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Database: PDB
Entry: 1D5R
LinkDB: 1D5R
Original site: 1D5R 
HEADER    HYDROLASE                               11-OCT-99   1D5R              
TITLE     CRYSTAL STRUCTURE OF THE PTEN TUMOR SUPPRESSOR                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOSPHOINOSITIDE PHOSPHATASE PTEN;                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 7-353;                                            
COMPND   5 EC: 3.1.3.48;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: 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: TRICHOPLUSIA NI;                                  
SOURCE   6 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: BACULOVIRUS;                               
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PVL1393                                   
KEYWDS    C2 DOMAIN, PHOSPHOTIDYLINOSITOL, PHOSPHATASE, HYDROLASE               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.O.LEE,H.YANG,M.-M.GEORGESCU,A.DI CRISTOFANO,N.P.PAVLETICH           
REVDAT   5   16-AUG-17 1D5R    1       SOURCE REMARK                            
REVDAT   4   24-FEB-16 1D5R    1       COMPND KEYWDS VERSN                      
REVDAT   3   24-FEB-09 1D5R    1       VERSN                                    
REVDAT   2   01-APR-03 1D5R    1       JRNL                                     
REVDAT   1   04-NOV-99 1D5R    0                                                
JRNL        AUTH   J.O.LEE,H.YANG,M.M.GEORGESCU,A.DI CRISTOFANO,T.MAEHAMA,      
JRNL        AUTH 2 Y.SHI,J.E.DIXON,P.PANDOLFI,N.P.PAVLETICH                     
JRNL        TITL   CRYSTAL STRUCTURE OF THE PTEN TUMOR SUPPRESSOR: IMPLICATIONS 
JRNL        TITL 2 FOR ITS PHOSPHOINOSITIDE PHOSPHATASE ACTIVITY AND MEMBRANE   
JRNL        TITL 3 ASSOCIATION.                                                 
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V.  99   323 1999              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   10555148                                                     
JRNL        DOI    10.1016/S0092-8674(00)81663-3                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 20302                          
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 SET) : 0.224                           
REMARK   3   FREE R VALUE                     : 0.276                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 960                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
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   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2576                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 10                                      
REMARK   3   SOLVENT ATOMS            : 382                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 25.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.660                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1D5R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-OCT-99.                  
REMARK 100 THE DEPOSITION ID IS D_1000009817.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-DEC-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 130.0                              
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : F2                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
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   : 20302                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 15.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.8                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.03700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 42.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.17                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 76.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.16300                            
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: NULL                         
REMARK 200 SOFTWARE USED: MLPHARE                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.43                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NA/K TARTRATE, 5% GLYCEROL, 100MM TRIS   
REMARK 280  -CL, 10MM DTT, PH 8.0, VAPOR DIFFUSION, HANGING DROP,               
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y,X,Z                                                  
REMARK 290       4555   Y,-X,Z                                                  
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290       8555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       56.57000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       56.57000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       29.27500            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       56.57000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       56.57000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       29.27500            
REMARK 290   SMTRY1   7  0.000000 -1.000000  0.000000       56.57000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       56.57000            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       29.27500            
REMARK 290   SMTRY1   8  0.000000  1.000000  0.000000       56.57000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000       56.57000            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       29.27500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     7                                                      
REMARK 465     ILE A     8                                                      
REMARK 465     VAL A     9                                                      
REMARK 465     SER A    10                                                      
REMARK 465     ARG A    11                                                      
REMARK 465     ASN A    12                                                      
REMARK 465     LYS A    13                                                      
REMARK 465     GLY A   282                                                      
REMARK 465     PRO A   283                                                      
REMARK 465     GLU A   284                                                      
REMARK 465     GLU A   285                                                      
REMARK 465     VAL A   309                                                      
REMARK 465     ASP A   310                                                      
REMARK 465     ASN A   311                                                      
REMARK 465     ASP A   312                                                      
REMARK 465     GLU A   352                                                      
REMARK 465     GLU A   353                                                      
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    HOH A  1503     O    HOH A  1690              2.15            
REMARK 500   O    HOH A  1433     O    HOH A  1633              2.15            
REMARK 500   O    ASP A    24     O    HOH A  1706              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    GLY A  20   N   -  CA  -  C   ANGL. DEV. = -15.1 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  16      -21.68    171.13                                   
REMARK 500    GLN A  17      137.04   -175.89                                   
REMARK 500    PHE A  21     -105.38   -117.07                                   
REMARK 500    ASP A  22       61.30    173.58                                   
REMARK 500    LEU A  42      154.21    -42.42                                   
REMARK 500    GLU A  43      152.98    174.12                                   
REMARK 500    ARG A  47      -45.04   -134.51                                   
REMARK 500    LYS A  62      -90.35    -40.31                                   
REMARK 500    GLU A  73     -116.07    -63.00                                   
REMARK 500    THR A  78       30.40    -58.52                                   
REMARK 500    SER A 113       36.82    -80.95                                   
REMARK 500    ASP A 116      -47.85   -141.69                                   
REMARK 500    ASN A 117     -154.78   -153.28                                   
REMARK 500    HIS A 118       16.81   -146.88                                   
REMARK 500    CYS A 124     -126.31   -129.29                                   
REMARK 500    LYS A 128     -102.44   -121.10                                   
REMARK 500    THR A 210     -167.71   -128.54                                   
REMARK 500    LEU A 220     -135.42     61.37                                   
REMARK 500    ASP A 236      106.83     29.63                                   
REMARK 500    LYS A 237      -23.01     77.38                                   
REMARK 500    MET A 270      -64.17    -92.91                                   
REMARK 500    GLU A 314      -44.84   -142.54                                   
REMARK 500    ASN A 334       49.48     36.04                                   
REMARK 500    ASN A 340      -18.07     82.76                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TLA A 1352                
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 RESIDUES 286-309 ARE REPLACED BY VAL                                 
DBREF  1D5R A    7   285  UNP    P60484   PTEN_HUMAN       7    285             
DBREF  1D5R A  310   353  UNP    P60484   PTEN_HUMAN     310    353             
SEQADV 1D5R MET A    7  UNP  P60484    GLU     7 CONFLICT                       
SEQADV 1D5R VAL A  309  UNP  P60484          309 SEE REMARK 999                 
SEQRES   1 A  324  MET ILE VAL SER ARG ASN LYS ARG ARG TYR GLN GLU ASP          
SEQRES   2 A  324  GLY PHE ASP LEU ASP LEU THR TYR ILE TYR PRO ASN ILE          
SEQRES   3 A  324  ILE ALA MET GLY PHE PRO ALA GLU ARG LEU GLU GLY VAL          
SEQRES   4 A  324  TYR ARG ASN ASN ILE ASP ASP VAL VAL ARG PHE LEU ASP          
SEQRES   5 A  324  SER LYS HIS LYS ASN HIS TYR LYS ILE TYR ASN LEU CYS          
SEQRES   6 A  324  ALA GLU ARG HIS TYR ASP THR ALA LYS PHE ASN CYS ARG          
SEQRES   7 A  324  VAL ALA GLN TYR PRO PHE GLU ASP HIS ASN PRO PRO GLN          
SEQRES   8 A  324  LEU GLU LEU ILE LYS PRO PHE CYS GLU ASP LEU ASP GLN          
SEQRES   9 A  324  TRP LEU SER GLU ASP ASP ASN HIS VAL ALA ALA ILE HIS          
SEQRES  10 A  324  CYS LYS ALA GLY LYS GLY ARG THR GLY VAL MET ILE CYS          
SEQRES  11 A  324  ALA TYR LEU LEU HIS ARG GLY LYS PHE LEU LYS ALA GLN          
SEQRES  12 A  324  GLU ALA LEU ASP PHE TYR GLY GLU VAL ARG THR ARG ASP          
SEQRES  13 A  324  LYS LYS GLY VAL THR ILE PRO SER GLN ARG ARG TYR VAL          
SEQRES  14 A  324  TYR TYR TYR SER TYR LEU LEU LYS ASN HIS LEU ASP TYR          
SEQRES  15 A  324  ARG PRO VAL ALA LEU LEU PHE HIS LYS MET MET PHE GLU          
SEQRES  16 A  324  THR ILE PRO MET PHE SER GLY GLY THR CYS ASN PRO GLN          
SEQRES  17 A  324  PHE VAL VAL CYS GLN LEU LYS VAL LYS ILE TYR SER SER          
SEQRES  18 A  324  ASN SER GLY PRO THR ARG ARG GLU ASP LYS PHE MET TYR          
SEQRES  19 A  324  PHE GLU PHE PRO GLN PRO LEU PRO VAL CYS GLY ASP ILE          
SEQRES  20 A  324  LYS VAL GLU PHE PHE HIS LYS GLN ASN LYS MET LEU LYS          
SEQRES  21 A  324  LYS ASP LYS MET PHE HIS PHE TRP VAL ASN THR PHE PHE          
SEQRES  22 A  324  ILE PRO GLY PRO GLU GLU VAL ASP ASN ASP LYS GLU TYR          
SEQRES  23 A  324  LEU VAL LEU THR LEU THR LYS ASN ASP LEU ASP LYS ALA          
SEQRES  24 A  324  ASN LYS ASP LYS ALA ASN ARG TYR PHE SER PRO ASN PHE          
SEQRES  25 A  324  LYS VAL LYS LEU TYR PHE THR LYS THR VAL GLU GLU              
HET    TLA  A1352      10                                                       
HETNAM     TLA L(+)-TARTARIC ACID                                               
FORMUL   2  TLA    C4 H6 O6                                                     
FORMUL   3  HOH   *382(H2 O)                                                    
HELIX    1   1 ASN A   49  HIS A   61  1                                  13    
HELIX    2   2 GLN A   97  GLU A   99  5                                   3    
HELIX    3   3 LEU A  100  SER A  113  1                                  14    
HELIX    4   4 LYS A  128  ARG A  142  1                                  15    
HELIX    5   5 LYS A  147  THR A  160  1                                  14    
HELIX    6   6 ILE A  168  HIS A  185  1                                  18    
HELIX    7   7 PHE A  278  ILE A  280  5                                   3    
HELIX    8   8 ASN A  323  LEU A  325  5                                   3    
HELIX    9   9 LYS A  327  ASP A  331  5                                   5    
SHEET    1   A 5 LEU A  25  TYR A  29  0                                        
SHEET    2   A 5 ILE A  32  MET A  35 -1  O  ILE A  32   N  ILE A  28           
SHEET    3   A 5 VAL A 119  HIS A 123  1  O  ALA A 120   N  ILE A  33           
SHEET    4   A 5 TYR A  65  CYS A  71  1  O  LYS A  66   N  ALA A 121           
SHEET    5   A 5 VAL A  85  PHE A  90  1  O  ALA A  86   N  ASN A  69           
SHEET    1   B 5 ARG A 233  GLU A 235  0                                        
SHEET    2   B 5 PHE A 238  CYS A 250 -1  O  PHE A 238   N  GLU A 235           
SHEET    3   B 5 ALA A 192  PHE A 200 -1  O  LEU A 193   N  VAL A 249           
SHEET    4   B 5 LYS A 342  LYS A 349 -1  N  LYS A 344   O  MET A 199           
SHEET    5   B 5 LEU A 316  THR A 321 -1  O  LEU A 316   N  PHE A 347           
SHEET    1   C 4 VAL A 222  SER A 226  0                                        
SHEET    2   C 4 PRO A 213  GLN A 219 -1  N  VAL A 217   O  TYR A 225           
SHEET    3   C 4 ASP A 252  HIS A 259 -1  N  LYS A 254   O  CYS A 218           
SHEET    4   C 4 ASP A 268  ASN A 276 -1  O  ASP A 268   N  HIS A 259           
SITE     1 AC1 10 ASP A  92  HIS A  93  CYS A 124  LYS A 125                    
SITE     2 AC1 10 ALA A 126  GLY A 129  ARG A 130  GLN A 171                    
SITE     3 AC1 10 HOH A1381  HOH A1439                                          
CRYST1  113.140  113.140   58.550  90.00  90.00  90.00 I 4           8          
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      0.008839  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008839  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017079        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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