BMRB Entry 19479

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19479
MolProbity Validation Chart

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

Title:
Solution Structure of an Active Site Mutant Pepitdyl Carrier Protein
Deposition date:
2013-09-06
Original release date:
2014-04-22
Authors:
Tufar, Peter; Rahighi, Simin; Kraas, Femke; Kirchner, Donata; Loehr, Frank; Henrich, Erik; Koepke, Juergen; Dikic, Ivan; Guentert, Peter; Marahiel, Mohamed; Doetsch, Volker
Citation:

Citation: Tufar, Peter; Rahighi, Simin; Kraas, Femke; Kirchner, Donata; Lohr, Frank; Henrich, Erik; Kopke, Jurgen; Dikic, Ivan; Guntert, Peter; Marahiel, Mohamed; Dotsch, Volker. "Crystal Structure of a PCP/Sfp Complex Reveals the Structural Basis for Carrier Protein Posttranslational Modification."  Chem. Biol. 21, 552-562 (2014).
PubMed: 24704508

Assembly members:

Assembly members:
PCP, polymer, 90 residues, 9972.533 Da.

Natural source:

Natural source:   Common Name: Bacillus brevis   Taxonomy ID: 1393   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacillus brevis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pQE70

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PCP: PVTEAQYVAPTNAVESKLAE IWERVLGVSGIGILDNFFQI GGHALKAMAVAAQVHREYQV ELPLKVLFAQPTIKALAQYV ATRSHHHHHH

Data sets:
Data typeCount
13C chemical shifts292
15N chemical shifts79
1H chemical shifts610

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Active Site Mutant Pepitdyl Carrier Protein1

Entities:

Entity 1, Active Site Mutant Pepitdyl Carrier Protein 90 residues - 9972.533 Da.

M1 is cleaved in vivo during expression. R84-H91 are a non-native.

1   PROVALTHRGLUALAGLNTYRVALALAPRO
2   THRASNALAVALGLUSERLYSLEUALAGLU
3   ILETRPGLUARGVALLEUGLYVALSERGLY
4   ILEGLYILELEUASPASNPHEPHEGLNILE
5   GLYGLYHISALALEULYSALAMETALAVAL
6   ALAALAGLNVALHISARGGLUTYRGLNVAL
7   GLULEUPROLEULYSVALLEUPHEALAGLN
8   PROTHRILELYSALALEUALAGLNTYRVAL
9   ALATHRARGSERHISHISHISHISHISHIS

Samples:

sample_1: PCP, [U-100% 13C; U-100% 15N], 0.7 mM; sodium phosphate 50 mM; DSS 0.15 mM; H2O 95%; D2O 5%

sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 298 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 HNCACBsample_1isotropicsample_conditions_1
3D H(CCCO)NH-TOCSYsample_1isotropicsample_conditions_1
3D (H)C(CCO)NH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

SPARKY v3.114, Goddard - chemical shift assignment, peak picking

TOPSPIN v3.0, Bruker Biospin - collection, processing

CYANA v3.96, Guntert, Mumenthaler and Wuthrich - structure solution

OPALp v1.4, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 900 MHz

Related Database Links:

UNP O30409
PDB
AlphaFold O30409

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