BMRBj - BMREntryMaster

Found 1 Document (1.838 seconds)

BMRB: 4670

1J6Y

Sequence-specific 1H,13C and 15N chemical shift backbone NMR assignment and secondary structure of the Arabidopsis thaliana PIN1At

Authors

Landrieu, I., Wieruszeski, J., Odaert, B., Inze, D., Lippens, G.

Assembly

PIN1At

Entity

1. PIN1At (polymer, Thiol state: all free), 120 monomers, 13151.69 Da Detail

HMASRDQVKA SHILIKHQGS RRKASWKDPE GKIILTTTRE AAVEQLKSIR EDIVSGKANF EEVATRVSDC SSAKRGGDLG SFGRGQMQKP FEEATYALKV GDISDIVDTD SGVHIIKRTA

Formula weight

13151.69 Da

Source organism

Arabidopsis thaliana

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 94.2 %, Completeness: 78.8 %, Completeness (bb): 90.5 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	78.8 % (1066 of 1353)	78.8 % (556 of 706)	77.6 % (405 of 522)	84.0 % (105 of 125)
Backbone	90.5 % (648 of 716)	90.7 % (225 of 248)	90.9 % (318 of 350)	89.0 % (105 of 118)
Sidechain	69.3 % (518 of 747)	72.3 % (331 of 458)	66.3 % (187 of 282)	0.0 % (0 of 7)
Aromatic	36.4 % (24 of 66)	63.6 % (21 of 33)	9.4 % (3 of 32)	0.0 % (0 of 1)
Methyl	75.8 % (97 of 128)	81.3 % (52 of 64)	70.3 % (45 of 64)

1. Arabidopsis thaliana prolyl cis/trans isomerase

HMASRDQVKA SHILIKHQGS RRKASWKDPE GKIILTTTRE AAVEQLKSIR EDIVSGKANF EEVATRVSDC SSAKRGGDLG SFGRGQMQKP FEEATYALKV GDISDIVDTD SGVHIIKRTA

Show sample condition

Sample #1

Temperature 293 (±0.2) K, pH 6.3 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Arabidopsis thaliana prolyl cis/trans isomerase	[U-98% 15N]		0.5 ~ 0.9 mM

Sample #2

Temperature 293 (±0.2) K, pH 6.3 (±0.1)

#	Name	Isotope labeling	Type	Concentration
2	Arabidopsis thaliana prolyl cis/trans isomerase	[U-98% 13C]		0.5 ~ 0.9 mM

Sample #3

Temperature 293 (±0.2) K, pH 6.3 (±0.1)

#	Name	Isotope labeling	Type	Concentration
3	Arabidopsis thaliana prolyl cis/trans isomerase	[U-98% 15N; U-13C]		0.5 ~ 0.9 mM

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type
¹³C	DSS	methyl protons	internal	indirect
¹H	DSS	methyl protons	internal	direct
¹⁵N	DSS	methyl protons	internal	indirect

Referencing offset: -0.58 ppm, Outliers: 1 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type
¹³C	DSS	methyl protons	internal	indirect
¹H	DSS	methyl protons	internal	direct
¹⁵N	DSS	methyl protons	internal	indirect

Referencing offset: -0.58 ppm, Outliers: 1 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type
¹³C	DSS	methyl protons	internal	indirect
¹H	DSS	methyl protons	internal	direct
¹⁵N	DSS	methyl protons	internal	indirect

Referencing offset: -0.05 ppm, Outliers: 3 Detail

LACS Plot; CO

Atom type	Mol. common name	Atom group	Ref. method	Ref. type
¹³C	DSS	methyl protons	internal	indirect
¹H	DSS	methyl protons	internal	direct
¹⁵N	DSS	methyl protons	internal	indirect

Referencing offset: -0.54 ppm, Outliers: 1 Detail

Release date

2000-04-11

Citation

Letter to the editor: sequence-specific 1H, 13C and 15N chemical shift backbone NMR assignment and secondary structure of the Arabidopsis thaliana PIN1At protein
Landrieu, I., Wieruszeski, J., Odaert, B., Inze, D., Grzesiek, S., Lippens, G.
J. Biomol. NMR (2000), 17, 271-272, PubMed 10959635 , DOI: , Abstract

Related entities 1. PIN1At, : 1 : 2 : 167 entities Detail

Interaction partners 1. PIN1At, : 2 interactors Detail

More details for 2 interactors identified by 1 citations

Experiments performed 1 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr4670_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: bmr4670_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	shift_set_1	Warning	1144		93.3 (chain: 1, length: 120)
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: 120, Sequence coverage: 93.3%
- Total number of assignments
  - ¹H chemical shifts: 648
  - ¹³C chemical shifts: 393
  - ¹⁵N chemical shifts: 103
- Completeness of assignments
  - Entity_assemble_ID: 1
- Redox state of CYS
- Peptide bond of PRO
- 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

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	248	223	89.9
¹³C chemical shifts	240	215	89.6
¹⁵N chemical shifts	118	103	87.3

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Sequence chart about interacting regions

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Found 1 Document (1.838 seconds)

BMRB: 4670

Sample #1

Sample #2

Sample #3

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. PIN1At, : 1 : 2 : 167 entities Detail

Interaction partners 1. PIN1At, : 2 interactors Detail

Experiments performed 1 experiments Detail

Instrument

Sample #1

Sample #2

Sample #3

Chemical shift validation 3 contents Detail

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	706	539	76.3
¹³C chemical shifts	522	393	75.3
¹⁵N chemical shifts	134	103	76.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	458	316	69.0
¹³C chemical shifts	282	178	63.1
¹⁵N chemical shifts	16	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	33	21	63.6
¹³C chemical shifts	32	3	9.4
¹⁵N chemical shifts	1	0	0.0