data_26806 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical Shift Assignment of Tom1 VHS Domain ; _BMRB_accession_number 26806 _BMRB_flat_file_name bmr26806.str _Entry_type original _Submission_date 2016-05-23 _Accession_date 2016-05-23 _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 Capelluto Daniel . . 2 Shanaiah Narasimhamurthy . . 3 Ellena Jeffrey . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 124 "13C chemical shifts" 380 "15N chemical shifts" 124 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2017-03-15 update BMRB 'update entry citation' 2016-10-13 original author 'original release' stop_ _Original_release_date 2016-10-13 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Backbone 1H, 15N, and 13C resonance assignments of the Tom1 VHS domain ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 27704363 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ellena Jeffrey . . 2 Xiong Wen . . 3 Zhao Xiaolin . . 4 Shanaiah Narasimhamurthy . . 5 Capelluto Daniel . . stop_ _Journal_abbreviation 'Biomol. NMR Assign.' _Journal_volume 11 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1 _Page_last 4 _Year 2017 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name Tom1-VHS _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Tom1-VHS $Tom1-VHS stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Tom1-VHS _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Tom1-VHS _Molecular_mass 15563.88 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 139 _Mol_residue_sequence ; SPVGQRIEKATDGSLQSEDW ALNMEICDIINETEEGPKDA LRAVKKRIVGNKNFHEVMLA LTVLETCVKNCGHRFHVLVA SQDFVESVLVRTILPKNNPP TIVHDKVLNLIQSWADAFRS SPDLTGVVTIYEDLRRKGL ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 11 SER 2 12 PRO 3 13 VAL 4 14 GLY 5 15 GLN 6 16 ARG 7 17 ILE 8 18 GLU 9 19 LYS 10 20 ALA 11 21 THR 12 22 ASP 13 23 GLY 14 24 SER 15 25 LEU 16 26 GLN 17 27 SER 18 28 GLU 19 29 ASP 20 30 TRP 21 31 ALA 22 32 LEU 23 33 ASN 24 34 MET 25 35 GLU 26 36 ILE 27 37 CYS 28 38 ASP 29 39 ILE 30 40 ILE 31 41 ASN 32 42 GLU 33 43 THR 34 44 GLU 35 45 GLU 36 46 GLY 37 47 PRO 38 48 LYS 39 49 ASP 40 50 ALA 41 51 LEU 42 52 ARG 43 53 ALA 44 54 VAL 45 55 LYS 46 56 LYS 47 57 ARG 48 58 ILE 49 59 VAL 50 60 GLY 51 61 ASN 52 62 LYS 53 63 ASN 54 64 PHE 55 65 HIS 56 66 GLU 57 67 VAL 58 68 MET 59 69 LEU 60 70 ALA 61 71 LEU 62 72 THR 63 73 VAL 64 74 LEU 65 75 GLU 66 76 THR 67 77 CYS 68 78 VAL 69 79 LYS 70 80 ASN 71 81 CYS 72 82 GLY 73 83 HIS 74 84 ARG 75 85 PHE 76 86 HIS 77 87 VAL 78 88 LEU 79 89 VAL 80 90 ALA 81 91 SER 82 92 GLN 83 93 ASP 84 94 PHE 85 95 VAL 86 96 GLU 87 97 SER 88 98 VAL 89 99 LEU 90 100 VAL 91 101 ARG 92 102 THR 93 103 ILE 94 104 LEU 95 105 PRO 96 106 LYS 97 107 ASN 98 108 ASN 99 109 PRO 100 110 PRO 101 111 THR 102 112 ILE 103 113 VAL 104 114 HIS 105 115 ASP 106 116 LYS 107 117 VAL 108 118 LEU 109 119 ASN 110 120 LEU 111 121 ILE 112 122 GLN 113 123 SER 114 124 TRP 115 125 ALA 116 126 ASP 117 127 ALA 118 128 PHE 119 129 ARG 120 130 SER 121 131 SER 122 132 PRO 123 133 ASP 124 134 LEU 125 135 THR 126 136 GLY 127 137 VAL 128 138 VAL 129 139 THR 130 140 ILE 131 141 TYR 132 142 GLU 133 143 ASP 134 144 LEU 135 145 ARG 136 146 ARG 137 147 LYS 138 148 GLY 139 149 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Tom1-VHS humans 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $Tom1-VHS 'recombinant technology' . Escherichia coli Rosetta pGEX4T3 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_Tom1-VHS_sam _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Tom1-VHS 800 uM '[U-13C; U-15N]' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task 'peak picking' stop_ _Details . save_ save_Sparky _Saveframe_category software _Name Sparky _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task processing stop_ _Details . save_ save_NMRview _Saveframe_category software _Name NMRview _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task processing stop_ _Details . save_ save_CCPNMR _Saveframe_category software _Name CCPNMR _Version . loop_ _Vendor _Address _Electronic_address 'Wayne Boucher and Tim Stevens' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model 'Avance III' _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $Tom1-VHS_sam save_ save_3D_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $Tom1-VHS_sam save_ save_3D_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $Tom1-VHS_sam save_ save_3D_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $Tom1-VHS_sam save_ save_3D_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $Tom1-VHS_sam save_ ####################### # Sample conditions # ####################### save_Tom1-VHS_con _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7 . pH temperature 273 . 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 C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 external direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 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_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCACB' '3D CBCA(CO)NH' '3D HNCA' '3D HNCO' stop_ loop_ _Sample_label $Tom1-VHS_sam stop_ _Sample_conditions_label $Tom1-VHS_con _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name Tom1-VHS _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 12 2 PRO C C 179.78 0.1 1 2 12 2 PRO CA C 65.45 0.1 1 3 12 2 PRO CB C 32.1 0.1 1 4 13 3 VAL H H 8.93 0.01 1 5 13 3 VAL C C 176.87 0.1 1 6 13 3 VAL CA C 65.64 0.1 1 7 13 3 VAL CB C 31.48 0.1 1 8 13 3 VAL N N 118.29 0.1 1 9 14 4 GLY H H 8.39 0.01 1 10 14 4 GLY CA C 47.7 0.1 1 11 14 4 GLY N N 111.98 0.1 1 12 15 5 GLN C C 179.23 0.1 1 13 15 5 GLN CA C 58.9 0.1 1 14 15 5 GLN CB C 28.57 0.1 1 15 16 6 ARG H H 7.24 0.01 1 16 16 6 ARG C C 178.44 0.1 1 17 16 6 ARG CA C 58.92 0.1 1 18 16 6 ARG CB C 30.2 0.1 1 19 16 6 ARG N N 117.9 0.1 1 20 17 7 ILE H H 8.45 0.01 1 21 17 7 ILE C C 178.54 0.1 1 22 17 7 ILE CA C 65.99 0.1 1 23 17 7 ILE CB C 37.35 0.1 1 24 17 7 ILE N N 119.96 0.1 1 25 18 8 GLU H H 8.39 0.01 1 26 18 8 GLU C C 178.41 0.1 1 27 18 8 GLU CA C 60.92 0.1 1 28 18 8 GLU CB C 29.21 0.1 1 29 18 8 GLU N N 122.59 0.1 1 30 19 9 LYS H H 7.37 0.01 1 31 19 9 LYS C C 178.35 0.1 1 32 19 9 LYS CA C 59.56 0.1 1 33 19 9 LYS CB C 32.52 0.1 1 34 19 9 LYS