BMRB Entry 11450

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11450
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:
1H, 13C, and 15N Chemical Shift Assignments for Musashi1 RBD1:r(GUAGU) complex
Deposition date:
2011-06-26
Original release date:
2012-08-17
Authors:
Ohyama, Takako; Nagata, Takashi; Tsuda, Kengo; Imai, Takao; Okano, Hideyuki; Yamazaki, Toshio; Katahira, Masato
Citation:

Citation: Ohyama, Takako; Nagata, Takashi; Tsuda, Kengo; Imai, Takao; Okano, Hideyuki; Yamazaki, Toshio; Katahira, Masato. "Structure of Musashi1 in Complex with Target RNA: The Role of Aromatic Stacking Interactions"  Nucleic Acids Res. 40, 3218-3231 (2012).
PubMed: 22140116

Assembly members:

Assembly members:
entity_1, polymer, 109 residues, 9613.169 Da.
entity_2, polymer, 5 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGSSHHHHHHSSGLVPRGSH MGSSGCKMFIGGLSWQTTQE GLREYFGQFGEVKECLVMRD PLTKRSRGFGFVTFMDQAGV DKVLAQSRHELDSKTIDPKV AFPRRAQPK
entity_2: GUAGU

Data sets:
Data typeCount
13C chemical shifts386
15N chemical shifts90
1H chemical shifts605

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Msi1 RBD11
2RNA2

Entities:

Entity 1, Msi1 RBD1 109 residues - 9613.169 Da.

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METGLYSERSERGLYCYSLYSMETPHEILE
4   GLYGLYLEUSERTRPGLNTHRTHRGLNGLU
5   GLYLEUARGGLUTYRPHEGLYGLNPHEGLY
6   GLUVALLYSGLUCYSLEUVALMETARGASP
7   PROLEUTHRLYSARGSERARGGLYPHEGLY
8   PHEVALTHRPHEMETASPGLNALAGLYVAL
9   ASPLYSVALLEUALAGLNSERARGHISGLU
10   LEUASPSERLYSTHRILEASPPROLYSVAL
11   ALAPHEPROARGARGALAGLNPROLYS

Entity 2, RNA 5 residues - Formula weight is not available

1   GUAGU

Samples:

sample_1: Msi1 RBD1, [U-13C; U-15N], 300 uM; RNA 300 uM; MES 20 mM; DTT 5 mM; H2O 95%; D2O 5%

sample_conditions_1: pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D DQF-COSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
2D 13C-15N [f1,f2]-filtered NOESYsample_1isotropicsample_conditions_1
2D 13C-15N [f2]-filtered NOESYsample_1isotropicsample_conditions_1

Software:

AMBER v9, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - geometry optimization

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB

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