BMRB Entry 16012

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16012
MolProbity Validation Chart

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NMR-STAR v3 text file.
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Title:
Solution NMR structure of BNIP3 transmembrane peptide dimer in detergent micelles
Deposition date:
2008-10-30
Original release date:
2009-05-20
Authors:
Sulistijo, Endah; MacKenzie, Kevin
Citation:

Citation: Sulistijo, Endah; MacKenzie, Kevin. "The structural basis for dimerization of the BNIP3 transmembrane domain"  Biochemistry 48, 5106-5120 (2009).
PubMed: 19415897

Assembly members:

Assembly members:
Bcl2/Adenovirus_E1B_19_kDa_protein-interacting_protein_3, polymer, 35 residues, 3790.626 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET3A

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Bcl2/Adenovirus_E1B_19_kDa_protein-interacting_protein_3: GGIFSAEFLKVFLPSLLLSH LLAIGLGIYIGRRLT

Data sets:
Data typeCount
13C chemical shifts178
15N chemical shifts39
1H chemical shifts284

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Bcl2/Adenovirus E1B 19 kDa protein-interacting protein 3_11
2Bcl2/Adenovirus E1B 19 kDa protein-interacting protein 3_21

Entities:

Entity 1, Bcl2/Adenovirus E1B 19 kDa protein-interacting protein 3_1 35 residues - 3790.626 Da.

1   GLYGLYILEPHESERALAGLUPHELEULYS
2   VALPHELEUPROSERLEULEULEUSERHIS
3   LEULEUALAILEGLYLEUGLYILETYRILE
4   GLYARGARGLEUTHR

Samples:

sample_1: Bcl2/Adenovirus E1B 19 kDa protein-interacting protein 3, [U-100% 13C; U-100% 15N], 0.4 mM; Bcl2/Adenovirus E1B 19 kDa protein-interacting protein 3 0.6 mM; phosphate buffer 10 mM

sample_conditions_1: pH: 5.1; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
3D CN-NOESY-HSQCsample_1isotropicsample_conditions_1
3D 15N-edited NOESY-HSQCsample_1isotropicsample_conditions_1
3D 13C-edited NOESY-HSQC optimized for aromatic carbonsample_1isotropicsample_conditions_1
half-filtered 3D CN-NOESY-HSQCsample_1isotropicsample_conditions_1
2D spin-echo difference CT HSQCsample_1isotropicsample_conditions_1
HNHAsample_1isotropicsample_conditions_1
HNCAsample_1isotropicsample_conditions_1
CBCACONNHsample_1isotropicsample_conditions_1
HNCOsample_1isotropicsample_conditions_1
H(C)CH-COSYsample_1isotropicsample_conditions_1
(H)CCH-TOCSYsample_1isotropicsample_conditions_1
HBCBCGCDHDsample_1isotropicsample_conditions_1
HBCBCGCDCEHEsample_1isotropicsample_conditions_1

Software:

ARIA v1.2, Linge, O'Donoghue and Nilges - refinement, structure solution

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

SPARKY, Goddard - chemical shift assignment, peak picking

VNMR, Varian - collection

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAB29214 BAC36072 BAD96346 BAE31356 BAG58159
EMBL CAX36485
GB AAC00022 AAC16738 AAD02922 AAF98317 AAH21989
REF NP_001015859 NP_001069834 NP_001083178 NP_004043 NP_033890
SP O55003 Q12983 Q32KN2
AlphaFold O55003 Q12983 Q32KN2

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