BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 30398

Title: Solution structure of Musashi2 RRM1

Deposition date: 2018-01-25 Original release date: 2019-01-24

Authors: Xing, M.; Lan, L.; Douglas, J.; Gao, P.; Hanzlik, R.; Xu, L.

Citation: Xing, M.; Lan, L.; Douglas, J.; Gao, P.; Hanzlik, R.; Xu, L.. "Solution structure of Musashi2 RRM1"  To be Published ., .-..

Assembly members:
entity_1, polymer, 115 residues, 13154.963 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

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

Entity Sequences (FASTA):
entity_1: MHHHHHHSTSVDLGTENLYF QSNAGKMFIGGLSWQTSPDS LRDYFSKFGEIRECMVMRDP TTKRSRGFGFVTFADPASVD KVLGQPHHELDSKTIDPKVA FPRRAQPKMVTRTKK

Data sets:
Data typeCount
13C chemical shifts477
15N chemical shifts107
1H chemical shifts742

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 115 residues - 13154.963 Da.

1   METHISHISHISHISHISHISSERTHRSER
2   VALASPLEUGLYTHRGLUASNLEUTYRPHE
3   GLNSERASNALAGLYLYSMETPHEILEGLY
4   GLYLEUSERTRPGLNTHRSERPROASPSER
5   LEUARGASPTYRPHESERLYSPHEGLYGLU
6   ILEARGGLUCYSMETVALMETARGASPPRO
7   THRTHRLYSARGSERARGGLYPHEGLYPHE
8   VALTHRPHEALAASPPROALASERVALASP
9   LYSVALLEUGLYGLNPROHISHISGLULEU
10   ASPSERLYSTHRILEASPPROLYSVALALA
11   PHEPROARGARGALAGLNPROLYSMETVAL
12   THRARGTHRLYSLYS

Samples:

sample_1: MSI2-RRM1, [U-90% 15N], 0.5 mM; NaCl 150 mM

sample_2: MSI2-RRM1, [U-95% 13C; U-90% 15N], 0.7 mM; NaCl 150 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HNCACOsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1

Software:

CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure calculation

CcpNMR, CCPN - chemical shift assignment, peak picking

NMRView, Johnson, One Moon Scientific - peak picking

TOPSPIN v2.1pl6, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker AvanceIII 600 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts