BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 25379

Title: Resonance assignment of PsbP an extrinsic protein from photosystem II of Spinacia oleracea

Deposition date: 2014-12-04 Original release date: 2015-06-04

Authors: Walnerova, Adriana; Chandra, Kousik; Rathner, Petr; Hornicakova, Michaela; Schlagnitweit, Judith; Mueller, Norbert

Citation: Walnerova, Adriana; Chandra, Kousik; Rathner, Petr; Hornicakova, Michaela; Schlagnitweit, Judith; Kohoutova, Jaroslava; Ettrich, Ruediger; Mueller, Norbert. "Resonance assignment of PsbP: an extrinsic protein from photosystem II of Spinacia oleracea"  Biomol. NMR Assign. ., .-. (2015).

Assembly members:
PsbP, polymer, 190 residues, Formula weight is not available

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: JR3133

Entity Sequences (FASTA):
PsbP: GSHMAYGEAANVFGKPKKNT EFMPYNGDGFKLLVPSKWNP SKEKEFPGQVLRYEDNFDAT SNLSVLVQPTDKKSITDFGS PEDFLSQVDYLLGKQAYFGK TDSEGGFDSGVVASANVLES STPVVDGKQYYSITVLTRTA DGDEGGKHQVIAATVKDGKL YICKAQAGDKRWFKGAKKFV ESATSSFSVA

Data sets:
Data typeCount
13C chemical shifts749
15N chemical shifts194
1H chemical shifts1254

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PsbP1

Entities:

Entity 1, PsbP 190 residues - Formula weight is not available

first four residues are from His-tag linker

1   GLYSERHISMETALATYRGLYGLUALAALA
2   ASNVALPHEGLYLYSPROLYSLYSASNTHR
3   GLUPHEMETPROTYRASNGLYASPGLYPHE
4   LYSLEULEUVALPROSERLYSTRPASNPRO
5   SERLYSGLULYSGLUPHEPROGLYGLNVAL
6   LEUARGTYRGLUASPASNPHEASPALATHR
7   SERASNLEUSERVALLEUVALGLNPROTHR
8   ASPLYSLYSSERILETHRASPPHEGLYSER
9   PROGLUASPPHELEUSERGLNVALASPTYR
10   LEULEUGLYLYSGLNALATYRPHEGLYLYS
11   THRASPSERGLUGLYGLYPHEASPSERGLY
12   VALVALALASERALAASNVALLEUGLUSER
13   SERTHRPROVALVALASPGLYLYSGLNTYR
14   TYRSERILETHRVALLEUTHRARGTHRALA
15   ASPGLYASPGLUGLYGLYLYSHISGLNVAL
16   ILEALAALATHRVALLYSASPGLYLYSLEU
17   TYRILECYSLYSALAGLNALAGLYASPLYS
18   ARGTRPPHELYSGLYALALYSLYSPHEVAL
19   GLUSERALATHRSERSERPHESERVALALA

Samples:

sample_1: PsbP, [U-13C; U-15N], 0.5 mM; Bis Tris 20 mM; EDTA 1 mM; sodium azide 50 uM; H2O 90%; D2O, [U-100% 2H], 10%; DSS, [U-99% 2H], 40 uM; Complete mini, EDTA-free 12 tablet/100mL

sample_conditions_1: ionic strength: 0.5 M; pH: 6; pressure: 1 atm; temperature: 313 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 HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
1D 1Hsample_1isotropicsample_conditions_1

Software:

CARA v1.8.4.2, Keller and Wuethrich - chemical shift assignment, peak picking

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

SPARKY v3.114, Goddard - data analysis

NMR spectrometers:

  • Bruker AVIII 700 MHz

Related Database Links:

PDB
EMBL CAA29055
GB KNA13956
PRF 1307179A
SP P12302
AlphaFold P12302

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