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Found 1 Document (5.443 seconds)

BMRB: 6702

4B0A

Resonance assignments of 30 kDa complexes of TFIID subunit TAF1 with TATA-binding protein

Authors

Mal, T.K., Liu, D., Masutomi, Y., Zheng, L., Nakatani, Y., Kokubo, T., Ikura, M.

Assembly

yeast TBP associated factor 1 (yTAF1)

Entity

1. yTAF1 (polymer, Thiol state: not present), 64 monomers, 6974.984 Da Detail

TNLANEDEAY EAIFGGEFGS LEIGSYIGGD EGANSKDYTE HLPDAVDFED EDELADDDDD LPEE

2. yTBPc (polymer, Thiol state: all free), 192 monomers, 21279.69 Da Detail

AAPESEKDTS ATSGIVPTLQ NIVATVTLGC RLDLKTVALH ARNAEYNPKR FAAVIMRIRE PKTTALIFAS GKMVVTGAKS EDDSKLASRK YARIIQKIGF AAKFTDFKIQ NIVGSCDVKF PIRLEGLAFS HGTFSSYEPE LFPGLIYRMV KPKIVLLIFV SGKIVLTGAK QREEIYQAFE AIYPVLSEFR KM

Total weight

28254.674 Da

Max. entity weight

21279.69 Da

Source organism

Saccharomyces cerevisiae

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 94.9 %, Completeness: 36.6 %, Completeness (bb): 64.7 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	36.6 % (1079 of 2945)	22.2 % (338 of 1522)	43.5 % (507 of 1166)	91.1 % (234 of 257)
Backbone	64.7 % (980 of 1514)	50.1 % (260 of 519)	64.8 % (486 of 750)	95.5 % (234 of 245)
Sidechain	19.4 % (323 of 1669)	7.8 % (78 of 1003)	37.5 % (245 of 654)	0.0 % (0 of 12)
Aromatic	2.6 % (6 of 234)	4.3 % (5 of 117)	0.9 % (1 of 117)
Methyl	14.3 % (43 of 300)	7.3 % (11 of 150)	21.3 % (32 of 150)

1. yTAF1

TNLANEDEAY EAIFGGEFGS LEIGSYIGGD EGANSKDYTE HLPDAVDFED EDELADDDDD LPEE

2. yTBPc

Show sample condition

Sample

Temperature 298 (±0.1) K, pH 7.5 (±0.2)

#	Name	Concentration
1	yTAF1	0.0 ~ 0.0 mM
2	yTBPc	0.0 ~ 0.0 mM
3	Tris buffer	20 mM

Release date

2006-11-05

Citation

Resonance assignments of 30 kDa complexes of TFIID subunit TAF1 with TATA-binding protein
Mal, T.K., Liu, D., Masutomi, Y., Zheng, L., Nakatani, Y., Kokubo, T., Ikura, M.
J. Biomol. NMR (2005), 33, 76-76, PubMed 16222567 , DOI 10.1007/s10858-005-1929-3 , Abstract

Entries sharing articles BMRB: 1 entries Detail

BMRB: 6700 released on 2005-10-27
Title Resonance Assignments of 30 kDa complexes of TFIID subunit TAF1 with TATA-binding protein

Related entities 1. yTAF1, : 1 : 2 : 1 entities Detail

Related entities 2. yTBPc, : 9 : 136 entities Detail

Interaction partners 1. yTAF1, : 49 : 1 interactors Detail

More details for 50 interactors identified by 7 citations

Interaction partners 2. yTBPc, : 74 interactors Detail

More details for 74 interactors identified by 21 citations

Experiments performed 4 experiments Detail

Chemical shift validation 4 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr6702_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: bmr6702_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	ytafc-STARch.txt	Warning	926		87.5 (chain: 1, length: 64), 95.8 (chain: 2, length: 192)
1	Chemical shift references	chemical_shift_referencing	OK	3		No information

Assigned chemical shifts

Saveframe: ytafc-STARch.txt
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 64, Sequence coverage: 87.5%
  - Entity_assembly_ID: 2, Chain length: 192, Sequence coverage: 95.8%
- Total number of assignments
  - ¹H chemical shifts: 232
  - ¹³C chemical shifts: 462
  - ¹⁵N chemical shifts: 232
- Completeness of assignments
  - Entity_assemble_ID: 1
  - Entity_assemble_ID: 2
- Redox state of CYS
- Peptide bond of PRO
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1
  - Chain_ID: 2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	339	56	16.5
¹³C chemical shifts	261	105	40.2
¹⁵N chemical shifts	65	56	86.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	133	56	42.1
¹³C chemical shifts	128	56	43.8
¹⁵N chemical shifts	62	56	90.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	206	0	0.0
¹³C chemical shifts	133	49	36.8
¹⁵N chemical shifts	3	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	26	0	0.0
¹³C chemical shifts	26	6	23.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	29	0	0.0
¹³C chemical shifts	29	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	1183	176	14.9
¹³C chemical shifts	905	357	39.4
¹⁵N chemical shifts	203	176	86.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	386	176	45.6
¹³C chemical shifts	384	184	47.9
¹⁵N chemical shifts	183	176	96.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	797	0	0.0
¹³C chemical shifts	521	173	33.2
¹⁵N chemical shifts	20	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	128	0	0.0
¹³C chemical shifts	128	18	14.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	88	0	0.0
¹³C chemical shifts	88	0	0.0

Keywords NMR, TBP

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Found 1 Document (5.443 seconds)

BMRB: 6702

Sample

Entries sharing articles BMRB: 1 entries Detail

Related entities 1. yTAF1, : 1 : 2 : 1 entities Detail

Related entities 2. yTBPc, : 9 : 136 entities Detail

Interaction partners 1. yTAF1, : 49 : 1 interactors Detail

Interaction partners 2. yTBPc, : 74 interactors Detail

Experiments performed 4 experiments Detail

Sample

Sample

Sample

Sample

Chemical shift validation 4 contents Detail