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BMRB: 17720

2LEP

Solution Structure of N-terminal Cytosolic Domain of Rhomboid Intramembrane Protease from Escherichia Coli

Authors

Sherratt, A.R., Ghasriani, H., Goto, N.K.

Assembly

NGlpG

Entity

1. NGlpG (polymer, Thiol state: unknown), 63 monomers, 7136.961 Da Detail

MLMITSFANP RVAQAFVDYM ATQGVILTIQ QHNQSDVWLA DESQAERVRA ELARFLENPA DLD

Formula weight

7136.961 Da

Source organism

Escherichia coli

Exptl. method

Refine. method

molecular dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 86.1 %, Completeness (bb): 94.4 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	86.1 % (626 of 727)	82.1 % (307 of 374)	89.0 % (251 of 282)	95.8 % (68 of 71)
Backbone	94.4 % (353 of 374)	94.4 % (118 of 125)	93.6 % (176 of 188)	96.7 % (59 of 61)
Sidechain	80.0 % (332 of 415)	75.9 % (189 of 249)	85.9 % (134 of 156)	90.0 % (9 of 10)
Aromatic	51.9 % (28 of 54)	51.9 % (14 of 27)	50.0 % (13 of 26)	100.0 % (1 of 1)
Methyl	95.0 % (76 of 80)	95.0 % (38 of 40)	95.0 % (38 of 40)

1. NGlpG

MLMITSFANP RVAQAFVDYM ATQGVILTIQ QHNQSDVWLA DESQAERVRA ELARFLENPA DLD

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293.15 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	Nglpg	[U-100% 13C; U-100% 15N]		1.0 (±0.05) mM
2	H2O	natural abundance		90 %
3	D2O	natural abundance		10 %

Sample #2

Solvent system 100% D2O, Pressure 1 atm, Temperature 293.15 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
4	Nglpg	[U-100% 13C; U-100% 15N]		1.0 (±0.05) mM
5	D2O	natural abundance		100 %

LACS Plot; CA

Referencing offset: -0.1 ppm, Outliers: 2 Detail

LACS Plot; CB

Referencing offset: -0.1 ppm, Outliers: 2 Detail

LACS Plot; HA

Referencing offset: -0.1 ppm, Outliers: 1 Detail

LACS Plot; CO

Referencing offset: 0.22 ppm, Outliers: 1 Detail

Protein Blocks Logo

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

Release date

2012-09-23

Citation

Activity-based protein profiling of the Escherichia coli GlpG rhomboid protein delineates the catalytic core
Sherratt, A.R., Blais, D.R., Ghasriani, H., Pezacki, J., Goto, N.K.
Biochemistry (2012), 51, 7794-7803, PubMed 22963263 , DOI 10.1021/bi301087c , Abstract

Related entities 1. NGlpG, : 1 : 1 : 11 : 23 entities Detail

Interaction partners 1. NGlpG, : 3 interactors Detail

More details for 3 interactors identified by 3 citations

Experiments performed 10 experiments Detail

1 2D 1H-15N HSQC

Instrument

Varian INOVA - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293.15 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	Nglpg	[U-100% 13C; U-100% 15N]		1.0 (±0.05) mM
2	H2O	natural abundance		90 %
3	D2O	natural abundance		10 %

2 3D HNCO

Instrument

Varian INOVA - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293.15 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	Nglpg	[U-100% 13C; U-100% 15N]		1.0 (±0.05) mM
2	H2O	natural abundance		90 %
3	D2O	natural abundance		10 %

3 3D HNCA

Instrument

Varian INOVA - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293.15 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	Nglpg	[U-100% 13C; U-100% 15N]		1.0 (±0.05) mM
2	H2O	natural abundance		90 %
3	D2O	natural abundance		10 %

4 3D HNCACB

Instrument

Varian INOVA - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293.15 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	Nglpg	[U-100% 13C; U-100% 15N]		1.0 (±0.05) mM
2	H2O	natural abundance		90 %
3	D2O	natural abundance		10 %

5 3D HBHA(CO)NH

Instrument

Varian INOVA - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293.15 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	Nglpg	[U-100% 13C; U-100% 15N]		1.0 (±0.05) mM
2	H2O	natural abundance		90 %
3	D2O	natural abundance		10 %

6 3D HN(CO)CA

Instrument

Varian INOVA - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293.15 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	Nglpg	[U-100% 13C; U-100% 15N]		1.0 (±0.05) mM
2	H2O	natural abundance		90 %
3	D2O	natural abundance		10 %

7 3D HCCH-TOCSY

Instrument

Varian INOVA - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293.15 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	Nglpg	[U-100% 13C; U-100% 15N]		1.0 (±0.05) mM
2	H2O	natural abundance		90 %
3	D2O	natural abundance		10 %

8 3D 1H-15N NOESY

Instrument

Varian INOVA - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293.15 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	Nglpg	[U-100% 13C; U-100% 15N]		1.0 (±0.05) mM
2	H2O	natural abundance		90 %
3	D2O	natural abundance		10 %

9 3D 1H-13C NOESY aliphatic

Instrument

Varian INOVA - 500 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 293.15 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
4	Nglpg	[U-100% 13C; U-100% 15N]		1.0 (±0.05) mM
5	D2O	natural abundance		100 %

10 3D 1H-13C NOESY aromatic

Instrument

Varian INOVA - 500 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 293.15 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
4	Nglpg	[U-100% 13C; U-100% 15N]		1.0 (±0.05) mM
5	D2O	natural abundance		100 %

NMR combined restraints 3 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Dihedral angle restraints	combined_17720_2lep.nef
Input source #2: Coordindates	2lep.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---------
MLMITSFANPRVAQAFVDYMATQGVILTIQQHNQSDVWLADESQAERVRAELARFLENPADLDHHHHHH
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MLMITSFANPRVAQAFVDYMATQGVILTIQQHNQSDVWLADESQAERVRAELARFLENPADLDHHHHHH

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	69	0	0	100.0

Content subtype: combined_17720_2lep.nef

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	631		91.3 (chain: A, length: 69)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	84 (84)	.	78.3 (chain: A, length: 69)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 69, Sequence coverage: 91.3%
- Total number of assignments
  - ¹H chemical shifts: 312
  - ¹³C chemical shifts: 251
  - ¹⁵N chemical shifts: 68
- Completeness of assignments
  - Entity_assemble_ID: A
- 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: A

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 69, Sequence coverage: 78.3%
- Total number of restraints: 84
- Total number of restraints per polymer type: 84
- Weight of restraints: 1.0 (84)
- Potential type of restraints: square-well-parabolic (84)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords Biomolecular, Cell Membrane, Cytosol, Domain Swapping, Escherichia Coli, Membrane Protein, Micelles, NMR, Nuclear Magnetic Resonance, Protein, Protein Conformation, Protein Structure, Secondary, Serine Protease, Tertiary