BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 19749

Title: Solution NMR structure of N-terminal domain (SH2 domain) of human Inositol polyphosphate phosphatase-like protein 1 (INPPL1) (fragment 20-117), Northeast Structural Genomics Consortium Target HR9134A.

Authors: Yang, Yunhuang; Ramelot, Theresa; Janjua, Haleema; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael

Citation: Yang, Yunhuang; Ramelot, Theresa; Janjua, Haleema; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of N-terminal domain (SH2 domain) of human Inositol polyphosphate phosphatase-like protein 1 (INPPL1) (fragment 20-117), Northeast Structural Genomics Consortium Target HR9134A."  To be published ., .-..

Assembly members:
HR9134A, polymer, 109 residues, 12198.978 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):
HR9134A: MGHHHHHHSHMSWYHRDLSR AAAEELLARAGRDGSFLVRD SESVAGAFALCVLYQKHVHT YRILPDGEDFLAVQTSQGVP VRRFQTLGELIGLYAQPNQG LVCALLLPV

Data sets:
Data typeCount
13C chemical shifts427
15N chemical shifts112
1H chemical shifts704

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HR9134A1

Entities:

Entity 1, HR9134A 109 residues - 12198.978 Da.

1   METGLYHISHISHISHISHISHISSERHIS
2   METSERTRPTYRHISARGASPLEUSERARG
3   ALAALAALAGLUGLULEULEUALAARGALA
4   GLYARGASPGLYSERPHELEUVALARGASP
5   SERGLUSERVALALAGLYALAPHEALALEU
6   CYSVALLEUTYRGLNLYSHISVALHISTHR
7   TYRARGILELEUPROASPGLYGLUASPPHE
8   LEUALAVALGLNTHRSERGLNGLYVALPRO
9   VALARGARGPHEGLNTHRLEUGLYGLULEU
10   ILEGLYLEUTYRALAGLNPROASNGLNGLY
11   LEUVALCYSALALEULEULEUPROVAL

Samples:

sample_1: HR9134A, [U-100% 13C; U-100% 15N], 0.58 mM; H2O 90%; D2O 10%

sample_2: HR9134A, [U-100% 13C; U-100% 15N], 0.58 mM; D2O 100%

sample_3: HR9134A, [U-5% 13C; U-100% 15N], 1.05 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D 1H-13C arom NOESYsample_3isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1
3D HN(CO)CAsample_3isotropicsample_conditions_1
3D HNCAsample_3isotropicsample_conditions_1
2D 1H-15N HSQC NH2 onlysample_3isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_3isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQC histidinesample_3isotropicsample_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

AutoStructure 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

XEASY, Bartels et al. - data analysis,peak picking,chemical shift assignment

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

PALES, PALES (Zweckstetter, Bax) - geometry optimization

REDCAT, Valafar, Prestegard - geometry optimization

PSVS, Bhattacharya, Montelione - structure validation

NMR spectrometers:

  • Bruker Avance 850 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAA81818 BAA82308
EMBL CAA74743
GB AAF28187 AAH63080 AAI40854 ADG23056 EAW74854
REF NP_001116211 NP_001177208 NP_001178105 NP_001247768 NP_001257772
SP O15357 Q6P549 Q9WVR3
TPG DAA21965