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Biological Magnetic Resonance Data Bank


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BMRB Entry 16681

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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/BMR16681
MolProbity Validation Chart

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Title: Solution NMR Structure of the SH3 Domain from the p85beta subunit of Phosphatidylinositol 3-kinase from H.sapiens. Northeast Structural Genomics Consortium Target HR5531E.

Deposition date: 2010-01-15 Original release date: 2010-02-22

Authors: Aramini, James; Ma, Li-Chung; Schauder, Curtis; Everett, John; Montelione, Gaetano

Citation: Aramini, James; Ma, Li-Chung; Schauder, Curtis; Everett, John; Montelione, Gaetano. "Solution NMR Structure of the SH3 Domain from the p85beta subunit of Phosphatidylinositol 3-kinase from H.sapiens. Northeast Structural Genomics Consortium Target HR5531E."  To be published ., .-..

Assembly members:
HR5531E, polymer, 88 residues, 9130.386 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   Vector: HR5531E-1-80-21.1

Entity Sequences (FASTA):
HR5531E: MAGPEGFQYRALYPFRRERP EDLELLPGDVLVVSRAALQA LGVAEGGERCPQSVGWMPGL NERTRQRGDFPGTYVEFLGP LEHHHHHH

Data typeCount
13C chemical shifts350
15N chemical shifts73
1H chemical shifts543

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HR5531E1

Entities:

Entity 1, HR5531E 88 residues - 9130.386 Da.

Contains additional C-terminal LEHHHHHH affinity tag

1   METALAGLYPROGLUGLYPHEGLNTYRARG
2   ALALEUTYRPROPHEARGARGGLUARGPRO
3   GLUASPLEUGLULEULEUPROGLYASPVAL
4   LEUVALVALSERARGALAALALEUGLNALA
5   LEUGLYVALALAGLUGLYGLYGLUARGCYS
6   PROGLNSERVALGLYTRPMETPROGLYLEU
7   ASNGLUARGTHRARGGLNARGGLYASPPHE
8   PROGLYTHRTYRVALGLUPHELEUGLYPRO
9   LEUGLUHISHISHISHISHISHIS

Samples:

sample_1: HR5531E, [U-100% 13C; U-100% 15N], 0.62 mM; sodium phosphate 20 mM; sodium chloride 100 mM; DSS 50 uM; DTT 10 mM; H2O 95%; D2O 5%

sample_2: HR5531E, [U-5% 13C; U-100% 15N], 0.50 mM; sodium phosphate 20 mM; sodium chloride 100 mM; DSS 50 uM; DTT 10 mM; H2O 95%; D2O 5%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_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
3D 1H-13C arom NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HBHANHsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
1D 1H-15N T1 and T2sample_1isotropicsample_conditions_1
2D 1H-13C HSQC high res. (L/V methyl stereoassignment)sample_2isotropicsample_conditions_1
2D 1H-15N hetNOEsample_2isotropicsample_conditions_1

Software:

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

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

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - RPF analysis

PINE v1.0, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY v3.112, Goddard - data analysis, peak picking

TOPSPIN v2.1, Bruker Biospin - collection, data analysis

PSVS v1.4, Bhattacharya and Montelione - structure quality analysis

TALOS vplus, Cornilescu, Delaglio and Bax - dihedral angle constraints

PDBStat v5.1, Tejero and Montelione - PDB coordinate analysis

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAG11075
EMBL CAA56868
GB AAA79510 AAD22671 AAH32647 AAH70082 AAH90249
REF NP_001244981 NP_005018 NP_777001 XP_002761945 XP_003275871
SP O00459 P23726
TPG DAA28159
AlphaFold O00459 P23726

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