data_10012 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structure of actin-interacting domain of troponin ; _BMRB_accession_number 10012 _BMRB_flat_file_name bmr10012.str _Entry_type original _Submission_date 2005-11-18 _Accession_date 2005-11-18 _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 Murakami Kenji . . 2 Yumoto Fumiaki . . 3 Ohki Shin-ya . . 4 Yasunaga Takuo . . 5 Tanokura Masaru . . 6 Wakabayashi Takeyuki . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 308 "13C chemical shifts" 195 "15N chemical shifts" 49 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-06-01 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 9500 'Assigned chemical shift of actin-binding domain of troponin in Ca2+-bound state' stop_ _Original_release_date 2009-06-01 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structural Basis for Ca(2+)-regulated Muscle Relaxation at Interaction Sites of Troponin with Actin and Tropomyosin ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 16061251 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Murakami Kenji . . 2 Yumoto Fumiaki . . 3 Ohki Shin-ya . . 4 Yasunaga Takuo . . 5 Tanokura Masaru . . 6 Wakabayashi Takeyuki . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 352 _Journal_issue 1 _Journal_ASTM JMOBAK _Journal_ISSN 0022-2836 _Journal_CSD 0353 _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 178 _Page_last 201 _Year 2005 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'troponin complex' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Troponin I' $TnI stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state 'protein-protein complex' _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_TnI _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common TnI _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 52 _Mol_residue_sequence ; KVNMDLRANLKQVKKEDTEK EKDLRDVGDWRKNIEEKSGM EGRKKMFEAGES ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 131 LYS 2 132 VAL 3 133 ASN 4 134 MET 5 135 ASP 6 136 LEU 7 137 ARG 8 138 ALA 9 139 ASN 10 140 LEU 11 141 LYS 12 142 GLN 13 143 VAL 14 144 LYS 15 145 LYS 16 146 GLU 17 147 ASP 18 148 THR 19 149 GLU 20 150 LYS 21 151 GLU 22 152 LYS 23 153 ASP 24 154 LEU 25 155 ARG 26 156 ASP 27 157 VAL 28 158 GLY 29 159 ASP 30 160 TRP 31 161 ARG 32 162 LYS 33 163 ASN 34 164 ILE 35 165 GLU 36 166 GLU 37 167 LYS 38 168 SER 39 169 GLY 40 170 MET 41 171 GLU 42 172 GLY 43 173 ARG 44 174 LYS 45 175 LYS 46 176 MET 47 177 PHE 48 178 GLU 49 179 ALA 50 180 GLY 51 181 GLU 52 182 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-07 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 PDB 1VDI "Solution Structure Of Actin-Binding Domain Of Troponin In Ca2+-Free State" 100.00 52 100.00 100.00 3.30e-26 PDB 1VDJ "Solution Structure Of Actin-Binding Domain Of Troponin In Ca2+-Bound State" 100.00 52 100.00 100.00 3.30e-26 PDB 1YTZ "Crystal Structure Of Skeletal Muscle Troponin In The Ca2+- Activated State" 100.00 182 100.00 100.00 2.24e-26 EMBL CAA27447 "sTnI protein (aa 85-182), partial [Gallus gallus]" 100.00 98 100.00 100.00 2.89e-26 GB AAA61952 "troponin I [Gallus gallus]" 100.00 183 100.00 100.00 2.71e-26 GB AAB00122 "troponin I [Coturnix coturnix]" 100.00 183 100.00 100.00 2.71e-26 GB ACU12238 "troponin I, partial [Alectoris rufa]" 88.46 67 100.00 100.00 1.04e-21 GB ACU12239 "troponin I, partial [Alectoris chukar]" 88.46 67 100.00 100.00 1.04e-21 GB EMC88037 "Troponin I, fast skeletal muscle, partial [Columba livia]" 100.00 178 100.00 100.00 2.37e-26 REF NP_990748 "troponin I, fast skeletal muscle [Gallus gallus]" 100.00 183 100.00 100.00 2.71e-26 REF XP_002199061 "PREDICTED: troponin I, fast skeletal muscle [Taeniopygia guttata]" 100.00 183 98.08 98.08 2.68e-25 REF XP_003206335 "PREDICTED: troponin I, fast skeletal muscle [Meleagris gallopavo]" 100.00 183 100.00 100.00 2.69e-26 REF XP_003206336 "PREDICTED: troponin I, fast skeletal muscle [Meleagris gallopavo]" 100.00 183 100.00 100.00 2.69e-26 REF XP_005019798 "PREDICTED: troponin I, fast skeletal muscle [Anas platyrhynchos]" 100.00 183 98.08 98.08 2.51e-25 SP P68246 "RecName: Full=Troponin I, fast skeletal muscle; AltName: Full=Troponin I, fast-twitch isoform" 100.00 183 100.00 100.00 2.71e-26 SP P68247 "RecName: Full=Troponin I, fast skeletal muscle; AltName: Full=Troponin I, fast-twitch isoform" 100.00 183 100.00 100.00 2.71e-26 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $TnI chicken 9031 Eukaryota Metazoa Gallus gallus 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 $TnI 'recombinant technology' . Escherichia coli . pET3a stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'The troponin ternary complex at low Ca2+' loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $assembly . mM 0.8 1.2 '[U-13C; U-15N]' $assembly . mM 0.8 1.2 'natural abundance' $assembly . mM 0.8 1.2 'natural abundance' KCl 240 mM . . . NaHCO3 0.3 mM . . . MgCl2 3 mM . . . EGTA 0.2 mM . . . H2O 90 % . . . D2O 10 % . . . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details 'The troponin ternary complex at low Ca2+' loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $assembly . mM 0.8 1.2 '[U-13C; U-15N]' $assembly . mM 0.8 1.2 'natural abundance' $assembly . mM 0.8 1.2 'natural abundance' KCl 240 mM . . . NaHCO3 0.3 mM . . . MgCl2 3 mM . . . EGTA 0.2 mM . . . D2O 100 % . . . 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 processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_CYANA _Saveframe_category software _Name CYANA _Version . loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 750 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_HNCACB_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label $sample_1 save_ save_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label $sample_1 save_ save_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_1 save_ save_HN(CO)CA_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label $sample_1 save_ save_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_1 save_ save_H(CCO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name H(CCO)NH _Sample_label $sample_1 save_ save_C(CO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name C(CO)NH _Sample_label $sample_1 save_ save_HCCH-TOCSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label $sample_1 save_ save_2D_13C-NOESY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 13C-NOESY' _Sample_label $sample_1 save_ save_2D_aromatic_13C-edited_NOESY_10 _Saveframe_category NMR_applied_experiment _Experiment_name '2D aromatic 13C-edited NOESY' _Sample_label $sample_2 save_ save_3D_13C-edited_NOESY_11 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-edited NOESY' _Sample_label $sample_1 save_ save_3D_15N-edited_NOESY_12 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-edited NOESY' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7 . pH temperature 298 . 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 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 . indirect . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 . 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_chemical_shifts_woCa _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label HNCACB CBCA(CO)NH HNCA HN(CO)CA HNCO H(CCO)NH C(CO)NH HCCH-TOCSY '2D 13C-NOESY' '2D aromatic 13C-edited NOESY' '3D 13C-edited NOESY' '3D 15N-edited NOESY' stop_ loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'Troponin I' _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 1 132 2 VAL HA H 4.099 . 1 2 132 2 VAL HB H 2.185 . 1 3 133 3 ASN H H 8.514 . 1 4 133 3 ASN HA H 4.691 . 1 5 133 3 ASN HB2 H 2.644 . 1 6 133 3 ASN HB3 H 2.644 . 1 7 133 3 ASN C C 176.4 . 1 8 133 3 ASN CA C 61.7 . 1 9 133 3 ASN CB C 33.5 . 1 10 133 3 ASN N N 122.8 . 1 11 134 4 MET H H 8.518 . 1 12 134 4 MET HA H 4.461 . 1 13 134 4 MET HB2 H 2.03 . 1 14 134 4 MET HB3 H 2.03 . 1 15 134 4 MET HG2 H 2.458 . 1 16 134 4 MET HG3 H 2.458 . 1 17 134 4 MET N N 120.6 . 1 18 135 5 ASP HA H 4.622 . 1 19 135 5 ASP HB2 H 2.565 . 1 20 135 5 ASP HB3 H 2.565 . 1 21 135 5 ASP C C 176.4 . 1 22 135 5 ASP CA C 55.8 . 1 23 135 5 ASP CB C 41.1 . 1 24 136 6 LEU H H 8.404 . 1 25 136 6 LEU HA H 4.322 . 1 26 136 6 LEU HB2 H 1.668 . 1 27 136 6 LEU HB3 H 1.668 . 1 28 136 6 LEU HG H 1.424 . 1 29 136 6 LEU HD1 H 0.915 . 1 30 136 6 LEU HD2 H 0.915 . 1 31 136 6 LEU C C 178 . 1 32 136 6 LEU CA C 55.8 . 1 33 136 6 LEU CB C 41.3 . 1 34 136 6 LEU N N 119.5 . 1 35 137 7 ARG H H 8.205 . 1 36 137 7 ARG HA H 4.25 . 1 37 137 7 ARG HB2 H 1.884 . 1 38 137 7 ARG HB3 H 1.884 . 1 39 137 7 ARG HG2 H 1.687 . 1 40 137 7 ARG HG3 H 1.687 . 1 41 137 7 ARG HD2 H 3.239 . 1 42 137 7 ARG HD3 H 3.239 . 1 43 137 7 ARG C C 176.7 . 1 44 137 7 ARG CA C 56.83 . 1 45 137 7 ARG CB C 30.46 . 1 46 137 7 ARG CG C 27.33 . 1 47 137 7 ARG CD C 43.47 . 1 48 137 7 ARG N N 120 . 1 49 138 8 ALA H H 8.091 . 1 50 138 8 ALA HA H 4.244 . 1 51 138 8 ALA HB H 1.413 . 1 52 138 8 ALA C C 177.8 . 1 53 138 8 ALA CA C 53.24 . 1 54 138 8 ALA CB C 19.44 . 1 55 138 8 ALA N N 123.2 . 1 56 139 9 ASN H H 8.272 . 1 57 139 9 ASN HA H 4.696 . 1 58 139 9 ASN HB2 H 2.777 . 2 59 139 9 ASN HB3 H 2.869 . 2 60 139 9 ASN C C 175.4 . 1 61 139 9 ASN CA C 53.56 . 1 62 139 9 ASN CB C 38.8 . 1 63 139 9 ASN N N 116.9 . 1 64 140 10 LEU H H 8.058 . 1 65 140 10 LEU HA H 4.294 . 1 66 140 10 LEU HB2 H 1.618 . 2 67 140 10 LEU HB3 H 1.682 . 2 68 140 10 LEU HD1 H 0.89 . 1 69 140 10 LEU HD2 H 0.89 . 1 70 140 10 LEU C C 177.4 . 1 71 140 10 LEU CA C 55.65 . 1 72 140 10 LEU CB C 42.29 . 1 73 140 10 LEU CG C 29.24 . 1 74 140 10 LEU N N 121.8 . 1 75 141 11 LYS H H 8.178 . 1 76 141 11 LYS HA H 4.298 . 1 77 141 11 LYS HB2 H 1.772 . 1 78 141 11 LYS HB3 H 1.772 . 1 79 141 11 LYS HG2 H 1.453 . 1 80 141 11 LYS HG3 H 1.453 . 1 81 141 11 LYS HD2 H 1.697 . 1 82 141 11 LYS HD3 H 1.697 . 1 83 141 11 LYS HE2 H 3.015 . 1 84 141 11 LYS HE3 H 3.015 . 1 85 141 11 LYS C C 176.5 . 1 86 141 11 LYS CA C 56.54 . 1 87 141 11 LYS CB C 32.99 . 1 88 141 11 LYS N N 121.1 . 1 89 142 12 GLN H H 8.269 . 1 90 142 12 GLN HA H 4.363 . 1 91 142 12 GLN HB2 H 2.016 . 1 92 142 12 GLN HB3 H 2.016 . 1 93 142 12 GLN HG2 H 2.358 . 2 94 142 12 GLN HG3 H 2.377 . 2 95 142 12 GLN C C 175.9 . 1 96 142 12 GLN CA C 55.82 . 1 97 142 12 GLN CB C 29.7 . 1 98 142 12 GLN CG C 33.81 . 1 99 142 12 GLN N N 121.3 . 1 100 143 13 VAL H H 8.197 . 1 101 143 13 VAL HA H 4.096 . 1 102 143 13 VAL HB H 2.072 . 1 103 143 13 VAL HG1 H 0.931 . 2 104 143 13 VAL HG2 H 0.95 . 2 105 143 13 VAL C C 176 . 1 106 143 13 VAL CA C 62.36 . 1 107 143 13 VAL CB C 32.98 . 1 108 143 13 VAL CG1 C 21.05 . 2 109 143 13 VAL N N 122.1 . 1 110 144 14 LYS H H 8.461 . 1 111 144 14 LYS HA H 4.364 . 1 112 144 14 LYS HB2 H 1.788 . 1 113 144 14 LYS HB3 H 1.788 . 1 114 144 14 LYS HG2 H 1.437 . 1 115 144 14 LYS HG3 H 1.437 . 1 116 144 14 LYS HD2 H 1.73 . 1 117 144 14 LYS HD3 H 1.73 . 1 118 144 14 LYS HE2 H 3.019 . 1 119 144 14 LYS HE3 H 3.019 . 1 120 144 14 LYS C C 176.4 . 1 121 144 14 LYS CA C 56.16 . 1 122 144 14 LYS CB C 33.33 . 1 123 144 14 LYS CG C 24.75 . 1 124 144 14 LYS CD C 29.2 . 1 125 144 14 LYS CE C 42.2 . 1 126 144 14 LYS N N 125.8 . 1 127 145 15 LYS H H 8.486 . 1 128 145 15 LYS HA H 4.333 . 1 129 145 15 LYS HB2 H 1.752 . 1 130 145 15 LYS HB3 H 1.752 . 1 131 145 15 LYS HG2 H 1.456 . 1 132 145 15 LYS HG3 H 1.456 . 1 133 145 15 LYS HD2 H 1.681 . 1 134 145 15 LYS HD3 H 1.681 . 1 135 145 15 LYS HE2 H 3.002 . 1 136 145 15 LYS HE3 H 3.002 . 1 137 145 15 LYS C C 176.7 . 1 138 145 15 LYS CA C 56.66 . 1 139 145 15 LYS CB C 33.23 . 1 140 145 15 LYS CG C 24.78 . 1 141 145 15 LYS CD C 29.26 . 1 142 145 15 LYS CE C 42.15 . 1 143 145 15 LYS N N 124.4 . 1 144 146 16 GLU H H 8.668 . 1 145 146 16 GLU HA H 4.327 . 1 146 146 16 GLU HB2 H 1.984 . 1 147 146 16 GLU HB3 H 1.984 . 1 148 146 16 GLU HG2 H 2.289 . 1 149 146 16 GLU HG3 H 2.289 . 1 150 146 16 GLU C C 176.4 . 1 151 146 16 GLU CA C 56.76 . 1 152 146 16 GLU CB C 30.48 . 1 153 146 16 GLU CG C 36.29 . 1 154 146 16 GLU N N 122.2 . 1 155 147 17 ASP H H 8.456 . 