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Database: PDB
Entry: 2RUS
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Original site: 2RUS 
HEADER    LYASE(CARBON-CARBON)                    11-OCT-91   2RUS              
TITLE     CRYSTAL STRUCTURE OF THE TERNARY COMPLEX OF RIBULOSE-1,5-             
TITLE    2 BISPHOSPHATE CARBOXYLASE, MG(II), AND ACTIVATOR CO2 AT 2.3-          
TITLE    3 ANGSTROMS RESOLUTION                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RUBISCO (RIBULOSE-1,5-BISPHOSPHATE                         
COMPND   3 CARBOXYLASE(SLASH)OXYGENASE);                                        
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 EC: 4.1.1.39;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RHODOSPIRILLUM RUBRUM;                          
SOURCE   3 ORGANISM_TAXID: 1085                                                 
KEYWDS    LYASE(CARBON-CARBON)                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.LUNDQVIST,G.SCHNEIDER                                               
REVDAT   3   24-FEB-09 2RUS    1       VERSN                                    
REVDAT   2   01-APR-03 2RUS    1       JRNL                                     
REVDAT   1   15-OCT-91 2RUS    0                                                
JRNL        AUTH   T.LUNDQVIST,G.SCHNEIDER                                      
JRNL        TITL   CRYSTAL STRUCTURE OF THE TERNARY COMPLEX OF                  
JRNL        TITL 2 RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE, MG(II), AND           
JRNL        TITL 3 ACTIVATOR CO2 AT 2.3-A RESOLUTION.                           
JRNL        REF    BIOCHEMISTRY                  V.  30   904 1991              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   1899197                                                      
JRNL        DOI    10.1021/BI00218A004                                          
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   G.SCHNEIDER,Y.LINDQVIST,T.LUNDQVIST                          
REMARK   1  TITL   CRYSTALLOGRAPHIC REFINEMENT AND STRUCTURE OF                 
REMARK   1  TITL 2 RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE FROM                   
REMARK   1  TITL 3 RHODOSPIRILLUM RUBRUM AT 1.7 ANGSTROMS RESOLUTION            
REMARK   1  REF    J.MOL.BIOL.                   V. 211   989 1990              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   T.LUNDQVIST,G.SCHNEIDER                                      
REMARK   1  TITL   CRYSTAL STRUCTURE OF THE COMPLEX OF                          
REMARK   1  TITL 2 RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE AND A                  
REMARK   1  TITL 3 TRANSITION STATE ANALOGUE, 2-CARBOXY-D-ARABINITOL            
REMARK   1  TITL 4 1,5-BISPHOSPHATE                                             
REMARK   1  REF    J.BIOL.CHEM.                  V. 264  7078 1989              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   I.ANDERSSON,S.KNIGHT,G.SCHNEIDER,Y.LINDQVIST,                
REMARK   1  AUTH 2 T.LUNDQVIST,C.-I.BRANDEN,G.H.LORIMER                         
REMARK   1  TITL   CRYSTAL STRUCTURE OF THE ACTIVE SITE OF                      
REMARK   1  TITL 2 RIBULOSE-BISPHOSPHATE CARBOXYLASE                            
REMARK   1  REF    NATURE                        V. 337   229 1989              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   T.LUNDQVIST,G.SCHNEIDER                                      
REMARK   1  TITL   CRYSTAL STRUCTURE OF THE BINARY COMPLEX OF                   
REMARK   1  TITL 2 RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE AND ITS                
REMARK   1  TITL 3 PRODUCT, 3-PHOSPHO-D-GLYCERATE                               
REMARK   1  REF    J.BIOL.CHEM.                  V. 263  3643 1988              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1 REFERENCE 5                                                          
REMARK   1  AUTH   G.SCHNEIDER,Y.LINDQVIST,C.-I.BRANDEN,G.LORIMER               
REMARK   1  TITL   THREE-DIMENSIONAL STRUCTURE OF                               
REMARK   1  TITL 2 RIBULOSE-1,5-BISPHOSPHATE                                    
REMARK   1  TITL 3 CARBOXYLASE(SLASH)OXYGENASE FROM RHODOSPIRILLUM              
REMARK   1  TITL 4 RUBRUM AT 2.9 ANGSTROMS RESOLUTION                           
REMARK   1  REF    EMBO J.                       V.   5  3409 1986              
REMARK   1  REFN                   ISSN 0261-4189                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PROLSQ                                               
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 5.50                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : NULL                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.193                           
REMARK   3   R VALUE            (WORKING SET) : NULL                            
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6725                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 8                                       
REMARK   3   SOLVENT ATOMS            : 714                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.013 ; 0.020               
REMARK   3    ANGLE DISTANCE                  (A) : 0.047 ; 0.040               
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.049 ; 0.050               
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : 0.012 ; 0.020               
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.182 ; 0.150               
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : 0.193 ; 0.300               
REMARK   3    MULTIPLE TORSION                (A) : 0.309 ; 0.300               
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : 0.192 ; 0.300               
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : 8.800 ; 3.000               
REMARK   3    STAGGERED                 (DEGREES) : 22.400; 15.000              
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND               (A**2) : NULL  ; NULL                
REMARK   3   MAIN-CHAIN ANGLE              (A**2) : NULL  ; NULL                
REMARK   3   SIDE-CHAIN BOND               (A**2) : NULL  ; NULL                
REMARK   3   SIDE-CHAIN ANGLE              (A**2) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:  THE STRUCTURE WAS DETERMINED BY          
REMARK   3  DIFFERENCE FOURIER TECHNIQUES WITH THE INITIAL PHASES DERIVED       
REMARK   3  FROM THE NATIVE STRUCTURE.                                          
