BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	34.0 % (200 of 588)	17.8 % (54 of 304)	42.9 % (99 of 231)	88.7 % (47 of 53)
Backbone	63.9 % (189 of 296)	48.5 % (49 of 101)	63.3 % (93 of 147)	97.9 % (47 of 48)
Sidechain	16.5 % (56 of 339)	3.0 % (6 of 203)	38.2 % (50 of 131)	0.0 % (0 of 5)
Aromatic	0.0 % (0 of 70)	0.0 % (0 of 35)	0.0 % (0 of 33)	0.0 % (0 of 2)
Methyl	25.0 % (13 of 52)	15.4 % (4 of 26)	34.6 % (9 of 26)

1. Palmitoyltransferase 1

MAEAHQAVGF RPSLTSDGAE VELSAPVLQE IYLSGLRSWK RHLSRFWNDF

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_1	[U-100% 13C; U-100% 15N; U-80% 2H]	0.5 mM
2	dodecyltrimethylammonium chloride	natural abundance	150 mM
3	MES	natural abundance	25 mM
4	H2O	natural abundance	95 %
5	D2O	natural abundance	5 %

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	na	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	na	indirect	0.1013291
³¹P	DSS	methyl protons	na	indirect	0.4048086

Referencing offset: 0.08 ppm, Outliers: 1 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	na	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	na	indirect	0.1013291
³¹P	DSS	methyl protons	na	indirect	0.4048086

Referencing offset: 0.08 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 2M76, Strand ID: A Detail

Release date

2013-09-09

Citation

Structural characterization of the regulatory domain of brain carnitine palmitoyltransferase 1
Samanta, S., Situ, A.J., Ulmer, T.S.
Biopolymers (2014), 101, 398-405, PubMed 24037959 , DOI 10.1002/bip.22396 , Abstract

Related entities 1. Regulatory Domain of Human Brain Carnitine Palmitoyltransferase 1, : 1 : 2 : 33 entities Detail

Experiments performed 4 experiments Detail

NMR combined restraints 3 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Dihedral angle restraints	combined_19174_2m76.nef
Input source #2: Coordindates	2m76.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
MAEAHQAVGFRPSLTSDGAEVELSAPVLQEIYLSGLRSWKRHLSRFWNDF
||||||||||||||||||||||||||||||||||||||||||||||||||
MAEAHQAVGFRPSLTSDGAEVELSAPVLQEIYLSGLRSWKRHLSRFWNDF

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	50	0	0	100.0

Content subtype: combined_19174_2m76.nef

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	OK	185		94.0 (chain: A, length: 50)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	52 (52)	.	58.0 (chain: A, length: 50)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 50, Sequence coverage: 94.0%
- Total number of assignments
  - ¹H chemical shifts: 47
  - ¹³C chemical shifts: 91
  - ¹⁵N chemical shifts: 47
- Completeness of assignments
  - Entity_assemble_ID: A
- 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	304	47	15.5
¹³C chemical shifts	231	91	39.4
¹⁵N chemical shifts	57	47	82.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	101	47	46.5
¹³C chemical shifts	100	47	47.0
¹⁵N chemical shifts	48	47	97.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	203	0	0.0
¹³C chemical shifts	131	44	33.6
¹⁵N chemical shifts	9	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	27	0	0.0
¹³C chemical shifts	27	5	18.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	35	0	0.0
¹³C chemical shifts	33	0	0.0
¹⁵N chemical shifts	2	0	0.0

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 50, Sequence coverage: 58.0%
- Total number of restraints: 52
- Total number of restraints per polymer type: 52
- Weight of restraints: 1.0 (52)
- Potential type of restraints: square-well-parabolic (52)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords acyl transfer, carnitine, malonyl-coenzyme A

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BMRB: 19174

Sample

Chemical shift reference

Chemical shift reference

Related entities 1. Regulatory Domain of Human Brain Carnitine Palmitoyltransferase 1, : 1 : 2 : 33 entities Detail

Experiments performed 4 experiments Detail

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Instrument

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Sample

NMR combined restraints 3 contents Detail