BMRB Entry 25493

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PDB ID:
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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Title:
Human Med26 N-Terminal Domain (1-92)
Deposition date:
2015-02-19
Original release date:
2016-06-30
Authors:
Peruzzini, Riccardo; Landrieu, Isabelle; Villeret, Vincent; Lens, Zoe; Cantrelle, Francois-Xavier
Citation:

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).
PubMed: 26861138

Assembly members:

Assembly members:
entity, polymer, 93 residues, 9410.110 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: pGex4T1-tev

Entity Sequences (FASTA):

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

Data sets:
Data typeCount
13C chemical shifts402
15N chemical shifts95
1H chemical shifts568

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 93 residues - 9410.110 Da.

1   GLYMETTHRALAALAPROALASERPROGLN
2   GLNILEARGASPARGLEULEUGLNALAILE
3   ASPPROGLNSERASNILEARGASNMETVAL
4   ALAVALLEUGLUVALILESERSERLEUGLU
5   LYSTYRPROILETHRLYSGLUALALEUGLU
6   GLUTHRARGLEUGLYLYSLEUILEASNASP
7   VALARGLYSLYSTHRLYSASNGLUGLULEU
8   ALALYSARGALALYSLYSLEULEUARGSER
9   TRPGLNLYSLEUILEGLUPROALAHISGLN
10   HISGLUALA

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNHAsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_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

Related Database Links:

UNP O95402
AlphaFold Q0VGB6

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