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 18341

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18341
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry

Title: Sgt2_NT   PubMed: 23001946

Deposition date: 2012-03-21 Original release date: 2012-11-15

Authors: Simon, Aline; Simpson, Peter; Isaacson, Rivka

Citation: Simon, Aline; Simpson, Peter; Hawthorne, William; Hale, Lisa; Goldstone, Rachael; Isaacson, Rivka. "1H, 13C and 15N assignments of Sgt2N-terminal dimerisation domain and its binding partner, Get5 Ubiquitin-like domain."  Biomol. NMR Assignments 7, 271-274 (2013).

Assembly members:
Sgt2_nt, polymer, 92 residues, 10081.1 Da.

Natural source:   Common Name: baker   Taxonomy ID: 4932   Superkingdom: not available   Kingdom: not available   Genus/species: Eukaryota Fungi

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

Entity Sequences (FASTA):
Sgt2_nt: MAHHHHHHVDDDDKMSASKE EIAALIVNYFSSIVEKKEIS EDGADSLNVAMDCISEAFGF EREAVSGILGKSEFKGQHLA DILNSASRVPES

Data sets:
Data typeCount
13C chemical shifts329
15N chemical shifts82
1H chemical shifts527

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Sgt2_NT, 11
2Sgt2_NT, 21

Entities:

Entity 1, Sgt2_NT, 1 92 residues - 10081.1 Da.

1   METALAHISHISHISHISHISHISVALASP
2   ASPASPASPLYSMETSERALASERLYSGLU
3   GLUILEALAALALEUILEVALASNTYRPHE
4   SERSERILEVALGLULYSLYSGLUILESER
5   GLUASPGLYALAASPSERLEUASNVALALA
6   METASPCYSILESERGLUALAPHEGLYPHE
7   GLUARGGLUALAVALSERGLYILELEUGLY
8   LYSSERGLUPHELYSGLYGLNHISLEUALA
9   ASPILELEUASNSERALASERARGVALPRO
10   GLUSER

Samples:

sample_1: Sgt2_nt, [U-98% 13C; U-98% 15N], 700 uM; MES 100 mM; potassium chloride 150 mM; TCEP 0.5 mM; H2O 90%; D2O 10%

sample_2: Sgt2_nt, [U-100% 13C; U-100% 15N], 500 uM; MES 100 mM; potassium chloride 150 mM; TCEP 0.5 mM; D2O 100%

sample_3: Sgt2_nt, [U-98% 13C; U-98% 15N], 700 uM; MES 100 mM; potassium chloride 150 mM; TCEP 0.5 mM; D2O 100%

sample_conditions_1: ionic strength: 0.250 M; pH: 6.0; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_3isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_3isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_3isotropicsample_conditions_1
3D F1 1H(13C,15N)-reject 13C NOESYsample_2isotropicsample_conditions_1

Software:

TOPSPIN v3.1, Bruker Biospin - collection

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

NMRView v5.2.2_01, Johnson, One Moon Scientific - data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz
  • Oxford Bespoke 950 MHz

Related Database Links:

BMRB 18670
PDB
DBJ GAA26330
EMBL CAA99195 CAY86295
GB AAC49487 AHY77314 AJP41546 AJT70966 AJT71456
REF NP_014649
SP Q12118
TPG DAA10789

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