BMRB Entry 4352

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR4352

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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, 13C, and 15N Chemical Shift Assignments for the Inhibitor-Bound DNase Domain of Colicin E9.

Deposition date:

1999-06-14

Original release date:

2006-10-27

Authors:

Whittaker, Sara; Czisch, Michael; Wechselberger, Rainer; Kaptein, Robert; Hemmings, Andrew; James, Richard; Kleanthous, Colin; Moore, Geoffrey

Citation:

Citation: Whittaker, Sara; Czisch, Michael; Wechselberger, Rainer; Kaptein, Robert; Hemmings, Andrew; James, Richard; Kleanthous, Colin; Moore, Geoffrey. "Slow Conformational Dynamics of an Endonuclease Persist in its Complex with its Natural Protein Inhibitor" Protein Sci. 9, 713-720 (2000).

Assembly members:

Assembly members:
DNase domain of colicin E9, polymer, 134 residues, 15090 Da.
Immunity protein of colicin E9, polymer, 86 residues, 9582 Da.

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Eubacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Eschericia coli Vector: pRJ353

Entity Sequences (FASTA):

Entity Sequences (FASTA):
DNase domain of colicin E9: MESKRNKPGKATGKGKPVGD KWLDDAGKDSGAPIPDRIAD KLRDKEFKSFDDFRKAVWEE VSKDPELSKNLNPSNKSSVS KGYSPFTPKNQQVGGRKVYE LHHDKPISQGGEVYDMDNIR VTTPKRHIDIHRGK
Immunity protein of colicin E9: MELKHSISDYTEAEFLQLVT TICNADTSSEEELVKLVTHF EEMTEHPSGSDLIYYPKEGD DDSPSGIVNTVKQWRAANGK SGFKQG

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_for_major_conformer_of_E9_DNase
- assigned_chemical_shifts_for_minor_conformer_of_E9_DNase

Data type	Count
13C chemical shifts	420
15N chemical shifts	156
1H chemical shifts	472

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	E9 DNase	1
2	Im9	2

Entities:

Entity 1, E9 DNase 134 residues - 15090 Da.

1

MET

GLU

SER

LYS

ARG

ASN

LYS

PRO

GLY

LYS

2

ALA

THR

GLY

LYS

GLY

LYS

PRO

VAL

GLY

ASP

3

LYS

TRP

LEU

ASP

ALA

GLY

LYS

ASP

SER

4

GLY

ALA

PRO

ILE

PRO

ASP

ARG

ILE

ALA

ASP

5

LYS

LEU

ARG

ASP

LYS

GLU

PHE

LYS

SER

PHE

6

ASP

PHE

ARG

LYS

ALA

VAL

TRP

GLU

7

VAL

SER

LYS

ASP

PRO

GLU

LEU

SER

LYS

ASN

8

LEU

ASN

PRO

SER

ASN

LYS

SER

VAL

SER

9

LYS

GLY

TYR

SER

PRO

PHE

THR

PRO

LYS

ASN

10

GLN

VAL

GLY

ARG

LYS

VAL

TYR

GLU

11

LEU

HIS

ASP

LYS

PRO

ILE

SER

GLN

GLY

12

GLY

GLU

VAL

TYR

ASP

MET

ASP

ASN

ILE

ARG

13

VAL

THR

PRO

LYS

ARG

HIS

ILE

ASP

ILE

14

HIS

ARG

GLY

LYS

Entity 2, Im9 86 residues - 9582 Da.

1

MET

GLU

LEU

LYS

HIS

SER

ILE

SER

ASP

TYR

2

THR

GLU

ALA

GLU

PHE

LEU

GLN

LEU

VAL

THR

3

THR

ILE

CYS

ASN

ALA

ASP

THR

SER

GLU

4

GLU

LEU

VAL

LYS

LEU

VAL

THR

HIS

PHE

5

GLU

MET

THR

GLU

HIS

PRO

SER

GLY

SER

6

ASP

LEU

ILE

TYR

PRO

LYS

GLU

GLY

ASP

7

ASP

SER

PRO

SER

GLY

ILE

VAL

ASN

THR

8

VAL

LYS

GLN

TRP

ARG

ALA

ASN

GLY

LYS

9

SER

GLY

PHE

LYS

GLN

GLY

Samples:

sample_one: DNase domain of colicin E9, [U-99% 13C; U-99% 15N], 2.0 mM; Immunity protein of colicin E9 2.5 mM; Potassium_phosphate 50.0 mM; H20 90%; D20 10%; Sodium_azide 0.01%

sample_conditions_one: pH: 6.2; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
1H-15N HSQC	sample_one	not available	sample_conditions_one
1H-1H-15N NOESY-HSQC	sample_one	not available	sample_conditions_one
HNCO	sample_one	not available	sample_conditions_one
HNCA	sample_one	not available	sample_conditions_one
CBCA(CO)NH	sample_one	not available	sample_conditions_one
HBHA(CBCACO)NH	sample_one	not available	sample_conditions_one

Software:

FELIX v95.0 - Simultaneous analysis of triple resonance spectra. Very useful for analysing multiple data sets simultaneously.

NMRPipe - Data processing.

XEASY v1.2 - Defining strips for 3D NOESY to aid sequential assignment.

NMR spectrometers:

Bruker DMX 500 MHz
Bruker DMX 600 MHz
Varian UNITY 750 MHz

BMRB	4293
PDB	1BXI 1EMV 1FR2 1FSJ 1V13 1V14 1V15 2GYK 2GZE 2GZF 2GZG 2GZI 2GZJ 2K5X 2VLN 2VLO 2VLP 2VLQ 2WPT
EMBL	CAA31104 CAA33862
GB	ACM07430
PRF	1615299E
REF	WP_012644886 WP_044860894 YP_002533537
SP	P09883
AlphaFold	P09883