BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 17202

Title: Solution structure of tandem SH2 domain from Spt6   PubMed: 21676864

Authors: Liu, Jianping; Zhang, Jiahai; Wu, Jihui; Shi, Yunyu

Citation: Liu, Jianping; Zhang, Jiahai; Gong, Qingguo; Xiong, Peng; Huang, Hongda; Wu, Bo; Lu, Guowei; Wu, Jihui; Shi, Yunyu. "Solution structure of tandem SH2 domains from Spt6 protein and their binding to the phosphorylated RNA polymerase II C-terminal domain."  J. Biol. Chem. 286, 29218-29226 (2011).

Assembly members:
Tandem SH2 domains of Spt6, polymer, 199 residues, 47542.332 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):
Tandem SH2 domains of Spt6: THRVINHPYYFPFNGRQAED YLRSKERGEFVIRQSSRGDD HLVITWKLDKDLFQHIDIQE LEKENPLALGKVLIVDNQKY NDLDQIIVEYLQNKVRLLNE MTSSEKFKSGTKKDVVKFIE DYSRVNPNKSVYYFSLNHDN PGWFYLMFKINANSKLYTWN VKLTNTGYFLVNYNYPSVIQ LCNGFKTLLKSLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts611
15N chemical shifts207
1H chemical shifts1342

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Tandem SH2 domains of Spt61

Entities:

Entity 1, Tandem SH2 domains of Spt6 199 residues - 47542.332 Da.

1   THRHISARGVALILEASNHISPROTYRTYR
2   PHEPROPHEASNGLYARGGLNALAGLUASP
3   TYRLEUARGSERLYSGLUARGGLYGLUPHE
4   VALILEARGGLNSERSERARGGLYASPASP
5   HISLEUVALILETHRTRPLYSLEUASPLYS
6   ASPLEUPHEGLNHISILEASPILEGLNGLU
7   LEUGLULYSGLUASNPROLEUALALEUGLY
8   LYSVALLEUILEVALASPASNGLNLYSTYR
9   ASNASPLEUASPGLNILEILEVALGLUTYR
10   LEUGLNASNLYSVALARGLEULEUASNGLU
11   METTHRSERSERGLULYSPHELYSSERGLY
12   THRLYSLYSASPVALVALLYSPHEILEGLU
13   ASPTYRSERARGVALASNPROASNLYSSER
14   VALTYRTYRPHESERLEUASNHISASPASN
15   PROGLYTRPPHETYRLEUMETPHELYSILE
16   ASNALAASNSERLYSLEUTYRTHRTRPASN
17   VALLYSLEUTHRASNTHRGLYTYRPHELEU
18   VALASNTYRASNTYRPROSERVALILEGLN
19   LEUCYSASNGLYPHELYSTHRLEULEULYS
20   SERLEUGLUHISHISHISHISHISHIS

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 0.5 mM; potassium phosphate 25 mM; sodium chloride 150 mM; EDTA 1 mM; DTT 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.175 M; pH: 5.5; pressure: 1 atm; temperature: 310 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 HCACOsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1

Software:

X-PLOR NIH v2.24, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ GAA23491
EMBL CAA97124 CAA97127
GB AAA35086 AJP38891 AJR76211 AJR76711 AJR77209
REF NP_011631
SP P23615
TPG DAA08208