BMRB Entry 16719

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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/BMR16719
MolProbity Validation Chart

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Title:
Solution structure of Cytotoxic T-Lymphocyte Antigent-2(CTLA-2) like protein, Crammer
Deposition date:
2010-02-11
Original release date:
2011-12-20
Authors:
Tzeng, Tain-Sheng; Cheng, Chao-Sheng; Liu, Yu-Nan; Shih, Min-fang; Lyu, Ping-Chiang
Citation:

Citation: Tseng, Tien-Sheng; Cheng, Chao-Sheng; Chen, Dian-Jiun; Shih, Min-Fang; Liu, Yu-Nan; Hsu, Shang-Te Danny; Lyu, Ping-Chiang. "A molten globule-to-ordered structure transition of Drosophila melanogaster crammer is required for its ability to inhibit cathepsin."  Biochem. J. 442, 563-572 (2012).
PubMed: 22150223

Assembly members:

Assembly members:
Crammer, polymer, 80 residues, 9595.900 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: PAED4

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Crammer: MMSLVSDEEWVEYKSKFDKN YEAEEDLMRRRIYAESKARI EEHNRKFEKGEVTWKMGINH LADLTPEEFAQRSGKKVPPN

Data sets:
Data typeCount
13C chemical shifts215
15N chemical shifts73
1H chemical shifts351

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1Crammer1

Entities:

Entity 1, Crammer 80 residues - 9595.900 Da.

1   METMETSERLEUVALSERASPGLUGLUTRP
2   VALGLUTYRLYSSERLYSPHEASPLYSASN
3   TYRGLUALAGLUGLUASPLEUMETARGARG
4   ARGILETYRALAGLUSERLYSALAARGILE
5   GLUGLUHISASNARGLYSPHEGLULYSGLY
6   GLUVALTHRTRPLYSMETGLYILEASNHIS
7   LEUALAASPLEUTHRPROGLUGLUPHEALA
8   GLNARGSERGLYLYSLYSVALPROPROASN

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 10 mM; Citric acid-phosphate 10 mM

sample_2: entity, [U-100% 15N], 10 mM; Citric acid-phosphate 10 mM

sample_3: entity 10 mM; Citric acid-phosphate 10 mM

sample_conditions_1: pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D DQF-COSYsample_3isotropicsample_conditions_1
2D 1H-1H COSYsample_3isotropicsample_conditions_1
2D 1H-1H NOESYsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment, chemical shift calculation, processing

PSVS, Bhattacharya and Montelione - data analysis, structure solution

Molmol, Koradi, Billeter and Wuthrich - data analysis, structure solution

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - data analysis, structure solution

NMR spectrometers:

  • Bruker AMX 600 MHz

Related Database Links:

BMRB 17367
PDB
GB AAF57567 ACJ13252 EDV55205 EDW48595 EDX07811
REF NP_611420 XP_001974805 XP_002034582 XP_002082226

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