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 16640

Title: Solution NMR Structure of 26S protease regulatory subunit 8 from H.sapiens, Northeast Structural Genomics Consortium Target Target HR3102A

Authors: Liu, G.; Janjua, J.; Xiao, R.; Ciccosanti, C.; Shastry, R.; Everett, J.; Nair, R.; Acton, T; Rost, B.; Montelione, G.

Citation: Liu, G.; Janjua, J.; Xiao, R.; Ciccosanti, C.; Shastry, R.; Everett, J.; Nair, R.; Acton, T.; Rost, B.; Montelione, G.. "Solution NMR Structure of 26S protease regulatory subunit 8 from H.sapiens, Northeast Structural Genomics Consortium Target HR3102A"  To be published ., .-..

Assembly members:
HR3102A, polymer, 86 residues, 9797.391 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):
HR3102A: MGHHHHHHSHPNEEARLDIL KIHSRKMNLTRGINLRKIAE LMPGASGAEVKGVCTEAGMY ALRERRVHVTQEDFEMAVAK VMQKDS

Data sets:
Data typeCount
13C chemical shifts259
15N chemical shifts84
1H chemical shifts564

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HR3102A1

Entities:

Entity 1, HR3102A 86 residues - 9797.391 Da.

1   METGLYHISHISHISHISHISHISSERHIS
2   PROASNGLUGLUALAARGLEUASPILELEU
3   LYSILEHISSERARGLYSMETASNLEUTHR
4   ARGGLYILEASNLEUARGLYSILEALAGLU
5   LEUMETPROGLYALASERGLYALAGLUVAL
6   LYSGLYVALCYSTHRGLUALAGLYMETTYR
7   ALALEUARGGLUARGARGVALHISVALTHR
8   GLNGLUASPPHEGLUMETALAVALALALYS
9   VALMETGLNLYSASPSER

Samples:

sample_1: HR3102A, [U-100% 13C; U-100% 15N], 0.82 mM; H2O 95%; D2O 5%

sample_2: HR3102A, [U-10% 13C; U-100% 15N], 0.52 mM; H2O 95%; D2O 5%

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-13C arom NOESYsample_1isotropicsample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
GFT HABCABcoNHNsample_1isotropicsample_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

AutoStruct v2.1, Huang, Tejero, Powers and Montelione - data analysis,refinement

AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - data analysis,chemical shift assignment

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

XEASY, Bartels et al. - data analysis,peak picking,chemical shift assignment

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAA07919 BAA11938 BAA22933 BAA22935 BAB26990
EMBL CAA57512 CAA61863 CAA61864 CAA90961 CAG12637
GB AAB88187 AAC19266 AAC41735 AAC46996 AAC48284
PRF 2106382A 2111282A
REF NP_001003740 NP_001081635 NP_001085482 NP_001127417 NP_001134720
SP O18413 P46470 P54814 P62194 P62195
TPG DAA18341