data_18132 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; THERMOSTABLE PROTEIN FROM HYPERTHERMOPHILIC VIRUS SSV-RH ; _BMRB_accession_number 18132 _BMRB_flat_file_name bmr18132.str _Entry_type original _Submission_date 2011-12-09 _Accession_date 2011-12-09 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Schlenker C. . . 2 Goel Anupam . . 3 Tripet B. P. . 4 Menon S. . . 5 Lawrence C. M. . 6 Copie V. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 269 "13C chemical shifts" 171 "15N chemical shifts" 69 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2012-05-10 update BMRB 'update entry citation' 2012-03-23 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Structural studies of E73 from a hyperthermophilic archaeal virus identify the "RH3" domain, an elaborated ribbon-helix-helix motif involved in DNA recognition.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 22409376 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Schlenker Casey . . 2 Goel Anupam . . 3 Tripet Brian P. . 4 Menon Smita . . 5 Willi Taylor . . 6 Dlakic Mensur . . 7 Young Mark J. . 8 Lawrence 'C. Martin' . . 9 Copie Valerie . . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 51 _Journal_issue 13 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2899 _Page_last 2910 _Year 2012 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'THERMOSTABLE PROTEIN FROM HYPERTHERMOPHILIC VIRUS SSV-RH' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'ORF E73, chain 1' $ORF_E73 'ORF E73, chain 2' $ORF_E73 stop_ _System_molecular_weight 17254.399 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_ORF_E73 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common ORF_E73 _Molecular_mass 8627.1995 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 73 _Mol_residue_sequence ; MVESKKIAKKKTTLAFDEDV YHTLKLVSVYLNRDMTEIIE EAVVMWLIQNKEKLPNELKP KIDEISKRFFPAK ; loop_ _Residue_seq_code _Residue_label 1 MET 2 VAL 3 GLU 4 SER 5 LYS 6 LYS 7 ILE 8 ALA 9 LYS 10 LYS 11 LYS 12 THR 13 THR 14 LEU 15 ALA 16 PHE 17 ASP 18 GLU 19 ASP 20 VAL 21 TYR 22 HIS 23 THR 24 LEU 25 LYS 26 LEU 27 VAL 28 SER 29 VAL 30 TYR 31 LEU 32 ASN 33 ARG 34 ASP 35 MET 36 THR 37 GLU 38 ILE 39 ILE 40 GLU 41 GLU 42 ALA 43 VAL 44 VAL 45 MET 46 TRP 47 LEU 48 ILE 49 GLN 50 ASN 51 LYS 52 GLU 53 LYS 54 LEU 55 PRO 56 ASN 57 GLU 58 LEU 59 LYS 60 PRO 61 LYS 62 ILE 63 ASP 64 GLU 65 ILE 66 SER 67 LYS 68 ARG 69 PHE 70 PHE 71 PRO 72 ALA 73 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-03-04 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 16177 E73 100.00 80 100.00 