BMRBj - BMREntryMaster

Found 1 Document (1.575 seconds)

BMRB: 4256

1L3G

1H, 15N and 13C Assignments of the DNA Binding Domain of Transcription Factor Mbp1 from S. cerevisiae in Both Its Free and DNA Bound Forms, and 1H Assignments of the Free DNA

Authors

McIntosh, P.B., Taylor, I.A., Smerdon, S.J., Frenkiel, T.A., Lane, A.N.

Assembly

Mbp1(2-124)

Entity

1. MLU1-BOX binding protein (polymer), 135 monomers, 15298.13 Da Detail

SNQIYSARYS GVDVYEFIHS TGSIMKRKKD DWVNATHILK AANFAKAKRT RILEKEVLKE THEKVQGGFG KYQGTWVPLN IAKQLAEKFS VYDQLKPLFD FTQTDGSASP PPAPKHHHAS KVDKLAAALE HHHHH

2. DNA binding domain of Mbp1 (polymer), 13 monomers, 4029.569 × 2 Da Detail

TTTGACGCGT CAA

Total weight

23357.268 Da

Max. entity weight

15298.13 Da

Source organism

Saccharomyces cerevisiae

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 82.4 %, Completeness: 39.9 %, Completeness (bb): 56.6 % Detail

Polymer type: polypeptide(L) polydeoxyribonucleotide

	Total	¹H	¹³C	¹⁵N
All	39.9 % (693 of 1738)	40.6 % (392 of 966)	29.3 % (185 of 631)	82.3 % (116 of 141)
Backbone	56.6 % (503 of 889)	60.2 % (218 of 362)	42.5 % (169 of 398)	89.9 % (116 of 129)
Sidechain	23.1 % (226 of 977)	28.8 % (174 of 604)	14.4 % (52 of 361)	0.0 % (0 of 12)
Aromatic	3.1 % (6 of 194)	3.6 % (4 of 110)	2.4 % (2 of 82)	0.0 % (0 of 2)
Methyl	29.7 % (41 of 138)	40.8 % (29 of 71)	17.9 % (12 of 67)

1. MLU1-BOX binding protein

SNQIYSARYS GVDVYEFIHS TGSIMKRKKD DWVNATHILK AANFAKAKRT RILEKEVLKE THEKVQGGFG KYQGTWVPLN IAKQLAEKFS VYDQLKPLFD FTQTDGSASP PPAPKHHHAS KVDKLAAALE HHHHH

2. DNA binding domain of Mbp1

TTTGACGCGT CAA

Show sample condition

Sample #1

Temperature 288 (±1) K, pH 7.6 (±0.2), Details Sample 1 is a complex of the DNA binding domain of Mbp1 (residues 2-124) and a 12 base pair DNA duplex (TTTGACGCGTCAA)2 (MBC12T)containing the Mbp1 recognition site Mbp1(124) was expressed in e.coli as a C-terminal hexaHis fusion protein containing a seven-residue linked. For 15N labelled and 15N/13C labelled protein, the growth medium was replaced by M9 minimal medium supplemented with (15NH4)2SO4 (1gL-1) and 12C or 13C6 D-glucose (1gL-1) as the sole nitrogen and carbon sources.

#	Name	Isotope labeling	Concentration
1	MLU1-BOX binding protein	[U-15N; U-13C]	0.8 mM
2	DNA binding domain of Mbp1		1.0 ~ 1.68 mM
3	Na phosphate		40 mM
4	NaCl		110 mM
5	D2O		10 %
6	H2O		90 %

Sample #2

Temperature 288 (±1) K, pH 7.6 (±0.2), Details Sample 2 is a complex of the DNA binding domain of Mbp1 (residues 2-124) and a 12 base pair DNA duplex (TTTGACGCGTCAA)2 (MBC12T)containing the Mbp1 recognition site Mbp1(124) was expressed in e.coli as a C-terminal hexaHis fusion protein containing a seven-residue linked. For 15N labelled and 15N/13C labelled protein, the growth medium was replaced by M9 minimal medium supplemented with (15NH4)2SO4 (1gL-1) and 12C or 13C6 D-glucose (1gL-1) as the sole nitrogen and carbon sources.

#	Name	Concentration
7	MLU1-BOX binding protein	0.5 mM
8	DNA binding domain of Mbp1	1.0 ~ 1.68 mM
9	Na phosphate	40 mM
10	NaCl	110 mM
11	D2O	10 %
12	H2O	90 %

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	null	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: 0.19 ppm, Outliers: 2 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	null	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: 0.19 ppm, Outliers: 2 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	null	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: 0.04 ppm, Outliers: 1 Detail

Release date

1999-11-22

Citation 1

1H, 15N and 13C Assignments of the DNA Binding Domain of Transcription Factor Mbp1 from S. cerevisiae in Both Its Free and DNA Bound Forms, and 1H Assignments of the Free DNA
McIntosh, P.B., Taylor, I.A., Smerdon, S.J., Frenkiel, T.A., Lane, A.N.
J. Biomol. NMR (1999), 13, 397-398

Show more 2 citaions

Citation 2

1H, 13C and 15N chemical shift referencing in biomolecular NMR
Wishart, D.S., Bigam, C.G., Yao, J., Abildgaard, F., Dyson, H.J., Oldfield, E., Markley, J.L., Sykes, B.D.
J. Biomol. NMR (1995), 6, 135-140, PubMed 8589602 , DOI: , Abstract

Citation 3

The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
J. Biomol. NMR (1995), 6, 1-10, PubMed 22911575 , DOI 10.1007/BF00417486 , Abstract

Hide non-primary 2 citaions

Related entities 1. MLU1-BOX binding protein, : 1 : 12 entities Detail

Experiments performed 1 experiments Detail

Chemical shift validation 4 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr4256_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: bmr4256_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts	Warning	690		89.6 (chain: 1, length: 135)
1	Chemical shift references	chemical_shift_reference_one	OK	3		No information

Assigned chemical shifts

Saveframe: assigned_chemical_shifts
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 135, Sequence coverage: 89.6%
- Total number of assignments
  - ¹³C chemical shifts: 156
  - ¹H chemical shifts: 419
  - ¹⁵N chemical shifts: 115
- Completeness of assignments
  - Entity_assemble_ID: 1
- 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	631	156	24.7
¹H chemical shifts	839	363	43.3
¹⁵N chemical shifts	145	115	79.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	270	121	44.8
¹H chemical shifts	271	214	79.0
¹⁵N chemical shifts	129	115	89.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	361	35	9.7
¹H chemical shifts	568	149	26.2
¹⁵N chemical shifts	16	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	68	11	16.2
¹H chemical shifts	68	28	41.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	82	0	0.0
¹H chemical shifts	84	0	0.0
¹⁵N chemical shifts	2	0	0.0

Keywords cell_cycle, MBp1, NMR assignments

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Found 1 Document (1.575 seconds)

BMRB: 4256

Sample #1

Sample #2

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. MLU1-BOX binding protein, : 1 : 12 entities Detail

Experiments performed 1 experiments Detail

Sample #1

Sample #2

Chemical shift validation 4 contents Detail