BMRBj - BMREntryMaster

Found 1 Document (0.508 seconds)

BMRB: 16551

2KPB

Specific motifs of the V-ATPase a2-subunit isoform interact with catalytic and regulatory domains of ARNO

Authors

Merkulova, M., Bakulina, A., Thaker, Y.R., Gr ber, G., Marshansky, V.

Assembly

ARNO-p

Entity

1. ARNO-p (polymer, Thiol state: not available), 26 monomers, 3156.588 Da Detail

VSVDPFYEML AARKKRIXVK KKQEQP

Formula weight

3156.588 Da

Source organism

Mus musculus

Exptl. method

solution NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 92.3 %, Completeness: 82.5 %, Completeness (bb): 91.7 % Detail

Polymer type: polypeptide(L)

	Total	¹H
All	82.5 % (146 of 177)	82.5 % (146 of 177)
Backbone	91.7 % (44 of 48)	91.7 % (44 of 48)
Sidechain	79.1 % (102 of 129)	79.1 % (102 of 129)
Aromatic	55.6 % (5 of 9)	55.6 % (5 of 9)
Methyl	83.3 % (10 of 12)	83.3 % (10 of 12)

1. ARNO-p(375-400)

VSVDPFYEML AARKKRIXVK KKQEQP

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Temperature 298 K

#	Name	Isotope labeling	Concentration
1	ARNO-p(375-400)	natural abundance	1.0 ~ 2.0 mM
2	H20	natural abundance	90 %
3	D20	natural abundance	10 %

Release date

2010-02-17

Citation

Specific motifs of the V-ATPase a2-subunit isoform interact with catalytic and regulatory domains of ARNO
Merkulova, M., Bakulina, A., Thaker, Y., Gruber, G., Marshansky, V.
Biochim. Biophys. Acta (2010), 1797, 1398-1409, PubMed 20153292 , DOI 10.1016/j.bbabio.2010.02.009 , Abstract

Entries sharing articles BMRB: 1 entries Detail

BMRB: 16550 released on 2010-02-17
Title Specific motifs of the V-ATPase a2-subunit isoform interact with catalytic and regulatory domains of ARNO

Related entities 1. ARNO-p, : 1 : 9 : 20 entities Detail

Interaction partners 1. ARNO-p, : 1 interactors Detail

More details for 1 interactors identified by 1 citations

Experiments performed 2 experiments Detail

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_16551_2kpb.nef
Input source #2: Coordindates	2kpb.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------
VSVDPFYEMLAARKKRISVKKKQEQP
||||||||||||||||||||||||||
VSVDPFYEMLAARKKRISVKKKQEQP

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	26	0	0	100.0

Content subtype: combined_16551_2kpb.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	152		96.2 (chain: A, length: 26)
1	Distance restraints	DYANA/DIANA_distance_constraints_4	Warning	408 (1)	noe	96.2 (chain: A, length: 26)
1	Dihedral angle restraints	DYANA/DIANA_dihedral_2	OK	47 (47)	.	100.0 (chain: A, length: 26)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 26, Sequence coverage: 96.2%
- Total number of assignments
  - ¹H chemical shifts: 152
- 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)
13	ARG	HH11	7.173
16	ARG	HH11	7.289

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	181	150	82.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	50	46	92.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	131	104	79.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	13	10	76.9

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

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_4
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 26, Sequence coverage: 96.2%
- Total number of restraints: 408
- Weight of restraints: 1.0 (408)
- Potential type of restraints: upper-bound-parabolic (408)
- Range of distance target values: 2.55, 5.5 (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: DYANA/DIANA_dihedral_2
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 26, Sequence coverage: 100.0%
- Total number of restraints: 47
- Total number of restraints per polymer type: 47
- Weight of restraints: 1.0 (47)
- Potential type of restraints: square-well-parabolic (47)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords ARNO PB domain

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Found 1 Document (0.508 seconds)

BMRB: 16551

Sample

Entries sharing articles BMRB: 1 entries Detail

Related entities 1. ARNO-p, : 1 : 9 : 20 entities Detail

Interaction partners 1. ARNO-p, : 1 interactors Detail

Experiments performed 2 experiments Detail

Instrument

Sample

Instrument

Sample

NMR combined restraints 4 contents Detail