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Found 1 Document (1.15 seconds)

BMRB: 4820

1HD6

1H and 13Ca Chemical Shift Assignments for the Pheromone Er-22

Authors

Zerbe, O., Liu, A., Luginbuhl, P., Luporini, P., Wuthrich, K.

Assembly

Pheromone Er-22

Entity

1. Pheromone Er-22 (polymer, Thiol state: all disulfide bound), 37 monomers, 3938.523 Da Detail

DICDIAIAQC SLTLCQDCEN TPICELAVKG SCPPPWS

Formula weight

3938.523 Da

Entity Connection

disulfide 3 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	disulfide	sing	1:CYS3:SG	1:CYS18:SG
2	disulfide	sing	1:CYS10:SG	1:CYS32:SG
3	disulfide	sing	1:CYS15:SG	1:CYS24:SG

Source organism

Euplotes raikovi

Exptl. method

NMR

Refine. method

DISTANCE GEOMETRY, RESTRAINED ENERGY REFINEMENT

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 67.4 %, Completeness (bb): 60.2 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C
All	67.4 % (242 of 359)	99.5 % (203 of 204)	25.2 % (39 of 155)
Backbone	60.2 % (109 of 181)	98.6 % (70 of 71)	35.5 % (39 of 110)
Sidechain	63.1 % (135 of 214)	100.0 % (133 of 133)	2.5 % (2 of 81)
Aromatic	54.5 % (6 of 11)	100.0 % (6 of 6)	0.0 % (0 of 5)
Methyl	54.8 % (23 of 42)	100.0 % (21 of 21)	9.5 % (2 of 21)

1. Pheromone Er-22

DICDIAIAQC SLTLCQDCEN TPICELAVKG SCPPPWS

Show sample condition

Sample #1

Temperature 296 (±1) K, pH 5.0 (±0.1)

#	Name	Isotope labeling	Concentration
1	Pheromone Er-22	natural abundance	6.5 mM
2	H2O		90 %
3	D2O		10 %

Sample #2

Temperature 296 (±1) K, pH 5.0 (±0.1)

#	Name	Isotope labeling	Type	Concentration
4	Pheromone Er-22	natural abundance		6.5 mM
5	D2O			100 %

Protein Blocks Logo

Calculated from 20 models in PDB: 1HD6, Strand ID: A Detail

Release date

2001-01-28

Citation 1

NMR structure of the pheromone Er-22 from Euplotes raikovi
Liu, A., Luginbuhl, P., Zerbe, O., Ortenzi, C., Luporini, P., Wuthrich, K.
J. Biomol. NMR (2001), 19, 75-78, PubMed 11246857 , DOI: , Abstract

Show more 3 citaions

Citation 2

The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
J. Biomol. NMR (1995), 6, 1-10, PubMed 22911575 , DOI 10.1007/BF00417486 , Abstract

Citation 3

Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA
Guntert, P., Braun, W., Wuthrich, K.
J. Mol. Biol. (1991), 217, 517-530, PubMed 1847217 , DOI 10.1016/0022-2836(91)90754-t , Abstract

Citation 4

The new program OPAL for molecular dynamics simulations and energy refinements of biological macromolecules
Luginbuhl, P., Guntert, P., Billeter, M., Wuethrich, K.
J. Biomol. NMR (1996), 8, 136-146, PubMed 8914272 , DOI 10.1007/bf00211160 , Abstract

Hide non-primary 3 citaions

Related entities 1. Pheromone Er-22, : 1 : 1 : 3 entities Detail

Experiments performed 6 experiments Detail

1 2QF-COSY

Instrument

#1 Model Bruker AMX (600 MHz)

#2 Model Varian Unity-plus (750 MHz)

Sample #1

Temperature 296 (±1) K, pH 5.0 (±0.1)

#	Name	Isotope labeling	Concentration
1	Pheromone Er-22	natural abundance	6.5 mM
2	H2O		90 %
3	D2O		10 %

Sample #2

Temperature 296 (±1) K, pH 5.0 (±0.1)

#	Name	Isotope labeling	Type	Concentration
4	Pheromone Er-22	natural abundance		6.5 mM
5	D2O			100 %

2 clean-TOCSY

Instrument

#1 Model Bruker AMX (600 MHz)

#2 Model Varian Unity-plus (750 MHz)

Sample #1

Temperature 296 (±1) K, pH 5.0 (±0.1)

#	Name	Isotope labeling	Concentration
1	Pheromone Er-22	natural abundance	6.5 mM
2	H2O		90 %
3	D2O		10 %

Sample #2

Temperature 296 (±1) K, pH 5.0 (±0.1)

#	Name	Isotope labeling	Type	Concentration
4	Pheromone Er-22	natural abundance		6.5 mM
5	D2O			100 %

3 2Q-spectrum

Instrument

#1 Model Bruker AMX (600 MHz)

#2 Model Varian Unity-plus (750 MHz)

Sample #1

Temperature 296 (±1) K, pH 5.0 (±0.1)

#	Name	Isotope labeling	Concentration
1	Pheromone Er-22	natural abundance	6.5 mM
2	H2O		90 %
3	D2O		10 %

Sample #2

Temperature 296 (±1) K, pH 5.0 (±0.1)

#	Name	Isotope labeling	Type	Concentration
4	Pheromone Er-22	natural abundance		6.5 mM
5	D2O			100 %

4 E.COSY

Instrument

#1 Model Bruker AMX (600 MHz)

#2 Model Varian Unity-plus (750 MHz)

Sample #1

Temperature 296 (±1) K, pH 5.0 (±0.1)

#	Name	Isotope labeling	Concentration
1	Pheromone Er-22	natural abundance	6.5 mM
2	H2O		90 %
3	D2O		10 %

Sample #2

Temperature 296 (±1) K, pH 5.0 (±0.1)

#	Name	Isotope labeling	Type	Concentration
4	Pheromone Er-22	natural abundance		6.5 mM
5	D2O			100 %

5 NOESY

Instrument

#1 Model Bruker AMX (600 MHz)

#2 Model Varian Unity-plus (750 MHz)

Sample #1

Temperature 296 (±1) K, pH 5.0 (±0.1)

#	Name	Isotope labeling	Concentration
1	Pheromone Er-22	natural abundance	6.5 mM
2	H2O		90 %
3	D2O		10 %

Sample #2

Temperature 296 (±1) K, pH 5.0 (±0.1)

#	Name	Isotope labeling	Type	Concentration
4	Pheromone Er-22	natural abundance		6.5 mM
5	D2O			100 %

6 13C-1H HSQC

Instrument

#1 Model Bruker AMX (600 MHz)

#2 Model Varian Unity-plus (750 MHz)

Sample #1

Temperature 296 (±1) K, pH 5.0 (±0.1)

#	Name	Isotope labeling	Concentration
1	Pheromone Er-22	natural abundance	6.5 mM
2	H2O		90 %
3	D2O		10 %

Sample #2

Temperature 296 (±1) K, pH 5.0 (±0.1)

#	Name	Isotope labeling	Type	Concentration
4	Pheromone Er-22	natural abundance		6.5 mM
5	D2O			100 %

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr4820_3.str
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	True (see coordinates for details)
Whether the assembly has a other bond	None
Whether the assembly contains a cyclic polymer	None
Overall data processing status	Warning

Disulfide bonds

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
1:3:CYS:SG	1:18:CYS:SG	unknown, CA 59.2 ppm	unknown, CA 54.4 ppm	n/a
1:10:CYS:SG	1:32:CYS:SG	unknown, CA 55.2 ppm	unknown, CA 54.8 ppm	n/a
1:15:CYS:SG	1:24:CYS:SG	unknown, CA 54.5 ppm	unknown, CA 59.7 ppm	n/a

Other bonds (neither disulfide, covalent nor hydrogen bonds, e.g. Zinc–sulphur bond)

None

Non-standard residues

None

Content subtype: bmr4820_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	13Ca_and_1H_shifts	Warning	282		100.0 (chain: 1, length: 37)
1	Chemical shift references	chemical_shift_reference	OK	2		No information

Assigned chemical shifts

Saveframe: 13Ca_and_1H_shifts
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 37, Sequence coverage: 100.0%
- Total number of assignments
  - ¹³C chemical shifts: 37
  - ¹H chemical shifts: 245
- Completeness of assignments
  - Entity_assemble_ID: 1
- Redox state of CYS
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1

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Found 1 Document (1.15 seconds)

BMRB: 4820

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Related entities 1. Pheromone Er-22, : 1 : 1 : 3 entities Detail

Experiments performed 6 experiments Detail

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Chemical shift validation 3 contents Detail