BMRB Entry 16040

Name: Solution structure of onconase C87A/C104A
Published: 2009-11-02

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PDB ID: 2kb6
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16040
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution structure of onconase C87A/C104A

Deposition date:

2008-11-21

Original release date:

2009-11-02

Authors:

Weininger, Ulrich; Schulenburg, Cindy; Arnold, Ulrich; Ulbrich-Hofmann, Renate; Balbach, Jochen

Citation:

Citation: Schulenburg, Cindy; Low, Christian; Weininger, Ulrich; Mrestani-Klaus, Carmen; Hofmann, Hagen; Balbach, Jochen; Ulbrich-Hofmann, Renate; Arnold, Ulrich. "The folding pathway of onconase is directed by a conserved intermediate" Biochemistry 48, 8449-8457 (2009).
PubMed: 19655705

Assembly members:

Assembly members:
onconase C87A/C104A, polymer, 104 residues, 11781.603 Da.

Natural source:

Natural source: Common Name: northern leopard frog Taxonomy ID: 8404 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: rana pipiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-26b(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
onconase C87A/C104A: XDWLTFQKKHITNTRDVDCD NIMSTNLFHCKDKNTFIYSR PEPVKAICKGIIASKNVLTT SEFYLSDCNVTSRPCKYKLK KSTNKFAVTCENQAPVHFVG VGSA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
15N chemical shifts	109
1H chemical shifts	744

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	onconase C87A/C104A	1

Entities:

Entity 1, onconase C87A/C104A 104 residues - 11781.603 Da.

1

PCA

ASP

TRP

LEU

THR

PHE

GLN

LYS

HIS

2

ILE

THR

ASN

THR

ARG

ASP

VAL

ASP

CYS

ASP

3

ASN

ILE

MET

SER

THR

ASN

LEU

PHE

HIS

CYS

4

LYS

ASP

LYS

ASN

THR

PHE

ILE

TYR

SER

ARG

5

PRO

GLU

PRO

VAL

LYS

ALA

ILE

CYS

LYS

GLY

6

ILE

ALA

SER

LYS

ASN

VAL

LEU

THR

7

SER

GLU

PHE

TYR

LEU

SER

ASP

CYS

ASN

VAL

8

THR

SER

ARG

PRO

CYS

LYS

TYR

LYS

LEU

LYS

9

LYS

SER

THR

ASN

LYS

PHE

ALA

VAL

THR

CYS

10

GLU

ASN

GLN

ALA

PRO

VAL

HIS

PHE

VAL

GLY

11

VAL

GLY

SER

ALA

Samples:

sample_1: entity, [U-15N], 1.0 mM; H2O 90%; D2O 10%; sodium phosphate 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1

Software:

ARIA, Linge, O'Donoghue and Nilges - structure solution

NMR spectrometers:

Bruker Avance 600 MHz

BMRB	4371
PDB	1ONC 1PU3 1YV4 1YV6 1YV7 2GMK 2I5S 2KB6 3FD7 3HG6 3PHN 3SNF 3U00 3U01
GB	AAL54383
SP	P22069
AlphaFold	P22069