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Database: PDB
Entry: 2RJQ
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Original site: 2RJQ 
HEADER    HYDROLASE                               15-OCT-07   2RJQ              
TITLE     CRYSTAL STRUCTURE OF ADAMTS5 WITH INHIBITOR BOUND                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ADAMTS-5;                                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 262-628;                                          
COMPND   5 SYNONYM: A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN     
COMPND   6 MOTIFS 5, ADAM-TS 5, ADAM-TS5, AGGRECANASE-2, ADMP-2, ADAM-TS 11;    
COMPND   7 EC: 3.4.24.-;                                                        
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 GENE: ADAMTS5, ADAMTS11, ADMP2;                                      
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: OVARY (CHO) CELLS                       
KEYWDS    METALLOPROTEASE DOMAIN, AGGRECANASE, CLEAVAGE ON PAIR OF BASIC        
KEYWDS   2 RESIDUES, EXTRACELLULAR MATRIX, GLYCOPROTEIN, HYDROLASE, METAL-      
KEYWDS   3 BINDING, SECRETED, ZYMOGEN                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.MOSYAK,M.STAHL,W.SOMERS                                             
REVDAT   5   25-OCT-17 2RJQ    1       REMARK                                   
REVDAT   4   13-JUL-11 2RJQ    1       VERSN                                    
REVDAT   3   24-FEB-09 2RJQ    1       VERSN                                    
REVDAT   2   08-JAN-08 2RJQ    1       JRNL                                     
REVDAT   1   11-DEC-07 2RJQ    0                                                
JRNL        AUTH   L.MOSYAK,K.GEORGIADIS,T.SHANE,K.SVENSON,T.HEBERT,T.MCDONAGH, 
JRNL        AUTH 2 S.MACKIE,S.OLLAND,L.LIN,X.ZHONG,R.KRIZ,E.L.REIFENBERG,       
JRNL        AUTH 3 L.A.COLLINS-RACIE,C.CORCORAN,B.FREEMAN,R.ZOLLNER,T.MARVELL,  
JRNL        AUTH 4 M.VERA,P.E.SUM,E.R.LAVALLIE,M.STAHL,W.SOMERS                 
JRNL        TITL   CRYSTAL STRUCTURES OF THE TWO MAJOR AGGRECAN DEGRADING       
JRNL        TITL 2 ENZYMES, ADAMTS4 AND ADAMTS5.                                
JRNL        REF    PROTEIN SCI.                  V.  17    16 2008              
JRNL        REFN                   ISSN 0961-8368                               
JRNL        PMID   18042673                                                     
JRNL        DOI    10.1110/PS.073287008                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 87.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 13609                          
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) : 0.231                           
REMARK   3   R VALUE            (WORKING SET) : 0.230                           
REMARK   3   FREE R VALUE                     : 0.260                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 683                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.67                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 434                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 39.34                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3390                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 18                           
REMARK   3   BIN FREE R VALUE                    : 0.2870                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2236                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 66                                      
REMARK   3   SOLVENT ATOMS            : 81                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 62.82                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.85000                                              
REMARK   3    B22 (A**2) : 3.85000                                              
REMARK   3    B33 (A**2) : -5.78000                                             
REMARK   3    B12 (A**2) : 1.93000                                              
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): 0.533         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.309         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.267         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 22.759        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.936                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.916                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2349 ; 0.006 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3186 ; 0.899 ; 1.985       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   291 ; 4.802 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   100 ;34.603 ;24.400       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   394 ;14.736 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;15.061 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   361 ; 0.056 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1744 ; 0.002 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   979 ; 0.167 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1558 ; 0.290 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    83 ; 0.129 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):    12 ; 0.116 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    41 ; 0.150 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     9 ; 0.130 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):     1 ; 0.039 ; 0.200       
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):  1486 ; 0.198 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2321 ; 0.380 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   953 ; 0.549 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   865 ; 1.038 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 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   264        A   485                          
REMARK   3    ORIGIN FOR THE GROUP (A): -43.2050 -14.5299  15.0999              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0633 T22:  -0.2603                                     
REMARK   3      T33:  -0.1667 T12:   0.1116                                     
REMARK   3      T13:   0.1140 T23:   0.0398                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.3094 L22:   5.3404                                     
REMARK   3      L33:   6.3778 L12:  -1.3582                                     
REMARK   3      L13:  -0.9123 L23:   0.6910                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3293 S12:   0.3399 S13:   0.7812                       
REMARK   3      S21:  -0.1339 S22:  -0.0200 S23:  -0.2070                       
REMARK   3      S31:  -0.7394 S32:  -0.2715 S33:  -0.3093                       
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 :   A   486        A   555                          
REMARK   3    ORIGIN FOR THE GROUP (A): -19.1383 -15.9099   8.0791              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1431 T22:   0.0178                                     
REMARK   3      T33:   0.4197 T12:  -0.0331                                     
REMARK   3      T13:   0.1112 T23:   0.0008                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.8705 L22:   3.1423                                     
REMARK   3      L33:  11.0450 L12:  -1.4137                                     
REMARK   3      L13:  -5.6126 L23:   3.1291                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4895 S12:   0.2798 S13:   1.7469                       
REMARK   3      S21:  -0.4582 S22:   0.3132 S23:  -0.7536                       
REMARK   3      S31:  -0.9428 S32:   0.6015 S33:  -0.8028                       
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. ALTHOUGH THE AMINO ACID SEQUENCE OF THE CRYSTALLIZED     
REMARK   3  PROTEIN ENCOMPASSES THREE DOMAINS: CATALYTIC, DISINTEGRIN-LIKE      
REMARK   3  DOMAIN AND THROMBOSPONDIN-LIKE DOMAIN, THE LATTER DOMAIN,           
REMARK   3  RESIDUES 557-628, HAS NO SUPPORTING ELECTRON DENSITY.               
REMARK   4                                                                      
REMARK   4 2RJQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-OCT-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000044942.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-OCT-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00000                            
REMARK 200  MONOCHROMATOR                  : SI 220, ROSENBAUM-ROCK DOUBLE      
REMARK 200                                   -CRYSTAL                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13624                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
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) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.50                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.29000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2RJP                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.35                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 8000, 0.2 M AMMONIUM SULFATE,    
REMARK 280  0.1M MES PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       31.16233            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       62.32467            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       62.32467            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       31.16233            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     SER A   262                                                      
REMARK 465     ILE A   263                                                      
REMARK 465     LYS A   556                                                      
REMARK 465     THR A   557                                                      
REMARK 465     LYS A   558                                                      
REMARK 465     LYS A   559                                                      
REMARK 465     LYS A   560                                                      
REMARK 465     TYR A   561                                                      
REMARK 465     TYR A   562                                                      
REMARK 465     SER A   563                                                      
REMARK 465     THR A   564                                                      
REMARK 465     SER A   565                                                      
REMARK 465     SER A   566                                                      
REMARK 465     HIS A   567                                                      
REMARK 465     GLY A   568                                                      
REMARK 465     ASN A   569                                                      
REMARK 465     TRP A   570                                                      
REMARK 465     GLY A   571                                                      
REMARK 465     SER A   572                                                      
REMARK 465     TRP A   573                                                      
REMARK 465     GLY A   574                                                      
REMARK 465     SER A   575                                                      
REMARK 465     TRP A   576                                                      
REMARK 465     GLY A   577                                                      
REMARK 465     GLN A   578                                                      
REMARK 465     CYS A   579                                                      
REMARK 465     SER A   580                                                      
REMARK 465     ARG A   581                                                      
REMARK 465     SER A   582                                                      
REMARK 465     CYS A   583                                                      
REMARK 465     GLY A   584                                                      
REMARK 465     GLY A   585                                                      
REMARK 465     GLY A   586                                                      
REMARK 465     VAL A   587                                                      
REMARK 465     GLN A   588                                                      
REMARK 465     PHE A   589                                                      
REMARK 465     ALA A   590                                                      
REMARK 465     TYR A   591                                                      
REMARK 465     ARG A   592                                                      
REMARK 465     HIS A   593                                                      
REMARK 465     CYS A   594                                                      
REMARK 465     ASN A   595                                                      
REMARK 465     ASN A   596                                                      
REMARK 465     PRO A   597                                                      
