BMRB Entry 5461

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5461
MolProbity Validation Chart

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Title:
Chemical shift assignments Itk SH2 domain, conformation corresponding to cis and trans proline 287
Deposition date:
2002-07-15
Original release date:
2003-02-20
Authors:
Mallis, Robert; Brazin, Kristine; Fulton, D.; Andreotti, Amy
Citation:

Citation: Mallis, Robert; Brazin, Kristine; Fulton, D.; Andreotti, Amy. "Structural Characterization of a Proline-driven Conformational Switch within the Itk SH2 Domain"  Nat. Struct. Biol. 9, 900-905 (2002).
PubMed: 12402030

Assembly members:

Assembly members:
Interleukin-2 tyrosine kinase src homology 2 domain, polymer, 118 residues, 12700 Da.

Natural source:

Natural source:   Common Name: house mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Interleukin-2 tyrosine kinase src homology 2 domain: GSPNNLETYEWYNKSISRDK AEKLLLDTGKEGAFMVRDSR TPGTYTVSVFTKAIISENPC IKHYHIKETNDSPKRYYVAE KYVFDSIPLLIQYHQYNGGG LVTRLRYPVCGSPGIHRD

Data sets:
Data typeCount
1H chemical shifts1483
13C chemical shifts724
15N chemical shifts234

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1Itk SH21

Entities:

Entity 1, Itk SH2 118 residues - 12700 Da.

1   GLYSERPROASNASNLEUGLUTHRTYRGLU
2   TRPTYRASNLYSSERILESERARGASPLYS
3   ALAGLULYSLEULEULEUASPTHRGLYLYS
4   GLUGLYALAPHEMETVALARGASPSERARG
5   THRPROGLYTHRTYRTHRVALSERVALPHE
6   THRLYSALAILEILESERGLUASNPROCYS
7   ILELYSHISTYRHISILELYSGLUTHRASN
8   ASPSERPROLYSARGTYRTYRVALALAGLU
9   LYSTYRVALPHEASPSERILEPROLEULEU
10   ILEGLNTYRHISGLNTYRASNGLYGLYGLY
11   LEUVALTHRARGLEUARGTYRPROVALCYS
12   GLYSERPROGLYILEHISARGASP

Samples:

sample_1: Interleukin-2 tyrosine kinase src homology 2 domain, [U-95% 13C; U-98% 15N], 1.0 mM; NaCl 75 mM; KPO4 50 mM

sample_conditions: pH: 7.4; temperature: 298 K; ionic strength: 0.15 M

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYnot availablenot availablenot available
3D 1H-15N TOCSYnot availablenot availablenot available
3D 1H-13C NOESYnot availablenot availablenot available
3D 15N-15N-1H NOESYnot availablenot availablenot available
3D 1H-13C HCCHnot availablenot availablenot available
3D 1H-13C-15N HNCACBnot availablenot availablenot available
3D 1H-13C-15N HN(CO)CACBnot availablenot availablenot available
2D 1H-15N HSQCnot availablenot availablenot available
2D 1H-1H NOESYnot availablenot availablenot available
2D 1H-1H TOCSYnot availablenot availablenot available
2D 1H-1H COSYnot availablenot availablenot available
2D 1H-1H ROESYnot availablenot availablenot available

Software:

Xwinnmr - spectrum acquisition, phasing

NmrView v4.1.3 - assignments, restraint generation

NMR spectrometers:

  • Bruker DRX 500 MHz

Related Database Links:

BMRB 15912 16809
PDB
DBJ BAA03129 BAC29830 BAE32118
GB AAA39337 AAA40518 AAI28375 AAI28376 EDL33821
REF NP_001102295 NP_001268894 NP_001268895 NP_001268897 NP_034713
SP Q03526
AlphaFold Q03526 Q03526 Q03526 Q03526

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks