BMRBj - BMREntryMaster

Found 1 Document (1.39 seconds)

BMRB: 7190

5I0I

The structure and function of a novel two-site calcium-binding fragment of calmodulin

Authors

Lakowski, T.M., Lee, G.M., Reid, R.E., McIntosh, L.P.

Assembly

CaM2/3

Entity

1. CaM2/3 (polymer, Thiol state: not present), 68 monomers, 7700.475 Da Detail

AELQDMINEV DADGNGTIDF PEFLTMMARK MKDTDSEEEI REAFRVFDKD GNGYISAAEL RHVMTNLG

2. CA (non-polymer), 40.078 × 2 Da

Total weight

7780.631 Da

Max. entity weight

7700.475 Da

Exptl. method

NMR

Refine. method

Restrained molecular dynamics, simulated annealing

Data set

assigned_chemical_shifts, heteronucl_NOEs, heteronucl_T1_relaxation, heteronucl_T2_relaxation

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 95.8 %, Completeness (bb): 97.5 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	95.8 % (735 of 767)	96.0 % (382 of 398)	95.3 % (283 of 297)	97.2 % (70 of 72)
Backbone	97.5 % (396 of 406)	97.9 % (137 of 140)	97.5 % (194 of 199)	97.0 % (65 of 67)
Sidechain	94.8 % (402 of 424)	95.0 % (245 of 258)	94.4 % (152 of 161)	100.0 % (5 of 5)
Aromatic	92.3 % (48 of 52)	92.3 % (24 of 26)	92.3 % (24 of 26)
Methyl	100.0 % (64 of 64)	100.0 % (32 of 32)	100.0 % (32 of 32)

1. CaM2/3

AELQDMINEV DADGNGTIDF PEFLTMMARK MKDTDSEEEI REAFRVFDKD GNGYISAAEL RHVMTNLG

Show sample condition

Sample

Temperature 298 (±0) K

#	Name	Isotope labeling	Type	Concentration
1	CaM2/3	[U-13C; U-15N]	protein	0.5 mM
2	Tris d11	11 D	buffer	20 mM
3	CaCl2		salt	10 mM
4	KCl		salt	50 mM

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	external	indirect	0.0
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	external	indirect	0.0

Referencing offset: 0.17 ppm, Outliers: 2 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	external	indirect	0.0
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	external	indirect	0.0

Referencing offset: 0.17 ppm, Outliers: 2 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	external	indirect	0.0
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	external	indirect	0.0

Referencing offset: -0.02 ppm, Outliers: 2 Detail

LACS Plot; CO

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	external	indirect	0.0
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	external	indirect	0.0

Referencing offset: -0.48 ppm, Outliers: 2 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 2HF5, Strand ID: A Detail

Heteronucl. T₁

64 T₁ values in 1 lists
Coherence Sz, Field strength (¹H) 500 MHz, Temperature 298 (±0) K Detail

Heteronucl. T₂

64 T₂ values in 1 lists
Coherence S(+,-), Field strength (¹H) 500 MHz, Temperature 298 (±0) K Detail

Heteronucl. NOE

64 NOE values in 1 lists
Value type na, Field strength (¹H) 500 MHz, Temperature 298 (±0) K Detail

Heteronucl. T₁/T₂

64 T₁/T₂ values in 1 lists
Field strength (¹H) 500 MHz, Temperature 298 (±0) K Detail

Release date

2007-09-23

Citation

Calcium-induced folding of a fragment of calmodulin composed of EF-hands 2 and 3
Lakowski, T.M., Lee, G.M., Okon, M., Reid, R.E., McIntosh, L.P.
Protein Sci. (2007), 16, 1119-1132, PubMed 17473011 , DOI 10.1110/ps.072777107 , Abstract

Related entities 1. CaM2/3, : 2 : 114 : 21 : 1 : 181 entities Detail

Interaction partners 1. CaM2/3, : 3 interactors Detail

More details for 3 interactors identified by 3 citations

Experiments performed 6 experiments Detail

1 1H-15N-1H NOESY-HSQC

Instrument

#1 Model Varian Unity (500 MHz)

#2 Model Varian Inova (600 MHz)

Sample #1

Temperature 298 (±0) K

#	Name	Isotope labeling	Type	Concentration
1	CaM2/3	[U-13C; U-15N]	protein	0.5 mM
2	Tris d11	11 D	buffer	20 mM
3	CaCl2		salt	10 mM
4	KCl		salt	50 mM

Sample #2

Temperature 298 (±0) K

#	Name	Isotope labeling	Type	Concentration
5	CaM2/3	[U-15N]	protein	0.2 mM
6	Tris d11	11 D	buffer	20 mM
7	CaCl2		salt	10 mM
8	KCl		salt	50 mM

2 SIMULTANEOUS 1H-13C/15N-1H

Instrument

#1 Model Varian Unity (500 MHz)

#2 Model Varian Inova (600 MHz)

Sample #1

Temperature 298 (±0) K

#	Name	Isotope labeling	Type	Concentration
1	CaM2/3	[U-13C; U-15N]	protein	0.5 mM
2	Tris d11	11 D	buffer	20 mM
3	CaCl2		salt	10 mM
4	KCl		salt	50 mM

Sample #2

Temperature 298 (±0) K

#	Name	Isotope labeling	Type	Concentration
5	CaM2/3	[U-15N]	protein	0.2 mM
6	Tris d11	11 D	buffer	20 mM
7	CaCl2		salt	10 mM
8	KCl		salt	50 mM

3 NOESY-HSQC

Instrument

#1 Model Varian Unity (500 MHz)

#2 Model Varian Inova (600 MHz)

Sample #1

Temperature 298 (±0) K

#	Name	Isotope labeling	Type	Concentration
1	CaM2/3	[U-13C; U-15N]	protein	0.5 mM
2	Tris d11	11 D	buffer	20 mM
3	CaCl2		salt	10 mM
4	KCl		salt	50 mM

Sample #2

Temperature 298 (±0) K

#	Name	Isotope labeling	Type	Concentration
5	CaM2/3	[U-15N]	protein	0.2 mM
6	Tris d11	11 D	buffer	20 mM
7	CaCl2		salt	10 mM
8	KCl		salt	50 mM

4 AROMATIC 1H-13C-1H

Instrument

#1 Model Varian Unity (500 MHz)

#2 Model Varian Inova (600 MHz)

Sample #1

Temperature 298 (±0) K

#	Name	Isotope labeling	Type	Concentration
1	CaM2/3	[U-13C; U-15N]	protein	0.5 mM
2	Tris d11	11 D	buffer	20 mM
3	CaCl2		salt	10 mM
4	KCl		salt	50 mM

Sample #2

Temperature 298 (±0) K

#	Name	Isotope labeling	Type	Concentration
5	CaM2/3	[U-15N]	protein	0.2 mM
6	Tris d11	11 D	buffer	20 mM
7	CaCl2		salt	10 mM
8	KCl		salt	50 mM

5 NOESY-HSQC

Instrument

#1 Model Varian Unity (500 MHz)

#2 Model Varian Inova (600 MHz)

Sample #1

Temperature 298 (±0) K

#	Name	Isotope labeling	Type	Concentration
1	CaM2/3	[U-13C; U-15N]	protein	0.5 mM
2	Tris d11	11 D	buffer	20 mM
3	CaCl2		salt	10 mM
4	KCl		salt	50 mM

Sample #2

Temperature 298 (±0) K

#	Name	Isotope labeling	Type	Concentration
5	CaM2/3	[U-15N]	protein	0.2 mM
6	Tris d11	11 D	buffer	20 mM
7	CaCl2		salt	10 mM
8	KCl		salt	50 mM

6 METHYL 1H-13C/15N-1H NOESY-HSQC

Instrument

#1 Model Varian Unity (500 MHz)

#2 Model Varian Inova (600 MHz)

Sample #1

Temperature 298 (±0) K

#	Name	Isotope labeling	Type	Concentration
1	CaM2/3	[U-13C; U-15N]	protein	0.5 mM
2	Tris d11	11 D	buffer	20 mM
3	CaCl2		salt	10 mM
4	KCl		salt	50 mM

Sample #2

Temperature 298 (±0) K

#	Name	Isotope labeling	Type	Concentration
5	CaM2/3	[U-15N]	protein	0.2 mM
6	Tris d11	11 D	buffer	20 mM
7	CaCl2		salt	10 mM
8	KCl		salt	50 mM

Chemical shift validation 4 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts, Heteronucl NOE exptl data, Heteronucl T1 relaxation data, Heteronucl T2 relaxation data	bmr7190_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: bmr7190_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	chem_shift_list_1	Warning	802		100.0 (chain: 1, length: 68)
1	Chemical shift references	chemical_shift_referencing	OK	3		No information

Assigned chemical shifts

Saveframe: chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 68, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 449
  - ¹³C chemical shifts: 283
  - ¹⁵N chemical shifts: 70
- Completeness of assignments
  - Entity_assemble_ID: 1
- Peptide bond of PRO
- Tautomeric state of HIS
- 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: 1

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
4	GLN	CD	180.267
8	ASN	CG	176.425
66	ASN	CG	177.304

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	398	381	95.7
¹³C chemical shifts	297	280	94.3
¹⁵N chemical shifts	76	70	92.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	140	137	97.9
¹³C chemical shifts	136	130	95.6
¹⁵N chemical shifts	67	65	97.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	258	244	94.6
¹³C chemical shifts	161	150	93.2
¹⁵N chemical shifts	9	5	55.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	37	34	91.9
¹³C chemical shifts	37	32	86.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	26	24	92.3
¹³C chemical shifts	26	24	92.3

Keywords calcium-binding, Calmodulin, calmoduin, calcium, calmodulin

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Found 1 Document (1.39 seconds)

BMRB: 7190

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. CaM2/3, : 2 : 114 : 21 : 1 : 181 entities Detail

Interaction partners 1. CaM2/3, : 3 interactors Detail

Experiments performed 6 experiments Detail

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Chemical shift validation 4 contents Detail