BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	61.0 % (307 of 503)	59.2 % (154 of 260)	57.1 % (113 of 198)	88.9 % (40 of 45)
Backbone	80.0 % (200 of 250)	95.3 % (81 of 85)	63.7 % (79 of 124)	97.6 % (40 of 41)
Sidechain	49.5 % (145 of 293)	41.7 % (73 of 175)	63.2 % (72 of 114)	0.0 % (0 of 4)
Aromatic	3.8 % (2 of 52)	7.7 % (2 of 26)	0.0 % (0 of 25)	0.0 % (0 of 1)
Methyl	66.0 % (33 of 50)	52.0 % (13 of 25)	80.0 % (20 of 25)

1. carnitine palmitoyltransferase 1A

MAEAHQAVAF QFTVTPDGID LRLSHEALRQ IYLSGLHSWK KK

Show sample condition

Sample

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 308.2 K, pH 5.6

#	Name	Isotope labeling	Concentration
1	palmitoyltransferase_1A	[U-100% 13C; U-100% 15N; U-80% 2H]	0.5 mM
2	palmitoyltransferase_1A	[U-99% 13C; U-99% 15N]	0.5 mM
3	H2O	natural abundance	95 %
4	D2O	natural abundance	5 %
5	MES+NaOH	natural abundance	25 mM
6	dodecytrimethylammonium chloride	natural abundance	150 mM

LACS Plot; CA

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹⁵C	water	protons	4.684 ppm	internal	indirect	0.101329
¹H	water	protons	4.684 ppm	internal	direct	1.0
¹³N	water	protons	4.684 ppm	internal	indirect	0.2514495

Referencing offset: 0.06 ppm, Outliers: 1 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹⁵C	water	protons	4.684 ppm	internal	indirect	0.101329
¹H	water	protons	4.684 ppm	internal	direct	1.0
¹³N	water	protons	4.684 ppm	internal	indirect	0.2514495

Referencing offset: 0.06 ppm, Outliers: 1 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹⁵C	water	protons	4.684 ppm	internal	indirect	0.101329
¹H	water	protons	4.684 ppm	internal	direct	1.0
¹³N	water	protons	4.684 ppm	internal	indirect	0.2514495

Referencing offset: -0.16 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 2LE3, Strand ID: A Detail

Release date

2011-10-25

Citation

An environment-dependent structural switch underlies the regulation of carnitine palmitoyltransferase 1A
Rao, J.N., Warren, G.Z.L., Estolt-Povedano, S., Zammit, V.A., Ulmer, T.S.
J. Biol. Chem. (2011), 286, 42545-42554, PubMed 21990363 , DOI 10.1074/jbc.M111.306951 , Abstract

Related entities 1. carnitine palmitoyltransferase 1A, : 1 : 2 : 38 entities Detail

Interaction partners 1. carnitine palmitoyltransferase 1A, : 38 interactors Detail

More details for 38 interactors identified by 13 citations

Experiments performed 4 experiments Detail

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_17690_2le3.nef
Input source #2: Coordindates	2le3.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--
MAEAHQAVAFQFTVTPDGIDLRLSHEALRQIYLSGLHSWKKK
||||||||||||||||||||||||||||||||||||||||||
MAEAHQAVAFQFTVTPDGIDLRLSHEALRQIYLSGLHSWKKK

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	42	0	0	100.0

Content subtype: combined_17690_2le3.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	304		95.2 (chain: A, length: 42)
1	Distance restraints	CNS/XPLOR_distance_constraints_3	Warning	306 (1)	noe	76.2 (chain: A, length: 42)
2	Distance restraints	CNS/XPLOR_distance_constraints_4	Warning	1 (1)	hbond	4.8 (chain: A, length: 42)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_5	OK	75 (75)	.	85.7 (chain: A, length: 42)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 42, Sequence coverage: 95.2%
- Total number of assignments
  - ¹H chemical shifts: 152
  - ¹³C chemical shifts: 112
  - ¹⁵N chemical shifts: 40
- Completeness of assignments
  - Entity_assemble_ID: A
- 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

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	260	152	58.5
¹³C chemical shifts	198	112	56.6
¹⁵N chemical shifts	47	40	85.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	85	80	94.1
¹³C chemical shifts	84	40	47.6
¹⁵N chemical shifts	41	40	97.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	175	72	41.1
¹³C chemical shifts	114	72	63.2
¹⁵N chemical shifts	6	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	26	13	50.0
¹³C chemical shifts	26	20	76.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	26	2	7.7
¹³C chemical shifts	25	0	0.0
¹⁵N chemical shifts	1	0	0.0

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_3
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 42, Sequence coverage: 76.2%
- Total number of restraints: 293
- Weight of restraints: 1.0 (293)
- Potential type of restraints: square-well-parabolic (293)
- Range of distance target values: 2.15, 3.9 (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: CNS/XPLOR_distance_constraints_4
  - Status: Warning
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 42, Sequence coverage: 4.8%
  - Total number of restraints: 1
  - Weight of restraints: 1.0 (1)
  - Potential type of restraints: square-well-parabolic (1)
  - Range of distance target values: 2.0, 2.0 (Å)
  - Distance restraints per residue
    - Chain_ID: A
  - Distance restraints on contact map

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_5
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 42, Sequence coverage: 85.7%
- Total number of restraints: 75
- Total number of restraints per polymer type: 75
- Weight of restraints: 1.0 (75)
- Potential type of restraints: square-well-parabolic (75)
- Plot of Phi-Psi angle restraints
- Plot of Chi1-Chi2 angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords amphiphilic structure, membrane protein, membrane-protein interaction

Search

Query history

Resources

Search for primary databases

Search for subsidiary databases

Display

Hits per page

Statistics

Query Changes will take effect after "OK" button is selected.

Maximum hits

Default conjunction operator

Omni-box

Search filter

Sequence search (BLAST)

E-value

Query sequence coverage

Miscellaneous

The number of previewed publications

Completeness of assigned chemical shift

Sequence chart about top aligned regions

Sequence chart about interacting regions

Hit context with highlight

Link destinations for BMRB, PDB and EMDB

Found 1 Document (2.428 seconds)

BMRB: 17690

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. carnitine palmitoyltransferase 1A, : 1 : 2 : 38 entities Detail

Interaction partners 1. carnitine palmitoyltransferase 1A, : 38 interactors Detail

Experiments performed 4 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 5 contents Detail