . ASP D  1 125 ? 20.316  85.341  52.845  1.00 15.00 ? 125 ASP D N   1 
ATOM   4247  C  CA  . ASP D  1 125 ? 20.167  85.018  51.419  1.00 13.22 ? 125 ASP D CA  1 
ATOM   4248  C  C   . ASP D  1 125 ? 18.722  85.005  50.947  1.00 15.14 ? 125 ASP D C   1 
ATOM   4249  O  O   . ASP D  1 125 ? 18.440  84.578  49.823  1.00 11.84 ? 125 ASP D O   1 
ATOM   4250  C  CB  . ASP D  1 125 ? 20.871  83.706  51.034  1.00 14.05 ? 125 ASP D CB  1 
ATOM   4251  C  CG  . ASP D  1 125 ? 20.205  82.445  51.613  1.00 17.16 ? 125 ASP D CG  1 
ATOM   4252  O  OD1 . ASP D  1 125 ? 19.019  82.447  52.063  1.00 12.83 ? 125 ASP D OD1 1 
ATOM   4253  O  OD2 . ASP D  1 125 ? 20.894  81.401  51.560  1.00 19.39 ? 125 ASP D OD2 1 
ATOM   4254  N  N   . LEU D  1 126 ? 17.816  85.446  51.821  1.00 14.71 ? 126 LEU D N   1 
ATOM   4255  C  CA  . LEU D  1 126 ? 16.394  85.597  51.467  1.00 15.97 ? 126 LEU D CA  1 
ATOM   4256  C  C   . LEU D  1 126 ? 15.743  84.310  50.944  1.00 13.18 ? 126 LEU D C   1 
ATOM   4257  O  O   . LEU D  1 126 ? 14.851  84.361  50.094  1.00 16.32 ? 126 LEU D O   1 
ATOM   4258  C  CB  . LEU D  1 126 ? 16.207  86.755  50.468  1.00 14.25 ? 126 LEU D CB  1 
ATOM   4259  C  CG  . LEU D  1 126 ? 16.976  88.057  50.816  1.00 16.88 ? 126 LEU D CG  1 
ATOM   4260  C  CD1 . LEU D  1 126 ? 16.844  89.112  49.707  1.00 17.10 ? 126 LEU D CD1 1 
ATOM   4261  C  CD2 . LEU D  1 126 ? 16.560  88.656  52.159  1.00 11.70 ? 126 LEU D CD2 1 
ATOM   4262  N  N   . GLY D  1 127 ? 16.183  83.163  51.460  1.00 14.27 ? 127 GLY D N   1 
ATOM   4263  C  CA  . GLY D  1 127 ? 15.623  81.866  51.101  1.00 10.39 ? 127 GLY D CA  1 
ATOM   4264  C  C   . GLY D  1 127 ? 16.023  81.321  49.739  1.00 16.19 ? 127 GLY D C   1 
ATOM   4265  O  O   . GLY D  1 127 ? 15.477  80.320  49.260  1.00 12.01 ? 127 GLY D O   1 
ATOM   4266  N  N   . LYS D  1 128 ? 17.004  81.951  49.105  1.00 15.07 ? 128 LYS D N   1 
ATOM   4267  C  CA  . LYS D  1 128 ? 17.384  81.536  47.752  1.00 18.69 ? 128 LYS D CA  1 
ATOM   4268  C  C   . LYS D  1 128 ? 18.670  80.720  47.698  1.00 18.49 ? 128 LYS D C   1 
ATOM   4269  O  O   . LYS D  1 128 ? 19.199  80.480  46.624  1.00 17.49 ? 128 LYS D O   1 
ATOM   4270  C  CB  . LYS D  1 128 ? 17.494  82.770  46.852  1.00 18.63 ? 128 LYS D CB  1 
ATOM   4271  C  CG  . LYS D  1 128 ? 16.271  83.699  47.013  1.00 19.43 ? 128 LYS D CG  1 
ATOM   4272  C  CD  . LYS D  1 128 ? 16.331  84.918  46.113  1.00 20.38 ? 128 LYS D CD  1 
ATOM   4273  C  CE  . LYS D  1 128 ? 16.325  84.518  44.643  1.00 24.03 ? 128 LYS D CE  1 
ATOM   4274  N  NZ  . LYS D  1 128 ? 16.479  85.718  43.785  1.00 29.48 ? 128 LYS D NZ  1 
ATOM   4275  N  N   . GLY D  1 129 ? 19.161  80.285  48.858  1.00 15.72 ? 129 GLY D N   1 
ATOM   4276  C  CA  . GLY D  1 129 ? 20.461  79.635  48.943  1.00 13.97 ? 129 GLY D CA  1 
ATOM   4277  C  C   . GLY D  1 129 ? 20.520  78.191  48.484  1.00 14.33 ? 129 GLY D C   1 
ATOM   4278  O  O   . GLY D  1 129 ? 21.602  77.674  48.233  1.00 15.12 ? 129 GLY D O   1 
ATOM   4279  N  N   . GLY D  1 130 ? 19.368  77.537  48.359  1.00 13.34 ? 130 GLY D N   1 
ATOM   4280  C  CA  . GLY D  1 130 ? 19.319  76.155  47.898  1.00 12.53 ? 130 GLY D CA  1 
ATOM   4281  C  C   . GLY D  1 130 ? 19.661  75.090  48.936  1.00 13.41 ? 130 GLY D C   1 
ATOM   4282  O  O   . GLY D  1 130 ? 19.648  73.908  48.645  1.00 15.42 ? 130 GLY D O   1 
ATOM   4283  N  N   . ASN D  1 131 ? 19.972  75.488  50.162  1.00 16.13 ? 131 ASN D N   1 
ATOM   4284  C  CA  . ASN D  1 131 ? 20.241  74.486  51.183  1.00 17.40 ? 131 ASN D CA  1 
ATOM   4285  C  C   . ASN D  1 131 ? 19.220  74.511  52.293  1.00 18.73 ? 131 ASN D C   1 
ATOM   4286  O  O   . ASN D  1 131 ? 18.440  75.455  52.416  1.00 19.47 ? 131 ASN D O   1 
ATOM   4287  C  CB  . ASN D  1 131 ? 21.674  74.583  51.748  1.00 14.37 ? 131 ASN D CB  1 
ATOM   4288  C  CG  . ASN D  1 131 ? 21.916  75.850  52.533  1.00 19.42 ? 131 ASN D CG  1 
ATOM   4289  O  OD1 . ASN D  1 131 ? 21.034  76.701  52.655  1.00 19.69 ? 131 ASN D OD1 1 
ATOM   4290  N  ND2 . ASN D  1 131 ? 23.120  75.973  53.110  1.00 16.24 ? 131 ASN D ND2 1 
ATOM   4291  N  N   . GLU D  1 132 ? 19.251  73.467  53.111  1.00 24.10 ? 132 GLU D N   1 
ATOM   4292  C  CA  . GLU D  1 132 ? 18.317  73.292  54.217  1.00 22.32 ? 132 GLU D CA  1 
ATOM   4293  C  C   . GLU D  1 132 ? 18.271  74.543  55.083  1.00 19.13 ? 132 GLU D C   1 
ATOM   4294  O  O   . GLU D  1 132 ? 17.216  75.079  55.381  1.00 17.98 ? 132 GLU D O   1 
ATOM   4295  C  CB  . GLU D  1 132 ? 18.752  72.068  55.024  1.00 23.39 ? 132 GLU D CB  1 
ATOM   4296  C  CG  . GLU D  1 132 ? 17.963  71.809  56.275  1.00 34.87 ? 132 GLU D CG  1 
ATOM   4297  C  CD  . GLU D  1 132 ? 18.491  70.591  57.026  1.00 38.23 ? 132 GLU D CD  1 
ATOM   4298  O  OE1 . GLU D  1 132 ? 19.149  69.736  56.379  1.00 38.86 ? 132 GLU D OE1 1 
ATOM   4299  O  OE2 . GLU D  1 132 ? 18.248  70.503  58.253  1.00 36.55 ? 132 GLU D OE2 1 
ATOM   4300  N  N   . GLU D  1 133 ? 19.440  75.042  55.432  1.00 17.01 ? 133 GLU D N   1 
ATOM   4301  C  CA  . GLU D  1 133 ? 19.540  76.248  56.240  1.00 18.50 ? 133 GLU D CA  1 
ATOM   4302  C  C   . GLU D  1 133 ? 18.899  77.513  55.603  1.00 21.45 ? 133 GLU D C   1 
ATOM   4303  O  O   . GLU D  1 133 ? 18.262  78.302  56.307  1.00 18.75 ? 133 GLU D O   1 
ATOM   4304  C  CB  . GLU D  1 133 ? 21.015  76.477  56.603  1.00 20.43 ? 133 GLU D CB  1 
ATOM   4305  C  CG  . GLU D  1 133 ? 21.251  77.617  57.559  1.00 26.33 ? 133 GLU D CG  1 
ATOM   4306  C  CD  . GLU D  1 133 ? 20.921  77.288  59.012  1.00 36.62 ? 133 GLU D CD  1 
ATOM   4307  O  OE1 . GLU D  1 133 ? 20.257  76.253  59.306  1.00 30.71 ? 133 GLU D OE1 1 
ATOM   4308  O  OE2 . GLU D  1 133 ? 21.340  78.102  59.865  1.00 41.64 ? 133 GLU D OE2 1 
ATOM   4309  N  N   . SER D  1 134 ? 19.061  77.703  54.287  1.00 18.63 ? 134 SER D N   1 
ATOM   4310  C  CA  . SER D  1 134 ? 18.440  78.851  53.604  1.00 18.91 ? 134 SER D CA  1 
ATOM   4311  C  C   . SER D  1 134 ? 16.929  78.916  53.853  1.00 17.70 ? 134 SER D C   1 
ATOM   4312  O  O   . SER D  1 134 ? 16.382  79.990  54.080  1.00 17.60 ? 134 SER D O   1 
ATOM   4313  C  CB  . SER D  1 134 ? 18.711  78.830  52.094  1.00 16.90 ? 134 SER D CB  1 
ATOM   4314  O  OG  . SER D  1 134 ? 18.165  79.983  51.466  1.00 15.60 ? 134 SER D OG  1 
ATOM   4315  N  N   . THR D  1 135 ? 16.268  77.765  53.844  1.00 16.25 ? 135 THR D N   1 
ATOM   4316  C  CA  . THR D  1 135 ? 14.828  77.694  54.145  1.00 20.13 ? 135 THR D CA  1 
ATOM   4317  C  C   . THR D  1 135 ? 14.467  78.014  55.603  1.00 18.54 ? 135 THR D C   1 
ATOM   4318  O  O   . THR D  1 135 ? 13.288  78.208  55.920  1.00 20.72 ? 135 THR D O   1 
ATOM   4319  C  CB  . THR D  1 135 ? 14.238  76.291  53.844  1.00 21.39 ? 135 THR D CB  1 
ATOM   4320  O  OG1 . THR D  1 135 ? 14.681  75.358  54.846  1.00 26.49 ? 135 THR D OG1 1 
ATOM   4321  C  CG2 . THR D  1 135 ? 14.664  75.787  52.476  1.00 15.67 ? 135 THR D CG2 1 
ATOM   4322  N  N   . LYS D  1 136 ? 15.463  78.067  56.490  1.00 19.99 ? 136 LYS D N   1 
ATOM   4323  C  CA  . LYS D  1 136 ? 15.191  78.315  57.914  1.00 20.32 ? 136 LYS D CA  1 
ATOM   4324  C  C   . LYS D  1 136 ? 15.689  79.667  58.406  1.00 19.57 ? 136 LYS D C   1 
ATOM   4325  O  O   . LYS D  1 136 ? 14.929  80.437  58.975  1.00 18.04 ? 136 LYS D O   1 
ATOM   4326  C  CB  . LYS D  1 136 ? 15.802  77.220  58.789  1.00 23.46 ? 136 LYS D CB  1 
ATOM   4327  C  CG  . LYS D  1 136 ? 15.134  75.849  58.660  1.00 26.15 ? 136 LYS D CG  1 
ATOM   4328  C  CD  . LYS D  1 136 ? 15.904  74.822  59.477  1.00 31.30 ? 136 LYS D CD  1 
ATOM   4329  C  CE  . LYS D  1 136 ? 15.446  73.397  59.208  1.00 34.10 ? 136 LYS D CE  1 
ATOM   4330  N  NZ  . LYS D  1 136 ? 16.257  72.426  60.021  1.00 39.37 ? 136 LYS D NZ  1 
ATOM   4331  N  N   . THR D  1 137 ? 16.976  79.939  58.196  1.00 19.19 ? 137 THR D N   1 
ATOM   4332  C  CA  . THR D  1 137 ? 17.598  81.154  58.703  1.00 19.15 ? 137 THR D CA  1 
ATOM   4333  C  C   . THR D  1 137 ? 18.143  82.061  57.604  1.00 20.63 ? 137 THR D C   1 
ATOM   4334  O  O   . THR D  1 137 ? 18.517  83.199  57.862  1.00 22.19 ? 137 THR D O   1 
ATOM   4335  C  CB  . THR D  1 137 ? 18.769  80.798  59.610  1.00 22.03 ? 137 THR D CB  1 
ATOM   4336  O  OG1 . THR D  1 137 ? 19.773  80.131  58.834  1.00 27.18 ? 137 THR D OG1 1 
ATOM   4337  C  CG2 . THR D  1 137 ? 18.303  79.865  60.708  1.00 28.21 ? 137 THR D CG2 1 
ATOM   4338  N  N   . GLY D  1 138 ? 18.212  81.553  56.384  1.00 15.29 ? 138 GLY D N   1 
ATOM   4339  C  CA  . GLY D  1 138 ? 18.779  82.322  55.295  1.00 16.77 ? 138 GLY D CA  1 
ATOM   4340  C  C   . GLY D  1 138 ? 20.291  82.497  55.391  1.00 21.85 ? 138 GLY D C   1 
ATOM   4341  O  O   . GLY D  1 138 ? 20.838  83.446  54.820  1.00 16.81 ? 138 GLY D O   1 
ATOM   4342  N  N   . ASN D  1 139 ? 20.946  81.579  56.109  1.00 21.72 ? 139 ASN D N   1 
ATOM   4343  C  CA  . ASN D  1 139 ? 22.401  81.572  56.333  1.00 20.88 ? 139 ASN D CA  1 
ATOM   4344  C  C   . ASN D  1 139 ? 22.971  82.894  56.811  1.00 17.26 ? 139 ASN D C   1 
ATOM   4345  O  O   . ASN D  1 139 ? 24.011  83.312  56.358  1.00 18.06 ? 139 ASN D O   1 
ATOM   4346  C  CB  . ASN D  1 139 ? 23.183  81.099  55.094  1.00 18.63 ? 139 ASN D CB  1 
ATOM   4347  C  CG  . ASN D  1 139 ? 22.799  79.685  54.646  1.00 24.89 ? 139 ASN D CG  1 
ATOM   4348  O  OD1 . ASN D  1 139 ? 23.122  78.703  55.309  1.00 26.54 ? 139 ASN D OD1 1 
ATOM   4349  N  ND2 . ASN D  1 139 ? 22.130  79.584  53.508  1.00 20.21 ? 139 ASN D ND2 1 
ATOM   4350  N  N   . ALA D  1 140 ? 22.312  83.553  57.743  1.00 17.35 ? 140 ALA D N   1 
ATOM   4351  C  CA  . ALA D  1 140 ? 22.830  84.833  58.188  1.00 19.22 ? 140 ALA D CA  1 
ATOM   4352  C  C   . ALA D  1 140 ? 23.853  84.663  59.328  1.00 24.64 ? 140 ALA D C   1 
ATOM   4353  O  O   . ALA D  1 140 ? 24.468  85.632  59.801  1.00 21.45 ? 140 ALA D O   1 
ATOM   4354  C  CB  . ALA D  1 140 ? 21.684  85.753  58.586  1.00 17.39 ? 140 ALA D CB  1 
ATOM   4355  N  N   . GLY D  1 141 ? 24.041  83.422  59.760  1.00 22.19 ? 141 GLY D N   1 
ATOM   4356  C  CA  . GLY D  1 141 ? 25.068  83.130  60.738  1.00 24.18 ? 141 GLY D CA  1 
ATOM   4357  C  C   . GLY D  1 141 ? 24.730  83.683  62.106  1.00 28.23 ? 141 GLY D C   1 
ATOM   4358  O  O   . GLY D  1 141 ? 23.576  83.990  62.409  1.00 25.35 ? 141 GLY D O   1 
ATOM   4359  N  N   . SER D  1 142 ? 25.762  83.830  62.926  1.00 29.19 ? 142 SER D N   1 
ATOM   4360  C  CA  . SER D  1 142 ? 25.617  84.170  64.336  1.00 28.54 ? 142 SER D CA  1 
ATOM   4361  C  C   . SER D  1 142 ? 24.892  85.483  64.613  1.00 22.94 ? 142 SER D C   1 
ATOM   4362  O  O   . SER D  1 142 ? 24.841  86.380  63.774  1.00 26.60 ? 142 SER D O   1 
ATOM   4363  C  CB  . SER D  1 142 ? 27.004  84.233  64.980  1.00 29.18 ? 142 SER D CB  1 
ATOM   4364  O  OG  . SER D  1 142 ? 27.557  85.517  64.777  1.00 28.92 ? 142 SER D OG  1 
ATOM   4365  N  N   . ARG D  1 143 ? 24.358  85.590  65.822  1.00 21.68 ? 143 ARG D N   1 
ATOM   4366  C  CA  . ARG D  1 143 ? 23.669  86.790  66.292  1.00 26.23 ? 143 ARG D CA  1 
ATOM   4367  C  C   . ARG D  1 143 ? 24.661  87.773  66.921  1.00 29.12 ? 143 ARG D C   1 
ATOM   4368  O  O   . ARG D  1 143 ? 25.266  87.474  67.952  1.00 29.65 ? 143 ARG D O   1 
ATOM   4369  C  CB  . ARG D  1 143 ? 22.577  86.379  67.291  1.00 23.83 ? 143 ARG D CB  1 
ATOM   4370  C  CG  . ARG D  1 143 ? 21.846  85.112  66.818  1.00 25.05 ? 143 ARG D CG  1 
ATOM   4371  C  CD  . ARG D  1 143 ? 20.661  84.689  67.672  1.00 27.30 ? 143 ARG D CD  1 
ATOM   4372  N  NE  . ARG D  1 143 ? 20.062  83.496  67.082  1.00 28.12 ? 143 ARG D NE  1 
ATOM   4373  C  CZ  . ARG D  1 143 ? 19.034  82.817  67.587  1.00 33.09 ? 143 ARG D CZ  1 
ATOM   4374  N  NH1 . ARG D  1 143 ? 18.457  83.191  68.727  1.00 32.31 ? 143 ARG D NH1 1 
ATOM   4375  N  NH2 . ARG D  1 143 ? 18.578  81.752  66.940  1.00 32.83 ? 143 ARG D NH2 1 
ATOM   4376  N  N   . LEU D  1 144 ? 24.827  88.938  66.295  1.00 25.95 ? 144 LEU D N   1 
ATOM   4377  C  CA  . LEU D  1 144 ? 25.826  89.923  66.725  1.00 27.38 ? 144 LEU D CA  1 
ATOM   4378  C  C   . LEU D  1 144 ? 25.307  90.859  67.802  1.00 29.32 ? 144 LEU D C   1 
ATOM   4379  O  O   . LEU D  1 144 ? 26.053  91.288  68.688  1.00 31.52 ? 144 LEU D O   1 
ATOM   4380  C  CB  . LEU D  1 144 ? 26.294  90.771  65.540  1.00 23.34 ? 144 LEU D CB  1 
ATOM   4381  C  CG  . LEU D  1 144 ? 27.047  90.057  64.422  1.00 30.70 ? 144 LEU D CG  1 
ATOM   4382  C  CD1 . LEU D  1 144 ? 27.368  91.046  63.308  1.00 29.40 ? 144 LEU D CD1 1 
ATOM   4383  C  CD2 . LEU D  1 144 ? 28.322  89.387  64.948  1.00 31.34 ? 144 LEU D CD2 1 
ATOM   4384  N  N   . ALA D  1 145 ? 24.030  91.204  67.708  1.00 25.14 ? 145 ALA D N   1 
ATOM   4385  C  CA  . ALA D  1 145 ? 23.424  92.110  68.669  1.00 24.59 ? 145 ALA D CA  1 
ATOM   4386  C  C   . ALA D  1 145 ? 21.942  91.842  68.683  1.00 25.72 ? 145 ALA D C   1 
ATOM   4387  O  O   . ALA D  1 145 ? 21.381  91.416  67.681  1.00 22.48 ? 145 ALA D O   1 
ATOM   4388  C  CB  . ALA D  1 145 ? 23.692  93.546  68.285  1.00 23.69 ? 145 ALA D CB  1 
ATOM   4389  N  N   . CYS D  1 146 ? 21.311  92.079  69.823  1.00 25.13 ? 146 CYS D N   1 
ATOM   4390  C  CA  . CYS D  1 146 ? 19.882  91.885  69.932  1.00 25.41 ? 146 CYS D CA  1 
ATOM   4391  C  C   . CYS D  1 146 ? 19.273  92.738  71.030  1.00 28.29 ? 146 CYS D C   1 
ATOM   4392  O  O   . CYS D  1 146 ? 19.976  93.463  71.744  1.00 26.40 ? 146 CYS D O   1 
ATOM   4393  C  CB  . CYS D  1 146 ? 19.556  90.410  70.136  1.00 28.23 ? 146 CYS D CB  1 
ATOM   4394  S  SG  . CYS D  1 146 ? 20.098  89.709  71.694  1.00 37.34 ? 146 CYS D SG  1 
ATOM   4395  N  N   . GLY D  1 147 ? 17.955  92.665  71.144  1.00 25.10 ? 147 GLY D N   1 
ATOM   4396  C  CA  . GLY D  1 147 ? 17.229  93.460  72.117  1.00 24.10 ? 147 GLY D CA  1 
ATOM   4397  C  C   . GLY D  1 147 ? 15.731  93.216  72.006  1.00 29.51 ? 147 GLY D C   1 
ATOM   4398  O  O   . GLY D  1 147 ? 15.228  92.824  70.947  1.00 27.28 ? 147 GLY D O   1 
ATOM   4399  N  N   . VAL D  1 148 ? 15.021  93.435  73.107  1.00 27.64 ? 148 VAL D N   1 
ATOM   4400  C  CA  . VAL D  1 148 ? 13.596  93.171  73.162  1.00 25.14 ? 148 VAL D CA  1 
ATOM   4401  C  C   . VAL D  1 148 ? 12.853  94.383  72.639  1.00 24.88 ? 148 VAL D C   1 
ATOM   4402  O  O   . VAL D  1 148 ? 13.125  95.501  73.048  1.00 25.57 ? 148 VAL D O   1 
ATOM   4403  C  CB  . VAL D  1 148 ? 13.137  92.861  74.605  1.00 27.31 ? 148 VAL D CB  1 
ATOM   4404  C  CG1 . VAL D  1 148 ? 11.630  92.681  74.659  1.00 24.46 ? 148 VAL D CG1 1 
ATOM   4405  C  CG2 . VAL D  1 148 ? 13.846  91.613  75.132  1.00 27.39 ? 148 VAL D CG2 1 
ATOM   4406  N  N   . ILE D  1 149 ? 11.920  94.167  71.720  1.00 23.95 ? 149 ILE D N   1 
ATOM   4407  C  CA  . ILE D  1 149 ? 11.158  95.271  71.172  1.00 20.06 ? 149 ILE D CA  1 
ATOM   4408  C  C   . ILE D  1 149 ? 10.136  95.765  72.179  1.00 24.55 ? 149 ILE D C   1 
ATOM   4409  O  O   . ILE D  1 149 ? 9.328   94.989  72.679  1.00 21.68 ? 149 ILE D O   1 
ATOM   4410  C  CB  . ILE D  1 149 ? 10.456  94.856  69.882  1.00 21.49 ? 149 ILE D CB  1 
ATOM   4411  C  CG1 . ILE D  1 149 ? 11.499  94.381  68.862  1.00 25.49 ? 149 ILE D CG1 1 
ATOM   4412  C  CG2 . ILE D  1 149 ? 9.667   96.027  69.324  1.00 16.23 ? 149 ILE D CG2 1 
ATOM   4413  C  CD1 . ILE D  1 149 ? 10.900  93.731  67.633  1.00 20.11 ? 149 ILE D CD1 1 
ATOM   4414  N  N   . GLY D  1 150 ? 10.167  97.060  72.473  1.00 24.16 ? 150 GLY D N   1 
ATOM   4415  C  CA  . GLY D  1 150 ? 9.322   97.603  73.518  1.00 27.47 ? 150 GLY D CA  1 
ATOM   4416  C  C   . GLY D  1 150 ? 8.485   98.782  73.082  1.00 28.20 ? 150 GLY D C   1 
ATOM   4417  O  O   . GLY D  1 150 ? 8.803   99.452  72.106  1.00 30.41 ? 150 GLY D O   1 
ATOM   4418  N  N   . ILE D  1 151 ? 7.418   99.039  73.824  1.00 29.08 ? 151 ILE D N   1 
ATOM   4419  C  CA  . ILE D  1 151 ? 6.489   100.126 73.518  1.00 28.73 ? 151 ILE D CA  1 
ATOM   4420  C  C   . ILE D  1 151 ? 7.079   101.506 73.803  1.00 33.89 ? 151 ILE D C   1 
ATOM   4421  O  O   . ILE D  1 151 ? 7.742   101.708 74.820  1.00 34.06 ? 151 ILE D O   1 
ATOM   4422  C  CB  . ILE D  1 151 ? 5.206   99.958  74.323  1.00 24.61 ? 151 ILE D CB  1 
ATOM   4423  C  CG1 . ILE D  1 151 ? 4.561   98.609  73.998  1.00 29.49 ? 151 ILE D CG1 1 
ATOM   4424  C  CG2 . ILE D  1 151 ? 4.255   101.106 74.064  1.00 32.06 ? 151 ILE D CG2 1 
ATOM   4425  C  CD1 . ILE D  1 151 ? 3.066   98.530  74.339  1.00 36.84 ? 151 ILE D CD1 1 
ATOM   4426  N  N   . ALA D  1 152 ? 6.835   102.459 72.910  1.00 30.15 ? 152 ALA D N   1 
ATOM   4427  C  CA  . ALA D  1 152 ? 7.418   103.784 73.052  1.00 33.11 ? 152 ALA D CA  1 
ATOM   4428  C  C   . ALA D  1 152 ? 6.358   104.881 72.995  1.00 38.46 ? 152 ALA D C   1 
ATOM   4429  O  O   . ALA D  1 152 ? 5.203   104.627 72.656  1.00 36.93 ? 152 ALA D O   1 
ATOM   4430  C  CB  . ALA D  1 152 ? 8.478   103.996 71.978  1.00 32.67 ? 152 ALA D CB  1 
ATOM   4431  N  N   . GLN D  1 153 ? 6.744   106.104 73.333  1.00 42.00 ? 153 GLN D N   1 
ATOM   4432  C  CA  . GLN D  1 153 ? 5.821   107.226 73.224  1.00 45.27 ? 153 GLN D CA  1 
ATOM   4433  C  C   . GLN D  1 153 ? 6.121   108.083 72.004  1.00 50.46 ? 153 GLN D C   1 
ATOM   4434  O  O   . GLN D  1 153 ? 7.279   108.230 71.600  1.00 49.54 ? 153 GLN D O   1 
ATOM   4435  C  CB  . GLN D  1 153 ? 5.872   108.094 74.473  1.00 48.25 ? 153 GLN D CB  1 
ATOM   4436  C  CG  . GLN D  1 153 ? 7.262   108.583 74.850  1.00 49.47 ? 153 GLN D CG  1 
ATOM   4437  C  CD  . GLN D  1 153 ? 7.216   109.680 75.903  1.00 54.27 ? 153 GLN D CD  1 
ATOM   4438  O  OE1 . GLN D  1 153 ? 6.145   110.213 76.217  1.00 50.98 ? 153 GLN D OE1 1 
ATOM   4439  N  NE2 . GLN D  1 153 ? 8.377   110.025 76.452  1.00 51.17 ? 153 GLN D NE2 1 
ATOM   4440  O  OXT . GLN D  1 153 ? 5.208   108.661 71.408  1.00 56.24 ? 153 GLN D OXT 1 
ATOM   4441  N  N   . THR E  1 2   ? 15.081  58.256  18.810  1.00 51.23 ? 2   THR E N   1 
ATOM   4442  C  CA  . THR E  1 2   ? 15.912  59.072  19.684  1.00 46.07 ? 2   THR E CA  1 
ATOM   4443  C  C   . THR E  1 2   ? 17.293  58.457  19.841  1.00 43.02 ? 2   THR E C   1 
ATOM   4444  O  O   . THR E  1 2   ? 17.563  57.379  19.331  1.00 43.78 ? 2   THR E O   1 
ATOM   4445  C  CB  . THR E  1 2   ? 15.282  59.213  21.078  1.00 41.33 ? 2   THR E CB  1 
ATOM   4446  O  OG1 . THR E  1 2   ? 13.919  58.764  21.045  1.00 41.51 ? 2   THR E OG1 1 
ATOM   4447  C  CG2 . THR E  1 2   ? 15.350  60.669  21.551  1.00 39.63 ? 2   THR E CG2 1 
ATOM   4448  N  N   . LYS E  1 3   ? 18.168  59.154  20.551  1.00 46.13 ? 3   LYS E N   1 
ATOM   4449  C  CA  . LYS E  1 3   ? 19.478  58.621  20.876  1.00 41.88 ? 3   LYS E CA  1 
ATOM   4450  C  C   . LYS E  1 3   ? 19.718  58.629  22.387  1.00 46.16 ? 3   LYS E C   1 
ATOM   4451  O  O   . LYS E  1 3   ? 19.267  59.534  23.103  1.00 41.36 ? 3   LYS E O   1 
ATOM   4452  C  CB  . LYS E  1 3   ? 20.578  59.405  20.154  1.00 43.57 ? 3   LYS E CB  1 
ATOM   4453  C  CG  . LYS E  1 3   ? 20.371  59.502  18.642  1.00 50.39 ? 3   LYS E CG  1 
ATOM   4454  C  CD  . LYS E  1 3   ? 21.682  59.724  17.890  1.00 46.32 ? 3   LYS E CD  1 
ATOM   4455  C  CE  . LYS E  1 3   ? 21.437  60.087  16.417  1.00 52.21 ? 3   LYS E CE  1 
ATOM   4456  N  NZ  . LYS E  1 3   ? 20.838  61.451  16.239  1.00 50.24 ? 3   LYS E NZ  1 
ATOM   4457  N  N   . ALA E  1 4   ? 20.425  57.606  22.864  1.00 46.17 ? 4   ALA E N   1 
ATOM   4458  C  CA  . ALA E  1 4   ? 20.853  57.534  24.259  1.00 42.92 ? 4   ALA E CA  1 
ATOM   4459  C  C   . ALA E  1 4   ? 22.269  56.976  24.358  1.00 39.83 ? 4   ALA E C   1 
ATOM   4460  O  O   . ALA E  1 4   ? 22.738  56.302  23.448  1.00 43.57 ? 4   ALA E O   1 
ATOM   4461  C  CB  . ALA E  1 4   ? 19.879  56.693  25.074  1.00 39.47 ? 4   ALA E CB  1 
ATOM   4462  N  N   . VAL E  1 5   ? 22.952  57.265  25.459  1.00 41.67 ? 5   VAL E N   1 
ATOM   4463  C  CA  . VAL E  1 5   ? 24.315  56.793  25.645  1.00 42.01 ? 5   VAL E CA  1 
ATOM   4464  C  C   . VAL E  1 5   ? 24.546  56.250  27.067  1.00 45.90 ? 5   VAL E C   1 
ATOM   4465  O  O   . VAL E  1 5   ? 23.770  56.525  27.990  1.00 41.81 ? 5   VAL E O   1 
ATOM   4466  C  CB  . VAL E  1 5   ? 25.339  57.908  25.322  1.00 43.53 ? 5   VAL E CB  1 
ATOM   4467  C  CG1 . VAL E  1 5   ? 25.516  58.847  26.512  1.00 44.52 ? 5   VAL E CG1 1 
ATOM   4468  C  CG2 . VAL E  1 5   ? 26.680  57.314  24.918  1.00 41.95 ? 5   VAL E CG2 1 
ATOM   4469  N  N   . CYS E  1 6   ? 25.619  55.482  27.233  1.00 44.75 ? 6   CYS E N   1 
ATOM   4470  C  CA  . CYS E  1 6   ? 25.947  54.880  28.511  1.00 35.93 ? 6   CYS E CA  1 
ATOM   4471  C  C   . CYS E  1 6   ? 27.438  54.685  28.670  1.00 35.06 ? 6   CYS E C   1 
ATOM   4472  O  O   . CYS E  1 6   ? 28.053  53.947  27.913  1.00 42.37 ? 6   CYS E O   1 
ATOM   4473  C  CB  . CYS E  1 6   ? 25.274  53.527  28.629  1.00 41.45 ? 6   CYS E CB  1 
ATOM   4474  S  SG  . CYS E  1 6   ? 25.388  52.829  30.281  1.00 38.64 ? 6   CYS E SG  1 
ATOM   4475  N  N   . VAL E  1 7   ? 28.017  55.356  29.653  1.00 36.18 ? 7   VAL E N   1 
ATOM   4476  C  CA  . VAL E  1 7   ? 29.409  55.137  30.026  1.00 38.56 ? 7   VAL E CA  1 
ATOM   4477  C  C   . VAL E  1 7   ? 29.485  54.080  31.142  1.00 48.80 ? 7   VAL E C   1 
ATOM   4478  O  O   . VAL E  1 7   ? 28.894  54.250  32.215  1.00 46.52 ? 7   VAL E O   1 
ATOM   4479  C  CB  . VAL E  1 7   ? 30.067  56.443  30.509  1.00 40.11 ? 7   VAL E CB  1 
ATOM   4480  C  CG1 . VAL E  1 7   ? 31.569  56.264  30.679  1.00 41.11 ? 7   VAL E CG1 1 
ATOM   4481  C  CG2 . VAL E  1 7   ? 29.769  57.577  29.535  1.00 48.41 ? 7   VAL E CG2 1 
ATOM   4482  N  N   . LEU E  1 8   ? 30.206  52.990  30.878  1.00 50.02 ? 8   LEU E N   1 
ATOM   4483  C  CA  . LEU E  1 8   ? 30.368  51.906  31.844  1.00 46.71 ? 8   LEU E CA  1 
ATOM   4484  C  C   . LEU E  1 8   ? 31.700  52.007  32.560  1.00 52.12 ? 8   LEU E C   1 
ATOM   4485  O  O   . LEU E  1 8   ? 32.750  51.821  31.953  1.00 54.87 ? 8   LEU E O   1 
ATOM   4486  C  CB  . LEU E  1 8   ? 30.319  50.562  31.127  1.00 46.26 ? 8   LEU E CB  1 
ATOM   4487  C  CG  . LEU E  1 8   ? 29.069  50.290  30.301  1.00 40.95 ? 8   LEU E CG  1 
ATOM   4488  C  CD1 . LEU E  1 8   ? 29.434  49.522  29.060  1.00 40.74 ? 8   LEU E CD1 1 
ATOM   4489  C  CD2 . LEU E  1 8   ? 28.067  49.510  31.133  1.00 45.21 ? 8   LEU E CD2 1 
ATOM   4490  N  N   . LYS E  1 9   ? 31.669  52.298  33.851  1.00 53.94 ? 9   LYS E N   1 
ATOM   4491  C  CA  . LYS E  1 9   ? 32.886  52.210  34.643  1.00 56.53 ? 9   LYS E CA  1 
ATOM   4492  C  C   . LYS E  1 9   ? 32.719  51.141  35.708  1.00 56.96 ? 9   LYS E C   1 
ATOM   4493  O  O   . LYS E  1 9   ? 31.605  50.694  35.978  1.00 50.20 ? 9   LYS E O   1 
ATOM   4494  C  CB  . LYS E  1 9   ? 33.264  53.562  35.259  1.00 58.18 ? 9   LYS E CB  1 
ATOM   4495  C  CG  . LYS E  1 9   ? 33.812  54.560  34.236  1.00 66.32 ? 9   LYS E CG  1 
ATOM   4496  C  CD  . LYS E  1 9   ? 34.537  55.734  34.901  1.00 73.48 ? 9   LYS E CD  1 
ATOM   4497  C  CE  . LYS E  1 9   ? 35.128  56.688  33.864  1.00 67.61 ? 9   LYS E CE  1 
ATOM   4498  N  NZ  . LYS E  1 9   ? 34.087  57.233  32.930  1.00 61.06 ? 9   LYS E NZ  1 
ATOM   4499  N  N   . GLY E  1 10  ? 33.839  50.726  36.290  1.00 59.83 ? 10  GLY E N   1 
ATOM   4500  C  CA  . GLY E  1 10  ? 33.842  49.712  37.325  1.00 62.37 ? 10  GLY E CA  1 
ATOM   4501  C  C   . GLY E  1 10  ? 35.201  49.654  37.993  1.00 69.29 ? 10  GLY E C   1 
ATOM   4502  O  O   . GLY E  1 10  ? 36.172  50.198  37.463  1.00 72.46 ? 10  GLY E O   1 
ATOM   4503  N  N   . ASP E  1 11  ? 35.271  48.996  39.148  1.00 70.41 ? 11  ASP E N   1 
ATOM   4504  C  CA  . ASP E  1 11  ? 36.514  48.899  39.911  1.00 72.48 ? 11  ASP E CA  1 
ATOM   4505  C  C   . ASP E  1 11  ? 37.633  48.278  39.091  1.00 71.69 ? 11  ASP E C   1 
ATOM   4506  O  O   . ASP E  1 11  ? 38.807  48.601  39.281  1.00 70.41 ? 11  ASP E O   1 
ATOM   4507  C  CB  . ASP E  1 11  ? 36.303  48.077  41.179  1.00 73.66 ? 11  ASP E CB  1 
ATOM   4508  C  CG  . ASP E  1 11  ? 35.279  48.693  42.100  1.00 74.79 ? 11  ASP E CG  1 
ATOM   4509  O  OD1 . ASP E  1 11  ? 35.076  49.923  42.007  1.00 73.25 ? 11  ASP E OD1 1 
ATOM   4510  O  OD2 . ASP E  1 11  ? 34.683  47.947  42.912  1.00 70.01 ? 11  ASP E OD2 1 
ATOM   4511  N  N   . GLY E  1 12  ? 37.256  47.390  38.175  1.00 72.85 ? 12  GLY E N   1 
ATOM   4512  C  CA  . GLY E  1 12  ? 38.220  46.674  37.366  1.00 70.53 ? 12  GLY E CA  1 
ATOM   4513  C  C   . GLY E  1 12  ? 38.584  47.410  36.098  1.00 65.96 ? 12  GLY E C   1 
ATOM   4514  O  O   . GLY E  1 12  ? 38.298  48.596  35.961  1.00 65.59 ? 12  GLY E O   1 
ATOM   4515  N  N   . PRO E  1 13  ? 39.226  46.702  35.162  1.00 68.07 ? 13  PRO E N   1 
ATOM   4516  C  CA  . PRO E  1 13  ? 39.647  47.239  33.869  1.00 67.41 ? 13  PRO E CA  1 
ATOM   4517  C  C   . PRO E  1 13  ? 38.474  47.271  32.913  1.00 64.17 ? 13  PRO E C   1 
ATOM   4518  O  O   . PRO E  1 13  ? 38.614  47.745  31.782  1.00 64.51 ? 13  PRO E O   1 
ATOM   4519  C  CB  . PRO E  1 13  ? 40.666  46.204  33.371  1.00 66.50 ? 13  PRO E CB  1 
ATOM   4520  C  CG  . PRO E  1 13  ? 40.886  45.252  34.521  1.00 68.68 ? 13  PRO E CG  1 
ATOM   4521  C  CD  . PRO E  1 13  ? 39.639  45.302  35.323  1.00 66.55 ? 13  PRO E CD  1 
ATOM   4522  N  N   . VAL E  1 14  ? 37.334  46.751  33.357  1.00 61.75 ? 14  VAL E N   1 
ATOM   4523  C  CA  . VAL E  1 14  ? 36.146  46.724  32.519  1.00 58.08 ? 14  VAL E CA  1 
ATOM   4524  C  C   . VAL E  1 14  ? 35.571  48.127  32.368  1.00 62.34 ? 14  VAL E C   1 
ATOM   4525  O  O   . VAL E  1 14  ? 35.152  48.749  33.347  1.00 59.28 ? 14  VAL E O   1 
ATOM   4526  C  CB  . VAL E  1 14  ? 35.067  45.791  33.082  1.00 55.80 ? 14  VAL E CB  1 
ATOM   4527  C  CG1 . VAL E  1 14  ? 33.903  45.687  32.104  1.00 51.50 ? 14  VAL E CG1 1 
ATOM   4528  C  CG2 . VAL E  1 14  ? 35.654  44.424  33.374  1.00 52.29 ? 14  VAL E CG2 1 
ATOM   4529  N  N   . GLN E  1 15  ? 35.573  48.622  31.134  1.00 62.68 ? 15  GLN E N   1 
ATOM   4530  C  CA  . GLN E  1 15  ? 35.029  49.939  30.828  1.00 60.66 ? 15  GLN E CA  1 
ATOM   4531  C  C   . GLN E  1 15  ? 34.626  49.999  29.362  1.00 55.99 ? 15  GLN E C   1 
ATOM   4532  O  O   . GLN E  1 15  ? 35.188  49.281  28.537  1.00 54.81 ? 15  GLN E O   1 
ATOM   4533  C  CB  . GLN E  1 15  ? 36.034  51.044  31.162  1.00 59.85 ? 15  GLN E CB  1 
ATOM   4534  C  CG  . GLN E  1 15  ? 37.158  51.216  30.157  1.00 59.75 ? 15  GLN E CG  1 
ATOM   4535  C  CD  . GLN E  1 15  ? 38.189  52.221  30.634  1.00 68.27 ? 15  GLN E CD  1 
ATOM   4536  O  OE1 . GLN E  1 15  ? 38.354  52.434  31.839  1.00 69.38 ? 15  GLN E OE1 1 
ATOM   4537  N  NE2 . GLN E  1 15  ? 38.883  52.853  29.694  1.00 70.14 ? 15  GLN E NE2 1 
ATOM   4538  N  N   . GLY E  1 16  ? 33.642  50.842  29.052  1.00 54.41 ? 16  GLY E N   1 
ATOM   4539  C  CA  . GLY E  1 16  ? 33.108  50.939  27.704  1.00 50.45 ? 16  GLY E CA  1 
ATOM   4540  C  C   . GLY E  1 16  ? 32.116  52.070  27.492  1.00 48.65 ? 16  GLY E C   1 
ATOM   4541  O  O   . GLY E  1 16  ? 31.691  52.733  28.437  1.00 49.57 ? 16  GLY E O   1 
ATOM   4542  N  N   . ILE E  1 17  ? 31.758  52.289  26.232  1.00 49.21 ? 17  ILE E N   1 
ATOM   4543  C  CA  . ILE E  1 17  ? 30.781  53.294  25.837  1.00 45.12 ? 17  ILE E CA  1 
ATOM   4544  C  C   . ILE E  1 17  ? 29.769  52.620  24.924  1.00 44.76 ? 17  ILE E C   1 
ATOM   4545  O  O   . ILE E  1 17  ? 30.123  52.138  23.852  1.00 47.24 ? 17  ILE E O   1 
ATOM   4546  C  CB  . ILE E  1 17  ? 31.442  54.448  25.049  1.00 43.25 ? 17  ILE E CB  1 
ATOM   4547  C  CG1 . ILE E  1 17  ? 32.354  55.277  25.950  1.00 47.09 ? 17  ILE E CG1 1 
ATOM   4548  C  CG2 . ILE E  1 17  ? 30.394  55.344  24.415  1.00 36.84 ? 17  ILE E CG2 1 
ATOM   4549  C  CD1 . ILE E  1 17  ? 33.147  56.327  25.195  1.00 44.84 ? 17  ILE E CD1 1 
ATOM   4550  N  N   . ILE E  1 18  ? 28.513  52.582  25.348  1.00 43.50 ? 18  ILE E N   1 
ATOM   4551  C  CA  . ILE E  1 18  ? 27.466  51.919  24.576  1.00 41.69 ? 18  ILE E CA  1 
ATOM   4552  C  C   . ILE E  1 18  ? 26.419  52.903  24.084  1.00 44.84 ? 18  ILE E C   1 
ATOM   4553  O  O   . ILE E  1 18  ? 25.771  53.584  24.881  1.00 45.00 ? 18  ILE E O   1 
ATOM   4554  C  CB  . ILE E  1 18  ? 26.757  50.841  25.409  1.00 41.90 ? 18  ILE E CB  1 
ATOM   4555  C  CG1 . ILE E  1 18  ? 27.707  49.668  25.677  1.00 49.85 ? 18  ILE E CG1 1 
ATOM   4556  C  CG2 . ILE E  1 18  ? 25.505  50.368  24.712  1.00 39.62 ? 18  ILE E CG2 1 
ATOM   4557  C  CD1 . ILE E  1 18  ? 28.227  49.005  24.418  1.00 46.12 ? 18  ILE E CD1 1 
ATOM   4558  N  N   . ASN E  1 19  ? 26.249  52.970  22.768  1.00 43.41 ? 19  ASN E N   1 
ATOM   4559  C  CA  . ASN E  1 19  ? 25.281  53.883  22.174  1.00 41.81 ? 19  ASN E CA  1 
ATOM   4560  C  C   . ASN E  1 19  ? 23.964  53.178  21.911  1.00 39.30 ? 19  ASN E C   1 
ATOM   4561  O  O   . ASN E  1 19  ? 23.938  51.972  21.702  1.00 38.39 ? 19  ASN E O   1 
ATOM   4562  C  CB  . ASN E  1 19  ? 25.835  54.524  20.895  1.00 35.45 ? 19  ASN E CB  1 
ATOM   4563  C  CG  . ASN E  1 19  ? 27.166  55.236  21.129  1.00 42.60 ? 19  ASN E CG  1 
ATOM   4564  O  OD1 . ASN E  1 19  ? 27.204  56.375  21.596  1.00 43.08 ? 19  ASN E OD1 1 
ATOM   4565  N  ND2 . ASN E  1 19  ? 28.265  54.560  20.806  1.00 44.20 ? 19  ASN E ND2 1 
ATOM   4566  N  N   . PHE E  1 20  ? 22.878  53.942  21.970  1.00 36.65 ? 20  PHE E N   1 
ATOM   4567  C  CA  . PHE E  1 20  ? 21.536  53.463  21.672  1.00 41.21 ? 20  PHE E CA  1 
ATOM   4568  C  C   . PHE E  1 20  ? 20.952  54.404  20.636  1.00 41.93 ? 20  PHE E C   1 
ATOM   4569  O  O   . PHE E  1 20  ? 21.264  55.599  20.631  1.00 43.15 ? 20  PHE E O   1 
ATOM   4570  C  CB  . PHE E  1 20  ? 20.632  53.519  22.913  1.00 44.24 ? 20  PHE E CB  1 
ATOM   4571  C  CG  . PHE E  1 20  ? 20.997  52.541  23.996  1.00 40.25 ? 20  PHE E CG  1 
ATOM   4572  C  CD1 . PHE E  1 20  ? 22.039  52.814  24.878  1.00 40.14 ? 20  PHE E CD1 1 
ATOM   4573  C  CD2 . PHE E  1 20  ? 20.277  51.367  24.153  1.00 36.33 ? 20  PHE E CD2 1 
ATOM   4574  C  CE1 . PHE E  1 20  ? 22.370  51.920  25.885  1.00 42.44 ? 20  PHE E CE1 1 
ATOM   4575  C  CE2 . PHE E  1 20  ? 20.601  50.468  25.159  1.00 41.18 ? 20  PHE E CE2 1 
ATOM   4576  C  CZ  . PHE E  1 20  ? 21.645  50.743  26.028  1.00 39.27 ? 20  PHE E CZ  1 
ATOM   4577  N  N   . GLU E  1 21  ? 20.082  53.876  19.786  1.00 41.34 ? 21  GLU E N   1 
ATOM   4578  C  CA  . GLU E  1 21  ? 19.484  54.663  18.720  1.00 44.22 ? 21  GLU E CA  1 
ATOM   4579  C  C   . GLU E  1 21  ? 18.198  54.019  18.263  1.00 41.75 ? 21  GLU E C   1 
ATOM   4580  O  O   . GLU E  1 21  ? 18.192  52.875  17.836  1.00 45.92 ? 21  GLU E O   1 
ATOM   4581  C  CB  . GLU E  1 21  ? 20.437  54.778  17.531  1.00 40.64 ? 21  GLU E CB  1 
ATOM   4582  C  CG  . GLU E  1 21  ? 20.723  56.206  17.118  1.00 45.47 ? 21  GLU E CG  1 
ATOM   4583  C  CD  . GLU E  1 21  ? 21.509  56.299  15.823  1.00 49.50 ? 21  GLU E CD  1 
ATOM   4584  O  OE1 . GLU E  1 21  ? 21.118  55.621  14.847  1.00 49.44 ? 21  GLU E OE1 1 
ATOM   4585  O  OE2 . GLU E  1 21  ? 22.514  57.049  15.784  1.00 47.57 ? 21  GLU E OE2 1 
ATOM   4586  N  N   . GLN E  1 22  ? 17.108  54.758  18.357  1.00 37.72 ? 22  GLN E N   1 
ATOM   4587  C  CA  . GLN E  1 22  ? 15.836  54.278  17.870  1.00 44.62 ? 22  GLN E CA  1 
ATOM   4588  C  C   . GLN E  1 22  ? 15.314  55.354  16.927  1.00 49.24 ? 22  GLN E C   1 
ATOM   4589  O  O   . GLN E  1 22  ? 14.955  56.446  17.371  1.00 48.86 ? 22  GLN E O   1 
ATOM   4590  C  CB  . GLN E  1 22  ? 14.882  54.067  19.050  1.00 46.73 ? 22  GLN E CB  1 
ATOM   4591  C  CG  . GLN E  1 22  ? 13.699  53.136  18.792  1.00 42.55 ? 22  GLN E CG  1 
ATOM   4592  C  CD  . GLN E  1 22  ? 12.740  53.078  19.985  1.00 44.10 ? 22  GLN E CD  1 
ATOM   4593  O  OE1 . GLN E  1 22  ? 13.029  53.631  21.046  1.00 47.60 ? 22  GLN E OE1 1 
ATOM   4594  N  NE2 . GLN E  1 22  ? 11.593  52.422  19.810  1.00 43.56 ? 22  GLN E NE2 1 
ATOM   4595  N  N   . LYS E  1 23  ? 15.306  55.067  15.626  1.00 51.86 ? 23  LYS E N   1 
ATOM   4596  C  CA  . LYS E  1 23  ? 14.803  56.029  14.639  1.00 52.86 ? 23  LYS E CA  1 
ATOM   4597  C  C   . LYS E  1 23  ? 13.318  56.321  14.865  1.00 50.08 ? 23  LYS E C   1 
ATOM   4598  O  O   . LYS E  1 23  ? 12.878  57.468  14.785  1.00 50.79 ? 23  LYS E O   1 
ATOM   4599  C  CB  . LYS E  1 23  ? 15.028  55.536  13.202  1.00 50.62 ? 23  LYS E CB  1 
ATOM   4600  C  CG  . LYS E  1 23  ? 16.483  55.530  12.732  1.00 52.27 ? 23  LYS E CG  1 
ATOM   4601  C  CD  . LYS E  1 23  ? 16.578  55.125  11.251  1.00 62.52 ? 23  LYS E CD  1 
ATOM   4602  C  CE  . LYS E  1 23  ? 18.000  54.736  10.833  1.00 60.62 ? 23  LYS E CE  1 
ATOM   4603  N  NZ  . LYS E  1 23  ? 18.322  53.291  11.088  1.00 56.45 ? 23  LYS E NZ  1 
ATOM   4604  N  N   . GLU E  1 24  ? 12.549  55.281  15.160  1.00 45.10 ? 24  GLU E N   1 
ATOM   4605  C  CA  . GLU E  1 24  ? 11.115  55.440  15.321  1.00 48.75 ? 24  GLU E CA  1 
ATOM   4606  C  C   . GLU E  1 24  ? 10.682  55.042  16.723  1.00 51.92 ? 24  GLU E C   1 
ATOM   4607  O  O   . GLU E  1 24  ? 11.292  54.166  17.340  1.00 44.19 ? 24  GLU E O   1 
ATOM   4608  C  CB  . GLU E  1 24  ? 10.372  54.609  14.279  1.00 47.60 ? 24  GLU E CB  1 
ATOM   4609  C  CG  . GLU E  1 24  ? 11.077  54.578  12.928  1.00 55.82 ? 24  GLU E CG  1 
ATOM   4610  C  CD  . GLU E  1 24  ? 11.292  55.971  12.335  1.00 62.43 ? 24  GLU E CD  1 
ATOM   4611  O  OE1 . GLU E  1 24  ? 10.477  56.884  12.609  1.00 63.10 ? 24  GLU E OE1 1 
ATOM   4612  O  OE2 . GLU E  1 24  ? 12.278  56.155  11.587  1.00 68.08 ? 24  GLU E OE2 1 
ATOM   4613  N  N   . SER E  1 25  ? 9.633   55.703  17.214  1.00 46.33 ? 25  SER E N   1 
ATOM   4614  C  CA  . SER E  1 25  ? 9.076   55.427  18.528  1.00 48.41 ? 25  SER E CA  1 
ATOM   4615  C  C   . SER E  1 25  ? 8.648   53.972  18.604  1.00 52.16 ? 25  SER E C   1 
ATOM   4616  O  O   . SER E  1 25  ? 8.803   53.328  19.648  1.00 48.21 ? 25  SER E O   1 
ATOM   4617  C  CB  . SER E  1 25  ? 7.866   56.327  18.807  1.00 44.93 ? 25  SER E CB  1 
ATOM   4618  O  OG  . SER E  1 25  ? 6.651   55.700  18.422  1.00 42.79 ? 25  SER E OG  1 
ATOM   4619  N  N   . ASN E  1 26  ? 8.115   53.456  17.495  1.00 44.84 ? 26  ASN E N   1 
ATOM   4620  C  CA  . ASN E  1 26  ? 7.644   52.075  17.456  1.00 46.60 ? 26  ASN E CA  1 
ATOM   4621  C  C   . ASN E  1 26  ? 8.611   51.128  16.732  1.00 46.21 ? 26  ASN E C   1 
ATOM   4622  O  O   . ASN E  1 26  ? 8.254   50.004  16.373  1.00 41.70 ? 26  ASN E O   1 
ATOM   4623  C  CB  . ASN E  1 26  ? 6.255   52.006  16.827  1.00 48.30 ? 26  ASN E CB  1 
ATOM   4624  C  CG  . ASN E  1 26  ? 6.247   52.477  15.388  1.00 47.84 ? 26  ASN E CG  1 
ATOM   4625  O  OD1 . ASN E  1 26  ? 7.121   53.245  14.964  1.00 47.31 ? 26  ASN E OD1 1 
ATOM   4626  N  ND2 . ASN E  1 26  ? 5.261   52.019  14.626  1.00 41.64 ? 26  ASN E ND2 1 
ATOM   4627  N  N   . GLY E  1 27  ? 9.839   51.589  16.529  1.00 43.62 ? 27  GLY E N   1 
ATOM   4628  C  CA  . GLY E  1 27  ? 10.861  50.776  15.893  1.00 47.63 ? 27  GLY E CA  1 
ATOM   4629  C  C   . GLY E  1 27  ? 11.878  50.181  16.861  1.00 52.91 ? 27  GLY E C   1 
ATOM   4630  O  O   . GLY E  1 27  ? 11.893  50.508  18.052  1.00 46.98 ? 27  GLY E O   1 
ATOM   4631  N  N   . PRO E  1 28  ? 12.739  49.292  16.350  1.00 45.48 ? 28  PRO E N   1 
ATOM   4632  C  CA  . PRO E  1 28  ? 13.791  48.627  17.119  1.00 45.04 ? 28  PRO E CA  1 
ATOM   4633  C  C   . PRO E  1 28  ? 14.919  49.559  17.538  1.00 46.86 ? 28  PRO E C   1 
ATOM   4634  O  O   . PRO E  1 28  ? 15.002  50.700  17.082  1.00 45.04 ? 28  PRO E O   1 
ATOM   4635  C  CB  . PRO E  1 28  ? 14.333  47.591  16.129  1.00 47.40 ? 28  PRO E CB  1 
ATOM   4636  C  CG  . PRO E  1 28  ? 13.976  48.127  14.787  1.00 46.46 ? 28  PRO E CG  1 
ATOM   4637  C  CD  . PRO E  1 28  ? 12.643  48.756  14.983  1.00 48.82 ? 28  PRO E CD  1 
ATOM   4638  N  N   . VAL E  1 29  ? 15.798  49.054  18.395  1.00 42.19 ? 29  VAL E N   1 
ATOM   4639  C  CA  . VAL E  1 29  ? 16.912  49.845  18.894  1.00 45.83 ? 29  VAL E CA  1 
ATOM   4640  C  C   . VAL E  1 29  ? 18.267  49.288  18.467  1.00 43.06 ? 29  VAL E C   1 
ATOM   4641  O  O   . VAL E  1 29  ? 18.557  48.108  18.640  1.00 43.75 ? 29  VAL E O   1 
ATOM   4642  C  CB  . VAL E  1 29  ? 16.874  49.954  20.437  1.00 43.50 ? 29  VAL E CB  1 
ATOM   4643  C  CG1 . VAL E  1 29  ? 18.037  50.825  20.957  1.00 39.03 ? 29  VAL E CG1 1 
ATOM   4644  C  CG2 . VAL E  1 29  ? 15.520  50.487  20.894  1.00 39.19 ? 29  VAL E CG2 1 
ATOM   4645  N  N   . LYS E  1 30  ? 19.093  50.151  17.900  1.00 43.74 ? 30  LYS E N   1 
ATOM   4646  C  CA  . LYS E  1 30  ? 20.468  49.793  17.631  1.00 46.11 ? 30  LYS E CA  1 
ATOM   4647  C  C   . LYS E  1 30  ? 21.240  49.968  18.923  1.00 46.80 ? 30  LYS E C   1 
ATOM   4648  O  O   . LYS E  1 30  ? 21.166  51.019  19.565  1.00 49.40 ? 30  LYS E O   1 
ATOM   4649  C  CB  . LYS E  1 30  ? 21.081  50.706  16.564  1.00 45.84 ? 30  LYS E CB  1 
ATOM   4650  C  CG  . LYS E  1 30  ? 20.275  50.834  15.289  1.00 52.94 ? 30  LYS E CG  1 
ATOM   4651  C  CD  . LYS E  1 30  ? 21.098  51.496  14.183  1.00 56.05 ? 30  LYS E CD  1 
ATOM   4652  C  CE  . LYS E  1 30  ? 21.166  50.606  12.942  1.00 60.41 ? 30  LYS E CE  1 
ATOM   4653  N  NZ  . LYS E  1 30  ? 21.753  49.269  13.256  1.00 50.51 ? 30  LYS E NZ  1 
ATOM   4654  N  N   . VAL E  1 31  ? 21.978  48.940  19.313  1.00 40.74 ? 31  VAL E N   1 
ATOM   4655  C  CA  . VAL E  1 31  ? 22.929  49.089  20.387  1.00 40.31 ? 31  VAL E CA  1 
ATOM   4656  C  C   . VAL E  1 31  ? 24.289  48.800  19.769  1.00 45.42 ? 31  VAL E C   1 
ATOM   4657  O  O   . VAL E  1 31  ? 24.429  47.834  19.026  1.00 49.94 ? 31  VAL E O   1 
ATOM   4658  C  CB  . VAL E  1 31  ? 22.622  48.104  21.529  1.00 42.73 ? 31  VAL E CB  1 
ATOM   4659  C  CG1 . VAL E  1 31  ? 23.636  48.249  22.643  1.00 44.31 ? 31  VAL E CG1 1 
ATOM   4660  C  CG2 . VAL E  1 31  ? 21.217  48.329  22.054  1.00 36.43 ? 31  VAL E CG2 1 
ATOM   4661  N  N   . TRP E  1 32  ? 25.281  49.641  20.040  1.00 41.39 ? 32  TRP E N   1 
ATOM   4662  C  CA  . TRP E  1 32  ? 26.614  49.404  19.504  1.00 44.39 ? 32  TRP E CA  1 
ATOM   4663  C  C   . TRP E  1 32  ? 27.677  50.153  20.292  1.00 45.20 ? 32  TRP E C   1 
ATOM   4664  O  O   . TRP E  1 32  ? 27.446  51.283  20.721  1.00 49.25 ? 32  TRP E O   1 
ATOM   4665  C  CB  . TRP E  1 32  ? 26.672  49.770  18.014  1.00 45.06 ? 32  TRP E CB  1 
ATOM   4666  C  CG  . TRP E  1 32  ? 26.274  51.184  17.713  1.00 44.46 ? 32  TRP E CG  1 
ATOM   4667  C  CD1 . TRP E  1 32  ? 25.022  51.640  17.388  1.00 43.21 ? 32  TRP E CD1 1 
ATOM   4668  C  CD2 . TRP E  1 32  ? 27.132  52.333  17.715  1.00 44.49 ? 32  TRP E CD2 1 
ATOM   4669  N  NE1 . TRP E  1 32  ? 25.057  53.002  17.184  1.00 44.40 ? 32  TRP E NE1 1 
ATOM   4670  C  CE2 . TRP E  1 32  ? 26.338  53.450  17.378  1.00 40.80 ? 32  TRP E CE2 1 
ATOM   4671  C  CE3 . TRP E  1 32  ? 28.497  52.524  17.967  1.00 47.49 ? 32  TRP E CE3 1 
ATOM   4672  C  CZ2 . TRP E  1 32  ? 26.865  54.739  17.289  1.00 44.42 ? 32  TRP E CZ2 1 
ATOM   4673  C  CZ3 . TRP E  1 32  ? 29.021  53.807  17.873  1.00 46.15 ? 32  TRP E CZ3 1 
ATOM   4674  C  CH2 . TRP E  1 32  ? 28.206  54.896  17.540  1.00 45.93 ? 32  TRP E CH2 1 
ATOM   4675  N  N   . GLY E  1 33  ? 28.837  49.529  20.492  1.00 45.31 ? 33  GLY E N   1 
ATOM   4676  C  CA  . GLY E  1 33  ? 29.893  50.151  21.277  1.00 46.61 ? 33  GLY E CA  1 
ATOM   4677  C  C   . GLY E  1 33  ? 31.136  49.305  21.479  1.00 51.09 ? 33  GLY E C   1 
ATOM   4678  O  O   . GLY E  1 33  ? 31.410  48.409  20.695  1.00 52.87 ? 33  GLY E O   1 
ATOM   4679  N  N   . SER E  1 34  ? 31.894  49.586  22.533  1.00 53.21 ? 34  SER E N   1 
ATOM   4680  C  CA  . SER E  1 34  ? 33.160  48.887  22.749  1.00 57.84 ? 34  SER E CA  1 
ATOM   4681  C  C   . SER E  1 34  ? 33.575  48.791  24.214  1.00 55.23 ? 34  SER E C   1 
ATOM   4682  O  O   . SER E  1 34  ? 33.932  49.794  24.834  1.00 54.12 ? 34  SER E O   1 
ATOM   4683  C  CB  . SER E  1 34  ? 34.282  49.553  21.944  1.00 60.24 ? 34  SER E CB  1 
ATOM   4684  O  OG  . SER E  1 34  ? 35.556  49.035  22.304  1.00 57.06 ? 34  SER E OG  1 
ATOM   4685  N  N   . ILE E  1 35  ? 33.550  47.577  24.755  1.00 53.55 ? 35  ILE E N   1 
ATOM   4686  C  CA  . ILE E  1 35  ? 33.979  47.354  26.131  1.00 57.10 ? 35  ILE E CA  1 
ATOM   4687  C  C   . ILE E  1 35  ? 35.340  46.659  26.183  1.00 55.99 ? 35  ILE E C   1 
ATOM   4688  O  O   . ILE E  1 35  ? 35.541  45.624  25.553  1.00 55.49 ? 35  ILE E O   1 
ATOM   4689  C  CB  . ILE E  1 35  ? 32.958  46.500  26.914  1.00 55.91 ? 35  ILE E CB  1 
ATOM   4690  C  CG1 . ILE E  1 35  ? 31.527  46.935  26.598  1.00 48.02 ? 35  ILE E CG1 1 
ATOM   4691  C  CG2 . ILE E  1 35  ? 33.240  46.567  28.409  1.00 57.51 ? 35  ILE E CG2 1 
ATOM   4692  C  CD1 . ILE E  1 35  ? 30.489  46.025  27.187  1.00 44.77 ? 35  ILE E CD1 1 
ATOM   4693  N  N   . LYS E  1 36  ? 36.272  47.229  26.937  1.00 55.05 ? 36  LYS E N   1 
ATOM   4694  C  CA  . LYS E  1 36  ? 37.581  46.614  27.099  1.00 59.87 ? 36  LYS E CA  1 
ATOM   4695  C  C   . LYS E  1 36  ? 37.805  46.188  28.541  1.00 59.92 ? 36  LYS E C   1 
ATOM   4696  O  O   . LYS E  1 36  ? 36.973  46.443  29.413  1.00 59.12 ? 36  LYS E O   1 
ATOM   4697  C  CB  . LYS E  1 36  ? 38.695  47.564  26.658  1.00 63.30 ? 36  LYS E CB  1 
ATOM   4698  C  CG  . LYS E  1 36  ? 38.940  48.736  27.597  1.00 59.54 ? 36  LYS E CG  1 
ATOM   4699  C  CD  . LYS E  1 36  ? 39.929  49.719  26.982  1.00 61.76 ? 36  LYS E CD  1 
ATOM   4700  C  CE  . LYS E  1 36  ? 40.509  50.662  28.026  1.00 63.84 ? 36  LYS E CE  1 
ATOM   4701  N  NZ  . LYS E  1 36  ? 40.874  51.994  27.455  1.00 58.24 ? 36  LYS E NZ  1 
ATOM   4702  N  N   . GLY E  1 37  ? 38.937  45.533  28.783  1.00 60.11 ? 37  GLY E N   1 
ATOM   4703  C  CA  . GLY E  1 37  ? 39.283  45.061  30.111  1.00 55.56 ? 37  GLY E CA  1 
ATOM   4704  C  C   . GLY E  1 37  ? 38.570  43.766  30.428  1.00 53.04 ? 37  GLY E C   1 
ATOM   4705  O  O   . GLY E  1 37  ? 38.755  43.189  31.496  1.00 58.98 ? 37  GLY E O   1 
ATOM   4706  N  N   . LEU E  1 38  ? 37.743  43.316  29.492  1.00 54.02 ? 38  LEU E N   1 
ATOM   4707  C  CA  . LEU E  1 38  ? 36.985  42.091  29.656  1.00 53.22 ? 38  LEU E CA  1 
ATOM   4708  C  C   . LEU E  1 38  ? 37.891  40.880  29.525  1.00 61.52 ? 38  LEU E C   1 
ATOM   4709  O  O   . LEU E  1 38  ? 38.918  40.933  28.845  1.00 60.11 ? 38  LEU E O   1 
ATOM   4710  C  CB  . LEU E  1 38  ? 35.876  42.012  28.608  1.00 52.08 ? 38  LEU E CB  1 
ATOM   4711  C  CG  . LEU E  1 38  ? 34.640  42.872  28.865  1.00 54.94 ? 38  LEU E CG  1 
ATOM   4712  C  CD1 . LEU E  1 38  ? 33.594  42.615  27.805  1.00 55.99 ? 38  LEU E CD1 1 
ATOM   4713  C  CD2 . LEU E  1 38  ? 34.073  42.582  30.242  1.00 51.99 ? 38  LEU E CD2 1 
ATOM   4714  N  N   . THR E  1 39  ? 37.518  39.790  30.188  1.00 62.28 ? 39  THR E N   1 
ATOM   4715  C  CA  . THR E  1 39  ? 38.166  38.514  29.939  1.00 58.84 ? 39  THR E CA  1 
ATOM   4716  C  C   . THR E  1 39  ? 37.596  37.976  28.639  1.00 60.50 ? 39  THR E C   1 
ATOM   4717  O  O   . THR E  1 39  ? 36.402  38.142  28.373  1.00 57.36 ? 39  THR E O   1 
ATOM   4718  C  CB  . THR E  1 39  ? 37.893  37.513  31.060  1.00 55.25 ? 39  THR E CB  1 
ATOM   4719  O  OG1 . THR E  1 39  ? 36.489  37.224  31.121  1.00 57.89 ? 39  THR E OG1 1 
ATOM   4720  C  CG2 . THR E  1 39  ? 38.356  38.082  32.385  1.00 58.16 ? 39  THR E CG2 1 
ATOM   4721  N  N   . GLU E  1 40  ? 38.447  37.350  27.828  1.00 59.05 ? 40  GLU E N   1 
ATOM   4722  C  CA  . GLU E  1 40  ? 38.015  36.793  26.549  1.00 60.26 ? 40  GLU E CA  1 
ATOM   4723  C  C   . GLU E  1 40  ? 36.826  35.855  26.734  1.00 56.43 ? 40  GLU E C   1 
ATOM   4724  O  O   . GLU E  1 40  ? 36.778  35.088  27.700  1.00 58.60 ? 40  GLU E O   1 
ATOM   4725  C  CB  . GLU E  1 40  ? 39.168  36.057  25.863  1.00 63.32 ? 40  GLU E CB  1 
ATOM   4726  C  CG  . GLU E  1 40  ? 38.796  35.440  24.517  1.00 67.47 ? 40  GLU E CG  1 
ATOM   4727  C  CD  . GLU E  1 40  ? 39.928  34.627  23.907  1.00 68.03 ? 40  GLU E CD  1 
ATOM   4728  O  OE1 . GLU E  1 40  ? 41.065  34.707  24.427  1.00 66.12 ? 40  GLU E OE1 1 
ATOM   4729  O  OE2 . GLU E  1 40  ? 39.679  33.908  22.912  1.00 59.92 ? 40  GLU E OE2 1 
ATOM   4730  N  N   . GLY E  1 41  ? 35.855  35.944  25.828  1.00 55.36 ? 41  GLY E N   1 
ATOM   4731  C  CA  . GLY E  1 41  ? 34.693  35.076  25.873  1.00 53.73 ? 41  GLY E CA  1 
ATOM   4732  C  C   . GLY E  1 41  ? 33.348  35.773  26.001  1.00 59.48 ? 41  GLY E C   1 
ATOM   4733  O  O   . GLY E  1 41  ? 33.172  36.913  25.567  1.00 57.86 ? 41  GLY E O   1 
ATOM   4734  N  N   . LEU E  1 42  ? 32.402  35.077  26.628  1.00 56.07 ? 42  LEU E N   1 
ATOM   4735  C  CA  . LEU E  1 42  ? 30.998  35.468  26.637  1.00 50.93 ? 42  LEU E CA  1 
ATOM   4736  C  C   . LEU E  1 42  ? 30.592  36.161  27.944  1.00 53.64 ? 42  LEU E C   1 
ATOM   4737  O  O   . LEU E  1 42  ? 30.830  35.640  29.036  1.00 51.42 ? 42  LEU E O   1 
ATOM   4738  C  CB  . LEU E  1 42  ? 30.141  34.223  26.418  1.00 47.90 ? 42  LEU E CB  1 
ATOM   4739  C  CG  . LEU E  1 42  ? 28.944  34.315  25.481  1.00 46.62 ? 42  LEU E CG  1 
ATOM   4740  C  CD1 . LEU E  1 42  ? 29.393  34.800  24.116  1.00 52.06 ? 42  LEU E CD1 1 
ATOM   4741  C  CD2 . LEU E  1 42  ? 28.269  32.967  25.377  1.00 39.31 ? 42  LEU E CD2 1 
ATOM   4742  N  N   . HIS E  1 43  ? 29.964  37.330  27.832  1.00 52.48 ? 43  HIS E N   1 
ATOM   4743  C  CA  . HIS E  1 43  ? 29.613  38.120  29.015  1.00 48.58 ? 43  HIS E CA  1 
ATOM   4744  C  C   . HIS E  1 43  ? 28.163  38.597  29.033  1.00 46.32 ? 43  HIS E C   1 
ATOM   4745  O  O   . HIS E  1 43  ? 27.688  39.186  28.068  1.00 47.10 ? 43  HIS E O   1 
ATOM   4746  C  CB  . HIS E  1 43  ? 30.547  39.318  29.141  1.00 47.81 ? 43  HIS E CB  1 
ATOM   4747  C  CG  . HIS E  1 43  ? 31.968  38.944  29.418  1.00 53.74 ? 43  HIS E CG  1 
ATOM   4748  N  ND1 . HIS E  1 43  ? 32.445  38.730  30.693  1.00 52.89 ? 43  HIS E ND1 1 
ATOM   4749  C  CD2 . HIS E  1 43  ? 33.018  38.746  28.585  1.00 53.92 ? 43  HIS E CD2 1 
ATOM   4750  C  CE1 . HIS E  1 43  ? 33.728  38.417  30.636  1.00 55.14 ? 43  HIS E CE1 1 
ATOM   4751  N  NE2 . HIS E  1 43  ? 34.100  38.422  29.368  1.00 60.55 ? 43  HIS E NE2 1 
ATOM   4752  N  N   . GLY E  1 44  ? 27.473  38.349  30.145  1.00 45.09 ? 44  GLY E N   1 
ATOM   4753  C  CA  . GLY E  1 44  ? 26.082  38.753  30.308  1.00 47.39 ? 44  GLY E CA  1 
ATOM   4754  C  C   . GLY E  1 44  ? 25.852  40.249  30.143  1.00 43.82 ? 44  GLY E C   1 
ATOM   4755  O  O   . GLY E  1 44  ? 26.615  41.071  30.671  1.00 40.50 ? 44  GLY E O   1 
ATOM   4756  N  N   . PHE E  1 45  ? 24.801  40.598  29.405  1.00 38.54 ? 45  PHE E N   1 
ATOM   4757  C  CA  . PHE E  1 45  ? 24.517  41.994  29.070  1.00 42.12 ? 45  PHE E CA  1 
ATOM   4758  C  C   . PHE E  1 45  ? 23.092  42.330  29.496  1.00 35.54 ? 45  PHE E C   1 
ATOM   4759  O  O   . PHE E  1 45  ? 22.133  41.815  28.926  1.00 33.83 ? 45  PHE E O   1 
ATOM   4760  C  CB  . PHE E  1 45  ? 24.672  42.201  27.562  1.00 38.17 ? 45  PHE E CB  1 
ATOM   4761  C  CG  . PHE E  1 45  ? 24.983  43.619  27.158  1.00 36.66 ? 45  PHE E CG  1 
ATOM   4762  C  CD1 . PHE E  1 45  ? 26.075  44.289  27.694  1.00 38.06 ? 45  PHE E CD1 1 
ATOM   4763  C  CD2 . PHE E  1 45  ? 24.213  44.264  26.198  1.00 40.78 ? 45  PHE E CD2 1 
ATOM   4764  C  CE1 . PHE E  1 45  ? 26.373  45.589  27.307  1.00 38.97 ? 45  PHE E CE1 1 
ATOM   4765  C  CE2 . PHE E  1 45  ? 24.509  45.570  25.801  1.00 40.38 ? 45  PHE E CE2 1 
ATOM   4766  C  CZ  . PHE E  1 45  ? 25.588  46.228  26.357  1.00 39.52 ? 45  PHE E CZ  1 
ATOM   4767  N  N   . HIS E  1 46  ? 22.949  43.194  30.495  1.00 33.08 ? 46  HIS E N   1 
ATOM   4768  C  CA  . HIS E  1 46  ? 21.629  43.420  31.079  1.00 36.39 ? 46  HIS E CA  1 
ATOM   4769  C  C   . HIS E  1 46  ? 21.257  44.894  31.277  1.00 33.70 ? 46  HIS E C   1 
ATOM   4770  O  O   . HIS E  1 46  ? 22.124  45.739  31.562  1.00 32.15 ? 46  HIS E O   1 
ATOM   4771  C  CB  . HIS E  1 46  ? 21.515  42.691  32.425  1.00 36.03 ? 46  HIS E CB  1 
ATOM   4772  C  CG  . HIS E  1 46  ? 21.656  41.205  32.330  1.00 38.21 ? 46  HIS E CG  1 
ATOM   4773  N  ND1 . HIS E  1 46  ? 22.231  40.450  33.329  1.00 39.19 ? 46  HIS E ND1 1 
ATOM   4774  C  CD2 . HIS E  1 46  ? 21.289  40.329  31.364  1.00 39.61 ? 46  HIS E CD2 1 
ATOM   4775  C  CE1 . HIS E  1 46  ? 22.228  39.177  32.975  1.00 38.38 ? 46  HIS E CE1 1 
ATOM   4776  N  NE2 . HIS E  1 46  ? 21.664  39.077  31.786  1.00 37.51 ? 46  HIS E NE2 1 
ATOM   4777  N  N   . VAL E  1 47  ? 19.964  45.185  31.127  1.00 25.07 ? 47  VAL E N   1 
ATOM   4778  C  CA  . VAL E  1 47  ? 19.411  46.458  31.562  1.00 26.86 ? 47  VAL E CA  1 
ATOM   4779  C  C   . VAL E  1 47  ? 18.722  46.227  32.911  1.00 28.92 ? 47  VAL E C   1 
ATOM   4780  O  O   . VAL E  1 47  ? 17.713  45.522  32.994  1.00 26.11 ? 47  VAL E O   1 
ATOM   4781  C  CB  . VAL E  1 47  ? 18.395  47.051  30.540  1.00 35.84 ? 47  VAL E CB  1 
ATOM   4782  C  CG1 . VAL E  1 47  ? 17.601  48.198  31.165  1.00 31.00 ? 47  VAL E CG1 1 
ATOM   4783  C  CG2 . VAL E  1 47  ? 19.102  47.539  29.278  1.00 29.71 ? 47  VAL E CG2 1 
ATOM   4784  N  N   . HIS E  1 48  ? 19.283  46.803  33.967  1.00 25.81 ? 48  HIS E N   1 
ATOM   4785  C  CA  . HIS E  1 48  ? 18.707  46.649  35.299  1.00 29.74 ? 48  HIS E CA  1 
ATOM   4786  C  C   . HIS E  1 48  ? 17.646  47.719  35.622  1.00 32.11 ? 48  HIS E C   1 
ATOM   4787  O  O   . HIS E  1 48  ? 17.650  48.808  35.044  1.00 31.80 ? 48  HIS E O   1 
ATOM   4788  C  CB  . HIS E  1 48  ? 19.816  46.594  36.356  1.00 28.40 ? 48  HIS E CB  1 
ATOM   4789  C  CG  . HIS E  1 48  ? 20.470  45.249  36.462  1.00 35.32 ? 48  HIS E CG  1 
ATOM   4790  N  ND1 . HIS E  1 48  ? 20.341  44.441  37.573  1.00 32.48 ? 48  HIS E ND1 1 
ATOM   4791  C  CD2 . HIS E  1 48  ? 21.227  44.556  35.578  1.00 30.44 ? 48  HIS E CD2 1 
ATOM   4792  C  CE1 . HIS E  1 48  ? 20.997  43.314  37.372  1.00 27.25 ? 48  HIS E CE1 1 
ATOM   4793  N  NE2 . HIS E  1 48  ? 21.547  43.361  36.173  1.00 32.71 ? 48  HIS E NE2 1 
ATOM   4794  N  N   . GLU E  1 49  ? 16.744  47.400  36.545  1.00 29.72 ? 49  GLU E N   1 
ATOM   4795  C  CA  . GLU E  1 49  ? 15.553  48.213  36.774  1.00 27.74 ? 49  GLU E CA  1 
ATOM   4796  C  C   . GLU E  1 49  ? 15.821  49.666  37.173  1.00 28.07 ? 49  GLU E C   1 
ATOM   4797  O  O   . GLU E  1 49  ? 15.135  50.549  36.687  1.00 27.06 ? 49  GLU E O   1 
ATOM   4798  C  CB  . GLU E  1 49  ? 14.609  47.539  37.768  1.00 28.83 ? 49  GLU E CB  1 
ATOM   4799  C  CG  . GLU E  1 49  ? 13.392  48.363  38.122  1.00 27.82 ? 49  GLU E CG  1 
ATOM   4800  C  CD  . GLU E  1 49  ? 12.379  47.586  38.933  1.00 29.55 ? 49  GLU E CD  1 
ATOM   4801  O  OE1 . GLU E  1 49  ? 12.683  46.437  39.321  1.00 36.51 ? 49  GLU E OE1 1 
ATOM   4802  O  OE2 . GLU E  1 49  ? 11.268  48.112  39.179  1.00 36.00 ? 49  GLU E OE2 1 
ATOM   4803  N  N   . PHE E  1 50  ? 16.825  49.917  38.017  1.00 27.83 ? 50  PHE E N   1 
ATOM   4804  C  CA  . PHE E  1 50  ? 17.036  51.258  38.577  1.00 27.12 ? 50  PHE E CA  1 
ATOM   4805  C  C   . PHE E  1 50  ? 18.360  51.873  38.154  1.00 29.57 ? 50  PHE E C   1 
ATOM   4806  O  O   . PHE E  1 50  ? 19.383  51.190  38.130  1.00 26.36 ? 50  PHE E O   1 
ATOM   4807  C  CB  . PHE E  1 50  ? 16.976  51.258  40.119  1.00 28.33 ? 50  PHE E CB  1 
ATOM   4808  C  CG  . PHE E  1 50  ? 15.783  50.543  40.694  1.00 26.13 ? 50  PHE E CG  1 
ATOM   4809  C  CD1 . PHE E  1 50  ? 14.516  51.055  40.552  1.00 23.53 ? 50  PHE E CD1 1 
ATOM   4810  C  CD2 . PHE E  1 50  ? 15.948  49.362  41.415  1.00 31.49 ? 50  PHE E CD2 1 
ATOM   4811  C  CE1 . PHE E  1 50  ? 13.423  50.394  41.090  1.00 30.25 ? 50  PHE E CE1 1 
ATOM   4812  C  CE2 . PHE E  1 50  ? 14.860  48.698  41.959  1.00 24.11 ? 50  PHE E CE2 1 
ATOM   4813  C  CZ  . PHE E  1 50  ? 13.597  49.212  41.795  1.00 27.60 ? 50  PHE E CZ  1 
ATOM   4814  N  N   . GLY E  1 51  ? 18.326  53.176  37.848  1.00 29.17 ? 51  GLY E N   1 
ATOM   4815  C  CA  . GLY E  1 51  ? 19.516  53.947  37.532  1.00 25.84 ? 51  GLY E CA  1 
ATOM   4816  C  C   . GLY E  1 51  ? 20.183  54.485  38.777  1.00 29.47 ? 51  GLY E C   1 
ATOM   4817  O  O   . GLY E  1 51  ? 20.578  55.655  38.854  1.00 31.78 ? 51  GLY E O   1 
ATOM   4818  N  N   . ASP E  1 52  ? 20.309  53.612  39.767  1.00 33.95 ? 52  ASP E N   1 
ATOM   4819  C  CA  . ASP E  1 52  ? 20.811  53.989  41.070  1.00 27.53 ? 52  ASP E CA  1 
ATOM   4820  C  C   . ASP E  1 52  ? 22.201  53.415  41.230  1.00 38.02 ? 52  ASP E C   1 
ATOM   4821  O  O   . ASP E  1 52  ? 22.391  52.196  41.252  1.00 37.44 ? 52  ASP E O   1 
ATOM   4822  C  CB  . ASP E  1 52  ? 19.891  53.441  42.156  1.00 30.49 ? 52  ASP E CB  1 
ATOM   4823  C  CG  . ASP E  1 52  ? 20.182  54.023  43.525  1.00 30.97 ? 52  ASP E CG  1 
ATOM   4824  O  OD1 . ASP E  1 52  ? 21.355  54.368  43.819  1.00 32.04 ? 52  ASP E OD1 1 
ATOM   4825  O  OD2 . ASP E  1 52  ? 19.221  54.141  44.311  1.00 29.63 ? 52  ASP E OD2 1 
ATOM   4826  N  N   . ASN E  1 53  ? 23.168  54.308  41.362  1.00 38.22 ? 53  ASN E N   1 
ATOM   4827  C  CA  . ASN E  1 53  ? 24.558  53.922  41.478  1.00 38.57 ? 53  ASN E CA  1 
ATOM   4828  C  C   . ASN E  1 53  ? 25.150  54.460  42.779  1.00 36.81 ? 53  ASN E C   1 
ATOM   4829  O  O   . ASN E  1 53  ? 26.356  54.670  42.888  1.00 39.79 ? 53  ASN E O   1 
ATOM   4830  C  CB  . ASN E  1 53  ? 25.334  54.428  40.257  1.00 41.46 ? 53  ASN E CB  1 
ATOM   4831  C  CG  . ASN E  1 53  ? 26.671  53.738  40.089  1.00 45.94 ? 53  ASN E CG  1 
ATOM   4832  O  OD1 . ASN E  1 53  ? 26.729  52.547  39.770  1.00 46.71 ? 53  ASN E OD1 1 
ATOM   4833  N  ND2 . ASN E  1 53  ? 27.758  54.483  40.301  1.00 44.44 ? 53  ASN E ND2 1 
ATOM   4834  N  N   . THR E  1 54  ? 24.287  54.679  43.766  1.00 37.66 ? 54  THR E N   1 
ATOM   4835  C  CA  . THR E  1 54  ? 24.721  55.154  45.076  1.00 36.49 ? 54  THR E CA  1 
ATOM   4836  C  C   . THR E  1 54  ? 25.486  54.073  45.827  1.00 40.06 ? 54  THR E C   1 
ATOM   4837  O  O   . THR E  1 54  ? 26.327  54.370  46.675  1.00 39.66 ? 54  THR E O   1 
ATOM   4838  C  CB  . THR E  1 54  ? 23.533  55.604  45.951  1.00 35.95 ? 54  THR E CB  1 
ATOM   4839  O  OG1 . THR E  1 54  ? 22.555  54.557  46.008  1.00 36.53 ? 54  THR E OG1 1 
ATOM   4840  C  CG2 . THR E  1 54  ? 22.884  56.851  45.377  1.00 31.21 ? 54  THR E CG2 1 
ATOM   4841  N  N   . ALA E  1 55  ? 25.183  52.816  45.524  1.00 43.98 ? 55  ALA E N   1 
ATOM   4842  C  CA  . ALA E  1 55  ? 25.910  51.701  46.121  1.00 45.84 ? 55  ALA E CA  1 
ATOM   4843  C  C   . ALA E  1 55  ? 26.628  50.950  45.016  1.00 44.29 ? 55  ALA E C   1 
ATOM   4844  O  O   . ALA E  1 55  ? 26.743  49.729  45.051  1.00 46.42 ? 55  ALA E O   1 
ATOM   4845  C  CB  . ALA E  1 55  ? 24.963  50.776  46.880  1.00 38.23 ? 55  ALA E CB  1 
ATOM   4846  N  N   . GLY E  1 56  ? 27.104  51.696  44.025  1.00 45.37 ? 56  GLY E N   1 
ATOM   4847  C  CA  . GLY E  1 56  ? 27.712  51.099  42.849  1.00 38.87 ? 56  GLY E CA  1 
ATOM   4848  C  C   . GLY E  1 56  ? 26.692  50.339  42.028  1.00 43.50 ? 56  GLY E C   1 
ATOM   4849  O  O   . GLY E  1 56  ? 25.515  50.718  41.965  1.00 46.39 ? 56  GLY E O   1 
ATOM   4850  N  N   . SER E  1 57  ? 27.127  49.253  41.401  1.00 40.43 ? 57  SER E N   1 
ATOM   4851  C  CA  . SER E  1 57  ? 26.214  48.447  40.609  1.00 36.45 ? 57  SER E CA  1 
ATOM   4852  C  C   . SER E  1 57  ? 25.241  47.646  41.480  1.00 39.46 ? 57  SER E C   1 
ATOM   4853  O  O   . SER E  1 57  ? 24.208  47.193  40.990  1.00 41.36 ? 57  SER E O   1 
ATOM   4854  C  CB  . SER E  1 57  ? 26.996  47.504  39.706  1.00 40.31 ? 57  SER E CB  1 
ATOM   4855  O  OG  . SER E  1 57  ? 27.586  46.478  40.478  1.00 41.42 ? 57  SER E OG  1 
ATOM   4856  N  N   . THR E  1 58  ? 25.567  47.467  42.763  1.00 41.98 ? 58  THR E N   1 
ATOM   4857  C  CA  . THR E  1 58  ? 24.712  46.686  43.667  1.00 40.38 ? 58  THR E CA  1 
ATOM   4858  C  C   . THR E  1 58  ? 23.294  47.254  43.747  1.00 41.63 ? 58  THR E C   1 
ATOM   4859  O  O   . THR E  1 58  ? 22.317  46.501  43.780  1.00 37.59 ? 58  THR E O   1 
ATOM   4860  C  CB  . THR E  1 58  ? 25.292  46.602  45.105  1.00 44.82 ? 58  THR E CB  1 
ATOM   4861  O  OG1 . THR E  1 58  ? 25.533  47.922  45.607  1.00 48.56 ? 58  THR E OG1 1 
ATOM   4862  C  CG2 . THR E  1 58  ? 26.593  45.811  45.139  1.00 37.09 ? 58  THR E CG2 1 
ATOM   4863  N  N   . SER E  1 59  ? 23.200  48.586  43.755  1.00 42.38 ? 59  SER E N   1 
ATOM   4864  C  CA  . SER E  1 59  ? 21.931  49.301  43.921  1.00 39.61 ? 59  SER E CA  1 
ATOM   4865  C  C   . SER E  1 59  ? 21.106  49.430  42.641  1.00 38.22 ? 59  SER E C   1 
ATOM   4866  O  O   . SER E  1 59  ? 20.118  50.163  42.613  1.00 34.75 ? 59  SER E O   1 
ATOM   4867  C  CB  . SER E  1 59  ? 22.173  50.690  44.524  1.00 36.79 ? 59  SER E CB  1 
ATOM   4868  O  OG  . SER E  1 59  ? 23.067  51.454  43.727  1.00 42.95 ? 59  SER E OG  1 
ATOM   4869  N  N   . ALA E  1 60  ? 21.495  48.699  41.597  1.00 35.99 ? 60  ALA E N   1 
ATOM   4870  C  CA  . ALA E  1 60  ? 20.780  48.740  40.319  1.00 33.80 ? 60  ALA E CA  1 
ATOM   4871  C  C   . ALA E  1 60  ? 19.528  47.884  40.296  1.00 30.05 ? 60  ALA E C   1 
ATOM   4872  O  O   . ALA E  1 60  ? 18.731  47.983  39.371  1.00 27.36 ? 60  ALA E O   1 
ATOM   4873  C  CB  . ALA E  1 60  ? 21.701  48.344  39.170  1.00 36.03 ? 60  ALA E CB  1 
ATOM   4874  N  N   . GLY E  1 61  ? 19.363  47.032  41.303  1.00 33.51 ? 61  GLY E N   1 
ATOM   4875  C  CA  . GLY E  1 61  ? 18.198  46.161  41.388  1.00 26.49 ? 61  GLY E CA  1 
ATOM   4876  C  C   . GLY E  1 61  ? 18.179  45.023  40.376  1.00 26.66 ? 61  GLY E C   1 
ATOM   4877  O  O   . GLY E  1 61  ? 19.170  44.767  39.699  1.00 26.67 ? 61  GLY E O   1 
ATOM   4878  N  N   . PRO E  1 62  ? 17.028  44.346  40.256  1.00 26.08 ? 62  PRO E N   1 
ATOM   4879  C  CA  . PRO E  1 62  ? 16.821  43.172  39.403  1.00 25.82 ? 62  PRO E CA  1 
ATOM   4880  C  C   . PRO E  1 62  ? 16.837  43.540  37.931  1.00 32.02 ? 62  PRO E C   1 
ATOM   4881  O  O   . PRO E  1 62  ? 17.071  44.705  37.607  1.00 31.60 ? 62  PRO E O   1 
ATOM   4882  C  CB  . PRO E  1 62  ? 15.406  42.716  39.785  1.00 23.80 ? 62  PRO E CB  1 
ATOM   4883  C  CG  . PRO E  1 62  ? 14.719  43.969  40.173  1.00 22.77 ? 62  PRO E CG  1 
ATOM   4884  C  CD  . PRO E  1 62  ? 15.770  44.777  40.900  1.00 25.42 ? 62  PRO E CD  1 
ATOM   4885  N  N   . HIS E  1 63  ? 16.605  42.556  37.063  1.00 27.38 ? 63  HIS E N   1 
ATOM   4886  C  CA  . HIS E  1 63  ? 16.500  42.797  35.633  1.00 27.05 ? 63  HIS E CA  1 
ATOM   4887  C  C   . HIS E  1 63  ? 15.243  43.601  35.382  1.00 31.17 ? 63  HIS E C   1 
ATOM   4888  O  O   . HIS E  1 63  ? 14.174  43.289  35.936  1.00 22.89 ? 63  HIS E O   1 
ATOM   4889  C  CB  . HIS E  1 63  ? 16.415  41.479  34.849  1.00 25.50 ? 63  HIS E CB  1 
ATOM   4890  C  CG  . HIS E  1 63  ? 17.716  40.745  34.757  1.00 33.41 ? 63  HIS E CG  1 
ATOM   4891  N  ND1 . HIS E  1 63  ? 17.917  39.687  33.893  1.00 30.56 ? 63  HIS E ND1 1 
ATOM   4892  C  CD2 . HIS E  1 63  ? 18.881  40.914  35.426  1.00 30.46 ? 63  HIS E CD2 1 
ATOM   4893  C  CE1 . HIS E  1 63  ? 19.154  39.243  34.030  1.00 33.57 ? 63  HIS E CE1 1 
ATOM   4894  N  NE2 . HIS E  1 63  ? 19.759  39.968  34.955  1.00 34.72 ? 63  HIS E NE2 1 
ATOM   4895  N  N   . PHE E  1 64  ? 15.368  44.633  34.549  1.00 31.20 ? 64  PHE E N   1 
ATOM   4896  C  CA  . PHE E  1 64  ? 14.196  45.399  34.156  1.00 28.66 ? 64  PHE E CA  1 
ATOM   4897  C  C   . PHE E  1 64  ? 13.161  44.440  33.584  1.00 28.76 ? 64  PHE E C   1 
ATOM   4898  O  O   . PHE E  1 64  ? 13.388  43.827  32.548  1.00 30.18 ? 64  PHE E O   1 
ATOM   4899  C  CB  . PHE E  1 64  ? 14.559  46.511  33.164  1.00 27.96 ? 64  PHE E CB  1 
ATOM   4900  C  CG  . PHE E  1 64  ? 13.373  47.313  32.706  1.00 33.78 ? 64  PHE E CG  1 
ATOM   4901  C  CD1 . PHE E  1 64  ? 12.412  47.747  33.624  1.00 32.93 ? 64  PHE E CD1 1 
ATOM   4902  C  CD2 . PHE E  1 64  ? 13.214  47.638  31.374  1.00 29.78 ? 64  PHE E CD2 1 
ATOM   4903  C  CE1 . PHE E  1 64  ? 11.312  48.484  33.212  1.00 35.47 ? 64  PHE E CE1 1 
ATOM   4904  C  CE2 . PHE E  1 64  ? 12.115  48.377  30.952  1.00 36.33 ? 64  PHE E CE2 1 
ATOM   4905  C  CZ  . PHE E  1 64  ? 11.159  48.799  31.875  1.00 35.50 ? 64  PHE E CZ  1 
ATOM   4906  N  N   . ASN E  1 65  ? 12.040  44.296  34.290  1.00 29.41 ? 65  ASN E N   1 
ATOM   4907  C  CA  . ASN E  1 65  ? 11.031  43.287  33.973  1.00 27.91 ? 65  ASN E CA  1 
ATOM   4908  C  C   . ASN E  1 65  ? 9.594   43.792  34.196  1.00 30.84 ? 65  ASN E C   1 
ATOM   4909  O  O   . ASN E  1 65  ? 8.868   43.282  35.052  1.00 30.09 ? 65  ASN E O   1 
ATOM   4910  C  CB  . ASN E  1 65  ? 11.309  42.043  34.821  1.00 29.92 ? 65  ASN E CB  1 
ATOM   4911  C  CG  . ASN E  1 65  ? 10.298  40.927  34.606  1.00 33.36 ? 65  ASN E CG  1 
ATOM   4912  O  OD1 . ASN E  1 65  ? 9.779   40.732  33.504  1.00 31.42 ? 65  ASN E OD1 1 
ATOM   4913  N  ND2 . ASN E  1 65  ? 10.011  40.185  35.678  1.00 31.16 ? 65  ASN E ND2 1 
ATOM   4914  N  N   . PRO E  1 66  ? 9.165   44.800  33.415  1.00 31.92 ? 66  PRO E N   1 
ATOM   4915  C  CA  . PRO E  1 66  ? 7.860   45.427  33.667  1.00 33.10 ? 66  PRO E CA  1 
ATOM   4916  C  C   . PRO E  1 66  ? 6.693   44.507  33.401  1.00 33.57 ? 66  PRO E C   1 
ATOM   4917  O  O   . PRO E  1 66  ? 5.588   44.788  33.844  1.00 33.65 ? 66  PRO E O   1 
ATOM   4918  C  CB  . PRO E  1 66  ? 7.830   46.580  32.666  1.00 32.61 ? 66  PRO E CB  1 
ATOM   4919  C  CG  . PRO E  1 66  ? 8.738   46.160  31.596  1.00 37.09 ? 66  PRO E CG  1 
ATOM   4920  C  CD  . PRO E  1 66  ? 9.857   45.445  32.290  1.00 32.34 ? 66  PRO E CD  1 
ATOM   4921  N  N   . LEU E  1 67  ? 6.933   43.421  32.681  1.00 36.05 ? 67  LEU E N   1 
ATOM   4922  C  CA  . LEU E  1 67  ? 5.852   42.518  32.316  1.00 36.43 ? 67  LEU E CA  1 
ATOM   4923  C  C   . LEU E  1 67  ? 5.810   41.246  33.167  1.00 37.95 ? 67  LEU E C   1 
ATOM   4924  O  O   . LEU E  1 67  ? 5.025   40.334  32.896  1.00 41.98 ? 67  LEU E O   1 
ATOM   4925  C  CB  . LEU E  1 67  ? 5.918   42.190  30.822  1.00 41.49 ? 67  LEU E CB  1 
ATOM   4926  C  CG  . LEU E  1 67  ? 5.713   43.400  29.905  1.00 44.26 ? 67  LEU E CG  1 
ATOM   4927  C  CD1 . LEU E  1 67  ? 6.029   43.062  28.457  1.00 46.71 ? 67  LEU E CD1 1 
ATOM   4928  C  CD2 . LEU E  1 67  ? 4.291   43.914  30.032  1.00 43.60 ? 67  LEU E CD2 1 
ATOM   4929  N  N   . SER E  1 68  ? 6.656   41.193  34.194  1.00 39.03 ? 68  SER E N   1 
ATOM   4930  C  CA  . SER E  1 68  ? 6.628   40.097  35.159  1.00 33.43 ? 68  SER E CA  1 
ATOM   4931  C  C   . SER E  1 68  ? 6.733   38.714  34.507  1.00 36.05 ? 68  SER E C   1 
ATOM   4932  O  O   . SER E  1 68  ? 5.922   37.833  34.774  1.00 41.34 ? 68  SER E O   1 
ATOM   4933  C  CB  . SER E  1 68  ? 5.353   40.188  35.976  1.00 35.06 ? 68  SER E CB  1 
ATOM   4934  O  OG  . SER E  1 68  ? 5.125   41.530  36.364  1.00 47.66 ? 68  SER E OG  1 
ATOM   4935  N  N   . ARG E  1 69  ? 7.725   38.546  33.643  1.00 35.40 ? 69  ARG E N   1 
ATOM   4936  C  CA  . ARG E  1 69  ? 7.973   37.282  32.959  1.00 40.60 ? 69  ARG E CA  1 
ATOM   4937  C  C   . ARG E  1 69  ? 9.283   36.695  33.492  1.00 37.77 ? 69  ARG E C   1 
ATOM   4938  O  O   . ARG E  1 69  ? 10.014  37.375  34.221  1.00 31.41 ? 69  ARG E O   1 
ATOM   4939  C  CB  . ARG E  1 69  ? 8.090   37.519  31.447  1.00 36.87 ? 69  ARG E CB  1 
ATOM   4940  C  CG  . ARG E  1 69  ? 7.115   38.569  30.902  1.00 47.07 ? 69  ARG E CG  1 
ATOM   4941  C  CD  . ARG E  1 69  ? 5.765   37.993  30.454  1.00 44.75 ? 69  ARG E CD  1 
ATOM   4942  N  NE  . ARG E  1 69  ? 5.822   37.465  29.093  1.00 54.96 ? 69  ARG E NE  1 
ATOM   4943  C  CZ  . ARG E  1 69  ? 5.796   38.213  27.987  1.00 59.69 ? 69  ARG E CZ  1 
ATOM   4944  N  NH1 . ARG E  1 69  ? 5.719   39.536  28.065  1.00 55.88 ? 69  ARG E NH1 1 
ATOM   4945  N  NH2 . ARG E  1 69  ? 5.855   37.639  26.793  1.00 63.36 ? 69  ARG E NH2 1 
ATOM   4946  N  N   . LYS E  1 70  ? 9.583   35.447  33.126  1.00 37.42 ? 70  LYS E N   1 
ATOM   4947  C  CA  . LYS E  1 70  ? 10.831  34.793  33.548  1.00 33.73 ? 70  LYS E CA  1 
ATOM   4948  C  C   . LYS E  1 70  ? 12.028  35.289  32.743  1.00 32.77 ? 70  LYS E C   1 
ATOM   4949  O  O   . LYS E  1 70  ? 11.856  35.930  31.710  1.00 33.77 ? 70  LYS E O   1 
ATOM   4950  C  CB  . LYS E  1 70  ? 10.716  33.276  33.410  1.00 38.16 ? 70  LYS E CB  1 
ATOM   4951  C  CG  . LYS E  1 70  ? 9.672   32.638  34.297  1.00 38.77 ? 70  LYS E CG  1 
ATOM   4952  C  CD  . LYS E  1 70  ? 9.552   31.148  34.006  1.00 46.13 ? 70  LYS E CD  1 
ATOM   4953  C  CE  . LYS E  1 70  ? 8.540   30.471  34.923  1.00 49.53 ? 70  LYS E CE  1 
ATOM   4954  N  NZ  . LYS E  1 70  ? 8.264   29.067  34.491  1.00 50.93 ? 70  LYS E NZ  1 
ATOM   4955  N  N   . HIS E  1 71  ? 13.240  35.003  33.213  1.00 28.91 ? 71  HIS E N   1 
ATOM   4956  C  CA  . HIS E  1 71  ? 14.442  35.432  32.493  1.00 31.93 ? 71  HIS E CA  1 
ATOM   4957  C  C   . HIS E  1 71  ? 14.605  34.636  31.213  1.00 32.78 ? 71  HIS E C   1 
ATOM   4958  O  O   . HIS E  1 71  ? 14.114  33.511  31.122  1.00 33.41 ? 71  HIS E O   1 
ATOM   4959  C  CB  . HIS E  1 71  ? 15.691  35.280  33.361  1.00 32.24 ? 71  HIS E CB  1 
ATOM   4960  C  CG  . HIS E  1 71  ? 16.975  35.504  32.620  1.00 32.43 ? 71  HIS E CG  1 
ATOM   4961  N  ND1 . HIS E  1 71  ? 17.570  36.743  32.514  1.00 37.51 ? 71  HIS E ND1 1 
ATOM   4962  C  CD2 . HIS E  1 71  ? 17.772  34.647  31.940  1.00 33.27 ? 71  HIS E CD2 1 
ATOM   4963  C  CE1 . HIS E  1 71  ? 18.684  36.640  31.812  1.00 33.32 ? 71  HIS E CE1 1 
ATOM   4964  N  NE2 . HIS E  1 71  ? 18.827  35.378  31.446  1.00 36.53 ? 71  HIS E NE2 1 
ATOM   4965  N  N   . GLY E  1 72  ? 15.285  35.225  30.229  1.00 36.07 ? 72  GLY E N   1 
ATOM   4966  C  CA  . GLY E  1 72  ? 15.501  34.585  28.941  1.00 29.70 ? 72  GLY E CA  1 
ATOM   4967  C  C   . GLY E  1 72  ? 16.630  35.221  28.151  1.00 34.43 ? 72  GLY E C   1 
ATOM   4968  O  O   . GLY E  1 72  ? 17.293  36.158  28.617  1.00 31.06 ? 72  GLY E O   1 
ATOM   4969  N  N   . GLY E  1 73  ? 16.873  34.683  26.959  1.00 35.19 ? 73  GLY E N   1 
ATOM   4970  C  CA  . GLY E  1 73  ? 17.742  35.335  25.993  1.00 32.69 ? 73  GLY E CA  1 
ATOM   4971  C  C   . GLY E  1 73  ? 16.935  36.291  25.122  1.00 33.39 ? 73  GLY E C   1 
ATOM   4972  O  O   . GLY E  1 73  ? 15.699  36.222  25.107  1.00 29.69 ? 73  GLY E O   1 
ATOM   4973  N  N   . PRO E  1 74  ? 17.626  37.197  24.405  1.00 36.03 ? 74  PRO E N   1 
ATOM   4974  C  CA  . PRO E  1 74  ? 17.004  38.197  23.526  1.00 36.04 ? 74  PRO E CA  1 
ATOM   4975  C  C   . PRO E  1 74  ? 15.968  37.604  22.572  1.00 39.29 ? 74  PRO E C   1 
ATOM   4976  O  O   . PRO E  1 74  ? 14.817  38.043  22.583  1.00 37.51 ? 74  PRO E O   1 
ATOM   4977  C  CB  . PRO E  1 74  ? 18.190  38.766  22.729  1.00 36.61 ? 74  PRO E CB  1 
ATOM   4978  C  CG  . PRO E  1 74  ? 19.444  38.154  23.319  1.00 36.65 ? 74  PRO E CG  1 
ATOM   4979  C  CD  . PRO E  1 74  ? 19.062  37.462  24.590  1.00 37.75 ? 74  PRO E CD  1 
ATOM   4980  N  N   . LYS E  1 75  ? 16.362  36.609  21.779  1.00 37.89 ? 75  LYS E N   1 
ATOM   4981  C  CA  . LYS E  1 75  ? 15.468  36.061  20.758  1.00 39.38 ? 75  LYS E CA  1 
ATOM   4982  C  C   . LYS E  1 75  ? 14.234  35.341  21.324  1.00 39.48 ? 75  LYS E C   1 
ATOM   4983  O  O   . LYS E  1 75  ? 13.358  34.946  20.562  1.00 39.21 ? 75  LYS E O   1 
ATOM   4984  C  CB  . LYS E  1 75  ? 16.223  35.129  19.797  1.00 43.94 ? 75  LYS E CB  1 
ATOM   4985  C  CG  . LYS E  1 75  ? 17.603  35.629  19.342  1.00 47.71 ? 75  LYS E CG  1 
ATOM   4986  C  CD  . LYS E  1 75  ? 18.185  34.756  18.216  1.00 52.86 ? 75  LYS E CD  1 
ATOM   4987  C  CE  . LYS E  1 75  ? 17.358  34.871  16.931  1.00 52.03 ? 75  LYS E CE  1 
ATOM   4988  N  NZ  . LYS E  1 75  ? 17.739  33.891  15.859  1.00 52.67 ? 75  LYS E NZ  1 
ATOM   4989  N  N   . ASP E  1 76  ? 14.158  35.166  22.644  1.00 39.45 ? 76  ASP E N   1 
ATOM   4990  C  CA  . ASP E  1 76  ? 13.024  34.443  23.242  1.00 39.96 ? 76  ASP E CA  1 
ATOM   4991  C  C   . ASP E  1 76  ? 11.811  35.321  23.470  1.00 40.99 ? 76  ASP E C   1 
ATOM   4992  O  O   . ASP E  1 76  ? 11.938  36.520  23.712  1.00 44.29 ? 76  ASP E O   1 
ATOM   4993  C  CB  . ASP E  1 76  ? 13.404  33.808  24.577  1.00 39.94 ? 76  ASP E CB  1 
ATOM   4994  C  CG  . ASP E  1 76  ? 14.560  32.857  24.457  1.00 47.61 ? 76  ASP E CG  1 
ATOM   4995  O  OD1 . ASP E  1 76  ? 14.603  32.111  23.448  1.00 47.51 ? 76  ASP E OD1 1 
ATOM   4996  O  OD2 . ASP E  1 76  ? 15.427  32.868  25.369  1.00 45.18 ? 76  ASP E OD2 1 
ATOM   4997  N  N   . GLU E  1 77  ? 10.633  34.714  23.422  1.00 40.27 ? 77  GLU E N   1 
ATOM   4998  C  CA  . GLU E  1 77  ? 9.416   35.436  23.732  1.00 43.88 ? 77  GLU E CA  1 
ATOM   4999  C  C   . GLU E  1 77  ? 9.301   35.577  25.239  1.00 49.56 ? 77  GLU E C   1 
ATOM   5000  O  O   . GLU E  1 77  ? 8.701   36.528  25.749  1.00 49.05 ? 77  GLU E O   1 
ATOM   5001  C  CB  . GLU E  1 77  ? 8.196   34.701  23.197  1.00 49.34 ? 77  GLU E CB  1 
ATOM   5002  C  CG  . GLU E  1 77  ? 6.888   35.400  23.549  1.00 62.07 ? 77  GLU E CG  1 
ATOM   5003  C  CD  . GLU E  1 77  ? 5.665   34.577  23.208  1.00 69.84 ? 77  GLU E CD  1 
ATOM   5004  O  OE1 . GLU E  1 77  ? 4.977   34.121  24.151  1.00 69.66 ? 77  GLU E OE1 1 
ATOM   5005  O  OE2 . GLU E  1 77  ? 5.389   34.398  22.001  1.00 72.44 ? 77  GLU E OE2 1 
ATOM   5006  N  N   . GLU E  1 78  ? 9.872   34.609  25.950  1.00 51.49 ? 78  GLU E N   1 
ATOM   5007  C  CA  . GLU E  1 78  ? 9.917   34.654  27.404  1.00 44.95 ? 78  GLU E CA  1 
ATOM   5008  C  C   . GLU E  1 78  ? 11.226  35.296  27.826  1.00 45.52 ? 78  GLU E C   1 
ATOM   5009  O  O   . GLU E  1 78  ? 12.284  34.654  27.831  1.00 42.82 ? 78  GLU E O   1 
ATOM   5010  C  CB  . GLU E  1 78  ? 9.787   33.254  27.997  1.00 47.81 ? 78  GLU E CB  1 
ATOM   5011  C  CG  . GLU E  1 78  ? 9.241   33.236  29.411  1.00 48.58 ? 78  GLU E CG  1 
ATOM   5012  C  CD  . GLU E  1 78  ? 7.861   33.858  29.501  1.00 51.49 ? 78  GLU E CD  1 
ATOM   5013  O  OE1 . GLU E  1 78  ? 7.156   33.908  28.465  1.00 56.45 ? 78  GLU E OE1 1 
ATOM   5014  O  OE2 . GLU E  1 78  ? 7.482   34.303  30.605  1.00 47.69 ? 78  GLU E OE2 1 
ATOM   5015  N  N   . ARG E  1 79  ? 11.153  36.581  28.151  1.00 39.41 ? 79  ARG E N   1 
ATOM   5016  C  CA  . ARG E  1 79  ? 12.333  37.328  28.552  1.00 35.26 ? 79  ARG E CA  1 
ATOM   5017  C  C   . ARG E  1 79  ? 11.933  38.528  29.397  1.00 36.64 ? 79  ARG E C   1 
ATOM   5018  O  O   . ARG E  1 79  ? 10.754  38.895  29.486  1.00 33.46 ? 79  ARG E O   1 
ATOM   5019  C  CB  . ARG E  1 79  ? 13.143  37.793  27.332  1.00 33.05 ? 79  ARG E CB  1 
ATOM   5020  C  CG  . ARG E  1 79  ? 12.306  38.478  26.244  1.00 36.93 ? 79  ARG E CG  1 
ATOM   5021  C  CD  . ARG E  1 79  ? 13.178  39.173  25.187  1.00 38.89 ? 79  ARG E CD  1 
ATOM   5022  N  NE  . ARG E  1 79  ? 13.814  40.390  25.692  1.00 39.24 ? 79  ARG E NE  1 
ATOM   5023  C  CZ  . ARG E  1 79  ? 14.576  41.197  24.959  1.00 38.94 ? 79  ARG E CZ  1 
ATOM   5024  N  NH1 . ARG E  1 79  ? 14.794  40.919  23.680  1.00 38.43 ? 79  ARG E NH1 1 
ATOM   5025  N  NH2 . ARG E  1 79  ? 15.118  42.284  25.499  1.00 31.73 ? 79  ARG E NH2 1 
ATOM   5026  N  N   . HIS E  1 80  ? 12.931  39.108  30.045  1.00 34.20 ? 80  HIS E N   1 
ATOM   5027  C  CA  . HIS E  1 80  ? 12.768  40.391  30.684  1.00 33.95 ? 80  HIS E CA  1 
ATOM   5028  C  C   . HIS E  1 80  ? 13.134  41.393  29.604  1.00 34.08 ? 80  HIS E C   1 
ATOM   5029  O  O   . HIS E  1 80  ? 14.032  41.135  28.786  1.00 28.42 ? 80  HIS E O   1 
ATOM   5030  C  CB  . HIS E  1 80  ? 13.722  40.520  31.875  1.00 28.62 ? 80  HIS E CB  1 
ATOM   5031  C  CG  . HIS E  1 80  ? 13.495  39.498  32.947  1.00 29.91 ? 80  HIS E CG  1 
ATOM   5032  N  ND1 . HIS E  1 80  ? 14.528  38.894  33.636  1.00 24.48 ? 80  HIS E ND1 1 
ATOM   5033  C  CD2 . HIS E  1 80  ? 12.352  38.963  33.437  1.00 29.00 ? 80  HIS E CD2 1 
ATOM   5034  C  CE1 . HIS E  1 80  ? 14.028  38.048  34.517  1.00 26.39 ? 80  HIS E CE1 1 
ATOM   5035  N  NE2 . HIS E  1 80  ? 12.710  38.064  34.412  1.00 27.25 ? 80  HIS E NE2 1 
ATOM   5036  N  N   . VAL E  1 81  ? 12.440  42.526  29.595  1.00 28.73 ? 81  VAL E N   1 
ATOM   5037  C  CA  . VAL E  1 81  ? 12.776  43.601  28.681  1.00 29.01 ? 81  VAL E CA  1 
ATOM   5038  C  C   . VAL E  1 81  ? 14.274  43.867  28.763  1.00 31.31 ? 81  VAL E C   1 
ATOM   5039  O  O   . VAL E  1 81  ? 14.943  44.047  27.748  1.00 34.59 ? 81  VAL E O   1 
ATOM   5040  C  CB  . VAL E  1 81  ? 11.996  44.888  29.020  1.00 35.68 ? 81  VAL E CB  1 
ATOM   5041  C  CG1 . VAL E  1 81  ? 12.582  46.106  28.260  1.00 27.70 ? 81  VAL E CG1 1 
ATOM   5042  C  CG2 . VAL E  1 81  ? 10.480  44.697  28.754  1.00 25.08 ? 81  VAL E CG2 1 
ATOM   5043  N  N   . GLY E  1 82  ? 14.811  43.845  29.974  1.00 26.87 ? 82  GLY E N   1 
ATOM   5044  C  CA  . GLY E  1 82  ? 16.224  44.099  30.159  1.00 29.96 ? 82  GLY E CA  1 
ATOM   5045  C  C   . GLY E  1 82  ? 17.154  43.004  29.661  1.00 28.52 ? 82  GLY E C   1 
ATOM   5046  O  O   . GLY E  1 82  ? 18.373  43.130  29.816  1.00 33.67 ? 82  GLY E O   1 
ATOM   5047  N  N   . ASP E  1 83  ? 16.602  41.948  29.060  1.00 29.52 ? 83  ASP E N   1 
ATOM   5048  C  CA  . ASP E  1 83  ? 17.409  40.784  28.646  1.00 35.00 ? 83  ASP E CA  1 
ATOM   5049  C  C   . ASP E  1 83  ? 18.067  40.887  27.268  1.00 32.39 ? 83  ASP E C   1 
ATOM   5050  O  O   . ASP E  1 83  ? 17.505  40.438  26.271  1.00 31.43 ? 83  ASP E O   1 
ATOM   5051  C  CB  . ASP E  1 83  ? 16.590  39.490  28.715  1.00 31.95 ? 83  ASP E CB  1 
ATOM   5052  C  CG  . ASP E  1 83  ? 16.359  39.035  30.123  1.00 31.88 ? 83  ASP E CG  1 
ATOM   5053  O  OD1 . ASP E  1 83  ? 17.204  39.386  30.994  1.00 30.32 ? 83  ASP E OD1 1 
ATOM   5054  O  OD2 . ASP E  1 83  ? 15.340  38.338  30.352  1.00 28.56 ? 83  ASP E OD2 1 
ATOM   5055  N  N   . LEU E  1 84  ? 19.277  41.438  27.236  1.00 34.01 ? 84  LEU E N   1 
ATOM   5056  C  CA  . LEU E  1 84  ? 20.008  41.630  25.987  1.00 36.16 ? 84  LEU E CA  1 
ATOM   5057  C  C   . LEU E  1 84  ? 21.010  40.509  25.696  1.00 40.38 ? 84  LEU E C   1 
ATOM   5058  O  O   . LEU E  1 84  ? 21.702  40.533  24.679  1.00 41.12 ? 84  LEU E O   1 
ATOM   5059  C  CB  . LEU E  1 84  ? 20.721  42.984  26.007  1.00 36.09 ? 84  LEU E CB  1 
ATOM   5060  C  CG  . LEU E  1 84  ? 19.762  44.158  26.226  1.00 36.35 ? 84  LEU E CG  1 
ATOM   5061  C  CD1 . LEU E  1 84  ? 20.493  45.488  26.126  1.00 36.65 ? 84  LEU E CD1 1 
ATOM   5062  C  CD2 . LEU E  1 84  ? 18.576  44.089  25.258  1.00 28.46 ? 84  LEU E CD2 1 
ATOM   5063  N  N   . GLY E  1 85  ? 21.094  39.539  26.601  1.00 39.54 ? 85  GLY E N   1 
ATOM   5064  C  CA  . GLY E  1 85  ? 21.880  38.345  26.364  1.00 37.00 ? 85  GLY E CA  1 
ATOM   5065  C  C   . GLY E  1 85  ? 23.349  38.451  26.693  1.00 39.17 ? 85  GLY E C   1 
ATOM   5066  O  O   . GLY E  1 85  ? 23.736  38.800  27.812  1.00 39.19 ? 85  GLY E O   1 
ATOM   5067  N  N   . ASN E  1 86  ? 24.173  38.139  25.702  1.00 39.02 ? 86  ASN E N   1 
ATOM   5068  C  CA  . ASN E  1 86  ? 25.608  38.079  25.897  1.00 40.99 ? 86  ASN E CA  1 
ATOM   5069  C  C   . ASN E  1 86  ? 26.351  38.947  24.903  1.00 37.94 ? 86  ASN E C   1 
ATOM   5070  O  O   . ASN E  1 86  ? 25.985  39.009  23.737  1.00 34.62 ? 86  ASN E O   1 
ATOM   5071  C  CB  . ASN E  1 86  ? 26.087  36.628  25.763  1.00 42.69 ? 86  ASN E CB  1 
ATOM   5072  C  CG  . ASN E  1 86  ? 25.634  35.754  26.921  1.00 41.34 ? 86  ASN E CG  1 
ATOM   5073  O  OD1 . ASN E  1 86  ? 26.208  35.810  28.010  1.00 45.16 ? 86  ASN E OD1 1 
ATOM   5074  N  ND2 . ASN E  1 86  ? 24.604  34.945  26.693  1.00 38.77 ? 86  ASN E ND2 1 
ATOM   5075  N  N   . VAL E  1 87  ? 27.383  39.634  25.371  1.00 39.50 ? 87  VAL E N   1 
ATOM   5076  C  CA  . VAL E  1 87  ? 28.340  40.242  24.461  1.00 46.12 ? 87  VAL E CA  1 
ATOM   5077  C  C   . VAL E  1 87  ? 29.584  39.371  24.464  1.00 49.36 ? 87  VAL E C   1 
ATOM   5078  O  O   . VAL E  1 87  ? 29.791  38.581  25.386  1.00 48.74 ? 87  VAL E O   1 
ATOM   5079  C  CB  . VAL E  1 87  ? 28.718  41.690  24.852  1.00 44.12 ? 87  VAL E CB  1 
ATOM   5080  C  CG1 . VAL E  1 87  ? 27.510  42.610  24.745  1.00 43.27 ? 87  VAL E CG1 1 
ATOM   5081  C  CG2 . VAL E  1 87  ? 29.332  41.731  26.236  1.00 40.81 ? 87  VAL E CG2 1 
ATOM   5082  N  N   . THR E  1 88  ? 30.418  39.533  23.441  1.00 57.50 ? 88  THR E N   1 
ATOM   5083  C  CA  . THR E  1 88  ? 31.531  38.621  23.212  1.00 54.95 ? 88  THR E CA  1 
ATOM   5084  C  C   . THR E  1 88  ? 32.878  39.331  23.037  1.00 57.30 ? 88  THR E C   1 
ATOM   5085  O  O   . THR E  1 88  ? 33.117  40.011  22.039  1.00 61.57 ? 88  THR E O   1 
ATOM   5086  C  CB  . THR E  1 88  ? 31.256  37.738  21.988  1.00 54.65 ? 88  THR E CB  1 
ATOM   5087  O  OG1 . THR E  1 88  ? 29.881  37.318  21.993  1.00 54.80 ? 88  THR E OG1 1 
ATOM   5088  C  CG2 . THR E  1 88  ? 32.163  36.524  22.006  1.00 58.28 ? 88  THR E CG2 1 
ATOM   5089  N  N   . ALA E  1 89  ? 33.756  39.156  24.019  1.00 56.83 ? 89  ALA E N   1 
ATOM   5090  C  CA  . ALA E  1 89  ? 35.088  39.747  23.985  1.00 61.95 ? 89  ALA E CA  1 
ATOM   5091  C  C   . ALA E  1 89  ? 36.054  38.932  23.122  1.00 66.04 ? 89  ALA E C   1 
ATOM   5092  O  O   . ALA E  1 89  ? 35.883  37.720  22.960  1.00 63.06 ? 89  ALA E O   1 
ATOM   5093  C  CB  . ALA E  1 89  ? 35.633  39.889  25.400  1.00 60.78 ? 89  ALA E CB  1 
ATOM   5094  N  N   . ASP E  1 90  ? 37.067  39.609  22.578  1.00 67.44 ? 90  ASP E N   1 
ATOM   5095  C  CA  . ASP E  1 90  ? 38.081  38.960  21.747  1.00 68.30 ? 90  ASP E CA  1 
ATOM   5096  C  C   . ASP E  1 90  ? 39.272  38.474  22.571  1.00 69.76 ? 90  ASP E C   1 
ATOM   5097  O  O   . ASP E  1 90  ? 39.264  38.569  23.804  1.00 70.17 ? 90  ASP E O   1 
ATOM   5098  C  CB  . ASP E  1 90  ? 38.545  39.884  20.606  1.00 66.51 ? 90  ASP E CB  1 
ATOM   5099  C  CG  . ASP E  1 90  ? 39.264  41.147  21.097  1.00 64.85 ? 90  ASP E CG  1 
ATOM   5100  O  OD1 . ASP E  1 90  ? 39.761  41.190  22.243  1.00 63.81 ? 90  ASP E OD1 1 
ATOM   5101  O  OD2 . ASP E  1 90  ? 39.348  42.113  20.311  1.00 62.80 ? 90  ASP E OD2 1 
ATOM   5102  N  N   . LYS E  1 91  ? 40.297  37.975  21.883  1.00 67.34 ? 91  LYS E N   1 
ATOM   5103  C  CA  . LYS E  1 91  ? 41.510  37.482  22.535  1.00 70.85 ? 91  LYS E CA  1 
ATOM   5104  C  C   . LYS E  1 91  ? 42.130  38.535  23.453  1.00 68.60 ? 91  LYS E C   1 
ATOM   5105  O  O   . LYS E  1 91  ? 42.682  38.209  24.506  1.00 66.65 ? 91  LYS E O   1 
ATOM   5106  C  CB  . LYS E  1 91  ? 42.520  37.000  21.480  1.00 72.99 ? 91  LYS E CB  1 
ATOM   5107  C  CG  . LYS E  1 91  ? 43.994  37.234  21.817  1.00 72.20 ? 91  LYS E CG  1 
ATOM   5108  C  CD  . LYS E  1 91  ? 44.525  36.245  22.850  1.00 72.47 ? 91  LYS E CD  1 
ATOM   5109  C  CE  . LYS E  1 91  ? 45.821  36.752  23.481  1.00 75.69 ? 91  LYS E CE  1 
ATOM   5110  N  NZ  . LYS E  1 91  ? 45.621  38.021  24.242  1.00 70.25 ? 91  LYS E NZ  1 
ATOM   5111  N  N   . ASP E  1 92  ? 42.015  39.799  23.056  1.00 70.61 ? 92  ASP E N   1 
ATOM   5112  C  CA  . ASP E  1 92  ? 42.587  40.908  23.818  1.00 72.47 ? 92  ASP E CA  1 
ATOM   5113  C  C   . ASP E  1 92  ? 41.660  41.399  24.938  1.00 71.54 ? 92  ASP E C   1 
ATOM   5114  O  O   . ASP E  1 92  ? 42.098  42.111  25.847  1.00 70.45 ? 92  ASP E O   1 
ATOM   5115  C  CB  . ASP E  1 92  ? 42.920  42.068  22.877  1.00 68.29 ? 92  ASP E CB  1 
ATOM   5116  C  CG  . ASP E  1 92  ? 43.616  41.606  21.617  1.00 66.78 ? 92  ASP E CG  1 
ATOM   5117  O  OD1 . ASP E  1 92  ? 44.448  40.679  21.706  1.00 63.18 ? 92  ASP E OD1 1 
ATOM   5118  O  OD2 . ASP E  1 92  ? 43.322  42.163  20.538  1.00 63.86 ? 92  ASP E OD2 1 
ATOM   5119  N  N   . GLY E  1 93  ? 40.384  41.019  24.865  1.00 68.59 ? 93  GLY E N   1 
ATOM   5120  C  CA  . GLY E  1 93  ? 39.400  41.444  25.845  1.00 63.43 ? 93  GLY E CA  1 
ATOM   5121  C  C   . GLY E  1 93  ? 38.628  42.672  25.396  1.00 64.88 ? 93  GLY E C   1 
ATOM   5122  O  O   . GLY E  1 93  ? 38.240  43.516  26.209  1.00 61.22 ? 93  GLY E O   1 
ATOM   5123  N  N   . VAL E  1 94  ? 38.408  42.769  24.088  1.00 66.38 ? 94  VAL E N   1 
ATOM   5124  C  CA  . VAL E  1 94  ? 37.682  43.892  23.510  1.00 63.26 ? 94  VAL E CA  1 
ATOM   5125  C  C   . VAL E  1 94  ? 36.429  43.407  22.773  1.00 63.43 ? 94  VAL E C   1 
ATOM   5126  O  O   . VAL E  1 94  ? 36.491  42.945  21.627  1.00 65.51 ? 94  VAL E O   1 
ATOM   5127  C  CB  . VAL E  1 94  ? 38.591  44.742  22.583  1.00 64.28 ? 94  VAL E CB  1 
ATOM   5128  C  CG1 . VAL E  1 94  ? 37.775  45.763  21.785  1.00 62.13 ? 94  VAL E CG1 1 
ATOM   5129  C  CG2 . VAL E  1 94  ? 39.678  45.437  23.398  1.00 62.47 ? 94  VAL E CG2 1 
ATOM   5130  N  N   . ALA E  1 95  ? 35.293  43.497  23.455  1.00 59.69 ? 95  ALA E N   1 
ATOM   5131  C  CA  . ALA E  1 95  ? 34.014  43.139  22.863  1.00 60.00 ? 95  ALA E CA  1 
ATOM   5132  C  C   . ALA E  1 95  ? 33.474  44.324  22.089  1.00 61.20 ? 95  ALA E C   1 
ATOM   5133  O  O   . ALA E  1 95  ? 33.253  45.393  22.658  1.00 65.34 ? 95  ALA E O   1 
ATOM   5134  C  CB  . ALA E  1 95  ? 33.026  42.733  23.943  1.00 61.37 ? 95  ALA E CB  1 
ATOM   5135  N  N   . ASP E  1 96  ? 33.267  44.141  20.792  1.00 62.94 ? 96  ASP E N   1 
ATOM   5136  C  CA  . ASP E  1 96  ? 32.630  45.172  19.988  1.00 59.89 ? 96  ASP E CA  1 
ATOM   5137  C  C   . ASP E  1 96  ? 31.151  44.882  19.847  1.00 56.51 ? 96  ASP E C   1 
ATOM   5138  O  O   . ASP E  1 96  ? 30.747  43.935  19.171  1.00 56.77 ? 96  ASP E O   1 
ATOM   5139  C  CB  . ASP E  1 96  ? 33.306  45.322  18.628  1.00 58.27 ? 96  ASP E CB  1 
ATOM   5140  C  CG  . ASP E  1 96  ? 34.626  46.058  18.726  1.00 66.68 ? 96  ASP E CG  1 
ATOM   5141  O  OD1 . ASP E  1 96  ? 34.610  47.309  18.707  1.00 64.32 ? 96  ASP E OD1 1 
ATOM   5142  O  OD2 . ASP E  1 96  ? 35.676  45.387  18.850  1.00 68.90 ? 96  ASP E OD2 1 
ATOM   5143  N  N   . VAL E  1 97  ? 30.357  45.718  20.507  1.00 54.25 ? 97  VAL E N   1 
ATOM   5144  C  CA  . VAL E  1 97  ? 28.922  45.521  20.618  1.00 50.84 ? 97  VAL E CA  1 
ATOM   5145  C  C   . VAL E  1 97  ? 28.180  46.019  19.387  1.00 49.34 ? 97  VAL E C   1 
ATOM   5146  O  O   . VAL E  1 97  ? 28.486  47.077  18.848  1.00 48.91 ? 97  VAL E O   1 
ATOM   5147  C  CB  . VAL E  1 97  ? 28.378  46.236  21.868  1.00 54.53 ? 97  VAL E CB  1 
ATOM   5148  C  CG1 . VAL E  1 97  ? 26.899  45.935  22.055  1.00 53.68 ? 97  VAL E CG1 1 
ATOM   5149  C  CG2 . VAL E  1 97  ? 29.177  45.814  23.102  1.00 52.60 ? 97  VAL E CG2 1 
ATOM   5150  N  N   . SER E  1 98  ? 27.206  45.238  18.946  1.00 47.33 ? 98  SER E N   1 
ATOM   5151  C  CA  . SER E  1 98  ? 26.374  45.604  17.817  1.00 43.70 ? 98  SER E CA  1 
ATOM   5152  C  C   . SER E  1 98  ? 25.167  44.695  17.855  1.00 43.60 ? 98  SER E C   1 
ATOM   5153  O  O   . SER E  1 98  ? 25.273  43.503  17.602  1.00 47.63 ? 98  SER E O   1 
ATOM   5154  C  CB  . SER E  1 98  ? 27.129  45.422  16.501  1.00 46.06 ? 98  SER E CB  1 
ATOM   5155  O  OG  . SER E  1 98  ? 26.413  46.003  15.424  1.00 48.20 ? 98  SER E OG  1 
ATOM   5156  N  N   . ILE E  1 99  ? 24.019  45.259  18.208  1.00 47.49 ? 99  ILE E N   1 
ATOM   5157  C  CA  . ILE E  1 99  ? 22.820  44.478  18.464  1.00 44.34 ? 99  ILE E CA  1 
ATOM   5158  C  C   . ILE E  1 99  ? 21.648  45.275  17.943  1.00 41.71 ? 99  ILE E C   1 
ATOM   5159  O  O   . ILE E  1 99  ? 21.722  46.498  17.874  1.00 44.01 ? 99  ILE E O   1 
ATOM   5160  C  CB  . ILE E  1 99  ? 22.612  44.278  19.990  1.00 44.01 ? 99  ILE E CB  1 
ATOM   5161  C  CG1 . ILE E  1 99  ? 23.911  43.819  20.671  1.00 46.19 ? 99  ILE E CG1 1 
ATOM   5162  C  CG2 . ILE E  1 99  ? 21.472  43.302  20.274  1.00 44.09 ? 99  ILE E CG2 1 
ATOM   5163  C  CD1 . ILE E  1 99  ? 23.924  43.984  22.185  1.00 47.64 ? 99  ILE E CD1 1 
ATOM   5164  N  N   . GLU E  1 100 ? 20.575  44.586  17.574  1.00 34.42 ? 100 GLU E N   1 
ATOM   5165  C  CA  . GLU E  1 100 ? 19.296  45.226  17.328  1.00 38.37 ? 100 GLU E CA  1 
ATOM   5166  C  C   . GLU E  1 100 ? 18.213  44.497  18.107  1.00 45.27 ? 100 GLU E C   1 
ATOM   5167  O  O   . GLU E  1 100 ? 18.025  43.291  17.934  1.00 45.25 ? 100 GLU E O   1 
ATOM   5168  C  CB  . GLU E  1 100 ? 18.942  45.208  15.844  1.00 46.44 ? 100 GLU E CB  1 
ATOM   5169  C  CG  . GLU E  1 100 ? 19.664  46.248  15.001  1.00 47.48 ? 100 GLU E CG  1 
ATOM   5170  C  CD  . GLU E  1 100 ? 18.733  46.890  13.975  1.00 51.24 ? 100 GLU E CD  1 
ATOM   5171  O  OE1 . GLU E  1 100 ? 17.621  46.346  13.754  1.00 44.69 ? 100 GLU E OE1 1 
ATOM   5172  O  OE2 . GLU E  1 100 ? 19.110  47.940  13.403  1.00 49.26 ? 100 GLU E OE2 1 
ATOM   5173  N  N   . ASP E  1 101 ? 17.488  45.229  18.950  1.00 43.14 ? 101 ASP E N   1 
ATOM   5174  C  CA  . ASP E  1 101 ? 16.455  44.621  19.780  1.00 39.28 ? 101 ASP E CA  1 
ATOM   5175  C  C   . ASP E  1 101 ? 15.127  45.342  19.652  1.00 37.95 ? 101 ASP E C   1 
ATOM   5176  O  O   . ASP E  1 101 ? 15.082  46.566  19.590  1.00 42.24 ? 101 ASP E O   1 
ATOM   5177  C  CB  . ASP E  1 101 ? 16.887  44.595  21.255  1.00 39.71 ? 101 ASP E CB  1 
ATOM   5178  C  CG  . ASP E  1 101 ? 16.053  43.641  22.079  1.00 36.63 ? 101 ASP E CG  1 
ATOM   5179  O  OD1 . ASP E  1 101 ? 16.437  42.460  22.150  1.00 38.81 ? 101 ASP E OD1 1 
ATOM   5180  O  OD2 . ASP E  1 101 ? 15.005  44.053  22.628  1.00 39.66 ? 101 ASP E OD2 1 
ATOM   5181  N  N   . SER E  1 102 ? 14.048  44.576  19.640  1.00 31.53 ? 102 SER E N   1 
ATOM   5182  C  CA  . SER E  1 102 ? 12.724  45.128  19.417  1.00 34.77 ? 102 SER E CA  1 
ATOM   5183  C  C   . SER E  1 102 ? 11.838  44.985  20.655  1.00 41.60 ? 102 SER E C   1 
ATOM   5184  O  O   . SER E  1 102 ? 10.610  45.030  20.558  1.00 43.12 ? 102 SER E O   1 
ATOM   5185  C  CB  . SER E  1 102 ? 12.052  44.413  18.250  1.00 46.30 ? 102 SER E CB  1 
ATOM   5186  O  OG  . SER E  1 102 ? 11.173  43.406  18.739  1.00 50.61 ? 102 SER E OG  1 
ATOM   5187  N  N   . VAL E  1 103 ? 12.456  44.786  21.816  1.00 40.99 ? 103 VAL E N   1 
ATOM   5188  C  CA  . VAL E  1 103 ? 11.695  44.689  23.056  1.00 38.98 ? 103 VAL E CA  1 
ATOM   5189  C  C   . VAL E  1 103 ? 11.988  45.919  23.917  1.00 32.53 ? 103 VAL E C   1 
ATOM   5190  O  O   . VAL E  1 103 ? 11.088  46.499  24.512  1.00 35.02 ? 103 VAL E O   1 
ATOM   5191  C  CB  . VAL E  1 103 ? 11.980  43.363  23.820  1.00 34.86 ? 103 VAL E CB  1 
ATOM   5192  C  CG1 . VAL E  1 103 ? 11.251  43.338  25.156  1.00 35.73 ? 103 VAL E CG1 1 
ATOM   5193  C  CG2 . VAL E  1 103 ? 11.542  42.175  22.988  1.00 36.34 ? 103 VAL E CG2 1 
ATOM   5194  N  N   . ILE E  1 104 ? 13.249  46.328  23.957  1.00 29.45 ? 104 ILE E N   1 
ATOM   5195  C  CA  . ILE E  1 104 ? 13.608  47.575  24.610  1.00 32.09 ? 104 ILE E CA  1 
ATOM   5196  C  C   . ILE E  1 104 ? 13.086  48.801  23.823  1.00 40.92 ? 104 ILE E C   1 
ATOM   5197  O  O   . ILE E  1 104 ? 12.605  48.672  22.692  1.00 38.34 ? 104 ILE E O   1 
ATOM   5198  C  CB  . ILE E  1 104 ? 15.124  47.683  24.805  1.00 33.86 ? 104 ILE E CB  1 
ATOM   5199  C  CG1 . ILE E  1 104 ? 15.852  47.558  23.470  1.00 26.19 ? 104 ILE E CG1 1 
ATOM   5200  C  CG2 . ILE E  1 104 ? 15.619  46.612  25.764  1.00 35.22 ? 104 ILE E CG2 1 
ATOM   5201  C  CD1 . ILE E  1 104 ? 17.273  48.089  23.532  1.00 25.08 ? 104 ILE E CD1 1 
ATOM   5202  N  N   . SER E  1 105 ? 13.162  49.979  24.437  1.00 39.48 ? 105 SER E N   1 
ATOM   5203  C  CA  . SER E  1 105 ? 12.755  51.224  23.783  1.00 41.69 ? 105 SER E CA  1 
ATOM   5204  C  C   . SER E  1 105 ? 13.429  52.429  24.427  1.00 43.64 ? 105 SER E C   1 
ATOM   5205  O  O   . SER E  1 105 ? 13.781  52.393  25.609  1.00 41.86 ? 105 SER E O   1 
ATOM   5206  C  CB  . SER E  1 105 ? 11.246  51.401  23.817  1.00 39.41 ? 105 SER E CB  1 
ATOM   5207  O  OG  . SER E  1 105 ? 10.901  52.589  23.131  1.00 44.60 ? 105 SER E OG  1 
ATOM   5208  N  N   . LEU E  1 106 ? 13.627  53.488  23.649  1.00 43.39 ? 106 LEU E N   1 
ATOM   5209  C  CA  . LEU E  1 106 ? 14.286  54.682  24.164  1.00 40.07 ? 106 LEU E CA  1 
ATOM   5210  C  C   . LEU E  1 106 ? 13.248  55.704  24.606  1.00 39.23 ? 106 LEU E C   1 
ATOM   5211  O  O   . LEU E  1 106 ? 13.582  56.815  25.021  1.00 38.12 ? 106 LEU E O   1 
ATOM   5212  C  CB  . LEU E  1 106 ? 15.218  55.292  23.117  1.00 38.98 ? 106 LEU E CB  1 
ATOM   5213  C  CG  . LEU E  1 106 ? 16.517  54.543  22.806  1.00 43.75 ? 106 LEU E CG  1 
ATOM   5214  C  CD1 . LEU E  1 106 ? 17.553  55.474  22.171  1.00 37.70 ? 106 LEU E CD1 1 
ATOM   5215  C  CD2 . LEU E  1 106 ? 17.083  53.881  24.055  1.00 40.38 ? 106 LEU E CD2 1 
ATOM   5216  N  N   . SER E  1 107 ? 11.985  55.306  24.526  1.00 35.39 ? 107 SER E N   1 
ATOM   5217  C  CA  . SER E  1 107 ? 10.875  56.203  24.769  1.00 40.51 ? 107 SER E CA  1 
ATOM   5218  C  C   . SER E  1 107 ? 9.676   55.350  25.122  1.00 41.08 ? 107 SER E C   1 
ATOM   5219  O  O   . SER E  1 107 ? 9.767   54.129  25.131  1.00 39.16 ? 107 SER E O   1 
ATOM   5220  C  CB  . SER E  1 107 ? 10.573  57.032  23.509  1.00 41.92 ? 107 SER E CB  1 
ATOM   5221  O  OG  . SER E  1 107 ? 10.152  56.215  22.419  1.00 38.19 ? 107 SER E OG  1 
ATOM   5222  N  N   . GLY E  1 108 ? 8.549   55.997  25.397  1.00 49.46 ? 108 GLY E N   1 
ATOM   5223  C  CA  . GLY E  1 108 ? 7.316   55.292  25.698  1.00 46.33 ? 108 GLY E CA  1 
ATOM   5224  C  C   . GLY E  1 108 ? 7.263   54.796  27.132  1.00 51.31 ? 108 GLY E C   1 
ATOM   5225  O  O   . GLY E  1 108 ? 8.209   54.987  27.902  1.00 56.28 ? 108 GLY E O   1 
ATOM   5226  N  N   . ASP E  1 109 ? 6.165   54.128  27.477  1.00 51.31 ? 109 ASP E N   1 
ATOM   5227  C  CA  . ASP E  1 109 ? 5.882   53.744  28.859  1.00 56.82 ? 109 ASP E CA  1 
ATOM   5228  C  C   . ASP E  1 109 ? 6.919   52.795  29.482  1.00 57.98 ? 109 ASP E C   1 
ATOM   5229  O  O   . ASP E  1 109 ? 7.224   52.901  30.674  1.00 59.26 ? 109 ASP E O   1 
ATOM   5230  C  CB  . ASP E  1 109 ? 4.474   53.142  28.954  1.00 58.63 ? 109 ASP E CB  1 
ATOM   5231  C  CG  . ASP E  1 109 ? 4.006   52.967  30.386  1.00 64.05 ? 109 ASP E CG  1 
ATOM   5232  O  OD1 . ASP E  1 109 ? 4.549   53.656  31.278  1.00 65.31 ? 109 ASP E OD1 1 
ATOM   5233  O  OD2 . ASP E  1 109 ? 3.089   52.146  30.618  1.00 63.21 ? 109 ASP E OD2 1 
ATOM   5234  N  N   . HIS E  1 110 ? 7.456   51.877  28.684  1.00 52.99 ? 110 HIS E N   1 
ATOM   5235  C  CA  . HIS E  1 110 ? 8.432   50.905  29.179  1.00 45.46 ? 110 HIS E CA  1 
ATOM   5236  C  C   . HIS E  1 110 ? 9.813   51.115  28.572  1.00 45.79 ? 110 HIS E C   1 
ATOM   5237  O  O   . HIS E  1 110 ? 10.462  50.172  28.117  1.00 42.29 ? 110 HIS E O   1 
ATOM   5238  C  CB  . HIS E  1 110 ? 7.940   49.491  28.912  1.00 46.63 ? 110 HIS E CB  1 
ATOM   5239  C  CG  . HIS E  1 110 ? 6.699   49.146  29.671  1.00 51.02 ? 110 HIS E CG  1 
ATOM   5240  N  ND1 . HIS E  1 110 ? 6.297   49.847  30.788  1.00 55.05 ? 110 HIS E ND1 1 
ATOM   5241  C  CD2 . HIS E  1 110 ? 5.765   48.185  29.475  1.00 52.55 ? 110 HIS E CD2 1 
ATOM   5242  C  CE1 . HIS E  1 110 ? 5.174   49.328  31.252  1.00 54.94 ? 110 HIS E CE1 1 
ATOM   5243  N  NE2 . HIS E  1 110 ? 4.828   48.320  30.472  1.00 54.70 ? 110 HIS E NE2 1 
ATOM   5244  N  N   . CYS E  1 111 ? 10.257  52.366  28.568  1.00 39.46 ? 111 CYS E N   1 
ATOM   5245  C  CA  . CYS E  1 111 ? 11.556  52.682  28.032  1.00 38.12 ? 111 CYS E CA  1 
ATOM   5246  C  C   . CYS E  1 111 ? 12.622  52.336  29.049  1.00 38.81 ? 111 CYS E C   1 
ATOM   5247  O  O   . CYS E  1 111 ? 12.321  52.066  30.210  1.00 43.94 ? 111 CYS E O   1 
ATOM   5248  C  CB  . CYS E  1 111 ? 11.647  54.159  27.620  1.00 42.17 ? 111 CYS E CB  1 
ATOM   5249  S  SG  . CYS E  1 111 ? 11.825  55.383  28.934  1.00 39.68 ? 111 CYS E SG  1 
ATOM   5250  N  N   . ILE E  1 112 ? 13.871  52.362  28.608  1.00 33.79 ? 112 ILE E N   1 
ATOM   5251  C  CA  . ILE E  1 112 ? 14.978  51.937  29.433  1.00 34.94 ? 112 ILE E CA  1 
ATOM   5252  C  C   . ILE E  1 112 ? 15.804  53.153  29.796  1.00 33.41 ? 112 ILE E C   1 
ATOM   5253  O  O   . ILE E  1 112 ? 16.857  53.034  30.410  1.00 27.80 ? 112 ILE E O   1 
ATOM   5254  C  CB  . ILE E  1 112 ? 15.866  50.950  28.669  1.00 36.81 ? 112 ILE E CB  1 
ATOM   5255  C  CG1 . ILE E  1 112 ? 16.593  51.689  27.538  1.00 35.54 ? 112 ILE E CG1 1 
ATOM   5256  C  CG2 . ILE E  1 112 ? 15.022  49.790  28.139  1.00 27.49 ? 112 ILE E CG2 1 
ATOM   5257  C  CD1 . ILE E  1 112 ? 17.732  50.911  26.919  1.00 37.14 ? 112 ILE E CD1 1 
ATOM   5258  N  N   . ILE E  1 113 ? 15.324  54.326  29.398  1.00 31.07 ? 113 ILE E N   1 
ATOM   5259  C  CA  . ILE E  1 113 ? 15.989  55.572  29.752  1.00 31.94 ? 113 ILE E CA  1 
ATOM   5260  C  C   . ILE E  1 113 ? 15.965  55.749  31.272  1.00 27.23 ? 113 ILE E C   1 
ATOM   5261  O  O   . ILE E  1 113 ? 14.944  55.535  31.891  1.00 28.48 ? 113 ILE E O   1 
ATOM   5262  C  CB  . ILE E  1 113 ? 15.318  56.779  29.048  1.00 32.94 ? 113 ILE E CB  1 
ATOM   5263  C  CG1 . ILE E  1 113 ? 15.723  56.819  27.573  1.00 34.74 ? 113 ILE E CG1 1 
ATOM   5264  C  CG2 . ILE E  1 113 ? 15.733  58.098  29.694  1.00 32.38 ? 113 ILE E CG2 1 
ATOM   5265  C  CD1 . ILE E  1 113 ? 17.218  57.102  27.384  1.00 34.86 ? 113 ILE E CD1 1 
ATOM   5266  N  N   . GLY E  1 114 ? 17.102  56.107  31.858  1.00 27.28 ? 114 GLY E N   1 
ATOM   5267  C  CA  . GLY E  1 114 ? 17.180  56.356  33.285  1.00 33.65 ? 114 GLY E CA  1 
ATOM   5268  C  C   . GLY E  1 114 ? 17.528  55.130  34.117  1.00 36.64 ? 114 GLY E C   1 
ATOM   5269  O  O   . GLY E  1 114 ? 17.591  55.202  35.353  1.00 30.57 ? 114 GLY E O   1 
ATOM   5270  N  N   . ARG E  1 115 ? 17.762  54.009  33.436  1.00 36.12 ? 115 ARG E N   1 
ATOM   5271  C  CA  . ARG E  1 115 ? 18.043  52.741  34.094  1.00 31.49 ? 115 ARG E CA  1 
ATOM   5272  C  C   . ARG E  1 115 ? 19.504  52.365  33.935  1.00 34.28 ? 115 ARG E C   1 
ATOM   5273  O  O   . ARG E  1 115 ? 20.297  53.155  33.423  1.00 35.06 ? 115 ARG E O   1 
ATOM   5274  C  CB  . ARG E  1 115 ? 17.109  51.654  33.577  1.00 27.68 ? 115 ARG E CB  1 
ATOM   5275  C  CG  . ARG E  1 115 ? 15.670  52.125  33.555  1.00 27.46 ? 115 ARG E CG  1 
ATOM   5276  C  CD  . ARG E  1 115 ? 14.676  50.997  33.532  1.00 22.75 ? 115 ARG E CD  1 
ATOM   5277  N  NE  . ARG E  1 115 ? 13.305  51.501  33.434  1.00 23.60 ? 115 ARG E NE  1 
ATOM   5278  C  CZ  . ARG E  1 115 ? 12.422  51.517  34.433  1.00 33.14 ? 115 ARG E CZ  1 
ATOM   5279  N  NH1 . ARG E  1 115 ? 12.738  51.051  35.645  1.00 28.84 ? 115 ARG E NH1 1 
ATOM   5280  N  NH2 . ARG E  1 115 ? 11.205  51.992  34.221  1.00 27.51 ? 115 ARG E NH2 1 
ATOM   5281  N  N   . THR E  1 116 ? 19.870  51.175  34.400  1.00 34.40 ? 116 THR E N   1 
ATOM   5282  C  CA  . THR E  1 116 ? 21.274  50.810  34.456  1.00 28.19 ? 116 THR E CA  1 
ATOM   5283  C  C   . THR E  1 116 ? 21.649  49.706  33.467  1.00 32.74 ? 116 THR E C   1 
ATOM   5284  O  O   . THR E  1 116 ? 20.942  48.712  33.320  1.00 32.92 ? 116 THR E O   1 
ATOM   5285  C  CB  . THR E  1 116 ? 21.695  50.455  35.892  1.00 31.93 ? 116 THR E CB  1 
ATOM   5286  O  OG1 . THR E  1 116 ? 21.281  51.509  36.770  1.00 33.90 ? 116 THR E OG1 1 
ATOM   5287  C  CG2 . THR E  1 116 ? 23.212  50.311  36.000  1.00 29.43 ? 116 THR E CG2 1 
ATOM   5288  N  N   . LEU E  1 117 ? 22.759  49.917  32.767  1.00 35.12 ? 117 LEU E N   1 
ATOM   5289  C  CA  . LEU E  1 117 ? 23.280  48.944  31.827  1.00 34.49 ? 117 LEU E CA  1 
ATOM   5290  C  C   . LEU E  1 117 ? 24.397  48.214  32.532  1.00 30.73 ? 117 LEU E C   1 
ATOM   5291  O  O   . LEU E  1 117 ? 25.236  48.841  33.171  1.00 32.46 ? 117 LEU E O   1 
ATOM   5292  C  CB  . LEU E  1 117 ? 23.832  49.636  30.579  1.00 34.10 ? 117 LEU E CB  1 
ATOM   5293  C  CG  . LEU E  1 117 ? 24.133  48.702  29.405  1.00 34.37 ? 117 LEU E CG  1 
ATOM   5294  C  CD1 . LEU E  1 117 ? 22.841  48.113  28.883  1.00 32.07 ? 117 LEU E CD1 1 
ATOM   5295  C  CD2 . LEU E  1 117 ? 24.899  49.412  28.292  1.00 36.32 ? 117 LEU E CD2 1 
ATOM   5296  N  N   . VAL E  1 118 ? 24.394  46.888  32.442  1.00 33.66 ? 118 VAL E N   1 
ATOM   5297  C  CA  . VAL E  1 118 ? 25.397  46.079  33.140  1.00 39.21 ? 118 VAL E CA  1 
ATOM   5298  C  C   . VAL E  1 118 ? 26.061  45.030  32.233  1.00 32.27 ? 118 VAL E C   1 
ATOM   5299  O  O   . VAL E  1 118 ? 25.400  44.357  31.438  1.00 33.33 ? 118 VAL E O   1 
ATOM   5300  C  CB  . VAL E  1 118 ? 24.797  45.393  34.406  1.00 36.70 ? 118 VAL E CB  1 
ATOM   5301  C  CG1 . VAL E  1 118 ? 25.878  44.670  35.208  1.00 29.40 ? 118 VAL E CG1 1 
ATOM   5302  C  CG2 . VAL E  1 118 ? 24.085  46.419  35.285  1.00 33.69 ? 118 VAL E CG2 1 
ATOM   5303  N  N   . VAL E  1 119 ? 27.378  44.913  32.357  1.00 39.67 ? 119 VAL E N   1 
ATOM   5304  C  CA  . VAL E  1 119 ? 28.128  43.853  31.691  1.00 42.21 ? 119 VAL E CA  1 
ATOM   5305  C  C   . VAL E  1 119 ? 28.689  42.915  32.760  1.00 43.04 ? 119 VAL E C   1 
ATOM   5306  O  O   . VAL E  1 119 ? 29.331  43.362  33.716  1.00 49.83 ? 119 VAL E O   1 
ATOM   5307  C  CB  . VAL E  1 119 ? 29.247  44.429  30.775  1.00 36.93 ? 119 VAL E CB  1 
ATOM   5308  C  CG1 . VAL E  1 119 ? 30.229  45.267  31.574  1.00 39.10 ? 119 VAL E CG1 1 
ATOM   5309  C  CG2 . VAL E  1 119 ? 29.956  43.310  30.005  1.00 41.07 ? 119 VAL E CG2 1 
ATOM   5310  N  N   . HIS E  1 120 ? 28.440  41.615  32.604  1.00 48.17 ? 120 HIS E N   1 
ATOM   5311  C  CA  . HIS E  1 120 ? 28.733  40.638  33.666  1.00 50.89 ? 120 HIS E CA  1 
ATOM   5312  C  C   . HIS E  1 120 ? 30.035  39.825  33.559  1.00 50.54 ? 120 HIS E C   1 
ATOM   5313  O  O   . HIS E  1 120 ? 30.699  39.800  32.521  1.00 48.66 ? 120 HIS E O   1 
ATOM   5314  C  CB  . HIS E  1 120 ? 27.549  39.688  33.851  1.00 46.02 ? 120 HIS E CB  1 
ATOM   5315  C  CG  . HIS E  1 120 ? 26.335  40.354  34.410  1.00 43.31 ? 120 HIS E CG  1 
ATOM   5316  N  ND1 . HIS E  1 120 ? 26.114  40.476  35.765  1.00 43.15 ? 120 HIS E ND1 1 
ATOM   5317  C  CD2 . HIS E  1 120 ? 25.285  40.951  33.800  1.00 38.58 ? 120 HIS E CD2 1 
ATOM   5318  C  CE1 . HIS E  1 120 ? 24.976  41.115  35.965  1.00 39.97 ? 120 HIS E CE1 1 
ATOM   5319  N  NE2 . HIS E  1 120 ? 24.458  41.419  34.789  1.00 41.92 ? 120 HIS E NE2 1 
ATOM   5320  N  N   . GLU E  1 121 ? 30.367  39.160  34.667  1.00 50.13 ? 121 GLU E N   1 
ATOM   5321  C  CA  . GLU E  1 121 ? 31.576  38.349  34.811  1.00 51.15 ? 121 GLU E CA  1 
ATOM   5322  C  C   . GLU E  1 121 ? 31.549  37.106  33.925  1.00 49.51 ? 121 GLU E C   1 
ATOM   5323  O  O   . GLU E  1 121 ? 32.490  36.838  33.179  1.00 53.14 ? 121 GLU E O   1 
ATOM   5324  C  CB  . GLU E  1 121 ? 31.740  37.947  36.283  1.00 54.68 ? 121 GLU E CB  1 
ATOM   5325  C  CG  . GLU E  1 121 ? 32.713  36.809  36.546  1.00 54.22 ? 121 GLU E CG  1 
ATOM   5326  C  CD  . GLU E  1 121 ? 32.721  36.382  38.007  1.00 58.58 ? 121 GLU E CD  1 
ATOM   5327  O  OE1 . GLU E  1 121 ? 32.956  35.186  38.285  1.00 60.60 ? 121 GLU E OE1 1 
ATOM   5328  O  OE2 . GLU E  1 121 ? 32.492  37.244  38.882  1.00 60.05 ? 121 GLU E OE2 1 
ATOM   5329  N  N   . LYS E  1 122 ? 30.465  36.346  34.014  1.00 51.72 ? 122 LYS E N   1 
ATOM   5330  C  CA  . LYS E  1 122 ? 30.297  35.166  33.179  1.00 49.63 ? 122 LYS E CA  1 
ATOM   5331  C  C   . LYS E  1 122 ? 29.254  35.448  32.122  1.00 45.95 ? 122 LYS E C   1 
ATOM   5332  O  O   . LYS E  1 122 ? 28.701  36.543  32.054  1.00 48.50 ? 122 LYS E O   1 
ATOM   5333  C  CB  . LYS E  1 122 ? 29.834  33.965  34.010  1.00 46.14 ? 122 LYS E CB  1 
ATOM   5334  C  CG  . LYS E  1 122 ? 30.521  33.826  35.352  1.00 52.89 ? 122 LYS E CG  1 
ATOM   5335  C  CD  . LYS E  1 122 ? 29.896  32.714  36.176  1.00 54.29 ? 122 LYS E CD  1 
ATOM   5336  C  CE  . LYS E  1 122 ? 30.518  32.652  37.557  1.00 53.84 ? 122 LYS E CE  1 
ATOM   5337  N  NZ  . LYS E  1 122 ? 30.286  31.325  38.169  1.00 59.83 ? 122 LYS E NZ  1 
ATOM   5338  N  N   . ALA E  1 123 ? 28.980  34.432  31.316  1.00 46.02 ? 123 ALA E N   1 
ATOM   5339  C  CA  . ALA E  1 123 ? 27.942  34.485  30.310  1.00 45.08 ? 123 ALA E CA  1 
ATOM   5340  C  C   . ALA E  1 123 ? 26.580  34.222  30.929  1.00 44.39 ? 123 ALA E C   1 
ATOM   5341  O  O   . ALA E  1 123 ? 26.480  33.722  32.044  1.00 46.38 ? 123 ALA E O   1 
ATOM   5342  C  CB  . ALA E  1 123 ? 28.221  33.468  29.236  1.00 47.44 ? 123 ALA E CB  1 
ATOM   5343  N  N   . ASP E  1 124 ? 25.538  34.539  30.170  1.00 39.99 ? 124 ASP E N   1 
ATOM   5344  C  CA  . ASP E  1 124 ? 24.151  34.414  30.597  1.00 41.76 ? 124 ASP E CA  1 
ATOM   5345  C  C   . ASP E  1 124 ? 23.584  33.105  30.058  1.00 43.86 ? 124 ASP E C   1 
ATOM   5346  O  O   . ASP E  1 124 ? 23.600  32.876  28.848  1.00 41.93 ? 124 ASP E O   1 
ATOM   5347  C  CB  . ASP E  1 124 ? 23.367  35.602  30.015  1.00 42.38 ? 124 ASP E CB  1 
ATOM   5348  C  CG  . ASP E  1 124 ? 21.937  35.688  30.526  1.00 44.84 ? 124 ASP E CG  1 
ATOM   5349  O  OD1 . ASP E  1 124 ? 21.194  34.676  30.481  1.00 40.51 ? 124 ASP E OD1 1 
ATOM   5350  O  OD2 . ASP E  1 124 ? 21.552  36.796  30.963  1.00 41.48 ? 124 ASP E OD2 1 
ATOM   5351  N  N   . ASP E  1 125 ? 23.060  32.251  30.933  1.00 38.83 ? 125 ASP E N   1 
ATOM   5352  C  CA  . ASP E  1 125 ? 22.558  30.955  30.472  1.00 38.08 ? 125 ASP E CA  1 
ATOM   5353  C  C   . ASP E  1 125 ? 21.242  31.050  29.711  1.00 40.56 ? 125 ASP E C   1 
ATOM   5354  O  O   . ASP E  1 125 ? 20.692  30.035  29.276  1.00 37.91 ? 125 ASP E O   1 
ATOM   5355  C  CB  . ASP E  1 125 ? 22.522  29.887  31.593  1.00 37.32 ? 125 ASP E CB  1 
ATOM   5356  C  CG  . ASP E  1 125 ? 21.501  30.179  32.692  1.00 35.50 ? 125 ASP E CG  1 
ATOM   5357  O  OD1 . ASP E  1 125 ? 20.306  30.356  32.400  1.00 34.09 ? 125 ASP E OD1 1 
ATOM   5358  O  OD2 . ASP E  1 125 ? 21.901  30.184  33.878  1.00 41.53 ? 125 ASP E OD2 1 
ATOM   5359  N  N   . LEU E  1 126 ? 20.745  32.276  29.556  1.00 41.46 ? 126 LEU E N   1 
ATOM   5360  C  CA  . LEU E  1 126 ? 19.550  32.546  28.763  1.00 34.49 ? 126 LEU E CA  1 
ATOM   5361  C  C   . LEU E  1 126 ? 18.335  31.830  29.316  1.00 35.20 ? 126 LEU E C   1 
ATOM   5362  O  O   . LEU E  1 126 ? 17.357  31.604  28.603  1.00 36.15 ? 126 LEU E O   1 
ATOM   5363  C  CB  . LEU E  1 126 ? 19.781  32.170  27.287  1.00 41.69 ? 126 LEU E CB  1 
ATOM   5364  C  CG  . LEU E  1 126 ? 21.097  32.701  26.711  1.00 41.49 ? 126 LEU E CG  1 
ATOM   5365  C  CD1 . LEU E  1 126 ? 21.320  32.222  25.290  1.00 44.63 ? 126 LEU E CD1 1 
ATOM   5366  C  CD2 . LEU E  1 126 ? 21.134  34.223  26.779  1.00 41.51 ? 126 LEU E CD2 1 
ATOM   5367  N  N   . GLY E  1 127 ? 18.399  31.462  30.590  1.00 35.96 ? 127 GLY E N   1 
ATOM   5368  C  CA  . GLY E  1 127 ? 17.292  30.774  31.226  1.00 33.54 ? 127 GLY E CA  1 
ATOM   5369  C  C   . GLY E  1 127 ? 17.247  29.279  30.964  1.00 36.90 ? 127 GLY E C   1 
ATOM   5370  O  O   . GLY E  1 127 ? 16.234  28.631  31.235  1.00 36.37 ? 127 GLY E O   1 
ATOM   5371  N  N   . LYS E  1 128 ? 18.338  28.720  30.452  1.00 36.96 ? 128 LYS E N   1 
ATOM   5372  C  CA  . LYS E  1 128 ? 18.360  27.292  30.114  1.00 44.48 ? 128 LYS E CA  1 
ATOM   5373  C  C   . LYS E  1 128 ? 19.225  26.495  31.091  1.00 42.43 ? 128 LYS E C   1 
ATOM   5374  O  O   . LYS E  1 128 ? 19.553  25.337  30.830  1.00 40.39 ? 128 LYS E O   1 
ATOM   5375  C  CB  . LYS E  1 128 ? 18.869  27.068  28.675  1.00 37.91 ? 128 LYS E CB  1 
ATOM   5376  C  CG  . LYS E  1 128 ? 18.152  27.874  27.593  1.00 35.64 ? 128 LYS E CG  1 
ATOM   5377  C  CD  . LYS E  1 128 ? 16.636  27.675  27.654  1.00 47.95 ? 128 LYS E CD  1 
ATOM   5378  C  CE  . LYS E  1 128 ? 15.928  28.224  26.407  1.00 47.36 ? 128 LYS E CE  1 
ATOM   5379  N  NZ  . LYS E  1 128 ? 16.169  29.688  26.175  1.00 45.59 ? 128 LYS E NZ  1 
ATOM   5380  N  N   . GLY E  1 129 ? 19.581  27.119  32.213  1.00 40.68 ? 129 GLY E N   1 
ATOM   5381  C  CA  . GLY E  1 129 ? 20.575  26.576  33.123  1.00 39.36 ? 129 GLY E CA  1 
ATOM   5382  C  C   . GLY E  1 129 ? 20.125  25.434  34.021  1.00 38.92 ? 129 GLY E C   1 
ATOM   5383  O  O   . GLY E  1 129 ? 20.960  24.758  34.636  1.00 38.82 ? 129 GLY E O   1 
ATOM   5384  N  N   . GLY E  1 130 ? 18.817  25.226  34.119  1.00 28.91 ? 130 GLY E N   1 
ATOM   5385  C  CA  . GLY E  1 130 ? 18.290  24.118  34.894  1.00 32.63 ? 130 GLY E CA  1 
ATOM   5386  C  C   . GLY E  1 130 ? 18.164  24.359  36.392  1.00 36.74 ? 130 GLY E C   1 
ATOM   5387  O  O   . GLY E  1 130 ? 18.042  23.413  37.170  1.00 34.41 ? 130 GLY E O   1 
ATOM   5388  N  N   . ASN E  1 131 ? 18.201  25.623  36.801  1.00 35.72 ? 131 ASN E N   1 
ATOM   5389  C  CA  . ASN E  1 131 ? 17.964  25.986  38.200  1.00 34.44 ? 131 ASN E CA  1 
ATOM   5390  C  C   . ASN E  1 131 ? 17.006  27.180  38.369  1.00 34.79 ? 131 ASN E C   1 
ATOM   5391  O  O   . ASN E  1 131 ? 16.660  27.868  37.404  1.00 33.18 ? 131 ASN E O   1 
ATOM   5392  C  CB  . ASN E  1 131 ? 19.282  26.235  38.945  1.00 30.42 ? 131 ASN E CB  1 
ATOM   5393  C  CG  . ASN E  1 131 ? 20.251  27.081  38.151  1.00 35.49 ? 131 ASN E CG  1 
ATOM   5394  O  OD1 . ASN E  1 131 ? 20.024  28.275  37.933  1.00 36.35 ? 131 ASN E OD1 1 
ATOM   5395  N  ND2 . ASN E  1 131 ? 21.349  26.466  37.714  1.00 38.59 ? 131 ASN E ND2 1 
ATOM   5396  N  N   . GLU E  1 132 ? 16.572  27.405  39.601  1.00 27.70 ? 132 GLU E N   1 
ATOM   5397  C  CA  . GLU E  1 132 ? 15.662  28.490  39.906  1.00 28.74 ? 132 GLU E CA  1 
ATOM   5398  C  C   . GLU E  1 132 ? 16.288  29.843  39.605  1.00 33.38 ? 132 GLU E C   1 
ATOM   5399  O  O   . GLU E  1 132 ? 15.610  30.761  39.150  1.00 33.82 ? 132 GLU E O   1 
ATOM   5400  C  CB  . GLU E  1 132 ? 15.208  28.413  41.366  1.00 27.17 ? 132 GLU E CB  1 
ATOM   5401  C  CG  . GLU E  1 132 ? 14.240  29.517  41.785  1.00 29.38 ? 132 GLU E CG  1 
ATOM   5402  C  CD  . GLU E  1 132 ? 12.942  29.528  40.981  1.00 36.72 ? 132 GLU E CD  1 
ATOM   5403  O  OE1 . GLU E  1 132 ? 12.694  28.574  40.206  1.00 39.43 ? 132 GLU E OE1 1 
ATOM   5404  O  OE2 . GLU E  1 132 ? 12.163  30.501  41.135  1.00 35.66 ? 132 GLU E OE2 1 
ATOM   5405  N  N   . GLU E  1 133 ? 17.593  29.952  39.827  1.00 32.93 ? 133 GLU E N   1 
ATOM   5406  C  CA  . GLU E  1 133 ? 18.291  31.215  39.640  1.00 31.95 ? 133 GLU E CA  1 
ATOM   5407  C  C   . GLU E  1 133 ? 18.398  31.550  38.160  1.00 36.57 ? 133 GLU E C   1 
ATOM   5408  O  O   . GLU E  1 133 ? 18.518  32.720  37.792  1.00 36.65 ? 133 GLU E O   1 
ATOM   5409  C  CB  . GLU E  1 133 ? 19.679  31.164  40.287  1.00 34.59 ? 133 GLU E CB  1 
ATOM   5410  C  CG  . GLU E  1 133 ? 20.327  32.521  40.526  1.00 37.24 ? 133 GLU E CG  1 
ATOM   5411  C  CD  . GLU E  1 133 ? 19.462  33.441  41.373  1.00 38.37 ? 133 GLU E CD  1 
ATOM   5412  O  OE1 . GLU E  1 133 ? 19.173  33.090  42.543  1.00 32.19 ? 133 GLU E OE1 1 
ATOM   5413  O  OE2 . GLU E  1 133 ? 19.066  34.512  40.858  1.00 33.66 ? 133 GLU E OE2 1 
ATOM   5414  N  N   . SER E  1 134 ? 18.346  30.519  37.317  1.00 35.59 ? 134 SER E N   1 
ATOM   5415  C  CA  . SER E  1 134 ? 18.452  30.696  35.876  1.00 31.16 ? 134 SER E CA  1 
ATOM   5416  C  C   . SER E  1 134 ? 17.227  31.415  35.312  1.00 32.23 ? 134 SER E C   1 
ATOM   5417  O  O   . SER E  1 134 ? 17.334  32.267  34.439  1.00 33.40 ? 134 SER E O   1 
ATOM   5418  C  CB  . SER E  1 134 ? 18.611  29.337  35.198  1.00 37.23 ? 134 SER E CB  1 
ATOM   5419  O  OG  . SER E  1 134 ? 18.519  29.447  33.791  1.00 34.55 ? 134 SER E OG  1 
ATOM   5420  N  N   . THR E  1 135 ? 16.053  31.070  35.817  1.00 33.69 ? 135 THR E N   1 
ATOM   5421  C  CA  . THR E  1 135 ? 14.840  31.731  35.383  1.00 34.07 ? 135 THR E CA  1 
ATOM   5422  C  C   . THR E  1 135 ? 14.700  33.106  36.038  1.00 37.07 ? 135 THR E C   1 
ATOM   5423  O  O   . THR E  1 135 ? 13.620  33.699  36.007  1.00 39.01 ? 135 THR E O   1 
ATOM   5424  C  CB  . THR E  1 135 ? 13.592  30.885  35.710  1.00 39.15 ? 135 THR E CB  1 
ATOM   5425  O  OG1 . THR E  1 135 ? 13.353  30.895  37.126  1.00 44.26 ? 135 THR E OG1 1 
ATOM   5426  C  CG2 . THR E  1 135 ? 13.798  29.456  35.246  1.00 47.28 ? 135 THR E CG2 1 
ATOM   5427  N  N   . LYS E  1 136 ? 15.780  33.609  36.634  1.00 34.04 ? 136 LYS E N   1 
ATOM   5428  C  CA  . LYS E  1 136 ? 15.748  34.906  37.318  1.00 30.16 ? 136 LYS E CA  1 
ATOM   5429  C  C   . LYS E  1 136 ? 16.840  35.867  36.858  1.00 31.57 ? 136 LYS E C   1 
ATOM   5430  O  O   . LYS E  1 136 ? 16.549  37.007  36.494  1.00 33.76 ? 136 LYS E O   1 
ATOM   5431  C  CB  . LYS E  1 136 ? 15.816  34.726  38.836  1.00 32.02 ? 136 LYS E CB  1 
ATOM   5432  C  CG  . LYS E  1 136 ? 14.492  34.296  39.456  1.00 34.11 ? 136 LYS E CG  1 
ATOM   5433  C  CD  . LYS E  1 136 ? 14.602  34.181  40.960  1.00 31.74 ? 136 LYS E CD  1 
ATOM   5434  C  CE  . LYS E  1 136 ? 13.334  33.628  41.533  1.00 28.51 ? 136 LYS E CE  1 
ATOM   5435  N  NZ  . LYS E  1 136 ? 12.152  34.477  41.215  1.00 28.22 ? 136 LYS E NZ  1 
ATOM   5436  N  N   . THR E  1 137 ? 18.090  35.411  36.869  1.00 30.17 ? 137 THR E N   1 
ATOM   5437  C  CA  . THR E  1 137 ? 19.211  36.259  36.476  1.00 32.10 ? 137 THR E CA  1 
ATOM   5438  C  C   . THR E  1 137 ? 20.078  35.657  35.377  1.00 31.66 ? 137 THR E C   1 
ATOM   5439  O  O   . THR E  1 137 ? 20.995  36.316  34.881  1.00 34.42 ? 137 THR E O   1 
ATOM   5440  C  CB  . THR E  1 137 ? 20.139  36.558  37.655  1.00 35.18 ? 137 THR E CB  1 
ATOM   5441  O  OG1 . THR E  1 137 ? 20.771  35.340  38.082  1.00 36.22 ? 137 THR E OG1 1 
ATOM   5442  C  CG2 . THR E  1 137 ? 19.365  37.202  38.808  1.00 30.74 ? 137 THR E CG2 1 
ATOM   5443  N  N   . GLY E  1 138 ? 19.800  34.409  35.012  1.00 31.19 ? 138 GLY E N   1 
ATOM   5444  C  CA  . GLY E  1 138 ? 20.571  33.731  33.985  1.00 36.66 ? 138 GLY E CA  1 
ATOM   5445  C  C   . GLY E  1 138 ? 22.013  33.442  34.382  1.00 37.60 ? 138 GLY E C   1 
ATOM   5446  O  O   . GLY E  1 138 ? 22.842  33.164  33.527  1.00 41.06 ? 138 GLY E O   1 
ATOM   5447  N  N   . ASN E  1 139 ? 22.315  33.542  35.675  1.00 34.46 ? 139 ASN E N   1 
ATOM   5448  C  CA  . ASN E  1 139 ? 23.603  33.108  36.235  1.00 34.88 ? 139 ASN E CA  1 
ATOM   5449  C  C   . ASN E  1 139 ? 24.857  33.695  35.591  1.00 41.28 ? 139 ASN E C   1 
ATOM   5450  O  O   . ASN E  1 139 ? 25.846  32.981  35.390  1.00 40.10 ? 139 ASN E O   1 
ATOM   5451  C  CB  . ASN E  1 139 ? 23.694  31.577  36.208  1.00 36.18 ? 139 ASN E CB  1 
ATOM   5452  C  CG  . ASN E  1 139 ? 22.823  30.926  37.255  1.00 29.51 ? 139 ASN E CG  1 
ATOM   5453  O  OD1 . ASN E  1 139 ? 22.922  31.249  38.435  1.00 38.03 ? 139 ASN E OD1 1 
ATOM   5454  N  ND2 . ASN E  1 139 ? 21.950  30.022  36.832  1.00 25.01 ? 139 ASN E ND2 1 
ATOM   5455  N  N   . ALA E  1 140 ? 24.838  34.990  35.293  1.00 41.40 ? 140 ALA E N   1 
ATOM   5456  C  CA  . ALA E  1 140 ? 25.949  35.608  34.568  1.00 40.39 ? 140 ALA E CA  1 
ATOM   5457  C  C   . ALA E  1 140 ? 27.084  36.136  35.453  1.00 44.86 ? 140 ALA E C   1 
ATOM   5458  O  O   . ALA E  1 140 ? 28.078  36.670  34.952  1.00 44.92 ? 140 ALA E O   1 
ATOM   5459  C  CB  . ALA E  1 140 ? 25.438  36.695  33.641  1.00 41.14 ? 140 ALA E CB  1 
ATOM   5460  N  N   . GLY E  1 141 ? 26.947  35.987  36.766  1.00 42.89 ? 141 GLY E N   1 
ATOM   5461  C  CA  . GLY E  1 141 ? 28.036  36.349  37.653  1.00 42.92 ? 141 GLY E CA  1 
ATOM   5462  C  C   . GLY E  1 141 ? 27.948  37.773  38.147  1.00 44.67 ? 141 GLY E C   1 
ATOM   5463  O  O   . GLY E  1 141 ? 26.902  38.423  38.029  1.00 41.58 ? 141 GLY E O   1 
ATOM   5464  N  N   . SER E  1 142 ? 29.054  38.258  38.700  1.00 43.22 ? 142 SER E N   1 
ATOM   5465  C  CA  . SER E  1 142 ? 29.097  39.593  39.273  1.00 47.34 ? 142 SER E CA  1 
ATOM   5466  C  C   . SER E  1 142 ? 28.941  40.673  38.208  1.00 52.19 ? 142 SER E C   1 
ATOM   5467  O  O   . SER E  1 142 ? 29.035  40.415  36.999  1.00 46.71 ? 142 SER E O   1 
ATOM   5468  C  CB  . SER E  1 142 ? 30.402  39.810  40.035  1.00 48.54 ? 142 SER E CB  1 
ATOM   5469  O  OG  . SER E  1 142 ? 31.518  39.660  39.174  1.00 53.94 ? 142 SER E OG  1 
ATOM   5470  N  N   . ARG E  1 143 ? 28.704  41.890  38.679  1.00 49.86 ? 143 ARG E N   1 
ATOM   5471  C  CA  . ARG E  1 143 ? 28.536  43.032  37.801  1.00 43.98 ? 143 ARG E CA  1 
ATOM   5472  C  C   . ARG E  1 143 ? 29.879  43.744  37.643  1.00 39.45 ? 143 ARG E C   1 
ATOM   5473  O  O   . ARG E  1 143 ? 30.390  44.343  38.590  1.00 42.17 ? 143 ARG E O   1 
ATOM   5474  C  CB  . ARG E  1 143 ? 27.449  43.942  38.373  1.00 38.30 ? 143 ARG E CB  1 
ATOM   5475  C  CG  . ARG E  1 143 ? 26.140  43.184  38.614  1.00 37.88 ? 143 ARG E CG  1 
ATOM   5476  C  CD  . ARG E  1 143 ? 25.040  44.053  39.194  1.00 38.20 ? 143 ARG E CD  1 
ATOM   5477  N  NE  . ARG E  1 143 ? 23.838  43.268  39.463  1.00 35.05 ? 143 ARG E NE  1 
ATOM   5478  C  CZ  . ARG E  1 143 ? 22.756  43.727  40.091  1.00 36.93 ? 143 ARG E CZ  1 
ATOM   5479  N  NH1 . ARG E  1 143 ? 22.695  44.989  40.519  1.00 35.48 ? 143 ARG E NH1 1 
ATOM   5480  N  NH2 . ARG E  1 143 ? 21.718  42.921  40.282  1.00 31.12 ? 143 ARG E NH2 1 
ATOM   5481  N  N   . LEU E  1 144 ? 30.453  43.655  36.447  1.00 42.04 ? 144 LEU E N   1 
ATOM   5482  C  CA  . LEU E  1 144 ? 31.812  44.150  36.208  1.00 46.83 ? 144 LEU E CA  1 
ATOM   5483  C  C   . LEU E  1 144 ? 31.885  45.670  36.049  1.00 43.15 ? 144 LEU E C   1 
ATOM   5484  O  O   . LEU E  1 144 ? 32.645  46.348  36.744  1.00 44.82 ? 144 LEU E O   1 
ATOM   5485  C  CB  . LEU E  1 144 ? 32.443  43.455  34.991  1.00 45.90 ? 144 LEU E CB  1 
ATOM   5486  C  CG  . LEU E  1 144 ? 32.722  41.950  35.084  1.00 46.56 ? 144 LEU E CG  1 
ATOM   5487  C  CD1 . LEU E  1 144 ? 33.542  41.470  33.903  1.00 45.58 ? 144 LEU E CD1 1 
ATOM   5488  C  CD2 . LEU E  1 144 ? 33.410  41.595  36.397  1.00 47.62 ? 144 LEU E CD2 1 
ATOM   5489  N  N   . ALA E  1 145 ? 31.111  46.193  35.111  1.00 43.19 ? 145 ALA E N   1 
ATOM   5490  C  CA  . ALA E  1 145 ? 30.985  47.631  34.948  1.00 47.68 ? 145 ALA E CA  1 
ATOM   5491  C  C   . ALA E  1 145 ? 29.525  47.961  34.691  1.00 45.83 ? 145 ALA E C   1 
ATOM   5492  O  O   . ALA E  1 145 ? 28.733  47.080  34.338  1.00 39.60 ? 145 ALA E O   1 
ATOM   5493  C  CB  . ALA E  1 145 ? 31.852  48.124  33.801  1.00 53.50 ? 145 ALA E CB  1 
ATOM   5494  N  N   . CYS E  1 146 ? 29.171  49.228  34.875  1.00 44.29 ? 146 CYS E N   1 
ATOM   5495  C  CA  . CYS E  1 146 ? 27.801  49.662  34.643  1.00 42.84 ? 146 CYS E CA  1 
ATOM   5496  C  C   . CYS E  1 146 ? 27.705  51.180  34.520  1.00 40.61 ? 146 CYS E C   1 
ATOM   5497  O  O   . CYS E  1 146 ? 28.610  51.910  34.930  1.00 42.79 ? 146 CYS E O   1 
ATOM   5498  C  CB  . CYS E  1 146 ? 26.901  49.195  35.778  1.00 38.77 ? 146 CYS E CB  1 
ATOM   5499  S  SG  . CYS E  1 146 ? 27.113  50.192  37.237  1.00 41.85 ? 146 CYS E SG  1 
ATOM   5500  N  N   . GLY E  1 147 ? 26.597  51.643  33.954  1.00 37.91 ? 147 GLY E N   1 
ATOM   5501  C  CA  . GLY E  1 147 ? 26.320  53.064  33.876  1.00 37.22 ? 147 GLY E CA  1 
ATOM   5502  C  C   . GLY E  1 147 ? 24.838  53.330  33.691  1.00 34.60 ? 147 GLY E C   1 
ATOM   5503  O  O   . GLY E  1 147 ? 24.099  52.457  33.223  1.00 32.18 ? 147 GLY E O   1 
ATOM   5504  N  N   . VAL E  1 148 ? 24.397  54.529  34.070  1.00 33.49 ? 148 VAL E N   1 
ATOM   5505  C  CA  . VAL E  1 148 ? 23.014  54.913  33.836  1.00 35.54 ? 148 VAL E CA  1 
ATOM   5506  C  C   . VAL E  1 148 ? 22.903  55.294  32.380  1.00 34.92 ? 148 VAL E C   1 
ATOM   5507  O  O   . VAL E  1 148 ? 23.834  55.874  31.821  1.00 35.62 ? 148 VAL E O   1 
ATOM   5508  C  CB  . VAL E  1 148 ? 22.582  56.118  34.705  1.00 33.50 ? 148 VAL E CB  1 
ATOM   5509  C  CG1 . VAL E  1 148 ? 21.106  56.429  34.482  1.00 30.84 ? 148 VAL E CG1 1 
ATOM   5510  C  CG2 . VAL E  1 148 ? 22.843  55.842  36.181  1.00 32.88 ? 148 VAL E CG2 1 
ATOM   5511  N  N   . ILE E  1 149 ? 21.783  54.964  31.751  1.00 34.80 ? 149 ILE E N   1 
ATOM   5512  C  CA  . ILE E  1 149 ? 21.589  55.391  30.376  1.00 39.09 ? 149 ILE E CA  1 
ATOM   5513  C  C   . ILE E  1 149 ? 20.889  56.748  30.298  1.00 45.12 ? 149 ILE E C   1 
ATOM   5514  O  O   . ILE E  1 149 ? 19.693  56.867  30.592  1.00 39.98 ? 149 ILE E O   1 
ATOM   5515  C  CB  . ILE E  1 149 ? 20.888  54.331  29.489  1.00 37.58 ? 149 ILE E CB  1 
ATOM   5516  C  CG1 . ILE E  1 149 ? 19.851  53.533  30.262  1.00 39.55 ? 149 ILE E CG1 1 
ATOM   5517  C  CG2 . ILE E  1 149 ? 21.901  53.343  28.979  1.00 48.57 ? 149 ILE E CG2 1 
ATOM   5518  C  CD1 . ILE E  1 149 ? 19.644  52.093  29.688  1.00 34.25 ? 149 ILE E CD1 1 
ATOM   5519  N  N   . GLY E  1 150 ? 21.666  57.761  29.912  1.00 42.15 ? 150 GLY E N   1 
ATOM   5520  C  CA  . GLY E  1 150 ? 21.170  59.112  29.720  1.00 43.31 ? 150 GLY E CA  1 
ATOM   5521  C  C   . GLY E  1 150 ? 20.881  59.469  28.267  1.00 47.80 ? 150 GLY E C   1 
ATOM   5522  O  O   . GLY E  1 150 ? 21.327  58.784  27.338  1.00 46.12 ? 150 GLY E O   1 
ATOM   5523  N  N   . ILE E  1 151 ? 20.125  60.544  28.063  1.00 43.44 ? 151 ILE E N   1 
ATOM   5524  C  CA  . ILE E  1 151 ? 19.724  60.938  26.718  1.00 44.02 ? 151 ILE E CA  1 
ATOM   5525  C  C   . ILE E  1 151 ? 20.891  61.589  26.006  1.00 42.28 ? 151 ILE E C   1 
ATOM   5526  O  O   . ILE E  1 151 ? 21.610  62.390  26.594  1.00 43.14 ? 151 ILE E O   1 
ATOM   5527  C  CB  . ILE E  1 151 ? 18.528  61.892  26.748  1.00 43.86 ? 151 ILE E CB  1 
ATOM   5528  C  CG1 . ILE E  1 151 ? 17.362  61.230  27.484  1.00 38.05 ? 151 ILE E CG1 1 
ATOM   5529  C  CG2 . ILE E  1 151 ? 18.110  62.267  25.335  1.00 44.54 ? 151 ILE E CG2 1 
ATOM   5530  C  CD1 . ILE E  1 151 ? 16.215  62.178  27.785  1.00 37.20 ? 151 ILE E CD1 1 
ATOM   5531  N  N   . ALA E  1 152 ? 21.106  61.207  24.751  1.00 48.54 ? 152 ALA E N   1 
ATOM   5532  C  CA  . ALA E  1 152 ? 22.165  61.804  23.943  1.00 46.98 ? 152 ALA E CA  1 
ATOM   5533  C  C   . ALA E  1 152 ? 21.564  62.598  22.781  1.00 41.45 ? 152 ALA E C   1 
ATOM   5534  O  O   . ALA E  1 152 ? 20.412  62.378  22.376  1.00 39.08 ? 152 ALA E O   1 
ATOM   5535  C  CB  . ALA E  1 152 ? 23.134  60.735  23.433  1.00 44.70 ? 152 ALA E CB  1 
ATOM   5536  N  N   . GLN E  1 153 ? 22.348  63.527  22.252  1.00 39.93 ? 153 GLN E N   1 
ATOM   5537  C  CA  . GLN E  1 153 ? 21.867  64.392  21.172  1.00 48.10 ? 153 GLN E CA  1 
ATOM   5538  C  C   . GLN E  1 153 ? 21.578  63.609  19.885  1.00 47.63 ? 153 GLN E C   1 
ATOM   5539  O  O   . GLN E  1 153 ? 22.393  62.789  19.432  1.00 44.43 ? 153 GLN E O   1 
ATOM   5540  C  CB  . GLN E  1 153 ? 22.852  65.549  20.942  1.00 52.92 ? 153 GLN E CB  1 
ATOM   5541  C  CG  . GLN E  1 153 ? 23.661  65.520  19.648  1.00 54.39 ? 153 GLN E CG  1 
ATOM   5542  C  CD  . GLN E  1 153 ? 24.597  66.713  19.530  1.00 56.02 ? 153 GLN E CD  1 
ATOM   5543  O  OE1 . GLN E  1 153 ? 24.433  67.716  20.232  1.00 52.93 ? 153 GLN E OE1 1 
ATOM   5544  N  NE2 . GLN E  1 153 ? 25.582  66.609  18.639  1.00 55.29 ? 153 GLN E NE2 1 
ATOM   5545  O  OXT . GLN E  1 153 ? 20.498  63.758  19.301  1.00 40.53 ? 153 GLN E OXT 1 
ATOM   5546  N  N   . ALA F  1 1   ? 4.476   57.247  44.266  1.00 50.88 ? 1   ALA F N   1 
ATOM   5547  C  CA  . ALA F  1 1   ? 5.419   58.330  43.993  1.00 41.73 ? 1   ALA F CA  1 
ATOM   5548  C  C   . ALA F  1 1   ? 6.646   57.865  43.192  1.00 35.11 ? 1   ALA F C   1 
ATOM   5549  O  O   . ALA F  1 1   ? 7.300   56.877  43.536  1.00 37.52 ? 1   ALA F O   1 
ATOM   5550  C  CB  . ALA F  1 1   ? 5.849   59.006  45.302  1.00 35.23 ? 1   ALA F CB  1 
ATOM   5551  N  N   . THR F  1 2   ? 6.950   58.581  42.119  1.00 30.84 ? 2   THR F N   1 
ATOM   5552  C  CA  . THR F  1 2   ? 8.179   58.326  41.384  1.00 30.39 ? 2   THR F CA  1 
ATOM   5553  C  C   . THR F  1 2   ? 9.332   58.950  42.150  1.00 26.23 ? 2   THR F C   1 
ATOM   5554  O  O   . THR F  1 2   ? 9.187   59.971  42.834  1.00 24.18 ? 2   THR F O   1 
ATOM   5555  C  CB  . THR F  1 2   ? 8.119   58.893  39.945  1.00 30.00 ? 2   THR F CB  1 
ATOM   5556  O  OG1 . THR F  1 2   ? 6.889   58.491  39.336  1.00 35.19 ? 2   THR F OG1 1 
ATOM   5557  C  CG2 . THR F  1 2   ? 9.284   58.387  39.088  1.00 29.88 ? 2   THR F CG2 1 
ATOM   5558  N  N   . LYS F  1 3   ? 10.484  58.321  42.040  1.00 20.25 ? 3   LYS F N   1 
ATOM   5559  C  CA  . LYS F  1 3   ? 11.643  58.780  42.743  1.00 21.79 ? 3   LYS F CA  1 
ATOM   5560  C  C   . LYS F  1 3   ? 12.797  58.691  41.788  1.00 20.59 ? 3   LYS F C   1 
ATOM   5561  O  O   . LYS F  1 3   ? 12.755  57.917  40.845  1.00 15.38 ? 3   LYS F O   1 
ATOM   5562  C  CB  . LYS F  1 3   ? 11.914  57.882  43.948  1.00 25.86 ? 3   LYS F CB  1 
ATOM   5563  C  CG  . LYS F  1 3   ? 10.763  57.819  44.960  1.00 31.06 ? 3   LYS F CG  1 
ATOM   5564  C  CD  . LYS F  1 3   ? 11.202  57.163  46.266  1.00 36.05 ? 3   LYS F CD  1 
ATOM   5565  C  CE  . LYS F  1 3   ? 10.349  55.947  46.589  1.00 44.86 ? 3   LYS F CE  1 
ATOM   5566  N  NZ  . LYS F  1 3   ? 10.780  55.327  47.880  1.00 47.18 ? 3   LYS F NZ  1 
ATOM   5567  N  N   . ALA F  1 4   ? 13.848  59.455  42.054  1.00 20.76 ? 4   ALA F N   1 
ATOM   5568  C  CA  . ALA F  1 4   ? 14.987  59.446  41.162  1.00 18.93 ? 4   ALA F CA  1 
ATOM   5569  C  C   . ALA F  1 4   ? 16.232  59.782  41.943  1.00 20.34 ? 4   ALA F C   1 
ATOM   5570  O  O   . ALA F  1 4   ? 16.155  60.289  43.069  1.00 19.13 ? 4   ALA F O   1 
ATOM   5571  C  CB  . ALA F  1 4   ? 14.758  60.441  40.028  1.00 20.73 ? 4   ALA F CB  1 
ATOM   5572  N  N   . VAL F  1 5   ? 17.387  59.482  41.366  1.00 21.40 ? 5   VAL F N   1 
ATOM   5573  C  CA  . VAL F  1 5   ? 18.639  59.708  42.076  1.00 20.86 ? 5   VAL F CA  1 
ATOM   5574  C  C   . VAL F  1 5   ? 19.748  60.054  41.095  1.00 20.26 ? 5   VAL F C   1 
ATOM   5575  O  O   . VAL F  1 5   ? 19.698  59.684  39.920  1.00 22.05 ? 5   VAL F O   1 
ATOM   5576  C  CB  . VAL F  1 5   ? 19.030  58.471  42.960  1.00 24.18 ? 5   VAL F CB  1 
ATOM   5577  C  CG1 . VAL F  1 5   ? 19.524  57.308  42.103  1.00 23.59 ? 5   VAL F CG1 1 
ATOM   5578  C  CG2 . VAL F  1 5   ? 20.078  58.843  43.984  1.00 17.88 ? 5   VAL F CG2 1 
ATOM   5579  N  N   . CYS F  1 6   ? 20.746  60.784  41.570  1.00 22.18 ? 6   CYS F N   1 
ATOM   5580  C  CA  . CYS F  1 6   ? 21.904  61.040  40.738  1.00 25.28 ? 6   CYS F CA  1 
ATOM   5581  C  C   . CYS F  1 6   ? 23.153  61.192  41.590  1.00 24.82 ? 6   CYS F C   1 
ATOM   5582  O  O   . CYS F  1 6   ? 23.137  61.848  42.639  1.00 24.51 ? 6   CYS F O   1 
ATOM   5583  C  CB  . CYS F  1 6   ? 21.663  62.260  39.825  1.00 32.34 ? 6   CYS F CB  1 
ATOM   5584  S  SG  . CYS F  1 6   ? 23.154  63.110  39.233  1.00 28.51 ? 6   CYS F SG  1 
ATOM   5585  N  N   . VAL F  1 7   ? 24.225  60.551  41.140  1.00 20.91 ? 7   VAL F N   1 
ATOM   5586  C  CA  . VAL F  1 7   ? 25.506  60.617  41.814  1.00 27.87 ? 7   VAL F CA  1 
ATOM   5587  C  C   . VAL F  1 7   ? 26.349  61.641  41.081  1.00 26.15 ? 7   VAL F C   1 
ATOM   5588  O  O   . VAL F  1 7   ? 26.574  61.521  39.890  1.00 27.96 ? 7   VAL F O   1 
ATOM   5589  C  CB  . VAL F  1 7   ? 26.233  59.246  41.794  1.00 29.11 ? 7   VAL F CB  1 
ATOM   5590  C  CG1 . VAL F  1 7   ? 27.474  59.289  42.680  1.00 26.71 ? 7   VAL F CG1 1 
ATOM   5591  C  CG2 . VAL F  1 7   ? 25.294  58.146  42.248  1.00 28.90 ? 7   VAL F CG2 1 
ATOM   5592  N  N   . LEU F  1 8   ? 26.799  62.656  41.801  1.00 28.13 ? 8   LEU F N   1 
ATOM   5593  C  CA  . LEU F  1 8   ? 27.592  63.709  41.206  1.00 28.80 ? 8   LEU F CA  1 
ATOM   5594  C  C   . LEU F  1 8   ? 29.067  63.424  41.423  1.00 36.59 ? 8   LEU F C   1 
ATOM   5595  O  O   . LEU F  1 8   ? 29.504  63.157  42.547  1.00 36.20 ? 8   LEU F O   1 
ATOM   5596  C  CB  . LEU F  1 8   ? 27.234  65.056  41.824  1.00 30.20 ? 8   LEU F CB  1 
ATOM   5597  C  CG  . LEU F  1 8   ? 25.785  65.530  41.662  1.00 28.82 ? 8   LEU F CG  1 
ATOM   5598  C  CD1 . LEU F  1 8   ? 25.554  66.729  42.563  1.00 27.08 ? 8   LEU F CD1 1 
ATOM   5599  C  CD2 . LEU F  1 8   ? 25.478  65.897  40.220  1.00 28.60 ? 8   LEU F CD2 1 
ATOM   5600  N  N   . LYS F  1 9   ? 29.826  63.497  40.334  1.00 39.73 ? 9   LYS F N   1 
ATOM   5601  C  CA  . LYS F  1 9   ? 31.269  63.293  40.360  1.00 42.27 ? 9   LYS F CA  1 
ATOM   5602  C  C   . LYS F  1 9   ? 31.871  63.889  39.100  1.00 43.10 ? 9   LYS F C   1 
ATOM   5603  O  O   . LYS F  1 9   ? 31.234  63.906  38.037  1.00 44.22 ? 9   LYS F O   1 
ATOM   5604  C  CB  . LYS F  1 9   ? 31.583  61.803  40.399  1.00 40.17 ? 9   LYS F CB  1 
ATOM   5605  C  CG  . LYS F  1 9   ? 30.752  61.014  39.401  1.00 41.17 ? 9   LYS F CG  1 
ATOM   5606  C  CD  . LYS F  1 9   ? 30.345  59.680  39.987  1.00 40.93 ? 9   LYS F CD  1 
ATOM   5607  C  CE  . LYS F  1 9   ? 29.009  59.224  39.448  1.00 34.54 ? 9   LYS F CE  1 
ATOM   5608  N  NZ  . LYS F  1 9   ? 28.784  57.796  39.830  1.00 44.77 ? 9   LYS F NZ  1 
ATOM   5609  N  N   . GLY F  1 10  ? 33.098  64.375  39.215  1.00 39.85 ? 10  GLY F N   1 
ATOM   5610  C  CA  . GLY F  1 10  ? 33.812  64.855  38.048  1.00 54.19 ? 10  GLY F CA  1 
ATOM   5611  C  C   . GLY F  1 10  ? 35.211  64.281  37.981  1.00 55.24 ? 10  GLY F C   1 
ATOM   5612  O  O   . GLY F  1 10  ? 35.412  63.133  37.582  1.00 53.24 ? 10  GLY F O   1 
ATOM   5613  N  N   . ASP F  1 11  ? 36.178  65.103  38.371  1.00 57.46 ? 11  ASP F N   1 
ATOM   5614  C  CA  . ASP F  1 11  ? 37.560  64.678  38.517  1.00 55.01 ? 11  ASP F CA  1 
ATOM   5615  C  C   . ASP F  1 11  ? 38.268  65.596  39.501  1.00 51.65 ? 11  ASP F C   1 
ATOM   5616  O  O   . ASP F  1 11  ? 39.488  65.573  39.624  1.00 58.20 ? 11  ASP F O   1 
ATOM   5617  C  CB  . ASP F  1 11  ? 38.292  64.611  37.167  1.00 56.48 ? 11  ASP F CB  1 
ATOM   5618  C  CG  . ASP F  1 11  ? 37.840  65.687  36.186  1.00 60.04 ? 11  ASP F CG  1 
ATOM   5619  O  OD1 . ASP F  1 11  ? 38.412  66.800  36.213  1.00 58.70 ? 11  ASP F OD1 1 
ATOM   5620  O  OD2 . ASP F  1 11  ? 36.927  65.408  35.372  1.00 59.44 ? 11  ASP F OD2 1 
ATOM   5621  N  N   . GLY F  1 12  ? 37.485  66.408  40.200  1.00 43.13 ? 12  GLY F N   1 
ATOM   5622  C  CA  . GLY F  1 12  ? 37.984  67.187  41.316  1.00 32.25 ? 12  GLY F CA  1 
ATOM   5623  C  C   . GLY F  1 12  ? 37.394  66.544  42.551  1.00 35.93 ? 12  GLY F C   1 
ATOM   5624  O  O   . GLY F  1 12  ? 36.777  65.498  42.441  1.00 41.77 ? 12  GLY F O   1 
ATOM   5625  N  N   . PRO F  1 13  ? 37.562  67.163  43.727  1.00 34.91 ? 13  PRO F N   1 
ATOM   5626  C  CA  . PRO F  1 13  ? 37.050  66.582  44.963  1.00 30.04 ? 13  PRO F CA  1 
ATOM   5627  C  C   . PRO F  1 13  ? 35.567  66.858  45.156  1.00 39.70 ? 13  PRO F C   1 
ATOM   5628  O  O   . PRO F  1 13  ? 35.100  66.756  46.291  1.00 37.12 ? 13  PRO F O   1 
ATOM   5629  C  CB  . PRO F  1 13  ? 37.801  67.369  46.029  1.00 34.54 ? 13  PRO F CB  1 
ATOM   5630  C  CG  . PRO F  1 13  ? 37.880  68.718  45.447  1.00 37.06 ? 13  PRO F CG  1 
ATOM   5631  C  CD  . PRO F  1 13  ? 38.151  68.487  43.969  1.00 35.60 ? 13  PRO F CD  1 
ATOM   5632  N  N   . VAL F  1 14  ? 34.838  67.222  44.103  1.00 39.58 ? 14  VAL F N   1 
ATOM   5633  C  CA  . VAL F  1 14  ? 33.417  67.499  44.285  1.00 38.72 ? 14  VAL F CA  1 
ATOM   5634  C  C   . VAL F  1 14  ? 32.573  66.268  43.989  1.00 35.45 ? 14  VAL F C   1 
ATOM   5635  O  O   . VAL F  1 14  ? 32.536  65.765  42.862  1.00 35.20 ? 14  VAL F O   1 
ATOM   5636  C  CB  . VAL F  1 14  ? 32.912  68.720  43.465  1.00 37.97 ? 14  VAL F CB  1 
ATOM   5637  C  CG1 . VAL F  1 14  ? 31.425  68.927  43.716  1.00 29.07 ? 14  VAL F CG1 1 
ATOM   5638  C  CG2 . VAL F  1 14  ? 33.685  69.978  43.842  1.00 31.24 ? 14  VAL F CG2 1 
ATOM   5639  N  N   . GLN F  1 15  ? 31.882  65.788  45.013  1.00 35.38 ? 15  GLN F N   1 
ATOM   5640  C  CA  . GLN F  1 15  ? 31.091  64.579  44.858  1.00 36.86 ? 15  GLN F CA  1 
ATOM   5641  C  C   . GLN F  1 15  ? 29.860  64.623  45.737  1.00 27.06 ? 15  GLN F C   1 
ATOM   5642  O  O   . GLN F  1 15  ? 29.868  65.199  46.823  1.00 29.01 ? 15  GLN F O   1 
ATOM   5643  C  CB  . GLN F  1 15  ? 31.936  63.356  45.212  1.00 39.23 ? 15  GLN F CB  1 
ATOM   5644  C  CG  . GLN F  1 15  ? 32.696  63.507  46.527  1.00 40.18 ? 15  GLN F CG  1 
ATOM   5645  C  CD  . GLN F  1 15  ? 33.653  62.344  46.803  1.00 46.49 ? 15  GLN F CD  1 
ATOM   5646  O  OE1 . GLN F  1 15  ? 33.234  61.270  47.233  1.00 43.98 ? 15  GLN F OE1 1 
ATOM   5647  N  NE2 . GLN F  1 15  ? 34.942  62.563  46.560  1.00 43.93 ? 15  GLN F NE2 1 
ATOM   5648  N  N   . GLY F  1 16  ? 28.797  63.998  45.272  1.00 24.96 ? 16  GLY F N   1 
ATOM   5649  C  CA  . GLY F  1 16  ? 27.618  63.930  46.089  1.00 25.01 ? 16  GLY F CA  1 
ATOM   5650  C  C   . GLY F  1 16  ? 26.536  63.076  45.508  1.00 23.84 ? 16  GLY F C   1 
ATOM   5651  O  O   . GLY F  1 16  ? 26.669  62.520  44.416  1.00 24.43 ? 16  GLY F O   1 
ATOM   5652  N  N   . ILE F  1 17  ? 25.449  62.985  46.262  1.00 22.45 ? 17  ILE F N   1 
ATOM   5653  C  CA  . ILE F  1 17  ? 24.293  62.212  45.846  1.00 22.81 ? 17  ILE F CA  1 
ATOM   5654  C  C   . ILE F  1 17  ? 23.068  63.110  45.988  1.00 21.86 ? 17  ILE F C   1 
ATOM   5655  O  O   . ILE F  1 17  ? 22.894  63.776  47.007  1.00 19.01 ? 17  ILE F O   1 
ATOM   5656  C  CB  . ILE F  1 17  ? 24.125  60.937  46.710  1.00 24.32 ? 17  ILE F CB  1 
ATOM   5657  C  CG1 . ILE F  1 17  ? 25.332  60.006  46.539  1.00 26.94 ? 17  ILE F CG1 1 
ATOM   5658  C  CG2 . ILE F  1 17  ? 22.835  60.210  46.350  1.00 19.31 ? 17  ILE F CG2 1 
ATOM   5659  C  CD1 . ILE F  1 17  ? 25.257  58.718  47.366  1.00 25.33 ? 17  ILE F CD1 1 
ATOM   5660  N  N   . ILE F  1 18  ? 22.234  63.154  44.958  1.00 19.84 ? 18  ILE F N   1 
ATOM   5661  C  CA  . ILE F  1 18  ? 21.046  63.998  45.021  1.00 22.40 ? 18  ILE F CA  1 
ATOM   5662  C  C   . ILE F  1 18  ? 19.809  63.150  44.773  1.00 17.95 ? 18  ILE F C   1 
ATOM   5663  O  O   . ILE F  1 18  ? 19.773  62.350  43.844  1.00 17.92 ? 18  ILE F O   1 
ATOM   5664  C  CB  . ILE F  1 18  ? 21.112  65.172  44.012  1.00 18.92 ? 18  ILE F CB  1 
ATOM   5665  C  CG1 . ILE F  1 18  ? 22.329  66.053  44.296  1.00 18.36 ? 18  ILE F CG1 1 
ATOM   5666  C  CG2 . ILE F  1 18  ? 19.863  66.018  44.082  1.00 18.45 ? 18  ILE F CG2 1 
ATOM   5667  C  CD1 . ILE F  1 18  ? 22.272  66.798  45.569  1.00 19.33 ? 18  ILE F CD1 1 
ATOM   5668  N  N   . ASN F  1 19  ? 18.806  63.325  45.625  1.00 13.74 ? 19  ASN F N   1 
ATOM   5669  C  CA  . ASN F  1 19  ? 17.568  62.574  45.507  1.00 17.32 ? 19  ASN F CA  1 
ATOM   5670  C  C   . ASN F  1 19  ? 16.425  63.440  44.987  1.00 17.24 ? 19  ASN F C   1 
ATOM   5671  O  O   . ASN F  1 19  ? 16.373  64.650  45.243  1.00 17.05 ? 19  ASN F O   1 
ATOM   5672  C  CB  . ASN F  1 19  ? 17.183  61.981  46.867  1.00 18.85 ? 19  ASN F CB  1 
ATOM   5673  C  CG  . ASN F  1 19  ? 18.323  61.215  47.507  1.00 17.94 ? 19  ASN F CG  1 
ATOM   5674  O  OD1 . ASN F  1 19  ? 18.649  60.114  47.086  1.00 20.31 ? 19  ASN F OD1 1 
ATOM   5675  N  ND2 . ASN F  1 19  ? 18.939  61.801  48.513  1.00 19.16 ? 19  ASN F ND2 1 
ATOM   5676  N  N   . PHE F  1 20  ? 15.495  62.801  44.293  1.00 17.01 ? 20  PHE F N   1 
ATOM   5677  C  CA  . PHE F  1 20  ? 14.352  63.472  43.714  1.00 16.61 ? 20  PHE F CA  1 
ATOM   5678  C  C   . PHE F  1 20  ? 13.118  62.653  44.068  1.00 19.41 ? 20  PHE F C   1 
ATOM   5679  O  O   . PHE F  1 20  ? 13.120  61.433  43.920  1.00 18.28 ? 20  PHE F O   1 
ATOM   5680  C  CB  . PHE F  1 20  ? 14.480  63.495  42.192  1.00 17.79 ? 20  PHE F CB  1 
ATOM   5681  C  CG  . PHE F  1 20  ? 15.667  64.261  41.669  1.00 17.59 ? 20  PHE F CG  1 
ATOM   5682  C  CD1 . PHE F  1 20  ? 16.898  63.647  41.525  1.00 18.65 ? 20  PHE F CD1 1 
ATOM   5683  C  CD2 . PHE F  1 20  ? 15.527  65.573  41.245  1.00 18.37 ? 20  PHE F CD2 1 
ATOM   5684  C  CE1 . PHE F  1 20  ? 17.986  64.345  41.002  1.00 21.64 ? 20  PHE F CE1 1 
ATOM   5685  C  CE2 . PHE F  1 20  ? 16.595  66.271  40.720  1.00 21.58 ? 20  PHE F CE2 1 
ATOM   5686  C  CZ  . PHE F  1 20  ? 17.837  65.657  40.602  1.00 19.96 ? 20  PHE F CZ  1 
ATOM   5687  N  N   . GLU F  1 21  ? 12.063  63.316  44.524  1.00 18.84 ? 21  GLU F N   1 
ATOM   5688  C  CA  . GLU F  1 21  ? 10.775  62.644  44.706  1.00 20.19 ? 21  GLU F CA  1 
ATOM   5689  C  C   . GLU F  1 21  ? 9.601   63.503  44.270  1.00 19.88 ? 21  GLU F C   1 
ATOM   5690  O  O   . GLU F  1 21  ? 9.561   64.702  44.535  1.00 19.64 ? 21  GLU F O   1 
ATOM   5691  C  CB  . GLU F  1 21  ? 10.570  62.193  46.157  1.00 22.56 ? 21  GLU F CB  1 
ATOM   5692  C  CG  . GLU F  1 21  ? 9.332   61.309  46.349  1.00 29.32 ? 21  GLU F CG  1 
ATOM   5693  C  CD  . GLU F  1 21  ? 9.138   60.862  47.792  1.00 33.34 ? 21  GLU F CD  1 
ATOM   5694  O  OE1 . GLU F  1 21  ? 8.050   60.347  48.122  1.00 42.00 ? 21  GLU F OE1 1 
ATOM   5695  O  OE2 . GLU F  1 21  ? 10.076  61.026  48.593  1.00 27.52 ? 21  GLU F OE2 1 
ATOM   5696  N  N   . GLN F  1 22  ? 8.645   62.867  43.604  1.00 25.30 ? 22  GLN F N   1 
ATOM   5697  C  CA  . GLN F  1 22  ? 7.453   63.529  43.117  1.00 26.91 ? 22  GLN F CA  1 
ATOM   5698  C  C   . GLN F  1 22  ? 6.267   62.686  43.552  1.00 27.74 ? 22  GLN F C   1 
ATOM   5699  O  O   . GLN F  1 22  ? 5.976   61.663  42.952  1.00 30.43 ? 22  GLN F O   1 
ATOM   5700  C  CB  . GLN F  1 22  ? 7.505   63.645  41.587  1.00 24.89 ? 22  GLN F CB  1 
