data_15508 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical shift values for the innermost lipoyl domain of E. coli PDH complex ; _BMRB_accession_number 15508 _BMRB_flat_file_name bmr15508.str _Entry_type original _Submission_date 2007-10-04 _Accession_date 2007-10-04 _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 Dafydd Jones . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 271 "15N chemical shifts" 76 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-03 update BMRB 'complete entry citation' 2007-10-12 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Restricted motion of the lipoyl-lysine swinging arm in the pyruvate dehydrogenase complex of Escherichia coli' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 10913250 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Jones Dafydd . . 2 Stott Katherine . . 3 Howard Mark . . 4 Perham Richard . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 39 _Journal_issue 29 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 8448 _Page_last 8459 _Year 2000 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'lipoyl domain' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label E2plip $lipoyl_domain 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_lipoyl_domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common lipoyl_domain _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 79 _Mol_residue_sequence ; VKEVNVPDIGGDEVEVTEVM VKVGDKVAAEQSLITVEGDK ASMEVPAPFAGVVKELKVNV GDKVKTGSLIMIFEVEGAA ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 2 VAL 2 3 LYS 3 4 GLU 4 5 VAL 5 6 ASN 6 7 VAL 7 8 PRO 8 9 ASP 9 10 ILE 10 11 GLY 11 12 GLY 12 13 ASP 13 14 GLU 14 15 VAL 15 16 GLU 16 17 VAL 17 18 THR 18 19 GLU 19 20 VAL 20 21 MET 21 22 VAL 22 23 LYS 23 24 VAL 24 25 GLY 25 26 ASP 26 27 LYS 27 28 VAL 28 29 ALA 29 30 ALA 30 31 GLU 31 32 GLN 32 33 SER 33 34 LEU 34 35 ILE 35 36 THR 36 37 VAL 37 38 GLU 38 39 GLY 39 40 ASP 40 41 LYS 41 42 ALA 42 43 SER 43 44 MET 44 45 GLU 45 46 VAL 46 47 PRO 47 48 ALA 48 49 PRO 49 50 PHE 50 51 ALA 51 52 GLY 52 53 VAL 53 54 VAL 54 55 LYS 55 56 GLU 56 57 LEU 57 58 LYS 58 59 VAL 59 60 ASN 60 61 VAL 61 62 GLY 62 63 ASP 63 64 LYS 64 65 VAL 65 66 LYS 66 67 THR 67 68 GLY 68 69 SER 69 70 LEU 70 71 ILE 71 72 MET 72 73 ILE 73 74 PHE 74 75 GLU 75 76 VAL 76 77 GLU 77 78 GLY 78 79 ALA 79 80 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-09-09 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 1QJO "Innermost Lipoyl Domain Of The