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Open data
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Basic information
Entry | Database: PDB / ID: 2crr | ||||||
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Title | Solution structure of ArfGap domain from human SMAP1 | ||||||
![]() | Stromal membrane-associated protein SMAP1B | ||||||
![]() | PROTEIN TRANSPORT / ArfGap domain / SMAP1 / zinc finger / Structural Genomics / NPPSFA / National Project on Protein Structural and Functional Analyses / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | ![]() regulation of clathrin-dependent endocytosis / clathrin binding / GTPase activator activity / positive regulation of erythrocyte differentiation / metal ion binding / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
![]() | Suetake, T. / Sato, M. / Hayashi, F. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
![]() | ![]() Title: Solution structure of ArfGap domain from human SMAP1 Authors: Suetake, T. / Sato, M. / Hayashi, F. / Yokoyama, S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 864.2 KB | Display | ![]() |
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PDB format | ![]() | 722.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 344.5 KB | Display | ![]() |
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Full document | ![]() | 505.8 KB | Display | |
Data in XML | ![]() | 63 KB | Display | |
Data in CIF | ![]() | 76.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 16047.194 Da / Num. of mol.: 1 / Fragment: ArfGap domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: OTTHUMP00000039271, GD:RP1-104A17.1-001, RP1-104A17.1-004 Plasmid: P040628-12 / References: UniProt: Q6PK24, UniProt: Q8IYB5*PLUS |
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#2: Chemical | ChemComp-ZN / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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Sample preparation
Details | Contents: 1.27mM 13C, 15N-labeled protein; 20mM d-Tris-HCl; 100mM NaCl; 2mM d10-DTT; 0.02% NaN3; 0.01mM ZnCl2; 90% H2O, 10% D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 100mM NaCl / pH: 7.0 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz |
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Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violation, target function Conformers calculated total number: 100 / Conformers submitted total number: 20 |