BMRB Entry 34094

Name: NMR structure calculation of a composite Cys2His2 type zinc finger protein containing a non-peptide (or oligourea) helical domain
Published: 2017-04-06

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PDB ID: 5n14
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34094
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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:

NMR structure calculation of a composite Cys2His2 type zinc finger protein containing a non-peptide (or oligourea) helical domain

Deposition date:

2017-02-05

Original release date:

2017-04-06

Authors:

Venkateshaiah M, V.; Salgado, G.

Citation:

Citation: Venkateshaiah Machohally, V.; Salgado, G.; Lombardo, C.; Mergny, J.; Guichard, G.. "NMR structure calculation of a composite Cys2His2 type zinc finger protein containing a non-peptide (or oligourea) helical domain." .

Assembly members:

Assembly members:
entity_1, polymer, 25 residues, 3254.846 Da.
entity_ZN, non-polymer, 65.409 Da.
entity_HOH, water, 18.015 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: PFACDICGRKFARSXXXXXX XXRKD

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	60
15N chemical shifts	30
1H chemical shifts	191

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1
2	entity_2	2
3	entity_3	3

Entities:

Entity 1, entity_1 25 residues - 3254.846 Da.

1

PRO

PHE

ALA

CYS

ASP

ILE

CYS

GLY

ARG

LYS

2

PHE

ALA

ARG

SER

OUD

OUE

OUK

OUR

OUH

OUK

3

OUI

OUH

ARG

LYS

ASP

Entity 2, entity_2 - Zn - 65.409 Da.

1

ZN

Entity 3, entity_3 - 18.015 Da.

1

HOH

Samples:

sample_1: CL112 3.2 ± 0.2 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; 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-13C HSQC	sample_1	isotropic	sample_conditions_1
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_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H COSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	anisotropic	sample_conditions_1

Software:

AMBER v12, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - structure calculation

SPARKY v12, Goddard - chemical shift assignment

TOPSPIN, Bruker Biospin - processing

UCSF Chimera, Pettersen EF, Goddard TD, Huang CC, Couch GS, Greenblatt DM, Meng EC, Ferrin - refinement

NMR spectrometers:

Bruker AvanceIII 950 MHz
Bruker AvanceIII 800 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks