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Database: PDB
Entry: 2RD0
LinkDB: 2RD0
Original site: 2RD0 
HEADER    TRANSFERASE/ONCOPROTEIN                 20-SEP-07   2RD0              
TITLE     STRUCTURE OF A HUMAN P110ALPHA/P85ALPHA COMPLEX                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE 3-KINASE CATALYTIC   
COMPND   3 SUBUNIT ALPHA ISOFORM;                                               
COMPND   4 CHAIN: A;                                                            
COMPND   5 SYNONYM: PI3-KINASE P110 SUBUNIT ALPHA, PTDINS-3- KINASE P110, PI3K; 
COMPND   6 EC: 2.7.1.153;                                                       
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: PHOSPHATIDYLINOSITOL 3-KINASE REGULATORY SUBUNIT ALPHA;    
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: UNP RESIDUES 322-600;                                      
COMPND  12 SYNONYM: PI3-KINASE P85 SUBUNIT ALPHA, PTDINS-3-KINASE P85-ALPHA,    
COMPND  13 PI3K;                                                                
COMPND  14 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: PIK3CA;                                                        
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: SF9;                                       
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PFASTBAC HTA;                             
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_COMMON: HUMAN;                                              
SOURCE  15 ORGANISM_TAXID: 9606;                                                
SOURCE  16 GENE: PIK3R1, GRB1;                                                  
SOURCE  17 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  18 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  19 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  20 EXPRESSION_SYSTEM_STRAIN: SF9;                                       
SOURCE  21 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  22 EXPRESSION_SYSTEM_PLASMID: PFASTBAC 1                                
KEYWDS    DISEASE MUTATION, KINASE, ONCOGENE, TRANSFERASE, HOST-VIRUS           
KEYWDS   2 INTERACTION, PHOSPHORYLATION, SH2 DOMAIN, SH3 DOMAIN, TRANSFERASE-   
KEYWDS   3 ONCOPROTEIN COMPLEX                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.HUANG,S.B.GABELLI,L.M.AMZEL                                         
REVDAT   3   13-JUL-11 2RD0    1       VERSN                                    
REVDAT   2   24-FEB-09 2RD0    1       VERSN                                    
REVDAT   1   25-DEC-07 2RD0    0                                                
JRNL        AUTH   C.H.HUANG,D.MANDELKER,O.SCHMIDT-KITTLER,Y.SAMUELS,           
JRNL        AUTH 2 V.E.VELCULESCU,K.W.KINZLER,B.VOGELSTEIN,S.B.GABELLI,         
JRNL        AUTH 3 L.M.AMZEL                                                    
JRNL        TITL   THE STRUCTURE OF A HUMAN P110ALPHA/P85ALPHA COMPLEX          
JRNL        TITL 2 ELUCIDATES THE EFFECTS OF ONCOGENIC PI3KALPHA MUTATIONS.     
JRNL        REF    SCIENCE                       V. 318  1744 2007              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   18079394                                                     
JRNL        DOI    10.1126/SCIENCE.1150799                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.05 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) : 3.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.37                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 38888                          
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) : 0.267                           
REMARK   3   R VALUE            (WORKING SET) : 0.263                           
REMARK   3   FREE R VALUE                     : 0.323                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2000                            
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) : 3.05                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.13                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2177                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 79.26                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3000                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 100                          
REMARK   3   BIN FREE R VALUE                    : 0.3570                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9365                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 80.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 85.66                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.92000                                              
REMARK   3    B22 (A**2) : 2.39000                                              
REMARK   3    B33 (A**2) : -3.32000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.508         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.438         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 24.793        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.913                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.872                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9566 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12902 ; 1.483 ; 1.963       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1127 ; 8.046 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   477 ;39.338 ;24.214       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1806 ;22.696 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    66 ;18.177 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1399 ; 0.108 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7172 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  5035 ; 0.255 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  6415 ; 0.319 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   330 ; 0.183 ; 0.200       
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):    77 ; 0.283 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     3 ; 0.164 ; 0.200       
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):  5813 ; 0.760 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9194 ; 1.429 ; 3.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4232 ; 5.602 ;10.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3708 ; 8.658 ;15.000       
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  : 6                                          
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    20        A   105                          
REMARK   3    ORIGIN FOR THE GROUP (A): 104.0560  67.2930 109.2790              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0349 T22:   0.9607                                     
REMARK   3      T33:  -0.2971 T12:   0.0674                                     
REMARK   3      T13:   0.0515 T23:   0.2937                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.0537 L22:   6.1545                                     
REMARK   3      L33:   3.3064 L12:   1.6080                                     
REMARK   3      L13:  -2.8059 L23:   0.5460                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2329 S12:   0.2569 S13:   0.8415                       
REMARK   3      S21:  -0.4011 S22:  -0.2859 S23:  -0.4547                       
REMARK   3      S31:  -0.1122 S32:   1.8416 S33:   0.0530                       
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   330        A   498                          
REMARK   3    ORIGIN FOR THE GROUP (A):  77.1800  42.3660  70.6760              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7467 T22:   0.6923                                     
REMARK   3      T33:  -0.0392 T12:   0.2426                                     
REMARK   3      T13:  -0.0314 T23:  -0.2845                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1905 L22:   4.2572                                     
REMARK   3      L33:   5.4336 L12:  -0.9911                                     
REMARK   3      L13:   0.2116 L23:  -0.8764                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0799 S12:   0.2287 S13:  -0.8795                       
REMARK   3      S21:   0.3406 S22:   0.0881 S23:  -0.1250                       
REMARK   3      S31:   1.4702 S32:  -0.3750 S33:  -0.1680                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   528        A   572                          
REMARK   3    ORIGIN FOR THE GROUP (A):  49.6360  56.4790  66.7020              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0774 T22:   1.1270                                     
REMARK   3      T33:  -0.2714 T12:   0.0449                                     
REMARK   3      T13:   0.0251 T23:  -0.3602                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  15.0653 L22:   5.1531                                     
REMARK   3      L33:   6.7835 L12:   0.3049                                     
REMARK   3      L13:   1.7831 L23:  -1.7906                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0476 S12:   0.5965 S13:  -0.1387                       
REMARK   3      S21:  -0.2057 S22:   0.1410 S23:   1.2977                       
REMARK   3      S31:   0.3178 S32:  -0.8475 S33:  -0.1886                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   973        A   988                          
REMARK   3    ORIGIN FOR THE GROUP (A):  32.9840  59.9340 101.1750              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0389 T22:   0.6168                                     
REMARK   3      T33:   0.2640 T12:   0.0628                                     
REMARK   3      T13:   0.1595 T23:  -0.0446                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  18.5042 L22:   2.4369                                     
REMARK   3      L33:  25.6494 L12:   5.0092                                     
REMARK   3      L13:  -6.0554 L23:   3.4187                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0059 S12:   1.6950 S13:   1.1938                       
REMARK   3      S21:   0.0793 S22:   0.4453 S23:   1.5653                       
REMARK   3      S31:  -0.3949 S32:  -1.9854 S33:  -0.4512                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  1031        A  1049                          
REMARK   3    ORIGIN FOR THE GROUP (A):  35.6660  49.4120  94.0960              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1409 T22:   0.8644                                     
REMARK   3      T33:   0.4904 T12:  -0.2771                                     
REMARK   3      T13:   0.0645 T23:  -0.3148                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.8958 L22:   3.1032                                     
REMARK   3      L33:  30.4702 L12:  -2.2699                                     
REMARK   3      L13:  17.0017 L23:   0.8150                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6553 S12:  -0.4825 S13:   0.7865                       
REMARK   3      S21:  -0.2680 S22:   0.2425 S23:   0.9453                       
REMARK   3      S31:   1.5071 S32:  -4.1601 S33:   0.4128                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   442        B   600                          
REMARK   3    ORIGIN FOR THE GROUP (A):  84.9680  39.7670  99.0880              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9448 T22:   0.6045                                     
REMARK   3      T33:   0.0160 T12:   0.5635                                     
REMARK   3      T13:   0.0850 T23:   0.1275                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  12.3243 L22:   4.4372                                     
REMARK   3      L33:   2.7320 L12:   5.8747                                     
REMARK   3      L13:   2.6187 L23:   1.5219                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0940 S12:  -0.5446 S13:  -1.0543                       
REMARK   3      S21:  -0.2977 S22:  -0.1208 S23:  -0.1705                       
REMARK   3      S31:   0.8564 S32:   0.0760 S33:   0.0268                       
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                                                           
REMARK   4                                                                      
REMARK   4 2RD0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-NOV-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB044711.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.081                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38994                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.400                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY                : 7.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.16                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.30                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.43300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.08                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM FORMATE, PH 7.0, VAPOR            
REMARK 280  DIFFUSION, TEMPERATURE 293K                                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       57.52900            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       75.79200            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       58.52500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       75.79200            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       57.52900            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       58.52500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3510 ANGSTROM**2                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -28                                                      
REMARK 465     PRO A   -13                                                      
REMARK 465     THR A   -12                                                      
REMARK 465     THR A   -11                                                      
REMARK 465     GLU A   -10                                                      
REMARK 465     ASN A    -9                                                      
REMARK 465     LEU A    -8                                                      
REMARK 465     TYR A    -7                                                      
REMARK 465     PHE A    -6                                                      
REMARK 465     GLN A    -5                                                      
REMARK 465     GLY A    -4                                                      
REMARK 465     ALA A    -3                                                      
REMARK 465     MET A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     PRO A     2                                                      
REMARK 465     PRO A     3                                                      
REMARK 465     ARG A     4                                                      
REMARK 465     PRO A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     SER A     7                                                      
REMARK 465     TYR A   307                                                      
REMARK 465     SER A   308                                                      
REMARK 465     ARG A   309                                                      
REMARK 465     ARG A   310                                                      
REMARK 465     ILE A   311                                                      
REMARK 465     SER A   312                                                      
REMARK 465     THR A   313                                                      
REMARK 465     ALA A   314                                                      
REMARK 465     THR A   315                                                      
REMARK 465     PRO A   316                                                      
REMARK 465     TYR A   317                                                      
REMARK 465     MET A   318                                                      
REMARK 465     ASN A   319                                                      
REMARK 465     GLY A   320                                                      
REMARK 465     GLU A   321                                                      
REMARK 465     THR A   322                                                      
REMARK 465     SER A   323                                                      
REMARK 465     THR A   324                                                      
REMARK 465     ALA A   415                                                      
REMARK 465     LYS A   416                                                      
REMARK 465     GLU A   417                                                      
REMARK 465     GLU A   418                                                      
REMARK 465     HIS A   419                                                      
REMARK 465     CYS A   420                                                      
REMARK 465     PRO A   421                                                      
REMARK 465     LEU A   422                                                      
REMARK 465     ALA A   423                                                      
REMARK 465     PHE A   506                                                      
REMARK 465     SER A   507                                                      
REMARK 465     TYR A   508                                                      
REMARK 465     SER A   509                                                      
REMARK 465     HIS A   510                                                      
REMARK 465     ALA A   511                                                      
REMARK 465     GLY A   512                                                      
REMARK 465     LEU A   513                                                      
REMARK 465     SER A   514                                                      
REMARK 465     ASN A   515                                                      
REMARK 465     ARG A   516                                                      
REMARK 465     LEU A   517                                                      
REMARK 465     ALA A   518                                                      
REMARK 465     ARG A   519                                                      
REMARK 465     ASP A   520                                                      
