BMRB Entry 11095

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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/BMR11095
MolProbity Validation Chart

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Title:
Solution structure of the chimera of the PTB domain of SNT-2 and 19-residue peptide (aa 1571-1589) of hALK
Deposition date:
2010-02-15
Original release date:
2011-02-14
Authors:
Li, H.; Koshiba, S.; Tomizawa, T.; Watanabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.
Citation:

Citation: Li, H.; Koshiba, S.; Tomizawa, T.; Watanabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.. "Solution structure of the chimera of the PTB domain of SNT-2 and 19-residue peptide (aa 1571-1589) of hALK"  .

Assembly members:

Assembly members:
PTB domain and 19-residue peptide, polymer, 153 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: cell free synthesis   Host organism: E. coli - cell free   Vector: P060724-01

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PTB domain and 19-residue peptide: GSSGSSGLNRDSVPDNHPTK FKVTNVDDEGVELGSGVMEL TQSELVLHLHRREAVRWPYL CLRRYGYDSNLFSFESGRRC QTGQGIFAFKCSRAEEIFNL LQDLMQCNSINVMEEPVIIT SGSSGSSGSSGSSGLFRLRH FPCGNVNYGYQQQ

Data sets:
Data typeCount
13C chemical shifts603
15N chemical shifts146
1H chemical shifts955

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1PTB domain and 19-residue peptide1

Entities:

Entity 1, PTB domain and 19-residue peptide 153 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYLEUASNARG
2   ASPSERVALPROASPASNHISPROTHRLYS
3   PHELYSVALTHRASNVALASPASPGLUGLY
4   VALGLULEUGLYSERGLYVALMETGLULEU
5   THRGLNSERGLULEUVALLEUHISLEUHIS
6   ARGARGGLUALAVALARGTRPPROTYRLEU
7   CYSLEUARGARGTYRGLYTYRASPSERASN
8   LEUPHESERPHEGLUSERGLYARGARGCYS
9   GLNTHRGLYGLNGLYILEPHEALAPHELYS
10   CYSSERARGALAGLUGLUILEPHEASNLEU
11   LEUGLNASPLEUMETGLNCYSASNSERILE
12   ASNVALMETGLUGLUPROVALILEILETHR
13   SERGLYSERSERGLYSERSERGLYSERSER
14   GLYSERSERGLYLEUPHEARGLEUARGHIS
15   PHEPROCYSGLYASNVALASNTYRGLYTYR
16   GLNGLNGLN

Samples:

sample_1: PTB domain and 19-residue peptide, [U-13C; U-15N], 1.12 mM; TRIS, [U-2H], 20 mM; sodium chloride 100 mM; DTT, [U-2H], 1 mM; sodium azide 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropiccondition_1
3D 1H-13C NOESYsample_1isotropiccondition_1

Software:

xwinnmr v3.5, Bruker - collection

NMRPipe v20031121, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B.A. - data analysis

Kujira v0.9820, Kobayashi, N. - data analysis

CYANA v2.0.17, Guntert, P. - structure solution

NMR spectrometers:

  • Bruker AVANCE 900 MHz

Related Database Links:

BMRB 11094
PDB
DBJ BAJ20358
EMBL CAG33307
GB AAB92555 AAH10611 ABM83001 ABM86194 ABW05536
REF NP_001162219 NP_001253120 NP_006644 XP_001501207 XP_002914538
SP O43559
AlphaFold O43559

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