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BMRB: 15403

2JYS

Simian Foamy Virus (mac) protease structure

Authors

Hartl, M., Schweimer, K., Woehrl, B.

Assembly

SFVmac Pol 1-101 6His

Entity

1. SFVmac Pol 1-101 6His (polymer, Thiol state: all free), 107 monomers, 12390.16 Da Detail

MDPLQLLQPL EAEIKGTKLK AHWDSGATIT CVPEAFLEDE RPIQTMLIKT IHGEKQQDVY YLTFKVQGRK VEAEVLASPY DYILLNPSDV PWLMKKPLQL THHHHHH

Formula weight

12390.16 Da

Source organism

Simian foamy virus

Exptl. method

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 92.5 %, Completeness: 86.3 %, Completeness (bb): 89.5 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	86.3 % (1127 of 1306)	85.3 % (581 of 681)	87.2 % (450 of 516)	88.1 % (96 of 109)
Backbone	89.5 % (560 of 626)	89.0 % (187 of 210)	89.3 % (283 of 317)	90.9 % (90 of 99)
Sidechain	84.4 % (661 of 783)	83.7 % (394 of 471)	86.4 % (261 of 302)	60.0 % (6 of 10)
Aromatic	75.9 % (82 of 108)	77.8 % (42 of 54)	73.1 % (38 of 52)	100.0 % (2 of 2)
Methyl	93.8 % (122 of 130)	95.4 % (62 of 65)	92.3 % (60 of 65)

1. SFVmac Pol 1-101 6His

MDPLQLLQPL EAEIKGTKLK AHWDSGATIT CVPEAFLEDE RPIQTMLIKT IHGEKQQDVY YLTFKVQGRK VEAEVLASPY DYILLNPSDV PWLMKKPLQL THHHHHH

Show sample condition

Sample

Pressure 1 atm, Temperature 298 K, pH 7.4

#	Name	Isotope labeling	Type	Concentration
1	SFVmac Pol 1-101 6His	[U-100% 13C; U-100% 15N]		1 mM
2	phosphate buffer 7.4			50 mM
3	NaCl			100 mM
4	DTT			0.0 ~ 0.0 mM

LACS Plot; CA

Referencing offset: 0.03 ppm, Outliers: 1 Detail

LACS Plot; CB

Referencing offset: 0.03 ppm, Outliers: 1 Detail

LACS Plot; HA

Referencing offset: -0.08 ppm, Outliers: 3 Detail

LACS Plot; CO

Referencing offset: 0.67 ppm, Outliers: 1 Detail

Release date

2007-09-23

Citation

Sequence-specific (1)H, (13)C and (15)N resonance assignments and secondary structure of a truncated protease from Simian Foamy Virus
Hartl, M.J., Wohrl, B.M., Schweimer, K.
Biomol. NMR Assign. (2007), 1, 175-177, PubMed 19636858 , DOI 10.1007/s12104-007-9048-6 , Abstract

Related entities 1. SFVmac Pol 1-101 6His, : 1 : 1 : 9 entities Detail

Experiments performed 9 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker Avance - 700 MHz equipped with CryoProbe

Sample

State isotropic, Pressure 1 atm, Temperature 298 K, pH 7.4

#	Name	Isotope labeling	Type	Concentration
1	SFVmac Pol 1-101 6His	[U-100% 13C; U-100% 15N]		1 mM
2	phosphate buffer 7.4			50 mM
3	NaCl			100 mM
4	DTT			0.0 ~ 0.0 mM

2 3D HNCO

Instrument

Bruker Avance - 700 MHz equipped with CryoProbe

Sample

State isotropic, Pressure 1 atm, Temperature 298 K, pH 7.4

#	Name	Isotope labeling	Type	Concentration
1	SFVmac Pol 1-101 6His	[U-100% 13C; U-100% 15N]		1 mM
2	phosphate buffer 7.4			50 mM
3	NaCl			100 mM
4	DTT			0.0 ~ 0.0 mM

3 3D HNCA

Instrument

Bruker Avance - 700 MHz equipped with CryoProbe

Sample

State isotropic, Pressure 1 atm, Temperature 298 K, pH 7.4

#	Name	Isotope labeling	Type	Concentration
1	SFVmac Pol 1-101 6His	[U-100% 13C; U-100% 15N]		1 mM
2	phosphate buffer 7.4			50 mM
3	NaCl			100 mM
4	DTT			0.0 ~ 0.0 mM

4 3D HNCACB

Instrument

Bruker Avance - 700 MHz equipped with CryoProbe

Sample

State isotropic, Pressure 1 atm, Temperature 298 K, pH 7.4

#	Name	Isotope labeling	Type	Concentration
1	SFVmac Pol 1-101 6His	[U-100% 13C; U-100% 15N]		1 mM
2	phosphate buffer 7.4			50 mM
3	NaCl			100 mM
4	DTT			0.0 ~ 0.0 mM

5 3D CBCA(CO)NH

Instrument

Bruker Avance - 700 MHz equipped with CryoProbe

Sample

State isotropic, Pressure 1 atm, Temperature 298 K, pH 7.4

#	Name	Isotope labeling	Type	Concentration
1	SFVmac Pol 1-101 6His	[U-100% 13C; U-100% 15N]		1 mM
2	phosphate buffer 7.4			50 mM
3	NaCl			100 mM
4	DTT			0.0 ~ 0.0 mM

6 3D C(CO)NH

Instrument

Bruker Avance - 700 MHz equipped with CryoProbe

Sample

State isotropic, Pressure 1 atm, Temperature 298 K, pH 7.4

#	Name	Isotope labeling	Type	Concentration
1	SFVmac Pol 1-101 6His	[U-100% 13C; U-100% 15N]		1 mM
2	phosphate buffer 7.4			50 mM
3	NaCl			100 mM
4	DTT			0.0 ~ 0.0 mM

7 2D 1H-13C HSQC

Instrument

Bruker Avance - 700 MHz equipped with CryoProbe

Sample

State isotropic, Pressure 1 atm, Temperature 298 K, pH 7.4

#	Name	Isotope labeling	Type	Concentration
1	SFVmac Pol 1-101 6His	[U-100% 13C; U-100% 15N]		1 mM
2	phosphate buffer 7.4			50 mM
3	NaCl			100 mM
4	DTT			0.0 ~ 0.0 mM

8 3D HCCH-TOCSY

Instrument

Bruker Avance - 700 MHz equipped with CryoProbe

Sample

State isotropic, Pressure 1 atm, Temperature 298 K, pH 7.4

#	Name	Isotope labeling	Type	Concentration
1	SFVmac Pol 1-101 6His	[U-100% 13C; U-100% 15N]		1 mM
2	phosphate buffer 7.4			50 mM
3	NaCl			100 mM
4	DTT			0.0 ~ 0.0 mM

9 3D HBHA(CO)NH

Instrument

Bruker Avance - 700 MHz equipped with CryoProbe

Sample

State isotropic, Pressure 1 atm, Temperature 298 K, pH 7.4

#	Name	Isotope labeling	Type	Concentration
1	SFVmac Pol 1-101 6His	[U-100% 13C; U-100% 15N]		1 mM
2	phosphate buffer 7.4			50 mM
3	NaCl			100 mM
4	DTT			0.0 ~ 0.0 mM

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr15403_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: bmr15403_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	1234		91.6 (chain: 1, length: 107)
1	Chemical shift references	chemical_shift_reference_1	OK	3		No information

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 107, Sequence coverage: 91.6%
- Total number of assignments
  - ¹H chemical shifts: 698
  - ¹³C chemical shifts: 442
  - ¹⁵N chemical shifts: 94
- Completeness of assignments
  - Entity_assemble_ID: 1
- Redox state of CYS
- 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: 1