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 18605

Title: Solution NMR Structure of Human Transcription Elongation Factor A protein 2, Central Domain, Northeast Structural Genomics Consortium (NESG) Target HR8682B

Deposition date: 2012-07-20 Original release date: 2012-08-27

Authors: Eletsky, Alexander; ., Wang; ., .; ., .; ., .; 7, .; Gaetano, 8; Szyperski, Thomas

Citation: Eletsky, Alexander; ., Wang; ., .; ., .; ., .; 18605, .; 8, 18605; Thomas, 9. "Solution NMR Structure of Human Transcription Elongation Factor A protein 2, Central Domain"  To be published ., .-..

Assembly members:
HR8682B, polymer, 113 residues, 12736.705 Da.

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

Experimental source:   Production method: recombinant technology' 'Escherichia coli

Entity Sequences (FASTA):
HR8682B: SHMPVPVTCDAVRNKCREML TAALQTDHDHVAIGADCERL SAQIEECIFRDVGNTDMKYK NRVRSRISNLKDAKNPDLRR NVLCGAITPQQIAVMTSEEM ASDELKEIRKAMT

Data sets:
Data typeCount
13C chemical shifts447
1071H chemical shifts

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HR8682B1

Entities:

Entity 1, HR8682B 113 residues - 12736.705 Da.

Residues 4-113 correspond to residues 130-239 of the native protein. Residues 1-3 represent the remainder of the purification tag following its cleavage

1   SER.186055.VAL.1860511.
2   ARG.1860517.MET.1860523.
3   GLN.1860529.VAL.1860535.
4   CYS.1860541.GLN.1860547.
5   PHE.1860553.THR.1860559.
6   ASN.1860565.ILE.1860571.
7   ALA.1860577.ARG.1860583.
8   GLY.1860589.GLN.1860595.
9   SER.18605101.ASP.18605107.
10   ARG.18605113

Samples:

NC: HR8682B.004, [U-100% 13C; U-100% 15N], 1.0 mM; natural abundance; .; . %; .

NC5: HR8682B.004, [5% 13C; U-100% 15N], 1.0 mM; natural abundance; .; . %; .

sample_conditions_1: pH: 7.5; 1: . 18605; .: K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNCisotropicsample_conditions_1
nosotropicnot availablenot available
not availablenot availablenot availablenot available
not availablenot available1not available
not availablenot available$sample_conditions_1not available
not availablesample_conditions_1not available750
not availablenot availablenot availablenot available
not availablenot availablenot availablenot available
not availablenot available2not available
not availablenot available$750not available
not available750not availablenot available
not availablenot availablenot availablenot available
1not availablenot availablenot available
$NCnot availablenot availablenot available
isotropicnot availablenot availablenot available

Software:

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution, geometry optimization

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - refinement, geometry optimization, structure solution

ASDP v1.0, Huang, Tejero, Powers and Montelione - data analysis, refinement

XEASY v1.3.13, Bartels et al. - data analysis

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, 18605

VNMRJ v2.2D, Varian - collection

PINE v2.0, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization

PSVS, Bhattacharya, Montelione - structure validation

NMR spectrometers:

  • Varian INOVA 750 MHz
  • Varian INOVA 600 MHz

Related Database Links:

UNP Q15560
2LW4 .
. transcription elongation factor S-II, hS-II-T1 [Homo sapiens] . . . . 97.35 . . . 18605
unnamed protein product [Homo sapiens] .
97.35 299
324 100.00
97.27 99.09
100.00 3.94e-72
4.06e-70 .
18605

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