BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	67.8 % (799 of 1178)	72.3 % (444 of 614)	57.2 % (266 of 465)	89.9 % (89 of 99)
Backbone	78.0 % (465 of 596)	91.5 % (184 of 201)	64.1 % (193 of 301)	93.6 % (88 of 94)
Sidechain	62.6 % (425 of 679)	63.0 % (260 of 413)	62.8 % (164 of 261)	20.0 % (1 of 5)
Aromatic	9.1 % (8 of 88)	9.1 % (4 of 44)	9.1 % (4 of 44)
Methyl	78.4 % (80 of 102)	84.3 % (43 of 51)	72.5 % (37 of 51)

1. DCL4 DUF283

ISGGSSISMM YKYCSRLPHD EFFQPKPEFQ FKPVDEFGGT ICRITLPANA PISEIESSLL PSTEAAKKDA CLKAVHELHN LGVLNDFLLP DSKDEIEDEL SD

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.3

#	Name	Isotope labeling	Concentration
1	protein	[U-100% 13C; U-100% 15N]	1 mM
2	H2O	natural abundance	90 %
3	D2O	natural abundance	10 %

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl carbon	na	direct	1.0
¹H	DSS	methyl protons	na	direct	1.0
¹⁵N	DSS	nitrogen	na	direct	1.0

Referencing offset: -0.24 ppm, Outliers: 1 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl carbon	na	direct	1.0
¹H	DSS	methyl protons	na	direct	1.0
¹⁵N	DSS	nitrogen	na	direct	1.0

Referencing offset: -0.24 ppm, Outliers: 1 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl carbon	na	direct	1.0
¹H	DSS	methyl protons	na	direct	1.0
¹⁵N	DSS	nitrogen	na	direct	1.0

Referencing offset: 0.11 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 10 models in PDB: 2KOU, Strand ID: A Detail

Release date

2010-02-07

Citation

Structure of the Arabidopsis thaliana DCL4 DUF283 domain reveals a noncanonical double-stranded RNA-binding fold for protein-protein interaction
Qin, H., Chen, F., Huan, X., Machida, S., Song, J., Yuan, Y.
RNA (2010), 16, 474-481, PubMed 20106953 , DOI 10.1261/rna.1965310 , Abstract

Entries sharing articles Swiss-Prot: 1 entries Detail

Swiss-Prot: P84634 released on 2005-09-13
Title DCL4_ARATH Entity Dicer-like protein 4

Related entities 1. DCL4 DUF283, : 1 : 2 : 73 entities Detail

Interaction partners 1. DCL4 DUF283, : 2 interactors Detail

More details for 2 interactors identified by 2 citations

Experiments performed 4 experiments Detail

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_16534_2kou.nef
Input source #2: Coordindates	2kou.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
ISGGSSISMMYKYCSRLPHDEFFQPKPEFQFKPVDEFGGTICRITLPANAPISEIESSLLPSTEAAKKDACLKAVHELHNLGVLNDFLLPDSKDEIEDEL
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
ISGGSSISMMYKYCSRLPHDEFFQPKPEFQFKPVDEFGGTICRITLPANAPISEIESSLLPSTEAAKKDACLKAVHELHNLGVLNDFLLPDSKDEIEDEL

--
SD
||
SD

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	102	0	0	100.0

Content subtype: combined_16534_2kou.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	767		91.2 (chain: A, length: 102)
1	Distance restraints	DYANA/DIANA_distance_constraints_2	Warning	1427 (1)	noe	91.2 (chain: A, length: 102)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	155 (155)	.	95.1 (chain: A, length: 102)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 102, Sequence coverage: 91.2%
- Total number of assignments
  - ¹H chemical shifts: 436
  - ¹³C chemical shifts: 246
  - ¹⁵N chemical shifts: 85
- Completeness of assignments
  - Entity_assemble_ID: A
- Redox state of CYS
- Peptide bond of PRO
- 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

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
45	THR	HG1	0.329
53	SER	HG	1.573

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	614	426	69.4
¹³C chemical shifts	465	246	52.9
¹⁵N chemical shifts	101	85	84.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	201	179	89.1
¹³C chemical shifts	204	93	45.6
¹⁵N chemical shifts	94	84	89.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	413	247	59.8
¹³C chemical shifts	261	153	58.6
¹⁵N chemical shifts	7	1	14.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	53	43	81.1
¹³C chemical shifts	53	36	67.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	44	0	0.0
¹³C chemical shifts	44	0	0.0

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_2
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 102, Sequence coverage: 91.2%
- Total number of restraints: 1427
- Weight of restraints: 1.0 (1427)
- Potential type of restraints: upper-bound-parabolic (1427)
- Range of distance target values: 2.8, 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: CNS/XPLOR_dihedral_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 102, Sequence coverage: 95.1%
- Total number of restraints: 155
- Total number of restraints per polymer type: 155
- Weight of restraints: 1.0 (155)
- Potential type of restraints: square-well-parabolic (155)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords DICER-LIKE protein

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Found 1 Document (0.823 seconds)

BMRB: 16534

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Entries sharing articles Swiss-Prot: 1 entries Detail

Related entities 1. DCL4 DUF283, : 1 : 2 : 73 entities Detail

Interaction partners 1. DCL4 DUF283, : 2 interactors Detail

Experiments performed 4 experiments Detail

Instrument

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Instrument

Sample

Instrument

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Sample

NMR combined restraints 4 contents Detail