Click here to enlarge.

PDB ID: 9qsb
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34989
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text 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

Please specify the pdb ID.

Title:

The solution structure of the cyanobacterial calcium binding protein CSE at 293 K

Deposition date:

2025-04-04

Original release date:

2026-07-30

Authors:

Kleusberg, F.; Scholl, J.; Selim, K.; Coles, M.

Citation:

Citation: Mueller, T.; Kleusberg, F.; Roganowicz, K.; Selim, K.; Weiss, G.; Coles, M.. "The solution structure of the cyanobacterial calcium binding protein CSE at 293 K " .

Assembly members:

Assembly members:
entity_1, polymer, 96 residues, 10539.474 Da.
entity_CA, non-polymer, 40.078 Da.

Natural source:

Natural source: Common Name: not available Taxonomy ID: 103690 Superkingdom: Bacteria Kingdom: not available Genus/species: Nostoc Nostoc sp. PCC 7120 = FACHB-418

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSSHHHHHHSSGLVPRGSHM ATEQELQSLFNTLDRDQDGK ISINELFLSPGLSAVISSET NTNSPQELLVQYDSDQDGSI TFEELKKAVKKASNLT

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	385
15N chemical shifts	103
1H chemical shifts	629

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1
2	unit_2	2
3	unit_3	2

Entities:

Entity 1, unit_1 96 residues - 10539.474 Da.

1

GLY

SER

HIS

SER

2

SER

GLY

LEU

VAL

PRO

ARG

GLY

SER

HIS

MET

3

ALA

THR

GLU

GLN

GLU

LEU

GLN

SER

LEU

PHE

4

ASN

THR

LEU

ASP

ARG

ASP

GLN

ASP

GLY

LYS

5

ILE

SER

ILE

ASN

GLU

LEU

PHE

LEU

SER

PRO

6

GLY

LEU

SER

ALA

VAL

ILE

SER

GLU

THR

7

ASN

THR

ASN

SER

PRO

GLN

GLU

LEU

VAL

8

GLN

TYR

ASP

SER

ASP

GLN

ASP

GLY

SER

ILE

9

THR

PHE

GLU

LEU

LYS

ALA

VAL

LYS

10

LYS

ALA

SER

ASN

LEU

THR

Entity 2, unit_2 - Ca - 40.078 Da.

1

CA

Samples:

sample_1: CSE, [U-100% 13C; U-100% 15N], 70 uM; TRIS 20 mM; sodium chloride 100 mM

sample_conditions_1: ionic strength: 116 mM; pH: 7.9; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CACO)NH	sample_1	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D CCH-TOCSY (arom)	sample_1	isotropic	sample_conditions_1
2D Plush-TACSY	sample_1	isotropic	sample_conditions_1
3D CNH-NOESY	sample_1	isotropic	sample_conditions_1
2D NOESY (14N-filtered)	sample_1	isotropic	sample_conditions_1

Software:

CoMAND, ElGamacy, Riss, Zhu, Truffault, Murray, Coles - refinement

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

Sparky, Goddard - chemical shift assignment

TopSpin, Bruker Biospin - collection, processing

NMR spectrometers:

Bruker AVANCE III 600 MHz
Bruker AVANCE III 800 MHz

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

BMRB Entry 34989