REMARK 465     ALA A   598                                                      
REMARK 465     PRO A   599                                                      
REMARK 465     ARG A   600                                                      
REMARK 465     ASN A   601                                                      
REMARK 465     ASN A   602                                                      
REMARK 465     GLY A   603                                                      
REMARK 465     ARG A   604                                                      
REMARK 465     TYR A   605                                                      
REMARK 465     CYS A   606                                                      
REMARK 465     THR A   607                                                      
REMARK 465     GLY A   608                                                      
REMARK 465     LYS A   609                                                      
REMARK 465     ARG A   610                                                      
REMARK 465     ALA A   611                                                      
REMARK 465     ILE A   612                                                      
REMARK 465     TYR A   613                                                      
REMARK 465     ARG A   614                                                      
REMARK 465     SER A   615                                                      
REMARK 465     CYS A   616                                                      
REMARK 465     SER A   617                                                      
REMARK 465     LEU A   618                                                      
REMARK 465     MET A   619                                                      
REMARK 465     PRO A   620                                                      
REMARK 465     CYS A   621                                                      
REMARK 465     PRO A   622                                                      
REMARK 465     PRO A   623                                                      
REMARK 465     ASN A   624                                                      
REMARK 465     GLY A   625                                                      
REMARK 465     LYS A   626                                                      
REMARK 465     SER A   627                                                      
REMARK 465     PHE A   628                                                      
REMARK 465     GLY A   629                                                      
REMARK 465     SER A   630                                                      
REMARK 465     ALA A   631                                                      
REMARK 465     TRP A   632                                                      
REMARK 465     SER A   633                                                      
REMARK 465     HIS A   634                                                      
REMARK 465     PRO A   635                                                      
REMARK 465     GLN A   636                                                      
REMARK 465     PHE A   637                                                      
REMARK 465     GLU A   638                                                      
REMARK 465     LYS A   639                                                      
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    ARG A 285       47.89   -150.09                                   
REMARK 500    GLN A 350       51.78    -91.13                                   
REMARK 500    ASP A 354       63.58   -104.35                                   
REMARK 500    ARG A 437     -163.94   -126.72                                   
REMARK 500    GLU A 484       45.03    -84.82                                   
REMARK 500    GLN A 524     -115.97     49.97                                   
REMARK 500    GLN A 550      -22.68     67.70                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A   5  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 270   OE2                                                    
REMARK 620 2 ASP A 360   OD1  87.2                                              
REMARK 620 3 CYS A 471   O   140.1  83.8                                        
REMARK 620 4 ASP A 474   OD1  69.8 157.0 113.9                                  
REMARK 620 5 HOH A 578   O    66.7  98.7  76.4  73.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A   6  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 369   OD1                                                    
REMARK 620 2 LEU A 370   O    88.7                                              
REMARK 620 3 CYS A 376   O    91.9  91.2                                        
REMARK 620 4 THR A 378   O   172.6  90.6  95.4                                  
REMARK 620 5 GLU A 398   OE1  79.2  94.9 169.1  93.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A   1  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 410   NE2                                                    
REMARK 620 2 HIS A 414   NE2  98.5                                              
REMARK 620 3 HIS A 420   NE2 110.5 106.3                                        
REMARK 620 4 BAT A 559   O1   98.8 159.8  77.1                                  
REMARK 620 5 BAT A 559   O2   99.2  85.4 145.6  81.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 557                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 558                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 2                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 3                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 4                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 5                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 6                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BAT A 559                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2RJP   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ADAMTS4 WITH INHIBITOR BOUND                    
REMARK 900 RELATED ID: 3B2Z   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ADAMTS4 (APO FORM)                              
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE CONSTRUCT THAT WAS CRYSTALLIZED ENCODES                          
REMARK 999 RESIDUES 262-628 OF HUMAN ADAMTS-5 PLUS A                            
REMARK 999 C-TERMINAL STREP-TAG (SEQUENCE: GSAWSHPQFEK).                        