ATOM   5701  C  CG  . GLN F  1 22  ? 6.428   64.543  40.976  1.00 28.52 ? 22  GLN F CG  1 
ATOM   5702  C  CD  . GLN F  1 22  ? 6.740   64.912  39.523  1.00 27.45 ? 22  GLN F CD  1 
ATOM   5703  O  OE1 . GLN F  1 22  ? 7.421   64.171  38.808  1.00 24.25 ? 22  GLN F OE1 1 
ATOM   5704  N  NE2 . GLN F  1 22  ? 6.252   66.069  39.089  1.00 27.36 ? 22  GLN F NE2 1 
ATOM   5705  N  N   . LYS F  1 23  ? 5.597   63.110  44.617  1.00 32.18 ? 23  LYS F N   1 
ATOM   5706  C  CA  . LYS F  1 23  ? 4.530   62.311  45.207  1.00 37.99 ? 23  LYS F CA  1 
ATOM   5707  C  C   . LYS F  1 23  ? 3.379   62.146  44.231  1.00 38.48 ? 23  LYS F C   1 
ATOM   5708  O  O   . LYS F  1 23  ? 2.847   61.052  44.056  1.00 42.40 ? 23  LYS F O   1 
ATOM   5709  C  CB  . LYS F  1 23  ? 4.046   62.921  46.533  1.00 40.43 ? 23  LYS F CB  1 
ATOM   5710  C  CG  . LYS F  1 23  ? 4.879   62.493  47.756  1.00 47.63 ? 23  LYS F CG  1 
ATOM   5711  C  CD  . LYS F  1 23  ? 4.359   63.108  49.062  1.00 55.48 ? 23  LYS F CD  1 
ATOM   5712  C  CE  . LYS F  1 23  ? 5.212   62.693  50.267  1.00 58.45 ? 23  LYS F CE  1 
ATOM   5713  N  NZ  . LYS F  1 23  ? 4.881   63.478  51.496  1.00 56.44 ? 23  LYS F NZ  1 
ATOM   5714  N  N   . GLU F  1 24  ? 3.019   63.241  43.581  1.00 33.77 ? 24  GLU F N   1 
ATOM   5715  C  CA  . GLU F  1 24  ? 1.923   63.235  42.633  1.00 36.64 ? 24  GLU F CA  1 
ATOM   5716  C  C   . GLU F  1 24  ? 2.378   63.745  41.286  1.00 34.86 ? 24  GLU F C   1 
ATOM   5717  O  O   . GLU F  1 24  ? 3.219   64.648  41.195  1.00 29.68 ? 24  GLU F O   1 
ATOM   5718  C  CB  . GLU F  1 24  ? 0.766   64.072  43.160  1.00 37.10 ? 24  GLU F CB  1 
ATOM   5719  C  CG  . GLU F  1 24  ? 0.070   63.407  44.318  1.00 42.76 ? 24  GLU F CG  1 
ATOM   5720  C  CD  . GLU F  1 24  ? -1.115  64.198  44.833  1.00 58.98 ? 24  GLU F CD  1 
ATOM   5721  O  OE1 . GLU F  1 24  ? -1.640  65.063  44.088  1.00 59.26 ? 24  GLU F OE1 1 
ATOM   5722  O  OE2 . GLU F  1 24  ? -1.516  63.948  45.991  1.00 54.64 ? 24  GLU F OE2 1 
ATOM   5723  N  N   . SER F  1 25  ? 1.839   63.137  40.237  1.00 33.62 ? 25  SER F N   1 
ATOM   5724  C  CA  . SER F  1 25  ? 2.203   63.516  38.886  1.00 37.45 ? 25  SER F CA  1 
ATOM   5725  C  C   . SER F  1 25  ? 1.801   64.972  38.690  1.00 40.48 ? 25  SER F C   1 
ATOM   5726  O  O   . SER F  1 25  ? 0.675   65.366  39.021  1.00 39.94 ? 25  SER F O   1 
ATOM   5727  C  CB  . SER F  1 25  ? 1.499   62.609  37.877  1.00 42.23 ? 25  SER F CB  1 
ATOM   5728  O  OG  . SER F  1 25  ? 1.679   63.085  36.560  1.00 41.74 ? 25  SER F OG  1 
ATOM   5729  N  N   . ASN F  1 26  ? 2.735   65.771  38.181  1.00 40.16 ? 26  ASN F N   1 
ATOM   5730  C  CA  . ASN F  1 26  ? 2.520   67.204  38.043  1.00 44.67 ? 26  ASN F CA  1 
ATOM   5731  C  C   . ASN F  1 26  ? 2.220   67.859  39.402  1.00 46.25 ? 26  ASN F C   1 
ATOM   5732  O  O   . ASN F  1 26  ? 1.380   68.760  39.523  1.00 48.94 ? 26  ASN F O   1 
ATOM   5733  C  CB  . ASN F  1 26  ? 1.409   67.476  37.023  1.00 47.95 ? 26  ASN F CB  1 
ATOM   5734  C  CG  . ASN F  1 26  ? 1.339   66.402  35.936  1.00 51.09 ? 26  ASN F CG  1 
ATOM   5735  O  OD1 . ASN F  1 26  ? 0.393   65.599  35.905  1.00 47.91 ? 26  ASN F OD1 1 
ATOM   5736  N  ND2 . ASN F  1 26  ? 2.341   66.380  35.042  1.00 48.59 ? 26  ASN F ND2 1 
ATOM   5737  N  N   . GLY F  1 27  ? 2.890   67.357  40.434  1.00 35.96 ? 27  GLY F N   1 
ATOM   5738  C  CA  . GLY F  1 27  ? 2.994   68.061  41.696  1.00 29.51 ? 27  GLY F CA  1 
ATOM   5739  C  C   . GLY F  1 27  ? 4.467   68.421  41.767  1.00 23.84 ? 27  GLY F C   1 
ATOM   5740  O  O   . GLY F  1 27  ? 5.227   68.039  40.879  1.00 26.20 ? 27  GLY F O   1 
ATOM   5741  N  N   . PRO F  1 28  ? 4.877   69.159  42.802  1.00 23.07 ? 28  PRO F N   1 
ATOM   5742  C  CA  . PRO F  1 28  ? 6.275   69.585  42.940  1.00 23.94 ? 28  PRO F CA  1 
ATOM   5743  C  C   . PRO F  1 28  ? 7.248   68.401  43.001  1.00 21.60 ? 28  PRO F C   1 
ATOM   5744  O  O   . PRO F  1 28  ? 6.864   67.276  43.331  1.00 23.20 ? 28  PRO F O   1 
ATOM   5745  C  CB  . PRO F  1 28  ? 6.284   70.326  44.292  1.00 21.00 ? 28  PRO F CB  1 
ATOM   5746  C  CG  . PRO F  1 28  ? 4.866   70.700  44.532  1.00 26.10 ? 28  PRO F CG  1 
ATOM   5747  C  CD  . PRO F  1 28  ? 4.060   69.576  43.952  1.00 21.08 ? 28  PRO F CD  1 
ATOM   5748  N  N   . VAL F  1 29  ? 8.511   68.665  42.703  1.00 17.70 ? 29  VAL F N   1 
ATOM   5749  C  CA  . VAL F  1 29  ? 9.545   67.662  42.867  1.00 17.56 ? 29  VAL F CA  1 
ATOM   5750  C  C   . VAL F  1 29  ? 10.468  68.094  44.020  1.00 15.32 ? 29  VAL F C   1 
ATOM   5751  O  O   . VAL F  1 29  ? 11.022  69.180  44.014  1.00 12.42 ? 29  VAL F O   1 
ATOM   5752  C  CB  . VAL F  1 29  ? 10.372  67.473  41.587  1.00 14.52 ? 29  VAL F CB  1 
ATOM   5753  C  CG1 . VAL F  1 29  ? 11.436  66.428  41.811  1.00 17.75 ? 29  VAL F CG1 1 
ATOM   5754  C  CG2 . VAL F  1 29  ? 9.479   67.069  40.411  1.00 20.05 ? 29  VAL F CG2 1 
ATOM   5755  N  N   . LYS F  1 30  ? 10.611  67.253  45.026  1.00 16.70 ? 30  LYS F N   1 
ATOM   5756  C  CA  . LYS F  1 30  ? 11.533  67.585  46.109  1.00 15.52 ? 30  LYS F CA  1 
ATOM   5757  C  C   . LYS F  1 30  ? 12.911  67.090  45.707  1.00 13.57 ? 30  LYS F C   1 
ATOM   5758  O  O   . LYS F  1 30  ? 13.045  66.010  45.150  1.00 11.77 ? 30  LYS F O   1 
ATOM   5759  C  CB  . LYS F  1 30  ? 11.086  66.960  47.411  1.00 15.47 ? 30  LYS F CB  1 
ATOM   5760  C  CG  . LYS F  1 30  ? 9.906   67.680  48.052  1.00 21.75 ? 30  LYS F CG  1 
ATOM   5761  C  CD  . LYS F  1 30  ? 8.887   66.673  48.541  1.00 28.65 ? 30  LYS F CD  1 
ATOM   5762  C  CE  . LYS F  1 30  ? 7.789   67.313  49.374  1.00 33.04 ? 30  LYS F CE  1 
ATOM   5763  N  NZ  . LYS F  1 30  ? 8.326   67.833  50.656  1.00 36.36 ? 30  LYS F NZ  1 
ATOM   5764  N  N   . VAL F  1 31  ? 13.917  67.917  45.953  1.00 11.75 ? 31  VAL F N   1 
ATOM   5765  C  CA  . VAL F  1 31  ? 15.281  67.639  45.537  1.00 14.80 ? 31  VAL F CA  1 
ATOM   5766  C  C   . VAL F  1 31  ? 16.174  67.855  46.751  1.00 16.16 ? 31  VAL F C   1 
ATOM   5767  O  O   . VAL F  1 31  ? 16.184  68.947  47.330  1.00 17.71 ? 31  VAL F O   1 
ATOM   5768  C  CB  . VAL F  1 31  ? 15.702  68.599  44.399  1.00 16.75 ? 31  VAL F CB  1 
ATOM   5769  C  CG1 . VAL F  1 31  ? 17.098  68.297  43.940  1.00 10.62 ? 31  VAL F CG1 1 
ATOM   5770  C  CG2 . VAL F  1 31  ? 14.680  68.530  43.238  1.00 10.16 ? 31  VAL F CG2 1 
ATOM   5771  N  N   . TRP F  1 32  ? 16.907  66.821  47.151  1.00 14.04 ? 32  TRP F N   1 
ATOM   5772  C  CA  . TRP F  1 32  ? 17.703  66.911  48.370  1.00 15.49 ? 32  TRP F CA  1 
ATOM   5773  C  C   . TRP F  1 32  ? 18.847  65.916  48.426  1.00 11.12 ? 32  TRP F C   1 
ATOM   5774  O  O   . TRP F  1 32  ? 18.806  64.879  47.802  1.00 16.73 ? 32  TRP F O   1 
ATOM   5775  C  CB  . TRP F  1 32  ? 16.817  66.754  49.610  1.00 15.52 ? 32  TRP F CB  1 
ATOM   5776  C  CG  . TRP F  1 32  ? 16.451  65.343  49.932  1.00 16.22 ? 32  TRP F CG  1 
ATOM   5777  C  CD1 . TRP F  1 32  ? 17.035  64.545  50.876  1.00 18.98 ? 32  TRP F CD1 1 
ATOM   5778  C  CD2 . TRP F  1 32  ? 15.409  64.555  49.333  1.00 15.92 ? 32  TRP F CD2 1 
ATOM   5779  N  NE1 . TRP F  1 32  ? 16.423  63.314  50.899  1.00 19.59 ? 32  TRP F NE1 1 
ATOM   5780  C  CE2 . TRP F  1 32  ? 15.418  63.296  49.970  1.00 18.59 ? 32  TRP F CE2 1 
ATOM   5781  C  CE3 . TRP F  1 32  ? 14.471  64.790  48.322  1.00 16.79 ? 32  TRP F CE3 1 
ATOM   5782  C  CZ2 . TRP F  1 32  ? 14.532  62.274  49.621  1.00 19.21 ? 32  TRP F CZ2 1 
ATOM   5783  C  CZ3 . TRP F  1 32  ? 13.593  63.773  47.980  1.00 16.93 ? 32  TRP F CZ3 1 
ATOM   5784  C  CH2 . TRP F  1 32  ? 13.624  62.532  48.637  1.00 18.26 ? 32  TRP F CH2 1 
ATOM   5785  N  N   . GLY F  1 33  ? 19.866  66.250  49.197  1.00 16.22 ? 33  GLY F N   1 
ATOM   5786  C  CA  . GLY F  1 33  ? 21.051  65.423  49.276  1.00 21.52 ? 33  GLY F CA  1 
ATOM   5787  C  C   . GLY F  1 33  ? 22.268  66.234  49.664  1.00 21.34 ? 33  GLY F C   1 
ATOM   5788  O  O   . GLY F  1 33  ? 22.164  67.415  49.995  1.00 21.48 ? 33  GLY F O   1 
ATOM   5789  N  N   . SER F  1 34  ? 23.431  65.603  49.616  1.00 21.60 ? 34  SER F N   1 
ATOM   5790  C  CA  . SER F  1 34  ? 24.635  66.211  50.152  1.00 20.53 ? 34  SER F CA  1 
ATOM   5791  C  C   . SER F  1 34  ? 25.700  66.268  49.068  1.00 23.90 ? 34  SER F C   1 
ATOM   5792  O  O   . SER F  1 34  ? 25.932  65.280  48.366  1.00 28.86 ? 34  SER F O   1 
ATOM   5793  C  CB  . SER F  1 34  ? 25.141  65.383  51.335  1.00 26.45 ? 34  SER F CB  1 
ATOM   5794  O  OG  . SER F  1 34  ? 26.000  66.138  52.172  1.00 27.96 ? 34  SER F OG  1 
ATOM   5795  N  N   . ILE F  1 35  ? 26.324  67.427  48.894  1.00 23.40 ? 35  ILE F N   1 
ATOM   5796  C  CA  . ILE F  1 35  ? 27.502  67.517  48.020  1.00 24.06 ? 35  ILE F CA  1 
ATOM   5797  C  C   . ILE F  1 35  ? 28.646  68.070  48.839  1.00 24.26 ? 35  ILE F C   1 
ATOM   5798  O  O   . ILE F  1 35  ? 28.493  69.064  49.559  1.00 21.03 ? 35  ILE F O   1 
ATOM   5799  C  CB  . ILE F  1 35  ? 27.264  68.393  46.774  1.00 26.09 ? 35  ILE F CB  1 
ATOM   5800  C  CG1 . ILE F  1 35  ? 25.837  68.209  46.256  1.00 19.72 ? 35  ILE F CG1 1 
ATOM   5801  C  CG2 . ILE F  1 35  ? 28.253  68.034  45.669  1.00 25.44 ? 35  ILE F CG2 1 
ATOM   5802  C  CD1 . ILE F  1 35  ? 25.465  69.143  45.124  1.00 18.21 ? 35  ILE F CD1 1 
ATOM   5803  N  N   . LYS F  1 36  ? 29.786  67.395  48.764  1.00 28.16 ? 36  LYS F N   1 
ATOM   5804  C  CA  . LYS F  1 36  ? 30.958  67.830  49.505  1.00 29.06 ? 36  LYS F CA  1 
ATOM   5805  C  C   . LYS F  1 36  ? 32.071  68.192  48.525  1.00 30.34 ? 36  LYS F C   1 
ATOM   5806  O  O   . LYS F  1 36  ? 32.028  67.792  47.361  1.00 31.92 ? 36  LYS F O   1 
ATOM   5807  C  CB  . LYS F  1 36  ? 31.415  66.728  50.454  1.00 34.43 ? 36  LYS F CB  1 
ATOM   5808  C  CG  . LYS F  1 36  ? 31.679  65.388  49.771  1.00 33.53 ? 36  LYS F CG  1 
ATOM   5809  C  CD  . LYS F  1 36  ? 32.316  64.432  50.771  1.00 43.28 ? 36  LYS F CD  1 
ATOM   5810  C  CE  . LYS F  1 36  ? 32.955  63.240  50.092  1.00 45.05 ? 36  LYS F CE  1 
ATOM   5811  N  NZ  . LYS F  1 36  ? 33.627  62.379  51.102  1.00 52.75 ? 36  LYS F NZ  1 
ATOM   5812  N  N   . GLY F  1 37  ? 33.053  68.953  48.997  1.00 33.00 ? 37  GLY F N   1 
ATOM   5813  C  CA  . GLY F  1 37  ? 34.185  69.328  48.166  1.00 35.12 ? 37  GLY F CA  1 
ATOM   5814  C  C   . GLY F  1 37  ? 34.204  70.783  47.714  1.00 40.19 ? 37  GLY F C   1 
ATOM   5815  O  O   . GLY F  1 37  ? 35.152  71.216  47.048  1.00 40.16 ? 37  GLY F O   1 
ATOM   5816  N  N   . LEU F  1 38  ? 33.179  71.542  48.104  1.00 35.77 ? 38  LEU F N   1 
ATOM   5817  C  CA  . LEU F  1 38  ? 32.919  72.868  47.549  1.00 30.95 ? 38  LEU F CA  1 
ATOM   5818  C  C   . LEU F  1 38  ? 33.518  73.996  48.377  1.00 34.21 ? 38  LEU F C   1 
ATOM   5819  O  O   . LEU F  1 38  ? 33.728  73.852  49.581  1.00 33.43 ? 38  LEU F O   1 
ATOM   5820  C  CB  . LEU F  1 38  ? 31.404  73.094  47.438  1.00 26.07 ? 38  LEU F CB  1 
ATOM   5821  C  CG  . LEU F  1 38  ? 30.645  72.135  46.532  1.00 25.09 ? 38  LEU F CG  1 
ATOM   5822  C  CD1 . LEU F  1 38  ? 29.131  72.266  46.706  1.00 26.51 ? 38  LEU F CD1 1 
ATOM   5823  C  CD2 . LEU F  1 38  ? 31.035  72.365  45.096  1.00 25.46 ? 38  LEU F CD2 1 
ATOM   5824  N  N   . THR F  1 39  ? 33.796  75.124  47.728  1.00 30.67 ? 39  THR F N   1 
ATOM   5825  C  CA  . THR F  1 39  ? 34.151  76.339  48.443  1.00 28.43 ? 39  THR F CA  1 
ATOM   5826  C  C   . THR F  1 39  ? 32.895  76.906  49.081  1.00 25.80 ? 39  THR F C   1 
ATOM   5827  O  O   . THR F  1 39  ? 31.823  76.816  48.496  1.00 28.35 ? 39  THR F O   1 
ATOM   5828  C  CB  . THR F  1 39  ? 34.718  77.394  47.484  1.00 30.25 ? 39  THR F CB  1 
ATOM   5829  O  OG1 . THR F  1 39  ? 33.984  77.338  46.253  1.00 39.19 ? 39  THR F OG1 1 
ATOM   5830  C  CG2 . THR F  1 39  ? 36.186  77.122  47.190  1.00 26.82 ? 39  THR F CG2 1 
ATOM   5831  N  N   . GLU F  1 40  ? 33.039  77.490  50.269  1.00 23.95 ? 40  GLU F N   1 
ATOM   5832  C  CA  . GLU F  1 40  ? 31.925  78.101  50.981  1.00 28.77 ? 40  GLU F CA  1 
ATOM   5833  C  C   . GLU F  1 40  ? 31.189  79.091  50.068  1.00 35.99 ? 40  GLU F C   1 
ATOM   5834  O  O   . GLU F  1 40  ? 31.823  79.830  49.310  1.00 32.24 ? 40  GLU F O   1 
ATOM   5835  C  CB  . GLU F  1 40  ? 32.413  78.797  52.252  1.00 27.81 ? 40  GLU F CB  1 
ATOM   5836  C  CG  . GLU F  1 40  ? 31.288  79.322  53.139  1.00 31.39 ? 40  GLU F CG  1 
ATOM   5837  C  CD  . GLU F  1 40  ? 31.789  80.010  54.403  1.00 41.67 ? 40  GLU F CD  1 
ATOM   5838  O  OE1 . GLU F  1 40  ? 33.016  80.239  54.506  1.00 37.44 ? 40  GLU F OE1 1 
ATOM   5839  O  OE2 . GLU F  1 40  ? 30.952  80.321  55.296  1.00 44.75 ? 40  GLU F OE2 1 
ATOM   5840  N  N   . GLY F  1 41  ? 29.855  79.072  50.117  1.00 31.05 ? 41  GLY F N   1 
ATOM   5841  C  CA  . GLY F  1 41  ? 29.048  79.961  49.300  1.00 23.77 ? 41  GLY F CA  1 
ATOM   5842  C  C   . GLY F  1 41  ? 28.347  79.328  48.110  1.00 26.88 ? 41  GLY F C   1 
ATOM   5843  O  O   . GLY F  1 41  ? 28.214  78.100  48.021  1.00 27.40 ? 41  GLY F O   1 
ATOM   5844  N  N   . LEU F  1 42  ? 27.935  80.183  47.174  1.00 23.25 ? 42  LEU F N   1 
ATOM   5845  C  CA  . LEU F  1 42  ? 26.962  79.846  46.136  1.00 24.06 ? 42  LEU F CA  1 
ATOM   5846  C  C   . LEU F  1 42  ? 27.537  79.063  44.970  1.00 21.93 ? 42  LEU F C   1 
ATOM   5847  O  O   . LEU F  1 42  ? 28.632  79.341  44.509  1.00 25.66 ? 42  LEU F O   1 
ATOM   5848  C  CB  . LEU F  1 42  ? 26.319  81.134  45.598  1.00 25.30 ? 42  LEU F CB  1 
ATOM   5849  C  CG  . LEU F  1 42  ? 24.934  81.677  45.994  1.00 26.08 ? 42  LEU F CG  1 
ATOM   5850  C  CD1 . LEU F  1 42  ? 24.294  80.993  47.186  1.00 21.33 ? 42  LEU F CD1 1 
ATOM   5851  C  CD2 . LEU F  1 42  ? 25.006  83.180  46.219  1.00 24.10 ? 42  LEU F CD2 1 
ATOM   5852  N  N   . HIS F  1 43  ? 26.766  78.100  44.480  1.00 19.63 ? 43  HIS F N   1 
ATOM   5853  C  CA  . HIS F  1 43  ? 27.141  77.302  43.334  1.00 19.90 ? 43  HIS F CA  1 
ATOM   5854  C  C   . HIS F  1 43  ? 25.924  77.013  42.464  1.00 22.18 ? 43  HIS F C   1 
ATOM   5855  O  O   . HIS F  1 43  ? 24.907  76.544  42.952  1.00 20.96 ? 43  HIS F O   1 
ATOM   5856  C  CB  . HIS F  1 43  ? 27.791  75.999  43.790  1.00 21.07 ? 43  HIS F CB  1 
ATOM   5857  C  CG  . HIS F  1 43  ? 29.081  76.201  44.525  1.00 24.29 ? 43  HIS F CG  1 
ATOM   5858  N  ND1 . HIS F  1 43  ? 30.313  76.056  43.920  1.00 22.32 ? 43  HIS F ND1 1 
ATOM   5859  C  CD2 . HIS F  1 43  ? 29.331  76.548  45.813  1.00 26.12 ? 43  HIS F CD2 1 
ATOM   5860  C  CE1 . HIS F  1 43  ? 31.264  76.309  44.802  1.00 29.17 ? 43  HIS F CE1 1 
ATOM   5861  N  NE2 . HIS F  1 43  ? 30.696  76.609  45.960  1.00 29.73 ? 43  HIS F NE2 1 
ATOM   5862  N  N   . GLY F  1 44  ? 26.033  77.306  41.175  1.00 20.90 ? 44  GLY F N   1 
ATOM   5863  C  CA  . GLY F  1 44  ? 24.928  77.142  40.249  1.00 20.00 ? 44  GLY F CA  1 
ATOM   5864  C  C   . GLY F  1 44  ? 24.580  75.684  40.115  1.00 21.16 ? 44  GLY F C   1 
ATOM   5865  O  O   . GLY F  1 44  ? 25.456  74.841  40.229  1.00 22.36 ? 44  GLY F O   1 
ATOM   5866  N  N   . PHE F  1 45  ? 23.315  75.387  39.840  1.00 17.97 ? 45  PHE F N   1 
ATOM   5867  C  CA  . PHE F  1 45  ? 22.804  74.037  40.000  1.00 18.73 ? 45  PHE F CA  1 
ATOM   5868  C  C   . PHE F  1 45  ? 21.724  73.843  38.960  1.00 19.00 ? 45  PHE F C   1 
ATOM   5869  O  O   . PHE F  1 45  ? 20.616  74.365  39.115  1.00 21.05 ? 45  PHE F O   1 
ATOM   5870  C  CB  . PHE F  1 45  ? 22.255  73.906  41.440  1.00 18.88 ? 45  PHE F CB  1 
ATOM   5871  C  CG  . PHE F  1 45  ? 21.947  72.490  41.892  1.00 20.94 ? 45  PHE F CG  1 
ATOM   5872  C  CD1 . PHE F  1 45  ? 22.962  71.586  42.169  1.00 21.16 ? 45  PHE F CD1 1 
ATOM   5873  C  CD2 . PHE F  1 45  ? 20.633  72.094  42.124  1.00 20.40 ? 45  PHE F CD2 1 
ATOM   5874  C  CE1 . PHE F  1 45  ? 22.666  70.283  42.610  1.00 18.48 ? 45  PHE F CE1 1 
ATOM   5875  C  CE2 . PHE F  1 45  ? 20.339  70.813  42.576  1.00 20.09 ? 45  PHE F CE2 1 
ATOM   5876  C  CZ  . PHE F  1 45  ? 21.366  69.906  42.821  1.00 15.97 ? 45  PHE F CZ  1 
ATOM   5877  N  N   . HIS F  1 46  ? 22.048  73.110  37.892  1.00 19.08 ? 46  HIS F N   1 
ATOM   5878  C  CA  . HIS F  1 46  ? 21.173  73.009  36.718  1.00 21.11 ? 46  HIS F CA  1 
ATOM   5879  C  C   . HIS F  1 46  ? 21.011  71.584  36.214  1.00 18.90 ? 46  HIS F C   1 
ATOM   5880  O  O   . HIS F  1 46  ? 21.894  70.757  36.341  1.00 23.05 ? 46  HIS F O   1 
ATOM   5881  C  CB  . HIS F  1 46  ? 21.724  73.846  35.547  1.00 22.32 ? 46  HIS F CB  1 
ATOM   5882  C  CG  . HIS F  1 46  ? 22.271  75.175  35.951  1.00 20.24 ? 46  HIS F CG  1 
ATOM   5883  N  ND1 . HIS F  1 46  ? 23.551  75.578  35.639  1.00 29.43 ? 46  HIS F ND1 1 
ATOM   5884  C  CD2 . HIS F  1 46  ? 21.716  76.196  36.644  1.00 22.33 ? 46  HIS F CD2 1 
ATOM   5885  C  CE1 . HIS F  1 46  ? 23.768  76.784  36.134  1.00 27.49 ? 46  HIS F CE1 1 
ATOM   5886  N  NE2 . HIS F  1 46  ? 22.669  77.182  36.750  1.00 27.92 ? 46  HIS F NE2 1 
ATOM   5887  N  N   . VAL F  1 47  ? 19.866  71.305  35.629  1.00 17.76 ? 47  VAL F N   1 
ATOM   5888  C  CA  . VAL F  1 47  ? 19.718  70.124  34.814  1.00 21.93 ? 47  VAL F CA  1 
ATOM   5889  C  C   . VAL F  1 47  ? 20.055  70.489  33.360  1.00 29.19 ? 47  VAL F C   1 
ATOM   5890  O  O   . VAL F  1 47  ? 19.333  71.258  32.734  1.00 27.23 ? 47  VAL F O   1 
ATOM   5891  C  CB  . VAL F  1 47  ? 18.300  69.621  34.881  1.00 20.13 ? 47  VAL F CB  1 
ATOM   5892  C  CG1 . VAL F  1 47  ? 18.109  68.430  33.962  1.00 17.78 ? 47  VAL F CG1 1 
ATOM   5893  C  CG2 . VAL F  1 47  ? 17.954  69.260  36.341  1.00 21.39 ? 47  VAL F CG2 1 
ATOM   5894  N  N   . HIS F  1 48  ? 21.169  69.968  32.844  1.00 28.44 ? 48  HIS F N   1 
ATOM   5895  C  CA  . HIS F  1 48  ? 21.506  70.115  31.421  1.00 27.40 ? 48  HIS F CA  1 
ATOM   5896  C  C   . HIS F  1 48  ? 20.807  69.059  30.576  1.00 30.29 ? 48  HIS F C   1 
ATOM   5897  O  O   . HIS F  1 48  ? 20.288  68.086  31.103  1.00 29.61 ? 48  HIS F O   1 
ATOM   5898  C  CB  . HIS F  1 48  ? 23.009  70.088  31.203  1.00 24.66 ? 48  HIS F CB  1 
ATOM   5899  C  CG  . HIS F  1 48  ? 23.720  71.270  31.783  1.00 26.15 ? 48  HIS F CG  1 
ATOM   5900  N  ND1 . HIS F  1 48  ? 24.514  72.105  31.028  1.00 24.78 ? 48  HIS F ND1 1 
ATOM   5901  C  CD2 . HIS F  1 48  ? 23.755  71.758  33.048  1.00 28.26 ? 48  HIS F CD2 1 
ATOM   5902  C  CE1 . HIS F  1 48  ? 25.010  73.054  31.803  1.00 30.88 ? 48  HIS F CE1 1 
ATOM   5903  N  NE2 . HIS F  1 48  ? 24.561  72.871  33.033  1.00 23.35 ? 48  HIS F NE2 1 
ATOM   5904  N  N   . GLU F  1 49  ? 20.773  69.273  29.266  1.00 32.04 ? 49  GLU F N   1 
ATOM   5905  C  CA  . GLU F  1 49  ? 19.848  68.560  28.379  1.00 34.73 ? 49  GLU F CA  1 
ATOM   5906  C  C   . GLU F  1 49  ? 20.103  67.067  28.180  1.00 33.47 ? 49  GLU F C   1 
ATOM   5907  O  O   . GLU F  1 49  ? 19.158  66.272  28.070  1.00 33.09 ? 49  GLU F O   1 
ATOM   5908  C  CB  . GLU F  1 49  ? 19.856  69.225  26.996  1.00 35.88 ? 49  GLU F CB  1 
ATOM   5909  C  CG  . GLU F  1 49  ? 18.802  68.699  26.040  1.00 28.68 ? 49  GLU F CG  1 
ATOM   5910  C  CD  . GLU F  1 49  ? 18.777  69.499  24.746  1.00 34.76 ? 49  GLU F CD  1 
ATOM   5911  O  OE1 . GLU F  1 49  ? 19.586  70.450  24.645  1.00 34.51 ? 49  GLU F OE1 1 
ATOM   5912  O  OE2 . GLU F  1 49  ? 17.958  69.191  23.846  1.00 26.87 ? 49  GLU F OE2 1 
ATOM   5913  N  N   . PHE F  1 50  ? 21.374  66.700  28.060  1.00 37.30 ? 50  PHE F N   1 
ATOM   5914  C  CA  . PHE F  1 50  ? 21.719  65.336  27.681  1.00 43.46 ? 50  PHE F CA  1 
ATOM   5915  C  C   . PHE F  1 50  ? 22.458  64.613  28.801  1.00 39.63 ? 50  PHE F C   1 
ATOM   5916  O  O   . PHE F  1 50  ? 23.408  65.146  29.383  1.00 39.55 ? 50  PHE F O   1 
ATOM   5917  C  CB  . PHE F  1 50  ? 22.577  65.311  26.406  1.00 40.75 ? 50  PHE F CB  1 
ATOM   5918  C  CG  . PHE F  1 50  ? 21.994  66.083  25.260  1.00 39.96 ? 50  PHE F CG  1 
ATOM   5919  C  CD1 . PHE F  1 50  ? 20.776  65.718  24.710  1.00 40.36 ? 50  PHE F CD1 1 
ATOM   5920  C  CD2 . PHE F  1 50  ? 22.675  67.161  24.716  1.00 40.77 ? 50  PHE F CD2 1 
ATOM   5921  C  CE1 . PHE F  1 50  ? 20.231  66.427  23.645  1.00 37.61 ? 50  PHE F CE1 1 
ATOM   5922  C  CE2 . PHE F  1 50  ? 22.143  67.868  23.646  1.00 35.98 ? 50  PHE F CE2 1 
ATOM   5923  C  CZ  . PHE F  1 50  ? 20.919  67.502  23.114  1.00 34.72 ? 50  PHE F CZ  1 
ATOM   5924  N  N   . GLY F  1 51  ? 22.018  63.395  29.093  1.00 40.79 ? 51  GLY F N   1 
ATOM   5925  C  CA  . GLY F  1 51  ? 22.739  62.542  30.016  1.00 41.40 ? 51  GLY F CA  1 
ATOM   5926  C  C   . GLY F  1 51  ? 23.877  61.867  29.272  1.00 44.54 ? 51  GLY F C   1 
ATOM   5927  O  O   . GLY F  1 51  ? 23.864  60.653  29.062  1.00 43.16 ? 51  GLY F O   1 
ATOM   5928  N  N   . ASP F  1 52  ? 24.856  62.669  28.858  1.00 46.38 ? 52  ASP F N   1 
ATOM   5929  C  CA  . ASP F  1 52  ? 25.953  62.198  28.025  1.00 38.54 ? 52  ASP F CA  1 
ATOM   5930  C  C   . ASP F  1 52  ? 27.257  62.572  28.680  1.00 46.06 ? 52  ASP F C   1 
ATOM   5931  O  O   . ASP F  1 52  ? 27.631  63.743  28.714  1.00 46.01 ? 52  ASP F O   1 
ATOM   5932  C  CB  . ASP F  1 52  ? 25.873  62.835  26.639  1.00 49.53 ? 52  ASP F CB  1 
ATOM   5933  C  CG  . ASP F  1 52  ? 26.772  62.149  25.620  1.00 48.83 ? 52  ASP F CG  1 
ATOM   5934  O  OD1 . ASP F  1 52  ? 27.948  61.863  25.946  1.00 42.90 ? 52  ASP F OD1 1 
ATOM   5935  O  OD2 . ASP F  1 52  ? 26.285  61.898  24.493  1.00 44.74 ? 52  ASP F OD2 1 
ATOM   5936  N  N   . ASN F  1 53  ? 27.955  61.572  29.198  1.00 47.16 ? 53  ASN F N   1 
ATOM   5937  C  CA  . ASN F  1 53  ? 29.192  61.813  29.926  1.00 50.03 ? 53  ASN F CA  1 
ATOM   5938  C  C   . ASN F  1 53  ? 30.416  61.385  29.106  1.00 54.09 ? 53  ASN F C   1 
ATOM   5939  O  O   . ASN F  1 53  ? 31.532  61.335  29.624  1.00 52.86 ? 53  ASN F O   1 
ATOM   5940  C  CB  . ASN F  1 53  ? 29.136  61.090  31.277  1.00 46.93 ? 53  ASN F CB  1 
ATOM   5941  C  CG  . ASN F  1 53  ? 30.328  61.386  32.154  1.00 55.36 ? 53  ASN F CG  1 
ATOM   5942  O  OD1 . ASN F  1 53  ? 30.725  62.542  32.316  1.00 59.00 ? 53  ASN F OD1 1 
ATOM   5943  N  ND2 . ASN F  1 53  ? 30.927  60.334  32.711  1.00 49.22 ? 53  ASN F ND2 1 
ATOM   5944  N  N   . THR F  1 54  ? 30.202  61.097  27.820  1.00 55.56 ? 54  THR F N   1 
ATOM   5945  C  CA  . THR F  1 54  ? 31.288  60.636  26.942  1.00 54.45 ? 54  THR F CA  1 
ATOM   5946  C  C   . THR F  1 54  ? 32.491  61.580  26.926  1.00 56.55 ? 54  THR F C   1 
ATOM   5947  O  O   . THR F  1 54  ? 33.638  61.134  26.996  1.00 56.06 ? 54  THR F O   1 
ATOM   5948  C  CB  . THR F  1 54  ? 30.809  60.407  25.499  1.00 50.56 ? 54  THR F CB  1 
ATOM   5949  O  OG1 . THR F  1 54  ? 30.202  61.604  25.011  1.00 50.44 ? 54  THR F OG1 1 
ATOM   5950  C  CG2 . THR F  1 54  ? 29.794  59.278  25.444  1.00 47.42 ? 54  THR F CG2 1 
ATOM   5951  N  N   . ALA F  1 55  ? 32.228  62.881  26.847  1.00 54.66 ? 55  ALA F N   1 
ATOM   5952  C  CA  . ALA F  1 55  ? 33.296  63.877  26.884  1.00 56.94 ? 55  ALA F CA  1 
ATOM   5953  C  C   . ALA F  1 55  ? 33.490  64.465  28.291  1.00 59.07 ? 55  ALA F C   1 
ATOM   5954  O  O   . ALA F  1 55  ? 34.180  65.472  28.472  1.00 55.15 ? 55  ALA F O   1 
ATOM   5955  C  CB  . ALA F  1 55  ? 33.015  64.980  25.881  1.00 52.08 ? 55  ALA F CB  1 
ATOM   5956  N  N   . GLY F  1 56  ? 32.885  63.827  29.288  1.00 57.43 ? 56  GLY F N   1 
ATOM   5957  C  CA  . GLY F  1 56  ? 32.871  64.378  30.631  1.00 54.97 ? 56  GLY F CA  1 
ATOM   5958  C  C   . GLY F  1 56  ? 31.621  65.218  30.812  1.00 55.49 ? 56  GLY F C   1 
ATOM   5959  O  O   . GLY F  1 56  ? 30.568  64.902  30.240  1.00 51.16 ? 56  GLY F O   1 
ATOM   5960  N  N   . SER F  1 57  ? 31.732  66.290  31.597  1.00 54.62 ? 57  SER F N   1 
ATOM   5961  C  CA  . SER F  1 57  ? 30.597  67.184  31.830  1.00 50.12 ? 57  SER F CA  1 
ATOM   5962  C  C   . SER F  1 57  ? 30.161  67.892  30.541  1.00 50.94 ? 57  SER F C   1 
ATOM   5963  O  O   . SER F  1 57  ? 28.980  67.858  30.170  1.00 46.62 ? 57  SER F O   1 
ATOM   5964  C  CB  . SER F  1 57  ? 30.921  68.196  32.931  1.00 47.85 ? 57  SER F CB  1 
ATOM   5965  O  OG  . SER F  1 57  ? 32.224  68.732  32.767  1.00 53.95 ? 57  SER F OG  1 
ATOM   5966  N  N   . THR F  1 58  ? 31.133  68.492  29.854  1.00 49.85 ? 58  THR F N   1 
ATOM   5967  C  CA  . THR F  1 58  ? 30.922  69.194  28.580  1.00 49.86 ? 58  THR F CA  1 
ATOM   5968  C  C   . THR F  1 58  ? 29.899  68.593  27.601  1.00 47.24 ? 58  THR F C   1 
ATOM   5969  O  O   . THR F  1 58  ? 29.230  69.325  26.880  1.00 50.05 ? 58  THR F O   1 
ATOM   5970  C  CB  . THR F  1 58  ? 32.250  69.364  27.827  1.00 50.87 ? 58  THR F CB  1 
ATOM   5971  O  OG1 . THR F  1 58  ? 32.073  68.962  26.459  1.00 48.34 ? 58  THR F OG1 1 
ATOM   5972  C  CG2 . THR F  1 58  ? 33.331  68.516  28.473  1.00 46.78 ? 58  THR F CG2 1 
ATOM   5973  N  N   . SER F  1 59  ? 29.780  67.271  27.564  1.00 47.55 ? 59  SER F N   1 
ATOM   5974  C  CA  . SER F  1 59  ? 28.858  66.625  26.630  1.00 42.32 ? 59  SER F CA  1 
ATOM   5975  C  C   . SER F  1 59  ? 27.419  66.600  27.140  1.00 43.76 ? 59  SER F C   1 
ATOM   5976  O  O   . SER F  1 59  ? 26.536  66.027  26.500  1.00 39.64 ? 59  SER F O   1 
ATOM   5977  C  CB  . SER F  1 59  ? 29.324  65.204  26.312  1.00 45.47 ? 59  SER F CB  1 
ATOM   5978  O  OG  . SER F  1 59  ? 29.968  64.616  27.433  1.00 53.36 ? 59  SER F OG  1 
ATOM   5979  N  N   . ALA F  1 60  ? 27.181  67.214  28.296  1.00 44.45 ? 60  ALA F N   1 
ATOM   5980  C  CA  . ALA F  1 60  ? 25.828  67.271  28.840  1.00 43.40 ? 60  ALA F CA  1 
ATOM   5981  C  C   . ALA F  1 60  ? 24.931  68.059  27.895  1.00 44.68 ? 60  ALA F C   1 
ATOM   5982  O  O   . ALA F  1 60  ? 23.769  67.705  27.654  1.00 38.17 ? 60  ALA F O   1 
ATOM   5983  C  CB  . ALA F  1 60  ? 25.840  67.915  30.204  1.00 41.72 ? 60  ALA F CB  1 
ATOM   5984  N  N   . GLY F  1 61  ? 25.492  69.130  27.348  1.00 42.90 ? 61  GLY F N   1 
ATOM   5985  C  CA  . GLY F  1 61  ? 24.724  70.045  26.537  1.00 41.70 ? 61  GLY F CA  1 
ATOM   5986  C  C   . GLY F  1 61  ? 24.497  71.333  27.304  1.00 37.72 ? 61  GLY F C   1 
ATOM   5987  O  O   . GLY F  1 61  ? 25.192  71.616  28.292  1.00 34.80 ? 61  GLY F O   1 
ATOM   5988  N  N   . PRO F  1 62  ? 23.528  72.128  26.841  1.00 35.60 ? 62  PRO F N   1 
ATOM   5989  C  CA  . PRO F  1 62  ? 23.190  73.406  27.462  1.00 39.75 ? 62  PRO F CA  1 
ATOM   5990  C  C   . PRO F  1 62  ? 22.170  73.118  28.544  1.00 36.15 ? 62  PRO F C   1 
ATOM   5991  O  O   . PRO F  1 62  ? 21.708  71.970  28.622  1.00 33.56 ? 62  PRO F O   1 
ATOM   5992  C  CB  . PRO F  1 62  ? 22.493  74.142  26.324  1.00 33.00 ? 62  PRO F CB  1 
ATOM   5993  C  CG  . PRO F  1 62  ? 21.716  73.037  25.644  1.00 32.74 ? 62  PRO F CG  1 
ATOM   5994  C  CD  . PRO F  1 62  ? 22.609  71.802  25.735  1.00 32.68 ? 62  PRO F CD  1 
ATOM   5995  N  N   . HIS F  1 63  ? 21.806  74.127  29.334  1.00 32.96 ? 63  HIS F N   1 
ATOM   5996  C  CA  . HIS F  1 63  ? 20.677  73.991  30.260  1.00 32.89 ? 63  HIS F CA  1 
ATOM   5997  C  C   . HIS F  1 63  ? 19.483  73.340  29.573  1.00 29.12 ? 63  HIS F C   1 
ATOM   5998  O  O   . HIS F  1 63  ? 19.186  73.638  28.420  1.00 32.08 ? 63  HIS F O   1 
ATOM   5999  C  CB  . HIS F  1 63  ? 20.276  75.354  30.814  1.00 28.86 ? 63  HIS F CB  1 
ATOM   6000  C  CG  . HIS F  1 63  ? 21.315  75.977  31.682  1.00 21.75 ? 63  HIS F CG  1 
ATOM   6001  N  ND1 . HIS F  1 63  ? 21.108  77.156  32.363  1.00 23.15 ? 63  HIS F ND1 1 
ATOM   6002  C  CD2 . HIS F  1 63  ? 22.576  75.587  31.977  1.00 28.80 ? 63  HIS F CD2 1 
ATOM   6003  C  CE1 . HIS F  1 63  ? 22.194  77.461  33.050  1.00 27.71 ? 63  HIS F CE1 1 
ATOM   6004  N  NE2 . HIS F  1 63  ? 23.101  76.525  32.832  1.00 31.36 ? 63  HIS F NE2 1 
ATOM   6005  N  N   . PHE F  1 64  ? 18.821  72.420  30.263  1.00 26.94 ? 64  PHE F N   1 
ATOM   6006  C  CA  . PHE F  1 64  ? 17.647  71.772  29.693  1.00 24.86 ? 64  PHE F CA  1 
ATOM   6007  C  C   . PHE F  1 64  ? 16.566  72.819  29.456  1.00 32.90 ? 64  PHE F C   1 
ATOM   6008  O  O   . PHE F  1 64  ? 16.045  73.426  30.406  1.00 25.68 ? 64  PHE F O   1 
ATOM   6009  C  CB  . PHE F  1 64  ? 17.137  70.674  30.627  1.00 27.13 ? 64  PHE F CB  1 
ATOM   6010  C  CG  . PHE F  1 64  ? 15.892  69.983  30.144  1.00 24.46 ? 64  PHE F CG  1 
ATOM   6011  C  CD1 . PHE F  1 64  ? 15.750  69.622  28.816  1.00 27.73 ? 64  PHE F CD1 1 
ATOM   6012  C  CD2 . PHE F  1 64  ? 14.873  69.665  31.030  1.00 23.55 ? 64  PHE F CD2 1 
ATOM   6013  C  CE1 . PHE F  1 64  ? 14.602  68.973  28.375  1.00 22.15 ? 64  PHE F CE1 1 
ATOM   6014  C  CE2 . PHE F  1 64  ? 13.733  69.016  30.601  1.00 24.83 ? 64  PHE F CE2 1 
ATOM   6015  C  CZ  . PHE F  1 64  ? 13.599  68.668  29.272  1.00 25.24 ? 64  PHE F CZ  1 
ATOM   6016  N  N   . ASN F  1 65  ? 16.225  73.030  28.188  1.00 35.46 ? 65  ASN F N   1 
ATOM   6017  C  CA  . ASN F  1 65  ? 15.337  74.130  27.817  1.00 30.28 ? 65  ASN F CA  1 
ATOM   6018  C  C   . ASN F  1 65  ? 14.356  73.794  26.714  1.00 31.50 ? 65  ASN F C   1 
ATOM   6019  O  O   . ASN F  1 65  ? 14.494  74.294  25.610  1.00 39.07 ? 65  ASN F O   1 
ATOM   6020  C  CB  . ASN F  1 65  ? 16.178  75.335  27.397  1.00 28.23 ? 65  ASN F CB  1 
ATOM   6021  C  CG  . ASN F  1 65  ? 15.346  76.580  27.145  1.00 33.68 ? 65  ASN F CG  1 
ATOM   6022  O  OD1 . ASN F  1 65  ? 14.166  76.642  27.506  1.00 29.45 ? 65  ASN F OD1 1 
ATOM   6023  N  ND2 . ASN F  1 65  ? 15.968  77.589  26.518  1.00 31.79 ? 65  ASN F ND2 1 
ATOM   6024  N  N   . PRO F  1 66  ? 13.345  72.965  27.012  1.00 32.63 ? 66  PRO F N   1 
ATOM   6025  C  CA  . PRO F  1 66  ? 12.427  72.490  25.975  1.00 31.11 ? 66  PRO F CA  1 
ATOM   6026  C  C   . PRO F  1 66  ? 11.310  73.463  25.625  1.00 39.24 ? 66  PRO F C   1 
ATOM   6027  O  O   . PRO F  1 66  ? 10.466  73.122  24.793  1.00 41.58 ? 66  PRO F O   1 
ATOM   6028  C  CB  . PRO F  1 66  ? 11.819  71.239  26.605  1.00 31.60 ? 66  PRO F CB  1 
ATOM   6029  C  CG  . PRO F  1 66  ? 11.813  71.532  28.046  1.00 30.79 ? 66  PRO F CG  1 
ATOM   6030  C  CD  . PRO F  1 66  ? 13.090  72.304  28.303  1.00 31.70 ? 66  PRO F CD  1 
ATOM   6031  N  N   . LEU F  1 67  ? 11.274  74.633  26.250  1.00 37.88 ? 67  LEU F N   1 
ATOM   6032  C  CA  . LEU F  1 67  ? 10.281  75.635  25.872  1.00 39.74 ? 67  LEU F CA  1 
ATOM   6033  C  C   . LEU F  1 67  ? 11.009  76.841  25.303  1.00 34.58 ? 67  LEU F C   1 
ATOM   6034  O  O   . LEU F  1 67  ? 10.415  77.890  25.086  1.00 40.57 ? 67  LEU F O   1 
ATOM   6035  C  CB  . LEU F  1 67  ? 9.405   76.030  27.066  1.00 41.46 ? 67  LEU F CB  1 
ATOM   6036  C  CG  . LEU F  1 67  ? 8.748   74.877  27.825  1.00 42.19 ? 67  LEU F CG  1 
ATOM   6037  C  CD1 . LEU F  1 67  ? 7.706   75.360  28.820  1.00 37.67 ? 67  LEU F CD1 1 
ATOM   6038  C  CD2 . LEU F  1 67  ? 8.130   73.905  26.865  1.00 46.38 ? 67  LEU F CD2 1 
ATOM   6039  N  N   . SER F  1 68  ? 12.307  76.658  25.071  1.00 36.91 ? 68  SER F N   1 
ATOM   6040  C  CA  . SER F  1 68  ? 13.211  77.694  24.565  1.00 34.61 ? 68  SER F CA  1 
ATOM   6041  C  C   . SER F  1 68  ? 12.954  79.077  25.163  1.00 37.57 ? 68  SER F C   1 
ATOM   6042  O  O   . SER F  1 68  ? 12.507  79.986  24.466  1.00 32.44 ? 68  SER F O   1 
ATOM   6043  C  CB  . SER F  1 68  ? 13.183  77.748  23.029  1.00 34.73 ? 68  SER F CB  1 
ATOM   6044  O  OG  . SER F  1 68  ? 12.342  76.732  22.501  1.00 41.66 ? 68  SER F OG  1 
ATOM   6045  N  N   . ARG F  1 69  ? 13.230  79.224  26.457  1.00 31.31 ? 69  ARG F N   1 
ATOM   6046  C  CA  . ARG F  1 69  ? 13.091  80.509  27.128  1.00 21.16 ? 69  ARG F CA  1 
ATOM   6047  C  C   . ARG F  1 69  ? 14.476  80.980  27.505  1.00 21.38 ? 69  ARG F C   1 
ATOM   6048  O  O   . ARG F  1 69  ? 15.465  80.281  27.265  1.00 24.09 ? 69  ARG F O   1 
ATOM   6049  C  CB  . ARG F  1 69  ? 12.190  80.399  28.363  1.00 29.61 ? 69  ARG F CB  1 
ATOM   6050  C  CG  . ARG F  1 69  ? 11.042  79.400  28.223  1.00 33.77 ? 69  ARG F CG  1 
ATOM   6051  C  CD  . ARG F  1 69  ? 9.732   80.032  27.736  1.00 30.78 ? 69  ARG F CD  1 
ATOM   6052  N  NE  . ARG F  1 69  ? 8.913   80.492  28.852  1.00 41.69 ? 69  ARG F NE  1 
ATOM   6053  C  CZ  . ARG F  1 69  ? 7.926   79.791  29.413  1.00 51.54 ? 69  ARG F CZ  1 
ATOM   6054  N  NH1 . ARG F  1 69  ? 7.610   78.587  28.954  1.00 52.23 ? 69  ARG F NH1 1 
ATOM   6055  N  NH2 . ARG F  1 69  ? 7.241   80.300  30.435  1.00 49.10 ? 69  ARG F NH2 1 
ATOM   6056  N  N   . LYS F  1 70  ? 14.564  82.177  28.067  1.00 22.61 ? 70  LYS F N   1 
ATOM   6057  C  CA  . LYS F  1 70  ? 15.852  82.705  28.509  1.00 23.65 ? 70  LYS F CA  1 
ATOM   6058  C  C   . LYS F  1 70  ? 16.220  82.101  29.865  1.00 24.41 ? 70  LYS F C   1 
ATOM   6059  O  O   . LYS F  1 70  ? 15.382  81.502  30.532  1.00 23.72 ? 70  LYS F O   1 
ATOM   6060  C  CB  . LYS F  1 70  ? 15.806  84.236  28.589  1.00 27.50 ? 70  LYS F CB  1 
ATOM   6061  C  CG  . LYS F  1 70  ? 15.565  84.929  27.230  1.00 33.31 ? 70  LYS F CG  1 
ATOM   6062  C  CD  . LYS F  1 70  ? 15.843  86.427  27.305  1.00 40.72 ? 70  LYS F CD  1 
ATOM   6063  C  CE  . LYS F  1 70  ? 15.776  87.102  25.929  1.00 51.49 ? 70  LYS F CE  1 
ATOM   6064  N  NZ  . LYS F  1 70  ? 14.381  87.399  25.470  1.00 45.65 ? 70  LYS F NZ  1 
ATOM   6065  N  N   . HIS F  1 71  ? 17.467  82.260  30.280  1.00 24.61 ? 71  HIS F N   1 
ATOM   6066  C  CA  . HIS F  1 71  ? 17.866  81.711  31.566  1.00 26.86 ? 71  HIS F CA  1 
ATOM   6067  C  C   . HIS F  1 71  ? 17.364  82.574  32.714  1.00 24.78 ? 71  HIS F C   1 
ATOM   6068  O  O   . HIS F  1 71  ? 17.586  83.793  32.722  1.00 19.51 ? 71  HIS F O   1 
ATOM   6069  C  CB  . HIS F  1 71  ? 19.384  81.615  31.649  1.00 21.66 ? 71  HIS F CB  1 
ATOM   6070  C  CG  . HIS F  1 71  ? 19.891  81.194  32.994  1.00 23.16 ? 71  HIS F CG  1 
ATOM   6071  N  ND1 . HIS F  1 71  ? 19.947  79.875  33.388  1.00 21.47 ? 71  HIS F ND1 1 
ATOM   6072  C  CD2 . HIS F  1 71  ? 20.390  81.918  34.025  1.00 20.32 ? 71  HIS F CD2 1 
ATOM   6073  C  CE1 . HIS F  1 71  ? 20.451  79.806  34.608  1.00 27.08 ? 71  HIS F CE1 1 
ATOM   6074  N  NE2 . HIS F  1 71  ? 20.742  81.032  35.011  1.00 24.52 ? 71  HIS F NE2 1 
ATOM   6075  N  N   . GLY F  1 72  ? 16.741  81.946  33.707  1.00 18.91 ? 72  GLY F N   1 
ATOM   6076  C  CA  . GLY F  1 72  ? 16.360  82.670  34.909  1.00 17.90 ? 72  GLY F CA  1 
ATOM   6077  C  C   . GLY F  1 72  ? 16.565  81.847  36.164  1.00 20.24 ? 72  GLY F C   1 
ATOM   6078  O  O   . GLY F  1 72  ? 17.180  80.789  36.123  1.00 24.31 ? 72  GLY F O   1 
ATOM   6079  N  N   . GLY F  1 73  ? 16.056  82.336  37.286  1.00 17.28 ? 73  GLY F N   1 
ATOM   6080  C  CA  . GLY F  1 73  ? 16.129  81.600  38.531  1.00 14.69 ? 73  GLY F CA  1 
ATOM   6081  C  C   . GLY F  1 73  ? 14.912  80.706  38.651  1.00 17.58 ? 73  GLY F C   1 
ATOM   6082  O  O   . GLY F  1 73  ? 13.974  80.807  37.854  1.00 14.74 ? 73  GLY F O   1 
ATOM   6083  N  N   . PRO F  1 74  ? 14.917  79.811  39.646  1.00 16.52 ? 74  PRO F N   1 
ATOM   6084  C  CA  . PRO F  1 74  ? 13.813  78.861  39.758  1.00 14.72 ? 74  PRO F CA  1 
ATOM   6085  C  C   . PRO F  1 74  ? 12.468  79.545  40.050  1.00 15.35 ? 74  PRO F C   1 
ATOM   6086  O  O   . PRO F  1 74  ? 11.438  78.974  39.718  1.00 14.22 ? 74  PRO F O   1 
ATOM   6087  C  CB  . PRO F  1 74  ? 14.241  77.957  40.913  1.00 13.36 ? 74  PRO F CB  1 
ATOM   6088  C  CG  . PRO F  1 74  ? 15.283  78.713  41.633  1.00 18.75 ? 74  PRO F CG  1 
ATOM   6089  C  CD  . PRO F  1 74  ? 15.970  79.568  40.638  1.00 14.50 ? 74  PRO F CD  1 
ATOM   6090  N  N   . LYS F  1 75  ? 12.488  80.740  40.635  1.00 14.72 ? 75  LYS F N   1 
ATOM   6091  C  CA  . LYS F  1 75  ? 11.258  81.447  40.969  1.00 19.04 ? 75  LYS F CA  1 
ATOM   6092  C  C   . LYS F  1 75  ? 10.689  82.241  39.785  1.00 20.55 ? 75  LYS F C   1 
ATOM   6093  O  O   . LYS F  1 75  ? 9.577   82.739  39.839  1.00 16.95 ? 75  LYS F O   1 
ATOM   6094  C  CB  . LYS F  1 75  ? 11.467  82.368  42.179  1.00 17.92 ? 75  LYS F CB  1 
ATOM   6095  C  CG  . LYS F  1 75  ? 12.066  81.671  43.380  1.00 18.57 ? 75  LYS F CG  1 
ATOM   6096  C  CD  . LYS F  1 75  ? 11.703  82.347  44.687  1.00 33.17 ? 75  LYS F CD  1 
ATOM   6097  C  CE  . LYS F  1 75  ? 12.458  83.642  44.934  1.00 29.99 ? 75  LYS F CE  1 
ATOM   6098  N  NZ  . LYS F  1 75  ? 11.823  84.373  46.087  1.00 25.21 ? 75  LYS F NZ  1 
ATOM   6099  N  N   . ASP F  1 76  ? 11.452  82.352  38.708  1.00 19.36 ? 76  ASP F N   1 
ATOM   6100  C  CA  . ASP F  1 76  ? 11.009  83.160  37.591  1.00 19.63 ? 76  ASP F CA  1 
ATOM   6101  C  C   . ASP F  1 76  ? 10.063  82.369  36.725  1.00 23.45 ? 76  ASP F C   1 
ATOM   6102  O  O   . ASP F  1 76  ? 10.212  81.153  36.570  1.00 21.11 ? 76  ASP F O   1 
ATOM   6103  C  CB  . ASP F  1 76  ? 12.209  83.626  36.764  1.00 19.46 ? 76  ASP F CB  1 
ATOM   6104  C  CG  . ASP F  1 76  ? 13.129  84.502  37.553  1.00 20.13 ? 76  ASP F CG  1 
ATOM   6105  O  OD1 . ASP F  1 76  ? 12.611  85.396  38.257  1.00 23.87 ? 76  ASP F OD1 1 
ATOM   6106  O  OD2 . ASP F  1 76  ? 14.357  84.282  37.507  1.00 21.79 ? 76  ASP F OD2 1 
ATOM   6107  N  N   . GLU F  1 77  ? 9.083   83.059  36.162  1.00 23.80 ? 77  GLU F N   1 
ATOM   6108  C  CA  . GLU F  1 77  ? 8.240   82.452  35.150  1.00 23.49 ? 77  GLU F CA  1 
ATOM   6109  C  C   . GLU F  1 77  ? 9.080   82.224  33.905  1.00 21.19 ? 77  GLU F C   1 
ATOM   6110  O  O   . GLU F  1 77  ? 8.917   81.234  33.205  1.00 24.09 ? 77  GLU F O   1 
ATOM   6111  C  CB  . GLU F  1 77  ? 7.056   83.359  34.835  1.00 24.23 ? 77  GLU F CB  1 
ATOM   6112  C  CG  . GLU F  1 77  ? 6.026   82.718  33.945  1.00 38.67 ? 77  GLU F CG  1 
ATOM   6113  C  CD  . GLU F  1 77  ? 4.659   83.352  34.115  1.00 50.27 ? 77  GLU F CD  1 
ATOM   6114  O  OE1 . GLU F  1 77  ? 4.478   84.149  35.064  1.00 43.81 ? 77  GLU F OE1 1 
ATOM   6115  O  OE2 . GLU F  1 77  ? 3.765   83.055  33.298  1.00 65.46 ? 77  GLU F OE2 1 
ATOM   6116  N  N   . GLU F  1 78  ? 9.995   83.142  33.631  1.00 20.57 ? 78  GLU F N   1 
ATOM   6117  C  CA  . GLU F  1 78  ? 10.878  82.993  32.477  1.00 18.46 ? 78  GLU F CA  1 
ATOM   6118  C  C   . GLU F  1 78  ? 12.174  82.298  32.884  1.00 17.41 ? 78  GLU F C   1 
ATOM   6119  O  O   . GLU F  1 78  ? 13.077  82.921  33.432  1.00 16.31 ? 78  GLU F O   1 
ATOM   6120  C  CB  . GLU F  1 78  ? 11.169  84.362  31.850  1.00 20.64 ? 78  GLU F CB  1 
ATOM   6121  C  CG  . GLU F  1 78  ? 12.176  84.355  30.699  1.00 19.19 ? 78  GLU F CG  1 
ATOM   6122  C  CD  . GLU F  1 78  ? 11.565  83.865  29.390  1.00 25.31 ? 78  GLU F CD  1 
ATOM   6123  O  OE1 . GLU F  1 78  ? 10.331  83.628  29.326  1.00 25.28 ? 78  GLU F OE1 1 
ATOM   6124  O  OE2 . GLU F  1 78  ? 12.334  83.710  28.421  1.00 28.78 ? 78  GLU F OE2 1 
ATOM   6125  N  N   . ARG F  1 79  ? 12.261  81.001  32.616  1.00 19.61 ? 79  ARG F N   1 
ATOM   6126  C  CA  . ARG F  1 79  ? 13.447  80.230  32.983  1.00 20.87 ? 79  ARG F CA  1 
ATOM   6127  C  C   . ARG F  1 79  ? 13.524  78.994  32.112  1.00 20.88 ? 79  ARG F C   1 
ATOM   6128  O  O   . ARG F  1 79  ? 12.523  78.606  31.525  1.00 21.46 ? 79  ARG F O   1 
ATOM   6129  C  CB  . ARG F  1 79  ? 13.311  79.770  34.425  1.00 15.39 ? 79  ARG F CB  1 
ATOM   6130  C  CG  . ARG F  1 79  ? 12.012  79.025  34.665  1.00 18.12 ? 79  ARG F CG  1 
ATOM   6131  C  CD  . ARG F  1 79  ? 11.928  78.431  36.078  1.00 18.49 ? 79  ARG F CD  1 
ATOM   6132  N  NE  . ARG F  1 79  ? 12.612  77.155  36.153  1.00 17.23 ? 79  ARG F NE  1 
ATOM   6133  C  CZ  . ARG F  1 79  ? 12.528  76.303  37.170  1.00 19.43 ? 79  ARG F CZ  1 
ATOM   6134  N  NH1 . ARG F  1 79  ? 11.786  76.579  38.248  1.00 12.96 ? 79  ARG F NH1 1 
ATOM   6135  N  NH2 . ARG F  1 79  ? 13.192  75.162  37.096  1.00 17.85 ? 79  ARG F NH2 1 
ATOM   6136  N  N   . HIS F  1 80  ? 14.682  78.335  32.059  1.00 21.01 ? 80  HIS F N   1 
ATOM   6137  C  CA  . HIS F  1 80  ? 14.687  76.984  31.504  1.00 21.98 ? 80  HIS F CA  1 
ATOM   6138  C  C   . HIS F  1 80  ? 14.009  76.038  32.489  1.00 23.27 ? 80  HIS F C   1 
ATOM   6139  O  O   . HIS F  1 80  ? 13.897  76.351  33.679  1.00 24.24 ? 80  HIS F O   1 
ATOM   6140  C  CB  . HIS F  1 80  ? 16.090  76.474  31.292  1.00 26.56 ? 80  HIS F CB  1 
ATOM   6141  C  CG  . HIS F  1 80  ? 16.992  77.441  30.605  1.00 26.63 ? 80  HIS F CG  1 
ATOM   6142  N  ND1 . HIS F  1 80  ? 18.244  77.740  31.091  1.00 16.08 ? 80  HIS F ND1 1 
ATOM   6143  C  CD2 . HIS F  1 80  ? 16.839  78.157  29.463  1.00 22.13 ? 80  HIS F CD2 1 
ATOM   6144  C  CE1 . HIS F  1 80  ? 18.821  78.610  30.275  1.00 27.98 ? 80  HIS F CE1 1 
ATOM   6145  N  NE2 . HIS F  1 80  ? 17.988  78.880  29.284  1.00 18.59 ? 80  HIS F NE2 1 
ATOM   6146  N  N   . VAL F  1 81  ? 13.575  74.880  32.007  1.00 20.29 ? 81  VAL F N   1 
ATOM   6147  C  CA  . VAL F  1 81  ? 13.164  73.826  32.913  1.00 23.72 ? 81  VAL F CA  1 
ATOM   6148  C  C   . VAL F  1 81  ? 14.311  73.475  33.851  1.00 20.17 ? 81  VAL F C   1 
ATOM   6149  O  O   . VAL F  1 81  ? 14.151  73.474  35.065  1.00 23.66 ? 81  VAL F O   1 
ATOM   6150  C  CB  . VAL F  1 81  ? 12.659  72.602  32.160  1.00 26.39 ? 81  VAL F CB  1 
ATOM   6151  C  CG1 . VAL F  1 81  ? 12.425  71.464  33.129  1.00 23.74 ? 81  VAL F CG1 1 
ATOM   6152  C  CG2 . VAL F  1 81  ? 11.374  72.954  31.435  1.00 23.43 ? 81  VAL F CG2 1 
ATOM   6153  N  N   . GLY F  1 82  ? 15.493  73.274  33.299  1.00 18.19 ? 82  GLY F N   1 
ATOM   6154  C  CA  . GLY F  1 82  ? 16.631  72.869  34.088  1.00 15.48 ? 82  GLY F CA  1 
ATOM   6155  C  C   . GLY F  1 82  ? 17.180  73.906  35.040  1.00 17.81 ? 82  GLY F C   1 
ATOM   6156  O  O   . GLY F  1 82  ? 18.239  73.691  35.616  1.00 12.84 ? 82  GLY F O   1 
ATOM   6157  N  N   . ASP F  1 83  ? 16.483  75.026  35.225  1.00 14.90 ? 83  ASP F N   1 
ATOM   6158  C  CA  . ASP F  1 83  ? 17.051  76.107  36.028  1.00 16.12 ? 83  ASP F CA  1 
ATOM   6159  C  C   . ASP F  1 83  ? 16.708  75.959  37.522  1.00 18.79 ? 83  ASP F C   1 
ATOM   6160  O  O   . ASP F  1 83  ? 15.633  76.378  37.959  1.00 15.45 ? 83  ASP F O   1 
ATOM   6161  C  CB  . ASP F  1 83  ? 16.546  77.470  35.534  1.00 22.84 ? 83  ASP F CB  1 
ATOM   6162  C  CG  . ASP F  1 83  ? 17.201  77.924  34.231  1.00 25.43 ? 83  ASP F CG  1 
ATOM   6163  O  OD1 . ASP F  1 83  ? 17.968  77.151  33.625  1.00 33.02 ? 83  ASP F OD1 1 
ATOM   6164  O  OD2 . ASP F  1 83  ? 16.949  79.069  33.809  1.00 22.71 ? 83  ASP F OD2 1 
ATOM   6165  N  N   . LEU F  1 84  ? 17.615  75.397  38.312  1.00 16.59 ? 84  LEU F N   1 
ATOM   6166  C  CA  . LEU F  1 84  ? 17.348  75.239  39.740  1.00 13.13 ? 84  LEU F CA  1 
ATOM   6167  C  C   . LEU F  1 84  ? 18.048  76.280  40.597  1.00 16.47 ? 84  LEU F C   1 
ATOM   6168  O  O   . LEU F  1 84  ? 17.944  76.255  41.823  1.00 12.55 ? 84  LEU F O   1 
ATOM   6169  C  CB  . LEU F  1 84  ? 17.691  73.830  40.205  1.00 10.67 ? 84  LEU F CB  1 
ATOM   6170  C  CG  . LEU F  1 84  ? 16.889  72.759  39.465  1.00 14.26 ? 84  LEU F CG  1 
ATOM   6171  C  CD1 . LEU F  1 84  ? 17.384  71.362  39.810  1.00 13.92 ? 84  LEU F CD1 1 
ATOM   6172  C  CD2 . LEU F  1 84  ? 15.373  72.899  39.725  1.00 9.22  ? 84  LEU F CD2 1 
ATOM   6173  N  N   . GLY F  1 85  ? 18.726  77.224  39.958  1.00 14.40 ? 85  GLY F N   1 
ATOM   6174  C  CA  . GLY F  1 85  ? 19.372  78.294  40.699  1.00 14.55 ? 85  GLY F CA  1 
ATOM   6175  C  C   . GLY F  1 85  ? 20.676  77.871  41.333  1.00 17.40 ? 85  GLY F C   1 
ATOM   6176  O  O   . GLY F  1 85  ? 21.525  77.295  40.671  1.00 22.17 ? 85  GLY F O   1 
ATOM   6177  N  N   . ASN F  1 86  ? 20.821  78.154  42.622  1.00 16.67 ? 86  ASN F N   1 
ATOM   6178  C  CA  . ASN F  1 86  ? 22.039  77.881  43.365  1.00 15.42 ? 86  ASN F CA  1 
ATOM   6179  C  C   . ASN F  1 86  ? 21.842  76.908  44.542  1.00 19.38 ? 86  ASN F C   1 
ATOM   6180  O  O   . ASN F  1 86  ? 20.746  76.792  45.099  1.00 17.67 ? 86  ASN F O   1 
ATOM   6181  C  CB  . ASN F  1 86  ? 22.588  79.193  43.926  1.00 15.13 ? 86  ASN F CB  1 
ATOM   6182  C  CG  . ASN F  1 86  ? 23.085  80.139  42.836  1.00 22.40 ? 86  ASN F CG  1 
ATOM   6183  O  OD1 . ASN F  1 86  ? 23.794  79.722  41.913  1.00 17.67 ? 86  ASN F OD1 1 
ATOM   6184  N  ND2 . ASN F  1 86  ? 22.710  81.416  42.936  1.00 14.57 ? 86  ASN F ND2 1 
ATOM   6185  N  N   . VAL F  1 87  ? 22.915  76.221  44.922  1.00 17.96 ? 87  VAL F N   1 
ATOM   6186  C  CA  . VAL F  1 87  ? 22.976  75.538  46.202  1.00 16.71 ? 87  VAL F CA  1 
ATOM   6187  C  C   . VAL F  1 87  ? 24.130  76.157  46.956  1.00 18.70 ? 87  VAL F C   1 
ATOM   6188  O  O   . VAL F  1 87  ? 24.977  76.796  46.365  1.00 21.40 ? 87  VAL F O   1 
ATOM   6189  C  CB  . VAL F  1 87  ? 23.194  74.031  46.056  1.00 17.66 ? 87  VAL F CB  1 
ATOM   6190  C  CG1 . VAL F  1 87  ? 22.065  73.413  45.266  1.00 12.88 ? 87  VAL F CG1 1 
ATOM   6191  C  CG2 . VAL F  1 87  ? 24.542  73.739  45.413  1.00 20.33 ? 87  VAL F CG2 1 
ATOM   6192  N  N   . THR F  1 88  ? 24.149  75.979  48.269  1.00 21.19 ? 88  THR F N   1 
ATOM   6193  C  CA  . THR F  1 88  ? 25.103  76.654  49.122  1.00 18.91 ? 88  THR F CA  1 
ATOM   6194  C  C   . THR F  1 88  ? 25.973  75.677  49.904  1.00 23.11 ? 88  THR F C   1 
ATOM   6195  O  O   . THR F  1 88  ? 25.468  74.756  50.530  1.00 24.03 ? 88  THR F O   1 
ATOM   6196  C  CB  . THR F  1 88  ? 24.371  77.554  50.097  1.00 17.34 ? 88  THR F CB  1 
ATOM   6197  O  OG1 . THR F  1 88  ? 23.752  78.601  49.359  1.00 20.29 ? 88  THR F OG1 1 
ATOM   6198  C  CG2 . THR F  1 88  ? 25.331  78.173  51.079  1.00 25.96 ? 88  THR F CG2 1 
ATOM   6199  N  N   . ALA F  1 89  ? 27.285  75.881  49.859  1.00 24.78 ? 89  ALA F N   1 
ATOM   6200  C  CA  . ALA F  1 89  ? 28.211  75.089  50.656  1.00 21.69 ? 89  ALA F CA  1 
ATOM   6201  C  C   . ALA F  1 89  ? 28.493  75.827  51.937  1.00 26.46 ? 89  ALA F C   1 
ATOM   6202  O  O   . ALA F  1 89  ? 28.546  77.062  51.932  1.00 24.43 ? 89  ALA F O   1 
ATOM   6203  C  CB  . ALA F  1 89  ? 29.485  74.875  49.900  1.00 27.09 ? 89  ALA F CB  1 
ATOM   6204  N  N   . ASP F  1 90  ? 28.649  75.085  53.040  1.00 25.16 ? 90  ASP F N   1 
ATOM   6205  C  CA  . ASP F  1 90  ? 28.987  75.697  54.323  1.00 27.55 ? 90  ASP F CA  1 
ATOM   6206  C  C   . ASP F  1 90  ? 30.502  75.827  54.506  1.00 27.60 ? 90  ASP F C   1 
ATOM   6207  O  O   . ASP F  1 90  ? 31.278  75.512  53.600  1.00 21.54 ? 90  ASP F O   1 
ATOM   6208  C  CB  . ASP F  1 90  ? 28.365  74.927  55.507  1.00 26.45 ? 90  ASP F CB  1 
ATOM   6209  C  CG  . ASP F  1 90  ? 28.816  73.465  55.575  1.00 29.76 ? 90  ASP F CG  1 
ATOM   6210  O  OD1 . ASP F  1 90  ? 29.851  73.104  54.966  1.00 27.46 ? 90  ASP F OD1 1 
ATOM   6211  O  OD2 . ASP F  1 90  ? 28.121  72.667  56.250  1.00 26.88 ? 90  ASP F OD2 1 
ATOM   6212  N  N   . LYS F  1 91  ? 30.906  76.256  55.700  1.00 29.95 ? 91  LYS F N   1 
ATOM   6213  C  CA  . LYS F  1 91  ? 32.325  76.415  56.043  1.00 34.68 ? 91  LYS F CA  1 
ATOM   6214  C  C   . LYS F  1 91  ? 33.159  75.146  55.796  1.00 35.32 ? 91  LYS F C   1 
ATOM   6215  O  O   . LYS F  1 91  ? 34.348  75.227  55.500  1.00 36.11 ? 91  LYS F O   1 
ATOM   6216  C  CB  . LYS F  1 91  ? 32.465  76.855  57.499  1.00 38.29 ? 91  LYS F CB  1 
ATOM   6217  C  CG  . LYS F  1 91  ? 33.762  77.583  57.823  1.00 48.22 ? 91  LYS F CG  1 
ATOM   6218  C  CD  . LYS F  1 91  ? 33.625  79.102  57.675  1.00 46.97 ? 91  LYS F CD  1 
ATOM   6219  C  CE  . LYS F  1 91  ? 34.860  79.826  58.219  1.00 45.60 ? 91  LYS F CE  1 
ATOM   6220  N  NZ  . LYS F  1 91  ? 34.707  81.320  58.226  1.00 38.91 ? 91  LYS F NZ  1 
ATOM   6221  N  N   . ASP F  1 92  ? 32.526  73.980  55.891  1.00 32.13 ? 92  ASP F N   1 
ATOM   6222  C  CA  . ASP F  1 92  ? 33.219  72.708  55.714  1.00 29.43 ? 92  ASP F CA  1 
ATOM   6223  C  C   . ASP F  1 92  ? 33.111  72.219  54.279  1.00 27.73 ? 92  ASP F C   1 
ATOM   6224  O  O   . ASP F  1 92  ? 33.486  71.090  53.961  1.00 28.53 ? 92  ASP F O   1 
ATOM   6225  C  CB  . ASP F  1 92  ? 32.654  71.646  56.669  1.00 32.09 ? 92  ASP F CB  1 
ATOM   6226  C  CG  . ASP F  1 92  ? 32.794  72.032  58.137  1.00 37.27 ? 92  ASP F CG  1 
ATOM   6227  O  OD1 . ASP F  1 92  ? 33.890  72.475  58.527  1.00 40.33 ? 92  ASP F OD1 1 
ATOM   6228  O  OD2 . ASP F  1 92  ? 31.808  71.895  58.905  1.00 41.37 ? 92  ASP F OD2 1 
ATOM   6229  N  N   . GLY F  1 93  ? 32.567  73.061  53.409  1.00 31.24 ? 93  GLY F N   1 
ATOM   6230  C  CA  . GLY F  1 93  ? 32.484  72.726  51.998  1.00 24.11 ? 93  GLY F CA  1 
ATOM   6231  C  C   . GLY F  1 93  ? 31.322  71.836  51.596  1.00 24.50 ? 93  GLY F C   1 
ATOM   6232  O  O   . GLY F  1 93  ? 31.315  71.247  50.508  1.00 19.39 ? 93  GLY F O   1 
ATOM   6233  N  N   . VAL F  1 94  ? 30.329  71.733  52.471  1.00 24.22 ? 94  VAL F N   1 
ATOM   6234  C  CA  . VAL F  1 94  ? 29.242  70.785  52.251  1.00 22.40 ? 94  VAL F CA  1 
ATOM   6235  C  C   . VAL F  1 94  ? 27.965  71.514  51.834  1.00 19.18 ? 94  VAL F C   1 
ATOM   6236  O  O   . VAL F  1 94  ? 27.535  72.444  52.503  1.00 20.91 ? 94  VAL F O   1 
ATOM   6237  C  CB  . VAL F  1 94  ? 28.974  69.943  53.535  1.00 25.52 ? 94  VAL F CB  1 
ATOM   6238  C  CG1 . VAL F  1 94  ? 27.683  69.130  53.396  1.00 25.51 ? 94  VAL F CG1 1 
ATOM   6239  C  CG2 . VAL F  1 94  ? 30.153  69.027  53.821  1.00 23.86 ? 94  VAL F CG2 1 
ATOM   6240  N  N   . ALA F  1 95  ? 27.378  71.110  50.718  1.00 17.70 ? 95  ALA F N   1 
ATOM   6241  C  CA  . ALA F  1 95  ? 26.073  71.630  50.329  1.00 19.96 ? 95  ALA F CA  1 
ATOM   6242  C  C   . ALA F  1 95  ? 24.997  70.607  50.693  1.00 17.07 ? 95  ALA F C   1 
ATOM   6243  O  O   . ALA F  1 95  ? 24.912  69.550  50.071  1.00 14.98 ? 95  ALA F O   1 
ATOM   6244  C  CB  . ALA F  1 95  ? 26.029  71.928  48.843  1.00 16.47 ? 95  ALA F CB  1 
ATOM   6245  N  N   . ASP F  1 96  ? 24.203  70.929  51.710  1.00 14.51 ? 96  ASP F N   1 
ATOM   6246  C  CA  . ASP F  1 96  ? 23.043  70.124  52.095  1.00 18.13 ? 96  ASP F CA  1 
ATOM   6247  C  C   . ASP F  1 96  ? 21.843  70.616  51.267  1.00 15.53 ? 96  ASP F C   1 
ATOM   6248  O  O   . ASP F  1 96  ? 21.050  71.455  51.703  1.00 15.26 ? 96  ASP F O   1 
ATOM   6249  C  CB  . ASP F  1 96  ? 22.766  70.253  53.605  1.00 16.02 ? 96  ASP F CB  1 
ATOM   6250  C  CG  . ASP F  1 96  ? 23.848  69.563  54.485  1.00 21.05 ? 96  ASP F CG  1 
ATOM   6251  O  OD1 . ASP F  1 96  ? 24.309  68.458  54.145  1.00 19.67 ? 96  ASP F OD1 1 
ATOM   6252  O  OD2 . ASP F  1 96  ? 24.230  70.130  55.529  1.00 21.53 ? 96  ASP F OD2 1 
ATOM   6253  N  N   . VAL F  1 97  ? 21.734  70.099  50.060  1.00 13.93 ? 97  VAL F N   1 
ATOM   6254  C  CA  . VAL F  1 97  ? 20.776  70.606  49.102  1.00 15.09 ? 97  VAL F CA  1 
ATOM   6255  C  C   . VAL F  1 97  ? 19.344  70.388  49.572  1.00 16.86 ? 97  VAL F C   1 
ATOM   6256  O  O   . VAL F  1 97  ? 18.991  69.309  50.008  1.00 16.58 ? 97  VAL F O   1 
ATOM   6257  C  CB  . VAL F  1 97  ? 20.980  69.934  47.750  1.00 16.45 ? 97  VAL F CB  1 
ATOM   6258  C  CG1 . VAL F  1 97  ? 20.004  70.491  46.700  1.00 15.72 ? 97  VAL F CG1 1 
ATOM   6259  C  CG2 . VAL F  1 97  ? 22.435  70.112  47.306  1.00 16.16 ? 97  VAL F CG2 1 
ATOM   6260  N  N   . SER F  1 98  ? 18.538  71.434  49.489  1.00 13.50 ? 98  SER F N   1 
ATOM   6261  C  CA  . SER F  1 98  ? 17.127  71.331  49.788  1.00 14.92 ? 98  SER F CA  1 
ATOM   6262  C  C   . SER F  1 98  ? 16.348  72.226  48.826  1.00 15.05 ? 98  SER F C   1 
ATOM   6263  O  O   . SER F  1 98  ? 16.305  73.448  48.981  1.00 14.44 ? 98  SER F O   1 
ATOM   6264  C  CB  . SER F  1 98  ? 16.841  71.720  51.239  1.00 17.80 ? 98  SER F CB  1 
ATOM   6265  O  OG  . SER F  1 98  ? 15.525  71.348  51.596  1.00 20.95 ? 98  SER F OG  1 
ATOM   6266  N  N   . ILE F  1 99  ? 15.744  71.614  47.819  1.00 13.12 ? 99  ILE F N   1 
ATOM   6267  C  CA  . ILE F  1 99  ? 14.990  72.373  46.819  1.00 14.11 ? 99  ILE F CA  1 
ATOM   6268  C  C   . ILE F  1 99  ? 13.635  71.737  46.559  1.00 13.87 ? 99  ILE F C   1 
ATOM   6269  O  O   . ILE F  1 99  ? 13.499  70.513  46.564  1.00 14.68 ? 99  ILE F O   1 
ATOM   6270  C  CB  . ILE F  1 99  ? 15.793  72.488  45.497  1.00 16.48 ? 99  ILE F CB  1 
ATOM   6271  C  CG1 . ILE F  1 99  ? 16.993  73.417  45.705  1.00 18.12 ? 99  ILE F CG1 1 
ATOM   6272  C  CG2 . ILE F  1 99  ? 14.933  73.001  44.360  1.00 12.20 ? 99  ILE F CG2 1 
ATOM   6273  C  CD1 . ILE F  1 99  ? 18.054  73.285  44.649  1.00 18.96 ? 99  ILE F CD1 1 
ATOM   6274  N  N   . GLU F  1 100 ? 12.623  72.572  46.382  1.00 11.93 ? 100 GLU F N   1 
ATOM   6275  C  CA  . GLU F  1 100 ? 11.356  72.096  45.878  1.00 17.40 ? 100 GLU F CA  1 
ATOM   6276  C  C   . GLU F  1 100 ? 11.063  72.839  44.595  1.00 16.75 ? 100 GLU F C   1 
ATOM   6277  O  O   . GLU F  1 100 ? 11.126  74.055  44.562  1.00 14.73 ? 100 GLU F O   1 
ATOM   6278  C  CB  . GLU F  1 100 ? 10.230  72.339  46.881  1.00 15.81 ? 100 GLU F CB  1 
ATOM   6279  C  CG  . GLU F  1 100 ? 8.944   71.664  46.460  1.00 19.39 ? 100 GLU F CG  1 
ATOM   6280  C  CD  . GLU F  1 100 ? 7.930   71.526  47.609  1.00 27.46 ? 100 GLU F CD  1 
ATOM   6281  O  OE1 . GLU F  1 100 ? 8.328   71.319  48.777  1.00 30.80 ? 100 GLU F OE1 1 
ATOM   6282  O  OE2 . GLU F  1 100 ? 6.728   71.626  47.331  1.00 27.80 ? 100 GLU F OE2 1 
ATOM   6283  N  N   . ASP F  1 101 ? 10.746  72.119  43.533  1.00 15.31 ? 101 ASP F N   1 
ATOM   6284  C  CA  . ASP F  1 101 ? 10.508  72.797  42.263  1.00 17.02 ? 101 ASP F CA  1 
ATOM   6285  C  C   . ASP F  1 101 ? 9.334   72.206  41.507  1.00 18.80 ? 101 ASP F C   1 
ATOM   6286  O  O   . ASP F  1 101 ? 9.201   70.986  41.412  1.00 21.91 ? 101 ASP F O   1 
ATOM   6287  C  CB  . ASP F  1 101 ? 11.761  72.778  41.381  1.00 16.00 ? 101 ASP F CB  1 
ATOM   6288  C  CG  . ASP F  1 101 ? 11.633  73.705  40.174  1.00 19.61 ? 101 ASP F CG  1 
ATOM   6289  O  OD1 . ASP F  1 101 ? 11.896  74.911  40.347  1.00 17.00 ? 101 ASP F OD1 1 
ATOM   6290  O  OD2 . ASP F  1 101 ? 11.251  73.238  39.073  1.00 16.59 ? 101 ASP F OD2 1 
ATOM   6291  N  N   . SER F  1 102 ? 8.488   73.068  40.954  1.00 18.85 ? 102 SER F N   1 
ATOM   6292  C  CA  . SER F  1 102 ? 7.324   72.579  40.210  1.00 21.62 ? 102 SER F CA  1 
ATOM   6293  C  C   . SER F  1 102 ? 7.466   72.661  38.709  1.00 20.21 ? 102 SER F C   1 
ATOM   6294  O  O   . SER F  1 102 ? 6.528   72.329  37.991  1.00 21.81 ? 102 SER F O   1 
ATOM   6295  C  CB  . SER F  1 102 ? 6.047   73.299  40.645  1.00 19.20 ? 102 SER F CB  1 
ATOM   6296  O  OG  . SER F  1 102 ? 5.618   72.792  41.896  1.00 23.46 ? 102 SER F OG  1 
ATOM   6297  N  N   . VAL F  1 103 ? 8.625   73.098  38.226  1.00 18.20 ? 103 VAL F N   1 
ATOM   6298  C  CA  . VAL F  1 103 ? 8.832   73.149  36.785  1.00 20.20 ? 103 VAL F CA  1 
ATOM   6299  C  C   . VAL F  1 103 ? 9.405   71.825  36.284  1.00 23.58 ? 103 VAL F C   1 
ATOM   6300  O  O   . VAL F  1 103 ? 8.855   71.224  35.367  1.00 23.21 ? 103 VAL F O   1 
ATOM   6301  C  CB  . VAL F  1 103 ? 9.714   74.340  36.366  1.00 20.53 ? 103 VAL F CB  1 
ATOM   6302  C  CG1 . VAL F  1 103 ? 10.025  74.286  34.889  1.00 21.60 ? 103 VAL F CG1 1 
ATOM   6303  C  CG2 . VAL F  1 103 ? 9.016   75.651  36.714  1.00 22.56 ? 103 VAL F CG2 1 
ATOM   6304  N  N   . ILE F  1 104 ? 10.494  71.359  36.893  1.00 21.20 ? 104 ILE F N   1 
ATOM   6305  C  CA  . ILE F  1 104 ? 10.993  70.025  36.581  1.00 19.26 ? 104 ILE F CA  1 
ATOM   6306  C  C   . ILE F  1 104 ? 9.916   68.988  36.899  1.00 23.29 ? 104 ILE F C   1 
ATOM   6307  O  O   . ILE F  1 104 ? 9.030   69.218  37.733  1.00 22.42 ? 104 ILE F O   1 
ATOM   6308  C  CB  . ILE F  1 104 ? 12.297  69.676  37.346  1.00 19.18 ? 104 ILE F CB  1 
ATOM   6309  C  CG1 . ILE F  1 104 ? 12.096  69.774  38.857  1.00 16.65 ? 104 ILE F CG1 1 
ATOM   6310  C  CG2 . ILE F  1 104 ? 13.431  70.577  36.938  1.00 14.74 ? 104 ILE F CG2 1 
ATOM   6311  C  CD1 . ILE F  1 104 ? 13.336  69.408  39.644  1.00 17.56 ? 104 ILE F CD1 1 
ATOM   6312  N  N   . SER F  1 105 ? 9.972   67.853  36.217  1.00 24.52 ? 105 SER F N   1 
ATOM   6313  C  CA  . SER F  1 105 ? 9.081   66.745  36.518  1.00 21.85 ? 105 SER F CA  1 
ATOM   6314  C  C   . SER F  1 105 ? 9.883   65.456  36.371  1.00 26.05 ? 105 SER F C   1 
ATOM   6315  O  O   . SER F  1 105 ? 11.003  65.475  35.846  1.00 23.09 ? 105 SER F O   1 
ATOM   6316  C  CB  . SER F  1 105 ? 7.874   66.748  35.574  1.00 28.16 ? 105 SER F CB  1 
ATOM   6317  O  OG  . SER F  1 105 ? 6.861   65.848  35.995  1.00 21.99 ? 105 SER F OG  1 
ATOM   6318  N  N   . LEU F  1 106 ? 9.321   64.349  36.849  1.00 24.40 ? 106 LEU F N   1 
ATOM   6319  C  CA  . LEU F  1 106 ? 9.943   63.047  36.659  1.00 29.52 ? 106 LEU F CA  1 
ATOM   6320  C  C   . LEU F  1 106 ? 9.118   62.218  35.683  1.00 32.83 ? 106 LEU F C   1 
ATOM   6321  O  O   . LEU F  1 106 ? 9.316   61.010  35.555  1.00 36.28 ? 106 LEU F O   1 
ATOM   6322  C  CB  . LEU F  1 106 ? 10.094  62.305  37.985  1.00 24.60 ? 106 LEU F CB  1 
ATOM   6323  C  CG  . LEU F  1 106 ? 10.890  63.018  39.075  1.00 20.16 ? 106 LEU F CG  1 
ATOM   6324  C  CD1 . LEU F  1 106 ? 10.746  62.255  40.383  1.00 23.56 ? 106 LEU F CD1 1 
ATOM   6325  C  CD2 . LEU F  1 106 ? 12.349  63.146  38.668  1.00 17.89 ? 106 LEU F CD2 1 
ATOM   6326  N  N   . SER F  1 107 ? 8.180   62.878  35.015  1.00 31.78 ? 107 SER F N   1 
ATOM   6327  C  CA  . SER F  1 107 ? 7.436   62.282  33.911  1.00 33.18 ? 107 SER F CA  1 
ATOM   6328  C  C   . SER F  1 107 ? 6.922   63.393  33.001  1.00 38.90 ? 107 SER F C   1 
ATOM   6329  O  O   . SER F  1 107 ? 6.799   64.542  33.433  1.00 37.23 ? 107 SER F O   1 
ATOM   6330  C  CB  . SER F  1 107 ? 6.266   61.463  34.425  1.00 31.04 ? 107 SER F CB  1 
ATOM   6331  O  OG  . SER F  1 107 ? 5.197   62.312  34.787  1.00 40.64 ? 107 SER F OG  1 
ATOM   6332  N  N   . GLY F  1 108 ? 6.631   63.052  31.746  1.00 32.83 ? 108 GLY F N   1 
ATOM   6333  C  CA  . GLY F  1 108 ? 6.031   63.994  30.816  1.00 36.43 ? 108 GLY F CA  1 
ATOM   6334  C  C   . GLY F  1 108 ? 7.047   64.853  30.096  1.00 32.74 ? 108 GLY F C   1 
ATOM   6335  O  O   . GLY F  1 108 ? 8.242   64.598  30.180  1.00 31.86 ? 108 GLY F O   1 
ATOM   6336  N  N   . ASP F  1 109 ? 6.573   65.883  29.401  1.00 35.66 ? 109 ASP F N   1 
ATOM   6337  C  CA  . ASP F  1 109 ? 7.439   66.764  28.616  1.00 33.22 ? 109 ASP F CA  1 
ATOM   6338  C  C   . ASP F  1 109 ? 8.569   67.404  29.418  1.00 35.61 ? 109 ASP F C   1 
ATOM   6339  O  O   . ASP F  1 109 ? 9.597   67.770  28.866  1.00 30.42 ? 109 ASP F O   1 
ATOM   6340  C  CB  . ASP F  1 109 ? 6.599   67.875  27.984  1.00 42.11 ? 109 ASP F CB  1 
ATOM   6341  C  CG  . ASP F  1 109 ? 5.434   67.335  27.161  1.00 48.15 ? 109 ASP F CG  1 
ATOM   6342  O  OD1 . ASP F  1 109 ? 5.203   66.106  27.168  1.00 49.72 ? 109 ASP F OD1 1 
ATOM   6343  O  OD2 . ASP F  1 109 ? 4.729   68.147  26.522  1.00 49.31 ? 109 ASP F OD2 1 
ATOM   6344  N  N   . HIS F  1 110 ? 8.378   67.560  30.723  1.00 38.08 ? 110 HIS F N   1 
ATOM   6345  C  CA  . HIS F  1 110 ? 9.400   68.212  31.540  1.00 33.81 ? 110 HIS F CA  1 
ATOM   6346  C  C   . HIS F  1 110 ? 10.288  67.215  32.297  1.00 32.79 ? 110 HIS F C   1 
ATOM   6347  O  O   . HIS F  1 110 ? 11.072  67.607  33.175  1.00 28.36 ? 110 HIS F O   1 
ATOM   6348  C  CB  . HIS F  1 110 ? 8.757   69.214  32.510  1.00 33.84 ? 110 HIS F CB  1 
ATOM   6349  C  CG  . HIS F  1 110 ? 8.065   70.357  31.829  1.00 42.85 ? 110 HIS F CG  1 
ATOM   6350  N  ND1 . HIS F  1 110 ? 6.994   71.021  32.392  1.00 43.81 ? 110 HIS F ND1 1 
ATOM   6351  C  CD2 . HIS F  1 110 ? 8.290   70.953  30.633  1.00 40.94 ? 110 HIS F CD2 1 
ATOM   6352  C  CE1 . HIS F  1 110 ? 6.590   71.974  31.571  1.00 43.46 ? 110 HIS F CE1 1 
ATOM   6353  N  NE2 . HIS F  1 110 ? 7.359   71.955  30.498  1.00 42.70 ? 110 HIS F NE2 1 
ATOM   6354  N  N   . CYS F  1 111 ? 10.172  65.938  31.934  1.00 31.61 ? 111 CYS F N   1 
ATOM   6355  C  CA  . CYS F  1 111 ? 10.895  64.858  32.604  1.00 30.20 ? 111 CYS F CA  1 
ATOM   6356  C  C   . CYS F  1 111 ? 12.397  65.052  32.540  1.00 29.00 ? 111 CYS F C   1 
ATOM   6357  O  O   . CYS F  1 111 ? 12.934  65.293  31.472  1.00 28.13 ? 111 CYS F O   1 
ATOM   6358  C  CB  . CYS F  1 111 ? 10.529  63.500  31.997  1.00 36.39 ? 111 CYS F CB  1 
ATOM   6359  S  SG  . CYS F  1 111 ? 11.092  62.069  32.967  1.00 40.73 ? 111 CYS F SG  1 
ATOM   6360  N  N   . ILE F  1 112 ? 13.068  64.946  33.688  1.00 24.88 ? 112 ILE F N   1 
ATOM   6361  C  CA  . ILE F  1 112 ? 14.511  65.159  33.753  1.00 24.59 ? 112 ILE F CA  1 
ATOM   6362  C  C   . ILE F  1 112 ? 15.299  63.865  33.948  1.00 25.69 ? 112 ILE F C   1 
ATOM   6363  O  O   . ILE F  1 112 ? 16.512  63.887  34.153  1.00 24.79 ? 112 ILE F O   1 
ATOM   6364  C  CB  . ILE F  1 112 ? 14.902  66.144  34.874  1.00 25.68 ? 112 ILE F CB  1 
ATOM   6365  C  CG1 . ILE F  1 112 ? 14.507  65.590  36.247  1.00 25.26 ? 112 ILE F CG1 1 
ATOM   6366  C  CG2 . ILE F  1 112 ? 14.272  67.519  34.629  1.00 22.64 ? 112 ILE F CG2 1 
ATOM   6367  C  CD1 . ILE F  1 112 ? 15.028  66.432  37.388  1.00 19.40 ? 112 ILE F CD1 1 
ATOM   6368  N  N   . ILE F  1 113 ? 14.598  62.744  33.895  1.00 26.33 ? 113 ILE F N   1 
ATOM   6369  C  CA  . ILE F  1 113 ? 15.228  61.449  34.008  1.00 29.85 ? 113 ILE F CA  1 
ATOM   6370  C  C   . ILE F  1 113 ? 15.939  61.151  32.688  1.00 36.34 ? 113 ILE F C   1 
ATOM   6371  O  O   . ILE F  1 113 ? 15.320  61.162  31.618  1.00 33.63 ? 113 ILE F O   1 
ATOM   6372  C  CB  . ILE F  1 113 ? 14.176  60.372  34.335  1.00 30.88 ? 113 ILE F CB  1 
ATOM   6373  C  CG1 . ILE F  1 113 ? 13.776  60.474  35.814  1.00 30.98 ? 113 ILE F CG1 1 
ATOM   6374  C  CG2 . ILE F  1 113 ? 14.712  58.983  34.021  1.00 30.51 ? 113 ILE F CG2 1 
ATOM   6375  C  CD1 . ILE F  1 113 ? 12.539  59.670  36.181  1.00 31.65 ? 113 ILE F CD1 1 
ATOM   6376  N  N   . GLY F  1 114 ? 17.243  60.912  32.764  1.00 31.97 ? 114 GLY F N   1 
ATOM   6377  C  CA  . GLY F  1 114 ? 18.037  60.661  31.578  1.00 34.80 ? 114 GLY F CA  1 
ATOM   6378  C  C   . GLY F  1 114 ? 18.919  61.850  31.275  1.00 36.79 ? 114 GLY F C   1 
ATOM   6379  O  O   . GLY F  1 114 ? 19.660  61.871  30.289  1.00 33.95 ? 114 GLY F O   1 
ATOM   6380  N  N   . ARG F  1 115 ? 18.859  62.852  32.141  1.00 31.23 ? 115 ARG F N   1 
ATOM   6381  C  CA  . ARG F  1 115 ? 19.548  64.091  31.843  1.00 30.72 ? 115 ARG F CA  1 
ATOM   6382  C  C   . ARG F  1 115 ? 20.672  64.284  32.825  1.00 32.54 ? 115 ARG F C   1 
ATOM   6383  O  O   . ARG F  1 115 ? 20.836  63.467  33.722  1.00 34.73 ? 115 ARG F O   1 
ATOM   6384  C  CB  . ARG F  1 115 ? 18.556  65.241  31.826  1.00 31.13 ? 115 ARG F CB  1 
ATOM   6385  C  CG  . ARG F  1 115 ? 17.389  64.948  30.896  1.00 26.19 ? 115 ARG F CG  1 
ATOM   6386  C  CD  . ARG F  1 115 ? 16.743  66.231  30.414  1.00 30.76 ? 115 ARG F CD  1 
ATOM   6387  N  NE  . ARG F  1 115 ? 15.598  65.992  29.537  1.00 25.90 ? 115 ARG F NE  1 
ATOM   6388  C  CZ  . ARG F  1 115 ? 15.712  65.888  28.219  1.00 31.09 ? 115 ARG F CZ  1 
ATOM   6389  N  NH1 . ARG F  1 115 ? 16.916  65.997  27.660  1.00 25.40 ? 115 ARG F NH1 1 
ATOM   6390  N  NH2 . ARG F  1 115 ? 14.639  65.674  27.470  1.00 25.02 ? 115 ARG F NH2 1 
ATOM   6391  N  N   . THR F  1 116 ? 21.485  65.316  32.641  1.00 30.92 ? 116 THR F N   1 
ATOM   6392  C  CA  . THR F  1 116 ? 22.623  65.492  33.524  1.00 29.66 ? 116 THR F CA  1 
ATOM   6393  C  C   . THR F  1 116 ? 22.352  66.595  34.511  1.00 34.23 ? 116 THR F C   1 
ATOM   6394  O  O   . THR F  1 116 ? 21.724  67.602  34.174  1.00 31.04 ? 116 THR F O   1 
ATOM   6395  C  CB  . THR F  1 116 ? 23.922  65.750  32.752  1.00 25.56 ? 116 THR F CB  1 
ATOM   6396  O  OG1 . THR F  1 116 ? 24.220  64.596  31.963  1.00 37.93 ? 116 THR F OG1 1 
ATOM   6397  C  CG2 . THR F  1 116 ? 25.088  66.005  33.681  1.00 26.83 ? 116 THR F CG2 1 
ATOM   6398  N  N   . LEU F  1 117 ? 22.795  66.374  35.743  1.00 27.13 ? 117 LEU F N   1 
ATOM   6399  C  CA  . LEU F  1 117 ? 22.706  67.369  36.780  1.00 24.94 ? 117 LEU F CA  1 
ATOM   6400  C  C   . LEU F  1 117 ? 24.113  67.860  36.972  1.00 26.56 ? 117 LEU F C   1 
ATOM   6401  O  O   . LEU F  1 117 ? 25.049  67.062  36.988  1.00 26.05 ? 117 LEU F O   1 
ATOM   6402  C  CB  . LEU F  1 117 ? 22.181  66.733  38.073  1.00 25.02 ? 117 LEU F CB  1 
ATOM   6403  C  CG  . LEU F  1 117 ? 22.083  67.662  39.282  1.00 23.55 ? 117 LEU F CG  1 
ATOM   6404  C  CD1 . LEU F  1 117 ? 20.983  68.695  39.047  1.00 22.11 ? 117 LEU F CD1 1 
ATOM   6405  C  CD2 . LEU F  1 117 ? 21.832  66.861  40.552  1.00 20.78 ? 117 LEU F CD2 1 
ATOM   6406  N  N   . VAL F  1 118 ? 24.282  69.169  37.112  1.00 24.21 ? 118 VAL F N   1 
ATOM   6407  C  CA  . VAL F  1 118 ? 25.619  69.726  37.235  1.00 26.64 ? 118 VAL F CA  1 
ATOM   6408  C  C   . VAL F  1 118 ? 25.668  70.752  38.357  1.00 22.82 ? 118 VAL F C   1 
ATOM   6409  O  O   . VAL F  1 118 ? 24.744  71.551  38.510  1.00 24.70 ? 118 VAL F O   1 
ATOM   6410  C  CB  . VAL F  1 118 ? 26.048  70.391  35.894  1.00 25.34 ? 118 VAL F CB  1 
ATOM   6411  C  CG1 . VAL F  1 118 ? 27.356  71.118  36.037  1.00 23.91 ? 118 VAL F CG1 1 
ATOM   6412  C  CG2 . VAL F  1 118 ? 26.118  69.361  34.782  1.00 24.24 ? 118 VAL F CG2 1 
ATOM   6413  N  N   . VAL F  1 119 ? 26.732  70.720  39.148  1.00 21.22 ? 119 VAL F N   1 
ATOM   6414  C  CA  . VAL F  1 119 ? 26.968  71.750  40.145  1.00 23.36 ? 119 VAL F CA  1 
ATOM   6415  C  C   . VAL F  1 119 ? 28.195  72.560  39.715  1.00 28.62 ? 119 VAL F C   1 
ATOM   6416  O  O   . VAL F  1 119 ? 29.180  71.991  39.256  1.00 28.82 ? 119 VAL F O   1 
ATOM   6417  C  CB  . VAL F  1 119 ? 27.120  71.171  41.594  1.00 19.65 ? 119 VAL F CB  1 
ATOM   6418  C  CG1 . VAL F  1 119 ? 28.053  69.983  41.619  1.00 25.70 ? 119 VAL F CG1 1 
ATOM   6419  C  CG2 . VAL F  1 119 ? 27.603  72.243  42.565  1.00 19.26 ? 119 VAL F CG2 1 
ATOM   6420  N  N   . HIS F  1 120 ? 28.133  73.881  39.883  1.00 27.23 ? 120 HIS F N   1 
ATOM   6421  C  CA  . HIS F  1 120 ? 29.077  74.786  39.244  1.00 20.53 ? 120 HIS F CA  1 
ATOM   6422  C  C   . HIS F  1 120 ? 30.082  75.453  40.148  1.00 28.22 ? 120 HIS F C   1 
ATOM   6423  O  O   . HIS F  1 120 ? 29.920  75.516  41.380  1.00 29.56 ? 120 HIS F O   1 
ATOM   6424  C  CB  . HIS F  1 120 ? 28.324  75.875  38.472  1.00 26.16 ? 120 HIS F CB  1 
ATOM   6425  C  CG  . HIS F  1 120 ? 27.758  75.416  37.167  1.00 22.53 ? 120 HIS F CG  1 
ATOM   6426  N  ND1 . HIS F  1 120 ? 28.412  75.601  35.965  1.00 30.41 ? 120 HIS F ND1 1 
ATOM   6427  C  CD2 . HIS F  1 120 ? 26.599  74.783  36.869  1.00 26.12 ? 120 HIS F CD2 1 
ATOM   6428  C  CE1 . HIS F  1 120 ? 27.677  75.102  34.984  1.00 28.72 ? 120 HIS F CE1 1 
ATOM   6429  N  NE2 . HIS F  1 120 ? 26.567  74.608  35.505  1.00 25.83 ? 120 HIS F NE2 1 
ATOM   6430  N  N   . GLU F  1 121 ? 31.116  75.976  39.489  1.00 27.78 ? 121 GLU F N   1 
ATOM   6431  C  CA  . GLU F  1 121 ? 32.228  76.664  40.110  1.00 27.32 ? 121 GLU F CA  1 
ATOM   6432  C  C   . GLU F  1 121 ? 31.799  77.868  40.937  1.00 28.64 ? 121 GLU F C   1 
ATOM   6433  O  O   . GLU F  1 121 ? 32.274  78.079  42.060  1.00 27.82 ? 121 GLU F O   1 
ATOM   6434  C  CB  . GLU F  1 121 ? 33.178  77.128  39.005  1.00 31.80 ? 121 GLU F CB  1 
ATOM   6435  C  CG  . GLU F  1 121 ? 34.470  77.783  39.484  1.00 37.74 ? 121 GLU F CG  1 
ATOM   6436  C  CD  . GLU F  1 121 ? 35.275  78.409  38.335  1.00 41.28 ? 121 GLU F CD  1 
ATOM   6437  O  OE1 . GLU F  1 121 ? 34.921  78.176  37.153  1.00 38.12 ? 121 GLU F OE1 1 
ATOM   6438  O  OE2 . GLU F  1 121 ? 36.243  79.155  38.625  1.00 38.62 ? 121 GLU F OE2 1 
ATOM   6439  N  N   . LYS F  1 122 ? 30.910  78.674  40.370  1.00 29.76 ? 122 LYS F N   1 
ATOM   6440  C  CA  . LYS F  1 122 ? 30.522  79.919  41.010  1.00 28.75 ? 122 LYS F CA  1 
ATOM   6441  C  C   . LYS F  1 122 ? 29.002  80.113  40.984  1.00 21.90 ? 122 LYS F C   1 
ATOM   6442  O  O   . LYS F  1 122 ? 28.263  79.320  40.401  1.00 18.71 ? 122 LYS F O   1 
ATOM   6443  C  CB  . LYS F  1 122 ? 31.222  81.115  40.328  1.00 33.45 ? 122 LYS F CB  1 
ATOM   6444  C  CG  . LYS F  1 122 ? 32.222  80.743  39.222  1.00 34.80 ? 122 LYS F CG  1 
ATOM   6445  C  CD  . LYS F  1 122 ? 32.277  81.775  38.078  1.00 32.66 ? 122 LYS F CD  1 
ATOM   6446  C  CE  . LYS F  1 122 ? 33.047  83.029  38.458  1.00 37.81 ? 122 LYS F CE  1 
ATOM   6447  N  NZ  . LYS F  1 122 ? 33.230  83.956  37.278  1.00 44.78 ? 122 LYS F NZ  1 
ATOM   6448  N  N   . ALA F  1 123 ? 28.563  81.191  41.618  1.00 23.78 ? 123 ALA F N   1 
ATOM   6449  C  CA  . ALA F  1 123 ? 27.154  81.563  41.676  1.00 26.24 ? 123 ALA F CA  1 
ATOM   6450  C  C   . ALA F  1 123 ? 26.505  81.735  40.304  1.00 20.85 ? 123 ALA F C   1 
ATOM   6451  O  O   . ALA F  1 123 ? 27.077  82.352  39.408  1.00 25.32 ? 123 ALA F O   1 
ATOM   6452  C  CB  . ALA F  1 123 ? 26.997  82.835  42.496  1.00 24.82 ? 123 ALA F CB  1 
ATOM   6453  N  N   . ASP F  1 124 ? 25.331  81.140  40.139  1.00 22.28 ? 124 ASP F N   1 
ATOM   6454  C  CA  . ASP F  1 124 ? 24.430  81.465  39.043  1.00 21.20 ? 124 ASP F CA  1 
ATOM   6455  C  C   . ASP F  1 124 ? 23.810  82.847  39.317  1.00 23.50 ? 124 ASP F C   1 
ATOM   6456  O  O   . ASP F  1 124 ? 23.252  83.076  40.397  1.00 21.55 ? 124 ASP F O   1 
ATOM   6457  C  CB  . ASP F  1 124 ? 23.357  80.395  38.944  1.00 18.34 ? 124 ASP F CB  1 
ATOM   6458  C  CG  . ASP F  1 124 ? 22.389  80.614  37.804  1.00 21.08 ? 124 ASP F CG  1 
ATOM   6459  O  OD1 . ASP F  1 124 ? 22.281  81.741  37.277  1.00 23.85 ? 124 ASP F OD1 1 
ATOM   6460  O  OD2 . ASP F  1 124 ? 21.712  79.636  37.433  1.00 21.59 ? 124 ASP F OD2 1 
ATOM   6461  N  N   . ASP F  1 125 ? 23.894  83.769  38.349  1.00 23.01 ? 125 ASP F N   1 
ATOM   6462  C  CA  . ASP F  1 125 ? 23.352  85.118  38.574  1.00 19.49 ? 125 ASP F CA  1 
ATOM   6463  C  C   . ASP F  1 125 ? 21.844  85.235  38.311  1.00 18.49 ? 125 ASP F C   1 
ATOM   6464  O  O   . ASP F  1 125 ? 21.274  86.315  38.455  1.00 18.27 ? 125 ASP F O   1 
ATOM   6465  C  CB  . ASP F  1 125 ? 24.142  86.214  37.828  1.00 21.75 ? 125 ASP F CB  1 
ATOM   6466  C  CG  . ASP F  1 125 ? 23.986  86.161  36.309  1.00 20.91 ? 125 ASP F CG  1 
ATOM   6467  O  OD1 . ASP F  1 125 ? 23.053  85.528  35.765  1.00 20.61 ? 125 ASP F OD1 1 
ATOM   6468  O  OD2 . ASP F  1 125 ? 24.826  86.798  35.639  1.00 32.04 ? 125 ASP F OD2 1 
ATOM   6469  N  N   . LEU F  1 126 ? 21.226  84.127  37.906  1.00 15.64 ? 126 LEU F N   1 
ATOM   6470  C  CA  . LEU F  1 126 ? 19.765  84.007  37.837  1.00 18.28 ? 126 LEU F CA  1 
ATOM   6471  C  C   . LEU F  1 126 ? 19.173  84.907  36.755  1.00 18.26 ? 126 LEU F C   1 
ATOM   6472  O  O   . LEU F  1 126 ? 18.013  85.309  36.831  1.00 16.19 ? 126 LEU F O   1 
ATOM   6473  C  CB  . LEU F  1 126 ? 19.114  84.271  39.210  1.00 16.60 ? 126 LEU F CB  1 
ATOM   6474  C  CG  . LEU F  1 126 ? 19.734  83.519  40.402  1.00 19.00 ? 126 LEU F CG  1 
ATOM   6475  C  CD1 . LEU F  1 126 ? 19.004  83.810  41.714  1.00 14.48 ? 126 LEU F CD1 1 
ATOM   6476  C  CD2 . LEU F  1 126 ? 19.739  82.033  40.114  1.00 17.75 ? 126 LEU F CD2 1 
ATOM   6477  N  N   . GLY F  1 127 ? 19.981  85.210  35.740  1.00 17.06 ? 127 GLY F N   1 
ATOM   6478  C  CA  . GLY F  1 127 ? 19.523  85.996  34.609  1.00 12.50 ? 127 GLY F CA  1 
ATOM   6479  C  C   . GLY F  1 127 ? 19.558  87.493  34.838  1.00 13.18 ? 127 GLY F C   1 
ATOM   6480  O  O   . GLY F  1 127 ? 19.019  88.241  34.039  1.00 14.29 ? 127 GLY F O   1 
ATOM   6481  N  N   . LYS F  1 128 ? 20.209  87.937  35.908  1.00 11.77 ? 128 LYS F N   1 
ATOM   6482  C  CA  . LYS F  1 128 ? 20.175  89.356  36.292  1.00 15.98 ? 128 LYS F CA  1 
ATOM   6483  C  C   . LYS F  1 128 ? 21.504  90.069  36.118  1.00 14.55 ? 128 LYS F C   1 
ATOM   6484  O  O   . LYS F  1 128 ? 21.719  91.130  36.694  1.00 16.14 ? 128 LYS F O   1 
ATOM   6485  C  CB  . LYS F  1 128 ? 19.689  89.496  37.739  1.00 14.04 ? 128 LYS F CB  1 
ATOM   6486  C  CG  . LYS F  1 128 ? 18.330  88.841  37.937  1.00 15.33 ? 128 LYS F CG  1 
ATOM   6487  C  CD  . LYS F  1 128 ? 17.975  88.668  39.392  1.00 15.96 ? 128 LYS F CD  1 
ATOM   6488  C  CE  . LYS F  1 128 ? 17.536  89.967  40.054  1.00 15.39 ? 128 LYS F CE  1 
ATOM   6489  N  NZ  . LYS F  1 128 ? 17.600  89.799  41.528  1.00 25.27 ? 128 LYS F NZ  1 
ATOM   6490  N  N   . GLY F  1 129 ? 22.385  89.469  35.325  1.00 15.67 ? 129 GLY F N   1 
ATOM   6491  C  CA  . GLY F  1 129 ? 23.719  89.993  35.113  1.00 21.57 ? 129 GLY F CA  1 
ATOM   6492  C  C   . GLY F  1 129 ? 23.819  91.071  34.039  1.00 22.12 ? 129 GLY F C   1 
ATOM   6493  O  O   . GLY F  1 129 ? 24.777  91.836  34.043  1.00 17.01 ? 129 GLY F O   1 
ATOM   6494  N  N   . GLY F  1 130 ? 22.834  91.141  33.139  1.00 17.33 ? 130 GLY F N   1 
ATOM   6495  C  CA  . GLY F  1 130 ? 22.720  92.245  32.191  1.00 14.09 ? 130 GLY F CA  1 
ATOM   6496  C  C   . GLY F  1 130 ? 23.693  92.153  31.026  1.00 21.50 ? 130 GLY F C   1 
ATOM   6497  O  O   . GLY F  1 130 ? 23.932  93.116  30.288  1.00 14.61 ? 130 GLY F O   1 
ATOM   6498  N  N   . ASN F  1 131 ? 24.280  90.980  30.872  1.00 21.91 ? 131 ASN F N   1 
ATOM   6499  C  CA  . ASN F  1 131 ? 25.001  90.684  29.665  1.00 22.65 ? 131 ASN F CA  1 
ATOM   6500  C  C   . ASN F  1 131 ? 24.389  89.525  28.928  1.00 27.69 ? 131 ASN F C   1 
ATOM   6501  O  O   . ASN F  1 131 ? 23.405  88.923  29.357  1.00 29.07 ? 131 ASN F O   1 
ATOM   6502  C  CB  . ASN F  1 131 ? 26.482  90.422  29.939  1.00 24.61 ? 131 ASN F CB  1 
ATOM   6503  C  CG  . ASN F  1 131 ? 26.719  89.276  30.905  1.00 27.52 ? 131 ASN F CG  1 
ATOM   6504  O  OD1 . ASN F  1 131 ? 25.895  88.363  31.048  1.00 30.66 ? 131 ASN F OD1 1 
ATOM   6505  N  ND2 . ASN F  1 131 ? 27.868  89.307  31.556  1.00 22.54 ? 131 ASN F ND2 1 
ATOM   6506  N  N   . GLU F  1 132 ? 25.005  89.226  27.801  1.00 31.13 ? 132 GLU F N   1 
ATOM   6507  C  CA  . GLU F  1 132 ? 24.660  88.091  26.969  1.00 35.88 ? 132 GLU F CA  1 
ATOM   6508  C  C   . GLU F  1 132 ? 24.619  86.760  27.725  1.00 31.24 ? 132 GLU F C   1 
ATOM   6509  O  O   . GLU F  1 132 ? 23.723  85.932  27.521  1.00 28.05 ? 132 GLU F O   1 
ATOM   6510  C  CB  . GLU F  1 132 ? 25.732  87.992  25.890  1.00 30.23 ? 132 GLU F CB  1 
ATOM   6511  C  CG  . GLU F  1 132 ? 26.152  89.341  25.365  1.00 28.95 ? 132 GLU F CG  1 
ATOM   6512  C  CD  . GLU F  1 132 ? 27.038  89.224  24.141  1.00 43.55 ? 132 GLU F CD  1 
ATOM   6513  O  OE1 . GLU F  1 132 ? 28.272  89.010  24.307  1.00 42.40 ? 132 GLU F OE1 1 
ATOM   6514  O  OE2 . GLU F  1 132 ? 26.488  89.334  23.018  1.00 40.31 ? 132 GLU F OE2 1 
ATOM   6515  N  N   . GLU F  1 133 ? 25.622  86.555  28.572  1.00 28.75 ? 133 GLU F N   1 
ATOM   6516  C  CA  . GLU F  1 133 ? 25.855  85.251  29.179  1.00 33.04 ? 133 GLU F CA  1 
ATOM   6517  C  C   . GLU F  1 133 ? 24.869  84.995  30.327  1.00 34.06 ? 133 GLU F C   1 
ATOM   6518  O  O   . GLU F  1 133 ? 24.423  83.860  30.535  1.00 34.44 ? 133 GLU F O   1 
ATOM   6519  C  CB  . GLU F  1 133 ? 27.314  85.149  29.653  1.00 31.65 ? 133 GLU F CB  1 
ATOM   6520  C  CG  . GLU F  1 133 ? 27.763  83.740  30.009  1.00 38.59 ? 133 GLU F CG  1 
ATOM   6521  C  CD  . GLU F  1 133 ? 27.786  82.800  28.821  1.00 37.57 ? 133 GLU F CD  1 
ATOM   6522  O  OE1 . GLU F  1 133 ? 27.856  83.278  27.669  1.00 38.44 ? 133 GLU F OE1 1 
ATOM   6523  O  OE2 . GLU F  1 133 ? 27.735  81.576  29.051  1.00 42.26 ? 133 GLU F OE2 1 
ATOM   6524  N  N   . SER F  1 134 ? 24.520  86.058  31.049  1.00 29.32 ? 134 SER F N   1 
ATOM   6525  C  CA  . SER F  1 134 ? 23.536  85.975  32.126  1.00 28.00 ? 134 SER F CA  1 
ATOM   6526  C  C   . SER F  1 134 ? 22.260  85.297  31.649  1.00 28.18 ? 134 SER F C   1 
ATOM   6527  O  O   . SER F  1 134 ? 21.688  84.454  32.339  1.00 27.79 ? 134 SER F O   1 
ATOM   6528  C  CB  . SER F  1 134 ? 23.222  87.373  32.657  1.00 25.21 ? 134 SER F CB  1 
ATOM   6529  O  OG  . SER F  1 134 ? 22.278  87.349  33.715  1.00 22.00 ? 134 SER F OG  1 
ATOM   6530  N  N   . THR F  1 135 ? 21.827  85.631  30.445  1.00 25.43 ? 135 THR F N   1 
ATOM   6531  C  CA  . THR F  1 135 ? 20.545  85.134  29.986  1.00 22.53 ? 135 THR F CA  1 
ATOM   6532  C  C   . THR F  1 135 ? 20.716  83.828  29.235  1.00 27.00 ? 135 THR F C   1 
ATOM   6533  O  O   . THR F  1 135 ? 19.757  83.295  28.664  1.00 23.65 ? 135 THR F O   1 
ATOM   6534  C  CB  . THR F  1 135 ? 19.856  86.138  29.077  1.00 30.44 ? 135 THR F CB  1 
ATOM   6535  O  OG1 . THR F  1 135 ? 18.637  85.562  28.609  1.00 40.99 ? 135 THR F OG1 1 
ATOM   6536  C  CG2 . THR F  1 135 ? 20.730  86.456  27.879  1.00 29.78 ? 135 THR F CG2 1 
ATOM   6537  N  N   . LYS F  1 136 ? 21.949  83.323  29.245  1.00 28.96 ? 136 LYS F N   1 
ATOM   6538  C  CA  . LYS F  1 136 ? 22.270  82.046  28.621  1.00 33.08 ? 136 LYS F CA  1 
ATOM   6539  C  C   . LYS F  1 136 ? 22.469  80.943  29.663  1.00 30.06 ? 136 LYS F C   1 
ATOM   6540  O  O   . LYS F  1 136 ? 21.774  79.921  29.660  1.00 29.04 ? 136 LYS F O   1 
ATOM   6541  C  CB  . LYS F  1 136 ? 23.534  82.182  27.754  1.00 34.02 ? 136 LYS F CB  1 
ATOM   6542  C  CG  . LYS F  1 136 ? 23.290  82.849  26.398  1.00 41.53 ? 136 LYS F CG  1 
ATOM   6543  C  CD  . LYS F  1 136 ? 24.525  82.781  25.473  1.00 43.27 ? 136 LYS F CD  1 
ATOM   6544  C  CE  . LYS F  1 136 ? 24.170  83.183  24.033  1.00 50.30 ? 136 LYS F CE  1 
ATOM   6545  N  NZ  . LYS F  1 136 ? 23.152  82.270  23.401  1.00 47.75 ? 136 LYS F NZ  1 
ATOM   6546  N  N   . THR F  1 137 ? 23.421  81.172  30.561  1.00 29.59 ? 137 THR F N   1 
ATOM   6547  C  CA  . THR F  1 137 ? 23.851  80.153  31.501  1.00 28.92 ? 137 THR F CA  1 
ATOM   6548  C  C   . THR F  1 137 ? 23.883  80.659  32.944  1.00 28.61 ? 137 THR F C   1 
ATOM   6549  O  O   . THR F  1 137 ? 23.881  79.877  33.890  1.00 31.36 ? 137 THR F O   1 
ATOM   6550  C  CB  . THR F  1 137 ? 25.270  79.712  31.150  1.00 31.74 ? 137 THR F CB  1 
ATOM   6551  O  OG1 . THR F  1 137 ? 26.198  80.757  31.506  1.00 29.32 ? 137 THR F OG1 1 
ATOM   6552  C  CG2 . THR F  1 137 ? 25.372  79.402  29.664  1.00 28.15 ? 137 THR F CG2 1 
ATOM   6553  N  N   . GLY F  1 138 ? 23.952  81.970  33.115  1.00 25.44 ? 138 GLY F N   1 
ATOM   6554  C  CA  . GLY F  1 138 ? 24.024  82.546  34.436  1.00 19.63 ? 138 GLY F CA  1 
ATOM   6555  C  C   . GLY F  1 138 ? 25.428  82.869  34.901  1.00 22.21 ? 138 GLY F C   1 
ATOM   6556  O  O   . GLY F  1 138 ? 25.605  83.276  36.044  1.00 21.28 ? 138 GLY F O   1 
ATOM   6557  N  N   . ASN F  1 139 ? 26.423  82.707  34.027  1.00 28.06 ? 139 ASN F N   1 
ATOM   6558  C  CA  . ASN F  1 139 ? 27.804  83.023  34.392  1.00 24.56 ? 139 ASN F CA  1 
ATOM   6559  C  C   . ASN F  1 139 ? 28.220  82.215  35.604  1.00 22.36 ? 139 ASN F C   1 
ATOM   6560  O  O   . ASN F  1 139 ? 28.870  82.765  36.505  1.00 18.59 ? 139 ASN F O   1 
ATOM   6561  C  CB  . ASN F  1 139 ? 27.960  84.505  34.788  1.00 22.63 ? 139 ASN F CB  1 
ATOM   6562  C  CG  . ASN F  1 139 ? 27.716  85.452  33.647  1.00 33.26 ? 139 ASN F CG  1 
ATOM   6563  O  OD1 . ASN F  1 139 ? 28.058  85.164  32.506  1.00 31.87 ? 139 ASN F OD1 1 
ATOM   6564  N  ND2 . ASN F  1 139 ? 27.129  86.609  33.955  1.00 29.17 ? 139 ASN F ND2 1 
ATOM   6565  N  N   . ALA F  1 140 ? 27.809  80.949  35.666  1.00 22.40 ? 140 ALA F N   1 
ATOM   6566  C  CA  . ALA F  1 140 ? 28.036  80.155  36.889  1.00 26.18 ? 140 ALA F CA  1 
ATOM   6567  C  C   . ALA F  1 140 ? 29.433  79.548  36.942  1.00 27.24 ? 140 ALA F C   1 
ATOM   6568  O  O   . ALA F  1 140 ? 29.889  79.091  37.998  1.00 29.47 ? 140 ALA F O   1 
ATOM   6569  C  CB  . ALA F  1 140 ? 26.970  79.071  37.053  1.00 22.13 ? 140 ALA F CB  1 
ATOM   6570  N  N   . GLY F  1 141 ? 30.108  79.541  35.799  1.00 28.57 ? 141 GLY F N   1 
ATOM   6571  C  CA  . GLY F  1 141 ? 31.501  79.136  35.754  1.00 30.50 ? 141 GLY F CA  1 
ATOM   6572  C  C   . GLY F  1 141 ? 31.690  77.713  35.286  1.00 27.76 ? 141 GLY F C   1 
ATOM   6573  O  O   . GLY F  1 141 ? 30.873  77.171  34.537  1.00 29.10 ? 141 GLY F O   1 
ATOM   6574  N  N   . SER F  1 142 ? 32.784  77.100  35.727  1.00 35.66 ? 142 SER F N   1 
ATOM   6575  C  CA  . SER F  1 142 ? 33.096  75.734  35.303  1.00 39.92 ? 142 SER F CA  1 
ATOM   6576  C  C   . SER F  1 142 ? 32.129  74.674  35.867  1.00 33.08 ? 142 SER F C   1 
ATOM   6577  O  O   . SER F  1 142 ? 31.553  74.862  36.944  1.00 28.77 ? 142 SER F O   1 
ATOM   6578  C  CB  . SER F  1 142 ? 34.563  75.377  35.610  1.00 38.01 ? 142 SER F CB  1 
ATOM   6579  O  OG  . SER F  1 142 ? 34.913  75.637  36.963  1.00 41.41 ? 142 SER F OG  1 
ATOM   6580  N  N   . ARG F  1 143 ? 31.947  73.592  35.104  1.00 33.27 ? 143 ARG F N   1 
ATOM   6581  C  CA  . ARG F  1 143 ? 31.143  72.436  35.496  1.00 32.20 ? 143 ARG F CA  1 
ATOM   6582  C  C   . ARG F  1 143 ? 31.881  71.488  36.468  1.00 37.38 ? 143 ARG F C   1 
ATOM   6583  O  O   . ARG F  1 143 ? 32.376  70.443  36.047  1.00 37.70 ? 143 ARG F O   1 
ATOM   6584  C  CB  . ARG F  1 143 ? 30.731  71.647  34.250  1.00 32.38 ? 143 ARG F CB  1 
ATOM   6585  C  CG  . ARG F  1 143 ? 29.967  72.454  33.211  1.00 37.65 ? 143 ARG F CG  1 
ATOM   6586  C  CD  . ARG F  1 143 ? 29.390  71.587  32.078  1.00 35.07 ? 143 ARG F CD  1 
ATOM   6587  N  NE  . ARG F  1 143 ? 28.562  72.378  31.159  1.00 36.17 ? 143 ARG F NE  1 
ATOM   6588  C  CZ  . ARG F  1 143 ? 27.915  71.894  30.097  1.00 41.60 ? 143 ARG F CZ  1 
ATOM   6589  N  NH1 . ARG F  1 143 ? 27.995  70.611  29.790  1.00 46.13 ? 143 ARG F NH1 1 
ATOM   6590  N  NH2 . ARG F  1 143 ? 27.181  72.696  29.331  1.00 39.71 ? 143 ARG F NH2 1 
ATOM   6591  N  N   . LEU F  1 144 ? 31.917  71.840  37.759  1.00 32.57 ? 144 LEU F N   1 
ATOM   6592  C  CA  . LEU F  1 144 ? 32.717  71.128  38.766  1.00 30.25 ? 144 LEU F CA  1 
ATOM   6593  C  C   . LEU F  1 144 ? 32.423  69.632  38.966  1.00 38.23 ? 144 LEU F C   1 
ATOM   6594  O  O   . LEU F  1 144 ? 33.334  68.861  39.277  1.00 37.63 ? 144 LEU F O   1 
ATOM   6595  C  CB  . LEU F  1 144 ? 32.616  71.826  40.114  1.00 33.73 ? 144 LEU F CB  1 
ATOM   6596  C  CG  . LEU F  1 144 ? 33.350  73.152  40.295  1.00 34.52 ? 144 LEU F CG  1 
ATOM   6597  C  CD1 . LEU F  1 144 ? 33.276  73.575  41.744  1.00 31.21 ? 144 LEU F CD1 1 
ATOM   6598  C  CD2 . LEU F  1 144 ? 34.793  73.036  39.848  1.00 40.38 ? 144 LEU F CD2 1 
ATOM   6599  N  N   . ALA F  1 145 ? 31.162  69.226  38.813  1.00 39.31 ? 145 ALA F N   1 
ATOM   6600  C  CA  . ALA F  1 145 ? 30.780  67.820  38.972  1.00 37.00 ? 145 ALA F CA  1 
ATOM   6601  C  C   . ALA F  1 145 ? 29.429  67.575  38.333  1.00 33.55 ? 145 ALA F C   1 
ATOM   6602  O  O   . ALA F  1 145 ? 28.586  68.468  38.295  1.00 34.89 ? 145 ALA F O   1 
ATOM   6603  C  CB  . ALA F  1 145 ? 30.749  67.420  40.454  1.00 34.66 ? 145 ALA F CB  1 
ATOM   6604  N  N   . CYS F  1 146 ? 29.216  66.364  37.840  1.00 33.55 ? 146 CYS F N   1 
ATOM   6605  C  CA  . CYS F  1 146 ? 27.985  66.054  37.133  1.00 27.70 ? 146 CYS F CA  1 
ATOM   6606  C  C   . CYS F  1 146 ? 27.583  64.587  37.284  1.00 27.81 ? 146 CYS F C   1 
ATOM   6607  O  O   . CYS F  1 146 ? 28.281  63.801  37.914  1.00 36.14 ? 146 CYS F O   1 
ATOM   6608  C  CB  . CYS F  1 146 ? 28.119  66.437  35.653  1.00 37.60 ? 146 CYS F CB  1 
ATOM   6609  S  SG  . CYS F  1 146 ? 28.597  65.108  34.510  1.00 40.95 ? 146 CYS F SG  1 
ATOM   6610  N  N   . GLY F  1 147 ? 26.445  64.227  36.705  1.00 30.48 ? 147 GLY F N   1 
ATOM   6611  C  CA  . GLY F  1 147 ? 25.965  62.863  36.735  1.00 23.52 ? 147 GLY F CA  1 
ATOM   6612  C  C   . GLY F  1 147 ? 24.622  62.772  36.064  1.00 23.64 ? 147 GLY F C   1 
ATOM   6613  O  O   . GLY F  1 147 ? 23.892  63.759  36.029  1.00 31.22 ? 147 GLY F O   1 
ATOM   6614  N  N   . VAL F  1 148 ? 24.291  61.600  35.532  1.00 20.90 ? 148 VAL F N   1 
ATOM   6615  C  CA  . VAL F  1 148 ? 22.979  61.370  34.942  1.00 24.19 ? 148 VAL F CA  1 
ATOM   6616  C  C   . VAL F  1 148 ? 21.971  61.055  36.034  1.00 32.69 ? 148 VAL F C   1 
ATOM   6617  O  O   . VAL F  1 148 ? 22.299  60.456  37.058  1.00 34.22 ? 148 VAL F O   1 
ATOM   6618  C  CB  . VAL F  1 148 ? 23.002  60.230  33.883  1.00 26.92 ? 148 VAL F CB  1 
ATOM   6619  C  CG1 . VAL F  1 148 ? 21.630  59.916  33.318  1.00 27.26 ? 148 VAL F CG1 1 
ATOM   6620  C  CG2 . VAL F  1 148 ? 23.955  60.580  32.764  1.00 35.22 ? 148 VAL F CG2 1 
ATOM   6621  N  N   . ILE F  1 149 ? 20.740  61.475  35.801  1.00 26.63 ? 149 ILE F N   1 
ATOM   6622  C  CA  . ILE F  1 149 ? 19.656  61.300  36.730  1.00 26.79 ? 149 ILE F CA  1 
ATOM   6623  C  C   . ILE F  1 149 ? 18.960  60.008  36.364  1.00 29.86 ? 149 ILE F C   1 
ATOM   6624  O  O   . ILE F  1 149 ? 18.466  59.875  35.251  1.00 25.38 ? 149 ILE F O   1 
ATOM   6625  C  CB  . ILE F  1 149 ? 18.668  62.470  36.567  1.00 24.95 ? 149 ILE F CB  1 
ATOM   6626  C  CG1 . ILE F  1 149 ? 19.339  63.785  36.987  1.00 27.70 ? 149 ILE F CG1 1 
ATOM   6627  C  CG2 . ILE F  1 149 ? 17.383  62.209  37.317  1.00 25.46 ? 149 ILE F CG2 1 
ATOM   6628  C  CD1 . ILE F  1 149 ? 18.520  65.048  36.651  1.00 29.20 ? 149 ILE F CD1 1 
ATOM   6629  N  N   . GLY F  1 150 ? 18.929  59.052  37.289  1.00 29.59 ? 150 GLY F N   1 
ATOM   6630  C  CA  . GLY F  1 150 ? 18.312  57.761  37.019  1.00 23.04 ? 150 GLY F CA  1 
ATOM   6631  C  C   . GLY F  1 150 ? 17.081  57.512  37.870  1.00 25.76 ? 150 GLY F C   1 
ATOM   6632  O  O   . GLY F  1 150 ? 16.854  58.192  38.873  1.00 24.92 ? 150 GLY F O   1 
ATOM   6633  N  N   . ILE F  1 151 ? 16.283  56.536  37.460  1.00 23.27 ? 151 ILE F N   1 
ATOM   6634  C  CA  . ILE F  1 151 ? 15.099  56.127  38.199  1.00 25.39 ? 151 ILE F CA  1 
ATOM   6635  C  C   . ILE F  1 151 ? 15.543  55.401  39.461  1.00 28.00 ? 151 ILE F C   1 
ATOM   6636  O  O   . ILE F  1 151 ? 16.393  54.525  39.385  1.00 27.29 ? 151 ILE F O   1 
ATOM   6637  C  CB  . ILE F  1 151 ? 14.237  55.205  37.329  1.00 25.83 ? 151 ILE F CB  1 
ATOM   6638  C  CG1 . ILE F  1 151 ? 13.941  55.899  35.992  1.00 32.41 ? 151 ILE F CG1 1 
ATOM   6639  C  CG2 . ILE F  1 151 ? 12.958  54.813  38.039  1.00 24.12 ? 151 ILE F CG2 1 
ATOM   6640  C  CD1 . ILE F  1 151 ? 13.049  55.113  35.023  1.00 30.06 ? 151 ILE F CD1 1 
ATOM   6641  N  N   . ALA F  1 152 ? 15.001  55.791  40.619  1.00 28.27 ? 152 ALA F N   1 
ATOM   6642  C  CA  . ALA F  1 152 ? 15.346  55.153  41.900  1.00 25.91 ? 152 ALA F CA  1 
ATOM   6643  C  C   . ALA F  1 152 ? 14.178  54.354  42.450  1.00 28.86 ? 152 ALA F C   1 
ATOM   6644  O  O   . ALA F  1 152 ? 13.035  54.549  42.032  1.00 25.29 ? 152 ALA F O   1 
ATOM   6645  C  CB  . ALA F  1 152 ? 15.805  56.190  42.943  1.00 19.71 ? 152 ALA F CB  1 
ATOM   6646  N  N   . GLN F  1 153 ? 14.472  53.448  43.382  1.00 26.96 ? 153 GLN F N   1 
ATOM   6647  C  CA  . GLN F  1 153 ? 13.429  52.633  44.007  1.00 31.45 ? 153 GLN F CA  1 
ATOM   6648  C  C   . GLN F  1 153 ? 12.711  53.409  45.100  1.00 34.20 ? 153 GLN F C   1 
ATOM   6649  O  O   . GLN F  1 153 ? 13.348  54.001  45.982  1.00 36.69 ? 153 GLN F O   1 
ATOM   6650  C  CB  . GLN F  1 153 ? 14.002  51.333  44.586  1.00 34.98 ? 153 GLN F CB  1 
ATOM   6651  C  CG  . GLN F  1 153 ? 12.991  50.512  45.386  1.00 35.56 ? 153 GLN F CG  1 
ATOM   6652  C  CD  . GLN F  1 153 ? 13.475  49.100  45.675  1.00 32.98 ? 153 GLN F CD  1 
ATOM   6653  O  OE1 . GLN F  1 153 ? 14.610  48.887  46.104  1.00 36.01 ? 153 GLN F OE1 1 
ATOM   6654  N  NE2 . GLN F  1 153 ? 12.622  48.127  45.410  1.00 35.29 ? 153 GLN F NE2 1 
ATOM   6655  O  OXT . GLN F  1 153 ? 11.476  53.445  45.106  1.00 38.76 ? 153 GLN F OXT 1 
ATOM   6656  N  N   . ALA G  1 1   ? 75.130  116.386 13.084  1.00 37.20 ? 1   ALA G N   1 
ATOM   6657  C  CA  . ALA G  1 1   ? 73.900  117.159 12.867  1.00 37.73 ? 1   ALA G CA  1 
ATOM   6658  C  C   . ALA G  1 1   ? 72.728  116.811 13.818  1.00 29.30 ? 1   ALA G C   1 
ATOM   6659  O  O   . ALA G  1 1   ? 71.936  115.914 13.543  1.00 38.56 ? 1   ALA G O   1 
ATOM   6660  C  CB  . ALA G  1 1   ? 73.444  117.046 11.389  1.00 29.84 ? 1   ALA G CB  1 
ATOM   6661  N  N   . THR G  1 2   ? 72.600  117.538 14.914  1.00 26.27 ? 2   THR G N   1 
ATOM   6662  C  CA  . THR G  1 2   ? 71.439  117.373 15.773  1.00 21.50 ? 2   THR G CA  1 
ATOM   6663  C  C   . THR G  1 2   ? 70.215  118.014 15.067  1.00 22.60 ? 2   THR G C   1 
ATOM   6664  O  O   . THR G  1 2   ? 70.344  118.951 14.253  1.00 17.50 ? 2   THR G O   1 
ATOM   6665  C  CB  . THR G  1 2   ? 71.696  117.971 17.190  1.00 18.61 ? 2   THR G CB  1 
ATOM   6666  O  OG1 . THR G  1 2   ? 72.966  117.531 17.671  1.00 31.03 ? 2   THR G OG1 1 
ATOM   6667  C  CG2 . THR G  1 2   ? 70.646  117.533 18.199  1.00 28.23 ? 2   THR G CG2 1 
ATOM   6668  N  N   . LYS G  1 3   ? 69.042  117.459 15.344  1.00 15.92 ? 3   LYS G N   1 
ATOM   6669  C  CA  . LYS G  1 3   ? 67.767  118.002 14.882  1.00 16.54 ? 3   LYS G CA  1 
ATOM   6670  C  C   . LYS G  1 3   ? 66.765  118.008 16.054  1.00 14.92 ? 3   LYS G C   1 
ATOM   6671  O  O   . LYS G  1 3   ? 66.771  117.122 16.907  1.00 9.62  ? 3   LYS G O   1 
ATOM   6672  C  CB  . LYS G  1 3   ? 67.213  117.186 13.717  1.00 17.01 ? 3   LYS G CB  1 
ATOM   6673  C  CG  . LYS G  1 3   ? 67.924  117.455 12.392  1.00 22.75 ? 3   LYS G CG  1 
ATOM   6674  C  CD  . LYS G  1 3   ? 67.487  116.500 11.281  1.00 20.50 ? 3   LYS G CD  1 
ATOM   6675  C  CE  . LYS G  1 3   ? 66.034  116.673 10.900  1.00 25.64 ? 3   LYS G CE  1 
ATOM   6676  N  NZ  . LYS G  1 3   ? 65.608  118.097 10.871  1.00 31.90 ? 3   LYS G NZ  1 
ATOM   6677  N  N   . ALA G  1 4   ? 65.912  119.014 16.098  1.00 11.93 ? 4   ALA G N   1 
ATOM   6678  C  CA  . ALA G  1 4   ? 64.913  119.063 17.138  1.00 14.86 ? 4   ALA G CA  1 
ATOM   6679  C  C   . ALA G  1 4   ? 63.601  119.550 16.537  1.00 12.87 ? 4   ALA G C   1 
ATOM   6680  O  O   . ALA G  1 4   ? 63.561  120.003 15.399  1.00 11.41 ? 4   ALA G O   1 
ATOM   6681  C  CB  . ALA G  1 4   ? 65.373  119.956 18.295  1.00 10.91 ? 4   ALA G CB  1 
ATOM   6682  N  N   . VAL G  1 5   ? 62.530  119.434 17.303  1.00 11.40 ? 5   VAL G N   1 
ATOM   6683  C  CA  . VAL G  1 5   ? 61.197  119.737 16.800  1.00 10.28 ? 5   VAL G CA  1 
ATOM   6684  C  C   . VAL G  1 5   ? 60.354  120.180 17.985  1.00 12.75 ? 5   VAL G C   1 
ATOM   6685  O  O   . VAL G  1 5   ? 60.634  119.808 19.133  1.00 12.61 ? 5   VAL G O   1 
ATOM   6686  C  CB  . VAL G  1 5   ? 60.593  118.491 16.100  1.00 15.84 ? 5   VAL G CB  1 
ATOM   6687  C  CG1 . VAL G  1 5   ? 60.239  117.422 17.099  1.00 11.05 ? 5   VAL G CG1 1 
ATOM   6688  C  CG2 . VAL G  1 5   ? 59.386  118.861 15.228  1.00 14.03 ? 5   VAL G CG2 1 
ATOM   6689  N  N   . CYS G  1 6   ? 59.354  121.011 17.733  1.00 12.14 ? 6   CYS G N   1 
ATOM   6690  C  CA  . CYS G  1 6   ? 58.487  121.468 18.795  1.00 12.83 ? 6   CYS G CA  1 
ATOM   6691  C  C   . CYS G  1 6   ? 57.069  121.615 18.253  1.00 13.34 ? 6   CYS G C   1 
ATOM   6692  O  O   . CYS G  1 6   ? 56.869  122.160 17.172  1.00 13.18 ? 6   CYS G O   1 
ATOM   6693  C  CB  . CYS G  1 6   ? 59.002  122.795 19.355  1.00 10.48 ? 6   CYS G CB  1 
ATOM   6694  S  SG  . CYS G  1 6   ? 57.958  123.516 20.629  1.00 11.20 ? 6   CYS G SG  1 
ATOM   6695  N  N   . VAL G  1 7   ? 56.096  121.072 18.972  1.00 11.78 ? 7   VAL G N   1 
ATOM   6696  C  CA  . VAL G  1 7   ? 54.701  121.258 18.598  1.00 15.32 ? 7   VAL G CA  1 
ATOM   6697  C  C   . VAL G  1 7   ? 54.117  122.373 19.462  1.00 13.56 ? 7   VAL G C   1 
ATOM   6698  O  O   . VAL G  1 7   ? 54.088  122.262 20.689  1.00 11.23 ? 7   VAL G O   1 
ATOM   6699  C  CB  . VAL G  1 7   ? 53.886  119.973 18.765  1.00 15.99 ? 7   VAL G CB  1 
ATOM   6700  C  CG1 . VAL G  1 7   ? 52.414  120.227 18.401  1.00 11.63 ? 7   VAL G CG1 1 
ATOM   6701  C  CG2 . VAL G  1 7   ? 54.462  118.881 17.881  1.00 16.26 ? 7   VAL G CG2 1 
ATOM   6702  N  N   . LEU G  1 8   ? 53.703  123.459 18.814  1.00 11.09 ? 8   LEU G N   1 
ATOM   6703  C  CA  . LEU G  1 8   ? 53.147  124.612 19.508  1.00 12.09 ? 8   LEU G CA  1 
ATOM   6704  C  C   . LEU G  1 8   ? 51.644  124.427 19.622  1.00 11.81 ? 8   LEU G C   1 
ATOM   6705  O  O   . LEU G  1 8   ? 50.957  124.326 18.615  1.00 12.80 ? 8   LEU G O   1 
ATOM   6706  C  CB  . LEU G  1 8   ? 53.470  125.915 18.772  1.00 11.71 ? 8   LEU G CB  1 
ATOM   6707  C  CG  . LEU G  1 8   ? 54.929  126.403 18.829  1.00 13.32 ? 8   LEU G CG  1 
ATOM   6708  C  CD1 . LEU G  1 8   ? 55.114  127.656 18.004  1.00 13.17 ? 8   LEU G CD1 1 
ATOM   6709  C  CD2 . LEU G  1 8   ? 55.287  126.676 20.249  1.00 10.16 ? 8   LEU G CD2 1 
ATOM   6710  N  N   . LYS G  1 9   ? 51.160  124.347 20.858  1.00 13.45 ? 9   LYS G N   1 
ATOM   6711  C  CA  . LYS G  1 9   ? 49.751  124.139 21.160  1.00 18.53 ? 9   LYS G CA  1 
ATOM   6712  C  C   . LYS G  1 9   ? 49.336  125.125 22.233  1.00 19.94 ? 9   LYS G C   1 
ATOM   6713  O  O   . LYS G  1 9   ? 50.157  125.523 23.058  1.00 15.62 ? 9   LYS G O   1 
ATOM   6714  C  CB  . LYS G  1 9   ? 49.537  122.715 21.690  1.00 24.72 ? 9   LYS G CB  1 
ATOM   6715  C  CG  . LYS G  1 9   ? 48.766  121.799 20.751  1.00 29.99 ? 9   LYS G CG  1 
ATOM   6716  C  CD  . LYS G  1 9   ? 48.641  120.384 21.344  1.00 35.66 ? 9   LYS G CD  1 
ATOM   6717  C  CE  . LYS G  1 9   ? 47.774  119.467 20.466  1.00 36.35 ? 9   LYS G CE  1 
ATOM   6718  N  NZ  . LYS G  1 9   ? 48.172  119.508 19.014  1.00 29.25 ? 9   LYS G NZ  1 
ATOM   6719  N  N   . GLY G  1 10  ? 48.058  125.493 22.246  1.00 17.04 ? 10  GLY G N   1 
ATOM   6720  C  CA  . GLY G  1 10  ? 47.530  126.383 23.264  1.00 19.29 ? 10  GLY G CA  1 
ATOM   6721  C  C   . GLY G  1 10  ? 46.020  126.221 23.479  1.00 26.79 ? 10  GLY G C   1 
ATOM   6722  O  O   . GLY G  1 10  ? 45.396  125.316 22.915  1.00 25.25 ? 10  GLY G O   1 
ATOM   6723  N  N   . ASP G  1 11  ? 45.438  127.109 24.284  1.00 21.78 ? 11  ASP G N   1 
ATOM   6724  C  CA  . ASP G  1 11  ? 44.015  127.054 24.617  1.00 25.68 ? 11  ASP G CA  1 
ATOM   6725  C  C   . ASP G  1 11  ? 43.155  127.803 23.615  1.00 23.95 ? 11  ASP G C   1 
ATOM   6726  O  O   . ASP G  1 11  ? 41.927  127.815 23.728  1.00 21.39 ? 11  ASP G O   1 
ATOM   6727  C  CB  . ASP G  1 11  ? 43.774  127.623 26.015  1.00 25.91 ? 11  ASP G CB  1 
ATOM   6728  C  CG  . ASP G  1 11  ? 44.439  126.801 27.091  1.00 33.68 ? 11  ASP G CG  1 
ATOM   6729  O  OD1 . ASP G  1 11  ? 44.003  125.652 27.319  1.00 40.99 ? 11  ASP G OD1 1 
ATOM   6730  O  OD2 . ASP G  1 11  ? 45.402  127.298 27.714  1.00 50.78 ? 11  ASP G OD2 1 
ATOM   6731  N  N   . GLY G  1 12  ? 43.811  128.421 22.638  1.00 21.62 ? 12  GLY G N   1 
ATOM   6732  C  CA  . GLY G  1 12  ? 43.147  129.188 21.609  1.00 15.73 ? 12  GLY G CA  1 
ATOM   6733  C  C   . GLY G  1 12  ? 43.379  128.533 20.275  1.00 18.62 ? 12  GLY G C   1 
ATOM   6734  O  O   . GLY G  1 12  ? 43.760  127.376 20.227  1.00 22.89 ? 12  GLY G O   1 
ATOM   6735  N  N   . PRO G  1 13  ? 43.183  129.280 19.177  1.00 20.42 ? 13  PRO G N   1 
ATOM   6736  C  CA  . PRO G  1 13  ? 43.335  128.766 17.808  1.00 20.09 ? 13  PRO G CA  1 
ATOM   6737  C  C   . PRO G  1 13  ? 44.802  128.659 17.331  1.00 20.78 ? 13  PRO G C   1 
ATOM   6738  O  O   . PRO G  1 13  ? 45.084  128.072 16.273  1.00 15.69 ? 13  PRO G O   1 
ATOM   6739  C  CB  . PRO G  1 13  ? 42.613  129.829 16.974  1.00 20.67 ? 13  PRO G CB  1 
ATOM   6740  C  CG  . PRO G  1 13  ? 42.830  131.092 17.737  1.00 20.03 ? 13  PRO G CG  1 
ATOM   6741  C  CD  . PRO G  1 13  ? 42.861  130.719 19.201  1.00 18.68 ? 13  PRO G CD  1 
ATOM   6742  N  N   . VAL G  1 14  ? 45.726  129.244 18.086  1.00 16.81 ? 14  VAL G N   1 
ATOM   6743  C  CA  . VAL G  1 14  ? 47.112  129.304 17.631  1.00 18.97 ? 14  VAL G CA  1 
ATOM   6744  C  C   . VAL G  1 14  ? 47.801  127.953 17.706  1.00 16.29 ? 14  VAL G C   1 
ATOM   6745  O  O   . VAL G  1 14  ? 47.816  127.317 18.756  1.00 17.02 ? 14  VAL G O   1 
ATOM   6746  C  CB  . VAL G  1 14  ? 47.944  130.359 18.390  1.00 20.15 ? 14  VAL G CB  1 
ATOM   6747  C  CG1 . VAL G  1 14  ? 49.431  130.269 17.985  1.00 16.89 ? 14  VAL G CG1 1 
ATOM   6748  C  CG2 . VAL G  1 14  ? 47.420  131.731 18.078  1.00 17.70 ? 14  VAL G CG2 1 
ATOM   6749  N  N   . GLN G  1 15  ? 48.369  127.520 16.582  1.00 16.92 ? 15  GLN G N   1 
ATOM   6750  C  CA  . GLN G  1 15  ? 49.095  126.267 16.567  1.00 19.13 ? 15  GLN G CA  1 
ATOM   6751  C  C   . GLN G  1 15  ? 50.100  126.200 15.442  1.00 21.04 ? 15  GLN G C   1 
ATOM   6752  O  O   . GLN G  1 15  ? 49.935  126.843 14.403  1.00 20.00 ? 15  GLN G O   1 
ATOM   6753  C  CB  . GLN G  1 15  ? 48.139  125.078 16.494  1.00 16.92 ? 15  GLN G CB  1 
ATOM   6754  C  CG  . GLN G  1 15  ? 47.181  125.146 15.325  1.00 26.02 ? 15  GLN G CG  1 
ATOM   6755  C  CD  . GLN G  1 15  ? 46.239  123.956 15.282  1.00 33.16 ? 15  GLN G CD  1 
ATOM   6756  O  OE1 . GLN G  1 15  ? 45.253  123.876 16.045  1.00 33.94 ? 15  GLN G OE1 1 
ATOM   6757  N  NE2 . GLN G  1 15  ? 46.546  123.010 14.398  1.00 30.62 ? 15  GLN G NE2 1 
ATOM   6758  N  N   . GLY G  1 16  ? 51.146  125.407 15.669  1.00 15.46 ? 16  GLY G N   1 
ATOM   6759  C  CA  . GLY G  1 16  ? 52.149  125.160 14.662  1.00 13.99 ? 16  GLY G CA  1 
ATOM   6760  C  C   . GLY G  1 16  ? 53.221  124.160 15.054  1.00 17.88 ? 16  GLY G C   1 
ATOM   6761  O  O   . GLY G  1 16  ? 53.181  123.506 16.115  1.00 15.46 ? 16  GLY G O   1 
ATOM   6762  N  N   . ILE G  1 17  ? 54.182  124.036 14.151  1.00 16.85 ? 17  ILE G N   1 
ATOM   6763  C  CA  . ILE G  1 17  ? 55.269  123.099 14.273  1.00 15.71 ? 17  ILE G CA  1 
ATOM   6764  C  C   . ILE G  1 17  ? 56.523  123.820 13.865  1.00 16.05 ? 17  ILE G C   1 
ATOM   6765  O  O   . ILE G  1 17  ? 56.586  124.430 12.794  1.00 16.54 ? 17  ILE G O   1 
ATOM   6766  C  CB  . ILE G  1 17  ? 55.124  121.946 13.307  1.00 15.72 ? 17  ILE G CB  1 
ATOM   6767  C  CG1 . ILE G  1 17  ? 53.837  121.168 13.569  1.00 14.45 ? 17  ILE G CG1 1 
ATOM   6768  C  CG2 . ILE G  1 17  ? 56.335  121.013 13.423  1.00 15.23 ? 17  ILE G CG2 1 
ATOM   6769  C  CD1 . ILE G  1 17  ? 53.601  120.107 12.521  1.00 16.35 ? 17  ILE G CD1 1 
ATOM   6770  N  N   . ILE G  1 18  ? 57.525  123.738 14.722  1.00 15.02 ? 18  ILE G N   1 
ATOM   6771  C  CA  . ILE G  1 18  ? 58.793  124.392 14.482  1.00 13.59 ? 18  ILE G CA  1 
ATOM   6772  C  C   . ILE G  1 18  ? 59.938  123.380 14.547  1.00 16.07 ? 18  ILE G C   1 
ATOM   6773  O  O   . ILE G  1 18  ? 60.082  122.642 15.526  1.00 12.51 ? 18  ILE G O   1 
ATOM   6774  C  CB  . ILE G  1 18  ? 59.014  125.509 15.502  1.00 10.73 ? 18  ILE G CB  1 
ATOM   6775  C  CG1 . ILE G  1 18  ? 57.934  126.581 15.330  1.00 14.32 ? 18  ILE G CG1 1 
ATOM   6776  C  CG2 . ILE G  1 18  ? 60.376  126.106 15.317  1.00 13.61 ? 18  ILE G CG2 1 
ATOM   6777  C  CD1 . ILE G  1 18  ? 58.015  127.333 13.982  1.00 13.33 ? 18  ILE G CD1 1 
ATOM   6778  N  N   . ASN G  1 19  ? 60.757  123.379 13.499  1.00 12.95 ? 19  ASN G N   1 
ATOM   6779  C  CA  . ASN G  1 19  ? 61.902  122.498 13.383  1.00 12.67 ? 19  ASN G CA  1 
ATOM   6780  C  C   . ASN G  1 19  ? 63.220  123.216 13.645  1.00 12.50 ? 19  ASN G C   1 
ATOM   6781  O  O   . ASN G  1 19  ? 63.342  124.409 13.417  1.00 12.06 ? 19  ASN G O   1 
ATOM   6782  C  CB  . ASN G  1 19  ? 61.945  121.923 11.972  1.00 15.45 ? 19  ASN G CB  1 
ATOM   6783  C  CG  . ASN G  1 19  ? 60.665  121.235 11.596  1.00 15.07 ? 19  ASN G CG  1 
ATOM   6784  O  OD1 . ASN G  1 19  ? 60.417  120.104 12.016  1.00 14.33 ? 19  ASN G OD1 1 
ATOM   6785  N  ND2 . ASN G  1 19  ? 59.844  121.906 10.790  1.00 16.50 ? 19  ASN G ND2 1 
ATOM   6786  N  N   . PHE G  1 20  ? 64.211  122.462 14.104  1.00 13.83 ? 20  PHE G N   1 
ATOM   6787  C  CA  . PHE G  1 20  ? 65.535  122.991 14.414  1.00 12.56 ? 20  PHE G CA  1 
ATOM   6788  C  C   . PHE G  1 20  ? 66.562  122.069 13.806  1.00 14.67 ? 20  PHE G C   1 
ATOM   6789  O  O   . PHE G  1 20  ? 66.394  120.853 13.830  1.00 12.43 ? 20  PHE G O   1 
ATOM   6790  C  CB  . PHE G  1 20  ? 65.774  123.014 15.912  1.00 10.28 ? 20  PHE G CB  1 
ATOM   6791  C  CG  . PHE G  1 20  ? 64.836  123.900 16.674  1.00 9.47  ? 20  PHE G CG  1 
ATOM   6792  C  CD1 . PHE G  1 20  ? 63.569  123.460 17.016  1.00 11.89 ? 20  PHE G CD1 1 
ATOM   6793  C  CD2 . PHE G  1 20  ? 65.241  125.151 17.094  1.00 9.37  ? 20  PHE G CD2 1 
ATOM   6794  C  CE1 . PHE G  1 20  ? 62.702  124.265 17.744  1.00 9.31  ? 20  PHE G CE1 1 
ATOM   6795  C  CE2 . PHE G  1 20  ? 64.375  125.971 17.825  1.00 13.87 ? 20  PHE G CE2 1 
ATOM   6796  C  CZ  . PHE G  1 20  ? 63.104  125.521 18.141  1.00 11.20 ? 20  PHE G CZ  1 
ATOM   6797  N  N   . GLU G  1 21  ? 67.634  122.651 13.280  1.00 12.08 ? 21  GLU G N   1 
ATOM   6798  C  CA  . GLU G  1 21  ? 68.709  121.858 12.725  1.00 16.15 ? 21  GLU G CA  1 
ATOM   6799  C  C   . GLU G  1 21  ? 70.063  122.541 12.922  1.00 16.35 ? 21  GLU G C   1 
ATOM   6800  O  O   . GLU G  1 21  ? 70.221  123.720 12.620  1.00 14.18 ? 21  GLU G O   1 
ATOM   6801  C  CB  . GLU G  1 21  ? 68.463  121.573 11.247  1.00 14.96 ? 21  GLU G CB  1 
ATOM   6802  C  CG  . GLU G  1 21  ? 69.644  120.852 10.612  1.00 23.29 ? 21  GLU G CG  1 
ATOM   6803  C  CD  . GLU G  1 21  ? 69.530  120.717 9.105   1.00 34.51 ? 21  GLU G CD  1 
ATOM   6804  O  OE1 . GLU G  1 21  ? 69.929  119.650 8.595   1.00 36.29 ? 21  GLU G OE1 1 
ATOM   6805  O  OE2 . GLU G  1 21  ? 69.061  121.677 8.436   1.00 33.56 ? 21  GLU G OE2 1 
ATOM   6806  N  N   . GLN G  1 22  ? 71.037  121.801 13.444  1.00 17.57 ? 22  GLN G N   1 
ATOM   6807  C  CA  . GLN G  1 22  ? 72.369  122.362 13.691  1.00 15.50 ? 22  GLN G CA  1 
ATOM   6808  C  C   . GLN G  1 22  ? 73.397  121.365 13.189  1.00 18.45 ? 22  GLN G C   1 
ATOM   6809  O  O   . GLN G  1 22  ? 73.609  120.326 13.805  1.00 17.48 ? 22  GLN G O   1 
ATOM   6810  C  CB  . GLN G  1 22  ? 72.559  122.651 15.184  1.00 16.10 ? 22  GLN G CB  1 
ATOM   6811  C  CG  . GLN G  1 22  ? 73.898  123.292 15.555  1.00 11.43 ? 22  GLN G CG  1 
ATOM   6812  C  CD  . GLN G  1 22  ? 74.018  123.491 17.036  1.00 15.46 ? 22  GLN G CD  1 
ATOM   6813  O  OE1 . GLN G  1 22  ? 73.390  122.764 17.827  1.00 16.69 ? 22  GLN G OE1 1 
ATOM   6814  N  NE2 . GLN G  1 22  ? 74.799  124.496 17.443  1.00 11.28 ? 22  GLN G NE2 1 
ATOM   6815  N  N   . LYS G  1 23  ? 73.999  121.670 12.039  1.00 23.82 ? 23  LYS G N   1 
ATOM   6816  C  CA  . LYS G  1 23  ? 74.891  120.739 11.359  1.00 21.51 ? 23  LYS G CA  1 
ATOM   6817  C  C   . LYS G  1 23  ? 76.158  120.484 12.151  1.00 20.37 ? 23  LYS G C   1 
ATOM   6818  O  O   . LYS G  1 23  ? 76.654  119.374 12.177  1.00 28.02 ? 23  LYS G O   1 
ATOM   6819  C  CB  . LYS G  1 23  ? 75.259  121.263 9.975   1.00 23.74 ? 23  LYS G CB  1 
ATOM   6820  C  CG  . LYS G  1 23  ? 75.070  120.229 8.888   1.00 30.74 ? 23  LYS G CG  1 
ATOM   6821  C  CD  . LYS G  1 23  ? 73.810  120.490 8.073   1.00 35.35 ? 23  LYS G CD  1 
ATOM   6822  C  CE  . LYS G  1 23  ? 74.135  121.318 6.835   1.00 41.98 ? 23  LYS G CE  1 
ATOM   6823  N  NZ  . LYS G  1 23  ? 72.951  121.572 5.962   1.00 42.06 ? 23  LYS G NZ  1 
ATOM   6824  N  N   . GLU G  1 24  ? 76.662  121.522 12.805  1.00 20.47 ? 24  GLU G N   1 
ATOM   6825  C  CA  . GLU G  1 24  ? 77.924  121.461 13.527  1.00 18.32 ? 24  GLU G CA  1 
ATOM   6826  C  C   . GLU G  1 24  ? 77.701  121.998 14.908  1.00 19.82 ? 24  GLU G C   1 
ATOM   6827  O  O   . GLU G  1 24  ? 77.000  122.996 15.073  1.00 18.63 ? 24  GLU G O   1 
ATOM   6828  C  CB  . GLU G  1 24  ? 78.965  122.339 12.832  1.00 20.70 ? 24  GLU G CB  1 
ATOM   6829  C  CG  . GLU G  1 24  ? 79.116  122.067 11.329  1.00 26.02 ? 24  GLU G CG  1 
ATOM   6830  C  CD  . GLU G  1 24  ? 80.057  120.906 11.028  1.00 35.97 ? 24  GLU G CD  1 
ATOM   6831  O  OE1 . GLU G  1 24  ? 80.301  120.082 11.939  1.00 35.14 ? 24  GLU G OE1 1 
ATOM   6832  O  OE2 . GLU G  1 24  ? 80.559  120.824 9.880   1.00 36.60 ? 24  GLU G OE2 1 
ATOM   6833  N  N   . SER G  1 25  ? 78.316  121.362 15.898  1.00 19.06 ? 25  SER G N   1 
ATOM   6834  C  CA  . SER G  1 25  ? 78.067  121.705 17.286  1.00 18.05 ? 25  SER G CA  1 
ATOM   6835  C  C   . SER G  1 25  ? 78.509  123.117 17.599  1.00 19.60 ? 25  SER G C   1 
ATOM   6836  O  O   . SER G  1 25  ? 78.000  123.728 18.539  1.00 17.06 ? 25  SER G O   1 
ATOM   6837  C  CB  . SER G  1 25  ? 78.757  120.716 18.242  1.00 20.45 ? 25  SER G CB  1 
ATOM   6838  O  OG  . SER G  1 25  ? 80.180  120.788 18.156  1.00 20.87 ? 25  SER G OG  1 
ATOM   6839  N  N   . ASN G  1 26  ? 79.463  123.635 16.825  1.00 14.68 ? 26  ASN G N   1 
ATOM   6840  C  CA  . ASN G  1 26  ? 79.863  125.018 17.005  1.00 16.12 ? 26  ASN G CA  1 
ATOM   6841  C  C   . ASN G  1 26  ? 79.359  125.964 15.897  1.00 18.25 ? 26  ASN G C   1 
ATOM   6842  O  O   . ASN G  1 26  ? 79.882  127.059 15.721  1.00 19.55 ? 26  ASN G O   1 
ATOM   6843  C  CB  . ASN G  1 26  ? 81.381  125.139 17.228  1.00 17.72 ? 26  ASN G CB  1 
ATOM   6844  C  CG  . ASN G  1 26  ? 82.193  124.902 15.959  1.00 18.78 ? 26  ASN G CG  1 
ATOM   6845  O  OD1 . ASN G  1 26  ? 81.761  124.192 15.030  1.00 19.20 ? 26  ASN G OD1 1 
ATOM   6846  N  ND2 . ASN G  1 26  ? 83.389  125.494 15.917  1.00 16.41 ? 26  ASN G ND2 1 
ATOM   6847  N  N   . GLY G  1 27  ? 78.314  125.554 15.184  1.00 18.65 ? 27  GLY G N   1 
ATOM   6848  C  CA  . GLY G  1 27  ? 77.739  126.388 14.135  1.00 18.05 ? 27  GLY G CA  1 
ATOM   6849  C  C   . GLY G  1 27  ? 76.308  126.823 14.409  1.00 16.22 ? 27  GLY G C   1 
ATOM   6850  O  O   . GLY G  1 27  ? 75.748  126.505 15.450  1.00 16.13 ? 27  GLY G O   1 
ATOM   6851  N  N   . PRO G  1 28  ? 75.710  127.561 13.468  1.00 18.85 ? 28  PRO G N   1 
ATOM   6852  C  CA  . PRO G  1 28  ? 74.364  128.124 13.645  1.00 16.68 ? 28  PRO G CA  1 
ATOM   6853  C  C   . PRO G  1 28  ? 73.273  127.055 13.726  1.00 15.95 ? 28  PRO G C   1 
ATOM   6854  O  O   . PRO G  1 28  ? 73.484  125.894 13.359  1.00 16.71 ? 28  PRO G O   1 
ATOM   6855  C  CB  . PRO G  1 28  ? 74.145  128.946 12.362  1.00 17.39 ? 28  PRO G CB  1 
ATOM   6856  C  CG  . PRO G  1 28  ? 75.410  129.003 11.666  1.00 16.82 ? 28  PRO G CG  1 
ATOM   6857  C  CD  . PRO G  1 28  ? 76.281  127.882 12.151  1.00 16.21 ? 28  PRO G CD  1 
ATOM   6858  N  N   . VAL G  1 29  ? 72.103  127.462 14.204  1.00 18.47 ? 29  VAL G N   1 
ATOM   6859  C  CA  . VAL G  1 29  ? 70.924  126.606 14.196  1.00 13.89 ? 29  VAL G CA  1 
ATOM   6860  C  C   . VAL G  1 29  ? 69.906  127.210 13.251  1.00 15.81 ? 29  VAL G C   1 
ATOM   6861  O  O   . VAL G  1 29  ? 69.562  128.386 13.360  1.00 16.30 ? 29  VAL G O   1 
ATOM   6862  C  CB  . VAL G  1 29  ? 70.312  126.470 15.590  1.00 14.20 ? 29  VAL G CB  1 
ATOM   6863  C  CG1 . VAL G  1 29  ? 69.066  125.569 15.552  1.00 9.97  ? 29  VAL G CG1 1 
ATOM   6864  C  CG2 . VAL G  1 29  ? 71.371  125.928 16.566  1.00 13.90 ? 29  VAL G CG2 1 
ATOM   6865  N  N   . LYS G  1 30  ? 69.450  126.417 12.297  1.00 13.04 ? 30  LYS G N   1 
ATOM   6866  C  CA  . LYS G  1 30  ? 68.358  126.847 11.453  1.00 18.26 ? 30  LYS G CA  1 
ATOM   6867  C  C   . LYS G  1 30  ? 67.053  126.519 12.154  1.00 17.62 ? 30  LYS G C   1 
ATOM   6868  O  O   . LYS G  1 30  ? 66.886  125.417 12.681  1.00 15.21 ? 30  LYS G O   1 
ATOM   6869  C  CB  . LYS G  1 30  ? 68.430  126.147 10.107  1.00 17.29 ? 30  LYS G CB  1 
ATOM   6870  C  CG  . LYS G  1 30  ? 69.692  126.494 9.356   1.00 21.33 ? 30  LYS G CG  1 
ATOM   6871  C  CD  . LYS G  1 30  ? 69.692  125.880 7.980   1.00 22.78 ? 30  LYS G CD  1 
ATOM   6872  C  CE  . LYS G  1 30  ? 70.930  126.303 7.202   1.00 29.12 ? 30  LYS G CE  1 
ATOM   6873  N  NZ  . LYS G  1 30  ? 70.946  125.686 5.840   1.00 33.26 ? 30  LYS G NZ  1 
ATOM   6874  N  N   . VAL G  1 31  ? 66.136  127.485 12.166  1.00 17.70 ? 31  VAL G N   1 
ATOM   6875  C  CA  . VAL G  1 31  ? 64.843  127.324 12.817  1.00 14.84 ? 31  VAL G CA  1 
ATOM   6876  C  C   . VAL G  1 31  ? 63.759  127.591 11.793  1.00 19.33 ? 31  VAL G C   1 
ATOM   6877  O  O   . VAL G  1 31  ? 63.739  128.659 11.170  1.00 19.09 ? 31  VAL G O   1 
ATOM   6878  C  CB  . VAL G  1 31  ? 64.668  128.314 13.991  1.00 17.86 ? 31  VAL G CB  1 
ATOM   6879  C  CG1 . VAL G  1 31  ? 63.278  128.185 14.589  1.00 15.58 ? 31  VAL G CG1 1 
ATOM   6880  C  CG2 . VAL G  1 31  ? 65.736  128.102 15.072  1.00 10.45 ? 31  VAL G CG2 1 
ATOM   6881  N  N   . TRP G  1 32  ? 62.847  126.641 11.606  1.00 14.75 ? 32  TRP G N   1 
ATOM   6882  C  CA  . TRP G  1 32  ? 61.849  126.835 10.573  1.00 15.63 ? 32  TRP G CA  1 
ATOM   6883  C  C   . TRP G  1 32  ? 60.576  126.053 10.764  1.00 17.23 ? 32  TRP G C   1 
ATOM   6884  O  O   . TRP G  1 32  ? 60.559  124.987 11.373  1.00 16.70 ? 32  TRP G O   1 
ATOM   6885  C  CB  . TRP G  1 32  ? 62.443  126.466 9.220   1.00 21.42 ? 32  TRP G CB  1 
ATOM   6886  C  CG  . TRP G  1 32  ? 62.785  125.012 9.088   1.00 20.06 ? 32  TRP G CG  1 
ATOM   6887  C  CD1 . TRP G  1 32  ? 63.941  124.390 9.494   1.00 17.50 ? 32  TRP G CD1 1 
ATOM   6888  C  CD2 . TRP G  1 32  ? 61.976  123.997 8.491   1.00 18.35 ? 32  TRP G CD2 1 
ATOM   6889  N  NE1 . TRP G  1 32  ? 63.888  123.044 9.186   1.00 15.02 ? 32  TRP G NE1 1 
ATOM   6890  C  CE2 . TRP G  1 32  ? 62.696  122.782 8.569   1.00 15.48 ? 32  TRP G CE2 1 
ATOM   6891  C  CE3 . TRP G  1 32  ? 60.712  123.994 7.904   1.00 20.76 ? 32  TRP G CE3 1 
ATOM   6892  C  CZ2 . TRP G  1 32  ? 62.191  121.593 8.088   1.00 21.86 ? 32  TRP G CZ2 1 
ATOM   6893  C  CZ3 . TRP G  1 32  ? 60.212  122.809 7.422   1.00 21.62 ? 32  TRP G CZ3 1 
ATOM   6894  C  CH2 . TRP G  1 32  ? 60.947  121.621 7.518   1.00 22.22 ? 32  TRP G CH2 1 
ATOM   6895  N  N   . GLY G  1 33  ? 59.506  126.586 10.196  1.00 18.61 ? 33  GLY G N   1 
ATOM   6896  C  CA  . GLY G  1 33  ? 58.231  125.916 10.212  1.00 17.34 ? 33  GLY G CA  1 
ATOM   6897  C  C   . GLY G  1 33  ? 57.117  126.917 10.012  1.00 20.97 ? 33  GLY G C   1 
ATOM   6898  O  O   . GLY G  1 33  ? 57.306  127.960 9.379   1.00 20.47 ? 33  GLY G O   1 
ATOM   6899  N  N   . SER G  1 34  ? 55.953  126.606 10.560  1.00 16.49 ? 34  SER G N   1 
ATOM   6900  C  CA  . SER G  1 34  ? 54.789  127.428 10.312  1.00 21.17 ? 34  SER G CA  1 
ATOM   6901  C  C   . SER G  1 34  ? 53.837  127.438 11.492  1.00 18.98 ? 34  SER G C   1 
ATOM   6902  O  O   . SER G  1 34  ? 53.624  126.421 12.149  1.00 19.47 ? 34  SER G O   1 
ATOM   6903  C  CB  . SER G  1 34  ? 54.066  126.943 9.058   1.00 20.06 ? 34  SER G CB  1 
ATOM   6904  O  OG  . SER G  1 34  ? 53.098  127.898 8.656   1.00 26.54 ? 34  SER G OG  1 
ATOM   6905  N  N   . ILE G  1 35  ? 53.275  128.603 11.769  1.00 20.36 ? 35  ILE G N   1 
ATOM   6906  C  CA  . ILE G  1 35  ? 52.293  128.739 12.825  1.00 15.40 ? 35  ILE G CA  1 
ATOM   6907  C  C   . ILE G  1 35  ? 51.094  129.440 12.223  1.00 21.64 ? 35  ILE G C   1 
ATOM   6908  O  O   . ILE G  1 35  ? 51.236  130.421 11.483  1.00 22.86 ? 35  ILE G O   1 
ATOM   6909  C  CB  . ILE G  1 35  ? 52.811  129.606 13.977  1.00 16.15 ? 35  ILE G CB  1 
ATOM   6910  C  CG1 . ILE G  1 35  ? 54.193  129.137 14.446  1.00 16.82 ? 35  ILE G CG1 1 
ATOM   6911  C  CG2 . ILE G  1 35  ? 51.815  129.584 15.137  1.00 13.78 ? 35  ILE G CG2 1 
ATOM   6912  C  CD1 . ILE G  1 35  ? 54.965  130.192 15.294  1.00 12.02 ? 35  ILE G CD1 1 
ATOM   6913  N  N   . LYS G  1 36  ? 49.911  128.946 12.540  1.00 21.82 ? 36  LYS G N   1 
ATOM   6914  C  CA  . LYS G  1 36  ? 48.694  129.531 12.007  1.00 26.14 ? 36  LYS G CA  1 
ATOM   6915  C  C   . LYS G  1 36  ? 47.822  129.921 13.170  1.00 23.50 ? 36  LYS G C   1 
ATOM   6916  O  O   . LYS G  1 36  ? 48.122  129.564 14.310  1.00 21.50 ? 36  LYS G O   1 
ATOM   6917  C  CB  . LYS G  1 36  ? 47.960  128.507 11.145  1.00 24.42 ? 36  LYS G CB  1 
ATOM   6918  C  CG  . LYS G  1 36  ? 47.348  127.381 11.966  1.00 26.43 ? 36  LYS G CG  1 
ATOM   6919  C  CD  . LYS G  1 36  ? 47.066  126.164 11.102  1.00 30.19 ? 36  LYS G CD  1 
ATOM   6920  C  CE  . LYS G  1 36  ? 46.026  125.271 11.747  1.00 28.62 ? 36  LYS G CE  1 
ATOM   6921  N  NZ  . LYS G  1 36  ? 45.918  123.990 11.023  1.00 33.02 ? 36  LYS G NZ  1 
ATOM   6922  N  N   . GLY G  1 37  ? 46.733  130.635 12.880  1.00 27.84 ? 37  GLY G N   1 
ATOM   6923  C  CA  . GLY G  1 37  ? 45.763  131.007 13.897  1.00 18.01 ? 37  GLY G CA  1 
ATOM   6924  C  C   . GLY G  1 37  ? 46.115  132.332 14.552  1.00 23.86 ? 37  GLY G C   1 
ATOM   6925  O  O   . GLY G  1 37  ? 45.487  132.735 15.533  1.00 26.33 ? 37  GLY G O   1 
ATOM   6926  N  N   . LEU G  1 38  ? 47.128  133.012 14.018  1.00 24.88 ? 38  LEU G N   1 
ATOM   6927  C  CA  . LEU G  1 38  ? 47.638  134.230 14.648  1.00 26.21 ? 38  LEU G CA  1 
ATOM   6928  C  C   . LEU G  1 38  ? 47.052  135.484 14.025  1.00 31.43 ? 38  LEU G C   1 
ATOM   6929  O  O   . LEU G  1 38  ? 46.825  135.536 12.815  1.00 29.89 ? 38  LEU G O   1 
ATOM   6930  C  CB  . LEU G  1 38  ? 49.156  134.310 14.499  1.00 27.95 ? 38  LEU G CB  1 
ATOM   6931  C  CG  . LEU G  1 38  ? 50.045  133.328 15.259  1.00 19.04 ? 38  LEU G CG  1 
ATOM   6932  C  CD1 . LEU G  1 38  ? 51.388  133.338 14.617  1.00 17.01 ? 38  LEU G CD1 1 
ATOM   6933  C  CD2 . LEU G  1 38  ? 50.152  133.757 16.698  1.00 18.63 ? 38  LEU G CD2 1 
ATOM   6934  N  N   . THR G  1 39  ? 46.841  136.510 14.843  1.00 28.71 ? 39  THR G N   1 
ATOM   6935  C  CA  . THR G  1 39  ? 46.506  137.819 14.302  1.00 32.45 ? 39  THR G CA  1 
ATOM   6936  C  C   . THR G  1 39  ? 47.611  138.279 13.358  1.00 31.32 ? 39  THR G C   1 
ATOM   6937  O  O   . THR G  1 39  ? 48.778  137.913 13.520  1.00 33.13 ? 39  THR G O   1 
ATOM   6938  C  CB  . THR G  1 39  ? 46.348  138.874 15.404  1.00 33.21 ? 39  THR G CB  1 
ATOM   6939  O  OG1 . THR G  1 39  ? 47.628  139.147 15.984  1.00 34.15 ? 39  THR G OG1 1 
ATOM   6940  C  CG2 . THR G  1 39  ? 45.386  138.405 16.470  1.00 27.61 ? 39  THR G CG2 1 
ATOM   6941  N  N   . GLU G  1 40  ? 47.237  139.076 12.365  1.00 33.47 ? 40  GLU G N   1 
ATOM   6942  C  CA  . GLU G  1 40  ? 48.185  139.605 11.391  1.00 32.08 ? 40  GLU G CA  1 
ATOM   6943  C  C   . GLU G  1 40  ? 49.255  140.448 12.086  1.00 31.36 ? 40  GLU G C   1 
ATOM   6944  O  O   . GLU G  1 40  ? 48.958  141.181 13.031  1.00 29.27 ? 40  GLU G O   1 
ATOM   6945  C  CB  . GLU G  1 40  ? 47.439  140.464 10.369  1.00 30.45 ? 40  GLU G CB  1 
ATOM   6946  C  CG  . GLU G  1 40  ? 48.206  140.728 9.095   1.00 32.85 ? 40  GLU G CG  1 
ATOM   6947  C  CD  . GLU G  1 40  ? 47.396  141.553 8.099   1.00 40.21 ? 40  GLU G CD  1 
ATOM   6948  O  OE1 . GLU G  1 40  ? 46.228  141.891 8.398   1.00 41.32 ? 40  GLU G OE1 1 
ATOM   6949  O  OE2 . GLU G  1 40  ? 47.932  141.864 7.019   1.00 36.95 ? 40  GLU G OE2 1 
ATOM   6950  N  N   . GLY G  1 41  ? 50.499  140.335 11.629  1.00 29.89 ? 41  GLY G N   1 
ATOM   6951  C  CA  . GLY G  1 41  ? 51.566  141.139 12.197  1.00 32.26 ? 41  GLY G CA  1 
ATOM   6952  C  C   . GLY G  1 41  ? 52.586  140.407 13.054  1.00 28.12 ? 41  GLY G C   1 
ATOM   6953  O  O   . GLY G  1 41  ? 52.858  139.225 12.858  1.00 30.11 ? 41  GLY G O   1 
ATOM   6954  N  N   . LEU G  1 42  ? 53.152  141.123 14.014  1.00 29.06 ? 42  LEU G N   1 
ATOM   6955  C  CA  . LEU G  1 42  ? 54.322  140.640 14.736  1.00 28.37 ? 42  LEU G CA  1 
ATOM   6956  C  C   . LEU G  1 42  ? 53.975  139.871 16.013  1.00 25.20 ? 42  LEU G C   1 
ATOM   6957  O  O   . LEU G  1 42  ? 53.063  140.243 16.742  1.00 28.04 ? 42  LEU G O   1 
ATOM   6958  C  CB  . LEU G  1 42  ? 55.244  141.813 15.067  1.00 27.35 ? 42  LEU G CB  1 
ATOM   6959  C  CG  . LEU G  1 42  ? 56.443  142.081 14.159  1.00 30.57 ? 42  LEU G CG  1 
ATOM   6960  C  CD1 . LEU G  1 42  ? 56.426  141.185 12.940  1.00 29.64 ? 42  LEU G CD1 1 
ATOM   6961  C  CD2 . LEU G  1 42  ? 56.454  143.526 13.749  1.00 28.51 ? 42  LEU G CD2 1 
ATOM   6962  N  N   . HIS G  1 43  ? 54.715  138.803 16.283  1.00 21.26 ? 43  HIS G N   1 
ATOM   6963  C  CA  . HIS G  1 43  ? 54.520  138.050 17.509  1.00 22.17 ? 43  HIS G CA  1 
ATOM   6964  C  C   . HIS G  1 43  ? 55.845  137.632 18.163  1.00 19.05 ? 43  HIS G C   1 
ATOM   6965  O  O   . HIS G  1 43  ? 56.701  137.036 17.512  1.00 19.61 ? 43  HIS G O   1 
ATOM   6966  C  CB  . HIS G  1 43  ? 53.665  136.826 17.200  1.00 20.17 ? 43  HIS G CB  1 
ATOM   6967  C  CG  . HIS G  1 43  ? 52.277  137.168 16.777  1.00 23.47 ? 43  HIS G CG  1 
ATOM   6968  N  ND1 . HIS G  1 43  ? 51.258  137.389 17.682  1.00 25.78 ? 43  HIS G ND1 1 
ATOM   6969  C  CD2 . HIS G  1 43  ? 51.740  137.363 15.548  1.00 24.02 ? 43  HIS G CD2 1 
ATOM   6970  C  CE1 . HIS G  1 43  ? 50.151  137.687 17.026  1.00 24.23 ? 43  HIS G CE1 1 
ATOM   6971  N  NE2 . HIS G  1 43  ? 50.416  137.682 15.732  1.00 23.01 ? 43  HIS G NE2 1 
ATOM   6972  N  N   . GLY G  1 44  ? 55.999  137.944 19.447  1.00 19.43 ? 44  GLY G N   1 
ATOM   6973  C  CA  . GLY G  1 44  ? 57.165  137.540 20.215  1.00 21.08 ? 44  GLY G CA  1 
ATOM   6974  C  C   . GLY G  1 44  ? 57.424  136.045 20.159  1.00 15.97 ? 44  GLY G C   1 
ATOM   6975  O  O   . GLY G  1 44  ? 56.509  135.239 20.215  1.00 15.74 ? 44  GLY G O   1 
ATOM   6976  N  N   . PHE G  1 45  ? 58.688  135.675 20.053  1.00 15.78 ? 45  PHE G N   1 
ATOM   6977  C  CA  . PHE G  1 45  ? 59.065  134.288 19.781  1.00 15.69 ? 45  PHE G CA  1 
ATOM   6978  C  C   . PHE G  1 45  ? 60.270  133.972 20.652  1.00 15.93 ? 45  PHE G C   1 
ATOM   6979  O  O   . PHE G  1 45  ? 61.378  134.396 20.343  1.00 16.00 ? 45  PHE G O   1 
ATOM   6980  C  CB  . PHE G  1 45  ? 59.412  134.166 18.307  1.00 13.51 ? 45  PHE G CB  1 
ATOM   6981  C  CG  . PHE G  1 45  ? 59.474  132.755 17.781  1.00 13.37 ? 45  PHE G CG  1 
ATOM   6982  C  CD1 . PHE G  1 45  ? 58.438  131.862 17.994  1.00 15.49 ? 45  PHE G CD1 1 
ATOM   6983  C  CD2 . PHE G  1 45  ? 60.556  132.348 17.002  1.00 13.04 ? 45  PHE G CD2 1 
ATOM   6984  C  CE1 . PHE G  1 45  ? 58.478  130.571 17.452  1.00 13.10 ? 45  PHE G CE1 1 
ATOM   6985  C  CE2 . PHE G  1 45  ? 60.623  131.064 16.473  1.00 13.55 ? 45  PHE G CE2 1 
ATOM   6986  C  CZ  . PHE G  1 45  ? 59.573  130.166 16.700  1.00 14.07 ? 45  PHE G CZ  1 
ATOM   6987  N  N   . HIS G  1 46  ? 60.042  133.243 21.745  1.00 12.44 ? 46  HIS G N   1 
ATOM   6988  C  CA  . HIS G  1 46  ? 61.051  133.049 22.770  1.00 11.09 ? 46  HIS G CA  1 
ATOM   6989  C  C   . HIS G  1 46  ? 61.250  131.590 23.131  1.00 16.14 ? 46  HIS G C   1 
ATOM   6990  O  O   . HIS G  1 46  ? 60.311  130.782 23.040  1.00 10.78 ? 46  HIS G O   1 
ATOM   6991  C  CB  . HIS G  1 46  ? 60.623  133.718 24.061  1.00 13.37 ? 46  HIS G CB  1 
ATOM   6992  C  CG  . HIS G  1 46  ? 60.243  135.150 23.910  1.00 14.24 ? 46  HIS G CG  1 
ATOM   6993  N  ND1 . HIS G  1 46  ? 59.162  135.695 24.560  1.00 13.71 ? 46  HIS G ND1 1 
ATOM   6994  C  CD2 . HIS G  1 46  ? 60.811  136.155 23.204  1.00 15.19 ? 46  HIS G CD2 1 
ATOM   6995  C  CE1 . HIS G  1 46  ? 59.072  136.975 24.255  1.00 20.24 ? 46  HIS G CE1 1 
ATOM   6996  N  NE2 . HIS G  1 46  ? 60.062  137.279 23.433  1.00 18.95 ? 46  HIS G NE2 1 
ATOM   6997  N  N   . VAL G  1 47  ? 62.467  131.272 23.583  1.00 10.11 ? 47  VAL G N   1 
ATOM   6998  C  CA  . VAL G  1 47  ? 62.692  130.017 24.274  1.00 12.26 ? 47  VAL G CA  1 
ATOM   6999  C  C   . VAL G  1 47  ? 62.670  130.366 25.746  1.00 12.28 ? 47  VAL G C   1 
ATOM   7000  O  O   . VAL G  1 47  ? 63.485  131.174 26.199  1.00 14.39 ? 47  VAL G O   1 
ATOM   7001  C  CB  . VAL G  1 47  ? 64.043  129.382 23.932  1.00 10.16 ? 47  VAL G CB  1 
ATOM   7002  C  CG1 . VAL G  1 47  ? 64.254  128.116 24.770  1.00 8.38  ? 47  VAL G CG1 1 
ATOM   7003  C  CG2 . VAL G  1 47  ? 64.112  129.059 22.428  1.00 10.51 ? 47  VAL G CG2 1 
ATOM   7004  N  N   . HIS G  1 48  ? 61.714  129.796 26.470  1.00 9.71  ? 48  HIS G N   1 
ATOM   7005  C  CA  . HIS G  1 48  ? 61.627  129.963 27.919  1.00 14.60 ? 48  HIS G CA  1 
ATOM   7006  C  C   . HIS G  1 48  ? 62.413  128.892 28.669  1.00 11.23 ? 48  HIS G C   1 
ATOM   7007  O  O   . HIS G  1 48  ? 62.742  127.867 28.111  1.00 11.94 ? 48  HIS G O   1 
ATOM   7008  C  CB  . HIS G  1 48  ? 60.165  130.003 28.361  1.00 12.96 ? 48  HIS G CB  1 
ATOM   7009  C  CG  . HIS G  1 48  ? 59.490  131.276 27.984  1.00 15.89 ? 48  HIS G CG  1 
ATOM   7010  N  ND1 . HIS G  1 48  ? 59.093  132.209 28.915  1.00 15.00 ? 48  HIS G ND1 1 
ATOM   7011  C  CD2 . HIS G  1 48  ? 59.213  131.810 26.771  1.00 12.61 ? 48  HIS G CD2 1 
ATOM   7012  C  CE1 . HIS G  1 48  ? 58.561  133.244 28.295  1.00 12.97 ? 48  HIS G CE1 1 
ATOM   7013  N  NE2 . HIS G  1 48  ? 58.613  133.023 26.996  1.00 15.92 ? 48  HIS G NE2 1 
ATOM   7014  N  N   . GLU G  1 49  ? 62.726  129.138 29.930  1.00 12.32 ? 49  GLU G N   1 
ATOM   7015  C  CA  . GLU G  1 49  ? 63.695  128.290 30.624  1.00 14.01 ? 49  GLU G CA  1 
ATOM   7016  C  C   . GLU G  1 49  ? 63.250  126.822 30.855  1.00 13.20 ? 49  GLU G C   1 
ATOM   7017  O  O   . GLU G  1 49  ? 64.041  125.891 30.701  1.00 12.32 ? 49  GLU G O   1 
ATOM   7018  C  CB  . GLU G  1 49  ? 64.138  128.949 31.936  1.00 13.56 ? 49  GLU G CB  1 
ATOM   7019  C  CG  . GLU G  1 49  ? 65.053  128.074 32.806  1.00 14.41 ? 49  GLU G CG  1 
ATOM   7020  C  CD  . GLU G  1 49  ? 65.565  128.784 34.057  1.00 16.46 ? 49  GLU G CD  1 
ATOM   7021  O  OE1 . GLU G  1 49  ? 65.089  129.892 34.369  1.00 17.51 ? 49  GLU G OE1 1 
ATOM   7022  O  OE2 . GLU G  1 49  ? 66.452  128.226 34.739  1.00 21.40 ? 49  GLU G OE2 1 
ATOM   7023  N  N   . PHE G  1 50  ? 61.999  126.600 31.211  1.00 10.61 ? 50  PHE G N   1 
ATOM   7024  C  CA  . PHE G  1 50  ? 61.602  125.243 31.596  1.00 12.14 ? 50  PHE G CA  1 
ATOM   7025  C  C   . PHE G  1 50  ? 60.688  124.543 30.586  1.00 11.75 ? 50  PHE G C   1 
ATOM   7026  O  O   . PHE G  1 50  ? 59.805  125.166 30.020  1.00 14.12 ? 50  PHE G O   1 
ATOM   7027  C  CB  . PHE G  1 50  ? 60.971  125.236 33.005  1.00 12.15 ? 50  PHE G CB  1 
ATOM   7028  C  CG  . PHE G  1 50  ? 61.822  125.920 34.051  1.00 12.50 ? 50  PHE G CG  1 
ATOM   7029  C  CD1 . PHE G  1 50  ? 63.043  125.396 34.420  1.00 12.02 ? 50  PHE G CD1 1 
ATOM   7030  C  CD2 . PHE G  1 50  ? 61.406  127.105 34.637  1.00 17.74 ? 50  PHE G CD2 1 
ATOM   7031  C  CE1 . PHE G  1 50  ? 63.830  126.035 35.365  1.00 19.22 ? 50  PHE G CE1 1 
ATOM   7032  C  CE2 . PHE G  1 50  ? 62.182  127.749 35.587  1.00 16.84 ? 50  PHE G CE2 1 
ATOM   7033  C  CZ  . PHE G  1 50  ? 63.400  127.210 35.952  1.00 19.41 ? 50  PHE G CZ  1 
ATOM   7034  N  N   . GLY G  1 51  ? 60.922  123.245 30.376  1.00 10.35 ? 51  GLY G N   1 
ATOM   7035  C  CA  . GLY G  1 51  ? 60.044  122.383 29.606  1.00 9.48  ? 51  GLY G CA  1 
ATOM   7036  C  C   . GLY G  1 51  ? 58.935  121.816 30.489  1.00 10.80 ? 51  GLY G C   1 
ATOM   7037  O  O   . GLY G  1 51  ? 58.632  120.626 30.481  1.00 10.38 ? 51  GLY G O   1 
ATOM   7038  N  N   . ASP G  1 52  ? 58.357  122.696 31.287  1.00 12.24 ? 52  ASP G N   1 
ATOM   7039  C  CA  . ASP G  1 52  ? 57.351  122.327 32.255  1.00 14.88 ? 52  ASP G CA  1 
ATOM   7040  C  C   . ASP G  1 52  ? 56.015  122.893 31.813  1.00 15.75 ? 52  ASP G C   1 
ATOM   7041  O  O   . ASP G  1 52  ? 55.790  124.099 31.893  1.00 15.79 ? 52  ASP G O   1 
ATOM   7042  C  CB  . ASP G  1 52  ? 57.737  122.889 33.624  1.00 16.39 ? 52  ASP G CB  1 
ATOM   7043  C  CG  . ASP G  1 52  ? 56.800  122.447 34.725  1.00 16.02 ? 52  ASP G CG  1 
ATOM   7044  O  OD1 . ASP G  1 52  ? 55.663  122.047 34.405  1.00 15.45 ? 52  ASP G OD1 1 
ATOM   7045  O  OD2 . ASP G  1 52  ? 57.195  122.513 35.908  1.00 15.93 ? 52  ASP G OD2 1 
ATOM   7046  N  N   . ASN G  1 53  ? 55.143  122.003 31.349  1.00 19.38 ? 53  ASN G N   1 
ATOM   7047  C  CA  . ASN G  1 53  ? 53.789  122.354 30.915  1.00 21.56 ? 53  ASN G CA  1 
ATOM   7048  C  C   . ASN G  1 53  ? 52.705  121.930 31.916  1.00 21.29 ? 53  ASN G C   1 
ATOM   7049  O  O   . ASN G  1 53  ? 51.536  121.791 31.545  1.00 22.77 ? 53  ASN G O   1 
ATOM   7050  C  CB  . ASN G  1 53  ? 53.503  121.673 29.584  1.00 20.76 ? 53  ASN G CB  1 
ATOM   7051  C  CG  . ASN G  1 53  ? 52.368  122.326 28.820  1.00 29.71 ? 53  ASN G CG  1 
ATOM   7052  O  OD1 . ASN G  1 53  ? 52.298  123.553 28.715  1.00 28.81 ? 53  ASN G OD1 1 
ATOM   7053  N  ND2 . ASN G  1 53  ? 51.466  121.503 28.278  1.00 28.77 ? 53  ASN G ND2 1 
ATOM   7054  N  N   . THR G  1 54  ? 53.091  121.695 33.170  1.00 19.72 ? 54  THR G N   1 
ATOM   7055  C  CA  . THR G  1 54  ? 52.147  121.197 34.170  1.00 20.81 ? 54  THR G CA  1 
ATOM   7056  C  C   . THR G  1 54  ? 51.008  122.177 34.434  1.00 25.87 ? 54  THR G C   1 
ATOM   7057  O  O   . THR G  1 54  ? 49.886  121.770 34.697  1.00 23.37 ? 54  THR G O   1 
ATOM   7058  C  CB  . THR G  1 54  ? 52.818  120.864 35.513  1.00 17.07 ? 54  THR G CB  1 
ATOM   7059  O  OG1 . THR G  1 54  ? 53.505  122.019 36.011  1.00 18.48 ? 54  THR G OG1 1 
ATOM   7060  C  CG2 . THR G  1 54  ? 53.781  119.693 35.365  1.00 16.13 ? 54  THR G CG2 1 
ATOM   7061  N  N   . ALA G  1 55  ? 51.315  123.467 34.379  1.00 28.64 ? 55  ALA G N   1 
ATOM   7062  C  CA  . ALA G  1 55  ? 50.290  124.504 34.461  1.00 27.87 ? 55  ALA G CA  1 
ATOM   7063  C  C   . ALA G  1 55  ? 50.197  125.251 33.127  1.00 24.92 ? 55  ALA G C   1 
ATOM   7064  O  O   . ALA G  1 55  ? 50.064  126.468 33.087  1.00 29.01 ? 55  ALA G O   1 
ATOM   7065  C  CB  . ALA G  1 55  ? 50.600  125.456 35.588  1.00 20.66 ? 55  ALA G CB  1 
ATOM   7066  N  N   . GLY G  1 56  ? 50.276  124.510 32.031  1.00 25.06 ? 56  GLY G N   1 
ATOM   7067  C  CA  . GLY G  1 56  ? 50.239  125.118 30.717  1.00 28.48 ? 56  GLY G CA  1 
ATOM   7068  C  C   . GLY G  1 56  ? 51.508  125.908 30.487  1.00 28.07 ? 56  GLY G C   1 
ATOM   7069  O  O   . GLY G  1 56  ? 52.578  125.501 30.935  1.00 26.82 ? 56  GLY G O   1 
ATOM   7070  N  N   . SER G  1 57  ? 51.387  127.046 29.809  1.00 28.99 ? 57  SER G N   1 
ATOM   7071  C  CA  . SER G  1 57  ? 52.544  127.880 29.476  1.00 27.60 ? 57  SER G CA  1 
ATOM   7072  C  C   . SER G  1 57  ? 53.079  128.696 30.658  1.00 29.04 ? 57  SER G C   1 
ATOM   7073  O  O   . SER G  1 57  ? 54.178  129.247 30.581  1.00 30.34 ? 57  SER G O   1 
ATOM   7074  C  CB  . SER G  1 57  ? 52.192  128.823 28.327  1.00 29.45 ? 57  SER G CB  1 
ATOM   7075  O  OG  . SER G  1 57  ? 50.987  129.511 28.598  1.00 28.60 ? 57  SER G OG  1 
ATOM   7076  N  N   . THR G  1 58  ? 52.313  128.767 31.746  1.00 27.77 ? 58  THR G N   1 
ATOM   7077  C  CA  . THR G  1 58  ? 52.676  129.630 32.874  1.00 26.20 ? 58  THR G CA  1 
ATOM   7078  C  C   . THR G  1 58  ? 53.824  129.014 33.661  1.00 25.26 ? 58  THR G C   1 
ATOM   7079  O  O   . THR G  1 58  ? 54.525  129.710 34.394  1.00 26.16 ? 58  THR G O   1 
ATOM   7080  C  CB  . THR G  1 58  ? 51.480  129.879 33.851  1.00 28.64 ? 58  THR G CB  1 
ATOM   7081  O  OG1 . THR G  1 58  ? 51.492  128.890 34.891  1.00 35.14 ? 58  THR G OG1 1 
ATOM   7082  C  CG2 . THR G  1 58  ? 50.148  129.806 33.132  1.00 31.14 ? 58  THR G CG2 1 
ATOM   7083  N  N   . SER G  1 59  ? 54.008  127.703 33.519  1.00 22.92 ? 59  SER G N   1 
ATOM   7084  C  CA  . SER G  1 59  ? 55.081  127.017 34.237  1.00 21.43 ? 59  SER G CA  1 
ATOM   7085  C  C   . SER G  1 59  ? 56.380  126.880 33.418  1.00 18.96 ? 59  SER G C   1 
ATOM   7086  O  O   . SER G  1 59  ? 57.311  126.203 33.828  1.00 16.47 ? 59  SER G O   1 
ATOM   7087  C  CB  . SER G  1 59  ? 54.597  125.661 34.766  1.00 21.18 ? 59  SER G CB  1 
ATOM   7088  O  OG  . SER G  1 59  ? 53.830  124.974 33.792  1.00 21.95 ? 59  SER G OG  1 
ATOM   7089  N  N   . ALA G  1 60  ? 56.434  127.550 32.272  1.00 22.30 ? 60  ALA G N   1 
ATOM   7090  C  CA  . ALA G  1 60  ? 57.615  127.542 31.409  1.00 15.76 ? 60  ALA G CA  1 
ATOM   7091  C  C   . ALA G  1 60  ? 58.726  128.436 31.962  1.00 16.12 ? 60  ALA G C   1 
ATOM   7092  O  O   . ALA G  1 60  ? 59.866  128.418 31.475  1.00 16.71 ? 60  ALA G O   1 
ATOM   7093  C  CB  . ALA G  1 60  ? 57.227  128.003 30.018  1.00 14.50 ? 60  ALA G CB  1 
ATOM   7094  N  N   . GLY G  1 61  ? 58.385  129.226 32.971  1.00 13.32 ? 61  GLY G N   1 
ATOM   7095  C  CA  . GLY G  1 61  ? 59.297  130.192 33.536  1.00 15.79 ? 61  GLY G CA  1 
ATOM   7096  C  C   . GLY G  1 61  ? 59.638  131.354 32.611  1.00 19.41 ? 61  GLY G C   1 
ATOM   7097  O  O   . GLY G  1 61  ? 58.897  131.672 31.666  1.00 15.90 ? 61  GLY G O   1 
ATOM   7098  N  N   . PRO G  1 62  ? 60.774  132.016 32.891  1.00 19.98 ? 62  PRO G N   1 
ATOM   7099  C  CA  . PRO G  1 62  ? 61.158  133.231 32.161  1.00 19.05 ? 62  PRO G CA  1 
ATOM   7100  C  C   . PRO G  1 62  ? 61.967  132.900 30.917  1.00 17.38 ? 62  PRO G C   1 
ATOM   7101  O  O   . PRO G  1 62  ? 62.116  131.730 30.600  1.00 16.97 ? 62  PRO G O   1 
ATOM   7102  C  CB  . PRO G  1 62  ? 62.027  133.978 33.166  1.00 15.14 ? 62  PRO G CB  1 
ATOM   7103  C  CG  . PRO G  1 62  ? 62.707  132.852 33.950  1.00 18.76 ? 62  PRO G CG  1 
ATOM   7104  C  CD  . PRO G  1 62  ? 61.698  131.708 34.002  1.00 17.62 ? 62  PRO G CD  1 
ATOM   7105  N  N   . HIS G  1 63  ? 62.466  133.918 30.227  1.00 15.48 ? 63  HIS G N   1 
ATOM   7106  C  CA  . HIS G  1 63  ? 63.277  133.700 29.046  1.00 16.31 ? 63  HIS G CA  1 
ATOM   7107  C  C   . HIS G  1 63  ? 64.527  132.924 29.440  1.00 13.92 ? 63  HIS G C   1 
ATOM   7108  O  O   . HIS G  1 63  ? 65.164  133.233 30.448  1.00 14.69 ? 63  HIS G O   1 
ATOM   7109  C  CB  . HIS G  1 63  ? 63.657  135.034 28.407  1.00 15.05 ? 63  HIS G CB  1 
ATOM   7110  C  CG  . HIS G  1 63  ? 62.502  135.766 27.802  1.00 17.36 ? 63  HIS G CG  1 
ATOM   7111  N  ND1 . HIS G  1 63  ? 62.664  136.786 26.893  1.00 18.07 ? 63  HIS G ND1 1 
ATOM   7112  C  CD2 . HIS G  1 63  ? 61.166  135.615 27.961  1.00 19.13 ? 63  HIS G CD2 1 
ATOM   7113  C  CE1 . HIS G  1 63  ? 61.480  137.240 26.527  1.00 18.41 ? 63  HIS G CE1 1 
ATOM   7114  N  NE2 . HIS G  1 63  ? 60.555  136.550 27.166  1.00 18.36 ? 63  HIS G NE2 1 
ATOM   7115  N  N   . PHE G  1 64  ? 64.837  131.885 28.677  1.00 12.96 ? 64  PHE G N   1 
ATOM   7116  C  CA  . PHE G  1 64  ? 66.066  131.148 28.875  1.00 15.14 ? 64  PHE G CA  1 
ATOM   7117  C  C   . PHE G  1 64  ? 67.244  132.130 28.826  1.00 13.77 ? 64  PHE G C   1 
ATOM   7118  O  O   . PHE G  1 64  ? 67.477  132.785 27.817  1.00 13.42 ? 64  PHE G O   1 
ATOM   7119  C  CB  . PHE G  1 64  ? 66.218  130.046 27.818  1.00 14.32 ? 64  PHE G CB  1 
ATOM   7120  C  CG  . PHE G  1 64  ? 67.455  129.195 28.011  1.00 15.57 ? 64  PHE G CG  1 
ATOM   7121  C  CD1 . PHE G  1 64  ? 67.816  128.766 29.276  1.00 13.98 ? 64  PHE G CD1 1 
ATOM   7122  C  CD2 . PHE G  1 64  ? 68.253  128.837 26.932  1.00 14.45 ? 64  PHE G CD2 1 
ATOM   7123  C  CE1 . PHE G  1 64  ? 68.949  127.982 29.466  1.00 16.02 ? 64  PHE G CE1 1 
ATOM   7124  C  CE2 . PHE G  1 64  ? 69.390  128.058 27.113  1.00 17.07 ? 64  PHE G CE2 1 
ATOM   7125  C  CZ  . PHE G  1 64  ? 69.740  127.635 28.375  1.00 16.05 ? 64  PHE G CZ  1 
ATOM   7126  N  N   . ASN G  1 65  ? 67.952  132.252 29.944  1.00 17.70 ? 65  ASN G N   1 
ATOM   7127  C  CA  . ASN G  1 65  ? 68.949  133.304 30.113  1.00 16.34 ? 65  ASN G CA  1 
ATOM   7128  C  C   . ASN G  1 65  ? 70.145  132.812 30.936  1.00 15.74 ? 65  ASN G C   1 
ATOM   7129  O  O   . ASN G  1 65  ? 70.416  133.304 32.029  1.00 13.49 ? 65  ASN G O   1 
ATOM   7130  C  CB  . ASN G  1 65  ? 68.294  134.519 30.778  1.00 14.44 ? 65  ASN G CB  1 
ATOM   7131  C  CG  . ASN G  1 65  ? 69.238  135.711 30.866  1.00 18.43 ? 65  ASN G CG  1 
ATOM   7132  O  OD1 . ASN G  1 65  ? 70.207  135.799 30.116  1.00 15.95 ? 65  ASN G OD1 1 
ATOM   7133  N  ND2 . ASN G  1 65  ? 68.962  136.623 31.788  1.00 17.29 ? 65  ASN G ND2 1 
ATOM   7134  N  N   . PRO G  1 66  ? 70.855  131.804 30.428  1.00 15.93 ? 66  PRO G N   1 
ATOM   7135  C  CA  . PRO G  1 66  ? 71.875  131.203 31.293  1.00 18.12 ? 66  PRO G CA  1 
ATOM   7136  C  C   . PRO G  1 66  ? 73.072  132.128 31.540  1.00 21.84 ? 66  PRO G C   1 
ATOM   7137  O  O   . PRO G  1 66  ? 73.789  131.910 32.515  1.00 19.79 ? 66  PRO G O   1 
ATOM   7138  C  CB  . PRO G  1 66  ? 72.307  129.961 30.509  1.00 19.58 ? 66  PRO G CB  1 
ATOM   7139  C  CG  . PRO G  1 66  ? 72.085  130.344 29.070  1.00 19.96 ? 66  PRO G CG  1 
ATOM   7140  C  CD  . PRO G  1 66  ? 70.802  131.166 29.104  1.00 16.75 ? 66  PRO G CD  1 
ATOM   7141  N  N   . LEU G  1 67  ? 73.275  133.138 30.692  1.00 19.52 ? 67  LEU G N   1 
ATOM   7142  C  CA  . LEU G  1 67  ? 74.368  134.094 30.903  1.00 19.71 ? 67  LEU G CA  1 
ATOM   7143  C  C   . LEU G  1 67  ? 73.921  135.389 31.610  1.00 24.07 ? 67  LEU G C   1 
ATOM   7144  O  O   . LEU G  1 67  ? 74.638  136.378 31.591  1.00 22.42 ? 67  LEU G O   1 
ATOM   7145  C  CB  . LEU G  1 67  ? 75.062  134.424 29.577  1.00 19.52 ? 67  LEU G CB  1 
ATOM   7146  C  CG  . LEU G  1 67  ? 75.495  133.217 28.726  1.00 24.62 ? 67  LEU G CG  1 
ATOM   7147  C  CD1 . LEU G  1 67  ? 76.183  133.625 27.435  1.00 22.60 ? 67  LEU G CD1 1 
ATOM   7148  C  CD2 . LEU G  1 67  ? 76.385  132.276 29.512  1.00 23.57 ? 67  LEU G CD2 1 
ATOM   7149  N  N   . SER G  1 68  ? 72.729  135.384 32.209  1.00 22.65 ? 68  SER G N   1 
ATOM   7150  C  CA  . SER G  1 68  ? 72.235  136.527 32.993  1.00 20.85 ? 68  SER G CA  1 
ATOM   7151  C  C   . SER G  1 68  ? 72.327  137.892 32.312  1.00 21.18 ? 68  SER G C   1 
ATOM   7152  O  O   . SER G  1 68  ? 72.754  138.862 32.925  1.00 27.07 ? 68  SER G O   1 
ATOM   7153  C  CB  . SER G  1 68  ? 72.951  136.595 34.347  1.00 23.45 ? 68  SER G CB  1 
ATOM   7154  O  OG  . SER G  1 68  ? 72.670  135.450 35.128  1.00 25.29 ? 68  SER G OG  1 
ATOM   7155  N  N   . ARG G  1 69  ? 71.944  137.967 31.049  1.00 19.95 ? 69  ARG G N   1 
