BMRB Entry 36059

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR36059
MolProbity Validation Chart

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Title:
Solution structure of musashi1 RBD2 in complex with RNA
Deposition date:
2017-02-09
Original release date:
2017-12-11
Authors:
Iwaoka, R.; Nagata, T.; Tsuda, K.; Imai, T.; Okano, H.; Kobayashi, N.; Katahira, M.
Citation:

Citation: Iwaoka, R.; Nagata, T.; Tsuda, K.; Imai, T.; Okano, H.; Kobayashi, N.; Katahira, M.. "Structural Insight into the Recognition of r(UAG) by Musashi-1 RBD2, and Construction of a Model of Musashi-1 RBD1-2 Bound to the Minimum Target RNA"  Molecules 22, 1207-1207 (2017).
PubMed: 28753936

Assembly members:

Assembly members:
entity_1, polymer, 96 residues, 10945.506 Da.
entity_2, polymer, 5 residues, 1586.992 Da.

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: GSHMKKIFVGGLSVNTTVED VKHYFEQFGKVDDAMLMFDK TTNRHRGFGFVTFESEDIVE KVCEIHFHEINNKMVECKKA QPKEVMSPTGSARGRS
entity_2: GUAGU

Data sets:
Data typeCount
13C chemical shifts416
15N chemical shifts98
1H chemical shifts614

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 96 residues - 10945.506 Da.

1   GLYSERHISMETLYSLYSILEPHEVALGLY
2   GLYLEUSERVALASNTHRTHRVALGLUASP
3   VALLYSHISTYRPHEGLUGLNPHEGLYLYS
4   VALASPASPALAMETLEUMETPHEASPLYS
5   THRTHRASNARGHISARGGLYPHEGLYPHE
6   VALTHRPHEGLUSERGLUASPILEVALGLU
7   LYSVALCYSGLUILEHISPHEHISGLUILE
8   ASNASNLYSMETVALGLUCYSLYSLYSALA
9   GLNPROLYSGLUVALMETSERPROTHRGLY
10   SERALAARGGLYARGSER

Entity 2, entity_2 5 residues - 1586.992 Da.

1   GUAGU

Samples:

sample_1: Msi1 RBD2, [U-100% 13C; U-100% 15N], 300 uM; RNA (5'-R(*GP*UP*AP*GP*U)-3') 300 uM; MES 20 mM; sodium chloride 100 mM; H2O 95%; D2O, [U-2H], 5%

sample_conditions_1: ionic strength: 100 mM; 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
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1

Software:

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

MagRO, Kobayashi - chemical shift assignment

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker AvanceIII 950 MHz

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