100.00 1.05e-43 BMRB 17069 E73 100.00 80 100.00 100.00 1.05e-43 PDB 4AAI "Thermostable Protein From Hyperthermophilic Virus Ssv-rh" 97.26 73 100.00 100.00 5.59e-42 GB AAR27912 "ORF E73 [Sulfolobus virus Ragged Hills]" 100.00 73 100.00 100.00 1.68e-43 REF NP_963940 "ORF E73 [Sulfolobus virus Ragged Hills]" 100.00 73 100.00 100.00 1.68e-43 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Details $ORF_E73 'Sulfolobus virus Ragged Hills' 256994 Viruses . Fusellovirus 'Sulfolobus virus Ragged Hills' 'ORF E73 obtained from Sulfolobus Spindle shaped virus (Ragged Hills) that attacks the Crenarchaea sulfolobus solfatarcus' stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Cell_line _Vector_type _Vector_name $ORF_E73 'recombinant technology' 'Escherichia coli' Escherichia coli . 'BL21 (DE3)' Pet14 na stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '1 mM' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $ORF_E73 1 mM '[U-13C; U-15N]' 'SODIUM AZIDE' 0.01 % 'natural abundance' 'POTASSIUM PHOSPHATE' 50 mM 'natural abundance' EDTA 1 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_ARIA _Saveframe_category software _Name ARIA _Version any loop_ _Vendor _Address _Electronic_address 'Linge, O'Donoghue and Nilges' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_AutoDep _Saveframe_category software _Name AutoDep _Version 4.3 loop_ _Vendor _Address _Electronic_address PDBe . . stop_ loop_ _Task collection stop_ _Details . save_ save_CNS _Saveframe_category software _Name CNS _Version any loop_ _Vendor _Address _Electronic_address BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details 'REFINEMENT DETAILS CAN BE FOUND IN THE' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_Bruker_DMX-600 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_HNCACB_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_C(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _Sample_label $sample_1 save_ save_3D_H(CCO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D H(CCO)NH' _Sample_label $sample_1 save_ save_3D_HNCA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_1 save_ save_3D_HBHA(CO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HBHA(CO)NH' _Sample_label $sample_1 save_ save_3D_HCCH-TOCSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_9 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_NMR_spectrometer_expt _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details 'pH [5.0], temp [312], pressure [1], ionStrength [0.05]' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.050 . mM pH 5.000 . pH pressure 1.000 . atm temperature 312.000 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 6.1 internal indirect . . . 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list _Saveframe_category assigned_chemical_shifts _Details 'Origin nmrStar file /ebi/msd/pdb_root/Processing/prepare/4aai/ebi/chemical_shift.str.csh' loop_ _Experiment_label '3D HNCACB' '3D CBCA(CO)NH' '3D C(CO)NH' '3D H(CCO)NH' '3D HNCA' '2D 1H-13C HSQC' '3D HBHA(CO)NH' '3D HCCH-TOCSY' '2D 1H-15N HSQC' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'ORF E73, chain 1' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 1 MET HA H 4.343 . 1 2 1 1 MET HB2 H 1.900 . 1 3 1 1 MET HG2 H 2.364 . 1 4 1 1 MET CA C 55.976 . 1 5 1 1 MET CB C 33.446 . 1 6 1 1 MET CG C 32.504 . 1 7 2 2 VAL H H 8.021 . 1 8 2 2 VAL HA H 3.975 . 1 9 2 2 VAL HB H 1.938 . 1 10 2 2 VAL HG1 H 0.803 . 1 11 2 2 VAL CA C 62.802 . 1 12 2 2 VAL CB C 33.192 . 1 13 2 2 VAL CG1 C 21.239 . 1 14 2 2 VAL CG2 C 21.351 . 1 15 2 2 VAL N N 121.358 . 1 16 3 3 GLU H H 8.353 . 1 17 3 3 GLU HA H 4.195 . 1 18 3 3 GLU HB2 H 1.888 . 1 19 3 3 GLU HG2 H 2.132 . 1 20 3 3 GLU CA C 56.968 . 1 21 3 3 GLU CB C 30.819 . 1 22 3 3 GLU CG C 36.677 . 1 23 3 3 GLU N N 124.728 . 1 24 4 4 SER H H 8.189 . 1 25 4 4 SER HA H 4.284 . 1 26 4 4 SER HB2 H 3.741 . 1 27 4 4 SER HB3 H 3.742 . 1 28 4 4 SER CA C 58.859 . 1 29 4 4 SER CB C 64.084 . 1 30 4 4 SER N N 117.206 . 1 31 5 5 LYS H H 8.119 . 1 32 5 5 LYS HA H 3.986 . 1 33 5 5 LYS HB2 H 1.679 . 1 34 5 5 LYS HG2 H 1.307 . 1 35 5 5 LYS HD2 H 1.579 . 1 36 5 5 LYS CA C 56.674 . 1 37 5 5 LYS CB C 33.415 . 1 38 5 5 LYS CG C 25.121 . 1 39 5 5 LYS CD C 29.567 . 1 40 5 5 LYS CE C 42.519 . 1 41 5 5 LYS N N 122.777 . 1 42 6 6 LYS H H 8.111 . 1 43 6 6 LYS HA H 4.212 . 1 44 6 6 LYS HB2 H 1.652 . 1 45 6 6 LYS HB3 H 1.830 . 1 46 6 6 LYS HG2 H 1.567 . 1 47 6 6 LYS HG3 H 1.306 . 1 48 6 6 LYS HD2 H 1.724 . 1 49 6 6 LYS HD3 H 1.624 . 1 50 6 6 LYS HE2 H 2.863 . 1 51 6 6 LYS CA C 56.531 . 1 52 6 6 LYS CB C 33.430 . 1 53 6 6 LYS CG C 25.166 . 1 54 6 6 LYS CD C 29.357 . 1 55 6 6 LYS CE C 42.954 . 1 56 6 6 LYS N N 122.547 . 1 57 7 7 ILE H H 7.975 . 1 58 7 7 ILE HA H 4.043 . 1 59 7 7 ILE HB H 1.704 . 1 60 7 7 ILE HG12 H 1.386 . 1 61 7 7 ILE HG13 H 1.122 . 1 62 7 7 ILE HG2 H 0.933 . 1 63 7 7 ILE HD1 H 0.727 . 1 64 7 7 ILE CA C 61.045 . 1 65 7 7 ILE CB C 39.221 . 1 66 7 7 ILE CG2 C 18.148 . 1 67 7 7 ILE CD1 C 12.913 . 1 68 7 7 ILE N N 123.836 . 1 69 8 8 ALA H H 8.442 . 1 70 8 8 ALA HA H 4.264 . 1 71 8 8 ALA HB H 1.299 . 1 72 8 8 ALA CA C 52.668 . 1 73 8 8 ALA CB C 20.027 . 