ATOM   7156  C  CA  . ARG G  1 69  ? 71.894  139.236 30.346  1.00 18.39 ? 69  ARG G CA  1 
ATOM   7157  C  C   . ARG G  1 69  ? 70.502  139.861 30.438  1.00 21.30 ? 69  ARG G C   1 
ATOM   7158  O  O   . ARG G  1 69  ? 69.572  139.278 31.007  1.00 16.77 ? 69  ARG G O   1 
ATOM   7159  C  CB  . ARG G  1 69  ? 72.264  139.035 28.882  1.00 21.25 ? 69  ARG G CB  1 
ATOM   7160  C  CG  . ARG G  1 69  ? 73.473  138.143 28.690  1.00 26.18 ? 69  ARG G CG  1 
ATOM   7161  C  CD  . ARG G  1 69  ? 74.737  138.824 29.155  1.00 27.84 ? 69  ARG G CD  1 
ATOM   7162  N  NE  . ARG G  1 69  ? 75.164  139.834 28.189  1.00 41.89 ? 69  ARG G NE  1 
ATOM   7163  C  CZ  . ARG G  1 69  ? 75.895  139.570 27.105  1.00 39.78 ? 69  ARG G CZ  1 
ATOM   7164  N  NH1 . ARG G  1 69  ? 76.284  138.322 26.843  1.00 39.02 ? 69  ARG G NH1 1 
ATOM   7165  N  NH2 . ARG G  1 69  ? 76.234  140.554 26.282  1.00 34.84 ? 69  ARG G NH2 1 
ATOM   7166  N  N   . LYS G  1 70  ? 70.365  141.052 29.869  1.00 20.68 ? 70  LYS G N   1 
ATOM   7167  C  CA  . LYS G  1 70  ? 69.073  141.710 29.793  1.00 21.45 ? 70  LYS G CA  1 
ATOM   7168  C  C   . LYS G  1 70  ? 68.406  141.306 28.487  1.00 21.49 ? 70  LYS G C   1 
ATOM   7169  O  O   . LYS G  1 70  ? 69.062  140.739 27.603  1.00 20.39 ? 70  LYS G O   1 
ATOM   7170  C  CB  . LYS G  1 70  ? 69.248  143.227 29.885  1.00 26.52 ? 70  LYS G CB  1 
ATOM   7171  C  CG  . LYS G  1 70  ? 69.291  143.737 31.334  1.00 31.12 ? 70  LYS G CG  1 
ATOM   7172  C  CD  . LYS G  1 70  ? 70.150  144.982 31.463  1.00 37.46 ? 70  LYS G CD  1 
ATOM   7173  C  CE  . LYS G  1 70  ? 69.737  146.050 30.463  1.00 43.18 ? 70  LYS G CE  1 
ATOM   7174  N  NZ  . LYS G  1 70  ? 70.682  147.211 30.486  1.00 54.75 ? 70  LYS G NZ  1 
ATOM   7175  N  N   . HIS G  1 71  ? 67.109  141.571 28.367  1.00 18.96 ? 71  HIS G N   1 
ATOM   7176  C  CA  . HIS G  1 71  ? 66.363  141.170 27.176  1.00 17.69 ? 71  HIS G CA  1 
ATOM   7177  C  C   . HIS G  1 71  ? 66.744  141.978 25.936  1.00 18.80 ? 71  HIS G C   1 
ATOM   7178  O  O   . HIS G  1 71  ? 66.963  143.177 26.020  1.00 19.16 ? 71  HIS G O   1 
ATOM   7179  C  CB  . HIS G  1 71  ? 64.854  141.271 27.415  1.00 15.78 ? 71  HIS G CB  1 
ATOM   7180  C  CG  . HIS G  1 71  ? 64.035  140.908 26.214  1.00 17.44 ? 71  HIS G CG  1 
ATOM   7181  N  ND1 . HIS G  1 71  ? 63.814  139.602 25.831  1.00 17.22 ? 71  HIS G ND1 1 
ATOM   7182  C  CD2 . HIS G  1 71  ? 63.416  141.680 25.288  1.00 17.55 ? 71  HIS G CD2 1 
ATOM   7183  C  CE1 . HIS G  1 71  ? 63.070  139.584 24.738  1.00 16.17 ? 71  HIS G CE1 1 
ATOM   7184  N  NE2 . HIS G  1 71  ? 62.813  140.831 24.390  1.00 18.14 ? 71  HIS G NE2 1 
ATOM   7185  N  N   . GLY G  1 72  ? 66.816  141.313 24.786  1.00 17.61 ? 72  GLY G N   1 
ATOM   7186  C  CA  . GLY G  1 72  ? 67.124  141.978 23.531  1.00 18.78 ? 72  GLY G CA  1 
ATOM   7187  C  C   . GLY G  1 72  ? 66.479  141.336 22.306  1.00 16.51 ? 72  GLY G C   1 
ATOM   7188  O  O   . GLY G  1 72  ? 65.677  140.415 22.416  1.00 19.36 ? 72  GLY G O   1 
ATOM   7189  N  N   . GLY G  1 73  ? 66.812  141.843 21.128  1.00 16.96 ? 73  GLY G N   1 
ATOM   7190  C  CA  . GLY G  1 73  ? 66.462  141.174 19.885  1.00 17.26 ? 73  GLY G CA  1 
ATOM   7191  C  C   . GLY G  1 73  ? 67.542  140.163 19.518  1.00 18.88 ? 73  GLY G C   1 
ATOM   7192  O  O   . GLY G  1 73  ? 68.635  140.161 20.101  1.00 19.32 ? 73  GLY G O   1 
ATOM   7193  N  N   . PRO G  1 74  ? 67.249  139.287 18.555  1.00 19.56 ? 74  PRO G N   1 
ATOM   7194  C  CA  . PRO G  1 74  ? 68.189  138.228 18.170  1.00 17.29 ? 74  PRO G CA  1 
ATOM   7195  C  C   . PRO G  1 74  ? 69.535  138.749 17.690  1.00 20.75 ? 74  PRO G C   1 
ATOM   7196  O  O   . PRO G  1 74  ? 70.511  138.032 17.844  1.00 17.61 ? 74  PRO G O   1 
ATOM   7197  C  CB  . PRO G  1 74  ? 67.465  137.486 17.037  1.00 18.37 ? 74  PRO G CB  1 
ATOM   7198  C  CG  . PRO G  1 74  ? 66.317  138.377 16.633  1.00 19.33 ? 74  PRO G CG  1 
ATOM   7199  C  CD  . PRO G  1 74  ? 65.960  139.173 17.854  1.00 17.03 ? 74  PRO G CD  1 
ATOM   7200  N  N   . LYS G  1 75  ? 69.600  139.963 17.148  1.00 22.14 ? 75  LYS G N   1 
ATOM   7201  C  CA  . LYS G  1 75  ? 70.874  140.482 16.659  1.00 19.58 ? 75  LYS G CA  1 
ATOM   7202  C  C   . LYS G  1 75  ? 71.669  141.299 17.691  1.00 24.00 ? 75  LYS G C   1 
ATOM   7203  O  O   . LYS G  1 75  ? 72.811  141.667 17.457  1.00 24.78 ? 75  LYS G O   1 
ATOM   7204  C  CB  . LYS G  1 75  ? 70.663  141.337 15.420  1.00 21.20 ? 75  LYS G CB  1 
ATOM   7205  C  CG  . LYS G  1 75  ? 69.565  140.891 14.497  1.00 28.26 ? 75  LYS G CG  1 
ATOM   7206  C  CD  . LYS G  1 75  ? 69.507  141.871 13.328  1.00 35.14 ? 75  LYS G CD  1 
ATOM   7207  C  CE  . LYS G  1 75  ? 68.303  141.661 12.441  1.00 35.52 ? 75  LYS G CE  1 
ATOM   7208  N  NZ  . LYS G  1 75  ? 68.360  142.615 11.294  1.00 47.52 ? 75  LYS G NZ  1 
ATOM   7209  N  N   . ASP G  1 76  ? 71.074  141.623 18.821  1.00 21.54 ? 76  ASP G N   1 
ATOM   7210  C  CA  . ASP G  1 76  ? 71.839  142.335 19.834  1.00 22.00 ? 76  ASP G CA  1 
ATOM   7211  C  C   . ASP G  1 76  ? 72.863  141.419 20.476  1.00 26.31 ? 76  ASP G C   1 
ATOM   7212  O  O   . ASP G  1 76  ? 72.643  140.217 20.593  1.00 26.67 ? 76  ASP G O   1 
ATOM   7213  C  CB  . ASP G  1 76  ? 70.917  142.894 20.910  1.00 22.30 ? 76  ASP G CB  1 
ATOM   7214  C  CG  . ASP G  1 76  ? 69.874  143.816 20.342  1.00 26.35 ? 76  ASP G CG  1 
ATOM   7215  O  OD1 . ASP G  1 76  ? 70.200  144.509 19.357  1.00 29.00 ? 76  ASP G OD1 1 
ATOM   7216  O  OD2 . ASP G  1 76  ? 68.732  143.853 20.866  1.00 27.66 ? 76  ASP G OD2 1 
ATOM   7217  N  N   . GLU G  1 77  ? 73.983  141.997 20.894  1.00 23.62 ? 77  GLU G N   1 
ATOM   7218  C  CA  . GLU G  1 77  ? 74.953  141.289 21.706  1.00 22.97 ? 77  GLU G CA  1 
ATOM   7219  C  C   . GLU G  1 77  ? 74.359  141.101 23.104  1.00 27.14 ? 77  GLU G C   1 
ATOM   7220  O  O   . GLU G  1 77  ? 74.589  140.076 23.750  1.00 24.89 ? 77  GLU G O   1 
ATOM   7221  C  CB  . GLU G  1 77  ? 76.251  142.101 21.784  1.00 30.12 ? 77  GLU G CB  1 
ATOM   7222  C  CG  . GLU G  1 77  ? 77.483  141.343 22.254  1.00 39.54 ? 77  GLU G CG  1 
ATOM   7223  C  CD  . GLU G  1 77  ? 78.764  142.166 22.072  1.00 52.95 ? 77  GLU G CD  1 
ATOM   7224  O  OE1 . GLU G  1 77  ? 79.143  142.905 23.013  1.00 53.52 ? 77  GLU G OE1 1 
ATOM   7225  O  OE2 . GLU G  1 77  ? 79.385  142.083 20.982  1.00 55.18 ? 77  GLU G OE2 1 
ATOM   7226  N  N   . GLU G  1 78  ? 73.601  142.096 23.568  1.00 23.20 ? 78  GLU G N   1 
ATOM   7227  C  CA  . GLU G  1 78  ? 72.911  141.988 24.855  1.00 22.27 ? 78  GLU G CA  1 
ATOM   7228  C  C   . GLU G  1 78  ? 71.545  141.361 24.640  1.00 23.10 ? 78  GLU G C   1 
ATOM   7229  O  O   . GLU G  1 78  ? 70.585  142.036 24.234  1.00 19.06 ? 78  GLU G O   1 
ATOM   7230  C  CB  . GLU G  1 78  ? 72.773  143.349 25.547  1.00 19.23 ? 78  GLU G CB  1 
ATOM   7231  C  CG  . GLU G  1 78  ? 72.203  143.278 26.970  1.00 24.22 ? 78  GLU G CG  1 
ATOM   7232  C  CD  . GLU G  1 78  ? 73.206  142.716 27.976  1.00 34.35 ? 78  GLU G CD  1 
ATOM   7233  O  OE1 . GLU G  1 78  ? 74.380  142.504 27.579  1.00 42.98 ? 78  GLU G OE1 1 
ATOM   7234  O  OE2 . GLU G  1 78  ? 72.835  142.483 29.155  1.00 25.76 ? 78  GLU G OE2 1 
ATOM   7235  N  N   . ARG G  1 79  ? 71.475  140.055 24.879  1.00 18.63 ? 79  ARG G N   1 
ATOM   7236  C  CA  . ARG G  1 79  ? 70.220  139.333 24.746  1.00 18.39 ? 79  ARG G CA  1 
ATOM   7237  C  C   . ARG G  1 79  ? 70.265  138.101 25.612  1.00 23.01 ? 79  ARG G C   1 
ATOM   7238  O  O   . ARG G  1 79  ? 71.339  137.602 25.956  1.00 18.55 ? 79  ARG G O   1 
ATOM   7239  C  CB  . ARG G  1 79  ? 69.962  138.925 23.299  1.00 17.45 ? 79  ARG G CB  1 
ATOM   7240  C  CG  . ARG G  1 79  ? 71.074  138.063 22.687  1.00 17.24 ? 79  ARG G CG  1 
ATOM   7241  C  CD  . ARG G  1 79  ? 70.642  137.492 21.369  1.00 16.49 ? 79  ARG G CD  1 
ATOM   7242  N  NE  . ARG G  1 79  ? 69.989  136.195 21.524  1.00 14.83 ? 79  ARG G NE  1 
ATOM   7243  C  CZ  . ARG G  1 79  ? 69.799  135.355 20.517  1.00 13.56 ? 79  ARG G CZ  1 
ATOM   7244  N  NH1 . ARG G  1 79  ? 70.197  135.696 19.302  1.00 13.58 ? 79  ARG G NH1 1 
ATOM   7245  N  NH2 . ARG G  1 79  ? 69.212  134.184 20.717  1.00 13.67 ? 79  ARG G NH2 1 
ATOM   7246  N  N   . HIS G  1 80  ? 69.082  137.642 25.992  1.00 17.26 ? 80  HIS G N   1 
ATOM   7247  C  CA  . HIS G  1 80  ? 68.910  136.314 26.526  1.00 14.74 ? 80  HIS G CA  1 
ATOM   7248  C  C   . HIS G  1 80  ? 69.197  135.307 25.416  1.00 13.68 ? 80  HIS G C   1 
ATOM   7249  O  O   . HIS G  1 80  ? 68.941  135.590 24.243  1.00 14.49 ? 80  HIS G O   1 
ATOM   7250  C  CB  . HIS G  1 80  ? 67.455  136.156 26.943  1.00 13.77 ? 80  HIS G CB  1 
ATOM   7251  C  CG  . HIS G  1 80  ? 67.040  137.098 28.017  1.00 16.27 ? 80  HIS G CG  1 
ATOM   7252  N  ND1 . HIS G  1 80  ? 65.759  137.590 28.122  1.00 14.70 ? 80  HIS G ND1 1 
ATOM   7253  C  CD2 . HIS G  1 80  ? 67.742  137.642 29.040  1.00 17.60 ? 80  HIS G CD2 1 
ATOM   7254  C  CE1 . HIS G  1 80  ? 65.684  138.390 29.169  1.00 16.25 ? 80  HIS G CE1 1 
ATOM   7255  N  NE2 . HIS G  1 80  ? 66.874  138.438 29.743  1.00 18.52 ? 80  HIS G NE2 1 
ATOM   7256  N  N   . VAL G  1 81  ? 69.699  134.132 25.776  1.00 14.16 ? 81  VAL G N   1 
ATOM   7257  C  CA  . VAL G  1 81  ? 69.849  133.058 24.792  1.00 16.08 ? 81  VAL G CA  1 
ATOM   7258  C  C   . VAL G  1 81  ? 68.485  132.795 24.137  1.00 14.33 ? 81  VAL G C   1 
ATOM   7259  O  O   . VAL G  1 81  ? 68.390  132.637 22.925  1.00 13.45 ? 81  VAL G O   1 
ATOM   7260  C  CB  . VAL G  1 81  ? 70.428  131.756 25.430  1.00 16.52 ? 81  VAL G CB  1 
ATOM   7261  C  CG1 . VAL G  1 81  ? 70.198  130.557 24.535  1.00 11.11 ? 81  VAL G CG1 1 
ATOM   7262  C  CG2 . VAL G  1 81  ? 71.938  131.917 25.750  1.00 16.46 ? 81  VAL G CG2 1 
ATOM   7263  N  N   . GLY G  1 82  ? 67.426  132.792 24.939  1.00 14.29 ? 82  GLY G N   1 
ATOM   7264  C  CA  . GLY G  1 82  ? 66.093  132.484 24.436  1.00 12.30 ? 82  GLY G CA  1 
ATOM   7265  C  C   . GLY G  1 82  ? 65.437  133.514 23.537  1.00 13.41 ? 82  GLY G C   1 
ATOM   7266  O  O   . GLY G  1 82  ? 64.291  133.327 23.100  1.00 14.48 ? 82  GLY G O   1 
ATOM   7267  N  N   . ASP G  1 83  ? 66.150  134.597 23.239  1.00 14.68 ? 83  ASP G N   1 
ATOM   7268  C  CA  . ASP G  1 83  ? 65.533  135.745 22.569  1.00 16.75 ? 83  ASP G CA  1 
ATOM   7269  C  C   . ASP G  1 83  ? 65.551  135.633 21.039  1.00 16.54 ? 83  ASP G C   1 
ATOM   7270  O  O   . ASP G  1 83  ? 66.473  136.130 20.397  1.00 14.48 ? 83  ASP G O   1 
ATOM   7271  C  CB  . ASP G  1 83  ? 66.232  137.047 22.981  1.00 14.19 ? 83  ASP G CB  1 
ATOM   7272  C  CG  . ASP G  1 83  ? 65.826  137.533 24.348  1.00 15.52 ? 83  ASP G CG  1 
ATOM   7273  O  OD1 . ASP G  1 83  ? 64.810  137.049 24.894  1.00 15.68 ? 83  ASP G OD1 1 
ATOM   7274  O  OD2 . ASP G  1 83  ? 66.516  138.436 24.871  1.00 15.33 ? 83  ASP G OD2 1 
ATOM   7275  N  N   . LEU G  1 84  ? 64.512  135.041 20.456  1.00 13.88 ? 84  LEU G N   1 
ATOM   7276  C  CA  . LEU G  1 84  ? 64.475  134.859 19.006  1.00 14.56 ? 84  LEU G CA  1 
ATOM   7277  C  C   . LEU G  1 84  ? 63.656  135.912 18.239  1.00 17.49 ? 84  LEU G C   1 
ATOM   7278  O  O   . LEU G  1 84  ? 63.268  135.682 17.107  1.00 17.39 ? 84  LEU G O   1 
ATOM   7279  C  CB  . LEU G  1 84  ? 63.986  133.447 18.653  1.00 15.29 ? 84  LEU G CB  1 
ATOM   7280  C  CG  . LEU G  1 84  ? 64.808  132.273 19.208  1.00 14.44 ? 84  LEU G CG  1 
ATOM   7281  C  CD1 . LEU G  1 84  ? 64.257  130.928 18.737  1.00 12.74 ? 84  LEU G CD1 1 
ATOM   7282  C  CD2 . LEU G  1 84  ? 66.199  132.406 18.742  1.00 13.57 ? 84  LEU G CD2 1 
ATOM   7283  N  N   . GLY G  1 85  ? 63.381  137.064 18.844  1.00 20.46 ? 85  GLY G N   1 
ATOM   7284  C  CA  . GLY G  1 85  ? 62.747  138.148 18.101  1.00 18.52 ? 85  GLY G CA  1 
ATOM   7285  C  C   . GLY G  1 85  ? 61.251  138.015 17.867  1.00 19.24 ? 85  GLY G C   1 
ATOM   7286  O  O   . GLY G  1 85  ? 60.500  137.670 18.775  1.00 18.42 ? 85  GLY G O   1 
ATOM   7287  N  N   . ASN G  1 86  ? 60.811  138.317 16.651  1.00 19.18 ? 86  ASN G N   1 
ATOM   7288  C  CA  . ASN G  1 86  ? 59.396  138.197 16.314  1.00 19.62 ? 86  ASN G CA  1 
ATOM   7289  C  C   . ASN G  1 86  ? 59.208  137.348 15.087  1.00 20.83 ? 86  ASN G C   1 
ATOM   7290  O  O   . ASN G  1 86  ? 60.109  137.255 14.241  1.00 20.73 ? 86  ASN G O   1 
ATOM   7291  C  CB  . ASN G  1 86  ? 58.748  139.566 16.056  1.00 19.83 ? 86  ASN G CB  1 
ATOM   7292  C  CG  . ASN G  1 86  ? 58.671  140.418 17.298  1.00 21.10 ? 86  ASN G CG  1 
ATOM   7293  O  OD1 . ASN G  1 86  ? 57.954  140.096 18.247  1.00 21.95 ? 86  ASN G OD1 1 
ATOM   7294  N  ND2 . ASN G  1 86  ? 59.395  141.531 17.293  1.00 22.54 ? 86  ASN G ND2 1 
ATOM   7295  N  N   . VAL G  1 87  ? 58.037  136.723 14.999  1.00 19.60 ? 87  VAL G N   1 
ATOM   7296  C  CA  . VAL G  1 87  ? 57.601  136.110 13.751  1.00 25.57 ? 87  VAL G CA  1 
ATOM   7297  C  C   . VAL G  1 87  ? 56.438  136.923 13.172  1.00 23.18 ? 87  VAL G C   1 
ATOM   7298  O  O   . VAL G  1 87  ? 55.689  137.568 13.912  1.00 20.74 ? 87  VAL G O   1 
ATOM   7299  C  CB  . VAL G  1 87  ? 57.172  134.635 13.946  1.00 24.62 ? 87  VAL G CB  1 
ATOM   7300  C  CG1 . VAL G  1 87  ? 58.338  133.805 14.428  1.00 20.18 ? 87  VAL G CG1 1 
ATOM   7301  C  CG2 . VAL G  1 87  ? 56.004  134.540 14.913  1.00 20.75 ? 87  VAL G CG2 1 
ATOM   7302  N  N   . THR G  1 88  ? 56.299  136.887 11.851  1.00 25.34 ? 88  THR G N   1 
ATOM   7303  C  CA  . THR G  1 88  ? 55.301  137.695 11.157  1.00 26.93 ? 88  THR G CA  1 
ATOM   7304  C  C   . THR G  1 88  ? 54.176  136.860 10.565  1.00 24.38 ? 88  THR G C   1 
ATOM   7305  O  O   . THR G  1 88  ? 54.413  136.040 9.682   1.00 26.29 ? 88  THR G O   1 
ATOM   7306  C  CB  . THR G  1 88  ? 55.939  138.487 10.010  1.00 29.73 ? 88  THR G CB  1 
ATOM   7307  O  OG1 . THR G  1 88  ? 56.982  139.309 10.532  1.00 29.23 ? 88  THR G OG1 1 
ATOM   7308  C  CG2 . THR G  1 88  ? 54.898  139.372 9.320   1.00 30.14 ? 88  THR G CG2 1 
ATOM   7309  N  N   . ALA G  1 89  ? 52.957  137.083 11.045  1.00 24.85 ? 89  ALA G N   1 
ATOM   7310  C  CA  . ALA G  1 89  ? 51.787  136.389 10.506  1.00 29.29 ? 89  ALA G CA  1 
ATOM   7311  C  C   . ALA G  1 89  ? 51.168  137.194 9.367   1.00 32.87 ? 89  ALA G C   1 
ATOM   7312  O  O   . ALA G  1 89  ? 50.992  138.407 9.478   1.00 32.71 ? 89  ALA G O   1 
ATOM   7313  C  CB  . ALA G  1 89  ? 50.750  136.152 11.596  1.00 25.32 ? 89  ALA G CB  1 
ATOM   7314  N  N   . ASP G  1 90  ? 50.830  136.513 8.282   1.00 33.78 ? 90  ASP G N   1 
ATOM   7315  C  CA  . ASP G  1 90  ? 50.265  137.181 7.122   1.00 31.02 ? 90  ASP G CA  1 
ATOM   7316  C  C   . ASP G  1 90  ? 48.777  137.426 7.327   1.00 32.46 ? 90  ASP G C   1 
ATOM   7317  O  O   . ASP G  1 90  ? 48.212  137.003 8.329   1.00 33.15 ? 90  ASP G O   1 
ATOM   7318  C  CB  . ASP G  1 90  ? 50.546  136.390 5.832   1.00 25.83 ? 90  ASP G CB  1 
ATOM   7319  C  CG  . ASP G  1 90  ? 49.830  135.037 5.779   1.00 26.30 ? 90  ASP G CG  1 
ATOM   7320  O  OD1 . ASP G  1 90  ? 48.849  134.802 6.514   1.00 32.51 ? 90  ASP G OD1 1 
ATOM   7321  O  OD2 . ASP G  1 90  ? 50.247  134.197 4.967   1.00 28.24 ? 90  ASP G OD2 1 
ATOM   7322  N  N   . LYS G  1 91  ? 48.162  138.106 6.363   1.00 38.74 ? 91  LYS G N   1 
ATOM   7323  C  CA  . LYS G  1 91  ? 46.733  138.435 6.360   1.00 34.43 ? 91  LYS G CA  1 
ATOM   7324  C  C   . LYS G  1 91  ? 45.854  137.289 6.860   1.00 32.20 ? 91  LYS G C   1 
ATOM   7325  O  O   . LYS G  1 91  ? 44.925  137.496 7.638   1.00 36.17 ? 91  LYS G O   1 
ATOM   7326  C  CB  . LYS G  1 91  ? 46.317  138.812 4.927   1.00 36.53 ? 91  LYS G CB  1 
ATOM   7327  C  CG  . LYS G  1 91  ? 44.830  139.085 4.736   1.00 46.48 ? 91  LYS G CG  1 
ATOM   7328  C  CD  . LYS G  1 91  ? 44.443  140.516 5.152   1.00 52.58 ? 91  LYS G CD  1 
ATOM   7329  C  CE  . LYS G  1 91  ? 43.075  140.921 4.582   1.00 52.22 ? 91  LYS G CE  1 
ATOM   7330  N  NZ  . LYS G  1 91  ? 42.857  142.399 4.626   1.00 48.89 ? 91  LYS G NZ  1 
ATOM   7331  N  N   . ASP G  1 92  ? 46.175  136.078 6.409   1.00 34.87 ? 92  ASP G N   1 
ATOM   7332  C  CA  . ASP G  1 92  ? 45.401  134.878 6.716   1.00 33.64 ? 92  ASP G CA  1 
ATOM   7333  C  C   . ASP G  1 92  ? 45.729  134.270 8.083   1.00 31.78 ? 92  ASP G C   1 
ATOM   7334  O  O   . ASP G  1 92  ? 45.084  133.322 8.513   1.00 33.14 ? 92  ASP G O   1 
ATOM   7335  C  CB  . ASP G  1 92  ? 45.611  133.837 5.609   1.00 34.89 ? 92  ASP G CB  1 
ATOM   7336  C  CG  . ASP G  1 92  ? 45.267  134.382 4.232   1.00 39.09 ? 92  ASP G CG  1 
ATOM   7337  O  OD1 . ASP G  1 92  ? 44.222  135.061 4.110   1.00 43.25 ? 92  ASP G OD1 1 
ATOM   7338  O  OD2 . ASP G  1 92  ? 46.042  134.156 3.278   1.00 37.09 ? 92  ASP G OD2 1 
ATOM   7339  N  N   . GLY G  1 93  ? 46.740  134.812 8.752   1.00 32.99 ? 93  GLY G N   1 
ATOM   7340  C  CA  . GLY G  1 93  ? 47.100  134.370 10.090  1.00 30.54 ? 93  GLY G CA  1 
ATOM   7341  C  C   . GLY G  1 93  ? 48.271  133.409 10.176  1.00 23.75 ? 93  GLY G C   1 
ATOM   7342  O  O   . GLY G  1 93  ? 48.573  132.870 11.233  1.00 26.55 ? 93  GLY G O   1 
ATOM   7343  N  N   . VAL G  1 94  ? 48.942  133.195 9.060   1.00 27.21 ? 94  VAL G N   1 
ATOM   7344  C  CA  . VAL G  1 94  ? 49.971  132.189 9.003   1.00 23.15 ? 94  VAL G CA  1 
ATOM   7345  C  C   . VAL G  1 94  ? 51.335  132.839 9.036   1.00 28.39 ? 94  VAL G C   1 
ATOM   7346  O  O   . VAL G  1 94  ? 51.684  133.623 8.149   1.00 28.15 ? 94  VAL G O   1 
ATOM   7347  C  CB  . VAL G  1 94  ? 49.848  131.315 7.731   1.00 28.20 ? 94  VAL G CB  1 
ATOM   7348  C  CG1 . VAL G  1 94  ? 50.887  130.212 7.750   1.00 27.14 ? 94  VAL G CG1 1 
ATOM   7349  C  CG2 . VAL G  1 94  ? 48.455  130.721 7.616   1.00 28.86 ? 94  VAL G CG2 1 
ATOM   7350  N  N   . ALA G  1 95  ? 52.100  132.524 10.079  1.00 24.74 ? 95  ALA G N   1 
ATOM   7351  C  CA  . ALA G  1 95  ? 53.493  132.930 10.141  1.00 23.74 ? 95  ALA G CA  1 
ATOM   7352  C  C   . ALA G  1 95  ? 54.368  131.828 9.571   1.00 23.13 ? 95  ALA G C   1 
ATOM   7353  O  O   . ALA G  1 95  ? 54.449  130.733 10.125  1.00 22.29 ? 95  ALA G O   1 
ATOM   7354  C  CB  . ALA G  1 95  ? 53.899  133.249 11.586  1.00 23.47 ? 95  ALA G CB  1 
ATOM   7355  N  N   . ASP G  1 96  ? 54.992  132.111 8.438   1.00 25.20 ? 96  ASP G N   1 
ATOM   7356  C  CA  . ASP G  1 96  ? 56.040  131.264 7.903   1.00 24.32 ? 96  ASP G CA  1 
ATOM   7357  C  C   . ASP G  1 96  ? 57.331  131.635 8.634   1.00 26.52 ? 96  ASP G C   1 
ATOM   7358  O  O   . ASP G  1 96  ? 57.795  132.764 8.546   1.00 30.72 ? 96  ASP G O   1 
ATOM   7359  C  CB  . ASP G  1 96  ? 56.174  131.522 6.397   1.00 31.73 ? 96  ASP G CB  1 
ATOM   7360  C  CG  . ASP G  1 96  ? 57.172  130.594 5.714   1.00 37.09 ? 96  ASP G CG  1 
ATOM   7361  O  OD1 . ASP G  1 96  ? 58.028  129.999 6.404   1.00 43.19 ? 96  ASP G OD1 1 
ATOM   7362  O  OD2 . ASP G  1 96  ? 57.115  130.471 4.469   1.00 46.69 ? 96  ASP G OD2 1 
ATOM   7363  N  N   . VAL G  1 97  ? 57.909  130.691 9.366   1.00 26.38 ? 97  VAL G N   1 
ATOM   7364  C  CA  . VAL G  1 97  ? 59.120  130.969 10.124  1.00 21.30 ? 97  VAL G CA  1 
ATOM   7365  C  C   . VAL G  1 97  ? 60.355  130.416 9.436   1.00 21.97 ? 97  VAL G C   1 
ATOM   7366  O  O   . VAL G  1 97  ? 60.411  129.234 9.120   1.00 22.77 ? 97  VAL G O   1 
ATOM   7367  C  CB  . VAL G  1 97  ? 59.058  130.357 11.534  1.00 24.25 ? 97  VAL G CB  1 
ATOM   7368  C  CG1 . VAL G  1 97  ? 60.366  130.624 12.283  1.00 19.56 ? 97  VAL G CG1 1 
ATOM   7369  C  CG2 . VAL G  1 97  ? 57.841  130.881 12.312  1.00 22.39 ? 97  VAL G CG2 1 
ATOM   7370  N  N   . SER G  1 98  ? 61.351  131.270 9.227   1.00 20.79 ? 98  SER G N   1 
ATOM   7371  C  CA  . SER G  1 98  ? 62.632  130.853 8.670   1.00 25.05 ? 98  SER G CA  1 
ATOM   7372  C  C   . SER G  1 98  ? 63.730  131.705 9.295   1.00 25.47 ? 98  SER G C   1 
ATOM   7373  O  O   . SER G  1 98  ? 63.930  132.846 8.908   1.00 26.63 ? 98  SER G O   1 
ATOM   7374  C  CB  . SER G  1 98  ? 62.644  131.004 7.141   1.00 26.92 ? 98  SER G CB  1 
ATOM   7375  O  OG  . SER G  1 98  ? 63.864  130.520 6.584   1.00 22.48 ? 98  SER G OG  1 
ATOM   7376  N  N   . ILE G  1 99  ? 64.433  131.142 10.269  1.00 21.53 ? 99  ILE G N   1 
ATOM   7377  C  CA  . ILE G  1 99  ? 65.400  131.876 11.064  1.00 20.67 ? 99  ILE G CA  1 
ATOM   7378  C  C   . ILE G  1 99  ? 66.725  131.118 11.091  1.00 21.55 ? 99  ILE G C   1 
ATOM   7379  O  O   . ILE G  1 99  ? 66.758  129.891 11.017  1.00 21.46 ? 99  ILE G O   1 
ATOM   7380  C  CB  . ILE G  1 99  ? 64.884  132.009 12.534  1.00 21.35 ? 99  ILE G CB  1 
ATOM   7381  C  CG1 . ILE G  1 99  ? 63.581  132.799 12.585  1.00 22.76 ? 99  ILE G CG1 1 
ATOM   7382  C  CG2 . ILE G  1 99  ? 65.894  132.659 13.442  1.00 19.63 ? 99  ILE G CG2 1 
ATOM   7383  C  CD1 . ILE G  1 99  ? 63.096  132.999 14.001  1.00 26.31 ? 99  ILE G CD1 1 
ATOM   7384  N  N   . GLU G  1 100 ? 67.825  131.840 11.210  1.00 20.47 ? 100 GLU G N   1 
ATOM   7385  C  CA  . GLU G  1 100 ? 69.080  131.201 11.548  1.00 16.82 ? 100 GLU G CA  1 
ATOM   7386  C  C   . GLU G  1 100 ? 69.646  131.955 12.735  1.00 16.30 ? 100 GLU G C   1 
ATOM   7387  O  O   . GLU G  1 100 ? 69.595  133.183 12.770  1.00 18.14 ? 100 GLU G O   1 
ATOM   7388  C  CB  . GLU G  1 100 ? 70.040  131.200 10.353  1.00 20.42 ? 100 GLU G CB  1 
ATOM   7389  C  CG  . GLU G  1 100 ? 71.447  130.860 10.767  1.00 24.02 ? 100 GLU G CG  1 
ATOM   7390  C  CD  . GLU G  1 100 ? 72.405  130.785 9.606   1.00 27.67 ? 100 GLU G CD  1 
ATOM   7391  O  OE1 . GLU G  1 100 ? 72.072  130.112 8.599   1.00 30.28 ? 100 GLU G OE1 1 
ATOM   7392  O  OE2 . GLU G  1 100 ? 73.490  131.407 9.715   1.00 27.83 ? 100 GLU G OE2 1 
ATOM   7393  N  N   . ASP G  1 101 ? 70.146  131.236 13.737  1.00 13.67 ? 101 ASP G N   1 
ATOM   7394  C  CA  . ASP G  1 101 ? 70.603  131.898 14.941  1.00 13.70 ? 101 ASP G CA  1 
ATOM   7395  C  C   . ASP G  1 101 ? 71.880  131.272 15.497  1.00 16.41 ? 101 ASP G C   1 
ATOM   7396  O  O   . ASP G  1 101 ? 72.021  130.052 15.542  1.00 14.23 ? 101 ASP G O   1 
ATOM   7397  C  CB  . ASP G  1 101 ? 69.494  131.889 15.994  1.00 14.40 ? 101 ASP G CB  1 
ATOM   7398  C  CG  . ASP G  1 101 ? 69.845  132.706 17.216  1.00 15.90 ? 101 ASP G CG  1 
ATOM   7399  O  OD1 . ASP G  1 101 ? 69.707  133.949 17.152  1.00 14.99 ? 101 ASP G OD1 1 
ATOM   7400  O  OD2 . ASP G  1 101 ? 70.270  132.110 18.239  1.00 14.80 ? 101 ASP G OD2 1 
ATOM   7401  N  N   . SER G  1 102 ? 72.792  132.120 15.956  1.00 15.45 ? 102 SER G N   1 
ATOM   7402  C  CA  . SER G  1 102 ? 74.123  131.661 16.361  1.00 19.27 ? 102 SER G CA  1 
ATOM   7403  C  C   . SER G  1 102 ? 74.358  131.611 17.856  1.00 16.92 ? 102 SER G C   1 
ATOM   7404  O  O   . SER G  1 102 ? 75.444  131.256 18.312  1.00 22.25 ? 102 SER G O   1 
ATOM   7405  C  CB  . SER G  1 102 ? 75.190  132.535 15.724  1.00 18.64 ? 102 SER G CB  1 
ATOM   7406  O  OG  . SER G  1 102 ? 75.666  131.886 14.566  1.00 29.01 ? 102 SER G OG  1 
ATOM   7407  N  N   . VAL G  1 103 ? 73.333  131.960 18.614  1.00 13.72 ? 103 VAL G N   1 
ATOM   7408  C  CA  . VAL G  1 103 ? 73.426  132.015 20.053  1.00 14.89 ? 103 VAL G CA  1 
ATOM   7409  C  C   . VAL G  1 103 ? 72.824  130.766 20.713  1.00 15.50 ? 103 VAL G C   1 
ATOM   7410  O  O   . VAL G  1 103 ? 73.452  130.176 21.596  1.00 17.26 ? 103 VAL G O   1 
ATOM   7411  C  CB  . VAL G  1 103 ? 72.743  133.274 20.561  1.00 17.62 ? 103 VAL G CB  1 
ATOM   7412  C  CG1 . VAL G  1 103 ? 72.621  133.240 22.084  1.00 16.17 ? 103 VAL G CG1 1 
ATOM   7413  C  CG2 . VAL G  1 103 ? 73.529  134.489 20.088  1.00 17.72 ? 103 VAL G CG2 1 
ATOM   7414  N  N   . ILE G  1 104 ? 71.623  130.364 20.287  1.00 13.68 ? 104 ILE G N   1 
ATOM   7415  C  CA  . ILE G  1 104 ? 71.056  129.081 20.718  1.00 13.63 ? 104 ILE G CA  1 
ATOM   7416  C  C   . ILE G  1 104 ? 71.860  127.913 20.129  1.00 14.31 ? 104 ILE G C   1 
ATOM   7417  O  O   . ILE G  1 104 ? 72.518  128.041 19.090  1.00 13.81 ? 104 ILE G O   1 
ATOM   7418  C  CB  . ILE G  1 104 ? 69.581  128.899 20.287  1.00 11.24 ? 104 ILE G CB  1 
ATOM   7419  C  CG1 . ILE G  1 104 ? 69.477  128.847 18.766  1.00 10.98 ? 104 ILE G CG1 1 
ATOM   7420  C  CG2 . ILE G  1 104 ? 68.699  130.006 20.854  1.00 12.06 ? 104 ILE G CG2 1 
ATOM   7421  C  CD1 . ILE G  1 104 ? 68.044  128.630 18.215  1.00 10.65 ? 104 ILE G CD1 1 
ATOM   7422  N  N   . SER G  1 105 ? 71.783  126.775 20.799  1.00 11.41 ? 105 SER G N   1 
ATOM   7423  C  CA  . SER G  1 105 ? 72.460  125.571 20.373  1.00 11.22 ? 105 SER G CA  1 
ATOM   7424  C  C   . SER G  1 105 ? 71.613  124.376 20.774  1.00 11.77 ? 105 SER G C   1 
ATOM   7425  O  O   . SER G  1 105 ? 70.882  124.422 21.760  1.00 14.24 ? 105 SER G O   1 
ATOM   7426  C  CB  . SER G  1 105 ? 73.836  125.461 21.058  1.00 12.00 ? 105 SER G CB  1 
ATOM   7427  O  OG  . SER G  1 105 ? 74.591  124.406 20.482  1.00 11.26 ? 105 SER G OG  1 
ATOM   7428  N  N   . LEU G  1 106 ? 71.738  123.298 20.018  1.00 14.89 ? 106 LEU G N   1 
ATOM   7429  C  CA  . LEU G  1 106 ? 71.057  122.052 20.315  1.00 13.89 ? 106 LEU G CA  1 
ATOM   7430  C  C   . LEU G  1 106 ? 71.951  121.109 21.124  1.00 13.86 ? 106 LEU G C   1 
ATOM   7431  O  O   . LEU G  1 106 ? 71.611  119.949 21.327  1.00 15.50 ? 106 LEU G O   1 
ATOM   7432  C  CB  . LEU G  1 106 ? 70.643  121.378 19.000  1.00 12.29 ? 106 LEU G CB  1 
ATOM   7433  C  CG  . LEU G  1 106 ? 69.730  122.227 18.101  1.00 14.00 ? 106 LEU G CG  1 
ATOM   7434  C  CD1 . LEU G  1 106 ? 69.226  121.456 16.876  1.00 9.01  ? 106 LEU G CD1 1 
ATOM   7435  C  CD2 . LEU G  1 106 ? 68.540  122.775 18.912  1.00 11.79 ? 106 LEU G CD2 1 
ATOM   7436  N  N   . SER G  1 107 ? 73.110  121.591 21.549  1.00 13.26 ? 107 SER G N   1 
ATOM   7437  C  CA  . SER G  1 107 ? 73.991  120.782 22.385  1.00 15.06 ? 107 SER G CA  1 
ATOM   7438  C  C   . SER G  1 107 ? 74.853  121.643 23.271  1.00 15.80 ? 107 SER G C   1 
ATOM   7439  O  O   . SER G  1 107 ? 74.841  122.871 23.194  1.00 16.49 ? 107 SER G O   1 
ATOM   7440  C  CB  . SER G  1 107 ? 74.876  119.861 21.552  1.00 18.49 ? 107 SER G CB  1 
ATOM   7441  O  OG  . SER G  1 107 ? 75.718  120.586 20.675  1.00 19.80 ? 107 SER G OG  1 
ATOM   7442  N  N   . GLY G  1 108 ? 75.606  120.990 24.130  1.00 19.93 ? 108 GLY G N   1 
ATOM   7443  C  CA  . GLY G  1 108 ? 76.436  121.704 25.063  1.00 20.78 ? 108 GLY G CA  1 
ATOM   7444  C  C   . GLY G  1 108 ? 75.633  122.129 26.275  1.00 28.55 ? 108 GLY G C   1 
ATOM   7445  O  O   . GLY G  1 108 ? 74.401  122.011 26.314  1.00 27.71 ? 108 GLY G O   1 
ATOM   7446  N  N   . ASP G  1 109 ? 76.352  122.648 27.262  1.00 32.05 ? 109 ASP G N   1 
ATOM   7447  C  CA  . ASP G  1 109 ? 75.809  122.961 28.573  1.00 34.80 ? 109 ASP G CA  1 
ATOM   7448  C  C   . ASP G  1 109 ? 74.647  123.945 28.532  1.00 32.43 ? 109 ASP G C   1 
ATOM   7449  O  O   . ASP G  1 109 ? 73.904  124.054 29.505  1.00 30.43 ? 109 ASP G O   1 
ATOM   7450  C  CB  . ASP G  1 109 ? 76.930  123.490 29.472  1.00 33.78 ? 109 ASP G CB  1 
ATOM   7451  C  CG  . ASP G  1 109 ? 78.133  122.558 29.495  1.00 48.04 ? 109 ASP G CG  1 
ATOM   7452  O  OD1 . ASP G  1 109 ? 78.896  122.521 28.490  1.00 51.53 ? 109 ASP G OD1 1 
ATOM   7453  O  OD2 . ASP G  1 109 ? 78.306  121.852 30.513  1.00 48.99 ? 109 ASP G OD2 1 
ATOM   7454  N  N   . HIS G  1 110 ? 74.481  124.641 27.411  1.00 26.93 ? 110 HIS G N   1 
ATOM   7455  C  CA  . HIS G  1 110 ? 73.444  125.666 27.308  1.00 26.35 ? 110 HIS G CA  1 
ATOM   7456  C  C   . HIS G  1 110 ? 72.500  125.423 26.134  1.00 26.27 ? 110 HIS G C   1 
ATOM   7457  O  O   . HIS G  1 110 ? 72.186  126.339 25.360  1.00 28.23 ? 110 HIS G O   1 
ATOM   7458  C  CB  . HIS G  1 110 ? 74.082  127.041 27.187  1.00 24.71 ? 110 HIS G CB  1 
ATOM   7459  C  CG  . HIS G  1 110 ? 74.808  127.474 28.428  1.00 36.80 ? 110 HIS G CG  1 
ATOM   7460  N  ND1 . HIS G  1 110 ? 74.519  126.961 29.677  1.00 35.73 ? 110 HIS G ND1 1 
ATOM   7461  C  CD2 . HIS G  1 110 ? 75.814  128.364 28.613  1.00 28.12 ? 110 HIS G CD2 1 
ATOM   7462  C  CE1 . HIS G  1 110 ? 75.311  127.521 30.576  1.00 31.41 ? 110 HIS G CE1 1 
ATOM   7463  N  NE2 . HIS G  1 110 ? 76.103  128.377 29.957  1.00 31.37 ? 110 HIS G NE2 1 
ATOM   7464  N  N   . CYS G  1 111 ? 72.053  124.184 25.992  1.00 21.94 ? 111 CYS G N   1 
ATOM   7465  C  CA  . CYS G  1 111 ? 71.213  123.854 24.857  1.00 19.26 ? 111 CYS G CA  1 
ATOM   7466  C  C   . CYS G  1 111 ? 69.741  124.078 25.179  1.00 16.33 ? 111 CYS G C   1 
ATOM   7467  O  O   . CYS G  1 111 ? 69.340  124.122 26.339  1.00 13.78 ? 111 CYS G O   1 
ATOM   7468  C  CB  . CYS G  1 111 ? 71.479  122.435 24.346  1.00 15.91 ? 111 CYS G CB  1 
ATOM   7469  S  SG  . CYS G  1 111 ? 70.678  121.102 25.202  1.00 21.67 ? 111 CYS G SG  1 
ATOM   7470  N  N   . ILE G  1 112 ? 68.939  124.223 24.140  1.00 11.53 ? 112 ILE G N   1 
ATOM   7471  C  CA  . ILE G  1 112 ? 67.534  124.557 24.329  1.00 12.80 ? 112 ILE G CA  1 
ATOM   7472  C  C   . ILE G  1 112 ? 66.643  123.306 24.314  1.00 12.19 ? 112 ILE G C   1 
ATOM   7473  O  O   . ILE G  1 112 ? 65.433  123.391 24.483  1.00 9.89  ? 112 ILE G O   1 
ATOM   7474  C  CB  . ILE G  1 112 ? 67.081  125.597 23.279  1.00 11.76 ? 112 ILE G CB  1 
ATOM   7475  C  CG1 . ILE G  1 112 ? 67.142  124.995 21.875  1.00 7.89  ? 112 ILE G CG1 1 
ATOM   7476  C  CG2 . ILE G  1 112 ? 67.967  126.870 23.386  1.00 11.87 ? 112 ILE G CG2 1 
ATOM   7477  C  CD1 . ILE G  1 112 ? 66.768  125.984 20.791  1.00 8.65  ? 112 ILE G CD1 1 
ATOM   7478  N  N   . ILE G  1 113 ? 67.254  122.140 24.129  1.00 11.47 ? 113 ILE G N   1 
ATOM   7479  C  CA  . ILE G  1 113 ? 66.502  120.894 24.127  1.00 12.15 ? 113 ILE G CA  1 
ATOM   7480  C  C   . ILE G  1 113 ? 65.833  120.657 25.482  1.00 12.15 ? 113 ILE G C   1 
ATOM   7481  O  O   . ILE G  1 113 ? 66.443  120.860 26.524  1.00 10.66 ? 113 ILE G O   1 
ATOM   7482  C  CB  . ILE G  1 113 ? 67.392  119.712 23.680  1.00 13.90 ? 113 ILE G CB  1 
ATOM   7483  C  CG1 . ILE G  1 113 ? 67.603  119.814 22.154  1.00 12.79 ? 113 ILE G CG1 1 
ATOM   7484  C  CG2 . ILE G  1 113 ? 66.769  118.362 24.089  1.00 11.23 ? 113 ILE G CG2 1 
ATOM   7485  C  CD1 . ILE G  1 113 ? 68.633  118.895 21.624  1.00 21.01 ? 113 ILE G CD1 1 
ATOM   7486  N  N   . GLY G  1 114 ? 64.555  120.282 25.472  1.00 10.01 ? 114 GLY G N   1 
ATOM   7487  C  CA  . GLY G  1 114 ? 63.857  120.087 26.729  1.00 8.82  ? 114 GLY G CA  1 
ATOM   7488  C  C   . GLY G  1 114 ? 63.417  121.379 27.402  1.00 9.32  ? 114 GLY G C   1 
ATOM   7489  O  O   . GLY G  1 114 ? 62.978  121.381 28.556  1.00 8.96  ? 114 GLY G O   1 
ATOM   7490  N  N   . ARG G  1 115 ? 63.543  122.487 26.687  1.00 7.60  ? 115 ARG G N   1 
ATOM   7491  C  CA  . ARG G  1 115 ? 63.036  123.754 27.186  1.00 10.98 ? 115 ARG G CA  1 
ATOM   7492  C  C   . ARG G  1 115 ? 61.770  124.081 26.367  1.00 8.97  ? 115 ARG G C   1 
ATOM   7493  O  O   . ARG G  1 115 ? 61.372  123.268 25.536  1.00 9.83  ? 115 ARG G O   1 
ATOM   7494  C  CB  . ARG G  1 115 ? 64.126  124.835 27.139  1.00 7.97  ? 115 ARG G CB  1 
ATOM   7495  C  CG  . ARG G  1 115 ? 65.402  124.378 27.880  1.00 10.91 ? 115 ARG G CG  1 
ATOM   7496  C  CD  . ARG G  1 115 ? 66.412  125.508 28.163  1.00 12.74 ? 115 ARG G CD  1 
ATOM   7497  N  NE  . ARG G  1 115 ? 67.614  125.009 28.840  1.00 11.71 ? 115 ARG G NE  1 
ATOM   7498  C  CZ  . ARG G  1 115 ? 67.776  124.955 30.162  1.00 14.83 ? 115 ARG G CZ  1 
ATOM   7499  N  NH1 . ARG G  1 115 ? 66.810  125.374 30.958  1.00 12.79 ? 115 ARG G NH1 1 
ATOM   7500  N  NH2 . ARG G  1 115 ? 68.910  124.491 30.703  1.00 12.22 ? 115 ARG G NH2 1 
ATOM   7501  N  N   . THR G  1 116 ? 61.129  125.215 26.621  1.00 8.17  ? 116 THR G N   1 
ATOM   7502  C  CA  . THR G  1 116 ? 59.824  125.512 26.003  1.00 11.42 ? 116 THR G CA  1 
ATOM   7503  C  C   . THR G  1 116 ? 59.857  126.646 24.973  1.00 10.41 ? 116 THR G C   1 
ATOM   7504  O  O   . THR G  1 116 ? 60.294  127.743 25.267  1.00 12.76 ? 116 THR G O   1 
ATOM   7505  C  CB  . THR G  1 116 ? 58.767  125.899 27.068  1.00 10.96 ? 116 THR G CB  1 
ATOM   7506  O  OG1 . THR G  1 116 ? 58.501  124.772 27.899  1.00 8.68  ? 116 THR G OG1 1 
ATOM   7507  C  CG2 . THR G  1 116 ? 57.447  126.351 26.401  1.00 12.07 ? 116 THR G CG2 1 
ATOM   7508  N  N   . LEU G  1 117 ? 59.378  126.384 23.770  1.00 8.94  ? 117 LEU G N   1 
ATOM   7509  C  CA  . LEU G  1 117 ? 59.277  127.437 22.763  1.00 9.27  ? 117 LEU G CA  1 
ATOM   7510  C  C   . LEU G  1 117 ? 57.918  128.092 22.886  1.00 13.29 ? 117 LEU G C   1 
ATOM   7511  O  O   . LEU G  1 117 ? 56.916  127.400 23.042  1.00 13.04 ? 117 LEU G O   1 
ATOM   7512  C  CB  . LEU G  1 117 ? 59.428  126.847 21.376  1.00 8.40  ? 117 LEU G CB  1 
ATOM   7513  C  CG  . LEU G  1 117 ? 59.429  127.836 20.214  1.00 14.16 ? 117 LEU G CG  1 
ATOM   7514  C  CD1 . LEU G  1 117 ? 60.564  128.831 20.399  1.00 12.12 ? 117 LEU G CD1 1 
ATOM   7515  C  CD2 . LEU G  1 117 ? 59.584  127.058 18.924  1.00 8.53  ? 117 LEU G CD2 1 
ATOM   7516  N  N   . VAL G  1 118 ? 57.873  129.421 22.828  1.00 12.82 ? 118 VAL G N   1 
ATOM   7517  C  CA  . VAL G  1 118 ? 56.615  130.142 23.035  1.00 13.04 ? 118 VAL G CA  1 
ATOM   7518  C  C   . VAL G  1 118 ? 56.372  131.188 21.961  1.00 14.51 ? 118 VAL G C   1 
ATOM   7519  O  O   . VAL G  1 118 ? 57.295  131.908 21.592  1.00 15.54 ? 118 VAL G O   1 
ATOM   7520  C  CB  . VAL G  1 118 ? 56.599  130.848 24.381  1.00 12.20 ? 118 VAL G CB  1 
ATOM   7521  C  CG1 . VAL G  1 118 ? 55.303  131.627 24.540  1.00 16.12 ? 118 VAL G CG1 1 
ATOM   7522  C  CG2 . VAL G  1 118 ? 56.756  129.844 25.509  1.00 14.64 ? 118 VAL G CG2 1 
ATOM   7523  N  N   . VAL G  1 119 ? 55.147  131.251 21.432  1.00 15.86 ? 119 VAL G N   1 
ATOM   7524  C  CA  . VAL G  1 119 ? 54.754  132.354 20.543  1.00 15.92 ? 119 VAL G CA  1 
ATOM   7525  C  C   . VAL G  1 119 ? 53.770  133.269 21.271  1.00 18.59 ? 119 VAL G C   1 
ATOM   7526  O  O   . VAL G  1 119 ? 52.841  132.794 21.943  1.00 20.77 ? 119 VAL G O   1 
ATOM   7527  C  CB  . VAL G  1 119 ? 54.201  131.872 19.179  1.00 16.45 ? 119 VAL G CB  1 
ATOM   7528  C  CG1 . VAL G  1 119 ? 52.857  131.149 19.332  1.00 11.00 ? 119 VAL G CG1 1 
ATOM   7529  C  CG2 . VAL G  1 119 ? 54.074  133.072 18.215  1.00 16.98 ? 119 VAL G CG2 1 
ATOM   7530  N  N   . HIS G  1 120 ? 53.994  134.580 21.181  1.00 17.63 ? 120 HIS G N   1 
ATOM   7531  C  CA  . HIS G  1 120 ? 53.261  135.534 22.036  1.00 21.12 ? 120 HIS G CA  1 
ATOM   7532  C  C   . HIS G  1 120 ? 52.106  136.290 21.388  1.00 18.90 ? 120 HIS G C   1 
ATOM   7533  O  O   . HIS G  1 120 ? 51.955  136.277 20.181  1.00 18.67 ? 120 HIS G O   1 
ATOM   7534  C  CB  . HIS G  1 120 ? 54.215  136.549 22.645  1.00 18.50 ? 120 HIS G CB  1 
ATOM   7535  C  CG  . HIS G  1 120 ? 54.974  136.018 23.807  1.00 21.30 ? 120 HIS G CG  1 
ATOM   7536  N  ND1 . HIS G  1 120 ? 54.528  136.150 25.105  1.00 20.00 ? 120 HIS G ND1 1 
ATOM   7537  C  CD2 . HIS G  1 120 ? 56.130  135.317 23.869  1.00 15.31 ? 120 HIS G CD2 1 
ATOM   7538  C  CE1 . HIS G  1 120 ? 55.386  135.568 25.919  1.00 18.15 ? 120 HIS G CE1 1 
ATOM   7539  N  NE2 . HIS G  1 120 ? 56.361  135.048 25.194  1.00 18.37 ? 120 HIS G NE2 1 
ATOM   7540  N  N   . GLU G  1 121 ? 51.324  136.976 22.224  1.00 23.42 ? 121 GLU G N   1 
ATOM   7541  C  CA  . GLU G  1 121 ? 50.154  137.749 21.786  1.00 21.21 ? 121 GLU G CA  1 
ATOM   7542  C  C   . GLU G  1 121 ? 50.513  138.937 20.906  1.00 25.87 ? 121 GLU G C   1 
ATOM   7543  O  O   . GLU G  1 121 ? 49.921  139.134 19.853  1.00 26.97 ? 121 GLU G O   1 
ATOM   7544  C  CB  . GLU G  1 121 ? 49.367  138.243 22.994  1.00 24.81 ? 121 GLU G CB  1 
ATOM   7545  C  CG  . GLU G  1 121 ? 48.348  139.330 22.672  1.00 29.15 ? 121 GLU G CG  1 
ATOM   7546  C  CD  . GLU G  1 121 ? 47.732  139.928 23.922  1.00 29.42 ? 121 GLU G CD  1 
ATOM   7547  O  OE1 . GLU G  1 121 ? 46.606  140.469 23.842  1.00 40.41 ? 121 GLU G OE1 1 
ATOM   7548  O  OE2 . GLU G  1 121 ? 48.373  139.863 24.991  1.00 26.79 ? 121 GLU G OE2 1 
ATOM   7549  N  N   . LYS G  1 122 ? 51.478  139.740 21.340  1.00 25.35 ? 122 LYS G N   1 
ATOM   7550  C  CA  . LYS G  1 122 ? 51.897  140.878 20.527  1.00 28.27 ? 122 LYS G CA  1 
ATOM   7551  C  C   . LYS G  1 122 ? 53.389  140.893 20.231  1.00 24.25 ? 122 LYS G C   1 
ATOM   7552  O  O   . LYS G  1 122 ? 54.088  139.922 20.486  1.00 23.51 ? 122 LYS G O   1 
ATOM   7553  C  CB  . LYS G  1 122 ? 51.456  142.211 21.147  1.00 29.91 ? 122 LYS G CB  1 
ATOM   7554  C  CG  . LYS G  1 122 ? 51.168  142.188 22.642  1.00 31.69 ? 122 LYS G CG  1 
ATOM   7555  C  CD  . LYS G  1 122 ? 51.111  143.621 23.211  1.00 29.72 ? 122 LYS G CD  1 
ATOM   7556  C  CE  . LYS G  1 122 ? 51.026  143.623 24.736  1.00 36.31 ? 122 LYS G CE  1 
ATOM   7557  N  NZ  . LYS G  1 122 ? 51.781  144.760 25.383  1.00 38.59 ? 122 LYS G NZ  1 
ATOM   7558  N  N   . ALA G  1 123 ? 53.862  141.996 19.672  1.00 23.19 ? 123 ALA G N   1 
ATOM   7559  C  CA  . ALA G  1 123 ? 55.274  142.150 19.344  1.00 23.27 ? 123 ALA G CA  1 
ATOM   7560  C  C   . ALA G  1 123 ? 56.195  142.170 20.568  1.00 20.37 ? 123 ALA G C   1 
ATOM   7561  O  O   . ALA G  1 123 ? 55.854  142.695 21.629  1.00 22.67 ? 123 ALA G O   1 
ATOM   7562  C  CB  . ALA G  1 123 ? 55.487  143.412 18.528  1.00 22.70 ? 123 ALA G CB  1 
ATOM   7563  N  N   . ASP G  1 124 ? 57.374  141.591 20.395  1.00 19.82 ? 124 ASP G N   1 
ATOM   7564  C  CA  . ASP G  1 124 ? 58.465  141.744 21.337  1.00 18.16 ? 124 ASP G CA  1 
ATOM   7565  C  C   . ASP G  1 124 ? 59.115  143.073 20.961  1.00 18.31 ? 124 ASP G C   1 
ATOM   7566  O  O   . ASP G  1 124 ? 59.492  143.270 19.813  1.00 17.20 ? 124 ASP G O   1 
ATOM   7567  C  CB  . ASP G  1 124 ? 59.440  140.580 21.144  1.00 18.08 ? 124 ASP G CB  1 
ATOM   7568  C  CG  . ASP G  1 124 ? 60.655  140.632 22.084  1.00 19.54 ? 124 ASP G CG  1 
ATOM   7569  O  OD1 . ASP G  1 124 ? 61.068  141.714 22.544  1.00 15.37 ? 124 ASP G OD1 1 
ATOM   7570  O  OD2 . ASP G  1 124 ? 61.219  139.552 22.343  1.00 20.05 ? 124 ASP G OD2 1 
ATOM   7571  N  N   . ASP G  1 125 ? 59.242  143.986 21.919  1.00 21.35 ? 125 ASP G N   1 
ATOM   7572  C  CA  . ASP G  1 125 ? 59.827  145.295 21.625  1.00 21.17 ? 125 ASP G CA  1 
ATOM   7573  C  C   . ASP G  1 125 ? 61.361  145.277 21.615  1.00 21.05 ? 125 ASP G C   1 
ATOM   7574  O  O   . ASP G  1 125 ? 61.999  146.320 21.728  1.00 23.31 ? 125 ASP G O   1 
ATOM   7575  C  CB  . ASP G  1 125 ? 59.268  146.388 22.568  1.00 20.00 ? 125 ASP G CB  1 
ATOM   7576  C  CG  . ASP G  1 125 ? 59.679  146.206 24.030  1.00 23.92 ? 125 ASP G CG  1 
ATOM   7577  O  OD1 . ASP G  1 125 ? 60.728  145.589 24.333  1.00 22.49 ? 125 ASP G OD1 1 
ATOM   7578  O  OD2 . ASP G  1 125 ? 58.937  146.715 24.897  1.00 29.38 ? 125 ASP G OD2 1 
ATOM   7579  N  N   . LEU G  1 126 ? 61.931  144.079 21.502  1.00 20.50 ? 126 LEU G N   1 
ATOM   7580  C  CA  . LEU G  1 126 ? 63.388  143.863 21.459  1.00 20.19 ? 126 LEU G CA  1 
ATOM   7581  C  C   . LEU G  1 126 ? 64.180  144.608 22.533  1.00 19.77 ? 126 LEU G C   1 
ATOM   7582  O  O   . LEU G  1 126 ? 65.329  144.956 22.325  1.00 19.59 ? 126 LEU G O   1 
ATOM   7583  C  CB  . LEU G  1 126 ? 63.944  144.197 20.076  1.00 19.77 ? 126 LEU G CB  1 
ATOM   7584  C  CG  . LEU G  1 126 ? 63.060  143.727 18.921  1.00 22.93 ? 126 LEU G CG  1 
ATOM   7585  C  CD1 . LEU G  1 126 ? 63.607  144.208 17.576  1.00 19.73 ? 126 LEU G CD1 1 
ATOM   7586  C  CD2 . LEU G  1 126 ? 62.868  142.203 18.935  1.00 18.26 ? 126 LEU G CD2 1 
ATOM   7587  N  N   . GLY G  1 127 ? 63.561  144.852 23.683  1.00 20.53 ? 127 GLY G N   1 
ATOM   7588  C  CA  . GLY G  1 127 ? 64.262  145.476 24.787  1.00 22.63 ? 127 GLY G CA  1 
ATOM   7589  C  C   . GLY G  1 127 ? 64.391  146.991 24.700  1.00 26.76 ? 127 GLY G C   1 
ATOM   7590  O  O   . GLY G  1 127 ? 65.126  147.598 25.478  1.00 27.84 ? 127 GLY G O   1 
ATOM   7591  N  N   . LYS G  1 128 ? 63.662  147.608 23.779  1.00 23.67 ? 128 LYS G N   1 
ATOM   7592  C  CA  . LYS G  1 128 ? 63.797  149.045 23.558  1.00 29.83 ? 128 LYS G CA  1 
ATOM   7593  C  C   . LYS G  1 128 ? 62.520  149.837 23.856  1.00 29.68 ? 128 LYS G C   1 
ATOM   7594  O  O   . LYS G  1 128 ? 62.314  150.926 23.324  1.00 26.11 ? 128 LYS G O   1 
ATOM   7595  C  CB  . LYS G  1 128 ? 64.291  149.304 22.131  1.00 32.93 ? 128 LYS G CB  1 
ATOM   7596  C  CG  . LYS G  1 128 ? 65.730  148.829 21.918  1.00 27.67 ? 128 LYS G CG  1 
ATOM   7597  C  CD  . LYS G  1 128 ? 66.184  149.028 20.486  1.00 35.23 ? 128 LYS G CD  1 
ATOM   7598  C  CE  . LYS G  1 128 ? 65.102  148.556 19.514  1.00 40.96 ? 128 LYS G CE  1 
ATOM   7599  N  NZ  . LYS G  1 128 ? 65.607  148.323 18.121  1.00 48.24 ? 128 LYS G NZ  1 
ATOM   7600  N  N   . GLY G  1 129 ? 61.680  149.286 24.731  1.00 27.39 ? 129 GLY G N   1 
ATOM   7601  C  CA  . GLY G  1 129 ? 60.380  149.859 25.023  1.00 24.73 ? 129 GLY G CA  1 
ATOM   7602  C  C   . GLY G  1 129 ? 60.429  150.934 26.091  1.00 26.88 ? 129 GLY G C   1 
ATOM   7603  O  O   . GLY G  1 129 ? 59.430  151.588 26.359  1.00 31.18 ? 129 GLY G O   1 
ATOM   7604  N  N   . GLY G  1 130 ? 61.593  151.114 26.706  1.00 24.61 ? 130 GLY G N   1 
ATOM   7605  C  CA  . GLY G  1 130 ? 61.762  152.149 27.708  1.00 27.98 ? 130 GLY G CA  1 
ATOM   7606  C  C   . GLY G  1 130 ? 60.994  151.945 29.005  1.00 30.90 ? 130 GLY G C   1 
ATOM   7607  O  O   . GLY G  1 130 ? 60.541  152.906 29.611  1.00 37.62 ? 130 GLY G O   1 
ATOM   7608  N  N   . ASN G  1 131 ? 60.826  150.700 29.429  1.00 26.58 ? 131 ASN G N   1 
ATOM   7609  C  CA  . ASN G  1 131 ? 60.288  150.423 30.754  1.00 26.35 ? 131 ASN G CA  1 
ATOM   7610  C  C   . ASN G  1 131 ? 60.986  149.210 31.325  1.00 24.85 ? 131 ASN G C   1 
ATOM   7611  O  O   . ASN G  1 131 ? 61.747  148.548 30.614  1.00 23.75 ? 131 ASN G O   1 
ATOM   7612  C  CB  . ASN G  1 131 ? 58.771  150.212 30.727  1.00 26.88 ? 131 ASN G CB  1 
ATOM   7613  C  CG  . ASN G  1 131 ? 58.341  149.195 29.691  1.00 28.44 ? 131 ASN G CG  1 
ATOM   7614  O  OD1 . ASN G  1 131 ? 58.772  148.045 29.717  1.00 27.79 ? 131 ASN G OD1 1 
ATOM   7615  N  ND2 . ASN G  1 131 ? 57.472  149.612 28.779  1.00 29.80 ? 131 ASN G ND2 1 
ATOM   7616  N  N   . GLU G  1 132 ? 60.721  148.909 32.594  1.00 20.96 ? 132 GLU G N   1 
ATOM   7617  C  CA  . GLU G  1 132 ? 61.454  147.858 33.294  1.00 22.22 ? 132 GLU G CA  1 
ATOM   7618  C  C   . GLU G  1 132 ? 61.171  146.462 32.724  1.00 26.03 ? 132 GLU G C   1 
ATOM   7619  O  O   . GLU G  1 132 ? 62.079  145.639 32.660  1.00 22.96 ? 132 GLU G O   1 
ATOM   7620  C  CB  . GLU G  1 132 ? 61.228  147.925 34.821  1.00 25.77 ? 132 GLU G CB  1 
ATOM   7621  C  CG  . GLU G  1 132 ? 61.877  146.793 35.659  1.00 24.28 ? 132 GLU G CG  1 
ATOM   7622  C  CD  . GLU G  1 132 ? 63.424  146.794 35.667  1.00 34.76 ? 132 GLU G CD  1 
ATOM   7623  O  OE1 . GLU G  1 132 ? 64.062  147.535 34.881  1.00 36.96 ? 132 GLU G OE1 1 
ATOM   7624  O  OE2 . GLU G  1 132 ? 64.008  146.041 36.485  1.00 39.13 ? 132 GLU G OE2 1 
ATOM   7625  N  N   . GLU G  1 133 ? 59.941  146.220 32.267  1.00 17.68 ? 133 GLU G N   1 
ATOM   7626  C  CA  . GLU G  1 133 ? 59.576  144.930 31.685  1.00 21.05 ? 133 GLU G CA  1 
ATOM   7627  C  C   . GLU G  1 133 ? 60.168  144.719 30.292  1.00 22.77 ? 133 GLU G C   1 
ATOM   7628  O  O   . GLU G  1 133 ? 60.362  143.583 29.860  1.00 20.62 ? 133 GLU G O   1 
ATOM   7629  C  CB  . GLU G  1 133 ? 58.051  144.751 31.621  1.00 21.83 ? 133 GLU G CB  1 
ATOM   7630  C  CG  . GLU G  1 133 ? 57.429  144.300 32.913  1.00 23.44 ? 133 GLU G CG  1 
ATOM   7631  C  CD  . GLU G  1 133 ? 57.837  142.903 33.306  1.00 26.48 ? 133 GLU G CD  1 
ATOM   7632  O  OE1 . GLU G  1 133 ? 57.805  142.009 32.436  1.00 28.88 ? 133 GLU G OE1 1 
ATOM   7633  O  OE2 . GLU G  1 133 ? 58.188  142.695 34.489  1.00 23.52 ? 133 GLU G OE2 1 
ATOM   7634  N  N   . SER G  1 134 ? 60.453  145.809 29.584  1.00 23.54 ? 134 SER G N   1 
ATOM   7635  C  CA  . SER G  1 134 ? 61.061  145.690 28.264  1.00 19.92 ? 134 SER G CA  1 
ATOM   7636  C  C   . SER G  1 134 ? 62.441  145.052 28.390  1.00 21.54 ? 134 SER G C   1 
ATOM   7637  O  O   . SER G  1 134 ? 62.899  144.368 27.476  1.00 20.41 ? 134 SER G O   1 
ATOM   7638  C  CB  . SER G  1 134 ? 61.163  147.050 27.577  1.00 20.33 ? 134 SER G CB  1 
ATOM   7639  O  OG  . SER G  1 134 ? 61.807  146.937 26.320  1.00 24.45 ? 134 SER G OG  1 
ATOM   7640  N  N   . THR G  1 135 ? 63.079  145.261 29.538  1.00 21.42 ? 135 THR G N   1 
ATOM   7641  C  CA  . THR G  1 135 ? 64.396  144.689 29.815  1.00 24.24 ? 135 THR G CA  1 
ATOM   7642  C  C   . THR G  1 135 ? 64.306  143.247 30.315  1.00 24.47 ? 135 THR G C   1 
ATOM   7643  O  O   . THR G  1 135 ? 65.323  142.592 30.558  1.00 22.68 ? 135 THR G O   1 
ATOM   7644  C  CB  . THR G  1 135 ? 65.246  145.581 30.803  1.00 24.80 ? 135 THR G CB  1 
ATOM   7645  O  OG1 . THR G  1 135 ? 65.042  145.186 32.168  1.00 28.93 ? 135 THR G OG1 1 
ATOM   7646  C  CG2 . THR G  1 135 ? 64.904  147.071 30.636  1.00 27.59 ? 135 THR G CG2 1 
ATOM   7647  N  N   . LYS G  1 136 ? 63.086  142.746 30.454  1.00 18.19 ? 136 LYS G N   1 
ATOM   7648  C  CA  . LYS G  1 136 ? 62.925  141.401 30.973  1.00 20.87 ? 136 LYS G CA  1 
ATOM   7649  C  C   . LYS G  1 136 ? 62.258  140.477 29.972  1.00 18.55 ? 136 LYS G C   1 
ATOM   7650  O  O   . LYS G  1 136 ? 62.755  139.382 29.716  1.00 18.28 ? 136 LYS G O   1 
ATOM   7651  C  CB  . LYS G  1 136 ? 62.166  141.421 32.302  1.00 21.59 ? 136 LYS G CB  1 
ATOM   7652  C  CG  . LYS G  1 136 ? 62.874  142.231 33.356  1.00 21.15 ? 136 LYS G CG  1 
ATOM   7653  C  CD  . LYS G  1 136 ? 62.263  142.061 34.726  1.00 31.16 ? 136 LYS G CD  1 
ATOM   7654  C  CE  . LYS G  1 136 ? 63.086  142.808 35.767  1.00 27.45 ? 136 LYS G CE  1 
ATOM   7655  N  NZ  . LYS G  1 136 ? 64.474  142.261 35.921  1.00 25.54 ? 136 LYS G NZ  1 
ATOM   7656  N  N   . THR G  1 137 ? 61.149  140.932 29.403  1.00 17.88 ? 137 THR G N   1 
ATOM   7657  C  CA  . THR G  1 137 ? 60.330  140.106 28.520  1.00 18.90 ? 137 THR G CA  1 
ATOM   7658  C  C   . THR G  1 137 ? 60.105  140.714 27.140  1.00 19.17 ? 137 THR G C   1 
ATOM   7659  O  O   . THR G  1 137 ? 59.706  140.021 26.212  1.00 19.09 ? 137 THR G O   1 
ATOM   7660  C  CB  . THR G  1 137 ? 58.943  139.904 29.116  1.00 20.96 ? 137 THR G CB  1 
ATOM   7661  O  OG1 . THR G  1 137 ? 58.221  141.139 29.041  1.00 20.87 ? 137 THR G OG1 1 
ATOM   7662  C  CG2 . THR G  1 137 ? 59.039  139.470 30.552  1.00 19.79 ? 137 THR G CG2 1 
ATOM   7663  N  N   . GLY G  1 138 ? 60.318  142.014 27.001  1.00 19.27 ? 138 GLY G N   1 
ATOM   7664  C  CA  . GLY G  1 138 ? 60.037  142.661 25.731  1.00 19.10 ? 138 GLY G CA  1 
ATOM   7665  C  C   . GLY G  1 138 ? 58.557  143.009 25.528  1.00 19.81 ? 138 GLY G C   1 
ATOM   7666  O  O   . GLY G  1 138 ? 58.158  143.365 24.416  1.00 19.57 ? 138 GLY G O   1 
ATOM   7667  N  N   . ASN G  1 139 ? 57.754  142.870 26.585  1.00 17.98 ? 139 ASN G N   1 
ATOM   7668  C  CA  . ASN G  1 139 ? 56.329  143.257 26.572  1.00 25.38 ? 139 ASN G CA  1 
ATOM   7669  C  C   . ASN G  1 139 ? 55.477  142.671 25.449  1.00 21.87 ? 139 ASN G C   1 
ATOM   7670  O  O   . ASN G  1 139 ? 54.709  143.396 24.832  1.00 23.93 ? 139 ASN G O   1 
ATOM   7671  C  CB  . ASN G  1 139 ? 56.185  144.789 26.539  1.00 22.09 ? 139 ASN G CB  1 
ATOM   7672  C  CG  . ASN G  1 139 ? 56.739  145.448 27.784  1.00 25.27 ? 139 ASN G CG  1 
ATOM   7673  O  OD1 . ASN G  1 139 ? 56.402  145.058 28.900  1.00 30.21 ? 139 ASN G OD1 1 
ATOM   7674  N  ND2 . ASN G  1 139 ? 57.611  146.433 27.603  1.00 21.63 ? 139 ASN G ND2 1 
ATOM   7675  N  N   . ALA G  1 140 ? 55.603  141.373 25.188  1.00 22.30 ? 140 ALA G N   1 
ATOM   7676  C  CA  . ALA G  1 140 ? 54.920  140.762 24.041  1.00 25.18 ? 140 ALA G CA  1 
ATOM   7677  C  C   . ALA G  1 140 ? 53.600  140.092 24.425  1.00 21.65 ? 140 ALA G C   1 
ATOM   7678  O  O   . ALA G  1 140 ? 53.004  139.377 23.631  1.00 24.14 ? 140 ALA G O   1 
ATOM   7679  C  CB  . ALA G  1 140 ? 55.826  139.762 23.336  1.00 20.26 ? 140 ALA G CB  1 
ATOM   7680  N  N   . GLY G  1 141 ? 53.150  140.326 25.642  1.00 21.06 ? 141 GLY G N   1 
ATOM   7681  C  CA  . GLY G  1 141 ? 51.836  139.870 26.040  1.00 27.46 ? 141 GLY G CA  1 
ATOM   7682  C  C   . GLY G  1 141 ? 51.758  138.398 26.396  1.00 30.32 ? 141 GLY G C   1 
ATOM   7683  O  O   . GLY G  1 141 ? 52.750  137.778 26.792  1.00 27.41 ? 141 GLY G O   1 
ATOM   7684  N  N   . SER G  1 142 ? 50.567  137.834 26.234  1.00 23.68 ? 142 SER G N   1 
ATOM   7685  C  CA  . SER G  1 142 ? 50.292  136.493 26.706  1.00 24.32 ? 142 SER G CA  1 
ATOM   7686  C  C   . SER G  1 142 ? 51.047  135.439 25.929  1.00 22.14 ? 142 SER G C   1 
ATOM   7687  O  O   . SER G  1 142 ? 51.496  135.670 24.809  1.00 22.30 ? 142 SER G O   1 
ATOM   7688  C  CB  . SER G  1 142 ? 48.796  136.216 26.618  1.00 24.93 ? 142 SER G CB  1 
ATOM   7689  O  OG  . SER G  1 142 ? 48.115  136.977 27.600  1.00 30.20 ? 142 SER G OG  1 
ATOM   7690  N  N   . ARG G  1 143 ? 51.164  134.271 26.540  1.00 25.16 ? 143 ARG G N   1 
ATOM   7691  C  CA  . ARG G  1 143 ? 51.729  133.108 25.883  1.00 24.76 ? 143 ARG G CA  1 
ATOM   7692  C  C   . ARG G  1 143 ? 50.584  132.421 25.145  1.00 21.89 ? 143 ARG G C   1 
ATOM   7693  O  O   . ARG G  1 143 ? 49.703  131.833 25.767  1.00 28.75 ? 143 ARG G O   1 
ATOM   7694  C  CB  . ARG G  1 143 ? 52.377  132.190 26.932  1.00 20.82 ? 143 ARG G CB  1 
ATOM   7695  C  CG  . ARG G  1 143 ? 53.234  132.986 27.929  1.00 22.68 ? 143 ARG G CG  1 
ATOM   7696  C  CD  . ARG G  1 143 ? 54.069  132.157 28.901  1.00 22.06 ? 143 ARG G CD  1 
ATOM   7697  N  NE  . ARG G  1 143 ? 54.878  133.050 29.736  1.00 22.26 ? 143 ARG G NE  1 
ATOM   7698  C  CZ  . ARG G  1 143 ? 55.740  132.667 30.677  1.00 19.44 ? 143 ARG G CZ  1 
ATOM   7699  N  NH1 . ARG G  1 143 ? 55.945  131.383 30.924  1.00 20.30 ? 143 ARG G NH1 1 
ATOM   7700  N  NH2 . ARG G  1 143 ? 56.406  133.585 31.381  1.00 17.50 ? 143 ARG G NH2 1 
ATOM   7701  N  N   . LEU G  1 144 ? 50.584  132.518 23.823  1.00 18.97 ? 144 LEU G N   1 
ATOM   7702  C  CA  . LEU G  1 144 ? 49.454  132.026 23.027  1.00 24.62 ? 144 LEU G CA  1 
ATOM   7703  C  C   . LEU G  1 144 ? 49.530  130.527 22.770  1.00 22.66 ? 144 LEU G C   1 
ATOM   7704  O  O   . LEU G  1 144 ? 48.510  129.850 22.689  1.00 17.56 ? 144 LEU G O   1 
ATOM   7705  C  CB  . LEU G  1 144 ? 49.361  132.746 21.676  1.00 21.70 ? 144 LEU G CB  1 
ATOM   7706  C  CG  . LEU G  1 144 ? 48.904  134.204 21.608  1.00 25.14 ? 144 LEU G CG  1 
ATOM   7707  C  CD1 . LEU G  1 144 ? 48.778  134.610 20.146  1.00 27.85 ? 144 LEU G CD1 1 
ATOM   7708  C  CD2 . LEU G  1 144 ? 47.597  134.434 22.349  1.00 23.35 ? 144 LEU G CD2 1 
ATOM   7709  N  N   . ALA G  1 145 ? 50.749  130.025 22.618  1.00 16.34 ? 145 ALA G N   1 
ATOM   7710  C  CA  . ALA G  1 145 ? 50.962  128.620 22.368  1.00 16.30 ? 145 ALA G CA  1 
ATOM   7711  C  C   . ALA G  1 145 ? 52.403  128.273 22.750  1.00 16.32 ? 145 ALA G C   1 
ATOM   7712  O  O   . ALA G  1 145 ? 53.298  129.098 22.640  1.00 18.07 ? 145 ALA G O   1 
ATOM   7713  C  CB  . ALA G  1 145 ? 50.692  128.304 20.897  1.00 11.56 ? 145 ALA G CB  1 
ATOM   7714  N  N   . CYS G  1 146 ? 52.619  127.056 23.208  1.00 12.76 ? 146 CYS G N   1 
ATOM   7715  C  CA  . CYS G  1 146 ? 53.950  126.638 23.572  1.00 15.91 ? 146 CYS G CA  1 
ATOM   7716  C  C   . CYS G  1 146 ? 54.049  125.152 23.361  1.00 16.25 ? 146 CYS G C   1 
ATOM   7717  O  O   . CYS G  1 146 ? 53.051  124.488 23.086  1.00 13.45 ? 146 CYS G O   1 
ATOM   7718  C  CB  . CYS G  1 146 ? 54.243  126.966 25.025  1.00 14.51 ? 146 CYS G CB  1 
ATOM   7719  S  SG  . CYS G  1 146 ? 53.168  126.122 26.185  1.00 24.37 ? 146 CYS G SG  1 
ATOM   7720  N  N   . GLY G  1 147 ? 55.267  124.644 23.473  1.00 13.86 ? 147 GLY G N   1 
ATOM   7721  C  CA  . GLY G  1 147 ? 55.539  123.219 23.416  1.00 13.21 ? 147 GLY G CA  1 
ATOM   7722  C  C   . GLY G  1 147 ? 56.958  123.002 23.913  1.00 13.57 ? 147 GLY G C   1 
ATOM   7723  O  O   . GLY G  1 147 ? 57.714  123.960 24.017  1.00 13.17 ? 147 GLY G O   1 
ATOM   7724  N  N   . VAL G  1 148 ? 57.301  121.759 24.235  1.00 10.68 ? 148 VAL G N   1 
ATOM   7725  C  CA  . VAL G  1 148 ? 58.630  121.419 24.695  1.00 12.17 ? 148 VAL G CA  1 
ATOM   7726  C  C   . VAL G  1 148 ? 59.467  121.039 23.477  1.00 11.65 ? 148 VAL G C   1 
ATOM   7727  O  O   . VAL G  1 148 ? 58.985  120.343 22.579  1.00 10.71 ? 148 VAL G O   1 
ATOM   7728  C  CB  . VAL G  1 148 ? 58.613  120.222 25.677  1.00 12.03 ? 148 VAL G CB  1 
ATOM   7729  C  CG1 . VAL G  1 148 ? 60.040  119.875 26.123  1.00 9.73  ? 148 VAL G CG1 1 
ATOM   7730  C  CG2 . VAL G  1 148 ? 57.729  120.513 26.878  1.00 12.48 ? 148 VAL G CG2 1 
ATOM   7731  N  N   . ILE G  1 149 ? 60.710  121.507 23.447  1.00 9.47  ? 149 ILE G N   1 
ATOM   7732  C  CA  . ILE G  1 149 ? 61.612  121.244 22.335  1.00 7.49  ? 149 ILE G CA  1 
ATOM   7733  C  C   . ILE G  1 149 ? 62.226  119.876 22.494  1.00 7.27  ? 149 ILE G C   1 
ATOM   7734  O  O   . ILE G  1 149 ? 62.952  119.623 23.443  1.00 7.48  ? 149 ILE G O   1 
ATOM   7735  C  CB  . ILE G  1 149 ? 62.695  122.341 22.231  1.00 11.53 ? 149 ILE G CB  1 
ATOM   7736  C  CG1 . ILE G  1 149 ? 62.014  123.705 22.062  1.00 11.17 ? 149 ILE G CG1 1 
ATOM   7737  C  CG2 . ILE G  1 149 ? 63.623  122.077 21.053  1.00 9.30  ? 149 ILE G CG2 1 
ATOM   7738  C  CD1 . ILE G  1 149 ? 62.892  124.897 22.355  1.00 11.99 ? 149 ILE G CD1 1 
ATOM   7739  N  N   . GLY G  1 150 ? 61.905  118.979 21.570  1.00 8.09  ? 150 GLY G N   1 
ATOM   7740  C  CA  . GLY G  1 150 ? 62.325  117.598 21.677  1.00 9.14  ? 150 GLY G CA  1 
ATOM   7741  C  C   . GLY G  1 150 ? 63.324  117.217 20.601  1.00 11.90 ? 150 GLY G C   1 
ATOM   7742  O  O   . GLY G  1 150 ? 63.378  117.851 19.550  1.00 14.49 ? 150 GLY G O   1 
ATOM   7743  N  N   . ILE G  1 151 ? 64.122  116.187 20.868  1.00 9.13  ? 151 ILE G N   1 
ATOM   7744  C  CA  . ILE G  1 151 ? 65.078  115.668 19.898  1.00 11.65 ? 151 ILE G CA  1 
ATOM   7745  C  C   . ILE G  1 151 ? 64.337  115.000 18.735  1.00 13.02 ? 151 ILE G C   1 
ATOM   7746  O  O   . ILE G  1 151 ? 63.397  114.230 18.956  1.00 10.53 ? 151 ILE G O   1 
ATOM   7747  C  CB  . ILE G  1 151 ? 66.005  114.630 20.559  1.00 12.53 ? 151 ILE G CB  1 
ATOM   7748  C  CG1 . ILE G  1 151 ? 66.786  115.288 21.696  1.00 15.29 ? 151 ILE G CG1 1 
ATOM   7749  C  CG2 . ILE G  1 151 ? 66.952  114.017 19.515  1.00 13.11 ? 151 ILE G CG2 1 
ATOM   7750  C  CD1 . ILE G  1 151 ? 67.562  114.322 22.550  1.00 14.40 ? 151 ILE G CD1 1 
ATOM   7751  N  N   . ALA G  1 152 ? 64.746  115.302 17.506  1.00 11.39 ? 152 ALA G N   1 
ATOM   7752  C  CA  . ALA G  1 152 ? 64.112  114.714 16.327  1.00 13.00 ? 152 ALA G CA  1 
ATOM   7753  C  C   . ALA G  1 152 ? 65.049  113.826 15.522  1.00 14.65 ? 152 ALA G C   1 
ATOM   7754  O  O   . ALA G  1 152 ? 66.261  113.863 15.695  1.00 13.95 ? 152 ALA G O   1 
ATOM   7755  C  CB  . ALA G  1 152 ? 63.546  115.784 15.445  1.00 13.14 ? 152 ALA G CB  1 
ATOM   7756  N  N   . GLN G  1 153 ? 64.467  113.030 14.634  1.00 18.53 ? 153 GLN G N   1 
ATOM   7757  C  CA  . GLN G  1 153 ? 65.247  112.124 13.812  1.00 24.01 ? 153 GLN G CA  1 
ATOM   7758  C  C   . GLN G  1 153 ? 65.883  112.856 12.651  1.00 26.21 ? 153 GLN G C   1 
ATOM   7759  O  O   . GLN G  1 153 ? 65.218  113.660 11.989  1.00 24.84 ? 153 GLN G O   1 
ATOM   7760  C  CB  . GLN G  1 153 ? 64.366  111.021 13.243  1.00 24.10 ? 153 GLN G CB  1 
ATOM   7761  C  CG  . GLN G  1 153 ? 65.163  110.021 12.426  1.00 22.49 ? 153 GLN G CG  1 
ATOM   7762  C  CD  . GLN G  1 153 ? 64.361  108.780 12.114  1.00 27.32 ? 153 GLN G CD  1 
ATOM   7763  O  OE1 . GLN G  1 153 ? 64.809  107.662 12.366  1.00 30.89 ? 153 GLN G OE1 1 
ATOM   7764  N  NE2 . GLN G  1 153 ? 63.161  108.968 11.580  1.00 25.31 ? 153 GLN G NE2 1 
ATOM   7765  O  OXT . GLN G  1 153 ? 67.054  112.626 12.348  1.00 30.27 ? 153 GLN G OXT 1 
ATOM   7766  N  N   . ALA H  1 1   ? 71.497  118.977 41.624  1.00 42.90 ? 1   ALA H N   1 
ATOM   7767  C  CA  . ALA H  1 1   ? 70.319  118.136 41.410  1.00 40.15 ? 1   ALA H CA  1 
ATOM   7768  C  C   . ALA H  1 1   ? 69.478  118.536 40.174  1.00 33.74 ? 1   ALA H C   1 
ATOM   7769  O  O   . ALA H  1 1   ? 68.808  119.574 40.150  1.00 31.90 ? 1   ALA H O   1 
ATOM   7770  C  CB  . ALA H  1 1   ? 69.453  118.093 42.681  1.00 33.35 ? 1   ALA H CB  1 
ATOM   7771  N  N   . THR H  1 2   ? 69.506  117.698 39.150  1.00 25.54 ? 2   THR H N   1 
ATOM   7772  C  CA  . THR H  1 2   ? 68.704  117.957 37.970  1.00 24.47 ? 2   THR H CA  1 
ATOM   7773  C  C   . THR H  1 2   ? 67.273  117.399 38.151  1.00 23.99 ? 2   THR H C   1 
ATOM   7774  O  O   . THR H  1 2   ? 67.045  116.377 38.811  1.00 19.51 ? 2   THR H O   1 
ATOM   7775  C  CB  . THR H  1 2   ? 69.378  117.386 36.702  1.00 28.45 ? 2   THR H CB  1 
ATOM   7776  O  OG1 . THR H  1 2   ? 70.794  117.386 36.877  1.00 41.22 ? 2   THR H OG1 1 
ATOM   7777  C  CG2 . THR H  1 2   ? 69.047  118.219 35.480  1.00 31.11 ? 2   THR H CG2 1 
ATOM   7778  N  N   . LYS H  1 3   ? 66.313  118.097 37.564  1.00 23.33 ? 3   LYS H N   1 
ATOM   7779  C  CA  . LYS H  1 3   ? 64.908  117.745 37.667  1.00 16.30 ? 3   LYS H CA  1 
ATOM   7780  C  C   . LYS H  1 3   ? 64.292  117.792 36.282  1.00 15.87 ? 3   LYS H C   1 
ATOM   7781  O  O   . LYS H  1 3   ? 64.605  118.668 35.478  1.00 16.51 ? 3   LYS H O   1 
ATOM   7782  C  CB  . LYS H  1 3   ? 64.180  118.740 38.573  1.00 17.99 ? 3   LYS H CB  1 
ATOM   7783  C  CG  . LYS H  1 3   ? 64.512  118.629 40.052  1.00 20.42 ? 3   LYS H CG  1 
ATOM   7784  C  CD  . LYS H  1 3   ? 63.500  119.411 40.860  1.00 26.51 ? 3   LYS H CD  1 
ATOM   7785  C  CE  . LYS H  1 3   ? 63.762  119.366 42.360  1.00 37.20 ? 3   LYS H CE  1 
ATOM   7786  N  NZ  . LYS H  1 3   ? 62.563  119.885 43.118  1.00 35.93 ? 3   LYS H NZ  1 
ATOM   7787  N  N   . ALA H  1 4   ? 63.416  116.845 35.996  1.00 14.71 ? 4   ALA H N   1 
ATOM   7788  C  CA  . ALA H  1 4   ? 62.677  116.866 34.757  1.00 11.73 ? 4   ALA H CA  1 
ATOM   7789  C  C   . ALA H  1 4   ? 61.189  116.597 35.048  1.00 13.27 ? 4   ALA H C   1 
ATOM   7790  O  O   . ALA H  1 4   ? 60.810  116.283 36.178  1.00 13.64 ? 4   ALA H O   1 
ATOM   7791  C  CB  . ALA H  1 4   ? 63.247  115.858 33.793  1.00 8.47  ? 4   ALA H CB  1 
ATOM   7792  N  N   . VAL H  1 5   ? 60.349  116.769 34.035  1.00 12.02 ? 5   VAL H N   1 
ATOM   7793  C  CA  . VAL H  1 5   ? 58.906  116.658 34.195  1.00 9.80  ? 5   VAL H CA  1 
ATOM   7794  C  C   . VAL H  1 5   ? 58.310  116.314 32.828  1.00 11.60 ? 5   VAL H C   1 
ATOM   7795  O  O   . VAL H  1 5   ? 58.845  116.700 31.780  1.00 12.04 ? 5   VAL H O   1 
ATOM   7796  C  CB  . VAL H  1 5   ? 58.295  117.983 34.726  1.00 12.32 ? 5   VAL H CB  1 
ATOM   7797  C  CG1 . VAL H  1 5   ? 58.339  119.054 33.665  1.00 10.24 ? 5   VAL H CG1 1 
ATOM   7798  C  CG2 . VAL H  1 5   ? 56.856  117.778 35.214  1.00 9.27  ? 5   VAL H CG2 1 
ATOM   7799  N  N   . CYS H  1 6   ? 57.215  115.571 32.831  1.00 9.78  ? 6   CYS H N   1 
ATOM   7800  C  CA  . CYS H  1 6   ? 56.572  115.202 31.583  1.00 10.36 ? 6   CYS H CA  1 
ATOM   7801  C  C   . CYS H  1 6   ? 55.056  115.217 31.789  1.00 9.18  ? 6   CYS H C   1 
ATOM   7802  O  O   . CYS H  1 6   ? 54.558  114.611 32.729  1.00 8.18  ? 6   CYS H O   1 
ATOM   7803  C  CB  . CYS H  1 6   ? 57.004  113.811 31.171  1.00 7.01  ? 6   CYS H CB  1 
ATOM   7804  S  SG  . CYS H  1 6   ? 56.316  113.299 29.601  1.00 11.19 ? 6   CYS H SG  1 
ATOM   7805  N  N   . VAL H  1 7   ? 54.345  115.932 30.932  1.00 6.04  ? 7   VAL H N   1 
ATOM   7806  C  CA  . VAL H  1 7   ? 52.898  115.911 30.979  1.00 10.87 ? 7   VAL H CA  1 
ATOM   7807  C  C   . VAL H  1 7   ? 52.428  114.865 29.987  1.00 8.74  ? 7   VAL H C   1 
ATOM   7808  O  O   . VAL H  1 7   ? 52.673  114.995 28.802  1.00 8.65  ? 7   VAL H O   1 
ATOM   7809  C  CB  . VAL H  1 7   ? 52.299  117.266 30.582  1.00 13.42 ? 7   VAL H CB  1 
ATOM   7810  C  CG1 . VAL H  1 7   ? 50.764  117.199 30.651  1.00 9.61  ? 7   VAL H CG1 1 
ATOM   7811  C  CG2 . VAL H  1 7   ? 52.840  118.366 31.483  1.00 10.73 ? 7   VAL H CG2 1 
ATOM   7812  N  N   . LEU H  1 8   ? 51.762  113.824 30.459  1.00 7.88  ? 8   LEU H N   1 
ATOM   7813  C  CA  . LEU H  1 8   ? 51.307  112.796 29.538  1.00 9.58  ? 8   LEU H CA  1 
ATOM   7814  C  C   . LEU H  1 8   ? 49.883  113.100 29.073  1.00 9.45  ? 8   LEU H C   1 
ATOM   7815  O  O   . LEU H  1 8   ? 48.990  113.216 29.884  1.00 10.66 ? 8   LEU H O   1 
ATOM   7816  C  CB  . LEU H  1 8   ? 51.387  111.417 30.191  1.00 10.43 ? 8   LEU H CB  1 
ATOM   7817  C  CG  . LEU H  1 8   ? 52.747  110.832 30.601  1.00 9.39  ? 8   LEU H CG  1 
ATOM   7818  C  CD1 . LEU H  1 8   ? 52.493  109.724 31.600  1.00 11.76 ? 8   LEU H CD1 1 
ATOM   7819  C  CD2 . LEU H  1 8   ? 53.446  110.265 29.411  1.00 7.22  ? 8   LEU H CD2 1 
ATOM   7820  N  N   . LYS H  1 9   ? 49.697  113.252 27.764  1.00 9.66  ? 9   LYS H N   1 
ATOM   7821  C  CA  . LYS H  1 9   ? 48.371  113.419 27.152  1.00 15.01 ? 9   LYS H CA  1 
ATOM   7822  C  C   . LYS H  1 9   ? 48.216  112.460 25.982  1.00 12.92 ? 9   LYS H C   1 
ATOM   7823  O  O   . LYS H  1 9   ? 49.205  112.060 25.352  1.00 11.90 ? 9   LYS H O   1 
ATOM   7824  C  CB  . LYS H  1 9   ? 48.143  114.865 26.665  1.00 15.28 ? 9   LYS H CB  1 
ATOM   7825  C  CG  . LYS H  1 9   ? 48.162  115.930 27.781  1.00 17.77 ? 9   LYS H CG  1 
ATOM   7826  C  CD  . LYS H  1 9   ? 47.245  115.553 28.964  1.00 22.43 ? 9   LYS H CD  1 
ATOM   7827  C  CE  . LYS H  1 9   ? 47.349  116.537 30.148  1.00 21.44 ? 9   LYS H CE  1 
ATOM   7828  N  NZ  . LYS H  1 9   ? 47.521  115.853 31.494  1.00 19.26 ? 9   LYS H NZ  1 
ATOM   7829  N  N   . GLY H  1 10  ? 46.972  112.089 25.693  1.00 14.39 ? 10  GLY H N   1 
ATOM   7830  C  CA  . GLY H  1 10  ? 46.652  111.293 24.511  1.00 11.55 ? 10  GLY H CA  1 
ATOM   7831  C  C   . GLY H  1 10  ? 45.226  111.487 23.998  1.00 14.93 ? 10  GLY H C   1 
ATOM   7832  O  O   . GLY H  1 10  ? 44.549  112.459 24.338  1.00 15.39 ? 10  GLY H O   1 
ATOM   7833  N  N   . ASP H  1 11  ? 44.763  110.540 23.193  1.00 15.54 ? 11  ASP H N   1 
ATOM   7834  C  CA  . ASP H  1 11  ? 43.468  110.660 22.534  1.00 21.50 ? 11  ASP H CA  1 
ATOM   7835  C  C   . ASP H  1 11  ? 42.297  110.237 23.432  1.00 22.86 ? 11  ASP H C   1 
ATOM   7836  O  O   . ASP H  1 11  ? 41.174  110.667 23.217  1.00 24.31 ? 11  ASP H O   1 
ATOM   7837  C  CB  . ASP H  1 11  ? 43.466  109.865 21.230  1.00 20.23 ? 11  ASP H CB  1 
ATOM   7838  C  CG  . ASP H  1 11  ? 44.307  110.527 20.149  1.00 35.85 ? 11  ASP H CG  1 
ATOM   7839  O  OD1 . ASP H  1 11  ? 44.372  111.778 20.119  1.00 36.95 ? 11  ASP H OD1 1 
ATOM   7840  O  OD2 . ASP H  1 11  ? 44.910  109.802 19.329  1.00 46.21 ? 11  ASP H OD2 1 
ATOM   7841  N  N   . GLY H  1 12  ? 42.567  109.408 24.439  1.00 19.66 ? 12  GLY H N   1 
ATOM   7842  C  CA  . GLY H  1 12  ? 41.531  108.952 25.348  1.00 13.07 ? 12  GLY H CA  1 
ATOM   7843  C  C   . GLY H  1 12  ? 41.606  109.604 26.713  1.00 13.31 ? 12  GLY H C   1 
ATOM   7844  O  O   . GLY H  1 12  ? 42.018  110.764 26.824  1.00 14.53 ? 12  GLY H O   1 
ATOM   7845  N  N   . PRO H  1 13  ? 41.192  108.870 27.767  1.00 11.45 ? 13  PRO H N   1 
ATOM   7846  C  CA  . PRO H  1 13  ? 41.181  109.463 29.104  1.00 10.00 ? 13  PRO H CA  1 
ATOM   7847  C  C   . PRO H  1 13  ? 42.531  109.392 29.848  1.00 10.30 ? 13  PRO H C   1 
ATOM   7848  O  O   . PRO H  1 13  ? 42.612  109.889 30.970  1.00 9.25  ? 13  PRO H O   1 
ATOM   7849  C  CB  . PRO H  1 13  ? 40.134  108.611 29.841  1.00 10.03 ? 13  PRO H CB  1 
ATOM   7850  C  CG  . PRO H  1 13  ? 40.239  107.271 29.193  1.00 10.25 ? 13  PRO H CG  1 
ATOM   7851  C  CD  . PRO H  1 13  ? 40.571  107.526 27.753  1.00 10.44 ? 13  PRO H CD  1 
ATOM   7852  N  N   . VAL H  1 14  ? 43.562  108.793 29.254  1.00 10.19 ? 14  VAL H N   1 
ATOM   7853  C  CA  . VAL H  1 14  ? 44.846  108.641 29.966  1.00 9.86  ? 14  VAL H CA  1 
ATOM   7854  C  C   . VAL H  1 14  ? 45.578  109.971 30.059  1.00 10.46 ? 14  VAL H C   1 
ATOM   7855  O  O   . VAL H  1 14  ? 45.855  110.610 29.060  1.00 10.29 ? 14  VAL H O   1 
ATOM   7856  C  CB  . VAL H  1 14  ? 45.762  107.595 29.310  1.00 8.88  ? 14  VAL H CB  1 
ATOM   7857  C  CG1 . VAL H  1 14  ? 47.124  107.559 30.038  1.00 7.25  ? 14  VAL H CG1 1 
ATOM   7858  C  CG2 . VAL H  1 14  ? 45.092  106.220 29.347  1.00 10.40 ? 14  VAL H CG2 1 
ATOM   7859  N  N   . GLN H  1 15  ? 45.888  110.411 31.263  1.00 10.35 ? 15  GLN H N   1 
ATOM   7860  C  CA  . GLN H  1 15  ? 46.579  111.686 31.366  1.00 12.02 ? 15  GLN H CA  1 
ATOM   7861  C  C   . GLN H  1 15  ? 47.299  111.724 32.682  1.00 11.39 ? 15  GLN H C   1 
ATOM   7862  O  O   . GLN H  1 15  ? 46.876  111.078 33.625  1.00 11.76 ? 15  GLN H O   1 
ATOM   7863  C  CB  . GLN H  1 15  ? 45.608  112.864 31.218  1.00 14.26 ? 15  GLN H CB  1 
ATOM   7864  C  CG  . GLN H  1 15  ? 44.373  112.768 32.111  1.00 19.08 ? 15  GLN H CG  1 
ATOM   7865  C  CD  . GLN H  1 15  ? 43.499  114.003 32.025  1.00 27.86 ? 15  GLN H CD  1 
ATOM   7866  O  OE1 . GLN H  1 15  ? 44.001  115.124 31.907  1.00 36.36 ? 15  GLN H OE1 1 
ATOM   7867  N  NE2 . GLN H  1 15  ? 42.178  113.806 32.084  1.00 31.39 ? 15  GLN H NE2 1 
ATOM   7868  N  N   . GLY H  1 16  ? 48.416  112.441 32.748  1.00 11.44 ? 16  GLY H N   1 
ATOM   7869  C  CA  . GLY H  1 16  ? 49.178  112.441 33.977  1.00 11.83 ? 16  GLY H CA  1 
ATOM   7870  C  C   . GLY H  1 16  ? 50.411  113.315 33.950  1.00 12.52 ? 16  GLY H C   1 
ATOM   7871  O  O   . GLY H  1 16  ? 50.761  113.894 32.918  1.00 11.79 ? 16  GLY H O   1 
ATOM   7872  N  N   . ILE H  1 17  ? 51.044  113.429 35.108  1.00 9.90  ? 17  ILE H N   1 
ATOM   7873  C  CA  . ILE H  1 17  ? 52.257  114.204 35.252  1.00 11.59 ? 17  ILE H CA  1 
ATOM   7874  C  C   . ILE H  1 17  ? 53.319  113.338 35.903  1.00 9.87  ? 17  ILE H C   1 
ATOM   7875  O  O   . ILE H  1 17  ? 53.125  112.837 36.990  1.00 11.26 ? 17  ILE H O   1 
ATOM   7876  C  CB  . ILE H  1 17  ? 52.009  115.433 36.120  1.00 13.46 ? 17  ILE H CB  1 
ATOM   7877  C  CG1 . ILE H  1 17  ? 51.193  116.454 35.328  1.00 12.14 ? 17  ILE H CG1 1 
ATOM   7878  C  CG2 . ILE H  1 17  ? 53.332  116.067 36.562  1.00 11.61 ? 17  ILE H CG2 1 
ATOM   7879  C  CD1 . ILE H  1 17  ? 50.622  117.549 36.183  1.00 17.69 ? 17  ILE H CD1 1 
ATOM   7880  N  N   . ILE H  1 18  ? 54.443  113.162 35.230  1.00 9.59  ? 18  ILE H N   1 
ATOM   7881  C  CA  . ILE H  1 18  ? 55.518  112.360 35.768  1.00 7.64  ? 18  ILE H CA  1 
ATOM   7882  C  C   . ILE H  1 18  ? 56.723  113.254 36.074  1.00 9.66  ? 18  ILE H C   1 
ATOM   7883  O  O   . ILE H  1 18  ? 57.175  114.022 35.218  1.00 9.86  ? 18  ILE H O   1 
ATOM   7884  C  CB  . ILE H  1 18  ? 55.891  111.274 34.777  1.00 7.81  ? 18  ILE H CB  1 
ATOM   7885  C  CG1 . ILE H  1 18  ? 54.750  110.260 34.658  1.00 8.35  ? 18  ILE H CG1 1 
ATOM   7886  C  CG2 . ILE H  1 18  ? 57.174  110.599 35.175  1.00 8.45  ? 18  ILE H CG2 1 
ATOM   7887  C  CD1 . ILE H  1 18  ? 54.429  109.537 35.973  1.00 7.20  ? 18  ILE H CD1 1 
ATOM   7888  N  N   . ASN H  1 19  ? 57.218  113.165 37.306  1.00 9.71  ? 19  ASN H N   1 
ATOM   7889  C  CA  . ASN H  1 19  ? 58.423  113.886 37.723  1.00 11.41 ? 19  ASN H CA  1 
ATOM   7890  C  C   . ASN H  1 19  ? 59.683  113.032 37.685  1.00 11.40 ? 19  ASN H C   1 
ATOM   7891  O  O   . ASN H  1 19  ? 59.633  111.830 37.952  1.00 11.69 ? 19  ASN H O   1 
ATOM   7892  C  CB  . ASN H  1 19  ? 58.256  114.428 39.146  1.00 11.32 ? 19  ASN H CB  1 
ATOM   7893  C  CG  . ASN H  1 19  ? 57.016  115.278 39.298  1.00 13.63 ? 19  ASN H CG  1 
ATOM   7894  O  OD1 . ASN H  1 19  ? 56.956  116.414 38.815  1.00 12.83 ? 19  ASN H OD1 1 
ATOM   7895  N  ND2 . ASN H  1 19  ? 56.010  114.727 39.966  1.00 15.98 ? 19  ASN H ND2 1 
ATOM   7896  N  N   . PHE H  1 20  ? 60.813  113.665 37.390  1.00 10.15 ? 20  PHE H N   1 
ATOM   7897  C  CA  . PHE H  1 20  ? 62.109  112.993 37.453  1.00 11.53 ? 20  PHE H CA  1 
ATOM   7898  C  C   . PHE H  1 20  ? 63.017  113.809 38.352  1.00 15.44 ? 20  PHE H C   1 
ATOM   7899  O  O   . PHE H  1 20  ? 63.005  115.035 38.284  1.00 14.71 ? 20  PHE H O   1 
ATOM   7900  C  CB  . PHE H  1 20  ? 62.762  112.891 36.063  1.00 9.08  ? 20  PHE H CB  1 
ATOM   7901  C  CG  . PHE H  1 20  ? 61.925  112.160 35.044  1.00 8.34  ? 20  PHE H CG  1 
ATOM   7902  C  CD1 . PHE H  1 20  ? 60.845  112.791 34.430  1.00 7.08  ? 20  PHE H CD1 1 
ATOM   7903  C  CD2 . PHE H  1 20  ? 62.205  110.840 34.713  1.00 6.35  ? 20  PHE H CD2 1 
ATOM   7904  C  CE1 . PHE H  1 20  ? 60.071  112.121 33.482  1.00 6.27  ? 20  PHE H CE1 1 
ATOM   7905  C  CE2 . PHE H  1 20  ? 61.445  110.165 33.772  1.00 7.30  ? 20  PHE H CE2 1 
ATOM   7906  C  CZ  . PHE H  1 20  ? 60.361  110.801 33.162  1.00 5.65  ? 20  PHE H CZ  1 
ATOM   7907  N  N   . GLU H  1 21  ? 63.805  113.138 39.187  1.00 13.35 ? 21  GLU H N   1 
ATOM   7908  C  CA  . GLU H  1 21  ? 64.827  113.838 39.965  1.00 17.47 ? 21  GLU H CA  1 
ATOM   7909  C  C   . GLU H  1 21  ? 66.103  113.012 40.073  1.00 17.82 ? 21  GLU H C   1 
ATOM   7910  O  O   . GLU H  1 21  ? 66.061  111.846 40.464  1.00 16.02 ? 21  GLU H O   1 
ATOM   7911  C  CB  . GLU H  1 21  ? 64.329  114.224 41.361  1.00 18.59 ? 21  GLU H CB  1 
ATOM   7912  C  CG  . GLU H  1 21  ? 65.305  115.151 42.095  1.00 23.02 ? 21  GLU H CG  1 
ATOM   7913  C  CD  . GLU H  1 21  ? 64.828  115.567 43.469  1.00 23.88 ? 21  GLU H CD  1 
ATOM   7914  O  OE1 . GLU H  1 21  ? 65.603  116.204 44.209  1.00 34.53 ? 21  GLU H OE1 1 
ATOM   7915  O  OE2 . GLU H  1 21  ? 63.683  115.259 43.819  1.00 26.08 ? 21  GLU H OE2 1 
ATOM   7916  N  N   . GLN H  1 22  ? 67.224  113.621 39.691  1.00 19.38 ? 22  GLN H N   1 
ATOM   7917  C  CA  . GLN H  1 22  ? 68.531  112.980 39.773  1.00 24.54 ? 22  GLN H CA  1 
ATOM   7918  C  C   . GLN H  1 22  ? 69.431  113.815 40.679  1.00 29.08 ? 22  GLN H C   1 
ATOM   7919  O  O   . GLN H  1 22  ? 70.002  114.811 40.238  1.00 26.47 ? 22  GLN H O   1 
ATOM   7920  C  CB  . GLN H  1 22  ? 69.163  112.840 38.385  1.00 19.85 ? 22  GLN H CB  1 
ATOM   7921  C  CG  . GLN H  1 22  ? 70.304  111.829 38.307  1.00 21.30 ? 22  GLN H CG  1 
ATOM   7922  C  CD  . GLN H  1 22  ? 70.884  111.701 36.898  1.00 20.54 ? 22  GLN H CD  1 
ATOM   7923  O  OE1 . GLN H  1 22  ? 70.851  112.653 36.118  1.00 18.95 ? 22  GLN H OE1 1 
ATOM   7924  N  NE2 . GLN H  1 22  ? 71.408  110.521 36.567  1.00 15.56 ? 22  GLN H NE2 1 
ATOM   7925  N  N   . LYS H  1 23  ? 69.525  113.403 41.945  1.00 33.05 ? 23  LYS H N   1 
ATOM   7926  C  CA  . LYS H  1 23  ? 70.323  114.082 42.974  1.00 35.33 ? 23  LYS H CA  1 
ATOM   7927  C  C   . LYS H  1 23  ? 71.775  114.301 42.546  1.00 36.48 ? 23  LYS H C   1 
ATOM   7928  O  O   . LYS H  1 23  ? 72.324  115.394 42.686  1.00 37.25 ? 23  LYS H O   1 
ATOM   7929  C  CB  . LYS H  1 23  ? 70.322  113.260 44.274  1.00 39.24 ? 23  LYS H CB  1 
ATOM   7930  C  CG  . LYS H  1 23  ? 69.121  113.453 45.182  1.00 37.50 ? 23  LYS H CG  1 
ATOM   7931  C  CD  . LYS H  1 23  ? 69.185  112.476 46.366  1.00 40.60 ? 23  LYS H CD  1 
ATOM   7932  C  CE  . LYS H  1 23  ? 68.131  112.776 47.431  1.00 49.31 ? 23  LYS H CE  1 
ATOM   7933  N  NZ  . LYS H  1 23  ? 68.288  111.914 48.655  1.00 53.94 ? 23  LYS H NZ  1 
ATOM   7934  N  N   . GLU H  1 24  ? 72.388  113.246 42.030  1.00 34.64 ? 24  GLU H N   1 
ATOM   7935  C  CA  . GLU H  1 24  ? 73.796  113.269 41.668  1.00 41.07 ? 24  GLU H CA  1 
ATOM   7936  C  C   . GLU H  1 24  ? 74.005  113.001 40.192  1.00 36.97 ? 24  GLU H C   1 
ATOM   7937  O  O   . GLU H  1 24  ? 73.342  112.147 39.607  1.00 31.30 ? 24  GLU H O   1 
ATOM   7938  C  CB  . GLU H  1 24  ? 74.571  112.242 42.488  1.00 38.27 ? 24  GLU H CB  1 
ATOM   7939  C  CG  . GLU H  1 24  ? 74.751  112.643 43.939  1.00 49.57 ? 24  GLU H CG  1 
ATOM   7940  C  CD  . GLU H  1 24  ? 75.420  111.546 44.754  1.00 63.29 ? 24  GLU H CD  1 
ATOM   7941  O  OE1 . GLU H  1 24  ? 74.994  110.372 44.628  1.00 58.47 ? 24  GLU H OE1 1 
ATOM   7942  O  OE2 . GLU H  1 24  ? 76.375  111.853 45.506  1.00 59.43 ? 24  GLU H OE2 1 
ATOM   7943  N  N   . SER H  1 25  ? 74.971  113.714 39.618  1.00 40.87 ? 25  SER H N   1 
ATOM   7944  C  CA  . SER H  1 25  ? 75.218  113.748 38.177  1.00 40.19 ? 25  SER H CA  1 
ATOM   7945  C  C   . SER H  1 25  ? 75.282  112.371 37.522  1.00 41.26 ? 25  SER H C   1 
ATOM   7946  O  O   . SER H  1 25  ? 75.023  112.208 36.322  1.00 47.30 ? 25  SER H O   1 
ATOM   7947  C  CB  . SER H  1 25  ? 76.521  114.503 37.911  1.00 47.25 ? 25  SER H CB  1 
ATOM   7948  O  OG  . SER H  1 25  ? 76.653  115.595 38.809  1.00 54.04 ? 25  SER H OG  1 
ATOM   7949  N  N   . ASN H  1 26  ? 75.620  111.376 38.322  1.00 37.56 ? 26  ASN H N   1 
ATOM   7950  C  CA  . ASN H  1 26  ? 75.821  110.035 37.815  1.00 41.29 ? 26  ASN H CA  1 
ATOM   7951  C  C   . ASN H  1 26  ? 74.709  109.100 38.265  1.00 36.05 ? 26  ASN H C   1 
ATOM   7952  O  O   . ASN H  1 26  ? 74.371  108.136 37.578  1.00 36.37 ? 26  ASN H O   1 
ATOM   7953  C  CB  . ASN H  1 26  ? 77.141  109.514 38.374  1.00 41.71 ? 26  ASN H CB  1 
ATOM   7954  C  CG  . ASN H  1 26  ? 77.203  109.620 39.900  1.00 39.55 ? 26  ASN H CG  1 
ATOM   7955  O  OD1 . ASN H  1 26  ? 77.359  110.716 40.456  1.00 40.90 ? 26  ASN H OD1 1 
ATOM   7956  N  ND2 . ASN H  1 26  ? 77.061  108.482 40.584  1.00 41.35 ? 26  ASN H ND2 1 
ATOM   7957  N  N   . GLY H  1 27  ? 74.151  109.409 39.430  1.00 36.88 ? 27  GLY H N   1 
ATOM   7958  C  CA  . GLY H  1 27  ? 73.387  108.462 40.216  1.00 36.50 ? 27  GLY H CA  1 
ATOM   7959  C  C   . GLY H  1 27  ? 71.992  108.132 39.739  1.00 26.21 ? 27  GLY H C   1 
ATOM   7960  O  O   . GLY H  1 27  ? 71.633  108.367 38.586  1.00 31.34 ? 27  GLY H O   1 
ATOM   7961  N  N   . PRO H  1 28  ? 71.195  107.569 40.640  1.00 25.46 ? 28  PRO H N   1 
ATOM   7962  C  CA  . PRO H  1 28  ? 69.865  107.060 40.323  1.00 25.43 ? 28  PRO H CA  1 
ATOM   7963  C  C   . PRO H  1 28  ? 68.879  108.193 40.021  1.00 21.11 ? 28  PRO H C   1 
ATOM   7964  O  O   . PRO H  1 28  ? 68.911  109.248 40.656  1.00 20.82 ? 28  PRO H O   1 
ATOM   7965  C  CB  . PRO H  1 28  ? 69.469  106.324 41.608  1.00 24.46 ? 28  PRO H CB  1 
ATOM   7966  C  CG  . PRO H  1 28  ? 70.221  107.053 42.692  1.00 30.12 ? 28  PRO H CG  1 
ATOM   7967  C  CD  . PRO H  1 28  ? 71.532  107.405 42.065  1.00 31.56 ? 28  PRO H CD  1 
ATOM   7968  N  N   . VAL H  1 29  ? 68.006  107.966 39.049  1.00 20.69 ? 29  VAL H N   1 
ATOM   7969  C  CA  . VAL H  1 29  ? 66.897  108.898 38.784  1.00 16.41 ? 29  VAL H CA  1 
ATOM   7970  C  C   . VAL H  1 29  ? 65.618  108.419 39.481  1.00 15.97 ? 29  VAL H C   1 
ATOM   7971  O  O   . VAL H  1 29  ? 65.178  107.289 39.261  1.00 15.47 ? 29  VAL H O   1 
ATOM   7972  C  CB  . VAL H  1 29  ? 66.638  109.031 37.274  1.00 15.15 ? 29  VAL H CB  1 
ATOM   7973  C  CG1 . VAL H  1 29  ? 65.557  110.098 36.989  1.00 13.40 ? 29  VAL H CG1 1 
ATOM   7974  C  CG2 . VAL H  1 29  ? 67.929  109.382 36.565  1.00 12.63 ? 29  VAL H CG2 1 
ATOM   7975  N  N   . LYS H  1 30  ? 65.033  109.268 40.327  1.00 14.24 ? 30  LYS H N   1 
ATOM   7976  C  CA  . LYS H  1 30  ? 63.712  108.989 40.892  1.00 16.10 ? 30  LYS H CA  1 
ATOM   7977  C  C   . LYS H  1 30  ? 62.582  109.431 39.942  1.00 12.94 ? 30  LYS H C   1 
ATOM   7978  O  O   . LYS H  1 30  ? 62.560  110.559 39.476  1.00 13.46 ? 30  LYS H O   1 
ATOM   7979  C  CB  . LYS H  1 30  ? 63.557  109.636 42.276  1.00 17.26 ? 30  LYS H CB  1 
ATOM   7980  C  CG  . LYS H  1 30  ? 64.359  108.897 43.358  1.00 24.43 ? 30  LYS H CG  1 
ATOM   7981  C  CD  . LYS H  1 30  ? 64.540  109.726 44.613  1.00 37.56 ? 30  LYS H CD  1 
ATOM   7982  C  CE  . LYS H  1 30  ? 65.419  108.998 45.633  1.00 39.61 ? 30  LYS H CE  1 
ATOM   7983  N  NZ  . LYS H  1 30  ? 65.740  109.873 46.798  1.00 45.52 ? 30  LYS H NZ  1 
ATOM   7984  N  N   . VAL H  1 31  ? 61.659  108.524 39.657  1.00 11.05 ? 31  VAL H N   1 
ATOM   7985  C  CA  . VAL H  1 31  ? 60.556  108.806 38.751  1.00 10.66 ? 31  VAL H CA  1 
ATOM   7986  C  C   . VAL H  1 31  ? 59.277  108.594 39.523  1.00 13.17 ? 31  VAL H C   1 
ATOM   7987  O  O   . VAL H  1 31  ? 59.087  107.531 40.116  1.00 12.10 ? 31  VAL H O   1 
ATOM   7988  C  CB  . VAL H  1 31  ? 60.547  107.845 37.557  1.00 7.92  ? 31  VAL H CB  1 
ATOM   7989  C  CG1 . VAL H  1 31  ? 59.502  108.303 36.515  1.00 7.29  ? 31  VAL H CG1 1 
ATOM   7990  C  CG2 . VAL H  1 31  ? 61.941  107.759 36.932  1.00 9.89  ? 31  VAL H CG2 1 
ATOM   7991  N  N   . TRP H  1 32  ? 58.408  109.597 39.540  1.00 9.81  ? 32  TRP H N   1 
ATOM   7992  C  CA  . TRP H  1 32  ? 57.158  109.461 40.282  1.00 10.69 ? 32  TRP H CA  1 
ATOM   7993  C  C   . TRP H  1 32  ? 56.103  110.445 39.822  1.00 10.68 ? 32  TRP H C   1 
ATOM   7994  O  O   . TRP H  1 32  ? 56.400  111.486 39.229  1.00 9.42  ? 32  TRP H O   1 
ATOM   7995  C  CB  . TRP H  1 32  ? 57.367  109.631 41.784  1.00 9.51  ? 32  TRP H CB  1 
ATOM   7996  C  CG  . TRP H  1 32  ? 57.468  111.067 42.208  1.00 11.81 ? 32  TRP H CG  1 
ATOM   7997  C  CD1 . TRP H  1 32  ? 56.474  111.851 42.762  1.00 12.83 ? 32  TRP H CD1 1 
ATOM   7998  C  CD2 . TRP H  1 32  ? 58.626  111.904 42.112  1.00 13.49 ? 32  TRP H CD2 1 
ATOM   7999  N  NE1 . TRP H  1 32  ? 56.954  113.118 43.008  1.00 13.67 ? 32  TRP H NE1 1 
ATOM   8000  C  CE2 . TRP H  1 32  ? 58.270  113.178 42.618  1.00 15.03 ? 32  TRP H CE2 1 
ATOM   8001  C  CE3 . TRP H  1 32  ? 59.927  111.704 41.637  1.00 14.37 ? 32  TRP H CE3 1 
ATOM   8002  C  CZ2 . TRP H  1 32  ? 59.170  114.236 42.668  1.00 15.35 ? 32  TRP H CZ2 1 
ATOM   8003  C  CZ3 . TRP H  1 32  ? 60.816  112.760 41.679  1.00 16.68 ? 32  TRP H CZ3 1 
ATOM   8004  C  CH2 . TRP H  1 32  ? 60.435  114.013 42.197  1.00 17.97 ? 32  TRP H CH2 1 
ATOM   8005  N  N   . GLY H  1 33  ? 54.855  110.105 40.110  1.00 10.21 ? 33  GLY H N   1 
ATOM   8006  C  CA  . GLY H  1 33  ? 53.753  110.951 39.708  1.00 11.42 ? 33  GLY H CA  1 
ATOM   8007  C  C   . GLY H  1 33  ? 52.497  110.138 39.525  1.00 12.87 ? 33  GLY H C   1 
ATOM   8008  O  O   . GLY H  1 33  ? 52.481  108.934 39.749  1.00 14.36 ? 33  GLY H O   1 
ATOM   8009  N  N   . SER H  1 34  ? 51.437  110.797 39.091  1.00 14.24 ? 34  SER H N   1 
ATOM   8010  C  CA  . SER H  1 34  ? 50.148  110.138 38.964  1.00 15.99 ? 34  SER H CA  1 
ATOM   8011  C  C   . SER H  1 34  ? 49.677  110.123 37.516  1.00 11.88 ? 34  SER H C   1 
ATOM   8012  O  O   . SER H  1 34  ? 49.737  111.138 36.830  1.00 15.63 ? 34  SER H O   1 
ATOM   8013  C  CB  . SER H  1 34  ? 49.124  110.849 39.843  1.00 13.79 ? 34  SER H CB  1 
ATOM   8014  O  OG  . SER H  1 34  ? 47.874  110.202 39.730  1.00 24.06 ? 34  SER H OG  1 
ATOM   8015  N  N   . ILE H  1 35  ? 49.247  108.965 37.039  1.00 8.25  ? 35  ILE H N   1 
ATOM   8016  C  CA  . ILE H  1 35  ? 48.590  108.878 35.749  1.00 10.01 ? 35  ILE H CA  1 
ATOM   8017  C  C   . ILE H  1 35  ? 47.167  108.350 35.955  1.00 11.04 ? 35  ILE H C   1 
ATOM   8018  O  O   . ILE H  1 35  ? 46.982  107.323 36.615  1.00 10.22 ? 35  ILE H O   1 
ATOM   8019  C  CB  . ILE H  1 35  ? 49.304  107.896 34.814  1.00 8.91  ? 35  ILE H CB  1 
ATOM   8020  C  CG1 . ILE H  1 35  ? 50.807  108.217 34.733  1.00 7.44  ? 35  ILE H CG1 1 
ATOM   8021  C  CG2 . ILE H  1 35  ? 48.632  107.925 33.441  1.00 8.81  ? 35  ILE H CG2 1 
ATOM   8022  C  CD1 . ILE H  1 35  ? 51.609  107.161 33.973  1.00 8.27  ? 35  ILE H CD1 1 
ATOM   8023  N  N   . LYS H  1 36  ? 46.164  109.037 35.421  1.00 7.18  ? 36  LYS H N   1 
ATOM   8024  C  CA  . LYS H  1 36  ? 44.804  108.509 35.554  1.00 11.86 ? 36  LYS H CA  1 
ATOM   8025  C  C   . LYS H  1 36  ? 44.249  108.030 34.230  1.00 10.11 ? 36  LYS H C   1 
ATOM   8026  O  O   . LYS H  1 36  ? 44.849  108.260 33.185  1.00 9.28  ? 36  LYS H O   1 
ATOM   8027  C  CB  . LYS H  1 36  ? 43.862  109.523 36.208  1.00 10.41 ? 36  LYS H CB  1 
ATOM   8028  C  CG  . LYS H  1 36  ? 43.618  110.767 35.384  1.00 16.22 ? 36  LYS H CG  1 
ATOM   8029  C  CD  . LYS H  1 36  ? 42.726  111.737 36.152  1.00 20.81 ? 36  LYS H CD  1 
ATOM   8030  C  CE  . LYS H  1 36  ? 42.383  112.974 35.335  1.00 29.50 ? 36  LYS H CE  1 
ATOM   8031  N  NZ  . LYS H  1 36  ? 41.608  113.972 36.142  1.00 29.48 ? 36  LYS H NZ  1 
ATOM   8032  N  N   . GLY H  1 37  ? 43.117  107.335 34.288  1.00 10.54 ? 37  GLY H N   1 
ATOM   8033  C  CA  . GLY H  1 37  ? 42.376  106.951 33.095  1.00 8.23  ? 37  GLY H CA  1 
ATOM   8034  C  C   . GLY H  1 37  ? 42.809  105.617 32.519  1.00 9.15  ? 37  GLY H C   1 
ATOM   8035  O  O   . GLY H  1 37  ? 42.436  105.275 31.398  1.00 7.99  ? 37  GLY H O   1 
ATOM   8036  N  N   . LEU H  1 38  ? 43.602  104.860 33.282  1.00 8.78  ? 38  LEU H N   1 
ATOM   8037  C  CA  . LEU H  1 38  ? 44.184  103.608 32.787  1.00 7.28  ? 38  LEU H CA  1 
ATOM   8038  C  C   . LEU H  1 38  ? 43.378  102.412 33.244  1.00 7.43  ? 38  LEU H C   1 
ATOM   8039  O  O   . LEU H  1 38  ? 42.861  102.426 34.350  1.00 7.09  ? 38  LEU H O   1 
ATOM   8040  C  CB  . LEU H  1 38  ? 45.609  103.433 33.329  1.00 7.95  ? 38  LEU H CB  1 
ATOM   8041  C  CG  . LEU H  1 38  ? 46.694  104.377 32.800  1.00 8.12  ? 38  LEU H CG  1 
ATOM   8042  C  CD1 . LEU H  1 38  ? 47.836  104.494 33.800  1.00 6.34  ? 38  LEU H CD1 1 
ATOM   8043  C  CD2 . LEU H  1 38  ? 47.177  103.827 31.477  1.00 4.66  ? 38  LEU H CD2 1 
ATOM   8044  N  N   . THR H  1 39  ? 43.301  101.367 32.419  1.00 7.40  ? 39  THR H N   1 
ATOM   8045  C  CA  . THR H  1 39  ? 42.667  100.132 32.858  1.00 10.04 ? 39  THR H CA  1 
ATOM   8046  C  C   . THR H  1 39  ? 43.449  99.534  34.026  1.00 14.50 ? 39  THR H C   1 
ATOM   8047  O  O   . THR H  1 39  ? 44.692  99.583  34.053  1.00 10.59 ? 39  THR H O   1 
ATOM   8048  C  CB  . THR H  1 39  ? 42.586  99.122  31.736  1.00 11.77 ? 39  THR H CB  1 
ATOM   8049  O  OG1 . THR H  1 39  ? 43.911  98.783  31.319  1.00 12.29 ? 39  THR H OG1 1 
ATOM   8050  C  CG2 . THR H  1 39  ? 41.817  99.720  30.524  1.00 12.17 ? 39  THR H CG2 1 
ATOM   8051  N  N   . GLU H  1 40  ? 42.714  98.995  34.994  1.00 13.22 ? 40  GLU H N   1 
ATOM   8052  C  CA  . GLU H  1 40  ? 43.298  98.368  36.162  1.00 13.23 ? 40  GLU H CA  1 
ATOM   8053  C  C   . GLU H  1 40  ? 44.339  97.336  35.744  1.00 13.11 ? 40  GLU H C   1 
ATOM   8054  O  O   . GLU H  1 40  ? 44.057  96.488  34.914  1.00 14.11 ? 40  GLU H O   1 
ATOM   8055  C  CB  . GLU H  1 40  ? 42.189  97.702  36.996  1.00 16.34 ? 40  GLU H CB  1 
ATOM   8056  C  CG  . GLU H  1 40  ? 42.637  97.021  38.294  1.00 19.21 ? 40  GLU H CG  1 
ATOM   8057  C  CD  . GLU H  1 40  ? 41.441  96.491  39.125  1.00 23.51 ? 40  GLU H CD  1 
ATOM   8058  O  OE1 . GLU H  1 40  ? 40.501  95.909  38.536  1.00 20.28 ? 40  GLU H OE1 1 
ATOM   8059  O  OE2 . GLU H  1 40  ? 41.445  96.682  40.363  1.00 25.91 ? 40  GLU H OE2 1 
ATOM   8060  N  N   . GLY H  1 41  ? 45.541  97.426  36.322  1.00 14.44 ? 41  GLY H N   1 
ATOM   8061  C  CA  . GLY H  1 41  ? 46.618  96.482  36.031  1.00 13.00 ? 41  GLY H CA  1 
ATOM   8062  C  C   . GLY H  1 41  ? 47.900  97.102  35.464  1.00 9.50  ? 41  GLY H C   1 
ATOM   8063  O  O   . GLY H  1 41  ? 48.145  98.289  35.581  1.00 7.40  ? 41  GLY H O   1 
ATOM   8064  N  N   . LEU H  1 42  ? 48.715  96.264  34.844  1.00 10.85 ? 42  LEU H N   1 
ATOM   8065  C  CA  . LEU H  1 42  ? 50.059  96.617  34.394  1.00 9.65  ? 42  LEU H CA  1 
ATOM   8066  C  C   . LEU H  1 42  ? 50.035  97.393  33.078  1.00 8.45  ? 42  LEU H C   1 
ATOM   8067  O  O   . LEU H  1 42  ? 49.288  97.043  32.162  1.00 10.12 ? 42  LEU H O   1 
ATOM   8068  C  CB  . LEU H  1 42  ? 50.809  95.313  34.164  1.00 11.88 ? 42  LEU H CB  1 
ATOM   8069  C  CG  . LEU H  1 42  ? 51.811  94.710  35.138  1.00 15.83 ? 42  LEU H CG  1 
ATOM   8070  C  CD1 . LEU H  1 42  ? 51.796  95.368  36.476  1.00 13.23 ? 42  LEU H CD1 1 
ATOM   8071  C  CD2 . LEU H  1 42  ? 51.593  93.223  35.230  1.00 11.90 ? 42  LEU H CD2 1 
ATOM   8072  N  N   . HIS H  1 43  ? 50.851  98.429  32.964  1.00 8.39  ? 43  HIS H N   1 
ATOM   8073  C  CA  . HIS H  1 43  ? 50.990  99.151  31.691  1.00 6.89  ? 43  HIS H CA  1 
ATOM   8074  C  C   . HIS H  1 43  ? 52.437  99.471  31.380  1.00 7.50  ? 43  HIS H C   1 
ATOM   8075  O  O   . HIS H  1 43  ? 53.120  100.093 32.191  1.00 8.09  ? 43  HIS H O   1 
ATOM   8076  C  CB  . HIS H  1 43  ? 50.183  100.462 31.727  1.00 6.18  ? 43  HIS H CB  1 
ATOM   8077  C  CG  . HIS H  1 43  ? 48.703  100.237 31.745  1.00 7.90  ? 43  HIS H CG  1 
ATOM   8078  N  ND1 . HIS H  1 43  ? 47.936  100.218 30.598  1.00 8.32  ? 43  HIS H ND1 1 
ATOM   8079  C  CD2 . HIS H  1 43  ? 47.861  99.939  32.764  1.00 6.89  ? 43  HIS H CD2 1 
ATOM   8080  C  CE1 . HIS H  1 43  ? 46.679  99.947  30.912  1.00 8.30  ? 43  HIS H CE1 1 
ATOM   8081  N  NE2 . HIS H  1 43  ? 46.606  99.771  32.219  1.00 7.70  ? 43  HIS H NE2 1 
ATOM   8082  N  N   . GLY H  1 44  ? 52.897  99.066  30.200  1.00 6.83  ? 44  GLY H N   1 
ATOM   8083  C  CA  . GLY H  1 44  ? 54.240  99.375  29.743  1.00 7.52  ? 44  GLY H CA  1 
ATOM   8084  C  C   . GLY H  1 44  ? 54.588  100.849 29.852  1.00 8.94  ? 44  GLY H C   1 
ATOM   8085  O  O   . GLY H  1 44  ? 53.759  101.724 29.614  1.00 5.21  ? 44  GLY H O   1 
ATOM   8086  N  N   . PHE H  1 45  ? 55.827  101.132 30.233  1.00 7.65  ? 45  PHE H N   1 
ATOM   8087  C  CA  . PHE H  1 45  ? 56.202  102.491 30.596  1.00 8.48  ? 45  PHE H CA  1 
ATOM   8088  C  C   . PHE H  1 45  ? 57.621  102.695 30.078  1.00 12.41 ? 45  PHE H C   1 
ATOM   8089  O  O   . PHE H  1 45  ? 58.588  102.138 30.643  1.00 8.77  ? 45  PHE H O   1 
ATOM   8090  C  CB  . PHE H  1 45  ? 56.113  102.618 32.114  1.00 6.51  ? 45  PHE H CB  1 
ATOM   8091  C  CG  . PHE H  1 45  ? 56.204  104.023 32.660  1.00 7.71  ? 45  PHE H CG  1 
ATOM   8092  C  CD1 . PHE H  1 45  ? 55.239  104.974 32.374  1.00 8.27  ? 45  PHE H CD1 1 
ATOM   8093  C  CD2 . PHE H  1 45  ? 57.210  104.352 33.560  1.00 7.38  ? 45  PHE H CD2 1 
ATOM   8094  C  CE1 . PHE H  1 45  ? 55.295  106.239 32.924  1.00 5.85  ? 45  PHE H CE1 1 
ATOM   8095  C  CE2 . PHE H  1 45  ? 57.286  105.628 34.105  1.00 9.63  ? 45  PHE H CE2 1 
ATOM   8096  C  CZ  . PHE H  1 45  ? 56.316  106.575 33.786  1.00 7.98  ? 45  PHE H CZ  1 
ATOM   8097  N  N   . HIS H  1 46  ? 57.741  103.468 28.993  1.00 9.15  ? 46  HIS H N   1 
ATOM   8098  C  CA  . HIS H  1 46  ? 59.023  103.590 28.288  1.00 10.11 ? 46  HIS H CA  1 
ATOM   8099  C  C   . HIS H  1 46  ? 59.420  105.011 27.909  1.00 9.05  ? 46  HIS H C   1 
ATOM   8100  O  O   . HIS H  1 46  ? 58.570  105.851 27.595  1.00 7.04  ? 46  HIS H O   1 
ATOM   8101  C  CB  . HIS H  1 46  ? 58.988  102.790 26.991  1.00 8.66  ? 46  HIS H CB  1 
ATOM   8102  C  CG  . HIS H  1 46  ? 58.450  101.410 27.148  1.00 12.53 ? 46  HIS H CG  1 
ATOM   8103  N  ND1 . HIS H  1 46  ? 57.470  100.905 26.325  1.00 12.29 ? 46  HIS H ND1 1 
ATOM   8104  C  CD2 . HIS H  1 46  ? 58.782  100.413 28.001  1.00 10.98 ? 46  HIS H CD2 1 
ATOM   8105  C  CE1 . HIS H  1 46  ? 57.211  99.658  26.671  1.00 13.32 ? 46  HIS H CE1 1 
ATOM   8106  N  NE2 . HIS H  1 46  ? 57.991  99.335  27.688  1.00 13.06 ? 46  HIS H NE2 1 
ATOM   8107  N  N   . VAL H  1 47  ? 60.730  105.253 27.903  1.00 8.03  ? 47  VAL H N   1 
ATOM   8108  C  CA  . VAL H  1 47  ? 61.260  106.439 27.275  1.00 7.71  ? 47  VAL H CA  1 
ATOM   8109  C  C   . VAL H  1 47  ? 61.550  106.038 25.835  1.00 10.12 ? 47  VAL H C   1 
ATOM   8110  O  O   . VAL H  1 47  ? 62.293  105.083 25.592  1.00 9.08  ? 47  VAL H O   1 
ATOM   8111  C  CB  . VAL H  1 47  ? 62.536  106.924 27.933  1.00 8.45  ? 47  VAL H CB  1 
ATOM   8112  C  CG1 . VAL H  1 47  ? 63.123  108.053 27.123  1.00 9.89  ? 47  VAL H CG1 1 
ATOM   8113  C  CG2 . VAL H  1 47  ? 62.255  107.372 29.388  1.00 6.63  ? 47  VAL H CG2 1 
ATOM   8114  N  N   . HIS H  1 48  ? 60.909  106.736 24.901  1.00 7.08  ? 48  HIS H N   1 
ATOM   8115  C  CA  . HIS H  1 48  ? 61.064  106.485 23.474  1.00 10.40 ? 48  HIS H CA  1 
ATOM   8116  C  C   . HIS H  1 48  ? 62.058  107.497 22.910  1.00 9.33  ? 48  HIS H C   1 
ATOM   8117  O  O   . HIS H  1 48  ? 62.254  108.555 23.489  1.00 8.18  ? 48  HIS H O   1 
ATOM   8118  C  CB  . HIS H  1 48  ? 59.713  106.588 22.745  1.00 7.05  ? 48  HIS H CB  1 
ATOM   8119  C  CG  . HIS H  1 48  ? 58.894  105.348 22.834  1.00 11.62 ? 48  HIS H CG  1 
ATOM   8120  N  ND1 . HIS H  1 48  ? 58.622  104.556 21.738  1.00 13.71 ? 48  HIS H ND1 1 
ATOM   8121  C  CD2 . HIS H  1 48  ? 58.318  104.733 23.897  1.00 9.22  ? 48  HIS H CD2 1 
ATOM   8122  C  CE1 . HIS H  1 48  ? 57.898  103.519 22.117  1.00 10.67 ? 48  HIS H CE1 1 
ATOM   8123  N  NE2 . HIS H  1 48  ? 57.704  103.602 23.419  1.00 11.54 ? 48  HIS H NE2 1 
ATOM   8124  N  N   . GLU H  1 49  ? 62.672  107.175 21.780  1.00 10.98 ? 49  GLU H N   1 
ATOM   8125  C  CA  . GLU H  1 49  ? 63.872  107.903 21.340  1.00 10.00 ? 49  GLU H CA  1 
ATOM   8126  C  C   . GLU H  1 49  ? 63.662  109.387 21.012  1.00 13.05 ? 49  GLU H C   1 
ATOM   8127  O  O   . GLU H  1 49  ? 64.461  110.246 21.435  1.00 13.66 ? 49  GLU H O   1 
ATOM   8128  C  CB  . GLU H  1 49  ? 64.522  107.175 20.146  1.00 13.82 ? 49  GLU H CB  1 
ATOM   8129  C  CG  . GLU H  1 49  ? 65.772  107.845 19.619  1.00 14.26 ? 49  GLU H CG  1 
ATOM   8130  C  CD  . GLU H  1 49  ? 66.454  107.069 18.502  1.00 20.82 ? 49  GLU H CD  1 
ATOM   8131  O  OE1 . GLU H  1 49  ? 65.805  106.207 17.853  1.00 19.30 ? 49  GLU H OE1 1 
ATOM   8132  O  OE2 . GLU H  1 49  ? 67.655  107.346 18.265  1.00 23.85 ? 49  GLU H OE2 1 
ATOM   8133  N  N   . PHE H  1 50  ? 62.605  109.699 20.261  1.00 10.07 ? 50  PHE H N   1 
ATOM   8134  C  CA  . PHE H  1 50  ? 62.431  111.065 19.771  1.00 10.57 ? 50  PHE H CA  1 
ATOM   8135  C  C   . PHE H  1 50  ? 61.370  111.884 20.514  1.00 11.19 ? 50  PHE H C   1 
ATOM   8136  O  O   . PHE H  1 50  ? 60.264  111.416 20.748  1.00 11.94 ? 50  PHE H O   1 
ATOM   8137  C  CB  . PHE H  1 50  ? 62.130  111.056 18.271  1.00 10.00 ? 50  PHE H CB  1 
ATOM   8138  C  CG  . PHE H  1 50  ? 63.161  110.333 17.463  1.00 14.07 ? 50  PHE H CG  1 
ATOM   8139  C  CD1 . PHE H  1 50  ? 64.467  110.802 17.405  1.00 13.27 ? 50  PHE H CD1 1 
ATOM   8140  C  CD2 . PHE H  1 50  ? 62.838  109.172 16.781  1.00 12.99 ? 50  PHE H CD2 1 
ATOM   8141  C  CE1 . PHE H  1 50  ? 65.420  110.126 16.684  1.00 16.67 ? 50  PHE H CE1 1 
ATOM   8142  C  CE2 . PHE H  1 50  ? 63.797  108.495 16.051  1.00 14.13 ? 50  PHE H CE2 1 
ATOM   8143  C  CZ  . PHE H  1 50  ? 65.085  108.967 16.008  1.00 16.21 ? 50  PHE H CZ  1 
ATOM   8144  N  N   . GLY H  1 51  ? 61.709  113.122 20.853  1.00 9.31  ? 51  GLY H N   1 
ATOM   8145  C  CA  . GLY H  1 51  ? 60.762  114.027 21.478  1.00 10.10 ? 51  GLY H CA  1 
ATOM   8146  C  C   . GLY H  1 51  ? 59.963  114.728 20.399  1.00 11.95 ? 51  GLY H C   1 
ATOM   8147  O  O   . GLY H  1 51  ? 59.872  115.955 20.369  1.00 12.86 ? 51  GLY H O   1 
ATOM   8148  N  N   . ASP H  1 52  ? 59.382  113.921 19.518  1.00 11.65 ? 52  ASP H N   1 
ATOM   8149  C  CA  . ASP H  1 52  ? 58.722  114.387 18.307  1.00 14.99 ? 52  ASP H CA  1 
ATOM   8150  C  C   . ASP H  1 52  ? 57.255  113.963 18.341  1.00 14.78 ? 52  ASP H C   1 
ATOM   8151  O  O   . ASP H  1 52  ? 56.934  112.791 18.147  1.00 12.94 ? 52  ASP H O   1 
ATOM   8152  C  CB  . ASP H  1 52  ? 59.432  113.770 17.093  1.00 14.17 ? 52  ASP H CB  1 
ATOM   8153  C  CG  . ASP H  1 52  ? 58.824  114.194 15.750  1.00 17.64 ? 52  ASP H CG  1 
ATOM   8154  O  OD1 . ASP H  1 52  ? 57.651  114.632 15.698  1.00 16.31 ? 52  ASP H OD1 1 
ATOM   8155  O  OD2 . ASP H  1 52  ? 59.538  114.061 14.726  1.00 14.30 ? 52  ASP H OD2 1 
ATOM   8156  N  N   . ASN H  1 53  ? 56.372  114.923 18.588  1.00 15.22 ? 53  ASN H N   1 
ATOM   8157  C  CA  . ASN H  1 53  ? 54.936  114.664 18.618  1.00 21.47 ? 53  ASN H CA  1 
ATOM   8158  C  C   . ASN H  1 53  ? 54.184  115.192 17.383  1.00 20.03 ? 53  ASN H C   1 
ATOM   8159  O  O   . ASN H  1 53  ? 52.978  115.381 17.434  1.00 22.13 ? 53  ASN H O   1 
ATOM   8160  C  CB  . ASN H  1 53  ? 54.324  115.263 19.892  1.00 21.02 ? 53  ASN H CB  1 
ATOM   8161  C  CG  . ASN H  1 53  ? 52.899  114.772 20.147  1.00 27.77 ? 53  ASN H CG  1 
ATOM   8162  O  OD1 . ASN H  1 53  ? 51.945  115.562 20.202  1.00 27.16 ? 53  ASN H OD1 1 
ATOM   8163  N  ND2 . ASN H  1 53  ? 52.748  113.459 20.277  1.00 28.04 ? 53  ASN H ND2 1 
ATOM   8164  N  N   . THR H  1 54  ? 54.885  115.437 16.275  1.00 22.52 ? 54  THR H N   1 
ATOM   8165  C  CA  . THR H  1 54  ? 54.221  115.960 15.070  1.00 21.41 ? 54  THR H CA  1 
ATOM   8166  C  C   . THR H  1 54  ? 53.113  115.038 14.551  1.00 24.24 ? 54  THR H C   1 
ATOM   8167  O  O   . THR H  1 54  ? 52.073  115.503 14.090  1.00 24.05 ? 54  THR H O   1 
ATOM   8168  C  CB  . THR H  1 54  ? 55.201  116.152 13.926  1.00 22.59 ? 54  THR H CB  1 
ATOM   8169  O  OG1 . THR H  1 54  ? 55.933  114.934 13.741  1.00 25.05 ? 54  THR H OG1 1 
ATOM   8170  C  CG2 . THR H  1 54  ? 56.148  117.313 14.212  1.00 13.77 ? 54  THR H CG2 1 
ATOM   8171  N  N   . ALA H  1 55  ? 53.347  113.731 14.617  1.00 25.14 ? 55  ALA H N   1 
ATOM   8172  C  CA  . ALA H  1 55  ? 52.368  112.760 14.135  1.00 25.90 ? 55  ALA H CA  1 
ATOM   8173  C  C   . ALA H  1 55  ? 51.848  111.942 15.297  1.00 27.38 ? 55  ALA H C   1 
ATOM   8174  O  O   . ALA H  1 55  ? 51.713  110.726 15.185  1.00 29.70 ? 55  ALA H O   1 
ATOM   8175  C  CB  . ALA H  1 55  ? 52.975  111.852 13.058  1.00 21.28 ? 55  ALA H CB  1 
ATOM   8176  N  N   . GLY H  1 56  ? 51.560  112.623 16.408  1.00 24.70 ? 56  GLY H N   1 
ATOM   8177  C  CA  . GLY H  1 56  ? 51.083  111.978 17.618  1.00 21.68 ? 56  GLY H CA  1 
ATOM   8178  C  C   . GLY H  1 56  ? 52.190  111.145 18.229  1.00 27.52 ? 56  GLY H C   1 
ATOM   8179  O  O   . GLY H  1 56  ? 53.366  111.373 17.949  1.00 27.43 ? 56  GLY H O   1 
ATOM   8180  N  N   . SER H  1 57  ? 51.830  110.165 19.050  1.00 26.42 ? 57  SER H N   1 
ATOM   8181  C  CA  . SER H  1 57  ? 52.835  109.340 19.708  1.00 24.14 ? 57  SER H CA  1 
ATOM   8182  C  C   . SER H  1 57  ? 53.620  108.496 18.707  1.00 20.67 ? 57  SER H C   1 
ATOM   8183  O  O   . SER H  1 57  ? 54.743  108.078 18.979  1.00 21.33 ? 57  SER H O   1 
ATOM   8184  C  CB  . SER H  1 57  ? 52.182  108.437 20.744  1.00 23.33 ? 57  SER H CB  1 
ATOM   8185  O  OG  . SER H  1 57  ? 51.059  107.783 20.177  1.00 22.71 ? 57  SER H OG  1 
ATOM   8186  N  N   . THR H  1 58  ? 53.053  108.261 17.534  1.00 21.54 ? 58  THR H N   1 
ATOM   8187  C  CA  . THR H  1 58  ? 53.715  107.367 16.592  1.00 21.28 ? 58  THR H CA  1 
ATOM   8188  C  C   . THR H  1 58  ? 55.074  107.883 16.089  1.00 24.04 ? 58  THR H C   1 
ATOM   8189  O  O   . THR H  1 58  ? 55.964  107.084 15.759  1.00 25.81 ? 58  THR H O   1 
ATOM   8190  C  CB  . THR H  1 58  ? 52.779  106.960 15.425  1.00 26.10 ? 58  THR H CB  1 
ATOM   8191  O  OG1 . THR H  1 58  ? 53.368  107.342 14.185  1.00 25.70 ? 58  THR H OG1 1 
ATOM   8192  C  CG2 . THR H  1 58  ? 51.410  107.617 15.566  1.00 23.45 ? 58  THR H CG2 1 
ATOM   8193  N  N   . SER H  1 59  ? 55.264  109.201 16.067  1.00 21.55 ? 59  SER H N   1 
ATOM   8194  C  CA  . SER H  1 59  ? 56.560  109.755 15.648  1.00 18.15 ? 59  SER H CA  1 
ATOM   8195  C  C   . SER H  1 59  ? 57.628  109.778 16.764  1.00 18.65 ? 59  SER H C   1 
ATOM   8196  O  O   . SER H  1 59  ? 58.735  110.280 16.560  1.00 14.53 ? 59  SER H O   1 
ATOM   8197  C  CB  . SER H  1 59  ? 56.405  111.147 15.009  1.00 16.85 ? 59  SER H CB  1 
ATOM   8198  O  OG  . SER H  1 59  ? 55.614  112.001 15.811  1.00 21.30 ? 59  SER H OG  1 
ATOM   8199  N  N   . ALA H  1 60  ? 57.301  109.213 17.922  1.00 14.75 ? 60  ALA H N   1 
ATOM   8200  C  CA  . ALA H  1 60  ? 58.244  109.141 19.038  1.00 16.14 ? 60  ALA H CA  1 
ATOM   8201  C  C   . ALA H  1 60  ? 59.382  108.154 18.753  1.00 11.77 ? 60  ALA H C   1 
ATOM   8202  O  O   . ALA H  1 60  ? 60.391  108.145 19.453  1.00 11.70 ? 60  ALA H O   1 
ATOM   8203  C  CB  . ALA H  1 60  ? 57.516  108.757 20.341  1.00 11.29 ? 60  ALA H CB  1 
ATOM   8204  N  N   . GLY H  1 61  ? 59.194  107.318 17.740  1.00 12.16 ? 61  GLY H N   1 
ATOM   8205  C  CA  . GLY H  1 61  ? 60.173  106.311 17.370  1.00 10.23 ? 61  GLY H CA  1 
ATOM   8206  C  C   . GLY H  1 61  ? 60.181  105.150 18.356  1.00 14.87 ? 61  GLY H C   1 
ATOM   8207  O  O   . GLY H  1 61  ? 59.237  104.973 19.126  1.00 12.32 ? 61  GLY H O   1 
ATOM   8208  N  N   . PRO H  1 62  ? 61.250  104.342 18.345  1.00 11.64 ? 62  PRO H N   1 
ATOM   8209  C  CA  . PRO H  1 62  ? 61.233  103.160 19.203  1.00 13.28 ? 62  PRO H CA  1 
ATOM   8210  C  C   . PRO H  1 62  ? 61.797  103.482 20.591  1.00 14.78 ? 62  PRO H C   1 
ATOM   8211  O  O   . PRO H  1 62  ? 62.038  104.662 20.901  1.00 12.45 ? 62  PRO H O   1 
ATOM   8212  C  CB  . PRO H  1 62  ? 62.143  102.189 18.454  1.00 15.18 ? 62  PRO H CB  1 
ATOM   8213  C  CG  . PRO H  1 62  ? 63.151  103.065 17.819  1.00 15.24 ? 62  PRO H CG  1 
ATOM   8214  C  CD  . PRO H  1 62  ? 62.367  104.303 17.381  1.00 15.92 ? 62  PRO H CD  1 
ATOM   8215  N  N   . HIS H  1 63  ? 62.004  102.453 21.412  1.00 12.11 ? 63  HIS H N   1 
ATOM   8216  C  CA  . HIS H  1 63  ? 62.551  102.670 22.740  1.00 14.01 ? 63  HIS H CA  1 
ATOM   8217  C  C   . HIS H  1 63  ? 63.940  103.278 22.615  1.00 13.46 ? 63  HIS H C   1 
ATOM   8218  O  O   . HIS H  1 63  ? 64.697  102.912 21.733  1.00 14.81 ? 63  HIS H O   1 
ATOM   8219  C  CB  . HIS H  1 63  ? 62.611  101.362 23.516  1.00 14.26 ? 63  HIS H CB  1 
ATOM   8220  C  CG  . HIS H  1 63  ? 61.279  100.711 23.686  1.00 16.62 ? 63  HIS H CG  1 
ATOM   8221  N  ND1 . HIS H  1 63  ? 61.120  99.492  24.309  1.00 16.52 ? 63  HIS H ND1 1 
ATOM   8222  C  CD2 . HIS H  1 63  ? 60.035  101.124 23.340  1.00 16.11 ? 63  HIS H CD2 1 
ATOM   8223  C  CE1 . HIS H  1 63  ? 59.838  99.171  24.318  1.00 17.96 ? 63  HIS H CE1 1 
ATOM   8224  N  NE2 . HIS H  1 63  ? 59.159  100.147 23.740  1.00 16.77 ? 63  HIS H NE2 1 
ATOM   8225  N  N   . PHE H  1 64  ? 64.236  104.240 23.476  1.00 13.34 ? 64  PHE H N   1 
ATOM   8226  C  CA  . PHE H  1 64  ? 65.533  104.870 23.515  1.00 13.89 ? 64  PHE H CA  1 
ATOM   8227  C  C   . PHE H  1 64  ? 66.546  103.765 23.746  1.00 14.63 ? 64  PHE H C   1 
ATOM   8228  O  O   . PHE H  1 64  ? 66.525  103.099 24.786  1.00 13.77 ? 64  PHE H O   1 
ATOM   8229  C  CB  . PHE H  1 64  ? 65.559  105.860 24.665  1.00 13.86 ? 64  PHE H CB  1 
ATOM   8230  C  CG  . PHE H  1 64  ? 66.853  106.618 24.802  1.00 15.45 ? 64  PHE H CG  1 
ATOM   8231  C  CD1 . PHE H  1 64  ? 67.581  106.999 23.675  1.00 16.66 ? 64  PHE H CD1 1 
ATOM   8232  C  CD2 . PHE H  1 64  ? 67.310  106.998 26.058  1.00 11.77 ? 64  PHE H CD2 1 
ATOM   8233  C  CE1 . PHE H  1 64  ? 68.757  107.700 23.795  1.00 13.44 ? 64  PHE H CE1 1 
ATOM   8234  C  CE2 . PHE H  1 64  ? 68.470  107.715 26.190  1.00 14.80 ? 64  PHE H CE2 1 
ATOM   8235  C  CZ  . PHE H  1 64  ? 69.208  108.064 25.056  1.00 19.31 ? 64  PHE H CZ  1 
ATOM   8236  N  N   . ASN H  1 65  ? 67.405  103.551 22.757  1.00 15.73 ? 65  ASN H N   1 
ATOM   8237  C  CA  . ASN H  1 65  ? 68.309  102.406 22.752  1.00 18.06 ? 65  ASN H CA  1 
ATOM   8238  C  C   . ASN H  1 65  ? 69.722  102.723 22.245  1.00 15.27 ? 65  ASN H C   1 
ATOM   8239  O  O   . ASN H  1 65  ? 70.175  102.127 21.287  1.00 18.01 ? 65  ASN H O   1 
ATOM   8240  C  CB  . ASN H  1 65  ? 67.707  101.271 21.919  1.00 15.23 ? 65  ASN H CB  1 
ATOM   8241  C  CG  . ASN H  1 65  ? 68.479  99.983  22.073  1.00 18.01 ? 65  ASN H CG  1 
ATOM   8242  O  OD1 . ASN H  1 65  ? 69.273  99.854  22.999  1.00 18.16 ? 65  ASN H OD1 1 
ATOM   8243  N  ND2 . ASN H  1 65  ? 68.254  99.025  21.176  1.00 16.57 ? 65  ASN H ND2 1 
ATOM   8244  N  N   . PRO H  1 66  ? 70.432  103.644 22.908  1.00 16.05 ? 66  PRO H N   1 
ATOM   8245  C  CA  . PRO H  1 66  ? 71.708  104.102 22.351  1.00 21.12 ? 66  PRO H CA  1 
ATOM   8246  C  C   . PRO H  1 66  ? 72.802  103.029 22.397  1.00 24.99 ? 66  PRO H C   1 
ATOM   8247  O  O   . PRO H  1 66  ? 73.845  103.233 21.791  1.00 25.37 ? 66  PRO H O   1 
ATOM   8248  C  CB  . PRO H  1 66  ? 72.081  105.272 23.269  1.00 15.54 ? 66  PRO H CB  1 
ATOM   8249  C  CG  . PRO H  1 66  ? 71.469  104.897 24.580  1.00 16.21 ? 66  PRO H CG  1 
ATOM   8250  C  CD  . PRO H  1 66  ? 70.177  104.209 24.242  1.00 14.35 ? 66  PRO H CD  1 
ATOM   8251  N  N   . LEU H  1 67  ? 72.579  101.923 23.110  1.00 24.07 ? 67  LEU H N   1 
ATOM   8252  C  CA  . LEU H  1 67  ? 73.591  100.865 23.194  1.00 21.95 ? 67  LEU H CA  1 
ATOM   8253  C  C   . LEU H  1 67  ? 73.204  99.657  22.341  1.00 23.66 ? 67  LEU H C   1 
ATOM   8254  O  O   . LEU H  1 67  ? 73.775  98.575  22.479  1.00 22.82 ? 67  LEU H O   1 
ATOM   8255  C  CB  . LEU H  1 67  ? 73.849  100.456 24.651  1.00 21.33 ? 67  LEU H CB  1 
ATOM   8256  C  CG  . LEU H  1 67  ? 74.531  101.532 25.497  1.00 25.79 ? 67  LEU H CG  1 
ATOM   8257  C  CD1 . LEU H  1 67  ? 74.610  101.111 26.965  1.00 28.55 ? 67  LEU H CD1 1 
ATOM   8258  C  CD2 . LEU H  1 67  ? 75.932  101.878 24.959  1.00 19.46 ? 67  LEU H CD2 1 
ATOM   8259  N  N   . SER H  1 68  ? 72.236  99.858  21.452  1.00 16.38 ? 68  SER H N   1 
ATOM   8260  C  CA  . SER H  1 68  ? 71.782  98.801  20.554  1.00 21.12 ? 68  SER H CA  1 
ATOM   8261  C  C   . SER H  1 68  ? 71.553  97.445  21.234  1.00 23.68 ? 68  SER H C   1 
ATOM   8262  O  O   . SER H  1 68  ? 71.974  96.405  20.722  1.00 24.19 ? 68  SER H O   1 
ATOM   8263  C  CB  . SER H  1 68  ? 72.762  98.649  19.370  1.00 21.59 ? 68  SER H CB  1 
ATOM   8264  O  OG  . SER H  1 68  ? 72.997  99.915  18.766  1.00 20.41 ? 68  SER H OG  1 
ATOM   8265  N  N   . ARG H  1 69  ? 70.876  97.446  22.382  1.00 20.58 ? 69  ARG H N   1 
ATOM   8266  C  CA  . ARG H  1 69  ? 70.646  96.201  23.091  1.00 18.85 ? 69  ARG H CA  1 
ATOM   8267  C  C   . ARG H  1 69  ? 69.279  95.663  22.729  1.00 19.56 ? 69  ARG H C   1 
ATOM   8268  O  O   . ARG H  1 69  ? 68.548  96.287  21.967  1.00 17.82 ? 69  ARG H O   1 
ATOM   8269  C  CB  . ARG H  1 69  ? 70.750  96.412  24.599  1.00 20.24 ? 69  ARG H CB  1 
ATOM   8270  C  CG  . ARG H  1 69  ? 72.043  97.083  25.072  1.00 23.09 ? 69  ARG H CG  1 
ATOM   8271  C  CD  . ARG H  1 69  ? 73.275  96.203  24.868  1.00 29.11 ? 69  ARG H CD  1 
ATOM   8272  N  NE  . ARG H  1 69  ? 74.444  96.692  25.618  1.00 32.88 ? 69  ARG H NE  1 
ATOM   8273  C  CZ  . ARG H  1 69  ? 75.668  96.843  25.097  1.00 35.19 ? 69  ARG H CZ  1 
ATOM   8274  N  NH1 . ARG H  1 69  ? 75.895  96.543  23.823  1.00 25.64 ? 69  ARG H NH1 1 
ATOM   8275  N  NH2 . ARG H  1 69  ? 76.676  97.293  25.842  1.00 32.87 ? 69  ARG H NH2 1 
ATOM   8276  N  N   . LYS H  1 70  ? 68.943  94.499  23.273  1.00 19.94 ? 70  LYS H N   1 
ATOM   8277  C  CA  . LYS H  1 70  ? 67.595  93.959  23.171  1.00 22.64 ? 70  LYS H CA  1 
ATOM   8278  C  C   . LYS H  1 70  ? 66.721  94.469  24.335  1.00 17.58 ? 70  LYS H C   1 
ATOM   8279  O  O   . LYS H  1 70  ? 67.226  94.876  25.388  1.00 14.71 ? 70  LYS H O   1 
ATOM   8280  C  CB  . LYS H  1 70  ? 67.635  92.429  23.191  1.00 25.63 ? 70  LYS H CB  1 
ATOM   8281  C  CG  . LYS H  1 70  ? 68.250  91.782  21.943  1.00 28.79 ? 70  LYS H CG  1 
ATOM   8282  C  CD  . LYS H  1 70  ? 68.581  90.321  22.222  1.00 33.63 ? 70  LYS H CD  1 
ATOM   8283  C  CE  . LYS H  1 70  ? 68.799  89.532  20.934  1.00 47.02 ? 70  LYS H CE  1 
ATOM   8284  N  NZ  . LYS H  1 70  ? 69.266  88.132  21.202  1.00 50.64 ? 70  LYS H NZ  1 
ATOM   8285  N  N   . HIS H  1 71  ? 65.416  94.424  24.128  1.00 14.76 ? 71  HIS H N   1 
ATOM   8286  C  CA  . HIS H  1 71  ? 64.438  94.890  25.112  1.00 17.23 ? 71  HIS H CA  1 
ATOM   8287  C  C   . HIS H  1 71  ? 64.401  94.017  26.361  1.00 12.25 ? 71  HIS H C   1 
ATOM   8288  O  O   . HIS H  1 71  ? 64.364  92.798  26.258  1.00 15.22 ? 71  HIS H O   1 
ATOM   8289  C  CB  . HIS H  1 71  ? 63.037  94.897  24.493  1.00 12.15 ? 71  HIS H CB  1 
ATOM   8290  C  CG  . HIS H  1 71  ? 61.971  95.292  25.458  1.00 15.22 ? 71  HIS H CG  1 
ATOM   8291  N  ND1 . HIS H  1 71  ? 61.761  96.602  25.828  1.00 17.03 ? 71  HIS H ND1 1 
ATOM   8292  C  CD2 . HIS H  1 71  ? 61.084  94.550  26.166  1.00 13.88 ? 71  HIS H CD2 1 
ATOM   8293  C  CE1 . HIS H  1 71  ? 60.786  96.652  26.721  1.00 12.55 ? 71  HIS H CE1 1 
ATOM   8294  N  NE2 . HIS H  1 71  ? 60.347  95.423  26.928  1.00 12.78 ? 71  HIS H NE2 1 
ATOM   8295  N  N   . GLY H  1 72  ? 64.401  94.639  27.537  1.00 15.81 ? 72  GLY H N   1 
ATOM   8296  C  CA  . GLY H  1 72  ? 64.283  93.897  28.787  1.00 14.66 ? 72  GLY H CA  1 
ATOM   8297  C  C   . GLY H  1 72  ? 63.497  94.647  29.846  1.00 16.47 ? 72  GLY H C   1 
ATOM   8298  O  O   . GLY H  1 72  ? 62.887  95.679  29.571  1.00 16.55 ? 72  GLY H O   1 
ATOM   8299  N  N   . GLY H  1 73  ? 63.497  94.118  31.065  1.00 12.50 ? 73  GLY H N   1 
ATOM   8300  C  CA  . GLY H  1 73  ? 62.940  94.821  32.191  1.00 10.80 ? 73  GLY H CA  1 
ATOM   8301  C  C   . GLY H  1 73  ? 64.004  95.729  32.791  1.00 16.00 ? 73  GLY H C   1 
ATOM   8302  O  O   . GLY H  1 73  ? 65.180  95.584  32.505  1.00 15.16 ? 73  GLY H O   1 
ATOM   8303  N  N   . PRO H  1 74  ? 63.598  96.668  33.647  1.00 11.69 ? 74  PRO H N   1 
ATOM   8304  C  CA  . PRO H  1 74  ? 64.599  97.578  34.192  1.00 13.56 ? 74  PRO H CA  1 
ATOM   8305  C  C   . PRO H  1 74  ? 65.661  96.900  35.079  1.00 19.99 ? 74  PRO H C   1 
ATOM   8306  O  O   . PRO H  1 74  ? 66.739  97.473  35.256  1.00 18.02 ? 74  PRO H O   1 
ATOM   8307  C  CB  . PRO H  1 74  ? 63.771  98.593  34.989  1.00 11.23 ? 74  PRO H CB  1 
ATOM   8308  C  CG  . PRO H  1 74  ? 62.441  97.946  35.208  1.00 13.71 ? 74  PRO H CG  1 
ATOM   8309  C  CD  . PRO H  1 74  ? 62.226  97.054  34.004  1.00 11.79 ? 74  PRO H CD  1 
ATOM   8310  N  N   . LYS H  1 75  ? 65.380  95.711  35.607  1.00 17.75 ? 75  LYS H N   1 
ATOM   8311  C  CA  . LYS H  1 75  ? 66.361  95.031  36.442  1.00 18.28 ? 75  LYS H CA  1 
ATOM   8312  C  C   . LYS H  1 75  ? 67.371  94.185  35.643  1.00 20.89 ? 75  LYS H C   1 
ATOM   8313  O  O   . LYS H  1 75  ? 68.387  93.766  36.182  1.00 23.96 ? 75  LYS H O   1 
ATOM   8314  C  CB  . LYS H  1 75  ? 65.660  94.207  37.528  1.00 21.37 ? 75  LYS H CB  1 
ATOM   8315  C  CG  . LYS H  1 75  ? 64.650  95.034  38.333  1.00 18.96 ? 75  LYS H CG  1 
ATOM   8316  C  CD  . LYS H  1 75  ? 64.227  94.365  39.634  1.00 30.31 ? 75  LYS H CD  1 
ATOM   8317  C  CE  . LYS H  1 75  ? 63.566  93.015  39.435  1.00 30.04 ? 75  LYS H CE  1 
ATOM   8318  N  NZ  . LYS H  1 75  ? 63.362  92.353  40.781  1.00 27.87 ? 75  LYS H NZ  1 
ATOM   8319  N  N   . ASP H  1 76  ? 67.104  93.956  34.360  1.00 20.72 ? 76  ASP H N   1 
ATOM   8320  C  CA  . ASP H  1 76  ? 68.029  93.202  33.518  1.00 17.96 ? 76  ASP H CA  1 
ATOM   8321  C  C   . ASP H  1 76  ? 69.188  94.073  33.063  1.00 22.86 ? 76  ASP H C   1 
ATOM   8322  O  O   . ASP H  1 76  ? 69.042  95.288  32.833  1.00 19.20 ? 76  ASP H O   1 
ATOM   8323  C  CB  . ASP H  1 76  ? 67.351  92.647  32.263  1.00 16.15 ? 76  ASP H CB  1 
ATOM   8324  C  CG  . ASP H  1 76  ? 66.143  91.744  32.568  1.00 21.95 ? 76  ASP H CG  1 
ATOM   8325  O  OD1 . ASP H  1 76  ? 66.229  90.864  33.448  1.00 20.10 ? 76  ASP H OD1 1 
ATOM   8326  O  OD2 . ASP H  1 76  ? 65.102  91.909  31.896  1.00 15.32 ? 76  ASP H OD2 1 
ATOM   8327  N  N   . GLU H  1 77  ? 70.345  93.439  32.908  1.00 19.90 ? 77  GLU H N   1 
ATOM   8328  C  CA  . GLU H  1 77  ? 71.484  94.115  32.303  1.00 23.36 ? 77  GLU H CA  1 
ATOM   8329  C  C   . GLU H  1 77  ? 71.242  94.362  30.815  1.00 18.13 ? 77  GLU H C   1 
ATOM   8330  O  O   . GLU H  1 77  ? 71.529  95.443  30.303  1.00 18.60 ? 77  GLU H O   1 
ATOM   8331  C  CB  . GLU H  1 77  ? 72.766  93.311  32.496  1.00 25.83 ? 77  GLU H CB  1 
ATOM   8332  C  CG  . GLU H  1 77  ? 73.890  93.791  31.611  1.00 25.90 ? 77  GLU H CG  1 
ATOM   8333  C  CD  . GLU H  1 77  ? 75.217  93.223  32.031  1.00 45.26 ? 77  GLU H CD  1 
ATOM   8334  O  OE1 . GLU H  1 77  ? 75.420  92.001  31.851  1.00 44.85 ? 77  GLU H OE1 1 
ATOM   8335  O  OE2 . GLU H  1 77  ? 76.048  93.999  32.556  1.00 58.98 ? 77  GLU H OE2 1 
ATOM   8336  N  N   . GLU H  1 78  ? 70.718  93.352  30.132  1.00 15.72 ? 78  GLU H N   1 
ATOM   8337  C  CA  . GLU H  1 78  ? 70.337  93.493  28.738  1.00 18.33 ? 78  GLU H CA  1 
ATOM   8338  C  C   . GLU H  1 78  ? 68.984  94.196  28.612  1.00 18.16 ? 78  GLU H C   1 
ATOM   8339  O  O   . GLU H  1 78  ? 67.938  93.570  28.710  1.00 14.83 ? 78  GLU H O   1 
ATOM   8340  C  CB  . GLU H  1 78  ? 70.268  92.124  28.058  1.00 13.54 ? 78  GLU H CB  1 
ATOM   8341  C  CG  . GLU H  1 78  ? 69.866  92.195  26.591  1.00 19.61 ? 78  GLU H CG  1 
ATOM   8342  C  CD  . GLU H  1 78  ? 71.029  92.582  25.677  1.00 26.15 ? 78  GLU H CD  1 
ATOM   8343  O  OE1 . GLU H  1 78  ? 72.144  92.887  26.191  1.00 23.89 ? 78  GLU H OE1 1 
ATOM   8344  O  OE2 . GLU H  1 78  ? 70.821  92.563  24.444  1.00 24.30 ? 78  GLU H OE2 1 
ATOM   8345  N  N   . ARG H  1 79  ? 69.017  95.505  28.404  1.00 18.03 ? 79  ARG H N   1 
ATOM   8346  C  CA  . ARG H  1 79  ? 67.792  96.272  28.255  1.00 18.19 ? 79  ARG H CA  1 
ATOM   8347  C  C   . ARG H  1 79  ? 68.090  97.507  27.428  1.00 19.07 ? 79  ARG H C   1 
ATOM   8348  O  O   . ARG H  1 79  ? 69.251  97.915  27.293  1.00 15.00 ? 79  ARG H O   1 
ATOM   8349  C  CB  . ARG H  1 79  ? 67.262  96.708  29.620  1.00 13.52 ? 79  ARG H CB  1 
ATOM   8350  C  CG  . ARG H  1 79  ? 68.284  97.484  30.465  1.00 14.06 ? 79  ARG H CG  1 
ATOM   8351  C  CD  . ARG H  1 79  ? 67.644  98.148  31.686  1.00 13.05 ? 79  ARG H CD  1 
ATOM   8352  N  NE  . ARG H  1 79  ? 67.107  99.477  31.391  1.00 13.04 ? 79  ARG H NE  1 
ATOM   8353  C  CZ  . ARG H  1 79  ? 66.789  100.377 32.315  1.00 13.38 ? 79  ARG H CZ  1 
ATOM   8354  N  NH1 . ARG H  1 79  ? 66.935  100.088 33.610  1.00 11.32 ? 79  ARG H NH1 1 
ATOM   8355  N  NH2 . ARG H  1 79  ? 66.334  101.575 31.949  1.00 10.22 ? 79  ARG H NH2 1 
ATOM   8356  N  N   . HIS H  1 80  ? 67.044  98.108  26.878  1.00 16.53 ? 80  HIS H N   1 
ATOM   8357  C  CA  . HIS H  1 80  ? 67.195  99.441  26.306  1.00 16.19 ? 80  HIS H CA  1 
ATOM   8358  C  C   . HIS H  1 80  ? 67.334  100.430 27.447  1.00 14.63 ? 80  HIS H C   1 
ATOM   8359  O  O   . HIS H  1 80  ? 66.815  100.183 28.549  1.00 14.86 ? 80  HIS H O   1 
ATOM   8360  C  CB  . HIS H  1 80  ? 65.952  99.804  25.503  1.00 14.21 ? 80  HIS H CB  1 
ATOM   8361  C  CG  . HIS H  1 80  ? 65.629  98.841  24.413  1.00 12.97 ? 80  HIS H CG  1 
ATOM   8362  N  ND1 . HIS H  1 80  ? 64.334  98.527  24.063  1.00 13.30 ? 80  HIS H ND1 1 
ATOM   8363  C  CD2 . HIS H  1 80  ? 66.428  98.161  23.557  1.00 12.68 ? 80  HIS H CD2 1 
ATOM   8364  C  CE1 . HIS H  1 80  ? 64.348  97.674  23.051  1.00 12.86 ? 80  HIS H CE1 1 
ATOM   8365  N  NE2 . HIS H  1 80  ? 65.608  97.444  22.719  1.00 13.00 ? 80  HIS H NE2 1 
ATOM   8366  N  N   . VAL H  1 81  ? 67.997  101.561 27.216  1.00 12.80 ? 81  VAL H N   1 
ATOM   8367  C  CA  . VAL H  1 81  ? 67.991  102.594 28.256  1.00 12.98 ? 81  VAL H CA  1 
ATOM   8368  C  C   . VAL H  1 81  ? 66.545  102.958 28.650  1.00 13.33 ? 81  VAL H C   1 
ATOM   8369  O  O   . VAL H  1 81  ? 66.218  103.104 29.835  1.00 11.52 ? 81  VAL H O   1 
ATOM   8370  C  CB  . VAL H  1 81  ? 68.770  103.855 27.834  1.00 15.77 ? 81  VAL H CB  1 
ATOM   8371  C  CG1 . VAL H  1 81  ? 68.474  105.031 28.788  1.00 11.17 ? 81  VAL H CG1 1 
ATOM   8372  C  CG2 . VAL H  1 81  ? 70.298  103.562 27.774  1.00 17.85 ? 81  VAL H CG2 1 
ATOM   8373  N  N   . GLY H  1 82  ? 65.680  103.085 27.655  1.00 12.36 ? 82  GLY H N   1 
ATOM   8374  C  CA  . GLY H  1 82  ? 64.313  103.508 27.901  1.00 12.26 ? 82  GLY H CA  1 
ATOM   8375  C  C   . GLY H  1 82  ? 63.369  102.478 28.516  1.00 12.07 ? 82  GLY H C   1 
ATOM   8376  O  O   . GLY H  1 82  ? 62.179  102.759 28.646  1.00 12.28 ? 82  GLY H O   1 
ATOM   8377  N  N   . ASP H  1 83  ? 63.878  101.306 28.907  1.00 10.38 ? 83  ASP H N   1 
ATOM   8378  C  CA  . ASP H  1 83  ? 63.025  100.226 29.403  1.00 10.12 ? 83  ASP H CA  1 
ATOM   8379  C  C   . ASP H  1 83  ? 62.714  100.357 30.903  1.00 11.94 ? 83  ASP H C   1 
ATOM   8380  O  O   . ASP H  1 83  ? 63.428  99.812  31.740  1.00 11.29 ? 83  ASP H O   1 
ATOM   8381  C  CB  . ASP H  1 83  ? 63.631  98.849  29.096  1.00 10.41 ? 83  ASP H CB  1 
ATOM   8382  C  CG  . ASP H  1 83  ? 63.515  98.465  27.630  1.00 13.49 ? 83  ASP H CG  1 
ATOM   8383  O  OD1 . ASP H  1 83  ? 62.766  99.148  26.891  1.00 11.19 ? 83  ASP H OD1 1 
ATOM   8384  O  OD2 . ASP H  1 83  ? 64.176  97.476  27.212  1.00 15.64 ? 83  ASP H OD2 1 
ATOM   8385  N  N   . LEU H  1 84  ? 61.660  101.091 31.251  1.00 9.39  ? 84  LEU H N   1 
ATOM   8386  C  CA  . LEU H  1 84  ? 61.356  101.288 32.672  1.00 10.29 ? 84  LEU H CA  1 
ATOM   8387  C  C   . LEU H  1 84  ? 60.318  100.317 33.212  1.00 8.82  ? 84  LEU H C   1 
ATOM   8388  O  O   . LEU H  1 84  ? 59.832  100.483 34.319  1.00 11.40 ? 84  LEU H O   1 
ATOM   8389  C  CB  . LEU H  1 84  ? 60.943  102.722 32.970  1.00 8.80  ? 84  LEU H CB  1 
ATOM   8390  C  CG  . LEU H  1 84  ? 62.021  103.747 32.664  1.00 11.19 ? 84  LEU H CG  1 
ATOM   8391  C  CD1 . LEU H  1 84  ? 61.471  105.168 32.817  1.00 12.05 ? 84  LEU H CD1 1 
ATOM   8392  C  CD2 . LEU H  1 84  ? 63.227  103.543 33.604  1.00 12.90 ? 84  LEU H CD2 1 
ATOM   8393  N  N   . GLY H  1 85  ? 59.985  99.302  32.433  1.00 8.51  ? 85  GLY H N   1 
ATOM   8394  C  CA  . GLY H  1 85  ? 59.124  98.230  32.902  1.00 10.37 ? 85  GLY H CA  1 
ATOM   8395  C  C   . GLY H  1 85  ? 57.632  98.528  32.832  1.00 10.85 ? 85  GLY H C   1 
ATOM   8396  O  O   . GLY H  1 85  ? 57.115  98.959  31.799  1.00 10.45 ? 85  GLY H O   1 
ATOM   8397  N  N   . ASN H  1 86  ? 56.931  98.276  33.930  1.00 12.12 ? 86  ASN H N   1 
ATOM   8398  C  CA  . ASN H  1 86  ? 55.495  98.527  33.992  1.00 10.27 ? 86  ASN H CA  1 
ATOM   8399  C  C   . ASN H  1 86  ? 55.142  99.505  35.089  1.00 9.58  ? 86  ASN H C   1 
ATOM   8400  O  O   . ASN H  1 86  ? 55.884  99.675  36.045  1.00 10.07 ? 86  ASN H O   1 
ATOM   8401  C  CB  . ASN H  1 86  ? 54.736  97.223  34.243  1.00 9.50  ? 86  ASN H CB  1 
ATOM   8402  C  CG  . ASN H  1 86  ? 54.706  96.342  33.034  1.00 11.38 ? 86  ASN H CG  1 
ATOM   8403  O  OD1 . ASN H  1 86  ? 54.224  96.747  31.965  1.00 9.35  ? 86  ASN H OD1 1 
ATOM   8404  N  ND2 . ASN H  1 86  ? 55.229  95.128  33.175  1.00 10.11 ? 86  ASN H ND2 1 
ATOM   8405  N  N   . VAL H  1 87  ? 53.981  100.137 34.946  1.00 11.73 ? 87  VAL H N   1 
ATOM   8406  C  CA  . VAL H  1 87  ? 53.363  100.833 36.050  1.00 8.95  ? 87  VAL H CA  1 
ATOM   8407  C  C   . VAL H  1 87  ? 52.005  100.183 36.273  1.00 8.02  ? 87  VAL H C   1 
ATOM   8408  O  O   . VAL H  1 87  ? 51.475  99.541  35.381  1.00 10.26 ? 87  VAL H O   1 
ATOM   8409  C  CB  . VAL H  1 87  ? 53.247  102.349 35.800  1.00 10.67 ? 87  VAL H CB  1 
ATOM   8410  C  CG1 . VAL H  1 87  ? 54.662  102.975 35.644  1.00 5.11  ? 87  VAL H CG1 1 
ATOM   8411  C  CG2 . VAL H  1 87  ? 52.351  102.623 34.574  1.00 7.26  ? 87  VAL H CG2 1 
ATOM   8412  N  N   . THR H  1 88  ? 51.460  100.327 37.474  1.00 7.78  ? 88  THR H N   1 
ATOM   8413  C  CA  . THR H  1 88  ? 50.259  99.600  37.849  1.00 8.47  ? 88  THR H CA  1 
ATOM   8414  C  C   . THR H  1 88  ? 49.163  100.579 38.197  1.00 7.71  ? 88  THR H C   1 
ATOM   8415  O  O   . THR H  1 88  ? 49.322  101.418 39.082  1.00 8.11  ? 88  THR H O   1 
ATOM   8416  C  CB  . THR H  1 88  ? 50.499  98.675  39.069  1.00 7.65  ? 88  THR H CB  1 
ATOM   8417  O  OG1 . THR H  1 88  ? 51.405  97.631  38.703  1.00 9.16  ? 88  THR H OG1 1 
ATOM   8418  C  CG2 . THR H  1 88  ? 49.184  98.034  39.509  1.00 10.70 ? 88  THR H CG2 1 
ATOM   8419  N  N   . ALA H  1 89  ? 48.053  100.483 37.487  1.00 5.45  ? 89  ALA H N   1 
ATOM   8420  C  CA  . ALA H  1 89  ? 46.900  101.309 37.810  1.00 9.44  ? 89  ALA H CA  1 
ATOM   8421  C  C   . ALA H  1 89  ? 46.023  100.566 38.837  1.00 8.55  ? 89  ALA H C   1 
ATOM   8422  O  O   . ALA H  1 89  ? 45.837  99.356  38.747  1.00 7.70  ? 89  ALA H O   1 
ATOM   8423  C  CB  . ALA H  1 89  ? 46.103  101.637 36.550  1.00 5.84  ? 89  ALA H CB  1 
ATOM   8424  N  N   . ASP H  1 90  ? 45.487  101.297 39.806  1.00 9.87  ? 90  ASP H N   1 
ATOM   8425  C  CA  . ASP H  1 90  ? 44.630  100.688 40.833  1.00 12.98 ? 90  ASP H CA  1 
ATOM   8426  C  C   . ASP H  1 90  ? 43.181  100.579 40.333  1.00 14.46 ? 90  ASP H C   1 
ATOM   8427  O  O   . ASP H  1 90  ? 42.897  100.883 39.174  1.00 12.82 ? 90  ASP H O   1 
ATOM   8428  C  CB  . ASP H  1 90  ? 44.693  101.515 42.115  1.00 9.23  ? 90  ASP H CB  1 
ATOM   8429  C  CG  . ASP H  1 90  ? 44.159  102.946 41.925  1.00 11.76 ? 90  ASP H CG  1 
ATOM   8430  O  OD1 . ASP H  1 90  ? 43.363  103.207 40.993  1.00 11.04 ? 90  ASP H OD1 1 
ATOM   8431  O  OD2 . ASP H  1 90  ? 44.532  103.826 42.717  1.00 11.76 ? 90  ASP H OD2 1 
ATOM   8432  N  N   . LYS H  1 91  ? 42.264  100.210 41.223  1.00 12.79 ? 91  LYS H N   1 
ATOM   8433  C  CA  . LYS H  1 91  ? 40.876  99.965  40.845  1.00 15.51 ? 91  LYS H CA  1 
ATOM   8434  C  C   . LYS H  1 91  ? 40.155  101.217 40.342  1.00 12.90 ? 91  LYS H C   1 
ATOM   8435  O  O   . LYS H  1 91  ? 39.118  101.108 39.714  1.00 14.77 ? 91  LYS H O   1 
ATOM   8436  C  CB  . LYS H  1 91  ? 40.099  99.359  42.021  1.00 18.72 ? 91  LYS H CB  1 
ATOM   8437  C  CG  . LYS H  1 91  ? 40.042  100.288 43.217  1.00 16.27 ? 91  LYS H CG  1 
ATOM   8438  C  CD  . LYS H  1 91  ? 39.214  99.719  44.367  1.00 22.14 ? 91  LYS H CD  1 
ATOM   8439  C  CE  . LYS H  1 91  ? 38.859  100.820 45.360  1.00 22.25 ? 91  LYS H CE  1 
ATOM   8440  N  NZ  . LYS H  1 91  ? 38.006  100.317 46.483  1.00 36.05 ? 91  LYS H NZ  1 
ATOM   8441  N  N   . ASP H  1 92  ? 40.693  102.400 40.618  1.00 11.76 ? 92  ASP H N   1 
ATOM   8442  C  CA  . ASP H  1 92  ? 40.106  103.642 40.104  1.00 13.74 ? 92  ASP H CA  1 
ATOM   8443  C  C   . ASP H  1 92  ? 40.737  104.078 38.771  1.00 14.10 ? 92  ASP H C   1 
ATOM   8444  O  O   . ASP H  1 92  ? 40.350  105.094 38.190  1.00 14.89 ? 92  ASP H O   1 
ATOM   8445  C  CB  . ASP H  1 92  ? 40.234  104.771 41.124  1.00 12.89 ? 92  ASP H CB  1 
ATOM   8446  C  CG  . ASP H  1 92  ? 39.591  104.425 42.455  1.00 17.38 ? 92  ASP H CG  1 
ATOM   8447  O  OD1 . ASP H  1 92  ? 38.476  103.870 42.459  1.00 15.31 ? 92  ASP H OD1 1 
ATOM   8448  O  OD2 . ASP H  1 92  ? 40.211  104.691 43.500  1.00 18.51 ? 92  ASP H OD2 1 
ATOM   8449  N  N   . GLY H  1 93  ? 41.710  103.313 38.292  1.00 11.19 ? 93  GLY H N   1 
ATOM   8450  C  CA  . GLY H  1 93  ? 42.356  103.643 37.038  1.00 10.75 ? 93  GLY H CA  1 
ATOM   8451  C  C   . GLY H  1 93  ? 43.541  104.568 37.186  1.00 10.56 ? 93  GLY H C   1 
ATOM   8452  O  O   . GLY H  1 93  ? 44.040  105.144 36.194  1.00 11.83 ? 93  GLY H O   1 
ATOM   8453  N  N   . VAL H  1 94  ? 44.008  104.694 38.423  1.00 10.89 ? 94  VAL H N   1 
ATOM   8454  C  CA  . VAL H  1 94  ? 45.113  105.586 38.765  1.00 11.00 ? 94  VAL H CA  1 
ATOM   8455  C  C   . VAL H  1 94  ? 46.414  104.824 39.042  1.00 11.86 ? 94  VAL H C   1 
ATOM   8456  O  O   . VAL H  1 94  ? 46.447  103.887 39.865  1.00 8.09  ? 94  VAL H O   1 
ATOM   8457  C  CB  . VAL H  1 94  ? 44.772  106.439 39.980  1.00 13.45 ? 94  VAL H CB  1 
ATOM   8458  C  CG1 . VAL H  1 94  ? 45.972  107.305 40.367  1.00 14.72 ? 94  VAL H CG1 1 
ATOM   8459  C  CG2 . VAL H  1 94  ? 43.558  107.308 39.683  1.00 11.99 ? 94  VAL H CG2 1 
ATOM   8460  N  N   . ALA H  1 95  ? 47.473  105.195 38.320  1.00 10.61 ? 95  ALA H N   1 
ATOM   8461  C  CA  . ALA H  1 95  ? 48.795  104.611 38.583  1.00 10.64 ? 95  ALA H CA  1 
ATOM   8462  C  C   . ALA H  1 95  ? 49.633  105.609 39.370  1.00 11.13 ? 95  ALA H C   1 
ATOM   8463  O  O   . ALA H  1 95  ? 50.017  106.659 38.846  1.00 9.03  ? 95  ALA H O   1 
ATOM   8464  C  CB  . ALA H  1 95  ? 49.505  104.210 37.293  1.00 8.67  ? 95  ALA H CB  1 
ATOM   8465  N  N   . ASP H  1 96  ? 49.882  105.300 40.636  1.00 7.19  ? 96  ASP H N   1 
ATOM   8466  C  CA  . ASP H  1 96  ? 50.761  106.140 41.421  1.00 12.42 ? 96  ASP H CA  1 
ATOM   8467  C  C   . ASP H  1 96  ? 52.226  105.696 41.196  1.00 11.43 ? 96  ASP H C   1 
ATOM   8468  O  O   . ASP H  1 96  ? 52.797  104.922 41.965  1.00 12.99 ? 96  ASP H O   1 
ATOM   8469  C  CB  . ASP H  1 96  ? 50.356  106.128 42.900  1.00 12.25 ? 96  ASP H CB  1 
ATOM   8470  C  CG  . ASP H  1 96  ? 48.983  106.785 43.141  1.00 18.27 ? 96  ASP H CG  1 
ATOM   8471  O  OD1 . ASP H  1 96  ? 48.744  107.893 42.604  1.00 20.50 ? 96  ASP H OD1 1 
ATOM   8472  O  OD2 . ASP H  1 96  ? 48.141  106.185 43.852  1.00 15.90 ? 96  ASP H OD2 1 
ATOM   8473  N  N   . VAL H  1 97  ? 52.822  106.225 40.145  1.00 9.53  ? 97  VAL H N   1 
ATOM   8474  C  CA  . VAL H  1 97  ? 54.111  105.731 39.654  1.00 10.63 ? 97  VAL H CA  1 
ATOM   8475  C  C   . VAL H  1 97  ? 55.188  105.991 40.678  1.00 11.77 ? 97  VAL H C   1 
ATOM   8476  O  O   . VAL H  1 97  ? 55.244  107.067 41.269  1.00 13.51 ? 97  VAL H O   1 
ATOM   8477  C  CB  . VAL H  1 97  ? 54.478  106.378 38.305  1.00 9.46  ? 97  VAL H CB  1 
ATOM   8478  C  CG1 . VAL H  1 97  ? 55.852  105.891 37.817  1.00 11.32 ? 97  VAL H CG1 1 
ATOM   8479  C  CG2 . VAL H  1 97  ? 53.365  106.086 37.242  1.00 7.81  ? 97  VAL H CG2 1 
ATOM   8480  N  N   . SER H  1 98  ? 56.025  104.994 40.911  1.00 8.68  ? 98  SER H N   1 
ATOM   8481  C  CA  . SER H  1 98  ? 57.127  105.148 41.848  1.00 11.58 ? 98  SER H CA  1 
ATOM   8482  C  C   . SER H  1 98  ? 58.246  104.222 41.423  1.00 12.14 ? 98  SER H C   1 
ATOM   8483  O  O   . SER H  1 98  ? 58.230  103.016 41.715  1.00 13.49 ? 98  SER H O   1 
ATOM   8484  C  CB  . SER H  1 98  ? 56.676  104.776 43.261  1.00 11.96 ? 98  SER H CB  1 
ATOM   8485  O  OG  . SER H  1 98  ? 57.776  104.810 44.143  1.00 17.78 ? 98  SER H OG  1 
ATOM   8486  N  N   . ILE H  1 99  ? 59.206  104.780 40.708  1.00 10.92 ? 99  ILE H N   1 
ATOM   8487  C  CA  . ILE H  1 99  ? 60.279  103.986 40.124  1.00 13.50 ? 99  ILE H CA  1 
ATOM   8488  C  C   . ILE H  1 99  ? 61.621  104.629 40.439  1.00 14.78 ? 99  ILE H C   1 
ATOM   8489  O  O   . ILE H  1 99  ? 61.738  105.845 40.501  1.00 15.83 ? 99  ILE H O   1 
ATOM   8490  C  CB  . ILE H  1 99  ? 60.080  103.859 38.605  1.00 12.91 ? 99  ILE H CB  1 
ATOM   8491  C  CG1 . ILE H  1 99  ? 58.915  102.914 38.307  1.00 9.48  ? 99  ILE H CG1 1 
ATOM   8492  C  CG2 . ILE H  1 99  ? 61.325  103.369 37.901  1.00 9.63  ? 99  ILE H CG2 1 
ATOM   8493  C  CD1 . ILE H  1 99  ? 58.555  102.897 36.820  1.00 8.22  ? 99  ILE H CD1 1 
ATOM   8494  N  N   . GLU H  1 100 ? 62.638  103.815 40.666  1.00 17.78 ? 100 GLU H N   1 
ATOM   8495  C  CA  . GLU H  1 100 ? 63.976  104.358 40.780  1.00 16.27 ? 100 GLU H CA  1 
ATOM   8496  C  C   . GLU H  1 100 ? 64.833  103.617 39.790  1.00 12.94 ? 100 GLU H C   1 
ATOM   8497  O  O   . GLU H  1 100 ? 64.843  102.404 39.784  1.00 14.70 ? 100 GLU H O   1 
ATOM   8498  C  CB  . GLU H  1 100 ? 64.527  104.211 42.209  1.00 17.61 ? 100 GLU H CB  1 
ATOM   8499  C  CG  . GLU H  1 100 ? 65.906  104.861 42.365  1.00 21.76 ? 100 GLU H CG  1 
ATOM   8500  C  CD  . GLU H  1 100 ? 66.481  104.761 43.784  1.00 30.05 ? 100 GLU H CD  1 
ATOM   8501  O  OE1 . GLU H  1 100 ? 65.888  105.344 44.714  1.00 30.02 ? 100 GLU H OE1 1 
ATOM   8502  O  OE2 . GLU H  1 100 ? 67.533  104.102 43.960  1.00 34.98 ? 100 GLU H OE2 1 
ATOM   8503  N  N   . ASP H  1 101 ? 65.529  104.345 38.925  1.00 13.64 ? 101 ASP H N   1 
ATOM   8504  C  CA  . ASP H  1 101 ? 66.298  103.696 37.889  1.00 12.09 ? 101 ASP H CA  1 
ATOM   8505  C  C   . ASP H  1 101 ? 67.689  104.293 37.752  1.00 16.36 ? 101 ASP H C   1 
ATOM   8506  O  O   . ASP H  1 101 ? 67.894  105.507 37.853  1.00 19.01 ? 101 ASP H O   1 
ATOM   8507  C  CB  . ASP H  1 101 ? 65.567  103.737 36.539  1.00 13.14 ? 101 ASP H CB  1 
ATOM   8508  C  CG  . ASP H  1 101 ? 66.147  102.750 35.535  1.00 16.53 ? 101 ASP H CG  1 
ATOM   8509  O  OD1 . ASP H  1 101 ? 65.869  101.532 35.659  1.00 20.20 ? 101 ASP H OD1 1 
ATOM   8510  O  OD2 . ASP H  1 101 ? 66.887  103.188 34.623  1.00 14.29 ? 101 ASP H OD2 1 
ATOM   8511  N  N   . SER H  1 102 ? 68.652  103.430 37.493  1.00 15.14 ? 102 SER H N   1 
ATOM   8512  C  CA  . SER H  1 102 ? 70.019  103.891 37.347  1.00 15.45 ? 102 SER H CA  1 
ATOM   8513  C  C   . SER H  1 102 ? 70.574  103.743 35.942  1.00 16.16 ? 102 SER H C   1 
ATOM   8514  O  O   . SER H  1 102 ? 71.739  104.034 35.719  1.00 16.57 ? 102 SER H O   1 
ATOM   8515  C  CB  . SER H  1 102 ? 70.906  103.170 38.340  1.00 16.52 ? 102 SER H CB  1 
ATOM   8516  O  OG  . SER H  1 102 ? 70.742  103.770 39.607  1.00 22.92 ? 102 SER H OG  1 
ATOM   8517  N  N   . VAL H  1 103 ? 69.753  103.301 34.991  1.00 11.06 ? 103 VAL H N   1 
ATOM   8518  C  CA  . VAL H  1 103 ? 70.206  103.261 33.607  1.00 11.07 ? 103 VAL H CA  1 
ATOM   8519  C  C   . VAL H  1 103 ? 69.884  104.586 32.915  1.00 15.13 ? 103 VAL H C   1 
ATOM   8520  O  O   . VAL H  1 103 ? 70.732  105.134 32.220  1.00 15.22 ? 103 VAL H O   1 
ATOM   8521  C  CB  . VAL H  1 103 ? 69.631  102.044 32.846  1.00 12.71 ? 103 VAL H CB  1 
ATOM   8522  C  CG1 . VAL H  1 103 ? 70.017  102.073 31.405  1.00 13.18 ? 103 VAL H CG1 1 
ATOM   8523  C  CG2 . VAL H  1 103 ? 70.127  100.760 33.471  1.00 20.30 ? 103 VAL H CG2 1 
ATOM   8524  N  N   . ILE H  1 104 ? 68.673  105.119 33.116  1.00 12.03 ? 104 ILE H N   1 
ATOM   8525  C  CA  . ILE H  1 104 ? 68.323  106.422 32.540  1.00 13.68 ? 104 ILE H CA  1 
ATOM   8526  C  C   . ILE H  1 104 ? 69.100  107.512 33.230  1.00 10.33 ? 104 ILE H C   1 
ATOM   8527  O  O   . ILE H  1 104 ? 69.530  107.346 34.365  1.00 12.59 ? 104 ILE H O   1 
ATOM   8528  C  CB  . ILE H  1 104 ? 66.818  106.771 32.699  1.00 11.18 ? 104 ILE H CB  1 
ATOM   8529  C  CG1 . ILE H  1 104 ? 66.393  106.641 34.169  1.00 9.17  ? 104 ILE H CG1 1 
ATOM   8530  C  CG2 . ILE H  1 104 ? 65.975  105.889 31.785  1.00 9.99  ? 104 ILE H CG2 1 
ATOM   8531  C  CD1 . ILE H  1 104 ? 64.994  107.178 34.498  1.00 9.11  ? 104 ILE H CD1 1 
ATOM   8532  N  N   . SER H  1 105 ? 69.249  108.653 32.578  1.00 10.09 ? 105 SER H N   1 
ATOM   8533  C  CA  . SER H  1 105 ? 69.880  109.786 33.253  1.00 13.31 ? 105 SER H CA  1 
ATOM   8534  C  C   . SER H  1 105 ? 69.320  111.106 32.770  1.00 11.71 ? 105 SER H C   1 
ATOM   8535  O  O   . SER H  1 105 ? 68.710  111.163 31.714  1.00 14.06 ? 105 SER H O   1 
ATOM   8536  C  CB  . SER H  1 105 ? 71.401  109.773 33.036  1.00 12.68 ? 105 SER H CB  1 
ATOM   8537  O  OG  . SER H  1 105 ? 71.995  110.738 33.896  1.00 18.64 ? 105 SER H OG  1 
ATOM   8538  N  N   . LEU H  1 106 ? 69.522  112.161 33.547  1.00 15.11 ? 106 LEU H N   1 
ATOM   8539  C  CA  . LEU H  1 106 ? 69.104  113.490 33.130  1.00 14.45 ? 106 LEU H CA  1 
ATOM   8540  C  C   . LEU H  1 106 ? 70.277  114.310 32.574  1.00 19.50 ? 106 LEU H C   1 
ATOM   8541  O  O   . LEU H  1 106 ? 70.191  115.539 32.469  1.00 19.78 ? 106 LEU H O   1 
ATOM   8542  C  CB  . LEU H  1 106 ? 68.435  114.224 34.277  1.00 15.98 ? 106 LEU H CB  1 
ATOM   8543  C  CG  . LEU H  1 106 ? 67.262  113.488 34.937  1.00 16.32 ? 106 LEU H CG  1 
ATOM   8544  C  CD1 . LEU H  1 106 ? 66.603  114.382 35.956  1.00 15.85 ? 106 LEU H CD1 1 
ATOM   8545  C  CD2 . LEU H  1 106 ? 66.252  113.031 33.877  1.00 12.19 ? 106 LEU H CD2 1 
ATOM   8546  N  N   . SER H  1 107 ? 71.362  113.623 32.220  1.00 19.76 ? 107 SER H N   1 
ATOM   8547  C  CA  . SER H  1 107 ? 72.498  114.234 31.506  1.00 23.01 ? 107 SER H CA  1 
ATOM   8548  C  C   . SER H  1 107 ? 73.340  113.146 30.833  1.00 25.49 ? 107 SER H C   1 
ATOM   8549  O  O   . SER H  1 107 ? 73.115  111.953 31.066  1.00 20.73 ? 107 SER H O   1 
ATOM   8550  C  CB  . SER H  1 107 ? 73.381  115.046 32.459  1.00 24.24 ? 107 SER H CB  1 
ATOM   8551  O  OG  . SER H  1 107 ? 74.136  114.194 33.306  1.00 21.64 ? 107 SER H OG  1 
ATOM   8552  N  N   . GLY H  1 108 ? 74.314  113.555 30.016  1.00 25.62 ? 108 GLY H N   1 
ATOM   8553  C  CA  . GLY H  1 108 ? 75.253  112.613 29.431  1.00 19.72 ? 108 GLY H CA  1 
ATOM   8554  C  C   . GLY H  1 108 ? 74.578  111.816 28.343  1.00 27.26 ? 108 GLY H C   1 
ATOM   8555  O  O   . GLY H  1 108 ? 73.465  112.154 27.928  1.00 23.55 ? 108 GLY H O   1 
ATOM   8556  N  N   . ASP H  1 109 ? 75.226  110.756 27.873  1.00 19.96 ? 109 ASP H N   1 
ATOM   8557  C  CA  . ASP H  1 109 ? 74.677  110.027 26.736  1.00 23.76 ? 109 ASP H CA  1 
ATOM   8558  C  C   . ASP H  1 109 ? 73.449  109.124 27.010  1.00 23.24 ? 109 ASP H C   1 
ATOM   8559  O  O   . ASP H  1 109 ? 72.822  108.636 26.065  1.00 21.71 ? 109 ASP H O   1 
ATOM   8560  C  CB  . ASP H  1 109 ? 75.774  109.309 25.929  1.00 28.58 ? 109 ASP H CB  1 
ATOM   8561  C  CG  . ASP H  1 109 ? 76.777  108.601 26.805  1.00 31.28 ? 109 ASP H CG  1 
ATOM   8562  O  OD1 . ASP H  1 109 ? 76.410  108.271 27.948  1.00 36.96 ? 109 ASP H OD1 1 
ATOM   8563  O  OD2 . ASP H  1 109 ? 77.918  108.360 26.357  1.00 22.97 ? 109 ASP H OD2 1 
ATOM   8564  N  N   . HIS H  1 110 ? 73.096  108.925 28.279  1.00 21.58 ? 110 HIS H N   1 
ATOM   8565  C  CA  . HIS H  1 110 ? 71.853  108.225 28.625  1.00 21.39 ? 110 HIS H CA  1 
ATOM   8566  C  C   . HIS H  1 110 ? 70.745  109.234 28.971  1.00 18.07 ? 110 HIS H C   1 
ATOM   8567  O  O   . HIS H  1 110 ? 69.731  108.872 29.568  1.00 15.75 ? 110 HIS H O   1 
ATOM   8568  C  CB  . HIS H  1 110 ? 72.040  107.250 29.802  1.00 16.27 ? 110 HIS H CB  1 
ATOM   8569  C  CG  . HIS H  1 110 ? 72.892  106.057 29.487  1.00 25.24 ? 110 HIS H CG  1 
ATOM   8570  N  ND1 . HIS H  1 110 ? 73.078  105.019 30.380  1.00 27.77 ? 110 HIS H ND1 1 
ATOM   8571  C  CD2 . HIS H  1 110 ? 73.621  105.741 28.389  1.00 25.27 ? 110 HIS H CD2 1 
ATOM   8572  C  CE1 . HIS H  1 110 ? 73.870  104.109 29.837  1.00 23.63 ? 110 HIS H CE1 1 
ATOM   8573  N  NE2 . HIS H  1 110 ? 74.217  104.525 28.633  1.00 24.43 ? 110 HIS H NE2 1 
ATOM   8574  N  N   . CYS H  1 111 ? 70.951  110.495 28.595  1.00 16.43 ? 111 CYS H N   1 
ATOM   8575  C  CA  . CYS H  1 111 ? 70.009  111.560 28.902  1.00 17.25 ? 111 CYS H CA  1 
ATOM   8576  C  C   . CYS H  1 111 ? 68.655  111.330 28.226  1.00 13.08 ? 111 CYS H C   1 
ATOM   8577  O  O   . CYS H  1 111 ? 68.581  111.080 27.018  1.00 13.33 ? 111 CYS H O   1 
ATOM   8578  C  CB  . CYS H  1 111 ? 70.563  112.911 28.456  1.00 18.38 ? 111 CYS H CB  1 
ATOM   8579  S  SG  . CYS H  1 111 ? 69.658  114.348 29.063  1.00 20.19 ? 111 CYS H SG  1 
ATOM   8580  N  N   . ILE H  1 112 ? 67.586  111.440 28.999  1.00 10.85 ? 112 ILE H N   1 
ATOM   8581  C  CA  . ILE H  1 112 ? 66.242  111.279 28.417  1.00 11.38 ? 112 ILE H CA  1 
ATOM   8582  C  C   . ILE H  1 112 ? 65.483  112.601 28.272  1.00 10.28 ? 112 ILE H C   1 
ATOM   8583  O  O   . ILE H  1 112 ? 64.334  112.613 27.835  1.00 11.73 ? 112 ILE H O   1 
ATOM   8584  C  CB  . ILE H  1 112 ? 65.397  110.297 29.248  1.00 10.13 ? 112 ILE H CB  1 
ATOM   8585  C  CG1 . ILE H  1 112 ? 65.178  110.849 30.647  1.00 6.72  ? 112 ILE H CG1 1 
ATOM   8586  C  CG2 . ILE H  1 112 ? 66.089  108.940 29.357  1.00 8.02  ? 112 ILE H CG2 1 
ATOM   8587  C  CD1 . ILE H  1 112 ? 64.313  109.943 31.528  1.00 8.61  ? 112 ILE H CD1 1 
ATOM   8588  N  N   . ILE H  1 113 ? 66.099  113.709 28.671  1.00 9.71  ? 113 ILE H N   1 
ATOM   8589  C  CA  . ILE H  1 113 ? 65.502  115.024 28.456  1.00 11.50 ? 113 ILE H CA  1 
ATOM   8590  C  C   . ILE H  1 113 ? 65.302  115.273 26.950  1.00 13.65 ? 113 ILE H C   1 
ATOM   8591  O  O   . ILE H  1 113 ? 66.117  114.844 26.137  1.00 10.14 ? 113 ILE H O   1 
ATOM   8592  C  CB  . ILE H  1 113 ? 66.322  116.134 29.147  1.00 11.71 ? 113 ILE H CB  1 
ATOM   8593  C  CG1 . ILE H  1 113 ? 66.178  115.988 30.665  1.00 11.55 ? 113 ILE H CG1 1 
ATOM   8594  C  CG2 . ILE H  1 113 ? 65.877  117.519 28.697  1.00 9.42  ? 113 ILE H CG2 1 
ATOM   8595  C  CD1 . ILE H  1 113 ? 66.971  116.974 31.487  1.00 13.59 ? 113 ILE H CD1 1 
ATOM   8596  N  N   . GLY H  1 114 ? 64.180  115.882 26.566  1.00 9.32  ? 114 GLY H N   1 
ATOM   8597  C  CA  . GLY H  1 114 ? 63.904  116.052 25.153  1.00 7.80  ? 114 GLY H CA  1 
ATOM   8598  C  C   . GLY H  1 114 ? 63.487  114.782 24.423  1.00 6.41  ? 114 GLY H C   1 
ATOM   8599  O  O   . GLY H  1 114 ? 63.246  114.806 23.236  1.00 7.07  ? 114 GLY H O   1 
ATOM   8600  N  N   . ARG H  1 115 ? 63.396  113.666 25.131  1.00 8.56  ? 115 ARG H N   1 
ATOM   8601  C  CA  . ARG H  1 115 ? 62.829  112.447 24.554  1.00 8.66  ? 115 ARG H CA  1 
ATOM   8602  C  C   . ARG H  1 115 ? 61.369  112.275 25.020  1.00 9.12  ? 115 ARG H C   1 
ATOM   8603  O  O   . ARG H  1 115 ? 60.848  113.154 25.708  1.00 9.23  ? 115 ARG H O   1 
ATOM   8604  C  CB  . ARG H  1 115 ? 63.718  111.258 24.894  1.00 9.19  ? 115 ARG H CB  1 
ATOM   8605  C  CG  . ARG H  1 115 ? 65.148  111.499 24.337  1.00 11.70 ? 115 ARG H CG  1 
ATOM   8606  C  CD  . ARG H  1 115 ? 66.044  110.273 24.343  1.00 16.07 ? 115 ARG H CD  1 
ATOM   8607  N  NE  . ARG H  1 115 ? 67.440  110.683 24.153  1.00 17.05 ? 115 ARG H NE  1 
ATOM   8608  C  CZ  . ARG H  1 115 ? 68.036  110.768 22.970  1.00 14.24 ? 115 ARG H CZ  1 
ATOM   8609  N  NH1 . ARG H  1 115 ? 67.365  110.454 21.870  1.00 13.90 ? 115 ARG H NH1 1 
ATOM   8610  N  NH2 . ARG H  1 115 ? 69.307  111.150 22.896  1.00 18.72 ? 115 ARG H NH2 1 