REMARK 465     ASN A   521                                                      
REMARK 465     GLU A   522                                                      
REMARK 465     LEU A   523                                                      
REMARK 465     ARG A   524                                                      
REMARK 465     GLU A   525                                                      
REMARK 465     ASN A   526                                                      
REMARK 465     ASP A   527                                                      
REMARK 465     LYS A   941                                                      
REMARK 465     LYS A   942                                                      
REMARK 465     LYS A   943                                                      
REMARK 465     LYS A   944                                                      
REMARK 465     PHE A   945                                                      
REMARK 465     GLY A   946                                                      
REMARK 465     TYR A   947                                                      
REMARK 465     LYS A   948                                                      
REMARK 465     ARG A   949                                                      
REMARK 465     GLU A   950                                                      
REMARK 465     TRP A  1051                                                      
REMARK 465     THR A  1052                                                      
REMARK 465     THR A  1053                                                      
REMARK 465     LYS A  1054                                                      
REMARK 465     MET A  1055                                                      
REMARK 465     ASP A  1056                                                      
REMARK 465     TRP A  1057                                                      
REMARK 465     ILE A  1058                                                      
REMARK 465     PHE A  1059                                                      
REMARK 465     HIS A  1060                                                      
REMARK 465     THR A  1061                                                      
REMARK 465     ILE A  1062                                                      
REMARK 465     LYS A  1063                                                      
REMARK 465     GLN A  1064                                                      
REMARK 465     HIS A  1065                                                      
REMARK 465     ALA A  1066                                                      
REMARK 465     LEU A  1067                                                      
REMARK 465     ASN A  1068                                                      
REMARK 465     MET B   322                                                      
REMARK 465     ASN B   323                                                      
REMARK 465     ASN B   324                                                      
REMARK 465     ASN B   325                                                      
REMARK 465     MET B   326                                                      
REMARK 465     SER B   327                                                      
REMARK 465     LEU B   328                                                      
REMARK 465     GLN B   329                                                      
REMARK 465     ASP B   330                                                      
REMARK 465     ALA B   331                                                      
REMARK 465     GLU B   332                                                      
REMARK 465     TRP B   333                                                      
REMARK 465     TYR B   334                                                      
REMARK 465     TRP B   335                                                      
REMARK 465     GLY B   336                                                      
REMARK 465     ASP B   337                                                      
REMARK 465     ILE B   338                                                      
REMARK 465     SER B   339                                                      
REMARK 465     ARG B   340                                                      
REMARK 465     GLU B   341                                                      
REMARK 465     GLU B   342                                                      
REMARK 465     VAL B   343                                                      
REMARK 465     ASN B   344                                                      
REMARK 465     GLU B   345                                                      
REMARK 465     LYS B   346                                                      
REMARK 465     LEU B   347                                                      
REMARK 465     ARG B   348                                                      
REMARK 465     ASP B   349                                                      
REMARK 465     THR B   350                                                      
REMARK 465     ALA B   351                                                      
REMARK 465     ASP B   352                                                      
REMARK 465     GLY B   353                                                      
REMARK 465     THR B   354                                                      
REMARK 465     PHE B   355                                                      
REMARK 465     LEU B   356                                                      
REMARK 465     VAL B   357                                                      
REMARK 465     ARG B   358                                                      
REMARK 465     ASP B   359                                                      
REMARK 465     ALA B   360                                                      
REMARK 465     SER B   361                                                      
REMARK 465     THR B   362                                                      
REMARK 465     LYS B   363                                                      
REMARK 465     MET B   364                                                      
REMARK 465     HIS B   365                                                      
REMARK 465     GLY B   366                                                      
REMARK 465     ASP B   367                                                      
REMARK 465     TYR B   368                                                      
REMARK 465     THR B   369                                                      
REMARK 465     LEU B   370                                                      
REMARK 465     THR B   371                                                      
REMARK 465     LEU B   372                                                      
REMARK 465     ARG B   373                                                      
REMARK 465     LYS B   374                                                      
REMARK 465     GLY B   375                                                      
REMARK 465     GLY B   376                                                      
REMARK 465     ASN B   377                                                      
REMARK 465     ASN B   378                                                      
REMARK 465     LYS B   379                                                      
REMARK 465     LEU B   380                                                      
REMARK 465     ILE B   381                                                      
REMARK 465     LYS B   382                                                      
REMARK 465     ILE B   383                                                      
REMARK 465     PHE B   384                                                      
REMARK 465     HIS B   385                                                      
REMARK 465     ARG B   386                                                      
REMARK 465     ASP B   387                                                      
REMARK 465     GLY B   388                                                      
REMARK 465     LYS B   389                                                      
REMARK 465     TYR B   390                                                      
REMARK 465     GLY B   391                                                      
REMARK 465     PHE B   392                                                      
REMARK 465     SER B   393                                                      
REMARK 465     ASP B   394                                                      
REMARK 465     PRO B   395                                                      
REMARK 465     LEU B   396                                                      
REMARK 465     THR B   397                                                      
REMARK 465     PHE B   398                                                      
REMARK 465     SER B   399                                                      
REMARK 465     SER B   400                                                      
REMARK 465     VAL B   401                                                      
REMARK 465     VAL B   402                                                      
REMARK 465     GLU B   403                                                      
REMARK 465     LEU B   404                                                      
REMARK 465     ILE B   405                                                      
REMARK 465     ASN B   406                                                      
REMARK 465     HIS B   407                                                      
REMARK 465     TYR B   408                                                      
REMARK 465     ARG B   409                                                      
REMARK 465     ASN B   410                                                      
REMARK 465     GLU B   411                                                      
REMARK 465     SER B   412                                                      
REMARK 465     LEU B   413                                                      
REMARK 465     ALA B   414                                                      
REMARK 465     GLN B   415                                                      
REMARK 465     TYR B   416                                                      
REMARK 465     ASN B   417                                                      
REMARK 465     PRO B   418                                                      
REMARK 465     LYS B   419                                                      
REMARK 465     LEU B   420                                                      
REMARK 465     ASP B   421                                                      
REMARK 465     VAL B   422                                                      
REMARK 465     LYS B   423                                                      
REMARK 465     LEU B   424                                                      
REMARK 465     LEU B   425                                                      
REMARK 465     TYR B   426                                                      
REMARK 465     PRO B   427                                                      
REMARK 465     VAL B   428                                                      
REMARK 465     SER B   429                                                      
REMARK 465     LYS B   430                                                      
REMARK 465     TYR B   431                                                      
REMARK 465     GLN B   432                                                      
REMARK 465     GLN B   433                                                      
REMARK 465     ASP B   434                                                      
REMARK 465     GLN B   435                                                      
REMARK 465     VAL B   436                                                      
REMARK 465     VAL B   437                                                      
REMARK 465     LYS B   438                                                      
REMARK 465     GLU B   439                                                      
REMARK 465     ASP B   440                                                      
REMARK 465     ASN B   441                                                      
REMARK 465     GLU B   510                                                      
REMARK 465     LYS B   511                                                      
REMARK 465     PHE B   512                                                      
REMARK 465     LYS B   513                                                      
REMARK 465     ARG B   514                                                      
REMARK 465     GLU B   515                                                      
REMARK 465     GLY B   516                                                      
REMARK 465     ASN B   517                                                      
REMARK 465     GLU B   518                                                      
REMARK 465     LYS B   519                                                      
REMARK 465     GLU B   520                                                      
REMARK 465     LEU B   584                                                      
REMARK 465     THR B   585                                                      
REMARK 465     GLN B   586                                                      
REMARK 465     LYS B   587                                                      
REMARK 465     GLY B   588                                                      
REMARK 465     VAL B   589                                                      
REMARK 465     ARG B   590                                                      
REMARK 465     GLN B   591                                                      
REMARK 465     LYS B   592                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    GLY A   106     N    ARG A   108              2.00            
REMARK 500   OG   SER A   773     CZ   ARG A   777              2.16            
REMARK 500   O    ALA A   163     O    VAL A   166              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PHE A 794   N   -  CA  -  C   ANGL. DEV. =  18.8 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    TYR A -25     -129.46    -98.51                                   
REMARK 500    LEU A  10      149.20   -173.69                                   
REMARK 500    PHE A  95      -65.21     71.12                                   
REMARK 500    PRO A 104       87.53    -49.83                                   
REMARK 500    ASN A 107       -7.26     15.80                                   
REMARK 500    GLU A 116      -81.54    -29.14                                   
REMARK 500    ILE A 117      -55.73     14.79                                   
REMARK 500    MET A 123      134.53    173.30                                   
REMARK 500    CYS A 126      -15.96   -176.73                                   
REMARK 500    ASP A 129       32.90    -61.18                                   
REMARK 500    MET A 130       -2.79   -165.38                                   
REMARK 500    ASP A 133      109.40    -24.79                                   
REMARK 500    LEU A 153       -0.40    -59.59                                   
REMARK 500    LEU A 156       98.12    -66.74                                   
REMARK 500    ASN A 157       22.05    106.17                                   
REMARK 500    SER A 158      -85.03     49.65                                   
REMARK 500    TYR A 165      -72.70    -68.57                                   
REMARK 500    ASP A 186       54.36    -44.87                                   
REMARK 500    ASN A 201        7.45    -67.27                                   
REMARK 500    ASN A 202      -20.07     52.55                                   
REMARK 500    CYS A 242      -50.66   -120.36                                   
REMARK 500    VAL A 243       59.90    -66.29                                   
REMARK 500    LEU A 244      -74.81   -179.03                                   
REMARK 500    GLU A 245       12.32    -62.98                                   
REMARK 500    TYR A 246       23.33   -161.69                                   
REMARK 500    CYS A 257     -159.78   -117.49                                   
REMARK 500    LYS A 264      108.39    -48.02                                   
REMARK 500    ILE A 277      -77.13    -58.07                                   
REMARK 500    MET A 299     -122.69    123.69                                   
REMARK 500    MET A 304       63.61   -170.47                                   
REMARK 500    SER A 326     -151.70   -106.55                                   
REMARK 500    VAL A 329       65.24    -69.73                                   
REMARK 500    ASN A 331       72.26   -108.63                                   
REMARK 500    LEU A 339      -81.94    -90.26                                   
REMARK 500    VAL A 344     -138.80   -143.56                                   
REMARK 500    ASN A 345      -28.61   -157.87                                   
REMARK 500    ILE A 348      134.30     52.43                                   
REMARK 500    ARG A 349      -59.81   -133.63                                   
REMARK 500    ASP A 350      -99.94   -149.77                                   
REMARK 500    ILE A 351       43.25    -78.73                                   
REMARK 500    GLU A 365       90.09     47.55                                   
REMARK 500    LEU A 367      142.78     69.02                                   
REMARK 500    THR A 373      124.79    -39.64                                   
REMARK 500    VAL A 376       97.89     43.98                                   
REMARK 500    CYS A 378      -76.65   -164.53                                   
REMARK 500    ASN A 380      105.10    -14.28                                   
REMARK 500    TRP A 383      -36.79   -134.05                                   
REMARK 500    ASN A 384       26.31     43.26                                   
REMARK 500    TYR A 392      170.75    -52.73                                   
REMARK 500    ALA A 399        7.27     97.17                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     142 RAMACHANDRAN OUTLIERS.                        
