BMRB

Biological Magnetic Resonance Data Bank


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BMRB Entry 19642

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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/BMR19642
MolProbity Validation Chart

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Title: NMR structure of the first RRM domain of the protein RBM39 from homo sapiens

Deposition date: 2013-12-02 Original release date: 2013-12-20

Authors: Serrano, Pedro; Geralt, Michael; Dutta, Samit; Wuthrich, Kurt

Citation: Serrano, Pedro; Wuthrich, Kurt; Geralt, Michael; Dutta, Samit. "NMR structure of the first RRM domain of the protein RBM39 from homo sapiens"  Not known ., .-..

Assembly members:
entity, polymer, 152 residues, 10574.261 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: GHMNLTPEERDARTVFCMQL AARIRPRDLEEFFSTVGKVR DVRMISDRNSRRSKGIAYVE FVDVSSVPLAIGLTGQRVLG VPIIVQASQAEKNRRRSKGI AYVEFVDVSSVPLAIGLTGQ RVLGVPIIVQASQAEKNRVP IIVQASQAEKNR

Data sets:
Data typeCount
13C chemical shifts385
15N chemical shifts95
1H chemical shifts643

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 152 residues - 10574.261 Da.

1   GLYHISMETASNLEUTHRPROGLUGLUARG
2   ASPALAARGTHRVALPHECYSMETGLNLEU
3   ALAALAARGILEARGPROARGASPLEUGLU
4   GLUPHEPHESERTHRVALGLYLYSVALARG
5   ASPVALARGMETILESERASPARGASNSER
6   ARGARGSERLYSGLYILEALATYRVALGLU
7   PHEVALASPVALSERSERVALPROLEUALA
8   ILEGLYLEUTHRGLYGLNARGVALLEUGLY
9   VALPROILEILEVALGLNALASERGLNALA
10   GLULYSASNARGARGARGSERLYSGLYILE
11   ALATYRVALGLUPHEVALASPVALSERSER
12   VALPROLEUALAILEGLYLEUTHRGLYGLN
13   ARGVALLEUGLYVALPROILEILEVALGLN
14   ALASERGLNALAGLULYSASNARGVALPRO
15   ILEILEVALGLNALASERGLNALAGLULYS
16   ASNARG

Samples:

sample_1: entity, [U-98% 13C; U-98% 15N], 0.6 mM; sodium chloride 100 mM; sodium acetate, [U-99% 2H], 10 mM; sodium azide 5 mM; DTT 2 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.220 M; pH: 5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
4D APSY HACANHsample_1isotropicsample_conditions_1
5D APSY CBCACONHsample_1isotropicsample_conditions_1
5D APSY HACACONHsample_1isotropicsample_conditions_1

Software:

CYANA, G ntert P. - refinement

Opalp, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

TOPSPIN, Bruker Biospin - collection, data analysis, processing

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAE22477 BAE27657 BAE32977 BAG54289 BAG59582
EMBL CAD97833 CAE45833 CAE45890 CAH18281 CAH90627
GB AAA16346 AAA16347 AAH04000 AAH30493 AAH82607
REF NP_001013225 NP_001125339 NP_001162566 NP_001164806 NP_001193433
SP Q14498 Q5RC80 Q8VH51
TPG DAA23046

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