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Database: PDB
Entry: 2WZ1
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Original site: 2WZ1 
HEADER    LYASE                                   23-NOV-09   2WZ1              
TITLE     STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN SOLUBLE GUANYLATE CYCLASE 1
TITLE    2 BETA 3.                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GUANYLATE CYCLASE SOLUBLE SUBUNIT BETA-1;                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 994-1205;                       
COMPND   5 SYNONYM: GUANYLATE CYCLASE 1 BETA 3, GCS-BETA-1, SOLUBLE GUANYLATE   
COMPND   6 CYCLASE SMALL SUBUNIT, GCS-BETA-3;                                   
COMPND   7 EC: 4.6.1.2;                                                         
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: R3 PRARE2;                                
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PNIC-CTHF                                 
KEYWDS    LYASE, GUCY1, METAL-BINDING, CGMP BIOSYNTHESIS, NUCLEOTIDE-BINDING,   
KEYWDS   2 CYCLASE, GUCY1B3, GTP-BINDING                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.K.ALLERSTON,C.D.O.COOPER,J.MUNIZ,A.C.W.PIKE,F.VON DELFT,            
AUTHOR   2 C.H.ARROWSMITH,J.WEIGELT,A.EDWARDS,C.BOUNTRA,O.GILEADI               
REVDAT   7   08-MAY-19 2WZ1    1       REMARK                                   
REVDAT   6   24-JAN-18 2WZ1    1       JRNL                                     
REVDAT   5   10-APR-13 2WZ1    1       JRNL   REMARK                            
REVDAT   4   13-JUL-11 2WZ1    1       VERSN                                    
REVDAT   3   09-FEB-11 2WZ1    1       REMARK                                   
REVDAT   2   26-JAN-10 2WZ1    1       REMARK                                   
REVDAT   1   01-DEC-09 2WZ1    0                                                
JRNL        AUTH   C.K.ALLERSTON,F.VON DELFT,O.GILEADI                          
JRNL        TITL   CRYSTAL STRUCTURES OF THE CATALYTIC DOMAIN OF HUMAN SOLUBLE  
JRNL        TITL 2 GUANYLATE CYCLASE.                                           
JRNL        REF    PLOS ONE                      V.   8 57644 2013              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   23505436                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0057644                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.63 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0089                                      
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) : 1.63                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 49220                          
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) : 0.185                           
REMARK   3   R VALUE            (WORKING SET) : 0.184                           
REMARK   3   FREE R VALUE                     : 0.219                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2637                            
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) : 1.63                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.67                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3626                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.84                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3020                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 180                          
REMARK   3   BIN FREE R VALUE                    : 0.3710                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3056                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 12                                      
REMARK   3   SOLVENT ATOMS            : 289                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 19.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 12.39                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.07000                                             
REMARK   3    B22 (A**2) : 0.31000                                              
REMARK   3    B33 (A**2) : -0.23000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.095         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.096         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.067         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.370         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.948                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3207 ; 0.016 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  2197 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4331 ; 1.585 ; 1.955       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5374 ; 1.238 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   394 ; 5.849 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   139 ;36.954 ;23.453       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   570 ;14.659 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    22 ;18.831 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   490 ; 0.099 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3506 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   642 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1974 ; 3.742 ; 3.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   805 ; 1.131 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3224 ; 5.452 ; 5.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1233 ; 8.715 ; 8.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1106 ;12.010 ;12.000       
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  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   412        A   610                          
REMARK   3    ORIGIN FOR THE GROUP (A): -37.1526 -10.7107 -13.8246              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0075 T22:   0.0206                                     
REMARK   3      T33:   0.0140 T12:   0.0053                                     
REMARK   3      T13:   0.0012 T23:  -0.0029                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2156 L22:   1.8888                                     
REMARK   3      L33:   2.1282 L12:   0.1997                                     
REMARK   3      L13:   0.4169 L23:   0.1773                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0264 S12:   0.0014 S13:   0.0066                       
REMARK   3      S21:  -0.0235 S22:   0.0086 S23:  -0.1588                       
REMARK   3      S31:   0.0326 S32:   0.1890 S33:  -0.0349                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   412        B   608                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.1851 -19.6296 -19.6586              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0406 T22:   0.0346                                     
REMARK   3      T33:   0.0198 T12:  -0.0176                                     
REMARK   3      T13:   0.0146 T23:   0.0036                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3964 L22:   2.0511                                     
REMARK   3      L33:   2.8682 L12:   0.0686                                     
REMARK   3      L13:  -0.0739 L23:  -0.0572                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0623 S12:  -0.0783 S13:  -0.0786                       
REMARK   3      S21:   0.1698 S22:  -0.0019 S23:   0.1699                       
REMARK   3      S31:   0.1244 S32:  -0.1275 S33:   0.0642                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : 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. ATOM RECORD CONTAINS RESIDUAL B FACTORS ONLY.            
REMARK   4                                                                      
REMARK   4 2WZ1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-NOV-09.                  
REMARK 100 THE DEPOSITION ID IS D_1290041774.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-OCT-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 287                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 49220                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.630                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 37.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.300                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.63                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.67                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.56000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3ET6                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.45                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CONCENTRATED TO 12 MG/ML     
REMARK 280  IN PURIFICATION BUFFER (10MM HEPES, 500MM NACL, 5% GLYCEROL, 10%    
REMARK 280  GALACTOSE, 0.5MM TCEP)AND SET UP IN SITTING DROP IN A 1:2 RATIO     
REMARK 280  WITH HAMPTON INDEX SCREEN - B8 (1.4M TRI-SODIUM CITRATE             
REMARK 280  DIHYDRATE, 0.1M HEPES, PH 7.5)., VAPOR DIFFUSION, SITTING DROP      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       70.01500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       70.01500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       32.79500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       45.19000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       32.79500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       45.19000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       70.01500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       32.79500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       45.19000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       70.01500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       32.79500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       45.19000            
REMARK 290   SMTRY3   8  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: 3370 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18100 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.7 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 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     HIS A   408                                                      
REMARK 465     LYS A   409                                                      
REMARK 465     ARG A   410                                                      
REMARK 465     PRO A   411                                                      
REMARK 465     GLY A   440                                                      
REMARK 465     GLU A   441                                                      
REMARK 465     THR A   611                                                      
REMARK 465     GLU A   612                                                      
REMARK 465     GLU A   613                                                      
REMARK 465     THR A   614                                                      
REMARK 465     LYS A   615                                                      
REMARK 465     GLN A   616                                                      
REMARK 465     ASP A   617                                                      
REMARK 465     ASP A   618                                                      
REMARK 465     ASP A   619                                                      
REMARK 465     ALA A   620                                                      
REMARK 465     GLU A   621                                                      
REMARK 465     ASN A   622                                                      
REMARK 465     LEU A   623                                                      
REMARK 465     TYR A   624                                                      
REMARK 465     PHE A   625                                                      
REMARK 465     GLN A   626                                                      
REMARK 465     HIS B   408                                                      
REMARK 465     LYS B   409                                                      
REMARK 465     ARG B   410                                                      
REMARK 465     PRO B   411                                                      
REMARK 465     GLY B   440                                                      
REMARK 465     THR B   609                                                      
REMARK 465     GLY B   610                                                      
REMARK 465     THR B   611                                                      
REMARK 465     GLU B   612                                                      
REMARK 465     GLU B   613                                                      
REMARK 465     THR B   614                                                      
REMARK 465     LYS B   615                                                      
REMARK 465     GLN B   616                                                      
REMARK 465     ASP B   617                                                      
REMARK 465     ASP B   618                                                      
REMARK 465     ASP B   619                                                      
REMARK 465     ALA B   620                                                      
REMARK 465     GLU B   621                                                      
REMARK 465     ASN B   622                                                      
REMARK 465     LEU B   623                                                      
REMARK 465     TYR B   624                                                      
REMARK 465     PHE B   625                                                      
REMARK 465     GLN B   626                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 415    CE   NZ                                             
REMARK 470     VAL B 412    CG1  CG2                                            
REMARK 470     LYS B 436    CD   CE   NZ                                        
REMARK 470     GLU B 441    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 515    CG   CD   OE1  OE2                                  
REMARK 470     MET B 537    SD   CE                                             
REMARK 470     LYS B 593    CD   CE   NZ                                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG   SER A   574     O    HOH A  2110              2.03            
REMARK 500   OE1  GLU A   505     O    HOH A  2064              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH B  2098     O    HOH B  2098     3554     1.20            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    CYS A 571   CB    CYS A 571   SG     -0.096                       
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    ARG A 456   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A 494   CB  -  CG  -  CD  ANGL. DEV. =  16.0 DEGREES          
REMARK 500    ARG A 494   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ARG A 494   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG A 494   NE  -  CZ  -  NH2 ANGL. DEV. =   4.7 DEGREES          
REMARK 500    ARG A 494   NE  -  CZ  -  NH2 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG B 587   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    ALA A 438       75.37    -68.88                                   
REMARK 500    HIS A 491       40.57   -103.81                                   
REMARK 500    HIS A 491       40.57   -103.48                                   
REMARK 500    ARG A 587      -60.99    -92.48                                   
REMARK 500    HIS B 437       51.33   -108.27                                   
REMARK 500    ASP B 513       24.86     49.03                                   
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 B2008        DISTANCE =  5.95 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1609                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1611                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1612                
DBREF  2WZ1 A  408   619  UNP    Q02153   GCYB1_HUMAN    994   1205             
DBREF  2WZ1 A  620   626  PDB    2WZ1     2WZ1           620    626             
DBREF  2WZ1 B  408   619  UNP    Q02153   GCYB1_HUMAN    994   1205             
DBREF  2WZ1 B  620   626  PDB    2WZ1     2WZ1           620    626             
SEQRES   1 A  219  HIS LYS ARG PRO VAL PRO ALA LYS ARG TYR ASP ASN VAL          
SEQRES   2 A  219  THR ILE LEU PHE SER GLY ILE VAL GLY PHE ASN ALA PHE          
SEQRES   3 A  219  CYS SER LYS HIS ALA SER GLY GLU GLY ALA MET LYS ILE          
SEQRES   4 A  219  VAL ASN LEU LEU ASN ASP LEU TYR THR ARG PHE ASP THR          
SEQRES   5 A  219  LEU THR ASP SER ARG LYS ASN PRO PHE VAL TYR LYS VAL          
SEQRES   6 A  219  GLU THR VAL GLY ASP LYS TYR MET THR VAL SER GLY LEU          
SEQRES   7 A  219  PRO GLU PRO CYS ILE HIS HIS ALA ARG SER ILE CYS HIS          
SEQRES   8 A  219  LEU ALA LEU ASP MET MET GLU ILE ALA GLY GLN VAL GLN          
SEQRES   9 A  219  VAL ASP GLY GLU SER VAL GLN ILE THR ILE GLY ILE HIS          
SEQRES  10 A  219  THR GLY GLU VAL VAL THR GLY VAL ILE GLY GLN ARG MET          
SEQRES  11 A  219  PRO ARG TYR CYS LEU PHE GLY ASN THR VAL ASN LEU THR          
SEQRES  12 A  219  SER ARG THR GLU THR THR GLY GLU LYS GLY LYS ILE ASN          
SEQRES  13 A  219  VAL SER GLU TYR THR TYR ARG CYS LEU MET SER PRO GLU          
SEQRES  14 A  219  ASN SER ASP PRO GLN PHE HIS LEU GLU HIS ARG GLY PRO          
SEQRES  15 A  219  VAL SER MET LYS GLY LYS LYS GLU PRO MET GLN VAL TRP          
SEQRES  16 A  219  PHE LEU SER ARG LYS ASN THR GLY THR GLU GLU THR LYS          
SEQRES  17 A  219  GLN ASP ASP ASP ALA GLU ASN LEU TYR PHE GLN                  
SEQRES   1 B  219  HIS LYS ARG PRO VAL PRO ALA LYS ARG TYR ASP ASN VAL          
SEQRES   2 B  219  THR ILE LEU PHE SER GLY ILE VAL GLY PHE ASN ALA PHE          
SEQRES   3 B  219  CYS SER LYS HIS ALA SER GLY GLU GLY ALA MET LYS ILE          
SEQRES   4 B  219  VAL ASN LEU LEU ASN ASP LEU TYR THR ARG PHE ASP THR          
SEQRES   5 B  219  LEU THR ASP SER ARG LYS ASN PRO PHE VAL TYR LYS VAL          
SEQRES   6 B  219  GLU THR VAL GLY ASP LYS TYR MET THR VAL SER GLY LEU          
SEQRES   7 B  219  PRO GLU PRO CYS ILE HIS HIS ALA ARG SER ILE CYS HIS          
SEQRES   8 B  219  LEU ALA LEU ASP MET MET GLU ILE ALA GLY GLN VAL GLN          
SEQRES   9 B  219  VAL ASP GLY GLU SER VAL GLN ILE THR ILE GLY ILE HIS          
SEQRES  10 B  219  THR GLY GLU VAL VAL THR GLY VAL ILE GLY GLN ARG MET          
SEQRES  11 B  219  PRO ARG TYR CYS LEU PHE GLY ASN THR VAL ASN LEU THR          
SEQRES  12 B  219  SER ARG THR GLU THR THR GLY GLU LYS GLY LYS ILE ASN          
SEQRES  13 B  219  VAL SER GLU TYR THR TYR ARG CYS LEU MET SER PRO GLU          
SEQRES  14 B  219  ASN SER ASP PRO GLN PHE HIS LEU GLU HIS ARG GLY PRO          
SEQRES  15 B  219  VAL SER MET LYS GLY LYS LYS GLU PRO MET GLN VAL TRP          
SEQRES  16 B  219  PHE LEU SER ARG LYS ASN THR GLY THR GLU GLU THR LYS          
SEQRES  17 B  219  GLN ASP ASP ASP ALA GLU ASN LEU TYR PHE GLN                  
HET    EDO  A1611       4                                                       
HET    EDO  A1612       4                                                       
HET    EDO  B1609       4                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  EDO    3(C2 H6 O2)                                                  
FORMUL   6  HOH   *289(H2 O)                                                    
HELIX    1   1 GLY A  429  HIS A  437  1                                   9    
HELIX    2   2 GLY A  442  ASP A  462  1                                  21    
HELIX    3   3 HIS A  491  GLY A  508  1                                  18    
HELIX    4   4 GLY A  544  THR A  556  1                                  13    
HELIX    5   5 GLU A  566  LEU A  572  1                                   7    
HELIX    6   6 GLY B  429  SER B  435  1                                   7    
HELIX    7   7 GLU B  441  ASP B  462  1                                  22    
HELIX    8   8 HIS B  491  VAL B  510  1                                  20    
HELIX    9   9 GLY B  544  THR B  556  1                                  13    
HELIX   10  10 GLU B  566  MET B  573  1                                   8    
SHEET    1  AA 5 TYR A 470  VAL A 472  0                                        
SHEET    2  AA 5 TYR A 479  SER A 483 -1  O  MET A 480   N  VAL A 472           
SHEET    3  AA 5 LYS A 415  ILE A 427 -1  O  THR A 421   N  SER A 483           
SHEET    4  AA 5 ILE A 519  ILE A 533 -1  O  THR A 520   N  GLY A 426           
SHEET    5  AA 5 ARG A 539  PHE A 543  1  O  ARG A 539   N  ILE A 533           
SHEET    1  AB 7 TYR A 470  VAL A 472  0                                        
SHEET    2  AB 7 TYR A 479  SER A 483 -1  O  MET A 480   N  VAL A 472           
SHEET    3  AB 7 LYS A 415  ILE A 427 -1  O  THR A 421   N  SER A 483           
SHEET    4  AB 7 ILE A 519  ILE A 533 -1  O  THR A 520   N  GLY A 426           
SHEET    5  AB 7 ILE A 562  SER A 565  1  O  ASN A 563   N  ILE A 523           
SHEET    6  AB 7 MET A 599  ARG A 606 -1  O  TRP A 602   N  VAL A 564           
SHEET    7  AB 7 PHE A 582  VAL A 590 -1  O  HIS A 583   N  SER A 605           
SHEET    1  AC 2 ARG A 539  PHE A 543  0                                        
SHEET    2  AC 2 ILE A 519  ILE A 533  1  O  VAL A 529   N  PHE A 543           
SHEET    1  AD 2 GLN A 511  VAL A 512  0                                        
SHEET    2  AD 2 GLU A 515  SER A 516 -1  O  GLU A 515   N  VAL A 512           
SHEET    1  BA 5 TYR B 470  VAL B 472  0                                        
SHEET    2  BA 5 TYR B 479  SER B 483 -1  O  MET B 480   N  VAL B 472           
SHEET    3  BA 5 LYS B 415  ILE B 427 -1  O  THR B 421   N  SER B 483           
SHEET    4  BA 5 ILE B 519  ILE B 533 -1  O  THR B 520   N  GLY B 426           
SHEET    5  BA 5 ARG B 539  PHE B 543  1  O  ARG B 539   N  ILE B 533           
SHEET    1  BB 7 TYR B 470  VAL B 472  0                                        
SHEET    2  BB 7 TYR B 479  SER B 483 -1  O  MET B 480   N  VAL B 472           
SHEET    3  BB 7 LYS B 415  ILE B 427 -1  O  THR B 421   N  SER B 483           
SHEET    4  BB 7 ILE B 519  ILE B 533 -1  O  THR B 520   N  GLY B 426           
SHEET    5  BB 7 ILE B 562  SER B 565  1  O  ASN B 563   N  ILE B 523           
SHEET    6  BB 7 MET B 599  ARG B 606 -1  O  TRP B 602   N  VAL B 564           
SHEET    7  BB 7 PHE B 582  VAL B 590 -1  O  HIS B 583   N  SER B 605           
SHEET    1  BC 2 ARG B 539  PHE B 543  0                                        
SHEET    2  BC 2 ILE B 519  ILE B 533  1  O  VAL B 529   N  PHE B 543           
SHEET    1  BD 2 GLN B 511  VAL B 512  0                                        
SHEET    2  BD 2 GLU B 515  SER B 516 -1  O  GLU B 515   N  VAL B 512           
CISPEP   1 LEU A  485    PRO A  486          0        -3.51                     
CISPEP   2 LEU B  485    PRO B  486          0         1.48                     
SITE     1 AC1  5 PHE B 468  GLY B 484  LEU B 485  PRO B 486                    
SITE     2 AC1  5 GLU B 487                                                     
SITE     1 AC2  4 PHE A 468  ARG A 494  SER A 495  HOH A2056                    
SITE     1 AC3  6 VAL A 428  GLY A 429  PHE A 430  PHE A 433                    
SITE     2 AC3  6 VAL A 517  HOH A2162                                          
CRYST1   65.590   90.380  140.030  90.00  90.00  90.00 C 2 2 21     16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015246  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011064  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007141        0.00000                         
MTRIX1   1 -0.946550 -0.088780  0.310100      -44.16552    1                    
MTRIX2   1  0.009400 -0.968570 -0.248580      -33.16879    1                    
MTRIX3   1  0.322430 -0.232380  0.917630        2.54190    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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