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BMRB: 19881

2MN7

transport protein m

Authors

Zhang, Y., Hu, Y., Jin, C.

Assembly

transport protein m

Entity

1. transport protein m (polymer, Thiol state: not present), 97 monomers, 10728.96 Da Detail

MGGISIWQLL IIAVIVVLLF GTKKLGSIGS DLGASIKGFK KAMSDDEPKQ DKTSQDADFT AKTIADKQAD TNQEQAKTED AKRHDKEQVL EHHHHHH

Formula weight

10728.96 Da

Source organism

Escherichia coli

Exptl. method

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 95.9 %, Completeness: 88.2 %, Completeness (bb): 91.7 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	88.2 % (988 of 1120)	90.0 % (524 of 582)	86.4 % (374 of 433)	85.7 % (90 of 105)
Backbone	91.7 % (532 of 580)	93.5 % (187 of 200)	90.8 % (258 of 284)	90.6 % (87 of 96)
Sidechain	85.7 % (540 of 630)	88.2 % (337 of 382)	83.7 % (200 of 239)	33.3 % (3 of 9)
Aromatic	25.7 % (18 of 70)	42.9 % (15 of 35)	5.9 % (2 of 34)	100.0 % (1 of 1)
Methyl	99.1 % (105 of 106)	100.0 % (53 of 53)	98.1 % (52 of 53)

1. entity

MGGISIWQLL IIAVIVVLLF GTKKLGSIGS DLGASIKGFK KAMSDDEPKQ DKTSQDADFT AKTIADKQAD TNQEQAKTED AKRHDKEQVL EHHHHHH

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 308 K, pH 7

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-99% 13C; U-99% 15N]		1 mM
2	sodium phosphate	natural abundance		50 mM
3	DPC	natural abundance		200 mM
4	H2O	natural abundance		90 %
5	D2O	natural abundance		10 %

LACS Plot; CA

Referencing offset: -0.16 ppm, Outliers: 1 Detail

LACS Plot; CB

Referencing offset: -0.16 ppm, Outliers: 1 Detail

LACS Plot; HA

Referencing offset: 0.06 ppm, Outliers: 4 Detail

LACS Plot; CO

Referencing offset: -0.06 ppm, Outliers: 3 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 2MN7, Strand ID: A Detail

Release date

2015-04-12

Citation

Structural basis for TatA oligomerization: an NMR study of Escherichia coli TatA dimeric structure
Zhang, Y., Hu, Y., Li, H., Jin, C.
PLoS One (2014), 9, e103157-e103157, PubMed 25090434 , DOI 10.1371/journal.pone.0103157 , Abstract

Related entities 1. transport protein m, : 1 : 1 : 2 : 38 entities Detail

Interaction partners 1. transport protein m, : 4 interactors Detail

More details for 4 interactors identified by 2 citations

Experiments performed 7 experiments Detail

1 3D 1H-13C NOESY

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 308 K, pH 7

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-99% 13C; U-99% 15N]		1 mM
2	sodium phosphate	natural abundance		50 mM
3	DPC	natural abundance		200 mM
4	H2O	natural abundance		90 %
5	D2O	natural abundance		10 %

2 2D 1H-15N HSQC

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 308 K, pH 7

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-99% 13C; U-99% 15N]		1 mM
2	sodium phosphate	natural abundance		50 mM
3	DPC	natural abundance		200 mM
4	H2O	natural abundance		90 %
5	D2O	natural abundance		10 %

3 2D 1H-13C HSQC

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 308 K, pH 7

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-99% 13C; U-99% 15N]		1 mM
2	sodium phosphate	natural abundance		50 mM
3	DPC	natural abundance		200 mM
4	H2O	natural abundance		90 %
5	D2O	natural abundance		10 %

4 3D 1H-15N NOESY

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 308 K, pH 7

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-99% 13C; U-99% 15N]		1 mM
2	sodium phosphate	natural abundance		50 mM
3	DPC	natural abundance		200 mM
4	H2O	natural abundance		90 %
5	D2O	natural abundance		10 %

5 3D 1H-13C NOESY aliphatic

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 308 K, pH 7

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-99% 13C; U-99% 15N]		1 mM
2	sodium phosphate	natural abundance		50 mM
3	DPC	natural abundance		200 mM
4	H2O	natural abundance		90 %
5	D2O	natural abundance		10 %

6 3D HNCO

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 308 K, pH 7

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-99% 13C; U-99% 15N]		1 mM
2	sodium phosphate	natural abundance		50 mM
3	DPC	natural abundance		200 mM
4	H2O	natural abundance		90 %
5	D2O	natural abundance		10 %

7 3D HNCA

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 308 K, pH 7

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-99% 13C; U-99% 15N]		1 mM
2	sodium phosphate	natural abundance		50 mM
3	DPC	natural abundance		200 mM
4	H2O	natural abundance		90 %
5	D2O	natural abundance		10 %

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_19881_2mn7.nef
Input source #2: Coordindates	2mn7.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-------
MGGISIWQLLIIAVIVVLLFGTKKLGSIGSDLGASIKGFKKAMSDDEPKQDKTSQDADFTAKTIADKQADTNQEQAKTEDAKRHDKEQVLEHHHHHH
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MGGISIWQLLIIAVIVVLLFGTKKLGSIGSDLGASIKGFKKAMSDDEPKQDKTSQDADFTAKTIADKQADTNQEQAKTEDAKRHDKEQVLEHHHHHH

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	97	0	0	100.0

Content subtype: combined_19881_2mn7.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	996		93.8 (chain: A, length: 97)
1	Distance restraints	CNS/XPLOR_distance_constraints_3	OK	4488 (1)	noe	49.5 (chain: A, length: 97)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_2	OK	65 (65)	.	38.1 (chain: A, length: 97)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 97, Sequence coverage: 93.8%
- Total number of assignments
  - ¹H chemical shifts: 536
  - ¹³C chemical shifts: 370
  - ¹⁵N chemical shifts: 90
- 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: CNS/XPLOR_distance_constraints_3
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 97, Sequence coverage: 49.5%
- Total number of restraints: 4273
- Weight of restraints: 1.0 (4273)
- Potential type of restraints: square-well-parabolic (4273)
- Range of distance target values: 1.95, 5.15 (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: CNS/XPLOR_dihedral_2
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 97, Sequence coverage: 38.1%
- Total number of restraints: 65
- Total number of restraints per polymer type: 65
- Weight of restraints: 1.0 (65)
- Potential type of restraints: square-well-parabolic (65)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue

Keywords protein