BMRBj - BMREntryMaster

Found 1 Document (1.594 seconds)

BMRB: 4086

7OZT

Tumor Suppressor p16ink4a: Structural Characterization of Wild-Type and Mutant Proteins by NMR and Circular Dichroism

Authors

Tevelev, A., Byeon, I.L., Selby, T., Ericson, K., Kim, H., Kraynov, V., Tsai, M.

Assembly

p16(INK4)/delta 1-8

Entity

1. p16(INK4)/delta 1-8 (polymer, Thiol state: all free), 148 monomers, 15801.66 Da Detail

MEPSADWLAT AAARGRVEEV RALLEAGALP NAPNSYGRRP IQVMMMGSAR VAELLLLHGA EPNCADPATL TRPVHDAARE GFLDTLVVLH RAGARLDVRD AWGRLPVDLA EELGHRDVAR YLRAAAGGTR GSNHARIDAA EGPSDIPD

Formula weight

15801.66 Da

Source organism

Homo sapiens

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 96.6 %, Completeness: 63.8 %, Completeness (bb): 73.8 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	63.8 % (1010 of 1583)	64.7 % (528 of 816)	57.2 % (356 of 622)	86.9 % (126 of 145)
Backbone	73.8 % (641 of 868)	85.3 % (255 of 299)	60.3 % (260 of 431)	91.3 % (126 of 138)
Sidechain	56.1 % (477 of 850)	53.0 % (274 of 517)	62.3 % (203 of 326)	0.0 % (0 of 7)
Aromatic	38.6 % (27 of 70)	77.1 % (27 of 35)	0.0 % (0 of 33)	0.0 % (0 of 2)
Methyl	93.5 % (172 of 184)	91.3 % (84 of 92)	95.7 % (88 of 92)

1. p16(INK4)/delta 1-8

MEPSADWLAT AAARGRVEEV RALLEAGALP NAPNSYGRRP IQVMMMGSAR VAELLLLHGA EPNCADPATL TRPVHDAARE GFLDTLVVLH RAGARLDVRD AWGRLPVDLA EELGHRDVAR YLRAAAGGTR GSNHARIDAA EGPSDIPD

Show sample condition

Sample

Temperature 300 K, pH 7.0

#	Name	Concentration
1	p16(INK4)/delta_1-8	0.2 mM
2	HEPES	4 mM
3	DTT	1 mM
4	EDTA	5 uM
5	D2O	10 %
6	H2O	90 %

LACS Plot; CA

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type
¹³C	DSS	methyl protons	0.0 ppm	na	null
¹H	DSS	methyl protons	0.0 ppm	na	null
¹⁵N	NH4NO3	na	21.6 ppm	external	null

Referencing offset: -0.13 ppm, Outliers: 1 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type
¹³C	DSS	methyl protons	0.0 ppm	na	null
¹H	DSS	methyl protons	0.0 ppm	na	null
¹⁵N	NH4NO3	na	21.6 ppm	external	null

Referencing offset: -0.13 ppm, Outliers: 1 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type
¹³C	DSS	methyl protons	0.0 ppm	na	null
¹H	DSS	methyl protons	0.0 ppm	na	null
¹⁵N	NH4NO3	na	21.6 ppm	external	null

Referencing offset: 0.07 ppm, Outliers: 1 Detail

Release date

1997-12-22

Citation

Tumor suppressor p16INK4A: structural characterization of wild-type and mutant proteins by NMR and circular dichroism
Tevelev, A., Byeon, I.L., Selby, T., Ericson, K., Kim, H., Kraynov, V., Tsai, M.
Biochemistry (1996), 35, 9475-9487, PubMed 8755727 , DOI 10.1021/bi960211+ , Abstract

Related entities 1. p16(INK4)/delta 1-8, : 1 : 5 : 1 : 221 entities Detail

Interaction partners 1. p16(INK4)/delta 1-8, : 47 interactors Detail

More details for 47 interactors identified by 11 citations

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr4086_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: bmr4086_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	chemical_shift_assignments	Warning	1137		95.9 (chain: 1, length: 148)
1	Chemical shift references	chem_shift_reference	OK	2		No information

Assigned chemical shifts

Saveframe: chemical_shift_assignments
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 148, Sequence coverage: 95.9%
- Total number of assignments
  - ¹³C chemical shifts: 330
  - ¹H chemical shifts: 684
  - ¹⁵N chemical shifts: 123
- Completeness of assignments
  - Entity_assemble_ID: 1
- Redox state of CYS
- Peptide bond of PRO
- 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 (%)
¹³C chemical shifts	622	330	53.1
¹H chemical shifts	816	512	62.7
¹⁵N chemical shifts	162	123	75.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	296	136	45.9
¹H chemical shifts	299	253	84.6
¹⁵N chemical shifts	138	123	89.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	326	194	59.5
¹H chemical shifts	517	259	50.1
¹⁵N chemical shifts	24	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	96	86	89.6
¹H chemical shifts	96	86	89.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	33	0	0.0
¹H chemical shifts	35	27	77.1
¹⁵N chemical shifts	2	0	0.0

Keywords multiple tumor suppressor (MTS1), NMR, Nuclear Magnetic Resonance, p16/delta 1-8

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Found 1 Document (1.594 seconds)

BMRB: 4086

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. p16(INK4)/delta 1-8, : 1 : 5 : 1 : 221 entities Detail

Interaction partners 1. p16(INK4)/delta 1-8, : 47 interactors Detail

Chemical shift validation 3 contents Detail