BMRB Entry 28105

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28105

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Title:
Backbone and ILV methyl chemical shift assignments of REC2 domain from SpyCas9
Deposition date:
2020-03-23
Original release date:
2020-12-02
Authors:
De Paula, Viviane; Sgourakis, Nikolaos
Citation:

Citation: Nerli, Santrupti; De Paula, Viviane; McShan, Andrew; Sgourakis, Nikolaos. "Backbone-independent NMR resonance assignments of methyl probes in large proteins"  Nat. Commun. 12, 691-691 (2021).
PubMed: 33514730

Assembly members:

Assembly members:
REC2_domain, polymer, 141 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Streptococcus pyogenes   Taxonomy ID: 1314   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Streptococcus pyogenes

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
REC2_domain: HFLIEGDLNPDNSDVDKLFI QLVQTYNQLFEENPINASGV DAKAILSARLSKSRRLENLI AQLPGEKKNGLFGNLIALSL GLTPNFKSNFDLAEDAKLQL SKDTYDDDLDNLLAQIGDQY ADLFLAAKNLSDAILLSDIL R

Data sets:
Data typeCount
13C chemical shifts419
15N chemical shifts126
1H chemical shifts315

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1REC21

Entities:

Entity 1, REC2 141 residues - Formula weight is not available

1   HISPHELEUILEGLUGLYASPLEUASNPRO
2   ASPASNSERASPVALASPLYSLEUPHEILE
3   GLNLEUVALGLNTHRTYRASNGLNLEUPHE
4   GLUGLUASNPROILEASNALASERGLYVAL
5   ASPALALYSALAILELEUSERALAARGLEU
6   SERLYSSERARGARGLEUGLUASNLEUILE
7   ALAGLNLEUPROGLYGLULYSLYSASNGLY
8   LEUPHEGLYASNLEUILEALALEUSERLEU
9   GLYLEUTHRPROASNPHELYSSERASNPHE
10   ASPLEUALAGLUASPALALYSLEUGLNLEU
11   SERLYSASPTHRTYRASPASPASPLEUASP
12   ASNLEULEUALAGLNILEGLYASPGLNTYR
13   ALAASPLEUPHELEUALAALALYSASNLEU
14   SERASPALAILELEULEUSERASPILELEU
15   ARG

Samples:

sample_1: REC2 domain, [U-100% 13C; U-100% 15N; ILV-methyl], 0.3 mM; sodium chloride 50 mM; sodium phosphate 20 mM

sample_2: REC2 domain, [U-13C; U-15N; U-2H; ILV-methyl], 0.5 mM; sodium chloride 50 mM; sodium phosphate 20 mM

sample_3: REC2 domain, [U-13C; U-15N; U-2H; IL(CD2)V(CG2)-methyl], 0.5 mM; sodium chloride 50 mM; sodium phosphate 20 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
2D 1H-13C SOFAST HMQCsample_2isotropicsample_conditions_1
2D 1H-15N SOFAST HMQCsample_1isotropicsample_conditions_1
3D Cm-CmHm SOFAST NOESY HMQCsample_2isotropicsample_conditions_1
3D Hn-CmHm SOFAST NOESY HMQCsample_1isotropicsample_conditions_1
3D N-CmHm SOFAST NOESY HMQCsample_1isotropicsample_conditions_1
2D 1H-13C SOFAST HMQCsample_3isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

CCPN, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz

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