BMRB Entry 27781

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27781
MolProbity Validation Chart

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Title:
NMR assignment of free 1H, 15N and 13C-Grb2-SH2 domain
Deposition date:
2019-02-11
Original release date:
2019-05-07
Authors:
Sanches, Karoline; Caruso, Icaro; Almeida, Fabio; Melo, Fernando
Citation:

Citation: Sanches, Karoline; Caruso, Icaro; Almeida, Fabio; Melo, Fernando. "NMR assignment of free 1H, 15N and 13C-Grb2-SH2 domain"  Biomol. NMR Assignments 13, 295-298 (2019).
PubMed: 31028611

Assembly members:

Assembly members:
SH2-Grb2, polymer, 106 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET 33

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SH2-Grb2: MGSSHHHHHHMKPHPWFFGK IPRAKAEEMLSKQRHDGAFL IRESESAPGDFSLSVKFGND VQHFKVLRDGAGKYFLWVVK FNSLNELVDYHRSTSVSRNQ QIFLRD

Data sets:
Data typeCount
13C chemical shifts414
15N chemical shifts81
1H chemical shifts633

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1SH2 domain1

Entities:

Entity 1, SH2 domain 106 residues - Formula weight is not available

Residues 1-10 represent a non-native affinity tag. In the manuscript residue 1 start at MKPH....

1   METGLYSERSERHISHISHISHISHISHIS
2   METLYSPROHISPROTRPPHEPHEGLYLYS
3   ILEPROARGALALYSALAGLUGLUMETLEU
4   SERLYSGLNARGHISASPGLYALAPHELEU
5   ILEARGGLUSERGLUSERALAPROGLYASP
6   PHESERLEUSERVALLYSPHEGLYASNASP
7   VALGLNHISPHELYSVALLEUARGASPGLY
8   ALAGLYLYSTYRPHELEUTRPVALVALLYS
9   PHEASNSERLEUASNGLULEUVALASPTYR
10   HISARGSERTHRSERVALSERARGASNGLN
11   GLNILEPHELEUARGASP

Samples:

sample_1: SH2-Grb2, [U-13C; U-15N], 350 mM; sodium phosphate 20 mM; sodium chloride 200 mM; PMSF 1 mM; EDTA 1 mM; sodium azide 5 mM; D2O 10%; H2O 90%

sample_conditions_1: ionic strength: 0.2 M; pH: 7; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

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

CCPN_Analysis v2.4.2, CCPN - chemical shift assignment

TOPSPIN v3.5 pl7, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance IIIHD 600 MHz
  • Bruker Avance III 800 MHz
  • Bruker Avance IIIHD 900 MHz
  • Bruker Avance IIIHD 700 MHz

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