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BMRB: 18871

2M1N

Solution structure of a chaperone in type III secretion system

Authors

Chen, L., Economou, A., Kalodimos, C.

Assembly

chaperone in type III secretion system

Entity

1. chaperone in type III secretion system (polymer, Thiol state: not present), 107 monomers, 12238.96 × 2 Da Detail

MSIVSQTRNK ELLLKKIDSL IEAIKKIIAE FDVVKESVNE LSEKAKTDPQ AAEKLNKLIE GYTYGEERKL YDSALSKIEK LIETLSPARS KSQSTMNQRN RNNRKIV

Total weight

24477.92 Da

Max. entity weight

12238.96 Da

Source organism

Escherichia coli

Exptl. method

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 73.8 %, Completeness: 27.0 %, Completeness (bb): 53.1 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	27.0 % (351 of 1301)	11.0 % (76 of 690)	42.8 % (212 of 495)	54.3 % (63 of 116)
Backbone	53.1 % (339 of 638)	31.3 % (67 of 214)	65.5 % (209 of 319)	60.0 % (63 of 105)
Sidechain	11.2 % (86 of 768)	1.9 % (9 of 476)	27.4 % (77 of 281)	0.0 % (0 of 11)
Aromatic	0.0 % (0 of 34)	0.0 % (0 of 17)	0.0 % (0 of 17)
Methyl	10.2 % (13 of 128)	6.3 % (4 of 64)	14.1 % (9 of 64)

1. CesAB

MSIVSQTRNK ELLLKKIDSL IEAIKKIIAE FDVVKESVNE LSEKAKTDPQ AAEKLNKLIE GYTYGEERKL YDSALSKIEK LIETLSPARS KSQSTMNQRN RNNRKIV

Show sample condition

Sample

Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 321 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	CesAB (Type III secretion system, chaperone for EspA and EspB)	[U-13C; U-15N; U-2H], 13CH3-Ala, Ile, Val, Leu		500 mM
2	KPi	natural abundance		50 mM
3	KCl	natural abundance		300 mM

Protein Blocks Logo

Calculated from 20 models in PDB: 2M1N, Strand ID: A, B Detail

Release date

2013-04-07

Citation

Substrate-activated conformational switch on chaperones encodes a targeting signal in type III secretion
Chen, L., Ai, X., Portaliou, A., Minetti, C., Remeta, D., Economou, A., Kalodimos, C.
Cell Rep. (2013), 3, 709-715, PubMed 23523349 , DOI 10.1016/j.celrep.2013.02.025 , Abstract

Related entities 1. chaperone in type III secretion system, : 1 : 2 : 3 entities Detail

Experiments performed 8 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker Avance - 700 MHz

Sample

State isotropic, Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 321 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	CesAB (Type III secretion system, chaperone for EspA and EspB)	[U-13C; U-15N; U-2H], 13CH3-Ala, Ile, Val, Leu		500 mM
2	KPi	natural abundance		50 mM
3	KCl	natural abundance		300 mM

2 2D 1H-13C HSQC aliphatic

Instrument

Bruker Avance - 700 MHz

Sample

State isotropic, Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 321 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	CesAB (Type III secretion system, chaperone for EspA and EspB)	[U-13C; U-15N; U-2H], 13CH3-Ala, Ile, Val, Leu		500 mM
2	KPi	natural abundance		50 mM
3	KCl	natural abundance		300 mM

3 3D HNCO

Instrument

Bruker Avance - 700 MHz

Sample

State isotropic, Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 321 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	CesAB (Type III secretion system, chaperone for EspA and EspB)	[U-13C; U-15N; U-2H], 13CH3-Ala, Ile, Val, Leu		500 mM
2	KPi	natural abundance		50 mM
3	KCl	natural abundance		300 mM

4 3D HNCA

Instrument

Bruker Avance - 700 MHz

Sample

State isotropic, Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 321 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	CesAB (Type III secretion system, chaperone for EspA and EspB)	[U-13C; U-15N; U-2H], 13CH3-Ala, Ile, Val, Leu		500 mM
2	KPi	natural abundance		50 mM
3	KCl	natural abundance		300 mM

5 3D HNCACB

Instrument

Bruker Avance - 700 MHz

Sample

State isotropic, Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 321 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	CesAB (Type III secretion system, chaperone for EspA and EspB)	[U-13C; U-15N; U-2H], 13CH3-Ala, Ile, Val, Leu		500 mM
2	KPi	natural abundance		50 mM
3	KCl	natural abundance		300 mM

6 3D CBCA(CO)NH

Instrument

Bruker Avance - 700 MHz

Sample

State isotropic, Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 321 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	CesAB (Type III secretion system, chaperone for EspA and EspB)	[U-13C; U-15N; U-2H], 13CH3-Ala, Ile, Val, Leu		500 mM
2	KPi	natural abundance		50 mM
3	KCl	natural abundance		300 mM

