BMRBj - BMREntryMaster

	Total	¹³C	¹⁵N
All	7.9 % (48 of 604)	1.6 % (8 of 497)	37.4 % (40 of 107)
Backbone	11.2 % (44 of 393)	1.3 % (4 of 297)	41.7 % (40 of 96)
Sidechain	2.0 % (6 of 306)	2.0 % (6 of 295)	0.0 % (0 of 11)
Aromatic	0.0 % (0 of 78)	0.0 % (0 of 73)	0.0 % (0 of 5)
Methyl	4.5 % (3 of 66)	4.5 % (3 of 66)

1. entity

MPKSKVRKKN DFTVSAVSRT PMKVKVGPSS VWFVSLFIGL MLIGLIWLMV FQLAAIGSQA PTALNWMAQL GPWNYAIAFA FMITGLLLTM RWHLEHHHHH H

Show sample condition

Sample

Solvent system No organic solvent used, Pressure 1 atm, Temperature 273 K, pH 8.0, Details Glass slide supported POPC/POPG (4:1 mol/mol) phospholipid bilayer in liquid crystalline state; 15NH4Cl - 1.0/13C glucose - 2.0

#	Name	Isotope labeling	Concentration
1	CrgA	[U-100% 13C; U-100% 15N]	2.0 g/L
2	CrgA	[U-15N]-Leu	200 mg/L
3	CrgA	[U-15N]-Ala	200 mg/L
4	CrgA	[U-15N]-Val	200 mg/L
5	CrgA	[U-15N]-Ile	200 mg/L
6	CrgA	[U-15N]-Trp	200 mg/L
7	CrgA	[U-15N]-Tyr	200 mg/L
8	CrgA	[U-15N]-Met	200 mg/L
9	CrgA	[U-15N]-Phe	200 mg/L
10	CrgA	[U-15N]-Thr	200 mg/L
11	CrgA	[U-15N]-Gly	200 mg/L
12	CrgA	[U-15N]-Ser	200 mg/L
13	CrgA	[U-15N]-Arg	200 mg/L
14	CrgA	[U-15N]-Asn	200 mg/L

Chem. Shift Complete2

Sequence coverage: 21.8 %, Completeness: 11.8 %, Completeness (bb): 16.0 % Detail

Polymer type: polypeptide(L)

	Total	¹³C	¹⁵N
All	11.8 % (142 of 1208)	8.1 % (81 of 994)	28.5 % (61 of 214)
Backbone	16.0 % (126 of 786)	10.9 % (65 of 594)	31.8 % (61 of 192)
Sidechain	6.0 % (37 of 612)	6.3 % (37 of 590)	0.0 % (0 of 22)
Aromatic	0.0 % (0 of 156)	0.0 % (0 of 146)	0.0 % (0 of 10)
Methyl	7.6 % (10 of 132)	7.6 % (10 of 132)

1. entity

MPKSKVRKKN DFTVSAVSRT PMKVKVGPSS VWFVSLFIGL MLIGLIWLMV FQLAAIGSQA PTALNWMAQL GPWNYAIAFA FMITGLLLTM RWHLEHHHHH H

Show sample condition

Sample

#	Name	Isotope labeling	Concentration
1	CrgA	[U-100% 13C; U-100% 15N]	2.0 g/L
2	CrgA	[U-15N]-Leu	200 mg/L
3	CrgA	[U-15N]-Ala	200 mg/L
4	CrgA	[U-15N]-Val	200 mg/L
5	CrgA	[U-15N]-Ile	200 mg/L
6	CrgA	[U-15N]-Trp	200 mg/L
7	CrgA	[U-15N]-Tyr	200 mg/L
8	CrgA	[U-15N]-Met	200 mg/L
9	CrgA	[U-15N]-Phe	200 mg/L
10	CrgA	[U-15N]-Thr	200 mg/L
11	CrgA	[U-15N]-Gly	200 mg/L
12	CrgA	[U-15N]-Ser	200 mg/L
13	CrgA	[U-15N]-Arg	200 mg/L
14	CrgA	[U-15N]-Asn	200 mg/L

Protein Blocks Logo

Calculated from 1 models in PDB: 2MMU, Strand ID: A Detail

Release date

2014-12-14

Citation

Transmembrane structural characterization of CrgA, a cell division regulatory protein from M. tuberculosis in lipid bilayers
Das, N., Dai, J., Hung, I., Rajagopalan, M., Zhou, H., Cross, T.
Proc. Natl. Acad. Sci.

Related entities 1. M. tuberculosis CrgA membrane protein, : 1 : 2 : 15 entities Detail

Experiments performed 3 experiments Detail

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, RDC restraints	combined_19867_2mmu.nef
Input source #2: Coordindates	2mmu.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
MPKSKVRKKNDFTVSAVSRTPMKVKVGPSSVWFVSLFIGLMLIGLIWLMVFQLAAIGSQAPTALNWMAQLGPWNYAIAFAFMITGLLLTMRWHLEHHHHH
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MPKSKVRKKNDFTVSAVSRTPMKVKVGPSSVWFVSLFIGLMLIGLIWLMVFQLAAIGSQAPTALNWMAQLGPWNYAIAFAFMITGLLLTMRWHLEHHHHH

-
H
|
H

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	101	0	0	100.0

Content subtype: combined_19867_2mmu.nef

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	40		39.6 (chain: A, length: 101)
2	Assigned chemical shifts	assigned_chem_shift_list_2	Warning	86		19.8 (chain: A, length: 101)
1	RDC restraints	CNS/XPLOR_dipolar_coupling_2	OK	40 (40)	.	39.6 (chain: A, length: 101)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 101, Sequence coverage: 39.6%
- Total number of assignments
  - ¹⁵N chemical shifts: 40
- Completeness of assignments
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: A
Saveframe: assigned_chem_shift_list_2
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 101, Sequence coverage: 19.8%
- Total number of assignments
  - ¹³C chemical shifts: 66
  - ¹⁵N chemical shifts: 20
- Completeness of assignments
- 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

RDC restraints

Saveframe: CNS/XPLOR_dipolar_coupling_2
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 101, Sequence coverage: 39.6%
- Total number of restraints: 40
- Potential type of restraints: undefined (40)
- Range of observed RDC values: 100.0, -100.0 (Hz)
- RDC restraints per residue

Keywords CrgA structure, Hydrated lipid bilayer, Membrane protein, M. tuberculosis, Solid-state NMR

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Found 1 Document (0.533 seconds)

BMRB: 19867

Sample

Sample

Related entities 1. M. tuberculosis CrgA membrane protein, : 1 : 2 : 15 entities Detail

Experiments performed 3 experiments Detail

Instrument

Sample

NMR combined restraints 4 contents Detail