BMRB Entry 26802

Name: Cold Shock Protein A
Published: 2017-05-30

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PDB ID: 5o6f
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26802
MolProbity Validation Chart

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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:

Cold Shock Protein A

Deposition date:

2016-05-17

Original release date:

2017-05-30

Authors:

Caruso, Icaro; Panwalkar, Vineet; Arni, Raghuvir; Cornelio, Marinonio

Citation:

Citation: Caruso, Icaro; Panwalkar, Vineet; Coronado, Monika; Dingley, Andrew; Cornelio, Marinonio; Willbold, Dieter; Arni, Raghuvir; Eberle, Raphael. "Structure and interaction of Corynebacterium pseudotuberculosis cold shock protein A with Y-box single-stranded DNA fragment." FEBS J. 285, 372-390 (2018).
PubMed: 29197185

Assembly members:

Assembly members:
Molecule_1, polymer, 82 residues, 9118.9276 Da.

Natural source:

Natural source: Common Name: high GC Gram+ Taxonomy ID: 1719 Superkingdom: Bacteria Kingdom: not available Genus/species: Corynebacterium pseudotuberculosis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pD441-SR

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Molecule_1: MAQGTVKWFNAEKGFGFIAP DDGSADVFVHYSEIQGNGFR TLEENQKVEFEIGEGAKGPQ AQQVHALGGENLYFQGHHHH HH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list
spectral_peak_list

Data type	Count
13C chemical shifts	322
15N chemical shifts	84
1H chemical shifts	494

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Cold Shock Protein A	1

Entities:

Entity 1, Cold Shock Protein A 82 residues - 9118.9276 Da.

1

MET

ALA

GLN

GLY

THR

VAL

LYS

TRP

PHE

ASN

2

ALA

GLU

LYS

GLY

PHE

GLY

PHE

ILE

ALA

PRO

3

ASP

GLY

SER

ALA

ASP

VAL

PHE

VAL

HIS

4

TYR

SER

GLU

ILE

GLN

GLY

ASN

GLY

PHE

ARG

5

THR

LEU

GLU

ASN

GLN

LYS

VAL

GLU

PHE

6

GLU

ILE

GLY

GLU

GLY

ALA

LYS

GLY

PRO

GLN

7

ALA

GLN

VAL

HIS

ALA

LEU

GLY

GLU

8

ASN

LEU

TYR

PHE

GLN

GLY

HIS

9

HIS

Samples:

CspA: Molecule 1, [U-13C; U-15N], 0.8 mM; K2HPO4 50.0 mM; NaCl 50.0 mM; DSS 0.1 mM; H2O 90%; D2O 10%

CspA_1: ionic strength: 0.050 M; pH: 6.500; pressure: 1.000 atm; temperature: 298.000 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC/HMQC	CspA	isotropic	CspA_1
2D 1H-13C HSQC/HMQC	CspA	isotropic	CspA_1
hbcbcgcdhd (hbCBcgcdHD)	CspA	isotropic	CspA_1
hbcbcgcdcehe (hbCBcgcdceHE)	CspA	isotropic	CspA_1
3D 1H-13C NOESY	CspA	isotropic	CspA_1
3D HNCO	CspA	isotropic	CspA_1

Software:

CcpNmr_Analysis v2.4, CCPN - Chemical shift assignment

NMR spectrometers:

Varian VNMRS 900 MHz
Bruker Avance 599 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks