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Found 1 Document (1.814 seconds)

BMRB: 5794

1LCK

1H, 13C, 15N Chemical Shift Assignments for the SH3-SH2 domain pair of the tyrosin kinase Lck

Authors

Schweimer, K., Kiessling, A., Bauer, F., Hor, S., Hoffmann, S., Roesch, P., Sticht, H.

Assembly

Lck SH3-SH2 domain pair

Entity

1. Lck SH3-SH2 domain pair (polymer, Thiol state: all free), 169 monomers, 19053.95 Da Detail

ASPLQDNLVI ALHSYEPSHD GDLGFEKGEQ LRILEQSGEW WKAQSLTTGQ EGFIPFNFVA KANSLEPEPW FFKNLSRKDA ERQLLAPGNT HGSFLIRESE STAGSFSLSV RDFDQNQGEV VKHYKIRNLD NGGFYISPRI TFPGLHELVR HYTNASDGLC TRLSRPCQT

Formula weight

19053.95 Da

Source organism

Homo sapiens

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 83.1 %, Completeness (bb): 98.0 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	83.1 % (1647 of 1982)	82.2 % (850 of 1034)	82.5 % (633 of 767)	90.6 % (164 of 181)
Backbone	98.0 % (976 of 996)	98.3 % (337 of 343)	97.8 % (482 of 493)	98.1 % (157 of 160)
Sidechain	72.4 % (826 of 1141)	74.2 % (513 of 691)	71.3 % (306 of 429)	33.3 % (7 of 21)
Aromatic	2.0 % (4 of 202)	2.0 % (2 of 101)	0.0 % (0 of 98)	66.7 % (2 of 3)
Methyl	92.4 % (146 of 158)	97.5 % (77 of 79)	87.3 % (69 of 79)

1. Tyrosine kinase

ASPLQDNLVI ALHSYEPSHD GDLGFEKGEQ LRILEQSGEW WKAQSLTTGQ EGFIPFNFVA KANSLEPEPW FFKNLSRKDA ERQLLAPGNT HGSFLIRESE STAGSFSLSV RDFDQNQGEV VKHYKIRNLD NGGFYISPRI TFPGLHELVR HYTNASDGLC TRLSRPCQT

Show sample condition

Sample

Temperature 298 (±0.5) K, pH 6.4 (±0.2)

#	Name	Isotope labeling	Type	Concentration
1	Tyrosine kinase	[U-95% 13C; U-95% 15N]		0.5 ~ 0.7 mM

LACS Plot; CA

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

Referencing offset: -0.3 ppm, Outliers: 2 Detail

LACS Plot; CB

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

Referencing offset: -0.3 ppm, Outliers: 2 Detail

LACS Plot; HA

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

Referencing offset: -0.03 ppm, Outliers: 1 Detail

LACS Plot; CO

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

Referencing offset: 0.37 ppm, Outliers: 4 Detail

Release date

2003-10-15

Citation

Sequence-specific 1H, 13C and 15N resonance assignments of the SH3-SH2 domain pair from the human tyrosine kinase Lck
Schweimer, K., Kiessling, A., Bauer, F., Hor, S., Hoffmann, S., Roesch, P., Sticht, H.
J. Biomol. NMR (2003), 27, 405-406, PubMed 14512743 , Abstract

Related entities 1. Lck SH3-SH2 domain pair, : 1 : 3 : 5 : 1 : 231 entities Detail

Interaction partners 1. Lck SH3-SH2 domain pair, : 71 interactors Detail

More details for 71 interactors identified by 49 citations

Experiments performed 10 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr5794_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: bmr5794_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	shift_set_1	Warning	1755		99.4 (chain: 1, length: 169)
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: 169, Sequence coverage: 99.4%
- Total number of assignments
  - ¹H chemical shifts: 981
  - ¹³C chemical shifts: 618
  - ¹⁵N chemical shifts: 156
- 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	1034	827	80.0
¹³C chemical shifts	767	618	80.6
¹⁵N chemical shifts	191	156	81.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	343	334	97.4
¹³C chemical shifts	338	320	94.7
¹⁵N chemical shifts	160	154	96.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	691	493	71.3
¹³C chemical shifts	429	298	69.5
¹⁵N chemical shifts	31	2	6.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	79	77	97.5
¹³C chemical shifts	79	67	84.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	101	2	2.0
¹³C chemical shifts	98	0	0.0
¹⁵N chemical shifts	3	2	66.7

Keywords kinase, Lck, Src-kinases

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Found 1 Document (1.814 seconds)

BMRB: 5794

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. Lck SH3-SH2 domain pair, : 1 : 3 : 5 : 1 : 231 entities Detail

Interaction partners 1. Lck SH3-SH2 domain pair, : 71 interactors Detail

Experiments performed 10 experiments Detail

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Chemical shift validation 3 contents Detail