BMRB Entry 5885

Click here to enlarge.

PDB ID: 1pzq
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5885
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

CHEMICAL SHIFTS OF A FUSED DOCKING DOMAIN FROM THE ERYTHROMYCIN POLYKETIDE SYNTHASE (DEBS), A MODEL FOR THE INTERACTION BETWEEN DEBS 2 AND DEBS 3

Deposition date:

2003-07-29

Original release date:

2003-10-06

Authors:

Broadhurst, Richard; Nietlispach, Daniel; Wheatcroft, Michael; Leadlay, Peter; Weissman, Kira

Citation:

Citation: Broadhurst, Richard; Nietlispach, Daniel; Wheatcroft, Michael; Leadlay, Peter; Weissman, Kira. "The Structure of Docking Domains in Modular Polyketide Synthases" Chem. Biol. 10, 723-731 (2003).
PubMed: 12954331

Assembly members:

Assembly members:
6-deoxyerythronolide B synthase, polymer, 120 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Streptomyces erythraeus Taxonomy ID: 1836 Superkingdom: Eubacteria Kingdom: not available Genus/species: Saccharopolyspora erythraea

Experimental source:

Experimental source: Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
6-deoxyerythronolide B synthase: GSAASPAVDIGDRLDELEKA LEALSAEDGHDDVGQRLESL LRRWNSRRADAPSTSAISED ASDDELFSMLDQRFGGGEDL LMSGDNGMTEEKLRRYLKRT VTELDSVTARLREVEHRAGE

Data sets:

assigned_chemical_shifts
- shift_1

Data type	Count
1H chemical shifts	672
13C chemical shifts	391
15N chemical shifts	116

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	DOCK23 subunit 1	1
2	DOCK23 subunit 2	1

Entities:

Entity 1, DOCK23 subunit 1 120 residues - Formula weight is not available

1	GLY	SER	ALA	ALA	SER	PRO	ALA	VAL	ASP	ILE
2	GLY	ASP	ARG	LEU	ASP	GLU	LEU	GLU	LYS	ALA
3	LEU	GLU	ALA	LEU	SER	ALA	GLU	ASP	GLY	HIS
4	ASP	ASP	VAL	GLY	GLN	ARG	LEU	GLU	SER	LEU
5	LEU	ARG	ARG	TRP	ASN	SER	ARG	ARG	ALA	ASP
6	ALA	PRO	SER	THR	SER	ALA	ILE	SER	GLU	ASP
7	ALA	SER	ASP	ASP	GLU	LEU	PHE	SER	MET	LEU
8	ASP	GLN	ARG	PHE	GLY	GLY	GLY	GLU	ASP	LEU
9	LEU	MET	SER	GLY	ASP	ASN	GLY	MET	THR	GLU
10	GLU	LYS	LEU	ARG	ARG	TYR	LEU	LYS	ARG	THR
11	VAL	THR	GLU	LEU	ASP	SER	VAL	THR	ALA	ARG
12	LEU	ARG	GLU	VAL	GLU	HIS	ARG	ALA	GLY	GLU

Samples:

sample_1: 6-deoxyerythronolide B synthase, [U-100% 13C; U-100% 15N], 1.0 mM; NaH2PO4 100 mM

sample_2: 6-deoxyerythronolide B synthase, [100% 13C; 100% 15N], 0.5 mM; 6-deoxyerythronolide B synthase 0.5 mM

condition_set_1: pH: 6.5 na; temperature: 298 K; ionic strength: 0.10 mM

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	not available	not available	not available
2D 1H-13C HSQC	not available	not available	not available
3D HNCACB	not available	not available	not available
3D CBCA(CO)NH	not available	not available	not available
3D HBHA(CBCACO)NH	not available	not available	not available
3D HNCA	not available	not available	not available
3D HN(CO)CA	not available	not available	not available
3D HNCO	not available	not available	not available
3D 15N-SEPARATED NOESY	not available	not available	not available
3D 15N-SEPARATED TOCSY	not available	not available	not available
3D 13C-SEPARATED NOESY	not available	not available	not available
3D HCCH-TOCSY	not available	not available	not available
3D 13C/15N X-FILTERED 13C-SEPARATED NOESY	not available	not available	not available

Software:

AZARA v2.7 - DATA PROCESSING

ANSIG v3.3 - MANUAL ASSIGNMENT

NMR spectrometers:

BRUKER DRX 500 MHz
BRUKER DRX 800 MHz

PDB	1PZQ 1PZR
EMBL	CAA44448 CAM00064
GB	AAA26494 AAV39551 AAV51821 EQD87035
REF	WP_011873138 WP_037306412 YP_001102990
SP	Q03132
AlphaFold	Q03132 Q03132

1	GLY	SER	ALA	ALA	SER	PRO	ALA	VAL	ASP	ILE
2	GLY	ASP	ARG	LEU	ASP	GLU	LEU	GLU	LYS	ALA
3	LEU	GLU	ALA	LEU	SER	ALA	GLU	ASP	GLY	HIS
4	ASP	ASP	VAL	GLY	GLN	ARG	LEU	GLU	SER	LEU
5	LEU	ARG	ARG	TRP	ASN	SER	ARG	ARG	ALA	ASP
6	ALA	PRO	SER	THR	SER	ALA	ILE	SER	GLU	ASP
7	ALA	SER	ASP	ASP	GLU	LEU	PHE	SER	MET	LEU
8	ASP	GLN	ARG	PHE	GLY	GLY	GLY	GLU	ASP	LEU
9	LEU	MET	SER	GLY	ASP	ASN	GLY	MET	THR	GLU
10	GLU	LYS	LEU	ARG	ARG	TYR	LEU	LYS	ARG	THR
11	VAL	THR	GLU	LEU	ASP	SER	VAL	THR	ALA	ARG
12	LEU	ARG	GLU	VAL	GLU	HIS	ARG	ALA	GLY	GLU

1	GLY	SER	ALA	ALA	SER	PRO	ALA	VAL	ASP	ILE
2	GLY	ASP	ARG	LEU	ASP	GLU	LEU	GLU	LYS	ALA
3	LEU	GLU	ALA	LEU	SER	ALA	GLU	ASP	GLY	HIS
4	ASP	ASP	VAL	GLY	GLN	ARG	LEU	GLU	SER	LEU
5	LEU	ARG	ARG	TRP	ASN	SER	ARG	ARG	ALA	ASP
6	ALA	PRO	SER	THR	SER	ALA	ILE	SER	GLU	ASP
7	ALA	SER	ASP	ASP	GLU	LEU	PHE	SER	MET	LEU
8	ASP	GLN	ARG	PHE	GLY	GLY	GLY	GLU	ASP	LEU
9	LEU	MET	SER	GLY	ASP	ASN	GLY	MET	THR	GLU
10	GLU	LYS	LEU	ARG	ARG	TYR	LEU	LYS	ARG	THR
11	VAL	THR	GLU	LEU	ASP	SER	VAL	THR	ALA	ARG
12	LEU	ARG	GLU	VAL	GLU	HIS	ARG	ALA	GLY	GLU