Pyruvate Dehydrogenase From Escherichia Coli" 100.00 80 100.00 100.00 9.32e-44 EMBL CSG13687 "dihydrolipoamide acetyltransferase [Shigella sonnei]" 75.95 406 100.00 100.00 2.40e-28 EMBL CSG32591 "dihydrolipoamide acetyltransferase [Shigella sonnei]" 100.00 425 98.73 100.00 1.29e-40 EMBL CSG39424 "dihydrolipoamide acetyltransferase [Shigella sonnei]" 72.15 403 98.25 100.00 4.27e-26 GB EFI22553 "dihydrolipoamide acetyltransferase [Escherichia coli FVEC1302]" 81.01 410 98.44 100.00 2.87e-30 GB EFZ46147 "dihydrolipoyllysine-residue acetyltransferase E2 component of pyruvate dehydrogenase complex [Escherichia coli E128010]" 100.00 440 98.73 100.00 6.45e-41 GB EGB41640 "2-oxoacid dehydrogenase acyltransferase [Escherichia coli H120]" 82.28 411 100.00 100.00 2.71e-31 GB EGB60459 "2-oxoacid dehydrogenase acyltransferase [Escherichia coli M863]" 100.00 456 100.00 100.00 5.79e-41 GB EGI12521 "dihydrolipoyllysine-residue acetyltransferase E2 component of pyruvate dehydrogenase complex [Escherichia coli H736]" 100.00 425 98.73 100.00 1.36e-40 REF WP_000295776 "dihydrolipoamide acetyltransferase, partial [Escherichia coli]" 100.00 429 98.73 100.00 2.15e-40 REF WP_000374927 "hypothetical protein, partial [Escherichia coli]" 82.28 411 100.00 100.00 2.71e-31 REF WP_032230881 "pyruvate dehydrogenase, partial [Escherichia coli]" 83.54 412 100.00 100.00 9.14e-32 REF WP_050541395 "pyruvate dehydrogenase, partial [Escherichia coli]" 84.81 433 97.01 100.00 1.57e-31 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $lipoyl_domain 'E. coli' 562 Eubacteria . Escherichia coli 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 $lipoyl_domain 'recombinant technology' . Escherichia coli . pET11c stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $lipoyl_domain 2-3 mM '[U-100% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_ANSIG _Saveframe_category software _Name ANSIG _Version . loop_ _Vendor _Address _Electronic_address Kraulis . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AM _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_2D_DQF-COSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D DQF-COSY' _Sample_label $sample_1 save_ save_2D_1H-1H_TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_1 save_ save_2D_1H-1H_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.5 . pH pressure 1 . atm 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 TSP H 1 'methyl protons' ppm 0 internal direct . . . 1.0 '[15N] ammonium chloride' N 15 nitrogen ppm 0 external direct . . . 1.0 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_E2plip-chemical-shift _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '2D 1H-1H NOESY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name E2plip _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 2 1 VAL H H 8.65 . 1 2 2 1 VAL HA H 5.75 . 1 3 2 1 VAL HB H 1.98 . 1 4 2 1 VAL N N 120.2 . 1 5 3 2 LYS H H 9.12 . 1 6 3 2 LYS HA H 4.61 . 1 7 3 2 LYS HB2 H 1.42 . 1 8 3 2 LYS HB3 H 1.42 . 1 9 3 2 LYS N N 122.1 . 1 10 4 3 GLU H H 8.76 . 1 11 4 3 GLU HA H 4.14 . 1 12 4 3 GLU HB2 H 1.89 . 1 13 4 3 GLU HB3 H 2.12 . 1 14 4 3 GLU N N 122.7 . 1 15 5 4 VAL H H 8.21 . 1 16 5 4 VAL HA H 3.97 . 1 17 5 4 VAL HB H 1.37 . 1 18 5 4 VAL N N 119.5 . 1 19 6 5 ASN H H 8.65 . 1 20 6 5 ASN HA H 5.65 . 1 21 6 5 ASN HB2 H 2.16 . 1 22 6 5 ASN HB3 H 2.29 . 1 23 6 5 ASN N N 124.6 . 1 24 7 6 VAL H H 8.82 . 1 25 7 6 VAL HA H 3.78 . 1 26 7 6 VAL HB H 2.38 . 1 27 7 6 VAL N N 121.6 . 1 28 9 8 ASP H H 8.01 . 1 29 9 8 ASP HA H 4.8 . 1 30 9 8 ASP HB2 H 2.55 . 1 31 9 8 ASP HB3 H 2.85 . 1 32 9 8 ASP N N 110.5 . 1 33 10 9 ILE H H 8.29 . 1 34 10 9 ILE HA H 4.46 . 1 35 10 9 ILE HB H 2.47 . 1 36 10 9 ILE N N 123.9 . 1 37 11 10 GLY H H 8.52 . 1 38 11 10 GLY HA2 H 3.81 . 1 39 11 10 GLY HA3 H 4.39 . 1 40 11 10 GLY N N 129.1 . 1 41 12 11 GLY H H 8.67 . 1 42 12 11 GLY HA2 H 3.75 . 1 43 12 11 GLY HA3 H 4.25 . 1 44 12 11 GLY N N 126 . 1 45 13 12 ASP H H 7.86 . 1 46 13 12 ASP HA H 4.85 . 1 47 13 12 ASP HB2 H 2.57 . 1 48 13 12 ASP HB3 H 2.72 . 1 49 13 12 ASP N N 118.1 . 1 50 14 13 GLU H H 8.6 . 1 51 14 13 GLU HA H 4.74 . 1 52 14 13 GLU HB2 H 1.91 . 1 53 14 13 GLU HB3 H 1.91 . 1 54 14 13 GLU N N 120.2 . 1 55 15 14 VAL H H 8.88 . 1 56 15 14 VAL HA H 4.73 . 1 57 15 14 VAL HB H 1.88 . 1 58 15 14 VAL N N 114.69 . 1 59 16 15 GLU H H 8.31 . 1 60 16 15 GLU HA H 5.06 . 1 61 16 15 GLU HB2 H 1.79 . 1 62 16 15 GLU HB3 H 1.85 . 1 63 16 15 GLU N N 119.05 . 1 64 17 16 VAL H H 9.13 . 1 65 17 16 VAL HA H 4.31 . 1 66 17 16 VAL HB H 2.36 . 1 67 17 16 VAL N N 123.88 . 1 68 18 17 THR H H 9.21 . 1 69 18 17 THR HA H 4.59 . 1 70 18 17 THR HB H 4.27 . 1 71 18 17 THR N N 120.27 . 1 72 19 18 GLU H H 7.53 . 1 73 19 18 GLU HA H 4.41 . 1 74 19 18 GLU HB2 H 1.87 . 1 75 19 18 GLU HB3 H 2 . 1 76 19 18 GLU N N 118.63 . 1 77 20 19 VAL H H 9.04 . 1 78 20 19 VAL HA H 4.41 . 1 79 20 19 VAL HB H 2.18 . 1 80 20 19 VAL N N 125.14 . 1 81 21 20 MET H H 8.4 . 1 82 21 20 MET HA H 4.46 . 1 83 21 20 MET HB2 H 1.66 . 1 84 21 20 MET HB3 H 1.7 . 1 85 21 20 MET N N 122.7 . 1 86 22 21 VAL H H 7.04 . 1 87 22 21 VAL HA H 4.68 . 1 88 22 21 VAL HB H 2.17 . 1 89 22 21 VAL N N 125.96 . 1 90 23 22 LYS H H 8.65 . 1 91 23 22 LYS HA H 4.64 . 1 92 23 22 LYS HB2 H 1.72 . 1 93 23 22 LYS HB3 H 1.72 . 1 94 23 22 LYS N N 117.24 . 1 95 24 23 VAL H H 8.41 . 1 96 24 23 VAL HA H 3.22 . 1 97 24 23 VAL HB H 1.89 . 1 98 24 23 VAL N N 117.99 . 1 99 25 24 GLY H H 9.19 . 1 100 25 24 GLY HA2 H 3.46 . 1 101 25 24 GLY HA3 H 4.43 . 1 102 25 24 GLY N N 114.64 . 1 103 26 25 ASP H H 8.06 . 1 104 26 25 ASP HA H 4.5 . 1 105 26 25 ASP HB2 H 2.43 . 1 106 26 25 ASP HB3 H 2.81 . 1 107 26 25 ASP N N 120.18 . 1 108 27 26 LYS H H 8.51 . 1 109 27 26 LYS HA H 4.49 . 1 110 27 26 LYS HB2 H 1.93 . 1 111 27 26 LYS HB3 H 1.93 . 1 112 27 26 LYS N N 120.54 . 1 113 28 27 VAL H H 8.96 . 1 114 28 27 VAL HA H 4.37 . 1 115 28 27 VAL HB H 1.59 . 1 116 28 27 VAL N N 124.82 . 1 117 29 28 ALA H H 8.2 . 1 118 29 28 ALA HA H 4.6 . 1 119 29 28 ALA HB H 1.42 . 1 120 29 28 ALA N N 128.22 . 1 121 30 29 ALA H H 8.52 . 1 122 30 29 ALA HA H 3.45 . 1 123 30 29 ALA HB H 1.36 . 1 124 30 29 ALA N N 120.12 . 1 125 31 30 GLU H H 8.77 . 1 126 31 30 GLU HA H 3.77 . 1 127 31 30 GLU HB2 H 2.4 . 1 128 31 30 GLU HB3 H 2.4 . 1 129 31 30 GLU N N 112.27 . 1 130 32 31 GLN H H 7.87 . 1 131 32 31 GLN HA H 4.17 . 1 132 32 31 GLN HB2 H 2.02 . 1 133 32 31 GLN HB3 H 2.21 . 1 134 32 31 GLN N N 121.83 . 1 135 33 32 SER H H 8.96 . 1 136 33 32 SER HA H 4.2 . 1 137 33 32 SER HB2 H 3.75 . 1 138 33 32 SER HB3 H 3.67 . 1 139 33 32 SER N N 121.67 . 1 140 34 33 LEU H H 9.05 . 1 141 34 33 LEU HA H 4.56 . 1 142 34 33 LEU HB2 H 1.31 . 1 143 34 33 LEU HB3 H 1.77 . 1 144 34 33 LEU N N 119.78 . 1 145 35 34 ILE H H 6.95 . 1 146 35 34 ILE HA H 5.07 . 1 147 35 34 ILE HB H 2.27 . 1 148 35 34 ILE N N 123.55 . 1 149 36 35 THR H H 8.83 . 1 150 36 35 THR HA H 5.15 . 1 151 36 35 THR HB H 3.9 . 1 152 36 35 THR N N 116.78 . 1 153 37 36 VAL H H 9.12 . 1 154 37 36 VAL HA H 5.63 . 1 155 37 36 VAL HB H 1.8 . 1 156 37 36 VAL N N 115.7 . 1 157 38 37 GLU H H 9.19 . 1 158 38 37 GLU HA H 4.91 . 1 159 38 37 GLU HB2 H 1.95 . 1 160 38 37 GLU HB3 H 2.01 . 1 161 38 37 GLU N N 119.1 . 1 162 39 38 GLY H H 8.42 . 1 163 39 38 GLY HA2 H 3.94 . 1 164 39 38 GLY HA3 H 4.71 . 1 165 39 38 GLY N N 113.2 . 1 166 40 39 ASP H H 8.73 . 1 167 40 39 ASP HA H 4.41 . 1 168 40 39 ASP HB2 H 2.7 . 1 169 40 39 ASP HB3 H 2.73 . 1 170 40 39 ASP N N 119.96 . 1 171 41 40 LYS H H 8.5 . 1 172 41 40 LYS HA H 4.36 . 