BMRB Entry 11548

Name: DESIGNED ARMADILLO REPEAT PROTEIN FRAGMENT (MAII)
Published: 2014-07-21

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PDB ID: 2ru5
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR11548
MolProbity Validation Chart

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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:

DESIGNED ARMADILLO REPEAT PROTEIN FRAGMENT (MAII)

Deposition date:

2013-12-09

Original release date:

2014-07-21

Authors:

Zerbe, Oliver; Christen, Martin; Plueckthun, Andreas; Watson, Randall

Citation:

Citation: Watson, Randall; Christen, Martin; Ewald, Christina; Bumback, Fabian; Reichen, Christian; Mihajlovic, Maja; Schmidt, E.; Guntert, Peter; Caflisch, Amedeo; Plueckthun, Andreas; Zerbe, Oliver. "Spontaneous Self-Assembly of Fragments of Engineered Armadillo Repeat Proteins into Folded Proteins" Structure 22, 985-995 (2014).
PubMed: 24931467

Assembly members:

Assembly members:
MA, polymer, 84 residues, 9104.170 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: recombinant technology Host organism: Escherichia coli Vector: pLIC_CR

Entity Sequences (FASTA):

Entity Sequences (FASTA):
MA: GNEQIQAVIDAGALPALVQL LSSPNEQILQEALWALSNIA SGGNEQKQAVKEAGALEKLE QLQSHENEKIQKEAQEALEK LQSH

Data sets:

assigned_chemical_shifts
- MA_shifts

Data type	Count
13C chemical shifts	281
15N chemical shifts	64
1H chemical shifts	456

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	MA	1

Entities:

Entity 1, MA 84 residues - 9104.170 Da.

1

GLY

ASN

GLU

GLN

ILE

GLN

ALA

VAL

ILE

ASP

2

ALA

GLY

ALA

LEU

PRO

ALA

LEU

VAL

GLN

LEU

3

LEU

SER

PRO

ASN

GLU

GLN

ILE

LEU

GLN

4

GLU

ALA

LEU

TRP

ALA

LEU

SER

ASN

ILE

ALA

5

SER

GLY

ASN

GLU

GLN

LYS

GLN

ALA

VAL

6

LYS

GLU

ALA

GLY

ALA

LEU

GLU

LYS

LEU

GLU

7

GLN

LEU

GLN

SER

HIS

GLU

ASN

GLU

LYS

ILE

8

GLN

LYS

GLU

ALA

GLN

GLU

ALA

LEU

GLU

LYS

9

LEU

GLN

SER

HIS

Samples:

sample_1: MA, [U-13C; U-15N], 0.75 mM; sodium phosphate 50 mM; sodium chloride 150 mM; glycerol 2%; TMSP 1 mM; sodium azide 0.02%; H2O 88%; D2O 10%

sample_conditions_1: ionic strength: 285 mM; pH: 7.4; pressure: 1 atm; temperature: 310 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment

CcpNMR v2.3.1, CCPN - chemical shift assignment, data analysis, peak picking

UNIO v2.0.2, (UNIO) Herrmann - data analysis, peak picking, structure solution

CYANA v3.96a, Guntert, Mumenthaler and Wuthrich - geometry optimization, structure solution

X-PLOR_NIH v2.32, Schwieters, Kuszewski, Tjandra and Clore - refinement

TALOS-N v4.01, Shen and Bax - data analysis

NMR spectrometers:

Bruker Avance 700 MHz
Bruker Avance 600 MHz