REMARK   4                                                                      
REMARK   4 2RUS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.49                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       35.30000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6640 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 31000 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -45.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400                                                                      
REMARK 400 RESIDUE 191 OF EACH IS CHAIN IS A MODIFIED ACTIVATOR LYSINE          
REMARK 400 WHICH IS CARBAMYLATED AT THE EPSILON-AMINO GROUP.  THE               
REMARK 400 CARBAMYL ACTIVATOR GROUP IS PRESENTED AS HET GROUP *FOR*             
REMARK 400 AT THE END OF EACH CHAIN.                                            
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     THR A   -23                                                      
REMARK 465     MET A   -22                                                      
REMARK 465     ILE A   -21                                                      
REMARK 465     THR A   -20                                                      
REMARK 465     ASN A   -19                                                      
REMARK 465     SER A   -18                                                      
REMARK 465     PRO A   -17                                                      
REMARK 465     ASP A   -16                                                      
REMARK 465     ARG A   -15                                                      
REMARK 465     TRP A   -14                                                      
REMARK 465     GLY A   -13                                                      
REMARK 465     TYR A   -12                                                      
REMARK 465     SER A   -11                                                      
REMARK 465     ALA A   -10                                                      
REMARK 465     PRO A    -9                                                      
REMARK 465     HIS A    -8                                                      
REMARK 465     ARG A    -7                                                      
REMARK 465     THR A    -6                                                      
REMARK 465     SER A    -5                                                      
REMARK 465     ARG A    -4                                                      
REMARK 465     GLU A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     PRO A    -1                                                      
REMARK 465     PRO A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     VAL A    55                                                      
REMARK 465     GLU A    56                                                      
REMARK 465     VAL A    57                                                      
REMARK 465     CYS A    58                                                      
REMARK 465     THR A    59                                                      
REMARK 465     THR A    60                                                      
REMARK 465     ASP A    61                                                      
REMARK 465     ASP A    62                                                      
REMARK 465     PHE A    63                                                      
REMARK 465     MET A   325                                                      
REMARK 465     GLY A   326                                                      
REMARK 465     PHE A   327                                                      
REMARK 465     GLY A   328                                                      
REMARK 465     LYS A   329                                                      
REMARK 465     MET A   330                                                      
REMARK 465     GLU A   331                                                      
REMARK 465     GLY A   332                                                      
REMARK 465     GLU A   333                                                      
REMARK 465     SER A   334                                                      
REMARK 465     GLU A   458                                                      
REMARK 465     ASP A   459                                                      
REMARK 465     THR A   460                                                      
REMARK 465     ARG A   461                                                      
REMARK 465     SER A   462                                                      
REMARK 465     ALA A   463                                                      
REMARK 465     LEU A   464                                                      
REMARK 465     PRO A   465                                                      
REMARK 465     ALA A   466                                                      
REMARK 465     THR B   -23                                                      
REMARK 465     MET B   -22                                                      
REMARK 465     ILE B   -21                                                      
REMARK 465     THR B   -20                                                      
REMARK 465     ASN B   -19                                                      
REMARK 465     SER B   -18                                                      
REMARK 465     PRO B   -17                                                      
REMARK 465     ASP B   -16                                                      
REMARK 465     ARG B   -15                                                      
REMARK 465     TRP B   -14                                                      
REMARK 465     GLY B   -13                                                      
REMARK 465     TYR B   -12                                                      
REMARK 465     SER B   -11                                                      
REMARK 465     ALA B   -10                                                      
REMARK 465     PRO B    -9                                                      
REMARK 465     HIS B    -8                                                      
REMARK 465     ARG B    -7                                                      
REMARK 465     THR B    -6                                                      
REMARK 465     SER B    -5                                                      
REMARK 465     ARG B    -4                                                      
