data_17846 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N chemical shift assignments of reduced yeast iso-1 cytochrome c ; _BMRB_accession_number 17846 _BMRB_flat_file_name bmr17846.str _Entry_type original _Submission_date 2011-08-09 _Accession_date 2011-08-09 _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 Volkov Alexander N. . 2 'Van de Water' Karen . . 3 Vanwetswinkel Sophie . . 4 'van Nuland' Nico 'A. J.' . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 238 "13C chemical shifts" 312 "15N chemical shifts" 221 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2012-03-14 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 17845 yCc 17847 hCc 17848 hCc 345 'proton assignements' 922 'proton assignements' stop_ _Original_release_date 2012-03-14 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Redox-dependent conformational changes in eukaryotic cytochromes revealed by paramagnetic NMR spectroscopy' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 22318343 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Volkov Alexander N. . 2 Vanwetswinkel Sophie . . 3 'Van de Water' Karen . . 4 'van Nuland' Nico 'A. J.' . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 52 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 245 _Page_last 256 _Year 2012 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name yCc _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label yCc $yCc HEC $HEC stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'electron transfer' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_yCc _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common yCc _Molecular_mass . _Mol_thiol_state 'all other bound' loop_ _Biological_function 'electron transfer' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 108 _Mol_residue_sequence ; AEFKAGSAKKGATLFKTRCL QCHTVEKGGPHKVGPNLHGI FGRHSGQAEGYSYTDANIKK NVLWDENNMSEYLTNPKKYI PGTKMAFGGLKKEKDRNDLI TYLKKATE ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -5 ALA 2 -4 GLU 3 -3 PHE 4 -2 LYS 5 -1 ALA 6 1 GLY 7 2 SER 8 3 ALA 9 4 LYS 10 5 LYS 11 6 GLY 12 7 ALA 13 8 THR 14 9 LEU 15 10 PHE 16 11 LYS 17 12 THR 18 13 ARG 19 14 CYS 20 15 LEU 21 16 GLN 22 17 CYS 23 18 HIS 24 19 THR 25 20 VAL 26 21 GLU 27 22 LYS 28 23 GLY 29 24 GLY 30 25 PRO 31 26 HIS 32 27 LYS 33 28 VAL 34 29 GLY 35 30 PRO 36 31 ASN 37 32 LEU 38 33 HIS 39 34 GLY 40 35 ILE 41 36 PHE 42 37 GLY 43 38 ARG 44 39 HIS 45 40 SER 46 41 GLY 47 42 GLN 48 43 ALA 49 44 GLU 50 45 GLY 51 46 TYR 52 47 SER 53 48 TYR 54 49 THR 55 50 ASP 56 51 ALA 57 52 ASN 58 53 ILE 59 54 LYS 60 55 LYS 61 56 ASN 62 57 VAL 63 58 LEU 64 59 TRP 65 60 ASP 66 61 GLU 67 62 ASN 68 63 ASN 69 64 MET 70 65 SER 71 66 GLU 72 67 TYR 73 68 LEU 74 69 THR 75 70 ASN 76 71 PRO 77 72 LYS 78 73 LYS 79 74 TYR 80 75 ILE 81 76 PRO 82 77 GLY 83 78 THR 84 79 LYS 85 80 MET 86 81 ALA 87 82 PHE 88 83 GLY 89 84 GLY 90 85 LEU 91 86 LYS 92 87 LYS 93 88 GLU 94 89 LYS 95 90 ASP 96 91 ARG 97 92 ASN 98 93 ASP 99 94 LEU 100 95 ILE 101 96 THR 102 97 TYR 103 98 LEU 104 99 LYS 105 100 LYS 106 101 ALA 107 102 THR 108 103 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-09-30 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 131 "cytochrome c" 99.07 108 99.07 99.07 9.45e-72 BMRB 15301 Cytc 99.07 108 99.07 99.07 1.84e-71 BMRB 1719 "cytochrome c" 99.07 108 97.20 97.20 4.85e-69 BMRB 1720 "cytochrome c" 99.07 108 97.20 97.20 4.85e-69 BMRB 17845 yCc 100.00 108 100.00 100.00 3.32e-73 BMRB 17903 Iso-1-cytochrome 99.07 108 98.13 98.13 2.66e-70 BMRB 17904 Iso-1-cytochrome 99.07 108 98.13 98.13 2.66e-70 BMRB 190 "cytochrome c" 99.07 108 97.20 97.20 4.85e-69 BMRB 19638 entity_1 99.07 108 98.13 99.07 4.86e-71 BMRB 345 "cytochrome c" 99.07 108 97.20 97.20 4.85e-69 BMRB 346 "cytochrome c" 99.07 108 97.20 97.20 4.85e-69 PDB 1CHH "Structural Studies Of The Roles Of Residues 82 And 85 At The Interactive Face Of Cytochrome C" 99.07 108 98.13 99.07 3.04e-71 PDB 1CHI "Structural Studies Of The Roles Of Residues 82 And 85 At The Interactive Face Of Cytochrome C" 99.07 108 97.20 98.13 1.82e-70 PDB 1CHJ "Structural Studies Of The Roles Of Residues 82 And 85 At The Interactive Face Of Cytochrome C" 99.07 108 98.13 98.13 6.31e-71 PDB 1CRG "The Role Of A Conserved Internal Water Molecule And Its Associated Hydrogen Bond Network In Cytochrome C" 99.07 108 98.13 98.13 1.49e-70 PDB 1CRH "The Role Of A Conserved Internal Water Molecule And Its Associated Hydrogen Bond Network In Cytochrome C" 99.07 108 97.20 97.20 1.41e-69 PDB 1CRI "The Role Of A Conserved Internal Water Molecule And Its Associated Hydrogen Bond Network In Cytochrome C" 99.07 108 97.20 98.13 4.60e-70 PDB 1CRJ "The Role Of A Conserved Internal Water Molecule And Its Associated Hydrogen Bond Network In Cytochrome C" 99.07 108 97.20 98.13 4.60e-70 PDB 1CSU "Replacements In A Conserved Leucine Cluster In The Hydrophobic Heme Pocket Of Cytochrome C" 99.07 108 98.13 98.13 8.29e-71 PDB 1CSV "Replacements In A Conserved Leucine Cluster In The Hydrophobic Heme Pocket Of Cytochrome C" 99.07 108 98.13 98.13 4.08e-71 PDB 1CSW "Replacements In A Conserved Leucine Cluster In The Hydrophobic Heme Pocket Of Cytochrome C" 99.07 108 98.13 99.07 1.72e-71 PDB 1CSX "Replacements In A Conserved Leucine Cluster In The Hydrophobic Heme Pocket Of Cytochrome C" 99.07 108 98.13 98.13 7.19e-71 PDB 1CTY "Mutation Of Tyrosine-67 In Cytochrome C Significantly Alters The Local Heme Environment" 99.07 108 98.13 99.07 2.78e-71 PDB 1CTZ "Mutation Of Tyrosine-67 In Cytochrome C Significantly Alters The Local Heme Environment" 99.07 108 98.13 99.07 2.78e-71 PDB 1IRV "Cytochrome C Isozyme 1, Reduced, Mutant With Ile 75 Replaced By Met And Cys 102 Replaced By Thr" 99.07 108 98.13 99.07 2.61e-71 PDB 1IRW "Cytochrome C Isozyme 1, Reduced, Mutant With Asn 52 Replaced By Ala And Cys 102 Replaced By Thr" 99.07 108 98.13 98.13 9.98e-71 PDB 1KYO "Yeast Cytochrome Bc1 Complex With Bound Substrate Cytochrome C" 99.07 108 98.13 98.13 8.11e-71 PDB 1LMS "Structural Model For An Alkaline Form Of Ferricytochrome C" 99.07 108 98.13 98.13 3.99e-71 PDB 1NMI "Solution Structure Of The Imidazole Complex Of Iso-1 Cytochrome C" 99.07 108 100.00 100.00 1.70e-72 PDB 1S6V "Structure Of A Cytochrome C Peroxidase-Cytochrome C Site Specific Cross-Link" 100.00 108 99.07 99.07 3.28e-72 PDB 1U74 "Electron Transfer Complex Between Cytochrome C And Cytochrome C Peroxidase" 99.07 108 99.07 100.00 3.70e-72 PDB 1YCC "High-Resolution Refinement Of Yeast Iso-1-Cytochrome C And Comparisons With Other Eukaryotic Cytochromes C" 99.07 108 98.13 98.13 8.11e-71 PDB 1YFC "Solution Nmr Structure Of A Yeast Iso-1-Ferrocytochrome C" 99.07 108 98.13 99.07 2.82e-71 PDB 1YIC "The Oxidized Saccharomyces Cerevisiae Iso-1-Cytochrome C, Nmr, 20 Structures" 99.07 108 98.13 99.07 2.31e-71 PDB 2B0Z "Crystal Structure Of The Protein-Protein Complex Between F82i Cytochrome C And Cytochrome C Peroxidase" 99.07 108 98.13 98.13 1.03e-70 PDB 2B10 "Crystal Structure Of The Protein-Protein Complex Between F82s Cytochrome C And Cytochrome C Peroxidase" 99.07 108 98.13 98.13 2.21e-70 PDB 2B11 "Crystal Structure Of The Protein-Protein Complex Between F82w Cytochrome C And Cytochrome C Peroxidase" 99.07 108 98.13 99.07 1.18e-70 PDB 2B12 "Crystal Structure Of The Protein-Protein Complex Between F82y Cytochrome C And Cytochrome C Peroxidase" 99.07 108 98.13 99.07 6.38e-71 PDB 2BCN "Solvent Isotope Effects On Interfacial Protein Electron Transfer Between Cytochrome C And Cytochrome C Peroxidase" 99.07 108 99.07 100.00 3.70e-72 PDB 2GB8 "Solution Structure Of The Complex Between Yeast Iso-1- Cytochrome C And Yeast Cytochrome C Peroxidase" 99.07 108 99.07 99.07 2.03e-71 PDB 2HV4 "Nmr Solution Structure Refinement Of Yeast Iso-1- Ferrocytochrome C" 99.07 108 100.00 100.00 1.70e-72 PDB 2JQR "Solution Model Of Crosslinked Complex Of Cytochrome C And Adrenodoxin" 99.07 108 99.07 99.07 1.84e-71 PDB 2JTI "Solution Structure Of The Yeast Iso-1-Cytochrome C (T12a) : Yeast Cytochrome C Peroxidase Complex" 99.07 108 98.13 98.13 9.45e-71 PDB 2LIR "Nmr Solution Structure Of Yeast Iso-1-Cytochrome C Mutant P71h In Oxidized States" 99.07 108 98.13 98.13 2.66e-70 PDB 2LIT "Nmr Solution Structure Of Yeast Iso-1-Cytochrome C Mutant P71h In Reduced States" 99.07 108 98.13 98.13 2.66e-70 PDB 2MHM "Solution Structure Of Cytochrome C Y67h" 99.07 108 98.13 99.07 4.86e-71 PDB 2N18 "Dominant Form Of The Low-affinity Complex Of Yeast Cytochrome C And Cytochrome C Peroxidase" 100.00 108 99.07 99.07 3.28e-72 PDB 2ORL "Solution Structure Of The Cytochrome C- Para-Aminophenol Adduct" 99.07 108 100.00 100.00 1.70e-72 PDB 2PCC "Crystal Structure Of A Complex Between Electron Transfer Partners, Cytochrome C Peroxidase And Cytochrome C" 99.07 108 99.07 99.07 2.03e-71 PDB 2YCC "Oxidation State-Dependent Conformational Changes In Cytochrome C" 99.07 108 99.07 99.07 9.45e-72 PDB 3CX5 "Structure Of Complex Iii With Bound Cytochrome C In Reduced State And Definition Of A Minimal Core Interface For Electron Trans" 99.07 108 98.13 98.13 8.11e-71 PDB 3TYI "Crystal Structure Of Cytochrome C - P-Sulfonatocalix[4]arene Complexes" 99.07 108 100.00 100.00 1.70e-72 PDB 4MU8 "Crystal Structure Of An Oxidized Form Of Yeast Iso-1-cytochrome C At Ph 8.8" 99.07 108 98.13 99.07 2.24e-71 PDB 4N0K "Atomic Resolution Crystal Structure Of A Cytochrome C-calixarene Complex" 99.07 108 99.07 99.07 1.63e-71 PDB 4P4Q "Complex Of Yeast Cytochrome C Peroxidase (w191f) With Iso-1 Cytochrome C" 95.37 103 99.03 99.03 1.85e-68 PDB 4YE1 "A Cytochrome C Plus Calixarene Structure - Alternative Ligand Binding Mode" 99.07 108 98.13 98.13 1.42e-70 DBJ GAA24396 "K7_Cyc1p [Saccharomyces cerevisiae Kyokai no. 7]" 99.07 109 99.07 99.07 1.49e-71 EMBL CAA24605 "unnamed protein product [Saccharomyces cerevisiae]" 99.07 109 99.07 99.07 1.49e-71 EMBL CAA89576 "CYC1 [Saccharomyces cerevisiae]" 99.07 109 99.07 99.07 1.49e-71 EMBL CAY80764 "Cyc1p [Saccharomyces