BMRB Entry 19966

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19966
MolProbity Validation Chart

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Title:
Structure and function of the JAK interaction region in the intrinsically disordered N-terminus of SOCS5
Deposition date:
2014-05-12
Original release date:
2015-05-18
Authors:
Chandrashekaran, Indu; Mohanty, Biswaranjan; Linossi, Edmond; Dagley, Laura; Murphy, James; Nicholson, Sandra; Babon, Jeffrey; Norton, Raymond
Citation:

Citation: Chandrashekaran, Indu; Mohanty, Biswaranjan; Linossi, Edmond; Dagley, Laura; Murphy, James; Nicholson, Sandra; Babon, Jeffrey; Norton, Raymond. "Structure and function of the JAK interaction region in the intrinsically disordered N-terminus of SOCS5"  J. Mol. Biol. ., .-..

Assembly members:

Assembly members:
entity, polymer, 70 residues, 8116.588 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):
entity: RSLRQRLQDTVGLCFPMRTY SKQSKPLFSNKRKIHLSELM LEKCPFPAGSDLAQKWHLIK QHTAPVSPHS

Data sets:
Data typeCount
13C chemical shifts232
15N chemical shifts63
1H chemical shifts452

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1N-terminus of SOCS51

Entities:

Entity 1, N-terminus of SOCS5 70 residues - 8116.588 Da.

1   ARGSERLEUARGGLNARGLEUGLNASPTHR
2   VALGLYLEUCYSPHEPROMETARGTHRTYR
3   SERLYSGLNSERLYSPROLEUPHESERASN
4   LYSARGLYSILEHISLEUSERGLULEUMET
5   LEUGLULYSCYSPROPHEPROALAGLYSER
6   ASPLEUALAGLNLYSTRPHISLEUILELYS
7   GLNHISTHRALAPROVALSERPROHISSER

Samples:

sample_1: SOCS5 JIR, [U-100% 13C; U-100% 15N], 0.3 mM; TCEP 5 mM; Sodium Citrate 20 mM; sodium azide 0.02%; D2O, [U-100% 2H], 6%; H2O 94%

sample_conditions_1: ionic strength: 0.02 M; pH: 4.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.2, Bruker Biospin - collection, processing

NMRPipe v3.0, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView vv8.2.33, Johnson, One Moon Scientific - chemical shift assignment, peak picking

CARA, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

TALOS, Cornilescu, Delaglio and Bax - data analysis

SPARKY, Goddard - data analysis, peak picking

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

OPALp, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

CANDID, Herrmann, Guntert and Wuthrich - NOE assignment

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAA31646 BAF82883 BAG11225 BAG59372
EMBL CAB66830
GB AAB96648 AAD40484 AAH32862 AAH53015 AAI14097
REF NP_001039647 NP_001102744 NP_001120786 NP_001156362 NP_001253857
SP O54928 O75159 Q29RN6
TPG DAA24700
AlphaFold O54928 O75159 Q29RN6

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