BMRB Entry 28110

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28110

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Title:
Backbone and ILV methyl assignments for REC3 domain of SpCas9
Deposition date:
2020-03-27
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:
REC3_domain, polymer, 207 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):
REC3_domain: KVLPKHSLLYEYFTVYNELT KVKYVTEGMRKPAFLSGEQK KAIVDLLFKTNRKVTVKQLK EDYFKKIECFDSVEISGVED RFNASLGTYHDLLKIIKDKD FLDNEENEDILEDIVLTLTL FEDREMIEERLKTYAHLFDD KVMKQLKRRRYTGWGRLSRK LINGIRDKQSGKTILDFLKS DGFANRNFMQLIHDDSLTFK EDIQKAQ

Data sets:
Data typeCount
13C chemical shifts304
15N chemical shifts86
1H chemical shifts341

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1REC31

Entities:

Entity 1, REC3 207 residues - Formula weight is not available

1   LYSVALLEUPROLYSHISSERLEULEUTYR
2   GLUTYRPHETHRVALTYRASNGLULEUTHR
3   LYSVALLYSTYRVALTHRGLUGLYMETARG
4   LYSPROALAPHELEUSERGLYGLUGLNLYS
5   LYSALAILEVALASPLEULEUPHELYSTHR
6   ASNARGLYSVALTHRVALLYSGLNLEULYS
7   GLUASPTYRPHELYSLYSILEGLUCYSPHE
8   ASPSERVALGLUILESERGLYVALGLUASP
9   ARGPHEASNALASERLEUGLYTHRTYRHIS
10   ASPLEULEULYSILEILELYSASPLYSASP
11   PHELEUASPASNGLUGLUASNGLUASPILE
12   LEUGLUASPILEVALLEUTHRLEUTHRLEU
13   PHEGLUASPARGGLUMETILEGLUGLUARG
14   LEULYSTHRTYRALAHISLEUPHEASPASP
15   LYSVALMETLYSGLNLEULYSARGARGARG
16   TYRTHRGLYTRPGLYARGLEUSERARGLYS
17   LEUILEASNGLYILEARGASPLYSGLNSER
18   GLYLYSTHRILELEUASPPHELEULYSSER
19   ASPGLYPHEALAASNARGASNPHEMETGLN
20   LEUILEHISASPASPSERLEUTHRPHELYS
21   GLUASPILEGLNLYSALAGLN

Samples:

sample_1: REC3 domain, [U-2H; U-15N; U-13C; ILV], 0.7 mM; Tris 20 mM; KCl 200 mM; glycerol-d8 5%; TCEP 1 mM

sample_2: REC3 domain, [U-15N; U-2H; U-13C-all methyl carbons], 0.5 mM; Tris 20 mM; KCl 200 mM; glycerol-d8 5%; TCEP 1 mM

sample_3: REC3 domain, [U-15N; U-2H; U-13C; IL(CD2)V(CG2)], 0.3 mM; Tris 20 mM; KCl 200 mM; glycerol-d8 5%; TCEP 1 mM

sample_conditions_1: ionic strength: 0.2 M; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCAsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HN(COCA)CBsample_2isotropicsample_conditions_1
2D 1H-15N TROSYsample_2isotropicsample_conditions_1
2D 1H-13C SOFAST HMQCsample_1isotropicsample_conditions_1
2D 1H-15N SOFAST HMQCsample_2isotropicsample_conditions_1
3D Hm-CmHm SOFAST NOESY HMQCsample_1isotropicsample_conditions_1
3D Cm-CmHm SOFAST NOESY HMQCsample_1isotropicsample_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