BMRB Entry 25493

Name: Human Med26 N-Terminal Domain (1-92)
Published: 2016-06-30

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PDB ID: 5odd
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25493
MolProbity Validation Chart

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Human Med26 N-Terminal Domain (1-92) PubMed: 26861138

Deposition date: 2015-02-19 Original release date: 2016-06-30

Authors: Peruzzini, Riccardo; Landrieu, Isabelle; Villeret, Vincent; Lens, Zoe; Cantrelle, Francois-Xavier

Citation: Peruzzini, Riccardo; Lens, Zoe; Verger, Alexis; Dewitte, Frederique; Ferreira, Elisabeth; Baert, Jean-Luc; Villeret, Vincent; Landrieu, Isabelle; Cantrelle, Francois-Xavier. "(1)H, (15)N and (13)C assignments of the N-terminal domain of the Mediator complex subunit MED26" Biomol. NMR Assign. 10, 233-236 (2016).

Assembly members:
entity, polymer, 93 residues, 9410.110 Da.

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

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

Entity Sequences (FASTA):
entity: GMTAAPASPQQIRDRLLQAI DPQSNIRNMVAVLEVISSLE KYPITKEALEETRLGKLIND VRKKTKNEELAKRAKKLLRS WQKLIEPAHQHEA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	402
15N chemical shifts	95
1H chemical shifts	568

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 93 residues - 9410.110 Da.

1

GLY

MET

THR

ALA

PRO

ALA

SER

PRO

GLN

2

GLN

ILE

ARG

ASP

ARG

LEU

GLN

ALA

ILE

3

ASP

PRO

GLN

SER

ASN

ILE

ARG

ASN

MET

VAL

4

ALA

VAL

LEU

GLU

VAL

ILE

SER

LEU

GLU

5

LYS

TYR

PRO

ILE

THR

LYS

GLU

ALA

LEU

GLU

6

GLU

THR

ARG

LEU

GLY

LYS

LEU

ILE

ASN

ASP

7

VAL

ARG

LYS

THR

LYS

ASN

GLU

LEU

8

ALA

LYS

ARG

ALA

LYS

LEU

ARG

SER

9

TRP

GLN

LYS

LEU

ILE

GLU

PRO

ALA

HIS

GLN

10

HIS

GLU

ALA

Samples:

sample_1: entity, [U-100% 15N], 0.4 – 1.4 mM; HEPES 50 mM; sodium chloride 100 mM; DTT 1 mM; EDTA 2.5 mM; H2O 90%; D2O 10%

sample_2: entity, [U-100% 13C; U-100% 15N], 0.4 – 1.4 mM; HEPES 50 mM; sodium chloride 100 mM; DTT 1 mM; EDTA 2.5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.1 M; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HNHA	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_2	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment, processing

UNIO, Herrmann, Guntert and Wuthrich - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

PSVS, Bhattacharya and Montelione - data analysis

NMR spectrometers:

Bruker Avance 900 MHz
Bruker Avance 600 MHz

Biological Magnetic Resonance Data Bank