N N 118.57 0.1 1 35 20 10 ALA H H 8.29 0.01 1 36 20 10 ALA C C 176.73 0.1 1 37 20 10 ALA CA C 53.63 0.1 1 38 20 10 ALA CB C 20.17 0.1 1 39 20 10 ALA N N 118.69 0.1 1 40 21 11 THR H H 7.17 0.01 1 41 21 11 THR C C 171.65 0.1 1 42 21 11 THR CA C 59.36 0.1 1 43 21 11 THR CB C 69.26 0.1 1 44 21 11 THR N N 102.45 0.1 1 45 22 12 ASP H H 6.66 0.01 1 46 22 12 ASP C C 177.13 0.1 1 47 22 12 ASP CA C 54.94 0.1 1 48 22 12 ASP CB C 43.93 0.1 1 49 22 12 ASP N N 122.42 0.1 1 50 23 13 GLY H H 9.29 0.01 1 51 23 13 GLY C C 174.22 0.1 1 52 23 13 GLY CA C 47.23 0.1 1 53 23 13 GLY N N 111.76 0.1 1 54 24 14 SER H H 8.67 0.01 1 55 24 14 SER C C 175.71 0.1 1 56 24 14 SER CA C 60.05 0.1 1 57 24 14 SER CB C 63.65 0.1 1 58 24 14 SER N N 115.37 0.1 1 59 25 15 LEU H H 8.17 0.01 1 60 25 15 LEU CA C 55.84 0.1 1 61 25 15 LEU CB C 41.62 0.1 1 62 25 15 LEU N N 125.5 0.1 1 63 26 16 GLN C C 176.04 0.1 1 64 26 16 GLN CA C 57.75 0.1 1 65 26 16 GLN CB C 29.24 0.1 1 66 27 17 SER H H 7.69 0.01 1 67 27 17 SER C C 171.75 0.1 1 68 27 17 SER CA C 56.71 0.1 1 69 27 17 SER CB C 64.81 0.1 1 70 27 17 SER N N 110.14 0.1 1 71 28 18 GLU H H 9.47 0.01 1 72 28 18 GLU C C 175.31 0.1 1 73 28 18 GLU CA C 58.06 0.1 1 74 28 18 GLU CB C 28.8 0.1 1 75 28 18 GLU N N 119.71 0.1 1 76 29 19 ASP H H 8.9 0.01 1 77 29 19 ASP C C 175.57 0.1 1 78 29 19 ASP CA C 52.1 0.1 1 79 29 19 ASP CB C 40.97 0.1 1 80 29 19 ASP N N 123.63 0.1 1 81 30 20 TRP H H 8.06 0.01 1 82 30 20 TRP C C 178.19 0.1 1 83 30 20 TRP CA C 61.04 0.1 1 84 30 20 TRP CB C 28.9 0.1 1 85 30 20 TRP N N 123.81 0.1 1 86 31 21 ALA H H 8.19 0.01 1 87 31 21 ALA C C 181.17 0.1 1 88 31 21 ALA CA C 55.22 0.1 1 89 31 21 ALA CB C 17.72 0.1 1 90 31 21 ALA N N 121.82 0.1 1 91 32 22 LEU H H 7.94 0.01 1 92 32 22 LEU C C 178.73 0.1 1 93 32 22 LEU CA C 57.33 0.1 1 94 32 22 LEU CB C 41.47 0.1 1 95 32 22 LEU N N 122.8 0.1 1 96 33 23 ASN H H 8.6 0.01 1 97 33 23 ASN C C 178.87 0.1 1 98 33 23 ASN CA C 56.27 0.1 1 99 33 23 ASN CB C 36.44 0.1 1 100 33 23 ASN N N 119.45 0.1 1 101 34 24 MET H H 8.13 0.01 1 102 34 24 MET C C 178.23 0.1 1 103 34 24 MET CA C 57.35 0.1 1 104 34 24 MET CB C 30.31 0.1 1 105 34 24 MET N N 118.77 0.1 1 106 35 25 GLU H H 7.97 0.01 1 107 35 25 GLU C C 179.11 0.1 1 108 35 25 GLU CA C 59.82 0.1 1 109 35 25 GLU CB C 29.59 0.1 1 110 35 25 GLU N N 123.63 0.1 1 111 36 26 ILE H H 8.3 0.01 1 112 36 26 ILE C C 176.93 0.1 1 113 36 26 ILE CA C 66.48 0.1 1 114 36 26 ILE CB C 37.69 0.1 1 115 36 26 ILE N N 118.59 0.1 1 116 37 27 CYS H H 7.13 0.01 1 117 37 27 CYS C C 175.63 0.1 1 118 37 27 CYS CA C 63.83 0.1 1 119 37 27 CYS CB C 26.47 0.1 1 120 37 27 CYS N N 116.13 0.1 1 121 38 28 ASP H H 7.87 0.01 1 122 38 28 ASP C C 178.28 0.1 1 123 38 28 ASP CA C 57.93 0.1 1 124 38 28 ASP CB C 40.07 0.1 1 125 38 28 ASP N N 119.57 0.1 1 126 39 29 ILE H H 8.11 0.01 1 127 39 29 ILE C C 180.04 0.1 1 128 39 29 ILE CA C 65.23 0.1 1 129 39 29 ILE CB C 38.2 0.1 1 130 39 29 ILE N N 119.32 0.1 1 131 40 30 ILE H H 8.23 0.01 1 132 40 30 ILE C C 177 0.1 1 133 40 30 ILE CA C 67.07 0.1 1 134 40 30 ILE CB C 37.73 0.1 1 135 40 30 ILE N N 122.11 0.1 1 136 41 31 ASN H H 8.1 0.01 1 137 41 31 ASN C