data_7139 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H,13C and 15N resonance assignments of barnase-barstar complex NMR deuterium methyl relaxation data for free barnase and barnase-barstar complex ; _BMRB_accession_number 7139 _BMRB_flat_file_name bmr7139.str _Entry_type original _Submission_date 2006-05-22 _Accession_date 2006-05-22 _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 Zhuravleva Anastasia V. . 2 Korzhnev Dmitry M. . 3 Nolde Svetlana B. . 4 Kay Lewis E. . 5 Arseniev Alexander S. . 6 Billiter Martin . . 7 Orekhov Vladislav Yu . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count S2_parameters 1 stop_ loop_ _Data_type _Data_type_count "order parameters" 41 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-16 update BMRB 'complete entry citation' 2007-03-06 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 4964 'chemical shifts of free barnase' 6227 'chemical shifts of free barstar' 7126 'complex of barnase and barstar' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Propagation of Dynamic Changes in Barnase Upon Binding of Barstar: An NMR and Computational Study' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 17306298 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Zhuravleva Anastasia V. . 2 Korzhnev Dmitry M. . 3 Nolde Svetlana B. . 4 Kay Lewis E. . 5 Arseniev Alexander S. . 6 Billiter Martin . . 7 Orekhov Vladislav Yu . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 367 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1079 _Page_last 1092 _Year 2007 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_nmrPipe_ref _Saveframe_category citation _Citation_full . _Citation_title 'Nmrpipe - a Multidimensional Spectral Processing System Based on Unix Pipes' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8520220 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Delaglio F. . . 2 Grzesiek S. . . 3 Vuister G. W. . 4 Zhu G. . . 5 Pfeifer J. . . 6 Bax A. . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full . _Journal_volume 6 _Journal_issue 3 _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 277 _Page_last 293 _Year 1995 _Details . save_ save_Dasha_ref _Saveframe_category citation _Citation_full . _Citation_title 'Processing of heteronuclear NMR relaxation data with the new software DASHA' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Orekhov V. Yu . 2 Nolde D. E. . 3 Golovanov A. P. . 4 Korzhnev D. M. . 5 Arseniev A. S. . stop_ _Journal_abbreviation 'Appl. Magn. Reson.' _Journal_name_full . _Journal_volume 9 _Journal_issue 4 _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 581 _Page_last 588 _Year 1995 _Details . save_ save_Cara_ref _Saveframe_category citation _Citation_full . _Citation_title 'optimizing the process of nuclear magnetic resonance spectrum analysis and computer aided resonance assigment' _Citation_status published _Citation_type thesis _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Keller Rochus . . stop_ _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 'swiss federal institute of technology' _Thesis_institution_city zurich _Thesis_institution_country swiss _Page_first . _Page_last . _Year . _Details . save_ save_H2exp_ref _Saveframe_category citation _Citation_full . _Citation_title 'Deuterium spin probes of side-chain dynamics in proteins.