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BMRB: 7082

2JXG

1H, 13C, and 15N assignments for the Psuedomonas putida protein PutA45

Authors

Halouska, S., Zhou, Y., Becker, D., Powers, R.

Assembly

PutA45

Entity

1. PutA45 (polymer, Thiol state: all free), 51 monomers, 6006.765 × 2 Da Detail

MATTTLGVKL DDPTRERLKA AAQSIDRTPH WLIKQAIFNY LEKLEHHHHH H

Total weight

12013.53 Da

Max. entity weight

6006.765 Da

Source organism

Pseudomonas putida

Exptl. method

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 88.2 %, Completeness: 82.3 %, Completeness (bb): 85.4 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	82.3 % (506 of 615)	81.2 % (259 of 319)	83.5 % (203 of 243)	83.0 % (44 of 53)
Backbone	85.4 % (258 of 302)	86.1 % (87 of 101)	84.9 % (129 of 152)	85.7 % (42 of 49)
Sidechain	80.4 % (292 of 363)	78.9 % (172 of 218)	83.7 % (118 of 141)	50.0 % (2 of 4)
Aromatic	58.6 % (34 of 58)	58.6 % (17 of 29)	57.1 % (16 of 28)	100.0 % (1 of 1)
Methyl	100.0 % (60 of 60)	100.0 % (30 of 30)	100.0 % (30 of 30)

1. PutA45

MATTTLGVKL DDPTRERLKA AAQSIDRTPH WLIKQAIFNY LEKLEHHHHH H

Show sample condition

Sample

Temperature 298 (±0.1) K, pH 6.2 (±0.1), Details 2.2mM PutA45 [99% 13C, 99% 15 N] 50mM phospate buffer 200mM NaCl 10% D2O

#	Name	Isotope labeling	Type	Concentration
1	PutA45	[U-99% 13C, U-99% 15 N]	protein	2.2 mM
2	phospate buffer		buffer	50 mM
3	NaCl		salt	200 mM
4	D2O			10 %
5	H2O			90 %

Release date

2009-05-26

Citation

Solution structure of the Pseudomonas putida protein PpPutA45 and its DNA complex
Halouska, S., Zhou, Y., Becker, D.F., Powers, R.
Proteins (2009), 75, 12-27, PubMed 18767154 , DOI 10.1002/prot.22217 , Abstract

Related entities 1. PutA45, : 1 : 2 : 15 entities Detail

Experiments performed 10 experiments Detail

1 HSQC

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Temperature 298 (±0.1) K, pH 6.2 (±0.1), Details 2.2mM PutA45 [99% 13C, 99% 15 N] 50mM phospate buffer 200mM NaCl 10% D2O

#	Name	Isotope labeling	Type	Concentration
1	PutA45	[U-99% 13C, U-99% 15 N]	protein	2.2 mM
2	phospate buffer		buffer	50 mM
3	NaCl		salt	200 mM
4	D2O			10 %
5	H2O			90 %

2 HNCO

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Temperature 298 (±0.1) K, pH 6.2 (±0.1), Details 2.2mM PutA45 [99% 13C, 99% 15 N] 50mM phospate buffer 200mM NaCl 10% D2O

#	Name	Isotope labeling	Type	Concentration
1	PutA45	[U-99% 13C, U-99% 15 N]	protein	2.2 mM
2	phospate buffer		buffer	50 mM
3	NaCl		salt	200 mM
4	D2O			10 %
5	H2O			90 %

3 HNCA

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Temperature 298 (±0.1) K, pH 6.2 (±0.1), Details 2.2mM PutA45 [99% 13C, 99% 15 N] 50mM phospate buffer 200mM NaCl 10% D2O

#	Name	Isotope labeling	Type	Concentration
1	PutA45	[U-99% 13C, U-99% 15 N]	protein	2.2 mM
2	phospate buffer		buffer	50 mM
3	NaCl		salt	200 mM
4	D2O			10 %
5	H2O			90 %

