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Found 1 Document (1.531 seconds)

BMRB: 4099

The Ca2+-Dependent Interaction of S100B(bb)with a Peptide Derived from p53

Authors

Rustandi, R.R., Drohat, A.C., Baldisseri, D.M., Wilder, P.T., Weber, D.J.

Assembly

S100B-Ca(2+)-p53 peptide complex

Entity

1. S100B beta (polymer), 91 monomers, 10612.73 × 2 Da Detail

SELEKAMVAL IDVFHQYSGR EGDKHKLKKS ELKELINNEL SHFLEEIKEQ EVVDKVMETL DEDGDGECDF QEFMAFVSMV TTACHEFFEH E

2. p53 (polymer), 22 monomers, 3687.789 × 2 Da Detail

XHLKSKKGQS TSRHKKLMFK TX

3. CALCIUM ION (non-polymer), 40.078 × 2 Da

Total weight

28681.195 Da

Max. entity weight

10612.73 Da

Source organism

Rattus norvegicus

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete1

Sequence coverage: 81.4 %, Completeness: 72.2 %, Completeness (bb): 71.2 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	72.2 % (968 of 1340)	76.5 % (537 of 702)	64.7 % (337 of 521)	80.3 % (94 of 117)
Backbone	71.2 % (474 of 666)	78.9 % (179 of 227)	62.8 % (206 of 328)	80.2 % (89 of 111)
Sidechain	74.6 % (582 of 780)	75.4 % (358 of 475)	73.2 % (219 of 299)	83.3 % (5 of 6)
Aromatic	59.5 % (69 of 116)	70.7 % (41 of 58)	48.3 % (28 of 58)
Methyl	87.8 % (86 of 98)	87.8 % (43 of 49)	87.8 % (43 of 49)

1. S100B beta

SELEKAMVAL IDVFHQYSGR EGDKHKLKKS ELKELINNEL SHFLEEIKEQ EVVDKVMETL DEDGDGECDF QEFMAFVSMV TTACHEFFEH E

2. p53

XHLKSKKGQS TSRHKKLMFK TX

Show sample condition

Sample #1

Temperature 310 K, pH 6.5

#	Name	Concentration
1	S100B beta	3.0 ~ 3.3 mM
2	p53	4.8 ~ 5.3 mM
3	EDTA	0.1 mM
4	NaN3	.34 mM
5	DTT	5 mM
6	NaCl	17 mM
7	Tris-HCl-d11	10 mM
8	D2O	10 %
9	CaCl2	6.3 mM

Sample #2

Temperature 310 K, pH 6.5

#	Name	Isotope labeling	Concentration
10	S100B beta	[U-15N]	3.0 ~ 3.3 mM
11	p53		4.8 ~ 5.3 mM
12	EDTA		0.1 mM
13	NaN3		.34 mM
14	DTT		5 mM
15	NaCl		17 mM
16	Tris-HCl-d11		10 mM
17	D2O		10 %
18	CaCl2		6.3 mM

Sample #3

Temperature 310 K, pH 6.5

#	Name	Isotope labeling	Concentration
19	S100B beta	[U-13C;U-15N]	3.0 ~ 3.3 mM
20	p53		4.8 ~ 5.3 mM
21	EDTA		0.1 mM
22	NaN3		.34 mM
23	DTT		5 mM
24	NaCl		17 mM
25	Tris-HCl-d11		10 mM
26	D2O		10 %
27	CaCl2		6.3 mM

Chem. Shift Complete2

Sequence coverage: 81.4 %, Completeness: 71.5 %, Completeness (bb): 70.6 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	71.5 % (1916 of 2680)	76.8 % (1078 of 1404)	62.4 % (650 of 1042)	80.3 % (188 of 234)
Backbone	70.6 % (941 of 1332)	80.0 % (363 of 454)	61.0 % (400 of 656)	80.2 % (178 of 222)
Sidechain	73.7 % (1150 of 1560)	75.3 % (715 of 950)	71.1 % (425 of 598)	83.3 % (10 of 12)
Aromatic	56.0 % (130 of 232)	70.7 % (82 of 116)	41.4 % (48 of 116)
Methyl	87.8 % (172 of 196)	87.8 % (86 of 98)	87.8 % (86 of 98)

1. S100B beta

SELEKAMVAL IDVFHQYSGR EGDKHKLKKS ELKELINNEL SHFLEEIKEQ EVVDKVMETL DEDGDGECDF QEFMAFVSMV TTACHEFFEH E

2. p53

XHLKSKKGQS TSRHKKLMFK TX

Show sample condition

Sample #1

Temperature 310 K, pH 6.5

#	Name	Concentration
1	S100B beta	3.0 ~ 3.3 mM
2	p53	4.8 ~ 5.3 mM
3	EDTA	0.1 mM
4	NaN3	.34 mM
5	DTT	5 mM
6	NaCl	17 mM
7	Tris-HCl-d11	10 mM
8	D2O	10 %
9	CaCl2	6.3 mM

Sample #2

Temperature 310 K, pH 6.5

#	Name	Isotope labeling	Concentration
10	S100B beta	[U-15N]	3.0 ~ 3.3 mM
11	p53		4.8 ~ 5.3 mM
12	EDTA		0.1 mM
13	NaN3		.34 mM
14	DTT		5 mM
15	NaCl		17 mM
16	Tris-HCl-d11		10 mM
17	D2O		10 %
18	CaCl2		6.3 mM

Sample #3

Temperature 310 K, pH 6.5

#	Name	Isotope labeling	Concentration
19	S100B beta	[U-13C;U-15N]	3.0 ~ 3.3 mM
20	p53		4.8 ~ 5.3 mM
21	EDTA		0.1 mM
22	NaN3		.34 mM
23	DTT		5 mM
24	NaCl		17 mM
25	Tris-HCl-d11		10 mM
26	D2O		10 %
27	CaCl2		6.3 mM

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	TSP	methyl	external	indirect	0.2514495
¹H	TSP	methyl	external	direct	0.0
¹⁵N	TSP	methyl	external	indirect	0.101329

Referencing offset: -0.3 ppm, Outliers: 3 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	TSP	methyl	external	indirect	0.2514495
¹H	TSP	methyl	external	direct	0.0
¹⁵N	TSP	methyl	external	indirect	0.101329

Referencing offset: -0.3 ppm, Outliers: 3 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	TSP	methyl	external	indirect	0.2514495
¹H	TSP	methyl	external	direct	0.0
¹⁵N	TSP	methyl	external	indirect	0.101329

Referencing offset: -0.03 ppm, Outliers: 2 Detail

Release date

1998-08-11

Citation

Calcium-binding properties of wild-type and EF-hand mutants of S100B in the presence and absence of a peptide derived from the C-terminal negative regulatory domain of p53
Rustandi, R.R., Drohat, A.C., Baldisseri, D.M., Wilder, P.T., Weber, D.J.
Biochemistry (2005), 44, 7305-7314, PubMed 15882069 , DOI 10.1021/bi050321t , Abstract

Related entities 1. S100B beta, : 1 : 1 : 80 entities Detail

Related entities 2. p53, : 1 : 1 entities Detail

Experiments performed 1 experiments Detail

Chemical shift validation 6 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr4099_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: bmr4099_3.str

#	Content subtype	Saveframe	Status	# of rows	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_one	Warning	1027	100.0 (chain: 1, length: 91)
2	Assigned chemical shifts	assigned_chemical_shifts_two	Warning	1027	100.0 (chain: 1, length: 91)
1	Chemical shift references	chemical_shift_reference_one	Warning	3	No information

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_one
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 91, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 637
  - ¹³C chemical shifts: 297
  - ¹⁵N chemical shifts: 93
- Completeness of assignments
  - Entity_assemble_ID: 1
- Redox state of CYS
- 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
Saveframe: assigned_chemical_shifts_two
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 91, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 637
  - ¹³C chemical shifts: 297
  - ¹⁵N chemical shifts: 93
- Completeness of assignments
  - Entity_assemble_ID: 1
- Redox state of CYS
- 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

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	560	543	97.0
¹³C chemical shifts	422	297	70.4
¹⁵N chemical shifts	97	93	95.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	186	182	97.8
¹³C chemical shifts	182	90	49.5
¹⁵N chemical shifts	91	88	96.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	374	361	96.5
¹³C chemical shifts	240	207	86.3
¹⁵N chemical shifts	6	5	83.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	47	47	100.0
¹³C chemical shifts	47	47	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	49	41	83.7
¹³C chemical shifts	49	20	40.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	560	543	97.0
¹³C chemical shifts	422	297	70.4
¹⁵N chemical shifts	97	93	95.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	186	182	97.8
¹³C chemical shifts	182	90	49.5
¹⁵N chemical shifts	91	88	96.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	374	361	96.5
¹³C chemical shifts	240	207	86.3
¹⁵N chemical shifts	6	5	83.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	47	47	100.0
¹³C chemical shifts	47	47	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	49	41	83.7
¹³C chemical shifts	49	20	40.8

Keywords NMR, nuclear magnetic resonance, S100B(bb), S100 family

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Found 1 Document (1.531 seconds)

BMRB: 4099

Sample #1

Sample #2

Sample #3

Sample #1

Sample #2

Sample #3

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. S100B beta, : 1 : 1 : 80 entities Detail

Related entities 2. p53, : 1 : 1 entities Detail

Experiments performed 1 experiments Detail

Instrument

Sample #1

Sample #2

Sample #3

Chemical shift validation 6 contents Detail