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Millet O. D. . 2 Muhandiram N. R. . 3 Skrynnikov N. R. . 4 Kay L. E. . stop_ _Journal_abbreviation 'J. Am. Chem. Soc.' _Journal_name_full . _Journal_volume 124 _Journal_issue 22 _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 6439 _Page_last 6448 _Year 2002 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'free barnase' _Enzyme_commission_number 3.1.27.3 loop_ _Mol_system_component_name _Mol_label barnase $barnase stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state protein _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'ribonuclease-inhibitor complex' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_barnase _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common barnase _Molecular_mass 12401.9 _Mol_thiol_state 'not present' loop_ _Biological_function 'endoribonuclease activity' 'RNA binding' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 110 _Mol_residue_sequence ; AQVINTFDGVADYLQTYHKL PDNYITKSEAQALGWVASKG NLADVAPGKSIGGDIFSNRE GKLPGKSGRTWREADINYTS GFRNSDRILYSSDWLIYKTT DHYQTFTKIR ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 GLN 3 VAL 4 ILE 5 ASN 6 THR 7 PHE 8 ASP 9 GLY 10 VAL 11 ALA 12 ASP 13 TYR 14 LEU 15 GLN 16 THR 17 TYR 18 HIS 19 LYS 20 LEU 21 PRO 22 ASP 23 ASN 24 TYR 25 ILE 26 THR 27 LYS 28 SER 29 GLU 30 ALA 31 GLN 32 ALA 33 LEU 34 GLY 35 TRP 36 VAL 37 ALA 38 SER 39 LYS 40 GLY 41 ASN 42 LEU 43 ALA 44 ASP 45 VAL 46 ALA 47 PRO 48 GLY 49 LYS 50 SER 51 ILE 52 GLY 53 GLY 54 ASP 55 ILE 56 PHE 57 SER 58 ASN 59 ARG 60 GLU 61 GLY 62 LYS 63 LEU 64 PRO 65 GLY 66 LYS 67 SER 68 GLY 69 ARG 70 THR 71 TRP 72 ARG 73 GLU 74 ALA 75 ASP 76 ILE 77 ASN 78 TYR 79 THR 80 SER 81 GLY 82 PHE 83 ARG 84 ASN 85 SER 86 ASP 87 ARG 88 ILE 89 LEU 90 TYR 91 SER 92 SER 93 ASP 94 TRP 95 LEU 96 ILE 97 TYR 98 LYS 99 THR 100 THR 101 ASP 102 HIS 103 TYR 104 GLN 105 THR 106 PHE 107 THR 108 LYS 109 ILE 110 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 16169 barnase 98.18 108 99.07 99.07 2.74e-71 BMRB 16170 barnase 98.18 108 99.07 99.07 2.74e-71 BMRB 16171 barnase 98.18 108 99.07 99.07 2.74e-71 BMRB 16172 barnase 98.18 108 99.07 99.07 2.74e-71 BMRB 2066 barnase 100.00 110 100.00 100.00 4.04e-74 BMRB 2067 barnase 100.00 110 100.00 100.00 4.04e-74 BMRB 2070 barnase 100.00 110 100.00 100.00 4.04e-74 BMRB 4964 barnase 100.00 110 100.00 100.00 4.04e-74 BMRB 975 barnase 100.00 110 100.00 100.00 4.04e-74 PDB 1A2P "Barnase Wildtype Structure At 1.5 Angstroms Resolution" 100.00 110 100.00 100.00 4.04e-74 PDB 1B20 "Deletion Of A Buried Salt-Bridge In Barnase" 100.00 110 99.09 99.09 2.85e-73 PDB 1B21 "Deletion Of A Buried Salt Bridge In Barnase" 100.00 110 98.18 99.09 1.03e-72 PDB 1B27 "Structural Response To Mutation At A Protein-Protein Interface" 100.00 110 100.00 100.00 4.04e-74 PDB 1B2S "Structural Response To Mutation At A Protein-Protein Interface" 100.00 110 99.09 99.09 1.97e-73 PDB 1B2U "Structural Response To Mutation At A Protein-Protein Interface" 100.00 110 99.09 99.09 1.97e-73 PDB 1B2X "Barnase Wildtype Structure At Ph 