1 74 8 8 ALA N N 130.325 . 1 75 9 9 LYS H H 8.068 . 1 76 9 9 LYS HA H 4.779 . 1 77 9 9 LYS HB2 H 1.235 . 1 78 9 9 LYS HB3 H 1.560 . 1 79 9 9 LYS HG2 H 1.295 . 1 80 9 9 LYS HG3 H 1.059 . 1 81 9 9 LYS HD2 H 1.458 . 1 82 9 9 LYS HE2 H 2.778 . 1 83 9 9 LYS CA C 54.572 . 1 84 9 9 LYS CB C 35.552 . 1 85 9 9 LYS CG C 25.021 . 1 86 9 9 LYS CD C 29.479 . 1 87 9 9 LYS CE C 42.791 . 1 88 9 9 LYS N N 117.661 . 1 89 10 10 LYS H H 9.150 . 1 90 10 10 LYS HA H 4.327 . 1 91 10 10 LYS HB2 H 1.173 . 1 92 10 10 LYS HB3 H 1.289 . 1 93 10 10 LYS HG2 H 0.595 . 1 94 10 10 LYS HG3 H 0.842 . 1 95 10 10 LYS HD2 H 1.279 . 1 96 10 10 LYS HD3 H 1.165 . 1 97 10 10 LYS HE2 H 2.587 . 1 98 10 10 LYS HE3 H 2.467 . 1 99 10 10 LYS CA C 54.457 . 1 100 10 10 LYS CB C 34.941 . 1 101 10 10 LYS CG C 24.337 . 1 102 10 10 LYS CD C 28.606 . 1 103 10 10 LYS CE C 42.348 . 1 104 10 10 LYS N N 123.396 . 1 105 11 11 LYS H H 8.381 . 1 106 11 11 LYS HA H 4.771 . 1 107 11 11 LYS HB2 H 1.535 . 1 108 11 11 LYS HB3 H 1.454 . 1 109 11 11 LYS HG2 H 1.091 . 1 110 11 11 LYS HD2 H 1.238 . 1 111 11 11 LYS HD3 H 1.261 . 1 112 11 11 LYS HE2 H 2.764 . 1 113 11 11 LYS CA C 56.473 . 1 114 11 11 LYS CB C 33.807 . 1 115 11 11 LYS CG C 25.675 . 1 116 11 11 LYS CD C 29.303 . 1 117 11 11 LYS CE C 42.319 . 1 118 11 11 LYS N N 125.807 . 1 119 12 12 THR H H 8.716 . 1 120 12 12 THR HA H 4.491 . 1 121 12 12 THR HB H 3.760 . 1 122 12 12 THR HG2 H 0.976 . 1 123 12 12 THR CA C 61.408 . 1 124 12 12 THR CB C 70.848 . 1 125 12 12 THR N N 119.245 . 1 126 13 13 THR H H 8.187 . 1 127 13 13 THR HA H 4.912 . 1 128 13 13 THR HB H 3.784 . 1 129 13 13 THR HG2 H 0.937 . 1 130 13 13 THR CA C 62.590 . 1 131 13 13 THR CB C 70.610 . 1 132 13 13 THR CG2 C 22.172 . 1 133 13 13 THR N N 122.630 . 1 134 14 14 LEU H H 8.707 . 1 135 14 14 LEU HA H 4.429 . 1 136 14 14 LEU HB2 H 1.230 . 1 137 14 14 LEU HB3 H 1.284 . 1 138 14 14 LEU HG H 1.389 . 1 139 14 14 LEU HD1 H 0.731 . 1 140 14 14 LEU HD2 H 0.667 . 1 141 14 14 LEU CA C 53.835 . 1 142 14 14 LEU CB C 45.299 . 1 143 14 14 LEU CG C 27.505 . 1 144 14 14 LEU CD1 C 24.946 . 1 145 14 14 LEU N N 126.794 . 1 146 15 15 ALA H H 7.768 . 1 147 15 15 ALA HA H 4.834 . 1 148 15 15 ALA HB H 0.980 . 1 149 15 15 ALA CA C 50.828 . 1 150 15 15 ALA CB C 20.869 . 1 151 15 15 ALA N N 122.460 . 1 152 16 16 PHE H H 8.267 . 1 153 16 16 PHE HA H 4.835 . 1 154 16 16 PHE HB2 H 3.202 . 1 155 16 16 PHE HB3 H 2.639 . 1 156 16 16 PHE CA C 55.964 . 1 157 16 16 PHE CB C 44.260 . 1 158 16 16 PHE N N 120.500 . 1 159 17 17 ASP H H 9.562 . 1 160 17 17 ASP HA H 4.568 . 1 161 17 17 ASP HB2 H 2.791 . 