BMRB Entry 6373

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6373

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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, 13C and 15N backbone resonance assignments of LexA catalytic domain with the L89P/Q92W/D150H/E152A/K156A mutations

Deposition date:

2004-10-29

Original release date:

2005-06-03

Authors:

Okon, Mark; Pfuetzner, Richard; Vockovic, Marija; Little, John; Strynadka, Natalie; McIntosh, Lawrence

Citation:

Citation: Okon, Mark; Pfuetzner, Richard; Vockovic, Marija; Little, John; Strynadka, Natalie; McIntosh, Lawrence. "Letter to the Editor: Backbone chemical shift assignments of the LexA catalytic domain in its active conformation." J. Biomol. NMR 31, 371-372 (2005).
PubMed: 15929009

Assembly members:

Assembly members:
catalytic domain of LexA L89P/Q92W/D150H/E152A/K156A mutant, polymer, 135 residues, 14850 Da.

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
catalytic domain of LexA L89P/Q92W/D150H/E152A/K156A mutant: LLQEEEEGLPLVGRVAAGEP LPAQWHIEGHYQVDPSLFKP NADFLLRVSGMSMKDIGIMD GDLLAVHKTQDVRNGQVVVA RIHDAVTVARLKKQGNKVEL LPENSEFKPIVVDLRQQSFT IEGLAVGVIRNGDWL

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts

Data type	Count
13C chemical shifts	377
15N chemical shifts	125
1H chemical shifts	125

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	catalytic domain of LexA L89P/Q92W/D150H/E152A/K156A mutant, chain 1	1
2	catalytic domain of LexA L89P/Q92W/D150H/E152A/K156A mutant, chain 2	1

Entities:

Entity 1, catalytic domain of LexA L89P/Q92W/D150H/E152A/K156A mutant, chain 1 135 residues - 14850 Da.

1

LEU

GLN

GLU

GLY

LEU

PRO

2

LEU

VAL

GLY

ARG

VAL

ALA

GLY

GLU

PRO

3

LEU

PRO

ALA

GLN

TRP

HIS

ILE

GLU

GLY

HIS

4

TYR

GLN

VAL

ASP

PRO

SER

LEU

PHE

LYS

PRO

5

ASN

ALA

ASP

PHE

LEU

ARG

VAL

SER

GLY

6

MET

SER

MET

LYS

ASP

ILE

GLY

ILE

MET

ASP

7

GLY

ASP

LEU

ALA

VAL

HIS

LYS

THR

GLN

8

ASP

VAL

ARG

ASN

GLY

GLN

VAL

ALA

9

ARG

ILE

HIS

ASP

ALA

VAL

THR

VAL

ALA

ARG

10

LEU

LYS

GLN

GLY

ASN

LYS

VAL

GLU

LEU

11

LEU

PRO

GLU

ASN

SER

GLU

PHE

LYS

PRO

ILE

12

VAL

ASP

LEU

ARG

GLN

SER

PHE

THR

13

ILE

GLU

GLY

LEU

ALA

VAL

GLY

VAL

ILE

ARG

14

ASN

GLY

ASP

TRP

LEU

Samples:

sample_1: catalytic domain of LexA L89P/Q92W/D150H/E152A/K156A mutant, [U-13C; U-15N], 1 mM; Phosphate buffer 20 mM

sample_conditions: pH: 7.0; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
1H15N HSQC TROSY	not available	not available	not available
HNCA TROSY	not available	not available	not available
HNCACB	not available	not available	not available
(HB)CBCA(CO)NH	not available	not available	not available
HNCO TROSY	not available	not available	not available
15N-edited NOESY	not available	not available	not available

Software:

VNMR v6.1C, VARIAN -

NMR spectrometers:

VARIAN UNITY-INOVA 600 MHz

PDB	1JHE 3JSO 3JSP 3K3R
GB	KFH80209 KFH96244