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Found 1 Document (1.393 seconds)

BMRB: 30196

5TP6

Solution structure of the CaM34 with the iNOS CaM binding domain peptide

Authors

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

Assembly

Calmodulin, Nitric oxide synthase, inducible (E.C.1.14.13.39)

Entity

1. Calmodulin (polymer, Thiol state: not present), 148 monomers, 16618.19 Da Detail

ADQLTEEQIA EFKEAFSLFD KDGDGTITTK ELGTVMRSLG QNPTEAELQD MINEVDADGN GTIDFPEFLT MMARKMKDTD SEEEIREAFR VFAKDGNGYI SAAELRHVMT NLGEKLTDEE VDEMIREAAI DGDGQVNYEE FVQMMTAK

2. Nitric oxide synthase, inducible (polymer), 29 monomers, 3393.297 Da Detail

AGHMRPKRRE IPLKVLVKAV LFACMLMRK

Total weight

20011.486 Da

Max. entity weight

16618.19 Da

Source organism

Homo sapiens

Exptl. method

solution NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 92.1 %, Completeness: 73.9 %, Completeness (bb): 78.1 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	73.9 % (1506 of 2038)	81.0 % (861 of 1063)	60.5 % (478 of 790)	90.3 % (167 of 185)
Backbone	78.1 % (823 of 1054)	91.7 % (332 of 362)	63.4 % (329 of 519)	93.6 % (162 of 173)
Sidechain	71.4 % (820 of 1149)	75.5 % (529 of 701)	65.6 % (286 of 436)	41.7 % (5 of 12)
Aromatic	13.2 % (15 of 114)	14.0 % (8 of 57)	12.3 % (7 of 57)
Methyl	82.1 % (151 of 184)	91.3 % (84 of 92)	72.8 % (67 of 92)

1. Calmodulin

ADQLTEEQIA EFKEAFSLFD KDGDGTITTK ELGTVMRSLG QNPTEAELQD MINEVDADGN GTIDFPEFLT MMARKMKDTD SEEEIREAFR VFAKDGNGYI SAAELRHVMT NLGEKLTDEE VDEMIREAAI DGDGQVNYEE FVQMMTAK

2. Nitric oxide synthase, inducible

AGHMRPKRRE IPLKVLVKAV LFACMLMRK

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0, Details 1 mM [U-99% 13C; U-99% 15N] CaM34, 1 mM iNOS CaM binding domain peptide, 100 mM potassium chloride, 10 mM Calcium chloride, 0.2 mM sodium azide, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
1	CaM34	[U-99% 13C; U-99% 15N]	1 mM
2	Calcium chloride	natural abundance	10 mM
3	iNOS CaM binding domain peptide	natural abundance	1 mM
4	potassium chloride	natural abundance	100 mM
5	sodium azide	natural abundance	0.2 mM
6	H2O	natural abundance	90 %
7	D2O	natural abundance	10 %

Protein Blocks Logo

Calculated from 20 models in PDB: 5TP6, Strand ID: A, B 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

Related entities 1. Calmodulin, : 11 : 85 entities Detail

Related entities 2. Nitric oxide synthase, inducible, : 1 : 3 : 5 entities Detail

Interaction partners 2. Nitric oxide synthase, inducible, : 5 interactors Detail

More details for 5 interactors identified by 2 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 1 mM [U-99% 13C; U-99% 15N] CaM34, 1 mM iNOS CaM binding domain peptide, 100 mM potassium chloride, 10 mM Calcium chloride, 0.2 mM sodium azide, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
1	CaM34	[U-99% 13C; U-99% 15N]	1 mM
2	Calcium chloride	natural abundance	10 mM
3	iNOS CaM binding domain peptide	natural abundance	1 mM
4	potassium chloride	natural abundance	100 mM
5	sodium azide	natural abundance	0.2 mM
6	H2O	natural abundance	90 %
7	D2O	natural abundance	10 %

2 3D HNCA

Instrument

Bruker DRX - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	CaM34	[U-99% 13C; U-99% 15N]	1 mM
2	Calcium chloride	natural abundance	10 mM
3	iNOS CaM binding domain peptide	natural abundance	1 mM
4	potassium chloride	natural abundance	100 mM
5	sodium azide	natural abundance	0.2 mM
6	H2O	natural abundance	90 %
7	D2O	natural abundance	10 %

3 3D HCCH-TOCSY

Instrument

Bruker DRX - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	CaM34	[U-99% 13C; U-99% 15N]	1 mM
2	Calcium chloride	natural abundance	10 mM
3	iNOS CaM binding domain peptide	natural abundance	1 mM
4	potassium chloride	natural abundance	100 mM
5	sodium azide	natural abundance	0.2 mM
6	H2O	natural abundance	90 %
7	D2O	natural abundance	10 %

4 3D 1H-13C NOESY

Instrument

Bruker DRX - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	CaM34	[U-99% 13C; U-99% 15N]	1 mM
2	Calcium chloride	natural abundance	10 mM
3	iNOS CaM binding domain peptide	natural abundance	1 mM
4	potassium chloride	natural abundance	100 mM
5	sodium azide	natural abundance	0.2 mM
6	H2O	natural abundance	90 %
7	D2O	natural abundance	10 %

5 3D 1H-15N NOESY

Instrument

Bruker DRX - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	CaM34	[U-99% 13C; U-99% 15N]	1 mM
2	Calcium chloride	natural abundance	10 mM
3	iNOS CaM binding domain peptide	natural abundance	1 mM
4	potassium chloride	natural abundance	100 mM
5	sodium azide	natural abundance	0.2 mM
6	H2O	natural abundance	90 %
7	D2O	natural abundance	10 %

6 2D 1H-15N double filtered NOESY

Instrument

Bruker DRX - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	CaM34	[U-99% 13C; U-99% 15N]	1 mM
2	Calcium chloride	natural abundance	10 mM
3	iNOS CaM binding domain peptide	natural abundance	1 mM
4	potassium chloride	natural abundance	100 mM
5	sodium azide	natural abundance	0.2 mM
6	H2O	natural abundance	90 %
7	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_30196_5tp6.nef
Input source #2: Coordindates	5tp6.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
ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFAKDGNGYI
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFAKDGNGYI

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

Entity_assembly_ID (NMR): B vs Auth_asym_ID (model): B

-----510-------520-------530-
AGHMRPKRREIPLKVLVKAVLFACMLMRK
|||||||||||||||||||||||||||||
AGHMRPKRREIPLKVLVKAVLFACMLMRK
--------10--------20---------

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	148	0	0	100.0
B	B	29	0	0	100.0

Content subtype: combined_30196_5tp6.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	1438		97.3 (chain: A, length: 148), 58.6 (chain: B, length: 29)
1	Distance restraints	CNS/XPLOR_distance_constraints_3	Warning	2870 (1)	noe	95.3 (chain: A, length: 148), 58.6 (chain: B, length: 29)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_2	OK	252 (252)	.	95.9 (chain: A, length: 148)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 148, Sequence coverage: 97.3%
  - Entity_assembly_ID: B, Chain length: 29, Sequence coverage: 58.6%
- Total number of assignments
  - ¹H chemical shifts: 839
  - ¹³C chemical shifts: 438
  - ¹⁵N chemical shifts: 161
- Completeness of assignments
  - Entity_assemble_ID: A
  - Entity_assemble_ID: B
- Redox state of CYS
- 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
  - Chain_ID: B

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
50	ASP	CG	33.593

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	865	741	85.7
¹³C chemical shifts	645	420	65.1
¹⁵N chemical shifts	164	144	87.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	305	298	97.7
¹³C chemical shifts	296	147	49.7
¹⁵N chemical shifts	146	144	98.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	560	443	79.1
¹³C chemical shifts	349	273	78.2
¹⁵N chemical shifts	18	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	82	71	86.6
¹³C chemical shifts	82	66	80.5

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

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	198	98	49.5
¹³C chemical shifts	145	17	11.7
¹⁵N chemical shifts	31	17	54.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	57	34	59.6
¹³C chemical shifts	58	17	29.3
¹⁵N chemical shifts	27	17	63.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	141	64	45.4
¹³C chemical shifts	87	0	0.0
¹⁵N chemical shifts	4	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	22	15	68.2
¹³C chemical shifts	22	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	7	2	28.6
¹³C chemical shifts	7	0	0.0

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_3
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 148, Sequence coverage: 95.3%
  - Entity_assembly_ID: B, Chain length: 29, Sequence coverage: 58.6%
- Total number of restraints: 2826
- Weight of restraints: 1.0 (2826)
- Potential type of restraints: square-well-parabolic (2826)
- Range of distance target values: 2.25, 3.9 (Å)
- Histogram of distance target values
- Histogram of discrepancy in distance target values
- Distance restraints per residue
  - Chain_ID: A
  - Chain_ID: B
- Distance restraints on contact map

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_2
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 148, Sequence coverage: 95.9%
- Total number of restraints: 252
- Total number of restraints per polymer type: 252
- Weight of restraints: 1.0 (252)
- Potential type of restraints: square-well-parabolic (252)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords Calcium deficient, OXIDOREDUCTASE, nitric oxide synthase

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Found 1 Document (1.393 seconds)

BMRB: 30196

Sample

Related entities 1. Calmodulin, : 11 : 85 entities Detail

Related entities 2. Nitric oxide synthase, inducible, : 1 : 3 : 5 entities Detail

Interaction partners 2. Nitric oxide synthase, inducible, : 5 interactors Detail

Experiments performed 6 experiments Detail

Instrument

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NMR combined restraints 4 contents Detail