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Biological Magnetic Resonance Data Bank


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BMRB Entry 6581

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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/BMR6581
MolProbity Validation Chart

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Title: Sequence-specific 1H, 13C and 15N resonance assignments of hemopoietic cell kinase SH3 domains in complex with a synthetic peptide   PubMed: 17141806

Deposition date: 2005-04-05 Original release date: 2007-02-07

Authors: Schmidt, Holger; Stoldt, Matthias; Tran, Tuyen; Hoffmann, Silke; Willbold, Dieter

Citation: Schmidt, Holger; Hoffmann, Silke; Tran, Tuyen; Stoldt, Matthias; Stangler, Thomas; Wiesehan, Katja; Willbold, Dieter. "Solution structure of a Hck SH3 Domain Ligand Complex Reveals Novel Interaction Modes"  J. Mol. Biol. 365, 1517-1532 (2007).

Assembly members:
hematopoetic cell kinase SH3 domain, polymer, 86 residues, 9487 Da.
PD1 peptide, polymer, 12 residues, 1389 Da.
ACE, non-polymer, 44.053 Da.
NH2, non-polymer, 16.023 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
hematopoetic cell kinase SH3 domain: GPLGSPGPNSHNSNTPGIRE AGSEDIIVVALYDYEAIHHE DLSFQKGDQMVVLEESGEWW KARSLATRKEGYIPSNYVAR VDSLET
PD1 peptide: XHSKYPLPPLPSLX

Data sets:
Data typeCount
1H chemical shifts584
13C chemical shifts358
15N chemical shifts91

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1Hck SH31
2peptide2

Entities:

Entity 1, Hck SH3 86 residues - 9487 Da.

1   GLYPROLEUGLYSERPROGLYPROASNSER
2   HISASNSERASNTHRPROGLYILEARGGLU
3   ALAGLYSERGLUASPILEILEVALVALALA
4   LEUTYRASPTYRGLUALAILEHISHISGLU
5   ASPLEUSERPHEGLNLYSGLYASPGLNMET
6   VALVALLEUGLUGLUSERGLYGLUTRPTRP
7   LYSALAARGSERLEUALATHRARGLYSGLU
8   GLYTYRILEPROSERASNTYRVALALAARG
9   VALASPSERLEUGLUTHR

Entity 2, peptide 12 residues - 1389 Da.

1   ACEHISSERLYSTYRPROLEUPROPROLEU
2   PROSERLEUNH2

Samples:

sample_one: hematopoetic cell kinase SH3 domain, [U-13C; U-15N], 1.3 mM; PD1 peptide 1.3 mM; KPO4 20 mM; NaCl 20 mM

ExpCondition: pH: 6.7; temperature: 298 K; pressure: 1 atm

Experiments:

NameSampleSample stateSample conditions
N-HSQCsample_onenot availableExpCondition
C-HSQCsample_onenot availableExpCondition
HNCACBsample_onenot availableExpCondition
C(CO)NHsample_onenot availableExpCondition
H(CCO)NHsample_onenot availableExpCondition
HNHAsample_onenot availableExpCondition
HNCOsample_onenot availableExpCondition
HCCH-COSYsample_onenot availableExpCondition
HCCH-TOCSYsample_onenot availableExpCondition
N-NOESYsample_onenot availableExpCondition
C-NOESYsample_onenot availableExpCondition
C/N-filtered/edited NOESYsample_onenot availableExpCondition
C/N-double filtered NOESYsample_onenot availableExpCondition
C/N-double filtered COSYsample_onenot availableExpCondition
C/N-double filtered TOCSYsample_onenot availableExpCondition

Software:

No software information available

NMR spectrometers:

  • VARIAN Unity_INOVA 600 MHz
  • VARIAN Unity_INOVA 800 MHz

Related Database Links:

SWISS-PROT P08631
REF XP_514571 NP_002101
GenBank AAI08931 AAH94847 AAH14435 AAA52644 AAA52643
EMBL CAI22967 CAI22966 CAI19695 CAI19694
DBJ BAG60878 BAF83617 BAB15482
PDB
BMRB 4122

Download simulated HSQC data in one of the following formats:
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