BMRB Entry 27179

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27179

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Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for the Hepatitis B Virus X protein (HBx)
Deposition date:
2017-07-14
Original release date:
2019-03-15
Authors:
Delgado, Leonildo; Grzesiek, Stephan
Citation:

Citation: Delgado, Leonildo; Grzesiek, Stephan; Delgado, Leonildo; Grzesiek, Stephan. "1H, 15N, 13C assignments and 15N relaxation data of the intrinsically disordered hepatitis B virus X protein (HBx) in a detergent mixture"  The BMRB entry is the only known published source for the data..

Assembly members:

Assembly members:
Hepatitis_B_virus_X_protein_(HBx), polymer, 177 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pROX180-9CS N-ter

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Hepatitis_B_virus_X_protein_(HBx): MGSSHHHHHHSSGRENLYFQ GSGSAARLSSQLDPARDVLS LRPVGAESRGRPFSGSLGTL SSPSPSAVPTDHGAHLSLRG LPVSAFSSAGPSALRFTSAR RMETTVNAHQILPKVLHKRT LGLSAMSTTDLEAYFKDSLF KDWEELGEEIRLKVFVLGGS RHKLVSAPAPSNFFTSA

Data typeCount
13C chemical shifts450
15N chemical shifts115
1H chemical shifts629
T1 relaxation values219
T2 relaxation values219
heteronuclear NOE values224

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Hepatitis B virus X protein (HBx)1

Entities:

Entity 1, Hepatitis B virus X protein (HBx) 177 residues - Formula weight is not available

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYARGGLUASNLEUTYRPHEGLN
3   GLYSERGLYSERALAALAARGLEUSERSER
4   GLNLEUASPPROALAARGASPVALLEUSER
5   LEUARGPROVALGLYALAGLUSERARGGLY
6   ARGPROPHESERGLYSERLEUGLYTHRLEU
7   SERSERPROSERPROSERALAVALPROTHR
8   ASPHISGLYALAHISLEUSERLEUARGGLY
9   LEUPROVALSERALAPHESERSERALAGLY
10   PROSERALALEUARGPHETHRSERALAARG
11   ARGMETGLUTHRTHRVALASNALAHISGLN
12   ILELEUPROLYSVALLEUHISLYSARGTHR
13   LEUGLYLEUSERALAMETSERTHRTHRASP
14   LEUGLUALATYRPHELYSASPSERLEUPHE
15   LYSASPTRPGLUGLULEUGLYGLUGLUILE
16   ARGLEULYSVALPHEVALLEUGLYGLYSER
17   ARGHISLYSLEUVALSERALAPROALAPRO
18   SERASNPHEPHETHRSERALA

Samples:

sample_1: Hepatitis B virus X protein (HBx), [U-100% 13C; U-100% 15N], 0.7 mM; sodium acetate 20 mM; EDTA 2 mM; DHPC 100 mM; Fos-Choline-12 2.8 mM; sodium chloride 0 mM

sample_conditions_1: pH: 4.0; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
4D (H)NNH)sample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

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

SPARKY, Goddard - chemical shift assignment, peak picking

PIPP, Garrett - peak picking

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 600 MHz

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