BMRB Entry 30209

Name: NMR structure of the precursor protein PawS1 comprising SFTI-1 and a seed storage albumin
Published: 2017-02-20

Click here to enlarge.

PDB ID: 5u87
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30209
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
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: NMR structure of the precursor protein PawS1 comprising SFTI-1 and a seed storage albumin

Deposition date: 2016-12-14 Original release date: 2017-02-20

Authors: Franke, B.; James, A.; Mobli, M.; Colgrave, M.; Mylne, J.; Rosengren, K.

Citation: Franke, B.; James, A.; Mobli, M.; Colgrave, M.; Mylne, J.; Rosengren, K.. "NMR structure of the precursor protein PawS1 comprising SFTI-1 and a seed storage albumin" to be published ., .-..

Assembly members:
entity_1, polymer, 116 residues, 13280.334 Da.

Natural source: Common Name: Common sunflower Taxonomy ID: 4232 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Helianthus annuus

Experimental source: Production method: recombinant technology Host organism: Escherichia coli

Entity Sequences (FASTA):
entity_1: GRCTKSIPPICFPDGLDNPR GCQIRIQQLNHCQMHLTSFD YKLRMAVENPKQQQHLSLCC NQLQEVEKQCQCEAIKQVVE QAQKQLQQGQGGQQQVQQMV KKAQMLPNQCNLQCSI

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	482
15N chemical shifts	109
1H chemical shifts	765

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 116 residues - 13280.334 Da.

1

GLY

ARG

CYS

THR

LYS

SER

ILE

PRO

ILE

2

CYS

PHE

PRO

ASP

GLY

LEU

ASP

ASN

PRO

ARG

3

GLY

CYS

GLN

ILE

ARG

ILE

GLN

LEU

ASN

4

HIS

CYS

GLN

MET

HIS

LEU

THR

SER

PHE

ASP

5

TYR

LYS

LEU

ARG

MET

ALA

VAL

GLU

ASN

PRO

6

LYS

GLN

HIS

LEU

SER

LEU

CYS

7

ASN

GLN

LEU

GLN

GLU

VAL

GLU

LYS

GLN

CYS

8

GLN

CYS

GLU

ALA

ILE

LYS

GLN

VAL

GLU

9

GLN

ALA

GLN

LYS

GLN

LEU

GLN

GLY

GLN

10

GLY

GLN

VAL

GLN

MET

VAL

11

LYS

ALA

GLN

MET

LEU

PRO

ASN

GLN

CYS

12

ASN

LEU

GLN

CYS

SER

ILE

Samples:

sample_1: Proalbumin PawS1, [U-13C; U-15N], 3.9 mg/mL

sample_conditions_1: ionic strength: 0 mM; pH: 4.62; pressure: 1 bar; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	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 HNCO	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CC)(CO)NH-TOCSY	sample_1	isotropic	sample_conditions_1
3D (H)CC(CO)NH-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
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1

Software:

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure calculation

CcpNMR, CCPN - peak picking

TOPSPIN v2.1, Bruker Biospin - collection

NMR spectrometers:

Bruker Avance 600 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts