data_4355 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, 15N Chemical Shift Assignments for the Asymmetric Strands of the Tetramerization Domain of the Mnt Repressor ; _BMRB_accession_number 4355 _BMRB_flat_file_name bmr4355.str _Entry_type original _Submission_date 1999-06-13 _Accession_date 1999-06-13 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; Two sets of resonances (A and B) are given, corresponding to the two asymmetric peptide chains in the structure of the homotetramer. ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Nooren Irene M.A. . 2 Kaptein Robert . . 3 Sauer Robert T. . 4 Boelens Rolf . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 391 "13C chemical shifts" 266 "15N chemical shifts" 68 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-10-07 original author . stop_ _Original_release_date 1999-10-07 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; The Tetramerization Domain of the Mnt Repressor Consists of two Right-handed Coiled Coils ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99356013 _PubMed_ID 10426954 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Nooren Irene M.A. . 2 Kaptein Robert . . 3 Sauer Robert T. . 4 Boelens Rolf . . stop_ _Journal_abbreviation 'Nat. Struct. Biol.' _Journal_volume 6 _Journal_issue 8 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 755 _Page_last 759 _Year 1999 _Details . loop_ _Keyword asymmetry 'coiled coil' homotetramer 'inter-subunit NOE' 'isotope filter' oligomer 'protein dynamics' 'protein structure' 'slow chemical exchange' stop_ save_ ################################## # Molecular system description # ################################## save_system_Mnt-C _Saveframe_category molecular_system _Mol_system_name 'tetramerization domain of the Mnt repressor' _Abbreviation_common Mnt-C _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Mnt-C subunit A' $Mnt-C 'Mnt-C subunit B' $Mnt-C 'Mnt-C subunit C' $Mnt-C 'Mnt-C subunit D' $Mnt-C stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state tetramer _System_paramagnetic no _System_thiol_state . loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'Mnt-C subunit A' 2 'Mnt-C subunit B' 1 'Mnt-C subunit C' 2 'Mnt-C subunit D' stop_ loop_ _Biological_function 'transcription regulatory protein' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Mnt-C _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'homotetrameric peptide' _Abbreviation_common Mnt-C _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 37 _Mol_residue_sequence ; RNDAERLADEQSELVKKMVF DTLKDLYKKTTHHHHHH ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 52 ARG 2 53 ASN 3 54 ASP 4 55 ALA 5 56 GLU 6 57 ARG 7 58 LEU 8 59 ALA 9 60 ASP 10 61 GLU 11 62 GLN 12 63 SER 13 64 GLU 14 65 LEU 15 66 VAL 16 67 LYS 17 68 LYS 18 69 MET 19 70 VAL 20 71 PHE 21 72 ASP 22 73 THR 23 74 LEU 24 75 LYS 25 76 ASP 26 77 LEU 27 78 TYR 28 79 LYS 29 80 LYS 30 81 THR 31 82 THR 32 83 HIS 33 84 HIS 34 85 HIS 35 86 HIS 36 87 HIS 37 88 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-17 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 4356 "homotetrameric peptide" 100.00 37 100.00 100.00 3.39e-16 PDB 1MNT "Solution Structure Of Dimeric Mnt Repressor (1-76)" 67.57 76 100.00 100.00 1.97e-07 PDB 1QEY "Nmr Structure Determination Of The Tetramerization Domain Of The Mnt Repressor: An Asymmetric A-Helical Assembly In Slow Exchan" 83.78 31 100.00 100.00 6.97e-12 DBJ BAF80731 "transcriptional repressor [Enterobacteria phage P22]" 83.78 83 100.00 100.00 7.73e-12 DBJ BAG12614 "transcriptional repressor [Enterobacteria phage P22]" 83.78 83 100.00 100.00 7.73e-12 EMBL CAA25989 "unnamed protein product [Enterobacteria phage P22]" 83.78 83 100.00 100.00 7.73e-12 GB AAF75057 "regulatory protein [Enterobacteria phage P22]" 83.78 83 100.00 100.00 7.73e-12 GB AAM81380 "Mnt protein [Salmonella phage P22-pbi]" 83.78 83 100.00 100.00 7.73e-12 GB ADM32399 "Mnt [Enterobacteria phage Phi75]" 83.78 83 100.00 100.00 7.73e-12 GB ADW81950 "Mnt [Enterobacteria phage Phi20]" 83.78 83 100.00 100.00 7.73e-12 GB AKJ74157 "hypothetical protein SP34_3 [Salmonella phage 34]" 81.08 113 100.00 100.00 1.25e-10 REF NP_059641 "Mnt [Enterobacteria phage P22]" 83.78 83 100.00 100.00 7.73e-12 REF WP_015975190 "Mnt [Salmonella enterica]" 83.78 83 100.00 100.00 7.73e-12 SP P03049 "RecName: Full=Regulatory protein mnt" 83.78 83 100.00 100.00 7.73e-12 TPG DAA00978 "TPA_inf: transcriptional repressor [Enterobacteria phage P22]" 83.78 83 100.00 100.00 7.73e-12 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Mnt-C 'Bacteriophage P22' 10754 Viruses . Bacteriophage P22 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 $Mnt-C 'recombinant technology' E.coli Escherichia coli X90 pTM203-st6 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_15N_labelled _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Mnt-C 3.0 mM '[U-95% 15N]' stop_ save_ save_13C_15N_labelled _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Mnt-C 3.0 mM '[U-95% 13C; U-95% 15N]' stop_ save_ save_10%_13C_labelled _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Mnt-C 3.0 mM '[U-10% 13C]' stop_ save_ save_unlabelled_labelled_mixture _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Mnt-C 3.0 mM '[50/50 U-95% 13C; U-95% 15N / unlabelled]' stop_ save_ ############################ # Computer software used # ############################ save_Regine _Saveframe_category software _Name Regine _Version . loop_ _Task bookkeeping stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMXT _Field_strength 600 _Details . save_ save_NMR_spectrometer2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Unity-Plus _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_(1H,15N)-HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D (1H,15N)-HSQC' _Sample_label . save_ save_2D_(1H,1H)_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D (1H,1H) NOESY' _Sample_label . save_ save_3D_TOCSY_(15N,1H)_HSQC_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TOCSY (15N,1H) HSQC' _Sample_label . save_ save_3D_NOESY_(15N,1H)_HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NOESY (15N,1H) HSQC' _Sample_label . save_ save_3D_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label . save_ save_3D_HNCA_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label . save_ save_3D_HN(CO)CA_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label . save_ save_3D_HNHA_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHA' _Sample_label . save_ save_3D_HCACO_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCACO' _Sample_label . save_ save_3D_TOCSY_(13C,1H)_HSQC_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TOCSY (13C,1H) HSQC' _Sample_label . save_ save_3D_HNHB_11 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHB' _Sample_label . save_ save_3D_H(C)CH_DISPSY_12 _Saveframe_category NMR_applied_experiment _Experiment_name '3D H(C)CH DISPSY' _Sample_label . save_ save_3D_HCC(H)_DISPSY_13 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCC(H) DISPSY' _Sample_label . save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.20 0.02 M pH 5.2 0.1 n/a temperature 298 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . 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_resonance_set_A _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $15N_labelled $13C_15N_labelled $10%_13C_labelled $unlabelled_labelled_mixture stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Mnt-C subunit A' _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 ARG CA C 53.4 . . 2 . 1 ARG HA H 4.13 . . 3 . 1 ARG CB C 29.4 . . 4 . 1 ARG HB2 H 1.94 . . 5 . 1 ARG HB3 H 1.94 . . 6 . 1 ARG CG C 24.5 . . 7 . 1 ARG HG2 H 1.71 . . 8 . 1 ARG HG3 H 1.71 . . 9 . 1 ARG CD C 41.8 . . 10 . 1 ARG HD2 H 3.18 . . 11 . 1 ARG HD3 H 3.18 . . 12 . 1 ARG NE N 84.9 . . 13 . 1 ARG HE H 7.51 . . 14 . 2 ASN N N 122.1 . . 15 . 2 ASN H H 8.60 . . 16 . 2 ASN C C 173.0 . . 17 . 2 ASN CA C 50.8 . . 18 . 2 ASN HA H 4.83 . . 19 . 2 ASN CB C 37.1 . . 20 . 2 ASN HB2 H 2.94 . . 21 . 2 ASN HB3 H 3.03 . . 22 . 2 ASN ND2 N 113.7 . . 23 . 2 ASN HD21 H 7.65 . . 24 . 2 ASN HD22 H 6.92 . . 25 . 3 ASP N N 122.1 . . 26 . 3 ASP H H 8.58 . . 27 . 3 ASP C C 173.0 . . 28 . 3 ASP CA C 54.7 . . 29 . 3 ASP HA H 4.41 . . 30 . 3 ASP CB C 38.9 . . 31 . 3 ASP HB2 H 2.65 . . 32 . 3 ASP HB3 H 2.65 . . 33 . 4 ALA N N 123.3 . . 34 . 4 ALA H H 8.24 . . 35 . 4 ALA C C 175.1 . . 36 . 4 ALA CA C 53.1 . . 37 . 4 ALA HA H 3.83 . . 38 . 4 ALA CB C 16.9 . . 39 . 4 ALA HB H 1.32 . . 40 . 5 GLU N N 117.7 . . 41 . 5 GLU H H 8.11 . . 42 . 5 GLU C C 177.2 . . 43 . 5 GLU CA C 57.7 . . 44 . 5 GLU HA H 3.88 . . 45 . 5 GLU CB C 27.9 . . 46 . 5 GLU HB2 H 2.18 . . 47 . 5 GLU HB3 H 2.18 . . 48 . 5 GLU CG C 35.4 . . 49 . 5 GLU HG2 H 2.31 . . 50 . 5 GLU HG3 H 2.47 . . 51 . 6 ARG N N 120.8 . . 52 . 6 ARG H H 8.05 . . 53 . 6 ARG C C 176.3 . . 54 . 6 ARG CA C 57.5 . . 55 . 6 ARG HA H 4.12 . . 56 . 6 ARG CB C 28.3 . . 57 . 6 ARG HB2 H 1.97 . . 58 . 6 ARG HB3 H 1.87 . . 59 . 6 ARG CG C 25.4 . . 60 . 6 ARG HG2 H 1.75 . . 61 . 6 ARG HG3 H 1.59 . . 62 . 6 ARG CD C 41.5 . . 63 . 6 ARG HD2 H 3.28 . . 64 . 6 ARG HD3 H 3.20 . . 65 . 6 ARG NE N 83.8 . . 66 . 6 ARG HE H 7.39 . . 67 . 7 LEU N N 121.3 . . 68 . 7 LEU H H 8.15 . . 69 . 7 LEU C C 176.8 . . 70 . 7 LEU CA C 55.8 . . 71 . 7 LEU HA H 4.14 . . 72 . 7 LEU CB C 39.7 . . 73 . 7 LEU HB2 H 1.54 . . 74 . 7 LEU HB3 H 1.54 . . 75 . 7 LEU CG C 25.1 . . 76 . 7 LEU HG H 1.57 . . 77 . 7 LEU CD1 C 22.3 . . 78 . 7 LEU CD2 C 22.3 . . 79 . 7 LEU HD1 H 0.73 . . 80 . 7 LEU HD2 H 0.64 . . 81 . 8 ALA N N 120.9 . . 82 . 8 ALA H H 8.39 . . 83 . 8 ALA C C 176.9 . . 84 . 8 ALA CA C 52.7 . . 85 . 8 ALA HA H 4.33 . . 86 . 8 ALA CB C 17.2 . . 87 . 8 ALA HB H 1.47 . . 88 . 9 ASP N N 122.4 . . 89 . 9 ASP H H 8.81 . . 90 . 9 ASP C C 179.2 . . 91 . 9 ASP CA C 56.0 . . 92 . 9 ASP HA H 4.28 . . 93 . 9 ASP CB C 40.0 . . 94 . 9 ASP HB2 H 3.02 . . 95 . 9 ASP HB3 H 2.96 . . 96 . 10 GLU N N 120.1 . . 97 . 10 GLU H H 8.45 . . 98 . 10 GLU C C 175.6 . . 99 . 10 GLU CA C 57.6 . . 100 . 10 GLU HA H 3.99 . . 101 . 10 GLU CB C 27.8 . . 102 . 10 GLU HB2 H 2.30 . . 103 . 10 GLU HB3 H 2.14 . . 104 . 10 GLU CG C 34.0 . . 105 . 10 GLU HG2 H 2.57 . . 106 . 10 GLU HG3 H 2.30 . . 