CNRS Nantes University UFIP UFIP
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***  HYDROLASE 18-AUG-15 5D8Z  ***

elNémo ID: 21031823295283691

Job options:

ID        	=	 21031823295283691
JOBID     	=	 HYDROLASE 18-AUG-15 5D8Z
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    HYDROLASE                               18-AUG-15   5D8Z              
TITLE     STRUCTRUE OF A LUCIDUM PROTEIN                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENDOGLUCANASE;                                             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: GANODERMA LUCIDUM;                              
SOURCE   3 ORGANISM_TAXID: 5315;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    GH5 FAMILY, GANODERMA LUCIDUM, ENDOGLUCANASE, HYDROLASE               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.GUO,Q.LI,N.SHANG,G.LIU,T.P.KO,C.C.CHEN,W.LIU                        
REVDAT   3   29-JUL-20 5D8Z    1       COMPND REMARK HET    HETNAM              
REVDAT   3 2                   1       FORMUL LINK   SITE   ATOM                
REVDAT   2   23-MAY-18 5D8Z    1       REMARK                                   
REVDAT   1   29-JUN-16 5D8Z    0                                                
JRNL        AUTH   G.LIU,Q.LI,N.SHANG,J.W.HUANG,T.P.KO,W.LIU,Y.ZHENG,X.HAN,     
JRNL        AUTH 2 Y.CHEN,C.C.CHEN,J.JIN,R.T.GUO                                
JRNL        TITL   FUNCTIONAL AND STRUCTURAL ANALYSES OF A                      
JRNL        TITL 2 1,4-BETA-ENDOGLUCANASE FROM GANODERMA LUCIDUM.               
JRNL        REF    ENZYME.MICROB.TECHNOL.        V.  86    67 2016              
JRNL        REFN                   ISSN 0141-0229                               
JRNL        PMID   26992795                                                     
JRNL        DOI    10.1016/J.ENZMICTEC.2016.01.013                              
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0049                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 20753                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.182                           
REMARK   3   R VALUE            (WORKING SET) : 0.179                           
REMARK   3   FREE R VALUE                     : 0.236                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1132                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.77                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1389                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 86.25                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3170                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 66                           
REMARK   3   BIN FREE R VALUE                    : 0.3590                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4864                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 46                                      
REMARK   3   SOLVENT ATOMS            : 73                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 46.03                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.86000                                              
REMARK   3    B22 (A**2) : -4.22000                                             
REMARK   3    B33 (A**2) : 2.36000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 1.261         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.325         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.240         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.887        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.920                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5043 ; 0.013 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  4384 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6910 ; 1.598 ; 1.915       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 10056 ; 0.908 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   646 ; 7.756 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   254 ;43.123 ;25.984       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   662 ;16.887 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    10 ;19.399 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   752 ; 0.095 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6058 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1232 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2590 ; 3.078 ; 4.531       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2589 ; 3.072 ; 4.529       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3234 ; 4.778 ; 6.793       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  3235 ; 4.778 ; 6.795       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2453 ; 3.747 ; 4.823       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  2453 ; 3.739 ; 4.823       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  3677 ; 5.721 ; 7.133       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  5932 ; 7.800 ;37.140       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  5924 ; 7.769 ;37.124       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3   POSITIONS                                                          
REMARK   4                                                                      
REMARK   4 5D8Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-AUG-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000212865.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-MAY-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSRRC                              
REMARK 200  BEAMLINE                       : BL13B1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97622                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21889                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.4                               
REMARK 200  DATA REDUNDANCY                : 7.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 20.4100                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 3QR3                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.66                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M MAGNESIUM CHLORIDE HEXAHYDRATE,     
REMARK 280  0.1M BIS-TRIS PH 5.5, 25% W/V POLYETHYLENE GLYCOL 3350, VAPOR       
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       41.79250            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       41.79250            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       42.21300            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      118.19950            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       42.21300            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      118.19950            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       41.79250            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       42.21300            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      118.19950            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       41.79250            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       42.21300            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      118.19950            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLN A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     THR A     3                                                      
REMARK 465     VAL A     4                                                      
REMARK 465     PRO A     5                                                      
REMARK 465     ALA A     6                                                      
REMARK 465     TRP A     7                                                      
REMARK 465     GLY A     8                                                      
REMARK 465     GLN A     9                                                      
REMARK 465     CYS A    10                                                      
REMARK 465     GLY A    11                                                      
REMARK 465     GLY A    12                                                      
REMARK 465     SER A    13                                                      
REMARK 465     VAL A    14                                                      
REMARK 465     PRO A    15                                                      
REMARK 465     ALA A    16                                                      
REMARK 465     SER A    17                                                      
REMARK 465     SER A    18                                                      
REMARK 465     ALA A    19                                                      
REMARK 465     GLY A    20                                                      
REMARK 465     LYS A    21                                                      
REMARK 465     GLN A   346                                                      
REMARK 465     LYS A   347                                                      
REMARK 465     GLN B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     THR B     3                                                      
REMARK 465     VAL B     4                                                      
REMARK 465     PRO B     5                                                      
REMARK 465     ALA B     6                                                      
REMARK 465     TRP B     7                                                      
REMARK 465     GLY B     8                                                      
REMARK 465     GLN B     9                                                      
REMARK 465     CYS B    10                                                      
REMARK 465     GLY B    11                                                      
REMARK 465     GLY B    12                                                      
REMARK 465     SER B    13                                                      
REMARK 465     VAL B    14                                                      
REMARK 465     PRO B    15                                                      
REMARK 465     ALA B    16                                                      
REMARK 465     SER B    17                                                      
REMARK 465     SER B    18                                                      
REMARK 465     ALA B    19                                                      
REMARK 465     GLY B    20                                                      
REMARK 465     LYS B    21                                                      
REMARK 465     GLN B   346                                                      
REMARK 465     LYS B   347                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    GLN B    53     N    TYR B    55              2.05            
REMARK 500   O    LEU A    51     O    GLN A    53              2.13            
REMARK 500   O    ALA A   148     O    LYS A   150              2.14            
REMARK 500   O    HOH A   552     O    HOH B   520              2.15            
REMARK 500   OD1  ASP A   224     OG   SER A   226              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH B   520     O    HOH B   520     3555     1.78            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  43       75.95    -27.45                                   
REMARK 500    GLN A  53      167.34     72.90                                   
REMARK 500    TYR A  54        5.82     45.86                                   
REMARK 500    ASN A  73      -35.05   -143.56                                   
REMARK 500    HIS A 120       59.50    -95.11                                   
REMARK 500    ALA A 123       16.31     59.07                                   
REMARK 500    ASN A 126       68.03     34.44                                   
REMARK 500    TYR A 151       -4.95     66.41                                   
REMARK 500    ASP A 167       49.60     34.07                                   
REMARK 500    ASN A 201       55.14     39.87                                   
REMARK 500    THR A 203       38.77     39.39                                   
REMARK 500    ASN A 242       23.11     47.46                                   
REMARK 500    THR A 251      161.84    179.35                                   
REMARK 500    ASN A 253       11.21     59.30                                   
REMARK 500    ALA A 257      -64.54   -134.19                                   
REMARK 500    ALA A 310       87.91    133.71                                   
REMARK 500    ALA A 311     -149.85   -120.04                                   
REMARK 500    CYS A 340      -52.89   -125.71                                   
REMARK 500    ASN A 344       46.08    -74.73                                   
REMARK 500    THR B  52      152.00    -47.95                                   
REMARK 500    GLN B  53      179.05     83.21                                   
REMARK 500    TYR B  54        8.33     35.63                                   
REMARK 500    HIS B 120       61.62   -103.04                                   
REMARK 500    ALA B 123       12.55     53.65                                   
REMARK 500    ASN B 126       54.99     35.36                                   
REMARK 500    HIS B 166      -47.85   -140.58                                   
REMARK 500    ALA B 190       77.14   -101.37                                   
REMARK 500    ASP B 224        5.20    -69.20                                   
REMARK 500    ASN B 253      -11.74     73.65                                   
REMARK 500    ALA B 257      -61.95   -130.70                                   
REMARK 500    ASN B 281       56.68    -99.28                                   
REMARK 500    SER B 300       -7.99    -59.12                                   
REMARK 500    ALA B 310       91.00    137.66                                   
REMARK 500    ALA B 311     -152.17   -121.33                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 PHE A   72     ASN A   73                 -147.74                    
REMARK 500 TRP A  309     ALA A  310                  130.47                    
REMARK 500 TRP B  309     ALA B  310                  131.27                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 553        DISTANCE =  6.07 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5D8W   RELATED DB: PDB                                   
DBREF  5D8Z A    1   347  PDB    5D8Z     5D8Z             1    347             
DBREF  5D8Z B    1   347  PDB    5D8Z     5D8Z             1    347             
SEQRES   1 A  347  GLN SER THR VAL PRO ALA TRP GLY GLN CYS GLY GLY SER          
SEQRES   2 A  347  VAL PRO ALA SER SER ALA GLY LYS LEU GLN PHE ALA GLY          
SEQRES   3 A  347  VAL ASN ILE ALA GLY PHE ASP PHE GLY CYS GLY SER ASP          
SEQRES   4 A  347  GLY THR CYS ASN ALA SER GLY ALA TRP PRO PRO LEU THR          
SEQRES   5 A  347  GLN TYR TYR GLY ALA ASP GLY ALA GLY GLN MET LYS HIS          
SEQRES   6 A  347  PHE VAL ASP ASP ASP GLY PHE ASN VAL PHE ARG LEU PRO          
SEQRES   7 A  347  VAL GLY TRP GLN PHE ILE THR ASP GLY VAL ALA GLY GLY          
SEQRES   8 A  347  ASP ILE ASP GLU ASP ASN TRP ALA GLU TYR ASP ALA LEU          
SEQRES   9 A  347  VAL GLN ALA CYS LEU ASP ALA GLY ALA SER CYS ILE VAL          
SEQRES  10 A  347  ASP VAL HIS ASN TYR ALA ARG PHE ASN GLY GLU ILE ILE          
SEQRES  11 A  347  GLY GLN GLY GLY PRO THR ASN GLN ASP PHE ALA ALA LEU          
SEQRES  12 A  347  TRP SER SER ILE ALA ALA LYS TYR ALA ASP ASN ASP LYS          
SEQRES  13 A  347  ILE ILE PHE GLY VAL MET ASN GLU PRO HIS ASP VAL PRO          
SEQRES  14 A  347  ASP ILE ASN LEU TRP ALA ASP SER VAL GLN ALA ALA VAL          
SEQRES  15 A  347  THR ALA ILE ARG GLN ALA GLY ALA THR SER GLN ILE ILE          
SEQRES  16 A  347  LEU LEU PRO GLY ASN ASN TRP THR SER ALA GLU THR PHE          
SEQRES  17 A  347  VAL SER ASN GLY SER ALA ASP ALA LEU LYS LYS VAL THR          
SEQRES  18 A  347  ASN PRO ASP GLY SER VAL THR ASN LEU ILE PHE ASP VAL          
SEQRES  19 A  347  HIS LYS TYR LEU ASP SER ASP ASN SER GLY THR HIS GLU          
SEQRES  20 A  347  GLU CYS THR THR ASN ASN ILE ASP ASN ALA TRP ALA PRO          
SEQRES  21 A  347  LEU ALA GLU TRP LEU ARG CYS ASN GLY ARG GLN ALA PHE          
SEQRES  22 A  347  ASN THR GLU THR GLY GLY GLY ASN VAL ALA SER CYS GLU          
SEQRES  23 A  347  THR PHE MET CYS GLN GLN VAL ALA TYR GLN ASN ALA ASN          
SEQRES  24 A  347  SER ASP VAL PHE LEU GLY TYR VAL GLY TRP ALA ALA GLY          
SEQRES  25 A  347  ASN PHE TYR GLN GLY TYR VAL LEU GLY GLU VAL PRO THR          
SEQRES  26 A  347  ASP THR ASN GLY VAL TRP THR ASP THR ALA LEU VAL SER          
SEQRES  27 A  347  ALA CYS LEU ALA PRO ASN ALA GLN LYS                          
SEQRES   1 B  347  GLN SER THR VAL PRO ALA TRP GLY GLN CYS GLY GLY SER          
SEQRES   2 B  347  VAL PRO ALA SER SER ALA GLY LYS LEU GLN PHE ALA GLY          
SEQRES   3 B  347  VAL ASN ILE ALA GLY PHE ASP PHE GLY CYS GLY SER ASP          
SEQRES   4 B  347  GLY THR CYS ASN ALA SER GLY ALA TRP PRO PRO LEU THR          
SEQRES   5 B  347  GLN TYR TYR GLY ALA ASP GLY ALA GLY GLN MET LYS HIS          
SEQRES   6 B  347  PHE VAL ASP ASP ASP GLY PHE ASN VAL PHE ARG LEU PRO          
SEQRES   7 B  347  VAL GLY TRP GLN PHE ILE THR ASP GLY VAL ALA GLY GLY          
SEQRES   8 B  347  ASP ILE ASP GLU ASP ASN TRP ALA GLU TYR ASP ALA LEU          
SEQRES   9 B  347  VAL GLN ALA CYS LEU ASP ALA GLY ALA SER CYS ILE VAL          
SEQRES  10 B  347  ASP VAL HIS ASN TYR ALA ARG PHE ASN GLY GLU ILE ILE          
SEQRES  11 B  347  GLY GLN GLY GLY PRO THR ASN GLN ASP PHE ALA ALA LEU          
SEQRES  12 B  347  TRP SER SER ILE ALA ALA LYS TYR ALA ASP ASN ASP LYS          
SEQRES  13 B  347  ILE ILE PHE GLY VAL MET ASN GLU PRO HIS ASP VAL PRO          
SEQRES  14 B  347  ASP ILE ASN LEU TRP ALA ASP SER VAL GLN ALA ALA VAL          
SEQRES  15 B  347  THR ALA ILE ARG GLN ALA GLY ALA THR SER GLN ILE ILE          
SEQRES  16 B  347  LEU LEU PRO GLY ASN ASN TRP THR SER ALA GLU THR PHE          
SEQRES  17 B  347  VAL SER ASN GLY SER ALA ASP ALA LEU LYS LYS VAL THR          
SEQRES  18 B  347  ASN PRO ASP GLY SER VAL THR ASN LEU ILE PHE ASP VAL          
SEQRES  19 B  347  HIS LYS TYR LEU ASP SER ASP ASN SER GLY THR HIS GLU          
SEQRES  20 B  347  GLU CYS THR THR ASN ASN ILE ASP ASN ALA TRP ALA PRO          
SEQRES  21 B  347  LEU ALA GLU TRP LEU ARG CYS ASN GLY ARG GLN ALA PHE          
SEQRES  22 B  347  ASN THR GLU THR GLY GLY GLY ASN VAL ALA SER CYS GLU          
SEQRES  23 B  347  THR PHE MET CYS GLN GLN VAL ALA TYR GLN ASN ALA ASN          
SEQRES  24 B  347  SER ASP VAL PHE LEU GLY TYR VAL GLY TRP ALA ALA GLY          
SEQRES  25 B  347  ASN PHE TYR GLN GLY TYR VAL LEU GLY GLU VAL PRO THR          
SEQRES  26 B  347  ASP THR ASN GLY VAL TRP THR ASP THR ALA LEU VAL SER          
SEQRES  27 B  347  ALA CYS LEU ALA PRO ASN ALA GLN LYS                          
HET    BGC  C   1      12                                                       
HET    BGC  C   2      11                                                       
HET    BGC  D   1      12                                                       
HET    BGC  D   2      11                                                       
HETNAM     BGC BETA-D-GLUCOPYRANOSE                                             
FORMUL   3  BGC    4(C6 H12 O6)                                                 
FORMUL   5  HOH   *73(H2 O)                                                     
HELIX    1 AA1 ASP A   58  ASP A   69  1                                  12    
HELIX    2 AA2 GLY A   80  ASP A   86  1                                   7    
HELIX    3 AA3 ASP A   94  ALA A  111  1                                  18    
HELIX    4 AA4 THR A  136  LYS A  150  1                                  15    
HELIX    5 AA5 ASP A  170  ALA A  188  1                                  19    
HELIX    6 AA6 GLY A  199  SER A  204  1                                   6    
HELIX    7 AA7 GLY A  212  LYS A  219  1                                   8    
HELIX    8 AA8 ALA A  257  ASN A  268  1                                  12    
HELIX    9 AA9 VAL A  282  ASN A  299  1                                  18    
HELIX   10 AB1 THR A  334  CYS A  340  1                                   7    
HELIX   11 AB2 ALA B   44  ALA B   47  5                                   4    
HELIX   12 AB3 ASP B   58  ASP B   69  1                                  12    
HELIX   13 AB4 GLY B   80  ASP B   86  1                                   7    
HELIX   14 AB5 ASP B   94  ALA B  111  1                                  18    
HELIX   15 AB6 THR B  136  ALA B  152  1                                  17    
HELIX   16 AB7 ASP B  170  ALA B  188  1                                  19    
HELIX   17 AB8 GLY B  199  SER B  204  1                                   6    
HELIX   18 AB9 GLY B  212  LYS B  218  1                                   7    
HELIX   19 AC1 ALA B  257  ASN B  268  1                                  12    
HELIX   20 AC2 VAL B  282  ALA B  298  1                                  17    
HELIX   21 AC3 THR B  334  CYS B  340  1                                   7    
SHEET    1 AA1 9 PHE A  24  ALA A  30  0                                        
SHEET    2 AA1 9 VAL A  74  VAL A  79  1  O  ARG A  76   N  ILE A  29           
SHEET    3 AA1 9 SER A 114  VAL A 119  1  O  ILE A 116   N  PHE A  75           
SHEET    4 AA1 9 ILE A 157  GLY A 160  1  O  ILE A 158   N  VAL A 117           
SHEET    5 AA1 9 ILE A 194  PRO A 198  1  O  LEU A 196   N  PHE A 159           
SHEET    6 AA1 9 LEU A 230  HIS A 235  1  O  ASP A 233   N  LEU A 197           
SHEET    7 AA1 9 ALA A 272  THR A 277  1  O  PHE A 273   N  VAL A 234           
SHEET    8 AA1 9 PHE A 303  GLY A 312  1  O  TRP A 309   N  THR A 277           
SHEET    9 AA1 9 PHE A  24  ALA A  30  1  N  ASN A  28   O  GLY A 308           
SHEET    1 AA2 2 ARG A 124  PHE A 125  0                                        
