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Biological Magnetic Resonance Data Bank


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BMRB Entry 16338

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16338
MolProbity Validation Chart

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Title: Solution NMR structure of the N-terminal Ubiquitin-like Domain from Tubulin-binding Cofactor B, CG11242, from Drosophila melanogaster. Northeast Structural Genomics Consortium Target FR629A (residues 8-92).

Deposition date: 2009-06-08 Original release date: 2009-07-08

Authors: Ramelot, Theresa; Cort, John; Shastry, Ritu; Ciccosanti, Colleen; Jiang, Mei; Nair, R; Rost, Burkhard; Swapna, G.V.T.; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael

Citation: Ramelot, Theresa; Cort, John; Shastry, Ritu; Ciccosanti, Colleen; Jiang, Mei; Nair, R; Rost, Burkhard; Swapna, G.V.T.; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of the N-terminal Ubiquitin-like Domain from Tubulin-binding Cofactor B, CG11242, from Drosophila melanogaster. Northeast Structural Genomics Consortium Target FR629A (residues 8-92)."  Not known ., .-..

Assembly members:
CG11242, polymer, 95 residues, 10300 Da.

Natural source:   Common Name: fruit fly   Taxonomy ID: 7227   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Drosophila melanogaster

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

Entity Sequences (FASTA):
CG11242: MGHHHHHHSHGKSDFIKVNV SNSHNDAVAFEVKLAKDLTV AQLKTKLEILTGGCAGTMKV QVFKGDTCVSTMDNNDAQLG YYANSDGLRLHVVDS

Data sets:
Data typeCount
13C chemical shifts373
15N chemical shifts96
1H chemical shifts588

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CG112421

Entities:

Entity 1, CG11242 95 residues - 10300 Da.

8 non-native residues at N-teriminus (MGHHHHHH)

1   METGLYHISHISHISHISHISHISSERHIS
2   GLYLYSSERASPPHEILELYSVALASNVAL
3   SERASNSERHISASNASPALAVALALAPHE
4   GLUVALLYSLEUALALYSASPLEUTHRVAL
5   ALAGLNLEULYSTHRLYSLEUGLUILELEU
6   THRGLYGLYCYSALAGLYTHRMETLYSVAL
7   GLNVALPHELYSGLYASPTHRCYSVALSER
8   THRMETASPASNASNASPALAGLNLEUGLY
9   TYRTYRALAASNSERASPGLYLEUARGLEU
10   HISVALVALASPSER

Samples:

NC_sample: MES 50 ± 2.5 mM; arginine 50 ± 2.5 mM; DTT 10 ± .5 mM; sodium azide 0.02 ± .001 %; entity, [U-100% 13C; U-100% 15N], 1.1 ± .05 mM; DSS 50 ± 2.5 uM; H2O 95%; D2O 5%

NC5_sample: MES 50 ± 2.5 mM; arginine 50 ± 2.5 mM; DTT 10 ± .5 mM; sodium azide 0.02 ± .001 %; entity, [U-5% 13C; U-100% 15N], 1.0 ± .05 mM; DSS 50 ± 2.5 uM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 50 mM; pH: 6.0; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNC_sampleisotropicsample_conditions_1
2D 1H-13C HSQC aliphaticNC_sampleisotropicsample_conditions_1
3D 1H-15N NOESYNC_sampleisotropicsample_conditions_1
3D 1H-13C NOESY aliphaticNC_sampleisotropicsample_conditions_1
3D HNCONC_sampleisotropicsample_conditions_1
3D HNCANC_sampleisotropicsample_conditions_1
3D CBCA(CO)NHNC_sampleisotropicsample_conditions_1
3D HNCACBNC_sampleisotropicsample_conditions_1
3D C(CO)NHNC_sampleisotropicsample_conditions_1
3D HBHA(CO)NHNC_sampleisotropicsample_conditions_1
3D HCCH-TOCSYNC_sampleisotropicsample_conditions_1
3D CCH-TOCSYNC_sampleisotropicsample_conditions_1
2D 1H-13C HSQCNC5_sampleisotropicsample_conditions_1
2D 1H-15N HSQCNC5_sampleisotropicsample_conditions_1
2D 1H-13C HSQC aromaticNC_sampleisotropicsample_conditions_1
3D 1H-13C NOESY aromaticNC_sampleisotropicsample_conditions_1

Software:

NMRPipe v2008, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

VNMR v6.1C, Varian - collection

TOPSPIN v2.1.3, Bruker Biospin - collection

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

X-PLOR NIH v2.20, Schwieters, Kuszewski, Tjandra and Clore - structure solution

SPARKY v3.113, Goddard - data analysis

PSVS v1.3, Bhattacharya and Montelione - structure validation

AutoAssign v2.3.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

PDBStat v5.1, (PDBStat) R. Tejero, G.T. Montelione - data analysis

NMR spectrometers:

  • Varian INOVA 500 MHz
  • Bruker AvanceIII 850 MHz

Related Database Links:

PDB
GB AAF57546 AAL29037 ACL84771 ACL89668 EDW48612
REF NP_611425 XP_002034599 XP_002076374

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