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Database: PDB
Entry: 3PUG
LinkDB: 3PUG
Original site: 3PUG 
HEADER    TRANSFERASE                             04-DEC-10   3PUG              
TITLE     HALOFERAX VOLCANII MALATE SYNTHASE NATIVE AT 3MM GLYOXYLATE           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MALATE SYNTHASE;                                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 2.3.3.9                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HALOFERAX VOLCANII;                             
SOURCE   3 ORGANISM_TAXID: 309800;                                              
SOURCE   4 STRAIN: ATCC 29605, DS2;                                             
SOURCE   5 OTHER_DETAILS: ATCC                                                  
KEYWDS    TIM BARREL, TRANSFERASE                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.R.HOWARD,C.D.BRACKEN,A.M.NEIGHBOR,G.C.THOMAS,K.K.LAMLENN,           
AUTHOR   2 H.L.SCHUBERT,F.G.WHITBY                                              
REVDAT   3   21-FEB-24 3PUG    1       REMARK HETSYN LINK                       
REVDAT   2   08-NOV-17 3PUG    1       REMARK                                   
REVDAT   1   01-JUN-11 3PUG    0                                                
JRNL        AUTH   C.D.BRACKEN,A.M.NEIGHBOR,K.K.LAMLENN,G.C.THOMAS,             
JRNL        AUTH 2 H.L.SCHUBERT,F.G.WHITBY,B.R.HOWARD                           
JRNL        TITL   CRYSTAL STRUCTURES OF A HALOPHILIC ARCHAEAL MALATE SYNTHASE  
JRNL        TITL 2 FROM HALOFERAX VOLCANII AND COMPARISONS WITH ISOFORMS A AND  
JRNL        TITL 3 G.                                                           
JRNL        REF    BMC STRUCT.BIOL.              V.  11    23 2011              
JRNL        REFN                   ESSN 1472-6807                               
JRNL        PMID   21569248                                                     
JRNL        DOI    10.1186/1472-6807-11-23                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
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) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 18194                          
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) : 0.202                           
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.263                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 935                             
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) : 1189                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.32                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2500                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 57                           
REMARK   3   BIN FREE R VALUE                    : 0.2930                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2747                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 14                                      
REMARK   3   SOLVENT ATOMS            : 71                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 58.34                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.36000                                              
REMARK   3    B22 (A**2) : 1.36000                                              
REMARK   3    B33 (A**2) : -2.04000                                             
REMARK   3    B12 (A**2) : 0.68000                                              
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.294         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.192         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.058         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.931                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.868                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2824 ; 0.014 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3831 ; 2.273 ; 1.956       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   349 ; 7.497 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   151 ;35.733 ;24.570       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   462 ;19.552 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    23 ;14.931 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   404 ; 0.135 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2230 ; 0.012 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  1739 ; 1.247 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2800 ; 2.310 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1085 ; 3.563 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1029 ; 5.516 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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 : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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 U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 3PUG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-DEC-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000062825.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-MAR-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : R-AXIS IV, CONFOCAL OPTICS         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18255                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 5.700                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.38300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SIRAS                                          
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS                        
REMARK 200 SOFTWARE USED: SOLVE 2.13, RESOLVE 2.13                              
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.45                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4500, GLYCEROL, 2M KCL,13 MM         
REMARK 280  MGCL2, 3MM GLYOXYLATE, PH 4.4, VAPOR DIFFUSION, SITTING DROP,       
REMARK 280  TEMPERATURE 295K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2                            
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z                                               
REMARK 290       6555   -X,-X+Y,-Z                                              
REMARK 290       7555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       8555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       9555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290      10555   Y+2/3,X+1/3,-Z+1/3                                      
REMARK 290      11555   X-Y+2/3,-Y+1/3,-Z+1/3                                   
REMARK 290      12555   -X+2/3,-X+Y+1/3,-Z+1/3                                  
REMARK 290      13555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290      14555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290      15555   -X+Y+1/3,-X+2/3,Z+2/3                                   
REMARK 290      16555   Y+1/3,X+2/3,-Z+2/3                                      
REMARK 290      17555   X-Y+1/3,-Y+2/3,-Z+2/3                                   
REMARK 290      18555   -X+1/3,-X+Y+2/3,-Z+2/3                                  
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  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        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000       78.18500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       45.14013            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       47.15167            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000       78.18500            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       45.14013            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       47.15167            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000       78.18500            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       45.14013            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       47.15167            
REMARK 290   SMTRY1  10 -0.500000  0.866025  0.000000       78.18500            
REMARK 290   SMTRY2  10  0.866025  0.500000  0.000000       45.14013            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       47.15167            
REMARK 290   SMTRY1  11  1.000000  0.000000  0.000000       78.18500            
REMARK 290   SMTRY2  11  0.000000 -1.000000  0.000000       45.14013            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       47.15167            
REMARK 290   SMTRY1  12 -0.500000 -0.866025  0.000000       78.18500            
REMARK 290   SMTRY2  12 -0.866025  0.500000  0.000000       45.14013            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       47.15167            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       90.28026            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000       94.30333            
REMARK 290   SMTRY1  14 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  14  0.866025 -0.500000  0.000000       90.28026            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000       94.30333            
REMARK 290   SMTRY1  15 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  15 -0.866025 -0.500000  0.000000       90.28026            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000       94.30333            
REMARK 290   SMTRY1  16 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  16  0.866025  0.500000  0.000000       90.28026            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       94.30333            
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  17  0.000000 -1.000000  0.000000       90.28026            
REMARK 290   SMTRY3  17  0.000000  0.000000 -1.000000       94.30333            
REMARK 290   SMTRY1  18 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  18 -0.866025  0.500000  0.000000       90.28026            
REMARK 290   SMTRY3  18  0.000000  0.000000 -1.000000       94.30333            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 16740 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 42110 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -161.0 KCAL/MOL                       
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   BIOMT1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 43070 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 74620 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -360.0 KCAL/MOL                       
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   BIOMT1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000      141.45500            
REMARK 350   BIOMT1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   5  0.000000  0.000000 -1.000000      141.45500            
REMARK 350   BIOMT1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   6  0.000000  0.000000 -1.000000      141.45500            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 CL    CL A 704  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 472  LIES ON A SPECIAL POSITION.                          
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     1                                                      