1 162 17 17 ASP HB3 H 2.581 . 1 163 17 17 ASP CA C 56.474 . 1 164 17 17 ASP CB C 42.236 . 1 165 17 17 ASP N N 124.606 . 1 166 18 18 GLU H H 8.990 . 1 167 18 18 GLU HA H 3.742 . 1 168 18 18 GLU HB2 H 1.901 . 1 169 18 18 GLU HB3 H 1.835 . 1 170 18 18 GLU HG2 H 2.221 . 1 171 18 18 GLU HG3 H 2.120 . 1 172 18 18 GLU CA C 60.959 . 1 173 18 18 GLU CB C 30.287 . 1 174 18 18 GLU CG C 36.589 . 1 175 18 18 GLU N N 123.565 . 1 176 19 19 ASP H H 8.334 . 1 177 19 19 ASP HA H 4.527 . 1 178 19 19 ASP HB2 H 2.694 . 1 179 19 19 ASP HB3 H 2.372 . 1 180 19 19 ASP CA C 56.926 . 1 181 19 19 ASP CB C 39.231 . 1 182 19 19 ASP N N 118.092 . 1 183 20 20 VAL H H 8.026 . 1 184 20 20 VAL HA H 3.275 . 1 185 20 20 VAL HB H 2.301 . 1 186 20 20 VAL HG1 H 0.947 . 1 187 20 20 VAL HG2 H 0.653 . 1 188 20 20 VAL CA C 67.607 . 1 189 20 20 VAL CB C 32.260 . 1 190 20 20 VAL CG1 C 23.800 . 1 191 20 20 VAL N N 126.938 . 1 192 21 21 TYR H H 8.367 . 1 193 21 21 TYR HA H 3.554 . 1 194 21 21 TYR HB2 H 2.965 . 1 195 21 21 TYR HB3 H 2.736 . 1 196 21 21 TYR CA C 63.011 . 1 197 21 21 TYR CB C 38.985 . 1 198 21 21 TYR N N 118.599 . 1 199 22 22 HIS H H 8.851 . 1 200 22 22 HIS HA H 4.050 . 1 201 22 22 HIS HB2 H 3.369 . 1 202 22 22 HIS HB3 H 3.189 . 1 203 22 22 HIS CA C 60.312 . 1 204 22 22 HIS CB C 30.311 . 1 205 22 22 HIS N N 116.358 . 1 206 23 23 THR H H 7.870 . 1 207 23 23 THR HA H 4.125 . 1 208 23 23 THR HB H 3.649 . 1 209 23 23 THR CA C 68.442 . 1 210 23 23 THR CG2 C 22.108 . 1 211 23 23 THR N N 115.251 . 1 212 24 24 LEU H H 8.260 . 1 213 24 24 LEU HA H 3.734 . 1 214 24 24 LEU HB2 H 1.384 . 1 215 24 24 LEU HB3 H 1.410 . 1 216 24 24 LEU HD1 H 0.768 . 1 217 24 24 LEU HD2 H 0.474 . 1 218 24 24 LEU CA C 58.398 . 1 219 24 24 LEU CB C 42.398 . 1 220 24 24 LEU CG C 24.981 . 1 221 24 24 LEU CD1 C 24.419 . 1 222 24 24 LEU N N 121.640 . 1 223 25 25 LYS H H 8.224 . 1 224 25 25 LYS HA H 3.742 . 1 225 25 25 LYS HB2 H 1.436 . 1 226 25 25 LYS HB3 H 1.729 . 1 227 25 25 LYS HG2 H 1.158 . 1 228 25 25 LYS HD2 H 1.479 . 1 229 25 25 LYS HE2 H 2.816 . 1 230 25 25 LYS CA C 60.037 . 1 231 25 25 LYS CB C 31.717 . 1 232 25 25 LYS CG C 25.034 . 1 233 25 25 LYS CD C 29.458 . 1 234 25 25 LYS CE C 42.444 . 1 235 25 25 LYS N N 120.687 . 1 236 26 26 LEU H H 7.607 . 1 237 26 26 LEU HA H 3.936 . 1 238 26 26 LEU HB2 H 1.898 . 1 239 26 26 LEU HB3 H 1.373 . 1 240 26 26 LEU HG H 1.598 . 1 241 26 26 LEU HD1 H 0.756 . 1 242 26 26 LEU CA C 58.553 . 1 243 26 26 LEU CB C 42.463 . 1 244 26 26 LEU CG C 25.773 . 1 245 26 26 LEU CD1 C 23.062 . 1 246 26 26 LEU N N 119.051 . 1 247 27 27 VAL H H 8.411 . 