BMRB Entry 25499

Click here to enlarge.

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/BMR25499
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
NMR structure of the RRM3 domain of Hrb1
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, 100 residues, 11106.278 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: GSVNEEARKFTENVVGGGER NRLIYCSNLPFSTAKSDLYD LFETIGKVNNAELRYDSKGA PTGIAVVEYDNVDDADVCIE RLNNYNYGGCDLDISYAKRL

Data sets:
Data typeCount
13C chemical shifts288
15N chemical shifts113
1H chemical shifts665

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RRM31

Entities:

Entity 1, RRM3 100 residues - 11106.278 Da.

From 357 to 454

1   GLYSERVALASNGLUGLUALAARGLYSPHE
2   THRGLUASNVALVALGLYGLYGLYGLUARG
3   ASNARGLEUILETYRCYSSERASNLEUPRO
4   PHESERTHRALALYSSERASPLEUTYRASP
5   LEUPHEGLUTHRILEGLYLYSVALASNASN
6   ALAGLULEUARGTYRASPSERLYSGLYALA
7   PROTHRGLYILEALAVALVALGLUTYRASP
8   ASNVALASPASPALAASPVALCYSILEGLU
9   ARGLEUASNASNTYRASNTYRGLYGLYCYS
10   ASPLEUASPILESERTYRALALYSARGLEU

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 TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_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