REMARK 465     GLU B    -3                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     PRO B    -1                                                      
REMARK 465     PRO B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ASP B     2                                                      
REMARK 465     VAL B    55                                                      
REMARK 465     GLU B    56                                                      
REMARK 465     VAL B    57                                                      
REMARK 465     CYS B    58                                                      
REMARK 465     THR B    59                                                      
REMARK 465     THR B    60                                                      
REMARK 465     ASP B    61                                                      
REMARK 465     ASP B    62                                                      
REMARK 465     PHE B    63                                                      
REMARK 465     MET B   330                                                      
REMARK 465     GLU B   331                                                      
REMARK 465     GLU B   458                                                      
REMARK 465     ASP B   459                                                      
REMARK 465     THR B   460                                                      
REMARK 465     ARG B   461                                                      
REMARK 465     SER B   462                                                      
REMARK 465     ALA B   463                                                      
REMARK 465     LEU B   464                                                      
REMARK 465     PRO B   465                                                      
REMARK 465     ALA B   466                                                      
REMARK 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C SSEQI                                                      
REMARK 475     THR A   64                                                       
REMARK 475     THR A  324                                                       
REMARK 475     GLN B    3                                                       
REMARK 475     ASN B   54                                                       
REMARK 475     THR B   64                                                       
REMARK 475     GLY B  332                                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH B   540     O    HOH B   691     2645     0.46            
REMARK 500   O    HOH A   661     O    HOH A   779     2656     1.54            
REMARK 500   O    HOH A   681     O    HOH A   685     2646     1.80            
REMARK 500   O    HOH A   738     O    HOH B   839     1545     1.87            
REMARK 500   O    PHE B   327     O    HOH B   690     2645     1.89            
REMARK 500   NE   ARG B   408     O    HOH B   851     2745     1.93            
REMARK 500   CD   LYS B   431     O    HOH B   521     2745     1.96            
REMARK 500   O    HOH B   644     O    HOH B   807     2755     1.99            
REMARK 500   CE   LYS B   431     O    HOH B   837     2745     2.11            
REMARK 500   O    HOH A   698     O    HOH B   563     1455     2.13            
REMARK 500   CG   GLU B   333     O    HOH A   803     2655     2.15            
REMARK 500   CA   GLY B   450     O    HOH B   833     2645     2.18            
REMARK 500   O    HOH A   631     O    HOH B   569     1545     2.18            
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    GLN A   3   N   -  CA  -  CB  ANGL. DEV. =  11.4 DEGREES          
REMARK 500    GLN A   3   CA  -  C   -  O   ANGL. DEV. =  16.9 DEGREES          
REMARK 500    SER A   4   N   -  CA  -  C   ANGL. DEV. = -16.5 DEGREES          
REMARK 500    ARG A   6   NE  -  CZ  -  NH1 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    LEU A  10   N   -  CA  -  C   ANGL. DEV. = -16.8 DEGREES          
REMARK 500    LEU A  10   CA  -  C   -  O   ANGL. DEV. = -12.7 DEGREES          
REMARK 500    ALA A  11   N   -  CA  -  CB  ANGL. DEV. =   8.9 DEGREES          
REMARK 500    GLU A  14   OE1 -  CD  -  OE2 ANGL. DEV. =  -8.1 DEGREES          
REMARK 500    LEU A  25   CB  -  CA  -  C   ANGL. DEV. =  12.9 DEGREES          
REMARK 500    ASP A  75   CB  -  CG  -  OD2 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    ARG A  78   CD  -  NE  -  CZ  ANGL. DEV. =   8.5 DEGREES          
REMARK 500    ARG A  78   NE  -  CZ  -  NH2 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ARG A  92   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ARG A  92   NE  -  CZ  -  NH2 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    THR A  95   CA  -  CB  -  CG2 ANGL. DEV. =  11.8 DEGREES          
REMARK 500    MET A 109   N   -  CA  -  CB  ANGL. DEV. = -11.9 DEGREES          
REMARK 500    MET A 109   CA  -  CB  -  CG  ANGL. DEV. =  12.2 DEGREES          
REMARK 500    GLY A 116   N   -  CA  -  C   ANGL. DEV. = -18.3 DEGREES          
REMARK 500    ASP A 125   CB  -  CG  -  OD1 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    TYR A 127   CB  -  CG  -  CD2 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    TYR A 127   CB  -  CG  -  CD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ARG A 133   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.3 DEGREES          
REMARK 500    ASP A 137   CB  -  CG  -  OD1 ANGL. DEV. =   8.0 DEGREES          
REMARK 500    ASP A 137   CB  -  CG  -  OD2 ANGL. DEV. =  -7.3 DEGREES          
REMARK 500    GLU A 154   OE1 -  CD  -  OE2 ANGL. DEV. =   7.3 DEGREES          
REMARK 500    ARG A 172   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES          
REMARK 500    ARG A 172   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    GLU A 178   OE1 -  CD  -  OE2 ANGL. DEV. =   7.4 DEGREES          
REMARK 500    PHE A 189   N   -  CA  -  CB  ANGL. DEV. = -10.9 DEGREES          
REMARK 500    ASP A 193   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ARG A 205   CD  -  NE  -  CZ  ANGL. DEV. =  11.5 DEGREES          
REMARK 500    ARG A 205   NE  -  CZ  -  NH1 ANGL. DEV. =  -6.6 DEGREES          
REMARK 500    ARG A 205   NE  -  CZ  -  NH2 ANGL. DEV. =   8.3 DEGREES          
REMARK 500    ASP A 206   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP A 213   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ARG A 217   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ASP A 235   CB  -  CG  -  OD2 ANGL. DEV. =  -7.0 DEGREES          
REMARK 500    GLU A 245   CA  -  CB  -  CG  ANGL. DEV. =  17.1 DEGREES          
REMARK 500    ALA A 259   N   -  CA  -  CB  ANGL. DEV. =   8.5 DEGREES          
REMARK 500    ASP A 263   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    GLY A 264   N   -  CA  -  C   ANGL. DEV. =  15.7 DEGREES          
REMARK 500    GLY A 264   C   -  N   -  CA  ANGL. DEV. =  20.4 DEGREES          
REMARK 500    TYR A 265   CB  -  CG  -  CD1 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ARG A 277   NE  -  CZ  -  NH1 ANGL. DEV. =   8.4 DEGREES          
REMARK 500    ARG A 278   CD  -  NE  -  CZ  ANGL. DEV. =   9.2 DEGREES          
REMARK 500    ARG A 278   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    GLY A 292   C   -  N   -  CA  ANGL. DEV. =  16.1 DEGREES          
REMARK 500    TYR A 303   CB  -  CG  -  CD2 ANGL. DEV. =  -4.4 DEGREES          
REMARK 500    TYR A 303   CB  -  CG  -  CD1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG A 313   CG  -  CD  -  NE  ANGL. DEV. =  15.0 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     120 ANGLE DEVIATIONS.                             
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    SER A   4     -153.61    -82.44                                   
REMARK 500    SER A   5      -55.41     56.86                                   
REMARK 500    ASN A   9       69.64   -152.59                                   
REMARK 500    ALA A  11      -11.74    140.16                                   
REMARK 500    LYS A  33      -81.38    -37.89                                   
REMARK 500    ALA A  34       98.27    174.13                                   
REMARK 500    SER A  50     -111.63   -127.99                                   
REMARK 500    THR A  53      -93.39     99.07                                   
REMARK 500    ARG A  65       48.80   -144.94                                   
REMARK 500    ASP A  75       97.56   -165.85                                   
REMARK 500    THR A  95      -72.73    -67.38                                   
REMARK 500    MET A 109       55.06   -167.55                                   
REMARK 500    GLN A 113       61.55   -116.42                                   
REMARK 500    ASP A 117      -41.35    129.72                                   
REMARK 500    ASN A 198       55.43   -118.04                                   
REMARK 500    ALA A 289      133.97    -24.47                                   
REMARK 500    VAL A 294      -60.15   -109.23                                   
REMARK 500    THR A 295       41.99    -79.03                                   
REMARK 500    PHE A 352      -34.41   -135.02                                   
REMARK 500    MET A 376      -66.30    -27.60                                   
REMARK 500    ASP A 443      -48.62    159.58                                   
REMARK 500    PRO A 449      -73.08    -26.96                                   
REMARK 500    TRP A 451      -66.64     17.33                                   
REMARK 500    ARG A 452      -71.74    -45.34                                   
REMARK 500    SER B   4      -75.38    -63.55                                   
REMARK 500    SER B   5       19.93    -54.91                                   
REMARK 500    ASN B   9       76.85   -164.73                                   
REMARK 500    SER B  50     -106.71   -136.99                                   
REMARK 500    THR B  53      -65.74     85.81                                   
REMARK 500    MET B 109      -55.85   -131.72                                   
REMARK 500    GLN B 113       33.23    -87.31                                   
REMARK 500    MET B 115       52.07   -107.88                                   
REMARK 500    TYR B 120      140.09     68.49                                   
REMARK 500    ALA B 134        2.47    -68.72                                   
REMARK 500    ASN B 142     -155.98   -147.71                                   
REMARK 500    ASP B 156       43.32     34.14                                   
REMARK 500    ASN B 198       52.42   -108.43                                   
REMARK 500    HIS B 291      -38.08    -29.60                                   
REMARK 500    SER B 296      138.50    -39.14                                   
REMARK 500    THR B 322     -159.77   -144.29                                   
REMARK 500    MET B 325     -121.67     74.28                                   
REMARK 500    PHE B 327       73.06    149.33                                   
REMARK 500    GLU B 333      -82.83    139.43                                   
REMARK 500    SER B 334     -131.18     77.23                                   
REMARK 500    ASP B 336       51.49    124.13                                   
REMARK 500    ASN B 387       58.82    -67.09                                   
REMARK 500    ALA B 396      -72.67    -80.04                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER                       
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    THR A  64        -20.59                                           
REMARK 500    GLY A 323        -12.21                                           
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 504        DISTANCE =  7.27 ANGSTROMS                       
REMARK 525    HOH A 506        DISTANCE =  6.80 ANGSTROMS                       
REMARK 525    HOH A 529        DISTANCE =  9.16 ANGSTROMS                       
REMARK 525    HOH A 530        DISTANCE =  5.49 ANGSTROMS                       
REMARK 525    HOH B 530        DISTANCE =  7.38 ANGSTROMS                       
REMARK 525    HOH A 536        DISTANCE = 10.06 ANGSTROMS                       
REMARK 525    HOH A 539        DISTANCE =  6.65 ANGSTROMS                       
REMARK 525    HOH B 551        DISTANCE =  7.06 ANGSTROMS                       
REMARK 525    HOH A 554        DISTANCE =  6.21 ANGSTROMS                       
REMARK 525    HOH A 560        DISTANCE = 10.37 ANGSTROMS                       
REMARK 525    HOH B 562        DISTANCE = 13.37 ANGSTROMS                       
REMARK 525    HOH A 569        DISTANCE =  7.90 ANGSTROMS                       
REMARK 525    HOH B 569        DISTANCE = 11.01 ANGSTROMS                       
REMARK 525    HOH A 570        DISTANCE =  5.44 ANGSTROMS                       
REMARK 525    HOH A 573        DISTANCE =  5.98 ANGSTROMS                       
