BMRBj - BMREntryMaster

Found 1 Document (0.971 seconds)

BMRB: 19036

2M55

NMR structure of the complex of an N-terminally acetylated alpha-synuclein peptide with calmodulin

Authors

Gruschus, J.M., Yap, T., Pistolesi, S., Maltsev, A.S., Lee, J.C.

Assembly

Calmodulin/a-syn peptide complex

Entity

1. calmodulin (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. peptide (polymer, Thiol state: not present), 20 monomers, 1950.347 Da Detail

MDVFMKGLSK AKEGVVAAAX

3. ACETYL GROUP (non-polymer, Thiol state: not present), 44.053 Da
4. CALCIUM ION (non-polymer, Thiol state: not present), 40.078 × 4 Da

Total weight

18860.924 Da

Max. entity weight

16706.21 Da

Source organism

Homo sapiens

Exptl. method

solution NMR

Refine. method

DGSA-distance geometry simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 98.8 %, Completeness: 47.6 %, Completeness (bb): 83.0 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	47.6 % (894 of 1879)	39.9 % (389 of 974)	47.7 % (347 of 728)	89.3 % (158 of 177)
Backbone	83.0 % (828 of 998)	98.8 % (341 of 345)	67.6 % (330 of 488)	95.2 % (157 of 165)
Sidechain	20.8 % (215 of 1035)	7.6 % (48 of 629)	42.1 % (166 of 394)	8.3 % (1 of 12)
Aromatic	0.0 % (0 of 110)	0.0 % (0 of 55)	0.0 % (0 of 55)
Methyl	18.7 % (31 of 166)	8.4 % (7 of 83)	28.9 % (24 of 83)

1. calmodulin

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

2. peptide

MDVFMKGLSK AKEGVVAAAX

Show sample condition

Sample #1

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 310 K, pH 6.36

#	Name	Isotope labeling	Concentration
1	calmodulin	[U-99% 13C; U-99% 15N]	600 uM
2	peptide	natural abundance	600 uM
3	MES	natural abundance	50 mM
4	potassium chloride	natural abundance	100 mM
5	CALCIUM ION	natural abundance	3 mM
6	H2O	natural abundance	95 %
7	D2O	natural abundance	5 %

Sample #2

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 310 K, pH 6.36

#	Name	Isotope labeling	Concentration
8	peptide	[U-13C; U-15N]-Met,Val,Phe,Gly,Leu,Ala	700 uM
9	calmodulin	natural abundance	700 uM
10	MES	natural abundance	50 mM
11	potassium chloride	natural abundance	100 mM
12	CALCIUM ION	natural abundance	3 mM
13	sodium azide	natural abundance	.1 %
14	H2O	natural abundance	95 %
15	D2O	natural abundance	5 %

Sample #3

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 310 K, pH 6.36

#	Name	Isotope labeling	Concentration
16	calmodulin	[U-99% 13C; U-99% 15N]	150 uM
17	peptide	natural abundance	150 uM
18	MES	natural abundance	50 mM
19	potassium chloride	natural abundance	100 mM
20	CALCIUM ION	natural abundance	3 mM
21	Pf1 phage	natural abundance	10 mg/mL
22	H2O	natural abundance	95 %
23	D2O	natural abundance	5 %

Protein Blocks Logo

Calculated from 20 models in PDB: 2M55, Strand ID: A, B Detail

Release date

2013-05-05

Citation

NMR structure of calmodulin complexed to an N-terminally acetylated α-synuclein peptide
Gruschus, J.M., Yap, T., Pistolesi, S., Maltsev, A.S., Lee, J.C.
Biochemistry (2013), 52, 3436-3445, PubMed 23607618 , DOI 10.1021/bi400199p , Abstract

