BMRB Entry 25496

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25496
MolProbity Validation Chart

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Title:
NMR structure of the RRM3 domain of Gbp2
Deposition date:
2015-02-23
Original release date:
2015-11-30
Authors:
Martinez-Lumbreras, Santiago; Seraphin, Bertrand; Perez-Canadillas, Jose Manuel
Citation:

Citation: Martinez-Lumbreras, Santiago; Taverniti, Valerio; Zorrilla, Silvia; Seraphin, Bertrand; Perez-Canadillas, Jose Manuel. "Gbp2 interacts with THO/TREX through a novel type of RRM domain"  Nucleic Acids Res. 44, 437-448 (2016).
PubMed: 26602689

Assembly members:

Assembly members:
RRM3, polymer, 101 residues, 11094.291 Da.

Natural source:

Natural source:   Common Name: Baker's Yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RRM3: GSHIDETAAKFTEGVNPGGD RNCFIYCSNLPFSTARSDLF DLFGPIGKINNAELKPQENG QPTGVAVVEYENLVDADFCI QKLNNYNYGGCSLQISYARR D

Data sets:
Data typeCount
13C chemical shifts369
15N chemical shifts112
1H chemical shifts663

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1RRM3 domain of Gbp21

Entities:

Entity 1, RRM3 domain of Gbp2 101 residues - 11094.291 Da.

From 329 to 427

1   GLYSERHISILEASPGLUTHRALAALALYS
2   PHETHRGLUGLYVALASNPROGLYGLYASP
3   ARGASNCYSPHEILETYRCYSSERASNLEU
4   PROPHESERTHRALAARGSERASPLEUPHE
5   ASPLEUPHEGLYPROILEGLYLYSILEASN
6   ASNALAGLULEULYSPROGLNGLUASNGLY
7   GLNPROTHRGLYVALALAVALVALGLUTYR
8   GLUASNLEUVALASPALAASPPHECYSILE
9   GLNLYSLEUASNASNTYRASNTYRGLYGLY
10   CYSSERLEUGLNILESERTYRALAARGARG
11   ASP

Samples:

sample_1: RRM3, [U-100% 13C; U-100% 15N], 0.8 mM; potassium phosphate 25 mM; sodium chloride 25 mM; DTT 0.1 mM; D2O 10%; H2O 90%

sample_2: RRM3, [U-100% 13C; U-100% 15N], 0.8 mM; potassium phosphate 25 mM; sodium chloride 25 mM; DTT 0.1 mM; D2O 100%

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

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

TOPSPIN, Bruker Biospin - collection

CcpNMR_Analysis, CCPN - chemical shift assignment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Bruker Avance 800 MHz

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