107 . 11 GLN N N 117.6 . . 108 . 11 GLN H H 8.92 . . 109 . 11 GLN C C 178.3 . . 110 . 11 GLN CA C 56.7 . . 111 . 11 GLN HA H 4.16 . . 112 . 11 GLN CB C 34.1 . . 113 . 11 GLN HB2 H 2.25 . . 114 . 11 GLN HB3 H 2.02 . . 115 . 11 GLN CG C 32.8 . . 116 . 11 GLN HG2 H 2.50 . . 117 . 11 GLN HG3 H 2.68 . . 118 . 11 GLN NE2 N 111.5 . . 119 . 11 GLN HE21 H 6.62 . . 120 . 11 GLN HE22 H 7.44 . . 121 . 12 SER N N 115.1 . . 122 . 12 SER H H 8.41 . . 123 . 12 SER C C 177.5 . . 124 . 12 SER CA C 60.5 . . 125 . 12 SER HA H 4.06 . . 126 . 12 SER HB2 H 4.46 . . 127 . 12 SER HB3 H 4.11 . . 128 . 12 SER HG H 5.64 . . 129 . 13 GLU N N 126.3 . . 130 . 13 GLU H H 8.21 . . 131 . 13 GLU C C 174.6 . . 132 . 13 GLU CA C 56.6 . . 133 . 13 GLU HA H 4.13 . . 134 . 13 GLU CB C 27.9 . . 135 . 13 GLU HB2 H 2.11 . . 136 . 13 GLU HB3 H 2.10 . . 137 . 13 GLU CG C 32.7 . . 138 . 13 GLU HG2 H 2.29 . . 139 . 13 GLU HG3 H 2.40 . . 140 . 14 LEU N N 120.0 . . 141 . 14 LEU H H 7.36 . . 142 . 14 LEU C C 176.3 . . 143 . 14 LEU CA C 56.2 . . 144 . 14 LEU HA H 4.16 . . 145 . 14 LEU CB C 39.5 . . 146 . 14 LEU HB2 H 2.03 . . 147 . 14 LEU HB3 H 1.69 . . 148 . 14 LEU CG C 25.0 . . 149 . 14 LEU HG H 1.88 . . 150 . 14 LEU CD1 C 23.3 . . 151 . 14 LEU CD2 C 21.6 . . 152 . 14 LEU HD1 H 0.99 . . 153 . 14 LEU HD2 H 0.92 . . 154 . 15 VAL N N 119.5 . . 155 . 15 VAL H H 7.27 . . 156 . 15 VAL C C 178.4 . . 157 . 15 VAL CA C 64.5 . . 158 . 15 VAL HA H 3.67 . . 159 . 15 VAL CB C 29.6 . . 160 . 15 VAL HB H 2.12 . . 161 . 15 VAL CG1 C 19.9 . . 162 . 15 VAL CG2 C 21.0 . . 163 . 15 VAL HG1 H 0.89 . . 164 . 15 VAL HG2 H 0.99 . . 165 . 16 LYS N N 121.5 . . 166 . 16 LYS H H 8.41 . . 167 . 16 LYS C C 175.1 . . 168 . 16 LYS CA C 58.5 . . 169 . 16 LYS HA H 3.72 . . 170 . 16 LYS CB C 30.7 . . 171 . 16 LYS HB2 H 1.82 . . 172 . 16 LYS HB3 H 2.23 . . 173 . 16 LYS CG C 23.1 . . 174 . 16 LYS HG2 H 1.23 . . 175 . 16 LYS HG3 H 1.40 . . 176 . 16 LYS CD C 27.6 . . 177 . 16 LYS HD2 H 1.61 . . 178 . 16 LYS HD3 H 1.61 . . 179 . 16 LYS CE C 41.0 . . 180 . 16 LYS HE2 H 2.87 . . 181 . 16 LYS HE3 H 3.04 . . 182 . 17 LYS N N 118.8 . . 183 . 17 LYS H H 8.12 . . 184 . 17 LYS C C 175.7 . . 185 . 17 LYS CA C 57.6 . . 186 . 17 LYS HA H 4.14 . . 187 . 17 LYS CB C 30.7 . . 188 . 17 LYS HB2 H 1.98 . . 189 . 17 LYS HB3 H 1.98 . . 190 . 17 LYS CG C 23.4 . . 191 . 17 LYS HG2 H 1.67 . . 192 . 17 LYS HG3 H 1.48 . . 193 . 17 LYS CD C 27.2 . . 194 . 17 LYS HD2 H 1.81 . . 195 . 17 LYS HD3 H 1.68 . . 196 . 17 LYS CE C 40.6 . . 197 . 18 MET N N 118.6 . . 198 . 18 MET H H 7.55 . . 199 . 18 MET C C 175.7 . . 200 . 18 MET CA C 57.0 . . 201 . 18 MET HA H 4.28 . . 202 . 18 MET CB C 31.3 . . 203 . 18 MET HB2 H 2.27 . . 204 . 18 MET HB3 H 2.29 . . 205 . 18 MET CG C 29.8 . . 206 . 18 MET HG2 H 2.48 . . 207 . 18 MET HG3 H 2.80 . . 208 . 18 MET CE C 15.1 . . 209 . 18 MET HE H 2.06 . . 210 . 19 VAL N N 121.1 . . 211 . 19 VAL H H 8.69 . . 212 . 19 VAL C C 177.8 . . 213 . 19 VAL CA C 65.2 . . 214 . 19 VAL HA H 3.43 . . 215 . 19 VAL CB C 29.7 . . 216 . 19 VAL HB H 2.14 . . 217 . 19 VAL CG1 C 19.8 . . 218 . 19 VAL CG2 C 22.1 . . 219 . 19 VAL HG1 H 0.84 . . 220 . 19 VAL HG2 H 1.00 . . 221 . 20 PHE N N 123.0 . . 222 . 20 PHE H H 9.48 . . 223 . 20 PHE C C 174.6 . . 224 . 20 PHE CA C 60.1 . . 225 . 20 PHE HA H 4.03 . . 226 . 20 PHE CB C 37.3 . . 227 . 20 PHE HB2 H 3.21 . . 228 . 20 PHE HB3 H 3.43 . . 229 . 20 PHE HD1 H 7.20 . . 230 . 20 PHE HE1 H 7.45 . . 231 . 