C 177.21 0.1 1 138 41 31 ASN CA C 55.2 0.1 1 139 41 31 ASN CB C 38.14 0.1 1 140 41 31 ASN N N 114.5 0.1 1 141 42 32 GLU H H 7.92 0.01 1 142 42 32 GLU C C 176.52 0.1 1 143 42 32 GLU CA C 56.71 0.1 1 144 42 32 GLU CB C 31.25 0.1 1 145 42 32 GLU N N 116.84 0.1 1 146 43 33 THR H H 7.52 0.01 1 147 43 33 THR CA C 60.08 0.1 1 148 43 33 THR CB C 72.7 0.1 1 149 43 33 THR N N 109.11 0.1 1 150 47 37 PRO C C 177.64 0.1 1 151 47 37 PRO CA C 67.59 0.1 1 152 47 37 PRO CB C 31.49 0.1 1 153 48 38 LYS H H 8.14 0.01 1 154 48 38 LYS C C 179.83 0.1 1 155 48 38 LYS CA C 57.79 0.1 1 156 48 38 LYS CB C 30.51 0.1 1 157 48 38 LYS N N 118.59 0.1 1 158 49 39 ASP H H 8.18 0.01 1 159 49 39 ASP C C 180.62 0.1 1 160 49 39 ASP CA C 58.24 0.1 1 161 49 39 ASP CB C 41.98 0.1 1 162 49 39 ASP N N 120.92 0.1 1 163 50 40 ALA H H 8.57 0.01 1 164 50 40 ALA C C 179.23 0.1 1 165 50 40 ALA CA C 55.57 0.1 1 166 50 40 ALA CB C 18.18 0.1 1 167 50 40 ALA N N 122.88 0.1 1 168 51 41 LEU H H 9.05 0.01 1 169 51 41 LEU C C 179.27 0.1 1 170 51 41 LEU CA C 58.24 0.1 1 171 51 41 LEU CB C 41.49 0.1 1 172 51 41 LEU N N 120.19 0.1 1 173 52 42 ARG H H 7.9 0.01 1 174 52 42 ARG C C 178.85 0.1 1 175 52 42 ARG CA C 59.97 0.1 1 176 52 42 ARG CB C 30.29 0.1 1 177 52 42 ARG N N 117.8 0.1 1 178 53 43 ALA H H 7.67 0.01 1 179 53 43 ALA C C 180.23 0.1 1 180 53 43 ALA CA C 54.9 0.1 1 181 53 43 ALA CB C 19.71 0.1 1 182 53 43 ALA N N 120.93 0.1 1 183 54 44 VAL H H 8.77 0.01 1 184 54 44 VAL C C 177.55 0.1 1 185 54 44 VAL CA C 67.45 0.1 1 186 54 44 VAL CB C 31.57 0.1 1 187 54 44 VAL N N 118.21 0.1 1 188 55 45 LYS H H 8.44 0.01 1 189 55 45 LYS C C 177.77 0.1 1 190 55 45 LYS CA C 61.26 0.1 1 191 55 45 LYS CB C 32.58 0.1 1 192 55 45 LYS N N 119.65 0.1 1 193 56 46 LYS H H 7.65 0.01 1 194 56 46 LYS C C 178.33 0.1 1 195 56 46 LYS CA C 58.62 0.1 1 196 56 46 LYS CB C 32.4 0.1 1 197 56 46 LYS N N 116.38 0.1 1 198 57 47 ARG H H 7.49 0.01 1 199 57 47 ARG C C 175.57 0.1 1 200 57 47 ARG CA C 55.23 0.1 1 201 57 47 ARG CB C 28.84 0.1 1 202 57 47 ARG N N 115.07 0.1 1 203 58 48 ILE H H 7.59 0.01 1 204 58 48 ILE C C 177.41 0.1 1 205 58 48 ILE CA C 64.91 0.1 1 206 58 48 ILE CB C 40.68 0.1 1 207 58 48 ILE N N 115.63 0.1 1 208 59 49 VAL H H 8.37 0.01 1 209 59 49 VAL C C 178.39 0.1 1 210 59 49 VAL CA C 65.81 0.1 1 211 59 49 VAL CB C 30.74 0.1 1 212 59 49 VAL N N 119.93 0.1 1 213 60 50 GLY H H 9.02 0.01 1 214 60 50 GLY C C 173.1 0.1 1 215 60 50 GLY CA C 45.4 0.1 1 216 60 50 GLY N N 116.86 0.1 1 217 61 51 ASN H H 7.5 0.01 1 218 61 51 ASN C C 175.85 0.1 1 219 61 51 ASN CA C 52.89 0.1 1 220 61 51 ASN CB C 38.49 0.1 1 221 61 51 ASN N N 119.67 0.1 1 222 62 52 LYS H H 8.5 0.01 1 223 62 52 LYS C C 175.82 0.1 1 224 62 52 LYS CA C 54.96 0.1 1 225 62 52 LYS CB C 31.66 0.1 1 226 62 52 LYS N N 124.02 0.1 1 227 63 53 ASN H H 8.42 0.01 1 228 63 53 ASN C C 175.67 0.1 1 229 63 53 ASN CA C 51.67 0.1 1 230 63 53 ASN CB C 36.94 0.1 1 231 63 53 ASN N N 119.35 0.1 1 232 64 54 PHE H H 8.43 0.01 1 233 64 54 PHE C C 177.1 0.1 1 234 64 54 PHE CA C 62.39 0.1 1 235 64 54 PHE CB C 38.07 0.1 1 236 64 54 PHE N N 121.41 0.1 1 237 65 55 HIS H H 8.36 0.01 1 238 65 55 HIS C C 177.45 0.1 1 239 65 55 HIS CA C 59.85 0.1 1 240 65 55 HIS CB C 30.71 0.1 1 241 65 55 HIS N N 123.02 0.1 1 242 66 56 GLU H H 7.1 0.01 1 243 66 56 GLU C C 179.42 0.1 1 244 66 56 GLU CA C 59.83 0.1 1 245 66 56 GLU CB C 30.25 0.1 1 246 66 56 GLU N N 117.81 0.1 1 247 67 57 VAL H H 7.59 0.01 1 248 67 57 VAL C C 176.84 0.1 1 249 67 57 VAL CA C 67.56 0.1 1 250 67 57 VAL CB C 31.68 0.1 1 251 67 57 VAL N N 116.74 0.1 1 252 68 58 MET H H 7.82 0.01 1 253 68 58 MET C C 179.72 0.1 1 254 68 58 MET CA C 59.95 0.1 1 255 68 58 MET CB C 32.27 0.1 1 256 68 58 MET N N 116.35 0.1 1 257 69 59 LEU H H 8.66 0.01 1 258 69 59 LEU C C 179.93 0.1 1 259 69 59 LEU CA C 57.4 0.1 1 260 69 59 LEU CB C 40.32 0.1 1 261 69 59 LEU N N 121.18 0.1 1 262 70 60 ALA H H 8.92 0.01 1 263 70 60 ALA C C 179.13 0.1 1 264 70 60 ALA CA C 54.78 0.1 1 265 70 60 ALA CB C 19.1 0.1 1 266 70 60 ALA N N 123.15 0.1 1 267 71 61 LEU H H 8.03 0.01 1 268 71 61 LEU C C 179.1 0.1 1 269 71 61 LEU CA C 58.3 0.1 1 270 71 61 LEU CB C 41.35 0.1 1 271 71 61 LEU N N 118.75 0.1 1 272 72 62 THR H H 8.28 0.01 1 273 72 62 THR C C 178.13 0.1 1 274 72 62 THR CA C 67.11 0.1 1 275 72 62 THR CB C 67.89 0.1 1 276 72 62 THR N N 118.06 0.1 1 277 73 63 VAL H H 8.13 0.01 1 278 73 63 VAL C C 178.13 0.1 1 279 73 63 VAL CA C 67.34 0.1 1 280 73 63 VAL CB C 31.6 0.1 1 281 73 63 VAL N N 126.91 0.1 1 282 74 64 LEU H H 8.57 0.01 1 283 74 64 LEU C C 177.7 0.1 1 284 74 64 LEU CA C 59.05 0.1 1 285 74 64 LEU CB C 42.64 0.1 1 286 74 64 LEU N N 121.02 0.1 1 287 75 65 GLU H H 8.97 0.01 1 288 75 65 GLU C C 179.09 0.1 1 289 75 65 GLU CA C 59.95 0.1 1 290 75 65 GLU CB C 31.07 0.1 1 291 75 65 GLU N N 119.33 0.1 1 292 76 66 THR H H 8.35 0.01 1 293 76 66 THR C C 176.67 0.1 1 294 76 66 THR CA C 67.23 0.1 1 295 76 66 THR CB C 68.77 0.1 1 296 76 66 THR N N 117.49 0.1 1 297 77 67 CYS H H 8.73 0.01 1 298 77 67 CYS C C 177.1 0.1 1 299 77 67 CYS CA C 62.84 0.1 1 300 77 67 CYS CB C 27.64 0.1 1 301 77 67 CYS N N 121.7 0.1 1 302 78 68 VAL H H 8.45 0.01 1 303 78 68 VAL C C 178.05 0.1 1 304 78 68 VAL CA C 68.5 0.1 1 305 78 68 VAL CB C 31.07 0.1 1 306 78 68 VAL N N 120.2 0.1 1 307 79 69 LYS H H 7.68 0.01 1 308 79 69 LYS C C 178.66 0.1 1 309 79 69 LYS CA C 59.84 0.1 1 310 79 69 LYS CB C 33.15 0.1 1 311 79 69 LYS N N 117.39 0.1 1 312 80 70 ASN H H 7.55 0.01 1 313 80 70 ASN C C 177.29 0.1 1 314 80 70 ASN CA C 54.85 0.1 1 315 80 70 ASN CB C 42.39 0.1 1 316 80 70 ASN N N 112.64 0.1 1 317 81 71 CYS H H 8.2 0.01 1 318 81 71 CYS C C 174.98 0.1 1 319 81 71 CYS CA C 59.4 0.1 1 320 81 71 CYS CB C 29.48 0.1 1 321 81 71 CYS N N 117.2 0.1 1 322 82 72 GLY H H 8.02 0.01 1 323 82 72 GLY CA C 44.85 0.1 1 324 82 72 GLY N N 105.98 0.1 1 325 83 73 HIS C C 175.86 0.1 1 326 83 73 HIS CA C 60.56 0.1 1 327 83 73 HIS CB C 31.03 0.1 1 328 84 74 ARG H H 8.51 0.01 1 329 84 74 ARG C C 176.61 0.1 1 330 84 74 ARG CA C 58.41 0.1 1 331 84 74 ARG CB C 30.19 0.1 1 332 84 74 ARG N N 112.81 0.1 1 333 85 75 PHE H H 7.35 0.01 1 334 85 75 PHE C C 176.27 0.1 1 335 85 75 PHE CA C 60.42 0.1 1 336 85 75 PHE CB C 42.15 0.1 1 337 85 75 PHE N N 117.78 0.1 1 338 86 76 HIS H H 8.08 0.01 1 339 86 76 HIS C C 176.51 0.1 1 340 86 76 HIS CA C 57.32 0.1 1 341 86 76 HIS CB C 31.56 0.1 1 342 86 76 HIS N N 120.36 0.1 1 343 87 77 VAL H H 8.08 0.01 1 344 87 77 VAL C C 177.29 0.1 1 345 87 77 VAL CA C 64.53 0.1 1 346 87 77 VAL CB C 31.7 0.1 1 347 87 77 VAL N N 111.82 0.1 1 348 88 78 LEU H H 6.69 0.01 1 349 88 78 LEU C C 178.6 0.1 1 350 88 78 LEU CA C 56.35 0.1 1 351 88 78 LEU CB C 41.93 0.1 1 352 88 78 LEU N N 117.88 0.1 1 353 89 79 VAL H H 6.78 0.01 1 354 89 79 VAL C C 173.63 0.1 1 355 89 79 VAL CA C 62.55 0.1 1 356 89 79 VAL CB C 30.94 0.1 1 357 89 79 VAL N N 114.53 0.1 1 358 90 80 ALA H H 7.56 0.01 1 359 90 80 ALA C C 176.7 0.1 1 360 90 80 ALA CA C 51.85 0.1 1 361 90 80 ALA CB C 19.79 0.1 1 362 90 80 ALA N N 116.01 0.1 1 363 91 81 SER H H 6.94 0.01 1 364 91 81 SER C C 175.08 0.1 1 365 91 81 SER CA C 57.91 0.1 1 366 91 81 SER CB C 64.71 0.1 1 367 91 81 SER N N 110.28 0.1 1 368 92 82 GLN H H 9.26 0.01 1 369 92 82 GLN C C 177.11 0.1 1 370 92 82 GLN CA C 60 0.1 1 371 92 82 GLN CB C 27.97 0.1 1 372 92 82 GLN N N 125.25 0.1 1 373 93 83 ASP H H 8.43 0.01 1 374 93 83 ASP C C 178.67 0.1 1 375 93 83 ASP CA C 57.18 0.1 1 376 93 83 ASP CB C 41.55 0.1 1 377 93 83 ASP N N 115.34 0.1 1 378 94 84 PHE H H 7.85 0.01 1 379 94 84 PHE C C 176.81 0.1 1 380 94 84 PHE CA C 62.42 0.1 1 381 94 84 PHE CB C 39.23 0.1 1 382 94 84 PHE N N 122.11 0.1 1 383 95 85 VAL H H 8.51 0.01 1 384 95 85 VAL C C 178.97 0.1 1 385 95 85 VAL CA C 67.62 0.1 1 386 95 85 VAL CB C 31.83 0.1 1 387 95 85 VAL N N 118.5 0.1 1 388 96 86 GLU H H 9.02 0.01 1 389 96 86 GLU C C 178.12 0.1 1 390 96 86 GLU CA C 60.48 0.1 1 391 96 86 GLU CB C 30.16 0.1 1 392 96 86 GLU N N 118.38 0.1 1 393 97 87 SER H H 7.89 0.01 1 394 97 87 SER C C 174.52 0.1 1 395 97 87 SER CA C 61.75 0.1 1 396 97 87 SER CB C 63.9 0.1 1 397 97 87 SER N N 112.2 0.1 1 398 98 88 VAL H H 7.85 0.01 1 399 98 88 VAL C C 175.85 0.1 1 400 98 88 VAL CA C 64.04 0.1 1 401 98 88 VAL CB C 31.77 0.1 1 402 98 88 VAL N N 117.89 0.1 1 403 99 89 LEU H H 6.98 0.01 1 404 99 89 LEU C C 176.77 0.1 1 405 99 89 LEU CA C 57.68 0.1 1 406 99 89 LEU CB C 40.92 0.1 1 407 99 89 LEU N N 117.68 0.1 1 408 100 90 VAL H H 8.71 0.01 1 409 100 90 VAL C C 178.57 0.1 1 410 100 90 VAL CA C 67.33 0.1 1 411 100 90 VAL CB C 30.66 0.1 1 412 100 90 VAL N N 118.77 0.1 1 413 101 91 ARG H H 7.28 0.01 1 414 101 91 ARG C C 177.9 0.1 1 415 101 91 ARG CA C 59.27 0.1 1 416 101 91 ARG CB C 30.15 0.1 1 417 101 91 ARG N N 115.23 0.1 1 418 102 92 THR H H 6.72 0.01 1 419 102 92 THR C C 174.86 0.1 1 420 102 92 THR CA C 65.56 0.1 1 421 102 92 THR CB C 69.11 0.1 1 422 102 92 THR N N 111.64 0.1 1 423 103 93 ILE H H 7.35 0.01 1 424 103 93 ILE C C 174.63 0.1 1 425 103 93 ILE CA C 60.26 0.1 1 426 103 93 ILE CB C 37.63 0.1 1 427 103 93 ILE N N 108.82 0.1 1 428 104 94 LEU H H 7.12 0.01 1 429 104 94 LEU CA C 54.09 0.1 1 430 104 94 LEU CB C 41 0.1 1 431 104 94 LEU N N 123.46 0.1 1 432 105 95 PRO C C 176.53 0.1 1 433 105 95 PRO CA C 55.45 0.1 1 434 105 95 PRO CB C 42.05 0.1 1 435 106 96 LYS H H 7.8 0.01 1 436 106 96 LYS C C 176.73 0.1 1 437 106 96 LYS CA C 57.87 0.1 1 438 106 96 LYS CB C 31.52 0.1 1 439 106 96 