BMRB Entry 16187

Name: Backbone 1H Chemical Shift Assignments for FP1
Published: 2009-04-17

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PDB ID: 2kfq
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16187
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Backbone 1H Chemical Shift Assignments for FP1

Deposition date:

2009-02-26

Original release date:

2009-04-17

Authors:

Araki, Mitsugu; Tamura, Atsuo

Citation:

Citation: Araki, Mitsugu; Tamura, Atsuo. "Solubility-dependent structural formation of a 25-residue natively unfolded protein, induced by addition of a seven-residue peptide fragment" FEBS J. 276, 2336-2347 (2009).
PubMed: 19292861

Assembly members:

Assembly members:
FP1, polymer, 32 residues, 3519.278 Da.

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: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
FP1: YAFACPACPKRFMRSDALSK HIKTAFIVVALG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
1H chemical shifts	225

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	FP1	1

Entities:

Entity 1, FP1 32 residues - 3519.278 Da.

1

TYR

ALA

PHE

ALA

CYS

PRO

ALA

CYS

PRO

LYS

2

ARG

PHE

MET

ARG

SER

ASP

ALA

LEU

SER

LYS

3

HIS

ILE

LYS

THR

ALA

PHE

ILE

VAL

ALA

4

LEU

GLY

Samples:

sample_1: FP1 3 mM; acetic acid, [U-100% 2H], 25 mM; sodium chloride 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 3.0; pressure: 1 atm; temperature: 293.15 K

Experiments:

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

Software:

DYANA v1.5, Guntert, Braun and Wuthrich - structure solution

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

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Bruker DMX 750 MHz