[English] 日本語
![](img/lk-miru.gif)
- PDB-1a9n: CRYSTAL STRUCTURE OF THE SPLICEOSOMAL U2B''-U2A' PROTEIN COMPLEX ... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1a9n | ||||||
---|---|---|---|---|---|---|---|
Title | CRYSTAL STRUCTURE OF THE SPLICEOSOMAL U2B''-U2A' PROTEIN COMPLEX BOUND TO A FRAGMENT OF U2 SMALL NUCLEAR RNA | ||||||
![]() |
| ||||||
![]() | RNA BINDING PROTEIN/RNA / COMPLEX (NUCLEAR PROTEIN-RNA) / RNA / SNRNP / RIBONUCLEOPROTEIN / RNA BINDING PROTEIN-RNA COMPLEX | ||||||
Function / homology | ![]() small nuclear ribonucleoprotein complex / U2-type spliceosomal complex / U2-type precatalytic spliceosome / U2-type prespliceosome assembly / U2-type catalytic step 2 spliceosome / U2 snRNP / U1 snRNP / U2 snRNA binding / U1 snRNA binding / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation ...small nuclear ribonucleoprotein complex / U2-type spliceosomal complex / U2-type precatalytic spliceosome / U2-type prespliceosome assembly / U2-type catalytic step 2 spliceosome / U2 snRNP / U1 snRNP / U2 snRNA binding / U1 snRNA binding / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / catalytic step 2 spliceosome / mRNA Splicing - Major Pathway / RNA splicing / spliceosomal complex / fibrillar center / mRNA splicing, via spliceosome / cytoplasmic ribonucleoprotein granule / spermatogenesis / nuclear body / nuclear speck / RNA binding / nucleoplasm / nucleus Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Price, S.R. / Evans, P.R. / Nagai, K. | ||||||
![]() | ![]() Title: Crystal structure of the spliceosomal U2B"-U2A' protein complex bound to a fragment of U2 small nuclear RNA. Authors: Price, S.R. / Evans, P.R. / Nagai, K. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 135.7 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 110.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 487.7 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 515.1 KB | Display | |
Data in XML | ![]() | 23.8 KB | Display | |
Data in CIF | ![]() | 32.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| ||||||||||||||||
2 | ![]()
| ||||||||||||||||
Unit cell |
| ||||||||||||||||
Noncrystallographic symmetry (NCS) | NCS oper:
|
-
Components
#1: RNA chain | Mass: 7622.534 Da / Num. of mol.: 2 / Fragment: U2 HAIRPIN IV Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() #2: Protein | Mass: 20226.555 Da / Num. of mol.: 2 Fragment: N-TERMINAL DOMAIN, RESIDUES 1 - 176 OF U2 A', A COMPONENT OF U2 SNRNP Mutation: C89D, S119C Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P09661 #3: Protein | Mass: 11149.093 Da / Num. of mol.: 2 Fragment: RESIDUES 4 - 99 OF U2 B'', A COMPONENT OF U2 SNRNP Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P08579 Sequence details | THE NUMBERING USED IN CHAINS B, D, Q, AND R IS CHOSEN TO CORRESPOND TO THE HOMOLOGOUS U1A FOUND IN ...THE NUMBERING USED IN CHAINS B, D, Q, AND R IS CHOSEN TO CORRESPOND | |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.69 Å3/Da / Density % sol: 42 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | pH: 7.3 Details: 50MM NACL, 9MM MGCL2, 0.25 MM SPERMINE, 0.25% N-OCTYL-BETA-D-GLUCOPYRANOSIDE, 50MM TRIS-CL PH 7.3, 1% PEG600 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Sep 15, 1996 / Details: TOROIDAL MIRROR |
Radiation | Monochromator: DOUBLE SI (111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 2.38→25.9 Å / Num. obs: 32587 / % possible obs: 94.7 % / Observed criterion σ(I): 6 / Redundancy: 4.2 % / Biso Wilson estimate: 59 Å2 / Rmerge(I) obs: 0.061 / Rsym value: 0.061 / Net I/σ(I): 8.3 |
Reflection shell | Resolution: 2.38→2.51 Å / Redundancy: 2.5 % / Rmerge(I) obs: 0.236 / Mean I/σ(I) obs: 3 / Rsym value: 0.236 / % possible all: 95 |
Reflection shell | *PLUS % possible obs: 74 % |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]()
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 55 Å2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.38→15 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.282 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |