BMRB Entry 16041

Name: FLNCCPGCCMEP_ReAsH_motif
Published: 2009-03-23

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR16041

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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:

FLNCCPGCCMEP_ReAsH_motif

Deposition date:

2008-11-24

Original release date:

2009-03-23

Authors:

Madani, Fatemeh; Lind, Jesper; Damberg, Peter; Adams, Stephen; Tsien, Roger; Graslund, Astrid

Citation:

Citation: Madani, Fatemeh; Lind, Jesper; Damberg, Peter; Adams, Stephen; Tsien, Roger; Graslund, Astrid. "Hairpin Structure of a Biarsenical-Tetracysteine Motif Determined by NMR" J. Am. Chem. Soc. 131, 4613-4615 (2009).
PubMed: 19281235

Assembly members:

Assembly members:
FLNCCPGCCMEP, polymer, 12 residues, Formula weight is not available
ReAsH, non-polymer, 360 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):
FLNCCPGCCMEP: FLNCCPGCCMEP

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
conformer_family_coord_set
- ensemble_of_conformers

Data type	Count
1H chemical shifts	66
conformer coordinate sets	1

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	FLNCCPGCCMEP	1
2	ReAsH, resorufin arsenical hairpin binder	2

Entities:

Entity 1, FLNCCPGCCMEP 12 residues - Formula weight is not available

1

PHE

LEU

ASN

CYS

PRO

GLY

CYS

MET

2

GLU

PRO

Entity 2, ReAsH, resorufin arsenical hairpin binder - C12 H4 N O3 As2 - 360 Da.

Samples:

sample_1: FLNCCPGCCMEP 0.6 mM

sample_conditions_1: ionic strength: 25 mM; pH: 7.4; pressure: 1 atm; temperature: 278 K

Experiments:

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

Software:

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

CYANA v2.0, Guntert, Mumenthaler and Wuthrich - refinement

NMR spectrometers:

Bruker Avance 500 MHz
Varian INOVA 600 MHz