BMRB Entry 18112

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18112
MolProbity Validation Chart

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Title:
Minimal Constraints Solution NMR Structure of Prospero Homeobox protein 1 from Homo sapiens. Northeast Structural Genomics Consortium Target HR4660B.
Deposition date:
2011-11-29
Original release date:
2011-12-20
Authors:
Rossi, Paolo; Lange, Oliver; Lee, Hsiau-Wei; Maglaqui, Melissa; Janjua, Haleema; Ciccosanti, Colleen; Zhao, Li; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano
Citation:

Citation: Rossi, Paolo; Lange, Oliver; Lee, Hsiau-Wei; Maglaqui, Melissa; Janjua, Haleema; Ciccosanti, Colleen; Zhao, Li; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano. "Minimal Constraints Solution NMR Structure of Prospero Homeobox protein 1 from Homo sapiens. Northeast Structural Genomics Consortium Target HR4660B."  To be published ., .-..

Assembly members:

Assembly members:
HR4660B, polymer, 174 residues, 20723.934 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET15_NESG

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HR4660B: MGHHHHHHSHMAMQEGLSPN HLKKAKLMFFYTRYPSSNML KTYFSDVKFNRCITSQLIKW FSNFREFYYIQMEKYARQAI NDGVTSTEELSITRDCELYR ALNMHYNKANDFEVPERFLE VAQITLREFFNAIIAGKDVD PSWKKAIYKVICKLDSEVPE IFKSPNCLQELLHE

Data sets:
Data typeCount
13C chemical shifts530
15N chemical shifts146
1H chemical shifts690

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HR4660B1

Entities:

Entity 1, HR4660B 174 residues - 20723.934 Da.

1   METGLYHISHISHISHISHISHISSERHIS
2   METALAMETGLNGLUGLYLEUSERPROASN
3   HISLEULYSLYSALALYSLEUMETPHEPHE
4   TYRTHRARGTYRPROSERSERASNMETLEU
5   LYSTHRTYRPHESERASPVALLYSPHEASN
6   ARGCYSILETHRSERGLNLEUILELYSTRP
7   PHESERASNPHEARGGLUPHETYRTYRILE
8   GLNMETGLULYSTYRALAARGGLNALAILE
9   ASNASPGLYVALTHRSERTHRGLUGLULEU
10   SERILETHRARGASPCYSGLULEUTYRARG
11   ALALEUASNMETHISTYRASNLYSALAASN
12   ASPPHEGLUVALPROGLUARGPHELEUGLU
13   VALALAGLNILETHRLEUARGGLUPHEPHE
14   ASNALAILEILEALAGLYLYSASPVALASP
15   PROSERTRPLYSLYSALAILETYRLYSVAL
16   ILECYSLYSLEUASPSERGLUVALPROGLU
17   ILEPHELYSSERPROASNCYSLEUGLNGLU
18   LEULEUHISGLU

Samples:

sample_1: HR4660B, [U-100% 13C; U-100% 15N], 0.96 mM; sodium chloride 200 mM; DTT 10 mM; Calcium Chloride 5 mM; sodium azide 0.02%; MES 20 mM; H2O 95%; D2O 5%

sample_2: HR4660B, [U-13C; U-15N; U-2H], 0.2 mM; sodium chloride 200 mM; DTT 10 mM; Calcium Chloride 5 mM; sodium azide 0.02%; MES 20 mM; H2O 95%; D2O 5%

sample_3: HR4660B, [5% 13C; U-100% 15N], 0.86 mM; sodium chloride 200 mM; DTT 10 mM; Calcium Chloride 5 mM; sodium azide 0.02%; MES 20 mM; H2O 95%; D2O 5%

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D 1H-13C arom NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C-13C HSQC_NOESY_HSQCsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_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

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

TOPSPIN, Bruker Biospin - 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

PSVS, Bhattacharya and Montelione - structure validation

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAC35190 BAE25293 BAF82865 BAG10650 BAG60453
GB AAB30541 AAC32824 AAC50656 AAC59938 AAH24201
REF NP_001005616 NP_001121962 NP_001180161 NP_001247802 NP_001257545
SP P48437 Q91018 Q92786
TPG DAA21012
AlphaFold P48437 Q91018 Q92786

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