cerevisiae EC1118]" 99.07 109 99.07 99.07 1.49e-71 GB AAA62856 "iso-1-cytochrome c [Saccharomyces cerevisiae]" 99.07 109 99.07 99.07 1.49e-71 GB AAA88751 "ORF; putative, partial [Saccharomyces cerevisiae]" 99.07 109 99.07 99.07 1.49e-71 GB AAB59344 "iso-1-cytochrome c [Saccharomyces cerevisiae]" 99.07 109 99.07 99.07 1.49e-71 GB AHY79034 "Cyc1p [Saccharomyces cerevisiae YJM993]" 99.07 109 99.07 99.07 1.49e-71 GB AJP39735 "Cyc1p [Saccharomyces cerevisiae YJM1078]" 99.07 109 99.07 99.07 1.49e-71 PRF 1409323A "CYC1 locus" 99.07 109 99.07 99.07 1.49e-71 REF NP_012582 "cytochrome c isoform 1 [Saccharomyces cerevisiae S288c]" 99.07 109 99.07 99.07 1.49e-71 SP P00044 "RecName: Full=Cytochrome c iso-1" 99.07 109 99.07 99.07 1.49e-71 TPG DAA08835 "TPA: cytochrome c isoform 1 [Saccharomyces cerevisiae S288c]" 99.07 109 99.07 99.07 1.49e-71 stop_ save_ ############# # Ligands # ############# save_HEC _Saveframe_category ligand _Mol_type non-polymer _Name_common "HEC (HEME C)" _BMRB_code . _PDB_code HEC _Molecular_mass 618.503 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic yes _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Wed Aug 10 10:52:32 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons FE FE FE . 0 . ? CHA CHA C . 0 . ? CHB CHB C . 0 . ? CHC CHC C . 0 . ? CHD CHD C . 0 . ? NA NA N . 0 . ? C1A C1A C . 0 . ? C2A C2A C . 0 . ? C3A C3A C . 0 . ? C4A C4A C . 0 . ? CMA CMA C . 0 . ? CAA CAA C . 0 . ? CBA CBA C . 0 . ? CGA CGA C . 0 . ? O1A O1A O . 0 . ? O2A O2A O . 0 . ? NB NB N . 0 . ? C1B C1B C . 0 . ? C2B C2B C . 0 . ? C3B C3B C . 0 . ? C4B C4B C . 0 . ? CMB CMB C . 0 . ? CAB CAB C . 0 . ? CBB CBB C . 0 . ? NC NC N . 0 . ? C1C C1C C . 0 . ? C2C C2C C . 0 . ? C3C C3C C . 0 . ? C4C C4C C . 0 . ? CMC CMC C . 0 . ? CAC CAC C . 0 . ? CBC CBC C . 0 . ? ND ND N . 0 . ? C1D C1D C . 0 . ? C2D C2D C . 0 . ? C3D C3D C . 0 . ? C4D C4D C . 0 . ? CMD CMD C . 0 . ? CAD CAD C . 0 . ? CBD CBD C . 0 . ? CGD CGD C . 0 . ? O1D O1D O . 0 . ? O2D O2D O . 0 . ? HHA HHA H . 0 . ? HHB HHB H . 0 . ? HHC HHC H . 0 . ? HHD HHD H . 0 . ? HMA1 HMA1 H . 0 . ? HMA2 HMA2 H . 0 . ? HMA3 HMA3 H . 0 . ? HAA1 HAA1 H . 0 . ? HAA2 HAA2 H . 0 . ? HBA1 HBA1 H . 0 . ? HBA2 HBA2 H . 0 . ? H2A H2A H . 0 . ? HMB1 HMB1 H . 0 . ? HMB2 HMB2 H . 0 . ? HMB3 HMB3 H . 0 . ? HAB HAB H . 0 . ? HBB1 HBB1 H . 0 . ? HBB2 HBB2 H . 0 . ? HBB3 HBB3 H . 0 . ? HMC1 HMC1 H . 0 . ? HMC2 HMC2 H . 0 . ? HMC3 HMC3 H . 0 . ? HAC HAC H . 0 . ? HBC1 HBC1 H . 0 . ? HBC2 HBC2 H . 0 . ? HBC3 HBC3 H . 0 . ? HMD1 HMD1 H . 0 . ? HMD2 HMD2 H . 0 . ? HMD3 HMD3 H . 0 . ? HAD1 HAD1 H . 0 . ? HAD2 HAD2 H . 0 . ? HBD1 HBD1 H . 0 . ? HBD2 HBD2 H . 0 . ? H2D H2D H . 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 FE NA ? ? SING FE NB ? ? SING FE NC ? ? SING FE ND ? ? DOUB CHA C1A ? ? SING CHA C4D ? ? SING CHA HHA ? ? DOUB CHB C4A ? ? SING CHB C1B ? ? SING CHB HHB ? ? DOUB CHC C4B ? ? SING CHC C1C ? ? SING CHC HHC ? ? DOUB CHD C4C ? ? SING CHD C1D ? ? SING CHD HHD ? ? SING NA C1A ? ? SING NA C4A ? ? SING C1A C2A ? ? DOUB C2A C3A ? ? SING C2A CAA ? ? SING C3A C4A ? ? SING C3A CMA ? ? SING CMA HMA1 ? ? SING CMA HMA2 ? ? SING CMA HMA3 ? ? SING CAA CBA ? ? SING CAA HAA1 ? ? SING CAA HAA2 ? ? SING CBA CGA ? ? SING CBA HBA1 ? ? SING CBA HBA2 ? ? DOUB CGA O1A ? ? SING CGA O2A ? ? SING O2A H2A ? ? SING NB C1B ? ? SING NB C4B ? ? DOUB C1B C2B ? ? SING C2B C3B ? ? SING C2B CMB ? ? SING C3B C4B ? ? DOUB C3B CAB ? ? SING CMB HMB1 ? ? SING CMB HMB2 ? ? SING CMB HMB3 ? ? SING CAB CBB ? ? SING CAB HAB ? ? SING CBB HBB1 ? ? SING CBB HBB2 ? ? SING CBB HBB3 ? ? SING NC C1C ? ? SING NC C4C ? ? DOUB C1C C2C ? ? SING C2C C3C ? ? SING C2C CMC ? ? SING C3C C4C ? ? DOUB C3C CAC ? ? SING CMC HMC1 ? ? SING CMC HMC2 ? ? SING CMC HMC3 ? ? SING CAC CBC ? ? SING CAC HAC ? ? SING CBC HBC1 ? ? SING CBC HBC2 ? ? SING CBC HBC3 ? ? SING ND C1D ? ? SING ND C4D ? ? DOUB C1D C2D ? ? SING C2D C3D ? ? SING C2D CMD ? ? DOUB C3D C4D ? ? SING C3D CAD ? ? SING CMD HMD1 ? ? SING CMD HMD2 ? ? SING CMD HMD3 ? ? SING CAD CBD ? ? SING CAD HAD1 ? ? SING CAD HAD2 ? ? SING CBD CGD ? ? SING CBD HBD1 ? ? SING CBD HBD2 ? ? DOUB CGD O1D ? ? SING CGD O2D ? ? SING O2D H2D ? ? 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 _Gene_mnemonic $yCc 'baker's yeast' 4932 Eukaryota Fungi Saccharomyces cerevisiae CYC1 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 $yCc 'recombinant technology' . Escherichia coli . pUCcc 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 $yCc 1 mM '[U-100% 13C; U-100% 15N]' 'sodium phosphate' 20 mM 'natural abundance' 'sodium chloride' 100 mM 'natural abundance' H2O 95 % 'natural abundance' D2O 5 % 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $yCc 1 mM '[U-100% 13C; U-100% 15N]' 'sodium phosphate' 20 mM 'natural abundance' H2O 95 % 'natural abundance' D2O 5 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_Analysis _Saveframe_category software _Name Analysis _Version . loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model 'Uniform NMR System' _Field_strength 800 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model 'Uniform NMR System' _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_2 save_ save_3D_NOESY-HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NOESY-HSQC' _Sample_label $sample_2 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 115 . mM pH 6.0 . pH pressure 1 . atm temperature 303 . K stop_ save_ save_sample_conditions_2 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 15 . mM pH 6.0 . pH pressure 1 . atm temperature 303 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_yCc_red_high_salt _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCACB' '3D CBCA(CO)NH' '3D HNCO' 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 yCc _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 -5 1 ALA C C 173.29 0.4 1 2 -5 1 ALA CA C 51.90 0.4 1 3 -5 1 ALA CB C 19.50 0.4 1 4 -4 2 GLU H H 8.70 0.04 1 5 -4 2 GLU C C 175.52 0.4 1 6 -4 2 GLU CA C 55.98 0.4 1 7 -4 2 GLU CB C 30.82 0.4 1 8 -4 2 GLU N N 120.52 0.2 1 9 -3 3 PHE H H 8.77 0.04 1 10 -3 3 PHE C C 174.53 0.4 1 11 -3 3 PHE CA C 58.88 0.4 1 12 -3 3 PHE CB C 39.82 0.4 1 13 -3 3 PHE N N 124.71 0.2 1 14 -2 4 LYS H H 6.56 0.04 1 15 -2 4 LYS C C 173.09 0.4 1 16 -2 4 LYS CA C 54.51 0.4 1 17 -2 4 LYS CB C 34.82 0.4 1 18 -2 4 LYS N N 127.74 0.2 1 19 -1 5 ALA H H 7.77 0.04 1 20 -1 5 ALA C C 178.44 0.4 1 21 -1 5 ALA CA C 53.41 0.4 1 22 -1 5 ALA CB C 18.67 0.4 1 23 -1 5 ALA N N 122.75 0.2 1 24 1 6 GLY H H 8.29 0.04 1 25 1 6 GLY C C 173.14 0.4 1 26 1 6 GLY CA C 43.85 0.4 1 27 1 6 GLY N N 111.02 0.2 1 28 2 7 SER H H 9.58 0.04 1 29 2 7 SER C C 175.45 0.4 1 30 2 7 SER CA C 55.47 0.4 1 31 2 7 SER CB C 63.17 0.4 1 32 2 7 SER N N 120.33 0.2 1 33 3 8 ALA H H 9.34 0.04 1 34 3 8 ALA C C 179.60 0.4 1 35 3 8 ALA CA C 55.33 0.4 1 36 3 8 ALA CB C 18.20 0.4 1 37 3 8 ALA N N 132.01 0.2 1 38 4 9 LYS H H 8.23 0.04 1 39 4 9 LYS C C 179.30 0.4 1 40 4 9 LYS CA C 59.69 0.4 1 41 4 9 LYS CB C 32.52 0.4 1 42 4 9 LYS N N 119.16 0.2 1 43 5 10 LYS H H 7.80 0.04 1 44 5 10 LYS C C 180.66 0.4 1 45 5 10 LYS CA C 58.40 0.4 1 46 5 10 LYS CB C 32.26 0.4 1 47 5 10 LYS N N 120.18 0.2 1 48 6 11 GLY H H 8.84 0.04 1 49 6 11 GLY C C 174.27 0.4 1 50 6 11 GLY CA C 47.25 0.4 1 51 6 11 GLY N N 107.99 0.2 1 52 7 12 ALA H H 8.11 0.04 1 53 7 12 ALA C C 180.60 0.4 1 54 7 12 ALA CA C 54.79 0.4 1 55 7 12 ALA CB C 18.67 0.4 1 56 7 12 ALA N N 125.27 0.2 1 57 8 13 THR H H 7.29 0.04 1 58 8 13 THR C C 177.40 0.4 1 59 8 13 THR CA C 66.35 0.4 1 60 8 13 THR CB C 68.59 0.4 1 61 8 13 THR N N 115.70 0.2 1 62 9 14 LEU H H 8.07 0.04 1 63 9 14 LEU C C 178.04 0.4 1 64 9 14 LEU CA C 58.40 0.4 1 65 9 14 LEU CB C 43.27 0.4 1 66 9 14 LEU N N 124.14 0.2 1 67 10 15 PHE H H 8.89 0.04 1 68 10 15 PHE C C 178.57 0.4 1 69 10 15 PHE CA C 62.83 0.4 1 70 10 15 PHE CB C 40.12 0.4 1 71 10 15 PHE N N 120.73 0.2 1 72 11 16 LYS H H 8.36 0.04 1 73 11 16 LYS C C 177.87 0.4 1 74 11 16 LYS CA C 59.89 0.4 1 75 11 16 LYS CB C 32.70 0.4 1 76 11 16 LYS N N 119.96 0.2 1 77 12 17 THR H H 8.02 0.04 1 78 12 17 THR C C 176.76 0.4 1 79 12 17 THR CA C 63.95 0.4 1 80 12 17 THR CB C 70.63 0.4 1 81 12 17 THR N N 107.89 0.2 1 82 13 18 ARG H H 8.63 0.04 1 83 13 18 ARG C C 177.36 0.4 1 84 13 18 ARG CA C 56.05 0.4 1 85 13 18 ARG CB C 32.27 0.4 1 86 13 18 ARG N N 117.13 0.2 1 87 14 19 CYS H H 8.09 0.04 1 88 14 19 CYS C C 176.56 0.4 1 89 14 19 CYS CA C 54.87 0.4 1 90 14 19 CYS CB C 37.06 0.4 1 91 14 19 CYS N N 115.44 0.2 1 92 15 20 LEU H H 7.26 0.04 1 93 15 20 LEU C C 175.89 0.4 1 94 15 20 LEU CA C 56.37 0.4 1 95 15 20 LEU CB C 43.00 0.4 1 96 15 20 LEU N N 121.69 0.2 1 97 16 21 GLN H H 8.88 0.04 1 98 16 21 GLN HE21 H 7.06 0.04 2 99 16 21 GLN HE22 H 7.63 0.04 2 100 16 21 GLN C C 176.24 0.4 1 101 16 21 GLN CA C 58.34 0.4 1 102 16 21 GLN CB C 28.35 0.4 1 103 16 21 GLN CG C 33.44 0.4 1 104 16 21 GLN CD C 180.47 0.4 1 105 16 21 GLN N N 115.89 0.2 1 106 16 21 GLN NE2 N 111.59 0.2 1 107 17 22 CYS H H 7.02 0.04 1 108 17 22 CYS C C 172.19 0.4 1 109 17 22 CYS CA C 54.11 0.4 1 110 17 22 CYS CB C 38.95 0.4 1 111 17 22 CYS N N 112.75 0.2 1 112 18 23 HIS H H 6.55 0.04 1 113 18 23 HIS C C 172.61 0.4 1 114 18 23 HIS CA C 54.02 0.4 1 115 18 23 HIS CB C 32.55 0.4 1 116 18 23 HIS N N 115.90 0.2 1 117 19 24 THR H H 7.21 0.04 1 118 19 24 THR C C 174.89 0.4 1 119 19 24 THR CA C 58.91 0.4 1 120 19 24 THR CB C 71.84 0.4 1 121 19 24 THR N N 105.78 0.2 1 122 20 25 VAL H H 7.49 0.04 1 123 20 25 VAL C C 174.60 0.4 1 124 20 25 VAL CA C 61.26 0.4 1 125 20 25 VAL CB C 33.61 0.4 1 126 20 25 VAL N N 108.82 0.2 1 127 21 26 GLU H H 8.85 0.04 1 128 21 26 GLU CA C 57.21 0.4 1 129 21 26 GLU CB C 29.75 0.4 1 130 21 26 GLU N N 120.41 0.2 1 131 22 27 LYS H H 8.70 0.04 1 132 22 27 LYS C C 177.50 0.4 1 133 22 27 LYS CA C 58.27 0.4 1 134 22 27 LYS CB C 31.53 0.4 1 135 22 27 LYS N N 125.54 0.2 1 136 23 28 GLY H H 9.26 0.04 1 137 23 28 GLY C C 174.53 0.4 1 138 23 28 GLY CA C 45.20 0.4 1 139 23 28 GLY N N 118.05 0.2 1 140 24 29 GLY H H 7.83 0.04 1 141 24 29 GLY CA C 44.05 0.4 1 142 24 29 GLY N N 108.22 0.2 1 143 25 30 PRO C C 178.64 0.4 1 144 25 30 PRO CA C 62.02 0.4 1 145 25 30 PRO CB C 31.77 0.4 1 146 26 31 HIS H H 8.41 0.04 1 147 26 31 HIS C C 175.39 0.4 1 148 26 31 HIS CA C 55.36 0.4 1 149 26 31 HIS CB C 30.57 0.4 1 150 26 31 HIS N N 121.09 0.2 1 151 27 32 LYS H H 7.71 0.04 1 152 27 32 LYS C C 175.88 0.4 1 153 27 32 LYS CA C 55.96 0.4 1 154 27 32 LYS CB C 31.68 0.4 1 155 27 32 LYS N N 125.34 0.2 1 156 28 33 VAL H H 7.05 0.04 1 157 28 33 VAL C C 177.93 0.4 1 158 28 33 VAL CA C 66.43 0.4 1 159 28 33 VAL CB C 34.27 0.4 1 160 28 33 VAL N N 121.95 0.2 1 161 29 34 GLY H H 7.70 0.04 1 162 29 34 GLY CA C 41.41 0.4 1 163 29 34 GLY N N 106.26 0.2 1 164 30 35 PRO C C 176.64 0.4 1 165 30 35 PRO CA C 60.03 0.4 1 166 30 35 PRO CB C 30.35 0.4 1 167 31 36 ASN H H 10.82 0.04 1 168 31 36 ASN HD21 H 7.45 0.04 2 169 31 36 ASN HD22 H 7.88 0.04 2 170 31 36 ASN C C 176.13 0.4 1 171 31 36 ASN CA C 54.89 0.4 1 172 31 36 ASN CB C 40.24 0.4 1 173 31 36 ASN N N 124.82 0.2 1 174 31 36 ASN ND2 N 115.23 0.2 1 175 32 37 LEU H H 7.80 0.04 1 176 32 37 LEU C C 175.55 0.4 1 177 32 37 LEU CA C 53.51 0.4 1 178 32 37 LEU CB C 43.52 0.4 1 179 32 37 LEU N N 121.50 0.2 1 180 33 38 HIS H H 7.48 0.04 1 181 33 38 HIS C C 177.40 0.4 1 182 33 38 HIS CA C 59.86 0.4 1 183 33 38 HIS CB C 27.81 0.4 1 184 33 38 HIS N N 118.58 0.2 1 185 34 39 GLY H H 9.10 0.04 1 186 34 39 GLY C C 175.12 0.4 1 187 34 39 GLY CA C 46.12 0.4 1 188 34 39 GLY N N 116.09 0.2 1 189 35 40 ILE H H 7.21 0.04 1 190 35 40 ILE C C 174.08 0.4 1 191 35 40 ILE CA C 61.53 0.4 1 192 35 40 ILE CB C 38.01 0.4 1 193 35 40 ILE N N 117.42 0.2 1 194 36 41 PHE H H 8.02 0.04 1 195 36 41 PHE C C 177.11 0.4 1 196 36 41 PHE CA C 60.90 0.4 1 197 36 41 PHE CB C 36.74 0.4 1 198 36 41 PHE N N 116.33 0.2 1 199 37 42 GLY H H 8.79 0.04 1 200 37 42 GLY C C 173.56 0.4 1 201 37 42 GLY CA C 44.97 0.4 1 202 37 42 GLY N N 110.44 0.2 1 203 38 43 ARG H H 8.12 0.04 1 204 38 43 ARG C C 175.03 0.4 1 205 38 43 ARG CA C 54.77 0.4 1 206 38 43 ARG CB C 33.07 0.4 1 207 38 43 ARG N N 121.26 0.2 1 208 39 44 HIS H H 7.97 0.04 1 209 39 44 HIS C C 176.45 0.4 1 210 39 44 HIS CA C 55.37 0.4 1 211 39 44 HIS CB C 30.35 0.4 1 212 39 44 HIS N N 116.51 0.2 1 213 40 45 SER H H 8.71 0.04 1 214 40 45 SER C C 175.45 0.4 1 215 40 45 SER CA C 59.20 0.4 1 216 40 45 SER CB C 62.29 0.4 1 217 40 45 SER N N 116.21 0.2 1 218 41 46 GLY H H 8.23 0.04 1 219 41 46 GLY C C 177.09 0.4 1 220 41 46 GLY CA C 47.22 0.4 1 221 41 46 GLY N N 113.18 0.2 1 222 42 47 GLN H H 8.22 0.04 1 223 42 47 GLN HE21 H 6.82 0.04 2 224 42 47 GLN HE22 H 7.55 0.04 2 225 42 47 GLN CA C 55.44 0.4 1 226 42 47 GLN CB C 30.89 0.4 1 227 42 47 GLN CG C 34.10 0.4 1 228 42 47 GLN CD C 181.02 0.4 1 229 42 47 GLN N N 114.35 0.2 1 230 42 47 GLN NE2 N 112.81 0.2 1 231 43 48 ALA H H 8.72 0.04 1 232 43 48 ALA C C 178.45 0.4 1 233 43 48 ALA CA C 54.07 0.4 1 234 43 48 ALA CB C 18.85 0.4 1 235 43 48 ALA N N 125.55 0.2 1 236 44 49 GLU H H 8.80 0.04 1 237 44 49 GLU C C 178.82 0.4 1 238 44 49 GLU CA C 57.83 0.4 1 239 44 49 GLU CB C 29.93 0.4 1 240 44 49 GLU N N 125.45 0.2 1 241 45 50 GLY H H 9.21 0.04 1 242 45 50 GLY C C 172.97 0.4 1 243 45 50 GLY CA C 45.98 0.4 1 244 45 50 GLY N N 113.90 0.2 1 245 46 51 TYR H H 7.19 0.04 1 246 46 51 TYR C C 173.86 0.4 1 247 46 51 TYR CA C 57.65 0.4 1 248 46 51 TYR CB C 39.43 0.4 1 249 46 51 TYR N N 120.05 0.2 1 250 47 52 SER H H 6.97 0.04 1 251 47 52 SER C C 172.00 0.4 1 252 47 52 SER CA C 56.31 0.4 1 253 47 52 SER CB C 61.94 0.4 1 254 47 52 SER N N 122.89 0.2 1 255 48 53 TYR H H 8.22 0.04 1 256 48 53 TYR C C 179.42 0.4 1 257 48 53 TYR CA C 59.16 0.4 1 258 48 53 TYR CB C 42.24 0.4 1 259 48 53 TYR N N 125.92 0.2 1 260 49 54 THR H H 10.30 0.04 1 261 49 54 THR C C 176.14 0.4 1 262 49 54 THR CA C 62.71 0.4 1 263 49 54 THR CB C 71.18 0.4 1 264 49 54 THR N N 112.89 0.2 1 265 50 55 ASP H H 8.70 0.04 1 266 50 55 ASP C C 178.10 0.4 1 267 50 55 ASP CA C 57.00 0.4 1 268 50 55 ASP CB C 40.60 0.4 1 269 50 55 ASP N N 120.74 0.2 1 270 51 56 ALA H H 7.74 0.04 1 271 51 56 ALA C C 179.67 0.4 1 272 51 56 ALA CA C 55.16 0.4 1 273 51 56 ALA CB C 18.40 0.4 1 274 51 56 ALA N N 119.40 0.2 1 275 52 57 ASN H H 8.26 0.04 1 276 52 57 ASN HD21 H 7.25 0.04 2 277 52 57 ASN HD22 H 8.86 0.04 2 278 52 57 ASN C C 177.74 0.4 1 279 52 57 ASN CA C 58.63 0.4 1 280 52 57 ASN CB C 39.81 0.4 1 281 52 57 ASN N N 119.12 0.2 1 282 52 57 ASN ND2 N 107.04 0.2 1 283 53 58 ILE H H 7.68 0.04 1 284 53 58 ILE C C 180.41 0.4 1 285 53 58 ILE CA C 65.82 0.4 1 286 53 58 ILE CB C 39.29 0.4 1 287 53 58 ILE N N 120.66 0.2 1 288 54 59 LYS H H 9.10 0.04 1 289 54 59 LYS C C 178.42 0.4 1 290 54 59 LYS CA C 58.07 0.4 1 291 54 59 LYS CB C 32.14 0.4 1 292 54 59 LYS N N 118.89 0.2 1 293 55 60 LYS H H 7.47 0.04 1 294 55 60 LYS C C 177.37 0.4 1 295 55 60 LYS CA C 57.22 0.4 1 296 55 60 LYS CB C 31.43 0.4 1 297 55 60 LYS N N 119.61 0.2 1 298 56 61 ASN H H 7.05 0.04 1 299 56 61 ASN HD21 H 6.36 0.04 2 300 56 61 ASN HD22 H 7.67 0.04 2 301 56 61 ASN C C 174.84 0.4 1 302 56 61 ASN CA C 54.14 0.4 1 303 56 61 ASN CB C 37.87 0.4 1 304 56 61 ASN CG C 177.92 0.4 1 305 56 61 ASN N N 112.86 0.2 1 306 56 61 ASN ND2 N 108.78 0.2 1 307 57 62 VAL H H 7.40 0.04 1 308 57 62 VAL C C 174.64 0.4 1 309 57 62 VAL CA C 60.63 0.4 1 310 57 62 VAL CB C 33.17 0.4 1 311 57 62 VAL N N 116.57 0.2 1 312 58 63 LEU H H 8.29 0.04 1 313 58 63 LEU C C 176.09 0.4 1 314 58 63 LEU CA C 53.69 0.4 1 315 58 63 LEU CB C 41.03 0.4 1 316 58 63 LEU N N 127.94 0.2 1 317 59 64 TRP H H 8.05 0.04 1 318 59 64 TRP C C 175.86 0.4 1 319 59 64 TRP CA C 57.84 0.4 1 320 59 64 TRP CB C 29.56 0.4 1 321 59 64 TRP N N 128.90 0.2 1 322 60 65 ASP H H 9.40 0.04 1 323 60 65 ASP C C 175.40 0.4 1 324 60 65 ASP CA C 52.35 0.4 1 325 60 65 ASP CB C 42.77 0.4 1 326 60 65 ASP N N 125.37 0.2 1 327 61 66 GLU H H 10.29 0.04 1 328 61 66 GLU C C 177.74 0.4 1 329 61 66 GLU CA C 61.97 0.4 1 330 61 66 GLU CB C 29.13 0.4 1 331 61 66 GLU N N 117.43 0.2 1 332 62 67 ASN H H 8.25 0.04 1 333 62 67 ASN HD21 H 7.18 0.04 2 334 62 67 ASN HD22 H 7.79 0.04 2 335 62 67 ASN C C 178.45 0.4 1 336 62 67 ASN CA C 56.35 0.4 1 337 62 67 ASN CB C 38.82 0.4 1 338 62 67 ASN CG C 176.28 0.4 1 339 62 67 ASN N N 116.35 0.2 1 340 62 67 ASN ND2 N 113.68 0.2 1 341 63 68 ASN H H 9.58 0.04 1 342 63 68 ASN HD21 H 6.97 0.04 2 343 63 68 ASN HD22 H 7.62 0.04 2 344 63 68 ASN C C 179.26 0.4 1 345 63 68 ASN CA C 55.92 0.4 1 346 63 68 ASN CB C 36.83 0.4 1 347 63 68 ASN CG C 175.87 0.4 1 348 63 68 ASN N N 122.13 0.2 1 349 63 68 ASN ND2 N 111.17 0.2 1 350 64 69 MET H H 8.99 0.04 1 351 64 69 MET C C 178.28 0.4 1 352 64 69 MET CA C 58.31 0.4 1 353 64 69 MET CB C 31.52 0.4 1 354 64 69 MET N N 121.27 0.2 1 355 65 70 SER H H 7.90 0.04 1 356 65 70 SER C C 177.81 0.4 1 357 65 70 SER CA C 61.85 0.4 1 358 65 70 SER CB C 63.07 0.4 1 359 65 70 SER N N 114.06 0.2 1 360 66 71 GLU H H 7.82 0.04 1 361 66 71 GLU C C 179.61 0.4 1 362 66 71 GLU CA C 60.12 0.4 1 363 66 71 GLU CB C 29.48 0.4 1 364 66 71 GLU N N 120.95 0.2 1 365 67 72 TYR H H 8.38 0.04 1 366 67 72 TYR C C 176.38 0.4 1 367 67 72 TYR CA C 60.68 0.4 1 368 67 72 TYR CB C 39.03 0.4 1 369 67 72 TYR N N 121.71 0.2 1 370 68 73 LEU H H 8.32 0.04 1 371 68 73 LEU C C 177.46 0.4 1 372 68 73 LEU CA C 55.66 0.4 1 373 68 73 LEU CB C 42.08 0.4 1 374 68 73 LEU N N 111.98 0.2 1 375 69 74 THR H H 7.36 0.04 1 376 69 74 THR C C 174.35 0.4 1 377 69 74 THR CA C 66.58 0.4 1 378 69 74 THR CB C 68.64 0.4 1 379 69 74 THR N N 115.86 0.2 1 380 70 75 ASN H H 6.24 0.04 1 381 70 75 ASN HD21 H 6.70 0.04 2 382 70 75 ASN HD22 H 7.60 0.04 2 383 70 75 ASN CA C 51.90 0.4 1 384 70 75 ASN CB C 37.12 0.4 1 385 70 75 ASN CG C 177.18 0.4 1 386 70 75 ASN N N 108.80 0.2 1 387 70 75 ASN ND2 N 111.56 0.2 1 388 71 76 PRO C C 176.71 0.4 1 389 71 76 PRO CA C 66.04 0.4 1 390 71 76 PRO CB C 30.46 0.4 1 391 72 77 LYS H H 7.62 0.04 1 392 72 77 LYS C C 177.52 0.4 1 393 72 77 LYS CA C 57.90 0.4 1 394 72 77 LYS CB C 31.91 0.4 1 395 72 77 LYS N N 113.26 0.2 1 396 73 78 LYS H H 6.97 0.04 1 397 73 78 LYS C C 177.01 0.4 1 398 73 78 LYS CA C 57.32 0.4 1 399 73 78 LYS CB C 33.28 0.4 1 400 73 78 LYS N N 118.04 0.2 1 401 74 79 TYR H H 7.40 0.04 1 402 74 79 TYR C C 175.93 0.4 1 403 74 79 TYR CA C 61.46 0.4 1 404 74 79 TYR CB C 39.99 0.4 1 405 74 79 TYR N N 119.65 0.2 1 406 75 80 ILE H H 8.26 0.04 1 407 75 80 ILE CA C 59.00 0.4 1 408 75 80 ILE CB C 37.66 0.4 1 409 75 80 ILE N N 113.80 0.2 1 410 76 81 PRO C C 178.70 0.4 1 411 76 81 PRO CA C 64.24 0.4 1 412 76 81 PRO CB C 31.10 0.4 1 413 77 82 GLY H H 8.66 0.04 1 414 77 82 GLY C C 175.77 0.4 1 415 77 82 GLY CA C 44.59 0.4 1 416 77 82 GLY N N 111.67 0.2 1 417 78 83 THR H H 8.27 0.04 1 418 78 83 THR C C 172.65 0.4 1 419 78 83 THR CA C 61.49 0.4 1 420 78 83 THR CB C 68.23 0.4 1 421 78 83 THR N N 115.23 0.2 1 422 79 84 LYS H H 7.85 0.04 1 423 79 84 LYS C C 176.23 0.4 1 424 79 84 LYS CA C 55.36 0.4 1 425 79 84 LYS CB C 32.88 0.4 1 426 79 84 LYS N N 122.53 0.2 1 427 80 85 MET H H 7.02 0.04 1 428 80 85 MET C C 172.26 0.4 1 429 80 85 MET CA C 56.57 0.4 1 430 80 85 MET CB C 27.42 0.4 1 431 80 85 MET N N 123.63 0.2 1 432 81 86 ALA H H 8.14 0.04 1 433 81 86 ALA C C 174.21 0.4 1 434 81 86 ALA CA C 51.11 0.4 1 435 81 86 ALA CB C 17.31 0.4 1 436 81 86 ALA N N 135.37 0.2 1 437 82 87 PHE H H 6.23 0.04 1 438 82 87 PHE C C 174.83 0.4 1 439 82 87 PHE CA C 56.51 0.4 1 440 82 87 PHE CB C 41.87 0.4 1 441 82 87 PHE N N 119.78 0.2 1 442 83 88 GLY H H 8.36 0.04 1 443 83 88 GLY CA C 46.36 0.4 1 444 83 88 GLY N N 115.31 0.2 1 445 84 89 GLY C C 172.57 0.4 1 446 84 89 GLY CA C 43.62 0.4 1 447 85 90 LEU H H 8.43 0.04 1 448 85 90 LEU C C 175.43 0.4 1 449 85 90 LEU CA C 53.10 0.4 1 450 85 90 LEU CB C 32.83 0.4 1 451 85 90 LEU N N 122.84 0.2 1 452 86 91 LYS H H 8.45 0.04 1 453 86 91 LYS C C 177.99 0.4 1 454 86 91 LYS CA C 58.29 0.4 1 455 86 91 LYS CB C 32.80 0.4 1 456 86 91 LYS N N 123.06 0.2 1 457 87 92 LYS H H 8.96 0.04 1 458 87 92 LYS C C 177.06 0.4 1 459 87 92 LYS CA C 56.02 0.4 