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 ASP A  -18     TYR A  -17                  141.17                    
REMARK 500 ARG A  115     GLU A  116                  147.65                    
REMARK 500 LEU A  185     ASP A  186                 -146.92                    
REMARK 500 ASP A  186     LYS A  187                  149.29                    
REMARK 500 LEU A  452     GLU A  453                  148.12                    
REMARK 500 ASN A  467     LYS A  468                  144.48                    
REMARK 500 SER A  773     SER A  774                 -143.87                    
REMARK 500 ALA A  775     LYS A  776                  143.19                    
REMARK 500 HIS A  936     PHE A  937                  147.79                    
REMARK 500 ILE B  524     MET B  525                 -142.80                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    LEU A  94        23.4      L          L   OUTSIDE RANGE           
REMARK 500    SER A 158        24.7      L          L   OUTSIDE RANGE           
REMARK 500    ASP A 186        24.6      L          L   OUTSIDE RANGE           
REMARK 500    TYR A 246        23.6      L          L   OUTSIDE RANGE           
REMARK 500    PHE A 794        17.5      L          L   OUTSIDE RANGE           
REMARK 500    GLN A 795        24.0      L          L   OUTSIDE RANGE           
REMARK 500    PHE A 937        24.1      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  2RD0 A    1  1068  UNP    P42336   PK3CA_HUMAN      1   1068             
DBREF  2RD0 B  322   600  UNP    P27986   P85A_HUMAN     322    600             
SEQADV 2RD0 MET A  -28  UNP  P42336              EXPRESSION TAG                 
SEQADV 2RD0 SER A  -27  UNP  P42336              EXPRESSION TAG                 
SEQADV 2RD0 TYR A  -26  UNP  P42336              EXPRESSION TAG                 
SEQADV 2RD0 TYR A  -25  UNP  P42336              EXPRESSION TAG                 
SEQADV 2RD0 HIS A  -24  UNP  P42336              EXPRESSION TAG                 
SEQADV 2RD0 HIS A  -23  UNP  P42336              EXPRESSION TAG                 
SEQADV 2RD0 HIS A  -22  UNP  P42336              EXPRESSION TAG                 
SEQADV 2RD0 HIS A  -21  UNP  P42336              EXPRESSION TAG                 
SEQADV 2RD0 HIS A  -20  UNP  P42336              EXPRESSION TAG                 
SEQADV 2RD0 HIS A  -19  UNP  P42336              EXPRESSION TAG                 
SEQADV 2RD0 ASP A  -18  UNP  P42336              EXPRESSION TAG                 
SEQADV 2RD0 TYR A  -17  UNP  P42336              EXPRESSION TAG                 
SEQADV 2RD0 ASP A  -16  UNP  P42336              EXPRESSION TAG                 
SEQADV 2RD0 ILE A  -15  UNP  P42336              EXPRESSION TAG                 
SEQADV 2RD0 PRO A  -13  UNP  P42336              EXPRESSION TAG                 
SEQADV 2RD0 THR A  -12  UNP  P42336              EXPRESSION TAG                 
SEQADV 2RD0 THR A  -11  UNP  P42336              EXPRESSION TAG                 
SEQADV 2RD0 GLU A  -10  UNP  P42336              EXPRESSION TAG                 
SEQADV 2RD0 ASN A   -9  UNP  P42336              EXPRESSION TAG                 
SEQADV 2RD0 LEU A   -8  UNP  P42336              EXPRESSION TAG                 
SEQADV 2RD0 TYR A   -7  UNP  P42336              EXPRESSION TAG                 
SEQADV 2RD0 PHE A   -6  UNP  P42336              EXPRESSION TAG                 
SEQADV 2RD0 GLN A   -5  UNP  P42336              EXPRESSION TAG                 
SEQADV 2RD0 GLY A   -4  UNP  P42336              EXPRESSION TAG                 
SEQADV 2RD0 ALA A   -3  UNP  P42336              EXPRESSION TAG                 
SEQADV 2RD0 MET A   -2  UNP  P42336              EXPRESSION TAG                 
SEQADV 2RD0 GLY A   -1  UNP  P42336              EXPRESSION TAG                 
SEQADV 2RD0 SER A    0  UNP  P42336              EXPRESSION TAG                 
SEQRES   1 A 1096  MET SER TYR TYR HIS HIS HIS HIS HIS HIS ASP TYR ASP          
SEQRES   2 A 1096  ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA MET          
SEQRES   3 A 1096  GLY SER MET PRO PRO ARG PRO SER SER GLY GLU LEU TRP          
SEQRES   4 A 1096  GLY ILE HIS LEU MET PRO PRO ARG ILE LEU VAL GLU CYS          
SEQRES   5 A 1096  LEU LEU PRO ASN GLY MET ILE VAL THR LEU GLU CYS LEU          
SEQRES   6 A 1096  ARG GLU ALA THR LEU ILE THR ILE LYS HIS GLU LEU PHE          
SEQRES   7 A 1096  LYS GLU ALA ARG LYS TYR PRO LEU HIS GLN LEU LEU GLN          
SEQRES   8 A 1096  ASP GLU SER SER TYR ILE PHE VAL SER VAL THR GLN GLU          
SEQRES   9 A 1096  ALA GLU ARG GLU GLU PHE PHE ASP GLU THR ARG ARG LEU          
SEQRES  10 A 1096  CYS ASP LEU ARG LEU PHE GLN PRO PHE LEU LYS VAL ILE          
SEQRES  11 A 1096  GLU PRO VAL GLY ASN ARG GLU GLU LYS ILE LEU ASN ARG          