7.5 From A Cryo_cooled Crystal At 100k" 100.00 110 100.00 100.00 4.04e-74 PDB 1B2Z "Deletion Of A Buried Salt Bridge In Barnase" 100.00 110 99.09 100.00 1.42e-73 PDB 1B3S "Structural Response To Mutation At A Protein-Protein Interface" 100.00 110 99.09 99.09 6.19e-73 PDB 1BAN "The Contribution Of Buried Hydrogen Bonds To Protein Stability: The Crystal Structures Of Two Barnase Mutants" 100.00 110 99.09 100.00 8.50e-74 PDB 1BAO "The Contribution Of Buried Hydrogen Bonds To Protein Stability: The Crystal Structures Of Two Barnase Mutants" 100.00 110 99.09 100.00 9.17e-74 PDB 1BGS "Recognition Between A Bacterial Ribonuclease, Barnase, And Its Natural Inhibitor, Barstar" 100.00 110 100.00 100.00 4.04e-74 PDB 1BNE "Barnase A43cS80C DISULFIDE MUTANT" 100.00 110 98.18 98.18 2.82e-73 PDB 1BNF "Barnase T70cS92C DISULFIDE MUTANT" 100.00 110 98.18 98.18 3.18e-73 PDB 1BNG "Barnase S85cH102C DISULFIDE MUTANT" 100.00 110 98.18 98.18 1.95e-72 PDB 1BNI "Barnase Wildtype Structure At Ph 6.0" 100.00 110 100.00 100.00 4.04e-74 PDB 1BNJ "Barnase Wildtype Structure At Ph 9.0" 100.00 110 100.00 100.00 4.04e-74 PDB 1BNR Barnase 100.00 110 100.00 100.00 4.04e-74 PDB 1BNS "Structural Studies Of Barnase Mutants" 100.00 110 99.09 99.09 1.52e-73 PDB 1BRG "Crystallographic Analysis Of Phe->leu Substitution In The Hydrophobic Core Of Barnase" 98.18 108 99.07 99.07 7.31e-72 PDB 1BRH "Barnase Mutant With Leu 14 Replaced By Ala" 100.00 110 99.09 99.09 1.91e-73 PDB 1BRI "Barnase Mutant With Ile 76 Replaced By Ala" 100.00 110 99.09 99.09 1.77e-73 PDB 1BRJ "Barnase Mutant With Ile 88 Replaced By Ala" 100.00 110 99.09 99.09 1.77e-73 PDB 1BRK "Barnase Mutant With Ile 96 Replaced By Ala" 100.00 110 99.09 99.09 1.77e-73 PDB 1BRN "Subsite Binding In An Rnase: Structure Of A Barnase- Tetranucleotide Complex At 1.76 Angstroms Resolution" 100.00 110 100.00 100.00 4.04e-74 PDB 1BRS "Protein-Protein Recognition: Crystal Structural Analysis Of A Barnase-Barstar Complex At 2.0-A Resolution" 100.00 110 100.00 100.00 4.04e-74 PDB 1BSA "Crystal Structural Analysis Of Mutations In The Hydrophobic Cores Of Barnase" 100.00 110 99.09 100.00 5.03e-74 PDB 1BSB "Crystal Structural Analysis Of Mutations In The Hydrophobic Cores Of Barnase" 100.00 110 99.09 100.00 5.03e-74 PDB 1BSC "Crystal Structural Analysis Of Mutations In The Hydrophobic Cores Of Barnase" 100.00 110 99.09 100.00 5.03e-74 PDB 1BSD "Crystal Structural Analysis Of Mutations In The Hydrophobic Cores Of Barnase" 100.00 110 99.09 100.00 5.03e-74 PDB 1BSE "Crystal Structural Analysis Of Mutations In The Hydrophobic Cores Of Barnase" 100.00 110 99.09 100.00 1.05e-73 PDB 1FW7 "Nmr Structure Of 15n-Labeled Barnase" 99.09 110 100.00 100.00 1.88e-73 PDB 1RNB "Crystal Structure Of A Barnase-D(GpC) Complex At 1.9 Angstroms Resolution" 100.00 110 98.18 100.00 1.00e-72 PDB 1X1U "Water-Mediate Interaction At Aprotein-Protein Interface" 100.00 110 100.00 100.00 4.04e-74 PDB 1X1W "Water-Mediate Interaction At Aprotein-Protein Interface" 100.00 110 100.00 100.00 4.04e-74 PDB 1X1X "Water-Mediate Interaction At Aprotein-Protein Interface" 100.00 110 100.00 100.00 4.04e-74 PDB 1X1Y "Water-Mediate Interaction At Aprotein-Protein Interface" 100.00 110 99.09 99.09 2.92e-73 PDB 1YVS "Trimeric Domain Swapped Barnase" 100.00 110 100.00 100.00 4.04e-74 PDB 2C4B "Inhibitor Cystine Knot Protein Mcoeeti Fused To The Catalytically Inactive Barnase Mutant H102a" 99.09 143 99.08 99.08 1.18e-72 PDB 2F4Y "Barnase Cross-Linked With Glutaraldehyde" 98.18 108 100.00 100.00 1.23e-72 PDB 2F56 "Barnase Cross-Linked With Glutaraldehyde Soaked In 6m Urea" 98.18 108 100.00 100.00 1.23e-72 PDB 2F5M "Cross-Linked Barnase Soaked In Bromo-Ethanol" 98.18 108 100.00 100.00 1.23e-72 PDB 2F5W "Cross-Linked Barnase Soaked In 3 M Thiourea" 98.18 108 100.00 100.00 1.23e-72 PDB 2KF3 "Barnase, Low Pressure Reference Nmr Structure" 100.00 110 99.09 99.09 6.19e-73 PDB 2KF4 "Barnase High Pressure Structure" 100.00 110 99.09 99.09 6.19e-73 PDB 2KF5 "Barnase Bound To D(Cgac), Low Pressure" 100.00 110 99.09 99.09 6.19e-73 PDB 2KF6 "Barnase Bound To D(Cgac) High Pressure" 100.00 110 99.09 99.09 6.19e-73 PDB 2ZA4 "Crystal Structural Analysis Of Barnase-barstar Complex" 100.00 110 99.09 99.09 1.97e-73 PDB 3KCH "Baranase Crosslinked By Glutaraldehyde" 100.00 110 100.00 100.00 4.04e-74 EMBL CAA31365 "barnase [Bacillus amyloliquefaciens]" 100.00 110 100.00 100.00 4.04e-74 EMBL CBI44445 "putative ribonuclease RBAM_031940 [Bacillus amyloliquefaciens DSM 7]" 100.00 157 100.00 100.00 4.01e-75 EMBL CCF06756 "Ribonuclease Barnase [Bacillus amyloliquefaciens subsp. plantarum CAU B946]" 100.00 157 98.18 99.09 2.24e-73 EMBL CCG51396 "Ribonuclease Barnase [Bacillus amyloliquefaciens subsp. plantarum YAU B9601-Y2]" 100.00 157 97.27 99.09 3.14e-73 EMBL CDG27389 "Ribonuclease [Bacillus amyloliquefaciens subsp. plantarum UCMB5113]" 100.00 149 98.18 99.09 6.56e-74 GB AAA86441 "barnase (RNase) precursor [Bacillus amyloliquefaciens]" 100.00 149 100.00 100.00 4.06e-75 GB AAB28825 "RNase Bci=extracellular ribonuclease {EC 3.1.27.1} [Bacillus circulans, BCF 247, Peptide, 110 aa]" 100.00 110 97.27 98.18 7.87e-72 GB AAB29635 "RNase=extracellular ribonuclease [Bacillus circulans, Peptide, 110 aa]" 100.00 110 97.27 98.18 7.87e-72 GB AAC53661 "barnase [synthetic construct]" 100.00 111 100.00 100.00 2.55e-74 GB AAP41137 "barnase ribonuclease precursor [Cloning vector pHRBar-6]" 100.00 131 100.00 100.00 1.33e-74 PRF 1204204A barnase 100.00 157 100.00 100.00 3.19e-75 PRF 2004243A RNase 100.00 110 97.27 98.18 7.87e-72 PRF 721946A RNase 100.00 110 98.18 100.00 1.00e-72 REF WP_003151497 "ribonuclease [Bacillus amyloliquefaciens]" 100.00 157 98.18 99.09 2.24e-73 REF WP_007407419 "MULTISPECIES: ribonuclease [Bacillales]" 100.00 157 97.27 99.09 3.14e-73 REF WP_012118533 "ribonuclease [Bacillus amyloliquefaciens]" 100.00 149 97.27 99.09 2.86e-73 REF WP_013353722 "ribonuclease [Bacillus amyloliquefaciens]" 100.00 157 100.00 100.00 4.01e-75 REF WP_014472289 "ribonuclease [Bacillus amyloliquefaciens]" 100.00 164 100.00 100.00 3.74e-75 SP P00648 "RecName: Full=Ribonuclease; AltName: Full=Barnase; AltName: Full=RNase Ba; Flags: Precursor [Bacillus amyloliquefaciens]" 100.00 157 100.00 100.00 3.19e-75 SP P35078 "RecName: Full=Ribonuclease; AltName: Full=RNase Bci [Bacillus circulans]" 100.00 110 97.27 98.18 7.87e-72 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $barnase 'Bacillus amyloliquefaciens' 1390 Eubacteria 'Not applicable' Bacillus amyloliquefaciens 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 $barnase 'recombinant technology' 'E. Coli' . . . . 