LYS N N 126.48 0.1 1 440 107 97 ASN H H 8.3 0.01 1 441 107 97 ASN C C 174.58 0.1 1 442 107 97 ASN CA C 53 0.1 1 443 107 97 ASN CB C 39.52 0.1 1 444 107 97 ASN N N 117.5 0.1 1 445 108 98 ASN H H 8.07 0.01 1 446 108 98 ASN CA C 53.95 0.1 1 447 108 98 ASN CB C 38.62 0.1 1 448 108 98 ASN N N 114.08 0.1 1 449 110 100 PRO C C 179.05 0.1 1 450 111 101 THR H H 8.35 0.01 1 451 111 101 THR C C 176 0.1 1 452 111 101 THR CA C 66.97 0.1 1 453 111 101 THR CB C 68.75 0.1 1 454 111 101 THR N N 117.48 0.1 1 455 112 102 ILE H H 8.31 0.01 1 456 112 102 ILE C C 177.84 0.1 1 457 112 102 ILE CA C 64.98 0.1 1 458 112 102 ILE CB C 37.99 0.1 1 459 112 102 ILE N N 115.62 0.1 1 460 113 103 VAL H H 6.85 0.01 1 461 113 103 VAL C C 176.34 0.1 1 462 113 103 VAL CA C 65.38 0.1 1 463 113 103 VAL CB C 32.21 0.1 1 464 113 103 VAL N N 121.71 0.1 1 465 114 104 HIS H H 7.73 0.01 1 466 114 104 HIS C C 176.2 0.1 1 467 114 104 HIS CA C 60.64 0.1 1 468 114 104 HIS CB C 30.19 0.1 1 469 114 104 HIS N N 119.86 0.1 1 470 115 105 ASP H H 8.93 0.01 1 471 115 105 ASP C C 178.4 0.1 1 472 115 105 ASP CA C 56.97 0.1 1 473 115 105 ASP CB C 39.84 0.1 1 474 115 105 ASP N N 115.91 0.1 1 475 116 106 LYS H H 7.65 0.01 1 476 116 106 LYS C C 178.3 0.1 1 477 116 106 LYS CA C 58.41 0.1 1 478 116 106 LYS CB C 31.67 0.1 1 479 116 106 LYS N N 120.74 0.1 1 480 117 107 VAL H H 8.38 0.01 1 481 117 107 VAL C C 177.4 0.1 1 482 117 107 VAL CA C 68.08 0.1 1 483 117 107 VAL CB C 31.24 0.1 1 484 117 107 VAL N N 118.07 0.1 1 485 118 108 LEU H H 7.84 0.01 1 486 118 108 LEU C C 179.29 0.1 1 487 118 108 LEU CA C 58.14 0.1 1 488 118 108 LEU CB C 40.59 0.1 1 489 118 108 LEU N N 118.07 0.1 1 490 119 109 ASN H H 8.21 0.01 1 491 119 109 ASN C C 178.21 0.1 1 492 119 109 ASN CA C 56.48 0.1 1 493 119 109 ASN CB C 38.97 0.1 1 494 119 109 ASN N N 117.83 0.1 1 495 120 110 LEU H H 8.21 0.01 1 496 120 110 LEU C C 176.93 0.1 1 497 120 110 LEU CA C 57.99 0.1 1 498 120 110 LEU CB C 40.63 0.1 1 499 120 110 LEU N N 123.12 0.1 1 500 121 111 ILE H H 7.82 0.01 1 501 121 111 ILE C C 177.03 0.1 1 502 121 111 ILE CA C 66.37 0.1 1 503 121 111 ILE CB C 37.89 0.1 1 504 121 111 ILE N N 116.34 0.1 1 505 122 112 GLN H H 7.97 0.01 1 506 122 112 GLN C C 177.42 0.1 1 507 122 112 GLN CA C 59.26 0.1 1 508 122 112 GLN CB C 28.26 0.1 1 509 122 112 GLN N N 117.92 0.1 1 510 123 113 SER H H 8 0.01 1 511 123 113 SER C C 177.84 0.1 1 512 123 113 SER CA C 61.71 0.1 1 513 123 113 SER CB C 62.9 0.1 1 514 123 113 SER N N 114.65 0.1 1 515 124 114 TRP H H 8.63 0.01 1 516 124 114 TRP C C 176.82 0.1 1 517 124 114 TRP CA C 57.21 0.1 1 518 124 114 TRP CB C 28.68 0.1 1 519 124 114 TRP N N 124.53 0.1 1 520 125 115 ALA H H 8.52 0.01 1 521 125 115 ALA C C 179.05 0.1 1 522 125 115 ALA CA C 55.68 0.1 1 523 125 115 ALA CB C 18.35 0.1 1 524 125 115 ALA N N 120.86 0.1 1 525 126 116 ASP H H 7.78 0.01 1 526 126 116 ASP C C 178.64 0.1 1 527 126 116 ASP CA C 56.9 0.1 1 528 126 116 ASP CB C 40.85 0.1 1 529 126 116 ASP N N 114.29 0.1 1 530 127 117 ALA H H 7.76 0.01 1 531 127 117 ALA C C 180.44 0.1 1 532 127 117 ALA CA C 54.5 0.1 1 533 127 117 ALA CB C 18.55 0.1 1 534 127 117 ALA N N 