ATOM   8611  N  N   . THR H  1 116 ? 60.712  111.180 24.637  1.00 7.87  ? 116 THR H N   1 
ATOM   8612  C  CA  . THR H  1 116 ? 59.279  111.032 24.895  1.00 8.59  ? 116 THR H CA  1 
ATOM   8613  C  C   . THR H  1 116 ? 58.971  109.901 25.841  1.00 7.53  ? 116 THR H C   1 
ATOM   8614  O  O   . THR H  1 116 ? 59.329  108.758 25.571  1.00 8.69  ? 116 THR H O   1 
ATOM   8615  C  CB  . THR H  1 116 ? 58.467  110.800 23.584  1.00 7.63  ? 116 THR H CB  1 
ATOM   8616  O  OG1 . THR H  1 116 ? 58.530  111.982 22.788  1.00 9.44  ? 116 THR H OG1 1 
ATOM   8617  C  CG2 . THR H  1 116 ? 56.974  110.520 23.893  1.00 5.15  ? 116 THR H CG2 1 
ATOM   8618  N  N   . LEU H  1 117 ? 58.289  110.220 26.936  1.00 6.87  ? 117 LEU H N   1 
ATOM   8619  C  CA  . LEU H  1 117 ? 57.792  109.204 27.847  1.00 6.82  ? 117 LEU H CA  1 
ATOM   8620  C  C   . LEU H  1 117 ? 56.480  108.676 27.288  1.00 6.98  ? 117 LEU H C   1 
ATOM   8621  O  O   . LEU H  1 117 ? 55.653  109.453 26.848  1.00 6.74  ? 117 LEU H O   1 
ATOM   8622  C  CB  . LEU H  1 117 ? 57.532  109.821 29.224  1.00 8.11  ? 117 LEU H CB  1 
ATOM   8623  C  CG  . LEU H  1 117 ? 57.033  108.903 30.345  1.00 8.10  ? 117 LEU H CG  1 
ATOM   8624  C  CD1 . LEU H  1 117 ? 58.066  107.818 30.652  1.00 7.32  ? 117 LEU H CD1 1 
ATOM   8625  C  CD2 . LEU H  1 117 ? 56.715  109.713 31.614  1.00 8.18  ? 117 LEU H CD2 1 
ATOM   8626  N  N   . VAL H  1 118 ? 56.282  107.365 27.322  1.00 7.22  ? 118 VAL H N   1 
ATOM   8627  C  CA  . VAL H  1 118 ? 55.056  106.769 26.784  1.00 6.97  ? 118 VAL H CA  1 
ATOM   8628  C  C   . VAL H  1 118 ? 54.469  105.741 27.733  1.00 7.02  ? 118 VAL H C   1 
ATOM   8629  O  O   . VAL H  1 118 ? 55.188  104.904 28.268  1.00 7.27  ? 118 VAL H O   1 
ATOM   8630  C  CB  . VAL H  1 118 ? 55.318  106.066 25.435  1.00 5.73  ? 118 VAL H CB  1 
ATOM   8631  C  CG1 . VAL H  1 118 ? 54.051  105.381 24.901  1.00 5.45  ? 118 VAL H CG1 1 
ATOM   8632  C  CG2 . VAL H  1 118 ? 55.871  107.068 24.406  1.00 7.46  ? 118 VAL H CG2 1 
ATOM   8633  N  N   . VAL H  1 119 ? 53.160  105.803 27.944  1.00 7.02  ? 119 VAL H N   1 
ATOM   8634  C  CA  . VAL H  1 119 ? 52.490  104.766 28.715  1.00 6.37  ? 119 VAL H CA  1 
ATOM   8635  C  C   . VAL H  1 119 ? 51.612  103.960 27.775  1.00 7.34  ? 119 VAL H C   1 
ATOM   8636  O  O   . VAL H  1 119 ? 50.884  104.522 26.948  1.00 6.99  ? 119 VAL H O   1 
ATOM   8637  C  CB  . VAL H  1 119 ? 51.721  105.337 29.939  1.00 6.05  ? 119 VAL H CB  1 
ATOM   8638  C  CG1 . VAL H  1 119 ? 50.597  106.277 29.501  1.00 6.46  ? 119 VAL H CG1 1 
ATOM   8639  C  CG2 . VAL H  1 119 ? 51.209  104.197 30.826  1.00 5.71  ? 119 VAL H CG2 1 
ATOM   8640  N  N   . HIS H  1 120 ? 51.725  102.641 27.872  1.00 6.01  ? 120 HIS H N   1 
ATOM   8641  C  CA  . HIS H  1 120 ? 51.121  101.732 26.910  1.00 8.53  ? 120 HIS H CA  1 
ATOM   8642  C  C   . HIS H  1 120 ? 49.833  101.075 27.345  1.00 8.27  ? 120 HIS H C   1 
ATOM   8643  O  O   . HIS H  1 120 ? 49.520  101.035 28.521  1.00 8.09  ? 120 HIS H O   1 
ATOM   8644  C  CB  . HIS H  1 120 ? 52.095  100.614 26.557  1.00 8.13  ? 120 HIS H CB  1 
ATOM   8645  C  CG  . HIS H  1 120 ? 53.174  101.054 25.632  1.00 11.62 ? 120 HIS H CG  1 
ATOM   8646  N  ND1 . HIS H  1 120 ? 53.112  100.839 24.274  1.00 12.97 ? 120 HIS H ND1 1 
ATOM   8647  C  CD2 . HIS H  1 120 ? 54.321  101.736 25.860  1.00 10.38 ? 120 HIS H CD2 1 
ATOM   8648  C  CE1 . HIS H  1 120 ? 54.184  101.356 23.703  1.00 13.25 ? 120 HIS H CE1 1 
ATOM   8649  N  NE2 . HIS H  1 120 ? 54.929  101.911 24.642  1.00 14.30 ? 120 HIS H NE2 1 
ATOM   8650  N  N   . GLU H  1 121 ? 49.155  100.506 26.350  1.00 8.48  ? 121 GLU H N   1 
ATOM   8651  C  CA  . GLU H  1 121 ? 47.873  99.820  26.465  1.00 10.33 ? 121 GLU H CA  1 
ATOM   8652  C  C   . GLU H  1 121 ? 47.917  98.589  27.373  1.00 10.17 ? 121 GLU H C   1 
ATOM   8653  O  O   . GLU H  1 121 ? 47.009  98.352  28.160  1.00 10.04 ? 121 GLU H O   1 
ATOM   8654  C  CB  . GLU H  1 121 ? 47.430  99.391  25.048  1.00 10.50 ? 121 GLU H CB  1 
ATOM   8655  C  CG  . GLU H  1 121 ? 46.287  98.399  25.008  1.00 12.79 ? 121 GLU H CG  1 
ATOM   8656  C  CD  . GLU H  1 121 ? 46.005  97.841  23.601  1.00 14.09 ? 121 GLU H CD  1 
ATOM   8657  O  OE1 . GLU H  1 121 ? 44.872  97.399  23.393  1.00 21.26 ? 121 GLU H OE1 1 
ATOM   8658  O  OE2 . GLU H  1 121 ? 46.891  97.820  22.720  1.00 14.82 ? 121 GLU H OE2 1 
ATOM   8659  N  N   . LYS H  1 122 ? 48.976  97.806  27.232  1.00 11.23 ? 122 LYS H N   1 
ATOM   8660  C  CA  . LYS H  1 122 ? 49.073  96.488  27.846  1.00 13.19 ? 122 LYS H CA  1 
ATOM   8661  C  C   . LYS H  1 122 ? 50.367  96.395  28.643  1.00 10.85 ? 122 LYS H C   1 
ATOM   8662  O  O   . LYS H  1 122 ? 51.212  97.288  28.585  1.00 8.54  ? 122 LYS H O   1 
ATOM   8663  C  CB  . LYS H  1 122 ? 49.138  95.403  26.760  1.00 15.72 ? 122 LYS H CB  1 
ATOM   8664  C  CG  . LYS H  1 122 ? 47.981  95.367  25.792  1.00 17.05 ? 122 LYS H CG  1 
ATOM   8665  C  CD  . LYS H  1 122 ? 47.921  94.001  25.090  1.00 20.86 ? 122 LYS H CD  1 
ATOM   8666  C  CE  . LYS H  1 122 ? 48.720  93.978  23.806  1.00 21.20 ? 122 LYS H CE  1 
ATOM   8667  N  NZ  . LYS H  1 122 ? 48.294  92.859  22.886  1.00 32.37 ? 122 LYS H NZ  1 
ATOM   8668  N  N   . ALA H  1 123 ? 50.519  95.281  29.353  1.00 11.03 ? 123 ALA H N   1 
ATOM   8669  C  CA  . ALA H  1 123 ? 51.708  94.983  30.126  1.00 10.35 ? 123 ALA H CA  1 
ATOM   8670  C  C   . ALA H  1 123 ? 52.937  94.818  29.234  1.00 9.44  ? 123 ALA H C   1 
ATOM   8671  O  O   . ALA H  1 123 ? 52.869  94.251  28.152  1.00 10.58 ? 123 ALA H O   1 
ATOM   8672  C  CB  . ALA H  1 123 ? 51.485  93.719  30.909  1.00 11.31 ? 123 ALA H CB  1 
ATOM   8673  N  N   . ASP H  1 124 ? 54.062  95.323  29.700  1.00 10.03 ? 124 ASP H N   1 
ATOM   8674  C  CA  . ASP H  1 124 ? 55.358  95.009  29.104  1.00 10.86 ? 124 ASP H CA  1 
ATOM   8675  C  C   . ASP H  1 124 ? 55.745  93.610  29.601  1.00 12.10 ? 124 ASP H C   1 
ATOM   8676  O  O   . ASP H  1 124 ? 55.754  93.368  30.800  1.00 11.36 ? 124 ASP H O   1 
ATOM   8677  C  CB  . ASP H  1 124 ? 56.366  96.038  29.579  1.00 9.74  ? 124 ASP H CB  1 
ATOM   8678  C  CG  . ASP H  1 124 ? 57.722  95.924  28.879  1.00 14.99 ? 124 ASP H CG  1 
ATOM   8679  O  OD1 . ASP H  1 124 ? 58.057  94.837  28.364  1.00 14.01 ? 124 ASP H OD1 1 
ATOM   8680  O  OD2 . ASP H  1 124 ? 58.447  96.946  28.855  1.00 10.64 ? 124 ASP H OD2 1 
ATOM   8681  N  N   . ASP H  1 125 ? 56.029  92.681  28.693  1.00 14.11 ? 125 ASP H N   1 
ATOM   8682  C  CA  . ASP H  1 125 ? 56.466  91.350  29.111  1.00 12.71 ? 125 ASP H CA  1 
ATOM   8683  C  C   . ASP H  1 125 ? 57.954  91.291  29.491  1.00 15.14 ? 125 ASP H C   1 
ATOM   8684  O  O   . ASP H  1 125 ? 58.482  90.216  29.772  1.00 14.86 ? 125 ASP H O   1 
ATOM   8685  C  CB  . ASP H  1 125 ? 56.098  90.261  28.087  1.00 13.63 ? 125 ASP H CB  1 
ATOM   8686  C  CG  . ASP H  1 125 ? 56.899  90.350  26.777  1.00 13.26 ? 125 ASP H CG  1 
ATOM   8687  O  OD1 . ASP H  1 125 ? 57.919  91.051  26.702  1.00 12.99 ? 125 ASP H OD1 1 
ATOM   8688  O  OD2 . ASP H  1 125 ? 56.494  89.698  25.801  1.00 16.26 ? 125 ASP H OD2 1 
ATOM   8689  N  N   . LEU H  1 126 ? 58.618  92.445  29.503  1.00 13.22 ? 126 LEU H N   1 
ATOM   8690  C  CA  . LEU H  1 126 ? 60.005  92.531  29.980  1.00 14.20 ? 126 LEU H CA  1 
ATOM   8691  C  C   . LEU H  1 126 ? 60.971  91.613  29.215  1.00 12.52 ? 126 LEU H C   1 
ATOM   8692  O  O   . LEU H  1 126 ? 61.956  91.140  29.770  1.00 12.27 ? 126 LEU H O   1 
ATOM   8693  C  CB  . LEU H  1 126 ? 60.081  92.230  31.478  1.00 12.21 ? 126 LEU H CB  1 
ATOM   8694  C  CG  . LEU H  1 126 ? 59.038  92.933  32.353  1.00 17.88 ? 126 LEU H CG  1 
ATOM   8695  C  CD1 . LEU H  1 126 ? 59.223  92.545  33.824  1.00 12.88 ? 126 LEU H CD1 1 
ATOM   8696  C  CD2 . LEU H  1 126 ? 59.123  94.434  32.167  1.00 11.59 ? 126 LEU H CD2 1 
ATOM   8697  N  N   . GLY H  1 127 ? 60.653  91.328  27.959  1.00 14.97 ? 127 GLY H N   1 
ATOM   8698  C  CA  . GLY H  1 127 ? 61.557  90.593  27.092  1.00 15.73 ? 127 GLY H CA  1 
ATOM   8699  C  C   . GLY H  1 127 ? 61.427  89.097  27.276  1.00 19.64 ? 127 GLY H C   1 
ATOM   8700  O  O   . GLY H  1 127 ? 62.185  88.309  26.697  1.00 22.12 ? 127 GLY H O   1 
ATOM   8701  N  N   . LYS H  1 128 ? 60.441  88.699  28.064  1.00 14.73 ? 128 LYS H N   1 
ATOM   8702  C  CA  . LYS H  1 128 ? 60.316  87.303  28.462  1.00 17.91 ? 128 LYS H CA  1 
ATOM   8703  C  C   . LYS H  1 128 ? 59.260  86.572  27.674  1.00 16.19 ? 128 LYS H C   1 
ATOM   8704  O  O   . LYS H  1 128 ? 58.915  85.436  27.996  1.00 18.89 ? 128 LYS H O   1 
ATOM   8705  C  CB  . LYS H  1 128 ? 60.009  87.202  29.964  1.00 17.24 ? 128 LYS H CB  1 
ATOM   8706  C  CG  . LYS H  1 128 ? 61.171  87.596  30.832  1.00 18.16 ? 128 LYS H CG  1 
ATOM   8707  C  CD  . LYS H  1 128 ? 60.774  87.669  32.297  1.00 26.40 ? 128 LYS H CD  1 
ATOM   8708  C  CE  . LYS H  1 128 ? 60.681  86.289  32.948  1.00 20.62 ? 128 LYS H CE  1 
ATOM   8709  N  NZ  . LYS H  1 128 ? 60.349  86.493  34.378  1.00 29.57 ? 128 LYS H NZ  1 
ATOM   8710  N  N   . GLY H  1 129 ? 58.749  87.219  26.634  1.00 17.18 ? 129 GLY H N   1 
ATOM   8711  C  CA  . GLY H  1 129 ? 57.627  86.676  25.884  1.00 16.22 ? 129 GLY H CA  1 
ATOM   8712  C  C   . GLY H  1 129 ? 57.987  85.628  24.842  1.00 18.20 ? 129 GLY H C   1 
ATOM   8713  O  O   . GLY H  1 129 ? 57.111  84.908  24.371  1.00 15.99 ? 129 GLY H O   1 
ATOM   8714  N  N   . GLY H  1 130 ? 59.267  85.529  24.488  1.00 16.42 ? 130 GLY H N   1 
ATOM   8715  C  CA  . GLY H  1 130 ? 59.715  84.486  23.572  1.00 23.96 ? 130 GLY H CA  1 
ATOM   8716  C  C   . GLY H  1 130 ? 59.431  84.662  22.082  1.00 24.89 ? 130 GLY H C   1 
ATOM   8717  O  O   . GLY H  1 130 ? 59.737  83.778  21.283  1.00 24.52 ? 130 GLY H O   1 
ATOM   8718  N  N   . ASN H  1 131 ? 58.828  85.785  21.701  1.00 23.00 ? 131 ASN H N   1 
ATOM   8719  C  CA  . ASN H  1 131 ? 58.623  86.086  20.288  1.00 21.58 ? 131 ASN H CA  1 
ATOM   8720  C  C   . ASN H  1 131 ? 59.506  87.251  19.860  1.00 21.82 ? 131 ASN H C   1 
ATOM   8721  O  O   . ASN H  1 131 ? 60.159  87.891  20.699  1.00 19.29 ? 131 ASN H O   1 
ATOM   8722  C  CB  . ASN H  1 131 ? 57.132  86.317  19.931  1.00 20.70 ? 131 ASN H CB  1 
ATOM   8723  C  CG  . ASN H  1 131 ? 56.531  87.555  20.603  1.00 18.58 ? 131 ASN H CG  1 
ATOM   8724  O  OD1 . ASN H  1 131 ? 57.189  88.225  21.382  1.00 22.04 ? 131 ASN H OD1 1 
ATOM   8725  N  ND2 . ASN H  1 131 ? 55.277  87.862  20.286  1.00 15.20 ? 131 ASN H ND2 1 
ATOM   8726  N  N   . GLU H  1 132 ? 59.546  87.517  18.559  1.00 19.42 ? 132 GLU H N   1 
ATOM   8727  C  CA  . GLU H  1 132 ? 60.379  88.588  18.037  1.00 18.85 ? 132 GLU H CA  1 
ATOM   8728  C  C   . GLU H  1 132 ? 60.033  89.892  18.702  1.00 14.39 ? 132 GLU H C   1 
ATOM   8729  O  O   . GLU H  1 132 ? 60.900  90.653  19.076  1.00 13.55 ? 132 GLU H O   1 
ATOM   8730  C  CB  . GLU H  1 132 ? 60.174  88.756  16.527  1.00 23.44 ? 132 GLU H CB  1 
ATOM   8731  C  CG  . GLU H  1 132 ? 60.734  87.650  15.694  1.00 29.71 ? 132 GLU H CG  1 
ATOM   8732  C  CD  . GLU H  1 132 ? 60.567  87.925  14.204  1.00 39.58 ? 132 GLU H CD  1 
ATOM   8733  O  OE1 . GLU H  1 132 ? 60.029  88.995  13.839  1.00 40.81 ? 132 GLU H OE1 1 
ATOM   8734  O  OE2 . GLU H  1 132 ? 60.978  87.069  13.399  1.00 47.51 ? 132 GLU H OE2 1 
ATOM   8735  N  N   . GLU H  1 133 ? 58.741  90.139  18.840  1.00 18.48 ? 133 GLU H N   1 
ATOM   8736  C  CA  . GLU H  1 133 ? 58.263  91.396  19.391  1.00 20.29 ? 133 GLU H CA  1 
ATOM   8737  C  C   . GLU H  1 133 ? 58.643  91.581  20.873  1.00 17.28 ? 133 GLU H C   1 
ATOM   8738  O  O   . GLU H  1 133 ? 58.992  92.689  21.301  1.00 16.55 ? 133 GLU H O   1 
ATOM   8739  C  CB  . GLU H  1 133 ? 56.749  91.504  19.178  1.00 21.29 ? 133 GLU H CB  1 
ATOM   8740  C  CG  . GLU H  1 133 ? 56.199  92.885  19.425  1.00 25.98 ? 133 GLU H CG  1 
ATOM   8741  C  CD  . GLU H  1 133 ? 56.573  93.879  18.328  1.00 33.27 ? 133 GLU H CD  1 
ATOM   8742  O  OE1 . GLU H  1 133 ? 57.294  93.496  17.366  1.00 31.24 ? 133 GLU H OE1 1 
ATOM   8743  O  OE2 . GLU H  1 133 ? 56.127  95.046  18.435  1.00 32.08 ? 133 GLU H OE2 1 
ATOM   8744  N  N   . SER H  1 134 ? 58.633  90.496  21.644  1.00 15.65 ? 134 SER H N   1 
ATOM   8745  C  CA  . SER H  1 134 ? 59.071  90.593  23.041  1.00 15.68 ? 134 SER H CA  1 
ATOM   8746  C  C   . SER H  1 134 ? 60.470  91.201  23.172  1.00 17.86 ? 134 SER H C   1 
ATOM   8747  O  O   . SER H  1 134 ? 60.721  92.039  24.044  1.00 14.49 ? 134 SER H O   1 
ATOM   8748  C  CB  . SER H  1 134 ? 59.058  89.226  23.715  1.00 16.16 ? 134 SER H CB  1 
ATOM   8749  O  OG  . SER H  1 134 ? 59.579  89.355  25.026  1.00 17.78 ? 134 SER H OG  1 
ATOM   8750  N  N   . THR H  1 135 ? 61.370  90.801  22.278  1.00 14.56 ? 135 THR H N   1 
ATOM   8751  C  CA  . THR H  1 135 ? 62.753  91.282  22.294  1.00 16.96 ? 135 THR H CA  1 
ATOM   8752  C  C   . THR H  1 135 ? 62.912  92.724  21.787  1.00 15.88 ? 135 THR H C   1 
ATOM   8753  O  O   . THR H  1 135 ? 63.987  93.292  21.866  1.00 19.20 ? 135 THR H O   1 
ATOM   8754  C  CB  . THR H  1 135 ? 63.646  90.390  21.421  1.00 22.52 ? 135 THR H CB  1 
ATOM   8755  O  OG1 . THR H  1 135 ? 63.187  89.037  21.486  1.00 22.45 ? 135 THR H OG1 1 
ATOM   8756  C  CG2 . THR H  1 135 ? 65.050  90.426  21.916  1.00 28.22 ? 135 THR H CG2 1 
ATOM   8757  N  N   . LYS H  1 136 ? 61.836  93.311  21.274  1.00 16.23 ? 136 LYS H N   1 
ATOM   8758  C  CA  . LYS H  1 136 ? 61.882  94.679  20.748  1.00 17.45 ? 136 LYS H CA  1 
ATOM   8759  C  C   . LYS H  1 136 ? 61.019  95.663  21.517  1.00 16.72 ? 136 LYS H C   1 
ATOM   8760  O  O   . LYS H  1 136 ? 61.485  96.730  21.895  1.00 17.75 ? 136 LYS H O   1 
ATOM   8761  C  CB  . LYS H  1 136 ? 61.481  94.686  19.262  1.00 22.25 ? 136 LYS H CB  1 
ATOM   8762  C  CG  . LYS H  1 136 ? 62.566  94.111  18.359  1.00 23.81 ? 136 LYS H CG  1 
ATOM   8763  C  CD  . LYS H  1 136 ? 62.015  93.730  16.990  1.00 35.33 ? 136 LYS H CD  1 
ATOM   8764  C  CE  . LYS H  1 136 ? 61.258  94.891  16.354  1.00 39.05 ? 136 LYS H CE  1 
ATOM   8765  N  NZ  . LYS H  1 136 ? 60.537  94.436  15.130  1.00 42.49 ? 136 LYS H NZ  1 
ATOM   8766  N  N   . THR H  1 137 ? 59.759  95.315  21.754  1.00 13.69 ? 137 THR H N   1 
ATOM   8767  C  CA  . THR H  1 137 ? 58.870  96.251  22.404  1.00 16.58 ? 137 THR H CA  1 
ATOM   8768  C  C   . THR H  1 137 ? 58.292  95.770  23.752  1.00 17.00 ? 137 THR H C   1 
ATOM   8769  O  O   . THR H  1 137 ? 57.761  96.563  24.516  1.00 15.72 ? 137 THR H O   1 
ATOM   8770  C  CB  . THR H  1 137 ? 57.705  96.583  21.479  1.00 19.48 ? 137 THR H CB  1 
ATOM   8771  O  OG1 . THR H  1 137 ? 56.860  95.435  21.377  1.00 15.18 ? 137 THR H OG1 1 
ATOM   8772  C  CG2 . THR H  1 137 ? 58.225  96.964  20.094  1.00 21.01 ? 137 THR H CG2 1 
ATOM   8773  N  N   . GLY H  1 138 ? 58.366  94.474  24.016  1.00 14.93 ? 138 GLY H N   1 
ATOM   8774  C  CA  . GLY H  1 138 ? 57.729  93.893  25.179  1.00 12.04 ? 138 GLY H CA  1 
ATOM   8775  C  C   . GLY H  1 138 ? 56.267  93.515  24.977  1.00 13.42 ? 138 GLY H C   1 
ATOM   8776  O  O   . GLY H  1 138 ? 55.630  93.076  25.935  1.00 14.20 ? 138 GLY H O   1 
ATOM   8777  N  N   . ASN H  1 139 ? 55.741  93.685  23.758  1.00 10.33 ? 139 ASN H N   1 
ATOM   8778  C  CA  . ASN H  1 139 ? 54.329  93.413  23.448  1.00 11.74 ? 139 ASN H CA  1 
ATOM   8779  C  C   . ASN H  1 139 ? 53.357  94.234  24.292  1.00 11.36 ? 139 ASN H C   1 
ATOM   8780  O  O   . ASN H  1 139 ? 52.308  93.734  24.695  1.00 11.84 ? 139 ASN H O   1 
ATOM   8781  C  CB  . ASN H  1 139 ? 53.985  91.932  23.626  1.00 12.45 ? 139 ASN H CB  1 
ATOM   8782  C  CG  . ASN H  1 139 ? 54.745  91.034  22.668  1.00 17.17 ? 139 ASN H CG  1 
ATOM   8783  O  OD1 . ASN H  1 139 ? 54.458  91.019  21.479  1.00 20.22 ? 139 ASN H OD1 1 
ATOM   8784  N  ND2 . ASN H  1 139 ? 55.709  90.263  23.190  1.00 14.57 ? 139 ASN H ND2 1 
ATOM   8785  N  N   . ALA H  1 140 ? 53.699  95.489  24.544  1.00 8.96  ? 140 ALA H N   1 
ATOM   8786  C  CA  . ALA H  1 140 ? 52.885  96.347  25.387  1.00 12.27 ? 140 ALA H CA  1 
ATOM   8787  C  C   . ALA H  1 140 ? 51.752  97.055  24.633  1.00 12.67 ? 140 ALA H C   1 
ATOM   8788  O  O   . ALA H  1 140 ? 51.072  97.922  25.190  1.00 10.93 ? 140 ALA H O   1 
ATOM   8789  C  CB  . ALA H  1 140 ? 53.764  97.364  26.127  1.00 11.63 ? 140 ALA H CB  1 
ATOM   8790  N  N   . GLY H  1 141 ? 51.542  96.674  23.378  1.00 13.78 ? 141 GLY H N   1 
ATOM   8791  C  CA  . GLY H  1 141 ? 50.490  97.259  22.564  1.00 12.52 ? 141 GLY H CA  1 
ATOM   8792  C  C   . GLY H  1 141 ? 50.641  98.741  22.311  1.00 11.43 ? 141 GLY H C   1 
ATOM   8793  O  O   . GLY H  1 141 ? 51.727  99.308  22.403  1.00 13.05 ? 141 GLY H O   1 
ATOM   8794  N  N   . SER H  1 142 ? 49.525  99.386  22.024  1.00 10.03 ? 142 SER H N   1 
ATOM   8795  C  CA  . SER H  1 142 ? 49.545  100.737 21.499  1.00 10.15 ? 142 SER H CA  1 
ATOM   8796  C  C   . SER H  1 142 ? 49.934  101.786 22.546  1.00 10.47 ? 142 SER H C   1 
ATOM   8797  O  O   . SER H  1 142 ? 50.009  101.511 23.758  1.00 11.32 ? 142 SER H O   1 
ATOM   8798  C  CB  . SER H  1 142 ? 48.165  101.062 20.926  1.00 13.18 ? 142 SER H CB  1 
ATOM   8799  O  OG  . SER H  1 142 ? 47.262  101.248 21.990  1.00 16.19 ? 142 SER H OG  1 
ATOM   8800  N  N   . ARG H  1 143 ? 50.157  102.999 22.069  1.00 9.80  ? 143 ARG H N   1 
ATOM   8801  C  CA  . ARG H  1 143 ? 50.634  104.088 22.894  1.00 9.83  ? 143 ARG H CA  1 
ATOM   8802  C  C   . ARG H  1 143 ? 49.434  104.914 23.321  1.00 10.53 ? 143 ARG H C   1 
ATOM   8803  O  O   . ARG H  1 143 ? 48.789  105.534 22.483  1.00 8.71  ? 143 ARG H O   1 
ATOM   8804  C  CB  . ARG H  1 143 ? 51.661  104.935 22.112  1.00 10.04 ? 143 ARG H CB  1 
ATOM   8805  C  CG  . ARG H  1 143 ? 52.699  104.079 21.365  1.00 10.56 ? 143 ARG H CG  1 
ATOM   8806  C  CD  . ARG H  1 143 ? 53.810  104.883 20.583  1.00 12.92 ? 143 ARG H CD  1 
ATOM   8807  N  NE  . ARG H  1 143 ? 54.780  103.949 20.010  1.00 15.57 ? 143 ARG H NE  1 
ATOM   8808  C  CZ  . ARG H  1 143 ? 55.863  104.270 19.294  1.00 18.77 ? 143 ARG H CZ  1 
ATOM   8809  N  NH1 . ARG H  1 143 ? 56.163  105.532 19.009  1.00 14.80 ? 143 ARG H NH1 1 
ATOM   8810  N  NH2 . ARG H  1 143 ? 56.652  103.307 18.845  1.00 14.55 ? 143 ARG H NH2 1 
ATOM   8811  N  N   . LEU H  1 144 ? 49.154  104.936 24.628  1.00 8.32  ? 144 LEU H N   1 
ATOM   8812  C  CA  . LEU H  1 144 ? 47.957  105.565 25.150  1.00 9.09  ? 144 LEU H CA  1 
ATOM   8813  C  C   . LEU H  1 144 ? 48.157  107.044 25.394  1.00 9.58  ? 144 LEU H C   1 
ATOM   8814  O  O   . LEU H  1 144 ? 47.281  107.855 25.086  1.00 10.04 ? 144 LEU H O   1 
ATOM   8815  C  CB  . LEU H  1 144 ? 47.476  104.876 26.444  1.00 8.25  ? 144 LEU H CB  1 
ATOM   8816  C  CG  . LEU H  1 144 ? 47.015  103.414 26.341  1.00 10.75 ? 144 LEU H CG  1 
ATOM   8817  C  CD1 . LEU H  1 144 ? 46.321  103.015 27.624  1.00 10.36 ? 144 LEU H CD1 1 
ATOM   8818  C  CD2 . LEU H  1 144 ? 46.089  103.200 25.158  1.00 10.48 ? 144 LEU H CD2 1 
ATOM   8819  N  N   . ALA H  1 145 ? 49.287  107.399 25.985  1.00 6.59  ? 145 ALA H N   1 
ATOM   8820  C  CA  . ALA H  1 145 ? 49.579  108.795 26.222  1.00 6.76  ? 145 ALA H CA  1 
ATOM   8821  C  C   . ALA H  1 145 ? 51.077  108.994 26.201  1.00 7.60  ? 145 ALA H C   1 
ATOM   8822  O  O   . ALA H  1 145 ? 51.839  108.056 26.446  1.00 8.59  ? 145 ALA H O   1 
ATOM   8823  C  CB  . ALA H  1 145 ? 48.978  109.277 27.562  1.00 7.34  ? 145 ALA H CB  1 
ATOM   8824  N  N   . CYS H  1 146 ? 51.501  110.216 25.919  1.00 5.70  ? 146 CYS H N   1 
ATOM   8825  C  CA  . CYS H  1 146 ? 52.905  110.474 25.788  1.00 9.77  ? 146 CYS H CA  1 
ATOM   8826  C  C   . CYS H  1 146 ? 53.096  111.947 25.986  1.00 11.16 ? 146 CYS H C   1 
ATOM   8827  O  O   . CYS H  1 146 ? 52.131  112.704 26.056  1.00 9.92  ? 146 CYS H O   1 
ATOM   8828  C  CB  . CYS H  1 146 ? 53.398  110.056 24.391  1.00 9.07  ? 146 CYS H CB  1 
ATOM   8829  S  SG  . CYS H  1 146 ? 52.891  111.200 23.143  1.00 18.56 ? 146 CYS H SG  1 
ATOM   8830  N  N   . GLY H  1 147 ? 54.349  112.349 26.094  1.00 9.79  ? 147 GLY H N   1 
ATOM   8831  C  CA  . GLY H  1 147 ? 54.688  113.753 26.168  1.00 9.24  ? 147 GLY H CA  1 
ATOM   8832  C  C   . GLY H  1 147 ? 56.199  113.854 26.126  1.00 10.15 ? 147 GLY H C   1 
ATOM   8833  O  O   . GLY H  1 147 ? 56.894  112.853 26.290  1.00 9.32  ? 147 GLY H O   1 
ATOM   8834  N  N   . VAL H  1 148 ? 56.703  115.062 25.926  1.00 7.65  ? 148 VAL H N   1 
ATOM   8835  C  CA  . VAL H  1 148 ? 58.125  115.282 25.839  1.00 10.43 ? 148 VAL H CA  1 
ATOM   8836  C  C   . VAL H  1 148 ? 58.680  115.594 27.225  1.00 9.15  ? 148 VAL H C   1 
ATOM   8837  O  O   . VAL H  1 148 ? 58.076  116.337 27.999  1.00 8.06  ? 148 VAL H O   1 
ATOM   8838  C  CB  . VAL H  1 148 ? 58.446  116.413 24.851  1.00 11.37 ? 148 VAL H CB  1 
ATOM   8839  C  CG1 . VAL H  1 148 ? 59.938  116.557 24.702  1.00 8.96  ? 148 VAL H CG1 1 
ATOM   8840  C  CG2 . VAL H  1 148 ? 57.777  116.133 23.493  1.00 7.52  ? 148 VAL H CG2 1 
ATOM   8841  N  N   . ILE H  1 149 ? 59.818  114.991 27.540  1.00 7.88  ? 149 ILE H N   1 
ATOM   8842  C  CA  . ILE H  1 149 ? 60.423  115.163 28.845  1.00 9.96  ? 149 ILE H CA  1 
ATOM   8843  C  C   . ILE H  1 149 ? 61.182  116.467 28.899  1.00 8.72  ? 149 ILE H C   1 
ATOM   8844  O  O   . ILE H  1 149 ? 62.131  116.668 28.165  1.00 10.22 ? 149 ILE H O   1 
ATOM   8845  C  CB  . ILE H  1 149 ? 61.350  113.996 29.178  1.00 9.02  ? 149 ILE H CB  1 
ATOM   8846  C  CG1 . ILE H  1 149 ? 60.554  112.698 29.141  1.00 10.33 ? 149 ILE H CG1 1 
ATOM   8847  C  CG2 . ILE H  1 149 ? 62.024  114.198 30.544  1.00 7.68  ? 149 ILE H CG2 1 
ATOM   8848  C  CD1 . ILE H  1 149 ? 61.401  111.482 29.316  1.00 10.80 ? 149 ILE H CD1 1 
ATOM   8849  N  N   . GLY H  1 150 ? 60.762  117.351 29.791  1.00 9.55  ? 150 GLY H N   1 
ATOM   8850  C  CA  . GLY H  1 150 ? 61.284  118.705 29.815  1.00 9.87  ? 150 GLY H CA  1 
ATOM   8851  C  C   . GLY H  1 150 ? 62.074  118.973 31.071  1.00 10.04 ? 150 GLY H C   1 
ATOM   8852  O  O   . GLY H  1 150 ? 61.869  118.312 32.081  1.00 13.15 ? 150 GLY H O   1 
ATOM   8853  N  N   . ILE H  1 151 ? 62.985  119.934 30.992  1.00 11.21 ? 151 ILE H N   1 
ATOM   8854  C  CA  . ILE H  1 151 ? 63.778  120.379 32.136  1.00 12.24 ? 151 ILE H CA  1 
ATOM   8855  C  C   . ILE H  1 151 ? 62.858  121.084 33.110  1.00 11.91 ? 151 ILE H C   1 
ATOM   8856  O  O   . ILE H  1 151 ? 62.089  121.957 32.709  1.00 14.63 ? 151 ILE H O   1 
ATOM   8857  C  CB  . ILE H  1 151 ? 64.880  121.368 31.678  1.00 12.32 ? 151 ILE H CB  1 
ATOM   8858  C  CG1 . ILE H  1 151 ? 65.951  120.624 30.884  1.00 14.37 ? 151 ILE H CG1 1 
ATOM   8859  C  CG2 . ILE H  1 151 ? 65.489  122.103 32.877  1.00 14.88 ? 151 ILE H CG2 1 
ATOM   8860  C  CD1 . ILE H  1 151 ? 66.863  121.552 30.067  1.00 12.52 ? 151 ILE H CD1 1 
ATOM   8861  N  N   . ALA H  1 152 ? 62.910  120.704 34.379  1.00 12.20 ? 152 ALA H N   1 
ATOM   8862  C  CA  . ALA H  1 152 ? 62.034  121.322 35.370  1.00 14.64 ? 152 ALA H CA  1 
ATOM   8863  C  C   . ALA H  1 152 ? 62.828  122.096 36.411  1.00 17.31 ? 152 ALA H C   1 
ATOM   8864  O  O   . ALA H  1 152 ? 64.014  121.833 36.624  1.00 18.47 ? 152 ALA H O   1 
ATOM   8865  C  CB  . ALA H  1 152 ? 61.142  120.285 36.036  1.00 16.56 ? 152 ALA H CB  1 
ATOM   8866  N  N   . GLN H  1 153 ? 62.165  123.061 37.039  1.00 16.27 ? 153 GLN H N   1 
ATOM   8867  C  CA  . GLN H  1 153 ? 62.804  124.009 37.945  1.00 21.64 ? 153 GLN H CA  1 
ATOM   8868  C  C   . GLN H  1 153 ? 63.242  123.357 39.245  1.00 23.93 ? 153 GLN H C   1 
ATOM   8869  O  O   . GLN H  1 153 ? 62.565  122.460 39.770  1.00 27.83 ? 153 GLN H O   1 
ATOM   8870  C  CB  . GLN H  1 153 ? 61.875  125.199 38.259  1.00 22.01 ? 153 GLN H CB  1 
ATOM   8871  C  CG  . GLN H  1 153 ? 62.528  126.215 39.180  1.00 25.34 ? 153 GLN H CG  1 
ATOM   8872  C  CD  . GLN H  1 153 ? 61.732  127.497 39.334  1.00 33.57 ? 153 GLN H CD  1 
ATOM   8873  O  OE1 . GLN H  1 153 ? 60.514  127.480 39.517  1.00 28.04 ? 153 GLN H OE1 1 
ATOM   8874  N  NE2 . GLN H  1 153 ? 62.424  128.624 39.256  1.00 34.02 ? 153 GLN H NE2 1 
ATOM   8875  O  OXT . GLN H  1 153 ? 64.284  123.730 39.788  1.00 28.71 ? 153 GLN H OXT 1 
ATOM   8876  N  N   . ALA I  1 1   ? 61.995  97.401  75.458  1.00 43.41 ? 1   ALA I N   1 
ATOM   8877  C  CA  . ALA I  1 1   ? 60.702  97.047  76.049  1.00 49.84 ? 1   ALA I CA  1 
ATOM   8878  C  C   . ALA I  1 1   ? 59.900  96.096  75.157  1.00 43.50 ? 1   ALA I C   1 
ATOM   8879  O  O   . ALA I  1 1   ? 59.091  96.541  74.349  1.00 38.20 ? 1   ALA I O   1 
ATOM   8880  C  CB  . ALA I  1 1   ? 59.885  98.313  76.356  1.00 45.93 ? 1   ALA I CB  1 
ATOM   8881  N  N   . THR I  1 2   ? 60.124  94.793  75.320  1.00 41.59 ? 2   THR I N   1 
ATOM   8882  C  CA  . THR I  1 2   ? 59.412  93.782  74.541  1.00 36.75 ? 2   THR I CA  1 
ATOM   8883  C  C   . THR I  1 2   ? 57.945  93.714  74.963  1.00 42.06 ? 2   THR I C   1 
ATOM   8884  O  O   . THR I  1 2   ? 57.615  93.795  76.158  1.00 39.01 ? 2   THR I O   1 
ATOM   8885  C  CB  . THR I  1 2   ? 60.058  92.375  74.699  1.00 39.22 ? 2   THR I CB  1 
ATOM   8886  O  OG1 . THR I  1 2   ? 61.471  92.464  74.503  1.00 47.67 ? 2   THR I OG1 1 
ATOM   8887  C  CG2 . THR I  1 2   ? 59.491  91.395  73.690  1.00 37.32 ? 2   THR I CG2 1 
ATOM   8888  N  N   . LYS I  1 3   ? 57.068  93.572  73.973  1.00 36.86 ? 3   LYS I N   1 
ATOM   8889  C  CA  . LYS I  1 3   ? 55.637  93.456  74.203  1.00 32.79 ? 3   LYS I CA  1 
ATOM   8890  C  C   . LYS I  1 3   ? 55.108  92.236  73.475  1.00 32.87 ? 3   LYS I C   1 
ATOM   8891  O  O   . LYS I  1 3   ? 55.569  91.913  72.379  1.00 34.50 ? 3   LYS I O   1 
ATOM   8892  C  CB  . LYS I  1 3   ? 54.901  94.689  73.681  1.00 35.09 ? 3   LYS I CB  1 
ATOM   8893  C  CG  . LYS I  1 3   ? 54.988  95.925  74.557  1.00 39.39 ? 3   LYS I CG  1 
ATOM   8894  C  CD  . LYS I  1 3   ? 53.608  96.563  74.688  1.00 41.70 ? 3   LYS I CD  1 
ATOM   8895  C  CE  . LYS I  1 3   ? 53.684  97.980  75.231  1.00 49.44 ? 3   LYS I CE  1 
ATOM   8896  N  NZ  . LYS I  1 3   ? 54.273  98.936  74.241  1.00 47.57 ? 3   LYS I NZ  1 
ATOM   8897  N  N   . ALA I  1 4   ? 54.141  91.562  74.083  1.00 26.87 ? 4   ALA I N   1 
ATOM   8898  C  CA  . ALA I  1 4   ? 53.498  90.415  73.464  1.00 27.48 ? 4   ALA I CA  1 
ATOM   8899  C  C   . ALA I  1 4   ? 51.986  90.479  73.687  1.00 33.16 ? 4   ALA I C   1 
ATOM   8900  O  O   . ALA I  1 4   ? 51.498  91.246  74.525  1.00 30.59 ? 4   ALA I O   1 
ATOM   8901  C  CB  . ALA I  1 4   ? 54.067  89.125  74.003  1.00 22.39 ? 4   ALA I CB  1 
ATOM   8902  N  N   . VAL I  1 5   ? 51.252  89.660  72.941  1.00 32.69 ? 5   VAL I N   1 
ATOM   8903  C  CA  . VAL I  1 5   ? 49.798  89.692  72.971  1.00 30.16 ? 5   VAL I CA  1 
ATOM   8904  C  C   . VAL I  1 5   ? 49.239  88.313  72.644  1.00 32.54 ? 5   VAL I C   1 
ATOM   8905  O  O   . VAL I  1 5   ? 49.887  87.490  71.992  1.00 33.02 ? 5   VAL I O   1 
ATOM   8906  C  CB  . VAL I  1 5   ? 49.225  90.744  71.973  1.00 31.25 ? 5   VAL I CB  1 
ATOM   8907  C  CG1 . VAL I  1 5   ? 49.264  90.210  70.570  1.00 28.41 ? 5   VAL I CG1 1 
ATOM   8908  C  CG2 . VAL I  1 5   ? 47.796  91.144  72.349  1.00 30.55 ? 5   VAL I CG2 1 
ATOM   8909  N  N   . CYS I  1 6   ? 48.030  88.060  73.116  1.00 30.75 ? 6   CYS I N   1 
ATOM   8910  C  CA  . CYS I  1 6   ? 47.377  86.798  72.866  1.00 32.90 ? 6   CYS I CA  1 
ATOM   8911  C  C   . CYS I  1 6   ? 45.868  86.996  72.886  1.00 36.42 ? 6   CYS I C   1 
ATOM   8912  O  O   . CYS I  1 6   ? 45.331  87.683  73.764  1.00 39.37 ? 6   CYS I O   1 
ATOM   8913  C  CB  . CYS I  1 6   ? 47.784  85.765  73.912  1.00 31.65 ? 6   CYS I CB  1 
ATOM   8914  S  SG  . CYS I  1 6   ? 46.959  84.189  73.708  1.00 34.57 ? 6   CYS I SG  1 
ATOM   8915  N  N   . VAL I  1 7   ? 45.198  86.402  71.903  1.00 36.09 ? 7   VAL I N   1 
ATOM   8916  C  CA  . VAL I  1 7   ? 43.747  86.407  71.821  1.00 33.68 ? 7   VAL I CA  1 
ATOM   8917  C  C   . VAL I  1 7   ? 43.230  85.037  72.248  1.00 37.99 ? 7   VAL I C   1 
ATOM   8918  O  O   . VAL I  1 7   ? 43.525  84.024  71.601  1.00 38.79 ? 7   VAL I O   1 
ATOM   8919  C  CB  . VAL I  1 7   ? 43.268  86.722  70.382  1.00 42.55 ? 7   VAL I CB  1 
ATOM   8920  C  CG1 . VAL I  1 7   ? 41.740  86.620  70.285  1.00 40.52 ? 7   VAL I CG1 1 
ATOM   8921  C  CG2 . VAL I  1 7   ? 43.767  88.100  69.943  1.00 38.17 ? 7   VAL I CG2 1 
ATOM   8922  N  N   . LEU I  1 8   ? 42.471  85.013  73.343  1.00 38.61 ? 8   LEU I N   1 
ATOM   8923  C  CA  . LEU I  1 8   ? 41.907  83.782  73.876  1.00 37.72 ? 8   LEU I CA  1 
ATOM   8924  C  C   . LEU I  1 8   ? 40.545  83.468  73.255  1.00 40.50 ? 8   LEU I C   1 
ATOM   8925  O  O   . LEU I  1 8   ? 39.670  84.330  73.206  1.00 42.98 ? 8   LEU I O   1 
ATOM   8926  C  CB  . LEU I  1 8   ? 41.784  83.890  75.397  1.00 44.94 ? 8   LEU I CB  1 
ATOM   8927  C  CG  . LEU I  1 8   ? 43.118  83.982  76.146  1.00 44.48 ? 8   LEU I CG  1 
ATOM   8928  C  CD1 . LEU I  1 8   ? 42.912  84.476  77.570  1.00 43.91 ? 8   LEU I CD1 1 
ATOM   8929  C  CD2 . LEU I  1 8   ? 43.818  82.625  76.143  1.00 37.60 ? 8   LEU I CD2 1 
ATOM   8930  N  N   . LYS I  1 9   ? 40.378  82.231  72.789  1.00 36.65 ? 9   LYS I N   1 
ATOM   8931  C  CA  . LYS I  1 9   ? 39.153  81.801  72.127  1.00 40.61 ? 9   LYS I CA  1 
ATOM   8932  C  C   . LYS I  1 9   ? 38.985  80.288  72.190  1.00 45.76 ? 9   LYS I C   1 
ATOM   8933  O  O   . LYS I  1 9   ? 39.975  79.550  72.241  1.00 39.48 ? 9   LYS I O   1 
ATOM   8934  C  CB  . LYS I  1 9   ? 39.143  82.248  70.658  1.00 47.01 ? 9   LYS I CB  1 
ATOM   8935  C  CG  . LYS I  1 9   ? 38.378  83.535  70.395  1.00 49.13 ? 9   LYS I CG  1 
ATOM   8936  C  CD  . LYS I  1 9   ? 38.171  83.767  68.902  1.00 55.36 ? 9   LYS I CD  1 
ATOM   8937  C  CE  . LYS I  1 9   ? 37.540  85.127  68.623  1.00 60.68 ? 9   LYS I CE  1 
ATOM   8938  N  NZ  . LYS I  1 9   ? 38.406  86.262  69.071  1.00 53.68 ? 9   LYS I NZ  1 
ATOM   8939  N  N   . GLY I  1 10  ? 37.730  79.834  72.174  1.00 51.34 ? 10  GLY I N   1 
ATOM   8940  C  CA  . GLY I  1 10  ? 37.410  78.412  72.175  1.00 57.81 ? 10  GLY I CA  1 
ATOM   8941  C  C   . GLY I  1 10  ? 35.991  78.086  71.715  1.00 60.13 ? 10  GLY I C   1 
ATOM   8942  O  O   . GLY I  1 10  ? 35.359  78.887  71.017  1.00 53.00 ? 10  GLY I O   1 
ATOM   8943  N  N   . ASP I  1 11  ? 35.497  76.906  72.101  1.00 60.48 ? 11  ASP I N   1 
ATOM   8944  C  CA  . ASP I  1 11  ? 34.133  76.473  71.769  1.00 60.38 ? 11  ASP I CA  1 
ATOM   8945  C  C   . ASP I  1 11  ? 33.153  76.751  72.909  1.00 58.21 ? 11  ASP I C   1 
ATOM   8946  O  O   . ASP I  1 11  ? 32.706  75.838  73.604  1.00 61.98 ? 11  ASP I O   1 
ATOM   8947  C  CB  . ASP I  1 11  ? 34.093  74.981  71.433  1.00 60.69 ? 11  ASP I CB  1 
ATOM   8948  C  CG  . ASP I  1 11  ? 35.254  74.544  70.571  1.00 63.86 ? 11  ASP I CG  1 
ATOM   8949  O  OD1 . ASP I  1 11  ? 35.947  75.418  70.009  1.00 66.15 ? 11  ASP I OD1 1 
ATOM   8950  O  OD2 . ASP I  1 11  ? 35.472  73.321  70.454  1.00 67.64 ? 11  ASP I OD2 1 
ATOM   8951  N  N   . GLY I  1 12  ? 32.822  78.018  73.099  1.00 51.04 ? 12  GLY I N   1 
ATOM   8952  C  CA  . GLY I  1 12  ? 31.886  78.396  74.130  1.00 49.11 ? 12  GLY I CA  1 
ATOM   8953  C  C   . GLY I  1 12  ? 31.871  79.899  74.253  1.00 53.20 ? 12  GLY I C   1 
ATOM   8954  O  O   . GLY I  1 12  ? 32.259  80.602  73.322  1.00 50.90 ? 12  GLY I O   1 
ATOM   8955  N  N   . PRO I  1 13  ? 31.431  80.403  75.411  1.00 57.26 ? 13  PRO I N   1 
ATOM   8956  C  CA  . PRO I  1 13  ? 31.354  81.847  75.653  1.00 54.15 ? 13  PRO I CA  1 
ATOM   8957  C  C   . PRO I  1 13  ? 32.685  82.451  76.126  1.00 51.83 ? 13  PRO I C   1 
ATOM   8958  O  O   . PRO I  1 13  ? 32.783  83.675  76.244  1.00 47.35 ? 13  PRO I O   1 
ATOM   8959  C  CB  . PRO I  1 13  ? 30.298  81.946  76.758  1.00 54.84 ? 13  PRO I CB  1 
ATOM   8960  C  CG  . PRO I  1 13  ? 30.473  80.675  77.538  1.00 55.77 ? 13  PRO I CG  1 
ATOM   8961  C  CD  . PRO I  1 13  ? 30.911  79.617  76.546  1.00 54.85 ? 13  PRO I CD  1 
ATOM   8962  N  N   . VAL I  1 14  ? 33.690  81.614  76.389  1.00 54.98 ? 14  VAL I N   1 
ATOM   8963  C  CA  . VAL I  1 14  ? 34.962  82.112  76.914  1.00 52.76 ? 14  VAL I CA  1 
ATOM   8964  C  C   . VAL I  1 14  ? 35.840  82.724  75.820  1.00 51.82 ? 14  VAL I C   1 
ATOM   8965  O  O   . VAL I  1 14  ? 36.058  82.129  74.763  1.00 51.86 ? 14  VAL I O   1 
ATOM   8966  C  CB  . VAL I  1 14  ? 35.734  81.046  77.720  1.00 55.46 ? 14  VAL I CB  1 
ATOM   8967  C  CG1 . VAL I  1 14  ? 36.922  81.688  78.426  1.00 47.18 ? 14  VAL I CG1 1 
ATOM   8968  C  CG2 . VAL I  1 14  ? 34.815  80.386  78.737  1.00 49.88 ? 14  VAL I CG2 1 
ATOM   8969  N  N   . GLN I  1 15  ? 36.346  83.921  76.107  1.00 52.12 ? 15  GLN I N   1 
ATOM   8970  C  CA  . GLN I  1 15  ? 36.904  84.806  75.100  1.00 53.31 ? 15  GLN I CA  1 
ATOM   8971  C  C   . GLN I  1 15  ? 37.628  85.947  75.805  1.00 56.62 ? 15  GLN I C   1 
ATOM   8972  O  O   . GLN I  1 15  ? 37.132  86.460  76.816  1.00 48.54 ? 15  GLN I O   1 
ATOM   8973  C  CB  . GLN I  1 15  ? 35.758  85.375  74.267  1.00 54.48 ? 15  GLN I CB  1 
ATOM   8974  C  CG  . GLN I  1 15  ? 36.154  86.459  73.299  1.00 56.99 ? 15  GLN I CG  1 
ATOM   8975  C  CD  . GLN I  1 15  ? 35.886  86.053  71.861  1.00 67.74 ? 15  GLN I CD  1 
ATOM   8976  O  OE1 . GLN I  1 15  ? 35.408  84.941  71.596  1.00 61.21 ? 15  GLN I OE1 1 
ATOM   8977  N  NE2 . GLN I  1 15  ? 36.190  86.950  70.922  1.00 65.96 ? 15  GLN I NE2 1 
ATOM   8978  N  N   . GLY I  1 16  ? 38.791  86.347  75.288  1.00 48.72 ? 16  GLY I N   1 
ATOM   8979  C  CA  . GLY I  1 16  ? 39.529  87.444  75.899  1.00 46.21 ? 16  GLY I CA  1 
ATOM   8980  C  C   . GLY I  1 16  ? 40.854  87.845  75.273  1.00 43.47 ? 16  GLY I C   1 
ATOM   8981  O  O   . GLY I  1 16  ? 41.408  87.142  74.426  1.00 42.41 ? 16  GLY I O   1 
ATOM   8982  N  N   . ILE I  1 17  ? 41.361  88.995  75.703  1.00 40.57 ? 17  ILE I N   1 
ATOM   8983  C  CA  . ILE I  1 17  ? 42.630  89.519  75.215  1.00 38.96 ? 17  ILE I CA  1 
ATOM   8984  C  C   . ILE I  1 17  ? 43.585  89.760  76.379  1.00 40.13 ? 17  ILE I C   1 
ATOM   8985  O  O   . ILE I  1 17  ? 43.264  90.521  77.301  1.00 41.44 ? 17  ILE I O   1 
ATOM   8986  C  CB  . ILE I  1 17  ? 42.450  90.874  74.488  1.00 41.84 ? 17  ILE I CB  1 
ATOM   8987  C  CG1 . ILE I  1 17  ? 41.495  90.746  73.306  1.00 35.71 ? 17  ILE I CG1 1 
ATOM   8988  C  CG2 . ILE I  1 17  ? 43.806  91.448  74.037  1.00 36.87 ? 17  ILE I CG2 1 
ATOM   8989  C  CD1 . ILE I  1 17  ? 41.301  92.056  72.568  1.00 40.40 ? 17  ILE I CD1 1 
ATOM   8990  N  N   . ILE I  1 18  ? 44.756  89.129  76.321  1.00 34.52 ? 18  ILE I N   1 
ATOM   8991  C  CA  . ILE I  1 18  ? 45.800  89.312  77.329  1.00 34.96 ? 18  ILE I CA  1 
ATOM   8992  C  C   . ILE I  1 18  ? 47.036  90.005  76.737  1.00 36.28 ? 18  ILE I C   1 
ATOM   8993  O  O   . ILE I  1 18  ? 47.484  89.648  75.644  1.00 33.44 ? 18  ILE I O   1 
ATOM   8994  C  CB  . ILE I  1 18  ? 46.223  87.965  77.962  1.00 33.34 ? 18  ILE I CB  1 
ATOM   8995  C  CG1 . ILE I  1 18  ? 45.003  87.218  78.520  1.00 36.78 ? 18  ILE I CG1 1 
ATOM   8996  C  CG2 . ILE I  1 18  ? 47.252  88.191  79.066  1.00 36.68 ? 18  ILE I CG2 1 
ATOM   8997  C  CD1 . ILE I  1 18  ? 44.306  87.930  79.680  1.00 36.22 ? 18  ILE I CD1 1 
ATOM   8998  N  N   . ASN I  1 19  ? 47.562  91.000  77.455  1.00 29.83 ? 19  ASN I N   1 
ATOM   8999  C  CA  . ASN I  1 19  ? 48.768  91.714  77.058  1.00 29.98 ? 19  ASN I CA  1 
ATOM   9000  C  C   . ASN I  1 19  ? 49.950  91.346  77.933  1.00 34.17 ? 19  ASN I C   1 
ATOM   9001  O  O   . ASN I  1 19  ? 49.775  91.030  79.106  1.00 36.66 ? 19  ASN I O   1 
ATOM   9002  C  CB  . ASN I  1 19  ? 48.573  93.222  77.168  1.00 34.24 ? 19  ASN I CB  1 
ATOM   9003  C  CG  . ASN I  1 19  ? 47.336  93.703  76.469  1.00 37.17 ? 19  ASN I CG  1 
ATOM   9004  O  OD1 . ASN I  1 19  ? 47.296  93.769  75.243  1.00 38.14 ? 19  ASN I OD1 1 
ATOM   9005  N  ND2 . ASN I  1 19  ? 46.317  94.062  77.245  1.00 37.49 ? 19  ASN I ND2 1 
ATOM   9006  N  N   . PHE I  1 20  ? 51.152  91.417  77.366  1.00 33.54 ? 20  PHE I N   1 
ATOM   9007  C  CA  . PHE I  1 20  ? 52.384  91.142  78.098  1.00 30.09 ? 20  PHE I CA  1 
ATOM   9008  C  C   . PHE I  1 20  ? 53.340  92.312  77.887  1.00 33.24 ? 20  PHE I C   1 
ATOM   9009  O  O   . PHE I  1 20  ? 53.435  92.847  76.782  1.00 33.61 ? 20  PHE I O   1 
ATOM   9010  C  CB  . PHE I  1 20  ? 53.064  89.861  77.598  1.00 26.00 ? 20  PHE I CB  1 
ATOM   9011  C  CG  . PHE I  1 20  ? 52.225  88.611  77.720  1.00 27.02 ? 20  PHE I CG  1 
ATOM   9012  C  CD1 . PHE I  1 20  ? 51.140  88.389  76.879  1.00 29.46 ? 20  PHE I CD1 1 
ATOM   9013  C  CD2 . PHE I  1 20  ? 52.570  87.621  78.630  1.00 30.20 ? 20  PHE I CD2 1 
ATOM   9014  C  CE1 . PHE I  1 20  ? 50.393  87.219  76.974  1.00 31.12 ? 20  PHE I CE1 1 
ATOM   9015  C  CE2 . PHE I  1 20  ? 51.836  86.451  78.729  1.00 26.59 ? 20  PHE I CE2 1 
ATOM   9016  C  CZ  . PHE I  1 20  ? 50.747  86.247  77.897  1.00 28.98 ? 20  PHE I CZ  1 
ATOM   9017  N  N   . GLU I  1 21  ? 54.050  92.714  78.935  1.00 32.28 ? 21  GLU I N   1 
ATOM   9018  C  CA  . GLU I  1 21  ? 55.066  93.750  78.783  1.00 32.16 ? 21  GLU I CA  1 
ATOM   9019  C  C   . GLU I  1 21  ? 56.239  93.543  79.729  1.00 34.43 ? 21  GLU I C   1 
ATOM   9020  O  O   . GLU I  1 21  ? 56.079  93.554  80.950  1.00 40.75 ? 21  GLU I O   1 
ATOM   9021  C  CB  . GLU I  1 21  ? 54.476  95.147  78.956  1.00 32.01 ? 21  GLU I CB  1 
ATOM   9022  C  CG  . GLU I  1 21  ? 55.479  96.269  78.760  1.00 35.50 ? 21  GLU I CG  1 
ATOM   9023  C  CD  . GLU I  1 21  ? 54.822  97.636  78.710  1.00 46.60 ? 21  GLU I CD  1 
ATOM   9024  O  OE1 . GLU I  1 21  ? 55.551  98.649  78.772  1.00 53.08 ? 21  GLU I OE1 1 
ATOM   9025  O  OE2 . GLU I  1 21  ? 53.575  97.698  78.601  1.00 49.91 ? 21  GLU I OE2 1 
ATOM   9026  N  N   . GLN I  1 22  ? 57.417  93.356  79.144  1.00 32.12 ? 22  GLN I N   1 
ATOM   9027  C  CA  . GLN I  1 22  ? 58.637  93.118  79.889  1.00 32.27 ? 22  GLN I CA  1 
ATOM   9028  C  C   . GLN I  1 22  ? 59.626  94.222  79.559  1.00 39.32 ? 22  GLN I C   1 
ATOM   9029  O  O   . GLN I  1 22  ? 60.289  94.188  78.522  1.00 37.18 ? 22  GLN I O   1 
ATOM   9030  C  CB  . GLN I  1 22  ? 59.216  91.761  79.517  1.00 30.72 ? 22  GLN I CB  1 
ATOM   9031  C  CG  . GLN I  1 22  ? 60.375  91.358  80.373  1.00 33.61 ? 22  GLN I CG  1 
ATOM   9032  C  CD  . GLN I  1 22  ? 60.936  89.998  80.006  1.00 33.49 ? 22  GLN I CD  1 
ATOM   9033  O  OE1 . GLN I  1 22  ? 60.614  89.437  78.956  1.00 34.50 ? 22  GLN I OE1 1 
ATOM   9034  N  NE2 . GLN I  1 22  ? 61.778  89.457  80.876  1.00 31.70 ? 22  GLN I NE2 1 
ATOM   9035  N  N   . LYS I  1 23  ? 59.721  95.213  80.439  1.00 42.38 ? 23  LYS I N   1 
ATOM   9036  C  CA  . LYS I  1 23  ? 60.528  96.393  80.148  1.00 43.00 ? 23  LYS I CA  1 
ATOM   9037  C  C   . LYS I  1 23  ? 62.031  96.086  80.118  1.00 40.57 ? 23  LYS I C   1 
ATOM   9038  O  O   . LYS I  1 23  ? 62.791  96.733  79.403  1.00 39.90 ? 23  LYS I O   1 
ATOM   9039  C  CB  . LYS I  1 23  ? 60.193  97.532  81.122  1.00 48.51 ? 23  LYS I CB  1 
ATOM   9040  C  CG  . LYS I  1 23  ? 58.784  98.098  80.938  1.00 46.70 ? 23  LYS I CG  1 
ATOM   9041  C  CD  . LYS I  1 23  ? 58.473  99.230  81.923  1.00 56.34 ? 23  LYS I CD  1 
ATOM   9042  C  CE  . LYS I  1 23  ? 59.184  100.523 81.544  1.00 57.40 ? 23  LYS I CE  1 
ATOM   9043  N  NZ  . LYS I  1 23  ? 58.862  100.948 80.144  1.00 58.97 ? 23  LYS I NZ  1 
ATOM   9044  N  N   . GLU I  1 24  ? 62.446  95.079  80.879  1.00 39.22 ? 24  GLU I N   1 
ATOM   9045  C  CA  . GLU I  1 24  ? 63.846  94.661  80.905  1.00 40.69 ? 24  GLU I CA  1 
ATOM   9046  C  C   . GLU I  1 24  ? 63.962  93.173  80.623  1.00 37.69 ? 24  GLU I C   1 
ATOM   9047  O  O   . GLU I  1 24  ? 63.186  92.374  81.158  1.00 35.23 ? 24  GLU I O   1 
ATOM   9048  C  CB  . GLU I  1 24  ? 64.491  94.978  82.264  1.00 37.06 ? 24  GLU I CB  1 
ATOM   9049  C  CG  . GLU I  1 24  ? 65.512  96.106  82.220  1.00 47.54 ? 24  GLU I CG  1 
ATOM   9050  C  CD  . GLU I  1 24  ? 64.867  97.471  82.054  1.00 49.63 ? 24  GLU I CD  1 
ATOM   9051  O  OE1 . GLU I  1 24  ? 63.658  97.602  82.344  1.00 48.72 ? 24  GLU I OE1 1 
ATOM   9052  O  OE2 . GLU I  1 24  ? 65.570  98.412  81.635  1.00 53.10 ? 24  GLU I OE2 1 
ATOM   9053  N  N   . SER I  1 25  ? 64.943  92.803  79.803  1.00 37.91 ? 25  SER I N   1 
ATOM   9054  C  CA  . SER I  1 25  ? 65.126  91.406  79.409  1.00 38.12 ? 25  SER I CA  1 
ATOM   9055  C  C   . SER I  1 25  ? 65.302  90.483  80.613  1.00 33.16 ? 25  SER I C   1 
ATOM   9056  O  O   . SER I  1 25  ? 64.850  89.340  80.595  1.00 31.29 ? 25  SER I O   1 
ATOM   9057  C  CB  . SER I  1 25  ? 66.290  91.257  78.412  1.00 39.27 ? 25  SER I CB  1 
ATOM   9058  O  OG  . SER I  1 25  ? 67.511  91.776  78.923  1.00 38.73 ? 25  SER I OG  1 
ATOM   9059  N  N   . ASN I  1 26  ? 65.943  90.994  81.662  1.00 36.74 ? 26  ASN I N   1 
ATOM   9060  C  CA  . ASN I  1 26  ? 66.099  90.242  82.910  1.00 38.61 ? 26  ASN I CA  1 
ATOM   9061  C  C   . ASN I  1 26  ? 65.180  90.773  84.002  1.00 40.88 ? 26  ASN I C   1 
ATOM   9062  O  O   . ASN I  1 26  ? 65.462  90.610  85.192  1.00 39.27 ? 26  ASN I O   1 
ATOM   9063  C  CB  . ASN I  1 26  ? 67.547  90.279  83.408  1.00 37.61 ? 26  ASN I CB  1 
ATOM   9064  C  CG  . ASN I  1 26  ? 67.965  91.661  83.878  1.00 40.19 ? 26  ASN I CG  1 
ATOM   9065  O  OD1 . ASN I  1 26  ? 67.454  92.676  83.388  1.00 35.72 ? 26  ASN I OD1 1 
ATOM   9066  N  ND2 . ASN I  1 26  ? 68.892  91.709  84.840  1.00 37.43 ? 26  ASN I ND2 1 
ATOM   9067  N  N   . GLY I  1 27  ? 64.098  91.432  83.592  1.00 40.82 ? 27  GLY I N   1 
ATOM   9068  C  CA  . GLY I  1 27  ? 63.116  91.966  84.522  1.00 40.95 ? 27  GLY I CA  1 
ATOM   9069  C  C   . GLY I  1 27  ? 61.809  91.201  84.423  1.00 40.58 ? 27  GLY I C   1 
ATOM   9070  O  O   . GLY I  1 27  ? 61.655  90.357  83.539  1.00 40.75 ? 27  GLY I O   1 
ATOM   9071  N  N   . PRO I  1 28  ? 60.847  91.501  85.313  1.00 40.63 ? 28  PRO I N   1 
ATOM   9072  C  CA  . PRO I  1 28  ? 59.626  90.689  85.316  1.00 39.73 ? 28  PRO I CA  1 
ATOM   9073  C  C   . PRO I  1 28  ? 58.711  91.025  84.135  1.00 35.12 ? 28  PRO I C   1 
ATOM   9074  O  O   . PRO I  1 28  ? 58.997  91.963  83.384  1.00 35.70 ? 28  PRO I O   1 
ATOM   9075  C  CB  . PRO I  1 28  ? 58.955  91.062  86.646  1.00 34.44 ? 28  PRO I CB  1 
ATOM   9076  C  CG  . PRO I  1 28  ? 59.703  92.278  87.174  1.00 36.63 ? 28  PRO I CG  1 
ATOM   9077  C  CD  . PRO I  1 28  ? 60.695  92.710  86.136  1.00 36.93 ? 28  PRO I CD  1 
ATOM   9078  N  N   . VAL I  1 29  ? 57.637  90.255  83.973  1.00 34.68 ? 29  VAL I N   1 
ATOM   9079  C  CA  . VAL I  1 29  ? 56.650  90.496  82.919  1.00 33.06 ? 29  VAL I CA  1 
ATOM   9080  C  C   . VAL I  1 29  ? 55.255  90.800  83.478  1.00 35.61 ? 29  VAL I C   1 
ATOM   9081  O  O   . VAL I  1 29  ? 54.652  89.974  84.175  1.00 33.62 ? 29  VAL I O   1 
ATOM   9082  C  CB  . VAL I  1 29  ? 56.526  89.284  81.981  1.00 29.47 ? 29  VAL I CB  1 
ATOM   9083  C  CG1 . VAL I  1 29  ? 55.554  89.594  80.847  1.00 25.49 ? 29  VAL I CG1 1 
ATOM   9084  C  CG2 . VAL I  1 29  ? 57.901  88.883  81.445  1.00 32.79 ? 29  VAL I CG2 1 
ATOM   9085  N  N   . LYS I  1 30  ? 54.738  91.982  83.160  1.00 32.97 ? 30  LYS I N   1 
ATOM   9086  C  CA  . LYS I  1 30  ? 53.350  92.289  83.455  1.00 33.56 ? 30  LYS I CA  1 
ATOM   9087  C  C   . LYS I  1 30  ? 52.436  91.529  82.505  1.00 39.58 ? 30  LYS I C   1 
ATOM   9088  O  O   . LYS I  1 30  ? 52.616  91.580  81.284  1.00 39.40 ? 30  LYS I O   1 
ATOM   9089  C  CB  . LYS I  1 30  ? 53.093  93.790  83.325  1.00 39.03 ? 30  LYS I CB  1 
ATOM   9090  C  CG  . LYS I  1 30  ? 53.756  94.620  84.410  1.00 43.44 ? 30  LYS I CG  1 
ATOM   9091  C  CD  . LYS I  1 30  ? 53.670  96.102  84.095  1.00 48.30 ? 30  LYS I CD  1 
ATOM   9092  C  CE  . LYS I  1 30  ? 54.185  96.926  85.257  1.00 49.69 ? 30  LYS I CE  1 
ATOM   9093  N  NZ  . LYS I  1 30  ? 53.386  96.653  86.488  1.00 46.27 ? 30  LYS I NZ  1 
ATOM   9094  N  N   . VAL I  1 31  ? 51.468  90.817  83.074  1.00 39.26 ? 31  VAL I N   1 
ATOM   9095  C  CA  . VAL I  1 31  ? 50.423  90.151  82.315  1.00 33.25 ? 31  VAL I CA  1 
ATOM   9096  C  C   . VAL I  1 31  ? 49.071  90.769  82.699  1.00 44.08 ? 31  VAL I C   1 
ATOM   9097  O  O   . VAL I  1 31  ? 48.508  90.454  83.764  1.00 41.09 ? 31  VAL I O   1 
ATOM   9098  C  CB  . VAL I  1 31  ? 50.382  88.654  82.655  1.00 32.65 ? 31  VAL I CB  1 
ATOM   9099  C  CG1 . VAL I  1 31  ? 49.238  87.969  81.932  1.00 27.68 ? 31  VAL I CG1 1 
ATOM   9100  C  CG2 . VAL I  1 31  ? 51.716  87.989  82.360  1.00 30.85 ? 31  VAL I CG2 1 
ATOM   9101  N  N   . TRP I  1 32  ? 48.543  91.653  81.856  1.00 40.18 ? 32  TRP I N   1 
ATOM   9102  C  CA  . TRP I  1 32  ? 47.233  92.247  82.146  1.00 42.12 ? 32  TRP I CA  1 
ATOM   9103  C  C   . TRP I  1 32  ? 46.256  92.066  80.985  1.00 39.00 ? 32  TRP I C   1 
ATOM   9104  O  O   . TRP I  1 32  ? 46.660  91.713  79.879  1.00 36.03 ? 32  TRP I O   1 
ATOM   9105  C  CB  . TRP I  1 32  ? 47.363  93.733  82.512  1.00 37.88 ? 32  TRP I CB  1 
ATOM   9106  C  CG  . TRP I  1 32  ? 47.462  94.662  81.320  1.00 41.35 ? 32  TRP I CG  1 
ATOM   9107  C  CD1 . TRP I  1 32  ? 46.435  95.339  80.715  1.00 48.94 ? 32  TRP I CD1 1 
ATOM   9108  C  CD2 . TRP I  1 32  ? 48.648  95.017  80.600  1.00 41.34 ? 32  TRP I CD2 1 
ATOM   9109  N  NE1 . TRP I  1 32  ? 46.911  96.090  79.664  1.00 45.35 ? 32  TRP I NE1 1 
ATOM   9110  C  CE2 . TRP I  1 32  ? 48.266  95.912  79.574  1.00 41.27 ? 32  TRP I CE2 1 
ATOM   9111  C  CE3 . TRP I  1 32  ? 49.997  94.668  80.721  1.00 41.96 ? 32  TRP I CE3 1 
ATOM   9112  C  CZ2 . TRP I  1 32  ? 49.187  96.461  78.677  1.00 46.47 ? 32  TRP I CZ2 1 
ATOM   9113  C  CZ3 . TRP I  1 32  ? 50.915  95.218  79.821  1.00 44.02 ? 32  TRP I CZ3 1 
ATOM   9114  C  CH2 . TRP I  1 32  ? 50.504  96.106  78.819  1.00 43.19 ? 32  TRP I CH2 1 
ATOM   9115  N  N   . GLY I  1 33  ? 44.973  92.314  81.248  1.00 39.69 ? 33  GLY I N   1 
ATOM   9116  C  CA  . GLY I  1 33  ? 43.926  92.189  80.242  1.00 42.46 ? 33  GLY I CA  1 
ATOM   9117  C  C   . GLY I  1 33  ? 42.643  91.601  80.806  1.00 43.46 ? 33  GLY I C   1 
ATOM   9118  O  O   . GLY I  1 33  ? 42.568  91.303  81.997  1.00 47.56 ? 33  GLY I O   1 
ATOM   9119  N  N   . SER I  1 34  ? 41.634  91.418  79.959  1.00 42.73 ? 34  SER I N   1 
ATOM   9120  C  CA  . SER I  1 34  ? 40.345  90.912  80.431  1.00 44.11 ? 34  SER I CA  1 
ATOM   9121  C  C   . SER I  1 34  ? 39.887  89.647  79.714  1.00 44.97 ? 34  SER I C   1 
ATOM   9122  O  O   . SER I  1 34  ? 40.103  89.487  78.510  1.00 51.67 ? 34  SER I O   1 
ATOM   9123  C  CB  . SER I  1 34  ? 39.268  91.990  80.314  1.00 49.48 ? 34  SER I CB  1 
ATOM   9124  O  OG  . SER I  1 34  ? 38.210  91.735  81.225  1.00 55.79 ? 34  SER I OG  1 
ATOM   9125  N  N   . ILE I  1 35  ? 39.257  88.748  80.466  1.00 40.65 ? 35  ILE I N   1 
ATOM   9126  C  CA  . ILE I  1 35  ? 38.711  87.508  79.925  1.00 43.83 ? 35  ILE I CA  1 
ATOM   9127  C  C   . ILE I  1 35  ? 37.248  87.417  80.361  1.00 50.44 ? 35  ILE I C   1 
ATOM   9128  O  O   . ILE I  1 35  ? 36.940  87.662  81.530  1.00 49.37 ? 35  ILE I O   1 
ATOM   9129  C  CB  . ILE I  1 35  ? 39.490  86.297  80.463  1.00 45.02 ? 35  ILE I CB  1 
ATOM   9130  C  CG1 . ILE I  1 35  ? 40.993  86.531  80.298  1.00 39.68 ? 35  ILE I CG1 1 
ATOM   9131  C  CG2 . ILE I  1 35  ? 39.033  85.004  79.789  1.00 41.68 ? 35  ILE I CG2 1 
ATOM   9132  C  CD1 . ILE I  1 35  ? 41.853  85.523  81.022  1.00 42.61 ? 35  ILE I CD1 1 
ATOM   9133  N  N   . LYS I  1 36  ? 36.345  87.083  79.435  1.00 49.84 ? 36  LYS I N   1 
ATOM   9134  C  CA  . LYS I  1 36  ? 34.909  87.108  79.736  1.00 52.81 ? 36  LYS I CA  1 
ATOM   9135  C  C   . LYS I  1 36  ? 34.140  85.831  79.368  1.00 55.10 ? 36  LYS I C   1 
ATOM   9136  O  O   . LYS I  1 36  ? 34.537  85.089  78.472  1.00 52.90 ? 36  LYS I O   1 
ATOM   9137  C  CB  . LYS I  1 36  ? 34.242  88.344  79.114  1.00 53.26 ? 36  LYS I CB  1 
ATOM   9138  C  CG  . LYS I  1 36  ? 34.051  88.292  77.611  1.00 52.87 ? 36  LYS I CG  1 
ATOM   9139  C  CD  . LYS I  1 36  ? 33.521  89.622  77.087  1.00 54.56 ? 36  LYS I CD  1 
ATOM   9140  C  CE  . LYS I  1 36  ? 33.332  89.600  75.572  1.00 58.44 ? 36  LYS I CE  1 
ATOM   9141  N  NZ  . LYS I  1 36  ? 32.929  90.934  75.035  1.00 53.22 ? 36  LYS I NZ  1 
ATOM   9142  N  N   . GLY I  1 37  ? 33.040  85.577  80.078  1.00 58.28 ? 37  GLY I N   1 
ATOM   9143  C  CA  . GLY I  1 37  ? 32.223  84.397  79.838  1.00 48.75 ? 37  GLY I CA  1 
ATOM   9144  C  C   . GLY I  1 37  ? 32.661  83.190  80.646  1.00 51.65 ? 37  GLY I C   1 
ATOM   9145  O  O   . GLY I  1 37  ? 32.520  82.046  80.208  1.00 52.82 ? 37  GLY I O   1 
ATOM   9146  N  N   . LEU I  1 38  ? 33.199  83.452  81.834  1.00 55.56 ? 38  LEU I N   1 
ATOM   9147  C  CA  . LEU I  1 38  ? 33.648  82.398  82.741  1.00 57.86 ? 38  LEU I CA  1 
ATOM   9148  C  C   . LEU I  1 38  ? 32.683  82.267  83.909  1.00 56.45 ? 38  LEU I C   1 
ATOM   9149  O  O   . LEU I  1 38  ? 32.132  83.267  84.373  1.00 54.36 ? 38  LEU I O   1 
ATOM   9150  C  CB  . LEU I  1 38  ? 35.035  82.735  83.298  1.00 57.86 ? 38  LEU I CB  1 
ATOM   9151  C  CG  . LEU I  1 38  ? 36.247  82.783  82.365  1.00 55.61 ? 38  LEU I CG  1 
ATOM   9152  C  CD1 . LEU I  1 38  ? 37.267  83.802  82.879  1.00 51.76 ? 38  LEU I CD1 1 
ATOM   9153  C  CD2 . LEU I  1 38  ? 36.868  81.392  82.224  1.00 48.05 ? 38  LEU I CD2 1 
ATOM   9154  N  N   . THR I  1 39  ? 32.483  81.040  84.387  1.00 58.68 ? 39  THR I N   1 
ATOM   9155  C  CA  . THR I  1 39  ? 31.779  80.834  85.652  1.00 61.95 ? 39  THR I CA  1 
ATOM   9156  C  C   . THR I  1 39  ? 32.568  81.556  86.726  1.00 61.97 ? 39  THR I C   1 
ATOM   9157  O  O   . THR I  1 39  ? 33.800  81.511  86.718  1.00 62.97 ? 39  THR I O   1 
ATOM   9158  C  CB  . THR I  1 39  ? 31.656  79.338  86.033  1.00 59.57 ? 39  THR I CB  1 
ATOM   9159  O  OG1 . THR I  1 39  ? 32.909  78.674  85.828  1.00 57.92 ? 39  THR I OG1 1 
ATOM   9160  C  CG2 . THR I  1 39  ? 30.584  78.653  85.196  1.00 60.28 ? 39  THR I CG2 1 
ATOM   9161  N  N   . GLU I  1 40  ? 31.868  82.239  87.630  1.00 62.18 ? 40  GLU I N   1 
ATOM   9162  C  CA  . GLU I  1 40  ? 32.532  83.026  88.668  1.00 63.00 ? 40  GLU I CA  1 
ATOM   9163  C  C   . GLU I  1 40  ? 33.470  82.167  89.512  1.00 61.26 ? 40  GLU I C   1 
ATOM   9164  O  O   . GLU I  1 40  ? 33.286  80.950  89.630  1.00 59.52 ? 40  GLU I O   1 
ATOM   9165  C  CB  . GLU I  1 40  ? 31.517  83.759  89.550  1.00 66.78 ? 40  GLU I CB  1 
ATOM   9166  C  CG  . GLU I  1 40  ? 30.439  82.875  90.158  1.00 69.06 ? 40  GLU I CG  1 
ATOM   9167  C  CD  . GLU I  1 40  ? 29.485  83.652  91.053  1.00 75.17 ? 40  GLU I CD  1 
ATOM   9168  O  OE1 . GLU I  1 40  ? 29.863  84.751  91.519  1.00 73.16 ? 40  GLU I OE1 1 
ATOM   9169  O  OE2 . GLU I  1 40  ? 28.357  83.163  91.285  1.00 82.78 ? 40  GLU I OE2 1 
ATOM   9170  N  N   . GLY I  1 41  ? 34.489  82.801  90.079  1.00 55.99 ? 41  GLY I N   1 
ATOM   9171  C  CA  . GLY I  1 41  ? 35.503  82.068  90.814  1.00 59.39 ? 41  GLY I CA  1 
ATOM   9172  C  C   . GLY I  1 41  ? 36.763  81.899  89.985  1.00 57.44 ? 41  GLY I C   1 
ATOM   9173  O  O   . GLY I  1 41  ? 36.853  82.412  88.871  1.00 55.29 ? 41  GLY I O   1 
ATOM   9174  N  N   . LEU I  1 42  ? 37.736  81.168  90.516  1.00 57.77 ? 42  LEU I N   1 
ATOM   9175  C  CA  . LEU I  1 42  ? 39.050  81.131  89.881  1.00 56.39 ? 42  LEU I CA  1 
ATOM   9176  C  C   . LEU I  1 42  ? 39.276  80.015  88.848  1.00 56.43 ? 42  LEU I C   1 
ATOM   9177  O  O   . LEU I  1 42  ? 38.720  78.913  88.954  1.00 57.66 ? 42  LEU I O   1 
ATOM   9178  C  CB  . LEU I  1 42  ? 40.183  81.199  90.922  1.00 54.69 ? 42  LEU I CB  1 
ATOM   9179  C  CG  . LEU I  1 42  ? 40.098  80.368  92.202  1.00 58.17 ? 42  LEU I CG  1 
ATOM   9180  C  CD1 . LEU I  1 42  ? 40.030  78.905  91.855  1.00 49.71 ? 42  LEU I CD1 1 
ATOM   9181  C  CD2 . LEU I  1 42  ? 41.287  80.655  93.129  1.00 51.91 ? 42  LEU I CD2 1 
ATOM   9182  N  N   . HIS I  1 43  ? 40.108  80.326  87.854  1.00 51.21 ? 43  HIS I N   1 
ATOM   9183  C  CA  . HIS I  1 43  ? 40.375  79.427  86.736  1.00 52.22 ? 43  HIS I CA  1 
ATOM   9184  C  C   . HIS I  1 43  ? 41.879  79.332  86.470  1.00 48.76 ? 43  HIS I C   1 
ATOM   9185  O  O   . HIS I  1 43  ? 42.577  80.348  86.480  1.00 40.85 ? 43  HIS I O   1 
ATOM   9186  C  CB  . HIS I  1 43  ? 39.667  79.935  85.473  1.00 53.98 ? 43  HIS I CB  1 
ATOM   9187  C  CG  . HIS I  1 43  ? 38.196  80.176  85.647  1.00 55.15 ? 43  HIS I CG  1 
ATOM   9188  N  ND1 . HIS I  1 43  ? 37.249  79.191  85.452  1.00 51.57 ? 43  HIS I ND1 1 
ATOM   9189  C  CD2 . HIS I  1 43  ? 37.509  81.296  85.982  1.00 53.98 ? 43  HIS I CD2 1 
ATOM   9190  C  CE1 . HIS I  1 43  ? 36.046  79.692  85.665  1.00 55.80 ? 43  HIS I CE1 1 
ATOM   9191  N  NE2 . HIS I  1 43  ? 36.175  80.968  85.988  1.00 57.52 ? 43  HIS I NE2 1 
ATOM   9192  N  N   . GLY I  1 44  ? 42.365  78.114  86.229  1.00 45.90 ? 44  GLY I N   1 
ATOM   9193  C  CA  . GLY I  1 44  ? 43.770  77.881  85.935  1.00 44.87 ? 44  GLY I CA  1 
ATOM   9194  C  C   . GLY I  1 44  ? 44.238  78.645  84.701  1.00 49.13 ? 44  GLY I C   1 
ATOM   9195  O  O   . GLY I  1 44  ? 43.541  78.703  83.690  1.00 45.12 ? 44  GLY I O   1 
ATOM   9196  N  N   . PHE I  1 45  ? 45.427  79.229  84.792  1.00 42.63 ? 45  PHE I N   1 
ATOM   9197  C  CA  . PHE I  1 45  ? 45.934  80.161  83.791  1.00 41.74 ? 45  PHE I CA  1 
ATOM   9198  C  C   . PHE I  1 45  ? 47.363  79.745  83.461  1.00 39.91 ? 45  PHE I C   1 
ATOM   9199  O  O   . PHE I  1 45  ? 48.300  80.059  84.203  1.00 38.28 ? 45  PHE I O   1 
ATOM   9200  C  CB  . PHE I  1 45  ? 45.884  81.581  84.372  1.00 39.12 ? 45  PHE I CB  1 
ATOM   9201  C  CG  . PHE I  1 45  ? 46.005  82.689  83.354  1.00 38.24 ? 45  PHE I CG  1 
ATOM   9202  C  CD1 . PHE I  1 45  ? 45.129  82.773  82.282  1.00 38.91 ? 45  PHE I CD1 1 
ATOM   9203  C  CD2 . PHE I  1 45  ? 46.972  83.679  83.504  1.00 39.78 ? 45  PHE I CD2 1 
ATOM   9204  C  CE1 . PHE I  1 45  ? 45.225  83.804  81.356  1.00 34.78 ? 45  PHE I CE1 1 
ATOM   9205  C  CE2 . PHE I  1 45  ? 47.081  84.720  82.579  1.00 42.27 ? 45  PHE I CE2 1 
ATOM   9206  C  CZ  . PHE I  1 45  ? 46.201  84.780  81.503  1.00 39.04 ? 45  PHE I CZ  1 
ATOM   9207  N  N   . HIS I  1 46  ? 47.520  79.007  82.364  1.00 39.79 ? 46  HIS I N   1 
ATOM   9208  C  CA  . HIS I  1 46  ? 48.811  78.416  82.014  1.00 37.36 ? 46  HIS I CA  1 
ATOM   9209  C  C   . HIS I  1 46  ? 49.357  78.797  80.636  1.00 39.06 ? 46  HIS I C   1 
ATOM   9210  O  O   . HIS I  1 46  ? 48.613  79.020  79.670  1.00 31.50 ? 46  HIS I O   1 
ATOM   9211  C  CB  . HIS I  1 46  ? 48.743  76.886  82.054  1.00 35.64 ? 46  HIS I CB  1 
ATOM   9212  C  CG  . HIS I  1 46  ? 48.006  76.339  83.228  1.00 42.58 ? 46  HIS I CG  1 
ATOM   9213  N  ND1 . HIS I  1 46  ? 46.646  76.120  83.213  1.00 46.21 ? 46  HIS I ND1 1 
ATOM   9214  C  CD2 . HIS I  1 46  ? 48.436  75.957  84.451  1.00 44.43 ? 46  HIS I CD2 1 
ATOM   9215  C  CE1 . HIS I  1 46  ? 46.269  75.623  84.376  1.00 44.39 ? 46  HIS I CE1 1 
ATOM   9216  N  NE2 . HIS I  1 46  ? 47.336  75.516  85.146  1.00 49.70 ? 46  HIS I NE2 1 
ATOM   9217  N  N   . VAL I  1 47  ? 50.679  78.823  80.549  1.00 37.50 ? 47  VAL I N   1 
ATOM   9218  C  CA  . VAL I  1 47  ? 51.335  78.779  79.258  1.00 33.67 ? 47  VAL I CA  1 
ATOM   9219  C  C   . VAL I  1 47  ? 51.664  77.326  78.921  1.00 32.26 ? 47  VAL I C   1 
ATOM   9220  O  O   . VAL I  1 47  ? 52.474  76.685  79.589  1.00 33.11 ? 47  VAL I O   1 
ATOM   9221  C  CB  . VAL I  1 47  ? 52.604  79.631  79.240  1.00 35.33 ? 47  VAL I CB  1 
ATOM   9222  C  CG1 . VAL I  1 47  ? 53.301  79.501  77.894  1.00 29.00 ? 47  VAL I CG1 1 
ATOM   9223  C  CG2 . VAL I  1 47  ? 52.260  81.099  79.555  1.00 29.96 ? 47  VAL I CG2 1 
ATOM   9224  N  N   . HIS I  1 48  ? 51.012  76.800  77.892  1.00 31.87 ? 48  HIS I N   1 
ATOM   9225  C  CA  . HIS I  1 48  ? 51.344  75.468  77.414  1.00 36.13 ? 48  HIS I CA  1 
ATOM   9226  C  C   . HIS I  1 48  ? 52.460  75.513  76.377  1.00 33.84 ? 48  HIS I C   1 
ATOM   9227  O  O   . HIS I  1 48  ? 52.768  76.568  75.830  1.00 32.41 ? 48  HIS I O   1 
ATOM   9228  C  CB  . HIS I  1 48  ? 50.115  74.750  76.884  1.00 35.33 ? 48  HIS I CB  1 
ATOM   9229  C  CG  . HIS I  1 48  ? 49.124  74.411  77.953  1.00 43.51 ? 48  HIS I CG  1 
ATOM   9230  N  ND1 . HIS I  1 48  ? 48.737  73.115  78.225  1.00 40.00 ? 48  HIS I ND1 1 
ATOM   9231  C  CD2 . HIS I  1 48  ? 48.462  75.198  78.836  1.00 37.32 ? 48  HIS I CD2 1 
ATOM   9232  C  CE1 . HIS I  1 48  ? 47.862  73.123  79.215  1.00 42.23 ? 48  HIS I CE1 1 
ATOM   9233  N  NE2 . HIS I  1 48  ? 47.678  74.373  79.602  1.00 42.69 ? 48  HIS I NE2 1 
ATOM   9234  N  N   . GLU I  1 49  ? 53.051  74.352  76.127  1.00 34.11 ? 49  GLU I N   1 
ATOM   9235  C  CA  . GLU I  1 49  ? 54.304  74.240  75.399  1.00 35.80 ? 49  GLU I CA  1 
ATOM   9236  C  C   . GLU I  1 49  ? 54.263  74.729  73.951  1.00 33.53 ? 49  GLU I C   1 
ATOM   9237  O  O   . GLU I  1 49  ? 55.154  75.466  73.512  1.00 29.37 ? 49  GLU I O   1 
ATOM   9238  C  CB  . GLU I  1 49  ? 54.780  72.795  75.429  1.00 34.76 ? 49  GLU I CB  1 
ATOM   9239  C  CG  . GLU I  1 49  ? 56.114  72.596  74.754  1.00 35.61 ? 49  GLU I CG  1 
ATOM   9240  C  CD  . GLU I  1 49  ? 56.719  71.271  75.108  1.00 36.33 ? 49  GLU I CD  1 
ATOM   9241  O  OE1 . GLU I  1 49  ? 56.010  70.468  75.746  1.00 41.66 ? 49  GLU I OE1 1 
ATOM   9242  O  OE2 . GLU I  1 49  ? 57.893  71.033  74.759  1.00 37.51 ? 49  GLU I OE2 1 
ATOM   9243  N  N   . PHE I  1 50  ? 53.224  74.312  73.230  1.00 33.22 ? 50  PHE I N   1 
ATOM   9244  C  CA  . PHE I  1 50  ? 53.133  74.516  71.786  1.00 35.65 ? 50  PHE I CA  1 
ATOM   9245  C  C   . PHE I  1 50  ? 52.101  75.542  71.386  1.00 35.89 ? 50  PHE I C   1 
ATOM   9246  O  O   . PHE I  1 50  ? 51.016  75.629  71.987  1.00 31.36 ? 50  PHE I O   1 
ATOM   9247  C  CB  . PHE I  1 50  ? 52.841  73.193  71.077  1.00 32.76 ? 50  PHE I CB  1 
ATOM   9248  C  CG  . PHE I  1 50  ? 53.818  72.123  71.420  1.00 35.14 ? 50  PHE I CG  1 
ATOM   9249  C  CD1 . PHE I  1 50  ? 55.162  72.294  71.145  1.00 35.45 ? 50  PHE I CD1 1 
ATOM   9250  C  CD2 . PHE I  1 50  ? 53.408  70.966  72.047  1.00 37.73 ? 50  PHE I CD2 1 
ATOM   9251  C  CE1 . PHE I  1 50  ? 56.075  71.324  71.472  1.00 37.88 ? 50  PHE I CE1 1 
ATOM   9252  C  CE2 . PHE I  1 50  ? 54.321  69.987  72.372  1.00 38.58 ? 50  PHE I CE2 1 
ATOM   9253  C  CZ  . PHE I  1 50  ? 55.654  70.169  72.092  1.00 38.72 ? 50  PHE I CZ  1 
ATOM   9254  N  N   . GLY I  1 51  ? 52.462  76.317  70.362  1.00 31.26 ? 51  GLY I N   1 
ATOM   9255  C  CA  . GLY I  1 51  ? 51.557  77.265  69.746  1.00 32.44 ? 51  GLY I CA  1 
ATOM   9256  C  C   . GLY I  1 51  ? 50.938  76.572  68.554  1.00 32.57 ? 51  GLY I C   1 
ATOM   9257  O  O   . GLY I  1 51  ? 50.998  77.059  67.429  1.00 31.84 ? 51  GLY I O   1 
ATOM   9258  N  N   . ASP I  1 52  ? 50.374  75.402  68.820  1.00 31.13 ? 52  ASP I N   1 
ATOM   9259  C  CA  . ASP I  1 52  ? 49.773  74.564  67.808  1.00 29.13 ? 52  ASP I CA  1 
ATOM   9260  C  C   . ASP I  1 52  ? 48.282  74.403  68.143  1.00 37.83 ? 52  ASP I C   1 
ATOM   9261  O  O   . ASP I  1 52  ? 47.905  73.706  69.096  1.00 34.65 ? 52  ASP I O   1 
ATOM   9262  C  CB  . ASP I  1 52  ? 50.493  73.221  67.788  1.00 30.57 ? 52  ASP I CB  1 
ATOM   9263  C  CG  . ASP I  1 52  ? 49.961  72.278  66.720  1.00 32.11 ? 52  ASP I CG  1 
ATOM   9264  O  OD1 . ASP I  1 52  ? 48.794  72.429  66.297  1.00 31.99 ? 52  ASP I OD1 1 
ATOM   9265  O  OD2 . ASP I  1 52  ? 50.717  71.370  66.313  1.00 33.56 ? 52  ASP I OD2 1 
ATOM   9266  N  N   . ASN I  1 53  ? 47.437  75.073  67.368  1.00 36.36 ? 53  ASN I N   1 
ATOM   9267  C  CA  . ASN I  1 53  ? 45.999  74.955  67.541  1.00 40.39 ? 53  ASN I CA  1 
ATOM   9268  C  C   . ASN I  1 53  ? 45.362  74.217  66.366  1.00 38.50 ? 53  ASN I C   1 
ATOM   9269  O  O   . ASN I  1 53  ? 44.208  74.459  66.032  1.00 37.15 ? 53  ASN I O   1 
ATOM   9270  C  CB  . ASN I  1 53  ? 45.358  76.333  67.734  1.00 38.17 ? 53  ASN I CB  1 
ATOM   9271  C  CG  . ASN I  1 53  ? 43.917  76.246  68.215  1.00 48.16 ? 53  ASN I CG  1 
ATOM   9272  O  OD1 . ASN I  1 53  ? 43.658  76.084  69.406  1.00 50.93 ? 53  ASN I OD1 1 
ATOM   9273  N  ND2 . ASN I  1 53  ? 42.971  76.345  67.283  1.00 48.66 ? 53  ASN I ND2 1 
ATOM   9274  N  N   . THR I  1 54  ? 46.128  73.325  65.740  1.00 36.51 ? 54  THR I N   1 
ATOM   9275  C  CA  . THR I  1 54  ? 45.617  72.517  64.635  1.00 35.46 ? 54  THR I CA  1 
ATOM   9276  C  C   . THR I  1 54  ? 44.454  71.645  65.112  1.00 40.50 ? 54  THR I C   1 
ATOM   9277  O  O   . THR I  1 54  ? 43.477  71.446  64.389  1.00 37.26 ? 54  THR I O   1 
ATOM   9278  C  CB  . THR I  1 54  ? 46.718  71.621  64.041  1.00 33.00 ? 54  THR I CB  1 
ATOM   9279  O  OG1 . THR I  1 54  ? 47.476  71.044  65.112  1.00 36.85 ? 54  THR I OG1 1 
ATOM   9280  C  CG2 . THR I  1 54  ? 47.667  72.442  63.179  1.00 29.83 ? 54  THR I CG2 1 
ATOM   9281  N  N   . ALA I  1 55  ? 44.573  71.123  66.331  1.00 40.64 ? 55  ALA I N   1 
ATOM   9282  C  CA  . ALA I  1 55  ? 43.502  70.352  66.954  1.00 39.27 ? 55  ALA I CA  1 
ATOM   9283  C  C   . ALA I  1 55  ? 42.976  71.106  68.163  1.00 42.51 ? 55  ALA I C   1 
ATOM   9284  O  O   . ALA I  1 55  ? 43.045  70.614  69.282  1.00 42.34 ? 55  ALA I O   1 
ATOM   9285  C  CB  . ALA I  1 55  ? 44.003  68.973  67.363  1.00 37.40 ? 55  ALA I CB  1 
ATOM   9286  N  N   . GLY I  1 56  ? 42.470  72.314  67.933  1.00 48.12 ? 56  GLY I N   1 
ATOM   9287  C  CA  . GLY I  1 56  ? 41.968  73.152  69.009  1.00 47.25 ? 56  GLY I CA  1 
ATOM   9288  C  C   . GLY I  1 56  ? 42.973  73.282  70.140  1.00 49.87 ? 56  GLY I C   1 
ATOM   9289  O  O   . GLY I  1 56  ? 44.175  73.383  69.899  1.00 46.12 ? 56  GLY I O   1 
ATOM   9290  N  N   . SER I  1 57  ? 42.487  73.252  71.377  1.00 54.29 ? 57  SER I N   1 
ATOM   9291  C  CA  . SER I  1 57  ? 43.363  73.384  72.536  1.00 44.88 ? 57  SER I CA  1 
ATOM   9292  C  C   . SER I  1 57  ? 44.128  72.097  72.853  1.00 46.01 ? 57  SER I C   1 
ATOM   9293  O  O   . SER I  1 57  ? 45.108  72.130  73.606  1.00 42.30 ? 57  SER I O   1 
ATOM   9294  C  CB  . SER I  1 57  ? 42.566  73.845  73.756  1.00 45.97 ? 57  SER I CB  1 
ATOM   9295  O  OG  . SER I  1 57  ? 42.978  75.139  74.161  1.00 48.95 ? 57  SER I OG  1 
ATOM   9296  N  N   . THR I  1 58  ? 43.710  70.972  72.273  1.00 39.21 ? 58  THR I N   1 
ATOM   9297  C  CA  . THR I  1 58  ? 44.360  69.700  72.599  1.00 43.40 ? 58  THR I CA  1 
ATOM   9298  C  C   . THR I  1 58  ? 45.790  69.521  72.046  1.00 44.34 ? 58  THR I C   1 
ATOM   9299  O  O   . THR I  1 58  ? 46.589  68.791  72.629  1.00 45.05 ? 58  THR I O   1 
ATOM   9300  C  CB  . THR I  1 58  ? 43.459  68.454  72.297  1.00 47.91 ? 58  THR I CB  1 
ATOM   9301  O  OG1 . THR I  1 58  ? 43.999  67.302  72.954  1.00 51.77 ? 58  THR I OG1 1 
ATOM   9302  C  CG2 . THR I  1 58  ? 43.377  68.155  70.826  1.00 40.15 ? 58  THR I CG2 1 
ATOM   9303  N  N   . SER I  1 59  ? 46.125  70.195  70.947  1.00 42.31 ? 59  SER I N   1 
ATOM   9304  C  CA  . SER I  1 59  ? 47.463  70.053  70.354  1.00 39.08 ? 59  SER I CA  1 
ATOM   9305  C  C   . SER I  1 59  ? 48.536  70.965  70.990  1.00 39.89 ? 59  SER I C   1 
ATOM   9306  O  O   . SER I  1 59  ? 49.723  70.896  70.628  1.00 36.47 ? 59  SER I O   1 
ATOM   9307  C  CB  . SER I  1 59  ? 47.407  70.260  68.829  1.00 39.74 ? 59  SER I CB  1 
ATOM   9308  O  OG  . SER I  1 59  ? 46.680  71.431  68.488  1.00 35.37 ? 59  SER I OG  1 
ATOM   9309  N  N   . ALA I  1 60  ? 48.113  71.800  71.940  1.00 34.38 ? 60  ALA I N   1 
ATOM   9310  C  CA  . ALA I  1 60  ? 49.009  72.741  72.620  1.00 38.80 ? 60  ALA I CA  1 
ATOM   9311  C  C   . ALA I  1 60  ? 49.963  72.100  73.647  1.00 37.80 ? 60  ALA I C   1 
ATOM   9312  O  O   . ALA I  1 60  ? 50.802  72.790  74.242  1.00 38.69 ? 60  ALA I O   1 
ATOM   9313  C  CB  . ALA I  1 60  ? 48.211  73.892  73.261  1.00 34.71 ? 60  ALA I CB  1 
ATOM   9314  N  N   . GLY I  1 61  ? 49.838  70.791  73.847  1.00 36.18 ? 61  GLY I N   1 
ATOM   9315  C  CA  . GLY I  1 61  ? 50.772  70.058  74.687  1.00 44.05 ? 61  GLY I CA  1 
ATOM   9316  C  C   . GLY I  1 61  ? 50.676  70.328  76.179  1.00 40.43 ? 61  GLY I C   1 
ATOM   9317  O  O   . GLY I  1 61  ? 49.701  70.924  76.646  1.00 39.09 ? 61  GLY I O   1 
ATOM   9318  N  N   . PRO I  1 62  ? 51.700  69.889  76.935  1.00 40.83 ? 62  PRO I N   1 
ATOM   9319  C  CA  . PRO I  1 62  ? 51.774  69.992  78.402  1.00 42.03 ? 62  PRO I CA  1 
ATOM   9320  C  C   . PRO I  1 62  ? 51.992  71.426  78.879  1.00 41.47 ? 62  PRO I C   1 
ATOM   9321  O  O   . PRO I  1 62  ? 52.048  72.353  78.064  1.00 40.56 ? 62  PRO I O   1 
ATOM   9322  C  CB  . PRO I  1 62  ? 53.015  69.156  78.753  1.00 36.95 ? 62  PRO I CB  1 
ATOM   9323  C  CG  . PRO I  1 62  ? 53.345  68.374  77.519  1.00 42.43 ? 62  PRO I CG  1 
ATOM   9324  C  CD  . PRO I  1 62  ? 52.880  69.212  76.376  1.00 42.50 ? 62  PRO I CD  1 
ATOM   9325  N  N   . HIS I  1 63  ? 52.132  71.606  80.190  1.00 41.17 ? 63  HIS I N   1 
ATOM   9326  C  CA  . HIS I  1 63  ? 52.485  72.919  80.735  1.00 42.54 ? 63  HIS I CA  1 
ATOM   9327  C  C   . HIS I  1 63  ? 53.916  73.275  80.307  1.00 39.38 ? 63  HIS I C   1 
ATOM   9328  O  O   . HIS I  1 63  ? 54.760  72.390  80.162  1.00 36.79 ? 63  HIS I O   1 
ATOM   9329  C  CB  . HIS I  1 63  ? 52.315  72.951  82.262  1.00 41.21 ? 63  HIS I CB  1 
ATOM   9330  C  CG  . HIS I  1 63  ? 50.892  72.808  82.709  1.00 44.15 ? 63  HIS I CG  1 
ATOM   9331  N  ND1 . HIS I  1 63  ? 50.471  73.134  83.981  1.00 46.57 ? 63  HIS I ND1 1 
ATOM   9332  C  CD2 . HIS I  1 63  ? 49.789  72.383  82.046  1.00 43.77 ? 63  HIS I CD2 1 
ATOM   9333  C  CE1 . HIS I  1 63  ? 49.172  72.916  84.083  1.00 46.13 ? 63  HIS I CE1 1 
ATOM   9334  N  NE2 . HIS I  1 63  ? 48.734  72.458  82.924  1.00 46.45 ? 63  HIS I NE2 1 
ATOM   9335  N  N   . PHE I  1 64  ? 54.187  74.552  80.054  1.00 37.73 ? 64  PHE I N   1 
ATOM   9336  C  CA  . PHE I  1 64  ? 55.527  74.902  79.606  1.00 37.92 ? 64  PHE I CA  1 
ATOM   9337  C  C   . PHE I  1 64  ? 56.526  74.664  80.739  1.00 36.11 ? 64  PHE I C   1 
ATOM   9338  O  O   . PHE I  1 64  ? 56.495  75.341  81.772  1.00 33.88 ? 64  PHE I O   1 
ATOM   9339  C  CB  . PHE I  1 64  ? 55.616  76.329  79.045  1.00 34.85 ? 64  PHE I CB  1 
ATOM   9340  C  CG  . PHE I  1 64  ? 56.959  76.650  78.434  1.00 34.68 ? 64  PHE I CG  1 
ATOM   9341  C  CD1 . PHE I  1 64  ? 57.656  75.681  77.717  1.00 32.01 ? 64  PHE I CD1 1 
ATOM   9342  C  CD2 . PHE I  1 64  ? 57.523  77.909  78.572  1.00 30.85 ? 64  PHE I CD2 1 
ATOM   9343  C  CE1 . PHE I  1 64  ? 58.886  75.957  77.154  1.00 29.80 ? 64  PHE I CE1 1 
ATOM   9344  C  CE2 . PHE I  1 64  ? 58.755  78.189  78.019  1.00 35.90 ? 64  PHE I CE2 1 
ATOM   9345  C  CZ  . PHE I  1 64  ? 59.438  77.203  77.305  1.00 33.83 ? 64  PHE I CZ  1 
ATOM   9346  N  N   . ASN I  1 65  ? 57.391  73.673  80.533  1.00 38.83 ? 65  ASN I N   1 
ATOM   9347  C  CA  . ASN I  1 65  ? 58.314  73.222  81.567  1.00 42.56 ? 65  ASN I CA  1 
ATOM   9348  C  C   . ASN I  1 65  ? 59.714  72.831  81.045  1.00 41.24 ? 65  ASN I C   1 
ATOM   9349  O  O   . ASN I  1 65  ? 60.089  71.651  81.052  1.00 42.63 ? 65  ASN I O   1 
ATOM   9350  C  CB  . ASN I  1 65  ? 57.682  72.062  82.337  1.00 41.96 ? 65  ASN I CB  1 
ATOM   9351  C  CG  . ASN I  1 65  ? 58.574  71.541  83.436  1.00 42.13 ? 65  ASN I CG  1 
ATOM   9352  O  OD1 . ASN I  1 65  ? 59.270  72.309  84.105  1.00 41.30 ? 65  ASN I OD1 1 
ATOM   9353  N  ND2 . ASN I  1 65  ? 58.578  70.228  83.614  1.00 40.19 ? 65  ASN I ND2 1 
ATOM   9354  N  N   . PRO I  1 66  ? 60.498  73.831  80.606  1.00 39.90 ? 66  PRO I N   1 
ATOM   9355  C  CA  . PRO I  1 66  ? 61.807  73.542  80.015  1.00 39.48 ? 66  PRO I CA  1 
ATOM   9356  C  C   . PRO I  1 66  ? 62.813  73.074  81.064  1.00 43.46 ? 66  PRO I C   1 
ATOM   9357  O  O   . PRO I  1 66  ? 63.721  72.311  80.729  1.00 43.61 ? 66  PRO I O   1 
ATOM   9358  C  CB  . PRO I  1 66  ? 62.224  74.896  79.423  1.00 34.89 ? 66  PRO I CB  1 
ATOM   9359  C  CG  . PRO I  1 66  ? 61.538  75.902  80.275  1.00 38.20 ? 66  PRO I CG  1 
ATOM   9360  C  CD  . PRO I  1 66  ? 60.227  75.281  80.672  1.00 37.98 ? 66  PRO I CD  1 
ATOM   9361  N  N   . LEU I  1 67  ? 62.636  73.517  82.311  1.00 47.21 ? 67  LEU I N   1 
ATOM   9362  C  CA  . LEU I  1 67  ? 63.539  73.181  83.422  1.00 44.54 ? 67  LEU I CA  1 
ATOM   9363  C  C   . LEU I  1 67  ? 63.206  71.836  84.107  1.00 47.46 ? 67  LEU I C   1 
ATOM   9364  O  O   . LEU I  1 67  ? 63.833  71.471  85.105  1.00 51.79 ? 67  LEU I O   1 
ATOM   9365  C  CB  . LEU I  1 67  ? 63.548  74.315  84.460  1.00 41.50 ? 67  LEU I CB  1 
ATOM   9366  C  CG  . LEU I  1 67  ? 64.386  75.584  84.221  1.00 45.16 ? 67  LEU I CG  1 
ATOM   9367  C  CD1 . LEU I  1 67  ? 63.825  76.470  83.109  1.00 47.63 ? 67  LEU I CD1 1 
ATOM   9368  C  CD2 . LEU I  1 67  ? 64.533  76.389  85.511  1.00 46.21 ? 67  LEU I CD2 1 
ATOM   9369  N  N   . SER I  1 68  ? 62.216  71.116  83.574  1.00 46.12 ? 68  SER I N   1 
ATOM   9370  C  CA  . SER I  1 68  ? 61.805  69.798  84.084  1.00 43.66 ? 68  SER I CA  1 
ATOM   9371  C  C   . SER I  1 68  ? 61.407  69.780  85.567  1.00 49.39 ? 68  SER I C   1 
ATOM   9372  O  O   . SER I  1 68  ? 61.537  68.753  86.234  1.00 45.76 ? 68  SER I O   1 
ATOM   9373  C  CB  . SER I  1 68  ? 62.892  68.751  83.828  1.00 47.02 ? 68  SER I CB  1 
ATOM   9374  O  OG  . SER I  1 68  ? 63.352  68.818  82.493  1.00 47.05 ? 68  SER I OG  1 
ATOM   9375  N  N   . ARG I  1 69  ? 60.923  70.914  86.069  1.00 50.75 ? 69  ARG I N   1 
ATOM   9376  C  CA  . ARG I  1 69  ? 60.421  71.014  87.438  1.00 50.57 ? 69  ARG I CA  1 
ATOM   9377  C  C   . ARG I  1 69  ? 58.992  70.486  87.505  1.00 52.72 ? 69  ARG I C   1 
ATOM   9378  O  O   . ARG I  1 69  ? 58.379  70.200  86.475  1.00 48.12 ? 69  ARG I O   1 
ATOM   9379  C  CB  . ARG I  1 69  ? 60.432  72.468  87.927  1.00 49.41 ? 69  ARG I CB  1 
ATOM   9380  C  CG  . ARG I  1 69  ? 61.692  73.266  87.592  1.00 55.59 ? 69  ARG I CG  1 
ATOM   9381  C  CD  . ARG I  1 69  ? 62.947  72.689  88.233  1.00 53.99 ? 69  ARG I CD  1 
ATOM   9382  N  NE  . ARG I  1 69  ? 62.737  72.354  89.640  1.00 63.23 ? 69  ARG I NE  1 
ATOM   9383  C  CZ  . ARG I  1 69  ? 63.694  71.921  90.459  1.00 71.43 ? 69  ARG I CZ  1 
ATOM   9384  N  NH1 . ARG I  1 69  ? 63.407  71.627  91.725  1.00 66.98 ? 69  ARG I NH1 1 
ATOM   9385  N  NH2 . ARG I  1 69  ? 64.939  71.783  90.014  1.00 72.91 ? 69  ARG I NH2 1 
ATOM   9386  N  N   . LYS I  1 70  ? 58.459  70.369  88.716  1.00 49.89 ? 70  LYS I N   1 
ATOM   9387  C  CA  . LYS I  1 70  ? 57.086  69.916  88.895  1.00 50.28 ? 70  LYS I CA  1 
ATOM   9388  C  C   . LYS I  1 70  ? 56.144  71.114  88.959  1.00 49.49 ? 70  LYS I C   1 
ATOM   9389  O  O   . LYS I  1 70  ? 56.604  72.257  89.062  1.00 45.53 ? 70  LYS I O   1 
ATOM   9390  C  CB  . LYS I  1 70  ? 56.971  69.083  90.166  1.00 54.65 ? 70  LYS I CB  1 
ATOM   9391  C  CG  . LYS I  1 70  ? 57.732  67.774  90.112  1.00 51.03 ? 70  LYS I CG  1 
ATOM   9392  C  CD  . LYS I  1 70  ? 57.904  67.213  91.506  1.00 60.91 ? 70  LYS I CD  1 
ATOM   9393  C  CE  . LYS I  1 70  ? 56.597  67.304  92.299  1.00 71.48 ? 70  LYS I CE  1 
ATOM   9394  N  NZ  . LYS I  1 70  ? 56.740  66.892  93.728  1.00 70.47 ? 70  LYS I NZ  1 
ATOM   9395  N  N   . HIS I  1 71  ? 54.837  70.851  88.902  1.00 43.66 ? 71  HIS I N   1 
ATOM   9396  C  CA  . HIS I  1 71  ? 53.825  71.912  88.909  1.00 45.95 ? 71  HIS I CA  1 
ATOM   9397  C  C   . HIS I  1 71  ? 53.673  72.611  90.268  1.00 46.21 ? 71  HIS I C   1 
ATOM   9398  O  O   . HIS I  1 71  ? 53.758  71.973  91.311  1.00 47.11 ? 71  HIS I O   1 
ATOM   9399  C  CB  . HIS I  1 71  ? 52.467  71.373  88.439  1.00 43.73 ? 71  HIS I CB  1 
ATOM   9400  C  CG  . HIS I  1 71  ? 51.373  72.394  88.460  1.00 44.91 ? 71  HIS I CG  1 
ATOM   9401  N  ND1 . HIS I  1 71  ? 51.318  73.447  87.575  1.00 45.13 ? 71  HIS I ND1 1 
ATOM   9402  C  CD2 . HIS I  1 71  ? 50.299  72.532  89.273  1.00 50.25 ? 71  HIS I CD2 1 
ATOM   9403  C  CE1 . HIS I  1 71  ? 50.254  74.186  87.832  1.00 47.22 ? 71  HIS I CE1 1 
ATOM   9404  N  NE2 . HIS I  1 71  ? 49.618  73.651  88.858  1.00 51.57 ? 71  HIS I NE2 1 
ATOM   9405  N  N   . GLY I  1 72  ? 53.446  73.924  90.234  1.00 42.39 ? 72  GLY I N   1 
ATOM   9406  C  CA  . GLY I  1 72  ? 53.226  74.711  91.433  1.00 43.86 ? 72  GLY I CA  1 
ATOM   9407  C  C   . GLY I  1 72  ? 52.548  76.053  91.181  1.00 45.82 ? 72  GLY I C   1 
ATOM   9408  O  O   . GLY I  1 72  ? 52.154  76.377  90.059  1.00 40.11 ? 72  GLY I O   1 
ATOM   9409  N  N   . GLY I  1 73  ? 52.405  76.842  92.240  1.00 44.08 ? 73  GLY I N   1 
ATOM   9410  C  CA  . GLY I  1 73  ? 51.879  78.184  92.100  1.00 43.28 ? 73  GLY I CA  1 
ATOM   9411  C  C   . GLY I  1 73  ? 52.939  79.140  91.580  1.00 40.09 ? 73  GLY I C   1 
ATOM   9412  O  O   . GLY I  1 73  ? 54.130  78.826  91.606  1.00 42.99 ? 73  GLY I O   1 
ATOM   9413  N  N   . PRO I  1 74  ? 52.510  80.322  91.112  1.00 37.45 ? 74  PRO I N   1 
ATOM   9414  C  CA  . PRO I  1 74  ? 53.394  81.346  90.544  1.00 41.87 ? 74  PRO I CA  1 
ATOM   9415  C  C   . PRO I  1 74  ? 54.405  81.943  91.530  1.00 44.42 ? 74  PRO I C   1 
ATOM   9416  O  O   . PRO I  1 74  ? 55.534  82.204  91.116  1.00 41.37 ? 74  PRO I O   1 
ATOM   9417  C  CB  . PRO I  1 74  ? 52.418  82.426  90.057  1.00 42.66 ? 74  PRO I CB  1 
ATOM   9418  C  CG  . PRO I  1 74  ? 51.166  82.192  90.824  1.00 40.97 ? 74  PRO I CG  1 
ATOM   9419  C  CD  . PRO I  1 74  ? 51.094  80.711  91.019  1.00 41.34 ? 74  PRO I CD  1 
ATOM   9420  N  N   . LYS I  1 75  ? 54.030  82.161  92.791  1.00 40.84 ? 75  LYS I N   1 
ATOM   9421  C  CA  . LYS I  1 75  ? 54.981  82.732  93.746  1.00 39.63 ? 75  LYS I CA  1 
ATOM   9422  C  C   . LYS I  1 75  ? 55.815  81.640  94.400  1.00 40.82 ? 75  LYS I C   1 
ATOM   9423  O  O   . LYS I  1 75  ? 56.637  81.906  95.280  1.00 42.99 ? 75  LYS I O   1 
ATOM   9424  C  CB  . LYS I  1 75  ? 54.277  83.606  94.791  1.00 37.31 ? 75  LYS I CB  1 
ATOM   9425  C  CG  . LYS I  1 75  ? 53.669  84.863  94.205  1.00 37.98 ? 75  LYS I CG  1 
ATOM   9426  C  CD  . LYS I  1 75  ? 54.711  85.591  93.356  1.00 40.51 ? 75  LYS I CD  1 
ATOM   9427  C  CE  . LYS I  1 75  ? 54.102  86.726  92.552  1.00 36.03 ? 75  LYS I CE  1 
ATOM   9428  N  NZ  . LYS I  1 75  ? 55.166  87.442  91.792  1.00 37.81 ? 75  LYS I NZ  1 
ATOM   9429  N  N   . ASP I  1 76  ? 55.606  80.408  93.951  1.00 38.75 ? 76  ASP I N   1 
ATOM   9430  C  CA  . ASP I  1 76  ? 56.366  79.279  94.463  1.00 44.48 ? 76  ASP I CA  1 
ATOM   9431  C  C   . ASP I  1 76  ? 57.612  79.023  93.613  1.00 49.61 ? 76  ASP I C   1 
ATOM   9432  O  O   . ASP I  1 76  ? 57.614  79.277  92.405  1.00 48.71 ? 76  ASP I O   1 
ATOM   9433  C  CB  . ASP I  1 76  ? 55.478  78.039  94.540  1.00 45.09 ? 76  ASP I CB  1 
ATOM   9434  C  CG  . ASP I  1 76  ? 56.268  76.778  94.772  1.00 51.22 ? 76  ASP I CG  1 
ATOM   9435  O  OD1 . ASP I  1 76  ? 56.837  76.599  95.874  1.00 60.08 ? 76  ASP I OD1 1 
ATOM   9436  O  OD2 . ASP I  1 76  ? 56.320  75.957  93.844  1.00 52.14 ? 76  ASP I OD2 1 
ATOM   9437  N  N   . GLU I  1 77  ? 58.677  78.539  94.247  1.00 49.68 ? 77  GLU I N   1 
ATOM   9438  C  CA  . GLU I  1 77  ? 59.939  78.296  93.549  1.00 48.91 ? 77  GLU I CA  1 
ATOM   9439  C  C   . GLU I  1 77  ? 59.908  77.012  92.700  1.00 52.36 ? 77  GLU I C   1 
ATOM   9440  O  O   . GLU I  1 77  ? 60.505  76.963  91.616  1.00 48.24 ? 77  GLU I O   1 
ATOM   9441  C  CB  . GLU I  1 77  ? 61.111  78.291  94.540  1.00 43.73 ? 77  GLU I CB  1 
ATOM   9442  C  CG  . GLU I  1 77  ? 62.482  78.145  93.899  1.00 49.18 ? 77  GLU I CG  1 
ATOM   9443  C  CD  . GLU I  1 77  ? 62.916  76.693  93.775  1.00 55.18 ? 77  GLU I CD  1 
ATOM   9444  O  OE1 . GLU I  1 77  ? 62.354  75.837  94.495  1.00 61.69 ? 77  GLU I OE1 1 
ATOM   9445  O  OE2 . GLU I  1 77  ? 63.806  76.393  92.950  1.00 57.32 ? 77  GLU I OE2 1 
ATOM   9446  N  N   . GLU I  1 78  ? 59.211  75.984  93.188  1.00 47.21 ? 78  GLU I N   1 
ATOM   9447  C  CA  . GLU I  1 78  ? 59.047  74.742  92.433  1.00 49.00 ? 78  GLU I CA  1 
ATOM   9448  C  C   . GLU I  1 78  ? 57.813  74.797  91.527  1.00 48.92 ? 78  GLU I C   1 
ATOM   9449  O  O   . GLU I  1 78  ? 56.725  74.347  91.903  1.00 46.79 ? 78  GLU I O   1 
ATOM   9450  C  CB  . GLU I  1 78  ? 58.962  73.533  93.373  1.00 47.99 ? 78  GLU I CB  1 
ATOM   9451  C  CG  . GLU I  1 78  ? 58.779  72.188  92.675  1.00 47.51 ? 78  GLU I CG  1 
ATOM   9452  C  CD  . GLU I  1 78  ? 60.042  71.700  91.985  1.00 56.54 ? 78  GLU I CD  1 
ATOM   9453  O  OE1 . GLU I  1 78  ? 61.093  72.364  92.130  1.00 58.15 ? 78  GLU I OE1 1 
ATOM   9454  O  OE2 . GLU I  1 78  ? 59.987  70.647  91.305  1.00 56.59 ? 78  GLU I OE2 1 
ATOM   9455  N  N   . ARG I  1 79  ? 57.987  75.345  90.329  1.00 46.12 ? 79  ARG I N   1 
ATOM   9456  C  CA  . ARG I  1 79  ? 56.879  75.475  89.390  1.00 40.51 ? 79  ARG I CA  1 
ATOM   9457  C  C   . ARG I  1 79  ? 57.338  75.193  87.965  1.00 42.96 ? 79  ARG I C   1 
ATOM   9458  O  O   . ARG I  1 79  ? 58.537  75.087  87.704  1.00 37.20 ? 79  ARG I O   1 
ATOM   9459  C  CB  . ARG I  1 79  ? 56.287  76.881  89.472  1.00 39.57 ? 79  ARG I CB  1 
ATOM   9460  C  CG  . ARG I  1 79  ? 57.330  77.975  89.349  1.00 37.73 ? 79  ARG I CG  1 
ATOM   9461  C  CD  . ARG I  1 79  ? 56.696  79.357  89.220  1.00 38.36 ? 79  ARG I CD  1 
ATOM   9462  N  NE  . ARG I  1 79  ? 56.247  79.650  87.859  1.00 35.52 ? 79  ARG I NE  1 
ATOM   9463  C  CZ  . ARG I  1 79  ? 55.895  80.861  87.434  1.00 36.72 ? 79  ARG I CZ  1 
ATOM   9464  N  NH1 . ARG I  1 79  ? 55.969  81.901  88.256  1.00 36.61 ? 79  ARG I NH1 1 
ATOM   9465  N  NH2 . ARG I  1 79  ? 55.505  81.051  86.176  1.00 35.58 ? 79  ARG I NH2 1 
ATOM   9466  N  N   . HIS I  1 80  ? 56.379  75.043  87.053  1.00 40.04 ? 80  HIS I N   1 
ATOM   9467  C  CA  . HIS I  1 80  ? 56.679  75.021  85.629  1.00 38.50 ? 80  HIS I CA  1 
ATOM   9468  C  C   . HIS I  1 80  ? 56.766  76.490  85.240  1.00 39.03 ? 80  HIS I C   1 
ATOM   9469  O  O   . HIS I  1 80  ? 56.123  77.336  85.887  1.00 32.39 ? 80  HIS I O   1 
ATOM   9470  C  CB  . HIS I  1 80  ? 55.547  74.361  84.837  1.00 36.02 ? 80  HIS I CB  1 
ATOM   9471  C  CG  . HIS I  1 80  ? 55.305  72.923  85.182  1.00 41.63 ? 80  HIS I CG  1 
ATOM   9472  N  ND1 . HIS I  1 80  ? 54.038  72.384  85.267  1.00 36.25 ? 80  HIS I ND1 1 
ATOM   9473  C  CD2 . HIS I  1 80  ? 56.163  71.910  85.442  1.00 41.79 ? 80  HIS I CD2 1 
ATOM   9474  C  CE1 . HIS I  1 80  ? 54.128  71.100  85.560  1.00 41.13 ? 80  HIS I CE1 1 
ATOM   9475  N  NE2 . HIS I  1 80  ? 55.406  70.788  85.674  1.00 41.68 ? 80  HIS I NE2 1 
ATOM   9476  N  N   . VAL I  1 81  ? 57.538  76.808  84.198  1.00 32.99 ? 81  VAL I N   1 
ATOM   9477  C  CA  . VAL I  1 81  ? 57.604  78.200  83.745  1.00 34.33 ? 81  VAL I CA  1 
ATOM   9478  C  C   . VAL I  1 81  ? 56.206  78.686  83.320  1.00 32.20 ? 81  VAL I C   1 
ATOM   9479  O  O   . VAL I  1 81  ? 55.841  79.843  83.561  1.00 30.02 ? 81  VAL I O   1 
ATOM   9480  C  CB  . VAL I  1 81  ? 58.676  78.431  82.643  1.00 34.34 ? 81  VAL I CB  1 
ATOM   9481  C  CG1 . VAL I  1 81  ? 58.513  79.811  81.990  1.00 32.84 ? 81  VAL I CG1 1 
ATOM   9482  C  CG2 . VAL I  1 81  ? 60.068  78.284  83.235  1.00 31.51 ? 81  VAL I CG2 1 
ATOM   9483  N  N   . GLY I  1 82  ? 55.407  77.773  82.762  1.00 31.75 ? 82  GLY I N   1 
ATOM   9484  C  CA  . GLY I  1 82  ? 54.058  78.087  82.312  1.00 33.08 ? 82  GLY I CA  1 
ATOM   9485  C  C   . GLY I  1 82  ? 53.010  78.311  83.397  1.00 35.73 ? 82  GLY I C   1 
ATOM   9486  O  O   . GLY I  1 82  ? 51.883  78.715  83.099  1.00 31.97 ? 82  GLY I O   1 
ATOM   9487  N  N   . ASP I  1 83  ? 53.377  78.060  84.655  1.00 41.27 ? 83  ASP I N   1 
ATOM   9488  C  CA  . ASP I  1 83  ? 52.427  78.149  85.770  1.00 38.55 ? 83  ASP I CA  1 
ATOM   9489  C  C   . ASP I  1 83  ? 52.171  79.583  86.204  1.00 36.23 ? 83  ASP I C   1 
ATOM   9490  O  O   . ASP I  1 83  ? 53.029  80.208  86.818  1.00 40.38 ? 83  ASP I O   1 
ATOM   9491  C  CB  . ASP I  1 83  ? 52.941  77.353  86.965  1.00 35.55 ? 83  ASP I CB  1 
ATOM   9492  C  CG  . ASP I  1 83  ? 53.082  75.887  86.665  1.00 37.58 ? 83  ASP I CG  1 
ATOM   9493  O  OD1 . ASP I  1 83  ? 52.347  75.379  85.790  1.00 33.25 ? 83  ASP I OD1 1 
ATOM   9494  O  OD2 . ASP I  1 83  ? 53.927  75.240  87.311  1.00 38.01 ? 83  ASP I OD2 1 
ATOM   9495  N  N   . LEU I  1 84  ? 50.990  80.104  85.893  1.00 38.05 ? 84  LEU I N   1 
ATOM   9496  C  CA  . LEU I  1 84  ? 50.652  81.480  86.267  1.00 39.13 ? 84  LEU I CA  1 
ATOM   9497  C  C   . LEU I  1 84  ? 49.446  81.525  87.212  1.00 41.04 ? 84  LEU I C   1 
ATOM   9498  O  O   . LEU I  1 84  ? 48.783  82.557  87.353  1.00 40.73 ? 84  LEU I O   1 
ATOM   9499  C  CB  . LEU I  1 84  ? 50.428  82.353  85.024  1.00 38.38 ? 84  LEU I CB  1 
ATOM   9500  C  CG  . LEU I  1 84  ? 51.665  82.539  84.139  1.00 39.94 ? 84  LEU I CG  1 
ATOM   9501  C  CD1 . LEU I  1 84  ? 51.341  83.383  82.917  1.00 41.53 ? 84  LEU I CD1 1 
ATOM   9502  C  CD2 . LEU I  1 84  ? 52.810  83.166  84.941  1.00 35.17 ? 84  LEU I CD2 1 
ATOM   9503  N  N   . GLY I  1 85  ? 49.181  80.388  87.851  1.00 40.81 ? 85  GLY I N   1 
ATOM   9504  C  CA  . GLY I  1 85  ? 48.229  80.310  88.937  1.00 39.23 ? 85  GLY I CA  1 
ATOM   9505  C  C   . GLY I  1 85  ? 46.788  80.228  88.492  1.00 41.95 ? 85  GLY I C   1 
ATOM   9506  O  O   . GLY I  1 85  ? 46.382  79.289  87.804  1.00 46.91 ? 85  GLY I O   1 
ATOM   9507  N  N   . ASN I  1 86  ? 46.008  81.215  88.912  1.00 38.70 ? 86  ASN I N   1 
ATOM   9508  C  CA  . ASN I  1 86  ? 44.593  81.266  88.598  1.00 40.97 ? 86  ASN I CA  1 
ATOM   9509  C  C   . ASN I  1 86  ? 44.182  82.697  88.336  1.00 38.47 ? 86  ASN I C   1 
ATOM   9510  O  O   . ASN I  1 86  ? 44.783  83.629  88.865  1.00 34.54 ? 86  ASN I O   1 
ATOM   9511  C  CB  . ASN I  1 86  ? 43.743  80.699  89.749  1.00 46.19 ? 86  ASN I CB  1 
ATOM   9512  C  CG  . ASN I  1 86  ? 43.848  79.187  89.874  1.00 47.55 ? 86  ASN I CG  1 
ATOM   9513  O  OD1 . ASN I  1 86  ? 43.211  78.443  89.129  1.00 48.81 ? 86  ASN I OD1 1 
ATOM   9514  N  ND2 . ASN I  1 86  ? 44.642  78.728  90.831  1.00 48.62 ? 86  ASN I ND2 1 
ATOM   9515  N  N   . VAL I  1 87  ? 43.171  82.873  87.497  1.00 44.72 ? 87  VAL I N   1 
ATOM   9516  C  CA  . VAL I  1 87  ? 42.493  84.156  87.417  1.00 50.74 ? 87  VAL I CA  1 
ATOM   9517  C  C   . VAL I  1 87  ? 41.086  83.950  87.964  1.00 49.70 ? 87  VAL I C   1 
ATOM   9518  O  O   . VAL I  1 87  ? 40.538  82.849  87.891  1.00 49.37 ? 87  VAL I O   1 
ATOM   9519  C  CB  . VAL I  1 87  ? 42.425  84.707  85.977  1.00 46.36 ? 87  VAL I CB  1 
ATOM   9520  C  CG1 . VAL I  1 87  ? 43.821  85.053  85.469  1.00 43.06 ? 87  VAL I CG1 1 
ATOM   9521  C  CG2 . VAL I  1 87  ? 41.712  83.713  85.059  1.00 44.07 ? 87  VAL I CG2 1 
ATOM   9522  N  N   . THR I  1 88  ? 40.500  85.002  88.515  1.00 50.37 ? 88  THR I N   1 
ATOM   9523  C  CA  . THR I  1 88  ? 39.182  84.874  89.119  1.00 53.07 ? 88  THR I CA  1 
ATOM   9524  C  C   . THR I  1 88  ? 38.122  85.675  88.361  1.00 51.97 ? 88  THR I C   1 
ATOM   9525  O  O   . THR I  1 88  ? 38.263  86.885  88.146  1.00 43.86 ? 88  THR I O   1 
ATOM   9526  C  CB  . THR I  1 88  ? 39.210  85.271  90.613  1.00 55.24 ? 88  THR I CB  1 
ATOM   9527  O  OG1 . THR I  1 88  ? 40.277  84.572  91.267  1.00 52.47 ? 88  THR I OG1 1 
ATOM   9528  C  CG2 . THR I  1 88  ? 37.882  84.927  91.295  1.00 52.64 ? 88  THR I CG2 1 
ATOM   9529  N  N   . ALA I  1 89  ? 37.071  84.977  87.944  1.00 54.04 ? 89  ALA I N   1 
ATOM   9530  C  CA  . ALA I  1 89  ? 35.927  85.610  87.307  1.00 57.36 ? 89  ALA I CA  1 
ATOM   9531  C  C   . ALA I  1 89  ? 34.910  86.108  88.348  1.00 63.01 ? 89  ALA I C   1 
ATOM   9532  O  O   . ALA I  1 89  ? 34.540  85.383  89.285  1.00 53.64 ? 89  ALA I O   1 
ATOM   9533  C  CB  . ALA I  1 89  ? 35.269  84.644  86.326  1.00 54.54 ? 89  ALA I CB  1 
ATOM   9534  N  N   . ASP I  1 90  ? 34.470  87.353  88.173  1.00 64.68 ? 90  ASP I N   1 
ATOM   9535  C  CA  . ASP I  1 90  ? 33.421  87.933  89.005  1.00 67.35 ? 90  ASP I CA  1 
ATOM   9536  C  C   . ASP I  1 90  ? 32.044  87.334  88.671  1.00 68.60 ? 90  ASP I C   1 
ATOM   9537  O  O   . ASP I  1 90  ? 31.944  86.384  87.888  1.00 65.88 ? 90  ASP I O   1 
ATOM   9538  C  CB  . ASP I  1 90  ? 33.416  89.469  88.886  1.00 63.60 ? 90  ASP I CB  1 
ATOM   9539  C  CG  . ASP I  1 90  ? 33.048  89.960  87.490  1.00 60.32 ? 90  ASP I CG  1 
ATOM   9540  O  OD1 . ASP I  1 90  ? 32.872  89.129  86.579  1.00 63.25 ? 90  ASP I OD1 1 
ATOM   9541  O  OD2 . ASP I  1 90  ? 32.945  91.188  87.296  1.00 58.03 ? 90  ASP I OD2 1 
ATOM   9542  N  N   . LYS I  1 91  ? 30.993  87.895  89.267  1.00 73.59 ? 91  LYS I N   1 
ATOM   9543  C  CA  . LYS I  1 91  ? 29.623  87.420  89.053  1.00 73.48 ? 91  LYS I CA  1 
ATOM   9544  C  C   . LYS I  1 91  ? 29.178  87.563  87.589  1.00 73.38 ? 91  LYS I C   1 
ATOM   9545  O  O   . LYS I  1 91  ? 28.546  86.665  87.027  1.00 72.34 ? 91  LYS I O   1 
ATOM   9546  C  CB  . LYS I  1 91  ? 28.636  88.119  90.010  1.00 74.85 ? 91  LYS I CB  1 
ATOM   9547  C  CG  . LYS I  1 91  ? 28.564  89.649  89.896  1.00 74.73 ? 91  LYS I CG  1 
ATOM   9548  C  CD  . LYS I  1 91  ? 29.656  90.354  90.702  1.00 72.25 ? 91  LYS I CD  1 
ATOM   9549  C  CE  . LYS I  1 91  ? 29.737  91.837  90.339  1.00 76.04 ? 91  LYS I CE  1 
ATOM   9550  N  NZ  . LYS I  1 91  ? 30.862  92.546  91.022  1.00 71.46 ? 91  LYS I NZ  1 
ATOM   9551  N  N   . ASP I  1 92  ? 29.531  88.690  86.976  1.00 73.75 ? 92  ASP I N   1 
ATOM   9552  C  CA  . ASP I  1 92  ? 29.215  88.951  85.576  1.00 72.23 ? 92  ASP I CA  1 
ATOM   9553  C  C   . ASP I  1 92  ? 29.929  87.954  84.653  1.00 71.49 ? 92  ASP I C   1 
ATOM   9554  O  O   . ASP I  1 92  ? 29.463  87.675  83.549  1.00 71.14 ? 92  ASP I O   1 
ATOM   9555  C  CB  . ASP I  1 92  ? 29.601  90.390  85.212  1.00 71.74 ? 92  ASP I CB  1 
ATOM   9556  C  CG  . ASP I  1 92  ? 29.035  91.416  86.194  1.00 75.28 ? 92  ASP I CG  1 
ATOM   9557  O  OD1 . ASP I  1 92  ? 27.798  91.441  86.406  1.00 77.29 ? 92  ASP I OD1 1 
ATOM   9558  O  OD2 . ASP I  1 92  ? 29.835  92.182  86.776  1.00 71.46 ? 92  ASP I OD2 1 
ATOM   9559  N  N   . GLY I  1 93  ? 31.060  87.421  85.113  1.00 68.63 ? 93  GLY I N   1 
ATOM   9560  C  CA  . GLY I  1 93  ? 31.809  86.423  84.365  1.00 65.93 ? 93  GLY I CA  1 
ATOM   9561  C  C   . GLY I  1 93  ? 33.122  86.954  83.813  1.00 59.97 ? 93  GLY I C   1 
ATOM   9562  O  O   . GLY I  1 93  ? 33.819  86.261  83.069  1.00 54.97 ? 93  GLY I O   1 
ATOM   9563  N  N   . VAL I  1 94  ? 33.447  88.191  84.184  1.00 58.32 ? 94  VAL I N   1 
ATOM   9564  C  CA  . VAL I  1 94  ? 34.646  88.871  83.713  1.00 56.74 ? 94  VAL I CA  1 
ATOM   9565  C  C   . VAL I  1 94  ? 35.800  88.698  84.698  1.00 58.99 ? 94  VAL I C   1 
ATOM   9566  O  O   . VAL I  1 94  ? 35.624  88.860  85.910  1.00 59.08 ? 94  VAL I O   1 
ATOM   9567  C  CB  . VAL I  1 94  ? 34.384  90.380  83.500  1.00 60.13 ? 94  VAL I CB  1 
ATOM   9568  C  CG1 . VAL I  1 94  ? 35.656  91.091  83.031  1.00 59.52 ? 94  VAL I CG1 1 
ATOM   9569  C  CG2 . VAL I  1 94  ? 33.247  90.593  82.508  1.00 53.72 ? 94  VAL I CG2 1 
ATOM   9570  N  N   . ALA I  1 95  ? 36.977  88.363  84.173  1.00 57.21 ? 95  ALA I N   1 
ATOM   9571  C  CA  . ALA I  1 95  ? 38.174  88.186  84.992  1.00 50.88 ? 95  ALA I CA  1 
ATOM   9572  C  C   . ALA I  1 95  ? 39.241  89.219  84.655  1.00 48.70 ? 95  ALA I C   1 
ATOM   9573  O  O   . ALA I  1 95  ? 40.099  88.959  83.815  1.00 52.28 ? 95  ALA I O   1 
ATOM   9574  C  CB  . ALA I  1 95  ? 38.738  86.770  84.822  1.00 48.09 ? 95  ALA I CB  1 
ATOM   9575  N  N   . ASP I  1 96  ? 39.178  90.387  85.295  1.00 50.80 ? 96  ASP I N   1 
ATOM   9576  C  CA  . ASP I  1 96  ? 40.239  91.391  85.175  1.00 49.34 ? 96  ASP I CA  1 
ATOM   9577  C  C   . ASP I  1 96  ? 41.573  90.779  85.629  1.00 52.18 ? 96  ASP I C   1 
ATOM   9578  O  O   . ASP I  1 96  ? 41.738  90.412  86.797  1.00 48.59 ? 96  ASP I O   1 
ATOM   9579  C  CB  . ASP I  1 96  ? 39.896  92.655  85.987  1.00 52.15 ? 96  ASP I CB  1 
ATOM   9580  C  CG  . ASP I  1 96  ? 41.004  93.729  85.934  1.00 57.95 ? 96  ASP I CG  1 
ATOM   9581  O  OD1 . ASP I  1 96  ? 42.035  93.571  86.630  1.00 58.60 ? 96  ASP I OD1 1 
ATOM   9582  O  OD2 . ASP I  1 96  ? 40.839  94.747  85.219  1.00 57.70 ? 96  ASP I OD2 1 
ATOM   9583  N  N   . VAL I  1 97  ? 42.511  90.649  84.690  1.00 48.36 ? 97  VAL I N   1 
ATOM   9584  C  CA  . VAL I  1 97  ? 43.812  90.057  84.978  1.00 44.23 ? 97  VAL I CA  1 
ATOM   9585  C  C   . VAL I  1 97  ? 44.874  91.142  85.143  1.00 40.66 ? 97  VAL I C   1 
ATOM   9586  O  O   . VAL I  1 97  ? 44.952  92.086  84.359  1.00 36.53 ? 97  VAL I O   1 
ATOM   9587  C  CB  . VAL I  1 97  ? 44.254  89.052  83.878  1.00 44.86 ? 97  VAL I CB  1 
ATOM   9588  C  CG1 . VAL I  1 97  ? 45.538  88.355  84.282  1.00 42.08 ? 97  VAL I CG1 1 
ATOM   9589  C  CG2 . VAL I  1 97  ? 43.163  88.024  83.613  1.00 41.36 ? 97  VAL I CG2 1 
ATOM   9590  N  N   . SER I  1 98  ? 45.675  91.006  86.191  1.00 43.32 ? 98  SER I N   1 
ATOM   9591  C  CA  . SER I  1 98  ? 46.804  91.890  86.434  1.00 40.25 ? 98  SER I CA  1 
ATOM   9592  C  C   . SER I  1 98  ? 47.843  91.132  87.258  1.00 39.80 ? 98  SER I C   1 
ATOM   9593  O  O   . SER I  1 98  ? 47.749  91.038  88.484  1.00 40.57 ? 98  SER I O   1 
ATOM   9594  C  CB  . SER I  1 98  ? 46.352  93.181  87.125  1.00 44.91 ? 98  SER I CB  1 
ATOM   9595  O  OG  . SER I  1 98  ? 45.358  92.922  88.108  1.00 43.87 ? 98  SER I OG  1 
ATOM   9596  N  N   . ILE I  1 99  ? 48.823  90.581  86.554  1.00 41.87 ? 99  ILE I N   1 
ATOM   9597  C  CA  . ILE I  1 99  ? 49.835  89.700  87.124  1.00 39.30 ? 99  ILE I CA  1 
ATOM   9598  C  C   . ILE I  1 99  ? 51.205  90.305  86.850  1.00 40.43 ? 99  ILE I C   1 
ATOM   9599  O  O   . ILE I  1 99  ? 51.394  90.986  85.838  1.00 37.96 ? 99  ILE I O   1 
ATOM   9600  C  CB  . ILE I  1 99  ? 49.741  88.275  86.476  1.00 36.79 ? 99  ILE I CB  1 
ATOM   9601  C  CG1 . ILE I  1 99  ? 48.540  87.512  87.037  1.00 36.94 ? 99  ILE I CG1 1 
ATOM   9602  C  CG2 . ILE I  1 99  ? 51.020  87.459  86.666  1.00 32.88 ? 99  ILE I CG2 1 
ATOM   9603  C  CD1 . ILE I  1 99  ? 48.190  86.251  86.257  1.00 35.80 ? 99  ILE I CD1 1 
ATOM   9604  N  N   . GLU I  1 100 ? 52.147  90.102  87.769  1.00 36.00 ? 100 GLU I N   1 
ATOM   9605  C  CA  . GLU I  1 100 ? 53.553  90.328  87.465  1.00 30.10 ? 100 GLU I CA  1 
ATOM   9606  C  C   . GLU I  1 100 ? 54.305  89.034  87.753  1.00 33.51 ? 100 GLU I C   1 
ATOM   9607  O  O   . GLU I  1 100 ? 54.133  88.429  88.806  1.00 30.92 ? 100 GLU I O   1 
ATOM   9608  C  CB  . GLU I  1 100 ? 54.135  91.497  88.257  1.00 35.51 ? 100 GLU I CB  1 
ATOM   9609  C  CG  . GLU I  1 100 ? 55.665  91.589  88.163  1.00 38.82 ? 100 GLU I CG  1 
ATOM   9610  C  CD  . GLU I  1 100 ? 56.229  92.862  88.775  1.00 41.08 ? 100 GLU I CD  1 
ATOM   9611  O  OE1 . GLU I  1 100 ? 55.576  93.925  88.666  1.00 39.95 ? 100 GLU I OE1 1 
ATOM   9612  O  OE2 . GLU I  1 100 ? 57.327  92.794  89.370  1.00 43.61 ? 100 GLU I OE2 1 
ATOM   9613  N  N   . ASP I  1 101 ? 55.108  88.593  86.793  1.00 34.54 ? 101 ASP I N   1 
ATOM   9614  C  CA  . ASP I  1 101 ? 55.811  87.323  86.915  1.00 34.73 ? 101 ASP I CA  1 
ATOM   9615  C  C   . ASP I  1 101 ? 57.261  87.448  86.438  1.00 37.07 ? 101 ASP I C   1 
ATOM   9616  O  O   . ASP I  1 101 ? 57.542  88.080  85.410  1.00 33.87 ? 101 ASP I O   1 
ATOM   9617  C  CB  . ASP I  1 101 ? 55.075  86.219  86.142  1.00 32.78 ? 101 ASP I CB  1 
ATOM   9618  C  CG  . ASP I  1 101 ? 55.557  84.827  86.513  1.00 35.26 ? 101 ASP I CG  1 
ATOM   9619  O  OD1 . ASP I  1 101 ? 55.005  84.243  87.477  1.00 34.31 ? 101 ASP I OD1 1 
ATOM   9620  O  OD2 . ASP I  1 101 ? 56.495  84.330  85.854  1.00 34.98 ? 101 ASP I OD2 1 
ATOM   9621  N  N   . SER I  1 102 ? 58.173  86.832  87.187  1.00 39.83 ? 102 SER I N   1 
ATOM   9622  C  CA  . SER I  1 102 ? 59.605  86.982  86.938  1.00 35.99 ? 102 SER I CA  1 
ATOM   9623  C  C   . SER I  1 102 ? 60.301  85.691  86.489  1.00 34.59 ? 102 SER I C   1 
ATOM   9624  O  O   . SER I  1 102 ? 61.535  85.626  86.475  1.00 45.56 ? 102 SER I O   1 
ATOM   9625  C  CB  . SER I  1 102 ? 60.297  87.535  88.186  1.00 33.15 ? 102 SER I CB  1 
ATOM   9626  O  OG  . SER I  1 102 ? 60.210  86.599  89.243  1.00 38.30 ? 102 SER I OG  1 
ATOM   9627  N  N   . VAL I  1 103 ? 59.542  84.664  86.122  1.00 33.87 ? 103 VAL I N   1 
ATOM   9628  C  CA  . VAL I  1 103 ? 60.180  83.487  85.522  1.00 38.52 ? 103 VAL I CA  1 
ATOM   9629  C  C   . VAL I  1 103 ? 59.880  83.374  84.012  1.00 34.44 ? 103 VAL I C   1 
ATOM   9630  O  O   . VAL I  1 103 ? 60.737  82.964  83.243  1.00 35.89 ? 103 VAL I O   1 
ATOM   9631  C  CB  . VAL I  1 103 ? 59.836  82.188  86.278  1.00 38.87 ? 103 VAL I CB  1 
ATOM   9632  C  CG1 . VAL I  1 103 ? 58.434  81.936  86.146  1.00 34.95 ? 103 VAL I CG1 1 
ATOM   9633  C  CG2 . VAL I  1 103 ? 60.587  81.000  85.714  1.00 33.16 ? 103 VAL I CG2 1 
ATOM   9634  N  N   . ILE I  1 104 ? 58.676  83.751  83.587  1.00 35.74 ? 104 ILE I N   1 
ATOM   9635  C  CA  . ILE I  1 104 ? 58.397  83.857  82.159  1.00 37.71 ? 104 ILE I CA  1 
ATOM   9636  C  C   . ILE I  1 104 ? 59.121  85.078  81.604  1.00 36.29 ? 104 ILE I C   1 
ATOM   9637  O  O   . ILE I  1 104 ? 59.289  86.086  82.298  1.00 34.10 ? 104 ILE I O   1 
ATOM   9638  C  CB  . ILE I  1 104 ? 56.882  84.029  81.840  1.00 28.78 ? 104 ILE I CB  1 
ATOM   9639  C  CG1 . ILE I  1 104 ? 56.334  85.296  82.502  1.00 29.67 ? 104 ILE I CG1 1 
ATOM   9640  C  CG2 . ILE I  1 104 ? 56.088  82.775  82.203  1.00 28.92 ? 104 ILE I CG2 1 
ATOM   9641  C  CD1 . ILE I  1 104 ? 54.978  85.740  81.968  1.00 32.83 ? 104 ILE I CD1 1 
ATOM   9642  N  N   . SER I  1 105 ? 59.558  84.991  80.353  1.00 36.61 ? 105 SER I N   1 
ATOM   9643  C  CA  . SER I  1 105 ? 60.066  86.171  79.661  1.00 34.31 ? 105 SER I CA  1 
ATOM   9644  C  C   . SER I  1 105 ? 59.584  86.171  78.229  1.00 31.53 ? 105 SER I C   1 
ATOM   9645  O  O   . SER I  1 105 ? 59.158  85.144  77.683  1.00 29.68 ? 105 SER I O   1 
ATOM   9646  C  CB  . SER I  1 105 ? 61.597  86.274  79.718  1.00 28.50 ? 105 SER I CB  1 
ATOM   9647  O  OG  . SER I  1 105 ? 62.184  85.068  79.283  1.00 37.47 ? 105 SER I OG  1 
ATOM   9648  N  N   . LEU I  1 106 ? 59.649  87.345  77.631  1.00 32.99 ? 106 LEU I N   1 
ATOM   9649  C  CA  . LEU I  1 106 ? 59.278  87.508  76.245  1.00 33.55 ? 106 LEU I CA  1 
ATOM   9650  C  C   . LEU I  1 106 ? 60.532  87.368  75.383  1.00 33.81 ? 106 LEU I C   1 
ATOM   9651  O  O   . LEU I  1 106 ? 60.485  87.473  74.154  1.00 30.82 ? 106 LEU I O   1 
ATOM   9652  C  CB  . LEU I  1 106 ? 58.621  88.872  76.055  1.00 31.36 ? 106 LEU I CB  1 
ATOM   9653  C  CG  . LEU I  1 106 ? 57.413  89.115  76.963  1.00 29.25 ? 106 LEU I CG  1 
ATOM   9654  C  CD1 . LEU I  1 106 ? 56.733  90.454  76.625  1.00 29.87 ? 106 LEU I CD1 1 
ATOM   9655  C  CD2 . LEU I  1 106 ? 56.427  87.933  76.881  1.00 23.08 ? 106 LEU I CD2 1 
ATOM   9656  N  N   . SER I  1 107 ? 61.655  87.118  76.049  1.00 32.94 ? 107 SER I N   1 
ATOM   9657  C  CA  . SER I  1 107 ? 62.940  87.007  75.374  1.00 34.04 ? 107 SER I CA  1 
ATOM   9658  C  C   . SER I  1 107 ? 63.750  85.830  75.906  1.00 36.31 ? 107 SER I C   1 
ATOM   9659  O  O   . SER I  1 107 ? 63.412  85.244  76.941  1.00 32.73 ? 107 SER I O   1 
ATOM   9660  C  CB  . SER I  1 107 ? 63.728  88.308  75.544  1.00 36.51 ? 107 SER I CB  1 
ATOM   9661  O  OG  . SER I  1 107 ? 63.233  89.072  76.640  1.00 32.82 ? 107 SER I OG  1 
ATOM   9662  N  N   . GLY I  1 108 ? 64.823  85.492  75.196  1.00 34.01 ? 108 GLY I N   1 
ATOM   9663  C  CA  . GLY I  1 108 ? 65.719  84.449  75.643  1.00 32.92 ? 108 GLY I CA  1 
ATOM   9664  C  C   . GLY I  1 108 ? 65.215  83.087  75.249  1.00 36.07 ? 108 GLY I C   1 
ATOM   9665  O  O   . GLY I  1 108 ? 64.045  82.928  74.929  1.00 37.98 ? 108 GLY I O   1 
ATOM   9666  N  N   . ASP I  1 109 ? 66.093  82.092  75.302  1.00 41.38 ? 109 ASP I N   1 
ATOM   9667  C  CA  . ASP I  1 109 ? 65.812  80.808  74.674  1.00 44.34 ? 109 ASP I CA  1 
ATOM   9668  C  C   . ASP I  1 109 ? 64.865  79.917  75.482  1.00 48.69 ? 109 ASP I C   1 
ATOM   9669  O  O   . ASP I  1 109 ? 64.743  78.722  75.216  1.00 49.43 ? 109 ASP I O   1 
ATOM   9670  C  CB  . ASP I  1 109 ? 67.114  80.081  74.299  1.00 49.23 ? 109 ASP I CB  1 
ATOM   9671  C  CG  . ASP I  1 109 ? 67.617  79.172  75.397  1.00 58.37 ? 109 ASP I CG  1 
ATOM   9672  O  OD1 . ASP I  1 109 ? 68.044  79.693  76.455  1.00 58.23 ? 109 ASP I OD1 1 
ATOM   9673  O  OD2 . ASP I  1 109 ? 67.586  77.935  75.193  1.00 58.08 ? 109 ASP I OD2 1 
ATOM   9674  N  N   . HIS I  1 110 ? 64.191  80.506  76.466  1.00 45.98 ? 110 HIS I N   1 
ATOM   9675  C  CA  . HIS I  1 110 ? 63.044  79.849  77.074  1.00 42.73 ? 110 HIS I CA  1 
ATOM   9676  C  C   . HIS I  1 110 ? 61.855  80.806  77.144  1.00 43.55 ? 110 HIS I C   1 
ATOM   9677  O  O   . HIS I  1 110 ? 61.053  80.753  78.078  1.00 45.50 ? 110 HIS I O   1 
ATOM   9678  C  CB  . HIS I  1 110 ? 63.395  79.300  78.452  1.00 42.68 ? 110 HIS I CB  1 
ATOM   9679  C  CG  . HIS I  1 110 ? 64.525  78.313  78.439  1.00 49.22 ? 110 HIS I CG  1 
ATOM   9680  N  ND1 . HIS I  1 110 ? 65.778  78.608  78.936  1.00 52.10 ? 110 HIS I ND1 1 
ATOM   9681  C  CD2 . HIS I  1 110 ? 64.588  77.035  77.995  1.00 44.32 ? 110 HIS I CD2 1 
ATOM   9682  C  CE1 . HIS I  1 110 ? 66.563  77.551  78.800  1.00 52.18 ? 110 HIS I CE1 1 
ATOM   9683  N  NE2 . HIS I  1 110 ? 65.866  76.584  78.233  1.00 48.97 ? 110 HIS I NE2 1 
ATOM   9684  N  N   . CYS I  1 111 ? 61.736  81.678  76.147  1.00 37.57 ? 111 CYS I N   1 
ATOM   9685  C  CA  . CYS I  1 111 ? 60.663  82.662  76.153  1.00 34.05 ? 111 CYS I CA  1 
ATOM   9686  C  C   . CYS I  1 111 ? 59.301  82.017  75.856  1.00 33.44 ? 111 CYS I C   1 
ATOM   9687  O  O   . CYS I  1 111 ? 59.218  80.840  75.482  1.00 29.47 ? 111 CYS I O   1 
ATOM   9688  C  CB  . CYS I  1 111 ? 60.979  83.863  75.230  1.00 36.29 ? 111 CYS I CB  1 
ATOM   9689  S  SG  . CYS I  1 111 ? 60.691  83.653  73.448  1.00 44.16 ? 111 CYS I SG  1 
ATOM   9690  N  N   . ILE I  1 112 ? 58.230  82.778  76.054  1.00 29.03 ? 112 ILE I N   1 
ATOM   9691  C  CA  . ILE I  1 112 ? 56.893  82.236  75.848  1.00 29.32 ? 112 ILE I CA  1 
ATOM   9692  C  C   . ILE I  1 112 ? 56.243  82.664  74.528  1.00 28.59 ? 112 ILE I C   1 
ATOM   9693  O  O   . ILE I  1 112 ? 55.091  82.305  74.265  1.00 24.18 ? 112 ILE I O   1 
ATOM   9694  C  CB  . ILE I  1 112 ? 55.942  82.594  77.002  1.00 25.56 ? 112 ILE I CB  1 
ATOM   9695  C  CG1 . ILE I  1 112 ? 55.946  84.107  77.245  1.00 23.90 ? 112 ILE I CG1 1 
ATOM   9696  C  CG2 . ILE I  1 112 ? 56.314  81.794  78.272  1.00 31.33 ? 112 ILE I CG2 1 
ATOM   9697  C  CD1 . ILE I  1 112 ? 54.858  84.567  78.182  1.00 27.69 ? 112 ILE I CD1 1 
ATOM   9698  N  N   . ILE I  1 113 ? 56.964  83.432  73.709  1.00 26.16 ? 113 ILE I N   1 
ATOM   9699  C  CA  . ILE I  1 113 ? 56.440  83.796  72.391  1.00 28.00 ? 113 ILE I CA  1 
ATOM   9700  C  C   . ILE I  1 113 ? 56.311  82.557  71.513  1.00 22.78 ? 113 ILE I C   1 
ATOM   9701  O  O   . ILE I  1 113 ? 57.203  81.712  71.483  1.00 24.76 ? 113 ILE I O   1 
ATOM   9702  C  CB  . ILE I  1 113 ? 57.236  84.935  71.705  1.00 29.79 ? 113 ILE I CB  1 
ATOM   9703  C  CG1 . ILE I  1 113 ? 56.702  86.275  72.196  1.00 26.63 ? 113 ILE I CG1 1 
ATOM   9704  C  CG2 . ILE I  1 113 ? 57.071  84.915  70.170  1.00 20.88 ? 113 ILE I CG2 1 
ATOM   9705  C  CD1 . ILE I  1 113 ? 57.414  86.820  73.368  1.00 29.47 ? 113 ILE I CD1 1 
ATOM   9706  N  N   . GLY I  1 114 ? 55.153  82.423  70.875  1.00 24.02 ? 114 GLY I N   1 
ATOM   9707  C  CA  . GLY I  1 114 ? 54.899  81.327  69.952  1.00 26.32 ? 114 GLY I CA  1 
ATOM   9708  C  C   . GLY I  1 114 ? 54.387  80.106  70.673  1.00 27.78 ? 114 GLY I C   1 
ATOM   9709  O  O   . GLY I  1 114 ? 54.336  79.000  70.119  1.00 26.96 ? 114 GLY I O   1 
ATOM   9710  N  N   . ARG I  1 115 ? 54.013  80.314  71.932  1.00 28.11 ? 115 ARG I N   1 
ATOM   9711  C  CA  . ARG I  1 115 ? 53.417  79.258  72.733  1.00 31.28 ? 115 ARG I CA  1 
ATOM   9712  C  C   . ARG I  1 115 ? 51.941  79.618  72.988  1.00 29.90 ? 115 ARG I C   1 
ATOM   9713  O  O   . ARG I  1 115 ? 51.465  80.651  72.500  1.00 27.03 ? 115 ARG I O   1 
ATOM   9714  C  CB  . ARG I  1 115 ? 54.231  79.036  74.019  1.00 27.20 ? 115 ARG I CB  1 
ATOM   9715  C  CG  . ARG I  1 115 ? 55.738  78.987  73.765  1.00 24.56 ? 115 ARG I CG  1 
ATOM   9716  C  CD  . ARG I  1 115 ? 56.508  78.291  74.875  1.00 31.32 ? 115 ARG I CD  1 
ATOM   9717  N  NE  . ARG I  1 115 ? 57.898  77.996  74.508  1.00 27.17 ? 115 ARG I NE  1 
ATOM   9718  C  CZ  . ARG I  1 115 ? 58.307  76.882  73.903  1.00 27.15 ? 115 ARG I CZ  1 
ATOM   9719  N  NH1 . ARG I  1 115 ? 57.449  75.925  73.572  1.00 26.58 ? 115 ARG I NH1 1 
ATOM   9720  N  NH2 . ARG I  1 115 ? 59.591  76.720  73.636  1.00 29.27 ? 115 ARG I NH2 1 
ATOM   9721  N  N   . THR I  1 116 ? 51.223  78.763  73.717  1.00 28.91 ? 116 THR I N   1 
ATOM   9722  C  CA  . THR I  1 116 ? 49.771  78.908  73.873  1.00 28.77 ? 116 THR I CA  1 
ATOM   9723  C  C   . THR I  1 116 ? 49.335  79.231  75.298  1.00 33.69 ? 116 THR I C   1 
ATOM   9724  O  O   . THR I  1 116 ? 49.520  78.428  76.216  1.00 30.28 ? 116 THR I O   1 
ATOM   9725  C  CB  . THR I  1 116 ? 49.034  77.628  73.441  1.00 30.81 ? 116 THR I CB  1 
ATOM   9726  O  OG1 . THR I  1 116 ? 49.401  77.299  72.098  1.00 32.13 ? 116 THR I OG1 1 
ATOM   9727  C  CG2 . THR I  1 116 ? 47.532  77.816  73.513  1.00 31.96 ? 116 THR I CG2 1 
ATOM   9728  N  N   . LEU I  1 117 ? 48.740  80.409  75.468  1.00 34.76 ? 117 LEU I N   1 
ATOM   9729  C  CA  . LEU I  1 117 ? 48.128  80.775  76.732  1.00 36.69 ? 117 LEU I CA  1 
ATOM   9730  C  C   . LEU I  1 117 ? 46.812  80.020  76.830  1.00 39.14 ? 117 LEU I C   1 
ATOM   9731  O  O   . LEU I  1 117 ? 46.069  79.947  75.853  1.00 39.68 ? 117 LEU I O   1 
ATOM   9732  C  CB  . LEU I  1 117 ? 47.886  82.284  76.796  1.00 31.34 ? 117 LEU I CB  1 
ATOM   9733  C  CG  . LEU I  1 117 ? 47.418  82.840  78.141  1.00 35.60 ? 117 LEU I CG  1 
ATOM   9734  C  CD1 . LEU I  1 117 ? 48.568  82.839  79.140  1.00 36.20 ? 117 LEU I CD1 1 
ATOM   9735  C  CD2 . LEU I  1 117 ? 46.816  84.229  77.999  1.00 28.62 ? 117 LEU I CD2 1 
ATOM   9736  N  N   . VAL I  1 118 ? 46.538  79.452  78.002  1.00 38.97 ? 118 VAL I N   1 
ATOM   9737  C  CA  . VAL I  1 118 ? 45.325  78.662  78.233  1.00 40.46 ? 118 VAL I CA  1 
ATOM   9738  C  C   . VAL I  1 118 ? 44.588  79.091  79.511  1.00 43.68 ? 118 VAL I C   1 
ATOM   9739  O  O   . VAL I  1 118 ? 45.201  79.255  80.577  1.00 46.09 ? 118 VAL I O   1 
ATOM   9740  C  CB  . VAL I  1 118 ? 45.642  77.144  78.311  1.00 39.43 ? 118 VAL I CB  1 
ATOM   9741  C  CG1 . VAL I  1 118 ? 44.453  76.365  78.863  1.00 38.91 ? 118 VAL I CG1 1 
ATOM   9742  C  CG2 . VAL I  1 118 ? 46.053  76.607  76.940  1.00 40.72 ? 118 VAL I CG2 1 
ATOM   9743  N  N   . VAL I  1 119 ? 43.280  79.301  79.394  1.00 43.57 ? 119 VAL I N   1 
ATOM   9744  C  CA  . VAL I  1 119 ? 42.439  79.542  80.560  1.00 48.27 ? 119 VAL I CA  1 
ATOM   9745  C  C   . VAL I  1 119 ? 41.596  78.291  80.788  1.00 49.54 ? 119 VAL I C   1 
ATOM   9746  O  O   . VAL I  1 119 ? 41.170  77.631  79.833  1.00 45.32 ? 119 VAL I O   1 
ATOM   9747  C  CB  . VAL I  1 119 ? 41.567  80.826  80.428  1.00 47.60 ? 119 VAL I CB  1 
ATOM   9748  C  CG1 . VAL I  1 119 ? 40.563  80.694  79.290  1.00 42.53 ? 119 VAL I CG1 1 
ATOM   9749  C  CG2 . VAL I  1 119 ? 40.858  81.139  81.748  1.00 47.77 ? 119 VAL I CG2 1 
ATOM   9750  N  N   . HIS I  1 120 ? 41.381  77.950  82.055  1.00 49.43 ? 120 HIS I N   1 
ATOM   9751  C  CA  . HIS I  1 120 ? 40.800  76.656  82.393  1.00 53.05 ? 120 HIS I CA  1 
ATOM   9752  C  C   . HIS I  1 120 ? 39.398  76.679  83.007  1.00 53.14 ? 120 HIS I C   1 
ATOM   9753  O  O   . HIS I  1 120 ? 38.843  77.734  83.325  1.00 47.28 ? 120 HIS I O   1 
ATOM   9754  C  CB  . HIS I  1 120 ? 41.744  75.879  83.306  1.00 52.67 ? 120 HIS I CB  1 
ATOM   9755  C  CG  . HIS I  1 120 ? 42.726  75.031  82.568  1.00 48.93 ? 120 HIS I CG  1 
ATOM   9756  N  ND1 . HIS I  1 120 ? 42.415  73.774  82.096  1.00 50.54 ? 120 HIS I ND1 1 
ATOM   9757  C  CD2 . HIS I  1 120 ? 44.010  75.261  82.213  1.00 45.66 ? 120 HIS I CD2 1 
ATOM   9758  C  CE1 . HIS I  1 120 ? 43.470  73.263  81.488  1.00 50.48 ? 120 HIS I CE1 1 
ATOM   9759  N  NE2 . HIS I  1 120 ? 44.452  74.145  81.548  1.00 46.94 ? 120 HIS I NE2 1 
ATOM   9760  N  N   . GLU I  1 121 ? 38.849  75.478  83.158  1.00 51.65 ? 121 GLU I N   1 
ATOM   9761  C  CA  . GLU I  1 121 ? 37.553  75.249  83.771  1.00 56.59 ? 121 GLU I CA  1 
ATOM   9762  C  C   . GLU I  1 121 ? 37.592  75.557  85.269  1.00 58.54 ? 121 GLU I C   1 
ATOM   9763  O  O   . GLU I  1 121 ? 36.978  76.526  85.727  1.00 56.47 ? 121 GLU I O   1 
ATOM   9764  C  CB  . GLU I  1 121 ? 37.163  73.789  83.537  1.00 58.62 ? 121 GLU I CB  1 
ATOM   9765  C  CG  . GLU I  1 121 ? 35.851  73.346  84.134  1.00 54.12 ? 121 GLU I CG  1 
ATOM   9766  C  CD  . GLU I  1 121 ? 35.700  71.837  84.077  1.00 58.97 ? 121 GLU I CD  1 
ATOM   9767  O  OE1 . GLU I  1 121 ? 36.482  71.194  83.348  1.00 55.65 ? 121 GLU I OE1 1 
ATOM   9768  O  OE2 . GLU I  1 121 ? 34.811  71.289  84.766  1.00 71.12 ? 121 GLU I OE2 1 
ATOM   9769  N  N   . LYS I  1 122 ? 38.340  74.742  86.014  1.00 59.77 ? 122 LYS I N   1 
ATOM   9770  C  CA  . LYS I  1 122 ? 38.359  74.797  87.478  1.00 58.45 ? 122 LYS I CA  1 
ATOM   9771  C  C   . LYS I  1 122 ? 39.611  75.457  88.059  1.00 56.87 ? 122 LYS I C   1 
ATOM   9772  O  O   . LYS I  1 122 ? 40.459  75.989  87.338  1.00 56.17 ? 122 LYS I O   1 
ATOM   9773  C  CB  . LYS I  1 122 ? 38.283  73.381  88.054  1.00 56.20 ? 122 LYS I CB  1 
ATOM   9774  C  CG  . LYS I  1 122 ? 37.294  72.448  87.386  1.00 58.45 ? 122 LYS I CG  1 
ATOM   9775  C  CD  . LYS I  1 122 ? 37.700  71.003  87.651  1.00 62.30 ? 122 LYS I CD  1 
ATOM   9776  C  CE  . LYS I  1 122 ? 36.635  70.015  87.213  1.00 62.06 ? 122 LYS I CE  1 
ATOM   9777  N  NZ  . LYS I  1 122 ? 37.073  68.615  87.477  1.00 57.13 ? 122 LYS I NZ  1 
ATOM   9778  N  N   . ALA I  1 123 ? 39.711  75.381  89.383  1.00 53.17 ? 123 ALA I N   1 
ATOM   9779  C  CA  . ALA I  1 123 ? 40.866  75.844  90.140  1.00 52.69 ? 123 ALA I CA  1 
ATOM   9780  C  C   . ALA I  1 123 ? 42.149  75.122  89.766  1.00 53.96 ? 123 ALA I C   1 
ATOM   9781  O  O   . ALA I  1 123 ? 42.171  73.895  89.661  1.00 55.90 ? 123 ALA I O   1 
ATOM   9782  C  CB  . ALA I  1 123 ? 40.613  75.636  91.619  1.00 49.41 ? 123 ALA I CB  1 
ATOM   9783  N  N   . ASP I  1 124 ? 43.224  75.886  89.594  1.00 50.55 ? 124 ASP I N   1 
ATOM   9784  C  CA  . ASP I  1 124 ? 44.558  75.309  89.591  1.00 53.24 ? 124 ASP I CA  1 
ATOM   9785  C  C   . ASP I  1 124 ? 44.937  75.127  91.061  1.00 52.90 ? 124 ASP I C   1 
ATOM   9786  O  O   . ASP I  1 124 ? 45.013  76.109  91.802  1.00 50.54 ? 124 ASP I O   1 
ATOM   9787  C  CB  . ASP I  1 124 ? 45.546  76.251  88.892  1.00 50.44 ? 124 ASP I CB  1 
ATOM   9788  C  CG  . ASP I  1 124 ? 46.909  75.616  88.673  1.00 52.39 ? 124 ASP I CG  1 
ATOM   9789  O  OD1 . ASP I  1 124 ? 47.248  74.657  89.397  1.00 50.73 ? 124 ASP I OD1 1 
ATOM   9790  O  OD2 . ASP I  1 124 ? 47.648  76.081  87.777  1.00 50.96 ? 124 ASP I OD2 1 
ATOM   9791  N  N   . ASP I  1 125 ? 45.165  73.884  91.490  1.00 53.79 ? 125 ASP I N   1 
ATOM   9792  C  CA  . ASP I  1 125 ? 45.404  73.617  92.917  1.00 57.15 ? 125 ASP I CA  1 
ATOM   9793  C  C   . ASP I  1 125 ? 46.848  73.875  93.361  1.00 56.26 ? 125 ASP I C   1 
ATOM   9794  O  O   . ASP I  1 125 ? 47.263  73.461  94.446  1.00 56.79 ? 125 ASP I O   1 
ATOM   9795  C  CB  . ASP I  1 125 ? 44.906  72.220  93.344  1.00 53.97 ? 125 ASP I CB  1 
ATOM   9796  C  CG  . ASP I  1 125 ? 45.753  71.075  92.790  1.00 56.50 ? 125 ASP I CG  1 
ATOM   9797  O  OD1 . ASP I  1 125 ? 46.964  71.253  92.549  1.00 55.47 ? 125 ASP I OD1 1 
ATOM   9798  O  OD2 . ASP I  1 125 ? 45.199  69.967  92.618  1.00 58.83 ? 125 ASP I OD2 1 
ATOM   9799  N  N   . LEU I  1 126 ? 47.604  74.544  92.495  1.00 54.02 ? 126 LEU I N   1 
ATOM   9800  C  CA  . LEU I  1 126 ? 48.945  75.033  92.810  1.00 51.15 ? 126 LEU I CA  1 
ATOM   9801  C  C   . LEU I  1 126 ? 49.918  73.944  93.288  1.00 50.88 ? 126 LEU I C   1 
ATOM   9802  O  O   . LEU I  1 126 ? 50.949  74.243  93.889  1.00 53.23 ? 126 LEU I O   1 
ATOM   9803  C  CB  . LEU I  1 126 ? 48.860  76.196  93.807  1.00 45.45 ? 126 LEU I CB  1 
ATOM   9804  C  CG  . LEU I  1 126 ? 47.728  77.193  93.514  1.00 48.34 ? 126 LEU I CG  1 
ATOM   9805  C  CD1 . LEU I  1 126 ? 47.647  78.272  94.581  1.00 43.96 ? 126 LEU I CD1 1 
ATOM   9806  C  CD2 . LEU I  1 126 ? 47.858  77.821  92.124  1.00 44.48 ? 126 LEU I CD2 1 
ATOM   9807  N  N   . GLY I  1 127 ? 49.597  72.687  92.995  1.00 52.37 ? 127 GLY I N   1 
ATOM   9808  C  CA  . GLY I  1 127 ? 50.436  71.573  93.394  1.00 53.48 ? 127 GLY I CA  1 
ATOM   9809  C  C   . GLY I  1 127 ? 50.191  71.135  94.829  1.00 57.17 ? 127 GLY I C   1 
ATOM   9810  O  O   . GLY I  1 127 ? 50.932  70.320  95.378  1.00 58.96 ? 127 GLY I O   1 
ATOM   9811  N  N   . LYS I  1 128 ? 49.139  71.677  95.433  1.00 57.27 ? 128 LYS I N   1 
ATOM   9812  C  CA  . LYS I  1 128 ? 48.819  71.409  96.832  1.00 59.08 ? 128 LYS I CA  1 
ATOM   9813  C  C   . LYS I  1 128 ? 47.499  70.647  96.967  1.00 61.72 ? 128 LYS I C   1 
ATOM   9814  O  O   . LYS I  1 128 ? 46.600  71.063  97.702  1.00 62.24 ? 128 LYS I O   1 
ATOM   9815  C  CB  . LYS I  1 128 ? 48.759  72.726  97.613  1.00 54.90 ? 128 LYS I CB  1 
ATOM   9816  C  CG  . LYS I  1 128 ? 50.067  73.513  97.592  1.00 55.32 ? 128 LYS I CG  1 
ATOM   9817  C  CD  . LYS I  1 128 ? 49.913  74.883  98.231  1.00 50.95 ? 128 LYS I CD  1 
ATOM   9818  C  CE  . LYS I  1 128 ? 48.932  75.754  97.458  1.00 52.08 ? 128 LYS I CE  1 
ATOM   9819  N  NZ  . LYS I  1 128 ? 48.709  77.077  98.118  1.00 53.05 ? 128 LYS I NZ  1 
ATOM   9820  N  N   . GLY I  1 129 ? 47.394  69.527  96.254  1.00 62.79 ? 129 GLY I N   1 
ATOM   9821  C  CA  . GLY I  1 129 ? 46.176  68.736  96.232  1.00 59.92 ? 129 GLY I CA  1 
ATOM   9822  C  C   . GLY I  1 129 ? 46.401  67.280  96.596  1.00 62.82 ? 129 GLY I C   1 
ATOM   9823  O  O   . GLY I  1 129 ? 45.476  66.468  96.535  1.00 59.73 ? 129 GLY I O   1 
ATOM   9824  N  N   . GLY I  1 130 ? 47.638  66.947  96.961  1.00 67.52 ? 130 GLY I N   1 
ATOM   9825  C  CA  . GLY I  1 130 ? 47.967  65.627  97.479  1.00 67.45 ? 130 GLY I CA  1 
ATOM   9826  C  C   . GLY I  1 130 ? 48.050  64.511  96.452  1.00 71.39 ? 130 GLY I C   1 
ATOM   9827  O  O   . GLY I  1 130 ? 48.886  63.611  96.568  1.00 69.34 ? 130 GLY I O   1 
ATOM   9828  N  N   . ASN I  1 131 ? 47.178  64.560  95.450  1.00 69.65 ? 131 ASN I N   1 
ATOM   9829  C  CA  . ASN I  1 131 ? 47.141  63.535  94.413  1.00 70.71 ? 131 ASN I CA  1 
ATOM   9830  C  C   . ASN I  1 131 ? 48.289  63.663  93.409  1.00 72.50 ? 131 ASN I C   1 
ATOM   9831  O  O   . ASN I  1 131 ? 48.980  64.687  93.364  1.00 70.93 ? 131 ASN I O   1 
ATOM   9832  C  CB  . ASN I  1 131 ? 45.797  63.570  93.686  1.00 65.28 ? 131 ASN I CB  1 
ATOM   9833  C  CG  . ASN I  1 131 ? 45.487  64.936  93.109  1.00 68.04 ? 131 ASN I CG  1 
ATOM   9834  O  OD1 . ASN I  1 131 ? 46.053  65.335  92.090  1.00 69.51 ? 131 ASN I OD1 1 
ATOM   9835  N  ND2 . ASN I  1 131 ? 44.584  65.661  93.758  1.00 67.60 ? 131 ASN I ND2 1 
ATOM   9836  N  N   . GLU I  1 132 ? 48.481  62.621  92.601  1.00 75.66 ? 132 GLU I N   1 
ATOM   9837  C  CA  . GLU I  1 132 ? 49.570  62.586  91.622  1.00 76.37 ? 132 GLU I CA  1 
ATOM   9838  C  C   . GLU I  1 132 ? 49.319  63.525  90.438  1.00 73.87 ? 132 GLU I C   1 
ATOM   9839  O  O   . GLU I  1 132 ? 50.258  63.991  89.785  1.00 69.83 ? 132 GLU I O   1 
ATOM   9840  C  CB  . GLU I  1 132 ? 49.797  61.156  91.121  1.00 80.40 ? 132 GLU I CB  1 
ATOM   9841  C  CG  . GLU I  1 132 ? 48.600  60.539  90.402  1.00 80.99 ? 132 GLU I CG  1 
ATOM   9842  C  CD  . GLU I  1 132 ? 48.997  59.374  89.513  1.00 78.92 ? 132 GLU I CD  1 
ATOM   9843  O  OE1 . GLU I  1 132 ? 50.187  59.298  89.127  1.00 68.71 ? 132 GLU I OE1 1 
ATOM   9844  O  OE2 . GLU I  1 132 ? 48.119  58.536  89.205  1.00 75.14 ? 132 GLU I OE2 1 
ATOM   9845  N  N   . GLU I  1 133 ? 48.044  63.788  90.168  1.00 74.46 ? 133 GLU I N   1 
ATOM   9846  C  CA  . GLU I  1 133 ? 47.643  64.691  89.102  1.00 68.54 ? 133 GLU I CA  1 
ATOM   9847  C  C   . GLU I  1 133 ? 47.946  66.148  89.467  1.00 68.84 ? 133 GLU I C   1 
ATOM   9848  O  O   . GLU I  1 133 ? 48.313  66.942  88.595  1.00 67.96 ? 133 GLU I O   1 
ATOM   9849  C  CB  . GLU I  1 133 ? 46.157  64.481  88.772  1.00 67.63 ? 133 GLU I CB  1 
ATOM   9850  C  CG  . GLU I  1 133 ? 45.435  65.682  88.173  1.00 64.71 ? 133 GLU I CG  1 
ATOM   9851  C  CD  . GLU I  1 133 ? 45.807  65.972  86.724  1.00 73.16 ? 133 GLU I CD  1 
ATOM   9852  O  OE1 . GLU I  1 133 ? 46.762  65.353  86.196  1.00 72.79 ? 133 GLU I OE1 1 
ATOM   9853  O  OE2 . GLU I  1 133 ? 45.129  66.828  86.111  1.00 72.58 ? 133 GLU I OE2 1 
ATOM   9854  N  N   . SER I  1 134 ? 47.819  66.488  90.753  1.00 65.62 ? 134 SER I N   1 
ATOM   9855  C  CA  . SER I  1 134 ? 48.073  67.852  91.235  1.00 61.41 ? 134 SER I CA  1 
ATOM   9856  C  C   . SER I  1 134 ? 49.535  68.286  91.116  1.00 63.12 ? 134 SER I C   1 
ATOM   9857  O  O   . SER I  1 134 ? 49.852  69.474  91.220  1.00 58.38 ? 134 SER I O   1 
ATOM   9858  C  CB  . SER I  1 134 ? 47.619  68.001  92.685  1.00 62.79 ? 134 SER I CB  1 
ATOM   9859  O  OG  . SER I  1 134 ? 48.036  69.243  93.220  1.00 58.63 ? 134 SER I OG  1 
ATOM   9860  N  N   . THR I  1 135 ? 50.419  67.316  90.907  1.00 63.70 ? 135 THR I N   1 
ATOM   9861  C  CA  . THR I  1 135 ? 51.842  67.580  90.744  1.00 62.95 ? 135 THR I CA  1 
ATOM   9862  C  C   . THR I  1 135 ? 52.199  67.874  89.286  1.00 62.04 ? 135 THR I C   1 
ATOM   9863  O  O   . THR I  1 135 ? 53.263  68.425  88.997  1.00 57.22 ? 135 THR I O   1 
ATOM   9864  C  CB  . THR I  1 135 ? 52.678  66.381  91.222  1.00 65.71 ? 135 THR I CB  1 
ATOM   9865  O  OG1 . THR I  1 135 ? 51.934  65.172  91.011  1.00 66.27 ? 135 THR I OG1 1 
ATOM   9866  C  CG2 . THR I  1 135 ? 53.014  66.515  92.701  1.00 60.52 ? 135 THR I CG2 1 
ATOM   9867  N  N   . LYS I  1 136 ? 51.301  67.502  88.375  1.00 62.98 ? 136 LYS I N   1 
ATOM   9868  C  CA  . LYS I  1 136 ? 51.535  67.655  86.942  1.00 63.04 ? 136 LYS I CA  1 
ATOM   9869  C  C   . LYS I  1 136 ? 50.718  68.791  86.339  1.00 60.69 ? 136 LYS I C   1 
ATOM   9870  O  O   . LYS I  1 136 ? 51.088  69.358  85.304  1.00 61.28 ? 136 LYS I O   1 
ATOM   9871  C  CB  . LYS I  1 136 ? 51.179  66.358  86.208  1.00 61.35 ? 136 LYS I CB  1 
ATOM   9872  C  CG  . LYS I  1 136 ? 52.014  65.172  86.633  1.00 63.71 ? 136 LYS I CG  1 
ATOM   9873  C  CD  . LYS I  1 136 ? 51.944  64.046  85.623  1.00 64.08 ? 136 LYS I CD  1 
ATOM   9874  C  CE  . LYS I  1 136 ? 53.009  63.014  85.926  1.00 60.77 ? 136 LYS I CE  1 
ATOM   9875  N  NZ  . LYS I  1 136 ? 54.337  63.670  86.105  1.00 61.93 ? 136 LYS I NZ  1 
ATOM   9876  N  N   . THR I  1 137 ? 49.613  69.126  86.995  1.00 57.44 ? 137 THR I N   1 
ATOM   9877  C  CA  . THR I  1 137 ? 48.565  69.890  86.343  1.00 54.29 ? 137 THR I CA  1 
ATOM   9878  C  C   . THR I  1 137 ? 47.931  70.945  87.236  1.00 53.30 ? 137 THR I C   1 
ATOM   9879  O  O   . THR I  1 137 ? 47.735  72.091  86.830  1.00 49.19 ? 137 THR I O   1 
ATOM   9880  C  CB  . THR I  1 137 ? 47.451  68.942  85.867  1.00 59.82 ? 137 THR I CB  1 
ATOM   9881  O  OG1 . THR I  1 137 ? 48.013  67.892  85.066  1.00 58.37 ? 137 THR I OG1 1 
ATOM   9882  C  CG2 . THR I  1 137 ? 46.418  69.698  85.064  1.00 62.88 ? 137 THR I CG2 1 
ATOM   9883  N  N   . GLY I  1 138 ? 47.595  70.547  88.454  1.00 56.89 ? 138 GLY I N   1 
ATOM   9884  C  CA  . GLY I  1 138 ? 46.872  71.419  89.356  1.00 55.65 ? 138 GLY I CA  1 
ATOM   9885  C  C   . GLY I  1 138 ? 45.375  71.191  89.278  1.00 55.29 ? 138 GLY I C   1 
ATOM   9886  O  O   . GLY I  1 138 ? 44.604  71.973  89.836  1.00 56.07 ? 138 GLY I O   1 
ATOM   9887  N  N   . ASN I  1 139 ? 44.972  70.127  88.581  1.00 56.22 ? 139 ASN I N   1 
ATOM   9888  C  CA  . ASN I  1 139 ? 43.564  69.739  88.471  1.00 57.47 ? 139 ASN I CA  1 
ATOM   9889  C  C   . ASN I  1 139 ? 42.637  70.877  88.036  1.00 60.45 ? 139 ASN I C   1 
ATOM   9890  O  O   . ASN I  1 139 ? 41.583  71.089  88.645  1.00 56.95 ? 139 ASN I O   1 
ATOM   9891  C  CB  . ASN I  1 139 ? 43.063  69.185  89.807  1.00 61.04 ? 139 ASN I CB  1 
ATOM   9892  C  CG  . ASN I  1 139 ? 43.740  67.887  90.200  1.00 62.04 ? 139 ASN I CG  1 
ATOM   9893  O  OD1 . ASN I  1 139 ? 43.202  66.806  89.974  1.00 64.27 ? 139 ASN I OD1 1 
ATOM   9894  N  ND2 . ASN I  1 139 ? 44.916  67.988  90.807  1.00 62.98 ? 139 ASN I ND2 1 
ATOM   9895  N  N   . ALA I  1 140 ? 43.022  71.608  86.994  1.00 57.88 ? 140 ALA I N   1 
ATOM   9896  C  CA  . ALA I  1 140 ? 42.275  72.804  86.604  1.00 58.74 ? 140 ALA I CA  1 
ATOM   9897  C  C   . ALA I  1 140 ? 41.094  72.526  85.664  1.00 55.64 ? 140 ALA I C   1 
ATOM   9898  O  O   . ALA I  1 140 ? 40.296  73.423  85.387  1.00 50.98 ? 140 ALA I O   1 
ATOM   9899  C  CB  . ALA I  1 140 ? 43.219  73.873  86.012  1.00 54.37 ? 140 ALA I CB  1 
ATOM   9900  N  N   . GLY I  1 141 ? 40.980  71.290  85.182  1.00 56.28 ? 141 GLY I N   1 
ATOM   9901  C  CA  . GLY I  1 141 ? 39.895  70.925  84.286  1.00 57.33 ? 141 GLY I CA  1 
ATOM   9902  C  C   . GLY I  1 141 ? 40.257  71.065  82.815  1.00 58.11 ? 141 GLY I C   1 
ATOM   9903  O  O   . GLY I  1 141 ? 41.436  71.112  82.453  1.00 54.63 ? 141 GLY I O   1 
ATOM   9904  N  N   . SER I  1 142 ? 39.238  71.134  81.963  1.00 59.86 ? 142 SER I N   1 
ATOM   9905  C  CA  . SER I  1 142 ? 39.440  71.253  80.522  1.00 57.13 ? 142 SER I CA  1 
ATOM   9906  C  C   . SER I  1 142 ? 39.855  72.669  80.121  1.00 57.94 ? 142 SER I C   1 
ATOM   9907  O  O   . SER I  1 142 ? 39.715  73.620  80.903  1.00 53.89 ? 142 SER I O   1 
ATOM   9908  C  CB  . SER I  1 142 ? 38.160  70.884  79.775  1.00 57.64 ? 142 SER I CB  1 
ATOM   9909  O  OG  . SER I  1 142 ? 37.181  71.899  79.948  1.00 54.58 ? 142 SER I OG  1 
ATOM   9910  N  N   . ARG I  1 143 ? 40.342  72.796  78.887  1.00 56.70 ? 143 ARG I N   1 
ATOM   9911  C  CA  . ARG I  1 143 ? 40.783  74.073  78.329  1.00 49.48 ? 143 ARG I CA  1 
ATOM   9912  C  C   . ARG I  1 143 ? 39.625  74.794  77.637  1.00 50.70 ? 143 ARG I C   1 
ATOM   9913  O  O   . ARG I  1 143 ? 39.063  74.294  76.658  1.00 52.06 ? 143 ARG I O   1 
ATOM   9914  C  CB  . ARG I  1 143 ? 41.943  73.836  77.357  1.00 48.56 ? 143 ARG I CB  1 
ATOM   9915  C  CG  . ARG I  1 143 ? 43.131  73.148  78.021  1.00 47.97 ? 143 ARG I CG  1 
ATOM   9916  C  CD  . ARG I  1 143 ? 44.152  72.600  77.038  1.00 46.79 ? 143 ARG I CD  1 
ATOM   9917  N  NE  . ARG I  1 143 ? 45.138  71.779  77.736  1.00 43.16 ? 143 ARG I NE  1 
ATOM   9918  C  CZ  . ARG I  1 143 ? 46.043  71.002  77.145  1.00 46.01 ? 143 ARG I CZ  1 
ATOM   9919  N  NH1 . ARG I  1 143 ? 46.106  70.926  75.821  1.00 42.63 ? 143 ARG I NH1 1 
ATOM   9920  N  NH2 . ARG I  1 143 ? 46.887  70.289  77.890  1.00 43.73 ? 143 ARG I NH2 1 
ATOM   9921  N  N   . LEU I  1 144 ? 39.279  75.973  78.150  1.00 47.94 ? 144 LEU I N   1 
ATOM   9922  C  CA  . LEU I  1 144 ? 38.064  76.679  77.727  1.00 54.94 ? 144 LEU I CA  1 
ATOM   9923  C  C   . LEU I  1 144 ? 38.269  77.727  76.627  1.00 51.33 ? 144 LEU I C   1 
ATOM   9924  O  O   . LEU I  1 144 ? 37.341  78.027  75.869  1.00 52.74 ? 144 LEU I O   1 
ATOM   9925  C  CB  . LEU I  1 144 ? 37.378  77.337  78.931  1.00 52.92 ? 144 LEU I CB  1 
ATOM   9926  C  CG  . LEU I  1 144 ? 36.976  76.443  80.107  1.00 56.53 ? 144 LEU I CG  1 
ATOM   9927  C  CD1 . LEU I  1 144 ? 36.098  77.224  81.079  1.00 53.92 ? 144 LEU I CD1 1 
ATOM   9928  C  CD2 . LEU I  1 144 ? 36.281  75.168  79.630  1.00 51.68 ? 144 LEU I CD2 1 
ATOM   9929  N  N   . ALA I  1 145 ? 39.471  78.295  76.568  1.00 46.45 ? 145 ALA I N   1 
ATOM   9930  C  CA  . ALA I  1 145 ? 39.828  79.283  75.546  1.00 47.14 ? 145 ALA I CA  1 
ATOM   9931  C  C   . ALA I  1 145 ? 41.347  79.456  75.447  1.00 47.36 ? 145 ALA I C   1 
ATOM   9932  O  O   . ALA I  1 145 ? 42.050  79.460  76.463  1.00 44.88 ? 145 ALA I O   1 
ATOM   9933  C  CB  . ALA I  1 145 ? 39.158  80.618  75.822  1.00 40.73 ? 145 ALA I CB  1 
ATOM   9934  N  N   . CYS I  1 146 ? 41.855  79.597  74.225  1.00 40.78 ? 146 CYS I N   1 
ATOM   9935  C  CA  . CYS I  1 146 ? 43.293  79.729  74.044  1.00 38.31 ? 146 CYS I CA  1 
ATOM   9936  C  C   . CYS I  1 146 ? 43.663  80.575  72.832  1.00 34.90 ? 146 CYS I C   1 
ATOM   9937  O  O   . CYS I  1 146 ? 42.817  80.925  72.017  1.00 33.23 ? 146 CYS I O   1 
ATOM   9938  C  CB  . CYS I  1 146 ? 43.942  78.355  73.933  1.00 37.76 ? 146 CYS I CB  1 
ATOM   9939  S  SG  . CYS I  1 146 ? 43.661  77.577  72.343  1.00 40.86 ? 146 CYS I SG  1 
ATOM   9940  N  N   . GLY I  1 147 ? 44.942  80.915  72.748  1.00 34.60 ? 147 GLY I N   1 
ATOM   9941  C  CA  . GLY I  1 147 ? 45.487  81.663  71.634  1.00 37.08 ? 147 GLY I CA  1 
ATOM   9942  C  C   . GLY I  1 147 ? 46.991  81.518  71.689  1.00 35.66 ? 147 GLY I C   1 
ATOM   9943  O  O   . GLY I  1 147 ? 47.547  81.310  72.770  1.00 27.47 ? 147 GLY I O   1 
ATOM   9944  N  N   . VAL I  1 148 ? 47.649  81.605  70.532  1.00 35.55 ? 148 VAL I N   1 
ATOM   9945  C  CA  . VAL I  1 148 ? 49.106  81.525  70.480  1.00 28.13 ? 148 VAL I CA  1 
ATOM   9946  C  C   . VAL I  1 148 ? 49.689  82.861  70.930  1.00 27.52 ? 148 VAL I C   1 
ATOM   9947  O  O   . VAL I  1 148 ? 49.132  83.920  70.645  1.00 29.18 ? 148 VAL I O   1 
ATOM   9948  C  CB  . VAL I  1 148 ? 49.605  81.164  69.064  1.00 29.66 ? 148 VAL I CB  1 
ATOM   9949  C  CG1 . VAL I  1 148 ? 51.141  81.108  69.024  1.00 29.01 ? 148 VAL I CG1 1 
ATOM   9950  C  CG2 . VAL I  1 148 ? 49.015  79.830  68.603  1.00 29.93 ? 148 VAL I CG2 1 
ATOM   9951  N  N   . ILE I  1 149 ? 50.798  82.825  71.654  1.00 28.57 ? 149 ILE I N   1 
ATOM   9952  C  CA  . ILE I  1 149 ? 51.374  84.066  72.148  1.00 29.90 ? 149 ILE I CA  1 
ATOM   9953  C  C   . ILE I  1 149 ? 52.184  84.708  71.021  1.00 30.62 ? 149 ILE I C   1 
ATOM   9954  O  O   . ILE I  1 149 ? 52.995  84.041  70.365  1.00 31.00 ? 149 ILE I O   1 
ATOM   9955  C  CB  . ILE I  1 149 ? 52.212  83.854  73.446  1.00 24.68 ? 149 ILE I CB  1 
ATOM   9956  C  CG1 . ILE I  1 149 ? 51.371  83.129  74.501  1.00 31.70 ? 149 ILE I CG1 1 
ATOM   9957  C  CG2 . ILE I  1 149 ? 52.680  85.189  73.994  1.00 23.89 ? 149 ILE I CG2 1 
ATOM   9958  C  CD1 . ILE I  1 149 ? 52.010  83.062  75.890  1.00 27.57 ? 149 ILE I CD1 1 
ATOM   9959  N  N   . GLY I  1 150 ? 51.937  85.991  70.771  1.00 26.48 ? 150 GLY I N   1 
ATOM   9960  C  CA  . GLY I  1 150 ? 52.521  86.638  69.615  1.00 26.99 ? 150 GLY I CA  1 
ATOM   9961  C  C   . GLY I  1 150 ? 53.174  87.968  69.913  1.00 29.58 ? 150 GLY I C   1 
ATOM   9962  O  O   . GLY I  1 150 ? 52.784  88.687  70.838  1.00 29.29 ? 150 GLY I O   1 
ATOM   9963  N  N   . ILE I  1 151 ? 54.167  88.310  69.111  1.00 20.88 ? 151 ILE I N   1 
ATOM   9964  C  CA  . ILE I  1 151 ? 54.876  89.560  69.313  1.00 24.86 ? 151 ILE I CA  1 
ATOM   9965  C  C   . ILE I  1 151 ? 53.949  90.749  69.045  1.00 29.72 ? 151 ILE I C   1 
ATOM   9966  O  O   . ILE I  1 151 ? 53.196  90.746  68.071  1.00 27.23 ? 151 ILE I O   1 
ATOM   9967  C  CB  . ILE I  1 151 ? 56.128  89.621  68.415  1.00 25.08 ? 151 ILE I CB  1 
ATOM   9968  C  CG1 . ILE I  1 151 ? 57.066  88.455  68.776  1.00 24.88 ? 151 ILE I CG1 1 
ATOM   9969  C  CG2 . ILE I  1 151 ? 56.808  90.973  68.553  1.00 24.51 ? 151 ILE I CG2 1 
ATOM   9970  C  CD1 . ILE I  1 151 ? 58.156  88.119  67.731  1.00 22.45 ? 151 ILE I CD1 1 
ATOM   9971  N  N   . ALA I  1 152 ? 53.983  91.753  69.919  1.00 27.14 ? 152 ALA I N   1 
ATOM   9972  C  CA  . ALA I  1 152 ? 53.110  92.896  69.763  1.00 27.10 ? 152 ALA I CA  1 
ATOM   9973  C  C   . ALA I  1 152 ? 53.928  94.156  69.554  1.00 31.58 ? 152 ALA I C   1 
ATOM   9974  O  O   . ALA I  1 152 ? 55.090  94.221  69.963  1.00 32.63 ? 152 ALA I O   1 
ATOM   9975  C  CB  . ALA I  1 152 ? 52.218  93.035  70.971  1.00 31.70 ? 152 ALA I CB  1 
ATOM   9976  N  N   . GLN I  1 153 ? 53.318  95.154  68.922  1.00 24.97 ? 153 GLN I N   1 
ATOM   9977  C  CA  . GLN I  1 153 ? 53.955  96.456  68.736  1.00 31.35 ? 153 GLN I CA  1 
ATOM   9978  C  C   . GLN I  1 153 ? 54.037  97.237  70.053  1.00 38.95 ? 153 GLN I C   1 
ATOM   9979  O  O   . GLN I  1 153 ? 53.100  97.211  70.859  1.00 39.93 ? 153 GLN I O   1 
ATOM   9980  C  CB  . GLN I  1 153 ? 53.178  97.284  67.711  1.00 30.01 ? 153 GLN I CB  1 
ATOM   9981  C  CG  . GLN I  1 153 ? 53.883  98.579  67.290  1.00 35.99 ? 153 GLN I CG  1 
ATOM   9982  C  CD  . GLN I  1 153 ? 53.146  99.311  66.173  1.00 39.89 ? 153 GLN I CD  1 
ATOM   9983  O  OE1 . GLN I  1 153 ? 51.916  99.439  66.199  1.00 36.35 ? 153 GLN I OE1 1 
ATOM   9984  N  NE2 . GLN I  1 153 ? 53.896  99.785  65.182  1.00 44.18 ? 153 GLN I NE2 1 
ATOM   9985  O  OXT . GLN I  1 153 ? 55.024  97.928  70.341  1.00 37.64 ? 153 GLN I OXT 1 
ATOM   9986  N  N   . ALA J  1 1   ? 66.707  71.057  64.881  1.00 50.30 ? 1   ALA J N   1 
ATOM   9987  C  CA  . ALA J  1 1   ? 65.652  70.930  63.876  1.00 42.23 ? 1   ALA J CA  1 
ATOM   9988  C  C   . ALA J  1 1   ? 64.294  71.381  64.408  1.00 41.87 ? 1   ALA J C   1 
ATOM   9989  O  O   . ALA J  1 1   ? 63.421  70.557  64.671  1.00 47.65 ? 1   ALA J O   1 
ATOM   9990  C  CB  . ALA J  1 1   ? 65.573  69.501  63.374  1.00 41.71 ? 1   ALA J CB  1 
ATOM   9991  N  N   . THR J  1 2   ? 64.109  72.688  64.558  1.00 36.64 ? 2   THR J N   1 
ATOM   9992  C  CA  . THR J  1 2   ? 62.844  73.193  65.069  1.00 29.39 ? 2   THR J CA  1 
ATOM   9993  C  C   . THR J  1 2   ? 61.744  73.147  64.007  1.00 33.33 ? 2   THR J C   1 
ATOM   9994  O  O   . THR J  1 2   ? 62.010  73.115  62.804  1.00 34.55 ? 2   THR J O   1 
ATOM   9995  C  CB  . THR J  1 2   ? 62.971  74.625  65.676  1.00 32.51 ? 2   THR J CB  1 
ATOM   9996  O  OG1 . THR J  1 2   ? 64.154  75.267  65.188  1.00 36.87 ? 2   THR J OG1 1 
ATOM   9997  C  CG2 . THR J  1 2   ? 63.058  74.560  67.175  1.00 33.74 ? 2   THR J CG2 1 
ATOM   9998  N  N   . LYS J  1 3   ? 60.501  73.110  64.466  1.00 32.39 ? 3   LYS J N   1 
ATOM   9999  C  CA  . LYS J  1 3   ? 59.347  73.060  63.585  1.00 29.96 ? 3   LYS J CA  1 
ATOM   10000 C  C   . LYS J  1 3   ? 58.321  74.035  64.112  1.00 29.63 ? 3   LYS J C   1 
ATOM   10001 O  O   . LYS J  1 3   ? 58.334  74.391  65.292  1.00 25.00 ? 3   LYS J O   1 
ATOM   10002 C  CB  . LYS J  1 3   ? 58.759  71.657  63.541  1.00 31.40 ? 3   LYS J CB  1 
ATOM   10003 C  CG  . LYS J  1 3   ? 59.753  70.623  63.090  1.00 34.00 ? 3   LYS J CG  1 
ATOM   10004 C  CD  . LYS J  1 3   ? 59.162  69.236  63.103  1.00 47.84 ? 3   LYS J CD  1 
ATOM   10005 C  CE  . LYS J  1 3   ? 60.100  68.254  62.424  1.00 48.75 ? 3   LYS J CE  1 
ATOM   10006 N  NZ  . LYS J  1 3   ? 59.649  66.853  62.636  1.00 60.06 ? 3   LYS J NZ  1 
ATOM   10007 N  N   . ALA J  1 4   ? 57.436  74.482  63.234  1.00 28.73 ? 4   ALA J N   1 
ATOM   10008 C  CA  . ALA J  1 4   ? 56.458  75.481  63.621  1.00 26.15 ? 4   ALA J CA  1 
ATOM   10009 C  C   . ALA J  1 4   ? 55.215  75.307  62.768  1.00 29.05 ? 4   ALA J C   1 
ATOM   10010 O  O   . ALA J  1 4   ? 55.237  74.600  61.751  1.00 27.59 ? 4   ALA J O   1 
ATOM   10011 C  CB  . ALA J  1 4   ? 57.046  76.886  63.482  1.00 21.97 ? 4   ALA J CB  1 
ATOM   10012 N  N   . VAL J  1 5   ? 54.116  75.922  63.183  1.00 26.11 ? 5   VAL J N   1 
ATOM   10013 C  CA  . VAL J  1 5   ? 52.855  75.640  62.518  1.00 25.61 ? 5   VAL J CA  1 
ATOM   10014 C  C   . VAL J  1 5   ? 51.953  76.848  62.595  1.00 24.85 ? 5   VAL J C   1 
ATOM   10015 O  O   . VAL J  1 5   ? 52.074  77.655  63.513  1.00 26.31 ? 5   VAL J O   1 
ATOM   10016 C  CB  . VAL J  1 5   ? 52.167  74.400  63.121  1.00 29.73 ? 5   VAL J CB  1 
ATOM   10017 C  CG1 . VAL J  1 5   ? 51.588  74.720  64.505  1.00 29.41 ? 5   VAL J CG1 1 
ATOM   10018 C  CG2 . VAL J  1 5   ? 51.101  73.866  62.180  1.00 29.96 ? 5   VAL J CG2 1 
ATOM   10019 N  N   . CYS J  1 6   ? 51.083  76.996  61.599  1.00 25.10 ? 6   CYS J N   1 
ATOM   10020 C  CA  . CYS J  1 6   ? 50.166  78.128  61.551  1.00 26.50 ? 6   CYS J CA  1 
ATOM   10021 C  C   . CYS J  1 6   ? 48.803  77.659  61.070  1.00 28.53 ? 6   CYS J C   1 
ATOM   10022 O  O   . CYS J  1 6   ? 48.696  76.916  60.088  1.00 22.17 ? 6   CYS J O   1 
ATOM   10023 C  CB  . CYS J  1 6   ? 50.688  79.235  60.624  1.00 16.55 ? 6   CYS J CB  1 
ATOM   10024 S  SG  . CYS J  1 6   ? 49.821  80.806  60.803  1.00 28.24 ? 6   CYS J SG  1 
ATOM   10025 N  N   . VAL J  1 7   ? 47.767  78.080  61.783  1.00 24.98 ? 7   VAL J N   1 
ATOM   10026 C  CA  . VAL J  1 7   ? 46.404  77.839  61.344  1.00 26.42 ? 7   VAL J CA  1 
ATOM   10027 C  C   . VAL J  1 7   ? 45.886  79.132  60.735  1.00 25.07 ? 7   VAL J C   1 
ATOM   10028 O  O   . VAL J  1 7   ? 45.863  80.182  61.379  1.00 27.30 ? 7   VAL J O   1 
ATOM   10029 C  CB  . VAL J  1 7   ? 45.500  77.384  62.509  1.00 30.37 ? 7   VAL J CB  1 
ATOM   10030 C  CG1 . VAL J  1 7   ? 44.038  77.310  62.060  1.00 27.53 ? 7   VAL J CG1 1 
ATOM   10031 C  CG2 . VAL J  1 7   ? 45.979  76.031  63.052  1.00 28.47 ? 7   VAL J CG2 1 
ATOM   10032 N  N   . LEU J  1 8   ? 45.513  79.063  59.469  1.00 24.30 ? 8   LEU J N   1 
ATOM   10033 C  CA  . LEU J  1 8   ? 45.059  80.245  58.768  1.00 23.81 ? 8   LEU J CA  1 
ATOM   10034 C  C   . LEU J  1 8   ? 43.542  80.295  58.860  1.00 23.16 ? 8   LEU J C   1 
ATOM   10035 O  O   . LEU J  1 8   ? 42.862  79.372  58.435  1.00 19.55 ? 8   LEU J O   1 
ATOM   10036 C  CB  . LEU J  1 8   ? 45.526  80.197  57.311  1.00 19.78 ? 8   LEU J CB  1 
ATOM   10037 C  CG  . LEU J  1 8   ? 47.049  80.332  57.100  1.00 22.43 ? 8   LEU J CG  1 
ATOM   10038 C  CD1 . LEU J  1 8   ? 47.454  79.921  55.691  1.00 17.19 ? 8   LEU J CD1 1 
ATOM   10039 C  CD2 . LEU J  1 8   ? 47.483  81.766  57.363  1.00 20.91 ? 8   LEU J CD2 1 
ATOM   10040 N  N   . LYS J  1 9   ? 43.024  81.375  59.423  1.00 23.23 ? 9   LYS J N   1 
ATOM   10041 C  CA  . LYS J  1 9   ? 41.589  81.553  59.544  1.00 26.77 ? 9   LYS J CA  1 
ATOM   10042 C  C   . LYS J  1 9   ? 41.223  82.986  59.242  1.00 24.69 ? 9   LYS J C   1 
ATOM   10043 O  O   . LYS J  1 9   ? 41.994  83.908  59.500  1.00 20.37 ? 9   LYS J O   1 
ATOM   10044 C  CB  . LYS J  1 9   ? 41.127  81.192  60.956  1.00 25.45 ? 9   LYS J CB  1 
ATOM   10045 C  CG  . LYS J  1 9   ? 41.260  79.720  61.270  1.00 31.46 ? 9   LYS J CG  1 
ATOM   10046 C  CD  . LYS J  1 9   ? 40.504  78.874  60.230  1.00 36.66 ? 9   LYS J CD  1 
ATOM   10047 C  CE  . LYS J  1 9   ? 40.637  77.376  60.485  1.00 33.62 ? 9   LYS J CE  1 
ATOM   10048 N  NZ  . LYS J  1 9   ? 40.144  76.994  61.849  1.00 45.31 ? 9   LYS J NZ  1 
ATOM   10049 N  N   . GLY J  1 10  ? 40.032  83.180  58.699  1.00 25.86 ? 10  GLY J N   1 
ATOM   10050 C  CA  . GLY J  1 10  ? 39.562  84.525  58.436  1.00 28.53 ? 10  GLY J CA  1 
ATOM   10051 C  C   . GLY J  1 10  ? 38.056  84.584  58.447  1.00 30.12 ? 10  GLY J C   1 
ATOM   10052 O  O   . GLY J  1 10  ? 37.395  83.610  58.793  1.00 28.49 ? 10  GLY J O   1 
ATOM   10053 N  N   . ASP J  1 11  ? 37.518  85.724  58.036  1.00 37.45 ? 11  ASP J N   1 
ATOM   10054 C  CA  . ASP J  1 11  ? 36.086  85.965  58.106  1.00 35.79 ? 11  ASP J CA  1 
ATOM   10055 C  C   . ASP J  1 11  ? 35.340  85.314  56.953  1.00 34.43 ? 11  ASP J C   1 
ATOM   10056 O  O   . ASP J  1 11  ? 34.115  85.240  56.958  1.00 40.22 ? 11  ASP J O   1 
ATOM   10057 C  CB  . ASP J  1 11  ? 35.826  87.464  58.129  1.00 35.59 ? 11  ASP J CB  1 
ATOM   10058 C  CG  . ASP J  1 11  ? 36.397  88.126  59.364  1.00 50.05 ? 11  ASP J CG  1 
ATOM   10059 O  OD1 . ASP J  1 11  ? 36.375  87.483  60.435  1.00 44.35 ? 11  ASP J OD1 1 
ATOM   10060 O  OD2 . ASP J  1 11  ? 36.871  89.283  59.269  1.00 61.17 ? 11  ASP J OD2 1 
ATOM   10061 N  N   . GLY J  1 12  ? 36.077  84.837  55.965  1.00 29.09 ? 12  GLY J N   1 
ATOM   10062 C  CA  . GLY J  1 12  ? 35.458  84.321  54.761  1.00 23.55 ? 12  GLY J CA  1 
ATOM   10063 C  C   . GLY J  1 12  ? 35.779  82.858  54.580  1.00 24.00 ? 12  GLY J C   1 
ATOM   10064 O  O   . GLY J  1 12  ? 36.099  82.172  55.540  1.00 25.16 ? 12  GLY J O   1 
ATOM   10065 N  N   . PRO J  1 13  ? 35.753  82.392  53.330  1.00 24.13 ? 13  PRO J N   1 