REMARK 525    HOH B 582        DISTANCE =  8.22 ANGSTROMS                       
REMARK 525    HOH B 583        DISTANCE =  7.67 ANGSTROMS                       
REMARK 525    HOH A 588        DISTANCE =  5.32 ANGSTROMS                       
REMARK 525    HOH B 594        DISTANCE =  9.77 ANGSTROMS                       
REMARK 525    HOH B 603        DISTANCE =  9.44 ANGSTROMS                       
REMARK 525    HOH B 607        DISTANCE =  6.97 ANGSTROMS                       
REMARK 525    HOH A 609        DISTANCE = 11.24 ANGSTROMS                       
REMARK 525    HOH A 615        DISTANCE =  6.65 ANGSTROMS                       
REMARK 525    HOH A 616        DISTANCE = 12.77 ANGSTROMS                       
REMARK 525    HOH A 617        DISTANCE =  9.30 ANGSTROMS                       
REMARK 525    HOH B 617        DISTANCE =  9.97 ANGSTROMS                       
REMARK 525    HOH A 618        DISTANCE =  9.32 ANGSTROMS                       
REMARK 525    HOH B 621        DISTANCE =  5.10 ANGSTROMS                       
REMARK 525    HOH A 623        DISTANCE =  7.51 ANGSTROMS                       
REMARK 525    HOH B 624        DISTANCE =  5.71 ANGSTROMS                       
REMARK 525    HOH A 625        DISTANCE = 11.64 ANGSTROMS                       
REMARK 525    HOH A 627        DISTANCE =  5.08 ANGSTROMS                       
REMARK 525    HOH A 629        DISTANCE =  9.69 ANGSTROMS                       
REMARK 525    HOH B 629        DISTANCE =  8.52 ANGSTROMS                       
REMARK 525    HOH B 630        DISTANCE =  5.98 ANGSTROMS                       
REMARK 525    HOH B 631        DISTANCE =  7.65 ANGSTROMS                       
REMARK 525    HOH A 632        DISTANCE =  5.55 ANGSTROMS                       
REMARK 525    HOH A 634        DISTANCE =  7.40 ANGSTROMS                       
REMARK 525    HOH A 642        DISTANCE =  9.95 ANGSTROMS                       
REMARK 525    HOH B 642        DISTANCE =  7.37 ANGSTROMS                       
REMARK 525    HOH B 653        DISTANCE =  6.35 ANGSTROMS                       
REMARK 525    HOH A 656        DISTANCE = 10.79 ANGSTROMS                       
REMARK 525    HOH B 657        DISTANCE = 10.68 ANGSTROMS                       
REMARK 525    HOH A 659        DISTANCE =  7.37 ANGSTROMS                       
REMARK 525    HOH B 659        DISTANCE =  5.28 ANGSTROMS                       
REMARK 525    HOH B 660        DISTANCE = 12.77 ANGSTROMS                       
REMARK 525    HOH A 661        DISTANCE = 10.54 ANGSTROMS                       
REMARK 525    HOH B 661        DISTANCE =  7.37 ANGSTROMS                       
REMARK 525    HOH B 663        DISTANCE =  5.27 ANGSTROMS                       
REMARK 525    HOH B 677        DISTANCE =  9.04 ANGSTROMS                       
REMARK 525    HOH B 680        DISTANCE =  5.11 ANGSTROMS                       
REMARK 525    HOH A 685        DISTANCE =  5.08 ANGSTROMS                       
REMARK 525    HOH A 688        DISTANCE =  9.18 ANGSTROMS                       
REMARK 525    HOH A 690        DISTANCE = 13.39 ANGSTROMS                       
REMARK 525    HOH B 690        DISTANCE =  9.10 ANGSTROMS                       
REMARK 525    HOH B 691        DISTANCE = 12.92 ANGSTROMS                       
REMARK 525    HOH A 695        DISTANCE =  8.19 ANGSTROMS                       
REMARK 525    HOH B 695        DISTANCE = 14.11 ANGSTROMS                       
REMARK 525    HOH B 696        DISTANCE =  6.54 ANGSTROMS                       
REMARK 525    HOH A 698        DISTANCE = 10.16 ANGSTROMS                       
REMARK 525    HOH B 702        DISTANCE =  5.25 ANGSTROMS                       
REMARK 525    HOH B 708        DISTANCE =  5.20 ANGSTROMS                       
REMARK 525    HOH B 710        DISTANCE =  7.53 ANGSTROMS                       
REMARK 525    HOH B 711        DISTANCE =  9.35 ANGSTROMS                       
REMARK 525    HOH A 713        DISTANCE =  5.27 ANGSTROMS                       
REMARK 525    HOH B 714        DISTANCE =  8.97 ANGSTROMS                       
REMARK 525    HOH B 715        DISTANCE =  5.91 ANGSTROMS                       
REMARK 525    HOH B 716        DISTANCE = 14.52 ANGSTROMS                       
REMARK 525    HOH A 717        DISTANCE = 10.00 ANGSTROMS                       
REMARK 525    HOH A 719        DISTANCE = 11.47 ANGSTROMS                       
REMARK 525    HOH A 721        DISTANCE = 14.89 ANGSTROMS                       
REMARK 525    HOH B 721        DISTANCE =  7.44 ANGSTROMS                       
REMARK 525    HOH B 723        DISTANCE =  9.73 ANGSTROMS                       
REMARK 525    HOH A 725        DISTANCE =  7.98 ANGSTROMS                       
REMARK 525    HOH A 728        DISTANCE = 11.03 ANGSTROMS                       
REMARK 525    HOH A 729        DISTANCE =  6.98 ANGSTROMS                       
REMARK 525    HOH B 729        DISTANCE =  5.78 ANGSTROMS                       
REMARK 525    HOH B 731        DISTANCE =  6.72 ANGSTROMS                       
REMARK 525    HOH A 733        DISTANCE =  6.18 ANGSTROMS                       
REMARK 525    HOH A 735        DISTANCE =  6.39 ANGSTROMS                       
REMARK 525    HOH A 736        DISTANCE =  6.07 ANGSTROMS                       
REMARK 525    HOH A 739        DISTANCE =  7.51 ANGSTROMS                       
REMARK 525    HOH B 739        DISTANCE = 13.39 ANGSTROMS                       
REMARK 525    HOH A 746        DISTANCE =  5.46 ANGSTROMS                       
REMARK 525    HOH A 747        DISTANCE = 14.38 ANGSTROMS                       
REMARK 525    HOH B 748        DISTANCE =  5.13 ANGSTROMS                       
REMARK 525    HOH B 751        DISTANCE =  5.78 ANGSTROMS                       
REMARK 525    HOH B 752        DISTANCE =  5.83 ANGSTROMS                       
REMARK 525    HOH A 754        DISTANCE =  6.59 ANGSTROMS                       
REMARK 525    HOH B 754        DISTANCE =  9.14 ANGSTROMS                       
REMARK 525    HOH A 755        DISTANCE = 11.07 ANGSTROMS                       
REMARK 525    HOH A 759        DISTANCE =  5.68 ANGSTROMS                       
REMARK 525    HOH B 759        DISTANCE =  5.26 ANGSTROMS                       
REMARK 525    HOH A 761        DISTANCE =  7.38 ANGSTROMS                       
REMARK 525    HOH A 762        DISTANCE = 12.89 ANGSTROMS                       
REMARK 525    HOH A 765        DISTANCE = 13.06 ANGSTROMS                       
REMARK 525    HOH A 769        DISTANCE = 10.38 ANGSTROMS                       