Related entities 1. calmodulin, : 11 : 88 entities Detail

Related entities 2. peptide, : 1 : 30 : 12 entities Detail

Interaction partners 2. peptide, : 1 interactors Detail

More details for 1 interactors identified by 1 citations

Experiments performed 15 experiments Detail

1 3D 1H-15N NOESY

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 310 K, pH 6.36

#	Name	Isotope labeling	Concentration
1	calmodulin	[U-99% 13C; U-99% 15N]	600 uM
2	peptide	natural abundance	600 uM
3	MES	natural abundance	50 mM
4	potassium chloride	natural abundance	100 mM
5	CALCIUM ION	natural abundance	3 mM
6	H2O	natural abundance	95 %
7	D2O	natural abundance	5 %

2 3D 1H-15N NOESY

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 310 K, pH 6.36

#	Name	Isotope labeling	Concentration
8	peptide	[U-13C; U-15N]-Met,Val,Phe,Gly,Leu,Ala	700 uM
9	calmodulin	natural abundance	700 uM
10	MES	natural abundance	50 mM
11	potassium chloride	natural abundance	100 mM
12	CALCIUM ION	natural abundance	3 mM
13	sodium azide	natural abundance	.1 %
14	H2O	natural abundance	95 %
15	D2O	natural abundance	5 %

3 3D 1H-13C NOESY aliphatic

Instrument

Bruker Avance - 900 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 310 K, pH 6.36

#	Name	Isotope labeling	Concentration
1	calmodulin	[U-99% 13C; U-99% 15N]	600 uM
2	peptide	natural abundance	600 uM
3	MES	natural abundance	50 mM
4	potassium chloride	natural abundance	100 mM
5	CALCIUM ION	natural abundance	3 mM
6	H2O	natural abundance	95 %
7	D2O	natural abundance	5 %

4 2D 1H-13C HSQC aromatic

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 310 K, pH 6.36

#	Name	Isotope labeling	Concentration
1	calmodulin	[U-99% 13C; U-99% 15N]	600 uM
2	peptide	natural abundance	600 uM
3	MES	natural abundance	50 mM
4	potassium chloride	natural abundance	100 mM
5	CALCIUM ION	natural abundance	3 mM
6	H2O	natural abundance	95 %
7	D2O	natural abundance	5 %

5 3D 1H-13C NOESY aliphatic

Instrument

Bruker Avance - 900 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 310 K, pH 6.36

#	Name	Isotope labeling	Concentration
8	peptide	[U-13C; U-15N]-Met,Val,Phe,Gly,Leu,Ala	700 uM
9	calmodulin	natural abundance	700 uM
10	MES	natural abundance	50 mM
11	potassium chloride	natural abundance	100 mM
12	CALCIUM ION	natural abundance	3 mM
13	sodium azide	natural abundance	.1 %
14	H2O	natural abundance	95 %
15	D2O	natural abundance	5 %

6 3D 1H-13C NOESY aromatic

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 310 K, pH 6.36

#	Name	Isotope labeling	Concentration
8	peptide	[U-13C; U-15N]-Met,Val,Phe,Gly,Leu,Ala	700 uM
9	calmodulin	natural abundance	700 uM
10	MES	natural abundance	50 mM
11	potassium chloride	natural abundance	100 mM
12	CALCIUM ION	natural abundance	3 mM
13	sodium azide	natural abundance	.1 %
14	H2O	natural abundance	95 %
15	D2O	natural abundance	5 %

7 2D 1H-15N HSQC

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 310 K, pH 6.36

#	Name	Isotope labeling	Concentration
1	calmodulin	[U-99% 13C; U-99% 15N]	600 uM
2	peptide	natural abundance	600 uM
3	MES	natural abundance	50 mM
4	potassium chloride	natural abundance	100 mM
5	CALCIUM ION	natural abundance	3 mM
6	H2O	natural abundance	95 %
7	D2O	natural abundance	5 %

8 2D 1H-15N HSQC

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 310 K, pH 6.36

#	Name	Isotope labeling	Concentration
8	peptide	[U-13C; U-15N]-Met,Val,Phe,Gly,Leu,Ala	700 uM
9	calmodulin	natural abundance	700 uM
10	MES	natural abundance	50 mM
11	potassium chloride	natural abundance	100 mM
12	CALCIUM ION	natural abundance	3 mM
13	sodium azide	natural abundance	.1 %
14	H2O	natural abundance	95 %
15	D2O	natural abundance	5 %