SEQRES  12 A 1096  GLU ILE GLY PHE ALA ILE GLY MET PRO VAL CYS GLU PHE          
SEQRES  13 A 1096  ASP MET VAL LYS ASP PRO GLU VAL GLN ASP PHE ARG ARG          
SEQRES  14 A 1096  ASN ILE LEU ASN VAL CYS LYS GLU ALA VAL ASP LEU ARG          
SEQRES  15 A 1096  ASP LEU ASN SER PRO HIS SER ARG ALA MET TYR VAL TYR          
SEQRES  16 A 1096  PRO PRO ASN VAL GLU SER SER PRO GLU LEU PRO LYS HIS          
SEQRES  17 A 1096  ILE TYR ASN LYS LEU ASP LYS GLY GLN ILE ILE VAL VAL          
SEQRES  18 A 1096  ILE TRP VAL ILE VAL SER PRO ASN ASN ASP LYS GLN LYS          
SEQRES  19 A 1096  TYR THR LEU LYS ILE ASN HIS ASP CYS VAL PRO GLU GLN          
SEQRES  20 A 1096  VAL ILE ALA GLU ALA ILE ARG LYS LYS THR ARG SER MET          
SEQRES  21 A 1096  LEU LEU SER SER GLU GLN LEU LYS LEU CYS VAL LEU GLU          
SEQRES  22 A 1096  TYR GLN GLY LYS TYR ILE LEU LYS VAL CYS GLY CYS ASP          
SEQRES  23 A 1096  GLU TYR PHE LEU GLU LYS TYR PRO LEU SER GLN TYR LYS          
SEQRES  24 A 1096  TYR ILE ARG SER CYS ILE MET LEU GLY ARG MET PRO ASN          
SEQRES  25 A 1096  LEU MET LEU MET ALA LYS GLU SER LEU TYR SER GLN LEU          
SEQRES  26 A 1096  PRO MET ASP CYS PHE THR MET PRO SER TYR SER ARG ARG          
SEQRES  27 A 1096  ILE SER THR ALA THR PRO TYR MET ASN GLY GLU THR SER          
SEQRES  28 A 1096  THR LYS SER LEU TRP VAL ILE ASN SER ALA LEU ARG ILE          
SEQRES  29 A 1096  LYS ILE LEU CYS ALA THR TYR VAL ASN VAL ASN ILE ARG          
SEQRES  30 A 1096  ASP ILE ASP LYS ILE TYR VAL ARG THR GLY ILE TYR HIS          
SEQRES  31 A 1096  GLY GLY GLU PRO LEU CYS ASP ASN VAL ASN THR GLN ARG          
SEQRES  32 A 1096  VAL PRO CYS SER ASN PRO ARG TRP ASN GLU TRP LEU ASN          
SEQRES  33 A 1096  TYR ASP ILE TYR ILE PRO ASP LEU PRO ARG ALA ALA ARG          
SEQRES  34 A 1096  LEU CYS LEU SER ILE CYS SER VAL LYS GLY ARG LYS GLY          
SEQRES  35 A 1096  ALA LYS GLU GLU HIS CYS PRO LEU ALA TRP GLY ASN ILE          
SEQRES  36 A 1096  ASN LEU PHE ASP TYR THR ASP THR LEU VAL SER GLY LYS          
SEQRES  37 A 1096  MET ALA LEU ASN LEU TRP PRO VAL PRO HIS GLY LEU GLU          
SEQRES  38 A 1096  ASP LEU LEU ASN PRO ILE GLY VAL THR GLY SER ASN PRO          
SEQRES  39 A 1096  ASN LYS GLU THR PRO CYS LEU GLU LEU GLU PHE ASP TRP          
SEQRES  40 A 1096  PHE SER SER VAL VAL LYS PHE PRO ASP MET SER VAL ILE          
SEQRES  41 A 1096  GLU GLU HIS ALA ASN TRP SER VAL SER ARG GLU ALA GLY          
SEQRES  42 A 1096  PHE SER TYR SER HIS ALA GLY LEU SER ASN ARG LEU ALA          
SEQRES  43 A 1096  ARG ASP ASN GLU LEU ARG GLU ASN ASP LYS GLU GLN LEU          
SEQRES  44 A 1096  LYS ALA ILE SER THR ARG ASP PRO LEU SER GLU ILE THR          
SEQRES  45 A 1096  GLU GLN GLU LYS ASP PHE LEU TRP SER HIS ARG HIS TYR          
SEQRES  46 A 1096  CYS VAL THR ILE PRO GLU ILE LEU PRO LYS LEU LEU LEU          
SEQRES  47 A 1096  SER VAL LYS TRP ASN SER ARG ASP GLU VAL ALA GLN MET          
SEQRES  48 A 1096  TYR CYS LEU VAL LYS ASP TRP PRO PRO ILE LYS PRO GLU          
SEQRES  49 A 1096  GLN ALA MET GLU LEU LEU ASP CYS ASN TYR PRO ASP PRO          
SEQRES  50 A 1096  MET VAL ARG GLY PHE ALA VAL ARG CYS LEU GLU LYS TYR          
SEQRES  51 A 1096  LEU THR ASP ASP LYS LEU SER GLN TYR LEU ILE GLN LEU          
SEQRES  52 A 1096  VAL GLN VAL LEU LYS TYR GLU GLN TYR LEU ASP ASN LEU          
SEQRES  53 A 1096  LEU VAL ARG PHE LEU LEU LYS LYS ALA LEU THR ASN GLN          
SEQRES  54 A 1096  ARG ILE GLY HIS PHE PHE PHE TRP HIS LEU LYS SER GLU          
SEQRES  55 A 1096  MET HIS ASN LYS THR VAL SER GLN ARG PHE GLY LEU LEU          
SEQRES  56 A 1096  LEU GLU SER TYR CYS ARG ALA CYS GLY MET TYR LEU LYS          
SEQRES  57 A 1096  HIS LEU ASN ARG GLN VAL GLU ALA MET GLU LYS LEU ILE          
SEQRES  58 A 1096  ASN LEU THR ASP ILE LEU LYS GLN GLU LYS LYS ASP GLU          
SEQRES  59 A 1096  THR GLN LYS VAL GLN MET LYS PHE LEU VAL GLU GLN MET          
SEQRES  60 A 1096  ARG ARG PRO ASP PHE MET ASP ALA LEU GLN GLY PHE LEU          
SEQRES  61 A 1096  SER PRO LEU ASN PRO ALA HIS GLN LEU GLY ASN LEU ARG          
SEQRES  62 A 1096  LEU GLU GLU CYS ARG ILE MET SER SER ALA LYS ARG PRO          
SEQRES  63 A 1096  LEU TRP LEU ASN TRP GLU ASN PRO ASP ILE MET SER GLU          
SEQRES  64 A 1096  LEU LEU PHE GLN ASN ASN GLU ILE ILE PHE LYS ASN GLY          
SEQRES  65 A 1096  ASP ASP LEU ARG GLN ASP MET LEU THR LEU GLN ILE ILE          
SEQRES  66 A 1096  ARG ILE MET GLU ASN ILE TRP GLN ASN GLN GLY LEU ASP          
SEQRES  67 A 1096  LEU ARG MET LEU PRO TYR GLY CYS LEU SER ILE GLY ASP          
SEQRES  68 A 1096  CYS VAL GLY LEU ILE GLU VAL VAL ARG ASN SER HIS THR          
SEQRES  69 A 1096  ILE MET GLN ILE GLN CYS LYS GLY GLY LEU LYS GLY ALA          
SEQRES  70 A 1096  LEU GLN PHE ASN SER HIS THR LEU HIS GLN TRP LEU LYS          
SEQRES  71 A 1096  ASP LYS ASN LYS GLY GLU ILE TYR ASP ALA ALA ILE ASP          
