BMRB Entry 4589

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PDB ID: 1ehx
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR4589
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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:

NMR Solution Structure of the Last Unknown Module of the Cellulosomal Scaffoldin Protein CIPC of Clostridum cellulolyticum

Deposition date:

2000-05-05

Original release date:

2001-03-08

Authors:

Mosbah, A.; Belaich, A.; Bornet, O.; Belaich, J.; Henrissat, B.; Darbon, H.

Citation:

Citation: Mosbah, A.; Belaich, A.; Bornet, O.; Belaich, J.; Henrissat, B.; Darbon, H.. "NMR Solution Structure of the Last Unknown Module of the Cellulosomal Scaffoldin Protein CIPC of Clostridum cellulolyticum" J. Mol. Biol. 304, 201-217 (2000).

Assembly members:

Assembly members:
scaffoldin protein, polymer, 94 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Clostridium cellulolyticum Taxonomy ID: 1521 Superkingdom: Bacteria Kingdom: not available Genus/species: Clostridium cellulolyticum

Experimental source:

Experimental source: Production method: .

Entity Sequences (FASTA):

Entity Sequences (FASTA):
scaffoldin protein: MQDPTINPTSISAKAGSFAD TKITLTPNGNTFNGISELQS SQYTKGTNEVTLLASYLNTL PENTTKTLTFDFGVGTKNPK LTITVLPKDIPGLE

Data sets:

assigned_chemical_shifts
- chemical_shift_set_1
coupling_constants
- coupling_constants

Data type	Count
15N chemical shifts	86
1H chemical shifts	525
coupling constants	77

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	scaffoldin protein	1

Entities:

Entity 1, scaffoldin protein 94 residues - Formula weight is not available

1

MET

GLN

ASP

PRO

THR

ILE

ASN

PRO

THR

SER

2

ILE

SER

ALA

LYS

ALA

GLY

SER

PHE

ALA

ASP

3

THR

LYS

ILE

THR

LEU

THR

PRO

ASN

GLY

ASN

4

THR

PHE

ASN

GLY

ILE

SER

GLU

LEU

GLN

SER

5

SER

GLN

TYR

THR

LYS

GLY

THR

ASN

GLU

VAL

6

THR

LEU

ALA

SER

TYR

LEU

ASN

THR

LEU

7

PRO

GLU

ASN

THR

LYS

THR

LEU

THR

PHE

8

ASP

PHE

GLY

VAL

GLY

THR

LYS

ASN

PRO

LYS

9

LEU

THR

ILE

THR

VAL

LEU

PRO

LYS

ASP

ILE

10

PRO

GLY

LEU

GLU

Samples:

sample_1: scaffoldin protein, [U-15N], 25 mM; sodium acetate buffer 20 mM; H2O 90%; D2O 10%

sample_cond_1: pH: 5.0; pressure: 1 atm; temperature: 300 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D NOESY	sample_1	not available	sample_cond_1
3D 15N-separated_NOESY	sample_1	not available	sample_cond_1
DQF-COSY	sample_1	not available	sample_cond_1
2D 15N HSQC	sample_1	not available	sample_cond_1
2D 15N HSQC_NOESY	sample_1	not available	sample_cond_1
2D 15N HSQC_TOCSY	sample_1	not available	sample_cond_1

Software:

xwinnmr v2.1 - processing

XEASY v1.2 - data analysis

DIANA v2.8 - structure solution

CNS v1.0 - refinement

NMR spectrometers:

Bruker DRX 500 MHz