BMRB Entry 16809

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16809
MolProbity Validation Chart

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Title:
Ensemble Structures of the binary complex between the SH3 and SH2 domain of interleukin-2 tyrosine kinase.
Deposition date:
2010-03-31
Original release date:
2012-08-03
Authors:
Andreotti, Amy; Severin, Andrew; Fulton, Donald
Citation:

Citation: Severin, Andrew; Fulton, Donald; Andreotti, Amy. "Solution Structure of the binary complex between the SH3 and SH2 domain of interleukin-2 tyrosine kinase"  .

Assembly members:

Assembly members:
Itk_SH3_domain, polymer, 63 residues, 7356.008 Da.
Itk_SH2_domain, polymer, 108 residues, 12534.314 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   Host organism: Escherichia coli   Vector: pgex2T

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Itk_SH3_domain: GSPEETLVIALYDYQTNDPQ ELALRCDEEYYLLDSSEIHW WRVQDKNGHEGYAPSSYLVE KSP
Itk_SH2_domain: NNLETYEWYNKSISRDKAEK LLLDTGKEGAFMVRDSRTPG TYTVSVFTKAIISENPCIKH YHIKETNDSPKRYYVAEKYV FDSIPLLIQYHQYNGGGLVT RLRYPVCG

Data typeCount
13C chemical shifts1330
15N chemical shifts358
1H chemical shifts2088

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Itk_SH3_domain1
2Itk_SH2_domain2

Entities:

Entity 1, Itk_SH3_domain 63 residues - 7356.008 Da.

GS is the remnant from GST tag cleavage.

1   GLYSERPROGLUGLUTHRLEUVALILEALA
2   LEUTYRASPTYRGLNTHRASNASPPROGLN
3   GLULEUALALEUARGCYSASPGLUGLUTYR
4   TYRLEULEUASPSERSERGLUILEHISTRP
5   TRPARGVALGLNASPLYSASNGLYHISGLU
6   GLYTYRALAPROSERSERTYRLEUVALGLU
7   LYSSERPRO

Entity 2, Itk_SH2_domain 108 residues - 12534.314 Da.

1   ASNASNLEUGLUTHRTYRGLUTRPTYRASN
2   LYSSERILESERARGASPLYSALAGLULYS
3   LEULEULEUASPTHRGLYLYSGLUGLYALA
4   PHEMETVALARGASPSERARGTHRPROGLY
5   THRTYRTHRVALSERVALPHETHRLYSALA
6   ILEILESERGLUASNPROCYSILELYSHIS
7   TYRHISILELYSGLUTHRASNASPSERPRO
8   LYSARGTYRTYRVALALAGLULYSTYRVAL
9   PHEASPSERILEPROLEULEUILEGLNTYR
10   HISGLNTYRASNGLYGLYGLYLEUVALTHR
11   ARGLEUARGTYRPROVALCYSGLY

Samples:

SH3_35%_bound: Itk SH3 domain, [U-100% 13C; U-100% 15N], 3.4 mM; Itk SH2 domain 1.5 mM; H2O 95%; D2O 5%; NaCl 75 mM

SH2_35%_bound: Itk SH2 domain, [U-100% 13C; U-100% 15N], 3.4 mM; Itk SH3 domain 1.5 mM; H2O 95%; D2O 5%; NaCl 75 mM

SH2_77%_bound: Itk SH2 domain, [U-100% 13C; U-100% 15N], 1.5 mM; Itk SH3 domain 3.4 mM; H2O 95%; D2O 5%; NaCl 75 mM

SH3_77%_bound: Itk SH3 domain, [U-100% 13C; U-100% 15N], 1.5 mM; Itk SH2 domain 3.4 mM; H2O 95%; D2O 5%; NaCl 75 mM

isotropic_conditions_1: ionic strength: 75 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