1 248 27 27 VAL HA H 3.461 . 1 249 27 27 VAL HB H 2.250 . 1 250 27 27 VAL HG1 H 1.048 . 1 251 27 27 VAL HG2 H 1.069 . 1 252 27 27 VAL CA C 67.719 . 1 253 27 27 VAL CB C 32.060 . 1 254 27 27 VAL CG1 C 23.109 . 1 255 27 27 VAL CG2 C 23.071 . 1 256 27 27 VAL N N 120.057 . 1 257 28 28 SER H H 8.443 . 1 258 28 28 SER HA H 3.973 . 1 259 28 28 SER CA C 63.069 . 1 260 28 28 SER N N 115.928 . 1 261 29 29 VAL H H 7.521 . 1 262 29 29 VAL HA H 3.748 . 1 263 29 29 VAL HB H 2.048 . 1 264 29 29 VAL HG1 H 1.017 . 1 265 29 29 VAL HG2 H 0.873 . 1 266 29 29 VAL CA C 66.369 . 1 267 29 29 VAL CB C 32.336 . 1 268 29 29 VAL CG1 C 22.837 . 1 269 29 29 VAL N N 120.712 . 1 270 30 30 TYR H H 7.968 . 1 271 30 30 TYR HA H 4.157 . 1 272 30 30 TYR HB2 H 3.149 . 1 273 30 30 TYR HB3 H 2.943 . 1 274 30 30 TYR CA C 62.036 . 1 275 30 30 TYR CB C 38.921 . 1 276 30 30 TYR N N 121.113 . 1 277 31 31 LEU H H 8.417 . 1 278 31 31 LEU HA H 4.051 . 1 279 31 31 LEU HB2 H 1.610 . 1 280 31 31 LEU HB3 H 1.504 . 1 281 31 31 LEU HG H 1.961 . 1 282 31 31 LEU HD1 H 0.989 . 1 283 31 31 LEU HD2 H 0.908 . 1 284 31 31 LEU CA C 55.028 . 1 285 31 31 LEU CB C 42.674 . 1 286 31 31 LEU CG C 27.174 . 1 287 31 31 LEU CD1 C 22.484 . 1 288 31 31 LEU N N 114.228 . 1 289 32 32 ASN H H 7.822 . 1 290 32 32 ASN HA H 4.220 . 1 291 32 32 ASN HB2 H 3.112 . 1 292 32 32 ASN HB3 H 2.519 . 1 293 32 32 ASN CA C 54.292 . 1 294 32 32 ASN CB C 37.677 . 1 295 32 32 ASN N N 117.898 . 1 296 33 33 ARG H H 7.944 . 1 297 33 33 ARG HA H 4.525 . 1 298 33 33 ARG HB2 H 1.669 . 1 299 33 33 ARG HB3 H 1.179 . 1 300 33 33 ARG HG2 H 1.498 . 1 301 33 33 ARG HG3 H 1.660 . 1 302 33 33 ARG HD2 H 3.256 . 1 303 33 33 ARG HD3 H 2.769 . 1 304 33 33 ARG CA C 54.725 . 1 305 33 33 ARG CB C 35.662 . 1 306 33 33 ARG CG C 27.074 . 1 307 33 33 ARG CD C 44.183 . 1 308 33 33 ARG N N 116.306 . 1 309 34 34 ASP H H 8.481 . 1 310 34 34 ASP HA H 4.311 . 1 311 34 34 ASP HB2 H 2.493 . 1 312 34 34 ASP HB3 H 2.572 . 1 313 34 34 ASP CA C 54.939 . 1 314 34 34 ASP CB C 43.261 . 1 315 34 34 ASP N N 122.875 . 1 316 35 35 MET H H 8.745 . 1 317 35 35 MET HA H 3.591 . 1 318 35 35 MET HB2 H 1.937 . 1 319 35 35 MET HG2 H 2.189 . 1 320 35 35 MET CA C 60.618 . 1 321 35 35 MET CB C 34.191 . 1 322 35 35 MET CG C 32.443 . 1 323 35 35 MET N N 125.065 . 1 324 36 36 THR H H 8.314 . 1 325 36 36 THR HA H 3.590 . 1 326 36 36 THR HB H 4.141 . 1 327 36 36 THR HG2 H 1.141 . 1 328 36 36 THR CA C 67.160 . 1 329 36 36 THR CB C 68.463 . 1 330 36 36 THR CG2 C 23.005 . 1 331 36 36 THR N N 112.506 . 1 332 37 37 GLU H H 7.312 . 1 333 37 37 GLU HA H 4.089 . 1 334 37 37 GLU HB2 H 2.123 . 1 335 37 37 GLU HB3 H 2.255 . 1 336 37 37 GLU HG2 H 2.260 . 1 337 37 37 GLU HG3 H 2.300 . 1 338 37 37 GLU CA C 59.658 . 1 339 37 37 GLU CB C 30.167 . 1 340 37 37 GLU CG C 37.355 . 1 341 37 37 GLU N N 121.383 . 1 342 38 38 ILE H H 7.207 . 1 343 38 38 ILE HA H 2.982 . 1 344 38 38 ILE HB H 1.302 . 1 345 38 38 ILE HG12 H 1.275 . 1 346 38 38 ILE HG2 H 0.443 . 1 347 38 38 ILE HD1 H 0.428 . 1 348 38 38 ILE CA C 65.725 . 1 349 38 38 ILE CB C 37.747 . 1 350 38 38 ILE CG2 C 14.264 . 1 351 38 38 ILE N N 118.923 . 1 352 39 39 ILE H H 7.756 . 1 353 39 39 ILE HA H 3.089 . 1 354 39 39 ILE HB H 1.655 . 1 355 39 39 ILE HG13 H 0.721 . 1 356 39 39 ILE HG2 H 0.674 . 1 357 39 39 ILE HD1 H 0.504 . 1 358 39 39 ILE CA C 66.580 . 1 359 39 39 ILE CB C 37.923 . 1 360 39 39 ILE CG2 C 18.243 . 1 361 39 39 ILE N N 117.749 . 1 362 40 40 GLU H H 8.164 . 1 363 40 40 GLU HA H 3.628 . 1 364 40 40 GLU HB2 H 2.097 . 1 365 40 40 GLU HB3 H 1.964 . 1 366 40 40 GLU HG2 H 2.281 . 1 367 40 40 GLU HG3 H 2.240 . 1 368 40 40 GLU CA C 61.668 . 1 369 40 40 GLU CB C 29.922 . 1 370 40 40 GLU CG C 38.746 . 1 371 40 40 GLU N N 117.948 . 1 372 41 41 GLU H H 7.952 . 1 373 41 41 GLU HA H 3.538 . 1 374 41 41 GLU HB2 H 2.146 . 1 375 41 41 GLU HG2 H 2.368 . 1 376 41 41 GLU HG3 H 2.433 . 1 377 41 41 GLU CA C 61.253 . 1 378 41 41 GLU CB C 30.458 . 1 379 41 41 GLU CG C 38.972 . 1 380 41 41 GLU N N 119.281 . 1 381 42 42 ALA H H 8.458 . 1 382 42 42 ALA HA H 4.038 . 1 383 42 42 ALA HB H 1.246 . 1 384 42 42 ALA CA C 55.889 . 1 385 42 42 ALA CB C 17.733 . 1 386 42 42 ALA N N 120.358 . 1 387 43 43 VAL H H 8.474 . 1 388 43 43 VAL HA H 3.449 . 1 389 43 43 VAL HB H 2.168 . 1 390 43 43 VAL HG1 H 0.906 . 1 391 43 43 VAL HG2 H 0.671 . 1 392 43 43 VAL CA C 67.362 . 1 393 43 43 VAL CB C 31.916 . 1 394 43 43 VAL CG1 C 22.717 . 1 395 43 43 VAL CG2 C 22.727 . 1 396 43 43 VAL N N 119.540 . 1 397 44 44 VAL H H 8.361 . 1 398 44 44 VAL HA H 3.402 . 1 399 44 44 VAL HB H 1.833 . 1 400 44 44 VAL HG1 H 0.742 . 1 401 44 44 VAL HG2 H 0.155 . 1 402 44 44 VAL CA C 68.759 . 1 403 44 44 VAL CB C 31.462 . 1 404 44 44 VAL N N 121.473 . 1 405 45 45 MET H H 8.681 . 1 406 45 45 MET HA H 4.063 . 1 407 45 45 MET HB2 H 2.273 . 1 408 45 45 MET HB3 H 2.265 . 1 409 45 45 MET HG2 H 2.821 . 1 410 45 45 MET HG3 H 2.549 . 1 411 45 45 MET CA C 59.733 . 1 412 45 45 MET CB C 33.079 . 1 413 45 45 MET CG C 33.166 . 1 414 45 45 MET N N 117.866 . 1 415 46 46 TRP H H 8.302 . 1 416 46 46 TRP HA H 3.929 . 1 417 46 46 TRP HB2 H 3.652 . 1 418 46 46 TRP HB3 H 3.213 . 1 419 46 46 TRP CA C 63.129 . 