BMRB Entry 2991

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR2991

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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:

Different conformations for the same polypeptide bound to chaperones DnaK and GroEL

Deposition date:

1995-07-31

Original release date:

1999-06-14

Authors:

Landry, Samuel; Jordan, Robert; McMacken, Roger; Gierasch, Lila

Citation:

Citation: Landry, Samuel; Jordan, Robert; McMacken, Roger; Gierasch, Lila. "Different conformations for the same polypeptide bound to chaperones DnaK and GroEL" Nature 355, 455-457 (1992).

Assembly members:

Assembly members:
ATPase-stimulating-peptide, polymer, 13 residues, Formula weight is not available

Natural source:

Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available

Experimental source:

Experimental source: Production method: not available

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ATPase-stimulating-peptide: XXIGVLSSLFRXK

Data sets:

assigned_chemical_shifts
- chemical_shift_assignment_data_set_one

Data type	Count
1H chemical shifts	10

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ATPase-stimulating-peptide	1

Entities:

Entity 1, ATPase-stimulating-peptide 13 residues - Formula weight is not available

1

X

ILE

GLY

VAL

LEU

SER

LEU

PHE

2

ARG

X

LYS

Samples:

sample_one:

sample_condition_set_one: pH: 6.1 na; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions

Software:

No software information available

NMR spectrometers:

unknown unknown 0 MHz