1 156 147 17 ASP HA H 4.675 . 1 157 147 17 ASP HB2 H 2.652 . 2 158 147 17 ASP HB3 H 2.77 . 2 159 147 17 ASP C C 176.8 . 1 160 147 17 ASP CA C 54.73 . 1 161 147 17 ASP CB C 41.25 . 1 162 147 17 ASP N N 121.8 . 1 163 148 18 THR H H 8.111 . 1 164 148 18 THR HA H 4.303 . 1 165 148 18 THR HB H 4.212 . 1 166 148 18 THR HG1 H 4.574 . 1 167 148 18 THR HG2 H 1.238 . 1 168 148 18 THR C C 175.1 . 1 169 148 18 THR CA C 62.38 . 1 170 148 18 THR CB C 69.6 . 1 171 148 18 THR CG2 C 21.97 . 1 172 148 18 THR N N 113.9 . 1 173 149 19 GLU H H 8.406 . 1 174 149 19 GLU HA H 4.288 . 1 175 149 19 GLU HB2 H 2.013 . 1 176 149 19 GLU HB3 H 2.013 . 1 177 149 19 GLU HG2 H 2.28 . 1 178 149 19 GLU HG3 H 2.28 . 1 179 149 19 GLU C C 176.8 . 1 180 149 19 GLU CA C 57.05 . 1 181 149 19 GLU CB C 30.2 . 1 182 149 19 GLU CG C 36.42 . 1 183 149 19 GLU N N 122.8 . 1 184 150 20 LYS H H 8.182 . 1 185 150 20 LYS HA H 4.275 . 1 186 150 20 LYS HB2 H 1.818 . 1 187 150 20 LYS HB3 H 1.818 . 1 188 150 20 LYS HG2 H 1.469 . 1 189 150 20 LYS HG3 H 1.469 . 1 190 150 20 LYS HD2 H 1.736 . 1 191 150 20 LYS HD3 H 1.736 . 1 192 150 20 LYS HE2 H 3.032 . 1 193 150 20 LYS HE3 H 3.032 . 1 194 150 20 LYS C C 176.9 . 1 195 150 20 LYS CA C 56.86 . 1 196 150 20 LYS CB C 33.14 . 1 197 150 20 LYS CG C 24.8 . 1 198 150 20 LYS CD C 29.15 . 1 199 150 20 LYS CE C 42.23 . 1 200 150 20 LYS N N 121.6 . 1 201 151 21 GLU H H 8.378 . 1 202 151 21 GLU HA H 4.224 . 1 203 151 21 GLU HB2 H 1.98 . 2 204 151 21 GLU HB3 H 2.076 . 2 205 151 21 GLU HG2 H 2.263 . 2 206 151 21 GLU HG3 H 2.309 . 2 207 151 21 GLU C C 176.8 . 1 208 151 21 GLU CA C 57 . 1 209 151 21 GLU CB C 30.12 . 1 210 151 21 GLU CG C 36.39 . 1 211 151 21 GLU N N 121.3 . 1 212 152 22 LYS H H 8.22 . 1 213 152 22 LYS HA H 4.227 . 1 214 152 22 LYS HB2 H 1.791 . 1 215 152 22 LYS HB3 H 1.791 . 1 216 152 22 LYS HG2 H 1.443 . 1 217 152 22 LYS HG3 H 1.443 . 1 218 152 22 LYS HD2 H 1.707 . 1 219 152 22 LYS HD3 H 1.707 . 1 220 152 22 LYS HE2 H 3.025 . 1 221 152 22 LYS HE3 H 3.025 . 1 222 152 22 LYS C C 176.4 . 1 223 152 22 LYS CA C 56.89 . 1 224 152 22 LYS CB C 33.18 . 1 225 152 22 LYS CG C 24.83 . 1 226 152 22 LYS CD C 29.15 . 1 227 152 22 LYS CE C 42.2 . 1 228 152 22 LYS N N 121.7 . 1 229 153 23 ASP H H 8.355 . 1 230 153 23 ASP HA H 4.598 . 1 231 153 23 ASP HB2 H 2.768 . 2 232 153 23 ASP HB3 H 2.629 . 2 233 153 23 ASP C C 176.4 . 1 234 153 23 ASP CA C 54.53 . 1 235 153 23 ASP CB C 41.32 . 1 236 153 23 ASP N N 121.2 . 1 237 154 24 LEU H H 8.188 . 1 238 154 24 LEU HA H 4.316 . 1 239 154 24 LEU HB2 H 1.617 . 2 240 154 24 LEU HB3 H 1.678 . 2 241 154 24 LEU HG H 1.383 . 1 242 154 24 LEU HD1 H 0.868 . 2 243 154 24 LEU HD2 H 0.929 . 2 244 154 24 LEU C C 177.7 . 1 245 154 24 LEU CA C 55.44 . 1 246 154 24 LEU CB C 42.1 . 1 247 154 24 LEU CG C 26.96 . 1 248 154 24 LEU CD1 C 23.5 . 2 249 154 24 LEU CD2 C 25.2 . 2 250 154 24 LEU N N 123 . 1 251 155 25 ARG H H 8.245 . 1 252 155 25 ARG HA H 4.249 . 1 253 155 25 ARG HB2 H 1.811 . 1 254 155 25 ARG HB3 H 1.811 . 