BMRB Entry 25886

Click here to enlarge.

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/BMR25886
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 acyl carrier protein LipD from Actinoplanes friuliensis
Deposition date:
2015-11-10
Original release date:
2016-11-14
Authors:
Paul, Subrata; Ishida, Hiroaki; Liu, Zhihong; Nguyen, Leonard; Vogel, Hans
Citation:

Citation: Paul, Subrata; Ishida, Hiroaki; Nguyen, Leonard; Liu, Zhihong; Vogel, Hans. "Structural and dynamic characterization of a freestanding acyl carrier protein involved in the biosynthesis of cyclic lipopeptide antibiotics"  Protein Sci. 26, 946-959 (2017).
PubMed: 28187530

Assembly members:

Assembly members:
entity, polymer, 90 residues, 9504.713 Da.

Natural source:

Natural source:   Common Name: high GC gram+   Taxonomy ID: 196914   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Actinoplanes friuliensis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET15MHL

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GHMSDLSTAPTLDSLRVWLV DCVAGHLGLDAATIATDLPL TSYGLDSVYALSIAAELEDH LDVSLDPTLIWDHPTIDALS TALVAELRSA

Data sets:
Data typeCount
13C chemical shifts375
15N chemical shifts85
1H chemical shifts599

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 90 residues - 9504.713 Da.

1   GLYHISMETSERASPLEUSERTHRALAPRO
2   THRLEUASPSERLEUARGVALTRPLEUVAL
3   ASPCYSVALALAGLYHISLEUGLYLEUASP
4   ALAALATHRILEALATHRASPLEUPROLEU
5   THRSERTYRGLYLEUASPSERVALTYRALA
6   LEUSERILEALAALAGLULEUGLUASPHIS
7   LEUASPVALSERLEUASPPROTHRLEUILE
8   TRPASPHISPROTHRILEASPALALEUSER
9   THRALALEUVALALAGLULEUARGSERALA

Samples:

sample_1: entity, [U-15N], 0.5 mM; D2O, [U-2H], 10%; H2O 90%; sodium azide 0.03%; potassium chloride 100 mM; DTT 10 mM; DSS 0.5 mM; potassium phosphate 50 mM

sample_2: entity, [U-13C; U-15N], 0.5 mM; potassium chloride 100 mM; DTT 10 mM; sodium azide 0.03%; D2O, [U-2H], 10%; H2O 90%; DSS 0.5 mM; potassium phosphate 50 mM

sample_3: entity, [U-13C; U-15N], 0.5 mM; potassium phosphate 50 mM; potassium chloride 100 mM; DTT 10 mM; sodium azide 0.03%; DSS 0.5 mM; D2O, [U-2H], 100%

sample_4: entity 1 mM; potassium phosphate 50 mM; potassium chloride 100 mM; sodium azide 0.03%; DTT 10 mM; DSS 0.5 mM; D2O, [U-2H], 100%

sample_5: entity, [U-15N], 0.5 mM; D2O, [U-2H], 10%; H2O 90%; potassium chloride 130 mM; potassium phosphate 50 mM; DTT 10 mM; DSS 0.5 mM; PMSF 0.03%; Pf1 phage 15 mg/mL

sample_conditions_1: ionic strength: 100 mM; pH: 6.0; pressure: 1 atm; temperature: 297 K

sample_conditions_2: ionic strength: 100 mM; pH: 6.0; pressure: 1 atm; temperature: 297 K

sample_conditions_3: ionic strength: 100 mM; pH: 6.4; pressure: 1 atm; temperature: 297 K

sample_conditions_4: ionic strength: 100 mM; pH: 6.4; pressure: 1 atm; temperature: 297 K

sample_conditions_5: ionic strength: 130 mM; pH*: 6.0; pressure: 1 atm; temperature: 297 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_2
3D HNCACBsample_2isotropicsample_conditions_2
3D CBCA(CO)NHsample_2isotropicsample_conditions_2
3D HN(CA)COsample_2isotropicsample_conditions_2
3D HBHA(CO)NHsample_2isotropicsample_conditions_2
3D H(CCO)NHsample_2isotropicsample_conditions_2
3D C(CO)NHsample_2isotropicsample_conditions_2
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_3
2D 1H-1H TOCSYsample_4isotropicsample_conditions_4
2D DQF-COSYsample_4isotropicsample_conditions_4
2D 1H-1H NOESYsample_4isotropicsample_conditions_4
IPAP-1H-15N-HSQCsample_5anisotropicsample_conditions_5
2D 1H-13C HSQC aromaticsample_3isotropicsample_conditions_3
IPAP-1H-15N-HSQCsample_1isotropicsample_conditions_1

Software:

CYANA v2.0, Guntert, Mumenthaler and Wuthrich - chemical shift assignment, structure solution

X-PLOR_NIH v2.19, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz

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