REMARK 465     GLY A    23                                                      
REMARK 465     GLU A    24                                                      
REMARK 465     ALA A   283                                                      
REMARK 465     ASP A   284                                                      
REMARK 465     GLY A   285                                                      
REMARK 465     GLU A   286                                                      
REMARK 465     GLU A   287                                                      
REMARK 465     VAL A   288                                                      
REMARK 465     GLU A   289                                                      
REMARK 465     LEU A   290                                                      
REMARK 465     ALA A   291                                                      
REMARK 465     SER A   292                                                      
REMARK 465     GLU A   293                                                      
REMARK 465     ASP A   294                                                      
REMARK 465     GLY A   295                                                      
REMARK 465     VAL A   296                                                      
REMARK 465     GLU A   297                                                      
REMARK 465     ALA A   298                                                      
REMARK 465     TYR A   299                                                      
REMARK 465     ASP A   300                                                      
REMARK 465     GLY A   301                                                      
REMARK 465     ASP A   302                                                      
REMARK 465     ARG A   303                                                      
REMARK 465     LEU A   304                                                      
REMARK 465     SER A   305                                                      
REMARK 465     LEU A   306                                                      
REMARK 465     GLU A   307                                                      
REMARK 465     ALA A   308                                                      
REMARK 465     THR A   309                                                      
REMARK 465     ASP A   310                                                      
REMARK 465     GLY A   311                                                      
REMARK 465     GLY A   312                                                      
REMARK 465     TYR A   313                                                      
REMARK 465     GLU A   314                                                      
REMARK 465     LEU A   315                                                      
REMARK 465     ARG A   316                                                      
REMARK 465     VAL A   317                                                      
REMARK 465     GLY A   318                                                      
REMARK 465     GLY A   319                                                      
REMARK 465     ASP A   320                                                      
REMARK 465     ALA A   321                                                      
REMARK 465     ARG A   322                                                      
REMARK 465     GLU A   323                                                      
REMARK 465     LEU A   324                                                      
REMARK 465     THR A   325                                                      
REMARK 465     ALA A   326                                                      
REMARK 465     ASP A   327                                                      
REMARK 465     GLU A   328                                                      
REMARK 465     LEU A   329                                                      
REMARK 465     ARG A   330                                                      
REMARK 465     ALA A   355                                                      
REMARK 465     ALA A   356                                                      
REMARK 465     LYS A   357                                                      
REMARK 465     GLU A   358                                                      
REMARK 465     ALA A   359                                                      
REMARK 465     GLY A   360                                                      
REMARK 465     ARG A   361                                                      
REMARK 465     GLY A   362                                                      
REMARK 465     ALA A   363                                                      
REMARK 465     ILE A   364                                                      
REMARK 465     ALA A   365                                                      
REMARK 465     MET A   366                                                      
REMARK 465     THR A   367                                                      
REMARK 465     GLN A   368                                                      
REMARK 465     SER A   369                                                      
REMARK 465     ALA A   370                                                      
REMARK 465     THR A   371                                                      
REMARK 465     LEU A   372                                                      
REMARK 465     ARG A   373                                                      
REMARK 465     ILE A   374                                                      
REMARK 465     GLY A   375                                                      
REMARK 465     GLY A   376                                                      
REMARK 465     THR A   377                                                      
REMARK 465     GLU A   378                                                      
REMARK 465     ILE A   379                                                      
REMARK 465     ASP A   380                                                      
REMARK 465     ILE A   381                                                      
REMARK 465     GLU A   382                                                      
REMARK 465     LYS A   383                                                      
REMARK 465     ASP A   384                                                      
REMARK 465     ARG A   385                                                      
REMARK 465     MET A   386                                                      
REMARK 465     LEU A   433                                                      
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    ARG A  32   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    MET A 102   CG  -  SD  -  CE  ANGL. DEV. = -11.2 DEGREES          
REMARK 500    ASP A 171   CB  -  CG  -  OD1 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    MET A 173   CG  -  SD  -  CE  ANGL. DEV. = -10.6 DEGREES          
REMARK 500    ARG A 244   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG A 244   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.3 DEGREES          
REMARK 500    ARG A 409   NE  -  CZ  -  NH2 ANGL. DEV. =   3.6 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    GLU A  51      -97.41   -103.63                                   
REMARK 500    SER A  91       88.11   -157.80                                   
REMARK 500    GLU A 109       16.13    -64.26                                   
REMARK 500    GLU A 123       18.60     59.34                                   
REMARK 500    GLU A 158       28.99   -142.19                                   
REMARK 500    LEU A 180       -3.85    -55.91                                   
REMARK 500    PHE A 184      -68.12   -128.56                                   
REMARK 500    ASP A 388     -154.73   -113.61                                   
REMARK 500    VAL A 431       38.68    -98.95                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A 803   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  51   OE2                                                    
REMARK 620 2 ASP A  52   OD2  91.9                                              
REMARK 620 3 ASP A  52   OD1  78.5  43.5                                        
REMARK 620 4 GLU A 123   OE1 100.6 136.7 179.1                                  
REMARK 620 5 ASP A 192   OD2 123.7  76.7 118.7  61.7                            
REMARK 620 6 HOH A 476   O    63.4  70.5 101.0  78.5  60.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 601  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  52   OD2                                                    
REMARK 620 2 GLU A 158   OE1 168.0                                              
REMARK 620 3 ASP A 192   OD2  88.2  91.4                                        
REMARK 620 4 HOH A 476   O    77.9  90.1  88.1                                  
REMARK 620 5 GLV A 501   O1  112.8  68.9 158.7  99.3                            
REMARK 620 6 GLV A 501   O3  130.7  61.2  89.8 151.2  74.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A 801   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 MET A 173   O                                                      
REMARK 620 2 LYS A 175   O   104.0                                              
REMARK 620 3 ASN A 178   OD1  79.6  92.0                                        
REMARK 620 4 ASN A 178   O   147.7  86.1  69.4                                  
REMARK 620 5 GLU A 181   OE1  85.7 167.9  97.0  89.5                            
REMARK 620 6 GLU A 181   OE2  76.7 131.9 133.9 119.2  42.6                      
REMARK 620 7 HOH A 435   O   122.0  88.9 157.5  88.2  79.7  55.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A 804   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PRO A 176   O                                                      
REMARK 620 2 ASN A 178   O    90.5                                              
REMARK 620 3 ASN A 179   OD1 165.3  78.1                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A 802   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A 217   OG                                                     
REMARK 620 2 SER A 217   O    66.8                                              
REMARK 620 3 SER A 221   OG  119.5  71.5                                        
REMARK 620 4 GLY A 252   O    68.7 126.5 160.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLV A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 702                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 703                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 704                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 801                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 802                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 803                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 804                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3OYX   RELATED DB: PDB                                   
REMARK 900 HIGH-OCCUPANCY GLYOXYLATE COMPLEX                                    
REMARK 900 RELATED ID: 3OYZ   RELATED DB: PDB                                   
REMARK 900 PYRUVATE/ACETYL-COA TERNARY COMPLEX                                  
DBREF  3PUG A    1   433  UNP    D4GTL2   D4GTL2_HALVD     1    433             
SEQRES   1 A  433  MET THR GLU ARG ARG HIS ASP ARG GLU PHE VAL ARG THR          
SEQRES   2 A  433  PHE PHE THR SER PRO THR ALA VAL GLU GLY GLU ASP ASP          
SEQRES   3 A  433  SER ALA LYS MET LEU ARG ARG ALA ALA GLY LEU ARG GLY          
SEQRES   4 A  433  MET GLN ALA PRO ASP VAL TRP VAL PRO ASP ASN GLU ASP          
SEQRES   5 A  433  ALA THR ALA PRO SER MET ARG ASP GLU GLY ALA GLU ASN          
SEQRES   6 A  433  ILE VAL GLU VAL ILE SER GLU GLN GLY ALA GLU PHE PRO          
SEQRES   7 A  433  GLY GLU ILE HIS PRO ARG MET VAL TRP HIS ARG ASP SER          
SEQRES   8 A  433  PRO GLU THR ARG TYR GLN GLY PHE GLN HIS MET LEU ASP          
SEQRES   9 A  433  ILE THR ASP PRO GLU ARG GLY ALA VAL GLU HIS ILE HIS          
SEQRES  10 A  433  GLY PHE VAL ILE PRO GLU VAL GLY GLY ILE ASP ASP TRP          
SEQRES  11 A  433  LYS LYS ALA ASP GLU PHE PHE THR ILE VAL GLU HIS GLU          
SEQRES  12 A  433  HIS GLY LEU ASP GLU GLY SER LEU ALA MET SER VAL ILE          
SEQRES  13 A  433  ILE GLU SER GLY GLU ALA GLU LEU ALA MET GLY ASP LEU          
SEQRES  14 A  433  ARG ASP GLU MET GLY LYS PRO THR ASN ASN LEU GLU ARG          
SEQRES  15 A  433  LEU PHE LEU LEU VAL ASP GLY GLU VAL ASP TYR THR LYS          
SEQRES  16 A  433  ASP MET ARG ALA MET THR PRO THR GLY GLU LEU PRO ALA          
SEQRES  17 A  433  TRP PRO GLU LEU ARG HIS ASN THR SER ARG GLY ALA SER          
SEQRES  18 A  433  ALA ALA GLY CYS VAL ALA VAL ASP GLY PRO TYR ASP ASP          
SEQRES  19 A  433  ILE ARG ASP VAL GLU GLY TYR ARG GLU ARG MET THR ASP          
SEQRES  20 A  433  ASN GLN ALA LYS GLY MET LEU GLY ILE TRP SER LEU THR          
SEQRES  21 A  433  PRO GLY GLN VAL VAL GLU ALA ASN THR SER PRO LEU PRO          
SEQRES  22 A  433  PRO LYS THR GLY SER TRP LEU LEU ASP ALA ASP GLY GLU          
SEQRES  23 A  433  GLU VAL GLU LEU ALA SER GLU ASP GLY VAL GLU ALA TYR          
SEQRES  24 A  433  ASP GLY ASP ARG LEU SER LEU GLU ALA THR ASP GLY GLY          
SEQRES  25 A  433  TYR GLU LEU ARG VAL GLY GLY ASP ALA ARG GLU LEU THR          
SEQRES  26 A  433  ALA ASP GLU LEU ARG GLU GLU LEU LEU GLY LEU THR SER          
SEQRES  27 A  433  TYR VAL PRO SER MET ASP ASP ILE VAL ASP SER MET GLU          
SEQRES  28 A  433  GLU PHE GLU ALA ALA LYS GLU ALA GLY ARG GLY ALA ILE          
SEQRES  29 A  433  ALA MET THR GLN SER ALA THR LEU ARG ILE GLY GLY THR          
SEQRES  30 A  433  GLU ILE ASP ILE GLU LYS ASP ARG MET TRP ASP GLU ALA          
SEQRES  31 A  433  THR TYR GLN ALA ALA MET THR PRO ILE SER LEU PHE GLN          
SEQRES  32 A  433  ASP VAL TYR GLU ASN ARG PRO ASP GLN HIS GLU GLU LEU          
SEQRES  33 A  433  GLU GLU ARG TYR GLY ALA GLY VAL VAL GLU ARG ALA MET          
SEQRES  34 A  433  GLU VAL GLY LEU                                              
HET    GLV  A 501       5                                                       
HET     MG  A 601       1                                                       
HET     CL  A 701       1                                                       
HET     CL  A 702       1                                                       
HET     CL  A 703       1                                                       
HET     CL  A 704       1                                                       
HET      K  A 801       1                                                       
HET      K  A 802       1                                                       
HET      K  A 803       1                                                       
HET      K  A 804       1                                                       
HETNAM     GLV GLYOXYLIC ACID                                                   
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      CL CHLORIDE ION                                                     
HETNAM       K POTASSIUM ION                                                    
HETSYN     GLV GLYOXALATE; GLYOXYLATE                                           
FORMUL   2  GLV    C2 H2 O3                                                     
FORMUL   3   MG    MG 2+                                                        
FORMUL   4   CL    4(CL 1-)                                                     
FORMUL   8    K    4(K 1+)                                                      
FORMUL  12  HOH   *71(H2 O)                                                     
HELIX    1   1 ALA A   28  ALA A   35  1                                   8    
HELIX    2   2 GLY A   36  LEU A   37  5                                   2    
HELIX    3   3 ARG A   38  ALA A   42  5                                   5    
HELIX    4   4 ALA A   55  SER A   57  5                                   3    
HELIX    5   5 MET A   58  GLY A   74  1                                  17    
HELIX    6   6 ALA A   75  PHE A   77  5                                   3    
HELIX    7   7 SER A   91  THR A  106  1                                  16    
HELIX    8   8 ASP A  107  GLY A  111  5                                   5    
HELIX    9   9 ALA A  112  ILE A  116  5                                   5    
HELIX   10  10 GLY A  126  HIS A  144  1                                  19    
HELIX   11  11 SER A  159  MET A  166  1                                   8    
HELIX   12  12 ASP A  168  MET A  173  1                                   6    
HELIX   13  13 ASN A  179  GLU A  181  5                                   3    
HELIX   14  14 GLY A  189  MET A  197  1                                   9    
HELIX   15  15 TRP A  209  GLY A  224  1                                  16    
HELIX   16  16 ASP A  237  ALA A  250  1                                  14    
HELIX   17  17 THR A  260  SER A  270  1                                  11    
HELIX   18  18 GLU A  332  THR A  337  5                                   6    
HELIX   19  19 SER A  342  GLU A  354  1                                  13    
HELIX   20  20 ASP A  388  ARG A  409  1                                  22    
HELIX   21  21 ARG A  409  GLY A  421  1                                  13    
HELIX   22  22 GLY A  421  MET A  429  1                                   9    
SHEET    1   A 8 GLU A  80  ILE A  81  0                                        
SHEET    2   A 8 VAL A  45  ASP A  49  1  N  TRP A  46   O  GLU A  80           
SHEET    3   A 8 THR A  13  PRO A  18  1  N  PHE A  15   O  VAL A  47           
SHEET    4   A 8 GLY A 255  SER A 258  1  O  SER A 258   N  PHE A  14           
SHEET    5   A 8 VAL A 226  ASP A 229  1  N  ASP A 229   O  GLY A 255           
SHEET    6   A 8 LEU A 183  ASP A 188  1  N  ASP A 188   O  VAL A 228           
SHEET    7   A 8 ALA A 152  ILE A 157  1  N  VAL A 155   O  VAL A 187           
SHEET    8   A 8 GLY A 118  ILE A 121  1  N  ILE A 121   O  SER A 154           
LINK         OE2 GLU A  51                 K     K A 803     1555   1555  2.94  
LINK         OD2 ASP A  52                MG    MG A 601     1555   1555  2.96  
LINK         OD2 ASP A  52                 K     K A 803     1555   1555  2.87  
LINK         OD1 ASP A  52                 K     K A 803     1555   1555  3.11  
LINK         OE1 GLU A 123                 K     K A 803     1555   1555  3.06  
LINK         OE1 GLU A 158                MG    MG A 601     1555   1555  2.87  
LINK         O   MET A 173                 K     K A 801     1555   1555  2.72  
LINK         O   LYS A 175                 K     K A 801     1555   1555  2.62  
LINK         O   PRO A 176                 K     K A 804     1555   1555  2.84  
LINK         OD1 ASN A 178                 K     K A 801     1555   1555  2.74  
LINK         O   ASN A 178                 K     K A 801     1555   1555  2.80  
LINK         O   ASN A 178                 K     K A 804     1555   1555  2.76  
LINK         OD1 ASN A 179                 K     K A 804     1555   1555  2.86  
LINK         OE1 GLU A 181                 K     K A 801     1555   1555  2.94  
LINK         OE2 GLU A 181                 K     K A 801     1555   1555  3.14  
LINK         OD2 ASP A 192                MG    MG A 601     1555   1555  1.99  
LINK         OD2 ASP A 192                 K     K A 803     1555   1555  2.78  
LINK         OG  SER A 217                 K     K A 802     1555   1555  2.68  
LINK         O   SER A 217                 K     K A 802     1555   1555  3.26  
LINK         OG  SER A 221                 K     K A 802     1555   1555  2.93  
LINK         O   GLY A 252                 K     K A 802     1555   1555  3.01  
LINK         O   HOH A 435                 K     K A 801     1555   1555  2.74  
LINK         O   HOH A 476                MG    MG A 601     1555   1555  1.95  
LINK         O   HOH A 476                 K     K A 803     1555   1555  2.63  
LINK         O1  GLV A 501                MG    MG A 601     1555   1555  2.00  
LINK         O3  GLV A 501                MG    MG A 601     1555   1555  2.42  
SITE     1 AC1 10 ARG A  84  GLU A 158  GLY A 189  GLU A 190                    
SITE     2 AC1 10 VAL A 191  ASP A 192  PRO A 231  HOH A 476                    
SITE     3 AC1 10 HOH A 485   MG A 601                                          
SITE     1 AC2  6 ASP A  52  GLU A 158  ASP A 192  HOH A 476                    
SITE     2 AC2  6 GLV A 501    K A 803                                          
SITE     1 AC3  3 ARG A 198  ALA A 227    K A 802                               
SITE     1 AC4  3 ARG A  89  PRO A  92  ARG A  95                               
SITE     1 AC5  1 ALA A 208                                                     
SITE     1 AC6  1 ARG A 218                                                     
SITE     1 AC7  5 MET A 173  LYS A 175  ASN A 178  GLU A 181                    
SITE     2 AC7  5 HOH A 435                                                     
SITE     1 AC8  5 MET A 197  SER A 217  SER A 221  GLY A 252                    
SITE     2 AC8  5  CL A 701                                                     
SITE     1 AC9  6 GLU A  51  ASP A  52  GLU A 123  ASP A 192                    
SITE     2 AC9  6 HOH A 476   MG A 601                                          
SITE     1 BC1  3 PRO A 176  ASN A 178  ASN A 179                               
CRYST1  156.370  156.370  141.455  90.00  90.00 120.00 H 3 2        18          
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      0.006395  0.003692  0.000000        0.00000                         
SCALE2      0.000000  0.007384  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007069        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system