BMRB Entry 15931

Name: Deletions in a surface loop divert the folding of a protein domain into a metastable dimeric form
Published: 2009-09-03

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PDB ID: 2k7v
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15931
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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:

Deletions in a surface loop divert the folding of a protein domain into a metastable dimeric form

Deposition date:

2008-08-27

Original release date:

2009-09-03

Authors:

Stott, Katherine

Citation:

Citation: Stott, Katherine; Yusof, Adlina; Perham, Richard; Jones, Dafydd. "A surface loop directs conformational switching of a lipoyl domain between a folded and a novel misfolded structure" Structure 17, 1117-1127 (2009).
PubMed: 19679089

Assembly members:

Assembly members:
E2plipD4, polymer, 85 residues, Formula weight is not available

Natural source:

Natural source: Common Name: E.coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET11c

Entity Sequences (FASTA):

Entity Sequences (FASTA):
E2plipD4: MVKEVNVPDIVEVTEVMVKV GDKVAAEQSLITVEGDKASM EVPAPFAGVVKELKVNVGDK VKTGSLIMIFEVEGAAPAAA PAKQE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
15N chemical shifts	72
1H chemical shifts	495

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	E2plipD4, chain 1	1
2	E2plipD4, chain 2	1

Entities:

Entity 1, E2plipD4, chain 1 85 residues - Formula weight is not available

1

MET

VAL

LYS

GLU

VAL

ASN

VAL

PRO

ASP

ILE

2

VAL

GLU

VAL

THR

GLU

VAL

MET

VAL

LYS

VAL

3

GLY

ASP

LYS

VAL

ALA

GLU

GLN

SER

LEU

4

ILE

THR

VAL

GLU

GLY

ASP

LYS

ALA

SER

MET

5

GLU

VAL

PRO

ALA

PRO

PHE

ALA

GLY

VAL

6

LYS

GLU

LEU

LYS

VAL

ASN

VAL

GLY

ASP

LYS

7

VAL

LYS

THR

GLY

SER

LEU

ILE

MET

ILE

PHE

8

GLU

VAL

GLU

GLY

ALA

PRO

ALA

9

PRO

ALA

LYS

GLN

GLU

Samples:

sample_1: E2plipD4, [U-15N], 1 mM; sodium phosphate 20 mM; TSP 40 uM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 20 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D DQF-COSY	sample_1	isotropic	sample_conditions_1

Software:

ARIA, Linge, O'Donoghue and Nilges - structure solution

NMR spectrometers:

Bruker DRX 500 MHz

PDB	2K7V
EMBL	CSG13687 CSG39424
GB	EFI22553 EGB41640 EGI23519 EGI24249 EGI43488
REF	WP_000374927 WP_032230881 WP_050541395