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Biological Magnetic Resonance Data Bank


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BMRB Entry 15329

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15329
MolProbity Validation Chart

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Title: Solution NMR structure of Tubulin polymerization-promoting protein family member 3 from Homo sapiens. Northeast Structural Genomics target HR387.   PubMed: TBA

Deposition date: 2007-06-25 Original release date: 2007-07-19

Authors: Aramini, James; Rossi, Paolo; Shastry, Ritu; Nwosu, Chioma; Cunningham, Kellie; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Rajan, P.; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano

Citation: Aramini, James; Rossi, Paolo; Shastry, Ritu; Nwosu, Chioma; Cunningham, Kellie; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Rajan, P.; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano. "Solution NMR structure of Tubulin polymerization-promoting protein family member 3 from Homo sapiens. Northeast Structural Genomics target HR387."  . ., .-..

Assembly members:
hr387, polymer, 184 residues, 20075.820 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):
hr387: MAASTDIAGLEESFRKFAIH GDPKASGQEMNGKNWAKLCK DCKVADGKSVTGTDVDIVFS KVKGKSARVINYEEFKKALE ELATKRFKGKSKEEAFDAIC QLVAGKEPANVGVTKAKTGG AVDRLTDTSRYTGSHKERFD ESGKGKGIAGRQDILDDSGY VSAYKNAGTYDAKVKKLEHH HHHH

Data sets:
Data typeCount
13C chemical shifts755
15N chemical shifts179
1H chemical shifts1114

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1hr3871

Entities:

Entity 1, hr387 184 residues - 20075.820 Da.

Sequence has a M7I mutation. Residues 177-184 constitute a non-native affinity purification tag (LEHHHHHH)

1   METALAALASERTHRASPILEALAGLYLEU
2   GLUGLUSERPHEARGLYSPHEALAILEHIS
3   GLYASPPROLYSALASERGLYGLNGLUMET
4   ASNGLYLYSASNTRPALALYSLEUCYSLYS
5   ASPCYSLYSVALALAASPGLYLYSSERVAL
6   THRGLYTHRASPVALASPILEVALPHESER
7   LYSVALLYSGLYLYSSERALAARGVALILE
8   ASNTYRGLUGLUPHELYSLYSALALEUGLU
9   GLULEUALATHRLYSARGPHELYSGLYLYS
10   SERLYSGLUGLUALAPHEASPALAILECYS
11   GLNLEUVALALAGLYLYSGLUPROALAASN
12   VALGLYVALTHRLYSALALYSTHRGLYGLY
13   ALAVALASPARGLEUTHRASPTHRSERARG
14   TYRTHRGLYSERHISLYSGLUARGPHEASP
15   GLUSERGLYLYSGLYLYSGLYILEALAGLY
16   ARGGLNASPILELEUASPASPSERGLYTYR
17   VALSERALATYRLYSASNALAGLYTHRTYR
18   ASPALALYSVALLYSLYSLEUGLUHISHIS
19   HISHISHISHIS

Samples:

sample_1: hr387, [U-100% 13C; U-100% 15N], 1.04 mM; ammonium acetate 20 mM; sodium chloride 100 mM; DTT 10 mM; calcium chloride 5 mM; sodium azide 0.02%; H2O 95%; D2O 5%

sample_2: hr387, [U-5% 13C; U-100% 15N], 0.7 mM; ammonium acetate 20 mM; calcium chloride 100 mM; DTT 10 mM; calcium chloride 5 mM; sodium azide 0.02%; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 100 mM; pH: 5.5; 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 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D C(CO)NH-TOCSYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D CCH-TOCSY aromaticsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC high res.sample_2isotropicsample_conditions_1

Software:

TOPSPIN v1.3, Bruker Biospin - collection

AutoAssign v2.4.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

SPARKY v3.110, Goddard - data analysis, peak picking

AutoStruct v2.1.1, Huang, Tejero, Powers and Montelione - structure solution

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

X-PLOR NIH v2.11.2, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

PSVS v1.3, Bhattacharya and Montelione - data analysis, structure validation

PDBStat v5.0, Tejero and Montelione - PDB analysis

TALOS, Cornilescu, Delaglio and Bax - dihedral angle constraints

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAB26493 BAB28237 BAE32991 BAE35831
GB AAD27747 AAH00691 AAH10788 ADQ33176 AIC51554
REF NP_001181772 NP_057048 NP_057224 NP_080757 XP_001496480
SP Q9BW30 Q9CRB6

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