BMRB Entry 7101

Name: Mistranslation of a computationally designed protein yields an exceptionally stable homodimer: Implications for protein evolution and engineering.
Published: 2006-11-17

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PDB ID: 2gjh
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR7101
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:

Mistranslation of a computationally designed protein yields an exceptionally stable homodimer: Implications for protein evolution and engineering.

Deposition date:

2006-05-05

Original release date:

2006-11-17

Authors:

Dantas, G.

Citation:

Citation: Dantas, G.; Watters, A.; Lunde, B.; Eletr, Z.; Isern, N.; Roseman, T.; Lipfert, J.; Doniach, S.; Tompa, M.; Kuhlman, B.; Stoddard, B.; Varani, G.; Baker, D.. "Mis-translation of a computationally designed protein yields an exceptionally stable homodimer: Implications for protein evolution and engineering." J. Mol. Biol. 362, 1004-1024 (2006).
PubMed: 16949611

Assembly members:

Assembly members:
Designed protein TOP7, polymer, 62 residues, Formula weight is not available

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Designed protein TOP7: MERVRISITARTKKEAEKFA AILIKVFAELGYNDINVTWD GDTVTVEGQLEGGSLEHHHH HH

Data sets:

assigned_chemical_shifts
- chemical_shift_set_1

Data type	Count
13C chemical shifts	223
15N chemical shifts	59
1H chemical shifts	390

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	DESIGNED PROTEIN TOP7, chain 1	1
2	DESIGNED PROTEIN TOP7, chain 2	1

Entities:

Entity 1, DESIGNED PROTEIN TOP7, chain 1 62 residues - Formula weight is not available

1

MET

GLU

ARG

VAL

ARG

ILE

SER

ILE

THR

ALA

2

ARG

THR

LYS

GLU

ALA

GLU

LYS

PHE

ALA

3

ALA

ILE

LEU

ILE

LYS

VAL

PHE

ALA

GLU

LEU

4

GLY

TYR

ASN

ASP

ILE

ASN

VAL

THR

TRP

ASP

5

GLY

ASP

THR

VAL

THR

VAL

GLU

GLY

GLN

LEU

6

GLU

GLY

SER

LEU

GLU

HIS

7

HIS

Samples:

sample_1: Designed protein TOP7 1 mM; phosphate buffer 25 mM; H2O 90%; D2O 10%

sample_2: Designed protein TOP7 1 mM; phosphate buffer 25 mM; D2O 100%

sample_3: Designed protein TOP7, [U-15N; U-13C], 1 mM; phosphate buffer 25 mM; H2O 90%; D2O 10%

sample_4: Designed protein TOP7, [U-15N], 1 mM; phosphate buffer 25 mM; H2O 90%; D2O 10%

sample_cond_1: ionic strength: 25 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D NOESY	not available	not available	sample_cond_1
3D 13C-separated NOESY	not available	not available	sample_cond_1
3D 15N-separated NOESY	not available	not available	sample_cond_1
3D 13C-filtered NOESY	not available	not available	sample_cond_1

Software:

CYANA v2.0 - refinement, structure solution

TALOS - data analysis

NMRPipe v2.3 - processing

SPARKY v3.112 - data analysis

NMR spectrometers:

Varian INOVA 600 MHz