BMRB Entry 4241

Name: 1H and 15N Assignments of Internal xylan binding domain from XYLD
Published: 1999-11-29

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PDB ID: 2xbd
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR4241
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:

1H and 15N Assignments of Internal xylan binding domain from XYLD

Deposition date:

1998-10-09

Original release date:

1999-11-29

Authors:

Simpson, Peter; Bolam, David; Cooper, Alan; Ciruela, Antonio; Hazlewood, Geoffrey; Gilbert, Harry; Williamson, Michael

Citation:

Citation: Simpson, Peter; Bolam, David; Cooper, Alan; Ciruela, Antonio; Hazlewood, Geoffrey; Gilbert, Harry; Williamson, Michael. "The Three-Dimensional Structure of a Family IIb Xylan Binding Domain: Evidence that the Orientation of the Solvent-Exposed Tryptophans Determines the Ligand Specificity of Type II Polysaccharide Binding Domains." Structure 7, 853-864 (1999).

Assembly members:

Assembly members:
xylanase D, polymer, 87 residues, Formula weight is not available

Natural source:

Natural source: Common Name: not available Taxonomy ID: 1708 Superkingdom: eubacteria Kingdom: not available Genus/species: Cellulomonas fimi

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli

Entity Sequences (FASTA):

Entity Sequences (FASTA):
xylanase D: TGCSVTATRAEEWSDRFNVT YSVSGSSAWTVNLALNGSQT IQASWNANVTGSGSTRTVTP NGSGNTFGVTVMKNGSSTTP AATCAGS

Data sets:

assigned_chemical_shifts
- chemical_shift_assignment_one

Data type	Count
15N chemical shifts	100
1H chemical shifts	532

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	XBD1-XYLD	1

Entities:

Entity 1, XBD1-XYLD 87 residues - Formula weight is not available

1

THR

GLY

CYS

SER

VAL

THR

ALA

THR

ARG

ALA

2

GLU

TRP

SER

ASP

ARG

PHE

ASN

VAL

THR

3

TYR

SER

VAL

SER

GLY

SER

ALA

TRP

THR

4

VAL

ASN

LEU

ALA

LEU

ASN

GLY

SER

GLN

THR

5

ILE

GLN

ALA

SER

TRP

ASN

ALA

ASN

VAL

THR

6

GLY

SER

GLY

SER

THR

ARG

THR

VAL

THR

PRO

7

ASN

GLY

SER

GLY

ASN

THR

PHE

GLY

VAL

THR

8

VAL

MET

LYS

ASN

GLY

SER

THR

PRO

9

ALA

THR

CYS

ALA

GLY

SER

Samples:

sample_one: xylanase D, [U-99% 15N], 1.0 mM; sodium_phosphate 50 mM

sample_conditions_one: pH: 5.0; temperature: 310 K

Experiments:

Name	Sample	Sample state	Sample conditions
COSY	sample_one	not available	not available
NOESY	sample_one	not available	not available
TOCSY	sample_one	not available	not available
E. COSY	sample_one	not available	not available
1H-15N HSQC	sample_one	not available	not available
NOESY-HMQC	sample_one	not available	not available
TOCSY-HMQC	sample_one	not available	not available
HNHA	sample_one	not available	not available
HNHB	sample_one	not available	not available

Software:

FELIX v97.0 -

NMR spectrometers:

Bruker DRX 500 MHz
Bruker DRX 600 MHz
Bruker DRX 800 MHz