BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 26619

Title: Amide/Methyl/Aromatic Chemical Shifts and Order Parameters of Free Barnase   PubMed: 28584100

Deposition date: 2015-07-30 Original release date: 2017-06-27

Authors: Caro, Jose; Kathleen, Valentine; Wand, Joshua

Citation: Caro, Jose; Harpole, Kyle; Kasinath, Vignesh; Lim, Jackwee; Granja, Jeffrey; Valentine, Kathleen; Sharp, Kim; Wand, A Joshua. "Entropy in molecular recognition by proteins"  Proc. Natl. Acad. Sci. U.S.A. 114, 6563-6568 (2017).

Assembly members:
Barnase, polymer, 110 residues, Formula weight is not available

Natural source:   Common Name: Bacillus amyloliquefaciens   Taxonomy ID: 1390   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacillus amyloliquefaciens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
Barnase: AQVINTFDGVADYLQTYHKL PDNYITKSEAQALGWVASKG NLADVAPGKSIGGDIFSNRE GKLPGKSGRTWREADINYTS GFRNSDRILYSSDWLIYKTT DHYQTFTKIR

Data sets:
Data typeCount
13C chemical shifts264
15N chemical shifts106
1H chemical shifts271
order parameters157

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Barnase monomer1

Entities:

Entity 1, Barnase monomer 110 residues - Formula weight is not available

1   ALAGLNVALILEASNTHRPHEASPGLYVAL
2   ALAASPTYRLEUGLNTHRTYRHISLYSLEU
3   PROASPASNTYRILETHRLYSSERGLUALA
4   GLNALALEUGLYTRPVALALASERLYSGLY
5   ASNLEUALAASPVALALAPROGLYLYSSER
6   ILEGLYGLYASPILEPHESERASNARGGLU
7   GLYLYSLEUPROGLYLYSSERGLYARGTHR
8   TRPARGGLUALAASPILEASNTYRTHRSER
9   GLYPHEARGASNSERASPARGILELEUTYR
10   SERSERASPTRPLEUILETYRLYSTHRTHR
11   ASPHISTYRGLNTHRPHETHRLYSILEARG

Samples:

sample_1: Barnase, [U-13C; U-15N; U-2H], 0.5 mM

sample_conditions_1: ionic strength: 10 mM; pH: 6.2; pressure: 1 atm; temperature: 308.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1

Software:

Felix, Accelrys Software Inc. - data analysis

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 750 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts