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Database: PDB
Entry: 1P22
LinkDB: 1P22
Original site: 1P22 
HEADER    SIGNALING PROTEIN                       14-APR-03   1P22              
TITLE     STRUCTURE OF A BETA-TRCP1-SKP1-BETA-CATENIN COMPLEX:                  
TITLE    2 DESTRUCTION MOTIF BINDING AND LYSINE SPECIFICITY ON THE              
TITLE    3 SCFBETA-TRCP1 UBIQUITIN LIGASE                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: F-BOX/WD-REPEAT PROTEIN 1A;                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: F-BOX AND WD-REPEATS PROTEIN BETA-TRCP,                     
COMPND   5 E3RSIKAPPAB, PIKAPPABALPHA-E3 RECEPTOR SUBUNIT;                      
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: SKP1;                                                      
COMPND   9 CHAIN: B;                                                            
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: BETA-CATENIN;                                              
COMPND  13 CHAIN: C;                                                            
COMPND  14 SYNONYM: PRO2286;                                                    
COMPND  15 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: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  15 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  17 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  19 MOL_ID: 3;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  21 ORGANISM_COMMON: HUMAN;                                              
SOURCE  22 ORGANISM_TAXID: 9606;                                                
SOURCE  23 GENE: CTNNB1 OR CTNNB;                                               
SOURCE  24 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  25 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  26 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  27 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE  28 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    UBIQUITINATION, DEGRADATION, SIGNALING PROTEIN                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.WU,G.XU,B.A.SCHULMAN,P.D.JEFFREY,J.W.HARPER,N.P.PAVLETICH           
REVDAT   2   24-FEB-09 1P22    1       VERSN                                    
REVDAT   1   08-JUL-03 1P22    0                                                
JRNL        AUTH   G.WU,G.XU,B.A.SCHULMAN,P.D.JEFFREY,J.W.HARPER,               
JRNL        AUTH 2 N.P.PAVLETICH                                                
JRNL        TITL   STRUCTURE OF A BETA-TRCP1-SKP1-BETA-CATENIN                  
JRNL        TITL 2 COMPLEX: DESTRUCTION MOTIF BINDING AND LYSINE                
JRNL        TITL 3 SPECIFICITY OF THE SCFBETA-TRCP1 UBIQUITIN LIGASE            
JRNL        REF    MOL.CELL                      V.  11  1445 2003              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   12820959                                                     
JRNL        DOI    10.1016/S1097-2765(03)00234-X                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1                                           
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ENGH & HUBER                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 16793                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.233                           
REMARK   3   R VALUE            (WORKING SET) : 0.230                           
REMARK   3   FREE R VALUE                     : 0.286                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 840                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE SET COUNT          : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4340                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : NULL                          
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : NULL                          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  NULL ;  NULL ;  NULL       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : NULL                                          
REMARK   3   ION PROBE RADIUS   : NULL                                          
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1P22 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-APR-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB018915.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-DEC-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 103.0                              
REMARK 200  PH                             : 6.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : F1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9500                             
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17628                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.04000                            
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) : 2.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.02                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: DM                                                    
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.23                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.17                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000, SODIUM CITRATE, BIS-TRIS        
REMARK 280  PROPANE, PH 6.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE         
REMARK 280  298.0K                                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31                             
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                                                                      
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       37.16667            
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       74.33333            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4500 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24770 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
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     LYS A   218                                                      
REMARK 465     ASN A   219                                                      
REMARK 465     LYS A   220                                                      
REMARK 465     PRO A   221                                                      
REMARK 465     PRO A   222                                                      
REMARK 465     ASP A   223                                                      
REMARK 465     GLY A   224                                                      
REMARK 465     ASN A   225                                                      
REMARK 465     ALA A   226                                                      
REMARK 465     PHE A   546                                                      
REMARK 465     LEU A   547                                                      
REMARK 465     ASN A   548                                                      
REMARK 465     ASP A   549                                                      
REMARK 465     PRO A   550                                                      
REMARK 465     ALA A   551                                                      
REMARK 465     ALA A   552                                                      
REMARK 465     GLN A   553                                                      
REMARK 465     ALA A   554                                                      
REMARK 465     GLU A   555                                                      
REMARK 465     PRO A   556                                                      
REMARK 465     PRO A   557                                                      
REMARK 465     ARG A   558                                                      
REMARK 465     SER A   559                                                      
REMARK 465     PRO A   560                                                      
REMARK 465     SER A   561                                                      
REMARK 465     ARG A   562                                                      
REMARK 465     THR A   563                                                      
REMARK 465     TYR A   564                                                      
REMARK 465     THR A   565                                                      
REMARK 465     TYR A   566                                                      
REMARK 465     ILE A   567                                                      
REMARK 465     SER A   568                                                      
REMARK 465     ARG A   569                                                      
REMARK 465     MET B     1                                                      
REMARK 465     LYS B    59A                                                     
REMARK 465     ASP B    59B                                                     
REMARK 465     ASP B    59C                                                     
REMARK 465     PRO B    59D                                                     
REMARK 465     PRO B    59E                                                     
REMARK 465     ASP B    59F                                                     
REMARK 465     ASP B    59G                                                     
REMARK 465     GLN B   137                                                      
REMARK 465     TRP B   138                                                      
REMARK 465     CYS B   139                                                      
REMARK 465     GLU B   140                                                      
REMARK 465     GLU B   141                                                      
REMARK 465     LYS B   142                                                      
REMARK 465     LYS C    19                                                      
REMARK 465     ALA C    20                                                      
REMARK 465     ALA C    21                                                      
REMARK 465     VAL C    22                                                      
REMARK 465     SER C    23                                                      
REMARK 465     HIS C    24                                                      
REMARK 465     TRP C    25                                                      
REMARK 465     GLN C    26                                                      
REMARK 465     GLN C    27                                                      
REMARK 465     GLN C    28                                                      
REMARK 465     SER C    29                                                      
REMARK 465     THR C    41                                                      
REMARK 465     THR C    42                                                      
REMARK 465     ALA C    43                                                      
REMARK 465     PRO C    44                                                      
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     SER A 135    OG                                                  
REMARK 470     PRO A 136    CG   CD                                             
REMARK 470     ILE A 138    CG1  CG2  CD1                                       
REMARK 470     PRO B   2    CG   CD                                             
REMARK 470     TYR C  30    CG   CD1  CD2  CE1  CE2  CZ   OH                    
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    PRO A 136   N   -  CA  -  CB  ANGL. DEV. =   7.4 DEGREES          
REMARK 500    LEU A 140   CA  -  CB  -  CG  ANGL. DEV. =  17.7 DEGREES          
REMARK 500    ASP A 200   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP A 286   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP A 373   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP A 409   CB  -  CG  -  OD2 ANGL. DEV. =   7.2 DEGREES          
REMARK 500    LEU A 472   CA  -  CB  -  CG  ANGL. DEV. =  18.3 DEGREES          
REMARK 500    PHE A 478   CB  -  CA  -  C   ANGL. DEV. = -14.2 DEGREES          
REMARK 500    ASP A 528   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    PRO B   2   N   -  CA  -  CB  ANGL. DEV. =   7.7 DEGREES          
REMARK 500    ASP B  37   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP B  75   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 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 137       58.15   -161.40                                   
REMARK 500    ILE A 138       43.99   -157.62                                   
REMARK 500    MET A 139      175.30     69.79                                   
REMARK 500    LEU A 140       -5.51    -57.20                                   
REMARK 500    GLN A 141      -73.40    -29.34                                   
REMARK 500    LEU A 153       79.17   -108.26                                   
REMARK 500    SER A 168      -37.64    156.11                                   
REMARK 500    MET A 187       60.91     29.05                                   
REMARK 500    LYS A 190      -62.58    -29.70                                   
REMARK 500    ARG A 198       -5.28    -54.74                                   
REMARK 500    THR A 199      -98.35   -135.03                                   
REMARK 500    ASP A 200      101.63    -38.07                                   
REMARK 500    SER A 201      -50.60    -19.96                                   
REMARK 500    ARG A 210       78.51     21.23                                   
REMARK 500    TRP A 212      -32.55    -29.73                                   
REMARK 500    ASN A 229      -32.86     98.32                                   
REMARK 500    ASP A 242      -71.38    -58.52                                   
REMARK 500    ILE A 246      -75.86    -57.86                                   
REMARK 500    SER A 248      -89.23    -79.82                                   
REMARK 500    ASN A 249      -13.22    -46.15                                   
REMARK 500    CYS A 252      -44.46   -140.71                                   
REMARK 500    SER A 256      -25.25   -163.72                                   
REMARK 500    LEU A 257      -65.38     51.35                                   
REMARK 500    GLN A 258       79.61     42.88                                   
REMARK 500    ARG A 263     -110.27   -133.81                                   
REMARK 500    SER A 264      171.08     69.05                                   
REMARK 500    GLU A 265     -133.26    -68.82                                   
REMARK 500    THR A 266      -92.56     23.50                                   
REMARK 500    SER A 267     -171.04    -65.80                                   
REMARK 500    LYS A 268       70.44   -173.03                                   
REMARK 500    GLN A 278       13.07   -155.54                                   
REMARK 500    ASN A 287       -3.67    102.55                                   
REMARK 500    ASN A 295      -70.89    -92.21                                   
REMARK 500    TYR A 315     -100.91    -51.77                                   
REMARK 500    ASP A 316      160.64     81.44                                   
REMARK 500    GLU A 317       56.31    -99.61                                   
REMARK 500    ARG A 318      -43.84   -173.46                                   
REMARK 500    THR A 336     -130.06    -85.00                                   
REMARK 500    LEU A 340      -83.15    -90.09                                   
REMARK 500    ILE A 344      -91.08    -75.58                                   
REMARK 500    HIS A 345      -65.24     51.12                                   
REMARK 500    CYS A 347       47.84   -145.28                                   
REMARK 500    GLU A 348      163.69    170.72                                   
REMARK 500    ALA A 349      118.29    -39.80                                   
REMARK 500    PHE A 355      -71.50   -127.31                                   
REMARK 500    ASN A 356      142.92     22.48                                   
REMARK 500    ASN A 357     -150.03     51.39                                   
REMARK 500    ARG A 367       -4.29     83.16                                   
REMARK 500    ASP A 379     -104.98    -92.38                                   
REMARK 500    ILE A 380      110.06     68.84                                   
REMARK 500    PHE A 422      137.56    -36.58                                   
REMARK 500    ASP A 440      -92.19     40.47                                   
REMARK 500    ARG A 464      132.98   -174.63                                   
REMARK 500    PHE A 478     -134.93    -67.02                                   
REMARK 500    ASP A 479      159.72    119.08                                   
REMARK 500    ASP A 489       28.70    -77.62                                   
REMARK 500    ARG A 513      138.13    -24.01                                   
REMARK 500    PHE A 527     -167.23   -123.24                                   
REMARK 500    ASP A 528     -156.45   -162.39                                   
REMARK 500    HIS A 537      -89.22    -45.08                                   
REMARK 500    ASP A 538       99.36    -28.45                                   
REMARK 500    ASP A 539       75.32    -60.83                                   
REMARK 500    SER B   3       88.51    167.79                                   
REMARK 500    SER B   9      -17.04    -49.61                                   
REMARK 500    GLU B  19      -25.74     98.99                                   
REMARK 500    LYS B  22       -4.10    -47.80                                   
REMARK 500    LEU B  31      -58.90   -120.93                                   
REMARK 500    ASP B  33      -56.33   -129.58                                   
REMARK 500    ASP B  37     -115.85    -45.17                                   
REMARK 500    ASN B  45      145.88    -10.68                                   
REMARK 500    HIS B  58       10.59    -56.74                                   
REMARK 500    VAL B  66      -71.77    -99.24                                   
REMARK 500    GLN B  76      -71.04    -16.30                                   
REMARK 500    ALA B  85      -49.65    157.71                                   
REMARK 500    ASP B  90       76.65     27.96                                   
REMARK 500    LYS B 107      152.70    -43.46                                   
REMARK 500    LYS B 109      155.57    -14.32                                   
REMARK 500    THR B 110      120.97     56.68                                   
REMARK 500    LYS B 116      -37.16    -38.80                                   
REMARK 500    ASN B 119     -101.78     87.41                                   
REMARK 500    ILE B 120       86.57     58.67                                   
REMARK 500    LEU C  31     -108.02   -110.57                                   
REMARK 500    ALA C  39     -104.97     72.38                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLN A  274     TYR A  275                 -147.26                    
REMARK 500 ASP A  397     PHE A  398                 -140.84                    
REMARK 500 LEU A  436     GLN A  437                  149.11                    
REMARK 500 VAL B   44     ASN B   45                  148.30                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 999                                                                      
REMARK 999 AN APPROPRIATE SEQUENCE DATABASE REFERENCE                           
REMARK 999 FOR SKP1, CHAIN B, WAS NOT                                           
REMARK 999 AVAILABLE AT THE TIME OF PROCESSING.                                 