REMARK 525    HOH B 769        DISTANCE =  9.24 ANGSTROMS                       
REMARK 525    HOH A 770        DISTANCE =  6.87 ANGSTROMS                       
REMARK 525    HOH B 771        DISTANCE =  6.16 ANGSTROMS                       
REMARK 525    HOH B 775        DISTANCE = 13.97 ANGSTROMS                       
REMARK 525    HOH B 777        DISTANCE =  5.35 ANGSTROMS                       
REMARK 525    HOH A 779        DISTANCE =  5.05 ANGSTROMS                       
REMARK 525    HOH B 782        DISTANCE =  6.22 ANGSTROMS                       
REMARK 525    HOH A 783        DISTANCE =  9.17 ANGSTROMS                       
REMARK 525    HOH B 783        DISTANCE = 11.44 ANGSTROMS                       
REMARK 525    HOH A 784        DISTANCE =  6.15 ANGSTROMS                       
REMARK 525    HOH A 786        DISTANCE =  5.65 ANGSTROMS                       
REMARK 525    HOH B 789        DISTANCE =  7.14 ANGSTROMS                       
REMARK 525    HOH A 792        DISTANCE =  6.44 ANGSTROMS                       
REMARK 525    HOH A 795        DISTANCE =  9.66 ANGSTROMS                       
REMARK 525    HOH B 795        DISTANCE =  9.91 ANGSTROMS                       
REMARK 525    HOH B 797        DISTANCE =  5.33 ANGSTROMS                       
REMARK 525    HOH A 798        DISTANCE =  5.73 ANGSTROMS                       
REMARK 525    HOH A 799        DISTANCE =  6.42 ANGSTROMS                       
REMARK 525    HOH B 799        DISTANCE =  7.62 ANGSTROMS                       
REMARK 525    HOH A 803        DISTANCE =  8.13 ANGSTROMS                       
REMARK 525    HOH B 803        DISTANCE =  6.08 ANGSTROMS                       
REMARK 525    HOH B 804        DISTANCE =  7.62 ANGSTROMS                       
REMARK 525    HOH A 805        DISTANCE =  8.41 ANGSTROMS                       
REMARK 525    HOH B 805        DISTANCE =  6.71 ANGSTROMS                       
REMARK 525    HOH A 809        DISTANCE =  6.10 ANGSTROMS                       
REMARK 525    HOH B 811        DISTANCE = 12.64 ANGSTROMS                       
REMARK 525    HOH A 812        DISTANCE =  7.91 ANGSTROMS                       
REMARK 525    HOH A 814        DISTANCE = 12.68 ANGSTROMS                       
REMARK 525    HOH A 815        DISTANCE =  8.34 ANGSTROMS                       
REMARK 525    HOH A 816        DISTANCE =  6.50 ANGSTROMS                       
REMARK 525    HOH B 817        DISTANCE = 12.28 ANGSTROMS                       
REMARK 525    HOH A 818        DISTANCE =  7.68 ANGSTROMS                       
REMARK 525    HOH A 819        DISTANCE =  7.78 ANGSTROMS                       
REMARK 525    HOH A 820        DISTANCE = 19.20 ANGSTROMS                       
REMARK 525    HOH A 821        DISTANCE = 13.75 ANGSTROMS                       
REMARK 525    HOH B 821        DISTANCE =  5.39 ANGSTROMS                       
REMARK 525    HOH B 822        DISTANCE =  8.11 ANGSTROMS                       
REMARK 525    HOH B 824        DISTANCE =  9.08 ANGSTROMS                       
REMARK 525    HOH A 826        DISTANCE =  9.61 ANGSTROMS                       
REMARK 525    HOH B 827        DISTANCE =  5.80 ANGSTROMS                       
REMARK 525    HOH A 828        DISTANCE =  8.50 ANGSTROMS                       
REMARK 525    HOH B 829        DISTANCE = 13.50 ANGSTROMS                       
REMARK 525    HOH B 830        DISTANCE =  6.58 ANGSTROMS                       
REMARK 525    HOH A 831        DISTANCE = 10.05 ANGSTROMS                       
REMARK 525    HOH B 833        DISTANCE = 10.00 ANGSTROMS                       
REMARK 525    HOH B 834        DISTANCE =  6.15 ANGSTROMS                       
REMARK 525    HOH A 836        DISTANCE =  5.29 ANGSTROMS                       
REMARK 525    HOH B 838        DISTANCE =  7.25 ANGSTROMS                       
REMARK 525    HOH B 855        DISTANCE =  6.17 ANGSTROMS                       
REMARK 525    HOH B 860        DISTANCE =  6.73 ANGSTROMS                       
REMARK 525    HOH B 868        DISTANCE =  7.97 ANGSTROMS                       
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                              MG A 500  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 FOR A 501   O                                                      
REMARK 620 2 HOH A 822   O    84.8                                              
REMARK 620 3 ASP A 193   OD2  89.6 165.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 500  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 875   O                                                      
REMARK 620 2 ASN A 111   ND2 128.5                                              
REMARK 620 N                    1                                               
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEETS PRESENTED AS *ACT* AND *BCT* ON SHEET RECORDS             
REMARK 700 BELOW ARE ACTUALLY EIGHT-STRANDED BETA-BARRELS.  THIS IS             
REMARK 700 REPRESENTED BY A NINE-STRANDED SHEET IN WHICH THE FIRST AND          
REMARK 700 LAST STRANDS ARE IDENTICAL.                                          
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 500                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 500                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FOR A 501                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FOR B 501                 
DBREF  2RUS A    1   466  UNP    P04718   RBL2_RHORU       1    466             
DBREF  2RUS B    1   466  UNP    P04718   RBL2_RHORU       1    466             
SEQADV 2RUS ASP A   91  UNP  P04718    HIS    91 CONFLICT                       
SEQADV 2RUS ASP B   91  UNP  P04718    HIS    91 CONFLICT                       
SEQRES   1 A  490  THR MET ILE THR ASN SER PRO ASP ARG TRP GLY TYR SER          
SEQRES   2 A  490  ALA PRO HIS ARG THR SER ARG GLU SER PRO PRO MET ASP          
SEQRES   3 A  490  GLN SER SER ARG TYR VAL ASN LEU ALA LEU LYS GLU GLU          
SEQRES   4 A  490  ASP LEU ILE ALA GLY GLY GLU HIS VAL LEU CYS ALA TYR          
SEQRES   5 A  490  ILE MET LYS PRO LYS ALA GLY TYR GLY TYR VAL ALA THR          
SEQRES   6 A  490  ALA ALA HIS PHE ALA ALA GLU SER SER THR GLY THR ASN          
SEQRES   7 A  490  VAL GLU VAL CYS THR THR ASP ASP PHE THR ARG GLY VAL          
SEQRES   8 A  490  ASP ALA LEU VAL TYR GLU VAL ASP GLU ALA ARG GLU LEU          
SEQRES   9 A  490  THR LYS ILE ALA TYR PRO VAL ALA LEU PHE ASP ARG ASN          
SEQRES  10 A  490  ILE THR ASP GLY LYS ALA MET ILE ALA SER PHE LEU THR          
SEQRES  11 A  490  LEU THR MET GLY ASN ASN GLN GLY MET GLY ASP VAL GLU          
SEQRES  12 A  490  TYR ALA LYS MET HIS ASP PHE TYR VAL PRO GLU ALA TYR          
SEQRES  13 A  490  ARG ALA LEU PHE ASP GLY PRO SER VAL ASN ILE SER ALA          
SEQRES  14 A  490  LEU TRP LYS VAL LEU GLY ARG PRO GLU VAL ASP GLY GLY          
SEQRES  15 A  490  LEU VAL VAL GLY THR ILE ILE LYS PRO LYS LEU GLY LEU          
SEQRES  16 A  490  ARG PRO LYS PRO PHE ALA GLU ALA CYS HIS ALA PHE TRP          
SEQRES  17 A  490  LEU GLY GLY ASP PHE ILE LYS ASN ASP GLU PRO GLN GLY          
SEQRES  18 A  490  ASN GLN PRO PHE ALA PRO LEU ARG ASP THR ILE ALA LEU          
SEQRES  19 A  490  VAL ALA ASP ALA MET ARG ARG ALA GLN ASP GLU THR GLY          
SEQRES  20 A  490  GLU ALA LYS LEU PHE SER ALA ASN ILE THR ALA ASP ASP          
SEQRES  21 A  490  PRO PHE GLU ILE ILE ALA ARG GLY GLU TYR VAL LEU GLU          
SEQRES  22 A  490  THR PHE GLY GLU ASN ALA SER HIS VAL ALA LEU LEU VAL          
SEQRES  23 A  490  ASP GLY TYR VAL ALA GLY ALA ALA ALA ILE THR THR ALA          
SEQRES  24 A  490  ARG ARG ARG PHE PRO ASP ASN PHE LEU HIS TYR HIS ARG          
SEQRES  25 A  490  ALA GLY HIS GLY ALA VAL THR SER PRO GLN SER LYS ARG          
SEQRES  26 A  490  GLY TYR THR ALA PHE VAL HIS CYS LYS MET ALA ARG LEU          
SEQRES  27 A  490  GLN GLY ALA SER GLY ILE HIS THR GLY THR MET GLY PHE          
SEQRES  28 A  490  GLY LYS MET GLU GLY GLU SER SER ASP ARG ALA ILE ALA          
SEQRES  29 A  490  TYR MET LEU THR GLN ASP GLU ALA GLN GLY PRO PHE TYR          
SEQRES  30 A  490  ARG GLN SER TRP GLY GLY MET LYS ALA CYS THR PRO ILE          
SEQRES  31 A  490  ILE SER GLY GLY MET ASN ALA LEU ARG MET PRO GLY PHE          
SEQRES  32 A  490  PHE GLU ASN LEU GLY ASN ALA ASN VAL ILE LEU THR ALA          
SEQRES  33 A  490  GLY GLY GLY ALA PHE GLY HIS ILE ASP GLY PRO VAL ALA          
SEQRES  34 A  490  GLY ALA ARG SER LEU ARG GLN ALA TRP GLN ALA TRP ARG          
SEQRES  35 A  490  ASP GLY VAL PRO VAL LEU ASP TYR ALA ARG GLU HIS LYS          
SEQRES  36 A  490  GLU LEU ALA ARG ALA PHE GLU SER PHE PRO GLY ASP ALA          
SEQRES  37 A  490  ASP GLN ILE TYR PRO GLY TRP ARG LYS ALA LEU GLY VAL          
SEQRES  38 A  490  GLU ASP THR ARG SER ALA LEU PRO ALA                          
SEQRES   1 B  490  THR MET ILE THR ASN SER PRO ASP ARG TRP GLY TYR SER          
SEQRES   2 B  490  ALA PRO HIS ARG THR SER ARG GLU SER PRO PRO MET ASP          
SEQRES   3 B  490  GLN SER SER ARG TYR VAL ASN LEU ALA LEU LYS GLU GLU          
SEQRES   4 B  490  ASP LEU ILE ALA GLY GLY GLU HIS VAL LEU CYS ALA TYR          
SEQRES   5 B  490  ILE MET LYS PRO LYS ALA GLY TYR GLY TYR VAL ALA THR          
SEQRES   6 B  490  ALA ALA HIS PHE ALA ALA GLU SER SER THR GLY THR ASN          
SEQRES   7 B  490  VAL GLU VAL CYS THR THR ASP ASP PHE THR ARG GLY VAL          
SEQRES   8 B  490  ASP ALA LEU VAL TYR GLU VAL ASP GLU ALA ARG GLU LEU          
SEQRES   9 B  490  THR LYS ILE ALA TYR PRO VAL ALA LEU PHE ASP ARG ASN          
SEQRES  10 B  490  ILE THR ASP GLY LYS ALA MET ILE ALA SER PHE LEU THR          
SEQRES  11 B  490  LEU THR MET GLY ASN ASN GLN GLY MET GLY ASP VAL GLU          
SEQRES  12 B  490  TYR ALA LYS MET HIS ASP PHE TYR VAL PRO GLU ALA TYR          
SEQRES  13 B  490  ARG ALA LEU PHE ASP GLY PRO SER VAL ASN ILE SER ALA          
SEQRES  14 B  490  LEU TRP LYS VAL LEU GLY ARG PRO GLU VAL ASP GLY GLY          
SEQRES  15 B  490  LEU VAL VAL GLY THR ILE ILE LYS PRO LYS LEU GLY LEU          
SEQRES  16 B  490  ARG PRO LYS PRO PHE ALA GLU ALA CYS HIS ALA PHE TRP          
SEQRES  17 B  490  LEU GLY GLY ASP PHE ILE LYS ASN ASP GLU PRO GLN GLY          
SEQRES  18 B  490  ASN GLN PRO PHE ALA PRO LEU ARG ASP THR ILE ALA LEU          
SEQRES  19 B  490  VAL ALA ASP ALA MET ARG ARG ALA GLN ASP GLU THR GLY          
SEQRES  20 B  490  GLU ALA LYS LEU PHE SER ALA ASN ILE THR ALA ASP ASP          
SEQRES  21 B  490  PRO PHE GLU ILE ILE ALA ARG GLY GLU TYR VAL LEU GLU          
SEQRES  22 B  490  THR PHE GLY GLU ASN ALA SER HIS VAL ALA LEU LEU VAL          
SEQRES  23 B  490  ASP GLY TYR VAL ALA GLY ALA ALA ALA ILE THR THR ALA          
SEQRES  24 B  490  ARG ARG ARG PHE PRO ASP ASN PHE LEU HIS TYR HIS ARG          
SEQRES  25 B  490  ALA GLY HIS GLY ALA VAL THR SER PRO GLN SER LYS ARG          
SEQRES  26 B  490  GLY TYR THR ALA PHE VAL HIS CYS LYS MET ALA ARG LEU          
SEQRES  27 B  490  GLN GLY ALA SER GLY ILE HIS THR GLY THR MET GLY PHE          
SEQRES  28 B  490  GLY LYS MET GLU GLY GLU SER SER ASP ARG ALA ILE ALA          
SEQRES  29 B  490  TYR MET LEU THR GLN ASP GLU ALA GLN GLY PRO PHE TYR          
SEQRES  30 B  490  ARG GLN SER TRP GLY GLY MET LYS ALA CYS THR PRO ILE          
SEQRES  31 B  490  ILE SER GLY GLY MET ASN ALA LEU ARG MET PRO GLY PHE          
SEQRES  32 B  490  PHE GLU ASN LEU GLY ASN ALA ASN VAL ILE LEU THR ALA          
SEQRES  33 B  490  GLY GLY GLY ALA PHE GLY HIS ILE ASP GLY PRO VAL ALA          
SEQRES  34 B  490  GLY ALA ARG SER LEU ARG GLN ALA TRP GLN ALA TRP ARG          
SEQRES  35 B  490  ASP GLY VAL PRO VAL LEU ASP TYR ALA ARG GLU HIS LYS          
SEQRES  36 B  490  GLU LEU ALA ARG ALA PHE GLU SER PHE PRO GLY ASP ALA          
SEQRES  37 B  490  ASP GLN ILE TYR PRO GLY TRP ARG LYS ALA LEU GLY VAL          
SEQRES  38 B  490  GLU ASP THR ARG SER ALA LEU PRO ALA                          
HET     MG  A 500       1                                                       
HET     MG  B 500       1                                                       
HET    FOR  A 501       3                                                       
HET    FOR  B 501       3                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     FOR FORMYL GROUP                                                     
FORMUL   3   MG    2(MG 2+)                                                     
FORMUL   5  FOR    2(C H2 O)                                                    
FORMUL   7  HOH   *714(H2 O)                                                    
HELIX    1 AHA GLU A   14  GLY A   20  1                                   7    
HELIX    2 AHB TYR A   38  SER A   49  1                                  12    
HELIX    3 AHC ILE A  101  MET A  109  1                                   9    
HELIX    4 AHD GLU A  130  ARG A  133  1                                   4    
HELIX    5 AHE SER A  144  LEU A  150  1                                   7    
HELIX    6 AH1 PRO A  173  TRP A  184  1                                  12    
