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 11147

Title: Solution structure of the tandem HMG box domain from Human High mobility group protein B1

Deposition date: 2010-03-31 Original release date: 2011-04-01

Authors: Tomizawa, T.; Koshiba, S.; Watanabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.

Citation: Tomizawa, T.; Koshiba, S.; Watanabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.. "Solution structure of the tandem HMG box domain from Human High mobility group protein B1"  . ., .-..

Assembly members:
HMG box domain, polymer, 173 residues, Formula weight is not available

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

Experimental source:   Production method: cell free synthesis   Host organism: E. coli - cell free

Entity Sequences (FASTA):
HMG box domain: GSSGSSGMGKGDPKKPRGKM SSYAFFVQTCREEHKKKHPD ASVNFSEFSKKCSERWKTMS AKEKGKFEDMAKADKARYER EMKTYIPPKGETKKKFKDPN APKRPPSAFFLFCSEYRPKI KGEHPGLSIGDVAKKLGEMW NNTAADDKQPYEKKAAKLKE KYEKDIAAYRAKG

Data sets:
Data typeCount
13C chemical shifts769
15N chemical shifts168
1H chemical shifts1196

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HMG box domain1

Entities:

Entity 1, HMG box domain 173 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYMETGLYLYS
2   GLYASPPROLYSLYSPROARGGLYLYSMET
3   SERSERTYRALAPHEPHEVALGLNTHRCYS
4   ARGGLUGLUHISLYSLYSLYSHISPROASP
5   ALASERVALASNPHESERGLUPHESERLYS
6   LYSCYSSERGLUARGTRPLYSTHRMETSER
7   ALALYSGLULYSGLYLYSPHEGLUASPMET
8   ALALYSALAASPLYSALAARGTYRGLUARG
9   GLUMETLYSTHRTYRILEPROPROLYSGLY
10   GLUTHRLYSLYSLYSPHELYSASPPROASN
11   ALAPROLYSARGPROPROSERALAPHEPHE
12   LEUPHECYSSERGLUTYRARGPROLYSILE
13   LYSGLYGLUHISPROGLYLEUSERILEGLY
14   ASPVALALALYSLYSLEUGLYGLUMETTRP
15   ASNASNTHRALAALAASPASPLYSGLNPRO
16   TYRGLULYSLYSALAALALYSLEULYSGLU
17   LYSTYRGLULYSASPILEALAALATYRARG
18   ALALYSGLY

Samples:

sample_1: HMG box domain, [U-13C; U-15N], 1.09 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 296 K

Experiments:

NameSampleSample stateSample conditions
3D 13C-separated NOESYsample_1isotropiccondition_1
3D 15N-separated NOESYsample_1isotropiccondition_1

Software:

TOPSPIN v1.3, Bruker - collection

NMRPipe v20060524, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B.A. - data analysis

Kujira v0.9823, Kobayashi, N. - data analysis

CYANA v2.0.17, Guntert, P. - structure solution

NMR spectrometers:

  • Bruker AVANCE II 900 MHz

Related Database Links:

BMRB 15148 15149 15502
PDB
DBJ BAA09924 BAC29902 BAC34367 BAC34773 BAC38678
EMBL CAA31110 CAA31284 CAA56631 CAA68441 CAA68526
GB AAA20508 AAA31050 AAA40729 AAA57042 AAA64970
PIR S29857
REF NP_001002937 NP_001004034 NP_001075304 NP_001102843 NP_001162380
SP A9RA84 B0CM99 B1MTB0 P07156 P09429
TPG DAA21468 DAA23902

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