BMRB Entry 10043

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PDB ID: 1wgw
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR10043
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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 N-terminal Domain of Mouse Putative Signal Recoginition Particle 54 (SRP54)

Deposition date:

2006-11-09

Original release date:

2008-08-13

Authors:

Li, H.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.

Citation:

Citation: Li, H.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution Structure of the N-terminal Domain of Mouse Putative Signal Recoginition Particle 54 (SRP54)" .

Assembly members:

Assembly members:
N-terminal domain, polymer, 99 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: P030908-15

Entity Sequences (FASTA):

Entity Sequences (FASTA):
N-terminal domain: GSSGSSGADLGRKITSALRS LSNATIINEEVLNAMLKEVC TALLEADVNIKLVKQLRENV KSAIDLEEMASGLNKRKMIQ HAVFKELVKVKVYSGPSSG

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	407
15N chemical shifts	103
1H chemical shifts	683

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Signal Recoginition Particle 54	1

Entities:

Entity 1, Signal Recoginition Particle 54 99 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

ALA

ASP

LEU

2

GLY

ARG

LYS

ILE

THR

SER

ALA

LEU

ARG

SER

3

LEU

SER

ASN

ALA

THR

ILE

ASN

GLU

4

VAL

LEU

ASN

ALA

MET

LEU

LYS

GLU

VAL

CYS

5

THR

ALA

LEU

GLU

ALA

ASP

VAL

ASN

ILE

6

LYS

LEU

VAL

LYS

GLN

LEU

ARG

GLU

ASN

VAL

7

LYS

SER

ALA

ILE

ASP

LEU

GLU

MET

ALA

8

SER

GLY

LEU

ASN

LYS

ARG

LYS

MET

ILE

GLN

9

HIS

ALA

VAL

PHE

LYS

GLU

LEU

VAL

LYS

VAL

10

LYS

VAL

TYR

SER

GLY

PRO

SER

GLY

Samples:

sample_1: Protein, [U-13C, U-15N], 1.04 mM; Phosphate 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 13C-separated NOESY	sample_1	not available	condition_1
3D 15N-separated NOESY	sample_1	not available	condition_1

Software:

xwinnmr v2.6, Bruker - collection

NMRPipe v20020425, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B. A. - data analysis

Kujira v0.897, Kobayashi, N. - data analysis

CYANA v1.0.7, Guntert, P. - refinement, structure solution

NMR spectrometers:

Bruker AVANCE 800 MHz

PDB	1WGW
GB	EAW65895 ELK11325 ELW63179 EPQ06973 KFO29291
REF	XP_004376574 XP_005989239 XP_010211978 XP_012513641 XP_012867695