9 2D 1H-15N HSQC

Instrument

Bruker Avance - 800 MHz

Sample

State anisotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 310 K, pH 6.36

#	Name	Isotope labeling	Concentration
16	calmodulin	[U-99% 13C; U-99% 15N]	150 uM
17	peptide	natural abundance	150 uM
18	MES	natural abundance	50 mM
19	potassium chloride	natural abundance	100 mM
20	CALCIUM ION	natural abundance	3 mM
21	Pf1 phage	natural abundance	10 mg/mL
22	H2O	natural abundance	95 %
23	D2O	natural abundance	5 %

10 2D 1H-13C HSQC aliphatic

Instrument

Bruker Avance - 900 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 310 K, pH 6.36

#	Name	Isotope labeling	Concentration
1	calmodulin	[U-99% 13C; U-99% 15N]	600 uM
2	peptide	natural abundance	600 uM
3	MES	natural abundance	50 mM
4	potassium chloride	natural abundance	100 mM
5	CALCIUM ION	natural abundance	3 mM
6	H2O	natural abundance	95 %
7	D2O	natural abundance	5 %

11 2D 1H-13C HSQC aromatic

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 310 K, pH 6.36

#	Name	Isotope labeling	Concentration
1	calmodulin	[U-99% 13C; U-99% 15N]	600 uM
2	peptide	natural abundance	600 uM
3	MES	natural abundance	50 mM
4	potassium chloride	natural abundance	100 mM
5	CALCIUM ION	natural abundance	3 mM
6	H2O	natural abundance	95 %
7	D2O	natural abundance	5 %

12 2D 1H-13C HSQC aliphatic

Instrument

Bruker Avance - 900 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 310 K, pH 6.36

#	Name	Isotope labeling	Concentration
8	peptide	[U-13C; U-15N]-Met,Val,Phe,Gly,Leu,Ala	700 uM
9	calmodulin	natural abundance	700 uM
10	MES	natural abundance	50 mM
11	potassium chloride	natural abundance	100 mM
12	CALCIUM ION	natural abundance	3 mM
13	sodium azide	natural abundance	.1 %
14	H2O	natural abundance	95 %
15	D2O	natural abundance	5 %

13 2D 1H-13C HSQC aromatic

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 310 K, pH 6.36

#	Name	Isotope labeling	Concentration
8	peptide	[U-13C; U-15N]-Met,Val,Phe,Gly,Leu,Ala	700 uM
9	calmodulin	natural abundance	700 uM
10	MES	natural abundance	50 mM
11	potassium chloride	natural abundance	100 mM
12	CALCIUM ION	natural abundance	3 mM
13	sodium azide	natural abundance	.1 %
14	H2O	natural abundance	95 %
15	D2O	natural abundance	5 %

14 2D 1H-13C HSQC aliphatic

Instrument

Bruker Avance - 800 MHz

Sample

State anisotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 310 K, pH 6.36

#	Name	Isotope labeling	Concentration
16	calmodulin	[U-99% 13C; U-99% 15N]	150 uM
17	peptide	natural abundance	150 uM
18	MES	natural abundance	50 mM
19	potassium chloride	natural abundance	100 mM
20	CALCIUM ION	natural abundance	3 mM
21	Pf1 phage	natural abundance	10 mg/mL
22	H2O	natural abundance	95 %
23	D2O	natural abundance	5 %

15 3D CBCA(CO)NH

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 310 K, pH 6.36

#	Name	Isotope labeling	Concentration
1	calmodulin	[U-99% 13C; U-99% 15N]	600 uM
2	peptide	natural abundance	600 uM
3	MES	natural abundance	50 mM
4	potassium chloride	natural abundance	100 mM
5	CALCIUM ION	natural abundance	3 mM
6	H2O	natural abundance	95 %
7	D2O	natural abundance	5 %

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints, RDC restraints	combined_19036_2m55.nef
Input source #2: Coordindates	2m55.cif
Diamagnetism of the molecular assembly	False (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:ACE:C	2:2:MET:N	unknown	unknown	n/a
2:20:ALA:C	2:21:NH2:N	unknown	unknown	n/a
1:129:ASP:OD1	3:4:CA:CA	unknown	unknown	n/a
1:26:THR:O	3:1:CA:CA	unknown	unknown	n/a
1:31:GLU:OE2	3:1:CA:CA	unknown	unknown	n/a
1:58:ASP:OD2	3:2:CA:CA	unknown	unknown	n/a
1:140:GLU:OE1	3:4:CA:CA	unknown	unknown	n/a
1:62:THR:O	3:2:CA:CA	unknown	unknown	n/a
1:131:ASP:OD1	3:4:CA:CA	unknown	unknown	n/a
1:93:ASP:OD1	3:3:CA:CA	unknown	unknown	n/a
1:60:ASN:OD1	3:2:CA:CA	unknown	unknown	n/a
1:56:ASP:OD1	3:2:CA:CA	unknown	unknown	n/a
1:135:GLN:O	3:4:CA:CA	unknown	unknown	n/a
1:67:GLU:OE2	3:2:CA:CA	unknown	unknown	n/a
1:97:ASN:OD1	3:3:CA:CA	unknown	unknown	n/a
1:99:TYR:O	3:3:CA:CA	unknown	unknown	n/a
1:24:ASP:OD2	3:1:CA:CA	unknown	unknown	n/a
1:22:ASP:OD2	3:1:CA:CA	unknown	unknown	n/a
1:20:ASP:OD1	3:1:CA:CA	unknown	unknown	n/a
1:95:ASP:OD2	3:3:CA:CA	unknown	unknown	n/a
1:104:GLU:OE2	3:3:CA:CA	unknown	unknown	n/a
1:140:GLU:OE2	3:4:CA:CA	unknown	unknown	n/a
1:31:GLU:OE1	3:1:CA:CA	unknown	unknown	n/a
1:58:ASP:OD1	3:2:CA:CA	unknown	unknown	n/a
1:133:ASP:OD1	3:4:CA:CA	unknown	unknown	n/a
1:67:GLU:OE1	3:2:CA:CA	unknown	unknown	n/a
1:104:GLU:OE1	3:3:CA:CA	unknown	unknown	n/a
1:24:ASP:OD1	3:1:CA:CA	unknown	unknown	n/a

Non-standard residues

Chain_ID	Seq_ID	Comp_ID	Chem_comp_name	Experimental evidences
B	200	ACE	ACETYL GROUP	Coordinates
B	220	NH2	AMINO GROUP	Coordinates
C	1	CA	CALCIUM ION	None
C	2	CA	CALCIUM ION	None
C	3	CA	CALCIUM ION	None
C	4	CA	CALCIUM ION	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

200-----210-------220
XMDVFMKGLSKAKEGVVAAAX
|||||||||||||||||||||
XMDVFMKGLSKAKEGVVAAAX
--------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	21	0	0	100.0

Content subtype: combined_19036_2m55.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Covalent bonds	assembly	OK	28		No information
1	Assigned chemical shifts	assigned_chem_shift_list_1	OK	806		100.0 (chain: A, length: 148), 85.7 (chain: B, length: 21)
1	Distance restraints	CNS/XPLOR_distance_constraints_3	Warning	4706 (1)	noe	99.3 (chain: A, length: 148), 90.5 (chain: B, length: 21)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_4	OK	282 (282)	.	97.3 (chain: A, length: 148), 85.7 (chain: B, length: 21)
1	RDC restraints	CNS/XPLOR_dipolar_coupling_2	OK	147 (147)	.	77.7 (chain: A, length: 148)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 148, Sequence coverage: 100.0%
  - Entity_assembly_ID: B, Chain length: 21, Sequence coverage: 85.7%
- Total number of assignments
  - ¹H chemical shifts: 341
  - ¹³C chemical shifts: 308
  - ¹⁵N chemical shifts: 157
- Completeness of assignments
  - Entity_assemble_ID: A
  - Entity_assemble_ID: B
- Peptide bond of PRO
- 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	303	34.9
¹³C chemical shifts	645	284	44.0
¹⁵N chemical shifts	164	144	87.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	305	303	99.3
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	562	0	0.0
¹³C chemical shifts	349	137	39.3
¹⁵N chemical shifts	18	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	80	0	0.0
¹³C chemical shifts	80	11	13.8

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	111	38	34.2
¹³C chemical shifts	85	24	28.2
¹⁵N chemical shifts	20	13	65.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	41	38	92.7
¹³C chemical shifts	38	13	34.2
¹⁵N chemical shifts	20	13	65.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	70	0	0.0
¹³C chemical shifts	47	11	23.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	15	0	0.0
¹³C chemical shifts	15	4	26.7

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_3
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 148, Sequence coverage: 99.3%
  - Entity_assembly_ID: B, Chain length: 21, Sequence coverage: 90.5%
- Total number of restraints: 4690
- Weight of restraints: 1.0 (4690)
- Potential type of restraints: lower-bound-parabolic (15), square-well-parabolic (4675)
- Range of distance target values: 1.73, 7.14 (Å)
- Histogram of distance target values
- Histogram of discrepancy in distance target values
- Distance restraints per residue
  - Chain_ID: A
  - Chain_ID: B
  - Chain_ID: C
    None
- Distance restraints on contact map

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_4
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 148, Sequence coverage: 97.3%
  - Entity_assembly_ID: B, Chain length: 21, Sequence coverage: 85.7%
- Total number of restraints: 282
- Total number of restraints per polymer type: 282
- Weight of restraints: 1.0 (282)
- Potential type of restraints: square-well-parabolic (282)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A
  - Chain_ID: B

RDC restraints

Saveframe: CNS/XPLOR_dipolar_coupling_2

Status: OK
Experiment type: .

Sequence coverage of experimental data

Entity_assembly_ID: A, Chain length: 148, Sequence coverage: 77.7%

--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100
ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYI
   ||||||||||| ||||||||||||||||||||||| ||| ||||  |||        |||||| ||||| |||  | ||| || || | || | |||
...LTEEQIAEFKE.FSLFDKDGDGTITTKELGTVMRS.GQN.TEAE..DMI........GTIDFP.FLTMM.RKM..T.SEE.IR.AF.V.DK.G.GYI
--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100

-------110-------120-------130-------140--------
SAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK
|||| |||||||||||||||||||| ||||| ||||||||||  ||| 
SAAE.RHVMTNLGEKLTDEEVDEMI.EADID.DGQVNYEEFV..MTA 
-------110-------120-------130-------140-------

Total number of restraints: 147
Potential type of restraints: undefined (147)
Range of observed RDC values: 100.0, -100.0 (Hz)
RDC restraints per residue
- Chain_ID: A
  None

Keywords Ca-binding, Protein/peptide

Search

Query history

Resources

Search for primary databases

Search for subsidiary databases

Display

Hits per page

Statistics

Query Changes will take effect after "OK" button is selected.

Maximum hits

Default conjunction operator

Omni-box

Search filter

Sequence search (BLAST)

E-value

Query sequence coverage

Miscellaneous

The number of previewed publications

Completeness of assigned chemical shift

Sequence chart about top aligned regions

Sequence chart about interacting regions

Hit context with highlight

Link destinations for BMRB, PDB and EMDB

Found 1 Document (0.971 seconds)

BMRB: 19036

Sample #1

Sample #2

Sample #3

Related entities 1. calmodulin, : 11 : 88 entities Detail

Related entities 2. peptide, : 1 : 30 : 12 entities Detail

Interaction partners 2. peptide, : 1 interactors Detail

Experiments performed 15 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 5 contents Detail