BMRB Entry 16965

Name: Backbone NMR assignment of the globular domain of HET-s(1-227) prion protein.
Published: 2010-06-30

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16965

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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:

Backbone NMR assignment of the globular domain of HET-s(1-227) prion protein.

Deposition date:

2010-05-30

Original release date:

2010-06-30

Authors:

Schuetz, Anne; Greenwald, Jason; Riek, Roland; Bockmann, Anja; Meier, Beat

Citation:

Citation: Schuetz, Anne; Wasmer, Christian; Habenstein, Birgit; Verel, Rene; Greenwald, Jason; Riek, Roland; Bockmann, Anja; Meier, Beat. "Protocols for the sequential solid-state NMR spectroscopic assignment of a uniformly labeled 25 kDa protein: HET-s(1-227)." Chembiochem 11, 1543-1551 (2010).
PubMed: 20572250

Assembly members:

Assembly members:
HET-s, polymer, 229 residues, 25470 Da.

Natural source:

Natural source: Common Name: ascomycetes Taxonomy ID: 5145 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Podospora anserina

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HET-s: GSMSEPFGIVAGALNVAGLF NNCVDCFEYVQLGRPFGRDY ERCQLRLDIAKARLSRWGEA VKINDDPRFHSSAPTDKSVQ LAKSIVEEILLLFESAQKTS KRYELVADQQDLVVFEDKDM KPIGRALHRRLNDLVSRRQK QTSLAKKTAWALYDGKSLEK IVDQVARFVDELEKAFPIEA VCHKLAEIEIEEVEDEASLT ILKDAAGGIDAAMSDAAAQK IDAIVGRNS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	367
15N chemical shifts	188

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HET-s(1-227)	1

Entities:

Entity 1, HET-s(1-227) 229 residues - 25470 Da.

The first two residues represent non-native remainders of a cleaved HIS-tag. This is the globular domain of a prion protein.

1

GLY

SER

MET

SER

GLU

PRO

PHE

GLY

ILE

VAL

2

ALA

GLY

ALA

LEU

ASN

VAL

ALA

GLY

LEU

PHE

3

ASN

CYS

VAL

ASP

CYS

PHE

GLU

TYR

VAL

4

GLN

LEU

GLY

ARG

PRO

PHE

GLY

ARG

ASP

TYR

5

GLU

ARG

CYS

GLN

LEU

ARG

LEU

ASP

ILE

ALA

6

LYS

ALA

ARG

LEU

SER

ARG

TRP

GLY

GLU

ALA

7

VAL

LYS

ILE

ASN

ASP

PRO

ARG

PHE

HIS

8

SER

ALA

PRO

THR

ASP

LYS

SER

VAL

GLN

9

LEU

ALA

LYS

SER

ILE

VAL

GLU

ILE

LEU

10

LEU

PHE

GLU

SER

ALA

GLN

LYS

THR

SER

11

LYS

ARG

TYR

GLU

LEU

VAL

ALA

ASP

GLN

12

ASP

LEU

VAL

PHE

GLU

ASP

LYS

ASP

MET

13

LYS

PRO

ILE

GLY

ARG

ALA

LEU

HIS

ARG

14

LEU

ASN

ASP

LEU

VAL

SER

ARG

GLN

LYS

15

GLN

THR

SER

LEU

ALA

LYS

THR

ALA

TRP

16

ALA

LEU

TYR

ASP

GLY

LYS

SER

LEU

GLU

LYS

17

ILE

VAL

ASP

GLN

VAL

ALA

ARG

PHE

VAL

ASP

18

GLU

LEU

GLU

LYS

ALA

PHE

PRO

ILE

GLU

ALA

19

VAL

CYS

HIS

LYS

LEU

ALA

GLU

ILE

GLU

ILE

20

GLU

VAL

GLU

ASP

GLU

ALA

SER

LEU

THR

21

ILE

LEU

LYS

ASP

ALA

GLY

ILE

ASP

22

ALA

MET

SER

ASP

ALA

GLN

LYS

23

ILE

ASP

ALA

ILE

VAL

GLY

ARG

ASN

SER

Samples:

sample_1: HET-s, [U-100% 13C; U-100% 15N; U-99% 2H], 1 mM; DTT 2 mM; potassium phosphate 50 mM; sodium chloride 20 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 70 mM; pH: 7; pressure: 1 atm; temperature: 297 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1

Software:

SPARKY v3.115, Goddard - chemical shift assignment

NMR spectrometers:

Bruker Avance 700 MHz

BMRB	16964
PDB	2WVN
GB	AAB19707 AAB94631
PRF	1718317A
SP	Q03689
AlphaFold	Q03689