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LongText Report for: 3GUU-pdb

Name Class
3GUU-pdb
HEADER    HYDROLASE                               30-MAR-09   3GUU              
TITLE     X-RAY STRUCTURE OF CANDIDA ANTARCTICA LIPASE A                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LIPASE A;                                                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 3.1.1.3                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CANDIDA ANTARCTICA;                             
SOURCE   3 ORGANISM_TAXID: 34362;                                               
SOURCE   4 OTHER_DETAILS: COMMERIAL ENZYME ROCHE CHIRAZYME L-5                  
KEYWDS    CANDIDA, LIPASE, PROTEIN STRUCTURE, HYDROLASE                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.-M.BRANDT,X.-G.LI,Y.NYMALM-REJSTROM,T.AIRENNE,L.T.KANERVA,          
AUTHOR   2 T.A.SALMINEN                                                         
REVDAT   1   31-MAR-10 3GUU    0                                                
JRNL        AUTH   A.-M.BRANDT,X.-G.LI,Y.NYMALM-REJSTROM,T.AIRENNE,             
JRNL        AUTH 2 L.T.KANERVA,T.A.SALMINEN                                     
JRNL        TITL   THE CRYSTAL STRUCTURE OF LIPASE A FROM CANDIDA               
JRNL        TITL 2 ANTARCTICA                                                   
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.3.0040                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.92                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 71879                          
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) : 0.191                           
REMARK   3   R VALUE            (WORKING SET) : 0.189                           
REMARK   3   FREE R VALUE                     : 0.234                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3784                            
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) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5208                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2040                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 275                          
REMARK   3   BIN FREE R VALUE                    : 0.2300                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6535                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 43                                      
REMARK   3   SOLVENT ATOMS            : 499                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 20.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.29                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.47000                                              
REMARK   3    B22 (A**2) : 0.47000                                              
REMARK   3    B33 (A**2) : -0.94000                                             
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): 0.166         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.158         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.114         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.309         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.929                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.892                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6789 ; 0.020 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):     8 ; 0.120 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9286 ; 1.713 ; 1.963       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    16 ; 3.689 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   868 ; 6.131 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   277 ;32.190 ;25.018       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   978 ;15.092 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;19.455 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1035 ; 0.125 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5250 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3377 ; 0.220 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    17 ; 0.375 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4686 ; 0.310 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):     5 ; 0.124 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   541 ; 0.178 ; 0.200       
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):    50 ; 0.178 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    10 ; 0.134 ; 0.200       
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):  4444 ; 0.869 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7018 ; 1.339 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2689 ; 2.366 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2268 ; 3.487 ; 4.500       
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 : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     12       A     441      5                      
REMARK   3           1     B     12       B     441      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1711 ;  0.15 ;  0.50           
REMARK   3   LOOSE POSITIONAL   1    A    (A):   1524 ;  0.33 ;  5.00           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   1711 ;  0.84 ;  2.00           
REMARK   3   LOOSE THERMAL      1    A (A**2):   1524 ;  1.16 ; 10.00           
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          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 3GUU COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-APR-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB052334.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-DEC-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.93300                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : INTEGRATE                          
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 86764                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.2                               
REMARK 200  DATA REDUNDANCY                : 6.500                              
REMARK 200  R MERGE                    (I) : 0.17400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 9.6400                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.30                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.43300                            
REMARK 200  R SYM FOR SHELL            (I) : 0.43400                            
REMARK 200   FOR SHELL         : 4.420                              
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: PDB ENTRY 2VEO                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.89                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.23                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5M AMMONIUM SULFATE, 12%               
REMARK 280  GLYCEROL, 100MM TRIS-HCL PH 8.5 , VAPOR DIFFUSION, HANGING          
REMARK 280  DROP, TEMPERATURE 294.0K                                            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
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   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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      150.20000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       46.05000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       46.05000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      225.30000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       46.05000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       46.05000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       75.10000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       46.05000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       46.05000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      225.30000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       46.05000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       46.05000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       75.10000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      150.20000            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
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     MET A   -20                                                      
REMARK 465     ARG A   -19                                                      
REMARK 465     VAL A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     LEU A   -16                                                      
REMARK 465     ARG A   -15                                                      
REMARK 465     SER A   -14                                                      
REMARK 465     ILE A   -13                                                      
REMARK 465     THR A   -12                                                      
REMARK 465     SER A   -11                                                      
REMARK 465     LEU A   -10                                                      
REMARK 465     LEU A    -9                                                      
REMARK 465     ALA A    -8                                                      
REMARK 465     ALA A    -7                                                      
REMARK 465     ALA A    -6                                                      
REMARK 465     THR A    -5                                                      
REMARK 465     ALA A    -4                                                      
REMARK 465     ALA A    -3                                                      
REMARK 465     VAL A    -2                                                      
REMARK 465     LEU A    -1                                                      
REMARK 465     ALA A     0                                                      
REMARK 465     ALA A     1                                                      
REMARK 465     PRO A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     GLU A     5                                                      
REMARK 465     THR A     6                                                      
REMARK 465     LEU A     7                                                      
REMARK 465     ASP A     8                                                      
REMARK 465     ARG A     9                                                      
REMARK 465     ARG A    10                                                      
REMARK 465     MET B   -20                                                      
REMARK 465     ARG B   -19                                                      
REMARK 465     VAL B   -18                                                      
REMARK 465     SER B   -17                                                      
REMARK 465     LEU B   -16                                                      
REMARK 465     ARG B   -15                                                      
REMARK 465     SER B   -14                                                      
REMARK 465     ILE B   -13                                                      
REMARK 465     THR B   -12                                                      
REMARK 465     SER B   -11                                                      
REMARK 465     LEU B   -10                                                      
REMARK 465     LEU B    -9                                                      
REMARK 465     ALA B    -8                                                      
REMARK 465     ALA B    -7                                                      
REMARK 465     ALA B    -6                                                      
REMARK 465     THR B    -5                                                      
REMARK 465     ALA B    -4                                                      
REMARK 465     ALA B    -3                                                      
REMARK 465     VAL B    -2                                                      
REMARK 465     LEU B    -1                                                      
REMARK 465     ALA B     0                                                      
REMARK 465     ALA B     1                                                      
REMARK 465     PRO B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     ALA B     4                                                      
REMARK 465     GLU B     5                                                      
REMARK 465     THR B     6                                                      
REMARK 465     LEU B     7                                                      
REMARK 465     ASP B     8                                                      
REMARK 465     ARG B     9                                                      
REMARK 465     ARG B    10                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     PRO A 441    O                                                   
REMARK 470     PRO B 441    O                                                   
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    HOH B   588     O    HOH B   676              1.60            
REMARK 500   O    HOH A   608     O    HOH A   665              1.75            
REMARK 500   O    HOH A   625     O    HOH A   650              1.96            
REMARK 500   CG1  ILE B   127     O    HOH B   631              2.05            
REMARK 500   O    HOH B   607     O    HOH B   667              2.08            
REMARK 500   OE1  GLU A   365     O    HOH A   453              2.13            
REMARK 500   O    HOH A   668     O    HOH B   621              2.15            
REMARK 500   OE1  GLN B    65     O    HOH B   673              2.15            
REMARK 500   ND1  HIS A   245     O3   GOL A   443              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A  95   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP A 247   O   -  C   -  N   ANGL. DEV. = -10.3 DEGREES          
REMARK 500    ARG A 326   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES          
REMARK 500    ARG A 326   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.9 DEGREES          
REMARK 500    LEU A 367   CA  -  CB  -  CG  ANGL. DEV. = -22.6 DEGREES          
REMARK 500    ARG B  60   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES          
REMARK 500    ARG B  60   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.7 DEGREES          
REMARK 500    LEU B 367   CA  -  CB  -  CG  ANGL. DEV. = -22.2 DEGREES          
REMARK 500    LEU B 367   CB  -  CG  -  CD1 ANGL. DEV. =  10.8 DEGREES          
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    TYR A  22       45.70    -95.86                                   
REMARK 500    VAL A 120     -165.21   -115.54                                   
REMARK 500    LEU A 121     -123.10     68.17                                   
REMARK 500    ILE A 150        4.41     85.32                                   
REMARK 500    SER A 184     -127.42     64.77                                   
REMARK 500    ALA A 201       59.97   -140.79                                   
REMARK 500    CYS A 273     -167.84   -110.33                                   
REMARK 500    GLU A 308       49.56    -91.32                                   
REMARK 500    ILE A 404      -63.62   -108.05                                   
REMARK 500    TYR B  22       54.63    -96.82                                   
REMARK 500    THR B  61     -157.65   -131.20                                   
REMARK 500    VAL B 120     -159.36   -107.23                                   
REMARK 500    LEU B 121     -126.99     69.79                                   
REMARK 500    ILE B 150       -0.32     80.73                                   
REMARK 500    SER B 184     -122.58     61.21                                   
REMARK 500    CYS B 273     -161.53   -124.27                                   
REMARK 500    GLU B 308       54.63    -95.42                                   
REMARK 500    ILE B 404      -66.25   -124.19                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ASP B 122        24.1      L          L   OUTSIDE RANGE           
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 619        DISTANCE =  5.20 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 442                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 443                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE B 442                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 443                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THERE IS NO UNP REFERENCE SEQUENCE DATABASE FOR THIS PROTEIN         
REMARK 999 AT THE TIME OF PROCESSING.                                           
REMARK 999 THIS SEQUENCE IS REFERRED IN CAN.J.BOT. VOL 73 (1995), PP.           
