BMRBj - BMREntryMaster

Found 1 Document (1.313 seconds)

BMRB: 1634

4CLN

Triple-Resonance Multidimensional NMR Study of Calmodulin Complexed with the Binding Domain of Skeletal Muscle Myosin Light-Chain Kinase: Indication of a Conformational Change in the Central Helix

Authors

Ikura, M., Kay, L.E., Krinks, M., Bax, A.

Assembly

calmodulin

Entity

1. calmodulin (polymer), 148 monomers, 16678.20 Da Detail

ADQLTEEQIA EFKEAFSLFD KDGDGTITTK ELGTVMRSLG QNPTEAELQD MINEVDADGN GTIDFPEFLT MMARKMKDTD SEEEIREAFR VFDKDGNGFI SAAELRHVMT NLGEKLTDEE VDEMIREANI DGDGQVNYEE FVTMMTSK

Formula weight

16678.2 Da

Source organism

Drosophila melanogaster

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 52.1 %, Completeness (bb): 86.4 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	52.1 % (870 of 1671)	44.2 % (383 of 867)	52.6 % (340 of 646)	93.0 % (147 of 158)
Backbone	86.4 % (764 of 884)	98.4 % (300 of 305)	73.7 % (319 of 433)	99.3 % (145 of 146)
Sidechain	14.3 % (132 of 924)	14.9 % (84 of 562)	13.1 % (46 of 350)	16.7 % (2 of 12)
Aromatic	4.9 % (5 of 102)	5.9 % (3 of 51)	3.9 % (2 of 51)
Methyl	14.8 % (21 of 142)	15.5 % (11 of 71)	14.1 % (10 of 71)

1. calmodulin

ADQLTEEQIA EFKEAFSLFD KDGDGTITTK ELGTVMRSLG QNPTEAELQD MINEVDADGN GTIDFPEFLT MMARKMKDTD SEEEIREAFR VFDKDGNGFI SAAELRHVMT NLGEKLTDEE VDEMIREANI DGDGQVNYEE FVTMMTSK

Show sample condition

Sample

Temperature 309 K, pH 6.8

Release date

1995-07-30

Citation

Triple-resonance multidimensional NMR study of calmodulin complexed with the binding domain of skeletal muscle myosin light-chain kinase: indication of a conformational change in the central helix
Ikura, M., Kay, L.E., Krinks, M., Bax, A.
Biochemistry (1991), 30, 5498-5504, PubMed 2036419 , DOI 10.1021/bi00236a024 , Abstract

Related entities 1. calmodulin, : 1 : 24 : 270 entities Detail

Interaction partners 1. calmodulin, : 1 interactors Detail

More details for 1 interactors identified by 1 citations

Experiments performed 1 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr1634_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: bmr1634_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	chemical_shift_assignment_data_set_one	Warning	746		100.0 (chain: 1, length: 148)

Assigned chemical shifts

Saveframe: chemical_shift_assignment_data_set_one
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 148, Sequence coverage: 100.0%
- Total number of assignments
  - ¹³C chemical shifts: 296
  - ¹H chemical shifts: 303
  - ¹⁵N chemical shifts: 147
- Completeness of assignments
  - Entity_assemble_ID: 1
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
43	PRO	N	136.4
66	PRO	N	137.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	80	0	0.0
¹H chemical shifts	80	0	0.0

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Found 1 Document (1.313 seconds)

BMRB: 1634

Sample

Related entities 1. calmodulin, : 1 : 24 : 270 entities Detail

Interaction partners 1. calmodulin, : 1 interactors Detail

Experiments performed 1 experiments Detail

Instrument

Sample

Chemical shift validation 3 contents Detail

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	646	296	45.8
¹H chemical shifts	867	303	34.9
¹⁵N chemical shifts	164	145	88.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	296	296	100.0
¹H chemical shifts	305	303	99.3
¹⁵N chemical shifts	146	145	99.3