BMRB Entry 10127

Name: Solution structure of the alpha-helical domain from mouse hypothetical PNPase
Published: 2008-09-02

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PDB ID: 1whu
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR10127
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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:

Solution structure of the alpha-helical domain from mouse hypothetical PNPase

Deposition date:

2007-04-02

Original release date:

2008-09-02

Authors:

Nagata, T.; Muto, Y.; Inoue, M.; Kigawa, T.; Terada, T.; Shirouzu, M.; Yokoyama, S.

Citation:

Citation: Nagata, T.; Muto, Y.; Inoue, M.; Kigawa, T.; Terada, T.; Shirouzu, M.; Yokoyama, S.. "Solution structure of the alpha-helical domain from mouse hypothetical PNPase" .

Assembly members:

Assembly members:
alpha-helical domain, polymer, 104 residues, Formula weight is not available

Natural source:

Natural source: Common Name: mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

Experimental source: Production method: cell free synthesis Vector: P031222-56

Entity Sequences (FASTA):

Entity Sequences (FASTA):
alpha-helical domain: GSSGSSGPQKIFTPSAEIVK YTKIIAMEKLYAVFTDYEHD KVSRDEAVNKIRLDTEEHLK EKFPEVDQFEIIESFNIVAK EVFRSIILNEYKRCDGRDSG PSSG

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	427
15N chemical shifts	88
1H chemical shifts	676

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	hypothetical PNPase	1

Entities:

Entity 1, hypothetical PNPase 104 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

PRO

GLN

LYS

2

ILE

PHE

THR

PRO

SER

ALA

GLU

ILE

VAL

LYS

3

TYR

THR

LYS

ILE

ALA

MET

GLU

LYS

LEU

4

TYR

ALA

VAL

PHE

THR

ASP

TYR

GLU

HIS

ASP

5

LYS

VAL

SER

ARG

ASP

GLU

ALA

VAL

ASN

LYS

6

ILE

ARG

LEU

ASP

THR

GLU

HIS

LEU

LYS

7

GLU

LYS

PHE

PRO

GLU

VAL

ASP

GLN

PHE

GLU

8

ILE

GLU

SER

PHE

ASN

ILE

VAL

ALA

LYS

9

GLU

VAL

PHE

ARG

SER

ILE

LEU

ASN

GLU

10

TYR

LYS

ARG

CYS

ASP

GLY

ARG

ASP

SER

GLY

11

PRO

SER

GLY

Samples:

sample_1: alpha-helical domain, [U-13C; U-15N], 1.12 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 13C-separated NOESY	sample_1	isotropic	condition_1
3D 15N-separated NOESY	sample_1	isotropic	condition_1

Software:

NMRView v5.0.4, Johnson - data analysis

CYANA v2.0, Guntert, P. - refinement, structure solution

NMRPipe v2.3, Delaglio, F. - processing

Kujira v0.901, Kobayashi, N. - data analysis

NMR spectrometers:

Bruker AVANCE 800 MHz

PDB	1WHU
DBJ	BAB23374 BAE25732 BAE28862 BAE36595 BAE38260
EMBL	CAD45436
GB	AAH27228 AAH55826 EDL23813 EDL23814
REF	NP_082145 XP_006514876 XP_011242053
SP	Q8K1R3
AlphaFold	Q8K1R3