anisotropic_conditions_2: ionic strength: 75 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCSH3_35%_boundisotropicisotropic_conditions_1
2D 1H-13C HSQCSH3_35%_boundisotropicisotropic_conditions_1
3D CBCA(CO)NHSH3_35%_boundisotropicisotropic_conditions_1
3D HNCOSH3_35%_boundisotropicisotropic_conditions_1
3D HNCACBSH3_35%_boundisotropicisotropic_conditions_1
3D HBHA(CO)NHSH3_35%_boundisotropicisotropic_conditions_1
3D HCCH-TOCSYSH3_35%_boundisotropicisotropic_conditions_1
3D 1H-15N NOESYSH3_35%_boundisotropicisotropic_conditions_1
3D 1H-15N TOCSYSH3_35%_boundisotropicisotropic_conditions_1
3D 1H-13C NOESYSH3_35%_boundisotropicisotropic_conditions_1
2D 1H-15N IPAPSH3_35%_boundisotropicisotropic_conditions_1
3D HNCA COSYSH3_35%_boundisotropicisotropic_conditions_1
2D 1H-15N IPAPSH3_35%_boundanisotropicanisotropic_conditions_2
3D HNCA COSYSH3_35%_boundanisotropicanisotropic_conditions_2
(HB)CB(CGCDCE)HESH3_35%_boundisotropicisotropic_conditions_1
(HB)CB(CGCD)HDSH3_35%_boundisotropicisotropic_conditions_1
2D 1H-15N HSQCSH2_35%_boundisotropicisotropic_conditions_1
2D 1H-13C HSQCSH2_35%_boundisotropicisotropic_conditions_1
3D CBCA(CO)NHSH2_35%_boundisotropicisotropic_conditions_1
3D HNCOSH2_35%_boundisotropicisotropic_conditions_1
3D HNCACBSH2_35%_boundisotropicisotropic_conditions_1
3D HNCACBSH2_35%_boundisotropicisotropic_conditions_1
3D HBHA(CO)NHSH2_35%_boundisotropicisotropic_conditions_1
3D HCCH-TOCSYSH2_35%_boundisotropicisotropic_conditions_1
3D 1H-15N NOESYSH2_35%_boundisotropicisotropic_conditions_1
3D 1H-15N TOCSYSH2_35%_boundisotropicisotropic_conditions_1
3D 1H-13C NOESYSH2_35%_boundisotropicisotropic_conditions_1
2D 1H-15N IPAPSH2_35%_boundisotropicisotropic_conditions_1
2D 1H-15N IPAPSH2_35%_boundanisotropicanisotropic_conditions_2
(HB)CB(CGCDCE)HESH2_35%_boundisotropicisotropic_conditions_1
(HB)CB(CGCD)HDSH2_35%_boundisotropicisotropic_conditions_1
2D 1H-15N HSQCSH2_35%_boundisotropicisotropic_conditions_1
2D 1H-15N HSQCSH2_77%_boundisotropicisotropic_conditions_1
2D 1H-15N HSQCSH3_77%_boundisotropicisotropic_conditions_1
2D 1H-13C HSQCSH2_77%_boundisotropicisotropic_conditions_1
2D 1H-13C HSQCSH3_77%_boundisotropicisotropic_conditions_1
3D CBCA(CO)NHSH2_77%_boundisotropicisotropic_conditions_1
3D CBCA(CO)NHSH3_77%_boundisotropicisotropic_conditions_1
3D HNCOSH2_77%_boundisotropicisotropic_conditions_1
3D HNCOSH3_77%_boundisotropicisotropic_conditions_1
3D HNHASH2_77%_boundisotropicisotropic_conditions_1
3D HNHASH3_77%_boundisotropicisotropic_conditions_1
3D HNCACBSH2_77%_boundisotropicisotropic_conditions_1
3D HNCACBSH3_77%_boundisotropicisotropic_conditions_1
3D 1H-15N NOESYSH2_77%_boundisotropicisotropic_conditions_1
3D 1H-15N NOESYSH3_77%_boundisotropicisotropic_conditions_1
3D 1H-15N TOCSYSH2_77%_boundisotropicisotropic_conditions_1
3D 1H-15N TOCSYSH3_77%_boundisotropicisotropic_conditions_1
3D 1H-13C NOESYSH2_77%_boundisotropicisotropic_conditions_1
3D 1H-13C NOESYSH3_77%_boundisotropicisotropic_conditions_1
(HB)CB(CGCD)HDSH2_77%_boundisotropicisotropic_conditions_1
(HB)CB(CGCD)HDSH3_77%_boundisotropicisotropic_conditions_1
(HB)CB(CGCDCE)HESH2_77%_boundisotropicisotropic_conditions_1
(HB)CB(CGCDCE)HESH3_77%_boundisotropicisotropic_conditions_1
2D 1H-15N IPAPSH2_77%_boundisotropicisotropic_conditions_1
2D 1H-15N IPAPSH3_77%_boundisotropicisotropic_conditions_1
3D HNCA COSYSH3_77%_boundisotropicisotropic_conditions_1
3D HNCA COSYSH3_77%_boundanisotropicanisotropic_conditions_2
2D 1H-15N IPAPSH2_77%_boundanisotropicanisotropic_conditions_2
2D 1H-15N IPAPSH3_77%_boundanisotropicanisotropic_conditions_2
3D HBHA(CO)NHSH2_77%_boundisotropicisotropic_conditions_1
3D HBHA(CO)NHSH3_77%_boundisotropicisotropic_conditions_1
3D HCCH-TOCSYSH2_77%_boundisotropicisotropic_conditions_1
3D HCCH-TOCSYSH3_77%_boundisotropicisotropic_conditions_1
2D 1H-15N HSQCSH2_77%_boundisotropicisotropic_conditions_1

Software:

X-PLOR NIH v2.19, Brunger A. T. et.al. - refinement

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avii 700 MHz

Related Database Links:

BMRB 11018 15912 15912 5461
PDB
DBJ BAA03129 BAE32118 BAA03129 BAC29830 BAE32118
GB AAA39337 AAA40518 AAI28375 AAI28376 EDL33821 AAA39337 AAA40518 AAI28375 AAI28376 EDL33821
REF NP_001102295 NP_001268894 NP_001268895 NP_001268896 NP_001268897 NP_001102295 NP_001268894 NP_001268895 NP_001268897 NP_034713
SP Q03526 Q03526
AlphaFold Q03526 Q03526

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