REMARK 999 S869-S875; HOEGH, S. ET.                                             
DBREF  3GUU A  -20   441  PDB    3GUU     3GUU             1    462             
DBREF  3GUU B  -20   441  PDB    3GUU     3GUU             1    462             
SEQRES   1 A  462  MET ARG VAL SER LEU ARG SER ILE THR SER LEU LEU ALA          
SEQRES   2 A  462  ALA ALA THR ALA ALA VAL LEU ALA ALA PRO ALA ALA GLU          
SEQRES   3 A  462  THR LEU ASP ARG ARG ALA ALA LEU PRO ASN PRO TYR ASP          
SEQRES   4 A  462  ASP PRO PHE TYR THR THR PRO SER ASN ILE GLY THR PHE          
SEQRES   5 A  462  ALA LYS GLY GLN VAL ILE GLN SER ARG LYS VAL PRO THR          
SEQRES   6 A  462  ASP ILE GLY ASN ALA ASN ASN ALA ALA SER PHE GLN LEU          
SEQRES   7 A  462  GLN TYR ARG THR THR ASN THR GLN ASN GLU ALA VAL ALA          
SEQRES   8 A  462  ASP VAL ALA THR VAL TRP ILE PRO ALA LYS PRO ALA SER          
SEQRES   9 A  462  PRO PRO LYS ILE PHE SER TYR GLN VAL TYR GLU ASP ALA          
SEQRES  10 A  462  THR ALA LEU ASP CYS ALA PRO SER TYR SER TYR LEU THR          
SEQRES  11 A  462  GLY LEU ASP GLN PRO ASN LYS VAL THR ALA VAL LEU ASP          
SEQRES  12 A  462  THR PRO ILE ILE ILE GLY TRP ALA LEU GLN GLN GLY TYR          
SEQRES  13 A  462  TYR VAL VAL SER SER ASP HIS GLU GLY PHE LYS ALA ALA          
SEQRES  14 A  462  PHE ILE ALA GLY TYR GLU GLU GLY MET ALA ILE LEU ASP          
SEQRES  15 A  462  GLY ILE ARG ALA LEU LYS ASN TYR GLN ASN LEU PRO SER          
SEQRES  16 A  462  ASP SER LYS VAL ALA LEU GLU GLY TYR SER GLY GLY ALA          
SEQRES  17 A  462  HIS ALA THR VAL TRP ALA THR SER LEU ALA GLU SER TYR          
SEQRES  18 A  462  ALA PRO GLU LEU ASN ILE VAL GLY ALA SER HIS GLY GLY          
SEQRES  19 A  462  THR PRO VAL SER ALA LYS ASP THR PHE THR PHE LEU ASN          
SEQRES  20 A  462  GLY GLY PRO PHE ALA GLY PHE ALA LEU ALA GLY VAL SER          
SEQRES  21 A  462  GLY LEU SER LEU ALA HIS PRO ASP MET GLU SER PHE ILE          
SEQRES  22 A  462  GLU ALA ARG LEU ASN ALA LYS GLY GLN ARG THR LEU LYS          
SEQRES  23 A  462  GLN ILE ARG GLY ARG GLY PHE CYS LEU PRO GLN VAL VAL          
SEQRES  24 A  462  LEU THR TYR PRO PHE LEU ASN VAL PHE SER LEU VAL ASN          
SEQRES  25 A  462  ASP THR ASN LEU LEU ASN GLU ALA PRO ILE ALA SER ILE          
SEQRES  26 A  462  LEU LYS GLN GLU THR VAL VAL GLN ALA GLU ALA SER TYR          
SEQRES  27 A  462  THR VAL SER VAL PRO LYS PHE PRO ARG PHE ILE TRP HIS          
SEQRES  28 A  462  ALA ILE PRO ASP GLU ILE VAL PRO TYR GLN PRO ALA ALA          
SEQRES  29 A  462  THR TYR VAL LYS GLU GLN CYS ALA LYS GLY ALA ASN ILE          
SEQRES  30 A  462  ASN PHE SER PRO TYR PRO ILE ALA GLU HIS LEU THR ALA          
SEQRES  31 A  462  GLU ILE PHE GLY LEU VAL PRO SER LEU TRP PHE ILE LYS          
SEQRES  32 A  462  GLN ALA PHE ASP GLY THR THR PRO LYS VAL ILE CYS GLY          
SEQRES  33 A  462  THR PRO ILE PRO ALA ILE ALA GLY ILE THR THR PRO SER          
SEQRES  34 A  462  ALA ASP GLN VAL LEU GLY SER ASP LEU ALA ASN GLN LEU          
SEQRES  35 A  462  ARG SER LEU ASP GLY LYS GLN SER ALA PHE GLY LYS PRO          
SEQRES  36 A  462  PHE GLY PRO ILE THR PRO PRO                                  
SEQRES   1 B  462  MET ARG VAL SER LEU ARG SER ILE THR SER LEU LEU ALA          
SEQRES   2 B  462  ALA ALA THR ALA ALA VAL LEU ALA ALA PRO ALA ALA GLU          
SEQRES   3 B  462  THR LEU ASP ARG ARG ALA ALA LEU PRO ASN PRO TYR ASP          
SEQRES   4 B  462  ASP PRO PHE TYR THR THR PRO SER ASN ILE GLY THR PHE          
SEQRES   5 B  462  ALA LYS GLY GLN VAL ILE GLN SER ARG LYS VAL PRO THR          
SEQRES   6 B  462  ASP ILE GLY ASN ALA ASN ASN ALA ALA SER PHE GLN LEU          
SEQRES   7 B  462  GLN TYR ARG THR THR ASN THR GLN ASN GLU ALA VAL ALA          
SEQRES   8 B  462  ASP VAL ALA THR VAL TRP ILE PRO ALA LYS PRO ALA SER          
SEQRES   9 B  462  PRO PRO LYS ILE PHE SER TYR GLN VAL TYR GLU ASP ALA          
SEQRES  10 B  462  THR ALA LEU ASP CYS ALA PRO SER TYR SER TYR LEU THR          
SEQRES  11 B  462  GLY LEU ASP GLN PRO ASN LYS VAL THR ALA VAL LEU ASP          
SEQRES  12 B  462  THR PRO ILE ILE ILE GLY TRP ALA LEU GLN GLN GLY TYR          
SEQRES  13 B  462  TYR VAL VAL SER SER ASP HIS GLU GLY PHE LYS ALA ALA          
SEQRES  14 B  462  PHE ILE ALA GLY TYR GLU GLU GLY MET ALA ILE LEU ASP          
SEQRES  15 B  462  GLY ILE ARG ALA LEU LYS ASN TYR GLN ASN LEU PRO SER          
SEQRES  16 B  462  ASP SER LYS VAL ALA LEU GLU GLY TYR SER GLY GLY ALA          
SEQRES  17 B  462  HIS ALA THR VAL TRP ALA THR SER LEU ALA GLU SER TYR          
SEQRES  18 B  462  ALA PRO GLU LEU ASN ILE VAL GLY ALA SER HIS GLY GLY          
SEQRES  19 B  462  THR PRO VAL SER ALA LYS ASP THR PHE THR PHE LEU ASN          
SEQRES  20 B  462  GLY GLY PRO PHE ALA GLY PHE ALA LEU ALA GLY VAL SER          
SEQRES  21 B  462  GLY LEU SER LEU ALA HIS PRO ASP MET GLU SER PHE ILE          
SEQRES  22 B  462  GLU ALA ARG LEU ASN ALA LYS GLY GLN ARG THR LEU LYS          
SEQRES  23 B  462  GLN ILE ARG GLY ARG GLY PHE CYS LEU PRO GLN VAL VAL          
SEQRES  24 B  462  LEU THR TYR PRO PHE LEU ASN VAL PHE SER LEU VAL ASN          
SEQRES  25 B  462  ASP THR ASN LEU LEU ASN GLU ALA PRO ILE ALA SER ILE          
SEQRES  26 B  462  LEU LYS GLN GLU THR VAL VAL GLN ALA GLU ALA SER TYR          
SEQRES  27 B  462  THR VAL SER VAL PRO LYS PHE PRO ARG PHE ILE TRP HIS          
SEQRES  28 B  462  ALA ILE PRO ASP GLU ILE VAL PRO TYR GLN PRO ALA ALA          
SEQRES  29 B  462  THR TYR VAL LYS GLU GLN CYS ALA LYS GLY ALA ASN ILE          
SEQRES  30 B  462  ASN PHE SER PRO TYR PRO ILE ALA GLU HIS LEU THR ALA          
SEQRES  31 B  462  GLU ILE PHE GLY LEU VAL PRO SER LEU TRP PHE ILE LYS          
SEQRES  32 B  462  GLN ALA PHE ASP GLY THR THR PRO LYS VAL ILE CYS GLY          
SEQRES  33 B  462  THR PRO ILE PRO ALA ILE ALA GLY ILE THR THR PRO SER          
SEQRES  34 B  462  ALA ASP GLN VAL LEU GLY SER ASP LEU ALA ASN GLN LEU          
SEQRES  35 B  462  ARG SER LEU ASP GLY LYS GLN SER ALA PHE GLY LYS PRO          
SEQRES  36 B  462  PHE GLY PRO ILE THR PRO PRO                                  
HET    1PE  A 442      16                                                       
HET    GOL  A 443       6                                                       
HET    1PE  B 442      16                                                       
HET    SO4  B 443       5                                                       
HETNAM     1PE PENTAETHYLENE GLYCOL                                             
HETNAM     GOL GLYCEROL                                                         
HETNAM     SO4 SULFATE ION                                                      
HETSYN     1PE PEG400                                                           
FORMUL   3  1PE    2(C10 H22 O6)                                                
FORMUL   4  GOL    C3 H8 O3                                                     
FORMUL   6  SO4    O4 S 2-                                                      
FORMUL   7  HOH   *499(H2 O)                                                    
HELIX    1   1 ASN A   15  THR A   23  5                                   9    
HELIX    2   2 ASN A   27  PHE A   31  5                                   5    
HELIX    3   3 THR A   44  ASN A   50  1                                   7    
HELIX    4   4 ALA A   98  CYS A  101  5                                   4    
HELIX    5   5 ALA A  102  LEU A  108  1                                   7    
HELIX    6   6 ASN A  115  VAL A  120  5                                   6    
HELIX    7   7 LEU A  121  GLN A  133  1                                  13    
HELIX    8   8 ALA A  151  GLN A  170  1                                  20    
HELIX    9   9 SER A  184  ALA A  201  1                                  18    
HELIX   10  10 SER A  217  ASN A  226  1                                  10    
HELIX   11  11 PHE A  230  HIS A  245  1                                  16    
HELIX   12  12 HIS A  245  ALA A  254  1                                  10    
HELIX   13  13 ASN A  257  ARG A  268  1                                  12    
HELIX   14  14 CYS A  273  TYR A  281  1                                   9    
HELIX   15  15 ASN A  285  VAL A  290  5                                   6    
HELIX   16  16 ASN A  294  GLU A  298  5                                   5    
HELIX   17  17 PRO A  300  GLU A  308  1                                   9    
HELIX   18  18 PRO A  338  LYS A  352  1                                  15    
HELIX   19  19 GLU A  365  GLY A  373  1                                   9    
HELIX   20  20 GLY A  373  GLY A  387  1                                  15    
HELIX   21  21 SER A  408  GLY A  414  1                                   7    
HELIX   22  22 GLY A  414  LEU A  424  1                                  11    
HELIX   23  23 ASN B   15  THR B   23  5                                   9    
HELIX   24  24 ASN B   27  PHE B   31  5                                   5    
HELIX   25  25 THR B   44  ASN B   51  1                                   8    
HELIX   26  26 ALA B   98  CYS B  101  5                                   4    
HELIX   27  27 ALA B  102  LEU B  108  1                                   7    
HELIX   28  28 ASN B  115  VAL B  120  5                                   6    
HELIX   29  29 ASP B  122  GLN B  133  1                                  12    
HELIX   30  30 ALA B  151  GLN B  170  1                                  20    
HELIX   31  31 SER B  184  ALA B  201  1                                  18    
HELIX   32  32 SER B  217  ASN B  226  1                                  10    
HELIX   33  33 PHE B  230  HIS B  245  1                                  16    
HELIX   34  34 HIS B  245  ALA B  254  1                                  10    
HELIX   35  35 ASN B  257  GLY B  269  1                                  13    
HELIX   36  36 CYS B  273  TYR B  281  1                                   9    
HELIX   37  37 ASN B  285  VAL B  290  5                                   6    
HELIX   38  38 ASN B  294  GLU B  298  5                                   5    
HELIX   39  39 PRO B  300  LYS B  306  1                                   7    
HELIX   40  40 PRO B  338  LYS B  352  1                                  15    
HELIX   41  41 GLU B  365  GLY B  373  1                                   9    
HELIX   42  42 GLY B  373  GLY B  387  1                                  15    
HELIX   43  43 SER B  408  GLY B  414  1                                   7    
HELIX   44  44 GLY B  414  SER B  423  1                                  10    
SHEET    1   A 9 VAL A  36  LYS A  41  0                                        
SHEET    2   A 9 ALA A  53  THR A  62 -1  O  GLN A  58   N  GLN A  38           
SHEET    3   A 9 ALA A  68  ILE A  77 -1  O  VAL A  69   N  THR A  61           
SHEET    4   A 9 TYR A 136  SER A 140 -1  O  SER A 139   N  THR A  74           
SHEET    5   A 9 LYS A  86  GLN A  91  1  N  PHE A  88   O  TYR A 136           
SHEET    6   A 9 LYS A 177  TYR A 183  1  O  ALA A 179   N  SER A  89           
SHEET    7   A 9 ASN A 205  GLY A 212  1  O  VAL A 207   N  VAL A 178           
SHEET    8   A 9 PRO A 325  ALA A 331  1  O  PHE A 327   N  ALA A 209           
SHEET    9   A 9 ASN A 355  TYR A 361  1  O  ASN A 357   N  ARG A 326           
SHEET    1   B 9 VAL B  36  LYS B  41  0                                        
SHEET    2   B 9 ALA B  53  THR B  62 -1  O  GLN B  58   N  ILE B  37           
SHEET    3   B 9 ALA B  68  ILE B  77 -1  O  VAL B  69   N  THR B  61           
SHEET    4   B 9 TYR B 136  SER B 140 -1  O  SER B 139   N  THR B  74           
SHEET    5   B 9 LYS B  86  GLN B  91  1  N  PHE B  88   O  TYR B 136           
SHEET    6   B 9 LYS B 177  TYR B 183  1  O  LYS B 177   N  ILE B  87           
SHEET    7   B 9 ASN B 205  GLY B 212  1  O  VAL B 207   N  VAL B 178           
SHEET    8   B 9 PRO B 325  ALA B 331  1  O  PHE B 327   N  HIS B 211           
SHEET    9   B 9 ASN B 355  TYR B 361  1  O  SER B 359   N  ILE B 328           
SSBOND   1 CYS A  101    CYS A  273                          1555   1555  1.96  
SSBOND   2 CYS A  350    CYS A  394                          1555   1555  2.07  
SSBOND   3 CYS B  101    CYS B  273                          1555   1555  2.05  
SSBOND   4 CYS B  350    CYS B  394                          1555   1555  2.10  
CISPEP   1 SER A   83    PRO A   84          0        -2.19                     
CISPEP   2 ALA A  299    PRO A  300          0         4.35                     
CISPEP   3 SER B   83    PRO B   84          0        -1.77                     
CISPEP   4 ALA B  299    PRO B  300          0         1.46                     
SITE     1 AC1 11 ASP A  95  PHE A 149  SER A 184  GLY A 185                    
SITE     2 AC1 11 ALA A 218  THR A 221  PHE A 222  PHE A 233                    
SITE     3 AC1 11 LEU A 241  LEU A 296  PHE A 431                               
SITE     1 AC2  7 GLN A  65  HIS A 245  PRO A 246  ASP A 247                    
SITE     2 AC2  7 MET A 248  PRO A 300  ILE A 304                               
SITE     1 AC3  9 ASP B  95  SER B 184  GLY B 185  ALA B 218                    
SITE     2 AC3  9 THR B 221  PHE B 222  PHE B 233  VAL B 238                    
SITE     3 AC3  9 LEU B 296                                                     
SITE     1 AC4  4 HIS B 245  PRO B 246  ASP B 247  MET B 248                    
CRYST1   92.100   92.100  300.400  90.00  90.00  90.00 P 43 21 2    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      0.010858  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010858  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003329        0.00000                         
TER    3273      PRO A 441                                                      
TER    6537      PRO B 441                                                      
MASTER      479    0    4   44   18    0    9    6 7077    2   51   72          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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