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BMRB: 19618

2MI2

1H, 15N and 13C resonance assignment of a transport protein

Authors

Zhang, Y., Wang, L., Hu, Y., Jin, C.

Assembly

transport protein

Entity

1. transport protein (polymer, Thiol state: not present), 109 monomers, 12325.12 Da Detail

MFDIGFSELL LVFIIGLVVL GPQRLPVAVK TVAGWIRALR SLATTVQNEL TQELKLQEFQ DSLKKVEKAS LTNLTPELKA SMDELRQAAE SMKRSYVAND PLEHHHHHH

Formula weight

12325.12 Da

Source organism

Escherichia coli

Exptl. method

Refine. method

torsion angle dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 98.2 %, Completeness: 90.3 %, Completeness (bb): 93.8 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	90.3 % (1173 of 1299)	88.9 % (598 of 673)	90.8 % (464 of 511)	96.5 % (111 of 115)
Backbone	93.8 % (606 of 646)	94.0 % (205 of 218)	92.9 % (300 of 323)	96.2 % (101 of 105)
Sidechain	87.9 % (666 of 758)	86.4 % (393 of 455)	89.8 % (263 of 293)	100.0 % (10 of 10)
Aromatic	69.0 % (58 of 84)	69.0 % (29 of 42)	68.3 % (28 of 41)	100.0 % (1 of 1)
Methyl	91.3 % (137 of 150)	92.0 % (69 of 75)	90.7 % (68 of 75)

1. protein

MFDIGFSELL LVFIIGLVVL GPQRLPVAVK TVAGWIRALR SLATTVQNEL TQELKLQEFQ DSLKKVEKAS LTNLTPELKA SMDELRQAAE SMKRSYVAND PLEHHHHHH

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 313 K, pH 5.5

#	Name	Isotope labeling	Type	Concentration
1	transport protein	[U-100% 13C; U-100% 15N]		1 mM
2	sodium acetate	natural abundance		20 mM
3	DPC	natural abundance		40 mM
4	H2O	natural abundance		90 %
5	D2O	natural abundance		10 %

LACS Plot; CA

Referencing offset: -0.41 ppm, Outliers: 3 Detail

LACS Plot; CB

Referencing offset: -0.41 ppm, Outliers: 3 Detail

LACS Plot; HA

Referencing offset: -0.02 ppm, Outliers: 2 Detail

LACS Plot; CO

Referencing offset: -0.15 ppm, Outliers: 2 Detail

Protein Blocks Logo

Calculated from 15 models in PDB: 2MI2, Strand ID: A Detail

Release date

2014-04-27

Citation

Solution structure of the TatB component of the twin-arginine translocation system
Zhang, Y., Wang, L., Hu, Y., Jin, C.
Biochim. Biophys. Acta (2014), 1838, 1881-1888, PubMed 24699374 , DOI 10.1016/j.bbamem.2014.03.015 , Abstract

Related entities 1. transport protein, : 1 : 77 entities Detail

Interaction partners 1. transport protein, : 6 interactors Detail

More details for 6 interactors identified by 2 citations

Experiments performed 13 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 313 K, pH 5.5

#	Name	Isotope labeling	Type	Concentration
1	transport protein	[U-100% 13C; U-100% 15N]		1 mM
2	sodium acetate	natural abundance		20 mM
3	DPC	natural abundance		40 mM
4	H2O	natural abundance		90 %
5	D2O	natural abundance		10 %

2 2D 1H-13C HSQC

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 313 K, pH 5.5

#	Name	Isotope labeling	Type	Concentration
1	transport protein	[U-100% 13C; U-100% 15N]		1 mM
2	sodium acetate	natural abundance		20 mM
3	DPC	natural abundance		40 mM
4	H2O	natural abundance		90 %
5	D2O	natural abundance		10 %

3 3D CBCA(CO)NH

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 313 K, pH 5.5

#	Name	Isotope labeling	Type	Concentration
1	transport protein	[U-100% 13C; U-100% 15N]		1 mM
2	sodium acetate	natural abundance		20 mM
3	DPC	natural abundance		40 mM
4	H2O	natural abundance		90 %
5	D2O	natural abundance		10 %

4 3D HNCO

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 313 K, pH 5.5

#	Name	Isotope labeling	Type	Concentration
1	transport protein	[U-100% 13C; U-100% 15N]		1 mM
2	sodium acetate	natural abundance		20 mM
3	DPC	natural abundance		40 mM
4	H2O	natural abundance		90 %
5	D2O	natural abundance		10 %

5 3D HNCA

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 313 K, pH 5.5

#	Name	Isotope labeling	Type	Concentration
1	transport protein	[U-100% 13C; U-100% 15N]		1 mM
2	sodium acetate	natural abundance		20 mM
3	DPC	natural abundance		40 mM
4	H2O	natural abundance		90 %
5	D2O	natural abundance		10 %

6 3D HNCACB

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 313 K, pH 5.5

#	Name	Isotope labeling	Type	Concentration
1	transport protein	[U-100% 13C; U-100% 15N]		1 mM
2	sodium acetate	natural abundance		20 mM
3	DPC	natural abundance		40 mM
4	H2O	natural abundance		90 %
5	D2O	natural abundance		10 %

7 3D HBHA(CO)NH

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 313 K, pH 5.5

#	Name	Isotope labeling	Type	Concentration
1	transport protein	[U-100% 13C; U-100% 15N]		1 mM
2	sodium acetate	natural abundance		20 mM
3	DPC	natural abundance		40 mM
4	H2O	natural abundance		90 %
5	D2O	natural abundance		10 %

