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Found 1 Document (0.993 seconds)

BMRB: 30195

5TP5

Solution structure of the calcium deficient mutant calmodulin CaM1234

Authors

Piazza, M., Dieckmann, T., Guillemette, J.G.

Assembly

Calmodulin

Entity

1. Calmodulin (polymer, Thiol state: not present), 148 monomers, 16530.17 Da Detail

ADQLTEEQIA EFKEAFSLFA KDGDGTITTK ELGTVMRSLG QNPTEAELQD MINEVAADGN GTIDFPEFLT MMARKMKDTD SEEEIREAFR VFAKDGNGYI SAAELRHVMT NLGEKLTDEE VDEMIREAAI DGDGQVNYEE FVQMMTAK

Formula weight

16530.17 Da

Source organism

Homo sapiens

Exptl. method

solution NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 95.9 %, Completeness: 63.9 %, Completeness (bb): 81.0 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	63.9 % (1065 of 1666)	72.2 % (623 of 863)	46.5 % (300 of 645)	89.9 % (142 of 158)
Backbone	81.0 % (716 of 884)	96.4 % (294 of 305)	64.7 % (280 of 433)	97.3 % (142 of 146)
Sidechain	51.5 % (473 of 919)	59.0 % (329 of 558)	41.3 % (144 of 349)	0.0 % (0 of 12)
Aromatic	0.0 % (0 of 100)	0.0 % (0 of 50)	0.0 % (0 of 50)
Methyl	58.7 % (88 of 150)	86.7 % (65 of 75)	30.7 % (23 of 75)

1. Calmodulin

ADQLTEEQIA EFKEAFSLFA KDGDGTITTK ELGTVMRSLG QNPTEAELQD MINEVAADGN GTIDFPEFLT MMARKMKDTD SEEEIREAFR VFAKDGNGYI SAAELRHVMT NLGEKLTDEE VDEMIREAAI DGDGQVNYEE FVQMMTAK

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0, Details 100 mM potassium chloride, 1 mM [U-99% 13C; U-99% 15N] CaM1234, 0.2 mM sodium azide, 0.2 mM EDTA, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
1	CaM1234	[U-99% 13C; U-99% 15N]	1 mM
2	EDTA	natural abundance	0.2 mM
3	potassium chloride	natural abundance	100 mM
4	sodium azide	natural abundance	0.2 mM
5	H2O	natural abundance	90 %
6	D2O	natural abundance	10 %

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	internal	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	internal	indirect	0.1013291

Referencing offset: 2.68 ppm, Outliers: 1 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	internal	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	internal	indirect	0.1013291

Referencing offset: 2.68 ppm, Outliers: 1 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	internal	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	internal	indirect	0.1013291

Referencing offset: 0.02 ppm, Outliers: 3 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 5TP5, Strand ID: A Detail

Release date

2016-11-27

Citation

Structural Consequences of Calmodulin EF Hand Mutations
Piazza, M., Taiakina, V., Dieckmann, T., Guillemette, J.G.
Biochemistry (2017), 56, 944-956, PubMed 28121131 , DOI 10.1021/acs.biochem.6b01296 , Abstract

Entries sharing articles BMRB: 1 entries Detail

BMRB: 30196 released on 2016-11-27
Title Solution structure of the CaM34 with the iNOS CaM binding domain peptide

Related entities 1. Calmodulin, : 1 : 115 : 180 entities Detail

Interaction partners 1. Calmodulin, : 1 interactors Detail

More details for 1 interactors identified by 1 citations

Experiments performed 6 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker DRX - 600 MHz

Sample

State anisotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0, Details 100 mM potassium chloride, 1 mM [U-99% 13C; U-99% 15N] CaM1234, 0.2 mM sodium azide, 0.2 mM EDTA, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
1	CaM1234	[U-99% 13C; U-99% 15N]	1 mM
2	EDTA	natural abundance	0.2 mM
3	potassium chloride	natural abundance	100 mM
4	sodium azide	natural abundance	0.2 mM
5	H2O	natural abundance	90 %
6	D2O	natural abundance	10 %