20 PHE HZ H 7.33 . . 232 . 21 ASP N N 118.6 . . 233 . 21 ASP H H 8.53 . . 234 . 21 ASP C C 174.3 . . 235 . 21 ASP CA C 55.5 . . 236 . 21 ASP HA H 4.02 . . 237 . 21 ASP CB C 38.1 . . 238 . 21 ASP HB2 H 2.79 . . 239 . 21 ASP HB3 H 2.64 . . 240 . 22 THR N N 116.3 . . 241 . 22 THR H H 7.60 . . 242 . 22 THR C C 177.0 . . 243 . 22 THR CA C 64.7 . . 244 . 22 THR HA H 3.91 . . 245 . 22 THR CB C 67.0 . . 246 . 22 THR HB H 4.12 . . 247 . 22 THR CG2 C 19.4 . . 248 . 22 THR HG2 H 1.17 . . 249 . 23 LEU N N 121.7 . . 250 . 23 LEU H H 8.79 . . 251 . 23 LEU C C 174.6 . . 252 . 23 LEU CA C 55.3 . . 253 . 23 LEU HA H 3.50 . . 254 . 23 LEU CB C 38.5 . . 255 . 23 LEU HB2 H 1.61 . . 256 . 23 LEU HB3 H 1.61 . . 257 . 23 LEU CG C 24.5 . . 258 . 23 LEU HG H 1.86 . . 259 . 23 LEU CD1 C 24.1 . . 260 . 23 LEU CD2 C 20.6 . . 261 . 23 LEU HD1 H 0.91 . . 262 . 23 LEU HD2 H 0.63 . . 263 . 24 LYS N N 120.2 . . 264 . 24 LYS H H 8.68 . . 265 . 24 LYS C C 175.3 . . 266 . 24 LYS CA C 58.1 . . 267 . 24 LYS HA H 3.50 . . 268 . 24 LYS CB C 28.9 . . 269 . 24 LYS HB2 H 1.14 . . 270 . 24 LYS HB3 H 1.25 . . 271 . 24 LYS CG C 22.8 . . 272 . 24 LYS HG2 H 1.03 . . 273 . 24 LYS HG3 H 1.23 . . 274 . 24 LYS CD C 27.9 . . 275 . 24 LYS HD2 H 1.30 . . 276 . 24 LYS HD3 H 1.47 . . 277 . 24 LYS CE C 40.0 . . 278 . 24 LYS HE2 H 2.82 . . 279 . 24 LYS HE3 H 2.76 . . 280 . 25 ASP N N 117.4 . . 281 . 25 ASP H H 6.74 . . 282 . 25 ASP C C 175.5 . . 283 . 25 ASP CA C 54.8 . . 284 . 25 ASP HA H 4.37 . . 285 . 25 ASP CB C 39.4 . . 286 . 25 ASP HB2 H 2.61 . . 287 . 25 ASP HB3 H 2.64 . . 288 . 26 LEU N N 120.5 . . 289 . 26 LEU H H 7.53 . . 290 . 26 LEU C C 175.7 . . 291 . 26 LEU CA C 55.5 . . 292 . 26 LEU HA H 4.07 . . 293 . 26 LEU CB C 41.0 . . 294 . 26 LEU HB2 H 1.42 . . 295 . 26 LEU HB3 H 1.49 . . 296 . 26 LEU CG C 25.1 . . 297 . 26 LEU HG H 1.52 . . 298 . 26 LEU CD1 C 21.9 . . 299 . 26 LEU CD2 C 23.6 . . 300 . 26 LEU HD1 H 0.84 . . 301 . 26 LEU HD2 H 0.73 . . 302 . 27 TYR N N 117.9 . . 303 . 27 TYR H H 8.90 . . 304 . 27 TYR C C 177.8 . . 305 . 27 TYR CA C 54.4 . . 306 . 27 TYR HA H 4.55 . . 307 . 27 TYR HB2 H 2.96 . . 308 . 27 TYR HB3 H 3.00 . . 309 . 27 TYR HD1 H 6.75 . . 310 . 27 TYR HE1 H 6.44 . . 311 . 27 TYR HH H 10.43 . . 312 . 28 LYS N N 122.0 . . 313 . 28 LYS H H 8.02 . . 314 . 28 LYS C C 176.6 . . 315 . 28 LYS CA C 57.0 . . 316 . 28 LYS HA H 4.09 . . 317 . 28 LYS CB C 30.7 . . 318 . 28 LYS HB2 H 1.92 . . 319 . 28 LYS HB3 H 1.92 . . 320 . 28 LYS CG C 23.7 . . 321 . 28 LYS HG2 H 1.57 . . 322 . 28 LYS HG3 H 1.46 . . 323 . 28 LYS CD C 27.8 . . 324 . 28 LYS HD2 H 1.68 . . 325 . 28 LYS HD3 H 1.68 . . 326 . 28 LYS CE C 40.2 . . 327 . 28 LYS HE2 H 2.97 . . 328 . 28 LYS HE3 H 2.97 . . 329 . 29 LYS N N 120.1 . . 330 . 29 LYS H H 7.88 . . 331 . 29 LYS C C 176.1 . . 332 . 29 LYS CA C 56.3 . . 333 . 29 LYS HA H 4.19 . . 334 . 29 LYS CB C 30.8 . . 335 . 29 LYS HB2 H 1.96 . . 336 . 29 LYS HB3 H 1.96 . . 337 . 29 LYS CG C 23.4 . . 338 . 29 LYS HG2 H 1.48 . . 339 . 29 LYS HG3 H 1.60 . . 340 . 29 LYS CD C 27.6 . . 341 . 29 LYS HD2 H 1.71 . . 342 . 29 LYS HD3 H 1.67 . . 343 . 29 LYS CE C 40.4 . . 344 . 29 LYS HE2 H 2.97 . . 345 . 29 LYS HE3 H 2.97 . . 346 . 30 THR N N 113.3 . . 347 . 30 THR H H 7.78 . . 348 . 30 THR C C 176.0 . . 349 . 30 THR CA C 61.9 . . 350 . 30 THR HA H 4.23 . . 351 . 30 THR CB C 67.4 . . 352 . 30 THR HB H 4.11 . . 353 . 30 THR CG2 C 20.0 . . 354 . 30 THR HG2 H 1.11 . . 355 . 31 THR N N 113.7 . . 