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Found 1 Document (2.826 seconds)

BMRB: 4110

8IZN

1H, 13C, 15N Resonance Assignment of the 20 KDa Double Stranded RNA Binding Domain of PKR

Authors

Nanduri, S., Carpick, B., Yang, Y.W., Williams, B.R.G., Qin, J.

Assembly

double stranded RNA binding domain of PKR

Entity

1. double stranded RNA binding domain of PKR (polymer), 179 monomers, 19677.16 Da Detail

GSHMEMAGDL SAGFFMEELN TRYQKQGVVL KYQELPNSGP PHDRRFTFQV IIDGREFPEG EGRSKKEAKN AAAKLAVEIL NKEKKAVSPL LLTTTNSSEG LSMGNYIGLI NRIAQKKRLT VNYEQCASGV HGPEGFHYKC KMGQKEYSIG TGSTKQEAKQ LAAKLAYLQI LSEETGSGC

Formula weight

19677.16 Da

Source organism

Homo sapiens

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 98.9 %, Completeness: 87.1 %, Completeness (bb): 83.7 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	87.1 % (1804 of 2072)	93.0 % (1012 of 1088)	77.3 % (613 of 793)	93.7 % (179 of 191)
Backbone	83.7 % (889 of 1062)	96.2 % (357 of 371)	70.3 % (364 of 518)	97.1 % (168 of 173)
Sidechain	91.8 % (1074 of 1170)	91.4 % (655 of 717)	93.8 % (408 of 435)	61.1 % (11 of 18)
Aromatic	79.5 % (105 of 132)	83.3 % (55 of 66)	75.8 % (50 of 66)
Methyl	98.2 % (167 of 170)	96.5 % (82 of 85)	100.0 % (85 of 85)

1. double stranded RNA binding domain of PKR

GSHMEMAGDL SAGFFMEELN TRYQKQGVVL KYQELPNSGP PHDRRFTFQV IIDGREFPEG EGRSKKEAKN AAAKLAVEIL NKEKKAVSPL LLTTTNSSEG LSMGNYIGLI NRIAQKKRLT VNYEQCASGV HGPEGFHYKC KMGQKEYSIG TGSTKQEAKQ LAAKLAYLQI LSEETGSGC

Show sample condition

Sample #1

Temperature 298 K, pH 6.5 (±0.05)

#	Name	Isotope labeling	Concentration
1	double stranded RNA binding domain of PKR	[U-15N]	.9 mM
2	NaCl		100 mM
3	sodium phosphate		20 mM
4	DTT		1 mM
5	H2O		93 %
6	D2O		7 %

Sample #2

Temperature 298 K, pH 6.5 (±0.05)

#	Name	Isotope labeling	Concentration
7	double stranded RNA binding domain of PKR	[U-15N;U-13C]	.9 mM
8	NaCl		100 mM
9	sodium phosphate		20 mM
10	DTT		1 mM
11	H2O		93 %
12	D2O		7 %

LACS Plot; CA

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type
¹³C	sodium acetate	methyl	25.85 ppm	null	null
¹H	H2O	proton	4.77 ppm	null	null
¹⁵N	ammonium chloride	ammonium	78.98 ppm	null	null

Referencing offset: -0.1 ppm, Outliers: 3 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type
¹³C	sodium acetate	methyl	25.85 ppm	null	null
¹H	H2O	proton	4.77 ppm	null	null
¹⁵N	ammonium chloride	ammonium	78.98 ppm	null	null

Referencing offset: -0.1 ppm, Outliers: 3 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type
¹³C	sodium acetate	methyl	25.85 ppm	null	null
¹H	H2O	proton	4.77 ppm	null	null
¹⁵N	ammonium chloride	ammonium	78.98 ppm	null	null

Referencing offset: -0.03 ppm, Outliers: 1 Detail

Release date

1998-10-13

Citation 1

1H, 13C, 15N resonance assignment of the 20 kDa double stranded RNA binding domain of PKR
Nanduri, S., Carpick, B., Yang, Y.W., Williams, B.R.G., Qin, J.
J. Biomol. NMR (1998), 12, 349-351, PubMed 9752004 , DOI:

Show more 1 citaion

Citation 2

NMRPipe: a multidimensional spectral processing system based on UNIX pipes
Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J., Bax, A.
J. Biomol. NMR (1995), 6, 277-293, PubMed 8520220 , Abstract

Hide non-primary 1 citaion

Related entities 1. double stranded RNA binding domain of PKR, : 1 : 4 : 49 entities Detail

Interaction partners 1. double stranded RNA binding domain of PKR, : 58 interactors Detail

More details for 58 interactors identified by 25 citations

Experiments performed 1 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr4110_3.str
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

Content subtype: bmr4110_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_one	Warning	1936		97.8 (chain: 1, length: 179)
1	Chemical shift references	chemical_shift_reference_one	Warning	3		No information

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_one
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 179, Sequence coverage: 97.8%
- Total number of assignments
  - ¹H chemical shifts: 1183
  - ¹³C chemical shifts: 577
  - ¹⁵N chemical shifts: 176
- Completeness of assignments
  - Entity_assemble_ID: 1
- Redox state of CYS
- Peptide bond of PRO
- Tautomeric state of HIS
- 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: 1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	1088	1013	93.1
¹³C chemical shifts	793	577	72.8
¹⁵N chemical shifts	198	176	88.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	371	359	96.8
¹³C chemical shifts	358	175	48.9
¹⁵N chemical shifts	173	166	96.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	717	654	91.2
¹³C chemical shifts	435	402	92.4
¹⁵N chemical shifts	25	10	40.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	90	85	94.4
¹³C chemical shifts	90	85	94.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	66	55	83.3
¹³C chemical shifts	66	50	75.8

Keywords dsRNA binding domain, NMR, PKR, resonance assignments

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Found 1 Document (2.826 seconds)

BMRB: 4110

Sample #1

Sample #2

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. double stranded RNA binding domain of PKR, : 1 : 4 : 49 entities Detail

Interaction partners 1. double stranded RNA binding domain of PKR, : 58 interactors Detail

Experiments performed 1 experiments Detail

Instrument

Sample #1

Sample #2

Chemical shift validation 3 contents Detail