2 3D HNCA

Instrument

Bruker DRX - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	CaM1234	[U-99% 13C; U-99% 15N]	1 mM
2	EDTA	natural abundance	0.2 mM
3	potassium chloride	natural abundance	100 mM
4	sodium azide	natural abundance	0.2 mM
5	H2O	natural abundance	90 %
6	D2O	natural abundance	10 %

3 3D CBCA(CO)NH

Instrument

Bruker DRX - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	CaM1234	[U-99% 13C; U-99% 15N]	1 mM
2	EDTA	natural abundance	0.2 mM
3	potassium chloride	natural abundance	100 mM
4	sodium azide	natural abundance	0.2 mM
5	H2O	natural abundance	90 %
6	D2O	natural abundance	10 %

4 3D HCCH-TOCSY

Instrument

Bruker DRX - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	CaM1234	[U-99% 13C; U-99% 15N]	1 mM
2	EDTA	natural abundance	0.2 mM
3	potassium chloride	natural abundance	100 mM
4	sodium azide	natural abundance	0.2 mM
5	H2O	natural abundance	90 %
6	D2O	natural abundance	10 %

5 3D 1H-15N NOESY

Instrument

Bruker DRX - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	CaM1234	[U-99% 13C; U-99% 15N]	1 mM
2	EDTA	natural abundance	0.2 mM
3	potassium chloride	natural abundance	100 mM
4	sodium azide	natural abundance	0.2 mM
5	H2O	natural abundance	90 %
6	D2O	natural abundance	10 %

6 3D 1H-13C NOESY

Instrument

Bruker DRX - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	CaM1234	[U-99% 13C; U-99% 15N]	1 mM
2	EDTA	natural abundance	0.2 mM
3	potassium chloride	natural abundance	100 mM
4	sodium azide	natural abundance	0.2 mM
5	H2O	natural abundance	90 %
6	D2O	natural abundance	10 %

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_30195_5tp5.nef
Input source #2: Coordindates	5tp5.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
ADQLTEEQIAEFKEAFSLFAKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVAADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFAKDGNGYI
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
ADQLTEEQIAEFKEAFSLFAKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVAADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFAKDGNGYI

-------110-------120-------130-------140--------
SAAELRHVMTNLGEKLTDEEVDEMIREAAIDGDGQVNYEEFVQMMTAK
||||||||||||||||||||||||||||||||||||||||||||||||
SAAELRHVMTNLGEKLTDEEVDEMIREAAIDGDGQVNYEEFVQMMTAK

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	148	0	0	100.0

Content subtype: combined_30195_5tp5.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	OK	1012		95.9 (chain: A, length: 148)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	Warning	2799 (1)	noe	95.9 (chain: A, length: 148)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	236 (236)	.	94.6 (chain: A, length: 148)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 148, Sequence coverage: 95.9%
- Total number of assignments
  - ¹H chemical shifts: 604
  - ¹³C chemical shifts: 266
  - ¹⁵N chemical shifts: 142
- 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

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	863	604	70.0
¹³C chemical shifts	645	266	41.2
¹⁵N chemical shifts	164	142	86.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	305	294	96.4
¹³C chemical shifts	296	142	48.0
¹⁵N chemical shifts	146	142	97.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	558	310	55.6
¹³C chemical shifts	349	124	35.5
¹⁵N chemical shifts	18	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	84	64	76.2
¹³C chemical shifts	84	14	16.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	50	0	0.0
¹³C chemical shifts	50	0	0.0

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 148, Sequence coverage: 95.9%
- Total number of restraints: 2757
- Weight of restraints: 1.0 (2757)
- Potential type of restraints: square-well-parabolic (2757)
- Range of distance target values: 2.25, 3.9 (Å)
- Histogram of 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: 148, Sequence coverage: 94.6%
- Total number of restraints: 236
- Total number of restraints per polymer type: 236
- Weight of restraints: 1.0 (236)
- Potential type of restraints: square-well-parabolic (236)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords Calcium deficient, calmodulin

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Found 1 Document (0.993 seconds)

BMRB: 30195

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Entries sharing articles BMRB: 1 entries Detail

Related entities 1. Calmodulin, : 1 : 115 : 180 entities Detail

Interaction partners 1. Calmodulin, : 1 interactors Detail

Experiments performed 6 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 4 contents Detail