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Found 1 Document (1.284 seconds)

BMRB: 4252

Triple Resonance Assignment for Abl SH(32) and One in the Complex with a Consolidated Ligand

Authors

Xu, R., Cahill, S., Cowburn, D.

Assembly

Abl SH(32) complex

Entity

1. Src homology domain 3 and 2 (polymer), 166 monomers, 18296.00 Da Detail

GSPGGSLFVA LYDFVASGDN TLSITKGEKL RVLGYNHNGE WAEAQTKNGQ GWVPSNYITP VNSLEKHSWY HGPVSRNAAE YLLSSGINGS FLVRESESSP GQRSISLRYE GRVYHYRINT ASDGKLYVSS ESRFNTLAEL VHHHSTVADG LITTLHYPAP KRGIRD

2. Abl SH3 binding peptide (polymer), 10 monomers, 1005.163 Da Detail

PPAYAPPPVP

3. Abl SH2 binding peptide (polymer), 6 monomers, 719.7816 Da Detail

PVYENV

4. G6-Kamide linker (polymer), 6 monomers, 360.3256 Da Detail

GGGGGG

Total weight

20381.27 Da

Max. entity weight

18296.0 Da

Source organism

Homo sapiens

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 83.5 %, Completeness: 63.3 %, Completeness (bb): 70.0 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	63.3 % (1327 of 2097)	69.0 % (747 of 1083)	52.1 % (429 of 823)	79.1 % (151 of 191)
Backbone	70.0 % (770 of 1100)	81.8 % (315 of 385)	56.4 % (305 of 541)	86.2 % (150 of 174)
Sidechain	59.6 % (692 of 1162)	62.2 % (434 of 698)	57.5 % (257 of 447)	5.9 % (1 of 17)
Aromatic	7.4 % (15 of 204)	12.7 % (13 of 102)	2.0 % (2 of 99)	0.0 % (0 of 3)
Methyl	83.3 % (155 of 186)	83.9 % (78 of 93)	82.8 % (77 of 93)

1. Src homology domain 3 and 2

GSPGGSLFVA LYDFVASGDN TLSITKGEKL RVLGYNHNGE WAEAQTKNGQ GWVPSNYITP VNSLEKHSWY HGPVSRNAAE YLLSSGINGS FLVRESESSP GQRSISLRYE GRVYHYRINT ASDGKLYVSS ESRFNTLAEL VHHHSTVADG LITTLHYPAP KRGIRD

2. Abl SH3 binding peptide

PPAYAPPPVP

3. Abl SH2 binding peptide

PVYENV

4. G6-Kamide linker

GGGGGG

Show sample condition

Sample

Temperature 308 (±0.1) K, pH 7.2 (±0.5)

#	Name	Isotope labeling	Type	Concentration
1	Src homology domain 3 and 2			0.8 mM

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹H	DSS	methyl protons	null	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: 0.13 ppm, Outliers: 1 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹H	DSS	methyl protons	null	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: 0.13 ppm, Outliers: 1 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹H	DSS	methyl protons	null	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: -0.05 ppm, Outliers: 1 Detail

Release date

2007-07-12

Citation 1

Triple resonance-based assignment for Abl SH(32) and its complex with a consolidated ligand
Xu, R., Cahill, S., Cowburn, D.
J. Biomol. NMR (1999), 14, 187-188, PubMed 10427746 , Abstract

Show more 1 citaion

Citation 2

1H, 13C and 15N chemical shift referencing in biomolecular NMR
Wishart, D.S., Bigam, C.G., Yao, J., Abildgaard, F., Dyson, H.J., Oldfield, E., Markley, J.L., Sykes, B.D.
J. Biomol. NMR (1995), 6, 135-140, PubMed 8589602 , DOI: , Abstract

Hide non-primary 1 citaion

Related entities 1. Src homology domain 3 and 2, : 3 : 93 entities Detail

Chemical shift validation 6 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr4252_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: bmr4252_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts	Warning	1440		92.8 (chain: 1, length: 166)
1	Chemical shift references	chemical_shift_reference_one	OK	3		No information

Assigned chemical shifts

Saveframe: assigned_chemical_shifts
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 166, Sequence coverage: 92.8%
- Total number of assignments
  - ¹⁵N chemical shifts: 151
  - ¹H chemical shifts: 882
  - ¹³C chemical shifts: 407
- Completeness of assignments
  - Entity_assemble_ID: 1
- 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 (%)
¹⁵N chemical shifts	185	151	81.6
¹H chemical shifts	967	724	74.9
¹³C chemical shifts	734	407	55.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹⁵N chemical shifts	159	151	95.0
¹H chemical shifts	342	315	92.1
¹³C chemical shifts	332	154	46.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹⁵N chemical shifts	26	0	0.0
¹H chemical shifts	625	409	65.4
¹³C chemical shifts	402	253	62.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	85	79	92.9
¹³C chemical shifts	85	78	91.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹⁵N chemical shifts	3	0	0.0
¹H chemical shifts	94	0	0.0
¹³C chemical shifts	91	0	0.0

Keywords Abl_SH(32), consolidated_ligand, NMR_assignment

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Found 1 Document (1.284 seconds)

BMRB: 4252

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. Src homology domain 3 and 2, : 3 : 93 entities Detail

Chemical shift validation 6 contents Detail