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 18167

Title: Solution Structure of Cyanobacterial PsbP (CyanoP) from Synechocystis sp. PCC 6803   PubMed: 22414666

Deposition date: 2011-12-28 Original release date: 2012-03-23

Authors: Jackson, Simon; Hinds, Mark; Eaton-Rye, Julian

Citation: Jackson, Simon; Hinds, Mark; Eaton-Rye, Julian. "Solution structure of CyanoP from Synechocystis sp. PCC 6803: new insights on the structural basis for functional specialization amongst PsbP family proteins."  Biochim. Biophys. Acta 1817, 1331-1338 (2012).

Assembly members:
entity, polymer, 170 residues, 18744.742 Da.

Natural source:   Common Name: Synechocystis sp.   Taxonomy ID: 1143   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Synechocystis sp.

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

Entity Sequences (FASTA):
entity: GPLGSCGGVGIASLQRYSDT KDGYEFLYPNGWIGVDVKGA SPGVDVVFRDLIERDENLSV IISEIPSDKTLTDLGTATDV GYRFMKTVNDASQGDRQAEL INAEARDEDGQVYYTLEYRV LVGDNVERHDLASVTTNRGK LITFDLSTAEDRWDTVKSLF DTVASSFHVY

Data sets:
Data typeCount
13C chemical shifts647
15N chemical shifts177
1H chemical shifts1112

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PsbP1

Entities:

Entity 1, PsbP 170 residues - 18744.742 Da.

There are 5 N-terminal vector derived residues (GPLGS). The sequence represents the enzymatically processed PsbP.

1   GLYPROLEUGLYSERCYSGLYGLYVALGLY
2   ILEALASERLEUGLNARGTYRSERASPTHR
3   LYSASPGLYTYRGLUPHELEUTYRPROASN
4   GLYTRPILEGLYVALASPVALLYSGLYALA
5   SERPROGLYVALASPVALVALPHEARGASP
6   LEUILEGLUARGASPGLUASNLEUSERVAL
7   ILEILESERGLUILEPROSERASPLYSTHR
8   LEUTHRASPLEUGLYTHRALATHRASPVAL
9   GLYTYRARGPHEMETLYSTHRVALASNASP
10   ALASERGLNGLYASPARGGLNALAGLULEU
11   ILEASNALAGLUALAARGASPGLUASPGLY
12   GLNVALTYRTYRTHRLEUGLUTYRARGVAL
13   LEUVALGLYASPASNVALGLUARGHISASP
14   LEUALASERVALTHRTHRASNARGGLYLYS
15   LEUILETHRPHEASPLEUSERTHRALAGLU
16   ASPARGTRPASPTHRVALLYSSERLEUPHE
17   ASPTHRVALALASERSERPHEHISVALTYR

Samples:

sample_1: PsbP, [U-100% 15N], 0.4 mM; TCEP 5 mM; sodium phosphate 25 mM; sodium chloride 10 mM; H2O 95%; D2O 5%

sample_2: PsbP, [U-100% 13C; U-100% 15N], 0.4 mM; TCEP 5 mM; sodium phosphate 25 mM; sodium chloride 10 mM; H2O 95%; D2O 5%

sample_conditions_1: pH: 6.7; pressure: 1 atm; temperature: 298.15 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2, Bruker Biospin - collection, processing

ANALYSIS, CCPN - data analysis

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

TALOS, Cornilescu, Delaglio and Bax - data analysis

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAA18019 BAK50191 BAL29190 BAL32359 BAL35528
GB AGF51707 ALJ67700
REF WP_010872644

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