data_4666 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Biotin carboxyl carrier domain of transcarboxylase (TC 1.3S) ; _BMRB_accession_number 4666 _BMRB_flat_file_name bmr4666.str _Entry_type original _Submission_date 2000-02-08 _Accession_date 2000-02-10 _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 Reddy D. V. . 2 Shenoy B. C. . 3 Carey P. R. . 4 Sonnichsen F. D. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 coupling_constants 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 433 "13C chemical shifts" 247 "15N chemical shifts" 80 "coupling constants" 47 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-05-26 original author . stop_ _Original_release_date 2000-05-26 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Reddy, D.V., Shenoy, B.C., Carey, P.R., and Sonnichsen, F.D., "High Resolution Solution Structure of the 1.3S Subunit of Transcarboxylase from Propionibacterium shermanii," Biochemistry 39, 2509-2516 (2000). ; _Citation_title ; High Resolution Solution Structure of the 1.3S Subunit of Transcarboxylase from Propionibacterium shermanii ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20170876 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Reddy D. V. . 2 Shenoy B. C. . 3 Carey P. R. . 4 Sonnichsen F. D. . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 39 _Journal_issue 10 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2509 _Page_last 2516 _Year 2000 _Details . loop_ _Keyword 'antiparallel beta sheet' hammerhead biocytin stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full 'DELAGLIO' _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ save_ref_2 _Saveframe_category citation _Citation_full 'GARRET' _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ save_ref_3 _Saveframe_category citation _Citation_full 'BRUNGER' _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_system_TC_1.3S _Saveframe_category molecular_system _Mol_system_name 'transcarboxylase 1.3S subunit' _Abbreviation_common 'TC 1.3S' _Enzyme_commission_number 2.1.3.1 loop_ _Mol_system_component_name _Mol_label 'transcarboxylase 1.3S subunit' $TC_1.3S 'biotin moiety' $entity_SNR stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomeric _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'Biotin carboxyl carrier domain' carboxylase stop_ _Database_query_date . _Details ; a biotin residues is covalently attached to the NZ of the Lys moiety: so , the NZ is actually a carbonamide, and the residue (lys +Biotin) is more correctly named: Biocytin. The shiftvalue is as observed for this amide Proton and N15 amide ; save_ ######################## # Monomeric polymers # ######################## save_TC_1.3S _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'TRANSCARBOXYLASE 1.3S SUBUNIT' _Abbreviation_common 'TC 1.3S' _Molecular_mass 12367 _Mol_thiol_state 'not present' _Details ; Biotin covalently atached to Lys 89 (Biocytin), but not included in structure calculation. Shifts for Biotin not included Lys89 : Biotin covalently attached ; ############################## # Polymer residue sequence # ############################## _Residue_count 77 _Mol_residue_sequence ; AGAGKAGEGEIPAPLAGTVS KILVKEGDTVKAGQTVLVLE AMKMETEINAPTDGKVEKVL VKERDAVQGGQGLIKIG ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 47 ALA 2 48 GLY 3 49 ALA 4 50 GLY 5 51 LYS 6 52 ALA 7 53 GLY 8 54 GLU 9 55 GLY 10 56 GLU 11 57 ILE 12 58 PRO 13 59 ALA 14 60 PRO 15 61 LEU 16 62 ALA 17 63 GLY 18 64 THR 19 65 VAL 20 66 SER 21 67 LYS 22 68 ILE 23 69 LEU 24 70 VAL 25 71 LYS 26 72 GLU 27 73 GLY 28 74 ASP 29 75 THR 30 76 VAL 31 77 LYS 32 78 ALA 33 79 GLY 34 80 GLN 35 81 THR 36 82 VAL 37 83 LEU 38 84 VAL 39 85 LEU 40 86 GLU 41 87 ALA 42 88 MET 43 89 LYS 44 90 MET 45 91 GLU 46 92 THR 47 93 GLU 48 94 ILE 49 95 ASN 50 96 ALA 51 97 PRO 52 98 THR 53 99 ASP 54 100 GLY 55 101 LYS 56 102 VAL 57 103 GLU 58 104 LYS 59 105 VAL 60 106 LEU 61 107 VAL 62 108 LYS 63 109 GLU 64 110 ARG 65 111 ASP 66 112 ALA 67 113 VAL 68 114 GLN 69 115 GLY 70 116 GLY 71 117 GLN 72 118 GLY 73 119 LEU 74 120 ILE 75 121 LYS 76 122 ILE 77 123 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-10 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 4667 "TRANSCARBOXYLASE 1.3S SUBUNIT" 100.00 77 100.00 100.00 1.51e-42 PDB 1DCZ "Biotin Carboxyl Carrier Domain Of Transcarboxylase (Tc 1.3s)" 100.00 77 100.00 100.00 1.51e-42 PDB 1DD2 "Biotin Carboxyl Carrier Domain Of Transcarboxylase (Tc 1.3s)" 100.00 77 100.00 100.00 1.51e-42 PDB 1O78 "Biotin Carboxyl Carrier Domain Of Transcarboxylase (1.3s) [10-48] Deletion Mutant" 98.70 84 100.00 100.00 5.32e-42 EMBL CAD59402 "putative methylmalonyl-CoA carboxyltransferase [Propionibacterium freudenreichii subsp. shermanii]" 100.00 123 100.00 100.00 6.47e-42 EMBL CBL57376 "Methylmalonyl-CoA carboxytransferase, 1.3S subunit (Transcarboxylase, 1.3S subunit). 