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BMRB: 34446

6TDD

Bam_5924 docking domain

Authors

Risser, F., Chagot, B.

Assembly

Beta-ketoacyl synthase

Entity

1. Beta-ketoacyl synthase (polymer, Thiol state: not present), 45 monomers, 5019.670 × 2 Da Detail

GPGSMNKPTS SDGWKDDYLS RLSRLSKNQL MALALKLKQQ QLEQG

Total weight

10039.34 Da

Max. entity weight

5019.67 Da

Source organism

Burkholderia ambifaria AMMD

Exptl. method

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 95.7 %, Completeness (bb): 96.2 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	95.7 % (514 of 537)	96.2 % (275 of 286)	95.5 % (189 of 198)	94.3 % (50 of 53)
Backbone	96.2 % (256 of 266)	96.7 % (89 of 92)	95.4 % (125 of 131)	97.7 % (42 of 43)
Sidechain	95.5 % (298 of 312)	95.9 % (186 of 194)	96.3 % (104 of 108)	80.0 % (8 of 10)
Aromatic	90.0 % (18 of 20)	100.0 % (10 of 10)	77.8 % (7 of 9)	100.0 % (1 of 1)
Methyl	100.0 % (38 of 38)	100.0 % (19 of 19)	100.0 % (19 of 19)

1. entity 1

GPGSMNKPTS SDGWKDDYLS RLSRLSKNQL MALALKLKQQ QLEQG

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5, Details 100 mM U- sodium phosphate, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	entity_1			0.0 ~ 0.0 mM
2	sodium phosphate	natural abundance		100 mM

Release date

2019-12-02

Citation

Towards improved understanding of intersubunit interactions in modular polyketide biosynthesis: Docking in the enacyloxin IIa polyketide synthase
Risser, F., Collin, S., Dos Santos-Morais, R., Gruez, A., Chagot, B., Weissman, K.J.
J. Struct. Biol. (2020), 212, 107581-107581, PubMed 32717326 , DOI 10.1016/j.jsb.2020.107581 , Abstract

Related entities 1. Beta-ketoacyl synthase, : 1 : 1 : 18 entities Detail

Experiments performed 12 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker DRX - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5, Details 100 mM U- sodium phosphate, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	entity_1			0.0 ~ 0.0 mM
2	sodium phosphate	natural abundance		100 mM

2 2D 1H-13C HSQC aliphatic

Instrument

Bruker DRX - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5, Details 100 mM U- sodium phosphate, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	entity_1			0.0 ~ 0.0 mM
2	sodium phosphate	natural abundance		100 mM

3 2D 1H-13C HSQC aromatic

Instrument

Bruker DRX - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5, Details 100 mM U- sodium phosphate, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	entity_1			0.0 ~ 0.0 mM
2	sodium phosphate	natural abundance		100 mM

4 3D CBCA(CO)NH

Instrument

Bruker DRX - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5, Details 100 mM U- sodium phosphate, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	entity_1			0.0 ~ 0.0 mM
2	sodium phosphate	natural abundance		100 mM

5 3D HNCO

Instrument

Bruker DRX - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5, Details 100 mM U- sodium phosphate, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	entity_1			0.0 ~ 0.0 mM
2	sodium phosphate	natural abundance		100 mM

6 3D 1H-13C NOESY aromatic

Instrument

Bruker DRX - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5, Details 100 mM U- sodium phosphate, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	entity_1			0.0 ~ 0.0 mM
2	sodium phosphate	natural abundance		100 mM

7 3D 1H-13C NOESY aliphatic

Instrument

Bruker DRX - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5, Details 100 mM U- sodium phosphate, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	entity_1			0.0 ~ 0.0 mM
2	sodium phosphate	natural abundance		100 mM

8 3D 1H-15N NOESY

Instrument

Bruker DRX - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5, Details 100 mM U- sodium phosphate, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	entity_1			0.0 ~ 0.0 mM
2	sodium phosphate	natural abundance		100 mM

9 3D C(CO)NH

Instrument

Bruker DRX - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5, Details 100 mM U- sodium phosphate, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	entity_1			0.0 ~ 0.0 mM
2	sodium phosphate	natural abundance		100 mM

10 3D HCCH-TOCSY

Instrument

Bruker DRX - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5, Details 100 mM U- sodium phosphate, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	entity_1			0.0 ~ 0.0 mM
2	sodium phosphate	natural abundance		100 mM

11 3D H(CCO)NH

Instrument

Bruker DRX - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5, Details 100 mM U- sodium phosphate, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	entity_1			0.0 ~ 0.0 mM
2	sodium phosphate	natural abundance		100 mM

12 3D HNCACB

Instrument

Bruker DRX - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5, Details 100 mM U- sodium phosphate, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	entity_1			0.0 ~ 0.0 mM
2	sodium phosphate	natural abundance		100 mM

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr34446_3.str
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	None
Whether the assembly has a other bond	None
Whether the assembly contains a cyclic polymer	None
Overall data processing status	Warning

Disulfide bonds

None

Other bonds (neither disulfide, covalent nor hydrogen bonds, e.g. Zinc–sulphur bond)

None

Non-standard residues

None

Content subtype: bmr34446_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	1136		100.0 (chain: 1, length: 45)
1	Chemical shift references	chem_shift_reference_1	OK	3		No information

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 45, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 650
  - ¹³C chemical shifts: 386
  - ¹⁵N chemical shifts: 100
- Completeness of assignments
  - Entity_assemble_ID: 1
- Peptide bond of PRO
- Rotameric state of ILE , LEU, and VAL
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1

Keywords PROTEIN BINDING, docking domain, polyketide synthase