BMRB Entry 18375

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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/BMR18375
MolProbity Validation Chart

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Title:
NMR solution structure of staphyloxanthin biosynthesis protein
Deposition date:
2012-04-03
Original release date:
2012-05-01
Authors:
Zhang, Yongbo; Winsor, James; Anderson, Wayne; Radhakrishnan, Ishwar
Citation:

Citation: Zhang, Yongbo; Winsor, James; Anderson, Wayne; Radhakrishnan, Ishwar. "Solution structure of a putative S. aureus enzyme involved in the biosynthesis of staphyloxanthin"  The BMRB entry is the only known published source for the data..

Assembly members:

Assembly members:
entity, polymer, 113 residues, 11722.638 Da.

Natural source:

Natural source:   Common Name: Firmicutes   Taxonomy ID: 1280   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Staphylococcus aureus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET 15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GSSISHSGNLYTAGQCTWYV YDKVGGEIGSTWGNANNWAA AAQGAGFTVNHTPSKGAILQ SSEGPFGHVAYVESVNSDGS VTISEMNYSGGPFSVSSRTI SASEAGNYNYIHI

Data sets:
Data typeCount
13C chemical shifts433
15N chemical shifts119
1H chemical shifts681

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1staphyloxanthin biosynthesis protein1

Entities:

Entity 1, staphyloxanthin biosynthesis protein 113 residues - 11722.638 Da.

1   GLYSERSERILESERHISSERGLYASNLEU
2   TYRTHRALAGLYGLNCYSTHRTRPTYRVAL
3   TYRASPLYSVALGLYGLYGLUILEGLYSER
4   THRTRPGLYASNALAASNASNTRPALAALA
5   ALAALAGLNGLYALAGLYPHETHRVALASN
6   HISTHRPROSERLYSGLYALAILELEUGLN
7   SERSERGLUGLYPROPHEGLYHISVALALA
8   TYRVALGLUSERVALASNSERASPGLYSER
9   VALTHRILESERGLUMETASNTYRSERGLY
10   GLYPROPHESERVALSERSERARGTHRILE
11   SERALASERGLUALAGLYASNTYRASNTYR
12   ILEHISILE

Samples:

sample_1: sodium chloride 137 mM; beta-mercaptoethanol 5 mM; potassium phosphate 2 mM; sodium phosphate 10 mM; H2O 90%; D2O 10%; staphyloxanthin_protein 0.7 mM

sample_2: sodium chloride 137 mM; beta-mercaptoethanol 5 mM; sodium phosphate 10 mM; potassium phosphate 2 mM; D2O 100%; staphyloxanthin_protein 0.7 mM

sample_conditions_1: ionic strength: 0.137 M; pH: 6.8; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 0.137 M; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_2
3D HCCH-COSYsample_2isotropicsample_conditions_2
3D HCCH-TOCSYsample_2isotropicsample_conditions_2
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_2

Software:

ARIA_CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read, Goddard, Linge, O'Donoghue and Nilges, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment, data analysis, refinement

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAB43396 BAB96087 BAD16609 BAF68475 BAF79171
EMBL CAG41369 CAG44005 CAI81865 CAQ50734 CBI50299
GB AAW38515 ABD20377 ABD31588 ABQ50107 ABR53195
PIR C90029
REF WP_000733941 WP_000737696 WP_000737697 WP_000737698 WP_000737699

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