BMRBj - BMREntryMaster

Found 1 Document (0.658 seconds)

BMRB: 19437

2MCE

Membrane induced structure of the mammalian tachykinin neuropeptide gamma

Authors

Chandrashekar, I., Ganjiwale, A., Cowsik, S.

Assembly

mammalian tachykinin neuropeptide gamma

Entity

1. NPgamma (polymer, Thiol state: not present), 21 monomers, 2321.573 Da Detail

DAGHGQISHK RHKTDSFVGL M

2. 5-ACETYLAMINO-4-AMINO-6-(PHENETHYL-PROPYL-CARBAMOYL)-5,6-DIHYDRO-4H-PYRAN-2-CARBOXYLIC ACID (non-polymer), 389.445 Da

Total weight

2711.018 Da

Max. entity weight

2321.573 Da

Exptl. method

solution NMR

Refine. method

torsion angle dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 73.0 %, Completeness (bb): 91.1 % Detail

Polymer type: polypeptide(L)

	Total	¹H
All	73.0 % (89 of 122)	73.0 % (89 of 122)
Backbone	91.1 % (41 of 45)	91.1 % (41 of 45)
Sidechain	62.3 % (48 of 77)	62.3 % (48 of 77)
Aromatic	27.3 % (3 of 11)	27.3 % (3 of 11)
Methyl	75.0 % (6 of 8)	75.0 % (6 of 8)

1. NPgamma

DAGHGQISHK RHKTDSFVGL M

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 305 K, pH 2.4, Details The NMR samples were prepared by dissolving 4 mg of NPg in approximately 0.5ml of water (90% H2O, 10% D2O, pH 2.4). 50 mg of perdeuterated DPC was added yielding in solution a lipid concentration of 250 mM.

#	Name	Isotope labeling	Concentration
1	entity	natural abundance	4 mg
2	DPC	[U-100% 2H]	250 mM
3	H2O	natural abundance	90 %
4	D2O	natural abundance	10 %

Protein Blocks Logo

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

Release date

2013-08-25

Citation

Membrane-induced structure of the mammalian tachykinin neuropeptide gamma
Chandrashekar, I., Ganjiwale, A., Cowsik, S.
J. Struct. Biol. (2004), 148, 315-325, PubMed 15522780 , DOI 10.1016/j.jsb.2004.08.008 , Abstract

Related entities 1. NPgamma, : 1 : 1 : 8 : 5 entities Detail

Interaction partners 1. NPgamma, : 7 interactors Detail

More details for 7 interactors identified by 3 citations

Experiments performed 3 experiments Detail

NMR combined restraints 3 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Dihedral angle restraints	combined_19437_2mce.nef
Input source #2: Coordindates	2mce.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-
DAGHGQISHKRHKTDSFVGLM
|||||||||||||||||||||
DAGHGQISHKRHKTDSFVGLM

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	21	0	0	100.0

Content subtype: combined_19437_2mce.nef

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	95		100.0 (chain: A, length: 21)
1	Dihedral angle restraints	DYANA/DIANA_dihedral_4	OK	20 (20)	.	100.0 (chain: A, length: 21)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 21, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 95
- 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

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
10	LYS	HZ1	7.59
10	LYS	HZ2	7.59
10	LYS	HZ3	7.59
12	HIS	HD1	7.3
13	LYS	HZ1	7.62
13	LYS	HZ2	7.62
13	LYS	HZ3	7.62

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	122	88	72.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	45	41	91.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	77	47	61.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	9	5	55.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	11	3	27.3

Dihedral angle restraints

Saveframe: DYANA/DIANA_dihedral_4
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 21, Sequence coverage: 100.0%
- Total number of restraints: 20
- Total number of restraints per polymer type: 20
- Weight of restraints: 1.0 (20)
- Potential type of restraints: square-well-parabolic (20)
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords Bioactive peptide, NK-2 selective agonists, Neuropeptide gamma, Peptide membrane interaction, Tachykinin

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Found 1 Document (0.658 seconds)

BMRB: 19437

Sample

Related entities 1. NPgamma, : 1 : 1 : 8 : 5 entities Detail

Interaction partners 1. NPgamma, : 7 interactors Detail

Experiments performed 3 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 3 contents Detail