BMRB Entry 18605

Name: Solution NMR Structure of Human Transcription Elongation Factor A protein 2, Central Domain, Northeast Structural Genomics Consortium (NESG) Target HR8682B
Published: 2012-08-27

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PDB ID: 2lw4
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18605
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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

Entity Sequences (FASTA):

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

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list

Data type	Count
13C chemical shifts	447
15N chemical shifts	107
1H chemical shifts	740

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HR8682B	1

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

HIS

MET

PRO

VAL

PRO

VAL

THR

CYS

ASP

2

ALA

VAL

ARG

ASN

LYS

CYS

ARG

GLU

MET

LEU

3

THR

ALA

LEU

GLN

THR

ASP

HIS

ASP

HIS

4

VAL

ALA

ILE

GLY

ALA

ASP

CYS

GLU

ARG

LEU

5

SER

ALA

GLN

ILE

GLU

CYS

ILE

PHE

ARG

6

ASP

VAL

GLY

ASN

THR

ASP

MET

LYS

TYR

LYS

7

ASN

ARG

VAL

ARG

SER

ARG

ILE

SER

ASN

LEU

8

LYS

ASP

ALA

LYS

ASN

PRO

ASP

LEU

ARG

9

ASN

VAL

LEU

CYS

GLY

ALA

ILE

THR

PRO

GLN

10

GLN

ILE

ALA

VAL

MET

THR

SER

GLU

MET

11

ALA

SER

ASP

GLU

LEU

LYS

GLU

ILE

ARG

LYS

12

ALA

MET

THR

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	NC	isotropic	sample_conditions_1
2D 1H-13C CT-HSQC aliphatic	NC	isotropic	sample_conditions_1
3D HNCO	NC	isotropic	sample_conditions_1
3D CBCA(CO)NH	NC	isotropic	sample_conditions_1
3D HNCACB	NC	isotropic	sample_conditions_1
3D HN(CA)CO	NC	isotropic	sample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESY	NC	isotropic	sample_conditions_1
3D (H)C(CO)NH-TOCSY	NC	isotropic	sample_conditions_1
3D HBHA(CO)NH	NC	isotropic	sample_conditions_1
3D (H)CCH-TOCSY	NC	isotropic	sample_conditions_1
2D 1H-13C CT-HSQC aromatic	NC	isotropic	sample_conditions_1
3D (H)CCH-COSY aliphatic	NC	isotropic	sample_conditions_1
1D 15N T1	NC	isotropic	sample_conditions_1
1D 15N T2	NC	isotropic	sample_conditions_1
2D 1H-13C CT-HSQC methyl	NC5	isotropic	sample_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

UNP	Q15560
PDB	2LW4
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