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 15502

Title: Mapping intramolecular interactions between domains in HMGB1 using a tail-truncation approach   PubMed: 17988686

Deposition date: 2007-10-02 Original release date: 2008-02-11

Authors: Watson, Matthew; Stott, Katherine; Thomas, Jean

Citation: Watson, Matthew; Stott, Katherine; Thomas, Jean. "Mapping intramolecular interactions between domains in HMGB1 using a tail-truncation approach"  J. Mol. Biol. 374, 1286-1297 (2007).

Assembly members:
HMGB1, polymer, 214 residues, Formula weight is not available

Natural source:   Common Name: Rat   Taxonomy ID: 10116   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Rattus norvegicus

Experimental source:   Production method: recombinant technology' 'Escherichia coli

Entity Sequences (FASTA):
HMGB1: GKGDPKKPRGKMSSYAFFVQ TCREEHKKKHPDASVNFSEF SKKCSERWKTMSAKEKGKFE DMAKADKARYEREMKTYIPP KGETKKKFKDPNAPKRPPSA FFLFCSEYRPKIKGEHPGLS IGDVAKKLGEMWNNTAADDK QPYEKKAAKLKEKYEKDIAA YRAKGKPDAAKKGVVKAEKS KKKKEEEDDEEDEEDEEEEE EEEDEDEEEDDDDE

Data sets:
Data typeCount
15N chemical shifts173
1H chemical shifts179

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HMGB11

Entities:

Entity 1, HMGB1 214 residues - Formula weight is not available

1   GLYLYSGLYASPPROLYSLYSPROARGGLY
2   LYSMETSERSERTYRALAPHEPHEVALGLN
3   THRCYSARGGLUGLUHISLYSLYSLYSHIS
4   PROASPALASERVALASNPHESERGLUPHE
5   SERLYSLYSCYSSERGLUARGTRPLYSTHR
6   METSERALALYSGLULYSGLYLYSPHEGLU
7   ASPMETALALYSALAASPLYSALAARGTYR
8   GLUARGGLUMETLYSTHRTYRILEPROPRO
9   LYSGLYGLUTHRLYSLYSLYSPHELYSASP
10   PROASNALAPROLYSARGPROPROSERALA
11   PHEPHELEUPHECYSSERGLUTYRARGPRO
12   LYSILELYSGLYGLUHISPROGLYLEUSER
13   ILEGLYASPVALALALYSLYSLEUGLYGLU
14   METTRPASNASNTHRALAALAASPASPLYS
15   GLNPROTYRGLULYSLYSALAALALYSLEU
16   LYSGLULYSTYRGLULYSASPILEALAALA
17   TYRARGALALYSGLYLYSPROASPALAALA
18   LYSLYSGLYVALVALLYSALAGLULYSSER
19   LYSLYSLYSLYSGLUGLUGLUASPASPGLU
20   GLUASPGLUGLUASPGLUGLUGLUGLUGLU
21   GLUGLUGLUASPGLUASPGLUGLUGLUASP
22   ASPASPASPGLU

Samples:

sample_1: HMGB1, [U-98% 15N], 0.3-1.4 mM

sample_conditions_1: ionic strength: 0.001 M; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1

Software:

Analysis, CCPN - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker DRX 500 MHz
  • Bruker DRX 800 MHz

Related Database Links:

BMRB 11147 15148 15149
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