BMRB Entry 27314

Name: Acidothermus cellulolyticus endoglucanase 1 catalytic domain Y245G (E1)
Published: 2017-12-04

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27314

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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:

Acidothermus cellulolyticus endoglucanase 1 catalytic domain Y245G (E1)

Deposition date:

2017-11-16

Original release date:

2017-12-04

Authors:

Summers, Samantha; Kaar, Joel; Summers, Michael; Marchant, Jan

Citation:

Citation: Summers, Samantha; Sprenger, Kayla; Pfaendtner, Jim; Marchant, Jan; Summers, Michael; Kaar, Joel. "Mechanism of Competitive Inhibition and Destabilization of Acidothermus cellulolyticus Endoglucanase 1 by Ionic Liquids" J. Phys. Chem. B 121, 10793-10803 (2017).
PubMed: 29120187

Assembly members:

Assembly members:
E1_Y245G, polymer, 361 residues, 40502 Da.

Natural source:

Natural source: Common Name: Acidothermus cellulolyticus Taxonomy ID: 28049 Superkingdom: Bacteria Kingdom: not available Genus/species: Acidothermus cellulolyticus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-21

Entity Sequences (FASTA):

Entity Sequences (FASTA):
E1_Y245G: MKLAGGGYWHTSGREILDAN NVPVRIAGINWFGFETCNYV VHGLWSRDYRSMLDQIKSLG YNTIRLPYSDDILKPGTMPN SINFYQMNQDLQGLTSLQVM DKIVAYAGQIGLRIILDRHR PDCSGQSALWYTSSVSEATW ISDLQALAQRYKGNPTVVGF DLHNEPHDPACWGCGDPSID WRLAAERAGNAVLSVNPNLL IFVEGVQSYNGDSYWWGGNL QGAGQYPVVLNVPNRLVYSA HDYATSVGPQTWFSDPTFPN NMPGIWNKNWGYLFNQNIAP VWLGEFGTTLQSTTDQTWLK TLVQYLRPTAQYGADSFQWT FWSWNPDSGDTGGILKDDWQ TVDTVKDGYLAPIKSSIFDP V

Data sets:

assigned_chemical_shifts
- E1_Y245G_assignments

Data type	Count
13C chemical shifts	803
15N chemical shifts	247
1H chemical shifts	247

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	E1 Y245G	1

Entities:

Entity 1, E1 Y245G 361 residues - 40502 Da.

1

MET

LYS

LEU

ALA

GLY

TYR

TRP

HIS

2

THR

SER

GLY

ARG

GLU

ILE

LEU

ASP

ALA

ASN

3

ASN

VAL

PRO

VAL

ARG

ILE

ALA

GLY

ILE

ASN

4

TRP

PHE

GLY

PHE

GLU

THR

CYS

ASN

TYR

VAL

5

VAL

HIS

GLY

LEU

TRP

SER

ARG

ASP

TYR

ARG

6

SER

MET

LEU

ASP

GLN

ILE

LYS

SER

LEU

GLY

7

TYR

ASN

THR

ILE

ARG

LEU

PRO

TYR

SER

ASP

8

ASP

ILE

LEU

LYS

PRO

GLY

THR

MET

PRO

ASN

9

SER

ILE

ASN

PHE

TYR

GLN

MET

ASN

GLN

ASP

10

LEU

GLN

GLY

LEU

THR

SER

LEU

GLN

VAL

MET

11

ASP

LYS

ILE

VAL

ALA

TYR

ALA

GLY

GLN

ILE

12

GLY

LEU

ARG

ILE

LEU

ASP

ARG

HIS

ARG

13

PRO

ASP

CYS

SER

GLY

GLN

SER

ALA

LEU

TRP

14

TYR

THR

SER

VAL

SER

GLU

ALA

THR

TRP

15

ILE

SER

ASP

LEU

GLN

ALA

LEU

ALA

GLN

ARG

16

TYR

LYS

GLY

ASN

PRO

THR

VAL

GLY

PHE

17

ASP

LEU

HIS

ASN

GLU

PRO

HIS

ASP

PRO

ALA

18

CYS

TRP

GLY

CYS

GLY

ASP

PRO

SER

ILE

ASP

19

TRP

ARG

LEU

ALA

GLU

ARG

ALA

GLY

ASN

20

ALA

VAL

LEU

SER

VAL

ASN

PRO

ASN

LEU

21

ILE

PHE

VAL

GLU

GLY

VAL

GLN

SER

TYR

ASN

22

GLY

ASP

SER

TYR

TRP

GLY

ASN

LEU

23

GLN

GLY

ALA

GLY

GLN

TYR

PRO

VAL

LEU

24

ASN

VAL

PRO

ASN

ARG

LEU

VAL

TYR

SER

ALA

25

HIS

ASP

TYR

ALA

THR

SER

VAL

GLY

PRO

GLN

26

THR

TRP

PHE

SER

ASP

PRO

THR

PHE

PRO

ASN

27

ASN

MET

PRO

GLY

ILE

TRP

ASN

LYS

ASN

TRP

28

GLY

TYR

LEU

PHE

ASN

GLN

ASN

ILE

ALA

PRO

29

VAL

TRP

LEU

GLY

GLU

PHE

GLY

THR

LEU

30

GLN

SER

THR

ASP

GLN

THR

TRP

LEU

LYS

31

THR

LEU

VAL

GLN

TYR

LEU

ARG

PRO

THR

ALA

32

GLN

TYR

GLY

ALA

ASP

SER

PHE

GLN

TRP

THR

33

PHE

TRP

SER

TRP

ASN

PRO

ASP

SER

GLY

ASP

34

THR

GLY

ILE

LEU

LYS

ASP

TRP

GLN

35

THR

VAL

ASP

THR

VAL

LYS

ASP

GLY

TYR

LEU

36

ALA

PRO

ILE

LYS

SER

ILE

PHE

ASP

PRO

37

VAL

Samples:

E1_Y245G_sample: E1 Y245G, [U-13C; U-15N], 150 mM; Na phosphate 25 mM

E1_sample_conditions: ionic strength: 25 mM; pH: 7.2; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	E1_Y245G_sample	isotropic	E1_sample_conditions
3D CBCA(CO)NH	E1_Y245G_sample	isotropic	E1_sample_conditions
3D HNCO	E1_Y245G_sample	isotropic	E1_sample_conditions
3D HNCA	E1_Y245G_sample	isotropic	E1_sample_conditions
3D HNCACB	E1_Y245G_sample	isotropic	E1_sample_conditions
3D HN(CO)CA	E1_Y245G_sample	isotropic	E1_sample_conditions
3D HCACO	E1_Y245G_sample	isotropic	E1_sample_conditions

Software:

NMRFx_Processor_and_NMRViewJ, Bruce Johnson - peak picking, processing

MARS, Markus Zweckstetter - chemical shift assignment

PINE, Arash Bahrami - chemical shift assignment

NMR spectrometers:

Bruker Avance 800 MHz

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