1 420 46 46 TRP CB C 30.767 . 1 421 46 46 TRP N N 121.939 . 1 422 47 47 LEU H H 8.779 . 1 423 47 47 LEU HA H 3.767 . 1 424 47 47 LEU HB2 H 2.331 . 1 425 47 47 LEU HB3 H 1.234 . 1 426 47 47 LEU HG H 2.290 . 1 427 47 47 LEU HD1 H 0.753 . 1 428 47 47 LEU HD2 H 0.930 . 1 429 47 47 LEU CA C 59.240 . 1 430 47 47 LEU CB C 42.369 . 1 431 47 47 LEU CG C 26.524 . 1 432 47 47 LEU CD1 C 24.008 . 1 433 47 47 LEU N N 121.457 . 1 434 48 48 ILE H H 4.066 . 1 435 48 48 ILE HA H 3.353 . 1 436 48 48 ILE HB H 1.827 . 1 437 48 48 ILE HG12 H 0.936 . 1 438 48 48 ILE HD1 H 0.771 . 1 439 48 48 ILE C C 0.119 . 1 440 48 48 ILE N N 0.099 . 1 441 49 49 GLN H H 0.006 . 1 442 49 49 GLN C C 0.069 . 1 443 49 49 GLN N N 0.079 . 1 444 50 50 ASN H H 0.008 . 1 445 50 50 ASN C C 0.123 . 1 446 50 50 ASN N N 0.041 . 1 447 51 51 LYS H H 0.008 . 1 448 51 51 LYS C C 0.196 . 1 449 51 51 LYS N N 0.055 . 1 450 52 52 GLU H H 0.056 . 1 451 52 52 GLU C C 0.089 . 1 452 52 52 GLU N N 0.152 . 1 453 53 53 LYS H H 0.120 . 1 454 53 53 LYS C C 0.188 . 1 455 53 53 LYS N N 0.054 . 1 456 54 54 LEU H H 0.010 . 1 457 54 54 LEU C C 0.078 . 1 458 54 54 LEU N N 0.044 . 1 459 55 55 PRO C C 0.092 . 1 460 56 56 ASN H H 0.008 . 1 461 56 56 ASN C C 0.114 . 1 462 56 56 ASN N N 0.121 . 1 463 57 57 GLU H H 0.009 . 1 464 57 57 GLU C C 0.088 . 1 465 57 57 GLU N N 0.044 . 1 466 58 58 LEU H H 0.006 . 1 467 58 58 LEU C C 0.071 . 1 468 58 58 LEU N N 0.047 . 1 469 59 59 LYS H H 0.007 . 1 470 59 59 LYS C C 0.224 . 1 471 59 59 LYS N N 0.053 . 1 472 60 60 PRO C C 0.047 . 1 473 61 61 LYS H H 0.006 . 1 474 61 61 LYS C C 0.112 . 1 475 61 61 LYS N N 0.065 . 1 476 62 62 ILE H H 0.008 . 1 477 62 62 ILE C C 0.087 . 1 478 62 62 ILE N N 0.053 . 1 479 63 63 ASP H H 0.010 . 1 480 63 63 ASP C C 0.106 . 1 481 63 63 ASP N N 0.061 . 1 482 64 64 GLU H H 0.008 . 1 483 64 64 GLU C C 0.074 . 1 484 64 64 GLU N N 0.072 . 1 485 65 65 ILE H H 0.010 . 1 486 65 65 ILE C C 0.102 . 1 487 65 65 ILE N N 0.102 . 1 488 66 66 SER H H 0.011 . 1 489 66 66 SER C C 0.253 . 1 490 66 66 SER N N 0.031 . 1 491 67 67 LYS H H 0.002 . 1 492 67 67 LYS C C 0.256 . 1 493 67 67 LYS N N 0.057 . 1 494 68 68 ARG H H 0.011 . 1 495 68 68 ARG C C 0.174 . 1 496 68 68 ARG N N 0.125 . 1 497 69 69 PHE H H 0.009 . 1 498 69 69 PHE C C 0.124 . 1 499 69 69 PHE N N 0.067 . 1 500 70 70 PHE H H 0.009 . 1 501 70 70 PHE C C 0.088 . 1 502 70 70 PHE N N 0.115 . 1 503 71 71 PRO C C 0.178 . 1 504 72 72 ALA H H 0.004 . 1 505 72 72 ALA C C 0.037 . 1 506 72 72 ALA N N 0.049 . 1 507 73 73 LYS H H 0.006 . 1 508 73 73 LYS C C 0.300 . 1 509 73 73 LYS N N 0.041 . 1 stop_ save_