BMRB Entry 15612

Name: Extended Polypeptide Linkers Establish the Spatial Architecture of a Pyruvate Dehydrogenase
Published: 2008-06-26

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15612

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Extended Polypeptide Linkers Establish the Spatial Architecture of a Pyruvate Dehydrogenase

Deposition date:

2008-01-02

Original release date:

2008-06-26

Authors:

Milne, Jacqueline; Stott, Katherine

Citation:

Citation: Lengyel, Jeffrey; Stott, Katherine; Wu, Xiongwu; Brooks, Bernard; Balbo, Andrea; Schuck, Peter; Perham, Richard; Subramaniam, Sriram; Milne, Jacqueline. "Extended polypeptide linkers establish the spatial architecture of a pyruvate dehydrogenase multienzyme complex" Structure 16, 93-103 (2008).
PubMed: 18184587

Assembly members:

Assembly members:
Inner-linker_peptide, polymer, 37 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Bacillus stearothermophilus Taxonomy ID: 1422 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus stearothermophilus

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Inner-linker_peptide: AGGAKPAPAAAEEKAAPAAA KPATTEGEFPETREKMS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	72
1H chemical shifts	160

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Inner-linker peptide	1

Entities:

Entity 1, Inner-linker peptide 37 residues - Formula weight is not available

1

ALA

GLY

ALA

LYS

PRO

ALA

PRO

ALA

2

ALA

GLU

LYS

ALA

PRO

ALA

3

LYS

PRO

ALA

THR

GLU

GLY

GLU

PHE

PRO

4

GLU

THR

ARG

GLU

LYS

MET

SER

Samples:

sample_1: Inner-linker peptide 1 mM; potassium phosphate 10 mM; DSS 0.01 mM; D2O, [U-100% 2H], 10%; H2O 90%

sample_conditions_1: ionic strength: 0.01 M; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1

Software:

CcpNMR, Wayne Boucher and Tim Stevens - chemical shift assignment

NMR spectrometers:

Bruker DRX 500 MHz

PDB	1B5S 3DUF 3DV0 3DVA
EMBL	CAA37630
GB	KFL17224 KFX35197 KMY60230 KMY60559 KMY62515
REF	WP_033008489 WP_033016211
SP	P11961
AlphaFold	P11961