1 173 41 40 LYS HB2 H 1.79 . 1 174 41 40 LYS HB3 H 1.79 . 1 175 41 40 LYS N N 114.02 . 1 176 42 41 ALA H H 7.57 . 1 177 42 41 ALA HA H 4.59 . 1 178 42 41 ALA HB H 1.38 . 1 179 42 41 ALA N N 119.53 . 1 180 43 42 SER H H 8.35 . 1 181 43 42 SER HA H 5.25 . 1 182 43 42 SER HB2 H 3.78 . 1 183 43 42 SER HB3 H 3.78 . 1 184 43 42 SER N N 113.69 . 1 185 44 43 MET H H 9.01 . 1 186 44 43 MET HA H 4.79 . 1 187 44 43 MET HB2 H 1.94 . 1 188 44 43 MET HB3 H 1.94 . 1 189 44 43 MET N N 119.49 . 1 190 45 44 GLU H H 8.63 . 1 191 45 44 GLU HA H 5.07 . 1 192 45 44 GLU HB2 H 2.08 . 1 193 45 44 GLU HB3 H 2.08 . 1 194 45 44 GLU N N 119.64 . 1 195 46 45 VAL H H 8.51 . 1 196 46 45 VAL HA H 4.39 . 1 197 46 45 VAL HB H 1.97 . 1 198 46 45 VAL N N 122.52 . 1 199 47 46 PRO HA H 4.57 . 1 200 47 46 PRO HB2 H 1.58 . 1 201 47 46 PRO HB3 H 1.58 . 1 202 48 47 ALA H H 8.81 . 1 203 48 47 ALA HA H 4.27 . 1 204 48 47 ALA HB H 1.55 . 1 205 48 47 ALA N N 121.6 . 1 206 49 48 PRO HA H 4.4 . 1 207 49 48 PRO HB2 H 2.16 . 1 208 49 48 PRO HB3 H 2.16 . 1 209 50 49 PHE H H 6.86 . 1 210 50 49 PHE HA H 4.57 . 1 211 50 49 PHE HB2 H 3.43 . 1 212 50 49 PHE HB3 H 3.43 . 1 213 50 49 PHE N N 110.4 . 1 214 51 50 ALA H H 8.48 . 1 215 51 50 ALA HA H 4.59 . 1 216 51 50 ALA HB H 1.61 . 1 217 51 50 ALA N N 117.45 . 1 218 52 51 GLY H H 8.15 . 1 219 52 51 GLY HA2 H 4.02 . 1 220 52 51 GLY HA3 H 4.02 . 1 221 52 51 GLY N N 121.61 . 1 222 53 52 VAL H H 8.36 . 1 223 53 52 VAL HA H 4.73 . 1 224 53 52 VAL HB H 1.72 . 1 225 53 52 VAL N N 117.96 . 1 226 54 53 VAL H H 8.53 . 1 227 54 53 VAL HA H 3.61 . 1 228 54 53 VAL HB H 2.37 . 1 229 54 53 VAL N N 124.54 . 1 230 55 54 LYS H H 9.45 . 1 231 55 54 LYS HA H 4.58 . 1 232 55 54 LYS HB2 H 1.74 . 1 233 55 54 LYS HB3 H 1.74 . 1 234 55 54 LYS N N 112.99 . 1 235 56 55 GLU H H 7.79 . 1 236 56 55 GLU HA H 4.5 . 1 237 56 55 GLU HB2 H 1.84 . 1 238 56 55 GLU HB3 H 1.84 . 1 239 56 55 GLU N N 112.88 . 1 240 57 56 LEU H H 9.21 . 1 241 57 56 LEU HA H 4.6 . 1 242 57 56 LEU HB2 H 1.9 . 1 243 57 56 LEU HB3 H 1.9 . 1 244 57 56 LEU N N 125.47 . 1 245 58 57 LYS H H 8.01 . 1 246 58 57 LYS HA H 4.66 . 1 247 58 57 LYS HB2 H 1.08 . 1 248 58 57 LYS HB3 H 2.07 . 1 249 58 57 LYS N N 119.49 . 1 250 59 58 VAL H H 7.03 . 1 251 59 58 VAL HA H 4.68 . 1 252 59 58 VAL HB H 2.23 . 1 253 59 58 VAL N N 110.45 . 1 254 60 59 ASN H H 8.63 . 1 255 60 59 ASN HA H 4.96 . 1 256 60 59 ASN HB2 H 2.54 . 1 257 60 59 ASN HB3 H 2.65 . 1 258 60 59 ASN N N 120.56 . 1 259 61 60 VAL H H 8.66 . 1 260 61 60 VAL HA H 3.32 . 1 261 61 60 VAL HB H 1.9 . 1 262 61 60 VAL N N 119.24 . 1 263 62 61 GLY H H 9.25 . 1 264 62 61 GLY HA2 H 3.76 . 1 265 62 61 GLY HA3 H 4.49 . 1 266 62 61 GLY N N 115.69 . 1 267 63 62 ASP H H 7.92 . 1 268 63 62 ASP HA H 4.61 . 1 269 63 62 ASP HB2 H 2.68 . 1 270 63 62 ASP HB3 H 2.83 . 1 271 63 62 ASP N N 119.7 . 1 272 64 63 LYS H H 8.53 . 1 273 64 63 LYS HA H 5.35 . 1 274 64 63 LYS HB2 H 1.54 . 1 275 64 63 LYS HB3 H 1.83 . 1 276 64 63 LYS N N 117.15 . 1 277 65 64 VAL H H 9.03 . 1 278 65 64 VAL HA H 4.72 . 1 279 65 64 VAL HB H 2.12 . 1 280 65 64 VAL N N 112.85 . 1 281 66 65 LYS H H 8.41 . 1 282 66 65 LYS HA H 4.74 . 1 283 66 65 LYS HB2 H 1.73 . 1 284 66 65 LYS HB3 H 1.88 . 1 285 66 65 LYS N N 114.32 . 1 286 67 66 THR H H 8.94 . 1 287 67 66 THR HA H 3.95 . 1 288 67 66 THR HB H 4.03 . 1 289 67 66 THR N N 116.9 . 1 290 68 67 GLY H H 8.7 . 1 291 68 67 GLY HA2 H 3.59 . 1 292 68 67 GLY HA3 H 4.35 . 1 293 68 67 GLY N N 114.67 . 1 294 69 68 SER H H 8.65 . 1 295 69 68 SER HA H 4.26 . 1 296 69 68 SER HB2 H 3.77 . 1 297 69 68 SER HB3 H 3.77 . 1 298 69 68 SER N N 118.42 . 1 299 70 69 LEU H H 8.69 . 1 300 70 69 LEU HA H 4.25 . 1 301 70 69 LEU HB2 H 1.85 . 1 302 70 69 LEU HB3 H 1.85 . 1 303 70 69 LEU N N 126.82 . 1 304 71 70 ILE H H 8.78 . 1 305 71 70 ILE HA H 3.77 . 1 306 71 70 ILE HB H 1.79 . 1 307 71 70 ILE N N 114.49 . 1 308 72 71 MET H H 7.88 . 1 309 72 71 MET HA H 4.79 . 1 310 72 71 MET HB2 H 2.02 . 1 311 72 71 MET HB3 H 2.73 . 1 312 72 71 MET N N 114.53 . 1 313 73 72 ILE H H 8.7 . 1 314 73 72 ILE HA H 4.74 . 1 315 73 72 ILE HB H 1.85 . 1 316 73 72 ILE N N 115.85 . 1 317 74 73 PHE H H 9.51 . 1 318 74 73 PHE HA H 5.9 . 1 319 74 73 PHE HB2 H 3.03 . 1 320 74 73 PHE HB3 H 3.19 . 1 321 74 73 PHE N N 127.07 . 1 322 75 74 GLU H H 9.4 . 1 323 75 74 GLU HA H 4.98 . 1 324 75 74 GLU HB2 H 1.88 . 1 325 75 74 GLU HB3 H 2.03 . 1 326 75 74 GLU N N 119.26 . 1 327 76 75 VAL H H 9.04 . 1 328 76 75 VAL HA H 5.24 . 1 329 76 75 VAL HB H 2.17 . 1 330 76 75 VAL N N 122.83 . 1 331 77 76 GLU H H 8.7 . 1 332 77 76 GLU HA H 4.3 . 1 333 77 76 GLU HB2 H 1.95 . 1 334 77 76 GLU HB3 H 2.03 . 1 335 77 76 GLU N N 123.27 . 1 336 78 77 GLY H H 8.49 . 1 337 78 77 GLY HA2 H 3.94 . 1 338 78 77 GLY HA3 H 3.94 . 1 339 78 77 GLY N N 128 . 1 340 79 78 ALA H H 8.16 . 1 341 79 78 ALA HA H 4.31 . 1 342 79 78 ALA HB H 1.35 . 1 343 79 78 ALA N N 122.47 . 1 344 80 79 ALA H H 8.33 . 1 345 80 79 ALA HA H 4.57 . 1 346 80 79 ALA HB H 1.34 . 1 347 80 79 ALA N N 124 . 1 stop_ save_