BMRB Entry 34447

Name: Bam_5920cDD 5919nDD docking domains
Published: 2020-08-06

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PDB ID: 6tdm
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34447
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:

Bam_5920cDD 5919nDD docking domains

Deposition date:

2019-11-08

Original release date:

2020-08-06

Authors:

Risser, F.; Chagot, B.

Citation:

Citation: Risser, F.; Collin, S.; Dos Santos-Morais, R.; Gruez, A.; Chagot, B.; Weissman, K.. "Towards improved understanding of intersubunit interactions in modular polyketide biosynthesis: Docking in the enacyloxin IIa polyketide synthase" J. Struct. Biol. 212, 107581-107581 (2020).
PubMed: 32717326

Assembly members:

Assembly members:
entity_1, polymer, 64 residues, 6734.480 Da.

Natural source:

Natural source: Common Name: Burkholderia ambifaria Taxonomy ID: 339670 Superkingdom: Bacteria Kingdom: not available Genus/species: Burkholderia ambifaria

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pBG102

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPGSYDAALPIDELSALLRQ EMGDDGGGSGGGSMQDIQQL LAKSLTEIKRLKAANQALEQ ARRE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	504
15N chemical shifts	144
1H chemical shifts	868

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1
2	unit_2	1

Entities:

Entity 1, unit_1 64 residues - 6734.480 Da.

1

GLY

PRO

GLY

SER

TYR

ASP

ALA

LEU

PRO

2

ILE

ASP

GLU

LEU

SER

ALA

LEU

ARG

GLN

3

GLU

MET

GLY

ASP

GLY

SER

GLY

4

GLY

SER

MET

GLN

ASP

ILE

GLN

LEU

5

LEU

ALA

LYS

SER

LEU

THR

GLU

ILE

LYS

ARG

6

LEU

LYS

ALA

ASN

GLN

ALA

LEU

GLU

GLN

7

ALA

ARG

GLU

Samples:

sample_1: protein, [U-100% 13C; U-100% 15N], 1 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1

Software:

Amber, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

Sparky, Goddard - chemical shift assignment

TopSpin, Bruker Biospin - collection

NMR spectrometers:

Bruker DRX 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks