BMRB Entry 17553

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17553
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 CoA binding protein from Babesia bovis T2Bo. Seattle Structure Genomics Center for Infectious Disease (SSGCID)
Deposition date:
2011-03-29
Original release date:
2011-04-11
Authors:
Yang, Fan; Barnwal, Ravi; Varani, Gabriele
Citation:

Citation: Yang, Fan; Barnwal, Ravi; Varani, Gabriele. "Solution structure of acyl CoA binding protein from Babesia bovis T2Bo"  .

Assembly members:

Assembly members:
entity, polymer, 88 residues, 10086.520 Da.

Natural source:

Natural source:   Common Name: Babesia bovis T2Bo   Taxonomy ID: 484906   Superkingdom: Eukaryota   Kingdom: Chromalveolata   Genus/species: Babesia bovis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: LIC VECTOR BG1861

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: MSADDFDAAVKYVSNTTTMM ASNDDKLCFYKYYKQATVGD CNKPKPGMLQLQEKYKWEAW NALRGMSTESAKEAYVKLLD TLAPSWRN

Data sets:
Data typeCount
13C chemical shifts367
15N chemical shifts97
1H chemical shifts547

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1acyl CoA binding protein1

Entities:

Entity 1, acyl CoA binding protein 88 residues - 10086.520 Da.

1   METSERALAASPASPPHEASPALAALAVAL
2   LYSTYRVALSERASNTHRTHRTHRMETMET
3   ALASERASNASPASPLYSLEUCYSPHETYR
4   LYSTYRTYRLYSGLNALATHRVALGLYASP
5   CYSASNLYSPROLYSPROGLYMETLEUGLN
6   LEUGLNGLULYSTYRLYSTRPGLUALATRP
7   ASNALALEUARGGLYMETSERTHRGLUSER
8   ALALYSGLUALATYRVALLYSLEULEUASP
9   THRLEUALAPROSERTRPARGASN

Samples:

sample_1: entity, [U-95% 15N], 0.8 mM; BIS-TRIS 20 mM; sodium chloride 100 mM; DTT 5 mM; EDTA 2 mM

sample_2: entity, [U-95% 13C; U-95% 15N], 0.8 mM; BIS-TRIS 20 mM; sodium chloride 100 mM; DTT 5 mM; EDTA 2 mM

sample_3: entity 1 mM; BIS-TRIS 20 mM; sodium chloride 100 mM; DTT 5 mM; EDTA 2 mM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D HCACOsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

Molmol, Koradi, Billeter and Wuthrich - structure display

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TOPSPIN, Bruker Biospin - collection

TALOS, Cornilescu, Delaglio and Bax - data analysis

CcpNMR, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker AMX 500 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAN64849
GB EDO05649
REF XP_001609217

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