123bp [Propionibacterium freudenreichii su" 100.00 123 100.00 100.00 6.47e-42 EMBL CDP49157 "Methylmalonyl-CoA carboxytransferase, 1.3S subunit (Transcarboxylase, 1.3S subunit). 123bp [Propionibacterium freudenreichii su" 100.00 123 100.00 100.00 6.47e-42 EMBL CEG86413 "Methylmalonyl-CoA carboxytransferase, 1.3S subunit (Transcarboxylase, 1.3S subunit). 123bp [Propionibacterium freudenreichii]" 100.00 123 100.00 100.00 6.47e-42 EMBL CEG88429 "Methylmalonyl-CoA carboxytransferase, 1.3S subunit (Transcarboxylase, 1.3S subunit). 123bp [Propionibacterium freudenreichii]" 100.00 123 100.00 100.00 6.47e-42 GB AAA25674 "transcarboxylase, 1.3S subunit [Propionibacterium freudenreichii subsp. shermanii]" 100.00 123 100.00 100.00 6.47e-42 GB AAA89090 "Biotin purification tag [Cloning vector PinPoint Xa-1]" 100.00 129 100.00 100.00 9.26e-42 GB AAA89092 "Biotin purification tag, partial [Cloning vector PinPoint Xa-2]" 100.00 129 100.00 100.00 9.26e-42 GB AAA89094 "Biotin purification tag [Cloning vector PinPoint Xa-3]" 100.00 129 100.00 100.00 9.26e-42 GB AJQ91496 "Biotin-requiring enzyme [Propionibacterium freudenreichii subsp. freudenreichii]" 100.00 123 100.00 100.00 6.47e-42 REF WP_013161729 "acetyl-CoA carboxylase biotin carboxyl carrier protein subunit [Propionibacterium freudenreichii]" 100.00 123 100.00 100.00 6.47e-42 REF WP_048769525 "acetyl-CoA carboxylase biotin carboxyl carrier protein subunit [Propionibacterium freudenreichii]" 100.00 127 100.00 100.00 8.28e-42 SP P02904 "RecName: Full=Methylmalonyl-CoA carboxyltransferase 1.3S subunit; AltName: Full=Biotin carboxyl carrier protein of transcarboxy" 100.00 123 100.00 100.00 6.47e-42 stop_ save_ ############# # Ligands # ############# save_SNR _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common NORBIOTIN _BMRB_code SNR _PDB_code SNR _Molecular_mass 230.284 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C1 C1 C . 0 . ? C12 C12 C . 0 . ? C13 C13 C . 0 . ? C14 C14 C . 0 . ? C15 C15 C . 0 . ? C3 C3 C . 0 . ? C4 C4 C . 0 . ? C6 C6 C . 0 . ? C8 C8 C . 0 . ? H11 H11 H . 0 . ? H12 H12 H . 0 . ? H13 H13 H . 0 . ? H16 H16 H . 0 . ? H21 H21 H . 0 . ? H22 H22 H . 0 . ? H23 H23 H . 0 . ? H3 H3 H . 0 . ? H4 H4 H . 0 . ? H6 H6 H . 0 . ? H81 H81 H . 0 . ? H82 H82 H . 0 . ? HN2 HN2 H . 0 . ? HN5 HN5 H . 0 . ? N2 N2 N . 0 . ? N5 N5 N . 0 . ? O11 O11 O . 0 . ? O16 O16 O . 0 . ? O17 O17 O . 0 . ? S7 S7 S . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING C1 N2 ? ? SING C1 N5 ? ? DOUB C1 O11 ? ? SING N2 C3 ? ? SING N2 HN2 ? ? SING C3 C4 ? ? SING C3 C8 ? ? SING C3 H3 ? ? SING C4 N5 ? ? SING C4 C6 ? ? SING C4 H4 ? ? SING N5 HN5 ? ? SING C6 S7 ? ? SING C6 C12 ? ? SING C6 H6 ? ? SING S7 C8 ? ? SING C8 H81 ? ? SING C8 H82 ? ? SING C12 C13 ? ? SING C12 H11 ? ? SING C12 H21 ? ? SING C13 C14 ? ? SING C13 H12 ? ? SING C13 H22 ? ? SING C14 C15 ? ? SING C14 H13 ? ? SING C14 H23 ? ? SING C15 O16 ? ? DOUB C15 O17 ? ? SING O16 H16 ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $TC_1.3S 'Propionibacterium Freudenreichii subsp shermanii' 1752 Bacteria . Propionibacterium 'Freudenreichii subsp shermanii' 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 $TC_1.3S 'recombinant technology' 'E. coli' Escherichia coli HB101 . 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $TC_1.3S . mM 1 2 '[U-95%13C; U-90%15N]' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $TC_1.3S . mM 1 2 '[U-90% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_NMRPIPE _Saveframe_category software _Name NMRPIPE _Version SGI6X.M4 loop_ _Task processing stop_ _Details ref_1 save_ save_PIPP _Saveframe_category software _Name PIPP _Version 3.7.3 loop_ _Task 'data analysis' stop_ _Details ref_2 save_ save_X-PLOR _Saveframe_category software _Name X-PLOR _Version 3.81 loop_ _Task 'structure solution' stop_ _Details ref_3 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 500 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.7 0.2 pH temperature 293 0.1 K pressure 1 . atm stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_ref_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_ref_1 _Mol_system_component_name 'transcarboxylase 1.3S subunit' _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 ALA N N 123.9800 0.20 1 2 . 1 ALA H H 8.3660 0.02 1 3 . 1 ALA HA H 4.3420 0.02 1 4 . 1 ALA HB H 1.4050 0.02 1 5 . 1 ALA CA C 51.8620 0.20 1 6 . 1 ALA CB C 18.4780 0.20 1 7 . 2 GLY N N 108.5200 0.20 1 8 . 2 GLY H H 8.4440 0.02 1 9 . 2 GLY HA2 H 3.9380 0.02 1 10 . 2 GLY HA3 H 3.9380 0.02 1 11 . 2 GLY CA C 44.4740 0.20 1 12 . 3 ALA N N 123.7320 0.20 1 13 . 3 ALA H H 8.1950 0.02 1 14 . 3 ALA HA H 4.3360 0.02 1 15 . 3 ALA HB H 1.3930 0.02 1 16 . 3 ALA CA C 51.8610 0.20 1 17 . 3 ALA CB C 18.3260 0.20 1 18 . 4 GLY N N 108.3650 0.20 1 19 . 4 GLY H H 8.4540 0.02 1 20 . 4 GLY HA2 H 3.9540 0.02 1 21 . 4 GLY HA3 H 3.9540 0.02 1 22 . 4 GLY CA C 44.3870 0.20 1 23 . 5 LYS N N 120.6460 0.20 1 24 . 5 LYS H H 8.1170 0.02 1 25 . 5 LYS HA H 4.3290 0.02 1 26 . 5 LYS HE2 H 2.9970 0.02 1 27 . 5 LYS HE3 H 2.9970 0.02 1 28 . 5 LYS HB3 H 1.7970 0.02 2 29 . 5 LYS HB2 H 1.7130 0.02 2 30 . 5 LYS HD2 H 1.6640 0.02 1 31 . 5 LYS HD3 H 1.6640 0.02 1 32 . 5 LYS HG2 H 1.4130 0.02 1 33 . 5 LYS HG3 H 1.4130 0.02 1 34 . 5 LYS CA C 54.9610 0.20 1 35 . 5 LYS CB C 32.9110 0.20 1 36 . 5 LYS CG C 23.9270 0.20 1 37 . 5 LYS CD C 28.2800 0.20 1 38 . 5 LYS CE C 41.0600 0.20 1 39 . 6 ALA N N 125.3780 0.20 1 40 . 6 ALA H H 8.3010 0.02 1 41 . 6 ALA HA H 4.2460 0.02 1 42 . 6 ALA HB H 1.3380 0.02 1 43 . 6 ALA CA C 51.9000 0.20 1 44 . 6 ALA CB C 18.3490 0.20 1 45 . 7 GLY N N 110.6610 0.20 1 46 . 7 GLY H H 8.4600 0.02 1 47 . 7 GLY HA3 H 4.2030 0.02 2 48 . 7 GLY HA2 H 3.7240 0.02 2 49 . 7 GLY CA C 43.4920 0.20 1 50 . 8 GLU N N 121.2780 0.20 1 51 . 8 GLU H H 8.4050 0.02 1 52 . 8 GLU HA H 4.1250 0.02 1 53 . 8 GLU HB2 H 2.0040 0.02 1 54 . 8 GLU HB3 H 2.0040 0.02 1 55 . 8 GLU HG2 H 2.2890 0.02 1 56 . 8 GLU HG3 H 2.2890 0.02 1 57 . 8 GLU CA C 57.0650 0.20 1 58 . 8 GLU CB C 28.9100 0.20 1 59 . 8 GLU CG C 35.3650 0.20 1 60 . 9 GLY N N 112.3540 0.20 1 61 . 9 GLY H H 8.9210 0.02 1 62 . 9 GLY HA3 H 4.2900 0.02 2 63 . 9 GLY HA2 H 3.7980 0.02 2 64 . 9 GLY CA C 45.0540 0.20 1 65 . 10 GLU N N 119.9300 0.20 1 66 . 10 GLU H H 7.9030 0.02 1 67 . 10 GLU HA H 5.0210 0.02 1 68 . 10 GLU HB2 H 2.0980 0.02 1 69 . 10 GLU HG3 H 2.0500 0.02 2 70 . 10 GLU HG2 H 1.7680 0.02 2 71 . 10 GLU HB3 H 1.4860 0.02 1 72 . 10 GLU CA C 54.1010 0.20 1 73 . 10 GLU CB C 29.8170 0.20 1 74 . 10 GLU CG C 36.0870 0.20 1 75 . 11 ILE N N 125.1510 0.20 1 76 . 11 ILE H H 8.7810 0.02 1 77 . 11 ILE HA H 4.3430 0.02 1 78 . 11 ILE HB H 1.7130 0.02 1 79 . 11 ILE HD1 H 0.8600 0.02 1 80 . 11 ILE HG2 H 0.8930 0.02 1 81 . 11 ILE HG13 H 1.0510 0.02 2 82 . 11 ILE HG12 H 1.8310 0.02 2 83 . 11 ILE CA C 58.4160 0.20 1 84 . 11 ILE CB C 39.2170 0.20 1 85 . 11 ILE CG1 C 26.7000 0.20 1 86 . 11 ILE CG2 C 15.7640 0.20 1 87 . 11 ILE CD1 C 13.5690 0.20 1 88 . 12 PRO HA H 5.0000 0.02 1 89 . 12 PRO HB3 H 1.9500 0.02 1 90 . 12 PRO HB2 H 1.6200 0.02 1 91 . 12 PRO HG2 H 2.0000 0.02 1 92 . 12 PRO HG3 H 2.0000 0.02 1 93 . 12 PRO HD3 H 4.2100 0.02 1 94 . 12 PRO HD2 H 3.8000 0.02 1 95 . 12 PRO CA C 59.6530 0.20 1 96 . 12 PRO CB C 31.6840 0.20 1 97 . 12 PRO CG C 25.4910 0.20 1 98 . 12 PRO CD C 50.2600 0.20 1 99 . 13 ALA N N 123.2960 0.20 1 100 . 13 ALA H H 8.7500 0.02 1 101 . 13 ALA HA H 4.4100 0.02 1 102 . 13 ALA HB H 1.5360 0.02 1 103 . 13 ALA CA C 49.3180 0.20 1 104 . 13 ALA CB C 16.8590 0.20 1 105 . 14 PRO HA H 4.4980 0.02 1 106 . 14 PRO HB3 H 2.3200 0.02 1 107 . 14 PRO HB2 H 2.0650 0.02 1 108 . 14 PRO HG3 H 1.9000 0.02 1 109 . 14 PRO HG2 H 2.2110 0.02 1 110 . 14 PRO HD3 H 4.0050 0.02 1 111 . 14 PRO HD2 H 3.5340 0.02 1 112 . 14 PRO CA C 63.0980 0.20 1 113 . 14 PRO CB C 30.7880 0.20 1 114 . 14 PRO CG C 26.0620 0.20 1 115 . 14 PRO CD C 50.2700 0.20 1 116 . 15 LEU N N 115.6280 0.20 1 117 . 15 LEU H H 7.2200 0.02 1 118 . 15 LEU HA H 4.3360 0.02 1 119 . 15 LEU HB3 H 1.6140 0.02 1 120 . 15 LEU HB2 H 1.8510 0.02 1 121 . 15 LEU HG H 1.5010 0.02 1 122 . 15 LEU HD1 H 0.8120 0.02 2 123 . 15 LEU HD2 H 0.7120 0.02 2 124 . 15 LEU CA C 52.6900 0.20 1 125 . 15 LEU CB C 42.5560 0.20 1 126 . 15 LEU CG C 25.8040 0.20 1 127 . 15 LEU CD1 C 24.6760 0.20 1 128 . 15 LEU CD2 C 24.6080 0.20 1 129 . 16 ALA N N 118.9760 0.20 1 130 . 16 ALA H H 7.9510 0.02 1 131 . 16 ALA HA H 4.3890 0.02 1 132 . 16 ALA HB H 1.4950 0.02 1 133 . 16 ALA CA C 50.6340 0.20 1 134 . 16 ALA CB C 18.5410 0.20 1 135 . 17 GLY N N 105.9100 0.20 1 136 . 17 GLY H H 7.7500 0.02 1 137 . 17 GLY HA3 H 4.2640 0.02 2 138 . 17 GLY HA2 H 3.9860 0.02 2 139 . 17 GLY CA C 45.1190 0.20 1 140 . 18 THR N N 116.7620 0.20 1 141 . 18 THR H H 9.0540 0.02 1 142 . 18 THR HA H 5.2730 0.02 1 143 . 18 THR HB H 3.8950 0.02 1 144 . 18 THR HG2 H 1.0100 0.02 1 145 . 18 THR CA C 59.9630 0.20 1 146 . 18 THR CB C 70.4860 0.20 1 147 . 18 THR CG2 C 20.8090 0.20 1 148 . 19 VAL N N 125.8650 0.20 1 149 . 19 VAL H H 9.0850 0.02 1 150 . 19 VAL HA H 3.8890 0.02 1 151 . 19 VAL HB H 2.4210 0.02 1 152 . 19 VAL HG1 H 0.9370 0.02 1 153 . 19 VAL HG2 H 0.7690 0.02 1 154 . 19 VAL CA C 63.1880 0.20 1 155 . 19 VAL CB C 30.4450 0.20 1 156 . 19 VAL CG1 C 20.8240 0.20 1 157 . 19 VAL CG2 C 21.4700 0.20 1 158 . 20 SER N N 127.7950 0.20 1 159 . 20 SER H H 9.0430 0.02 1 160 . 20 SER HA H 4.5710 0.02 1 161 . 20 SER HB3 H 3.7540 0.02 2 162 . 20 SER HB2 H 3.6240 0.02 2 163 . 20 SER CA C 58.3800 0.20 1 164 . 20 SER CB C 63.2720 0.20 1 165 . 21 LYS N N 116.8480 0.20 1 166 . 21 LYS H H 7.5390 0.02 1 167 . 21 LYS HA H 4.6910 0.02 1 168 . 21 LYS HB3 H 1.6360 0.02 2 169 . 21 LYS HB2 H 1.5590 0.02 2 170 . 21 LYS HD2 H 1.6600 0.02 1 171 . 21 LYS HD3 H 1.6600 0.02 1 172 . 21 LYS HG2 H 1.3330 0.02 1 173 . 21 LYS HG3 H 1.3330 0.02 1 174 . 21 LYS HE2 H 2.9090 0.02 1 175 . 21 LYS HE3 H 2.9090 0.02 1 176 . 21 LYS CA C 54.6820 0.20 1 177 . 21 LYS CB C 36.4390 0.20 1 178 . 21 LYS CG C 23.9660 0.20 1 179 . 21 LYS CD C 28.3070 0.20 1 180 . 21 LYS CE C 41.3030 0.20 1 181 . 22 ILE N N 124.9930 0.20 1 182 . 22 ILE H H 9.4920 0.02 1 183 . 22 ILE HA H 4.2950 0.02 1 184 . 22 ILE HB H 1.8970 0.02 1 185 . 22 ILE HG13 H 1.4630 0.02 2 186 . 22 ILE HG12 H 0.7380 0.02 2 187 . 22 ILE HG2 H 1.2030 0.02 1 188 . 22 ILE HD1 H 0.8130 0.02 1 189 . 22 ILE CA C 61.7610 0.20 1 190 . 22 ILE CB C 38.4100 0.20 1 191 . 22 ILE CG1 C 27.3370 0.20 1 192 . 22 ILE CG2 C 17.2920 0.20 1 193 . 22 ILE CD1 C 14.1940 0.20 1 194 . 23 LEU N N 126.2140 0.20 1 195 . 23 LEU H H 8.1010 0.02 1 196 . 23 LEU HA H 4.4960 0.02 1 197 . 23 LEU HB3 H 1.9270 0.02 1 198 . 23 LEU HB2 H 1.3990 0.02 1 199 . 23 LEU HG H 1.3670 0.02 1 200 . 23 LEU HD1 H 0.7910 0.02 2 201 . 23 LEU HD2 H 0.7020 0.02 2 202 . 23 LEU CA C 55.3630 0.20 1 203 . 23 LEU CB C 41.6990 0.20 1 204 . 23 LEU CG C 27.9350 0.20 1 205 . 23 LEU CD1 C 23.2940 0.20 1 206 . 23 LEU CD2 C 24.5630 0.20 1 207 . 24 VAL N N 108.7910 0.20 1 208 . 24 VAL H H 7.0470 0.02 1 209 . 24 VAL HA H 4.8250 0.02 1 210 . 24 VAL HB H 2.2520 0.02 1 211 . 24 VAL HG1 H 0.9260 0.02 1 212 . 24 VAL HG2 H 0.7370 0.02 1 213 . 24 VAL CA C 57.4730 0.20 1 214 . 24 VAL CB C 35.2920 0.20 1 215 . 24 VAL CG1 C 21.7010 0.20 1 216 . 24 VAL CG2 C 17.2690 0.20 1 217 . 25 LYS N N 118.5050 0.20 1 218 . 25 LYS H H 8.6770 0.02 1 219 . 25 LYS HA H 4.5840 0.02 1 220 . 25 LYS HB2 H 1.7690 0.02 1 221 . 25 LYS HB3 H 1.7690 0.02 1 222 . 25 LYS HD2 H 1.7030 0.02 1 223 . 25 LYS HD3 H 1.7030 0.02 1 224 . 25 LYS HG3 H 1.5170 0.02 2 225 . 25 LYS HG2 H 1.2950 0.02 2 226 . 25 LYS HE2 H 3.0560 0.02 1 227 . 25 LYS HE3 H 3.0560 0.02 1 228 . 25 LYS CA C 53.1690 0.20 1 229 . 25 LYS CB C 35.1050 0.20 1 230 . 25 LYS CG C 22.9740 0.20 1 231 . 25 LYS CD C 28.2810 0.20 1 232 . 25 LYS CE C 41.3250 0.20 1 233 . 26 GLU N N 119.8610 0.20 1 234 . 26 GLU H H 8.7320 0.02 1 235 . 26 GLU HA H 3.6030 0.02 1 236 . 26 GLU HG3 H 2.3270 0.02 2 237 . 26 GLU HG2 H 2.1450 0.02 2 238 . 26 GLU HB2 H 1.9590 0.02 2 239 . 26 GLU HB3 H 1.8990 0.02 2 240 . 26 GLU CA C 58.4350 0.20 1 241 . 26 GLU CB C 28.0340 0.20 1 242 . 26 GLU CG C 36.7910 0.20 1 243 . 27 GLY N N 113.7640 0.20 1 244 . 27 GLY H H 9.2220 0.02 1 245 . 27 GLY HA3 H 4.5250 0.02 2 246 . 27 GLY HA2 H 3.5700 0.02 2 247 . 27 GLY CA C 44.1060 0.20 1 248 . 28 ASP N N 121.5610 0.20 1 249 . 28 ASP H H 8.0760 0.02 1 250 . 28 ASP HA H 4.6670 0.02 1 251 . 28 ASP HB2 H 2.8280 0.02 2 252 . 28 ASP HB3 H 2.6290 0.02 2 253 . 28 ASP CA C 54.3770 0.20 1 254 . 28 ASP CB C 40.3680 0.20 1 255 . 29 THR N N 115.8980 0.20 1 256 . 29 THR H H 8.6910 0.02 1 257 . 29 THR HA H 4.8510 0.02 1 258 . 29 THR HB H 4.1370 0.02 1 259 . 29 THR HG2 H 1.2210 0.02 1 260 . 29 THR CA C 61.5170 0.20 1 261 . 29 THR CB C 69.2220 0.20 1 262 . 29 THR CG2 C 21.1830 0.20 1 263 . 30 VAL N N 118.2460 0.20 1 264 . 30 VAL H H 9.1510 0.02 1 265 . 30 VAL HA H 4.9500 0.02 1 266 . 30 VAL HB H 1.7460 0.02 1 267 . 30 VAL HG1 H 0.6760 0.02 1 268 . 30 VAL HG2 H 0.6090 0.02 1 269 . 30 VAL CA C 57.4810 0.20 1 270 . 30 VAL CB C 34.6570 0.20 1 271 . 30 VAL CG1 C 22.0540 0.20 1 272 . 30 VAL CG2 C 18.2530 0.20 1 273 . 31 LYS N N 122.3130 0.20 1 274 . 31 LYS H H 8.0060 0.02 1 275 . 31 LYS HA H 4.9280 0.02 1 276 . 31 LYS HB3 H 1.7870 0.02 1 277 . 31 LYS HD2 H 1.6710 0.02 1 278 . 31 LYS HD3 H 1.6710 0.02 1 279 . 31 LYS HB2 H 1.6160 0.02 1 280 . 31 LYS HG2 H 1.4610 0.02 1 281 . 31 LYS HG3 H 1.4610 0.02 1 282 . 31 LYS HE2 H 3.0000 0.02 1 283 . 31 LYS HE3 H 3.0000 0.02 1 284 . 