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Found 1 Document (1.166 seconds)

BMRB: 19586

2MG5

Solution Structure of Calmodulin bound to the target peptide of Endothelial Nitrogen Oxide Synthase phosphorylated at Thr495

Authors

Piazza, M., Dieckmann, T.

Assembly

Calmodulin bound to the target peptide of Endothelial Nitrogen Oxide Synthase phosphorylated at Thr495

Entity

1. Calmodulin bound to the target peptide of Endothelial Nitrogen Oxide Synthase phosphorylated at Thr495, entity 1 (polymer, Thiol state: not present), 148 monomers, 16706.21 Da Detail

ADQLTEEQIA EFKEAFSLFD KDGDGTITTK ELGTVMRSLG QNPTEAELQD MINEVDADGN GTIDFPEFLT MMARKMKDTD SEEEIREAFR VFDKDGNGYI SAAELRHVMT NLGEKLTDEE VDEMIREADI DGDGQVNYEE FVQMMTAK

2. Calmodulin bound to the target peptide of Endothelial Nitrogen Oxide Synthase phosphorylated at Thr495, entity 2 (polymer, Thiol state: not present), 16 monomers, 1709.014 Da Detail

TFKEVANAVK ISASLM

Total weight

18415.225 Da

Max. entity weight

16706.21 Da

Source organism

Homo sapiens

Exptl. method

solution NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 99.4 %, Completeness: 77.7 %, Completeness (bb): 79.8 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	77.7 % (1440 of 1853)	88.5 % (850 of 960)	62.0 % (445 of 718)	82.9 % (145 of 175)
Backbone	79.8 % (782 of 980)	98.5 % (332 of 337)	63.4 % (305 of 481)	89.5 % (145 of 162)
Sidechain	77.1 % (791 of 1026)	83.1 % (518 of 623)	70.0 % (273 of 390)	0.0 % (0 of 13)
Aromatic	37.3 % (41 of 110)	58.2 % (32 of 55)	16.4 % (9 of 55)
Methyl	81.3 % (135 of 166)	90.4 % (75 of 83)	72.3 % (60 of 83)

1. entity 1

ADQLTEEQIA EFKEAFSLFD KDGDGTITTK ELGTVMRSLG QNPTEAELQD MINEVDADGN GTIDFPEFLT MMARKMKDTD SEEEIREAFR VFDKDGNGYI SAAELRHVMT NLGEKLTDEE VDEMIREADI DGDGQVNYEE FVQMMTAK

2. entity 2

TFKEVANAVK ISASLM

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Concentration
1	entity_1	[U-99% 13C; U-99% 15N]	1 mM
2	entity_2	natural abundance	1 mM
3	KCl	natural abundance	100 mM

Protein Blocks Logo

Calculated from 20 models in PDB: 2MG5, Strand ID: A, B Detail

Release date

2014-02-10

Citation

Solution structure of calmodulin bound to the target peptide of endothelial nitric oxide synthase phosphorylated at Thr495
Piazza, M., Taiakina, V., Guillemette, S.R., Guillemette, J., Dieckmann, T.
Biochemistry (2014), 53, 1241-1249, PubMed 24495081 , DOI 10.1021/bi401466s , Abstract

Related entities 1. Calmodulin bound to the target peptide of Endothelial Nitrogen Oxide Synthase phosphorylated at Thr495, entity 1, : 11 : 88 entities Detail

Related entities 2. Calmodulin bound to the target peptide of Endothelial Nitrogen Oxide Synthase phosphorylated at Thr495, entity 2, : 1 : 11 : 1 : 1 entities Detail

Interaction partners 2. Calmodulin bound to the target peptide of Endothelial Nitrogen Oxide Synthase phosphorylated at Thr495, entity 2, : 2 interactors Detail

More details for 2 interactors identified by 2 citations

Experiments performed 5 experiments Detail

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_19586_2mg5.nef
Input source #2: Coordindates	2mg5.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	True (see coodinates for details)
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)

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
2:1:TPO:C	2:2:PHE:N	unknown	unknown	n/a

Non-standard residues

Chain_ID	Seq_ID	Comp_ID	Chem_comp_name	Experimental evidences
B	495	TPO	PHOSPHOTHREONINE	None

Sequence alignments

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

--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100
ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYI
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYI

-------110-------120-------130-------140--------
SAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK
||||||||||||||||||||||||||||||||||||||||||||||||
SAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK

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

----500-------510
TXFKEVANAVKISASLM
 ||||||||||||||||
.XFKEVANAVKISASLM
0--------10------

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	148	0	0	100.0
B	B	16	1	0	100.0

Content subtype: combined_19586_2mg5.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Covalent bonds	assembly	OK	1		No information
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	1396		98.6 (chain: A, length: 148), 94.1 (chain: B, length: 17)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	Warning	2448 (1)	noe	98.0 (chain: A, length: 148), 88.2 (chain: B, length: 17)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	273 (273)	.	99.3 (chain: A, length: 148)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 148, Sequence coverage: 98.6%
  - Entity_assembly_ID: B, Chain length: 17, Sequence coverage: 94.1%
- Total number of assignments
  - ¹H chemical shifts: 854
  - ¹³C chemical shifts: 397
  - ¹⁵N chemical shifts: 145
- Completeness of assignments
  - Entity_assemble_ID: A
  - Entity_assemble_ID: B
- 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

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	867	753	86.9
¹³C chemical shifts	645	397	61.6
¹⁵N chemical shifts	164	145	88.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	305	301	98.7
¹³C chemical shifts	296	144	48.6
¹⁵N chemical shifts	146	145	99.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	562	452	80.4
¹³C chemical shifts	349	253	72.5
¹⁵N chemical shifts	18	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	80	65	81.2
¹³C chemical shifts	80	60	75.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	50	30	60.0
¹³C chemical shifts	50	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	97	76	78.4
¹³C chemical shifts	77	0	0.0
¹⁵N chemical shifts	18	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	34	30	88.2
¹³C chemical shifts	34	0	0.0
¹⁵N chemical shifts	17	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	63	46	73.0
¹³C chemical shifts	43	0	0.0
¹⁵N chemical shifts	1	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	14	11	78.6
¹³C chemical shifts	14	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	5	0	0.0
¹³C chemical shifts	5	0	0.0

Covalent bonds

Saveframe: assembly
- Status: OK

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: 98.0%
  - Entity_assembly_ID: B, Chain length: 17, Sequence coverage: 88.2%
- Total number of restraints: 2403
- Weight of restraints: 1.0 (2403)
- Potential type of restraints: square-well-parabolic (2403)
- Range of distance target values: 2.25, 4.4 (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_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 148, Sequence coverage: 99.3%
- Total number of restraints: 273
- Total number of restraints per polymer type: 273
- Weight of restraints: 1.0 (273)
- Potential type of restraints: square-well-parabolic (273)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords Calmodulin, eNOS, Nitric Oxide Synthase

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Found 1 Document (1.166 seconds)

BMRB: 19586

Sample

Related entities 1. Calmodulin bound to the target peptide of Endothelial Nitrogen Oxide Synthase phosphorylated at Thr495, entity 1, : 11 : 88 entities Detail

Related entities 2. Calmodulin bound to the target peptide of Endothelial Nitrogen Oxide Synthase phosphorylated at Thr495, entity 2, : 1 : 11 : 1 : 1 entities Detail

Interaction partners 2. Calmodulin bound to the target peptide of Endothelial Nitrogen Oxide Synthase phosphorylated at Thr495, entity 2, : 2 interactors Detail

Experiments performed 5 experiments Detail

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NMR combined restraints 4 contents Detail