4 CBCANH

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Temperature 298 (±0.1) K, pH 6.2 (±0.1), Details 2.2mM PutA45 [99% 13C, 99% 15 N] 50mM phospate buffer 200mM NaCl 10% D2O

#	Name	Isotope labeling	Type	Concentration
1	PutA45	[U-99% 13C, U-99% 15 N]	protein	2.2 mM
2	phospate buffer		buffer	50 mM
3	NaCl		salt	200 mM
4	D2O			10 %
5	H2O			90 %

5 CBCACONH

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Temperature 298 (±0.1) K, pH 6.2 (±0.1), Details 2.2mM PutA45 [99% 13C, 99% 15 N] 50mM phospate buffer 200mM NaCl 10% D2O

#	Name	Isotope labeling	Type	Concentration
1	PutA45	[U-99% 13C, U-99% 15 N]	protein	2.2 mM
2	phospate buffer		buffer	50 mM
3	NaCl		salt	200 mM
4	D2O			10 %
5	H2O			90 %

6 HCCCONH

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Temperature 298 (±0.1) K, pH 6.2 (±0.1), Details 2.2mM PutA45 [99% 13C, 99% 15 N] 50mM phospate buffer 200mM NaCl 10% D2O

#	Name	Isotope labeling	Type	Concentration
1	PutA45	[U-99% 13C, U-99% 15 N]	protein	2.2 mM
2	phospate buffer		buffer	50 mM
3	NaCl		salt	200 mM
4	D2O			10 %
5	H2O			90 %

7 CCCONH

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Temperature 298 (±0.1) K, pH 6.2 (±0.1), Details 2.2mM PutA45 [99% 13C, 99% 15 N] 50mM phospate buffer 200mM NaCl 10% D2O

#	Name	Isotope labeling	Type	Concentration
1	PutA45	[U-99% 13C, U-99% 15 N]	protein	2.2 mM
2	phospate buffer		buffer	50 mM
3	NaCl		salt	200 mM
4	D2O			10 %
5	H2O			90 %

8 C13-NOESY

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Temperature 298 (±0.1) K, pH 6.2 (±0.1), Details 2.2mM PutA45 [99% 13C, 99% 15 N] 50mM phospate buffer 200mM NaCl 10% D2O

#	Name	Isotope labeling	Type	Concentration
1	PutA45	[U-99% 13C, U-99% 15 N]	protein	2.2 mM
2	phospate buffer		buffer	50 mM
3	NaCl		salt	200 mM
4	D2O			10 %
5	H2O			90 %

9 N15-NOESY

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Temperature 298 (±0.1) K, pH 6.2 (±0.1), Details 2.2mM PutA45 [99% 13C, 99% 15 N] 50mM phospate buffer 200mM NaCl 10% D2O

#	Name	Isotope labeling	Type	Concentration
1	PutA45	[U-99% 13C, U-99% 15 N]	protein	2.2 mM
2	phospate buffer		buffer	50 mM
3	NaCl		salt	200 mM
4	D2O			10 %
5	H2O			90 %

10 HNHA

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Temperature 298 (±0.1) K, pH 6.2 (±0.1), Details 2.2mM PutA45 [99% 13C, 99% 15 N] 50mM phospate buffer 200mM NaCl 10% D2O

#	Name	Isotope labeling	Type	Concentration
1	PutA45	[U-99% 13C, U-99% 15 N]	protein	2.2 mM
2	phospate buffer		buffer	50 mM
3	NaCl		salt	200 mM
4	D2O			10 %
5	H2O			90 %

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr7082_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: bmr7082_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	chem_shift_list_1	Warning	558		86.3 (chain: 1, length: 51)
1	Chemical shift references	chemical_shift_referencing	OK	3		No information

Assigned chemical shifts

Saveframe: chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 51, Sequence coverage: 86.3%
- Total number of assignments
  - ¹H chemical shifts: 316
  - ¹³C chemical shifts: 200
  - ¹⁵N chemical shifts: 42
- Completeness of assignments
  - Entity_assemble_ID: 1
- 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

Keywords Halouska, PutA45