BMRB Entry 5404

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5404

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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 and Side Chain assignments of Peptide Deformylase complexed with Actinonin

Deposition date:

2002-06-26

Original release date:

2005-05-20

Authors:

Byerly, Doug; McElroy, Craig; Foster, Mark

Citation:

Citation: Byerly, D.; McElroy, C.; Foster, M.. "Mapping the surface of Escherichia coli peptide deformylase by NMR with organic solvents." Protein Sci. 11, 1850-1853 (2002).
PubMed: 12070337

Assembly members:

Assembly members:
Peptide Deformylase, polymer, 147 residues, 16684 Da.
ACTINONIN, non-polymer, 385.498 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Peptide Deformylase: SVLQVLHIPDERLRKVAKPV EEVNAEIQRIVDDMFETMYA EEGIGLAATQVDIHQRIIVI DVSENRDERLVLINPELLEK SGETGIEEGCLSIPEQRALV PRAEKVKIRALDRDGKPFEL EADGLLAICIQHEMDHLVGK LFMDYLS

Data sets:

assigned_chemical_shifts
- shift_set_1

Data type	Count
13C chemical shifts	618
15N chemical shifts	149
1H chemical shifts	1045

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PDF	1
2	Actinonin	2

Entities:

Entity 1, PDF 147 residues - 16684 Da.

1

SER

VAL

LEU

GLN

VAL

LEU

HIS

ILE

PRO

ASP

2

GLU

ARG

LEU

ARG

LYS

VAL

ALA

LYS

PRO

VAL

3

GLU

VAL

ASN

ALA

GLU

ILE

GLN

ARG

ILE

4

VAL

ASP

MET

PHE

GLU

THR

MET

TYR

ALA

5

GLU

GLY

ILE

GLY

LEU

ALA

THR

GLN

6

VAL

ASP

ILE

HIS

GLN

ARG

ILE

VAL

ILE

7

ASP

VAL

SER

GLU

ASN

ARG

ASP

GLU

ARG

LEU

8

VAL

LEU

ILE

ASN

PRO

GLU

LEU

GLU

LYS

9

SER

GLY

GLU

THR

GLY

ILE

GLU

GLY

CYS

10

LEU

SER

ILE

PRO

GLU

GLN

ARG

ALA

LEU

VAL

11

PRO

ARG

ALA

GLU

LYS

VAL

LYS

ILE

ARG

ALA

12

LEU

ASP

ARG

ASP

GLY

LYS

PRO

PHE

GLU

LEU

13

GLU

ALA

ASP

GLY

LEU

ALA

ILE

CYS

ILE

14

GLN

HIS

GLU

MET

ASP

HIS

LEU

VAL

GLY

LYS

15

LEU

PHE

MET

ASP

TYR

LEU

SER

Entity 2, Actinonin - C19 H35 N3 O5 - 385.498 Da.

1

BB2

Samples:

sample_1: Peptide Deformylase, [U-95% 13C; U-90% 15N], 0.5 – 1.2 mM; TRIS 20 mM; NaN3 0.02%

cond_1: pH: 7.2; temperature: 310 K

Experiments:

Name	Sample	Sample state	Sample conditions
15N TOCSY-HSQC	sample_1	not available	cond_1
15N NOESY-HSQC	sample_1	not available	cond_1
HNHA	sample_1	not available	cond_1
HBHA(CBCACO)NH	sample_1	not available	cond_1
CBCA(CO)NH	sample_1	not available	cond_1
HNCACB	sample_1	not available	cond_1
13C NOESY-HSQC	sample_1	not available	cond_1
HCCH-TOCSY	sample_1	not available	cond_1
HCCH-COSY	sample_1	not available	cond_1
HNCO	sample_1	not available	cond_1
HACAHB-COSY	sample_1	not available	cond_1
C(CO)NH-TOCSY	sample_1	not available	cond_1

Software:

NMRPipe -

NMRView -

NMR spectrometers:

Bruker DMX 600 MHz
Bruker DRX 600 MHz
Bruker DRX 800 MHz

BMRB	4089 6142
PDB	1BS4 1BS5 1BS6 1BS7 1BS8 1BSJ 1BSK 1BSZ 1DEF 1DFF 1G27 1G2A 1ICJ 1LRU 1XEM 1XEN 1XEO 2AI8 2DEF 2KMN 2W3T 2W3U 3K6L 4AL2 4AL3 4AZ4
DBJ	BAB37575 BAE78005 BAG79085 BAH66202 BAI27558
EMBL	CAA11508 CAA45206 CAA54367 CAA54826 CAD09179
GB	AAA58084 AAC76312 AAF76758 AAG58408 AAL22269
PIR	AB1010
REF	NP_289848 NP_312179 NP_417745 NP_458493 NP_462310
SP	A1AGH8 A8A591 A8AQI1 A9MN80 A9N8B1
AlphaFold	A1AGH8 A8A591 A8AQI1 A9MN80 A9N8B1