BMRB Entry 16090

Name: NMR Structure of a Monomeric Folding Intermediate Reveals the Structural Basis for Rapid Assembly of an Evolutionary Optimized Trimerization Module
Published: 2009-04-22

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PDB ID: 2kbl
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16090
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NMR Structure of a Monomeric Folding Intermediate Reveals the Structural Basis for Rapid Assembly of an Evolutionary Optimized Trimerization Module

Deposition date:

2008-12-24

Original release date:

2009-04-22

Authors:

Habazettl, Judith; Reiner, Andreas; Kiefhaber, Thomas

Citation:

Citation: Habazettl, Judith; Reiner, Andreas; Kiefhaber, Thomas. "NMR Structure of a Monomeric Intermediate on the Evolutionarily Optimized Assembly Pathway of a Small Trimerization Domain" J. Mol. Biol. 389, 103-114 (2009).
PubMed: 19361528

Assembly members:

Assembly members:
foldon_E5R, polymer, 29 residues, 3112.573 Da.

Natural source:

Natural source: Common Name: Enterobacteria phage T4 sensu lato Taxonomy ID: 348604 Superkingdom: Viruses Kingdom: not available Genus/species: T4-like viruses Enterobacteria phage T4 sensu lato

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET32A

Entity Sequences (FASTA):

Entity Sequences (FASTA):
foldon_E5R: GSGYIPRAPRDGQAYVRKDG EWVLLSTFL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
15N chemical shifts	26
1H chemical shifts	192

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	foldon_E5R	1

Entities:

Entity 1, foldon_E5R 29 residues - 3112.573 Da.

residues 1-27 represent the residues 458-484 in native fibritin

1

GLY

SER

GLY

TYR

ILE

PRO

ARG

ALA

PRO

ARG

2

ASP

GLY

GLN

ALA

TYR

VAL

ARG

LYS

ASP

GLY

3

GLU

TRP

VAL

LEU

SER

THR

PHE

LEU

Samples:

sample_1: foldon E5R 200 uM; K_3 PO_4 10 mM

sample_2: foldon E5R, [U-99% 15N], 210 uM; K_3 PO_4 10 mM

sample_conditions_1: ionic strength: 10 mM; pH: 7.0; pressure: 1 atm; temperature: 296.7 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-15N HSQC	sample_2	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_2	isotropic	sample_conditions_1

Software:

xwinnmr, Bruker - data analysis

SPARKY, Goddard - data analysis

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

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

NMR spectrometers:

Bruker DRX 600 MHz
Bruker DRX 800 MHz