BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 15060

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15060

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry

Title: NMR structure of the murine DLC2 (deleted in liver cancer -2) SAM (sterile alpha motif) domain   PubMed: 17519008

Deposition date: 2006-11-30 Original release date: 2007-10-16

Authors: Donaldson, Logan

Citation: Kwan, Jamie; Donaldson, Logan. "The NMR structure of the murine DLC2 SAM domain reveals a variant fold that is similar to an anti-parallel four helix bundle"  BMC Struct. Biol. 7, .-. (2007).

Assembly members:
DLC2_SAM_domain, polymer, 107 residues, 7167.181 Da.

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

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

Entity Sequences (FASTA):
DLC2_SAM_domain: GSSHHHHHHSSGLVPRGSML VTKIQQEIEAKEACDWLRAA GFPQYAQLYEDSQFPINIAA VKKDHDFLERDLVEPLCRRL NTLNKCASMRLDVNFQRKKG DDSDEED

Data sets:
Data typeCount
13C chemical shifts321
15N chemical shifts94
1H chemical shifts559

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1monomeric DLC2 SAM domain1

Entities:

Entity 1, monomeric DLC2 SAM domain 107 residues - 7167.181 Da.

The expressed protein contains the following additional amino acids not present in the deposited structure. At the amino terminus - an terminal affinity tag, a thrombin cleavage sequence (GSSHHHHHHSSGLVPRGSM) and several disordered amino acids (LVTKIQQ). At the carboxy terminus, several disorderd amino acids (MRLDVNFQRKKGDDSDEED).

1   GLYSERSERHISHISHISHISHISHISSER
2   SERGLYLEUVALPROARGGLYSERMETLEU
3   VALTHRLYSILEGLNGLNGLUILEGLUALA
4   LYSGLUALACYSASPTRPLEUARGALAALA
5   GLYPHEPROGLNTYRALAGLNLEUTYRGLU
6   ASPSERGLNPHEPROILEASNILEALAALA
7   VALLYSLYSASPHISASPPHELEUGLUARG
8   ASPLEUVALGLUPROLEUCYSARGARGLEU
9   ASNTHRLEUASNLYSCYSALASERMETARG
10   LEUASPVALASNPHEGLNARGLYSLYSGLY
11   ASPASPSERASPGLUGLUASP

Samples:

primary_sample: DLC2 SAM domain, [U-99% 13C; U-99% 15N], 0.9 mM; sodium phosphate 20 mM; sodium chloride 0.15 M; sodium azide 0.05%

sample_conditions_1: ionic strength: 0.15 M; pH: 7.8; pressure: 1 atm; temperature: 295 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCprimary_sampleisotropicsample_conditions_1
2D 1H-13C HSQCprimary_sampleisotropicsample_conditions_1
3D CBCA(CO)NHprimary_sampleisotropicsample_conditions_1
3D C(CO)NHprimary_sampleisotropicsample_conditions_1
3D HNCOprimary_sampleisotropicsample_conditions_1
3D HNCACBprimary_sampleisotropicsample_conditions_1
3D H(CCO)NHprimary_sampleisotropicsample_conditions_1
3D HCCH-TOCSYprimary_sampleisotropicsample_conditions_1
3D 1H-15N NOESYprimary_sampleisotropicsample_conditions_1
3D 1H-13C NOESYprimary_sampleisotropicsample_conditions_1
3D 1H-13C aromatic NOESYprimary_sampleisotropicsample_conditions_1
2D aromatic (HB)CB(CGCD)HDprimary_sampleisotropicsample_conditions_1
2D aromatic (HB)CB(CGCDCE)HEprimary_sampleisotropicsample_conditions_1

Software:

X-PLOR NIH v2.16.0, Berjanskii, Neal, Wishart, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Guntert, Mumenthaler and Wuthrich, Johnson, One Moon Scientific, Schwieters, Kuszewski, Tjandra and Clore - chemical shift assignment, processing, refinement, structure solution

NMR spectrometers:

  • Varian NMRS 600 MHz

Related Database Links:

GB AAH27830 AGV29471 AGV29472 EDL05887 EDL05888
REF NP_001102530 NP_001156965 NP_666370 XP_005083217 XP_005083218
SP Q923Q2

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