BMRB Entry 18662

Title:
Solution NMR structure of SH3 domain of growth arrest-specific protein 7 (GAS7)(fragment 1-60)from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR8574A
Deposition date:
2012-08-15
Original release date:
2012-10-09
Authors:
Yang, Yunhuang; Ramelot, Theresa; Dan, Lee; Kohan, Eitan; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Everett, John; Montelione, Gaetano; Kennedy, Michael
Citation:

Citation: Yang, Yunhuang; Ramelot, Theresa; Dan, Lee; Kohan, Eitan; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Everett, John; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of SH3 domain of growth arrest-specific protein 7 (GAS7) (fragment 1-60)from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR8574A"  To be published ., .-..

Assembly members:

Assembly members:
SH3_domain_of_GAS7, polymer, 60 residues, 6718.633 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: HR8574A-1-60-AV6HT.2

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SH3_domain_of_GAS7: MSGARCRTLYPFSGERHGQG LRFAAGELITLLQVPDGGWW EGEKEDGLRGWFPASYVQLL

Data sets:
Data typeCount
13C chemical shifts266
15N chemical shifts64
1H chemical shifts413

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SH3_domain_of_GAS71

Entities:

Entity 1, SH3_domain_of_GAS7 60 residues - 6718.633 Da.

1   METSERGLYALAARGCYSARGTHRLEUTYR
2   PROPHESERGLYGLUARGHISGLYGLNGLY
3   LEUARGPHEALAALAGLYGLULEUILETHR
4   LEULEUGLNVALPROASPGLYGLYTRPTRP
5   GLUGLYGLULYSGLUASPGLYLEUARGGLY
6   TRPPHEPROALASERTYRVALGLNLEULEU

Samples:

NC_sample: SH3_domain_of_GAS7, [U-100% 13C; U-100% 15N], 0.26 ± 0.02 mM; NaN3 0.02 ± 0.001 %; DTT 10 ± 0.05 mM; CaCL2 5 ± 0.025 mM; NaCL 100 ± 0.5 mM; Proteinase Inhibitors 1 x; MES pH 6.5 20 ± 0.01 mM; D2O 10 ± 0.005 %; DSS 50 ± 0.025 uM; H2O 90 ± 0.005 %

NC5_sample: SH3_domain_of_GAS7, [U-10% 13C; U-100% 15N], 0.45 ± 0.02 mM; NaN3 0.02 ± 0.001 %; DTT 10 ± 0.05 mM; CaCL2 5 ± 0.025 mM; NaCL 100 ± 0.5 mM; Proteinase Inhibitors 1 x; MES pH 6.5 20 ± 0.01 mM; D2O 10 ± 0.005 %; DSS 50 ± 0.025 uM; H2O 90 ± 0.005 %

NC_sample_in_D2O: SH3_domain_of_GAS7, [U-100% 13C; U-100% 15N], 0.26 ± 0.02 mM; NaN3 0.02 ± 0.001 %; DTT 10 ± 0.05 mM; CaCL2 5 ± 0.025 mM; NaCL 100 ± 0.5 mM; Proteinase Inhibitors 1 x; MES pH 6.5 20 ± 0.01 mM; DSS 50 ± 0.025 uM; D2O 100 ± 0.005 %

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNC_sampleisotropicsample_conditions_1
2D 1H-13C HSQCNC_sampleisotropicsample_conditions_1
3D HNCONC_sampleisotropicsample_conditions_1
3D CBCA(CO)NHNC_sampleisotropicsample_conditions_1
3D HNCACBNC_sampleisotropicsample_conditions_1
3D 1H-15N NOESYNC_sampleisotropicsample_conditions_1
3D 1H-13C NOESY aliphaticNC_sampleisotropicsample_conditions_1
3D 1H-13C NOESY aromaticNC_sampleisotropicsample_conditions_1
4D CC-NOESYNC_sample_in_D2Oisotropicsample_conditions_1
3D HNCANC_sampleisotropicsample_conditions_1
3D HN(CO)CANC_sampleisotropicsample_conditions_1
3D H(CCO)NHNC_sampleisotropicsample_conditions_1
3D C(CO)NHNC_sampleisotropicsample_conditions_1
3D HBHA(CO)NHNC_sampleisotropicsample_conditions_1
3D HCCH-TOCSYNC_sampleisotropicsample_conditions_1
3D HCCH-COSYNC_sampleisotropicsample_conditions_1
3D HNHANC_sampleisotropicsample_conditions_1
3D (H)CCH-TOCSYNC_sample_in_D2Oisotropicsample_conditions_1
2D 1H-13C HSQC-aromNC_sampleisotropicsample_conditions_1
2D 1H-15N HSQC-HistidineNC_sampleisotropicsample_conditions_1
2D 1H-13C HSQC - NC5NC5_sampleisotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinemen,structure solution,geometry optimization

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

AutoStruct v2.1, Huang, Tejero, Powers and Montelione - data analysis,refinement

AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - data analysis,chemical shift assignment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

SPARKY, Goddard - data analysis

TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization

PSVS, Bhattacharya, Montelione - structure validation

NMR spectrometers:

  • Bruker Avance 850 MHz
  • Varian INOVA 600 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAC21639 BAE89369
GB AAP92798 EAW90011 ELK03871 ELW53078
REF NP_958839 XP_002747958 XP_002827074 XP_003274725 XP_003315707
SP O60861
AlphaFold O60861

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