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 $barnase 1.3 mM '[U-13C; U-15N; U-40% 2H]' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Frank Delaglio' . spin.niddk.nih.gov/bax/software/NMRPipe stop_ _Details ; NMRPipe provides comprehensive facilities for Fourier processing of spectra in one to four dimensions, as well as a variety of facilities for spectral display and analysis. It is currently used in over 300 academic and commercial laboratories. ; _Citation_label $nmrPipe_ref save_ save_CARA _Saveframe_category software _Name CARA _Version . _Details ; CARA is a program for computer-aided resonance assignment of multidimensional NMR spectra of macromolecules. Dedicated tools along with a well organized database allow for efficient assignment. Custom applications can be developed with scripts. All major platforms are supported. ; _Citation_label $Cara_ref save_ save_DASHA _Saveframe_category software _Name DASHA _Version 4.1 loop_ _Vendor _Address _Electronic_address 'Prof. A.S Arseniev' ; Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, RAS Ul. Miklukho-Maklaya 16/10 Moscow, 117871, Russia ; aars@nmr.ru stop_ _Details 'Model-Free Analysis of Protein Dynamics from Heteronuclear NMR Relaxation Data' _Citation_label $Dasha_ref save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_500MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 500 _Details . save_ save_600MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ save_800MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_HNCACB_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label $sample_1 save_ save_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label $sample_1 save_ save_(H)CC(CO)TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name (H)CC(CO)TOCSY _Sample_label $sample_1 save_ save_H(CC)(CO)NH-TOCSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name H(CC)(CO)NH-TOCSY _Sample_label $sample_1 save_ save_13C_HSQC-RQ(3Dz2-2)_5 _Saveframe_category NMR_applied_experiment _Experiment_name '13C HSQC-RQ(3Dz2-2)' _Sample_label $sample_1 save_ save_13C_HSQC-RQ(D+z+Dz+)_6 _Saveframe_category NMR_applied_experiment _Experiment_name '13C HSQC-RQ(D+z+Dz+)' _Sample_label $sample_1 save_ save_13C_HSQC-RQ(Dz)_7 _Saveframe_category NMR_applied_experiment _Experiment_name '13C HSQC-RQ(Dz)' _Sample_label $sample_1 save_ save_13C_HSQC-RQ(D+)_8 _Saveframe_category NMR_applied_experiment _Experiment_name '13C HSQC-RQ(D+)' _Sample_label $sample_1 save_ save_15N_HSQC_9 _Saveframe_category NMR_applied_experiment _Experiment_name '15N HSQC' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.03 0.0 M pH 6.7 0.5 pH temperature 303 0.2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _Saveframe_category chemical_shift_reference _Details "'setref' macro from VNMR software, Solvent is 'D2O'" loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 stop_ save_ save_S2_free _Saveframe_category S2_parameters _Details 'Methyl axial order parameters of sub-nanosecond motions for free barnase' loop_ _Software_label $DASHA stop_ loop_ _Experiment_label $13C_HSQC-RQ(3Dz2-2)_5 $13C_HSQC-RQ(D+z+Dz+)_6 $13C_HSQC-RQ(Dz)_7 $13C_HSQC-RQ(D+)_8 stop_ loop_ _Sample_label $sample_1 $sample_1 $sample_1 $sample_1 $sample_1 $sample_1 $sample_1 $sample_1 stop_ _Sample_conditions_label $conditions_1 _Mol_system_component_name barnase _Tau_e_value_units . _Text_data_format . _Text_data . loop_ _Residue_seq_code _Residue_label _Atom_name _Model_fit _S2_value _S2_value_fit_error _Tau_e_value _Tau_e_value_fit_error _S2f_value _S2f_value_fit_error _S2s_value _S2s_value_fit_error _Tau_s_value _Tau_s_value_fit_error _S2H_value _S2H_value_fit_error _S2N_value _S2N_value_fit_error 1 ALA CB . 0.153 0.009 0.0240 0.0005 . . . . . . . . . . 3 VAL CG1 . 0.522 0.018 0.0460 0.0010 . . . . . . . . . . 6 THR CG2 . 0.927 0.036 0.0300 0.0020 . . . . . . . . . . 10 VAL CG1 . 0.882 0.018 0.0490 0.0015 . . . . . . . . . . 11 ALA CB . 0.900 0.022 0.0340 0.0015 . . . . . . . . . . 14 LEU CD1 . 0.792 0.108 0.0860 0.0050 . . . . . . . . . . 14 LEU CD2 . 0.801 0.031 0.0130 0.0015 . . . . . . . . . . 16 THR CG2 . 0.900 0.040 0.0520 0.0025 . . . . . . . . . . 20 LEU CD1 . 1.188 0.103 0.0700 0.0060 . . . . . . . . . . 20 LEU CD2 . 0.774 0.108 0.1070 0.0040 . . . . . . . . . . 25 ILE CG2 . 0.819 0.027 0.0450 0.0015 . . . . . . . . . . 25 ILE CD1 . 0.774 0.013 0.0250 0.0005 . . . . . . . . . . 30 ALA CB . 0.918 0.040 0.0660 0.0025 . . . . . . . . . . 32 ALA CB . 0.900 0.018 0.0250 0.0010 . . . . . . . . . . 33 LEU CD2 . 0.720 0.023 0.0290 0.0015 . . . . . . . . . . 36 VAL CG1 . 0.801 0.009 0.0340 0.0005 . . . . . . . . . . 37 ALA CB . 0.891 0.031 0.0490 0.0015 . . . . . . . . . . 42 LEU CD1 . 1.008 0.099 0.0480 0.0045 . . . . . . . . . . 42 LEU CD2 . 0.810 0.027 0.0490 0.0020 . . . . . . . . . . 43 ALA CB . 0.972 0.041 0.0680 0.0025 . . . . . . . . . . 45 VAL CG1 . 0.810 0.009 0.0160 0.0005 . . . . . . . . . . 45 VAL CG2 . 0.855 0.018 0.0300 0.0010 . . . . . . . . . . 46 ALA CB . 0.909 0.031 0.0560 0.0020 . . . . . . . . . . 51 ILE CG2 . 0.855 0.032 0.0550 0.0020 . . . . . . . . . . 51 ILE CD1 . 0.369 0.013 0.0240 0.0010 . . . . . . . . . . 55 ILE CD1 . 0.378 0.013 0.0230 0.0010 . . . . . . . . . . 63 LEU CD2 . 0.675 0.027 0.0480 0.0020 . . . . . . . . . . 74 ALA CB . 0.927 0.013 0.0210 0.0010 . . . . . . . . . . 76 ILE CG2 . 0.891 0.023 0.0330 0.0015 . . . . . . . . . . 76 ILE CD1 . 0.819 0.018 0.0050 0.0010 . . . . . . . . . . 79 THR CG2 . 0.810 0.027 0.0500 0.0020 . . . . . . . . . . 88 ILE CD1 . 0.675 0.014 0.0130 0.0010 . . . . . . . . . . 89 LEU CD1 . 0.648 0.018 0.0350 0.0010 . . . . . . . . . . 89 LEU CD2 . 0.666 0.058 0.0970 0.0030 . . . . . . . . . . 95 LEU CD1 . 0.369 0.014 0.0360 0.0005 . . . . . . . . . . 95 LEU CD2 . 0.369 0.018 0.0810 0.0015 . . . . . . . . . . 96 ILE CG2 . 0.855 0.018 0.0210 0.0010 . . . . . . . . . . 96 ILE CD1 . 0.576 0.023 0.0250 0.0015 . . . . . . . . . . 105 THR CG2 . 0.828 0.036 0.0550 0.0025 . . . . . . . . . . 107 THR CG2 . 0.855 0.023 0.0560 0.0020 . . . . . . . . . . 109 ILE CG2 . 0.756 0.018 0.0340 0.0010 . . . . . . . . . . stop_ _Tau_s_value_units . save_