DBREF  2RJQ A  262   628  UNP    Q9UNA0   ATS5_HUMAN     262    628             
SEQADV 2RJQ GLY A  629  UNP  Q9UNA0              EXPRESSION TAG                 
SEQADV 2RJQ SER A  630  UNP  Q9UNA0              EXPRESSION TAG                 
SEQADV 2RJQ ALA A  631  UNP  Q9UNA0              EXPRESSION TAG                 
SEQADV 2RJQ TRP A  632  UNP  Q9UNA0              EXPRESSION TAG                 
SEQADV 2RJQ SER A  633  UNP  Q9UNA0              EXPRESSION TAG                 
SEQADV 2RJQ HIS A  634  UNP  Q9UNA0              EXPRESSION TAG                 
SEQADV 2RJQ PRO A  635  UNP  Q9UNA0              EXPRESSION TAG                 
SEQADV 2RJQ GLN A  636  UNP  Q9UNA0              EXPRESSION TAG                 
SEQADV 2RJQ PHE A  637  UNP  Q9UNA0              EXPRESSION TAG                 
SEQADV 2RJQ GLU A  638  UNP  Q9UNA0              EXPRESSION TAG                 
SEQADV 2RJQ LYS A  639  UNP  Q9UNA0              EXPRESSION TAG                 
SEQRES   1 A  378  SER ILE SER ARG ALA ARG GLN VAL GLU LEU LEU LEU VAL          
SEQRES   2 A  378  ALA ASP ALA SER MET ALA ARG LEU TYR GLY ARG GLY LEU          
SEQRES   3 A  378  GLN HIS TYR LEU LEU THR LEU ALA SER ILE ALA ASN ARG          
SEQRES   4 A  378  LEU TYR SER HIS ALA SER ILE GLU ASN HIS ILE ARG LEU          
SEQRES   5 A  378  ALA VAL VAL LYS VAL VAL VAL LEU GLY ASP LYS ASP LYS          
SEQRES   6 A  378  SER LEU GLU VAL SER LYS ASN ALA ALA THR THR LEU LYS          
SEQRES   7 A  378  ASN PHE CYS LYS TRP GLN HIS GLN HIS ASN GLN LEU GLY          
SEQRES   8 A  378  ASP ASP HIS GLU GLU HIS TYR ASP ALA ALA ILE LEU PHE          
SEQRES   9 A  378  THR ARG GLU ASP LEU CYS GLY HIS HIS SER CYS ASP THR          
SEQRES  10 A  378  LEU GLY MET ALA ASP VAL GLY THR ILE CYS SER PRO GLU          
SEQRES  11 A  378  ARG SER CYS ALA VAL ILE GLU ASP ASP GLY LEU HIS ALA          
SEQRES  12 A  378  ALA PHE THR VAL ALA HIS GLU ILE GLY HIS LEU LEU GLY          
SEQRES  13 A  378  LEU SER HIS ASP ASP SER LYS PHE CYS GLU GLU THR PHE          
SEQRES  14 A  378  GLY SER THR GLU ASP LYS ARG LEU MET SER SER ILE LEU          
SEQRES  15 A  378  THR SER ILE ASP ALA SER LYS PRO TRP SER LYS CYS THR          
SEQRES  16 A  378  SER ALA THR ILE THR GLU PHE LEU ASP ASP GLY HIS GLY          
SEQRES  17 A  378  ASN CYS LEU LEU ASP LEU PRO ARG LYS GLN ILE LEU GLY          
SEQRES  18 A  378  PRO GLU GLU LEU PRO GLY GLN THR TYR ASP ALA THR GLN          
SEQRES  19 A  378  GLN CYS ASN LEU THR PHE GLY PRO GLU TYR SER VAL CYS          
SEQRES  20 A  378  PRO GLY MET ASP VAL CYS ALA ARG LEU TRP CYS ALA VAL          
SEQRES  21 A  378  VAL ARG GLN GLY GLN MET VAL CYS LEU THR LYS LYS LEU          
SEQRES  22 A  378  PRO ALA VAL GLU GLY THR PRO CYS GLY LYS GLY ARG ILE          
SEQRES  23 A  378  CYS LEU GLN GLY LYS CYS VAL ASP LYS THR LYS LYS LYS          
SEQRES  24 A  378  TYR TYR SER THR SER SER HIS GLY ASN TRP GLY SER TRP          
SEQRES  25 A  378  GLY SER TRP GLY GLN CYS SER ARG SER CYS GLY GLY GLY          
SEQRES  26 A  378  VAL GLN PHE ALA TYR ARG HIS CYS ASN ASN PRO ALA PRO          
SEQRES  27 A  378  ARG ASN ASN GLY ARG TYR CYS THR GLY LYS ARG ALA ILE          
SEQRES  28 A  378  TYR ARG SER CYS SER LEU MET PRO CYS PRO PRO ASN GLY          
SEQRES  29 A  378  LYS SER PHE GLY SER ALA TRP SER HIS PRO GLN PHE GLU          
SEQRES  30 A  378  LYS                                                          
MODRES 2RJQ ASN A  498  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 557      14                                                       
HET    NAG  A 558      14                                                       