121.13 0.1 1 535 128 118 PHE H H 8.65 0.01 1 536 128 118 PHE C C 177.59 0.1 1 537 128 118 PHE CA C 54.84 0.1 1 538 128 118 PHE CB C 37.86 0.1 1 539 128 118 PHE N N 116.27 0.1 1 540 129 119 ARG H H 7.38 0.01 1 541 129 119 ARG CA C 59.81 0.1 1 542 129 119 ARG CB C 30 0.1 1 543 129 119 ARG N N 119.3 0.1 1 544 132 122 PRO C C 176.85 0.1 1 545 132 122 PRO CA C 64.89 0.1 1 546 132 122 PRO CB C 32.09 0.1 1 547 133 123 ASP H H 8.54 0.01 1 548 133 123 ASP C C 176.31 0.1 1 549 133 123 ASP CA C 54.28 0.1 1 550 133 123 ASP CB C 40.09 0.1 1 551 133 123 ASP N N 114.45 0.1 1 552 134 124 LEU H H 7.53 0.01 1 553 134 124 LEU C C 175.84 0.1 1 554 134 124 LEU CA C 54.02 0.1 1 555 134 124 LEU CB C 41.14 0.1 1 556 134 124 LEU N N 119.92 0.1 1 557 135 125 THR H H 7.19 0.01 1 558 135 125 THR C C 177.25 0.1 1 559 135 125 THR CA C 64.3 0.1 1 560 135 125 THR CB C 70.02 0.1 1 561 135 125 THR N N 106.6 0.1 1 562 136 126 GLY H H 9.16 0.01 1 563 136 126 GLY C C 176.85 0.1 1 564 136 126 GLY CA C 48.59 0.1 1 565 136 126 GLY N N 114.02 0.1 1 566 137 127 VAL H H 7.97 0.01 1 567 137 127 VAL C C 174.98 0.1 1 568 137 127 VAL CA C 64.73 0.1 1 569 137 127 VAL CB C 32.01 0.1 1 570 137 127 VAL N N 117.92 0.1 1 571 138 128 VAL H H 7.27 0.01 1 572 138 128 VAL C C 177.95 0.1 1 573 138 128 VAL CA C 66.72 0.1 1 574 138 128 VAL CB C 31.57 0.1 1 575 138 128 VAL N N 123.13 0.1 1 576 139 129 THR H H 8.42 0.01 1 577 139 129 THR C C 177.1 0.1 1 578 139 129 THR CA C 66.27 0.1 1 579 139 129 THR CB C 69.15 0.1 1 580 139 129 THR N N 115.79 0.1 1 581 140 130 ILE H H 7.87 0.01 1 582 140 130 ILE C C 177.64 0.1 1 583 140 130 ILE CA C 64.11 0.1 1 584 140 130 ILE CB C 37.42 0.1 1 585 140 130 ILE N N 121.18 0.1 1 586 141 131 TYR H H 8.51 0.01 1 587 141 131 TYR C C 176.75 0.1 1 588 141 131 TYR CA C 61.81 0.1 1 589 141 131 TYR CB C 38.11 0.1 1 590 141 131 TYR N N 120.71 0.1 1 591 142 132 GLU H H 8.24 0.01 1 592 142 132 GLU C C 179.28 0.1 1 593 142 132 GLU CA C 59.22 0.1 1 594 142 132 GLU CB C 28.87 0.1 1 595 142 132 GLU N N 116.57 0.1 1 596 143 133 ASP H H 7.89 0.01 1 597 143 133 ASP C C 178.55 0.1 1 598 143 133 ASP CA C 57.43 0.1 1 599 143 133 ASP CB C 41.39 0.1 1 600 143 133 ASP N N 120.28 0.1 1 601 144 134 LEU H H 8.45 0.01 1 602 144 134 LEU C C 180.15 0.1 1 603 144 134 LEU CA C 58.02 0.1 1 604 144 134 LEU CB C 41.52 0.1 1 605 144 134 LEU N N 120.22 0.1 1 606 145 135 ARG H H 8.18 0.01 1 607 145 135 ARG C C 179.06 0.1 1 608 145 135 ARG CA C 58.29 0.1 1 609 145 135 ARG CB C 29.58 0.1 1 610 145 135 ARG N N 118.64 0.1 1 611 146 136 ARG H H 7.77 0.01 1 612 146 136 ARG C C 177.88 0.1 1 613 146 136 ARG CA C 58.47 0.1 1 614 146 136 ARG CB C 30.32 0.1 1 615 146 136 ARG N N 119.6 0.1 1 616 147 137 LYS H H 7.94 0.01 1 617 147 137 LYS C C 177.14 0.1 1 618 147 137 LYS CA C 57.23 0.1 1 619 147 137 LYS CB C 33.32 0.1 1 620 147 137 LYS N N 118.05 0.1 1 621 148 138 GLY H H 7.91 0.01 1 622 148 138 GLY C C 173.23 0.1 1 623 148 138 GLY CA C 45.47 0.1 1 624 148 138 GLY N N 108.57 0.1 1 625 149 139 LEU H H 7.62 0.01 1 626 149 139 LEU CA C 56.81 0.1 1 627 149 139 LEU CB C 43.33 0.1 1 628 149 139 LEU N N 126.58 0.1 1 stop_ save_