1 460 87 92 LYS CB C 32.32 0.4 1 461 87 92 LYS N N 120.09 0.2 1 462 88 93 GLU H H 9.01 0.04 1 463 88 93 GLU C C 177.69 0.4 1 464 88 93 GLU CA C 60.33 0.4 1 465 88 93 GLU CB C 29.80 0.4 1 466 88 93 GLU N N 129.41 0.2 1 467 89 94 LYS H H 8.74 0.04 1 468 89 94 LYS C C 178.02 0.4 1 469 89 94 LYS CA C 59.78 0.4 1 470 89 94 LYS CB C 32.60 0.4 1 471 89 94 LYS N N 117.02 0.2 1 472 90 95 ASP H H 6.50 0.04 1 473 90 95 ASP C C 178.22 0.4 1 474 90 95 ASP CA C 57.06 0.4 1 475 90 95 ASP CB C 40.40 0.4 1 476 90 95 ASP N N 115.97 0.2 1 477 91 96 ARG H H 7.60 0.04 1 478 91 96 ARG C C 177.99 0.4 1 479 91 96 ARG CA C 61.67 0.4 1 480 91 96 ARG CB C 30.63 0.4 1 481 91 96 ARG N N 118.35 0.2 1 482 92 97 ASN H H 8.83 0.04 1 483 92 97 ASN HD21 H 7.25 0.04 2 484 92 97 ASN HD22 H 7.29 0.04 2 485 92 97 ASN C C 179.92 0.4 1 486 92 97 ASN CA C 56.19 0.4 1 487 92 97 ASN CB C 37.28 0.4 1 488 92 97 ASN CG C 175.89 0.4 1 489 92 97 ASN N N 118.21 0.2 1 490 92 97 ASN ND2 N 110.60 0.2 1 491 93 98 ASP H H 8.80 0.04 1 492 93 98 ASP C C 177.93 0.4 1 493 93 98 ASP CA C 59.15 0.4 1 494 93 98 ASP CB C 40.23 0.4 1 495 93 98 ASP N N 125.69 0.2 1 496 94 99 LEU H H 8.66 0.04 1 497 94 99 LEU C C 179.30 0.4 1 498 94 99 LEU CA C 59.06 0.4 1 499 94 99 LEU CB C 42.16 0.4 1 500 94 99 LEU N N 121.04 0.2 1 501 95 100 ILE H H 9.31 0.04 1 502 95 100 ILE C C 176.60 0.4 1 503 95 100 ILE CA C 66.62 0.4 1 504 95 100 ILE CB C 37.78 0.4 1 505 95 100 ILE N N 120.59 0.2 1 506 96 101 THR H H 8.30 0.04 1 507 96 101 THR C C 177.07 0.4 1 508 96 101 THR CA C 68.51 0.4 1 509 96 101 THR N N 117.96 0.2 1 510 97 102 TYR H H 7.92 0.04 1 511 97 102 TYR C C 176.40 0.4 1 512 97 102 TYR CA C 61.49 0.4 1 513 97 102 TYR CB C 38.07 0.4 1 514 97 102 TYR N N 120.09 0.2 1 515 98 103 LEU H H 9.41 0.04 1 516 98 103 LEU C C 179.55 0.4 1 517 98 103 LEU CA C 57.74 0.4 1 518 98 103 LEU CB C 43.32 0.4 1 519 98 103 LEU N N 120.64 0.2 1 520 99 104 LYS H H 8.79 0.04 1 521 99 104 LYS C C 177.08 0.4 1 522 99 104 LYS CA C 59.23 0.4 1 523 99 104 LYS CB C 31.50 0.4 1 524 99 104 LYS N N 121.40 0.2 1 525 100 105 LYS H H 6.60 0.04 1 526 100 105 LYS C C 178.72 0.4 1 527 100 105 LYS CA C 57.19 0.4 1 528 100 105 LYS CB C 32.50 0.4 1 529 100 105 LYS N N 115.65 0.2 1 530 101 106 ALA H H 8.39 0.04 1 531 101 106 ALA C C 178.61 0.4 1 532 101 106 ALA CA C 53.97 0.4 1 533 101 106 ALA CB C 18.79 0.4 1 534 101 106 ALA N N 120.08 0.2 1 535 102 107 THR H H 7.44 0.04 1 536 102 107 THR C C 173.54 0.4 1 537 102 107 THR CA C 61.46 0.4 1 538 102 107 THR CB C 70.02 0.4 1 539 102 107 THR N N 102.52 0.2 1 540 103 108 GLU H H 6.81 0.04 1 541 103 108 GLU CA C 58.48 0.4 1 542 103 108 GLU CB C 30.57 0.4 1 543 103 108 GLU N N 127.18 0.2 1 stop_ save_ save_yCc_red_low_salt _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D NOESY-HSQC' stop_ loop_ _Sample_label $sample_2 stop_ _Sample_conditions_label $sample_conditions_2 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name yCc _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 -4 2 GLU H H 8.70 0.04 1 2 -4 2 GLU N N 120.41 0.2 1 3 -3 3 PHE H H 8.76 0.04 1 4 -3 3 PHE N N 124.70 0.2 1 5 -2 4 LYS H H 6.59 0.04 1 6 -2 4 LYS N N 127.83 0.2 1 7 -1 5 ALA H H 7.77 0.04 1 8 -1 5 ALA N N 122.87 0.2 1 9 1 6 GLY H H 8.28 0.04 1 10 1 6 GLY N N 111.05 0.2 1 11 2 7 SER H H 9.58 0.04 1 12 2 7 SER N N 120.45 0.2 1 13 3 8 ALA H H 9.33 0.04 1 14 3 8 ALA N N 132.11 0.2 1 15 4 9 LYS H H 8.29 0.04 1 16 4 9 LYS N N 119.59 0.2 1 17 5 10 LYS H H 7.87 0.04 1 18 5 10 LYS N N 120.45 0.2 1 19 6 11 GLY H H 8.85 0.04 1 20 6 11 GLY N N 108.01 0.2 1 21 7 12 ALA H H 8.10 0.04 1 22 7 12 ALA N N 125.29 0.2 1 23 8 13 THR H H 7.29 0.04 1 24 8 13 THR N N 115.88 0.2 1 25 9 14 LEU H H 8.09 0.04 1 26 9 14 LEU N N 124.27 0.2 1 27 10 15 PHE H H 8.88 0.04 1 28 10 15 PHE N N 120.80 0.2 1 29 11 16 LYS H H 8.34 0.04 1 30 11 16 LYS N N 120.02 0.2 1 31 12 17 THR H H 8.03 0.04 1 32 12 17 THR N N 108.09 0.2 1 33 13 18 ARG H H 8.65 0.04 1 34 13 18 ARG N N 117.21 0.2 1 35 14 19 CYS H H 8.08 0.04 1 36 14 19 CYS N N 115.47 0.2 1 37 15 20 LEU H H 7.26 0.04 1 38 15 20 LEU N N 121.72 0.2 1 39 16 21 GLN H H 8.88 0.04 1 40 16 21 GLN HE21 H 7.06 0.04 2 41 16 21 GLN HE22 H 7.62 0.04 2 42 16 21 GLN N N 115.93 0.2 1 43 16 21 GLN NE2 N 111.56 0.2 1 44 17 22 CYS H H 7.02 0.04 1 45 17 22 CYS N N 112.82 0.2 1 46 18 23 HIS H H 6.54 0.04 1 47 18 23 HIS N N 115.94 0.2 1 48 19 24 THR H H 7.21 0.04 1 49 19 24 THR N N 105.84 0.2 1 50 20 25 VAL H H 7.45 0.04 1 51 20 25 VAL N N 108.72 0.2 1 52 21 26 GLU H H 8.87 0.04 1 53 21 26 GLU N N 120.41 0.2 1 54 22 27 LYS H H 8.71 0.04 1 55 22 27 LYS N N 125.56 0.2 1 56 23 28 GLY H H 9.26 0.04 1 57 23 28 GLY N N 118.13 0.2 1 58 24 29 GLY H H 7.83 0.04 1 59 24 29 GLY N N 108.23 0.2 1 60 26 31 HIS H H 8.41 0.04 1 61 26 31 HIS N N 121.14 0.2 1 62 27 32 LYS H H 7.71 0.04 1 63 27 32 LYS N N 125.40 0.2 1 64 28 33 VAL H H 7.04 0.04 1 65 28 33 VAL N N 121.97 0.2 1 66 29 34 GLY H H 7.70 0.04 1 67 29 34 GLY N N 106.27 0.2 1 68 31 36 ASN H H 10.82 0.04 1 69 31 36 ASN HD21 H 7.45 0.04 2 70 31 36 ASN HD22 H 7.87 0.04 2 71 31 36 ASN N N 124.91 0.2 1 72 31 36 ASN ND2 N 115.23 0.2 1 73 32 37 LEU H H 7.79 0.04 1 74 32 37 LEU N N 121.56 0.2 1 75 33 38 HIS H H 7.47 0.04 1 76 33 38 HIS N N 118.56 0.2 1 77 34 39 GLY H H 9.10 0.04 1 78 34 39 GLY N N 116.16 0.2 1 79 35 40 ILE H H 7.20 0.04 1 80 35 40 ILE N N 117.46 0.2 1 81 36 41 PHE H H 8.02 0.04 1 82 36 41 PHE N N 116.39 0.2 1 83 37 42 GLY H H 8.78 0.04 1 84 37 42 GLY N N 110.52 0.2 1 85 38 43 ARG H H 8.12 0.04 1 86 38 43 ARG N N 121.32 0.2 1 87 39 44 HIS H H 7.96 0.04 1 88 39 44 HIS N N 116.45 0.2 1 89 40 45 SER H H 8.70 0.04 1 90 40 45 SER N N 116.24 0.2 1 91 41 46 GLY H H 8.23 0.04 1 92 41 46 GLY N N 113.11 0.2 1 93 42 47 GLN H H 8.22 0.04 1 94 42 47 GLN HE21 H 6.81 0.04 2 95 42 47 GLN HE22 H 7.55 0.04 2 96 42 47 GLN N N 114.52 0.2 1 97 42 47 GLN NE2 N 112.78 0.2 1 98 43 48 ALA H H 8.71 0.04 1 99 43 48 ALA N N 125.58 0.2 1 100 44 49 GLU H H 8.80 0.04 1 101 44 49 GLU N N 125.40 0.2 1 102 45 50 GLY H H 9.21 0.04 1 103 45 50 GLY N N 113.90 0.2 1 104 46 51 TYR H H 7.19 0.04 1 105 46 51 TYR N N 120.09 0.2 1 106 47 52 SER H H 6.96 0.04 1 107 47 52 SER N N 122.88 0.2 1 108 48 53 TYR H H 8.24 0.04 1 109 48 53 TYR N N 126.04 0.2 1 110 49 54 THR H H 10.29 0.04 1 111 49 54 THR N N 112.86 0.2 1 112 50 55 ASP H H 8.69 0.04 1 113 50 55 ASP N N 120.86 0.2 1 114 51 56 ALA H H 7.73 0.04 1 115 51 56 ALA N N 119.39 0.2 1 116 52 57 ASN H H 8.25 0.04 1 117 52 57 ASN HD21 H 7.25 0.04 2 118 52 57 ASN HD22 H 8.84 0.04 2 119 52 57 ASN N N 119.13 0.2 1 120 52 57 ASN ND2 N 107.02 0.2 1 121 53 58 ILE H H 7.68 0.04 1 122 53 58 ILE N N 120.70 0.2 1 123 54 59 LYS H H 9.09 0.04 1 124 54 59 LYS N N 118.87 0.2 1 125 55 60 LYS H H 7.46 0.04 1 126 55 60 LYS N N 119.65 0.2 1 127 56 61 ASN H H 7.04 0.04 1 128 56 61 ASN HD21 H 6.36 0.04 2 129 56 61 ASN HD22 H 7.67 0.04 2 130 56 61 ASN N N 112.86 0.2 1 131 56 61 ASN ND2 N 108.72 0.2 1 132 57 62 VAL H H 7.39 0.04 1 133 57 62 VAL N N 116.58 0.2 1 134 58 63 LEU H H 8.29 0.04 1 135 58 63 LEU N N 128.00 0.2 1 136 59 64 TRP H H 8.05 0.04 1 137 59 64 TRP N N 128.95 0.2 1 138 60 65 ASP H H 9.37 0.04 1 139 60 65 ASP N N 125.44 0.2 1 140 61 66 GLU H H 10.28 0.04 1 141 61 66 GLU N N 117.51 0.2 1 142 62 67 ASN H H 8.26 0.04 1 143 62 67 ASN HD21 H 7.17 0.04 2 144 62 67 ASN HD22 H 7.79 0.04 2 145 62 67 ASN N N 116.43 0.2 1 146 62 67 ASN ND2 N 113.69 0.2 1 147 63 68 ASN H H 9.58 0.04 1 148 63 68 ASN HD21 H 6.97 0.04 2 149 63 68 ASN N N 122.20 0.2 1 150 63 68 ASN ND2 N 111.19 0.2 1 151 64 69 MET H H 8.99 0.04 1 152 64 69 MET N N 121.34 0.2 1 153 65 70 SER H H 7.89 0.04 1 154 65 70 SER N N 114.16 0.2 1 155 66 71 GLU H H 7.82 0.04 1 156 66 71 GLU N N 121.02 0.2 1 157 67 72 TYR H H 8.37 0.04 1 158 67 72 TYR N N 121.73 0.2 1 159 68 73 LEU H H 8.31 0.04 1 160 68 73 LEU N N 112.05 0.2 1 161 69 74 THR H H 7.36 0.04 1 162 69 74 THR N N 115.91 0.2 1 163 70 75 ASN H H 6.23 0.04 1 164 70 75 ASN HD21 H 6.69 0.04 2 165 70 75 ASN HD22 H 7.62 0.04 2 166 70 75 ASN N N 108.70 0.2 1 167 70 75 ASN ND2 N 111.65 0.2 1 168 72 77 LYS H H 7.61 0.04 1 169 72 77 LYS N N 113.33 0.2 1 170 73 78 LYS H H 6.97 0.04 1 171 73 78 LYS N N 118.11 0.2 1 172 74 79 TYR H H 7.39 0.04 1 173 74 79 TYR N N 119.70 0.2 1 174 75 80 ILE H H 8.26 0.04 1 175 75 80 ILE N N 113.82 0.2 1 176 77 82 GLY H H 8.66 0.04 1 177 77 82 GLY N N 111.65 0.2 1 178 78 83 THR H H 8.27 0.04 1 179 78 83 THR N N 115.29 0.2 1 180 79 84 LYS H H 7.86 0.04 1 181 79 84 LYS N N 122.63 0.2 1 182 80 85 MET H H 7.03 0.04 1 183 80 85 MET N N 123.72 0.2 1 184 81 86 ALA H H 8.15 0.04 1 185 81 86 ALA N N 135.43 0.2 1 186 82 87 PHE H H 6.21 0.04 1 187 82 87 PHE N N 119.82 0.2 1 188 85 90 LEU H H 8.42 0.04 1 189 85 90 LEU N N 123.01 0.2 1 190 86 91 LYS H H 8.55 0.04 1 191 86 91 LYS N N 123.37 0.2 1 192 87 92 LYS H H 8.95 0.04 1 193 87 92 LYS N N 120.23 0.2 1 194 88 93 GLU H H 9.01 0.04 1 195 88 93 GLU N N 129.37 0.2 1 196 89 94 LYS H H 8.75 0.04 1 197 89 94 LYS N N 117.05 0.2 1 198 90 95 ASP H H 6.49 0.04 1 199 90 95 ASP N N 116.00 0.2 1 200 91 96 ARG H H 7.59 0.04 1 201 91 96 ARG N N 118.39 0.2 1 202 92 97 ASN H H 8.82 0.04 1 203 92 97 ASN HD21 H 7.24 0.04 2 204 92 97 ASN HD22 H 7.29 0.04 2 205 92 97 ASN N N 118.32 0.2 1 206 92 97 ASN ND2 N 110.62 0.2 1 207 93 98 ASP H H 8.83 0.04 1 208 93 98 ASP N N 125.90 0.2 1 209 94 99 LEU H H 8.67 0.04 1 210 94 99 LEU N N 121.09 0.2 1 211 95 100 ILE H H 9.30 0.04 1 212 95 100 ILE N N 120.61 0.2 1 213 96 101 THR H H 8.29 0.04 1 214 96 101 THR N N 118.03 0.2 1 215 97 102 TYR H H 7.92 0.04 1 216 97 102 TYR N N 120.13 0.2 1 217 98 103 LEU H H 9.41 0.04 1 218 98 103 LEU N N 120.70 0.2 1 219 99 104 LYS H H 8.79 0.04 1 220 99 104 LYS N N 121.47 0.2 1 221 100 105 LYS H H 6.59 0.04 1 222 100 105 LYS N N 115.64 0.2 1 223 101 106 ALA H H 8.39 0.04 1 224 101 106 ALA N N 120.18 0.2 1 225 102 107 THR H H 7.44 0.04 1 226 102 107 THR N N 102.55 0.2 1 227 103 108 GLU H H 6.80 0.04 1 228 103 108 GLU N N 127.29 0.2 1 stop_ save_