HET     ZN  A   1       1                                                       
HET     ZN  A   2       1                                                       
HET     CL  A   3       1                                                       
HET     CL  A   4       1                                                       
HET     CA  A   5       1                                                       
HET     CA  A   6       1                                                       
HET    BAT  A 559      32                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM      ZN ZINC ION                                                         
HETNAM      CL CHLORIDE ION                                                     
HETNAM      CA CALCIUM ION                                                      
HETNAM     BAT 4-(N-HYDROXYAMINO)-2R-ISOBUTYL-2S-(2-                            
HETNAM   2 BAT  THIENYLTHIOMETHYL)SUCCINYL-L-PHENYLALANINE-N-                   
HETNAM   3 BAT  METHYLAMIDE                                                     
HETSYN     BAT BATIMASTAT; BB94                                                 
FORMUL   2  NAG    2(C8 H15 N O6)                                               
FORMUL   3   ZN    2(ZN 2+)                                                     
FORMUL   5   CL    2(CL 1-)                                                     
FORMUL   7   CA    2(CA 2+)                                                     
FORMUL   9  BAT    C23 H31 N3 O4 S2                                             
FORMUL  10  HOH   *81(H2 O)                                                     
HELIX    1   1 ASP A  276  GLY A  284  1                                   9    
HELIX    2   2 GLY A  286  SER A  303  1                                  18    
HELIX    3   3 HIS A  304  GLU A  308  5                                   5    
HELIX    4   4 ASN A  333  HIS A  348  1                                  16    
HELIX    5   5 SER A  389  ARG A  392  5                                   4    
HELIX    6   6 HIS A  403  LEU A  416  1                                  14    
HELIX    7   7 SER A  423  PHE A  430  1                                   8    
HELIX    8   8 SER A  453  ASP A  466  1                                  14    
HELIX    9   9 GLY A  469  LEU A  473  5                                   5    
HELIX   10  10 LEU A  486  TYR A  491  1                                   6    
HELIX   11  11 ASP A  492  GLY A  502  1                                  11    
SHEET    1   A 5 ILE A 311  VAL A 320  0                                        
SHEET    2   A 5 ARG A 267  ALA A 275  1  N  LEU A 271   O  ALA A 314           
SHEET    3   A 5 ALA A 361  THR A 366  1  O  ILE A 363   N  VAL A 274           
SHEET    4   A 5 CYS A 394  GLU A 398  1  O  ILE A 397   N  LEU A 364           
SHEET    5   A 5 GLY A 380  ALA A 382 -1  N  MET A 381   O  VAL A 396           
SHEET    1   B 3 SER A 506  VAL A 507  0                                        
SHEET    2   B 3 CYS A 519  ARG A 523 -1  O  ALA A 520   N  SER A 506           
SHEET    3   B 3 GLN A 526  LEU A 530 -1  O  LEU A 530   N  CYS A 519           
SHEET    1   C 2 ILE A 547  LEU A 549  0                                        
SHEET    2   C 2 LYS A 552  VAL A 554 -1  O  LYS A 552   N  LEU A 549           
SSBOND   1 CYS A  342    CYS A  394                          1555   1555  2.04  
SSBOND   2 CYS A  371    CYS A  376                          1555   1555  2.05  
SSBOND   3 CYS A  388    CYS A  471                          1555   1555  2.04  
SSBOND   4 CYS A  426    CYS A  455                          1555   1555  2.04  
SSBOND   5 CYS A  497    CYS A  519                          1555   1555  2.04  
SSBOND   6 CYS A  508    CYS A  529                          1555   1555  2.04  
SSBOND   7 CYS A  514    CYS A  548                          1555   1555  2.04  
SSBOND   8 CYS A  542    CYS A  553                          1555   1555  2.04  
LINK         OE2 GLU A 270                CA    CA A   5     1555   1555  2.30  
LINK         OD1 ASP A 360                CA    CA A   5     1555   1555  2.34  
LINK         OD1 ASP A 369                CA    CA A   6     1555   1555  2.32  
LINK         O   LEU A 370                CA    CA A   6     1555   1555  2.43  
LINK         ND1 HIS A 374                ZN    ZN A   2     1555   1555  2.02  
LINK         O   CYS A 376                CA    CA A   6     1555   1555  2.38  
LINK         O   THR A 378                CA    CA A   6     1555   1555  2.38  
LINK         OE1 GLU A 398                CA    CA A   6     1555   1555  2.38  
LINK         NE2 HIS A 410                ZN    ZN A   1     1555   1555  1.99  
LINK         NE2 HIS A 414                ZN    ZN A   1     1555   1555  2.13  
LINK         NE2 HIS A 420                ZN    ZN A   1     1555   1555  2.14  
LINK         O   CYS A 471                CA    CA A   5     1555   1555  2.31  
LINK         OD1 ASP A 474                CA    CA A   5     1555   1555  2.71  
LINK         ND2 ASN A 498                 C1  NAG A 557     1555   1555  1.44  
LINK         O4  NAG A 557                 C1  NAG A 558     1555   1555  1.45  
LINK        ZN    ZN A   1                 O1  BAT A 559     1555   1555  2.14  
LINK        ZN    ZN A   1                 O2  BAT A 559     1555   1555  2.33  
LINK        CA    CA A   5                 O   HOH A 578     1555   1555  2.32  
CISPEP   1 ARG A  285    GLY A  286          0        -6.19                     
SITE     1 AC1  6 LEU A 282  GLN A 495  ASN A 498  LEU A 499                    
SITE     2 AC1  6 NAG A 558  HOH A 612                                          
SITE     1 AC2  4 ARG A 281  LEU A 282  GLY A 284  NAG A 557                    
SITE     1 AC3  4 HIS A 410  HIS A 414  HIS A 420  BAT A 559                    
SITE     1 AC4  4  CL A   3   CL A   4  HIS A 348  HIS A 374                    
SITE     1 AC5  4  ZN A   2  HIS A 348  HIS A 374  BAT A 559                    
SITE     1 AC6  5  ZN A   2  HIS A 348  GLY A 372  HIS A 374                    
SITE     2 AC6  5 SER A 375                                                     
SITE     1 AC7  5 GLU A 270  ASP A 360  CYS A 471  ASP A 474                    
SITE     2 AC7  5 HOH A 578                                                     
SITE     1 AC8  5 ASP A 369  LEU A 370  CYS A 376  THR A 378                    
SITE     2 AC8  5 GLU A 398                                                     
SITE     1 AC9 17  ZN A   1   CL A   3  GLN A 347  HIS A 348                    
SITE     2 AC9 17 ASP A 377  THR A 378  LEU A 379  GLY A 380                    
SITE     3 AC9 17 HIS A 410  GLU A 411  HIS A 414  HIS A 420                    
SITE     4 AC9 17 SER A 440  SER A 441  ILE A 442  LEU A 443                    
SITE     5 AC9 17 HOH A 634                                                     
CRYST1   95.471   95.471   93.487  90.00  90.00 120.00 P 31 2 1      6          
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      0.010474  0.006047  0.000000        0.00000                         
SCALE2      0.000000  0.012095  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010697        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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