BMRBj - BMREntryMaster

Found 1 Document (1.242 seconds)

BMRB: 4905

1RKN

1H, 13C and 15N Chemical Shift Assignments for Urea-denatured G88W-110 Fragment of Staphylococcal Nuclease

Authors

Ye, K., Wang, J.

Assembly

G88W110 fragment of staphylococcal nuclease

Entity

1. G88W110 fragment of staphylococcal nuclease (polymer, Thiol state: not present), 110 monomers, 12430.36 Da Detail

ATSTKKLHKE PATLIKAIDG DTVKLMYKGQ PMTFRLLLVD TPETKHPKKG VEKYGPEASA FTKKMVENAK KIEVEFDKGQ RTDKYGRWLA YIYADGKMVN EALVRQGLAK

Formula weight

12430.36 Da

Source organism

Staphylococcus aureus

Exptl. method

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 78.6 %, Completeness (bb): 97.5 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	78.6 % (1046 of 1330)	85.6 % (599 of 700)	66.3 % (344 of 519)	92.8 % (103 of 111)
Backbone	97.5 % (634 of 650)	97.8 % (218 of 223)	97.2 % (313 of 322)	98.1 % (103 of 105)
Sidechain	64.3 % (503 of 782)	78.8 % (376 of 477)	42.5 % (127 of 299)	0.0 % (0 of 6)
Aromatic	0.0 % (0 of 90)	0.0 % (0 of 45)	0.0 % (0 of 44)	0.0 % (0 of 1)
Methyl	60.2 % (71 of 118)	93.2 % (55 of 59)	27.1 % (16 of 59)

1. Staphylococcal Nuclease

ATSTKKLHKE PATLIKAIDG DTVKLMYKGQ PMTFRLLLVD TPETKHPKKG VEKYGPEASA FTKKMVENAK KIEVEFDKGQ RTDKYGRWLA YIYADGKMVN EALVRQGLAK

Show sample condition

Sample

Temperature 305 (±0.1) K, pH 4.9 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Staphylococcal Nuclease	[U-95% 13C; U-90% 15N]		2.5 mM
2	acetate buffer	[U-99% 2H]		50 mM
3	Urea			6 M
4	H2O			90 %
5	D2O			10 %

LACS Plot; CA

Referencing offset: -0.12 ppm, Outliers: 1 Detail

LACS Plot; CB

Referencing offset: -0.12 ppm, Outliers: 1 Detail

LACS Plot; HA

Referencing offset: 0.03 ppm, Outliers: 2 Detail

LACS Plot; CO

Referencing offset: 0.22 ppm, Outliers: 1 Detail

Release date

2001-08-07

Citation

Self-association reaction of denatured staphylococcal nuclease fragments characterized by heteronuclear NMR
Ye, K., Wang, J.
J. Mol. Biol. (2001), 307, 309-322, PubMed 11243822 , DOI 10.1006/jmbi.2000.4449 , Abstract

Related entities 1. G88W110 fragment of staphylococcal nuclease, : 1 : 76 : 41 entities Detail

Experiments performed 10 experiments Detail

1 HNCACB

Instrument

Bruker DMX - 600 MHz

Sample

State isotropic, Temperature 305 (±0.1) K, pH 4.9 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Staphylococcal Nuclease	[U-95% 13C; U-90% 15N]		2.5 mM
2	acetate buffer	[U-99% 2H]		50 mM
3	Urea			6 M
4	H2O			90 %
5	D2O			10 %

2 CBCA(CO)NH

Instrument

Bruker DMX - 600 MHz

Sample

State isotropic, Temperature 305 (±0.1) K, pH 4.9 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Staphylococcal Nuclease	[U-95% 13C; U-90% 15N]		2.5 mM
2	acetate buffer	[U-99% 2H]		50 mM
3	Urea			6 M
4	H2O			90 %
5	D2O			10 %

3 HNCO

Instrument

Bruker DMX - 600 MHz

Sample

State isotropic, Temperature 305 (±0.1) K, pH 4.9 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Staphylococcal Nuclease	[U-95% 13C; U-90% 15N]		2.5 mM
2	acetate buffer	[U-99% 2H]		50 mM
3	Urea			6 M
4	H2O			90 %
5	D2O			10 %

4 HN(CA)CO

Instrument

Bruker DMX - 600 MHz

Sample

State isotropic, Temperature 305 (±0.1) K, pH 4.9 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Staphylococcal Nuclease	[U-95% 13C; U-90% 15N]		2.5 mM
2	acetate buffer	[U-99% 2H]		50 mM
3	Urea			6 M
4	H2O			90 %
5	D2O			10 %

5 H(CCO)NH

Instrument

Bruker DMX - 600 MHz

Sample

State isotropic, Temperature 305 (±0.1) K, pH 4.9 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Staphylococcal Nuclease	[U-95% 13C; U-90% 15N]		2.5 mM
2	acetate buffer	[U-99% 2H]		50 mM
3	Urea			6 M
4	H2O			90 %
5	D2O			10 %

6 3D 1H-15N TOCSY-HSQC

Instrument

Bruker DMX - 600 MHz

Sample

State isotropic, Temperature 305 (±0.1) K, pH 4.9 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Staphylococcal Nuclease	[U-95% 13C; U-90% 15N]		2.5 mM
2	acetate buffer	[U-99% 2H]		50 mM
3	Urea			6 M
4	H2O			90 %
5	D2O			10 %

7 3D 1H-15N NOESY-HSQC

Instrument

Bruker DMX - 600 MHz

Sample

State isotropic, Temperature 305 (±0.1) K, pH 4.9 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Staphylococcal Nuclease	[U-95% 13C; U-90% 15N]		2.5 mM
2	acetate buffer	[U-99% 2H]		50 mM
3	Urea			6 M
4	H2O			90 %
5	D2O			10 %

8 3D 1H-15N/1H-15N HSQC-NOESY-HSQC

Instrument

Bruker DMX - 600 MHz

Sample

State isotropic, Temperature 305 (±0.1) K, pH 4.9 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Staphylococcal Nuclease	[U-95% 13C; U-90% 15N]		2.5 mM
2	acetate buffer	[U-99% 2H]		50 mM
3	Urea			6 M
4	H2O			90 %
5	D2O			10 %

9 HNHA

Instrument

Bruker DMX - 600 MHz

Sample

State isotropic, Temperature 305 (±0.1) K, pH 4.9 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Staphylococcal Nuclease	[U-95% 13C; U-90% 15N]		2.5 mM
2	acetate buffer	[U-99% 2H]		50 mM
3	Urea			6 M
4	H2O			90 %
5	D2O			10 %

10 1H-13C CT-HSQC

Instrument

Bruker DMX - 600 MHz

Sample

State isotropic, Temperature 305 (±0.1) K, pH 4.9 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Staphylococcal Nuclease	[U-95% 13C; U-90% 15N]		2.5 mM
2	acetate buffer	[U-99% 2H]		50 mM
3	Urea			6 M
4	H2O			90 %
5	D2O			10 %

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr4905_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: bmr4905_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	shift_set_1	Warning	1119		100.0 (chain: 1, length: 110)
1	Chemical shift references	chemical_shift_reference	OK	3		No information

Assigned chemical shifts

Saveframe: shift_set_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 110, Sequence coverage: 100.0%
- Total number of assignments
  - ¹³C chemical shifts: 322
  - ¹H chemical shifts: 693
  - ¹⁵N chemical shifts: 104
- Completeness of assignments
  - Entity_assemble_ID: 1
- Peptide bond of PRO
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1

Keywords Denatured Protein, Self-association, Staphylococcal Nuclease