BMRB Entry 17519

Name: Solution Strucuture of CBM25-2 of beta/alpha-amylase from Paenibacillus polymyxa
Published: 2012-08-07

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PDB ID: 2lab
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17519
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution Strucuture of CBM25-2 of beta/alpha-amylase from Paenibacillus polymyxa

Deposition date:

2011-03-09

Original release date:

2012-08-07

Authors:

Takahashi, Ryosuke; Yoshida, Takuya; Ohkubo, Tadayasu; Sumitani, Jun-ichi; Nishimura, Shigenori

Citation:

Citation: Takahashi, Ryosuke; Horibe, Ippei; Fukada, Harumi; Yoshida, Takuya; Ohkubo, Tadayasu; Inui, Takashi; Nishimura, Shigenori; Sumitani, Jun-ichi. "A functional and structural analysis of tundem family 25 carbohydrate-binding modules from Paenibacillus polymyxa beta/alpha-amylase" Protein Sci. ., .-..

Assembly members:

Assembly members:
carbohydrate_binding_module, polymer, 104 residues, 10844.803 Da.

Natural source:

Natural source: Common Name: Bacillus polymyxa Taxonomy ID: 1406 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus polymyxa

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET16b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
carbohydrate_binding_module: GGTTNKVTVYYKKGFNSPYI HYRPAGGSWTAAPGVKMQDA EISGYAKITVDIGSASQLEA AFNDGNNNWDSNNTKNYLFS TGTSTYTPGSNGAAGTIRTG APSG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	398
15N chemical shifts	112
1H chemical shifts	595

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Starch Binding Domain 2 of beta/alpha-amylase	1

Entities:

Entity 1, Starch Binding Domain 2 of beta/alpha-amylase 104 residues - 10844.803 Da.

1

GLY

THR

ASN

LYS

VAL

THR

VAL

TYR

2

TYR

LYS

GLY

PHE

ASN

SER

PRO

TYR

ILE

3

HIS

TYR

ARG

PRO

ALA

GLY

SER

TRP

THR

4

ALA

PRO

GLY

VAL

LYS

MET

GLN

ASP

ALA

5

GLU

ILE

SER

GLY

TYR

ALA

LYS

ILE

THR

VAL

6

ASP

ILE

GLY

SER

ALA

SER

GLN

LEU

GLU

ALA

7

ALA

PHE

ASN

ASP

GLY

ASN

TRP

ASP

8

SER

ASN

THR

LYS

ASN

TYR

LEU

PHE

SER

9

THR

GLY

THR

SER

THR

TYR

THR

PRO

GLY

SER

10

ASN

GLY

ALA

GLY

THR

ILE

ARG

THR

GLY

11

ALA

PRO

SER

GLY

Samples:

sample_1: sodium acetate, [U-100% 15N], 0.5-1.2 mM; sodium acetate, [U-13C; U-15N], 0.5-1.2 mM

sample_2: sodium acetate, [U-100% 15N], 0.6 mM

sample_conditions_1: ionic strength: 20 mM; pH: 5.5; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(COCA)CB	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1

Software:

DYANA, Guntert, Braun and Wuthrich - refinement, structure solution

SPARKY, Goddard - chemical shift assignment

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - collection

NMR spectrometers:

Varian INOVA 600 MHz