1 255 155 25 ARG HG2 H 1.654 . 1 256 155 25 ARG HG3 H 1.654 . 1 257 155 25 ARG HD2 H 3.179 . 1 258 155 25 ARG HD3 H 3.179 . 1 259 155 25 ARG C C 176.3 . 1 260 155 25 ARG CA C 56.64 . 1 261 155 25 ARG CB C 30.86 . 1 262 155 25 ARG CG C 27.07 . 1 263 155 25 ARG CD C 43.45 . 1 264 155 25 ARG N N 120.7 . 1 265 156 26 ASP H H 8.335 . 1 266 156 26 ASP HA H 4.666 . 1 267 156 26 ASP HB2 H 2.641 . 2 268 156 26 ASP HB3 H 2.765 . 2 269 156 26 ASP C C 176.4 . 1 270 156 26 ASP CA C 54.45 . 1 271 156 26 ASP CB C 41.4 . 1 272 156 26 ASP N N 120.9 . 1 273 157 27 VAL H H 8.043 . 1 274 157 27 VAL HA H 4.128 . 1 275 157 27 VAL HB H 2.185 . 1 276 157 27 VAL HG1 H 0.945 . 2 277 157 27 VAL HG2 H 0.956 . 2 278 157 27 VAL C C 176.8 . 1 279 157 27 VAL CA C 62.54 . 1 280 157 27 VAL CB C 32.6 . 1 281 157 27 VAL CG1 C 20.4 . 2 282 157 27 VAL CG2 C 21.32 . 2 283 157 27 VAL N N 119.4 . 1 284 158 28 GLY H H 8.408 . 1 285 158 28 GLY HA2 H 3.904 . 1 286 158 28 GLY HA3 H 3.904 . 1 287 158 28 GLY C C 174.1 . 1 288 158 28 GLY CA C 45.5 . 1 289 158 28 GLY N N 111.1 . 1 290 159 29 ASP H H 8.213 . 1 291 159 29 ASP HA H 4.585 . 1 292 159 29 ASP HB2 H 2.616 . 2 293 159 29 ASP HB3 H 2.766 . 2 294 159 29 ASP C C 176.6 . 1 295 159 29 ASP CA C 54.51 . 1 296 159 29 ASP CB C 41.2 . 1 297 159 29 ASP N N 121 . 1 298 160 30 TRP H H 7.982 . 1 299 160 30 TRP HA H 4.538 . 1 300 160 30 TRP HB2 H 3.3 . 2 301 160 30 TRP HB3 H 3.396 . 2 302 160 30 TRP HD1 H 7.364 . 1 303 160 30 TRP HE1 H 10.24 . 1 304 160 30 TRP HE3 H 7.495 . 1 305 160 30 TRP HZ2 H 7.552 . 1 306 160 30 TRP HZ3 H 7.216 . 1 307 160 30 TRP HH2 H 7.13 . 1 308 160 30 TRP C C 176.8 . 1 309 160 30 TRP CA C 58 . 1 310 160 30 TRP CB C 29.02 . 1 311 160 30 TRP N N 122 . 1 312 161 31 ARG H H 7.788 . 1 313 161 31 ARG HA H 3.927 . 1 314 161 31 ARG HB2 H 1.457 . 2 315 161 31 ARG HB3 H 1.621 . 2 316 161 31 ARG HG2 H 0.942 . 2 317 161 31 ARG HG3 H 1.055 . 2 318 161 31 ARG HD2 H 2.988 . 1 319 161 31 ARG HD3 H 2.988 . 1 320 161 31 ARG C C 176.7 . 1 321 161 31 ARG CA C 57 . 1 322 161 31 ARG CB C 30.21 . 1 323 161 31 ARG CG C 26.76 . 1 324 161 31 ARG CD C 43.21 . 1 325 161 31 ARG N N 121.4 . 1 326 162 32 LYS H H 7.885 . 1 327 162 32 LYS HA H 4.16 . 1 328 162 32 LYS HB2 H 1.778 . 1 329 162 32 LYS HB3 H 1.778 . 1 330 162 32 LYS HG2 H 1.417 . 1 331 162 32 LYS HG3 H 1.417 . 1 332 162 32 LYS HD2 H 1.681 . 1 333 162 32 LYS HD3 H 1.681 . 1 334 162 32 LYS HE2 H 2.993 . 1 335 162 32 LYS HE3 H 2.993 . 1 336 162 32 LYS C C 176.6 . 1 337 162 32 LYS CA C 56.9 . 1 338 162 32 LYS CB C 33.01 . 1 339 162 32 LYS CG C 24.8 . 1 340 162 32 LYS CD C 29.19 . 1 341 162 32 LYS CE C 42.28 . 1 342 162 32 LYS N N 120.3 . 1 343 163 33 ASN H H 8.248 . 1 344 163 33 ASN HA H 4.696 . 1 345 163 33 ASN HB2 H 2.765 . 2 346 163 33 ASN HB3 H 2.857 . 2 347 163 33 ASN C C 175.5 . 1 348 163 33 ASN CA C 53.71 . 1 349 163 33 ASN CB C 38.92 . 1 350 163 33 ASN N N 118.8 . 1 351 164 34 ILE H H 7.973 . 1 352 164 34 ILE HA H 4.132 . 1 353 164 34 ILE HB H 1.906 . 1 354 164 34 ILE HG12 H 1.459 . 2 355 164 34 ILE HG13 H 1.201 . 2 356 164 34 ILE HG2 H 0.912 . 1 357 164 34 ILE HD1 H 0.868 . 1 358 164 34 ILE C C 176.5 . 1 359 164 34 ILE CA C 61.68 . 1 360 164 34 ILE CB C 38.79 . 1 361 164 34 ILE CG1 C 27.45 . 1 362 164 34 ILE CG2 C 17.72 . 1 363 164 34 ILE CD1 C 13.24 . 1 364 164 34 ILE N N 120.3 . 1 365 165 35 GLU H H 8.393 . 1 366 165 35 GLU HA H 4.282 . 1 367 165 35 GLU HB2 H 2.029 . 1 368 165 35 GLU HB3 H 2.029 . 1 369 165 35 GLU HG2 H 2.283 . 1 370 165 35 GLU HG3 H 2.283 . 1 371 165 35 GLU C C 176.8 . 1 372 165 35 GLU CA C 56.98 . 1 373 165 35 GLU CB C 30.44 . 1 374 165 35 GLU CG C 36.44 . 1 375 165 35 GLU N N 124 . 1 376 166 36 GLU H H 8.376 . 1 377 166 36 GLU HA H 4.3 . 1 378 166 36 GLU HB2 H 2.026 . 1 379 166 36 GLU HB3 H 2.026 . 1 380 166 36 GLU HG2 H 2.289 . 1 381 166 36 GLU HG3 H 2.289 . 1 382 166 36 GLU C C 176.7 . 1 383 166 36 GLU CA C 56.91 . 1 384 166 36 GLU CB C 30.48 . 1 385 166 36 GLU CG C 36.44 . 1 386 166 36 GLU N N 122.3 . 1 387 167 37 LYS H H 8.351 . 1 388 167 37 LYS HA H 4.367 . 1 389 167 37 LYS HB2 H 1.876 . 1 390 167 37 LYS HB3 H 1.876 . 1 391 167 37 LYS HG2 H 1.459 . 1 392 167 37 LYS HG3 H 1.459 . 1 393 167 37 LYS HD2 H 1.707 . 1 394 167 37 LYS HD3 H 1.707 . 1 395 167 37 LYS HE2 H 3.006 . 1 396 167 37 LYS HE3 H 3.006 . 1 397 167 37 LYS C C 176.9 . 1 398 167 37 LYS CA C 56.58 . 1 399 167 37 LYS CB C 33.08 . 1 400 167 37 LYS CG C 24.8 . 1 401 167 37 LYS CD C 29.13 . 1 402 167 37 LYS CE C 42.23 . 1 403 167 37 LYS N N 122.1 . 1 404 168 38 SER H H 8.405 . 1 405 168 38 SER HA H 4.451 . 1 406 168 38 SER HB2 H 3.907 . 2 407 168 38 SER HB3 H 3.934 . 2 408 168 38 SER C C 175.4 . 1 409 168 38 SER CA C 58.86 . 1 410 168 38 SER CB C 63.86 . 1 411 168 38 SER N N 116.6 . 1 412 169 39 GLY H H 8.529 . 1 413 169 39 GLY HA2 H 4.031 . 1 414 169 39 GLY HA3 H 4.031 . 1 415 169 39 GLY C C 174.7 . 1 416 169 39 GLY CA C 45.67 . 1 417 169 39 GLY N N 11.09 . 1 418 170 40 MET H H 8.264 . 1 419 170 40 MET HA H 4.472 . 1 420 170 40 MET HB2 H 2.029 . 2 421 170 40 MET HB3 H 2.13 . 2 422 170 40 MET HG2 H 2.525 . 2 423 170 40 MET HG3 H 2.621 . 2 424 170 40 MET HE H 1.775 . 1 425 170 40 MET C C 176.8 . 1 426 170 40 MET CA C 55.91 . 1 427 170 40 MET CB C 32.91 . 1 428 170 40 MET CG C 32.2 . 1 429 170 40 MET N N 119.7 . 1 430 171 41 GLU H H 8.612 . 1 431 171 41 GLU HA H 4.246 . 1 432 171 41 GLU HB2 H 2.042 . 1 433 171 41 GLU HB3 H 2.042 . 1 434 171 41 GLU HG2 H 2.299 . 1 435 171 41 GLU HG3 H 2.299 . 1 436 171 41 GLU C C 177.3 . 1 437 171 41 GLU CA C 57.51 . 1 438 171 41 GLU CB C 29.99 . 1 439 171 41 GLU CG C 36.31 . 1 440 171 41 GLU N N 121.5 . 1 441 172 42 GLY H H 8.434 . 1 442 172 42 GLY HA2 H 3.954 . 1 443 172 42 GLY HA3 H 3.954 . 1 444 172 42 GLY C C 174.4 . 1 445 172 42 GLY CA C 45.64 . 1 446 172 42 GLY N N 109.5 . 1 447 173 43 ARG H H 8.055 . 1 448 173 43 ARG HA H 4.327 . 1 449 173 43 ARG HB2 H 1.811 . 1 450 173 43 ARG HB3 H 1.811 . 1 451 173 43 ARG HG2 H 1.655 . 1 452 173 43 ARG HG3 H 1.655 . 1 453 173 43 ARG HD2 H 3.206 . 