ATOM   10066 C  CA  . PRO J  1 13  ? 35.890  80.977  52.987  1.00 21.56 ? 13  PRO J CA  1 
ATOM   10067 C  C   . PRO J  1 13  ? 37.305  80.472  53.158  1.00 23.96 ? 13  PRO J C   1 
ATOM   10068 O  O   . PRO J  1 13  ? 37.524  79.267  53.116  1.00 26.22 ? 13  PRO J O   1 
ATOM   10069 C  CB  . PRO J  1 13  ? 35.549  80.934  51.494  1.00 23.59 ? 13  PRO J CB  1 
ATOM   10070 C  CG  . PRO J  1 13  ? 35.210  82.339  51.097  1.00 24.97 ? 13  PRO J CG  1 
ATOM   10071 C  CD  . PRO J  1 13  ? 35.711  83.251  52.141  1.00 20.07 ? 13  PRO J CD  1 
ATOM   10072 N  N   . VAL J  1 14  ? 38.267  81.368  53.311  1.00 22.76 ? 14  VAL J N   1 
ATOM   10073 C  CA  . VAL J  1 14  ? 39.652  80.919  53.265  1.00 25.23 ? 14  VAL J CA  1 
ATOM   10074 C  C   . VAL J  1 14  ? 40.129  80.406  54.609  1.00 20.16 ? 14  VAL J C   1 
ATOM   10075 O  O   . VAL J  1 14  ? 40.002  81.081  55.627  1.00 21.56 ? 14  VAL J O   1 
ATOM   10076 C  CB  . VAL J  1 14  ? 40.604  81.998  52.721  1.00 22.74 ? 14  VAL J CB  1 
ATOM   10077 C  CG1 . VAL J  1 14  ? 42.063  81.492  52.747  1.00 17.19 ? 14  VAL J CG1 1 
ATOM   10078 C  CG2 . VAL J  1 14  ? 40.170  82.389  51.302  1.00 19.62 ? 14  VAL J CG2 1 
ATOM   10079 N  N   . GLN J  1 15  ? 40.665  79.194  54.592  1.00 18.16 ? 15  GLN J N   1 
ATOM   10080 C  CA  . GLN J  1 15  ? 41.242  78.608  55.787  1.00 26.78 ? 15  GLN J CA  1 
ATOM   10081 C  C   . GLN J  1 15  ? 42.241  77.552  55.360  1.00 23.57 ? 15  GLN J C   1 
ATOM   10082 O  O   . GLN J  1 15  ? 42.109  76.976  54.270  1.00 24.88 ? 15  GLN J O   1 
ATOM   10083 C  CB  . GLN J  1 15  ? 40.146  77.993  56.665  1.00 29.89 ? 15  GLN J CB  1 
ATOM   10084 C  CG  . GLN J  1 15  ? 39.377  76.869  55.996  1.00 27.99 ? 15  GLN J CG  1 
ATOM   10085 C  CD  . GLN J  1 15  ? 38.072  76.550  56.725  1.00 44.45 ? 15  GLN J CD  1 
ATOM   10086 O  OE1 . GLN J  1 15  ? 38.065  76.314  57.938  1.00 50.14 ? 15  GLN J OE1 1 
ATOM   10087 N  NE2 . GLN J  1 15  ? 36.960  76.553  55.987  1.00 43.02 ? 15  GLN J NE2 1 
ATOM   10088 N  N   . GLY J  1 16  ? 43.238  77.300  56.206  1.00 20.39 ? 16  GLY J N   1 
ATOM   10089 C  CA  . GLY J  1 16  ? 44.230  76.276  55.910  1.00 22.45 ? 16  GLY J CA  1 
ATOM   10090 C  C   . GLY J  1 16  ? 45.241  76.064  57.021  1.00 26.23 ? 16  GLY J C   1 
ATOM   10091 O  O   . GLY J  1 16  ? 45.208  76.746  58.054  1.00 23.97 ? 16  GLY J O   1 
ATOM   10092 N  N   . ILE J  1 17  ? 46.153  75.123  56.793  1.00 24.24 ? 17  ILE J N   1 
ATOM   10093 C  CA  . ILE J  1 17  ? 47.188  74.802  57.762  1.00 20.38 ? 17  ILE J CA  1 
ATOM   10094 C  C   . ILE J  1 17  ? 48.563  74.811  57.113  1.00 23.12 ? 17  ILE J C   1 
ATOM   10095 O  O   . ILE J  1 17  ? 48.784  74.141  56.106  1.00 22.09 ? 17  ILE J O   1 
ATOM   10096 C  CB  . ILE J  1 17  ? 46.964  73.403  58.379  1.00 24.40 ? 17  ILE J CB  1 
ATOM   10097 C  CG1 . ILE J  1 17  ? 45.511  73.229  58.828  1.00 23.43 ? 17  ILE J CG1 1 
ATOM   10098 C  CG2 . ILE J  1 17  ? 47.956  73.162  59.522  1.00 26.63 ? 17  ILE J CG2 1 
ATOM   10099 C  CD1 . ILE J  1 17  ? 45.309  72.121  59.853  1.00 27.52 ? 17  ILE J CD1 1 
ATOM   10100 N  N   . ILE J  1 18  ? 49.496  75.553  57.698  1.00 19.52 ? 18  ILE J N   1 
ATOM   10101 C  CA  . ILE J  1 18  ? 50.826  75.645  57.118  1.00 22.30 ? 18  ILE J CA  1 
ATOM   10102 C  C   . ILE J  1 18  ? 51.894  75.168  58.096  1.00 24.26 ? 18  ILE J C   1 
ATOM   10103 O  O   . ILE J  1 18  ? 51.932  75.607  59.242  1.00 22.83 ? 18  ILE J O   1 
ATOM   10104 C  CB  . ILE J  1 18  ? 51.135  77.088  56.644  1.00 20.97 ? 18  ILE J CB  1 
ATOM   10105 C  CG1 . ILE J  1 18  ? 50.180  77.499  55.512  1.00 20.92 ? 18  ILE J CG1 1 
ATOM   10106 C  CG2 . ILE J  1 18  ? 52.576  77.213  56.166  1.00 21.54 ? 18  ILE J CG2 1 
ATOM   10107 C  CD1 . ILE J  1 18  ? 50.266  76.611  54.281  1.00 18.22 ? 18  ILE J CD1 1 
ATOM   10108 N  N   . ASN J  1 19  ? 52.753  74.264  57.628  1.00 25.56 ? 19  ASN J N   1 
ATOM   10109 C  CA  . ASN J  1 19  ? 53.883  73.768  58.409  1.00 24.13 ? 19  ASN J CA  1 
ATOM   10110 C  C   . ASN J  1 19  ? 55.214  74.388  58.006  1.00 28.55 ? 19  ASN J C   1 
ATOM   10111 O  O   . ASN J  1 19  ? 55.448  74.680  56.821  1.00 26.76 ? 19  ASN J O   1 
ATOM   10112 C  CB  . ASN J  1 19  ? 53.995  72.258  58.251  1.00 23.09 ? 19  ASN J CB  1 
ATOM   10113 C  CG  . ASN J  1 19  ? 52.681  71.560  58.513  1.00 32.55 ? 19  ASN J CG  1 
ATOM   10114 O  OD1 . ASN J  1 19  ? 52.175  71.577  59.646  1.00 26.58 ? 19  ASN J OD1 1 
ATOM   10115 N  ND2 . ASN J  1 19  ? 52.107  70.951  57.470  1.00 24.97 ? 19  ASN J ND2 1 
ATOM   10116 N  N   . PHE J  1 20  ? 56.084  74.576  58.994  1.00 26.52 ? 20  PHE J N   1 
ATOM   10117 C  CA  . PHE J  1 20  ? 57.444  75.051  58.766  1.00 26.84 ? 20  PHE J CA  1 
ATOM   10118 C  C   . PHE J  1 20  ? 58.424  74.071  59.368  1.00 27.80 ? 20  PHE J C   1 
ATOM   10119 O  O   . PHE J  1 20  ? 58.160  73.514  60.434  1.00 30.93 ? 20  PHE J O   1 
ATOM   10120 C  CB  . PHE J  1 20  ? 57.674  76.396  59.441  1.00 23.40 ? 20  PHE J CB  1 
ATOM   10121 C  CG  . PHE J  1 20  ? 56.780  77.493  58.960  1.00 25.28 ? 20  PHE J CG  1 
ATOM   10122 C  CD1 . PHE J  1 20  ? 55.492  77.628  59.467  1.00 25.19 ? 20  PHE J CD1 1 
ATOM   10123 C  CD2 . PHE J  1 20  ? 57.242  78.428  58.046  1.00 19.61 ? 20  PHE J CD2 1 
ATOM   10124 C  CE1 . PHE J  1 20  ? 54.676  78.654  59.049  1.00 23.47 ? 20  PHE J CE1 1 
ATOM   10125 C  CE2 . PHE J  1 20  ? 56.430  79.454  57.631  1.00 21.24 ? 20  PHE J CE2 1 
ATOM   10126 C  CZ  . PHE J  1 20  ? 55.144  79.575  58.138  1.00 19.36 ? 20  PHE J CZ  1 
ATOM   10127 N  N   . GLU J  1 21  ? 59.572  73.899  58.720  1.00 27.37 ? 21  GLU J N   1 
ATOM   10128 C  CA  . GLU J  1 21  ? 60.583  72.952  59.191  1.00 31.17 ? 21  GLU J CA  1 
ATOM   10129 C  C   . GLU J  1 21  ? 62.008  73.378  58.831  1.00 33.22 ? 21  GLU J C   1 
ATOM   10130 O  O   . GLU J  1 21  ? 62.338  73.506  57.651  1.00 28.10 ? 21  GLU J O   1 
ATOM   10131 C  CB  . GLU J  1 21  ? 60.313  71.564  58.617  1.00 33.92 ? 21  GLU J CB  1 
ATOM   10132 C  CG  . GLU J  1 21  ? 61.241  70.484  59.162  1.00 43.28 ? 21  GLU J CG  1 
ATOM   10133 C  CD  . GLU J  1 21  ? 61.007  69.119  58.520  1.00 51.25 ? 21  GLU J CD  1 
ATOM   10134 O  OE1 . GLU J  1 21  ? 61.414  68.103  59.128  1.00 51.78 ? 21  GLU J OE1 1 
ATOM   10135 O  OE2 . GLU J  1 21  ? 60.426  69.064  57.409  1.00 47.10 ? 21  GLU J OE2 1 
ATOM   10136 N  N   . GLN J  1 22  ? 62.854  73.569  59.844  1.00 26.11 ? 22  GLN J N   1 
ATOM   10137 C  CA  . GLN J  1 22  ? 64.234  74.008  59.615  1.00 30.51 ? 22  GLN J CA  1 
ATOM   10138 C  C   . GLN J  1 22  ? 65.219  73.063  60.288  1.00 35.50 ? 22  GLN J C   1 
ATOM   10139 O  O   . GLN J  1 22  ? 65.392  73.115  61.494  1.00 34.33 ? 22  GLN J O   1 
ATOM   10140 C  CB  . GLN J  1 22  ? 64.447  75.426  60.161  1.00 30.66 ? 22  GLN J CB  1 
ATOM   10141 C  CG  . GLN J  1 22  ? 65.771  76.066  59.766  1.00 25.72 ? 22  GLN J CG  1 
ATOM   10142 C  CD  . GLN J  1 22  ? 65.967  77.437  60.382  1.00 29.18 ? 22  GLN J CD  1 
ATOM   10143 O  OE1 . GLN J  1 22  ? 65.353  77.768  61.406  1.00 31.32 ? 22  GLN J OE1 1 
ATOM   10144 N  NE2 . GLN J  1 22  ? 66.817  78.255  59.758  1.00 25.08 ? 22  GLN J NE2 1 
ATOM   10145 N  N   . LYS J  1 23  ? 65.875  72.213  59.509  1.00 36.78 ? 23  LYS J N   1 
ATOM   10146 C  CA  . LYS J  1 23  ? 66.799  71.225  60.074  1.00 44.22 ? 23  LYS J CA  1 
ATOM   10147 C  C   . LYS J  1 23  ? 68.047  71.820  60.748  1.00 41.13 ? 23  LYS J C   1 
ATOM   10148 O  O   . LYS J  1 23  ? 68.381  71.452  61.875  1.00 39.06 ? 23  LYS J O   1 
ATOM   10149 C  CB  . LYS J  1 23  ? 67.176  70.177  59.021  1.00 46.26 ? 23  LYS J CB  1 
ATOM   10150 C  CG  . LYS J  1 23  ? 65.994  69.311  58.603  1.00 51.37 ? 23  LYS J CG  1 
ATOM   10151 C  CD  . LYS J  1 23  ? 66.305  68.480  57.370  1.00 57.16 ? 23  LYS J CD  1 
ATOM   10152 C  CE  . LYS J  1 23  ? 65.109  67.622  56.976  1.00 59.15 ? 23  LYS J CE  1 
ATOM   10153 N  NZ  . LYS J  1 23  ? 65.309  66.986  55.640  1.00 58.62 ? 23  LYS J NZ  1 
ATOM   10154 N  N   . GLU J  1 24  ? 68.735  72.734  60.074  1.00 38.43 ? 24  GLU J N   1 
ATOM   10155 C  CA  . GLU J  1 24  ? 69.859  73.416  60.703  1.00 35.81 ? 24  GLU J CA  1 
ATOM   10156 C  C   . GLU J  1 24  ? 69.510  74.845  61.062  1.00 37.63 ? 24  GLU J C   1 
ATOM   10157 O  O   . GLU J  1 24  ? 68.704  75.471  60.389  1.00 38.10 ? 24  GLU J O   1 
ATOM   10158 C  CB  . GLU J  1 24  ? 71.049  73.428  59.770  1.00 44.19 ? 24  GLU J CB  1 
ATOM   10159 C  CG  . GLU J  1 24  ? 71.485  72.060  59.337  1.00 48.95 ? 24  GLU J CG  1 
ATOM   10160 C  CD  . GLU J  1 24  ? 72.671  72.132  58.410  1.00 57.71 ? 24  GLU J CD  1 
ATOM   10161 O  OE1 . GLU J  1 24  ? 72.916  73.227  57.856  1.00 62.69 ? 24  GLU J OE1 1 
ATOM   10162 O  OE2 . GLU J  1 24  ? 73.359  71.102  58.239  1.00 67.42 ? 24  GLU J OE2 1 
ATOM   10163 N  N   . SER J  1 25  ? 70.146  75.367  62.103  1.00 30.92 ? 25  SER J N   1 
ATOM   10164 C  CA  . SER J  1 25  ? 69.924  76.745  62.547  1.00 37.18 ? 25  SER J CA  1 
ATOM   10165 C  C   . SER J  1 25  ? 70.169  77.778  61.447  1.00 35.16 ? 25  SER J C   1 
ATOM   10166 O  O   . SER J  1 25  ? 69.554  78.849  61.413  1.00 37.46 ? 25  SER J O   1 
ATOM   10167 C  CB  . SER J  1 25  ? 70.836  77.054  63.744  1.00 40.74 ? 25  SER J CB  1 
ATOM   10168 O  OG  . SER J  1 25  ? 70.841  78.441  64.042  1.00 44.14 ? 25  SER J OG  1 
ATOM   10169 N  N   . ASN J  1 26  ? 71.082  77.446  60.552  1.00 35.02 ? 26  ASN J N   1 
ATOM   10170 C  CA  . ASN J  1 26  ? 71.535  78.370  59.529  1.00 42.36 ? 26  ASN J CA  1 
ATOM   10171 C  C   . ASN J  1 26  ? 71.005  77.970  58.153  1.00 40.61 ? 26  ASN J C   1 
ATOM   10172 O  O   . ASN J  1 26  ? 71.524  78.404  57.120  1.00 45.89 ? 26  ASN J O   1 
ATOM   10173 C  CB  . ASN J  1 26  ? 73.062  78.356  59.511  1.00 36.74 ? 26  ASN J CB  1 
ATOM   10174 C  CG  . ASN J  1 26  ? 73.628  76.937  59.508  1.00 46.07 ? 26  ASN J CG  1 
ATOM   10175 O  OD1 . ASN J  1 26  ? 73.722  76.292  58.457  1.00 50.31 ? 26  ASN J OD1 1 
ATOM   10176 N  ND2 . ASN J  1 26  ? 73.996  76.441  60.691  1.00 46.57 ? 26  ASN J ND2 1 
ATOM   10177 N  N   . GLY J  1 27  ? 69.983  77.125  58.138  1.00 35.48 ? 27  GLY J N   1 
ATOM   10178 C  CA  . GLY J  1 27  ? 69.594  76.474  56.904  1.00 36.31 ? 27  GLY J CA  1 
ATOM   10179 C  C   . GLY J  1 27  ? 68.238  76.886  56.384  1.00 28.04 ? 27  GLY J C   1 
ATOM   10180 O  O   . GLY J  1 27  ? 67.555  77.704  56.993  1.00 26.36 ? 27  GLY J O   1 
ATOM   10181 N  N   . PRO J  1 28  ? 67.842  76.303  55.249  1.00 28.99 ? 28  PRO J N   1 
ATOM   10182 C  CA  . PRO J  1 28  ? 66.582  76.613  54.579  1.00 28.54 ? 28  PRO J CA  1 
ATOM   10183 C  C   . PRO J  1 28  ? 65.389  76.220  55.438  1.00 29.54 ? 28  PRO J C   1 
ATOM   10184 O  O   . PRO J  1 28  ? 65.473  75.317  56.280  1.00 31.61 ? 28  PRO J O   1 
ATOM   10185 C  CB  . PRO J  1 28  ? 66.623  75.725  53.335  1.00 29.19 ? 28  PRO J CB  1 
ATOM   10186 C  CG  . PRO J  1 28  ? 68.044  75.339  53.176  1.00 27.39 ? 28  PRO J CG  1 
ATOM   10187 C  CD  . PRO J  1 28  ? 68.578  75.240  54.548  1.00 29.95 ? 28  PRO J CD  1 
ATOM   10188 N  N   . VAL J  1 29  ? 64.275  76.898  55.226  1.00 25.03 ? 29  VAL J N   1 
ATOM   10189 C  CA  . VAL J  1 29  ? 63.057  76.542  55.918  1.00 22.52 ? 29  VAL J CA  1 
ATOM   10190 C  C   . VAL J  1 29  ? 62.060  76.034  54.891  1.00 25.76 ? 29  VAL J C   1 
ATOM   10191 O  O   . VAL J  1 29  ? 61.695  76.760  53.954  1.00 25.25 ? 29  VAL J O   1 
ATOM   10192 C  CB  . VAL J  1 29  ? 62.464  77.751  56.641  1.00 18.10 ? 29  VAL J CB  1 
ATOM   10193 C  CG1 . VAL J  1 29  ? 61.160  77.368  57.337  1.00 17.94 ? 29  VAL J CG1 1 
ATOM   10194 C  CG2 . VAL J  1 29  ? 63.462  78.320  57.622  1.00 20.06 ? 29  VAL J CG2 1 
ATOM   10195 N  N   . LYS J  1 30  ? 61.634  74.786  55.046  1.00 23.24 ? 30  LYS J N   1 
ATOM   10196 C  CA  . LYS J  1 30  ? 60.569  74.251  54.208  1.00 24.86 ? 30  LYS J CA  1 
ATOM   10197 C  C   . LYS J  1 30  ? 59.220  74.685  54.744  1.00 24.76 ? 30  LYS J C   1 
ATOM   10198 O  O   . LYS J  1 30  ? 58.999  74.743  55.950  1.00 24.62 ? 30  LYS J O   1 
ATOM   10199 C  CB  . LYS J  1 30  ? 60.665  72.736  54.072  1.00 26.75 ? 30  LYS J CB  1 
ATOM   10200 C  CG  . LYS J  1 30  ? 61.897  72.309  53.310  1.00 32.05 ? 30  LYS J CG  1 
ATOM   10201 C  CD  . LYS J  1 30  ? 61.785  70.886  52.797  1.00 39.41 ? 30  LYS J CD  1 
ATOM   10202 C  CE  . LYS J  1 30  ? 63.042  70.493  52.028  1.00 42.72 ? 30  LYS J CE  1 
ATOM   10203 N  NZ  . LYS J  1 30  ? 62.904  69.173  51.345  1.00 48.14 ? 30  LYS J NZ  1 
ATOM   10204 N  N   . VAL J  1 31  ? 58.326  75.030  53.833  1.00 25.48 ? 31  VAL J N   1 
ATOM   10205 C  CA  . VAL J  1 31  ? 57.043  75.594  54.197  1.00 21.94 ? 31  VAL J CA  1 
ATOM   10206 C  C   . VAL J  1 31  ? 56.013  74.896  53.357  1.00 24.50 ? 31  VAL J C   1 
ATOM   10207 O  O   . VAL J  1 31  ? 56.024  75.043  52.144  1.00 24.57 ? 31  VAL J O   1 
ATOM   10208 C  CB  . VAL J  1 31  ? 56.966  77.078  53.823  1.00 24.08 ? 31  VAL J CB  1 
ATOM   10209 C  CG1 . VAL J  1 31  ? 55.578  77.641  54.152  1.00 16.27 ? 31  VAL J CG1 1 
ATOM   10210 C  CG2 . VAL J  1 31  ? 58.071  77.867  54.510  1.00 18.51 ? 31  VAL J CG2 1 
ATOM   10211 N  N   . TRP J  1 32  ? 55.127  74.131  53.983  1.00 24.87 ? 32  TRP J N   1 
ATOM   10212 C  CA  . TRP J  1 32  ? 54.153  73.366  53.227  1.00 26.21 ? 32  TRP J CA  1 
ATOM   10213 C  C   . TRP J  1 32  ? 52.854  73.147  53.994  1.00 25.93 ? 32  TRP J C   1 
ATOM   10214 O  O   . TRP J  1 32  ? 52.793  73.303  55.217  1.00 31.47 ? 32  TRP J O   1 
ATOM   10215 C  CB  . TRP J  1 32  ? 54.733  72.015  52.823  1.00 23.30 ? 32  TRP J CB  1 
ATOM   10216 C  CG  . TRP J  1 32  ? 54.548  71.026  53.911  1.00 33.40 ? 32  TRP J CG  1 
ATOM   10217 C  CD1 . TRP J  1 32  ? 53.491  70.173  54.079  1.00 30.20 ? 32  TRP J CD1 1 
ATOM   10218 C  CD2 . TRP J  1 32  ? 55.419  70.813  55.026  1.00 31.59 ? 32  TRP J CD2 1 
ATOM   10219 N  NE1 . TRP J  1 32  ? 53.664  69.430  55.218  1.00 33.45 ? 32  TRP J NE1 1 
ATOM   10220 C  CE2 . TRP J  1 32  ? 54.839  69.800  55.820  1.00 30.85 ? 32  TRP J CE2 1 
ATOM   10221 C  CE3 . TRP J  1 32  ? 56.637  71.376  55.428  1.00 30.74 ? 32  TRP J CE3 1 
ATOM   10222 C  CZ2 . TRP J  1 32  ? 55.435  69.334  56.992  1.00 31.45 ? 32  TRP J CZ2 1 
ATOM   10223 C  CZ3 . TRP J  1 32  ? 57.230  70.911  56.593  1.00 32.92 ? 32  TRP J CZ3 1 
ATOM   10224 C  CH2 . TRP J  1 32  ? 56.628  69.899  57.361  1.00 34.55 ? 32  TRP J CH2 1 
ATOM   10225 N  N   . GLY J  1 33  ? 51.821  72.750  53.263  1.00 26.30 ? 33  GLY J N   1 
ATOM   10226 C  CA  . GLY J  1 33  ? 50.498  72.576  53.831  1.00 26.07 ? 33  GLY J CA  1 
ATOM   10227 C  C   . GLY J  1 33  ? 49.459  72.737  52.739  1.00 27.91 ? 33  GLY J C   1 
ATOM   10228 O  O   . GLY J  1 33  ? 49.793  72.779  51.555  1.00 30.16 ? 33  GLY J O   1 
ATOM   10229 N  N   . SER J  1 34  ? 48.195  72.832  53.123  1.00 23.91 ? 34  SER J N   1 
ATOM   10230 C  CA  . SER J  1 34  ? 47.156  73.029  52.135  1.00 24.80 ? 34  SER J CA  1 
ATOM   10231 C  C   . SER J  1 34  ? 46.325  74.232  52.526  1.00 26.96 ? 34  SER J C   1 
ATOM   10232 O  O   . SER J  1 34  ? 46.077  74.459  53.714  1.00 28.91 ? 34  SER J O   1 
ATOM   10233 C  CB  . SER J  1 34  ? 46.283  71.781  52.003  1.00 27.17 ? 34  SER J CB  1 
ATOM   10234 O  OG  . SER J  1 34  ? 46.394  71.213  50.698  1.00 36.74 ? 34  SER J OG  1 
ATOM   10235 N  N   . ILE J  1 35  ? 45.922  75.021  51.532  1.00 24.86 ? 35  ILE J N   1 
ATOM   10236 C  CA  . ILE J  1 35  ? 45.007  76.130  51.780  1.00 25.33 ? 35  ILE J CA  1 
ATOM   10237 C  C   . ILE J  1 35  ? 43.803  75.988  50.870  1.00 21.58 ? 35  ILE J C   1 
ATOM   10238 O  O   . ILE J  1 35  ? 43.951  75.654  49.697  1.00 22.45 ? 35  ILE J O   1 
ATOM   10239 C  CB  . ILE J  1 35  ? 45.665  77.499  51.542  1.00 24.26 ? 35  ILE J CB  1 
ATOM   10240 C  CG1 . ILE J  1 35  ? 47.064  77.540  52.168  1.00 18.97 ? 35  ILE J CG1 1 
ATOM   10241 C  CG2 . ILE J  1 35  ? 44.776  78.617  52.087  1.00 19.96 ? 35  ILE J CG2 1 
ATOM   10242 C  CD1 . ILE J  1 35  ? 47.663  78.936  52.201  1.00 18.37 ? 35  ILE J CD1 1 
ATOM   10243 N  N   . LYS J  1 36  ? 42.608  76.209  51.408  1.00 21.31 ? 36  LYS J N   1 
ATOM   10244 C  CA  . LYS J  1 36  ? 41.405  76.039  50.597  1.00 20.47 ? 36  LYS J CA  1 
ATOM   10245 C  C   . LYS J  1 36  ? 40.444  77.206  50.721  1.00 19.14 ? 36  LYS J C   1 
ATOM   10246 O  O   . LYS J  1 36  ? 40.599  78.057  51.582  1.00 20.66 ? 36  LYS J O   1 
ATOM   10247 C  CB  . LYS J  1 36  ? 40.713  74.701  50.904  1.00 25.26 ? 36  LYS J CB  1 
ATOM   10248 C  CG  . LYS J  1 36  ? 40.712  74.309  52.370  1.00 30.15 ? 36  LYS J CG  1 
ATOM   10249 C  CD  . LYS J  1 36  ? 39.823  73.087  52.651  1.00 37.58 ? 36  LYS J CD  1 
ATOM   10250 C  CE  . LYS J  1 36  ? 38.509  73.507  53.343  1.00 38.35 ? 36  LYS J CE  1 
ATOM   10251 N  NZ  . LYS J  1 36  ? 37.795  72.359  53.977  1.00 44.62 ? 36  LYS J NZ  1 
ATOM   10252 N  N   . GLY J  1 37  ? 39.452  77.241  49.836  1.00 23.95 ? 37  GLY J N   1 
ATOM   10253 C  CA  . GLY J  1 37  ? 38.480  78.316  49.811  1.00 18.34 ? 37  GLY J CA  1 
ATOM   10254 C  C   . GLY J  1 37  ? 38.966  79.521  49.026  1.00 20.73 ? 37  GLY J C   1 
ATOM   10255 O  O   . GLY J  1 37  ? 38.363  80.586  49.104  1.00 21.37 ? 37  GLY J O   1 
ATOM   10256 N  N   . LEU J  1 38  ? 40.046  79.345  48.264  1.00 20.93 ? 38  LEU J N   1 
ATOM   10257 C  CA  . LEU J  1 38  ? 40.679  80.434  47.507  1.00 20.37 ? 38  LEU J CA  1 
ATOM   10258 C  C   . LEU J  1 38  ? 40.167  80.529  46.078  1.00 20.05 ? 38  LEU J C   1 
ATOM   10259 O  O   . LEU J  1 38  ? 39.800  79.533  45.496  1.00 20.26 ? 38  LEU J O   1 
ATOM   10260 C  CB  . LEU J  1 38  ? 42.180  80.179  47.406  1.00 15.55 ? 38  LEU J CB  1 
ATOM   10261 C  CG  . LEU J  1 38  ? 43.069  80.335  48.628  1.00 17.46 ? 38  LEU J CG  1 
ATOM   10262 C  CD1 . LEU J  1 38  ? 44.380  79.611  48.376  1.00 16.99 ? 38  LEU J CD1 1 
ATOM   10263 C  CD2 . LEU J  1 38  ? 43.298  81.817  48.910  1.00 19.14 ? 38  LEU J CD2 1 
ATOM   10264 N  N   . THR J  1 39  ? 40.188  81.715  45.487  1.00 18.53 ? 39  THR J N   1 
ATOM   10265 C  CA  . THR J  1 39  ? 39.973  81.790  44.047  1.00 20.40 ? 39  THR J CA  1 
ATOM   10266 C  C   . THR J  1 39  ? 41.174  81.231  43.296  1.00 24.07 ? 39  THR J C   1 
ATOM   10267 O  O   . THR J  1 39  ? 42.332  81.360  43.746  1.00 18.67 ? 39  THR J O   1 
ATOM   10268 C  CB  . THR J  1 39  ? 39.712  83.214  43.584  1.00 19.45 ? 39  THR J CB  1 
ATOM   10269 O  OG1 . THR J  1 39  ? 40.760  84.065  44.077  1.00 22.76 ? 39  THR J OG1 1 
ATOM   10270 C  CG2 . THR J  1 39  ? 38.365  83.689  44.114  1.00 16.62 ? 39  THR J CG2 1 
ATOM   10271 N  N   . GLU J  1 40  ? 40.899  80.612  42.151  1.00 20.31 ? 40  GLU J N   1 
ATOM   10272 C  CA  . GLU J  1 40  ? 41.959  80.046  41.330  1.00 21.73 ? 40  GLU J CA  1 
ATOM   10273 C  C   . GLU J  1 40  ? 43.008  81.097  40.978  1.00 20.76 ? 40  GLU J C   1 
ATOM   10274 O  O   . GLU J  1 40  ? 42.688  82.266  40.781  1.00 18.32 ? 40  GLU J O   1 
ATOM   10275 C  CB  . GLU J  1 40  ? 41.389  79.443  40.045  1.00 24.04 ? 40  GLU J CB  1 
ATOM   10276 C  CG  . GLU J  1 40  ? 42.386  78.545  39.340  1.00 25.93 ? 40  GLU J CG  1 
ATOM   10277 C  CD  . GLU J  1 40  ? 41.878  77.976  38.031  1.00 38.54 ? 40  GLU J CD  1 
ATOM   10278 O  OE1 . GLU J  1 40  ? 40.794  78.394  37.553  1.00 34.50 ? 40  GLU J OE1 1 
ATOM   10279 O  OE2 . GLU J  1 40  ? 42.581  77.100  37.474  1.00 49.04 ? 40  GLU J OE2 1 
ATOM   10280 N  N   . GLY J  1 41  ? 44.263  80.674  40.900  1.00 18.74 ? 41  GLY J N   1 
ATOM   10281 C  CA  . GLY J  1 41  ? 45.332  81.592  40.577  1.00 21.33 ? 41  GLY J CA  1 
ATOM   10282 C  C   . GLY J  1 41  ? 46.251  81.925  41.744  1.00 18.31 ? 41  GLY J C   1 
ATOM   10283 O  O   . GLY J  1 41  ? 46.231  81.255  42.785  1.00 19.39 ? 41  GLY J O   1 
ATOM   10284 N  N   . LEU J  1 42  ? 47.051  82.970  41.550  1.00 16.12 ? 42  LEU J N   1 
ATOM   10285 C  CA  . LEU J  1 42  ? 48.112  83.372  42.479  1.00 18.09 ? 42  LEU J CA  1 
ATOM   10286 C  C   . LEU J  1 42  ? 47.583  84.138  43.690  1.00 16.28 ? 42  LEU J C   1 
ATOM   10287 O  O   . LEU J  1 42  ? 46.629  84.912  43.593  1.00 16.40 ? 42  LEU J O   1 
ATOM   10288 C  CB  . LEU J  1 42  ? 49.131  84.254  41.752  1.00 15.35 ? 42  LEU J CB  1 
ATOM   10289 C  CG  . LEU J  1 42  ? 50.403  83.742  41.050  1.00 20.79 ? 42  LEU J CG  1 
ATOM   10290 C  CD1 . LEU J  1 42  ? 50.730  82.278  41.297  1.00 19.65 ? 42  LEU J CD1 1 
ATOM   10291 C  CD2 . LEU J  1 42  ? 50.410  84.050  39.578  1.00 19.55 ? 42  LEU J CD2 1 
ATOM   10292 N  N   . HIS J  1 43  ? 48.224  83.938  44.830  1.00 14.25 ? 43  HIS J N   1 
ATOM   10293 C  CA  . HIS J  1 43  ? 47.874  84.686  46.028  1.00 16.05 ? 43  HIS J CA  1 
ATOM   10294 C  C   . HIS J  1 43  ? 49.125  85.010  46.802  1.00 12.51 ? 43  HIS J C   1 
ATOM   10295 O  O   . HIS J  1 43  ? 49.944  84.127  47.045  1.00 14.11 ? 43  HIS J O   1 
ATOM   10296 C  CB  . HIS J  1 43  ? 46.911  83.877  46.914  1.00 15.74 ? 43  HIS J CB  1 
ATOM   10297 C  CG  . HIS J  1 43  ? 45.555  83.696  46.312  1.00 15.13 ? 43  HIS J CG  1 
ATOM   10298 N  ND1 . HIS J  1 43  ? 44.526  84.594  46.517  1.00 18.99 ? 43  HIS J ND1 1 
ATOM   10299 C  CD2 . HIS J  1 43  ? 45.061  82.735  45.496  1.00 16.05 ? 43  HIS J CD2 1 
ATOM   10300 C  CE1 . HIS J  1 43  ? 43.453  84.186  45.861  1.00 17.83 ? 43  HIS J CE1 1 
ATOM   10301 N  NE2 . HIS J  1 43  ? 43.750  83.058  45.239  1.00 20.14 ? 43  HIS J NE2 1 
ATOM   10302 N  N   . GLY J  1 44  ? 49.264  86.280  47.170  1.00 12.14 ? 44  GLY J N   1 
ATOM   10303 C  CA  . GLY J  1 44  ? 50.346  86.745  48.011  1.00 11.98 ? 44  GLY J CA  1 
ATOM   10304 C  C   . GLY J  1 44  ? 50.405  85.929  49.294  1.00 16.55 ? 44  GLY J C   1 
ATOM   10305 O  O   . GLY J  1 44  ? 49.363  85.542  49.861  1.00 13.56 ? 44  GLY J O   1 
ATOM   10306 N  N   . PHE J  1 45  ? 51.631  85.663  49.738  1.00 13.96 ? 45  PHE J N   1 
ATOM   10307 C  CA  . PHE J  1 45  ? 51.886  84.775  50.862  1.00 13.16 ? 45  PHE J CA  1 
ATOM   10308 C  C   . PHE J  1 45  ? 53.043  85.347  51.668  1.00 12.15 ? 45  PHE J C   1 
ATOM   10309 O  O   . PHE J  1 45  ? 54.206  85.254  51.268  1.00 12.23 ? 45  PHE J O   1 
ATOM   10310 C  CB  . PHE J  1 45  ? 52.215  83.392  50.317  1.00 14.41 ? 45  PHE J CB  1 
ATOM   10311 C  CG  . PHE J  1 45  ? 52.199  82.286  51.351  1.00 15.38 ? 45  PHE J CG  1 
ATOM   10312 C  CD1 . PHE J  1 45  ? 51.044  81.990  52.054  1.00 16.58 ? 45  PHE J CD1 1 
ATOM   10313 C  CD2 . PHE J  1 45  ? 53.332  81.508  51.569  1.00 14.02 ? 45  PHE J CD2 1 
ATOM   10314 C  CE1 . PHE J  1 45  ? 51.024  80.950  52.978  1.00 18.40 ? 45  PHE J CE1 1 
ATOM   10315 C  CE2 . PHE J  1 45  ? 53.327  80.470  52.490  1.00 19.75 ? 45  PHE J CE2 1 
ATOM   10316 C  CZ  . PHE J  1 45  ? 52.166  80.184  53.195  1.00 19.06 ? 45  PHE J CZ  1 
ATOM   10317 N  N   . HIS J  1 46  ? 52.723  85.964  52.794  1.00 11.35 ? 46  HIS J N   1 
ATOM   10318 C  CA  . HIS J  1 46  ? 53.698  86.750  53.538  1.00 13.41 ? 46  HIS J CA  1 
ATOM   10319 C  C   . HIS J  1 46  ? 53.743  86.496  55.050  1.00 18.93 ? 46  HIS J C   1 
ATOM   10320 O  O   . HIS J  1 46  ? 52.722  86.166  55.681  1.00 18.53 ? 46  HIS J O   1 
ATOM   10321 C  CB  . HIS J  1 46  ? 53.394  88.230  53.327  1.00 15.50 ? 46  HIS J CB  1 
ATOM   10322 C  CG  . HIS J  1 46  ? 53.208  88.607  51.893  1.00 13.93 ? 46  HIS J CG  1 
ATOM   10323 N  ND1 . HIS J  1 46  ? 52.264  89.521  51.483  1.00 15.19 ? 46  HIS J ND1 1 
ATOM   10324 C  CD2 . HIS J  1 46  ? 53.859  88.209  50.774  1.00 11.27 ? 46  HIS J CD2 1 
ATOM   10325 C  CE1 . HIS J  1 46  ? 52.322  89.653  50.170  1.00 16.92 ? 46  HIS J CE1 1 
ATOM   10326 N  NE2 . HIS J  1 46  ? 53.282  88.868  49.715  1.00 16.20 ? 46  HIS J NE2 1 
ATOM   10327 N  N   . VAL J  1 47  ? 54.920  86.683  55.642  1.00 15.83 ? 47  VAL J N   1 
ATOM   10328 C  CA  . VAL J  1 47  ? 54.990  86.791  57.085  1.00 14.52 ? 47  VAL J CA  1 
ATOM   10329 C  C   . VAL J  1 47  ? 54.866  88.264  57.456  1.00 17.10 ? 47  VAL J C   1 
ATOM   10330 O  O   . VAL J  1 47  ? 55.610  89.110  56.947  1.00 14.64 ? 47  VAL J O   1 
ATOM   10331 C  CB  . VAL J  1 47  ? 56.277  86.189  57.664  1.00 14.29 ? 47  VAL J CB  1 
ATOM   10332 C  CG1 . VAL J  1 47  ? 56.296  86.360  59.150  1.00 15.76 ? 47  VAL J CG1 1 
ATOM   10333 C  CG2 . VAL J  1 47  ? 56.376  84.721  57.327  1.00 13.88 ? 47  VAL J CG2 1 
ATOM   10334 N  N   . HIS J  1 48  ? 53.893  88.575  58.311  1.00 15.75 ? 48  HIS J N   1 
ATOM   10335 C  CA  . HIS J  1 48  ? 53.700  89.949  58.790  1.00 17.61 ? 48  HIS J CA  1 
ATOM   10336 C  C   . HIS J  1 48  ? 54.328  90.168  60.170  1.00 18.49 ? 48  HIS J C   1 
ATOM   10337 O  O   . HIS J  1 48  ? 54.487  89.226  60.941  1.00 15.32 ? 48  HIS J O   1 
ATOM   10338 C  CB  . HIS J  1 48  ? 52.218  90.297  58.830  1.00 18.80 ? 48  HIS J CB  1 
ATOM   10339 C  CG  . HIS J  1 48  ? 51.648  90.643  57.495  1.00 18.39 ? 48  HIS J CG  1 
ATOM   10340 N  ND1 . HIS J  1 48  ? 51.183  91.904  57.192  1.00 19.99 ? 48  HIS J ND1 1 
ATOM   10341 C  CD2 . HIS J  1 48  ? 51.479  89.900  56.378  1.00 15.50 ? 48  HIS J CD2 1 
ATOM   10342 C  CE1 . HIS J  1 48  ? 50.735  91.918  55.952  1.00 18.15 ? 48  HIS J CE1 1 
ATOM   10343 N  NE2 . HIS J  1 48  ? 50.896  90.712  55.438  1.00 17.92 ? 48  HIS J NE2 1 
ATOM   10344 N  N   . GLU J  1 49  ? 54.673  91.415  60.472  1.00 19.83 ? 49  GLU J N   1 
ATOM   10345 C  CA  . GLU J  1 49  ? 55.515  91.716  61.633  1.00 22.76 ? 49  GLU J CA  1 
ATOM   10346 C  C   . GLU J  1 49  ? 54.932  91.308  63.005  1.00 24.53 ? 49  GLU J C   1 
ATOM   10347 O  O   . GLU J  1 49  ? 55.637  90.746  63.850  1.00 23.90 ? 49  GLU J O   1 
ATOM   10348 C  CB  . GLU J  1 49  ? 55.910  93.196  61.656  1.00 21.35 ? 49  GLU J CB  1 
ATOM   10349 C  CG  . GLU J  1 49  ? 56.800  93.537  62.857  1.00 24.64 ? 49  GLU J CG  1 
ATOM   10350 C  CD  . GLU J  1 49  ? 57.159  95.009  62.938  1.00 29.74 ? 49  GLU J CD  1 
ATOM   10351 O  OE1 . GLU J  1 49  ? 56.556  95.799  62.177  1.00 21.16 ? 49  GLU J OE1 1 
ATOM   10352 O  OE2 . GLU J  1 49  ? 58.039  95.373  63.765  1.00 28.97 ? 49  GLU J OE2 1 
ATOM   10353 N  N   . PHE J  1 50  ? 53.656  91.579  63.240  1.00 24.07 ? 50  PHE J N   1 
ATOM   10354 C  CA  . PHE J  1 50  ? 53.114  91.303  64.573  1.00 24.83 ? 50  PHE J CA  1 
ATOM   10355 C  C   . PHE J  1 50  ? 52.251  90.048  64.643  1.00 27.28 ? 50  PHE J C   1 
ATOM   10356 O  O   . PHE J  1 50  ? 51.473  89.761  63.733  1.00 30.23 ? 50  PHE J O   1 
ATOM   10357 C  CB  . PHE J  1 50  ? 52.356  92.512  65.085  1.00 24.31 ? 50  PHE J CB  1 
ATOM   10358 C  CG  . PHE J  1 50  ? 53.152  93.780  65.026  1.00 23.03 ? 50  PHE J CG  1 
ATOM   10359 C  CD1 . PHE J  1 50  ? 54.320  93.910  65.759  1.00 24.61 ? 50  PHE J CD1 1 
ATOM   10360 C  CD2 . PHE J  1 50  ? 52.728  94.840  64.250  1.00 23.02 ? 50  PHE J CD2 1 
ATOM   10361 C  CE1 . PHE J  1 50  ? 55.058  95.070  65.700  1.00 26.05 ? 50  PHE J CE1 1 
ATOM   10362 C  CE2 . PHE J  1 50  ? 53.462  96.009  64.184  1.00 29.35 ? 50  PHE J CE2 1 
ATOM   10363 C  CZ  . PHE J  1 50  ? 54.633  96.124  64.903  1.00 26.94 ? 50  PHE J CZ  1 
ATOM   10364 N  N   . GLY J  1 51  ? 52.400  89.293  65.724  1.00 25.22 ? 51  GLY J N   1 
ATOM   10365 C  CA  . GLY J  1 51  ? 51.515  88.173  65.994  1.00 26.37 ? 51  GLY J CA  1 
ATOM   10366 C  C   . GLY J  1 51  ? 50.304  88.659  66.782  1.00 32.89 ? 51  GLY J C   1 
ATOM   10367 O  O   . GLY J  1 51  ? 49.870  88.039  67.759  1.00 33.35 ? 51  GLY J O   1 
ATOM   10368 N  N   . ASP J  1 52  ? 49.760  89.786  66.342  1.00 30.62 ? 52  ASP J N   1 
ATOM   10369 C  CA  . ASP J  1 52  ? 48.677  90.459  67.039  1.00 32.65 ? 52  ASP J CA  1 
ATOM   10370 C  C   . ASP J  1 52  ? 47.395  90.322  66.222  1.00 37.24 ? 52  ASP J C   1 
ATOM   10371 O  O   . ASP J  1 52  ? 47.290  90.868  65.125  1.00 34.86 ? 52  ASP J O   1 
ATOM   10372 C  CB  . ASP J  1 52  ? 49.040  91.935  67.218  1.00 31.37 ? 52  ASP J CB  1 
ATOM   10373 C  CG  . ASP J  1 52  ? 48.015  92.712  68.035  1.00 36.77 ? 52  ASP J CG  1 
ATOM   10374 O  OD1 . ASP J  1 52  ? 46.813  92.375  68.007  1.00 36.87 ? 52  ASP J OD1 1 
ATOM   10375 O  OD2 . ASP J  1 52  ? 48.422  93.682  68.704  1.00 36.24 ? 52  ASP J OD2 1 
ATOM   10376 N  N   . ASN J  1 53  ? 46.418  89.619  66.784  1.00 39.14 ? 53  ASN J N   1 
ATOM   10377 C  CA  . ASN J  1 53  ? 45.127  89.404  66.143  1.00 34.57 ? 53  ASN J CA  1 
ATOM   10378 C  C   . ASN J  1 53  ? 43.982  90.119  66.906  1.00 40.96 ? 53  ASN J C   1 
ATOM   10379 O  O   . ASN J  1 53  ? 42.811  89.766  66.772  1.00 38.09 ? 53  ASN J O   1 
ATOM   10380 C  CB  . ASN J  1 53  ? 44.881  87.892  66.058  1.00 37.85 ? 53  ASN J CB  1 
ATOM   10381 C  CG  . ASN J  1 53  ? 43.595  87.525  65.318  1.00 43.74 ? 53  ASN J CG  1 
ATOM   10382 O  OD1 . ASN J  1 53  ? 43.155  88.229  64.399  1.00 43.19 ? 53  ASN J OD1 1 
ATOM   10383 N  ND2 . ASN J  1 53  ? 42.985  86.411  65.725  1.00 40.50 ? 53  ASN J ND2 1 
ATOM   10384 N  N   . THR J  1 54  ? 44.314  91.127  67.712  1.00 38.40 ? 54  THR J N   1 
ATOM   10385 C  CA  . THR J  1 54  ? 43.273  91.858  68.443  1.00 40.38 ? 54  THR J CA  1 
ATOM   10386 C  C   . THR J  1 54  ? 42.255  92.483  67.493  1.00 42.78 ? 54  THR J C   1 
ATOM   10387 O  O   . THR J  1 54  ? 41.044  92.326  67.677  1.00 45.06 ? 54  THR J O   1 
ATOM   10388 C  CB  . THR J  1 54  ? 43.836  92.952  69.381  1.00 38.15 ? 54  THR J CB  1 
ATOM   10389 O  OG1 . THR J  1 54  ? 44.577  93.916  68.621  1.00 36.84 ? 54  THR J OG1 1 
ATOM   10390 C  CG2 . THR J  1 54  ? 44.715  92.338  70.469  1.00 35.55 ? 54  THR J CG2 1 
ATOM   10391 N  N   . ALA J  1 55  ? 42.750  93.181  66.475  1.00 40.78 ? 55  ALA J N   1 
ATOM   10392 C  CA  . ALA J  1 55  ? 41.882  93.769  65.462  1.00 38.61 ? 55  ALA J CA  1 
ATOM   10393 C  C   . ALA J  1 55  ? 41.898  92.928  64.197  1.00 42.08 ? 55  ALA J C   1 
ATOM   10394 O  O   . ALA J  1 55  ? 42.040  93.459  63.086  1.00 40.39 ? 55  ALA J O   1 
ATOM   10395 C  CB  . ALA J  1 55  ? 42.302  95.202  65.152  1.00 42.43 ? 55  ALA J CB  1 
ATOM   10396 N  N   . GLY J  1 56  ? 41.742  91.616  64.365  1.00 36.85 ? 56  GLY J N   1 
ATOM   10397 C  CA  . GLY J  1 56  ? 41.811  90.708  63.234  1.00 40.94 ? 56  GLY J CA  1 
ATOM   10398 C  C   . GLY J  1 56  ? 43.170  90.777  62.552  1.00 40.90 ? 56  GLY J C   1 
ATOM   10399 O  O   . GLY J  1 56  ? 44.176  91.106  63.189  1.00 35.61 ? 56  GLY J O   1 
ATOM   10400 N  N   . SER J  1 57  ? 43.196  90.485  61.251  1.00 42.10 ? 57  SER J N   1 
ATOM   10401 C  CA  . SER J  1 57  ? 44.442  90.492  60.481  1.00 35.62 ? 57  SER J CA  1 
ATOM   10402 C  C   . SER J  1 57  ? 45.015  91.904  60.359  1.00 34.94 ? 57  SER J C   1 
ATOM   10403 O  O   . SER J  1 57  ? 46.206  92.087  60.093  1.00 34.18 ? 57  SER J O   1 
ATOM   10404 C  CB  . SER J  1 57  ? 44.215  89.894  59.090  1.00 35.14 ? 57  SER J CB  1 
ATOM   10405 O  OG  . SER J  1 57  ? 43.084  90.482  58.465  1.00 36.76 ? 57  SER J OG  1 
ATOM   10406 N  N   . THR J  1 58  ? 44.171  92.906  60.559  1.00 30.53 ? 58  THR J N   1 
ATOM   10407 C  CA  . THR J  1 58  ? 44.618  94.269  60.362  1.00 32.71 ? 58  THR J CA  1 
ATOM   10408 C  C   . THR J  1 58  ? 45.662  94.695  61.419  1.00 36.83 ? 58  THR J C   1 
ATOM   10409 O  O   . THR J  1 58  ? 46.459  95.607  61.181  1.00 33.42 ? 58  THR J O   1 
ATOM   10410 C  CB  . THR J  1 58  ? 43.426  95.248  60.271  1.00 37.58 ? 58  THR J CB  1 
ATOM   10411 O  OG1 . THR J  1 58  ? 43.409  96.105  61.417  1.00 45.26 ? 58  THR J OG1 1 
ATOM   10412 C  CG2 . THR J  1 58  ? 42.085  94.481  60.157  1.00 37.64 ? 58  THR J CG2 1 
ATOM   10413 N  N   . SER J  1 59  ? 45.679  94.015  62.566  1.00 28.71 ? 59  SER J N   1 
ATOM   10414 C  CA  . SER J  1 59  ? 46.679  94.306  63.591  1.00 33.35 ? 59  SER J CA  1 
ATOM   10415 C  C   . SER J  1 59  ? 47.917  93.401  63.500  1.00 32.66 ? 59  SER J C   1 
ATOM   10416 O  O   . SER J  1 59  ? 48.682  93.287  64.463  1.00 34.54 ? 59  SER J O   1 
ATOM   10417 C  CB  . SER J  1 59  ? 46.073  94.268  65.010  1.00 35.01 ? 59  SER J CB  1 
ATOM   10418 O  OG  . SER J  1 59  ? 45.588  92.979  65.348  1.00 34.76 ? 59  SER J OG  1 
ATOM   10419 N  N   . ALA J  1 60  ? 48.119  92.769  62.345  1.00 30.58 ? 60  ALA J N   1 
ATOM   10420 C  CA  . ALA J  1 60  ? 49.363  92.037  62.090  1.00 25.19 ? 60  ALA J CA  1 
ATOM   10421 C  C   . ALA J  1 60  ? 50.508  92.980  61.691  1.00 19.48 ? 60  ALA J C   1 
ATOM   10422 O  O   . ALA J  1 60  ? 51.669  92.614  61.770  1.00 25.70 ? 60  ALA J O   1 
ATOM   10423 C  CB  . ALA J  1 60  ? 49.156  90.951  61.043  1.00 22.80 ? 60  ALA J CB  1 
ATOM   10424 N  N   . GLY J  1 61  ? 50.182  94.203  61.294  1.00 21.86 ? 61  GLY J N   1 
ATOM   10425 C  CA  . GLY J  1 61  ? 51.195  95.154  60.861  1.00 25.17 ? 61  GLY J CA  1 
ATOM   10426 C  C   . GLY J  1 61  ? 51.684  94.851  59.450  1.00 22.40 ? 61  GLY J C   1 
ATOM   10427 O  O   . GLY J  1 61  ? 51.060  94.057  58.740  1.00 20.36 ? 61  GLY J O   1 
ATOM   10428 N  N   . PRO J  1 62  ? 52.811  95.464  59.040  1.00 22.90 ? 62  PRO J N   1 
ATOM   10429 C  CA  . PRO J  1 62  ? 53.305  95.283  57.671  1.00 20.64 ? 62  PRO J CA  1 
ATOM   10430 C  C   . PRO J  1 62  ? 54.059  93.976  57.553  1.00 19.33 ? 62  PRO J C   1 
ATOM   10431 O  O   . PRO J  1 62  ? 54.132  93.229  58.538  1.00 16.63 ? 62  PRO J O   1 
ATOM   10432 C  CB  . PRO J  1 62  ? 54.285  96.444  57.493  1.00 17.02 ? 62  PRO J CB  1 
ATOM   10433 C  CG  . PRO J  1 62  ? 54.524  97.010  58.906  1.00 19.89 ? 62  PRO J CG  1 
ATOM   10434 C  CD  . PRO J  1 62  ? 53.813  96.134  59.878  1.00 22.02 ? 62  PRO J CD  1 
ATOM   10435 N  N   . HIS J  1 63  ? 54.593  93.706  56.362  1.00 16.94 ? 63  HIS J N   1 
ATOM   10436 C  CA  . HIS J  1 63  ? 55.490  92.574  56.135  1.00 14.29 ? 63  HIS J CA  1 
ATOM   10437 C  C   . HIS J  1 63  ? 56.633  92.631  57.132  1.00 14.89 ? 63  HIS J C   1 
ATOM   10438 O  O   . HIS J  1 63  ? 57.133  93.713  57.416  1.00 16.32 ? 63  HIS J O   1 
ATOM   10439 C  CB  . HIS J  1 63  ? 56.048  92.626  54.699  1.00 12.72 ? 63  HIS J CB  1 
ATOM   10440 C  CG  . HIS J  1 63  ? 54.993  92.473  53.653  1.00 15.05 ? 63  HIS J CG  1 
ATOM   10441 N  ND1 . HIS J  1 63  ? 55.272  92.449  52.307  1.00 15.36 ? 63  HIS J ND1 1 
ATOM   10442 C  CD2 . HIS J  1 63  ? 53.649  92.313  53.766  1.00 15.03 ? 63  HIS J CD2 1 
ATOM   10443 C  CE1 . HIS J  1 63  ? 54.147  92.291  51.630  1.00 15.71 ? 63  HIS J CE1 1 
ATOM   10444 N  NE2 . HIS J  1 63  ? 53.149  92.204  52.494  1.00 17.19 ? 63  HIS J NE2 1 
ATOM   10445 N  N   . PHE J  1 64  ? 57.042  91.470  57.646  1.00 13.04 ? 64  PHE J N   1 
ATOM   10446 C  CA  . PHE J  1 64  ? 58.172  91.378  58.553  1.00 15.48 ? 64  PHE J CA  1 
ATOM   10447 C  C   . PHE J  1 64  ? 59.447  91.811  57.836  1.00 20.66 ? 64  PHE J C   1 
ATOM   10448 O  O   . PHE J  1 64  ? 59.943  91.127  56.921  1.00 20.38 ? 64  PHE J O   1 
ATOM   10449 C  CB  . PHE J  1 64  ? 58.326  89.949  59.085  1.00 15.28 ? 64  PHE J CB  1 
ATOM   10450 C  CG  . PHE J  1 64  ? 59.463  89.774  60.056  1.00 19.24 ? 64  PHE J CG  1 
ATOM   10451 C  CD1 . PHE J  1 64  ? 59.732  90.745  61.022  1.00 19.40 ? 64  PHE J CD1 1 
ATOM   10452 C  CD2 . PHE J  1 64  ? 60.252  88.631  60.021  1.00 16.20 ? 64  PHE J CD2 1 
ATOM   10453 C  CE1 . PHE J  1 64  ? 60.783  90.585  61.923  1.00 21.05 ? 64  PHE J CE1 1 
ATOM   10454 C  CE2 . PHE J  1 64  ? 61.294  88.461  60.932  1.00 23.83 ? 64  PHE J CE2 1 
ATOM   10455 C  CZ  . PHE J  1 64  ? 61.559  89.441  61.888  1.00 18.87 ? 64  PHE J CZ  1 
ATOM   10456 N  N   . ASN J  1 65  ? 59.991  92.935  58.289  1.00 22.07 ? 65  ASN J N   1 
ATOM   10457 C  CA  . ASN J  1 65  ? 61.046  93.621  57.571  1.00 19.62 ? 65  ASN J CA  1 
ATOM   10458 C  C   . ASN J  1 65  ? 62.136  94.150  58.509  1.00 18.99 ? 65  ASN J C   1 
ATOM   10459 O  O   . ASN J  1 65  ? 62.321  95.364  58.619  1.00 19.02 ? 65  ASN J O   1 
ATOM   10460 C  CB  . ASN J  1 65  ? 60.414  94.781  56.806  1.00 17.17 ? 65  ASN J CB  1 
ATOM   10461 C  CG  . ASN J  1 65  ? 61.361  95.414  55.844  1.00 18.57 ? 65  ASN J CG  1 
ATOM   10462 O  OD1 . ASN J  1 65  ? 62.393  94.832  55.497  1.00 18.93 ? 65  ASN J OD1 1 
ATOM   10463 N  ND2 . ASN J  1 65  ? 61.022  96.612  55.390  1.00 17.33 ? 65  ASN J ND2 1 
ATOM   10464 N  N   . PRO J  1 66  ? 62.873  93.244  59.176  1.00 18.07 ? 66  PRO J N   1 
ATOM   10465 C  CA  . PRO J  1 66  ? 63.811  93.733  60.192  1.00 22.53 ? 66  PRO J CA  1 
ATOM   10466 C  C   . PRO J  1 66  ? 65.079  94.355  59.602  1.00 28.92 ? 66  PRO J C   1 
ATOM   10467 O  O   . PRO J  1 66  ? 65.837  94.982  60.344  1.00 30.49 ? 66  PRO J O   1 
ATOM   10468 C  CB  . PRO J  1 66  ? 64.137  92.473  61.008  1.00 18.20 ? 66  PRO J CB  1 
ATOM   10469 C  CG  . PRO J  1 66  ? 63.968  91.354  60.050  1.00 20.09 ? 66  PRO J CG  1 
ATOM   10470 C  CD  . PRO J  1 66  ? 62.852  91.771  59.109  1.00 19.97 ? 66  PRO J CD  1 
ATOM   10471 N  N   . LEU J  1 67  ? 65.303  94.203  58.297  1.00 24.91 ? 67  LEU J N   1 
ATOM   10472 C  CA  . LEU J  1 67  ? 66.484  94.783  57.677  1.00 23.39 ? 67  LEU J CA  1 
ATOM   10473 C  C   . LEU J  1 67  ? 66.103  96.031  56.912  1.00 28.17 ? 67  LEU J C   1 
ATOM   10474 O  O   . LEU J  1 67  ? 66.894  96.544  56.123  1.00 30.33 ? 67  LEU J O   1 
ATOM   10475 C  CB  . LEU J  1 67  ? 67.157  93.787  56.737  1.00 28.22 ? 67  LEU J CB  1 
ATOM   10476 C  CG  . LEU J  1 67  ? 67.292  92.361  57.251  1.00 27.42 ? 67  LEU J CG  1 
ATOM   10477 C  CD1 . LEU J  1 67  ? 67.963  91.527  56.194  1.00 30.53 ? 67  LEU J CD1 1 
ATOM   10478 C  CD2 . LEU J  1 67  ? 68.086  92.329  58.547  1.00 28.23 ? 67  LEU J CD2 1 
ATOM   10479 N  N   . SER J  1 68  ? 64.876  96.496  57.131  1.00 28.11 ? 68  SER J N   1 
ATOM   10480 C  CA  . SER J  1 68  ? 64.398  97.748  56.543  1.00 32.38 ? 68  SER J CA  1 
ATOM   10481 C  C   . SER J  1 68  ? 64.673  97.833  55.051  1.00 27.87 ? 68  SER J C   1 
ATOM   10482 O  O   . SER J  1 68  ? 65.271  98.790  54.585  1.00 29.80 ? 68  SER J O   1 
ATOM   10483 C  CB  . SER J  1 68  ? 65.051  98.951  57.240  1.00 31.22 ? 68  SER J CB  1 
ATOM   10484 O  OG  . SER J  1 68  ? 65.059  98.781  58.646  1.00 31.94 ? 68  SER J OG  1 
ATOM   10485 N  N   . ARG J  1 69  ? 64.259  96.816  54.306  1.00 30.15 ? 69  ARG J N   1 
ATOM   10486 C  CA  . ARG J  1 69  ? 64.434  96.817  52.858  1.00 24.50 ? 69  ARG J CA  1 
ATOM   10487 C  C   . ARG J  1 69  ? 63.078  96.988  52.196  1.00 24.46 ? 69  ARG J C   1 
ATOM   10488 O  O   . ARG J  1 69  ? 62.043  96.927  52.863  1.00 23.63 ? 69  ARG J O   1 
ATOM   10489 C  CB  . ARG J  1 69  ? 65.096  95.517  52.391  1.00 28.30 ? 69  ARG J CB  1 
ATOM   10490 C  CG  . ARG J  1 69  ? 66.102  94.960  53.381  1.00 26.20 ? 69  ARG J CG  1 
ATOM   10491 C  CD  . ARG J  1 69  ? 67.546  95.176  52.941  1.00 31.47 ? 69  ARG J CD  1 
ATOM   10492 N  NE  . ARG J  1 69  ? 67.979  94.139  52.005  1.00 41.81 ? 69  ARG J NE  1 
ATOM   10493 C  CZ  . ARG J  1 69  ? 68.758  93.099  52.308  1.00 37.92 ? 69  ARG J CZ  1 
ATOM   10494 N  NH1 . ARG J  1 69  ? 69.238  92.937  53.533  1.00 36.72 ? 69  ARG J NH1 1 
ATOM   10495 N  NH2 . ARG J  1 69  ? 69.071  92.219  51.367  1.00 36.26 ? 69  ARG J NH2 1 
ATOM   10496 N  N   . LYS J  1 70  ? 63.085  97.227  50.892  1.00 19.06 ? 70  LYS J N   1 
ATOM   10497 C  CA  . LYS J  1 70  ? 61.853  97.303  50.127  1.00 20.78 ? 70  LYS J CA  1 
ATOM   10498 C  C   . LYS J  1 70  ? 61.334  95.898  49.792  1.00 19.93 ? 70  LYS J C   1 
ATOM   10499 O  O   . LYS J  1 70  ? 62.087  94.917  49.837  1.00 17.37 ? 70  LYS J O   1 
ATOM   10500 C  CB  . LYS J  1 70  ? 62.074  98.104  48.839  1.00 20.77 ? 70  LYS J CB  1 
ATOM   10501 C  CG  . LYS J  1 70  ? 62.453  99.566  49.065  1.00 29.14 ? 70  LYS J CG  1 
ATOM   10502 C  CD  . LYS J  1 70  ? 62.603  100.314 47.738  1.00 37.00 ? 70  LYS J CD  1 
ATOM   10503 C  CE  . LYS J  1 70  ? 63.165  101.718 47.942  1.00 45.24 ? 70  LYS J CE  1 
ATOM   10504 N  NZ  . LYS J  1 70  ? 64.595  101.695 48.375  1.00 44.94 ? 70  LYS J NZ  1 
ATOM   10505 N  N   . HIS J  1 71  ? 60.045  95.820  49.461  1.00 17.28 ? 71  HIS J N   1 
ATOM   10506 C  CA  . HIS J  1 71  ? 59.373  94.564  49.095  1.00 16.73 ? 71  HIS J CA  1 
ATOM   10507 C  C   . HIS J  1 71  ? 59.905  93.961  47.796  1.00 14.18 ? 71  HIS J C   1 
ATOM   10508 O  O   . HIS J  1 71  ? 60.132  94.682  46.829  1.00 14.31 ? 71  HIS J O   1 
ATOM   10509 C  CB  . HIS J  1 71  ? 57.865  94.811  48.926  1.00 11.44 ? 71  HIS J CB  1 
ATOM   10510 C  CG  . HIS J  1 71  ? 57.098  93.586  48.556  1.00 12.06 ? 71  HIS J CG  1 
ATOM   10511 N  ND1 . HIS J  1 71  ? 56.705  92.647  49.480  1.00 9.43  ? 71  HIS J ND1 1 
ATOM   10512 C  CD2 . HIS J  1 71  ? 56.672  93.132  47.355  1.00 13.35 ? 71  HIS J CD2 1 
ATOM   10513 C  CE1 . HIS J  1 71  ? 56.057  91.675  48.870  1.00 11.89 ? 71  HIS J CE1 1 
ATOM   10514 N  NE2 . HIS J  1 71  ? 56.021  91.946  47.579  1.00 11.81 ? 71  HIS J NE2 1 
ATOM   10515 N  N   . GLY J  1 72  ? 60.069  92.638  47.778  1.00 12.72 ? 72  GLY J N   1 
ATOM   10516 C  CA  . GLY J  1 72  ? 60.458  91.916  46.583  1.00 11.48 ? 72  GLY J CA  1 
ATOM   10517 C  C   . GLY J  1 72  ? 59.849  90.521  46.524  1.00 16.09 ? 72  GLY J C   1 
ATOM   10518 O  O   . GLY J  1 72  ? 58.965  90.189  47.322  1.00 12.54 ? 72  GLY J O   1 
ATOM   10519 N  N   . GLY J  1 73  ? 60.300  89.711  45.565  1.00 10.64 ? 73  GLY J N   1 
ATOM   10520 C  CA  . GLY J  1 73  ? 59.965  88.302  45.530  1.00 12.39 ? 73  GLY J CA  1 
ATOM   10521 C  C   . GLY J  1 73  ? 60.991  87.515  46.341  1.00 14.37 ? 73  GLY J C   1 
ATOM   10522 O  O   . GLY J  1 73  ? 62.025  88.057  46.705  1.00 14.14 ? 73  GLY J O   1 
ATOM   10523 N  N   . PRO J  1 74  ? 60.710  86.234  46.638  1.00 15.41 ? 74  PRO J N   1 
ATOM   10524 C  CA  . PRO J  1 74  ? 61.607  85.482  47.535  1.00 15.56 ? 74  PRO J CA  1 
ATOM   10525 C  C   . PRO J  1 74  ? 63.027  85.328  46.998  1.00 18.42 ? 74  PRO J C   1 
ATOM   10526 O  O   . PRO J  1 74  ? 63.969  85.126  47.774  1.00 14.17 ? 74  PRO J O   1 
ATOM   10527 C  CB  . PRO J  1 74  ? 60.933  84.102  47.636  1.00 11.94 ? 74  PRO J CB  1 
ATOM   10528 C  CG  . PRO J  1 74  ? 59.873  84.070  46.544  1.00 10.75 ? 74  PRO J CG  1 
ATOM   10529 C  CD  . PRO J  1 74  ? 59.463  85.495  46.368  1.00 11.98 ? 74  PRO J CD  1 
ATOM   10530 N  N   . LYS J  1 75  ? 63.162  85.423  45.680  1.00 13.46 ? 75  LYS J N   1 
ATOM   10531 C  CA  . LYS J  1 75  ? 64.427  85.192  45.018  1.00 19.58 ? 75  LYS J CA  1 
ATOM   10532 C  C   . LYS J  1 75  ? 65.258  86.449  45.005  1.00 16.87 ? 75  LYS J C   1 
ATOM   10533 O  O   . LYS J  1 75  ? 66.441  86.398  44.755  1.00 20.59 ? 75  LYS J O   1 
ATOM   10534 C  CB  . LYS J  1 75  ? 64.192  84.705  43.582  1.00 20.00 ? 75  LYS J CB  1 
ATOM   10535 C  CG  . LYS J  1 75  ? 63.241  83.516  43.527  1.00 26.77 ? 75  LYS J CG  1 
ATOM   10536 C  CD  . LYS J  1 75  ? 63.370  82.756  42.243  1.00 34.26 ? 75  LYS J CD  1 
ATOM   10537 C  CE  . LYS J  1 75  ? 63.287  83.702  41.065  1.00 36.41 ? 75  LYS J CE  1 
ATOM   10538 N  NZ  . LYS J  1 75  ? 63.907  83.103  39.863  1.00 31.81 ? 75  LYS J NZ  1 
ATOM   10539 N  N   . ASP J  1 76  ? 64.635  87.582  45.268  1.00 16.84 ? 76  ASP J N   1 
ATOM   10540 C  CA  . ASP J  1 76  ? 65.354  88.842  45.215  1.00 20.33 ? 76  ASP J CA  1 
ATOM   10541 C  C   . ASP J  1 76  ? 66.215  89.060  46.459  1.00 22.43 ? 76  ASP J C   1 
ATOM   10542 O  O   . ASP J  1 76  ? 65.831  88.698  47.576  1.00 17.32 ? 76  ASP J O   1 
ATOM   10543 C  CB  . ASP J  1 76  ? 64.370  90.004  45.057  1.00 16.51 ? 76  ASP J CB  1 
ATOM   10544 C  CG  . ASP J  1 76  ? 63.641  89.980  43.725  1.00 17.85 ? 76  ASP J CG  1 
ATOM   10545 O  OD1 . ASP J  1 76  ? 64.301  89.837  42.681  1.00 23.93 ? 76  ASP J OD1 1 
ATOM   10546 O  OD2 . ASP J  1 76  ? 62.395  90.097  43.713  1.00 20.94 ? 76  ASP J OD2 1 
ATOM   10547 N  N   . GLU J  1 77  ? 67.376  89.672  46.268  1.00 21.49 ? 77  GLU J N   1 
ATOM   10548 C  CA  . GLU J  1 77  ? 68.174  90.089  47.402  1.00 21.78 ? 77  GLU J CA  1 
ATOM   10549 C  C   . GLU J  1 77  ? 67.485  91.246  48.117  1.00 24.02 ? 77  GLU J C   1 
ATOM   10550 O  O   . GLU J  1 77  ? 67.530  91.350  49.341  1.00 23.73 ? 77  GLU J O   1 
ATOM   10551 C  CB  . GLU J  1 77  ? 69.580  90.506  46.967  1.00 27.64 ? 77  GLU J CB  1 
ATOM   10552 C  CG  . GLU J  1 77  ? 70.512  90.771  48.152  1.00 36.40 ? 77  GLU J CG  1 
ATOM   10553 C  CD  . GLU J  1 77  ? 71.943  91.091  47.736  1.00 50.74 ? 77  GLU J CD  1 
ATOM   10554 O  OE1 . GLU J  1 77  ? 72.147  91.698  46.658  1.00 52.38 ? 77  GLU J OE1 1 
ATOM   10555 O  OE2 . GLU J  1 77  ? 72.871  90.725  48.491  1.00 59.69 ? 77  GLU J OE2 1 
ATOM   10556 N  N   . GLU J  1 78  ? 66.864  92.134  47.352  1.00 18.96 ? 78  GLU J N   1 
ATOM   10557 C  CA  . GLU J  1 78  ? 66.089  93.198  47.955  1.00 18.12 ? 78  GLU J CA  1 
ATOM   10558 C  C   . GLU J  1 78  ? 64.670  92.676  48.215  1.00 19.33 ? 78  GLU J C   1 
ATOM   10559 O  O   . GLU J  1 78  ? 63.845  92.593  47.303  1.00 17.95 ? 78  GLU J O   1 
ATOM   10560 C  CB  . GLU J  1 78  ? 66.063  94.434  47.053  1.00 22.90 ? 78  GLU J CB  1 
ATOM   10561 C  CG  . GLU J  1 78  ? 65.354  95.650  47.647  1.00 18.54 ? 78  GLU J CG  1 
ATOM   10562 C  CD  . GLU J  1 78  ? 66.153  96.288  48.776  1.00 27.64 ? 78  GLU J CD  1 
ATOM   10563 O  OE1 . GLU J  1 78  ? 67.259  95.782  49.060  1.00 31.14 ? 78  GLU J OE1 1 
ATOM   10564 O  OE2 . GLU J  1 78  ? 65.682  97.286  49.378  1.00 27.50 ? 78  GLU J OE2 1 
ATOM   10565 N  N   . ARG J  1 79  ? 64.399  92.311  49.462  1.00 17.74 ? 79  ARG J N   1 
ATOM   10566 C  CA  . ARG J  1 79  ? 63.088  91.813  49.824  1.00 17.56 ? 79  ARG J CA  1 
ATOM   10567 C  C   . ARG J  1 79  ? 62.887  92.007  51.324  1.00 17.48 ? 79  ARG J C   1 
ATOM   10568 O  O   . ARG J  1 79  ? 63.847  92.242  52.054  1.00 16.24 ? 79  ARG J O   1 
ATOM   10569 C  CB  . ARG J  1 79  ? 62.998  90.328  49.492  1.00 11.88 ? 79  ARG J CB  1 
ATOM   10570 C  CG  . ARG J  1 79  ? 64.027  89.495  50.246  1.00 12.15 ? 79  ARG J CG  1 
ATOM   10571 C  CD  . ARG J  1 79  ? 63.787  88.030  50.064  1.00 15.74 ? 79  ARG J CD  1 
ATOM   10572 N  NE  . ARG J  1 79  ? 62.934  87.469  51.110  1.00 13.33 ? 79  ARG J NE  1 
ATOM   10573 C  CZ  . ARG J  1 79  ? 62.771  86.163  51.301  1.00 14.06 ? 79  ARG J CZ  1 
ATOM   10574 N  NH1 . ARG J  1 79  ? 63.406  85.300  50.516  1.00 8.41  ? 79  ARG J NH1 1 
ATOM   10575 N  NH2 . ARG J  1 79  ? 61.985  85.718  52.286  1.00 14.47 ? 79  ARG J NH2 1 
ATOM   10576 N  N   . HIS J  1 80  ? 61.642  91.893  51.778  1.00 13.67 ? 80  HIS J N   1 
ATOM   10577 C  CA  . HIS J  1 80  ? 61.360  91.812  53.199  1.00 13.25 ? 80  HIS J CA  1 
ATOM   10578 C  C   . HIS J  1 80  ? 61.695  90.384  53.587  1.00 14.33 ? 80  HIS J C   1 
ATOM   10579 O  O   . HIS J  1 80  ? 61.655  89.500  52.732  1.00 13.45 ? 80  HIS J O   1 
ATOM   10580 C  CB  . HIS J  1 80  ? 59.876  92.098  53.464  1.00 15.00 ? 80  HIS J CB  1 
ATOM   10581 C  CG  . HIS J  1 80  ? 59.433  93.463  53.040  1.00 13.47 ? 80  HIS J CG  1 
ATOM   10582 N  ND1 . HIS J  1 80  ? 58.246  93.691  52.371  1.00 14.37 ? 80  HIS J ND1 1 
ATOM   10583 C  CD2 . HIS J  1 80  ? 60.019  94.672  53.187  1.00 11.22 ? 80  HIS J CD2 1 
ATOM   10584 C  CE1 . HIS J  1 80  ? 58.108  94.987  52.154  1.00 13.87 ? 80  HIS J CE1 1 
ATOM   10585 N  NE2 . HIS J  1 80  ? 59.179  95.603  52.633  1.00 12.57 ? 80  HIS J NE2 1 
ATOM   10586 N  N   . VAL J  1 81  ? 62.049  90.150  54.852  1.00 12.21 ? 81  VAL J N   1 
ATOM   10587 C  CA  . VAL J  1 81  ? 62.285  88.788  55.329  1.00 12.21 ? 81  VAL J CA  1 
ATOM   10588 C  C   . VAL J  1 81  ? 61.014  87.956  55.185  1.00 14.77 ? 81  VAL J C   1 
ATOM   10589 O  O   . VAL J  1 81  ? 61.066  86.758  54.892  1.00 14.71 ? 81  VAL J O   1 
ATOM   10590 C  CB  . VAL J  1 81  ? 62.768  88.762  56.799  1.00 20.54 ? 81  VAL J CB  1 
ATOM   10591 C  CG1 . VAL J  1 81  ? 62.673  87.347  57.388  1.00 16.57 ? 81  VAL J CG1 1 
ATOM   10592 C  CG2 . VAL J  1 81  ? 64.201  89.308  56.896  1.00 19.72 ? 81  VAL J CG2 1 
ATOM   10593 N  N   . GLY J  1 82  ? 59.868  88.605  55.359  1.00 13.67 ? 82  GLY J N   1 
ATOM   10594 C  CA  . GLY J  1 82  ? 58.596  87.917  55.252  1.00 13.11 ? 82  GLY J CA  1 
ATOM   10595 C  C   . GLY J  1 82  ? 58.048  87.711  53.848  1.00 15.56 ? 82  GLY J C   1 
ATOM   10596 O  O   . GLY J  1 82  ? 56.925  87.209  53.692  1.00 14.02 ? 82  GLY J O   1 
ATOM   10597 N  N   . ASP J  1 83  ? 58.826  88.072  52.826  1.00 12.09 ? 83  ASP J N   1 
ATOM   10598 C  CA  . ASP J  1 83  ? 58.331  87.999  51.445  1.00 14.82 ? 83  ASP J CA  1 
ATOM   10599 C  C   . ASP J  1 83  ? 58.448  86.598  50.860  1.00 11.25 ? 83  ASP J C   1 
ATOM   10600 O  O   . ASP J  1 83  ? 59.487  86.242  50.311  1.00 9.64  ? 83  ASP J O   1 
ATOM   10601 C  CB  . ASP J  1 83  ? 59.064  89.011  50.536  1.00 10.06 ? 83  ASP J CB  1 
ATOM   10602 C  CG  . ASP J  1 83  ? 58.722  90.453  50.870  1.00 13.07 ? 83  ASP J CG  1 
ATOM   10603 O  OD1 . ASP J  1 83  ? 57.712  90.705  51.605  1.00 7.41  ? 83  ASP J OD1 1 
ATOM   10604 O  OD2 . ASP J  1 83  ? 59.474  91.341  50.400  1.00 10.73 ? 83  ASP J OD2 1 
ATOM   10605 N  N   . LEU J  1 84  ? 57.378  85.817  50.942  1.00 9.19  ? 84  LEU J N   1 
ATOM   10606 C  CA  . LEU J  1 84  ? 57.424  84.447  50.440  1.00 12.87 ? 84  LEU J CA  1 
ATOM   10607 C  C   . LEU J  1 84  ? 56.795  84.286  49.052  1.00 11.85 ? 84  LEU J C   1 
ATOM   10608 O  O   . LEU J  1 84  ? 56.589  83.166  48.575  1.00 12.36 ? 84  LEU J O   1 
ATOM   10609 C  CB  . LEU J  1 84  ? 56.812  83.457  51.439  1.00 12.00 ? 84  LEU J CB  1 
ATOM   10610 C  CG  . LEU J  1 84  ? 57.530  83.349  52.786  1.00 14.74 ? 84  LEU J CG  1 
ATOM   10611 C  CD1 . LEU J  1 84  ? 56.698  82.534  53.782  1.00 11.85 ? 84  LEU J CD1 1 
ATOM   10612 C  CD2 . LEU J  1 84  ? 58.915  82.732  52.589  1.00 18.04 ? 84  LEU J CD2 1 
ATOM   10613 N  N   . GLY J  1 85  ? 56.533  85.403  48.385  1.00 12.30 ? 85  GLY J N   1 
ATOM   10614 C  CA  . GLY J  1 85  ? 56.023  85.352  47.026  1.00 11.73 ? 85  GLY J CA  1 
ATOM   10615 C  C   . GLY J  1 85  ? 54.572  84.933  46.933  1.00 12.38 ? 85  GLY J C   1 
ATOM   10616 O  O   . GLY J  1 85  ? 53.711  85.487  47.619  1.00 13.52 ? 85  GLY J O   1 
ATOM   10617 N  N   . ASN J  1 86  ? 54.306  83.935  46.096  1.00 12.07 ? 86  ASN J N   1 
ATOM   10618 C  CA  . ASN J  1 86  ? 52.941  83.520  45.816  1.00 15.13 ? 86  ASN J CA  1 
ATOM   10619 C  C   . ASN J  1 86  ? 52.684  82.056  46.068  1.00 15.60 ? 86  ASN J C   1 
ATOM   10620 O  O   . ASN J  1 86  ? 53.581  81.223  45.926  1.00 15.10 ? 86  ASN J O   1 
ATOM   10621 C  CB  . ASN J  1 86  ? 52.575  83.799  44.346  1.00 13.83 ? 86  ASN J CB  1 
ATOM   10622 C  CG  . ASN J  1 86  ? 52.276  85.263  44.091  1.00 16.70 ? 86  ASN J CG  1 
ATOM   10623 O  OD1 . ASN J  1 86  ? 51.312  85.814  44.635  1.00 14.08 ? 86  ASN J OD1 1 
ATOM   10624 N  ND2 . ASN J  1 86  ? 53.108  85.910  43.275  1.00 12.46 ? 86  ASN J ND2 1 
ATOM   10625 N  N   . VAL J  1 87  ? 51.440  81.753  46.426  1.00 13.25 ? 87  VAL J N   1 
ATOM   10626 C  CA  . VAL J  1 87  ? 50.921  80.392  46.312  1.00 15.92 ? 87  VAL J CA  1 
ATOM   10627 C  C   . VAL J  1 87  ? 49.849  80.341  45.205  1.00 15.93 ? 87  VAL J C   1 
ATOM   10628 O  O   . VAL J  1 87  ? 49.216  81.353  44.889  1.00 15.97 ? 87  VAL J O   1 
ATOM   10629 C  CB  . VAL J  1 87  ? 50.349  79.897  47.648  1.00 13.92 ? 87  VAL J CB  1 
ATOM   10630 C  CG1 . VAL J  1 87  ? 51.404  80.016  48.727  1.00 14.83 ? 87  VAL J CG1 1 
ATOM   10631 C  CG2 . VAL J  1 87  ? 49.125  80.708  48.026  1.00 14.10 ? 87  VAL J CG2 1 
ATOM   10632 N  N   . THR J  1 88  ? 49.653  79.166  44.622  1.00 18.78 ? 88  THR J N   1 
ATOM   10633 C  CA  . THR J  1 88  ? 48.737  79.003  43.496  1.00 17.80 ? 88  THR J CA  1 
ATOM   10634 C  C   . THR J  1 88  ? 47.537  78.130  43.858  1.00 22.54 ? 88  THR J C   1 
ATOM   10635 O  O   . THR J  1 88  ? 47.702  76.970  44.224  1.00 22.19 ? 88  THR J O   1 
ATOM   10636 C  CB  . THR J  1 88  ? 49.456  78.342  42.315  1.00 20.84 ? 88  THR J CB  1 
ATOM   10637 O  OG1 . THR J  1 88  ? 50.487  79.211  41.826  1.00 20.91 ? 88  THR J OG1 1 
ATOM   10638 C  CG2 . THR J  1 88  ? 48.471  78.021  41.188  1.00 19.12 ? 88  THR J CG2 1 
ATOM   10639 N  N   . ALA J  1 89  ? 46.333  78.683  43.754  1.00 21.25 ? 89  ALA J N   1 
ATOM   10640 C  CA  . ALA J  1 89  ? 45.117  77.892  43.950  1.00 21.68 ? 89  ALA J CA  1 
ATOM   10641 C  C   . ALA J  1 89  ? 44.619  77.324  42.633  1.00 25.28 ? 89  ALA J C   1 
ATOM   10642 O  O   . ALA J  1 89  ? 44.544  78.052  41.623  1.00 21.22 ? 89  ALA J O   1 
ATOM   10643 C  CB  . ALA J  1 89  ? 44.035  78.726  44.578  1.00 21.50 ? 89  ALA J CB  1 
ATOM   10644 N  N   . ASP J  1 90  ? 44.256  76.037  42.658  1.00 25.64 ? 90  ASP J N   1 
ATOM   10645 C  CA  . ASP J  1 90  ? 43.740  75.354  41.473  1.00 23.83 ? 90  ASP J CA  1 
ATOM   10646 C  C   . ASP J  1 90  ? 42.253  75.598  41.195  1.00 26.72 ? 90  ASP J C   1 
ATOM   10647 O  O   . ASP J  1 90  ? 41.608  76.427  41.839  1.00 26.51 ? 90  ASP J O   1 
ATOM   10648 C  CB  . ASP J  1 90  ? 44.040  73.850  41.514  1.00 24.93 ? 90  ASP J CB  1 
ATOM   10649 C  CG  . ASP J  1 90  ? 43.405  73.139  42.708  1.00 28.50 ? 90  ASP J CG  1 
ATOM   10650 O  OD1 . ASP J  1 90  ? 42.313  73.550  43.182  1.00 28.77 ? 90  ASP J OD1 1 
ATOM   10651 O  OD2 . ASP J  1 90  ? 44.012  72.144  43.172  1.00 29.75 ? 90  ASP J OD2 1 
ATOM   10652 N  N   . LYS J  1 91  ? 41.743  74.866  40.206  1.00 31.06 ? 91  LYS J N   1 
ATOM   10653 C  CA  . LYS J  1 91  ? 40.341  74.880  39.811  1.00 32.70 ? 91  LYS J CA  1 
ATOM   10654 C  C   . LYS J  1 91  ? 39.411  74.833  41.028  1.00 28.43 ? 91  LYS J C   1 
ATOM   10655 O  O   . LYS J  1 91  ? 38.409  75.537  41.091  1.00 30.67 ? 91  LYS J O   1 
ATOM   10656 C  CB  . LYS J  1 91  ? 40.092  73.656  38.924  1.00 38.76 ? 91  LYS J CB  1 
ATOM   10657 C  CG  . LYS J  1 91  ? 38.880  73.741  38.009  1.00 49.39 ? 91  LYS J CG  1 
ATOM   10658 C  CD  . LYS J  1 91  ? 39.246  74.254  36.612  1.00 51.79 ? 91  LYS J CD  1 
ATOM   10659 C  CE  . LYS J  1 91  ? 37.990  74.459  35.763  1.00 45.68 ? 91  LYS J CE  1 
ATOM   10660 N  NZ  . LYS J  1 91  ? 38.278  74.910  34.370  1.00 41.16 ? 91  LYS J NZ  1 
ATOM   10661 N  N   . ASP J  1 92  ? 39.782  74.023  42.015  1.00 29.03 ? 92  ASP J N   1 
ATOM   10662 C  CA  . ASP J  1 92  ? 38.910  73.728  43.146  1.00 29.76 ? 92  ASP J CA  1 
ATOM   10663 C  C   . ASP J  1 92  ? 39.122  74.625  44.346  1.00 30.49 ? 92  ASP J C   1 
ATOM   10664 O  O   . ASP J  1 92  ? 38.546  74.398  45.419  1.00 27.78 ? 92  ASP J O   1 
ATOM   10665 C  CB  . ASP J  1 92  ? 39.051  72.258  43.528  1.00 29.65 ? 92  ASP J CB  1 
ATOM   10666 C  CG  . ASP J  1 92  ? 38.601  71.341  42.406  1.00 37.47 ? 92  ASP J CG  1 
ATOM   10667 O  OD1 . ASP J  1 92  ? 37.375  71.316  42.097  1.00 35.85 ? 92  ASP J OD1 1 
ATOM   10668 O  OD2 . ASP J  1 92  ? 39.475  70.662  41.825  1.00 36.82 ? 92  ASP J OD2 1 
ATOM   10669 N  N   . GLY J  1 93  ? 39.933  75.659  44.157  1.00 23.63 ? 93  GLY J N   1 
ATOM   10670 C  CA  . GLY J  1 93  ? 40.121  76.631  45.203  1.00 23.19 ? 93  GLY J CA  1 
ATOM   10671 C  C   . GLY J  1 93  ? 41.129  76.183  46.232  1.00 21.77 ? 93  GLY J C   1 
ATOM   10672 O  O   . GLY J  1 93  ? 41.204  76.753  47.323  1.00 23.82 ? 93  GLY J O   1 
ATOM   10673 N  N   . VAL J  1 94  ? 41.917  75.172  45.879  1.00 23.60 ? 94  VAL J N   1 
ATOM   10674 C  CA  . VAL J  1 94  ? 42.905  74.635  46.802  1.00 22.71 ? 94  VAL J CA  1 
ATOM   10675 C  C   . VAL J  1 94  ? 44.339  74.929  46.384  1.00 24.63 ? 94  VAL J C   1 
ATOM   10676 O  O   . VAL J  1 94  ? 44.756  74.601  45.271  1.00 23.44 ? 94  VAL J O   1 
ATOM   10677 C  CB  . VAL J  1 94  ? 42.751  73.129  46.952  1.00 25.14 ? 94  VAL J CB  1 
ATOM   10678 C  CG1 . VAL J  1 94  ? 43.547  72.658  48.143  1.00 23.33 ? 94  VAL J CG1 1 
ATOM   10679 C  CG2 . VAL J  1 94  ? 41.263  72.759  47.094  1.00 26.06 ? 94  VAL J CG2 1 
ATOM   10680 N  N   . ALA J  1 95  ? 45.099  75.549  47.281  1.00 21.53 ? 95  ALA J N   1 
ATOM   10681 C  CA  . ALA J  1 95  ? 46.511  75.769  47.023  1.00 19.79 ? 95  ALA J CA  1 
ATOM   10682 C  C   . ALA J  1 95  ? 47.313  74.770  47.830  1.00 27.97 ? 95  ALA J C   1 
ATOM   10683 O  O   . ALA J  1 95  ? 47.211  74.737  49.072  1.00 22.92 ? 95  ALA J O   1 
ATOM   10684 C  CB  . ALA J  1 95  ? 46.904  77.158  47.395  1.00 20.49 ? 95  ALA J CB  1 
ATOM   10685 N  N   . ASP J  1 96  ? 48.098  73.949  47.134  1.00 24.03 ? 96  ASP J N   1 
ATOM   10686 C  CA  . ASP J  1 96  ? 48.976  73.017  47.825  1.00 27.03 ? 96  ASP J CA  1 
ATOM   10687 C  C   . ASP J  1 96  ? 50.366  73.608  47.977  1.00 25.58 ? 96  ASP J C   1 
ATOM   10688 O  O   . ASP J  1 96  ? 51.198  73.499  47.088  1.00 27.64 ? 96  ASP J O   1 
ATOM   10689 C  CB  . ASP J  1 96  ? 49.000  71.654  47.125  1.00 28.77 ? 96  ASP J CB  1 
ATOM   10690 C  CG  . ASP J  1 96  ? 47.665  70.920  47.253  1.00 37.41 ? 96  ASP J CG  1 
ATOM   10691 O  OD1 . ASP J  1 96  ? 47.302  70.514  48.394  1.00 41.05 ? 96  ASP J OD1 1 
ATOM   10692 O  OD2 . ASP J  1 96  ? 46.972  70.760  46.221  1.00 34.67 ? 96  ASP J OD2 1 
ATOM   10693 N  N   . VAL J  1 97  ? 50.599  74.238  49.121  1.00 27.53 ? 97  VAL J N   1 
ATOM   10694 C  CA  . VAL J  1 97  ? 51.784  75.057  49.316  1.00 24.14 ? 97  VAL J CA  1 
ATOM   10695 C  C   . VAL J  1 97  ? 53.060  74.242  49.500  1.00 24.77 ? 97  VAL J C   1 
ATOM   10696 O  O   . VAL J  1 97  ? 53.116  73.337  50.315  1.00 24.66 ? 97  VAL J O   1 
ATOM   10697 C  CB  . VAL J  1 97  ? 51.598  75.951  50.528  1.00 22.22 ? 97  VAL J CB  1 
ATOM   10698 C  CG1 . VAL J  1 97  ? 52.817  76.842  50.726  1.00 20.46 ? 97  VAL J CG1 1 
ATOM   10699 C  CG2 . VAL J  1 97  ? 50.346  76.763  50.359  1.00 22.04 ? 97  VAL J CG2 1 
ATOM   10700 N  N   . SER J  1 98  ? 54.087  74.575  48.733  1.00 22.78 ? 98  SER J N   1 
ATOM   10701 C  CA  . SER J  1 98  ? 55.411  73.995  48.945  1.00 25.55 ? 98  SER J CA  1 
ATOM   10702 C  C   . SER J  1 98  ? 56.486  74.950  48.483  1.00 21.97 ? 98  SER J C   1 
ATOM   10703 O  O   . SER J  1 98  ? 56.751  75.077  47.294  1.00 20.53 ? 98  SER J O   1 
ATOM   10704 C  CB  . SER J  1 98  ? 55.587  72.665  48.231  1.00 23.19 ? 98  SER J CB  1 
ATOM   10705 O  OG  . SER J  1 98  ? 56.869  72.150  48.536  1.00 26.59 ? 98  SER J OG  1 
ATOM   10706 N  N   . ILE J  1 99  ? 57.102  75.604  49.455  1.00 18.50 ? 99  ILE J N   1 
ATOM   10707 C  CA  . ILE J  1 99  ? 58.082  76.631  49.227  1.00 19.07 ? 99  ILE J CA  1 
ATOM   10708 C  C   . ILE J  1 99  ? 59.291  76.313  50.087  1.00 25.78 ? 99  ILE J C   1 
ATOM   10709 O  O   . ILE J  1 99  ? 59.138  75.879  51.239  1.00 27.29 ? 99  ILE J O   1 
ATOM   10710 C  CB  . ILE J  1 99  ? 57.515  77.978  49.697  1.00 21.46 ? 99  ILE J CB  1 
ATOM   10711 C  CG1 . ILE J  1 99  ? 56.305  78.391  48.853  1.00 23.70 ? 99  ILE J CG1 1 
ATOM   10712 C  CG2 . ILE J  1 99  ? 58.558  79.063  49.652  1.00 22.06 ? 99  ILE J CG2 1 
ATOM   10713 C  CD1 . ILE J  1 99  ? 55.642  79.688  49.353  1.00 14.62 ? 99  ILE J CD1 1 
ATOM   10714 N  N   . GLU J  1 100 ? 60.490  76.533  49.555  1.00 22.51 ? 100 GLU J N   1 
ATOM   10715 C  CA  . GLU J  1 100 ? 61.689  76.534  50.390  1.00 20.31 ? 100 GLU J CA  1 
ATOM   10716 C  C   . GLU J  1 100 ? 62.322  77.922  50.402  1.00 21.42 ? 100 GLU J C   1 
ATOM   10717 O  O   . GLU J  1 100 ? 62.501  78.529  49.351  1.00 21.75 ? 100 GLU J O   1 
ATOM   10718 C  CB  . GLU J  1 100 ? 62.698  75.499  49.910  1.00 21.47 ? 100 GLU J CB  1 
ATOM   10719 C  CG  . GLU J  1 100 ? 63.856  75.345  50.871  1.00 27.53 ? 100 GLU J CG  1 
ATOM   10720 C  CD  . GLU J  1 100 ? 64.831  74.256  50.460  1.00 34.01 ? 100 GLU J CD  1 
ATOM   10721 O  OE1 . GLU J  1 100 ? 64.460  73.061  50.516  1.00 31.54 ? 100 GLU J OE1 1 
ATOM   10722 O  OE2 . GLU J  1 100 ? 65.972  74.606  50.089  1.00 42.29 ? 100 GLU J OE2 1 
ATOM   10723 N  N   . ASP J  1 101 ? 62.631  78.442  51.586  1.00 15.80 ? 101 ASP J N   1 
ATOM   10724 C  CA  . ASP J  1 101 ? 63.201  79.775  51.682  1.00 16.96 ? 101 ASP J CA  1 
ATOM   10725 C  C   . ASP J  1 101 ? 64.387  79.852  52.650  1.00 23.90 ? 101 ASP J C   1 
ATOM   10726 O  O   . ASP J  1 101 ? 64.363  79.267  53.732  1.00 20.79 ? 101 ASP J O   1 
ATOM   10727 C  CB  . ASP J  1 101 ? 62.143  80.807  52.071  1.00 14.39 ? 101 ASP J CB  1 
ATOM   10728 C  CG  . ASP J  1 101 ? 62.628  82.218  51.864  1.00 16.80 ? 101 ASP J CG  1 
ATOM   10729 O  OD1 . ASP J  1 101 ? 62.716  82.659  50.696  1.00 19.34 ? 101 ASP J OD1 1 
ATOM   10730 O  OD2 . ASP J  1 101 ? 62.948  82.899  52.859  1.00 19.85 ? 101 ASP J OD2 1 
ATOM   10731 N  N   . SER J  1 102 ? 65.416  80.597  52.261  1.00 19.29 ? 102 SER J N   1 
ATOM   10732 C  CA  . SER J  1 102 ? 66.627  80.668  53.061  1.00 22.60 ? 102 SER J CA  1 
ATOM   10733 C  C   . SER J  1 102 ? 66.725  81.958  53.822  1.00 16.53 ? 102 SER J C   1 
ATOM   10734 O  O   . SER J  1 102 ? 67.691  82.185  54.510  1.00 19.81 ? 102 SER J O   1 
ATOM   10735 C  CB  . SER J  1 102 ? 67.865  80.521  52.177  1.00 21.49 ? 102 SER J CB  1 
ATOM   10736 O  OG  . SER J  1 102 ? 67.917  79.225  51.619  1.00 26.33 ? 102 SER J OG  1 
ATOM   10737 N  N   . VAL J  1 103 ? 65.744  82.828  53.693  1.00 17.80 ? 103 VAL J N   1 
ATOM   10738 C  CA  . VAL J  1 103 ? 65.851  84.113  54.377  1.00 19.47 ? 103 VAL J CA  1 
ATOM   10739 C  C   . VAL J  1 103 ? 65.087  84.139  55.717  1.00 18.97 ? 103 VAL J C   1 
ATOM   10740 O  O   . VAL J  1 103 ? 65.589  84.680  56.710  1.00 22.47 ? 103 VAL J O   1 
ATOM   10741 C  CB  . VAL J  1 103 ? 65.414  85.269  53.471  1.00 18.12 ? 103 VAL J CB  1 
ATOM   10742 C  CG1 . VAL J  1 103 ? 65.339  86.570  54.271  1.00 16.18 ? 103 VAL J CG1 1 
ATOM   10743 C  CG2 . VAL J  1 103 ? 66.378  85.408  52.268  1.00 14.09 ? 103 VAL J CG2 1 
ATOM   10744 N  N   . ILE J  1 104 ? 63.881  83.574  55.743  1.00 16.33 ? 104 ILE J N   1 
ATOM   10745 C  CA  . ILE J  1 104 ? 63.166  83.399  57.009  1.00 19.86 ? 104 ILE J CA  1 
ATOM   10746 C  C   . ILE J  1 104 ? 63.917  82.387  57.841  1.00 18.26 ? 104 ILE J C   1 
ATOM   10747 O  O   . ILE J  1 104 ? 64.677  81.590  57.305  1.00 19.81 ? 104 ILE J O   1 
ATOM   10748 C  CB  . ILE J  1 104 ? 61.736  82.857  56.824  1.00 17.39 ? 104 ILE J CB  1 
ATOM   10749 C  CG1 . ILE J  1 104 ? 61.741  81.557  56.015  1.00 16.18 ? 104 ILE J CG1 1 
ATOM   10750 C  CG2 . ILE J  1 104 ? 60.855  83.893  56.179  1.00 17.65 ? 104 ILE J CG2 1 
ATOM   10751 C  CD1 . ILE J  1 104 ? 60.395  80.842  55.996  1.00 14.13 ? 104 ILE J CD1 1 
ATOM   10752 N  N   . SER J  1 105 ? 63.691  82.413  59.150  1.00 25.06 ? 105 SER J N   1 
ATOM   10753 C  CA  . SER J  1 105 ? 64.271  81.416  60.043  1.00 25.35 ? 105 SER J CA  1 
ATOM   10754 C  C   . SER J  1 105 ? 63.337  81.102  61.217  1.00 22.82 ? 105 SER J C   1 
ATOM   10755 O  O   . SER J  1 105 ? 62.385  81.843  61.471  1.00 23.13 ? 105 SER J O   1 
ATOM   10756 C  CB  . SER J  1 105 ? 65.624  81.906  60.573  1.00 19.41 ? 105 SER J CB  1 
ATOM   10757 O  OG  . SER J  1 105 ? 66.262  80.867  61.274  1.00 24.42 ? 105 SER J OG  1 
ATOM   10758 N  N   . LEU J  1 106 ? 63.623  80.013  61.936  1.00 24.16 ? 106 LEU J N   1 
ATOM   10759 C  CA  . LEU J  1 106 ? 62.901  79.717  63.184  1.00 26.07 ? 106 LEU J CA  1 
ATOM   10760 C  C   . LEU J  1 106 ? 63.763  79.976  64.422  1.00 28.17 ? 106 LEU J C   1 
ATOM   10761 O  O   . LEU J  1 106 ? 63.465  79.477  65.500  1.00 26.48 ? 106 LEU J O   1 
ATOM   10762 C  CB  . LEU J  1 106 ? 62.356  78.290  63.206  1.00 18.28 ? 106 LEU J CB  1 
ATOM   10763 C  CG  . LEU J  1 106 ? 61.643  77.839  61.928  1.00 26.42 ? 106 LEU J CG  1 
ATOM   10764 C  CD1 . LEU J  1 106 ? 61.323  76.361  61.979  1.00 29.55 ? 106 LEU J CD1 1 
ATOM   10765 C  CD2 . LEU J  1 106 ? 60.388  78.649  61.710  1.00 25.41 ? 106 LEU J CD2 1 
ATOM   10766 N  N   . SER J  1 107 ? 64.829  80.750  64.248  1.00 22.68 ? 107 SER J N   1 
ATOM   10767 C  CA  . SER J  1 107 ? 65.618  81.241  65.366  1.00 24.87 ? 107 SER J CA  1 
ATOM   10768 C  C   . SER J  1 107 ? 66.326  82.526  64.965  1.00 28.95 ? 107 SER J C   1 
ATOM   10769 O  O   . SER J  1 107 ? 66.386  82.858  63.788  1.00 27.00 ? 107 SER J O   1 
ATOM   10770 C  CB  . SER J  1 107 ? 66.640  80.191  65.798  1.00 24.14 ? 107 SER J CB  1 
ATOM   10771 O  OG  . SER J  1 107 ? 67.417  79.742  64.704  1.00 29.96 ? 107 SER J OG  1 
ATOM   10772 N  N   . GLY J  1 108 ? 66.861  83.249  65.942  1.00 27.60 ? 108 GLY J N   1 
ATOM   10773 C  CA  . GLY J  1 108 ? 67.684  84.413  65.660  1.00 24.78 ? 108 GLY J CA  1 
ATOM   10774 C  C   . GLY J  1 108 ? 66.916  85.610  65.138  1.00 27.41 ? 108 GLY J C   1 
ATOM   10775 O  O   . GLY J  1 108 ? 65.686  85.629  65.181  1.00 23.88 ? 108 GLY J O   1 
ATOM   10776 N  N   . ASP J  1 109 ? 67.662  86.604  64.660  1.00 21.60 ? 109 ASP J N   1 
ATOM   10777 C  CA  . ASP J  1 109 ? 67.138  87.862  64.129  1.00 27.97 ? 109 ASP J CA  1 
ATOM   10778 C  C   . ASP J  1 109 ? 65.954  87.700  63.166  1.00 29.05 ? 109 ASP J C   1 
ATOM   10779 O  O   . ASP J  1 109 ? 65.012  88.490  63.199  1.00 23.46 ? 109 ASP J O   1 
ATOM   10780 C  CB  . ASP J  1 109 ? 68.260  88.618  63.391  1.00 28.31 ? 109 ASP J CB  1 
ATOM   10781 C  CG  . ASP J  1 109 ? 69.269  89.250  64.338  1.00 34.76 ? 109 ASP J CG  1 
ATOM   10782 O  OD1 . ASP J  1 109 ? 69.194  88.993  65.562  1.00 36.07 ? 109 ASP J OD1 1 
ATOM   10783 O  OD2 . ASP J  1 109 ? 70.142  90.004  63.852  1.00 36.78 ? 109 ASP J OD2 1 
ATOM   10784 N  N   . HIS J  1 110 ? 66.024  86.686  62.307  1.00 23.28 ? 110 HIS J N   1 
ATOM   10785 C  CA  . HIS J  1 110 ? 65.055  86.518  61.231  1.00 25.90 ? 110 HIS J CA  1 
ATOM   10786 C  C   . HIS J  1 110 ? 63.924  85.591  61.634  1.00 25.36 ? 110 HIS J C   1 
ATOM   10787 O  O   . HIS J  1 110 ? 63.186  85.098  60.775  1.00 20.10 ? 110 HIS J O   1 
ATOM   10788 C  CB  . HIS J  1 110 ? 65.735  85.972  59.969  1.00 22.98 ? 110 HIS J CB  1 
ATOM   10789 C  CG  . HIS J  1 110 ? 66.707  86.925  59.345  1.00 30.51 ? 110 HIS J CG  1 
ATOM   10790 N  ND1 . HIS J  1 110 ? 67.515  86.576  58.282  1.00 37.09 ? 110 HIS J ND1 1 
ATOM   10791 C  CD2 . HIS J  1 110 ? 66.992  88.219  59.626  1.00 28.47 ? 110 HIS J CD2 1 
ATOM   10792 C  CE1 . HIS J  1 110 ? 68.258  87.613  57.938  1.00 33.72 ? 110 HIS J CE1 1 
ATOM   10793 N  NE2 . HIS J  1 110 ? 67.958  88.623  58.736  1.00 36.37 ? 110 HIS J NE2 1 
ATOM   10794 N  N   . CYS J  1 111 ? 63.793  85.351  62.939  1.00 24.54 ? 111 CYS J N   1 
ATOM   10795 C  CA  . CYS J  1 111 ? 62.796  84.407  63.442  1.00 21.97 ? 111 CYS J CA  1 
ATOM   10796 C  C   . CYS J  1 111 ? 61.383  84.839  63.094  1.00 16.71 ? 111 CYS J C   1 
ATOM   10797 O  O   . CYS J  1 111 ? 61.030  85.994  63.272  1.00 18.77 ? 111 CYS J O   1 
ATOM   10798 C  CB  . CYS J  1 111 ? 62.904  84.272  64.961  1.00 23.08 ? 111 CYS J CB  1 
ATOM   10799 S  SG  . CYS J  1 111 ? 61.966  82.909  65.596  1.00 27.59 ? 111 CYS J SG  1 
ATOM   10800 N  N   . ILE J  1 112 ? 60.566  83.912  62.608  1.00 17.72 ? 112 ILE J N   1 
ATOM   10801 C  CA  . ILE J  1 112 ? 59.164  84.245  62.296  1.00 21.28 ? 112 ILE J CA  1 
ATOM   10802 C  C   . ILE J  1 112 ? 58.157  83.654  63.297  1.00 23.43 ? 112 ILE J C   1 
ATOM   10803 O  O   . ILE J  1 112 ? 56.936  83.821  63.155  1.00 22.08 ? 112 ILE J O   1 
ATOM   10804 C  CB  . ILE J  1 112 ? 58.790  83.789  60.893  1.00 17.87 ? 112 ILE J CB  1 
ATOM   10805 C  CG1 . ILE J  1 112 ? 58.920  82.266  60.812  1.00 14.65 ? 112 ILE J CG1 1 
ATOM   10806 C  CG2 . ILE J  1 112 ? 59.669  84.536  59.847  1.00 14.87 ? 112 ILE J CG2 1 
ATOM   10807 C  CD1 . ILE J  1 112 ? 58.551  81.665  59.471  1.00 18.25 ? 112 ILE J CD1 1 
ATOM   10808 N  N   . ILE J  1 113 ? 58.669  82.965  64.311  1.00 23.54 ? 113 ILE J N   1 
ATOM   10809 C  CA  . ILE J  1 113 ? 57.800  82.434  65.365  1.00 23.40 ? 113 ILE J CA  1 
ATOM   10810 C  C   . ILE J  1 113 ? 57.144  83.578  66.113  1.00 19.15 ? 113 ILE J C   1 
ATOM   10811 O  O   . ILE J  1 113 ? 57.794  84.576  66.409  1.00 17.37 ? 113 ILE J O   1 
ATOM   10812 C  CB  . ILE J  1 113 ? 58.562  81.501  66.298  1.00 19.09 ? 113 ILE J CB  1 
ATOM   10813 C  CG1 . ILE J  1 113 ? 58.917  80.227  65.526  1.00 17.54 ? 113 ILE J CG1 1 
ATOM   10814 C  CG2 . ILE J  1 113 ? 57.714  81.178  67.515  1.00 28.87 ? 113 ILE J CG2 1 
ATOM   10815 C  CD1 . ILE J  1 113 ? 60.035  79.443  66.103  1.00 26.62 ? 113 ILE J CD1 1 
ATOM   10816 N  N   . GLY J  1 114 ? 55.839  83.462  66.360  1.00 21.59 ? 114 GLY J N   1 
ATOM   10817 C  CA  . GLY J  1 114 ? 55.112  84.492  67.086  1.00 19.73 ? 114 GLY J CA  1 
ATOM   10818 C  C   . GLY J  1 114 ? 54.747  85.648  66.179  1.00 22.82 ? 114 GLY J C   1 
ATOM   10819 O  O   . GLY J  1 114 ? 54.408  86.745  66.621  1.00 25.07 ? 114 GLY J O   1 
ATOM   10820 N  N   . ARG J  1 115 ? 54.823  85.403  64.880  1.00 25.62 ? 115 ARG J N   1 
ATOM   10821 C  CA  . ARG J  1 115 ? 54.388  86.401  63.920  1.00 23.01 ? 115 ARG J CA  1 
ATOM   10822 C  C   . ARG J  1 115 ? 53.263  85.818  63.094  1.00 19.95 ? 115 ARG J C   1 
ATOM   10823 O  O   . ARG J  1 115 ? 52.972  84.632  63.198  1.00 22.11 ? 115 ARG J O   1 
ATOM   10824 C  CB  . ARG J  1 115 ? 55.566  86.864  63.061  1.00 21.72 ? 115 ARG J CB  1 
ATOM   10825 C  CG  . ARG J  1 115 ? 56.622  87.545  63.910  1.00 26.50 ? 115 ARG J CG  1 
ATOM   10826 C  CD  . ARG J  1 115 ? 57.771  88.074  63.102  1.00 20.87 ? 115 ARG J CD  1 
ATOM   10827 N  NE  . ARG J  1 115 ? 58.952  88.268  63.932  1.00 23.07 ? 115 ARG J NE  1 
ATOM   10828 C  CZ  . ARG J  1 115 ? 59.231  89.379  64.610  1.00 23.00 ? 115 ARG J CZ  1 
ATOM   10829 N  NH1 . ARG J  1 115 ? 58.399  90.410  64.587  1.00 19.74 ? 115 ARG J NH1 1 
ATOM   10830 N  NH2 . ARG J  1 115 ? 60.353  89.452  65.318  1.00 20.55 ? 115 ARG J NH2 1 
ATOM   10831 N  N   . THR J  1 116 ? 52.652  86.655  62.264  1.00 19.67 ? 116 THR J N   1 
ATOM   10832 C  CA  . THR J  1 116 ? 51.424  86.298  61.570  1.00 21.51 ? 116 THR J CA  1 
ATOM   10833 C  C   . THR J  1 116 ? 51.660  85.938  60.101  1.00 19.68 ? 116 THR J C   1 
ATOM   10834 O  O   . THR J  1 116 ? 52.042  86.783  59.299  1.00 20.08 ? 116 THR J O   1 
ATOM   10835 C  CB  . THR J  1 116 ? 50.416  87.469  61.649  1.00 25.31 ? 116 THR J CB  1 
ATOM   10836 O  OG1 . THR J  1 116 ? 50.262  87.887  63.016  1.00 20.22 ? 116 THR J OG1 1 
ATOM   10837 C  CG2 . THR J  1 116 ? 49.057  87.077  61.056  1.00 19.89 ? 116 THR J CG2 1 
ATOM   10838 N  N   . LEU J  1 117 ? 51.456  84.676  59.757  1.00 16.42 ? 117 LEU J N   1 
ATOM   10839 C  CA  . LEU J  1 117 ? 51.404  84.291  58.362  1.00 19.28 ? 117 LEU J CA  1 
ATOM   10840 C  C   . LEU J  1 117 ? 50.099  84.815  57.753  1.00 21.91 ? 117 LEU J C   1 
ATOM   10841 O  O   . LEU J  1 117 ? 49.040  84.667  58.362  1.00 20.61 ? 117 LEU J O   1 
ATOM   10842 C  CB  . LEU J  1 117 ? 51.460  82.777  58.244  1.00 15.96 ? 117 LEU J CB  1 
ATOM   10843 C  CG  . LEU J  1 117 ? 51.570  82.341  56.794  1.00 17.30 ? 117 LEU J CG  1 
ATOM   10844 C  CD1 . LEU J  1 117 ? 52.860  82.911  56.192  1.00 13.08 ? 117 LEU J CD1 1 
ATOM   10845 C  CD2 . LEU J  1 117 ? 51.542  80.830  56.700  1.00 18.12 ? 117 LEU J CD2 1 
ATOM   10846 N  N   . VAL J  1 118 ? 50.167  85.428  56.572  1.00 18.91 ? 118 VAL J N   1 
ATOM   10847 C  CA  . VAL J  1 118 ? 48.959  85.928  55.887  1.00 17.63 ? 118 VAL J CA  1 
ATOM   10848 C  C   . VAL J  1 118 ? 48.871  85.484  54.428  1.00 18.77 ? 118 VAL J C   1 
ATOM   10849 O  O   . VAL J  1 118 ? 49.866  85.545  53.690  1.00 15.40 ? 118 VAL J O   1 
ATOM   10850 C  CB  . VAL J  1 118 ? 48.880  87.467  55.906  1.00 16.48 ? 118 VAL J CB  1 
ATOM   10851 C  CG1 . VAL J  1 118 ? 47.654  87.948  55.135  1.00 16.68 ? 118 VAL J CG1 1 
ATOM   10852 C  CG2 . VAL J  1 118 ? 48.847  87.990  57.328  1.00 16.60 ? 118 VAL J CG2 1 
ATOM   10853 N  N   . VAL J  1 119 ? 47.683  85.028  54.019  1.00 16.70 ? 119 VAL J N   1 
ATOM   10854 C  CA  . VAL J  1 119 ? 47.393  84.765  52.614  1.00 14.45 ? 119 VAL J CA  1 
ATOM   10855 C  C   . VAL J  1 119 ? 46.423  85.813  52.049  1.00 16.42 ? 119 VAL J C   1 
ATOM   10856 O  O   . VAL J  1 119 ? 45.369  86.111  52.633  1.00 18.40 ? 119 VAL J O   1 
ATOM   10857 C  CB  . VAL J  1 119 ? 46.882  83.320  52.359  1.00 17.11 ? 119 VAL J CB  1 
ATOM   10858 C  CG1 . VAL J  1 119 ? 45.568  83.049  53.080  1.00 16.57 ? 119 VAL J CG1 1 
ATOM   10859 C  CG2 . VAL J  1 119 ? 46.724  83.082  50.871  1.00 13.85 ? 119 VAL J CG2 1 
ATOM   10860 N  N   . HIS J  1 120 ? 46.785  86.362  50.897  1.00 17.63 ? 120 HIS J N   1 
ATOM   10861 C  CA  . HIS J  1 120 ? 46.135  87.550  50.342  1.00 17.05 ? 120 HIS J CA  1 
ATOM   10862 C  C   . HIS J  1 120 ? 45.153  87.324  49.207  1.00 17.64 ? 120 HIS J C   1 
ATOM   10863 O  O   . HIS J  1 120 ? 45.157  86.279  48.550  1.00 17.99 ? 120 HIS J O   1 
ATOM   10864 C  CB  . HIS J  1 120 ? 47.205  88.526  49.839  1.00 16.08 ? 120 HIS J CB  1 
ATOM   10865 C  CG  . HIS J  1 120 ? 47.906  89.243  50.939  1.00 16.89 ? 120 HIS J CG  1 
ATOM   10866 N  ND1 . HIS J  1 120 ? 47.566  90.521  51.322  1.00 16.25 ? 120 HIS J ND1 1 
ATOM   10867 C  CD2 . HIS J  1 120 ? 48.900  88.847  51.769  1.00 14.59 ? 120 HIS J CD2 1 
ATOM   10868 C  CE1 . HIS J  1 120 ? 48.329  90.888  52.333  1.00 16.56 ? 120 HIS J CE1 1 
ATOM   10869 N  NE2 . HIS J  1 120 ? 49.149  89.892  52.620  1.00 17.70 ? 120 HIS J NE2 1 
ATOM   10870 N  N   . GLU J  1 121 ? 44.371  88.371  48.959  1.00 17.32 ? 121 GLU J N   1 
ATOM   10871 C  CA  . GLU J  1 121 ? 43.313  88.405  47.957  1.00 17.95 ? 121 GLU J CA  1 
ATOM   10872 C  C   . GLU J  1 121 ? 43.831  88.227  46.533  1.00 18.56 ? 121 GLU J C   1 
ATOM   10873 O  O   . GLU J  1 121 ? 43.207  87.549  45.723  1.00 17.95 ? 121 GLU J O   1 
ATOM   10874 C  CB  . GLU J  1 121 ? 42.571  89.744  48.070  1.00 17.02 ? 121 GLU J CB  1 
ATOM   10875 C  CG  . GLU J  1 121 ? 41.439  89.948  47.066  1.00 21.59 ? 121 GLU J CG  1 
ATOM   10876 C  CD  . GLU J  1 121 ? 41.013  91.409  46.964  1.00 28.21 ? 121 GLU J CD  1 
ATOM   10877 O  OE1 . GLU J  1 121 ? 40.174  91.712  46.091  1.00 35.80 ? 121 GLU J OE1 1 
ATOM   10878 O  OE2 . GLU J  1 121 ? 41.525  92.259  47.735  1.00 25.17 ? 121 GLU J OE2 1 
ATOM   10879 N  N   . LYS J  1 122 ? 44.970  88.841  46.232  1.00 16.82 ? 122 LYS J N   1 
ATOM   10880 C  CA  . LYS J  1 122 ? 45.493  88.861  44.862  1.00 19.31 ? 122 LYS J CA  1 
ATOM   10881 C  C   . LYS J  1 122 ? 46.956  88.449  44.785  1.00 15.49 ? 122 LYS J C   1 
ATOM   10882 O  O   . LYS J  1 122 ? 47.602  88.233  45.809  1.00 15.22 ? 122 LYS J O   1 
ATOM   10883 C  CB  . LYS J  1 122 ? 45.351  90.262  44.278  1.00 19.93 ? 122 LYS J CB  1 
ATOM   10884 C  CG  . LYS J  1 122 ? 43.924  90.757  44.234  1.00 22.89 ? 122 LYS J CG  1 
ATOM   10885 C  CD  . LYS J  1 122 ? 43.844  92.109  43.561  1.00 20.81 ? 122 LYS J CD  1 
ATOM   10886 C  CE  . LYS J  1 122 ? 44.383  93.180  44.455  1.00 22.82 ? 122 LYS J CE  1 
ATOM   10887 N  NZ  . LYS J  1 122 ? 44.235  94.508  43.808  1.00 31.63 ? 122 LYS J NZ  1 
ATOM   10888 N  N   . ALA J  1 123 ? 47.475  88.354  43.565  1.00 12.47 ? 123 ALA J N   1 
ATOM   10889 C  CA  . ALA J  1 123 ? 48.880  88.027  43.346  1.00 17.54 ? 123 ALA J CA  1 
ATOM   10890 C  C   . ALA J  1 123 ? 49.787  89.099  43.923  1.00 11.01 ? 123 ALA J C   1 
ATOM   10891 O  O   . ALA J  1 123 ? 49.466  90.274  43.886  1.00 13.60 ? 123 ALA J O   1 
ATOM   10892 C  CB  . ALA J  1 123 ? 49.182  87.844  41.841  1.00 15.19 ? 123 ALA J CB  1 
ATOM   10893 N  N   . ASP J  1 124 ? 50.901  88.662  44.481  1.00 9.95  ? 124 ASP J N   1 
ATOM   10894 C  CA  . ASP J  1 124 ? 52.002  89.534  44.823  1.00 11.66 ? 124 ASP J CA  1 
ATOM   10895 C  C   . ASP J  1 124 ? 52.815  89.761  43.524  1.00 14.65 ? 124 ASP J C   1 
ATOM   10896 O  O   . ASP J  1 124 ? 53.198  88.791  42.837  1.00 10.81 ? 124 ASP J O   1 
ATOM   10897 C  CB  . ASP J  1 124 ? 52.844  88.839  45.897  1.00 11.21 ? 124 ASP J CB  1 
ATOM   10898 C  CG  . ASP J  1 124 ? 54.040  89.683  46.381  1.00 13.02 ? 124 ASP J CG  1 
ATOM   10899 O  OD1 . ASP J  1 124 ? 54.524  90.550  45.628  1.00 11.03 ? 124 ASP J OD1 1 
ATOM   10900 O  OD2 . ASP J  1 124 ? 54.495  89.464  47.534  1.00 11.01 ? 124 ASP J OD2 1 
ATOM   10901 N  N   . ASP J  1 125 ? 53.085  91.028  43.204  1.00 11.81 ? 125 ASP J N   1 
ATOM   10902 C  CA  . ASP J  1 125 ? 53.797  91.382  41.970  1.00 13.09 ? 125 ASP J CA  1 
ATOM   10903 C  C   . ASP J  1 125 ? 55.315  91.428  42.164  1.00 13.21 ? 125 ASP J C   1 
ATOM   10904 O  O   . ASP J  1 125 ? 56.044  91.887  41.289  1.00 12.10 ? 125 ASP J O   1 
ATOM   10905 C  CB  . ASP J  1 125 ? 53.261  92.692  41.350  1.00 11.72 ? 125 ASP J CB  1 
ATOM   10906 C  CG  . ASP J  1 125 ? 53.619  93.944  42.152  1.00 11.71 ? 125 ASP J CG  1 
ATOM   10907 O  OD1 . ASP J  1 125 ? 54.485  93.918  43.050  1.00 12.06 ? 125 ASP J OD1 1 
ATOM   10908 O  OD2 . ASP J  1 125 ? 53.041  95.000  41.849  1.00 12.42 ? 125 ASP J OD2 1 
ATOM   10909 N  N   . LEU J  1 126 ? 55.765  90.981  43.333  1.00 11.26 ? 126 LEU J N   1 
ATOM   10910 C  CA  . LEU J  1 126 ? 57.189  90.791  43.624  1.00 10.24 ? 126 LEU J CA  1 
ATOM   10911 C  C   . LEU J  1 126 ? 58.008  92.076  43.485  1.00 11.26 ? 126 LEU J C   1 
ATOM   10912 O  O   . LEU J  1 126 ? 59.197  92.023  43.207  1.00 12.80 ? 126 LEU J O   1 
ATOM   10913 C  CB  . LEU J  1 126 ? 57.791  89.677  42.748  1.00 11.52 ? 126 LEU J CB  1 
ATOM   10914 C  CG  . LEU J  1 126 ? 56.956  88.391  42.613  1.00 14.24 ? 126 LEU J CG  1 
ATOM   10915 C  CD1 . LEU J  1 126 ? 57.700  87.321  41.787  1.00 12.90 ? 126 LEU J CD1 1 
ATOM   10916 C  CD2 . LEU J  1 126 ? 56.543  87.841  43.987  1.00 14.19 ? 126 LEU J CD2 1 
ATOM   10917 N  N   . GLY J  1 127 ? 57.373  93.226  43.694  1.00 12.41 ? 127 GLY J N   1 
ATOM   10918 C  CA  . GLY J  1 127 ? 58.063  94.509  43.629  1.00 10.35 ? 127 GLY J CA  1 
ATOM   10919 C  C   . GLY J  1 127 ? 58.256  95.078  42.233  1.00 10.18 ? 127 GLY J C   1 
ATOM   10920 O  O   . GLY J  1 127 ? 58.898  96.111  42.062  1.00 9.54  ? 127 GLY J O   1 
ATOM   10921 N  N   . LYS J  1 128 ? 57.662  94.432  41.233  1.00 10.98 ? 128 LYS J N   1 
ATOM   10922 C  CA  . LYS J  1 128 ? 57.868  94.822  39.840  1.00 11.99 ? 128 LYS J CA  1 
ATOM   10923 C  C   . LYS J  1 128 ? 56.713  95.660  39.282  1.00 14.13 ? 128 LYS J C   1 
ATOM   10924 O  O   . LYS J  1 128 ? 56.599  95.834  38.064  1.00 11.45 ? 128 LYS J O   1 
ATOM   10925 C  CB  . LYS J  1 128 ? 58.074  93.561  38.993  1.00 11.77 ? 128 LYS J CB  1 
ATOM   10926 C  CG  . LYS J  1 128 ? 59.176  92.622  39.573  1.00 14.26 ? 128 LYS J CG  1 
ATOM   10927 C  CD  . LYS J  1 128 ? 59.292  91.330  38.788  1.00 19.89 ? 128 LYS J CD  1 
ATOM   10928 C  CE  . LYS J  1 128 ? 59.947  91.577  37.409  1.00 24.47 ? 128 LYS J CE  1 
ATOM   10929 N  NZ  . LYS J  1 128 ? 59.688  90.438  36.490  1.00 30.58 ? 128 LYS J NZ  1 
ATOM   10930 N  N   . GLY J  1 129 ? 55.861  96.171  40.169  1.00 9.41  ? 129 GLY J N   1 
ATOM   10931 C  CA  . GLY J  1 129 ? 54.622  96.823  39.750  1.00 10.17 ? 129 GLY J CA  1 
ATOM   10932 C  C   . GLY J  1 129 ? 54.741  98.272  39.275  1.00 11.03 ? 129 GLY J C   1 
ATOM   10933 O  O   . GLY J  1 129 ? 53.843  98.784  38.585  1.00 8.78  ? 129 GLY J O   1 
ATOM   10934 N  N   . GLY J  1 130 ? 55.838  98.928  39.660  1.00 8.52  ? 130 GLY J N   1 
ATOM   10935 C  CA  . GLY J  1 130 ? 56.135  100.296 39.275  1.00 10.82 ? 130 GLY J CA  1 
ATOM   10936 C  C   . GLY J  1 130 ? 55.257  101.349 39.950  1.00 13.09 ? 130 GLY J C   1 
ATOM   10937 O  O   . GLY J  1 130 ? 55.266  102.515 39.571  1.00 10.14 ? 130 GLY J O   1 
ATOM   10938 N  N   . ASN J  1 131 ? 54.479  100.943 40.945  1.00 9.26  ? 131 ASN J N   1 
ATOM   10939 C  CA  . ASN J  1 131 ? 53.724  101.914 41.707  1.00 13.22 ? 131 ASN J CA  1 
ATOM   10940 C  C   . ASN J  1 131 ? 54.194  101.895 43.161  1.00 14.09 ? 131 ASN J C   1 
ATOM   10941 O  O   . ASN J  1 131 ? 54.974  101.017 43.543  1.00 16.88 ? 131 ASN J O   1 
ATOM   10942 C  CB  . ASN J  1 131 ? 52.202  101.728 41.531  1.00 11.44 ? 131 ASN J CB  1 
ATOM   10943 C  CG  . ASN J  1 131 ? 51.642  100.557 42.317  1.00 11.43 ? 131 ASN J CG  1 
ATOM   10944 O  OD1 . ASN J  1 131 ? 52.355  99.620  42.671  1.00 12.89 ? 131 ASN J OD1 1 
ATOM   10945 N  ND2 . ASN J  1 131 ? 50.347  100.613 42.598  1.00 10.85 ? 131 ASN J ND2 1 
ATOM   10946 N  N   . GLU J  1 132 ? 53.785  102.888 43.942  1.00 12.82 ? 132 GLU J N   1 
ATOM   10947 C  CA  . GLU J  1 132 ? 54.219  103.015 45.341  1.00 13.52 ? 132 GLU J CA  1 
ATOM   10948 C  C   . GLU J  1 132 ? 53.952  101.736 46.122  1.00 16.30 ? 132 GLU J C   1 
ATOM   10949 O  O   . GLU J  1 132 ? 54.792  101.254 46.885  1.00 15.76 ? 132 GLU J O   1 
ATOM   10950 C  CB  . GLU J  1 132 ? 53.456  104.151 46.027  1.00 16.24 ? 132 GLU J CB  1 
ATOM   10951 C  CG  . GLU J  1 132 ? 53.652  105.534 45.428  1.00 20.49 ? 132 GLU J CG  1 
ATOM   10952 C  CD  . GLU J  1 132 ? 52.737  106.592 46.046  1.00 28.51 ? 132 GLU J CD  1 
ATOM   10953 O  OE1 . GLU J  1 132 ? 52.111  106.323 47.100  1.00 30.95 ? 132 GLU J OE1 1 
ATOM   10954 O  OE2 . GLU J  1 132 ? 52.641  107.700 45.473  1.00 29.91 ? 132 GLU J OE2 1 
ATOM   10955 N  N   . GLU J  1 133 ? 52.757  101.194 45.934  1.00 14.74 ? 133 GLU J N   1 
ATOM   10956 C  CA  . GLU J  1 133 ? 52.331  100.030 46.690  1.00 15.86 ? 133 GLU J CA  1 
ATOM   10957 C  C   . GLU J  1 133 ? 53.173  98.785  46.367  1.00 16.68 ? 133 GLU J C   1 
ATOM   10958 O  O   . GLU J  1 133 ? 53.379  97.938  47.229  1.00 16.93 ? 133 GLU J O   1 
ATOM   10959 C  CB  . GLU J  1 133 ? 50.824  99.788  46.466  1.00 18.30 ? 133 GLU J CB  1 
ATOM   10960 C  CG  . GLU J  1 133 ? 50.165  98.906  47.513  1.00 24.91 ? 133 GLU J CG  1 
ATOM   10961 C  CD  . GLU J  1 133 ? 49.896  99.617  48.840  1.00 26.26 ? 133 GLU J CD  1 
ATOM   10962 O  OE1 . GLU J  1 133 ? 50.781  100.331 49.371  1.00 27.28 ? 133 GLU J OE1 1 
ATOM   10963 O  OE2 . GLU J  1 133 ? 48.777  99.451  49.362  1.00 36.21 ? 133 GLU J OE2 1 
ATOM   10964 N  N   . SER J  1 134 ? 53.687  98.689  45.140  1.00 14.70 ? 134 SER J N   1 
ATOM   10965 C  CA  . SER J  1 134 ? 54.470  97.516  44.738  1.00 13.68 ? 134 SER J CA  1 
ATOM   10966 C  C   . SER J  1 134 ? 55.664  97.250  45.653  1.00 13.43 ? 134 SER J C   1 
ATOM   10967 O  O   . SER J  1 134 ? 55.914  96.118  46.053  1.00 13.56 ? 134 SER J O   1 
ATOM   10968 C  CB  . SER J  1 134 ? 54.961  97.639  43.289  1.00 12.01 ? 134 SER J CB  1 
ATOM   10969 O  OG  . SER J  1 134 ? 55.607  96.439  42.893  1.00 12.51 ? 134 SER J OG  1 
ATOM   10970 N  N   . THR J  1 135 ? 56.414  98.289  45.981  1.00 13.88 ? 135 THR J N   1 
ATOM   10971 C  CA  . THR J  1 135 ? 57.566  98.091  46.849  1.00 18.49 ? 135 THR J CA  1 
ATOM   10972 C  C   . THR J  1 135 ? 57.222  98.091  48.340  1.00 16.82 ? 135 THR J C   1 
ATOM   10973 O  O   . THR J  1 135 ? 58.116  98.030  49.178  1.00 16.46 ? 135 THR J O   1 
ATOM   10974 C  CB  . THR J  1 135 ? 58.674  99.098  46.557  1.00 20.28 ? 135 THR J CB  1 
ATOM   10975 O  OG1 . THR J  1 135 ? 58.084  100.382 46.346  1.00 25.77 ? 135 THR J OG1 1 
ATOM   10976 C  CG2 . THR J  1 135 ? 59.422  98.670  45.299  1.00 21.43 ? 135 THR J CG2 1 
ATOM   10977 N  N   . LYS J  1 136 ? 55.928  98.125  48.653  1.00 15.00 ? 136 LYS J N   1 
ATOM   10978 C  CA  . LYS J  1 136 ? 55.461  97.949  50.040  1.00 21.72 ? 136 LYS J CA  1 
ATOM   10979 C  C   . LYS J  1 136 ? 54.829  96.585  50.253  1.00 16.85 ? 136 LYS J C   1 
ATOM   10980 O  O   . LYS J  1 136 ? 55.245  95.823  51.116  1.00 17.76 ? 136 LYS J O   1 
ATOM   10981 C  CB  . LYS J  1 136 ? 54.434  99.021  50.421  1.00 18.71 ? 136 LYS J CB  1 
ATOM   10982 C  CG  . LYS J  1 136 ? 55.009  100.410 50.665  1.00 21.05 ? 136 LYS J CG  1 
ATOM   10983 C  CD  . LYS J  1 136 ? 53.889  101.431 50.848  1.00 25.85 ? 136 LYS J CD  1 
ATOM   10984 C  CE  . LYS J  1 136 ? 54.427  102.853 50.812  1.00 32.58 ? 136 LYS J CE  1 
ATOM   10985 N  NZ  . LYS J  1 136 ? 53.338  103.879 50.875  1.00 34.46 ? 136 LYS J NZ  1 
ATOM   10986 N  N   . THR J  1 137 ? 53.809  96.281  49.459  1.00 17.36 ? 137 THR J N   1 
ATOM   10987 C  CA  . THR J  1 137 ? 53.026  95.076  49.672  1.00 17.09 ? 137 THR J CA  1 
ATOM   10988 C  C   . THR J  1 137 ? 52.971  94.177  48.450  1.00 15.46 ? 137 THR J C   1 
ATOM   10989 O  O   . THR J  1 137 ? 52.489  93.060  48.533  1.00 15.35 ? 137 THR J O   1 
ATOM   10990 C  CB  . THR J  1 137 ? 51.590  95.433  50.088  1.00 18.23 ? 137 THR J CB  1 
ATOM   10991 O  OG1 . THR J  1 137 ? 50.934  96.095  49.002  1.00 21.71 ? 137 THR J OG1 1 
ATOM   10992 C  CG2 . THR J  1 137 ? 51.618  96.378  51.280  1.00 19.60 ? 137 THR J CG2 1 
ATOM   10993 N  N   . GLY J  1 138 ? 53.472  94.657  47.314  1.00 15.44 ? 138 GLY J N   1 
ATOM   10994 C  CA  . GLY J  1 138 ? 53.407  93.886  46.080  1.00 12.80 ? 138 GLY J CA  1 
ATOM   10995 C  C   . GLY J  1 138 ? 51.988  93.868  45.510  1.00 13.63 ? 138 GLY J C   1 
ATOM   10996 O  O   . GLY J  1 138 ? 51.638  92.982  44.733  1.00 12.01 ? 138 GLY J O   1 
ATOM   10997 N  N   . ASN J  1 139 ? 51.166  94.831  45.928  1.00 13.87 ? 139 ASN J N   1 
ATOM   10998 C  CA  . ASN J  1 139 ? 49.757  94.933  45.493  1.00 14.80 ? 139 ASN J CA  1 
ATOM   10999 C  C   . ASN J  1 139 ? 48.908  93.678  45.701  1.00 11.07 ? 139 ASN J C   1 
ATOM   11000 O  O   . ASN J  1 139 ? 48.045  93.393  44.894  1.00 13.96 ? 139 ASN J O   1 
ATOM   11001 C  CB  . ASN J  1 139 ? 49.684  95.330  44.009  1.00 11.89 ? 139 ASN J CB  1 
ATOM   11002 C  CG  . ASN J  1 139 ? 50.224  96.721  43.751  1.00 14.24 ? 139 ASN J CG  1 
ATOM   11003 O  OD1 . ASN J  1 139 ? 49.612  97.713  44.132  1.00 16.07 ? 139 ASN J OD1 1 
ATOM   11004 N  ND2 . ASN J  1 139 ? 51.381  96.799  43.098  1.00 12.32 ? 139 ASN J ND2 1 
ATOM   11005 N  N   . ALA J  1 140 ? 49.164  92.905  46.747  1.00 13.50 ? 140 ALA J N   1 
ATOM   11006 C  CA  . ALA J  1 140 ? 48.492  91.612  46.874  1.00 17.36 ? 140 ALA J CA  1 
ATOM   11007 C  C   . ALA J  1 140 ? 47.107  91.736  47.517  1.00 14.25 ? 140 ALA J C   1 
ATOM   11008 O  O   . ALA J  1 140 ? 46.410  90.745  47.700  1.00 15.63 ? 140 ALA J O   1 
ATOM   11009 C  CB  . ALA J  1 140 ? 49.368  90.592  47.629  1.00 11.85 ? 140 ALA J CB  1 
ATOM   11010 N  N   . GLY J  1 141 ? 46.716  92.959  47.844  1.00 14.78 ? 141 GLY J N   1 
ATOM   11011 C  CA  . GLY J  1 141 ? 45.353  93.225  48.247  1.00 17.10 ? 141 GLY J CA  1 
ATOM   11012 C  C   . GLY J  1 141 ? 45.075  92.798  49.670  1.00 17.47 ? 141 GLY J C   1 
ATOM   11013 O  O   . GLY J  1 141 ? 45.980  92.724  50.508  1.00 16.39 ? 141 GLY J O   1 
ATOM   11014 N  N   . SER J  1 142 ? 43.813  92.498  49.941  1.00 16.99 ? 142 SER J N   1 
ATOM   11015 C  CA  . SER J  1 142 ? 43.359  92.316  51.314  1.00 18.67 ? 142 SER J CA  1 
ATOM   11016 C  C   . SER J  1 142 ? 43.835  90.993  51.900  1.00 19.64 ? 142 SER J C   1 
ATOM   11017 O  O   . SER J  1 142 ? 44.361  90.119  51.191  1.00 18.10 ? 142 SER J O   1 
ATOM   11018 C  CB  . SER J  1 142 ? 41.834  92.437  51.399  1.00 23.01 ? 142 SER J CB  1 
ATOM   11019 O  OG  . SER J  1 142 ? 41.222  91.283  50.863  1.00 26.62 ? 142 SER J OG  1 
ATOM   11020 N  N   . ARG J  1 143 ? 43.668  90.873  53.209  1.00 19.98 ? 143 ARG J N   1 
ATOM   11021 C  CA  . ARG J  1 143 ? 44.171  89.737  53.956  1.00 20.88 ? 143 ARG J CA  1 
ATOM   11022 C  C   . ARG J  1 143 ? 43.038  88.747  54.142  1.00 20.73 ? 143 ARG J C   1 
ATOM   11023 O  O   . ARG J  1 143 ? 42.122  88.986  54.925  1.00 24.47 ? 143 ARG J O   1 
ATOM   11024 C  CB  . ARG J  1 143 ? 44.729  90.208  55.305  1.00 17.88 ? 143 ARG J CB  1 
ATOM   11025 C  CG  . ARG J  1 143 ? 45.671  91.388  55.156  1.00 21.72 ? 143 ARG J CG  1 
ATOM   11026 C  CD  . ARG J  1 143 ? 46.397  91.800  56.446  1.00 22.43 ? 143 ARG J CD  1 
ATOM   11027 N  NE  . ARG J  1 143 ? 47.242  92.957  56.148  1.00 24.23 ? 143 ARG J NE  1 
ATOM   11028 C  CZ  . ARG J  1 143 ? 48.114  93.528  56.982  1.00 26.36 ? 143 ARG J CZ  1 
ATOM   11029 N  NH1 . ARG J  1 143 ? 48.289  93.064  58.218  1.00 23.55 ? 143 ARG J NH1 1 
ATOM   11030 N  NH2 . ARG J  1 143 ? 48.820  94.578  56.560  1.00 20.74 ? 143 ARG J NH2 1 
ATOM   11031 N  N   . LEU J  1 144 ? 43.110  87.636  53.421  1.00 22.04 ? 144 LEU J N   1 
ATOM   11032 C  CA  . LEU J  1 144 ? 42.001  86.681  53.362  1.00 21.30 ? 144 LEU J CA  1 
ATOM   11033 C  C   . LEU J  1 144 ? 41.939  85.778  54.583  1.00 25.09 ? 144 LEU J C   1 
ATOM   11034 O  O   . LEU J  1 144 ? 40.850  85.454  55.068  1.00 21.47 ? 144 LEU J O   1 
ATOM   11035 C  CB  . LEU J  1 144 ? 42.121  85.802  52.126  1.00 21.96 ? 144 LEU J CB  1 
ATOM   11036 C  CG  . LEU J  1 144 ? 42.081  86.477  50.762  1.00 23.19 ? 144 LEU J CG  1 
ATOM   11037 C  CD1 . LEU J  1 144 ? 41.957  85.409  49.711  1.00 22.86 ? 144 LEU J CD1 1 
ATOM   11038 C  CD2 . LEU J  1 144 ? 40.922  87.475  50.665  1.00 24.02 ? 144 LEU J CD2 1 
ATOM   11039 N  N   . ALA J  1 145 ? 43.108  85.346  55.058  1.00 23.57 ? 145 ALA J N   1 
ATOM   11040 C  CA  . ALA J  1 145 ? 43.188  84.498  56.248  1.00 21.46 ? 145 ALA J CA  1 
ATOM   11041 C  C   . ALA J  1 145 ? 44.554  84.669  56.866  1.00 21.67 ? 145 ALA J C   1 
ATOM   11042 O  O   . ALA J  1 145 ? 45.548  84.874  56.161  1.00 21.97 ? 145 ALA J O   1 
ATOM   11043 C  CB  . ALA J  1 145 ? 42.948  83.041  55.899  1.00 17.40 ? 145 ALA J CB  1 
ATOM   11044 N  N   . CYS J  1 146 ? 44.608  84.588  58.185  1.00 22.74 ? 146 CYS J N   1 
ATOM   11045 C  CA  . CYS J  1 146 ? 45.861  84.797  58.883  1.00 21.07 ? 146 CYS J CA  1 
ATOM   11046 C  C   . CYS J  1 146 ? 45.926  83.921  60.123  1.00 25.46 ? 146 CYS J C   1 
ATOM   11047 O  O   . CYS J  1 146 ? 44.925  83.341  60.548  1.00 22.07 ? 146 CYS J O   1 
ATOM   11048 C  CB  . CYS J  1 146 ? 46.015  86.275  59.254  1.00 23.14 ? 146 CYS J CB  1 
ATOM   11049 S  SG  . CYS J  1 146 ? 45.001  86.821  60.672  1.00 32.79 ? 146 CYS J SG  1 
ATOM   11050 N  N   . GLY J  1 147 ? 47.118  83.822  60.694  1.00 23.77 ? 147 GLY J N   1 
ATOM   11051 C  CA  . GLY J  1 147 ? 47.323  83.047  61.898  1.00 26.48 ? 147 GLY J CA  1 
ATOM   11052 C  C   . GLY J  1 147 ? 48.689  83.348  62.489  1.00 28.95 ? 147 GLY J C   1 
ATOM   11053 O  O   . GLY J  1 147 ? 49.618  83.753  61.759  1.00 21.27 ? 147 GLY J O   1 
ATOM   11054 N  N   . VAL J  1 148 ? 48.804  83.163  63.807  1.00 23.88 ? 148 VAL J N   1 
ATOM   11055 C  CA  . VAL J  1 148 ? 50.080  83.288  64.500  1.00 22.96 ? 148 VAL J CA  1 
ATOM   11056 C  C   . VAL J  1 148 ? 50.928  82.034  64.294  1.00 23.43 ? 148 VAL J C   1 
ATOM   11057 O  O   . VAL J  1 148 ? 50.438  80.907  64.380  1.00 27.79 ? 148 VAL J O   1 
ATOM   11058 C  CB  . VAL J  1 148 ? 49.882  83.569  66.000  1.00 24.33 ? 148 VAL J CB  1 
ATOM   11059 C  CG1 . VAL J  1 148 ? 51.233  83.784  66.691  1.00 22.95 ? 148 VAL J CG1 1 
ATOM   11060 C  CG2 . VAL J  1 148 ? 49.017  84.794  66.175  1.00 24.91 ? 148 VAL J CG2 1 
ATOM   11061 N  N   . ILE J  1 149 ? 52.197  82.233  63.977  1.00 20.48 ? 149 ILE J N   1 
ATOM   11062 C  CA  . ILE J  1 149 ? 53.098  81.107  63.800  1.00 24.18 ? 149 ILE J CA  1 
ATOM   11063 C  C   . ILE J  1 149 ? 53.622  80.676  65.167  1.00 26.27 ? 149 ILE J C   1 
ATOM   11064 O  O   . ILE J  1 149 ? 54.246  81.460  65.889  1.00 23.54 ? 149 ILE J O   1 
ATOM   11065 C  CB  . ILE J  1 149 ? 54.286  81.465  62.885  1.00 25.86 ? 149 ILE J CB  1 
ATOM   11066 C  CG1 . ILE J  1 149 ? 53.779  82.046  61.553  1.00 24.21 ? 149 ILE J CG1 1 
ATOM   11067 C  CG2 . ILE J  1 149 ? 55.167  80.246  62.675  1.00 19.21 ? 149 ILE J CG2 1 
ATOM   11068 C  CD1 . ILE J  1 149 ? 54.896  82.591  60.666  1.00 21.67 ? 149 ILE J CD1 1 
ATOM   11069 N  N   . GLY J  1 150 ? 53.359  79.428  65.519  1.00 27.53 ? 150 GLY J N   1 
ATOM   11070 C  CA  . GLY J  1 150 ? 53.670  78.949  66.850  1.00 29.88 ? 150 GLY J CA  1 
ATOM   11071 C  C   . GLY J  1 150 ? 54.598  77.760  66.799  1.00 31.62 ? 150 GLY J C   1 
ATOM   11072 O  O   . GLY J  1 150 ? 54.617  77.004  65.816  1.00 28.59 ? 150 GLY J O   1 
ATOM   11073 N  N   . ILE J  1 151 ? 55.380  77.612  67.864  1.00 31.91 ? 151 ILE J N   1 
ATOM   11074 C  CA  . ILE J  1 151 ? 56.326  76.515  67.982  1.00 28.26 ? 151 ILE J CA  1 
ATOM   11075 C  C   . ILE J  1 151 ? 55.534  75.219  67.966  1.00 31.88 ? 151 ILE J C   1 
ATOM   11076 O  O   . ILE J  1 151 ? 54.448  75.136  68.545  1.00 32.41 ? 151 ILE J O   1 
ATOM   11077 C  CB  . ILE J  1 151 ? 57.169  76.646  69.280  1.00 29.19 ? 151 ILE J CB  1 
ATOM   11078 C  CG1 . ILE J  1 151 ? 57.824  78.028  69.338  1.00 31.47 ? 151 ILE J CG1 1 
ATOM   11079 C  CG2 . ILE J  1 151 ? 58.234  75.565  69.354  1.00 26.39 ? 151 ILE J CG2 1 
ATOM   11080 C  CD1 . ILE J  1 151 ? 58.337  78.438  70.721  1.00 33.93 ? 151 ILE J CD1 1 
ATOM   11081 N  N   . ALA J  1 152 ? 56.054  74.219  67.268  1.00 32.56 ? 152 ALA J N   1 
ATOM   11082 C  CA  . ALA J  1 152 ? 55.373  72.939  67.176  1.00 31.85 ? 152 ALA J CA  1 
ATOM   11083 C  C   . ALA J  1 152 ? 56.363  71.865  67.524  1.00 36.55 ? 152 ALA J C   1 
ATOM   11084 O  O   . ALA J  1 152 ? 57.574  72.096  67.489  1.00 38.97 ? 152 ALA J O   1 
ATOM   11085 C  CB  . ALA J  1 152 ? 54.844  72.718  65.762  1.00 33.16 ? 152 ALA J CB  1 
ATOM   11086 N  N   . GLN J  1 153 ? 55.856  70.684  67.857  1.00 42.03 ? 153 GLN J N   1 
ATOM   11087 C  CA  . GLN J  1 153 ? 56.725  69.523  67.985  1.00 46.73 ? 153 GLN J CA  1 
ATOM   11088 C  C   . GLN J  1 153 ? 56.687  68.704  66.703  1.00 47.02 ? 153 GLN J C   1 
ATOM   11089 O  O   . GLN J  1 153 ? 55.730  68.795  65.929  1.00 46.70 ? 153 GLN J O   1 
ATOM   11090 C  CB  . GLN J  1 153 ? 56.319  68.658  69.174  1.00 46.60 ? 153 GLN J CB  1 
ATOM   11091 C  CG  . GLN J  1 153 ? 55.000  67.943  68.998  1.00 51.03 ? 153 GLN J CG  1 
ATOM   11092 C  CD  . GLN J  1 153 ? 54.790  66.888  70.056  1.00 49.60 ? 153 GLN J CD  1 
ATOM   11093 O  OE1 . GLN J  1 153 ? 55.614  66.738  70.961  1.00 50.20 ? 153 GLN J OE1 1 
ATOM   11094 N  NE2 . GLN J  1 153 ? 53.690  66.146  69.949  1.00 39.89 ? 153 GLN J NE2 1 
ATOM   11095 O  OXT . GLN J  1 153 ? 57.608  67.932  66.422  1.00 53.08 ? 153 GLN J OXT 1 
ATOM   11096 N  N   . ALA K  1 1   ? 72.958  51.037  27.837  1.00 52.04 ? 1   ALA K N   1 
ATOM   11097 C  CA  . ALA K  1 1   ? 72.077  50.562  26.772  1.00 54.70 ? 1   ALA K CA  1 
ATOM   11098 C  C   . ALA K  1 1   ? 71.282  51.691  26.104  1.00 53.31 ? 1   ALA K C   1 
ATOM   11099 O  O   . ALA K  1 1   ? 70.077  51.830  26.338  1.00 54.85 ? 1   ALA K O   1 
ATOM   11100 C  CB  . ALA K  1 1   ? 71.130  49.480  27.305  1.00 44.15 ? 1   ALA K CB  1 
ATOM   11101 N  N   . THR K  1 2   ? 71.958  52.487  25.276  1.00 49.85 ? 2   THR K N   1 
ATOM   11102 C  CA  . THR K  1 2   ? 71.300  53.540  24.500  1.00 47.16 ? 2   THR K CA  1 
ATOM   11103 C  C   . THR K  1 2   ? 70.171  52.970  23.644  1.00 50.34 ? 2   THR K C   1 
ATOM   11104 O  O   . THR K  1 2   ? 70.278  51.867  23.109  1.00 51.89 ? 2   THR K O   1 
ATOM   11105 C  CB  . THR K  1 2   ? 72.288  54.255  23.552  1.00 47.82 ? 2   THR K CB  1 
ATOM   11106 O  OG1 . THR K  1 2   ? 73.493  54.581  24.250  1.00 52.82 ? 2   THR K OG1 1 
ATOM   11107 C  CG2 . THR K  1 2   ? 71.674  55.529  22.987  1.00 51.13 ? 2   THR K CG2 1 
ATOM   11108 N  N   . LYS K  1 3   ? 69.085  53.725  23.526  1.00 51.12 ? 3   LYS K N   1 
ATOM   11109 C  CA  . LYS K  1 3   ? 67.963  53.347  22.678  1.00 47.85 ? 3   LYS K CA  1 
ATOM   11110 C  C   . LYS K  1 3   ? 67.516  54.532  21.831  1.00 51.03 ? 3   LYS K C   1 
ATOM   11111 O  O   . LYS K  1 3   ? 67.722  55.691  22.207  1.00 48.67 ? 3   LYS K O   1 
ATOM   11112 C  CB  . LYS K  1 3   ? 66.784  52.876  23.520  1.00 46.31 ? 3   LYS K CB  1 
ATOM   11113 C  CG  . LYS K  1 3   ? 67.066  51.666  24.385  1.00 51.41 ? 3   LYS K CG  1 
ATOM   11114 C  CD  . LYS K  1 3   ? 65.858  51.378  25.251  1.00 48.09 ? 3   LYS K CD  1 
ATOM   11115 C  CE  . LYS K  1 3   ? 65.916  50.009  25.887  1.00 48.97 ? 3   LYS K CE  1 
ATOM   11116 N  NZ  . LYS K  1 3   ? 64.548  49.601  26.312  1.00 52.74 ? 3   LYS K NZ  1 
ATOM   11117 N  N   . ALA K  1 4   ? 66.893  54.238  20.693  1.00 49.58 ? 4   ALA K N   1 
ATOM   11118 C  CA  . ALA K  1 4   ? 66.340  55.275  19.832  1.00 49.33 ? 4   ALA K CA  1 
ATOM   11119 C  C   . ALA K  1 4   ? 65.138  54.729  19.070  1.00 49.64 ? 4   ALA K C   1 
ATOM   11120 O  O   . ALA K  1 4   ? 64.990  53.513  18.954  1.00 52.19 ? 4   ALA K O   1 
ATOM   11121 C  CB  . ALA K  1 4   ? 67.410  55.804  18.872  1.00 44.80 ? 4   ALA K CB  1 
ATOM   11122 N  N   . VAL K  1 5   ? 64.269  55.626  18.594  1.00 52.40 ? 5   VAL K N   1 
ATOM   11123 C  CA  . VAL K  1 5   ? 63.128  55.256  17.755  1.00 49.95 ? 5   VAL K CA  1 
ATOM   11124 C  C   . VAL K  1 5   ? 63.041  56.168  16.554  1.00 50.89 ? 5   VAL K C   1 
ATOM   11125 O  O   . VAL K  1 5   ? 63.597  57.273  16.546  1.00 46.50 ? 5   VAL K O   1 
ATOM   11126 C  CB  . VAL K  1 5   ? 61.756  55.402  18.455  1.00 49.89 ? 5   VAL K CB  1 
ATOM   11127 C  CG1 . VAL K  1 5   ? 60.731  54.433  17.840  1.00 52.13 ? 5   VAL K CG1 1 
ATOM   11128 C  CG2 . VAL K  1 5   ? 61.866  55.153  19.902  1.00 53.97 ? 5   VAL K CG2 1 
ATOM   11129 N  N   . CYS K  1 6   ? 62.308  55.689  15.554  1.00 50.28 ? 6   CYS K N   1 
ATOM   11130 C  CA  . CYS K  1 6   ? 61.972  56.460  14.377  1.00 52.07 ? 6   CYS K CA  1 
ATOM   11131 C  C   . CYS K  1 6   ? 60.545  56.101  13.977  1.00 51.38 ? 6   CYS K C   1 
ATOM   11132 O  O   . CYS K  1 6   ? 60.198  54.926  13.853  1.00 46.78 ? 6   CYS K O   1 
ATOM   11133 C  CB  . CYS K  1 6   ? 62.945  56.144  13.244  1.00 45.38 ? 6   CYS K CB  1 
ATOM   11134 S  SG  . CYS K  1 6   ? 62.739  57.189  11.787  1.00 56.17 ? 6   CYS K SG  1 
ATOM   11135 N  N   . VAL K  1 7   ? 59.706  57.113  13.814  1.00 54.08 ? 7   VAL K N   1 
ATOM   11136 C  CA  . VAL K  1 7   ? 58.364  56.875  13.314  1.00 54.48 ? 7   VAL K CA  1 
ATOM   11137 C  C   . VAL K  1 7   ? 58.288  57.310  11.862  1.00 56.36 ? 7   VAL K C   1 
ATOM   11138 O  O   . VAL K  1 7   ? 58.294  58.500  11.557  1.00 55.84 ? 7   VAL K O   1 
ATOM   11139 C  CB  . VAL K  1 7   ? 57.306  57.597  14.142  1.00 58.67 ? 7   VAL K CB  1 
ATOM   11140 C  CG1 . VAL K  1 7   ? 55.960  57.551  13.432  1.00 56.93 ? 7   VAL K CG1 1 
ATOM   11141 C  CG2 . VAL K  1 7   ? 57.209  56.960  15.528  1.00 63.62 ? 7   VAL K CG2 1 
ATOM   11142 N  N   . LEU K  1 8   ? 58.244  56.328  10.970  1.00 57.85 ? 8   LEU K N   1 
ATOM   11143 C  CA  . LEU K  1 8   ? 58.218  56.588  9.543   1.00 57.38 ? 8   LEU K CA  1 
ATOM   11144 C  C   . LEU K  1 8   ? 56.813  56.956  9.103   1.00 58.87 ? 8   LEU K C   1 
ATOM   11145 O  O   . LEU K  1 8   ? 55.858  56.253  9.429   1.00 61.17 ? 8   LEU K O   1 
ATOM   11146 C  CB  . LEU K  1 8   ? 58.689  55.359  8.771   1.00 56.46 ? 8   LEU K CB  1 
ATOM   11147 C  CG  . LEU K  1 8   ? 60.093  54.813  9.028   1.00 51.92 ? 8   LEU K CG  1 
ATOM   11148 C  CD1 . LEU K  1 8   ? 60.395  53.740  8.004   1.00 60.62 ? 8   LEU K CD1 1 
ATOM   11149 C  CD2 . LEU K  1 8   ? 61.134  55.909  8.960   1.00 52.06 ? 8   LEU K CD2 1 
ATOM   11150 N  N   . LYS K  1 9   ? 56.696  58.070  8.385   1.00 58.80 ? 9   LYS K N   1 
ATOM   11151 C  CA  . LYS K  1 9   ? 55.445  58.470  7.735   1.00 62.74 ? 9   LYS K CA  1 
ATOM   11152 C  C   . LYS K  1 9   ? 55.770  59.193  6.431   1.00 62.10 ? 9   LYS K C   1 
ATOM   11153 O  O   . LYS K  1 9   ? 56.783  59.884  6.329   1.00 62.75 ? 9   LYS K O   1 
ATOM   11154 C  CB  . LYS K  1 9   ? 54.602  59.396  8.622   1.00 58.84 ? 9   LYS K CB  1 
ATOM   11155 C  CG  . LYS K  1 9   ? 54.144  58.821  9.963   1.00 67.16 ? 9   LYS K CG  1 
ATOM   11156 C  CD  . LYS K  1 9   ? 53.121  57.699  9.805   1.00 66.81 ? 9   LYS K CD  1 
ATOM   11157 C  CE  . LYS K  1 9   ? 51.927  58.123  8.968   1.00 62.29 ? 9   LYS K CE  1 
ATOM   11158 N  NZ  . LYS K  1 9   ? 50.942  57.014  8.852   1.00 63.78 ? 9   LYS K NZ  1 
ATOM   11159 N  N   . GLY K  1 10  ? 54.910  59.028  5.435   1.00 66.49 ? 10  GLY K N   1 
ATOM   11160 C  CA  . GLY K  1 10  ? 55.045  59.755  4.187   1.00 64.75 ? 10  GLY K CA  1 
ATOM   11161 C  C   . GLY K  1 10  ? 53.723  60.380  3.786   1.00 65.76 ? 10  GLY K C   1 
ATOM   11162 O  O   . GLY K  1 10  ? 52.771  60.404  4.570   1.00 65.39 ? 10  GLY K O   1 
ATOM   11163 N  N   . ASP K  1 11  ? 53.660  60.889  2.561   1.00 66.16 ? 11  ASP K N   1 
ATOM   11164 C  CA  . ASP K  1 11  ? 52.423  61.457  2.034   1.00 71.27 ? 11  ASP K CA  1 
ATOM   11165 C  C   . ASP K  1 11  ? 51.550  60.374  1.411   1.00 71.51 ? 11  ASP K C   1 
ATOM   11166 O  O   . ASP K  1 11  ? 50.812  60.634  0.463   1.00 76.38 ? 11  ASP K O   1 
ATOM   11167 C  CB  . ASP K  1 11  ? 52.721  62.563  1.014   1.00 70.19 ? 11  ASP K CB  1 
ATOM   11168 C  CG  . ASP K  1 11  ? 53.980  62.289  0.201   1.00 79.64 ? 11  ASP K CG  1 
ATOM   11169 O  OD1 . ASP K  1 11  ? 53.910  61.467  -0.739  1.00 79.16 ? 11  ASP K OD1 1 
ATOM   11170 O  OD2 . ASP K  1 11  ? 55.038  62.895  0.502   1.00 76.22 ? 11  ASP K OD2 1 
ATOM   11171 N  N   . GLY K  1 12  ? 51.638  59.162  1.951   1.00 66.73 ? 12  GLY K N   1 
ATOM   11172 C  CA  . GLY K  1 12  ? 50.876  58.038  1.443   1.00 68.93 ? 12  GLY K CA  1 
ATOM   11173 C  C   . GLY K  1 12  ? 50.573  56.989  2.496   1.00 70.26 ? 12  GLY K C   1 
ATOM   11174 O  O   . GLY K  1 12  ? 50.481  57.303  3.683   1.00 70.86 ? 12  GLY K O   1 
ATOM   11175 N  N   . PRO K  1 13  ? 50.417  55.729  2.062   1.00 71.90 ? 13  PRO K N   1 
ATOM   11176 C  CA  . PRO K  1 13  ? 50.031  54.601  2.919   1.00 74.79 ? 13  PRO K CA  1 
ATOM   11177 C  C   . PRO K  1 13  ? 51.189  54.001  3.725   1.00 71.20 ? 13  PRO K C   1 
ATOM   11178 O  O   . PRO K  1 13  ? 50.949  53.218  4.648   1.00 67.09 ? 13  PRO K O   1 
ATOM   11179 C  CB  . PRO K  1 13  ? 49.519  53.572  1.909   1.00 69.80 ? 13  PRO K CB  1 
ATOM   11180 C  CG  . PRO K  1 13  ? 50.338  53.833  0.695   1.00 67.80 ? 13  PRO K CG  1 
ATOM   11181 C  CD  . PRO K  1 13  ? 50.540  55.326  0.649   1.00 65.81 ? 13  PRO K CD  1 
ATOM   11182 N  N   . VAL K  1 14  ? 52.422  54.354  3.379   1.00 68.72 ? 14  VAL K N   1 
ATOM   11183 C  CA  . VAL K  1 14  ? 53.583  53.771  4.039   1.00 68.04 ? 14  VAL K CA  1 
ATOM   11184 C  C   . VAL K  1 14  ? 53.809  54.383  5.423   1.00 67.94 ? 14  VAL K C   1 
ATOM   11185 O  O   . VAL K  1 14  ? 53.811  55.604  5.575   1.00 70.65 ? 14  VAL K O   1 
ATOM   11186 C  CB  . VAL K  1 14  ? 54.844  53.927  3.181   1.00 66.44 ? 14  VAL K CB  1 
ATOM   11187 C  CG1 . VAL K  1 14  ? 56.000  53.177  3.811   1.00 67.87 ? 14  VAL K CG1 1 
ATOM   11188 C  CG2 . VAL K  1 14  ? 54.580  53.425  1.769   1.00 67.13 ? 14  VAL K CG2 1 
ATOM   11189 N  N   . GLN K  1 15  ? 53.996  53.526  6.424   1.00 65.13 ? 15  GLN K N   1 
ATOM   11190 C  CA  . GLN K  1 15  ? 54.128  53.966  7.811   1.00 64.61 ? 15  GLN K CA  1 
ATOM   11191 C  C   . GLN K  1 15  ? 54.571  52.832  8.748   1.00 67.15 ? 15  GLN K C   1 
ATOM   11192 O  O   . GLN K  1 15  ? 54.407  51.655  8.426   1.00 66.92 ? 15  GLN K O   1 
ATOM   11193 C  CB  . GLN K  1 15  ? 52.808  54.582  8.296   1.00 67.90 ? 15  GLN K CB  1 
ATOM   11194 C  CG  . GLN K  1 15  ? 51.976  53.732  9.255   1.00 66.92 ? 15  GLN K CG  1 
ATOM   11195 C  CD  . GLN K  1 15  ? 51.000  52.807  8.551   1.00 70.06 ? 15  GLN K CD  1 
ATOM   11196 O  OE1 . GLN K  1 15  ? 51.160  52.494  7.370   1.00 71.59 ? 15  GLN K OE1 1 
ATOM   11197 N  NE2 . GLN K  1 15  ? 49.975  52.366  9.279   1.00 71.57 ? 15  GLN K NE2 1 
ATOM   11198 N  N   . GLY K  1 16  ? 55.140  53.186  9.900   1.00 65.55 ? 16  GLY K N   1 
ATOM   11199 C  CA  . GLY K  1 16  ? 55.522  52.191  10.889  1.00 62.37 ? 16  GLY K CA  1 
ATOM   11200 C  C   . GLY K  1 16  ? 56.491  52.689  11.942  1.00 61.01 ? 16  GLY K C   1 
ATOM   11201 O  O   . GLY K  1 16  ? 56.694  53.892  12.089  1.00 63.71 ? 16  GLY K O   1 
ATOM   11202 N  N   . ILE K  1 17  ? 57.090  51.754  12.676  1.00 61.13 ? 17  ILE K N   1 
ATOM   11203 C  CA  . ILE K  1 17  ? 58.026  52.084  13.751  1.00 60.94 ? 17  ILE K CA  1 
ATOM   11204 C  C   . ILE K  1 17  ? 59.280  51.203  13.728  1.00 60.81 ? 17  ILE K C   1 
ATOM   11205 O  O   . ILE K  1 17  ? 59.188  49.974  13.665  1.00 64.22 ? 17  ILE K O   1 
ATOM   11206 C  CB  . ILE K  1 17  ? 57.371  51.962  15.158  1.00 61.15 ? 17  ILE K CB  1 
ATOM   11207 C  CG1 . ILE K  1 17  ? 56.010  51.257  15.074  1.00 65.06 ? 17  ILE K CG1 1 
ATOM   11208 C  CG2 . ILE K  1 17  ? 57.243  53.334  15.816  1.00 59.06 ? 17  ILE K CG2 1 
ATOM   11209 C  CD1 . ILE K  1 17  ? 55.443  50.816  16.424  1.00 55.74 ? 17  ILE K CD1 1 
ATOM   11210 N  N   . ILE K  1 18  ? 60.448  51.837  13.796  1.00 56.92 ? 18  ILE K N   1 
ATOM   11211 C  CA  . ILE K  1 18  ? 61.722  51.113  13.849  1.00 58.43 ? 18  ILE K CA  1 
ATOM   11212 C  C   . ILE K  1 18  ? 62.538  51.480  15.089  1.00 57.24 ? 18  ILE K C   1 
ATOM   11213 O  O   . ILE K  1 18  ? 62.671  52.655  15.437  1.00 54.49 ? 18  ILE K O   1 
ATOM   11214 C  CB  . ILE K  1 18  ? 62.551  51.345  12.572  1.00 54.30 ? 18  ILE K CB  1 
ATOM   11215 C  CG1 . ILE K  1 18  ? 61.854  50.687  11.393  1.00 55.84 ? 18  ILE K CG1 1 
ATOM   11216 C  CG2 . ILE K  1 18  ? 63.948  50.778  12.717  1.00 54.34 ? 18  ILE K CG2 1 
ATOM   11217 C  CD1 . ILE K  1 18  ? 61.883  51.518  10.185  1.00 60.56 ? 18  ILE K CD1 1 
ATOM   11218 N  N   . ASN K  1 19  ? 63.078  50.463  15.751  1.00 56.97 ? 19  ASN K N   1 
ATOM   11219 C  CA  . ASN K  1 19  ? 63.758  50.649  17.020  1.00 51.94 ? 19  ASN K CA  1 
ATOM   11220 C  C   . ASN K  1 19  ? 65.258  50.399  16.919  1.00 52.96 ? 19  ASN K C   1 
ATOM   11221 O  O   . ASN K  1 19  ? 65.718  49.592  16.113  1.00 53.76 ? 19  ASN K O   1 
ATOM   11222 C  CB  . ASN K  1 19  ? 63.127  49.747  18.081  1.00 52.13 ? 19  ASN K CB  1 
ATOM   11223 C  CG  . ASN K  1 19  ? 61.645  50.001  18.244  1.00 55.45 ? 19  ASN K CG  1 
ATOM   11224 O  OD1 . ASN K  1 19  ? 61.235  50.792  19.089  1.00 58.30 ? 19  ASN K OD1 1 
ATOM   11225 N  ND2 . ASN K  1 19  ? 60.831  49.343  17.423  1.00 57.60 ? 19  ASN K ND2 1 
ATOM   11226 N  N   . PHE K  1 20  ? 66.020  51.109  17.736  1.00 51.24 ? 20  PHE K N   1 
ATOM   11227 C  CA  . PHE K  1 20  ? 67.469  50.974  17.739  1.00 52.12 ? 20  PHE K CA  1 
ATOM   11228 C  C   . PHE K  1 20  ? 67.923  50.712  19.169  1.00 51.56 ? 20  PHE K C   1 
ATOM   11229 O  O   . PHE K  1 20  ? 67.631  51.495  20.073  1.00 46.97 ? 20  PHE K O   1 
ATOM   11230 C  CB  . PHE K  1 20  ? 68.138  52.242  17.195  1.00 51.26 ? 20  PHE K CB  1 
ATOM   11231 C  CG  . PHE K  1 20  ? 67.729  52.597  15.787  1.00 54.05 ? 20  PHE K CG  1 
ATOM   11232 C  CD1 . PHE K  1 20  ? 66.482  53.148  15.523  1.00 54.21 ? 20  PHE K CD1 1 
ATOM   11233 C  CD2 . PHE K  1 20  ? 68.599  52.395  14.729  1.00 51.94 ? 20  PHE K CD2 1 
ATOM   11234 C  CE1 . PHE K  1 20  ? 66.106  53.472  14.231  1.00 53.34 ? 20  PHE K CE1 1 
ATOM   11235 C  CE2 . PHE K  1 20  ? 68.230  52.719  13.443  1.00 48.40 ? 20  PHE K CE2 1 
ATOM   11236 C  CZ  . PHE K  1 20  ? 66.985  53.263  13.193  1.00 49.16 ? 20  PHE K CZ  1 
ATOM   11237 N  N   . GLU K  1 21  ? 68.613  49.596  19.377  1.00 54.90 ? 21  GLU K N   1 
ATOM   11238 C  CA  . GLU K  1 21  ? 69.157  49.277  20.693  1.00 55.49 ? 21  GLU K CA  1 
ATOM   11239 C  C   . GLU K  1 21  ? 70.653  48.984  20.575  1.00 51.79 ? 21  GLU K C   1 
ATOM   11240 O  O   . GLU K  1 21  ? 71.074  48.248  19.688  1.00 56.25 ? 21  GLU K O   1 
ATOM   11241 C  CB  . GLU K  1 21  ? 68.401  48.105  21.329  1.00 50.45 ? 21  GLU K CB  1 
ATOM   11242 C  CG  . GLU K  1 21  ? 68.803  47.828  22.772  1.00 52.43 ? 21  GLU K CG  1 
ATOM   11243 C  CD  . GLU K  1 21  ? 67.898  46.813  23.453  1.00 55.73 ? 21  GLU K CD  1 
ATOM   11244 O  OE1 . GLU K  1 21  ? 68.357  46.134  24.400  1.00 61.76 ? 21  GLU K OE1 1 
ATOM   11245 O  OE2 . GLU K  1 21  ? 66.724  46.700  23.046  1.00 48.42 ? 21  GLU K OE2 1 
ATOM   11246 N  N   . GLN K  1 22  ? 71.454  49.586  21.449  1.00 45.03 ? 22  GLN K N   1 
ATOM   11247 C  CA  . GLN K  1 22  ? 72.903  49.434  21.392  1.00 44.08 ? 22  GLN K CA  1 
ATOM   11248 C  C   . GLN K  1 22  ? 73.460  49.336  22.809  1.00 49.90 ? 22  GLN K C   1 
ATOM   11249 O  O   . GLN K  1 22  ? 73.868  50.337  23.411  1.00 48.29 ? 22  GLN K O   1 
ATOM   11250 C  CB  . GLN K  1 22  ? 73.545  50.595  20.623  1.00 41.69 ? 22  GLN K CB  1 
ATOM   11251 C  CG  . GLN K  1 22  ? 74.952  50.315  20.129  1.00 42.27 ? 22  GLN K CG  1 
ATOM   11252 C  CD  . GLN K  1 22  ? 75.683  51.570  19.700  1.00 45.99 ? 22  GLN K CD  1 
ATOM   11253 O  OE1 . GLN K  1 22  ? 75.087  52.633  19.603  1.00 42.37 ? 22  GLN K OE1 1 
ATOM   11254 N  NE2 . GLN K  1 22  ? 76.987  51.454  19.457  1.00 45.42 ? 22  GLN K NE2 1 
ATOM   11255 N  N   . LYS K  1 23  ? 73.471  48.113  23.333  1.00 56.11 ? 23  LYS K N   1 
ATOM   11256 C  CA  . LYS K  1 23  ? 73.806  47.866  24.735  1.00 53.95 ? 23  LYS K CA  1 
ATOM   11257 C  C   . LYS K  1 23  ? 75.279  48.097  25.067  1.00 47.49 ? 23  LYS K C   1 
ATOM   11258 O  O   . LYS K  1 23  ? 75.662  48.026  26.225  1.00 54.32 ? 23  LYS K O   1 
ATOM   11259 C  CB  . LYS K  1 23  ? 73.356  46.460  25.163  1.00 56.52 ? 23  LYS K CB  1 
ATOM   11260 C  CG  . LYS K  1 23  ? 71.855  46.356  25.480  1.00 59.08 ? 23  LYS K CG  1 
ATOM   11261 C  CD  . LYS K  1 23  ? 71.394  44.909  25.664  1.00 65.07 ? 23  LYS K CD  1 
ATOM   11262 C  CE  . LYS K  1 23  ? 71.152  44.216  24.318  1.00 68.05 ? 23  LYS K CE  1 
ATOM   11263 N  NZ  . LYS K  1 23  ? 70.653  42.813  24.469  1.00 62.06 ? 23  LYS K NZ  1 
ATOM   11264 N  N   . GLU K  1 24  ? 76.099  48.370  24.057  1.00 42.93 ? 24  GLU K N   1 
ATOM   11265 C  CA  . GLU K  1 24  ? 77.478  48.796  24.282  1.00 45.78 ? 24  GLU K CA  1 
ATOM   11266 C  C   . GLU K  1 24  ? 77.848  49.875  23.266  1.00 50.41 ? 24  GLU K C   1 
ATOM   11267 O  O   . GLU K  1 24  ? 77.455  49.800  22.100  1.00 51.82 ? 24  GLU K O   1 
ATOM   11268 C  CB  . GLU K  1 24  ? 78.465  47.622  24.156  1.00 54.74 ? 24  GLU K CB  1 
ATOM   11269 C  CG  . GLU K  1 24  ? 78.009  46.286  24.768  1.00 53.26 ? 24  GLU K CG  1 
ATOM   11270 C  CD  . GLU K  1 24  ? 78.090  46.258  26.286  1.00 53.36 ? 24  GLU K CD  1 
ATOM   11271 O  OE1 . GLU K  1 24  ? 78.904  47.015  26.859  1.00 51.06 ? 24  GLU K OE1 1 
ATOM   11272 O  OE2 . GLU K  1 24  ? 77.332  45.478  26.906  1.00 58.87 ? 24  GLU K OE2 1 
ATOM   11273 N  N   . SER K  1 25  ? 78.617  50.865  23.709  1.00 48.71 ? 25  SER K N   1 
ATOM   11274 C  CA  . SER K  1 25  ? 79.019  51.980  22.856  1.00 48.46 ? 25  SER K CA  1 
ATOM   11275 C  C   . SER K  1 25  ? 79.791  51.534  21.610  1.00 54.46 ? 25  SER K C   1 
ATOM   11276 O  O   . SER K  1 25  ? 79.665  52.136  20.538  1.00 54.24 ? 25  SER K O   1 
ATOM   11277 C  CB  . SER K  1 25  ? 79.874  52.967  23.651  1.00 44.23 ? 25  SER K CB  1 
ATOM   11278 O  OG  . SER K  1 25  ? 81.253  52.821  23.345  1.00 43.65 ? 25  SER K OG  1 
ATOM   11279 N  N   . ASN K  1 26  ? 80.591  50.482  21.756  1.00 54.25 ? 26  ASN K N   1 
ATOM   11280 C  CA  . ASN K  1 26  ? 81.464  50.032  20.678  1.00 50.19 ? 26  ASN K CA  1 
ATOM   11281 C  C   . ASN K  1 26  ? 80.953  48.760  20.022  1.00 46.50 ? 26  ASN K C   1 
ATOM   11282 O  O   . ASN K  1 26  ? 81.626  48.166  19.185  1.00 44.55 ? 26  ASN K O   1 
ATOM   11283 C  CB  . ASN K  1 26  ? 82.887  49.824  21.197  1.00 48.57 ? 26  ASN K CB  1 
ATOM   11284 C  CG  . ASN K  1 26  ? 82.992  48.666  22.171  1.00 49.72 ? 26  ASN K CG  1 
ATOM   11285 O  OD1 . ASN K  1 26  ? 81.976  48.149  22.660  1.00 44.87 ? 26  ASN K OD1 1 
ATOM   11286 N  ND2 . ASN K  1 26  ? 84.226  48.255  22.468  1.00 45.35 ? 26  ASN K ND2 1 
ATOM   11287 N  N   . GLY K  1 27  ? 79.761  48.340  20.420  1.00 47.72 ? 27  GLY K N   1 
ATOM   11288 C  CA  . GLY K  1 27  ? 79.162  47.146  19.867  1.00 48.60 ? 27  GLY K CA  1 
ATOM   11289 C  C   . GLY K  1 27  ? 78.265  47.481  18.693  1.00 55.03 ? 27  GLY K C   1 
ATOM   11290 O  O   . GLY K  1 27  ? 78.144  48.646  18.309  1.00 53.40 ? 27  GLY K O   1 
ATOM   11291 N  N   . PRO K  1 28  ? 77.633  46.458  18.107  1.00 53.48 ? 28  PRO K N   1 
ATOM   11292 C  CA  . PRO K  1 28  ? 76.755  46.699  16.964  1.00 53.48 ? 28  PRO K CA  1 
ATOM   11293 C  C   . PRO K  1 28  ? 75.396  47.214  17.415  1.00 52.83 ? 28  PRO K C   1 
ATOM   11294 O  O   . PRO K  1 28  ? 75.011  47.043  18.578  1.00 53.42 ? 28  PRO K O   1 
ATOM   11295 C  CB  . PRO K  1 28  ? 76.618  45.308  16.341  1.00 57.31 ? 28  PRO K CB  1 
ATOM   11296 C  CG  . PRO K  1 28  ? 76.744  44.380  17.499  1.00 53.69 ? 28  PRO K CG  1 
ATOM   11297 C  CD  . PRO K  1 28  ? 77.757  45.022  18.416  1.00 53.05 ? 28  PRO K CD  1 
ATOM   11298 N  N   . VAL K  1 29  ? 74.678  47.843  16.491  1.00 51.45 ? 29  VAL K N   1 
ATOM   11299 C  CA  . VAL K  1 29  ? 73.333  48.333  16.761  1.00 55.93 ? 29  VAL K CA  1 
ATOM   11300 C  C   . VAL K  1 29  ? 72.303  47.286  16.350  1.00 58.96 ? 29  VAL K C   1 
ATOM   11301 O  O   . VAL K  1 29  ? 72.354  46.749  15.237  1.00 58.66 ? 29  VAL K O   1 
ATOM   11302 C  CB  . VAL K  1 29  ? 73.032  49.653  16.001  1.00 50.54 ? 29  VAL K CB  1 
ATOM   11303 C  CG1 . VAL K  1 29  ? 71.666  50.185  16.394  1.00 51.01 ? 29  VAL K CG1 1 
ATOM   11304 C  CG2 . VAL K  1 29  ? 74.103  50.696  16.275  1.00 48.68 ? 29  VAL K CG2 1 
ATOM   11305 N  N   . LYS K  1 30  ? 71.377  46.986  17.252  1.00 54.93 ? 30  LYS K N   1 
ATOM   11306 C  CA  . LYS K  1 30  ? 70.238  46.161  16.887  1.00 57.12 ? 30  LYS K CA  1 
ATOM   11307 C  C   . LYS K  1 30  ? 69.142  47.059  16.328  1.00 58.93 ? 30  LYS K C   1 
ATOM   11308 O  O   . LYS K  1 30  ? 68.875  48.136  16.870  1.00 55.07 ? 30  LYS K O   1 
ATOM   11309 C  CB  . LYS K  1 30  ? 69.748  45.347  18.082  1.00 49.32 ? 30  LYS K CB  1 
ATOM   11310 C  CG  . LYS K  1 30  ? 70.736  44.276  18.499  1.00 54.01 ? 30  LYS K CG  1 
ATOM   11311 C  CD  . LYS K  1 30  ? 70.464  43.769  19.907  1.00 60.38 ? 30  LYS K CD  1 
ATOM   11312 C  CE  . LYS K  1 30  ? 71.484  42.715  20.327  1.00 56.70 ? 30  LYS K CE  1 
ATOM   11313 N  NZ  . LYS K  1 30  ? 71.145  42.114  21.652  1.00 62.30 ? 30  LYS K NZ  1 
ATOM   11314 N  N   . VAL K  1 31  ? 68.540  46.619  15.225  1.00 59.78 ? 31  VAL K N   1 
ATOM   11315 C  CA  . VAL K  1 31  ? 67.500  47.372  14.526  1.00 58.01 ? 31  VAL K CA  1 
ATOM   11316 C  C   . VAL K  1 31  ? 66.322  46.454  14.202  1.00 58.39 ? 31  VAL K C   1 
ATOM   11317 O  O   . VAL K  1 31  ? 66.505  45.413  13.570  1.00 61.13 ? 31  VAL K O   1 
ATOM   11318 C  CB  . VAL K  1 31  ? 68.033  47.966  13.194  1.00 57.04 ? 31  VAL K CB  1 
ATOM   11319 C  CG1 . VAL K  1 31  ? 67.021  48.942  12.597  1.00 54.55 ? 31  VAL K CG1 1 
ATOM   11320 C  CG2 . VAL K  1 31  ? 69.383  48.647  13.395  1.00 53.37 ? 31  VAL K CG2 1 
ATOM   11321 N  N   . TRP K  1 32  ? 65.118  46.839  14.619  1.00 56.65 ? 32  TRP K N   1 
ATOM   11322 C  CA  . TRP K  1 32  ? 63.935  46.005  14.399  1.00 58.13 ? 32  TRP K CA  1 
ATOM   11323 C  C   . TRP K  1 32  ? 62.632  46.805  14.453  1.00 61.51 ? 32  TRP K C   1 
ATOM   11324 O  O   . TRP K  1 32  ? 62.592  47.922  14.973  1.00 60.73 ? 32  TRP K O   1 
ATOM   11325 C  CB  . TRP K  1 32  ? 63.874  44.873  15.427  1.00 55.51 ? 32  TRP K CB  1 
ATOM   11326 C  CG  . TRP K  1 32  ? 63.328  45.315  16.733  1.00 53.69 ? 32  TRP K CG  1 
ATOM   11327 C  CD1 . TRP K  1 32  ? 62.038  45.196  17.170  1.00 57.28 ? 32  TRP K CD1 1 
ATOM   11328 C  CD2 . TRP K  1 32  ? 64.050  45.970  17.779  1.00 58.02 ? 32  TRP K CD2 1 
ATOM   11329 N  NE1 . TRP K  1 32  ? 61.915  45.733  18.431  1.00 56.89 ? 32  TRP K NE1 1 
ATOM   11330 C  CE2 . TRP K  1 32  ? 63.136  46.215  18.827  1.00 57.41 ? 32  TRP K CE2 1 
ATOM   11331 C  CE3 . TRP K  1 32  ? 65.382  46.369  17.936  1.00 54.60 ? 32  TRP K CE3 1 
ATOM   11332 C  CZ2 . TRP K  1 32  ? 63.513  46.841  20.015  1.00 62.45 ? 32  TRP K CZ2 1 
ATOM   11333 C  CZ3 . TRP K  1 32  ? 65.756  46.994  19.115  1.00 56.16 ? 32  TRP K CZ3 1 
ATOM   11334 C  CH2 . TRP K  1 32  ? 64.826  47.223  20.139  1.00 60.57 ? 32  TRP K CH2 1 
ATOM   11335 N  N   . GLY K  1 33  ? 61.562  46.211  13.931  1.00 64.20 ? 33  GLY K N   1 
ATOM   11336 C  CA  . GLY K  1 33  ? 60.274  46.879  13.841  1.00 64.28 ? 33  GLY K CA  1 
ATOM   11337 C  C   . GLY K  1 33  ? 59.492  46.398  12.630  1.00 64.13 ? 33  GLY K C   1 
ATOM   11338 O  O   . GLY K  1 33  ? 59.833  45.375  12.029  1.00 60.33 ? 33  GLY K O   1 
ATOM   11339 N  N   . SER K  1 34  ? 58.438  47.127  12.274  1.00 62.59 ? 34  SER K N   1 
ATOM   11340 C  CA  . SER K  1 34  ? 57.602  46.744  11.138  1.00 67.37 ? 34  SER K CA  1 
ATOM   11341 C  C   . SER K  1 34  ? 56.989  47.950  10.427  1.00 69.81 ? 34  SER K C   1 
ATOM   11342 O  O   . SER K  1 34  ? 56.509  48.892  11.068  1.00 68.19 ? 34  SER K O   1 
ATOM   11343 C  CB  . SER K  1 34  ? 56.515  45.737  11.553  1.00 66.00 ? 34  SER K CB  1 
ATOM   11344 O  OG  . SER K  1 34  ? 55.613  46.283  12.500  1.00 59.12 ? 34  SER K OG  1 
ATOM   11345 N  N   . ILE K  1 35  ? 57.013  47.905  9.097   1.00 66.08 ? 35  ILE K N   1 
ATOM   11346 C  CA  . ILE K  1 35  ? 56.534  49.003  8.263   1.00 67.83 ? 35  ILE K CA  1 
ATOM   11347 C  C   . ILE K  1 35  ? 55.469  48.514  7.269   1.00 70.19 ? 35  ILE K C   1 
ATOM   11348 O  O   . ILE K  1 35  ? 55.776  47.821  6.298   1.00 75.10 ? 35  ILE K O   1 
ATOM   11349 C  CB  . ILE K  1 35  ? 57.722  49.727  7.550   1.00 63.57 ? 35  ILE K CB  1 
ATOM   11350 C  CG1 . ILE K  1 35  ? 57.262  50.476  6.301   1.00 64.90 ? 35  ILE K CG1 1 
ATOM   11351 C  CG2 . ILE K  1 35  ? 58.832  48.748  7.197   1.00 62.75 ? 35  ILE K CG2 1 
ATOM   11352 C  CD1 . ILE K  1 35  ? 58.412  50.985  5.466   1.00 64.89 ? 35  ILE K CD1 1 
ATOM   11353 N  N   . LYS K  1 36  ? 54.213  48.866  7.532   1.00 71.36 ? 36  LYS K N   1 
ATOM   11354 C  CA  . LYS K  1 36  ? 53.088  48.396  6.722   1.00 70.29 ? 36  LYS K CA  1 
ATOM   11355 C  C   . LYS K  1 36  ? 52.697  49.392  5.625   1.00 69.26 ? 36  LYS K C   1 
ATOM   11356 O  O   . LYS K  1 36  ? 52.963  50.589  5.738   1.00 66.33 ? 36  LYS K O   1 
ATOM   11357 C  CB  . LYS K  1 36  ? 51.877  48.114  7.616   1.00 69.50 ? 36  LYS K CB  1 
ATOM   11358 C  CG  . LYS K  1 36  ? 51.063  49.354  7.962   1.00 69.58 ? 36  LYS K CG  1 
ATOM   11359 C  CD  . LYS K  1 36  ? 49.902  49.027  8.881   1.00 70.41 ? 36  LYS K CD  1 
ATOM   11360 C  CE  . LYS K  1 36  ? 50.392  48.665  10.266  1.00 67.74 ? 36  LYS K CE  1 
ATOM   11361 N  NZ  . LYS K  1 36  ? 49.286  48.124  11.099  1.00 73.05 ? 36  LYS K NZ  1 
ATOM   11362 N  N   . GLY K  1 37  ? 52.063  48.890  4.567   1.00 74.34 ? 37  GLY K N   1 
ATOM   11363 C  CA  . GLY K  1 37  ? 51.575  49.736  3.491   1.00 67.53 ? 37  GLY K CA  1 
ATOM   11364 C  C   . GLY K  1 37  ? 52.531  49.849  2.319   1.00 68.19 ? 37  GLY K C   1 
ATOM   11365 O  O   . GLY K  1 37  ? 52.520  50.842  1.590   1.00 69.24 ? 37  GLY K O   1 
ATOM   11366 N  N   . LEU K  1 38  ? 53.367  48.832  2.141   1.00 67.70 ? 38  LEU K N   1 
ATOM   11367 C  CA  . LEU K  1 38  ? 54.288  48.797  1.014   1.00 68.10 ? 38  LEU K CA  1 
ATOM   11368 C  C   . LEU K  1 38  ? 53.772  47.838  -0.049  1.00 74.93 ? 38  LEU K C   1 
ATOM   11369 O  O   . LEU K  1 38  ? 52.886  47.021  0.214   1.00 72.44 ? 38  LEU K O   1 
ATOM   11370 C  CB  . LEU K  1 38  ? 55.680  48.341  1.462   1.00 68.85 ? 38  LEU K CB  1 
ATOM   11371 C  CG  . LEU K  1 38  ? 56.573  49.280  2.277   1.00 65.31 ? 38  LEU K CG  1 
ATOM   11372 C  CD1 . LEU K  1 38  ? 57.888  48.602  2.604   1.00 65.45 ? 38  LEU K CD1 1 
ATOM   11373 C  CD2 . LEU K  1 38  ? 56.827  50.565  1.527   1.00 67.26 ? 38  LEU K CD2 1 
ATOM   11374 N  N   . THR K  1 39  ? 54.328  47.944  -1.252  1.00 75.41 ? 39  THR K N   1 
ATOM   11375 C  CA  . THR K  1 39  ? 54.112  46.938  -2.280  1.00 75.28 ? 39  THR K CA  1 
ATOM   11376 C  C   . THR K  1 39  ? 54.911  45.706  -1.871  1.00 78.33 ? 39  THR K C   1 
ATOM   11377 O  O   . THR K  1 39  ? 55.828  45.805  -1.051  1.00 77.34 ? 39  THR K O   1 
ATOM   11378 C  CB  . THR K  1 39  ? 54.573  47.429  -3.670  1.00 73.62 ? 39  THR K CB  1 
ATOM   11379 O  OG1 . THR K  1 39  ? 55.995  47.619  -3.671  1.00 69.14 ? 39  THR K OG1 1 
ATOM   11380 C  CG2 . THR K  1 39  ? 53.883  48.743  -4.028  1.00 71.44 ? 39  THR K CG2 1 
ATOM   11381 N  N   . GLU K  1 40  ? 54.563  44.550  -2.431  1.00 81.58 ? 40  GLU K N   1 
ATOM   11382 C  CA  . GLU K  1 40  ? 55.226  43.298  -2.065  1.00 80.89 ? 40  GLU K CA  1 
ATOM   11383 C  C   . GLU K  1 40  ? 56.684  43.263  -2.514  1.00 75.61 ? 40  GLU K C   1 
ATOM   11384 O  O   . GLU K  1 40  ? 56.998  43.587  -3.658  1.00 74.88 ? 40  GLU K O   1 
ATOM   11385 C  CB  . GLU K  1 40  ? 54.474  42.097  -2.647  1.00 81.51 ? 40  GLU K CB  1 
ATOM   11386 C  CG  . GLU K  1 40  ? 55.151  40.754  -2.388  1.00 81.60 ? 40  GLU K CG  1 
ATOM   11387 C  CD  . GLU K  1 40  ? 54.437  39.597  -3.070  1.00 85.09 ? 40  GLU K CD  1 
ATOM   11388 O  OE1 . GLU K  1 40  ? 53.208  39.699  -3.279  1.00 85.33 ? 40  GLU K OE1 1 
ATOM   11389 O  OE2 . GLU K  1 40  ? 55.106  38.590  -3.402  1.00 80.41 ? 40  GLU K OE2 1 
ATOM   11390 N  N   . GLY K  1 41  ? 57.572  42.877  -1.602  1.00 77.33 ? 41  GLY K N   1 
ATOM   11391 C  CA  . GLY K  1 41  ? 58.960  42.648  -1.953  1.00 75.34 ? 41  GLY K CA  1 
ATOM   11392 C  C   . GLY K  1 41  ? 59.965  43.591  -1.324  1.00 75.88 ? 41  GLY K C   1 
ATOM   11393 O  O   . GLY K  1 41  ? 59.779  44.065  -0.199  1.00 76.28 ? 41  GLY K O   1 
ATOM   11394 N  N   . LEU K  1 42  ? 61.040  43.849  -2.066  1.00 73.70 ? 42  LEU K N   1 
ATOM   11395 C  CA  . LEU K  1 42  ? 62.144  44.681  -1.601  1.00 73.09 ? 42  LEU K CA  1 
ATOM   11396 C  C   . LEU K  1 42  ? 61.813  46.158  -1.667  1.00 74.96 ? 42  LEU K C   1 
ATOM   11397 O  O   . LEU K  1 42  ? 61.212  46.637  -2.635  1.00 70.90 ? 42  LEU K O   1 
ATOM   11398 C  CB  . LEU K  1 42  ? 63.407  44.432  -2.427  1.00 66.22 ? 42  LEU K CB  1 
ATOM   11399 C  CG  . LEU K  1 42  ? 64.196  43.152  -2.175  1.00 69.83 ? 42  LEU K CG  1 
ATOM   11400 C  CD1 . LEU K  1 42  ? 65.483  43.159  -2.996  1.00 67.91 ? 42  LEU K CD1 1 
ATOM   11401 C  CD2 . LEU K  1 42  ? 64.493  43.000  -0.694  1.00 70.52 ? 42  LEU K CD2 1 
ATOM   11402 N  N   . HIS K  1 43  ? 62.225  46.871  -0.625  1.00 77.18 ? 43  HIS K N   1 
ATOM   11403 C  CA  . HIS K  1 43  ? 62.135  48.323  -0.585  1.00 72.54 ? 43  HIS K CA  1 
ATOM   11404 C  C   . HIS K  1 43  ? 63.422  48.911  0.005   1.00 71.31 ? 43  HIS K C   1 
ATOM   11405 O  O   . HIS K  1 43  ? 63.894  48.458  1.057   1.00 68.43 ? 43  HIS K O   1 
ATOM   11406 C  CB  . HIS K  1 43  ? 60.896  48.772  0.198   1.00 70.53 ? 43  HIS K CB  1 
ATOM   11407 C  CG  . HIS K  1 43  ? 59.607  48.538  -0.529  1.00 71.31 ? 43  HIS K CG  1 
ATOM   11408 N  ND1 . HIS K  1 43  ? 58.880  49.559  -1.103  1.00 70.21 ? 43  HIS K ND1 1 
ATOM   11409 C  CD2 . HIS K  1 43  ? 58.918  47.399  -0.781  1.00 72.66 ? 43  HIS K CD2 1 
ATOM   11410 C  CE1 . HIS K  1 43  ? 57.799  49.060  -1.676  1.00 72.04 ? 43  HIS K CE1 1 
ATOM   11411 N  NE2 . HIS K  1 43  ? 57.797  47.751  -1.494  1.00 73.14 ? 43  HIS K NE2 1 
ATOM   11412 N  N   . GLY K  1 44  ? 63.990  49.899  -0.691  1.00 70.14 ? 44  GLY K N   1 
ATOM   11413 C  CA  . GLY K  1 44  ? 65.205  50.582  -0.262  1.00 66.85 ? 44  GLY K CA  1 
ATOM   11414 C  C   . GLY K  1 44  ? 65.103  51.182  1.131   1.00 62.86 ? 44  GLY K C   1 
ATOM   11415 O  O   . GLY K  1 44  ? 64.019  51.567  1.573   1.00 60.93 ? 44  GLY K O   1 
ATOM   11416 N  N   . PHE K  1 45  ? 66.236  51.273  1.819   1.00 60.84 ? 45  PHE K N   1 
ATOM   11417 C  CA  . PHE K  1 45  ? 66.222  51.547  3.254   1.00 63.05 ? 45  PHE K CA  1 
ATOM   11418 C  C   . PHE K  1 45  ? 67.515  52.210  3.724   1.00 60.22 ? 45  PHE K C   1 
ATOM   11419 O  O   . PHE K  1 45  ? 68.534  51.543  3.913   1.00 59.11 ? 45  PHE K O   1 
ATOM   11420 C  CB  . PHE K  1 45  ? 66.002  50.238  4.006   1.00 61.58 ? 45  PHE K CB  1 
ATOM   11421 C  CG  . PHE K  1 45  ? 65.311  50.404  5.313   1.00 60.25 ? 45  PHE K CG  1 
ATOM   11422 C  CD1 . PHE K  1 45  ? 64.020  50.878  5.370   1.00 60.70 ? 45  PHE K CD1 1 
ATOM   11423 C  CD2 . PHE K  1 45  ? 65.944  50.065  6.484   1.00 59.72 ? 45  PHE K CD2 1 
ATOM   11424 C  CE1 . PHE K  1 45  ? 63.382  51.023  6.581   1.00 62.74 ? 45  PHE K CE1 1 
ATOM   11425 C  CE2 . PHE K  1 45  ? 65.319  50.207  7.696   1.00 60.30 ? 45  PHE K CE2 1 
ATOM   11426 C  CZ  . PHE K  1 45  ? 64.036  50.685  7.746   1.00 62.73 ? 45  PHE K CZ  1 
ATOM   11427 N  N   . HIS K  1 46  ? 67.469  53.526  3.916   1.00 59.36 ? 46  HIS K N   1 
ATOM   11428 C  CA  . HIS K  1 46  ? 68.683  54.291  4.189   1.00 57.45 ? 46  HIS K CA  1 
ATOM   11429 C  C   . HIS K  1 46  ? 68.565  55.265  5.356   1.00 54.68 ? 46  HIS K C   1 
ATOM   11430 O  O   . HIS K  1 46  ? 67.474  55.671  5.767   1.00 51.42 ? 46  HIS K O   1 
ATOM   11431 C  CB  . HIS K  1 46  ? 69.126  55.060  2.937   1.00 53.40 ? 46  HIS K CB  1 
ATOM   11432 C  CG  . HIS K  1 46  ? 69.260  54.199  1.723   1.00 59.93 ? 46  HIS K CG  1 
ATOM   11433 N  ND1 . HIS K  1 46  ? 68.577  54.452  0.552   1.00 58.18 ? 46  HIS K ND1 1 
ATOM   11434 C  CD2 . HIS K  1 46  ? 69.983  53.075  1.502   1.00 57.26 ? 46  HIS K CD2 1 
ATOM   11435 C  CE1 . HIS K  1 46  ? 68.880  53.525  -0.338  1.00 61.32 ? 46  HIS K CE1 1 
ATOM   11436 N  NE2 . HIS K  1 46  ? 69.732  52.678  0.213   1.00 61.39 ? 46  HIS K NE2 1 
ATOM   11437 N  N   . VAL K  1 47  ? 69.723  55.630  5.883   1.00 52.36 ? 47  VAL K N   1 
ATOM   11438 C  CA  . VAL K  1 47  ? 69.822  56.761  6.770   1.00 48.89 ? 47  VAL K CA  1 
ATOM   11439 C  C   . VAL K  1 47  ? 70.337  57.919  5.938   1.00 47.15 ? 47  VAL K C   1 
ATOM   11440 O  O   . VAL K  1 47  ? 71.486  57.901  5.478   1.00 46.19 ? 47  VAL K O   1 
ATOM   11441 C  CB  . VAL K  1 47  ? 70.771  56.485  7.946   1.00 48.14 ? 47  VAL K CB  1 
ATOM   11442 C  CG1 . VAL K  1 47  ? 71.119  57.775  8.664   1.00 44.24 ? 47  VAL K CG1 1 
ATOM   11443 C  CG2 . VAL K  1 47  ? 70.131  55.493  8.902   1.00 46.09 ? 47  VAL K CG2 1 
ATOM   11444 N  N   . HIS K  1 48  ? 69.465  58.904  5.721   1.00 46.46 ? 48  HIS K N   1 
ATOM   11445 C  CA  . HIS K  1 48  ? 69.839  60.130  5.026   1.00 42.52 ? 48  HIS K CA  1 
ATOM   11446 C  C   . HIS K  1 48  ? 70.405  61.144  6.013   1.00 39.71 ? 48  HIS K C   1 
ATOM   11447 O  O   . HIS K  1 48  ? 70.094  61.098  7.200   1.00 41.35 ? 48  HIS K O   1 
ATOM   11448 C  CB  . HIS K  1 48  ? 68.653  60.714  4.254   1.00 46.71 ? 48  HIS K CB  1 
ATOM   11449 C  CG  . HIS K  1 48  ? 68.432  60.085  2.911   1.00 53.65 ? 48  HIS K CG  1 
ATOM   11450 N  ND1 . HIS K  1 48  ? 69.020  60.563  1.757   1.00 50.44 ? 48  HIS K ND1 1 
ATOM   11451 C  CD2 . HIS K  1 48  ? 67.689  59.016  2.537   1.00 51.16 ? 48  HIS K CD2 1 
ATOM   11452 C  CE1 . HIS K  1 48  ? 68.642  59.819  0.732   1.00 49.10 ? 48  HIS K CE1 1 
ATOM   11453 N  NE2 . HIS K  1 48  ? 67.830  58.876  1.178   1.00 51.67 ? 48  HIS K NE2 1 
ATOM   11454 N  N   . GLU K  1 49  ? 71.227  62.056  5.504   1.00 36.47 ? 49  GLU K N   1 
ATOM   11455 C  CA  . GLU K  1 49  ? 72.091  62.894  6.323   1.00 35.11 ? 49  GLU K CA  1 
ATOM   11456 C  C   . GLU K  1 49  ? 71.372  63.858  7.274   1.00 41.77 ? 49  GLU K C   1 
ATOM   11457 O  O   . GLU K  1 49  ? 71.858  64.121  8.383   1.00 35.11 ? 49  GLU K O   1 
ATOM   11458 C  CB  . GLU K  1 49  ? 73.047  63.679  5.432   1.00 37.80 ? 49  GLU K CB  1 
ATOM   11459 C  CG  . GLU K  1 49  ? 73.991  64.573  6.196   1.00 36.16 ? 49  GLU K CG  1 
ATOM   11460 C  CD  . GLU K  1 49  ? 74.961  65.302  5.300   1.00 42.26 ? 49  GLU K CD  1 
ATOM   11461 O  OE1 . GLU K  1 49  ? 74.822  65.194  4.058   1.00 43.40 ? 49  GLU K OE1 1 
ATOM   11462 O  OE2 . GLU K  1 49  ? 75.863  65.984  5.839   1.00 43.79 ? 49  GLU K OE2 1 
ATOM   11463 N  N   . PHE K  1 50  ? 70.219  64.375  6.850   1.00 39.54 ? 50  PHE K N   1 
ATOM   11464 C  CA  . PHE K  1 50  ? 69.555  65.435  7.598   1.00 35.62 ? 50  PHE K CA  1 
ATOM   11465 C  C   . PHE K  1 50  ? 68.187  65.046  8.136   1.00 37.55 ? 50  PHE K C   1 
ATOM   11466 O  O   . PHE K  1 50  ? 67.333  64.560  7.392   1.00 37.98 ? 50  PHE K O   1 
ATOM   11467 C  CB  . PHE K  1 50  ? 69.439  66.698  6.743   1.00 36.90 ? 50  PHE K CB  1 
ATOM   11468 C  CG  . PHE K  1 50  ? 70.761  67.244  6.300   1.00 40.11 ? 50  PHE K CG  1 
ATOM   11469 C  CD1 . PHE K  1 50  ? 71.670  67.725  7.230   1.00 41.88 ? 50  PHE K CD1 1 
ATOM   11470 C  CD2 . PHE K  1 50  ? 71.101  67.274  4.956   1.00 43.41 ? 50  PHE K CD2 1 
ATOM   11471 C  CE1 . PHE K  1 50  ? 72.890  68.218  6.827   1.00 41.31 ? 50  PHE K CE1 1 
ATOM   11472 C  CE2 . PHE K  1 50  ? 72.318  67.774  4.548   1.00 37.54 ? 50  PHE K CE2 1 
ATOM   11473 C  CZ  . PHE K  1 50  ? 73.213  68.244  5.481   1.00 42.17 ? 50  PHE K CZ  1 
ATOM   11474 N  N   . GLY K  1 51  ? 67.994  65.261  9.439   1.00 36.39 ? 51  GLY K N   1 
ATOM   11475 C  CA  . GLY K  1 51  ? 66.687  65.139  10.062  1.00 35.33 ? 51  GLY K CA  1 
ATOM   11476 C  C   . GLY K  1 51  ? 65.918  66.428  9.835   1.00 39.62 ? 51  GLY K C   1 
ATOM   11477 O  O   . GLY K  1 51  ? 65.535  67.107  10.789  1.00 38.42 ? 51  GLY K O   1 
ATOM   11478 N  N   . ASP K  1 52  ? 65.712  66.763  8.560   1.00 35.05 ? 52  ASP K N   1 
ATOM   11479 C  CA  . ASP K  1 52  ? 65.049  67.994  8.141   1.00 36.69 ? 52  ASP K CA  1 
ATOM   11480 C  C   . ASP K  1 52  ? 63.762  67.643  7.392   1.00 38.86 ? 52  ASP K C   1 
ATOM   11481 O  O   . ASP K  1 52  ? 63.798  67.270  6.215   1.00 40.11 ? 52  ASP K O   1 
ATOM   11482 C  CB  . ASP K  1 52  ? 65.983  68.805  7.235   1.00 40.24 ? 52  ASP K CB  1 
ATOM   11483 C  CG  . ASP K  1 52  ? 65.437  70.193  6.904   1.00 33.64 ? 52  ASP K CG  1 
ATOM   11484 O  OD1 . ASP K  1 52  ? 64.204  70.364  6.817   1.00 32.50 ? 52  ASP K OD1 1 
ATOM   11485 O  OD2 . ASP K  1 52  ? 66.256  71.119  6.728   1.00 33.12 ? 52  ASP K OD2 1 
ATOM   11486 N  N   . ASN K  1 53  ? 62.633  67.783  8.083   1.00 31.88 ? 53  ASN K N   1 
ATOM   11487 C  CA  . ASN K  1 53  ? 61.322  67.414  7.559   1.00 36.90 ? 53  ASN K CA  1 
ATOM   11488 C  C   . ASN K  1 53  ? 60.525  68.599  7.014   1.00 37.94 ? 53  ASN K C   1 
ATOM   11489 O  O   . ASN K  1 53  ? 59.316  68.489  6.799   1.00 33.93 ? 53  ASN K O   1 
ATOM   11490 C  CB  . ASN K  1 53  ? 60.501  66.750  8.671   1.00 40.41 ? 53  ASN K CB  1 
ATOM   11491 C  CG  . ASN K  1 53  ? 59.492  65.753  8.136   1.00 45.94 ? 53  ASN K CG  1 
ATOM   11492 O  OD1 . ASN K  1 53  ? 59.726  65.102  7.107   1.00 43.82 ? 53  ASN K OD1 1 
ATOM   11493 N  ND2 . ASN K  1 53  ? 58.354  65.633  8.825   1.00 39.96 ? 53  ASN K ND2 1 
ATOM   11494 N  N   . THR K  1 54  ? 61.190  69.732  6.805   1.00 38.23 ? 54  THR K N   1 
ATOM   11495 C  CA  . THR K  1 54  ? 60.487  70.949  6.390   1.00 40.28 ? 54  THR K CA  1 
ATOM   11496 C  C   . THR K  1 54  ? 59.877  70.824  4.988   1.00 39.58 ? 54  THR K C   1 
ATOM   11497 O  O   . THR K  1 54  ? 58.788  71.342  4.726   1.00 39.26 ? 54  THR K O   1 
ATOM   11498 C  CB  . THR K  1 54  ? 61.396  72.198  6.473   1.00 38.44 ? 54  THR K CB  1 
ATOM   11499 O  OG1 . THR K  1 54  ? 62.535  72.031  5.616   1.00 34.29 ? 54  THR K OG1 1 
ATOM   11500 C  CG2 . THR K  1 54  ? 61.862  72.428  7.927   1.00 36.15 ? 54  THR K CG2 1 
ATOM   11501 N  N   . ALA K  1 55  ? 60.582  70.131  4.100   1.00 36.34 ? 55  ALA K N   1 
ATOM   11502 C  CA  . ALA K  1 55  ? 60.058  69.828  2.770   1.00 40.05 ? 55  ALA K CA  1 
ATOM   11503 C  C   . ALA K  1 55  ? 59.794  68.322  2.644   1.00 45.60 ? 55  ALA K C   1 
ATOM   11504 O  O   . ALA K  1 55  ? 59.940  67.732  1.563   1.00 42.58 ? 55  ALA K O   1 
ATOM   11505 C  CB  . ALA K  1 55  ? 61.027  70.305  1.686   1.00 36.35 ? 55  ALA K CB  1 
ATOM   11506 N  N   . GLY K  1 56  ? 59.411  67.711  3.765   1.00 43.13 ? 56  GLY K N   1 
ATOM   11507 C  CA  . GLY K  1 56  ? 59.136  66.288  3.827   1.00 40.48 ? 56  GLY K CA  1 
ATOM   11508 C  C   . GLY K  1 56  ? 60.368  65.469  3.515   1.00 41.51 ? 56  GLY K C   1 
ATOM   11509 O  O   . GLY K  1 56  ? 61.460  65.765  3.993   1.00 44.68 ? 56  GLY K O   1 
ATOM   11510 N  N   . SER K  1 57  ? 60.199  64.450  2.681   1.00 48.48 ? 57  SER K N   1 
ATOM   11511 C  CA  . SER K  1 57  ? 61.305  63.572  2.311   1.00 50.17 ? 57  SER K CA  1 
ATOM   11512 C  C   . SER K  1 57  ? 62.398  64.294  1.509   1.00 47.68 ? 57  SER K C   1 
ATOM   11513 O  O   . SER K  1 57  ? 63.560  63.875  1.507   1.00 46.42 ? 57  SER K O   1 
ATOM   11514 C  CB  . SER K  1 57  ? 60.776  62.362  1.530   1.00 54.39 ? 57  SER K CB  1 
ATOM   11515 O  OG  . SER K  1 57  ? 59.667  61.762  2.190   1.00 56.69 ? 57  SER K OG  1 
ATOM   11516 N  N   . THR K  1 58  ? 62.027  65.382  0.841   1.00 46.44 ? 58  THR K N   1 
ATOM   11517 C  CA  . THR K  1 58  ? 62.935  66.074  -0.075  1.00 46.04 ? 58  THR K CA  1 
ATOM   11518 C  C   . THR K  1 58  ? 64.109  66.763  0.631   1.00 46.83 ? 58  THR K C   1 
ATOM   11519 O  O   . THR K  1 58  ? 65.205  66.864  0.079   1.00 45.17 ? 58  THR K O   1 
