BMRB Entry 25837

Name: Chemical shift assignment, NMR constraints and PDB for chromodomain 3 (CD3) of cpSRP43
Published: 2015-12-07

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PDB ID: 2n88
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25837
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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:

Chemical shift assignment, NMR constraints and PDB for chromodomain 3 (CD3) of cpSRP43

Deposition date:

2015-10-06

Original release date:

2015-12-07

Authors:

Hennig, Janosch; Sattler, Michael

Citation:

Citation: Horn, Annemarie; Hennig, Janosch; Ahmed, Yasar; Stier, Gunter; Wild, Klemes; Sattler, Michael; Sinning, Irmgard. "Structural basis for cpSRP43 chromodomain selectivity and dynamics in Alb3 insertase interaction" Nat. Commun. 6, 8875-8875 (2015).
PubMed: 26568381

Assembly members:

Assembly members:
CD3, polymer, 58 residues, 6580.293 Da.

Natural source:

Natural source: Common Name: Thale cress Taxonomy ID: 3702 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Arabidopsis thaliana

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pETtrx_1a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CD3: GLEYAVAESVIGKRVGDDGK TIEYLVKWTDMSDATWEPQD NVDSTLVLLYQQQQPMNE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	242
15N chemical shifts	67
1H chemical shifts	408

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CD3	1

Entities:

Entity 1, CD3 58 residues - 6580.293 Da.

1

GLY

LEU

GLU

TYR

ALA

VAL

ALA

GLU

SER

VAL

2

ILE

GLY

LYS

ARG

VAL

GLY

ASP

GLY

LYS

3

THR

ILE

GLU

TYR

LEU

VAL

LYS

TRP

THR

ASP

4

MET

SER

ASP

ALA

THR

TRP

GLU

PRO

GLN

ASP

5

ASN

VAL

ASP

SER

THR

LEU

VAL

LEU

TYR

6

GLN

PRO

MET

ASN

GLU

Samples:

sample_1: CD3, [U-100% 13C; U-100% 15N], 0.26 mM

sample_2: CD3, [U-100% 13C; U-100% 15N], 0.8 mM

sample_conditions_1: ionic strength: 0.15 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
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_2	isotropic	sample_conditions_1

Software:

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

ARIA v1.2, Linge, O'Donoghue and Nilges - refinement

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

CARA, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

TOPSPIN, Bruker Biospin - collection

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

NMR spectrometers:

Bruker Avance III 800 MHz
Bruker Avance III 600 MHz

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