7 3D 1H-15N NOESY

Instrument

Bruker Avance - 700 MHz

Sample

State isotropic, Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 321 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	CesAB (Type III secretion system, chaperone for EspA and EspB)	[U-13C; U-15N; U-2H], 13CH3-Ala, Ile, Val, Leu		500 mM
2	KPi	natural abundance		50 mM
3	KCl	natural abundance		300 mM

8 3D HMQC-NOESY-HMQC

Instrument

Bruker Avance - 700 MHz

Sample

State isotropic, Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 321 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	CesAB (Type III secretion system, chaperone for EspA and EspB)	[U-13C; U-15N; U-2H], 13CH3-Ala, Ile, Val, Leu		500 mM
2	KPi	natural abundance		50 mM
3	KCl	natural abundance		300 mM

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_18871_2m1n.nef
Input source #2: Coordindates	2m1n.cif
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

Sequence alignments

Entity_assembly_ID (NMR): A vs Auth_asym_ID (model): A

--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100
MSIVSQTRNKELLLKKIDSLIEAIKKIIAEFDVVKESVNELSEKAKTDPQAAEKLNKLIEGYTYGEERKLYDSALSKIEKLIETLSPARSKSQSTMNQRN
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MSIVSQTRNKELLLKKIDSLIEAIKKIIAEFDVVKESVNELSEKAKTDPQAAEKLNKLIEGYTYGEERKLYDSALSKIEKLIETLSPARSKSQSTMNQRN

-------
RNNRKIV
|||||||
RNNRKIV

Entity_assembly_ID (NMR): B vs Auth_asym_ID (model): B

--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100
MSIVSQTRNKELLLKKIDSLIEAIKKIIAEFDVVKESVNELSEKAKTDPQAAEKLNKLIEGYTYGEERKLYDSALSKIEKLIETLSPARSKSQSTMNQRN
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MSIVSQTRNKELLLKKIDSLIEAIKKIIAEFDVVKESVNELSEKAKTDPQAAEKLNKLIEGYTYGEERKLYDSALSKIEKLIETLSPARSKSQSTMNQRN

-------
RNNRKIV
|||||||
RNNRKIV

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	107	0	0	100.0
B	B	107	0	0	100.0

Content subtype: combined_18871_2m1n.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	323		72.0 (chain: B, length: 107)
1	Distance restraints	CNS/XPLOR_distance_constraints_4	OK	165 (1)	noe	43.0 (chain: A, length: 107), 43.0 (chain: B, length: 107)
2	Distance restraints	CNS/XPLOR_distance_constraints_3	Warning	260 (1)	hbond	72.9 (chain: A, length: 107), 72.9 (chain: B, length: 107)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_2	OK	268 (268)	.	73.8 (chain: A, length: 107), 73.8 (chain: B, length: 107)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: B, Chain length: 107, Sequence coverage: 72.0%
- Total number of assignments
  - ¹³C chemical shifts: 203
  - ¹H chemical shifts: 60
  - ¹⁵N chemical shifts: 60
- Completeness of assignments
  - Entity_assemble_ID: B
- Peptide bond of PRO
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: B

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_4
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 107, Sequence coverage: 43.0%
  - Entity_assembly_ID: B, Chain length: 107, Sequence coverage: 43.0%
- Total number of restraints: 165
- Weight of restraints: 1.0 (165)
- Potential type of restraints: square-well-parabolic (165)
- Range of distance target values: 3.0, 4.5 (Å)
- Histogram of distance target values
- Distance restraints per residue
  - Chain_ID: A
  - Chain_ID: B
- Distance restraints on contact map
- Saveframe: CNS/XPLOR_distance_constraints_3
  - Status: Warning
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 107, Sequence coverage: 72.9%
    - Entity_assembly_ID: B, Chain length: 107, Sequence coverage: 72.9%
  - Total number of restraints: 260
  - Weight of restraints: 1.0 (260)
  - Potential type of restraints: square-well-parabolic (260)
  - Range of distance target values: 2.02, 3.52 (Å)
  - Histogram of distance target values
  - Distance restraints per residue
    - Chain_ID: A
    - Chain_ID: B
  - Distance restraints on contact map

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_2
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 107, Sequence coverage: 73.8%
  - Entity_assembly_ID: B, Chain length: 107, Sequence coverage: 73.8%
- Total number of restraints: 268
- Total number of restraints per polymer type: 268
- Weight of restraints: 1.0 (268)
- Potential type of restraints: square-well-parabolic (268)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A
  - Chain_ID: B

Keywords Chaperone, Helix bundle, Type III secretion