ATOM   11520 C  CB  . THR K  1 58  ? 62.190  67.124  -0.931  1.00 44.07 ? 58  THR K CB  1 
ATOM   11521 O  OG1 . THR K  1 58  ? 60.827  66.718  -1.134  1.00 42.52 ? 58  THR K OG1 1 
ATOM   11522 C  CG2 . THR K  1 58  ? 62.878  67.290  -2.277  1.00 44.02 ? 58  THR K CG2 1 
ATOM   11523 N  N   . SER K  1 59  ? 63.880  67.236  1.851   1.00 47.04 ? 59  SER K N   1 
ATOM   11524 C  CA  . SER K  1 59  ? 64.904  67.991  2.569   1.00 39.80 ? 59  SER K CA  1 
ATOM   11525 C  C   . SER K  1 59  ? 65.834  67.103  3.395   1.00 39.83 ? 59  SER K C   1 
ATOM   11526 O  O   . SER K  1 59  ? 66.733  67.605  4.073   1.00 40.05 ? 59  SER K O   1 
ATOM   11527 C  CB  . SER K  1 59  ? 64.257  69.071  3.443   1.00 36.45 ? 59  SER K CB  1 
ATOM   11528 O  OG  . SER K  1 59  ? 63.088  68.584  4.079   1.00 37.23 ? 59  SER K OG  1 
ATOM   11529 N  N   . ALA K  1 60  ? 65.628  65.788  3.318   1.00 46.62 ? 60  ALA K N   1 
ATOM   11530 C  CA  . ALA K  1 60  ? 66.414  64.815  4.098   1.00 44.05 ? 60  ALA K CA  1 
ATOM   11531 C  C   . ALA K  1 60  ? 67.893  64.747  3.706   1.00 42.61 ? 60  ALA K C   1 
ATOM   11532 O  O   . ALA K  1 60  ? 68.731  64.340  4.511   1.00 40.49 ? 60  ALA K O   1 
ATOM   11533 C  CB  . ALA K  1 60  ? 65.781  63.422  4.018   1.00 40.63 ? 60  ALA K CB  1 
ATOM   11534 N  N   . GLY K  1 61  ? 68.208  65.123  2.466   1.00 42.10 ? 61  GLY K N   1 
ATOM   11535 C  CA  . GLY K  1 61  ? 69.589  65.134  2.007   1.00 37.72 ? 61  GLY K CA  1 
ATOM   11536 C  C   . GLY K  1 61  ? 70.060  63.811  1.422   1.00 38.70 ? 61  GLY K C   1 
ATOM   11537 O  O   . GLY K  1 61  ? 69.284  62.861  1.324   1.00 42.17 ? 61  GLY K O   1 
ATOM   11538 N  N   . PRO K  1 62  ? 71.344  63.738  1.033   1.00 40.18 ? 62  PRO K N   1 
ATOM   11539 C  CA  . PRO K  1 62  ? 71.902  62.513  0.443   1.00 40.15 ? 62  PRO K CA  1 
ATOM   11540 C  C   . PRO K  1 62  ? 72.069  61.419  1.498   1.00 44.78 ? 62  PRO K C   1 
ATOM   11541 O  O   . PRO K  1 62  ? 71.693  61.632  2.655   1.00 45.00 ? 62  PRO K O   1 
ATOM   11542 C  CB  . PRO K  1 62  ? 73.266  62.971  -0.061  1.00 38.58 ? 62  PRO K CB  1 
ATOM   11543 C  CG  . PRO K  1 62  ? 73.649  64.089  0.881   1.00 37.56 ? 62  PRO K CG  1 
ATOM   11544 C  CD  . PRO K  1 62  ? 72.360  64.796  1.186   1.00 34.21 ? 62  PRO K CD  1 
ATOM   11545 N  N   . HIS K  1 63  ? 72.609  60.267  1.109   1.00 42.80 ? 63  HIS K N   1 
ATOM   11546 C  CA  . HIS K  1 63  ? 72.858  59.180  2.060   1.00 47.37 ? 63  HIS K CA  1 
ATOM   11547 C  C   . HIS K  1 63  ? 73.887  59.636  3.101   1.00 45.27 ? 63  HIS K C   1 
ATOM   11548 O  O   . HIS K  1 63  ? 74.863  60.314  2.761   1.00 41.65 ? 63  HIS K O   1 
ATOM   11549 C  CB  . HIS K  1 63  ? 73.351  57.911  1.344   1.00 46.37 ? 63  HIS K CB  1 
ATOM   11550 C  CG  . HIS K  1 63  ? 72.324  57.260  0.467   1.00 48.14 ? 63  HIS K CG  1 
ATOM   11551 N  ND1 . HIS K  1 63  ? 72.255  55.894  0.291   1.00 51.14 ? 63  HIS K ND1 1 
ATOM   11552 C  CD2 . HIS K  1 63  ? 71.332  57.786  -0.291  1.00 54.97 ? 63  HIS K CD2 1 
ATOM   11553 C  CE1 . HIS K  1 63  ? 71.265  55.607  -0.534  1.00 55.43 ? 63  HIS K CE1 1 
ATOM   11554 N  NE2 . HIS K  1 63  ? 70.685  56.736  -0.899  1.00 53.09 ? 63  HIS K NE2 1 
ATOM   11555 N  N   . PHE K  1 64  ? 73.660  59.289  4.366   1.00 42.91 ? 64  PHE K N   1 
ATOM   11556 C  CA  . PHE K  1 64  ? 74.607  59.653  5.412   1.00 42.20 ? 64  PHE K CA  1 
ATOM   11557 C  C   . PHE K  1 64  ? 75.959  58.982  5.107   1.00 44.11 ? 64  PHE K C   1 
ATOM   11558 O  O   . PHE K  1 64  ? 76.087  57.753  5.144   1.00 39.38 ? 64  PHE K O   1 
ATOM   11559 C  CB  . PHE K  1 64  ? 74.064  59.262  6.796   1.00 45.88 ? 64  PHE K CB  1 
ATOM   11560 C  CG  . PHE K  1 64  ? 74.937  59.696  7.951   1.00 45.13 ? 64  PHE K CG  1 
ATOM   11561 C  CD1 . PHE K  1 64  ? 75.752  60.816  7.851   1.00 41.26 ? 64  PHE K CD1 1 
ATOM   11562 C  CD2 . PHE K  1 64  ? 74.941  58.976  9.136   1.00 46.88 ? 64  PHE K CD2 1 
ATOM   11563 C  CE1 . PHE K  1 64  ? 76.555  61.206  8.907   1.00 46.80 ? 64  PHE K CE1 1 
ATOM   11564 C  CE2 . PHE K  1 64  ? 75.748  59.357  10.201  1.00 46.08 ? 64  PHE K CE2 1 
ATOM   11565 C  CZ  . PHE K  1 64  ? 76.555  60.478  10.087  1.00 44.10 ? 64  PHE K CZ  1 
ATOM   11566 N  N   . ASN K  1 65  ? 76.950  59.806  4.775   1.00 43.20 ? 65  ASN K N   1 
ATOM   11567 C  CA  . ASN K  1 65  ? 78.268  59.322  4.373   1.00 46.17 ? 65  ASN K CA  1 
ATOM   11568 C  C   . ASN K  1 65  ? 79.388  60.185  4.959   1.00 46.07 ? 65  ASN K C   1 
ATOM   11569 O  O   . ASN K  1 65  ? 80.051  60.926  4.234   1.00 45.72 ? 65  ASN K O   1 
ATOM   11570 C  CB  . ASN K  1 65  ? 78.367  59.288  2.840   1.00 49.00 ? 65  ASN K CB  1 
ATOM   11571 C  CG  . ASN K  1 65  ? 79.615  58.559  2.332   1.00 49.77 ? 65  ASN K CG  1 
ATOM   11572 O  OD1 . ASN K  1 65  ? 79.922  58.602  1.143   1.00 50.52 ? 65  ASN K OD1 1 
ATOM   11573 N  ND2 . ASN K  1 65  ? 80.325  57.881  3.229   1.00 52.65 ? 65  ASN K ND2 1 
ATOM   11574 N  N   . PRO K  1 66  ? 79.613  60.080  6.279   1.00 46.77 ? 66  PRO K N   1 
ATOM   11575 C  CA  . PRO K  1 66  ? 80.616  60.913  6.954   1.00 46.18 ? 66  PRO K CA  1 
ATOM   11576 C  C   . PRO K  1 66  ? 82.045  60.543  6.584   1.00 46.00 ? 66  PRO K C   1 
ATOM   11577 O  O   . PRO K  1 66  ? 82.973  61.270  6.933   1.00 45.49 ? 66  PRO K O   1 
ATOM   11578 C  CB  . PRO K  1 66  ? 80.376  60.611  8.438   1.00 43.97 ? 66  PRO K CB  1 
ATOM   11579 C  CG  . PRO K  1 66  ? 79.806  59.236  8.442   1.00 45.38 ? 66  PRO K CG  1 
ATOM   11580 C  CD  . PRO K  1 66  ? 78.920  59.191  7.224   1.00 46.83 ? 66  PRO K CD  1 
ATOM   11581 N  N   . LEU K  1 67  ? 82.231  59.421  5.904   1.00 49.33 ? 67  LEU K N   1 
ATOM   11582 C  CA  . LEU K  1 67  ? 83.586  58.991  5.580   1.00 50.63 ? 67  LEU K CA  1 
ATOM   11583 C  C   . LEU K  1 67  ? 83.910  59.161  4.097   1.00 51.37 ? 67  LEU K C   1 
ATOM   11584 O  O   . LEU K  1 67  ? 85.020  58.849  3.659   1.00 54.08 ? 67  LEU K O   1 
ATOM   11585 C  CB  . LEU K  1 67  ? 83.838  57.562  6.072   1.00 50.90 ? 67  LEU K CB  1 
ATOM   11586 C  CG  . LEU K  1 67  ? 83.779  57.430  7.603   1.00 50.61 ? 67  LEU K CG  1 
ATOM   11587 C  CD1 . LEU K  1 67  ? 84.159  56.030  8.059   1.00 52.64 ? 67  LEU K CD1 1 
ATOM   11588 C  CD2 . LEU K  1 67  ? 84.660  58.479  8.297   1.00 48.85 ? 67  LEU K CD2 1 
ATOM   11589 N  N   . SER K  1 68  ? 82.931  59.663  3.343   1.00 51.41 ? 68  SER K N   1 
ATOM   11590 C  CA  . SER K  1 68  ? 83.114  60.036  1.939   1.00 55.52 ? 68  SER K CA  1 
ATOM   11591 C  C   . SER K  1 68  ? 83.427  58.841  1.036   1.00 55.48 ? 68  SER K C   1 
ATOM   11592 O  O   . SER K  1 68  ? 84.542  58.719  0.516   1.00 53.76 ? 68  SER K O   1 
ATOM   11593 C  CB  . SER K  1 68  ? 84.206  61.104  1.809   1.00 52.49 ? 68  SER K CB  1 
ATOM   11594 O  OG  . SER K  1 68  ? 83.984  62.166  2.722   1.00 47.95 ? 68  SER K OG  1 
ATOM   11595 N  N   . ARG K  1 69  ? 82.431  57.978  0.843   1.00 54.37 ? 69  ARG K N   1 
ATOM   11596 C  CA  . ARG K  1 69  ? 82.610  56.733  0.102   1.00 56.57 ? 69  ARG K CA  1 
ATOM   11597 C  C   . ARG K  1 69  ? 81.673  56.638  -1.095  1.00 59.21 ? 69  ARG K C   1 
ATOM   11598 O  O   . ARG K  1 69  ? 81.305  57.645  -1.698  1.00 62.09 ? 69  ARG K O   1 
ATOM   11599 C  CB  . ARG K  1 69  ? 82.361  55.530  1.015   1.00 56.39 ? 69  ARG K CB  1 
ATOM   11600 C  CG  . ARG K  1 69  ? 83.080  55.601  2.342   1.00 56.42 ? 69  ARG K CG  1 
ATOM   11601 C  CD  . ARG K  1 69  ? 84.538  55.225  2.208   1.00 55.99 ? 69  ARG K CD  1 
ATOM   11602 N  NE  . ARG K  1 69  ? 84.752  53.818  2.530   1.00 61.23 ? 69  ARG K NE  1 
ATOM   11603 C  CZ  . ARG K  1 69  ? 85.232  53.385  3.692   1.00 64.35 ? 69  ARG K CZ  1 
ATOM   11604 N  NH1 . ARG K  1 69  ? 85.561  54.254  4.642   1.00 59.03 ? 69  ARG K NH1 1 
ATOM   11605 N  NH2 . ARG K  1 69  ? 85.388  52.082  3.903   1.00 62.58 ? 69  ARG K NH2 1 
ATOM   11606 N  N   . LYS K  1 70  ? 81.296  55.408  -1.427  1.00 59.52 ? 70  LYS K N   1 
ATOM   11607 C  CA  . LYS K  1 70  ? 80.361  55.134  -2.510  1.00 59.14 ? 70  LYS K CA  1 
ATOM   11608 C  C   . LYS K  1 70  ? 79.288  54.181  -1.999  1.00 57.46 ? 70  LYS K C   1 
ATOM   11609 O  O   . LYS K  1 70  ? 79.525  53.449  -1.042  1.00 58.24 ? 70  LYS K O   1 
ATOM   11610 C  CB  . LYS K  1 70  ? 81.103  54.535  -3.708  1.00 63.48 ? 70  LYS K CB  1 
ATOM   11611 C  CG  . LYS K  1 70  ? 81.996  55.541  -4.431  1.00 66.77 ? 70  LYS K CG  1 
ATOM   11612 C  CD  . LYS K  1 70  ? 82.896  54.877  -5.464  1.00 75.07 ? 70  LYS K CD  1 
ATOM   11613 C  CE  . LYS K  1 70  ? 82.103  54.105  -6.506  1.00 68.09 ? 70  LYS K CE  1 
ATOM   11614 N  NZ  . LYS K  1 70  ? 83.007  53.395  -7.455  1.00 71.93 ? 70  LYS K NZ  1 
ATOM   11615 N  N   . HIS K  1 71  ? 78.108  54.203  -2.615  1.00 55.83 ? 71  HIS K N   1 
ATOM   11616 C  CA  . HIS K  1 71  ? 76.984  53.392  -2.139  1.00 53.97 ? 71  HIS K CA  1 
ATOM   11617 C  C   . HIS K  1 71  ? 77.324  51.914  -2.138  1.00 56.11 ? 71  HIS K C   1 
ATOM   11618 O  O   . HIS K  1 71  ? 78.146  51.456  -2.929  1.00 56.36 ? 71  HIS K O   1 
ATOM   11619 C  CB  . HIS K  1 71  ? 75.726  53.642  -2.981  1.00 56.19 ? 71  HIS K CB  1 
ATOM   11620 C  CG  . HIS K  1 71  ? 74.543  52.815  -2.572  1.00 55.27 ? 71  HIS K CG  1 
ATOM   11621 N  ND1 . HIS K  1 71  ? 73.661  53.208  -1.588  1.00 55.67 ? 71  HIS K ND1 1 
ATOM   11622 C  CD2 . HIS K  1 71  ? 74.097  51.615  -3.015  1.00 58.42 ? 71  HIS K CD2 1 
ATOM   11623 C  CE1 . HIS K  1 71  ? 72.726  52.286  -1.440  1.00 56.45 ? 71  HIS K CE1 1 
ATOM   11624 N  NE2 . HIS K  1 71  ? 72.968  51.308  -2.293  1.00 58.10 ? 71  HIS K NE2 1 
ATOM   11625 N  N   . GLY K  1 72  ? 76.694  51.173  -1.234  1.00 58.41 ? 72  GLY K N   1 
ATOM   11626 C  CA  . GLY K  1 72  ? 76.859  49.737  -1.184  1.00 58.48 ? 72  GLY K CA  1 
ATOM   11627 C  C   . GLY K  1 72  ? 75.702  49.069  -0.477  1.00 59.63 ? 72  GLY K C   1 
ATOM   11628 O  O   . GLY K  1 72  ? 74.691  49.703  -0.167  1.00 61.65 ? 72  GLY K O   1 
ATOM   11629 N  N   . GLY K  1 73  ? 75.846  47.771  -0.243  1.00 62.91 ? 73  GLY K N   1 
ATOM   11630 C  CA  . GLY K  1 73  ? 74.942  47.052  0.630   1.00 63.03 ? 73  GLY K CA  1 
ATOM   11631 C  C   . GLY K  1 73  ? 75.549  47.063  2.019   1.00 57.93 ? 73  GLY K C   1 
ATOM   11632 O  O   . GLY K  1 73  ? 76.708  47.455  2.188   1.00 54.91 ? 73  GLY K O   1 
ATOM   11633 N  N   . PRO K  1 74  ? 74.774  46.629  3.022   1.00 60.56 ? 74  PRO K N   1 
ATOM   11634 C  CA  . PRO K  1 74  ? 75.276  46.616  4.406   1.00 60.36 ? 74  PRO K CA  1 
ATOM   11635 C  C   . PRO K  1 74  ? 76.544  45.764  4.541   1.00 58.60 ? 74  PRO K C   1 
ATOM   11636 O  O   . PRO K  1 74  ? 77.501  46.173  5.208   1.00 56.23 ? 74  PRO K O   1 
ATOM   11637 C  CB  . PRO K  1 74  ? 74.111  46.016  5.208   1.00 56.75 ? 74  PRO K CB  1 
ATOM   11638 C  CG  . PRO K  1 74  ? 73.250  45.301  4.191   1.00 58.16 ? 74  PRO K CG  1 
ATOM   11639 C  CD  . PRO K  1 74  ? 73.426  46.043  2.895   1.00 56.90 ? 74  PRO K CD  1 
ATOM   11640 N  N   . LYS K  1 75  ? 76.552  44.611  3.876   1.00 56.25 ? 75  LYS K N   1 
ATOM   11641 C  CA  . LYS K  1 75  ? 77.670  43.679  3.933   1.00 48.55 ? 75  LYS K CA  1 
ATOM   11642 C  C   . LYS K  1 75  ? 78.915  44.245  3.260   1.00 51.79 ? 75  LYS K C   1 
ATOM   11643 O  O   . LYS K  1 75  ? 80.042  43.894  3.616   1.00 54.17 ? 75  LYS K O   1 
ATOM   11644 C  CB  . LYS K  1 75  ? 77.285  42.334  3.305   1.00 55.65 ? 75  LYS K CB  1 
ATOM   11645 C  CG  . LYS K  1 75  ? 76.321  41.482  4.144   1.00 51.67 ? 75  LYS K CG  1 
ATOM   11646 C  CD  . LYS K  1 75  ? 74.901  42.014  4.088   1.00 52.20 ? 75  LYS K CD  1 
ATOM   11647 C  CE  . LYS K  1 75  ? 74.046  41.430  5.194   1.00 58.75 ? 75  LYS K CE  1 
ATOM   11648 N  NZ  . LYS K  1 75  ? 72.863  42.294  5.462   1.00 58.85 ? 75  LYS K NZ  1 
ATOM   11649 N  N   . ASP K  1 76  ? 78.716  45.131  2.295   1.00 53.62 ? 76  ASP K N   1 
ATOM   11650 C  CA  . ASP K  1 76  ? 79.840  45.710  1.573   1.00 56.70 ? 76  ASP K CA  1 
ATOM   11651 C  C   . ASP K  1 76  ? 80.743  46.524  2.485   1.00 58.00 ? 76  ASP K C   1 
ATOM   11652 O  O   . ASP K  1 76  ? 80.275  47.176  3.415   1.00 54.73 ? 76  ASP K O   1 
ATOM   11653 C  CB  . ASP K  1 76  ? 79.357  46.570  0.401   1.00 57.40 ? 76  ASP K CB  1 
ATOM   11654 C  CG  . ASP K  1 76  ? 78.847  45.735  -0.753  1.00 60.73 ? 76  ASP K CG  1 
ATOM   11655 O  OD1 . ASP K  1 76  ? 79.152  44.525  -0.774  1.00 64.20 ? 76  ASP K OD1 1 
ATOM   11656 O  OD2 . ASP K  1 76  ? 78.147  46.278  -1.636  1.00 66.29 ? 76  ASP K OD2 1 
ATOM   11657 N  N   . GLU K  1 77  ? 82.042  46.476  2.212   1.00 58.98 ? 77  GLU K N   1 
ATOM   11658 C  CA  . GLU K  1 77  ? 83.005  47.298  2.927   1.00 59.00 ? 77  GLU K CA  1 
ATOM   11659 C  C   . GLU K  1 77  ? 82.982  48.715  2.364   1.00 62.61 ? 77  GLU K C   1 
ATOM   11660 O  O   . GLU K  1 77  ? 83.072  49.693  3.109   1.00 63.84 ? 77  GLU K O   1 
ATOM   11661 C  CB  . GLU K  1 77  ? 84.406  46.699  2.821   1.00 58.73 ? 77  GLU K CB  1 
ATOM   11662 C  CG  . GLU K  1 77  ? 85.339  47.110  3.951   1.00 59.23 ? 77  GLU K CG  1 
ATOM   11663 C  CD  . GLU K  1 77  ? 85.786  48.551  3.844   1.00 63.36 ? 77  GLU K CD  1 
ATOM   11664 O  OE1 . GLU K  1 77  ? 85.916  49.052  2.705   1.00 68.67 ? 77  GLU K OE1 1 
ATOM   11665 O  OE2 . GLU K  1 77  ? 86.005  49.187  4.896   1.00 66.53 ? 77  GLU K OE2 1 
ATOM   11666 N  N   . GLU K  1 78  ? 82.873  48.823  1.043   1.00 62.96 ? 78  GLU K N   1 
ATOM   11667 C  CA  . GLU K  1 78  ? 82.647  50.117  0.410   1.00 62.86 ? 78  GLU K CA  1 
ATOM   11668 C  C   . GLU K  1 78  ? 81.155  50.433  0.463   1.00 61.33 ? 78  GLU K C   1 
ATOM   11669 O  O   . GLU K  1 78  ? 80.344  49.823  -0.246  1.00 53.61 ? 78  GLU K O   1 
ATOM   11670 C  CB  . GLU K  1 78  ? 83.165  50.138  -1.034  1.00 62.55 ? 78  GLU K CB  1 
ATOM   11671 C  CG  . GLU K  1 78  ? 83.256  51.534  -1.661  1.00 61.01 ? 78  GLU K CG  1 
ATOM   11672 C  CD  . GLU K  1 78  ? 84.344  52.405  -1.037  1.00 62.70 ? 78  GLU K CD  1 
ATOM   11673 O  OE1 . GLU K  1 78  ? 85.125  51.894  -0.206  1.00 65.70 ? 78  GLU K OE1 1 
ATOM   11674 O  OE2 . GLU K  1 78  ? 84.418  53.607  -1.379  1.00 57.45 ? 78  GLU K OE2 1 
ATOM   11675 N  N   . ARG K  1 79  ? 80.811  51.377  1.337   1.00 58.98 ? 79  ARG K N   1 
ATOM   11676 C  CA  . ARG K  1 79  ? 79.431  51.769  1.570   1.00 54.40 ? 79  ARG K CA  1 
ATOM   11677 C  C   . ARG K  1 79  ? 79.380  53.142  2.228   1.00 56.15 ? 79  ARG K C   1 
ATOM   11678 O  O   . ARG K  1 79  ? 80.407  53.701  2.624   1.00 53.77 ? 79  ARG K O   1 
ATOM   11679 C  CB  . ARG K  1 79  ? 78.742  50.759  2.485   1.00 54.55 ? 79  ARG K CB  1 
ATOM   11680 C  CG  . ARG K  1 79  ? 79.432  50.616  3.835   1.00 55.45 ? 79  ARG K CG  1 
ATOM   11681 C  CD  . ARG K  1 79  ? 78.727  49.621  4.751   1.00 57.07 ? 79  ARG K CD  1 
ATOM   11682 N  NE  . ARG K  1 79  ? 77.474  50.130  5.302   1.00 55.94 ? 79  ARG K NE  1 
ATOM   11683 C  CZ  . ARG K  1 79  ? 76.806  49.541  6.292   1.00 55.99 ? 79  ARG K CZ  1 
ATOM   11684 N  NH1 . ARG K  1 79  ? 77.283  48.440  6.852   1.00 55.92 ? 79  ARG K NH1 1 
ATOM   11685 N  NH2 . ARG K  1 79  ? 75.675  50.065  6.745   1.00 54.78 ? 79  ARG K NH2 1 
ATOM   11686 N  N   . HIS K  1 80  ? 78.169  53.680  2.332   1.00 54.73 ? 80  HIS K N   1 
ATOM   11687 C  CA  . HIS K  1 80  ? 77.897  54.817  3.203   1.00 55.28 ? 80  HIS K CA  1 
ATOM   11688 C  C   . HIS K  1 80  ? 77.428  54.213  4.525   1.00 50.05 ? 80  HIS K C   1 
ATOM   11689 O  O   . HIS K  1 80  ? 76.907  53.100  4.532   1.00 51.71 ? 80  HIS K O   1 
ATOM   11690 C  CB  . HIS K  1 80  ? 76.797  55.694  2.595   1.00 47.66 ? 80  HIS K CB  1 
ATOM   11691 C  CG  . HIS K  1 80  ? 77.013  56.017  1.147   1.00 53.89 ? 80  HIS K CG  1 
ATOM   11692 N  ND1 . HIS K  1 80  ? 75.981  56.074  0.234   1.00 47.51 ? 80  HIS K ND1 1 
ATOM   11693 C  CD2 . HIS K  1 80  ? 78.142  56.296  0.455   1.00 52.66 ? 80  HIS K CD2 1 
ATOM   11694 C  CE1 . HIS K  1 80  ? 76.464  56.385  -0.954  1.00 46.19 ? 80  HIS K CE1 1 
ATOM   11695 N  NE2 . HIS K  1 80  ? 77.772  56.526  -0.848  1.00 52.01 ? 80  HIS K NE2 1 
ATOM   11696 N  N   . VAL K  1 81  ? 77.609  54.907  5.646   1.00 47.38 ? 81  VAL K N   1 
ATOM   11697 C  CA  . VAL K  1 81  ? 77.116  54.340  6.901   1.00 48.89 ? 81  VAL K CA  1 
ATOM   11698 C  C   . VAL K  1 81  ? 75.600  54.259  6.848   1.00 49.01 ? 81  VAL K C   1 
ATOM   11699 O  O   . VAL K  1 81  ? 74.994  53.394  7.481   1.00 49.19 ? 81  VAL K O   1 
ATOM   11700 C  CB  . VAL K  1 81  ? 77.557  55.117  8.160   1.00 49.94 ? 81  VAL K CB  1 
ATOM   11701 C  CG1 . VAL K  1 81  ? 79.081  55.165  8.278   1.00 50.93 ? 81  VAL K CG1 1 
ATOM   11702 C  CG2 . VAL K  1 81  ? 76.973  56.498  8.159   1.00 49.71 ? 81  VAL K CG2 1 
ATOM   11703 N  N   . GLY K  1 82  ? 74.995  55.148  6.064   1.00 47.03 ? 82  GLY K N   1 
ATOM   11704 C  CA  . GLY K  1 82  ? 73.557  55.150  5.892   1.00 45.39 ? 82  GLY K CA  1 
ATOM   11705 C  C   . GLY K  1 82  ? 73.090  53.921  5.145   1.00 49.63 ? 82  GLY K C   1 
ATOM   11706 O  O   . GLY K  1 82  ? 71.920  53.555  5.223   1.00 48.91 ? 82  GLY K O   1 
ATOM   11707 N  N   . ASP K  1 83  ? 74.008  53.283  4.417   1.00 54.19 ? 83  ASP K N   1 
ATOM   11708 C  CA  . ASP K  1 83  ? 73.661  52.131  3.586   1.00 54.45 ? 83  ASP K CA  1 
ATOM   11709 C  C   . ASP K  1 83  ? 73.272  50.935  4.426   1.00 53.01 ? 83  ASP K C   1 
ATOM   11710 O  O   . ASP K  1 83  ? 74.117  50.315  5.056   1.00 55.43 ? 83  ASP K O   1 
ATOM   11711 C  CB  . ASP K  1 83  ? 74.821  51.748  2.669   1.00 53.20 ? 83  ASP K CB  1 
ATOM   11712 C  CG  . ASP K  1 83  ? 75.042  52.756  1.571   1.00 51.02 ? 83  ASP K CG  1 
ATOM   11713 O  OD1 . ASP K  1 83  ? 74.039  53.368  1.132   1.00 52.37 ? 83  ASP K OD1 1 
ATOM   11714 O  OD2 . ASP K  1 83  ? 76.207  52.930  1.154   1.00 43.79 ? 83  ASP K OD2 1 
ATOM   11715 N  N   . LEU K  1 84  ? 71.990  50.605  4.443   1.00 53.73 ? 84  LEU K N   1 
ATOM   11716 C  CA  . LEU K  1 84  ? 71.583  49.416  5.161   1.00 55.58 ? 84  LEU K CA  1 
ATOM   11717 C  C   . LEU K  1 84  ? 70.725  48.517  4.274   1.00 59.15 ? 84  LEU K C   1 
ATOM   11718 O  O   . LEU K  1 84  ? 70.018  47.623  4.747   1.00 57.96 ? 84  LEU K O   1 
ATOM   11719 C  CB  . LEU K  1 84  ? 70.921  49.781  6.485   1.00 56.70 ? 84  LEU K CB  1 
ATOM   11720 C  CG  . LEU K  1 84  ? 69.429  50.042  6.540   1.00 57.97 ? 84  LEU K CG  1 
ATOM   11721 C  CD1 . LEU K  1 84  ? 68.823  48.933  7.372   1.00 67.05 ? 84  LEU K CD1 1 
ATOM   11722 C  CD2 . LEU K  1 84  ? 69.162  51.397  7.152   1.00 60.26 ? 84  LEU K CD2 1 
ATOM   11723 N  N   . GLY K  1 85  ? 70.822  48.758  2.970   1.00 62.40 ? 85  GLY K N   1 
ATOM   11724 C  CA  . GLY K  1 85  ? 70.286  47.848  1.977   1.00 57.67 ? 85  GLY K CA  1 
ATOM   11725 C  C   . GLY K  1 85  ? 68.779  47.837  1.871   1.00 59.19 ? 85  GLY K C   1 
ATOM   11726 O  O   . GLY K  1 85  ? 68.162  48.860  1.574   1.00 61.50 ? 85  GLY K O   1 
ATOM   11727 N  N   . ASN K  1 86  ? 68.183  46.674  2.108   1.00 59.83 ? 86  ASN K N   1 
ATOM   11728 C  CA  . ASN K  1 86  ? 66.759  46.496  1.861   1.00 60.94 ? 86  ASN K CA  1 
ATOM   11729 C  C   . ASN K  1 86  ? 66.016  45.810  3.009   1.00 60.15 ? 86  ASN K C   1 
ATOM   11730 O  O   . ASN K  1 86  ? 66.593  45.031  3.775   1.00 59.08 ? 86  ASN K O   1 
ATOM   11731 C  CB  . ASN K  1 86  ? 66.523  45.719  0.551   1.00 62.00 ? 86  ASN K CB  1 
ATOM   11732 C  CG  . ASN K  1 86  ? 66.912  46.513  -0.701  1.00 64.17 ? 86  ASN K CG  1 
ATOM   11733 O  OD1 . ASN K  1 86  ? 66.217  47.452  -1.097  1.00 66.04 ? 86  ASN K OD1 1 
ATOM   11734 N  ND2 . ASN K  1 86  ? 68.007  46.112  -1.346  1.00 57.59 ? 86  ASN K ND2 1 
ATOM   11735 N  N   . VAL K  1 87  ? 64.733  46.136  3.122   1.00 60.90 ? 87  VAL K N   1 
ATOM   11736 C  CA  . VAL K  1 87  ? 63.799  45.408  3.967   1.00 63.89 ? 87  VAL K CA  1 
ATOM   11737 C  C   . VAL K  1 87  ? 62.853  44.667  3.040   1.00 69.78 ? 87  VAL K C   1 
ATOM   11738 O  O   . VAL K  1 87  ? 62.787  44.954  1.842   1.00 69.30 ? 87  VAL K O   1 
ATOM   11739 C  CB  . VAL K  1 87  ? 62.972  46.343  4.875   1.00 64.95 ? 87  VAL K CB  1 
ATOM   11740 C  CG1 . VAL K  1 87  ? 63.848  46.953  5.974   1.00 60.40 ? 87  VAL K CG1 1 
ATOM   11741 C  CG2 . VAL K  1 87  ? 62.272  47.423  4.046   1.00 61.37 ? 87  VAL K CG2 1 
ATOM   11742 N  N   . THR K  1 88  ? 62.112  43.719  3.592   1.00 71.07 ? 88  THR K N   1 
ATOM   11743 C  CA  . THR K  1 88  ? 61.314  42.829  2.763   1.00 74.29 ? 88  THR K CA  1 
ATOM   11744 C  C   . THR K  1 88  ? 59.837  42.871  3.137   1.00 74.90 ? 88  THR K C   1 
ATOM   11745 O  O   . THR K  1 88  ? 59.444  42.364  4.190   1.00 72.88 ? 88  THR K O   1 
ATOM   11746 C  CB  . THR K  1 88  ? 61.831  41.387  2.885   1.00 74.46 ? 88  THR K CB  1 
ATOM   11747 O  OG1 . THR K  1 88  ? 61.845  41.007  4.267   1.00 77.76 ? 88  THR K OG1 1 
ATOM   11748 C  CG2 . THR K  1 88  ? 63.248  41.285  2.335   1.00 70.33 ? 88  THR K CG2 1 
ATOM   11749 N  N   . ALA K  1 89  ? 59.022  43.479  2.277   1.00 75.98 ? 89  ALA K N   1 
ATOM   11750 C  CA  . ALA K  1 89  ? 57.580  43.516  2.502   1.00 75.71 ? 89  ALA K CA  1 
ATOM   11751 C  C   . ALA K  1 89  ? 56.959  42.197  2.051   1.00 79.92 ? 89  ALA K C   1 
ATOM   11752 O  O   . ALA K  1 89  ? 57.195  41.745  0.926   1.00 75.69 ? 89  ALA K O   1 
ATOM   11753 C  CB  . ALA K  1 89  ? 56.946  44.692  1.775   1.00 72.93 ? 89  ALA K CB  1 
ATOM   11754 N  N   . ASP K  1 90  ? 56.180  41.577  2.937   1.00 80.09 ? 90  ASP K N   1 
ATOM   11755 C  CA  . ASP K  1 90  ? 55.580  40.277  2.643   1.00 78.06 ? 90  ASP K CA  1 
ATOM   11756 C  C   . ASP K  1 90  ? 54.378  40.385  1.695   1.00 80.53 ? 90  ASP K C   1 
ATOM   11757 O  O   . ASP K  1 90  ? 54.303  41.310  0.880   1.00 83.25 ? 90  ASP K O   1 
ATOM   11758 C  CB  . ASP K  1 90  ? 55.237  39.501  3.932   1.00 76.24 ? 90  ASP K CB  1 
ATOM   11759 C  CG  . ASP K  1 90  ? 54.209  40.207  4.811   1.00 78.21 ? 90  ASP K CG  1 
ATOM   11760 O  OD1 . ASP K  1 90  ? 53.508  41.118  4.325   1.00 78.24 ? 90  ASP K OD1 1 
ATOM   11761 O  OD2 . ASP K  1 90  ? 54.088  39.835  6.000   1.00 72.14 ? 90  ASP K OD2 1 
ATOM   11762 N  N   . LYS K  1 91  ? 53.444  39.443  1.807   1.00 80.37 ? 91  LYS K N   1 
ATOM   11763 C  CA  . LYS K  1 91  ? 52.280  39.411  0.926   1.00 77.23 ? 91  LYS K CA  1 
ATOM   11764 C  C   . LYS K  1 91  ? 51.357  40.619  1.131   1.00 75.90 ? 91  LYS K C   1 
ATOM   11765 O  O   . LYS K  1 91  ? 50.897  41.235  0.165   1.00 77.16 ? 91  LYS K O   1 
ATOM   11766 C  CB  . LYS K  1 91  ? 51.511  38.088  1.091   1.00 78.14 ? 91  LYS K CB  1 
ATOM   11767 C  CG  . LYS K  1 91  ? 50.831  37.880  2.448   1.00 75.40 ? 91  LYS K CG  1 
ATOM   11768 C  CD  . LYS K  1 91  ? 50.119  36.531  2.517   1.00 71.68 ? 91  LYS K CD  1 
ATOM   11769 C  CE  . LYS K  1 91  ? 48.818  36.620  3.301   1.00 69.37 ? 91  LYS K CE  1 
ATOM   11770 N  NZ  . LYS K  1 91  ? 47.777  37.373  2.546   1.00 71.68 ? 91  LYS K NZ  1 
ATOM   11771 N  N   . ASP K  1 92  ? 51.119  40.964  2.394   1.00 78.27 ? 92  ASP K N   1 
ATOM   11772 C  CA  . ASP K  1 92  ? 50.207  42.040  2.770   1.00 78.47 ? 92  ASP K CA  1 
ATOM   11773 C  C   . ASP K  1 92  ? 50.923  43.389  2.812   1.00 76.18 ? 92  ASP K C   1 
ATOM   11774 O  O   . ASP K  1 92  ? 50.429  44.348  3.414   1.00 72.35 ? 92  ASP K O   1 
ATOM   11775 C  CB  . ASP K  1 92  ? 49.593  41.746  4.146   1.00 77.78 ? 92  ASP K CB  1 
ATOM   11776 C  CG  . ASP K  1 92  ? 48.998  40.347  4.242   1.00 79.19 ? 92  ASP K CG  1 
ATOM   11777 O  OD1 . ASP K  1 92  ? 48.310  39.923  3.287   1.00 80.86 ? 92  ASP K OD1 1 
ATOM   11778 O  OD2 . ASP K  1 92  ? 49.222  39.671  5.274   1.00 77.64 ? 92  ASP K OD2 1 
ATOM   11779 N  N   . GLY K  1 93  ? 52.090  43.452  2.177   1.00 76.68 ? 93  GLY K N   1 
ATOM   11780 C  CA  . GLY K  1 93  ? 52.923  44.638  2.216   1.00 76.59 ? 93  GLY K CA  1 
ATOM   11781 C  C   . GLY K  1 93  ? 53.270  45.061  3.632   1.00 76.68 ? 93  GLY K C   1 
ATOM   11782 O  O   . GLY K  1 93  ? 53.098  46.223  3.998   1.00 74.71 ? 93  GLY K O   1 
ATOM   11783 N  N   . VAL K  1 94  ? 53.742  44.105  4.428   1.00 78.93 ? 94  VAL K N   1 
ATOM   11784 C  CA  . VAL K  1 94  ? 54.196  44.363  5.798   1.00 77.25 ? 94  VAL K CA  1 
ATOM   11785 C  C   . VAL K  1 94  ? 55.606  43.790  6.017   1.00 79.18 ? 94  VAL K C   1 
ATOM   11786 O  O   . VAL K  1 94  ? 55.790  42.569  6.132   1.00 76.85 ? 94  VAL K O   1 
ATOM   11787 C  CB  . VAL K  1 94  ? 53.209  43.792  6.856   1.00 76.56 ? 94  VAL K CB  1 
ATOM   11788 C  CG1 . VAL K  1 94  ? 53.804  43.871  8.264   1.00 70.28 ? 94  VAL K CG1 1 
ATOM   11789 C  CG2 . VAL K  1 94  ? 51.860  44.516  6.785   1.00 73.32 ? 94  VAL K CG2 1 
ATOM   11790 N  N   . ALA K  1 95  ? 56.597  44.681  6.056   1.00 76.56 ? 95  ALA K N   1 
ATOM   11791 C  CA  . ALA K  1 95  ? 57.998  44.289  6.193   1.00 73.02 ? 95  ALA K CA  1 
ATOM   11792 C  C   . ALA K  1 95  ? 58.410  44.183  7.656   1.00 73.67 ? 95  ALA K C   1 
ATOM   11793 O  O   . ALA K  1 95  ? 58.277  45.147  8.410   1.00 73.47 ? 95  ALA K O   1 
ATOM   11794 C  CB  . ALA K  1 95  ? 58.896  45.276  5.466   1.00 69.31 ? 95  ALA K CB  1 
ATOM   11795 N  N   . ASP K  1 96  ? 58.908  43.013  8.053   1.00 72.54 ? 96  ASP K N   1 
ATOM   11796 C  CA  . ASP K  1 96  ? 59.373  42.806  9.423   1.00 66.68 ? 96  ASP K CA  1 
ATOM   11797 C  C   . ASP K  1 96  ? 60.890  42.954  9.520   1.00 67.35 ? 96  ASP K C   1 
ATOM   11798 O  O   . ASP K  1 96  ? 61.654  42.055  9.153   1.00 62.44 ? 96  ASP K O   1 
ATOM   11799 C  CB  . ASP K  1 96  ? 58.913  41.451  9.975   1.00 68.90 ? 96  ASP K CB  1 
ATOM   11800 C  CG  . ASP K  1 96  ? 57.463  41.468  10.441  1.00 72.68 ? 96  ASP K CG  1 
ATOM   11801 O  OD1 . ASP K  1 96  ? 56.561  41.634  9.586   1.00 70.22 ? 96  ASP K OD1 1 
ATOM   11802 O  OD2 . ASP K  1 96  ? 57.228  41.305  11.661  1.00 73.47 ? 96  ASP K OD2 1 
ATOM   11803 N  N   . VAL K  1 97  ? 61.312  44.109  10.017  1.00 65.64 ? 97  VAL K N   1 
ATOM   11804 C  CA  . VAL K  1 97  ? 62.723  44.430  10.124  1.00 62.06 ? 97  VAL K CA  1 
ATOM   11805 C  C   . VAL K  1 97  ? 63.350  43.715  11.322  1.00 62.74 ? 97  VAL K C   1 
ATOM   11806 O  O   . VAL K  1 97  ? 62.754  43.627  12.398  1.00 62.18 ? 97  VAL K O   1 
ATOM   11807 C  CB  . VAL K  1 97  ? 62.935  45.961  10.256  1.00 59.23 ? 97  VAL K CB  1 
ATOM   11808 C  CG1 . VAL K  1 97  ? 64.401  46.320  10.079  1.00 61.56 ? 97  VAL K CG1 1 
ATOM   11809 C  CG2 . VAL K  1 97  ? 62.073  46.713  9.246   1.00 61.01 ? 97  VAL K CG2 1 
ATOM   11810 N  N   . SER K  1 98  ? 64.546  43.180  11.111  1.00 63.38 ? 98  SER K N   1 
ATOM   11811 C  CA  . SER K  1 98  ? 65.393  42.706  12.193  1.00 57.64 ? 98  SER K CA  1 
ATOM   11812 C  C   . SER K  1 98  ? 66.801  42.623  11.645  1.00 61.94 ? 98  SER K C   1 
ATOM   11813 O  O   . SER K  1 98  ? 67.124  41.736  10.860  1.00 65.08 ? 98  SER K O   1 
ATOM   11814 C  CB  . SER K  1 98  ? 64.945  41.352  12.720  1.00 58.93 ? 98  SER K CB  1 
ATOM   11815 O  OG  . SER K  1 98  ? 65.604  41.076  13.942  1.00 55.28 ? 98  SER K OG  1 
ATOM   11816 N  N   . ILE K  1 99  ? 67.637  43.564  12.057  1.00 62.77 ? 99  ILE K N   1 
ATOM   11817 C  CA  . ILE K  1 99  ? 68.924  43.772  11.415  1.00 58.86 ? 99  ILE K CA  1 
ATOM   11818 C  C   . ILE K  1 99  ? 70.020  43.995  12.448  1.00 60.28 ? 99  ILE K C   1 
ATOM   11819 O  O   . ILE K  1 99  ? 69.796  44.617  13.486  1.00 59.40 ? 99  ILE K O   1 
ATOM   11820 C  CB  . ILE K  1 99  ? 68.839  44.980  10.444  1.00 63.34 ? 99  ILE K CB  1 
ATOM   11821 C  CG1 . ILE K  1 99  ? 67.980  44.615  9.225   1.00 63.98 ? 99  ILE K CG1 1 
ATOM   11822 C  CG2 . ILE K  1 99  ? 70.226  45.466  10.018  1.00 58.68 ? 99  ILE K CG2 1 
ATOM   11823 C  CD1 . ILE K  1 99  ? 67.627  45.790  8.334   1.00 66.92 ? 99  ILE K CD1 1 
ATOM   11824 N  N   . GLU K  1 100 ? 71.198  43.452  12.175  1.00 57.82 ? 100 GLU K N   1 
ATOM   11825 C  CA  . GLU K  1 100 ? 72.359  43.703  13.006  1.00 59.28 ? 100 GLU K CA  1 
ATOM   11826 C  C   . GLU K  1 100 ? 73.344  44.498  12.166  1.00 61.28 ? 100 GLU K C   1 
ATOM   11827 O  O   . GLU K  1 100 ? 73.780  44.041  11.102  1.00 64.23 ? 100 GLU K O   1 
ATOM   11828 C  CB  . GLU K  1 100 ? 72.986  42.379  13.448  1.00 62.47 ? 100 GLU K CB  1 
ATOM   11829 C  CG  . GLU K  1 100 ? 73.907  42.467  14.662  1.00 60.32 ? 100 GLU K CG  1 
ATOM   11830 C  CD  . GLU K  1 100 ? 73.411  41.624  15.834  1.00 60.46 ? 100 GLU K CD  1 
ATOM   11831 O  OE1 . GLU K  1 100 ? 72.175  41.477  15.987  1.00 58.02 ? 100 GLU K OE1 1 
ATOM   11832 O  OE2 . GLU K  1 100 ? 74.256  41.107  16.602  1.00 58.50 ? 100 GLU K OE2 1 
ATOM   11833 N  N   . ASP K  1 101 ? 73.678  45.697  12.622  1.00 52.65 ? 101 ASP K N   1 
ATOM   11834 C  CA  . ASP K  1 101 ? 74.667  46.497  11.921  1.00 51.57 ? 101 ASP K CA  1 
ATOM   11835 C  C   . ASP K  1 101 ? 75.706  46.990  12.901  1.00 52.64 ? 101 ASP K C   1 
ATOM   11836 O  O   . ASP K  1 101 ? 75.410  47.189  14.072  1.00 57.02 ? 101 ASP K O   1 
ATOM   11837 C  CB  . ASP K  1 101 ? 74.016  47.678  11.210  1.00 51.82 ? 101 ASP K CB  1 
ATOM   11838 C  CG  . ASP K  1 101 ? 74.897  48.251  10.126  1.00 49.02 ? 101 ASP K CG  1 
ATOM   11839 O  OD1 . ASP K  1 101 ? 75.803  49.047  10.454  1.00 53.54 ? 101 ASP K OD1 1 
ATOM   11840 O  OD2 . ASP K  1 101 ? 74.689  47.894  8.949   1.00 52.72 ? 101 ASP K OD2 1 
ATOM   11841 N  N   . SER K  1 102 ? 76.925  47.192  12.421  1.00 50.66 ? 102 SER K N   1 
ATOM   11842 C  CA  . SER K  1 102 ? 78.023  47.576  13.293  1.00 48.05 ? 102 SER K CA  1 
ATOM   11843 C  C   . SER K  1 102 ? 78.847  48.715  12.702  1.00 47.51 ? 102 SER K C   1 
ATOM   11844 O  O   . SER K  1 102 ? 80.016  48.908  13.056  1.00 46.44 ? 102 SER K O   1 
ATOM   11845 C  CB  . SER K  1 102 ? 78.902  46.364  13.597  1.00 52.17 ? 102 SER K CB  1 
ATOM   11846 O  OG  . SER K  1 102 ? 79.024  45.529  12.457  1.00 58.17 ? 102 SER K OG  1 
ATOM   11847 N  N   . VAL K  1 103 ? 78.233  49.471  11.798  1.00 48.26 ? 103 VAL K N   1 
ATOM   11848 C  CA  . VAL K  1 103 ? 78.878  50.670  11.268  1.00 55.45 ? 103 VAL K CA  1 
ATOM   11849 C  C   . VAL K  1 103 ? 78.061  51.917  11.636  1.00 51.66 ? 103 VAL K C   1 
ATOM   11850 O  O   . VAL K  1 103 ? 78.618  53.011  11.780  1.00 52.92 ? 103 VAL K O   1 
ATOM   11851 C  CB  . VAL K  1 103 ? 79.136  50.586  9.738   1.00 53.09 ? 103 VAL K CB  1 
ATOM   11852 C  CG1 . VAL K  1 103 ? 77.892  50.959  8.973   1.00 53.20 ? 103 VAL K CG1 1 
ATOM   11853 C  CG2 . VAL K  1 103 ? 80.284  51.504  9.336   1.00 53.26 ? 103 VAL K CG2 1 
ATOM   11854 N  N   . ILE K  1 104 ? 76.748  51.745  11.793  1.00 47.90 ? 104 ILE K N   1 
ATOM   11855 C  CA  . ILE K  1 104 ? 75.916  52.800  12.350  1.00 49.96 ? 104 ILE K CA  1 
ATOM   11856 C  C   . ILE K  1 104 ? 76.106  52.774  13.863  1.00 46.82 ? 104 ILE K C   1 
ATOM   11857 O  O   . ILE K  1 104 ? 76.419  51.725  14.421  1.00 46.86 ? 104 ILE K O   1 
ATOM   11858 C  CB  . ILE K  1 104 ? 74.425  52.610  12.008  1.00 46.73 ? 104 ILE K CB  1 
ATOM   11859 C  CG1 . ILE K  1 104 ? 73.921  51.258  12.512  1.00 47.84 ? 104 ILE K CG1 1 
ATOM   11860 C  CG2 . ILE K  1 104 ? 74.192  52.756  10.509  1.00 45.76 ? 104 ILE K CG2 1 
ATOM   11861 C  CD1 . ILE K  1 104 ? 72.416  51.155  12.547  1.00 40.12 ? 104 ILE K CD1 1 
ATOM   11862 N  N   . SER K  1 105 ? 75.941  53.918  14.522  1.00 44.48 ? 105 SER K N   1 
ATOM   11863 C  CA  . SER K  1 105 ? 76.094  53.982  15.981  1.00 44.53 ? 105 SER K CA  1 
ATOM   11864 C  C   . SER K  1 105 ? 75.068  54.925  16.591  1.00 41.71 ? 105 SER K C   1 
ATOM   11865 O  O   . SER K  1 105 ? 74.428  55.702  15.885  1.00 38.69 ? 105 SER K O   1 
ATOM   11866 C  CB  . SER K  1 105 ? 77.504  54.437  16.353  1.00 41.94 ? 105 SER K CB  1 
ATOM   11867 O  OG  . SER K  1 105 ? 77.779  54.212  17.726  1.00 48.23 ? 105 SER K OG  1 
ATOM   11868 N  N   . LEU K  1 106 ? 74.904  54.856  17.905  1.00 45.90 ? 106 LEU K N   1 
ATOM   11869 C  CA  . LEU K  1 106 ? 74.010  55.787  18.582  1.00 41.30 ? 106 LEU K CA  1 
ATOM   11870 C  C   . LEU K  1 106 ? 74.841  56.797  19.363  1.00 41.32 ? 106 LEU K C   1 
ATOM   11871 O  O   . LEU K  1 106 ? 74.333  57.496  20.238  1.00 46.09 ? 106 LEU K O   1 
ATOM   11872 C  CB  . LEU K  1 106 ? 72.997  55.060  19.477  1.00 40.02 ? 106 LEU K CB  1 
ATOM   11873 C  CG  . LEU K  1 106 ? 72.229  53.902  18.827  1.00 41.27 ? 106 LEU K CG  1 
ATOM   11874 C  CD1 . LEU K  1 106 ? 71.080  53.406  19.720  1.00 34.17 ? 106 LEU K CD1 1 
ATOM   11875 C  CD2 . LEU K  1 106 ? 71.738  54.283  17.437  1.00 37.73 ? 106 LEU K CD2 1 
ATOM   11876 N  N   . SER K  1 107 ? 76.125  56.868  19.030  1.00 36.57 ? 107 SER K N   1 
ATOM   11877 C  CA  . SER K  1 107 ? 77.018  57.886  19.578  1.00 42.58 ? 107 SER K CA  1 
ATOM   11878 C  C   . SER K  1 107 ? 78.227  58.050  18.670  1.00 46.17 ? 107 SER K C   1 
ATOM   11879 O  O   . SER K  1 107 ? 78.306  57.425  17.618  1.00 48.63 ? 107 SER K O   1 
ATOM   11880 C  CB  . SER K  1 107 ? 77.467  57.532  21.001  1.00 46.66 ? 107 SER K CB  1 
ATOM   11881 O  OG  . SER K  1 107 ? 77.976  56.205  21.076  1.00 45.19 ? 107 SER K OG  1 
ATOM   11882 N  N   . GLY K  1 108 ? 79.172  58.886  19.079  1.00 48.60 ? 108 GLY K N   1 
ATOM   11883 C  CA  . GLY K  1 108 ? 80.320  59.174  18.243  1.00 51.40 ? 108 GLY K CA  1 
ATOM   11884 C  C   . GLY K  1 108 ? 79.888  59.927  16.998  1.00 56.73 ? 108 GLY K C   1 
ATOM   11885 O  O   . GLY K  1 108 ? 78.915  60.679  17.032  1.00 52.62 ? 108 GLY K O   1 
ATOM   11886 N  N   . ASP K  1 109 ? 80.597  59.702  15.893  1.00 56.83 ? 109 ASP K N   1 
ATOM   11887 C  CA  . ASP K  1 109 ? 80.420  60.498  14.683  1.00 52.75 ? 109 ASP K CA  1 
ATOM   11888 C  C   . ASP K  1 109 ? 79.952  59.651  13.497  1.00 55.97 ? 109 ASP K C   1 
ATOM   11889 O  O   . ASP K  1 109 ? 80.021  60.074  12.340  1.00 53.59 ? 109 ASP K O   1 
ATOM   11890 C  CB  . ASP K  1 109 ? 81.724  61.214  14.347  1.00 57.52 ? 109 ASP K CB  1 
ATOM   11891 C  CG  . ASP K  1 109 ? 82.473  61.667  15.589  1.00 61.44 ? 109 ASP K CG  1 
ATOM   11892 O  OD1 . ASP K  1 109 ? 81.835  62.241  16.506  1.00 58.66 ? 109 ASP K OD1 1 
ATOM   11893 O  OD2 . ASP K  1 109 ? 83.700  61.433  15.650  1.00 62.10 ? 109 ASP K OD2 1 
ATOM   11894 N  N   . HIS K  1 110 ? 79.499  58.442  13.804  1.00 54.88 ? 110 HIS K N   1 
ATOM   11895 C  CA  . HIS K  1 110 ? 78.737  57.625  12.873  1.00 50.63 ? 110 HIS K CA  1 
ATOM   11896 C  C   . HIS K  1 110 ? 77.338  57.681  13.416  1.00 44.11 ? 110 HIS K C   1 
ATOM   11897 O  O   . HIS K  1 110 ? 76.471  56.887  13.045  1.00 43.17 ? 110 HIS K O   1 
ATOM   11898 C  CB  . HIS K  1 110 ? 79.212  56.169  12.902  1.00 53.05 ? 110 HIS K CB  1 
ATOM   11899 C  CG  . HIS K  1 110 ? 80.593  55.973  12.361  1.00 55.94 ? 110 HIS K CG  1 
ATOM   11900 N  ND1 . HIS K  1 110 ? 80.833  55.425  11.119  1.00 55.30 ? 110 HIS K ND1 1 
ATOM   11901 C  CD2 . HIS K  1 110 ? 81.806  56.264  12.886  1.00 57.45 ? 110 HIS K CD2 1 
ATOM   11902 C  CE1 . HIS K  1 110 ? 82.135  55.381  10.906  1.00 55.92 ? 110 HIS K CE1 1 
ATOM   11903 N  NE2 . HIS K  1 110 ? 82.748  55.886  11.961  1.00 55.82 ? 110 HIS K NE2 1 
ATOM   11904 N  N   . CYS K  1 111 ? 77.142  58.616  14.336  1.00 41.90 ? 111 CYS K N   1 
ATOM   11905 C  CA  . CYS K  1 111 ? 75.943  58.639  15.150  1.00 42.08 ? 111 CYS K CA  1 
ATOM   11906 C  C   . CYS K  1 111 ? 74.742  59.090  14.323  1.00 36.29 ? 111 CYS K C   1 
ATOM   11907 O  O   . CYS K  1 111 ? 74.796  60.120  13.661  1.00 37.93 ? 111 CYS K O   1 
ATOM   11908 C  CB  . CYS K  1 111 ? 76.174  59.525  16.378  1.00 41.93 ? 111 CYS K CB  1 
ATOM   11909 S  SG  . CYS K  1 111 ? 74.711  60.268  17.083  1.00 39.63 ? 111 CYS K SG  1 
ATOM   11910 N  N   . ILE K  1 112 ? 73.666  58.308  14.368  1.00 35.91 ? 112 ILE K N   1 
ATOM   11911 C  CA  . ILE K  1 112 ? 72.529  58.497  13.473  1.00 38.70 ? 112 ILE K CA  1 
ATOM   11912 C  C   . ILE K  1 112 ? 71.304  59.155  14.096  1.00 40.12 ? 112 ILE K C   1 
ATOM   11913 O  O   . ILE K  1 112 ? 70.279  59.324  13.422  1.00 39.93 ? 112 ILE K O   1 
ATOM   11914 C  CB  . ILE K  1 112 ? 72.057  57.158  12.891  1.00 43.71 ? 112 ILE K CB  1 
ATOM   11915 C  CG1 . ILE K  1 112 ? 71.591  56.227  14.017  1.00 39.34 ? 112 ILE K CG1 1 
ATOM   11916 C  CG2 . ILE K  1 112 ? 73.149  56.536  12.030  1.00 44.50 ? 112 ILE K CG2 1 
ATOM   11917 C  CD1 . ILE K  1 112 ? 70.908  54.961  13.512  1.00 43.69 ? 112 ILE K CD1 1 
ATOM   11918 N  N   . ILE K  1 113 ? 71.392  59.499  15.376  1.00 36.76 ? 113 ILE K N   1 
ATOM   11919 C  CA  . ILE K  1 113 ? 70.307  60.205  16.046  1.00 37.53 ? 113 ILE K CA  1 
ATOM   11920 C  C   . ILE K  1 113 ? 70.279  61.630  15.512  1.00 37.08 ? 113 ILE K C   1 
ATOM   11921 O  O   . ILE K  1 113 ? 71.326  62.265  15.387  1.00 33.28 ? 113 ILE K O   1 
ATOM   11922 C  CB  . ILE K  1 113 ? 70.472  60.156  17.588  1.00 42.09 ? 113 ILE K CB  1 
ATOM   11923 C  CG1 . ILE K  1 113 ? 69.776  58.911  18.143  1.00 38.00 ? 113 ILE K CG1 1 
ATOM   11924 C  CG2 . ILE K  1 113 ? 69.941  61.418  18.254  1.00 37.19 ? 113 ILE K CG2 1 
ATOM   11925 C  CD1 . ILE K  1 113 ? 70.457  58.335  19.344  1.00 38.28 ? 113 ILE K CD1 1 
ATOM   11926 N  N   . GLY K  1 114 ? 69.087  62.110  15.158  1.00 36.24 ? 114 GLY K N   1 
ATOM   11927 C  CA  . GLY K  1 114 ? 68.938  63.421  14.542  1.00 39.08 ? 114 GLY K CA  1 
ATOM   11928 C  C   . GLY K  1 114 ? 69.041  63.394  13.022  1.00 39.56 ? 114 GLY K C   1 
ATOM   11929 O  O   . GLY K  1 114 ? 68.967  64.440  12.357  1.00 34.74 ? 114 GLY K O   1 
ATOM   11930 N  N   . ARG K  1 115 ? 69.216  62.190  12.478  1.00 37.91 ? 115 ARG K N   1 
ATOM   11931 C  CA  . ARG K  1 115 ? 69.269  61.981  11.032  1.00 40.24 ? 115 ARG K CA  1 
ATOM   11932 C  C   . ARG K  1 115 ? 67.991  61.322  10.524  1.00 40.90 ? 115 ARG K C   1 
ATOM   11933 O  O   . ARG K  1 115 ? 67.102  60.970  11.306  1.00 38.36 ? 115 ARG K O   1 
ATOM   11934 C  CB  . ARG K  1 115 ? 70.487  61.143  10.663  1.00 33.23 ? 115 ARG K CB  1 
ATOM   11935 C  CG  . ARG K  1 115 ? 71.707  61.595  11.406  1.00 35.55 ? 115 ARG K CG  1 
ATOM   11936 C  CD  . ARG K  1 115 ? 72.949  61.428  10.605  1.00 38.12 ? 115 ARG K CD  1 
ATOM   11937 N  NE  . ARG K  1 115 ? 74.044  62.154  11.231  1.00 36.06 ? 115 ARG K NE  1 
ATOM   11938 C  CZ  . ARG K  1 115 ? 74.520  63.312  10.790  1.00 34.70 ? 115 ARG K CZ  1 
ATOM   11939 N  NH1 . ARG K  1 115 ? 74.011  63.879  9.698   1.00 36.19 ? 115 ARG K NH1 1 
ATOM   11940 N  NH2 . ARG K  1 115 ? 75.515  63.894  11.434  1.00 31.16 ? 115 ARG K NH2 1 
ATOM   11941 N  N   . THR K  1 116 ? 67.901  61.150  9.209   1.00 41.44 ? 116 THR K N   1 
ATOM   11942 C  CA  . THR K  1 116 ? 66.653  60.680  8.617   1.00 42.87 ? 116 THR K CA  1 
ATOM   11943 C  C   . THR K  1 116 ? 66.684  59.249  8.082   1.00 43.39 ? 116 THR K C   1 
ATOM   11944 O  O   . THR K  1 116 ? 67.535  58.887  7.261   1.00 41.25 ? 116 THR K O   1 
ATOM   11945 C  CB  . THR K  1 116 ? 66.160  61.630  7.521   1.00 40.48 ? 116 THR K CB  1 
ATOM   11946 O  OG1 . THR K  1 116 ? 65.808  62.887  8.109   1.00 31.53 ? 116 THR K OG1 1 
ATOM   11947 C  CG2 . THR K  1 116 ? 64.938  61.052  6.845   1.00 47.67 ? 116 THR K CG2 1 
ATOM   11948 N  N   . LEU K  1 117 ? 65.738  58.448  8.566   1.00 44.48 ? 117 LEU K N   1 
ATOM   11949 C  CA  . LEU K  1 117 ? 65.539  57.095  8.079   1.00 50.74 ? 117 LEU K CA  1 
ATOM   11950 C  C   . LEU K  1 117 ? 64.543  57.103  6.920   1.00 56.03 ? 117 LEU K C   1 
ATOM   11951 O  O   . LEU K  1 117 ? 63.351  57.363  7.116   1.00 54.07 ? 117 LEU K O   1 
ATOM   11952 C  CB  . LEU K  1 117 ? 65.025  56.190  9.200   1.00 45.44 ? 117 LEU K CB  1 
ATOM   11953 C  CG  . LEU K  1 117 ? 64.970  54.702  8.840   1.00 52.92 ? 117 LEU K CG  1 
ATOM   11954 C  CD1 . LEU K  1 117 ? 66.323  54.194  8.347   1.00 48.27 ? 117 LEU K CD1 1 
ATOM   11955 C  CD2 . LEU K  1 117 ? 64.497  53.892  10.021  1.00 52.27 ? 117 LEU K CD2 1 
ATOM   11956 N  N   . VAL K  1 118 ? 65.039  56.820  5.718   1.00 55.23 ? 118 VAL K N   1 
ATOM   11957 C  CA  . VAL K  1 118 ? 64.197  56.774  4.522   1.00 56.36 ? 118 VAL K CA  1 
ATOM   11958 C  C   . VAL K  1 118 ? 64.003  55.351  3.983   1.00 58.07 ? 118 VAL K C   1 
ATOM   11959 O  O   . VAL K  1 118 ? 64.970  54.650  3.695   1.00 59.87 ? 118 VAL K O   1 
ATOM   11960 C  CB  . VAL K  1 118 ? 64.787  57.656  3.395   1.00 57.18 ? 118 VAL K CB  1 
ATOM   11961 C  CG1 . VAL K  1 118 ? 64.227  57.253  2.045   1.00 55.50 ? 118 VAL K CG1 1 
ATOM   11962 C  CG2 . VAL K  1 118 ? 64.531  59.132  3.676   1.00 55.99 ? 118 VAL K CG2 1 
ATOM   11963 N  N   . VAL K  1 119 ? 62.752  54.924  3.856   1.00 58.84 ? 119 VAL K N   1 
ATOM   11964 C  CA  . VAL K  1 119 ? 62.456  53.691  3.137   1.00 61.94 ? 119 VAL K CA  1 
ATOM   11965 C  C   . VAL K  1 119 ? 61.995  54.040  1.727   1.00 63.50 ? 119 VAL K C   1 
ATOM   11966 O  O   . VAL K  1 119 ? 61.116  54.885  1.551   1.00 65.87 ? 119 VAL K O   1 
ATOM   11967 C  CB  . VAL K  1 119 ? 61.381  52.848  3.848   1.00 63.14 ? 119 VAL K CB  1 
ATOM   11968 C  CG1 . VAL K  1 119 ? 60.241  53.734  4.326   1.00 61.69 ? 119 VAL K CG1 1 
ATOM   11969 C  CG2 . VAL K  1 119 ? 60.882  51.731  2.928   1.00 62.50 ? 119 VAL K CG2 1 
ATOM   11970 N  N   . HIS K  1 120 ? 62.585  53.400  0.722   1.00 59.54 ? 120 HIS K N   1 
ATOM   11971 C  CA  . HIS K  1 120 ? 62.314  53.777  -0.668  1.00 64.71 ? 120 HIS K CA  1 
ATOM   11972 C  C   . HIS K  1 120 ? 61.203  53.009  -1.398  1.00 67.77 ? 120 HIS K C   1 
ATOM   11973 O  O   . HIS K  1 120 ? 60.622  52.061  -0.863  1.00 68.96 ? 120 HIS K O   1 
ATOM   11974 C  CB  . HIS K  1 120 ? 63.592  53.716  -1.491  1.00 61.36 ? 120 HIS K CB  1 
ATOM   11975 C  CG  . HIS K  1 120 ? 64.572  54.792  -1.157  1.00 58.04 ? 120 HIS K CG  1 
ATOM   11976 N  ND1 . HIS K  1 120 ? 64.517  56.046  -1.723  1.00 57.12 ? 120 HIS K ND1 1 
ATOM   11977 C  CD2 . HIS K  1 120 ? 65.635  54.801  -0.321  1.00 60.19 ? 120 HIS K CD2 1 
ATOM   11978 C  CE1 . HIS K  1 120 ? 65.507  56.782  -1.253  1.00 55.90 ? 120 HIS K CE1 1 
ATOM   11979 N  NE2 . HIS K  1 120 ? 66.198  56.051  -0.398  1.00 57.06 ? 120 HIS K NE2 1 
ATOM   11980 N  N   . GLU K  1 121 ? 60.928  53.447  -2.630  1.00 65.78 ? 121 GLU K N   1 
ATOM   11981 C  CA  . GLU K  1 121 ? 59.912  52.857  -3.504  1.00 65.24 ? 121 GLU K CA  1 
ATOM   11982 C  C   . GLU K  1 121 ? 60.339  51.495  -4.041  1.00 62.02 ? 121 GLU K C   1 
ATOM   11983 O  O   . GLU K  1 121 ? 59.734  50.468  -3.739  1.00 59.06 ? 121 GLU K O   1 
ATOM   11984 C  CB  . GLU K  1 121 ? 59.642  53.795  -4.688  1.00 67.93 ? 121 GLU K CB  1 
ATOM   11985 C  CG  . GLU K  1 121 ? 58.714  53.224  -5.764  1.00 67.39 ? 121 GLU K CG  1 
ATOM   11986 C  CD  . GLU K  1 121 ? 58.736  54.027  -7.066  1.00 69.69 ? 121 GLU K CD  1 
ATOM   11987 O  OE1 . GLU K  1 121 ? 59.682  54.820  -7.271  1.00 64.06 ? 121 GLU K OE1 1 
ATOM   11988 O  OE2 . GLU K  1 121 ? 57.807  53.860  -7.889  1.00 78.20 ? 121 GLU K OE2 1 
ATOM   11989 N  N   . LYS K  1 122 ? 61.389  51.503  -4.850  1.00 63.42 ? 122 LYS K N   1 
ATOM   11990 C  CA  . LYS K  1 122 ? 61.868  50.290  -5.495  1.00 66.27 ? 122 LYS K CA  1 
ATOM   11991 C  C   . LYS K  1 122 ? 62.787  49.535  -4.549  1.00 64.93 ? 122 LYS K C   1 
ATOM   11992 O  O   . LYS K  1 122 ? 62.599  49.562  -3.339  1.00 63.34 ? 122 LYS K O   1 
ATOM   11993 C  CB  . LYS K  1 122 ? 62.609  50.643  -6.789  1.00 62.43 ? 122 LYS K CB  1 
ATOM   11994 C  CG  . LYS K  1 122 ? 61.843  51.602  -7.690  1.00 60.30 ? 122 LYS K CG  1 
ATOM   11995 C  CD  . LYS K  1 122 ? 62.673  52.049  -8.885  1.00 67.37 ? 122 LYS K CD  1 
ATOM   11996 C  CE  . LYS K  1 122 ? 61.893  53.031  -9.760  1.00 69.35 ? 122 LYS K CE  1 
ATOM   11997 N  NZ  . LYS K  1 122 ? 62.695  53.563  -10.899 1.00 64.37 ? 122 LYS K NZ  1 
ATOM   11998 N  N   . ALA K  1 123 ? 63.787  48.869  -5.108  1.00 62.70 ? 123 ALA K N   1 
ATOM   11999 C  CA  . ALA K  1 123 ? 64.798  48.222  -4.298  1.00 59.47 ? 123 ALA K CA  1 
ATOM   12000 C  C   . ALA K  1 123 ? 66.128  48.927  -4.477  1.00 61.98 ? 123 ALA K C   1 
ATOM   12001 O  O   . ALA K  1 123 ? 66.449  49.401  -5.563  1.00 59.88 ? 123 ALA K O   1 
ATOM   12002 C  CB  . ALA K  1 123 ? 64.927  46.760  -4.677  1.00 64.44 ? 123 ALA K CB  1 
ATOM   12003 N  N   . ASP K  1 124 ? 66.878  49.016  -3.386  1.00 64.05 ? 124 ASP K N   1 
ATOM   12004 C  CA  . ASP K  1 124 ? 68.285  49.389  -3.422  1.00 64.63 ? 124 ASP K CA  1 
ATOM   12005 C  C   . ASP K  1 124 ? 68.963  48.345  -4.310  1.00 65.53 ? 124 ASP K C   1 
ATOM   12006 O  O   . ASP K  1 124 ? 68.679  47.148  -4.179  1.00 67.13 ? 124 ASP K O   1 
ATOM   12007 C  CB  . ASP K  1 124 ? 68.848  49.310  -1.992  1.00 61.12 ? 124 ASP K CB  1 
ATOM   12008 C  CG  . ASP K  1 124 ? 70.138  50.084  -1.812  1.00 60.90 ? 124 ASP K CG  1 
ATOM   12009 O  OD1 . ASP K  1 124 ? 70.664  50.632  -2.801  1.00 62.24 ? 124 ASP K OD1 1 
ATOM   12010 O  OD2 . ASP K  1 124 ? 70.633  50.132  -0.667  1.00 61.70 ? 124 ASP K OD2 1 
ATOM   12011 N  N   . ASP K  1 125 ? 69.835  48.769  -5.223  1.00 65.62 ? 125 ASP K N   1 
ATOM   12012 C  CA  . ASP K  1 125 ? 70.524  47.787  -6.068  1.00 65.88 ? 125 ASP K CA  1 
ATOM   12013 C  C   . ASP K  1 125 ? 71.884  47.363  -5.496  1.00 65.08 ? 125 ASP K C   1 
ATOM   12014 O  O   . ASP K  1 125 ? 72.608  46.572  -6.101  1.00 64.53 ? 125 ASP K O   1 
ATOM   12015 C  CB  . ASP K  1 125 ? 70.599  48.242  -7.535  1.00 61.46 ? 125 ASP K CB  1 
ATOM   12016 C  CG  . ASP K  1 125 ? 71.603  49.358  -7.774  1.00 65.25 ? 125 ASP K CG  1 
ATOM   12017 O  OD1 . ASP K  1 125 ? 72.301  49.787  -6.834  1.00 68.34 ? 125 ASP K OD1 1 
ATOM   12018 O  OD2 . ASP K  1 125 ? 71.713  49.808  -8.934  1.00 68.12 ? 125 ASP K OD2 1 
ATOM   12019 N  N   . LEU K  1 126 ? 72.203  47.912  -4.324  1.00 65.80 ? 126 LEU K N   1 
ATOM   12020 C  CA  . LEU K  1 126 ? 73.382  47.548  -3.527  1.00 62.02 ? 126 LEU K CA  1 
ATOM   12021 C  C   . LEU K  1 126 ? 74.739  47.886  -4.149  1.00 63.55 ? 126 LEU K C   1 
ATOM   12022 O  O   . LEU K  1 126 ? 75.760  47.344  -3.730  1.00 67.64 ? 126 LEU K O   1 
ATOM   12023 C  CB  . LEU K  1 126 ? 73.343  46.074  -3.092  1.00 61.28 ? 126 LEU K CB  1 
ATOM   12024 C  CG  . LEU K  1 126 ? 72.271  45.641  -2.082  1.00 65.53 ? 126 LEU K CG  1 
ATOM   12025 C  CD1 . LEU K  1 126 ? 70.915  45.454  -2.746  1.00 61.49 ? 126 LEU K CD1 1 
ATOM   12026 C  CD2 . LEU K  1 126 ? 72.690  44.371  -1.352  1.00 63.22 ? 126 LEU K CD2 1 
ATOM   12027 N  N   . GLY K  1 127 ? 74.755  48.779  -5.135  1.00 65.77 ? 127 GLY K N   1 
ATOM   12028 C  CA  . GLY K  1 127 ? 76.009  49.248  -5.710  1.00 67.42 ? 127 GLY K CA  1 
ATOM   12029 C  C   . GLY K  1 127 ? 76.484  48.455  -6.916  1.00 65.62 ? 127 GLY K C   1 
ATOM   12030 O  O   . GLY K  1 127 ? 77.473  48.808  -7.559  1.00 64.11 ? 127 GLY K O   1 
ATOM   12031 N  N   . LYS K  1 128 ? 75.772  47.375  -7.215  1.00 66.52 ? 128 LYS K N   1 
ATOM   12032 C  CA  . LYS K  1 128 ? 76.112  46.503  -8.330  1.00 67.00 ? 128 LYS K CA  1 
ATOM   12033 C  C   . LYS K  1 128 ? 75.045  46.616  -9.417  1.00 67.11 ? 128 LYS K C   1 
ATOM   12034 O  O   . LYS K  1 128 ? 74.405  45.632  -9.784  1.00 66.31 ? 128 LYS K O   1 
ATOM   12035 C  CB  . LYS K  1 128 ? 76.224  45.053  -7.850  1.00 68.50 ? 128 LYS K CB  1 
ATOM   12036 C  CG  . LYS K  1 128 ? 77.199  44.832  -6.695  1.00 70.33 ? 128 LYS K CG  1 
ATOM   12037 C  CD  . LYS K  1 128 ? 78.640  45.069  -7.122  1.00 67.61 ? 128 LYS K CD  1 
ATOM   12038 C  CE  . LYS K  1 128 ? 79.628  44.625  -6.043  1.00 69.22 ? 128 LYS K CE  1 
ATOM   12039 N  NZ  . LYS K  1 128 ? 79.496  45.414  -4.785  1.00 70.73 ? 128 LYS K NZ  1 
ATOM   12040 N  N   . GLY K  1 129 ? 74.847  47.829  -9.918  1.00 69.57 ? 129 GLY K N   1 
ATOM   12041 C  CA  . GLY K  1 129 ? 73.865  48.073  -10.956 1.00 68.29 ? 129 GLY K CA  1 
ATOM   12042 C  C   . GLY K  1 129 ? 74.542  48.560  -12.216 1.00 69.79 ? 129 GLY K C   1 
ATOM   12043 O  O   . GLY K  1 129 ? 73.890  48.784  -13.232 1.00 71.87 ? 129 GLY K O   1 
ATOM   12044 N  N   . GLY K  1 130 ? 75.859  48.737  -12.137 1.00 73.21 ? 130 GLY K N   1 
ATOM   12045 C  CA  . GLY K  1 130 ? 76.662  49.133  -13.283 1.00 72.36 ? 130 GLY K CA  1 
ATOM   12046 C  C   . GLY K  1 130 ? 76.592  50.608  -13.639 1.00 76.62 ? 130 GLY K C   1 
ATOM   12047 O  O   . GLY K  1 130 ? 77.611  51.229  -13.953 1.00 78.97 ? 130 GLY K O   1 
ATOM   12048 N  N   . ASN K  1 131 ? 75.388  51.171  -13.595 1.00 77.04 ? 131 ASN K N   1 
ATOM   12049 C  CA  . ASN K  1 131 ? 75.180  52.571  -13.954 1.00 79.54 ? 131 ASN K CA  1 
ATOM   12050 C  C   . ASN K  1 131 ? 75.913  53.574  -13.050 1.00 81.51 ? 131 ASN K C   1 
ATOM   12051 O  O   . ASN K  1 131 ? 76.576  53.196  -12.079 1.00 78.45 ? 131 ASN K O   1 
ATOM   12052 C  CB  . ASN K  1 131 ? 73.679  52.893  -14.029 1.00 77.96 ? 131 ASN K CB  1 
ATOM   12053 C  CG  . ASN K  1 131 ? 72.951  52.655  -12.710 1.00 72.55 ? 131 ASN K CG  1 
ATOM   12054 O  OD1 . ASN K  1 131 ? 73.432  53.030  -11.641 1.00 72.10 ? 131 ASN K OD1 1 
ATOM   12055 N  ND2 . ASN K  1 131 ? 71.780  52.031  -12.788 1.00 68.43 ? 131 ASN K ND2 1 
ATOM   12056 N  N   . GLU K  1 132 ? 75.776  54.856  -13.375 1.00 81.06 ? 132 GLU K N   1 
ATOM   12057 C  CA  . GLU K  1 132 ? 76.483  55.918  -12.665 1.00 79.59 ? 132 GLU K CA  1 
ATOM   12058 C  C   . GLU K  1 132 ? 75.760  56.354  -11.387 1.00 76.72 ? 132 GLU K C   1 
ATOM   12059 O  O   . GLU K  1 132 ? 76.249  57.217  -10.651 1.00 75.55 ? 132 GLU K O   1 
ATOM   12060 C  CB  . GLU K  1 132 ? 76.693  57.123  -13.593 1.00 81.83 ? 132 GLU K CB  1 
ATOM   12061 C  CG  . GLU K  1 132 ? 77.481  56.819  -14.876 1.00 86.24 ? 132 GLU K CG  1 
ATOM   12062 C  CD  . GLU K  1 132 ? 76.625  56.222  -15.993 1.00 86.81 ? 132 GLU K CD  1 
ATOM   12063 O  OE1 . GLU K  1 132 ? 75.431  56.580  -16.095 1.00 87.33 ? 132 GLU K OE1 1 
ATOM   12064 O  OE2 . GLU K  1 132 ? 77.150  55.394  -16.770 1.00 80.53 ? 132 GLU K OE2 1 
ATOM   12065 N  N   . GLU K  1 133 ? 74.599  55.756  -11.129 1.00 74.27 ? 133 GLU K N   1 
ATOM   12066 C  CA  . GLU K  1 133 ? 73.778  56.119  -9.973  1.00 72.94 ? 133 GLU K CA  1 
ATOM   12067 C  C   . GLU K  1 133 ? 73.868  55.098  -8.843  1.00 71.81 ? 133 GLU K C   1 
ATOM   12068 O  O   . GLU K  1 133 ? 73.660  55.434  -7.674  1.00 69.13 ? 133 GLU K O   1 
ATOM   12069 C  CB  . GLU K  1 133 ? 72.309  56.308  -10.375 1.00 69.19 ? 133 GLU K CB  1 
ATOM   12070 C  CG  . GLU K  1 133 ? 71.939  57.719  -10.827 1.00 71.90 ? 133 GLU K CG  1 
ATOM   12071 C  CD  . GLU K  1 133 ? 72.048  58.757  -9.713  1.00 69.86 ? 133 GLU K CD  1 
ATOM   12072 O  OE1 . GLU K  1 133 ? 71.136  58.823  -8.862  1.00 59.73 ? 133 GLU K OE1 1 
ATOM   12073 O  OE2 . GLU K  1 133 ? 73.046  59.513  -9.694  1.00 73.46 ? 133 GLU K OE2 1 
ATOM   12074 N  N   . SER K  1 134 ? 74.166  53.851  -9.189  1.00 72.39 ? 134 SER K N   1 
ATOM   12075 C  CA  . SER K  1 134 ? 74.228  52.795  -8.187  1.00 71.66 ? 134 SER K CA  1 
ATOM   12076 C  C   . SER K  1 134 ? 75.380  53.044  -7.219  1.00 66.50 ? 134 SER K C   1 
ATOM   12077 O  O   . SER K  1 134 ? 75.367  52.567  -6.086  1.00 63.84 ? 134 SER K O   1 
ATOM   12078 C  CB  . SER K  1 134 ? 74.380  51.429  -8.850  1.00 70.14 ? 134 SER K CB  1 
ATOM   12079 O  OG  . SER K  1 134 ? 74.256  50.396  -7.891  1.00 66.95 ? 134 SER K OG  1 
ATOM   12080 N  N   . THR K  1 135 ? 76.366  53.806  -7.678  1.00 65.10 ? 135 THR K N   1 
ATOM   12081 C  CA  . THR K  1 135 ? 77.518  54.165  -6.865  1.00 63.90 ? 135 THR K CA  1 
ATOM   12082 C  C   . THR K  1 135 ? 77.236  55.416  -6.031  1.00 63.50 ? 135 THR K C   1 
ATOM   12083 O  O   . THR K  1 135 ? 78.146  56.009  -5.449  1.00 61.26 ? 135 THR K O   1 
ATOM   12084 C  CB  . THR K  1 135 ? 78.728  54.436  -7.754  1.00 62.33 ? 135 THR K CB  1 
ATOM   12085 O  OG1 . THR K  1 135 ? 78.574  55.710  -8.391  1.00 65.83 ? 135 THR K OG1 1 
ATOM   12086 C  CG2 . THR K  1 135 ? 78.849  53.351  -8.811  1.00 62.14 ? 135 THR K CG2 1 
ATOM   12087 N  N   . LYS K  1 136 ? 75.969  55.813  -5.983  1.00 63.57 ? 136 LYS K N   1 
ATOM   12088 C  CA  . LYS K  1 136 ? 75.557  57.008  -5.257  1.00 64.47 ? 136 LYS K CA  1 
ATOM   12089 C  C   . LYS K  1 136 ? 74.320  56.735  -4.401  1.00 63.57 ? 136 LYS K C   1 
ATOM   12090 O  O   . LYS K  1 136 ? 74.328  56.961  -3.189  1.00 58.17 ? 136 LYS K O   1 
ATOM   12091 C  CB  . LYS K  1 136 ? 75.271  58.155  -6.233  1.00 65.08 ? 136 LYS K CB  1 
ATOM   12092 C  CG  . LYS K  1 136 ? 76.497  58.679  -6.973  1.00 68.13 ? 136 LYS K CG  1 
ATOM   12093 C  CD  . LYS K  1 136 ? 76.088  59.558  -8.150  1.00 69.82 ? 136 LYS K CD  1 
ATOM   12094 C  CE  . LYS K  1 136 ? 77.254  60.382  -8.667  1.00 67.90 ? 136 LYS K CE  1 
ATOM   12095 N  NZ  . LYS K  1 136 ? 77.739  61.343  -7.634  1.00 67.30 ? 136 LYS K NZ  1 
ATOM   12096 N  N   . THR K  1 137 ? 73.265  56.237  -5.038  1.00 61.60 ? 137 THR K N   1 
ATOM   12097 C  CA  . THR K  1 137 ? 71.980  56.060  -4.374  1.00 60.95 ? 137 THR K CA  1 
ATOM   12098 C  C   . THR K  1 137 ? 71.504  54.605  -4.355  1.00 59.87 ? 137 THR K C   1 
ATOM   12099 O  O   . THR K  1 137 ? 70.705  54.214  -3.501  1.00 55.99 ? 137 THR K O   1 
ATOM   12100 C  CB  . THR K  1 137 ? 70.900  56.930  -5.042  1.00 61.19 ? 137 THR K CB  1 
ATOM   12101 O  OG1 . THR K  1 137 ? 70.684  56.473  -6.382  1.00 65.49 ? 137 THR K OG1 1 
ATOM   12102 C  CG2 . THR K  1 137 ? 71.336  58.389  -5.076  1.00 59.47 ? 137 THR K CG2 1 
ATOM   12103 N  N   . GLY K  1 138 ? 71.988  53.808  -5.303  1.00 63.59 ? 138 GLY K N   1 
ATOM   12104 C  CA  . GLY K  1 138 ? 71.584  52.416  -5.390  1.00 64.16 ? 138 GLY K CA  1 
ATOM   12105 C  C   . GLY K  1 138 ? 70.282  52.197  -6.147  1.00 63.39 ? 138 GLY K C   1 
ATOM   12106 O  O   . GLY K  1 138 ? 69.753  51.083  -6.171  1.00 62.76 ? 138 GLY K O   1 
ATOM   12107 N  N   . ASN K  1 139 ? 69.764  53.268  -6.751  1.00 64.98 ? 139 ASN K N   1 
ATOM   12108 C  CA  . ASN K  1 139 ? 68.578  53.210  -7.617  1.00 68.33 ? 139 ASN K CA  1 
ATOM   12109 C  C   . ASN K  1 139 ? 67.329  52.618  -6.959  1.00 67.16 ? 139 ASN K C   1 
ATOM   12110 O  O   . ASN K  1 139 ? 66.752  51.651  -7.463  1.00 65.33 ? 139 ASN K O   1 
ATOM   12111 C  CB  . ASN K  1 139 ? 68.889  52.457  -8.924  1.00 64.57 ? 139 ASN K CB  1 
ATOM   12112 C  CG  . ASN K  1 139 ? 70.068  53.048  -9.671  1.00 65.94 ? 139 ASN K CG  1 
ATOM   12113 O  OD1 . ASN K  1 139 ? 69.988  54.157  -10.195 1.00 70.68 ? 139 ASN K OD1 1 
ATOM   12114 N  ND2 . ASN K  1 139 ? 71.172  52.307  -9.729  1.00 66.50 ? 139 ASN K ND2 1 
ATOM   12115 N  N   . ALA K  1 140 ? 66.902  53.206  -5.845  1.00 65.49 ? 140 ALA K N   1 
ATOM   12116 C  CA  . ALA K  1 140 ? 65.783  52.647  -5.095  1.00 61.35 ? 140 ALA K CA  1 
ATOM   12117 C  C   . ALA K  1 140 ? 64.484  53.429  -5.280  1.00 60.49 ? 140 ALA K C   1 
ATOM   12118 O  O   . ALA K  1 140 ? 63.465  53.097  -4.679  1.00 62.79 ? 140 ALA K O   1 
ATOM   12119 C  CB  . ALA K  1 140 ? 66.141  52.525  -3.621  1.00 60.89 ? 140 ALA K CB  1 
ATOM   12120 N  N   . GLY K  1 141 ? 64.518  54.465  -6.111  1.00 61.80 ? 141 GLY K N   1 
ATOM   12121 C  CA  . GLY K  1 141 ? 63.309  55.202  -6.438  1.00 64.28 ? 141 GLY K CA  1 
ATOM   12122 C  C   . GLY K  1 141 ? 62.917  56.306  -5.469  1.00 62.14 ? 141 GLY K C   1 
ATOM   12123 O  O   . GLY K  1 141 ? 63.768  56.999  -4.910  1.00 62.65 ? 141 GLY K O   1 
ATOM   12124 N  N   . SER K  1 142 ? 61.613  56.471  -5.278  1.00 62.15 ? 142 SER K N   1 
ATOM   12125 C  CA  . SER K  1 142 ? 61.081  57.543  -4.437  1.00 67.28 ? 142 SER K CA  1 
ATOM   12126 C  C   . SER K  1 142 ? 61.158  57.229  -2.941  1.00 65.58 ? 142 SER K C   1 
ATOM   12127 O  O   . SER K  1 142 ? 61.087  56.068  -2.536  1.00 64.71 ? 142 SER K O   1 
ATOM   12128 C  CB  . SER K  1 142 ? 59.627  57.852  -4.820  1.00 66.36 ? 142 SER K CB  1 
ATOM   12129 O  OG  . SER K  1 142 ? 59.545  58.511  -6.076  1.00 68.68 ? 142 SER K OG  1 
ATOM   12130 N  N   . ARG K  1 143 ? 61.300  58.273  -2.128  1.00 61.93 ? 143 ARG K N   1 
ATOM   12131 C  CA  . ARG K  1 143 ? 61.205  58.139  -0.677  1.00 60.19 ? 143 ARG K CA  1 
ATOM   12132 C  C   . ARG K  1 143 ? 59.728  58.099  -0.280  1.00 60.46 ? 143 ARG K C   1 
ATOM   12133 O  O   . ARG K  1 143 ? 59.002  59.081  -0.444  1.00 60.94 ? 143 ARG K O   1 
ATOM   12134 C  CB  . ARG K  1 143 ? 61.924  59.297  0.017   1.00 52.04 ? 143 ARG K CB  1 
ATOM   12135 C  CG  . ARG K  1 143 ? 63.345  59.499  -0.469  1.00 51.51 ? 143 ARG K CG  1 
ATOM   12136 C  CD  . ARG K  1 143 ? 63.912  60.849  -0.072  1.00 49.09 ? 143 ARG K CD  1 
ATOM   12137 N  NE  . ARG K  1 143 ? 65.201  61.081  -0.716  1.00 45.44 ? 143 ARG K NE  1 
ATOM   12138 C  CZ  . ARG K  1 143 ? 65.963  62.158  -0.524  1.00 50.14 ? 143 ARG K CZ  1 
ATOM   12139 N  NH1 . ARG K  1 143 ? 65.565  63.118  0.303   1.00 51.40 ? 143 ARG K NH1 1 
ATOM   12140 N  NH2 . ARG K  1 143 ? 67.127  62.279  -1.160  1.00 45.94 ? 143 ARG K NH2 1 
ATOM   12141 N  N   . LEU K  1 144 ? 59.284  56.953  0.225   1.00 62.91 ? 144 LEU K N   1 
ATOM   12142 C  CA  . LEU K  1 144 ? 57.867  56.739  0.500   1.00 63.15 ? 144 LEU K CA  1 
ATOM   12143 C  C   . LEU K  1 144 ? 57.468  57.316  1.847   1.00 61.05 ? 144 LEU K C   1 
ATOM   12144 O  O   . LEU K  1 144 ? 56.568  58.148  1.926   1.00 63.78 ? 144 LEU K O   1 
ATOM   12145 C  CB  . LEU K  1 144 ? 57.522  55.248  0.425   1.00 65.59 ? 144 LEU K CB  1 
ATOM   12146 C  CG  . LEU K  1 144 ? 57.707  54.603  -0.954  1.00 65.67 ? 144 LEU K CG  1 
ATOM   12147 C  CD1 . LEU K  1 144 ? 57.576  53.102  -0.849  1.00 66.29 ? 144 LEU K CD1 1 
ATOM   12148 C  CD2 . LEU K  1 144 ? 56.710  55.153  -1.965  1.00 58.67 ? 144 LEU K CD2 1 
ATOM   12149 N  N   . ALA K  1 145 ? 58.143  56.871  2.902   1.00 63.45 ? 145 ALA K N   1 
ATOM   12150 C  CA  . ALA K  1 145 ? 57.901  57.385  4.250   1.00 64.68 ? 145 ALA K CA  1 
ATOM   12151 C  C   . ALA K  1 145 ? 59.200  57.850  4.906   1.00 64.54 ? 145 ALA K C   1 
ATOM   12152 O  O   . ALA K  1 145 ? 60.286  57.334  4.614   1.00 61.06 ? 145 ALA K O   1 
ATOM   12153 C  CB  . ALA K  1 145 ? 57.206  56.341  5.116   1.00 62.77 ? 145 ALA K CB  1 
ATOM   12154 N  N   . CYS K  1 146 ? 59.077  58.819  5.806   1.00 63.94 ? 146 CYS K N   1 
ATOM   12155 C  CA  . CYS K  1 146 ? 60.240  59.489  6.366   1.00 60.71 ? 146 CYS K CA  1 
ATOM   12156 C  C   . CYS K  1 146 ? 60.178  59.533  7.881   1.00 56.98 ? 146 CYS K C   1 
ATOM   12157 O  O   . CYS K  1 146 ? 59.106  59.424  8.470   1.00 58.58 ? 146 CYS K O   1 
ATOM   12158 C  CB  . CYS K  1 146 ? 60.312  60.917  5.831   1.00 58.65 ? 146 CYS K CB  1 
ATOM   12159 S  SG  . CYS K  1 146 ? 61.908  61.348  5.179   1.00 69.25 ? 146 CYS K SG  1 
ATOM   12160 N  N   . GLY K  1 147 ? 61.331  59.709  8.509   1.00 50.14 ? 147 GLY K N   1 
ATOM   12161 C  CA  . GLY K  1 147 ? 61.370  59.890  9.944   1.00 47.04 ? 147 GLY K CA  1 
ATOM   12162 C  C   . GLY K  1 147 ? 62.724  60.360  10.418  1.00 47.10 ? 147 GLY K C   1 
ATOM   12163 O  O   . GLY K  1 147 ? 63.750  60.091  9.786   1.00 44.01 ? 147 GLY K O   1 
ATOM   12164 N  N   . VAL K  1 148 ? 62.727  61.073  11.537  1.00 44.77 ? 148 VAL K N   1 
ATOM   12165 C  CA  . VAL K  1 148 ? 63.976  61.505  12.152  1.00 44.24 ? 148 VAL K CA  1 
ATOM   12166 C  C   . VAL K  1 148 ? 64.287  60.550  13.307  1.00 41.15 ? 148 VAL K C   1 
ATOM   12167 O  O   . VAL K  1 148 ? 63.403  60.237  14.104  1.00 43.07 ? 148 VAL K O   1 
ATOM   12168 C  CB  . VAL K  1 148 ? 63.876  62.978  12.636  1.00 40.29 ? 148 VAL K CB  1 
ATOM   12169 C  CG1 . VAL K  1 148 ? 65.178  63.429  13.299  1.00 37.60 ? 148 VAL K CG1 1 
ATOM   12170 C  CG2 . VAL K  1 148 ? 63.493  63.903  11.466  1.00 34.97 ? 148 VAL K CG2 1 
ATOM   12171 N  N   . ILE K  1 149 ? 65.522  60.059  13.378  1.00 38.72 ? 149 ILE K N   1 
ATOM   12172 C  CA  . ILE K  1 149 ? 65.905  59.152  14.458  1.00 39.96 ? 149 ILE K CA  1 
ATOM   12173 C  C   . ILE K  1 149 ? 66.099  59.897  15.781  1.00 40.35 ? 149 ILE K C   1 
ATOM   12174 O  O   . ILE K  1 149 ? 66.982  60.744  15.902  1.00 36.52 ? 149 ILE K O   1 
ATOM   12175 C  CB  . ILE K  1 149 ? 67.186  58.358  14.130  1.00 38.31 ? 149 ILE K CB  1 
ATOM   12176 C  CG1 . ILE K  1 149 ? 66.968  57.469  12.907  1.00 44.51 ? 149 ILE K CG1 1 
ATOM   12177 C  CG2 . ILE K  1 149 ? 67.622  57.521  15.327  1.00 39.83 ? 149 ILE K CG2 1 
ATOM   12178 C  CD1 . ILE K  1 149 ? 67.817  57.866  11.705  1.00 44.72 ? 149 ILE K CD1 1 
ATOM   12179 N  N   . GLY K  1 150 ? 65.275  59.568  16.772  1.00 38.78 ? 150 GLY K N   1 
ATOM   12180 C  CA  . GLY K  1 150 ? 65.335  60.238  18.056  1.00 41.46 ? 150 GLY K CA  1 
ATOM   12181 C  C   . GLY K  1 150 ? 65.554  59.322  19.244  1.00 40.77 ? 150 GLY K C   1 
ATOM   12182 O  O   . GLY K  1 150 ? 65.061  58.197  19.264  1.00 46.34 ? 150 GLY K O   1 
ATOM   12183 N  N   . ILE K  1 151 ? 66.279  59.830  20.240  1.00 38.64 ? 151 ILE K N   1 
ATOM   12184 C  CA  . ILE K  1 151 ? 66.540  59.128  21.501  1.00 40.20 ? 151 ILE K CA  1 
ATOM   12185 C  C   . ILE K  1 151 ? 65.259  58.662  22.186  1.00 38.50 ? 151 ILE K C   1 
ATOM   12186 O  O   . ILE K  1 151 ? 64.247  59.353  22.162  1.00 38.67 ? 151 ILE K O   1 
ATOM   12187 C  CB  . ILE K  1 151 ? 67.345  60.027  22.473  1.00 39.03 ? 151 ILE K CB  1 
ATOM   12188 C  CG1 . ILE K  1 151 ? 68.524  60.679  21.740  1.00 37.82 ? 151 ILE K CG1 1 
ATOM   12189 C  CG2 . ILE K  1 151 ? 67.819  59.233  23.676  1.00 38.01 ? 151 ILE K CG2 1 
ATOM   12190 C  CD1 . ILE K  1 151 ? 69.429  61.521  22.623  1.00 36.00 ? 151 ILE K CD1 1 
ATOM   12191 N  N   . ALA K  1 152 ? 65.307  57.472  22.777  1.00 45.60 ? 152 ALA K N   1 
ATOM   12192 C  CA  . ALA K  1 152 ? 64.145  56.884  23.447  1.00 43.99 ? 152 ALA K CA  1 
ATOM   12193 C  C   . ALA K  1 152 ? 64.507  56.412  24.844  1.00 43.89 ? 152 ALA K C   1 
ATOM   12194 O  O   . ALA K  1 152 ? 65.683  56.402  25.216  1.00 40.12 ? 152 ALA K O   1 
ATOM   12195 C  CB  . ALA K  1 152 ? 63.627  55.732  22.656  1.00 47.09 ? 152 ALA K CB  1 
ATOM   12196 N  N   . GLN K  1 153 ? 63.501  55.999  25.612  1.00 44.90 ? 153 GLN K N   1 
ATOM   12197 C  CA  . GLN K  1 153 ? 63.749  55.600  26.991  1.00 43.81 ? 153 GLN K CA  1 
ATOM   12198 C  C   . GLN K  1 153 ? 64.572  54.323  27.081  1.00 50.16 ? 153 GLN K C   1 
ATOM   12199 O  O   . GLN K  1 153 ? 64.013  53.229  27.200  1.00 51.61 ? 153 GLN K O   1 
ATOM   12200 C  CB  . GLN K  1 153 ? 62.447  55.434  27.768  1.00 46.50 ? 153 GLN K CB  1 
ATOM   12201 C  CG  . GLN K  1 153 ? 62.672  55.258  29.264  1.00 44.39 ? 153 GLN K CG  1 
ATOM   12202 C  CD  . GLN K  1 153 ? 61.483  55.697  30.093  1.00 46.26 ? 153 GLN K CD  1 
ATOM   12203 O  OE1 . GLN K  1 153 ? 60.458  56.115  29.551  1.00 51.42 ? 153 GLN K OE1 1 
ATOM   12204 N  NE2 . GLN K  1 153 ? 61.615  55.614  31.417  1.00 46.20 ? 153 GLN K NE2 1 
ATOM   12205 O  OXT . GLN K  1 153 ? 65.806  54.371  27.053  1.00 48.82 ? 153 GLN K OXT 1 
ATOM   12206 N  N   . ALA L  1 1   ? 79.344  76.128  11.790  1.00 59.77 ? 1   ALA L N   1 
ATOM   12207 C  CA  . ALA L  1 1   ? 78.186  76.022  12.673  1.00 55.54 ? 1   ALA L CA  1 
ATOM   12208 C  C   . ALA L  1 1   ? 77.454  74.678  12.550  1.00 48.41 ? 1   ALA L C   1 
ATOM   12209 O  O   . ALA L  1 1   ? 77.577  73.969  11.551  1.00 50.37 ? 1   ALA L O   1 
ATOM   12210 C  CB  . ALA L  1 1   ? 77.214  77.181  12.408  1.00 55.76 ? 1   ALA L CB  1 
ATOM   12211 N  N   . THR L  1 2   ? 76.706  74.329  13.587  1.00 45.39 ? 2   THR L N   1 
ATOM   12212 C  CA  . THR L  1 2   ? 75.714  73.271  13.489  1.00 42.34 ? 2   THR L CA  1 
ATOM   12213 C  C   . THR L  1 2   ? 74.365  73.982  13.359  1.00 41.23 ? 2   THR L C   1 
ATOM   12214 O  O   . THR L  1 2   ? 74.177  75.102  13.855  1.00 34.80 ? 2   THR L O   1 
ATOM   12215 C  CB  . THR L  1 2   ? 75.684  72.360  14.756  1.00 41.70 ? 2   THR L CB  1 
ATOM   12216 O  OG1 . THR L  1 2   ? 76.980  72.303  15.359  1.00 43.30 ? 2   THR L OG1 1 
ATOM   12217 C  CG2 . THR L  1 2   ? 75.211  70.940  14.418  1.00 40.99 ? 2   THR L CG2 1 
ATOM   12218 N  N   . LYS L  1 3   ? 73.435  73.337  12.673  1.00 36.00 ? 3   LYS L N   1 
ATOM   12219 C  CA  . LYS L  1 3   ? 72.071  73.811  12.625  1.00 33.14 ? 3   LYS L CA  1 
ATOM   12220 C  C   . LYS L  1 3   ? 71.162  72.633  12.886  1.00 26.59 ? 3   LYS L C   1 
ATOM   12221 O  O   . LYS L  1 3   ? 71.561  71.486  12.784  1.00 28.35 ? 3   LYS L O   1 
ATOM   12222 C  CB  . LYS L  1 3   ? 71.745  74.454  11.267  1.00 35.76 ? 3   LYS L CB  1 
ATOM   12223 C  CG  . LYS L  1 3   ? 72.320  75.857  11.087  1.00 41.54 ? 3   LYS L CG  1 
ATOM   12224 C  CD  . LYS L  1 3   ? 71.791  76.565  9.827   1.00 46.06 ? 3   LYS L CD  1 
ATOM   12225 C  CE  . LYS L  1 3   ? 70.294  76.896  9.915   1.00 45.10 ? 3   LYS L CE  1 
ATOM   12226 N  NZ  . LYS L  1 3   ? 69.909  77.791  11.063  1.00 42.88 ? 3   LYS L NZ  1 
ATOM   12227 N  N   . ALA L  1 4   ? 69.921  72.920  13.217  1.00 27.08 ? 4   ALA L N   1 
ATOM   12228 C  CA  . ALA L  1 4   ? 68.997  71.867  13.569  1.00 26.79 ? 4   ALA L CA  1 
ATOM   12229 C  C   . ALA L  1 4   ? 67.624  72.444  13.377  1.00 27.11 ? 4   ALA L C   1 
ATOM   12230 O  O   . ALA L  1 4   ? 67.449  73.669  13.403  1.00 26.04 ? 4   ALA L O   1 
ATOM   12231 C  CB  . ALA L  1 4   ? 69.206  71.452  15.028  1.00 29.78 ? 4   ALA L CB  1 
ATOM   12232 N  N   . VAL L  1 5   ? 66.645  71.573  13.198  1.00 22.96 ? 5   VAL L N   1 
ATOM   12233 C  CA  . VAL L  1 5   ? 65.321  72.031  12.882  1.00 20.18 ? 5   VAL L CA  1 
ATOM   12234 C  C   . VAL L  1 5   ? 64.339  71.031  13.442  1.00 21.37 ? 5   VAL L C   1 
ATOM   12235 O  O   . VAL L  1 5   ? 64.660  69.870  13.639  1.00 21.33 ? 5   VAL L O   1 
ATOM   12236 C  CB  . VAL L  1 5   ? 65.144  72.205  11.341  1.00 27.26 ? 5   VAL L CB  1 
ATOM   12237 C  CG1 . VAL L  1 5   ? 65.002  70.845  10.647  1.00 27.72 ? 5   VAL L CG1 1 
ATOM   12238 C  CG2 . VAL L  1 5   ? 63.956  73.116  11.017  1.00 20.11 ? 5   VAL L CG2 1 
ATOM   12239 N  N   . CYS L  1 6   ? 63.136  71.505  13.718  1.00 26.21 ? 6   CYS L N   1 
ATOM   12240 C  CA  . CYS L  1 6   ? 62.099  70.676  14.297  1.00 28.49 ? 6   CYS L CA  1 
ATOM   12241 C  C   . CYS L  1 6   ? 60.742  71.078  13.743  1.00 25.56 ? 6   CYS L C   1 
ATOM   12242 O  O   . CYS L  1 6   ? 60.382  72.256  13.743  1.00 26.24 ? 6   CYS L O   1 
ATOM   12243 C  CB  . CYS L  1 6   ? 62.076  70.807  15.830  1.00 24.78 ? 6   CYS L CB  1 
ATOM   12244 S  SG  . CYS L  1 6   ? 60.584  70.047  16.562  1.00 29.28 ? 6   CYS L SG  1 
ATOM   12245 N  N   . VAL L  1 7   ? 59.988  70.091  13.289  1.00 28.77 ? 7   VAL L N   1 
ATOM   12246 C  CA  . VAL L  1 7   ? 58.642  70.344  12.814  1.00 29.90 ? 7   VAL L CA  1 
ATOM   12247 C  C   . VAL L  1 7   ? 57.664  69.973  13.904  1.00 26.36 ? 7   VAL L C   1 
ATOM   12248 O  O   . VAL L  1 7   ? 57.645  68.844  14.393  1.00 23.56 ? 7   VAL L O   1 
ATOM   12249 C  CB  . VAL L  1 7   ? 58.314  69.557  11.530  1.00 33.02 ? 7   VAL L CB  1 
ATOM   12250 C  CG1 . VAL L  1 7   ? 56.841  69.733  11.167  1.00 31.35 ? 7   VAL L CG1 1 
ATOM   12251 C  CG2 . VAL L  1 7   ? 59.227  70.000  10.373  1.00 33.20 ? 7   VAL L CG2 1 
ATOM   12252 N  N   . LEU L  1 8   ? 56.849  70.947  14.280  1.00 28.12 ? 8   LEU L N   1 
ATOM   12253 C  CA  . LEU L  1 8   ? 55.864  70.760  15.326  1.00 33.55 ? 8   LEU L CA  1 
ATOM   12254 C  C   . LEU L  1 8   ? 54.503  70.448  14.725  1.00 32.37 ? 8   LEU L C   1 
ATOM   12255 O  O   . LEU L  1 8   ? 54.010  71.180  13.850  1.00 26.15 ? 8   LEU L O   1 
ATOM   12256 C  CB  . LEU L  1 8   ? 55.761  72.016  16.212  1.00 26.73 ? 8   LEU L CB  1 
ATOM   12257 C  CG  . LEU L  1 8   ? 56.939  72.338  17.130  1.00 30.12 ? 8   LEU L CG  1 
ATOM   12258 C  CD1 . LEU L  1 8   ? 56.926  73.806  17.555  1.00 23.77 ? 8   LEU L CD1 1 
ATOM   12259 C  CD2 . LEU L  1 8   ? 56.903  71.429  18.333  1.00 32.26 ? 8   LEU L CD2 1 
ATOM   12260 N  N   . LYS L  1 9   ? 53.902  69.374  15.227  1.00 31.38 ? 9   LYS L N   1 
ATOM   12261 C  CA  . LYS L  1 9   ? 52.520  69.043  14.929  1.00 32.99 ? 9   LYS L CA  1 
ATOM   12262 C  C   . LYS L  1 9   ? 51.932  68.347  16.137  1.00 31.36 ? 9   LYS L C   1 
ATOM   12263 O  O   . LYS L  1 9   ? 52.657  67.793  16.951  1.00 38.62 ? 9   LYS L O   1 
ATOM   12264 C  CB  . LYS L  1 9   ? 52.437  68.126  13.702  1.00 40.10 ? 9   LYS L CB  1 
ATOM   12265 C  CG  . LYS L  1 9   ? 52.415  68.859  12.372  1.00 44.01 ? 9   LYS L CG  1 
ATOM   12266 C  CD  . LYS L  1 9   ? 52.533  67.886  11.195  1.00 57.29 ? 9   LYS L CD  1 
ATOM   12267 C  CE  . LYS L  1 9   ? 52.281  68.590  9.859   1.00 50.16 ? 9   LYS L CE  1 
ATOM   12268 N  NZ  . LYS L  1 9   ? 53.180  69.771  9.668   1.00 37.80 ? 9   LYS L NZ  1 
ATOM   12269 N  N   . GLY L  1 10  ? 50.615  68.369  16.255  1.00 35.66 ? 10  GLY L N   1 
ATOM   12270 C  CA  . GLY L  1 10  ? 49.957  67.665  17.334  1.00 38.95 ? 10  GLY L CA  1 
ATOM   12271 C  C   . GLY L  1 10  ? 48.571  67.223  16.918  1.00 49.18 ? 10  GLY L C   1 
ATOM   12272 O  O   . GLY L  1 10  ? 48.265  67.144  15.723  1.00 48.68 ? 10  GLY L O   1 
ATOM   12273 N  N   . ASP L  1 11  ? 47.728  66.946  17.906  1.00 52.00 ? 11  ASP L N   1 
ATOM   12274 C  CA  . ASP L  1 11  ? 46.379  66.471  17.641  1.00 53.49 ? 11  ASP L CA  1 
ATOM   12275 C  C   . ASP L  1 11  ? 45.478  67.571  17.075  1.00 55.35 ? 11  ASP L C   1 
ATOM   12276 O  O   . ASP L  1 11  ? 44.669  67.316  16.182  1.00 61.69 ? 11  ASP L O   1 
ATOM   12277 C  CB  . ASP L  1 11  ? 45.768  65.878  18.910  1.00 53.81 ? 11  ASP L CB  1 
ATOM   12278 C  CG  . ASP L  1 11  ? 44.417  65.261  18.664  1.00 62.26 ? 11  ASP L CG  1 
ATOM   12279 O  OD1 . ASP L  1 11  ? 44.177  64.807  17.524  1.00 69.37 ? 11  ASP L OD1 1 
ATOM   12280 O  OD2 . ASP L  1 11  ? 43.594  65.228  19.602  1.00 66.23 ? 11  ASP L OD2 1 
ATOM   12281 N  N   . GLY L  1 12  ? 45.615  68.790  17.592  1.00 51.01 ? 12  GLY L N   1 
ATOM   12282 C  CA  . GLY L  1 12  ? 44.765  69.895  17.175  1.00 44.20 ? 12  GLY L CA  1 
ATOM   12283 C  C   . GLY L  1 12  ? 45.335  70.701  16.020  1.00 45.44 ? 12  GLY L C   1 
ATOM   12284 O  O   . GLY L  1 12  ? 46.088  70.167  15.195  1.00 44.86 ? 12  GLY L O   1 
ATOM   12285 N  N   . PRO L  1 13  ? 44.993  72.000  15.957  1.00 37.87 ? 13  PRO L N   1 
ATOM   12286 C  CA  . PRO L  1 13  ? 45.415  72.886  14.860  1.00 39.12 ? 13  PRO L CA  1 
ATOM   12287 C  C   . PRO L  1 13  ? 46.844  73.451  14.973  1.00 41.00 ? 13  PRO L C   1 
ATOM   12288 O  O   . PRO L  1 13  ? 47.234  74.213  14.077  1.00 36.84 ? 13  PRO L O   1 
ATOM   12289 C  CB  . PRO L  1 13  ? 44.413  74.039  14.957  1.00 37.26 ? 13  PRO L CB  1 
ATOM   12290 C  CG  . PRO L  1 13  ? 44.140  74.135  16.421  1.00 37.57 ? 13  PRO L CG  1 
ATOM   12291 C  CD  . PRO L  1 13  ? 44.134  72.702  16.925  1.00 34.49 ? 13  PRO L CD  1 
ATOM   12292 N  N   . VAL L  1 14  ? 47.596  73.103  16.027  1.00 37.99 ? 14  VAL L N   1 
ATOM   12293 C  CA  . VAL L  1 14  ? 48.905  73.717  16.259  1.00 30.53 ? 14  VAL L CA  1 
ATOM   12294 C  C   . VAL L  1 14  ? 50.008  73.077  15.421  1.00 29.70 ? 14  VAL L C   1 
ATOM   12295 O  O   . VAL L  1 14  ? 50.193  71.861  15.423  1.00 32.91 ? 14  VAL L O   1 
ATOM   12296 C  CB  . VAL L  1 14  ? 49.321  73.697  17.768  1.00 30.57 ? 14  VAL L CB  1 
ATOM   12297 C  CG1 . VAL L  1 14  ? 50.615  74.494  17.983  1.00 25.86 ? 14  VAL L CG1 1 
ATOM   12298 C  CG2 . VAL L  1 14  ? 48.216  74.249  18.645  1.00 28.46 ? 14  VAL L CG2 1 
ATOM   12299 N  N   . GLN L  1 15  ? 50.758  73.901  14.710  1.00 29.31 ? 15  GLN L N   1 
ATOM   12300 C  CA  . GLN L  1 15  ? 51.830  73.376  13.880  1.00 30.10 ? 15  GLN L CA  1 
ATOM   12301 C  C   . GLN L  1 15  ? 52.857  74.446  13.609  1.00 26.57 ? 15  GLN L C   1 
ATOM   12302 O  O   . GLN L  1 15  ? 52.558  75.638  13.649  1.00 25.49 ? 15  GLN L O   1 
ATOM   12303 C  CB  . GLN L  1 15  ? 51.277  72.878  12.544  1.00 36.80 ? 15  GLN L CB  1 
ATOM   12304 C  CG  . GLN L  1 15  ? 50.630  73.976  11.713  1.00 35.94 ? 15  GLN L CG  1 
ATOM   12305 C  CD  . GLN L  1 15  ? 50.038  73.458  10.417  1.00 57.37 ? 15  GLN L CD  1 
ATOM   12306 O  OE1 . GLN L  1 15  ? 50.248  74.044  9.352   1.00 61.93 ? 15  GLN L OE1 1 
ATOM   12307 N  NE2 . GLN L  1 15  ? 49.280  72.358  10.502  1.00 57.82 ? 15  GLN L NE2 1 
ATOM   12308 N  N   . GLY L  1 16  ? 54.078  74.038  13.322  1.00 25.33 ? 16  GLY L N   1 
ATOM   12309 C  CA  . GLY L  1 16  ? 55.040  75.043  12.938  1.00 31.87 ? 16  GLY L CA  1 
ATOM   12310 C  C   . GLY L  1 16  ? 56.411  74.488  12.738  1.00 26.20 ? 16  GLY L C   1 
ATOM   12311 O  O   . GLY L  1 16  ? 56.621  73.297  12.899  1.00 29.99 ? 16  GLY L O   1 
ATOM   12312 N  N   . ILE L  1 17  ? 57.337  75.373  12.392  1.00 30.91 ? 17  ILE L N   1 
ATOM   12313 C  CA  . ILE L  1 17  ? 58.719  75.001  12.140  1.00 31.10 ? 17  ILE L CA  1 
ATOM   12314 C  C   . ILE L  1 17  ? 59.652  75.835  12.993  1.00 34.14 ? 17  ILE L C   1 
ATOM   12315 O  O   . ILE L  1 17  ? 59.635  77.069  12.927  1.00 33.25 ? 17  ILE L O   1 
ATOM   12316 C  CB  . ILE L  1 17  ? 59.104  75.218  10.669  1.00 31.17 ? 17  ILE L CB  1 
ATOM   12317 C  CG1 . ILE L  1 17  ? 58.284  74.287  9.762   1.00 33.25 ? 17  ILE L CG1 1 
ATOM   12318 C  CG2 . ILE L  1 17  ? 60.627  75.039  10.494  1.00 29.10 ? 17  ILE L CG2 1 
ATOM   12319 C  CD1 . ILE L  1 17  ? 58.548  74.488  8.277   1.00 32.12 ? 17  ILE L CD1 1 
ATOM   12320 N  N   . ILE L  1 18  ? 60.473  75.155  13.786  1.00 30.84 ? 18  ILE L N   1 
ATOM   12321 C  CA  . ILE L  1 18  ? 61.432  75.824  14.647  1.00 28.32 ? 18  ILE L CA  1 
ATOM   12322 C  C   . ILE L  1 18  ? 62.857  75.548  14.186  1.00 25.44 ? 18  ILE L C   1 
ATOM   12323 O  O   . ILE L  1 18  ? 63.233  74.400  13.995  1.00 24.67 ? 18  ILE L O   1 
ATOM   12324 C  CB  . ILE L  1 18  ? 61.283  75.336  16.085  1.00 30.76 ? 18  ILE L CB  1 
ATOM   12325 C  CG1 . ILE L  1 18  ? 59.891  75.692  16.603  1.00 26.43 ? 18  ILE L CG1 1 
ATOM   12326 C  CG2 . ILE L  1 18  ? 62.381  75.936  16.946  1.00 27.54 ? 18  ILE L CG2 1 
ATOM   12327 C  CD1 . ILE L  1 18  ? 59.655  77.195  16.664  1.00 30.28 ? 18  ILE L CD1 1 
ATOM   12328 N  N   . ASN L  1 19  ? 63.640  76.607  14.016  1.00 26.37 ? 19  ASN L N   1 
ATOM   12329 C  CA  . ASN L  1 19  ? 65.033  76.497  13.568  1.00 26.40 ? 19  ASN L CA  1 
ATOM   12330 C  C   . ASN L  1 19  ? 66.027  76.659  14.730  1.00 27.01 ? 19  ASN L C   1 
ATOM   12331 O  O   . ASN L  1 19  ? 65.781  77.436  15.653  1.00 27.30 ? 19  ASN L O   1 
ATOM   12332 C  CB  . ASN L  1 19  ? 65.305  77.561  12.501  1.00 23.71 ? 19  ASN L CB  1 
ATOM   12333 C  CG  . ASN L  1 19  ? 64.262  77.555  11.413  1.00 29.67 ? 19  ASN L CG  1 
ATOM   12334 O  OD1 . ASN L  1 19  ? 64.061  76.539  10.755  1.00 33.44 ? 19  ASN L OD1 1 
ATOM   12335 N  ND2 . ASN L  1 19  ? 63.560  78.671  11.243  1.00 27.04 ? 19  ASN L ND2 1 
ATOM   12336 N  N   . PHE L  1 20  ? 67.145  75.939  14.684  1.00 26.31 ? 20  PHE L N   1 
ATOM   12337 C  CA  . PHE L  1 20  ? 68.187  76.100  15.692  1.00 24.49 ? 20  PHE L CA  1 
ATOM   12338 C  C   . PHE L  1 20  ? 69.517  76.401  15.006  1.00 27.52 ? 20  PHE L C   1 
ATOM   12339 O  O   . PHE L  1 20  ? 69.915  75.688  14.091  1.00 26.95 ? 20  PHE L O   1 
ATOM   12340 C  CB  . PHE L  1 20  ? 68.323  74.831  16.549  1.00 23.78 ? 20  PHE L CB  1 
ATOM   12341 C  CG  . PHE L  1 20  ? 67.044  74.403  17.255  1.00 28.30 ? 20  PHE L CG  1 
ATOM   12342 C  CD1 . PHE L  1 20  ? 66.113  73.587  16.618  1.00 21.77 ? 20  PHE L CD1 1 
ATOM   12343 C  CD2 . PHE L  1 20  ? 66.805  74.776  18.573  1.00 31.72 ? 20  PHE L CD2 1 
ATOM   12344 C  CE1 . PHE L  1 20  ? 64.966  73.172  17.260  1.00 24.58 ? 20  PHE L CE1 1 
ATOM   12345 C  CE2 . PHE L  1 20  ? 65.644  74.366  19.234  1.00 29.08 ? 20  PHE L CE2 1 
ATOM   12346 C  CZ  . PHE L  1 20  ? 64.721  73.560  18.570  1.00 29.27 ? 20  PHE L CZ  1 
ATOM   12347 N  N   . GLU L  1 21  ? 70.214  77.443  15.446  1.00 25.97 ? 21  GLU L N   1 
ATOM   12348 C  CA  . GLU L  1 21  ? 71.534  77.738  14.887  1.00 32.07 ? 21  GLU L CA  1 
ATOM   12349 C  C   . GLU L  1 21  ? 72.593  78.073  15.930  1.00 31.94 ? 21  GLU L C   1 
ATOM   12350 O  O   . GLU L  1 21  ? 72.454  79.043  16.686  1.00 25.86 ? 21  GLU L O   1 
ATOM   12351 C  CB  . GLU L  1 21  ? 71.486  78.871  13.856  1.00 31.28 ? 21  GLU L CB  1 
ATOM   12352 C  CG  . GLU L  1 21  ? 72.886  79.433  13.537  1.00 38.10 ? 21  GLU L CG  1 
ATOM   12353 C  CD  . GLU L  1 21  ? 72.890  80.507  12.452  1.00 47.79 ? 21  GLU L CD  1 
ATOM   12354 O  OE1 . GLU L  1 21  ? 73.859  80.538  11.647  1.00 42.82 ? 21  GLU L OE1 1 
ATOM   12355 O  OE2 . GLU L  1 21  ? 71.938  81.327  12.416  1.00 47.54 ? 21  GLU L OE2 1 
ATOM   12356 N  N   . GLN L  1 22  ? 73.665  77.285  15.929  1.00 29.52 ? 22  GLN L N   1 
ATOM   12357 C  CA  . GLN L  1 22  ? 74.775  77.483  16.845  1.00 33.69 ? 22  GLN L CA  1 
ATOM   12358 C  C   . GLN L  1 22  ? 76.056  77.717  16.047  1.00 39.53 ? 22  GLN L C   1 
ATOM   12359 O  O   . GLN L  1 22  ? 76.611  76.791  15.449  1.00 33.88 ? 22  GLN L O   1 
ATOM   12360 C  CB  . GLN L  1 22  ? 74.911  76.264  17.769  1.00 35.27 ? 22  GLN L CB  1 
ATOM   12361 C  CG  . GLN L  1 22  ? 75.809  76.465  18.984  1.00 31.56 ? 22  GLN L CG  1 
ATOM   12362 C  CD  . GLN L  1 22  ? 75.777  75.268  19.927  1.00 35.20 ? 22  GLN L CD  1 
ATOM   12363 O  OE1 . GLN L  1 22  ? 75.391  74.158  19.533  1.00 30.89 ? 22  GLN L OE1 1 
ATOM   12364 N  NE2 . GLN L  1 22  ? 76.164  75.493  21.185  1.00 31.75 ? 22  GLN L NE2 1 
ATOM   12365 N  N   . LYS L  1 23  ? 76.509  78.969  16.038  1.00 40.29 ? 23  LYS L N   1 
ATOM   12366 C  CA  . LYS L  1 23  ? 77.684  79.367  15.267  1.00 45.45 ? 23  LYS L CA  1 
ATOM   12367 C  C   . LYS L  1 23  ? 78.951  78.696  15.781  1.00 45.94 ? 23  LYS L C   1 
ATOM   12368 O  O   . LYS L  1 23  ? 79.653  78.031  15.028  1.00 46.30 ? 23  LYS L O   1 
ATOM   12369 C  CB  . LYS L  1 23  ? 77.846  80.894  15.270  1.00 46.96 ? 23  LYS L CB  1 
ATOM   12370 C  CG  . LYS L  1 23  ? 76.793  81.631  14.444  1.00 44.25 ? 23  LYS L CG  1 
ATOM   12371 C  CD  . LYS L  1 23  ? 76.903  83.147  14.592  1.00 47.83 ? 23  LYS L CD  1 
ATOM   12372 C  CE  . LYS L  1 23  ? 75.876  83.866  13.717  1.00 52.37 ? 23  LYS L CE  1 
ATOM   12373 N  NZ  . LYS L  1 23  ? 74.461  83.463  14.025  1.00 52.38 ? 23  LYS L NZ  1 
ATOM   12374 N  N   . GLU L  1 24  ? 79.232  78.867  17.067  1.00 43.16 ? 24  GLU L N   1 
ATOM   12375 C  CA  . GLU L  1 24  ? 80.413  78.279  17.678  1.00 45.25 ? 24  GLU L CA  1 
ATOM   12376 C  C   . GLU L  1 24  ? 80.011  77.119  18.565  1.00 46.90 ? 24  GLU L C   1 
ATOM   12377 O  O   . GLU L  1 24  ? 78.898  77.095  19.086  1.00 48.44 ? 24  GLU L O   1 
ATOM   12378 C  CB  . GLU L  1 24  ? 81.150  79.326  18.500  1.00 47.61 ? 24  GLU L CB  1 
ATOM   12379 C  CG  . GLU L  1 24  ? 81.580  80.524  17.691  1.00 49.93 ? 24  GLU L CG  1 
ATOM   12380 C  CD  . GLU L  1 24  ? 81.518  81.815  18.486  1.00 67.48 ? 24  GLU L CD  1 
ATOM   12381 O  OE1 . GLU L  1 24  ? 81.542  81.756  19.738  1.00 65.29 ? 24  GLU L OE1 1 
ATOM   12382 O  OE2 . GLU L  1 24  ? 81.435  82.891  17.852  1.00 72.04 ? 24  GLU L OE2 1 
ATOM   12383 N  N   . SER L  1 25  ? 80.926  76.170  18.749  1.00 48.25 ? 25  SER L N   1 
ATOM   12384 C  CA  . SER L  1 25  ? 80.620  74.926  19.454  1.00 48.14 ? 25  SER L CA  1 
ATOM   12385 C  C   . SER L  1 25  ? 80.057  75.162  20.843  1.00 51.30 ? 25  SER L C   1 
ATOM   12386 O  O   . SER L  1 25  ? 79.097  74.507  21.265  1.00 46.39 ? 25  SER L O   1 
ATOM   12387 C  CB  . SER L  1 25  ? 81.860  74.048  19.567  1.00 49.04 ? 25  SER L CB  1 
ATOM   12388 O  OG  . SER L  1 25  ? 81.551  72.905  20.339  1.00 48.87 ? 25  SER L OG  1 
ATOM   12389 N  N   . ASN L  1 26  ? 80.666  76.099  21.557  1.00 50.09 ? 26  ASN L N   1 
ATOM   12390 C  CA  . ASN L  1 26  ? 80.187  76.434  22.881  1.00 49.04 ? 26  ASN L CA  1 
ATOM   12391 C  C   . ASN L  1 26  ? 79.840  77.909  22.992  1.00 51.12 ? 26  ASN L C   1 
ATOM   12392 O  O   . ASN L  1 26  ? 80.571  78.720  23.575  1.00 49.68 ? 26  ASN L O   1 
ATOM   12393 C  CB  . ASN L  1 26  ? 81.174  75.965  23.942  1.00 52.50 ? 26  ASN L CB  1 
ATOM   12394 C  CG  . ASN L  1 26  ? 81.345  74.455  23.927  1.00 57.19 ? 26  ASN L CG  1 
ATOM   12395 O  OD1 . ASN L  1 26  ? 80.459  73.710  24.377  1.00 53.41 ? 26  ASN L OD1 1 
ATOM   12396 N  ND2 . ASN L  1 26  ? 82.482  73.989  23.395  1.00 51.37 ? 26  ASN L ND2 1 
ATOM   12397 N  N   . GLY L  1 27  ? 78.704  78.228  22.389  1.00 45.39 ? 27  GLY L N   1 
ATOM   12398 C  CA  . GLY L  1 27  ? 78.168  79.569  22.369  1.00 43.32 ? 27  GLY L CA  1 
ATOM   12399 C  C   . GLY L  1 27  ? 76.670  79.452  22.205  1.00 32.16 ? 27  GLY L C   1 
ATOM   12400 O  O   . GLY L  1 27  ? 76.139  78.344  22.094  1.00 28.85 ? 27  GLY L O   1 
ATOM   12401 N  N   . PRO L  1 28  ? 75.984  80.599  22.168  1.00 36.05 ? 28  PRO L N   1 
ATOM   12402 C  CA  . PRO L  1 28  ? 74.520  80.629  22.218  1.00 31.67 ? 28  PRO L CA  1 
ATOM   12403 C  C   . PRO L  1 28  ? 73.889  79.938  21.022  1.00 30.64 ? 28  PRO L C   1 
ATOM   12404 O  O   . PRO L  1 28  ? 74.427  79.984  19.913  1.00 29.24 ? 28  PRO L O   1 
ATOM   12405 C  CB  . PRO L  1 28  ? 74.188  82.128  22.182  1.00 31.85 ? 28  PRO L CB  1 
ATOM   12406 C  CG  . PRO L  1 28  ? 75.470  82.837  22.480  1.00 40.92 ? 28  PRO L CG  1 
ATOM   12407 C  CD  . PRO L  1 28  ? 76.564  81.942  21.995  1.00 35.92 ? 28  PRO L CD  1 
ATOM   12408 N  N   . VAL L  1 29  ? 72.750  79.308  21.273  1.00 26.46 ? 29  VAL L N   1 
ATOM   12409 C  CA  . VAL L  1 29  ? 71.911  78.723  20.235  1.00 28.00 ? 29  VAL L CA  1 
ATOM   12410 C  C   . VAL L  1 29  ? 70.773  79.687  19.940  1.00 27.48 ? 29  VAL L C   1 
ATOM   12411 O  O   . VAL L  1 29  ? 70.063  80.108  20.853  1.00 25.09 ? 29  VAL L O   1 
ATOM   12412 C  CB  . VAL L  1 29  ? 71.306  77.401  20.725  1.00 19.45 ? 29  VAL L CB  1 
ATOM   12413 C  CG1 . VAL L  1 29  ? 70.254  76.870  19.759  1.00 23.62 ? 29  VAL L CG1 1 
ATOM   12414 C  CG2 . VAL L  1 29  ? 72.410  76.385  20.961  1.00 24.86 ? 29  VAL L CG2 1 
ATOM   12415 N  N   . LYS L  1 30  ? 70.619  80.056  18.672  1.00 28.19 ? 30  LYS L N   1 
ATOM   12416 C  CA  . LYS L  1 30  ? 69.469  80.845  18.226  1.00 27.87 ? 30  LYS L CA  1 
ATOM   12417 C  C   . LYS L  1 30  ? 68.290  79.931  17.867  1.00 24.60 ? 30  LYS L C   1 
ATOM   12418 O  O   . LYS L  1 30  ? 68.451  78.905  17.241  1.00 23.50 ? 30  LYS L O   1 
ATOM   12419 C  CB  . LYS L  1 30  ? 69.846  81.770  17.064  1.00 26.80 ? 30  LYS L CB  1 
ATOM   12420 C  CG  . LYS L  1 30  ? 70.869  82.835  17.470  1.00 34.04 ? 30  LYS L CG  1 
ATOM   12421 C  CD  . LYS L  1 30  ? 71.486  83.548  16.275  1.00 39.33 ? 30  LYS L CD  1 
ATOM   12422 C  CE  . LYS L  1 30  ? 70.751  84.834  15.918  1.00 42.93 ? 30  LYS L CE  1 
ATOM   12423 N  NZ  . LYS L  1 30  ? 71.230  85.410  14.613  1.00 47.56 ? 30  LYS L NZ  1 
ATOM   12424 N  N   . VAL L  1 31  ? 67.111  80.299  18.335  1.00 26.03 ? 31  VAL L N   1 
ATOM   12425 C  CA  . VAL L  1 31  ? 65.902  79.527  18.101  1.00 28.26 ? 31  VAL L CA  1 
ATOM   12426 C  C   . VAL L  1 31  ? 64.906  80.497  17.511  1.00 27.63 ? 31  VAL L C   1 
ATOM   12427 O  O   . VAL L  1 31  ? 64.570  81.506  18.125  1.00 27.17 ? 31  VAL L O   1 
ATOM   12428 C  CB  . VAL L  1 31  ? 65.306  78.968  19.416  1.00 26.95 ? 31  VAL L CB  1 
ATOM   12429 C  CG1 . VAL L  1 31  ? 64.083  78.090  19.117  1.00 23.60 ? 31  VAL L CG1 1 
ATOM   12430 C  CG2 . VAL L  1 31  ? 66.372  78.198  20.231  1.00 24.32 ? 31  VAL L CG2 1 
ATOM   12431 N  N   . TRP L  1 32  ? 64.446  80.207  16.310  1.00 31.17 ? 32  TRP L N   1 
ATOM   12432 C  CA  . TRP L  1 32  ? 63.539  81.118  15.623  1.00 29.84 ? 32  TRP L CA  1 
ATOM   12433 C  C   . TRP L  1 32  ? 62.653  80.317  14.694  1.00 25.57 ? 32  TRP L C   1 
ATOM   12434 O  O   . TRP L  1 32  ? 63.088  79.345  14.092  1.00 25.80 ? 32  TRP L O   1 
ATOM   12435 C  CB  . TRP L  1 32  ? 64.315  82.197  14.855  1.00 26.50 ? 32  TRP L CB  1 
ATOM   12436 C  CG  . TRP L  1 32  ? 65.214  81.651  13.762  1.00 33.34 ? 32  TRP L CG  1 
ATOM   12437 C  CD1 . TRP L  1 32  ? 66.471  81.110  13.912  1.00 31.08 ? 32  TRP L CD1 1 
ATOM   12438 C  CD2 . TRP L  1 32  ? 64.927  81.608  12.357  1.00 33.30 ? 32  TRP L CD2 1 
ATOM   12439 N  NE1 . TRP L  1 32  ? 66.973  80.731  12.686  1.00 34.28 ? 32  TRP L NE1 1 
ATOM   12440 C  CE2 . TRP L  1 32  ? 66.048  81.032  11.716  1.00 36.22 ? 32  TRP L CE2 1 
ATOM   12441 C  CE3 . TRP L  1 32  ? 63.830  81.999  11.578  1.00 36.71 ? 32  TRP L CE3 1 
ATOM   12442 C  CZ2 . TRP L  1 32  ? 66.097  80.835  10.332  1.00 38.76 ? 32  TRP L CZ2 1 
ATOM   12443 C  CZ3 . TRP L  1 32  ? 63.884  81.809  10.200  1.00 37.86 ? 32  TRP L CZ3 1 
ATOM   12444 C  CH2 . TRP L  1 32  ? 65.006  81.227  9.595   1.00 37.08 ? 32  TRP L CH2 1 
ATOM   12445 N  N   . GLY L  1 33  ? 61.397  80.719  14.608  1.00 29.84 ? 33  GLY L N   1 
ATOM   12446 C  CA  . GLY L  1 33  ? 60.439  80.047  13.758  1.00 29.97 ? 33  GLY L CA  1 
ATOM   12447 C  C   . GLY L  1 33  ? 59.055  80.616  13.973  1.00 31.76 ? 33  GLY L C   1 
ATOM   12448 O  O   . GLY L  1 33  ? 58.870  81.624  14.666  1.00 33.15 ? 33  GLY L O   1 
ATOM   12449 N  N   . SER L  1 34  ? 58.072  79.954  13.386  1.00 36.12 ? 34  SER L N   1 
ATOM   12450 C  CA  . SER L  1 34  ? 56.705  80.424  13.452  1.00 33.84 ? 34  SER L CA  1 
ATOM   12451 C  C   . SER L  1 34  ? 55.788  79.251  13.769  1.00 30.85 ? 34  SER L C   1 
ATOM   12452 O  O   . SER L  1 34  ? 55.926  78.172  13.214  1.00 31.49 ? 34  SER L O   1 
ATOM   12453 C  CB  . SER L  1 34  ? 56.325  81.079  12.121  1.00 34.70 ? 34  SER L CB  1 
ATOM   12454 O  OG  . SER L  1 34  ? 55.077  81.737  12.209  1.00 36.27 ? 34  SER L OG  1 
ATOM   12455 N  N   . ILE L  1 35  ? 54.859  79.460  14.687  1.00 31.62 ? 35  ILE L N   1 
ATOM   12456 C  CA  . ILE L  1 35  ? 53.934  78.410  15.065  1.00 30.89 ? 35  ILE L CA  1 
ATOM   12457 C  C   . ILE L  1 35  ? 52.532  78.969  15.008  1.00 32.14 ? 35  ILE L C   1 
ATOM   12458 O  O   . ILE L  1 35  ? 52.253  80.007  15.613  1.00 32.81 ? 35  ILE L O   1 
ATOM   12459 C  CB  . ILE L  1 35  ? 54.190  77.924  16.496  1.00 28.85 ? 35  ILE L CB  1 
ATOM   12460 C  CG1 . ILE L  1 35  ? 55.652  77.491  16.659  1.00 31.79 ? 35  ILE L CG1 1 
ATOM   12461 C  CG2 . ILE L  1 35  ? 53.247  76.794  16.827  1.00 29.18 ? 35  ILE L CG2 1 
ATOM   12462 C  CD1 . ILE L  1 35  ? 56.060  77.219  18.098  1.00 33.73 ? 35  ILE L CD1 1 
ATOM   12463 N  N   . LYS L  1 36  ? 51.651  78.273  14.294  1.00 33.93 ? 36  LYS L N   1 
ATOM   12464 C  CA  . LYS L  1 36  ? 50.282  78.739  14.079  1.00 34.79 ? 36  LYS L CA  1 
ATOM   12465 C  C   . LYS L  1 36  ? 49.280  77.896  14.861  1.00 32.23 ? 36  LYS L C   1 
ATOM   12466 O  O   . LYS L  1 36  ? 49.638  76.864  15.444  1.00 26.23 ? 36  LYS L O   1 
ATOM   12467 C  CB  . LYS L  1 36  ? 49.931  78.718  12.580  1.00 33.00 ? 36  LYS L CB  1 
ATOM   12468 C  CG  . LYS L  1 36  ? 51.103  79.025  11.666  1.00 30.95 ? 36  LYS L CG  1 
ATOM   12469 C  CD  . LYS L  1 36  ? 50.971  80.362  10.965  1.00 39.02 ? 36  LYS L CD  1 
ATOM   12470 C  CE  . LYS L  1 36  ? 52.320  80.838  10.422  1.00 41.69 ? 36  LYS L CE  1 
ATOM   12471 N  NZ  . LYS L  1 36  ? 53.174  79.709  9.928   1.00 42.77 ? 36  LYS L NZ  1 
ATOM   12472 N  N   . GLY L  1 37  ? 48.027  78.354  14.866  1.00 28.38 ? 37  GLY L N   1 
ATOM   12473 C  CA  . GLY L  1 37  ? 46.936  77.623  15.474  1.00 26.06 ? 37  GLY L CA  1 
ATOM   12474 C  C   . GLY L  1 37  ? 46.907  77.713  16.981  1.00 34.69 ? 37  GLY L C   1 
ATOM   12475 O  O   . GLY L  1 37  ? 46.302  76.860  17.620  1.00 37.34 ? 37  GLY L O   1 
ATOM   12476 N  N   . LEU L  1 38  ? 47.550  78.745  17.541  1.00 32.43 ? 38  LEU L N   1 
ATOM   12477 C  CA  . LEU L  1 38  ? 47.721  78.904  18.991  1.00 33.28 ? 38  LEU L CA  1 
ATOM   12478 C  C   . LEU L  1 38  ? 46.740  79.924  19.556  1.00 31.96 ? 38  LEU L C   1 
ATOM   12479 O  O   . LEU L  1 38  ? 46.406  80.887  18.878  1.00 31.81 ? 38  LEU L O   1 
ATOM   12480 C  CB  . LEU L  1 38  ? 49.149  79.376  19.321  1.00 31.20 ? 38  LEU L CB  1 
ATOM   12481 C  CG  . LEU L  1 38  ? 50.298  78.370  19.415  1.00 32.05 ? 38  LEU L CG  1 
ATOM   12482 C  CD1 . LEU L  1 38  ? 51.649  79.080  19.403  1.00 28.33 ? 38  LEU L CD1 1 
ATOM   12483 C  CD2 . LEU L  1 38  ? 50.159  77.502  20.655  1.00 22.89 ? 38  LEU L CD2 1 
ATOM   12484 N  N   . THR L  1 39  ? 46.276  79.707  20.791  1.00 30.68 ? 39  THR L N   1 
ATOM   12485 C  CA  . THR L  1 39  ? 45.506  80.729  21.510  1.00 31.94 ? 39  THR L CA  1 
ATOM   12486 C  C   . THR L  1 39  ? 46.399  81.947  21.815  1.00 33.82 ? 39  THR L C   1 
ATOM   12487 O  O   . THR L  1 39  ? 47.628  81.817  21.971  1.00 30.67 ? 39  THR L O   1 
ATOM   12488 C  CB  . THR L  1 39  ? 44.883  80.204  22.843  1.00 27.43 ? 39  THR L CB  1 
ATOM   12489 O  OG1 . THR L  1 39  ? 45.923  79.899  23.779  1.00 28.99 ? 39  THR L OG1 1 
ATOM   12490 C  CG2 . THR L  1 39  ? 43.984  78.996  22.622  1.00 24.79 ? 39  THR L CG2 1 
ATOM   12491 N  N   . GLU L  1 40  ? 45.788  83.128  21.885  1.00 27.51 ? 40  GLU L N   1 
ATOM   12492 C  CA  . GLU L  1 40  ? 46.545  84.338  22.143  1.00 31.74 ? 40  GLU L CA  1 
ATOM   12493 C  C   . GLU L  1 40  ? 47.136  84.293  23.546  1.00 31.01 ? 40  GLU L C   1 
ATOM   12494 O  O   . GLU L  1 40  ? 46.480  83.860  24.500  1.00 31.31 ? 40  GLU L O   1 
ATOM   12495 C  CB  . GLU L  1 40  ? 45.677  85.587  22.000  1.00 26.08 ? 40  GLU L CB  1 
ATOM   12496 C  CG  . GLU L  1 40  ? 46.491  86.874  22.134  1.00 30.55 ? 40  GLU L CG  1 
ATOM   12497 C  CD  . GLU L  1 40  ? 45.650  88.146  22.143  1.00 37.25 ? 40  GLU L CD  1 
ATOM   12498 O  OE1 . GLU L  1 40  ? 44.412  88.061  22.328  1.00 33.21 ? 40  GLU L OE1 1 
ATOM   12499 O  OE2 . GLU L  1 40  ? 46.244  89.234  21.966  1.00 34.41 ? 40  GLU L OE2 1 
ATOM   12500 N  N   . GLY L  1 41  ? 48.371  84.758  23.667  1.00 28.68 ? 41  GLY L N   1 
ATOM   12501 C  CA  . GLY L  1 41  ? 49.043  84.767  24.944  1.00 25.41 ? 41  GLY L CA  1 
ATOM   12502 C  C   . GLY L  1 41  ? 50.181  83.771  25.064  1.00 26.53 ? 41  GLY L C   1 
ATOM   12503 O  O   . GLY L  1 41  ? 50.849  83.418  24.078  1.00 26.16 ? 41  GLY L O   1 
ATOM   12504 N  N   . LEU L  1 42  ? 50.363  83.299  26.295  1.00 30.21 ? 42  LEU L N   1 
ATOM   12505 C  CA  . LEU L  1 42  ? 51.570  82.613  26.733  1.00 24.48 ? 42  LEU L CA  1 
ATOM   12506 C  C   . LEU L  1 42  ? 51.523  81.090  26.561  1.00 22.33 ? 42  LEU L C   1 
ATOM   12507 O  O   . LEU L  1 42  ? 50.585  80.424  27.004  1.00 17.10 ? 42  LEU L O   1 
ATOM   12508 C  CB  . LEU L  1 42  ? 51.770  82.936  28.216  1.00 21.90 ? 42  LEU L CB  1 
ATOM   12509 C  CG  . LEU L  1 42  ? 52.941  83.780  28.725  1.00 24.84 ? 42  LEU L CG  1 
ATOM   12510 C  CD1 . LEU L  1 42  ? 53.634  84.598  27.647  1.00 19.64 ? 42  LEU L CD1 1 
ATOM   12511 C  CD2 . LEU L  1 42  ? 52.469  84.667  29.898  1.00 18.25 ? 42  LEU L CD2 1 
ATOM   12512 N  N   . HIS L  1 43  ? 52.564  80.522  25.964  1.00 21.29 ? 43  HIS L N   1 
ATOM   12513 C  CA  . HIS L  1 43  ? 52.633  79.059  25.872  1.00 22.84 ? 43  HIS L CA  1 
ATOM   12514 C  C   . HIS L  1 43  ? 53.953  78.462  26.358  1.00 19.13 ? 43  HIS L C   1 
ATOM   12515 O  O   . HIS L  1 43  ? 55.024  78.901  25.953  1.00 20.63 ? 43  HIS L O   1 
ATOM   12516 C  CB  . HIS L  1 43  ? 52.276  78.609  24.447  1.00 24.59 ? 43  HIS L CB  1 
ATOM   12517 C  CG  . HIS L  1 43  ? 50.859  78.926  24.075  1.00 25.05 ? 43  HIS L CG  1 
ATOM   12518 N  ND1 . HIS L  1 43  ? 49.805  78.088  24.375  1.00 26.00 ? 43  HIS L ND1 1 
ATOM   12519 C  CD2 . HIS L  1 43  ? 50.314  80.024  23.499  1.00 26.10 ? 43  HIS L CD2 1 
ATOM   12520 C  CE1 . HIS L  1 43  ? 48.676  78.638  23.965  1.00 28.38 ? 43  HIS L CE1 1 
ATOM   12521 N  NE2 . HIS L  1 43  ? 48.957  79.812  23.428  1.00 30.20 ? 43  HIS L NE2 1 
ATOM   12522 N  N   . GLY L  1 44  ? 53.861  77.486  27.261  1.00 22.55 ? 44  GLY L N   1 
ATOM   12523 C  CA  . GLY L  1 44  ? 55.027  76.771  27.746  1.00 24.06 ? 44  GLY L CA  1 
ATOM   12524 C  C   . GLY L  1 44  ? 55.784  76.121  26.597  1.00 26.46 ? 44  GLY L C   1 
ATOM   12525 O  O   . GLY L  1 44  ? 55.197  75.464  25.744  1.00 26.70 ? 44  GLY L O   1 
ATOM   12526 N  N   . PHE L  1 45  ? 57.098  76.312  26.587  1.00 25.99 ? 45  PHE L N   1 
ATOM   12527 C  CA  . PHE L  1 45  ? 57.950  75.892  25.493  1.00 27.40 ? 45  PHE L CA  1 
ATOM   12528 C  C   . PHE L  1 45  ? 59.132  75.092  26.030  1.00 24.81 ? 45  PHE L C   1 
ATOM   12529 O  O   . PHE L  1 45  ? 60.110  75.664  26.496  1.00 22.32 ? 45  PHE L O   1 
ATOM   12530 C  CB  . PHE L  1 45  ? 58.477  77.137  24.785  1.00 24.47 ? 45  PHE L CB  1 
ATOM   12531 C  CG  . PHE L  1 45  ? 58.898  76.906  23.368  1.00 22.70 ? 45  PHE L CG  1 
ATOM   12532 C  CD1 . PHE L  1 45  ? 58.099  76.174  22.502  1.00 29.01 ? 45  PHE L CD1 1 
ATOM   12533 C  CD2 . PHE L  1 45  ? 60.075  77.461  22.884  1.00 27.59 ? 45  PHE L CD2 1 
ATOM   12534 C  CE1 . PHE L  1 45  ? 58.474  75.980  21.181  1.00 25.25 ? 45  PHE L CE1 1 
ATOM   12535 C  CE2 . PHE L  1 45  ? 60.460  77.267  21.566  1.00 31.55 ? 45  PHE L CE2 1 
ATOM   12536 C  CZ  . PHE L  1 45  ? 59.646  76.527  20.708  1.00 29.35 ? 45  PHE L CZ  1 
ATOM   12537 N  N   . HIS L  1 46  ? 59.061  73.769  25.935  1.00 30.69 ? 46  HIS L N   1 
ATOM   12538 C  CA  . HIS L  1 46  ? 60.110  72.923  26.508  1.00 31.37 ? 46  HIS L CA  1 
ATOM   12539 C  C   . HIS L  1 46  ? 60.770  71.930  25.534  1.00 32.77 ? 46  HIS L C   1 
ATOM   12540 O  O   . HIS L  1 46  ? 60.179  71.491  24.543  1.00 28.73 ? 46  HIS L O   1 
ATOM   12541 C  CB  . HIS L  1 46  ? 59.538  72.119  27.674  1.00 26.11 ? 46  HIS L CB  1 
ATOM   12542 C  CG  . HIS L  1 46  ? 58.737  72.930  28.635  1.00 25.04 ? 46  HIS L CG  1 
ATOM   12543 N  ND1 . HIS L  1 46  ? 57.573  72.462  29.202  1.00 26.58 ? 46  HIS L ND1 1 
ATOM   12544 C  CD2 . HIS L  1 46  ? 58.938  74.169  29.146  1.00 23.14 ? 46  HIS L CD2 1 
ATOM   12545 C  CE1 . HIS L  1 46  ? 57.080  73.385  30.010  1.00 28.42 ? 46  HIS L CE1 1 
ATOM   12546 N  NE2 . HIS L  1 46  ? 57.893  74.428  29.999  1.00 26.38 ? 46  HIS L NE2 1 
ATOM   12547 N  N   . VAL L  1 47  ? 62.003  71.560  25.843  1.00 31.02 ? 47  VAL L N   1 
ATOM   12548 C  CA  . VAL L  1 47  ? 62.561  70.348  25.273  1.00 31.08 ? 47  VAL L CA  1 
ATOM   12549 C  C   . VAL L  1 47  ? 62.378  69.198  26.263  1.00 33.03 ? 47  VAL L C   1 
ATOM   12550 O  O   . VAL L  1 47  ? 62.826  69.278  27.413  1.00 30.27 ? 47  VAL L O   1 
ATOM   12551 C  CB  . VAL L  1 47  ? 64.036  70.478  24.985  1.00 29.02 ? 47  VAL L CB  1 
ATOM   12552 C  CG1 . VAL L  1 47  ? 64.531  69.166  24.426  1.00 31.31 ? 47  VAL L CG1 1 
ATOM   12553 C  CG2 . VAL L  1 47  ? 64.285  71.620  24.019  1.00 31.98 ? 47  VAL L CG2 1 
ATOM   12554 N  N   . HIS L  1 48  ? 61.712  68.136  25.824  1.00 31.40 ? 48  HIS L N   1 
ATOM   12555 C  CA  . HIS L  1 48  ? 61.541  66.955  26.657  1.00 30.44 ? 48  HIS L CA  1 
ATOM   12556 C  C   . HIS L  1 48  ? 62.623  65.911  26.347  1.00 33.11 ? 48  HIS L C   1 
ATOM   12557 O  O   . HIS L  1 48  ? 63.298  65.999  25.323  1.00 32.46 ? 48  HIS L O   1 
ATOM   12558 C  CB  . HIS L  1 48  ? 60.140  66.397  26.473  1.00 28.51 ? 48  HIS L CB  1 
ATOM   12559 C  CG  . HIS L  1 48  ? 59.081  67.216  27.135  1.00 28.37 ? 48  HIS L CG  1 
ATOM   12560 N  ND1 . HIS L  1 48  ? 58.343  66.752  28.203  1.00 30.45 ? 48  HIS L ND1 1 
ATOM   12561 C  CD2 . HIS L  1 48  ? 58.643  68.475  26.894  1.00 29.20 ? 48  HIS L CD2 1 
ATOM   12562 C  CE1 . HIS L  1 48  ? 57.484  67.683  28.580  1.00 29.01 ? 48  HIS L CE1 1 
ATOM   12563 N  NE2 . HIS L  1 48  ? 57.652  68.741  27.807  1.00 28.66 ? 48  HIS L NE2 1 
ATOM   12564 N  N   . GLU L  1 49  ? 62.794  64.933  27.234  1.00 38.98 ? 49  GLU L N   1 
ATOM   12565 C  CA  . GLU L  1 49  ? 63.969  64.046  27.202  1.00 33.42 ? 49  GLU L CA  1 
ATOM   12566 C  C   . GLU L  1 49  ? 64.057  63.114  25.990  1.00 33.50 ? 49  GLU L C   1 
ATOM   12567 O  O   . GLU L  1 49  ? 65.144  62.879  25.457  1.00 36.59 ? 49  GLU L O   1 
ATOM   12568 C  CB  . GLU L  1 49  ? 64.051  63.223  28.496  1.00 35.40 ? 49  GLU L CB  1 
ATOM   12569 C  CG  . GLU L  1 49  ? 65.328  62.395  28.639  1.00 37.04 ? 49  GLU L CG  1 
ATOM   12570 C  CD  . GLU L  1 49  ? 65.392  61.602  29.953  1.00 39.55 ? 49  GLU L CD  1 
ATOM   12571 O  OE1 . GLU L  1 49  ? 64.356  61.501  30.666  1.00 31.05 ? 49  GLU L OE1 1 
ATOM   12572 O  OE2 . GLU L  1 49  ? 66.494  61.086  30.265  1.00 34.60 ? 49  GLU L OE2 1 
ATOM   12573 N  N   . PHE L  1 50  ? 62.911  62.605  25.555  1.00 36.65 ? 50  PHE L N   1 
ATOM   12574 C  CA  . PHE L  1 50  ? 62.856  61.577  24.514  1.00 44.34 ? 50  PHE L CA  1 
ATOM   12575 C  C   . PHE L  1 50  ? 62.311  62.065  23.174  1.00 41.28 ? 50  PHE L C   1 
ATOM   12576 O  O   . PHE L  1 50  ? 61.164  62.505  23.086  1.00 42.35 ? 50  PHE L O   1 
ATOM   12577 C  CB  . PHE L  1 50  ? 62.009  60.399  25.011  1.00 41.34 ? 50  PHE L CB  1 
ATOM   12578 C  CG  . PHE L  1 50  ? 62.518  59.807  26.286  1.00 39.36 ? 50  PHE L CG  1 
ATOM   12579 C  CD1 . PHE L  1 50  ? 63.886  59.671  26.497  1.00 40.30 ? 50  PHE L CD1 1 
ATOM   12580 C  CD2 . PHE L  1 50  ? 61.645  59.418  27.286  1.00 40.68 ? 50  PHE L CD2 1 
ATOM   12581 C  CE1 . PHE L  1 50  ? 64.371  59.135  27.676  1.00 39.62 ? 50  PHE L CE1 1 
ATOM   12582 C  CE2 . PHE L  1 50  ? 62.123  58.883  28.462  1.00 37.80 ? 50  PHE L CE2 1 
ATOM   12583 C  CZ  . PHE L  1 50  ? 63.486  58.742  28.658  1.00 33.03 ? 50  PHE L CZ  1 
ATOM   12584 N  N   . GLY L  1 51  ? 63.131  61.959  22.128  1.00 40.15 ? 51  GLY L N   1 
ATOM   12585 C  CA  . GLY L  1 51  ? 62.667  62.185  20.770  1.00 38.85 ? 51  GLY L CA  1 
ATOM   12586 C  C   . GLY L  1 51  ? 61.826  61.016  20.294  1.00 44.03 ? 51  GLY L C   1 
ATOM   12587 O  O   . GLY L  1 51  ? 62.104  60.421  19.253  1.00 44.38 ? 51  GLY L O   1 
ATOM   12588 N  N   . ASP L  1 52  ? 60.786  60.703  21.066  1.00 45.12 ? 52  ASP L N   1 
ATOM   12589 C  CA  . ASP L  1 52  ? 59.987  59.505  20.888  1.00 46.26 ? 52  ASP L CA  1 
ATOM   12590 C  C   . ASP L  1 52  ? 58.505  59.856  20.862  1.00 56.05 ? 52  ASP L C   1 
ATOM   12591 O  O   . ASP L  1 52  ? 57.939  60.247  21.881  1.00 53.80 ? 52  ASP L O   1 
ATOM   12592 C  CB  . ASP L  1 52  ? 60.261  58.561  22.052  1.00 50.28 ? 52  ASP L CB  1 
ATOM   12593 C  CG  . ASP L  1 52  ? 59.274  57.421  22.124  1.00 58.08 ? 52  ASP L CG  1 
ATOM   12594 O  OD1 . ASP L  1 52  ? 58.174  57.613  22.681  1.00 59.24 ? 52  ASP L OD1 1 
ATOM   12595 O  OD2 . ASP L  1 52  ? 59.604  56.322  21.638  1.00 58.13 ? 52  ASP L OD2 1 
ATOM   12596 N  N   . ASN L  1 53  ? 57.872  59.714  19.701  1.00 63.05 ? 53  ASN L N   1 
ATOM   12597 C  CA  . ASN L  1 53  ? 56.450  60.042  19.574  1.00 67.94 ? 53  ASN L CA  1 
ATOM   12598 C  C   . ASN L  1 53  ? 55.551  58.832  19.311  1.00 68.86 ? 53  ASN L C   1 
ATOM   12599 O  O   . ASN L  1 53  ? 54.430  58.982  18.813  1.00 66.96 ? 53  ASN L O   1 
ATOM   12600 C  CB  . ASN L  1 53  ? 56.221  61.090  18.481  1.00 70.77 ? 53  ASN L CB  1 
ATOM   12601 C  CG  . ASN L  1 53  ? 56.425  60.524  17.082  1.00 80.02 ? 53  ASN L CG  1 
ATOM   12602 O  OD1 . ASN L  1 53  ? 57.327  59.714  16.861  1.00 79.54 ? 53  ASN L OD1 1 
ATOM   12603 N  ND2 . ASN L  1 53  ? 55.582  60.941  16.133  1.00 74.83 ? 53  ASN L ND2 1 
ATOM   12604 N  N   . THR L  1 54  ? 56.039  57.641  19.651  1.00 67.07 ? 54  THR L N   1 
ATOM   12605 C  CA  . THR L  1 54  ? 55.285  56.412  19.413  1.00 69.26 ? 54  THR L CA  1 
ATOM   12606 C  C   . THR L  1 54  ? 53.955  56.427  20.159  1.00 68.78 ? 54  THR L C   1 
ATOM   12607 O  O   . THR L  1 54  ? 52.985  55.807  19.727  1.00 68.98 ? 54  THR L O   1 
ATOM   12608 C  CB  . THR L  1 54  ? 56.087  55.162  19.812  1.00 65.16 ? 54  THR L CB  1 
ATOM   12609 O  OG1 . THR L  1 54  ? 56.339  55.182  21.224  1.00 67.86 ? 54  THR L OG1 1 
ATOM   12610 C  CG2 . THR L  1 54  ? 57.405  55.122  19.054  1.00 61.85 ? 54  THR L CG2 1 
ATOM   12611 N  N   . ALA L  1 55  ? 53.925  57.134  21.283  1.00 64.79 ? 55  ALA L N   1 
ATOM   12612 C  CA  . ALA L  1 55  ? 52.679  57.415  21.976  1.00 65.06 ? 55  ALA L CA  1 
ATOM   12613 C  C   . ALA L  1 55  ? 52.422  58.918  21.926  1.00 65.80 ? 55  ALA L C   1 
ATOM   12614 O  O   . ALA L  1 55  ? 51.882  59.499  22.869  1.00 62.43 ? 55  ALA L O   1 
ATOM   12615 C  CB  . ALA L  1 55  ? 52.731  56.914  23.412  1.00 67.07 ? 55  ALA L CB  1 
ATOM   12616 N  N   . GLY L  1 56  ? 52.828  59.536  20.815  1.00 67.26 ? 56  GLY L N   1 
ATOM   12617 C  CA  . GLY L  1 56  ? 52.602  60.953  20.567  1.00 66.49 ? 56  GLY L CA  1 
ATOM   12618 C  C   . GLY L  1 56  ? 53.528  61.904  21.312  1.00 68.86 ? 56  GLY L C   1 
ATOM   12619 O  O   . GLY L  1 56  ? 54.705  61.605  21.551  1.00 69.68 ? 56  GLY L O   1 
ATOM   12620 N  N   . SER L  1 57  ? 52.997  63.068  21.674  1.00 65.52 ? 57  SER L N   1 
ATOM   12621 C  CA  . SER L  1 57  ? 53.738  64.022  22.496  1.00 60.42 ? 57  SER L CA  1 
ATOM   12622 C  C   . SER L  1 57  ? 53.966  63.487  23.920  1.00 60.61 ? 57  SER L C   1 
ATOM   12623 O  O   . SER L  1 57  ? 54.952  63.832  24.574  1.00 60.54 ? 57  SER L O   1 
ATOM   12624 C  CB  . SER L  1 57  ? 53.006  65.366  22.533  1.00 54.41 ? 57  SER L CB  1 
ATOM   12625 O  OG  . SER L  1 57  ? 51.610  65.172  22.682  1.00 50.50 ? 57  SER L OG  1 
ATOM   12626 N  N   . THR L  1 58  ? 53.065  62.617  24.368  1.00 59.01 ? 58  THR L N   1 
ATOM   12627 C  CA  . THR L  1 58  ? 53.032  62.131  25.744  1.00 56.03 ? 58  THR L CA  1 
ATOM   12628 C  C   . THR L  1 58  ? 54.132  61.118  26.121  1.00 57.60 ? 58  THR L C   1 
ATOM   12629 O  O   . THR L  1 58  ? 54.362  60.846  27.301  1.00 52.10 ? 58  THR L O   1 
ATOM   12630 C  CB  . THR L  1 58  ? 51.653  61.537  26.037  1.00 60.47 ? 58  THR L CB  1 
ATOM   12631 O  OG1 . THR L  1 58  ? 51.374  60.504  25.084  1.00 61.31 ? 58  THR L OG1 1 
ATOM   12632 C  CG2 . THR L  1 58  ? 50.591  62.622  25.903  1.00 61.48 ? 58  THR L CG2 1 
ATOM   12633 N  N   . SER L  1 59  ? 54.818  60.566  25.127  1.00 57.51 ? 59  SER L N   1 
ATOM   12634 C  CA  . SER L  1 59  ? 55.911  59.636  25.410  1.00 58.32 ? 59  SER L CA  1 
ATOM   12635 C  C   . SER L  1 59  ? 57.291  60.262  25.177  1.00 57.09 ? 59  SER L C   1 
ATOM   12636 O  O   . SER L  1 59  ? 58.267  59.553  24.918  1.00 57.93 ? 59  SER L O   1 
ATOM   12637 C  CB  . SER L  1 59  ? 55.768  58.358  24.578  1.00 60.97 ? 59  SER L CB  1 
ATOM   12638 O  OG  . SER L  1 59  ? 56.023  58.601  23.203  1.00 55.60 ? 59  SER L OG  1 
ATOM   12639 N  N   . ALA L  1 60  ? 57.376  61.586  25.270  1.00 54.11 ? 60  ALA L N   1 
ATOM   12640 C  CA  . ALA L  1 60  ? 58.651  62.277  25.072  1.00 50.45 ? 60  ALA L CA  1 
ATOM   12641 C  C   . ALA L  1 60  ? 59.426  62.401  26.391  1.00 46.50 ? 60  ALA L C   1 
ATOM   12642 O  O   . ALA L  1 60  ? 60.592  62.819  26.415  1.00 45.54 ? 60  ALA L O   1 
ATOM   12643 C  CB  . ALA L  1 60  ? 58.430  63.651  24.433  1.00 39.69 ? 60  ALA L CB  1 
ATOM   12644 N  N   . GLY L  1 61  ? 58.774  62.035  27.487  1.00 36.40 ? 61  GLY L N   1 
ATOM   12645 C  CA  . GLY L  1 61  ? 59.433  62.042  28.777  1.00 38.73 ? 61  GLY L CA  1 
ATOM   12646 C  C   . GLY L  1 61  ? 59.211  63.336  29.532  1.00 35.72 ? 61  GLY L C   1 
ATOM   12647 O  O   . GLY L  1 61  ? 58.343  64.134  29.166  1.00 36.03 ? 61  GLY L O   1 
ATOM   12648 N  N   . PRO L  1 62  ? 59.953  63.532  30.635  1.00 35.96 ? 62  PRO L N   1 
ATOM   12649 C  CA  . PRO L  1 62  ? 59.851  64.795  31.370  1.00 31.11 ? 62  PRO L CA  1 
ATOM   12650 C  C   . PRO L  1 62  ? 60.761  65.819  30.702  1.00 32.60 ? 62  PRO L C   1 
ATOM   12651 O  O   . PRO L  1 62  ? 61.313  65.535  29.615  1.00 28.52 ? 62  PRO L O   1 
ATOM   12652 C  CB  . PRO L  1 62  ? 60.376  64.423  32.749  1.00 32.26 ? 62  PRO L CB  1 
ATOM   12653 C  CG  . PRO L  1 62  ? 61.419  63.373  32.459  1.00 31.30 ? 62  PRO L CG  1 
ATOM   12654 C  CD  . PRO L  1 62  ? 60.942  62.620  31.238  1.00 36.25 ? 62  PRO L CD  1 
ATOM   12655 N  N   . HIS L  1 63  ? 60.921  66.986  31.321  1.00 25.98 ? 63  HIS L N   1 
ATOM   12656 C  CA  . HIS L  1 63  ? 61.819  67.986  30.756  1.00 27.70 ? 63  HIS L CA  1 
ATOM   12657 C  C   . HIS L  1 63  ? 63.223  67.403  30.647  1.00 24.80 ? 63  HIS L C   1 
ATOM   12658 O  O   . HIS L  1 63  ? 63.655  66.653  31.514  1.00 29.66 ? 63  HIS L O   1 
ATOM   12659 C  CB  . HIS L  1 63  ? 61.805  69.279  31.581  1.00 21.11 ? 63  HIS L CB  1 
ATOM   12660 C  CG  . HIS L  1 63  ? 60.449  69.907  31.696  1.00 26.27 ? 63  HIS L CG  1 
ATOM   12661 N  ND1 . HIS L  1 63  ? 60.210  71.031  32.457  1.00 25.04 ? 63  HIS L ND1 1 
ATOM   12662 C  CD2 . HIS L  1 63  ? 59.256  69.563  31.149  1.00 29.79 ? 63  HIS L CD2 1 
ATOM   12663 C  CE1 . HIS L  1 63  ? 58.930  71.351  32.375  1.00 28.41 ? 63  HIS L CE1 1 
ATOM   12664 N  NE2 . HIS L  1 63  ? 58.329  70.477  31.587  1.00 27.40 ? 63  HIS L NE2 1 
ATOM   12665 N  N   . PHE L  1 64  ? 63.922  67.711  29.562  1.00 25.80 ? 64  PHE L N   1 
ATOM   12666 C  CA  . PHE L  1 64  ? 65.294  67.253  29.410  1.00 27.26 ? 64  PHE L CA  1 
ATOM   12667 C  C   . PHE L  1 64  ? 66.167  67.823  30.540  1.00 27.85 ? 64  PHE L C   1 
ATOM   12668 O  O   . PHE L  1 64  ? 66.466  69.018  30.561  1.00 25.45 ? 64  PHE L O   1 
ATOM   12669 C  CB  . PHE L  1 64  ? 65.835  67.665  28.048  1.00 27.47 ? 64  PHE L CB  1 
ATOM   12670 C  CG  . PHE L  1 64  ? 67.247  67.224  27.800  1.00 27.74 ? 64  PHE L CG  1 
ATOM   12671 C  CD1 . PHE L  1 64  ? 67.640  65.926  28.076  1.00 27.80 ? 64  PHE L CD1 1 
ATOM   12672 C  CD2 . PHE L  1 64  ? 68.176  68.099  27.265  1.00 26.69 ? 64  PHE L CD2 1 
ATOM   12673 C  CE1 . PHE L  1 64  ? 68.942  65.520  27.840  1.00 24.70 ? 64  PHE L CE1 1 
ATOM   12674 C  CE2 . PHE L  1 64  ? 69.480  67.692  27.022  1.00 28.05 ? 64  PHE L CE2 1 
ATOM   12675 C  CZ  . PHE L  1 64  ? 69.859  66.406  27.312  1.00 25.51 ? 64  PHE L CZ  1 
ATOM   12676 N  N   . ASN L  1 65  ? 66.575  66.956  31.468  1.00 29.75 ? 65  ASN L N   1 
ATOM   12677 C  CA  . ASN L  1 65  ? 67.225  67.379  32.711  1.00 26.53 ? 65  ASN L CA  1 
ATOM   12678 C  C   . ASN L  1 65  ? 68.462  66.550  33.036  1.00 29.53 ? 65  ASN L C   1 
ATOM   12679 O  O   . ASN L  1 65  ? 68.453  65.778  33.992  1.00 32.95 ? 65  ASN L O   1 
ATOM   12680 C  CB  . ASN L  1 65  ? 66.214  67.264  33.863  1.00 23.91 ? 65  ASN L CB  1 
ATOM   12681 C  CG  . ASN L  1 65  ? 66.708  67.893  35.181  1.00 24.24 ? 65  ASN L CG  1 
ATOM   12682 O  OD1 . ASN L  1 65  ? 67.610  68.726  35.203  1.00 22.96 ? 65  ASN L OD1 1 
ATOM   12683 N  ND2 . ASN L  1 65  ? 66.084  67.497  36.277  1.00 15.22 ? 65  ASN L ND2 1 
ATOM   12684 N  N   . PRO L  1 66  ? 69.535  66.696  32.248  1.00 28.55 ? 66  PRO L N   1 
ATOM   12685 C  CA  . PRO L  1 66  ? 70.696  65.850  32.540  1.00 29.30 ? 66  PRO L CA  1 
ATOM   12686 C  C   . PRO L  1 66  ? 71.457  66.263  33.802  1.00 36.27 ? 66  PRO L C   1 
ATOM   12687 O  O   . PRO L  1 66  ? 72.258  65.469  34.297  1.00 39.41 ? 66  PRO L O   1 
ATOM   12688 C  CB  . PRO L  1 66  ? 71.585  66.031  31.302  1.00 28.72 ? 66  PRO L CB  1 
ATOM   12689 C  CG  . PRO L  1 66  ? 71.217  67.368  30.772  1.00 29.36 ? 66  PRO L CG  1 
ATOM   12690 C  CD  . PRO L  1 66  ? 69.737  67.512  31.039  1.00 27.75 ? 66  PRO L CD  1 
ATOM   12691 N  N   . LEU L  1 67  ? 71.218  67.464  34.322  1.00 33.80 ? 67  LEU L N   1 
ATOM   12692 C  CA  . LEU L  1 67  ? 71.969  67.921  35.489  1.00 32.93 ? 67  LEU L CA  1 
ATOM   12693 C  C   . LEU L  1 67  ? 71.187  67.750  36.786  1.00 34.28 ? 67  LEU L C   1 
ATOM   12694 O  O   . LEU L  1 67  ? 71.681  68.076  37.864  1.00 39.00 ? 67  LEU L O   1 
ATOM   12695 C  CB  . LEU L  1 67  ? 72.419  69.367  35.331  1.00 27.82 ? 67  LEU L CB  1 
ATOM   12696 C  CG  . LEU L  1 67  ? 73.088  69.723  34.002  1.00 30.55 ? 67  LEU L CG  1 
ATOM   12697 C  CD1 . LEU L  1 67  ? 73.761  71.077  34.094  1.00 27.93 ? 67  LEU L CD1 1 
ATOM   12698 C  CD2 . LEU L  1 67  ? 74.090  68.659  33.561  1.00 42.13 ? 67  LEU L CD2 1 
ATOM   12699 N  N   . SER L  1 68  ? 69.975  67.223  36.671  1.00 29.68 ? 68  SER L N   1 
ATOM   12700 C  CA  . SER L  1 68  ? 69.132  66.970  37.828  1.00 29.61 ? 68  SER L CA  1 
ATOM   12701 C  C   . SER L  1 68  ? 68.851  68.232  38.661  1.00 36.23 ? 68  SER L C   1 
ATOM   12702 O  O   . SER L  1 68  ? 68.897  68.195  39.894  1.00 36.43 ? 68  SER L O   1 
ATOM   12703 C  CB  . SER L  1 68  ? 69.743  65.865  38.708  1.00 38.62 ? 68  SER L CB  1 
ATOM   12704 O  OG  . SER L  1 68  ? 69.906  64.652  37.985  1.00 43.17 ? 68  SER L OG  1 
ATOM   12705 N  N   . ARG L  1 69  ? 68.549  69.342  37.991  1.00 35.04 ? 69  ARG L N   1 
ATOM   12706 C  CA  . ARG L  1 69  ? 68.144  70.564  38.686  1.00 27.09 ? 69  ARG L CA  1 
ATOM   12707 C  C   . ARG L  1 69  ? 66.637  70.629  38.784  1.00 23.86 ? 69  ARG L C   1 
ATOM   12708 O  O   . ARG L  1 69  ? 65.931  69.755  38.278  1.00 24.67 ? 69  ARG L O   1 
ATOM   12709 C  CB  . ARG L  1 69  ? 68.644  71.804  37.942  1.00 30.01 ? 69  ARG L CB  1 
ATOM   12710 C  CG  . ARG L  1 69  ? 69.972  71.619  37.262  1.00 31.73 ? 69  ARG L CG  1 
ATOM   12711 C  CD  . ARG L  1 69  ? 71.127  71.786  38.221  1.00 30.39 ? 69  ARG L CD  1 
ATOM   12712 N  NE  . ARG L  1 69  ? 71.494  73.191  38.365  1.00 40.29 ? 69  ARG L NE  1 
ATOM   12713 C  CZ  . ARG L  1 69  ? 72.421  73.816  37.636  1.00 43.00 ? 69  ARG L CZ  1 
ATOM   12714 N  NH1 . ARG L  1 69  ? 73.097  73.164  36.695  1.00 42.50 ? 69  ARG L NH1 1 
ATOM   12715 N  NH2 . ARG L  1 69  ? 72.676  75.105  37.854  1.00 41.67 ? 69  ARG L NH2 1 
ATOM   12716 N  N   . LYS L  1 70  ? 66.140  71.677  39.433  1.00 25.64 ? 70  LYS L N   1 
ATOM   12717 C  CA  . LYS L  1 70  ? 64.708  71.939  39.478  1.00 23.66 ? 70  LYS L CA  1 
ATOM   12718 C  C   . LYS L  1 70  ? 64.226  72.758  38.278  1.00 20.32 ? 70  LYS L C   1 
ATOM   12719 O  O   . LYS L  1 70  ? 65.025  73.380  37.581  1.00 18.61 ? 70  LYS L O   1 
ATOM   12720 C  CB  . LYS L  1 70  ? 64.342  72.679  40.771  1.00 25.77 ? 70  LYS L CB  1 
ATOM   12721 C  CG  . LYS L  1 70  ? 64.641  71.899  42.036  1.00 29.55 ? 70  LYS L CG  1 
ATOM   12722 C  CD  . LYS L  1 70  ? 64.221  70.452  41.883  1.00 32.72 ? 70  LYS L CD  1 
ATOM   12723 C  CE  . LYS L  1 70  ? 62.704  70.295  41.811  1.00 33.60 ? 70  LYS L CE  1 
ATOM   12724 N  NZ  . LYS L  1 70  ? 62.316  68.985  41.169  1.00 37.82 ? 70  LYS L NZ  1 
ATOM   12725 N  N   . HIS L  1 71  ? 62.915  72.767  38.056  1.00 22.22 ? 71  HIS L N   1 
ATOM   12726 C  CA  . HIS L  1 71  ? 62.319  73.563  36.974  1.00 21.30 ? 71  HIS L CA  1 
ATOM   12727 C  C   . HIS L  1 71  ? 62.437  75.067  37.222  1.00 22.24 ? 71  HIS L C   1 
ATOM   12728 O  O   . HIS L  1 71  ? 62.057  75.553  38.295  1.00 16.99 ? 71  HIS L O   1 
ATOM   12729 C  CB  . HIS L  1 71  ? 60.834  73.214  36.775  1.00 18.27 ? 71  HIS L CB  1 
ATOM   12730 C  CG  . HIS L  1 71  ? 60.186  73.988  35.668  1.00 23.54 ? 71  HIS L CG  1 
ATOM   12731 N  ND1 . HIS L  1 71  ? 60.258  73.596  34.347  1.00 18.60 ? 71  HIS L ND1 1 
ATOM   12732 C  CD2 . HIS L  1 71  ? 59.493  75.154  35.678  1.00 20.15 ? 71  HIS L CD2 1 
ATOM   12733 C  CE1 . HIS L  1 71  ? 59.632  74.483  33.595  1.00 22.18 ? 71  HIS L CE1 1 
ATOM   12734 N  NE2 . HIS L  1 71  ? 59.153  75.433  34.378  1.00 22.72 ? 71  HIS L NE2 1 
ATOM   12735 N  N   . GLY L  1 72  ? 62.938  75.794  36.218  1.00 19.57 ? 72  GLY L N   1 
ATOM   12736 C  CA  . GLY L  1 72  ? 62.941  77.254  36.223  1.00 17.82 ? 72  GLY L CA  1 
ATOM   12737 C  C   . GLY L  1 72  ? 62.544  77.852  34.873  1.00 20.43 ? 72  GLY L C   1 
ATOM   12738 O  O   . GLY L  1 72  ? 62.064  77.153  33.970  1.00 19.53 ? 72  GLY L O   1 
ATOM   12739 N  N   . GLY L  1 73  ? 62.735  79.158  34.730  1.00 20.24 ? 73  GLY L N   1 
ATOM   12740 C  CA  . GLY L  1 73  ? 62.635  79.792  33.430  1.00 19.03 ? 73  GLY L CA  1 
ATOM   12741 C  C   . GLY L  1 73  ? 64.017  79.780  32.812  1.00 18.60 ? 73  GLY L C   1 
ATOM   12742 O  O   . GLY L  1 73  ? 64.981  79.443  33.499  1.00 17.67 ? 73  GLY L O   1 
ATOM   12743 N  N   . PRO L  1 74  ? 64.129  80.143  31.519  1.00 20.63 ? 74  PRO L N   1 
ATOM   12744 C  CA  . PRO L  1 74  ? 65.432  80.069  30.844  1.00 17.75 ? 74  PRO L CA  1 
ATOM   12745 C  C   . PRO L  1 74  ? 66.479  80.991  31.433  1.00 20.75 ? 74  PRO L C   1 
ATOM   12746 O  O   . PRO L  1 74  ? 67.674  80.726  31.288  1.00 21.46 ? 74  PRO L O   1 
ATOM   12747 C  CB  . PRO L  1 74  ? 65.121  80.490  29.394  1.00 17.65 ? 74  PRO L CB  1 
ATOM   12748 C  CG  . PRO L  1 74  ? 63.749  81.125  29.436  1.00 17.47 ? 74  PRO L CG  1 
ATOM   12749 C  CD  . PRO L  1 74  ? 63.034  80.455  30.581  1.00 17.57 ? 74  PRO L CD  1 
ATOM   12750 N  N   . LYS L  1 75  ? 66.051  82.067  32.077  1.00 21.59 ? 75  LYS L N   1 
ATOM   12751 C  CA  . LYS L  1 75  ? 67.003  83.030  32.606  1.00 21.35 ? 75  LYS L CA  1 
ATOM   12752 C  C   . LYS L  1 75  ? 67.626  82.579  33.924  1.00 17.30 ? 75  LYS L C   1 
ATOM   12753 O  O   . LYS L  1 75  ? 68.661  83.097  34.325  1.00 21.32 ? 75  LYS L O   1 
ATOM   12754 C  CB  . LYS L  1 75  ? 66.360  84.418  32.765  1.00 22.18 ? 75  LYS L CB  1 
ATOM   12755 C  CG  . LYS L  1 75  ? 65.871  85.040  31.456  1.00 25.28 ? 75  LYS L CG  1 
ATOM   12756 C  CD  . LYS L  1 75  ? 65.013  86.316  31.681  1.00 26.62 ? 75  LYS L CD  1 
ATOM   12757 C  CE  . LYS L  1 75  ? 65.518  87.171  32.861  1.00 32.61 ? 75  LYS L CE  1 
ATOM   12758 N  NZ  . LYS L  1 75  ? 65.097  88.617  32.780  1.00 24.36 ? 75  LYS L NZ  1 
ATOM   12759 N  N   . ASP L  1 76  ? 67.004  81.620  34.599  1.00 21.47 ? 76  ASP L N   1 
ATOM   12760 C  CA  . ASP L  1 76  ? 67.465  81.200  35.931  1.00 20.15 ? 76  ASP L CA  1 
ATOM   12761 C  C   . ASP L  1 76  ? 68.698  80.302  35.837  1.00 22.37 ? 76  ASP L C   1 
ATOM   12762 O  O   . ASP L  1 76  ? 68.891  79.601  34.847  1.00 21.28 ? 76  ASP L O   1 
ATOM   12763 C  CB  . ASP L  1 76  ? 66.370  80.423  36.676  1.00 19.15 ? 76  ASP L CB  1 
ATOM   12764 C  CG  . ASP L  1 76  ? 65.116  81.231  36.911  1.00 21.54 ? 76  ASP L CG  1 
ATOM   12765 O  OD1 . ASP L  1 76  ? 65.220  82.408  37.318  1.00 25.53 ? 76  ASP L OD1 1 
ATOM   12766 O  OD2 . ASP L  1 76  ? 64.017  80.672  36.707  1.00 20.53 ? 76  ASP L OD2 1 
ATOM   12767 N  N   . GLU L  1 77  ? 69.524  80.308  36.875  1.00 23.69 ? 77  GLU L N   1 
ATOM   12768 C  CA  . GLU L  1 77  ? 70.617  79.350  36.957  1.00 25.07 ? 77  GLU L CA  1 
ATOM   12769 C  C   . GLU L  1 77  ? 70.045  77.970  37.291  1.00 24.21 ? 77  GLU L C   1 
ATOM   12770 O  O   . GLU L  1 77  ? 70.490  76.947  36.774  1.00 26.42 ? 77  GLU L O   1 
ATOM   12771 C  CB  . GLU L  1 77  ? 71.659  79.804  37.985  1.00 27.46 ? 77  GLU L CB  1 
ATOM   12772 C  CG  . GLU L  1 77  ? 72.721  78.755  38.354  1.00 37.73 ? 77  GLU L CG  1 
ATOM   12773 C  CD  . GLU L  1 77  ? 73.726  78.455  37.241  1.00 45.14 ? 77  GLU L CD  1 
ATOM   12774 O  OE1 . GLU L  1 77  ? 73.716  79.154  36.202  1.00 52.09 ? 77  GLU L OE1 1 
ATOM   12775 O  OE2 . GLU L  1 77  ? 74.535  77.511  37.410  1.00 47.16 ? 77  GLU L OE2 1 
ATOM   12776 N  N   . GLU L  1 78  ? 69.029  77.955  38.140  1.00 24.80 ? 78  GLU L N   1 
ATOM   12777 C  CA  . GLU L  1 78  ? 68.355  76.725  38.515  1.00 21.83 ? 78  GLU L CA  1 
ATOM   12778 C  C   . GLU L  1 78  ? 67.211  76.458  37.543  1.00 21.33 ? 78  GLU L C   1 
ATOM   12779 O  O   . GLU L  1 78  ? 66.121  77.019  37.686  1.00 19.67 ? 78  GLU L O   1 
ATOM   12780 C  CB  . GLU L  1 78  ? 67.825  76.849  39.949  1.00 20.58 ? 78  GLU L CB  1 
ATOM   12781 C  CG  . GLU L  1 78  ? 67.166  75.581  40.519  1.00 22.53 ? 78  GLU L CG  1 
ATOM   12782 C  CD  . GLU L  1 78  ? 68.174  74.470  40.826  1.00 26.86 ? 78  GLU L CD  1 
ATOM   12783 O  OE1 . GLU L  1 78  ? 69.387  74.757  40.939  1.00 27.95 ? 78  GLU L OE1 1 
ATOM   12784 O  OE2 . GLU L  1 78  ? 67.750  73.302  40.943  1.00 28.61 ? 78  GLU L OE2 1 
ATOM   12785 N  N   . ARG L  1 79  ? 67.463  75.583  36.573  1.00 20.19 ? 79  ARG L N   1 
ATOM   12786 C  CA  . ARG L  1 79  ? 66.521  75.276  35.503  1.00 16.88 ? 79  ARG L CA  1 
ATOM   12787 C  C   . ARG L  1 79  ? 66.844  73.918  34.907  1.00 21.48 ? 79  ARG L C   1 
ATOM   12788 O  O   . ARG L  1 79  ? 67.961  73.422  35.062  1.00 21.18 ? 79  ARG L O   1 
ATOM   12789 C  CB  . ARG L  1 79  ? 66.643  76.315  34.394  1.00 18.87 ? 79  ARG L CB  1 
ATOM   12790 C  CG  . ARG L  1 79  ? 68.060  76.415  33.794  1.00 18.33 ? 79  ARG L CG  1 
ATOM   12791 C  CD  . ARG L  1 79  ? 68.081  77.260  32.508  1.00 19.32 ? 79  ARG L CD  1 
ATOM   12792 N  NE  . ARG L  1 79  ? 67.631  76.505  31.343  1.00 19.10 ? 79  ARG L NE  1 
ATOM   12793 C  CZ  . ARG L  1 79  ? 67.728  76.935  30.078  1.00 21.33 ? 79  ARG L CZ  1 
ATOM   12794 N  NH1 . ARG L  1 79  ? 68.252  78.129  29.788  1.00 12.83 ? 79  ARG L NH1 1 
ATOM   12795 N  NH2 . ARG L  1 79  ? 67.293  76.164  29.097  1.00 20.55 ? 79  ARG L NH2 1 
ATOM   12796 N  N   . HIS L  1 80  ? 65.882  73.315  34.205  1.00 19.30 ? 80  HIS L N   1 
ATOM   12797 C  CA  . HIS L  1 80  ? 66.195  72.132  33.407  1.00 18.79 ? 80  HIS L CA  1 
ATOM   12798 C  C   . HIS L  1 80  ? 66.894  72.586  32.132  1.00 22.20 ? 80  HIS L C   1 
ATOM   12799 O  O   . HIS L  1 80  ? 66.711  73.727  31.704  1.00 18.45 ? 80  HIS L O   1 
ATOM   12800 C  CB  . HIS L  1 80  ? 64.934  71.347  33.053  1.00 21.11 ? 80  HIS L CB  1 
ATOM   12801 C  CG  . HIS L  1 80  ? 64.144  70.901  34.238  1.00 19.93 ? 80  HIS L CG  1 
ATOM   12802 N  ND1 . HIS L  1 80  ? 62.772  71.001  34.291  1.00 19.02 ? 80  HIS L ND1 1 
ATOM   12803 C  CD2 . HIS L  1 80  ? 64.527  70.332  35.409  1.00 19.15 ? 80  HIS L CD2 1 
ATOM   12804 C  CE1 . HIS L  1 80  ? 62.342  70.514  35.441  1.00 19.96 ? 80  HIS L CE1 1 
ATOM   12805 N  NE2 . HIS L  1 80  ? 63.386  70.109  36.142  1.00 17.03 ? 80  HIS L NE2 1 
ATOM   12806 N  N   . VAL L  1 81  ? 67.701  71.717  31.527  1.00 23.30 ? 81  VAL L N   1 
ATOM   12807 C  CA  . VAL L  1 81  ? 68.326  72.082  30.252  1.00 25.99 ? 81  VAL L CA  1 
ATOM   12808 C  C   . VAL L  1 81  ? 67.251  72.457  29.238  1.00 21.57 ? 81  VAL L C   1 
ATOM   12809 O  O   . VAL L  1 81  ? 67.428  73.387  28.466  1.00 23.49 ? 81  VAL L O   1 
ATOM   12810 C  CB  . VAL L  1 81  ? 69.261  70.991  29.691  1.00 26.56 ? 81  VAL L CB  1 
ATOM   12811 C  CG1 . VAL L  1 81  ? 69.716  71.344  28.258  1.00 24.56 ? 81  VAL L CG1 1 
ATOM   12812 C  CG2 . VAL L  1 81  ? 70.472  70.844  30.593  1.00 25.02 ? 81  VAL L CG2 1 
ATOM   12813 N  N   . GLY L  1 82  ? 66.110  71.780  29.299  1.00 20.99 ? 82  GLY L N   1 
ATOM   12814 C  CA  . GLY L  1 82  ? 65.047  72.015  28.344  1.00 23.73 ? 82  GLY L CA  1 
ATOM   12815 C  C   . GLY L  1 82  ? 64.008  73.068  28.705  1.00 24.61 ? 82  GLY L C   1 
ATOM   12816 O  O   . GLY L  1 82  ? 62.947  73.115  28.085  1.00 29.66 ? 82  GLY L O   1 
ATOM   12817 N  N   . ASP L  1 83  ? 64.295  73.910  29.690  1.00 20.48 ? 83  ASP L N   1 
ATOM   12818 C  CA  . ASP L  1 83  ? 63.334  74.926  30.115  1.00 22.27 ? 83  ASP L CA  1 
ATOM   12819 C  C   . ASP L  1 83  ? 63.534  76.164  29.247  1.00 21.65 ? 83  ASP L C   1 
ATOM   12820 O  O   . ASP L  1 83  ? 64.388  77.000  29.521  1.00 22.38 ? 83  ASP L O   1 
ATOM   12821 C  CB  . ASP L  1 83  ? 63.505  75.270  31.594  1.00 22.30 ? 83  ASP L CB  1 
ATOM   12822 C  CG  . ASP L  1 83  ? 63.078  74.131  32.527  1.00 23.02 ? 83  ASP L CG  1 
ATOM   12823 O  OD1 . ASP L  1 83  ? 62.381  73.205  32.079  1.00 23.05 ? 83  ASP L OD1 1 
ATOM   12824 O  OD2 . ASP L  1 83  ? 63.435  74.166  33.722  1.00 21.79 ? 83  ASP L OD2 1 
ATOM   12825 N  N   . LEU L  1 84  ? 62.771  76.266  28.172  1.00 21.64 ? 84  LEU L N   1 
ATOM   12826 C  CA  . LEU L  1 84  ? 62.967  77.385  27.263  1.00 22.62 ? 84  LEU L CA  1 
ATOM   12827 C  C   . LEU L  1 84  ? 61.961  78.485  27.567  1.00 20.12 ? 84  LEU L C   1 
ATOM   12828 O  O   . LEU L  1 84  ? 61.994  79.550  26.964  1.00 23.34 ? 84  LEU L O   1 
ATOM   12829 C  CB  . LEU L  1 84  ? 62.910  76.938  25.789  1.00 24.48 ? 84  LEU L CB  1 
ATOM   12830 C  CG  . LEU L  1 84  ? 64.130  76.159  25.263  1.00 26.44 ? 84  LEU L CG  1 
ATOM   12831 C  CD1 . LEU L  1 84  ? 64.136  76.063  23.738  1.00 22.35 ? 84  LEU L CD1 1 
ATOM   12832 C  CD2 . LEU L  1 84  ? 65.436  76.749  25.738  1.00 23.96 ? 84  LEU L CD2 1 
ATOM   12833 N  N   . GLY L  1 85  ? 61.076  78.240  28.524  1.00 19.31 ? 85  GLY L N   1 
ATOM   12834 C  CA  . GLY L  1 85  ? 60.213  79.301  29.010  1.00 17.02 ? 85  GLY L CA  1 
ATOM   12835 C  C   . GLY L  1 85  ? 58.896  79.364  28.273  1.00 21.24 ? 85  GLY L C   1 
ATOM   12836 O  O   . GLY L  1 85  ? 58.244  78.337  28.086  1.00 21.62 ? 85  GLY L O   1 
ATOM   12837 N  N   . ASN L  1 86  ? 58.472  80.564  27.883  1.00 17.40 ? 86  ASN L N   1 
ATOM   12838 C  CA  . ASN L  1 86  ? 57.211  80.686  27.161  1.00 18.25 ? 86  ASN L CA  1 
ATOM   12839 C  C   . ASN L  1 86  ? 57.401  81.229  25.767  1.00 19.73 ? 86  ASN L C   1 
ATOM   12840 O  O   . ASN L  1 86  ? 58.410  81.882  25.470  1.00 23.24 ? 86  ASN L O   1 
ATOM   12841 C  CB  . ASN L  1 86  ? 56.215  81.563  27.916  1.00 17.16 ? 86  ASN L CB  1 
ATOM   12842 C  CG  . ASN L  1 86  ? 55.721  80.907  29.200  1.00 21.08 ? 86  ASN L CG  1 
ATOM   12843 O  OD1 . ASN L  1 86  ? 55.009  79.906  29.160  1.00 20.51 ? 86  ASN L OD1 1 
ATOM   12844 N  ND2 . ASN L  1 86  ? 56.082  81.482  30.345  1.00 18.47 ? 86  ASN L ND2 1 
ATOM   12845 N  N   . VAL L  1 87  ? 56.428  80.968  24.908  1.00 20.52 ? 87  VAL L N   1 
ATOM   12846 C  CA  . VAL L  1 87  ? 56.351  81.695  23.644  1.00 18.83 ? 87  VAL L CA  1 
ATOM   12847 C  C   . VAL L  1 87  ? 55.022  82.446  23.586  1.00 19.83 ? 87  VAL L C   1 
ATOM   12848 O  O   . VAL L  1 87  ? 54.001  81.955  24.054  1.00 19.65 ? 87  VAL L O   1 
ATOM   12849 C  CB  . VAL L  1 87  ? 56.495  80.769  22.410  1.00 22.44 ? 87  VAL L CB  1 
ATOM   12850 C  CG1 . VAL L  1 87  ? 57.929  80.263  22.299  1.00 22.06 ? 87  VAL L CG1 1 
ATOM   12851 C  CG2 . VAL L  1 87  ? 55.480  79.606  22.477  1.00 18.26 ? 87  VAL L CG2 1 
ATOM   12852 N  N   . THR L  1 88  ? 55.038  83.635  22.997  1.00 19.39 ? 88  THR L N   1 
ATOM   12853 C  CA  . THR L  1 88  ? 53.833  84.450  22.925  1.00 24.31 ? 88  THR L CA  1 
ATOM   12854 C  C   . THR L  1 88  ? 53.226  84.399  21.517  1.00 26.52 ? 88  THR L C   1 
ATOM   12855 O  O   . THR L  1 88  ? 53.899  84.665  20.508  1.00 24.16 ? 88  THR L O   1 
ATOM   12856 C  CB  . THR L  1 88  ? 54.133  85.906  23.306  1.00 21.51 ? 88  THR L CB  1 
ATOM   12857 O  OG1 . THR L  1 88  ? 54.715  85.948  24.611  1.00 20.13 ? 88  THR L OG1 1 
ATOM   12858 C  CG2 . THR L  1 88  ? 52.858  86.749  23.271  1.00 24.14 ? 88  THR L CG2 1 
ATOM   12859 N  N   . ALA L  1 89  ? 51.957  84.029  21.466  1.00 25.07 ? 89  ALA L N   1 
ATOM   12860 C  CA  . ALA L  1 89  ? 51.220  83.991  20.224  1.00 26.10 ? 89  ALA L CA  1 
ATOM   12861 C  C   . ALA L  1 89  ? 50.364  85.258  20.137  1.00 31.51 ? 89  ALA L C   1 
ATOM   12862 O  O   . ALA L  1 89  ? 49.767  85.681  21.141  1.00 28.36 ? 89  ALA L O   1 
ATOM   12863 C  CB  . ALA L  1 89  ? 50.348  82.766  20.199  1.00 30.27 ? 89  ALA L CB  1 
ATOM   12864 N  N   . ASP L  1 90  ? 50.293  85.857  18.947  1.00 26.71 ? 90  ASP L N   1 
ATOM   12865 C  CA  . ASP L  1 90  ? 49.528  87.095  18.792  1.00 29.87 ? 90  ASP L CA  1 
ATOM   12866 C  C   . ASP L  1 90  ? 48.027  86.877  18.673  1.00 25.11 ? 90  ASP L C   1 
ATOM   12867 O  O   . ASP L  1 90  ? 47.529  85.776  18.866  1.00 25.64 ? 90  ASP L O   1 
ATOM   12868 C  CB  . ASP L  1 90  ? 50.045  87.952  17.622  1.00 30.29 ? 90  ASP L CB  1 
ATOM   12869 C  CG  . ASP L  1 90  ? 49.929  87.255  16.267  1.00 29.43 ? 90  ASP L CG  1 
ATOM   12870 O  OD1 . ASP L  1 90  ? 48.978  86.477  16.034  1.00 28.07 ? 90  ASP L OD1 1 
ATOM   12871 O  OD2 . ASP L  1 90  ? 50.810  87.504  15.425  1.00 33.24 ? 90  ASP L OD2 1 
ATOM   12872 N  N   . LYS L  1 91  ? 47.324  87.957  18.360  1.00 33.41 ? 91  LYS L N   1 
ATOM   12873 C  CA  . LYS L  1 91  ? 45.876  87.947  18.165  1.00 35.00 ? 91  LYS L CA  1 
ATOM   12874 C  C   . LYS L  1 91  ? 45.459  87.001  17.017  1.00 33.74 ? 91  LYS L C   1 
ATOM   12875 O  O   . LYS L  1 91  ? 44.368  86.427  17.040  1.00 36.09 ? 91  LYS L O   1 
ATOM   12876 C  CB  . LYS L  1 91  ? 45.399  89.382  17.919  1.00 35.06 ? 91  LYS L CB  1 
ATOM   12877 C  CG  . LYS L  1 91  ? 43.940  89.536  17.577  1.00 46.70 ? 91  LYS L CG  1 
ATOM   12878 C  CD  . LYS L  1 91  ? 43.647  90.958  17.118  1.00 50.99 ? 91  LYS L CD  1 
ATOM   12879 C  CE  . LYS L  1 91  ? 42.258  91.071  16.478  1.00 62.24 ? 91  LYS L CE  1 
ATOM   12880 N  NZ  . LYS L  1 91  ? 41.146  90.831  17.441  1.00 52.84 ? 91  LYS L NZ  1 
ATOM   12881 N  N   . ASP L  1 92  ? 46.333  86.813  16.030  1.00 30.21 ? 92  ASP L N   1 
ATOM   12882 C  CA  . ASP L  1 92  ? 46.046  85.856  14.957  1.00 34.67 ? 92  ASP L CA  1 
ATOM   12883 C  C   . ASP L  1 92  ? 46.489  84.446  15.329  1.00 33.62 ? 92  ASP L C   1 
ATOM   12884 O  O   . ASP L  1 92  ? 46.315  83.511  14.556  1.00 30.15 ? 92  ASP L O   1 
ATOM   12885 C  CB  . ASP L  1 92  ? 46.688  86.276  13.634  1.00 29.96 ? 92  ASP L CB  1 
ATOM   12886 C  CG  . ASP L  1 92  ? 46.211  87.639  13.162  1.00 37.83 ? 92  ASP L CG  1 
ATOM   12887 O  OD1 . ASP L  1 92  ? 45.015  87.952  13.348  1.00 39.07 ? 92  ASP L OD1 1 
ATOM   12888 O  OD2 . ASP L  1 92  ? 47.037  88.400  12.610  1.00 44.12 ? 92  ASP L OD2 1 
ATOM   12889 N  N   . GLY L  1 93  ? 47.065  84.290  16.513  1.00 28.86 ? 93  GLY L N   1 
ATOM   12890 C  CA  . GLY L  1 93  ? 47.422  82.965  16.981  1.00 29.12 ? 93  GLY L CA  1 
ATOM   12891 C  C   . GLY L  1 93  ? 48.771  82.476  16.500  1.00 28.33 ? 93  GLY L C   1 
ATOM   12892 O  O   . GLY L  1 93  ? 49.071  81.294  16.588  1.00 30.37 ? 93  GLY L O   1 
ATOM   12893 N  N   . VAL L  1 94  ? 49.590  83.384  15.986  1.00 25.80 ? 94  VAL L N   1 
ATOM   12894 C  CA  . VAL L  1 94  ? 50.925  83.011  15.534  1.00 28.66 ? 94  VAL L CA  1 
ATOM   12895 C  C   . VAL L  1 94  ? 51.982  83.435  16.546  1.00 27.56 ? 94  VAL L C   1 
ATOM   12896 O  O   . VAL L  1 94  ? 51.976  84.577  17.029  1.00 24.10 ? 94  VAL L O   1 
ATOM   12897 C  CB  . VAL L  1 94  ? 51.265  83.553  14.088  1.00 28.95 ? 94  VAL L CB  1 
ATOM   12898 C  CG1 . VAL L  1 94  ? 50.402  84.740  13.717  1.00 33.75 ? 94  VAL L CG1 1 
ATOM   12899 C  CG2 . VAL L  1 94  ? 52.745  83.900  13.947  1.00 30.65 ? 94  VAL L CG2 1 
ATOM   12900 N  N   . ALA L  1 95  ? 52.873  82.503  16.878  1.00 25.96 ? 95  ALA L N   1 
ATOM   12901 C  CA  . ALA L  1 95  ? 54.013  82.821  17.717  1.00 24.57 ? 95  ALA L CA  1 
ATOM   12902 C  C   . ALA L  1 95  ? 55.245  82.911  16.851  1.00 26.53 ? 95  ALA L C   1 
ATOM   12903 O  O   . ALA L  1 95  ? 55.747  81.904  16.372  1.00 23.80 ? 95  ALA L O   1 
ATOM   12904 C  CB  . ALA L  1 95  ? 54.205  81.770  18.794  1.00 24.56 ? 95  ALA L CB  1 
ATOM   12905 N  N   . ASP L  1 96  ? 55.739  84.123  16.661  1.00 25.69 ? 96  ASP L N   1 
ATOM   12906 C  CA  . ASP L  1 96  ? 56.981  84.317  15.931  1.00 30.08 ? 96  ASP L CA  1 
ATOM   12907 C  C   . ASP L  1 96  ? 58.174  84.134  16.857  1.00 30.14 ? 96  ASP L C   1 
ATOM   12908 O  O   . ASP L  1 96  ? 58.837  85.104  17.243  1.00 25.46 ? 96  ASP L O   1 
ATOM   12909 C  CB  . ASP L  1 96  ? 56.999  85.688  15.246  1.00 31.84 ? 96  ASP L CB  1 
ATOM   12910 C  CG  . ASP L  1 96  ? 56.057  85.741  14.048  1.00 40.10 ? 96  ASP L CG  1 
ATOM   12911 O  OD1 . ASP L  1 96  ? 56.127  84.802  13.220  1.00 45.30 ? 96  ASP L OD1 1 
ATOM   12912 O  OD2 . ASP L  1 96  ? 55.236  86.687  13.944  1.00 34.43 ? 96  ASP L OD2 1 
ATOM   12913 N  N   . VAL L  1 97  ? 58.440  82.869  17.183  1.00 30.90 ? 97  VAL L N   1 
ATOM   12914 C  CA  . VAL L  1 97  ? 59.455  82.491  18.163  1.00 25.09 ? 97  VAL L CA  1 
ATOM   12915 C  C   . VAL L  1 97  ? 60.836  83.090  17.874  1.00 28.74 ? 97  VAL L C   1 
ATOM   12916 O  O   . VAL L  1 97  ? 61.323  83.047  16.753  1.00 24.87 ? 97  VAL L O   1 
ATOM   12917 C  CB  . VAL L  1 97  ? 59.542  80.960  18.271  1.00 29.95 ? 97  VAL L CB  1 
ATOM   12918 C  CG1 . VAL L  1 97  ? 60.608  80.551  19.279  1.00 28.64 ? 97  VAL L CG1 1 
ATOM   12919 C  CG2 . VAL L  1 97  ? 58.170  80.372  18.651  1.00 22.18 ? 97  VAL L CG2 1 
ATOM   12920 N  N   . SER L  1 98  ? 61.460  83.679  18.887  1.00 28.99 ? 98  SER L N   1 
ATOM   12921 C  CA  . SER L  1 98  ? 62.813  84.188  18.712  1.00 28.97 ? 98  SER L CA  1 
ATOM   12922 C  C   . SER L  1 98  ? 63.591  84.140  20.009  1.00 29.59 ? 98  SER L C   1 
ATOM   12923 O  O   . SER L  1 98  ? 63.683  85.133  20.724  1.00 31.68 ? 98  SER L O   1 
ATOM   12924 C  CB  . SER L  1 98  ? 62.814  85.610  18.149  1.00 27.49 ? 98  SER L CB  1 
ATOM   12925 O  OG  . SER L  1 98  ? 64.134  86.126  18.133  1.00 27.10 ? 98  SER L OG  1 
ATOM   12926 N  N   . ILE L  1 99  ? 64.167  82.981  20.297  1.00 33.20 ? 99  ILE L N   1 
ATOM   12927 C  CA  . ILE L  1 99  ? 64.889  82.776  21.537  1.00 24.02 ? 99  ILE L CA  1 
ATOM   12928 C  C   . ILE L  1 99  ? 66.389  82.642  21.291  1.00 28.22 ? 99  ILE L C   1 
ATOM   12929 O  O   . ILE L  1 99  ? 66.823  82.111  20.272  1.00 31.22 ? 99  ILE L O   1 
ATOM   12930 C  CB  . ILE L  1 99  ? 64.323  81.550  22.263  1.00 24.17 ? 99  ILE L CB  1 
ATOM   12931 C  CG1 . ILE L  1 99  ? 62.872  81.821  22.648  1.00 23.63 ? 99  ILE L CG1 1 
ATOM   12932 C  CG2 . ILE L  1 99  ? 65.153  81.187  23.504  1.00 25.58 ? 99  ILE L CG2 1 
ATOM   12933 C  CD1 . ILE L  1 99  ? 62.075  80.575  22.890  1.00 22.23 ? 99  ILE L CD1 1 
ATOM   12934 N  N   . GLU L  1 100 ? 67.181  83.173  22.209  1.00 28.19 ? 100 GLU L N   1 
ATOM   12935 C  CA  . GLU L  1 100 ? 68.603  82.889  22.235  1.00 29.23 ? 100 GLU L CA  1 
ATOM   12936 C  C   . GLU L  1 100 ? 68.945  82.252  23.586  1.00 29.19 ? 100 GLU L C   1 
ATOM   12937 O  O   . GLU L  1 100 ? 68.751  82.867  24.638  1.00 25.66 ? 100 GLU L O   1 
ATOM   12938 C  CB  . GLU L  1 100 ? 69.405  84.161  22.028  1.00 29.45 ? 100 GLU L CB  1 
ATOM   12939 C  CG  . GLU L  1 100 ? 70.858  83.904  21.712  1.00 35.35 ? 100 GLU L CG  1 
ATOM   12940 C  CD  . GLU L  1 100 ? 71.628  85.186  21.484  1.00 47.87 ? 100 GLU L CD  1 
ATOM   12941 O  OE1 . GLU L  1 100 ? 71.162  86.017  20.672  1.00 57.32 ? 100 GLU L OE1 1 
ATOM   12942 O  OE2 . GLU L  1 100 ? 72.691  85.369  22.123  1.00 50.03 ? 100 GLU L OE2 1 
ATOM   12943 N  N   . ASP L  1 101 ? 69.436  81.015  23.555  1.00 29.47 ? 101 ASP L N   1 
ATOM   12944 C  CA  . ASP L  1 101 ? 69.740  80.286  24.780  1.00 24.84 ? 101 ASP L CA  1 
ATOM   12945 C  C   . ASP L  1 101 ? 71.160  79.724  24.830  1.00 26.82 ? 101 ASP L C   1 
ATOM   12946 O  O   . ASP L  1 101 ? 71.651  79.170  23.852  1.00 27.64 ? 101 ASP L O   1 
ATOM   12947 C  CB  . ASP L  1 101 ? 68.740  79.156  25.007  1.00 23.13 ? 101 ASP L CB  1 
ATOM   12948 C  CG  . ASP L  1 101 ? 68.752  78.672  26.447  1.00 31.17 ? 101 ASP L CG  1 
ATOM   12949 O  OD1 . ASP L  1 101 ? 68.507  79.510  27.354  1.00 25.00 ? 101 ASP L OD1 1 
ATOM   12950 O  OD2 . ASP L  1 101 ? 69.057  77.478  26.673  1.00 27.91 ? 101 ASP L OD2 1 
ATOM   12951 N  N   . SER L  1 102 ? 71.801  79.872  25.984  1.00 26.66 ? 102 SER L N   1 
ATOM   12952 C  CA  . SER L  1 102 ? 73.151  79.386  26.203  1.00 28.93 ? 102 SER L CA  1 
ATOM   12953 C  C   . SER L  1 102 ? 73.237  78.079  27.005  1.00 28.91 ? 102 SER L C   1 
ATOM   12954 O  O   . SER L  1 102 ? 74.325  77.606  27.288  1.00 26.05 ? 102 SER L O   1 
ATOM   12955 C  CB  . SER L  1 102 ? 73.997  80.465  26.879  1.00 31.72 ? 102 SER L CB  1 
ATOM   12956 O  OG  . SER L  1 102 ? 74.568  81.336  25.913  1.00 39.51 ? 102 SER L OG  1 
ATOM   12957 N  N   . VAL L  1 103 ? 72.100  77.485  27.351  1.00 28.31 ? 103 VAL L N   1 
ATOM   12958 C  CA  . VAL L  1 103 ? 72.125  76.264  28.138  1.00 28.12 ? 103 VAL L CA  1 
ATOM   12959 C  C   . VAL L  1 103 ? 71.906  75.038  27.256  1.00 30.62 ? 103 VAL L C   1 
ATOM   12960 O  O   . VAL L  1 103 ? 72.539  73.994  27.449  1.00 26.82 ? 103 VAL L O   1 
ATOM   12961 C  CB  . VAL L  1 103 ? 71.109  76.325  29.307  1.00 25.92 ? 103 VAL L CB  1 
ATOM   12962 C  CG1 . VAL L  1 103 ? 70.865  74.947  29.903  1.00 20.69 ? 103 VAL L CG1 1 
ATOM   12963 C  CG2 . VAL L  1 103 ? 71.621  77.288  30.369  1.00 26.61 ? 103 VAL L CG2 1 
ATOM   12964 N  N   . ILE L  1 104 ? 71.006  75.159  26.290  1.00 27.57 ? 104 ILE L N   1 
ATOM   12965 C  CA  . ILE L  1 104 ? 70.875  74.109  25.287  1.00 27.93 ? 104 ILE L CA  1 
ATOM   12966 C  C   . ILE L  1 104 ? 72.067  74.166  24.347  1.00 26.04 ? 104 ILE L C   1 
ATOM   12967 O  O   . ILE L  1 104 ? 72.762  75.183  24.249  1.00 26.77 ? 104 ILE L O   1 
ATOM   12968 C  CB  . ILE L  1 104 ? 69.589  74.236  24.484  1.00 31.42 ? 104 ILE L CB  1 
ATOM   12969 C  CG1 . ILE L  1 104 ? 69.522  75.602  23.787  1.00 25.05 ? 104 ILE L CG1 1 
ATOM   12970 C  CG2 . ILE L  1 104 ? 68.398  74.038  25.395  1.00 27.37 ? 104 ILE L CG2 1 
ATOM   12971 C  CD1 . ILE L  1 104 ? 68.376  75.716  22.767  1.00 28.20 ? 104 ILE L CD1 1 
ATOM   12972 N  N   . SER L  1 105 ? 72.334  73.055  23.683  1.00 31.57 ? 105 SER L N   1 
ATOM   12973 C  CA  . SER L  1 105 ? 73.458  72.989  22.762  1.00 31.32 ? 105 SER L CA  1 
ATOM   12974 C  C   . SER L  1 105 ? 73.082  72.035  21.667  1.00 27.87 ? 105 SER L C   1 