SEQRES  72 A 1096  LEU PHE THR ARG SER CYS ALA GLY TYR CYS VAL ALA THR          
SEQRES  73 A 1096  PHE ILE LEU GLY ILE GLY ASP ARG HIS ASN SER ASN ILE          
SEQRES  74 A 1096  MET VAL LYS ASP ASP GLY GLN LEU PHE HIS ILE ASP PHE          
SEQRES  75 A 1096  GLY HIS PHE LEU ASP HIS LYS LYS LYS LYS PHE GLY TYR          
SEQRES  76 A 1096  LYS ARG GLU ARG VAL PRO PHE VAL LEU THR GLN ASP PHE          
SEQRES  77 A 1096  LEU ILE VAL ILE SER LYS GLY ALA GLN GLU CYS THR LYS          
SEQRES  78 A 1096  THR ARG GLU PHE GLU ARG PHE GLN GLU MET CYS TYR LYS          
SEQRES  79 A 1096  ALA TYR LEU ALA ILE ARG GLN HIS ALA ASN LEU PHE ILE          
SEQRES  80 A 1096  ASN LEU PHE SER MET MET LEU GLY SER GLY MET PRO GLU          
SEQRES  81 A 1096  LEU GLN SER PHE ASP ASP ILE ALA TYR ILE ARG LYS THR          
SEQRES  82 A 1096  LEU ALA LEU ASP LYS THR GLU GLN GLU ALA LEU GLU TYR          
SEQRES  83 A 1096  PHE MET LYS GLN MET ASN ASP ALA HIS HIS GLY GLY TRP          
SEQRES  84 A 1096  THR THR LYS MET ASP TRP ILE PHE HIS THR ILE LYS GLN          
SEQRES  85 A 1096  HIS ALA LEU ASN                                              
SEQRES   1 B  279  MET ASN ASN ASN MET SER LEU GLN ASP ALA GLU TRP TYR          
SEQRES   2 B  279  TRP GLY ASP ILE SER ARG GLU GLU VAL ASN GLU LYS LEU          
SEQRES   3 B  279  ARG ASP THR ALA ASP GLY THR PHE LEU VAL ARG ASP ALA          
SEQRES   4 B  279  SER THR LYS MET HIS GLY ASP TYR THR LEU THR LEU ARG          
SEQRES   5 B  279  LYS GLY GLY ASN ASN LYS LEU ILE LYS ILE PHE HIS ARG          
SEQRES   6 B  279  ASP GLY LYS TYR GLY PHE SER ASP PRO LEU THR PHE SER          
SEQRES   7 B  279  SER VAL VAL GLU LEU ILE ASN HIS TYR ARG ASN GLU SER          
SEQRES   8 B  279  LEU ALA GLN TYR ASN PRO LYS LEU ASP VAL LYS LEU LEU          
SEQRES   9 B  279  TYR PRO VAL SER LYS TYR GLN GLN ASP GLN VAL VAL LYS          
SEQRES  10 B  279  GLU ASP ASN ILE GLU ALA VAL GLY LYS LYS LEU HIS GLU          
SEQRES  11 B  279  TYR ASN THR GLN PHE GLN GLU LYS SER ARG GLU TYR ASP          
SEQRES  12 B  279  ARG LEU TYR GLU GLU TYR THR ARG THR SER GLN GLU ILE          
SEQRES  13 B  279  GLN MET LYS ARG THR ALA ILE GLU ALA PHE ASN GLU THR          
SEQRES  14 B  279  ILE LYS ILE PHE GLU GLU GLN CYS GLN THR GLN GLU ARG          
SEQRES  15 B  279  TYR SER LYS GLU TYR ILE GLU LYS PHE LYS ARG GLU GLY          
SEQRES  16 B  279  ASN GLU LYS GLU ILE GLN ARG ILE MET HIS ASN TYR ASP          
SEQRES  17 B  279  LYS LEU LYS SER ARG ILE SER GLU ILE ILE ASP SER ARG          
SEQRES  18 B  279  ARG ARG LEU GLU GLU ASP LEU LYS LYS GLN ALA ALA GLU          
SEQRES  19 B  279  TYR ARG GLU ILE ASP LYS ARG MET ASN SER ILE LYS PRO          
SEQRES  20 B  279  ASP LEU ILE GLN LEU ARG LYS THR ARG ASP GLN TYR LEU          
SEQRES  21 B  279  MET TRP LEU THR GLN LYS GLY VAL ARG GLN LYS LYS LEU          
SEQRES  22 B  279  ASN GLU TRP LEU GLY ASN                                      
HELIX    1   1 THR A   41  ALA A   53  1                                  13    
HELIX    2   2 ARG A   54  TYR A   56  5                                   3    
HELIX    3   3 LEU A   58  LEU A   62  5                                   5    
HELIX    4   4 ASP A   64  TYR A   68  5                                   5    
HELIX    5   5 ARG A   88  LEU A   92  5                                   5    
HELIX    6   6 ARG A  108  ASN A  114  1                                   7    
HELIX    7   7 ILE A  117  GLY A  122  1                                   6    
HELIX    8   8 ASP A  133  ILE A  143  1                                  11    
HELIX    9   9 ILE A  143  LEU A  156  1                                  14    
HELIX   10  10 PRO A  159  VAL A  166  1                                   8    
HELIX   11  11 ILE A  181  ASP A  186  1                                   6    
HELIX   12  12 VAL A  216  ARG A  230  1                                  15    
HELIX   13  13 SER A  235  LEU A  241  1                                   7    
HELIX   14  14 TYR A  246  GLY A  248  5                                   3    
HELIX   15  15 PRO A  266  GLN A  269  5                                   4    
HELIX   16  16 TYR A  270  GLY A  280  1                                  11    
HELIX   17  17 LYS A  290  SER A  295  1                                   6    
HELIX   18  18 PRO A  487  GLU A  493  1                                   7    
HELIX   19  19 GLU A  494  SER A  499  1                                   6    
HELIX   20  20 ASP A  538  GLU A  542  5                                   5    
HELIX   21  21 THR A  544  HIS A  554  1                                  11    
HELIX   22  22 ARG A  555  VAL A  559  5                                   5    
HELIX   23  23 ILE A  561  GLU A  563  5                                   3    
HELIX   24  24 ILE A  564  SER A  571  1                                   8    
HELIX   25  25 SER A  576  ASP A  589  1                                  14    
HELIX   26  26 GLU A  596  ASP A  603  5                                   8    
HELIX   27  27 ASP A  608  LEU A  623  1                                  16    
HELIX   28  28 THR A  624  TYR A  631  1                                   8    
HELIX   29  29 TYR A  631  LEU A  639  1                                   9    
HELIX   30  30 LYS A  640  GLU A  642  5                                   3    
HELIX   31  31 ASN A  647  LEU A  658  1                                  12    
HELIX   32  32 ASN A  660  SER A  673  1                                  14    
HELIX   33  33 ASN A  677  CYS A  695  1                                  19    
HELIX   34  34 MET A  697  GLN A  721  1                                  25    
HELIX   35  35 THR A  727  MET A  739  1                                  13    
HELIX   36  36 ARG A  741  LEU A  748  1                                   8    
HELIX   37  37 LEU A  807  GLN A  827  1                                  21    
HELIX   38  38 ILE A  857  LYS A  863  1                                   7    
HELIX   39  39 LEU A  870  SER A  874  5                                   5    
HELIX   40  40 HIS A  878  ASP A  883  1                                   6    
HELIX   41  41 GLU A  888  GLY A  912  1                                  25    
HELIX   42  42 THR A  957  ILE A  964  1                                   8    
HELIX   43  43 THR A  974  HIS A  994  1                                  21    
HELIX   44  44 HIS A  994  MET A 1004  1                                  11    
HELIX   45  45 ILE A 1019  LEU A 1026  1                                   8    
HELIX   46  46 THR A 1031  HIS A 1048  1                                  18    
HELIX   47  47 LYS B  447  GLN B  499  1                                  53    
HELIX   48  48 MET B  525  LEU B  573  1                                  49    
HELIX   49  49 ARG B  574  TYR B  580  1                                   7    
SHEET    1   A 5 ILE A  31  LEU A  37  0                                        
SHEET    2   A 5 ARG A  19  LEU A  25 -1  N  VAL A  22   O  LEU A  34           
SHEET    3   A 5 PHE A  98  ILE A 102  1  O  VAL A 101   N  LEU A  25           
SHEET    4   A 5 ILE A  69  THR A  74 -1  N  ILE A  69   O  ILE A 102           
SHEET    5   A 5 GLU A  78  PHE A  82 -1  O  PHE A  82   N  PHE A  70           
SHEET    1   B 5 ASP A 203  ASN A 212  0                                        
SHEET    2   B 5 GLN A 189  VAL A 198 -1  N  VAL A 198   O  ASP A 203           
SHEET    3   B 5 ASN A 284  ALA A 289  1  O  LEU A 285   N  TRP A 195           
SHEET    4   B 5 TYR A 250  VAL A 254 -1  N  ILE A 251   O  MET A 288           
SHEET    5   B 5 TYR A 260  PHE A 261 -1  O  PHE A 261   N  LEU A 252           
SHEET    1   C 4 ARG A 382  TYR A 392  0                                        
SHEET    2   C 4 ALA A 333  ALA A 341 -1  N  LEU A 334   O  TYR A 389           
SHEET    3   C 4 CYS A 472  PHE A 477 -1  O  GLU A 476   N  LYS A 337           
SHEET    4   C 4 GLY A 439  ASN A 444 -1  N  LEU A 443   O  LEU A 473           
SHEET    1   D 4 ASN A 370  VAL A 371  0                                        
SHEET    2   D 4 ARG A 357  TYR A 361 -1  N  THR A 358   O  ASN A 370           
SHEET    3   D 4 ARG A 401  SER A 405 -1  O  ARG A 401   N  TYR A 361           
SHEET    4   D 4 GLY A 425  ASN A 428 -1  O  GLY A 425   N  LEU A 404           
SHEET    1   E 2 PHE A 751  SER A 753  0                                        
SHEET    2   E 2 ASN A 756  LEU A 761 -1  O  LEU A 761   N  PHE A 751           
SHEET    1   F 5 ARG A 770  ILE A 771  0                                        
SHEET    2   F 5 LEU A 779  TRP A 783 -1  O  TRP A 780   N  ARG A 770           
SHEET    3   F 5 ASN A 797  ASN A 803 -1  O  ASN A 797   N  TRP A 783           
SHEET    4   F 5 VAL A 845  GLU A 849 -1  O  ILE A 848   N  ILE A 800           
SHEET    5   F 5 CYS A 838  GLY A 842 -1  N  LEU A 839   O  LEU A 847           
SHEET    1   G 3 SER A 854  THR A 856  0                                        
SHEET    2   G 3 ILE A 921  LYS A 924 -1  O  VAL A 923   N  HIS A 855           
SHEET    3   G 3 LEU A 929  HIS A 931 -1  O  PHE A 930   N  MET A 922           
CISPEP   1 SER A  199    PRO A  200          0        -0.25                     
CRYST1  115.058  117.050  151.584  90.00  90.00  90.00 P 21 21 21    4          
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      0.008691  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008543  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006597        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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