8 3D HN(CO)CA

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 313 K, pH 5.5

#	Name	Isotope labeling	Type	Concentration
1	transport protein	[U-100% 13C; U-100% 15N]		1 mM
2	sodium acetate	natural abundance		20 mM
3	DPC	natural abundance		40 mM
4	H2O	natural abundance		90 %
5	D2O	natural abundance		10 %

9 3D HCCH-TOCSY

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 313 K, pH 5.5

#	Name	Isotope labeling	Type	Concentration
1	transport protein	[U-100% 13C; U-100% 15N]		1 mM
2	sodium acetate	natural abundance		20 mM
3	DPC	natural abundance		40 mM
4	H2O	natural abundance		90 %
5	D2O	natural abundance		10 %

10 3D HCCH-COSY

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 313 K, pH 5.5

#	Name	Isotope labeling	Type	Concentration
1	transport protein	[U-100% 13C; U-100% 15N]		1 mM
2	sodium acetate	natural abundance		20 mM
3	DPC	natural abundance		40 mM
4	H2O	natural abundance		90 %
5	D2O	natural abundance		10 %

11 3D 1H-13C NOESY aromatic

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 313 K, pH 5.5

#	Name	Isotope labeling	Type	Concentration
1	transport protein	[U-100% 13C; U-100% 15N]		1 mM
2	sodium acetate	natural abundance		20 mM
3	DPC	natural abundance		40 mM
4	H2O	natural abundance		90 %
5	D2O	natural abundance		10 %

12 3D 1H-13C NOESY aliphatic

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 313 K, pH 5.5

#	Name	Isotope labeling	Type	Concentration
1	transport protein	[U-100% 13C; U-100% 15N]		1 mM
2	sodium acetate	natural abundance		20 mM
3	DPC	natural abundance		40 mM
4	H2O	natural abundance		90 %
5	D2O	natural abundance		10 %

13 3D 1H-15N NOESY

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 313 K, pH 5.5

#	Name	Isotope labeling	Type	Concentration
1	transport protein	[U-100% 13C; U-100% 15N]		1 mM
2	sodium acetate	natural abundance		20 mM
3	DPC	natural abundance		40 mM
4	H2O	natural abundance		90 %
5	D2O	natural abundance		10 %

NMR combined restraints 6 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_19618_2mi2.nef
Input source #2: Coordindates	2mi2.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
MFDIGFSELLLVFIIGLVVLGPQRLPVAVKTVAGWIRALRSLATTVQNELTQELKLQEFQDSLKKVEKASLTNLTPELKASMDELRQAAESMKRSYVAND
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MFDIGFSELLLVFIIGLVVLGPQRLPVAVKTVAGWIRALRSLATTVQNELTQELKLQEFQDSLKKVEKASLTNLTPELKASMDELRQAAESMKRSYVAND

---------
PLEHHHHHH
|||||||||
PLEHHHHHH

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	109	0	0	100.0

Content subtype: combined_19618_2mi2.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	1188		96.3 (chain: A, length: 109)
1	Distance restraints	DYANA/DIANA_distance_constraints_2	Warning	2774 (1)	noe	95.4 (chain: A, length: 109)
2	Distance restraints	DYANA/DIANA_distance_constraints_4	Warning	2378 (1)	noe	94.5 (chain: A, length: 109)
3	Distance restraints	DYANA/DIANA_distance_constraints_3	Warning	222 (1)	hbond	66.1 (chain: A, length: 109)
1	Dihedral angle restraints	DYANA/DIANA_dihedral_5	OK	139 (139)	.	71.6 (chain: A, length: 109)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 109, Sequence coverage: 96.3%
- Total number of assignments
  - ¹H chemical shifts: 603
  - ¹³C chemical shifts: 469
  - ¹⁵N chemical shifts: 116
- 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

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_2
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 109, Sequence coverage: 95.4%
- Total number of restraints: 2774
- Weight of restraints: 1.0 (2774)
- Potential type of restraints: upper-bound-parabolic (2774)
- Range of distance target values: 0.0, 6.53 (Å)
- Histogram of distance target values
- Histogram of discrepancy in distance target values
- Distance restraints per residue
  - Chain_ID: A
- Distance restraints on contact map
- Saveframe: DYANA/DIANA_distance_constraints_4
  - Status: Warning
  - Experiment type: noe
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 109, Sequence coverage: 94.5%
  - Total number of restraints: 2378
  - Weight of restraints: 1.0 (2378)
  - Potential type of restraints: upper-bound-parabolic (2378)
  - Range of distance target values: 0.0, 5.53 (Å)
  - Histogram of distance target values
  - Histogram of discrepancy in distance target values
  - Distance restraints per residue
    - Chain_ID: A
  - Distance restraints on contact map
  - Saveframe: DYANA/DIANA_distance_constraints_3
    - Status: Warning
    - Experiment type: hbond
    - Sequence coverage of experimental data
      - Entity_assembly_ID: A, Chain length: 109, Sequence coverage: 66.1%
    - Total number of restraints: 222
    - Weight of restraints: 1.0 (222)
    - Potential type of restraints: upper-bound-parabolic (222)
    - Range of distance target values: 1.8, 3.0 (Å)
    - Histogram of distance target values
    - Histogram of discrepancy in distance target values
    - Distance restraints per residue
      - Chain_ID: A
    - Distance restraints on contact map

Dihedral angle restraints

Saveframe: DYANA/DIANA_dihedral_5
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 109, Sequence coverage: 71.6%
- Total number of restraints: 139
- Total number of restraints per polymer type: 139
- Weight of restraints: 1.0 (139)
- Potential type of restraints: square-well-parabolic (139)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A