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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/BMR16640
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
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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 Vector: BL21
Entity Sequences (FASTA):
HR3102A: MGHHHHHHSHPNEEARLDIL
KIHSRKMNLTRGINLRKIAE
LMPGASGAEVKGVCTEAGMY
ALRERRVHVTQEDFEMAVAK
VMQKDS
Data type | Count |
13C chemical shifts | 259 |
15N chemical shifts | 84 |
1H chemical shifts | 564 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | HR3102A | 1 |
Entity 1, HR3102A 86 residues - 9797.391 Da.
1 | MET | GLY | HIS | HIS | HIS | HIS | HIS | HIS | SER | HIS | ||||
2 | PRO | ASN | GLU | GLU | ALA | ARG | LEU | ASP | ILE | LEU | ||||
3 | LYS | ILE | HIS | SER | ARG | LYS | MET | ASN | LEU | THR | ||||
4 | ARG | GLY | ILE | ASN | LEU | ARG | LYS | ILE | ALA | GLU | ||||
5 | LEU | MET | PRO | GLY | ALA | SER | GLY | ALA | GLU | VAL | ||||
6 | LYS | GLY | VAL | CYS | THR | GLU | ALA | GLY | MET | TYR | ||||
7 | ALA | LEU | ARG | GLU | ARG | ARG | VAL | HIS | VAL | THR | ||||
8 | GLN | GLU | ASP | PHE | GLU | MET | ALA | VAL | ALA | LYS | ||||
9 | VAL | MET | GLN | LYS | ASP | SER |
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
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C arom NOESY | sample_1 | isotropic | sample_conditions_1 |
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
GFT HABCABcoNHN | sample_1 | isotropic | sample_conditions_1 |
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
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 |
AlphaFold | O18413 P46470 P54814 P62194 P62195 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks