BMRB Entry 17357

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17357

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
PsbQ protein
Deposition date:
2010-12-13
Original release date:
2011-02-01
Authors:
Hornicakova, Michaela; Muller, Norbert
Citation:

Citation: Horniakova, Michaela; Kohoutova, Jaroslava; Schlagnitweit, Judith; Wohlschlager, Christian; Ettrich, Rudiger; Fiala, Radovan; Schoefberger, Wolfgang; Muller, Norbert. "Backbone assignment and secondary structure of the PsbQ protein from photosystem II."  Biomol. NMR Assignments 5, 169-175 (2011).
PubMed: 21259076

Assembly members:

Assembly members:
PsbQ_protein, polymer, 149 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: spinach   Taxonomy ID: 3562   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Spinacea oleracea

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: JR2592

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PsbQ_protein: EARPIVVGPPPPLSGGLPGT ENSDQARDGTLPYTKDRFYL QPLPPTEAAQRAKVSASEIL NVKQFIDRKAWPSLQNDLRL RASYLRYDLKTVISAKPKDE KKSLQELTSKLFSSIDNLDH AAKIKSPTEAEKYYGQTVSN INEVLAKLG

Data sets:
Data typeCount
13C chemical shifts401
15N chemical shifts112
1H chemical shifts448

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PsbQ1

Entities:

Entity 1, PsbQ 149 residues - Formula weight is not available

1   GLUALAARGPROILEVALVALGLYPROPRO
2   PROPROLEUSERGLYGLYLEUPROGLYTHR
3   GLUASNSERASPGLNALAARGASPGLYTHR
4   LEUPROTYRTHRLYSASPARGPHETYRLEU
5   GLNPROLEUPROPROTHRGLUALAALAGLN
6   ARGALALYSVALSERALASERGLUILELEU
7   ASNVALLYSGLNPHEILEASPARGLYSALA
8   TRPPROSERLEUGLNASNASPLEUARGLEU
9   ARGALASERTYRLEUARGTYRASPLEULYS
10   THRVALILESERALALYSPROLYSASPGLU
11   LYSLYSSERLEUGLNGLULEUTHRSERLYS
12   LEUPHESERSERILEASPASNLEUASPHIS
13   ALAALALYSILELYSSERPROTHRGLUALA
14   GLULYSTYRTYRGLYGLNTHRVALSERASN
15   ILEASNGLUVALLEUALALYSLEUGLY

Samples:

sample_1: PsbQ protein, [U-99% 13C; U-99% 15N], 0.5 mM; D2O 10%; H2O 90%; sodium phosphate 20 mM

sample_conditions_1: ionic strength: 20 mM; pH: 7.00; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 13C detected CBCACONsample_1isotropicsample_conditions_1
3D 13C detected CBCANCOsample_1isotropicsample_conditions_1
2D 13C detected CONsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, peak picking

TOPSPIN v2.1, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker Avance 750 MHz
  • Bruker DRX 600 MHz
  • Bruker Avance 600 MHz
  • Bruker DRX 500 MHz

Related Database Links:

BMRB 25350
PDB
EMBL CAA29056
GB KNA09121
PRF 1307179B
SP P12301
AlphaFold P12301

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