BMRB Entry 17851

Name: Backbone 1H, 15N, 13C assignments for beta phosphoglucomutase in a binary complex with BeF3-
Published: 2012-06-01

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR17851

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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:

Backbone 1H, 15N, 13C assignments for beta phosphoglucomutase in a binary complex with BeF3-

Deposition date:

2011-08-10

Original release date:

2012-06-01

Authors:

Baxter, Nicola; Griffin, Joanna; Waltho, Jonathan

Citation:

Citation: Griffin, Joanna; Bowler, Matthew; Baxter, Nicola; Leigh, Katherine; Dannatt, Hugh; Hounslow, Andrea; Blackburn, G. Michael; Webster, Charles Edwin; Cliff, Matthew; Waltho, Jonathan. "Near attack conformers dominate beta-phosphoglucomutase complexes where geometry and charge distribution reflect those of substrate." Proc. Natl. Acad. Sci. U. S. A. 109, 6910-6915 (2012).
PubMed: 22505741

Assembly members:

Assembly members:
beta_phosphoglucomutase, polymer, 221 residues, Formula weight is not available
BEF, non-polymer, 66.007 Da.
MG, non-polymer, 24.305 Da.

Natural source:

Natural source: Common Name: Lactococcus lactis Taxonomy ID: 1358 Superkingdom: Bacteria Kingdom: not available Genus/species: Lactococcus lactis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-22b(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
beta_phosphoglucomutase: MFKAVLFDLDGVITDTAEYH FRAWKALAEEIGINGVDRQF NEQLKGVSREDSLQKILDLA DKKVSAEEFKELAKRKNDNY VKMIQDVSPADVYPGILQLL KDLRSNKIKIALASASKNGP FLLERMNLTGYFDAIADPAE VAASKPAPDIFIAAAHAVGV APSESIGLEDSQAGIQAIKD SGALPIGVGRPEDLGDDIVI VPDTSHYTLEFLKEVWLQKQ K

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	643
15N chemical shifts	208
19F chemical shifts	3
1H chemical shifts	208

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	phosphoenzyme analogue	1
2	BERYLLIUM TRIFLUORIDE ION	2
3	Magnesium ion	3

Entities:

Entity 1, phosphoenzyme analogue 221 residues - Formula weight is not available

1

MET

PHE

LYS

ALA

VAL

LEU

PHE

ASP

LEU

ASP

2

GLY

VAL

ILE

THR

ASP

THR

ALA

GLU

TYR

HIS

3

PHE

ARG

ALA

TRP

LYS

ALA

LEU

ALA

GLU

4

ILE

GLY

ILE

ASN

GLY

VAL

ASP

ARG

GLN

PHE

5

ASN

GLU

GLN

LEU

LYS

GLY

VAL

SER

ARG

GLU

6

ASP

SER

LEU

GLN

LYS

ILE

LEU

ASP

LEU

ALA

7

ASP

LYS

VAL

SER

ALA

GLU

PHE

LYS

8

GLU

LEU

ALA

LYS

ARG

LYS

ASN

ASP

ASN

TYR

9

VAL

LYS

MET

ILE

GLN

ASP

VAL

SER

PRO

ALA

10

ASP

VAL

TYR

PRO

GLY

ILE

LEU

GLN

LEU

11

LYS

ASP

LEU

ARG

SER

ASN

LYS

ILE

LYS

ILE

12

ALA

LEU

ALA

SER

ALA

SER

LYS

ASN

GLY

PRO

13

PHE

LEU

GLU

ARG

MET

ASN

LEU

THR

GLY

14

TYR

PHE

ASP

ALA

ILE

ALA

ASP

PRO

ALA

GLU

15

VAL

ALA

SER

LYS

PRO

ALA

PRO

ASP

ILE

16

PHE

ILE

ALA

HIS

ALA

VAL

GLY

VAL

17

ALA

PRO

SER

GLU

SER

ILE

GLY

LEU

GLU

ASP

18

SER

GLN

ALA

GLY

ILE

GLN

ALA

ILE

LYS

ASP

19

SER

GLY

ALA

LEU

PRO

ILE

GLY

VAL

GLY

ARG

20

PRO

GLU

ASP

LEU

GLY

ASP

ILE

VAL

ILE

21

VAL

PRO

ASP

THR

SER

HIS

TYR

THR

LEU

GLU

22

PHE

LEU

LYS

GLU

VAL

TRP

LEU

GLN

LYS

GLN

23

LYS

Entity 2, BERYLLIUM TRIFLUORIDE ION - Be F3 - 66.007 Da.

1

BEF

Entity 3, Magnesium ion - Mg - 24.305 Da.

1

MG

Samples:

sample_1: beta phosphoglucomutase, [U-13C; U-15N; U-2H], 1 mM; magnesium chloride 5 mM; ammonium fluoride 10 mM; beryllium chloride 5 mM; sodium azide 2 mM; D2O, [U-100% 2H], 10%; potassium HEPES 50 mM; H2O 90%

sample_2: beta phosphoglucomutase 0.5 mM; magnesium chloride 5 mM; ammonium fluoride 10 mM; beryllium chloride 5 mM; sodium azide 2 mM; D2O, [U-100% 2H], 10%; potassium HEPES 50 mM; H2O 90%

sample_conditions_1: ionic strength: 70 mM; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N TROSY	sample_1	isotropic	sample_conditions_1
3D TROSY HNCA	sample_1	isotropic	sample_conditions_1
3D TROSY HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D TROSY HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D TROSY HNCO	sample_1	isotropic	sample_conditions_1
3D TROSY HN(CA)CB	sample_1	isotropic	sample_conditions_1
3D TROSY HN(COCA)CB	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
19F 1D	sample_2	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, data analysis

FELIX, Accelrys Software Inc. - chemical shift assignment, data analysis, peak picking, processing

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 500 MHz