DBREF  1P22 A  139   569  UNP    Q9Y297   FBW1A_HUMAN    175    605             
DBREF  1P22 B    2   142  UNP    P63208   SKP1_HUMAN       1    162             
DBREF  1P22 C   19    44  UNP    P35222   CTNB1_HUMAN     19     44             
SEQADV 1P22 SER A  135  UNP  Q9Y297              CLONING ARTIFACT               
SEQADV 1P22 PRO A  136  UNP  Q9Y297              CLONING ARTIFACT               
SEQADV 1P22 ALA A  137  UNP  Q9Y297              CLONING ARTIFACT               
SEQADV 1P22 ILE A  138  UNP  Q9Y297              CLONING ARTIFACT               
SEQADV 1P22 SEP C   33  UNP  P35222    SER    33 MODIFIED RESIDUE               
SEQADV 1P22 SEP C   37  UNP  P35222    SER    37 MODIFIED RESIDUE               
SEQRES   1 A  435  SER PRO ALA ILE MET LEU GLN ARG ASP PHE ILE THR ALA          
SEQRES   2 A  435  LEU PRO ALA ARG GLY LEU ASP HIS ILE ALA GLU ASN ILE          
SEQRES   3 A  435  LEU SER TYR LEU ASP ALA LYS SER LEU CYS ALA ALA GLU          
SEQRES   4 A  435  LEU VAL CYS LYS GLU TRP TYR ARG VAL THR SER ASP GLY          
SEQRES   5 A  435  MET LEU TRP LYS LYS LEU ILE GLU ARG MET VAL ARG THR          
SEQRES   6 A  435  ASP SER LEU TRP ARG GLY LEU ALA GLU ARG ARG GLY TRP          
SEQRES   7 A  435  GLY GLN TYR LEU PHE LYS ASN LYS PRO PRO ASP GLY ASN          
SEQRES   8 A  435  ALA PRO PRO ASN SER PHE TYR ARG ALA LEU TYR PRO LYS          
SEQRES   9 A  435  ILE ILE GLN ASP ILE GLU THR ILE GLU SER ASN TRP ARG          
SEQRES  10 A  435  CYS GLY ARG HIS SER LEU GLN ARG ILE HIS CYS ARG SER          
SEQRES  11 A  435  GLU THR SER LYS GLY VAL TYR CYS LEU GLN TYR ASP ASP          
SEQRES  12 A  435  GLN LYS ILE VAL SER GLY LEU ARG ASP ASN THR ILE LYS          
SEQRES  13 A  435  ILE TRP ASP LYS ASN THR LEU GLU CYS LYS ARG ILE LEU          
SEQRES  14 A  435  THR GLY HIS THR GLY SER VAL LEU CYS LEU GLN TYR ASP          
SEQRES  15 A  435  GLU ARG VAL ILE ILE THR GLY SER SER ASP SER THR VAL          
SEQRES  16 A  435  ARG VAL TRP ASP VAL ASN THR GLY GLU MET LEU ASN THR          
SEQRES  17 A  435  LEU ILE HIS HIS CYS GLU ALA VAL LEU HIS LEU ARG PHE          
SEQRES  18 A  435  ASN ASN GLY MET MET VAL THR CYS SER LYS ASP ARG SER          
SEQRES  19 A  435  ILE ALA VAL TRP ASP MET ALA SER PRO THR ASP ILE THR          
SEQRES  20 A  435  LEU ARG ARG VAL LEU VAL GLY HIS ARG ALA ALA VAL ASN          
SEQRES  21 A  435  VAL VAL ASP PHE ASP ASP LYS TYR ILE VAL SER ALA SER          
SEQRES  22 A  435  GLY ASP ARG THR ILE LYS VAL TRP ASN THR SER THR CYS          
SEQRES  23 A  435  GLU PHE VAL ARG THR LEU ASN GLY HIS LYS ARG GLY ILE          
SEQRES  24 A  435  ALA CYS LEU GLN TYR ARG ASP ARG LEU VAL VAL SER GLY          
SEQRES  25 A  435  SER SER ASP ASN THR ILE ARG LEU TRP ASP ILE GLU CYS          
SEQRES  26 A  435  GLY ALA CYS LEU ARG VAL LEU GLU GLY HIS GLU GLU LEU          
SEQRES  27 A  435  VAL ARG CYS ILE ARG PHE ASP ASN LYS ARG ILE VAL SER          
SEQRES  28 A  435  GLY ALA TYR ASP GLY LYS ILE LYS VAL TRP ASP LEU VAL          
SEQRES  29 A  435  ALA ALA LEU ASP PRO ARG ALA PRO ALA GLY THR LEU CYS          
SEQRES  30 A  435  LEU ARG THR LEU VAL GLU HIS SER GLY ARG VAL PHE ARG          
SEQRES  31 A  435  LEU GLN PHE ASP GLU PHE GLN ILE VAL SER SER SER HIS          
SEQRES  32 A  435  ASP ASP THR ILE LEU ILE TRP ASP PHE LEU ASN ASP PRO          
SEQRES  33 A  435  ALA ALA GLN ALA GLU PRO PRO ARG SER PRO SER ARG THR          
SEQRES  34 A  435  TYR THR TYR ILE SER ARG                                      
SEQRES   1 B  145  MET PRO SER ILE LYS LEU GLN SER SER ASP GLY GLU ILE          
SEQRES   2 B  145  PHE GLU VAL ASP VAL GLU ILE ALA LYS GLN SER VAL THR          
SEQRES   3 B  145  ILE LYS THR MET LEU GLU ASP LEU GLY MET ASP PRO VAL          
SEQRES   4 B  145  PRO LEU PRO ASN VAL ASN ALA ALA ILE LEU LYS LYS VAL          
SEQRES   5 B  145  ILE GLN TRP CYS THR HIS HIS LYS ASP ASP PRO PRO ASP          
SEQRES   6 B  145  ASP ILE PRO VAL TRP ASP GLN GLU PHE LEU LYS VAL ASP          
SEQRES   7 B  145  GLN GLY THR LEU PHE GLU LEU ILE LEU ALA ALA ASN TYR          
SEQRES   8 B  145  LEU ASP ILE LYS GLY LEU LEU ASP VAL THR CYS LYS THR          
SEQRES   9 B  145  VAL ALA ASN MET ILE LYS GLY LYS THR PRO GLU GLU ILE          
SEQRES  10 B  145  ARG LYS THR PHE ASN ILE LYS ASN ASP PHE THR GLU GLU          
SEQRES  11 B  145  GLU GLU ALA GLN VAL ARG LYS GLU ASN GLN TRP CYS GLU          
SEQRES  12 B  145  GLU LYS                                                      
SEQRES   1 C   26  LYS ALA ALA VAL SER HIS TRP GLN GLN GLN SER TYR LEU          
SEQRES   2 C   26  ASP SEP GLY ILE HIS SEP GLY ALA THR THR THR ALA PRO          
MODRES 1P22 SEP C   33  SER  PHOSPHOSERINE                                      
MODRES 1P22 SEP C   37  SER  PHOSPHOSERINE                                      
HET    SEP  C  33      10                                                       
HET    SEP  C  37      10                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETSYN     SEP PHOSPHONOSERINE                                                  
FORMUL   3  SEP    2(C3 H8 N O6 P)                                              
HELIX    1   1 ASP A  143  LEU A  148  1                                   6    
HELIX    2   2 PRO A  149  GLY A  152  5                                   4    
HELIX    3   3 LEU A  153  SER A  162  1                                  10    
HELIX    4   4 ASP A  165  CYS A  176  1                                  12    
HELIX    5   5 CYS A  176  GLY A  186  1                                  11    
HELIX    6   6 MET A  187  ARG A  198  1                                  12    
HELIX    7   7 ASP A  200  ARG A  209  1                                  10    
HELIX    8   8 GLY A  211  LEU A  216  5                                   6    
HELIX    9   9 ASN A  229  TRP A  250  1                                  22    
HELIX   10  10 LEU A  497  LEU A  501  1                                   5    
HELIX   11  11 SER B   24  ASP B   33  1                                  10    
HELIX   12  12 ASN B   45  THR B   57  1                                  13    
HELIX   13  13 VAL B   66  LEU B   72  1                                   7    
HELIX   14  14 ASP B   75  ASN B   87  1                                  13    
HELIX   15  15 ILE B   91  MET B  105  1                                  15    
HELIX   16  16 THR B  110  ASN B  119  1                                  10    
HELIX   17  17 THR B  125  LYS B  134  1                                  10    
SHEET    1   A 4 ILE A 260  HIS A 261  0                                        
SHEET    2   A 4 THR A 540  TRP A 544 -1  O  ILE A 541   N  ILE A 260           
SHEET    3   A 4 ILE A 532  SER A 534 -1  N  SER A 534   O  LEU A 542           
SHEET    4   A 4 LEU A 525  PHE A 527 -1  N  GLN A 526   O  VAL A 533           
SHEET    1   B 4 VAL A 270  GLN A 274  0                                        
SHEET    2   B 4 LYS A 279  LEU A 284 -1  O  VAL A 281   N  GLN A 274           
SHEET    3   B 4 ILE A 289  ASP A 293 -1  O  LYS A 290   N  SER A 282           
SHEET    4   B 4 CYS A 299  LEU A 303 -1  O  LYS A 300   N  ILE A 291           
SHEET    1   C 4 VAL A 310  GLN A 314  0                                        
SHEET    2   C 4 VAL A 319  SER A 324 -1  O  GLY A 323   N  CYS A 312           
SHEET    3   C 4 VAL A 329  ASP A 333 -1  O  TRP A 332   N  ILE A 320           
SHEET    4   C 4 MET A 339  LEU A 343 -1  O  LEU A 343   N  VAL A 329           
SHEET    1   D 4 VAL A 350  ARG A 354  0                                        
SHEET    2   D 4 MET A 359  SER A 364 -1  O  VAL A 361   N  ARG A 354           
SHEET    3   D 4 ILE A 369  ASP A 373 -1  O  TRP A 372   N  MET A 360           
SHEET    4   D 4 THR A 381  LEU A 386 -1  O  ARG A 384   N  VAL A 371           
SHEET    1   E 4 VAL A 393  ASP A 399  0                                        
SHEET    2   E 4 TYR A 402  SER A 407 -1  O  VAL A 404   N  ASP A 397           
SHEET    3   E 4 THR A 411  ASN A 416 -1  O  TRP A 415   N  ILE A 403           
SHEET    4   E 4 PHE A 422  ASN A 427 -1  O  LEU A 426   N  ILE A 412           
SHEET    1   F 4 ILE A 433  ARG A 439  0                                        
SHEET    2   F 4 LEU A 442  SER A 447 -1  O  LEU A 442   N  ARG A 439           
SHEET    3   F 4 ILE A 452  ASP A 456 -1  O  TRP A 455   N  VAL A 443           
SHEET    4   F 4 CYS A 462  LEU A 466 -1  O  LEU A 463   N  LEU A 454           
SHEET    1   G 4 VAL A 473  ARG A 477  0                                        
SHEET    2   G 4 ARG A 482  ALA A 487 -1  O  GLY A 486   N  CYS A 475           
SHEET    3   G 4 ILE A 492  ASP A 496 -1  O  TRP A 495   N  ILE A 483           
SHEET    4   G 4 CYS A 511  LEU A 515 -1  O  LEU A 515   N  ILE A 492           
SHEET    1   H 3 ILE B  13  VAL B  16  0                                        
SHEET    2   H 3 ILE B   4  SER B   8 -1  N  ILE B   4   O  VAL B  16           
SHEET    3   H 3 VAL B  39  LEU B  41  1  O  VAL B  39   N  GLN B   7           
LINK         C   ASP C  32                 N   SEP C  33     1555   1555  1.31  
LINK         C   SEP C  33                 N   GLY C  34     1555   1555  1.33  
LINK         C   HIS C  36                 N   SEP C  37     1555   1555  1.32  
LINK         C   SEP C  37                 N   GLY C  38     1555   1555  1.33  
CRYST1   82.600   82.600  111.500  90.00  90.00 120.00 P 31          3          
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      0.012107  0.006990  0.000000        0.00000                         
SCALE2      0.000000  0.013979  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008969        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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