31 LYS CA C 52.0100 0.20 1 285 . 31 LYS CB C 34.2510 0.20 1 286 . 31 LYS CG C 23.6580 0.20 1 287 . 31 LYS CD C 27.9550 0.20 1 288 . 31 LYS CE C 41.3290 0.20 1 289 . 32 ALA N N 123.3120 0.20 1 290 . 32 ALA H H 8.9160 0.02 1 291 . 32 ALA HA H 3.4590 0.02 1 292 . 32 ALA HB H 1.2100 0.02 1 293 . 32 ALA CA C 52.7680 0.20 1 294 . 32 ALA CB C 17.2870 0.20 1 295 . 33 GLY N N 112.3210 0.20 1 296 . 33 GLY H H 9.3310 0.02 1 297 . 33 GLY HA3 H 4.3350 0.02 2 298 . 33 GLY HA2 H 3.5250 0.02 2 299 . 33 GLY CA C 44.1710 0.20 1 300 . 34 GLN N N 123.2460 0.20 1 301 . 34 GLN H H 8.4210 0.02 1 302 . 34 GLN HA H 4.1730 0.02 1 303 . 34 GLN HG3 H 2.4120 0.02 2 304 . 34 GLN HB2 H 2.2990 0.02 1 305 . 34 GLN HG2 H 2.2330 0.02 2 306 . 34 GLN HB3 H 1.9720 0.02 1 307 . 34 GLN HE21 H 7.3770 0.02 1 308 . 34 GLN HE22 H 7.6160 0.02 1 309 . 34 GLN NE2 N 110.7370 0.20 1 310 . 34 GLN CA C 55.3410 0.20 1 311 . 34 GLN CB C 29.7520 0.20 1 312 . 34 GLN CG C 31.9700 0.20 1 313 . 35 THR N N 125.1850 0.20 1 314 . 35 THR H H 8.9270 0.02 1 315 . 35 THR HA H 4.7580 0.02 1 316 . 35 THR HB H 3.8430 0.02 1 317 . 35 THR HG2 H 1.1310 0.02 1 318 . 35 THR CA C 63.0000 0.20 1 319 . 35 THR CB C 67.7570 0.20 1 320 . 35 THR CG2 C 22.3550 0.20 1 321 . 36 VAL N N 117.7920 0.20 1 322 . 36 VAL H H 9.2330 0.02 1 323 . 36 VAL HA H 4.6020 0.02 1 324 . 36 VAL HB H 2.1430 0.02 1 325 . 36 VAL HG1 H 0.8670 0.02 1 326 . 36 VAL HG2 H 0.7730 0.02 1 327 . 36 VAL CA C 60.5560 0.20 1 328 . 36 VAL CB C 32.0540 0.20 1 329 . 36 VAL CG1 C 22.0500 0.20 1 330 . 36 VAL CG2 C 17.7000 0.20 1 331 . 37 LEU N N 121.6090 0.20 1 332 . 37 LEU H H 7.9020 0.02 1 333 . 37 LEU HA H 4.8570 0.02 1 334 . 37 LEU HB3 H 1.9010 0.02 1 335 . 37 LEU HB2 H 1.6100 0.02 1 336 . 37 LEU HG H 1.9640 0.02 1 337 . 37 LEU HD1 H 0.8550 0.02 1 338 . 37 LEU HD2 H 0.8490 0.02 1 339 . 37 LEU CA C 54.9770 0.20 1 340 . 37 LEU CB C 44.9700 0.20 1 341 . 37 LEU CG C 26.1160 0.20 1 342 . 37 LEU CD1 C 27.6600 0.20 1 343 . 37 LEU CD2 C 27.0150 0.20 1 344 . 38 VAL N N 122.2280 0.20 1 345 . 38 VAL H H 8.9800 0.02 1 346 . 38 VAL HA H 4.7030 0.02 1 347 . 38 VAL HB H 1.8040 0.02 1 348 . 38 VAL HG1 H 0.8620 0.02 1 349 . 38 VAL CA C 61.1230 0.20 1 350 . 38 VAL CB C 34.2010 0.20 1 351 . 38 VAL CG1 C 20.5830 0.20 1 352 . 39 LEU N N 128.2510 0.20 1 353 . 39 LEU H H 8.9220 0.02 1 354 . 39 LEU HA H 5.0740 0.02 1 355 . 39 LEU HB2 H 1.3800 0.02 1 356 . 39 LEU HB3 H 1.3800 0.02 1 357 . 39 LEU HG H 1.4580 0.02 2 358 . 39 LEU HD2 H 0.7000 0.02 2 359 . 39 LEU HD1 H 0.7200 0.02 2 360 . 39 LEU CA C 51.8930 0.20 1 361 . 39 LEU CB C 45.5950 0.20 1 362 . 39 LEU CG C 26.3800 0.20 1 363 . 39 LEU CD1 C 25.1620 0.20 1 364 . 39 LEU CD2 C 24.8720 0.20 1 365 . 40 GLU N N 123.7530 0.20 1 366 . 40 GLU H H 9.5050 0.02 1 367 . 40 GLU HA H 5.0460 0.02 1 368 . 40 GLU HG3 H 2.1200 0.02 2 369 . 40 GLU HB3 H 2.0070 0.02 2 370 . 40 GLU HG2 H 1.9700 0.02 2 371 . 40 GLU HB2 H 1.8770 0.02 2 372 . 40 GLU CA C 54.3460 0.20 1 373 . 40 GLU CB C 31.3820 0.20 1 374 . 40 GLU CG C 35.7190 0.20 1 375 . 41 ALA N N 128.7520 0.20 1 376 . 41 ALA H H 8.6060 0.02 1 377 . 41 ALA HA H 4.7060 0.02 1 378 . 41 ALA HB H 1.4710 0.02 1 379 . 41 ALA CA C 51.3250 0.20 1 380 . 41 ALA CB C 20.8030 0.20 1 381 . 42 MET N N 122.3120 0.20 1 382 . 42 MET H H 9.3600 0.02 1 383 . 42 MET HA H 4.0540 0.02 1 384 . 42 MET HG3 H 2.6310 0.02 2 385 . 42 MET HG2 H 2.5380 0.02 2 386 . 42 MET HB3 H 2.2030 0.02 2 387 . 42 MET HB2 H 2.1600 0.02 2 388 . 42 MET HE H 2.1400 0.02 1 389 . 42 MET CA C 55.8060 0.20 1 390 . 42 MET CB C 29.1460 0.20 1 391 . 42 MET CG C 31.7650 0.20 1 392 . 42 MET CE C 16.9000 0.20 1 393 . 43 LYS N N 110.3130 0.20 1 394 . 43 LYS H H 8.8170 0.02 1 395 . 43 LYS HA H 3.8220 0.02 1 396 . 43 LYS HB2 H 2.1030 0.02 2 397 . 43 LYS HB3 H 1.9810 0.02 2 398 . 43 LYS HD3 H 1.5510 0.02 2 399 . 43 LYS HD2 H 1.4730 0.02 2 400 . 43 LYS HG2 H 1.3000 0.02 1 401 . 43 LYS HG3 H 1.3000 0.02 1 402 . 43 LYS NZ N 127.4650 0.20 1 403 . 43 LYS HZ H 8.0380 0.02 1 404 . 43 LYS HE2 H 3.1760 0.02 1 405 . 43 LYS HE3 H 3.1760 0.02 1 406 . 43 LYS CA C 57.1460 0.20 1 407 . 43 LYS CB C 29.6800 0.20 1 408 . 43 LYS CG C 25.1550 0.20 1 409 . 43 LYS CD C 29.8340 0.20 1 410 . 43 LYS CE C 41.2410 0.20 1 411 . 44 MET N N 118.7390 0.20 1 412 . 44 MET H H 7.9110 0.02 1 413 . 44 MET HA H 4.7780 0.02 1 414 . 44 MET HG2 H 2.5670 0.02 1 415 . 44 MET HG3 H 2.5670 0.02 1 416 . 44 MET HB2 H 2.0910 0.02 1 417 . 44 MET HB3 H 2.0910 0.02 1 418 . 44 MET HE H 2.1400 0.02 1 419 . 44 MET CA C 53.5700 0.20 1 420 . 44 MET CB C 34.1710 0.20 1 421 . 44 MET CG C 30.8120 0.20 1 422 . 44 MET CE C 16.9000 0.20 1 423 . 45 GLU N N 123.4910 0.20 1 424 . 45 GLU H H 8.7220 0.02 1 425 . 45 GLU HA H 4.9770 0.02 1 426 . 45 GLU HG3 H 2.2940 0.02 2 427 . 45 GLU HB2 H 1.9660 0.02 1 428 . 45 GLU HG2 H 1.9410 0.02 2 429 . 45 GLU HB3 H 1.7500 0.02 1 430 . 45 GLU CA C 55.2280 0.20 1 431 . 45 GLU CB C 30.7140 0.20 1 432 . 45 GLU CG C 36.3510 0.20 1 433 . 46 THR N N 120.9620 0.20 1 434 . 46 THR H H 9.3110 0.02 1 435 . 46 THR HA H 4.4740 0.02 1 436 . 46 THR HB H 3.7960 0.02 1 437 . 46 THR HG2 H 1.1060 0.02 1 438 . 46 THR CA C 61.4770 0.20 1 439 . 46 THR CB C 70.5710 0.20 1 440 . 46 THR CG2 C 19.9080 0.20 1 441 . 47 GLU N N 127.3010 0.20 1 442 . 47 GLU H H 8.9210 0.02 1 443 . 47 GLU HA H 4.2650 0.02 1 444 . 47 GLU HG3 H 2.4120 0.02 2 445 . 47 GLU HG2 H 2.1760 0.02 2 446 . 47 GLU HB3 H 2.0590 0.02 2 447 . 47 GLU HB2 H 2.0080 0.02 2 448 . 47 GLU CA C 56.2200 0.20 1 449 . 47 GLU CB C 29.4540 0.20 1 450 . 47 GLU CG C 36.2020 0.20 1 451 . 48 ILE N N 123.8100 0.20 1 452 . 48 ILE H H 8.8020 0.02 1 453 . 48 ILE HA H 4.2880 0.02 1 454 . 48 ILE HB H 2.0790 0.02 1 455 . 48 ILE HG2 H 0.7630 0.02 1 456 . 48 ILE HG13 H 1.3990 0.02 2 457 . 48 ILE HG12 H 1.1600 0.02 2 458 . 48 ILE HD1 H 0.6920 0.02 1 459 . 48 ILE CA C 58.0850 0.20 1 460 . 48 ILE CB C 35.7040 0.20 1 461 . 48 ILE CG1 C 26.7490 0.20 1 462 . 48 ILE CG2 C 16.6860 0.20 1 463 . 48 ILE CD1 C 11.0940 0.20 1 464 . 49 ASN N N 126.1060 0.20 1 465 . 49 ASN H H 8.7180 0.02 1 466 . 49 ASN HA H 5.6000 0.02 1 467 . 49 ASN HB2 H 2.4880 0.02 2 468 . 49 ASN HB3 H 2.1470 0.02 2 469 . 49 ASN HD21 H 6.8690 0.02 1 470 . 49 ASN HD22 H 7.0220 0.02 1 471 . 49 ASN ND2 N 109.8220 0.20 1 472 . 49 ASN CA C 50.0880 0.20 1 473 . 49 ASN CB C 39.7320 0.20 1 474 . 50 ALA N N 124.7110 0.20 1 475 . 50 ALA H H 9.0820 0.02 1 476 . 50 ALA HA H 4.3510 0.02 1 477 . 50 ALA HB H 1.4150 0.02 1 478 . 50 ALA CA C 49.3670 0.20 1 479 . 50 ALA CB C 16.6960 0.20 1 480 . 51 PRO HA H 4.5400 0.02 1 481 . 51 PRO HB3 H 2.3690 0.02 1 482 . 51 PRO HG3 H 2.2000 0.02 1 483 . 51 PRO HG2 H 2.1210 0.02 1 484 . 51 PRO HB2 H 2.1040 0.02 1 485 . 51 PRO HD3 H 3.9980 0.02 1 486 . 51 PRO HD2 H 3.7990 0.02 1 487 . 51 PRO CA C 63.3570 0.20 1 488 . 51 PRO CB C 31.6330 0.20 1 489 . 51 PRO CG C 26.3940 0.20 1 490 . 51 PRO CD C 50.5950 0.20 1 491 . 52 THR N N 108.1320 0.20 1 492 . 52 THR H H 7.3310 0.02 1 493 . 52 THR HA H 4.5390 0.02 1 494 . 52 THR HB H 4.2700 0.02 1 495 . 52 THR HG2 H 1.0900 0.02 1 496 . 52 THR CA C 58.3610 0.20 1 497 . 52 THR CB C 71.3580 0.20 1 498 . 52 THR CG2 C 19.5530 0.20 1 499 . 53 ASP N N 119.3620 0.20 1 500 . 53 ASP H H 8.2140 0.02 1 501 . 53 ASP HA H 4.7630 0.02 1 502 . 53 ASP HB3 H 2.8680 0.02 1 503 . 53 ASP HB2 H 2.5830 0.02 1 504 . 53 ASP CA C 53.2000 0.20 1 505 . 53 ASP CB C 40.6900 0.20 1 506 . 54 GLY N N 108.0300 0.20 1 507 . 54 GLY H H 8.2050 0.02 1 508 . 54 GLY HA3 H 4.0720 0.02 2 509 . 54 GLY HA2 H 4.0140 0.02 2 510 . 54 GLY CA C 45.2280 0.20 1 511 . 55 LYS N N 121.1260 0.20 1 512 . 55 LYS H H 8.9840 0.02 1 513 . 55 LYS HA H 5.1530 0.02 1 514 . 55 LYS HB2 H 1.6520 0.02 1 515 . 55 LYS HB3 H 1.6520 0.02 1 516 . 55 LYS HG3 H 1.2820 0.02 2 517 . 55 LYS HG2 H 1.2290 0.02 2 518 . 55 LYS HD2 H 1.6460 0.02 1 519 . 55 LYS HD3 H 1.6460 0.02 1 520 . 55 LYS HE2 H 2.9470 0.02 1 521 . 55 LYS HE3 H 2.9470 0.02 1 522 . 55 LYS CA C 53.1680 0.20 1 523 . 55 LYS CB C 34.2430 0.20 1 524 . 55 LYS CG C 23.9060 0.20 1 525 . 55 LYS CD C 28.4770 0.20 1 526 . 55 LYS CE C 41.0780 0.20 1 527 . 56 VAL N N 123.2930 0.20 1 528 . 56 VAL H H 9.2110 0.02 1 529 . 56 VAL HA H 3.8790 0.02 1 530 . 56 VAL HB H 2.3620 0.02 1 531 . 56 VAL HG1 H 0.8120 0.02 1 532 . 56 VAL HG2 H 0.6020 0.02 1 533 . 56 VAL CA C 62.7200 0.20 1 534 . 56 VAL CB C 29.8620 0.20 1 535 . 56 VAL CG1 C 20.8130 0.20 1 536 . 56 VAL CG2 C 21.4280 0.20 1 537 . 57 GLU N N 133.0060 0.20 1 538 . 57 GLU H H 9.0090 0.02 1 539 . 57 GLU HA H 4.2990 0.02 1 540 . 57 GLU HG3 H 2.2970 0.02 2 541 . 57 GLU HG2 H 2.0870 0.02 2 542 . 57 GLU HB3 H 1.9030 0.02 1 543 . 57 GLU HB2 H 1.7250 0.02 1 544 . 57 GLU CA C 57.1300 0.20 1 545 . 57 GLU CB C 30.6570 0.20 1 546 . 57 GLU CG C 35.4920 0.20 1 547 . 58 LYS N N 113.7290 0.20 1 548 . 58 LYS H H 7.4720 0.02 1 549 . 58 LYS HA H 4.6160 0.02 1 550 . 58 LYS HD2 H 1.7040 0.02 1 551 . 58 LYS HD3 H 1.7040 0.02 1 552 . 58 LYS HB2 H 1.6540 0.02 1 553 . 58 LYS HB3 H 1.6540 0.02 1 554 . 58 LYS HG2 H 1.3280 0.02 1 555 . 58 LYS HG3 H 1.3280 0.02 1 556 . 58 LYS HE2 H 2.9460 0.02 1 557 . 58 LYS HE3 H 2.9460 0.02 1 558 . 58 LYS CA C 54.3930 0.20 1 559 . 58 LYS CB C 36.6240 0.20 1 560 . 