BMRB Entry 11544

Name: DESIGNED ARMADILLO REPEAT PROTEIN SELF-ASSEMBLED COMPLEX (YIIM2-MAII)
Published: 2014-07-21

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PDB ID: 2ru4
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11544
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

DESIGNED ARMADILLO REPEAT PROTEIN SELF-ASSEMBLED COMPLEX (YIIM2-MAII)

Deposition date:

2013-11-22

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:
YM2, polymer, 115 residues, 12193.641 Da.
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):
YM2: GELPQMTQQLNSDDMQEQLS ATRKFSQILSDGNEQIQAVI DAGALPALVQLLSSPNEQIL QEALWALSNIASGGNEQIQA VIDAGALPALVQLLSSPNEQ ILQEALWALSNIASG
MA: GNEQIQAVIDAGALPALVQL LSSPNEQILQEALWALSNIA SGGNEQKQAVKEAGALEKLE QLQSHENEKIQKEAQEALEK LQSH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
- assigned_chem_shift_list_2

Data type	Count
13C chemical shifts	632
15N chemical shifts	186
1H chemical shifts	1081

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	YM2	1
2	MA	2

Entities:

Entity 1, YM2 115 residues - 12193.641 Da.

1

GLY

GLU

LEU

PRO

GLN

MET

THR

GLN

LEU

2

ASN

SER

ASP

MET

GLN

GLU

GLN

LEU

SER

3

ALA

THR

ARG

LYS

PHE

SER

GLN

ILE

LEU

SER

4

ASP

GLY

ASN

GLU

GLN

ILE

GLN

ALA

VAL

ILE

5

ASP

ALA

GLY

ALA

LEU

PRO

ALA

LEU

VAL

GLN

6

LEU

SER

PRO

ASN

GLU

GLN

ILE

LEU

7

GLN

GLU

ALA

LEU

TRP

ALA

LEU

SER

ASN

ILE

8

ALA

SER

GLY

ASN

GLU

GLN

ILE

GLN

ALA

9

VAL

ILE

ASP

ALA

GLY

ALA

LEU

PRO

ALA

LEU

10

VAL

GLN

LEU

SER

PRO

ASN

GLU

GLN

11

ILE

LEU

GLN

GLU

ALA

LEU

TRP

ALA

LEU

SER

12

ASN

ILE

ALA

SER

GLY

Entity 2, 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: YM2, [U-13C; U-15N], 1.0 mM; MA 1.5 mM; sodium phosphate 50 mM; sodium chloride 150 mM; glycerol 2%; TMSP 1 mM; sodium azide 0.02%; H2O 88%; D2O 10%

sample_2: YM2 0.90 mM; 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 HNCA	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 C(CO)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
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
4D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_2	isotropic	sample_conditions_1
3D-13C edited/filtered NOESY	sample_1	isotropic	sample_conditions_1
3D-13C-edited/filtered NOESY	sample_2	isotropic	sample_conditions_1
3D-15N-edited/filtered NOESY	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	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
Varian DirectDrive 700 MHz