1 454 173 43 ARG HD3 H 3.206 . 1 455 173 43 ARG HE H 3.028 . 1 456 173 43 ARG C C 176.6 . 1 457 173 43 ARG CA C 56.45 . 1 458 173 43 ARG CB C 30.88 . 1 459 173 43 ARG CG C 27.23 . 1 460 173 43 ARG CD C 43.47 . 1 461 173 43 ARG N N 120.5 . 1 462 174 44 LYS H H 8.291 . 1 463 174 44 LYS HA H 4.301 . 1 464 174 44 LYS HB2 H 1.814 . 1 465 174 44 LYS HB3 H 1.814 . 1 466 174 44 LYS HG2 H 1.443 . 1 467 174 44 LYS HG3 H 1.443 . 1 468 174 44 LYS HD2 H 1.713 . 1 469 174 44 LYS HD3 H 1.713 . 1 470 174 44 LYS HE2 H 2.999 . 1 471 174 44 LYS HE3 H 2.999 . 1 472 174 44 LYS C C 176.7 . 1 473 174 44 LYS CA C 56.66 . 1 474 174 44 LYS CB C 33.15 . 1 475 174 44 LYS CG C 24.88 . 1 476 174 44 LYS CD C 29.15 . 1 477 174 44 LYS CE C 42.25 . 1 478 174 44 LYS N N 122.3 . 1 479 175 45 LYS H H 8.302 . 1 480 175 45 LYS HA H 4.272 . 1 481 175 45 LYS HB2 H 1.752 . 1 482 175 45 LYS HB3 H 1.752 . 1 483 175 45 LYS HG2 H 1.427 . 1 484 175 45 LYS HG3 H 1.427 . 1 485 175 45 LYS HD2 H 1.681 . 1 486 175 45 LYS HD3 H 1.681 . 1 487 175 45 LYS C C 176.5 . 1 488 175 45 LYS CA C 56.6 . 1 489 175 45 LYS CB C 33.14 . 1 490 175 45 LYS CG C 24.8 . 1 491 175 45 LYS CD C 29.26 . 1 492 175 45 LYS CE C 42.28 . 1 493 175 45 LYS N N 122.4 . 1 494 176 46 MET H H 8.31 . 1 495 176 46 MET HA H 4.383 . 1 496 176 46 MET HB2 H 1.932 . 1 497 176 46 MET HB3 H 1.932 . 1 498 176 46 MET HG2 H 2.411 . 2 499 176 46 MET HG3 H 2.488 . 2 500 176 46 MET C C 175.9 . 1 501 176 46 MET CA C 55.83 . 1 502 176 46 MET CB C 33.07 . 1 503 176 46 MET N N 121.3 . 1 504 177 47 PHE H H 8.195 . 1 505 177 47 PHE HA H 4.632 . 1 506 177 47 PHE HB2 H 3.04 . 2 507 177 47 PHE HB3 H 3.171 . 2 508 177 47 PHE HD1 H 7.27 . 1 509 177 47 PHE HD2 H 7.317 . 1 510 177 47 PHE HE1 H 7.026 . 1 511 177 47 PHE HE2 H 6.915 . 1 512 177 47 PHE HZ H 7.84 . 1 513 177 47 PHE C C 175.7 . 1 514 177 47 PHE CA C 57.76 . 1 515 177 47 PHE CB C 39.69 . 1 516 177 47 PHE N N 120.5 . 1 517 178 48 GLU H H 8.346 . 1 518 178 48 GLU HA H 4.269 . 1 519 178 48 GLU HB2 H 1.988 . 2 520 178 48 GLU HB3 H 2.068 . 2 521 178 48 GLU HG2 H 2.309 . 2 522 178 48 GLU HG3 H 2.238 . 2 523 178 48 GLU C C 175.9 . 1 524 178 48 GLU CA C 56.36 . 1 525 178 48 GLU CB C 30.63 . 1 526 178 48 GLU CG C 36.37 . 1 527 178 48 GLU N N 122.6 . 1 528 179 49 ALA H H 8.339 . 1 529 179 49 ALA HA H 4.301 . 1 530 179 49 ALA HB H 1.432 . 1 531 179 49 ALA C C 178.2 . 1 532 179 49 ALA CA C 52.86 . 1 533 179 49 ALA CB C 19.44 . 1 534 179 49 ALA N N 125 . 1 535 180 50 GLY H H 8.366 . 1 536 180 50 GLY HA2 H 3.992 . 1 537 180 50 GLY HA3 H 3.992 . 1 538 180 50 GLY C C 174.1 . 1 539 180 50 GLY CA C 45.35 . 1 540 180 50 GLY N N 108.2 . 1 541 181 51 GLU H H 8.253 . 1 542 181 51 GLU HA H 4.394 . 1 543 181 51 GLU C C 175.8 . 1 544 181 51 GLU CA C 56.54 . 1 545 181 51 GLU CB C 30.88 . 1 546 181 51 GLU CG C 36.39 . 1 547 181 51 GLU N N 120.8 . 1 548 182 52 SER H H 8.024 . 1 549 182 52 SER HA H 4.251 . 1 550 182 52 SER CA C 60.02 . 1 551 182 52 SER CB C 64.92 . 1 552 182 52 SER N N 122.2 . 1 stop_ save_