BMRB Entry 25350

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25350
MolProbity Validation Chart

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Title:
Solution structure of PsbQ from spinacia oleracea
Deposition date:
2014-11-19
Original release date:
2015-07-27
Authors:
Rathner, Petr; Mueller, Norbert; Wimmer, Reinhard; Chandra, Kousik
Citation:

Citation: Rathner, Petr; Walnerova, Adriana; Hornicakova, Michaela; Wohlschlager, Christian; Chandra, Kousik; Kohoutova, Jaroslava; Ettrich, Ruediger; Wimmer, Reinhard; Mueller, Norbert. "Solution NMR and molecular dynamics reveal a persistent alpha helix within the dynamic region of PsbQ from photosystem II of higher plants"  Proteins 83, 1677-1686 (2015).
PubMed: 26138376

Assembly members:

Assembly members:
PsbQ, polymer, 149 residues, 16544.906 Da.

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

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

Data sets:
Data typeCount
13C chemical shifts638
15N chemical shifts148
1H chemical shifts924

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PsbQ1

Entities:

Entity 1, PsbQ 149 residues - 16544.906 Da.

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, [U-13C; U-15N], 0.8 mM; sodium phosphate 20 mM; sodium azide 50 uM; EDTA 1 mM; D2O, [U-100% 2H], 10%; H2O 90%

sample_2: PsbQ, [U-13C; U-15N], 0.8 mM; sodium phosphate 20 mM; sodium azide 50 uM; EDTA 1 mM; D2O, [U-100% 2H], 100%

sample_conditions_1: ionic strength: 0.06 M; pH: 7.0; pressure: 1 atm; temperature: 298.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HC(C)H-TOCSYsample_1isotropicsample_conditions_1
3D (H)C(C)(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HC(C)H-COSYsample_1isotropicsample_conditions_1
3D TOCSY-HSQCsample_1isotropicsample_conditions_1
2D (HB)CB(CGCD)HDsample_1isotropicsample_conditions_1
2D (HB)CB(CGCDCE)HEsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1

Software:

TOPSPIN v3.1, Bruker Biospin - collection, data analysis

CARA v1.5.5, Keller and Wuthrich - chemical shift assignment, peak picking

TALOS, Cornilescu, Delaglio and Bax - data analysis

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - geometry optimization, structure solution

YASARA v12.1.19, YASARA Biosciences - geometry optimization, refinement

NMR spectrometers:

  • Bruker AVIII 700 MHz

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