58 LYS CG C 24.1950 0.20 1 561 . 58 LYS CD C 28.0030 0.20 1 562 . 58 LYS CE C 41.3010 0.20 1 563 . 59 VAL N N 128.2390 0.20 1 564 . 59 VAL H H 9.7090 0.02 1 565 . 59 VAL HA H 4.1710 0.02 1 566 . 59 VAL HB H 2.2560 0.02 1 567 . 59 VAL HG1 H 1.2700 0.02 2 568 . 59 VAL HG2 H 0.8300 0.02 2 569 . 59 VAL CA C 62.7830 0.20 1 570 . 59 VAL CB C 30.9980 0.20 1 571 . 59 VAL CG2 C 20.5640 0.20 1 572 . 59 VAL CG1 C 21.4070 0.20 1 573 . 60 LEU N N 125.5330 0.20 1 574 . 60 LEU H H 8.0630 0.02 1 575 . 60 LEU HA H 4.2830 0.02 1 576 . 60 LEU HB3 H 1.6780 0.02 1 577 . 60 LEU HB2 H 1.5590 0.02 1 578 . 60 LEU HG H 1.2700 0.02 1 579 . 60 LEU HD1 H 0.7480 0.02 2 580 . 60 LEU HD2 H 0.5790 0.02 2 581 . 60 LEU CA C 56.2070 0.20 1 582 . 60 LEU CB C 41.0300 0.20 1 583 . 60 LEU CG C 27.3430 0.20 1 584 . 60 LEU CD1 C 22.9010 0.20 1 585 . 60 LEU CD2 C 23.8970 0.20 1 586 . 61 VAL N N 109.0350 0.20 1 587 . 61 VAL H H 7.0220 0.02 1 588 . 61 VAL HA H 4.7140 0.02 1 589 . 61 VAL HB H 2.3480 0.02 1 590 . 61 VAL HG1 H 1.0110 0.02 1 591 . 61 VAL HG2 H 0.7870 0.02 1 592 . 61 VAL CA C 57.7550 0.20 1 593 . 61 VAL CB C 35.3780 0.20 1 594 . 61 VAL CG1 C 21.7850 0.20 1 595 . 61 VAL CG2 C 16.7540 0.20 1 596 . 62 LYS N N 118.3250 0.20 1 597 . 62 LYS H H 8.5760 0.02 1 598 . 62 LYS HA H 4.5460 0.02 1 599 . 62 LYS HB2 H 1.7390 0.02 1 600 . 62 LYS HB3 H 1.7390 0.02 1 601 . 62 LYS HG3 H 1.4780 0.02 2 602 . 62 LYS HG2 H 1.3950 0.02 2 603 . 62 LYS HD2 H 1.3870 0.02 1 604 . 62 LYS HD3 H 1.3870 0.02 1 605 . 62 LYS HE2 H 3.0560 0.02 1 606 . 62 LYS HE3 H 3.0560 0.02 1 607 . 62 LYS CA C 53.3640 0.20 1 608 . 62 LYS CB C 34.5440 0.20 1 609 . 62 LYS CG C 23.5940 0.20 1 610 . 62 LYS CD C 28.1600 0.20 1 611 . 62 LYS CE C 41.0040 0.20 1 612 . 63 GLU N N 120.1800 0.20 1 613 . 63 GLU H H 8.7510 0.02 1 614 . 63 GLU HA H 3.5640 0.02 1 615 . 63 GLU HG3 H 2.3160 0.02 2 616 . 63 GLU HG2 H 2.1070 0.02 2 617 . 63 GLU HB2 H 1.9300 0.02 1 618 . 63 GLU HB3 H 1.9300 0.02 1 619 . 63 GLU CA C 58.7040 0.20 1 620 . 63 GLU CB C 28.5110 0.20 1 621 . 63 GLU CG C 37.2100 0.20 1 622 . 64 ARG N N 115.1980 0.20 1 623 . 64 ARG H H 9.2330 0.02 1 624 . 64 ARG HA H 3.6510 0.02 1 625 . 64 ARG HB2 H 2.4340 0.02 2 626 . 64 ARG HB3 H 2.1210 0.02 2 627 . 64 ARG HG3 H 1.7380 0.02 2 628 . 64 ARG HG2 H 1.6470 0.02 2 629 . 64 ARG HD2 H 3.2220 0.02 2 630 . 64 ARG HD3 H 3.2910 0.02 2 631 . 64 ARG HE H 7.2900 0.02 1 632 . 64 ARG NE N 83.7000 0.20 1 633 . 64 ARG CA C 57.4880 0.20 1 634 . 64 ARG CB C 26.1010 0.20 1 635 . 64 ARG CG C 26.2530 0.20 1 636 . 64 ARG CD C 41.9460 0.20 1 637 . 65 ASP N N 121.1180 0.20 1 638 . 65 ASP H H 8.0640 0.02 1 639 . 65 ASP HA H 4.5790 0.02 1 640 . 65 ASP HB2 H 2.9010 0.02 2 641 . 65 ASP HB3 H 2.4870 0.02 2 642 . 65 ASP CA C 54.7270 0.20 1 643 . 65 ASP CB C 40.1040 0.20 1 644 . 66 ALA N N 124.4770 0.20 1 645 . 66 ALA H H 8.5710 0.02 1 646 . 66 ALA HA H 4.9850 0.02 1 647 . 66 ALA HB H 1.4180 0.02 1 648 . 66 ALA CA C 50.6220 0.20 1 649 . 66 ALA CB C 18.3640 0.20 1 650 . 67 VAL N N 115.6860 0.20 1 651 . 67 VAL H H 9.0850 0.02 1 652 . 67 VAL HA H 4.9700 0.02 1 653 . 67 VAL HB H 1.8800 0.02 1 654 . 67 VAL HG1 H 0.7490 0.02 1 655 . 67 VAL HG2 H 0.6790 0.02 1 656 . 67 VAL CA C 57.5040 0.20 1 657 . 67 VAL CB C 34.1910 0.20 1 658 . 67 VAL CG1 C 21.4700 0.20 1 659 . 67 VAL CG2 C 18.3290 0.20 1 660 . 68 GLN N N 120.3950 0.20 1 661 . 68 GLN H H 8.2280 0.02 1 662 . 68 GLN HA H 4.5610 0.02 1 663 . 68 GLN HG2 H 2.4300 0.02 1 664 . 68 GLN HG3 H 2.4300 0.02 1 665 . 68 GLN HB3 H 2.1880 0.02 1 666 . 68 GLN HB2 H 1.8370 0.02 1 667 . 68 GLN HE21 H 6.8310 0.02 1 668 . 68 GLN HE22 H 7.6310 0.02 1 669 . 68 GLN NE2 N 112.6580 0.20 1 670 . 68 GLN CA C 52.4890 0.20 1 671 . 68 GLN CB C 30.4790 0.20 1 672 . 68 GLN CG C 32.9730 0.20 1 673 . 69 GLY N N 107.1110 0.20 1 674 . 69 GLY H H 8.5660 0.02 1 675 . 69 GLY HA3 H 3.5860 0.02 2 676 . 69 GLY HA2 H 3.1810 0.02 2 677 . 69 GLY CA C 45.3950 0.20 1 678 . 70 GLY N N 114.2160 0.20 1 679 . 70 GLY H H 9.3250 0.02 1 680 . 70 GLY HA3 H 4.3630 0.02 2 681 . 70 GLY HA2 H 3.5550 0.02 2 682 . 70 GLY CA C 44.3710 0.20 1 683 . 71 GLN N N 122.2890 0.20 1 684 . 71 GLN H H 7.8500 0.02 1 685 . 71 GLN HA H 4.1530 0.02 1 686 . 71 GLN HB3 H 2.2010 0.02 1 687 . 71 GLN HB2 H 1.9390 0.02 1 688 . 71 GLN HG2 H 2.4530 0.02 1 689 . 71 GLN HG3 H 2.4530 0.02 1 690 . 71 GLN HE21 H 7.3980 0.02 1 691 . 71 GLN HE22 H 7.6610 0.02 1 692 . 71 GLN NE2 N 111.0830 0.20 1 693 . 71 GLN CA C 55.5310 0.20 1 694 . 71 GLN CB C 29.5450 0.20 1 695 . 71 GLN CG C 32.0240 0.20 1 696 . 72 GLY N N 112.8230 0.20 1 697 . 72 GLY H H 9.0330 0.02 1 698 . 72 GLY HA2 H 3.7180 0.02 1 699 . 