356 . 31 THR H H 7.69 . . 357 . 31 THR C C 173.0 . . 358 . 31 THR CA C 60.2 . . 359 . 31 THR HA H 4.29 . . 360 . 31 THR CB C 67.7 . . 361 . 31 THR HB H 4.23 . . 362 . 31 THR CG2 C 20.1 . . 363 . 31 THR HG2 H 1.18 . . stop_ save_ save_resonance_set_B _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $15N_labelled $13C_15N_labelled $10%_13C_labelled $unlabelled_labelled_mixture stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Mnt-C subunit B' _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 ARG CA C 53.4 . . 2 . 1 ARG HA H 4.13 . . 3 . 1 ARG CB C 29.4 . . 4 . 1 ARG HB2 H 1.94 . . 5 . 1 ARG HB3 H 1.94 . . 6 . 1 ARG CG C 24.5 . . 7 . 1 ARG HG2 H 1.72 . . 8 . 1 ARG HG3 H 1.72 . . 9 . 1 ARG CD C 41.8 . . 10 . 1 ARG HD2 H 3.19 . . 11 . 1 ARG HD3 H 3.19 . . 12 . 1 ARG NE N 84.9 . . 13 . 1 ARG HE H 7.53 . . 14 . 2 ASN N N 122.1 . . 15 . 2 ASN H H 8.59 . . 16 . 2 ASN C C 173.0 . . 17 . 2 ASN CA C 50.8 . . 18 . 2 ASN HA H 4.83 . . 19 . 2 ASN CB C 37.1 . . 20 . 2 ASN HB2 H 2.93 . . 21 . 2 ASN HB3 H 3.03 . . 22 . 2 ASN HD21 H 7.70 . . 23 . 2 ASN HD22 H 6.90 . . 24 . 2 ASN ND2 N 113.4 . . 25 . 3 ASP N N 122.1 . . 26 . 3 ASP H H 8.60 . . 27 . 3 ASP C C 173.0 . . 28 . 3 ASP CA C 55.1 . . 29 . 3 ASP HA H 4.42 . . 30 . 3 ASP CB C 38.9 . . 31 . 3 ASP HB2 H 2.62 . . 32 . 3 ASP HB3 H 2.62 . . 33 . 4 ALA N N 122.4 . . 34 . 4 ALA H H 8.33 . . 35 . 4 ALA C C 175.0 . . 36 . 4 ALA CA C 53.7 . . 37 . 4 ALA HA H 3.97 . . 38 . 4 ALA CB C 17.0 . . 39 . 4 ALA HB H 1.44 . . 40 . 5 GLU N N 116.6 . . 41 . 5 GLU H H 8.13 . . 42 . 5 GLU C C 176.9 . . 43 . 5 GLU CA C 58.0 . . 44 . 5 GLU HA H 3.86 . . 45 . 5 GLU CB C 27.9 . . 46 . 5 GLU HB2 H 2.18 . . 47 . 5 GLU HB3 H 2.18 . . 48 . 5 GLU CG C 35.7 . . 49 . 5 GLU HG2 H 2.36 . . 50 . 5 GLU HG3 H 2.45 . . 51 . 6 ARG N N 121.0 . . 52 . 6 ARG H H 8.15 . . 53 . 6 ARG C C 176.1 . . 54 . 6 ARG CA C 57.7 . . 55 . 6 ARG HA H 4.13 . . 56 . 6 ARG CB C 28.3 . . 57 . 6 ARG HB2 H 2.02 . . 58 . 6 ARG HB3 H 1.85 . . 59 . 6 ARG CG C 25.4 . . 60 . 6 ARG HG2 H 1.74 . . 61 . 6 ARG HG3 H 1.59 . . 62 . 6 ARG CD C 41.4 . . 63 . 6 ARG HD2 H 3.31 . . 64 . 6 ARG HD3 H 3.19 . . 65 . 6 ARG NE N 107.7 . . 66 . 6 ARG HE H 7.41 . . 67 . 7 LEU N N 120.7 . . 68 . 7 LEU H H 8.44 . . 69 . 7 LEU C C 176.7 . . 70 . 7 LEU CA C 55.8 . . 71 . 7 LEU HA H 4.11 . . 72 . 7 LEU CB C 41.3 . . 73 . 7 LEU HB2 H 1.85 . . 74 . 7 LEU HB3 H 1.38 . . 75 . 7 LEU CG C 25.4 . . 76 . 7 LEU HG H 1.62 . . 77 . 7 LEU CD1 C 22.9 . . 78 . 7 LEU CD2 C 21.7 . . 79 . 7 LEU HD1 H 0.56 . . 80 . 7 LEU HD2 H 0.73 . . 81 . 8 ALA N N 120.1 . . 82 . 8 ALA H H 8.19 . . 83 . 8 ALA C C 176.9 . . 84 . 8 ALA CA C 53.3 . . 85 . 8 ALA HA H 4.11 . . 86 . 8 ALA CB C 17.4 . . 87 . 8 ALA HB H 1.39 . . 88 . 9 ASP N N 121.5 . . 89 . 9 ASP H H 8.92 . . 90 . 9 ASP C C 178.6 . . 91 . 9 ASP CA C 55.9 . . 92 . 9 ASP HA H 4.40 . . 93 . 9 ASP CB C 40.0 . . 94 . 9 ASP HB2 H 3.03 . . 95 . 9 ASP HB3 H 3.03 . . 96 . 10 GLU N N 119.9 . . 97 . 10 GLU H H 8.63 . . 98 . 10 GLU C C 176.1 . . 99 . 10 GLU CA C 57.5 . . 100 . 10 GLU HA H 4.01 . . 101 . 10 GLU CB C 27.8 . . 102 . 10 GLU HB2 H 2.28 . . 103 . 10 GLU HB3 H 2.14 . . 104 . 10 GLU CG C 33.9 . . 105 . 10 GLU HG2 H 2.40 . . 106 . 10 GLU HG3 H 2.58 . . 107 . 11 GLN N N 119.3 . . 108 . 11 GLN H H 8.73 . . 109 . 11 GLN C C 178.4 . . 110 . 11 GLN CA C 57.6 . . 111 . 11 GLN HA H 4.09 . . 112 . 11 GLN HB2 H 2.16 . . 113 . 11 GLN HB3 H 1.99 . . 114 . 