ATOM   12975 O  O   . SER L  1 105 ? 72.118  71.272  21.813  1.00 27.86 ? 105 SER L O   1 
ATOM   12976 C  CB  . SER L  1 105 ? 74.721  72.496  23.468  1.00 32.28 ? 105 SER L CB  1 
ATOM   12977 O  OG  . SER L  1 105 ? 75.873  72.715  22.668  1.00 32.23 ? 105 SER L OG  1 
ATOM   12978 N  N   . LEU L  1 106 ? 73.824  72.085  20.565  1.00 29.49 ? 106 LEU L N   1 
ATOM   12979 C  CA  . LEU L  1 106 ? 73.610  71.133  19.477  1.00 33.32 ? 106 LEU L CA  1 
ATOM   12980 C  C   . LEU L  1 106 ? 74.729  70.076  19.430  1.00 37.11 ? 106 LEU L C   1 
ATOM   12981 O  O   . LEU L  1 106 ? 74.877  69.341  18.451  1.00 38.09 ? 106 LEU L O   1 
ATOM   12982 C  CB  . LEU L  1 106 ? 73.488  71.870  18.149  1.00 29.99 ? 106 LEU L CB  1 
ATOM   12983 C  CG  . LEU L  1 106 ? 72.315  72.846  18.081  1.00 31.45 ? 106 LEU L CG  1 
ATOM   12984 C  CD1 . LEU L  1 106 ? 72.344  73.638  16.766  1.00 30.74 ? 106 LEU L CD1 1 
ATOM   12985 C  CD2 . LEU L  1 106 ? 70.971  72.114  18.278  1.00 25.15 ? 106 LEU L CD2 1 
ATOM   12986 N  N   . SER L  1 107 ? 75.506  70.013  20.506  1.00 33.67 ? 107 SER L N   1 
ATOM   12987 C  CA  . SER L  1 107 ? 76.555  69.016  20.671  1.00 36.28 ? 107 SER L CA  1 
ATOM   12988 C  C   . SER L  1 107 ? 76.899  68.901  22.160  1.00 39.85 ? 107 SER L C   1 
ATOM   12989 O  O   . SER L  1 107 ? 76.741  69.867  22.919  1.00 33.08 ? 107 SER L O   1 
ATOM   12990 C  CB  . SER L  1 107 ? 77.798  69.420  19.880  1.00 33.14 ? 107 SER L CB  1 
ATOM   12991 O  OG  . SER L  1 107 ? 78.307  70.660  20.342  1.00 43.30 ? 107 SER L OG  1 
ATOM   12992 N  N   . GLY L  1 108 ? 77.360  67.726  22.582  1.00 35.57 ? 108 GLY L N   1 
ATOM   12993 C  CA  . GLY L  1 108 ? 77.689  67.516  23.982  1.00 40.81 ? 108 GLY L CA  1 
ATOM   12994 C  C   . GLY L  1 108 ? 76.576  66.885  24.800  1.00 36.39 ? 108 GLY L C   1 
ATOM   12995 O  O   . GLY L  1 108 ? 75.649  66.296  24.263  1.00 38.93 ? 108 GLY L O   1 
ATOM   12996 N  N   . ASP L  1 109 ? 76.659  66.983  26.118  1.00 44.31 ? 109 ASP L N   1 
ATOM   12997 C  CA  . ASP L  1 109 ? 75.646  66.332  26.948  1.00 40.78 ? 109 ASP L CA  1 
ATOM   12998 C  C   . ASP L  1 109 ? 74.419  67.216  27.139  1.00 38.56 ? 109 ASP L C   1 
ATOM   12999 O  O   . ASP L  1 109 ? 73.366  66.746  27.557  1.00 35.17 ? 109 ASP L O   1 
ATOM   13000 C  CB  . ASP L  1 109 ? 76.227  65.865  28.283  1.00 40.15 ? 109 ASP L CB  1 
ATOM   13001 C  CG  . ASP L  1 109 ? 77.206  66.851  28.864  1.00 43.33 ? 109 ASP L CG  1 
ATOM   13002 O  OD1 . ASP L  1 109 ? 76.941  68.064  28.744  1.00 45.72 ? 109 ASP L OD1 1 
ATOM   13003 O  OD2 . ASP L  1 109 ? 78.242  66.423  29.429  1.00 45.20 ? 109 ASP L OD2 1 
ATOM   13004 N  N   . HIS L  1 110 ? 74.550  68.495  26.803  1.00 38.37 ? 110 HIS L N   1 
ATOM   13005 C  CA  . HIS L  1 110 ? 73.381  69.364  26.764  1.00 38.63 ? 110 HIS L CA  1 
ATOM   13006 C  C   . HIS L  1 110 ? 72.742  69.287  25.383  1.00 38.00 ? 110 HIS L C   1 
ATOM   13007 O  O   . HIS L  1 110 ? 71.703  69.905  25.143  1.00 34.24 ? 110 HIS L O   1 
ATOM   13008 C  CB  . HIS L  1 110 ? 73.747  70.811  27.107  1.00 36.81 ? 110 HIS L CB  1 
ATOM   13009 C  CG  . HIS L  1 110 ? 74.368  70.974  28.460  1.00 42.40 ? 110 HIS L CG  1 
ATOM   13010 N  ND1 . HIS L  1 110 ? 75.327  71.928  28.729  1.00 47.34 ? 110 HIS L ND1 1 
ATOM   13011 C  CD2 . HIS L  1 110 ? 74.166  70.306  29.621  1.00 36.12 ? 110 HIS L CD2 1 
ATOM   13012 C  CE1 . HIS L  1 110 ? 75.693  71.838  29.996  1.00 46.73 ? 110 HIS L CE1 1 
ATOM   13013 N  NE2 . HIS L  1 110 ? 75.001  70.864  30.561  1.00 43.46 ? 110 HIS L NE2 1 
ATOM   13014 N  N   . CYS L  1 111 ? 73.368  68.524  24.485  1.00 36.04 ? 111 CYS L N   1 
ATOM   13015 C  CA  . CYS L  1 111 ? 72.890  68.409  23.103  1.00 35.74 ? 111 CYS L CA  1 
ATOM   13016 C  C   . CYS L  1 111 ? 71.425  68.031  23.026  1.00 31.77 ? 111 CYS L C   1 
ATOM   13017 O  O   . CYS L  1 111 ? 70.972  67.070  23.650  1.00 32.45 ? 111 CYS L O   1 
ATOM   13018 C  CB  . CYS L  1 111 ? 73.731  67.442  22.260  1.00 37.26 ? 111 CYS L CB  1 
ATOM   13019 S  SG  . CYS L  1 111 ? 73.085  67.196  20.582  1.00 32.29 ? 111 CYS L SG  1 
ATOM   13020 N  N   . ILE L  1 112 ? 70.694  68.814  22.246  1.00 29.01 ? 112 ILE L N   1 
ATOM   13021 C  CA  . ILE L  1 112 ? 69.246  68.729  22.210  1.00 33.33 ? 112 ILE L CA  1 
ATOM   13022 C  C   . ILE L  1 112 ? 68.739  67.910  21.020  1.00 37.09 ? 112 ILE L C   1 
ATOM   13023 O  O   . ILE L  1 112 ? 67.565  67.514  20.974  1.00 34.82 ? 112 ILE L O   1 
ATOM   13024 C  CB  . ILE L  1 112 ? 68.655  70.152  22.185  1.00 34.33 ? 112 ILE L CB  1 
ATOM   13025 C  CG1 . ILE L  1 112 ? 67.424  70.207  23.054  1.00 40.24 ? 112 ILE L CG1 1 
ATOM   13026 C  CG2 . ILE L  1 112 ? 68.421  70.674  20.772  1.00 33.84 ? 112 ILE L CG2 1 
ATOM   13027 C  CD1 . ILE L  1 112 ? 67.787  70.087  24.517  1.00 43.15 ? 112 ILE L CD1 1 
ATOM   13028 N  N   . ILE L  1 113 ? 69.642  67.670  20.066  1.00 34.71 ? 113 ILE L N   1 
ATOM   13029 C  CA  . ILE L  1 113 ? 69.333  66.931  18.847  1.00 34.53 ? 113 ILE L CA  1 
ATOM   13030 C  C   . ILE L  1 113 ? 68.894  65.511  19.161  1.00 33.46 ? 113 ILE L C   1 
ATOM   13031 O  O   . ILE L  1 113 ? 69.528  64.809  19.947  1.00 31.22 ? 113 ILE L O   1 
ATOM   13032 C  CB  . ILE L  1 113 ? 70.546  66.892  17.896  1.00 34.29 ? 113 ILE L CB  1 
ATOM   13033 C  CG1 . ILE L  1 113 ? 70.845  68.298  17.356  1.00 34.40 ? 113 ILE L CG1 1 
ATOM   13034 C  CG2 . ILE L  1 113 ? 70.295  65.914  16.760  1.00 36.92 ? 113 ILE L CG2 1 
ATOM   13035 C  CD1 . ILE L  1 113 ? 72.152  68.409  16.594  1.00 37.97 ? 113 ILE L CD1 1 
ATOM   13036 N  N   . GLY L  1 114 ? 67.797  65.094  18.545  1.00 33.94 ? 114 GLY L N   1 
ATOM   13037 C  CA  . GLY L  1 114 ? 67.266  63.770  18.767  1.00 32.72 ? 114 GLY L CA  1 
ATOM   13038 C  C   . GLY L  1 114 ? 66.243  63.803  19.870  1.00 32.84 ? 114 GLY L C   1 
ATOM   13039 O  O   . GLY L  1 114 ? 65.602  62.802  20.165  1.00 35.22 ? 114 GLY L O   1 
ATOM   13040 N  N   . ARG L  1 115 ? 66.068  64.967  20.483  1.00 37.88 ? 115 ARG L N   1 
ATOM   13041 C  CA  . ARG L  1 115 ? 65.065  65.100  21.532  1.00 34.78 ? 115 ARG L CA  1 
ATOM   13042 C  C   . ARG L  1 115 ? 63.804  65.791  21.017  1.00 33.30 ? 115 ARG L C   1 
ATOM   13043 O  O   . ARG L  1 115 ? 63.741  66.205  19.864  1.00 33.59 ? 115 ARG L O   1 
ATOM   13044 C  CB  . ARG L  1 115 ? 65.677  65.798  22.747  1.00 37.25 ? 115 ARG L CB  1 
ATOM   13045 C  CG  . ARG L  1 115 ? 67.080  65.267  23.044  1.00 36.26 ? 115 ARG L CG  1 
ATOM   13046 C  CD  . ARG L  1 115 ? 67.551  65.541  24.454  1.00 30.73 ? 115 ARG L CD  1 
ATOM   13047 N  NE  . ARG L  1 115 ? 68.803  64.839  24.741  1.00 33.34 ? 115 ARG L NE  1 
ATOM   13048 C  CZ  . ARG L  1 115 ? 68.881  63.645  25.331  1.00 33.91 ? 115 ARG L CZ  1 
ATOM   13049 N  NH1 . ARG L  1 115 ? 67.769  63.021  25.722  1.00 29.55 ? 115 ARG L NH1 1 
ATOM   13050 N  NH2 . ARG L  1 115 ? 70.073  63.088  25.550  1.00 29.29 ? 115 ARG L NH2 1 
ATOM   13051 N  N   . THR L  1 116 ? 62.795  65.901  21.870  1.00 34.21 ? 116 THR L N   1 
ATOM   13052 C  CA  . THR L  1 116 ? 61.489  66.403  21.463  1.00 33.59 ? 116 THR L CA  1 
ATOM   13053 C  C   . THR L  1 116 ? 61.194  67.818  21.965  1.00 37.67 ? 116 THR L C   1 
ATOM   13054 O  O   . THR L  1 116 ? 61.152  68.065  23.175  1.00 33.48 ? 116 THR L O   1 
ATOM   13055 C  CB  . THR L  1 116 ? 60.373  65.483  21.974  1.00 36.74 ? 116 THR L CB  1 
ATOM   13056 O  OG1 . THR L  1 116 ? 60.427  64.245  21.266  1.00 40.26 ? 116 THR L OG1 1 
ATOM   13057 C  CG2 . THR L  1 116 ? 59.004  66.121  21.762  1.00 32.58 ? 116 THR L CG2 1 
ATOM   13058 N  N   . LEU L  1 117 ? 60.974  68.736  21.029  1.00 34.13 ? 117 LEU L N   1 
ATOM   13059 C  CA  . LEU L  1 117 ? 60.523  70.077  21.355  1.00 30.75 ? 117 LEU L CA  1 
ATOM   13060 C  C   . LEU L  1 117 ? 59.010  70.056  21.478  1.00 30.07 ? 117 LEU L C   1 
ATOM   13061 O  O   . LEU L  1 117 ? 58.341  69.432  20.671  1.00 36.25 ? 117 LEU L O   1 
ATOM   13062 C  CB  . LEU L  1 117 ? 60.934  71.050  20.254  1.00 35.55 ? 117 LEU L CB  1 
ATOM   13063 C  CG  . LEU L  1 117 ? 60.357  72.454  20.401  1.00 34.32 ? 117 LEU L CG  1 
ATOM   13064 C  CD1 . LEU L  1 117 ? 60.994  73.154  21.592  1.00 23.81 ? 117 LEU L CD1 1 
ATOM   13065 C  CD2 . LEU L  1 117 ? 60.538  73.258  19.120  1.00 28.37 ? 117 LEU L CD2 1 
ATOM   13066 N  N   . VAL L  1 118 ? 58.471  70.740  22.482  1.00 29.43 ? 118 VAL L N   1 
ATOM   13067 C  CA  . VAL L  1 118 ? 57.042  70.673  22.793  1.00 31.78 ? 118 VAL L CA  1 
ATOM   13068 C  C   . VAL L  1 118 ? 56.473  72.060  23.087  1.00 34.34 ? 118 VAL L C   1 
ATOM   13069 O  O   . VAL L  1 118 ? 57.088  72.836  23.824  1.00 33.89 ? 118 VAL L O   1 
ATOM   13070 C  CB  . VAL L  1 118 ? 56.781  69.774  24.023  1.00 28.55 ? 118 VAL L CB  1 
ATOM   13071 C  CG1 . VAL L  1 118 ? 55.334  69.898  24.494  1.00 26.10 ? 118 VAL L CG1 1 
ATOM   13072 C  CG2 . VAL L  1 118 ? 57.128  68.340  23.712  1.00 32.34 ? 118 VAL L CG2 1 
ATOM   13073 N  N   . VAL L  1 119 ? 55.314  72.386  22.509  1.00 32.87 ? 119 VAL L N   1 
ATOM   13074 C  CA  . VAL L  1 119 ? 54.617  73.620  22.892  1.00 30.44 ? 119 VAL L CA  1 
ATOM   13075 C  C   . VAL L  1 119 ? 53.310  73.336  23.652  1.00 30.55 ? 119 VAL L C   1 
ATOM   13076 O  O   . VAL L  1 119 ? 52.527  72.461  23.280  1.00 27.60 ? 119 VAL L O   1 
ATOM   13077 C  CB  . VAL L  1 119 ? 54.430  74.610  21.707  1.00 33.65 ? 119 VAL L CB  1 
ATOM   13078 C  CG1 . VAL L  1 119 ? 53.507  74.036  20.630  1.00 32.59 ? 119 VAL L CG1 1 
ATOM   13079 C  CG2 . VAL L  1 119 ? 53.917  75.965  22.215  1.00 30.20 ? 119 VAL L CG2 1 
ATOM   13080 N  N   . HIS L  1 120 ? 53.106  74.080  24.737  1.00 33.80 ? 120 HIS L N   1 
ATOM   13081 C  CA  . HIS L  1 120 ? 52.092  73.751  25.742  1.00 29.46 ? 120 HIS L CA  1 
ATOM   13082 C  C   . HIS L  1 120 ? 50.804  74.551  25.697  1.00 31.16 ? 120 HIS L C   1 
ATOM   13083 O  O   . HIS L  1 120 ? 50.710  75.604  25.068  1.00 34.06 ? 120 HIS L O   1 
ATOM   13084 C  CB  . HIS L  1 120 ? 52.676  73.907  27.141  1.00 30.01 ? 120 HIS L CB  1 
ATOM   13085 C  CG  . HIS L  1 120 ? 53.301  72.659  27.673  1.00 29.19 ? 120 HIS L CG  1 
ATOM   13086 N  ND1 . HIS L  1 120 ? 52.657  71.830  28.566  1.00 32.50 ? 120 HIS L ND1 1 
ATOM   13087 C  CD2 . HIS L  1 120 ? 54.505  72.092  27.433  1.00 26.14 ? 120 HIS L CD2 1 
ATOM   13088 C  CE1 . HIS L  1 120 ? 53.443  70.810  28.858  1.00 32.80 ? 120 HIS L CE1 1 
ATOM   13089 N  NE2 . HIS L  1 120 ? 54.568  70.943  28.181  1.00 28.80 ? 120 HIS L NE2 1 
ATOM   13090 N  N   . GLU L  1 121 ? 49.821  74.038  26.420  1.00 28.14 ? 121 GLU L N   1 
ATOM   13091 C  CA  . GLU L  1 121 ? 48.532  74.678  26.559  1.00 32.25 ? 121 GLU L CA  1 
ATOM   13092 C  C   . GLU L  1 121 ? 48.626  76.099  27.081  1.00 37.30 ? 121 GLU L C   1 
ATOM   13093 O  O   . GLU L  1 121 ? 48.233  77.043  26.386  1.00 32.01 ? 121 GLU L O   1 
ATOM   13094 C  CB  . GLU L  1 121 ? 47.677  73.875  27.527  1.00 30.75 ? 121 GLU L CB  1 
ATOM   13095 C  CG  . GLU L  1 121 ? 46.270  74.375  27.632  1.00 35.01 ? 121 GLU L CG  1 
ATOM   13096 C  CD  . GLU L  1 121 ? 45.494  73.602  28.670  1.00 34.72 ? 121 GLU L CD  1 
ATOM   13097 O  OE1 . GLU L  1 121 ? 44.345  73.993  28.971  1.00 37.44 ? 121 GLU L OE1 1 
ATOM   13098 O  OE2 . GLU L  1 121 ? 46.049  72.609  29.189  1.00 33.55 ? 121 GLU L OE2 1 
ATOM   13099 N  N   . LYS L  1 122 ? 49.146  76.229  28.309  1.00 33.72 ? 122 LYS L N   1 
ATOM   13100 C  CA  . LYS L  1 122 ? 49.181  77.489  29.045  1.00 30.70 ? 122 LYS L CA  1 
ATOM   13101 C  C   . LYS L  1 122 ? 50.595  77.995  29.321  1.00 26.23 ? 122 LYS L C   1 
ATOM   13102 O  O   . LYS L  1 122 ? 51.585  77.446  28.832  1.00 26.42 ? 122 LYS L O   1 
ATOM   13103 C  CB  . LYS L  1 122 ? 48.468  77.321  30.389  1.00 28.13 ? 122 LYS L CB  1 
ATOM   13104 C  CG  . LYS L  1 122 ? 47.353  76.302  30.348  1.00 35.36 ? 122 LYS L CG  1 
ATOM   13105 C  CD  . LYS L  1 122 ? 46.601  76.230  31.658  1.00 31.58 ? 122 LYS L CD  1 
ATOM   13106 C  CE  . LYS L  1 122 ? 47.459  75.679  32.765  1.00 34.14 ? 122 LYS L CE  1 
ATOM   13107 N  NZ  . LYS L  1 122 ? 46.649  75.382  33.980  1.00 37.08 ? 122 LYS L NZ  1 
ATOM   13108 N  N   . ALA L  1 123 ? 50.668  79.046  30.132  1.00 21.99 ? 123 ALA L N   1 
ATOM   13109 C  CA  . ALA L  1 123 ? 51.945  79.596  30.582  1.00 23.02 ? 123 ALA L CA  1 
ATOM   13110 C  C   . ALA L  1 123 ? 52.707  78.637  31.488  1.00 19.63 ? 123 ALA L C   1 
ATOM   13111 O  O   . ALA L  1 123 ? 52.135  78.002  32.380  1.00 15.36 ? 123 ALA L O   1 
ATOM   13112 C  CB  . ALA L  1 123 ? 51.729  80.915  31.311  1.00 15.67 ? 123 ALA L CB  1 
ATOM   13113 N  N   . ASP L  1 124 ? 54.002  78.538  31.220  1.00 18.60 ? 124 ASP L N   1 
ATOM   13114 C  CA  . ASP L  1 124 ? 54.965  77.979  32.150  1.00 20.95 ? 124 ASP L CA  1 
ATOM   13115 C  C   . ASP L  1 124 ? 55.122  79.020  33.274  1.00 18.25 ? 124 ASP L C   1 
ATOM   13116 O  O   . ASP L  1 124 ? 55.458  80.173  33.002  1.00 17.81 ? 124 ASP L O   1 
ATOM   13117 C  CB  . ASP L  1 124 ? 56.284  77.769  31.390  1.00 19.89 ? 124 ASP L CB  1 
ATOM   13118 C  CG  . ASP L  1 124 ? 57.364  77.103  32.227  1.00 22.95 ? 124 ASP L CG  1 
ATOM   13119 O  OD1 . ASP L  1 124 ? 57.286  77.178  33.468  1.00 18.97 ? 124 ASP L OD1 1 
ATOM   13120 O  OD2 . ASP L  1 124 ? 58.315  76.530  31.634  1.00 18.64 ? 124 ASP L OD2 1 
ATOM   13121 N  N   . ASP L  1 125 ? 54.880  78.634  34.527  1.00 16.42 ? 125 ASP L N   1 
ATOM   13122 C  CA  . ASP L  1 125 ? 55.031  79.600  35.628  1.00 18.31 ? 125 ASP L CA  1 
ATOM   13123 C  C   . ASP L  1 125 ? 56.484  79.900  35.998  1.00 18.98 ? 125 ASP L C   1 
ATOM   13124 O  O   . ASP L  1 125 ? 56.751  80.738  36.864  1.00 15.93 ? 125 ASP L O   1 
ATOM   13125 C  CB  . ASP L  1 125 ? 54.173  79.265  36.877  1.00 20.72 ? 125 ASP L CB  1 
ATOM   13126 C  CG  . ASP L  1 125 ? 54.630  78.004  37.630  1.00 21.28 ? 125 ASP L CG  1 
ATOM   13127 O  OD1 . ASP L  1 125 ? 55.782  77.555  37.492  1.00 19.67 ? 125 ASP L OD1 1 
ATOM   13128 O  OD2 . ASP L  1 125 ? 53.807  77.464  38.393  1.00 21.65 ? 125 ASP L OD2 1 
ATOM   13129 N  N   . LEU L  1 126 ? 57.403  79.211  35.327  1.00 17.48 ? 126 LEU L N   1 
ATOM   13130 C  CA  . LEU L  1 126 ? 58.833  79.453  35.462  1.00 17.73 ? 126 LEU L CA  1 
ATOM   13131 C  C   . LEU L  1 126 ? 59.300  79.159  36.885  1.00 17.75 ? 126 LEU L C   1 
ATOM   13132 O  O   . LEU L  1 126 ? 60.305  79.711  37.344  1.00 16.23 ? 126 LEU L O   1 
ATOM   13133 C  CB  . LEU L  1 126 ? 59.190  80.891  35.035  1.00 14.00 ? 126 LEU L CB  1 
ATOM   13134 C  CG  . LEU L  1 126 ? 58.589  81.375  33.703  1.00 18.81 ? 126 LEU L CG  1 
ATOM   13135 C  CD1 . LEU L  1 126 ? 59.100  82.772  33.338  1.00 17.54 ? 126 LEU L CD1 1 
ATOM   13136 C  CD2 . LEU L  1 126 ? 58.890  80.410  32.587  1.00 15.73 ? 126 LEU L CD2 1 
ATOM   13137 N  N   . GLY L  1 127 ? 58.545  78.311  37.581  1.00 16.65 ? 127 GLY L N   1 
ATOM   13138 C  CA  . GLY L  1 127 ? 58.923  77.855  38.907  1.00 18.98 ? 127 GLY L CA  1 
ATOM   13139 C  C   . GLY L  1 127 ? 58.524  78.759  40.066  1.00 16.04 ? 127 GLY L C   1 
ATOM   13140 O  O   . GLY L  1 127 ? 58.924  78.527  41.189  1.00 16.44 ? 127 GLY L O   1 
ATOM   13141 N  N   . LYS L  1 128 ? 57.721  79.778  39.810  1.00 15.13 ? 128 LYS L N   1 
ATOM   13142 C  CA  . LYS L  1 128 ? 57.369  80.720  40.862  1.00 14.01 ? 128 LYS L CA  1 
ATOM   13143 C  C   . LYS L  1 128 ? 55.938  80.543  41.348  1.00 17.40 ? 128 LYS L C   1 
ATOM   13144 O  O   . LYS L  1 128 ? 55.346  81.471  41.914  1.00 15.09 ? 128 LYS L O   1 
ATOM   13145 C  CB  . LYS L  1 128 ? 57.590  82.149  40.377  1.00 18.10 ? 128 LYS L CB  1 
ATOM   13146 C  CG  . LYS L  1 128 ? 59.015  82.432  39.919  1.00 16.88 ? 128 LYS L CG  1 
ATOM   13147 C  CD  . LYS L  1 128 ? 59.070  83.751  39.162  1.00 23.11 ? 128 LYS L CD  1 
ATOM   13148 C  CE  . LYS L  1 128 ? 59.821  84.820  39.934  1.00 25.88 ? 128 LYS L CE  1 
ATOM   13149 N  NZ  . LYS L  1 128 ? 59.696  86.151  39.281  1.00 31.42 ? 128 LYS L NZ  1 
ATOM   13150 N  N   . GLY L  1 129 ? 55.386  79.349  41.140  1.00 15.84 ? 129 GLY L N   1 
ATOM   13151 C  CA  . GLY L  1 129 ? 54.004  79.072  41.516  1.00 17.93 ? 129 GLY L CA  1 
ATOM   13152 C  C   . GLY L  1 129 ? 53.785  78.782  42.995  1.00 19.81 ? 129 GLY L C   1 
ATOM   13153 O  O   . GLY L  1 129 ? 52.688  78.954  43.509  1.00 21.18 ? 129 GLY L O   1 
ATOM   13154 N  N   . GLY L  1 130 ? 54.828  78.346  43.692  1.00 20.72 ? 130 GLY L N   1 
ATOM   13155 C  CA  . GLY L  1 130 ? 54.717  78.147  45.126  1.00 19.13 ? 130 GLY L CA  1 
ATOM   13156 C  C   . GLY L  1 130 ? 54.100  76.805  45.481  1.00 21.68 ? 130 GLY L C   1 
ATOM   13157 O  O   . GLY L  1 130 ? 53.573  76.615  46.576  1.00 15.17 ? 130 GLY L O   1 
ATOM   13158 N  N   . ASN L  1 131 ? 54.138  75.883  44.527  1.00 19.26 ? 131 ASN L N   1 
ATOM   13159 C  CA  . ASN L  1 131 ? 53.731  74.517  44.785  1.00 23.37 ? 131 ASN L CA  1 
ATOM   13160 C  C   . ASN L  1 131 ? 54.783  73.597  44.222  1.00 22.98 ? 131 ASN L C   1 
ATOM   13161 O  O   . ASN L  1 131 ? 55.725  74.054  43.568  1.00 23.45 ? 131 ASN L O   1 
ATOM   13162 C  CB  . ASN L  1 131 ? 52.345  74.214  44.209  1.00 24.56 ? 131 ASN L CB  1 
ATOM   13163 C  CG  . ASN L  1 131 ? 52.257  74.470  42.721  1.00 21.58 ? 131 ASN L CG  1 
ATOM   13164 O  OD1 . ASN L  1 131 ? 53.160  74.128  41.954  1.00 22.75 ? 131 ASN L OD1 1 
ATOM   13165 N  ND2 . ASN L  1 131 ? 51.163  75.074  42.303  1.00 19.47 ? 131 ASN L ND2 1 
ATOM   13166 N  N   . GLU L  1 132 ? 54.643  72.305  44.485  1.00 25.35 ? 132 GLU L N   1 
ATOM   13167 C  CA  . GLU L  1 132 ? 55.681  71.359  44.102  1.00 29.87 ? 132 GLU L CA  1 
ATOM   13168 C  C   . GLU L  1 132 ? 55.697  71.139  42.594  1.00 25.60 ? 132 GLU L C   1 
ATOM   13169 O  O   . GLU L  1 132 ? 56.742  70.865  42.015  1.00 32.43 ? 132 GLU L O   1 
ATOM   13170 C  CB  . GLU L  1 132 ? 55.500  70.030  44.835  1.00 32.09 ? 132 GLU L CB  1 
ATOM   13171 C  CG  . GLU L  1 132 ? 56.784  69.233  44.950  1.00 41.11 ? 132 GLU L CG  1 
ATOM   13172 C  CD  . GLU L  1 132 ? 56.533  67.774  45.291  1.00 54.27 ? 132 GLU L CD  1 
ATOM   13173 O  OE1 . GLU L  1 132 ? 55.395  67.447  45.697  1.00 57.04 ? 132 GLU L OE1 1 
ATOM   13174 O  OE2 . GLU L  1 132 ? 57.472  66.957  45.144  1.00 57.29 ? 132 GLU L OE2 1 
ATOM   13175 N  N   . GLU L  1 133 ? 54.538  71.261  41.961  1.00 23.80 ? 133 GLU L N   1 
ATOM   13176 C  CA  . GLU L  1 133 ? 54.449  71.060  40.527  1.00 28.65 ? 133 GLU L CA  1 
ATOM   13177 C  C   . GLU L  1 133 ? 55.159  72.194  39.769  1.00 27.07 ? 133 GLU L C   1 
ATOM   13178 O  O   . GLU L  1 133 ? 55.688  71.993  38.682  1.00 26.14 ? 133 GLU L O   1 
ATOM   13179 C  CB  . GLU L  1 133 ? 52.983  70.926  40.112  1.00 32.64 ? 133 GLU L CB  1 
ATOM   13180 C  CG  . GLU L  1 133 ? 52.767  70.223  38.776  1.00 37.39 ? 133 GLU L CG  1 
ATOM   13181 C  CD  . GLU L  1 133 ? 53.398  68.838  38.724  1.00 38.83 ? 133 GLU L CD  1 
ATOM   13182 O  OE1 . GLU L  1 133 ? 53.373  68.102  39.736  1.00 44.21 ? 133 GLU L OE1 1 
ATOM   13183 O  OE2 . GLU L  1 133 ? 53.938  68.489  37.664  1.00 36.75 ? 133 GLU L OE2 1 
ATOM   13184 N  N   . SER L  1 134 ? 55.185  73.378  40.372  1.00 27.02 ? 134 SER L N   1 
ATOM   13185 C  CA  . SER L  1 134 ? 55.887  74.536  39.817  1.00 20.47 ? 134 SER L CA  1 
ATOM   13186 C  C   . SER L  1 134 ? 57.358  74.245  39.657  1.00 23.39 ? 134 SER L C   1 
ATOM   13187 O  O   . SER L  1 134 ? 57.939  74.563  38.626  1.00 22.22 ? 134 SER L O   1 
ATOM   13188 C  CB  . SER L  1 134 ? 55.709  75.755  40.729  1.00 17.79 ? 134 SER L CB  1 
ATOM   13189 O  OG  . SER L  1 134 ? 56.167  76.952  40.141  1.00 16.37 ? 134 SER L OG  1 
ATOM   13190 N  N   . THR L  1 135 ? 57.954  73.634  40.678  1.00 19.71 ? 135 THR L N   1 
ATOM   13191 C  CA  . THR L  1 135 ? 59.372  73.327  40.670  1.00 22.14 ? 135 THR L CA  1 
ATOM   13192 C  C   . THR L  1 135 ? 59.654  72.098  39.826  1.00 22.10 ? 135 THR L C   1 
ATOM   13193 O  O   . THR L  1 135 ? 60.798  71.695  39.697  1.00 23.30 ? 135 THR L O   1 
ATOM   13194 C  CB  . THR L  1 135 ? 59.910  73.041  42.088  1.00 26.04 ? 135 THR L CB  1 
ATOM   13195 O  OG1 . THR L  1 135 ? 59.440  71.757  42.521  1.00 33.48 ? 135 THR L OG1 1 
ATOM   13196 C  CG2 . THR L  1 135 ? 59.454  74.108  43.073  1.00 26.50 ? 135 THR L CG2 1 
ATOM   13197 N  N   . LYS L  1 136 ? 58.615  71.513  39.243  1.00 25.60 ? 136 LYS L N   1 
ATOM   13198 C  CA  . LYS L  1 136 ? 58.776  70.284  38.462  1.00 29.45 ? 136 LYS L CA  1 
ATOM   13199 C  C   . LYS L  1 136 ? 58.425  70.453  36.976  1.00 26.35 ? 136 LYS L C   1 
ATOM   13200 O  O   . LYS L  1 136 ? 59.202  70.064  36.109  1.00 27.71 ? 136 LYS L O   1 
ATOM   13201 C  CB  . LYS L  1 136 ? 57.970  69.142  39.101  1.00 32.65 ? 136 LYS L CB  1 
ATOM   13202 C  CG  . LYS L  1 136 ? 58.304  67.751  38.587  1.00 37.17 ? 136 LYS L CG  1 
ATOM   13203 C  CD  . LYS L  1 136 ? 57.709  66.674  39.508  1.00 43.48 ? 136 LYS L CD  1 
ATOM   13204 C  CE  . LYS L  1 136 ? 58.033  65.267  39.015  1.00 41.75 ? 136 LYS L CE  1 
ATOM   13205 N  NZ  . LYS L  1 136 ? 57.387  64.968  37.704  1.00 46.42 ? 136 LYS L NZ  1 
ATOM   13206 N  N   . THR L  1 137 ? 57.272  71.044  36.674  1.00 28.52 ? 137 THR L N   1 
ATOM   13207 C  CA  . THR L  1 137 ? 56.853  71.199  35.268  1.00 29.64 ? 137 THR L CA  1 
ATOM   13208 C  C   . THR L  1 137 ? 56.621  72.637  34.862  1.00 26.45 ? 137 THR L C   1 
ATOM   13209 O  O   . THR L  1 137 ? 56.864  73.007  33.717  1.00 28.11 ? 137 THR L O   1 
ATOM   13210 C  CB  . THR L  1 137 ? 55.537  70.489  34.981  1.00 27.08 ? 137 THR L CB  1 
ATOM   13211 O  OG1 . THR L  1 137 ? 54.548  70.961  35.902  1.00 29.13 ? 137 THR L OG1 1 
ATOM   13212 C  CG2 . THR L  1 137 ? 55.699  68.984  35.114  1.00 29.40 ? 137 THR L CG2 1 
ATOM   13213 N  N   . GLY L  1 138 ? 56.128  73.438  35.797  1.00 23.65 ? 138 GLY L N   1 
ATOM   13214 C  CA  . GLY L  1 138 ? 55.801  74.819  35.520  1.00 24.00 ? 138 GLY L CA  1 
ATOM   13215 C  C   . GLY L  1 138 ? 54.305  75.014  35.372  1.00 24.68 ? 138 GLY L C   1 
ATOM   13216 O  O   . GLY L  1 138 ? 53.843  76.121  35.070  1.00 25.24 ? 138 GLY L O   1 
ATOM   13217 N  N   . ASN L  1 139 ? 53.549  73.939  35.588  1.00 25.07 ? 139 ASN L N   1 
ATOM   13218 C  CA  . ASN L  1 139 ? 52.086  73.970  35.479  1.00 25.31 ? 139 ASN L CA  1 
ATOM   13219 C  C   . ASN L  1 139 ? 51.601  74.539  34.149  1.00 23.14 ? 139 ASN L C   1 
ATOM   13220 O  O   . ASN L  1 139 ? 50.690  75.365  34.115  1.00 24.78 ? 139 ASN L O   1 
ATOM   13221 C  CB  . ASN L  1 139 ? 51.464  74.731  36.668  1.00 24.70 ? 139 ASN L CB  1 
ATOM   13222 C  CG  . ASN L  1 139 ? 51.927  74.184  38.009  1.00 27.49 ? 139 ASN L CG  1 
ATOM   13223 O  OD1 . ASN L  1 139 ? 51.576  73.070  38.381  1.00 30.12 ? 139 ASN L OD1 1 
ATOM   13224 N  ND2 . ASN L  1 139 ? 52.735  74.962  38.733  1.00 26.61 ? 139 ASN L ND2 1 
ATOM   13225 N  N   . ALA L  1 140 ? 52.226  74.095  33.060  1.00 24.91 ? 140 ALA L N   1 
ATOM   13226 C  CA  . ALA L  1 140 ? 51.968  74.645  31.737  1.00 23.60 ? 140 ALA L CA  1 
ATOM   13227 C  C   . ALA L  1 140 ? 50.896  73.880  30.969  1.00 30.38 ? 140 ALA L C   1 
ATOM   13228 O  O   . ALA L  1 140 ? 50.648  74.157  29.783  1.00 31.95 ? 140 ALA L O   1 
ATOM   13229 C  CB  . ALA L  1 140 ? 53.268  74.735  30.923  1.00 26.79 ? 140 ALA L CB  1 
ATOM   13230 N  N   . GLY L  1 141 ? 50.254  72.926  31.636  1.00 27.83 ? 141 GLY L N   1 
ATOM   13231 C  CA  . GLY L  1 141 ? 49.149  72.208  31.021  1.00 31.91 ? 141 GLY L CA  1 
ATOM   13232 C  C   . GLY L  1 141 ? 49.550  71.230  29.924  1.00 32.63 ? 141 GLY L C   1 
ATOM   13233 O  O   . GLY L  1 141 ? 50.702  70.783  29.863  1.00 32.45 ? 141 GLY L O   1 
ATOM   13234 N  N   . SER L  1 142 ? 48.589  70.918  29.054  1.00 29.37 ? 142 SER L N   1 
ATOM   13235 C  CA  . SER L  1 142 ? 48.701  69.870  28.032  1.00 31.10 ? 142 SER L CA  1 
ATOM   13236 C  C   . SER L  1 142 ? 49.781  70.112  27.000  1.00 31.27 ? 142 SER L C   1 
ATOM   13237 O  O   . SER L  1 142 ? 50.183  71.254  26.763  1.00 34.30 ? 142 SER L O   1 
ATOM   13238 C  CB  . SER L  1 142 ? 47.369  69.715  27.276  1.00 36.82 ? 142 SER L CB  1 
ATOM   13239 O  OG  . SER L  1 142 ? 46.292  69.414  28.152  1.00 41.09 ? 142 SER L OG  1 
ATOM   13240 N  N   . ARG L  1 143 ? 50.223  69.026  26.370  1.00 32.38 ? 143 ARG L N   1 
ATOM   13241 C  CA  . ARG L  1 143 ? 51.194  69.093  25.276  1.00 37.80 ? 143 ARG L CA  1 
ATOM   13242 C  C   . ARG L  1 143 ? 50.457  69.203  23.939  1.00 38.33 ? 143 ARG L C   1 
ATOM   13243 O  O   . ARG L  1 143 ? 49.856  68.241  23.462  1.00 38.38 ? 143 ARG L O   1 
ATOM   13244 C  CB  . ARG L  1 143 ? 52.145  67.881  25.300  1.00 35.47 ? 143 ARG L CB  1 
ATOM   13245 C  CG  . ARG L  1 143 ? 52.924  67.737  26.625  1.00 36.45 ? 143 ARG L CG  1 
ATOM   13246 C  CD  . ARG L  1 143 ? 53.637  66.388  26.770  1.00 39.91 ? 143 ARG L CD  1 
ATOM   13247 N  NE  . ARG L  1 143 ? 54.066  66.142  28.151  1.00 40.76 ? 143 ARG L NE  1 
ATOM   13248 C  CZ  . ARG L  1 143 ? 54.978  65.238  28.522  1.00 43.63 ? 143 ARG L CZ  1 
ATOM   13249 N  NH1 . ARG L  1 143 ? 55.585  64.473  27.618  1.00 37.83 ? 143 ARG L NH1 1 
ATOM   13250 N  NH2 . ARG L  1 143 ? 55.291  65.103  29.810  1.00 42.93 ? 143 ARG L NH2 1 
ATOM   13251 N  N   . LEU L  1 144 ? 50.503  70.386  23.336  1.00 39.72 ? 144 LEU L N   1 
ATOM   13252 C  CA  . LEU L  1 144 ? 49.716  70.639  22.129  1.00 36.67 ? 144 LEU L CA  1 
ATOM   13253 C  C   . LEU L  1 144 ? 50.397  70.176  20.841  1.00 36.41 ? 144 LEU L C   1 
ATOM   13254 O  O   . LEU L  1 144 ? 49.743  69.629  19.959  1.00 34.79 ? 144 LEU L O   1 
ATOM   13255 C  CB  . LEU L  1 144 ? 49.330  72.119  22.029  1.00 31.64 ? 144 LEU L CB  1 
ATOM   13256 C  CG  . LEU L  1 144 ? 48.474  72.688  23.163  1.00 34.76 ? 144 LEU L CG  1 
ATOM   13257 C  CD1 . LEU L  1 144 ? 47.773  73.966  22.707  1.00 39.52 ? 144 LEU L CD1 1 
ATOM   13258 C  CD2 . LEU L  1 144 ? 47.470  71.666  23.655  1.00 28.47 ? 144 LEU L CD2 1 
ATOM   13259 N  N   . ALA L  1 145 ? 51.699  70.411  20.719  1.00 29.33 ? 145 ALA L N   1 
ATOM   13260 C  CA  . ALA L  1 145 ? 52.412  69.981  19.517  1.00 35.44 ? 145 ALA L CA  1 
ATOM   13261 C  C   . ALA L  1 145 ? 53.848  69.638  19.832  1.00 33.12 ? 145 ALA L C   1 
ATOM   13262 O  O   . ALA L  1 145 ? 54.430  70.176  20.764  1.00 34.23 ? 145 ALA L O   1 
ATOM   13263 C  CB  . ALA L  1 145 ? 52.347  71.048  18.413  1.00 31.64 ? 145 ALA L CB  1 
ATOM   13264 N  N   . CYS L  1 146 ? 54.417  68.741  19.042  1.00 32.02 ? 146 CYS L N   1 
ATOM   13265 C  CA  . CYS L  1 146 ? 55.765  68.283  19.293  1.00 33.87 ? 146 CYS L CA  1 
ATOM   13266 C  C   . CYS L  1 146 ? 56.501  67.942  18.006  1.00 33.61 ? 146 CYS L C   1 
ATOM   13267 O  O   . CYS L  1 146 ? 55.933  67.980  16.911  1.00 39.53 ? 146 CYS L O   1 
ATOM   13268 C  CB  . CYS L  1 146 ? 55.761  67.087  20.249  1.00 39.90 ? 146 CYS L CB  1 
ATOM   13269 S  SG  . CYS L  1 146 ? 54.916  65.646  19.607  1.00 46.89 ? 146 CYS L SG  1 
ATOM   13270 N  N   . GLY L  1 147 ? 57.778  67.623  18.148  1.00 28.93 ? 147 GLY L N   1 
ATOM   13271 C  CA  . GLY L  1 147 ? 58.592  67.263  17.015  1.00 29.80 ? 147 GLY L CA  1 
ATOM   13272 C  C   . GLY L  1 147 ? 59.958  66.821  17.481  1.00 36.10 ? 147 GLY L C   1 
ATOM   13273 O  O   . GLY L  1 147 ? 60.519  67.373  18.436  1.00 34.11 ? 147 GLY L O   1 
ATOM   13274 N  N   . VAL L  1 148 ? 60.497  65.808  16.823  1.00 29.72 ? 148 VAL L N   1 
ATOM   13275 C  CA  . VAL L  1 148 ? 61.853  65.399  17.112  1.00 33.79 ? 148 VAL L CA  1 
ATOM   13276 C  C   . VAL L  1 148 ? 62.828  66.364  16.438  1.00 30.54 ? 148 VAL L C   1 
ATOM   13277 O  O   . VAL L  1 148 ? 62.660  66.707  15.275  1.00 35.32 ? 148 VAL L O   1 
ATOM   13278 C  CB  . VAL L  1 148 ? 62.099  63.981  16.630  1.00 36.57 ? 148 VAL L CB  1 
ATOM   13279 C  CG1 . VAL L  1 148 ? 63.587  63.649  16.742  1.00 32.98 ? 148 VAL L CG1 1 
ATOM   13280 C  CG2 . VAL L  1 148 ? 61.211  63.006  17.421  1.00 33.66 ? 148 VAL L CG2 1 
ATOM   13281 N  N   . ILE L  1 149 ? 63.830  66.814  17.184  1.00 31.59 ? 149 ILE L N   1 
ATOM   13282 C  CA  . ILE L  1 149 ? 64.798  67.800  16.706  1.00 29.52 ? 149 ILE L CA  1 
ATOM   13283 C  C   . ILE L  1 149 ? 65.894  67.139  15.874  1.00 35.47 ? 149 ILE L C   1 
ATOM   13284 O  O   . ILE L  1 149 ? 66.669  66.340  16.403  1.00 38.93 ? 149 ILE L O   1 
ATOM   13285 C  CB  . ILE L  1 149 ? 65.448  68.531  17.900  1.00 31.90 ? 149 ILE L CB  1 
ATOM   13286 C  CG1 . ILE L  1 149 ? 64.381  69.268  18.720  1.00 35.17 ? 149 ILE L CG1 1 
ATOM   13287 C  CG2 . ILE L  1 149 ? 66.528  69.483  17.434  1.00 31.33 ? 149 ILE L CG2 1 
ATOM   13288 C  CD1 . ILE L  1 149 ? 64.937  70.048  19.913  1.00 33.12 ? 149 ILE L CD1 1 
ATOM   13289 N  N   . GLY L  1 150 ? 65.960  67.468  14.580  1.00 34.76 ? 150 GLY L N   1 
ATOM   13290 C  CA  . GLY L  1 150 ? 66.888  66.816  13.663  1.00 30.28 ? 150 GLY L CA  1 
ATOM   13291 C  C   . GLY L  1 150 ? 68.039  67.698  13.209  1.00 34.29 ? 150 GLY L C   1 
ATOM   13292 O  O   . GLY L  1 150 ? 67.978  68.935  13.309  1.00 31.03 ? 150 GLY L O   1 
ATOM   13293 N  N   . ILE L  1 151 ? 69.104  67.074  12.712  1.00 34.68 ? 151 ILE L N   1 
ATOM   13294 C  CA  . ILE L  1 151 ? 70.208  67.856  12.166  1.00 36.38 ? 151 ILE L CA  1 
ATOM   13295 C  C   . ILE L  1 151 ? 69.789  68.478  10.832  1.00 34.91 ? 151 ILE L C   1 
ATOM   13296 O  O   . ILE L  1 151 ? 68.990  67.907  10.090  1.00 35.85 ? 151 ILE L O   1 
ATOM   13297 C  CB  . ILE L  1 151 ? 71.529  67.044  12.042  1.00 36.58 ? 151 ILE L CB  1 
ATOM   13298 C  CG1 . ILE L  1 151 ? 71.888  66.410  13.387  1.00 35.40 ? 151 ILE L CG1 1 
ATOM   13299 C  CG2 . ILE L  1 151 ? 72.691  67.939  11.595  1.00 32.19 ? 151 ILE L CG2 1 
ATOM   13300 C  CD1 . ILE L  1 151 ? 73.277  65.800  13.434  1.00 35.39 ? 151 ILE L CD1 1 
ATOM   13301 N  N   . ALA L  1 152 ? 70.310  69.672  10.565  1.00 39.41 ? 152 ALA L N   1 
ATOM   13302 C  CA  . ALA L  1 152 ? 70.003  70.424  9.357   1.00 36.75 ? 152 ALA L CA  1 
ATOM   13303 C  C   . ALA L  1 152 ? 71.296  70.841  8.647   1.00 41.05 ? 152 ALA L C   1 
ATOM   13304 O  O   . ALA L  1 152 ? 72.369  70.873  9.265   1.00 35.25 ? 152 ALA L O   1 
ATOM   13305 C  CB  . ALA L  1 152 ? 69.177  71.651  9.719   1.00 34.30 ? 152 ALA L CB  1 
ATOM   13306 N  N   . GLN L  1 153 ? 71.191  71.158  7.354   1.00 44.02 ? 153 GLN L N   1 
ATOM   13307 C  CA  . GLN L  1 153 ? 72.334  71.660  6.585   1.00 40.81 ? 153 GLN L CA  1 
ATOM   13308 C  C   . GLN L  1 153 ? 72.634  73.121  6.918   1.00 50.76 ? 153 GLN L C   1 
ATOM   13309 O  O   . GLN L  1 153 ? 71.734  73.890  7.276   1.00 51.10 ? 153 GLN L O   1 
ATOM   13310 C  CB  . GLN L  1 153 ? 72.107  71.504  5.072   1.00 43.60 ? 153 GLN L CB  1 
ATOM   13311 C  CG  . GLN L  1 153 ? 71.159  72.536  4.443   1.00 49.40 ? 153 GLN L CG  1 
ATOM   13312 C  CD  . GLN L  1 153 ? 71.049  72.412  2.918   1.00 49.47 ? 153 GLN L CD  1 
ATOM   13313 O  OE1 . GLN L  1 153 ? 71.856  71.738  2.275   1.00 41.77 ? 153 GLN L OE1 1 
ATOM   13314 N  NE2 . GLN L  1 153 ? 70.044  73.068  2.341   1.00 49.85 ? 153 GLN L NE2 1 
ATOM   13315 O  OXT . GLN L  1 153 ? 73.783  73.572  6.829   1.00 54.45 ? 153 GLN L OXT 1 
HETATM 13316 ZN ZN  . ZN  M  2 .   ? 27.238  121.365 9.962   0.85 22.48 ? 201 ZN  A ZN  1 
HETATM 13317 ZN ZN  . ZN  N  2 .   ? 21.529  123.309 6.233   1.00 13.87 ? 202 ZN  A ZN  1 
HETATM 13318 S  S   . SO4 O  3 .   ? 28.425  119.707 7.243   0.69 16.07 ? 203 SO4 A S   1 
HETATM 13319 O  O1  . SO4 O  3 .   ? 29.265  120.361 6.243   0.69 21.04 ? 203 SO4 A O1  1 
HETATM 13320 O  O2  . SO4 O  3 .   ? 27.531  118.717 6.645   0.69 22.83 ? 203 SO4 A O2  1 
HETATM 13321 O  O3  . SO4 O  3 .   ? 29.316  119.040 8.181   0.69 19.01 ? 203 SO4 A O3  1 
HETATM 13322 O  O4  . SO4 O  3 .   ? 27.596  120.713 7.911   0.69 15.52 ? 203 SO4 A O4  1 
HETATM 13323 ZN ZN  . ZN  P  2 .   ? 22.896  106.242 38.730  0.67 21.76 ? 201 ZN  B ZN  1 
HETATM 13324 ZN ZN  . ZN  Q  2 .   ? 16.461  104.167 40.490  1.00 13.12 ? 202 ZN  B ZN  1 
HETATM 13325 S  S   . SO4 R  3 .   ? 23.219  108.009 41.790  0.66 23.20 ? 203 SO4 B S   1 
HETATM 13326 O  O1  . SO4 R  3 .   ? 24.413  108.650 41.244  0.66 23.16 ? 203 SO4 B O1  1 
HETATM 13327 O  O2  . SO4 R  3 .   ? 22.763  106.949 40.910  0.66 14.88 ? 203 SO4 B O2  1 
HETATM 13328 O  O3  . SO4 R  3 .   ? 23.615  107.456 43.093  0.66 26.51 ? 203 SO4 B O3  1 
HETATM 13329 O  O4  . SO4 R  3 .   ? 22.123  108.969 41.907  0.66 22.85 ? 203 SO4 B O4  1 
HETATM 13330 S  S   . SO4 S  3 .   ? 13.510  88.597  43.295  0.98 67.44 ? 204 SO4 B S   1 
HETATM 13331 O  O1  . SO4 S  3 .   ? 13.421  88.891  41.850  0.98 46.33 ? 204 SO4 B O1  1 
HETATM 13332 O  O2  . SO4 S  3 .   ? 12.905  89.669  44.103  0.98 42.52 ? 204 SO4 B O2  1 
HETATM 13333 O  O3  . SO4 S  3 .   ? 12.837  87.328  43.617  0.98 44.06 ? 204 SO4 B O3  1 
HETATM 13334 O  O4  . SO4 S  3 .   ? 14.927  88.496  43.635  0.98 49.48 ? 204 SO4 B O4  1 
HETATM 13335 ZN ZN  . ZN  T  2 .   ? 9.125   103.231 89.820  0.88 62.43 ? 201 ZN  C ZN  1 
HETATM 13336 ZN ZN  . ZN  U  2 .   ? 2.105   103.999 90.700  0.88 49.08 ? 202 ZN  C ZN  1 
HETATM 13337 S  S   . SO4 V  3 .   ? 9.515   106.409 89.958  0.75 63.50 ? 203 SO4 C S   1 
HETATM 13338 O  O1  . SO4 V  3 .   ? 10.828  106.245 89.338  0.75 56.65 ? 203 SO4 C O1  1 
HETATM 13339 O  O2  . SO4 V  3 .   ? 8.826   107.523 89.307  0.75 56.29 ? 203 SO4 C O2  1 
HETATM 13340 O  O3  . SO4 V  3 .   ? 8.711   105.195 89.829  0.75 54.69 ? 203 SO4 C O3  1 
HETATM 13341 O  O4  . SO4 V  3 .   ? 9.717   106.671 91.383  0.75 69.39 ? 203 SO4 C O4  1 
HETATM 13342 ZN ZN  . ZN  W  2 .   ? 17.971  85.923  62.925  0.62 32.18 ? 201 ZN  D ZN  1 
HETATM 13343 ZN ZN  . ZN  X  2 .   ? 13.056  83.763  58.524  1.00 15.00 ? 202 ZN  D ZN  1 
HETATM 13344 S  S   . SO4 Y  3 .   ? 19.495  82.183  63.317  0.64 38.65 ? 203 SO4 D S   1 
HETATM 13345 O  O1  . SO4 Y  3 .   ? 20.381  82.100  62.151  0.64 34.65 ? 203 SO4 D O1  1 
HETATM 13346 O  O2  . SO4 Y  3 .   ? 18.869  80.895  63.585  0.64 32.06 ? 203 SO4 D O2  1 
HETATM 13347 O  O3  . SO4 Y  3 .   ? 20.280  82.576  64.490  0.64 33.48 ? 203 SO4 D O3  1 
HETATM 13348 O  O4  . SO4 Y  3 .   ? 18.464  83.178  63.044  0.64 27.09 ? 203 SO4 D O4  1 
HETATM 13349 ZN ZN  . ZN  Z  2 .   ? 22.613  41.593  35.321  0.78 36.14 ? 201 ZN  E ZN  1 
HETATM 13350 ZN ZN  . ZN  AA 2 .   ? 16.403  38.737  32.848  1.00 28.50 ? 202 ZN  E ZN  1 
HETATM 13351 S  S   . SO4 BA 3 .   ? 22.242  39.850  37.958  0.73 35.39 ? 203 SO4 E S   1 
HETATM 13352 O  O1  . SO4 BA 3 .   ? 22.674  38.501  38.322  0.73 37.96 ? 203 SO4 E O1  1 
HETATM 13353 O  O2  . SO4 BA 3 .   ? 22.088  39.919  36.507  0.73 37.05 ? 203 SO4 E O2  1 
HETATM 13354 O  O3  . SO4 BA 3 .   ? 20.937  40.134  38.559  0.73 34.33 ? 203 SO4 E O3  1 
HETATM 13355 O  O4  . SO4 BA 3 .   ? 23.239  40.806  38.424  0.73 24.68 ? 203 SO4 E O4  1 
HETATM 13356 ZN ZN  . ZN  CA 2 .   ? 25.249  74.447  34.039  0.92 40.68 ? 201 ZN  F ZN  1 
HETATM 13357 ZN ZN  . ZN  DA 2 .   ? 19.388  78.250  32.445  1.00 23.28 ? 202 ZN  F ZN  1 
HETATM 13358 S  S   . SO4 EA 3 .   ? 26.957  76.336  31.682  0.72 33.61 ? 203 SO4 F S   1 
HETATM 13359 O  O1  . SO4 EA 3 .   ? 28.005  75.335  31.866  0.72 40.57 ? 203 SO4 F O1  1 
HETATM 13360 O  O2  . SO4 EA 3 .   ? 25.878  75.783  30.851  0.72 31.98 ? 203 SO4 F O2  1 
HETATM 13361 O  O3  . SO4 EA 3 .   ? 26.429  76.760  32.977  0.72 36.59 ? 203 SO4 F O3  1 
HETATM 13362 O  O4  . SO4 EA 3 .   ? 27.555  77.496  31.034  0.72 42.04 ? 203 SO4 F O4  1 
HETATM 13363 ZN ZN  . ZN  FA 2 .   ? 58.010  134.766 26.120  0.83 20.62 ? 201 ZN  G ZN  1 
HETATM 13364 ZN ZN  . ZN  GA 2 .   ? 64.410  137.787 26.592  1.00 15.01 ? 202 ZN  G ZN  1 
HETATM 13365 S  S   . SO4 HA 3 .   ? 56.983  136.405 28.785  0.82 21.83 ? 203 SO4 G S   1 
HETATM 13366 O  O1  . SO4 HA 3 .   ? 57.880  136.171 27.670  0.82 16.69 ? 203 SO4 G O1  1 
HETATM 13367 O  O2  . SO4 HA 3 .   ? 55.873  135.450 28.774  0.82 25.84 ? 203 SO4 G O2  1 
HETATM 13368 O  O3  . SO4 HA 3 .   ? 57.721  136.246 30.034  0.82 22.16 ? 203 SO4 G O3  1 
HETATM 13369 O  O4  . SO4 HA 3 .   ? 56.427  137.753 28.655  0.82 23.33 ? 203 SO4 G O4  1 
HETATM 13370 ZN ZN  . ZN  IA 2 .   ? 56.703  101.980 24.152  0.68 23.04 ? 201 ZN  H ZN  1 
HETATM 13371 ZN ZN  . ZN  JA 2 .   ? 62.604  98.329  25.183  1.00 12.29 ? 202 ZN  H ZN  1 
HETATM 13372 S  S   . SO4 KA 3 .   ? 56.128  100.419 21.090  0.72 16.70 ? 203 SO4 H S   1 
HETATM 13373 O  O1  . SO4 KA 3 .   ? 57.262  100.464 20.171  0.72 23.29 ? 203 SO4 H O1  1 
HETATM 13374 O  O2  . SO4 KA 3 .   ? 55.164  101.455 20.732  0.72 15.24 ? 203 SO4 H O2  1 
HETATM 13375 O  O3  . SO4 KA 3 .   ? 55.406  99.140  21.010  0.72 22.24 ? 203 SO4 H O3  1 
HETATM 13376 O  O4  . SO4 KA 3 .   ? 56.660  100.575 22.446  0.72 11.89 ? 203 SO4 H O4  1 
HETATM 13377 S  S   . SO4 LA 3 .   ? 62.892  87.368  37.356  0.89 70.61 ? 204 SO4 H S   1 
HETATM 13378 O  O1  . SO4 LA 3 .   ? 63.590  87.555  36.067  0.89 33.87 ? 204 SO4 H O1  1 
HETATM 13379 O  O2  . SO4 LA 3 .   ? 61.529  86.906  37.093  0.89 50.85 ? 204 SO4 H O2  1 
HETATM 13380 O  O3  . SO4 LA 3 .   ? 63.540  86.352  38.197  0.89 50.09 ? 204 SO4 H O3  1 
HETATM 13381 O  O4  . SO4 LA 3 .   ? 62.838  88.632  38.109  0.89 48.77 ? 204 SO4 H O4  1 
HETATM 13382 ZN ZN  . ZN  MA 2 .   ? 46.635  74.285  81.617  0.69 45.38 ? 201 ZN  I ZN  1 
HETATM 13383 ZN ZN  . ZN  NA 2 .   ? 52.401  73.442  85.672  0.94 32.63 ? 202 ZN  I ZN  1 
HETATM 13384 S  S   . SO4 OA 3 .   ? 46.221  70.606  81.168  0.87 54.17 ? 203 SO4 I S   1 
HETATM 13385 O  O1  . SO4 OA 3 .   ? 47.565  70.030  81.076  0.87 42.60 ? 203 SO4 I O1  1 
HETATM 13386 O  O2  . SO4 OA 3 .   ? 45.492  70.415  79.916  0.87 45.17 ? 203 SO4 I O2  1 
HETATM 13387 O  O3  . SO4 OA 3 .   ? 45.452  69.923  82.201  0.87 58.07 ? 203 SO4 I O3  1 
HETATM 13388 O  O4  . SO4 OA 3 .   ? 46.312  72.027  81.502  0.87 42.11 ? 203 SO4 I O4  1 
HETATM 13389 ZN ZN  . ZN  PA 2 .   ? 50.880  90.408  53.280  0.54 26.88 ? 201 ZN  J ZN  1 
HETATM 13390 ZN ZN  . ZN  QA 2 .   ? 57.090  92.469  51.484  1.00 12.90 ? 202 ZN  J ZN  1 
HETATM 13391 S  S   . SO4 RA 3 .   ? 49.651  93.933  53.405  0.56 22.03 ? 203 SO4 J S   1 
HETATM 13392 O  O1  . SO4 RA 3 .   ? 50.501  94.820  54.205  0.56 22.63 ? 203 SO4 J O1  1 
HETATM 13393 O  O2  . SO4 RA 3 .   ? 49.237  94.554  52.146  0.56 25.17 ? 203 SO4 J O2  1 
HETATM 13394 O  O3  . SO4 RA 3 .   ? 50.407  92.718  53.121  0.56 17.48 ? 203 SO4 J O3  1 
HETATM 13395 O  O4  . SO4 RA 3 .   ? 48.429  93.602  54.117  0.56 20.62 ? 203 SO4 J O4  1 
HETATM 13396 ZN ZN  . ZN  SA 2 .   ? 67.852  56.826  0.150   0.91 58.15 ? 201 ZN  K ZN  1 
HETATM 13397 ZN ZN  . ZN  TA 2 .   ? 74.284  54.954  0.056   0.81 46.67 ? 202 ZN  K ZN  1 
HETATM 13398 S  S   . SO4 UA 3 .   ? 68.225  58.712  -2.770  0.79 51.31 ? 203 SO4 K S   1 
HETATM 13399 O  O1  . SO4 UA 3 .   ? 69.389  59.599  -2.760  0.79 49.09 ? 203 SO4 K O1  1 
HETATM 13400 O  O2  . SO4 UA 3 .   ? 68.080  58.104  -4.091  0.79 60.73 ? 203 SO4 K O2  1 
HETATM 13401 O  O3  . SO4 UA 3 .   ? 68.420  57.666  -1.771  0.79 56.46 ? 203 SO4 K O3  1 
HETATM 13402 O  O4  . SO4 UA 3 .   ? 67.002  59.450  -2.477  0.79 46.23 ? 203 SO4 K O4  1 
HETATM 13403 ZN ZN  . ZN  VA 2 .   ? 56.619  70.487  28.584  0.83 36.98 ? 201 ZN  L ZN  1 
HETATM 13404 ZN ZN  . ZN  WA 2 .   ? 61.486  72.209  33.412  1.00 20.50 ? 202 ZN  L ZN  1 
HETATM 13405 S  S   . SO4 XA 3 .   ? 55.005  68.771  31.023  0.76 37.50 ? 203 SO4 L S   1 
HETATM 13406 O  O1  . SO4 XA 3 .   ? 56.011  69.706  30.519  0.76 26.89 ? 203 SO4 L O1  1 
HETATM 13407 O  O2  . SO4 XA 3 .   ? 54.255  68.228  29.895  0.76 36.25 ? 203 SO4 L O2  1 
HETATM 13408 O  O3  . SO4 XA 3 .   ? 55.654  67.682  31.752  0.76 37.09 ? 203 SO4 L O3  1 
HETATM 13409 O  O4  . SO4 XA 3 .   ? 54.082  69.465  31.925  0.76 30.55 ? 203 SO4 L O4  1 
HETATM 13410 O  O   . HOH YA 4 .   ? 27.434  114.859 23.941  1.00 13.07 ? 301 HOH A O   1 
HETATM 13411 O  O   . HOH YA 4 .   ? 26.116  117.726 25.268  1.00 11.72 ? 302 HOH A O   1 
HETATM 13412 O  O   . HOH YA 4 .   ? 2.562   123.124 21.021  1.00 13.28 ? 303 HOH A O   1 
HETATM 13413 O  O   . HOH YA 4 .   ? 13.997  131.611 1.069   1.00 25.44 ? 304 HOH A O   1 
HETATM 13414 O  O   . HOH YA 4 .   ? 38.438  127.982 14.684  1.00 15.72 ? 305 HOH A O   1 
HETATM 13415 O  O   . HOH YA 4 .   ? 23.196  119.063 5.068   1.00 12.76 ? 306 HOH A O   1 
HETATM 13416 O  O   . HOH YA 4 .   ? 25.200  134.519 18.141  1.00 24.88 ? 307 HOH A O   1 
HETATM 13417 O  O   . HOH YA 4 .   ? 0.557   129.980 25.883  1.00 21.89 ? 308 HOH A O   1 
HETATM 13418 O  O   . HOH YA 4 .   ? 19.683  134.093 7.386   1.00 18.66 ? 309 HOH A O   1 
HETATM 13419 O  O   . HOH YA 4 .   ? 26.037  109.478 20.600  1.00 12.51 ? 310 HOH A O   1 
HETATM 13420 O  O   . HOH YA 4 .   ? 19.633  133.615 13.907  1.00 15.59 ? 311 HOH A O   1 
HETATM 13421 O  O   . HOH YA 4 .   ? 20.007  120.341 34.133  1.00 17.43 ? 312 HOH A O   1 
HETATM 13422 O  O   . HOH YA 4 .   ? 12.902  123.443 7.195   1.00 16.56 ? 313 HOH A O   1 
HETATM 13423 O  O   . HOH YA 4 .   ? 34.835  116.979 9.969   1.00 20.63 ? 314 HOH A O   1 
HETATM 13424 O  O   . HOH YA 4 .   ? 25.894  135.114 9.029   1.00 21.49 ? 315 HOH A O   1 
HETATM 13425 O  O   . HOH YA 4 .   ? 13.682  120.961 7.277   1.00 12.20 ? 316 HOH A O   1 
HETATM 13426 O  O   . HOH YA 4 .   ? 24.418  129.207 -4.140  1.00 22.02 ? 317 HOH A O   1 
HETATM 13427 O  O   . HOH YA 4 .   ? 22.715  128.154 8.363   1.00 12.94 ? 318 HOH A O   1 
HETATM 13428 O  O   . HOH YA 4 .   ? 23.485  107.031 13.471  1.00 21.38 ? 319 HOH A O   1 
HETATM 13429 O  O   . HOH YA 4 .   ? 17.231  132.363 14.097  1.00 13.63 ? 320 HOH A O   1 
HETATM 13430 O  O   . HOH YA 4 .   ? 8.674   122.823 23.875  1.00 17.96 ? 321 HOH A O   1 
HETATM 13431 O  O   . HOH YA 4 .   ? 13.527  132.094 13.304  1.00 21.44 ? 322 HOH A O   1 
HETATM 13432 O  O   . HOH YA 4 .   ? 16.182  108.842 12.540  1.00 30.03 ? 323 HOH A O   1 
HETATM 13433 O  O   . HOH YA 4 .   ? 22.818  134.442 9.512   1.00 23.54 ? 324 HOH A O   1 
HETATM 13434 O  O   . HOH YA 4 .   ? 19.770  120.098 1.287   1.00 23.00 ? 325 HOH A O   1 
HETATM 13435 O  O   . HOH YA 4 .   ? 39.617  130.767 22.699  1.00 29.32 ? 326 HOH A O   1 
HETATM 13436 O  O   . HOH YA 4 .   ? 22.258  132.885 14.032  1.00 18.38 ? 327 HOH A O   1 
HETATM 13437 O  O   . HOH YA 4 .   ? 37.621  120.576 22.540  1.00 28.48 ? 328 HOH A O   1 
HETATM 13438 O  O   . HOH YA 4 .   ? 15.985  111.348 12.060  1.00 24.02 ? 329 HOH A O   1 
HETATM 13439 O  O   . HOH YA 4 .   ? 12.241  133.783 16.710  1.00 25.74 ? 330 HOH A O   1 
HETATM 13440 O  O   . HOH YA 4 .   ? 31.529  115.341 21.580  1.00 31.15 ? 331 HOH A O   1 
HETATM 13441 O  O   . HOH YA 4 .   ? 13.926  119.106 38.580  1.00 30.18 ? 332 HOH A O   1 
HETATM 13442 O  O   . HOH YA 4 .   ? 31.082  129.513 -0.458  1.00 27.87 ? 333 HOH A O   1 
HETATM 13443 O  O   . HOH YA 4 .   ? 24.054  126.865 -5.529  1.00 25.29 ? 334 HOH A O   1 
HETATM 13444 O  O   . HOH YA 4 .   ? 38.778  127.404 11.965  1.00 19.56 ? 335 HOH A O   1 
HETATM 13445 O  O   . HOH YA 4 .   ? 26.978  136.104 14.496  1.00 31.30 ? 336 HOH A O   1 
HETATM 13446 O  O   . HOH YA 4 .   ? 33.731  109.078 20.875  1.00 26.87 ? 337 HOH A O   1 
HETATM 13447 O  O   . HOH YA 4 .   ? 40.352  125.483 24.550  1.00 27.77 ? 338 HOH A O   1 
HETATM 13448 O  O   . HOH YA 4 .   ? 24.281  133.694 15.279  1.00 21.57 ? 339 HOH A O   1 
HETATM 13449 O  O   . HOH YA 4 .   ? 12.956  113.764 22.182  1.00 31.30 ? 340 HOH A O   1 
HETATM 13450 O  O   . HOH YA 4 .   ? 37.780  120.735 19.333  1.00 25.42 ? 341 HOH A O   1 
HETATM 13451 O  O   . HOH YA 4 .   ? 29.970  116.791 24.484  1.00 25.76 ? 342 HOH A O   1 
HETATM 13452 O  O   . HOH YA 4 .   ? 34.779  135.484 8.891   1.00 25.98 ? 343 HOH A O   1 
HETATM 13453 O  O   . HOH YA 4 .   ? 13.195  120.871 30.481  1.00 24.49 ? 344 HOH A O   1 
HETATM 13454 O  O   . HOH YA 4 .   ? 29.292  114.138 21.509  1.00 23.37 ? 345 HOH A O   1 
HETATM 13455 O  O   . HOH YA 4 .   ? 20.090  117.867 5.443   1.00 22.35 ? 346 HOH A O   1 
HETATM 13456 O  O   . HOH YA 4 .   ? 8.162   120.864 15.935  1.00 28.41 ? 347 HOH A O   1 
HETATM 13457 O  O   . HOH YA 4 .   ? 40.510  126.443 16.298  1.00 20.54 ? 348 HOH A O   1 
HETATM 13458 O  O   . HOH YA 4 .   ? 8.767   129.781 23.599  1.00 20.95 ? 349 HOH A O   1 
HETATM 13459 O  O   . HOH YA 4 .   ? 32.951  130.060 4.144   1.00 26.66 ? 350 HOH A O   1 
HETATM 13460 O  O   . HOH YA 4 .   ? 33.112  123.123 27.405  1.00 30.20 ? 351 HOH A O   1 
HETATM 13461 O  O   . HOH YA 4 .   ? 23.690  133.996 11.531  1.00 20.09 ? 352 HOH A O   1 
HETATM 13462 O  O   . HOH YA 4 .   ? 20.876  120.606 -4.413  1.00 30.33 ? 353 HOH A O   1 
HETATM 13463 O  O   . HOH YA 4 .   ? 23.977  131.820 31.242  1.00 41.15 ? 354 HOH A O   1 
HETATM 13464 O  O   . HOH YA 4 .   ? 30.104  121.821 -4.369  1.00 31.88 ? 355 HOH A O   1 
HETATM 13465 O  O   . HOH YA 4 .   ? 18.107  128.387 0.671   1.00 18.83 ? 356 HOH A O   1 
HETATM 13466 O  O   . HOH YA 4 .   ? 20.634  133.079 2.504   1.00 26.48 ? 357 HOH A O   1 
HETATM 13467 O  O   . HOH YA 4 .   ? 12.520  115.353 16.047  1.00 16.76 ? 358 HOH A O   1 
HETATM 13468 O  O   . HOH YA 4 .   ? 24.806  108.304 11.760  1.00 23.23 ? 359 HOH A O   1 
HETATM 13469 O  O   . HOH YA 4 .   ? 3.682   125.437 26.336  1.00 25.75 ? 360 HOH A O   1 
HETATM 13470 O  O   . HOH YA 4 .   ? 27.941  134.871 17.838  1.00 24.07 ? 361 HOH A O   1 
HETATM 13471 O  O   . HOH YA 4 .   ? 33.622  114.735 19.505  1.00 39.83 ? 362 HOH A O   1 
HETATM 13472 O  O   . HOH YA 4 .   ? 13.623  111.005 13.376  1.00 34.89 ? 363 HOH A O   1 
HETATM 13473 O  O   . HOH YA 4 .   ? 24.558  136.894 19.273  1.00 33.43 ? 364 HOH A O   1 
HETATM 13474 O  O   . HOH YA 4 .   ? 39.289  122.480 17.659  1.00 25.79 ? 365 HOH A O   1 
HETATM 13475 O  O   . HOH YA 4 .   ? 7.948   124.866 25.665  1.00 22.47 ? 366 HOH A O   1 
HETATM 13476 O  O   . HOH YA 4 .   ? 11.511  115.072 13.279  1.00 25.58 ? 367 HOH A O   1 
HETATM 13477 O  O   . HOH YA 4 .   ? 35.713  132.455 9.005   1.00 27.00 ? 368 HOH A O   1 
HETATM 13478 O  O   . HOH YA 4 .   ? 12.732  113.435 11.518  1.00 23.85 ? 369 HOH A O   1 
HETATM 13479 O  O   . HOH YA 4 .   ? 29.889  104.234 13.634  1.00 28.05 ? 370 HOH A O   1 
HETATM 13480 O  O   . HOH YA 4 .   ? 40.497  123.641 15.801  1.00 26.80 ? 371 HOH A O   1 
HETATM 13481 O  O   . HOH YA 4 .   ? 28.077  133.935 5.038   1.00 24.77 ? 372 HOH A O   1 
HETATM 13482 O  O   . HOH YA 4 .   ? 29.467  121.980 -7.096  1.00 27.48 ? 373 HOH A O   1 
HETATM 13483 O  O   . HOH YA 4 .   ? 25.766  134.610 25.747  1.00 27.61 ? 374 HOH A O   1 
HETATM 13484 O  O   . HOH YA 4 .   ? 17.670  113.999 6.456   1.00 27.91 ? 375 HOH A O   1 
HETATM 13485 O  O   . HOH YA 4 .   ? 10.973  125.300 7.859   1.00 21.15 ? 376 HOH A O   1 
HETATM 13486 O  O   . HOH YA 4 .   ? 33.227  106.218 20.869  1.00 28.31 ? 377 HOH A O   1 
HETATM 13487 O  O   . HOH YA 4 .   ? 18.432  135.514 16.295  1.00 26.64 ? 378 HOH A O   1 
HETATM 13488 O  O   . HOH YA 4 .   ? 31.691  118.232 7.276   1.00 27.43 ? 379 HOH A O   1 
HETATM 13489 O  O   . HOH YA 4 .   ? 10.142  115.771 4.138   1.00 29.18 ? 380 HOH A O   1 
HETATM 13490 O  O   . HOH YA 4 .   ? 26.262  138.000 20.661  1.00 25.24 ? 381 HOH A O   1 
HETATM 13491 O  O   . HOH YA 4 .   ? 9.151   125.838 9.756   1.00 27.91 ? 382 HOH A O   1 
HETATM 13492 O  O   . HOH YA 4 .   ? 15.010  119.216 -0.750  1.00 29.00 ? 383 HOH A O   1 
HETATM 13493 O  O   . HOH YA 4 .   ? 43.038  136.280 17.359  1.00 37.44 ? 384 HOH A O   1 
HETATM 13494 O  O   . HOH YA 4 .   ? 27.695  133.275 -5.188  1.00 35.12 ? 385 HOH A O   1 
HETATM 13495 O  O   . HOH YA 4 .   ? 31.130  111.825 22.956  1.00 23.52 ? 386 HOH A O   1 
HETATM 13496 O  O   . HOH YA 4 .   ? 29.593  138.986 12.773  1.00 34.20 ? 387 HOH A O   1 
HETATM 13497 O  O   . HOH YA 4 .   ? 12.614  122.108 -1.727  1.00 27.55 ? 388 HOH A O   1 
HETATM 13498 O  O   . HOH YA 4 .   ? 36.793  114.413 19.989  1.00 45.01 ? 389 HOH A O   1 
HETATM 13499 O  O   . HOH YA 4 .   ? 40.550  134.094 10.977  1.00 36.19 ? 390 HOH A O   1 
HETATM 13500 O  O   . HOH YA 4 .   ? 19.382  123.417 34.376  1.00 29.91 ? 391 HOH A O   1 
HETATM 13501 O  O   . HOH YA 4 .   ? 33.495  107.674 9.789   1.00 41.17 ? 392 HOH A O   1 
HETATM 13502 O  O   . HOH YA 4 .   ? 27.801  138.988 10.277  1.00 36.74 ? 393 HOH A O   1 
HETATM 13503 O  O   . HOH YA 4 .   ? 42.216  119.405 23.584  1.00 41.44 ? 394 HOH A O   1 
HETATM 13504 O  O   . HOH YA 4 .   ? 28.371  131.256 28.388  1.00 31.81 ? 395 HOH A O   1 
HETATM 13505 O  O   . HOH YA 4 .   ? 27.085  133.290 27.702  1.00 29.71 ? 396 HOH A O   1 
HETATM 13506 O  O   . HOH YA 4 .   ? 13.556  114.102 19.899  1.00 31.78 ? 397 HOH A O   1 
HETATM 13507 O  O   . HOH YA 4 .   ? 13.805  134.533 14.744  1.00 27.08 ? 398 HOH A O   1 
HETATM 13508 O  O   . HOH YA 4 .   ? 27.373  135.544 6.418   1.00 35.48 ? 399 HOH A O   1 
HETATM 13509 O  O   . HOH YA 4 .   ? 26.462  126.609 32.312  1.00 24.84 ? 400 HOH A O   1 
HETATM 13510 O  O   . HOH YA 4 .   ? 24.601  125.537 31.375  1.00 24.87 ? 401 HOH A O   1 
HETATM 13511 O  O   . HOH YA 4 .   ? 33.244  115.009 11.109  1.00 38.23 ? 402 HOH A O   1 
HETATM 13512 O  O   . HOH YA 4 .   ? 18.248  131.155 1.100   1.00 29.61 ? 403 HOH A O   1 
HETATM 13513 O  O   . HOH YA 4 .   ? 7.120   131.011 17.466  1.00 27.23 ? 404 HOH A O   1 
HETATM 13514 O  O   . HOH YA 4 .   ? 3.342   131.097 21.980  1.00 31.49 ? 405 HOH A O   1 
HETATM 13515 O  O   . HOH YA 4 .   ? 17.327  133.279 29.177  1.00 39.31 ? 406 HOH A O   1 
HETATM 13516 O  O   . HOH YA 4 .   ? 13.095  133.097 10.817  1.00 35.52 ? 407 HOH A O   1 
HETATM 13517 O  O   . HOH YA 4 .   ? 15.427  134.224 31.532  1.00 34.45 ? 408 HOH A O   1 
HETATM 13518 O  O   . HOH YA 4 .   ? 19.908  111.526 5.912   1.00 39.14 ? 409 HOH A O   1 
HETATM 13519 O  O   . HOH YA 4 .   ? 20.652  125.071 29.967  1.00 22.15 ? 410 HOH A O   1 
HETATM 13520 O  O   . HOH YA 4 .   ? 13.033  133.794 2.873   1.00 30.39 ? 411 HOH A O   1 
HETATM 13521 O  O   . HOH YA 4 .   ? 20.028  135.231 4.620   1.00 28.85 ? 412 HOH A O   1 
HETATM 13522 O  O   . HOH YA 4 .   ? 33.997  130.732 26.984  1.00 31.61 ? 413 HOH A O   1 
HETATM 13523 O  O   . HOH YA 4 .   ? 35.187  131.650 6.500   1.00 30.96 ? 414 HOH A O   1 
HETATM 13524 O  O   . HOH YA 4 .   ? 18.471  117.241 3.838   1.00 27.95 ? 415 HOH A O   1 
HETATM 13525 O  O   . HOH YA 4 .   ? 12.436  130.536 8.011   1.00 28.24 ? 416 HOH A O   1 
HETATM 13526 O  O   . HOH YA 4 .   ? 5.192   118.759 15.317  1.00 33.63 ? 417 HOH A O   1 
HETATM 13527 O  O   . HOH YA 4 .   ? 18.645  126.288 29.294  1.00 23.06 ? 418 HOH A O   1 
HETATM 13528 O  O   . HOH YA 4 .   ? 28.896  118.844 -6.970  1.00 28.76 ? 419 HOH A O   1 
HETATM 13529 O  O   . HOH YA 4 .   ? 26.509  136.441 10.925  1.00 29.69 ? 420 HOH A O   1 
HETATM 13530 O  O   . HOH YA 4 .   ? 20.092  134.605 29.181  1.00 36.35 ? 421 HOH A O   1 
HETATM 13531 O  O   . HOH YA 4 .   ? 17.200  120.058 41.579  1.00 34.29 ? 422 HOH A O   1 
HETATM 13532 O  O   . HOH YA 4 .   ? 37.273  119.706 25.148  1.00 31.11 ? 423 HOH A O   1 
HETATM 13533 O  O   . HOH YA 4 .   ? 16.262  131.864 -0.290  1.00 34.10 ? 424 HOH A O   1 
HETATM 13534 O  O   . HOH YA 4 .   ? 16.202  134.333 12.015  1.00 28.59 ? 425 HOH A O   1 
HETATM 13535 O  O   . HOH YA 4 .   ? 8.916   113.044 21.883  1.00 37.97 ? 426 HOH A O   1 
HETATM 13536 O  O   . HOH YA 4 .   ? 25.181  136.411 12.764  1.00 34.98 ? 427 HOH A O   1 
HETATM 13537 O  O   . HOH YA 4 .   ? 33.356  125.886 27.563  1.00 31.56 ? 428 HOH A O   1 
HETATM 13538 O  O   . HOH YA 4 .   ? 37.069  118.063 16.355  1.00 32.19 ? 429 HOH A O   1 
HETATM 13539 O  O   . HOH YA 4 .   ? 22.134  130.691 32.420  1.00 41.06 ? 430 HOH A O   1 
HETATM 13540 O  O   . HOH YA 4 .   ? 5.504   132.298 22.713  1.00 36.52 ? 431 HOH A O   1 
HETATM 13541 O  O   . HOH YA 4 .   ? 8.532   119.164 26.836  1.00 38.04 ? 432 HOH A O   1 
HETATM 13542 O  O   . HOH YA 4 .   ? 44.204  121.746 22.029  1.00 34.85 ? 433 HOH A O   1 
HETATM 13543 O  O   . HOH YA 4 .   ? 8.142   120.480 29.356  1.00 39.55 ? 434 HOH A O   1 
HETATM 13544 O  O   . HOH YA 4 .   ? 30.646  133.359 3.308   1.00 28.28 ? 435 HOH A O   1 
HETATM 13545 O  O   . HOH YA 4 .   ? 26.536  128.712 29.902  1.00 33.03 ? 436 HOH A O   1 
HETATM 13546 O  O   . HOH YA 4 .   ? 10.774  117.077 24.664  1.00 34.94 ? 437 HOH A O   1 
HETATM 13547 O  O   . HOH YA 4 .   ? 11.541  130.941 24.874  1.00 28.84 ? 438 HOH A O   1 
HETATM 13548 O  O   . HOH YA 4 .   ? 16.859  115.286 8.931   1.00 15.33 ? 439 HOH A O   1 
HETATM 13549 O  O   . HOH YA 4 .   ? 27.776  113.674 18.308  1.00 28.95 ? 440 HOH A O   1 
HETATM 13550 O  O   . HOH YA 4 .   ? 25.015  114.998 -3.760  1.00 32.33 ? 441 HOH A O   1 
HETATM 13551 O  O   . HOH YA 4 .   ? 8.069   115.449 21.929  1.00 35.07 ? 442 HOH A O   1 
HETATM 13552 O  O   . HOH ZA 4 .   ? 18.353  99.310  38.767  1.00 9.93  ? 301 HOH B O   1 
HETATM 13553 O  O   . HOH ZA 4 .   ? 36.534  107.401 30.208  1.00 7.60  ? 302 HOH B O   1 
HETATM 13554 O  O   . HOH ZA 4 .   ? 26.371  109.956 23.444  1.00 8.62  ? 303 HOH B O   1 
HETATM 13555 O  O   . HOH ZA 4 .   ? 35.042  99.903  37.397  1.00 15.18 ? 304 HOH B O   1 
HETATM 13556 O  O   . HOH ZA 4 .   ? 25.005  117.913 27.982  1.00 6.82  ? 305 HOH B O   1 
HETATM 13557 O  O   . HOH ZA 4 .   ? 14.523  94.499  43.461  1.00 14.90 ? 306 HOH B O   1 
HETATM 13558 O  O   . HOH ZA 4 .   ? 9.481   106.610 37.238  1.00 17.00 ? 307 HOH B O   1 
HETATM 13559 O  O   . HOH ZA 4 .   ? 30.009  90.829  30.092  1.00 18.81 ? 308 HOH B O   1 
HETATM 13560 O  O   . HOH ZA 4 .   ? 26.746  102.099 17.496  1.00 16.36 ? 309 HOH B O   1 
HETATM 13561 O  O   . HOH ZA 4 .   ? 21.813  91.562  41.730  1.00 22.65 ? 310 HOH B O   1 
HETATM 13562 O  O   . HOH ZA 4 .   ? 15.747  98.164  51.029  1.00 16.56 ? 311 HOH B O   1 
HETATM 13563 O  O   . HOH ZA 4 .   ? 26.678  88.676  37.067  1.00 18.72 ? 312 HOH B O   1 
HETATM 13564 O  O   . HOH ZA 4 .   ? 39.020  96.598  30.174  1.00 13.27 ? 313 HOH B O   1 
HETATM 13565 O  O   . HOH ZA 4 .   ? 7.589   95.923  42.967  1.00 21.80 ? 314 HOH B O   1 
HETATM 13566 O  O   . HOH ZA 4 .   ? 15.326  93.410  38.704  1.00 17.47 ? 315 HOH B O   1 
HETATM 13567 O  O   . HOH ZA 4 .   ? 17.852  108.397 42.131  1.00 20.70 ? 316 HOH B O   1 
HETATM 13568 O  O   . HOH ZA 4 .   ? 12.734  115.981 33.204  1.00 21.56 ? 317 HOH B O   1 
HETATM 13569 O  O   . HOH ZA 4 .   ? 29.580  111.091 25.770  1.00 16.36 ? 318 HOH B O   1 
HETATM 13570 O  O   . HOH ZA 4 .   ? 22.355  102.724 18.017  1.00 14.59 ? 319 HOH B O   1 
HETATM 13571 O  O   . HOH ZA 4 .   ? 40.447  100.298 27.199  1.00 15.08 ? 320 HOH B O   1 
HETATM 13572 O  O   . HOH ZA 4 .   ? 36.947  101.745 36.143  1.00 12.62 ? 321 HOH B O   1 
HETATM 13573 O  O   . HOH ZA 4 .   ? 34.836  109.030 35.927  1.00 16.61 ? 322 HOH B O   1 
HETATM 13574 O  O   . HOH ZA 4 .   ? 20.286  93.156  45.408  1.00 20.81 ? 323 HOH B O   1 
HETATM 13575 O  O   . HOH ZA 4 .   ? 14.741  94.931  31.730  1.00 21.73 ? 324 HOH B O   1 
HETATM 13576 O  O   . HOH ZA 4 .   ? 6.826   93.276  41.245  1.00 22.79 ? 325 HOH B O   1 
HETATM 13577 O  O   . HOH ZA 4 .   ? 7.388   99.293  36.474  1.00 22.75 ? 326 HOH B O   1 
HETATM 13578 O  O   . HOH ZA 4 .   ? 8.351   100.640 25.928  1.00 20.09 ? 327 HOH B O   1 
HETATM 13579 O  O   . HOH ZA 4 .   ? 40.073  102.491 28.688  1.00 12.98 ? 328 HOH B O   1 
HETATM 13580 O  O   . HOH ZA 4 .   ? 26.143  88.633  39.887  1.00 24.14 ? 329 HOH B O   1 
HETATM 13581 O  O   . HOH ZA 4 .   ? 22.289  93.504  43.215  1.00 16.83 ? 330 HOH B O   1 
HETATM 13582 O  O   . HOH ZA 4 .   ? 31.714  89.694  28.458  1.00 26.14 ? 331 HOH B O   1 
HETATM 13583 O  O   . HOH ZA 4 .   ? 16.084  92.708  51.961  1.00 17.45 ? 332 HOH B O   1 
HETATM 13584 O  O   . HOH ZA 4 .   ? 11.050  95.407  31.468  1.00 18.83 ? 333 HOH B O   1 
HETATM 13585 O  O   . HOH ZA 4 .   ? 39.362  95.935  35.227  1.00 23.17 ? 334 HOH B O   1 
HETATM 13586 O  O   . HOH ZA 4 .   ? 29.706  95.980  44.091  1.00 18.39 ? 335 HOH B O   1 
HETATM 13587 O  O   . HOH ZA 4 .   ? 8.606   104.055 36.884  1.00 19.23 ? 336 HOH B O   1 
HETATM 13588 O  O   . HOH ZA 4 .   ? 8.788   112.717 24.588  1.00 26.66 ? 337 HOH B O   1 
HETATM 13589 O  O   . HOH ZA 4 .   ? 39.130  95.803  25.883  1.00 18.00 ? 338 HOH B O   1 
HETATM 13590 O  O   . HOH ZA 4 .   ? 30.001  91.955  41.812  1.00 21.10 ? 339 HOH B O   1 
HETATM 13591 O  O   . HOH ZA 4 .   ? 37.331  114.119 33.451  1.00 28.36 ? 340 HOH B O   1 
HETATM 13592 O  O   . HOH ZA 4 .   ? 13.271  96.255  45.779  1.00 20.29 ? 341 HOH B O   1 
HETATM 13593 O  O   . HOH ZA 4 .   ? 21.215  119.467 36.563  1.00 19.33 ? 342 HOH B O   1 
HETATM 13594 O  O   . HOH ZA 4 .   ? 12.423  97.366  48.370  1.00 24.90 ? 343 HOH B O   1 
HETATM 13595 O  O   . HOH ZA 4 .   ? 10.527  111.529 28.743  1.00 16.68 ? 344 HOH B O   1 
HETATM 13596 O  O   . HOH ZA 4 .   ? 39.593  109.386 37.420  1.00 23.46 ? 345 HOH B O   1 
HETATM 13597 O  O   . HOH ZA 4 .   ? 29.955  110.286 41.199  1.00 20.98 ? 346 HOH B O   1 
HETATM 13598 O  O   . HOH ZA 4 .   ? 15.106  116.389 39.652  1.00 29.49 ? 347 HOH B O   1 
HETATM 13599 O  O   . HOH ZA 4 .   ? 6.660   106.138 26.713  1.00 17.23 ? 348 HOH B O   1 
HETATM 13600 O  O   . HOH ZA 4 .   ? 35.967  105.989 34.084  1.00 9.71  ? 349 HOH B O   1 
HETATM 13601 O  O   . HOH ZA 4 .   ? 36.623  104.565 36.063  1.00 14.90 ? 350 HOH B O   1 
HETATM 13602 O  O   . HOH ZA 4 .   ? 34.097  106.199 24.946  1.00 17.87 ? 351 HOH B O   1 
HETATM 13603 O  O   . HOH ZA 4 .   ? 8.250   96.693  35.969  1.00 23.73 ? 352 HOH B O   1 
HETATM 13604 O  O   . HOH ZA 4 .   ? 23.355  104.444 41.649  1.00 20.74 ? 353 HOH B O   1 
HETATM 13605 O  O   . HOH ZA 4 .   ? 27.274  112.462 25.258  1.00 14.93 ? 354 HOH B O   1 
HETATM 13606 O  O   . HOH ZA 4 .   ? 20.183  94.572  34.213  1.00 17.72 ? 355 HOH B O   1 
HETATM 13607 O  O   . HOH ZA 4 .   ? 9.834   97.150  20.320  1.00 20.08 ? 356 HOH B O   1 
HETATM 13608 O  O   . HOH ZA 4 .   ? 26.534  97.643  46.264  1.00 25.16 ? 357 HOH B O   1 
HETATM 13609 O  O   . HOH ZA 4 .   ? 36.991  108.706 27.714  1.00 19.32 ? 358 HOH B O   1 
HETATM 13610 O  O   . HOH ZA 4 .   ? 34.978  97.013  23.632  1.00 31.89 ? 359 HOH B O   1 
HETATM 13611 O  O   . HOH ZA 4 .   ? 39.936  97.549  27.958  1.00 17.85 ? 360 HOH B O   1 
HETATM 13612 O  O   . HOH ZA 4 .   ? 21.169  99.148  15.555  1.00 31.07 ? 361 HOH B O   1 
HETATM 13613 O  O   . HOH ZA 4 .   ? 13.305  107.525 44.659  1.00 21.23 ? 362 HOH B O   1 
HETATM 13614 O  O   . HOH ZA 4 .   ? 21.252  113.650 41.667  1.00 21.03 ? 363 HOH B O   1 
HETATM 13615 O  O   . HOH ZA 4 .   ? 14.473  92.682  49.923  1.00 22.70 ? 364 HOH B O   1 
HETATM 13616 O  O   . HOH ZA 4 .   ? 42.868  97.012  28.216  1.00 24.63 ? 365 HOH B O   1 
HETATM 13617 O  O   . HOH ZA 4 .   ? 12.656  112.656 24.890  1.00 28.23 ? 366 HOH B O   1 
HETATM 13618 O  O   . HOH ZA 4 .   ? 23.899  91.072  46.528  1.00 25.60 ? 367 HOH B O   1 
HETATM 13619 O  O   . HOH ZA 4 .   ? 36.300  92.994  23.697  1.00 27.34 ? 368 HOH B O   1 
HETATM 13620 O  O   . HOH ZA 4 .   ? 11.309  93.789  28.271  1.00 24.63 ? 369 HOH B O   1 
HETATM 13621 O  O   . HOH ZA 4 .   ? 27.872  113.645 28.150  1.00 20.73 ? 370 HOH B O   1 
HETATM 13622 O  O   . HOH ZA 4 .   ? 9.105   95.048  19.377  1.00 28.26 ? 371 HOH B O   1 
HETATM 13623 O  O   . HOH ZA 4 .   ? 23.876  114.683 41.013  1.00 27.82 ? 372 HOH B O   1 
HETATM 13624 O  O   . HOH ZA 4 .   ? 6.069   104.434 24.597  1.00 27.25 ? 373 HOH B O   1 
HETATM 13625 O  O   . HOH ZA 4 .   ? 29.458  98.591  21.471  1.00 16.11 ? 374 HOH B O   1 
HETATM 13626 O  O   . HOH ZA 4 .   ? 3.128   106.201 29.304  1.00 26.99 ? 375 HOH B O   1 
HETATM 13627 O  O   . HOH ZA 4 .   ? 10.683  116.262 30.889  1.00 38.33 ? 376 HOH B O   1 
HETATM 13628 O  O   . HOH ZA 4 .   ? 28.261  99.022  18.960  1.00 23.70 ? 377 HOH B O   1 
HETATM 13629 O  O   . HOH ZA 4 .   ? 7.234   101.915 35.845  1.00 21.84 ? 378 HOH B O   1 
HETATM 13630 O  O   . HOH ZA 4 .   ? 42.833  100.619 26.015  1.00 21.62 ? 379 HOH B O   1 
HETATM 13631 O  O   . HOH ZA 4 .   ? 31.798  96.119  41.569  1.00 28.84 ? 380 HOH B O   1 
HETATM 13632 O  O   . HOH ZA 4 .   ? 8.499   112.317 31.280  1.00 37.90 ? 381 HOH B O   1 
HETATM 13633 O  O   . HOH ZA 4 .   ? 6.023   105.088 45.763  1.00 32.28 ? 382 HOH B O   1 
HETATM 13634 O  O   . HOH ZA 4 .   ? 34.939  102.447 23.690  1.00 27.37 ? 383 HOH B O   1 
HETATM 13635 O  O   . HOH ZA 4 .   ? 39.768  97.194  32.407  1.00 19.44 ? 384 HOH B O   1 
HETATM 13636 O  O   . HOH ZA 4 .   ? 24.583  93.006  44.377  1.00 24.84 ? 385 HOH B O   1 
HETATM 13637 O  O   . HOH ZA 4 .   ? 37.168  95.416  24.226  1.00 27.20 ? 386 HOH B O   1 
HETATM 13638 O  O   . HOH ZA 4 .   ? 20.535  101.155 17.557  1.00 22.77 ? 387 HOH B O   1 
HETATM 13639 O  O   . HOH ZA 4 .   ? 34.622  99.854  40.095  1.00 17.37 ? 388 HOH B O   1 
HETATM 13640 O  O   . HOH ZA 4 .   ? 30.307  112.001 28.596  1.00 20.47 ? 389 HOH B O   1 
HETATM 13641 O  O   . HOH ZA 4 .   ? 28.983  100.863 17.111  1.00 28.63 ? 390 HOH B O   1 
HETATM 13642 O  O   . HOH ZA 4 .   ? 8.922   93.188  42.885  1.00 31.04 ? 391 HOH B O   1 
HETATM 13643 O  O   . HOH ZA 4 .   ? 28.848  112.760 39.888  1.00 29.74 ? 392 HOH B O   1 
HETATM 13644 O  O   . HOH ZA 4 .   ? 26.368  123.270 35.627  1.00 27.53 ? 393 HOH B O   1 
HETATM 13645 O  O   . HOH ZA 4 .   ? 26.558  93.203  23.898  1.00 25.84 ? 394 HOH B O   1 
HETATM 13646 O  O   . HOH ZA 4 .   ? 26.282  112.873 41.724  1.00 30.71 ? 395 HOH B O   1 
HETATM 13647 O  O   . HOH ZA 4 .   ? 26.114  90.340  48.252  1.00 28.65 ? 396 HOH B O   1 
HETATM 13648 O  O   . HOH ZA 4 .   ? 36.539  90.000  27.126  1.00 23.58 ? 397 HOH B O   1 
HETATM 13649 O  O   . HOH ZA 4 .   ? 22.729  123.464 32.728  1.00 22.44 ? 398 HOH B O   1 
HETATM 13650 O  O   . HOH ZA 4 .   ? 7.921   103.622 16.222  1.00 36.50 ? 399 HOH B O   1 
HETATM 13651 O  O   . HOH ZA 4 .   ? 11.766  92.777  30.473  1.00 29.54 ? 400 HOH B O   1 
HETATM 13652 O  O   . HOH ZA 4 .   ? 39.829  90.983  38.070  1.00 28.43 ? 401 HOH B O   1 
HETATM 13653 O  O   . HOH ZA 4 .   ? 40.086  103.417 22.844  1.00 27.51 ? 402 HOH B O   1 
HETATM 13654 O  O   . HOH ZA 4 .   ? 6.494   102.142 29.748  1.00 27.99 ? 403 HOH B O   1 
HETATM 13655 O  O   . HOH ZA 4 .   ? 31.717  98.991  20.376  1.00 24.92 ? 404 HOH B O   1 
HETATM 13656 O  O   . HOH ZA 4 .   ? 36.305  101.636 43.559  1.00 26.35 ? 405 HOH B O   1 
HETATM 13657 O  O   . HOH ZA 4 .   ? 5.057   96.305  44.299  1.00 33.07 ? 406 HOH B O   1 
HETATM 13658 O  O   . HOH ZA 4 .   ? 15.277  109.462 41.198  1.00 29.24 ? 407 HOH B O   1 
HETATM 13659 O  O   . HOH ZA 4 .   ? 5.210   112.056 39.653  1.00 39.62 ? 408 HOH B O   1 
HETATM 13660 O  O   . HOH ZA 4 .   ? 25.053  109.565 45.879  1.00 40.54 ? 409 HOH B O   1 
HETATM 13661 O  O   . HOH ZA 4 .   ? 11.590  97.767  44.679  1.00 26.81 ? 410 HOH B O   1 
HETATM 13662 O  O   . HOH ZA 4 .   ? 19.680  108.840 51.224  1.00 34.50 ? 411 HOH B O   1 
HETATM 13663 O  O   . HOH ZA 4 .   ? 40.810  105.412 24.201  1.00 29.33 ? 412 HOH B O   1 
HETATM 13664 O  O   . HOH ZA 4 .   ? 25.335  104.529 49.377  1.00 31.02 ? 413 HOH B O   1 
HETATM 13665 O  O   . HOH ZA 4 .   ? 32.014  118.817 30.467  1.00 27.97 ? 414 HOH B O   1 
HETATM 13666 O  O   . HOH ZA 4 .   ? 11.674  90.998  22.059  1.00 30.27 ? 415 HOH B O   1 
HETATM 13667 O  O   . HOH ZA 4 .   ? 25.869  96.437  17.708  1.00 35.74 ? 416 HOH B O   1 
HETATM 13668 O  O   . HOH ZA 4 .   ? 12.684  95.817  20.139  1.00 23.76 ? 417 HOH B O   1 
HETATM 13669 O  O   . HOH ZA 4 .   ? 15.766  106.341 15.065  1.00 15.26 ? 418 HOH B O   1 
HETATM 13670 O  O   . HOH ZA 4 .   ? 19.513  93.406  23.898  1.00 21.59 ? 419 HOH B O   1 
HETATM 13671 O  O   . HOH ZA 4 .   ? 38.870  112.415 30.461  1.00 33.11 ? 420 HOH B O   1 
HETATM 13672 O  O   . HOH ZA 4 .   ? 11.027  91.765  26.494  1.00 31.07 ? 421 HOH B O   1 
HETATM 13673 O  O   . HOH ZA 4 .   ? 38.230  111.061 27.985  1.00 30.53 ? 422 HOH B O   1 
HETATM 13674 O  O   . HOH ZA 4 .   ? 20.103  90.363  30.108  1.00 26.13 ? 423 HOH B O   1 
HETATM 13675 O  O   . HOH ZA 4 .   ? 3.121   99.968  18.541  1.00 34.93 ? 424 HOH B O   1 
HETATM 13676 O  O   . HOH ZA 4 .   ? 26.955  107.228 45.604  1.00 28.50 ? 425 HOH B O   1 
HETATM 13677 O  O   . HOH ZA 4 .   ? 25.981  100.806 14.977  1.00 37.42 ? 426 HOH B O   1 
HETATM 13678 O  O   . HOH ZA 4 .   ? 33.608  104.490 22.676  1.00 22.91 ? 427 HOH B O   1 
HETATM 13679 O  O   . HOH ZA 4 .   ? 17.210  97.661  11.947  1.00 38.89 ? 428 HOH B O   1 
HETATM 13680 O  O   . HOH ZA 4 .   ? 14.410  91.240  30.598  1.00 27.95 ? 429 HOH B O   1 
HETATM 13681 O  O   . HOH ZA 4 .   ? 35.243  86.198  33.094  1.00 24.14 ? 430 HOH B O   1 
HETATM 13682 O  O   . HOH ZA 4 .   ? 16.945  92.305  30.535  1.00 20.96 ? 431 HOH B O   1 
HETATM 13683 O  O   . HOH ZA 4 .   ? 36.502  107.681 25.022  1.00 26.24 ? 432 HOH B O   1 
HETATM 13684 O  O   . HOH ZA 4 .   ? 22.362  103.908 12.816  1.00 30.75 ? 433 HOH B O   1 
HETATM 13685 O  O   . HOH ZA 4 .   ? 4.423   95.616  19.872  1.00 34.88 ? 434 HOH B O   1 
HETATM 13686 O  O   . HOH ZA 4 .   ? 6.059   97.651  30.803  1.00 25.45 ? 435 HOH B O   1 
HETATM 13687 O  O   . HOH ZA 4 .   ? 11.729  117.200 37.474  1.00 31.74 ? 436 HOH B O   1 
HETATM 13688 O  O   . HOH ZA 4 .   ? 4.845   106.555 22.497  1.00 29.16 ? 437 HOH B O   1 
HETATM 13689 O  O   . HOH ZA 4 .   ? 6.691   98.144  26.406  1.00 29.82 ? 438 HOH B O   1 
HETATM 13690 O  O   . HOH ZA 4 .   ? 5.572   103.274 27.321  1.00 35.55 ? 439 HOH B O   1 
HETATM 13691 O  O   . HOH ZA 4 .   ? 23.091  102.349 15.337  1.00 33.88 ? 440 HOH B O   1 
HETATM 13692 O  O   . HOH ZA 4 .   ? 17.699  117.070 40.824  1.00 35.66 ? 441 HOH B O   1 
HETATM 13693 O  O   . HOH ZA 4 .   ? 5.425   101.174 16.366  1.00 37.25 ? 442 HOH B O   1 
HETATM 13694 O  O   . HOH ZA 4 .   ? 32.676  96.297  20.768  1.00 35.89 ? 443 HOH B O   1 
HETATM 13695 O  O   . HOH ZA 4 .   ? 14.152  88.528  47.395  1.00 29.47 ? 444 HOH B O   1 
HETATM 13696 O  O   . HOH ZA 4 .   ? 9.791   90.989  39.984  1.00 31.18 ? 445 HOH B O   1 
HETATM 13697 O  O   . HOH ZA 4 .   ? 4.655   99.484  42.070  1.00 26.98 ? 446 HOH B O   1 
HETATM 13698 O  O   . HOH ZA 4 .   ? 11.072  109.949 19.437  1.00 28.16 ? 447 HOH B O   1 
HETATM 13699 O  O   . HOH ZA 4 .   ? 22.826  110.014 6.549   1.00 35.41 ? 448 HOH B O   1 
HETATM 13700 O  O   . HOH ZA 4 .   ? 5.472   112.516 25.192  1.00 31.50 ? 449 HOH B O   1 
HETATM 13701 O  O   . HOH ZA 4 .   ? 25.689  113.632 30.508  1.00 17.30 ? 450 HOH B O   1 
HETATM 13702 O  O   . HOH ZA 4 .   ? 12.783  112.109 36.639  1.00 20.14 ? 451 HOH B O   1 
HETATM 13703 O  O   . HOH ZA 4 .   ? 32.432  88.588  36.228  1.00 23.00 ? 452 HOH B O   1 
HETATM 13704 O  O   . HOH ZA 4 .   ? 9.337   102.292 17.458  1.00 31.72 ? 453 HOH B O   1 
HETATM 13705 O  O   . HOH ZA 4 .   ? 25.809  114.517 32.762  1.00 23.60 ? 454 HOH B O   1 
HETATM 13706 O  O   . HOH ZA 4 .   ? 13.153  111.169 41.850  1.00 34.05 ? 455 HOH B O   1 
HETATM 13707 O  O   . HOH AB 4 .   ? -3.986  83.298  85.793  1.00 33.65 ? 301 HOH C O   1 
HETATM 13708 O  O   . HOH AB 4 .   ? -3.262  102.204 85.931  1.00 43.76 ? 302 HOH C O   1 
HETATM 13709 O  O   . HOH AB 4 .   ? 5.435   93.818  97.526  1.00 47.95 ? 303 HOH C O   1 
HETATM 13710 O  O   . HOH AB 4 .   ? -5.137  94.404  78.873  1.00 39.16 ? 304 HOH C O   1 
HETATM 13711 O  O   . HOH AB 4 .   ? 4.442   80.886  75.231  1.00 33.30 ? 305 HOH C O   1 
HETATM 13712 O  O   . HOH AB 4 .   ? -4.310  88.950  85.906  1.00 35.81 ? 306 HOH C O   1 
HETATM 13713 O  O   . HOH AB 4 .   ? -3.236  77.472  81.140  1.00 44.50 ? 307 HOH C O   1 
HETATM 13714 O  O   . HOH AB 4 .   ? -1.499  82.055  86.672  1.00 35.57 ? 308 HOH C O   1 
HETATM 13715 O  O   . HOH AB 4 .   ? 13.783  99.812  74.456  1.00 31.97 ? 309 HOH C O   1 
HETATM 13716 O  O   . HOH AB 4 .   ? 3.932   83.487  76.168  1.00 30.94 ? 310 HOH C O   1 
HETATM 13717 O  O   . HOH AB 4 .   ? -2.219  95.114  82.804  1.00 40.56 ? 311 HOH C O   1 
HETATM 13718 O  O   . HOH AB 4 .   ? 9.925   106.225 74.339  1.00 43.96 ? 312 HOH C O   1 
HETATM 13719 O  O   . HOH AB 4 .   ? -2.783  84.435  79.489  1.00 36.26 ? 313 HOH C O   1 
HETATM 13720 O  O   . HOH AB 4 .   ? 8.195   91.622  97.157  1.00 47.87 ? 314 HOH C O   1 
HETATM 13721 O  O   . HOH AB 4 .   ? 12.567  80.276  83.922  1.00 46.41 ? 315 HOH C O   1 
HETATM 13722 O  O   . HOH AB 4 .   ? 19.431  103.706 85.470  1.00 49.10 ? 316 HOH C O   1 
HETATM 13723 O  O   . HOH AB 4 .   ? 10.596  109.500 88.291  1.00 45.48 ? 317 HOH C O   1 
HETATM 13724 O  O   . HOH AB 4 .   ? -7.216  82.111  79.085  1.00 38.77 ? 318 HOH C O   1 
HETATM 13725 O  O   . HOH AB 4 .   ? 15.661  94.688  78.256  1.00 28.54 ? 319 HOH C O   1 
HETATM 13726 O  O   . HOH AB 4 .   ? 0.245   89.208  74.886  1.00 33.19 ? 320 HOH C O   1 
HETATM 13727 O  O   . HOH AB 4 .   ? 18.517  93.502  78.996  1.00 35.87 ? 321 HOH C O   1 
HETATM 13728 O  O   . HOH BB 4 .   ? 12.663  90.212  49.652  1.00 13.62 ? 301 HOH D O   1 
HETATM 13729 O  O   . HOH BB 4 .   ? 16.506  78.209  48.432  1.00 9.61  ? 302 HOH D O   1 
HETATM 13730 O  O   . HOH BB 4 .   ? 14.642  87.984  55.489  1.00 13.83 ? 303 HOH D O   1 
HETATM 13731 O  O   . HOH BB 4 .   ? 22.165  73.652  54.991  1.00 14.26 ? 304 HOH D O   1 
HETATM 13732 O  O   . HOH BB 4 .   ? 21.697  92.683  48.018  1.00 21.08 ? 305 HOH D O   1 
HETATM 13733 O  O   . HOH BB 4 .   ? 4.569   84.562  57.548  1.00 19.01 ? 306 HOH D O   1 
HETATM 13734 O  O   . HOH BB 4 .   ? 20.427  81.940  44.613  1.00 16.76 ? 307 HOH D O   1 
HETATM 13735 O  O   . HOH BB 4 .   ? 4.879   83.336  59.903  1.00 18.43 ? 308 HOH D O   1 
HETATM 13736 O  O   . HOH BB 4 .   ? 9.547   95.409  53.674  1.00 19.32 ? 309 HOH D O   1 
HETATM 13737 O  O   . HOH BB 4 .   ? 15.647  94.783  54.257  1.00 19.37 ? 310 HOH D O   1 
HETATM 13738 O  O   . HOH BB 4 .   ? 24.837  73.639  53.376  1.00 18.75 ? 311 HOH D O   1 
HETATM 13739 O  O   . HOH BB 4 .   ? 5.532   82.798  70.768  1.00 31.77 ? 312 HOH D O   1 
HETATM 13740 O  O   . HOH BB 4 .   ? 6.663   83.490  47.859  1.00 24.90 ? 313 HOH D O   1 
HETATM 13741 O  O   . HOH BB 4 .   ? 14.652  100.324 52.426  1.00 20.18 ? 314 HOH D O   1 
HETATM 13742 O  O   . HOH BB 4 .   ? 22.141  84.769  47.019  1.00 25.46 ? 315 HOH D O   1 
HETATM 13743 O  O   . HOH BB 4 .   ? 13.813  86.005  48.037  1.00 15.39 ? 316 HOH D O   1 
HETATM 13744 O  O   . HOH BB 4 .   ? 31.963  86.575  59.641  1.00 34.92 ? 317 HOH D O   1 
HETATM 13745 O  O   . HOH BB 4 .   ? 10.660  81.962  50.311  1.00 29.63 ? 318 HOH D O   1 
HETATM 13746 O  O   . HOH BB 4 .   ? 0.902   95.740  59.432  1.00 27.48 ? 319 HOH D O   1 
HETATM 13747 O  O   . HOH BB 4 .   ? 16.117  81.535  43.706  1.00 21.08 ? 320 HOH D O   1 
HETATM 13748 O  O   . HOH BB 4 .   ? 23.493  94.880  48.685  1.00 17.59 ? 321 HOH D O   1 
HETATM 13749 O  O   . HOH BB 4 .   ? 12.946  82.912  48.415  1.00 26.56 ? 322 HOH D O   1 
HETATM 13750 O  O   . HOH BB 4 .   ? 0.551   102.220 59.428  1.00 29.76 ? 323 HOH D O   1 
HETATM 13751 O  O   . HOH BB 4 .   ? 20.376  92.455  74.667  1.00 28.86 ? 324 HOH D O   1 
HETATM 13752 O  O   . HOH BB 4 .   ? -1.264  91.240  63.343  1.00 29.36 ? 325 HOH D O   1 
HETATM 13753 O  O   . HOH BB 4 .   ? 11.131  77.474  58.216  1.00 21.86 ? 326 HOH D O   1 
HETATM 13754 O  O   . HOH BB 4 .   ? 5.826   86.257  46.272  1.00 25.66 ? 327 HOH D O   1 
HETATM 13755 O  O   . HOH BB 4 .   ? 3.623   87.287  53.862  1.00 29.61 ? 328 HOH D O   1 
HETATM 13756 O  O   . HOH BB 4 .   ? 15.812  77.751  45.953  1.00 22.38 ? 329 HOH D O   1 
HETATM 13757 O  O   . HOH BB 4 .   ? 28.847  92.718  68.886  1.00 28.21 ? 330 HOH D O   1 
HETATM 13758 O  O   . HOH BB 4 .   ? 24.694  95.135  46.314  1.00 22.79 ? 331 HOH D O   1 
HETATM 13759 O  O   . HOH BB 4 .   ? 6.977   81.882  65.687  1.00 20.20 ? 332 HOH D O   1 
HETATM 13760 O  O   . HOH BB 4 .   ? 23.257  97.135  49.957  1.00 21.78 ? 333 HOH D O   1 
HETATM 13761 O  O   . HOH BB 4 .   ? 23.221  102.347 55.947  1.00 27.28 ? 334 HOH D O   1 
HETATM 13762 O  O   . HOH BB 4 .   ? 15.383  96.974  73.695  1.00 28.72 ? 335 HOH D O   1 
HETATM 13763 O  O   . HOH BB 4 .   ? 14.436  79.303  45.217  1.00 21.98 ? 336 HOH D O   1 
HETATM 13764 O  O   . HOH BB 4 .   ? 2.151   88.271  68.276  1.00 22.92 ? 337 HOH D O   1 
HETATM 13765 O  O   . HOH BB 4 .   ? 16.853  106.969 66.776  1.00 32.27 ? 338 HOH D O   1 
HETATM 13766 O  O   . HOH BB 4 .   ? 0.508   85.424  66.962  1.00 31.02 ? 339 HOH D O   1 
HETATM 13767 O  O   . HOH BB 4 .   ? 23.887  87.989  49.939  1.00 31.87 ? 340 HOH D O   1 
HETATM 13768 O  O   . HOH BB 4 .   ? 20.984  88.447  50.038  1.00 17.80 ? 341 HOH D O   1 
HETATM 13769 O  O   . HOH BB 4 .   ? 15.775  85.668  41.469  1.00 25.26 ? 342 HOH D O   1 
HETATM 13770 O  O   . HOH BB 4 .   ? 18.075  79.795  43.714  1.00 21.78 ? 343 HOH D O   1 
HETATM 13771 O  O   . HOH BB 4 .   ? 12.784  95.096  50.230  1.00 22.99 ? 344 HOH D O   1 
HETATM 13772 O  O   . HOH BB 4 .   ? 5.921   94.267  53.425  1.00 25.79 ? 345 HOH D O   1 
HETATM 13773 O  O   . HOH BB 4 .   ? 10.723  104.647 68.619  1.00 30.79 ? 346 HOH D O   1 
HETATM 13774 O  O   . HOH BB 4 .   ? 31.261  93.891  64.158  1.00 27.93 ? 347 HOH D O   1 
HETATM 13775 O  O   . HOH BB 4 .   ? 31.086  91.708  65.766  1.00 27.35 ? 348 HOH D O   1 
HETATM 13776 O  O   . HOH BB 4 .   ? 8.880   81.804  47.290  1.00 27.24 ? 349 HOH D O   1 
HETATM 13777 O  O   . HOH BB 4 .   ? 24.918  84.530  53.413  1.00 23.87 ? 350 HOH D O   1 
HETATM 13778 O  O   . HOH BB 4 .   ? 3.158   81.449  51.065  1.00 28.59 ? 351 HOH D O   1 
HETATM 13779 O  O   . HOH BB 4 .   ? 14.209  80.147  61.691  1.00 23.67 ? 352 HOH D O   1 
HETATM 13780 O  O   . HOH BB 4 .   ? -2.331  94.375  62.461  1.00 32.87 ? 353 HOH D O   1 
HETATM 13781 O  O   . HOH BB 4 .   ? 23.785  87.003  47.009  1.00 27.22 ? 354 HOH D O   1 
HETATM 13782 O  O   . HOH BB 4 .   ? 15.477  72.765  62.367  1.00 36.55 ? 355 HOH D O   1 
HETATM 13783 O  O   . HOH BB 4 .   ? 4.554   81.925  67.179  1.00 27.50 ? 356 HOH D O   1 
HETATM 13784 O  O   . HOH BB 4 .   ? 12.700  79.635  48.042  1.00 29.35 ? 357 HOH D O   1 
HETATM 13785 O  O   . HOH BB 4 .   ? 37.778  100.009 49.449  1.00 40.31 ? 358 HOH D O   1 
HETATM 13786 O  O   . HOH BB 4 .   ? 6.871   111.704 69.829  1.00 46.53 ? 359 HOH D O   1 
HETATM 13787 O  O   . HOH BB 4 .   ? 9.819   108.305 77.048  1.00 44.82 ? 360 HOH D O   1 
HETATM 13788 O  O   . HOH BB 4 .   ? 22.630  80.488  59.691  1.00 32.77 ? 361 HOH D O   1 
HETATM 13789 O  O   . HOH BB 4 .   ? 18.560  95.891  74.755  1.00 30.27 ? 362 HOH D O   1 
HETATM 13790 O  O   . HOH BB 4 .   ? 0.860   80.451  65.519  1.00 26.94 ? 363 HOH D O   1 
HETATM 13791 O  O   . HOH BB 4 .   ? 8.913   87.273  45.258  1.00 29.75 ? 364 HOH D O   1 
HETATM 13792 O  O   . HOH BB 4 .   ? 24.948  104.556 56.177  1.00 36.96 ? 365 HOH D O   1 
HETATM 13793 O  O   . HOH BB 4 .   ? -1.298  100.294 69.713  1.00 39.78 ? 366 HOH D O   1 
HETATM 13794 O  O   . HOH BB 4 .   ? 5.597   76.047  53.552  1.00 35.78 ? 367 HOH D O   1 
HETATM 13795 O  O   . HOH BB 4 .   ? 14.374  96.089  52.250  1.00 19.68 ? 368 HOH D O   1 
HETATM 13796 O  O   . HOH BB 4 .   ? 5.632   113.815 70.723  1.00 46.40 ? 369 HOH D O   1 
HETATM 13797 O  O   . HOH BB 4 .   ? 16.331  94.810  75.382  1.00 29.83 ? 370 HOH D O   1 
HETATM 13798 O  O   . HOH BB 4 .   ? 3.036   86.512  56.137  1.00 28.51 ? 371 HOH D O   1 
HETATM 13799 O  O   . HOH BB 4 .   ? 33.703  98.524  60.842  1.00 40.33 ? 372 HOH D O   1 
HETATM 13800 O  O   . HOH BB 4 .   ? 34.025  93.409  63.721  1.00 39.23 ? 373 HOH D O   1 
HETATM 13801 O  O   . HOH BB 4 .   ? 19.045  91.674  50.202  1.00 21.41 ? 374 HOH D O   1 
HETATM 13802 O  O   . HOH BB 4 .   ? 22.901  89.136  45.329  1.00 31.72 ? 375 HOH D O   1 
HETATM 13803 O  O   . HOH BB 4 .   ? 3.197   78.981  65.946  1.00 39.48 ? 376 HOH D O   1 
HETATM 13804 O  O   . HOH BB 4 .   ? 19.357  69.311  59.912  1.00 32.37 ? 377 HOH D O   1 
HETATM 13805 O  O   . HOH BB 4 .   ? 28.457  98.804  51.766  1.00 31.81 ? 378 HOH D O   1 
HETATM 13806 O  O   . HOH BB 4 .   ? 26.729  95.580  72.458  1.00 35.13 ? 379 HOH D O   1 
HETATM 13807 O  O   . HOH BB 4 .   ? 2.100   83.102  67.758  1.00 29.93 ? 380 HOH D O   1 
HETATM 13808 O  O   . HOH BB 4 .   ? 17.656  92.386  75.491  1.00 39.39 ? 381 HOH D O   1 
HETATM 13809 O  O   . HOH BB 4 .   ? 20.211  86.356  47.934  1.00 22.93 ? 382 HOH D O   1 
HETATM 13810 O  O   . HOH BB 4 .   ? 5.587   78.090  63.439  1.00 29.86 ? 383 HOH D O   1 
HETATM 13811 O  O   . HOH BB 4 .   ? 5.161   97.720  53.475  1.00 30.14 ? 384 HOH D O   1 
HETATM 13812 O  O   . HOH BB 4 .   ? 27.846  88.192  54.015  1.00 27.10 ? 385 HOH D O   1 
HETATM 13813 O  O   . HOH BB 4 .   ? -4.543  93.504  64.549  1.00 39.63 ? 386 HOH D O   1 
HETATM 13814 O  O   . HOH BB 4 .   ? 17.077  88.545  73.696  1.00 26.49 ? 387 HOH D O   1 
HETATM 13815 O  O   . HOH BB 4 .   ? 5.240   89.454  51.945  1.00 27.26 ? 388 HOH D O   1 
HETATM 13816 O  O   . HOH BB 4 .   ? 16.927  79.232  67.452  1.00 34.62 ? 389 HOH D O   1 
HETATM 13817 O  O   . HOH BB 4 .   ? 11.609  96.884  52.898  1.00 28.77 ? 390 HOH D O   1 
HETATM 13818 O  O   . HOH BB 4 .   ? 16.265  90.804  73.384  1.00 36.74 ? 391 HOH D O   1 
HETATM 13819 O  O   . HOH BB 4 .   ? 5.444   91.990  51.413  1.00 32.95 ? 392 HOH D O   1 
HETATM 13820 O  O   . HOH BB 4 .   ? 9.660   77.670  62.690  1.00 34.28 ? 393 HOH D O   1 
HETATM 13821 O  O   . HOH CB 4 .   ? 24.783  62.721  20.237  1.00 40.47 ? 301 HOH E O   1 
HETATM 13822 O  O   . HOH CB 4 .   ? 22.361  56.910  39.982  1.00 23.28 ? 302 HOH E O   1 
HETATM 13823 O  O   . HOH CB 4 .   ? 19.405  28.247  41.543  1.00 22.20 ? 303 HOH E O   1 
HETATM 13824 O  O   . HOH CB 4 .   ? 11.700  45.804  41.727  1.00 36.23 ? 304 HOH E O   1 
HETATM 13825 O  O   . HOH CB 4 .   ? 17.285  52.835  44.027  1.00 29.35 ? 305 HOH E O   1 
HETATM 13826 O  O   . HOH CB 4 .   ? 6.510   48.639  15.877  1.00 47.38 ? 306 HOH E O   1 
HETATM 13827 O  O   . HOH CB 4 .   ? 22.301  29.068  40.716  1.00 36.19 ? 307 HOH E O   1 
HETATM 13828 O  O   . HOH CB 4 .   ? 9.110   58.398  16.415  1.00 44.25 ? 308 HOH E O   1 
HETATM 13829 O  O   . HOH CB 4 .   ? 16.219  26.314  33.485  1.00 39.60 ? 309 HOH E O   1 
HETATM 13830 O  O   . HOH CB 4 .   ? 21.978  67.946  19.561  1.00 36.00 ? 310 HOH E O   1 
HETATM 13831 O  O   . HOH CB 4 .   ? 12.329  36.715  36.924  1.00 32.01 ? 311 HOH E O   1 
HETATM 13832 O  O   . HOH CB 4 .   ? 12.029  59.505  25.793  1.00 28.03 ? 312 HOH E O   1 
HETATM 13833 O  O   . HOH CB 4 .   ? 10.065  48.392  26.445  1.00 35.60 ? 313 HOH E O   1 
HETATM 13834 O  O   . HOH CB 4 .   ? 26.586  44.548  42.275  1.00 40.40 ? 314 HOH E O   1 
HETATM 13835 O  O   . HOH CB 4 .   ? 26.597  56.886  31.757  1.00 34.38 ? 315 HOH E O   1 
HETATM 13836 O  O   . HOH CB 4 .   ? 11.976  48.588  20.099  1.00 36.73 ? 316 HOH E O   1 
HETATM 13837 O  O   . HOH CB 4 .   ? 25.068  34.093  24.018  1.00 40.88 ? 317 HOH E O   1 
HETATM 13838 O  O   . HOH CB 4 .   ? 19.457  37.715  28.175  1.00 38.46 ? 318 HOH E O   1 
HETATM 13839 O  O   . HOH CB 4 .   ? 18.988  54.120  14.189  1.00 46.12 ? 319 HOH E O   1 
HETATM 13840 O  O   . HOH CB 4 .   ? 4.568   47.154  35.571  1.00 36.01 ? 320 HOH E O   1 
HETATM 13841 O  O   . HOH CB 4 .   ? 11.772  45.978  36.561  1.00 29.78 ? 321 HOH E O   1 
HETATM 13842 O  O   . HOH CB 4 .   ? 16.315  39.603  37.895  1.00 26.37 ? 322 HOH E O   1 
HETATM 13843 O  O   . HOH CB 4 .   ? 24.025  45.320  13.966  1.00 40.21 ? 323 HOH E O   1 
HETATM 13844 O  O   . HOH CB 4 .   ? 18.793  40.731  16.853  1.00 40.38 ? 324 HOH E O   1 
HETATM 13845 O  O   . HOH CB 4 .   ? 33.561  34.179  29.676  1.00 49.81 ? 325 HOH E O   1 
HETATM 13846 O  O   . HOH CB 4 .   ? 11.486  36.792  41.506  1.00 40.18 ? 326 HOH E O   1 
HETATM 13847 O  O   . HOH CB 4 .   ? 37.635  49.244  24.373  1.00 49.61 ? 327 HOH E O   1 
HETATM 13848 O  O   . HOH CB 4 .   ? 41.548  43.118  28.298  1.00 47.67 ? 328 HOH E O   1 
HETATM 13849 O  O   . HOH CB 4 .   ? 2.757   42.366  35.844  1.00 35.09 ? 329 HOH E O   1 
HETATM 13850 O  O   . HOH CB 4 .   ? 21.026  32.208  44.267  1.00 27.04 ? 330 HOH E O   1 
HETATM 13851 O  O   . HOH CB 4 .   ? 19.481  55.505  46.664  1.00 29.67 ? 331 HOH E O   1 
HETATM 13852 O  O   . HOH CB 4 .   ? 11.492  40.365  38.434  1.00 28.97 ? 332 HOH E O   1 
HETATM 13853 O  O   . HOH CB 4 .   ? 23.136  37.098  35.754  1.00 37.77 ? 333 HOH E O   1 
HETATM 13854 O  O   . HOH CB 4 .   ? 23.701  37.598  22.903  1.00 33.46 ? 334 HOH E O   1 
HETATM 13855 O  O   . HOH CB 4 .   ? 25.829  34.888  38.956  1.00 34.24 ? 335 HOH E O   1 
HETATM 13856 O  O   . HOH CB 4 .   ? 8.954   40.939  29.069  1.00 40.87 ? 336 HOH E O   1 
HETATM 13857 O  O   . HOH CB 4 .   ? 19.387  35.121  22.592  1.00 34.73 ? 337 HOH E O   1 
HETATM 13858 O  O   . HOH DB 4 .   ? 23.424  81.100  50.315  1.00 16.49 ? 301 HOH F O   1 
HETATM 13859 O  O   . HOH DB 4 .   ? 15.810  86.826  35.604  1.00 16.05 ? 302 HOH F O   1 
HETATM 13860 O  O   . HOH DB 4 .   ? 18.927  78.877  37.636  1.00 16.61 ? 303 HOH F O   1 
HETATM 13861 O  O   . HOH DB 4 .   ? 33.917  74.902  45.332  1.00 31.58 ? 304 HOH F O   1 
HETATM 13862 O  O   . HOH DB 4 .   ? 19.495  93.600  37.107  1.00 17.44 ? 305 HOH F O   1 
HETATM 13863 O  O   . HOH DB 4 .   ? 14.683  82.395  41.457  1.00 19.67 ? 306 HOH F O   1 
HETATM 13864 O  O   . HOH DB 4 .   ? 8.894   76.048  41.138  1.00 21.87 ? 307 HOH F O   1 
HETATM 13865 O  O   . HOH DB 4 .   ? 9.840   85.784  34.802  1.00 26.31 ? 308 HOH F O   1 
HETATM 13866 O  O   . HOH DB 4 .   ? 6.836   65.450  46.229  1.00 30.97 ? 309 HOH F O   1 
HETATM 13867 O  O   . HOH DB 4 .   ? 8.095   85.630  37.220  1.00 30.58 ? 310 HOH F O   1 
HETATM 13868 O  O   . HOH DB 4 .   ? 21.514  92.453  39.131  1.00 18.88 ? 311 HOH F O   1 
HETATM 13869 O  O   . HOH DB 4 .   ? 17.253  92.259  37.322  1.00 16.45 ? 312 HOH F O   1 
HETATM 13870 O  O   . HOH DB 4 .   ? 28.664  84.427  39.273  1.00 27.83 ? 313 HOH F O   1 
HETATM 13871 O  O   . HOH DB 4 .   ? 20.137  57.884  47.817  1.00 23.62 ? 314 HOH F O   1 
HETATM 13872 O  O   . HOH DB 4 .   ? 16.108  70.278  22.168  1.00 30.31 ? 315 HOH F O   1 
HETATM 13873 O  O   . HOH DB 4 .   ? 33.639  73.648  33.302  1.00 30.58 ? 316 HOH F O   1 
HETATM 13874 O  O   . HOH DB 4 .   ? 21.503  87.490  41.060  1.00 22.72 ? 317 HOH F O   1 
HETATM 13875 O  O   . HOH DB 4 .   ? 12.295  75.677  42.911  1.00 17.53 ? 318 HOH F O   1 
HETATM 13876 O  O   . HOH DB 4 .   ? 13.263  75.573  46.336  1.00 18.18 ? 319 HOH F O   1 
HETATM 13877 O  O   . HOH DB 4 .   ? 18.091  76.869  44.050  1.00 18.73 ? 320 HOH F O   1 
HETATM 13878 O  O   . HOH DB 4 .   ? 25.290  72.493  55.632  1.00 20.84 ? 321 HOH F O   1 
HETATM 13879 O  O   . HOH DB 4 .   ? 10.993  76.885  30.675  1.00 31.04 ? 322 HOH F O   1 
HETATM 13880 O  O   . HOH DB 4 .   ? 26.612  76.236  27.712  1.00 35.86 ? 323 HOH F O   1 
HETATM 13881 O  O   . HOH DB 4 .   ? 16.956  58.900  45.920  1.00 23.09 ? 324 HOH F O   1 
HETATM 13882 O  O   . HOH DB 4 .   ? 33.558  82.366  34.413  1.00 33.93 ? 325 HOH F O   1 
HETATM 13883 O  O   . HOH DB 4 .   ? 8.758   76.824  32.013  1.00 38.64 ? 326 HOH F O   1 
HETATM 13884 O  O   . HOH DB 4 .   ? 11.513  60.039  31.182  1.00 33.66 ? 327 HOH F O   1 
HETATM 13885 O  O   . HOH DB 4 .   ? 30.298  85.240  41.001  1.00 28.38 ? 328 HOH F O   1 
HETATM 13886 O  O   . HOH DB 4 .   ? 30.210  82.450  42.891  1.00 31.66 ? 329 HOH F O   1 
HETATM 13887 O  O   . HOH DB 4 .   ? 16.552  89.411  34.287  1.00 23.98 ? 330 HOH F O   1 
HETATM 13888 O  O   . HOH DB 4 .   ? 13.824  59.908  46.257  1.00 23.28 ? 331 HOH F O   1 
HETATM 13889 O  O   . HOH DB 4 .   ? 8.063   78.643  34.517  1.00 33.50 ? 332 HOH F O   1 
HETATM 13890 O  O   . HOH DB 4 .   ? 29.220  77.079  57.740  1.00 32.01 ? 333 HOH F O   1 
HETATM 13891 O  O   . HOH DB 4 .   ? 20.705  60.579  50.286  1.00 26.96 ? 334 HOH F O   1 
HETATM 13892 O  O   . HOH DB 4 .   ? 22.217  71.601  57.173  1.00 29.25 ? 335 HOH F O   1 
HETATM 13893 O  O   . HOH DB 4 .   ? -1.048  67.523  40.646  1.00 36.49 ? 336 HOH F O   1 
HETATM 13894 O  O   . HOH DB 4 .   ? 8.533   79.231  37.380  1.00 29.90 ? 337 HOH F O   1 
HETATM 13895 O  O   . HOH DB 4 .   ? 10.222  86.914  38.254  1.00 36.92 ? 338 HOH F O   1 
HETATM 13896 O  O   . HOH DB 4 .   ? 22.120  66.554  53.183  1.00 27.40 ? 339 HOH F O   1 
HETATM 13897 O  O   . HOH DB 4 .   ? 19.495  68.132  52.810  1.00 27.86 ? 340 HOH F O   1 
HETATM 13898 O  O   . HOH DB 4 .   ? 16.641  91.616  35.297  1.00 23.16 ? 341 HOH F O   1 
HETATM 13899 O  O   . HOH DB 4 .   ? 18.690  92.390  33.353  1.00 24.58 ? 342 HOH F O   1 
HETATM 13900 O  O   . HOH DB 4 .   ? 23.017  85.048  42.215  1.00 22.12 ? 343 HOH F O   1 
HETATM 13901 O  O   . HOH DB 4 .   ? 6.376   69.274  37.943  1.00 28.62 ? 344 HOH F O   1 
HETATM 13902 O  O   . HOH DB 4 .   ? 23.590  89.293  41.194  1.00 27.37 ? 345 HOH F O   1 
HETATM 13903 O  O   . HOH DB 4 .   ? 21.858  76.976  28.200  1.00 34.13 ? 346 HOH F O   1 
HETATM 13904 O  O   . HOH DB 4 .   ? 7.611   73.890  43.966  1.00 25.59 ? 347 HOH F O   1 
HETATM 13905 O  O   . HOH DB 4 .   ? 12.588  75.453  28.717  1.00 31.77 ? 348 HOH F O   1 
HETATM 13906 O  O   . HOH DB 4 .   ? 16.087  85.727  38.704  1.00 18.36 ? 349 HOH F O   1 
HETATM 13907 O  O   . HOH DB 4 .   ? 12.848  75.579  49.217  1.00 30.79 ? 350 HOH F O   1 
HETATM 13908 O  O   . HOH DB 4 .   ? 17.451  49.838  44.762  1.00 37.75 ? 351 HOH F O   1 
HETATM 13909 O  O   . HOH DB 4 .   ? 35.804  72.783  51.292  1.00 36.40 ? 352 HOH F O   1 
HETATM 13910 O  O   . HOH DB 4 .   ? 28.897  70.555  57.948  1.00 31.52 ? 353 HOH F O   1 
HETATM 13911 O  O   . HOH DB 4 .   ? 34.275  66.863  33.739  1.00 46.89 ? 354 HOH F O   1 
HETATM 13912 O  O   . HOH DB 4 .   ? 2.817   63.609  33.197  1.00 44.92 ? 355 HOH F O   1 
HETATM 13913 O  O   . HOH DB 4 .   ? 30.378  65.357  54.032  1.00 38.12 ? 356 HOH F O   1 
HETATM 13914 O  O   . HOH DB 4 .   ? 32.675  66.824  54.490  1.00 35.38 ? 357 HOH F O   1 
HETATM 13915 O  O   . HOH DB 4 .   ? 23.063  79.900  21.206  1.00 36.70 ? 358 HOH F O   1 
HETATM 13916 O  O   . HOH DB 4 .   ? 23.248  62.522  49.987  1.00 26.99 ? 359 HOH F O   1 
HETATM 13917 O  O   . HOH DB 4 .   ? 5.722   70.008  34.716  1.00 38.51 ? 360 HOH F O   1 
HETATM 13918 O  O   . HOH DB 4 .   ? 25.721  66.585  55.235  1.00 35.63 ? 361 HOH F O   1 
HETATM 13919 O  O   . HOH DB 4 .   ? 28.519  65.930  56.170  1.00 36.06 ? 362 HOH F O   1 
HETATM 13920 O  O   . HOH DB 4 .   ? 20.345  90.403  32.966  1.00 18.02 ? 363 HOH F O   1 
HETATM 13921 O  O   . HOH DB 4 .   ? 15.202  68.578  52.355  1.00 18.69 ? 364 HOH F O   1 
HETATM 13922 O  O   . HOH DB 4 .   ? 4.189   66.197  43.843  1.00 24.72 ? 365 HOH F O   1 
HETATM 13923 O  O   . HOH DB 4 .   ? 13.643  56.027  49.263  1.00 38.36 ? 366 HOH F O   1 
HETATM 13924 O  O   . HOH DB 4 .   ? 28.480  88.556  28.407  1.00 23.76 ? 367 HOH F O   1 
HETATM 13925 O  O   . HOH DB 4 .   ? 24.296  59.521  39.108  1.00 29.95 ? 368 HOH F O   1 
HETATM 13926 O  O   . HOH DB 4 .   ? 18.629  91.008  44.294  1.00 30.59 ? 369 HOH F O   1 
HETATM 13927 O  O   . HOH DB 4 .   ? 5.171   60.577  30.627  1.00 33.93 ? 370 HOH F O   1 
HETATM 13928 O  O   . HOH DB 4 .   ? 13.222  61.059  30.156  1.00 37.01 ? 371 HOH F O   1 
HETATM 13929 O  O   . HOH DB 4 .   ? 37.328  72.916  48.931  1.00 34.65 ? 372 HOH F O   1 
HETATM 13930 O  O   . HOH DB 4 .   ? 35.383  80.869  39.777  1.00 37.82 ? 373 HOH F O   1 
HETATM 13931 O  O   . HOH DB 4 .   ? 6.603   75.150  32.496  1.00 36.49 ? 374 HOH F O   1 
HETATM 13932 O  O   . HOH DB 4 .   ? 12.903  58.875  48.734  1.00 34.18 ? 375 HOH F O   1 
HETATM 13933 O  O   . HOH DB 4 .   ? 25.369  81.788  52.384  1.00 27.87 ? 376 HOH F O   1 
HETATM 13934 O  O   . HOH DB 4 .   ? 19.642  81.119  27.098  1.00 33.96 ? 377 HOH F O   1 
HETATM 13935 O  O   . HOH DB 4 .   ? 31.345  87.571  32.494  1.00 26.80 ? 378 HOH F O   1 
HETATM 13936 O  O   . HOH DB 4 .   ? 17.392  76.101  24.241  1.00 33.94 ? 379 HOH F O   1 
HETATM 13937 O  O   . HOH DB 4 .   ? 14.862  71.664  54.579  1.00 29.89 ? 380 HOH F O   1 
HETATM 13938 O  O   . HOH DB 4 .   ? 30.603  87.581  29.750  1.00 32.12 ? 381 HOH F O   1 
HETATM 13939 O  O   . HOH DB 4 .   ? 26.908  59.102  30.151  1.00 37.54 ? 382 HOH F O   1 
HETATM 13940 O  O   . HOH DB 4 .   ? 27.876  79.067  53.525  1.00 32.13 ? 383 HOH F O   1 
HETATM 13941 O  O   . HOH DB 4 .   ? 34.633  76.889  43.538  1.00 33.64 ? 384 HOH F O   1 
HETATM 13942 O  O   . HOH DB 4 .   ? 25.408  59.208  34.939  1.00 34.48 ? 385 HOH F O   1 
HETATM 13943 O  O   . HOH DB 4 .   ? 14.032  85.535  34.223  1.00 22.34 ? 386 HOH F O   1 
HETATM 13944 O  O   . HOH DB 4 .   ? 23.376  86.992  24.484  1.00 40.71 ? 387 HOH F O   1 
HETATM 13945 O  O   . HOH EB 4 .   ? 70.942  123.906 28.518  1.00 18.45 ? 301 HOH G O   1 
HETATM 13946 O  O   . HOH EB 4 .   ? 56.256  119.378 30.690  1.00 8.64  ? 302 HOH G O   1 
HETATM 13947 O  O   . HOH EB 4 .   ? 74.742  128.103 17.266  1.00 13.66 ? 303 HOH G O   1 
HETATM 13948 O  O   . HOH EB 4 .   ? 61.842  112.662 14.612  1.00 20.85 ? 304 HOH G O   1 
HETATM 13949 O  O   . HOH EB 4 .   ? 84.365  127.292 17.685  1.00 15.80 ? 305 HOH G O   1 
HETATM 13950 O  O   . HOH EB 4 .   ? 55.199  119.764 24.128  1.00 12.75 ? 306 HOH G O   1 
HETATM 13951 O  O   . HOH EB 4 .   ? 57.188  138.672 26.017  1.00 25.96 ? 307 HOH G O   1 
HETATM 13952 O  O   . HOH EB 4 .   ? 72.259  134.860 15.877  1.00 18.21 ? 308 HOH G O   1 
HETATM 13953 O  O   . HOH EB 4 .   ? 56.760  119.615 21.093  1.00 10.73 ? 309 HOH G O   1 
HETATM 13954 O  O   . HOH EB 4 .   ? 67.286  141.919 16.865  1.00 21.06 ? 310 HOH G O   1 
HETATM 13955 O  O   . HOH EB 4 .   ? 51.834  122.395 24.796  1.00 23.23 ? 311 HOH G O   1 
HETATM 13956 O  O   . HOH EB 4 .   ? 63.531  138.709 21.404  1.00 18.29 ? 312 HOH G O   1 
HETATM 13957 O  O   . HOH EB 4 .   ? 59.498  123.456 36.815  1.00 23.35 ? 313 HOH G O   1 
HETATM 13958 O  O   . HOH EB 4 .   ? 75.293  119.827 15.658  1.00 19.68 ? 314 HOH G O   1 
HETATM 13959 O  O   . HOH EB 4 .   ? 75.579  124.374 12.550  1.00 16.21 ? 315 HOH G O   1 
HETATM 13960 O  O   . HOH EB 4 .   ? 81.899  128.523 16.175  1.00 22.86 ? 316 HOH G O   1 
HETATM 13961 O  O   . HOH EB 4 .   ? 66.437  136.159 13.763  1.00 21.43 ? 317 HOH G O   1 
HETATM 13962 O  O   . HOH EB 4 .   ? 71.690  134.219 28.431  1.00 17.39 ? 318 HOH G O   1 
HETATM 13963 O  O   . HOH EB 4 .   ? 69.087  114.847 16.122  1.00 17.06 ? 319 HOH G O   1 
HETATM 13964 O  O   . HOH EB 4 .   ? 73.977  128.595 24.175  1.00 25.35 ? 320 HOH G O   1 
HETATM 13965 O  O   . HOH EB 4 .   ? 74.293  120.445 18.361  1.00 20.95 ? 321 HOH G O   1 
HETATM 13966 O  O   . HOH EB 4 .   ? 73.581  142.357 31.599  1.00 29.63 ? 322 HOH G O   1 
HETATM 13967 O  O   . HOH EB 4 .   ? 50.454  133.829 29.388  1.00 20.89 ? 323 HOH G O   1 
HETATM 13968 O  O   . HOH EB 4 .   ? 46.352  125.433 19.989  1.00 23.27 ? 324 HOH G O   1 
HETATM 13969 O  O   . HOH EB 4 .   ? 57.922  135.406 10.538  1.00 32.71 ? 325 HOH G O   1 
HETATM 13970 O  O   . HOH EB 4 .   ? 72.502  124.152 10.545  1.00 20.95 ? 326 HOH G O   1 
HETATM 13971 O  O   . HOH EB 4 .   ? 57.288  142.003 9.578   1.00 31.55 ? 327 HOH G O   1 
HETATM 13972 O  O   . HOH EB 4 .   ? 70.348  135.522 10.857  1.00 26.21 ? 328 HOH G O   1 
HETATM 13973 O  O   . HOH EB 4 .   ? 63.916  136.110 14.546  1.00 21.31 ? 329 HOH G O   1 
HETATM 13974 O  O   . HOH EB 4 .   ? 61.683  136.001 12.854  1.00 24.67 ? 330 HOH G O   1 
HETATM 13975 O  O   . HOH EB 4 .   ? 72.698  135.500 26.390  1.00 14.75 ? 331 HOH G O   1 
HETATM 13976 O  O   . HOH EB 4 .   ? 74.426  144.890 19.598  1.00 27.69 ? 332 HOH G O   1 
HETATM 13977 O  O   . HOH EB 4 .   ? 57.450  121.245 9.472   1.00 23.09 ? 333 HOH G O   1 
HETATM 13978 O  O   . HOH EB 4 .   ? 53.733  141.699 27.827  1.00 26.58 ? 334 HOH G O   1 
HETATM 13979 O  O   . HOH EB 4 .   ? 74.290  126.823 5.112   1.00 33.42 ? 335 HOH G O   1 
HETATM 13980 O  O   . HOH EB 4 .   ? 43.748  130.732 11.056  1.00 31.28 ? 336 HOH G O   1 
HETATM 13981 O  O   . HOH EB 4 .   ? 53.019  120.690 22.789  1.00 19.36 ? 337 HOH G O   1 
HETATM 13982 O  O   . HOH EB 4 .   ? 56.428  124.945 38.091  1.00 30.19 ? 338 HOH G O   1 
HETATM 13983 O  O   . HOH EB 4 .   ? 58.431  118.115 11.485  1.00 25.39 ? 339 HOH G O   1 
HETATM 13984 O  O   . HOH EB 4 .   ? 55.671  123.534 27.967  1.00 18.26 ? 340 HOH G O   1 
HETATM 13985 O  O   . HOH EB 4 .   ? 59.712  135.786 31.455  1.00 25.36 ? 341 HOH G O   1 
HETATM 13986 O  O   . HOH EB 4 .   ? 60.749  145.127 15.033  1.00 42.44 ? 342 HOH G O   1 
HETATM 13987 O  O   . HOH EB 4 .   ? 57.503  147.994 32.769  1.00 25.63 ? 343 HOH G O   1 
HETATM 13988 O  O   . HOH EB 4 .   ? 75.289  124.896 24.604  1.00 27.92 ? 344 HOH G O   1 
HETATM 13989 O  O   . HOH EB 4 .   ? 62.323  136.753 31.201  1.00 20.83 ? 345 HOH G O   1 
HETATM 13990 O  O   . HOH EB 4 .   ? 67.398  125.510 33.982  1.00 23.91 ? 346 HOH G O   1 
HETATM 13991 O  O   . HOH EB 4 .   ? 69.412  133.944 34.584  1.00 26.63 ? 347 HOH G O   1 
HETATM 13992 O  O   . HOH EB 4 .   ? 55.333  143.199 9.725   1.00 39.58 ? 348 HOH G O   1 
HETATM 13993 O  O   . HOH EB 4 .   ? 67.733  134.912 10.877  1.00 27.99 ? 349 HOH G O   1 
HETATM 13994 O  O   . HOH EB 4 .   ? 56.487  137.153 31.915  1.00 33.82 ? 350 HOH G O   1 
HETATM 13995 O  O   . HOH EB 4 .   ? 67.068  138.805 12.649  1.00 33.38 ? 351 HOH G O   1 
HETATM 13996 O  O   . HOH EB 4 .   ? 54.961  125.395 29.405  1.00 23.55 ? 352 HOH G O   1 
HETATM 13997 O  O   . HOH EB 4 .   ? 58.175  125.953 36.262  1.00 27.21 ? 353 HOH G O   1 
HETATM 13998 O  O   . HOH EB 4 .   ? 73.419  145.115 22.225  1.00 32.50 ? 354 HOH G O   1 
HETATM 13999 O  O   . HOH EB 4 .   ? 55.914  123.214 10.037  1.00 24.24 ? 355 HOH G O   1 
HETATM 14000 O  O   . HOH EB 4 .   ? 63.949  149.989 27.215  1.00 27.07 ? 356 HOH G O   1 
HETATM 14001 O  O   . HOH EB 4 .   ? 68.731  134.908 14.763  1.00 24.48 ? 357 HOH G O   1 
HETATM 14002 O  O   . HOH EB 4 .   ? 59.338  145.305 17.530  1.00 29.30 ? 358 HOH G O   1 
HETATM 14003 O  O   . HOH EB 4 .   ? 67.460  130.893 32.291  1.00 22.97 ? 359 HOH G O   1 
HETATM 14004 O  O   . HOH EB 4 .   ? 66.479  140.080 32.061  1.00 21.55 ? 360 HOH G O   1 
HETATM 14005 O  O   . HOH EB 4 .   ? 47.313  136.040 17.567  1.00 30.48 ? 361 HOH G O   1 
HETATM 14006 O  O   . HOH EB 4 .   ? 73.318  137.256 16.911  1.00 29.45 ? 362 HOH G O   1 
HETATM 14007 O  O   . HOH EB 4 .   ? 46.057  130.859 9.775   1.00 34.58 ? 363 HOH G O   1 
HETATM 14008 O  O   . HOH EB 4 .   ? 65.402  120.952 9.382   1.00 26.88 ? 364 HOH G O   1 
HETATM 14009 O  O   . HOH EB 4 .   ? 73.886  124.305 6.360   1.00 34.81 ? 365 HOH G O   1 
HETATM 14010 O  O   . HOH EB 4 .   ? 56.490  120.247 37.791  1.00 25.87 ? 366 HOH G O   1 
HETATM 14011 O  O   . HOH EB 4 .   ? 49.486  139.078 3.989   1.00 36.25 ? 367 HOH G O   1 
HETATM 14012 O  O   . HOH EB 4 .   ? 62.876  138.964 14.659  1.00 29.28 ? 368 HOH G O   1 
HETATM 14013 O  O   . HOH EB 4 .   ? 74.108  137.972 19.285  1.00 29.56 ? 369 HOH G O   1 
HETATM 14014 O  O   . HOH EB 4 .   ? 55.381  147.388 30.773  1.00 21.74 ? 370 HOH G O   1 
HETATM 14015 O  O   . HOH EB 4 .   ? 50.188  141.588 16.908  1.00 34.55 ? 371 HOH G O   1 
HETATM 14016 O  O   . HOH EB 4 .   ? 59.677  127.920 6.539   1.00 30.22 ? 372 HOH G O   1 
HETATM 14017 O  O   . HOH EB 4 .   ? 63.023  110.942 9.795   1.00 31.83 ? 373 HOH G O   1 
HETATM 14018 O  O   . HOH EB 4 .   ? 64.594  150.376 33.714  1.00 33.20 ? 374 HOH G O   1 
HETATM 14019 O  O   . HOH EB 4 .   ? 46.562  129.916 25.117  1.00 35.97 ? 375 HOH G O   1 
HETATM 14020 O  O   . HOH EB 4 .   ? 54.346  145.193 22.141  1.00 33.78 ? 376 HOH G O   1 
HETATM 14021 O  O   . HOH EB 4 .   ? 67.907  148.442 26.172  1.00 32.60 ? 377 HOH G O   1 
HETATM 14022 O  O   . HOH EB 4 .   ? 75.027  133.863 34.634  1.00 32.99 ? 378 HOH G O   1 
HETATM 14023 O  O   . HOH EB 4 .   ? 54.095  134.284 6.538   1.00 38.45 ? 379 HOH G O   1 
HETATM 14024 O  O   . HOH EB 4 .   ? 52.236  140.461 7.715   1.00 34.75 ? 380 HOH G O   1 
HETATM 14025 O  O   . HOH EB 4 .   ? 81.261  122.074 19.962  1.00 19.01 ? 381 HOH G O   1 
HETATM 14026 O  O   . HOH EB 4 .   ? 62.673  114.168 11.456  1.00 27.84 ? 382 HOH G O   1 
HETATM 14027 O  O   . HOH EB 4 .   ? 53.922  139.477 5.893   1.00 30.55 ? 383 HOH G O   1 
HETATM 14028 O  O   . HOH EB 4 .   ? 60.546  134.128 10.408  1.00 32.98 ? 384 HOH G O   1 
HETATM 14029 O  O   . HOH EB 4 .   ? 50.566  131.230 30.472  1.00 33.26 ? 385 HOH G O   1 
HETATM 14030 O  O   . HOH EB 4 .   ? 51.267  119.270 27.356  1.00 25.96 ? 386 HOH G O   1 
HETATM 14031 O  O   . HOH EB 4 .   ? 74.211  131.510 7.204   1.00 34.81 ? 387 HOH G O   1 
HETATM 14032 O  O   . HOH EB 4 .   ? 71.625  141.494 33.344  1.00 34.89 ? 388 HOH G O   1 
HETATM 14033 O  O   . HOH EB 4 .   ? 44.161  142.067 9.923   1.00 37.60 ? 389 HOH G O   1 
HETATM 14034 O  O   . HOH EB 4 .   ? 56.646  148.137 24.360  1.00 36.53 ? 390 HOH G O   1 
HETATM 14035 O  O   . HOH EB 4 .   ? 64.435  131.000 36.865  1.00 31.13 ? 391 HOH G O   1 
HETATM 14036 O  O   . HOH EB 4 .   ? 80.305  124.365 27.949  1.00 34.50 ? 392 HOH G O   1 
HETATM 14037 O  O   . HOH EB 4 .   ? 69.581  123.949 33.490  1.00 34.42 ? 393 HOH G O   1 
HETATM 14038 O  O   . HOH EB 4 .   ? 49.017  128.351 26.542  1.00 35.72 ? 394 HOH G O   1 
HETATM 14039 O  O   . HOH EB 4 .   ? 61.175  142.095 14.801  1.00 28.13 ? 395 HOH G O   1 
HETATM 14040 O  O   . HOH EB 4 .   ? 46.333  135.258 0.567   1.00 47.64 ? 396 HOH G O   1 
HETATM 14041 O  O   . HOH EB 4 .   ? 47.215  138.077 19.249  1.00 27.55 ? 397 HOH G O   1 
HETATM 14042 O  O   . HOH EB 4 .   ? 63.255  118.956 12.885  1.00 22.20 ? 398 HOH G O   1 
HETATM 14043 O  O   . HOH EB 4 .   ? 75.362  131.083 23.809  1.00 32.14 ? 399 HOH G O   1 
HETATM 14044 O  O   . HOH EB 4 .   ? 42.885  131.983 6.709   1.00 40.98 ? 400 HOH G O   1 
HETATM 14045 O  O   . HOH EB 4 .   ? 71.912  126.087 31.193  1.00 28.79 ? 401 HOH G O   1 
HETATM 14046 O  O   . HOH EB 4 .   ? 66.669  142.111 34.845  1.00 41.27 ? 402 HOH G O   1 
HETATM 14047 O  O   . HOH EB 4 .   ? 69.910  122.787 5.560   1.00 39.81 ? 403 HOH G O   1 
HETATM 14048 O  O   . HOH EB 4 .   ? 54.756  130.538 36.956  1.00 29.48 ? 404 HOH G O   1 
HETATM 14049 O  O   . HOH EB 4 .   ? 45.589  123.016 20.188  1.00 32.76 ? 405 HOH G O   1 
HETATM 14050 O  O   . HOH EB 4 .   ? 78.412  117.231 17.778  1.00 22.42 ? 406 HOH G O   1 
HETATM 14051 O  O   . HOH EB 4 .   ? 57.067  120.802 6.540   1.00 25.39 ? 407 HOH G O   1 
HETATM 14052 O  O   . HOH EB 4 .   ? 78.081  118.062 20.719  1.00 30.71 ? 408 HOH G O   1 
HETATM 14053 O  O   . HOH EB 4 .   ? 61.851  106.075 10.579  1.00 38.18 ? 409 HOH G O   1 
HETATM 14054 O  O   . HOH EB 4 .   ? 50.425  122.284 12.925  1.00 27.09 ? 410 HOH G O   1 
HETATM 14055 O  O   . HOH EB 4 .   ? 64.903  141.504 15.026  1.00 31.24 ? 411 HOH G O   1 
HETATM 14056 O  O   . HOH EB 4 .   ? 64.284  104.879 10.939  1.00 34.06 ? 412 HOH G O   1 
HETATM 14057 O  O   . HOH EB 4 .   ? 77.963  132.257 13.287  1.00 34.51 ? 413 HOH G O   1 
HETATM 14058 O  O   . HOH EB 4 .   ? 71.202  121.306 4.151   1.00 34.79 ? 414 HOH G O   1 
HETATM 14059 O  O   . HOH EB 4 .   ? 50.553  122.125 15.581  1.00 26.26 ? 415 HOH G O   1 
HETATM 14060 O  O   . HOH EB 4 .   ? 48.034  128.244 29.487  1.00 40.14 ? 416 HOH G O   1 
HETATM 14061 O  O   . HOH EB 4 .   ? 61.608  134.631 7.965   1.00 34.31 ? 417 HOH G O   1 
HETATM 14062 O  O   . HOH EB 4 .   ? 56.899  129.499 35.549  1.00 35.24 ? 418 HOH G O   1 
HETATM 14063 O  O   . HOH EB 4 .   ? 67.092  128.811 8.406   1.00 26.97 ? 419 HOH G O   1 
HETATM 14064 O  O   . HOH EB 4 .   ? 74.534  125.619 9.178   1.00 32.41 ? 420 HOH G O   1 
HETATM 14065 O  O   . HOH EB 4 .   ? 60.724  112.868 10.324  1.00 36.91 ? 421 HOH G O   1 
HETATM 14066 O  O   . HOH EB 4 .   ? 81.256  143.175 24.790  1.00 46.51 ? 422 HOH G O   1 
HETATM 14067 O  O   . HOH EB 4 .   ? 69.247  144.696 25.430  1.00 27.26 ? 423 HOH G O   1 
HETATM 14068 O  O   . HOH EB 4 .   ? 50.137  141.812 5.996   1.00 35.30 ? 424 HOH G O   1 
HETATM 14069 O  O   . HOH EB 4 .   ? 42.720  133.406 15.025  1.00 24.08 ? 425 HOH G O   1 
HETATM 14070 O  O   . HOH EB 4 .   ? 44.134  139.564 11.964  1.00 32.84 ? 426 HOH G O   1 
HETATM 14071 O  O   . HOH EB 4 .   ? 45.264  133.940 18.276  1.00 29.49 ? 427 HOH G O   1 
HETATM 14072 O  O   . HOH EB 4 .   ? 48.926  120.367 31.274  1.00 31.69 ? 428 HOH G O   1 
HETATM 14073 O  O   . HOH EB 4 .   ? 77.335  129.631 16.612  1.00 21.06 ? 429 HOH G O   1 
HETATM 14074 O  O   . HOH EB 4 .   ? 59.339  139.900 34.177  1.00 30.84 ? 430 HOH G O   1 
HETATM 14075 O  O   . HOH EB 4 .   ? 72.384  117.094 22.399  1.00 29.63 ? 431 HOH G O   1 
HETATM 14076 O  O   . HOH EB 4 .   ? 66.230  145.972 28.133  1.00 30.32 ? 432 HOH G O   1 
HETATM 14077 O  O   . HOH EB 4 .   ? 54.279  121.828 26.728  1.00 27.98 ? 433 HOH G O   1 
HETATM 14078 O  O   . HOH EB 4 .   ? 57.697  133.071 34.450  1.00 31.94 ? 434 HOH G O   1 
HETATM 14079 O  O   . HOH EB 4 .   ? 74.545  137.669 22.394  1.00 27.80 ? 435 HOH G O   1 
HETATM 14080 O  O   . HOH EB 4 .   ? 66.276  135.666 33.322  1.00 27.99 ? 436 HOH G O   1 
HETATM 14081 O  O   . HOH EB 4 .   ? 74.757  135.671 24.686  1.00 25.65 ? 437 HOH G O   1 
HETATM 14082 O  O   . HOH FB 4 .   ? 60.441  97.460  30.000  1.00 9.66  ? 301 HOH H O   1 
HETATM 14083 O  O   . HOH FB 4 .   ? 41.310  107.109 36.493  1.00 11.56 ? 302 HOH H O   1 
HETATM 14084 O  O   . HOH FB 4 .   ? 70.851  99.782  27.252  1.00 14.39 ? 303 HOH H O   1 
HETATM 14085 O  O   . HOH FB 4 .   ? 58.602  99.421  36.470  1.00 10.19 ? 304 HOH H O   1 
HETATM 14086 O  O   . HOH FB 4 .   ? 44.227  101.887 29.849  1.00 7.81  ? 305 HOH H O   1 
HETATM 14087 O  O   . HOH FB 4 .   ? 44.069  107.844 26.357  1.00 14.68 ? 306 HOH H O   1 
HETATM 14088 O  O   . HOH FB 4 .   ? 55.630  117.500 28.863  1.00 8.99  ? 307 HOH H O   1 
HETATM 14089 O  O   . HOH FB 4 .   ? 42.296  103.854 29.195  1.00 9.11  ? 308 HOH H O   1 
HETATM 14090 O  O   . HOH FB 4 .   ? 63.058  94.090  35.387  1.00 13.06 ? 309 HOH H O   1 
HETATM 14091 O  O   . HOH FB 4 .   ? 41.113  111.758 32.597  1.00 17.23 ? 310 HOH H O   1 
HETATM 14092 O  O   . HOH FB 4 .   ? 44.419  99.643  28.178  1.00 11.46 ? 311 HOH H O   1 
HETATM 14093 O  O   . HOH FB 4 .   ? 64.100  84.910  28.186  1.00 25.77 ? 312 HOH H O   1 
HETATM 14094 O  O   . HOH FB 4 .   ? 50.082  103.464 19.216  1.00 18.24 ? 313 HOH H O   1 
HETATM 14095 O  O   . HOH FB 4 .   ? 52.510  90.440  32.215  1.00 18.56 ? 314 HOH H O   1 
HETATM 14096 O  O   . HOH FB 4 .   ? 39.918  99.095  34.957  1.00 12.24 ? 315 HOH H O   1 
HETATM 14097 O  O   . HOH FB 4 .   ? 60.164  110.320 14.125  1.00 16.27 ? 316 HOH H O   1 
HETATM 14098 O  O   . HOH FB 4 .   ? 64.450  100.728 37.917  1.00 18.40 ? 317 HOH H O   1 
HETATM 14099 O  O   . HOH FB 4 .   ? 57.450  117.314 19.571  1.00 14.52 ? 318 HOH H O   1 
HETATM 14100 O  O   . HOH FB 4 .   ? 61.699  86.218  25.242  1.00 18.76 ? 319 HOH H O   1 
HETATM 14101 O  O   . HOH FB 4 .   ? 55.142  91.323  32.762  1.00 22.56 ? 320 HOH H O   1 
HETATM 14102 O  O   . HOH FB 4 .   ? 53.291  87.809  28.688  1.00 21.10 ? 321 HOH H O   1 
HETATM 14103 O  O   . HOH FB 4 .   ? 61.886  99.142  20.457  1.00 14.77 ? 322 HOH H O   1 
HETATM 14104 O  O   . HOH FB 4 .   ? 53.936  115.475 23.244  1.00 21.55 ? 323 HOH H O   1 
HETATM 14105 O  O   . HOH FB 4 .   ? 61.962  84.269  30.527  1.00 19.70 ? 324 HOH H O   1 
HETATM 14106 O  O   . HOH FB 4 .   ? 64.678  89.769  29.704  1.00 17.02 ? 325 HOH H O   1 
HETATM 14107 O  O   . HOH FB 4 .   ? 52.460  95.097  21.261  1.00 14.41 ? 326 HOH H O   1 
HETATM 14108 O  O   . HOH FB 4 .   ? 47.849  93.460  34.517  1.00 17.12 ? 327 HOH H O   1 
HETATM 14109 O  O   . HOH FB 4 .   ? 62.818  90.330  32.339  1.00 17.13 ? 328 HOH H O   1 
HETATM 14110 O  O   . HOH FB 4 .   ? 42.858  104.519 26.284  1.00 19.91 ? 329 HOH H O   1 
HETATM 14111 O  O   . HOH FB 4 .   ? 53.319  115.789 40.386  1.00 24.99 ? 330 HOH H O   1 
HETATM 14112 O  O   . HOH FB 4 .   ? 54.535  86.479  17.858  1.00 26.40 ? 331 HOH H O   1 
HETATM 14113 O  O   . HOH FB 4 .   ? 70.401  101.147 25.000  1.00 19.68 ? 332 HOH H O   1 
HETATM 14114 O  O   . HOH FB 4 .   ? 70.828  111.532 25.173  1.00 20.79 ? 333 HOH H O   1 
HETATM 14115 O  O   . HOH FB 4 .   ? 48.316  93.364  29.578  1.00 18.33 ? 334 HOH H O   1 
HETATM 14116 O  O   . HOH FB 4 .   ? 52.945  90.475  29.500  1.00 13.81 ? 335 HOH H O   1 
HETATM 14117 O  O   . HOH FB 4 .   ? 66.600  91.234  28.087  1.00 23.17 ? 336 HOH H O   1 
HETATM 14118 O  O   . HOH FB 4 .   ? 58.601  119.697 42.336  1.00 39.33 ? 337 HOH H O   1 
HETATM 14119 O  O   . HOH FB 4 .   ? 59.282  117.609 38.117  1.00 15.14 ? 338 HOH H O   1 
HETATM 14120 O  O   . HOH FB 4 .   ? 54.964  117.359 25.612  1.00 15.35 ? 339 HOH H O   1 
HETATM 14121 O  O   . HOH FB 4 .   ? 57.341  84.222  30.201  1.00 23.20 ? 340 HOH H O   1 
HETATM 14122 O  O   . HOH FB 4 .   ? 68.826  109.198 45.465  1.00 40.82 ? 341 HOH H O   1 
HETATM 14123 O  O   . HOH FB 4 .   ? 58.037  99.828  17.746  1.00 31.04 ? 342 HOH H O   1 
HETATM 14124 O  O   . HOH FB 4 .   ? 70.263  90.527  31.302  1.00 18.26 ? 343 HOH H O   1 
HETATM 14125 O  O   . HOH FB 4 .   ? 48.683  91.966  32.088  1.00 31.89 ? 344 HOH H O   1 
HETATM 14126 O  O   . HOH FB 4 .   ? 54.221  88.282  26.118  1.00 17.31 ? 345 HOH H O   1 
HETATM 14127 O  O   . HOH FB 4 .   ? 60.679  94.764  36.801  1.00 17.87 ? 346 HOH H O   1 
HETATM 14128 O  O   . HOH FB 4 .   ? 74.360  109.258 30.832  1.00 25.36 ? 347 HOH H O   1 
HETATM 14129 O  O   . HOH FB 4 .   ? 61.986  100.831 40.399  1.00 19.57 ? 348 HOH H O   1 
HETATM 14130 O  O   . HOH FB 4 .   ? 48.927  92.123  36.938  1.00 22.90 ? 349 HOH H O   1 
HETATM 14131 O  O   . HOH FB 4 .   ? 71.947  107.527 35.365  1.00 19.20 ? 350 HOH H O   1 
HETATM 14132 O  O   . HOH FB 4 .   ? 56.739  88.594  17.310  1.00 24.53 ? 351 HOH H O   1 
HETATM 14133 O  O   . HOH FB 4 .   ? 66.424  99.685  18.495  1.00 32.65 ? 352 HOH H O   1 
HETATM 14134 O  O   . HOH FB 4 .   ? 61.878  93.607  42.397  1.00 21.99 ? 353 HOH H O   1 
HETATM 14135 O  O   . HOH FB 4 .   ? 56.346  84.908  32.420  1.00 23.07 ? 354 HOH H O   1 
HETATM 14136 O  O   . HOH FB 4 .   ? 67.763  104.917 20.526  1.00 21.79 ? 355 HOH H O   1 
HETATM 14137 O  O   . HOH FB 4 .   ? 44.468  112.431 27.459  1.00 20.47 ? 356 HOH H O   1 
HETATM 14138 O  O   . HOH FB 4 .   ? 65.848  95.579  20.286  1.00 24.00 ? 357 HOH H O   1 
HETATM 14139 O  O   . HOH FB 4 .   ? 55.192  87.442  31.020  1.00 23.31 ? 358 HOH H O   1 
HETATM 14140 O  O   . HOH FB 4 .   ? 52.452  89.775  25.629  1.00 19.07 ? 359 HOH H O   1 
HETATM 14141 O  O   . HOH FB 4 .   ? 60.360  82.963  29.021  1.00 20.50 ? 360 HOH H O   1 
HETATM 14142 O  O   . HOH FB 4 .   ? 49.492  104.950 46.169  1.00 25.40 ? 361 HOH H O   1 
HETATM 14143 O  O   . HOH FB 4 .   ? 69.072  110.279 19.457  1.00 29.46 ? 362 HOH H O   1 
HETATM 14144 O  O   . HOH FB 4 .   ? 43.647  96.300  24.989  1.00 24.05 ? 363 HOH H O   1 
HETATM 14145 O  O   . HOH FB 4 .   ? 71.069  110.772 42.106  1.00 32.13 ? 364 HOH H O   1 
HETATM 14146 O  O   . HOH FB 4 .   ? 52.939  87.704  32.506  1.00 20.30 ? 365 HOH H O   1 
HETATM 14147 O  O   . HOH FB 4 .   ? 44.996  102.753 20.565  1.00 28.88 ? 366 HOH H O   1 
HETATM 14148 O  O   . HOH FB 4 .   ? 72.648  115.621 39.730  1.00 39.59 ? 367 HOH H O   1 
HETATM 14149 O  O   . HOH FB 4 .   ? 61.603  116.520 39.689  1.00 20.22 ? 368 HOH H O   1 
HETATM 14150 O  O   . HOH FB 4 .   ? 70.282  97.362  34.514  1.00 26.49 ? 369 HOH H O   1 
HETATM 14151 O  O   . HOH FB 4 .   ? 58.510  96.554  35.810  1.00 19.72 ? 370 HOH H O   1 
HETATM 14152 O  O   . HOH FB 4 .   ? 73.664  105.890 33.234  1.00 25.44 ? 371 HOH H O   1 
HETATM 14153 O  O   . HOH FB 4 .   ? 47.332  96.031  42.059  1.00 20.16 ? 372 HOH H O   1 
HETATM 14154 O  O   . HOH FB 4 .   ? 63.071  84.180  26.052  1.00 25.61 ? 373 HOH H O   1 
HETATM 14155 O  O   . HOH FB 4 .   ? 51.618  91.764  27.192  1.00 19.04 ? 374 HOH H O   1 
HETATM 14156 O  O   . HOH FB 4 .   ? 58.462  97.004  16.697  1.00 36.00 ? 375 HOH H O   1 
HETATM 14157 O  O   . HOH FB 4 .   ? 56.998  89.208  32.021  1.00 16.84 ? 376 HOH H O   1 
HETATM 14158 O  O   . HOH FB 4 .   ? 55.770  91.720  35.410  1.00 22.02 ? 377 HOH H O   1 
HETATM 14159 O  O   . HOH FB 4 .   ? 45.683  96.712  40.241  1.00 19.86 ? 378 HOH H O   1 
HETATM 14160 O  O   . HOH FB 4 .   ? 51.410  113.801 39.075  1.00 18.30 ? 379 HOH H O   1 
HETATM 14161 O  O   . HOH FB 4 .   ? 56.987  89.717  14.438  1.00 31.37 ? 380 HOH H O   1 
HETATM 14162 O  O   . HOH FB 4 .   ? 66.932  120.562 36.684  1.00 26.58 ? 381 HOH H O   1 
HETATM 14163 O  O   . HOH FB 4 .   ? 52.506  116.748 26.754  1.00 19.42 ? 382 HOH H O   1 
HETATM 14164 O  O   . HOH FB 4 .   ? 65.219  87.448  28.107  1.00 31.43 ? 383 HOH H O   1 
HETATM 14165 O  O   . HOH FB 4 .   ? 59.043  92.586  15.893  1.00 30.40 ? 384 HOH H O   1 
HETATM 14166 O  O   . HOH FB 4 .   ? 70.190  106.960 20.410  1.00 23.85 ? 385 HOH H O   1 
HETATM 14167 O  O   . HOH FB 4 .   ? 77.344  115.103 41.852  1.00 48.54 ? 386 HOH H O   1 
HETATM 14168 O  O   . HOH FB 4 .   ? 72.214  99.775  29.687  1.00 31.28 ? 387 HOH H O   1 
HETATM 14169 O  O   . HOH FB 4 .   ? 59.115  120.357 39.450  1.00 37.28 ? 388 HOH H O   1 
HETATM 14170 O  O   . HOH FB 4 .   ? 49.182  94.295  20.555  1.00 37.65 ? 389 HOH H O   1 
HETATM 14171 O  O   . HOH FB 4 .   ? 74.861  116.303 29.652  1.00 28.61 ? 390 HOH H O   1 
HETATM 14172 O  O   . HOH FB 4 .   ? 50.861  109.743 42.993  1.00 25.43 ? 391 HOH H O   1 
HETATM 14173 O  O   . HOH FB 4 .   ? 64.596  100.508 20.297  1.00 28.53 ? 392 HOH H O   1 
HETATM 14174 O  O   . HOH FB 4 .   ? 51.013  114.810 24.113  1.00 26.74 ? 393 HOH H O   1 
HETATM 14175 O  O   . HOH FB 4 .   ? 55.042  118.588 38.571  1.00 25.78 ? 394 HOH H O   1 
HETATM 14176 O  O   . HOH FB 4 .   ? 58.296  85.136  36.296  1.00 25.79 ? 395 HOH H O   1 
HETATM 14177 O  O   . HOH FB 4 .   ? 48.688  101.373 17.631  1.00 30.18 ? 396 HOH H O   1 
HETATM 14178 O  O   . HOH FB 4 .   ? 64.870  89.935  25.204  1.00 33.81 ? 397 HOH H O   1 
HETATM 14179 O  O   . HOH FB 4 .   ? 70.791  114.428 24.195  1.00 32.39 ? 398 HOH H O   1 
HETATM 14180 O  O   . HOH FB 4 .   ? 52.020  89.890  20.090  1.00 35.60 ? 399 HOH H O   1 
HETATM 14181 O  O   . HOH FB 4 .   ? 66.085  104.937 15.648  1.00 24.14 ? 400 HOH H O   1 
HETATM 14182 O  O   . HOH FB 4 .   ? 68.146  100.569 37.669  1.00 27.98 ? 401 HOH H O   1 
HETATM 14183 O  O   . HOH FB 4 .   ? 72.208  115.050 36.894  1.00 32.46 ? 402 HOH H O   1 
HETATM 14184 O  O   . HOH FB 4 .   ? 69.202  115.119 26.090  1.00 25.85 ? 403 HOH H O   1 
HETATM 14185 O  O   . HOH FB 4 .   ? 62.569  84.833  13.911  1.00 37.35 ? 404 HOH H O   1 
HETATM 14186 O  O   . HOH FB 4 .   ? 58.035  100.067 42.599  1.00 22.53 ? 405 HOH H O   1 
HETATM 14187 O  O   . HOH FB 4 .   ? 60.407  107.041 42.927  1.00 22.48 ? 406 HOH H O   1 
HETATM 14188 O  O   . HOH FB 4 .   ? 42.990  105.799 43.525  1.00 17.88 ? 407 HOH H O   1 
HETATM 14189 O  O   . HOH FB 4 .   ? 72.377  92.565  22.459  1.00 28.59 ? 408 HOH H O   1 
HETATM 14190 O  O   . HOH FB 4 .   ? 72.141  109.383 44.782  1.00 39.33 ? 409 HOH H O   1 
HETATM 14191 O  O   . HOH FB 4 .   ? 48.832  114.733 22.710  1.00 31.96 ? 410 HOH H O   1 
HETATM 14192 O  O   . HOH FB 4 .   ? 65.104  129.242 39.016  1.00 30.32 ? 411 HOH H O   1 
HETATM 14193 O  O   . HOH FB 4 .   ? 49.847  112.597 21.330  1.00 26.97 ? 412 HOH H O   1 
HETATM 14194 O  O   . HOH FB 4 .   ? 72.592  109.074 23.285  1.00 30.90 ? 413 HOH H O   1 
HETATM 14195 O  O   . HOH FB 4 .   ? 71.410  117.762 30.570  1.00 30.79 ? 414 HOH H O   1 
HETATM 14196 O  O   . HOH FB 4 .   ? 67.022  103.280 18.585  1.00 30.66 ? 415 HOH H O   1 
HETATM 14197 O  O   . HOH FB 4 .   ? 58.789  128.062 37.483  1.00 29.29 ? 416 HOH H O   1 
HETATM 14198 O  O   . HOH FB 4 .   ? 49.005  114.213 37.753  1.00 21.90 ? 417 HOH H O   1 
HETATM 14199 O  O   . HOH FB 4 .   ? 39.248  95.469  41.802  1.00 26.76 ? 418 HOH H O   1 
HETATM 14200 O  O   . HOH FB 4 .   ? 51.728  118.012 21.690  1.00 28.02 ? 419 HOH H O   1 
HETATM 14201 O  O   . HOH FB 4 .   ? 55.826  113.010 21.612  1.00 17.93 ? 420 HOH H O   1 
HETATM 14202 O  O   . HOH FB 4 .   ? 43.995  93.272  36.392  1.00 32.88 ? 421 HOH H O   1 
HETATM 14203 O  O   . HOH FB 4 .   ? 48.191  106.188 17.460  1.00 38.08 ? 422 HOH H O   1 
HETATM 14204 O  O   . HOH FB 4 .   ? 61.274  117.460 42.721  1.00 31.49 ? 423 HOH H O   1 
HETATM 14205 O  O   . HOH FB 4 .   ? 43.299  95.957  41.648  1.00 29.53 ? 424 HOH H O   1 
HETATM 14206 O  O   . HOH FB 4 .   ? 41.315  94.899  36.121  1.00 30.53 ? 425 HOH H O   1 
HETATM 14207 O  O   . HOH FB 4 .   ? 49.834  110.422 22.725  1.00 21.53 ? 426 HOH H O   1 
HETATM 14208 O  O   . HOH FB 4 .   ? 67.974  102.371 40.609  1.00 20.15 ? 427 HOH H O   1 
HETATM 14209 O  O   . HOH FB 4 .   ? 59.852  130.105 37.636  1.00 34.21 ? 428 HOH H O   1 
HETATM 14210 O  O   . HOH FB 4 .   ? 49.165  91.691  28.271  1.00 26.29 ? 429 HOH H O   1 
HETATM 14211 O  O   . HOH FB 4 .   ? 74.010  101.009 30.593  1.00 26.16 ? 430 HOH H O   1 
HETATM 14212 O  O   . HOH FB 4 .   ? 47.282  104.678 18.843  1.00 33.81 ? 431 HOH H O   1 
HETATM 14213 O  O   . HOH FB 4 .   ? 36.927  96.491  43.037  1.00 31.27 ? 432 HOH H O   1 
HETATM 14214 O  O   . HOH FB 4 .   ? 69.160  98.449  36.810  1.00 30.75 ? 433 HOH H O   1 
HETATM 14215 O  O   . HOH FB 4 .   ? 75.121  110.680 33.338  1.00 38.24 ? 434 HOH H O   1 
HETATM 14216 O  O   . HOH FB 4 .   ? 44.507  101.011 18.151  1.00 38.97 ? 435 HOH H O   1 
HETATM 14217 O  O   . HOH FB 4 .   ? 71.988  119.107 34.676  1.00 37.77 ? 436 HOH H O   1 
HETATM 14218 O  O   . HOH FB 4 .   ? 74.209  97.299  27.868  1.00 30.34 ? 437 HOH H O   1 
HETATM 14219 O  O   . HOH FB 4 .   ? 56.001  98.347  23.952  1.00 24.14 ? 438 HOH H O   1 
HETATM 14220 O  O   . HOH FB 4 .   ? 58.275  103.601 16.382  1.00 24.70 ? 439 HOH H O   1 
HETATM 14221 O  O   . HOH FB 4 .   ? 67.802  110.348 42.447  1.00 31.00 ? 440 HOH H O   1 
HETATM 14222 O  O   . HOH FB 4 .   ? 38.931  93.822  38.120  1.00 27.44 ? 441 HOH H O   1 
HETATM 14223 O  O   . HOH FB 4 .   ? 67.316  99.981  40.248  1.00 31.95 ? 442 HOH H O   1 
HETATM 14224 O  O   . HOH FB 4 .   ? 52.681  111.312 43.160  1.00 32.68 ? 443 HOH H O   1 
HETATM 14225 O  O   . HOH FB 4 .   ? 55.477  108.677 12.529  1.00 32.83 ? 444 HOH H O   1 
HETATM 14226 O  O   . HOH FB 4 .   ? 47.215  96.850  19.997  1.00 31.73 ? 445 HOH H O   1 
HETATM 14227 O  O   . HOH FB 4 .   ? 41.566  113.085 25.110  1.00 34.77 ? 446 HOH H O   1 
HETATM 14228 O  O   . HOH FB 4 .   ? 69.871  106.350 16.486  1.00 37.75 ? 447 HOH H O   1 
HETATM 14229 O  O   . HOH FB 4 .   ? 43.005  117.977 32.594  1.00 39.66 ? 448 HOH H O   1 
HETATM 14230 O  O   . HOH FB 4 .   ? 55.705  113.743 10.912  1.00 36.44 ? 449 HOH H O   1 
HETATM 14231 O  O   . HOH FB 4 .   ? 74.905  101.273 19.504  1.00 34.57 ? 450 HOH H O   1 
HETATM 14232 O  O   . HOH FB 4 .   ? 36.647  103.819 40.714  1.00 15.20 ? 451 HOH H O   1 
HETATM 14233 O  O   . HOH FB 4 .   ? 47.307  103.839 43.467  1.00 13.39 ? 452 HOH H O   1 
HETATM 14234 O  O   . HOH FB 4 .   ? 70.358  90.703  33.580  1.00 28.12 ? 453 HOH H O   1 
HETATM 14235 O  O   . HOH FB 4 .   ? 60.500  103.771 43.746  1.00 30.11 ? 454 HOH H O   1 
HETATM 14236 O  O   . HOH FB 4 .   ? 37.747  105.930 38.557  1.00 21.64 ? 455 HOH H O   1 
HETATM 14237 O  O   . HOH FB 4 .   ? 36.650  108.245 38.316  1.00 25.36 ? 456 HOH H O   1 
HETATM 14238 O  O   . HOH FB 4 .   ? 46.543  95.433  31.877  1.00 26.44 ? 457 HOH H O   1 
HETATM 14239 O  O   . HOH FB 4 .   ? 51.128  105.988 18.107  1.00 27.66 ? 458 HOH H O   1 
HETATM 14240 O  O   . HOH FB 4 .   ? 36.638  101.477 40.900  1.00 22.84 ? 459 HOH H O   1 
HETATM 14241 O  O   . HOH FB 4 .   ? 43.183  98.770  44.206  1.00 27.21 ? 460 HOH H O   1 
HETATM 14242 O  O   . HOH GB 4 .   ? 53.256  86.324  88.669  1.00 33.30 ? 301 HOH I O   1 
HETATM 14243 O  O   . HOH GB 4 .   ? 46.563  85.344  69.917  1.00 30.06 ? 302 HOH I O   1 
HETATM 14244 O  O   . HOH GB 4 .   ? 65.090  87.589  78.490  1.00 33.28 ? 303 HOH I O   1 
HETATM 14245 O  O   . HOH GB 4 .   ? 59.183  73.588  72.978  1.00 33.01 ? 304 HOH I O   1 
HETATM 14246 O  O   . HOH GB 4 .   ? 60.905  87.663  83.972  1.00 31.91 ? 305 HOH I O   1 
HETATM 14247 O  O   . HOH GB 4 .   ? 50.226  69.420  81.590  1.00 37.37 ? 306 HOH I O   1 
HETATM 14248 O  O   . HOH GB 4 .   ? 57.874  72.211  78.244  1.00 36.76 ? 307 HOH I O   1 
HETATM 14249 O  O   . HOH GB 4 .   ? 51.036  89.220  90.109  1.00 34.40 ? 308 HOH I O   1 
HETATM 14250 O  O   . HOH GB 4 .   ? 46.699  77.797  70.442  1.00 34.58 ? 309 HOH I O   1 
HETATM 14251 O  O   . HOH GB 4 .   ? 58.198  83.626  91.521  1.00 33.96 ? 310 HOH I O   1 
HETATM 14252 O  O   . HOH GB 4 .   ? 50.637  85.686  89.939  1.00 32.78 ? 311 HOH I O   1 
HETATM 14253 O  O   . HOH GB 4 .   ? 33.905  79.032  82.791  1.00 47.74 ? 312 HOH I O   1 
HETATM 14254 O  O   . HOH GB 4 .   ? 57.256  85.844  89.539  1.00 32.29 ? 313 HOH I O   1 
HETATM 14255 O  O   . HOH GB 4 .   ? 57.750  94.053  71.197  1.00 28.40 ? 314 HOH I O   1 
HETATM 14256 O  O   . HOH GB 4 .   ? 41.816  87.005  91.310  1.00 48.21 ? 315 HOH I O   1 
HETATM 14257 O  O   . HOH GB 4 .   ? 41.899  65.248  91.492  1.00 45.18 ? 316 HOH I O   1 
HETATM 14258 O  O   . HOH GB 4 .   ? 60.048  74.682  83.798  1.00 40.05 ? 317 HOH I O   1 
HETATM 14259 O  O   . HOH GB 4 .   ? 50.973  66.277  80.719  1.00 37.00 ? 318 HOH I O   1 
HETATM 14260 O  O   . HOH GB 4 .   ? 61.065  79.394  90.200  1.00 41.97 ? 319 HOH I O   1 
HETATM 14261 O  O   . HOH GB 4 .   ? 50.903  70.067  64.107  1.00 39.15 ? 320 HOH I O   1 
HETATM 14262 O  O   . HOH GB 4 .   ? 48.476  84.923  89.109  1.00 36.90 ? 321 HOH I O   1 
HETATM 14263 O  O   . HOH GB 4 .   ? 42.169  87.547  87.900  1.00 41.97 ? 322 HOH I O   1 
HETATM 14264 O  O   . HOH GB 4 .   ? 50.027  77.549  88.214  1.00 41.63 ? 323 HOH I O   1 
HETATM 14265 O  O   . HOH GB 4 .   ? 44.891  79.463  68.825  1.00 36.77 ? 324 HOH I O   1 
HETATM 14266 O  O   . HOH GB 4 .   ? 45.558  91.722  90.769  1.00 39.77 ? 325 HOH I O   1 
HETATM 14267 O  O   . HOH GB 4 .   ? 66.940  95.033  78.529  1.00 40.16 ? 326 HOH I O   1 
HETATM 14268 O  O   . HOH GB 4 .   ? 34.823  78.631  75.565  1.00 50.84 ? 327 HOH I O   1 
HETATM 14269 O  O   . HOH GB 4 .   ? 61.089  94.127  83.110  1.00 38.28 ? 328 HOH I O   1 
HETATM 14270 O  O   . HOH GB 4 .   ? 66.209  78.046  91.734  1.00 35.46 ? 329 HOH I O   1 
HETATM 14271 O  O   . HOH GB 4 .   ? 68.646  89.615  79.746  1.00 36.69 ? 330 HOH I O   1 
HETATM 14272 O  O   . HOH GB 4 .   ? 51.477  68.618  69.585  1.00 39.55 ? 331 HOH I O   1 
HETATM 14273 O  O   . HOH GB 4 .   ? 61.092  79.220  74.356  1.00 35.96 ? 332 HOH I O   1 
HETATM 14274 O  O   . HOH GB 4 .   ? 60.086  82.697  79.121  1.00 37.69 ? 333 HOH I O   1 
HETATM 14275 O  O   . HOH GB 4 .   ? 59.556  81.051  91.462  1.00 43.89 ? 334 HOH I O   1 
HETATM 14276 O  O   . HOH GB 4 .   ? 54.333  68.241  84.117  1.00 42.54 ? 335 HOH I O   1 
HETATM 14277 O  O   . HOH GB 4 .   ? 46.653  71.648  100.813 1.00 44.45 ? 336 HOH I O   1 
HETATM 14278 O  O   . HOH GB 4 .   ? 38.624  67.903  86.024  1.00 54.01 ? 337 HOH I O   1 
HETATM 14279 O  O   . HOH GB 4 .   ? 65.299  76.463  88.970  1.00 42.64 ? 338 HOH I O   1 
HETATM 14280 O  O   . HOH GB 4 .   ? 62.488  74.118  92.654  1.00 51.25 ? 339 HOH I O   1 
HETATM 14281 O  O   . HOH GB 4 .   ? 63.266  75.253  90.188  1.00 44.97 ? 340 HOH I O   1 
HETATM 14282 O  O   . HOH GB 4 .   ? 40.130  93.741  82.701  1.00 49.10 ? 341 HOH I O   1 
HETATM 14283 O  O   . HOH GB 4 .   ? 62.475  91.218  72.021  1.00 37.12 ? 342 HOH I O   1 
HETATM 14284 O  O   . HOH GB 4 .   ? 64.584  72.222  78.138  1.00 38.81 ? 343 HOH I O   1 
HETATM 14285 O  O   . HOH GB 4 .   ? 49.946  93.936  73.854  1.00 34.50 ? 344 HOH I O   1 
HETATM 14286 O  O   . HOH GB 4 .   ? 58.878  65.850  94.068  1.00 44.31 ? 345 HOH I O   1 
HETATM 14287 O  O   . HOH GB 4 .   ? 62.812  92.851  77.778  1.00 38.00 ? 346 HOH I O   1 
HETATM 14288 O  O   . HOH GB 4 .   ? 46.023  67.962  80.000  1.00 38.64 ? 347 HOH I O   1 
HETATM 14289 O  O   . HOH GB 4 .   ? 65.629  94.385  85.286  1.00 39.89 ? 348 HOH I O   1 
HETATM 14290 O  O   . HOH GB 4 .   ? 31.868  86.725  92.891  1.00 47.29 ? 349 HOH I O   1 
HETATM 14291 O  O   . HOH GB 4 .   ? 45.852  83.044  68.303  1.00 32.56 ? 350 HOH I O   1 
HETATM 14292 O  O   . HOH GB 4 .   ? 48.932  77.296  65.434  1.00 32.12 ? 351 HOH I O   1 
HETATM 14293 O  O   . HOH GB 4 .   ? 41.858  93.589  76.828  1.00 34.73 ? 352 HOH I O   1 
HETATM 14294 O  O   . HOH HB 4 .   ? 51.305  94.987  39.814  1.00 9.19  ? 301 HOH J O   1 
HETATM 14295 O  O   . HOH HB 4 .   ? 58.355  98.199  41.028  1.00 9.92  ? 302 HOH J O   1 
HETATM 14296 O  O   . HOH HB 4 .   ? 48.849  102.741 41.617  1.00 10.51 ? 303 HOH J O   1 
HETATM 14297 O  O   . HOH HB 4 .   ? 56.496  94.326  35.934  1.00 15.69 ? 304 HOH J O   1 
HETATM 14298 O  O   . HOH HB 4 .   ? 56.873  88.281  48.118  1.00 10.12 ? 305 HOH J O   1 
HETATM 14299 O  O   . HOH HB 4 .   ? 63.779  92.590  56.256  1.00 20.39 ? 306 HOH J O   1 
HETATM 14300 O  O   . HOH HB 4 .   ? 67.303  92.276  44.551  1.00 20.92 ? 307 HOH J O   1 
HETATM 14301 O  O   . HOH HB 4 .   ? 48.581  91.813  41.713  1.00 19.63 ? 308 HOH J O   1 
HETATM 14302 O  O   . HOH HB 4 .   ? 54.598  95.971  53.950  1.00 14.90 ? 309 HOH J O   1 
HETATM 14303 O  O   . HOH HB 4 .   ? 50.842  79.730  39.108  1.00 26.58 ? 310 HOH J O   1 
HETATM 14304 O  O   . HOH HB 4 .   ? 55.313  90.353  38.888  1.00 20.66 ? 311 HOH J O   1 
HETATM 14305 O  O   . HOH HB 4 .   ? 50.545  102.660 44.529  1.00 15.42 ? 312 HOH J O   1 
HETATM 14306 O  O   . HOH HB 4 .   ? 61.069  85.904  43.651  1.00 16.55 ? 313 HOH J O   1 
HETATM 14307 O  O   . HOH HB 4 .   ? 40.431  83.918  47.318  1.00 20.10 ? 314 HOH J O   1 
HETATM 14308 O  O   . HOH HB 4 .   ? 53.863  72.215  61.802  1.00 31.10 ? 315 HOH J O   1 
HETATM 14309 O  O   . HOH HB 4 .   ? 52.674  71.201  46.262  1.00 27.00 ? 316 HOH J O   1 
HETATM 14310 O  O   . HOH HB 4 .   ? 57.189  66.459  64.097  1.00 51.47 ? 317 HOH J O   1 
HETATM 14311 O  O   . HOH HB 4 .   ? 65.086  91.424  54.321  1.00 19.44 ? 318 HOH J O   1 
HETATM 14312 O  O   . HOH HB 4 .   ? 48.562  74.512  44.333  1.00 27.82 ? 319 HOH J O   1 
HETATM 14313 O  O   . HOH HB 4 .   ? 48.113  101.514 44.806  1.00 18.39 ? 320 HOH J O   1 
HETATM 14314 O  O   . HOH HB 4 .   ? 37.220  78.428  44.622  1.00 23.75 ? 321 HOH J O   1 
HETATM 14315 O  O   . HOH HB 4 .   ? 42.837  93.443  54.547  1.00 21.18 ? 322 HOH J O   1 
HETATM 14316 O  O   . HOH HB 4 .   ? 65.167  81.547  49.565  1.00 26.45 ? 323 HOH J O   1 
HETATM 14317 O  O   . HOH HB 4 .   ? 45.562  85.268  64.498  1.00 30.60 ? 324 HOH J O   1 
HETATM 14318 O  O   . HOH HB 4 .   ? 51.366  88.289  38.821  1.00 16.09 ? 325 HOH J O   1 
HETATM 14319 O  O   . HOH HB 4 .   ? 48.172  79.725  64.304  1.00 21.86 ? 326 HOH J O   1 
HETATM 14320 O  O   . HOH HB 4 .   ? 66.980  89.296  53.269  1.00 24.03 ? 327 HOH J O   1 
HETATM 14321 O  O   . HOH HB 4 .   ? 68.274  89.779  43.164  1.00 31.66 ? 328 HOH J O   1 
HETATM 14322 O  O   . HOH HB 4 .   ? 37.862  82.929  48.271  1.00 22.59 ? 329 HOH J O   1 
HETATM 14323 O  O   . HOH HB 4 .   ? 62.017  81.013  48.586  1.00 21.43 ? 330 HOH J O   1 
HETATM 14324 O  O   . HOH HB 4 .   ? 45.699  88.289  41.041  1.00 23.94 ? 331 HOH J O   1 
HETATM 14325 O  O   . HOH HB 4 .   ? 46.685  98.738  43.308  1.00 27.82 ? 332 HOH J O   1 
HETATM 14326 O  O   . HOH HB 4 .   ? 51.359  92.510  38.353  1.00 24.05 ? 333 HOH J O   1 
HETATM 14327 O  O   . HOH HB 4 .   ? 61.174  96.253  38.491  1.00 21.06 ? 334 HOH J O   1 
HETATM 14328 O  O   . HOH HB 4 .   ? 53.631  88.122  40.374  1.00 17.09 ? 335 HOH J O   1 
HETATM 14329 O  O   . HOH HB 4 .   ? 38.119  81.198  57.785  1.00 31.33 ? 336 HOH J O   1 
HETATM 14330 O  O   . HOH HB 4 .   ? 61.590  96.712  42.454  1.00 29.44 ? 337 HOH J O   1 
HETATM 14331 O  O   . HOH HB 4 .   ? 60.932  90.421  41.785  1.00 18.59 ? 338 HOH J O   1 
HETATM 14332 O  O   . HOH HB 4 .   ? 49.846  70.340  60.767  1.00 28.68 ? 339 HOH J O   1 
HETATM 14333 O  O   . HOH HB 4 .   ? 46.127  81.507  64.849  1.00 30.52 ? 340 HOH J O   1 
HETATM 14334 O  O   . HOH HB 4 .   ? 37.569  85.246  50.026  1.00 26.64 ? 341 HOH J O   1 
HETATM 14335 O  O   . HOH HB 4 .   ? 59.171  93.969  60.772  1.00 27.25 ? 342 HOH J O   1 
HETATM 14336 O  O   . HOH HB 4 .   ? 49.896  96.086  65.613  1.00 33.03 ? 343 HOH J O   1 
HETATM 14337 O  O   . HOH HB 4 .   ? 51.978  89.295  36.702  1.00 22.48 ? 344 HOH J O   1 
HETATM 14338 O  O   . HOH HB 4 .   ? 58.436  93.516  65.751  1.00 25.55 ? 345 HOH J O   1 
HETATM 14339 O  O   . HOH HB 4 .   ? 50.673  90.765  40.508  1.00 21.13 ? 346 HOH J O   1 
HETATM 14340 O  O   . HOH HB 4 .   ? 36.941  77.508  42.129  1.00 27.82 ? 347 HOH J O   1 
HETATM 14341 O  O   . HOH HB 4 .   ? 59.147  98.675  52.082  1.00 24.45 ? 348 HOH J O   1 
HETATM 14342 O  O   . HOH HB 4 .   ? 46.281  91.166  40.485  1.00 28.09 ? 349 HOH J O   1 
HETATM 14343 O  O   . HOH HB 4 .   ? 59.909  98.749  38.874  1.00 17.92 ? 350 HOH J O   1 
HETATM 14344 O  O   . HOH HB 4 .   ? 50.910  92.023  50.751  1.00 20.09 ? 351 HOH J O   1 
HETATM 14345 O  O   . HOH HB 4 .   ? 51.645  81.783  37.518  1.00 25.96 ? 352 HOH J O   1 
HETATM 14346 O  O   . HOH HB 4 .   ? 59.277  83.823  43.026  1.00 21.26 ? 353 HOH J O   1 
HETATM 14347 O  O   . HOH HB 4 .   ? 50.529  95.101  67.798  1.00 32.66 ? 354 HOH J O   1 
HETATM 14348 O  O   . HOH HB 4 .   ? 60.519  77.650  46.986  1.00 24.59 ? 355 HOH J O   1 
HETATM 14349 O  O   . HOH HB 4 .   ? 37.858  79.686  41.594  1.00 26.90 ? 356 HOH J O   1 
HETATM 14350 O  O   . HOH HB 4 .   ? 40.735  86.304  46.045  1.00 21.28 ? 357 HOH J O   1 
HETATM 14351 O  O   . HOH HB 4 .   ? 50.742  76.816  45.746  1.00 25.68 ? 358 HOH J O   1 
HETATM 14352 O  O   . HOH HB 4 .   ? 67.620  73.636  57.274  1.00 38.68 ? 359 HOH J O   1 
HETATM 14353 O  O   . HOH HB 4 .   ? 67.080  80.414  57.285  1.00 26.64 ? 360 HOH J O   1 
HETATM 14354 O  O   . HOH HB 4 .   ? 44.910  93.761  39.227  1.00 36.61 ? 361 HOH J O   1 
HETATM 14355 O  O   . HOH HB 4 .   ? 58.741  72.191  47.050  1.00 29.54 ? 362 HOH J O   1 
HETATM 14356 O  O   . HOH HB 4 .   ? 56.199  81.494  46.319  1.00 21.24 ? 363 HOH J O   1 
HETATM 14357 O  O   . HOH HB 4 .   ? 64.913  71.931  56.651  1.00 45.49 ? 364 HOH J O   1 
HETATM 14358 O  O   . HOH HB 4 .   ? 47.623  95.787  47.962  1.00 25.00 ? 365 HOH J O   1 
HETATM 14359 O  O   . HOH HB 4 .   ? 56.450  71.491  60.893  1.00 28.45 ? 366 HOH J O   1 
HETATM 14360 O  O   . HOH HB 4 .   ? 56.874  83.875  44.141  1.00 21.39 ? 367 HOH J O   1 
HETATM 14361 O  O   . HOH HB 4 .   ? 51.627  71.280  49.881  1.00 31.04 ? 368 HOH J O   1 
HETATM 14362 O  O   . HOH HB 4 .   ? 67.125  65.846  53.991  1.00 43.60 ? 369 HOH J O   1 
HETATM 14363 O  O   . HOH HB 4 .   ? 35.574  81.054  45.217  1.00 24.68 ? 370 HOH J O   1 
HETATM 14364 O  O   . HOH HB 4 .   ? 52.323  105.275 49.473  1.00 32.58 ? 371 HOH J O   1 
HETATM 14365 O  O   . HOH HB 4 .   ? 35.904  81.149  42.762  1.00 32.40 ? 372 HOH J O   1 
HETATM 14366 O  O   . HOH HB 4 .   ? 35.983  72.267  44.461  1.00 33.44 ? 373 HOH J O   1 
HETATM 14367 O  O   . HOH HB 4 .   ? 50.268  108.422 45.881  1.00 36.12 ? 374 HOH J O   1 
HETATM 14368 O  O   . HOH HB 4 .   ? 53.724  87.367  35.423  1.00 26.65 ? 375 HOH J O   1 
HETATM 14369 O  O   . HOH HB 4 .   ? 49.320  70.195  50.696  1.00 33.20 ? 376 HOH J O   1 
HETATM 14370 O  O   . HOH HB 4 .   ? 42.403  84.648  41.997  1.00 27.49 ? 377 HOH J O   1 
HETATM 14371 O  O   . HOH HB 4 .   ? 41.780  70.102  43.422  1.00 37.10 ? 378 HOH J O   1 
HETATM 14372 O  O   . HOH HB 4 .   ? 38.414  83.847  54.331  1.00 23.53 ? 379 HOH J O   1 
HETATM 14373 O  O   . HOH HB 4 .   ? 68.102  84.392  61.756  1.00 25.69 ? 380 HOH J O   1 
HETATM 14374 O  O   . HOH HB 4 .   ? 48.778  82.640  37.237  1.00 33.20 ? 381 HOH J O   1 
HETATM 14375 O  O   . HOH HB 4 .   ? 38.763  74.946  48.292  1.00 32.57 ? 382 HOH J O   1 
HETATM 14376 O  O   . HOH HB 4 .   ? 69.327  88.230  54.885  1.00 35.66 ? 383 HOH J O   1 
HETATM 14377 O  O   . HOH HB 4 .   ? 62.676  91.035  35.160  1.00 30.39 ? 384 HOH J O   1 
HETATM 14378 O  O   . HOH HB 4 .   ? 63.300  93.885  44.841  1.00 25.48 ? 385 HOH J O   1 
HETATM 14379 O  O   . HOH HB 4 .   ? 39.542  70.577  54.717  1.00 40.32 ? 386 HOH J O   1 
HETATM 14380 O  O   . HOH HB 4 .   ? 52.983  68.613  66.238  1.00 39.73 ? 387 HOH J O   1 
HETATM 14381 O  O   . HOH HB 4 .   ? 44.091  95.107  53.156  1.00 33.48 ? 388 HOH J O   1 
HETATM 14382 O  O   . HOH HB 4 .   ? 65.959  100.259 50.491  1.00 31.42 ? 389 HOH J O   1 
HETATM 14383 O  O   . HOH HB 4 .   ? 65.829  79.261  47.796  1.00 34.81 ? 390 HOH J O   1 
HETATM 14384 O  O   . HOH HB 4 .   ? 41.580  86.827  42.704  1.00 37.91 ? 391 HOH J O   1 
HETATM 14385 O  O   . HOH HB 4 .   ? 54.093  108.264 43.479  1.00 24.13 ? 392 HOH J O   1 
HETATM 14386 O  O   . HOH HB 4 .   ? 70.719  79.159  54.429  1.00 39.99 ? 393 HOH J O   1 
HETATM 14387 O  O   . HOH HB 4 .   ? 48.462  94.354  40.679  1.00 17.72 ? 394 HOH J O   1 
HETATM 14388 O  O   . HOH HB 4 .   ? 46.705  84.489  38.826  1.00 25.46 ? 395 HOH J O   1 
HETATM 14389 O  O   . HOH HB 4 .   ? 47.224  87.271  63.706  1.00 27.91 ? 396 HOH J O   1 
HETATM 14390 O  O   . HOH HB 4 .   ? 46.252  94.519  53.638  1.00 26.25 ? 397 HOH J O   1 
HETATM 14391 O  O   . HOH HB 4 .   ? 51.024  99.638  52.498  1.00 37.34 ? 398 HOH J O   1 
HETATM 14392 O  O   . HOH HB 4 .   ? 43.319  84.662  63.029  1.00 29.54 ? 399 HOH J O   1 
HETATM 14393 O  O   . HOH HB 4 .   ? 40.405  91.505  59.985  1.00 42.27 ? 400 HOH J O   1 
HETATM 14394 O  O   . HOH IB 4 .   ? 48.299  38.064  6.865   1.00 53.56 ? 301 HOH K O   1 
HETATM 14395 O  O   . HOH IB 4 .   ? 75.708  55.155  21.687  1.00 40.08 ? 302 HOH K O   1 
HETATM 14396 O  O   . HOH IB 4 .   ? 60.834  59.746  14.272  1.00 33.52 ? 303 HOH K O   1 
HETATM 14397 O  O   . HOH IB 4 .   ? 83.056  60.038  11.821  1.00 47.96 ? 304 HOH K O   1 
HETATM 14398 O  O   . HOH IB 4 .   ? 82.409  52.350  25.656  1.00 41.18 ? 305 HOH K O   1 
HETATM 14399 O  O   . HOH IB 4 .   ? 69.906  42.163  14.732  1.00 48.59 ? 306 HOH K O   1 
HETATM 14400 O  O   . HOH IB 4 .   ? 76.852  62.806  5.092   1.00 37.09 ? 307 HOH K O   1 
HETATM 14401 O  O   . HOH IB 4 .   ? 63.044  42.810  5.807   1.00 57.79 ? 308 HOH K O   1 
HETATM 14402 O  O   . HOH IB 4 .   ? 77.721  45.042  9.982   1.00 45.69 ? 309 HOH K O   1 
HETATM 14403 O  O   . HOH IB 4 .   ? 60.227  62.375  12.647  1.00 38.49 ? 310 HOH K O   1 
HETATM 14404 O  O   . HOH IB 4 .   ? 57.149  68.160  7.182   1.00 37.76 ? 311 HOH K O   1 
HETATM 14405 O  O   . HOH IB 4 .   ? 78.664  64.045  7.028   1.00 39.35 ? 312 HOH K O   1 
HETATM 14406 O  O   . HOH IB 4 .   ? 75.594  66.484  8.831   1.00 45.44 ? 313 HOH K O   1 
HETATM 14407 O  O   . HOH IB 4 .   ? 76.490  47.158  21.488  1.00 45.48 ? 314 HOH K O   1 
HETATM 14408 O  O   . HOH IB 4 .   ? 78.088  49.992  15.521  1.00 44.06 ? 315 HOH K O   1 
HETATM 14409 O  O   . HOH IB 4 .   ? 65.484  73.966  7.022   1.00 35.73 ? 316 HOH K O   1 
HETATM 14410 O  O   . HOH IB 4 .   ? 53.686  54.880  11.621  1.00 50.83 ? 317 HOH K O   1 
HETATM 14411 O  O   . HOH IB 4 .   ? 72.958  58.563  17.099  1.00 33.68 ? 318 HOH K O   1 
HETATM 14412 O  O   . HOH IB 4 .   ? 62.764  68.112  10.866  1.00 29.48 ? 319 HOH K O   1 
HETATM 14413 O  O   . HOH IB 4 .   ? 51.241  44.550  -0.570  1.00 71.33 ? 320 HOH K O   1 
HETATM 14414 O  O   . HOH IB 4 .   ? 78.617  51.034  26.708  1.00 44.57 ? 321 HOH K O   1 
HETATM 14415 O  O   . HOH IB 4 .   ? 65.082  60.974  -4.337  1.00 47.99 ? 322 HOH K O   1 
HETATM 14416 O  O   . HOH IB 4 .   ? 57.778  60.718  11.144  1.00 44.89 ? 323 HOH K O   1 
HETATM 14417 O  O   . HOH IB 4 .   ? 59.174  43.148  13.619  1.00 57.03 ? 324 HOH K O   1 
HETATM 14418 O  O   . HOH IB 4 .   ? 65.844  45.299  25.337  1.00 44.99 ? 325 HOH K O   1 
HETATM 14419 O  O   . HOH IB 4 .   ? 59.512  65.456  11.964  1.00 37.41 ? 326 HOH K O   1 
HETATM 14420 O  O   . HOH IB 4 .   ? 70.971  44.232  6.291   1.00 48.49 ? 327 HOH K O   1 
HETATM 14421 O  O   . HOH IB 4 .   ? 79.477  56.495  5.578   1.00 45.20 ? 328 HOH K O   1 
HETATM 14422 O  O   . HOH IB 4 .   ? 62.324  64.500  8.247   1.00 44.26 ? 329 HOH K O   1 
HETATM 14423 O  O   . HOH IB 4 .   ? 63.110  52.571  20.588  1.00 42.04 ? 330 HOH K O   1 
HETATM 14424 O  O   . HOH IB 4 .   ? 79.195  62.900  11.410  1.00 45.84 ? 331 HOH K O   1 
HETATM 14425 O  O   . HOH IB 4 .   ? 73.843  57.340  24.217  1.00 46.17 ? 332 HOH K O   1 
HETATM 14426 O  O   . HOH IB 4 .   ? 61.528  41.702  13.694  1.00 54.46 ? 333 HOH K O   1 
HETATM 14427 O  O   . HOH JB 4 .   ? 52.611  82.997  34.011  1.00 18.45 ? 301 HOH L O   1 
HETATM 14428 O  O   . HOH JB 4 .   ? 54.763  71.941  32.010  1.00 31.28 ? 302 HOH L O   1 
HETATM 14429 O  O   . HOH JB 4 .   ? 61.279  82.326  26.311  1.00 22.52 ? 303 HOH L O   1 
