BMRB Entry 15149

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15149

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Title:
HMGB1 Full Length backbone assignment
Deposition date:
2007-02-26
Original release date:
2007-06-05
Authors:
Mollica, Luca; De Marchis, Francesco; Spitaleri, Andrea; Dallacosta, Corrado; Zamai, Moreno; Agresti, Alessandra; Trisciuoglio, Lisa; Bianchi, Marco; Musco, Giovanna
Citation:

Citation: Mollica, Luca; De Marchis, Francesco; Spitaleri, Andrea; Dallacosta, Corrado; Zamai, Moreno; Agresti, Alessandra; Trisciuoglio, Lisa; Bianchi, Marco; Musco, Giovanna. "Glycyrrhizin binds to high-mobility group box 1 protein and inhibits its cytokine activities"  Chem. Biol. 14, 431-441 (2007).
PubMed: 17462578

Assembly members:

Assembly members:
HMGB1_Full_Length, polymer, 214 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-24d

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HMGB1_Full_Length: GKGDPKKPRGKMSSYAFFVQ TCREEHKKKHPDASVNFSEF SKKCSERWKTMSAKEKGKFE DMAKADKARYEREMKTYIPP KGETKKKFKDPNAPKRPPSA FFLFCSEYRPKIKGEHPGLS IGDVAKKLGEMWNNTAADDK QPYEKKAAKLKEKYEKDIAA YRAKGKPDAAKKGVVKAEKS KKKKEEEDDEEDEEDEEEEE EEEDEDEEEDDDDE

Data sets:
Data typeCount
15N chemical shifts152
1H chemical shifts152

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HMGB1 Full Length1

Entities:

Entity 1, HMGB1 Full Length 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 Full Length, [U-100% 13C; U-100% 15N], 0.1 – 0.3 mM; NaCl 150 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Bruker AMX 500 MHz
  • Bruker AMX 600 MHz

Related Database Links:

BMRB 11147 15148 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
AlphaFold A9RA84 B0CM99 B1MTB0 P07156 P09429

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks