| NESG ID: | NAME |
| PDB ID: | |
| Deposition date: | |
| Common Name: | |
| Class: | |
| Length (a.a.): | 452 |
| Organism: | |
| SwissProt / TrEMBL ID: | |
| Oligomerization: | 9 mer |
| Molecular weight: | 50935 |
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Procheck analysis,RMSD calculation and structure superimposition are based on: all residues
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Secondary Structure Elements:
Inter-chain break(s) between 57 & 68, 123 & 134, 190 & 201, 257 & 268, 323 & 334, 389 & 400, 456 & 467, 522 & 533
alpha helices:
beta strands: 14T-16T, 4P-9P, 47L-53L, 22U-24U, 29U-33U, 39A-43A, 14T-16T, 4P-9P, 47L-53L, 22U-24U, 29U-33U, 39A-43A, 15E-16E, 4P-9P, 47L-53L, 18P-24P, 29U-33U, 39A-43A, 14T-16T, 4P-9P, 47L-53L, 22U-24U, 29U-33U, 39A-43A, 14T-17T, 4P-9P, 47L-53L, 22U-24U, 29U-32U, 40T-43T, 14T-17T, 5R-9R, 47L-52L, 22U-24U, 29U-33U, 39A-43A, 14T-17T, 4P-9P, 47L-53L, 22U-24U, 29U-33U, 39A-43A, 13G-17G, 4P-9P, 47L-53L, 22U-24U, 29U-32U, 40T-43T
| Resolution: | 2.700 Å | R-factor: | 0.238 | R-free: | 0.253 |
Structure Factors deposited in the PDB? no
Ramachandran Plot Summary from Procheck
| Most favoured regions | Additionally allowed regions | Generously allowed regions | Disallowed regions |
| 88.9% | 10.6% | 0.5% | 0.0% |
Ramachandran Plot Summary from Richardson Lab's Molprobity
| Most favoured regions | Allowed regions | Disallowed regions | View plot View model summary |
| 93.7% | 4.9% | 1.4% |
Global quality scores
| Program | Verify3D | ProsaII (-ve) | Procheck (phi-psi) | Procheck (all) | MolProbity Clashscore |
| -Raw score | 0.36 | 0.28 | -0.56 | -0.37 | 18.76 |
| Z-score1 | -1.61 | -1.53 | -1.89 | -2.19 | -1.69 |
Close Contacts and Deviations from Ideal Geometry (from PDB validation software)
| Number of close contacts (within 2.2 Å): | 0 |
| RMS deviation for bond angles: | 1.2 ° |
| RMS deviation for bond lengths: | 0.007 Å |
1 With respect to mean and standard deviation for a set of 252 X-ray structures < 500 residues, of resolution <= 1.80 Å, R-factor <= 0.25 and R-free <= 0.28; a positive value indicates a 'better' score
Residue Plot of Ramachandran anlysis(based on data from Richardson Lab's Molprobity)
References:
1. Luthy R, Bowie J U and Eisenberg D, "Assessment of protein models with three-dimensional profiles", Nature 356 (1992): 83-85
2. Bowie J U, Luthy R and Eisenberg D, "A Method to Identify Protein Sequences that Fold into a Known Three-Dimensional Structure", Science 253 (1991): 164-169
3. Sippl M J, "Recognition of Errors in Three-Dimensional Structures of Proteins", Proteins 17 (1993): 355-362
4. Sippl M J, "Calculation of Conformation Ensembles from Potentials of Mean Force", J Mol Biol 213 (1990): 859-883
5. Laskowski R Ai et al, "AQUA and PROCHECK_NMR: Programs for checking the quality of proteins structures solved by NMR", J Biomolec NMR 8 (1996): 477-486
6. Laskowski R A et al "PROCHECK: a program to check the stereochemical quality of protein structures" J Appl Cryst, 26 (1993): 283-291
7. Word J M et al, "Exploring steric constrains on protein mutations using MAGE / PROBE", Prot Sci 9 (2000): 2251-2259
8. Word J M et al, "Asparagine and Glutamine: Using Hydrogen Atom Contacts in the Choice of Side-chain Amide Orientation", J Mol Biol 285 (1999): 1735-1747
9. Word J M et al, "Visualizing and Quantifying Molecular Goodness-of-Fit: Small-probe Contact Dots with Explicit Hydrogens", J Mol Biol 285 (1999): 1711-1733
10. Tejero R and Montelione G T, "PDBStat", unpublished
11. Luthy R, McLachlan A D and Eisenberg D, "Secondary Structure-Based Profiles: Use of Structure-Conserving Scoring Tables in Searching Protein Sequence Databases for Structural Similarities", Proteins 10 (1991): 229-239
12. Richardson D C, Richardson J S, "The kinemage: a tool for scientific communication", Prot Sci 1(1) (1992): 3-9
13. Koradi, R, et al, "MOLMOL: a program for display and analysis of macromolecular structures ", J Mol Graphics 14 (1996): 51-55.
14. Güntert, P, Mumenthaler, C & Wüthrich, K "Torsion angle dynamics for NMR structure calculation with the new program DYANA", J. Mol. Biol 273 (1997): 283-298
15. Lovell S C et al, "Structure validation by Calpha geometry: phi,psi and Cbeta deviation" Proteins (2003) 50: 437-450
16. Kabsch W, Sander C, "Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features", Biopolymers (1983) 22: 2577-2637
17. Bagaria, A., Jaravine, V., Huang, Y.J., Montelione, G.T., and Guntert, P. "Protein structure validation by generalized linear model root-mean-square deviation prediction". Protein Sci 21(2012), 229-238.