BMRB Entry 15478

Name: 1H and 15N resonance assignment of M7, a computationally-designed artificial protein
Published: 2008-06-25

Click here to enlarge.

PDB ID: 2jvf
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15478
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

1H and 15N resonance assignment of M7, a computationally-designed artificial protein

Deposition date:

2007-09-19

Original release date:

2008-06-25

Authors:

Stordeur, Claudius; Dalluege, Roman; Birkenmeier, Olaf; Wienk, Hans; Rudolph, Rainer; Lange, Christian; Luecke, Christian

Citation:

Citation: Stordeur, Claudius; Dalluege, Roman; Birkenmeier, Olaf; Wienk, Hans; Rudolph, Rainer; Lange, Christian; Luecke, Christian. "The NMR solution structure of the artificial protein M7 matches the computationally designed model" Proteins 72, 1104-1107 (2008).
PubMed: 18498106

Assembly members:

Assembly members:
M7, polymer, 96 residues, 10820.4 Da.

Natural source:

Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not applicable

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
M7: GSHMKVDITIKIQRDGQEIE IDIRVSTGKELERALQELEK ALARAGARNVQITISAENDE QAKELLELIARLLQKLGYKD INVRVNGTEVKIEVRV

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
15N chemical shifts	111
1H chemical shifts	728

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	M7	1

Entities:

Entity 1, M7 96 residues - 10820.4 Da.

The first four residues GSHM represent a cloning artifact; the protein sequence starts at Lys1.

1

GLY

SER

HIS

MET

LYS

VAL

ASP

ILE

THR

ILE

2

LYS

ILE

GLN

ARG

ASP

GLY

GLN

GLU

ILE

GLU

3

ILE

ASP

ILE

ARG

VAL

SER

THR

GLY

LYS

GLU

4

LEU

GLU

ARG

ALA

LEU

GLN

GLU

LEU

GLU

LYS

5

ALA

LEU

ALA

ARG

ALA

GLY

ALA

ARG

ASN

VAL

6

GLN

ILE

THR

ILE

SER

ALA

GLU

ASN

ASP

GLU

7

GLN

ALA

LYS

GLU

LEU

GLU

LEU

ILE

ALA

8

ARG

LEU

GLN

LYS

LEU

GLY

TYR

LYS

ASP

9

ILE

ASN

VAL

ARG

VAL

ASN

GLY

THR

GLU

VAL

10

LYS

ILE

GLU

VAL

ARG

VAL

Samples:

sample_1: M7 1.0 mM; sodium phosphate 25 mM; sodium azide 0.05%; H2O 95%; D2O 5%

sample_2: M7, [U-98% 15N], 1.3 mM; sodium phosphate 25 mM; sodium azide 0.05%; H2O 95%; D2O 5%

sample_3: M7 1.0 mM; sodium phosphate 25 mM; sodium azide 0.05%; D2O 100%

sample_conditions_1: ionic strength: 25 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
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_2	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
2D 1H-15N HTQC	sample_2	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_3	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_3	isotropic	sample_conditions_1

Software:

xwinnmr v3.5, Bruker Biospin - collection, processing

FELIX v2000, Accelrys Software Inc. - data analysis

DYANA v1.5, Guntert, Braun and Wuthrich - structure solution

DISCOVER v2000, Accelrys Software Inc. - refinement

NMR spectrometers:

Bruker DRX 500 MHz