72 GLY HA3 H 3.7180 0.02 1 700 . 72 GLY CA C 45.9140 0.20 1 701 . 73 LEU N N 121.0100 0.20 1 702 . 73 LEU H H 8.8820 0.02 1 703 . 73 LEU HA H 4.6690 0.02 1 704 . 73 LEU HG H 2.1680 0.02 1 705 . 73 LEU HB2 H 1.8070 0.02 1 706 . 73 LEU HB3 H 1.3600 0.02 1 707 . 73 LEU HD1 H 0.8430 0.02 2 708 . 73 LEU HD2 H 0.8050 0.02 2 709 . 73 LEU CA C 55.2000 0.20 1 710 . 73 LEU CB C 43.8590 0.20 1 711 . 73 LEU CG C 25.5630 0.20 1 712 . 73 LEU CD1 C 26.0310 0.20 1 713 . 73 LEU CD2 C 23.2680 0.20 1 714 . 74 ILE N N 113.9870 0.20 1 715 . 74 ILE H H 6.7590 0.02 1 716 . 74 ILE HA H 4.6280 0.02 1 717 . 74 ILE HB H 1.6880 0.02 1 718 . 74 ILE HG13 H 1.0950 0.02 2 719 . 74 ILE HG2 H 0.8880 0.02 1 720 . 74 ILE HD1 H 0.7860 0.02 1 721 . 74 ILE HG12 H 1.6100 0.02 2 722 . 74 ILE CA C 58.2080 0.20 1 723 . 74 ILE CB C 42.8790 0.20 1 724 . 74 ILE CG1 C 27.3270 0.20 1 725 . 74 ILE CG2 C 17.1810 0.20 1 726 . 74 ILE CD1 C 13.5840 0.20 1 727 . 75 LYS N N 128.2430 0.20 1 728 . 75 LYS H H 9.3120 0.02 1 729 . 75 LYS HA H 4.9410 0.02 1 730 . 75 LYS HB3 H 1.9010 0.02 2 731 . 75 LYS HB2 H 1.5820 0.02 2 732 . 75 LYS HG3 H 1.3400 0.02 2 733 . 75 LYS HG2 H 1.2960 0.02 2 734 . 75 LYS HD3 H 1.7460 0.02 2 735 . 75 LYS HD2 H 1.5800 0.02 2 736 . 75 LYS HE2 H 3.0720 0.02 1 737 . 75 LYS HE3 H 3.0720 0.02 1 738 . 75 LYS CA C 54.4560 0.20 1 739 . 75 LYS CB C 35.3400 0.20 1 740 . 75 LYS CG C 24.8260 0.20 1 741 . 75 LYS CD C 28.6470 0.20 1 742 . 75 LYS CE C 41.4990 0.20 1 743 . 76 ILE N N 129.6790 0.20 1 744 . 76 ILE H H 8.7460 0.02 1 745 . 76 ILE HA H 4.9900 0.02 1 746 . 76 ILE HB H 1.8380 0.02 1 747 . 76 ILE HG13 H 1.1500 0.02 2 748 . 76 ILE HG12 H 1.5160 0.02 2 749 . 76 ILE HG2 H 0.7480 0.02 1 750 . 76 ILE HD1 H 0.7360 0.02 1 751 . 76 ILE CA C 57.9600 0.20 1 752 . 76 ILE CB C 38.5320 0.20 1 753 . 76 ILE CG1 C 26.7260 0.20 1 754 . 76 ILE CG2 C 16.3530 0.20 1 755 . 76 ILE CD1 C 12.0170 0.20 1 756 . 77 GLY N N 121.6450 0.20 1 757 . 77 GLY H H 9.0910 0.02 1 758 . 77 GLY HA3 H 4.2360 0.02 2 759 . 77 GLY HA2 H 3.6910 0.02 2 760 . 77 GLY CA C 45.4580 0.20 2 stop_ save_ ######################## # Coupling constants # ######################## save_coupling_constants _Saveframe_category coupling_constants _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Spectrometer_frequency_1H 600 _Mol_system_component_name 'transcarboxylase 1.3S subunit' _Text_data_format . _Text_data . loop_ _Coupling_constant_ID _Coupling_constant_code _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_name _Coupling_constant_value _Coupling_constant_min_value _Coupling_constant_max_value _Coupling_constant_value_error 1 3JHNHA 10 GLU H 10 GLU HA 7.4 . . 1.0 2 3JHNHA 11 ILE H 11 ILE HA 6.7 . . 1.0 3 3JHNHA 15 LEU H 15 LEU HA 6.2 . . 1.0 4 3JHNHA 18 THR H 18 THR HA 9.4 . . 1.0 5 3JHNHA 19 VAL H 19 VAL HA 5.8 . . 1.0 6 3JHNHA 20 SER H 20 SER HA 9.3 . . 1.0 7 3JHNHA 21 LYS H 21 LYS HA 8.2 . . 1.0 8 3JHNHA 22 ILE H 22 ILE HA 9.5 . . 1.0 9 3JHNHA 23 LEU H 23 LEU HA 9.1 . . 1.0 10 3JHNHA 25 LYS H 25 LYS HA 9.6 . . 1.0 11 3JHNHA 29 THR H 29 THR HA 9.0 . . 1.0 12 3JHNHA 30 VAL H 30 VAL HA 10.2 . . 1.0 13 3JHNHA 31 LYS H 31 LYS HA 10.0 . . 1.0 14 3JHNHA 34 GLN H 34 GLN HA 4.4 . . 1.0 15 3JHNHA 35 THR H 35 THR HA 5.1 . . 1.0 16 3JHNHA 36 VAL H 36 VAL HA 10.4 . . 1.0 17 3JHNHA 37 LEU H 37 LEU HA 6.7 . . 1.0 18 3JHNHA 38 VAL H 38 VAL HA 9.2 . . 1.0 19 3JHNHA 39 LEU H 39 LEU HA 10.6 . . 1.0 20 3JHNHA 40 GLU H 40 GLU HA 9.3 . . 1.0 21 3JHNHA 41 ALA H 41 ALA HA 8.1 . . 1.0 22 3JHNHA 42 MET H 42 MET HA 7.1 . . 1.0 23 3JHNHA 43 LYS H 43 LYS HA 6.5 . . 1.0 24 3JHNHA 44 MET H 44 MET HA 9.3 . . 1.0 25 3JHNHA 46 THR H 46 THR HA 10.3 . . 1.0 26 3JHNHA 47 GLU H 47 GLU HA 7.6 . . 1.0 27 3JHNHA 48 ILE H 48 ILE HA 9.9 . . 1.0 28 3JHNHA 49 ASN H 49 ASN HA 8.9 . . 1.0 29 3JHNHA 50 ALA H 50 ALA HA 4.4 . . 1.0 30 3JHNHA 52 THR H 52 THR HA 8.5 . . 1.0 31 3JHNHA 53 ASP H 53 ASP HA 5.4 . . 1.0 32 3JHNHA 55 LYS H 55 LYS HA 9.7 . . 1.0 33 3JHNHA 56 VAL H 56 VAL HA 6.2 . . 1.0 34 3JHNHA 57 GLU H 57 GLU HA 8.4 . . 1.0 35 3JHNHA 58 LYS H 58 LYS HA 7.1 . . 1.0 36 3JHNHA 59 VAL H 59 VAL HA 9.2 . . 1.0 37 3JHNHA 60 LEU H 60 LEU HA 7.1 . . 1.0 38 3JHNHA 62 LYS H 62 LYS HA 10.1 . . 1.0 39 3JHNHA 64 ARG H 64 ARG HA 6.6 . . 1.0 40 3JHNHA 66 ALA H 66 ALA HA 8.2 . . 1.0 41 3JHNHA 67 VAL H 67 VAL HA 10.7 . . 1.0 42 3JHNHA 68 GLN H 68 GLN HA 8.9 . . 1.0 43 3JHNHA 71 GLN H 71 GLN HA 4.2 . . 1.0 44 3JHNHA 73 LEU H 73 LEU HA 8.1 . . 1.0 45 3JHNHA 74 ILE H 74 ILE HA 8.1 . . 1.0 46 3JHNHA 75 LYS H 75 LYS HA 8.9 . . 1.0 47 3JHNHA 76 ILE H 76 ILE HA 9.9 . . 1.0 stop_ save_