BMRB Entry 7126

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR7126

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Title:
1H,13C and 15N resonance assignments of barnase-barstar complex NMR deuterium methyl relaxation data for free barnase and barnase-barstar complex
Deposition date:
2006-05-22
Original release date:
2007-03-06
Authors:
Zhuravleva, Anastasia; Korzhnev, Dmitry; Nolde, Svetlana; Kay, Lewis; Arseniev, Alexander; Billiter, Martin; Orekhov, Vladislav
Citation:

Citation: Zhuravleva, Anastasia; Korzhnev, Dmitry; Nolde, Svetlana; Kay, Lewis; Arseniev, Alexander; Billiter, Martin; Orekhov, Vladislav. "Propagation of dynamic changes in barnase upon binding of barstar: an NMR and computational study"  J. Mol. Biol. 367, 1079-1092 (2007).
PubMed: 17306298

Assembly members:

Assembly members:
barnase, polymer, 110 residues, 12401.9 Da.
barstar, polymer, 89 residues, 10223.7 Da.

Natural source:

Natural source:   Common Name: Bacillus amyloliquefaciens   Taxonomy ID: 1390   Superkingdom: Eubacteria   Kingdom: Not applicable   Genus/species: Bacillus amyloliquefaciens

Experimental source:

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
barnase: AQVINTFDGVADYLQTYHKL PDNYITKSEAQALGWVASKG NLADVAPGKSIGGDIFSNRE GKLPGKSGRTWREADINYTS GFRNSDRILYSSDWLIYKTT DHYQTFTKIR
barstar: KKAVINGEQIRSISDLHQTL KKELALPEYYGENLDALWDC LTGWVEYPLVLEWRQFEQSK QLTENGAESVLQVFREAKAE GCDITIILS

Data sets:
Data typeCount
13C chemical shifts250
15N chemical shifts102
1H chemical shifts266
order parameters38

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1barnase1
2barstar2

Entities:

Entity 1, barnase 110 residues - 12401.9 Da.

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

Entity 2, barstar 89 residues - 10223.7 Da.

1   LYSLYSALAVALILEASNGLYGLUGLNILE
2   ARGSERILESERASPLEUHISGLNTHRLEU
3   LYSLYSGLULEUALALEUPROGLUTYRTYR
4   GLYGLUASNLEUASPALALEUTRPASPCYS
5   LEUTHRGLYTRPVALGLUTYRPROLEUVAL
6   LEUGLUTRPARGGLNPHEGLUGLNSERLYS
7   GLNLEUTHRGLUASNGLYALAGLUSERVAL
8   LEUGLNVALPHEARGGLUALALYSALAGLU
9   GLYCYSASPILETHRILEILELEUSER

Samples:

sample_1: barnase, [U-13C; U-15N; U-40% 2H], 1.17 mM; barstar 1.17 mM

conditions_1: ionic strength: 0.03 M; pH: 6.7; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
HNCACBsample_1not availableconditions_1
CBCA(CO)NHsample_1not availableconditions_1
(H)CC(CO)TOCSYsample_1not availableconditions_1
H(CC)(CO)NH-TOCSYsample_1not availableconditions_1
13C HSQC-RQ(3Dz2-2)sample_1not availableconditions_1
13C HSQC-RQ(D+z+Dz+)sample_1not availableconditions_1
13C HSQC-RQ(Dz)sample_1not availableconditions_1
13C HSQC-RQ(D+)sample_1not availableconditions_1
15N HSQCsample_1not availableconditions_1

Software:

NMRPipe, Frank Delaglio -

CARA, . -

DASHA v4.1, Prof. A.S Arseniev -

NMR spectrometers:

  • Varian INOVA 500 MHz
  • Varian INOVA 600 MHz
  • Varian INOVA 800 MHz

Related Database Links:

BMRB 5293 6227
PDB
EMBL CAA33551 CBI41926 CCG48789 CCP20814 CDG25099
GB AAM10782 AAO92245 AAP41138 AAP41140 ABS73233
REF WP_007408543 WP_007610138 WP_013351425 WP_014720882 WP_015239422
SP P11540
AlphaFold P11540

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks