BMRB Entry 15442

Name: Multienzyme Docking in Hybrid Megasynthetases
Published: 2008-06-26

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PDB ID: 2jug
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15442
MolProbity Validation Chart

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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:

Multienzyme Docking in Hybrid Megasynthetases

Deposition date:

2007-08-24

Original release date:

2008-06-26

Authors:

Richter, Carsten; Nietlispach, Daniel; Broadhurst, Richard; Weissman, Kira

Citation:

Citation: Richter, Carsten; Nietlispach, Daniel; Broadhurst, Richard; Weissman, Kira. "Multienzyme docking in hybrid megasynthetases" Nat. Chem. Biol. 4, 75-81 (2008).
PubMed: 18066054

Assembly members:

Assembly members:
TubCdd, polymer, 78 residues, 8132.495 Da.

Natural source:

Natural source: Common Name: Angiococcus disciformis Taxonomy ID: 38 Superkingdom: Bacteria Kingdom: not available Genus/species: Angiococcus disciformis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEX-6P-1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TubCdd: GPLGSSAGALLAHAASLGVR LWVEGERLRFQAPPGVMTPE LQSRLGGARHELIALLRQLQ PSSQGGSLLAPVARNGRL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	308
15N chemical shifts	75
1H chemical shifts	515

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	TubCdd A	1
2	TubCdd B	1

Entities:

Entity 1, TubCdd A 78 residues - 8132.495 Da.

The first four residues represent the remnant of the Precission protease cleavage sequence that separated the polypeptide from its N-terminal glutathoine-S-transferase fusion partner.

1

GLY

PRO

LEU

GLY

SER

ALA

GLY

ALA

LEU

2

LEU

ALA

HIS

ALA

SER

LEU

GLY

VAL

ARG

3

LEU

TRP

VAL

GLU

GLY

GLU

ARG

LEU

ARG

PHE

4

GLN

ALA

PRO

GLY

VAL

MET

THR

PRO

GLU

5

LEU

GLN

SER

ARG

LEU

GLY

ALA

ARG

HIS

6

GLU

LEU

ILE

ALA

LEU

ARG

GLN

LEU

GLN

7

PRO

SER

GLN

GLY

SER

LEU

ALA

8

PRO

VAL

ALA

ARG

ASN

GLY

ARG

LEU

Name	Sample	Sample state	Sample conditions
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 13C-separated 12C-selected NOESY	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1

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SPARKY: Backbone or all simulated peaks

BMRB Entry 15442

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: