BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 15864

Title: Solution structure of 1-112 fragment of human programmed cell death 5 protein   PubMed: 19358820

Authors: Feng, Yingang; Yao, Hongwei; Liu, Dongsheng; Wang, Jinfeng

Citation: Yao, Hongwei; Xu, Lanjun; Feng, Yingang; Liu, Dongsheng; Chen, Yingyu; Wang, Jinfeng. "Structure-function correlation of human programmed cell death 5 protein"  Arch. Biochem. Biophys. 486, 141-149 (2009).

Assembly members:
pdcd5, polymer, 113 residues, 12692.453 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):
pdcd5: GSADEELEALRRQRLAELQA KHGDPGDAAQQEAKHREAEM RNSILAQVLDQSARARLSNL ALVKPEKTKAVENYLIQMAR YGQLSEKVSEQGLIEILKKV SQQTEKTTTVKFN

Data sets:
Data typeCount
13C chemical shifts477
15N chemical shifts114
1H chemical shifts761

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1pdcd51

Entities:

Entity 1, pdcd5 113 residues - 12692.453 Da.

1   GLYSERALAASPGLUGLULEUGLUALALEU
2   ARGARGGLNARGLEUALAGLULEUGLNALA
3   LYSHISGLYASPPROGLYASPALAALAGLN
4   GLNGLUALALYSHISARGGLUALAGLUMET
5   ARGASNSERILELEUALAGLNVALLEUASP
6   GLNSERALAARGALAARGLEUSERASNLEU
7   ALALEUVALLYSPROGLULYSTHRLYSALA
8   VALGLUASNTYRLEUILEGLNMETALAARG
9   TYRGLYGLNLEUSERGLULYSVALSERGLU
10   GLNGLYLEUILEGLUILELEULYSLYSVAL
11   SERGLNGLNTHRGLULYSTHRTHRTHRVAL
12   LYSPHEASN

Samples:

sample_1: pdcd5, [U-13C; U-15N], 1.0-2.0 mM; acetic acid, [U-2H], 100 mM; sodium chloride 100 mM; DSS 0.01%; sodium azide 0.01%

sample_2: pdcd5, [U-13C], 1.0-2.0 mM; acetic acid, [U-2H], 100 mM; sodium chloride 100 mM; DSS 0.01%; sodium azide 0.01%

sample_conditions_1: ionic strength: 0.1 M; pH: 4.7; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

xwinnmr, Bruker Biospin - collection

FELIX, Accelrys Software Inc. - data analysis, processing

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

NMR spectrometers:

  • Bruker DMX 600 MHz

Related Database Links:

PDB
DBJ BAJ20402
EMBL CAG33215 CAH90780
GB AAD11579 AAH15519 AAP35340 AAP36696 AAX36432
REF NP_001125439 NP_001252621 NP_004699 XP_002762025 XP_003275098
SP O14737 Q5RBT0