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BMRB: 26802

5O6F

Cold Shock Protein A

Authors

Caruso, I.P., Panwalkar, V., Arni, R.K., Cornelio, M.L.

Assembly

Cold Shock Protein A

Entity

1. Cold Shock Protein A (polymer, Thiol state: not present), 82 monomers, 9116.809 Da Detail

MAQGTVKWFN AEKGFGFIAP DDGSADVFVH YSEIQGNGFR TLEENQKVEF EIGEGAKGPQ AQQVHALGGE NLYFQGHHHH HH

Formula weight

9116.809 Da

Source organism

Corynebacterium pseudotuberculosis

Exptl. method

Refine. method

semi-autometed noe assignment, simulated annealing

Data set

assigned_chemical_shifts, spectral_peak_list

Chem. Shift Complete

Sequence coverage: 91.5 %, Completeness: 88.0 %, Completeness (bb): 90.8 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	88.0 % (829 of 942)	88.9 % (433 of 487)	85.7 % (311 of 363)	92.4 % (85 of 92)
Backbone	90.8 % (443 of 488)	92.0 % (160 of 174)	89.7 % (210 of 234)	91.3 % (73 of 80)
Sidechain	85.7 % (449 of 524)	87.2 % (273 of 313)	82.4 % (164 of 199)	100.0 % (12 of 12)
Aromatic	63.1 % (82 of 130)	66.2 % (43 of 65)	59.4 % (38 of 64)	100.0 % (1 of 1)
Methyl	100.0 % (62 of 62)	100.0 % (31 of 31)	100.0 % (31 of 31)

1. Molecule 1

MAQGTVKWFN AEKGFGFIAP DDGSADVFVH YSEIQGNGFR TLEENQKVEF EIGEGAKGPQ AQQVHALGGE NLYFQGHHHH HH

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1.000 atm, Temperature 298.000 K, pH 6.500, Details 0.8 mM

#	Name	Isotope labeling	Type	Concentration
1	Molecule 1	[U-13C; U-15N]		0.8 mM
2	K2HPO4	natural abundance		50.0 mM
3	NaCl	natural abundance		50.0 mM
4	DSS	natural abundance		0.1 mM
5	H2O	natural abundance		90 %
6	D2O	natural abundance		10 %

LACS Plot; CA

Referencing offset: -0.1 ppm, Outliers: 1 Detail

LACS Plot; CB

Referencing offset: -0.1 ppm, Outliers: 1 Detail

LACS Plot; HA

Referencing offset: 0.06 ppm, Outliers: 2 Detail

LACS Plot; CO

Referencing offset: 0.43 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 15 models in PDB: 5O6F, Strand ID: A Detail

Release date

2016-05-16

Citation

Structure and interaction of Corynebacterium pseudotuberculosis cold shock protein A with Y-box single-stranded DNA fragment
Caruso, I.P., Panwalkar, V., Coronado, M.A., Dingley, A.J., Cornelio, M.L., Willbold, D., Arni, R.K., Eberle, R.J.
FEBS J. (2017), 285, 372-390, PubMed 29197185 , DOI 10.1111/febs.14350 , Abstract

Related entities 1. Cold Shock Protein A, : 1 : 117 entities Detail

Experiments performed 6 experiments Detail

1 2D 1H-15N HSQC/HMQC

Instrument

Varian VNMRS - 900 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1.000 atm, Temperature 298.000 K, pH 6.500, Details 0.8 mM

#	Name	Isotope labeling	Type	Concentration
1	Molecule 1	[U-13C; U-15N]		0.8 mM
2	K2HPO4	natural abundance		50.0 mM
3	NaCl	natural abundance		50.0 mM
4	DSS	natural abundance		0.1 mM
5	H2O	natural abundance		90 %
6	D2O	natural abundance		10 %

2 2D 1H-13C HSQC/HMQC

Instrument

Bruker Avance - na MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1.000 atm, Temperature 298.000 K, pH 6.500, Details 0.8 mM

#	Name	Isotope labeling	Type	Concentration
1	Molecule 1	[U-13C; U-15N]		0.8 mM
2	K2HPO4	natural abundance		50.0 mM
3	NaCl	natural abundance		50.0 mM
4	DSS	natural abundance		0.1 mM
5	H2O	natural abundance		90 %
6	D2O	natural abundance		10 %

3 hbcbcgcdhd (hbCBcgcdHD)

Instrument

Varian VNMRS - 900 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1.000 atm, Temperature 298.000 K, pH 6.500, Details 0.8 mM

#	Name	Isotope labeling	Type	Concentration
1	Molecule 1	[U-13C; U-15N]		0.8 mM
2	K2HPO4	natural abundance		50.0 mM
3	NaCl	natural abundance		50.0 mM
4	DSS	natural abundance		0.1 mM
5	H2O	natural abundance		90 %
6	D2O	natural abundance		10 %

4 hbcbcgcdcehe (hbCBcgcdceHE)

Instrument

Varian VNMRS - 900 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1.000 atm, Temperature 298.000 K, pH 6.500, Details 0.8 mM

#	Name	Isotope labeling	Type	Concentration
1	Molecule 1	[U-13C; U-15N]		0.8 mM
2	K2HPO4	natural abundance		50.0 mM
3	NaCl	natural abundance		50.0 mM
4	DSS	natural abundance		0.1 mM
5	H2O	natural abundance		90 %
6	D2O	natural abundance		10 %

5 3D 1H-13C NOESY

Instrument

Varian VNMRS - 900 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1.000 atm, Temperature 298.000 K, pH 6.500, Details 0.8 mM

#	Name	Isotope labeling	Type	Concentration
1	Molecule 1	[U-13C; U-15N]		0.8 mM
2	K2HPO4	natural abundance		50.0 mM
3	NaCl	natural abundance		50.0 mM
4	DSS	natural abundance		0.1 mM
5	H2O	natural abundance		90 %
6	D2O	natural abundance		10 %

6 3D HNCO

Instrument

Bruker Avance - na MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1.000 atm, Temperature 298.000 K, pH 6.500, Details 0.8 mM

#	Name	Isotope labeling	Type	Concentration
1	Molecule 1	[U-13C; U-15N]		0.8 mM
2	K2HPO4	natural abundance		50.0 mM
3	NaCl	natural abundance		50.0 mM
4	DSS	natural abundance		0.1 mM
5	H2O	natural abundance		90 %
6	D2O	natural abundance		10 %

NMR combined restraints 2 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts	combined_26802_5o6f.nef
Input source #2: Coordindates	5o6f.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	Error

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--
MAQGTVKWFNAEKGFGFIAPDDGSADVFVHYSEIQGNGFRTLEENQKVEFEIGEGAKGPQAQQVHALGGENLYFQGHHHHHH
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MAQGTVKWFNAEKGFGFIAPDDGSADVFVHYSEIQGNGFRTLEENQKVEFEIGEGAKGPQAQQVHALGGENLYFQGHHHHHH

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	82	0	0	100.0

Content subtype: combined_26802_5o6f.nef

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list	Warning	838		91.5 (chain: A, length: 82)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 82, Sequence coverage: 91.5%
- Total number of assignments
  - ¹H chemical shifts: 432
  - ¹³C chemical shifts: 322
  - ¹⁵N chemical shifts: 84
- Completeness of assignments
  - Entity_assemble_ID: A
- Peptide bond of PRO
- Tautomeric state of HIS
- 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

Keywords Cold shock protein, NMR, Protein Structure, Protein dynamics