SHEET    2 AA2 2 GLU A 128  ILE A 129 -1  O  GLU A 128   N  PHE A 125           
SHEET    1 AA3 2 THR A 325  THR A 327  0                                        
SHEET    2 AA3 2 VAL A 330  THR A 332 -1  O  VAL A 330   N  THR A 327           
SHEET    1 AA4 9 PHE B  24  ALA B  30  0                                        
SHEET    2 AA4 9 VAL B  74  VAL B  79  1  O  ARG B  76   N  ILE B  29           
SHEET    3 AA4 9 SER B 114  VAL B 119  1  O  ILE B 116   N  LEU B  77           
SHEET    4 AA4 9 ILE B 157  GLY B 160  1  O  ILE B 158   N  VAL B 117           
SHEET    5 AA4 9 ILE B 195  PRO B 198  1  O  LEU B 196   N  PHE B 159           
SHEET    6 AA4 9 LEU B 230  HIS B 235  1  O  ILE B 231   N  LEU B 197           
SHEET    7 AA4 9 ALA B 272  THR B 277  1  O  PHE B 273   N  PHE B 232           
SHEET    8 AA4 9 PHE B 303  GLY B 312  1  O  LEU B 304   N  ALA B 272           
SHEET    9 AA4 9 PHE B  24  ALA B  30  1  N  PHE B  24   O  LEU B 304           
SHEET    1 AA5 2 CYS B  36  GLY B  37  0                                        
SHEET    2 AA5 2 THR B  41  CYS B  42 -1  O  THR B  41   N  GLY B  37           
SHEET    1 AA6 2 ARG B 124  PHE B 125  0                                        
SHEET    2 AA6 2 GLU B 128  ILE B 129 -1  O  GLU B 128   N  PHE B 125           
SHEET    1 AA7 2 THR B 325  THR B 327  0                                        
SHEET    2 AA7 2 VAL B 330  THR B 332 -1  O  THR B 332   N  THR B 325           
SSBOND   1 CYS A   36    CYS A   42                          1555   1555  2.09  
SSBOND   2 CYS A  108    CYS A  115                          1555   1555  2.05  
SSBOND   3 CYS A  249    CYS A  285                          1555   1555  2.02  
SSBOND   4 CYS A  290    CYS A  340                          1555   1555  2.10  
SSBOND   5 CYS B   36    CYS B   42                          1555   1555  2.07  
SSBOND   6 CYS B  108    CYS B  115                          1555   1555  2.05  
SSBOND   7 CYS B  249    CYS B  285                          1555   1555  2.06  
SSBOND   8 CYS B  290    CYS B  340                          1555   1555  2.03  
LINK         O4  BGC C   1                 C1  BGC C   2     1555   1555  1.44  
LINK         O4  BGC D   1                 C1  BGC D   2     1555   1555  1.43  
CRYST1   84.426  236.399   83.585  90.00  90.00  90.00 C 2 2 21     16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011845  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004230  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011964        0.00000                                                                            
ATOM 4867  C2  BGC C   1      -1.822 -25.579  -8.511  1.00 90.25           C  
ATOM 4868  C3  BGC C   1      -2.743 -24.492  -7.921  1.00 90.59           C  
ATOM 4869  C4  BGC C   1      -1.990 -23.563  -6.942  1.00 89.85           C  
ATOM 4870  C5  BGC C   1      -0.522 -23.265  -7.372  1.00 90.03           C  
ATOM 4871  C6  BGC C   1       0.358 -22.869  -6.189  1.00 84.96           C  
ATOM 4872  C1  BGC C   1      -0.556 -24.944  -9.094  1.00 93.77           C  
ATOM 4873  O1  BGC C   1       0.262 -25.922  -9.750  1.00 90.66           O  
ATOM 4874  O2  BGC C   1      -2.513 -26.328  -9.517  1.00 79.74           O  
ATOM 4875  O3  BGC C   1      -3.885 -25.104  -7.276  1.00 87.32           O  
ATOM 4876  O4  BGC C   1      -2.690 -22.303  -6.818  1.00 85.62           O  
ATOM 4877  O5  BGC C   1       0.177 -24.342  -8.025  1.00 89.53           O  
ATOM 4878  O6  BGC C   1       1.719 -22.902  -6.625  1.00 78.67           O  
ATOM 4879  C2  BGC C   2      -4.012 -20.639  -5.590  1.00 80.07           C  
ATOM 4880  C3  BGC C   2      -5.380 -20.312  -4.951  1.00 82.25           C  
ATOM 4881  C4  BGC C   2      -6.522 -21.110  -5.555  1.00 76.48           C  
ATOM 4882  C5  BGC C   2      -6.151 -22.604  -5.655  1.00 74.28           C  
ATOM 4883  C6  BGC C   2      -7.169 -23.375  -6.492  1.00 72.61           C  
ATOM 4884  C1  BGC C   2      -3.729 -22.146  -5.828  1.00 84.47           C  
ATOM 4885  O2  BGC C   2      -2.996 -20.099  -4.738  1.00 64.47           O  
ATOM 4886  O3  BGC C   2      -5.759 -18.930  -5.118  1.00 88.65           O  
ATOM 4887  O4  BGC C   2      -7.703 -20.795  -4.778  1.00 68.78           O  
ATOM 4888  O5  BGC C   2      -4.889 -22.841  -6.302  1.00 82.82           O  
ATOM 4889  O6  BGC C   2      -6.585 -23.914  -7.683  1.00 64.45           O  
TER



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.