BMRB Entry 17693

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR17693
MolProbity Validation Chart

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Title:
RRM domain of mRNA export adaptor REF2-I bound to HVS ORF57 peptide
Deposition date:
2011-06-07
Original release date:
2012-06-11
Authors:
Tunnicliffe, Richard; Hautbergue, G.; Kalra, P.; Wilson, S.; Golovanov, A.; Golova, A.
Citation:

Citation: Tunnicliffe, Richard; Hautbergue, G.; Kalra, P.; Jackson, B.; Whitehouse, A.; Wilson, S.; Golovanov, A.. "Structural Basis for the Recognition of Cellular mRNA Export Factor REF by Herpes Viral Proteins HSV-1 ICP27 and HVS ORF57"  PLoS Pathog. 7, e1001244-e1001244 (2011).
PubMed: 21253573

Assembly members:

Assembly members:
RNA_AND_EXPORT_FACTOR-BINDING_PROTEIN_2, polymer, 124 residues, 13567.0128 Da.
52_KDA_IMMEDIATE-EARLY_PHOSPHOPROTEIN, polymer, 23 residues, 2504.8024 Da.

Natural source:

Natural source:   Common Name: herpesvirus saimiri HVS   Taxonomy ID: 10381   Superkingdom: Viruses   Kingdom: not available   Genus/species: Rhadinovirus Saimiriine herpesvirus 2

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET24b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RNA_AND_EXPORT_FACTOR-BINDING_PROTEIN_2: MASMTGGQQMGRDPDKWQHD LFDSGCGGGEGVETGAKLLV SNLDFGVSDADIQELFAEFG TLKKAAVDYDRSGRSLGTAD VHFERRADALKAMKQYKGVP LDGRPMDIQLVASQIDLEHH HHHH
52_KDA_IMMEDIATE-EARLY_PHOSPHOPROTEIN: GPLGSSCKTSWADRVREAAA QRR

Data sets:
Data typeCount
13C chemical shifts535
15N chemical shifts153
1H chemical shifts922

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1RNA AND EXPORT FACTOR-BINDING PROTEIN 21
252 KDA IMMEDIATE-EARLY PHOSPHOPROTEIN2

Entities:

Entity 1, RNA AND EXPORT FACTOR-BINDING PROTEIN 2 124 residues - 13567.0128 Da.

1   METALASERMETTHRGLYGLYGLNGLNMET
2   GLYARGASPPROASPLYSTRPGLNHISASP
3   LEUPHEASPSERGLYCYSGLYGLYGLYGLU
4   GLYVALGLUTHRGLYALALYSLEULEUVAL
5   SERASNLEUASPPHEGLYVALSERASPALA
6   ASPILEGLNGLULEUPHEALAGLUPHEGLY
7   THRLEULYSLYSALAALAVALASPTYRASP
8   ARGSERGLYARGSERLEUGLYTHRALAASP
9   VALHISPHEGLUARGARGALAASPALALEU
10   LYSALAMETLYSGLNTYRLYSGLYVALPRO
11   LEUASPGLYARGPROMETASPILEGLNLEU
12   VALALASERGLNILEASPLEUGLUHISHIS
13   HISHISHISHIS

Entity 2, 52 KDA IMMEDIATE-EARLY PHOSPHOPROTEIN 23 residues - 2504.8024 Da.

1   GLYPROLEUGLYSERSERCYSLYSTHRSER
2   TRPALAASPARGVALARGGLUALAALAALA
3   GLNARGARG

Samples:

sample_1: RNA_AND_EXPORT_FACTOR-BINDING_PROTEIN_2, [U-99% 13C; U-99% 15N], 1 mM; 52 KDA IMMEDIATE-EARLY PHOSPHOPROTEIN, [U-99% 13C; U-99% 15N], 3 mM; NaCl 50 mM

sample_2: RNA_AND_EXPORT_FACTOR-BINDING_PROTEIN_2, [U-99% 13C; U-99% 15N], 3 mM; 52 KDA IMMEDIATE-EARLY PHOSPHOPROTEIN, [U-99% 13C; U-99% 15N], 1 mM; NaCl 50 mM

sample_conditions_1: ionic strength: 50.000 mM; pH: 6.200; pressure: 1.000 atm; temperature: 303.000 K

Experiments:

NameSampleSample stateSample conditions
HSQCsample_1solutionsample_conditions_1
HNCAsample_1solutionsample_conditions_1
CBCA(CO)NHsample_1solutionsample_conditions_1
HNCACBsample_1solutionsample_conditions_1
HNCOsample_1solutionsample_conditions_1
HN(CA)COsample_1solutionsample_conditions_1
TOCSY-HSQCsample_1solutionsample_conditions_1
HBHA(CO)NHsample_1solutionsample_conditions_1
HCCH-TOCSYsample_1solutionsample_conditions_1
CCH-TOCSYsample_1solutionsample_conditions_1
NOESY-HSQCsample_1solutionsample_conditions_1
Filtered 13C-NOESYsample_1solutionsample_conditions_1
HSQCsample_2solutionsample_conditions_1
HNCAsample_2solutionsample_conditions_1
CBCA(CO)NHsample_2solutionsample_conditions_1
HNCACBsample_2solutionsample_conditions_1
HNCOsample_2solutionsample_conditions_1
TOCSY-HSQCsample_2solutionsample_conditions_1
HBHA(CO)NHsample_2solutionsample_conditions_1
NOESY-HSQCsample_2solutionsample_conditions_1
NOESY-HSQC HSQCsample_1solutionsample_conditions_1

Software:

AutoDep v4.3, PDBe - collection

CYANA v2.1, P. Guntert et al. - chemical shift assignment

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Varian Inova 800 MHz

Related Database Links:

UNP REFP2_MOUSE IE63_SHV21
BMRB 16683 16697 16698 17663 17664 7435
PDB
EMBL CAA45680 CAC84353 CAC84354
GB AAA46125 AAA66558
PIR WMBEHA
REF NP_040259
SP P13199
AlphaFold Q8C869 P13199 P13199

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