11 GLN CG C 33.2 . . 115 . 11 GLN HG2 H 2.65 . . 116 . 11 GLN HG3 H 3.01 . . 117 . 11 GLN NE2 N 107.6 . . 118 . 11 GLN HE21 H 7.41 . . 119 . 11 GLN HE22 H 6.91 . . 120 . 12 SER N N 116.1 . . 121 . 12 SER H H 8.59 . . 122 . 12 SER C C 177.0 . . 123 . 12 SER CA C 60.7 . . 124 . 12 SER HA H 4.05 . . 125 . 12 SER HB2 H 4.47 . . 126 . 12 SER HB3 H 4.12 . . 127 . 12 SER HG H 5.56 . . 128 . 13 GLU N N 125.9 . . 129 . 13 GLU H H 8.09 . . 130 . 13 GLU C C 174.5 . . 131 . 13 GLU CA C 56.6 . . 132 . 13 GLU HA H 4.23 . . 133 . 13 GLU HB2 H 2.11 . . 134 . 13 GLU HB3 H 2.18 . . 135 . 13 GLU CG C 32.7 . . 136 . 13 GLU HG2 H 2.34 . . 137 . 13 GLU HG3 H 2.40 . . 138 . 14 LEU N N 121.9 . . 139 . 14 LEU H H 7.51 . . 140 . 14 LEU C C 176.6 . . 141 . 14 LEU CA C 56.4 . . 142 . 14 LEU HA H 4.18 . . 143 . 14 LEU CB C 39.6 . . 144 . 14 LEU HB2 H 2.09 . . 145 . 14 LEU HB3 H 1.72 . . 146 . 14 LEU CG C 25.1 . . 147 . 14 LEU HG H 1.92 . . 148 . 14 LEU CD1 C 23.8 . . 149 . 14 LEU CD2 C 21.7 . . 150 . 14 LEU HD1 H 1.02 . . 151 . 14 LEU HD2 H 0.93 . . 152 . 15 VAL N N 119.9 . . 153 . 15 VAL H H 7.76 . . 154 . 15 VAL C C 178.5 . . 155 . 15 VAL CA C 64.6 . . 156 . 15 VAL HA H 3.66 . . 157 . 15 VAL CB C 29.4 . . 158 . 15 VAL HB H 2.23 . . 159 . 15 VAL CG1 C 19.8 . . 160 . 15 VAL CG2 C 21.9 . . 161 . 15 VAL HG1 H 0.87 . . 162 . 15 VAL HG2 H 1.07 . . 163 . 16 LYS N N 121.4 . . 164 . 16 LYS H H 8.59 . . 165 . 16 LYS C C 174.7 . . 166 . 16 LYS CA C 58.5 . . 167 . 16 LYS HA H 3.72 . . 168 . 16 LYS CB C 30.7 . . 169 . 16 LYS HB2 H 1.87 . . 170 . 16 LYS HB3 H 2.26 . . 171 . 16 LYS CG C 23.1 . . 172 . 16 LYS HG2 H 1.35 . . 173 . 16 LYS HG3 H 1.35 . . 174 . 16 LYS CD C 27.6 . . 175 . 16 LYS HD2 H 1.62 . . 176 . 16 LYS HD3 H 1.62 . . 177 . 16 LYS CE C 40.9 . . 178 . 16 LYS HE2 H 2.85 . . 179 . 16 LYS HE3 H 2.90 . . 180 . 17 LYS N N 118.4 . . 181 . 17 LYS H H 7.94 . . 182 . 17 LYS C C 175.7 . . 183 . 17 LYS CA C 57.6 . . 184 . 17 LYS HA H 4.12 . . 185 . 17 LYS CB C 30.7 . . 186 . 17 LYS HB2 H 1.96 . . 187 . 17 LYS HB3 H 2.01 . . 188 . 17 LYS CG C 23.4 . . 189 . 17 LYS HG2 H 1.67 . . 190 . 17 LYS HG3 H 1.48 . . 191 . 17 LYS CD C 27.2 . . 192 . 17 LYS HD2 H 1.81 . . 193 . 17 LYS HD3 H 1.68 . . 194 . 17 LYS CE C 40.6 . . 195 . 17 LYS HE2 H 3.05 . . 196 . 17 LYS HE3 H 3.05 . . 197 . 18 MET N N 118.7 . . 198 . 18 MET H H 7.63 . . 199 . 18 MET C C 175.5 . . 200 . 18 MET CA C 56.9 . . 201 . 18 MET HA H 4.29 . . 202 . 18 MET CB C 32.0 . . 203 . 18 MET HB2 H 2.24 . . 204 . 18 MET HB3 H 2.38 . . 205 . 18 MET CG C 29.1 . . 206 . 18 MET HG2 H 2.67 . . 207 . 18 MET HG3 H 2.40 . . 208 . 18 MET CE C 15.1 . . 209 . 18 MET HE H 2.05 . . 210 . 19 VAL N N 122.8 . . 211 . 19 VAL H H 8.59 . . 212 . 19 VAL C C 177.2 . . 213 . 19 VAL CA C 63.4 . . 214 . 19 VAL HA H 4.21 . . 215 . 19 VAL CB C 30.6 . . 216 . 19 VAL HB H 2.12 . . 217 . 19 VAL CG1 C 19.8 . . 218 . 19 VAL CG2 C 21.7 . . 219 . 19 VAL HG1 H 1.02 . . 220 . 19 VAL HG2 H 1.17 . . 221 . 20 PHE N N 123.3 . . 222 . 20 PHE H H 9.45 . . 223 . 20 PHE C C 175.5 . . 224 . 20 PHE CA C 59.8 . . 225 . 20 PHE HA H 4.12 . . 226 . 20 PHE CB C 37.8 . . 227 . 20 PHE HB2 H 3.30 . . 228 . 20 PHE HB3 H 3.46 . . 229 . 20 PHE HD1 H 7.22 . . 230 . 20 PHE HE1 H 7.48 . . 231 . 20 PHE HZ H 7.35 . . 232 . 21 ASP N N 118.2 . . 233 . 21 ASP H H 8.63 . . 234 . 21 ASP C C 174.7 . . 235 . 21 ASP CA C 55.3 . . 236 . 21 ASP HA H 4.12 . . 237 . 21 ASP CB C 38.1 . . 238 . 21 ASP HB2 H 2.82 . . 239 . 21 ASP HB3 H 2.63 . . 240 . 22 THR N N 117.7 . . 241 . 22 THR H H 7.74 . . 242 . 22 THR C C 177.2 . . 243 . 22 THR CA C 64.9 . . 244 . 22 THR HA H 3.79 . . 245 . 22 THR CB C 66.4 . . 246 . 22 THR HB H 4.46 . . 247 . 22 THR CG2 C 19.9 . . 248 . 22 THR HG2 H 0.64 . . 249 . 23 LEU N N 122.1 . . 250 . 23 LEU H H 9.00 . . 251 . 23 LEU C C 174.1 . . 252 . 23 LEU CA C 55.9 . . 253 . 23 LEU HA H 3.70 . . 254 . 23 LEU CB C 40.3 . . 255 . 23 LEU HB2 H 2.00 . . 256 . 23 LEU HB3 H 2.00 . . 257 . 23 LEU CG C 25.2 . . 258 . 23 LEU HG H 2.13 . . 259 . 23 LEU CD1 C 26.8 . . 260 . 23 LEU CD2 C 21.1 . . 261 . 23 LEU HD1 H 1.14 . . 262 . 23 LEU HD2 H 0.89 . . 263 . 24 LYS N N 117.8 . . 264 . 24 LYS H H 8.20 . . 265 . 24 LYS C C 176.1 . . 266 . 24 LYS CA C 58.4 . . 267 . 24 LYS HA H 3.68 . . 268 . 24 LYS CB C 29.6 . . 269 . 24 LYS HB2 H 1.50 . . 270 . 24 LYS HB3 H 1.50 . . 271 . 24 LYS CG C 23.2 . . 272 . 24 LYS HG2 H 1.17 . . 273 . 24 LYS HG3 H 1.12 . . 274 . 24 LYS CD C 27.9 . . 275 . 24 LYS HD2 H 1.44 . . 276 . 24 LYS HD3 H 1.37 . . 277 . 24 LYS CE C 39.7 . . 278 . 24 LYS HE2 H 2.53 . . 279 . 24 LYS HE3 H 2.79 . . 280 . 25 ASP N N 118.7 . . 281 . 25 ASP H H 7.12 . . 282 . 25 ASP C C 176.4 . . 283 . 25 ASP CA C 55.0 . . 284 . 25 ASP HA H 4.42 . . 285 . 25 ASP CB C 39.1 . . 286 . 25 ASP HB2 H 2.68 . . 287 . 25 ASP HB3 H 2.74 . . 288 . 26 LEU N N 120.7 . . 289 . 26 LEU H H 8.31 . . 290 . 26 LEU C C 176.6 . . 291 . 26 LEU CA C 55.6 . . 292 . 26 LEU HA H 3.96 . . 293 . 26 LEU CB C 40.0 . . 294 . 26 LEU HB2 H 1.63 . . 295 . 26 LEU HB3 H 1.27 . . 296 . 26 LEU CG C 24.5 . . 297 . 26 LEU HG H 1.65 . . 298 . 26 LEU CD1 C 24.0 . . 299 . 26 LEU CD2 C 20.4 . . 300 . 26 LEU HD1 H 0.51 . . 301 . 26 LEU HD2 H 0.64 . . 302 . 27 TYR N N 118.3 . . 303 . 27 TYR H H 8.55 . . 304 . 27 TYR C C 178.3 . . 305 . 27 TYR CA C 57.0 . . 306 . 27 TYR HA H 4.53 . . 307 . 27 TYR HB2 H 3.15 . . 308 . 27 TYR HB3 H 2.94 . . 309 . 27 TYR HD1 H 6.99 . . 310 . 27 TYR HE1 H 6.64 . . 311 . 28 LYS N N 120.6 . . 312 . 28 LYS H H 7.64 . . 313 . 28 LYS C C 175.9 . . 314 . 28 LYS CA C 56.0 . . 315 . 28 LYS HA H 4.20 . . 316 . 28 LYS CB C 30.7 . . 317 . 28 LYS HB2 H 1.96 . . 318 . 28 LYS HB3 H 1.96 . . 319 . 28 LYS CG C 23.4 . . 320 . 28 LYS HG2 H 1.49 . . 321 . 28 LYS HG3 H 1.61 . . 322 . 28 LYS CD C 27.6 . . 323 . 28 LYS HD2 H 1.71 . . 324 . 28 LYS HD3 H 1.71 . . 325 . 28 LYS CE C 40.4 . . 326 . 28 LYS HE2 H 2.98 . . 327 . 28 LYS HE3 H 2.98 . . 328 . 29 LYS N N 120.6 . . 329 . 29 LYS H H 7.97 . . 330 . 29 LYS C C 175.3 . . 331 . 29 LYS CA C 55.2 . . 332 . 29 LYS HA H 4.27 . . 333 . 29 LYS CB C 30.9 . . 334 . 29 LYS HB2 H 1.88 . . 335 . 29 LYS HB3 H 1.90 . . 336 . 29 LYS CG C 23.3 . . 337 . 29 LYS HG2 H 1.47 . . 338 . 29 LYS HG3 H 1.55 . . 339 . 29 LYS CD C 27.4 . . 340 . 29 LYS HD2 H 1.66 . . 341 . 29 LYS HD3 H 1.67 . . 342 . 29 LYS CE C 40.0 . . 343 . 29 LYS HE2 H 2.93 . . 344 . 29 LYS HE3 H 2.93 . . 345 . 30 THR N N 114.4 . . 346 . 30 THR H H 7.97 . . 347 . 30 THR C C 175.2 . . 348 . 30 THR CA C 60.0 . . 349 . 30 THR HA H 4.39 . . 350 . 30 THR CB C 67.7 . . 351 . 30 THR HB H 4.24 . . 352 . 30 THR CG2 C 19.8 . . 353 . 30 THR HG2 H 1.19 . . 354 . 31 THR N N 116.7 . . 355 . 31 THR H H 7.97 . . 356 . 31 THR C C 172.6 . . 357 . 31 THR CA C 59.9 . . 358 . 31 THR HA H 4.27 . . 359 . 31 THR CB C 67.6 . . 360 . 31 THR HB H 4.12 . . 361 . 31 THR CG2 C 19.8 . . 362 . 31 THR HG2 H 1.9 . . stop_ save_