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- PDB-2kl7: Solution NMR Structure of the EGF-like 1 Domain of Human Fibulin-... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2kl7 | ||||||
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Title | Solution NMR Structure of the EGF-like 1 Domain of Human Fibulin-4. Northeast Structural Genomics Target HR6275 | ||||||
![]() | Fibulin-4 | ||||||
![]() | SIGNALING PROTEIN / STRUCTURAL PROTEIN / secreted / Calcium / Disease mutation / Disulfide bond / EGF-like domain / Glycoprotein / Polymorphism / Structural Genomics / PSI-2 / Protein Structure Initiative / Northeast Structural Genomics Consortium / NESG / METAL BINDING PROTEIN | ||||||
Function / homology | ![]() elastic fiber assembly / Molecules associated with elastic fibres / extracellular matrix structural constituent / basement membrane / extracellular vesicle / collagen-containing extracellular matrix / calcium ion binding / extracellular exosome / extracellular region Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / molecular dynamics | ||||||
Model details | lowest energy, model 1 | ||||||
![]() | Rossi, P. / Chiang, Y. / Anderson, S. / Montelione, G.T. / Northeast Structural Genomics Consortium (NESG) | ||||||
![]() | ![]() Title: Solution NMR Structure of the EGF-like 1 Domain of Human Fibulin-4. Northeast Structural Genomics Target HR6275 Authors: Rossi, P. / Chiang, Y. / Anderson, S. / Montelione, G.T. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 447.4 KB | Display | ![]() |
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PDB format | ![]() | 390.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 387.6 KB | Display | ![]() |
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Full document | ![]() | 443.1 KB | Display | |
Data in XML | ![]() | 22 KB | Display | |
Data in CIF | ![]() | 37.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data | |
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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: 7576.424 Da / Num. of mol.: 1 / Fragment: EGF-like 1 domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: MONOMER BY GEL FILTRATION CHROMATOGRAPHY/LIGHT SCATTERING AND BY NMR. T1/T2(CPMG) T1=664.9 MS T2=128.48 MS TAUC=4.8 NS. CONSISTENT WITH MOLECULAR WEIGHT OF MONOMERIC UNIT. STRUCTURE DETERMINED ...Text: MONOMER BY GEL FILTRATION CHROMATOGRAPHY/LIGHT SCATTERING AND BY NMR. T1/T2(CPMG) T1=664.9 MS T2=128.48 MS TAUC=4.8 NS. CONSISTENT WITH MOLECULAR WEIGHT OF MONOMERIC UNIT. STRUCTURE DETERMINED BY TRIPLE RESONANCE NMR SPECTROSCOPY. ASSIGNMENT STATS (ALL RESIDUES INCLUDED): BACKBONE 91.89%, SIDECHAIN 83.74%, AROMATIC (SC) 100%. UNAMBIGUOUS SIDECHAIN NH2 100%. |
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Sample preparation
Details |
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Sample |
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Sample conditions | Ionic strength: 0.15 / pH: 6.5 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: molecular dynamics / Software ordinal: 1 Details: NOESY ASSIGNMENTS BY CYANA-3.0. 20 OF 100 STRUCTURES LOWEST TARGET FUNCTION SELECTED WITH CYANA-3.0. SELECTED MODELS ARE FURTHER REFINED USING CNS IN EXPLICIT WATER SHELL (NILGES PROTOCOL ...Details: NOESY ASSIGNMENTS BY CYANA-3.0. 20 OF 100 STRUCTURES LOWEST TARGET FUNCTION SELECTED WITH CYANA-3.0. SELECTED MODELS ARE FURTHER REFINED USING CNS IN EXPLICIT WATER SHELL (NILGES PROTOCOL WITH PARAM19). STRUCTURE BASED ON 776 NOE, 106 DIHE. MAX NOE VIOLATION: 0.23 A (1MODEL); MAX DIHE VIOLATION: 7.1 DEG. 1 TOTAL CLOSE CONTACTS PER 20 MODELS. STRUCTURE QUALITY FACTOR (PSVS 1.3): ORDERED RESIDUES RANGES: 11-34,53-66 (FINDCORE). SECONDARY STRUCTURE - BETA STRANDS: 17-21, 25-29, 61-63. RMSD(ANG): BACKBONE 1.0, ALL HEAVY ATOMS 1.3. RAMA. DISTRIBUTION: 94.1/5.9/0.0/0.0. PROCHECK (PSI-PHI): -0.38/-1.18 (RAW/Z), PROCHECK (ALL): -0.22/-1.30 (RAW/Z), MOLPROBITY CLASH: 16.14/-1.24 (RAW/Z). RPF SCORES ALL ASSIGNED RESIDUES (FIT OF NOESY PEAKLISTS TO STRUCTURE): RECALL: 0.880, PRECISION: 0.916, F-MEASURE: 0.898, DP-SCORE: 0.651. | ||||||||||||||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 20 |