BMRBj - BMREntryMaster

Found 1 Document (1.252 seconds)

BMRB: 4321

5GCN

1H, 13C, and 15N Chemical Shift Assignments for the Catalytic Domain of Tetrahymena GCN5 Histone Acetyltransferase in Complex with CoA

Authors

Lin, Y., Wagner, G.

Assembly

p55 monomer in complex with CoA

Entity

1. Tetrahymena histone acetyltransferase (polymer, Thiol state: all free), 166 monomers, 19698.71 Da Detail

MKGLLDFDIL TNDGTHRNMK LLIDLKNIFS RQLPKMPKEY IVKLVFDRHH ESMVILKNKQ KVIGGICFRQ YKPQRFAEVA FLAVTANEQV RGYGTRLMNK FKDHMQKQNI EYLLTYADNF AIGYFKKQGF TKEHRMPQEK WKGYIKDYDG GTLMECYIHP YVDYGN

2. COENZYME A (non-polymer), 767.534 Da

Total weight

20466.244 Da

Max. entity weight

19698.71 Da

Source organism

Tetrahymena thermophila

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 98.8 %, Completeness: 89.4 %, Completeness (bb): 96.8 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	89.4 % (1872 of 2095)	92.9 % (1026 of 1104)	82.9 % (672 of 811)	96.7 % (174 of 180)
Backbone	96.8 % (954 of 986)	97.3 % (330 of 339)	96.5 % (469 of 486)	96.3 % (155 of 161)
Sidechain	84.5 % (1067 of 1263)	91.0 % (696 of 765)	73.5 % (352 of 479)	100.0 % (19 of 19)
Aromatic	40.2 % (90 of 224)	77.7 % (87 of 112)	1.8 % (2 of 111)	100.0 % (1 of 1)
Methyl	100.0 % (158 of 158)	100.0 % (79 of 79)	100.0 % (79 of 79)

1. Tetrahymena histone acetyltransferase

MKGLLDFDIL TNDGTHRNMK LLIDLKNIFS RQLPKMPKEY IVKLVFDRHH ESMVILKNKQ KVIGGICFRQ YKPQRFAEVA FLAVTANEQV RGYGTRLMNK FKDHMQKQNI EYLLTYADNF AIGYFKKQGF TKEHRMPQEK WKGYIKDYDG GTLMECYIHP YVDYGN

Show sample condition

Sample

Temperature 300 (±1) K, pH 6.5 (±0.1)

#	Name	Concentration
1	Tetrahymena histone acetyltransferase	0.4 mM
2	coenzyme A	0.8 mM
3	sodium phosphate	50 mM
4	NaCl	100 mM
5	DTT	0.1 mM
6	NaN3	0.1 mM
7	EDTA	0.1 mM

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: -0.1 ppm, Outliers: 4 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: -0.1 ppm, Outliers: 4 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: -0.04 ppm, Outliers: 2 Detail

LACS Plot; CO

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: 1.21 ppm, Outliers: 1 Detail

Release date

2000-12-13

Citation

Efficient side-chain and backbone assignment in large proteins: application to tGCN5
Lin, Y., Wagner, G.
J. Biomol. NMR (1999), 15, 227-239, PubMed 10677826 , DOI: , Abstract

Related entities 1. Tetrahymena histone acetyltransferase, : 1 : 8 : 50 entities Detail

Experiments performed 1 experiments Detail

Chemical shift validation 4 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr4321_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: bmr4321_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts	Warning	2040		98.8 (chain: 1, length: 166)
1	Chemical shift references	chemical_shift_reference	OK	3		No information

Assigned chemical shifts

Saveframe: assigned_chemical_shifts
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 166, Sequence coverage: 98.8%
- Total number of assignments
  - ¹³C chemical shifts: 668
  - ¹H chemical shifts: 1197
  - ¹⁵N chemical shifts: 175
- 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

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Found 1 Document (1.252 seconds)

BMRB: 4321

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. Tetrahymena histone acetyltransferase, : 1 : 8 : 50 entities Detail

Experiments performed 1 experiments Detail

Instrument

Sample

Chemical shift validation 4 contents Detail

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	811	668	82.4
¹H chemical shifts	1104	1025	92.8
¹⁵N chemical shifts	188	175	93.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	332	321	96.7
¹H chemical shifts	339	332	97.9
¹⁵N chemical shifts	161	156	96.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	479	347	72.4
¹H chemical shifts	765	693	90.6
¹⁵N chemical shifts	27	19	70.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	111	0	0.0
¹H chemical shifts	112	85	75.9
¹⁵N chemical shifts	1	1	100.0