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, Dongyan; Kohan, Eitan; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Everett, John; Montelione, Gaetano; Szyperski, Thomas
Citation:

Citation: Eletsky, Alexander; Wang, Dongyan; Kohan, Eitan; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Everett, John; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR Structure of Human Transcription Elongation Factor A protein 2, Central Domain"  To be published ., .-..

Assembly members:

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

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: pET15Avi6HT_NESG

Data sets:
Data typeCount
13C chemical shifts447
15N chemical shifts107
1H chemical shifts740

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   SERHISMETPROVALPROVALTHRCYSASP
2   ALAVALARGASNLYSCYSARGGLUMETLEU
3   THRALAALALEUGLNTHRASPHISASPHIS
4   VALALAILEGLYALAASPCYSGLUARGLEU
5   SERALAGLNILEGLUGLUCYSILEPHEARG
6   ASPVALGLYASNTHRASPMETLYSTYRLYS
7   ASNARGVALARGSERARGILESERASNLEU
8   LYSASPALALYSASNPROASPLEUARGARG
9   ASNVALLEUCYSGLYALAILETHRPROGLN
10   GLNILEALAVALMETTHRSERGLUGLUMET
11   ALASERASPGLULEULYSGLUILEARGLYS
12   ALAMETTHR

Samples:

NC: HR8682B.004, [U-100% 13C; U-100% 15N], 1.0 mM; NaCl 100 mM; DTT 5 mM; NaN3 0.02%; TRIS 10 mM

NC5: HR8682B.004, [5% 13C; U-100% 15N], 1.0 mM; NaCl 100 mM; DTT 5 mM; NaN3 0.02%; TRIS 10 mM

sample_conditions_1: pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNCisotropicsample_conditions_1
2D 1H-13C CT-HSQC aliphaticNCisotropicsample_conditions_1
3D HNCONCisotropicsample_conditions_1
3D CBCA(CO)NHNCisotropicsample_conditions_1
3D HNCACBNCisotropicsample_conditions_1
3D HN(CA)CONCisotropicsample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESYNCisotropicsample_conditions_1
3D (H)C(CO)NH-TOCSYNCisotropicsample_conditions_1
3D HBHA(CO)NHNCisotropicsample_conditions_1
3D (H)CCH-TOCSYNCisotropicsample_conditions_1
2D 1H-13C CT-HSQC aromaticNCisotropicsample_conditions_1
3D (H)CCH-COSY aliphaticNCisotropicsample_conditions_1
1D 15N T1NCisotropicsample_conditions_1
1D 15N T2NCisotropicsample_conditions_1
2D 1H-13C CT-HSQC methylNC5isotropicsample_conditions_1

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, data analysis, peak picking

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
PDB
DBJ BAA09089 BAG51383 BAJ20194
EMBL CAG33221 CAH59746
GB AAH18896 ABZ92433 EAW75168 EAW75170 EHH19498
PRF 2204253A
REF NP_001244428 NP_003186 NP_942016 XP_001153063 XP_003787843
SP Q15560
AlphaFold Q8TD38 Q15560

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