HELIX    7 AH2 LEU A  204  THR A  222  1                                  19    
HELIX    8 AH3 ASP A  235  PHE A  251  1                                  17    
HELIX    9 AH4 ALA A  269  ARG A  278  1                                  10    
HELIX   10 AHF GLY A  292  THR A  295  1                                   4    
HELIX   11 AH5 ALA A  305  GLN A  315  1                                  11    
HELIX   12 AH6 ARG A  337  THR A  344  1                                   8    
HELIX   13 AH7 MET A  376  LEU A  383  1                                   8    
HELIX   14 AH8 PRO A  403  ASP A  419  1                                  17    
HELIX   15 AHG VAL A  423  GLU A  429  1                                   7    
HELIX   16 AHH LYS A  431  PHE A  440  1                                  10    
HELIX   17 AHI GLY A  442  TYR A  448  1                                   7    
HELIX   18 AHJ TRP A  451  LEU A  455  1                                   5    
HELIX   19 AHA GLU B   14  GLY B   20  1                                   7    
HELIX   20 AHB TYR B   38  SER B   49  1                                  12    
HELIX   21 AHC ILE B  101  MET B  109  1                                   9    
HELIX   22 AHD GLU B  130  ARG B  133  1                                   4    
HELIX   23 AHE SER B  144  LEU B  150  1                                   7    
HELIX   24 AH1 PRO B  173  TRP B  184  1                                  12    
HELIX   25 AH2 LEU B  204  THR B  222  1                                  19    
HELIX   26 AH3 ASP B  235  PHE B  251  1                                  17    
HELIX   27 AH4 ALA B  269  ARG B  278  1                                  10    
HELIX   28 AHF GLY B  292  THR B  295  1                                   4    
HELIX   29 AH5 ALA B  305  GLN B  315  1                                  11    
HELIX   30 AH6 ARG B  337  THR B  344  1                                   8    
HELIX   31 AH7 MET B  376  LEU B  383  1                                   8    
HELIX   32 AH8 PRO B  403  ASP B  419  1                                  17    
HELIX   33 AHG VAL B  423  GLU B  429  1                                   7    
HELIX   34 AHH LYS B  431  PHE B  440  1                                  10    
HELIX   35 AHI GLY B  442  TYR B  448  1                                   7    
HELIX   36 AHJ TRP B  451  LEU B  455  1                                   5    
SHEET    1 ANT 5 VAL A   8  LEU A  10  0                                        
SHEET    2 ANT 5 LEU A  70  ASP A  75  1                                        
SHEET    3 ANT 5 GLU A  79  PRO A  86 -1                                        
SHEET    4 ANT 5 HIS A  23  PRO A  32 -1                                        
SHEET    5 ANT 5 ASP A 117  TYR A 127 -1                                        
SHEET    1 ACT 9 VAL A 160  ILE A 164  0                                        
SHEET    2 ACT 9 PHE A 189  LYS A 191  1                                        
SHEET    3 ACT 9 LEU A 227  ASN A 231  1                                        
SHEET    4 ACT 9 VAL A 258  ASP A 263  1                                        
SHEET    5 ACT 9 LEU A 284  HIS A 287  1                                        
SHEET    6 ACT 9 GLY A 319  HIS A 321  1                                        
SHEET    7 ACT 9 THR A 364  GLY A 369  1                                        
SHEET    8 ACT 9 ILE A 389  ALA A 392  1                                        
SHEET    9 ACT 9 VAL A 160  ILE A 164  1                                        
SHEET    1 BNT 5 VAL B   8  LEU B  10  0                                        
SHEET    2 BNT 5 LEU B  70  ASP B  75  1                                        
SHEET    3 BNT 5 GLU B  79  PRO B  86 -1                                        
SHEET    4 BNT 5 HIS B  23  PRO B  32 -1                                        
SHEET    5 BNT 5 ASP B 117  TYR B 127 -1                                        
SHEET    1 BCT 9 VAL B 160  ILE B 164  0                                        
SHEET    2 BCT 9 PHE B 189  LYS B 191  1                                        
SHEET    3 BCT 9 LEU B 227  ASN B 231  1                                        
SHEET    4 BCT 9 VAL B 258  ASP B 263  1                                        
SHEET    5 BCT 9 LEU B 284  HIS B 287  1                                        
SHEET    6 BCT 9 GLY B 319  HIS B 321  1                                        
SHEET    7 BCT 9 THR B 364  GLY B 369  1                                        
SHEET    8 BCT 9 ILE B 389  ALA B 392  1                                        
SHEET    9 BCT 9 VAL B 160  ILE B 164  1                                        
LINK         NZ  LYS A 191                 C   FOR A 501     1555   1555  1.51  
LINK         NZ  LYS B 191                 C   FOR B 501     1555   1555  1.48  
LINK        MG    MG A 500                 O   FOR A 501     1555   1555  2.72  
LINK        MG    MG A 500                 O   HOH A 822     1555   1555  2.67  
LINK        MG    MG A 500                 OD2 ASP A 193     1555   1555  2.83  
LINK        MG    MG B 500                 O   HOH B 875     1555   1555  2.50  
LINK        MG    MG B 500                 ND2 ASN A 111     1555   1555  3.09  
CISPEP   1 LYS A  166    PRO A  167          0         1.27                     
CISPEP   2 LYS B  166    PRO B  167          0         0.31                     
SITE     1 AC1  4 ASP A 193  GLU A 194  FOR A 501  HOH A 822                    
SITE     1 AC2  5 ASN A 111  ASP B 193  GLU B 194  FOR B 501                    
SITE     2 AC2  5 HOH B 875                                                     
SITE     1 AC3  4 ILE A 164  LYS A 191  ASP A 193   MG A 500                    
SITE     1 AC4  4 ILE B 164  LYS B 191   MG B 500  HOH B 632                    
CRYST1   65.500   70.600  104.100  90.00  92.10  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.036668        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000672        0.00000                         
SCALE1      0.015267  0.000000  0.000560        0.00000                         
SCALE2      0.000000  0.014164  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009613        0.00000                         
MTRIX1   1  0.373740 -0.056207  0.940855        6.14161    1                    
MTRIX2   1 -0.073400 -0.996800 -0.033512       17.87800    1                    
MTRIX3   1  0.909789 -0.054363 -0.376740       -7.57091    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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