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 5558

Title: Sp100b SAND domain chemical shift assignments   PubMed: 11427895

Deposition date: 2002-10-15 Original release date: 2002-12-27

Authors: Bottomley, Matthew; Collard, Michael; Huggenvik, Jodi; Liu, Zhihong; Gibson, Toby; Sattler, Michael

Citation: Bottomley, Matthew; Collard, Michael; Huggenvik, Jodi; Liu, Zhihong; Gibson, Toby; Sattler, Michael. "The SAND domain structure defines a novel DNA-binding fold in transcriptional regulation"  Nat. Struct. Biol. 8, 626-633 (2001).

Assembly members:
SAND domain from human Sp100b protein, polymer, 104 residues, 12212 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):
SAND domain from human Sp100b protein: MKHHHHHHPMDENINFKQSE LPVTCGEVKGTLYKERFKQG TSKKCIQSEDKKWFTPREFE IEGDRGASKNWKLSIRCGGY TLKVLMENKFLPEPPSTRKK VTIK

Data sets:
Data typeCount
1H chemical shifts485
13C chemical shifts296
15N chemical shifts97
coupling constants30

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1Sp100b SAND domain1

Entities:

Entity 1, Sp100b SAND domain 104 residues - 12212 Da.

1   METLYSHISHISHISHISHISHISPROMET
2   ASPGLUASNILEASNPHELYSGLNSERGLU
3   LEUPROVALTHRCYSGLYGLUVALLYSGLY
4   THRLEUTYRLYSGLUARGPHELYSGLNGLY
5   THRSERLYSLYSCYSILEGLNSERGLUASP
6   LYSLYSTRPPHETHRPROARGGLUPHEGLU
7   ILEGLUGLYASPARGGLYALASERLYSASN
8   TRPLYSLEUSERILEARGCYSGLYGLYTYR
9   THRLEULYSVALLEUMETGLUASNLYSPHE
10   LEUPROGLUPROPROSERTHRARGLYSLYS
11   VALTHRILELYS

Samples:

Sample_1: SAND domain from human Sp100b protein, [U-95% 15N], 1.2 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 4 mM

Sample_2: SAND domain from human Sp100b protein, [U-95% 13C; U-15N], 1.2 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 4 mM

Sample_condition_1: pH: 6.5; temperature: 295 K; ionic strength: 0.07 M

Experiments:

NameSampleSample stateSample conditions
HNCAnot availablenot availablenot available
CBCANHnot availablenot availablenot available
CBCA(CO)NHnot availablenot availablenot available
H(C)CH TOCSYnot availablenot availablenot available
CCH TOCSYnot availablenot availablenot available
15N-edited NOESYnot availablenot availablenot available
13C-edited NOESYnot availablenot availablenot available

Software:

No software information available

NMR spectrometers:

  • Bruker DRX 500 MHz
  • Bruker DRX 600 MHz
  • Bruker DRX 700 MHz

Related Database Links:

PDB
EMBL CAH18143
GB AAC50743 AAY14879 EAW70929
REF NP_001193630 XP_004033374 XP_009442793 XP_009442794

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