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BMRB: 17880

2LI6

1H, 13C, and 15N Chemical Shift Assignments for a yeast protein

Authors

Assembly

yeast protein

Entity

1. yeast protein (polymer, Thiol state: unknown), 125 monomers, 14998.12 Da Detail

MQSLNPALQE KISTELNNKQ YELFMKSLIE NCKKRNMPLQ SIPEIGNRKI NLFYLYMLVQ KFGGADQVTR TQQWSMVAQR LQISDYQQLE SIYFRILLPY ERHMISQEGI KETQAKRLEH HHHHH

Formula weight

14998.12 Da

Source organism

Saccharomyces cerevisiae

Exptl. method

Refine. method

DGSA-distance geometry simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 92.8 %, Completeness: 56.9 %, Completeness (bb): 74.5 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	56.9 % (901 of 1584)	55.0 % (462 of 840)	54.6 % (328 of 601)	77.6 % (111 of 143)
Backbone	74.5 % (553 of 742)	84.8 % (212 of 250)	62.0 % (230 of 371)	91.7 % (111 of 121)
Sidechain	47.4 % (456 of 963)	42.4 % (250 of 590)	58.7 % (206 of 351)	0.0 % (0 of 22)
Aromatic	0.0 % (0 of 128)	0.0 % (0 of 64)	0.0 % (0 of 63)	0.0 % (0 of 1)
Methyl	59.7 % (74 of 124)	62.9 % (39 of 62)	56.5 % (35 of 62)

1. yeast protein

MQSLNPALQE KISTELNNKQ YELFMKSLIE NCKKRNMPLQ SIPEIGNRKI NLFYLYMLVQ KFGGADQVTR TQQWSMVAQR LQISDYQQLE SIYFRILLPY ERHMISQEGI KETQAKRLEH HHHHH

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	yeast protein	[U-100% 13C; U-100% 15N]		0.5 mM
2	sodium chloride	natural abundance		100 mM
3	sodium phosphate	natural abundance		2 mM
4	EDTA	natural abundance		1.5 mM
5	H2O	natural abundance		90 %
6	D2O	natural abundance		10 %

LACS Plot; CA

Referencing offset: 0.02 ppm, Outliers: 2 Detail

LACS Plot; CB

Referencing offset: 0.02 ppm, Outliers: 2 Detail

LACS Plot; HA

Referencing offset: 0.06 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 2LI6, Strand ID: A Detail

Release date

2012-04-22

Citation

Solution structure of SWI1 AT-rich interaction domain from Saccharomyces cerevisiae and its nonspecific binding to DNA
Wang, T., Zhang, J., Zhang, X., Tu, X.
Proteins (2012), 80, 1911-1917, PubMed 22488857 , DOI 10.1002/prot.24091 , Abstract

Related entities 1. yeast protein, : 1 : 19 entities Detail

Interaction partners 1. yeast protein, : 27 interactors Detail

More details for 27 interactors identified by 12 citations

Experiments performed 9 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker DMX - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	yeast protein	[U-100% 13C; U-100% 15N]		0.5 mM
2	sodium chloride	natural abundance		100 mM
3	sodium phosphate	natural abundance		2 mM
4	EDTA	natural abundance		1.5 mM
5	H2O	natural abundance		90 %
6	D2O	natural abundance		10 %

2 3D CBCA(CO)NH

Instrument

Bruker DMX - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	yeast protein	[U-100% 13C; U-100% 15N]		0.5 mM
2	sodium chloride	natural abundance		100 mM
3	sodium phosphate	natural abundance		2 mM
4	EDTA	natural abundance		1.5 mM
5	H2O	natural abundance		90 %
6	D2O	natural abundance		10 %

3 3D C(CO)NH

Instrument

Bruker DMX - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	yeast protein	[U-100% 13C; U-100% 15N]		0.5 mM
2	sodium chloride	natural abundance		100 mM
3	sodium phosphate	natural abundance		2 mM
4	EDTA	natural abundance		1.5 mM
5	H2O	natural abundance		90 %
6	D2O	natural abundance		10 %

4 3D HNCACB

Instrument

Bruker DMX - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	yeast protein	[U-100% 13C; U-100% 15N]		0.5 mM
2	sodium chloride	natural abundance		100 mM
3	sodium phosphate	natural abundance		2 mM
4	EDTA	natural abundance		1.5 mM
5	H2O	natural abundance		90 %
6	D2O	natural abundance		10 %

5 3D HBHA(CO)NH

Instrument

Bruker DMX - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	yeast protein	[U-100% 13C; U-100% 15N]		0.5 mM
2	sodium chloride	natural abundance		100 mM
3	sodium phosphate	natural abundance		2 mM
4	EDTA	natural abundance		1.5 mM
5	H2O	natural abundance		90 %
6	D2O	natural abundance		10 %

6 3D H(CCO)NH

Instrument

Bruker DMX - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	yeast protein	[U-100% 13C; U-100% 15N]		0.5 mM
2	sodium chloride	natural abundance		100 mM
3	sodium phosphate	natural abundance		2 mM
4	EDTA	natural abundance		1.5 mM
5	H2O	natural abundance		90 %
6	D2O	natural abundance		10 %

7 2D 1H-13C HSQC

Instrument

Bruker DMX - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	yeast protein	[U-100% 13C; U-100% 15N]		0.5 mM
2	sodium chloride	natural abundance		100 mM
3	sodium phosphate	natural abundance		2 mM
4	EDTA	natural abundance		1.5 mM
5	H2O	natural abundance		90 %
6	D2O	natural abundance		10 %

8 3D 1H-15N NOESY

Instrument

Bruker DMX - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	yeast protein	[U-100% 13C; U-100% 15N]		0.5 mM
2	sodium chloride	natural abundance		100 mM
3	sodium phosphate	natural abundance		2 mM
4	EDTA	natural abundance		1.5 mM
5	H2O	natural abundance		90 %
6	D2O	natural abundance		10 %

9 3D 1H-13C NOESY

Instrument

Bruker DMX - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	yeast protein	[U-100% 13C; U-100% 15N]		0.5 mM
2	sodium chloride	natural abundance		100 mM
3	sodium phosphate	natural abundance		2 mM
4	EDTA	natural abundance		1.5 mM
5	H2O	natural abundance		90 %
6	D2O	natural abundance		10 %

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_17880_2li6.nef
Input source #2: Coordindates	2li6.cif
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

Sequence alignments

Entity_assembly_ID (NMR): A vs Auth_asym_ID (model): A

--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100
QSLNPALQEKISTELNNKQYELFMKSLIENCKKRNMPLQSIPEIGNRKINLFYLYMLVQKFGGADQVTRTQQWSMVAQRLQISDYQQLESIYFRILLPYE
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
QSLNPALQEKISTELNNKQYELFMKSLIENCKKRNMPLQSIPEIGNRKINLFYLYMLVQKFGGADQVTRTQQWSMVAQRLQISDYQQLESIYFRILLPYE

-------110------
RHMISQEGIKETQAKR
||||||||||||||||
RHMISQEGIKETQAKR

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	116	0	0	100.0

Content subtype: combined_17880_2li6.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	840		100.0 (chain: A, length: 116)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	Warning	1517 (1)	noe	99.1 (chain: A, length: 116)
2	Distance restraints	CNS/XPLOR_distance_constraints_3	Warning	28 (1)	hbond	20.7 (chain: A, length: 116)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_4	OK	178 (178)	.	90.5 (chain: A, length: 116)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 116, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 427
  - ¹³C chemical shifts: 303
  - ¹⁵N chemical shifts: 110
- Completeness of assignments
  - Entity_assemble_ID: A
- 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: A

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 116, Sequence coverage: 99.1%
- Total number of restraints: 1516
- Weight of restraints: 1.0 (1516)
- Potential type of restraints: square-well-parabolic (1516)
- Range of distance target values: 2.4, 4.15 (Å)
- Histogram of distance target values
- Histogram of discrepancy in distance target values
- Distance restraints per residue
  - Chain_ID: A
- Distance restraints on contact map
- Saveframe: CNS/XPLOR_distance_constraints_3
  - Status: Warning
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 116, Sequence coverage: 20.7%
  - Total number of restraints: 28
  - Weight of restraints: 1.0 (28)
  - Potential type of restraints: square-well-parabolic (28)
  - Range of distance target values: 2.0, 3.0 (Å)
  - Histogram of distance target values
  - Distance restraints per residue
    - Chain_ID: A
  - Distance restraints on contact map

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_4
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 116, Sequence coverage: 90.5%
- Total number of restraints: 178
- Total number of restraints per polymer type: 178
- Weight of restraints: 1.0 (178)
- Potential type of restraints: square-well-parabolic (178)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A