HETATM 14430 O  O   . HOH JB 4 .   ? 63.491  83.096  32.843  1.00 21.32 ? 304 HOH L O   1 
HETATM 14431 O  O   . HOH JB 4 .   ? 50.064  78.693  34.415  1.00 23.28 ? 305 HOH L O   1 
HETATM 14432 O  O   . HOH JB 4 .   ? 68.979  70.942  6.081   1.00 33.80 ? 306 HOH L O   1 
HETATM 14433 O  O   . HOH JB 4 .   ? 61.482  78.248  9.041   1.00 28.50 ? 307 HOH L O   1 
HETATM 14434 O  O   . HOH JB 4 .   ? 71.826  76.400  40.101  1.00 37.36 ? 308 HOH L O   1 
HETATM 14435 O  O   . HOH JB 4 .   ? 54.887  82.793  33.555  1.00 18.68 ? 309 HOH L O   1 
HETATM 14436 O  O   . HOH JB 4 .   ? 57.538  78.409  43.595  1.00 18.41 ? 310 HOH L O   1 
HETATM 14437 O  O   . HOH JB 4 .   ? 55.171  84.063  42.030  1.00 18.98 ? 311 HOH L O   1 
HETATM 14438 O  O   . HOH JB 4 .   ? 62.029  80.024  39.736  1.00 22.75 ? 312 HOH L O   1 
HETATM 14439 O  O   . HOH JB 4 .   ? 71.624  76.938  34.080  1.00 26.43 ? 313 HOH L O   1 
HETATM 14440 O  O   . HOH JB 4 .   ? 56.123  83.212  36.268  1.00 23.69 ? 314 HOH L O   1 
HETATM 14441 O  O   . HOH JB 4 .   ? 48.711  90.709  18.649  1.00 36.31 ? 315 HOH L O   1 
HETATM 14442 O  O   . HOH JB 4 .   ? 76.713  70.425  25.344  1.00 36.13 ? 316 HOH L O   1 
HETATM 14443 O  O   . HOH JB 4 .   ? 69.441  82.412  38.987  1.00 30.18 ? 317 HOH L O   1 
HETATM 14444 O  O   . HOH JB 4 .   ? 53.406  87.770  15.630  1.00 29.29 ? 318 HOH L O   1 
HETATM 14445 O  O   . HOH JB 4 .   ? 48.348  80.954  30.719  1.00 25.15 ? 319 HOH L O   1 
HETATM 14446 O  O   . HOH JB 4 .   ? 60.409  77.119  31.232  1.00 22.26 ? 320 HOH L O   1 
HETATM 14447 O  O   . HOH JB 4 .   ? 70.894  81.468  28.462  1.00 34.24 ? 321 HOH L O   1 
HETATM 14448 O  O   . HOH JB 4 .   ? 58.033  80.006  45.138  1.00 22.55 ? 322 HOH L O   1 
HETATM 14449 O  O   . HOH JB 4 .   ? 62.276  86.045  22.179  1.00 26.66 ? 323 HOH L O   1 
HETATM 14450 O  O   . HOH JB 4 .   ? 45.789  77.188  24.615  1.00 35.41 ? 324 HOH L O   1 
HETATM 14451 O  O   . HOH JB 4 .   ? 68.087  80.229  40.087  1.00 25.78 ? 325 HOH L O   1 
HETATM 14452 O  O   . HOH JB 4 .   ? 53.909  83.684  37.742  1.00 22.97 ? 326 HOH L O   1 
HETATM 14453 O  O   . HOH JB 4 .   ? 66.066  84.658  24.660  1.00 30.35 ? 327 HOH L O   1 
HETATM 14454 O  O   . HOH JB 4 .   ? 61.349  87.734  41.216  1.00 26.53 ? 328 HOH L O   1 
HETATM 14455 O  O   . HOH JB 4 .   ? 61.996  82.062  37.500  1.00 28.07 ? 329 HOH L O   1 
HETATM 14456 O  O   . HOH JB 4 .   ? 66.377  87.132  23.265  1.00 39.33 ? 330 HOH L O   1 
HETATM 14457 O  O   . HOH JB 4 .   ? 70.918  79.285  33.070  1.00 29.49 ? 331 HOH L O   1 
HETATM 14458 O  O   . HOH JB 4 .   ? 54.032  89.715  17.532  1.00 30.17 ? 332 HOH L O   1 
HETATM 14459 O  O   . HOH JB 4 .   ? 55.125  85.467  39.514  1.00 23.52 ? 333 HOH L O   1 
HETATM 14460 O  O   . HOH JB 4 .   ? 51.553  80.881  35.173  1.00 23.54 ? 334 HOH L O   1 
HETATM 14461 O  O   . HOH JB 4 .   ? 57.748  55.199  24.173  1.00 40.93 ? 335 HOH L O   1 
HETATM 14462 O  O   . HOH JB 4 .   ? 61.265  76.487  7.099   1.00 28.70 ? 336 HOH L O   1 
HETATM 14463 O  O   . HOH JB 4 .   ? 45.138  76.364  19.439  1.00 30.24 ? 337 HOH L O   1 
HETATM 14464 O  O   . HOH JB 4 .   ? 72.289  74.007  33.172  1.00 35.20 ? 338 HOH L O   1 
HETATM 14465 O  O   . HOH JB 4 .   ? 61.295  67.668  13.212  1.00 28.59 ? 339 HOH L O   1 
HETATM 14466 O  O   . HOH JB 4 .   ? 68.204  62.853  35.280  1.00 34.72 ? 340 HOH L O   1 
HETATM 14467 O  O   . HOH JB 4 .   ? 47.327  81.301  14.026  1.00 32.58 ? 341 HOH L O   1 
HETATM 14468 O  O   . HOH JB 4 .   ? 76.968  80.221  18.606  1.00 36.69 ? 342 HOH L O   1 
HETATM 14469 O  O   . HOH JB 4 .   ? 57.846  63.509  19.716  1.00 42.32 ? 343 HOH L O   1 
HETATM 14470 O  O   . HOH JB 4 .   ? 63.567  75.592  8.104   1.00 34.75 ? 344 HOH L O   1 
HETATM 14471 O  O   . HOH JB 4 .   ? 42.334  86.412  14.783  1.00 40.69 ? 345 HOH L O   1 
HETATM 14472 O  O   . HOH JB 4 .   ? 74.391  81.358  17.200  1.00 34.45 ? 346 HOH L O   1 
HETATM 14473 O  O   . HOH JB 4 .   ? 75.520  76.193  24.253  1.00 34.86 ? 347 HOH L O   1 
HETATM 14474 O  O   . HOH JB 4 .   ? 44.015  81.595  17.233  1.00 37.84 ? 348 HOH L O   1 
HETATM 14475 O  O   . HOH JB 4 .   ? 44.225  82.775  23.755  1.00 33.90 ? 349 HOH L O   1 
HETATM 14476 O  O   . HOH JB 4 .   ? 59.420  67.569  33.913  1.00 31.34 ? 350 HOH L O   1 
HETATM 14477 O  O   . HOH JB 4 .   ? 70.117  71.791  34.077  1.00 22.86 ? 351 HOH L O   1 
HETATM 14478 O  O   . HOH JB 4 .   ? 48.053  67.057  20.702  1.00 42.35 ? 352 HOH L O   1 
HETATM 14479 O  O   . HOH JB 4 .   ? 57.534  87.881  37.652  1.00 31.93 ? 353 HOH L O   1 
HETATM 14480 O  O   . HOH JB 4 .   ? 69.196  69.645  33.685  1.00 26.67 ? 354 HOH L O   1 
HETATM 14481 O  O   . HOH JB 4 .   ? 71.398  65.508  21.180  1.00 35.87 ? 355 HOH L O   1 
HETATM 14482 O  O   . HOH JB 4 .   ? 50.755  87.072  29.038  1.00 26.70 ? 356 HOH L O   1 
HETATM 14483 O  O   . HOH JB 4 .   ? 77.260  73.343  26.234  1.00 42.98 ? 357 HOH L O   1 
HETATM 14484 O  O   . HOH JB 4 .   ? 67.973  60.455  28.134  1.00 38.93 ? 358 HOH L O   1 
HETATM 14485 O  O   . HOH JB 4 .   ? 75.003  71.544  10.751  1.00 42.57 ? 359 HOH L O   1 
HETATM 14486 O  O   . HOH JB 4 .   ? 62.328  68.546  38.734  1.00 25.64 ? 360 HOH L O   1 
HETATM 14487 O  O   . HOH JB 4 .   ? 54.442  54.152  22.842  1.00 56.12 ? 361 HOH L O   1 
HETATM 14488 O  O   . HOH JB 4 .   ? 69.696  80.627  12.071  1.00 42.35 ? 362 HOH L O   1 
HETATM 14489 O  O   . HOH JB 4 .   ? 60.373  83.785  13.976  1.00 36.05 ? 363 HOH L O   1 
HETATM 14490 O  O   . HOH JB 4 .   ? 76.763  81.661  25.796  1.00 35.10 ? 364 HOH L O   1 
HETATM 14491 O  O   . HOH JB 4 .   ? 71.164  60.939  26.223  1.00 39.94 ? 365 HOH L O   1 
HETATM 14492 O  O   . HOH JB 4 .   ? 69.253  79.863  8.846   1.00 39.67 ? 366 HOH L O   1 
HETATM 14493 O  O   . HOH JB 4 .   ? 44.450  68.553  13.360  1.00 43.12 ? 367 HOH L O   1 
HETATM 14494 O  O   . HOH JB 4 .   ? 46.603  77.423  21.721  1.00 30.28 ? 368 HOH L O   1 
HETATM 14495 O  O   . HOH JB 4 .   ? 64.370  78.541  39.104  1.00 23.72 ? 369 HOH L O   1 
HETATM 14496 O  O   . HOH JB 4 .   ? 57.276  62.851  31.292  1.00 36.70 ? 370 HOH L O   1 
HETATM 14497 O  O   . HOH JB 4 .   ? 66.669  64.367  31.236  1.00 32.41 ? 371 HOH L O   1 
HETATM 14498 O  O   . HOH JB 4 .   ? 44.938  89.418  10.460  1.00 39.47 ? 372 HOH L O   1 
HETATM 14499 O  O   . HOH JB 4 .   ? 58.957  65.203  14.526  1.00 34.39 ? 373 HOH L O   1 
HETATM 14500 O  O   . HOH JB 4 .   ? 50.071  88.517  22.248  1.00 32.99 ? 374 HOH L O   1 
HETATM 14501 O  O   . HOH JB 4 .   ? 73.133  63.295  33.089  1.00 36.81 ? 375 HOH L O   1 
HETATM 14502 O  O   . HOH JB 4 .   ? 49.003  84.710  28.529  1.00 26.37 ? 376 HOH L O   1 
HETATM 14503 O  O   . HOH JB 4 .   ? 59.006  78.405  10.198  1.00 31.56 ? 377 HOH L O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ALA 1   1   1   ALA ALA A . n 
A 1 2   THR 2   2   2   THR THR A . n 
A 1 3   LYS 3   3   3   LYS LYS A . n 
A 1 4   ALA 4   4   4   ALA ALA A . n 
A 1 5   VAL 5   5   5   VAL VAL A . n 
A 1 6   CYS 6   6   6   CYS CYS A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   LEU 8   8   8   LEU LEU A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  GLY 10  10  10  GLY GLY A . n 
A 1 11  ASP 11  11  11  ASP ASP A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  VAL 14  14  14  VAL VAL A . n 
A 1 15  GLN 15  15  15  GLN GLN A . n 
A 1 16  GLY 16  16  16  GLY GLY A . n 
A 1 17  ILE 17  17  17  ILE ILE A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  ASN 19  19  19  ASN ASN A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  GLU 21  21  21  GLU GLU A . n 
A 1 22  GLN 22  22  22  GLN GLN A . n 
A 1 23  LYS 23  23  23  LYS LYS A . n 
A 1 24  GLU 24  24  24  GLU GLU A . n 
A 1 25  SER 25  25  25  SER SER A . n 
A 1 26  ASN 26  26  26  ASN ASN A . n 
A 1 27  GLY 27  27  27  GLY GLY A . n 
A 1 28  PRO 28  28  28  PRO PRO A . n 
A 1 29  VAL 29  29  29  VAL VAL A . n 
A 1 30  LYS 30  30  30  LYS LYS A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  TRP 32  32  32  TRP TRP A . n 
A 1 33  GLY 33  33  33  GLY GLY A . n 
A 1 34  SER 34  34  34  SER SER A . n 
A 1 35  ILE 35  35  35  ILE ILE A . n 
A 1 36  LYS 36  36  36  LYS LYS A . n 
A 1 37  GLY 37  37  37  GLY GLY A . n 
A 1 38  LEU 38  38  38  LEU LEU A . n 
A 1 39  THR 39  39  39  THR THR A . n 
A 1 40  GLU 40  40  40  GLU GLU A . n 
A 1 41  GLY 41  41  41  GLY GLY A . n 
A 1 42  LEU 42  42  42  LEU LEU A . n 
A 1 43  HIS 43  43  43  HIS HIS A . n 
A 1 44  GLY 44  44  44  GLY GLY A . n 
A 1 45  PHE 45  45  45  PHE PHE A . n 
A 1 46  HIS 46  46  46  HIS HIS A . n 
A 1 47  VAL 47  47  47  VAL VAL A . n 
A 1 48  HIS 48  48  48  HIS HIS A . n 
A 1 49  GLU 49  49  49  GLU GLU A . n 
A 1 50  PHE 50  50  50  PHE PHE A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  THR 54  54  54  THR THR A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  GLY 56  56  56  GLY GLY A . n 
A 1 57  SER 57  57  57  SER SER A . n 
A 1 58  THR 58  58  58  THR THR A . n 
A 1 59  SER 59  59  59  SER SER A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  GLY 61  61  61  GLY GLY A . n 
A 1 62  PRO 62  62  62  PRO PRO A . n 
A 1 63  HIS 63  63  63  HIS HIS A . n 
A 1 64  PHE 64  64  64  PHE PHE A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  PRO 66  66  66  PRO PRO A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  SER 68  68  68  SER SER A . n 
A 1 69  ARG 69  69  69  ARG ARG A . n 
A 1 70  LYS 70  70  70  LYS LYS A . n 
A 1 71  HIS 71  71  71  HIS HIS A . n 
A 1 72  GLY 72  72  72  GLY GLY A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LYS 75  75  75  LYS LYS A . n 
A 1 76  ASP 76  76  76  ASP ASP A . n 
A 1 77  GLU 77  77  77  GLU GLU A . n 
A 1 78  GLU 78  78  78  GLU GLU A . n 
A 1 79  ARG 79  79  79  ARG ARG A . n 
A 1 80  HIS 80  80  80  HIS HIS A . n 
A 1 81  VAL 81  81  81  VAL VAL A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  ASP 83  83  83  ASP ASP A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  ASN 86  86  86  ASN ASN A . n 
A 1 87  VAL 87  87  87  VAL VAL A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  ASP 90  90  90  ASP ASP A . n 
A 1 91  LYS 91  91  91  LYS LYS A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  GLY 93  93  93  GLY GLY A . n 
A 1 94  VAL 94  94  94  VAL VAL A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  ASP 96  96  96  ASP ASP A . n 
A 1 97  VAL 97  97  97  VAL VAL A . n 
A 1 98  SER 98  98  98  SER SER A . n 
A 1 99  ILE 99  99  99  ILE ILE A . n 
A 1 100 GLU 100 100 100 GLU GLU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 SER 102 102 102 SER SER A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 ILE 104 104 104 ILE ILE A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 SER 107 107 107 SER SER A . n 
A 1 108 GLY 108 108 108 GLY GLY A . n 
A 1 109 ASP 109 109 109 ASP ASP A . n 
A 1 110 HIS 110 110 110 HIS HIS A . n 
A 1 111 CYS 111 111 111 CYS CYS A . n 
A 1 112 ILE 112 112 112 ILE ILE A . n 
A 1 113 ILE 113 113 113 ILE ILE A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 ARG 115 115 115 ARG ARG A . n 
A 1 116 THR 116 116 116 THR THR A . n 
A 1 117 LEU 117 117 117 LEU LEU A . n 
A 1 118 VAL 118 118 118 VAL VAL A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 HIS 120 120 120 HIS HIS A . n 
A 1 121 GLU 121 121 121 GLU GLU A . n 
A 1 122 LYS 122 122 122 LYS LYS A . n 
A 1 123 ALA 123 123 123 ALA ALA A . n 
A 1 124 ASP 124 124 124 ASP ASP A . n 
A 1 125 ASP 125 125 125 ASP ASP A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 GLY 127 127 127 GLY GLY A . n 
A 1 128 LYS 128 128 128 LYS LYS A . n 
A 1 129 GLY 129 129 129 GLY GLY A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ASN 131 131 131 ASN ASN A . n 
A 1 132 GLU 132 132 132 GLU GLU A . n 
A 1 133 GLU 133 133 133 GLU GLU A . n 
A 1 134 SER 134 134 134 SER SER A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 LYS 136 136 136 LYS LYS A . n 
A 1 137 THR 137 137 137 THR THR A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 ASN 139 139 139 ASN ASN A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 GLY 141 141 141 GLY GLY A . n 
A 1 142 SER 142 142 142 SER SER A . n 
A 1 143 ARG 143 143 143 ARG ARG A . n 
A 1 144 LEU 144 144 144 LEU LEU A . n 
A 1 145 ALA 145 145 145 ALA ALA A . n 
A 1 146 CYS 146 146 146 CYS CYS A . n 
A 1 147 GLY 147 147 147 GLY GLY A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 ILE 149 149 149 ILE ILE A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 ILE 151 151 151 ILE ILE A . n 
A 1 152 ALA 152 152 152 ALA ALA A . n 
A 1 153 GLN 153 153 153 GLN GLN A . n 
B 1 1   ALA 1   1   1   ALA ALA B . n 
B 1 2   THR 2   2   2   THR THR B . n 
B 1 3   LYS 3   3   3   LYS LYS B . n 
B 1 4   ALA 4   4   4   ALA ALA B . n 
B 1 5   VAL 5   5   5   VAL VAL B . n 
B 1 6   CYS 6   6   6   CYS CYS B . n 
B 1 7   VAL 7   7   7   VAL VAL B . n 
B 1 8   LEU 8   8   8   LEU LEU B . n 
B 1 9   LYS 9   9   9   LYS LYS B . n 
B 1 10  GLY 10  10  10  GLY GLY B . n 
B 1 11  ASP 11  11  11  ASP ASP B . n 
B 1 12  GLY 12  12  12  GLY GLY B . n 
B 1 13  PRO 13  13  13  PRO PRO B . n 
B 1 14  VAL 14  14  14  VAL VAL B . n 
B 1 15  GLN 15  15  15  GLN GLN B . n 
B 1 16  GLY 16  16  16  GLY GLY B . n 
B 1 17  ILE 17  17  17  ILE ILE B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  ASN 19  19  19  ASN ASN B . n 
B 1 20  PHE 20  20  20  PHE PHE B . n 
B 1 21  GLU 21  21  21  GLU GLU B . n 
B 1 22  GLN 22  22  22  GLN GLN B . n 
B 1 23  LYS 23  23  23  LYS LYS B . n 
B 1 24  GLU 24  24  24  GLU GLU B . n 
B 1 25  SER 25  25  25  SER SER B . n 
B 1 26  ASN 26  26  26  ASN ASN B . n 
B 1 27  GLY 27  27  27  GLY GLY B . n 
B 1 28  PRO 28  28  28  PRO PRO B . n 
B 1 29  VAL 29  29  29  VAL VAL B . n 
B 1 30  LYS 30  30  30  LYS LYS B . n 
B 1 31  VAL 31  31  31  VAL VAL B . n 
B 1 32  TRP 32  32  32  TRP TRP B . n 
B 1 33  GLY 33  33  33  GLY GLY B . n 
B 1 34  SER 34  34  34  SER SER B . n 
B 1 35  ILE 35  35  35  ILE ILE B . n 
B 1 36  LYS 36  36  36  LYS LYS B . n 
B 1 37  GLY 37  37  37  GLY GLY B . n 
B 1 38  LEU 38  38  38  LEU LEU B . n 
B 1 39  THR 39  39  39  THR THR B . n 
B 1 40  GLU 40  40  40  GLU GLU B . n 
B 1 41  GLY 41  41  41  GLY GLY B . n 
B 1 42  LEU 42  42  42  LEU LEU B . n 
B 1 43  HIS 43  43  43  HIS HIS B . n 
B 1 44  GLY 44  44  44  GLY GLY B . n 
B 1 45  PHE 45  45  45  PHE PHE B . n 
B 1 46  HIS 46  46  46  HIS HIS B . n 
B 1 47  VAL 47  47  47  VAL VAL B . n 
B 1 48  HIS 48  48  48  HIS HIS B . n 
B 1 49  GLU 49  49  49  GLU GLU B . n 
B 1 50  PHE 50  50  50  PHE PHE B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ASP 52  52  52  ASP ASP B . n 
B 1 53  ASN 53  53  53  ASN ASN B . n 
B 1 54  THR 54  54  54  THR THR B . n 
B 1 55  ALA 55  55  55  ALA ALA B . n 
B 1 56  GLY 56  56  56  GLY GLY B . n 
B 1 57  SER 57  57  57  SER SER 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   ?   ?   ?   C . n 
C 1 2   THR 2   2   2   THR THR C . n 
C 1 3   LYS 3   3   3   LYS LYS C . n 
C 1 4   ALA 4   4   4   ALA ALA C . n 
C 1 5   VAL 5   5   5   VAL VAL C . n 
C 1 6   CYS 6   6   6   CYS CYS C . n 
C 1 7   VAL 7   7   7   VAL VAL C . n 
C 1 8   LEU 8   8   8   LEU LEU C . n 
C 1 9   LYS 9   9   9   LYS LYS C . n 
C 1 10  GLY 10  10  10  GLY GLY C . n 
C 1 11  ASP 11  11  11  ASP ASP C . n 
C 1 12  GLY 12  12  12  GLY GLY C . n 
C 1 13  PRO 13  13  13  PRO PRO C . n 
C 1 14  VAL 14  14  14  VAL VAL C . n 
C 1 15  GLN 15  15  15  GLN GLN C . n 
C 1 16  GLY 16  16  16  GLY GLY C . n 
C 1 17  ILE 17  17  17  ILE ILE C . n 
C 1 18  ILE 18  18  18  ILE ILE C . n 
C 1 19  ASN 19  19  19  ASN ASN C . n 
C 1 20  PHE 20  20  20  PHE PHE C . n 
C 1 21  GLU 21  21  21  GLU GLU C . n 
C 1 22  GLN 22  22  22  GLN GLN C . n 
C 1 23  LYS 23  23  23  LYS LYS C . n 
C 1 24  GLU 24  24  24  GLU GLU C . n 
C 1 25  SER 25  25  25  SER SER C . n 
C 1 26  ASN 26  26  26  ASN ASN C . n 
C 1 27  GLY 27  27  27  GLY GLY C . n 
C 1 28  PRO 28  28  28  PRO PRO C . n 
C 1 29  VAL 29  29  29  VAL VAL C . n 
C 1 30  LYS 30  30  30  LYS LYS C . n 
C 1 31  VAL 31  31  31  VAL VAL C . n 
C 1 32  TRP 32  32  32  TRP TRP C . n 
C 1 33  GLY 33  33  33  GLY GLY C . n 
C 1 34  SER 34  34  34  SER SER C . n 
C 1 35  ILE 35  35  35  ILE ILE C . n 
C 1 36  LYS 36  36  36  LYS LYS C . n 
C 1 37  GLY 37  37  37  GLY GLY C . n 
C 1 38  LEU 38  38  38  LEU LEU C . n 
C 1 39  THR 39  39  39  THR THR C . n 
C 1 40  GLU 40  40  40  GLU GLU C . n 
C 1 41  GLY 41  41  41  GLY GLY C . n 
C 1 42  LEU 42  42  42  LEU LEU C . n 
C 1 43  HIS 43  43  43  HIS HIS C . n 
C 1 44  GLY 44  44  44  GLY GLY C . n 
C 1 45  PHE 45  45  45  PHE PHE C . n 
C 1 46  HIS 46  46  46  HIS HIS C . n 
C 1 47  VAL 47  47  47  VAL VAL C . n 
C 1 48  HIS 48  48  48  HIS HIS C . n 
C 1 49  GLU 49  49  49  GLU GLU C . n 
C 1 50  PHE 50  50  50  PHE PHE C . n 
C 1 51  GLY 51  51  51  GLY GLY C . n 
C 1 52  ASP 52  52  52  ASP ASP C . n 
C 1 53  ASN 53  53  53  ASN ASN C . n 
C 1 54  THR 54  54  54  THR THR C . n 
C 1 55  ALA 55  55  55  ALA ALA C . n 
C 1 56  GLY 56  56  56  GLY GLY C . n 
C 1 57  SER 57  57  57  SER SER 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  68  SER SER C . n 
C 1 69  ARG 69  69  69  ARG ARG C . n 
C 1 70  LYS 70  70  70  LYS LYS C . n 
C 1 71  HIS 71  71  71  HIS HIS C . n 
C 1 72  GLY 72  72  72  GLY GLY C . n 
C 1 73  GLY 73  73  73  GLY GLY C . n 
C 1 74  PRO 74  74  74  PRO PRO C . n 
C 1 75  LYS 75  75  75  LYS LYS C . n 
C 1 76  ASP 76  76  76  ASP ASP C . n 
C 1 77  GLU 77  77  77  GLU GLU C . n 
C 1 78  GLU 78  78  78  GLU GLU C . n 
C 1 79  ARG 79  79  79  ARG ARG C . n 
C 1 80  HIS 80  80  80  HIS HIS C . n 
C 1 81  VAL 81  81  81  VAL VAL C . n 
C 1 82  GLY 82  82  82  GLY GLY C . n 
C 1 83  ASP 83  83  83  ASP ASP C . n 
C 1 84  LEU 84  84  84  LEU LEU C . n 
C 1 85  GLY 85  85  85  GLY GLY C . n 
C 1 86  ASN 86  86  86  ASN ASN C . n 
C 1 87  VAL 87  87  87  VAL VAL C . n 
C 1 88  THR 88  88  88  THR THR C . n 
C 1 89  ALA 89  89  89  ALA ALA C . n 
C 1 90  ASP 90  90  90  ASP ASP C . n 
C 1 91  LYS 91  91  91  LYS LYS C . n 
C 1 92  ASP 92  92  92  ASP ASP C . n 
C 1 93  GLY 93  93  93  GLY GLY C . n 
C 1 94  VAL 94  94  94  VAL VAL C . n 
C 1 95  ALA 95  95  95  ALA ALA C . n 
C 1 96  ASP 96  96  96  ASP ASP C . n 
C 1 97  VAL 97  97  97  VAL VAL C . n 
C 1 98  SER 98  98  98  SER SER C . n 
C 1 99  ILE 99  99  99  ILE ILE C . n 
C 1 100 GLU 100 100 100 GLU GLU C . n 
C 1 101 ASP 101 101 101 ASP ASP C . n 
C 1 102 SER 102 102 102 SER SER C . n 
C 1 103 VAL 103 103 103 VAL VAL C . n 
C 1 104 ILE 104 104 104 ILE ILE C . n 
C 1 105 SER 105 105 105 SER SER C . n 
C 1 106 LEU 106 106 106 LEU LEU C . n 
C 1 107 SER 107 107 107 SER SER C . n 
C 1 108 GLY 108 108 108 GLY GLY C . n 
C 1 109 ASP 109 109 109 ASP ASP C . n 
C 1 110 HIS 110 110 110 HIS HIS C . n 
C 1 111 CYS 111 111 111 CYS CYS C . n 
C 1 112 ILE 112 112 112 ILE ILE C . n 
C 1 113 ILE 113 113 113 ILE ILE C . n 
C 1 114 GLY 114 114 114 GLY GLY C . n 
C 1 115 ARG 115 115 115 ARG ARG C . n 
C 1 116 THR 116 116 116 THR THR C . n 
C 1 117 LEU 117 117 117 LEU LEU C . n 
C 1 118 VAL 118 118 118 VAL VAL C . n 
C 1 119 VAL 119 119 119 VAL VAL C . n 
C 1 120 HIS 120 120 120 HIS HIS C . n 
C 1 121 GLU 121 121 121 GLU GLU C . n 
C 1 122 LYS 122 122 122 LYS LYS C . n 
C 1 123 ALA 123 123 123 ALA ALA C . n 
C 1 124 ASP 124 124 124 ASP ASP C . n 
C 1 125 ASP 125 125 125 ASP ASP C . n 
C 1 126 LEU 126 126 126 LEU LEU C . n 
C 1 127 GLY 127 127 127 GLY GLY C . n 
C 1 128 LYS 128 128 128 LYS LYS C . n 
C 1 129 GLY 129 129 129 GLY GLY C . n 
C 1 130 GLY 130 130 130 GLY GLY C . n 
C 1 131 ASN 131 131 131 ASN ASN C . n 
C 1 132 GLU 132 132 132 GLU GLU C . n 
C 1 133 GLU 133 133 133 GLU GLU C . n 
C 1 134 SER 134 134 134 SER SER C . n 
C 1 135 THR 135 135 135 THR THR C . n 
C 1 136 LYS 136 136 136 LYS LYS C . n 
C 1 137 THR 137 137 137 THR THR C . n 
C 1 138 GLY 138 138 138 GLY GLY C . n 
C 1 139 ASN 139 139 139 ASN ASN C . n 
C 1 140 ALA 140 140 140 ALA ALA C . n 
C 1 141 GLY 141 141 141 GLY GLY C . n 
C 1 142 SER 142 142 142 SER SER C . n 
C 1 143 ARG 143 143 143 ARG ARG C . n 
C 1 144 LEU 144 144 144 LEU LEU C . n 
C 1 145 ALA 145 145 145 ALA ALA C . n 
C 1 146 CYS 146 146 146 CYS CYS C . n 
C 1 147 GLY 147 147 147 GLY GLY C . n 
C 1 148 VAL 148 148 148 VAL VAL C . n 
C 1 149 ILE 149 149 149 ILE ILE C . n 
C 1 150 GLY 150 150 150 GLY GLY C . n 
C 1 151 ILE 151 151 151 ILE ILE C . n 
C 1 152 ALA 152 152 152 ALA ALA C . n 
C 1 153 GLN 153 153 153 GLN GLN C . n 
D 1 1   ALA 1   1   1   ALA ALA D . n 
D 1 2   THR 2   2   2   THR THR D . n 
D 1 3   LYS 3   3   3   LYS LYS D . n 
D 1 4   ALA 4   4   4   ALA ALA D . n 
D 1 5   VAL 5   5   5   VAL VAL D . n 
D 1 6   CYS 6   6   6   CYS CYS D . n 
D 1 7   VAL 7   7   7   VAL VAL D . n 
D 1 8   LEU 8   8   8   LEU LEU D . n 
D 1 9   LYS 9   9   9   LYS LYS D . n 
D 1 10  GLY 10  10  10  GLY GLY D . n 
D 1 11  ASP 11  11  11  ASP ASP D . n 
D 1 12  GLY 12  12  12  GLY GLY D . n 
D 1 13  PRO 13  13  13  PRO PRO D . n 
D 1 14  VAL 14  14  14  VAL VAL D . n 
D 1 15  GLN 15  15  15  GLN GLN D . n 
D 1 16  GLY 16  16  16  GLY GLY D . n 
D 1 17  ILE 17  17  17  ILE ILE D . n 
D 1 18  ILE 18  18  18  ILE ILE D . n 
D 1 19  ASN 19  19  19  ASN ASN D . n 
D 1 20  PHE 20  20  20  PHE PHE D . n 
D 1 21  GLU 21  21  21  GLU GLU D . n 
D 1 22  GLN 22  22  22  GLN GLN D . n 
D 1 23  LYS 23  23  23  LYS LYS D . n 
D 1 24  GLU 24  24  24  GLU GLU D . n 
D 1 25  SER 25  25  25  SER SER D . n 
D 1 26  ASN 26  26  26  ASN ASN D . n 
D 1 27  GLY 27  27  27  GLY GLY D . n 
D 1 28  PRO 28  28  28  PRO PRO D . n 
D 1 29  VAL 29  29  29  VAL VAL D . n 
D 1 30  LYS 30  30  30  LYS LYS D . n 
D 1 31  VAL 31  31  31  VAL VAL D . n 
D 1 32  TRP 32  32  32  TRP TRP D . n 
D 1 33  GLY 33  33  33  GLY GLY D . n 
D 1 34  SER 34  34  34  SER SER D . n 
D 1 35  ILE 35  35  35  ILE ILE D . n 
D 1 36  LYS 36  36  36  LYS LYS D . n 
D 1 37  GLY 37  37  37  GLY GLY D . n 
D 1 38  LEU 38  38  38  LEU LEU D . n 
D 1 39  THR 39  39  39  THR THR D . n 
D 1 40  GLU 40  40  40  GLU GLU D . n 
D 1 41  GLY 41  41  41  GLY GLY D . n 
D 1 42  LEU 42  42  42  LEU LEU D . n 
D 1 43  HIS 43  43  43  HIS HIS D . n 
D 1 44  GLY 44  44  44  GLY GLY D . n 
D 1 45  PHE 45  45  45  PHE PHE D . n 
D 1 46  HIS 46  46  46  HIS HIS D . n 
D 1 47  VAL 47  47  47  VAL VAL D . n 
D 1 48  HIS 48  48  48  HIS HIS D . n 
D 1 49  GLU 49  49  49  GLU GLU D . n 
D 1 50  PHE 50  50  50  PHE PHE D . n 
D 1 51  GLY 51  51  51  GLY GLY D . n 
D 1 52  ASP 52  52  52  ASP ASP D . n 
D 1 53  ASN 53  53  53  ASN ASN D . n 
D 1 54  THR 54  54  54  THR THR D . n 
D 1 55  ALA 55  55  55  ALA ALA D . n 
D 1 56  GLY 56  56  56  GLY GLY D . n 
D 1 57  SER 57  57  57  SER SER 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  67  LEU LEU D . n 
D 1 68  SER 68  68  68  SER SER D . n 
D 1 69  ARG 69  69  69  ARG ARG D . n 
D 1 70  LYS 70  70  70  LYS LYS D . n 
D 1 71  HIS 71  71  71  HIS HIS D . n 
D 1 72  GLY 72  72  72  GLY GLY D . n 
D 1 73  GLY 73  73  73  GLY GLY D . n 
D 1 74  PRO 74  74  74  PRO PRO D . n 
D 1 75  LYS 75  75  75  LYS LYS D . n 
D 1 76  ASP 76  76  76  ASP ASP D . n 
D 1 77  GLU 77  77  77  GLU GLU D . n 
D 1 78  GLU 78  78  78  GLU GLU D . n 
D 1 79  ARG 79  79  79  ARG ARG D . n 
D 1 80  HIS 80  80  80  HIS HIS D . n 
D 1 81  VAL 81  81  81  VAL VAL D . n 
D 1 82  GLY 82  82  82  GLY GLY D . n 
D 1 83  ASP 83  83  83  ASP ASP D . n 
D 1 84  LEU 84  84  84  LEU LEU D . n 
D 1 85  GLY 85  85  85  GLY GLY D . n 
D 1 86  ASN 86  86  86  ASN ASN D . n 
D 1 87  VAL 87  87  87  VAL VAL D . n 
D 1 88  THR 88  88  88  THR THR D . n 
D 1 89  ALA 89  89  89  ALA ALA D . n 
D 1 90  ASP 90  90  90  ASP ASP D . n 
D 1 91  LYS 91  91  91  LYS LYS D . n 
D 1 92  ASP 92  92  92  ASP ASP D . n 
D 1 93  GLY 93  93  93  GLY GLY D . n 
D 1 94  VAL 94  94  94  VAL VAL D . n 
D 1 95  ALA 95  95  95  ALA ALA D . n 
D 1 96  ASP 96  96  96  ASP ASP D . n 
D 1 97  VAL 97  97  97  VAL VAL D . n 
D 1 98  SER 98  98  98  SER SER D . n 
D 1 99  ILE 99  99  99  ILE ILE D . n 
D 1 100 GLU 100 100 100 GLU GLU D . n 
D 1 101 ASP 101 101 101 ASP ASP D . n 
D 1 102 SER 102 102 102 SER SER D . n 
D 1 103 VAL 103 103 103 VAL VAL D . n 
D 1 104 ILE 104 104 104 ILE ILE D . n 
D 1 105 SER 105 105 105 SER SER D . n 
D 1 106 LEU 106 106 106 LEU LEU D . n 
D 1 107 SER 107 107 107 SER SER D . n 
D 1 108 GLY 108 108 108 GLY GLY D . n 
D 1 109 ASP 109 109 109 ASP ASP D . n 
D 1 110 HIS 110 110 110 HIS HIS D . n 
D 1 111 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 125 125 125 ASP ASP D . n 
D 1 126 LEU 126 126 126 LEU LEU D . n 
D 1 127 GLY 127 127 127 GLY GLY D . n 
D 1 128 LYS 128 128 128 LYS LYS D . n 
D 1 129 GLY 129 129 129 GLY GLY D . n 
D 1 130 GLY 130 130 130 GLY GLY D . n 
D 1 131 ASN 131 131 131 ASN ASN D . n 
D 1 132 GLU 132 132 132 GLU GLU D . n 
D 1 133 GLU 133 133 133 GLU GLU D . n 
D 1 134 SER 134 134 134 SER SER D . n 
D 1 135 THR 135 135 135 THR THR D . n 
D 1 136 LYS 136 136 136 LYS LYS D . n 
D 1 137 THR 137 137 137 THR THR D . n 
D 1 138 GLY 138 138 138 GLY GLY D . n 
D 1 139 ASN 139 139 139 ASN ASN D . n 
D 1 140 ALA 140 140 140 ALA ALA D . n 
D 1 141 GLY 141 141 141 GLY GLY 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 
E 1 1   ALA 1   1   ?   ?   ?   E . n 
E 1 2   THR 2   2   2   THR THR E . n 
E 1 3   LYS 3   3   3   LYS LYS E . n 
E 1 4   ALA 4   4   4   ALA ALA E . n 
E 1 5   VAL 5   5   5   VAL VAL E . n 
E 1 6   CYS 6   6   6   CYS CYS E . n 
E 1 7   VAL 7   7   7   VAL VAL E . n 
E 1 8   LEU 8   8   8   LEU LEU E . n 
E 1 9   LYS 9   9   9   LYS LYS E . n 
E 1 10  GLY 10  10  10  GLY GLY E . n 
E 1 11  ASP 11  11  11  ASP ASP E . n 
E 1 12  GLY 12  12  12  GLY GLY E . n 
E 1 13  PRO 13  13  13  PRO PRO E . n 
E 1 14  VAL 14  14  14  VAL VAL E . n 
E 1 15  GLN 15  15  15  GLN GLN E . n 
E 1 16  GLY 16  16  16  GLY GLY E . n 
E 1 17  ILE 17  17  17  ILE ILE E . n 
E 1 18  ILE 18  18  18  ILE ILE E . n 
E 1 19  ASN 19  19  19  ASN ASN E . n 
E 1 20  PHE 20  20  20  PHE PHE E . n 
E 1 21  GLU 21  21  21  GLU GLU E . n 
E 1 22  GLN 22  22  22  GLN GLN E . n 
E 1 23  LYS 23  23  23  LYS LYS E . n 
E 1 24  GLU 24  24  24  GLU GLU E . n 
E 1 25  SER 25  25  25  SER SER E . n 
E 1 26  ASN 26  26  26  ASN ASN E . n 
E 1 27  GLY 27  27  27  GLY GLY E . n 
E 1 28  PRO 28  28  28  PRO PRO E . n 
E 1 29  VAL 29  29  29  VAL VAL E . n 
E 1 30  LYS 30  30  30  LYS LYS E . n 
E 1 31  VAL 31  31  31  VAL VAL E . n 
E 1 32  TRP 32  32  32  TRP TRP E . n 
E 1 33  GLY 33  33  33  GLY GLY E . n 
E 1 34  SER 34  34  34  SER SER E . n 
E 1 35  ILE 35  35  35  ILE ILE E . n 
E 1 36  LYS 36  36  36  LYS LYS E . n 
E 1 37  GLY 37  37  37  GLY GLY E . n 
E 1 38  LEU 38  38  38  LEU LEU E . n 
E 1 39  THR 39  39  39  THR THR E . n 
E 1 40  GLU 40  40  40  GLU GLU E . n 
E 1 41  GLY 41  41  41  GLY GLY E . n 
E 1 42  LEU 42  42  42  LEU LEU E . n 
E 1 43  HIS 43  43  43  HIS HIS E . n 
E 1 44  GLY 44  44  44  GLY GLY E . n 
E 1 45  PHE 45  45  45  PHE PHE E . n 
E 1 46  HIS 46  46  46  HIS HIS E . n 
E 1 47  VAL 47  47  47  VAL VAL E . n 
E 1 48  HIS 48  48  48  HIS HIS E . n 
E 1 49  GLU 49  49  49  GLU GLU E . n 
E 1 50  PHE 50  50  50  PHE PHE E . n 
E 1 51  GLY 51  51  51  GLY GLY E . n 
E 1 52  ASP 52  52  52  ASP ASP E . n 
E 1 53  ASN 53  53  53  ASN ASN E . n 
E 1 54  THR 54  54  54  THR THR E . n 
E 1 55  ALA 55  55  55  ALA ALA E . n 
E 1 56  GLY 56  56  56  GLY GLY E . n 
E 1 57  SER 57  57  57  SER SER E . n 
E 1 58  THR 58  58  58  THR THR E . n 
E 1 59  SER 59  59  59  SER SER E . n 
E 1 60  ALA 60  60  60  ALA ALA E . n 
E 1 61  GLY 61  61  61  GLY GLY E . n 
E 1 62  PRO 62  62  62  PRO PRO E . n 
E 1 63  HIS 63  63  63  HIS HIS E . n 
E 1 64  PHE 64  64  64  PHE PHE E . n 
E 1 65  ASN 65  65  65  ASN ASN E . n 
E 1 66  PRO 66  66  66  PRO PRO E . n 
E 1 67  LEU 67  67  67  LEU LEU E . n 
E 1 68  SER 68  68  68  SER SER E . n 
E 1 69  ARG 69  69  69  ARG ARG E . n 
E 1 70  LYS 70  70  70  LYS LYS E . n 
E 1 71  HIS 71  71  71  HIS HIS E . n 
E 1 72  GLY 72  72  72  GLY GLY E . n 
E 1 73  GLY 73  73  73  GLY GLY E . n 
E 1 74  PRO 74  74  74  PRO PRO E . n 
E 1 75  LYS 75  75  75  LYS LYS E . n 
E 1 76  ASP 76  76  76  ASP ASP E . n 
E 1 77  GLU 77  77  77  GLU GLU E . n 
E 1 78  GLU 78  78  78  GLU GLU E . n 
E 1 79  ARG 79  79  79  ARG ARG E . n 
E 1 80  HIS 80  80  80  HIS HIS E . n 
E 1 81  VAL 81  81  81  VAL VAL E . n 
E 1 82  GLY 82  82  82  GLY GLY E . n 
E 1 83  ASP 83  83  83  ASP ASP E . n 
E 1 84  LEU 84  84  84  LEU LEU E . n 
E 1 85  GLY 85  85  85  GLY GLY E . n 
E 1 86  ASN 86  86  86  ASN ASN E . n 
E 1 87  VAL 87  87  87  VAL VAL E . n 
E 1 88  THR 88  88  88  THR THR E . n 
E 1 89  ALA 89  89  89  ALA ALA E . n 
E 1 90  ASP 90  90  90  ASP ASP E . n 
E 1 91  LYS 91  91  91  LYS LYS E . n 
E 1 92  ASP 92  92  92  ASP ASP E . n 
E 1 93  GLY 93  93  93  GLY GLY E . n 
E 1 94  VAL 94  94  94  VAL VAL E . n 
E 1 95  ALA 95  95  95  ALA ALA E . n 
E 1 96  ASP 96  96  96  ASP ASP E . n 
E 1 97  VAL 97  97  97  VAL VAL E . n 
E 1 98  SER 98  98  98  SER SER E . n 
E 1 99  ILE 99  99  99  ILE ILE E . n 
E 1 100 GLU 100 100 100 GLU GLU E . n 
E 1 101 ASP 101 101 101 ASP ASP E . n 
E 1 102 SER 102 102 102 SER SER E . n 
E 1 103 VAL 103 103 103 VAL VAL E . n 
E 1 104 ILE 104 104 104 ILE ILE E . n 
E 1 105 SER 105 105 105 SER SER E . n 
E 1 106 LEU 106 106 106 LEU LEU E . n 
E 1 107 SER 107 107 107 SER SER E . n 
E 1 108 GLY 108 108 108 GLY GLY E . n 
E 1 109 ASP 109 109 109 ASP ASP E . n 
E 1 110 HIS 110 110 110 HIS HIS E . n 
E 1 111 CYS 111 111 111 CYS CYS E . n 
E 1 112 ILE 112 112 112 ILE ILE E . n 
E 1 113 ILE 113 113 113 ILE ILE E . n 
E 1 114 GLY 114 114 114 GLY GLY E . n 
E 1 115 ARG 115 115 115 ARG ARG E . n 
E 1 116 THR 116 116 116 THR THR E . n 
E 1 117 LEU 117 117 117 LEU LEU E . n 
E 1 118 VAL 118 118 118 VAL VAL E . n 
E 1 119 VAL 119 119 119 VAL VAL E . n 
E 1 120 HIS 120 120 120 HIS HIS E . n 
E 1 121 GLU 121 121 121 GLU GLU E . n 
E 1 122 LYS 122 122 122 LYS LYS E . n 
E 1 123 ALA 123 123 123 ALA ALA E . n 
E 1 124 ASP 124 124 124 ASP ASP E . n 
E 1 125 ASP 125 125 125 ASP ASP E . n 
E 1 126 LEU 126 126 126 LEU LEU E . n 
E 1 127 GLY 127 127 127 GLY GLY E . n 
E 1 128 LYS 128 128 128 LYS LYS E . n 
E 1 129 GLY 129 129 129 GLY GLY E . n 
E 1 130 GLY 130 130 130 GLY GLY E . n 
E 1 131 ASN 131 131 131 ASN ASN E . n 
E 1 132 GLU 132 132 132 GLU GLU E . n 
E 1 133 GLU 133 133 133 GLU GLU E . n 
E 1 134 SER 134 134 134 SER SER E . n 
E 1 135 THR 135 135 135 THR THR E . n 
E 1 136 LYS 136 136 136 LYS LYS E . n 
E 1 137 THR 137 137 137 THR THR E . n 
E 1 138 GLY 138 138 138 GLY GLY E . n 
E 1 139 ASN 139 139 139 ASN ASN E . n 
E 1 140 ALA 140 140 140 ALA ALA E . n 
E 1 141 GLY 141 141 141 GLY GLY E . n 
E 1 142 SER 142 142 142 SER SER E . n 
E 1 143 ARG 143 143 143 ARG ARG E . n 
E 1 144 LEU 144 144 144 LEU LEU E . n 
E 1 145 ALA 145 145 145 ALA ALA E . n 
E 1 146 CYS 146 146 146 CYS CYS E . n 
E 1 147 GLY 147 147 147 GLY GLY E . n 
E 1 148 VAL 148 148 148 VAL VAL E . n 
E 1 149 ILE 149 149 149 ILE ILE E . n 
E 1 150 GLY 150 150 150 GLY GLY E . n 
E 1 151 ILE 151 151 151 ILE ILE E . n 
E 1 152 ALA 152 152 152 ALA ALA E . n 
E 1 153 GLN 153 153 153 GLN GLN E . n 
F 1 1   ALA 1   1   1   ALA ALA F . n 
F 1 2   THR 2   2   2   THR THR F . n 
F 1 3   LYS 3   3   3   LYS LYS F . n 
F 1 4   ALA 4   4   4   ALA ALA F . n 
F 1 5   VAL 5   5   5   VAL VAL F . n 
F 1 6   CYS 6   6   6   CYS CYS F . n 
F 1 7   VAL 7   7   7   VAL VAL F . n 
F 1 8   LEU 8   8   8   LEU LEU F . n 
F 1 9   LYS 9   9   9   LYS LYS F . n 
F 1 10  GLY 10  10  10  GLY GLY F . n 
F 1 11  ASP 11  11  11  ASP ASP F . n 
F 1 12  GLY 12  12  12  GLY GLY F . n 
F 1 13  PRO 13  13  13  PRO PRO F . n 
F 1 14  VAL 14  14  14  VAL VAL F . n 
F 1 15  GLN 15  15  15  GLN GLN F . n 
F 1 16  GLY 16  16  16  GLY GLY F . n 
F 1 17  ILE 17  17  17  ILE ILE F . n 
F 1 18  ILE 18  18  18  ILE ILE F . n 
F 1 19  ASN 19  19  19  ASN ASN F . n 
F 1 20  PHE 20  20  20  PHE PHE F . n 
F 1 21  GLU 21  21  21  GLU GLU F . n 
F 1 22  GLN 22  22  22  GLN GLN F . n 
F 1 23  LYS 23  23  23  LYS LYS F . n 
F 1 24  GLU 24  24  24  GLU GLU F . n 
F 1 25  SER 25  25  25  SER SER F . n 
F 1 26  ASN 26  26  26  ASN ASN F . n 
F 1 27  GLY 27  27  27  GLY GLY F . n 
F 1 28  PRO 28  28  28  PRO PRO F . n 
F 1 29  VAL 29  29  29  VAL VAL F . n 
F 1 30  LYS 30  30  30  LYS LYS F . n 
F 1 31  VAL 31  31  31  VAL VAL F . n 
F 1 32  TRP 32  32  32  TRP TRP F . n 
F 1 33  GLY 33  33  33  GLY GLY F . n 
F 1 34  SER 34  34  34  SER SER F . n 
F 1 35  ILE 35  35  35  ILE ILE F . n 
F 1 36  LYS 36  36  36  LYS LYS F . n 
F 1 37  GLY 37  37  37  GLY GLY F . n 
F 1 38  LEU 38  38  38  LEU LEU F . n 
F 1 39  THR 39  39  39  THR THR F . n 
F 1 40  GLU 40  40  40  GLU GLU F . n 
F 1 41  GLY 41  41  41  GLY GLY F . n 
F 1 42  LEU 42  42  42  LEU LEU F . n 
F 1 43  HIS 43  43  43  HIS HIS F . n 
F 1 44  GLY 44  44  44  GLY GLY F . n 
F 1 45  PHE 45  45  45  PHE PHE F . n 
F 1 46  HIS 46  46  46  HIS HIS F . n 
F 1 47  VAL 47  47  47  VAL VAL F . n 
F 1 48  HIS 48  48  48  HIS HIS F . n 
F 1 49  GLU 49  49  49  GLU GLU F . n 
F 1 50  PHE 50  50  50  PHE PHE F . n 
F 1 51  GLY 51  51  51  GLY GLY F . n 
F 1 52  ASP 52  52  52  ASP ASP F . n 
F 1 53  ASN 53  53  53  ASN ASN F . n 
F 1 54  THR 54  54  54  THR THR F . n 
F 1 55  ALA 55  55  55  ALA ALA F . n 
F 1 56  GLY 56  56  56  GLY GLY F . n 
F 1 57  SER 57  57  57  SER SER F . n 
F 1 58  THR 58  58  58  THR THR F . n 
F 1 59  SER 59  59  59  SER SER F . n 
F 1 60  ALA 60  60  60  ALA ALA F . n 
F 1 61  GLY 61  61  61  GLY GLY F . n 
F 1 62  PRO 62  62  62  PRO PRO F . n 
F 1 63  HIS 63  63  63  HIS HIS F . n 
F 1 64  PHE 64  64  64  PHE PHE F . n 
F 1 65  ASN 65  65  65  ASN ASN F . n 
F 1 66  PRO 66  66  66  PRO PRO F . n 
F 1 67  LEU 67  67  67  LEU LEU F . n 
F 1 68  SER 68  68  68  SER SER F . n 
F 1 69  ARG 69  69  69  ARG ARG F . n 
F 1 70  LYS 70  70  70  LYS LYS F . n 
F 1 71  HIS 71  71  71  HIS HIS F . n 
F 1 72  GLY 72  72  72  GLY GLY F . n 
F 1 73  GLY 73  73  73  GLY GLY F . n 
F 1 74  PRO 74  74  74  PRO PRO F . n 
F 1 75  LYS 75  75  75  LYS LYS F . n 
F 1 76  ASP 76  76  76  ASP ASP F . n 
F 1 77  GLU 77  77  77  GLU GLU F . n 
F 1 78  GLU 78  78  78  GLU GLU F . n 
F 1 79  ARG 79  79  79  ARG ARG F . n 
F 1 80  HIS 80  80  80  HIS HIS F . n 
F 1 81  VAL 81  81  81  VAL VAL F . n 
F 1 82  GLY 82  82  82  GLY GLY F . n 
F 1 83  ASP 83  83  83  ASP ASP F . n 
F 1 84  LEU 84  84  84  LEU LEU F . n 
F 1 85  GLY 85  85  85  GLY GLY F . n 
F 1 86  ASN 86  86  86  ASN ASN F . n 
F 1 87  VAL 87  87  87  VAL VAL F . n 
F 1 88  THR 88  88  88  THR THR F . n 
F 1 89  ALA 89  89  89  ALA ALA F . n 
F 1 90  ASP 90  90  90  ASP ASP F . n 
F 1 91  LYS 91  91  91  LYS LYS F . n 
F 1 92  ASP 92  92  92  ASP ASP F . n 
F 1 93  GLY 93  93  93  GLY GLY F . n 
F 1 94  VAL 94  94  94  VAL VAL F . n 
F 1 95  ALA 95  95  95  ALA ALA F . n 
F 1 96  ASP 96  96  96  ASP ASP F . n 
F 1 97  VAL 97  97  97  VAL VAL F . n 
F 1 98  SER 98  98  98  SER SER F . n 
F 1 99  ILE 99  99  99  ILE ILE F . n 
F 1 100 GLU 100 100 100 GLU GLU F . n 
F 1 101 ASP 101 101 101 ASP ASP F . n 
F 1 102 SER 102 102 102 SER SER F . n 
F 1 103 VAL 103 103 103 VAL VAL F . n 
F 1 104 ILE 104 104 104 ILE ILE F . n 
F 1 105 SER 105 105 105 SER SER F . n 
F 1 106 LEU 106 106 106 LEU LEU F . n 
F 1 107 SER 107 107 107 SER SER F . n 
F 1 108 GLY 108 108 108 GLY GLY F . n 
F 1 109 ASP 109 109 109 ASP ASP F . n 
F 1 110 HIS 110 110 110 HIS HIS F . n 
F 1 111 CYS 111 111 111 CYS CYS F . n 
F 1 112 ILE 112 112 112 ILE ILE F . n 
F 1 113 ILE 113 113 113 ILE ILE F . n 
F 1 114 GLY 114 114 114 GLY GLY F . n 
F 1 115 ARG 115 115 115 ARG ARG F . n 
F 1 116 THR 116 116 116 THR THR F . n 
F 1 117 LEU 117 117 117 LEU LEU F . n 
F 1 118 VAL 118 118 118 VAL VAL F . n 
F 1 119 VAL 119 119 119 VAL VAL F . n 
F 1 120 HIS 120 120 120 HIS HIS F . n 
F 1 121 GLU 121 121 121 GLU GLU F . n 
F 1 122 LYS 122 122 122 LYS LYS F . n 
F 1 123 ALA 123 123 123 ALA ALA F . n 
F 1 124 ASP 124 124 124 ASP ASP F . n 
F 1 125 ASP 125 125 125 ASP ASP F . n 
F 1 126 LEU 126 126 126 LEU LEU F . n 
F 1 127 GLY 127 127 127 GLY GLY F . n 
F 1 128 LYS 128 128 128 LYS LYS F . n 
F 1 129 GLY 129 129 129 GLY GLY F . n 
F 1 130 GLY 130 130 130 GLY GLY F . n 
F 1 131 ASN 131 131 131 ASN ASN F . n 
F 1 132 GLU 132 132 132 GLU GLU F . n 
F 1 133 GLU 133 133 133 GLU GLU F . n 
F 1 134 SER 134 134 134 SER SER F . n 
F 1 135 THR 135 135 135 THR THR F . n 
F 1 136 LYS 136 136 136 LYS LYS F . n 
F 1 137 THR 137 137 137 THR THR F . n 
F 1 138 GLY 138 138 138 GLY GLY F . n 
F 1 139 ASN 139 139 139 ASN ASN F . n 
F 1 140 ALA 140 140 140 ALA ALA F . n 
F 1 141 GLY 141 141 141 GLY GLY F . n 
F 1 142 SER 142 142 142 SER SER F . n 
F 1 143 ARG 143 143 143 ARG ARG F . n 
F 1 144 LEU 144 144 144 LEU LEU F . n 
F 1 145 ALA 145 145 145 ALA ALA F . n 
F 1 146 CYS 146 146 146 CYS CYS F . n 
F 1 147 GLY 147 147 147 GLY GLY F . n 
F 1 148 VAL 148 148 148 VAL VAL F . n 
F 1 149 ILE 149 149 149 ILE ILE F . n 
F 1 150 GLY 150 150 150 GLY GLY F . n 
F 1 151 ILE 151 151 151 ILE ILE F . n 
F 1 152 ALA 152 152 152 ALA ALA F . n 
F 1 153 GLN 153 153 153 GLN GLN F . n 
G 1 1   ALA 1   1   1   ALA ALA G . n 
G 1 2   THR 2   2   2   THR THR G . n 
G 1 3   LYS 3   3   3   LYS LYS G . n 
G 1 4   ALA 4   4   4   ALA ALA G . n 
G 1 5   VAL 5   5   5   VAL VAL G . n 
G 1 6   CYS 6   6   6   CYS CYS G . n 
G 1 7   VAL 7   7   7   VAL VAL G . n 
G 1 8   LEU 8   8   8   LEU LEU G . n 
G 1 9   LYS 9   9   9   LYS LYS G . n 
G 1 10  GLY 10  10  10  GLY GLY G . n 
G 1 11  ASP 11  11  11  ASP ASP G . n 
G 1 12  GLY 12  12  12  GLY GLY G . n 
G 1 13  PRO 13  13  13  PRO PRO G . n 
G 1 14  VAL 14  14  14  VAL VAL G . n 
G 1 15  GLN 15  15  15  GLN GLN G . n 
G 1 16  GLY 16  16  16  GLY GLY G . n 
G 1 17  ILE 17  17  17  ILE ILE G . n 
G 1 18  ILE 18  18  18  ILE ILE G . n 
G 1 19  ASN 19  19  19  ASN ASN G . n 
G 1 20  PHE 20  20  20  PHE PHE G . n 
G 1 21  GLU 21  21  21  GLU GLU G . n 
G 1 22  GLN 22  22  22  GLN GLN G . n 
G 1 23  LYS 23  23  23  LYS LYS G . n 
G 1 24  GLU 24  24  24  GLU GLU G . n 
G 1 25  SER 25  25  25  SER SER G . n 
G 1 26  ASN 26  26  26  ASN ASN G . n 
G 1 27  GLY 27  27  27  GLY GLY G . n 
G 1 28  PRO 28  28  28  PRO PRO G . n 
G 1 29  VAL 29  29  29  VAL VAL G . n 
G 1 30  LYS 30  30  30  LYS LYS G . n 
G 1 31  VAL 31  31  31  VAL VAL G . n 
G 1 32  TRP 32  32  32  TRP TRP G . n 
G 1 33  GLY 33  33  33  GLY GLY G . n 
G 1 34  SER 34  34  34  SER SER G . n 
G 1 35  ILE 35  35  35  ILE ILE G . n 
G 1 36  LYS 36  36  36  LYS LYS G . n 
G 1 37  GLY 37  37  37  GLY GLY G . n 
G 1 38  LEU 38  38  38  LEU LEU G . n 
G 1 39  THR 39  39  39  THR THR G . n 
G 1 40  GLU 40  40  40  GLU GLU G . n 
G 1 41  GLY 41  41  41  GLY GLY G . n 
G 1 42  LEU 42  42  42  LEU LEU G . n 
G 1 43  HIS 43  43  43  HIS HIS G . n 
G 1 44  GLY 44  44  44  GLY GLY G . n 
G 1 45  PHE 45  45  45  PHE PHE G . n 
G 1 46  HIS 46  46  46  HIS HIS G . n 
G 1 47  VAL 47  47  47  VAL VAL G . n 
G 1 48  HIS 48  48  48  HIS HIS G . n 
G 1 49  GLU 49  49  49  GLU GLU G . n 
G 1 50  PHE 50  50  50  PHE PHE G . n 
G 1 51  GLY 51  51  51  GLY GLY G . n 
G 1 52  ASP 52  52  52  ASP ASP G . n 
G 1 53  ASN 53  53  53  ASN ASN G . n 
G 1 54  THR 54  54  54  THR THR G . n 
G 1 55  ALA 55  55  55  ALA ALA G . n 
G 1 56  GLY 56  56  56  GLY GLY G . n 
G 1 57  SER 57  57  57  SER SER G . n 
G 1 58  THR 58  58  58  THR THR G . n 
G 1 59  SER 59  59  59  SER SER G . n 
G 1 60  ALA 60  60  60  ALA ALA G . n 
G 1 61  GLY 61  61  61  GLY GLY G . n 
G 1 62  PRO 62  62  62  PRO PRO G . n 
G 1 63  HIS 63  63  63  HIS HIS G . n 
G 1 64  PHE 64  64  64  PHE PHE G . n 
G 1 65  ASN 65  65  65  ASN ASN G . n 
G 1 66  PRO 66  66  66  PRO PRO G . n 
G 1 67  LEU 67  67  67  LEU LEU G . n 
G 1 68  SER 68  68  68  SER SER G . n 
G 1 69  ARG 69  69  69  ARG ARG G . n 
G 1 70  LYS 70  70  70  LYS LYS G . n 
G 1 71  HIS 71  71  71  HIS HIS G . n 
G 1 72  GLY 72  72  72  GLY GLY G . n 
G 1 73  GLY 73  73  73  GLY GLY G . n 
G 1 74  PRO 74  74  74  PRO PRO G . n 
G 1 75  LYS 75  75  75  LYS LYS G . n 
G 1 76  ASP 76  76  76  ASP ASP G . n 
G 1 77  GLU 77  77  77  GLU GLU G . n 
G 1 78  GLU 78  78  78  GLU GLU G . n 
G 1 79  ARG 79  79  79  ARG ARG G . n 
G 1 80  HIS 80  80  80  HIS HIS G . n 
G 1 81  VAL 81  81  81  VAL VAL G . n 
G 1 82  GLY 82  82  82  GLY GLY G . n 
G 1 83  ASP 83  83  83  ASP ASP G . n 
G 1 84  LEU 84  84  84  LEU LEU G . n 
G 1 85  GLY 85  85  85  GLY GLY G . n 
G 1 86  ASN 86  86  86  ASN ASN G . n 
G 1 87  VAL 87  87  87  VAL VAL G . n 
G 1 88  THR 88  88  88  THR THR G . n 
G 1 89  ALA 89  89  89  ALA ALA G . n 
G 1 90  ASP 90  90  90  ASP ASP G . n 
G 1 91  LYS 91  91  91  LYS LYS G . n 
G 1 92  ASP 92  92  92  ASP ASP G . n 
G 1 93  GLY 93  93  93  GLY GLY G . n 
G 1 94  VAL 94  94  94  VAL VAL G . n 
G 1 95  ALA 95  95  95  ALA ALA G . n 
G 1 96  ASP 96  96  96  ASP ASP G . n 
G 1 97  VAL 97  97  97  VAL VAL G . n 
G 1 98  SER 98  98  98  SER SER G . n 
G 1 99  ILE 99  99  99  ILE ILE G . n 
G 1 100 GLU 100 100 100 GLU GLU G . n 
G 1 101 ASP 101 101 101 ASP ASP G . n 
G 1 102 SER 102 102 102 SER SER G . n 
G 1 103 VAL 103 103 103 VAL VAL G . n 
G 1 104 ILE 104 104 104 ILE ILE G . n 
G 1 105 SER 105 105 105 SER SER G . n 
G 1 106 LEU 106 106 106 LEU LEU G . n 
G 1 107 SER 107 107 107 SER SER G . n 
G 1 108 GLY 108 108 108 GLY GLY G . n 
G 1 109 ASP 109 109 109 ASP ASP G . n 
G 1 110 HIS 110 110 110 HIS HIS G . n 
G 1 111 CYS 111 111 111 CYS CYS G . n 
G 1 112 ILE 112 112 112 ILE ILE G . n 
G 1 113 ILE 113 113 113 ILE ILE G . n 
G 1 114 GLY 114 114 114 GLY GLY G . n 
G 1 115 ARG 115 115 115 ARG ARG G . n 
G 1 116 THR 116 116 116 THR THR G . n 
G 1 117 LEU 117 117 117 LEU LEU G . n 
G 1 118 VAL 118 118 118 VAL VAL G . n 
G 1 119 VAL 119 119 119 VAL VAL G . n 
G 1 120 HIS 120 120 120 HIS HIS G . n 
G 1 121 GLU 121 121 121 GLU GLU G . n 
G 1 122 LYS 122 122 122 LYS LYS G . n 
G 1 123 ALA 123 123 123 ALA ALA G . n 
G 1 124 ASP 124 124 124 ASP ASP G . n 
G 1 125 ASP 125 125 125 ASP ASP G . n 
G 1 126 LEU 126 126 126 LEU LEU G . n 
G 1 127 GLY 127 127 127 GLY GLY G . n 
G 1 128 LYS 128 128 128 LYS LYS G . n 
G 1 129 GLY 129 129 129 GLY GLY G . n 
G 1 130 GLY 130 130 130 GLY GLY G . n 
G 1 131 ASN 131 131 131 ASN ASN G . n 
G 1 132 GLU 132 132 132 GLU GLU G . n 
G 1 133 GLU 133 133 133 GLU GLU G . n 
G 1 134 SER 134 134 134 SER SER G . n 
G 1 135 THR 135 135 135 THR THR G . n 
G 1 136 LYS 136 136 136 LYS LYS G . n 
G 1 137 THR 137 137 137 THR THR G . n 
G 1 138 GLY 138 138 138 GLY GLY G . n 
G 1 139 ASN 139 139 139 ASN ASN G . n 
G 1 140 ALA 140 140 140 ALA ALA G . n 
G 1 141 GLY 141 141 141 GLY GLY G . n 
G 1 142 SER 142 142 142 SER SER G . n 
G 1 143 ARG 143 143 143 ARG ARG G . n 
G 1 144 LEU 144 144 144 LEU LEU G . n 
G 1 145 ALA 145 145 145 ALA ALA G . n 
G 1 146 CYS 146 146 146 CYS CYS G . n 
G 1 147 GLY 147 147 147 GLY GLY G . n 
G 1 148 VAL 148 148 148 VAL VAL G . n 
G 1 149 ILE 149 149 149 ILE ILE G . n 
G 1 150 GLY 150 150 150 GLY GLY G . n 
G 1 151 ILE 151 151 151 ILE ILE G . n 
G 1 152 ALA 152 152 152 ALA ALA G . n 
G 1 153 GLN 153 153 153 GLN GLN G . n 
H 1 1   ALA 1   1   1   ALA ALA H . n 
H 1 2   THR 2   2   2   THR THR H . n 
H 1 3   LYS 3   3   3   LYS LYS H . n 
H 1 4   ALA 4   4   4   ALA ALA H . n 
H 1 5   VAL 5   5   5   VAL VAL H . n 
H 1 6   CYS 6   6   6   CYS CYS H . n 
H 1 7   VAL 7   7   7   VAL VAL H . n 
H 1 8   LEU 8   8   8   LEU LEU H . n 
H 1 9   LYS 9   9   9   LYS LYS H . n 
H 1 10  GLY 10  10  10  GLY GLY H . n 
H 1 11  ASP 11  11  11  ASP ASP H . n 
H 1 12  GLY 12  12  12  GLY GLY H . n 
H 1 13  PRO 13  13  13  PRO PRO H . n 
H 1 14  VAL 14  14  14  VAL VAL H . n 
H 1 15  GLN 15  15  15  GLN GLN H . n 
H 1 16  GLY 16  16  16  GLY GLY H . n 
H 1 17  ILE 17  17  17  ILE ILE H . n 
H 1 18  ILE 18  18  18  ILE ILE H . n 
H 1 19  ASN 19  19  19  ASN ASN H . n 
H 1 20  PHE 20  20  20  PHE PHE H . n 
H 1 21  GLU 21  21  21  GLU GLU H . n 
H 1 22  GLN 22  22  22  GLN GLN H . n 
H 1 23  LYS 23  23  23  LYS LYS H . n 
H 1 24  GLU 24  24  24  GLU GLU H . n 
H 1 25  SER 25  25  25  SER SER H . n 
H 1 26  ASN 26  26  26  ASN ASN H . n 
H 1 27  GLY 27  27  27  GLY GLY H . n 
H 1 28  PRO 28  28  28  PRO PRO H . n 
H 1 29  VAL 29  29  29  VAL VAL H . n 
H 1 30  LYS 30  30  30  LYS LYS H . n 
H 1 31  VAL 31  31  31  VAL VAL H . n 
H 1 32  TRP 32  32  32  TRP TRP H . n 
H 1 33  GLY 33  33  33  GLY GLY H . n 
H 1 34  SER 34  34  34  SER SER H . n 
H 1 35  ILE 35  35  35  ILE ILE H . n 
H 1 36  LYS 36  36  36  LYS LYS H . n 
H 1 37  GLY 37  37  37  GLY GLY H . n 
H 1 38  LEU 38  38  38  LEU LEU H . n 
H 1 39  THR 39  39  39  THR THR H . n 
H 1 40  GLU 40  40  40  GLU GLU H . n 
H 1 41  GLY 41  41  41  GLY GLY H . n 
H 1 42  LEU 42  42  42  LEU LEU H . n 
H 1 43  HIS 43  43  43  HIS HIS H . n 
H 1 44  GLY 44  44  44  GLY GLY H . n 
H 1 45  PHE 45  45  45  PHE PHE H . n 
H 1 46  HIS 46  46  46  HIS HIS H . n 
H 1 47  VAL 47  47  47  VAL VAL H . n 
H 1 48  HIS 48  48  48  HIS HIS H . n 
H 1 49  GLU 49  49  49  GLU GLU H . n 
H 1 50  PHE 50  50  50  PHE PHE H . n 
H 1 51  GLY 51  51  51  GLY GLY H . n 
H 1 52  ASP 52  52  52  ASP ASP H . n 
H 1 53  ASN 53  53  53  ASN ASN H . n 
H 1 54  THR 54  54  54  THR THR H . n 
H 1 55  ALA 55  55  55  ALA ALA H . n 
H 1 56  GLY 56  56  56  GLY GLY H . n 
H 1 57  SER 57  57  57  SER SER H . n 
H 1 58  THR 58  58  58  THR THR H . n 
H 1 59  SER 59  59  59  SER SER H . n 
H 1 60  ALA 60  60  60  ALA ALA H . n 
H 1 61  GLY 61  61  61  GLY GLY H . n 
H 1 62  PRO 62  62  62  PRO PRO H . n 
H 1 63  HIS 63  63  63  HIS HIS H . n 
H 1 64  PHE 64  64  64  PHE PHE H . n 
H 1 65  ASN 65  65  65  ASN ASN H . n 
H 1 66  PRO 66  66  66  PRO PRO H . n 
H 1 67  LEU 67  67  67  LEU LEU H . n 
H 1 68  SER 68  68  68  SER SER H . n 
H 1 69  ARG 69  69  69  ARG ARG H . n 
H 1 70  LYS 70  70  70  LYS LYS H . n 
H 1 71  HIS 71  71  71  HIS HIS H . n 
H 1 72  GLY 72  72  72  GLY GLY H . n 
H 1 73  GLY 73  73  73  GLY GLY H . n 
H 1 74  PRO 74  74  74  PRO PRO H . n 
H 1 75  LYS 75  75  75  LYS LYS H . n 
H 1 76  ASP 76  76  76  ASP ASP H . n 
H 1 77  GLU 77  77  77  GLU GLU H . n 
H 1 78  GLU 78  78  78  GLU GLU H . n 
H 1 79  ARG 79  79  79  ARG ARG H . n 
H 1 80  HIS 80  80  80  HIS HIS H . n 
H 1 81  VAL 81  81  81  VAL VAL H . n 
H 1 82  GLY 82  82  82  GLY GLY H . n 
H 1 83  ASP 83  83  83  ASP ASP H . n 
H 1 84  LEU 84  84  84  LEU LEU H . n 
H 1 85  GLY 85  85  85  GLY GLY H . n 
H 1 86  ASN 86  86  86  ASN ASN H . n 
H 1 87  VAL 87  87  87  VAL VAL H . n 
H 1 88  THR 88  88  88  THR THR H . n 
H 1 89  ALA 89  89  89  ALA ALA H . n 
H 1 90  ASP 90  90  90  ASP ASP H . n 
H 1 91  LYS 91  91  91  LYS LYS H . n 
H 1 92  ASP 92  92  92  ASP ASP H . n 
H 1 93  GLY 93  93  93  GLY GLY H . n 
H 1 94  VAL 94  94  94  VAL VAL H . n 
H 1 95  ALA 95  95  95  ALA ALA H . n 
H 1 96  ASP 96  96  96  ASP ASP H . n 
H 1 97  VAL 97  97  97  VAL VAL H . n 
H 1 98  SER 98  98  98  SER SER H . n 
H 1 99  ILE 99  99  99  ILE ILE H . n 
H 1 100 GLU 100 100 100 GLU GLU H . n 
H 1 101 ASP 101 101 101 ASP ASP H . n 
H 1 102 SER 102 102 102 SER SER H . n 
H 1 103 VAL 103 103 103 VAL VAL H . n 
H 1 104 ILE 104 104 104 ILE ILE H . n 
H 1 105 SER 105 105 105 SER SER H . n 
H 1 106 LEU 106 106 106 LEU LEU H . n 
H 1 107 SER 107 107 107 SER SER H . n 
H 1 108 GLY 108 108 108 GLY GLY H . n 
H 1 109 ASP 109 109 109 ASP ASP H . n 
H 1 110 HIS 110 110 110 HIS HIS H . n 
H 1 111 CYS 111 111 111 CYS CYS H . n 
H 1 112 ILE 112 112 112 ILE ILE H . n 
H 1 113 ILE 113 113 113 ILE ILE H . n 
H 1 114 GLY 114 114 114 GLY GLY H . n 
H 1 115 ARG 115 115 115 ARG ARG H . n 
H 1 116 THR 116 116 116 THR THR H . n 
H 1 117 LEU 117 117 117 LEU LEU H . n 
H 1 118 VAL 118 118 118 VAL VAL H . n 
H 1 119 VAL 119 119 119 VAL VAL H . n 
H 1 120 HIS 120 120 120 HIS HIS H . n 
H 1 121 GLU 121 121 121 GLU GLU H . n 
H 1 122 LYS 122 122 122 LYS LYS H . n 
H 1 123 ALA 123 123 123 ALA ALA H . n 
H 1 124 ASP 124 124 124 ASP ASP H . n 
H 1 125 ASP 125 125 125 ASP ASP H . n 
H 1 126 LEU 126 126 126 LEU LEU H . n 
H 1 127 GLY 127 127 127 GLY GLY H . n 
H 1 128 LYS 128 128 128 LYS LYS H . n 
H 1 129 GLY 129 129 129 GLY GLY H . n 
H 1 130 GLY 130 130 130 GLY GLY H . n 
H 1 131 ASN 131 131 131 ASN ASN H . n 
H 1 132 GLU 132 132 132 GLU GLU H . n 
H 1 133 GLU 133 133 133 GLU GLU H . n 
H 1 134 SER 134 134 134 SER SER H . n 
H 1 135 THR 135 135 135 THR THR H . n 
H 1 136 LYS 136 136 136 LYS LYS H . n 
H 1 137 THR 137 137 137 THR THR H . n 
H 1 138 GLY 138 138 138 GLY GLY H . n 
H 1 139 ASN 139 139 139 ASN ASN H . n 
H 1 140 ALA 140 140 140 ALA ALA H . n 
H 1 141 GLY 141 141 141 GLY GLY H . n 
H 1 142 SER 142 142 142 SER SER H . n 
H 1 143 ARG 143 143 143 ARG ARG H . n 
H 1 144 LEU 144 144 144 LEU LEU H . n 
H 1 145 ALA 145 145 145 ALA ALA H . n 
H 1 146 CYS 146 146 146 CYS CYS H . n 
H 1 147 GLY 147 147 147 GLY GLY H . n 
H 1 148 VAL 148 148 148 VAL VAL H . n 
H 1 149 ILE 149 149 149 ILE ILE H . n 
H 1 150 GLY 150 150 150 GLY GLY H . n 
H 1 151 ILE 151 151 151 ILE ILE H . n 
H 1 152 ALA 152 152 152 ALA ALA H . n 
H 1 153 GLN 153 153 153 GLN GLN H . n 
I 1 1   ALA 1   1   1   ALA ALA I . n 
I 1 2   THR 2   2   2   THR THR I . n 
I 1 3   LYS 3   3   3   LYS LYS I . n 
I 1 4   ALA 4   4   4   ALA ALA I . n 
I 1 5   VAL 5   5   5   VAL VAL I . n 
I 1 6   CYS 6   6   6   CYS CYS I . n 
I 1 7   VAL 7   7   7   VAL VAL I . n 
I 1 8   LEU 8   8   8   LEU LEU I . n 
I 1 9   LYS 9   9   9   LYS LYS I . n 
I 1 10  GLY 10  10  10  GLY GLY I . n 
I 1 11  ASP 11  11  11  ASP ASP I . n 
I 1 12  GLY 12  12  12  GLY GLY I . n 
I 1 13  PRO 13  13  13  PRO PRO I . n 
I 1 14  VAL 14  14  14  VAL VAL I . n 
I 1 15  GLN 15  15  15  GLN GLN I . n 
I 1 16  GLY 16  16  16  GLY GLY I . n 
I 1 17  ILE 17  17  17  ILE ILE I . n 
I 1 18  ILE 18  18  18  ILE ILE I . n 
I 1 19  ASN 19  19  19  ASN ASN I . n 
I 1 20  PHE 20  20  20  PHE PHE I . n 
I 1 21  GLU 21  21  21  GLU GLU I . n 
I 1 22  GLN 22  22  22  GLN GLN I . n 
I 1 23  LYS 23  23  23  LYS LYS I . n 
I 1 24  GLU 24  24  24  GLU GLU I . n 
I 1 25  SER 25  25  25  SER SER I . n 
I 1 26  ASN 26  26  26  ASN ASN I . n 
I 1 27  GLY 27  27  27  GLY GLY I . n 
I 1 28  PRO 28  28  28  PRO PRO I . n 
I 1 29  VAL 29  29  29  VAL VAL I . n 
I 1 30  LYS 30  30  30  LYS LYS I . n 
I 1 31  VAL 31  31  31  VAL VAL I . n 
I 1 32  TRP 32  32  32  TRP TRP I . n 
I 1 33  GLY 33  33  33  GLY GLY I . n 
I 1 34  SER 34  34  34  SER SER I . n 
I 1 35  ILE 35  35  35  ILE ILE I . n 
I 1 36  LYS 36  36  36  LYS LYS I . n 
I 1 37  GLY 37  37  37  GLY GLY I . n 
I 1 38  LEU 38  38  38  LEU LEU I . n 
I 1 39  THR 39  39  39  THR THR I . n 
I 1 40  GLU 40  40  40  GLU GLU I . n 
I 1 41  GLY 41  41  41  GLY GLY I . n 
I 1 42  LEU 42  42  42  LEU LEU I . n 
I 1 43  HIS 43  43  43  HIS HIS I . n 
I 1 44  GLY 44  44  44  GLY GLY I . n 
I 1 45  PHE 45  45  45  PHE PHE I . n 
I 1 46  HIS 46  46  46  HIS HIS I . n 
I 1 47  VAL 47  47  47  VAL VAL I . n 
I 1 48  HIS 48  48  48  HIS HIS I . n 
I 1 49  GLU 49  49  49  GLU GLU I . n 
I 1 50  PHE 50  50  50  PHE PHE I . n 
I 1 51  GLY 51  51  51  GLY GLY I . n 
I 1 52  ASP 52  52  52  ASP ASP I . n 
I 1 53  ASN 53  53  53  ASN ASN I . n 
I 1 54  THR 54  54  54  THR THR I . n 
I 1 55  ALA 55  55  55  ALA ALA I . n 
I 1 56  GLY 56  56  56  GLY GLY I . n 
I 1 57  SER 57  57  57  SER SER I . n 
I 1 58  THR 58  58  58  THR THR I . n 
I 1 59  SER 59  59  59  SER SER I . n 
I 1 60  ALA 60  60  60  ALA ALA I . n 
I 1 61  GLY 61  61  61  GLY GLY I . n 
I 1 62  PRO 62  62  62  PRO PRO I . n 
I 1 63  HIS 63  63  63  HIS HIS I . n 
I 1 64  PHE 64  64  64  PHE PHE I . n 
I 1 65  ASN 65  65  65  ASN ASN I . n 
I 1 66  PRO 66  66  66  PRO PRO I . n 
I 1 67  LEU 67  67  67  LEU LEU I . n 
I 1 68  SER 68  68  68  SER SER I . n 
I 1 69  ARG 69  69  69  ARG ARG I . n 
I 1 70  LYS 70  70  70  LYS LYS I . n 
I 1 71  HIS 71  71  71  HIS HIS I . n 
I 1 72  GLY 72  72  72  GLY GLY I . n 
I 1 73  GLY 73  73  73  GLY GLY I . n 
I 1 74  PRO 74  74  74  PRO PRO I . n 
I 1 75  LYS 75  75  75  LYS LYS I . n 
I 1 76  ASP 76  76  76  ASP ASP I . n 
I 1 77  GLU 77  77  77  GLU GLU I . n 
I 1 78  GLU 78  78  78  GLU GLU I . n 
I 1 79  ARG 79  79  79  ARG ARG I . n 
I 1 80  HIS 80  80  80  HIS HIS I . n 
I 1 81  VAL 81  81  81  VAL VAL I . n 
I 1 82  GLY 82  82  82  GLY GLY I . n 
I 1 83  ASP 83  83  83  ASP ASP I . n 
I 1 84  LEU 84  84  84  LEU LEU I . n 
I 1 85  GLY 85  85  85  GLY GLY I . n 
I 1 86  ASN 86  86  86  ASN ASN I . n 
I 1 87  VAL 87  87  87  VAL VAL I . n 
I 1 88  THR 88  88  88  THR THR I . n 
I 1 89  ALA 89  89  89  ALA ALA I . n 
I 1 90  ASP 90  90  90  ASP ASP I . n 
I 1 91  LYS 91  91  91  LYS LYS I . n 
I 1 92  ASP 92  92  92  ASP ASP I . n 
I 1 93  GLY 93  93  93  GLY GLY I . n 
I 1 94  VAL 94  94  94  VAL VAL I . n 
I 1 95  ALA 95  95  95  ALA ALA I . n 
I 1 96  ASP 96  96  96  ASP ASP I . n 
I 1 97  VAL 97  97  97  VAL VAL I . n 
I 1 98  SER 98  98  98  SER SER I . n 
I 1 99  ILE 99  99  99  ILE ILE I . n 
I 1 100 GLU 100 100 100 GLU GLU I . n 
I 1 101 ASP 101 101 101 ASP ASP I . n 
I 1 102 SER 102 102 102 SER SER I . n 
I 1 103 VAL 103 103 103 VAL VAL I . n 
I 1 104 ILE 104 104 104 ILE ILE I . n 
I 1 105 SER 105 105 105 SER SER I . n 
I 1 106 LEU 106 106 106 LEU LEU I . n 
I 1 107 SER 107 107 107 SER SER I . n 
I 1 108 GLY 108 108 108 GLY GLY I . n 
I 1 109 ASP 109 109 109 ASP ASP I . n 
I 1 110 HIS 110 110 110 HIS HIS I . n 
I 1 111 CYS 111 111 111 CYS CYS I . n 
I 1 112 ILE 112 112 112 ILE ILE I . n 
I 1 113 ILE 113 113 113 ILE ILE I . n 
I 1 114 GLY 114 114 114 GLY GLY I . n 
I 1 115 ARG 115 115 115 ARG ARG I . n 
I 1 116 THR 116 116 116 THR THR I . n 
I 1 117 LEU 117 117 117 LEU LEU I . n 
I 1 118 VAL 118 118 118 VAL VAL I . n 
I 1 119 VAL 119 119 119 VAL VAL I . n 
I 1 120 HIS 120 120 120 HIS HIS I . n 
I 1 121 GLU 121 121 121 GLU GLU I . n 
I 1 122 LYS 122 122 122 LYS LYS I . n 
I 1 123 ALA 123 123 123 ALA ALA I . n 
I 1 124 ASP 124 124 124 ASP ASP I . n 
I 1 125 ASP 125 125 125 ASP ASP I . n 
I 1 126 LEU 126 126 126 LEU LEU I . n 
I 1 127 GLY 127 127 127 GLY GLY I . n 
I 1 128 LYS 128 128 128 LYS LYS I . n 
I 1 129 GLY 129 129 129 GLY GLY I . n 
I 1 130 GLY 130 130 130 GLY GLY I . n 
I 1 131 ASN 131 131 131 ASN ASN I . n 
I 1 132 GLU 132 132 132 GLU GLU I . n 
I 1 133 GLU 133 133 133 GLU GLU I . n 
I 1 134 SER 134 134 134 SER SER I . n 
I 1 135 THR 135 135 135 THR THR I . n 
I 1 136 LYS 136 136 136 LYS LYS I . n 
I 1 137 THR 137 137 137 THR THR I . n 
I 1 138 GLY 138 138 138 GLY GLY I . n 
I 1 139 ASN 139 139 139 ASN ASN I . n 
I 1 140 ALA 140 140 140 ALA ALA I . n 
I 1 141 GLY 141 141 141 GLY GLY I . n 
I 1 142 SER 142 142 142 SER SER I . n 
I 1 143 ARG 143 143 143 ARG ARG I . n 
I 1 144 LEU 144 144 144 LEU LEU I . n 
I 1 145 ALA 145 145 145 ALA ALA I . n 
I 1 146 CYS 146 146 146 CYS CYS I . n 
I 1 147 GLY 147 147 147 GLY GLY I . n 
I 1 148 VAL 148 148 148 VAL VAL I . n 
I 1 149 ILE 149 149 149 ILE ILE I . n 
I 1 150 GLY 150 150 150 GLY GLY I . n 
I 1 151 ILE 151 151 151 ILE ILE I . n 
I 1 152 ALA 152 152 152 ALA ALA I . n 
I 1 153 GLN 153 153 153 GLN GLN I . n 
J 1 1   ALA 1   1   1   ALA ALA J . n 
J 1 2   THR 2   2   2   THR THR J . n 
J 1 3   LYS 3   3   3   LYS LYS J . n 
J 1 4   ALA 4   4   4   ALA ALA J . n 
J 1 5   VAL 5   5   5   VAL VAL J . n 
J 1 6   CYS 6   6   6   CYS CYS J . n 
J 1 7   VAL 7   7   7   VAL VAL J . n 
J 1 8   LEU 8   8   8   LEU LEU J . n 
J 1 9   LYS 9   9   9   LYS LYS J . n 
J 1 10  GLY 10  10  10  GLY GLY J . n 
J 1 11  ASP 11  11  11  ASP ASP J . n 
J 1 12  GLY 12  12  12  GLY GLY J . n 
J 1 13  PRO 13  13  13  PRO PRO J . n 
J 1 14  VAL 14  14  14  VAL VAL J . n 
J 1 15  GLN 15  15  15  GLN GLN J . n 
J 1 16  GLY 16  16  16  GLY GLY J . n 
J 1 17  ILE 17  17  17  ILE ILE J . n 
J 1 18  ILE 18  18  18  ILE ILE J . n 
J 1 19  ASN 19  19  19  ASN ASN J . n 
J 1 20  PHE 20  20  20  PHE PHE J . n 
J 1 21  GLU 21  21  21  GLU GLU J . n 
J 1 22  GLN 22  22  22  GLN GLN J . n 
J 1 23  LYS 23  23  23  LYS LYS J . n 
J 1 24  GLU 24  24  24  GLU GLU J . n 
J 1 25  SER 25  25  25  SER SER J . n 
J 1 26  ASN 26  26  26  ASN ASN J . n 
J 1 27  GLY 27  27  27  GLY GLY J . n 
J 1 28  PRO 28  28  28  PRO PRO J . n 
J 1 29  VAL 29  29  29  VAL VAL J . n 
J 1 30  LYS 30  30  30  LYS LYS J . n 
J 1 31  VAL 31  31  31  VAL VAL J . n 
J 1 32  TRP 32  32  32  TRP TRP J . n 
J 1 33  GLY 33  33  33  GLY GLY J . n 
J 1 34  SER 34  34  34  SER SER J . n 
J 1 35  ILE 35  35  35  ILE ILE J . n 
J 1 36  LYS 36  36  36  LYS LYS J . n 
J 1 37  GLY 37  37  37  GLY GLY J . n 
J 1 38  LEU 38  38  38  LEU LEU J . n 
J 1 39  THR 39  39  39  THR THR J . n 
J 1 40  GLU 40  40  40  GLU GLU J . n 
J 1 41  GLY 41  41  41  GLY GLY J . n 
J 1 42  LEU 42  42  42  LEU LEU J . n 
J 1 43  HIS 43  43  43  HIS HIS J . n 
J 1 44  GLY 44  44  44  GLY GLY J . n 
J 1 45  PHE 45  45  45  PHE PHE J . n 
J 1 46  HIS 46  46  46  HIS HIS J . n 
J 1 47  VAL 47  47  47  VAL VAL J . n 
J 1 48  HIS 48  48  48  HIS HIS J . n 
J 1 49  GLU 49  49  49  GLU GLU J . n 
J 1 50  PHE 50  50  50  PHE PHE J . n 
J 1 51  GLY 51  51  51  GLY GLY J . n 
J 1 52  ASP 52  52  52  ASP ASP J . n 
J 1 53  ASN 53  53  53  ASN ASN J . n 
J 1 54  THR 54  54  54  THR THR J . n 
J 1 55  ALA 55  55  55  ALA ALA J . n 
J 1 56  GLY 56  56  56  GLY GLY J . n 
J 1 57  SER 57  57  57  SER SER J . n 
J 1 58  THR 58  58  58  THR THR J . n 
J 1 59  SER 59  59  59  SER SER J . n 
J 1 60  ALA 60  60  60  ALA ALA J . n 
J 1 61  GLY 61  61  61  GLY GLY J . n 
J 1 62  PRO 62  62  62  PRO PRO J . n 
J 1 63  HIS 63  63  63  HIS HIS J . n 
J 1 64  PHE 64  64  64  PHE PHE J . n 
J 1 65  ASN 65  65  65  ASN ASN J . n 
J 1 66  PRO 66  66  66  PRO PRO J . n 
J 1 67  LEU 67  67  67  LEU LEU J . n 
J 1 68  SER 68  68  68  SER SER J . n 
J 1 69  ARG 69  69  69  ARG ARG J . n 
J 1 70  LYS 70  70  70  LYS LYS J . n 
J 1 71  HIS 71  71  71  HIS HIS J . n 
J 1 72  GLY 72  72  72  GLY GLY J . n 
J 1 73  GLY 73  73  73  GLY GLY J . n 
J 1 74  PRO 74  74  74  PRO PRO J . n 
J 1 75  LYS 75  75  75  LYS LYS J . n 
J 1 76  ASP 76  76  76  ASP ASP J . n 
J 1 77  GLU 77  77  77  GLU GLU J . n 
J 1 78  GLU 78  78  78  GLU GLU J . n 
J 1 79  ARG 79  79  79  ARG ARG J . n 
J 1 80  HIS 80  80  80  HIS HIS J . n 
J 1 81  VAL 81  81  81  VAL VAL J . n 
J 1 82  GLY 82  82  82  GLY GLY J . n 
J 1 83  ASP 83  83  83  ASP ASP J . n 
J 1 84  LEU 84  84  84  LEU LEU J . n 
J 1 85  GLY 85  85  85  GLY GLY J . n 
J 1 86  ASN 86  86  86  ASN ASN J . n 
J 1 87  VAL 87  87  87  VAL VAL J . n 
J 1 88  THR 88  88  88  THR THR J . n 
J 1 89  ALA 89  89  89  ALA ALA J . n 
J 1 90  ASP 90  90  90  ASP ASP J . n 
J 1 91  LYS 91  91  91  LYS LYS J . n 
J 1 92  ASP 92  92  92  ASP ASP J . n 
J 1 93  GLY 93  93  93  GLY GLY J . n 
J 1 94  VAL 94  94  94  VAL VAL J . n 
J 1 95  ALA 95  95  95  ALA ALA J . n 
J 1 96  ASP 96  96  96  ASP ASP J . n 
J 1 97  VAL 97  97  97  VAL VAL J . n 
J 1 98  SER 98  98  98  SER SER J . n 
J 1 99  ILE 99  99  99  ILE ILE J . n 
J 1 100 GLU 100 100 100 GLU GLU J . n 
J 1 101 ASP 101 101 101 ASP ASP J . n 
J 1 102 SER 102 102 102 SER SER J . n 
J 1 103 VAL 103 103 103 VAL VAL J . n 
J 1 104 ILE 104 104 104 ILE ILE J . n 
J 1 105 SER 105 105 105 SER SER J . n 
J 1 106 LEU 106 106 106 LEU LEU J . n 
J 1 107 SER 107 107 107 SER SER J . n 
J 1 108 GLY 108 108 108 GLY GLY J . n 
J 1 109 ASP 109 109 109 ASP ASP J . n 
J 1 110 HIS 110 110 110 HIS HIS J . n 
J 1 111 CYS 111 111 111 CYS CYS J . n 
J 1 112 ILE 112 112 112 ILE ILE J . n 
J 1 113 ILE 113 113 113 ILE ILE J . n 
J 1 114 GLY 114 114 114 GLY GLY J . n 
J 1 115 ARG 115 115 115 ARG ARG J . n 
J 1 116 THR 116 116 116 THR THR J . n 
J 1 117 LEU 117 117 117 LEU LEU J . n 
J 1 118 VAL 118 118 118 VAL VAL J . n 
J 1 119 VAL 119 119 119 VAL VAL J . n 
J 1 120 HIS 120 120 120 HIS HIS J . n 
J 1 121 GLU 121 121 121 GLU GLU J . n 
J 1 122 LYS 122 122 122 LYS LYS J . n 
J 1 123 ALA 123 123 123 ALA ALA J . n 
J 1 124 ASP 124 124 124 ASP ASP J . n 
J 1 125 ASP 125 125 125 ASP ASP J . n 
J 1 126 LEU 126 126 126 LEU LEU J . n 
J 1 127 GLY 127 127 127 GLY GLY J . n 
J 1 128 LYS 128 128 128 LYS LYS J . n 
J 1 129 GLY 129 129 129 GLY GLY J . n 
J 1 130 GLY 130 130 130 GLY GLY J . n 
J 1 131 ASN 131 131 131 ASN ASN J . n 
J 1 132 GLU 132 132 132 GLU GLU J . n 
J 1 133 GLU 133 133 133 GLU GLU J . n 
J 1 134 SER 134 134 134 SER SER J . n 
J 1 135 THR 135 135 135 THR THR J . n 
J 1 136 LYS 136 136 136 LYS LYS J . n 
J 1 137 THR 137 137 137 THR THR J . n 
J 1 138 GLY 138 138 138 GLY GLY J . n 
J 1 139 ASN 139 139 139 ASN ASN J . n 
J 1 140 ALA 140 140 140 ALA ALA J . n 
J 1 141 GLY 141 141 141 GLY GLY J . n 
J 1 142 SER 142 142 142 SER SER J . n 
J 1 143 ARG 143 143 143 ARG ARG J . n 
J 1 144 LEU 144 144 144 LEU LEU J . n 
J 1 145 ALA 145 145 145 ALA ALA J . n 
J 1 146 CYS 146 146 146 CYS CYS J . n 
J 1 147 GLY 147 147 147 GLY GLY J . n 
J 1 148 VAL 148 148 148 VAL VAL J . n 
J 1 149 ILE 149 149 149 ILE ILE J . n 
J 1 150 GLY 150 150 150 GLY GLY J . n 
J 1 151 ILE 151 151 151 ILE ILE J . n 
J 1 152 ALA 152 152 152 ALA ALA J . n 
J 1 153 GLN 153 153 153 GLN GLN J . n 
K 1 1   ALA 1   1   1   ALA ALA K . n 
K 1 2   THR 2   2   2   THR THR K . n 
K 1 3   LYS 3   3   3   LYS LYS K . n 
K 1 4   ALA 4   4   4   ALA ALA K . n 
K 1 5   VAL 5   5   5   VAL VAL K . n 
K 1 6   CYS 6   6   6   CYS CYS K . n 
K 1 7   VAL 7   7   7   VAL VAL K . n 
K 1 8   LEU 8   8   8   LEU LEU K . n 
K 1 9   LYS 9   9   9   LYS LYS K . n 
K 1 10  GLY 10  10  10  GLY GLY K . n 
K 1 11  ASP 11  11  11  ASP ASP K . n 
K 1 12  GLY 12  12  12  GLY GLY K . n 
K 1 13  PRO 13  13  13  PRO PRO K . n 
K 1 14  VAL 14  14  14  VAL VAL K . n 
K 1 15  GLN 15  15  15  GLN GLN K . n 
K 1 16  GLY 16  16  16  GLY GLY K . n 
K 1 17  ILE 17  17  17  ILE ILE K . n 
K 1 18  ILE 18  18  18  ILE ILE K . n 
K 1 19  ASN 19  19  19  ASN ASN K . n 
K 1 20  PHE 20  20  20  PHE PHE K . n 
K 1 21  GLU 21  21  21  GLU GLU K . n 
K 1 22  GLN 22  22  22  GLN GLN K . n 
K 1 23  LYS 23  23  23  LYS LYS K . n 
K 1 24  GLU 24  24  24  GLU GLU K . n 
K 1 25  SER 25  25  25  SER SER K . n 
K 1 26  ASN 26  26  26  ASN ASN K . n 
K 1 27  GLY 27  27  27  GLY GLY K . n 
K 1 28  PRO 28  28  28  PRO PRO K . n 
K 1 29  VAL 29  29  29  VAL VAL K . n 
K 1 30  LYS 30  30  30  LYS LYS K . n 
K 1 31  VAL 31  31  31  VAL VAL K . n 
K 1 32  TRP 32  32  32  TRP TRP K . n 
K 1 33  GLY 33  33  33  GLY GLY K . n 
K 1 34  SER 34  34  34  SER SER K . n 
K 1 35  ILE 35  35  35  ILE ILE K . n 
K 1 36  LYS 36  36  36  LYS LYS K . n 
K 1 37  GLY 37  37  37  GLY GLY K . n 
K 1 38  LEU 38  38  38  LEU LEU K . n 
K 1 39  THR 39  39  39  THR THR K . n 
K 1 40  GLU 40  40  40  GLU GLU K . n 
K 1 41  GLY 41  41  41  GLY GLY K . n 
K 1 42  LEU 42  42  42  LEU LEU K . n 
K 1 43  HIS 43  43  43  HIS HIS K . n 
K 1 44  GLY 44  44  44  GLY GLY K . n 
K 1 45  PHE 45  45  45  PHE PHE K . n 
K 1 46  HIS 46  46  46  HIS HIS K . n 
K 1 47  VAL 47  47  47  VAL VAL K . n 
K 1 48  HIS 48  48  48  HIS HIS K . n 
K 1 49  GLU 49  49  49  GLU GLU K . n 
K 1 50  PHE 50  50  50  PHE PHE K . n 
K 1 51  GLY 51  51  51  GLY GLY K . n 
K 1 52  ASP 52  52  52  ASP ASP K . n 
K 1 53  ASN 53  53  53  ASN ASN K . n 
K 1 54  THR 54  54  54  THR THR K . n 
K 1 55  ALA 55  55  55  ALA ALA K . n 
K 1 56  GLY 56  56  56  GLY GLY K . n 
K 1 57  SER 57  57  57  SER SER K . n 
K 1 58  THR 58  58  58  THR THR K . n 
K 1 59  SER 59  59  59  SER SER K . n 
K 1 60  ALA 60  60  60  ALA ALA K . n 
K 1 61  GLY 61  61  61  GLY GLY K . n 
K 1 62  PRO 62  62  62  PRO PRO K . n 
K 1 63  HIS 63  63  63  HIS HIS K . n 
K 1 64  PHE 64  64  64  PHE PHE K . n 
K 1 65  ASN 65  65  65  ASN ASN K . n 
K 1 66  PRO 66  66  66  PRO PRO K . n 
K 1 67  LEU 67  67  67  LEU LEU K . n 
K 1 68  SER 68  68  68  SER SER K . n 
K 1 69  ARG 69  69  69  ARG ARG K . n 
K 1 70  LYS 70  70  70  LYS LYS K . n 
K 1 71  HIS 71  71  71  HIS HIS K . n 
K 1 72  GLY 72  72  72  GLY GLY K . n 
K 1 73  GLY 73  73  73  GLY GLY K . n 
K 1 74  PRO 74  74  74  PRO PRO K . n 
K 1 75  LYS 75  75  75  LYS LYS K . n 
K 1 76  ASP 76  76  76  ASP ASP K . n 
K 1 77  GLU 77  77  77  GLU GLU K . n 
K 1 78  GLU 78  78  78  GLU GLU K . n 
K 1 79  ARG 79  79  79  ARG ARG K . n 
K 1 80  HIS 80  80  80  HIS HIS K . n 
K 1 81  VAL 81  81  81  VAL VAL K . n 
K 1 82  GLY 82  82  82  GLY GLY K . n 
K 1 83  ASP 83  83  83  ASP ASP K . n 
K 1 84  LEU 84  84  84  LEU LEU K . n 
K 1 85  GLY 85  85  85  GLY GLY K . n 
K 1 86  ASN 86  86  86  ASN ASN K . n 
K 1 87  VAL 87  87  87  VAL VAL K . n 
K 1 88  THR 88  88  88  THR THR K . n 
K 1 89  ALA 89  89  89  ALA ALA K . n 
K 1 90  ASP 90  90  90  ASP ASP K . n 
K 1 91  LYS 91  91  91  LYS LYS K . n 
K 1 92  ASP 92  92  92  ASP ASP K . n 
K 1 93  GLY 93  93  93  GLY GLY K . n 
K 1 94  VAL 94  94  94  VAL VAL K . n 
K 1 95  ALA 95  95  95  ALA ALA K . n 
K 1 96  ASP 96  96  96  ASP ASP K . n 
K 1 97  VAL 97  97  97  VAL VAL K . n 
K 1 98  SER 98  98  98  SER SER K . n 
K 1 99  ILE 99  99  99  ILE ILE K . n 
K 1 100 GLU 100 100 100 GLU GLU K . n 
K 1 101 ASP 101 101 101 ASP ASP K . n 
K 1 102 SER 102 102 102 SER SER K . n 
K 1 103 VAL 103 103 103 VAL VAL K . n 
K 1 104 ILE 104 104 104 ILE ILE K . n 
K 1 105 SER 105 105 105 SER SER K . n 
K 1 106 LEU 106 106 106 LEU LEU K . n 
K 1 107 SER 107 107 107 SER SER K . n 
K 1 108 GLY 108 108 108 GLY GLY K . n 
K 1 109 ASP 109 109 109 ASP ASP K . n 
K 1 110 HIS 110 110 110 HIS HIS K . n 
K 1 111 CYS 111 111 111 CYS CYS K . n 
K 1 112 ILE 112 112 112 ILE ILE K . n 
K 1 113 ILE 113 113 113 ILE ILE K . n 
K 1 114 GLY 114 114 114 GLY GLY K . n 
K 1 115 ARG 115 115 115 ARG ARG K . n 
K 1 116 THR 116 116 116 THR THR K . n 
K 1 117 LEU 117 117 117 LEU LEU K . n 
K 1 118 VAL 118 118 118 VAL VAL K . n 
K 1 119 VAL 119 119 119 VAL VAL K . n 
K 1 120 HIS 120 120 120 HIS HIS K . n 
K 1 121 GLU 121 121 121 GLU GLU K . n 
K 1 122 LYS 122 122 122 LYS LYS K . n 
K 1 123 ALA 123 123 123 ALA ALA K . n 
K 1 124 ASP 124 124 124 ASP ASP K . n 
K 1 125 ASP 125 125 125 ASP ASP K . n 
K 1 126 LEU 126 126 126 LEU LEU K . n 
K 1 127 GLY 127 127 127 GLY GLY K . n 
K 1 128 LYS 128 128 128 LYS LYS K . n 
K 1 129 GLY 129 129 129 GLY GLY K . n 
K 1 130 GLY 130 130 130 GLY GLY K . n 
K 1 131 ASN 131 131 131 ASN ASN K . n 
K 1 132 GLU 132 132 132 GLU GLU K . n 
K 1 133 GLU 133 133 133 GLU GLU K . n 
K 1 134 SER 134 134 134 SER SER K . n 
K 1 135 THR 135 135 135 THR THR K . n 
K 1 136 LYS 136 136 136 LYS LYS K . n 
K 1 137 THR 137 137 137 THR THR K . n 
K 1 138 GLY 138 138 138 GLY GLY K . n 
K 1 139 ASN 139 139 139 ASN ASN K . n 
K 1 140 ALA 140 140 140 ALA ALA K . n 
K 1 141 GLY 141 141 141 GLY GLY K . n 
K 1 142 SER 142 142 142 SER SER K . n 
K 1 143 ARG 143 143 143 ARG ARG K . n 
K 1 144 LEU 144 144 144 LEU LEU K . n 
K 1 145 ALA 145 145 145 ALA ALA K . n 
K 1 146 CYS 146 146 146 CYS CYS K . n 
K 1 147 GLY 147 147 147 GLY GLY K . n 
K 1 148 VAL 148 148 148 VAL VAL K . n 
K 1 149 ILE 149 149 149 ILE ILE K . n 
K 1 150 GLY 150 150 150 GLY GLY K . n 
K 1 151 ILE 151 151 151 ILE ILE K . n 
K 1 152 ALA 152 152 152 ALA ALA K . n 
K 1 153 GLN 153 153 153 GLN GLN K . n 
L 1 1   ALA 1   1   1   ALA ALA L . n 
L 1 2   THR 2   2   2   THR THR L . n 
L 1 3   LYS 3   3   3   LYS LYS L . n 
L 1 4   ALA 4   4   4   ALA ALA L . n 
L 1 5   VAL 5   5   5   VAL VAL L . n 
L 1 6   CYS 6   6   6   CYS CYS L . n 
L 1 7   VAL 7   7   7   VAL VAL L . n 
L 1 8   LEU 8   8   8   LEU LEU L . n 
L 1 9   LYS 9   9   9   LYS LYS L . n 
L 1 10  GLY 10  10  10  GLY GLY L . n 
L 1 11  ASP 11  11  11  ASP ASP L . n 
L 1 12  GLY 12  12  12  GLY GLY L . n 
L 1 13  PRO 13  13  13  PRO PRO L . n 
L 1 14  VAL 14  14  14  VAL VAL L . n 
L 1 15  GLN 15  15  15  GLN GLN L . n 
L 1 16  GLY 16  16  16  GLY GLY L . n 
L 1 17  ILE 17  17  17  ILE ILE L . n 
L 1 18  ILE 18  18  18  ILE ILE L . n 
L 1 19  ASN 19  19  19  ASN ASN L . n 
L 1 20  PHE 20  20  20  PHE PHE L . n 
L 1 21  GLU 21  21  21  GLU GLU L . n 
L 1 22  GLN 22  22  22  GLN GLN L . n 
L 1 23  LYS 23  23  23  LYS LYS L . n 
L 1 24  GLU 24  24  24  GLU GLU L . n 
L 1 25  SER 25  25  25  SER SER L . n 
L 1 26  ASN 26  26  26  ASN ASN L . n 
L 1 27  GLY 27  27  27  GLY GLY L . n 
L 1 28  PRO 28  28  28  PRO PRO L . n 
L 1 29  VAL 29  29  29  VAL VAL L . n 
L 1 30  LYS 30  30  30  LYS LYS L . n 
L 1 31  VAL 31  31  31  VAL VAL L . n 
L 1 32  TRP 32  32  32  TRP TRP L . n 
L 1 33  GLY 33  33  33  GLY GLY L . n 
L 1 34  SER 34  34  34  SER SER L . n 
L 1 35  ILE 35  35  35  ILE ILE L . n 
L 1 36  LYS 36  36  36  LYS LYS L . n 
L 1 37  GLY 37  37  37  GLY GLY L . n 
L 1 38  LEU 38  38  38  LEU LEU L . n 
L 1 39  THR 39  39  39  THR THR L . n 
L 1 40  GLU 40  40  40  GLU GLU L . n 
L 1 41  GLY 41  41  41  GLY GLY L . n 
L 1 42  LEU 42  42  42  LEU LEU L . n 
L 1 43  HIS 43  43  43  HIS HIS L . n 
L 1 44  GLY 44  44  44  GLY GLY L . n 
L 1 45  PHE 45  45  45  PHE PHE L . n 
L 1 46  HIS 46  46  46  HIS HIS L . n 
L 1 47  VAL 47  47  47  VAL VAL L . n 
L 1 48  HIS 48  48  48  HIS HIS L . n 
L 1 49  GLU 49  49  49  GLU GLU L . n 
L 1 50  PHE 50  50  50  PHE PHE L . n 
L 1 51  GLY 51  51  51  GLY GLY L . n 
L 1 52  ASP 52  52  52  ASP ASP L . n 
L 1 53  ASN 53  53  53  ASN ASN L . n 
L 1 54  THR 54  54  54  THR THR L . n 
L 1 55  ALA 55  55  55  ALA ALA L . n 
L 1 56  GLY 56  56  56  GLY GLY L . n 
L 1 57  SER 57  57  57  SER SER L . n 
L 1 58  THR 58  58  58  THR THR L . n 
L 1 59  SER 59  59  59  SER SER L . n 
L 1 60  ALA 60  60  60  ALA ALA L . n 
L 1 61  GLY 61  61  61  GLY GLY L . n 
L 1 62  PRO 62  62  62  PRO PRO L . n 
L 1 63  HIS 63  63  63  HIS HIS L . n 
L 1 64  PHE 64  64  64  PHE PHE L . n 
L 1 65  ASN 65  65  65  ASN ASN L . n 
L 1 66  PRO 66  66  66  PRO PRO L . n 
L 1 67  LEU 67  67  67  LEU LEU L . n 
L 1 68  SER 68  68  68  SER SER L . n 
L 1 69  ARG 69  69  69  ARG ARG L . n 
L 1 70  LYS 70  70  70  LYS LYS L . n 
L 1 71  HIS 71  71  71  HIS HIS L . n 
L 1 72  GLY 72  72  72  GLY GLY L . n 
L 1 73  GLY 73  73  73  GLY GLY L . n 
L 1 74  PRO 74  74  74  PRO PRO L . n 
L 1 75  LYS 75  75  75  LYS LYS L . n 
L 1 76  ASP 76  76  76  ASP ASP L . n 
L 1 77  GLU 77  77  77  GLU GLU L . n 
L 1 78  GLU 78  78  78  GLU GLU L . n 
L 1 79  ARG 79  79  79  ARG ARG L . n 
L 1 80  HIS 80  80  80  HIS HIS L . n 
L 1 81  VAL 81  81  81  VAL VAL L . n 
L 1 82  GLY 82  82  82  GLY GLY L . n 
L 1 83  ASP 83  83  83  ASP ASP L . n 
L 1 84  LEU 84  84  84  LEU LEU L . n 
L 1 85  GLY 85  85  85  GLY GLY L . n 
L 1 86  ASN 86  86  86  ASN ASN L . n 
L 1 87  VAL 87  87  87  VAL VAL L . n 
L 1 88  THR 88  88  88  THR THR L . n 
L 1 89  ALA 89  89  89  ALA ALA L . n 
L 1 90  ASP 90  90  90  ASP ASP L . n 
L 1 91  LYS 91  91  91  LYS LYS L . n 
L 1 92  ASP 92  92  92  ASP ASP L . n 
L 1 93  GLY 93  93  93  GLY GLY L . n 
L 1 94  VAL 94  94  94  VAL VAL L . n 
L 1 95  ALA 95  95  95  ALA ALA L . n 
L 1 96  ASP 96  96  96  ASP ASP L . n 
L 1 97  VAL 97  97  97  VAL VAL L . n 
L 1 98  SER 98  98  98  SER SER L . n 
L 1 99  ILE 99  99  99  ILE ILE L . n 
L 1 100 GLU 100 100 100 GLU GLU L . n 
L 1 101 ASP 101 101 101 ASP ASP L . n 
L 1 102 SER 102 102 102 SER SER L . n 
L 1 103 VAL 103 103 103 VAL VAL L . n 
L 1 104 ILE 104 104 104 ILE ILE L . n 
L 1 105 SER 105 105 105 SER SER L . n 
L 1 106 LEU 106 106 106 LEU LEU L . n 
L 1 107 SER 107 107 107 SER SER L . n 
L 1 108 GLY 108 108 108 GLY GLY L . n 
L 1 109 ASP 109 109 109 ASP ASP L . n 
L 1 110 HIS 110 110 110 HIS HIS L . n 
L 1 111 CYS 111 111 111 CYS CYS L . n 
L 1 112 ILE 112 112 112 ILE ILE L . n 
L 1 113 ILE 113 113 113 ILE ILE L . n 
L 1 114 GLY 114 114 114 GLY GLY L . n 
L 1 115 ARG 115 115 115 ARG ARG L . n 
L 1 116 THR 116 116 116 THR THR L . n 
L 1 117 LEU 117 117 117 LEU LEU L . n 
L 1 118 VAL 118 118 118 VAL VAL L . n 
L 1 119 VAL 119 119 119 VAL VAL L . n 
L 1 120 HIS 120 120 120 HIS HIS L . n 
L 1 121 GLU 121 121 121 GLU GLU L . n 
L 1 122 LYS 122 122 122 LYS LYS L . n 
L 1 123 ALA 123 123 123 ALA ALA L . n 
L 1 124 ASP 124 124 124 ASP ASP L . n 
L 1 125 ASP 125 125 125 ASP ASP L . n 
L 1 126 LEU 126 126 126 LEU LEU L . n 
L 1 127 GLY 127 127 127 GLY GLY L . n 
L 1 128 LYS 128 128 128 LYS LYS L . n 
L 1 129 GLY 129 129 129 GLY GLY L . n 
L 1 130 GLY 130 130 130 GLY GLY L . n 
L 1 131 ASN 131 131 131 ASN ASN L . n 
L 1 132 GLU 132 132 132 GLU GLU L . n 
L 1 133 GLU 133 133 133 GLU GLU L . n 
L 1 134 SER 134 134 134 SER SER L . n 
L 1 135 THR 135 135 135 THR THR L . n 
L 1 136 LYS 136 136 136 LYS LYS L . n 
L 1 137 THR 137 137 137 THR THR L . n 
L 1 138 GLY 138 138 138 GLY GLY L . n 
L 1 139 ASN 139 139 139 ASN ASN L . n 
L 1 140 ALA 140 140 140 ALA ALA L . n 
L 1 141 GLY 141 141 141 GLY GLY L . n 
L 1 142 SER 142 142 142 SER SER L . n 
L 1 143 ARG 143 143 143 ARG ARG L . n 
L 1 144 LEU 144 144 144 LEU LEU L . n 
L 1 145 ALA 145 145 145 ALA ALA L . n 
L 1 146 CYS 146 146 146 CYS CYS L . n 
L 1 147 GLY 147 147 147 GLY GLY L . n 
L 1 148 VAL 148 148 148 VAL VAL L . n 
L 1 149 ILE 149 149 149 ILE ILE L . n 
L 1 150 GLY 150 150 150 GLY GLY L . n 
L 1 151 ILE 151 151 151 ILE ILE L . n 
L 1 152 ALA 152 152 152 ALA ALA L . n 
L 1 153 GLN 153 153 153 GLN GLN L . n 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA dimeric 2 
2 author_and_software_defined_assembly PISA dimeric 2 
3 author_and_software_defined_assembly PISA dimeric 2 
4 author_and_software_defined_assembly PISA dimeric 2 
5 author_and_software_defined_assembly PISA dimeric 2 
6 author_and_software_defined_assembly PISA dimeric 2 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,M,N,O,P,Q,R,S,YA,ZA        
2 1 C,D,T,U,V,W,X,Y,AB,BB          
3 1 E,F,Z,AA,BA,CA,DA,EA,CB,DB     
4 1 G,H,FA,GA,HA,IA,JA,KA,LA,EB,FB 
5 1 I,J,MA,NA,OA,PA,QA,RA,GB,HB    
6 1 K,L,SA,TA,UA,VA,WA,XA,IB,JB    
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 2270  ? 
1 MORE         -140  ? 
1 'SSA (A^2)'  13800 ? 
2 'ABSA (A^2)' 1980  ? 
2 MORE         -103  ? 
2 'SSA (A^2)'  13960 ? 
3 'ABSA (A^2)' 2110  ? 
3 MORE         -132  ? 
3 'SSA (A^2)'  13840 ? 
4 'ABSA (A^2)' 2110  ? 
4 MORE         -135  ? 
4 'SSA (A^2)'  14000 ? 
5 'ABSA (A^2)' 1910  ? 
5 MORE         -78   ? 
5 'SSA (A^2)'  14030 ? 
6 'ABSA (A^2)' 2120  ? 
6 MORE         -115  ? 
6 'SSA (A^2)'  13910 ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1   OD1 ? B  ASP 83  ? B ASP 83  ? 1_555 ZN ? Q  ZN . ? B ZN 202 ? 1_555 ND1 ? B  HIS 63  ? B HIS 63  ? 1_555 104.1 ? 
2   OD1 ? B  ASP 83  ? B ASP 83  ? 1_555 ZN ? Q  ZN . ? B ZN 202 ? 1_555 ND1 ? B  HIS 71  ? B HIS 71  ? 1_555 94.0  ? 
3   ND1 ? B  HIS 63  ? B HIS 63  ? 1_555 ZN ? Q  ZN . ? B ZN 202 ? 1_555 ND1 ? B  HIS 71  ? B HIS 71  ? 1_555 101.1 ? 
4   OD1 ? B  ASP 83  ? B ASP 83  ? 1_555 ZN ? Q  ZN . ? B ZN 202 ? 1_555 ND1 ? B  HIS 80  ? B HIS 80  ? 1_555 122.1 ? 
5   ND1 ? B  HIS 63  ? B HIS 63  ? 1_555 ZN ? Q  ZN . ? B ZN 202 ? 1_555 ND1 ? B  HIS 80  ? B HIS 80  ? 1_555 109.3 ? 
6   ND1 ? B  HIS 71  ? B HIS 71  ? 1_555 ZN ? Q  ZN . ? B ZN 202 ? 1_555 ND1 ? B  HIS 80  ? B HIS 80  ? 1_555 122.9 ? 
7   NE2 ? H  HIS 120 ? H HIS 120 ? 1_555 ZN ? IA ZN . ? H ZN 201 ? 1_555 NE2 ? H  HIS 48  ? H HIS 48  ? 1_555 126.7 ? 
8   NE2 ? H  HIS 120 ? H HIS 120 ? 1_555 ZN ? IA ZN . ? H ZN 201 ? 1_555 O4  ? KA SO4 .   ? H SO4 203 ? 1_555 99.4  ? 
9   NE2 ? H  HIS 48  ? H HIS 48  ? 1_555 ZN ? IA ZN . ? H ZN 201 ? 1_555 O4  ? KA SO4 .   ? H SO4 203 ? 1_555 103.7 ? 
10  NE2 ? H  HIS 120 ? H HIS 120 ? 1_555 ZN ? IA ZN . ? H ZN 201 ? 1_555 ND1 ? H  HIS 46  ? H HIS 46  ? 1_555 92.7  ? 
11  NE2 ? H  HIS 48  ? H HIS 48  ? 1_555 ZN ? IA ZN . ? H ZN 201 ? 1_555 ND1 ? H  HIS 46  ? H HIS 46  ? 1_555 119.6 ? 
12  O4  ? KA SO4 .   ? H SO4 203 ? 1_555 ZN ? IA ZN . ? H ZN 201 ? 1_555 ND1 ? H  HIS 46  ? H HIS 46  ? 1_555 113.4 ? 
13  ND1 ? F  HIS 80  ? F HIS 80  ? 1_555 ZN ? DA ZN . ? F ZN 202 ? 1_555 ND1 ? F  HIS 71  ? F HIS 71  ? 1_555 139.4 ? 
14  ND1 ? F  HIS 80  ? F HIS 80  ? 1_555 ZN ? DA ZN . ? F ZN 202 ? 1_555 ND1 ? F  HIS 63  ? F HIS 63  ? 1_555 110.2 ? 
15  ND1 ? F  HIS 71  ? F HIS 71  ? 1_555 ZN ? DA ZN . ? F ZN 202 ? 1_555 ND1 ? F  HIS 63  ? F HIS 63  ? 1_555 102.9 ? 
16  ND1 ? F  HIS 80  ? F HIS 80  ? 1_555 ZN ? DA ZN . ? F ZN 202 ? 1_555 OD1 ? F  ASP 83  ? F ASP 83  ? 1_555 81.5  ? 
17  ND1 ? F  HIS 71  ? F HIS 71  ? 1_555 ZN ? DA ZN . ? F ZN 202 ? 1_555 OD1 ? F  ASP 83  ? F ASP 83  ? 1_555 110.4 ? 
18  ND1 ? F  HIS 63  ? F HIS 63  ? 1_555 ZN ? DA ZN . ? F ZN 202 ? 1_555 OD1 ? F  ASP 83  ? F ASP 83  ? 1_555 107.8 ? 
19  NE2 ? D  HIS 120 ? D HIS 120 ? 1_555 ZN ? W  ZN . ? D ZN 201 ? 1_555 NE2 ? D  HIS 48  ? D HIS 48  ? 1_555 118.3 ? 
20  NE2 ? D  HIS 120 ? D HIS 120 ? 1_555 ZN ? W  ZN . ? D ZN 201 ? 1_555 ND1 ? D  HIS 46  ? D HIS 46  ? 1_555 93.9  ? 
21  NE2 ? D  HIS 48  ? D HIS 48  ? 1_555 ZN ? W  ZN . ? D ZN 201 ? 1_555 ND1 ? D  HIS 46  ? D HIS 46  ? 1_555 137.1 ? 
22  OD1 ? D  ASP 83  ? D ASP 83  ? 1_555 ZN ? X  ZN . ? D ZN 202 ? 1_555 ND1 ? D  HIS 80  ? D HIS 80  ? 1_555 117.3 ? 
23  OD1 ? D  ASP 83  ? D ASP 83  ? 1_555 ZN ? X  ZN . ? D ZN 202 ? 1_555 ND1 ? D  HIS 71  ? D HIS 71  ? 1_555 96.8  ? 
24  ND1 ? D  HIS 80  ? D HIS 80  ? 1_555 ZN ? X  ZN . ? D ZN 202 ? 1_555 ND1 ? D  HIS 71  ? D HIS 71  ? 1_555 119.9 ? 
25  OD1 ? D  ASP 83  ? D ASP 83  ? 1_555 ZN ? X  ZN . ? D ZN 202 ? 1_555 ND1 ? D  HIS 63  ? D HIS 63  ? 1_555 106.1 ? 
26  ND1 ? D  HIS 80  ? D HIS 80  ? 1_555 ZN ? X  ZN . ? D ZN 202 ? 1_555 ND1 ? D  HIS 63  ? D HIS 63  ? 1_555 110.9 ? 
27  ND1 ? D  HIS 71  ? D HIS 71  ? 1_555 ZN ? X  ZN . ? D ZN 202 ? 1_555 ND1 ? D  HIS 63  ? D HIS 63  ? 1_555 103.9 ? 
28  OD1 ? J  ASP 83  ? J ASP 83  ? 1_555 ZN ? QA ZN . ? J ZN 202 ? 1_555 ND1 ? J  HIS 80  ? J HIS 80  ? 1_555 111.9 ? 
29  OD1 ? J  ASP 83  ? J ASP 83  ? 1_555 ZN ? QA ZN . ? J ZN 202 ? 1_555 ND1 ? J  HIS 63  ? J HIS 63  ? 1_555 105.4 ? 
30  ND1 ? J  HIS 80  ? J HIS 80  ? 1_555 ZN ? QA ZN . ? J ZN 202 ? 1_555 ND1 ? J  HIS 63  ? J HIS 63  ? 1_555 111.6 ? 
31  OD1 ? J  ASP 83  ? J ASP 83  ? 1_555 ZN ? QA ZN . ? J ZN 202 ? 1_555 ND1 ? J  HIS 71  ? J HIS 71  ? 1_555 102.0 ? 
32  ND1 ? J  HIS 80  ? J HIS 80  ? 1_555 ZN ? QA ZN . ? J ZN 202 ? 1_555 ND1 ? J  HIS 71  ? J HIS 71  ? 1_555 121.0 ? 
33  ND1 ? J  HIS 63  ? J HIS 63  ? 1_555 ZN ? QA ZN . ? J ZN 202 ? 1_555 ND1 ? J  HIS 71  ? J HIS 71  ? 1_555 103.5 ? 
34  OD1 ? L  ASP 83  ? L ASP 83  ? 1_555 ZN ? WA ZN . ? L ZN 202 ? 1_555 ND1 ? L  HIS 80  ? L HIS 80  ? 1_555 109.2 ? 
35  OD1 ? L  ASP 83  ? L ASP 83  ? 1_555 ZN ? WA ZN . ? L ZN 202 ? 1_555 ND1 ? L  HIS 63  ? L HIS 63  ? 1_555 106.2 ? 
36  ND1 ? L  HIS 80  ? L HIS 80  ? 1_555 ZN ? WA ZN . ? L ZN 202 ? 1_555 ND1 ? L  HIS 63  ? L HIS 63  ? 1_555 105.7 ? 
37  OD1 ? L  ASP 83  ? L ASP 83  ? 1_555 ZN ? WA ZN . ? L ZN 202 ? 1_555 ND1 ? L  HIS 71  ? L HIS 71  ? 1_555 104.2 ? 
38  ND1 ? L  HIS 80  ? L HIS 80  ? 1_555 ZN ? WA ZN . ? L ZN 202 ? 1_555 ND1 ? L  HIS 71  ? L HIS 71  ? 1_555 126.5 ? 
39  ND1 ? L  HIS 63  ? L HIS 63  ? 1_555 ZN ? WA ZN . ? L ZN 202 ? 1_555 ND1 ? L  HIS 71  ? L HIS 71  ? 1_555 103.5 ? 
40  OD1 ? G  ASP 83  ? G ASP 83  ? 1_555 ZN ? GA ZN . ? G ZN 202 ? 1_555 ND1 ? G  HIS 63  ? G HIS 63  ? 1_555 97.0  ? 
41  OD1 ? G  ASP 83  ? G ASP 83  ? 1_555 ZN ? GA ZN . ? G ZN 202 ? 1_555 ND1 ? G  HIS 80  ? G HIS 80  ? 1_555 119.5 ? 
42  ND1 ? G  HIS 63  ? G HIS 63  ? 1_555 ZN ? GA ZN . ? G ZN 202 ? 1_555 ND1 ? G  HIS 80  ? G HIS 80  ? 1_555 114.0 ? 
43  OD1 ? G  ASP 83  ? G ASP 83  ? 1_555 ZN ? GA ZN . ? G ZN 202 ? 1_555 ND1 ? G  HIS 71  ? G HIS 71  ? 1_555 94.2  ? 
44  ND1 ? G  HIS 63  ? G HIS 63  ? 1_555 ZN ? GA ZN . ? G ZN 202 ? 1_555 ND1 ? G  HIS 71  ? G HIS 71  ? 1_555 103.9 ? 
45  ND1 ? G  HIS 80  ? G HIS 80  ? 1_555 ZN ? GA ZN . ? G ZN 202 ? 1_555 ND1 ? G  HIS 71  ? G HIS 71  ? 1_555 123.5 ? 
46  OD1 ? H  ASP 83  ? H ASP 83  ? 1_555 ZN ? JA ZN . ? H ZN 202 ? 1_555 ND1 ? H  HIS 71  ? H HIS 71  ? 1_555 96.7  ? 
47  OD1 ? H  ASP 83  ? H ASP 83  ? 1_555 ZN ? JA ZN . ? H ZN 202 ? 1_555 ND1 ? H  HIS 80  ? H HIS 80  ? 1_555 111.9 ? 
48  ND1 ? H  HIS 71  ? H HIS 71  ? 1_555 ZN ? JA ZN . ? H ZN 202 ? 1_555 ND1 ? H  HIS 80  ? H HIS 80  ? 1_555 126.9 ? 
49  OD1 ? H  ASP 83  ? H ASP 83  ? 1_555 ZN ? JA ZN . ? H ZN 202 ? 1_555 ND1 ? H  HIS 63  ? H HIS 63  ? 1_555 101.4 ? 
50  ND1 ? H  HIS 71  ? H HIS 71  ? 1_555 ZN ? JA ZN . ? H ZN 202 ? 1_555 ND1 ? H  HIS 63  ? H HIS 63  ? 1_555 108.3 ? 
51  ND1 ? H  HIS 80  ? H HIS 80  ? 1_555 ZN ? JA ZN . ? H ZN 202 ? 1_555 ND1 ? H  HIS 63  ? H HIS 63  ? 1_555 108.4 ? 
52  NE2 ? K  HIS 120 ? K HIS 120 ? 1_555 ZN ? SA ZN . ? K ZN 201 ? 1_555 O3  ? UA SO4 .   ? K SO4 203 ? 1_555 97.5  ? 
53  NE2 ? K  HIS 120 ? K HIS 120 ? 1_555 ZN ? SA ZN . ? K ZN 201 ? 1_555 NE2 ? K  HIS 48  ? K HIS 48  ? 1_555 118.9 ? 
54  O3  ? UA SO4 .   ? K SO4 203 ? 1_555 ZN ? SA ZN . ? K ZN 201 ? 1_555 NE2 ? K  HIS 48  ? K HIS 48  ? 1_555 93.1  ? 
55  NE2 ? K  HIS 120 ? K HIS 120 ? 1_555 ZN ? SA ZN . ? K ZN 201 ? 1_555 ND1 ? K  HIS 46  ? K HIS 46  ? 1_555 85.0  ? 
56  O3  ? UA SO4 .   ? K SO4 203 ? 1_555 ZN ? SA ZN . ? K ZN 201 ? 1_555 ND1 ? K  HIS 46  ? K HIS 46  ? 1_555 115.5 ? 
57  NE2 ? K  HIS 48  ? K HIS 48  ? 1_555 ZN ? SA ZN . ? K ZN 201 ? 1_555 ND1 ? K  HIS 46  ? K HIS 46  ? 1_555 140.8 ? 
58  OD1 ? A  ASP 83  ? A ASP 83  ? 1_555 ZN ? N  ZN . ? A ZN 202 ? 1_555 ND1 ? A  HIS 80  ? A HIS 80  ? 1_555 115.7 ? 
59  OD1 ? A  ASP 83  ? A ASP 83  ? 1_555 ZN ? N  ZN . ? A ZN 202 ? 1_555 ND1 ? A  HIS 71  ? A HIS 71  ? 1_555 96.9  ? 
60  ND1 ? A  HIS 80  ? A HIS 80  ? 1_555 ZN ? N  ZN . ? A ZN 202 ? 1_555 ND1 ? A  HIS 71  ? A HIS 71  ? 1_555 126.0 ? 
61  OD1 ? A  ASP 83  ? A ASP 83  ? 1_555 ZN ? N  ZN . ? A ZN 202 ? 1_555 ND1 ? A  HIS 63  ? A HIS 63  ? 1_555 107.3 ? 
62  ND1 ? A  HIS 80  ? A HIS 80  ? 1_555 ZN ? N  ZN . ? A ZN 202 ? 1_555 ND1 ? A  HIS 63  ? A HIS 63  ? 1_555 107.4 ? 
63  ND1 ? A  HIS 71  ? A HIS 71  ? 1_555 ZN ? N  ZN . ? A ZN 202 ? 1_555 ND1 ? A  HIS 63  ? A HIS 63  ? 1_555 101.6 ? 
64  NE2 ? G  HIS 120 ? G HIS 120 ? 1_555 ZN ? FA ZN . ? G ZN 201 ? 1_555 NE2 ? G  HIS 48  ? G HIS 48  ? 1_555 126.0 ? 
65  NE2 ? G  HIS 120 ? G HIS 120 ? 1_555 ZN ? FA ZN . ? G ZN 201 ? 1_555 O1  ? HA SO4 .   ? G SO4 203 ? 1_555 101.9 ? 
66  NE2 ? G  HIS 48  ? G HIS 48  ? 1_555 ZN ? FA ZN . ? G ZN 201 ? 1_555 O1  ? HA SO4 .   ? G SO4 203 ? 1_555 105.9 ? 
67  NE2 ? G  HIS 120 ? G HIS 120 ? 1_555 ZN ? FA ZN . ? G ZN 201 ? 1_555 ND1 ? G  HIS 46  ? G HIS 46  ? 1_555 92.7  ? 
68  NE2 ? G  HIS 48  ? G HIS 48  ? 1_555 ZN ? FA ZN . ? G ZN 201 ? 1_555 ND1 ? G  HIS 46  ? G HIS 46  ? 1_555 121.5 ? 
69  O1  ? HA SO4 .   ? G SO4 203 ? 1_555 ZN ? FA ZN . ? G ZN 201 ? 1_555 ND1 ? G  HIS 46  ? G HIS 46  ? 1_555 106.3 ? 
70  NE2 ? J  HIS 120 ? J HIS 120 ? 1_555 ZN ? PA ZN . ? J ZN 201 ? 1_555 NE2 ? J  HIS 48  ? J HIS 48  ? 1_555 112.6 ? 
71  NE2 ? J  HIS 120 ? J HIS 120 ? 1_555 ZN ? PA ZN . ? J ZN 201 ? 1_555 O3  ? RA SO4 .   ? J SO4 203 ? 1_555 93.4  ? 
72  NE2 ? J  HIS 48  ? J HIS 48  ? 1_555 ZN ? PA ZN . ? J ZN 201 ? 1_555 O3  ? RA SO4 .   ? J SO4 203 ? 1_555 86.1  ? 
73  NE2 ? J  HIS 120 ? J HIS 120 ? 1_555 ZN ? PA ZN . ? J ZN 201 ? 1_555 ND1 ? J  HIS 46  ? J HIS 46  ? 1_555 99.2  ? 
74  NE2 ? J  HIS 48  ? J HIS 48  ? 1_555 ZN ? PA ZN . ? J ZN 201 ? 1_555 ND1 ? J  HIS 46  ? J HIS 46  ? 1_555 141.0 ? 
75  O3  ? RA SO4 .   ? J SO4 203 ? 1_555 ZN ? PA ZN . ? J ZN 201 ? 1_555 ND1 ? J  HIS 46  ? J HIS 46  ? 1_555 114.8 ? 
76  NE2 ? E  HIS 120 ? E HIS 120 ? 1_555 ZN ? Z  ZN . ? E ZN 201 ? 1_555 O2  ? BA SO4 .   ? E SO4 203 ? 1_555 108.7 ? 
77  NE2 ? E  HIS 120 ? E HIS 120 ? 1_555 ZN ? Z  ZN . ? E ZN 201 ? 1_555 NE2 ? E  HIS 48  ? E HIS 48  ? 1_555 129.3 ? 
78  O2  ? BA SO4 .   ? E SO4 203 ? 1_555 ZN ? Z  ZN . ? E ZN 201 ? 1_555 NE2 ? E  HIS 48  ? E HIS 48  ? 1_555 107.1 ? 
79  NE2 ? E  HIS 120 ? E HIS 120 ? 1_555 ZN ? Z  ZN . ? E ZN 201 ? 1_555 ND1 ? E  HIS 46  ? E HIS 46  ? 1_555 82.9  ? 
80  O2  ? BA SO4 .   ? E SO4 203 ? 1_555 ZN ? Z  ZN . ? E ZN 201 ? 1_555 ND1 ? E  HIS 46  ? E HIS 46  ? 1_555 92.9  ? 
81  NE2 ? E  HIS 48  ? E HIS 48  ? 1_555 ZN ? Z  ZN . ? E ZN 201 ? 1_555 ND1 ? E  HIS 46  ? E HIS 46  ? 1_555 129.5 ? 
82  OD1 ? K  ASP 83  ? K ASP 83  ? 1_555 ZN ? TA ZN . ? K ZN 202 ? 1_555 ND1 ? K  HIS 80  ? K HIS 80  ? 1_555 120.5 ? 
83  OD1 ? K  ASP 83  ? K ASP 83  ? 1_555 ZN ? TA ZN . ? K ZN 202 ? 1_555 ND1 ? K  HIS 63  ? K HIS 63  ? 1_555 99.8  ? 
84  ND1 ? K  HIS 80  ? K HIS 80  ? 1_555 ZN ? TA ZN . ? K ZN 202 ? 1_555 ND1 ? K  HIS 63  ? K HIS 63  ? 1_555 120.8 ? 
85  OD1 ? K  ASP 83  ? K ASP 83  ? 1_555 ZN ? TA ZN . ? K ZN 202 ? 1_555 ND1 ? K  HIS 71  ? K HIS 71  ? 1_555 76.1  ? 
86  ND1 ? K  HIS 80  ? K HIS 80  ? 1_555 ZN ? TA ZN . ? K ZN 202 ? 1_555 ND1 ? K  HIS 71  ? K HIS 71  ? 1_555 130.8 ? 
87  ND1 ? K  HIS 63  ? K HIS 63  ? 1_555 ZN ? TA ZN . ? K ZN 202 ? 1_555 ND1 ? K  HIS 71  ? K HIS 71  ? 1_555 97.9  ? 
88  OD1 ? I  ASP 83  ? I ASP 83  ? 1_555 ZN ? NA ZN . ? I ZN 202 ? 1_555 ND1 ? I  HIS 80  ? I HIS 80  ? 1_555 124.4 ? 
89  OD1 ? I  ASP 83  ? I ASP 83  ? 1_555 ZN ? NA ZN . ? I ZN 202 ? 1_555 ND1 ? I  HIS 71  ? I HIS 71  ? 1_555 86.1  ? 
90  ND1 ? I  HIS 80  ? I HIS 80  ? 1_555 ZN ? NA ZN . ? I ZN 202 ? 1_555 ND1 ? I  HIS 71  ? I HIS 71  ? 1_555 125.8 ? 
91  OD1 ? I  ASP 83  ? I ASP 83  ? 1_555 ZN ? NA ZN . ? I ZN 202 ? 1_555 ND1 ? I  HIS 63  ? I HIS 63  ? 1_555 97.9  ? 
92  ND1 ? I  HIS 80  ? I HIS 80  ? 1_555 ZN ? NA ZN . ? I ZN 202 ? 1_555 ND1 ? I  HIS 63  ? I HIS 63  ? 1_555 114.7 ? 
93  ND1 ? I  HIS 71  ? I HIS 71  ? 1_555 ZN ? NA ZN . ? I ZN 202 ? 1_555 ND1 ? I  HIS 63  ? I HIS 63  ? 1_555 101.5 ? 
94  NE2 ? B  HIS 120 ? B HIS 120 ? 1_555 ZN ? P  ZN . ? B ZN 201 ? 1_555 NE2 ? B  HIS 48  ? B HIS 48  ? 1_555 117.9 ? 
95  NE2 ? B  HIS 120 ? B HIS 120 ? 1_555 ZN ? P  ZN . ? B ZN 201 ? 1_555 O2  ? R  SO4 .   ? B SO4 203 ? 1_555 93.9  ? 
96  NE2 ? B  HIS 48  ? B HIS 48  ? 1_555 ZN ? P  ZN . ? B ZN 201 ? 1_555 O2  ? R  SO4 .   ? B SO4 203 ? 1_555 105.0 ? 
97  NE2 ? B  HIS 120 ? B HIS 120 ? 1_555 ZN ? P  ZN . ? B ZN 201 ? 1_555 ND1 ? B  HIS 46  ? B HIS 46  ? 1_555 97.9  ? 
98  NE2 ? B  HIS 48  ? B HIS 48  ? 1_555 ZN ? P  ZN . ? B ZN 201 ? 1_555 ND1 ? B  HIS 46  ? B HIS 46  ? 1_555 126.0 ? 
99  O2  ? R  SO4 .   ? B SO4 203 ? 1_555 ZN ? P  ZN . ? B ZN 201 ? 1_555 ND1 ? B  HIS 46  ? B HIS 46  ? 1_555 111.7 ? 
100 NE2 ? F  HIS 120 ? F HIS 120 ? 1_555 ZN ? CA ZN . ? F ZN 201 ? 1_555 NE2 ? F  HIS 48  ? F HIS 48  ? 1_555 132.0 ? 
101 NE2 ? F  HIS 120 ? F HIS 120 ? 1_555 ZN ? CA ZN . ? F ZN 201 ? 1_555 ND1 ? F  HIS 46  ? F HIS 46  ? 1_555 86.8  ? 
102 NE2 ? F  HIS 48  ? F HIS 48  ? 1_555 ZN ? CA ZN . ? F ZN 201 ? 1_555 ND1 ? F  HIS 46  ? F HIS 46  ? 1_555 115.5 ? 
103 O3  ? V  SO4 .   ? C SO4 203 ? 1_555 ZN ? T  ZN . ? C ZN 201 ? 1_555 NE2 ? C  HIS 120 ? C HIS 120 ? 1_555 123.7 ? 
104 O3  ? V  SO4 .   ? C SO4 203 ? 1_555 ZN ? T  ZN . ? C ZN 201 ? 1_555 ND1 ? C  HIS 46  ? C HIS 46  ? 1_555 117.1 ? 
105 NE2 ? C  HIS 120 ? C HIS 120 ? 1_555 ZN ? T  ZN . ? C ZN 201 ? 1_555 ND1 ? C  HIS 46  ? C HIS 46  ? 1_555 89.5  ? 
106 O3  ? V  SO4 .   ? C SO4 203 ? 1_555 ZN ? T  ZN . ? C ZN 201 ? 1_555 NE2 ? C  HIS 48  ? C HIS 48  ? 1_555 91.7  ? 
107 NE2 ? C  HIS 120 ? C HIS 120 ? 1_555 ZN ? T  ZN . ? C ZN 201 ? 1_555 NE2 ? C  HIS 48  ? C HIS 48  ? 1_555 108.6 ? 
108 ND1 ? C  HIS 46  ? C HIS 46  ? 1_555 ZN ? T  ZN . ? C ZN 201 ? 1_555 NE2 ? C  HIS 48  ? C HIS 48  ? 1_555 129.5 ? 
109 NE2 ? A  HIS 120 ? A HIS 120 ? 1_555 ZN ? M  ZN . ? A ZN 201 ? 1_555 NE2 ? A  HIS 48  ? A HIS 48  ? 1_555 122.1 ? 
110 NE2 ? A  HIS 120 ? A HIS 120 ? 1_555 ZN ? M  ZN . ? A ZN 201 ? 1_555 O4  ? O  SO4 .   ? A SO4 203 ? 1_555 97.7  ? 
111 NE2 ? A  HIS 48  ? A HIS 48  ? 1_555 ZN ? M  ZN . ? A ZN 201 ? 1_555 O4  ? O  SO4 .   ? A SO4 203 ? 1_555 100.9 ? 
112 NE2 ? A  HIS 120 ? A HIS 120 ? 1_555 ZN ? M  ZN . ? A ZN 201 ? 1_555 ND1 ? A  HIS 46  ? A HIS 46  ? 1_555 94.4  ? 
113 NE2 ? A  HIS 48  ? A HIS 48  ? 1_555 ZN ? M  ZN . ? A ZN 201 ? 1_555 ND1 ? A  HIS 46  ? A HIS 46  ? 1_555 131.4 ? 
114 O4  ? O  SO4 .   ? A SO4 203 ? 1_555 ZN ? M  ZN . ? A ZN 201 ? 1_555 ND1 ? A  HIS 46  ? A HIS 46  ? 1_555 104.9 ? 
115 ND1 ? E  HIS 80  ? E HIS 80  ? 1_555 ZN ? AA ZN . ? E ZN 202 ? 1_555 ND1 ? E  HIS 63  ? E HIS 63  ? 1_555 116.2 ? 
116 ND1 ? E  HIS 80  ? E HIS 80  ? 1_555 ZN ? AA ZN . ? E ZN 202 ? 1_555 OD1 ? E  ASP 83  ? E ASP 83  ? 1_555 131.4 ? 
117 ND1 ? E  HIS 63  ? E HIS 63  ? 1_555 ZN ? AA ZN . ? E ZN 202 ? 1_555 OD1 ? E  ASP 83  ? E ASP 83  ? 1_555 91.4  ? 
118 ND1 ? E  HIS 80  ? E HIS 80  ? 1_555 ZN ? AA ZN . ? E ZN 202 ? 1_555 ND1 ? E  HIS 71  ? E HIS 71  ? 1_555 125.5 ? 
119 ND1 ? E  HIS 63  ? E HIS 63  ? 1_555 ZN ? AA ZN . ? E ZN 202 ? 1_555 ND1 ? E  HIS 71  ? E HIS 71  ? 1_555 95.7  ? 
120 OD1 ? E  ASP 83  ? E ASP 83  ? 1_555 ZN ? AA ZN . ? E ZN 202 ? 1_555 ND1 ? E  HIS 71  ? E HIS 71  ? 1_555 87.0  ? 
121 NE2 ? L  HIS 120 ? L HIS 120 ? 1_555 ZN ? VA ZN . ? L ZN 201 ? 1_555 NE2 ? L  HIS 48  ? L HIS 48  ? 1_555 124.0 ? 
122 NE2 ? L  HIS 120 ? L HIS 120 ? 1_555 ZN ? VA ZN . ? L ZN 201 ? 1_555 O1  ? XA SO4 .   ? L SO4 203 ? 1_555 88.6  ? 
123 NE2 ? L  HIS 48  ? L HIS 48  ? 1_555 ZN ? VA ZN . ? L ZN 201 ? 1_555 O1  ? XA SO4 .   ? L SO4 203 ? 1_555 99.4  ? 
124 NE2 ? L  HIS 120 ? L HIS 120 ? 1_555 ZN ? VA ZN . ? L ZN 201 ? 1_555 ND1 ? L  HIS 46  ? L HIS 46  ? 1_555 105.5 ? 
125 NE2 ? L  HIS 48  ? L HIS 48  ? 1_555 ZN ? VA ZN . ? L ZN 201 ? 1_555 ND1 ? L  HIS 46  ? L HIS 46  ? 1_555 126.5 ? 
126 O1  ? XA SO4 .   ? L SO4 203 ? 1_555 ZN ? VA ZN . ? L ZN 201 ? 1_555 ND1 ? L  HIS 46  ? L HIS 46  ? 1_555 100.8 ? 
127 OD1 ? C  ASP 83  ? C ASP 83  ? 1_555 ZN ? U  ZN . ? C ZN 202 ? 1_555 ND1 ? C  HIS 80  ? C HIS 80  ? 1_555 153.8 ? 
128 OD1 ? C  ASP 83  ? C ASP 83  ? 1_555 ZN ? U  ZN . ? C ZN 202 ? 1_555 ND1 ? C  HIS 63  ? C HIS 63  ? 1_555 76.8  ? 
129 ND1 ? C  HIS 80  ? C HIS 80  ? 1_555 ZN ? U  ZN . ? C ZN 202 ? 1_555 ND1 ? C  HIS 63  ? C HIS 63  ? 1_555 119.6 ? 
130 OD1 ? C  ASP 83  ? C ASP 83  ? 1_555 ZN ? U  ZN . ? C ZN 202 ? 1_555 OD2 ? C  ASP 83  ? C ASP 83  ? 1_555 56.5  ? 
131 ND1 ? C  HIS 80  ? C HIS 80  ? 1_555 ZN ? U  ZN . ? C ZN 202 ? 1_555 OD2 ? C  ASP 83  ? C ASP 83  ? 1_555 103.2 ? 
132 ND1 ? C  HIS 63  ? C HIS 63  ? 1_555 ZN ? U  ZN . ? C ZN 202 ? 1_555 OD2 ? C  ASP 83  ? C ASP 83  ? 1_555 133.1 ? 
133 OD1 ? C  ASP 83  ? C ASP 83  ? 1_555 ZN ? U  ZN . ? C ZN 202 ? 1_555 ND1 ? C  HIS 71  ? C HIS 71  ? 1_555 69.9  ? 
134 ND1 ? C  HIS 80  ? C HIS 80  ? 1_555 ZN ? U  ZN . ? C ZN 202 ? 1_555 ND1 ? C  HIS 71  ? C HIS 71  ? 1_555 126.2 ? 
135 ND1 ? C  HIS 63  ? C HIS 63  ? 1_555 ZN ? U  ZN . ? C ZN 202 ? 1_555 ND1 ? C  HIS 71  ? C HIS 71  ? 1_555 89.7  ? 
136 OD2 ? C  ASP 83  ? C ASP 83  ? 1_555 ZN ? U  ZN . ? C ZN 202 ? 1_555 ND1 ? C  HIS 71  ? C HIS 71  ? 1_555 78.9  ? 
137 NE2 ? I  HIS 120 ? I HIS 120 ? 1_555 ZN ? MA ZN . ? I ZN 201 ? 1_555 NE2 ? I  HIS 48  ? I HIS 48  ? 1_555 115.6 ? 
138 NE2 ? I  HIS 120 ? I HIS 120 ? 1_555 ZN ? MA ZN . ? I ZN 201 ? 1_555 O4  ? OA SO4 .   ? I SO4 203 ? 1_555 78.1  ? 
139 NE2 ? I  HIS 48  ? I HIS 48  ? 1_555 ZN ? MA ZN . ? I ZN 201 ? 1_555 O4  ? OA SO4 .   ? I SO4 203 ? 1_555 93.4  ? 
140 NE2 ? I  HIS 120 ? I HIS 120 ? 1_555 ZN ? MA ZN . ? I ZN 201 ? 1_555 ND1 ? I  HIS 46  ? I HIS 46  ? 1_555 94.2  ? 
141 NE2 ? I  HIS 48  ? I HIS 48  ? 1_555 ZN ? MA ZN . ? I ZN 201 ? 1_555 ND1 ? I  HIS 46  ? I HIS 46  ? 1_555 123.4 ? 
142 O4  ? OA SO4 .   ? I SO4 203 ? 1_555 ZN ? MA ZN . ? I ZN 201 ? 1_555 ND1 ? I  HIS 46  ? I HIS 46  ? 1_555 141.2 ? 
# 
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 2014-08-27 
2 'Structure model' 1 1 2014-12-24 
3 'Structure model' 1 2 2015-02-11 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 3 'Structure model' 'Database references' 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
MOLREP   phasing          .                             ? 1 
PHENIX   refinement       '(phenix.refine: 1.8.1_1161)' ? 2 
HKL-2000 'data reduction' .                             ? 3 
HKL-2000 'data scaling'   .                             ? 4 
# 
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 ALA A 55  ? ? -116.03 55.13   
2  1 ALA B 55  ? ? -106.25 40.34   
3  1 ASP B 90  ? ? -74.06  -169.15 
4  1 PHE C 64  ? ? -65.19  99.35   
5  1 SER C 68  ? ? 55.62   74.11   
6  1 ARG C 69  ? ? -121.00 -138.42 
7  1 ASP C 90  ? ? -79.08  -159.53 
8  1 SER C 98  ? ? -163.85 95.04   
9  1 HIS C 110 ? ? -99.61  36.36   
10 1 LYS C 128 ? ? -118.53 68.67   
11 1 SER E 98  ? ? -164.43 108.31  
12 1 LYS E 136 ? ? -127.33 -52.08  
13 1 ASP F 11  ? ? -155.79 11.80   
14 1 THR F 58  ? ? -36.92  -33.71  
15 1 SER F 68  ? ? 39.57   67.93   
16 1 LEU G 126 ? ? 47.29   29.20   
17 1 ALA I 55  ? ? -114.14 60.02   
18 1 LEU I 126 ? ? 56.10   19.25   
19 1 LYS I 128 ? ? -114.39 53.12   
20 1 THR I 137 ? ? -140.41 -46.77  
21 1 ALA J 55  ? ? -102.18 47.53   
22 1 ASP K 11  ? ? -86.09  31.28   
23 1 SER K 68  ? ? 65.06   69.33   
24 1 ARG K 69  ? ? -121.84 -149.36 
25 1 ASP K 90  ? ? -76.45  -151.94 
26 1 SER K 98  ? ? -160.87 106.26  
27 1 LYS K 122 ? ? -84.16  -146.66 
28 1 LYS K 128 ? ? -111.71 58.47   
29 1 LYS K 136 ? ? -133.78 -54.95  
30 1 SER L 98  ? ? -150.16 84.04   
# 
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 ALA 1 ? C ALA 1 
2 1 Y 1 E ALA 1 ? E ALA 1 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'    ZN  
3 'SULFATE ION' SO4 
4 water         HOH 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
M  2 ZN  1   201 154  ZN  ZN  A . 
N  2 ZN  1   202 155  ZN  ZN  A . 
O  3 SO4 1   203 1    SO4 SO4 A . 
P  2 ZN  1   201 154  ZN  ZN  B . 
Q  2 ZN  1   202 155  ZN  ZN  B . 
R  3 SO4 1   203 2    SO4 SO4 B . 
S  3 SO4 1   204 7    SO4 SO4 B . 
T  2 ZN  1   201 154  ZN  ZN  C . 
U  2 ZN  1   202 155  ZN  ZN  C . 
V  3 SO4 1   203 3    SO4 SO4 C . 
W  2 ZN  1   201 154  ZN  ZN  D . 
X  2 ZN  1   202 155  ZN  ZN  D . 
Y  3 SO4 1   203 4    SO4 SO4 D . 
Z  2 ZN  1   201 154  ZN  ZN  E . 
AA 2 ZN  1   202 155  ZN  ZN  E . 
BA 3 SO4 1   203 5    SO4 SO4 E . 
CA 2 ZN  1   201 154  ZN  ZN  F . 
DA 2 ZN  1   202 155  ZN  ZN  F . 
EA 3 SO4 1   203 6    SO4 SO4 F . 
FA 2 ZN  1   201 154  ZN  ZN  G . 
GA 2 ZN  1   202 155  ZN  ZN  G . 
HA 3 SO4 1   203 8    SO4 SO4 G . 
IA 2 ZN  1   201 154  ZN  ZN  H . 
JA 2 ZN  1   202 155  ZN  ZN  H . 
KA 3 SO4 1   203 9    SO4 SO4 H . 
LA 3 SO4 1   204 14   SO4 SO4 H . 
MA 2 ZN  1   201 154  ZN  ZN  I . 
NA 2 ZN  1   202 155  ZN  ZN  I . 
OA 3 SO4 1   203 10   SO4 SO4 I . 
PA 2 ZN  1   201 154  ZN  ZN  J . 
QA 2 ZN  1   202 155  ZN  ZN  J . 
RA 3 SO4 1   203 11   SO4 SO4 J . 
SA 2 ZN  1   201 154  ZN  ZN  K . 
TA 2 ZN  1   202 155  ZN  ZN  K . 
UA 3 SO4 1   203 12   SO4 SO4 K . 
VA 2 ZN  1   201 154  ZN  ZN  L . 
WA 2 ZN  1   202 155  ZN  ZN  L . 
XA 3 SO4 1   203 13   SO4 SO4 L . 
YA 4 HOH 1   301 2    HOH HOH A . 
YA 4 HOH 2   302 5    HOH HOH A . 
YA 4 HOH 3   303 18   HOH HOH A . 
YA 4 HOH 4   304 21   HOH HOH A . 
YA 4 HOH 5   305 25   HOH HOH A . 
YA 4 HOH 6   306 37   HOH HOH A . 
YA 4 HOH 7   307 51   HOH HOH A . 
YA 4 HOH 8   308 52   HOH HOH A . 
YA 4 HOH 9   309 53   HOH HOH A . 
YA 4 HOH 10  310 56   HOH HOH A . 
YA 4 HOH 11  311 57   HOH HOH A . 
YA 4 HOH 12  312 58   HOH HOH A . 
YA 4 HOH 13  313 70   HOH HOH A . 
YA 4 HOH 14  314 81   HOH HOH A . 
YA 4 HOH 15  315 86   HOH HOH A . 
YA 4 HOH 16  316 89   HOH HOH A . 
YA 4 HOH 17  317 97   HOH HOH A . 
YA 4 HOH 18  318 101  HOH HOH A . 
YA 4 HOH 19  319 112  HOH HOH A . 
YA 4 HOH 20  320 117  HOH HOH A . 
YA 4 HOH 21  321 123  HOH HOH A . 
YA 4 HOH 22  322 129  HOH HOH A . 
YA 4 HOH 23  323 133  HOH HOH A . 
YA 4 HOH 24  324 137  HOH HOH A . 
YA 4 HOH 25  325 161  HOH HOH A . 
YA 4 HOH 26  326 198  HOH HOH A . 
YA 4 HOH 27  327 209  HOH HOH A . 
YA 4 HOH 28  328 213  HOH HOH A . 
YA 4 HOH 29  329 231  HOH HOH A . 
YA 4 HOH 30  330 234  HOH HOH A . 
YA 4 HOH 31  331 236  HOH HOH A . 
YA 4 HOH 32  332 239  HOH HOH A . 
YA 4 HOH 33  333 242  HOH HOH A . 
YA 4 HOH 34  334 245  HOH HOH A . 
YA 4 HOH 35  335 267  HOH HOH A . 
YA 4 HOH 36  336 280  HOH HOH A . 
YA 4 HOH 37  337 293  HOH HOH A . 
YA 4 HOH 38  338 297  HOH HOH A . 
YA 4 HOH 39  339 300  HOH HOH A . 
YA 4 HOH 40  340 302  HOH HOH A . 
YA 4 HOH 41  341 306  HOH HOH A . 
YA 4 HOH 42  342 326  HOH HOH A . 
YA 4 HOH 43  343 332  HOH HOH A . 
YA 4 HOH 44  344 348  HOH HOH A . 
YA 4 HOH 45  345 356  HOH HOH A . 
YA 4 HOH 46  346 360  HOH HOH A . 
YA 4 HOH 47  347 368  HOH HOH A . 
YA 4 HOH 48  348 377  HOH HOH A . 
YA 4 HOH 49  349 386  HOH HOH A . 
YA 4 HOH 50  350 391  HOH HOH A . 
YA 4 HOH 51  351 396  HOH HOH A . 
YA 4 HOH 52  352 412  HOH HOH A . 
YA 4 HOH 53  353 417  HOH HOH A . 
YA 4 HOH 54  354 450  HOH HOH A . 
YA 4 HOH 55  355 452  HOH HOH A . 
YA 4 HOH 56  356 456  HOH HOH A . 
YA 4 HOH 57  357 465  HOH HOH A . 
YA 4 HOH 58  358 466  HOH HOH A . 
YA 4 HOH 59  359 493  HOH HOH A . 
YA 4 HOH 60  360 496  HOH HOH A . 
YA 4 HOH 61  361 497  HOH HOH A . 
YA 4 HOH 62  362 515  HOH HOH A . 
YA 4 HOH 63  363 523  HOH HOH A . 
YA 4 HOH 64  364 524  HOH HOH A . 
YA 4 HOH 65  365 526  HOH HOH A . 
YA 4 HOH 66  366 528  HOH HOH A . 
YA 4 HOH 67  367 543  HOH HOH A . 
YA 4 HOH 68  368 545  HOH HOH A . 
YA 4 HOH 69  369 563  HOH HOH A . 
YA 4 HOH 70  370 574  HOH HOH A . 
YA 4 HOH 71  371 580  HOH HOH A . 
YA 4 HOH 72  372 591  HOH HOH A . 
YA 4 HOH 73  373 598  HOH HOH A . 
YA 4 HOH 74  374 600  HOH HOH A . 
YA 4 HOH 75  375 605  HOH HOH A . 
YA 4 HOH 76  376 606  HOH HOH A . 
YA 4 HOH 77  377 610  HOH HOH A . 
YA 4 HOH 78  378 615  HOH HOH A . 
YA 4 HOH 79  379 626  HOH HOH A . 
YA 4 HOH 80  380 628  HOH HOH A . 
YA 4 HOH 81  381 632  HOH HOH A . 
YA 4 HOH 82  382 635  HOH HOH A . 
YA 4 HOH 83  383 639  HOH HOH A . 
YA 4 HOH 84  384 656  HOH HOH A . 
YA 4 HOH 85  385 672  HOH HOH A . 
YA 4 HOH 86  386 686  HOH HOH A . 
YA 4 HOH 87  387 688  HOH HOH A . 
YA 4 HOH 88  388 697  HOH HOH A . 
YA 4 HOH 89  389 698  HOH HOH A . 
YA 4 HOH 90  390 701  HOH HOH A . 
YA 4 HOH 91  391 702  HOH HOH A . 
YA 4 HOH 92  392 704  HOH HOH A . 
YA 4 HOH 93  393 705  HOH HOH A . 
YA 4 HOH 94  394 745  HOH HOH A . 
YA 4 HOH 95  395 771  HOH HOH A . 
YA 4 HOH 96  396 793  HOH HOH A . 
YA 4 HOH 97  397 798  HOH HOH A . 
YA 4 HOH 98  398 800  HOH HOH A . 
YA 4 HOH 99  399 803  HOH HOH A . 
YA 4 HOH 100 400 804  HOH HOH A . 
YA 4 HOH 101 401 816  HOH HOH A . 
YA 4 HOH 102 402 817  HOH HOH A . 
YA 4 HOH 103 403 851  HOH HOH A . 
YA 4 HOH 104 404 861  HOH HOH A . 
YA 4 HOH 105 405 863  HOH HOH A . 
YA 4 HOH 106 406 868  HOH HOH A . 
YA 4 HOH 107 407 870  HOH HOH A . 
YA 4 HOH 108 408 875  HOH HOH A . 
YA 4 HOH 109 409 879  HOH HOH A . 
YA 4 HOH 110 410 888  HOH HOH A . 
YA 4 HOH 111 411 894  HOH HOH A . 
YA 4 HOH 112 412 899  HOH HOH A . 
YA 4 HOH 113 413 900  HOH HOH A . 
YA 4 HOH 114 414 901  HOH HOH A . 
YA 4 HOH 115 415 909  HOH HOH A . 
YA 4 HOH 116 416 911  HOH HOH A . 
YA 4 HOH 117 417 915  HOH HOH A . 
YA 4 HOH 118 418 916  HOH HOH A . 
YA 4 HOH 119 419 919  HOH HOH A . 
YA 4 HOH 120 420 921  HOH HOH A . 
YA 4 HOH 121 421 927  HOH HOH A . 
YA 4 HOH 122 422 930  HOH HOH A . 
YA 4 HOH 123 423 934  HOH HOH A . 
YA 4 HOH 124 424 937  HOH HOH A . 
YA 4 HOH 125 425 939  HOH HOH A . 
YA 4 HOH 126 426 941  HOH HOH A . 
YA 4 HOH 127 427 953  HOH HOH A . 
YA 4 HOH 128 428 955  HOH HOH A . 
YA 4 HOH 129 429 957  HOH HOH A . 
YA 4 HOH 130 430 969  HOH HOH A . 
YA 4 HOH 131 431 986  HOH HOH A . 
YA 4 HOH 132 432 987  HOH HOH A . 
YA 4 HOH 133 433 989  HOH HOH A . 
YA 4 HOH 134 434 1000 HOH HOH A . 
YA 4 HOH 135 435 1003 HOH HOH A . 
YA 4 HOH 136 436 1021 HOH HOH A . 
YA 4 HOH 137 437 1035 HOH HOH A . 
YA 4 HOH 138 438 1036 HOH HOH A . 
YA 4 HOH 139 439 1052 HOH HOH A . 
YA 4 HOH 140 440 1053 HOH HOH A . 
YA 4 HOH 141 441 1078 HOH HOH A . 
YA 4 HOH 142 442 1089 HOH HOH A . 
ZA 4 HOH 1   301 3    HOH HOH B . 
ZA 4 HOH 2   302 6    HOH HOH B . 
ZA 4 HOH 3   303 7    HOH HOH B . 
ZA 4 HOH 4   304 9    HOH HOH B . 
ZA 4 HOH 5   305 16   HOH HOH B . 
ZA 4 HOH 6   306 31   HOH HOH B . 
ZA 4 HOH 7   307 33   HOH HOH B . 
ZA 4 HOH 8   308 40   HOH HOH B . 
ZA 4 HOH 9   309 42   HOH HOH B . 
ZA 4 HOH 10  310 47   HOH HOH B . 
ZA 4 HOH 11  311 48   HOH HOH B . 
ZA 4 HOH 12  312 59   HOH HOH B . 
ZA 4 HOH 13  313 61   HOH HOH B . 
ZA 4 HOH 14  314 62   HOH HOH B . 
ZA 4 HOH 15  315 72   HOH HOH B . 
ZA 4 HOH 16  316 73   HOH HOH B . 
ZA 4 HOH 17  317 78   HOH HOH B . 
ZA 4 HOH 18  318 79   HOH HOH B . 
ZA 4 HOH 19  319 80   HOH HOH B . 
ZA 4 HOH 20  320 82   HOH HOH B . 
ZA 4 HOH 21  321 90   HOH HOH B . 
ZA 4 HOH 22  322 96   HOH HOH B . 
ZA 4 HOH 23  323 102  HOH HOH B . 
ZA 4 HOH 24  324 105  HOH HOH B . 
ZA 4 HOH 25  325 109  HOH HOH B . 
ZA 4 HOH 26  326 113  HOH HOH B . 
ZA 4 HOH 27  327 118  HOH HOH B . 
ZA 4 HOH 28  328 122  HOH HOH B . 
ZA 4 HOH 29  329 126  HOH HOH B . 
ZA 4 HOH 30  330 130  HOH HOH B . 
ZA 4 HOH 31  331 134  HOH HOH B . 
ZA 4 HOH 32  332 139  HOH HOH B . 
ZA 4 HOH 33  333 142  HOH HOH B . 
ZA 4 HOH 34  334 144  HOH HOH B . 
ZA 4 HOH 35  335 146  HOH HOH B . 
ZA 4 HOH 36  336 164  HOH HOH B . 
ZA 4 HOH 37  337 168  HOH HOH B . 
ZA 4 HOH 38  338 169  HOH HOH B . 
ZA 4 HOH 39  339 175  HOH HOH B . 
ZA 4 HOH 40  340 179  HOH HOH B . 
ZA 4 HOH 41  341 181  HOH HOH B . 
ZA 4 HOH 42  342 194  HOH HOH B . 
ZA 4 HOH 43  343 205  HOH HOH B . 
ZA 4 HOH 44  344 212  HOH HOH B . 
ZA 4 HOH 45  345 221  HOH HOH B . 
ZA 4 HOH 46  346 225  HOH HOH B . 
ZA 4 HOH 47  347 226  HOH HOH B . 
ZA 4 HOH 48  348 227  HOH HOH B . 
ZA 4 HOH 49  349 237  HOH HOH B . 
ZA 4 HOH 50  350 240  HOH HOH B . 
ZA 4 HOH 51  351 246  HOH HOH B . 
ZA 4 HOH 52  352 256  HOH HOH B . 
ZA 4 HOH 53  353 257  HOH HOH B . 
ZA 4 HOH 54  354 259  HOH HOH B . 
ZA 4 HOH 55  355 262  HOH HOH B . 
ZA 4 HOH 56  356 264  HOH HOH B . 
ZA 4 HOH 57  357 277  HOH HOH B . 
ZA 4 HOH 58  358 282  HOH HOH B . 
ZA 4 HOH 59  359 294  HOH HOH B . 
ZA 4 HOH 60  360 304  HOH HOH B . 
ZA 4 HOH 61  361 311  HOH HOH B . 
ZA 4 HOH 62  362 314  HOH HOH B . 
ZA 4 HOH 63  363 317  HOH HOH B . 
ZA 4 HOH 64  364 328  HOH HOH B . 
ZA 4 HOH 65  365 338  HOH HOH B . 
ZA 4 HOH 66  366 340  HOH HOH B . 
ZA 4 HOH 67  367 370  HOH HOH B . 
ZA 4 HOH 68  368 372  HOH HOH B . 
ZA 4 HOH 69  369 383  HOH HOH B . 
ZA 4 HOH 70  370 388  HOH HOH B . 
ZA 4 HOH 71  371 392  HOH HOH B . 
ZA 4 HOH 72  372 398  HOH HOH B . 
ZA 4 HOH 73  373 411  HOH HOH B . 
ZA 4 HOH 74  374 413  HOH HOH B . 
ZA 4 HOH 75  375 414  HOH HOH B . 
ZA 4 HOH 76  376 422  HOH HOH B . 
ZA 4 HOH 77  377 427  HOH HOH B . 
ZA 4 HOH 78  378 434  HOH HOH B . 
ZA 4 HOH 79  379 436  HOH HOH B . 
ZA 4 HOH 80  380 439  HOH HOH B . 
ZA 4 HOH 81  381 447  HOH HOH B . 
ZA 4 HOH 82  382 448  HOH HOH B . 
ZA 4 HOH 83  383 449  HOH HOH B . 
ZA 4 HOH 84  384 458  HOH HOH B . 
ZA 4 HOH 85  385 463  HOH HOH B . 
ZA 4 HOH 86  386 468  HOH HOH B . 
ZA 4 HOH 87  387 469  HOH HOH B . 
ZA 4 HOH 88  388 471  HOH HOH B . 
ZA 4 HOH 89  389 481  HOH HOH B . 
ZA 4 HOH 90  390 489  HOH HOH B . 
ZA 4 HOH 91  391 498  HOH HOH B . 
ZA 4 HOH 92  392 518  HOH HOH B . 
ZA 4 HOH 93  393 538  HOH HOH B . 
ZA 4 HOH 94  394 553  HOH HOH B . 
ZA 4 HOH 95  395 568  HOH HOH B . 
ZA 4 HOH 96  396 575  HOH HOH B . 
ZA 4 HOH 97  397 583  HOH HOH B . 
ZA 4 HOH 98  398 587  HOH HOH B . 
ZA 4 HOH 99  399 597  HOH HOH B . 
ZA 4 HOH 100 400 599  HOH HOH B . 
ZA 4 HOH 101 401 603  HOH HOH B . 
ZA 4 HOH 102 402 612  HOH HOH B . 
ZA 4 HOH 103 403 617  HOH HOH B . 
ZA 4 HOH 104 404 640  HOH HOH B . 
ZA 4 HOH 105 405 641  HOH HOH B . 
ZA 4 HOH 106 406 644  HOH HOH B . 
ZA 4 HOH 107 407 658  HOH HOH B . 
ZA 4 HOH 108 408 684  HOH HOH B . 
ZA 4 HOH 109 409 703  HOH HOH B . 
ZA 4 HOH 110 410 712  HOH HOH B . 
ZA 4 HOH 111 411 723  HOH HOH B . 
ZA 4 HOH 112 412 726  HOH HOH B . 
ZA 4 HOH 113 413 728  HOH HOH B . 
ZA 4 HOH 114 414 732  HOH HOH B . 
ZA 4 HOH 115 415 733  HOH HOH B . 
ZA 4 HOH 116 416 752  HOH HOH B . 
ZA 4 HOH 117 417 763  HOH HOH B . 
ZA 4 HOH 118 418 775  HOH HOH B . 
ZA 4 HOH 119 419 776  HOH HOH B . 
ZA 4 HOH 120 420 782  HOH HOH B . 
ZA 4 HOH 121 421 786  HOH HOH B . 
ZA 4 HOH 122 422 795  HOH HOH B . 
ZA 4 HOH 123 423 811  HOH HOH B . 
ZA 4 HOH 124 424 823  HOH HOH B . 
ZA 4 HOH 125 425 825  HOH HOH B . 
ZA 4 HOH 126 426 826  HOH HOH B . 
ZA 4 HOH 127 427 834  HOH HOH B . 
ZA 4 HOH 128 428 852  HOH HOH B . 
ZA 4 HOH 129 429 874  HOH HOH B . 
ZA 4 HOH 130 430 878  HOH HOH B . 
ZA 4 HOH 131 431 885  HOH HOH B . 
ZA 4 HOH 132 432 903  HOH HOH B . 
ZA 4 HOH 133 433 904  HOH HOH B . 
ZA 4 HOH 134 434 929  HOH HOH B . 
ZA 4 HOH 135 435 935  HOH HOH B . 
ZA 4 HOH 136 436 940  HOH HOH B . 
ZA 4 HOH 137 437 942  HOH HOH B . 
ZA 4 HOH 138 438 960  HOH HOH B . 
ZA 4 HOH 139 439 975  HOH HOH B . 
ZA 4 HOH 140 440 985  HOH HOH B . 
ZA 4 HOH 141 441 990  HOH HOH B . 
ZA 4 HOH 142 442 994  HOH HOH B . 
ZA 4 HOH 143 443 1002 HOH HOH B . 
ZA 4 HOH 144 444 1012 HOH HOH B . 
ZA 4 HOH 145 445 1022 HOH HOH B . 
ZA 4 HOH 146 446 1024 HOH HOH B . 
ZA 4 HOH 147 447 1028 HOH HOH B . 
ZA 4 HOH 148 448 1031 HOH HOH B . 
ZA 4 HOH 149 449 1049 HOH HOH B . 
ZA 4 HOH 150 450 1055 HOH HOH B . 
ZA 4 HOH 151 451 1057 HOH HOH B . 
ZA 4 HOH 152 452 1069 HOH HOH B . 
ZA 4 HOH 153 453 1070 HOH HOH B . 
ZA 4 HOH 154 454 1082 HOH HOH B . 
ZA 4 HOH 155 455 1091 HOH HOH B . 
AB 4 HOH 1   301 49   HOH HOH C . 
AB 4 HOH 2   302 230  HOH HOH C . 
AB 4 HOH 3   303 301  HOH HOH C . 
AB 4 HOH 4   304 408  HOH HOH C . 
AB 4 HOH 5   305 426  HOH HOH C . 
AB 4 HOH 6   306 462  HOH HOH C . 
AB 4 HOH 7   307 484  HOH HOH C . 
AB 4 HOH 8   308 490  HOH HOH C . 
AB 4 HOH 9   309 517  HOH HOH C . 
AB 4 HOH 10  310 602  HOH HOH C . 
AB 4 HOH 11  311 620  HOH HOH C . 
AB 4 HOH 12  312 661  HOH HOH C . 
AB 4 HOH 13  313 751  HOH HOH C . 
AB 4 HOH 14  314 820  HOH HOH C . 
AB 4 HOH 15  315 831  HOH HOH C . 
AB 4 HOH 16  316 856  HOH HOH C . 
AB 4 HOH 17  317 864  HOH HOH C . 
AB 4 HOH 18  318 926  HOH HOH C . 
AB 4 HOH 19  319 1041 HOH HOH C . 
AB 4 HOH 20  320 1043 HOH HOH C . 
AB 4 HOH 21  321 1046 HOH HOH C . 
BB 4 HOH 1   301 12   HOH HOH D . 
BB 4 HOH 2   302 14   HOH HOH D . 
BB 4 HOH 3   303 55   HOH HOH D . 
BB 4 HOH 4   304 60   HOH HOH D . 
BB 4 HOH 5   305 71   HOH HOH D . 
BB 4 HOH 6   306 88   HOH HOH D . 
BB 4 HOH 7   307 111  HOH HOH D . 
BB 4 HOH 8   308 121  HOH HOH D . 
BB 4 HOH 9   309 151  HOH HOH D . 
BB 4 HOH 10  310 152  HOH HOH D . 
BB 4 HOH 11  311 167  HOH HOH D . 
BB 4 HOH 12  312 186  HOH HOH D . 
BB 4 HOH 13  313 189  HOH HOH D . 
BB 4 HOH 14  314 192  HOH HOH D . 
BB 4 HOH 15  315 193  HOH HOH D . 
BB 4 HOH 16  316 195  HOH HOH D . 
BB 4 HOH 17  317 235  HOH HOH D . 
BB 4 HOH 18  318 238  HOH HOH D . 
BB 4 HOH 19  319 243  HOH HOH D . 
BB 4 HOH 20  320 252  HOH HOH D . 
BB 4 HOH 21  321 253  HOH HOH D . 
BB 4 HOH 22  322 261  HOH HOH D . 
BB 4 HOH 23  323 268  HOH HOH D . 
BB 4 HOH 24  324 276  HOH HOH D . 
BB 4 HOH 25  325 290  HOH HOH D . 
BB 4 HOH 26  326 295  HOH HOH D . 
BB 4 HOH 27  327 309  HOH HOH D . 
BB 4 HOH 28  328 315  HOH HOH D . 
BB 4 HOH 29  329 320  HOH HOH D . 
BB 4 HOH 30  330 327  HOH HOH D . 
BB 4 HOH 31  331 333  HOH HOH D . 
BB 4 HOH 32  332 335  HOH HOH D . 
BB 4 HOH 33  333 339  HOH HOH D . 
BB 4 HOH 34  334 350  HOH HOH D . 
BB 4 HOH 35  335 362  HOH HOH D . 
BB 4 HOH 36  336 389  HOH HOH D . 
BB 4 HOH 37  337 390  HOH HOH D . 
BB 4 HOH 38  338 402  HOH HOH D . 
BB 4 HOH 39  339 405  HOH HOH D . 
BB 4 HOH 40  340 409  HOH HOH D . 
BB 4 HOH 41  341 467  HOH HOH D . 
BB 4 HOH 42  342 472  HOH HOH D . 
BB 4 HOH 43  343 473  HOH HOH D . 
BB 4 HOH 44  344 491  HOH HOH D . 
BB 4 HOH 45  345 500  HOH HOH D . 
BB 4 HOH 46  346 509  HOH HOH D . 
BB 4 HOH 47  347 519  HOH HOH D . 
BB 4 HOH 48  348 530  HOH HOH D . 
BB 4 HOH 49  349 534  HOH HOH D . 
BB 4 HOH 50  350 536  HOH HOH D . 
BB 4 HOH 51  351 542  HOH HOH D . 
BB 4 HOH 52  352 560  HOH HOH D . 
BB 4 HOH 53  353 562  HOH HOH D . 
BB 4 HOH 54  354 569  HOH HOH D . 
BB 4 HOH 55  355 581  HOH HOH D . 
BB 4 HOH 56  356 604  HOH HOH D . 
BB 4 HOH 57  357 627  HOH HOH D . 
BB 4 HOH 58  358 642  HOH HOH D . 
BB 4 HOH 59  359 651  HOH HOH D . 
BB 4 HOH 60  360 662  HOH HOH D . 
BB 4 HOH 61  361 674  HOH HOH D . 
BB 4 HOH 62  362 700  HOH HOH D . 
BB 4 HOH 63  363 731  HOH HOH D . 
BB 4 HOH 64  364 749  HOH HOH D . 
BB 4 HOH 65  365 753  HOH HOH D . 
BB 4 HOH 66  366 755  HOH HOH D . 
BB 4 HOH 67  367 760  HOH HOH D . 
BB 4 HOH 68  368 790  HOH HOH D . 
BB 4 HOH 69  369 806  HOH HOH D . 
BB 4 HOH 70  370 809  HOH HOH D . 
BB 4 HOH 71  371 818  HOH HOH D . 
BB 4 HOH 72  372 844  HOH HOH D . 
BB 4 HOH 73  373 857  HOH HOH D . 
BB 4 HOH 74  374 895  HOH HOH D . 
BB 4 HOH 75  375 896  HOH HOH D . 
BB 4 HOH 76  376 947  HOH HOH D . 
BB 4 HOH 77  377 951  HOH HOH D . 
BB 4 HOH 78  378 962  HOH HOH D . 
BB 4 HOH 79  379 972  HOH HOH D . 
BB 4 HOH 80  380 973  HOH HOH D . 
BB 4 HOH 81  381 981  HOH HOH D . 
BB 4 HOH 82  382 1006 HOH HOH D . 
BB 4 HOH 83  383 1018 HOH HOH D . 
BB 4 HOH 84  384 1029 HOH HOH D . 
BB 4 HOH 85  385 1034 HOH HOH D . 
BB 4 HOH 86  386 1048 HOH HOH D . 
BB 4 HOH 87  387 1054 HOH HOH D . 
BB 4 HOH 88  388 1073 HOH HOH D . 
BB 4 HOH 89  389 1080 HOH HOH D . 
BB 4 HOH 90  390 1083 HOH HOH D . 
BB 4 HOH 91  391 1088 HOH HOH D . 
BB 4 HOH 92  392 1092 HOH HOH D . 
BB 4 HOH 93  393 1096 HOH HOH D . 
CB 4 HOH 1   301 115  HOH HOH E . 
CB 4 HOH 2   302 135  HOH HOH E . 
CB 4 HOH 3   303 141  HOH HOH E . 
CB 4 HOH 4   304 308  HOH HOH E . 
CB 4 HOH 5   305 312  HOH HOH E . 
CB 4 HOH 6   306 323  HOH HOH E . 
CB 4 HOH 7   307 342  HOH HOH E . 
CB 4 HOH 8   308 371  HOH HOH E . 
CB 4 HOH 9   309 376  HOH HOH E . 
CB 4 HOH 10  310 384  HOH HOH E . 
CB 4 HOH 11  311 406  HOH HOH E . 
CB 4 HOH 12  312 441  HOH HOH E . 
CB 4 HOH 13  313 488  HOH HOH E . 
CB 4 HOH 14  314 516  HOH HOH E . 
CB 4 HOH 15  315 559  HOH HOH E . 
CB 4 HOH 16  316 633  HOH HOH E . 
CB 4 HOH 17  317 643  HOH HOH E . 
CB 4 HOH 18  318 669  HOH HOH E . 
CB 4 HOH 19  319 675  HOH HOH E . 
CB 4 HOH 20  320 677  HOH HOH E . 
CB 4 HOH 21  321 679  HOH HOH E . 
CB 4 HOH 22  322 687  HOH HOH E . 
CB 4 HOH 23  323 694  HOH HOH E . 
CB 4 HOH 24  324 696  HOH HOH E . 
CB 4 HOH 25  325 699  HOH HOH E . 
CB 4 HOH 26  326 715  HOH HOH E . 
CB 4 HOH 27  327 725  HOH HOH E . 
CB 4 HOH 28  328 741  HOH HOH E . 
CB 4 HOH 29  329 757  HOH HOH E . 
CB 4 HOH 30  330 769  HOH HOH E . 
CB 4 HOH 31  331 813  HOH HOH E . 
CB 4 HOH 32  332 833  HOH HOH E . 
CB 4 HOH 33  333 887  HOH HOH E . 
CB 4 HOH 34  334 938  HOH HOH E . 
CB 4 HOH 35  335 948  HOH HOH E . 
CB 4 HOH 36  336 1037 HOH HOH E . 
CB 4 HOH 37  337 1081 HOH HOH E . 
DB 4 HOH 1   301 11   HOH HOH F . 
DB 4 HOH 2   302 43   HOH HOH F . 
DB 4 HOH 3   303 74   HOH HOH F . 
DB 4 HOH 4   304 104  HOH HOH F . 
DB 4 HOH 5   305 132  HOH HOH F . 
DB 4 HOH 6   306 145  HOH HOH F . 
DB 4 HOH 7   307 147  HOH HOH F . 
DB 4 HOH 8   308 158  HOH HOH F . 
DB 4 HOH 9   309 163  HOH HOH F . 
DB 4 HOH 10  310 173  HOH HOH F . 
DB 4 HOH 11  311 178  HOH HOH F . 
DB 4 HOH 12  312 180  HOH HOH F . 
DB 4 HOH 13  313 182  HOH HOH F . 
DB 4 HOH 14  314 190  HOH HOH F . 
DB 4 HOH 15  315 232  HOH HOH F . 
DB 4 HOH 16  316 258  HOH HOH F . 
DB 4 HOH 17  317 260  HOH HOH F . 
DB 4 HOH 18  318 273  HOH HOH F . 
DB 4 HOH 19  319 287  HOH HOH F . 
DB 4 HOH 20  320 292  HOH HOH F . 
DB 4 HOH 21  321 298  HOH HOH F . 
DB 4 HOH 22  322 303  HOH HOH F . 
DB 4 HOH 23  323 318  HOH HOH F . 
DB 4 HOH 24  324 322  HOH HOH F . 
DB 4 HOH 25  325 337  HOH HOH F . 
DB 4 HOH 26  326 341  HOH HOH F . 
DB 4 HOH 27  327 358  HOH HOH F . 
DB 4 HOH 28  328 367  HOH HOH F . 
DB 4 HOH 29  329 374  HOH HOH F . 
DB 4 HOH 30  330 380  HOH HOH F . 
DB 4 HOH 31  331 382  HOH HOH F . 
DB 4 HOH 32  332 394  HOH HOH F . 
DB 4 HOH 33  333 401  HOH HOH F . 
DB 4 HOH 34  334 404  HOH HOH F . 
DB 4 HOH 35  335 407  HOH HOH F . 
DB 4 HOH 36  336 419  HOH HOH F . 
DB 4 HOH 37  337 421  HOH HOH F . 
DB 4 HOH 38  338 424  HOH HOH F . 
DB 4 HOH 39  339 428  HOH HOH F . 
DB 4 HOH 40  340 444  HOH HOH F . 
DB 4 HOH 41  341 477  HOH HOH F . 
DB 4 HOH 42  342 494  HOH HOH F . 
DB 4 HOH 43  343 529  HOH HOH F . 
DB 4 HOH 44  344 546  HOH HOH F . 
DB 4 HOH 45  345 554  HOH HOH F . 
DB 4 HOH 46  346 561  HOH HOH F . 
DB 4 HOH 47  347 588  HOH HOH F . 
DB 4 HOH 48  348 646  HOH HOH F . 
DB 4 HOH 49  349 647  HOH HOH F . 
DB 4 HOH 50  350 650  HOH HOH F . 
DB 4 HOH 51  351 659  HOH HOH F . 
DB 4 HOH 52  352 676  HOH HOH F . 
DB 4 HOH 53  353 681  HOH HOH F . 
DB 4 HOH 54  354 682  HOH HOH F . 
DB 4 HOH 55  355 695  HOH HOH F . 
DB 4 HOH 56  356 706  HOH HOH F . 
DB 4 HOH 57  357 708  HOH HOH F . 
DB 4 HOH 58  358 734  HOH HOH F . 
DB 4 HOH 59  359 738  HOH HOH F . 
DB 4 HOH 60  360 739  HOH HOH F . 
DB 4 HOH 61  361 759  HOH HOH F . 
DB 4 HOH 62  362 762  HOH HOH F . 
DB 4 HOH 63  363 765  HOH HOH F . 
DB 4 HOH 64  364 766  HOH HOH F . 
DB 4 HOH 65  365 770  HOH HOH F . 
DB 4 HOH 66  366 773  HOH HOH F . 
DB 4 HOH 67  367 785  HOH HOH F . 
DB 4 HOH 68  368 791  HOH HOH F . 
DB 4 HOH 69  369 829  HOH HOH F . 
DB 4 HOH 70  370 839  HOH HOH F . 
DB 4 HOH 71  371 840  HOH HOH F . 
DB 4 HOH 72  372 841  HOH HOH F . 
DB 4 HOH 73  373 848  HOH HOH F . 
DB 4 HOH 74  374 853  HOH HOH F . 
DB 4 HOH 75  375 859  HOH HOH F . 
DB 4 HOH 76  376 860  HOH HOH F . 
DB 4 HOH 77  377 865  HOH HOH F . 
DB 4 HOH 78  378 905  HOH HOH F . 
DB 4 HOH 79  379 907  HOH HOH F . 
DB 4 HOH 80  380 931  HOH HOH F . 
DB 4 HOH 81  381 936  HOH HOH F . 
DB 4 HOH 82  382 952  HOH HOH F . 
DB 4 HOH 83  383 977  HOH HOH F . 
DB 4 HOH 84  384 1019 HOH HOH F . 
DB 4 HOH 85  385 1030 HOH HOH F . 
DB 4 HOH 86  386 1066 HOH HOH F . 
DB 4 HOH 87  387 1077 HOH HOH F . 
EB 4 HOH 1   301 10   HOH HOH G . 
EB 4 HOH 2   302 19   HOH HOH G . 
EB 4 HOH 3   303 24   HOH HOH G . 
EB 4 HOH 4   304 26   HOH HOH G . 
EB 4 HOH 5   305 32   HOH HOH G . 
EB 4 HOH 6   306 39   HOH HOH G . 
EB 4 HOH 7   307 45   HOH HOH G . 
EB 4 HOH 8   308 54   HOH HOH G . 
EB 4 HOH 9   309 65   HOH HOH G . 
EB 4 HOH 10  310 92   HOH HOH G . 
EB 4 HOH 11  311 103  HOH HOH G . 
EB 4 HOH 12  312 110  HOH HOH G . 
EB 4 HOH 13  313 128  HOH HOH G . 
EB 4 HOH 14  314 131  HOH HOH G . 
EB 4 HOH 15  315 136  HOH HOH G . 
EB 4 HOH 16  316 150  HOH HOH G . 
EB 4 HOH 17  317 154  HOH HOH G . 
EB 4 HOH 18  318 160  HOH HOH G . 
EB 4 HOH 19  319 162  HOH HOH G . 
EB 4 HOH 20  320 171  HOH HOH G . 
EB 4 HOH 21  321 188  HOH HOH G . 
EB 4 HOH 22  322 201  HOH HOH G . 
EB 4 HOH 23  323 203  HOH HOH G . 
EB 4 HOH 24  324 204  HOH HOH G . 
EB 4 HOH 25  325 207  HOH HOH G . 
EB 4 HOH 26  326 215  HOH HOH G . 
EB 4 HOH 27  327 216  HOH HOH G . 
EB 4 HOH 28  328 219  HOH HOH G . 
EB 4 HOH 29  329 250  HOH HOH G . 
EB 4 HOH 30  330 255  HOH HOH G . 
EB 4 HOH 31  331 263  HOH HOH G . 
EB 4 HOH 32  332 265  HOH HOH G . 
EB 4 HOH 33  333 270  HOH HOH G . 
EB 4 HOH 34  334 278  HOH HOH G . 
EB 4 HOH 35  335 279  HOH HOH G . 
EB 4 HOH 36  336 289  HOH HOH G . 
EB 4 HOH 37  337 291  HOH HOH G . 
EB 4 HOH 38  338 325  HOH HOH G . 
EB 4 HOH 39  339 331  HOH HOH G . 
EB 4 HOH 40  340 345  HOH HOH G . 
EB 4 HOH 41  341 352  HOH HOH G . 
EB 4 HOH 42  342 354  HOH HOH G . 
EB 4 HOH 43  343 363  HOH HOH G . 
EB 4 HOH 44  344 365  HOH HOH G . 
EB 4 HOH 45  345 381  HOH HOH G . 
EB 4 HOH 46  346 397  HOH HOH G . 
EB 4 HOH 47  347 410  HOH HOH G . 
EB 4 HOH 48  348 420  HOH HOH G . 
EB 4 HOH 49  349 431  HOH HOH G . 
EB 4 HOH 50  350 435  HOH HOH G . 
EB 4 HOH 51  351 437  HOH HOH G . 
EB 4 HOH 52  352 445  HOH HOH G . 
EB 4 HOH 53  353 464  HOH HOH G . 
EB 4 HOH 54  354 474  HOH HOH G . 
EB 4 HOH 55  355 475  HOH HOH G . 
EB 4 HOH 56  356 478  HOH HOH G . 
EB 4 HOH 57  357 485  HOH HOH G . 
EB 4 HOH 58  358 492  HOH HOH G . 
EB 4 HOH 59  359 495  HOH HOH G . 
EB 4 HOH 60  360 499  HOH HOH G . 
EB 4 HOH 61  361 504  HOH HOH G . 
EB 4 HOH 62  362 506  HOH HOH G . 
EB 4 HOH 63  363 507  HOH HOH G . 
EB 4 HOH 64  364 522  HOH HOH G . 
EB 4 HOH 65  365 525  HOH HOH G . 
EB 4 HOH 66  366 531  HOH HOH G . 
EB 4 HOH 67  367 537  HOH HOH G . 
EB 4 HOH 68  368 540  HOH HOH G . 
EB 4 HOH 69  369 550  HOH HOH G . 
EB 4 HOH 70  370 555  HOH HOH G . 
EB 4 HOH 71  371 572  HOH HOH G . 
EB 4 HOH 72  372 577  HOH HOH G . 
EB 4 HOH 73  373 582  HOH HOH G . 
EB 4 HOH 74  374 586  HOH HOH G . 
EB 4 HOH 75  375 589  HOH HOH G . 
EB 4 HOH 76  376 601  HOH HOH G . 
EB 4 HOH 77  377 621  HOH HOH G . 
EB 4 HOH 78  378 648  HOH HOH G . 
EB 4 HOH 79  379 655  HOH HOH G . 
EB 4 HOH 80  380 668  HOH HOH G . 
EB 4 HOH 81  381 683  HOH HOH G . 
EB 4 HOH 82  382 685  HOH HOH G . 
EB 4 HOH 83  383 690  HOH HOH G . 
EB 4 HOH 84  384 692  HOH HOH G . 
EB 4 HOH 85  385 719  HOH HOH G . 
EB 4 HOH 86  386 729  HOH HOH G . 
EB 4 HOH 87  387 735  HOH HOH G . 
EB 4 HOH 88  388 737  HOH HOH G . 
EB 4 HOH 89  389 740  HOH HOH G . 
EB 4 HOH 90  390 744  HOH HOH G . 
EB 4 HOH 91  391 747  HOH HOH G . 
EB 4 HOH 92  392 756  HOH HOH G . 
EB 4 HOH 93  393 758  HOH HOH G . 
EB 4 HOH 94  394 768  HOH HOH G . 
EB 4 HOH 95  395 774  HOH HOH G . 
EB 4 HOH 96  396 777  HOH HOH G . 
EB 4 HOH 97  397 787  HOH HOH G . 
EB 4 HOH 98  398 792  HOH HOH G . 
EB 4 HOH 99  399 819  HOH HOH G . 
EB 4 HOH 100 400 836  HOH HOH G . 
EB 4 HOH 101 401 838  HOH HOH G . 
EB 4 HOH 102 402 843  HOH HOH G . 
EB 4 HOH 103 403 849  HOH HOH G . 
EB 4 HOH 104 404 854  HOH HOH G . 
EB 4 HOH 105 405 871  HOH HOH G . 
EB 4 HOH 106 406 876  HOH HOH G . 
EB 4 HOH 107 407 877  HOH HOH G . 
EB 4 HOH 108 408 880  HOH HOH G . 
EB 4 HOH 109 409 886  HOH HOH G . 
EB 4 HOH 110 410 891  HOH HOH G . 
EB 4 HOH 111 411 898  HOH HOH G . 
EB 4 HOH 112 412 914  HOH HOH G . 
EB 4 HOH 113 413 918  HOH HOH G . 
EB 4 HOH 114 414 923  HOH HOH G . 
EB 4 HOH 115 415 933  HOH HOH G . 
EB 4 HOH 116 416 943  HOH HOH G . 
EB 4 HOH 117 417 945  HOH HOH G . 
EB 4 HOH 118 418 950  HOH HOH G . 
EB 4 HOH 119 419 956  HOH HOH G . 
EB 4 HOH 120 420 958  HOH HOH G . 
EB 4 HOH 121 421 959  HOH HOH G . 
EB 4 HOH 122 422 978  HOH HOH G . 
EB 4 HOH 123 423 980  HOH HOH G . 
EB 4 HOH 124 424 988  HOH HOH G . 
EB 4 HOH 125 425 1014 HOH HOH G . 
EB 4 HOH 126 426 1020 HOH HOH G . 
EB 4 HOH 127 427 1023 HOH HOH G . 
EB 4 HOH 128 428 1044 HOH HOH G . 
EB 4 HOH 129 429 1058 HOH HOH G . 
EB 4 HOH 130 430 1061 HOH HOH G . 
EB 4 HOH 131 431 1062 HOH HOH G . 
EB 4 HOH 132 432 1071 HOH HOH G . 
EB 4 HOH 133 433 1075 HOH HOH G . 
EB 4 HOH 134 434 1076 HOH HOH G . 
EB 4 HOH 135 435 1085 HOH HOH G . 
EB 4 HOH 136 436 1087 HOH HOH G . 
EB 4 HOH 137 437 1097 HOH HOH G . 
FB 4 HOH 1   301 1    HOH HOH H . 
FB 4 HOH 2   302 8    HOH HOH H . 
FB 4 HOH 3   303 13   HOH HOH H . 
FB 4 HOH 4   304 17   HOH HOH H . 
FB 4 HOH 5   305 20   HOH HOH H . 
FB 4 HOH 6   306 22   HOH HOH H . 
FB 4 HOH 7   307 29   HOH HOH H . 
FB 4 HOH 8   308 35   HOH HOH H . 
FB 4 HOH 9   309 38   HOH HOH H . 
FB 4 HOH 10  310 41   HOH HOH H . 
FB 4 HOH 11  311 44   HOH HOH H . 
FB 4 HOH 12  312 64   HOH HOH H . 
FB 4 HOH 13  313 66   HOH HOH H . 
FB 4 HOH 14  314 67   HOH HOH H . 
FB 4 HOH 15  315 68   HOH HOH H . 
FB 4 HOH 16  316 75   HOH HOH H . 
FB 4 HOH 17  317 85   HOH HOH H . 
FB 4 HOH 18  318 87   HOH HOH H . 
FB 4 HOH 19  319 91   HOH HOH H . 
FB 4 HOH 20  320 99   HOH HOH H . 
FB 4 HOH 21  321 106  HOH HOH H . 
FB 4 HOH 22  322 119  HOH HOH H . 
FB 4 HOH 23  323 124  HOH HOH H . 
FB 4 HOH 24  324 138  HOH HOH H . 
FB 4 HOH 25  325 140  HOH HOH H . 
FB 4 HOH 26  326 149  HOH HOH H . 
FB 4 HOH 27  327 153  HOH HOH H . 
FB 4 HOH 28  328 157  HOH HOH H . 
FB 4 HOH 29  329 165  HOH HOH H . 
FB 4 HOH 30  330 170  HOH HOH H . 
FB 4 HOH 31  331 174  HOH HOH H . 
FB 4 HOH 32  332 177  HOH HOH H . 
FB 4 HOH 33  333 183  HOH HOH H . 
FB 4 HOH 34  334 185  HOH HOH H . 
FB 4 HOH 35  335 196  HOH HOH H . 
FB 4 HOH 36  336 200  HOH HOH H . 
FB 4 HOH 37  337 208  HOH HOH H . 
FB 4 HOH 38  338 214  HOH HOH H . 
FB 4 HOH 39  339 217  HOH HOH H . 
FB 4 HOH 40  340 218  HOH HOH H . 
FB 4 HOH 41  341 224  HOH HOH H . 
FB 4 HOH 42  342 233  HOH HOH H . 
FB 4 HOH 43  343 241  HOH HOH H . 
FB 4 HOH 44  344 244  HOH HOH H . 
FB 4 HOH 45  345 247  HOH HOH H . 
FB 4 HOH 46  346 251  HOH HOH H . 
FB 4 HOH 47  347 271  HOH HOH H . 
FB 4 HOH 48  348 272  HOH HOH H . 
FB 4 HOH 49  349 274  HOH HOH H . 
FB 4 HOH 50  350 275  HOH HOH H . 
FB 4 HOH 51  351 281  HOH HOH H . 
FB 4 HOH 52  352 288  HOH HOH H . 
FB 4 HOH 53  353 299  HOH HOH H . 
FB 4 HOH 54  354 305  HOH HOH H . 
FB 4 HOH 55  355 310  HOH HOH H . 
FB 4 HOH 56  356 329  HOH HOH H . 
FB 4 HOH 57  357 336  HOH HOH H . 
FB 4 HOH 58  358 347  HOH HOH H . 
FB 4 HOH 59  359 351  HOH HOH H . 
FB 4 HOH 60  360 355  HOH HOH H . 
FB 4 HOH 61  361 361  HOH HOH H . 
FB 4 HOH 62  362 385  HOH HOH H . 
FB 4 HOH 63  363 387  HOH HOH H . 
FB 4 HOH 64  364 399  HOH HOH H . 
FB 4 HOH 65  365 403  HOH HOH H . 
FB 4 HOH 66  366 423  HOH HOH H . 
FB 4 HOH 67  367 429  HOH HOH H . 
FB 4 HOH 68  368 432  HOH HOH H . 
FB 4 HOH 69  369 433  HOH HOH H . 
FB 4 HOH 70  370 438  HOH HOH H . 
FB 4 HOH 71  371 443  HOH HOH H . 
FB 4 HOH 72  372 476  HOH HOH H . 
FB 4 HOH 73  373 479  HOH HOH H . 
FB 4 HOH 74  374 480  HOH HOH H . 
FB 4 HOH 75  375 483  HOH HOH H . 
FB 4 HOH 76  376 501  HOH HOH H . 
FB 4 HOH 77  377 503  HOH HOH H . 
FB 4 HOH 78  378 505  HOH HOH H . 
FB 4 HOH 79  379 508  HOH HOH H . 
FB 4 HOH 80  380 513  HOH HOH H . 
FB 4 HOH 81  381 514  HOH HOH H . 
FB 4 HOH 82  382 521  HOH HOH H . 
FB 4 HOH 83  383 533  HOH HOH H . 
FB 4 HOH 84  384 535  HOH HOH H . 
FB 4 HOH 85  385 539  HOH HOH H . 
FB 4 HOH 86  386 541  HOH HOH H . 
FB 4 HOH 87  387 548  HOH HOH H . 
FB 4 HOH 88  388 549  HOH HOH H . 
FB 4 HOH 89  389 556  HOH HOH H . 
FB 4 HOH 90  390 558  HOH HOH H . 
FB 4 HOH 91  391 564  HOH HOH H . 
FB 4 HOH 92  392 567  HOH HOH H . 
FB 4 HOH 93  393 576  HOH HOH H . 
FB 4 HOH 94  394 578  HOH HOH H . 
FB 4 HOH 95  395 590  HOH HOH H . 
FB 4 HOH 96  396 594  HOH HOH H . 
FB 4 HOH 97  397 595  HOH HOH H . 
FB 4 HOH 98  398 613  HOH HOH H . 
FB 4 HOH 99  399 618  HOH HOH H . 
FB 4 HOH 100 400 622  HOH HOH H . 
FB 4 HOH 101 401 623  HOH HOH H . 
FB 4 HOH 102 402 637  HOH HOH H . 
FB 4 HOH 103 403 653  HOH HOH H . 
FB 4 HOH 104 404 663  HOH HOH H . 
FB 4 HOH 105 405 666  HOH HOH H . 
FB 4 HOH 106 406 667  HOH HOH H . 
FB 4 HOH 107 407 671  HOH HOH H . 
FB 4 HOH 108 408 673  HOH HOH H . 
FB 4 HOH 109 409 693  HOH HOH H . 
FB 4 HOH 110 410 707  HOH HOH H . 
FB 4 HOH 111 411 713  HOH HOH H . 
FB 4 HOH 112 412 714  HOH HOH H . 
FB 4 HOH 113 413 720  HOH HOH H . 
FB 4 HOH 114 414 724  HOH HOH H . 
FB 4 HOH 115 415 730  HOH HOH H . 
FB 4 HOH 116 416 736  HOH HOH H . 
FB 4 HOH 117 417 743  HOH HOH H . 
FB 4 HOH 118 418 746  HOH HOH H . 
FB 4 HOH 119 419 754  HOH HOH H . 
FB 4 HOH 120 420 764  HOH HOH H . 
FB 4 HOH 121 421 779  HOH HOH H . 
FB 4 HOH 122 422 781  HOH HOH H . 
FB 4 HOH 123 423 784  HOH HOH H . 
FB 4 HOH 124 424 788  HOH HOH H . 
FB 4 HOH 125 425 789  HOH HOH H . 
FB 4 HOH 126 426 794  HOH HOH H . 
FB 4 HOH 127 427 796  HOH HOH H . 
FB 4 HOH 128 428 807  HOH HOH H . 
FB 4 HOH 129 429 810  HOH HOH H . 
FB 4 HOH 130 430 822  HOH HOH H . 
FB 4 HOH 131 431 824  HOH HOH H . 
FB 4 HOH 132 432 828  HOH HOH H . 
FB 4 HOH 133 433 835  HOH HOH H . 
FB 4 HOH 134 434 855  HOH HOH H . 
FB 4 HOH 135 435 872  HOH HOH H . 
FB 4 HOH 136 436 881  HOH HOH H . 
FB 4 HOH 137 437 890  HOH HOH H . 
FB 4 HOH 138 438 897  HOH HOH H . 
FB 4 HOH 139 439 912  HOH HOH H . 
FB 4 HOH 140 440 913  HOH HOH H . 
FB 4 HOH 141 441 924  HOH HOH H . 
FB 4 HOH 142 442 949  HOH HOH H . 
FB 4 HOH 143 443 971  HOH HOH H . 
FB 4 HOH 144 444 974  HOH HOH H . 
FB 4 HOH 145 445 976  HOH HOH H . 
FB 4 HOH 146 446 992  HOH HOH H . 
FB 4 HOH 147 447 993  HOH HOH H . 
FB 4 HOH 148 448 995  HOH HOH H . 
FB 4 HOH 149 449 997  HOH HOH H . 
FB 4 HOH 150 450 998  HOH HOH H . 
FB 4 HOH 151 451 1004 HOH HOH H . 
FB 4 HOH 152 452 1007 HOH HOH H . 
FB 4 HOH 153 453 1015 HOH HOH H . 
FB 4 HOH 154 454 1045 HOH HOH H . 
FB 4 HOH 155 455 1056 HOH HOH H . 
FB 4 HOH 156 456 1063 HOH HOH H . 
FB 4 HOH 157 457 1064 HOH HOH H . 
FB 4 HOH 158 458 1067 HOH HOH H . 
FB 4 HOH 159 459 1074 HOH HOH H . 
FB 4 HOH 160 460 1079 HOH HOH H . 
GB 4 HOH 1   301 69   HOH HOH I . 
GB 4 HOH 2   302 77   HOH HOH I . 
GB 4 HOH 3   303 127  HOH HOH I . 
GB 4 HOH 4   304 176  HOH HOH I . 
GB 4 HOH 5   305 206  HOH HOH I . 
GB 4 HOH 6   306 286  HOH HOH I . 
GB 4 HOH 7   307 321  HOH HOH I . 
GB 4 HOH 8   308 393  HOH HOH I . 
GB 4 HOH 9   309 430  HOH HOH I . 
GB 4 HOH 10  310 446  HOH HOH I . 
GB 4 HOH 11  311 451  HOH HOH I . 
GB 4 HOH 12  312 457  HOH HOH I . 
GB 4 HOH 13  313 544  HOH HOH I . 
GB 4 HOH 14  314 547  HOH HOH I . 
GB 4 HOH 15  315 573  HOH HOH I . 
GB 4 HOH 16  316 596  HOH HOH I . 
GB 4 HOH 17  317 607  HOH HOH I . 
GB 4 HOH 18  318 624  HOH HOH I . 
GB 4 HOH 19  319 638  HOH HOH I . 
GB 4 HOH 20  320 645  HOH HOH I . 
GB 4 HOH 21  321 654  HOH HOH I . 
GB 4 HOH 22  322 665  HOH HOH I . 
GB 4 HOH 23  323 680  HOH HOH I . 
GB 4 HOH 24  324 689  HOH HOH I . 
GB 4 HOH 25  325 691  HOH HOH I . 
GB 4 HOH 26  326 710  HOH HOH I . 
GB 4 HOH 27  327 711  HOH HOH I . 
GB 4 HOH 28  328 722  HOH HOH I . 
GB 4 HOH 29  329 778  HOH HOH I . 
GB 4 HOH 30  330 799  HOH HOH I . 
GB 4 HOH 31  331 805  HOH HOH I . 
GB 4 HOH 32  332 814  HOH HOH I . 
GB 4 HOH 33  333 830  HOH HOH I . 
GB 4 HOH 34  334 837  HOH HOH I . 
GB 4 HOH 35  335 845  HOH HOH I . 
GB 4 HOH 36  336 846  HOH HOH I . 
GB 4 HOH 37  337 862  HOH HOH I . 
GB 4 HOH 38  338 884  HOH HOH I . 
GB 4 HOH 39  339 902  HOH HOH I . 
GB 4 HOH 40  340 906  HOH HOH I . 
GB 4 HOH 41  341 917  HOH HOH I . 
GB 4 HOH 42  342 967  HOH HOH I . 
GB 4 HOH 43  343 979  HOH HOH I . 
GB 4 HOH 44  344 983  HOH HOH I . 
GB 4 HOH 45  345 991  HOH HOH I . 
GB 4 HOH 46  346 996  HOH HOH I . 
GB 4 HOH 47  347 1009 HOH HOH I . 
GB 4 HOH 48  348 1038 HOH HOH I . 
GB 4 HOH 49  349 1040 HOH HOH I . 
GB 4 HOH 50  350 1042 HOH HOH I . 
GB 4 HOH 51  351 1047 HOH HOH I . 
GB 4 HOH 52  352 1093 HOH HOH I . 
HB 4 HOH 1   301 4    HOH HOH J . 
HB 4 HOH 2   302 15   HOH HOH J . 
HB 4 HOH 3   303 23   HOH HOH J . 
HB 4 HOH 4   304 27   HOH HOH J . 
HB 4 HOH 5   305 30   HOH HOH J . 
HB 4 HOH 6   306 36   HOH HOH J . 
HB 4 HOH 7   307 46   HOH HOH J . 
HB 4 HOH 8   308 50   HOH HOH J . 
HB 4 HOH 9   309 63   HOH HOH J . 
HB 4 HOH 10  310 83   HOH HOH J . 
HB 4 HOH 11  311 84   HOH HOH J . 
HB 4 HOH 12  312 93   HOH HOH J . 
HB 4 HOH 13  313 95   HOH HOH J . 
HB 4 HOH 14  314 98   HOH HOH J . 
HB 4 HOH 15  315 108  HOH HOH J . 
HB 4 HOH 16  316 114  HOH HOH J . 
HB 4 HOH 17  317 116  HOH HOH J . 
HB 4 HOH 18  318 125  HOH HOH J . 
HB 4 HOH 19  319 155  HOH HOH J . 
HB 4 HOH 20  320 156  HOH HOH J . 
HB 4 HOH 21  321 159  HOH HOH J . 
HB 4 HOH 22  322 166  HOH HOH J . 
HB 4 HOH 23  323 184  HOH HOH J . 
HB 4 HOH 24  324 187  HOH HOH J . 
HB 4 HOH 25  325 191  HOH HOH J . 
HB 4 HOH 26  326 197  HOH HOH J . 
HB 4 HOH 27  327 199  HOH HOH J . 
HB 4 HOH 28  328 211  HOH HOH J . 
HB 4 HOH 29  329 222  HOH HOH J . 
HB 4 HOH 30  330 229  HOH HOH J . 
HB 4 HOH 31  331 248  HOH HOH J . 
HB 4 HOH 32  332 254  HOH HOH J . 
HB 4 HOH 33  333 266  HOH HOH J . 
HB 4 HOH 34  334 269  HOH HOH J . 
HB 4 HOH 35  335 283  HOH HOH J . 
HB 4 HOH 36  336 307  HOH HOH J . 
HB 4 HOH 37  337 330  HOH HOH J . 
HB 4 HOH 38  338 334  HOH HOH J . 
HB 4 HOH 39  339 343  HOH HOH J . 
HB 4 HOH 40  340 349  HOH HOH J . 
HB 4 HOH 41  341 366  HOH HOH J . 
HB 4 HOH 42  342 369  HOH HOH J . 
HB 4 HOH 43  343 373  HOH HOH J . 
HB 4 HOH 44  344 415  HOH HOH J . 
HB 4 HOH 45  345 416  HOH HOH J . 
HB 4 HOH 46  346 425  HOH HOH J . 
HB 4 HOH 47  347 442  HOH HOH J . 
HB 4 HOH 48  348 455  HOH HOH J . 
HB 4 HOH 49  349 459  HOH HOH J . 
HB 4 HOH 50  350 460  HOH HOH J . 
HB 4 HOH 51  351 461  HOH HOH J . 
HB 4 HOH 52  352 487  HOH HOH J . 
HB 4 HOH 53  353 512  HOH HOH J . 
HB 4 HOH 54  354 520  HOH HOH J . 
HB 4 HOH 55  355 565  HOH HOH J . 
HB 4 HOH 56  356 566  HOH HOH J . 
HB 4 HOH 57  357 570  HOH HOH J . 
HB 4 HOH 58  358 571  HOH HOH J . 
HB 4 HOH 59  359 609  HOH HOH J . 
HB 4 HOH 60  360 611  HOH HOH J . 
HB 4 HOH 61  361 629  HOH HOH J . 
HB 4 HOH 62  362 631  HOH HOH J . 
HB 4 HOH 63  363 657  HOH HOH J . 
HB 4 HOH 64  364 664  HOH HOH J . 
HB 4 HOH 65  365 670  HOH HOH J . 
HB 4 HOH 66  366 678  HOH HOH J . 
HB 4 HOH 67  367 716  HOH HOH J . 
HB 4 HOH 68  368 718  HOH HOH J . 
HB 4 HOH 69  369 742  HOH HOH J . 
HB 4 HOH 70  370 767  HOH HOH J . 
HB 4 HOH 71  371 783  HOH HOH J . 
HB 4 HOH 72  372 802  HOH HOH J . 
HB 4 HOH 73  373 827  HOH HOH J . 
HB 4 HOH 74  374 832  HOH HOH J . 
HB 4 HOH 75  375 842  HOH HOH J . 
HB 4 HOH 76  376 847  HOH HOH J . 
HB 4 HOH 77  377 858  HOH HOH J . 
HB 4 HOH 78  378 866  HOH HOH J . 
HB 4 HOH 79  379 889  HOH HOH J . 
HB 4 HOH 80  380 893  HOH HOH J . 
HB 4 HOH 81  381 908  HOH HOH J . 
HB 4 HOH 82  382 920  HOH HOH J . 
HB 4 HOH 83  383 922  HOH HOH J . 
HB 4 HOH 84  384 928  HOH HOH J . 
HB 4 HOH 85  385 932  HOH HOH J . 
HB 4 HOH 86  386 946  HOH HOH J . 
HB 4 HOH 87  387 963  HOH HOH J . 
HB 4 HOH 88  388 968  HOH HOH J . 
HB 4 HOH 89  389 970  HOH HOH J . 
HB 4 HOH 90  390 984  HOH HOH J . 
HB 4 HOH 91  391 999  HOH HOH J . 
HB 4 HOH 92  392 1011 HOH HOH J . 
HB 4 HOH 93  393 1025 HOH HOH J . 
HB 4 HOH 94  394 1051 HOH HOH J . 
HB 4 HOH 95  395 1060 HOH HOH J . 
HB 4 HOH 96  396 1065 HOH HOH J . 
HB 4 HOH 97  397 1072 HOH HOH J . 
HB 4 HOH 98  398 1084 HOH HOH J . 
HB 4 HOH 99  399 1086 HOH HOH J . 
HB 4 HOH 100 400 1095 HOH HOH J . 
IB 4 HOH 1   301 202  HOH HOH K . 
IB 4 HOH 2   302 228  HOH HOH K . 
IB 4 HOH 3   303 284  HOH HOH K . 
IB 4 HOH 4   304 285  HOH HOH K . 
IB 4 HOH 5   305 357  HOH HOH K . 
IB 4 HOH 6   306 395  HOH HOH K . 
IB 4 HOH 7   307 400  HOH HOH K . 
IB 4 HOH 8   308 418  HOH HOH K . 
IB 4 HOH 9   309 453  HOH HOH K . 
IB 4 HOH 10  310 454  HOH HOH K . 
IB 4 HOH 11  311 470  HOH HOH K . 
IB 4 HOH 12  312 532  HOH HOH K . 
IB 4 HOH 13  313 593  HOH HOH K . 
IB 4 HOH 14  314 619  HOH HOH K . 
IB 4 HOH 15  315 634  HOH HOH K . 
IB 4 HOH 16  316 636  HOH HOH K . 
IB 4 HOH 17  317 649  HOH HOH K . 
IB 4 HOH 18  318 709  HOH HOH K . 
IB 4 HOH 19  319 727  HOH HOH K . 
IB 4 HOH 20  320 761  HOH HOH K . 
IB 4 HOH 21  321 772  HOH HOH K . 
IB 4 HOH 22  322 780  HOH HOH K . 
IB 4 HOH 23  323 812  HOH HOH K . 
IB 4 HOH 24  324 850  HOH HOH K . 
IB 4 HOH 25  325 869  HOH HOH K . 
IB 4 HOH 26  326 910  HOH HOH K . 
IB 4 HOH 27  327 965  HOH HOH K . 
IB 4 HOH 28  328 1008 HOH HOH K . 
IB 4 HOH 29  329 1013 HOH HOH K . 
IB 4 HOH 30  330 1017 HOH HOH K . 
IB 4 HOH 31  331 1050 HOH HOH K . 
IB 4 HOH 32  332 1068 HOH HOH K . 
IB 4 HOH 33  333 1090 HOH HOH K . 
JB 4 HOH 1   301 28   HOH HOH L . 
JB 4 HOH 2   302 34   HOH HOH L . 
JB 4 HOH 3   303 76   HOH HOH L . 
JB 4 HOH 4   304 94   HOH HOH L . 
JB 4 HOH 5   305 100  HOH HOH L . 
JB 4 HOH 6   306 107  HOH HOH L . 
JB 4 HOH 7   307 120  HOH HOH L . 
JB 4 HOH 8   308 143  HOH HOH L . 
JB 4 HOH 9   309 148  HOH HOH L . 
JB 4 HOH 10  310 172  HOH HOH L . 
JB 4 HOH 11  311 210  HOH HOH L . 
JB 4 HOH 12  312 220  HOH HOH L . 
JB 4 HOH 13  313 223  HOH HOH L . 
JB 4 HOH 14  314 249  HOH HOH L . 
JB 4 HOH 15  315 296  HOH HOH L . 
JB 4 HOH 16  316 313  HOH HOH L . 
JB 4 HOH 17  317 316  HOH HOH L . 
JB 4 HOH 18  318 319  HOH HOH L . 
JB 4 HOH 19  319 324  HOH HOH L . 
JB 4 HOH 20  320 344  HOH HOH L . 
JB 4 HOH 21  321 346  HOH HOH L . 
JB 4 HOH 22  322 353  HOH HOH L . 
JB 4 HOH 23  323 359  HOH HOH L . 
JB 4 HOH 24  324 364  HOH HOH L . 
JB 4 HOH 25  325 375  HOH HOH L . 
JB 4 HOH 26  326 378  HOH HOH L . 
JB 4 HOH 27  327 379  HOH HOH L . 
JB 4 HOH 28  328 440  HOH HOH L . 
JB 4 HOH 29  329 482  HOH HOH L . 
JB 4 HOH 30  330 486  HOH HOH L . 
JB 4 HOH 31  331 502  HOH HOH L . 
JB 4 HOH 32  332 510  HOH HOH L . 
JB 4 HOH 33  333 511  HOH HOH L . 
JB 4 HOH 34  334 527  HOH HOH L . 
JB 4 HOH 35  335 551  HOH HOH L . 
JB 4 HOH 36  336 552  HOH HOH L . 
JB 4 HOH 37  337 557  HOH HOH L . 
JB 4 HOH 38  338 579  HOH HOH L . 
JB 4 HOH 39  339 584  HOH HOH L . 
JB 4 HOH 40  340 585  HOH HOH L . 
JB 4 HOH 41  341 592  HOH HOH L . 
JB 4 HOH 42  342 608  HOH HOH L . 
JB 4 HOH 43  343 614  HOH HOH L . 
JB 4 HOH 44  344 616  HOH HOH L . 
JB 4 HOH 45  345 625  HOH HOH L . 
JB 4 HOH 46  346 630  HOH HOH L . 
JB 4 HOH 47  347 652  HOH HOH L . 
JB 4 HOH 48  348 660  HOH HOH L . 
JB 4 HOH 49  349 717  HOH HOH L . 
JB 4 HOH 50  350 721  HOH HOH L . 
JB 4 HOH 51  351 748  HOH HOH L . 
JB 4 HOH 52  352 750  HOH HOH L . 
JB 4 HOH 53  353 797  HOH HOH L . 
JB 4 HOH 54  354 801  HOH HOH L . 
JB 4 HOH 55  355 808  HOH HOH L . 
JB 4 HOH 56  356 815  HOH HOH L . 
JB 4 HOH 57  357 821  HOH HOH L . 
JB 4 HOH 58  358 873  HOH HOH L . 
JB 4 HOH 59  359 883  HOH HOH L . 
JB 4 HOH 60  360 892  HOH HOH L . 
JB 4 HOH 61  361 925  HOH HOH L . 
JB 4 HOH 62  362 944  HOH HOH L . 
JB 4 HOH 63  363 954  HOH HOH L . 
JB 4 HOH 64  364 961  HOH HOH L . 
JB 4 HOH 65  365 964  HOH HOH L . 
JB 4 HOH 66  366 966  HOH HOH L . 
JB 4 HOH 67  367 982  HOH HOH L . 
JB 4 HOH 68  368 1005 HOH HOH L . 
JB 4 HOH 69  369 1010 HOH HOH L . 
JB 4 HOH 70  370 1016 HOH HOH L . 
JB 4 HOH 71  371 1026 HOH HOH L . 
JB 4 HOH 72  372 1027 HOH HOH L . 
JB 4 HOH 73  373 1032 HOH HOH L . 
JB 4 HOH 74  374 1033 HOH HOH L . 
JB 4 HOH 75  375 1039 HOH HOH L . 
JB 4 HOH 76  376 1059 HOH HOH L . 
JB 4 HOH 77  377 1094 HOH HOH L . 
# 
